HEADER MEMBRANE PROTEIN 17-JUN-22 8A6C TITLE 1 PICOSECOND LIGHT ACTIVATED CRYSTAL STRUCTURE OF BOVINE RHODOPSIN IN TITLE 2 LIPIDIC CUBIC PHASE COMPND MOL_ID: 1; COMPND 2 MOLECULE: RHODOPSIN; COMPND 3 CHAIN: A, B SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: CATTLE; SOURCE 4 ORGANISM_TAXID: 9913 KEYWDS GPCR, OPSIN, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR T.GRUHL,T.WEINERT,M.J.RODRIGUES,C.J.MILNE,G.ORTOLANI,K.NASS,E.NANGO, AUTHOR 2 S.SEN,P.J.M.JOHNSON,C.CIRELLI,A.FURRER,S.MOUS,P.SKOPINTSEV,D.JAMES, AUTHOR 3 F.DWORKOWSKI,P.BAATH,D.KEKILLI,D.OSEROV,R.TANAKA,H.GLOVER, AUTHOR 4 C.BACELLAR,S.BRUENLE,C.M.CASADEI,A.D.DIETHELM,D.GASHI,G.GOTTHARD, AUTHOR 5 R.GUIXA-GONZALEZ,Y.JOTI,V.KABANOVA,G.KNOPP,E.LESCA,P.MA,I.MARTIEL, AUTHOR 6 J.MUEHLE,S.OWADA,F.PAMULA,D.SARABI,O.TEJERO,C.J.TSAI,N.VARMA,A.WACH, AUTHOR 7 S.BOUTET,K.TONO,P.NOGLY,X.DEUPI,S.IWATA,R.NEUTZE,J.STANDFUSS, AUTHOR 8 G.F.X.SCHERTLER,V.PANNEELS REVDAT 3 12-APR-23 8A6C 1 JRNL REVDAT 2 05-APR-23 8A6C 1 JRNL REVDAT 1 29-MAR-23 8A6C 0 JRNL AUTH T.GRUHL,T.WEINERT,M.J.RODRIGUES,C.J.MILNE,G.ORTOLANI,K.NASS, JRNL AUTH 2 E.NANGO,S.SEN,P.J.M.JOHNSON,C.CIRELLI,A.FURRER,S.MOUS, JRNL AUTH 3 P.SKOPINTSEV,D.JAMES,F.DWORKOWSKI,P.BATH,D.KEKILLI,D.OZEROV, JRNL AUTH 4 R.TANAKA,H.GLOVER,C.BACELLAR,S.BRUNLE,C.M.CASADEI, JRNL AUTH 5 A.D.DIETHELM,D.GASHI,G.GOTTHARD,R.GUIXA-GONZALEZ,Y.JOTI, JRNL AUTH 6 V.KABANOVA,G.KNOPP,E.LESCA,P.MA,I.MARTIEL,J.MUHLE,S.OWADA, JRNL AUTH 7 F.PAMULA,D.SARABI,O.TEJERO,C.J.TSAI,N.VARMA,A.WACH,S.BOUTET, JRNL AUTH 8 K.TONO,P.NOGLY,X.DEUPI,S.IWATA,R.NEUTZE,J.STANDFUSS, JRNL AUTH 9 G.SCHERTLER,V.PANNEELS JRNL TITL ULTRAFAST STRUCTURAL CHANGES DIRECT THE FIRST MOLECULAR JRNL TITL 2 EVENTS OF VISION. JRNL REF NATURE V. 615 939 2023 JRNL REFN ESSN 1476-4687 JRNL PMID 36949205 JRNL DOI 10.1038/S41586-023-05863-6 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.GRUHL,T.WEINERT,M.RODRIGUES,C.J.MILNE,G.ORTOLANI,K.NASS, REMARK 1 AUTH 2 E.NANGO,S.SEN,P.J.M.JOHNSON,C.CIRELLI,A.FURRER,S.MOUS, REMARK 1 AUTH 3 P.SKOPINTSEV,D.JAMES,F.DWORKOWSKI,P.BATH,D.KEKILLI,D.OZEROV, REMARK 1 AUTH 4 R.TANAKA,H.GLOVER,C.BACELLAR,S.BRUNLE,C.M.CASADEI, REMARK 1 AUTH 5 A.D.DIETHELM,D.GASHI,G.GOTTHARD,R.GUIXA-GONZALEZ,Y.JOTI, REMARK 1 AUTH 6 V.KABANOVA,G.KNOPP,E.LESCA,P.MA,I.MARTIEL,J.MUHLE,S.OWADA, REMARK 1 AUTH 7 F.PAMULA,D.SARABI,O.TEJERO,C.J.TSAI,N.VARMA,A.WACH,S.BOUTET, REMARK 1 AUTH 8 K.TONO,P.NOGLY,X.DEUPI,S.IWATA,R.NEUTZE,J.STANDFUSS, REMARK 1 AUTH 9 G.F.SCHERTLER,V.PANNEELS REMARK 1 TITL ULTRAFAST STRUCTURAL CHANGES DIRECT THE FIRST MOLECULAR REMARK 1 TITL 2 EVENTS OF VISION REMARK 1 REF BIORXIV 2022 REMARK 1 REFN ISSN 2692-8205 REMARK 1 DOI 10.1101/2022.10.14.511948 REMARK 2 REMARK 2 RESOLUTION. 1.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20_4459 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 9.99 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 82.3 REMARK 3 NUMBER OF REFLECTIONS : 64866 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.351 REMARK 3 R VALUE (WORKING SET) : 0.350 REMARK 3 FREE R VALUE : 0.398 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.440 REMARK 3 FREE R VALUE TEST SET COUNT : 935 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 9.9900 - 3.4000 0.90 10368 153 0.3139 0.3528 REMARK 3 2 3.4000 - 2.7200 0.86 9622 138 0.3115 0.3946 REMARK 3 3 2.7200 - 2.3800 0.86 9578 142 0.3236 0.3703 REMARK 3 4 2.3800 - 2.1700 0.85 9379 140 0.3660 0.3779 REMARK 3 5 2.1700 - 2.0100 0.79 8671 123 0.4184 0.4592 REMARK 3 6 2.0100 - 1.8900 0.75 8229 119 0.5042 0.5762 REMARK 3 7 1.8900 - 1.8000 0.74 8084 120 0.5856 0.6041 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.359 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 49.269 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 23.68 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.93 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 : 0.004 5479 REMARK 3 ANGLE : 0.678 7433 REMARK 3 CHIRALITY : 0.043 830 REMARK 3 PLANARITY : 0.006 908 REMARK 3 DIHEDRAL : 12.534 1997 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): -5.4925 28.4465 37.7141 REMARK 3 T TENSOR REMARK 3 T11: 0.2035 T22: 0.1898 REMARK 3 T33: 0.1976 T12: -0.0071 REMARK 3 T13: 0.0116 T23: 0.0009 REMARK 3 L TENSOR REMARK 3 L11: 0.4529 L22: 0.2713 REMARK 3 L33: 0.1734 L12: -0.1851 REMARK 3 L13: -0.1528 L23: 0.0353 REMARK 3 S TENSOR REMARK 3 S11: -0.0182 S12: -0.0020 S13: 0.0042 REMARK 3 S21: 0.0159 S22: -0.0108 S23: -0.0198 REMARK 3 S31: 0.0201 S32: -0.0399 S33: -0.0001 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 8A6C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JUN-22. REMARK 100 THE DEPOSITION ID IS D_1292121930. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 03-DEC-18 REMARK 200 TEMPERATURE (KELVIN) : 294 REMARK 200 PH : 9.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER REMARK 200 BEAMLINE : 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 : 79304 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 : 296.3 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7600 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 : 185.2 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.790 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 1U19 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 54.15 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 36% PEG 600, 100 MM BICINE PH 9.0, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 294K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 X,-Y,-Z REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 -X,-Y+1/2,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.50500 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: 6090 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 26860 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 9.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -45.50500 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 75.55500 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 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 MET B 1 CG SD CE REMARK 470 LYS B 66 CG 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 1.96 REMARK 500 SG CYS B 322 O2 PLM B 408 1.98 REMARK 500 OH TYR B 74 OE2 GLU B 150 2.11 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 GLN A 28 35.78 -94.33 REMARK 500 SER A 176 -164.11 60.17 REMARK 500 HIS A 195 67.02 38.64 REMARK 500 PHE A 212 -51.89 -123.92 REMARK 500 PHE A 212 -55.15 -123.92 REMARK 500 GLN B 28 37.37 -96.67 REMARK 500 SER B 176 -164.54 56.55 REMARK 500 PHE B 212 -56.47 -130.01 REMARK 500 PHE B 228 50.39 -94.46 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 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 B 404 REMARK 610 OLC B 405 REMARK 610 OLC B 406 REMARK 610 OLC B 407 REMARK 610 PLM B 408 REMARK 610 OLC B 409 DBREF 8A6C A 1 348 UNP P02699 OPSD_BOVIN 1 348 DBREF 8A6C 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 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 10 HET OLC B 406 18 HET OLC B 407 17 HET PLM B 408 7 HET OLC B 409 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 *171(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 PHE A 212 1 14 HELIX 9 AA9 PHE A 212 PHE A 228 1 17 HELIX 10 AB1 LYS A 245 HIS A 278 1 34 HELIX 11 AB2 PRO A 285 LYS A 296 1 12 HELIX 12 AB3 THR A 297 ALA A 299 5 3 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 THR B 277 1 33 HELIX 25 AC7 PRO B 285 LYS B 296 1 12 HELIX 26 AC8 THR B 297 ALA B 299 5 3 HELIX 27 AC9 VAL B 300 ASN B 310 1 11 HELIX 28 AD1 ASN B 310 CYS B 322 1 13 SHEET 1 AA1 2 THR A 4 GLU A 5 0 SHEET 2 AA1 2 TYR A 10 VAL A 11 -1 O VAL A 11 N THR A 4 SHEET 1 AA2 2 TYR A 178 GLU A 181 0 SHEET 2 AA2 2 SER A 186 ILE A 189 -1 O GLY A 188 N ILE A 179 SHEET 1 AA3 2 THR B 4 GLU B 5 0 SHEET 2 AA3 2 TYR B 10 VAL B 11 -1 O VAL B 11 N THR B 4 SHEET 1 AA4 2 TYR B 178 GLU B 181 0 SHEET 2 AA4 2 SER B 186 ILE B 189 -1 O SER B 186 N GLU B 181 SSBOND 1 CYS A 110 CYS A 187 1555 1555 2.02 SSBOND 2 CYS B 110 CYS B 187 1555 1555 2.03 LINK N MET A 1 C ACE A 401 1555 1555 1.33 LINK ND2 ASN A 2 C1 NAG A 403 1555 1555 1.45 LINK ND2 ASN A 15 C1 NAG C 1 1555 1555 1.45 LINK NZ LYS A 296 C15 RET A 402 1555 1555 1.34 LINK SG CYS A 322 C1 PLM A 410 1555 1555 1.77 LINK N MET B 1 C ACE B 401 1555 1555 1.33 LINK ND2 ASN B 2 C1 NAG B 403 1555 1555 1.45 LINK ND2 ASN B 15 C1 NAG D 1 1555 1555 1.45 LINK NZ LYS B 296 C15 RET B 402 1555 1555 1.34 LINK SG CYS B 322 C1 PLM B 408 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 1.45 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 16.256 34.613 4.931 1.00 49.18 N ANISOU 1 N MET A 1 6279 6160 6247 559 853 750 N ATOM 2 CA MET A 1 15.969 33.591 5.934 1.00 43.13 C ANISOU 2 CA MET A 1 5516 5389 5482 514 804 689 C ATOM 3 C MET A 1 16.724 32.289 5.671 1.00 42.78 C ANISOU 3 C MET A 1 5480 5349 5426 508 807 664 C ATOM 4 O MET A 1 16.725 31.764 4.556 1.00 42.42 O ANISOU 4 O MET A 1 5450 5342 5324 541 825 667 O ATOM 5 CB MET A 1 14.465 33.316 5.994 1.00 44.32 C ANISOU 5 CB MET A 1 5681 5587 5571 512 762 652 C ATOM 6 N ASN A 2 17.364 31.771 6.714 1.00 41.19 N ANISOU 6 N ASN A 2 5268 5107 5277 466 789 640 N ATOM 7 CA ASN A 2 18.142 30.545 6.628 1.00 35.67 C ANISOU 7 CA ASN A 2 4573 4402 4576 457 792 617 C ATOM 8 C ASN A 2 17.361 29.311 7.070 1.00 33.57 C ANISOU 8 C ASN A 2 4323 4160 4271 432 748 556 C ATOM 9 O ASN A 2 17.922 28.209 7.085 1.00 31.67 O ANISOU 9 O ASN A 2 4088 3915 4031 422 747 533 O ATOM 10 CB ASN A 2 19.420 30.694 7.456 1.00 34.15 C ANISOU 10 CB ASN A 2 4358 4152 4466 431 802 630 C ATOM 11 CG ASN A 2 20.355 31.763 6.902 1.00 32.44 C ANISOU 11 CG ASN A 2 4124 3909 4293 456 854 689 C ATOM 12 OD1 ASN A 2 21.115 31.508 5.967 1.00 33.82 O ANISOU 12 OD1 ASN A 2 4301 4089 4458 483 892 713 O ATOM 13 ND2 ASN A 2 20.303 32.964 7.476 1.00 34.54 N ANISOU 13 ND2 ASN A 2 4371 4144 4609 446 855 712 N ATOM 14 N GLY A 3 16.089 29.468 7.425 1.00 24.58 N ANISOU 14 N GLY A 3 3190 3045 3102 423 713 532 N ATOM 15 CA GLY A 3 15.239 28.345 7.765 1.00 26.08 C ANISOU 15 CA GLY A 3 3395 3260 3256 402 674 476 C ATOM 16 C GLY A 3 14.031 28.249 6.855 1.00 31.24 C ANISOU 16 C GLY A 3 4064 3972 3833 428 664 460 C ATOM 17 O GLY A 3 13.983 28.906 5.810 1.00 28.54 O ANISOU 17 O GLY A 3 3726 3658 3461 469 691 494 O ATOM 18 N THR A 4 13.043 27.448 7.245 1.00 26.04 N ANISOU 18 N THR A 4 3413 3335 3145 407 626 409 N ATOM 19 CA THR A 4 11.867 27.196 6.421 1.00 23.41 C ANISOU 19 CA THR A 4 3093 3061 2742 428 612 383 C ATOM 20 C THR A 4 10.620 27.440 7.257 1.00 29.90 C ANISOU 20 C THR A 4 3911 3891 3560 404 572 358 C ATOM 21 O THR A 4 10.382 26.735 8.245 1.00 25.00 O ANISOU 21 O THR A 4 3288 3249 2960 365 544 322 O ATOM 22 CB THR A 4 11.877 25.766 5.871 1.00 23.48 C ANISOU 22 CB THR A 4 3116 3093 2713 428 607 338 C ATOM 23 OG1 THR A 4 13.104 25.532 5.166 1.00 22.14 O ANISOU 23 OG1 THR A 4 2949 2912 2550 449 646 362 O ATOM 24 CG2 THR A 4 10.694 25.550 4.925 1.00 24.36 C ANISOU 24 CG2 THR A 4 3237 3269 2749 453 592 309 C ATOM 25 N GLU A 5 9.830 28.435 6.868 1.00 26.60 N ANISOU 25 N GLU A 5 3491 3501 3116 429 570 379 N ATOM 26 CA GLU A 5 8.593 28.746 7.565 1.00 26.34 C ANISOU 26 CA GLU A 5 3453 3479 3076 411 535 358 C ATOM 27 C GLU A 5 7.410 28.147 6.817 1.00 26.46 C ANISOU 27 C GLU A 5 3477 3556 3022 426 513 318 C ATOM 28 O GLU A 5 7.348 28.197 5.585 1.00 24.07 O ANISOU 28 O GLU A 5 3181 3296 2668 467 530 328 O ATOM 29 CB GLU A 5 8.396 30.257 7.723 1.00 28.52 C ANISOU 29 CB GLU A 5 3718 3745 3372 426 545 405 C ATOM 30 CG GLU A 5 7.194 30.610 8.598 1.00 28.68 C ANISOU 30 CG GLU A 5 3732 3770 3394 404 510 383 C ATOM 31 CD GLU A 5 6.893 32.097 8.638 1.00 30.23 C ANISOU 31 CD GLU A 5 3920 3961 3606 424 520 428 C ATOM 32 OE1 GLU A 5 7.674 32.881 8.064 1.00 33.41 O ANISOU 32 OE1 GLU A 5 4320 4351 4024 452 558 477 O ATOM 33 OE2 GLU A 5 5.874 32.480 9.251 1.00 33.92 O ANISOU 33 OE2 GLU A 5 4382 4436 4072 412 494 414 O ATOM 34 N GLY A 6 6.488 27.560 7.573 1.00 26.96 N ANISOU 34 N GLY A 6 3538 3622 3083 393 477 271 N ATOM 35 CA GLY A 6 5.237 27.078 7.044 1.00 22.53 C ANISOU 35 CA GLY A 6 2979 3115 2464 401 451 229 C ATOM 36 C GLY A 6 4.081 27.680 7.816 1.00 24.20 C ANISOU 36 C GLY A 6 3181 3332 2681 386 422 222 C ATOM 37 O GLY A 6 4.256 28.614 8.603 1.00 23.01 O ANISOU 37 O GLY A 6 3023 3147 2572 376 426 254 O ATOM 38 N PRO A 7 2.870 27.161 7.598 1.00 23.28 N ANISOU 38 N PRO A 7 3062 3258 2523 383 393 176 N ATOM 39 CA PRO A 7 1.690 27.787 8.222 1.00 21.83 C ANISOU 39 CA PRO A 7 2869 3086 2340 373 367 170 C ATOM 40 C PRO A 7 1.733 27.795 9.741 1.00 24.38 C ANISOU 40 C PRO A 7 3186 3356 2722 328 354 166 C ATOM 41 O PRO A 7 1.287 28.768 10.360 1.00 24.65 O ANISOU 41 O PRO A 7 3212 3379 2774 325 348 187 O ATOM 42 CB PRO A 7 0.524 26.939 7.689 1.00 25.54 C ANISOU 42 CB PRO A 7 3336 3609 2758 374 339 114 C ATOM 43 CG PRO A 7 1.059 26.273 6.451 1.00 24.69 C ANISOU 43 CG PRO A 7 3239 3533 2610 402 355 102 C ATOM 44 CD PRO A 7 2.509 26.034 6.722 1.00 29.49 C ANISOU 44 CD PRO A 7 3856 4089 3261 391 384 127 C ATOM 45 N ASN A 8 2.273 26.742 10.361 1.00 19.61 N ANISOU 45 N ASN A 8 2586 2719 2147 294 352 139 N ATOM 46 CA ASN A 8 2.290 26.642 11.814 1.00 24.85 C ANISOU 46 CA ASN A 8 3245 3337 2861 253 339 132 C ATOM 47 C ASN A 8 3.618 26.102 12.343 1.00 24.31 C ANISOU 47 C ASN A 8 3181 3219 2835 234 356 142 C ATOM 48 O ASN A 8 3.654 25.505 13.423 1.00 21.08 O ANISOU 48 O ASN A 8 2772 2780 2459 200 343 122 O ATOM 49 CB ASN A 8 1.145 25.754 12.309 1.00 23.44 C ANISOU 49 CB ASN A 8 3063 3172 2671 224 310 80 C ATOM 50 CG ASN A 8 1.081 24.429 11.574 1.00 23.03 C ANISOU 50 CG ASN A 8 3017 3142 2591 223 309 35 C ATOM 51 OD1 ASN A 8 1.951 24.118 10.766 1.00 20.79 O ANISOU 51 OD1 ASN A 8 2742 2862 2297 241 329 44 O ATOM 52 ND2 ASN A 8 0.051 23.642 11.853 1.00 27.86 N ANISOU 52 ND2 ASN A 8 3623 3768 3193 200 286 -13 N ATOM 53 N PHE A 9 4.716 26.292 11.607 1.00 23.29 N ANISOU 53 N PHE A 9 3058 3084 2709 258 384 172 N ATOM 54 CA PHE A 9 6.013 25.797 12.057 1.00 25.29 C ANISOU 54 CA PHE A 9 3313 3293 3004 242 400 182 C ATOM 55 C PHE A 9 7.132 26.665 11.499 1.00 22.75 C ANISOU 55 C PHE A 9 2989 2956 2698 270 432 232 C ATOM 56 O PHE A 9 6.936 27.441 10.563 1.00 20.57 O ANISOU 56 O PHE A 9 2714 2710 2394 304 446 258 O ATOM 57 CB PHE A 9 6.227 24.326 11.665 1.00 19.85 C ANISOU 57 CB PHE A 9 2633 2608 2299 234 402 143 C ATOM 58 CG PHE A 9 6.172 24.061 10.182 1.00 23.87 C ANISOU 58 CG PHE A 9 3150 3162 2757 268 416 136 C ATOM 59 CD1 PHE A 9 7.306 24.195 9.392 1.00 24.68 C ANISOU 59 CD1 PHE A 9 3258 3260 2860 294 448 167 C ATOM 60 CD2 PHE A 9 4.994 23.642 9.583 1.00 23.28 C ANISOU 60 CD2 PHE A 9 3077 3135 2633 275 397 96 C ATOM 61 CE1 PHE A 9 7.258 23.935 8.036 1.00 26.52 C ANISOU 61 CE1 PHE A 9 3500 3537 3042 328 461 159 C ATOM 62 CE2 PHE A 9 4.941 23.382 8.222 1.00 22.81 C ANISOU 62 CE2 PHE A 9 3024 3121 2523 308 407 86 C ATOM 63 CZ PHE A 9 6.073 23.529 7.451 1.00 26.33 C ANISOU 63 CZ PHE A 9 3477 3562 2965 336 440 118 C ATOM 64 N TYR A 10 8.314 26.536 12.106 1.00 21.25 N ANISOU 64 N TYR A 10 2795 2720 2556 254 445 248 N ATOM 65 CA TYR A 10 9.537 27.142 11.586 1.00 22.07 C ANISOU 65 CA TYR A 10 2896 2806 2683 277 479 293 C ATOM 66 C TYR A 10 10.674 26.152 11.801 1.00 20.69 C ANISOU 66 C TYR A 10 2724 2602 2537 262 491 285 C ATOM 67 O TYR A 10 11.119 25.951 12.937 1.00 18.29 O ANISOU 67 O TYR A 10 2412 2260 2276 233 480 280 O ATOM 68 CB TYR A 10 9.852 28.481 12.256 1.00 18.50 C ANISOU 68 CB TYR A 10 2429 2322 2276 274 484 331 C ATOM 69 CG TYR A 10 11.055 29.169 11.646 1.00 20.35 C ANISOU 69 CG TYR A 10 2658 2537 2538 298 523 378 C ATOM 70 CD1 TYR A 10 10.909 30.023 10.557 1.00 26.96 C ANISOU 70 CD1 TYR A 10 3496 3399 3349 337 548 412 C ATOM 71 CD2 TYR A 10 12.339 28.942 12.133 1.00 25.51 C ANISOU 71 CD2 TYR A 10 3303 3148 3242 284 536 388 C ATOM 72 CE1 TYR A 10 12.002 30.643 9.980 1.00 22.24 C ANISOU 72 CE1 TYR A 10 2892 2781 2777 360 587 457 C ATOM 73 CE2 TYR A 10 13.440 29.560 11.562 1.00 23.71 C ANISOU 73 CE2 TYR A 10 3067 2901 3042 305 573 431 C ATOM 74 CZ TYR A 10 13.265 30.409 10.486 1.00 23.94 C ANISOU 74 CZ TYR A 10 3098 2953 3046 342 600 466 C ATOM 75 OH TYR A 10 14.357 31.027 9.911 1.00 24.24 O ANISOU 75 OH TYR A 10 3126 2969 3114 364 641 511 O ATOM 76 N VAL A 11 11.146 25.539 10.721 1.00 18.81 N ANISOU 76 N VAL A 11 2496 2381 2272 284 513 284 N ATOM 77 CA VAL A 11 12.213 24.546 10.789 1.00 18.81 C ANISOU 77 CA VAL A 11 2498 2355 2294 275 526 276 C ATOM 78 C VAL A 11 13.551 25.265 10.625 1.00 22.15 C ANISOU 78 C VAL A 11 2911 2749 2758 289 559 324 C ATOM 79 O VAL A 11 13.732 25.990 9.633 1.00 20.55 O ANISOU 79 O VAL A 11 2708 2563 2537 323 585 356 O ATOM 80 CB VAL A 11 12.029 23.455 9.730 1.00 24.63 C ANISOU 80 CB VAL A 11 3250 3126 2983 290 534 245 C ATOM 81 CG1 VAL A 11 13.201 22.488 9.752 1.00 20.18 C ANISOU 81 CG1 VAL A 11 2689 2534 2446 283 552 241 C ATOM 82 CG2 VAL A 11 10.706 22.712 9.975 1.00 25.39 C ANISOU 82 CG2 VAL A 11 3352 3247 3048 271 501 193 C ATOM 83 N PRO A 12 14.494 25.115 11.563 1.00 23.69 N ANISOU 83 N PRO A 12 3094 2898 3007 267 559 331 N ATOM 84 CA PRO A 12 15.815 25.759 11.428 1.00 23.70 C ANISOU 84 CA PRO A 12 3082 2869 3053 278 590 374 C ATOM 85 C PRO A 12 16.733 25.006 10.470 1.00 22.93 C ANISOU 85 C PRO A 12 2992 2776 2947 298 622 380 C ATOM 86 O PRO A 12 17.817 24.529 10.833 1.00 21.67 O ANISOU 86 O PRO A 12 2825 2584 2826 289 632 384 O ATOM 87 CB PRO A 12 16.328 25.759 12.877 1.00 18.82 C ANISOU 87 CB PRO A 12 2449 2209 2493 245 571 370 C ATOM 88 CG PRO A 12 15.669 24.590 13.515 1.00 18.95 C ANISOU 88 CG PRO A 12 2477 2232 2492 220 541 325 C ATOM 89 CD PRO A 12 14.316 24.470 12.878 1.00 18.40 C ANISOU 89 CD PRO A 12 2422 2206 2364 230 529 302 C ATOM 90 N PHE A 13 16.300 24.908 9.213 1.00 23.23 N ANISOU 90 N PHE A 13 3044 2855 2929 330 637 379 N ATOM 91 CA PHE A 13 17.020 24.146 8.201 1.00 23.65 C ANISOU 91 CA PHE A 13 3107 2918 2962 352 667 379 C ATOM 92 C PHE A 13 16.554 24.643 6.840 1.00 23.80 C ANISOU 92 C PHE A 13 3136 2984 2924 394 687 395 C ATOM 93 O PHE A 13 15.347 24.703 6.588 1.00 22.07 O ANISOU 93 O PHE A 13 2926 2803 2658 400 665 373 O ATOM 94 CB PHE A 13 16.755 22.642 8.363 1.00 22.90 C ANISOU 94 CB PHE A 13 3024 2829 2849 334 649 328 C ATOM 95 CG PHE A 13 17.692 21.762 7.581 1.00 22.15 C ANISOU 95 CG PHE A 13 2937 2732 2748 350 679 325 C ATOM 96 CD1 PHE A 13 17.436 21.454 6.252 1.00 27.28 C ANISOU 96 CD1 PHE A 13 3601 3424 3339 384 696 316 C ATOM 97 CD2 PHE A 13 18.818 21.225 8.181 1.00 19.99 C ANISOU 97 CD2 PHE A 13 2655 2417 2525 334 688 331 C ATOM 98 CE1 PHE A 13 18.296 20.638 5.533 1.00 22.85 C ANISOU 98 CE1 PHE A 13 3047 2862 2772 400 725 312 C ATOM 99 CE2 PHE A 13 19.684 20.410 7.468 1.00 28.01 C ANISOU 99 CE2 PHE A 13 3676 3430 3537 350 717 329 C ATOM 100 CZ PHE A 13 19.420 20.114 6.146 1.00 23.46 C ANISOU 100 CZ PHE A 13 3117 2895 2904 383 736 319 C ATOM 101 N SER A 14 17.503 25.014 5.983 1.00 25.33 N ANISOU 101 N SER A 14 3327 3175 3123 426 729 435 N ATOM 102 CA SER A 14 17.165 25.552 4.672 1.00 25.96 C ANISOU 102 CA SER A 14 3417 3299 3148 471 753 458 C ATOM 103 C SER A 14 16.480 24.499 3.808 1.00 24.38 C ANISOU 103 C SER A 14 3237 3149 2877 487 743 412 C ATOM 104 O SER A 14 16.868 23.328 3.804 1.00 25.43 O ANISOU 104 O SER A 14 3378 3276 3010 475 742 379 O ATOM 105 CB SER A 14 18.430 26.060 3.972 1.00 27.97 C ANISOU 105 CB SER A 14 3664 3537 3427 501 804 510 C ATOM 106 OG SER A 14 18.143 26.563 2.679 1.00 30.95 O ANISOU 106 OG SER A 14 4052 3959 3748 550 831 536 O ATOM 107 N ASN A 15 15.452 24.922 3.065 1.00 24.02 N ANISOU 107 N ASN A 15 3200 3155 2771 515 735 409 N ATOM 108 CA ASN A 15 14.802 24.061 2.083 1.00 27.74 C ANISOU 108 CA ASN A 15 3688 3681 3170 536 728 367 C ATOM 109 C ASN A 15 15.361 24.277 0.680 1.00 27.20 C ANISOU 109 C ASN A 15 3629 3646 3059 590 770 399 C ATOM 110 O ASN A 15 14.651 24.072 -0.307 1.00 26.39 O ANISOU 110 O ASN A 15 3538 3602 2885 622 766 378 O ATOM 111 CB ASN A 15 13.284 24.268 2.085 1.00 22.29 C ANISOU 111 CB ASN A 15 3001 3035 2434 536 690 338 C ATOM 112 CG ASN A 15 12.534 23.087 1.477 1.00 24.29 C ANISOU 112 CG ASN A 15 3266 3334 2627 539 669 274 C ATOM 113 OD1 ASN A 15 13.053 21.972 1.449 1.00 23.07 O ANISOU 113 OD1 ASN A 15 3118 3166 2481 526 673 241 O ATOM 114 ND2 ASN A 15 11.314 23.325 0.988 1.00 23.16 N ANISOU 114 ND2 ASN A 15 3127 3246 2428 557 645 253 N ATOM 115 N LYS A 16 16.632 24.675 0.574 1.00 27.46 N ANISOU 115 N LYS A 16 3655 3644 3135 601 812 448 N ATOM 116 CA LYS A 16 17.225 24.918 -0.739 1.00 28.90 C ANISOU 116 CA LYS A 16 3846 3855 3281 654 857 484 C ATOM 117 C LYS A 16 17.323 23.640 -1.567 1.00 30.09 C ANISOU 117 C LYS A 16 4014 4040 3381 669 861 438 C ATOM 118 O LYS A 16 17.283 23.699 -2.801 1.00 32.48 O ANISOU 118 O LYS A 16 4329 4391 3622 718 885 448 O ATOM 119 CB LYS A 16 18.608 25.556 -0.582 1.00 31.40 C ANISOU 119 CB LYS A 16 4148 4120 3663 657 902 544 C ATOM 120 CG LYS A 16 19.628 24.664 0.107 1.00 37.93 C ANISOU 120 CG LYS A 16 4969 4898 4547 623 904 526 C ATOM 121 CD LYS A 16 20.824 25.446 0.631 1.00 35.71 C ANISOU 121 CD LYS A 16 4664 4558 4345 613 935 579 C ATOM 122 CE LYS A 16 21.653 24.577 1.569 1.00 43.90 C ANISOU 122 CE LYS A 16 5693 5547 5442 573 925 556 C ATOM 123 NZ LYS A 16 22.614 25.368 2.390 1.00 37.63 N ANISOU 123 NZ LYS A 16 4871 4695 4731 553 940 597 N ATOM 124 N THR A 17 17.461 22.484 -0.921 1.00 30.21 N ANISOU 124 N THR A 17 4030 4029 3420 630 840 388 N ATOM 125 CA THR A 17 17.510 21.216 -1.636 1.00 28.39 C ANISOU 125 CA THR A 17 3815 3826 3147 640 842 339 C ATOM 126 C THR A 17 16.169 20.493 -1.668 1.00 29.31 C ANISOU 126 C THR A 17 3940 3982 3214 627 797 270 C ATOM 127 O THR A 17 16.073 19.424 -2.278 1.00 28.82 O ANISOU 127 O THR A 17 3890 3947 3115 635 795 221 O ATOM 128 CB THR A 17 18.580 20.300 -1.029 1.00 28.58 C ANISOU 128 CB THR A 17 3835 3796 3229 610 853 327 C ATOM 129 OG1 THR A 17 18.354 20.159 0.380 1.00 30.15 O ANISOU 129 OG1 THR A 17 4022 3950 3484 558 819 311 O ATOM 130 CG2 THR A 17 19.969 20.875 -1.267 1.00 34.28 C ANISOU 130 CG2 THR A 17 4549 4486 3992 630 902 390 C ATOM 131 N GLY A 18 15.138 21.039 -1.028 1.00 27.43 N ANISOU 131 N GLY A 18 3694 3750 2976 608 761 264 N ATOM 132 CA GLY A 18 13.801 20.489 -1.137 1.00 28.59 C ANISOU 132 CA GLY A 18 3847 3942 3076 599 720 202 C ATOM 133 C GLY A 18 13.449 19.376 -0.173 1.00 25.98 C ANISOU 133 C GLY A 18 3513 3579 2778 547 688 144 C ATOM 134 O GLY A 18 12.349 18.822 -0.277 1.00 25.11 O ANISOU 134 O GLY A 18 3406 3503 2633 537 656 88 O ATOM 135 N VAL A 19 14.327 19.041 0.779 1.00 23.13 N ANISOU 135 N VAL A 19 3147 3156 2486 513 696 155 N ATOM 136 CA VAL A 19 14.102 17.872 1.625 1.00 22.13 C ANISOU 136 CA VAL A 19 3019 2998 2390 468 672 103 C ATOM 137 C VAL A 19 13.295 18.182 2.881 1.00 23.72 C ANISOU 137 C VAL A 19 3210 3178 2624 428 636 96 C ATOM 138 O VAL A 19 12.981 17.255 3.641 1.00 25.90 O ANISOU 138 O VAL A 19 3486 3431 2926 391 616 55 O ATOM 139 CB VAL A 19 15.438 17.224 2.040 1.00 27.94 C ANISOU 139 CB VAL A 19 3754 3681 3181 454 698 116 C ATOM 140 CG1 VAL A 19 16.290 16.926 0.816 1.00 23.21 C ANISOU 140 CG1 VAL A 19 3166 3101 2552 494 737 124 C ATOM 141 CG2 VAL A 19 16.181 18.113 3.025 1.00 27.50 C ANISOU 141 CG2 VAL A 19 3684 3577 3188 438 706 172 C ATOM 142 N VAL A 20 12.953 19.444 3.126 1.00 23.70 N ANISOU 142 N VAL A 20 3200 3183 2624 436 630 137 N ATOM 143 CA VAL A 20 12.285 19.827 4.367 1.00 24.05 C ANISOU 143 CA VAL A 20 3233 3203 2702 399 599 135 C ATOM 144 C VAL A 20 10.825 19.394 4.316 1.00 25.55 C ANISOU 144 C VAL A 20 3424 3431 2852 388 563 81 C ATOM 145 O VAL A 20 10.114 19.677 3.345 1.00 25.15 O ANISOU 145 O VAL A 20 3377 3436 2743 419 558 70 O ATOM 146 CB VAL A 20 12.406 21.341 4.607 1.00 21.04 C ANISOU 146 CB VAL A 20 2842 2815 2338 412 606 195 C ATOM 147 CG1 VAL A 20 11.628 21.748 5.857 1.00 25.77 C ANISOU 147 CG1 VAL A 20 3430 3394 2967 377 573 189 C ATOM 148 CG2 VAL A 20 13.872 21.743 4.733 1.00 24.88 C ANISOU 148 CG2 VAL A 20 3322 3258 2872 418 641 246 C ATOM 149 N AARG A 21 10.376 18.699 5.357 0.46 26.96 N ANISOU 149 N AARG A 21 3599 3582 3063 346 538 46 N ATOM 150 N BARG A 21 10.379 18.705 5.367 0.54 26.97 N ANISOU 150 N BARG A 21 3600 3582 3064 345 538 46 N ATOM 151 CA AARG A 21 8.991 18.271 5.465 0.46 26.91 C ANISOU 151 CA AARG A 21 3590 3604 3029 329 504 -6 C ATOM 152 CA BARG A 21 9.011 18.228 5.494 0.54 26.92 C ANISOU 152 CA BARG A 21 3592 3604 3033 328 504 -7 C ATOM 153 C AARG A 21 8.429 18.693 6.814 0.46 25.39 C ANISOU 153 C AARG A 21 3388 3384 2877 294 480 1 C ATOM 154 C BARG A 21 8.434 18.710 6.819 0.54 25.40 C ANISOU 154 C BARG A 21 3388 3384 2878 294 480 2 C ATOM 155 O AARG A 21 9.162 18.822 7.800 0.46 24.01 O ANISOU 155 O AARG A 21 3209 3159 2754 273 486 29 O ATOM 156 O BARG A 21 9.164 18.898 7.797 0.54 24.00 O ANISOU 156 O BARG A 21 3208 3159 2753 274 486 32 O ATOM 157 CB AARG A 21 8.846 16.751 5.270 0.46 27.70 C ANISOU 157 CB AARG A 21 3696 3703 3125 312 501 -68 C ATOM 158 CB BARG A 21 8.942 16.690 5.406 0.54 27.72 C ANISOU 158 CB BARG A 21 3699 3698 3136 308 502 -67 C ATOM 159 CG AARG A 21 9.074 16.307 3.824 0.46 31.05 C ANISOU 159 CG AARG A 21 4130 4169 3497 349 518 -90 C ATOM 160 CG BARG A 21 9.644 16.112 4.175 0.54 31.78 C ANISOU 160 CG BARG A 21 4224 4232 3618 339 528 -79 C ATOM 161 CD AARG A 21 8.446 14.953 3.525 0.46 34.15 C ANISOU 161 CD AARG A 21 4526 4575 3874 333 505 -165 C ATOM 162 CD BARG A 21 9.660 14.586 4.176 0.54 33.71 C ANISOU 162 CD BARG A 21 4474 4460 3874 317 529 -138 C ATOM 163 NE AARG A 21 9.218 13.842 4.070 0.46 36.14 N ANISOU 163 NE AARG A 21 4782 4774 4175 306 520 -181 N ATOM 164 NE BARG A 21 8.390 14.011 3.747 0.54 36.71 N ANISOU 164 NE BARG A 21 4851 4881 4216 311 502 -202 N ATOM 165 CZ AARG A 21 8.888 12.565 3.929 0.46 38.82 C ANISOU 165 CZ AARG A 21 5124 5110 4517 288 515 -243 C ATOM 166 CZ BARG A 21 8.158 12.711 3.628 0.54 38.84 C ANISOU 166 CZ BARG A 21 5123 5144 4491 293 500 -263 C ATOM 167 NH1AARG A 21 7.803 12.201 3.264 0.46 39.39 N ANISOU 167 NH1AARG A 21 5192 5228 4544 292 494 -300 N ATOM 168 NH1BARG A 21 9.092 11.814 3.905 0.54 39.29 N ANISOU 168 NH1BARG A 21 5187 5155 4588 279 522 -266 N ATOM 169 NH2AARG A 21 9.667 11.630 4.467 0.46 37.28 N ANISOU 169 NH2AARG A 21 4933 4863 4370 266 533 -248 N ATOM 170 NH2BARG A 21 6.961 12.299 3.220 0.54 39.28 N ANISOU 170 NH2BARG A 21 5173 5240 4514 288 474 -322 N ATOM 171 N SER A 22 7.117 18.908 6.840 1.00 23.29 N ANISOU 171 N SER A 22 3116 3151 2582 290 451 -25 N ATOM 172 CA SER A 22 6.463 19.444 8.029 1.00 25.92 C ANISOU 172 CA SER A 22 3440 3464 2946 262 428 -16 C ATOM 173 C SER A 22 6.647 18.512 9.225 1.00 22.61 C ANISOU 173 C SER A 22 3019 2996 2577 218 422 -37 C ATOM 174 O SER A 22 6.513 17.288 9.088 1.00 19.50 O ANISOU 174 O SER A 22 2629 2598 2182 204 421 -82 O ATOM 175 CB SER A 22 4.968 19.654 7.773 1.00 24.72 C ANISOU 175 CB SER A 22 3280 3360 2753 264 399 -48 C ATOM 176 OG SER A 22 4.292 20.036 8.964 1.00 28.13 O ANISOU 176 OG SER A 22 3703 3772 3215 235 378 -46 O ATOM 177 N PRO A 23 6.939 19.058 10.412 1.00 19.84 N ANISOU 177 N PRO A 23 2662 2606 2270 199 418 -6 N ATOM 178 CA PRO A 23 7.048 18.225 11.619 1.00 22.73 C ANISOU 178 CA PRO A 23 3028 2928 2681 161 411 -22 C ATOM 179 C PRO A 23 5.720 17.703 12.133 1.00 25.69 C ANISOU 179 C PRO A 23 3397 3312 3050 135 385 -65 C ATOM 180 O PRO A 23 5.709 16.988 13.144 1.00 21.38 O ANISOU 180 O PRO A 23 2851 2733 2540 105 380 -78 O ATOM 181 CB PRO A 23 7.684 19.180 12.640 1.00 18.43 C ANISOU 181 CB PRO A 23 2476 2349 2177 154 411 26 C ATOM 182 CG PRO A 23 7.240 20.532 12.196 1.00 22.73 C ANISOU 182 CG PRO A 23 3015 2923 2697 177 407 53 C ATOM 183 CD PRO A 23 7.249 20.472 10.690 1.00 22.15 C ANISOU 183 CD PRO A 23 2948 2892 2576 212 421 47 C ATOM 184 N PHE A 24 4.606 18.069 11.504 1.00 24.10 N ANISOU 184 N PHE A 24 3192 3158 2807 146 368 -86 N ATOM 185 CA PHE A 24 3.311 17.468 11.781 1.00 25.07 C ANISOU 185 CA PHE A 24 3308 3296 2923 124 346 -134 C ATOM 186 C PHE A 24 2.941 16.390 10.770 1.00 26.55 C ANISOU 186 C PHE A 24 3497 3510 3081 128 346 -188 C ATOM 187 O PHE A 24 1.825 15.866 10.826 1.00 21.40 O ANISOU 187 O PHE A 24 2836 2874 2420 110 328 -234 O ATOM 188 CB PHE A 24 2.222 18.549 11.813 1.00 24.31 C ANISOU 188 CB PHE A 24 3202 3234 2802 132 324 -126 C ATOM 189 CG PHE A 24 2.448 19.608 12.865 1.00 23.47 C ANISOU 189 CG PHE A 24 3092 3100 2726 126 321 -80 C ATOM 190 CD1 PHE A 24 2.496 19.271 14.206 1.00 23.40 C ANISOU 190 CD1 PHE A 24 3081 3049 2761 93 316 -79 C ATOM 191 CD2 PHE A 24 2.614 20.935 12.509 1.00 25.91 C ANISOU 191 CD2 PHE A 24 3399 3426 3021 153 324 -38 C ATOM 192 CE1 PHE A 24 2.704 20.233 15.173 1.00 24.47 C ANISOU 192 CE1 PHE A 24 3213 3163 2922 88 311 -41 C ATOM 193 CE2 PHE A 24 2.821 21.908 13.476 1.00 23.30 C ANISOU 193 CE2 PHE A 24 3063 3068 2720 146 322 0 C ATOM 194 CZ PHE A 24 2.866 21.554 14.810 1.00 21.60 C ANISOU 194 CZ PHE A 24 2846 2814 2546 113 314 -4 C ATOM 195 N GLU A 25 3.849 16.043 9.852 1.00 26.28 N ANISOU 195 N GLU A 25 3473 3481 3032 150 368 -186 N ATOM 196 CA GLU A 25 3.556 15.094 8.781 1.00 24.21 C ANISOU 196 CA GLU A 25 3213 3249 2738 159 369 -240 C ATOM 197 C GLU A 25 4.533 13.932 8.686 1.00 27.67 C ANISOU 197 C GLU A 25 3661 3651 3201 151 393 -255 C ATOM 198 O GLU A 25 4.103 12.808 8.419 1.00 28.76 O ANISOU 198 O GLU A 25 3797 3790 3338 136 391 -311 O ATOM 199 CB GLU A 25 3.516 15.834 7.440 1.00 28.85 C ANISOU 199 CB GLU A 25 3804 3894 3266 204 371 -230 C ATOM 200 CG GLU A 25 2.364 16.808 7.316 1.00 31.89 C ANISOU 200 CG GLU A 25 4177 4323 3617 216 346 -227 C ATOM 201 CD GLU A 25 2.357 17.529 5.984 1.00 40.51 C ANISOU 201 CD GLU A 25 5271 5472 4648 265 350 -213 C ATOM 202 OE1 GLU A 25 3.371 17.440 5.252 1.00 39.81 O ANISOU 202 OE1 GLU A 25 5194 5384 4546 290 376 -195 O ATOM 203 OE2 GLU A 25 1.336 18.179 5.670 1.00 42.74 O ANISOU 203 OE2 GLU A 25 5545 5800 4894 280 329 -219 O ATOM 204 N ALA A 26 5.826 14.163 8.878 1.00 20.12 N ANISOU 204 N ALA A 26 2712 2662 2268 160 417 -209 N ATOM 205 CA ALA A 26 6.819 13.148 8.566 1.00 25.00 C ANISOU 205 CA ALA A 26 3341 3255 2904 161 442 -220 C ATOM 206 C ALA A 26 7.958 13.186 9.572 1.00 24.93 C ANISOU 206 C ALA A 26 3334 3190 2947 148 459 -174 C ATOM 207 O ALA A 26 8.221 14.226 10.186 1.00 22.71 O ANISOU 207 O ALA A 26 3048 2899 2681 150 455 -127 O ATOM 208 CB ALA A 26 7.374 13.336 7.147 1.00 35.08 C ANISOU 208 CB ALA A 26 4625 4568 4134 202 460 -216 C ATOM 209 N PRO A 27 8.665 12.067 9.750 1.00 26.07 N ANISOU 209 N PRO A 27 3484 3298 3123 137 477 -188 N ATOM 210 CA PRO A 27 9.850 12.069 10.611 1.00 26.33 C ANISOU 210 CA PRO A 27 3518 3282 3204 130 493 -145 C ATOM 211 C PRO A 27 10.881 13.073 10.125 1.00 25.60 C ANISOU 211 C PRO A 27 3427 3197 3104 160 510 -93 C ATOM 212 O PRO A 27 11.021 13.330 8.930 1.00 22.38 O ANISOU 212 O PRO A 27 3024 2824 2657 190 521 -95 O ATOM 213 CB PRO A 27 10.371 10.634 10.495 1.00 23.81 C ANISOU 213 CB PRO A 27 3206 2933 2907 121 514 -175 C ATOM 214 CG PRO A 27 9.153 9.830 10.186 1.00 27.07 C ANISOU 214 CG PRO A 27 3618 3365 3303 105 500 -238 C ATOM 215 CD PRO A 27 8.313 10.707 9.303 1.00 29.76 C ANISOU 215 CD PRO A 27 3955 3763 3588 125 482 -248 C ATOM 216 N GLN A 28 11.615 13.648 11.073 1.00 19.76 N ANISOU 216 N GLN A 28 2682 2424 2403 154 512 -48 N ATOM 217 CA GLN A 28 12.535 14.735 10.749 1.00 23.34 C ANISOU 217 CA GLN A 28 3131 2880 2857 179 526 3 C ATOM 218 C GLN A 28 13.949 14.239 10.497 1.00 22.15 C ANISOU 218 C GLN A 28 2983 2701 2732 190 557 22 C ATOM 219 O GLN A 28 14.926 14.906 10.841 1.00 22.68 O ANISOU 219 O GLN A 28 3043 2747 2828 197 568 67 O ATOM 220 CB GLN A 28 12.506 15.778 11.859 1.00 20.97 C ANISOU 220 CB GLN A 28 2820 2562 2585 166 510 40 C ATOM 221 CG GLN A 28 11.114 16.378 12.088 1.00 26.64 C ANISOU 221 CG GLN A 28 3534 3308 3278 157 481 25 C ATOM 222 CD GLN A 28 10.655 17.273 10.946 1.00 21.72 C ANISOU 222 CD GLN A 28 2913 2733 2608 187 483 32 C ATOM 223 OE1 GLN A 28 11.085 18.422 10.832 1.00 24.70 O ANISOU 223 OE1 GLN A 28 3284 3111 2988 205 491 75 O ATOM 224 NE2 GLN A 28 9.773 16.751 10.097 1.00 22.41 N ANISOU 224 NE2 GLN A 28 3006 2858 2652 195 476 -10 N ATOM 225 N TYR A 29 14.083 13.059 9.889 1.00 20.53 N ANISOU 225 N TYR A 29 2787 2495 2517 193 571 -14 N ATOM 226 CA TYR A 29 15.398 12.454 9.711 1.00 23.76 C ANISOU 226 CA TYR A 29 3198 2875 2952 203 600 1 C ATOM 227 C TYR A 29 16.282 13.224 8.739 1.00 23.86 C ANISOU 227 C TYR A 29 3211 2905 2950 238 626 38 C ATOM 228 O TYR A 29 17.481 12.938 8.670 1.00 21.81 O ANISOU 228 O TYR A 29 2950 2620 2718 247 651 60 O ATOM 229 CB TYR A 29 15.247 11.004 9.249 1.00 26.18 C ANISOU 229 CB TYR A 29 3516 3178 3253 197 611 -50 C ATOM 230 CG TYR A 29 14.502 10.111 10.228 1.00 23.98 C ANISOU 230 CG TYR A 29 3237 2874 2999 162 594 -83 C ATOM 231 CD1 TYR A 29 14.567 10.332 11.602 1.00 26.96 C ANISOU 231 CD1 TYR A 29 3607 3221 3417 140 580 -57 C ATOM 232 CD2 TYR A 29 13.734 9.046 9.773 1.00 30.03 C ANISOU 232 CD2 TYR A 29 4010 3650 3750 153 592 -141 C ATOM 233 CE1 TYR A 29 13.884 9.511 12.491 1.00 21.80 C ANISOU 233 CE1 TYR A 29 2954 2545 2786 111 567 -84 C ATOM 234 CE2 TYR A 29 13.054 8.224 10.646 1.00 27.25 C ANISOU 234 CE2 TYR A 29 3657 3272 3425 121 581 -170 C ATOM 235 CZ TYR A 29 13.129 8.459 12.002 1.00 23.93 C ANISOU 235 CZ TYR A 29 3229 2820 3042 101 570 -139 C ATOM 236 OH TYR A 29 12.447 7.639 12.868 1.00 25.80 O ANISOU 236 OH TYR A 29 3465 3032 3305 72 562 -163 O ATOM 237 N TYR A 30 15.733 14.193 8.001 1.00 24.62 N ANISOU 237 N TYR A 30 3308 3043 3004 259 622 47 N ATOM 238 CA TYR A 30 16.564 14.998 7.109 1.00 23.45 C ANISOU 238 CA TYR A 30 3159 2909 2843 294 649 88 C ATOM 239 C TYR A 30 17.476 15.957 7.869 1.00 23.30 C ANISOU 239 C TYR A 30 3125 2857 2873 291 656 144 C ATOM 240 O TYR A 30 18.464 16.428 7.295 1.00 26.56 O ANISOU 240 O TYR A 30 3533 3265 3292 316 686 181 O ATOM 241 CB TYR A 30 15.691 15.790 6.127 1.00 24.41 C ANISOU 241 CB TYR A 30 3285 3085 2905 321 644 86 C ATOM 242 CG TYR A 30 14.779 16.801 6.794 1.00 25.00 C ANISOU 242 CG TYR A 30 3351 3169 2980 308 615 99 C ATOM 243 CD1 TYR A 30 15.208 18.101 7.036 1.00 23.59 C ANISOU 243 CD1 TYR A 30 3162 2981 2821 318 622 153 C ATOM 244 CD2 TYR A 30 13.493 16.454 7.182 1.00 20.23 C ANISOU 244 CD2 TYR A 30 2748 2580 2359 286 583 57 C ATOM 245 CE1 TYR A 30 14.379 19.025 7.651 1.00 25.47 C ANISOU 245 CE1 TYR A 30 3392 3225 3062 307 598 164 C ATOM 246 CE2 TYR A 30 12.660 17.370 7.793 1.00 26.58 C ANISOU 246 CE2 TYR A 30 3544 3393 3163 276 558 68 C ATOM 247 CZ TYR A 30 13.108 18.656 8.024 1.00 25.08 C ANISOU 247 CZ TYR A 30 3345 3192 2991 287 565 122 C ATOM 248 OH TYR A 30 12.276 19.570 8.632 1.00 27.47 O ANISOU 248 OH TYR A 30 3640 3503 3296 277 542 132 O ATOM 249 N LEU A 31 17.174 16.248 9.139 1.00 23.13 N ANISOU 249 N LEU A 31 3094 2811 2885 262 630 150 N ATOM 250 CA LEU A 31 17.932 17.232 9.903 1.00 23.28 C ANISOU 250 CA LEU A 31 3096 2801 2949 257 632 197 C ATOM 251 C LEU A 31 18.701 16.640 11.079 1.00 21.14 C ANISOU 251 C LEU A 31 2816 2484 2732 233 628 201 C ATOM 252 O LEU A 31 19.482 17.362 11.706 1.00 19.16 O ANISOU 252 O LEU A 31 2549 2209 2522 230 630 236 O ATOM 253 CB LEU A 31 17.004 18.362 10.398 1.00 23.47 C ANISOU 253 CB LEU A 31 3113 2838 2966 249 606 207 C ATOM 254 CG LEU A 31 15.734 18.146 11.236 1.00 27.98 C ANISOU 254 CG LEU A 31 3686 3415 3528 222 570 174 C ATOM 255 CD1 LEU A 31 16.057 17.666 12.640 1.00 18.62 C ANISOU 255 CD1 LEU A 31 2495 2191 2390 191 555 171 C ATOM 256 CD2 LEU A 31 14.892 19.426 11.314 1.00 21.09 C ANISOU 256 CD2 LEU A 31 2809 2565 2640 226 554 189 C ATOM 257 N ALA A 32 18.506 15.361 11.390 1.00 19.19 N ANISOU 257 N ALA A 32 2578 2226 2488 217 622 165 N ATOM 258 CA ALA A 32 19.282 14.677 12.416 1.00 25.04 C ANISOU 258 CA ALA A 32 3312 2926 3277 199 621 170 C ATOM 259 C ALA A 32 19.166 13.179 12.182 1.00 22.17 C ANISOU 259 C ALA A 32 2962 2556 2906 194 630 132 C ATOM 260 O ALA A 32 18.179 12.702 11.615 1.00 23.86 O ANISOU 260 O ALA A 32 3189 2794 3083 192 624 93 O ATOM 261 CB ALA A 32 18.800 15.043 13.826 1.00 22.86 C ANISOU 261 CB ALA A 32 3027 2635 3025 173 589 174 C ATOM 262 N GLU A 33 20.176 12.442 12.620 1.00 22.97 N ANISOU 262 N GLU A 33 3059 2622 3045 192 644 141 N ATOM 263 CA GLU A 33 20.156 11.003 12.422 1.00 24.76 C ANISOU 263 CA GLU A 33 3299 2837 3273 187 657 107 C ATOM 264 C GLU A 33 19.249 10.324 13.444 1.00 24.36 C ANISOU 264 C GLU A 33 3251 2772 3231 158 633 80 C ATOM 265 O GLU A 33 18.972 10.881 14.508 1.00 27.07 O ANISOU 265 O GLU A 33 3586 3108 3590 143 610 96 O ATOM 266 CB GLU A 33 21.566 10.442 12.512 1.00 32.37 C ANISOU 266 CB GLU A 33 4256 3768 4275 198 682 128 C ATOM 267 CG GLU A 33 22.481 10.919 11.410 1.00 28.31 C ANISOU 267 CG GLU A 33 3738 3265 3752 227 712 152 C ATOM 268 CD GLU A 33 23.708 10.058 11.298 1.00 39.11 C ANISOU 268 CD GLU A 33 5105 4605 5152 238 741 161 C ATOM 269 OE1 GLU A 33 23.550 8.846 11.036 1.00 34.14 O ANISOU 269 OE1 GLU A 33 4488 3966 4517 236 752 127 O ATOM 270 OE2 GLU A 33 24.826 10.586 11.495 1.00 44.89 O ANISOU 270 OE2 GLU A 33 5819 5320 5916 248 753 201 O ATOM 271 N PRO A 34 18.754 9.121 13.126 1.00 26.73 N ANISOU 271 N PRO A 34 3565 3069 3523 151 641 38 N ATOM 272 CA PRO A 34 17.840 8.437 14.056 1.00 21.14 C ANISOU 272 CA PRO A 34 2860 2346 2826 124 623 13 C ATOM 273 C PRO A 34 18.402 8.237 15.453 1.00 27.03 C ANISOU 273 C PRO A 34 3597 3056 3617 112 617 41 C ATOM 274 O PRO A 34 17.648 8.338 16.428 1.00 22.01 O ANISOU 274 O PRO A 34 2959 2416 2986 92 595 39 O ATOM 275 CB PRO A 34 17.579 7.101 13.349 1.00 21.90 C ANISOU 275 CB PRO A 34 2968 2436 2916 123 642 -34 C ATOM 276 CG PRO A 34 17.666 7.443 11.897 1.00 25.81 C ANISOU 276 CG PRO A 34 3470 2968 3371 147 655 -46 C ATOM 277 CD PRO A 34 18.748 8.494 11.789 1.00 26.54 C ANISOU 277 CD PRO A 34 3553 3062 3470 168 664 6 C ATOM 278 N TRP A 35 19.700 7.953 15.593 1.00 22.81 N ANISOU 278 N TRP A 35 3057 2496 3113 124 636 68 N ATOM 279 CA TRP A 35 20.231 7.734 16.935 1.00 22.17 C ANISOU 279 CA TRP A 35 2967 2384 3072 116 628 95 C ATOM 280 C TRP A 35 20.152 8.990 17.793 1.00 22.16 C ANISOU 280 C TRP A 35 2953 2394 3074 110 600 124 C ATOM 281 O TRP A 35 20.121 8.883 19.024 1.00 22.34 O ANISOU 281 O TRP A 35 2970 2400 3117 99 584 136 O ATOM 282 CB TRP A 35 21.672 7.221 16.865 1.00 23.33 C ANISOU 282 CB TRP A 35 3108 2505 3250 133 654 118 C ATOM 283 CG TRP A 35 22.663 8.191 16.291 1.00 24.49 C ANISOU 283 CG TRP A 35 3242 2663 3399 153 662 149 C ATOM 284 CD1 TRP A 35 23.083 8.262 14.996 1.00 29.61 C ANISOU 284 CD1 TRP A 35 3895 3324 4030 172 687 146 C ATOM 285 CD2 TRP A 35 23.373 9.214 16.999 1.00 27.87 C ANISOU 285 CD2 TRP A 35 3650 3088 3850 156 648 188 C ATOM 286 NE1 TRP A 35 24.006 9.269 14.852 1.00 28.62 N ANISOU 286 NE1 TRP A 35 3753 3203 3918 187 692 183 N ATOM 287 CE2 TRP A 35 24.202 9.869 16.067 1.00 28.85 C ANISOU 287 CE2 TRP A 35 3766 3221 3973 176 667 208 C ATOM 288 CE3 TRP A 35 23.385 9.645 18.332 1.00 32.93 C ANISOU 288 CE3 TRP A 35 4279 3721 4512 144 621 207 C ATOM 289 CZ2 TRP A 35 25.035 10.931 16.423 1.00 31.69 C ANISOU 289 CZ2 TRP A 35 4104 3578 4358 182 661 244 C ATOM 290 CZ3 TRP A 35 24.215 10.700 18.682 1.00 28.76 C ANISOU 290 CZ3 TRP A 35 3729 3193 4005 150 612 239 C ATOM 291 CH2 TRP A 35 25.027 11.329 17.733 1.00 26.00 C ANISOU 291 CH2 TRP A 35 3370 2848 3660 168 633 257 C ATOM 292 N GLN A 36 20.101 10.176 17.174 1.00 22.87 N ANISOU 292 N GLN A 36 3038 2510 3143 119 594 134 N ATOM 293 CA GLN A 36 19.945 11.407 17.945 1.00 22.28 C ANISOU 293 CA GLN A 36 2949 2443 3072 113 568 157 C ATOM 294 C GLN A 36 18.533 11.533 18.509 1.00 23.68 C ANISOU 294 C GLN A 36 3134 2635 3230 93 543 135 C ATOM 295 O GLN A 36 18.354 11.949 19.661 1.00 18.93 O ANISOU 295 O GLN A 36 2524 2027 2642 82 520 148 O ATOM 296 CB GLN A 36 20.292 12.619 17.078 1.00 24.66 C ANISOU 296 CB GLN A 36 3243 2765 3362 130 574 177 C ATOM 297 CG GLN A 36 21.723 12.628 16.552 1.00 27.25 C ANISOU 297 CG GLN A 36 3561 3079 3714 150 601 203 C ATOM 298 CD GLN A 36 21.972 13.735 15.542 1.00 24.85 C ANISOU 298 CD GLN A 36 3251 2796 3395 168 614 222 C ATOM 299 OE1 GLN A 36 21.834 13.534 14.336 1.00 28.57 O ANISOU 299 OE1 GLN A 36 3734 3285 3836 184 635 210 O ATOM 300 NE2 GLN A 36 22.342 14.907 16.032 1.00 29.73 N ANISOU 300 NE2 GLN A 36 3851 3410 4034 168 603 251 N ATOM 301 N PHE A 37 17.516 11.184 17.711 1.00 22.71 N ANISOU 301 N PHE A 37 3024 2532 3074 89 545 101 N ATOM 302 CA PHE A 37 16.147 11.150 18.226 1.00 21.10 C ANISOU 302 CA PHE A 37 2825 2339 2854 70 523 77 C ATOM 303 C PHE A 37 16.002 10.105 19.324 1.00 20.24 C ANISOU 303 C PHE A 37 2719 2201 2770 53 522 70 C ATOM 304 O PHE A 37 15.301 10.330 20.316 1.00 19.51 O ANISOU 304 O PHE A 37 2624 2108 2680 38 501 71 O ATOM 305 CB PHE A 37 15.150 10.858 17.099 1.00 22.23 C ANISOU 305 CB PHE A 37 2978 2509 2958 70 527 37 C ATOM 306 CG PHE A 37 15.015 11.967 16.092 1.00 22.79 C ANISOU 306 CG PHE A 37 3047 2615 2997 87 525 44 C ATOM 307 CD1 PHE A 37 14.178 13.048 16.334 1.00 18.17 C ANISOU 307 CD1 PHE A 37 2457 2053 2394 83 502 49 C ATOM 308 CD2 PHE A 37 15.717 11.922 14.892 1.00 22.49 C ANISOU 308 CD2 PHE A 37 3013 2587 2945 111 549 46 C ATOM 309 CE1 PHE A 37 14.052 14.068 15.407 1.00 20.98 C ANISOU 309 CE1 PHE A 37 2811 2440 2720 102 503 60 C ATOM 310 CE2 PHE A 37 15.593 12.936 13.964 1.00 18.66 C ANISOU 310 CE2 PHE A 37 2526 2135 2429 130 550 57 C ATOM 311 CZ PHE A 37 14.763 14.010 14.218 1.00 18.49 C ANISOU 311 CZ PHE A 37 2500 2135 2391 126 528 65 C ATOM 312 N ASER A 38 16.653 8.948 19.162 0.83 20.10 N ANISOU 312 N ASER A 38 2706 2158 2772 57 545 64 N ATOM 313 N BSER A 38 16.647 8.948 19.151 0.18 19.33 N ANISOU 313 N BSER A 38 2609 2061 2674 57 545 64 N ATOM 314 CA ASER A 38 16.551 7.900 20.172 0.83 23.39 C ANISOU 314 CA ASER A 38 3127 2545 3216 44 549 62 C ATOM 315 CA BSER A 38 16.577 7.895 20.157 0.18 21.78 C ANISOU 315 CA BSER A 38 2922 2340 3011 45 549 62 C ATOM 316 C ASER A 38 17.164 8.337 21.499 0.83 20.06 C ANISOU 316 C ASER A 38 2694 2110 2817 46 534 100 C ATOM 317 C BSER A 38 17.138 8.364 21.492 0.18 19.65 C ANISOU 317 C BSER A 38 2642 2059 2764 46 533 99 C ATOM 318 O ASER A 38 16.740 7.869 22.561 0.83 21.83 O ANISOU 318 O ASER A 38 2921 2321 3054 34 527 102 O ATOM 319 O BSER A 38 16.652 7.952 22.552 0.18 21.67 O ANISOU 319 O BSER A 38 2900 2303 3031 34 525 100 O ATOM 320 CB ASER A 38 17.219 6.620 19.671 0.83 21.42 C ANISOU 320 CB ASER A 38 2884 2270 2984 52 580 51 C ATOM 321 CB BSER A 38 17.330 6.659 19.667 0.18 21.38 C ANISOU 321 CB BSER A 38 2879 2264 2981 54 581 54 C ATOM 322 OG ASER A 38 16.981 5.542 20.563 0.83 19.87 O ANISOU 322 OG ASER A 38 2693 2044 2814 40 587 47 O ATOM 323 OG BSER A 38 17.026 6.381 18.311 0.18 21.22 O ANISOU 323 OG BSER A 38 2866 2259 2936 58 595 20 O ATOM 324 N MET A 39 18.161 9.221 21.460 1.00 18.80 N ANISOU 324 N MET A 39 2522 1955 2665 60 530 129 N ATOM 325 CA MET A 39 18.719 9.763 22.696 1.00 22.41 C ANISOU 325 CA MET A 39 2967 2406 3144 61 511 160 C ATOM 326 C MET A 39 17.718 10.664 23.408 1.00 20.09 C ANISOU 326 C MET A 39 2670 2130 2833 48 481 158 C ATOM 327 O MET A 39 17.682 10.707 24.643 1.00 18.07 O ANISOU 327 O MET A 39 2410 1869 2589 43 465 171 O ATOM 328 CB MET A 39 20.003 10.537 22.404 1.00 24.46 C ANISOU 328 CB MET A 39 3209 2665 3419 78 514 188 C ATOM 329 CG MET A 39 21.169 9.685 21.963 1.00 24.83 C ANISOU 329 CG MET A 39 3254 2690 3488 94 542 198 C ATOM 330 SD MET A 39 22.635 10.692 21.699 1.00 40.13 S ANISOU 330 SD MET A 39 5169 4628 5450 112 544 232 S ATOM 331 CE MET A 39 22.915 11.341 23.347 1.00 41.61 C ANISOU 331 CE MET A 39 5337 4813 5658 106 510 254 C ATOM 332 N LEU A 40 16.928 11.428 22.648 1.00 22.18 N ANISOU 332 N LEU A 40 2938 2421 3071 44 474 142 N ATOM 333 CA LEU A 40 15.896 12.254 23.267 1.00 20.99 C ANISOU 333 CA LEU A 40 2785 2288 2904 32 448 138 C ATOM 334 C LEU A 40 14.841 11.394 23.950 1.00 20.42 C ANISOU 334 C LEU A 40 2723 2210 2827 15 445 118 C ATOM 335 O LEU A 40 14.344 11.746 25.026 1.00 19.88 O ANISOU 335 O LEU A 40 2652 2144 2759 6 425 124 O ATOM 336 CB LEU A 40 15.238 13.162 22.227 1.00 18.63 C ANISOU 336 CB LEU A 40 2486 2016 2575 34 444 126 C ATOM 337 CG LEU A 40 16.098 14.151 21.431 1.00 21.47 C ANISOU 337 CG LEU A 40 2837 2385 2937 51 451 147 C ATOM 338 CD1 LEU A 40 15.217 15.040 20.577 1.00 17.99 C ANISOU 338 CD1 LEU A 40 2398 1975 2464 54 446 137 C ATOM 339 CD2 LEU A 40 16.961 14.990 22.346 1.00 21.74 C ANISOU 339 CD2 LEU A 40 2854 2409 2999 54 438 177 C ATOM 340 N ALA A 41 14.475 10.268 23.332 1.00 17.57 N ANISOU 340 N ALA A 41 2372 1839 2463 10 465 92 N ATOM 341 CA ALA A 41 13.414 9.429 23.881 1.00 21.23 C ANISOU 341 CA ALA A 41 2845 2295 2927 -7 466 71 C ATOM 342 C ALA A 41 13.878 8.687 25.128 1.00 17.88 C ANISOU 342 C ALA A 41 2421 1842 2530 -7 470 92 C ATOM 343 O ALA A 41 13.102 8.503 26.072 1.00 20.40 O ANISOU 343 O ALA A 41 2742 2159 2850 -18 462 91 O ATOM 344 CB ALA A 41 12.924 8.443 22.820 1.00 21.27 C ANISOU 344 CB ALA A 41 2859 2296 2925 -13 486 34 C ATOM 345 N ALA A 42 15.133 8.237 25.145 1.00 17.95 N ANISOU 345 N ALA A 42 2427 1831 2561 8 485 113 N ATOM 346 CA ALA A 42 15.662 7.570 26.331 1.00 17.97 C ANISOU 346 CA ALA A 42 2428 1810 2587 14 489 137 C ATOM 347 C ALA A 42 15.726 8.529 27.510 1.00 22.14 C ANISOU 347 C ALA A 42 2947 2352 3112 16 460 161 C ATOM 348 O ALA A 42 15.472 8.140 28.656 1.00 22.42 O ANISOU 348 O ALA A 42 2986 2380 3154 15 456 173 O ATOM 349 CB ALA A 42 17.044 6.993 26.035 1.00 18.13 C ANISOU 349 CB ALA A 42 2446 1811 2632 32 509 155 C ATOM 350 N TYR A 43 16.088 9.783 27.244 1.00 22.05 N ANISOU 350 N TYR A 43 2925 2361 3092 21 441 169 N ATOM 351 CA TYR A 43 16.133 10.800 28.285 1.00 20.18 C ANISOU 351 CA TYR A 43 2677 2138 2852 23 413 185 C ATOM 352 C TYR A 43 14.738 11.097 28.831 1.00 21.33 C ANISOU 352 C TYR A 43 2829 2298 2977 7 398 170 C ATOM 353 O TYR A 43 14.558 11.216 30.045 1.00 22.62 O ANISOU 353 O TYR A 43 2990 2463 3140 8 382 182 O ATOM 354 CB TYR A 43 16.811 12.043 27.708 1.00 24.67 C ANISOU 354 CB TYR A 43 3231 2721 3422 30 402 194 C ATOM 355 CG TYR A 43 16.835 13.293 28.554 1.00 21.05 C ANISOU 355 CG TYR A 43 2760 2278 2962 30 372 204 C ATOM 356 CD1 TYR A 43 17.681 13.410 29.651 1.00 19.93 C ANISOU 356 CD1 TYR A 43 2604 2130 2837 40 357 224 C ATOM 357 CD2 TYR A 43 16.064 14.389 28.203 1.00 19.75 C ANISOU 357 CD2 TYR A 43 2593 2132 2780 22 358 193 C ATOM 358 CE1 TYR A 43 17.715 14.582 30.401 1.00 21.74 C ANISOU 358 CE1 TYR A 43 2820 2374 3067 40 329 228 C ATOM 359 CE2 TYR A 43 16.091 15.551 28.934 1.00 19.46 C ANISOU 359 CE2 TYR A 43 2543 2106 2744 22 333 200 C ATOM 360 CZ TYR A 43 16.911 15.645 30.032 1.00 25.69 C ANISOU 360 CZ TYR A 43 3319 2890 3551 30 318 216 C ATOM 361 OH TYR A 43 16.922 16.816 30.744 1.00 26.82 O ANISOU 361 OH TYR A 43 3449 3045 3698 29 292 218 O ATOM 362 N MET A 44 13.730 11.184 27.958 1.00 19.56 N ANISOU 362 N MET A 44 2612 2085 2734 -6 402 144 N ATOM 363 CA MET A 44 12.374 11.451 28.437 1.00 18.15 C ANISOU 363 CA MET A 44 2438 1921 2538 -20 388 129 C ATOM 364 C MET A 44 11.815 10.271 29.222 1.00 18.80 C ANISOU 364 C MET A 44 2530 1985 2630 -28 402 126 C ATOM 365 O MET A 44 11.091 10.464 30.206 1.00 19.35 O ANISOU 365 O MET A 44 2600 2061 2692 -34 389 130 O ATOM 366 CB MET A 44 11.450 11.796 27.268 1.00 18.85 C ANISOU 366 CB MET A 44 2530 2029 2606 -30 389 101 C ATOM 367 CG MET A 44 11.763 13.121 26.577 1.00 22.57 C ANISOU 367 CG MET A 44 2991 2520 3064 -22 376 107 C ATOM 368 SD MET A 44 11.843 14.531 27.703 1.00 22.69 S ANISOU 368 SD MET A 44 2994 2547 3079 -19 346 128 S ATOM 369 CE MET A 44 10.285 14.388 28.583 1.00 19.50 C ANISOU 369 CE MET A 44 2598 2153 2660 -36 334 111 C ATOM 370 N PHE A 45 12.115 9.042 28.795 1.00 18.16 N ANISOU 370 N PHE A 45 2456 1880 2565 -28 429 120 N ATOM 371 CA PHE A 45 11.665 7.879 29.556 1.00 22.45 C ANISOU 371 CA PHE A 45 3007 2400 3122 -33 446 122 C ATOM 372 C PHE A 45 12.262 7.883 30.957 1.00 24.67 C ANISOU 372 C PHE A 45 3286 2676 3412 -19 438 157 C ATOM 373 O PHE A 45 11.593 7.512 31.927 1.00 21.91 O ANISOU 373 O PHE A 45 2940 2321 3062 -23 440 163 O ATOM 374 CB PHE A 45 12.025 6.586 28.819 1.00 21.31 C ANISOU 374 CB PHE A 45 2870 2229 3000 -33 479 110 C ATOM 375 CG PHE A 45 11.390 5.350 29.410 1.00 27.10 C ANISOU 375 CG PHE A 45 3610 2934 3751 -42 502 106 C ATOM 376 CD1 PHE A 45 10.006 5.212 29.451 1.00 26.72 C ANISOU 376 CD1 PHE A 45 3565 2890 3697 -63 503 80 C ATOM 377 CD2 PHE A 45 12.174 4.317 29.899 1.00 21.82 C ANISOU 377 CD2 PHE A 45 2946 2234 3109 -30 526 129 C ATOM 378 CE1 PHE A 45 9.418 4.077 29.983 1.00 28.04 C ANISOU 378 CE1 PHE A 45 3738 3029 3887 -72 528 77 C ATOM 379 CE2 PHE A 45 11.594 3.179 30.426 1.00 23.05 C ANISOU 379 CE2 PHE A 45 3110 2363 3287 -37 552 128 C ATOM 380 CZ PHE A 45 10.214 3.056 30.473 1.00 25.61 C ANISOU 380 CZ PHE A 45 3435 2689 3607 -59 554 102 C ATOM 381 N LEU A 46 13.523 8.303 31.079 1.00 24.07 N ANISOU 381 N LEU A 46 3201 2602 3343 -1 429 180 N ATOM 382 CA LEU A 46 14.136 8.450 32.394 1.00 26.26 C ANISOU 382 CA LEU A 46 3473 2882 3624 15 415 210 C ATOM 383 C LEU A 46 13.363 9.445 33.251 1.00 20.22 C ANISOU 383 C LEU A 46 2705 2141 2837 10 387 209 C ATOM 384 O LEU A 46 13.064 9.175 34.420 1.00 27.26 O ANISOU 384 O LEU A 46 3599 3033 3724 15 384 224 O ATOM 385 CB LEU A 46 15.590 8.898 32.242 1.00 20.81 C ANISOU 385 CB LEU A 46 2769 2192 2945 33 406 228 C ATOM 386 CG LEU A 46 16.329 9.091 33.568 1.00 27.16 C ANISOU 386 CG LEU A 46 3563 3003 3752 52 388 256 C ATOM 387 CD1 LEU A 46 16.425 7.764 34.302 1.00 29.55 C ANISOU 387 CD1 LEU A 46 3876 3285 4066 63 410 275 C ATOM 388 CD2 LEU A 46 17.705 9.705 33.363 1.00 26.70 C ANISOU 388 CD2 LEU A 46 3488 2950 3708 66 375 269 C ATOM 389 N LEU A 47 13.023 10.602 32.682 1.00 17.68 N ANISOU 389 N LEU A 47 2376 1840 2501 1 368 194 N ATOM 390 CA LEU A 47 12.397 11.654 33.476 1.00 18.20 C ANISOU 390 CA LEU A 47 2438 1929 2548 -3 341 193 C ATOM 391 C LEU A 47 10.993 11.267 33.919 1.00 24.77 C ANISOU 391 C LEU A 47 3280 2763 3368 -17 347 181 C ATOM 392 O LEU A 47 10.566 11.651 35.015 1.00 20.87 O ANISOU 392 O LEU A 47 2787 2282 2863 -14 332 188 O ATOM 393 CB LEU A 47 12.370 12.966 32.690 1.00 18.24 C ANISOU 393 CB LEU A 47 2434 1953 2545 -8 323 180 C ATOM 394 CG LEU A 47 13.731 13.570 32.323 1.00 23.12 C ANISOU 394 CG LEU A 47 3038 2570 3178 5 317 193 C ATOM 395 CD1 LEU A 47 13.563 14.901 31.601 1.00 19.43 C ANISOU 395 CD1 LEU A 47 2561 2118 2703 0 303 184 C ATOM 396 CD2 LEU A 47 14.613 13.727 33.548 1.00 29.50 C ANISOU 396 CD2 LEU A 47 3834 3378 3995 21 300 214 C ATOM 397 N ILE A 48 10.260 10.519 33.091 1.00 23.41 N ANISOU 397 N ILE A 48 3116 2579 3199 -31 369 160 N ATOM 398 CA ILE A 48 8.932 10.053 33.483 1.00 21.31 C ANISOU 398 CA ILE A 48 2858 2312 2928 -46 378 147 C ATOM 399 C ILE A 48 9.036 9.020 34.598 1.00 19.60 C ANISOU 399 C ILE A 48 2649 2076 2724 -37 395 170 C ATOM 400 O ILE A 48 8.312 9.085 35.597 1.00 26.30 O ANISOU 400 O ILE A 48 3500 2932 3563 -38 391 177 O ATOM 401 CB ILE A 48 8.180 9.478 32.268 1.00 25.90 C ANISOU 401 CB ILE A 48 3442 2886 3512 -64 396 115 C ATOM 402 CG1 ILE A 48 8.015 10.537 31.180 1.00 17.71 C ANISOU 402 CG1 ILE A 48 2398 1873 2457 -68 379 96 C ATOM 403 CG2 ILE A 48 6.823 8.937 32.694 1.00 24.83 C ANISOU 403 CG2 ILE A 48 3311 2746 3376 -81 407 101 C ATOM 404 CD1 ILE A 48 7.468 9.980 29.890 1.00 26.16 C ANISOU 404 CD1 ILE A 48 3472 2942 3528 -81 395 63 C ATOM 405 N MET A 49 9.934 8.046 34.440 1.00 23.61 N ANISOU 405 N MET A 49 3159 2559 3252 -27 417 183 N ATOM 406 CA MET A 49 10.015 6.948 35.400 1.00 25.13 C ANISOU 406 CA MET A 49 3359 2730 3459 -17 439 207 C ATOM 407 C MET A 49 10.588 7.399 36.739 1.00 23.26 C ANISOU 407 C MET A 49 3119 2508 3209 6 419 239 C ATOM 408 O MET A 49 10.310 6.777 37.769 1.00 24.90 O ANISOU 408 O MET A 49 3334 2709 3419 16 432 260 O ATOM 409 CB MET A 49 10.844 5.808 34.814 1.00 21.09 C ANISOU 409 CB MET A 49 2852 2187 2976 -10 468 212 C ATOM 410 CG MET A 49 10.186 5.139 33.627 1.00 27.61 C ANISOU 410 CG MET A 49 3682 2996 3815 -32 492 178 C ATOM 411 SD MET A 49 8.627 4.358 34.072 1.00 27.30 S ANISOU 411 SD MET A 49 3648 2940 3785 -53 514 163 S ATOM 412 CE MET A 49 9.207 2.955 35.017 1.00 30.81 C ANISOU 412 CE MET A 49 4102 3347 4260 -34 551 201 C ATOM 413 N LEU A 50 11.394 8.462 36.742 1.00 22.48 N ANISOU 413 N LEU A 50 3010 2431 3100 16 389 243 N ATOM 414 CA LEU A 50 11.841 9.103 37.970 1.00 24.22 C ANISOU 414 CA LEU A 50 3224 2672 3306 36 364 264 C ATOM 415 C LEU A 50 10.844 10.138 38.458 1.00 24.93 C ANISOU 415 C LEU A 50 3313 2789 3372 26 340 251 C ATOM 416 O LEU A 50 10.600 10.241 39.665 1.00 22.40 O ANISOU 416 O LEU A 50 2995 2482 3036 38 332 266 O ATOM 417 CB LEU A 50 13.198 9.785 37.761 1.00 26.88 C ANISOU 417 CB LEU A 50 3546 3018 3648 50 342 271 C ATOM 418 CG LEU A 50 14.411 8.922 37.425 1.00 30.94 C ANISOU 418 CG LEU A 50 4058 3512 4186 65 360 288 C ATOM 419 CD1 LEU A 50 15.687 9.740 37.555 1.00 29.77 C ANISOU 419 CD1 LEU A 50 3891 3378 4042 81 333 297 C ATOM 420 CD2 LEU A 50 14.458 7.693 38.304 1.00 26.48 C ANISOU 420 CD2 LEU A 50 3503 2931 3627 82 383 315 C ATOM 421 N GLY A 51 10.268 10.906 37.531 1.00 23.54 N ANISOU 421 N GLY A 51 3133 2621 3190 7 332 224 N ATOM 422 CA GLY A 51 9.419 12.019 37.921 1.00 24.99 C ANISOU 422 CA GLY A 51 3313 2829 3352 -1 308 212 C ATOM 423 C GLY A 51 8.151 11.594 38.636 1.00 21.46 C ANISOU 423 C GLY A 51 2876 2383 2894 -8 320 211 C ATOM 424 O GLY A 51 7.744 12.228 39.611 1.00 24.47 O ANISOU 424 O GLY A 51 3256 2784 3256 -2 302 215 O ATOM 425 N PHE A 52 7.493 10.540 38.149 1.00 21.70 N ANISOU 425 N PHE A 52 2914 2392 2938 -22 350 203 N ATOM 426 CA PHE A 52 6.239 10.113 38.768 1.00 25.32 C ANISOU 426 CA PHE A 52 3380 2849 3392 -31 365 202 C ATOM 427 C PHE A 52 6.421 9.631 40.205 1.00 20.53 C ANISOU 427 C PHE A 52 2780 2242 2780 -10 372 234 C ATOM 428 O PHE A 52 5.680 10.102 41.083 1.00 22.29 O ANISOU 428 O PHE A 52 3004 2483 2983 -7 363 237 O ATOM 429 CB PHE A 52 5.563 9.061 37.877 1.00 26.23 C ANISOU 429 CB PHE A 52 3499 2938 3528 -52 397 183 C ATOM 430 CG PHE A 52 4.495 8.259 38.571 1.00 24.12 C ANISOU 430 CG PHE A 52 3239 2659 3269 -59 422 187 C ATOM 431 CD1 PHE A 52 3.409 8.882 39.167 1.00 24.68 C ANISOU 431 CD1 PHE A 52 3307 2748 3321 -66 412 182 C ATOM 432 CD2 PHE A 52 4.566 6.878 38.603 1.00 29.33 C ANISOU 432 CD2 PHE A 52 3904 3283 3955 -59 459 198 C ATOM 433 CE1 PHE A 52 2.429 8.148 39.793 1.00 24.76 C ANISOU 433 CE1 PHE A 52 3321 2745 3340 -73 439 187 C ATOM 434 CE2 PHE A 52 3.586 6.134 39.233 1.00 27.55 C ANISOU 434 CE2 PHE A 52 3682 3042 3742 -67 487 204 C ATOM 435 CZ PHE A 52 2.518 6.771 39.831 1.00 26.10 C ANISOU 435 CZ PHE A 52 3497 2880 3540 -73 477 199 C ATOM 436 N PRO A 53 7.372 8.744 40.529 1.00 23.32 N ANISOU 436 N PRO A 53 3137 2577 3146 9 388 260 N ATOM 437 CA PRO A 53 7.464 8.277 41.922 1.00 19.26 C ANISOU 437 CA PRO A 53 2630 2066 2622 33 396 293 C ATOM 438 C PRO A 53 7.917 9.338 42.911 1.00 23.77 C ANISOU 438 C PRO A 53 3196 2673 3164 54 359 303 C ATOM 439 O PRO A 53 7.356 9.423 44.010 1.00 24.13 O ANISOU 439 O PRO A 53 3246 2733 3188 66 358 316 O ATOM 440 CB PRO A 53 8.475 7.121 41.838 1.00 24.76 C ANISOU 440 CB PRO A 53 3329 2735 3342 49 420 317 C ATOM 441 CG PRO A 53 8.471 6.702 40.434 1.00 25.62 C ANISOU 441 CG PRO A 53 3438 2820 3477 27 436 292 C ATOM 442 CD PRO A 53 8.256 7.961 39.651 1.00 26.43 C ANISOU 442 CD PRO A 53 3531 2946 3566 10 405 261 C ATOM 443 N AILE A 54 8.914 10.153 42.561 0.53 22.26 N ANISOU 443 N AILE A 54 2993 2495 2971 60 330 296 N ATOM 444 N BILE A 54 8.933 10.133 42.566 0.48 22.27 N ANISOU 444 N BILE A 54 2994 2496 2973 60 330 296 N ATOM 445 CA AILE A 54 9.465 11.091 43.535 0.53 21.45 C ANISOU 445 CA AILE A 54 2882 2423 2844 81 295 302 C ATOM 446 CA BILE A 54 9.466 11.111 43.513 0.48 21.46 C ANISOU 446 CA BILE A 54 2883 2425 2846 81 294 302 C ATOM 447 C AILE A 54 8.462 12.198 43.852 0.53 22.13 C ANISOU 447 C AILE A 54 2966 2534 2908 70 274 281 C ATOM 448 C BILE A 54 8.406 12.145 43.862 0.48 22.22 C ANISOU 448 C BILE A 54 2979 2545 2920 69 276 282 C ATOM 449 O AILE A 54 8.362 12.649 45.000 0.53 20.49 O ANISOU 449 O AILE A 54 2759 2351 2676 87 257 289 O ATOM 450 O BILE A 54 8.214 12.491 45.035 0.48 20.48 O ANISOU 450 O BILE A 54 2760 2348 2675 87 262 291 O ATOM 451 CB AILE A 54 10.821 11.641 43.047 0.53 22.71 C ANISOU 451 CB AILE A 54 3026 2587 3015 88 272 298 C ATOM 452 CB BILE A 54 10.735 11.772 42.944 0.48 22.73 C ANISOU 452 CB BILE A 54 3028 2590 3017 85 270 294 C ATOM 453 CG1AILE A 54 11.579 12.294 44.205 0.53 24.07 C ANISOU 453 CG1AILE A 54 3189 2789 3168 115 239 308 C ATOM 454 CG1BILE A 54 11.779 10.713 42.588 0.48 23.69 C ANISOU 454 CG1BILE A 54 3150 2689 3163 97 290 314 C ATOM 455 CG2AILE A 54 10.655 12.619 41.887 0.53 22.60 C ANISOU 455 CG2AILE A 54 3004 2574 3009 64 258 268 C ATOM 456 CG2BILE A 54 11.309 12.772 43.938 0.48 24.09 C ANISOU 456 CG2BILE A 54 3188 2794 3169 105 232 295 C ATOM 457 CD1AILE A 54 12.920 12.854 43.805 0.53 22.78 C ANISOU 457 CD1AILE A 54 3006 2629 3019 122 216 303 C ATOM 458 CD1BILE A 54 13.023 11.285 41.937 0.48 20.60 C ANISOU 458 CD1BILE A 54 2742 2299 2786 100 271 308 C ATOM 459 N ASN A 55 7.696 12.647 42.852 1.00 20.34 N ANISOU 459 N ASN A 55 2738 2302 2689 42 276 255 N ATOM 460 CA ASN A 55 6.673 13.658 43.096 1.00 19.79 C ANISOU 460 CA ASN A 55 2666 2252 2599 32 259 236 C ATOM 461 C ASN A 55 5.454 13.068 43.801 1.00 21.76 C ANISOU 461 C ASN A 55 2927 2501 2838 29 281 243 C ATOM 462 O ASN A 55 4.876 13.710 44.687 1.00 17.57 O ANISOU 462 O ASN A 55 2398 1993 2285 36 268 242 O ATOM 463 CB ASN A 55 6.279 14.326 41.778 1.00 17.69 C ANISOU 463 CB ASN A 55 2395 1984 2344 7 254 208 C ATOM 464 CG ASN A 55 7.345 15.283 41.267 1.00 17.32 C ANISOU 464 CG ASN A 55 2333 1943 2303 10 228 200 C ATOM 465 OD1 ASN A 55 7.567 16.343 41.850 1.00 17.86 O ANISOU 465 OD1 ASN A 55 2394 2032 2361 19 200 195 O ATOM 466 ND2 ASN A 55 8.001 14.919 40.171 1.00 16.70 N ANISOU 466 ND2 ASN A 55 2253 1848 2246 5 239 199 N ATOM 467 N PHE A 56 5.050 11.847 43.436 1.00 20.98 N ANISOU 467 N PHE A 56 2837 2376 2759 20 317 251 N ATOM 468 CA PHE A 56 3.926 11.221 44.128 1.00 23.69 C ANISOU 468 CA PHE A 56 3189 2714 3098 18 343 260 C ATOM 469 C PHE A 56 4.252 10.948 45.591 1.00 21.36 C ANISOU 469 C PHE A 56 2901 2432 2782 49 345 294 C ATOM 470 O PHE A 56 3.383 11.070 46.461 1.00 19.05 O ANISOU 470 O PHE A 56 2614 2153 2472 54 350 300 O ATOM 471 CB PHE A 56 3.507 9.925 43.440 1.00 22.87 C ANISOU 471 CB PHE A 56 3090 2575 3025 1 383 260 C ATOM 472 CG PHE A 56 2.384 9.221 44.146 1.00 26.29 C ANISOU 472 CG PHE A 56 3530 2998 3460 -2 414 272 C ATOM 473 CD1 PHE A 56 1.075 9.625 43.957 1.00 28.28 C ANISOU 473 CD1 PHE A 56 3778 3257 3709 -24 415 249 C ATOM 474 CD2 PHE A 56 2.637 8.175 45.020 1.00 26.77 C ANISOU 474 CD2 PHE A 56 3601 3043 3527 19 443 308 C ATOM 475 CE1 PHE A 56 0.039 8.995 44.619 1.00 29.53 C ANISOU 475 CE1 PHE A 56 3940 3406 3873 -27 446 260 C ATOM 476 CE2 PHE A 56 1.601 7.539 45.678 1.00 30.76 C ANISOU 476 CE2 PHE A 56 4112 3538 4038 17 476 322 C ATOM 477 CZ PHE A 56 0.305 7.951 45.480 1.00 21.31 C ANISOU 477 CZ PHE A 56 2909 2347 2840 -7 477 297 C ATOM 478 N ALEU A 57 5.494 10.556 45.880 0.31 23.73 N ANISOU 478 N ALEU A 57 3201 2730 3084 73 341 316 N ATOM 479 N BLEU A 57 5.492 10.546 45.880 0.69 23.78 N ANISOU 479 N BLEU A 57 3208 2736 3091 73 341 316 N ATOM 480 CA ALEU A 57 5.882 10.311 47.265 0.31 21.41 C ANISOU 480 CA ALEU A 57 2914 2454 2768 108 340 348 C ATOM 481 CA BLEU A 57 5.882 10.314 47.266 0.69 21.44 C ANISOU 481 CA BLEU A 57 2918 2458 2771 108 340 348 C ATOM 482 C ALEU A 57 5.884 11.602 48.075 0.31 22.36 C ANISOU 482 C ALEU A 57 3028 2614 2852 121 300 336 C ATOM 483 C BLEU A 57 5.857 11.609 48.068 0.69 22.37 C ANISOU 483 C BLEU A 57 3030 2615 2854 120 300 336 C ATOM 484 O ALEU A 57 5.523 11.599 49.256 0.31 22.73 O ANISOU 484 O ALEU A 57 3083 2682 2873 143 301 353 O ATOM 485 O BLEU A 57 5.459 11.615 49.238 0.69 22.79 O ANISOU 485 O BLEU A 57 3090 2689 2879 142 302 352 O ATOM 486 CB ALEU A 57 7.250 9.632 47.313 0.31 23.11 C ANISOU 486 CB ALEU A 57 3129 2660 2994 131 342 372 C ATOM 487 CB BLEU A 57 7.269 9.675 47.329 0.69 23.14 C ANISOU 487 CB BLEU A 57 3131 2664 2996 132 341 371 C ATOM 488 CG ALEU A 57 7.258 8.174 46.843 0.31 23.19 C ANISOU 488 CG ALEU A 57 3146 2628 3036 127 388 391 C ATOM 489 CG BLEU A 57 7.718 9.285 48.741 0.69 21.42 C ANISOU 489 CG BLEU A 57 2920 2466 2753 173 342 408 C ATOM 490 CD1ALEU A 57 8.680 7.641 46.747 0.31 24.02 C ANISOU 490 CD1ALEU A 57 3249 2726 3154 149 387 411 C ATOM 491 CD1BLEU A 57 6.779 8.243 49.330 0.69 24.16 C ANISOU 491 CD1BLEU A 57 3282 2797 3102 178 386 436 C ATOM 492 CD2ALEU A 57 6.410 7.303 47.758 0.31 25.78 C ANISOU 492 CD2ALEU A 57 3488 2948 3359 138 425 420 C ATOM 493 CD2BLEU A 57 9.154 8.788 48.758 0.69 27.86 C ANISOU 493 CD2BLEU A 57 3731 3278 3578 198 337 429 C ATOM 494 N THR A 58 6.292 12.715 47.461 1.00 20.82 N ANISOU 494 N THR A 58 2820 2430 2659 109 266 308 N ATOM 495 CA THR A 58 6.249 14.000 48.153 1.00 20.79 C ANISOU 495 CA THR A 58 2810 2462 2628 118 229 291 C ATOM 496 C THR A 58 4.812 14.405 48.468 1.00 24.82 C ANISOU 496 C THR A 58 3326 2981 3123 106 236 280 C ATOM 497 O THR A 58 4.522 14.915 49.559 1.00 24.31 O ANISOU 497 O THR A 58 3264 2945 3029 124 222 282 O ATOM 498 CB THR A 58 6.952 15.066 47.308 1.00 20.76 C ANISOU 498 CB THR A 58 2789 2460 2637 105 198 264 C ATOM 499 OG1 THR A 58 8.342 14.736 47.189 1.00 23.95 O ANISOU 499 OG1 THR A 58 3186 2859 3054 120 190 276 O ATOM 500 CG2 THR A 58 6.828 16.438 47.938 1.00 20.58 C ANISOU 500 CG2 THR A 58 2758 2468 2593 110 162 243 C ATOM 501 N LEU A 59 3.894 14.174 47.529 1.00 21.83 N ANISOU 501 N LEU A 59 2949 2582 2764 76 257 267 N ATOM 502 CA LEU A 59 2.484 14.458 47.779 1.00 19.96 C ANISOU 502 CA LEU A 59 2717 2352 2517 63 267 256 C ATOM 503 C LEU A 59 1.934 13.568 48.889 1.00 22.55 C ANISOU 503 C LEU A 59 3057 2681 2831 81 296 286 C ATOM 504 O LEU A 59 1.257 14.041 49.810 1.00 25.43 O ANISOU 504 O LEU A 59 3425 3068 3169 92 291 287 O ATOM 505 CB LEU A 59 1.689 14.272 46.484 1.00 26.52 C ANISOU 505 CB LEU A 59 3544 3160 3373 29 283 236 C ATOM 506 CG LEU A 59 0.162 14.407 46.492 1.00 28.14 C ANISOU 506 CG LEU A 59 3749 3367 3575 11 298 223 C ATOM 507 CD1 LEU A 59 -0.312 14.896 45.143 1.00 34.92 C ANISOU 507 CD1 LEU A 59 4598 4220 4450 -18 291 192 C ATOM 508 CD2 LEU A 59 -0.522 13.088 46.837 1.00 31.65 C ANISOU 508 CD2 LEU A 59 4203 3791 4033 9 340 243 C ATOM 509 N TYR A 60 2.215 12.268 48.809 1.00 22.25 N ANISOU 509 N TYR A 60 3026 2616 2811 86 329 312 N ATOM 510 CA TYR A 60 1.682 11.320 49.781 1.00 26.09 C ANISOU 510 CA TYR A 60 3525 3098 3291 103 364 344 C ATOM 511 C TYR A 60 2.211 11.610 51.185 1.00 22.77 C ANISOU 511 C TYR A 60 3110 2711 2830 144 347 367 C ATOM 512 O TYR A 60 1.439 11.681 52.148 1.00 22.28 O ANISOU 512 O TYR A 60 3054 2666 2744 158 357 379 O ATOM 513 CB TYR A 60 2.031 9.897 49.337 1.00 23.33 C ANISOU 513 CB TYR A 60 3180 2709 2974 101 402 367 C ATOM 514 CG TYR A 60 1.316 8.798 50.082 1.00 25.73 C ANISOU 514 CG TYR A 60 3495 2997 3284 111 449 400 C ATOM 515 CD1 TYR A 60 1.763 8.373 51.326 1.00 33.91 C ANISOU 515 CD1 TYR A 60 4541 4046 4296 152 459 440 C ATOM 516 CD2 TYR A 60 0.206 8.166 49.536 1.00 28.57 C ANISOU 516 CD2 TYR A 60 3854 3326 3675 82 485 390 C ATOM 517 CE1 TYR A 60 1.120 7.363 52.012 1.00 30.65 C ANISOU 517 CE1 TYR A 60 4139 3617 3890 164 506 475 C ATOM 518 CE2 TYR A 60 -0.444 7.149 50.218 1.00 27.20 C ANISOU 518 CE2 TYR A 60 3689 3134 3514 91 532 422 C ATOM 519 CZ TYR A 60 0.020 6.755 51.456 1.00 31.58 C ANISOU 519 CZ TYR A 60 4254 3700 4043 132 544 466 C ATOM 520 OH TYR A 60 -0.615 5.750 52.146 1.00 32.29 O ANISOU 520 OH TYR A 60 4354 3770 4146 143 594 502 O ATOM 521 N VAL A 61 3.527 11.802 51.316 1.00 20.73 N ANISOU 521 N VAL A 61 2846 2465 2564 165 320 372 N ATOM 522 CA VAL A 61 4.121 12.049 52.629 1.00 20.29 C ANISOU 522 CA VAL A 61 2793 2446 2469 206 301 391 C ATOM 523 C VAL A 61 3.582 13.344 53.230 1.00 23.04 C ANISOU 523 C VAL A 61 3138 2830 2785 208 269 365 C ATOM 524 O VAL A 61 3.320 13.420 54.436 1.00 20.37 O ANISOU 524 O VAL A 61 2808 2522 2411 238 269 380 O ATOM 525 CB VAL A 61 5.662 12.064 52.536 1.00 27.47 C ANISOU 525 CB VAL A 61 3694 3362 3381 225 275 395 C ATOM 526 CG1 VAL A 61 6.280 12.521 53.859 1.00 23.05 C ANISOU 526 CG1 VAL A 61 3134 2848 2778 267 245 405 C ATOM 527 CG2 VAL A 61 6.196 10.686 52.167 1.00 20.62 C ANISOU 527 CG2 VAL A 61 2832 2461 2542 230 310 427 C ATOM 528 N THR A 62 3.413 14.383 52.407 1.00 21.70 N ANISOU 528 N THR A 62 2957 2660 2627 180 244 326 N ATOM 529 CA THR A 62 2.951 15.665 52.937 1.00 26.98 C ANISOU 529 CA THR A 62 3622 3361 3270 182 214 300 C ATOM 530 C THR A 62 1.536 15.561 53.499 1.00 26.46 C ANISOU 530 C THR A 62 3567 3300 3188 180 239 306 C ATOM 531 O THR A 62 1.253 16.071 54.590 1.00 29.78 O ANISOU 531 O THR A 62 3991 3753 3572 203 227 306 O ATOM 532 CB THR A 62 3.017 16.740 51.853 1.00 23.85 C ANISOU 532 CB THR A 62 3210 2957 2894 151 187 261 C ATOM 533 OG1 THR A 62 4.374 16.903 51.422 1.00 19.71 O ANISOU 533 OG1 THR A 62 2674 2429 2384 156 164 256 O ATOM 534 CG2 THR A 62 2.500 18.066 52.396 1.00 22.95 C ANISOU 534 CG2 THR A 62 3092 2872 2758 153 159 234 C ATOM 535 N VAL A 63 0.637 14.899 52.768 1.00 28.82 N ANISOU 535 N VAL A 63 3869 3568 3515 152 274 310 N ATOM 536 CA VAL A 63 -0.751 14.771 53.203 1.00 27.11 C ANISOU 536 CA VAL A 63 3658 3353 3290 147 301 314 C ATOM 537 C VAL A 63 -0.845 13.901 54.452 1.00 24.10 C ANISOU 537 C VAL A 63 3292 2981 2885 181 330 356 C ATOM 538 O VAL A 63 -1.655 14.164 55.350 1.00 27.98 O ANISOU 538 O VAL A 63 3789 3494 3350 195 338 361 O ATOM 539 CB VAL A 63 -1.609 14.214 52.050 1.00 27.94 C ANISOU 539 CB VAL A 63 3759 3421 3435 108 331 305 C ATOM 540 CG1 VAL A 63 -3.013 13.850 52.532 1.00 28.21 C ANISOU 540 CG1 VAL A 63 3798 3452 3467 103 365 315 C ATOM 541 CG2 VAL A 63 -1.670 15.211 50.900 1.00 30.65 C ANISOU 541 CG2 VAL A 63 4089 3763 3793 79 302 265 C ATOM 542 N GLN A 64 -0.013 12.859 54.534 1.00 22.98 N ANISOU 542 N GLN A 64 3155 2824 2752 198 347 387 N ATOM 543 CA GLN A 64 -0.105 11.901 55.635 1.00 29.20 C ANISOU 543 CA GLN A 64 3958 3617 3522 233 381 432 C ATOM 544 C GLN A 64 0.240 12.530 56.982 1.00 29.14 C ANISOU 544 C GLN A 64 3954 3658 3459 276 355 440 C ATOM 545 O GLN A 64 -0.439 12.272 57.982 1.00 29.51 O ANISOU 545 O GLN A 64 4012 3720 3479 299 379 465 O ATOM 546 CB GLN A 64 0.809 10.705 55.364 1.00 25.12 C ANISOU 546 CB GLN A 64 3444 3072 3029 243 403 464 C ATOM 547 CG GLN A 64 0.782 9.642 56.452 1.00 30.56 C ANISOU 547 CG GLN A 64 4148 3763 3703 282 442 516 C ATOM 548 CD GLN A 64 1.601 8.418 56.095 1.00 27.71 C ANISOU 548 CD GLN A 64 3789 3367 3371 289 469 547 C ATOM 549 OE1 GLN A 64 2.715 8.530 55.586 1.00 34.29 O ANISOU 549 OE1 GLN A 64 4615 4200 4212 290 442 538 O ATOM 550 NE2 GLN A 64 1.050 7.239 56.357 1.00 26.48 N ANISOU 550 NE2 GLN A 64 3644 3182 3236 295 525 585 N ATOM 551 N HIS A 65 1.296 13.343 57.039 1.00 32.50 N ANISOU 551 N HIS A 65 4372 4110 3868 288 306 419 N ATOM 552 CA HIS A 65 1.817 13.863 58.302 1.00 25.96 C ANISOU 552 CA HIS A 65 3545 3330 2988 331 278 424 C ATOM 553 C HIS A 65 1.288 15.273 58.530 1.00 23.61 C ANISOU 553 C HIS A 65 3242 3061 2669 322 243 381 C ATOM 554 O HIS A 65 1.728 16.223 57.875 1.00 24.45 O ANISOU 554 O HIS A 65 3333 3168 2789 302 206 342 O ATOM 555 CB HIS A 65 3.342 13.841 58.301 1.00 23.70 C ANISOU 555 CB HIS A 65 3250 3055 2699 352 246 425 C ATOM 556 CG HIS A 65 3.920 12.471 58.147 1.00 25.60 C ANISOU 556 CG HIS A 65 3498 3270 2959 365 279 468 C ATOM 557 ND1 HIS A 65 4.293 11.695 59.222 1.00 29.72 N ANISOU 557 ND1 HIS A 65 4030 3811 3450 412 295 512 N ATOM 558 CD2 HIS A 65 4.187 11.737 57.042 1.00 24.88 C ANISOU 558 CD2 HIS A 65 3404 3134 2916 338 300 474 C ATOM 559 CE1 HIS A 65 4.769 10.542 58.786 1.00 29.55 C ANISOU 559 CE1 HIS A 65 4012 3756 3458 414 326 544 C ATOM 560 NE2 HIS A 65 4.716 10.543 57.466 1.00 27.31 N ANISOU 560 NE2 HIS A 65 3720 3433 3224 369 329 520 N ATOM 561 N LYS A 66 0.358 15.409 59.481 1.00 25.21 N ANISOU 561 N LYS A 66 3454 3286 2838 340 258 390 N ATOM 562 CA LYS A 66 -0.319 16.683 59.697 1.00 24.70 C ANISOU 562 CA LYS A 66 3385 3246 2756 331 233 351 C ATOM 563 C LYS A 66 0.628 17.783 60.159 1.00 29.69 C ANISOU 563 C LYS A 66 4006 3915 3360 350 177 318 C ATOM 564 O LYS A 66 0.276 18.962 60.064 1.00 34.91 O ANISOU 564 O LYS A 66 4658 4587 4018 335 150 278 O ATOM 565 CB LYS A 66 -1.444 16.510 60.719 1.00 35.43 C ANISOU 565 CB LYS A 66 4758 4623 4081 352 263 372 C ATOM 566 N LYS A 67 1.816 17.425 60.652 1.00 30.00 N ANISOU 566 N LYS A 67 4045 3974 3382 383 160 333 N ATOM 567 CA LYS A 67 2.775 18.420 61.121 1.00 27.75 C ANISOU 567 CA LYS A 67 3745 3724 3073 402 105 299 C ATOM 568 C LYS A 67 3.381 19.243 59.989 1.00 27.31 C ANISOU 568 C LYS A 67 3669 3647 3060 365 74 259 C ATOM 569 O LYS A 67 3.943 20.311 60.251 1.00 22.54 O ANISOU 569 O LYS A 67 3051 3068 2446 370 30 220 O ATOM 570 CB LYS A 67 3.899 17.736 61.899 1.00 33.33 C ANISOU 570 CB LYS A 67 4453 4458 3751 447 96 327 C ATOM 571 CG LYS A 67 4.470 16.505 61.204 1.00 32.58 C ANISOU 571 CG LYS A 67 4360 4326 3690 441 124 365 C ATOM 572 CD LYS A 67 5.935 16.284 61.549 1.00 37.14 C ANISOU 572 CD LYS A 67 4928 4927 4257 473 95 373 C ATOM 573 CE LYS A 67 6.236 16.640 62.996 1.00 39.71 C ANISOU 573 CE LYS A 67 5255 5314 4520 525 67 371 C ATOM 574 NZ LYS A 67 7.688 16.485 63.315 1.00 50.78 N ANISOU 574 NZ LYS A 67 6643 6741 5911 557 33 373 N ATOM 575 N LEU A 68 3.302 18.767 58.747 1.00 27.65 N ANISOU 575 N LEU A 68 3710 3645 3150 329 95 266 N ATOM 576 CA LEU A 68 3.974 19.426 57.625 1.00 23.29 C ANISOU 576 CA LEU A 68 3139 3071 2638 298 70 235 C ATOM 577 C LEU A 68 3.052 20.481 57.010 1.00 30.31 C ANISOU 577 C LEU A 68 4023 3949 3544 264 64 200 C ATOM 578 O LEU A 68 2.518 20.328 55.911 1.00 32.83 O ANISOU 578 O LEU A 68 4341 4234 3897 230 85 200 O ATOM 579 CB LEU A 68 4.409 18.393 56.591 1.00 24.63 C ANISOU 579 CB LEU A 68 3309 3201 2847 280 95 260 C ATOM 580 CG LEU A 68 5.475 17.381 57.021 1.00 19.56 C ANISOU 580 CG LEU A 68 2670 2565 2197 312 100 294 C ATOM 581 CD1 LEU A 68 5.622 16.275 55.990 1.00 28.48 C ANISOU 581 CD1 LEU A 68 3804 3651 3368 292 135 320 C ATOM 582 CD2 LEU A 68 6.809 18.079 57.247 1.00 22.36 C ANISOU 582 CD2 LEU A 68 3005 2944 2548 328 52 271 C ATOM 583 N ARG A 69 2.891 21.590 57.736 1.00 30.10 N ANISOU 583 N ARG A 69 3991 3953 3492 275 35 169 N ATOM 584 CA ARG A 69 1.995 22.656 57.301 1.00 25.20 C ANISOU 584 CA ARG A 69 3366 3325 2884 248 29 137 C ATOM 585 C ARG A 69 2.653 24.032 57.377 1.00 28.58 C ANISOU 585 C ARG A 69 3774 3766 3317 247 -16 92 C ATOM 586 O ARG A 69 1.968 25.044 57.533 1.00 27.87 O ANISOU 586 O ARG A 69 3682 3685 3223 240 -26 63 O ATOM 587 CB ARG A 69 0.700 22.644 58.112 1.00 29.05 C ANISOU 587 CB ARG A 69 3868 3830 3339 259 51 144 C ATOM 588 CG ARG A 69 -0.097 21.354 58.005 1.00 31.72 C ANISOU 588 CG ARG A 69 4222 4149 3679 256 100 186 C ATOM 589 CD ARG A 69 -0.606 21.119 56.589 1.00 31.69 C ANISOU 589 CD ARG A 69 4214 4104 3722 214 121 185 C ATOM 590 NE ARG A 69 -1.373 19.881 56.488 1.00 31.09 N ANISOU 590 NE ARG A 69 4151 4008 3653 209 168 220 N ATOM 591 CZ ARG A 69 -0.878 18.719 56.082 1.00 30.54 C ANISOU 591 CZ ARG A 69 4085 3915 3603 208 190 249 C ATOM 592 NH1 ARG A 69 0.387 18.595 55.711 1.00 30.65 N ANISOU 592 NH1 ARG A 69 4092 3923 3629 212 170 249 N ATOM 593 NH2 ARG A 69 -1.674 17.655 56.041 1.00 32.60 N ANISOU 593 NH2 ARG A 69 4356 4156 3874 202 235 277 N ATOM 594 N THR A 70 3.976 24.097 57.259 1.00 22.75 N ANISOU 594 N THR A 70 3022 3030 2592 254 -42 85 N ATOM 595 CA THR A 70 4.632 25.386 57.130 1.00 23.02 C ANISOU 595 CA THR A 70 3034 3068 2643 246 -81 41 C ATOM 596 C THR A 70 4.398 25.940 55.728 1.00 26.88 C ANISOU 596 C THR A 70 3514 3518 3182 206 -74 29 C ATOM 597 O THR A 70 3.953 25.218 54.832 1.00 25.29 O ANISOU 597 O THR A 70 3321 3289 2998 187 -43 53 O ATOM 598 CB THR A 70 6.131 25.269 57.411 1.00 25.10 C ANISOU 598 CB THR A 70 3282 3346 2911 266 -111 37 C ATOM 599 OG1 THR A 70 6.751 24.448 56.415 1.00 29.05 O ANISOU 599 OG1 THR A 70 3780 3815 3444 251 -94 63 O ATOM 600 CG2 THR A 70 6.383 24.674 58.794 1.00 26.04 C ANISOU 600 CG2 THR A 70 3410 3508 2977 310 -118 52 C ATOM 601 N PRO A 71 4.650 27.236 55.521 1.00 27.83 N ANISOU 601 N PRO A 71 3616 3635 3323 194 -101 -10 N ATOM 602 CA PRO A 71 4.593 27.763 54.149 1.00 20.32 C ANISOU 602 CA PRO A 71 2655 2648 2419 160 -94 -18 C ATOM 603 C PRO A 71 5.494 27.011 53.181 1.00 25.13 C ANISOU 603 C PRO A 71 3258 3232 3058 150 -84 4 C ATOM 604 O PRO A 71 5.117 26.813 52.019 1.00 21.53 O ANISOU 604 O PRO A 71 2806 2748 2628 126 -62 16 O ATOM 605 CB PRO A 71 5.028 29.222 54.328 1.00 25.19 C ANISOU 605 CB PRO A 71 3251 3268 3054 157 -127 -62 C ATOM 606 CG PRO A 71 4.563 29.565 55.703 1.00 30.04 C ANISOU 606 CG PRO A 71 3871 3919 3624 182 -142 -80 C ATOM 607 CD PRO A 71 4.750 28.317 56.521 1.00 26.95 C ANISOU 607 CD PRO A 71 3495 3553 3193 211 -134 -49 C ATOM 608 N LEU A 72 6.675 26.579 53.631 1.00 22.03 N ANISOU 608 N LEU A 72 2858 2851 2662 169 -101 9 N ATOM 609 CA LEU A 72 7.543 25.775 52.775 1.00 22.44 C ANISOU 609 CA LEU A 72 2905 2880 2740 162 -90 33 C ATOM 610 C LEU A 72 6.882 24.451 52.410 1.00 21.64 C ANISOU 610 C LEU A 72 2826 2766 2630 159 -51 71 C ATOM 611 O LEU A 72 6.956 24.012 51.255 1.00 23.23 O ANISOU 611 O LEU A 72 3029 2938 2860 138 -31 84 O ATOM 612 CB LEU A 72 8.887 25.539 53.469 1.00 26.13 C ANISOU 612 CB LEU A 72 3359 3368 3202 188 -116 32 C ATOM 613 CG LEU A 72 9.946 24.674 52.771 1.00 20.72 C ANISOU 613 CG LEU A 72 2667 2663 2542 187 -107 56 C ATOM 614 CD1 LEU A 72 10.590 25.414 51.607 1.00 20.29 C ANISOU 614 CD1 LEU A 72 2592 2580 2538 161 -113 39 C ATOM 615 CD2 LEU A 72 11.002 24.225 53.779 1.00 26.39 C ANISOU 615 CD2 LEU A 72 3376 3411 3239 221 -130 61 C ATOM 616 N ASN A 73 6.223 23.802 53.377 1.00 22.05 N ANISOU 616 N ASN A 73 2896 2840 2643 179 -38 88 N ATOM 617 CA ASN A 73 5.583 22.518 53.095 1.00 23.52 C ANISOU 617 CA ASN A 73 3102 3010 2824 176 1 124 C ATOM 618 C ASN A 73 4.466 22.668 52.068 1.00 24.01 C ANISOU 618 C ASN A 73 3170 3048 2907 143 25 120 C ATOM 619 O ASN A 73 4.297 21.808 51.198 1.00 19.72 O ANISOU 619 O ASN A 73 2632 2478 2383 128 52 139 O ATOM 620 CB ASN A 73 5.031 21.892 54.375 1.00 22.77 C ANISOU 620 CB ASN A 73 3024 2942 2686 205 13 145 C ATOM 621 CG ASN A 73 6.093 21.674 55.428 1.00 26.07 C ANISOU 621 CG ASN A 73 3437 3390 3077 242 -10 151 C ATOM 622 OD1 ASN A 73 5.918 22.058 56.583 1.00 24.75 O ANISOU 622 OD1 ASN A 73 3272 3258 2872 268 -27 142 O ATOM 623 ND2 ASN A 73 7.199 21.056 55.039 1.00 24.13 N ANISOU 623 ND2 ASN A 73 3184 3133 2851 247 -12 167 N ATOM 624 N TYR A 74 3.671 23.738 52.176 1.00 26.67 N ANISOU 624 N TYR A 74 3503 3392 3238 134 14 94 N ATOM 625 CA TYR A 74 2.585 23.957 51.224 1.00 21.73 C ANISOU 625 CA TYR A 74 2880 2746 2629 106 34 89 C ATOM 626 C TYR A 74 3.113 24.190 49.818 1.00 24.63 C ANISOU 626 C TYR A 74 3236 3088 3036 83 33 83 C ATOM 627 O TYR A 74 2.572 23.651 48.845 1.00 20.93 O ANISOU 627 O TYR A 74 2772 2598 2581 64 57 93 O ATOM 628 CB TYR A 74 1.733 25.149 51.653 1.00 23.99 C ANISOU 628 CB TYR A 74 3163 3048 2903 104 20 63 C ATOM 629 CG TYR A 74 0.730 24.842 52.735 1.00 27.29 C ANISOU 629 CG TYR A 74 3596 3488 3285 120 34 71 C ATOM 630 CD1 TYR A 74 -0.416 24.116 52.456 1.00 27.49 C ANISOU 630 CD1 TYR A 74 3633 3503 3309 108 68 89 C ATOM 631 CD2 TYR A 74 0.916 25.301 54.030 1.00 25.41 C ANISOU 631 CD2 TYR A 74 3358 3281 3014 147 13 60 C ATOM 632 CE1 TYR A 74 -1.344 23.843 53.442 1.00 30.35 C ANISOU 632 CE1 TYR A 74 4007 3884 3640 122 83 98 C ATOM 633 CE2 TYR A 74 -0.003 25.033 55.020 1.00 33.15 C ANISOU 633 CE2 TYR A 74 4353 4283 3960 164 28 70 C ATOM 634 CZ TYR A 74 -1.133 24.305 54.722 1.00 34.01 C ANISOU 634 CZ TYR A 74 4474 4379 4070 151 64 90 C ATOM 635 OH TYR A 74 -2.051 24.036 55.713 1.00 35.66 O ANISOU 635 OH TYR A 74 4695 4607 4246 168 82 102 O ATOM 636 N AILE A 75 4.162 25.008 49.692 0.60 22.76 N ANISOU 636 N AILE A 75 2982 2850 2816 85 6 66 N ATOM 637 N BILE A 75 4.169 24.993 49.687 0.40 22.75 N ANISOU 637 N BILE A 75 2982 2849 2815 85 6 66 N ATOM 638 CA AILE A 75 4.708 25.329 48.377 0.60 21.64 C ANISOU 638 CA AILE A 75 2828 2682 2710 65 7 62 C ATOM 639 CA BILE A 75 4.684 25.316 48.361 0.40 21.65 C ANISOU 639 CA BILE A 75 2830 2683 2712 65 8 62 C ATOM 640 C AILE A 75 5.310 24.088 47.729 0.60 22.07 C ANISOU 640 C AILE A 75 2888 2720 2777 63 27 87 C ATOM 641 C BILE A 75 5.326 24.092 47.719 0.40 22.06 C ANISOU 641 C BILE A 75 2886 2718 2776 63 26 87 C ATOM 642 O AILE A 75 5.133 23.850 46.529 0.60 21.87 O ANISOU 642 O AILE A 75 2863 2673 2772 45 44 92 O ATOM 643 O BILE A 75 5.189 23.867 46.511 0.40 21.86 O ANISOU 643 O BILE A 75 2861 2671 2772 45 44 92 O ATOM 644 CB AILE A 75 5.733 26.471 48.492 0.60 21.61 C ANISOU 644 CB AILE A 75 2803 2681 2726 69 -24 38 C ATOM 645 CB BILE A 75 5.652 26.508 48.448 0.40 21.60 C ANISOU 645 CB BILE A 75 2803 2679 2726 68 -23 38 C ATOM 646 CG1AILE A 75 5.052 27.750 48.981 0.60 22.04 C ANISOU 646 CG1AILE A 75 2853 2747 2775 68 -40 10 C ATOM 647 CG1BILE A 75 4.888 27.744 48.927 0.40 22.05 C ANISOU 647 CG1BILE A 75 2856 2748 2776 66 -38 11 C ATOM 648 CG2AILE A 75 6.411 26.724 47.153 0.60 21.52 C ANISOU 648 CG2AILE A 75 2780 2643 2754 52 -20 39 C ATOM 649 CG2BILE A 75 6.318 26.766 47.104 0.40 21.51 C ANISOU 649 CG2BILE A 75 2779 2641 2753 51 -19 39 C ATOM 650 CD1AILE A 75 4.010 28.292 48.023 0.60 20.89 C ANISOU 650 CD1AILE A 75 2709 2586 2641 47 -25 6 C ATOM 651 CD1BILE A 75 5.601 29.041 48.688 0.40 21.49 C ANISOU 651 CD1BILE A 75 2763 2668 2735 61 -61 -16 C ATOM 652 N LEU A 76 6.021 23.272 48.510 1.00 22.06 N ANISOU 652 N LEU A 76 2890 2728 2763 84 24 104 N ATOM 653 CA LEU A 76 6.608 22.055 47.959 1.00 19.09 C ANISOU 653 CA LEU A 76 2520 2335 2400 84 45 129 C ATOM 654 C LEU A 76 5.529 21.063 47.538 1.00 21.71 C ANISOU 654 C LEU A 76 2869 2653 2728 72 81 145 C ATOM 655 O LEU A 76 5.671 20.386 46.511 1.00 22.73 O ANISOU 655 O LEU A 76 3000 2759 2878 59 101 154 O ATOM 656 CB LEU A 76 7.576 21.432 48.968 1.00 18.35 C ANISOU 656 CB LEU A 76 2425 2256 2291 113 35 145 C ATOM 657 CG LEU A 76 9.052 21.759 48.699 1.00 21.85 C ANISOU 657 CG LEU A 76 2848 2696 2758 119 13 138 C ATOM 658 CD1 LEU A 76 9.505 21.115 47.400 1.00 22.14 C ANISOU 658 CD1 LEU A 76 2884 2702 2826 103 35 152 C ATOM 659 CD2 LEU A 76 9.293 23.262 48.643 1.00 21.58 C ANISOU 659 CD2 LEU A 76 2794 2667 2738 111 -17 105 C ATOM 660 N LEU A 77 4.437 20.973 48.306 1.00 18.72 N ANISOU 660 N LEU A 77 2501 2287 2323 76 89 147 N ATOM 661 CA LEU A 77 3.294 20.167 47.880 1.00 18.19 C ANISOU 661 CA LEU A 77 2447 2207 2258 61 123 157 C ATOM 662 C LEU A 77 2.697 20.696 46.582 1.00 19.61 C ANISOU 662 C LEU A 77 2621 2373 2458 33 127 139 C ATOM 663 O LEU A 77 2.369 19.916 45.678 1.00 17.88 O ANISOU 663 O LEU A 77 2406 2134 2254 17 150 144 O ATOM 664 CB LEU A 77 2.232 20.131 48.982 1.00 24.61 C ANISOU 664 CB LEU A 77 3270 3038 3041 72 131 161 C ATOM 665 CG LEU A 77 0.890 19.453 48.666 1.00 20.49 C ANISOU 665 CG LEU A 77 2758 2505 2523 55 164 168 C ATOM 666 CD1 LEU A 77 1.091 18.013 48.251 1.00 20.29 C ANISOU 666 CD1 LEU A 77 2741 2455 2515 51 196 191 C ATOM 667 CD2 LEU A 77 -0.046 19.533 49.868 1.00 27.19 C ANISOU 667 CD2 LEU A 77 3614 3374 3341 69 171 173 C ATOM 668 N ASN A 78 2.553 22.020 46.466 1.00 20.00 N ANISOU 668 N ASN A 78 2660 2432 2508 28 104 116 N ATOM 669 CA ASN A 78 2.056 22.601 45.221 1.00 21.24 C ANISOU 669 CA ASN A 78 2810 2577 2682 6 107 101 C ATOM 670 C ASN A 78 2.976 22.262 44.052 1.00 21.26 C ANISOU 670 C ASN A 78 2808 2560 2710 -1 112 106 C ATOM 671 O ASN A 78 2.504 21.948 42.953 1.00 20.45 O ANISOU 671 O ASN A 78 2707 2446 2618 -18 128 104 O ATOM 672 CB ASN A 78 1.911 24.116 45.369 1.00 22.35 C ANISOU 672 CB ASN A 78 2941 2730 2822 7 82 80 C ATOM 673 CG ASN A 78 1.287 24.772 44.148 1.00 26.20 C ANISOU 673 CG ASN A 78 3421 3209 3323 -12 86 68 C ATOM 674 OD1 ASN A 78 0.352 24.240 43.549 1.00 26.41 O ANISOU 674 OD1 ASN A 78 3454 3232 3349 -25 106 70 O ATOM 675 ND2 ASN A 78 1.804 25.937 43.775 1.00 24.82 N ANISOU 675 ND2 ASN A 78 3234 3031 3165 -12 69 55 N ATOM 676 N LEU A 79 4.294 22.316 44.269 1.00 22.04 N ANISOU 676 N LEU A 79 2899 2657 2818 11 98 112 N ATOM 677 CA LEU A 79 5.234 21.988 43.198 1.00 18.73 C ANISOU 677 CA LEU A 79 2474 2218 2423 6 104 118 C ATOM 678 C LEU A 79 5.139 20.519 42.796 1.00 20.65 C ANISOU 678 C LEU A 79 2730 2447 2670 2 133 134 C ATOM 679 O LEU A 79 5.222 20.191 41.605 1.00 21.27 O ANISOU 679 O LEU A 79 2808 2510 2765 -11 147 134 O ATOM 680 CB LEU A 79 6.661 22.340 43.624 1.00 20.66 C ANISOU 680 CB LEU A 79 2706 2465 2679 21 83 120 C ATOM 681 CG LEU A 79 6.959 23.828 43.837 1.00 20.87 C ANISOU 681 CG LEU A 79 2716 2500 2714 22 55 99 C ATOM 682 CD1 LEU A 79 8.400 24.029 44.276 1.00 22.49 C ANISOU 682 CD1 LEU A 79 2906 2707 2933 36 35 99 C ATOM 683 CD2 LEU A 79 6.655 24.623 42.574 1.00 22.85 C ANISOU 683 CD2 LEU A 79 2961 2738 2984 5 61 90 C ATOM 684 N ALA A 80 4.965 19.617 43.769 1.00 20.36 N ANISOU 684 N ALA A 80 2704 2414 2618 14 143 150 N ATOM 685 CA ALA A 80 4.790 18.203 43.442 1.00 19.11 C ANISOU 685 CA ALA A 80 2557 2238 2468 9 174 166 C ATOM 686 C ALA A 80 3.548 17.976 42.586 1.00 21.05 C ANISOU 686 C ALA A 80 2806 2474 2716 -14 194 153 C ATOM 687 O ALA A 80 3.530 17.083 41.731 1.00 18.06 O ANISOU 687 O ALA A 80 2432 2077 2354 -24 216 155 O ATOM 688 CB ALA A 80 4.713 17.367 44.720 1.00 21.78 C ANISOU 688 CB ALA A 80 2906 2582 2789 28 185 187 C ATOM 689 N VAL A 81 2.492 18.758 42.814 1.00 23.23 N ANISOU 689 N VAL A 81 3081 2766 2979 -20 186 139 N ATOM 690 CA VAL A 81 1.272 18.601 42.025 1.00 21.40 C ANISOU 690 CA VAL A 81 2851 2530 2750 -41 202 125 C ATOM 691 C VAL A 81 1.489 19.094 40.599 1.00 20.47 C ANISOU 691 C VAL A 81 2724 2408 2646 -54 196 110 C ATOM 692 O VAL A 81 1.096 18.434 39.629 1.00 23.73 O ANISOU 692 O VAL A 81 3139 2810 3068 -68 214 103 O ATOM 693 CB VAL A 81 0.096 19.322 42.703 1.00 23.94 C ANISOU 693 CB VAL A 81 3172 2871 3054 -43 195 115 C ATOM 694 CG1 VAL A 81 -1.084 19.418 41.752 1.00 21.94 C ANISOU 694 CG1 VAL A 81 2914 2617 2804 -64 204 97 C ATOM 695 CG2 VAL A 81 -0.305 18.582 43.976 1.00 19.90 C ANISOU 695 CG2 VAL A 81 2669 2362 2528 -32 209 132 C ATOM 696 N ALA A 82 2.118 20.263 40.451 1.00 19.00 N ANISOU 696 N ALA A 82 2529 2229 2460 -48 173 105 N ATOM 697 CA ALA A 82 2.400 20.787 39.119 1.00 23.76 C ANISOU 697 CA ALA A 82 3124 2828 3075 -55 170 96 C ATOM 698 C ALA A 82 3.391 19.899 38.379 1.00 22.56 C ANISOU 698 C ALA A 82 2974 2658 2940 -54 184 105 C ATOM 699 O ALA A 82 3.284 19.723 37.159 1.00 19.25 O ANISOU 699 O ALA A 82 2554 2233 2526 -63 194 97 O ATOM 700 CB ALA A 82 2.922 22.221 39.213 1.00 21.35 C ANISOU 700 CB ALA A 82 2808 2531 2774 -48 146 92 C ATOM 701 N ASP A 83 4.369 19.336 39.099 1.00 20.15 N ANISOU 701 N ASP A 83 2672 2345 2640 -42 184 121 N ATOM 702 CA ASP A 83 5.297 18.396 38.477 1.00 20.49 C ANISOU 702 CA ASP A 83 2717 2370 2700 -40 199 131 C ATOM 703 C ASP A 83 4.559 17.185 37.914 1.00 21.55 C ANISOU 703 C ASP A 83 2860 2491 2836 -52 227 127 C ATOM 704 O ASP A 83 4.880 16.709 36.821 1.00 20.75 O ANISOU 704 O ASP A 83 2759 2378 2746 -58 240 122 O ATOM 705 CB ASP A 83 6.353 17.937 39.485 1.00 18.17 C ANISOU 705 CB ASP A 83 2424 2072 2409 -21 195 151 C ATOM 706 CG ASP A 83 7.346 19.026 39.858 1.00 17.51 C ANISOU 706 CG ASP A 83 2325 1997 2329 -10 168 151 C ATOM 707 OD1 ASP A 83 7.262 20.153 39.336 1.00 17.38 O ANISOU 707 OD1 ASP A 83 2299 1986 2317 -16 155 138 O ATOM 708 OD2 ASP A 83 8.228 18.742 40.696 1.00 21.88 O ANISOU 708 OD2 ASP A 83 2876 2552 2884 7 160 164 O ATOM 709 N LEU A 84 3.575 16.661 38.652 1.00 16.36 N ANISOU 709 N LEU A 84 2210 1835 2170 -57 237 127 N ATOM 710 CA LEU A 84 2.832 15.502 38.164 1.00 17.06 C ANISOU 710 CA LEU A 84 2306 1910 2268 -71 265 120 C ATOM 711 C LEU A 84 2.052 15.841 36.900 1.00 19.73 C ANISOU 711 C LEU A 84 2638 2254 2604 -88 265 94 C ATOM 712 O LEU A 84 1.979 15.028 35.968 1.00 16.36 O ANISOU 712 O LEU A 84 2212 1815 2189 -98 283 83 O ATOM 713 CB LEU A 84 1.903 14.975 39.263 1.00 17.77 C ANISOU 713 CB LEU A 84 2402 2000 2351 -72 277 127 C ATOM 714 CG LEU A 84 2.676 14.154 40.294 1.00 17.75 C ANISOU 714 CG LEU A 84 2407 1986 2352 -53 288 155 C ATOM 715 CD1 LEU A 84 1.892 13.965 41.597 1.00 20.99 C ANISOU 715 CD1 LEU A 84 2823 2404 2748 -46 296 168 C ATOM 716 CD2 LEU A 84 3.072 12.811 39.691 1.00 20.77 C ANISOU 716 CD2 LEU A 84 2794 2340 2758 -58 317 160 C ATOM 717 N PHE A 85 1.481 17.046 36.845 1.00 21.36 N ANISOU 717 N PHE A 85 2838 2481 2796 -89 245 84 N ATOM 718 CA PHE A 85 0.817 17.505 35.629 1.00 21.93 C ANISOU 718 CA PHE A 85 2904 2565 2864 -100 242 62 C ATOM 719 C PHE A 85 1.793 17.587 34.459 1.00 20.29 C ANISOU 719 C PHE A 85 2693 2352 2663 -96 243 62 C ATOM 720 O PHE A 85 1.429 17.273 33.321 1.00 23.21 O ANISOU 720 O PHE A 85 3062 2724 3033 -104 251 45 O ATOM 721 CB PHE A 85 0.158 18.864 35.870 1.00 21.04 C ANISOU 721 CB PHE A 85 2784 2474 2736 -99 221 57 C ATOM 722 CG PHE A 85 -1.248 18.775 36.387 1.00 23.85 C ANISOU 722 CG PHE A 85 3139 2840 3083 -109 225 46 C ATOM 723 CD1 PHE A 85 -2.297 18.497 35.528 1.00 25.43 C ANISOU 723 CD1 PHE A 85 3334 3048 3282 -123 233 24 C ATOM 724 CD2 PHE A 85 -1.524 18.981 37.728 1.00 25.54 C ANISOU 724 CD2 PHE A 85 3356 3058 3290 -103 221 56 C ATOM 725 CE1 PHE A 85 -3.599 18.415 35.999 1.00 26.53 C ANISOU 725 CE1 PHE A 85 3470 3195 3416 -133 237 14 C ATOM 726 CE2 PHE A 85 -2.822 18.901 38.203 1.00 26.70 C ANISOU 726 CE2 PHE A 85 3501 3214 3430 -111 227 48 C ATOM 727 CZ PHE A 85 -3.859 18.620 37.336 1.00 29.15 C ANISOU 727 CZ PHE A 85 3804 3528 3742 -127 236 27 C ATOM 728 N MET A 86 3.030 18.022 34.715 1.00 23.02 N ANISOU 728 N MET A 86 3038 2693 3017 -82 233 79 N ATOM 729 CA MET A 86 4.036 18.050 33.657 1.00 20.07 C ANISOU 729 CA MET A 86 2662 2312 2652 -77 237 82 C ATOM 730 C MET A 86 4.325 16.647 33.135 1.00 20.15 C ANISOU 730 C MET A 86 2679 2303 2674 -81 261 80 C ATOM 731 O MET A 86 4.449 16.441 31.922 1.00 20.48 O ANISOU 731 O MET A 86 2720 2345 2716 -83 270 68 O ATOM 732 CB MET A 86 5.329 18.705 34.157 1.00 20.87 C ANISOU 732 CB MET A 86 2757 2408 2764 -62 224 101 C ATOM 733 CG MET A 86 5.218 20.181 34.539 1.00 20.86 C ANISOU 733 CG MET A 86 2746 2422 2758 -58 201 101 C ATOM 734 SD MET A 86 6.772 20.872 35.189 1.00 25.03 S ANISOU 734 SD MET A 86 3263 2942 3305 -43 185 117 S ATOM 735 CE MET A 86 7.780 20.930 33.709 1.00 21.56 C ANISOU 735 CE MET A 86 2817 2491 2882 -39 198 123 C ATOM 736 N VAL A 87 4.424 15.667 34.037 1.00 19.83 N ANISOU 736 N VAL A 87 2645 2247 2642 -81 273 90 N ATOM 737 CA VAL A 87 4.864 14.327 33.652 1.00 18.66 C ANISOU 737 CA VAL A 87 2504 2077 2510 -82 297 90 C ATOM 738 C VAL A 87 3.810 13.630 32.799 1.00 24.58 C ANISOU 738 C VAL A 87 3255 2824 3259 -100 313 63 C ATOM 739 O VAL A 87 4.122 13.050 31.752 1.00 20.66 O ANISOU 739 O VAL A 87 2760 2320 2771 -102 327 51 O ATOM 740 CB VAL A 87 5.215 13.498 34.900 1.00 22.84 C ANISOU 740 CB VAL A 87 3039 2590 3049 -74 307 112 C ATOM 741 CG1 VAL A 87 5.169 12.009 34.586 1.00 25.21 C ANISOU 741 CG1 VAL A 87 3347 2864 3367 -81 338 109 C ATOM 742 CG2 VAL A 87 6.586 13.888 35.418 1.00 23.89 C ANISOU 742 CG2 VAL A 87 3169 2722 3187 -55 294 136 C ATOM 743 N PHE A 88 2.550 13.672 33.231 1.00 20.51 N ANISOU 743 N PHE A 88 2738 2318 2736 -112 312 51 N ATOM 744 CA PHE A 88 1.499 12.915 32.563 1.00 20.80 C ANISOU 744 CA PHE A 88 2774 2352 2778 -130 328 22 C ATOM 745 C PHE A 88 0.786 13.725 31.488 1.00 22.35 C ANISOU 745 C PHE A 88 2962 2575 2955 -135 313 -3 C ATOM 746 O PHE A 88 0.393 13.172 30.453 1.00 23.08 O ANISOU 746 O PHE A 88 3052 2669 3049 -145 322 -30 O ATOM 747 CB PHE A 88 0.489 12.403 33.597 1.00 22.38 C ANISOU 747 CB PHE A 88 2974 2545 2983 -140 338 23 C ATOM 748 CG PHE A 88 1.037 11.327 34.483 1.00 23.25 C ANISOU 748 CG PHE A 88 3094 2627 3113 -134 361 46 C ATOM 749 CD1 PHE A 88 1.482 10.136 33.941 1.00 26.44 C ANISOU 749 CD1 PHE A 88 3502 3004 3540 -138 386 41 C ATOM 750 CD2 PHE A 88 1.119 11.508 35.853 1.00 23.39 C ANISOU 750 CD2 PHE A 88 3115 2645 3125 -123 358 74 C ATOM 751 CE1 PHE A 88 1.991 9.141 34.746 1.00 30.96 C ANISOU 751 CE1 PHE A 88 4083 3550 4133 -130 409 65 C ATOM 752 CE2 PHE A 88 1.627 10.517 36.659 1.00 28.17 C ANISOU 752 CE2 PHE A 88 3729 3227 3747 -113 379 98 C ATOM 753 CZ PHE A 88 2.063 9.333 36.106 1.00 27.95 C ANISOU 753 CZ PHE A 88 3706 3171 3744 -117 405 95 C ATOM 754 N GLY A 89 0.599 15.023 31.718 1.00 22.00 N ANISOU 754 N GLY A 89 2913 2554 2894 -128 290 4 N ATOM 755 CA GLY A 89 -0.011 15.859 30.702 1.00 22.93 C ANISOU 755 CA GLY A 89 3022 2697 2992 -129 277 -14 C ATOM 756 C GLY A 89 0.931 16.181 29.557 1.00 22.59 C ANISOU 756 C GLY A 89 2979 2658 2944 -117 276 -12 C ATOM 757 O GLY A 89 0.525 16.168 28.391 1.00 25.22 O ANISOU 757 O GLY A 89 3309 3008 3266 -118 277 -33 O ATOM 758 N GLY A 90 2.189 16.492 29.867 1.00 19.17 N ANISOU 758 N GLY A 90 2550 2214 2521 -104 274 14 N ATOM 759 CA GLY A 90 3.122 16.919 28.841 1.00 19.95 C ANISOU 759 CA GLY A 90 2648 2316 2618 -91 274 20 C ATOM 760 C GLY A 90 4.189 15.934 28.399 1.00 23.04 C ANISOU 760 C GLY A 90 3044 2686 3024 -87 293 24 C ATOM 761 O GLY A 90 4.384 15.749 27.194 1.00 21.38 O ANISOU 761 O GLY A 90 2834 2481 2807 -83 302 12 O ATOM 762 N PHE A 91 4.869 15.281 29.352 1.00 18.68 N ANISOU 762 N PHE A 91 2497 2111 2492 -86 300 41 N ATOM 763 CA PHE A 91 6.026 14.449 29.025 1.00 21.14 C ANISOU 763 CA PHE A 91 2812 2400 2819 -78 318 50 C ATOM 764 C PHE A 91 5.645 13.171 28.289 1.00 18.82 C ANISOU 764 C PHE A 91 2524 2096 2531 -88 340 25 C ATOM 765 O PHE A 91 6.490 12.599 27.592 1.00 17.42 O ANISOU 765 O PHE A 91 2350 1905 2362 -81 355 26 O ATOM 766 CB PHE A 91 6.814 14.080 30.292 1.00 18.29 C ANISOU 766 CB PHE A 91 2453 2019 2476 -72 318 76 C ATOM 767 CG PHE A 91 7.648 15.200 30.849 1.00 16.37 C ANISOU 767 CG PHE A 91 2202 1783 2235 -59 299 98 C ATOM 768 CD1 PHE A 91 7.641 16.453 30.263 1.00 21.61 C ANISOU 768 CD1 PHE A 91 2858 2464 2889 -55 285 97 C ATOM 769 CD2 PHE A 91 8.452 14.991 31.958 1.00 24.78 C ANISOU 769 CD2 PHE A 91 3267 2837 3314 -50 295 120 C ATOM 770 CE1 PHE A 91 8.413 17.479 30.776 1.00 22.76 C ANISOU 770 CE1 PHE A 91 2994 2612 3043 -45 268 114 C ATOM 771 CE2 PHE A 91 9.225 16.012 32.480 1.00 20.82 C ANISOU 771 CE2 PHE A 91 2755 2341 2816 -39 275 135 C ATOM 772 CZ PHE A 91 9.204 17.257 31.889 1.00 21.25 C ANISOU 772 CZ PHE A 91 2800 2409 2864 -38 262 131 C ATOM 773 N THR A 92 4.408 12.698 28.446 1.00 24.62 N ANISOU 773 N THR A 92 3259 2832 3262 -104 343 3 N ATOM 774 CA THR A 92 3.969 11.531 27.688 1.00 20.22 C ANISOU 774 CA THR A 92 2704 2265 2712 -116 363 -27 C ATOM 775 C THR A 92 3.939 11.826 26.192 1.00 20.86 C ANISOU 775 C THR A 92 2783 2369 2775 -111 360 -50 C ATOM 776 O THR A 92 4.271 10.960 25.376 1.00 19.61 O ANISOU 776 O THR A 92 2629 2200 2624 -111 378 -68 O ATOM 777 CB THR A 92 2.596 11.069 28.180 1.00 20.36 C ANISOU 777 CB THR A 92 2719 2283 2734 -135 366 -48 C ATOM 778 OG1 THR A 92 1.650 12.146 28.074 1.00 19.12 O ANISOU 778 OG1 THR A 92 2554 2158 2553 -138 343 -58 O ATOM 779 CG2 THR A 92 2.683 10.604 29.626 1.00 24.47 C ANISOU 779 CG2 THR A 92 3245 2781 3273 -137 374 -23 C ATOM 780 N THR A 93 3.549 13.045 25.814 1.00 16.94 N ANISOU 780 N THR A 93 2280 1903 2253 -105 340 -50 N ATOM 781 CA THR A 93 3.581 13.428 24.404 1.00 23.63 C ANISOU 781 CA THR A 93 3126 2774 3078 -95 338 -66 C ATOM 782 C THR A 93 5.014 13.576 23.895 1.00 21.47 C ANISOU 782 C THR A 93 2856 2491 2809 -76 347 -43 C ATOM 783 O THR A 93 5.311 13.210 22.750 1.00 19.74 O ANISOU 783 O THR A 93 2640 2280 2581 -68 359 -59 O ATOM 784 CB THR A 93 2.787 14.722 24.200 1.00 22.39 C ANISOU 784 CB THR A 93 2961 2652 2895 -90 316 -66 C ATOM 785 OG1 THR A 93 1.385 14.439 24.281 1.00 22.63 O ANISOU 785 OG1 THR A 93 2985 2695 2918 -106 310 -96 O ATOM 786 CG2 THR A 93 3.089 15.348 22.855 1.00 22.28 C ANISOU 786 CG2 THR A 93 2946 2664 2856 -71 315 -68 C ATOM 787 N THR A 94 5.925 14.098 24.725 1.00 18.58 N ANISOU 787 N THR A 94 2490 2112 2458 -68 343 -8 N ATOM 788 CA THR A 94 7.314 14.226 24.290 1.00 20.97 C ANISOU 788 CA THR A 94 2794 2405 2771 -52 353 14 C ATOM 789 C THR A 94 7.915 12.863 23.964 1.00 19.97 C ANISOU 789 C THR A 94 2674 2253 2660 -52 377 4 C ATOM 790 O THR A 94 8.558 12.687 22.922 1.00 23.95 O ANISOU 790 O THR A 94 3180 2759 3159 -41 390 1 O ATOM 791 CB THR A 94 8.160 14.928 25.353 1.00 22.28 C ANISOU 791 CB THR A 94 2954 2558 2954 -45 343 48 C ATOM 792 OG1 THR A 94 7.493 16.109 25.807 1.00 23.03 O ANISOU 792 OG1 THR A 94 3042 2670 3036 -47 321 54 O ATOM 793 CG2 THR A 94 9.519 15.326 24.763 1.00 20.11 C ANISOU 793 CG2 THR A 94 2675 2277 2688 -27 351 70 C ATOM 794 N LEU A 95 7.702 11.880 24.842 1.00 17.99 N ANISOU 794 N LEU A 95 2428 1980 2430 -65 385 1 N ATOM 795 CA LEU A 95 8.266 10.553 24.623 1.00 21.06 C ANISOU 795 CA LEU A 95 2822 2340 2838 -66 410 -7 C ATOM 796 C LEU A 95 7.750 9.952 23.323 1.00 21.42 C ANISOU 796 C LEU A 95 2871 2396 2872 -70 422 -46 C ATOM 797 O LEU A 95 8.534 9.507 22.479 1.00 20.73 O ANISOU 797 O LEU A 95 2788 2302 2787 -59 438 -50 O ATOM 798 CB LEU A 95 7.942 9.637 25.808 1.00 17.97 C ANISOU 798 CB LEU A 95 2435 1923 2471 -78 418 -3 C ATOM 799 CG LEU A 95 8.406 8.178 25.701 1.00 17.60 C ANISOU 799 CG LEU A 95 2395 1842 2450 -80 448 -10 C ATOM 800 CD1 LEU A 95 9.909 8.090 25.594 1.00 17.62 C ANISOU 800 CD1 LEU A 95 2398 1830 2466 -60 457 18 C ATOM 801 CD2 LEU A 95 7.905 7.343 26.889 1.00 17.67 C ANISOU 801 CD2 LEU A 95 2406 1826 2481 -91 458 -3 C ATOM 802 N TYR A 96 6.426 9.953 23.137 1.00 21.27 N ANISOU 802 N TYR A 96 2849 2395 2837 -84 413 -77 N ATOM 803 CA TYR A 96 5.841 9.411 21.912 1.00 21.44 C ANISOU 803 CA TYR A 96 2871 2431 2845 -88 420 -121 C ATOM 804 C TYR A 96 6.351 10.152 20.682 1.00 22.05 C ANISOU 804 C TYR A 96 2948 2538 2893 -67 416 -120 C ATOM 805 O TYR A 96 6.725 9.529 19.681 1.00 22.83 O ANISOU 805 O TYR A 96 3050 2636 2986 -60 432 -141 O ATOM 806 CB TYR A 96 4.319 9.499 21.998 1.00 21.87 C ANISOU 806 CB TYR A 96 2917 2505 2887 -106 406 -152 C ATOM 807 CG TYR A 96 3.564 8.712 20.954 1.00 25.24 C ANISOU 807 CG TYR A 96 3340 2943 3305 -115 412 -205 C ATOM 808 CD1 TYR A 96 3.473 7.328 21.029 1.00 22.73 C ANISOU 808 CD1 TYR A 96 3024 2593 3018 -131 435 -231 C ATOM 809 CD2 TYR A 96 2.917 9.358 19.907 1.00 30.29 C ANISOU 809 CD2 TYR A 96 3974 3627 3908 -108 396 -230 C ATOM 810 CE1 TYR A 96 2.771 6.609 20.082 1.00 29.04 C ANISOU 810 CE1 TYR A 96 3819 3402 3813 -141 440 -285 C ATOM 811 CE2 TYR A 96 2.217 8.649 18.954 1.00 30.63 C ANISOU 811 CE2 TYR A 96 4012 3684 3942 -115 399 -283 C ATOM 812 CZ TYR A 96 2.147 7.276 19.045 1.00 31.74 C ANISOU 812 CZ TYR A 96 4154 3792 4115 -133 420 -312 C ATOM 813 OH TYR A 96 1.442 6.570 18.095 1.00 32.61 O ANISOU 813 OH TYR A 96 4257 3916 4218 -141 422 -370 O ATOM 814 N THR A 97 6.393 11.484 20.750 1.00 19.46 N ANISOU 814 N THR A 97 2615 2232 2546 -56 398 -94 N ATOM 815 CA THR A 97 6.888 12.280 19.631 1.00 23.66 C ANISOU 815 CA THR A 97 3148 2791 3052 -33 398 -86 C ATOM 816 C THR A 97 8.346 11.957 19.319 1.00 21.13 C ANISOU 816 C THR A 97 2832 2448 2747 -18 418 -65 C ATOM 817 O THR A 97 8.716 11.780 18.153 1.00 21.91 O ANISOU 817 O THR A 97 2935 2561 2830 -3 431 -76 O ATOM 818 CB THR A 97 6.724 13.767 19.945 1.00 21.63 C ANISOU 818 CB THR A 97 2883 2553 2782 -25 378 -58 C ATOM 819 OG1 THR A 97 5.337 14.062 20.187 1.00 18.41 O ANISOU 819 OG1 THR A 97 2470 2166 2358 -38 359 -78 O ATOM 820 CG2 THR A 97 7.253 14.628 18.793 1.00 22.17 C ANISOU 820 CG2 THR A 97 2951 2646 2825 1 382 -44 C ATOM 821 N ASER A 98 9.190 11.878 20.353 0.81 21.08 N ANISOU 821 N ASER A 98 2826 2412 2773 -20 422 -33 N ATOM 822 N BSER A 98 9.186 11.863 20.355 0.19 21.07 N ANISOU 822 N BSER A 98 2824 2410 2771 -20 422 -34 N ATOM 823 CA ASER A 98 10.608 11.599 20.151 0.81 21.30 C ANISOU 823 CA ASER A 98 2854 2418 2819 -5 441 -10 C ATOM 824 CA BSER A 98 10.605 11.594 20.140 0.19 21.28 C ANISOU 824 CA BSER A 98 2852 2416 2816 -5 441 -11 C ATOM 825 C ASER A 98 10.862 10.172 19.684 0.81 20.70 C ANISOU 825 C ASER A 98 2787 2322 2755 -8 465 -35 C ATOM 826 C BSER A 98 10.846 10.171 19.649 0.19 20.73 C ANISOU 826 C BSER A 98 2790 2327 2758 -7 465 -36 C ATOM 827 O ASER A 98 11.893 9.918 19.052 0.81 22.70 O ANISOU 827 O ASER A 98 3043 2568 3015 8 483 -26 O ATOM 828 O BSER A 98 11.844 9.916 18.964 0.19 21.78 O ANISOU 828 O BSER A 98 2926 2453 2895 8 483 -29 O ATOM 829 CB ASER A 98 11.378 11.875 21.443 0.81 20.62 C ANISOU 829 CB ASER A 98 2764 2308 2763 -6 434 27 C ATOM 830 CB BSER A 98 11.392 11.857 21.424 0.19 20.62 C ANISOU 830 CB BSER A 98 2764 2308 2763 -6 435 26 C ATOM 831 OG ASER A 98 11.381 13.263 21.738 0.81 17.97 O ANISOU 831 OG ASER A 98 2420 1990 2420 0 415 50 O ATOM 832 OG BSER A 98 10.923 11.048 22.489 0.19 20.55 O ANISOU 832 OG BSER A 98 2757 2279 2771 -22 434 20 O ATOM 833 N LEU A 99 9.960 9.234 19.994 1.00 23.08 N ANISOU 833 N LEU A 99 3092 2614 3064 -27 467 -66 N ATOM 834 CA LEU A 99 10.086 7.874 19.474 1.00 20.33 C ANISOU 834 CA LEU A 99 2750 2245 2730 -31 491 -96 C ATOM 835 C LEU A 99 9.902 7.844 17.962 1.00 25.00 C ANISOU 835 C LEU A 99 3345 2866 3290 -20 496 -130 C ATOM 836 O LEU A 99 10.623 7.129 17.253 1.00 21.68 O ANISOU 836 O LEU A 99 2929 2433 2875 -10 519 -140 O ATOM 837 CB LEU A 99 9.061 6.955 20.145 1.00 21.51 C ANISOU 837 CB LEU A 99 2900 2376 2897 -56 493 -123 C ATOM 838 CG LEU A 99 9.270 6.494 21.588 1.00 20.79 C ANISOU 838 CG LEU A 99 2809 2249 2840 -65 498 -95 C ATOM 839 CD1 LEU A 99 8.021 5.810 22.118 1.00 26.73 C ANISOU 839 CD1 LEU A 99 3560 2992 3605 -89 500 -123 C ATOM 840 CD2 LEU A 99 10.459 5.561 21.683 1.00 22.27 C ANISOU 840 CD2 LEU A 99 3002 2401 3058 -55 525 -80 C ATOM 841 N HIS A 100 8.935 8.608 17.453 1.00 23.00 N ANISOU 841 N HIS A 100 3086 2650 3001 -20 477 -148 N ATOM 842 CA HIS A 100 8.569 8.585 16.045 1.00 24.40 C ANISOU 842 CA HIS A 100 3265 2862 3142 -8 478 -183 C ATOM 843 C HIS A 100 9.300 9.622 15.206 1.00 25.93 C ANISOU 843 C HIS A 100 3460 3084 3308 21 479 -156 C ATOM 844 O HIS A 100 9.206 9.572 13.980 1.00 24.48 O ANISOU 844 O HIS A 100 3279 2930 3092 37 484 -180 O ATOM 845 CB HIS A 100 7.060 8.798 15.896 1.00 18.87 C ANISOU 845 CB HIS A 100 2557 2194 2418 -22 456 -220 C ATOM 846 CG HIS A 100 6.239 7.633 16.349 1.00 21.19 C ANISOU 846 CG HIS A 100 2849 2465 2738 -50 460 -260 C ATOM 847 ND1 HIS A 100 5.915 6.581 15.517 1.00 23.07 N ANISOU 847 ND1 HIS A 100 3088 2704 2975 -55 472 -312 N ATOM 848 CD2 HIS A 100 5.677 7.350 17.548 1.00 22.42 C ANISOU 848 CD2 HIS A 100 3000 2595 2922 -73 457 -254 C ATOM 849 CE1 HIS A 100 5.186 5.703 16.184 1.00 22.77 C ANISOU 849 CE1 HIS A 100 3045 2639 2968 -82 477 -338 C ATOM 850 NE2 HIS A 100 5.032 6.143 17.420 1.00 25.54 N ANISOU 850 NE2 HIS A 100 3393 2974 3336 -93 468 -302 N ATOM 851 N GLY A 101 10.014 10.559 15.823 1.00 21.87 N ANISOU 851 N GLY A 101 2942 2561 2805 29 475 -106 N ATOM 852 CA GLY A 101 10.720 11.576 15.071 1.00 18.54 C ANISOU 852 CA GLY A 101 2520 2161 2364 56 479 -76 C ATOM 853 C GLY A 101 9.895 12.767 14.625 1.00 22.09 C ANISOU 853 C GLY A 101 2964 2653 2776 66 460 -74 C ATOM 854 O GLY A 101 10.426 13.616 13.899 1.00 21.01 O ANISOU 854 O GLY A 101 2827 2534 2621 91 467 -48 O ATOM 855 N TYR A 102 8.624 12.860 15.022 1.00 21.87 N ANISOU 855 N TYR A 102 2932 2639 2738 49 438 -97 N ATOM 856 CA TYR A 102 7.791 14.017 14.694 1.00 24.76 C ANISOU 856 CA TYR A 102 3293 3044 3070 58 419 -92 C ATOM 857 C TYR A 102 6.500 13.953 15.506 1.00 25.01 C ANISOU 857 C TYR A 102 3318 3079 3104 33 397 -114 C ATOM 858 O TYR A 102 6.184 12.939 16.135 1.00 22.20 O ANISOU 858 O TYR A 102 2963 2700 2772 10 398 -138 O ATOM 859 CB TYR A 102 7.488 14.101 13.189 1.00 23.67 C ANISOU 859 CB TYR A 102 3158 2951 2885 83 423 -115 C ATOM 860 CG TYR A 102 6.457 13.113 12.684 1.00 21.41 C ANISOU 860 CG TYR A 102 2871 2684 2579 72 416 -175 C ATOM 861 CD1 TYR A 102 6.780 11.774 12.485 1.00 24.10 C ANISOU 861 CD1 TYR A 102 3218 3003 2936 62 432 -208 C ATOM 862 CD2 TYR A 102 5.163 13.527 12.397 1.00 24.71 C ANISOU 862 CD2 TYR A 102 3282 3142 2965 71 393 -200 C ATOM 863 CE1 TYR A 102 5.828 10.871 12.023 1.00 28.12 C ANISOU 863 CE1 TYR A 102 3724 3527 3432 49 426 -267 C ATOM 864 CE2 TYR A 102 4.209 12.641 11.943 1.00 26.46 C ANISOU 864 CE2 TYR A 102 3500 3382 3172 59 385 -258 C ATOM 865 CZ TYR A 102 4.544 11.316 11.749 1.00 26.57 C ANISOU 865 CZ TYR A 102 3519 3372 3205 48 402 -293 C ATOM 866 OH TYR A 102 3.583 10.445 11.290 1.00 19.85 O ANISOU 866 OH TYR A 102 2661 2537 2343 35 394 -356 O ATOM 867 N PHE A 103 5.753 15.061 15.476 1.00 18.96 N ANISOU 867 N PHE A 103 2545 2342 2315 40 378 -105 N ATOM 868 CA PHE A 103 4.494 15.197 16.212 1.00 23.85 C ANISOU 868 CA PHE A 103 3157 2969 2934 19 356 -122 C ATOM 869 C PHE A 103 3.391 14.443 15.473 1.00 22.69 C ANISOU 869 C PHE A 103 3007 2851 2763 13 349 -177 C ATOM 870 O PHE A 103 2.596 15.007 14.717 1.00 23.48 O ANISOU 870 O PHE A 103 3101 2994 2825 26 336 -191 O ATOM 871 CB PHE A 103 4.138 16.667 16.404 1.00 21.88 C ANISOU 871 CB PHE A 103 2901 2740 2671 31 340 -92 C ATOM 872 CG PHE A 103 4.721 17.275 17.654 1.00 23.23 C ANISOU 872 CG PHE A 103 3070 2879 2877 22 338 -53 C ATOM 873 CD1 PHE A 103 4.088 17.118 18.877 1.00 20.29 C ANISOU 873 CD1 PHE A 103 2695 2491 2525 -1 325 -58 C ATOM 874 CD2 PHE A 103 5.900 18.002 17.602 1.00 25.13 C ANISOU 874 CD2 PHE A 103 3311 3106 3129 39 349 -12 C ATOM 875 CE1 PHE A 103 4.621 17.669 20.027 1.00 24.79 C ANISOU 875 CE1 PHE A 103 3263 3035 3122 -7 321 -26 C ATOM 876 CE2 PHE A 103 6.434 18.561 18.741 1.00 20.25 C ANISOU 876 CE2 PHE A 103 2689 2461 2544 32 344 18 C ATOM 877 CZ PHE A 103 5.795 18.389 19.962 1.00 24.24 C ANISOU 877 CZ PHE A 103 3191 2953 3064 9 329 10 C ATOM 878 N VAL A 104 3.350 13.130 15.714 1.00 23.85 N ANISOU 878 N VAL A 104 3157 2972 2934 -8 359 -208 N ATOM 879 CA VAL A 104 2.292 12.284 15.167 1.00 21.15 C ANISOU 879 CA VAL A 104 2808 2650 2579 -20 353 -266 C ATOM 880 C VAL A 104 0.919 12.798 15.588 1.00 27.02 C ANISOU 880 C VAL A 104 3539 3416 3313 -33 329 -280 C ATOM 881 O VAL A 104 -0.045 12.743 14.815 1.00 29.67 O ANISOU 881 O VAL A 104 3865 3790 3618 -30 315 -320 O ATOM 882 CB VAL A 104 2.512 10.825 15.608 1.00 22.78 C ANISOU 882 CB VAL A 104 3018 2812 2824 -44 371 -292 C ATOM 883 CG1 VAL A 104 1.416 9.916 15.064 1.00 23.75 C ANISOU 883 CG1 VAL A 104 3131 2950 2941 -60 366 -356 C ATOM 884 CG2 VAL A 104 3.884 10.345 15.165 1.00 27.67 C ANISOU 884 CG2 VAL A 104 3649 3410 3454 -29 396 -277 C ATOM 885 N PHE A 105 0.810 13.310 16.816 1.00 24.58 N ANISOU 885 N PHE A 105 3228 3086 3027 -46 322 -248 N ATOM 886 CA PHE A 105 -0.434 13.875 17.332 1.00 24.77 C ANISOU 886 CA PHE A 105 3240 3128 3044 -57 301 -255 C ATOM 887 C PHE A 105 -0.718 15.269 16.778 1.00 22.51 C ANISOU 887 C PHE A 105 2949 2884 2720 -31 285 -235 C ATOM 888 O PHE A 105 -1.786 15.827 17.052 1.00 26.54 O ANISOU 888 O PHE A 105 3448 3416 3219 -36 266 -242 O ATOM 889 CB PHE A 105 -0.376 13.913 18.868 1.00 29.23 C ANISOU 889 CB PHE A 105 3806 3655 3645 -76 302 -228 C ATOM 890 CG PHE A 105 -1.715 13.762 19.556 1.00 31.40 C ANISOU 890 CG PHE A 105 4069 3934 3929 -99 290 -251 C ATOM 891 CD1 PHE A 105 -2.907 13.984 18.885 1.00 35.45 C ANISOU 891 CD1 PHE A 105 4568 4488 4415 -99 273 -285 C ATOM 892 CD2 PHE A 105 -1.772 13.398 20.892 1.00 33.20 C ANISOU 892 CD2 PHE A 105 4298 4125 4191 -120 296 -236 C ATOM 893 CE1 PHE A 105 -4.124 13.854 19.534 1.00 33.45 C ANISOU 893 CE1 PHE A 105 4302 4237 4172 -120 263 -306 C ATOM 894 CE2 PHE A 105 -2.982 13.261 21.540 1.00 31.42 C ANISOU 894 CE2 PHE A 105 4061 3903 3975 -140 288 -255 C ATOM 895 CZ PHE A 105 -4.159 13.490 20.859 1.00 34.73 C ANISOU 895 CZ PHE A 105 4465 4360 4370 -141 272 -290 C ATOM 896 N GLY A 106 0.212 15.856 16.033 1.00 24.19 N ANISOU 896 N GLY A 106 3170 3108 2914 -4 293 -208 N ATOM 897 CA GLY A 106 -0.044 17.091 15.327 1.00 24.45 C ANISOU 897 CA GLY A 106 3198 3181 2909 24 283 -189 C ATOM 898 C GLY A 106 -0.032 18.314 16.222 1.00 21.26 C ANISOU 898 C GLY A 106 2793 2768 2519 26 275 -145 C ATOM 899 O GLY A 106 0.602 18.333 17.280 1.00 25.49 O ANISOU 899 O GLY A 106 3332 3264 3090 12 280 -120 O ATOM 900 N PRO A 107 -0.720 19.377 15.790 1.00 24.00 N ANISOU 900 N PRO A 107 3132 3151 2835 45 261 -136 N ATOM 901 CA PRO A 107 -0.766 20.604 16.606 1.00 20.09 C ANISOU 901 CA PRO A 107 2633 2646 2353 47 254 -97 C ATOM 902 C PRO A 107 -1.364 20.404 17.989 1.00 23.72 C ANISOU 902 C PRO A 107 3089 3082 2843 17 243 -104 C ATOM 903 O PRO A 107 -0.947 21.090 18.931 1.00 26.65 O ANISOU 903 O PRO A 107 3461 3428 3238 13 243 -72 O ATOM 904 CB PRO A 107 -1.617 21.558 15.752 1.00 21.22 C ANISOU 904 CB PRO A 107 2768 2839 2456 73 242 -95 C ATOM 905 CG PRO A 107 -1.435 21.064 14.338 1.00 22.24 C ANISOU 905 CG PRO A 107 2901 3000 2548 96 250 -115 C ATOM 906 CD PRO A 107 -1.311 19.568 14.451 1.00 22.84 C ANISOU 906 CD PRO A 107 2981 3057 2641 70 255 -156 C ATOM 907 N THR A 108 -2.336 19.498 18.142 1.00 21.85 N ANISOU 907 N THR A 108 2845 2852 2606 -4 235 -146 N ATOM 908 CA THR A 108 -2.861 19.193 19.472 1.00 21.02 C ANISOU 908 CA THR A 108 2736 2720 2530 -33 230 -151 C ATOM 909 C THR A 108 -1.764 18.657 20.384 1.00 20.60 C ANISOU 909 C THR A 108 2694 2620 2514 -45 245 -131 C ATOM 910 O THR A 108 -1.699 19.015 21.567 1.00 23.81 O ANISOU 910 O THR A 108 3100 3004 2941 -55 241 -110 O ATOM 911 CB THR A 108 -4.009 18.184 19.376 1.00 24.38 C ANISOU 911 CB THR A 108 3152 3158 2954 -53 224 -201 C ATOM 912 OG1 THR A 108 -5.124 18.781 18.702 1.00 21.55 O ANISOU 912 OG1 THR A 108 2780 2846 2562 -42 206 -219 O ATOM 913 CG2 THR A 108 -4.448 17.722 20.771 1.00 27.24 C ANISOU 913 CG2 THR A 108 3511 3488 3350 -82 225 -203 C ATOM 914 N GLY A 109 -0.894 17.795 19.853 1.00 21.81 N ANISOU 914 N GLY A 109 2855 2759 2672 -43 261 -137 N ATOM 915 CA GLY A 109 0.205 17.278 20.652 1.00 22.86 C ANISOU 915 CA GLY A 109 2998 2849 2839 -52 275 -116 C ATOM 916 C GLY A 109 1.209 18.350 21.030 1.00 19.47 C ANISOU 916 C GLY A 109 2572 2408 2419 -37 276 -71 C ATOM 917 O GLY A 109 1.785 18.317 22.119 1.00 22.21 O ANISOU 917 O GLY A 109 2922 2725 2794 -45 278 -50 O ATOM 918 N CYS A 110 1.439 19.305 20.129 1.00 22.98 N ANISOU 918 N CYS A 110 3015 2876 2841 -13 275 -55 N ATOM 919 CA CYS A 110 2.318 20.430 20.425 1.00 20.74 C ANISOU 919 CA CYS A 110 2730 2580 2569 1 277 -13 C ATOM 920 C CYS A 110 1.733 21.313 21.523 1.00 21.88 C ANISOU 920 C CYS A 110 2868 2721 2724 -7 260 -1 C ATOM 921 O CYS A 110 2.466 21.799 22.394 1.00 21.78 O ANISOU 921 O CYS A 110 2855 2684 2737 -9 260 24 O ATOM 922 CB CYS A 110 2.561 21.225 19.142 1.00 25.67 C ANISOU 922 CB CYS A 110 3354 3231 3167 30 283 1 C ATOM 923 SG CYS A 110 3.736 22.598 19.227 1.00 20.02 S ANISOU 923 SG CYS A 110 2636 2499 2472 50 293 52 S ATOM 924 N ASN A 111 0.414 21.532 21.496 1.00 25.66 N ANISOU 924 N ASN A 111 3341 3226 3184 -12 246 -21 N ATOM 925 CA ASN A 111 -0.231 22.316 22.544 1.00 20.52 C ANISOU 925 CA ASN A 111 2683 2572 2540 -19 232 -12 C ATOM 926 C ASN A 111 -0.115 21.630 23.900 1.00 21.71 C ANISOU 926 C ASN A 111 2837 2692 2718 -42 231 -15 C ATOM 927 O ASN A 111 0.133 22.290 24.914 1.00 19.56 O ANISOU 927 O ASN A 111 2564 2405 2463 -44 224 5 O ATOM 928 CB ASN A 111 -1.703 22.571 22.196 1.00 17.27 C ANISOU 928 CB ASN A 111 2263 2195 2102 -19 218 -35 C ATOM 929 CG ASN A 111 -1.881 23.664 21.146 1.00 25.29 C ANISOU 929 CG ASN A 111 3275 3243 3092 8 216 -20 C ATOM 930 OD1 ASN A 111 -0.964 24.438 20.878 1.00 24.36 O ANISOU 930 OD1 ASN A 111 3160 3116 2981 26 225 11 O ATOM 931 ND2 ASN A 111 -3.069 23.733 20.555 1.00 22.41 N ANISOU 931 ND2 ASN A 111 2902 2915 2699 13 205 -43 N ATOM 932 N LEU A 112 -0.300 20.308 23.946 1.00 19.04 N ANISOU 932 N LEU A 112 2504 2346 2385 -57 238 -39 N ATOM 933 CA LEU A 112 -0.137 19.596 25.213 1.00 22.09 C ANISOU 933 CA LEU A 112 2894 2703 2797 -75 242 -37 C ATOM 934 C LEU A 112 1.302 19.671 25.703 1.00 22.98 C ANISOU 934 C LEU A 112 3012 2787 2931 -68 248 -8 C ATOM 935 O LEU A 112 1.554 19.914 26.891 1.00 22.05 O ANISOU 935 O LEU A 112 2894 2653 2829 -73 243 8 O ATOM 936 CB LEU A 112 -0.571 18.135 25.064 1.00 20.76 C ANISOU 936 CB LEU A 112 2727 2526 2633 -92 253 -67 C ATOM 937 CG LEU A 112 -2.034 17.805 24.768 1.00 21.46 C ANISOU 937 CG LEU A 112 2808 2638 2709 -104 247 -102 C ATOM 938 CD1 LEU A 112 -2.137 16.390 24.209 1.00 26.71 C ANISOU 938 CD1 LEU A 112 3473 3293 3381 -117 262 -135 C ATOM 939 CD2 LEU A 112 -2.895 17.940 26.016 1.00 21.46 C ANISOU 939 CD2 LEU A 112 2803 2632 2719 -119 240 -101 C ATOM 940 N GLU A 113 2.265 19.477 24.799 1.00 20.20 N ANISOU 940 N GLU A 113 2664 2432 2580 -56 260 -1 N ATOM 941 CA GLU A 113 3.667 19.462 25.206 1.00 19.76 C ANISOU 941 CA GLU A 113 2611 2350 2548 -50 268 24 C ATOM 942 C GLU A 113 4.096 20.813 25.766 1.00 22.50 C ANISOU 942 C GLU A 113 2951 2695 2904 -41 256 50 C ATOM 943 O GLU A 113 4.781 20.882 26.796 1.00 24.17 O ANISOU 943 O GLU A 113 3162 2886 3137 -44 252 66 O ATOM 944 CB GLU A 113 4.541 19.061 24.017 1.00 23.77 C ANISOU 944 CB GLU A 113 3122 2856 3053 -37 285 26 C ATOM 945 CG GLU A 113 5.803 18.298 24.383 1.00 25.37 C ANISOU 945 CG GLU A 113 3330 3029 3282 -37 298 39 C ATOM 946 CD GLU A 113 6.904 19.191 24.931 1.00 25.90 C ANISOU 946 CD GLU A 113 3390 3081 3369 -27 294 71 C ATOM 947 OE1 GLU A 113 6.990 20.364 24.515 1.00 24.25 O ANISOU 947 OE1 GLU A 113 3174 2884 3154 -16 289 85 O ATOM 948 OE2 GLU A 113 7.681 18.717 25.785 1.00 26.61 O ANISOU 948 OE2 GLU A 113 3481 3149 3482 -30 296 83 O ATOM 949 N GLY A 114 3.687 21.897 25.116 1.00 22.10 N ANISOU 949 N GLY A 114 2894 2665 2837 -30 251 55 N ATOM 950 CA GLY A 114 4.119 23.223 25.500 1.00 18.71 C ANISOU 950 CA GLY A 114 2457 2230 2420 -21 243 79 C ATOM 951 C GLY A 114 3.355 23.815 26.663 1.00 19.85 C ANISOU 951 C GLY A 114 2598 2376 2568 -30 226 76 C ATOM 952 O GLY A 114 3.959 24.438 27.541 1.00 20.37 O ANISOU 952 O GLY A 114 2658 2426 2654 -29 218 90 O ATOM 953 N PHE A 115 2.032 23.620 26.686 1.00 19.57 N ANISOU 953 N PHE A 115 2563 2360 2512 -38 219 56 N ATOM 954 CA PHE A 115 1.202 24.214 27.733 1.00 21.16 C ANISOU 954 CA PHE A 115 2760 2565 2713 -45 204 52 C ATOM 955 C PHE A 115 1.616 23.733 29.120 1.00 23.23 C ANISOU 955 C PHE A 115 3026 2806 2993 -56 199 56 C ATOM 956 O PHE A 115 1.773 24.537 30.046 1.00 16.94 O ANISOU 956 O PHE A 115 2225 2004 2207 -54 188 64 O ATOM 957 CB PHE A 115 -0.275 23.893 27.487 1.00 22.55 C ANISOU 957 CB PHE A 115 2936 2766 2867 -53 200 29 C ATOM 958 CG PHE A 115 -1.176 24.274 28.632 1.00 21.35 C ANISOU 958 CG PHE A 115 2780 2616 2715 -62 187 24 C ATOM 959 CD1 PHE A 115 -1.557 25.590 28.820 1.00 20.59 C ANISOU 959 CD1 PHE A 115 2677 2529 2617 -53 177 33 C ATOM 960 CD2 PHE A 115 -1.636 23.317 29.520 1.00 24.35 C ANISOU 960 CD2 PHE A 115 3164 2988 3099 -78 189 12 C ATOM 961 CE1 PHE A 115 -2.376 25.945 29.873 1.00 25.22 C ANISOU 961 CE1 PHE A 115 3261 3118 3203 -60 166 27 C ATOM 962 CE2 PHE A 115 -2.459 23.667 30.573 1.00 16.45 C ANISOU 962 CE2 PHE A 115 2162 1992 2098 -84 180 8 C ATOM 963 CZ PHE A 115 -2.829 24.983 30.747 1.00 15.72 C ANISOU 963 CZ PHE A 115 2062 1910 2001 -75 168 15 C ATOM 964 N PHE A 116 1.787 22.421 29.290 1.00 23.45 N ANISOU 964 N PHE A 116 3061 2823 3024 -65 209 48 N ATOM 965 CA PHE A 116 2.050 21.909 30.631 1.00 20.64 C ANISOU 965 CA PHE A 116 2710 2452 2682 -72 206 52 C ATOM 966 C PHE A 116 3.475 22.200 31.083 1.00 22.71 C ANISOU 966 C PHE A 116 2969 2695 2964 -62 204 73 C ATOM 967 O PHE A 116 3.735 22.269 32.290 1.00 23.18 O ANISOU 967 O PHE A 116 3028 2747 3031 -62 194 79 O ATOM 968 CB PHE A 116 1.751 20.413 30.696 1.00 20.92 C ANISOU 968 CB PHE A 116 2753 2479 2718 -83 220 40 C ATOM 969 CG PHE A 116 0.284 20.102 30.804 1.00 22.95 C ANISOU 969 CG PHE A 116 3010 2750 2962 -96 220 19 C ATOM 970 CD1 PHE A 116 -0.412 20.402 31.963 1.00 21.54 C ANISOU 970 CD1 PHE A 116 2829 2573 2781 -101 212 21 C ATOM 971 CD2 PHE A 116 -0.398 19.525 29.748 1.00 22.12 C ANISOU 971 CD2 PHE A 116 2903 2656 2848 -103 229 -3 C ATOM 972 CE1 PHE A 116 -1.765 20.123 32.067 1.00 25.97 C ANISOU 972 CE1 PHE A 116 3388 3147 3334 -112 214 2 C ATOM 973 CE2 PHE A 116 -1.744 19.245 29.845 1.00 25.72 C ANISOU 973 CE2 PHE A 116 3354 3124 3295 -115 228 -24 C ATOM 974 CZ PHE A 116 -2.430 19.544 31.008 1.00 25.07 C ANISOU 974 CZ PHE A 116 3270 3042 3213 -121 221 -20 C ATOM 975 N ALA A 117 4.407 22.370 30.145 1.00 20.98 N ANISOU 975 N ALA A 117 2748 2471 2754 -53 212 82 N ATOM 976 CA ALA A 117 5.760 22.769 30.518 1.00 19.81 C ANISOU 976 CA ALA A 117 2593 2306 2628 -45 209 100 C ATOM 977 C ALA A 117 5.825 24.246 30.890 1.00 21.13 C ANISOU 977 C ALA A 117 2749 2476 2804 -39 194 107 C ATOM 978 O ALA A 117 6.513 24.620 31.849 1.00 22.70 O ANISOU 978 O ALA A 117 2940 2665 3020 -37 182 113 O ATOM 979 CB ALA A 117 6.730 22.456 29.377 1.00 23.85 C ANISOU 979 CB ALA A 117 3104 2810 3149 -36 225 109 C ATOM 980 N THR A 118 5.120 25.097 30.138 1.00 20.83 N ANISOU 980 N THR A 118 2707 2452 2755 -36 194 105 N ATOM 981 CA THR A 118 5.084 26.523 30.449 1.00 17.86 C ANISOU 981 CA THR A 118 2320 2075 2389 -30 183 110 C ATOM 982 C THR A 118 4.332 26.780 31.746 1.00 19.21 C ANISOU 982 C THR A 118 2492 2252 2555 -38 166 99 C ATOM 983 O THR A 118 4.762 27.600 32.566 1.00 22.34 O ANISOU 983 O THR A 118 2880 2641 2969 -35 153 101 O ATOM 984 CB THR A 118 4.440 27.298 29.296 1.00 18.02 C ANISOU 984 CB THR A 118 2338 2110 2397 -22 190 114 C ATOM 985 OG1 THR A 118 5.176 27.058 28.089 1.00 22.88 O ANISOU 985 OG1 THR A 118 2955 2724 3016 -12 208 125 O ATOM 986 CG2 THR A 118 4.428 28.794 29.590 1.00 24.32 C ANISOU 986 CG2 THR A 118 3125 2905 3212 -16 182 121 C ATOM 987 N LEU A 119 3.211 26.080 31.949 1.00 19.28 N ANISOU 987 N LEU A 119 2510 2275 2542 -46 166 86 N ATOM 988 CA LEU A 119 2.450 26.213 33.189 1.00 20.43 C ANISOU 988 CA LEU A 119 2657 2426 2679 -52 153 76 C ATOM 989 C LEU A 119 3.277 25.791 34.397 1.00 20.23 C ANISOU 989 C LEU A 119 2632 2388 2665 -51 145 81 C ATOM 990 O LEU A 119 3.351 26.514 35.395 1.00 21.14 O ANISOU 990 O LEU A 119 2743 2505 2786 -48 130 78 O ATOM 991 CB LEU A 119 1.170 25.380 33.107 1.00 22.32 C ANISOU 991 CB LEU A 119 2903 2679 2896 -62 158 63 C ATOM 992 CG LEU A 119 0.389 25.223 34.419 1.00 26.00 C ANISOU 992 CG LEU A 119 3374 3151 3355 -68 151 55 C ATOM 993 CD1 LEU A 119 -0.263 26.527 34.810 1.00 21.24 C ANISOU 993 CD1 LEU A 119 2764 2559 2749 -64 138 51 C ATOM 994 CD2 LEU A 119 -0.648 24.104 34.323 1.00 23.76 C ANISOU 994 CD2 LEU A 119 3096 2874 3057 -79 162 43 C ATOM 995 N GLY A 120 3.908 24.617 34.324 1.00 21.83 N ANISOU 995 N GLY A 120 2841 2581 2871 -53 155 86 N ATOM 996 CA GLY A 120 4.660 24.117 35.464 1.00 19.03 C ANISOU 996 CA GLY A 120 2488 2219 2524 -49 149 92 C ATOM 997 C GLY A 120 5.890 24.947 35.778 1.00 18.62 C ANISOU 997 C GLY A 120 2423 2157 2494 -40 136 99 C ATOM 998 O GLY A 120 6.247 25.126 36.944 1.00 20.24 O ANISOU 998 O GLY A 120 2625 2365 2702 -35 121 98 O ATOM 999 N GLY A 121 6.569 25.444 34.745 1.00 18.06 N ANISOU 999 N GLY A 121 2344 2078 2440 -37 143 106 N ATOM 1000 CA GLY A 121 7.712 26.310 34.975 1.00 15.81 C ANISOU 1000 CA GLY A 121 2042 1781 2182 -30 132 111 C ATOM 1001 C GLY A 121 7.330 27.631 35.615 1.00 21.17 C ANISOU 1001 C GLY A 121 2712 2465 2866 -30 115 100 C ATOM 1002 O GLY A 121 8.047 28.141 36.484 1.00 19.87 O ANISOU 1002 O GLY A 121 2535 2295 2718 -26 99 96 O ATOM 1003 N GLU A 122 6.198 28.207 35.198 1.00 20.46 N ANISOU 1003 N GLU A 122 2626 2385 2764 -33 118 95 N ATOM 1004 CA GLU A 122 5.785 29.489 35.756 1.00 18.95 C ANISOU 1004 CA GLU A 122 2426 2196 2579 -32 104 85 C ATOM 1005 C GLU A 122 5.251 29.342 37.176 1.00 19.78 C ANISOU 1005 C GLU A 122 2536 2314 2667 -33 87 71 C ATOM 1006 O GLU A 122 5.415 30.259 37.988 1.00 20.20 O ANISOU 1006 O GLU A 122 2579 2366 2732 -30 71 60 O ATOM 1007 CB GLU A 122 4.744 30.160 34.858 1.00 19.58 C ANISOU 1007 CB GLU A 122 2507 2283 2649 -32 114 86 C ATOM 1008 CG GLU A 122 5.336 30.942 33.682 1.00 19.71 C ANISOU 1008 CG GLU A 122 2513 2287 2689 -25 127 100 C ATOM 1009 CD GLU A 122 6.196 32.125 34.114 1.00 20.18 C ANISOU 1009 CD GLU A 122 2554 2328 2786 -22 119 99 C ATOM 1010 OE1 GLU A 122 6.001 32.642 35.232 1.00 20.48 O ANISOU 1010 OE1 GLU A 122 2588 2367 2828 -24 101 84 O ATOM 1011 OE2 GLU A 122 7.078 32.540 33.332 1.00 22.71 O ANISOU 1011 OE2 GLU A 122 2864 2632 3133 -17 132 113 O ATOM 1012 N ILE A 123 4.625 28.206 37.499 1.00 17.34 N ANISOU 1012 N ILE A 123 2241 2015 2332 -36 92 71 N ATOM 1013 CA ILE A 123 4.244 27.953 38.888 1.00 18.29 C ANISOU 1013 CA ILE A 123 2366 2146 2435 -34 80 63 C ATOM 1014 C ILE A 123 5.482 27.931 39.772 1.00 17.44 C ANISOU 1014 C ILE A 123 2251 2034 2341 -25 64 63 C ATOM 1015 O ILE A 123 5.484 28.482 40.880 1.00 21.70 O ANISOU 1015 O ILE A 123 2786 2583 2876 -18 46 50 O ATOM 1016 CB ILE A 123 3.443 26.642 39.009 1.00 19.51 C ANISOU 1016 CB ILE A 123 2538 2309 2566 -38 93 67 C ATOM 1017 CG1 ILE A 123 2.070 26.780 38.356 1.00 22.38 C ANISOU 1017 CG1 ILE A 123 2906 2682 2915 -47 103 61 C ATOM 1018 CG2 ILE A 123 3.293 26.236 40.472 1.00 19.74 C ANISOU 1018 CG2 ILE A 123 2573 2349 2578 -32 84 65 C ATOM 1019 CD1 ILE A 123 1.307 25.477 38.267 1.00 24.71 C ANISOU 1019 CD1 ILE A 123 3213 2981 3194 -55 120 62 C ATOM 1020 N ALA A 124 6.561 27.305 39.290 1.00 17.81 N ANISOU 1020 N ALA A 124 2295 2069 2403 -23 71 75 N ATOM 1021 CA ALA A 124 7.794 27.246 40.066 1.00 17.45 C ANISOU 1021 CA ALA A 124 2238 2021 2371 -13 56 75 C ATOM 1022 C ALA A 124 8.389 28.633 40.286 1.00 18.41 C ANISOU 1022 C ALA A 124 2339 2136 2519 -11 38 61 C ATOM 1023 O ALA A 124 8.884 28.935 41.379 1.00 24.06 O ANISOU 1023 O ALA A 124 3046 2860 3237 -3 16 49 O ATOM 1024 CB ALA A 124 8.804 26.328 39.377 1.00 18.04 C ANISOU 1024 CB ALA A 124 2313 2082 2460 -11 69 92 C ATOM 1025 N LEU A 125 8.358 29.487 39.262 1.00 18.18 N ANISOU 1025 N LEU A 125 2302 2094 2512 -17 47 62 N ATOM 1026 CA LEU A 125 8.961 30.814 39.381 1.00 22.56 C ANISOU 1026 CA LEU A 125 2834 2636 3099 -17 35 50 C ATOM 1027 C LEU A 125 8.155 31.719 40.307 1.00 22.77 C ANISOU 1027 C LEU A 125 2860 2674 3117 -16 18 29 C ATOM 1028 O LEU A 125 8.728 32.435 41.138 1.00 21.38 O ANISOU 1028 O LEU A 125 2668 2498 2959 -13 -2 10 O ATOM 1029 CB LEU A 125 9.100 31.453 37.998 1.00 21.33 C ANISOU 1029 CB LEU A 125 2672 2463 2970 -21 55 63 C ATOM 1030 CG LEU A 125 9.516 32.928 37.970 1.00 22.70 C ANISOU 1030 CG LEU A 125 2823 2619 3182 -22 50 53 C ATOM 1031 CD1 LEU A 125 10.860 33.162 38.659 1.00 19.59 C ANISOU 1031 CD1 LEU A 125 2406 2216 2821 -20 32 41 C ATOM 1032 CD2 LEU A 125 9.550 33.436 36.541 1.00 22.32 C ANISOU 1032 CD2 LEU A 125 2772 2556 3155 -22 75 72 C ATOM 1033 N TRP A 126 6.827 31.714 40.178 1.00 20.80 N ANISOU 1033 N TRP A 126 2626 2436 2842 -20 26 29 N ATOM 1034 CA TRP A 126 6.018 32.523 41.079 1.00 23.37 C ANISOU 1034 CA TRP A 126 2951 2773 3157 -18 12 9 C ATOM 1035 C TRP A 126 5.958 31.925 42.480 1.00 20.69 C ANISOU 1035 C TRP A 126 2619 2453 2789 -10 -5 -2 C ATOM 1036 O TRP A 126 5.681 32.654 43.438 1.00 22.54 O ANISOU 1036 O TRP A 126 2849 2698 3019 -5 -22 -23 O ATOM 1037 CB TRP A 126 4.610 32.720 40.496 1.00 18.42 C ANISOU 1037 CB TRP A 126 2336 2152 2512 -23 27 13 C ATOM 1038 CG TRP A 126 4.587 33.648 39.287 1.00 17.88 C ANISOU 1038 CG TRP A 126 2258 2067 2469 -25 40 21 C ATOM 1039 CD1 TRP A 126 4.452 33.291 37.976 1.00 19.64 C ANISOU 1039 CD1 TRP A 126 2486 2286 2691 -27 61 40 C ATOM 1040 CD2 TRP A 126 4.708 35.080 39.299 1.00 22.38 C ANISOU 1040 CD2 TRP A 126 2812 2622 3070 -24 36 11 C ATOM 1041 NE1 TRP A 126 4.483 34.409 37.171 1.00 19.44 N ANISOU 1041 NE1 TRP A 126 2449 2246 2690 -25 71 46 N ATOM 1042 CE2 TRP A 126 4.637 35.518 37.959 1.00 21.18 C ANISOU 1042 CE2 TRP A 126 2657 2458 2934 -24 57 29 C ATOM 1043 CE3 TRP A 126 4.865 36.032 40.314 1.00 23.63 C ANISOU 1043 CE3 TRP A 126 2957 2776 3244 -22 18 -14 C ATOM 1044 CZ2 TRP A 126 4.716 36.865 37.607 1.00 17.66 C ANISOU 1044 CZ2 TRP A 126 2195 1992 2521 -21 63 28 C ATOM 1045 CZ3 TRP A 126 4.946 37.368 39.962 1.00 25.56 C ANISOU 1045 CZ3 TRP A 126 3186 3000 3524 -22 22 -19 C ATOM 1046 CH2 TRP A 126 4.873 37.771 38.620 1.00 19.31 C ANISOU 1046 CH2 TRP A 126 2392 2194 2751 -22 46 4 C ATOM 1047 N SER A 127 6.229 30.623 42.623 1.00 19.64 N ANISOU 1047 N SER A 127 2496 2327 2638 -7 0 13 N ATOM 1048 CA SER A 127 6.400 30.048 43.955 1.00 21.45 C ANISOU 1048 CA SER A 127 2731 2576 2843 6 -15 7 C ATOM 1049 C SER A 127 7.651 30.592 44.634 1.00 21.11 C ANISOU 1049 C SER A 127 2668 2533 2821 14 -40 -8 C ATOM 1050 O SER A 127 7.659 30.804 45.853 1.00 22.42 O ANISOU 1050 O SER A 127 2832 2717 2969 26 -61 -26 O ATOM 1051 CB SER A 127 6.454 28.522 43.873 1.00 20.39 C ANISOU 1051 CB SER A 127 2613 2445 2690 8 0 30 C ATOM 1052 OG SER A 127 5.211 28.002 43.433 1.00 20.03 O ANISOU 1052 OG SER A 127 2584 2402 2625 0 21 39 O ATOM 1053 N LEU A 128 8.723 30.817 43.868 1.00 18.80 N ANISOU 1053 N LEU A 128 2358 2219 2564 10 -38 -4 N ATOM 1054 CA LEU A 128 9.919 31.420 44.446 1.00 21.85 C ANISOU 1054 CA LEU A 128 2721 2604 2978 16 -62 -22 C ATOM 1055 C LEU A 128 9.661 32.854 44.885 1.00 21.05 C ANISOU 1055 C LEU A 128 2605 2501 2894 13 -78 -53 C ATOM 1056 O LEU A 128 10.249 33.311 45.869 1.00 20.98 O ANISOU 1056 O LEU A 128 2580 2502 2890 22 -105 -78 O ATOM 1057 CB LEU A 128 11.081 31.373 43.453 1.00 19.64 C ANISOU 1057 CB LEU A 128 2424 2300 2737 11 -52 -10 C ATOM 1058 CG LEU A 128 11.664 30.019 43.049 1.00 23.49 C ANISOU 1058 CG LEU A 128 2921 2787 3217 15 -39 17 C ATOM 1059 CD1 LEU A 128 12.745 30.226 41.992 1.00 26.98 C ANISOU 1059 CD1 LEU A 128 3345 3204 3703 10 -28 27 C ATOM 1060 CD2 LEU A 128 12.222 29.258 44.237 1.00 20.18 C ANISOU 1060 CD2 LEU A 128 2502 2390 2777 32 -59 14 C ATOM 1061 N VAL A 129 8.794 33.580 44.172 1.00 22.56 N ANISOU 1061 N VAL A 129 2800 2679 3093 3 -63 -52 N ATOM 1062 CA VAL A 129 8.419 34.920 44.619 1.00 22.99 C ANISOU 1062 CA VAL A 129 2843 2730 3164 1 -75 -80 C ATOM 1063 C VAL A 129 7.716 34.844 45.969 1.00 19.92 C ANISOU 1063 C VAL A 129 2465 2370 2735 12 -93 -100 C ATOM 1064 O VAL A 129 7.966 35.661 46.866 1.00 17.29 O ANISOU 1064 O VAL A 129 2118 2043 2410 17 -116 -132 O ATOM 1065 CB VAL A 129 7.545 35.620 43.559 1.00 26.32 C ANISOU 1065 CB VAL A 129 3269 3134 3598 -9 -52 -69 C ATOM 1066 CG1 VAL A 129 6.930 36.892 44.131 1.00 23.39 C ANISOU 1066 CG1 VAL A 129 2891 2761 3237 -9 -62 -97 C ATOM 1067 CG2 VAL A 129 8.365 35.945 42.317 1.00 20.25 C ANISOU 1067 CG2 VAL A 129 2485 2335 2872 -16 -35 -53 C ATOM 1068 N VAL A 130 6.834 33.857 46.138 1.00 19.21 N ANISOU 1068 N VAL A 130 2400 2299 2601 16 -82 -82 N ATOM 1069 CA VAL A 130 6.128 33.687 47.407 1.00 18.50 C ANISOU 1069 CA VAL A 130 2322 2238 2470 29 -95 -95 C ATOM 1070 C VAL A 130 7.114 33.365 48.522 1.00 23.99 C ANISOU 1070 C VAL A 130 3008 2952 3154 45 -121 -109 C ATOM 1071 O VAL A 130 7.064 33.949 49.613 1.00 24.29 O ANISOU 1071 O VAL A 130 3041 3009 3180 56 -144 -138 O ATOM 1072 CB VAL A 130 5.049 32.595 47.282 1.00 24.40 C ANISOU 1072 CB VAL A 130 3096 2997 3180 29 -73 -70 C ATOM 1073 CG1 VAL A 130 4.368 32.366 48.613 1.00 22.16 C ANISOU 1073 CG1 VAL A 130 2824 2742 2853 44 -82 -79 C ATOM 1074 CG2 VAL A 130 4.022 32.972 46.225 1.00 24.39 C ANISOU 1074 CG2 VAL A 130 3099 2981 3186 14 -51 -61 C ATOM 1075 N LEU A 131 8.030 32.430 48.263 1.00 20.26 N ANISOU 1075 N LEU A 131 2534 2478 2686 48 -119 -89 N ATOM 1076 CA LEU A 131 9.010 32.054 49.279 1.00 21.86 C ANISOU 1076 CA LEU A 131 2728 2702 2877 67 -144 -99 C ATOM 1077 C LEU A 131 9.907 33.228 49.640 1.00 20.08 C ANISOU 1077 C LEU A 131 2471 2471 2686 67 -172 -136 C ATOM 1078 O LEU A 131 10.257 33.415 50.811 1.00 25.04 O ANISOU 1078 O LEU A 131 3092 3126 3297 84 -201 -162 O ATOM 1079 CB LEU A 131 9.838 30.865 48.790 1.00 26.21 C ANISOU 1079 CB LEU A 131 3281 3247 3432 70 -133 -68 C ATOM 1080 CG LEU A 131 9.102 29.526 48.808 1.00 22.28 C ANISOU 1080 CG LEU A 131 2812 2759 2896 75 -110 -36 C ATOM 1081 CD1 LEU A 131 9.875 28.455 48.055 1.00 21.95 C ANISOU 1081 CD1 LEU A 131 2771 2701 2866 74 -94 -7 C ATOM 1082 CD2 LEU A 131 8.854 29.104 50.251 1.00 19.42 C ANISOU 1082 CD2 LEU A 131 2460 2431 2488 100 -124 -40 C ATOM 1083 N ALA A 132 10.288 34.036 48.648 1.00 17.75 N ANISOU 1083 N ALA A 132 2159 2143 2441 49 -164 -140 N ATOM 1084 CA ALA A 132 11.137 35.189 48.929 1.00 22.67 C ANISOU 1084 CA ALA A 132 2751 2757 3107 46 -188 -177 C ATOM 1085 C ALA A 132 10.434 36.177 49.851 1.00 21.69 C ANISOU 1085 C ALA A 132 2625 2645 2971 50 -205 -214 C ATOM 1086 O ALA A 132 11.037 36.687 50.803 1.00 20.34 O ANISOU 1086 O ALA A 132 2434 2489 2804 60 -236 -252 O ATOM 1087 CB ALA A 132 11.551 35.866 47.621 1.00 24.80 C ANISOU 1087 CB ALA A 132 3004 2985 3434 26 -168 -169 C ATOM 1088 N ILE A 133 9.152 36.450 49.590 1.00 21.95 N ANISOU 1088 N ILE A 133 2677 2674 2988 44 -186 -207 N ATOM 1089 CA ILE A 133 8.377 37.336 50.459 1.00 23.05 C ANISOU 1089 CA ILE A 133 2818 2827 3114 49 -199 -241 C ATOM 1090 C ILE A 133 8.246 36.741 51.855 1.00 24.67 C ANISOU 1090 C ILE A 133 3034 3075 3264 73 -221 -253 C ATOM 1091 O ILE A 133 8.400 37.444 52.861 1.00 25.68 O ANISOU 1091 O ILE A 133 3149 3220 3387 83 -248 -294 O ATOM 1092 CB ILE A 133 6.996 37.623 49.837 1.00 17.87 C ANISOU 1092 CB ILE A 133 2180 2159 2449 40 -172 -225 C ATOM 1093 CG1 ILE A 133 7.134 38.556 48.633 1.00 17.83 C ANISOU 1093 CG1 ILE A 133 2160 2114 2500 22 -154 -221 C ATOM 1094 CG2 ILE A 133 6.053 38.223 50.876 1.00 20.37 C ANISOU 1094 CG2 ILE A 133 2505 2497 2738 50 -183 -254 C ATOM 1095 CD1 ILE A 133 5.886 38.639 47.765 1.00 20.02 C ANISOU 1095 CD1 ILE A 133 2455 2380 2769 14 -125 -196 C ATOM 1096 N GLU A 134 7.958 35.439 51.943 1.00 21.91 N ANISOU 1096 N GLU A 134 2708 2745 2873 82 -209 -218 N ATOM 1097 CA GLU A 134 7.814 34.813 53.254 1.00 27.65 C ANISOU 1097 CA GLU A 134 3447 3513 3545 108 -225 -223 C ATOM 1098 C GLU A 134 9.110 34.903 54.051 1.00 26.66 C ANISOU 1098 C GLU A 134 3298 3407 3423 124 -261 -250 C ATOM 1099 O GLU A 134 9.087 35.210 55.248 1.00 23.02 O ANISOU 1099 O GLU A 134 2835 2979 2933 144 -287 -281 O ATOM 1100 CB GLU A 134 7.367 33.358 53.096 1.00 25.99 C ANISOU 1100 CB GLU A 134 3263 3313 3298 115 -201 -177 C ATOM 1101 CG GLU A 134 7.080 32.634 54.407 1.00 25.68 C ANISOU 1101 CG GLU A 134 3241 3316 3201 144 -210 -173 C ATOM 1102 CD GLU A 134 8.245 31.775 54.869 1.00 22.46 C ANISOU 1102 CD GLU A 134 2827 2927 2781 164 -225 -162 C ATOM 1103 OE1 GLU A 134 9.280 31.759 54.175 1.00 25.66 O ANISOU 1103 OE1 GLU A 134 3213 3311 3224 153 -230 -160 O ATOM 1104 OE2 GLU A 134 8.126 31.107 55.919 1.00 23.40 O ANISOU 1104 OE2 GLU A 134 2959 3081 2851 191 -231 -154 O ATOM 1105 N ARG A 135 10.250 34.651 53.400 1.00 21.64 N ANISOU 1105 N ARG A 135 2645 2754 2825 117 -263 -240 N ATOM 1106 CA ARG A 135 11.542 34.755 54.075 1.00 22.36 C ANISOU 1106 CA ARG A 135 2709 2862 2926 130 -298 -267 C ATOM 1107 C ARG A 135 11.813 36.183 54.529 1.00 28.66 C ANISOU 1107 C ARG A 135 3479 3656 3755 125 -325 -323 C ATOM 1108 O ARG A 135 12.256 36.411 55.659 1.00 26.50 O ANISOU 1108 O ARG A 135 3193 3416 3462 145 -360 -360 O ATOM 1109 CB ARG A 135 12.663 34.274 53.150 1.00 23.22 C ANISOU 1109 CB ARG A 135 2802 2947 3074 120 -290 -245 C ATOM 1110 CG ARG A 135 12.774 32.766 53.000 1.00 19.00 C ANISOU 1110 CG ARG A 135 2288 2422 2507 133 -274 -198 C ATOM 1111 CD ARG A 135 13.107 32.093 54.328 1.00 24.49 C ANISOU 1111 CD ARG A 135 2987 3165 3153 167 -299 -201 C ATOM 1112 NE ARG A 135 11.905 31.714 55.062 1.00 28.51 N ANISOU 1112 NE ARG A 135 3527 3701 3606 181 -289 -191 N ATOM 1113 CZ ARG A 135 11.891 31.323 56.329 1.00 25.01 C ANISOU 1113 CZ ARG A 135 3091 3301 3110 213 -308 -196 C ATOM 1114 NH1 ARG A 135 13.000 31.269 57.049 1.00 21.89 N ANISOU 1114 NH1 ARG A 135 2675 2934 2710 235 -342 -215 N ATOM 1115 NH2 ARG A 135 10.736 30.976 56.886 1.00 21.08 N ANISOU 1115 NH2 ARG A 135 2621 2822 2565 225 -293 -182 N ATOM 1116 N TYR A 136 11.540 37.159 53.659 1.00 20.54 N ANISOU 1116 N TYR A 136 2442 2588 2776 100 -309 -332 N ATOM 1117 CA TYR A 136 11.790 38.554 53.998 1.00 23.30 C ANISOU 1117 CA TYR A 136 2763 2926 3165 92 -330 -385 C ATOM 1118 C TYR A 136 10.928 39.008 55.172 1.00 33.93 C ANISOU 1118 C TYR A 136 4120 4303 4468 108 -347 -419 C ATOM 1119 O TYR A 136 11.393 39.762 56.036 1.00 33.44 O ANISOU 1119 O TYR A 136 4036 4256 4414 116 -379 -471 O ATOM 1120 CB TYR A 136 11.549 39.436 52.773 1.00 30.87 C ANISOU 1120 CB TYR A 136 3714 3833 4183 65 -302 -378 C ATOM 1121 CG TYR A 136 11.356 40.896 53.101 1.00 31.32 C ANISOU 1121 CG TYR A 136 3751 3873 4276 57 -314 -428 C ATOM 1122 CD1 TYR A 136 12.416 41.673 53.545 1.00 36.66 C ANISOU 1122 CD1 TYR A 136 4390 4544 4997 54 -342 -476 C ATOM 1123 CD2 TYR A 136 10.116 41.498 52.962 1.00 35.88 C ANISOU 1123 CD2 TYR A 136 4346 4441 4847 51 -295 -428 C ATOM 1124 CE1 TYR A 136 12.244 43.011 53.847 1.00 36.21 C ANISOU 1124 CE1 TYR A 136 4314 4469 4978 46 -351 -524 C ATOM 1125 CE2 TYR A 136 9.933 42.835 53.260 1.00 39.58 C ANISOU 1125 CE2 TYR A 136 4796 4891 5350 45 -303 -472 C ATOM 1126 CZ TYR A 136 11.001 43.583 53.702 1.00 39.92 C ANISOU 1126 CZ TYR A 136 4803 4927 5439 41 -330 -521 C ATOM 1127 OH TYR A 136 10.824 44.913 53.999 1.00 47.47 O ANISOU 1127 OH TYR A 136 5740 5862 6435 34 -336 -568 O ATOM 1128 N VAL A 137 9.668 38.568 55.216 1.00 30.01 N ANISOU 1128 N VAL A 137 3658 3818 3927 114 -324 -392 N ATOM 1129 CA VAL A 137 8.785 38.945 56.318 1.00 30.15 C ANISOU 1129 CA VAL A 137 3688 3866 3900 130 -336 -420 C ATOM 1130 C VAL A 137 9.237 38.295 57.622 1.00 32.64 C ANISOU 1130 C VAL A 137 4006 4234 4161 163 -366 -433 C ATOM 1131 O VAL A 137 9.316 38.954 58.665 1.00 27.16 O ANISOU 1131 O VAL A 137 3301 3566 3452 178 -396 -481 O ATOM 1132 CB VAL A 137 7.327 38.583 55.985 1.00 32.45 C ANISOU 1132 CB VAL A 137 4013 4156 4161 127 -302 -384 C ATOM 1133 CG1 VAL A 137 6.466 38.651 57.244 1.00 35.27 C ANISOU 1133 CG1 VAL A 137 4387 4552 4460 151 -312 -404 C ATOM 1134 CG2 VAL A 137 6.788 39.515 54.923 1.00 31.08 C ANISOU 1134 CG2 VAL A 137 3835 3938 4037 101 -279 -383 C ATOM 1135 N VAL A 138 9.540 36.993 57.586 1.00 28.20 N ANISOU 1135 N VAL A 138 3458 3689 3568 175 -359 -390 N ATOM 1136 CA VAL A 138 9.877 36.276 58.814 1.00 27.39 C ANISOU 1136 CA VAL A 138 3361 3639 3408 211 -383 -394 C ATOM 1137 C VAL A 138 11.233 36.721 59.352 1.00 31.79 C ANISOU 1137 C VAL A 138 3882 4211 3985 220 -426 -439 C ATOM 1138 O VAL A 138 11.408 36.894 60.566 1.00 34.38 O ANISOU 1138 O VAL A 138 4204 4583 4274 248 -458 -474 O ATOM 1139 CB VAL A 138 9.838 34.755 58.575 1.00 27.19 C ANISOU 1139 CB VAL A 138 3360 3622 3350 222 -360 -334 C ATOM 1140 CG1 VAL A 138 10.530 34.010 59.714 1.00 31.56 C ANISOU 1140 CG1 VAL A 138 3912 4226 3853 260 -386 -334 C ATOM 1141 CG2 VAL A 138 8.406 34.274 58.418 1.00 29.54 C ANISOU 1141 CG2 VAL A 138 3692 3917 3614 219 -323 -298 C ATOM 1142 N VAL A 139 12.211 36.915 58.470 1.00 30.95 N ANISOU 1142 N VAL A 139 3750 4071 3940 199 -427 -439 N ATOM 1143 CA VAL A 139 13.571 37.183 58.924 1.00 29.87 C ANISOU 1143 CA VAL A 139 3576 3948 3825 208 -467 -477 C ATOM 1144 C VAL A 139 13.757 38.661 59.267 1.00 35.25 C ANISOU 1144 C VAL A 139 4226 4619 4546 196 -493 -545 C ATOM 1145 O VAL A 139 14.352 38.998 60.297 1.00 38.05 O ANISOU 1145 O VAL A 139 4560 5011 4887 216 -534 -594 O ATOM 1146 CB VAL A 139 14.590 36.705 57.871 1.00 30.12 C ANISOU 1146 CB VAL A 139 3590 3948 3905 191 -456 -447 C ATOM 1147 CG1 VAL A 139 15.999 37.142 58.250 1.00 36.31 C ANISOU 1147 CG1 VAL A 139 4330 4741 4725 196 -496 -491 C ATOM 1148 CG2 VAL A 139 14.528 35.189 57.727 1.00 24.81 C ANISOU 1148 CG2 VAL A 139 2946 3291 3190 207 -435 -386 C ATOM 1149 N CYS A 140 13.259 39.566 58.416 1.00 37.15 N ANISOU 1149 N CYS A 140 4464 4812 4839 166 -469 -551 N ATOM 1150 CA CYS A 140 13.457 41.000 58.614 1.00 32.30 C ANISOU 1150 CA CYS A 140 3819 4178 4275 152 -488 -613 C ATOM 1151 C CYS A 140 12.381 41.638 59.486 1.00 40.55 C ANISOU 1151 C CYS A 140 4880 5244 5283 163 -494 -647 C ATOM 1152 O CYS A 140 12.606 42.731 60.020 1.00 48.04 O ANISOU 1152 O CYS A 140 5803 6191 6259 160 -519 -709 O ATOM 1153 CB CYS A 140 13.502 41.728 57.265 1.00 34.99 C ANISOU 1153 CB CYS A 140 4146 4454 4695 115 -457 -601 C ATOM 1154 SG CYS A 140 14.913 41.304 56.207 1.00 41.24 S ANISOU 1154 SG CYS A 140 4909 5213 5546 99 -451 -574 S ATOM 1155 N LYS A 141 11.233 40.981 59.633 1.00 41.85 N ANISOU 1155 N LYS A 141 5085 5428 5389 176 -471 -608 N ATOM 1156 CA LYS A 141 10.089 41.456 60.407 1.00 42.68 C ANISOU 1156 CA LYS A 141 5210 5554 5454 188 -470 -631 C ATOM 1157 C LYS A 141 9.759 42.932 60.146 1.00 48.82 C ANISOU 1157 C LYS A 141 5969 6291 6287 165 -467 -675 C ATOM 1158 O LYS A 141 9.778 43.747 61.072 1.00 52.87 O ANISOU 1158 O LYS A 141 6468 6823 6796 176 -495 -735 O ATOM 1159 CB LYS A 141 10.290 41.199 61.896 1.00 39.30 C ANISOU 1159 CB LYS A 141 4782 5189 4960 226 -508 -664 C ATOM 1160 CG LYS A 141 10.303 39.719 62.262 1.00 36.97 C ANISOU 1160 CG LYS A 141 4513 4935 4599 254 -503 -613 C ATOM 1161 CD LYS A 141 10.932 39.468 63.617 1.00 42.42 C ANISOU 1161 CD LYS A 141 5195 5688 5236 293 -546 -646 C ATOM 1162 CE LYS A 141 11.296 38.001 63.777 1.00 44.44 C ANISOU 1162 CE LYS A 141 5467 5974 5443 318 -541 -592 C ATOM 1163 NZ LYS A 141 12.330 37.582 62.786 1.00 42.12 N ANISOU 1163 NZ LYS A 141 5154 5648 5202 298 -537 -566 N ATOM 1164 N PRO A 142 9.431 43.297 58.894 1.00 54.24 N ANISOU 1164 N PRO A 142 6656 6924 7027 136 -432 -647 N ATOM 1165 CA PRO A 142 9.137 44.700 58.597 1.00 55.61 C ANISOU 1165 CA PRO A 142 6813 7058 7259 116 -425 -684 C ATOM 1166 C PRO A 142 7.706 45.089 58.959 1.00 58.88 C ANISOU 1166 C PRO A 142 7253 7479 7638 123 -409 -687 C ATOM 1167 O PRO A 142 7.274 44.846 60.088 1.00 64.02 O ANISOU 1167 O PRO A 142 7920 8178 8228 149 -427 -706 O ATOM 1168 CB PRO A 142 9.353 44.777 57.085 1.00 55.77 C ANISOU 1168 CB PRO A 142 6827 7022 7341 88 -392 -642 C ATOM 1169 CG PRO A 142 8.931 43.432 56.605 1.00 54.82 C ANISOU 1169 CG PRO A 142 6738 6917 7173 94 -369 -577 C ATOM 1170 CD PRO A 142 9.320 42.448 57.694 1.00 53.62 C ANISOU 1170 CD PRO A 142 6595 6822 6958 122 -398 -580 C ATOM 1171 N ARG A 147 2.343 38.396 60.935 1.00 60.82 N ANISOU 1171 N ARG A 147 7707 7916 7484 231 -294 -421 N ATOM 1172 CA ARG A 147 3.181 37.234 60.669 1.00 53.42 C ANISOU 1172 CA ARG A 147 6772 6984 6541 235 -293 -384 C ATOM 1173 C ARG A 147 2.621 36.399 59.524 1.00 61.52 C ANISOU 1173 C ARG A 147 7814 7980 7582 214 -255 -329 C ATOM 1174 O ARG A 147 1.416 36.144 59.457 1.00 64.00 O ANISOU 1174 O ARG A 147 8148 8294 7876 212 -226 -307 O ATOM 1175 CB ARG A 147 3.315 36.369 61.923 1.00 58.91 C ANISOU 1175 CB ARG A 147 7481 7732 7169 274 -304 -376 C ATOM 1176 N PHE A 148 3.502 35.978 58.620 1.00 57.03 N ANISOU 1176 N PHE A 148 7233 7386 7048 198 -253 -310 N ATOM 1177 CA PHE A 148 3.089 35.134 57.506 1.00 50.35 C ANISOU 1177 CA PHE A 148 6401 6514 6216 179 -219 -261 C ATOM 1178 C PHE A 148 2.570 33.806 58.038 1.00 49.65 C ANISOU 1178 C PHE A 148 6338 6451 6075 198 -199 -221 C ATOM 1179 O PHE A 148 3.294 33.082 58.727 1.00 52.51 O ANISOU 1179 O PHE A 148 6702 6840 6410 222 -212 -212 O ATOM 1180 CB PHE A 148 4.270 34.906 56.559 1.00 43.08 C ANISOU 1180 CB PHE A 148 5463 5566 5339 163 -223 -250 C ATOM 1181 CG PHE A 148 3.881 34.323 55.226 1.00 37.23 C ANISOU 1181 CG PHE A 148 4732 4793 4622 139 -190 -210 C ATOM 1182 CD1 PHE A 148 3.654 32.964 55.083 1.00 38.73 C ANISOU 1182 CD1 PHE A 148 4940 4988 4786 144 -168 -167 C ATOM 1183 CD2 PHE A 148 3.746 35.137 54.114 1.00 39.06 C ANISOU 1183 CD2 PHE A 148 4952 4989 4902 114 -181 -216 C ATOM 1184 CE1 PHE A 148 3.294 32.431 53.858 1.00 38.32 C ANISOU 1184 CE1 PHE A 148 4895 4908 4756 123 -139 -136 C ATOM 1185 CE2 PHE A 148 3.385 34.609 52.888 1.00 38.84 C ANISOU 1185 CE2 PHE A 148 4932 4935 4890 95 -152 -181 C ATOM 1186 CZ PHE A 148 3.158 33.254 52.763 1.00 32.59 C ANISOU 1186 CZ PHE A 148 4159 4151 4073 99 -132 -144 C ATOM 1187 N GLY A 149 1.322 33.469 57.714 1.00 49.52 N ANISOU 1187 N GLY A 149 6340 6428 6049 190 -167 -196 N ATOM 1188 CA GLY A 149 0.748 32.244 58.234 1.00 46.54 C ANISOU 1188 CA GLY A 149 5986 6071 5628 207 -144 -158 C ATOM 1189 C GLY A 149 0.162 31.311 57.193 1.00 43.54 C ANISOU 1189 C GLY A 149 5617 5664 5263 186 -107 -117 C ATOM 1190 O GLY A 149 0.389 31.475 55.993 1.00 47.72 O ANISOU 1190 O GLY A 149 6137 6161 5834 160 -102 -113 O ATOM 1191 N GLU A 150 -0.593 30.320 57.673 1.00 42.68 N ANISOU 1191 N GLU A 150 5527 5569 5118 198 -81 -85 N ATOM 1192 CA GLU A 150 -1.189 29.328 56.783 1.00 39.12 C ANISOU 1192 CA GLU A 150 5087 5095 4682 179 -45 -48 C ATOM 1193 C GLU A 150 -2.041 29.991 55.712 1.00 34.61 C ANISOU 1193 C GLU A 150 4510 4497 4144 149 -33 -58 C ATOM 1194 O GLU A 150 -1.958 29.637 54.533 1.00 41.24 O ANISOU 1194 O GLU A 150 5346 5308 5014 126 -21 -43 O ATOM 1195 CB GLU A 150 -2.024 28.342 57.606 1.00 41.42 C ANISOU 1195 CB GLU A 150 5399 5406 4934 198 -17 -18 C ATOM 1196 CG GLU A 150 -1.938 26.894 57.152 1.00 39.43 C ANISOU 1196 CG GLU A 150 5157 5138 4688 194 13 24 C ATOM 1197 CD GLU A 150 -1.899 25.928 58.321 1.00 43.46 C ANISOU 1197 CD GLU A 150 5683 5674 5156 227 26 53 C ATOM 1198 OE1 GLU A 150 -1.624 26.375 59.455 1.00 44.73 O ANISOU 1198 OE1 GLU A 150 5845 5870 5280 257 5 38 O ATOM 1199 OE2 GLU A 150 -2.141 24.723 58.110 1.00 47.31 O ANISOU 1199 OE2 GLU A 150 6182 6149 5647 225 59 90 O ATOM 1200 N ASN A 151 -2.866 30.967 56.110 1.00 33.60 N ANISOU 1200 N ASN A 151 4380 4378 4007 151 -38 -82 N ATOM 1201 CA ASN A 151 -3.707 31.670 55.144 1.00 39.70 C ANISOU 1201 CA ASN A 151 5147 5128 4809 126 -27 -90 C ATOM 1202 C ASN A 151 -2.868 32.358 54.075 1.00 35.61 C ANISOU 1202 C ASN A 151 4611 4583 4335 107 -43 -104 C ATOM 1203 O ASN A 151 -3.215 32.330 52.889 1.00 37.90 O ANISOU 1203 O ASN A 151 4898 4850 4652 86 -28 -93 O ATOM 1204 CB ASN A 151 -4.589 32.694 55.861 1.00 38.05 C ANISOU 1204 CB ASN A 151 4938 4935 4584 135 -32 -116 C ATOM 1205 CG ASN A 151 -5.572 32.051 56.824 1.00 37.67 C ANISOU 1205 CG ASN A 151 4907 4912 4495 153 -11 -100 C ATOM 1206 OD1 ASN A 151 -6.169 31.015 56.528 1.00 33.83 O ANISOU 1206 OD1 ASN A 151 4430 4420 4004 146 18 -69 O ATOM 1207 ND2 ASN A 151 -5.741 32.667 57.988 1.00 39.78 N ANISOU 1207 ND2 ASN A 151 5177 5207 4732 176 -24 -123 N ATOM 1208 N HIS A 152 -1.766 32.994 54.482 1.00 34.33 N ANISOU 1208 N HIS A 152 4437 4425 4181 117 -72 -128 N ATOM 1209 CA HIS A 152 -0.890 33.654 53.520 1.00 38.57 C ANISOU 1209 CA HIS A 152 4956 4936 4764 100 -85 -140 C ATOM 1210 C HIS A 152 -0.271 32.648 52.557 1.00 35.78 C ANISOU 1210 C HIS A 152 4603 4564 4427 88 -73 -110 C ATOM 1211 O HIS A 152 -0.176 32.909 51.352 1.00 37.12 O ANISOU 1211 O HIS A 152 4765 4707 4631 69 -65 -104 O ATOM 1212 CB HIS A 152 0.208 34.429 54.251 1.00 41.30 C ANISOU 1212 CB HIS A 152 5286 5290 5115 113 -119 -174 C ATOM 1213 CG HIS A 152 -0.302 35.508 55.156 1.00 48.74 C ANISOU 1213 CG HIS A 152 6226 6248 6046 124 -134 -211 C ATOM 1214 ND1 HIS A 152 -0.782 35.254 56.423 1.00 46.38 N ANISOU 1214 ND1 HIS A 152 5939 5984 5698 148 -137 -217 N ATOM 1215 CD2 HIS A 152 -0.394 36.848 54.982 1.00 49.57 C ANISOU 1215 CD2 HIS A 152 6315 6337 6181 116 -144 -243 C ATOM 1216 CE1 HIS A 152 -1.155 36.389 56.986 1.00 57.10 C ANISOU 1216 CE1 HIS A 152 7291 7349 7056 154 -150 -254 C ATOM 1217 NE2 HIS A 152 -0.929 37.372 56.134 1.00 56.93 N ANISOU 1217 NE2 HIS A 152 7252 7296 7084 134 -154 -271 N ATOM 1218 N ALA A 153 0.160 31.495 53.073 1.00 36.21 N ANISOU 1218 N ALA A 153 4668 4633 4457 102 -69 -89 N ATOM 1219 CA ALA A 153 0.804 30.495 52.228 1.00 33.75 C ANISOU 1219 CA ALA A 153 4357 4303 4161 92 -57 -61 C ATOM 1220 C ALA A 153 -0.166 29.928 51.197 1.00 31.37 C ANISOU 1220 C ALA A 153 4066 3985 3869 73 -26 -39 C ATOM 1221 O ALA A 153 0.173 29.804 50.015 1.00 34.41 O ANISOU 1221 O ALA A 153 4445 4347 4282 56 -18 -30 O ATOM 1222 CB ALA A 153 1.386 29.376 53.092 1.00 33.12 C ANISOU 1222 CB ALA A 153 4288 4244 4053 115 -58 -42 C ATOM 1223 N ILE A 154 -1.380 29.575 51.626 1.00 34.62 N ANISOU 1223 N ILE A 154 4490 4409 4255 75 -7 -31 N ATOM 1224 CA ILE A 154 -2.349 28.997 50.699 1.00 28.65 C ANISOU 1224 CA ILE A 154 3741 3639 3508 56 21 -13 C ATOM 1225 C ILE A 154 -2.794 30.037 49.681 1.00 34.30 C ANISOU 1225 C ILE A 154 4445 4340 4250 38 19 -28 C ATOM 1226 O ILE A 154 -2.975 29.730 48.496 1.00 25.71 O ANISOU 1226 O ILE A 154 3354 3234 3180 21 32 -18 O ATOM 1227 CB ILE A 154 -3.544 28.404 51.468 1.00 31.61 C ANISOU 1227 CB ILE A 154 4129 4029 3852 64 42 -2 C ATOM 1228 CG1 ILE A 154 -3.065 27.313 52.427 1.00 34.43 C ANISOU 1228 CG1 ILE A 154 4499 4400 4185 84 48 19 C ATOM 1229 CG2 ILE A 154 -4.578 27.846 50.501 1.00 38.08 C ANISOU 1229 CG2 ILE A 154 4951 4835 4685 42 69 11 C ATOM 1230 CD1 ILE A 154 -4.181 26.476 53.009 1.00 36.61 C ANISOU 1230 CD1 ILE A 154 4788 4685 4437 89 78 39 C ATOM 1231 N MET A 155 -2.982 31.280 50.128 1.00 32.83 N ANISOU 1231 N MET A 155 4250 4159 4064 44 2 -53 N ATOM 1232 CA MET A 155 -3.276 32.367 49.203 1.00 29.69 C ANISOU 1232 CA MET A 155 3841 3746 3694 31 0 -66 C ATOM 1233 C MET A 155 -2.181 32.492 48.153 1.00 30.32 C ANISOU 1233 C MET A 155 3910 3804 3807 21 -6 -62 C ATOM 1234 O MET A 155 -2.463 32.731 46.973 1.00 25.02 O ANISOU 1234 O MET A 155 3233 3116 3155 8 5 -55 O ATOM 1235 CB MET A 155 -3.429 33.672 49.982 1.00 29.67 C ANISOU 1235 CB MET A 155 3831 3751 3690 41 -18 -95 C ATOM 1236 CG MET A 155 -3.971 34.839 49.194 1.00 35.78 C ANISOU 1236 CG MET A 155 4594 4510 4490 31 -16 -106 C ATOM 1237 SD MET A 155 -3.924 36.342 50.190 1.00 49.39 S ANISOU 1237 SD MET A 155 6308 6238 6218 44 -38 -144 S ATOM 1238 CE MET A 155 -4.178 35.669 51.828 1.00 31.62 C ANISOU 1238 CE MET A 155 4072 4022 3918 64 -43 -150 C ATOM 1239 N GLY A 156 -0.923 32.329 48.571 1.00 25.43 N ANISOU 1239 N GLY A 156 3286 3183 3192 29 -22 -65 N ATOM 1240 CA GLY A 156 0.173 32.349 47.624 1.00 22.85 C ANISOU 1240 CA GLY A 156 2949 2836 2898 21 -24 -59 C ATOM 1241 C GLY A 156 0.104 31.206 46.634 1.00 25.17 C ANISOU 1241 C GLY A 156 3251 3120 3193 10 -3 -32 C ATOM 1242 O GLY A 156 0.440 31.374 45.460 1.00 25.33 O ANISOU 1242 O GLY A 156 3264 3122 3238 0 4 -25 O ATOM 1243 N VAL A 157 -0.340 30.031 47.089 1.00 24.46 N ANISOU 1243 N VAL A 157 3176 3042 3077 14 10 -17 N ATOM 1244 CA VAL A 157 -0.455 28.882 46.193 1.00 22.30 C ANISOU 1244 CA VAL A 157 2910 2758 2806 3 32 5 C ATOM 1245 C VAL A 157 -1.428 29.187 45.065 1.00 25.48 C ANISOU 1245 C VAL A 157 3310 3154 3218 -12 46 4 C ATOM 1246 O VAL A 157 -1.104 29.030 43.883 1.00 21.82 O ANISOU 1246 O VAL A 157 2842 2676 2772 -22 54 12 O ATOM 1247 CB VAL A 157 -0.889 27.626 46.969 1.00 26.91 C ANISOU 1247 CB VAL A 157 3508 3352 3363 10 47 21 C ATOM 1248 CG1 VAL A 157 -1.314 26.525 45.990 1.00 27.52 C ANISOU 1248 CG1 VAL A 157 3592 3418 3448 -5 73 37 C ATOM 1249 CG2 VAL A 157 0.225 27.141 47.872 1.00 24.11 C ANISOU 1249 CG2 VAL A 157 3156 3005 3000 28 36 28 C ATOM 1250 N ALA A 158 -2.632 29.650 45.416 1.00 26.46 N ANISOU 1250 N ALA A 158 3436 3289 3328 -12 50 -4 N ATOM 1251 CA ALA A 158 -3.620 29.991 44.399 1.00 23.13 C ANISOU 1251 CA ALA A 158 3011 2866 2914 -24 61 -6 C ATOM 1252 C ALA A 158 -3.107 31.097 43.489 1.00 21.93 C ANISOU 1252 C ALA A 158 2846 2700 2786 -26 52 -12 C ATOM 1253 O ALA A 158 -3.394 31.109 42.288 1.00 20.28 O ANISOU 1253 O ALA A 158 2634 2486 2587 -35 62 -6 O ATOM 1254 CB ALA A 158 -4.933 30.405 45.063 1.00 28.18 C ANISOU 1254 CB ALA A 158 3652 3521 3535 -22 64 -15 C ATOM 1255 N PHE A 159 -2.342 32.032 44.050 1.00 25.13 N ANISOU 1255 N PHE A 159 3244 3101 3204 -18 34 -24 N ATOM 1256 CA PHE A 159 -1.761 33.113 43.265 1.00 23.46 C ANISOU 1256 CA PHE A 159 3019 2873 3023 -20 29 -27 C ATOM 1257 C PHE A 159 -0.788 32.592 42.212 1.00 20.32 C ANISOU 1257 C PHE A 159 2617 2460 2643 -25 36 -12 C ATOM 1258 O PHE A 159 -0.703 33.159 41.118 1.00 19.91 O ANISOU 1258 O PHE A 159 2558 2397 2610 -28 43 -6 O ATOM 1259 CB PHE A 159 -1.081 34.103 44.216 1.00 25.27 C ANISOU 1259 CB PHE A 159 3237 3098 3264 -11 8 -47 C ATOM 1260 CG PHE A 159 -0.190 35.102 43.542 1.00 27.08 C ANISOU 1260 CG PHE A 159 3450 3305 3532 -12 4 -51 C ATOM 1261 CD1 PHE A 159 -0.718 36.236 42.946 1.00 27.78 C ANISOU 1261 CD1 PHE A 159 3532 3385 3641 -13 10 -54 C ATOM 1262 CD2 PHE A 159 1.187 34.925 43.540 1.00 28.85 C ANISOU 1262 CD2 PHE A 159 3666 3518 3777 -12 -5 -50 C ATOM 1263 CE1 PHE A 159 0.106 37.162 42.336 1.00 27.58 C ANISOU 1263 CE1 PHE A 159 3490 3335 3654 -14 10 -54 C ATOM 1264 CE2 PHE A 159 2.016 35.847 42.932 1.00 28.14 C ANISOU 1264 CE2 PHE A 159 3559 3405 3727 -14 -6 -52 C ATOM 1265 CZ PHE A 159 1.475 36.969 42.333 1.00 30.62 C ANISOU 1265 CZ PHE A 159 3867 3708 4062 -15 2 -54 C ATOM 1266 N THR A 160 -0.052 31.516 42.510 1.00 20.37 N ANISOU 1266 N THR A 160 2630 2467 2643 -24 36 -3 N ATOM 1267 CA THR A 160 0.893 30.994 41.526 1.00 17.18 C ANISOU 1267 CA THR A 160 2224 2048 2256 -28 44 11 C ATOM 1268 C THR A 160 0.172 30.406 40.317 1.00 21.42 C ANISOU 1268 C THR A 160 2767 2586 2786 -36 63 22 C ATOM 1269 O THR A 160 0.647 30.547 39.184 1.00 17.38 O ANISOU 1269 O THR A 160 2250 2063 2290 -38 71 31 O ATOM 1270 CB THR A 160 1.826 29.951 42.152 1.00 22.80 C ANISOU 1270 CB THR A 160 2940 2760 2962 -23 40 18 C ATOM 1271 OG1 THR A 160 1.082 28.792 42.543 1.00 17.76 O ANISOU 1271 OG1 THR A 160 2316 2132 2298 -24 52 26 O ATOM 1272 CG2 THR A 160 2.555 30.525 43.365 1.00 16.22 C ANISOU 1272 CG2 THR A 160 2099 1932 2133 -12 17 4 C ATOM 1273 N TRP A 161 -0.976 29.753 40.532 1.00 18.94 N ANISOU 1273 N TRP A 161 2462 2285 2448 -41 72 21 N ATOM 1274 CA TRP A 161 -1.734 29.198 39.408 1.00 20.87 C ANISOU 1274 CA TRP A 161 2711 2533 2687 -50 88 26 C ATOM 1275 C TRP A 161 -2.336 30.295 38.535 1.00 20.71 C ANISOU 1275 C TRP A 161 2681 2515 2671 -49 89 23 C ATOM 1276 O TRP A 161 -2.365 30.171 37.303 1.00 19.74 O ANISOU 1276 O TRP A 161 2556 2392 2552 -51 98 29 O ATOM 1277 CB TRP A 161 -2.831 28.263 39.919 1.00 26.49 C ANISOU 1277 CB TRP A 161 3431 3256 3377 -56 98 23 C ATOM 1278 CG TRP A 161 -2.340 26.900 40.299 1.00 30.46 C ANISOU 1278 CG TRP A 161 3943 3754 3876 -58 107 32 C ATOM 1279 CD1 TRP A 161 -1.818 26.520 41.505 1.00 27.91 C ANISOU 1279 CD1 TRP A 161 3626 3431 3547 -50 102 37 C ATOM 1280 CD2 TRP A 161 -2.327 25.732 39.471 1.00 24.06 C ANISOU 1280 CD2 TRP A 161 3137 2936 3068 -67 124 38 C ATOM 1281 NE1 TRP A 161 -1.479 25.191 41.474 1.00 26.23 N ANISOU 1281 NE1 TRP A 161 3422 3210 3334 -52 117 48 N ATOM 1282 CE2 TRP A 161 -1.781 24.684 40.236 1.00 27.17 C ANISOU 1282 CE2 TRP A 161 3541 3323 3461 -64 131 48 C ATOM 1283 CE3 TRP A 161 -2.723 25.471 38.155 1.00 25.99 C ANISOU 1283 CE3 TRP A 161 3379 3180 3314 -76 134 34 C ATOM 1284 CZ2 TRP A 161 -1.621 23.395 39.728 1.00 26.73 C ANISOU 1284 CZ2 TRP A 161 3491 3256 3410 -71 149 54 C ATOM 1285 CZ3 TRP A 161 -2.567 24.190 37.657 1.00 21.28 C ANISOU 1285 CZ3 TRP A 161 2789 2576 2722 -84 150 36 C ATOM 1286 CH2 TRP A 161 -2.021 23.170 38.442 1.00 26.90 C ANISOU 1286 CH2 TRP A 161 3508 3276 3435 -82 159 46 C ATOM 1287 N VAL A 162 -2.836 31.369 39.151 1.00 18.55 N ANISOU 1287 N VAL A 162 2403 2247 2399 -44 79 14 N ATOM 1288 CA VAL A 162 -3.441 32.458 38.386 1.00 19.04 C ANISOU 1288 CA VAL A 162 2456 2311 2467 -40 81 13 C ATOM 1289 C VAL A 162 -2.404 33.116 37.489 1.00 21.39 C ANISOU 1289 C VAL A 162 2745 2592 2790 -35 83 24 C ATOM 1290 O VAL A 162 -2.642 33.345 36.299 1.00 22.37 O ANISOU 1290 O VAL A 162 2866 2718 2915 -32 93 33 O ATOM 1291 CB VAL A 162 -4.094 33.484 39.329 1.00 20.82 C ANISOU 1291 CB VAL A 162 2677 2542 2692 -34 72 0 C ATOM 1292 CG1 VAL A 162 -4.467 34.744 38.566 1.00 26.96 C ANISOU 1292 CG1 VAL A 162 3444 3315 3483 -27 74 3 C ATOM 1293 CG2 VAL A 162 -5.317 32.881 39.994 1.00 21.68 C ANISOU 1293 CG2 VAL A 162 2794 2670 2776 -38 75 -7 C ATOM 1294 N MET A 163 -1.235 33.432 38.049 1.00 20.06 N ANISOU 1294 N MET A 163 2571 2407 2642 -32 74 22 N ATOM 1295 CA MET A 163 -0.180 34.043 37.245 1.00 22.29 C ANISOU 1295 CA MET A 163 2844 2670 2954 -28 78 33 C ATOM 1296 C MET A 163 0.323 33.090 36.168 1.00 18.21 C ANISOU 1296 C MET A 163 2333 2153 2434 -30 92 48 C ATOM 1297 O MET A 163 0.595 33.514 35.040 1.00 23.95 O ANISOU 1297 O MET A 163 3054 2872 3172 -25 103 62 O ATOM 1298 CB MET A 163 0.977 34.493 38.136 1.00 20.35 C ANISOU 1298 CB MET A 163 2590 2409 2734 -27 65 24 C ATOM 1299 CG MET A 163 0.600 35.565 39.145 1.00 24.92 C ANISOU 1299 CG MET A 163 3162 2987 3320 -23 51 5 C ATOM 1300 SD MET A 163 -0.176 37.005 38.386 1.00 25.91 S ANISOU 1300 SD MET A 163 3277 3104 3461 -18 62 9 S ATOM 1301 CE MET A 163 1.162 37.637 37.397 1.00 25.20 C ANISOU 1301 CE MET A 163 3173 2986 3416 -15 72 25 C ATOM 1302 N ALA A 164 0.480 31.806 36.495 1.00 17.96 N ANISOU 1302 N ALA A 164 2311 2127 2388 -36 92 47 N ATOM 1303 CA ALA A 164 1.030 30.878 35.514 1.00 17.62 C ANISOU 1303 CA ALA A 164 2272 2080 2343 -38 105 59 C ATOM 1304 C ALA A 164 0.067 30.669 34.352 1.00 20.49 C ANISOU 1304 C ALA A 164 2640 2458 2688 -39 117 62 C ATOM 1305 O ALA A 164 0.496 30.533 33.203 1.00 18.76 O ANISOU 1305 O ALA A 164 2419 2236 2472 -34 129 72 O ATOM 1306 CB ALA A 164 1.379 29.549 36.180 1.00 18.09 C ANISOU 1306 CB ALA A 164 2341 2139 2393 -44 104 58 C ATOM 1307 N LEU A 165 -1.238 30.644 34.629 1.00 18.91 N ANISOU 1307 N LEU A 165 2443 2276 2468 -42 115 51 N ATOM 1308 CA LEU A 165 -2.214 30.517 33.553 1.00 21.78 C ANISOU 1308 CA LEU A 165 2806 2657 2814 -41 123 50 C ATOM 1309 C LEU A 165 -2.316 31.801 32.738 1.00 20.78 C ANISOU 1309 C LEU A 165 2670 2531 2694 -28 126 60 C ATOM 1310 O LEU A 165 -2.618 31.749 31.541 1.00 24.72 O ANISOU 1310 O LEU A 165 3168 3044 3182 -21 135 66 O ATOM 1311 CB LEU A 165 -3.575 30.116 34.125 1.00 17.23 C ANISOU 1311 CB LEU A 165 2232 2098 2217 -49 120 35 C ATOM 1312 CG LEU A 165 -3.742 28.630 34.468 1.00 21.61 C ANISOU 1312 CG LEU A 165 2795 2653 2761 -62 126 28 C ATOM 1313 CD1 LEU A 165 -4.819 28.414 35.518 1.00 18.18 C ANISOU 1313 CD1 LEU A 165 2363 2229 2316 -69 123 16 C ATOM 1314 CD2 LEU A 165 -4.053 27.810 33.211 1.00 20.23 C ANISOU 1314 CD2 LEU A 165 2622 2489 2576 -66 137 23 C ATOM 1315 N ALA A 166 -2.047 32.956 33.356 1.00 21.40 N ANISOU 1315 N ALA A 166 2742 2597 2793 -23 119 62 N ATOM 1316 CA ALA A 166 -2.010 34.212 32.614 1.00 23.58 C ANISOU 1316 CA ALA A 166 3008 2868 3082 -9 126 75 C ATOM 1317 C ALA A 166 -0.906 34.230 31.566 1.00 18.99 C ANISOU 1317 C ALA A 166 2424 2275 2517 -1 139 94 C ATOM 1318 O ALA A 166 -0.977 35.020 30.619 1.00 19.59 O ANISOU 1318 O ALA A 166 2494 2351 2597 13 150 110 O ATOM 1319 CB ALA A 166 -1.826 35.386 33.575 1.00 21.60 C ANISOU 1319 CB ALA A 166 2749 2601 2857 -7 117 70 C ATOM 1320 N CYS A 167 0.112 33.386 31.723 1.00 19.30 N ANISOU 1320 N CYS A 167 2467 2302 2563 -8 139 95 N ATOM 1321 CA CYS A 167 1.196 33.229 30.762 1.00 22.74 C ANISOU 1321 CA CYS A 167 2902 2727 3013 -2 154 112 C ATOM 1322 C CYS A 167 0.982 32.051 29.819 1.00 20.74 C ANISOU 1322 C CYS A 167 2658 2491 2732 -2 163 112 C ATOM 1323 O CYS A 167 1.243 32.171 28.617 1.00 21.43 O ANISOU 1323 O CYS A 167 2744 2582 2815 10 177 126 O ATOM 1324 CB CYS A 167 2.525 33.060 31.513 1.00 21.30 C ANISOU 1324 CB CYS A 167 2715 2520 2859 -8 148 112 C ATOM 1325 SG CYS A 167 4.028 32.896 30.516 1.00 23.77 S ANISOU 1325 SG CYS A 167 3022 2815 3196 -1 167 133 S ATOM 1326 N ALA A 168 0.492 30.918 30.331 1.00 16.58 N ANISOU 1326 N ALA A 168 2140 1973 2186 -15 156 95 N ATOM 1327 CA ALA A 168 0.472 29.684 29.549 1.00 19.16 C ANISOU 1327 CA ALA A 168 2475 2311 2494 -18 165 91 C ATOM 1328 C ALA A 168 -0.762 29.550 28.662 1.00 21.66 C ANISOU 1328 C ALA A 168 2793 2657 2781 -14 167 82 C ATOM 1329 O ALA A 168 -0.696 28.879 27.625 1.00 21.83 O ANISOU 1329 O ALA A 168 2818 2688 2787 -11 177 80 O ATOM 1330 CB ALA A 168 0.567 28.476 30.483 1.00 20.72 C ANISOU 1330 CB ALA A 168 2680 2502 2690 -34 160 78 C ATOM 1331 N ALA A 169 -1.890 30.155 29.044 1.00 21.60 N ANISOU 1331 N ALA A 169 2780 2662 2763 -14 158 74 N ATOM 1332 CA ALA A 169 -3.166 29.939 28.358 1.00 23.98 C ANISOU 1332 CA ALA A 169 3081 2995 3037 -12 157 61 C ATOM 1333 C ALA A 169 -3.358 30.732 27.062 1.00 18.88 C ANISOU 1333 C ALA A 169 2429 2366 2377 9 164 75 C ATOM 1334 O ALA A 169 -3.903 30.175 26.101 1.00 18.82 O ANISOU 1334 O ALA A 169 2422 2385 2344 14 166 65 O ATOM 1335 CB ALA A 169 -4.334 30.233 29.304 1.00 17.37 C ANISOU 1335 CB ALA A 169 2240 2166 2194 -20 146 48 C ATOM 1336 N PRO A 170 -2.982 32.011 26.983 1.00 21.32 N ANISOU 1336 N PRO A 170 2732 2665 2702 24 168 97 N ATOM 1337 CA PRO A 170 -3.254 32.792 25.751 1.00 24.35 C ANISOU 1337 CA PRO A 170 3112 3068 3072 49 177 114 C ATOM 1338 C PRO A 170 -2.711 32.142 24.486 1.00 21.19 C ANISOU 1338 C PRO A 170 2716 2680 2655 60 189 120 C ATOM 1339 O PRO A 170 -3.369 32.228 23.437 1.00 26.05 O ANISOU 1339 O PRO A 170 3330 3327 3241 77 192 121 O ATOM 1340 CB PRO A 170 -2.566 34.138 26.030 1.00 28.18 C ANISOU 1340 CB PRO A 170 3590 3526 3590 60 184 139 C ATOM 1341 CG PRO A 170 -2.662 34.282 27.496 1.00 21.91 C ANISOU 1341 CG PRO A 170 2795 2714 2816 42 171 125 C ATOM 1342 CD PRO A 170 -2.485 32.889 28.063 1.00 20.22 C ANISOU 1342 CD PRO A 170 2590 2499 2595 21 163 104 C ATOM 1343 N PRO A 171 -1.532 31.500 24.505 1.00 22.82 N ANISOU 1343 N PRO A 171 2928 2864 2877 53 197 124 N ATOM 1344 CA PRO A 171 -1.070 30.813 23.279 1.00 18.59 C ANISOU 1344 CA PRO A 171 2398 2343 2323 64 210 126 C ATOM 1345 C PRO A 171 -1.970 29.674 22.817 1.00 20.24 C ANISOU 1345 C PRO A 171 2610 2581 2497 57 203 96 C ATOM 1346 O PRO A 171 -1.817 29.221 21.674 1.00 26.00 O ANISOU 1346 O PRO A 171 3343 3330 3204 70 211 94 O ATOM 1347 CB PRO A 171 0.322 30.293 23.661 1.00 20.51 C ANISOU 1347 CB PRO A 171 2645 2552 2594 54 218 133 C ATOM 1348 CG PRO A 171 0.778 31.224 24.717 1.00 22.58 C ANISOU 1348 CG PRO A 171 2901 2786 2891 48 214 145 C ATOM 1349 CD PRO A 171 -0.445 31.558 25.507 1.00 18.42 C ANISOU 1349 CD PRO A 171 2372 2271 2357 40 197 130 C ATOM 1350 N LEU A 172 -2.872 29.178 23.662 1.00 17.98 N ANISOU 1350 N LEU A 172 2323 2300 2209 37 188 71 N ATOM 1351 CA LEU A 172 -3.872 28.214 23.222 1.00 20.99 C ANISOU 1351 CA LEU A 172 2703 2709 2562 29 181 40 C ATOM 1352 C LEU A 172 -5.012 28.861 22.443 1.00 19.83 C ANISOU 1352 C LEU A 172 2547 2602 2386 48 174 37 C ATOM 1353 O LEU A 172 -5.687 28.164 21.679 1.00 19.99 O ANISOU 1353 O LEU A 172 2564 2652 2378 49 169 12 O ATOM 1354 CB LEU A 172 -4.458 27.458 24.423 1.00 17.48 C ANISOU 1354 CB LEU A 172 2258 2253 2129 2 172 17 C ATOM 1355 CG LEU A 172 -3.571 26.500 25.227 1.00 18.73 C ANISOU 1355 CG LEU A 172 2427 2379 2311 -18 177 14 C ATOM 1356 CD1 LEU A 172 -4.273 26.071 26.521 1.00 22.43 C ANISOU 1356 CD1 LEU A 172 2894 2838 2790 -39 170 -1 C ATOM 1357 CD2 LEU A 172 -3.197 25.283 24.399 1.00 25.62 C ANISOU 1357 CD2 LEU A 172 3305 3255 3176 -21 187 -2 C ATOM 1358 N VAL A 173 -5.251 30.164 22.620 1.00 18.88 N ANISOU 1358 N VAL A 173 2421 2482 2271 63 173 59 N ATOM 1359 CA VAL A 173 -6.493 30.771 22.148 1.00 21.11 C ANISOU 1359 CA VAL A 173 2693 2800 2527 78 163 55 C ATOM 1360 C VAL A 173 -6.290 32.052 21.340 1.00 22.02 C ANISOU 1360 C VAL A 173 2805 2926 2636 112 174 90 C ATOM 1361 O VAL A 173 -7.224 32.851 21.200 1.00 20.99 O ANISOU 1361 O VAL A 173 2666 2818 2493 127 167 96 O ATOM 1362 CB VAL A 173 -7.443 31.042 23.331 1.00 19.76 C ANISOU 1362 CB VAL A 173 2515 2624 2368 62 150 43 C ATOM 1363 CG1 VAL A 173 -7.883 29.727 23.974 1.00 23.04 C ANISOU 1363 CG1 VAL A 173 2932 3037 2786 32 143 9 C ATOM 1364 CG2 VAL A 173 -6.780 31.948 24.361 1.00 23.34 C ANISOU 1364 CG2 VAL A 173 2971 3041 2856 59 154 66 C ATOM 1365 N GLY A 174 -5.092 32.274 20.806 1.00 19.63 N ANISOU 1365 N GLY A 174 2510 2607 2343 125 191 116 N ATOM 1366 CA GLY A 174 -4.912 33.283 19.775 1.00 23.99 C ANISOU 1366 CA GLY A 174 3059 3173 2883 161 205 149 C ATOM 1367 C GLY A 174 -3.925 34.398 20.056 1.00 23.50 C ANISOU 1367 C GLY A 174 2997 3073 2859 170 223 187 C ATOM 1368 O GLY A 174 -3.708 35.230 19.167 1.00 24.18 O ANISOU 1368 O GLY A 174 3081 3167 2938 202 240 219 O ATOM 1369 N TRP A 175 -3.327 34.500 21.243 1.00 26.14 N ANISOU 1369 N TRP A 175 3332 3366 3234 146 221 186 N ATOM 1370 CA TRP A 175 -2.248 35.455 21.484 1.00 23.54 C ANISOU 1370 CA TRP A 175 3000 2998 2946 152 238 216 C ATOM 1371 C TRP A 175 -0.955 34.653 21.546 1.00 24.75 C ANISOU 1371 C TRP A 175 3159 3126 3117 139 246 215 C ATOM 1372 O TRP A 175 -0.742 33.885 22.491 1.00 19.70 O ANISOU 1372 O TRP A 175 2522 2471 2490 112 234 192 O ATOM 1373 CB TRP A 175 -2.475 36.259 22.761 1.00 24.13 C ANISOU 1373 CB TRP A 175 3068 3046 3055 138 229 213 C ATOM 1374 CG TRP A 175 -1.587 37.467 22.880 1.00 21.10 C ANISOU 1374 CG TRP A 175 2677 2625 2714 148 247 244 C ATOM 1375 CD1 TRP A 175 -0.912 38.097 21.874 1.00 23.59 C ANISOU 1375 CD1 TRP A 175 2990 2934 3038 174 273 279 C ATOM 1376 CD2 TRP A 175 -1.276 38.181 24.080 1.00 24.20 C ANISOU 1376 CD2 TRP A 175 3063 2982 3150 133 242 240 C ATOM 1377 NE1 TRP A 175 -0.206 39.166 22.374 1.00 20.95 N ANISOU 1377 NE1 TRP A 175 2646 2559 2754 173 286 297 N ATOM 1378 CE2 TRP A 175 -0.413 39.238 23.727 1.00 21.52 C ANISOU 1378 CE2 TRP A 175 2715 2613 2848 148 265 271 C ATOM 1379 CE3 TRP A 175 -1.650 38.032 25.418 1.00 20.55 C ANISOU 1379 CE3 TRP A 175 2600 2510 2698 109 221 212 C ATOM 1380 CZ2 TRP A 175 0.087 40.138 24.667 1.00 20.56 C ANISOU 1380 CZ2 TRP A 175 2584 2453 2777 138 266 272 C ATOM 1381 CZ3 TRP A 175 -1.151 38.928 26.351 1.00 23.44 C ANISOU 1381 CZ3 TRP A 175 2957 2841 3108 102 221 213 C ATOM 1382 CH2 TRP A 175 -0.296 39.966 25.972 1.00 21.74 C ANISOU 1382 CH2 TRP A 175 2733 2596 2932 115 242 240 C ATOM 1383 N SER A 176 -0.105 34.832 20.532 1.00 17.25 N ANISOU 1383 N SER A 176 2211 2175 2168 160 269 242 N ATOM 1384 CA SER A 176 1.013 33.937 20.254 1.00 22.78 C ANISOU 1384 CA SER A 176 2918 2862 2875 153 279 241 C ATOM 1385 C SER A 176 0.500 32.528 19.980 1.00 23.30 C ANISOU 1385 C SER A 176 2993 2957 2904 143 266 207 C ATOM 1386 O SER A 176 -0.692 32.331 19.723 1.00 20.97 O ANISOU 1386 O SER A 176 2698 2696 2574 146 253 189 O ATOM 1387 CB SER A 176 2.026 33.920 21.402 1.00 19.77 C ANISOU 1387 CB SER A 176 2533 2437 2542 130 277 239 C ATOM 1388 OG SER A 176 3.132 33.094 21.073 1.00 18.66 O ANISOU 1388 OG SER A 176 2397 2284 2408 126 288 241 O ATOM 1389 N ARG A 177 1.395 31.547 20.033 1.00 21.95 N ANISOU 1389 N ARG A 177 2828 2771 2742 130 271 198 N ATOM 1390 CA ARG A 177 1.076 30.162 19.714 1.00 19.95 C ANISOU 1390 CA ARG A 177 2582 2537 2459 120 264 167 C ATOM 1391 C ARG A 177 2.251 29.300 20.148 1.00 20.55 C ANISOU 1391 C ARG A 177 2664 2583 2562 103 270 164 C ATOM 1392 O ARG A 177 3.382 29.780 20.262 1.00 19.44 O ANISOU 1392 O ARG A 177 2520 2413 2452 107 284 189 O ATOM 1393 CB ARG A 177 0.801 29.979 18.215 1.00 22.58 C ANISOU 1393 CB ARG A 177 2919 2910 2749 147 274 169 C ATOM 1394 CG ARG A 177 1.993 30.352 17.322 1.00 22.13 C ANISOU 1394 CG ARG A 177 2865 2843 2700 171 301 203 C ATOM 1395 CD ARG A 177 1.666 30.213 15.843 1.00 25.59 C ANISOU 1395 CD ARG A 177 3307 3326 3089 203 311 205 C ATOM 1396 NE ARG A 177 2.776 30.640 14.996 1.00 18.80 N ANISOU 1396 NE ARG A 177 2450 2457 2236 229 341 242 N ATOM 1397 CZ ARG A 177 2.755 30.607 13.672 1.00 24.47 C ANISOU 1397 CZ ARG A 177 3173 3211 2913 262 356 252 C ATOM 1398 NH1 ARG A 177 1.699 30.162 13.010 1.00 22.05 N ANISOU 1398 NH1 ARG A 177 2869 2954 2557 273 341 224 N ATOM 1399 NH2 ARG A 177 3.818 31.032 12.995 1.00 25.71 N ANISOU 1399 NH2 ARG A 177 3331 3356 3081 285 386 289 N ATOM 1400 N TYR A 178 1.976 28.020 20.381 1.00 16.75 N ANISOU 1400 N TYR A 178 2189 2106 2069 84 261 132 N ATOM 1401 CA TYR A 178 3.036 27.058 20.643 1.00 21.22 C ANISOU 1401 CA TYR A 178 2761 2646 2655 72 269 129 C ATOM 1402 C TYR A 178 3.521 26.467 19.327 1.00 19.03 C ANISOU 1402 C TYR A 178 2490 2384 2356 89 287 129 C ATOM 1403 O TYR A 178 2.721 26.131 18.451 1.00 18.59 O ANISOU 1403 O TYR A 178 2437 2364 2263 99 285 111 O ATOM 1404 CB TYR A 178 2.564 25.947 21.579 1.00 17.78 C ANISOU 1404 CB TYR A 178 2328 2203 2222 44 256 98 C ATOM 1405 CG TYR A 178 2.296 26.433 22.981 1.00 17.60 C ANISOU 1405 CG TYR A 178 2301 2162 2222 28 240 100 C ATOM 1406 CD1 TYR A 178 3.339 26.844 23.801 1.00 17.89 C ANISOU 1406 CD1 TYR A 178 2335 2168 2295 24 242 118 C ATOM 1407 CD2 TYR A 178 0.999 26.489 23.485 1.00 22.12 C ANISOU 1407 CD2 TYR A 178 2871 2752 2781 18 224 81 C ATOM 1408 CE1 TYR A 178 3.102 27.296 25.087 1.00 21.47 C ANISOU 1408 CE1 TYR A 178 2783 2608 2765 12 226 117 C ATOM 1409 CE2 TYR A 178 0.751 26.937 24.775 1.00 21.25 C ANISOU 1409 CE2 TYR A 178 2757 2627 2689 6 212 82 C ATOM 1410 CZ TYR A 178 1.809 27.342 25.570 1.00 23.17 C ANISOU 1410 CZ TYR A 178 2998 2840 2964 3 212 99 C ATOM 1411 OH TYR A 178 1.577 27.796 26.849 1.00 19.83 O ANISOU 1411 OH TYR A 178 2572 2406 2556 -7 199 97 O ATOM 1412 N ILE A 179 4.837 26.347 19.198 1.00 18.85 N ANISOU 1412 N ILE A 179 2468 2336 2357 93 305 148 N ATOM 1413 CA ILE A 179 5.458 25.942 17.939 1.00 19.70 C ANISOU 1413 CA ILE A 179 2581 2456 2447 114 326 155 C ATOM 1414 C ILE A 179 6.633 25.017 18.250 1.00 18.08 C ANISOU 1414 C ILE A 179 2380 2221 2269 102 336 154 C ATOM 1415 O ILE A 179 7.326 25.220 19.260 1.00 24.78 O ANISOU 1415 O ILE A 179 3222 3036 3155 89 333 166 O ATOM 1416 CB ILE A 179 5.876 27.186 17.134 1.00 19.08 C ANISOU 1416 CB ILE A 179 2498 2384 2368 143 344 193 C ATOM 1417 CG1 ILE A 179 6.185 26.849 15.674 1.00 19.94 C ANISOU 1417 CG1 ILE A 179 2615 2519 2444 171 365 198 C ATOM 1418 CG2 ILE A 179 7.047 27.905 17.800 1.00 20.17 C ANISOU 1418 CG2 ILE A 179 2626 2480 2556 139 354 223 C ATOM 1419 CD1 ILE A 179 6.568 28.075 14.863 1.00 19.00 C ANISOU 1419 CD1 ILE A 179 2491 2405 2324 203 387 240 C ATOM 1420 N PRO A 180 6.878 23.980 17.451 1.00 24.39 N ANISOU 1420 N PRO A 180 3188 3029 3049 107 348 138 N ATOM 1421 CA PRO A 180 8.006 23.088 17.739 1.00 18.51 C ANISOU 1421 CA PRO A 180 2446 2254 2331 98 360 138 C ATOM 1422 C PRO A 180 9.336 23.810 17.605 1.00 20.03 C ANISOU 1422 C PRO A 180 2632 2425 2555 112 379 177 C ATOM 1423 O PRO A 180 9.463 24.790 16.864 1.00 17.41 O ANISOU 1423 O PRO A 180 2295 2103 2215 135 392 202 O ATOM 1424 CB PRO A 180 7.866 21.983 16.687 1.00 17.91 C ANISOU 1424 CB PRO A 180 2381 2199 2224 106 370 112 C ATOM 1425 CG PRO A 180 6.458 22.051 16.229 1.00 21.11 C ANISOU 1425 CG PRO A 180 2788 2644 2590 108 355 86 C ATOM 1426 CD PRO A 180 6.084 23.499 16.306 1.00 20.39 C ANISOU 1426 CD PRO A 180 2689 2563 2497 121 349 113 C ATOM 1427 N GLU A 181 10.334 23.314 18.340 1.00 17.78 N ANISOU 1427 N GLU A 181 2343 2106 2306 100 382 182 N ATOM 1428 CA GLU A 181 11.655 23.928 18.381 1.00 17.24 C ANISOU 1428 CA GLU A 181 2264 2012 2274 109 398 215 C ATOM 1429 C GLU A 181 12.738 22.882 18.162 1.00 17.30 C ANISOU 1429 C GLU A 181 2275 2002 2296 110 416 215 C ATOM 1430 O GLU A 181 12.539 21.690 18.408 1.00 17.26 O ANISOU 1430 O GLU A 181 2280 1996 2284 97 411 189 O ATOM 1431 CB GLU A 181 11.922 24.634 19.723 1.00 20.23 C ANISOU 1431 CB GLU A 181 2629 2364 2692 93 381 225 C ATOM 1432 CG GLU A 181 10.807 25.551 20.222 1.00 21.30 C ANISOU 1432 CG GLU A 181 2762 2513 2818 87 361 221 C ATOM 1433 CD GLU A 181 11.302 26.518 21.281 1.00 20.85 C ANISOU 1433 CD GLU A 181 2688 2430 2803 79 351 236 C ATOM 1434 OE1 GLU A 181 11.966 27.500 20.904 1.00 17.49 O ANISOU 1434 OE1 GLU A 181 2251 1993 2401 92 366 262 O ATOM 1435 OE2 GLU A 181 11.051 26.288 22.489 1.00 26.17 O ANISOU 1435 OE2 GLU A 181 3361 3095 3487 60 328 220 O ATOM 1436 N GLY A 182 13.898 23.351 17.697 1.00 21.11 N ANISOU 1436 N GLY A 182 2749 2471 2803 125 438 244 N ATOM 1437 CA GLY A 182 15.077 22.494 17.646 1.00 17.51 C ANISOU 1437 CA GLY A 182 2292 1993 2369 126 454 248 C ATOM 1438 C GLY A 182 14.924 21.393 16.618 1.00 20.36 C ANISOU 1438 C GLY A 182 2669 2372 2696 136 470 229 C ATOM 1439 O GLY A 182 14.665 21.648 15.438 1.00 20.69 O ANISOU 1439 O GLY A 182 2717 2439 2705 158 486 232 O ATOM 1440 N MET A 183 15.112 20.151 17.058 1.00 17.64 N ANISOU 1440 N MET A 183 2331 2014 2358 123 467 208 N ATOM 1441 CA MET A 183 14.877 18.960 16.246 1.00 17.81 C ANISOU 1441 CA MET A 183 2367 2048 2351 127 480 181 C ATOM 1442 C MET A 183 13.364 18.662 16.046 1.00 20.07 C ANISOU 1442 C MET A 183 2665 2364 2597 119 462 145 C ATOM 1443 O MET A 183 13.026 17.591 15.517 1.00 20.24 O ANISOU 1443 O MET A 183 2698 2395 2598 118 468 114 O ATOM 1444 CB MET A 183 15.586 17.757 16.876 1.00 17.78 C ANISOU 1444 CB MET A 183 2366 2015 2376 115 484 172 C ATOM 1445 CG MET A 183 17.106 17.771 16.704 1.00 17.89 C ANISOU 1445 CG MET A 183 2370 2006 2423 128 507 201 C ATOM 1446 SD MET A 183 17.970 16.470 17.611 1.00 22.25 S ANISOU 1446 SD MET A 183 2920 2522 3010 116 510 197 S ATOM 1447 CE MET A 183 17.014 15.038 17.144 1.00 17.97 C ANISOU 1447 CE MET A 183 2401 1991 2437 108 513 152 C ATOM 1448 N GLN A 184 12.522 19.605 16.485 1.00 19.60 N ANISOU 1448 N GLN A 184 2600 2317 2530 114 442 149 N ATOM 1449 CA GLN A 184 11.070 19.612 16.299 1.00 19.02 C ANISOU 1449 CA GLN A 184 2532 2275 2421 108 424 121 C ATOM 1450 C GLN A 184 10.340 18.594 17.173 1.00 19.76 C ANISOU 1450 C GLN A 184 2630 2358 2518 81 407 88 C ATOM 1451 O GLN A 184 9.174 18.280 16.910 1.00 24.13 O ANISOU 1451 O GLN A 184 3188 2937 3044 75 396 57 O ATOM 1452 CB GLN A 184 10.685 19.396 14.827 1.00 18.60 C ANISOU 1452 CB GLN A 184 2488 2258 2322 130 436 105 C ATOM 1453 CG GLN A 184 11.429 20.288 13.818 1.00 18.25 C ANISOU 1453 CG GLN A 184 2441 2224 2269 162 459 140 C ATOM 1454 CD GLN A 184 11.105 21.760 13.968 1.00 18.94 C ANISOU 1454 CD GLN A 184 2519 2320 2358 171 452 170 C ATOM 1455 OE1 GLN A 184 9.994 22.192 13.678 1.00 22.32 O ANISOU 1455 OE1 GLN A 184 2948 2780 2753 176 438 159 O ATOM 1456 NE2 GLN A 184 12.080 22.541 14.428 1.00 22.66 N ANISOU 1456 NE2 GLN A 184 2979 2762 2869 173 462 207 N ATOM 1457 N CYS A 185 10.971 18.064 18.219 1.00 17.42 N ANISOU 1457 N CYS A 185 2332 2029 2258 66 406 94 N ATOM 1458 CA CYS A 185 10.313 17.087 19.079 1.00 19.62 C ANISOU 1458 CA CYS A 185 2614 2295 2543 42 395 68 C ATOM 1459 C CYS A 185 9.885 17.670 20.423 1.00 20.37 C ANISOU 1459 C CYS A 185 2704 2382 2655 27 373 77 C ATOM 1460 O CYS A 185 9.469 16.917 21.307 1.00 23.76 O ANISOU 1460 O CYS A 185 3135 2798 3094 9 366 63 O ATOM 1461 CB CYS A 185 11.216 15.870 19.282 1.00 21.16 C ANISOU 1461 CB CYS A 185 2815 2462 2764 38 412 65 C ATOM 1462 SG CYS A 185 11.454 14.878 17.775 1.00 22.33 S ANISOU 1462 SG CYS A 185 2974 2620 2891 52 437 40 S ATOM 1463 N SER A 186 9.961 18.991 20.588 1.00 19.97 N ANISOU 1463 N SER A 186 2643 2338 2606 34 364 101 N ATOM 1464 CA SER A 186 9.400 19.676 21.746 1.00 19.74 C ANISOU 1464 CA SER A 186 2608 2306 2586 22 342 106 C ATOM 1465 C SER A 186 8.860 21.024 21.290 1.00 19.65 C ANISOU 1465 C SER A 186 2591 2317 2558 33 334 116 C ATOM 1466 O SER A 186 9.224 21.523 20.224 1.00 24.03 O ANISOU 1466 O SER A 186 3144 2883 3102 53 348 129 O ATOM 1467 CB SER A 186 10.434 19.860 22.864 1.00 21.29 C ANISOU 1467 CB SER A 186 2796 2473 2819 18 337 128 C ATOM 1468 OG SER A 186 11.478 20.727 22.453 1.00 25.96 O ANISOU 1468 OG SER A 186 3378 3058 3428 33 347 155 O ATOM 1469 N CYS A 187 7.985 21.620 22.106 1.00 21.03 N ANISOU 1469 N CYS A 187 2762 2498 2731 23 314 112 N ATOM 1470 CA CYS A 187 7.270 22.827 21.706 1.00 26.97 C ANISOU 1470 CA CYS A 187 3508 3272 3466 33 307 119 C ATOM 1471 C CYS A 187 7.417 23.938 22.741 1.00 22.27 C ANISOU 1471 C CYS A 187 2902 2663 2895 29 294 137 C ATOM 1472 O CYS A 187 7.544 23.685 23.941 1.00 24.83 O ANISOU 1472 O CYS A 187 3226 2970 3239 14 282 133 O ATOM 1473 CB CYS A 187 5.778 22.536 21.466 1.00 21.98 C ANISOU 1473 CB CYS A 187 2882 2670 2802 26 296 90 C ATOM 1474 SG CYS A 187 5.461 21.760 19.865 1.00 22.34 S ANISOU 1474 SG CYS A 187 2934 2744 2809 40 310 68 S ATOM 1475 N GLY A 188 7.402 25.179 22.251 1.00 21.17 N ANISOU 1475 N GLY A 188 2756 2532 2756 44 297 156 N ATOM 1476 CA GLY A 188 7.465 26.364 23.089 1.00 23.96 C ANISOU 1476 CA GLY A 188 3098 2872 3133 42 286 170 C ATOM 1477 C GLY A 188 6.843 27.585 22.432 1.00 22.24 C ANISOU 1477 C GLY A 188 2876 2672 2903 58 289 183 C ATOM 1478 O GLY A 188 6.118 27.462 21.440 1.00 21.26 O ANISOU 1478 O GLY A 188 2757 2576 2744 70 295 178 O ATOM 1479 N ILE A 189 7.123 28.771 22.980 1.00 20.85 N ANISOU 1479 N ILE A 189 2688 2479 2756 60 286 200 N ATOM 1480 CA ILE A 189 6.552 30.008 22.454 1.00 20.89 C ANISOU 1480 CA ILE A 189 2687 2496 2754 76 291 216 C ATOM 1481 C ILE A 189 7.232 30.385 21.140 1.00 22.67 C ANISOU 1481 C ILE A 189 2911 2723 2978 100 319 244 C ATOM 1482 O ILE A 189 8.429 30.147 20.940 1.00 20.83 O ANISOU 1482 O ILE A 189 2675 2471 2770 103 334 257 O ATOM 1483 CB ILE A 189 6.677 31.129 23.502 1.00 22.25 C ANISOU 1483 CB ILE A 189 2847 2646 2963 68 281 222 C ATOM 1484 CG1 ILE A 189 5.682 30.893 24.636 1.00 21.90 C ANISOU 1484 CG1 ILE A 189 2806 2608 2907 50 255 196 C ATOM 1485 CG2 ILE A 189 6.458 32.506 22.889 1.00 18.98 C ANISOU 1485 CG2 ILE A 189 2423 2231 2555 88 294 247 C ATOM 1486 CD1 ILE A 189 4.245 30.777 24.154 1.00 18.86 C ANISOU 1486 CD1 ILE A 189 2428 2258 2481 55 249 184 C ATOM 1487 N ASP A 190 6.456 30.979 20.231 1.00 19.20 N ANISOU 1487 N ASP A 190 2474 2310 2511 121 326 254 N ATOM 1488 CA ASP A 190 6.944 31.377 18.910 1.00 23.48 C ANISOU 1488 CA ASP A 190 3016 2861 3043 150 355 283 C ATOM 1489 C ASP A 190 7.823 32.620 19.033 1.00 20.30 C ANISOU 1489 C ASP A 190 2599 2426 2689 158 373 317 C ATOM 1490 O ASP A 190 7.321 33.744 19.080 1.00 19.32 O ANISOU 1490 O ASP A 190 2468 2300 2573 168 375 332 O ATOM 1491 CB ASP A 190 5.765 31.637 17.979 1.00 18.24 C ANISOU 1491 CB ASP A 190 2359 2240 2332 172 354 283 C ATOM 1492 CG ASP A 190 6.190 31.864 16.537 1.00 24.43 C ANISOU 1492 CG ASP A 190 3146 3042 3095 206 384 311 C ATOM 1493 OD1 ASP A 190 7.379 32.155 16.289 1.00 21.95 O ANISOU 1493 OD1 ASP A 190 2827 2702 2813 214 408 338 O ATOM 1494 OD2 ASP A 190 5.325 31.751 15.648 1.00 20.61 O ANISOU 1494 OD2 ASP A 190 2669 2600 2563 226 382 306 O ATOM 1495 N TYR A 191 9.143 32.423 19.068 1.00 18.37 N ANISOU 1495 N TYR A 191 2348 2153 2479 155 388 330 N ATOM 1496 CA TYR A 191 10.100 33.520 18.967 1.00 20.43 C ANISOU 1496 CA TYR A 191 2592 2382 2788 165 412 363 C ATOM 1497 C TYR A 191 10.609 33.728 17.547 1.00 22.96 C ANISOU 1497 C TYR A 191 2915 2712 3098 196 448 397 C ATOM 1498 O TYR A 191 11.475 34.582 17.332 1.00 27.75 O ANISOU 1498 O TYR A 191 3507 3289 3747 206 474 428 O ATOM 1499 CB TYR A 191 11.314 33.279 19.878 1.00 27.88 C ANISOU 1499 CB TYR A 191 3522 3288 3782 144 407 357 C ATOM 1500 CG TYR A 191 11.031 32.515 21.150 1.00 19.39 C ANISOU 1500 CG TYR A 191 2451 2211 2706 116 373 322 C ATOM 1501 CD1 TYR A 191 10.467 33.141 22.246 1.00 21.09 C ANISOU 1501 CD1 TYR A 191 2659 2418 2935 101 350 307 C ATOM 1502 CD2 TYR A 191 11.350 31.166 21.254 1.00 24.38 C ANISOU 1502 CD2 TYR A 191 3093 2849 3323 106 366 304 C ATOM 1503 CE1 TYR A 191 10.216 32.444 23.409 1.00 19.13 C ANISOU 1503 CE1 TYR A 191 2415 2170 2684 79 321 278 C ATOM 1504 CE2 TYR A 191 11.097 30.460 22.408 1.00 21.19 C ANISOU 1504 CE2 TYR A 191 2692 2442 2917 84 339 276 C ATOM 1505 CZ TYR A 191 10.532 31.106 23.484 1.00 21.97 C ANISOU 1505 CZ TYR A 191 2784 2536 3027 71 317 264 C ATOM 1506 OH TYR A 191 10.281 30.414 24.647 1.00 27.19 O ANISOU 1506 OH TYR A 191 3449 3196 3685 51 291 238 O ATOM 1507 N TYR A 192 10.093 32.973 16.580 1.00 25.02 N ANISOU 1507 N TYR A 192 3192 3010 3303 212 452 390 N ATOM 1508 CA TYR A 192 10.737 32.810 15.282 1.00 21.17 C ANISOU 1508 CA TYR A 192 2710 2534 2800 241 485 416 C ATOM 1509 C TYR A 192 10.114 33.636 14.166 1.00 20.53 C ANISOU 1509 C TYR A 192 2632 2482 2686 277 505 445 C ATOM 1510 O TYR A 192 10.838 34.091 13.274 1.00 21.50 O ANISOU 1510 O TYR A 192 2752 2599 2817 304 541 483 O ATOM 1511 CB TYR A 192 10.719 31.328 14.888 1.00 22.77 C ANISOU 1511 CB TYR A 192 2928 2761 2963 237 478 387 C ATOM 1512 CG TYR A 192 11.337 30.427 15.937 1.00 20.00 C ANISOU 1512 CG TYR A 192 2575 2383 2643 205 461 362 C ATOM 1513 CD1 TYR A 192 12.694 30.134 15.918 1.00 24.43 C ANISOU 1513 CD1 TYR A 192 3128 2915 3239 203 480 376 C ATOM 1514 CD2 TYR A 192 10.567 29.872 16.945 1.00 22.06 C ANISOU 1514 CD2 TYR A 192 2839 2647 2896 178 427 326 C ATOM 1515 CE1 TYR A 192 13.268 29.315 16.885 1.00 17.97 C ANISOU 1515 CE1 TYR A 192 2307 2074 2447 177 464 355 C ATOM 1516 CE2 TYR A 192 11.131 29.048 17.912 1.00 21.36 C ANISOU 1516 CE2 TYR A 192 2748 2534 2832 152 413 307 C ATOM 1517 CZ TYR A 192 12.479 28.776 17.875 1.00 18.86 C ANISOU 1517 CZ TYR A 192 2425 2191 2549 153 431 321 C ATOM 1518 OH TYR A 192 13.039 27.962 18.832 1.00 20.83 O ANISOU 1518 OH TYR A 192 2672 2420 2822 131 417 304 O ATOM 1519 N THR A 193 8.801 33.853 14.189 1.00 21.36 N ANISOU 1519 N THR A 193 2744 2619 2755 281 485 431 N ATOM 1520 CA THR A 193 8.093 34.466 13.078 1.00 23.53 C ANISOU 1520 CA THR A 193 3024 2930 2988 319 500 455 C ATOM 1521 C THR A 193 7.286 35.664 13.546 1.00 25.69 C ANISOU 1521 C THR A 193 3288 3198 3275 322 492 468 C ATOM 1522 O THR A 193 6.895 35.728 14.712 1.00 21.67 O ANISOU 1522 O THR A 193 2774 2672 2789 292 466 443 O ATOM 1523 CB THR A 193 7.143 33.461 12.407 1.00 27.11 C ANISOU 1523 CB THR A 193 3492 3438 3371 328 481 423 C ATOM 1524 OG1 THR A 193 6.024 33.199 13.269 1.00 26.26 O ANISOU 1524 OG1 THR A 193 3384 3341 3252 303 444 385 O ATOM 1525 CG2 THR A 193 7.861 32.154 12.111 1.00 23.47 C ANISOU 1525 CG2 THR A 193 3040 2978 2899 320 485 401 C ATOM 1526 N PRO A 194 7.009 36.626 12.654 1.00 26.27 N ANISOU 1526 N PRO A 194 3360 3287 3333 360 517 507 N ATOM 1527 CA PRO A 194 6.139 37.760 13.024 1.00 27.31 C ANISOU 1527 CA PRO A 194 3484 3417 3476 366 511 519 C ATOM 1528 C PRO A 194 4.708 37.333 13.301 1.00 25.37 C ANISOU 1528 C PRO A 194 3244 3211 3182 358 474 482 C ATOM 1529 O PRO A 194 4.141 37.689 14.340 1.00 26.88 O ANISOU 1529 O PRO A 194 3429 3387 3396 335 451 464 O ATOM 1530 CB PRO A 194 6.201 38.675 11.792 1.00 26.52 C ANISOU 1530 CB PRO A 194 3384 3332 3361 415 550 572 C ATOM 1531 CG PRO A 194 7.423 38.230 11.060 1.00 29.38 C ANISOU 1531 CG PRO A 194 3750 3686 3729 427 581 592 C ATOM 1532 CD PRO A 194 7.548 36.769 11.301 1.00 25.25 C ANISOU 1532 CD PRO A 194 3236 3176 3182 400 555 545 C ATOM 1533 N HIS A 195 4.121 36.599 12.354 1.00 27.59 N ANISOU 1533 N HIS A 195 3538 3546 3400 378 467 468 N ATOM 1534 CA HIS A 195 2.761 36.072 12.403 1.00 28.45 C ANISOU 1534 CA HIS A 195 3651 3700 3459 374 433 430 C ATOM 1535 C HIS A 195 1.754 37.036 13.024 1.00 25.86 C ANISOU 1535 C HIS A 195 3314 3370 3141 373 419 434 C ATOM 1536 O HIS A 195 1.231 36.755 14.105 1.00 19.18 O ANISOU 1536 O HIS A 195 2465 2514 2310 339 390 400 O ATOM 1537 CB HIS A 195 2.691 34.749 13.157 1.00 22.79 C ANISOU 1537 CB HIS A 195 2939 2979 2741 334 404 378 C ATOM 1538 CG HIS A 195 1.553 33.889 12.707 1.00 26.87 C ANISOU 1538 CG HIS A 195 3461 3550 3199 336 378 339 C ATOM 1539 ND1 HIS A 195 0.479 33.581 13.513 1.00 25.05 N ANISOU 1539 ND1 HIS A 195 3227 3329 2963 311 346 302 N ATOM 1540 CD2 HIS A 195 1.308 33.301 11.511 1.00 25.32 C ANISOU 1540 CD2 HIS A 195 3273 3401 2947 363 381 330 C ATOM 1541 CE1 HIS A 195 -0.366 32.817 12.844 1.00 26.71 C ANISOU 1541 CE1 HIS A 195 3441 3588 3120 320 330 270 C ATOM 1542 NE2 HIS A 195 0.115 32.630 11.628 1.00 28.74 N ANISOU 1542 NE2 HIS A 195 3704 3870 3345 351 349 285 N ATOM 1543 N GLU A 196 1.483 38.162 12.356 1.00 22.46 N ANISOU 1543 N GLU A 196 2880 2951 2704 411 441 476 N ATOM 1544 CA GLU A 196 0.670 39.229 12.941 1.00 29.03 C ANISOU 1544 CA GLU A 196 3701 3773 3554 413 434 486 C ATOM 1545 C GLU A 196 -0.744 38.787 13.331 1.00 26.15 C ANISOU 1545 C GLU A 196 3337 3447 3153 401 395 445 C ATOM 1546 O GLU A 196 -1.392 39.473 14.128 1.00 26.54 O ANISOU 1546 O GLU A 196 3378 3483 3224 391 383 442 O ATOM 1547 CB GLU A 196 0.592 40.409 11.966 1.00 29.75 C ANISOU 1547 CB GLU A 196 3790 3877 3638 463 467 542 C ATOM 1548 CG GLU A 196 1.897 41.196 11.803 1.00 35.19 C ANISOU 1548 CG GLU A 196 4474 4516 4382 473 510 589 C ATOM 1549 CD GLU A 196 2.836 40.630 10.744 1.00 40.87 C ANISOU 1549 CD GLU A 196 5202 5247 5080 494 537 608 C ATOM 1550 OE1 GLU A 196 2.651 39.469 10.315 1.00 41.67 O ANISOU 1550 OE1 GLU A 196 5315 5389 5131 492 518 576 O ATOM 1551 OE2 GLU A 196 3.772 41.354 10.340 1.00 44.09 O ANISOU 1551 OE2 GLU A 196 5606 5623 5524 513 578 655 O ATOM 1552 N GLU A 197 -1.244 37.681 12.774 1.00 27.85 N ANISOU 1552 N GLU A 197 3558 3709 3313 402 376 411 N ATOM 1553 CA GLU A 197 -2.574 37.197 13.135 1.00 27.33 C ANISOU 1553 CA GLU A 197 3489 3678 3216 388 340 369 C ATOM 1554 C GLU A 197 -2.692 36.895 14.626 1.00 27.54 C ANISOU 1554 C GLU A 197 3513 3668 3284 340 318 337 C ATOM 1555 O GLU A 197 -3.769 37.071 15.207 1.00 23.69 O ANISOU 1555 O GLU A 197 3018 3192 2791 330 296 318 O ATOM 1556 CB GLU A 197 -2.910 35.943 12.324 1.00 31.39 C ANISOU 1556 CB GLU A 197 4010 4242 3675 393 325 333 C ATOM 1557 CG GLU A 197 -4.281 35.351 12.620 1.00 39.63 C ANISOU 1557 CG GLU A 197 5048 5323 4688 377 288 286 C ATOM 1558 CD GLU A 197 -4.564 34.083 11.835 1.00 50.25 C ANISOU 1558 CD GLU A 197 6397 6713 5984 379 274 245 C ATOM 1559 OE1 GLU A 197 -3.761 33.128 11.922 1.00 53.90 O ANISOU 1559 OE1 GLU A 197 6867 7155 6457 357 278 226 O ATOM 1560 OE2 GLU A 197 -5.592 34.045 11.127 1.00 56.78 O ANISOU 1560 OE2 GLU A 197 7216 7595 6761 402 258 230 O ATOM 1561 N THR A 198 -1.614 36.422 15.256 1.00 23.82 N ANISOU 1561 N THR A 198 3046 3154 2851 312 323 330 N ATOM 1562 CA THR A 198 -1.620 36.084 16.677 1.00 25.15 C ANISOU 1562 CA THR A 198 3212 3288 3056 269 303 301 C ATOM 1563 C THR A 198 -0.853 37.096 17.525 1.00 24.89 C ANISOU 1563 C THR A 198 3172 3202 3083 260 317 326 C ATOM 1564 O THR A 198 -0.628 36.851 18.716 1.00 22.48 O ANISOU 1564 O THR A 198 2865 2866 2809 227 303 305 O ATOM 1565 CB THR A 198 -1.059 34.673 16.890 1.00 24.70 C ANISOU 1565 CB THR A 198 3163 3226 2997 242 295 269 C ATOM 1566 OG1 THR A 198 0.163 34.516 16.161 1.00 22.77 O ANISOU 1566 OG1 THR A 198 2924 2969 2759 255 320 292 O ATOM 1567 CG2 THR A 198 -2.059 33.621 16.412 1.00 24.52 C ANISOU 1567 CG2 THR A 198 3144 3250 2924 240 274 231 C ATOM 1568 N ASN A 199 -0.451 38.223 16.937 1.00 26.27 N ANISOU 1568 N ASN A 199 3342 3365 3273 289 344 370 N ATOM 1569 CA ASN A 199 0.220 39.317 17.639 1.00 25.05 C ANISOU 1569 CA ASN A 199 3179 3160 3180 283 360 394 C ATOM 1570 C ASN A 199 1.418 38.803 18.445 1.00 24.94 C ANISOU 1570 C ASN A 199 3163 3104 3208 251 358 380 C ATOM 1571 O ASN A 199 1.532 39.007 19.654 1.00 19.86 O ANISOU 1571 O ASN A 199 2514 2430 2601 224 344 363 O ATOM 1572 CB ASN A 199 -0.781 40.072 18.517 1.00 28.48 C ANISOU 1572 CB ASN A 199 3605 3590 3626 275 343 383 C ATOM 1573 CG ASN A 199 -2.007 40.527 17.739 1.00 30.25 C ANISOU 1573 CG ASN A 199 3828 3859 3807 308 342 396 C ATOM 1574 OD1 ASN A 199 -1.985 41.560 17.076 1.00 28.74 O ANISOU 1574 OD1 ASN A 199 3633 3665 3622 340 367 436 O ATOM 1575 ND2 ASN A 199 -3.080 39.747 17.810 1.00 33.74 N ANISOU 1575 ND2 ASN A 199 4273 4340 4205 299 314 361 N ATOM 1576 N ASN A 200 2.324 38.131 17.730 1.00 22.67 N ANISOU 1576 N ASN A 200 2882 2818 2914 257 374 388 N ATOM 1577 CA ASN A 200 3.412 37.397 18.374 1.00 23.79 C ANISOU 1577 CA ASN A 200 3024 2929 3086 229 370 373 C ATOM 1578 C ASN A 200 4.321 38.318 19.181 1.00 19.16 C ANISOU 1578 C ASN A 200 2423 2290 2566 217 381 387 C ATOM 1579 O ASN A 200 4.739 37.972 20.291 1.00 20.29 O ANISOU 1579 O ASN A 200 2563 2409 2738 187 363 363 O ATOM 1580 CB ASN A 200 4.225 36.642 17.318 1.00 23.48 C ANISOU 1580 CB ASN A 200 2992 2901 3027 243 390 384 C ATOM 1581 CG ASN A 200 3.633 35.290 16.972 1.00 21.20 C ANISOU 1581 CG ASN A 200 2717 2652 2686 238 371 350 C ATOM 1582 OD1 ASN A 200 2.492 34.974 17.333 1.00 19.34 O ANISOU 1582 OD1 ASN A 200 2484 2442 2424 228 346 322 O ATOM 1583 ND2 ASN A 200 4.414 34.473 16.274 1.00 18.07 N ANISOU 1583 ND2 ASN A 200 2327 2260 2278 244 385 352 N ATOM 1584 N GLU A 201 4.647 39.490 18.633 1.00 21.78 N ANISOU 1584 N GLU A 201 2746 2605 2925 241 410 427 N ATOM 1585 CA GLU A 201 5.672 40.340 19.235 1.00 24.95 C ANISOU 1585 CA GLU A 201 3131 2953 3396 230 426 441 C ATOM 1586 C GLU A 201 5.264 40.827 20.619 1.00 22.02 C ANISOU 1586 C GLU A 201 2751 2560 3055 205 400 414 C ATOM 1587 O GLU A 201 6.077 40.824 21.550 1.00 24.27 O ANISOU 1587 O GLU A 201 3026 2811 3384 180 392 398 O ATOM 1588 CB GLU A 201 5.974 41.534 18.329 1.00 26.15 C ANISOU 1588 CB GLU A 201 3274 3089 3571 263 466 490 C ATOM 1589 CG GLU A 201 7.177 42.341 18.787 1.00 26.80 C ANISOU 1589 CG GLU A 201 3336 3114 3730 252 487 505 C ATOM 1590 CD GLU A 201 7.325 43.642 18.037 1.00 26.80 C ANISOU 1590 CD GLU A 201 3327 3094 3762 282 529 554 C ATOM 1591 OE1 GLU A 201 6.317 44.361 17.892 1.00 30.64 O ANISOU 1591 OE1 GLU A 201 3815 3594 4233 300 530 565 O ATOM 1592 OE2 GLU A 201 8.450 43.944 17.590 1.00 32.64 O ANISOU 1592 OE2 GLU A 201 4056 3803 4542 290 562 583 O ATOM 1593 N SER A 202 4.014 41.275 20.773 1.00 21.40 N ANISOU 1593 N SER A 202 2676 2502 2954 212 388 408 N ATOM 1594 CA SER A 202 3.621 41.842 22.060 1.00 19.72 C ANISOU 1594 CA SER A 202 2455 2268 2770 190 367 384 C ATOM 1595 C SER A 202 3.557 40.782 23.153 1.00 18.88 C ANISOU 1595 C SER A 202 2354 2168 2652 158 333 340 C ATOM 1596 O SER A 202 3.787 41.096 24.326 1.00 23.38 O ANISOU 1596 O SER A 202 2916 2712 3257 137 318 319 O ATOM 1597 CB SER A 202 2.286 42.585 21.943 1.00 18.52 C ANISOU 1597 CB SER A 202 2304 2137 2597 208 365 389 C ATOM 1598 OG SER A 202 1.232 41.742 21.516 1.00 22.43 O ANISOU 1598 OG SER A 202 2813 2682 3028 214 347 376 O ATOM 1599 N PHE A 203 3.261 39.529 22.803 1.00 17.48 N ANISOU 1599 N PHE A 203 2191 2025 2427 155 321 326 N ATOM 1600 CA PHE A 203 3.237 38.489 23.827 1.00 22.21 C ANISOU 1600 CA PHE A 203 2795 2626 3016 126 292 289 C ATOM 1601 C PHE A 203 4.638 38.187 24.353 1.00 18.01 C ANISOU 1601 C PHE A 203 2256 2061 2525 110 294 285 C ATOM 1602 O PHE A 203 4.823 37.995 25.560 1.00 20.48 O ANISOU 1602 O PHE A 203 2565 2359 2855 88 273 260 O ATOM 1603 CB PHE A 203 2.588 37.210 23.297 1.00 20.77 C ANISOU 1603 CB PHE A 203 2628 2484 2779 126 282 273 C ATOM 1604 CG PHE A 203 2.548 36.102 24.310 1.00 18.56 C ANISOU 1604 CG PHE A 203 2355 2205 2492 99 258 239 C ATOM 1605 CD1 PHE A 203 1.492 35.999 25.198 1.00 17.47 C ANISOU 1605 CD1 PHE A 203 2219 2080 2340 86 236 214 C ATOM 1606 CD2 PHE A 203 3.583 35.187 24.403 1.00 18.60 C ANISOU 1606 CD2 PHE A 203 2363 2198 2507 88 260 234 C ATOM 1607 CE1 PHE A 203 1.451 34.998 26.137 1.00 17.55 C ANISOU 1607 CE1 PHE A 203 2234 2089 2343 63 217 188 C ATOM 1608 CE2 PHE A 203 3.550 34.181 25.352 1.00 21.98 C ANISOU 1608 CE2 PHE A 203 2797 2626 2930 65 240 207 C ATOM 1609 CZ PHE A 203 2.480 34.085 26.218 1.00 20.66 C ANISOU 1609 CZ PHE A 203 2632 2471 2747 53 219 185 C ATOM 1610 N VAL A 204 5.633 38.119 23.465 1.00 21.94 N ANISOU 1610 N VAL A 204 2752 2548 3036 122 319 310 N ATOM 1611 CA VAL A 204 6.994 37.809 23.903 1.00 19.64 C ANISOU 1611 CA VAL A 204 2452 2228 2784 108 321 308 C ATOM 1612 C VAL A 204 7.513 38.897 24.837 1.00 23.56 C ANISOU 1612 C VAL A 204 2928 2685 3339 98 318 304 C ATOM 1613 O VAL A 204 8.147 38.610 25.862 1.00 22.40 O ANISOU 1613 O VAL A 204 2774 2521 3216 78 300 282 O ATOM 1614 CB VAL A 204 7.914 37.600 22.683 1.00 23.31 C ANISOU 1614 CB VAL A 204 2916 2688 3252 126 352 338 C ATOM 1615 CG1 VAL A 204 9.368 37.461 23.117 1.00 19.91 C ANISOU 1615 CG1 VAL A 204 2472 2224 2871 113 357 338 C ATOM 1616 CG2 VAL A 204 7.481 36.360 21.915 1.00 17.17 C ANISOU 1616 CG2 VAL A 204 2158 1949 2418 132 350 331 C ATOM 1617 N AILE A 205 7.257 40.161 24.497 0.12 20.74 N ANISOU 1617 N AILE A 205 2562 2314 3005 112 336 325 N ATOM 1618 N BILE A 205 7.255 40.162 24.500 0.88 20.59 N ANISOU 1618 N BILE A 205 2543 2295 2986 112 336 325 N ATOM 1619 CA AILE A 205 7.623 41.259 25.387 0.12 21.41 C ANISOU 1619 CA AILE A 205 2626 2361 3146 102 334 318 C ATOM 1620 CA BILE A 205 7.634 41.252 25.393 0.88 21.40 C ANISOU 1620 CA BILE A 205 2626 2360 3146 102 334 317 C ATOM 1621 C AILE A 205 6.864 41.147 26.703 0.12 20.80 C ANISOU 1621 C AILE A 205 2553 2292 3057 83 299 279 C ATOM 1622 C BILE A 205 6.866 41.149 26.705 0.88 20.74 C ANISOU 1622 C BILE A 205 2545 2284 3050 83 299 279 C ATOM 1623 O AILE A 205 7.429 41.354 27.784 0.12 21.94 O ANISOU 1623 O AILE A 205 2684 2414 3237 65 282 256 O ATOM 1624 O BILE A 205 7.428 41.353 27.787 0.88 21.97 O ANISOU 1624 O BILE A 205 2688 2418 3241 65 282 256 O ATOM 1625 CB AILE A 205 7.370 42.612 24.696 0.12 21.58 C ANISOU 1625 CB AILE A 205 2640 2366 3195 124 364 350 C ATOM 1626 CB BILE A 205 7.420 42.611 24.700 0.88 21.59 C ANISOU 1626 CB BILE A 205 2640 2366 3197 123 365 350 C ATOM 1627 CG1AILE A 205 8.225 42.730 23.433 0.12 22.12 C ANISOU 1627 CG1AILE A 205 2703 2424 3277 144 403 391 C ATOM 1628 CG1BILE A 205 8.353 42.737 23.490 0.88 22.12 C ANISOU 1628 CG1BILE A 205 2702 2420 3283 142 403 390 C ATOM 1629 CG2AILE A 205 7.656 43.765 25.647 0.12 22.34 C ANISOU 1629 CG2AILE A 205 2715 2422 3353 112 361 336 C ATOM 1630 CG2BILE A 205 7.644 43.768 25.673 0.88 22.36 C ANISOU 1630 CG2BILE A 205 2717 2424 3355 111 361 336 C ATOM 1631 CD1AILE A 205 9.709 42.620 23.693 0.12 22.76 C ANISOU 1631 CD1AILE A 205 2767 2470 3410 130 411 390 C ATOM 1632 CD1BILE A 205 8.212 44.046 22.752 0.88 23.69 C ANISOU 1632 CD1BILE A 205 2891 2600 3510 167 439 428 C ATOM 1633 N TYR A 206 5.573 40.815 26.630 1.00 19.77 N ANISOU 1633 N TYR A 206 2438 2196 2876 88 286 272 N ATOM 1634 CA TYR A 206 4.782 40.615 27.842 1.00 20.21 C ANISOU 1634 CA TYR A 206 2499 2264 2916 72 256 237 C ATOM 1635 C TYR A 206 5.317 39.454 28.674 1.00 20.48 C ANISOU 1635 C TYR A 206 2538 2303 2942 52 233 212 C ATOM 1636 O TYR A 206 5.406 39.553 29.904 1.00 22.34 O ANISOU 1636 O TYR A 206 2768 2529 3192 37 211 186 O ATOM 1637 CB TYR A 206 3.314 40.401 27.455 1.00 19.05 C ANISOU 1637 CB TYR A 206 2367 2154 2718 81 250 237 C ATOM 1638 CG TYR A 206 2.470 39.644 28.456 1.00 19.40 C ANISOU 1638 CG TYR A 206 2421 2221 2730 65 221 204 C ATOM 1639 CD1 TYR A 206 2.004 40.258 29.615 1.00 19.15 C ANISOU 1639 CD1 TYR A 206 2384 2180 2712 56 205 182 C ATOM 1640 CD2 TYR A 206 2.116 38.317 28.226 1.00 16.98 C ANISOU 1640 CD2 TYR A 206 2129 1943 2379 60 212 195 C ATOM 1641 CE1 TYR A 206 1.218 39.562 30.531 1.00 20.30 C ANISOU 1641 CE1 TYR A 206 2539 2347 2827 43 181 155 C ATOM 1642 CE2 TYR A 206 1.336 37.615 29.126 1.00 16.39 C ANISOU 1642 CE2 TYR A 206 2063 1886 2278 45 190 168 C ATOM 1643 CZ TYR A 206 0.891 38.242 30.278 1.00 21.89 C ANISOU 1643 CZ TYR A 206 2754 2575 2987 38 175 150 C ATOM 1644 OH TYR A 206 0.113 37.542 31.163 1.00 22.16 O ANISOU 1644 OH TYR A 206 2796 2627 2995 25 156 126 O ATOM 1645 N MET A 207 5.697 38.350 28.026 1.00 16.64 N ANISOU 1645 N MET A 207 2062 1830 2431 53 238 219 N ATOM 1646 CA MET A 207 6.220 37.210 28.777 1.00 20.86 C ANISOU 1646 CA MET A 207 2601 2368 2958 36 220 199 C ATOM 1647 C MET A 207 7.544 37.541 29.462 1.00 20.36 C ANISOU 1647 C MET A 207 2520 2273 2945 27 216 194 C ATOM 1648 O MET A 207 7.770 37.142 30.610 1.00 22.96 O ANISOU 1648 O MET A 207 2846 2600 3276 14 193 170 O ATOM 1649 CB MET A 207 6.393 35.998 27.862 1.00 24.09 C ANISOU 1649 CB MET A 207 3023 2795 3335 40 230 208 C ATOM 1650 CG MET A 207 6.790 34.717 28.612 1.00 17.26 C ANISOU 1650 CG MET A 207 2166 1934 2459 25 213 189 C ATOM 1651 SD MET A 207 7.150 33.341 27.499 1.00 26.57 S ANISOU 1651 SD MET A 207 3358 3128 3609 30 229 199 S ATOM 1652 CE MET A 207 8.409 34.087 26.484 1.00 16.49 C ANISOU 1652 CE MET A 207 2068 1828 2372 46 258 230 C ATOM 1653 N PHE A 208 8.437 38.258 28.776 1.00 19.15 N ANISOU 1653 N PHE A 208 2351 2094 2832 36 239 216 N ATOM 1654 CA PHE A 208 9.747 38.516 29.364 1.00 20.13 C ANISOU 1654 CA PHE A 208 2454 2187 3006 26 236 209 C ATOM 1655 C PHE A 208 9.681 39.570 30.468 1.00 21.43 C ANISOU 1655 C PHE A 208 2603 2334 3208 17 220 186 C ATOM 1656 O PHE A 208 10.433 39.487 31.444 1.00 22.33 O ANISOU 1656 O PHE A 208 2703 2436 3346 5 200 164 O ATOM 1657 CB PHE A 208 10.742 38.932 28.280 1.00 20.53 C ANISOU 1657 CB PHE A 208 2491 2214 3093 37 269 241 C ATOM 1658 CG PHE A 208 11.485 37.773 27.654 1.00 27.65 C ANISOU 1658 CG PHE A 208 3401 3125 3980 40 279 253 C ATOM 1659 CD1 PHE A 208 12.354 36.995 28.412 1.00 25.54 C ANISOU 1659 CD1 PHE A 208 3127 2853 3724 27 261 235 C ATOM 1660 CD2 PHE A 208 11.325 37.469 26.308 1.00 25.65 C ANISOU 1660 CD2 PHE A 208 3159 2885 3700 57 305 281 C ATOM 1661 CE1 PHE A 208 13.040 35.932 27.843 1.00 23.86 C ANISOU 1661 CE1 PHE A 208 2921 2646 3499 30 271 246 C ATOM 1662 CE2 PHE A 208 12.008 36.410 25.733 1.00 25.13 C ANISOU 1662 CE2 PHE A 208 3101 2827 3622 60 315 289 C ATOM 1663 CZ PHE A 208 12.868 35.641 26.503 1.00 26.45 C ANISOU 1663 CZ PHE A 208 3262 2985 3802 46 299 272 C ATOM 1664 N VAL A 209 8.791 40.554 30.343 1.00 17.07 N ANISOU 1664 N VAL A 209 2051 1779 2658 24 226 190 N ATOM 1665 CA VAL A 209 8.694 41.607 31.350 1.00 20.72 C ANISOU 1665 CA VAL A 209 2497 2222 3156 16 213 166 C ATOM 1666 C VAL A 209 7.888 41.139 32.558 1.00 19.37 C ANISOU 1666 C VAL A 209 2338 2075 2947 7 180 133 C ATOM 1667 O VAL A 209 8.360 41.209 33.698 1.00 21.53 O ANISOU 1667 O VAL A 209 2601 2342 3240 -5 156 103 O ATOM 1668 CB VAL A 209 8.094 42.881 30.726 1.00 24.87 C ANISOU 1668 CB VAL A 209 3017 2731 3702 29 237 186 C ATOM 1669 CG1 VAL A 209 7.637 43.839 31.812 1.00 24.15 C ANISOU 1669 CG1 VAL A 209 2915 2626 3634 22 221 156 C ATOM 1670 CG2 VAL A 209 9.109 43.543 29.812 1.00 19.88 C ANISOU 1670 CG2 VAL A 209 2367 2065 3122 38 271 216 C ATOM 1671 N VAL A 210 6.671 40.640 32.333 1.00 20.95 N ANISOU 1671 N VAL A 210 2559 2306 3095 12 177 136 N ATOM 1672 CA VAL A 210 5.792 40.304 33.454 1.00 20.03 C ANISOU 1672 CA VAL A 210 2454 2211 2946 4 150 108 C ATOM 1673 C VAL A 210 6.170 38.969 34.095 1.00 22.65 C ANISOU 1673 C VAL A 210 2795 2560 3251 -5 131 94 C ATOM 1674 O VAL A 210 6.038 38.801 35.315 1.00 21.13 O ANISOU 1674 O VAL A 210 2603 2376 3050 -12 107 68 O ATOM 1675 CB VAL A 210 4.321 40.308 32.994 1.00 18.39 C ANISOU 1675 CB VAL A 210 2262 2028 2697 13 155 116 C ATOM 1676 CG1 VAL A 210 3.407 39.796 34.097 1.00 21.72 C ANISOU 1676 CG1 VAL A 210 2696 2475 3083 5 131 89 C ATOM 1677 CG2 VAL A 210 3.901 41.701 32.572 1.00 17.06 C ANISOU 1677 CG2 VAL A 210 2083 1843 2556 24 172 128 C ATOM 1678 N HIS A 211 6.649 38.004 33.311 1.00 22.08 N ANISOU 1678 N HIS A 211 2730 2494 3165 -4 142 112 N ATOM 1679 CA HIS A 211 6.864 36.659 33.827 1.00 22.70 C ANISOU 1679 CA HIS A 211 2820 2590 3216 -10 128 103 C ATOM 1680 C HIS A 211 8.325 36.214 33.815 1.00 21.10 C ANISOU 1680 C HIS A 211 2605 2370 3040 -13 129 107 C ATOM 1681 O HIS A 211 8.586 35.017 33.972 1.00 18.52 O ANISOU 1681 O HIS A 211 2289 2056 2691 -15 123 107 O ATOM 1682 CB HIS A 211 5.995 35.665 33.048 1.00 19.41 C ANISOU 1682 CB HIS A 211 2424 2198 2752 -8 138 114 C ATOM 1683 CG HIS A 211 4.523 35.898 33.212 1.00 21.99 C ANISOU 1683 CG HIS A 211 2761 2545 3049 -6 133 106 C ATOM 1684 ND1 HIS A 211 3.836 35.557 34.360 1.00 19.52 N ANISOU 1684 ND1 HIS A 211 2456 2246 2715 -14 113 85 N ATOM 1685 CD2 HIS A 211 3.608 36.448 32.376 1.00 19.21 C ANISOU 1685 CD2 HIS A 211 2413 2202 2686 2 145 117 C ATOM 1686 CE1 HIS A 211 2.563 35.885 34.223 1.00 22.33 C ANISOU 1686 CE1 HIS A 211 2818 2618 3049 -11 115 82 C ATOM 1687 NE2 HIS A 211 2.397 36.424 33.027 1.00 23.69 N ANISOU 1687 NE2 HIS A 211 2987 2788 3226 -1 133 101 N ATOM 1688 N PHE A 212 9.276 37.105 33.523 1.00 23.77 N ANISOU 1688 N PHE A 212 2923 2681 3428 -11 139 114 N ATOM 1689 CA PHE A 212 10.678 36.863 33.858 1.00 19.74 C ANISOU 1689 CA PHE A 212 2394 2154 2950 -15 133 110 C ATOM 1690 C PHE A 212 11.297 37.959 34.718 1.00 21.44 C ANISOU 1690 C PHE A 212 2585 2349 3215 -21 119 88 C ATOM 1691 O PHE A 212 11.836 37.673 35.794 1.00 18.28 O ANISOU 1691 O PHE A 212 2175 1952 2818 -26 93 64 O ATOM 1692 CB PHE A 212 11.476 36.680 32.557 1.00 22.42 C ANISOU 1692 CB PHE A 212 2731 2481 3309 -9 162 140 C ATOM 1693 CG PHE A 212 12.918 36.309 32.764 1.00 22.10 C ANISOU 1693 CG PHE A 212 2672 2425 3301 -12 159 140 C ATOM 1694 CD1 PHE A 212 13.265 35.167 33.467 1.00 21.47 C ANISOU 1694 CD1 PHE A 212 2599 2360 3200 -15 140 128 C ATOM 1695 CD2 PHE A 212 13.928 37.087 32.220 1.00 25.57 C ANISOU 1695 CD2 PHE A 212 3087 2834 3794 -10 178 152 C ATOM 1696 CE1 PHE A 212 14.591 34.826 33.641 1.00 28.35 C ANISOU 1696 CE1 PHE A 212 3452 3220 4101 -16 137 129 C ATOM 1697 CE2 PHE A 212 15.250 36.751 32.391 1.00 21.82 C ANISOU 1697 CE2 PHE A 212 2593 2346 3352 -13 175 151 C ATOM 1698 CZ PHE A 212 15.584 35.621 33.099 1.00 26.90 C ANISOU 1698 CZ PHE A 212 3242 3006 3971 -15 154 139 C ATOM 1699 N AILE A 213 11.181 39.221 34.306 0.78 22.87 N ANISOU 1699 N AILE A 213 2752 2506 3432 -19 134 93 N ATOM 1700 N BILE A 213 11.234 39.212 34.265 0.22 22.84 N ANISOU 1700 N BILE A 213 2748 2502 3429 -18 135 94 N ATOM 1701 CA AILE A 213 11.976 40.281 34.921 0.78 22.15 C ANISOU 1701 CA AILE A 213 2631 2387 3399 -25 126 73 C ATOM 1702 CA BILE A 213 12.005 40.291 34.877 0.22 22.18 C ANISOU 1702 CA BILE A 213 2635 2390 3404 -25 127 74 C ATOM 1703 C AILE A 213 11.339 40.776 36.212 0.78 22.12 C ANISOU 1703 C AILE A 213 2626 2392 3388 -30 98 36 C ATOM 1704 C BILE A 213 11.384 40.722 36.197 0.22 22.14 C ANISOU 1704 C BILE A 213 2628 2394 3389 -30 98 37 C ATOM 1705 O AILE A 213 12.032 41.014 37.208 0.78 21.69 O ANISOU 1705 O AILE A 213 2552 2331 3358 -36 74 6 O ATOM 1706 O BILE A 213 12.081 40.881 37.206 0.22 21.80 O ANISOU 1706 O BILE A 213 2567 2347 3368 -36 73 6 O ATOM 1707 CB AILE A 213 12.189 41.426 33.913 0.78 23.49 C ANISOU 1707 CB AILE A 213 2785 2522 3616 -20 160 96 C ATOM 1708 CB BILE A 213 12.123 41.474 33.898 0.22 23.40 C ANISOU 1708 CB BILE A 213 2775 2512 3606 -20 160 96 C ATOM 1709 CG1AILE A 213 13.221 41.019 32.861 0.78 24.01 C ANISOU 1709 CG1AILE A 213 2843 2575 3703 -16 186 127 C ATOM 1710 CG1BILE A 213 12.936 41.081 32.661 0.22 23.72 C ANISOU 1710 CG1BILE A 213 2812 2541 3659 -13 191 132 C ATOM 1711 CG2AILE A 213 12.624 42.700 34.618 0.78 22.55 C ANISOU 1711 CG2AILE A 213 2637 2372 3558 -28 153 70 C ATOM 1712 CG2BILE A 213 12.745 42.680 34.583 0.22 22.55 C ANISOU 1712 CG2BILE A 213 2635 2371 3562 -28 154 71 C ATOM 1713 CD1AILE A 213 13.532 42.109 31.876 0.78 27.35 C ANISOU 1713 CD1AILE A 213 3251 2964 4177 -9 223 154 C ATOM 1714 CD1BILE A 213 14.413 40.906 32.927 0.22 23.88 C ANISOU 1714 CD1BILE A 213 2806 2542 3724 -20 186 125 C ATOM 1715 N AILE A 214 10.019 40.960 36.218 0.78 23.13 N ANISOU 1715 N AILE A 214 2773 2536 3480 -26 99 37 N ATOM 1716 N BILE A 214 10.066 40.932 36.206 0.22 23.05 N ANISOU 1716 N BILE A 214 2762 2524 3470 -26 99 37 N ATOM 1717 CA AILE A 214 9.341 41.403 37.437 0.78 22.04 C ANISOU 1717 CA AILE A 214 2636 2408 3331 -29 74 2 C ATOM 1718 CA BILE A 214 9.397 41.393 37.425 0.22 21.99 C ANISOU 1718 CA BILE A 214 2629 2401 3326 -29 74 3 C ATOM 1719 C AILE A 214 9.508 40.404 38.579 0.78 23.34 C ANISOU 1719 C AILE A 214 2808 2600 3460 -31 42 -20 C ATOM 1720 C BILE A 214 9.544 40.396 38.571 0.22 23.16 C ANISOU 1720 C BILE A 214 2784 2576 3438 -31 42 -20 C ATOM 1721 O AILE A 214 9.841 40.830 39.696 0.78 20.88 O ANISOU 1721 O AILE A 214 2482 2288 3163 -34 18 -54 O ATOM 1722 O BILE A 214 9.878 40.822 39.689 0.22 21.01 O ANISOU 1722 O BILE A 214 2498 2304 3181 -34 18 -54 O ATOM 1723 CB AILE A 214 7.872 41.741 37.129 0.78 21.65 C ANISOU 1723 CB AILE A 214 2605 2371 3250 -23 84 11 C ATOM 1724 CB BILE A 214 7.931 41.746 37.121 0.22 21.67 C ANISOU 1724 CB BILE A 214 2606 2372 3254 -23 84 11 C ATOM 1725 CG1AILE A 214 7.782 43.103 36.439 0.78 21.89 C ANISOU 1725 CG1AILE A 214 2621 2369 3327 -18 108 23 C ATOM 1726 CG1BILE A 214 7.858 43.021 36.279 0.22 21.85 C ANISOU 1726 CG1BILE A 214 2617 2364 3322 -18 112 28 C ATOM 1727 CG2AILE A 214 7.032 41.723 38.388 0.78 20.86 C ANISOU 1727 CG2AILE A 214 2514 2292 3118 -24 58 -20 C ATOM 1728 CG2BILE A 214 7.134 41.903 38.407 0.22 21.04 C ANISOU 1728 CG2BILE A 214 2533 2311 3150 -24 58 -22 C ATOM 1729 CD1AILE A 214 6.365 43.583 36.197 0.78 21.48 C ANISOU 1729 CD1AILE A 214 2584 2329 3250 -10 118 31 C ATOM 1730 CD1BILE A 214 8.618 44.188 36.871 0.22 22.27 C ANISOU 1730 CD1BILE A 214 2640 2382 3439 -24 107 3 C ATOM 1731 N PRO A 215 9.313 39.088 38.384 1.00 22.05 N ANISOU 1731 N PRO A 215 2665 2461 3251 -29 43 -4 N ATOM 1732 CA PRO A 215 9.579 38.154 39.497 1.00 19.71 C ANISOU 1732 CA PRO A 215 2375 2188 2926 -28 16 -22 C ATOM 1733 C PRO A 215 11.010 38.186 40.017 1.00 22.88 C ANISOU 1733 C PRO A 215 2751 2579 3363 -30 0 -37 C ATOM 1734 O PRO A 215 11.215 38.112 41.237 1.00 18.09 O ANISOU 1734 O PRO A 215 2140 1988 2747 -28 -29 -66 O ATOM 1735 CB PRO A 215 9.231 36.788 38.891 1.00 21.36 C ANISOU 1735 CB PRO A 215 2609 2416 3093 -26 28 4 C ATOM 1736 CG PRO A 215 8.220 37.092 37.873 1.00 20.96 C ANISOU 1736 CG PRO A 215 2570 2364 3030 -25 51 23 C ATOM 1737 CD PRO A 215 8.675 38.384 37.253 1.00 19.93 C ANISOU 1737 CD PRO A 215 2418 2203 2951 -25 66 28 C ATOM 1738 N LEU A 216 12.005 38.314 39.133 1.00 22.10 N ANISOU 1738 N LEU A 216 2637 2456 3306 -32 17 -20 N ATOM 1739 CA LEU A 216 13.397 38.332 39.579 1.00 19.59 C ANISOU 1739 CA LEU A 216 2291 2127 3025 -34 2 -35 C ATOM 1740 C LEU A 216 13.733 39.602 40.349 1.00 24.24 C ANISOU 1740 C LEU A 216 2852 2699 3658 -40 -16 -72 C ATOM 1741 O LEU A 216 14.547 39.561 41.279 1.00 22.28 O ANISOU 1741 O LEU A 216 2584 2458 3423 -39 -43 -100 O ATOM 1742 CB LEU A 216 14.345 38.178 38.388 1.00 21.08 C ANISOU 1742 CB LEU A 216 2469 2292 3249 -36 29 -5 C ATOM 1743 CG LEU A 216 14.516 36.753 37.857 1.00 23.23 C ANISOU 1743 CG LEU A 216 2760 2580 3486 -30 39 22 C ATOM 1744 CD1 LEU A 216 15.491 36.739 36.703 1.00 26.38 C ANISOU 1744 CD1 LEU A 216 3146 2955 3923 -30 66 48 C ATOM 1745 CD2 LEU A 216 14.984 35.823 38.968 1.00 22.19 C ANISOU 1745 CD2 LEU A 216 2629 2472 3330 -26 10 6 C ATOM 1746 N ILE A 217 13.124 40.734 39.980 1.00 21.65 N ANISOU 1746 N ILE A 217 2520 2350 3355 -43 0 -73 N ATOM 1747 CA ILE A 217 13.312 41.955 40.756 1.00 25.31 C ANISOU 1747 CA ILE A 217 2958 2797 3861 -48 -16 -112 C ATOM 1748 C ILE A 217 12.804 41.760 42.180 1.00 22.17 C ANISOU 1748 C ILE A 217 2569 2432 3422 -44 -52 -149 C ATOM 1749 O ILE A 217 13.462 42.155 43.151 1.00 24.14 O ANISOU 1749 O ILE A 217 2795 2683 3694 -46 -80 -188 O ATOM 1750 CB ILE A 217 12.625 43.142 40.056 1.00 23.99 C ANISOU 1750 CB ILE A 217 2790 2602 3725 -50 12 -102 C ATOM 1751 CG1 ILE A 217 13.349 43.472 38.747 1.00 23.33 C ANISOU 1751 CG1 ILE A 217 2691 2483 3690 -52 47 -68 C ATOM 1752 CG2 ILE A 217 12.599 44.366 40.967 1.00 27.90 C ANISOU 1752 CG2 ILE A 217 3262 3081 4258 -56 -5 -147 C ATOM 1753 CD1 ILE A 217 12.721 44.627 37.983 1.00 29.32 C ANISOU 1753 CD1 ILE A 217 3448 3212 4480 -51 79 -51 C ATOM 1754 N VAL A 218 11.630 41.141 42.327 1.00 19.61 N ANISOU 1754 N VAL A 218 2278 2137 3038 -38 -52 -137 N ATOM 1755 CA VAL A 218 11.067 40.919 43.656 1.00 21.80 C ANISOU 1755 CA VAL A 218 2566 2446 3272 -31 -81 -168 C ATOM 1756 C VAL A 218 11.936 39.956 44.461 1.00 25.42 C ANISOU 1756 C VAL A 218 3020 2930 3710 -24 -108 -178 C ATOM 1757 O VAL A 218 12.182 40.171 45.657 1.00 19.89 O ANISOU 1757 O VAL A 218 2308 2247 3003 -19 -139 -215 O ATOM 1758 CB VAL A 218 9.615 40.416 43.550 1.00 18.79 C ANISOU 1758 CB VAL A 218 2219 2088 2834 -26 -70 -149 C ATOM 1759 CG1 VAL A 218 9.092 40.016 44.931 1.00 19.35 C ANISOU 1759 CG1 VAL A 218 2302 2195 2856 -17 -98 -174 C ATOM 1760 CG2 VAL A 218 8.730 41.488 42.934 1.00 20.99 C ANISOU 1760 CG2 VAL A 218 2498 2346 3132 -29 -49 -144 C ATOM 1761 N ILE A 219 12.403 38.877 43.826 1.00 18.47 N ANISOU 1761 N ILE A 219 2148 2053 2817 -22 -96 -145 N ATOM 1762 CA ILE A 219 13.220 37.889 44.527 1.00 23.84 C ANISOU 1762 CA ILE A 219 2825 2757 3477 -14 -118 -149 C ATOM 1763 C ILE A 219 14.502 38.527 45.042 1.00 23.71 C ANISOU 1763 C ILE A 219 2770 2730 3509 -15 -141 -182 C ATOM 1764 O ILE A 219 14.900 38.322 46.194 1.00 21.12 O ANISOU 1764 O ILE A 219 2433 2427 3163 -5 -174 -210 O ATOM 1765 CB ILE A 219 13.528 36.694 43.607 1.00 21.77 C ANISOU 1765 CB ILE A 219 2577 2494 3202 -12 -96 -108 C ATOM 1766 CG1 ILE A 219 12.258 35.898 43.316 1.00 23.04 C ANISOU 1766 CG1 ILE A 219 2774 2671 3309 -10 -79 -83 C ATOM 1767 CG2 ILE A 219 14.601 35.806 44.232 1.00 24.14 C ANISOU 1767 CG2 ILE A 219 2868 2811 3494 -3 -117 -111 C ATOM 1768 CD1 ILE A 219 12.428 34.898 42.195 1.00 20.64 C ANISOU 1768 CD1 ILE A 219 2484 2361 2999 -11 -53 -45 C ATOM 1769 N PHE A 220 15.171 39.310 44.191 1.00 26.22 N ANISOU 1769 N PHE A 220 3063 3009 3889 -27 -124 -178 N ATOM 1770 CA PHE A 220 16.456 39.878 44.568 1.00 20.45 C ANISOU 1770 CA PHE A 220 2292 2265 3213 -31 -143 -209 C ATOM 1771 C PHE A 220 16.320 41.132 45.416 1.00 22.96 C ANISOU 1771 C PHE A 220 2589 2577 3559 -36 -165 -258 C ATOM 1772 O PHE A 220 17.291 41.521 46.069 1.00 22.70 O ANISOU 1772 O PHE A 220 2522 2542 3560 -37 -191 -295 O ATOM 1773 CB PHE A 220 17.297 40.161 43.321 1.00 25.75 C ANISOU 1773 CB PHE A 220 2943 2896 3944 -42 -113 -183 C ATOM 1774 CG PHE A 220 17.970 38.934 42.762 1.00 28.84 C ANISOU 1774 CG PHE A 220 3341 3295 4321 -36 -103 -148 C ATOM 1775 CD1 PHE A 220 19.238 38.570 43.187 1.00 29.55 C ANISOU 1775 CD1 PHE A 220 3404 3390 4432 -33 -123 -161 C ATOM 1776 CD2 PHE A 220 17.325 38.131 41.836 1.00 28.83 C ANISOU 1776 CD2 PHE A 220 3373 3298 4284 -33 -74 -105 C ATOM 1777 CE1 PHE A 220 19.857 37.440 42.684 1.00 35.03 C ANISOU 1777 CE1 PHE A 220 4104 4091 5114 -26 -112 -129 C ATOM 1778 CE2 PHE A 220 17.939 36.998 41.328 1.00 30.21 C ANISOU 1778 CE2 PHE A 220 3554 3477 4446 -28 -64 -76 C ATOM 1779 CZ PHE A 220 19.207 36.654 41.753 1.00 34.82 C ANISOU 1779 CZ PHE A 220 4112 4064 5053 -24 -82 -87 C ATOM 1780 N PHE A 221 15.146 41.767 45.438 1.00 20.23 N ANISOU 1780 N PHE A 221 2260 2227 3199 -38 -155 -263 N ATOM 1781 CA PHE A 221 14.916 42.812 46.431 1.00 21.91 C ANISOU 1781 CA PHE A 221 2457 2440 3427 -39 -179 -314 C ATOM 1782 C PHE A 221 14.789 42.212 47.827 1.00 24.96 C ANISOU 1782 C PHE A 221 2853 2876 3755 -23 -218 -344 C ATOM 1783 O PHE A 221 15.359 42.741 48.791 1.00 20.88 O ANISOU 1783 O PHE A 221 2310 2368 3256 -20 -250 -393 O ATOM 1784 CB PHE A 221 13.672 43.625 46.074 1.00 22.15 C ANISOU 1784 CB PHE A 221 2505 2454 3457 -43 -156 -309 C ATOM 1785 CG PHE A 221 13.241 44.583 47.152 1.00 24.90 C ANISOU 1785 CG PHE A 221 2843 2808 3810 -41 -179 -361 C ATOM 1786 CD1 PHE A 221 13.789 45.853 47.231 1.00 23.85 C ANISOU 1786 CD1 PHE A 221 2675 2639 3748 -53 -181 -398 C ATOM 1787 CD2 PHE A 221 12.288 44.212 48.083 1.00 20.73 C ANISOU 1787 CD2 PHE A 221 2341 2319 3216 -29 -197 -374 C ATOM 1788 CE1 PHE A 221 13.395 46.730 48.223 1.00 28.88 C ANISOU 1788 CE1 PHE A 221 3304 3280 4390 -52 -203 -449 C ATOM 1789 CE2 PHE A 221 11.889 45.083 49.077 1.00 27.27 C ANISOU 1789 CE2 PHE A 221 3161 3153 4045 -26 -218 -423 C ATOM 1790 CZ PHE A 221 12.442 46.345 49.148 1.00 26.45 C ANISOU 1790 CZ PHE A 221 3023 3014 4012 -37 -222 -462 C ATOM 1791 N CYS A 222 14.047 41.105 47.955 1.00 24.25 N ANISOU 1791 N CYS A 222 2799 2819 3597 -11 -215 -314 N ATOM 1792 CA CYS A 222 13.905 40.456 49.255 1.00 24.32 C ANISOU 1792 CA CYS A 222 2819 2875 3547 8 -247 -335 C ATOM 1793 C CYS A 222 15.235 39.900 49.740 1.00 21.51 C ANISOU 1793 C CYS A 222 2440 2536 3199 16 -274 -347 C ATOM 1794 O CYS A 222 15.578 40.026 50.921 1.00 25.94 O ANISOU 1794 O CYS A 222 2987 3126 3743 29 -311 -387 O ATOM 1795 CB CYS A 222 12.861 39.345 49.185 1.00 18.84 C ANISOU 1795 CB CYS A 222 2167 2206 2786 18 -232 -296 C ATOM 1796 SG CYS A 222 11.206 39.910 48.806 1.00 28.11 S ANISOU 1796 SG CYS A 222 3367 3370 3942 11 -206 -286 S ATOM 1797 N TYR A 223 15.993 39.272 48.844 1.00 23.93 N ANISOU 1797 N TYR A 223 2740 2825 3526 11 -257 -312 N ATOM 1798 CA TYR A 223 17.299 38.751 49.226 1.00 23.43 C ANISOU 1798 CA TYR A 223 2652 2776 3474 20 -280 -321 C ATOM 1799 C TYR A 223 18.232 39.876 49.644 1.00 25.06 C ANISOU 1799 C TYR A 223 2813 2968 3742 12 -306 -373 C ATOM 1800 O TYR A 223 18.982 39.743 50.618 1.00 30.67 O ANISOU 1800 O TYR A 223 3501 3706 4444 25 -343 -406 O ATOM 1801 CB TYR A 223 17.905 37.952 48.075 1.00 29.01 C ANISOU 1801 CB TYR A 223 3362 3463 4199 15 -253 -274 C ATOM 1802 CG TYR A 223 19.169 37.232 48.466 1.00 30.41 C ANISOU 1802 CG TYR A 223 3517 3658 4380 26 -275 -276 C ATOM 1803 CD1 TYR A 223 19.171 36.329 49.521 1.00 35.99 C ANISOU 1803 CD1 TYR A 223 4236 4410 5028 50 -301 -279 C ATOM 1804 CD2 TYR A 223 20.357 37.449 47.784 1.00 34.34 C ANISOU 1804 CD2 TYR A 223 3981 4127 4940 16 -268 -274 C ATOM 1805 CE1 TYR A 223 20.323 35.667 49.888 1.00 39.40 C ANISOU 1805 CE1 TYR A 223 4648 4861 5462 64 -322 -280 C ATOM 1806 CE2 TYR A 223 21.518 36.792 48.147 1.00 35.14 C ANISOU 1806 CE2 TYR A 223 4060 4245 5045 28 -289 -276 C ATOM 1807 CZ TYR A 223 21.492 35.901 49.196 1.00 36.41 C ANISOU 1807 CZ TYR A 223 4234 4453 5145 53 -316 -279 C ATOM 1808 OH TYR A 223 22.638 35.238 49.569 1.00 43.39 O ANISOU 1808 OH TYR A 223 5096 5356 6032 68 -338 -279 O ATOM 1809 N GLY A 224 18.195 40.995 48.922 1.00 22.26 N ANISOU 1809 N GLY A 224 2441 2568 3449 -8 -285 -381 N ATOM 1810 CA GLY A 224 19.027 42.127 49.283 1.00 22.31 C ANISOU 1810 CA GLY A 224 2402 2554 3521 -19 -305 -432 C ATOM 1811 C GLY A 224 18.730 42.650 50.670 1.00 28.88 C ANISOU 1811 C GLY A 224 3227 3417 4328 -9 -345 -491 C ATOM 1812 O GLY A 224 19.638 43.102 51.371 1.00 31.11 O ANISOU 1812 O GLY A 224 3471 3706 4642 -8 -378 -540 O ATOM 1813 N GLN A 225 17.460 42.600 51.082 1.00 28.43 N ANISOU 1813 N GLN A 225 3205 3381 4215 0 -342 -488 N ATOM 1814 CA GLN A 225 17.107 42.933 52.459 1.00 26.45 C ANISOU 1814 CA GLN A 225 2954 3168 3927 15 -380 -539 C ATOM 1815 C GLN A 225 17.685 41.923 53.445 1.00 34.58 C ANISOU 1815 C GLN A 225 3983 4252 4902 40 -416 -547 C ATOM 1816 O GLN A 225 18.200 42.308 54.502 1.00 30.37 O ANISOU 1816 O GLN A 225 3425 3745 4368 51 -457 -602 O ATOM 1817 CB GLN A 225 15.590 43.017 52.602 1.00 25.60 C ANISOU 1817 CB GLN A 225 2886 3070 3771 20 -363 -527 C ATOM 1818 CG GLN A 225 14.966 44.116 51.775 1.00 30.46 C ANISOU 1818 CG GLN A 225 3500 3636 4437 -1 -331 -524 C ATOM 1819 CD GLN A 225 15.550 45.481 52.092 1.00 36.11 C ANISOU 1819 CD GLN A 225 4173 4323 5223 -14 -346 -584 C ATOM 1820 OE1 GLN A 225 16.449 45.963 51.400 1.00 41.32 O ANISOU 1820 OE1 GLN A 225 4802 4943 5956 -30 -335 -585 O ATOM 1821 NE2 GLN A 225 15.040 46.111 53.141 1.00 32.59 N ANISOU 1821 NE2 GLN A 225 3728 3897 4759 -6 -370 -634 N ATOM 1822 N LEU A 226 17.616 40.628 53.113 1.00 29.02 N ANISOU 1822 N LEU A 226 3306 3565 4153 51 -402 -493 N ATOM 1823 CA LEU A 226 18.168 39.597 53.991 1.00 32.51 C ANISOU 1823 CA LEU A 226 3750 4057 4544 78 -432 -492 C ATOM 1824 C LEU A 226 19.655 39.814 54.242 1.00 32.20 C ANISOU 1824 C LEU A 226 3664 4020 4552 79 -463 -526 C ATOM 1825 O LEU A 226 20.119 39.739 55.384 1.00 34.73 O ANISOU 1825 O LEU A 226 3968 4384 4844 100 -505 -565 O ATOM 1826 CB LEU A 226 17.942 38.206 53.392 1.00 33.95 C ANISOU 1826 CB LEU A 226 3967 4246 4687 86 -404 -426 C ATOM 1827 CG LEU A 226 16.524 37.637 53.388 1.00 37.75 C ANISOU 1827 CG LEU A 226 4496 4740 5108 93 -380 -392 C ATOM 1828 CD1 LEU A 226 16.557 36.145 53.097 1.00 36.35 C ANISOU 1828 CD1 LEU A 226 4344 4577 4890 106 -363 -337 C ATOM 1829 CD2 LEU A 226 15.861 37.915 54.711 1.00 33.11 C ANISOU 1829 CD2 LEU A 226 3918 4193 4468 113 -407 -428 C ATOM 1830 N VAL A 227 20.420 40.074 53.179 1.00 35.69 N ANISOU 1830 N VAL A 227 4080 4416 5063 57 -442 -512 N ATOM 1831 CA VAL A 227 21.869 40.177 53.310 1.00 30.29 C ANISOU 1831 CA VAL A 227 3350 3732 4428 56 -467 -539 C ATOM 1832 C VAL A 227 22.250 41.441 54.072 1.00 37.92 C ANISOU 1832 C VAL A 227 4275 4697 5437 49 -502 -614 C ATOM 1833 O VAL A 227 22.931 41.378 55.102 1.00 38.00 O ANISOU 1833 O VAL A 227 4259 4747 5432 67 -547 -657 O ATOM 1834 CB VAL A 227 22.540 40.137 51.928 1.00 35.00 C ANISOU 1834 CB VAL A 227 3932 4279 5090 34 -431 -501 C ATOM 1835 CG1 VAL A 227 24.001 40.535 52.055 1.00 30.73 C ANISOU 1835 CG1 VAL A 227 3334 3728 4613 28 -456 -538 C ATOM 1836 CG2 VAL A 227 22.404 38.756 51.309 1.00 33.53 C ANISOU 1836 CG2 VAL A 227 3780 4101 4860 45 -405 -435 C ATOM 1837 N PHE A 228 21.823 42.602 53.580 1.00 38.32 N ANISOU 1837 N PHE A 228 4318 4702 5542 24 -481 -632 N ATOM 1838 CA PHE A 228 22.260 43.889 54.123 1.00 40.22 C ANISOU 1838 CA PHE A 228 4514 4928 5841 12 -507 -704 C ATOM 1839 C PHE A 228 21.228 44.501 55.070 1.00 38.01 C ANISOU 1839 C PHE A 228 4252 4671 5521 21 -524 -746 C ATOM 1840 O PHE A 228 20.674 45.565 54.803 1.00 51.96 O ANISOU 1840 O PHE A 228 6015 6398 7328 3 -506 -765 O ATOM 1841 CB PHE A 228 22.575 44.858 52.980 1.00 41.78 C ANISOU 1841 CB PHE A 228 4685 5054 6135 -20 -470 -699 C ATOM 1842 N THR A 229 20.979 43.848 56.204 1.00 48.37 N ANISOU 1842 N THR A 229 5581 6044 6752 51 -558 -760 N ATOM 1843 CA THR A 229 20.192 44.504 57.258 1.00 48.92 C ANISOU 1843 CA THR A 229 5660 6142 6787 62 -582 -811 C ATOM 1844 C THR A 229 21.101 45.334 58.166 1.00 56.80 C ANISOU 1844 C THR A 229 6607 7154 7823 63 -630 -895 C ATOM 1845 O THR A 229 20.850 45.475 59.367 1.00 59.01 O ANISOU 1845 O THR A 229 6888 7482 8052 86 -668 -943 O ATOM 1846 CB THR A 229 19.404 43.504 58.130 1.00 48.05 C ANISOU 1846 CB THR A 229 5593 6094 6570 97 -595 -790 C ATOM 1847 OG1 THR A 229 20.176 42.315 58.328 1.00 48.02 O ANISOU 1847 OG1 THR A 229 5589 6128 6530 118 -611 -762 O ATOM 1848 CG2 THR A 229 18.057 43.160 57.501 1.00 44.46 C ANISOU 1848 CG2 THR A 229 5189 5623 6079 93 -550 -732 C ATOM 1849 N GLN A 244 15.254 30.002 64.816 1.00 43.32 N ANISOU 1849 N GLN A 244 5367 5985 5109 486 -531 -303 N ATOM 1850 CA GLN A 244 16.584 30.559 64.579 1.00 46.97 C ANISOU 1850 CA GLN A 244 5783 6442 5620 476 -570 -344 C ATOM 1851 C GLN A 244 17.425 29.582 63.768 1.00 43.66 C ANISOU 1851 C GLN A 244 5359 5998 5232 471 -553 -297 C ATOM 1852 O GLN A 244 17.740 29.829 62.606 1.00 36.37 O ANISOU 1852 O GLN A 244 4422 5023 4375 431 -538 -294 O ATOM 1853 CB GLN A 244 17.279 30.885 65.901 1.00 52.56 C ANISOU 1853 CB GLN A 244 6469 7218 6285 518 -625 -392 C ATOM 1854 N LYS A 245 17.806 28.477 64.411 1.00 41.80 N ANISOU 1854 N LYS A 245 5134 5803 4947 514 -555 -259 N ATOM 1855 CA LYS A 245 18.385 27.357 63.680 1.00 40.50 C ANISOU 1855 CA LYS A 245 4972 5614 4803 513 -529 -203 C ATOM 1856 C LYS A 245 17.361 26.741 62.736 1.00 36.02 C ANISOU 1856 C LYS A 245 4442 4996 4249 485 -471 -151 C ATOM 1857 O LYS A 245 17.695 26.353 61.610 1.00 37.20 O ANISOU 1857 O LYS A 245 4587 5099 4448 458 -446 -125 O ATOM 1858 CB LYS A 245 18.914 26.313 64.664 1.00 44.13 C ANISOU 1858 CB LYS A 245 5437 6128 5203 570 -541 -171 C ATOM 1859 CG LYS A 245 19.450 25.054 64.015 1.00 42.66 C ANISOU 1859 CG LYS A 245 5258 5919 5033 574 -511 -110 C ATOM 1860 CD LYS A 245 19.829 24.019 65.060 1.00 44.65 C ANISOU 1860 CD LYS A 245 5518 6225 5220 634 -519 -73 C ATOM 1861 N ALA A 246 16.105 26.649 63.180 1.00 41.38 N ANISOU 1861 N ALA A 246 5154 5685 4885 492 -448 -138 N ATOM 1862 CA ALA A 246 15.048 26.110 62.332 1.00 36.02 C ANISOU 1862 CA ALA A 246 4506 4961 4218 465 -394 -94 C ATOM 1863 C ALA A 246 14.731 27.049 61.175 1.00 33.14 C ANISOU 1863 C ALA A 246 4132 4543 3915 412 -385 -120 C ATOM 1864 O ALA A 246 14.417 26.594 60.069 1.00 29.56 O ANISOU 1864 O ALA A 246 3691 4044 3496 384 -348 -87 O ATOM 1865 CB ALA A 246 13.796 25.842 63.165 1.00 39.13 C ANISOU 1865 CB ALA A 246 4935 5381 4552 487 -374 -76 C ATOM 1866 N GLU A 247 14.787 28.361 61.411 1.00 30.69 N ANISOU 1866 N GLU A 247 3799 4239 3621 401 -417 -179 N ATOM 1867 CA GLU A 247 14.532 29.305 60.332 1.00 34.05 C ANISOU 1867 CA GLU A 247 4215 4615 4108 354 -407 -202 C ATOM 1868 C GLU A 247 15.717 29.415 59.383 1.00 27.13 C ANISOU 1868 C GLU A 247 3308 3706 3294 332 -414 -205 C ATOM 1869 O GLU A 247 15.523 29.697 58.196 1.00 25.30 O ANISOU 1869 O GLU A 247 3076 3426 3112 295 -390 -198 O ATOM 1870 CB GLU A 247 14.179 30.685 60.894 1.00 35.43 C ANISOU 1870 CB GLU A 247 4376 4803 4283 349 -436 -262 C ATOM 1871 CG GLU A 247 12.870 30.744 61.677 1.00 36.11 C ANISOU 1871 CG GLU A 247 4492 4913 4313 364 -424 -261 C ATOM 1872 CD GLU A 247 11.627 30.615 60.808 1.00 41.34 C ANISOU 1872 CD GLU A 247 5182 5536 4988 335 -378 -230 C ATOM 1873 OE1 GLU A 247 11.745 30.293 59.604 1.00 37.57 O ANISOU 1873 OE1 GLU A 247 4705 5015 4556 306 -352 -203 O ATOM 1874 OE2 GLU A 247 10.520 30.845 61.338 1.00 39.08 O ANISOU 1874 OE2 GLU A 247 4917 5265 4668 342 -367 -234 O ATOM 1875 N LYS A 248 16.938 29.204 59.884 1.00 28.99 N ANISOU 1875 N LYS A 248 3518 3970 3529 356 -447 -217 N ATOM 1876 CA LYS A 248 18.114 29.234 59.020 1.00 31.64 C ANISOU 1876 CA LYS A 248 3822 4275 3924 338 -452 -218 C ATOM 1877 C LYS A 248 18.070 28.111 57.992 1.00 23.82 C ANISOU 1877 C LYS A 248 2852 3250 2948 327 -408 -158 C ATOM 1878 O LYS A 248 18.433 28.313 56.829 1.00 25.59 O ANISOU 1878 O LYS A 248 3065 3430 3230 295 -392 -153 O ATOM 1879 CB LYS A 248 19.389 29.146 59.858 1.00 29.50 C ANISOU 1879 CB LYS A 248 3518 4046 3643 370 -497 -241 C ATOM 1880 CG LYS A 248 20.670 29.420 59.081 1.00 31.21 C ANISOU 1880 CG LYS A 248 3696 4236 3928 350 -508 -254 C ATOM 1881 CD LYS A 248 21.908 29.272 59.965 1.00 30.64 C ANISOU 1881 CD LYS A 248 3589 4209 3843 384 -555 -277 C ATOM 1882 CE LYS A 248 22.044 27.847 60.487 1.00 35.20 C ANISOU 1882 CE LYS A 248 4189 4822 4364 426 -546 -224 C ATOM 1883 NZ LYS A 248 23.161 27.698 61.462 1.00 47.20 N ANISOU 1883 NZ LYS A 248 5678 6396 5862 466 -593 -246 N ATOM 1884 N GLU A 249 17.623 26.920 58.405 1.00 25.93 N ANISOU 1884 N GLU A 249 3150 3537 3166 353 -387 -112 N ATOM 1885 CA GLU A 249 17.533 25.788 57.484 1.00 27.95 C ANISOU 1885 CA GLU A 249 3427 3759 3434 343 -344 -57 C ATOM 1886 C GLU A 249 16.607 26.098 56.315 1.00 25.93 C ANISOU 1886 C GLU A 249 3187 3455 3210 302 -308 -50 C ATOM 1887 O GLU A 249 16.920 25.775 55.161 1.00 26.05 O ANISOU 1887 O GLU A 249 3200 3431 3267 279 -284 -29 O ATOM 1888 CB GLU A 249 17.053 24.539 58.234 1.00 31.03 C ANISOU 1888 CB GLU A 249 3848 4176 3765 379 -324 -12 C ATOM 1889 CG GLU A 249 17.179 23.228 57.450 1.00 29.67 C ANISOU 1889 CG GLU A 249 3693 3975 3606 376 -284 44 C ATOM 1890 CD GLU A 249 16.324 22.104 58.028 1.00 28.36 C ANISOU 1890 CD GLU A 249 3564 3823 3390 402 -252 89 C ATOM 1891 OE1 GLU A 249 15.161 22.374 58.401 1.00 31.93 O ANISOU 1891 OE1 GLU A 249 4036 4281 3814 398 -241 85 O ATOM 1892 OE2 GLU A 249 16.812 20.952 58.116 1.00 22.77 O ANISOU 1892 OE2 GLU A 249 2862 3116 2672 425 -236 131 O ATOM 1893 N VAL A 250 15.461 26.725 56.591 1.00 25.21 N ANISOU 1893 N VAL A 250 3111 3367 3100 293 -304 -67 N ATOM 1894 CA VAL A 250 14.523 27.060 55.524 1.00 23.21 C ANISOU 1894 CA VAL A 250 2872 3072 2873 256 -272 -61 C ATOM 1895 C VAL A 250 15.135 28.085 54.579 1.00 23.90 C ANISOU 1895 C VAL A 250 2931 3127 3024 226 -281 -90 C ATOM 1896 O VAL A 250 15.082 27.930 53.356 1.00 23.68 O ANISOU 1896 O VAL A 250 2906 3059 3031 200 -253 -70 O ATOM 1897 CB VAL A 250 13.191 27.563 56.110 1.00 25.06 C ANISOU 1897 CB VAL A 250 3126 3321 3073 257 -268 -75 C ATOM 1898 CG1 VAL A 250 12.204 27.887 54.989 1.00 22.74 C ANISOU 1898 CG1 VAL A 250 2846 2987 2806 221 -236 -68 C ATOM 1899 CG2 VAL A 250 12.608 26.533 57.062 1.00 23.39 C ANISOU 1899 CG2 VAL A 250 2943 3142 2802 289 -256 -44 C ATOM 1900 N THR A 251 15.731 29.145 55.135 1.00 25.98 N ANISOU 1900 N THR A 251 3164 3404 3301 229 -319 -137 N ATOM 1901 CA THR A 251 16.346 30.174 54.303 1.00 20.75 C ANISOU 1901 CA THR A 251 2472 2709 2704 200 -326 -164 C ATOM 1902 C THR A 251 17.451 29.586 53.433 1.00 21.55 C ANISOU 1902 C THR A 251 2558 2786 2844 194 -316 -140 C ATOM 1903 O THR A 251 17.581 29.941 52.256 1.00 21.93 O ANISOU 1903 O THR A 251 2598 2794 2940 167 -295 -134 O ATOM 1904 CB THR A 251 16.900 31.300 55.179 1.00 23.20 C ANISOU 1904 CB THR A 251 2750 3040 3024 208 -370 -222 C ATOM 1905 OG1 THR A 251 15.853 31.843 55.998 1.00 20.74 O ANISOU 1905 OG1 THR A 251 2455 2752 2675 215 -378 -245 O ATOM 1906 CG2 THR A 251 17.489 32.411 54.319 1.00 20.07 C ANISOU 1906 CG2 THR A 251 2322 2604 2701 177 -373 -250 C ATOM 1907 N ARG A 252 18.256 28.682 53.994 1.00 19.89 N ANISOU 1907 N ARG A 252 2342 2602 2612 222 -329 -124 N ATOM 1908 CA ARG A 252 19.294 28.028 53.206 1.00 22.55 C ANISOU 1908 CA ARG A 252 2666 2919 2984 219 -317 -98 C ATOM 1909 C ARG A 252 18.695 27.240 52.048 1.00 22.14 C ANISOU 1909 C ARG A 252 2643 2831 2938 201 -270 -54 C ATOM 1910 O ARG A 252 19.231 27.258 50.933 1.00 23.22 O ANISOU 1910 O ARG A 252 2769 2934 3121 182 -252 -43 O ATOM 1911 CB ARG A 252 20.134 27.118 54.100 1.00 20.22 C ANISOU 1911 CB ARG A 252 2363 2661 2657 256 -338 -86 C ATOM 1912 CG ARG A 252 21.043 27.869 55.053 1.00 22.61 C ANISOU 1912 CG ARG A 252 2629 2998 2965 273 -388 -133 C ATOM 1913 CD ARG A 252 21.723 26.924 56.037 1.00 22.68 C ANISOU 1913 CD ARG A 252 2634 3053 2932 316 -410 -117 C ATOM 1914 NE ARG A 252 22.824 27.577 56.734 1.00 27.94 N ANISOU 1914 NE ARG A 252 3256 3747 3611 330 -459 -163 N ATOM 1915 CZ ARG A 252 23.662 26.965 57.563 1.00 27.18 C ANISOU 1915 CZ ARG A 252 3146 3694 3488 368 -486 -159 C ATOM 1916 NH1 ARG A 252 23.547 25.676 57.839 1.00 26.13 N ANISOU 1916 NH1 ARG A 252 3039 3578 3310 398 -468 -108 N ATOM 1917 NH2 ARG A 252 24.633 27.668 58.136 1.00 34.07 N ANISOU 1917 NH2 ARG A 252 3975 4593 4379 377 -533 -208 N ATOM 1918 N MET A 253 17.584 26.538 52.290 1.00 22.13 N ANISOU 1918 N MET A 253 2678 2839 2892 208 -248 -28 N ATOM 1919 CA MET A 253 16.966 25.762 51.218 1.00 20.91 C ANISOU 1919 CA MET A 253 2549 2653 2743 191 -204 9 C ATOM 1920 C MET A 253 16.392 26.666 50.132 1.00 20.10 C ANISOU 1920 C MET A 253 2445 2515 2675 157 -188 -3 C ATOM 1921 O MET A 253 16.490 26.347 48.941 1.00 18.54 O ANISOU 1921 O MET A 253 2252 2286 2505 140 -160 18 O ATOM 1922 CB MET A 253 15.882 24.836 51.775 1.00 20.29 C ANISOU 1922 CB MET A 253 2506 2591 2613 206 -184 36 C ATOM 1923 CG MET A 253 15.357 23.857 50.717 1.00 21.93 C ANISOU 1923 CG MET A 253 2738 2766 2827 190 -140 74 C ATOM 1924 SD MET A 253 14.051 22.738 51.248 1.00 22.53 S ANISOU 1924 SD MET A 253 2853 2854 2854 202 -110 106 S ATOM 1925 CE MET A 253 13.156 22.567 49.698 1.00 19.07 C ANISOU 1925 CE MET A 253 2431 2373 2443 165 -69 117 C ATOM 1926 N VAL A 254 15.780 27.791 50.516 1.00 19.92 N ANISOU 1926 N VAL A 254 2419 2500 2651 149 -203 -36 N ATOM 1927 CA VAL A 254 15.213 28.690 49.513 1.00 19.79 C ANISOU 1927 CA VAL A 254 2401 2452 2666 120 -187 -46 C ATOM 1928 C VAL A 254 16.314 29.257 48.628 1.00 24.96 C ANISOU 1928 C VAL A 254 3026 3078 3379 105 -188 -53 C ATOM 1929 O VAL A 254 16.099 29.494 47.433 1.00 21.36 O ANISOU 1929 O VAL A 254 2573 2591 2953 84 -162 -41 O ATOM 1930 CB VAL A 254 14.392 29.814 50.180 1.00 22.11 C ANISOU 1930 CB VAL A 254 2694 2757 2948 117 -204 -80 C ATOM 1931 CG1 VAL A 254 13.784 30.733 49.126 1.00 24.23 C ANISOU 1931 CG1 VAL A 254 2962 2993 3250 90 -185 -86 C ATOM 1932 CG2 VAL A 254 13.299 29.229 51.059 1.00 23.68 C ANISOU 1932 CG2 VAL A 254 2923 2986 3090 133 -200 -71 C ATOM 1933 N ILE A 255 17.505 29.479 49.192 1.00 19.66 N ANISOU 1933 N ILE A 255 2324 2418 2726 117 -217 -73 N ATOM 1934 CA ILE A 255 18.620 30.009 48.409 1.00 23.46 C ANISOU 1934 CA ILE A 255 2774 2873 3268 103 -218 -80 C ATOM 1935 C ILE A 255 19.003 29.037 47.300 1.00 20.07 C ANISOU 1935 C ILE A 255 2353 2420 2852 99 -185 -39 C ATOM 1936 O ILE A 255 19.222 29.435 46.151 1.00 19.29 O ANISOU 1936 O ILE A 255 2247 2289 2795 80 -164 -32 O ATOM 1937 CB ILE A 255 19.822 30.310 49.322 1.00 24.23 C ANISOU 1937 CB ILE A 255 2835 2991 3380 119 -258 -110 C ATOM 1938 CG1 ILE A 255 19.506 31.464 50.269 1.00 23.02 C ANISOU 1938 CG1 ILE A 255 2668 2856 3224 120 -290 -159 C ATOM 1939 CG2 ILE A 255 21.062 30.617 48.489 1.00 25.45 C ANISOU 1939 CG2 ILE A 255 2955 3116 3598 107 -254 -111 C ATOM 1940 CD1 ILE A 255 20.578 31.680 51.317 1.00 27.76 C ANISOU 1940 CD1 ILE A 255 3234 3486 3828 139 -334 -194 C ATOM 1941 N ILE A 256 19.102 27.749 47.636 1.00 18.55 N ANISOU 1941 N ILE A 256 2178 2245 2625 118 -180 -12 N ATOM 1942 CA ILE A 256 19.481 26.741 46.649 1.00 20.85 C ANISOU 1942 CA ILE A 256 2479 2515 2928 116 -149 25 C ATOM 1943 C ILE A 256 18.381 26.575 45.604 1.00 19.71 C ANISOU 1943 C ILE A 256 2364 2348 2778 96 -112 44 C ATOM 1944 O ILE A 256 18.661 26.371 44.416 1.00 21.88 O ANISOU 1944 O ILE A 256 2638 2596 3079 84 -86 62 O ATOM 1945 CB ILE A 256 19.812 25.413 47.353 1.00 18.54 C ANISOU 1945 CB ILE A 256 2198 2246 2601 142 -151 49 C ATOM 1946 CG1 ILE A 256 21.001 25.596 48.305 1.00 23.91 C ANISOU 1946 CG1 ILE A 256 2845 2951 3288 164 -190 30 C ATOM 1947 CG2 ILE A 256 20.108 24.320 46.336 1.00 24.54 C ANISOU 1947 CG2 ILE A 256 2970 2982 3372 140 -116 86 C ATOM 1948 CD1 ILE A 256 22.316 25.908 47.600 1.00 20.01 C ANISOU 1948 CD1 ILE A 256 2317 2436 2851 156 -192 26 C ATOM 1949 N MET A 257 17.116 26.677 46.026 1.00 17.89 N ANISOU 1949 N MET A 257 2156 2129 2510 94 -110 39 N ATOM 1950 CA MET A 257 16.005 26.605 45.082 1.00 18.66 C ANISOU 1950 CA MET A 257 2278 2210 2603 76 -80 52 C ATOM 1951 C MET A 257 16.112 27.689 44.017 1.00 20.26 C ANISOU 1951 C MET A 257 2466 2386 2848 56 -70 42 C ATOM 1952 O MET A 257 15.834 27.441 42.837 1.00 18.24 O ANISOU 1952 O MET A 257 2220 2109 2600 44 -42 61 O ATOM 1953 CB MET A 257 14.670 26.720 45.823 1.00 17.49 C ANISOU 1953 CB MET A 257 2151 2081 2413 78 -83 44 C ATOM 1954 CG MET A 257 14.322 25.513 46.682 1.00 17.56 C ANISOU 1954 CG MET A 257 2182 2112 2379 98 -80 62 C ATOM 1955 SD MET A 257 12.741 25.698 47.523 1.00 20.38 S ANISOU 1955 SD MET A 257 2562 2490 2690 100 -80 54 S ATOM 1956 CE MET A 257 11.609 25.684 46.123 1.00 17.13 C ANISOU 1956 CE MET A 257 2169 2052 2288 72 -45 64 C ATOM 1957 N VAL A 258 16.506 28.898 44.415 1.00 20.35 N ANISOU 1957 N VAL A 258 2451 2396 2884 53 -94 13 N ATOM 1958 CA VAL A 258 16.664 29.983 43.451 1.00 20.34 C ANISOU 1958 CA VAL A 258 2433 2366 2928 36 -83 6 C ATOM 1959 C VAL A 258 17.844 29.712 42.525 1.00 19.59 C ANISOU 1959 C VAL A 258 2321 2250 2873 33 -68 24 C ATOM 1960 O VAL A 258 17.744 29.887 41.304 1.00 23.85 O ANISOU 1960 O VAL A 258 2864 2766 3432 22 -40 40 O ATOM 1961 CB VAL A 258 16.816 31.328 44.182 1.00 20.04 C ANISOU 1961 CB VAL A 258 2371 2332 2914 33 -111 -32 C ATOM 1962 CG1 VAL A 258 17.186 32.426 43.198 1.00 19.82 C ANISOU 1962 CG1 VAL A 258 2320 2269 2940 16 -96 -36 C ATOM 1963 CG2 VAL A 258 15.530 31.673 44.925 1.00 22.07 C ANISOU 1963 CG2 VAL A 258 2646 2607 3132 34 -120 -48 C ATOM 1964 N ILE A 259 18.979 29.284 43.090 1.00 19.10 N ANISOU 1964 N ILE A 259 2239 2197 2821 46 -86 21 N ATOM 1965 CA ILE A 259 20.163 28.993 42.277 1.00 20.95 C ANISOU 1965 CA ILE A 259 2455 2411 3095 45 -72 37 C ATOM 1966 C ILE A 259 19.873 27.873 41.286 1.00 20.49 C ANISOU 1966 C ILE A 259 2424 2343 3019 45 -37 72 C ATOM 1967 O ILE A 259 20.274 27.938 40.117 1.00 19.38 O ANISOU 1967 O ILE A 259 2278 2178 2908 37 -11 88 O ATOM 1968 CB ILE A 259 21.360 28.642 43.177 1.00 18.26 C ANISOU 1968 CB ILE A 259 2089 2087 2763 62 -100 28 C ATOM 1969 CG1 ILE A 259 21.802 29.857 43.989 1.00 19.24 C ANISOU 1969 CG1 ILE A 259 2179 2216 2914 60 -134 -13 C ATOM 1970 CG2 ILE A 259 22.522 28.106 42.347 1.00 18.33 C ANISOU 1970 CG2 ILE A 259 2082 2076 2806 63 -82 50 C ATOM 1971 CD1 ILE A 259 22.885 29.531 44.985 1.00 18.91 C ANISOU 1971 CD1 ILE A 259 2111 2198 2874 78 -168 -27 C ATOM 1972 N ALA A 260 19.192 26.821 41.742 1.00 18.37 N ANISOU 1972 N ALA A 260 2183 2092 2703 54 -34 85 N ATOM 1973 CA ALA A 260 18.852 25.707 40.863 1.00 22.76 C ANISOU 1973 CA ALA A 260 2766 2639 3244 53 -2 113 C ATOM 1974 C ALA A 260 17.926 26.150 39.736 1.00 20.56 C ANISOU 1974 C ALA A 260 2502 2345 2965 36 23 117 C ATOM 1975 O ALA A 260 18.048 25.677 38.602 1.00 19.83 O ANISOU 1975 O ALA A 260 2418 2237 2882 32 51 136 O ATOM 1976 CB ALA A 260 18.211 24.582 41.676 1.00 17.83 C ANISOU 1976 CB ALA A 260 2167 2035 2573 65 -3 123 C ATOM 1977 N PHE A 261 16.979 27.044 40.037 1.00 22.00 N ANISOU 1977 N PHE A 261 2689 2534 3137 28 14 100 N ATOM 1978 CA PHE A 261 16.083 27.556 39.004 1.00 20.97 C ANISOU 1978 CA PHE A 261 2570 2392 3006 15 35 103 C ATOM 1979 C PHE A 261 16.851 28.331 37.939 1.00 21.37 C ANISOU 1979 C PHE A 261 2600 2418 3102 9 50 109 C ATOM 1980 O PHE A 261 16.576 28.196 36.740 1.00 24.12 O ANISOU 1980 O PHE A 261 2959 2755 3450 5 78 126 O ATOM 1981 CB PHE A 261 15.011 28.441 39.642 1.00 20.54 C ANISOU 1981 CB PHE A 261 2520 2350 2936 10 20 83 C ATOM 1982 CG PHE A 261 13.976 28.945 38.677 1.00 19.92 C ANISOU 1982 CG PHE A 261 2454 2263 2851 0 40 87 C ATOM 1983 CD1 PHE A 261 14.152 30.149 38.015 1.00 20.48 C ANISOU 1983 CD1 PHE A 261 2508 2316 2956 -6 46 84 C ATOM 1984 CD2 PHE A 261 12.815 28.224 38.448 1.00 18.49 C ANISOU 1984 CD2 PHE A 261 2300 2093 2633 -3 53 95 C ATOM 1985 CE1 PHE A 261 13.199 30.615 37.129 1.00 20.60 C ANISOU 1985 CE1 PHE A 261 2535 2328 2964 -12 65 91 C ATOM 1986 CE2 PHE A 261 11.856 28.689 37.563 1.00 25.80 C ANISOU 1986 CE2 PHE A 261 3235 3015 3551 -11 69 97 C ATOM 1987 CZ PHE A 261 12.056 29.883 36.900 1.00 20.00 C ANISOU 1987 CZ PHE A 261 2486 2267 2848 -14 75 96 C ATOM 1988 N LEU A 262 17.805 29.166 38.360 1.00 18.75 N ANISOU 1988 N LEU A 262 2237 2078 2808 10 33 95 N ATOM 1989 CA LEU A 262 18.568 29.957 37.401 1.00 24.27 C ANISOU 1989 CA LEU A 262 2913 2751 3555 4 50 102 C ATOM 1990 C LEU A 262 19.414 29.064 36.503 1.00 23.66 C ANISOU 1990 C LEU A 262 2836 2663 3489 10 73 127 C ATOM 1991 O LEU A 262 19.499 29.293 35.291 1.00 24.53 O ANISOU 1991 O LEU A 262 2948 2756 3616 7 102 144 O ATOM 1992 CB LEU A 262 19.438 30.977 38.134 1.00 23.04 C ANISOU 1992 CB LEU A 262 2722 2589 3444 3 25 78 C ATOM 1993 CG LEU A 262 18.647 32.109 38.793 1.00 26.87 C ANISOU 1993 CG LEU A 262 3203 3077 3928 -4 7 51 C ATOM 1994 CD1 LEU A 262 19.530 32.954 39.703 1.00 26.11 C ANISOU 1994 CD1 LEU A 262 3071 2978 3872 -5 -22 20 C ATOM 1995 CD2 LEU A 262 17.996 32.980 37.731 1.00 24.43 C ANISOU 1995 CD2 LEU A 262 2900 2748 3634 -13 34 62 C ATOM 1996 N ILE A 263 20.040 28.037 37.079 1.00 23.19 N ANISOU 1996 N ILE A 263 2777 2614 3421 19 63 131 N ATOM 1997 CA ILE A 263 20.787 27.070 36.277 1.00 26.54 C ANISOU 1997 CA ILE A 263 3204 3028 3852 26 87 155 C ATOM 1998 C ILE A 263 19.870 26.412 35.253 1.00 23.92 C ANISOU 1998 C ILE A 263 2904 2695 3488 23 116 171 C ATOM 1999 O ILE A 263 20.246 26.209 34.090 1.00 21.92 O ANISOU 1999 O ILE A 263 2652 2428 3249 24 144 189 O ATOM 2000 CB ILE A 263 21.452 26.026 37.197 1.00 20.24 C ANISOU 2000 CB ILE A 263 2403 2244 3043 39 70 156 C ATOM 2001 CG1 ILE A 263 22.652 26.633 37.921 1.00 22.21 C ANISOU 2001 CG1 ILE A 263 2614 2493 3332 44 44 141 C ATOM 2002 CG2 ILE A 263 21.847 24.782 36.422 1.00 22.58 C ANISOU 2002 CG2 ILE A 263 2712 2532 3333 46 97 181 C ATOM 2003 CD1 ILE A 263 23.478 25.614 38.669 1.00 22.13 C ANISOU 2003 CD1 ILE A 263 2597 2497 3314 61 29 147 C ATOM 2004 N CYS A 264 18.647 26.084 35.668 1.00 20.94 N ANISOU 2004 N CYS A 264 2552 2334 3069 20 110 164 N ATOM 2005 CA CYS A 264 17.741 25.351 34.794 1.00 24.69 C ANISOU 2005 CA CYS A 264 3055 2811 3514 17 135 175 C ATOM 2006 C CYS A 264 17.239 26.212 33.638 1.00 19.77 C ANISOU 2006 C CYS A 264 2435 2181 2898 10 154 179 C ATOM 2007 O CYS A 264 17.160 25.738 32.502 1.00 26.06 O ANISOU 2007 O CYS A 264 3243 2972 3687 12 180 192 O ATOM 2008 CB CYS A 264 16.569 24.805 35.608 1.00 20.22 C ANISOU 2008 CB CYS A 264 2512 2264 2906 15 124 166 C ATOM 2009 SG CYS A 264 15.448 23.757 34.672 1.00 24.93 S ANISOU 2009 SG CYS A 264 3141 2863 3468 10 152 174 S ATOM 2010 N TRP A 265 16.897 27.478 33.895 1.00 21.15 N ANISOU 2010 N TRP A 265 2598 2354 3084 5 142 167 N ATOM 2011 CA TRP A 265 16.143 28.251 32.916 1.00 18.70 C ANISOU 2011 CA TRP A 265 2294 2041 2772 2 159 172 C ATOM 2012 C TRP A 265 16.926 29.348 32.206 1.00 23.65 C ANISOU 2012 C TRP A 265 2897 2647 3443 3 173 182 C ATOM 2013 O TRP A 265 16.490 29.785 31.136 1.00 20.34 O ANISOU 2013 O TRP A 265 2484 2224 3020 5 195 194 O ATOM 2014 CB TRP A 265 14.898 28.873 33.575 1.00 20.55 C ANISOU 2014 CB TRP A 265 2537 2289 2983 -4 142 155 C ATOM 2015 CG TRP A 265 13.847 27.849 33.915 1.00 21.08 C ANISOU 2015 CG TRP A 265 2630 2375 3004 -6 139 150 C ATOM 2016 CD1 TRP A 265 13.627 27.277 35.133 1.00 22.12 C ANISOU 2016 CD1 TRP A 265 2767 2519 3117 -6 119 139 C ATOM 2017 CD2 TRP A 265 12.895 27.260 33.018 1.00 22.96 C ANISOU 2017 CD2 TRP A 265 2890 2623 3212 -8 158 156 C ATOM 2018 NE1 TRP A 265 12.590 26.378 35.054 1.00 22.39 N ANISOU 2018 NE1 TRP A 265 2826 2566 3115 -9 127 140 N ATOM 2019 CE2 TRP A 265 12.126 26.348 33.766 1.00 21.66 C ANISOU 2019 CE2 TRP A 265 2742 2472 3016 -11 149 147 C ATOM 2020 CE3 TRP A 265 12.616 27.417 31.658 1.00 23.70 C ANISOU 2020 CE3 TRP A 265 2990 2715 3302 -6 181 167 C ATOM 2021 CZ2 TRP A 265 11.097 25.598 33.198 1.00 20.14 C ANISOU 2021 CZ2 TRP A 265 2570 2289 2792 -16 163 146 C ATOM 2022 CZ3 TRP A 265 11.599 26.673 31.099 1.00 18.81 C ANISOU 2022 CZ3 TRP A 265 2390 2109 2646 -8 191 164 C ATOM 2023 CH2 TRP A 265 10.850 25.775 31.868 1.00 24.40 C ANISOU 2023 CH2 TRP A 265 3113 2829 3328 -14 182 152 C ATOM 2024 N LEU A 266 18.051 29.809 32.756 1.00 23.11 N ANISOU 2024 N LEU A 266 2800 2564 3416 3 161 177 N ATOM 2025 CA LEU A 266 18.801 30.875 32.090 1.00 21.17 C ANISOU 2025 CA LEU A 266 2530 2295 3220 3 178 186 C ATOM 2026 C LEU A 266 19.331 30.493 30.711 1.00 24.52 C ANISOU 2026 C LEU A 266 2958 2709 3652 11 214 214 C ATOM 2027 O LEU A 266 19.258 31.341 29.803 1.00 23.19 O ANISOU 2027 O LEU A 266 2784 2528 3501 14 237 229 O ATOM 2028 CB LEU A 266 19.944 31.368 32.990 1.00 27.12 C ANISOU 2028 CB LEU A 266 3249 3036 4020 0 157 171 C ATOM 2029 CG LEU A 266 19.577 32.309 34.144 1.00 25.08 C ANISOU 2029 CG LEU A 266 2977 2780 3771 -7 126 142 C ATOM 2030 CD1 LEU A 266 20.828 32.745 34.891 1.00 25.04 C ANISOU 2030 CD1 LEU A 266 2935 2764 3816 -9 106 124 C ATOM 2031 CD2 LEU A 266 18.801 33.525 33.667 1.00 22.61 C ANISOU 2031 CD2 LEU A 266 2665 2456 3469 -12 139 142 C ATOM 2032 N PRO A 267 19.895 29.298 30.480 1.00 22.76 N ANISOU 2032 N PRO A 267 2741 2488 3417 16 222 223 N ATOM 2033 CA PRO A 267 20.312 28.970 29.104 1.00 25.97 C ANISOU 2033 CA PRO A 267 3153 2887 3827 26 258 248 C ATOM 2034 C PRO A 267 19.175 29.015 28.091 1.00 26.07 C ANISOU 2034 C PRO A 267 3192 2912 3802 30 277 257 C ATOM 2035 O PRO A 267 19.355 29.557 26.991 1.00 22.44 O ANISOU 2035 O PRO A 267 2728 2444 3353 38 306 277 O ATOM 2036 CB PRO A 267 20.895 27.556 29.248 1.00 26.20 C ANISOU 2036 CB PRO A 267 3190 2922 3844 30 258 251 C ATOM 2037 CG PRO A 267 21.334 27.478 30.657 1.00 21.05 C ANISOU 2037 CG PRO A 267 2522 2271 3204 26 224 233 C ATOM 2038 CD PRO A 267 20.314 28.252 31.432 1.00 20.66 C ANISOU 2038 CD PRO A 267 2477 2233 3141 18 201 214 C ATOM 2039 N TYR A 268 18.005 28.466 28.432 1.00 23.08 N ANISOU 2039 N TYR A 268 2838 2555 3377 25 263 243 N ATOM 2040 CA TYR A 268 16.864 28.531 27.523 1.00 21.75 C ANISOU 2040 CA TYR A 268 2691 2402 3172 29 278 247 C ATOM 2041 C TYR A 268 16.430 29.973 27.293 1.00 21.12 C ANISOU 2041 C TYR A 268 2602 2317 3108 30 281 252 C ATOM 2042 O TYR A 268 16.176 30.383 26.153 1.00 23.43 O ANISOU 2042 O TYR A 268 2899 2612 3392 41 306 270 O ATOM 2043 CB TYR A 268 15.697 27.704 28.074 1.00 19.25 C ANISOU 2043 CB TYR A 268 2397 2106 2809 22 260 228 C ATOM 2044 CG TYR A 268 14.461 27.727 27.191 1.00 23.49 C ANISOU 2044 CG TYR A 268 2954 2663 3308 25 271 228 C ATOM 2045 CD1 TYR A 268 14.395 26.960 26.037 1.00 23.45 C ANISOU 2045 CD1 TYR A 268 2963 2666 3279 33 294 235 C ATOM 2046 CD2 TYR A 268 13.365 28.521 27.513 1.00 20.33 C ANISOU 2046 CD2 TYR A 268 2557 2273 2894 21 258 218 C ATOM 2047 CE1 TYR A 268 13.273 26.982 25.222 1.00 20.93 C ANISOU 2047 CE1 TYR A 268 2660 2369 2923 38 301 231 C ATOM 2048 CE2 TYR A 268 12.241 28.546 26.710 1.00 21.04 C ANISOU 2048 CE2 TYR A 268 2663 2384 2949 25 266 218 C ATOM 2049 CZ TYR A 268 12.199 27.775 25.566 1.00 23.43 C ANISOU 2049 CZ TYR A 268 2978 2698 3228 34 286 223 C ATOM 2050 OH TYR A 268 11.079 27.801 24.762 1.00 23.86 O ANISOU 2050 OH TYR A 268 3045 2775 3244 40 292 219 O ATOM 2051 N ALA A 269 16.356 30.762 28.367 1.00 22.82 N ANISOU 2051 N ALA A 269 2802 2525 3343 21 258 237 N ATOM 2052 CA ALA A 269 15.904 32.147 28.259 1.00 24.76 C ANISOU 2052 CA ALA A 269 3037 2762 3607 21 261 240 C ATOM 2053 C ALA A 269 16.840 32.977 27.387 1.00 20.04 C ANISOU 2053 C ALA A 269 2419 2140 3055 30 290 264 C ATOM 2054 O ALA A 269 16.387 33.826 26.606 1.00 18.30 O ANISOU 2054 O ALA A 269 2200 1917 2836 39 310 281 O ATOM 2055 CB ALA A 269 15.785 32.761 29.655 1.00 25.63 C ANISOU 2055 CB ALA A 269 3134 2868 3735 10 229 215 C ATOM 2056 N GLY A 270 18.149 32.762 27.523 1.00 18.76 N ANISOU 2056 N GLY A 270 2237 1960 2931 29 294 269 N ATOM 2057 CA GLY A 270 19.102 33.519 26.724 1.00 25.35 C ANISOU 2057 CA GLY A 270 3049 2768 3814 36 324 293 C ATOM 2058 C GLY A 270 19.022 33.194 25.243 1.00 20.41 C ANISOU 2058 C GLY A 270 2440 2150 3165 54 361 322 C ATOM 2059 O GLY A 270 19.030 34.095 24.400 1.00 17.85 O ANISOU 2059 O GLY A 270 2109 1814 2858 64 390 346 O ATOM 2060 N VAL A 271 18.944 31.904 24.904 1.00 18.96 N ANISOU 2060 N VAL A 271 2277 1986 2940 58 362 321 N ATOM 2061 CA VAL A 271 18.859 31.510 23.496 1.00 18.74 C ANISOU 2061 CA VAL A 271 2266 1969 2885 76 396 345 C ATOM 2062 C VAL A 271 17.557 32.009 22.880 1.00 19.58 C ANISOU 2062 C VAL A 271 2391 2096 2952 85 401 350 C ATOM 2063 O VAL A 271 17.542 32.558 21.770 1.00 22.35 O ANISOU 2063 O VAL A 271 2743 2447 3301 103 432 376 O ATOM 2064 CB VAL A 271 19.000 29.984 23.352 1.00 22.28 C ANISOU 2064 CB VAL A 271 2732 2432 3299 77 393 336 C ATOM 2065 CG1 VAL A 271 18.729 29.555 21.914 1.00 20.80 C ANISOU 2065 CG1 VAL A 271 2565 2262 3075 96 424 353 C ATOM 2066 CG2 VAL A 271 20.391 29.541 23.784 1.00 26.50 C ANISOU 2066 CG2 VAL A 271 3247 2947 3876 73 394 338 C ATOM 2067 N ALA A 272 16.445 31.832 23.596 1.00 18.51 N ANISOU 2067 N ALA A 272 2269 1979 2784 74 372 325 N ATOM 2068 CA ALA A 272 15.152 32.266 23.077 1.00 18.39 C ANISOU 2068 CA ALA A 272 2270 1986 2731 82 374 327 C ATOM 2069 C ALA A 272 15.134 33.768 22.825 1.00 20.92 C ANISOU 2069 C ALA A 272 2575 2290 3085 91 390 347 C ATOM 2070 O ALA A 272 14.567 34.230 21.826 1.00 21.01 O ANISOU 2070 O ALA A 272 2595 2315 3074 109 411 368 O ATOM 2071 CB ALA A 272 14.035 31.875 24.048 1.00 24.68 C ANISOU 2071 CB ALA A 272 3080 2801 3496 67 340 297 C ATOM 2072 N PHE A 273 15.732 34.548 23.729 1.00 19.09 N ANISOU 2072 N PHE A 273 2319 2030 2905 78 380 341 N ATOM 2073 CA PHE A 273 15.799 35.991 23.517 1.00 26.26 C ANISOU 2073 CA PHE A 273 3209 2914 3853 85 398 360 C ATOM 2074 C PHE A 273 16.728 36.347 22.364 1.00 20.39 C ANISOU 2074 C PHE A 273 2455 2154 3140 103 441 397 C ATOM 2075 O PHE A 273 16.491 37.339 21.667 1.00 20.50 O ANISOU 2075 O PHE A 273 2465 2160 3166 118 467 424 O ATOM 2076 CB PHE A 273 16.241 36.702 24.798 1.00 21.28 C ANISOU 2076 CB PHE A 273 2553 2256 3275 65 376 338 C ATOM 2077 CG PHE A 273 16.234 38.201 24.687 1.00 23.44 C ANISOU 2077 CG PHE A 273 2808 2502 3596 69 393 352 C ATOM 2078 CD1 PHE A 273 15.040 38.899 24.630 1.00 21.49 C ANISOU 2078 CD1 PHE A 273 2572 2266 3327 76 391 353 C ATOM 2079 CD2 PHE A 273 17.422 38.912 24.640 1.00 24.76 C ANISOU 2079 CD2 PHE A 273 2944 2631 3831 67 413 364 C ATOM 2080 CE1 PHE A 273 15.034 40.284 24.524 1.00 26.73 C ANISOU 2080 CE1 PHE A 273 3217 2901 4037 80 410 367 C ATOM 2081 CE2 PHE A 273 17.424 40.292 24.532 1.00 25.53 C ANISOU 2081 CE2 PHE A 273 3024 2700 3978 70 433 377 C ATOM 2082 CZ PHE A 273 16.232 40.979 24.475 1.00 23.10 C ANISOU 2082 CZ PHE A 273 2727 2400 3648 77 432 379 C ATOM 2083 N TYR A 274 17.789 35.563 22.151 1.00 18.35 N ANISOU 2083 N TYR A 274 2191 1888 2893 102 450 402 N ATOM 2084 CA TYR A 274 18.657 35.796 20.999 1.00 20.42 C ANISOU 2084 CA TYR A 274 2444 2136 3177 122 493 439 C ATOM 2085 C TYR A 274 17.918 35.557 19.690 1.00 19.71 C ANISOU 2085 C TYR A 274 2381 2078 3031 148 517 461 C ATOM 2086 O TYR A 274 18.058 36.334 18.735 1.00 19.13 O ANISOU 2086 O TYR A 274 2302 1996 2968 169 554 497 O ATOM 2087 CB TYR A 274 19.895 34.902 21.078 1.00 21.22 C ANISOU 2087 CB TYR A 274 2536 2227 3299 116 496 436 C ATOM 2088 CG TYR A 274 20.837 35.073 19.911 1.00 28.52 C ANISOU 2088 CG TYR A 274 3452 3138 4248 136 543 474 C ATOM 2089 CD1 TYR A 274 21.809 36.061 19.922 1.00 29.58 C ANISOU 2089 CD1 TYR A 274 3553 3233 4454 135 566 493 C ATOM 2090 CD2 TYR A 274 20.750 34.252 18.792 1.00 26.43 C ANISOU 2090 CD2 TYR A 274 3210 2898 3935 157 565 490 C ATOM 2091 CE1 TYR A 274 22.669 36.227 18.857 1.00 30.03 C ANISOU 2091 CE1 TYR A 274 3601 3276 4534 154 612 531 C ATOM 2092 CE2 TYR A 274 21.605 34.411 17.721 1.00 30.95 C ANISOU 2092 CE2 TYR A 274 3775 3460 4527 178 610 526 C ATOM 2093 CZ TYR A 274 22.561 35.401 17.761 1.00 28.40 C ANISOU 2093 CZ TYR A 274 3418 3096 4275 177 634 548 C ATOM 2094 OH TYR A 274 23.415 35.565 16.704 1.00 32.42 O ANISOU 2094 OH TYR A 274 3919 3593 4805 198 682 586 O ATOM 2095 N ILE A 275 17.139 34.477 19.619 1.00 21.04 N ANISOU 2095 N ILE A 275 2575 2281 3137 147 498 441 N ATOM 2096 CA ILE A 275 16.388 34.195 18.400 1.00 23.91 C ANISOU 2096 CA ILE A 275 2962 2680 3443 172 516 455 C ATOM 2097 C ILE A 275 15.396 35.317 18.128 1.00 21.10 C ANISOU 2097 C ILE A 275 2608 2332 3076 184 520 469 C ATOM 2098 O ILE A 275 15.301 35.824 17.006 1.00 20.51 O ANISOU 2098 O ILE A 275 2537 2267 2988 213 553 502 O ATOM 2099 CB ILE A 275 15.696 32.822 18.503 1.00 20.88 C ANISOU 2099 CB ILE A 275 2602 2329 3001 164 490 423 C ATOM 2100 CG1 ILE A 275 16.746 31.710 18.540 1.00 21.29 C ANISOU 2100 CG1 ILE A 275 2654 2372 3064 158 494 417 C ATOM 2101 CG2 ILE A 275 14.721 32.617 17.346 1.00 23.44 C ANISOU 2101 CG2 ILE A 275 2949 2694 3264 188 501 430 C ATOM 2102 CD1 ILE A 275 16.178 30.311 18.674 1.00 23.60 C ANISOU 2102 CD1 ILE A 275 2968 2690 3308 149 473 386 C ATOM 2103 N PHE A 276 14.693 35.763 19.172 1.00 20.66 N ANISOU 2103 N PHE A 276 2549 2272 3029 166 491 446 N ATOM 2104 CA PHE A 276 13.669 36.793 19.021 1.00 24.37 C ANISOU 2104 CA PHE A 276 3021 2750 3489 177 492 457 C ATOM 2105 C PHE A 276 14.233 38.084 18.432 1.00 22.78 C ANISOU 2105 C PHE A 276 2801 2519 3334 196 531 498 C ATOM 2106 O PHE A 276 13.523 38.804 17.720 1.00 19.62 O ANISOU 2106 O PHE A 276 2408 2133 2916 220 549 522 O ATOM 2107 CB PHE A 276 13.016 37.042 20.385 1.00 22.13 C ANISOU 2107 CB PHE A 276 2733 2460 3215 152 454 423 C ATOM 2108 CG PHE A 276 12.011 38.162 20.400 1.00 23.14 C ANISOU 2108 CG PHE A 276 2859 2591 3340 161 455 431 C ATOM 2109 CD1 PHE A 276 10.785 38.027 19.765 1.00 25.65 C ANISOU 2109 CD1 PHE A 276 3197 2949 3600 178 452 433 C ATOM 2110 CD2 PHE A 276 12.277 39.337 21.092 1.00 23.62 C ANISOU 2110 CD2 PHE A 276 2900 2616 3460 152 457 434 C ATOM 2111 CE1 PHE A 276 9.852 39.052 19.792 1.00 23.65 C ANISOU 2111 CE1 PHE A 276 2942 2699 3346 188 452 442 C ATOM 2112 CE2 PHE A 276 11.349 40.367 21.129 1.00 22.91 C ANISOU 2112 CE2 PHE A 276 2808 2526 3370 161 458 441 C ATOM 2113 CZ PHE A 276 10.135 40.223 20.475 1.00 27.36 C ANISOU 2113 CZ PHE A 276 3392 3130 3874 180 457 447 C ATOM 2114 N THR A 277 15.500 38.387 18.700 1.00 22.12 N ANISOU 2114 N THR A 277 2694 2396 3314 187 546 507 N ATOM 2115 CA THR A 277 16.132 39.603 18.209 1.00 19.39 C ANISOU 2115 CA THR A 277 2328 2016 3024 201 587 546 C ATOM 2116 C THR A 277 17.001 39.366 16.981 1.00 23.21 C ANISOU 2116 C THR A 277 2812 2499 3508 226 630 584 C ATOM 2117 O THR A 277 17.622 40.312 16.486 1.00 25.30 O ANISOU 2117 O THR A 277 3059 2733 3821 240 670 620 O ATOM 2118 CB THR A 277 16.964 40.248 19.325 1.00 22.03 C ANISOU 2118 CB THR A 277 2631 2303 3437 174 577 530 C ATOM 2119 OG1 THR A 277 17.818 39.262 19.924 1.00 19.91 O ANISOU 2119 OG1 THR A 277 2356 2030 3178 154 556 504 O ATOM 2120 CG2 THR A 277 16.046 40.823 20.398 1.00 23.70 C ANISOU 2120 CG2 THR A 277 2841 2512 3652 157 543 500 C ATOM 2121 N HIS A 278 17.078 38.128 16.498 1.00 19.69 N ANISOU 2121 N HIS A 278 2385 2084 3012 231 626 575 N ATOM 2122 CA HIS A 278 17.824 37.767 15.296 1.00 23.42 C ANISOU 2122 CA HIS A 278 2861 2562 3474 257 666 608 C ATOM 2123 C HIS A 278 16.999 36.794 14.462 1.00 21.40 C ANISOU 2123 C HIS A 278 2638 2361 3134 276 659 601 C ATOM 2124 O HIS A 278 17.464 35.720 14.082 1.00 23.32 O ANISOU 2124 O HIS A 278 2891 2618 3353 279 662 592 O ATOM 2125 CB HIS A 278 19.186 37.166 15.634 1.00 24.80 C ANISOU 2125 CB HIS A 278 3020 2711 3693 241 669 601 C ATOM 2126 CG HIS A 278 20.037 38.046 16.493 1.00 29.32 C ANISOU 2126 CG HIS A 278 3558 3232 4351 220 671 601 C ATOM 2127 ND1 HIS A 278 19.737 38.314 17.811 1.00 19.62 N ANISOU 2127 ND1 HIS A 278 2318 1990 3147 190 631 566 N ATOM 2128 CD2 HIS A 278 21.176 38.723 16.221 1.00 27.08 C ANISOU 2128 CD2 HIS A 278 3246 2909 4134 224 708 631 C ATOM 2129 CE1 HIS A 278 20.653 39.121 18.313 1.00 23.86 C ANISOU 2129 CE1 HIS A 278 2821 2482 3761 177 642 570 C ATOM 2130 NE2 HIS A 278 21.540 39.381 17.370 1.00 22.13 N ANISOU 2130 NE2 HIS A 278 2590 2245 3572 196 689 609 N ATOM 2131 N GLN A 279 15.739 37.142 14.219 1.00 26.25 N ANISOU 2131 N GLN A 279 3266 3004 3702 290 649 600 N ATOM 2132 CA GLN A 279 14.859 36.256 13.467 1.00 24.70 C ANISOU 2132 CA GLN A 279 3097 2861 3426 307 639 587 C ATOM 2133 C GLN A 279 15.392 36.039 12.053 1.00 25.99 C ANISOU 2133 C GLN A 279 3270 3044 3563 343 681 621 C ATOM 2134 O GLN A 279 15.845 36.973 11.387 1.00 25.72 O ANISOU 2134 O GLN A 279 3225 2994 3554 369 722 667 O ATOM 2135 CB GLN A 279 13.437 36.827 13.428 1.00 25.71 C ANISOU 2135 CB GLN A 279 3235 3019 3516 317 623 584 C ATOM 2136 CG GLN A 279 12.731 36.825 14.782 1.00 23.66 C ANISOU 2136 CG GLN A 279 2971 2750 3266 283 578 544 C ATOM 2137 CD GLN A 279 11.315 37.358 14.704 1.00 23.93 C ANISOU 2137 CD GLN A 279 3015 2815 3263 294 564 541 C ATOM 2138 OE1 GLN A 279 10.974 38.115 13.798 1.00 25.58 O ANISOU 2138 OE1 GLN A 279 3226 3038 3456 327 590 576 O ATOM 2139 NE2 GLN A 279 10.482 36.965 15.656 1.00 24.45 N ANISOU 2139 NE2 GLN A 279 3085 2890 3314 268 523 501 N ATOM 2140 N GLY A 280 15.362 34.784 11.610 1.00 26.81 N ANISOU 2140 N GLY A 280 3391 3178 3618 346 672 598 N ATOM 2141 CA GLY A 280 15.801 34.432 10.276 1.00 29.52 C ANISOU 2141 CA GLY A 280 3744 3544 3926 381 708 623 C ATOM 2142 C GLY A 280 17.291 34.235 10.109 1.00 29.70 C ANISOU 2142 C GLY A 280 3754 3533 3996 381 740 644 C ATOM 2143 O GLY A 280 17.734 33.964 8.986 1.00 27.55 O ANISOU 2143 O GLY A 280 3491 3280 3698 412 774 667 O ATOM 2144 N SER A 281 18.077 34.356 11.178 1.00 28.12 N ANISOU 2144 N SER A 281 3533 3287 3864 348 730 635 N ATOM 2145 CA SER A 281 19.521 34.189 11.090 1.00 28.44 C ANISOU 2145 CA SER A 281 3557 3294 3955 346 759 653 C ATOM 2146 C SER A 281 19.875 32.708 10.964 1.00 29.67 C ANISOU 2146 C SER A 281 3727 3467 4080 340 748 624 C ATOM 2147 O SER A 281 19.016 31.827 11.031 1.00 28.92 O ANISOU 2147 O SER A 281 3652 3404 3930 334 718 588 O ATOM 2148 CB SER A 281 20.210 34.829 12.296 1.00 28.73 C ANISOU 2148 CB SER A 281 3564 3280 4074 314 748 649 C ATOM 2149 OG SER A 281 19.653 34.385 13.520 1.00 23.51 O ANISOU 2149 OG SER A 281 2904 2619 3409 280 697 604 O ATOM 2150 N ASP A 282 21.161 32.428 10.769 1.00 27.24 N ANISOU 2150 N ASP A 282 3406 3134 3810 342 775 640 N ATOM 2151 CA ASP A 282 21.621 31.072 10.475 1.00 30.01 C ANISOU 2151 CA ASP A 282 3770 3498 4136 342 775 620 C ATOM 2152 C ASP A 282 21.918 30.338 11.778 1.00 28.55 C ANISOU 2152 C ASP A 282 3575 3291 3981 304 736 582 C ATOM 2153 O ASP A 282 23.017 30.441 12.327 1.00 32.85 O ANISOU 2153 O ASP A 282 4097 3799 4587 290 743 589 O ATOM 2154 CB ASP A 282 22.849 31.105 9.572 1.00 29.38 C ANISOU 2154 CB ASP A 282 3680 3404 4079 367 825 658 C ATOM 2155 CG ASP A 282 23.220 29.731 9.044 1.00 36.95 C ANISOU 2155 CG ASP A 282 4655 4382 5001 375 830 638 C ATOM 2156 OD1 ASP A 282 22.393 28.800 9.171 1.00 33.87 O ANISOU 2156 OD1 ASP A 282 4288 4022 4560 366 799 598 O ATOM 2157 OD2 ASP A 282 24.338 29.580 8.503 1.00 43.52 O ANISOU 2157 OD2 ASP A 282 5478 5199 5858 389 868 663 O ATOM 2158 N PHE A 283 20.944 29.574 12.263 1.00 26.33 N ANISOU 2158 N PHE A 283 3314 3034 3658 288 697 541 N ATOM 2159 CA PHE A 283 21.151 28.654 13.372 1.00 27.84 C ANISOU 2159 CA PHE A 283 3502 3212 3865 257 664 506 C ATOM 2160 C PHE A 283 20.585 27.294 12.987 1.00 26.05 C ANISOU 2160 C PHE A 283 3302 3017 3580 259 653 474 C ATOM 2161 O PHE A 283 19.730 27.183 12.105 1.00 19.88 O ANISOU 2161 O PHE A 283 2540 2272 2742 278 658 470 O ATOM 2162 CB PHE A 283 20.516 29.165 14.683 1.00 23.75 C ANISOU 2162 CB PHE A 283 2975 2682 3367 229 624 486 C ATOM 2163 CG PHE A 283 19.054 29.514 14.569 1.00 24.07 C ANISOU 2163 CG PHE A 283 3033 2754 3360 232 606 474 C ATOM 2164 CD1 PHE A 283 18.080 28.564 14.821 1.00 25.14 C ANISOU 2164 CD1 PHE A 283 3188 2915 3448 221 576 437 C ATOM 2165 CD2 PHE A 283 18.657 30.800 14.241 1.00 28.12 C ANISOU 2165 CD2 PHE A 283 3539 3267 3879 246 619 500 C ATOM 2166 CE1 PHE A 283 16.738 28.881 14.726 1.00 24.02 C ANISOU 2166 CE1 PHE A 283 3058 2802 3264 223 559 425 C ATOM 2167 CE2 PHE A 283 17.304 31.131 14.145 1.00 26.47 C ANISOU 2167 CE2 PHE A 283 3344 3087 3627 250 602 490 C ATOM 2168 CZ PHE A 283 16.347 30.170 14.385 1.00 23.64 C ANISOU 2168 CZ PHE A 283 3004 2757 3220 239 571 452 C ATOM 2169 N GLY A 284 21.093 26.251 13.640 1.00 25.39 N ANISOU 2169 N GLY A 284 3217 2918 3510 241 639 452 N ATOM 2170 CA GLY A 284 20.678 24.900 13.342 1.00 25.43 C ANISOU 2170 CA GLY A 284 3246 2946 3471 240 631 420 C ATOM 2171 C GLY A 284 19.752 24.312 14.388 1.00 19.19 C ANISOU 2171 C GLY A 284 2464 2161 2667 213 590 382 C ATOM 2172 O GLY A 284 19.379 24.969 15.366 1.00 21.61 O ANISOU 2172 O GLY A 284 2759 2456 2994 195 565 380 O ATOM 2173 N PRO A 285 19.364 23.045 14.192 1.00 21.13 N ANISOU 2173 N PRO A 285 2728 2421 2878 210 584 352 N ATOM 2174 CA PRO A 285 18.436 22.406 15.142 1.00 22.33 C ANISOU 2174 CA PRO A 285 2889 2578 3018 184 548 316 C ATOM 2175 C PRO A 285 19.027 22.140 16.516 1.00 21.37 C ANISOU 2175 C PRO A 285 2755 2425 2942 161 529 313 C ATOM 2176 O PRO A 285 18.283 22.146 17.505 1.00 24.74 O ANISOU 2176 O PRO A 285 3182 2852 3367 142 499 296 O ATOM 2177 CB PRO A 285 18.054 21.094 14.438 1.00 20.10 C ANISOU 2177 CB PRO A 285 2628 2315 2695 189 555 286 C ATOM 2178 CG PRO A 285 19.111 20.875 13.406 1.00 25.79 C ANISOU 2178 CG PRO A 285 3348 3033 3419 213 591 306 C ATOM 2179 CD PRO A 285 19.581 22.229 12.985 1.00 23.01 C ANISOU 2179 CD PRO A 285 2981 2678 3083 231 610 346 C ATOM 2180 N ILE A 286 20.332 21.879 16.618 1.00 20.31 N ANISOU 2180 N ILE A 286 2606 2265 2845 165 545 330 N ATOM 2181 CA ILE A 286 20.905 21.599 17.928 1.00 26.19 C ANISOU 2181 CA ILE A 286 3338 2984 3629 146 525 326 C ATOM 2182 C ILE A 286 20.927 22.855 18.793 1.00 22.97 C ANISOU 2182 C ILE A 286 2910 2565 3254 136 506 338 C ATOM 2183 O ILE A 286 20.929 22.762 20.027 1.00 22.25 O ANISOU 2183 O ILE A 286 2811 2463 3181 119 479 328 O ATOM 2184 CB ILE A 286 22.310 20.983 17.763 1.00 25.12 C ANISOU 2184 CB ILE A 286 3191 2826 3526 154 547 340 C ATOM 2185 CG1 ILE A 286 22.237 19.715 16.912 1.00 28.28 C ANISOU 2185 CG1 ILE A 286 3613 3237 3895 164 567 325 C ATOM 2186 CG2 ILE A 286 22.924 20.655 19.114 1.00 20.97 C ANISOU 2186 CG2 ILE A 286 2650 2278 3038 139 525 337 C ATOM 2187 CD1 ILE A 286 21.544 18.546 17.600 1.00 28.54 C ANISOU 2187 CD1 ILE A 286 3662 3272 3911 148 546 293 C ATOM 2188 N PHE A 287 20.871 24.030 18.165 1.00 18.50 N ANISOU 2188 N PHE A 287 2335 2002 2691 148 521 359 N ATOM 2189 CA PHE A 287 21.033 25.295 18.876 1.00 24.96 C ANISOU 2189 CA PHE A 287 3131 2805 3548 139 509 372 C ATOM 2190 C PHE A 287 20.027 25.435 20.022 1.00 27.06 C ANISOU 2190 C PHE A 287 3401 3077 3802 119 470 348 C ATOM 2191 O PHE A 287 20.396 25.785 21.150 1.00 23.78 O ANISOU 2191 O PHE A 287 2969 2646 3422 105 449 343 O ATOM 2192 CB PHE A 287 20.905 26.441 17.866 1.00 25.23 C ANISOU 2192 CB PHE A 287 3162 2844 3580 158 535 398 C ATOM 2193 CG PHE A 287 21.147 27.807 18.437 1.00 24.24 C ANISOU 2193 CG PHE A 287 3011 2697 3500 151 530 413 C ATOM 2194 CD1 PHE A 287 22.338 28.109 19.083 1.00 28.85 C ANISOU 2194 CD1 PHE A 287 3568 3251 4144 143 530 421 C ATOM 2195 CD2 PHE A 287 20.196 28.805 18.294 1.00 21.53 C ANISOU 2195 CD2 PHE A 287 2671 2365 3142 154 526 418 C ATOM 2196 CE1 PHE A 287 22.560 29.375 19.599 1.00 33.00 C ANISOU 2196 CE1 PHE A 287 4068 3755 4716 136 526 430 C ATOM 2197 CE2 PHE A 287 20.414 30.071 18.807 1.00 22.97 C ANISOU 2197 CE2 PHE A 287 2831 2525 3372 148 524 430 C ATOM 2198 CZ PHE A 287 21.597 30.356 19.461 1.00 28.30 C ANISOU 2198 CZ PHE A 287 3478 3168 4107 138 524 434 C ATOM 2199 N MET A 288 18.754 25.143 19.763 1.00 20.67 N ANISOU 2199 N MET A 288 2615 2295 2945 118 461 330 N ATOM 2200 CA MET A 288 17.742 25.208 20.811 1.00 18.91 C ANISOU 2200 CA MET A 288 2397 2080 2710 100 427 307 C ATOM 2201 C MET A 288 17.392 23.842 21.396 1.00 21.50 C ANISOU 2201 C MET A 288 2740 2413 3018 87 412 282 C ATOM 2202 O MET A 288 16.722 23.786 22.429 1.00 25.13 O ANISOU 2202 O MET A 288 3202 2875 3472 72 385 265 O ATOM 2203 CB MET A 288 16.474 25.899 20.273 1.00 18.99 C ANISOU 2203 CB MET A 288 2418 2114 2684 106 425 305 C ATOM 2204 CG MET A 288 15.354 26.140 21.292 1.00 23.04 C ANISOU 2204 CG MET A 288 2934 2636 3185 88 393 284 C ATOM 2205 SD MET A 288 15.866 27.051 22.763 1.00 24.48 S ANISOU 2205 SD MET A 288 3093 2793 3417 73 370 285 S ATOM 2206 CE MET A 288 15.079 28.638 22.468 1.00 18.03 C ANISOU 2206 CE MET A 288 2269 1981 2599 80 371 297 C ATOM 2207 N THR A 289 17.846 22.742 20.791 1.00 20.16 N ANISOU 2207 N THR A 289 2580 2242 2838 94 430 279 N ATOM 2208 CA THR A 289 17.464 21.423 21.291 1.00 19.15 C ANISOU 2208 CA THR A 289 2466 2115 2694 83 419 255 C ATOM 2209 C THR A 289 17.986 21.178 22.709 1.00 23.63 C ANISOU 2209 C THR A 289 3023 2664 3292 70 398 254 C ATOM 2210 O THR A 289 17.226 20.798 23.608 1.00 19.99 O ANISOU 2210 O THR A 289 2569 2207 2818 57 377 237 O ATOM 2211 CB THR A 289 17.968 20.331 20.342 1.00 18.95 C ANISOU 2211 CB THR A 289 2452 2090 2659 94 445 253 C ATOM 2212 OG1 THR A 289 17.263 20.401 19.093 1.00 21.10 O ANISOU 2212 OG1 THR A 289 2737 2386 2892 106 460 246 O ATOM 2213 CG2 THR A 289 17.761 18.957 20.954 1.00 17.55 C ANISOU 2213 CG2 THR A 289 2287 1906 2477 82 438 231 C ATOM 2214 N AILE A 290 19.282 21.383 22.923 0.72 20.12 N ANISOU 2214 N AILE A 290 2559 2199 2886 76 405 273 N ATOM 2215 N BILE A 290 19.282 21.378 22.922 0.28 19.69 N ANISOU 2215 N BILE A 290 2505 2145 2832 76 405 273 N ATOM 2216 CA AILE A 290 19.919 21.066 24.202 0.72 21.61 C ANISOU 2216 CA AILE A 290 2736 2374 3103 69 386 272 C ATOM 2217 CA BILE A 290 19.913 21.062 24.202 0.28 21.64 C ANISOU 2217 CA BILE A 290 2739 2377 3106 68 386 272 C ATOM 2218 C AILE A 290 19.387 21.954 25.325 0.72 22.33 C ANISOU 2218 C AILE A 290 2817 2468 3198 57 355 265 C ATOM 2219 C BILE A 290 19.377 21.952 25.323 0.28 22.34 C ANISOU 2219 C BILE A 290 2819 2470 3200 57 355 265 C ATOM 2220 O AILE A 290 19.054 21.426 26.398 0.72 24.32 O ANISOU 2220 O AILE A 290 3074 2723 3444 49 334 253 O ATOM 2221 O BILE A 290 19.013 21.424 26.384 0.28 23.45 O ANISOU 2221 O BILE A 290 2964 2612 3332 48 334 253 O ATOM 2222 CB AILE A 290 21.451 21.157 24.099 0.72 22.19 C ANISOU 2222 CB AILE A 290 2786 2426 3218 78 399 292 C ATOM 2223 CB BILE A 290 21.445 21.140 24.094 0.28 22.19 C ANISOU 2223 CB BILE A 290 2787 2428 3218 78 399 292 C ATOM 2224 CG1AILE A 290 21.962 20.277 22.955 0.72 23.51 C ANISOU 2224 CG1AILE A 290 2964 2591 3378 92 432 299 C ATOM 2225 CG1BILE A 290 21.948 20.104 23.085 0.28 23.93 C ANISOU 2225 CG1BILE A 290 3018 2643 3431 91 430 297 C ATOM 2226 CG2AILE A 290 22.097 20.757 25.415 0.72 22.32 C ANISOU 2226 CG2AILE A 290 2789 2433 3258 74 377 290 C ATOM 2227 CG2BILE A 290 22.088 20.924 25.452 0.28 22.62 C ANISOU 2227 CG2BILE A 290 2825 2470 3298 73 375 291 C ATOM 2228 CD1AILE A 290 21.629 18.820 23.117 0.72 21.04 C ANISOU 2228 CD1AILE A 290 2671 2279 3044 89 434 284 C ATOM 2229 CD1BILE A 290 23.429 20.188 22.803 0.28 22.07 C ANISOU 2229 CD1BILE A 290 2760 2389 3235 102 448 319 C ATOM 2230 N PRO A 291 19.309 23.283 25.167 1.00 19.29 N ANISOU 2230 N PRO A 291 2419 2084 2827 57 352 272 N ATOM 2231 CA PRO A 291 18.698 24.091 26.241 1.00 21.69 C ANISOU 2231 CA PRO A 291 2716 2392 3133 46 323 261 C ATOM 2232 C PRO A 291 17.228 23.784 26.472 1.00 21.13 C ANISOU 2232 C PRO A 291 2668 2341 3020 38 311 243 C ATOM 2233 O PRO A 291 16.735 23.968 27.591 1.00 24.54 O ANISOU 2233 O PRO A 291 3099 2778 3449 28 285 230 O ATOM 2234 CB PRO A 291 18.911 25.538 25.766 1.00 24.45 C ANISOU 2234 CB PRO A 291 3049 2735 3508 50 331 274 C ATOM 2235 CG PRO A 291 19.115 25.435 24.305 1.00 23.63 C ANISOU 2235 CG PRO A 291 2951 2632 3394 64 365 291 C ATOM 2236 CD PRO A 291 19.848 24.157 24.103 1.00 22.41 C ANISOU 2236 CD PRO A 291 2803 2473 3240 69 377 292 C ATOM 2237 N ALA A 292 16.509 23.332 25.441 1.00 23.58 N ANISOU 2237 N ALA A 292 2997 2665 3298 41 327 239 N ATOM 2238 CA ALA A 292 15.109 22.961 25.615 1.00 21.60 C ANISOU 2238 CA ALA A 292 2764 2432 3009 33 316 219 C ATOM 2239 C ALA A 292 14.966 21.711 26.472 1.00 22.30 C ANISOU 2239 C ALA A 292 2864 2518 3091 24 307 207 C ATOM 2240 O ALA A 292 14.156 21.677 27.405 1.00 24.79 O ANISOU 2240 O ALA A 292 3184 2841 3395 14 288 194 O ATOM 2241 CB ALA A 292 14.449 22.742 24.256 1.00 17.15 C ANISOU 2241 CB ALA A 292 2216 1886 2415 40 336 215 C ATOM 2242 N PHE A 293 15.731 20.663 26.161 1.00 19.28 N ANISOU 2242 N PHE A 293 2485 2125 2716 29 324 211 N ATOM 2243 CA PHE A 293 15.598 19.411 26.896 1.00 23.45 C ANISOU 2243 CA PHE A 293 3024 2648 3240 23 320 202 C ATOM 2244 C PHE A 293 16.322 19.435 28.237 1.00 24.41 C ANISOU 2244 C PHE A 293 3133 2759 3384 24 302 210 C ATOM 2245 O PHE A 293 15.958 18.671 29.138 1.00 21.30 O ANISOU 2245 O PHE A 293 2748 2365 2983 19 293 204 O ATOM 2246 CB PHE A 293 16.082 18.242 26.031 1.00 24.48 C ANISOU 2246 CB PHE A 293 3164 2769 3369 30 346 201 C ATOM 2247 CG PHE A 293 15.019 17.704 25.098 1.00 22.29 C ANISOU 2247 CG PHE A 293 2905 2506 3060 26 359 181 C ATOM 2248 CD1 PHE A 293 14.698 18.372 23.933 1.00 19.90 C ANISOU 2248 CD1 PHE A 293 2603 2219 2740 32 368 179 C ATOM 2249 CD2 PHE A 293 14.328 16.543 25.406 1.00 17.40 C ANISOU 2249 CD2 PHE A 293 2300 1884 2429 16 361 163 C ATOM 2250 CE1 PHE A 293 13.715 17.886 23.088 1.00 23.50 C ANISOU 2250 CE1 PHE A 293 3073 2692 3165 30 376 157 C ATOM 2251 CE2 PHE A 293 13.354 16.052 24.565 1.00 19.93 C ANISOU 2251 CE2 PHE A 293 2633 2217 2724 11 371 140 C ATOM 2252 CZ PHE A 293 13.044 16.727 23.407 1.00 21.71 C ANISOU 2252 CZ PHE A 293 2858 2462 2929 18 376 135 C ATOM 2253 N PHE A 294 17.324 20.299 28.405 1.00 22.73 N ANISOU 2253 N PHE A 294 2898 2538 3200 30 296 223 N ATOM 2254 CA PHE A 294 17.882 20.492 29.738 1.00 23.93 C ANISOU 2254 CA PHE A 294 3035 2686 3370 30 272 226 C ATOM 2255 C PHE A 294 16.840 21.099 30.669 1.00 22.51 C ANISOU 2255 C PHE A 294 2859 2521 3174 21 247 212 C ATOM 2256 O PHE A 294 16.771 20.751 31.855 1.00 22.01 O ANISOU 2256 O PHE A 294 2796 2461 3105 21 230 209 O ATOM 2257 CB PHE A 294 19.131 21.374 29.673 1.00 25.86 C ANISOU 2257 CB PHE A 294 3252 2919 3653 37 270 238 C ATOM 2258 CG PHE A 294 19.848 21.512 30.994 1.00 25.66 C ANISOU 2258 CG PHE A 294 3209 2893 3648 40 244 237 C ATOM 2259 CD1 PHE A 294 20.291 20.391 31.678 1.00 30.00 C ANISOU 2259 CD1 PHE A 294 3761 3440 4195 47 241 242 C ATOM 2260 CD2 PHE A 294 20.089 22.761 31.542 1.00 20.76 C ANISOU 2260 CD2 PHE A 294 2566 2273 3049 37 223 232 C ATOM 2261 CE1 PHE A 294 20.953 20.509 32.895 1.00 29.26 C ANISOU 2261 CE1 PHE A 294 3651 3352 4116 53 215 241 C ATOM 2262 CE2 PHE A 294 20.753 22.886 32.757 1.00 29.46 C ANISOU 2262 CE2 PHE A 294 3649 3377 4167 41 197 226 C ATOM 2263 CZ PHE A 294 21.186 21.758 33.433 1.00 24.40 C ANISOU 2263 CZ PHE A 294 3012 2740 3519 50 192 232 C ATOM 2264 N ALA A 295 16.005 21.995 30.139 1.00 23.02 N ANISOU 2264 N ALA A 295 2926 2594 3226 16 247 206 N ATOM 2265 CA ALA A 295 14.988 22.659 30.944 1.00 21.55 C ANISOU 2265 CA ALA A 295 2742 2421 3024 8 226 193 C ATOM 2266 C ALA A 295 13.965 21.685 31.513 1.00 21.59 C ANISOU 2266 C ALA A 295 2767 2436 2999 1 222 182 C ATOM 2267 O ALA A 295 13.344 21.987 32.539 1.00 23.54 O ANISOU 2267 O ALA A 295 3016 2693 3237 -3 203 174 O ATOM 2268 CB ALA A 295 14.279 23.731 30.108 1.00 20.58 C ANISOU 2268 CB ALA A 295 2619 2305 2894 5 231 191 C ATOM 2269 N LYS A 296 13.780 20.525 30.879 1.00 18.63 N ANISOU 2269 N LYS A 296 2408 2058 2613 1 243 182 N ATOM 2270 CA LYS A 296 12.768 19.567 31.311 1.00 20.82 C ANISOU 2270 CA LYS A 296 2702 2340 2867 -7 245 171 C ATOM 2271 C LYS A 296 13.154 18.821 32.582 1.00 18.11 C ANISOU 2271 C LYS A 296 2360 1991 2528 -2 236 178 C ATOM 2272 O LYS A 296 12.318 18.089 33.123 1.00 17.75 O ANISOU 2272 O LYS A 296 2328 1949 2467 -8 239 172 O ATOM 2273 CB LYS A 296 12.476 18.577 30.181 1.00 16.65 C ANISOU 2273 CB LYS A 296 2188 1809 2329 -9 270 165 C ATOM 2274 CG LYS A 296 11.985 19.266 28.918 1.00 23.64 C ANISOU 2274 CG LYS A 296 3074 2706 3202 -10 277 158 C ATOM 2275 CD LYS A 296 11.554 18.275 27.850 1.00 22.58 C ANISOU 2275 CD LYS A 296 2953 2573 3053 -13 299 144 C ATOM 2276 CE LYS A 296 11.281 18.993 26.538 1.00 26.20 C ANISOU 2276 CE LYS A 296 3411 3047 3498 -7 306 141 C ATOM 2277 NZ LYS A 296 10.259 20.016 26.696 1.00 24.27 N ANISOU 2277 NZ LYS A 296 3163 2820 3237 -11 290 135 N ATOM 2278 N THR A 297 14.379 18.995 33.080 1.00 20.19 N ANISOU 2278 N THR A 297 2609 2249 2814 8 228 191 N ATOM 2279 CA THR A 297 14.719 18.490 34.403 1.00 24.88 C ANISOU 2279 CA THR A 297 3202 2844 3408 17 215 198 C ATOM 2280 C THR A 297 13.964 19.217 35.507 1.00 21.18 C ANISOU 2280 C THR A 297 2732 2392 2924 14 190 188 C ATOM 2281 O THR A 297 14.026 18.787 36.662 1.00 23.56 O ANISOU 2281 O THR A 297 3036 2700 3217 23 180 194 O ATOM 2282 CB THR A 297 16.220 18.613 34.667 1.00 18.49 C ANISOU 2282 CB THR A 297 2373 2027 2626 30 207 210 C ATOM 2283 OG1 THR A 297 16.593 19.994 34.671 1.00 22.14 O ANISOU 2283 OG1 THR A 297 2815 2494 3104 29 189 205 O ATOM 2284 CG2 THR A 297 17.012 17.888 33.603 1.00 20.31 C ANISOU 2284 CG2 THR A 297 2604 2241 2874 35 233 221 C ATOM 2285 N SER A 298 13.273 20.309 35.176 1.00 20.25 N ANISOU 2285 N SER A 298 2612 2283 2801 5 182 176 N ATOM 2286 CA SER A 298 12.545 21.092 36.167 1.00 19.49 C ANISOU 2286 CA SER A 298 2513 2202 2690 3 160 165 C ATOM 2287 C SER A 298 11.475 20.284 36.891 1.00 25.71 C ANISOU 2287 C SER A 298 3319 2998 3451 0 163 163 C ATOM 2288 O SER A 298 11.070 20.662 37.997 1.00 22.11 O ANISOU 2288 O SER A 298 2863 2556 2982 4 145 158 O ATOM 2289 CB SER A 298 11.905 22.308 35.493 1.00 20.53 C ANISOU 2289 CB SER A 298 2640 2338 2822 -6 156 154 C ATOM 2290 OG SER A 298 11.013 21.900 34.471 1.00 21.95 O ANISOU 2290 OG SER A 298 2834 2519 2987 -15 176 151 O ATOM 2291 N ALA A 299 11.009 19.186 36.303 1.00 21.01 N ANISOU 2291 N ALA A 299 2740 2395 2850 -6 187 165 N ATOM 2292 CA ALA A 299 9.931 18.419 36.907 1.00 20.31 C ANISOU 2292 CA ALA A 299 2666 2311 2741 -10 195 163 C ATOM 2293 C ALA A 299 10.391 17.469 38.011 1.00 22.75 C ANISOU 2293 C ALA A 299 2980 2616 3048 3 197 179 C ATOM 2294 O ALA A 299 9.534 16.881 38.683 1.00 23.17 O ANISOU 2294 O ALA A 299 3045 2673 3086 2 204 181 O ATOM 2295 CB ALA A 299 9.196 17.617 35.831 1.00 19.33 C ANISOU 2295 CB ALA A 299 2554 2178 2614 -23 220 155 C ATOM 2296 N AVAL A 300 11.699 17.313 38.221 0.38 22.05 N ANISOU 2296 N AVAL A 300 2881 2522 2975 18 192 192 N ATOM 2297 N BVAL A 300 11.697 17.299 38.223 0.62 22.06 N ANISOU 2297 N BVAL A 300 2882 2523 2976 18 192 193 N ATOM 2298 CA AVAL A 300 12.211 16.292 39.131 0.38 22.43 C ANISOU 2298 CA AVAL A 300 2934 2566 3021 34 197 212 C ATOM 2299 CA BVAL A 300 12.176 16.300 39.176 0.62 22.43 C ANISOU 2299 CA BVAL A 300 2934 2567 3021 34 196 212 C ATOM 2300 C AVAL A 300 13.047 16.895 40.258 0.38 21.38 C ANISOU 2300 C AVAL A 300 2786 2450 2886 53 168 217 C ATOM 2301 C BVAL A 300 13.028 16.915 40.285 0.62 21.37 C ANISOU 2301 C BVAL A 300 2785 2450 2885 53 167 217 C ATOM 2302 O AVAL A 300 13.080 16.356 41.371 0.38 23.20 O ANISOU 2302 O AVAL A 300 3023 2690 3104 69 164 230 O ATOM 2303 O BVAL A 300 13.058 16.398 41.408 0.62 23.23 O ANISOU 2303 O BVAL A 300 3025 2694 3106 69 163 230 O ATOM 2304 CB AVAL A 300 13.029 15.245 38.347 0.38 23.99 C ANISOU 2304 CB AVAL A 300 3134 2741 3240 38 221 224 C ATOM 2305 CB BVAL A 300 12.960 15.189 38.447 0.62 24.04 C ANISOU 2305 CB BVAL A 300 3142 2749 3245 38 221 225 C ATOM 2306 CG1AVAL A 300 13.668 14.230 39.281 0.38 23.32 C ANISOU 2306 CG1AVAL A 300 3051 2652 3156 59 227 247 C ATOM 2307 CG1BVAL A 300 14.134 15.771 37.676 0.62 23.12 C ANISOU 2307 CG1BVAL A 300 3007 2626 3150 41 215 224 C ATOM 2308 CG2AVAL A 300 12.150 14.541 37.317 0.38 23.28 C ANISOU 2308 CG2AVAL A 300 3059 2637 3151 20 249 214 C ATOM 2309 CG2BVAL A 300 13.442 14.125 39.428 0.62 23.46 C ANISOU 2309 CG2BVAL A 300 3073 2671 3170 58 229 248 C ATOM 2310 N TYR A 301 13.704 18.032 40.003 1.00 19.75 N ANISOU 2310 N TYR A 301 2561 2248 2695 52 147 206 N ATOM 2311 CA TYR A 301 14.792 18.451 40.890 1.00 23.96 C ANISOU 2311 CA TYR A 301 3076 2794 3235 70 121 209 C ATOM 2312 C TYR A 301 14.319 19.050 42.219 1.00 24.46 C ANISOU 2312 C TYR A 301 3138 2883 3274 78 94 200 C ATOM 2313 O TYR A 301 15.052 18.963 43.208 1.00 22.77 O ANISOU 2313 O TYR A 301 2914 2684 3054 99 75 205 O ATOM 2314 CB TYR A 301 15.747 19.409 40.164 1.00 22.30 C ANISOU 2314 CB TYR A 301 2842 2576 3055 65 110 200 C ATOM 2315 CG TYR A 301 15.305 20.847 40.031 1.00 21.77 C ANISOU 2315 CG TYR A 301 2765 2515 2991 52 93 179 C ATOM 2316 CD1 TYR A 301 15.339 21.718 41.120 1.00 21.10 C ANISOU 2316 CD1 TYR A 301 2667 2449 2900 59 62 164 C ATOM 2317 CD2 TYR A 301 14.904 21.349 38.810 1.00 23.47 C ANISOU 2317 CD2 TYR A 301 2982 2718 3217 36 108 174 C ATOM 2318 CE1 TYR A 301 14.941 23.032 40.997 1.00 21.11 C ANISOU 2318 CE1 TYR A 301 2659 2453 2908 48 49 144 C ATOM 2319 CE2 TYR A 301 14.511 22.663 38.671 1.00 23.67 C ANISOU 2319 CE2 TYR A 301 2997 2747 3248 27 96 157 C ATOM 2320 CZ TYR A 301 14.530 23.502 39.764 1.00 22.23 C ANISOU 2320 CZ TYR A 301 2803 2579 3062 32 67 142 C ATOM 2321 OH TYR A 301 14.134 24.814 39.619 1.00 22.38 O ANISOU 2321 OH TYR A 301 2813 2600 3092 22 57 126 O ATOM 2322 N ASN A 302 13.145 19.688 42.267 1.00 22.64 N ANISOU 2322 N ASN A 302 2915 2660 3027 65 91 184 N ATOM 2323 CA ASN A 302 12.754 20.355 43.510 1.00 21.04 C ANISOU 2323 CA ASN A 302 2710 2482 2801 75 66 173 C ATOM 2324 C ASN A 302 12.566 19.380 44.670 1.00 22.68 C ANISOU 2324 C ASN A 302 2931 2704 2981 95 69 190 C ATOM 2325 O ASN A 302 13.059 19.671 45.773 1.00 23.69 O ANISOU 2325 O ASN A 302 3050 2855 3097 116 44 188 O ATOM 2326 CB ASN A 302 11.508 21.223 43.284 1.00 20.39 C ANISOU 2326 CB ASN A 302 2634 2404 2709 57 65 154 C ATOM 2327 CG ASN A 302 11.842 22.597 42.717 1.00 23.87 C ANISOU 2327 CG ASN A 302 3056 2841 3174 47 49 135 C ATOM 2328 OD1 ASN A 302 11.335 22.994 41.662 1.00 27.09 O ANISOU 2328 OD1 ASN A 302 3465 3236 3591 30 62 130 O ATOM 2329 ND2 ASN A 302 12.703 23.330 43.418 1.00 19.02 N ANISOU 2329 ND2 ASN A 302 2421 2236 2569 57 21 123 N ATOM 2330 N PRO A 303 11.869 18.244 44.522 1.00 21.03 N ANISOU 2330 N PRO A 303 2743 2484 2763 93 100 208 N ATOM 2331 CA PRO A 303 11.799 17.296 45.646 1.00 20.70 C ANISOU 2331 CA PRO A 303 2713 2454 2698 116 106 230 C ATOM 2332 C PRO A 303 13.139 16.682 46.023 1.00 22.95 C ANISOU 2332 C PRO A 303 2989 2741 2991 140 101 249 C ATOM 2333 O PRO A 303 13.282 16.206 47.161 1.00 25.29 O ANISOU 2333 O PRO A 303 3290 3056 3264 167 96 266 O ATOM 2334 CB PRO A 303 10.812 16.227 45.154 1.00 21.41 C ANISOU 2334 CB PRO A 303 2824 2523 2788 103 145 243 C ATOM 2335 CG PRO A 303 9.981 16.930 44.147 1.00 24.14 C ANISOU 2335 CG PRO A 303 3169 2860 3142 74 148 220 C ATOM 2336 CD PRO A 303 10.945 17.848 43.445 1.00 21.11 C ANISOU 2336 CD PRO A 303 2766 2474 2780 70 128 206 C ATOM 2337 N VAL A 304 14.117 16.657 45.113 1.00 20.59 N ANISOU 2337 N VAL A 304 2677 2424 2722 135 102 249 N ATOM 2338 CA VAL A 304 15.457 16.201 45.481 1.00 22.99 C ANISOU 2338 CA VAL A 304 2968 2732 3036 159 94 265 C ATOM 2339 C VAL A 304 16.085 17.161 46.487 1.00 20.57 C ANISOU 2339 C VAL A 304 2640 2456 2718 176 52 250 C ATOM 2340 O VAL A 304 16.599 16.741 47.531 1.00 24.19 O ANISOU 2340 O VAL A 304 3095 2937 3158 206 39 264 O ATOM 2341 CB VAL A 304 16.340 16.039 44.231 1.00 25.81 C ANISOU 2341 CB VAL A 304 3314 3063 3430 148 106 267 C ATOM 2342 CG1 VAL A 304 17.721 15.529 44.622 1.00 24.14 C ANISOU 2342 CG1 VAL A 304 3087 2855 3230 174 98 284 C ATOM 2343 CG2 VAL A 304 15.688 15.092 43.239 1.00 28.51 C ANISOU 2343 CG2 VAL A 304 3675 3375 3780 132 146 276 C ATOM 2344 N ILE A 305 16.029 18.466 46.194 1.00 17.87 N ANISOU 2344 N ILE A 305 2283 2118 2387 160 30 220 N ATOM 2345 CA ILE A 305 16.514 19.476 47.135 1.00 19.39 C ANISOU 2345 CA ILE A 305 2454 2339 2572 172 -11 198 C ATOM 2346 C ILE A 305 15.791 19.343 48.465 1.00 18.21 C ANISOU 2346 C ILE A 305 2319 2221 2379 192 -21 200 C ATOM 2347 O ILE A 305 16.400 19.449 49.535 1.00 20.63 O ANISOU 2347 O ILE A 305 2614 2557 2668 219 -49 197 O ATOM 2348 CB ILE A 305 16.325 20.889 46.550 1.00 18.25 C ANISOU 2348 CB ILE A 305 2296 2188 2450 148 -25 166 C ATOM 2349 CG1 ILE A 305 17.087 21.054 45.235 1.00 17.74 C ANISOU 2349 CG1 ILE A 305 2217 2094 2429 131 -13 167 C ATOM 2350 CG2 ILE A 305 16.748 21.954 47.559 1.00 22.79 C ANISOU 2350 CG2 ILE A 305 2848 2791 3020 159 -67 138 C ATOM 2351 CD1 ILE A 305 16.963 22.444 44.652 1.00 17.60 C ANISOU 2351 CD1 ILE A 305 2184 2068 2436 110 -24 140 C ATOM 2352 N TYR A 306 14.478 19.120 48.409 1.00 18.78 N ANISOU 2352 N TYR A 306 2415 2288 2432 181 1 204 N ATOM 2353 CA TYR A 306 13.659 18.968 49.606 1.00 22.34 C ANISOU 2353 CA TYR A 306 2881 2765 2841 199 -2 209 C ATOM 2354 C TYR A 306 14.230 17.906 50.538 1.00 20.94 C ANISOU 2354 C TYR A 306 2710 2606 2642 234 1 240 C ATOM 2355 O TYR A 306 14.426 18.150 51.734 1.00 26.57 O ANISOU 2355 O TYR A 306 3418 3354 3324 262 -25 236 O ATOM 2356 CB TYR A 306 12.236 18.605 49.176 1.00 21.74 C ANISOU 2356 CB TYR A 306 2829 2673 2757 178 31 216 C ATOM 2357 CG TYR A 306 11.127 18.918 50.157 1.00 21.07 C ANISOU 2357 CG TYR A 306 2758 2612 2636 186 27 210 C ATOM 2358 CD1 TYR A 306 11.354 19.678 51.296 1.00 23.28 C ANISOU 2358 CD1 TYR A 306 3028 2927 2889 207 -7 193 C ATOM 2359 CD2 TYR A 306 9.845 18.440 49.936 1.00 23.10 C ANISOU 2359 CD2 TYR A 306 3035 2857 2885 172 58 220 C ATOM 2360 CE1 TYR A 306 10.324 19.955 52.187 1.00 22.02 C ANISOU 2360 CE1 TYR A 306 2881 2790 2695 215 -8 188 C ATOM 2361 CE2 TYR A 306 8.813 18.712 50.815 1.00 18.08 C ANISOU 2361 CE2 TYR A 306 2410 2242 2217 179 58 216 C ATOM 2362 CZ TYR A 306 9.055 19.469 51.935 1.00 22.30 C ANISOU 2362 CZ TYR A 306 2937 2811 2724 201 25 201 C ATOM 2363 OH TYR A 306 8.020 19.734 52.806 1.00 24.37 O ANISOU 2363 OH TYR A 306 3211 3095 2953 209 27 197 O ATOM 2364 N ILE A 307 14.519 16.721 49.999 1.00 20.72 N ANISOU 2364 N ILE A 307 2691 2553 2629 236 32 270 N ATOM 2365 CA ILE A 307 14.990 15.620 50.832 1.00 22.22 C ANISOU 2365 CA ILE A 307 2888 2756 2800 272 41 304 C ATOM 2366 C ILE A 307 16.353 15.943 51.436 1.00 24.96 C ANISOU 2366 C ILE A 307 3210 3130 3145 299 4 299 C ATOM 2367 O ILE A 307 16.626 15.620 52.597 1.00 26.33 O ANISOU 2367 O ILE A 307 3384 3336 3286 336 -9 314 O ATOM 2368 CB ILE A 307 15.018 14.318 50.010 1.00 24.87 C ANISOU 2368 CB ILE A 307 3238 3054 3160 265 84 335 C ATOM 2369 CG1 ILE A 307 13.591 13.879 49.676 1.00 32.98 C ANISOU 2369 CG1 ILE A 307 4288 4060 4182 244 120 340 C ATOM 2370 CG2 ILE A 307 15.752 13.214 50.753 1.00 26.85 C ANISOU 2370 CG2 ILE A 307 3490 3312 3398 304 94 373 C ATOM 2371 CD1 ILE A 307 13.521 12.838 48.577 1.00 37.48 C ANISOU 2371 CD1 ILE A 307 4869 4588 4785 226 161 356 C ATOM 2372 N MET A 308 17.226 16.590 50.662 1.00 23.27 N ANISOU 2372 N MET A 308 2971 2903 2966 283 -14 278 N ATOM 2373 CA MET A 308 18.590 16.833 51.118 1.00 19.33 C ANISOU 2373 CA MET A 308 2444 2427 2474 307 -48 272 C ATOM 2374 C MET A 308 18.666 17.953 52.151 1.00 24.13 C ANISOU 2374 C MET A 308 3035 3075 3058 319 -93 238 C ATOM 2375 O MET A 308 19.607 17.988 52.949 1.00 24.68 O ANISOU 2375 O MET A 308 3085 3175 3116 349 -123 235 O ATOM 2376 CB MET A 308 19.488 17.162 49.925 1.00 22.18 C ANISOU 2376 CB MET A 308 2783 2759 2885 284 -48 260 C ATOM 2377 CG MET A 308 19.732 15.994 48.976 1.00 30.43 C ANISOU 2377 CG MET A 308 3840 3768 3955 279 -7 292 C ATOM 2378 SD MET A 308 20.654 16.482 47.502 1.00 50.95 S ANISOU 2378 SD MET A 308 6415 6334 6610 252 -4 277 S ATOM 2379 CE MET A 308 22.129 17.189 48.233 1.00 37.57 C ANISOU 2379 CE MET A 308 4679 4669 4926 275 -52 260 C ATOM 2380 N MET A 309 17.711 18.882 52.151 1.00 20.72 N ANISOU 2380 N MET A 309 2609 2645 2618 298 -100 210 N ATOM 2381 CA MET A 309 17.883 20.120 52.900 1.00 24.06 C ANISOU 2381 CA MET A 309 3011 3099 3030 303 -143 170 C ATOM 2382 C MET A 309 16.765 20.428 53.893 1.00 24.38 C ANISOU 2382 C MET A 309 3071 3169 3025 314 -149 161 C ATOM 2383 O MET A 309 16.788 21.504 54.505 1.00 21.72 O ANISOU 2383 O MET A 309 2719 2857 2679 316 -184 123 O ATOM 2384 CB MET A 309 18.056 21.289 51.930 1.00 21.20 C ANISOU 2384 CB MET A 309 2629 2712 2715 267 -153 136 C ATOM 2385 CG MET A 309 19.239 21.134 50.973 1.00 21.30 C ANISOU 2385 CG MET A 309 2619 2698 2775 258 -149 141 C ATOM 2386 SD MET A 309 19.599 22.666 50.090 1.00 21.56 S ANISOU 2386 SD MET A 309 2622 2708 2861 223 -165 100 S ATOM 2387 CE MET A 309 20.356 23.644 51.395 1.00 19.49 C ANISOU 2387 CE MET A 309 2326 2488 2591 244 -221 58 C ATOM 2388 N ASN A 310 15.781 19.541 54.072 1.00 24.56 N ANISOU 2388 N ASN A 310 3125 3187 3021 319 -115 193 N ATOM 2389 CA ASN A 310 14.783 19.714 55.130 1.00 22.51 C ANISOU 2389 CA ASN A 310 2883 2958 2714 336 -118 190 C ATOM 2390 C ASN A 310 14.744 18.442 55.970 1.00 24.16 C ANISOU 2390 C ASN A 310 3110 3184 2884 374 -98 234 C ATOM 2391 O ASN A 310 14.239 17.407 55.521 1.00 23.60 O ANISOU 2391 O ASN A 310 3061 3086 2820 368 -55 270 O ATOM 2392 CB ASN A 310 13.396 20.053 54.577 1.00 24.78 C ANISOU 2392 CB ASN A 310 3188 3222 3005 303 -93 182 C ATOM 2393 CG ASN A 310 12.445 20.579 55.662 1.00 26.05 C ANISOU 2393 CG ASN A 310 3361 3416 3121 317 -103 168 C ATOM 2394 OD1 ASN A 310 11.711 19.814 56.288 1.00 25.05 O ANISOU 2394 OD1 ASN A 310 3258 3301 2961 336 -79 197 O ATOM 2395 ND2 ASN A 310 12.472 21.885 55.894 1.00 19.42 N ANISOU 2395 ND2 ASN A 310 2504 2591 2283 310 -138 124 N ATOM 2396 N LYS A 311 15.279 18.532 57.188 1.00 20.36 N ANISOU 2396 N LYS A 311 2620 2750 2364 414 -129 231 N ATOM 2397 CA LYS A 311 15.408 17.358 58.046 1.00 25.08 C ANISOU 2397 CA LYS A 311 3233 3370 2925 458 -112 276 C ATOM 2398 C LYS A 311 14.049 16.794 58.442 1.00 25.61 C ANISOU 2398 C LYS A 311 3334 3435 2963 462 -73 304 C ATOM 2399 O LYS A 311 13.865 15.572 58.490 1.00 24.32 O ANISOU 2399 O LYS A 311 3190 3258 2794 477 -34 351 O ATOM 2400 CB LYS A 311 16.219 17.719 59.290 1.00 23.55 C ANISOU 2400 CB LYS A 311 3021 3234 2691 502 -158 261 C ATOM 2401 CG LYS A 311 16.327 16.611 60.318 1.00 21.65 C ANISOU 2401 CG LYS A 311 2798 3026 2404 555 -144 309 C ATOM 2402 CD LYS A 311 17.309 16.993 61.415 1.00 31.17 C ANISOU 2402 CD LYS A 311 3980 4291 3573 599 -195 290 C ATOM 2403 N GLN A 312 13.090 17.667 58.750 1.00 22.64 N ANISOU 2403 N GLN A 312 2964 3071 2568 450 -82 275 N ATOM 2404 CA GLN A 312 11.770 17.199 59.159 1.00 24.40 C ANISOU 2404 CA GLN A 312 3216 3293 2764 453 -45 300 C ATOM 2405 C GLN A 312 11.092 16.411 58.043 1.00 26.19 C ANISOU 2405 C GLN A 312 3457 3465 3028 419 4 325 C ATOM 2406 O GLN A 312 10.565 15.315 58.273 1.00 25.89 O ANISOU 2406 O GLN A 312 3441 3416 2981 432 46 367 O ATOM 2407 CB GLN A 312 10.909 18.387 59.577 1.00 27.95 C ANISOU 2407 CB GLN A 312 3666 3763 3192 443 -65 260 C ATOM 2408 CG GLN A 312 9.619 18.001 60.265 1.00 29.23 C ANISOU 2408 CG GLN A 312 3855 3935 3318 455 -32 283 C ATOM 2409 CD GLN A 312 8.759 19.203 60.563 1.00 31.73 C ANISOU 2409 CD GLN A 312 4171 4268 3619 442 -50 242 C ATOM 2410 OE1 GLN A 312 8.490 20.022 59.681 1.00 35.01 O ANISOU 2410 OE1 GLN A 312 4576 4657 4070 402 -58 209 O ATOM 2411 NE2 GLN A 312 8.330 19.328 61.812 1.00 37.46 N ANISOU 2411 NE2 GLN A 312 4906 5036 4289 478 -56 244 N ATOM 2412 N PHE A 313 11.105 16.948 56.820 1.00 19.83 N ANISOU 2412 N PHE A 313 2641 2625 2268 375 2 298 N ATOM 2413 CA PHE A 313 10.483 16.241 55.706 1.00 24.52 C ANISOU 2413 CA PHE A 313 3248 3171 2898 342 45 316 C ATOM 2414 C PHE A 313 11.199 14.926 55.420 1.00 26.60 C ANISOU 2414 C PHE A 313 3516 3413 3179 356 72 356 C ATOM 2415 O PHE A 313 10.555 13.907 55.142 1.00 23.93 O ANISOU 2415 O PHE A 313 3196 3047 2851 349 116 386 O ATOM 2416 CB PHE A 313 10.469 17.119 54.455 1.00 24.53 C ANISOU 2416 CB PHE A 313 3236 3145 2940 299 34 280 C ATOM 2417 CG PHE A 313 9.942 16.416 53.242 1.00 26.53 C ANISOU 2417 CG PHE A 313 3499 3353 3228 267 74 293 C ATOM 2418 CD1 PHE A 313 8.584 16.180 53.100 1.00 27.44 C ANISOU 2418 CD1 PHE A 313 3632 3455 3341 249 104 298 C ATOM 2419 CD2 PHE A 313 10.801 15.971 52.254 1.00 22.46 C ANISOU 2419 CD2 PHE A 313 2975 2809 2749 255 81 299 C ATOM 2420 CE1 PHE A 313 8.095 15.521 51.991 1.00 25.34 C ANISOU 2420 CE1 PHE A 313 3373 3150 3107 220 138 305 C ATOM 2421 CE2 PHE A 313 10.320 15.309 51.145 1.00 24.29 C ANISOU 2421 CE2 PHE A 313 3216 3002 3012 227 116 308 C ATOM 2422 CZ PHE A 313 8.962 15.088 51.011 1.00 25.49 C ANISOU 2422 CZ PHE A 313 3384 3142 3159 209 144 309 C ATOM 2423 N ARG A 314 12.533 14.930 55.483 1.00 25.72 N ANISOU 2423 N ARG A 314 3386 3313 3074 374 46 356 N ATOM 2424 CA ARG A 314 13.293 13.716 55.211 1.00 23.74 C ANISOU 2424 CA ARG A 314 3138 3042 2841 389 70 393 C ATOM 2425 C ARG A 314 12.980 12.624 56.230 1.00 22.77 C ANISOU 2425 C ARG A 314 3035 2933 2685 429 99 440 C ATOM 2426 O ARG A 314 12.855 11.447 55.873 1.00 22.36 O ANISOU 2426 O ARG A 314 2996 2847 2651 429 142 476 O ATOM 2427 CB ARG A 314 14.789 14.037 55.190 1.00 26.27 C ANISOU 2427 CB ARG A 314 3431 3377 3172 405 33 382 C ATOM 2428 CG ARG A 314 15.689 12.837 54.955 1.00 28.47 C ANISOU 2428 CG ARG A 314 3710 3639 3470 424 54 420 C ATOM 2429 CD ARG A 314 17.156 13.242 54.834 1.00 32.63 C ANISOU 2429 CD ARG A 314 4206 4180 4012 435 16 405 C ATOM 2430 NE ARG A 314 17.682 13.866 56.045 1.00 30.79 N ANISOU 2430 NE ARG A 314 3957 4001 3740 471 -29 391 N ATOM 2431 CZ ARG A 314 18.069 15.132 56.130 1.00 32.17 C ANISOU 2431 CZ ARG A 314 4108 4198 3918 461 -75 344 C ATOM 2432 NH1 ARG A 314 17.980 15.956 55.098 1.00 26.66 N ANISOU 2432 NH1 ARG A 314 3399 3472 3260 418 -80 311 N ATOM 2433 NH2 ARG A 314 18.571 15.581 57.276 1.00 30.96 N ANISOU 2433 NH2 ARG A 314 3940 4096 3728 497 -115 330 N ATOM 2434 N ASN A 315 12.848 12.993 57.504 1.00 26.74 N ANISOU 2434 N ASN A 315 3540 3483 3138 464 78 441 N ATOM 2435 CA ASN A 315 12.506 12.001 58.520 1.00 27.69 C ANISOU 2435 CA ASN A 315 3680 3618 3222 505 107 489 C ATOM 2436 C ASN A 315 11.101 11.446 58.303 1.00 26.90 C ANISOU 2436 C ASN A 315 3605 3487 3130 483 158 508 C ATOM 2437 O ASN A 315 10.873 10.242 58.472 1.00 30.40 O ANISOU 2437 O ASN A 315 4064 3910 3577 500 204 554 O ATOM 2438 CB ASN A 315 12.649 12.610 59.914 1.00 26.99 C ANISOU 2438 CB ASN A 315 3588 3592 3074 548 71 481 C ATOM 2439 CG ASN A 315 14.091 12.891 60.278 1.00 32.21 C ANISOU 2439 CG ASN A 315 4225 4289 3726 578 25 470 C ATOM 2440 OD1 ASN A 315 15.014 12.378 59.643 1.00 29.65 O ANISOU 2440 OD1 ASN A 315 3889 3941 3435 575 28 482 O ATOM 2441 ND2 ASN A 315 14.295 13.699 61.311 1.00 33.13 N ANISOU 2441 ND2 ASN A 315 4331 4460 3796 607 -18 445 N ATOM 2442 N CYS A 316 10.149 12.305 57.927 1.00 24.91 N ANISOU 2442 N CYS A 316 3353 3229 2884 448 153 472 N ATOM 2443 CA CYS A 316 8.797 11.836 57.633 1.00 28.37 C ANISOU 2443 CA CYS A 316 3810 3635 3334 423 199 484 C ATOM 2444 C CYS A 316 8.781 10.885 56.443 1.00 25.95 C ANISOU 2444 C CYS A 316 3507 3274 3080 393 238 499 C ATOM 2445 O CYS A 316 8.051 9.888 56.448 1.00 24.81 O ANISOU 2445 O CYS A 316 3378 3101 2946 392 286 530 O ATOM 2446 CB CYS A 316 7.867 13.021 57.368 1.00 27.78 C ANISOU 2446 CB CYS A 316 3732 3566 3257 390 181 440 C ATOM 2447 SG CYS A 316 7.550 14.050 58.802 1.00 28.00 S ANISOU 2447 SG CYS A 316 3760 3655 3224 423 146 422 S ATOM 2448 N MET A 317 9.559 11.184 55.402 1.00 25.00 N ANISOU 2448 N MET A 317 3371 3135 2994 369 218 475 N ATOM 2449 CA MET A 317 9.612 10.285 54.255 1.00 29.32 C ANISOU 2449 CA MET A 317 3921 3631 3589 343 254 485 C ATOM 2450 C MET A 317 10.151 8.918 54.656 1.00 29.53 C ANISOU 2450 C MET A 317 3957 3644 3619 376 287 535 C ATOM 2451 O MET A 317 9.574 7.882 54.304 1.00 32.46 O ANISOU 2451 O MET A 317 4340 3976 4015 365 336 559 O ATOM 2452 CB MET A 317 10.466 10.888 53.142 1.00 20.02 C ANISOU 2452 CB MET A 317 2724 2440 2441 318 226 453 C ATOM 2453 CG MET A 317 10.623 9.944 51.962 1.00 31.22 C ANISOU 2453 CG MET A 317 4146 3811 3907 295 261 462 C ATOM 2454 SD MET A 317 11.850 10.492 50.773 1.00 47.78 S ANISOU 2454 SD MET A 317 6222 5897 6037 276 232 435 S ATOM 2455 CE MET A 317 13.252 10.746 51.855 1.00 40.67 C ANISOU 2455 CE MET A 317 5305 5038 5110 323 193 448 C ATOM 2456 N VAL A 318 11.252 8.897 55.411 1.00 30.80 N ANISOU 2456 N VAL A 318 4110 3837 3756 417 262 552 N ATOM 2457 CA VAL A 318 11.820 7.633 55.872 1.00 31.71 C ANISOU 2457 CA VAL A 318 4233 3943 3871 454 293 603 C ATOM 2458 C VAL A 318 10.807 6.873 56.719 1.00 34.07 C ANISOU 2458 C VAL A 318 4554 4240 4150 474 337 642 C ATOM 2459 O VAL A 318 10.645 5.655 56.578 1.00 36.10 O ANISOU 2459 O VAL A 318 4823 4460 4432 479 387 680 O ATOM 2460 CB VAL A 318 13.128 7.887 56.645 1.00 32.36 C ANISOU 2460 CB VAL A 318 4301 4070 3924 499 252 611 C ATOM 2461 CG1 VAL A 318 13.658 6.595 57.241 1.00 32.12 C ANISOU 2461 CG1 VAL A 318 4280 4036 3889 544 284 669 C ATOM 2462 CG2 VAL A 318 14.170 8.521 55.728 1.00 38.57 C ANISOU 2462 CG2 VAL A 318 5063 4851 4740 478 216 576 C ATOM 2463 N THR A 319 10.107 7.581 57.607 1.00 31.32 N ANISOU 2463 N THR A 319 4210 3930 3759 486 321 633 N ATOM 2464 CA THR A 319 9.086 6.949 58.438 1.00 33.63 C ANISOU 2464 CA THR A 319 4524 4223 4032 505 364 670 C ATOM 2465 C THR A 319 7.983 6.329 57.587 1.00 37.87 C ANISOU 2465 C THR A 319 5070 4704 4614 462 414 671 C ATOM 2466 O THR A 319 7.582 5.179 57.808 1.00 42.56 O ANISOU 2466 O THR A 319 5677 5269 5223 473 468 714 O ATOM 2467 CB THR A 319 8.503 7.975 59.410 1.00 29.95 C ANISOU 2467 CB THR A 319 4059 3808 3513 520 335 652 C ATOM 2468 OG1 THR A 319 9.472 8.282 60.419 1.00 34.04 O ANISOU 2468 OG1 THR A 319 4571 4380 3984 570 296 660 O ATOM 2469 CG2 THR A 319 7.235 7.444 60.069 1.00 39.15 C ANISOU 2469 CG2 THR A 319 5244 4966 4664 529 383 683 C ATOM 2470 N THR A 320 7.486 7.076 56.598 1.00 34.57 N ANISOU 2470 N THR A 320 4644 4271 4221 412 399 623 N ATOM 2471 CA THR A 320 6.396 6.582 55.761 1.00 33.70 C ANISOU 2471 CA THR A 320 4539 4112 4152 370 441 616 C ATOM 2472 C THR A 320 6.849 5.415 54.892 1.00 38.23 C ANISOU 2472 C THR A 320 5114 4636 4776 358 476 633 C ATOM 2473 O THR A 320 6.179 4.377 54.832 1.00 42.53 O ANISOU 2473 O THR A 320 5669 5142 5348 352 530 658 O ATOM 2474 CB THR A 320 5.848 7.715 54.896 1.00 31.29 C ANISOU 2474 CB THR A 320 4223 3808 3856 324 411 560 C ATOM 2475 OG1 THR A 320 5.020 8.565 55.694 1.00 30.38 O ANISOU 2475 OG1 THR A 320 4112 3728 3704 330 396 548 O ATOM 2476 CG2 THR A 320 5.033 7.163 53.737 1.00 35.17 C ANISOU 2476 CG2 THR A 320 4716 4250 4398 279 447 546 C ATOM 2477 N LEU A 321 7.990 5.566 54.215 1.00 39.92 N ANISOU 2477 N LEU A 321 5316 4846 5005 355 450 618 N ATOM 2478 CA LEU A 321 8.474 4.531 53.309 1.00 34.13 C ANISOU 2478 CA LEU A 321 4583 4066 4320 342 481 630 C ATOM 2479 C LEU A 321 8.930 3.274 54.042 1.00 42.62 C ANISOU 2479 C LEU A 321 5669 5128 5397 384 520 687 C ATOM 2480 O LEU A 321 8.924 2.191 53.448 1.00 41.04 O ANISOU 2480 O LEU A 321 5474 4880 5241 374 564 703 O ATOM 2481 CB LEU A 321 9.618 5.083 52.458 1.00 35.75 C ANISOU 2481 CB LEU A 321 4771 4274 4537 332 442 601 C ATOM 2482 CG LEU A 321 9.580 4.758 50.966 1.00 37.05 C ANISOU 2482 CG LEU A 321 4932 4393 4751 290 458 575 C ATOM 2483 CD1 LEU A 321 8.213 5.085 50.398 1.00 39.62 C ANISOU 2483 CD1 LEU A 321 5261 4705 5089 248 470 543 C ATOM 2484 CD2 LEU A 321 10.661 5.532 50.229 1.00 35.76 C ANISOU 2484 CD2 LEU A 321 4752 4242 4594 282 416 546 C ATOM 2485 N CYS A 322 9.329 3.391 55.305 1.00 45.43 N ANISOU 2485 N CYS A 322 6028 5527 5707 433 506 718 N ATOM 2486 CA CYS A 322 9.757 2.235 56.088 1.00 52.14 C ANISOU 2486 CA CYS A 322 6889 6370 6554 480 543 778 C ATOM 2487 C CYS A 322 8.733 1.892 57.164 1.00 50.93 C ANISOU 2487 C CYS A 322 6752 6226 6374 502 578 814 C ATOM 2488 O CYS A 322 9.072 1.791 58.344 1.00 56.57 O ANISOU 2488 O CYS A 322 7472 6978 7044 555 575 852 O ATOM 2489 CB CYS A 322 11.122 2.493 56.732 1.00 46.91 C ANISOU 2489 CB CYS A 322 6217 5752 5856 527 503 794 C ATOM 2490 SG CYS A 322 12.390 3.070 55.590 1.00 61.45 S ANISOU 2490 SG CYS A 322 8035 7589 7723 504 456 752 S TER 2491 CYS A 322 ATOM 2492 N MET B 1 -14.370 22.449 70.974 1.00 27.38 N ANISOU 2492 N MET B 1 3821 3921 2663 556 454 334 N ATOM 2493 CA MET B 1 -14.607 23.322 69.831 1.00 30.49 C ANISOU 2493 CA MET B 1 4194 4285 3106 505 425 286 C ATOM 2494 C MET B 1 -13.809 24.614 69.961 1.00 28.82 C ANISOU 2494 C MET B 1 3979 4103 2870 513 361 229 C ATOM 2495 O MET B 1 -13.664 25.170 71.049 1.00 27.60 O ANISOU 2495 O MET B 1 3835 3994 2658 555 346 214 O ATOM 2496 CB MET B 1 -16.100 23.635 69.688 1.00 28.01 C ANISOU 2496 CB MET B 1 3871 3957 2812 484 458 282 C ATOM 2497 N ASN B 2 -13.298 25.094 68.835 1.00 30.19 N ANISOU 2497 N ASN B 2 4136 4247 3088 473 326 196 N ATOM 2498 CA ASN B 2 -12.482 26.296 68.814 1.00 25.92 C ANISOU 2498 CA ASN B 2 3588 3724 2537 475 267 141 C ATOM 2499 C ASN B 2 -13.255 27.539 68.386 1.00 27.82 C ANISOU 2499 C ASN B 2 3816 3956 2800 449 253 96 C ATOM 2500 O ASN B 2 -12.715 28.646 68.472 1.00 27.97 O ANISOU 2500 O ASN B 2 3827 3989 2810 452 209 48 O ATOM 2501 CB ASN B 2 -11.272 26.072 67.899 1.00 27.30 C ANISOU 2501 CB ASN B 2 3754 3875 2746 452 236 135 C ATOM 2502 CG ASN B 2 -10.296 25.042 68.466 1.00 30.32 C ANISOU 2502 CG ASN B 2 4148 4274 3099 486 240 172 C ATOM 2503 OD1 ASN B 2 -9.544 25.340 69.396 1.00 32.14 O ANISOU 2503 OD1 ASN B 2 4385 4547 3280 526 211 160 O ATOM 2504 ND2 ASN B 2 -10.302 23.824 67.906 1.00 34.06 N ANISOU 2504 ND2 ASN B 2 4623 4714 3602 471 275 217 N ATOM 2505 N GLY B 3 -14.501 27.388 67.943 1.00 23.36 N ANISOU 2505 N GLY B 3 3245 3367 2263 425 290 110 N ATOM 2506 CA GLY B 3 -15.349 28.521 67.633 1.00 23.38 C ANISOU 2506 CA GLY B 3 3235 3364 2282 406 282 72 C ATOM 2507 C GLY B 3 -16.561 28.562 68.537 1.00 26.00 C ANISOU 2507 C GLY B 3 3576 3718 2585 429 320 85 C ATOM 2508 O GLY B 3 -16.598 27.858 69.549 1.00 30.48 O ANISOU 2508 O GLY B 3 4160 4312 3110 466 346 118 O ATOM 2509 N THR B 4 -17.563 29.369 68.195 1.00 23.30 N ANISOU 2509 N THR B 4 3222 3366 2264 410 324 61 N ATOM 2510 CA THR B 4 -18.745 29.543 69.032 1.00 24.19 C ANISOU 2510 CA THR B 4 3341 3500 2352 431 359 68 C ATOM 2511 C THR B 4 -19.989 29.252 68.208 1.00 24.24 C ANISOU 2511 C THR B 4 3331 3473 2407 395 395 84 C ATOM 2512 O THR B 4 -20.231 29.914 67.195 1.00 23.31 O ANISOU 2512 O THR B 4 3196 3330 2331 360 377 57 O ATOM 2513 CB THR B 4 -18.811 30.959 69.606 1.00 21.67 C ANISOU 2513 CB THR B 4 3021 3208 2005 449 328 18 C ATOM 2514 OG1 THR B 4 -17.597 31.245 70.310 1.00 27.02 O ANISOU 2514 OG1 THR B 4 3710 3916 2640 480 289 -3 O ATOM 2515 CG2 THR B 4 -19.992 31.095 70.552 1.00 23.81 C ANISOU 2515 CG2 THR B 4 3299 3503 2244 476 365 27 C ATOM 2516 N GLU B 5 -20.783 28.283 68.650 1.00 24.26 N ANISOU 2516 N GLU B 5 3338 3475 2404 404 447 128 N ATOM 2517 CA GLU B 5 -22.028 27.942 67.979 1.00 26.36 C ANISOU 2517 CA GLU B 5 3588 3713 2717 372 485 142 C ATOM 2518 C GLU B 5 -23.194 28.609 68.691 1.00 23.44 C ANISOU 2518 C GLU B 5 3216 3364 2327 389 507 134 C ATOM 2519 O GLU B 5 -23.286 28.566 69.922 1.00 24.28 O ANISOU 2519 O GLU B 5 3339 3503 2382 432 525 147 O ATOM 2520 CB GLU B 5 -22.254 26.430 67.930 1.00 28.01 C ANISOU 2520 CB GLU B 5 3797 3900 2943 366 534 195 C ATOM 2521 CG GLU B 5 -23.588 26.070 67.266 1.00 31.47 C ANISOU 2521 CG GLU B 5 4214 4310 3432 332 573 206 C ATOM 2522 CD GLU B 5 -23.752 24.586 67.000 1.00 36.56 C ANISOU 2522 CD GLU B 5 4856 4925 4110 317 618 251 C ATOM 2523 OE1 GLU B 5 -22.841 23.809 67.359 1.00 36.83 O ANISOU 2523 OE1 GLU B 5 4907 4960 4125 336 622 279 O ATOM 2524 OE2 GLU B 5 -24.795 24.201 66.420 1.00 33.57 O ANISOU 2524 OE2 GLU B 5 4457 4521 3777 287 650 258 O ATOM 2525 N GLY B 6 -24.071 29.235 67.911 1.00 26.35 N ANISOU 2525 N GLY B 6 3563 3713 2735 359 506 111 N ATOM 2526 CA GLY B 6 -25.318 29.755 68.415 1.00 23.41 C ANISOU 2526 CA GLY B 6 3184 3354 2355 369 533 106 C ATOM 2527 C GLY B 6 -26.483 29.116 67.692 1.00 22.57 C ANISOU 2527 C GLY B 6 3055 3218 2300 336 573 128 C ATOM 2528 O GLY B 6 -26.317 28.159 66.929 1.00 22.71 O ANISOU 2528 O GLY B 6 3065 3208 2355 308 584 149 O ATOM 2529 N PRO B 7 -27.692 29.633 67.925 1.00 22.43 N ANISOU 2529 N PRO B 7 3027 3209 2288 338 596 120 N ATOM 2530 CA PRO B 7 -28.884 29.002 67.330 1.00 23.76 C ANISOU 2530 CA PRO B 7 3170 3352 2505 308 636 140 C ATOM 2531 C PRO B 7 -28.879 28.996 65.814 1.00 25.01 C ANISOU 2531 C PRO B 7 3304 3478 2720 261 613 122 C ATOM 2532 O PRO B 7 -29.350 28.030 65.200 1.00 23.58 O ANISOU 2532 O PRO B 7 3106 3271 2581 233 641 143 O ATOM 2533 CB PRO B 7 -30.040 29.847 67.888 1.00 29.73 C ANISOU 2533 CB PRO B 7 3918 4127 3251 324 654 127 C ATOM 2534 CG PRO B 7 -29.481 30.498 69.116 1.00 22.25 C ANISOU 2534 CG PRO B 7 2998 3218 2239 371 640 116 C ATOM 2535 CD PRO B 7 -28.041 30.760 68.805 1.00 26.21 C ANISOU 2535 CD PRO B 7 3513 3719 2727 370 588 95 C ATOM 2536 N ASN B 8 -28.355 30.053 65.190 1.00 24.32 N ANISOU 2536 N ASN B 8 3214 3391 2636 252 563 84 N ATOM 2537 CA ASN B 8 -28.370 30.162 63.738 1.00 25.30 C ANISOU 2537 CA ASN B 8 3316 3488 2809 212 540 67 C ATOM 2538 C ASN B 8 -27.055 30.721 63.193 1.00 24.71 C ANISOU 2538 C ASN B 8 3250 3409 2729 208 488 43 C ATOM 2539 O ASN B 8 -27.035 31.324 62.113 1.00 19.95 O ANISOU 2539 O ASN B 8 2632 2793 2156 184 460 19 O ATOM 2540 CB ASN B 8 -29.546 31.025 63.274 1.00 26.36 C ANISOU 2540 CB ASN B 8 3425 3623 2968 200 541 45 C ATOM 2541 CG ASN B 8 -29.668 32.317 64.059 1.00 26.55 C ANISOU 2541 CG ASN B 8 3458 3671 2957 230 526 20 C ATOM 2542 OD1 ASN B 8 -28.830 32.626 64.906 1.00 24.14 O ANISOU 2542 OD1 ASN B 8 3178 3385 2610 259 511 14 O ATOM 2543 ND2 ASN B 8 -30.721 33.078 63.783 1.00 26.54 N ANISOU 2543 ND2 ASN B 8 3437 3672 2975 224 531 4 N ATOM 2544 N PHE B 9 -25.950 30.523 63.911 1.00 23.70 N ANISOU 2544 N PHE B 9 3147 3294 2565 232 475 49 N ATOM 2545 CA PHE B 9 -24.658 31.021 63.455 1.00 23.04 C ANISOU 2545 CA PHE B 9 3070 3206 2478 229 428 27 C ATOM 2546 C PHE B 9 -23.546 30.142 64.008 1.00 22.11 C ANISOU 2546 C PHE B 9 2974 3093 2333 246 427 50 C ATOM 2547 O PHE B 9 -23.751 29.366 64.945 1.00 20.62 O ANISOU 2547 O PHE B 9 2798 2918 2118 268 461 80 O ATOM 2548 CB PHE B 9 -24.443 32.490 63.862 1.00 20.10 C ANISOU 2548 CB PHE B 9 2703 2852 2084 248 395 -12 C ATOM 2549 CG PHE B 9 -24.494 32.738 65.350 1.00 26.00 C ANISOU 2549 CG PHE B 9 3469 3633 2778 290 405 -13 C ATOM 2550 CD1 PHE B 9 -23.337 32.686 66.117 1.00 28.17 C ANISOU 2550 CD1 PHE B 9 3764 3927 3012 317 384 -16 C ATOM 2551 CD2 PHE B 9 -25.690 33.060 65.976 1.00 23.65 C ANISOU 2551 CD2 PHE B 9 3168 3350 2469 304 435 -12 C ATOM 2552 CE1 PHE B 9 -23.377 32.930 67.478 1.00 24.69 C ANISOU 2552 CE1 PHE B 9 3340 3522 2518 358 392 -19 C ATOM 2553 CE2 PHE B 9 -25.736 33.304 67.345 1.00 27.85 C ANISOU 2553 CE2 PHE B 9 3718 3916 2949 346 445 -13 C ATOM 2554 CZ PHE B 9 -24.581 33.242 68.094 1.00 25.59 C ANISOU 2554 CZ PHE B 9 3452 3650 2619 373 423 -18 C ATOM 2555 N TYR B 10 -22.364 30.259 63.399 1.00 19.94 N ANISOU 2555 N TYR B 10 2702 2808 2067 236 390 36 N ATOM 2556 CA TYR B 10 -21.138 29.658 63.928 1.00 20.54 C ANISOU 2556 CA TYR B 10 2797 2893 2115 255 379 51 C ATOM 2557 C TYR B 10 -20.008 30.658 63.734 1.00 19.87 C ANISOU 2557 C TYR B 10 2714 2812 2023 258 327 15 C ATOM 2558 O TYR B 10 -19.579 30.899 62.602 1.00 19.52 O ANISOU 2558 O TYR B 10 2658 2745 2015 230 304 1 O ATOM 2559 CB TYR B 10 -20.797 28.329 63.245 1.00 21.70 C ANISOU 2559 CB TYR B 10 2942 3013 2290 234 396 83 C ATOM 2560 CG TYR B 10 -19.600 27.644 63.874 1.00 24.57 C ANISOU 2560 CG TYR B 10 3325 3388 2624 258 390 103 C ATOM 2561 CD1 TYR B 10 -19.758 26.792 64.957 1.00 23.94 C ANISOU 2561 CD1 TYR B 10 3261 3325 2512 288 426 139 C ATOM 2562 CD2 TYR B 10 -18.309 27.871 63.404 1.00 26.00 C ANISOU 2562 CD2 TYR B 10 3508 3563 2808 253 349 87 C ATOM 2563 CE1 TYR B 10 -18.669 26.177 65.551 1.00 26.85 C ANISOU 2563 CE1 TYR B 10 3647 3705 2850 314 420 160 C ATOM 2564 CE2 TYR B 10 -17.214 27.260 63.995 1.00 21.77 C ANISOU 2564 CE2 TYR B 10 2988 3039 2245 277 342 105 C ATOM 2565 CZ TYR B 10 -17.401 26.413 65.065 1.00 26.14 C ANISOU 2565 CZ TYR B 10 3558 3611 2765 308 377 141 C ATOM 2566 OH TYR B 10 -16.320 25.798 65.656 1.00 25.87 O ANISOU 2566 OH TYR B 10 3538 3591 2700 336 370 161 O ATOM 2567 N VAL B 11 -19.522 31.237 64.828 1.00 20.14 N ANISOU 2567 N VAL B 11 2762 2877 2012 293 310 -2 N ATOM 2568 CA VAL B 11 -18.454 32.229 64.740 1.00 20.03 C ANISOU 2568 CA VAL B 11 2748 2868 1995 297 261 -41 C ATOM 2569 C VAL B 11 -17.107 31.526 64.875 1.00 21.64 C ANISOU 2569 C VAL B 11 2962 3076 2185 307 244 -28 C ATOM 2570 O VAL B 11 -16.901 30.761 65.829 1.00 22.19 O ANISOU 2570 O VAL B 11 3047 3167 2215 336 260 -2 O ATOM 2571 CB VAL B 11 -18.624 33.331 65.797 1.00 20.33 C ANISOU 2571 CB VAL B 11 2792 2937 1995 328 247 -74 C ATOM 2572 CG1 VAL B 11 -17.482 34.335 65.708 1.00 21.83 C ANISOU 2572 CG1 VAL B 11 2979 3129 2188 331 198 -117 C ATOM 2573 CG2 VAL B 11 -19.971 34.028 65.631 1.00 20.31 C ANISOU 2573 CG2 VAL B 11 2778 2929 2009 319 266 -86 C ATOM 2574 N PRO B 12 -16.174 31.731 63.946 1.00 21.19 N ANISOU 2574 N PRO B 12 2896 2996 2158 285 213 -42 N ATOM 2575 CA PRO B 12 -14.840 31.112 64.061 1.00 20.01 C ANISOU 2575 CA PRO B 12 2754 2850 1998 294 194 -32 C ATOM 2576 C PRO B 12 -13.930 31.855 65.038 1.00 24.06 C ANISOU 2576 C PRO B 12 3274 3396 2473 327 158 -63 C ATOM 2577 O PRO B 12 -12.839 32.315 64.693 1.00 28.53 O ANISOU 2577 O PRO B 12 3832 3955 3051 321 121 -88 O ATOM 2578 CB PRO B 12 -14.330 31.164 62.615 1.00 19.98 C ANISOU 2578 CB PRO B 12 2736 2810 2046 256 177 -38 C ATOM 2579 CG PRO B 12 -15.017 32.350 62.017 1.00 20.88 C ANISOU 2579 CG PRO B 12 2836 2912 2187 238 168 -69 C ATOM 2580 CD PRO B 12 -16.373 32.407 62.648 1.00 19.44 C ANISOU 2580 CD PRO B 12 2656 2744 1986 249 199 -62 C ATOM 2581 N PHE B 13 -14.382 31.960 66.288 1.00 20.45 N ANISOU 2581 N PHE B 13 2829 2974 1966 362 169 -64 N ATOM 2582 CA PHE B 13 -13.677 32.717 67.317 1.00 27.23 C ANISOU 2582 CA PHE B 13 3693 3869 2783 396 135 -99 C ATOM 2583 C PHE B 13 -14.110 32.175 68.671 1.00 22.57 C ANISOU 2583 C PHE B 13 3123 3320 2133 440 161 -76 C ATOM 2584 O PHE B 13 -15.308 32.004 68.912 1.00 25.32 O ANISOU 2584 O PHE B 13 3476 3670 2476 442 199 -58 O ATOM 2585 CB PHE B 13 -13.989 34.219 67.205 1.00 25.79 C ANISOU 2585 CB PHE B 13 3499 3683 2617 388 112 -152 C ATOM 2586 CG PHE B 13 -12.997 35.114 67.910 1.00 25.49 C ANISOU 2586 CG PHE B 13 3459 3670 2555 411 67 -200 C ATOM 2587 CD1 PHE B 13 -11.854 35.553 67.257 1.00 31.36 C ANISOU 2587 CD1 PHE B 13 4189 4395 3331 393 29 -226 C ATOM 2588 CD2 PHE B 13 -13.218 35.534 69.212 1.00 28.50 C ANISOU 2588 CD2 PHE B 13 3852 4095 2883 450 64 -222 C ATOM 2589 CE1 PHE B 13 -10.943 36.386 67.897 1.00 29.48 C ANISOU 2589 CE1 PHE B 13 3945 4179 3076 412 -12 -274 C ATOM 2590 CE2 PHE B 13 -12.311 36.364 69.856 1.00 27.90 C ANISOU 2590 CE2 PHE B 13 3772 4044 2786 471 20 -272 C ATOM 2591 CZ PHE B 13 -11.175 36.791 69.195 1.00 27.16 C ANISOU 2591 CZ PHE B 13 3662 3929 2730 450 -18 -299 C ATOM 2592 N SER B 14 -13.144 31.902 69.543 1.00 28.28 N ANISOU 2592 N SER B 14 3856 4077 2811 475 141 -77 N ATOM 2593 CA SER B 14 -13.448 31.331 70.850 1.00 26.01 C ANISOU 2593 CA SER B 14 3589 3834 2461 522 166 -50 C ATOM 2594 C SER B 14 -14.087 32.361 71.775 1.00 27.12 C ANISOU 2594 C SER B 14 3733 4007 2564 549 161 -88 C ATOM 2595 O SER B 14 -13.634 33.506 71.866 1.00 29.59 O ANISOU 2595 O SER B 14 4037 4328 2878 549 119 -144 O ATOM 2596 CB SER B 14 -12.174 30.780 71.489 1.00 26.60 C ANISOU 2596 CB SER B 14 3672 3939 2497 556 142 -42 C ATOM 2597 OG SER B 14 -12.413 30.323 72.807 1.00 28.81 O ANISOU 2597 OG SER B 14 3971 4266 2709 608 163 -18 O ATOM 2598 N ASN B 15 -15.148 31.945 72.480 1.00 23.90 N ANISOU 2598 N ASN B 15 3338 3617 2125 571 205 -57 N ATOM 2599 CA ASN B 15 -15.774 32.781 73.499 1.00 26.06 C ANISOU 2599 CA ASN B 15 3619 3928 2355 603 206 -87 C ATOM 2600 C ASN B 15 -15.208 32.528 74.894 1.00 28.45 C ANISOU 2600 C ASN B 15 3940 4290 2580 662 198 -84 C ATOM 2601 O ASN B 15 -15.906 32.751 75.893 1.00 24.05 O ANISOU 2601 O ASN B 15 3396 3768 1975 698 218 -86 O ATOM 2602 CB ASN B 15 -17.296 32.590 73.502 1.00 27.69 C ANISOU 2602 CB ASN B 15 3827 4122 2571 596 260 -59 C ATOM 2603 CG ASN B 15 -18.025 33.776 74.117 1.00 26.87 C ANISOU 2603 CG ASN B 15 3723 4040 2446 612 255 -102 C ATOM 2604 OD1 ASN B 15 -17.485 34.877 74.148 1.00 23.28 O ANISOU 2604 OD1 ASN B 15 3262 3593 1992 612 211 -159 O ATOM 2605 ND2 ASN B 15 -19.249 33.560 74.610 1.00 33.13 N ANISOU 2605 ND2 ASN B 15 4523 4842 3222 626 303 -77 N ATOM 2606 N LYS B 16 -13.958 32.070 74.998 1.00 23.72 N ANISOU 2606 N LYS B 16 3343 3704 1965 676 169 -80 N ATOM 2607 CA LYS B 16 -13.387 31.854 76.322 1.00 27.77 C ANISOU 2607 CA LYS B 16 3872 4278 2400 736 157 -79 C ATOM 2608 C LYS B 16 -13.196 33.160 77.085 1.00 30.16 C ANISOU 2608 C LYS B 16 4172 4620 2667 760 116 -149 C ATOM 2609 O LYS B 16 -13.051 33.131 78.313 1.00 26.86 O ANISOU 2609 O LYS B 16 3769 4259 2177 814 112 -154 O ATOM 2610 CB LYS B 16 -12.055 31.104 76.213 1.00 29.84 C ANISOU 2610 CB LYS B 16 4134 4546 2657 744 132 -61 C ATOM 2611 CG LYS B 16 -10.985 31.828 75.420 1.00 30.81 C ANISOU 2611 CG LYS B 16 4236 4647 2824 712 76 -111 C ATOM 2612 CD LYS B 16 -9.748 30.964 75.246 1.00 32.97 C ANISOU 2612 CD LYS B 16 4508 4923 3097 719 58 -86 C ATOM 2613 CE LYS B 16 -8.871 31.505 74.130 1.00 33.58 C ANISOU 2613 CE LYS B 16 4562 4961 3236 674 17 -123 C ATOM 2614 NZ LYS B 16 -7.638 30.693 73.935 1.00 31.81 N ANISOU 2614 NZ LYS B 16 4334 4738 3013 680 -1 -100 N ATOM 2615 N THR B 17 -13.200 34.299 76.392 1.00 24.32 N ANISOU 2615 N THR B 17 3414 3850 1976 723 86 -204 N ATOM 2616 CA THR B 17 -13.078 35.600 77.033 1.00 26.85 C ANISOU 2616 CA THR B 17 3729 4199 2272 740 49 -276 C ATOM 2617 C THR B 17 -14.389 36.371 77.082 1.00 27.79 C ANISOU 2617 C THR B 17 3849 4308 2402 732 75 -293 C ATOM 2618 O THR B 17 -14.410 37.494 77.599 1.00 28.39 O ANISOU 2618 O THR B 17 3921 4404 2463 746 49 -353 O ATOM 2619 CB THR B 17 -12.016 36.447 76.323 1.00 25.78 C ANISOU 2619 CB THR B 17 3571 4039 2186 709 -6 -332 C ATOM 2620 OG1 THR B 17 -12.385 36.625 74.949 1.00 31.32 O ANISOU 2620 OG1 THR B 17 4257 4677 2965 652 5 -323 O ATOM 2621 CG2 THR B 17 -10.657 35.764 76.399 1.00 35.45 C ANISOU 2621 CG2 THR B 17 4793 5281 3394 722 -37 -321 C ATOM 2622 N GLY B 18 -15.477 35.813 76.549 1.00 25.68 N ANISOU 2622 N GLY B 18 3585 4010 2164 710 126 -244 N ATOM 2623 CA GLY B 18 -16.793 36.402 76.698 1.00 25.58 C ANISOU 2623 CA GLY B 18 3572 3991 2155 708 157 -252 C ATOM 2624 C GLY B 18 -17.172 37.481 75.705 1.00 27.95 C ANISOU 2624 C GLY B 18 3853 4246 2523 662 143 -292 C ATOM 2625 O GLY B 18 -18.219 38.115 75.885 1.00 27.17 O ANISOU 2625 O GLY B 18 3752 4145 2425 664 164 -306 O ATOM 2626 N VAL B 19 -16.376 37.706 74.653 1.00 23.52 N ANISOU 2626 N VAL B 19 3274 3647 2017 623 111 -308 N ATOM 2627 CA VAL B 19 -16.619 38.855 73.782 1.00 23.20 C ANISOU 2627 CA VAL B 19 3214 3565 2035 586 95 -349 C ATOM 2628 C VAL B 19 -17.480 38.533 72.568 1.00 29.13 C ANISOU 2628 C VAL B 19 3955 4268 2846 542 128 -312 C ATOM 2629 O VAL B 19 -17.930 39.465 71.882 1.00 26.72 O ANISOU 2629 O VAL B 19 3635 3932 2587 516 123 -339 O ATOM 2630 CB VAL B 19 -15.294 39.475 73.292 1.00 26.12 C ANISOU 2630 CB VAL B 19 3568 3919 2437 568 42 -393 C ATOM 2631 CG1 VAL B 19 -14.390 39.802 74.471 1.00 31.09 C ANISOU 2631 CG1 VAL B 19 4204 4599 3010 610 5 -436 C ATOM 2632 CG2 VAL B 19 -14.599 38.543 72.312 1.00 27.15 C ANISOU 2632 CG2 VAL B 19 3693 4020 2602 539 40 -353 C ATOM 2633 N VAL B 20 -17.732 37.255 72.278 1.00 22.55 N ANISOU 2633 N VAL B 20 3128 3426 2013 536 161 -252 N ATOM 2634 CA VAL B 20 -18.437 36.894 71.053 1.00 25.98 C ANISOU 2634 CA VAL B 20 3550 3815 2506 492 187 -220 C ATOM 2635 C VAL B 20 -19.883 37.363 71.133 1.00 30.10 C ANISOU 2635 C VAL B 20 4068 4334 3035 491 220 -221 C ATOM 2636 O VAL B 20 -20.580 37.126 72.130 1.00 29.55 O ANISOU 2636 O VAL B 20 4012 4296 2920 523 250 -207 O ATOM 2637 CB VAL B 20 -18.354 35.381 70.807 1.00 27.73 C ANISOU 2637 CB VAL B 20 3778 4030 2727 487 216 -160 C ATOM 2638 CG1 VAL B 20 -19.157 35.002 69.567 1.00 24.77 C ANISOU 2638 CG1 VAL B 20 3389 3611 2410 443 243 -132 C ATOM 2639 CG2 VAL B 20 -16.904 34.951 70.654 1.00 25.16 C ANISOU 2639 CG2 VAL B 20 3455 3706 2399 488 182 -159 C ATOM 2640 N ARG B 21 -20.340 38.039 70.082 1.00 30.51 N ANISOU 2640 N ARG B 21 4101 4348 3142 455 216 -236 N ATOM 2641 CA ARG B 21 -21.713 38.503 69.985 1.00 28.55 C ANISOU 2641 CA ARG B 21 3846 4093 2909 450 246 -236 C ATOM 2642 C ARG B 21 -22.296 38.055 68.654 1.00 24.77 C ANISOU 2642 C ARG B 21 3350 3575 2487 408 265 -206 C ATOM 2643 O ARG B 21 -21.577 37.913 67.660 1.00 27.28 O ANISOU 2643 O ARG B 21 3659 3866 2841 380 243 -204 O ATOM 2644 CB ARG B 21 -21.804 40.032 70.138 1.00 28.63 C ANISOU 2644 CB ARG B 21 3848 4102 2927 455 222 -292 C ATOM 2645 CG ARG B 21 -21.230 40.532 71.466 1.00 38.01 C ANISOU 2645 CG ARG B 21 5052 5332 4060 497 201 -330 C ATOM 2646 CD ARG B 21 -22.047 41.673 72.063 1.00 43.09 C ANISOU 2646 CD ARG B 21 5694 5987 4693 516 207 -369 C ATOM 2647 NE ARG B 21 -21.851 42.933 71.354 1.00 44.95 N ANISOU 2647 NE ARG B 21 5912 6190 4978 493 179 -414 N ATOM 2648 CZ ARG B 21 -22.471 44.067 71.658 1.00 47.14 C ANISOU 2648 CZ ARG B 21 6183 6466 5260 503 180 -453 C ATOM 2649 NH1 ARG B 21 -23.343 44.133 72.652 1.00 50.43 N ANISOU 2649 NH1 ARG B 21 6611 6915 5634 535 207 -454 N ATOM 2650 NH2 ARG B 21 -22.212 45.160 70.946 1.00 45.21 N ANISOU 2650 NH2 ARG B 21 5924 6189 5067 482 156 -490 N ATOM 2651 N SER B 22 -23.605 37.825 68.653 1.00 25.22 N ANISOU 2651 N SER B 22 3402 3631 2551 405 305 -183 N ATOM 2652 CA SER B 22 -24.271 37.285 67.476 1.00 25.02 C ANISOU 2652 CA SER B 22 3359 3573 2575 368 325 -154 C ATOM 2653 C SER B 22 -24.079 38.213 66.279 1.00 23.04 C ANISOU 2653 C SER B 22 3090 3291 2374 338 295 -182 C ATOM 2654 O SER B 22 -24.204 39.438 66.413 1.00 20.88 O ANISOU 2654 O SER B 22 2811 3018 2104 346 279 -220 O ATOM 2655 CB SER B 22 -25.763 37.091 67.750 1.00 27.11 C ANISOU 2655 CB SER B 22 3617 3844 2840 372 370 -134 C ATOM 2656 OG SER B 22 -26.473 36.854 66.546 1.00 26.28 O ANISOU 2656 OG SER B 22 3489 3708 2786 335 383 -119 O ATOM 2657 N PRO B 23 -23.789 37.668 65.093 1.00 23.98 N ANISOU 2657 N PRO B 23 3197 3382 2531 305 290 -164 N ATOM 2658 CA PRO B 23 -23.657 38.512 63.897 1.00 20.79 C ANISOU 2658 CA PRO B 23 2776 2950 2174 279 266 -185 C ATOM 2659 C PRO B 23 -24.970 39.092 63.407 1.00 24.93 C ANISOU 2659 C PRO B 23 3282 3465 2725 269 284 -188 C ATOM 2660 O PRO B 23 -24.967 39.843 62.422 1.00 21.29 O ANISOU 2660 O PRO B 23 2805 2982 2301 251 267 -203 O ATOM 2661 CB PRO B 23 -23.066 37.550 62.860 1.00 19.66 C ANISOU 2661 CB PRO B 23 2628 2785 2057 250 261 -160 C ATOM 2662 CG PRO B 23 -23.571 36.214 63.273 1.00 22.36 C ANISOU 2662 CG PRO B 23 2976 3136 2382 253 297 -121 C ATOM 2663 CD PRO B 23 -23.600 36.239 64.784 1.00 20.21 C ANISOU 2663 CD PRO B 23 2723 2897 2058 292 308 -123 C ATOM 2664 N PHE B 24 -26.089 38.739 64.031 1.00 21.28 N ANISOU 2664 N PHE B 24 2819 3019 2247 281 320 -172 N ATOM 2665 CA PHE B 24 -27.374 39.368 63.764 1.00 22.43 C ANISOU 2665 CA PHE B 24 2948 3162 2414 277 338 -177 C ATOM 2666 C PHE B 24 -27.731 40.434 64.791 1.00 26.85 C ANISOU 2666 C PHE B 24 3514 3740 2947 308 339 -207 C ATOM 2667 O PHE B 24 -28.824 41.005 64.716 1.00 25.02 O ANISOU 2667 O PHE B 24 3268 3508 2729 310 356 -212 O ATOM 2668 CB PHE B 24 -28.483 38.310 63.718 1.00 21.55 C ANISOU 2668 CB PHE B 24 2826 3053 2308 268 380 -141 C ATOM 2669 CG PHE B 24 -28.234 37.220 62.720 1.00 23.24 C ANISOU 2669 CG PHE B 24 3032 3249 2550 237 382 -115 C ATOM 2670 CD1 PHE B 24 -28.128 37.515 61.371 1.00 20.28 C ANISOU 2670 CD1 PHE B 24 2640 2852 2215 210 361 -122 C ATOM 2671 CD2 PHE B 24 -28.094 35.905 63.127 1.00 22.29 C ANISOU 2671 CD2 PHE B 24 2921 3132 2415 238 406 -83 C ATOM 2672 CE1 PHE B 24 -27.895 36.519 60.444 1.00 21.35 C ANISOU 2672 CE1 PHE B 24 2767 2971 2374 183 362 -102 C ATOM 2673 CE2 PHE B 24 -27.857 34.902 62.205 1.00 22.87 C ANISOU 2673 CE2 PHE B 24 2987 3186 2516 209 408 -62 C ATOM 2674 CZ PHE B 24 -27.761 35.209 60.861 1.00 21.36 C ANISOU 2674 CZ PHE B 24 2778 2975 2364 181 385 -73 C ATOM 2675 N GLU B 25 -26.849 40.715 65.748 1.00 23.70 N ANISOU 2675 N GLU B 25 3135 3359 2511 333 321 -228 N ATOM 2676 CA GLU B 25 -27.185 41.633 66.826 1.00 23.25 C ANISOU 2676 CA GLU B 25 3086 3324 2424 365 323 -258 C ATOM 2677 C GLU B 25 -26.226 42.801 66.991 1.00 28.18 C ANISOU 2677 C GLU B 25 3714 3943 3048 374 283 -306 C ATOM 2678 O GLU B 25 -26.659 43.861 67.448 1.00 26.25 O ANISOU 2678 O GLU B 25 3469 3704 2802 390 283 -339 O ATOM 2679 CB GLU B 25 -27.274 40.873 68.157 1.00 29.46 C ANISOU 2679 CB GLU B 25 3894 4146 3155 397 347 -242 C ATOM 2680 CG GLU B 25 -28.420 39.875 68.199 1.00 30.87 C ANISOU 2680 CG GLU B 25 4067 4329 3334 393 394 -197 C ATOM 2681 CD GLU B 25 -28.426 39.029 69.457 1.00 38.49 C ANISOU 2681 CD GLU B 25 5053 5327 4245 425 422 -174 C ATOM 2682 OE1 GLU B 25 -27.468 39.127 70.257 1.00 34.36 O ANISOU 2682 OE1 GLU B 25 4550 4826 3680 451 400 -190 O ATOM 2683 OE2 GLU B 25 -29.395 38.263 69.640 1.00 39.50 O ANISOU 2683 OE2 GLU B 25 5176 5458 4372 425 465 -138 O ATOM 2684 N ALA B 26 -24.952 42.653 66.639 1.00 25.51 N ANISOU 2684 N ALA B 26 3381 3595 2717 363 251 -314 N ATOM 2685 CA ALA B 26 -23.966 43.668 66.985 1.00 26.52 C ANISOU 2685 CA ALA B 26 3512 3722 2842 374 215 -361 C ATOM 2686 C ALA B 26 -22.812 43.601 65.999 1.00 26.97 C ANISOU 2686 C ALA B 26 3562 3751 2933 348 184 -362 C ATOM 2687 O ALA B 26 -22.561 42.548 65.401 1.00 29.42 O ANISOU 2687 O ALA B 26 3873 4056 3251 330 189 -326 O ATOM 2688 CB ALA B 26 -23.452 43.475 68.417 1.00 30.66 C ANISOU 2688 CB ALA B 26 4057 4286 3306 410 208 -378 C ATOM 2689 N PRO B 27 -22.075 44.703 65.823 1.00 25.97 N ANISOU 2689 N PRO B 27 3429 3608 2831 346 153 -404 N ATOM 2690 CA PRO B 27 -20.879 44.666 64.976 1.00 25.84 C ANISOU 2690 CA PRO B 27 3406 3567 2846 323 124 -406 C ATOM 2691 C PRO B 27 -19.858 43.662 65.491 1.00 25.57 C ANISOU 2691 C PRO B 27 3385 3554 2776 331 111 -395 C ATOM 2692 O PRO B 27 -19.740 43.416 66.695 1.00 28.58 O ANISOU 2692 O PRO B 27 3781 3970 3107 361 111 -404 O ATOM 2693 CB PRO B 27 -20.338 46.100 65.059 1.00 26.17 C ANISOU 2693 CB PRO B 27 3439 3592 2913 327 98 -459 C ATOM 2694 CG PRO B 27 -21.509 46.931 65.432 1.00 25.83 C ANISOU 2694 CG PRO B 27 3392 3551 2870 341 118 -475 C ATOM 2695 CD PRO B 27 -22.362 46.064 66.311 1.00 28.55 C ANISOU 2695 CD PRO B 27 3752 3933 3164 361 147 -450 C ATOM 2696 N GLN B 28 -19.104 43.090 64.555 1.00 26.09 N ANISOU 2696 N GLN B 28 3446 3599 2868 307 100 -373 N ATOM 2697 CA GLN B 28 -18.166 42.005 64.834 1.00 22.72 C ANISOU 2697 CA GLN B 28 3030 3187 2414 312 90 -354 C ATOM 2698 C GLN B 28 -16.748 42.522 65.025 1.00 23.19 C ANISOU 2698 C GLN B 28 3087 3244 2478 315 50 -391 C ATOM 2699 O GLN B 28 -15.781 41.891 64.588 1.00 20.69 O ANISOU 2699 O GLN B 28 2770 2921 2171 304 36 -376 O ATOM 2700 CB GLN B 28 -18.214 40.969 63.713 1.00 23.18 C ANISOU 2700 CB GLN B 28 3085 3226 2499 284 104 -308 C ATOM 2701 CG GLN B 28 -19.598 40.380 63.471 1.00 19.77 C ANISOU 2701 CG GLN B 28 2652 2795 2067 277 144 -274 C ATOM 2702 CD GLN B 28 -20.049 39.483 64.606 1.00 23.44 C ANISOU 2702 CD GLN B 28 3132 3292 2480 302 169 -252 C ATOM 2703 OE1 GLN B 28 -19.529 38.382 64.786 1.00 23.38 O ANISOU 2703 OE1 GLN B 28 3135 3293 2454 305 173 -225 O ATOM 2704 NE2 GLN B 28 -21.015 39.955 65.385 1.00 20.33 N ANISOU 2704 NE2 GLN B 28 2742 2918 2066 322 187 -263 N ATOM 2705 N TYR B 29 -16.608 43.688 65.663 1.00 23.63 N ANISOU 2705 N TYR B 29 3140 3307 2533 331 32 -441 N ATOM 2706 CA TYR B 29 -15.307 44.322 65.840 1.00 23.83 C ANISOU 2706 CA TYR B 29 3157 3326 2569 332 -7 -483 C ATOM 2707 C TYR B 29 -14.383 43.552 66.774 1.00 30.12 C ANISOU 2707 C TYR B 29 3967 4161 3318 356 -26 -485 C ATOM 2708 O TYR B 29 -13.184 43.849 66.809 1.00 23.60 O ANISOU 2708 O TYR B 29 3132 3332 2503 354 -60 -514 O ATOM 2709 CB TYR B 29 -15.488 45.746 66.368 1.00 24.23 C ANISOU 2709 CB TYR B 29 3201 3375 2631 344 -19 -540 C ATOM 2710 CG TYR B 29 -16.224 46.674 65.426 1.00 24.81 C ANISOU 2710 CG TYR B 29 3260 3409 2759 323 -5 -542 C ATOM 2711 CD1 TYR B 29 -16.022 46.610 64.052 1.00 25.88 C ANISOU 2711 CD1 TYR B 29 3382 3505 2945 292 -2 -516 C ATOM 2712 CD2 TYR B 29 -17.123 47.610 65.912 1.00 25.31 C ANISOU 2712 CD2 TYR B 29 3322 3474 2821 338 7 -570 C ATOM 2713 CE1 TYR B 29 -16.694 47.459 63.193 1.00 23.99 C ANISOU 2713 CE1 TYR B 29 3131 3233 2753 278 11 -516 C ATOM 2714 CE2 TYR B 29 -17.798 48.460 65.061 1.00 25.57 C ANISOU 2714 CE2 TYR B 29 3342 3471 2904 322 21 -570 C ATOM 2715 CZ TYR B 29 -17.583 48.379 63.706 1.00 20.60 C ANISOU 2715 CZ TYR B 29 2699 2805 2322 292 23 -542 C ATOM 2716 OH TYR B 29 -18.260 49.226 62.861 1.00 25.22 O ANISOU 2716 OH TYR B 29 3272 3358 2954 280 37 -539 O ATOM 2717 N TYR B 30 -14.901 42.585 67.535 1.00 24.05 N ANISOU 2717 N TYR B 30 3215 3427 2494 378 -4 -454 N ATOM 2718 CA TYR B 30 -14.036 41.797 68.403 1.00 22.16 C ANISOU 2718 CA TYR B 30 2988 3225 2206 404 -19 -449 C ATOM 2719 C TYR B 30 -13.137 40.833 67.632 1.00 23.01 C ANISOU 2719 C TYR B 30 3094 3317 2333 385 -26 -414 C ATOM 2720 O TYR B 30 -12.130 40.381 68.184 1.00 27.37 O ANISOU 2720 O TYR B 30 3650 3893 2856 403 -49 -419 O ATOM 2721 CB TYR B 30 -14.878 41.028 69.422 1.00 26.16 C ANISOU 2721 CB TYR B 30 3515 3772 2651 436 11 -421 C ATOM 2722 CG TYR B 30 -15.838 40.036 68.810 1.00 21.41 C ANISOU 2722 CG TYR B 30 2919 3155 2060 420 55 -361 C ATOM 2723 CD1 TYR B 30 -17.126 40.417 68.448 1.00 21.29 C ANISOU 2723 CD1 TYR B 30 2899 3124 2065 408 84 -354 C ATOM 2724 CD2 TYR B 30 -15.462 38.717 68.611 1.00 21.28 C ANISOU 2724 CD2 TYR B 30 2911 3142 2034 417 67 -313 C ATOM 2725 CE1 TYR B 30 -18.012 39.506 67.889 1.00 25.85 C ANISOU 2725 CE1 TYR B 30 3478 3689 2656 392 122 -303 C ATOM 2726 CE2 TYR B 30 -16.336 37.799 68.053 1.00 24.25 C ANISOU 2726 CE2 TYR B 30 3288 3501 2423 400 106 -263 C ATOM 2727 CZ TYR B 30 -17.607 38.196 67.696 1.00 26.01 C ANISOU 2727 CZ TYR B 30 3505 3710 2667 387 133 -259 C ATOM 2728 OH TYR B 30 -18.469 37.273 67.145 1.00 27.95 O ANISOU 2728 OH TYR B 30 3750 3940 2929 370 171 -213 O ATOM 2729 N LEU B 31 -13.461 40.511 66.376 1.00 22.29 N ANISOU 2729 N LEU B 31 2995 3187 2287 351 -9 -382 N ATOM 2730 CA LEU B 31 -12.664 39.565 65.600 1.00 27.45 C ANISOU 2730 CA LEU B 31 3646 3825 2959 332 -12 -348 C ATOM 2731 C LEU B 31 -11.924 40.191 64.424 1.00 22.04 C ANISOU 2731 C LEU B 31 2941 3098 2333 301 -34 -364 C ATOM 2732 O LEU B 31 -11.243 39.467 63.691 1.00 19.85 O ANISOU 2732 O LEU B 31 2662 2806 2076 284 -36 -338 O ATOM 2733 CB LEU B 31 -13.539 38.406 65.093 1.00 23.38 C ANISOU 2733 CB LEU B 31 3139 3302 2443 320 28 -292 C ATOM 2734 CG LEU B 31 -14.825 38.632 64.289 1.00 20.25 C ANISOU 2734 CG LEU B 31 2735 2880 2078 298 57 -277 C ATOM 2735 CD1 LEU B 31 -14.552 39.056 62.845 1.00 19.55 C ANISOU 2735 CD1 LEU B 31 2629 2750 2049 262 47 -279 C ATOM 2736 CD2 LEU B 31 -15.666 37.364 64.314 1.00 21.06 C ANISOU 2736 CD2 LEU B 31 2848 2990 2164 297 96 -228 C ATOM 2737 N ALA B 32 -12.040 41.499 64.216 1.00 25.13 N ANISOU 2737 N ALA B 32 3320 3471 2757 293 -46 -404 N ATOM 2738 CA ALA B 32 -11.336 42.175 63.132 1.00 24.57 C ANISOU 2738 CA ALA B 32 3230 3360 2745 265 -63 -419 C ATOM 2739 C ALA B 32 -11.459 43.675 63.341 1.00 22.63 C ANISOU 2739 C ALA B 32 2972 3102 2524 268 -76 -470 C ATOM 2740 O ALA B 32 -12.398 44.151 63.984 1.00 25.97 O ANISOU 2740 O ALA B 32 3401 3540 2927 283 -64 -485 O ATOM 2741 CB ALA B 32 -11.886 41.779 61.754 1.00 24.07 C ANISOU 2741 CB ALA B 32 3163 3265 2719 236 -39 -378 C ATOM 2742 N AGLU B 33 -10.501 44.408 62.794 0.62 25.36 N ANISOU 2742 N AGLU B 33 3300 3419 2916 252 -100 -496 N ATOM 2743 N BGLU B 33 -10.497 44.410 62.787 0.38 25.39 N ANISOU 2743 N BGLU B 33 3303 3422 2920 252 -100 -496 N ATOM 2744 CA AGLU B 33 -10.498 45.854 62.943 0.62 25.49 C ANISOU 2744 CA AGLU B 33 3303 3418 2966 252 -112 -547 C ATOM 2745 CA BGLU B 33 -10.450 45.859 62.880 0.38 25.52 C ANISOU 2745 CA BGLU B 33 3305 3419 2972 251 -112 -546 C ATOM 2746 C AGLU B 33 -11.447 46.512 61.943 0.62 25.05 C ANISOU 2746 C AGLU B 33 3240 3326 2953 234 -87 -532 C ATOM 2747 C BGLU B 33 -11.479 46.497 61.945 0.38 25.03 C ANISOU 2747 C BGLU B 33 3237 3323 2949 234 -86 -531 C ATOM 2748 O AGLU B 33 -11.708 45.965 60.866 0.62 24.48 O ANISOU 2748 O AGLU B 33 3167 3236 2900 215 -69 -489 O ATOM 2749 O BGLU B 33 -11.837 45.915 60.916 0.38 24.43 O ANISOU 2749 O BGLU B 33 3162 3232 2889 216 -67 -487 O ATOM 2750 CB AGLU B 33 -9.091 46.404 62.756 0.62 27.22 C ANISOU 2750 CB AGLU B 33 3503 3618 3223 243 -144 -581 C ATOM 2751 CB BGLU B 33 -9.059 46.363 62.522 0.38 27.22 C ANISOU 2751 CB BGLU B 33 3501 3610 3230 238 -142 -575 C ATOM 2752 CG AGLU B 33 -8.143 46.050 63.878 0.62 27.40 C ANISOU 2752 CG AGLU B 33 3528 3678 3204 265 -175 -610 C ATOM 2753 CG BGLU B 33 -7.921 45.688 63.268 0.38 28.88 C ANISOU 2753 CG BGLU B 33 3714 3852 3408 252 -170 -586 C ATOM 2754 CD AGLU B 33 -6.803 46.731 63.730 0.62 29.61 C ANISOU 2754 CD AGLU B 33 3784 3937 3529 255 -207 -651 C ATOM 2755 CD BGLU B 33 -7.494 46.458 64.499 0.38 28.45 C ANISOU 2755 CD BGLU B 33 3653 3822 3334 276 -199 -649 C ATOM 2756 OE1AGLU B 33 -6.761 47.978 63.793 0.62 31.63 O ANISOU 2756 OE1AGLU B 33 4024 4170 3823 250 -216 -698 O ATOM 2757 OE1BGLU B 33 -8.372 46.830 65.305 0.38 28.77 O ANISOU 2757 OE1BGLU B 33 3705 3885 3343 295 -191 -668 O ATOM 2758 OE2AGLU B 33 -5.797 46.019 63.537 0.62 34.23 O ANISOU 2758 OE2AGLU B 33 4366 4527 4113 251 -223 -637 O ATOM 2759 OE2BGLU B 33 -6.280 46.703 64.654 0.38 32.82 O ANISOU 2759 OE2BGLU B 33 4190 4374 3905 274 -231 -682 O ATOM 2760 N PRO B 34 -11.969 47.695 62.282 1.00 21.51 N ANISOU 2760 N PRO B 34 2784 2868 2520 241 -85 -570 N ATOM 2761 CA PRO B 34 -12.930 48.360 61.389 1.00 27.03 C ANISOU 2761 CA PRO B 34 3476 3536 3258 228 -60 -555 C ATOM 2762 C PRO B 34 -12.382 48.651 60.000 1.00 20.23 C ANISOU 2762 C PRO B 34 2599 2631 2457 202 -60 -537 C ATOM 2763 O PRO B 34 -13.155 48.647 59.037 1.00 24.24 O ANISOU 2763 O PRO B 34 3105 3121 2985 191 -37 -503 O ATOM 2764 CB PRO B 34 -13.270 49.654 62.144 1.00 21.11 C ANISOU 2764 CB PRO B 34 2721 2782 2517 243 -64 -607 C ATOM 2765 CG PRO B 34 -12.924 49.381 63.562 1.00 25.97 C ANISOU 2765 CG PRO B 34 3348 3441 3079 269 -84 -640 C ATOM 2766 CD PRO B 34 -11.750 48.459 63.525 1.00 30.56 C ANISOU 2766 CD PRO B 34 3930 4034 3647 264 -105 -628 C ATOM 2767 N TRP B 35 -11.079 48.909 59.863 1.00 22.40 N ANISOU 2767 N TRP B 35 2862 2888 2760 194 -84 -558 N ATOM 2768 CA TRP B 35 -10.524 49.133 58.533 1.00 24.20 C ANISOU 2768 CA TRP B 35 3075 3075 3044 170 -80 -537 C ATOM 2769 C TRP B 35 -10.604 47.874 57.677 1.00 22.86 C ANISOU 2769 C TRP B 35 2915 2912 2859 158 -68 -482 C ATOM 2770 O TRP B 35 -10.692 47.968 56.448 1.00 25.07 O ANISOU 2770 O TRP B 35 3186 3163 3174 142 -54 -452 O ATOM 2771 CB TRP B 35 -9.079 49.631 58.630 1.00 25.17 C ANISOU 2771 CB TRP B 35 3182 3180 3203 164 -107 -573 C ATOM 2772 CG TRP B 35 -8.093 48.624 59.160 1.00 27.62 C ANISOU 2772 CG TRP B 35 3498 3519 3479 168 -131 -573 C ATOM 2773 CD1 TRP B 35 -7.645 48.520 60.444 1.00 27.41 C ANISOU 2773 CD1 TRP B 35 3475 3527 3414 187 -155 -612 C ATOM 2774 CD2 TRP B 35 -7.415 47.600 58.416 1.00 26.10 C ANISOU 2774 CD2 TRP B 35 3307 3325 3287 155 -131 -534 C ATOM 2775 NE1 TRP B 35 -6.742 47.488 60.551 1.00 26.82 N ANISOU 2775 NE1 TRP B 35 3403 3471 3315 188 -171 -596 N ATOM 2776 CE2 TRP B 35 -6.583 46.908 59.321 1.00 30.19 C ANISOU 2776 CE2 TRP B 35 3829 3875 3768 168 -156 -548 C ATOM 2777 CE3 TRP B 35 -7.434 47.197 57.075 1.00 32.17 C ANISOU 2777 CE3 TRP B 35 4073 4068 4081 136 -113 -488 C ATOM 2778 CZ2 TRP B 35 -5.782 45.840 58.931 1.00 33.45 C ANISOU 2778 CZ2 TRP B 35 4244 4294 4172 161 -162 -518 C ATOM 2779 CZ3 TRP B 35 -6.640 46.136 56.691 1.00 36.31 C ANISOU 2779 CZ3 TRP B 35 4601 4599 4597 128 -119 -460 C ATOM 2780 CH2 TRP B 35 -5.824 45.467 57.617 1.00 32.40 C ANISOU 2780 CH2 TRP B 35 4110 4133 4068 140 -143 -474 C ATOM 2781 N GLN B 36 -10.571 46.693 58.305 1.00 24.98 N ANISOU 2781 N GLN B 36 3198 3216 3075 167 -71 -466 N ATOM 2782 CA GLN B 36 -10.742 45.450 57.559 1.00 22.08 C ANISOU 2782 CA GLN B 36 2840 2855 2694 156 -57 -416 C ATOM 2783 C GLN B 36 -12.149 45.330 56.986 1.00 19.27 C ANISOU 2783 C GLN B 36 2488 2498 2335 152 -28 -386 C ATOM 2784 O GLN B 36 -12.319 44.904 55.838 1.00 19.29 O ANISOU 2784 O GLN B 36 2488 2486 2356 136 -15 -352 O ATOM 2785 CB GLN B 36 -10.422 44.252 58.451 1.00 26.47 C ANISOU 2785 CB GLN B 36 3412 3449 3198 169 -64 -406 C ATOM 2786 CG GLN B 36 -9.043 44.313 59.083 1.00 27.38 C ANISOU 2786 CG GLN B 36 3522 3570 3310 176 -96 -437 C ATOM 2787 CD GLN B 36 -8.756 43.126 59.968 1.00 26.92 C ANISOU 2787 CD GLN B 36 3479 3551 3198 194 -101 -423 C ATOM 2788 OE1 GLN B 36 -8.955 43.180 61.179 1.00 27.07 O ANISOU 2788 OE1 GLN B 36 3507 3603 3175 218 -109 -446 O ATOM 2789 NE2 GLN B 36 -8.284 42.042 59.368 1.00 29.54 N ANISOU 2789 NE2 GLN B 36 3815 3880 3528 183 -97 -386 N ATOM 2790 N PHE B 37 -13.170 45.680 57.773 1.00 18.84 N ANISOU 2790 N PHE B 37 2440 2462 2257 168 -17 -400 N ATOM 2791 CA PHE B 37 -14.537 45.682 57.260 1.00 18.70 C ANISOU 2791 CA PHE B 37 2423 2444 2240 165 10 -375 C ATOM 2792 C PHE B 37 -14.707 46.707 56.144 1.00 20.45 C ANISOU 2792 C PHE B 37 2627 2629 2513 153 16 -374 C ATOM 2793 O PHE B 37 -15.414 46.454 55.164 1.00 20.42 O ANISOU 2793 O PHE B 37 2620 2619 2520 144 33 -342 O ATOM 2794 CB PHE B 37 -15.535 45.964 58.384 1.00 24.25 C ANISOU 2794 CB PHE B 37 3133 3171 2909 186 20 -393 C ATOM 2795 CG PHE B 37 -15.694 44.835 59.367 1.00 24.39 C ANISOU 2795 CG PHE B 37 3168 3227 2872 199 24 -382 C ATOM 2796 CD1 PHE B 37 -16.547 43.777 59.097 1.00 20.05 C ANISOU 2796 CD1 PHE B 37 2625 2690 2304 194 49 -342 C ATOM 2797 CD2 PHE B 37 -15.003 44.845 60.570 1.00 26.70 C ANISOU 2797 CD2 PHE B 37 3469 3542 3133 219 6 -411 C ATOM 2798 CE1 PHE B 37 -16.698 42.742 59.997 1.00 19.44 C ANISOU 2798 CE1 PHE B 37 2562 2643 2179 208 58 -327 C ATOM 2799 CE2 PHE B 37 -15.158 43.815 61.482 1.00 22.91 C ANISOU 2799 CE2 PHE B 37 3006 3098 2601 235 12 -396 C ATOM 2800 CZ PHE B 37 -16.006 42.761 61.190 1.00 22.75 C ANISOU 2800 CZ PHE B 37 2992 3086 2565 230 40 -352 C ATOM 2801 N ASER B 38 -14.074 47.877 56.277 0.83 22.68 N ANISOU 2801 N ASER B 38 2899 2888 2829 156 2 -409 N ATOM 2802 N BSER B 38 -14.069 47.874 56.286 0.17 22.00 N ANISOU 2802 N BSER B 38 2813 2802 2743 156 2 -409 N ATOM 2803 CA ASER B 38 -14.206 48.913 55.259 0.83 19.99 C ANISOU 2803 CA ASER B 38 2543 2510 2541 148 11 -406 C ATOM 2804 CA BSER B 38 -14.174 48.919 55.274 0.17 19.88 C ANISOU 2804 CA BSER B 38 2530 2497 2528 148 10 -406 C ATOM 2805 C ASER B 38 -13.565 48.513 53.937 0.83 20.04 C ANISOU 2805 C ASER B 38 2542 2496 2574 130 12 -372 C ATOM 2806 C BSER B 38 -13.607 48.466 53.937 0.17 19.92 C ANISOU 2806 C BSER B 38 2528 2482 2558 130 13 -371 C ATOM 2807 O ASER B 38 -13.948 49.048 52.894 0.83 19.27 O ANISOU 2807 O ASER B 38 2435 2376 2509 125 26 -353 O ATOM 2808 O BSER B 38 -14.076 48.908 52.883 0.17 19.56 O ANISOU 2808 O BSER B 38 2474 2418 2541 125 28 -349 O ATOM 2809 CB ASER B 38 -13.600 50.228 55.752 0.83 21.34 C ANISOU 2809 CB ASER B 38 2703 2657 2747 154 -2 -452 C ATOM 2810 CB BSER B 38 -13.454 50.182 55.751 0.17 21.52 C ANISOU 2810 CB BSER B 38 2726 2680 2771 153 -4 -453 C ATOM 2811 OG ASER B 38 -13.996 51.303 54.914 0.83 21.60 O ANISOU 2811 OG ASER B 38 2722 2656 2828 152 14 -447 O ATOM 2812 OG BSER B 38 -13.962 50.622 56.999 0.17 21.91 O ANISOU 2812 OG BSER B 38 2781 2748 2795 171 -7 -490 O ATOM 2813 N MET B 39 -12.593 47.598 53.958 1.00 23.74 N ANISOU 2813 N MET B 39 3016 2972 3030 122 -2 -365 N ATOM 2814 CA MET B 39 -12.068 47.048 52.711 1.00 21.19 C ANISOU 2814 CA MET B 39 2690 2636 2726 106 2 -331 C ATOM 2815 C MET B 39 -13.090 46.149 52.028 1.00 19.05 C ANISOU 2815 C MET B 39 2425 2380 2432 101 21 -292 C ATOM 2816 O MET B 39 -13.201 46.156 50.800 1.00 18.58 O ANISOU 2816 O MET B 39 2358 2306 2394 92 31 -266 O ATOM 2817 CB MET B 39 -10.774 46.280 52.971 1.00 25.73 C ANISOU 2817 CB MET B 39 3269 3216 3293 100 -17 -334 C ATOM 2818 CG MET B 39 -9.570 47.162 53.217 1.00 27.32 C ANISOU 2818 CG MET B 39 3457 3393 3532 99 -36 -368 C ATOM 2819 SD MET B 39 -8.115 46.167 53.581 1.00 41.40 S ANISOU 2819 SD MET B 39 5242 5188 5300 95 -60 -370 S ATOM 2820 CE MET B 39 -8.197 44.968 52.250 1.00 47.43 C ANISOU 2820 CE MET B 39 6012 5950 6059 80 -43 -315 C ATOM 2821 N LEU B 40 -13.833 45.354 52.804 1.00 21.38 N ANISOU 2821 N LEU B 40 2733 2707 2684 108 26 -288 N ATOM 2822 CA LEU B 40 -14.909 44.551 52.226 1.00 24.13 C ANISOU 2822 CA LEU B 40 3083 3070 3014 102 45 -256 C ATOM 2823 C LEU B 40 -15.959 45.436 51.565 1.00 19.46 C ANISOU 2823 C LEU B 40 2480 2468 2444 106 60 -251 C ATOM 2824 O LEU B 40 -16.372 45.189 50.425 1.00 20.13 O ANISOU 2824 O LEU B 40 2558 2550 2539 98 70 -225 O ATOM 2825 CB LEU B 40 -15.560 43.679 53.303 1.00 18.56 C ANISOU 2825 CB LEU B 40 2391 2396 2264 111 52 -256 C ATOM 2826 CG LEU B 40 -14.702 42.647 54.041 1.00 21.09 C ANISOU 2826 CG LEU B 40 2725 2733 2556 112 42 -255 C ATOM 2827 CD1 LEU B 40 -15.564 41.837 54.996 1.00 17.87 C ANISOU 2827 CD1 LEU B 40 2329 2354 2105 123 57 -247 C ATOM 2828 CD2 LEU B 40 -13.979 41.728 53.054 1.00 19.99 C ANISOU 2828 CD2 LEU B 40 2585 2583 2427 95 40 -228 C ATOM 2829 N ALA B 41 -16.397 46.484 52.268 1.00 18.05 N ANISOU 2829 N ALA B 41 2299 2287 2272 120 61 -277 N ATOM 2830 CA ALA B 41 -17.436 47.361 51.735 1.00 20.46 C ANISOU 2830 CA ALA B 41 2593 2584 2597 126 76 -272 C ATOM 2831 C ALA B 41 -16.964 48.095 50.483 1.00 17.87 C ANISOU 2831 C ALA B 41 2253 2225 2313 121 77 -259 C ATOM 2832 O ALA B 41 -17.732 48.266 49.530 1.00 21.39 O ANISOU 2832 O ALA B 41 2689 2670 2768 122 91 -236 O ATOM 2833 CB ALA B 41 -17.879 48.356 52.807 1.00 20.22 C ANISOU 2833 CB ALA B 41 2563 2554 2566 143 78 -306 C ATOM 2834 N ALA B 42 -15.711 48.555 50.476 1.00 19.31 N ANISOU 2834 N ALA B 42 2432 2383 2522 117 64 -274 N ATOM 2835 CA ALA B 42 -15.176 49.239 49.306 1.00 19.45 C ANISOU 2835 CA ALA B 42 2438 2369 2583 113 68 -259 C ATOM 2836 C ALA B 42 -15.103 48.298 48.111 1.00 21.17 C ANISOU 2836 C ALA B 42 2656 2594 2793 102 73 -221 C ATOM 2837 O ALA B 42 -15.452 48.678 46.987 1.00 22.23 O ANISOU 2837 O ALA B 42 2781 2718 2946 105 85 -197 O ATOM 2838 CB ALA B 42 -13.794 49.817 49.620 1.00 19.55 C ANISOU 2838 CB ALA B 42 2446 2353 2628 109 54 -284 C ATOM 2839 N TYR B 43 -14.657 47.063 48.345 1.00 17.46 N ANISOU 2839 N TYR B 43 2197 2143 2295 92 64 -216 N ATOM 2840 CA TYR B 43 -14.606 46.053 47.294 1.00 20.07 C ANISOU 2840 CA TYR B 43 2529 2482 2615 81 68 -185 C ATOM 2841 C TYR B 43 -15.998 45.742 46.759 1.00 20.12 C ANISOU 2841 C TYR B 43 2531 2509 2603 84 82 -166 C ATOM 2842 O TYR B 43 -16.179 45.561 45.549 1.00 22.82 O ANISOU 2842 O TYR B 43 2867 2852 2952 81 88 -141 O ATOM 2843 CB TYR B 43 -13.928 44.801 47.852 1.00 22.55 C ANISOU 2843 CB TYR B 43 2855 2811 2902 71 57 -186 C ATOM 2844 CG TYR B 43 -13.909 43.571 46.981 1.00 26.02 C ANISOU 2844 CG TYR B 43 3298 3261 3326 59 61 -159 C ATOM 2845 CD1 TYR B 43 -13.048 43.472 45.896 1.00 29.64 C ANISOU 2845 CD1 TYR B 43 3752 3704 3806 52 60 -142 C ATOM 2846 CD2 TYR B 43 -14.707 42.476 47.286 1.00 26.37 C ANISOU 2846 CD2 TYR B 43 3349 3331 3337 55 68 -151 C ATOM 2847 CE1 TYR B 43 -13.008 42.325 45.117 1.00 27.40 C ANISOU 2847 CE1 TYR B 43 3472 3430 3507 41 64 -121 C ATOM 2848 CE2 TYR B 43 -14.678 41.331 46.515 1.00 24.89 C ANISOU 2848 CE2 TYR B 43 3165 3153 3141 43 73 -130 C ATOM 2849 CZ TYR B 43 -13.825 41.259 45.435 1.00 27.60 C ANISOU 2849 CZ TYR B 43 3504 3480 3502 36 70 -116 C ATOM 2850 OH TYR B 43 -13.794 40.115 44.673 1.00 29.10 O ANISOU 2850 OH TYR B 43 3696 3678 3681 25 74 -99 O ATOM 2851 N MET B 44 -16.998 45.683 47.644 1.00 17.25 N ANISOU 2851 N MET B 44 2171 2165 2217 90 87 -177 N ATOM 2852 CA MET B 44 -18.362 45.418 47.194 1.00 17.22 C ANISOU 2852 CA MET B 44 2160 2182 2200 93 100 -162 C ATOM 2853 C MET B 44 -18.915 46.582 46.384 1.00 17.31 C ANISOU 2853 C MET B 44 2158 2182 2238 105 109 -154 C ATOM 2854 O MET B 44 -19.607 46.371 45.380 1.00 21.35 O ANISOU 2854 O MET B 44 2660 2705 2746 106 116 -133 O ATOM 2855 CB MET B 44 -19.273 45.113 48.385 1.00 17.81 C ANISOU 2855 CB MET B 44 2241 2280 2247 98 106 -176 C ATOM 2856 CG MET B 44 -19.026 43.752 49.034 1.00 17.25 C ANISOU 2856 CG MET B 44 2183 2226 2146 88 104 -174 C ATOM 2857 SD MET B 44 -18.766 42.408 47.847 1.00 27.37 S ANISOU 2857 SD MET B 44 3463 3512 3423 68 105 -147 S ATOM 2858 CE MET B 44 -20.295 42.445 46.894 1.00 19.41 C ANISOU 2858 CE MET B 44 2438 2521 2417 69 119 -133 C ATOM 2859 N PHE B 45 -18.615 47.819 46.795 1.00 18.48 N ANISOU 2859 N PHE B 45 2303 2307 2412 116 108 -171 N ATOM 2860 CA PHE B 45 -19.089 48.979 46.044 1.00 20.15 C ANISOU 2860 CA PHE B 45 2502 2503 2653 130 120 -160 C ATOM 2861 C PHE B 45 -18.513 48.991 44.634 1.00 21.05 C ANISOU 2861 C PHE B 45 2609 2604 2784 128 121 -132 C ATOM 2862 O PHE B 45 -19.191 49.396 43.680 1.00 22.02 O ANISOU 2862 O PHE B 45 2721 2732 2915 140 132 -110 O ATOM 2863 CB PHE B 45 -18.732 50.273 46.777 1.00 23.73 C ANISOU 2863 CB PHE B 45 2952 2927 3136 140 120 -186 C ATOM 2864 CG PHE B 45 -19.325 51.503 46.149 1.00 27.74 C ANISOU 2864 CG PHE B 45 3447 3417 3676 158 136 -176 C ATOM 2865 CD1 PHE B 45 -20.695 51.614 45.984 1.00 23.92 C ANISOU 2865 CD1 PHE B 45 2956 2954 3178 170 147 -165 C ATOM 2866 CD2 PHE B 45 -18.519 52.549 45.733 1.00 25.33 C ANISOU 2866 CD2 PHE B 45 3135 3073 3415 163 140 -175 C ATOM 2867 CE1 PHE B 45 -21.250 52.739 45.408 1.00 27.86 C ANISOU 2867 CE1 PHE B 45 3442 3438 3705 189 162 -152 C ATOM 2868 CE2 PHE B 45 -19.071 53.679 45.166 1.00 19.96 C ANISOU 2868 CE2 PHE B 45 2443 2374 2766 181 158 -162 C ATOM 2869 CZ PHE B 45 -20.438 53.774 45.003 1.00 18.41 C ANISOU 2869 CZ PHE B 45 2240 2202 2553 195 168 -150 C ATOM 2870 N ALEU B 46 -17.257 48.572 44.481 0.75 22.32 N ANISOU 2870 N ALEU B 46 2776 2751 2952 116 112 -132 N ATOM 2871 N BLEU B 46 -17.263 48.550 44.483 0.25 22.27 N ANISOU 2871 N BLEU B 46 2769 2745 2945 116 112 -132 N ATOM 2872 CA ALEU B 46 -16.672 48.483 43.149 0.75 22.41 C ANISOU 2872 CA ALEU B 46 2783 2754 2978 114 115 -104 C ATOM 2873 CA BLEU B 46 -16.646 48.471 43.162 0.25 22.38 C ANISOU 2873 CA BLEU B 46 2780 2750 2975 114 115 -105 C ATOM 2874 C ALEU B 46 -17.431 47.483 42.287 0.75 21.36 C ANISOU 2874 C ALEU B 46 2648 2652 2814 111 117 -82 C ATOM 2875 C BLEU B 46 -17.371 47.463 42.276 0.25 21.16 C ANISOU 2875 C BLEU B 46 2623 2626 2789 111 117 -82 C ATOM 2876 O ALEU B 46 -17.807 47.787 41.149 0.75 22.23 O ANISOU 2876 O ALEU B 46 2749 2767 2930 122 125 -59 O ATOM 2877 O BLEU B 46 -17.656 47.739 41.105 0.25 22.23 O ANISOU 2877 O BLEU B 46 2750 2766 2931 121 125 -58 O ATOM 2878 CB ALEU B 46 -15.198 48.093 43.250 0.75 21.95 C ANISOU 2878 CB ALEU B 46 2732 2678 2932 101 105 -110 C ATOM 2879 CB BLEU B 46 -15.165 48.110 43.312 0.25 22.09 C ANISOU 2879 CB BLEU B 46 2750 2695 2949 101 104 -112 C ATOM 2880 CG ALEU B 46 -14.471 47.957 41.911 0.75 26.07 C ANISOU 2880 CG ALEU B 46 3250 3189 3468 99 109 -82 C ATOM 2881 CG BLEU B 46 -14.227 48.079 42.100 0.25 25.41 C ANISOU 2881 CG BLEU B 46 3166 3098 3389 98 108 -87 C ATOM 2882 CD1ALEU B 46 -14.392 49.303 41.207 0.75 26.92 C ANISOU 2882 CD1ALEU B 46 3345 3268 3614 116 124 -67 C ATOM 2883 CD1BLEU B 46 -14.183 46.695 41.457 0.25 22.73 C ANISOU 2883 CD1BLEU B 46 2834 2784 3018 87 104 -70 C ATOM 2884 CD2ALEU B 46 -13.087 47.358 42.101 0.75 22.07 C ANISOU 2884 CD2ALEU B 46 2750 2669 2966 85 98 -88 C ATOM 2885 CD2BLEU B 46 -14.614 49.144 41.082 0.25 26.33 C ANISOU 2885 CD2BLEU B 46 3271 3201 3532 116 125 -64 C ATOM 2886 N LEU B 47 -17.682 46.286 42.824 1.00 20.73 N ANISOU 2886 N LEU B 47 2576 2596 2702 98 110 -91 N ATOM 2887 CA LEU B 47 -18.314 45.236 42.031 1.00 19.72 C ANISOU 2887 CA LEU B 47 2445 2496 2549 91 112 -75 C ATOM 2888 C LEU B 47 -19.725 45.626 41.611 1.00 22.14 C ANISOU 2888 C LEU B 47 2738 2824 2850 105 120 -67 C ATOM 2889 O LEU B 47 -20.168 45.284 40.510 1.00 17.22 O ANISOU 2889 O LEU B 47 2106 2218 2217 107 122 -50 O ATOM 2890 CB LEU B 47 -18.325 43.921 42.815 1.00 21.57 C ANISOU 2890 CB LEU B 47 2691 2748 2758 74 107 -86 C ATOM 2891 CG LEU B 47 -16.964 43.282 43.129 1.00 22.39 C ANISOU 2891 CG LEU B 47 2807 2837 2862 62 98 -90 C ATOM 2892 CD1 LEU B 47 -17.129 42.010 43.959 1.00 21.84 C ANISOU 2892 CD1 LEU B 47 2748 2785 2765 49 96 -98 C ATOM 2893 CD2 LEU B 47 -16.185 42.987 41.854 1.00 23.75 C ANISOU 2893 CD2 LEU B 47 2978 3002 3043 57 96 -71 C ATOM 2894 N ILE B 48 -20.453 46.320 42.487 1.00 17.19 N ANISOU 2894 N ILE B 48 2109 2197 2227 114 125 -81 N ATOM 2895 CA ILE B 48 -21.788 46.805 42.146 1.00 19.13 C ANISOU 2895 CA ILE B 48 2340 2461 2470 129 134 -74 C ATOM 2896 C ILE B 48 -21.714 47.814 41.003 1.00 20.28 C ANISOU 2896 C ILE B 48 2474 2594 2636 148 139 -52 C ATOM 2897 O ILE B 48 -22.463 47.724 40.023 1.00 19.83 O ANISOU 2897 O ILE B 48 2404 2560 2569 158 142 -35 O ATOM 2898 CB ILE B 48 -22.468 47.401 43.394 1.00 23.24 C ANISOU 2898 CB ILE B 48 2861 2980 2991 137 139 -95 C ATOM 2899 CG1 ILE B 48 -22.776 46.292 44.406 1.00 19.34 C ANISOU 2899 CG1 ILE B 48 2374 2504 2469 122 138 -110 C ATOM 2900 CG2 ILE B 48 -23.738 48.163 43.024 1.00 19.14 C ANISOU 2900 CG2 ILE B 48 2324 2472 2476 156 150 -86 C ATOM 2901 CD1 ILE B 48 -23.180 46.811 45.779 1.00 19.59 C ANISOU 2901 CD1 ILE B 48 2412 2533 2499 130 143 -132 C ATOM 2902 N MET B 49 -20.789 48.772 41.096 1.00 19.49 N ANISOU 2902 N MET B 49 2378 2459 2567 155 142 -52 N ATOM 2903 CA MET B 49 -20.729 49.849 40.112 1.00 23.53 C ANISOU 2903 CA MET B 49 2880 2955 3105 176 153 -29 C ATOM 2904 C MET B 49 -20.178 49.395 38.768 1.00 24.18 C ANISOU 2904 C MET B 49 2961 3044 3181 176 152 -2 C ATOM 2905 O MET B 49 -20.432 50.056 37.756 1.00 24.43 O ANISOU 2905 O MET B 49 2984 3078 3223 198 162 24 O ATOM 2906 CB MET B 49 -19.895 51.011 40.653 1.00 20.62 C ANISOU 2906 CB MET B 49 2515 2544 2778 181 160 -39 C ATOM 2907 CG MET B 49 -20.514 51.684 41.861 1.00 25.50 C ANISOU 2907 CG MET B 49 3132 3154 3402 186 163 -66 C ATOM 2908 SD MET B 49 -22.082 52.484 41.474 1.00 27.16 S ANISOU 2908 SD MET B 49 3326 3381 3613 213 178 -50 S ATOM 2909 CE MET B 49 -21.517 53.783 40.378 1.00 28.51 C ANISOU 2909 CE MET B 49 3489 3516 3829 235 195 -20 C ATOM 2910 N LEU B 50 -19.414 48.303 38.732 1.00 27.37 N ANISOU 2910 N LEU B 50 3375 3453 3570 156 142 -7 N ATOM 2911 CA LEU B 50 -18.979 47.718 37.469 1.00 19.00 C ANISOU 2911 CA LEU B 50 2315 2405 2500 156 141 15 C ATOM 2912 C LEU B 50 -19.945 46.650 36.985 1.00 20.75 C ANISOU 2912 C LEU B 50 2531 2669 2685 151 134 16 C ATOM 2913 O LEU B 50 -20.227 46.567 35.786 1.00 23.86 O ANISOU 2913 O LEU B 50 2916 3083 3067 164 135 35 O ATOM 2914 CB LEU B 50 -17.583 47.107 37.614 1.00 21.00 C ANISOU 2914 CB LEU B 50 2581 2639 2760 137 134 10 C ATOM 2915 CG LEU B 50 -16.387 48.053 37.522 1.00 28.96 C ANISOU 2915 CG LEU B 50 3590 3605 3807 142 142 18 C ATOM 2916 CD1 LEU B 50 -15.113 47.351 37.958 1.00 27.47 C ANISOU 2916 CD1 LEU B 50 3413 3401 3623 121 133 6 C ATOM 2917 CD2 LEU B 50 -16.250 48.574 36.097 1.00 33.14 C ANISOU 2917 CD2 LEU B 50 4113 4133 4346 162 155 52 C ATOM 2918 N GLY B 51 -20.464 45.840 37.911 1.00 23.75 N ANISOU 2918 N GLY B 51 2913 3063 3047 134 127 -7 N ATOM 2919 CA GLY B 51 -21.330 44.735 37.528 1.00 20.86 C ANISOU 2919 CA GLY B 51 2540 2734 2652 125 122 -10 C ATOM 2920 C GLY B 51 -22.616 45.174 36.854 1.00 21.65 C ANISOU 2920 C GLY B 51 2620 2862 2743 145 124 -1 C ATOM 2921 O GLY B 51 -23.039 44.576 35.863 1.00 22.97 O ANISOU 2921 O GLY B 51 2777 3058 2892 146 119 5 O ATOM 2922 N PHE B 52 -23.271 46.206 37.385 1.00 20.63 N ANISOU 2922 N PHE B 52 2485 2727 2628 160 132 -2 N ATOM 2923 CA PHE B 52 -24.528 46.636 36.772 1.00 20.10 C ANISOU 2923 CA PHE B 52 2397 2688 2552 181 134 7 C ATOM 2924 C PHE B 52 -24.343 47.124 35.337 1.00 22.80 C ANISOU 2924 C PHE B 52 2731 3039 2893 205 136 36 C ATOM 2925 O PHE B 52 -25.070 46.645 34.450 1.00 24.75 O ANISOU 2925 O PHE B 52 2964 3324 3118 212 128 40 O ATOM 2926 CB PHE B 52 -25.211 47.689 37.654 1.00 25.88 C ANISOU 2926 CB PHE B 52 3124 3409 3301 195 144 2 C ATOM 2927 CG PHE B 52 -26.305 48.447 36.955 1.00 26.04 C ANISOU 2927 CG PHE B 52 3124 3450 3320 223 149 18 C ATOM 2928 CD1 PHE B 52 -27.383 47.782 36.394 1.00 30.01 C ANISOU 2928 CD1 PHE B 52 3607 3996 3798 225 141 16 C ATOM 2929 CD2 PHE B 52 -26.253 49.827 36.854 1.00 29.65 C ANISOU 2929 CD2 PHE B 52 3579 3885 3803 250 161 34 C ATOM 2930 CE1 PHE B 52 -28.385 48.475 35.750 1.00 29.35 C ANISOU 2930 CE1 PHE B 52 3503 3936 3713 253 144 31 C ATOM 2931 CE2 PHE B 52 -27.255 50.528 36.212 1.00 32.21 C ANISOU 2931 CE2 PHE B 52 3884 4230 4126 279 167 52 C ATOM 2932 CZ PHE B 52 -28.321 49.852 35.657 1.00 33.25 C ANISOU 2932 CZ PHE B 52 3997 4408 4230 282 157 51 C ATOM 2933 N PRO B 53 -23.409 48.032 35.027 1.00 25.21 N ANISOU 2933 N PRO B 53 3045 3313 3222 218 145 54 N ATOM 2934 CA PRO B 53 -23.315 48.515 33.638 1.00 19.66 C ANISOU 2934 CA PRO B 53 2334 2621 2516 245 150 86 C ATOM 2935 C PRO B 53 -22.845 47.472 32.639 1.00 20.60 C ANISOU 2935 C PRO B 53 2456 2762 2609 238 140 91 C ATOM 2936 O PRO B 53 -23.380 47.414 31.526 1.00 19.17 O ANISOU 2936 O PRO B 53 2262 2616 2406 258 137 106 O ATOM 2937 CB PRO B 53 -22.325 49.685 33.738 1.00 23.33 C ANISOU 2937 CB PRO B 53 2808 3038 3018 257 166 103 C ATOM 2938 CG PRO B 53 -22.348 50.089 35.159 1.00 32.66 C ANISOU 2938 CG PRO B 53 3995 4192 4222 244 168 78 C ATOM 2939 CD PRO B 53 -22.555 48.822 35.928 1.00 24.46 C ANISOU 2939 CD PRO B 53 2963 3172 3160 215 153 49 C ATOM 2940 N AILE B 54 -21.851 46.650 32.989 0.57 19.81 N ANISOU 2940 N AILE B 54 2371 2645 2510 211 135 78 N ATOM 2941 N BILE B 54 -21.841 46.664 32.990 0.43 19.83 N ANISOU 2941 N BILE B 54 2374 2647 2513 211 135 78 N ATOM 2942 CA AILE B 54 -21.319 45.712 32.008 0.57 20.29 C ANISOU 2942 CA AILE B 54 2436 2724 2550 205 128 83 C ATOM 2943 CA BILE B 54 -21.314 45.698 32.032 0.43 20.31 C ANISOU 2943 CA BILE B 54 2438 2726 2553 204 128 82 C ATOM 2944 C AILE B 54 -22.284 44.564 31.741 0.57 21.91 C ANISOU 2944 C AILE B 54 2630 2973 2723 194 114 64 C ATOM 2945 C BILE B 54 -22.358 44.641 31.703 0.43 21.97 C ANISOU 2945 C BILE B 54 2635 2982 2730 196 114 65 C ATOM 2946 O AILE B 54 -22.229 43.954 30.666 0.57 21.55 O ANISOU 2946 O AILE B 54 2580 2954 2654 198 107 68 O ATOM 2947 O BILE B 54 -22.441 44.174 30.560 0.43 21.32 O ANISOU 2947 O BILE B 54 2547 2930 2625 205 108 72 O ATOM 2948 CB AILE B 54 -19.936 45.184 32.436 0.57 21.58 C ANISOU 2948 CB AILE B 54 2618 2855 2726 181 128 76 C ATOM 2949 CB BILE B 54 -20.014 45.068 32.562 0.43 21.52 C ANISOU 2949 CB BILE B 54 2610 2849 2717 178 126 72 C ATOM 2950 CG1AILE B 54 -19.212 44.582 31.227 0.57 23.10 C ANISOU 2950 CG1AILE B 54 2815 3060 2904 184 127 90 C ATOM 2951 CG1BILE B 54 -18.975 46.156 32.838 0.43 24.39 C ANISOU 2951 CG1BILE B 54 2982 3167 3117 186 139 87 C ATOM 2952 CG2AILE B 54 -20.062 44.167 33.566 0.57 21.45 C ANISOU 2952 CG2AILE B 54 2608 2839 2704 150 119 46 C ATOM 2953 CG2BILE B 54 -19.460 44.063 31.564 0.43 22.71 C ANISOU 2953 CG2BILE B 54 2765 3017 2847 172 121 76 C ATOM 2954 CD1AILE B 54 -17.750 44.311 31.452 0.57 20.97 C ANISOU 2954 CD1AILE B 54 2561 2756 2652 168 130 92 C ATOM 2955 CD1BILE B 54 -17.631 45.620 33.277 0.43 19.92 C ANISOU 2955 CD1BILE B 54 2432 2573 2564 163 137 78 C ATOM 2956 N ASN B 55 -23.178 44.257 32.681 1.00 23.52 N ANISOU 2956 N ASN B 55 2827 3185 2926 179 110 41 N ATOM 2957 CA ASN B 55 -24.184 43.232 32.433 1.00 19.47 C ANISOU 2957 CA ASN B 55 2299 2711 2388 168 99 22 C ATOM 2958 C ASN B 55 -25.432 43.809 31.771 1.00 21.82 C ANISOU 2958 C ASN B 55 2572 3045 2673 196 96 29 C ATOM 2959 O ASN B 55 -26.018 43.163 30.892 1.00 19.00 O ANISOU 2959 O ASN B 55 2199 2727 2293 198 85 22 O ATOM 2960 CB ASN B 55 -24.525 42.510 33.735 1.00 19.36 C ANISOU 2960 CB ASN B 55 2288 2688 2379 140 99 -4 C ATOM 2961 CG ASN B 55 -23.420 41.575 34.181 1.00 20.78 C ANISOU 2961 CG ASN B 55 2488 2845 2563 113 99 -14 C ATOM 2962 OD1 ASN B 55 -23.178 40.543 33.557 1.00 18.44 O ANISOU 2962 OD1 ASN B 55 2192 2562 2253 100 93 -21 O ATOM 2963 ND2 ASN B 55 -22.746 41.929 35.267 1.00 22.30 N ANISOU 2963 ND2 ASN B 55 2697 3004 2773 106 105 -15 N ATOM 2964 N PHE B 56 -25.838 45.028 32.143 1.00 17.96 N ANISOU 2964 N PHE B 56 2078 2545 2201 217 106 43 N ATOM 2965 CA PHE B 56 -26.944 45.657 31.430 1.00 21.41 C ANISOU 2965 CA PHE B 56 2492 3016 2626 248 104 55 C ATOM 2966 C PHE B 56 -26.589 45.881 29.967 1.00 22.29 C ANISOU 2966 C PHE B 56 2600 3148 2720 275 101 80 C ATOM 2967 O PHE B 56 -27.424 45.670 29.082 1.00 20.66 O ANISOU 2967 O PHE B 56 2374 2988 2488 292 90 80 O ATOM 2968 CB PHE B 56 -27.345 46.984 32.075 1.00 23.89 C ANISOU 2968 CB PHE B 56 2804 3310 2964 268 117 67 C ATOM 2969 CG PHE B 56 -28.529 47.638 31.405 1.00 21.86 C ANISOU 2969 CG PHE B 56 2522 3089 2696 302 116 81 C ATOM 2970 CD1 PHE B 56 -29.822 47.267 31.739 1.00 28.10 C ANISOU 2970 CD1 PHE B 56 3290 3910 3476 297 108 61 C ATOM 2971 CD2 PHE B 56 -28.350 48.604 30.424 1.00 28.64 C ANISOU 2971 CD2 PHE B 56 3378 3951 3555 340 124 116 C ATOM 2972 CE1 PHE B 56 -30.914 47.854 31.118 1.00 25.00 C ANISOU 2972 CE1 PHE B 56 2872 3553 3074 329 106 73 C ATOM 2973 CE2 PHE B 56 -29.440 49.192 29.797 1.00 22.53 C ANISOU 2973 CE2 PHE B 56 2580 3213 2769 374 122 131 C ATOM 2974 CZ PHE B 56 -30.722 48.817 30.148 1.00 22.81 C ANISOU 2974 CZ PHE B 56 2592 3280 2793 369 112 108 C ATOM 2975 N ALEU B 57 -25.356 46.314 29.696 0.41 21.28 N ANISOU 2975 N ALEU B 57 2492 2989 2605 281 112 102 N ATOM 2976 N BLEU B 57 -25.356 46.318 29.694 0.59 21.23 N ANISOU 2976 N BLEU B 57 2485 2983 2599 281 112 102 N ATOM 2977 CA ALEU B 57 -24.940 46.542 28.316 0.41 22.11 C ANISOU 2977 CA ALEU B 57 2596 3112 2693 309 113 130 C ATOM 2978 CA BLEU B 57 -24.941 46.541 28.312 0.59 22.00 C ANISOU 2978 CA BLEU B 57 2582 3099 2680 310 113 130 C ATOM 2979 C ALEU B 57 -24.940 45.246 27.514 0.41 22.66 C ANISOU 2979 C ALEU B 57 2662 3219 2729 297 96 112 C ATOM 2980 C BLEU B 57 -24.944 45.243 27.514 0.59 22.68 C ANISOU 2980 C BLEU B 57 2664 3222 2731 297 96 112 C ATOM 2981 O ALEU B 57 -25.337 45.231 26.343 0.41 20.84 O ANISOU 2981 O ALEU B 57 2419 3031 2470 324 89 123 O ATOM 2982 O BLEU B 57 -25.341 45.228 26.342 0.59 20.73 O ANISOU 2982 O BLEU B 57 2404 3017 2455 324 89 123 O ATOM 2983 CB ALEU B 57 -23.559 47.195 28.291 0.41 22.49 C ANISOU 2983 CB ALEU B 57 2664 3113 2767 314 131 155 C ATOM 2984 CB BLEU B 57 -23.556 47.187 28.274 0.59 22.39 C ANISOU 2984 CB BLEU B 57 2652 3101 2754 314 130 155 C ATOM 2985 CG ALEU B 57 -23.007 47.549 26.911 0.41 25.02 C ANISOU 2985 CG ALEU B 57 2986 3445 3074 346 139 190 C ATOM 2986 CG BLEU B 57 -23.476 48.692 28.525 0.59 24.11 C ANISOU 2986 CG BLEU B 57 2870 3286 3006 340 151 182 C ATOM 2987 CD1ALEU B 57 -23.973 48.462 26.176 0.41 27.89 C ANISOU 2987 CD1ALEU B 57 3332 3841 3426 390 143 216 C ATOM 2988 CD1BLEU B 57 -22.025 49.142 28.544 0.59 28.96 C ANISOU 2988 CD1BLEU B 57 3503 3851 3650 336 168 200 C ATOM 2989 CD2ALEU B 57 -21.635 48.194 27.038 0.41 29.66 C ANISOU 2989 CD2ALEU B 57 3592 3980 3696 346 159 212 C ATOM 2990 CD2BLEU B 57 -24.262 49.456 27.470 0.59 28.12 C ANISOU 2990 CD2BLEU B 57 3361 3827 3497 385 156 214 C ATOM 2991 N THR B 58 -24.485 44.148 28.124 1.00 18.66 N ANISOU 2991 N THR B 58 2166 2699 2225 259 90 84 N ATOM 2992 CA THR B 58 -24.490 42.862 27.434 1.00 24.03 C ANISOU 2992 CA THR B 58 2842 3411 2879 244 75 63 C ATOM 2993 C THR B 58 -25.914 42.415 27.127 1.00 25.58 C ANISOU 2993 C THR B 58 3010 3656 3052 247 59 41 C ATOM 2994 O THR B 58 -26.193 41.900 26.037 1.00 22.57 O ANISOU 2994 O THR B 58 2618 3318 2642 258 46 34 O ATOM 2995 CB THR B 58 -23.752 41.816 28.276 1.00 23.14 C ANISOU 2995 CB THR B 58 2747 3268 2779 203 75 40 C ATOM 2996 OG1 THR B 58 -22.366 42.169 28.362 1.00 19.75 O ANISOU 2996 OG1 THR B 58 2339 2798 2366 202 87 60 O ATOM 2997 CG2 THR B 58 -23.868 40.428 27.657 1.00 20.16 C ANISOU 2997 CG2 THR B 58 2363 2919 2377 184 62 13 C ATOM 2998 N LEU B 59 -26.829 42.615 28.074 1.00 19.22 N ANISOU 2998 N LEU B 59 2194 2849 2261 238 60 28 N ATOM 2999 CA LEU B 59 -28.239 42.342 27.812 1.00 22.43 C ANISOU 2999 CA LEU B 59 2569 3301 2651 244 46 8 C ATOM 3000 C LEU B 59 -28.761 43.213 26.674 1.00 25.57 C ANISOU 3000 C LEU B 59 2950 3738 3027 290 42 33 C ATOM 3001 O LEU B 59 -29.394 42.718 25.733 1.00 23.20 O ANISOU 3001 O LEU B 59 2629 3487 2698 301 24 19 O ATOM 3002 CB LEU B 59 -29.048 42.567 29.094 1.00 21.69 C ANISOU 3002 CB LEU B 59 2469 3193 2581 230 53 -4 C ATOM 3003 CG LEU B 59 -30.568 42.345 29.144 1.00 26.44 C ANISOU 3003 CG LEU B 59 3037 3834 3175 231 43 -25 C ATOM 3004 CD1 LEU B 59 -31.002 42.051 30.573 1.00 28.64 C ANISOU 3004 CD1 LEU B 59 3316 4088 3477 202 53 -44 C ATOM 3005 CD2 LEU B 59 -31.335 43.548 28.615 1.00 28.06 C ANISOU 3005 CD2 LEU B 59 3224 4065 3373 274 42 -2 C ATOM 3006 N TYR B 60 -28.484 44.517 26.740 1.00 23.78 N ANISOU 3006 N TYR B 60 2733 3489 2815 319 57 68 N ATOM 3007 CA TYR B 60 -29.054 45.464 25.788 1.00 23.72 C ANISOU 3007 CA TYR B 60 2708 3514 2789 366 56 97 C ATOM 3008 C TYR B 60 -28.581 45.179 24.367 1.00 24.28 C ANISOU 3008 C TYR B 60 2781 3619 2826 389 49 110 C ATOM 3009 O TYR B 60 -29.389 45.118 23.431 1.00 23.03 O ANISOU 3009 O TYR B 60 2599 3516 2635 416 33 108 O ATOM 3010 CB TYR B 60 -28.683 46.885 26.211 1.00 27.22 C ANISOU 3010 CB TYR B 60 3164 3916 3262 389 80 134 C ATOM 3011 CG TYR B 60 -29.364 47.974 25.425 1.00 23.58 C ANISOU 3011 CG TYR B 60 2686 3484 2790 440 84 167 C ATOM 3012 CD1 TYR B 60 -30.602 48.465 25.813 1.00 29.65 C ANISOU 3012 CD1 TYR B 60 3432 4270 3563 454 82 163 C ATOM 3013 CD2 TYR B 60 -28.761 48.526 24.303 1.00 32.65 C ANISOU 3013 CD2 TYR B 60 3842 4640 3924 477 93 206 C ATOM 3014 CE1 TYR B 60 -31.230 49.472 25.092 1.00 37.94 C ANISOU 3014 CE1 TYR B 60 4466 5347 4603 503 87 196 C ATOM 3015 CE2 TYR B 60 -29.378 49.530 23.578 1.00 31.71 C ANISOU 3015 CE2 TYR B 60 3707 4547 3793 528 99 240 C ATOM 3016 CZ TYR B 60 -30.610 49.998 23.976 1.00 29.92 C ANISOU 3016 CZ TYR B 60 3457 4338 3571 541 96 236 C ATOM 3017 OH TYR B 60 -31.224 50.998 23.260 1.00 37.42 O ANISOU 3017 OH TYR B 60 4392 5316 4510 593 102 272 O ATOM 3018 N VAL B 61 -27.270 44.983 24.194 1.00 20.62 N ANISOU 3018 N VAL B 61 2342 3124 2367 380 58 122 N ATOM 3019 CA VAL B 61 -26.711 44.718 22.871 1.00 24.82 C ANISOU 3019 CA VAL B 61 2878 3685 2868 402 54 135 C ATOM 3020 C VAL B 61 -27.297 43.438 22.282 1.00 25.26 C ANISOU 3020 C VAL B 61 2917 3792 2890 388 28 95 C ATOM 3021 O VAL B 61 -27.655 43.393 21.099 1.00 25.46 O ANISOU 3021 O VAL B 61 2928 3869 2876 420 16 99 O ATOM 3022 CB VAL B 61 -25.172 44.662 22.948 1.00 25.93 C ANISOU 3022 CB VAL B 61 3048 3777 3025 388 71 152 C ATOM 3023 CG1 VAL B 61 -24.571 44.188 21.622 1.00 23.65 C ANISOU 3023 CG1 VAL B 61 2766 3520 2702 407 67 160 C ATOM 3024 CG2 VAL B 61 -24.612 46.028 23.317 1.00 22.90 C ANISOU 3024 CG2 VAL B 61 2678 3348 2677 408 97 192 C ATOM 3025 N THR B 62 -27.410 42.382 23.092 1.00 22.44 N ANISOU 3025 N THR B 62 2559 3421 2546 342 20 54 N ATOM 3026 CA THR B 62 -27.914 41.111 22.578 1.00 24.56 C ANISOU 3026 CA THR B 62 2810 3731 2789 324 -2 12 C ATOM 3027 C THR B 62 -29.327 41.261 22.023 1.00 25.27 C ANISOU 3027 C THR B 62 2866 3881 2856 348 -21 -1 C ATOM 3028 O THR B 62 -29.626 40.791 20.918 1.00 25.25 O ANISOU 3028 O THR B 62 2847 3931 2817 365 -40 -16 O ATOM 3029 CB THR B 62 -27.886 40.042 23.674 1.00 25.18 C ANISOU 3029 CB THR B 62 2894 3779 2894 271 -2 -26 C ATOM 3030 OG1 THR B 62 -26.541 39.853 24.138 1.00 19.46 O ANISOU 3030 OG1 THR B 62 2202 3004 2190 251 14 -14 O ATOM 3031 CG2 THR B 62 -28.418 38.718 23.132 1.00 24.00 C ANISOU 3031 CG2 THR B 62 2724 3668 2725 251 -22 -71 C ATOM 3032 N VAL B 63 -30.209 41.920 22.778 1.00 25.62 N ANISOU 3032 N VAL B 63 2895 3921 2919 352 -18 3 N ATOM 3033 CA VAL B 63 -31.594 42.079 22.350 1.00 26.05 C ANISOU 3033 CA VAL B 63 2913 4031 2954 374 -36 -10 C ATOM 3034 C VAL B 63 -31.687 42.984 21.127 1.00 28.70 C ANISOU 3034 C VAL B 63 3242 4408 3255 432 -39 26 C ATOM 3035 O VAL B 63 -32.533 42.769 20.249 1.00 25.81 O ANISOU 3035 O VAL B 63 2847 4105 2856 455 -62 10 O ATOM 3036 CB VAL B 63 -32.447 42.605 23.523 1.00 27.90 C ANISOU 3036 CB VAL B 63 3136 4245 3221 365 -27 -11 C ATOM 3037 CG1 VAL B 63 -33.866 42.878 23.073 1.00 31.81 C ANISOU 3037 CG1 VAL B 63 3592 4798 3699 391 -45 -20 C ATOM 3038 CG2 VAL B 63 -32.436 41.609 24.669 1.00 28.47 C ANISOU 3038 CG2 VAL B 63 3212 4283 3321 310 -24 -47 C ATOM 3039 N GLN B 64 -30.818 43.998 21.039 1.00 21.82 N ANISOU 3039 N GLN B 64 2395 3503 2392 458 -17 74 N ATOM 3040 CA GLN B 64 -30.891 44.959 19.942 1.00 28.92 C ANISOU 3040 CA GLN B 64 3289 4437 3262 517 -14 117 C ATOM 3041 C GLN B 64 -30.505 44.334 18.606 1.00 29.73 C ANISOU 3041 C GLN B 64 3392 4587 3318 536 -28 111 C ATOM 3042 O GLN B 64 -31.056 44.718 17.566 1.00 28.28 O ANISOU 3042 O GLN B 64 3190 4460 3095 583 -40 126 O ATOM 3043 CB GLN B 64 -29.987 46.158 20.232 1.00 24.98 C ANISOU 3043 CB GLN B 64 2817 3883 2790 536 19 169 C ATOM 3044 CG GLN B 64 -30.246 47.359 19.342 1.00 32.57 C ANISOU 3044 CG GLN B 64 3771 4872 3733 598 29 220 C ATOM 3045 CD GLN B 64 -29.206 48.451 19.513 1.00 30.89 C ANISOU 3045 CD GLN B 64 3586 4600 3552 615 64 271 C ATOM 3046 OE1 GLN B 64 -28.044 48.176 19.807 1.00 31.43 O ANISOU 3046 OE1 GLN B 64 3678 4622 3640 588 77 271 O ATOM 3047 NE2 GLN B 64 -29.621 49.698 19.331 1.00 37.19 N ANISOU 3047 NE2 GLN B 64 4376 5399 4357 660 80 313 N ATOM 3048 N HIS B 65 -29.574 43.384 18.608 1.00 30.77 N ANISOU 3048 N HIS B 65 3543 4697 3451 502 -28 91 N ATOM 3049 CA HIS B 65 -29.000 42.828 17.385 1.00 21.18 C ANISOU 3049 CA HIS B 65 2335 3519 2195 520 -37 88 C ATOM 3050 C HIS B 65 -29.537 41.415 17.185 1.00 24.04 C ANISOU 3050 C HIS B 65 2677 3918 2539 488 -66 25 C ATOM 3051 O HIS B 65 -29.133 40.488 17.893 1.00 27.73 O ANISOU 3051 O HIS B 65 3155 4349 3033 438 -65 -7 O ATOM 3052 CB HIS B 65 -27.474 42.830 17.456 1.00 26.38 C ANISOU 3052 CB HIS B 65 3029 4123 2870 508 -13 113 C ATOM 3053 CG HIS B 65 -26.873 44.194 17.607 1.00 29.75 C ANISOU 3053 CG HIS B 65 3474 4509 3319 537 18 172 C ATOM 3054 ND1 HIS B 65 -26.420 44.932 16.533 1.00 31.58 N ANISOU 3054 ND1 HIS B 65 3713 4760 3525 589 32 219 N ATOM 3055 CD2 HIS B 65 -26.644 44.952 18.706 1.00 28.30 C ANISOU 3055 CD2 HIS B 65 3302 4267 3184 523 38 191 C ATOM 3056 CE1 HIS B 65 -25.939 46.084 16.966 1.00 34.01 C ANISOU 3056 CE1 HIS B 65 4034 5018 3868 603 61 265 C ATOM 3057 NE2 HIS B 65 -26.066 46.123 18.280 1.00 24.84 N ANISOU 3057 NE2 HIS B 65 2876 3810 2753 563 64 247 N ATOM 3058 N LYS B 66 -30.433 41.251 16.209 1.00 28.75 N ANISOU 3058 N LYS B 66 3244 4587 3092 518 -92 7 N ATOM 3059 CA LYS B 66 -31.079 39.963 15.969 1.00 24.49 C ANISOU 3059 CA LYS B 66 2679 4086 2538 490 -121 -58 C ATOM 3060 C LYS B 66 -30.132 38.917 15.394 1.00 32.53 C ANISOU 3060 C LYS B 66 3715 5104 3541 472 -124 -82 C ATOM 3061 O LYS B 66 -30.491 37.736 15.369 1.00 36.59 O ANISOU 3061 O LYS B 66 4213 5634 4054 438 -143 -139 O ATOM 3062 CB LYS B 66 -32.271 40.136 15.027 1.00 35.46 C ANISOU 3062 CB LYS B 66 4030 5558 3884 532 -150 -72 C ATOM 3063 N LYS B 67 -28.949 39.319 14.928 1.00 32.59 N ANISOU 3063 N LYS B 67 3755 5092 3538 493 -104 -40 N ATOM 3064 CA LYS B 67 -27.960 38.365 14.444 1.00 26.27 C ANISOU 3064 CA LYS B 67 2973 4283 2724 476 -103 -60 C ATOM 3065 C LYS B 67 -27.347 37.542 15.570 1.00 29.98 C ANISOU 3065 C LYS B 67 3461 4687 3243 415 -91 -83 C ATOM 3066 O LYS B 67 -26.763 36.488 15.301 1.00 29.00 O ANISOU 3066 O LYS B 67 3346 4558 3114 390 -94 -114 O ATOM 3067 CB LYS B 67 -26.852 39.102 13.692 1.00 31.61 C ANISOU 3067 CB LYS B 67 3677 4952 3379 517 -81 -4 C ATOM 3068 CG LYS B 67 -26.078 40.088 14.562 1.00 29.52 C ANISOU 3068 CG LYS B 67 3439 4618 3160 514 -47 49 C ATOM 3069 CD LYS B 67 -25.202 41.020 13.728 1.00 34.03 C ANISOU 3069 CD LYS B 67 4030 5188 3710 563 -24 109 C ATOM 3070 CE LYS B 67 -24.041 40.280 13.089 1.00 33.20 C ANISOU 3070 CE LYS B 67 3948 5078 3590 557 -16 104 C ATOM 3071 NZ LYS B 67 -23.256 41.147 12.162 1.00 50.91 N ANISOU 3071 NZ LYS B 67 6207 7326 5809 610 8 163 N ATOM 3072 N LEU B 68 -27.459 38.000 16.817 1.00 28.07 N ANISOU 3072 N LEU B 68 3224 4395 3046 391 -76 -69 N ATOM 3073 CA LEU B 68 -26.813 37.333 17.949 1.00 27.27 C ANISOU 3073 CA LEU B 68 3142 4230 2990 338 -62 -83 C ATOM 3074 C LEU B 68 -27.788 36.327 18.553 1.00 27.54 C ANISOU 3074 C LEU B 68 3151 4272 3041 297 -78 -138 C ATOM 3075 O LEU B 68 -28.395 36.548 19.602 1.00 34.06 O ANISOU 3075 O LEU B 68 3969 5075 3898 278 -74 -140 O ATOM 3076 CB LEU B 68 -26.351 38.361 18.976 1.00 25.47 C ANISOU 3076 CB LEU B 68 2935 3945 2799 337 -38 -40 C ATOM 3077 CG LEU B 68 -25.289 39.348 18.488 1.00 25.85 C ANISOU 3077 CG LEU B 68 3006 3973 2841 372 -16 15 C ATOM 3078 CD1 LEU B 68 -25.115 40.490 19.471 1.00 24.73 C ANISOU 3078 CD1 LEU B 68 2876 3783 2738 374 5 52 C ATOM 3079 CD2 LEU B 68 -23.967 38.636 18.253 1.00 24.37 C ANISOU 3079 CD2 LEU B 68 2845 3759 2655 354 -6 14 C ATOM 3080 N ARG B 69 -27.935 35.186 17.868 1.00 28.31 N ANISOU 3080 N ARG B 69 3236 4402 3120 284 -96 -184 N ATOM 3081 CA ARG B 69 -28.836 34.137 18.333 1.00 27.10 C ANISOU 3081 CA ARG B 69 3056 4254 2985 244 -110 -240 C ATOM 3082 C ARG B 69 -28.203 32.750 18.217 1.00 29.86 C ANISOU 3082 C ARG B 69 3416 4587 3344 207 -109 -279 C ATOM 3083 O ARG B 69 -28.911 31.754 18.035 1.00 29.27 O ANISOU 3083 O ARG B 69 3314 4535 3271 184 -126 -333 O ATOM 3084 CB ARG B 69 -30.162 34.172 17.569 1.00 31.18 C ANISOU 3084 CB ARG B 69 3531 4842 3473 267 -138 -270 C ATOM 3085 CG ARG B 69 -30.903 35.503 17.638 1.00 34.14 C ANISOU 3085 CG ARG B 69 3892 5239 3839 306 -140 -233 C ATOM 3086 CD ARG B 69 -31.517 35.749 19.011 1.00 34.39 C ANISOU 3086 CD ARG B 69 3917 5232 3916 278 -128 -230 C ATOM 3087 NE ARG B 69 -32.181 37.047 19.089 1.00 33.72 N ANISOU 3087 NE ARG B 69 3821 5164 3826 316 -127 -194 N ATOM 3088 CZ ARG B 69 -31.604 38.158 19.529 1.00 33.24 C ANISOU 3088 CZ ARG B 69 3787 5067 3777 335 -105 -141 C ATOM 3089 NH1 ARG B 69 -30.342 38.171 19.932 1.00 23.40 N ANISOU 3089 NH1 ARG B 69 2578 3767 2548 321 -83 -118 N ATOM 3090 NH2 ARG B 69 -32.312 39.283 19.571 1.00 34.51 N ANISOU 3090 NH2 ARG B 69 3934 5246 3934 370 -104 -112 N ATOM 3091 N THR B 70 -26.883 32.665 18.314 1.00 21.55 N ANISOU 3091 N THR B 70 2398 3492 2297 201 -90 -254 N ATOM 3092 CA THR B 70 -26.211 31.381 18.415 1.00 24.21 C ANISOU 3092 CA THR B 70 2748 3802 2651 164 -85 -286 C ATOM 3093 C THR B 70 -26.384 30.833 19.828 1.00 24.83 C ANISOU 3093 C THR B 70 2827 3828 2778 116 -71 -299 C ATOM 3094 O THR B 70 -26.793 31.558 20.740 1.00 27.04 O ANISOU 3094 O THR B 70 3105 4089 3078 115 -63 -276 O ATOM 3095 CB THR B 70 -24.733 31.533 18.047 1.00 23.17 C ANISOU 3095 CB THR B 70 2651 3643 2509 176 -68 -253 C ATOM 3096 OG1 THR B 70 -24.079 32.376 19.002 1.00 26.37 O ANISOU 3096 OG1 THR B 70 3081 3998 2942 175 -47 -205 O ATOM 3097 CG2 THR B 70 -24.588 32.147 16.661 1.00 24.48 C ANISOU 3097 CG2 THR B 70 2816 3861 2623 228 -78 -234 C ATOM 3098 N PRO B 71 -26.120 29.540 20.039 1.00 25.28 N ANISOU 3098 N PRO B 71 2887 3863 2857 78 -67 -335 N ATOM 3099 CA PRO B 71 -26.156 29.012 21.414 1.00 22.73 C ANISOU 3099 CA PRO B 71 2569 3487 2580 36 -49 -340 C ATOM 3100 C PRO B 71 -25.264 29.783 22.375 1.00 23.89 C ANISOU 3100 C PRO B 71 2748 3584 2745 38 -28 -289 C ATOM 3101 O PRO B 71 -25.629 29.975 23.541 1.00 22.07 O ANISOU 3101 O PRO B 71 2517 3326 2542 21 -17 -281 O ATOM 3102 CB PRO B 71 -25.687 27.563 21.234 1.00 26.32 C ANISOU 3102 CB PRO B 71 3028 3924 3050 4 -44 -378 C ATOM 3103 CG PRO B 71 -26.156 27.201 19.858 1.00 26.65 C ANISOU 3103 CG PRO B 71 3046 4024 3056 20 -68 -417 C ATOM 3104 CD PRO B 71 -26.041 28.460 19.034 1.00 24.74 C ANISOU 3104 CD PRO B 71 2808 3822 2771 71 -80 -381 C ATOM 3105 N LEU B 72 -24.102 30.239 21.907 1.00 24.80 N ANISOU 3105 N LEU B 72 2890 3689 2844 59 -22 -257 N ATOM 3106 CA LEU B 72 -23.235 31.057 22.745 1.00 22.96 C ANISOU 3106 CA LEU B 72 2684 3411 2628 63 -4 -212 C ATOM 3107 C LEU B 72 -23.906 32.379 23.109 1.00 22.45 C ANISOU 3107 C LEU B 72 2611 3356 2562 87 -5 -184 C ATOM 3108 O LEU B 72 -23.835 32.820 24.261 1.00 21.06 O ANISOU 3108 O LEU B 72 2445 3145 2413 76 7 -166 O ATOM 3109 CB LEU B 72 -21.905 31.298 22.031 1.00 20.50 C ANISOU 3109 CB LEU B 72 2399 3091 2301 83 4 -184 C ATOM 3110 CG LEU B 72 -20.829 32.105 22.762 1.00 23.12 C ANISOU 3110 CG LEU B 72 2757 3375 2652 88 22 -140 C ATOM 3111 CD1 LEU B 72 -20.259 31.324 23.940 1.00 24.27 C ANISOU 3111 CD1 LEU B 72 2919 3472 2832 50 35 -148 C ATOM 3112 CD2 LEU B 72 -19.722 32.493 21.788 1.00 24.83 C ANISOU 3112 CD2 LEU B 72 2992 3594 2849 115 28 -113 C ATOM 3113 N ASN B 73 -24.574 33.019 22.143 1.00 21.12 N ANISOU 3113 N ASN B 73 2425 3238 2363 122 -20 -181 N ATOM 3114 CA ASN B 73 -25.224 34.299 22.416 1.00 21.67 C ANISOU 3114 CA ASN B 73 2484 3316 2431 148 -20 -153 C ATOM 3115 C ASN B 73 -26.330 34.147 23.454 1.00 22.41 C ANISOU 3115 C ASN B 73 2559 3406 2550 125 -21 -174 C ATOM 3116 O ASN B 73 -26.504 35.013 24.319 1.00 20.78 O ANISOU 3116 O ASN B 73 2357 3177 2362 129 -11 -150 O ATOM 3117 CB ASN B 73 -25.791 34.901 21.128 1.00 25.78 C ANISOU 3117 CB ASN B 73 2986 3896 2912 192 -36 -147 C ATOM 3118 CG ASN B 73 -24.736 35.121 20.062 1.00 22.81 C ANISOU 3118 CG ASN B 73 2630 3529 2509 220 -32 -122 C ATOM 3119 OD1 ASN B 73 -24.903 34.700 18.919 1.00 24.90 O ANISOU 3119 OD1 ASN B 73 2882 3839 2737 238 -47 -141 O ATOM 3120 ND2 ASN B 73 -23.647 35.780 20.429 1.00 26.05 N ANISOU 3120 ND2 ASN B 73 3067 3895 2935 226 -11 -82 N ATOM 3121 N TYR B 74 -27.099 33.058 23.373 1.00 25.98 N ANISOU 3121 N TYR B 74 2988 3878 3006 100 -32 -219 N ATOM 3122 CA TYR B 74 -28.172 32.828 24.336 1.00 19.64 C ANISOU 3122 CA TYR B 74 2164 3069 2228 76 -30 -239 C ATOM 3123 C TYR B 74 -27.624 32.616 25.741 1.00 20.98 C ANISOU 3123 C TYR B 74 2357 3181 2433 46 -8 -227 C ATOM 3124 O TYR B 74 -28.129 33.194 26.710 1.00 19.29 O ANISOU 3124 O TYR B 74 2141 2952 2236 45 0 -215 O ATOM 3125 CB TYR B 74 -29.007 31.625 23.909 1.00 21.16 C ANISOU 3125 CB TYR B 74 2326 3291 2422 53 -44 -292 C ATOM 3126 CG TYR B 74 -30.006 31.929 22.826 1.00 22.70 C ANISOU 3126 CG TYR B 74 2487 3550 2586 82 -69 -310 C ATOM 3127 CD1 TYR B 74 -31.143 32.665 23.103 1.00 28.96 C ANISOU 3127 CD1 TYR B 74 3255 4368 3382 96 -75 -306 C ATOM 3128 CD2 TYR B 74 -29.823 31.469 21.532 1.00 26.17 C ANISOU 3128 CD2 TYR B 74 2919 4030 2994 96 -87 -333 C ATOM 3129 CE1 TYR B 74 -32.070 32.939 22.128 1.00 36.11 C ANISOU 3129 CE1 TYR B 74 4127 5335 4259 124 -100 -322 C ATOM 3130 CE2 TYR B 74 -30.746 31.740 20.545 1.00 30.97 C ANISOU 3130 CE2 TYR B 74 3494 4701 3570 124 -112 -351 C ATOM 3131 CZ TYR B 74 -31.868 32.478 20.852 1.00 32.86 C ANISOU 3131 CZ TYR B 74 3707 4964 3813 139 -119 -345 C ATOM 3132 OH TYR B 74 -32.801 32.760 19.884 1.00 37.80 O ANISOU 3132 OH TYR B 74 4299 5656 4407 170 -145 -362 O ATOM 3133 N ILE B 75 -26.590 31.782 25.868 1.00 21.19 N ANISOU 3133 N ILE B 75 2406 3175 2468 25 2 -231 N ATOM 3134 CA ILE B 75 -26.036 31.472 27.184 1.00 18.62 C ANISOU 3134 CA ILE B 75 2103 2799 2174 -2 22 -221 C ATOM 3135 C ILE B 75 -25.441 32.722 27.825 1.00 22.44 C ANISOU 3135 C ILE B 75 2609 3257 2661 17 31 -179 C ATOM 3136 O ILE B 75 -25.636 32.981 29.017 1.00 21.27 O ANISOU 3136 O ILE B 75 2465 3083 2532 7 42 -171 O ATOM 3137 CB ILE B 75 -25.003 30.339 27.064 1.00 21.17 C ANISOU 3137 CB ILE B 75 2444 3095 2503 -25 29 -232 C ATOM 3138 CG1 ILE B 75 -25.679 29.054 26.578 1.00 23.10 C ANISOU 3138 CG1 ILE B 75 2665 3359 2752 -48 23 -278 C ATOM 3139 CG2 ILE B 75 -24.304 30.100 28.391 1.00 19.25 C ANISOU 3139 CG2 ILE B 75 2226 2802 2287 -46 49 -216 C ATOM 3140 CD1 ILE B 75 -26.648 28.461 27.581 1.00 25.03 C ANISOU 3140 CD1 ILE B 75 2892 3592 3028 -77 33 -299 C ATOM 3141 N LEU B 76 -24.722 33.526 27.043 1.00 22.09 N ANISOU 3141 N LEU B 76 2576 3218 2597 46 27 -153 N ATOM 3142 CA LEU B 76 -24.133 34.740 27.598 1.00 20.36 C ANISOU 3142 CA LEU B 76 2376 2973 2388 64 37 -116 C ATOM 3143 C LEU B 76 -25.208 35.742 28.003 1.00 19.71 C ANISOU 3143 C LEU B 76 2276 2904 2307 81 35 -108 C ATOM 3144 O LEU B 76 -25.061 36.440 29.014 1.00 25.55 O ANISOU 3144 O LEU B 76 3028 3616 3066 81 46 -91 O ATOM 3145 CB LEU B 76 -23.156 35.353 26.592 1.00 18.62 C ANISOU 3145 CB LEU B 76 2169 2755 2150 92 37 -89 C ATOM 3146 CG LEU B 76 -21.681 34.974 26.777 1.00 23.08 C ANISOU 3146 CG LEU B 76 2762 3281 2726 79 48 -78 C ATOM 3147 CD1 LEU B 76 -21.098 35.657 27.994 1.00 17.45 C ANISOU 3147 CD1 LEU B 76 2066 2524 2040 74 60 -57 C ATOM 3148 CD2 LEU B 76 -21.511 33.472 26.899 1.00 20.77 C ANISOU 3148 CD2 LEU B 76 2471 2981 2438 46 47 -108 C ATOM 3149 N LEU B 77 -26.298 35.832 27.232 1.00 21.18 N ANISOU 3149 N LEU B 77 2434 3137 2476 97 22 -121 N ATOM 3150 CA LEU B 77 -27.420 36.668 27.648 1.00 18.82 C ANISOU 3150 CA LEU B 77 2116 2853 2181 111 20 -116 C ATOM 3151 C LEU B 77 -28.021 36.161 28.951 1.00 22.62 C ANISOU 3151 C LEU B 77 2592 3314 2688 80 30 -135 C ATOM 3152 O LEU B 77 -28.375 36.956 29.830 1.00 22.33 O ANISOU 3152 O LEU B 77 2557 3264 2665 87 38 -121 O ATOM 3153 CB LEU B 77 -28.487 36.716 26.553 1.00 25.63 C ANISOU 3153 CB LEU B 77 2946 3773 3018 133 2 -131 C ATOM 3154 CG LEU B 77 -29.843 37.330 26.929 1.00 27.23 C ANISOU 3154 CG LEU B 77 3122 3999 3226 144 -2 -134 C ATOM 3155 CD1 LEU B 77 -29.714 38.804 27.277 1.00 23.72 C ANISOU 3155 CD1 LEU B 77 2688 3538 2787 174 9 -94 C ATOM 3156 CD2 LEU B 77 -30.850 37.132 25.810 1.00 30.53 C ANISOU 3156 CD2 LEU B 77 3505 4478 3619 162 -24 -155 C ATOM 3157 N ASN B 78 -28.147 34.838 29.090 1.00 20.50 N ANISOU 3157 N ASN B 78 2318 3044 2426 48 29 -166 N ATOM 3158 CA ASN B 78 -28.650 34.265 30.334 1.00 23.03 C ANISOU 3158 CA ASN B 78 2636 3344 2773 19 42 -180 C ATOM 3159 C ASN B 78 -27.741 34.620 31.504 1.00 22.40 C ANISOU 3159 C ASN B 78 2588 3217 2708 13 59 -157 C ATOM 3160 O ASN B 78 -28.221 35.000 32.579 1.00 22.53 O ANISOU 3160 O ASN B 78 2603 3220 2737 10 70 -152 O ATOM 3161 CB ASN B 78 -28.776 32.749 30.196 1.00 21.48 C ANISOU 3161 CB ASN B 78 2429 3147 2584 -14 43 -214 C ATOM 3162 CG ASN B 78 -29.479 32.110 31.374 1.00 23.96 C ANISOU 3162 CG ASN B 78 2735 3444 2925 -41 59 -228 C ATOM 3163 OD1 ASN B 78 -30.477 32.630 31.877 1.00 27.93 O ANISOU 3163 OD1 ASN B 78 3219 3958 3435 -35 62 -228 O ATOM 3164 ND2 ASN B 78 -28.965 30.968 31.818 1.00 25.93 N ANISOU 3164 ND2 ASN B 78 2996 3665 3190 -70 72 -239 N ATOM 3165 N LEU B 79 -26.421 34.522 31.307 1.00 21.53 N ANISOU 3165 N LEU B 79 2503 3083 2594 13 61 -143 N ATOM 3166 CA LEU B 79 -25.484 34.853 32.379 1.00 20.24 C ANISOU 3166 CA LEU B 79 2368 2877 2444 8 74 -124 C ATOM 3167 C LEU B 79 -25.576 36.327 32.765 1.00 20.86 C ANISOU 3167 C LEU B 79 2450 2950 2525 34 76 -101 C ATOM 3168 O LEU B 79 -25.478 36.671 33.949 1.00 22.65 O ANISOU 3168 O LEU B 79 2688 3152 2765 29 86 -96 O ATOM 3169 CB LEU B 79 -24.054 34.486 31.966 1.00 18.85 C ANISOU 3169 CB LEU B 79 2216 2680 2266 4 74 -114 C ATOM 3170 CG LEU B 79 -23.760 32.994 31.773 1.00 19.24 C ANISOU 3170 CG LEU B 79 2267 2725 2317 -23 76 -136 C ATOM 3171 CD1 LEU B 79 -22.279 32.744 31.550 1.00 23.55 C ANISOU 3171 CD1 LEU B 79 2838 3246 2864 -25 79 -123 C ATOM 3172 CD2 LEU B 79 -24.283 32.172 32.948 1.00 21.80 C ANISOU 3172 CD2 LEU B 79 2589 3034 2660 -49 89 -150 C ATOM 3173 N ALA B 80 -25.762 37.212 31.782 1.00 19.83 N ANISOU 3173 N ALA B 80 2310 2843 2382 62 67 -88 N ATOM 3174 CA ALA B 80 -25.944 38.631 32.081 1.00 19.94 C ANISOU 3174 CA ALA B 80 2324 2850 2402 88 72 -66 C ATOM 3175 C ALA B 80 -27.177 38.867 32.947 1.00 20.62 C ANISOU 3175 C ALA B 80 2393 2944 2496 86 76 -76 C ATOM 3176 O ALA B 80 -27.152 39.701 33.861 1.00 19.63 O ANISOU 3176 O ALA B 80 2277 2798 2384 93 85 -66 O ATOM 3177 CB ALA B 80 -26.045 39.437 30.784 1.00 22.59 C ANISOU 3177 CB ALA B 80 2650 3213 2722 122 64 -48 C ATOM 3178 N VAL B 81 -28.274 38.158 32.666 1.00 23.81 N ANISOU 3178 N VAL B 81 2772 3380 2894 77 70 -98 N ATOM 3179 CA VAL B 81 -29.487 38.319 33.468 1.00 20.00 C ANISOU 3179 CA VAL B 81 2271 2907 2421 74 76 -109 C ATOM 3180 C VAL B 81 -29.277 37.789 34.884 1.00 21.12 C ANISOU 3180 C VAL B 81 2429 3017 2579 49 91 -116 C ATOM 3181 O VAL B 81 -29.698 38.418 35.863 1.00 19.00 O ANISOU 3181 O VAL B 81 2162 2738 2320 54 101 -111 O ATOM 3182 CB VAL B 81 -30.678 37.634 32.777 1.00 22.33 C ANISOU 3182 CB VAL B 81 2531 3244 2709 69 65 -133 C ATOM 3183 CG1 VAL B 81 -31.848 37.528 33.730 1.00 19.54 C ANISOU 3183 CG1 VAL B 81 2160 2895 2371 58 75 -146 C ATOM 3184 CG2 VAL B 81 -31.079 38.406 31.517 1.00 18.50 C ANISOU 3184 CG2 VAL B 81 2028 2797 2204 103 49 -123 C ATOM 3185 N ALA B 82 -28.640 36.623 35.017 1.00 20.01 N ANISOU 3185 N ALA B 82 2300 2861 2441 22 94 -126 N ATOM 3186 CA ALA B 82 -28.369 36.081 36.345 1.00 25.49 C ANISOU 3186 CA ALA B 82 3010 3526 3147 2 110 -129 C ATOM 3187 C ALA B 82 -27.379 36.957 37.105 1.00 19.11 C ANISOU 3187 C ALA B 82 2231 2688 2342 13 115 -110 C ATOM 3188 O ALA B 82 -27.487 37.105 38.328 1.00 17.61 O ANISOU 3188 O ALA B 82 2050 2482 2158 10 126 -110 O ATOM 3189 CB ALA B 82 -27.854 34.644 36.238 1.00 19.04 C ANISOU 3189 CB ALA B 82 2201 2700 2334 -26 113 -142 C ATOM 3190 N ASP B 83 -26.412 37.549 36.395 1.00 17.87 N ANISOU 3190 N ASP B 83 2086 2522 2180 28 106 -95 N ATOM 3191 CA ASP B 83 -25.474 38.470 37.031 1.00 20.01 C ANISOU 3191 CA ASP B 83 2380 2765 2459 39 109 -80 C ATOM 3192 C ASP B 83 -26.194 39.681 37.616 1.00 21.22 C ANISOU 3192 C ASP B 83 2526 2918 2619 58 114 -76 C ATOM 3193 O ASP B 83 -25.809 40.188 38.673 1.00 20.69 O ANISOU 3193 O ASP B 83 2473 2827 2559 60 121 -74 O ATOM 3194 CB ASP B 83 -24.418 38.938 36.026 1.00 19.44 C ANISOU 3194 CB ASP B 83 2317 2684 2385 52 102 -64 C ATOM 3195 CG ASP B 83 -23.397 37.867 35.677 1.00 21.73 C ANISOU 3195 CG ASP B 83 2621 2964 2672 34 99 -67 C ATOM 3196 OD1 ASP B 83 -23.427 36.761 36.256 1.00 18.88 O ANISOU 3196 OD1 ASP B 83 2264 2598 2311 11 104 -80 O ATOM 3197 OD2 ASP B 83 -22.553 38.145 34.797 1.00 22.79 O ANISOU 3197 OD2 ASP B 83 2762 3094 2804 44 95 -54 O ATOM 3198 N LEU B 84 -27.216 40.188 36.921 1.00 18.28 N ANISOU 3198 N LEU B 84 2131 2574 2243 75 110 -74 N ATOM 3199 CA LEU B 84 -27.951 41.340 37.435 1.00 17.57 C ANISOU 3199 CA LEU B 84 2032 2483 2159 95 116 -69 C ATOM 3200 C LEU B 84 -28.734 40.986 38.691 1.00 20.69 C ANISOU 3200 C LEU B 84 2424 2878 2558 83 128 -84 C ATOM 3201 O LEU B 84 -28.865 41.820 39.595 1.00 18.26 O ANISOU 3201 O LEU B 84 2123 2557 2259 93 136 -82 O ATOM 3202 CB LEU B 84 -28.877 41.903 36.353 1.00 17.79 C ANISOU 3202 CB LEU B 84 2034 2544 2181 118 110 -62 C ATOM 3203 CG LEU B 84 -28.136 42.755 35.319 1.00 17.80 C ANISOU 3203 CG LEU B 84 2042 2541 2181 142 104 -39 C ATOM 3204 CD1 LEU B 84 -28.970 42.964 34.058 1.00 18.04 C ANISOU 3204 CD1 LEU B 84 2047 2612 2197 165 95 -32 C ATOM 3205 CD2 LEU B 84 -27.753 44.090 35.929 1.00 20.97 C ANISOU 3205 CD2 LEU B 84 2454 2911 2600 161 115 -24 C ATOM 3206 N PHE B 85 -29.248 39.758 38.769 1.00 23.67 N ANISOU 3206 N PHE B 85 2792 3270 2932 60 130 -98 N ATOM 3207 CA PHE B 85 -29.898 39.305 39.994 1.00 21.55 C ANISOU 3207 CA PHE B 85 2522 2999 2669 48 145 -109 C ATOM 3208 C PHE B 85 -28.908 39.219 41.153 1.00 18.54 C ANISOU 3208 C PHE B 85 2170 2586 2287 40 153 -107 C ATOM 3209 O PHE B 85 -29.263 39.526 42.297 1.00 22.82 O ANISOU 3209 O PHE B 85 2717 3122 2831 44 165 -110 O ATOM 3210 CB PHE B 85 -30.578 37.957 39.759 1.00 20.59 C ANISOU 3210 CB PHE B 85 2381 2894 2547 24 148 -124 C ATOM 3211 CG PHE B 85 -31.983 38.068 39.243 1.00 23.79 C ANISOU 3211 CG PHE B 85 2752 3333 2955 30 146 -133 C ATOM 3212 CD1 PHE B 85 -33.024 38.378 40.100 1.00 26.95 C ANISOU 3212 CD1 PHE B 85 3139 3739 3363 34 160 -137 C ATOM 3213 CD2 PHE B 85 -32.269 37.852 37.904 1.00 19.83 C ANISOU 3213 CD2 PHE B 85 2229 2858 2448 33 130 -139 C ATOM 3214 CE1 PHE B 85 -34.325 38.480 39.631 1.00 28.04 C ANISOU 3214 CE1 PHE B 85 3241 3908 3505 40 158 -146 C ATOM 3215 CE2 PHE B 85 -33.567 37.944 37.434 1.00 26.32 C ANISOU 3215 CE2 PHE B 85 3015 3713 3271 39 125 -150 C ATOM 3216 CZ PHE B 85 -34.595 38.261 38.301 1.00 25.02 C ANISOU 3216 CZ PHE B 85 2837 3554 3118 43 139 -153 C ATOM 3217 N MET B 86 -27.667 38.797 40.880 1.00 21.74 N ANISOU 3217 N MET B 86 2594 2974 2690 32 146 -102 N ATOM 3218 CA MET B 86 -26.638 38.779 41.920 1.00 19.44 C ANISOU 3218 CA MET B 86 2331 2657 2399 28 151 -100 C ATOM 3219 C MET B 86 -26.346 40.185 42.434 1.00 19.36 C ANISOU 3219 C MET B 86 2330 2632 2394 49 149 -97 C ATOM 3220 O MET B 86 -26.211 40.394 43.646 1.00 22.09 O ANISOU 3220 O MET B 86 2689 2968 2738 52 156 -102 O ATOM 3221 CB MET B 86 -25.347 38.137 41.398 1.00 19.24 C ANISOU 3221 CB MET B 86 2321 2617 2372 17 142 -95 C ATOM 3222 CG MET B 86 -25.443 36.661 41.011 1.00 21.29 C ANISOU 3222 CG MET B 86 2576 2884 2629 -6 146 -101 C ATOM 3223 SD MET B 86 -23.863 36.003 40.393 1.00 24.21 S ANISOU 3223 SD MET B 86 2966 3235 2998 -16 137 -95 S ATOM 3224 CE MET B 86 -22.882 35.996 41.887 1.00 21.16 C ANISOU 3224 CE MET B 86 2606 2823 2610 -17 143 -91 C ATOM 3225 N VAL B 87 -26.245 41.160 41.530 1.00 21.50 N ANISOU 3225 N VAL B 87 2594 2904 2672 66 141 -88 N ATOM 3226 CA VAL B 87 -25.840 42.507 41.927 1.00 18.99 C ANISOU 3226 CA VAL B 87 2283 2565 2365 86 141 -85 C ATOM 3227 C VAL B 87 -26.924 43.180 42.762 1.00 23.65 C ANISOU 3227 C VAL B 87 2865 3163 2958 98 152 -92 C ATOM 3228 O VAL B 87 -26.652 43.710 43.844 1.00 22.41 O ANISOU 3228 O VAL B 87 2720 2990 2804 104 156 -101 O ATOM 3229 CB VAL B 87 -25.485 43.345 40.687 1.00 19.52 C ANISOU 3229 CB VAL B 87 2345 2630 2443 102 134 -69 C ATOM 3230 CG1 VAL B 87 -25.562 44.838 41.007 1.00 22.33 C ANISOU 3230 CG1 VAL B 87 2699 2968 2815 125 140 -66 C ATOM 3231 CG2 VAL B 87 -24.095 42.975 40.185 1.00 18.72 C ANISOU 3231 CG2 VAL B 87 2259 2511 2344 93 127 -62 C ATOM 3232 N PHE B 88 -28.168 43.165 42.280 1.00 25.21 N ANISOU 3232 N PHE B 88 3039 3386 3153 104 155 -91 N ATOM 3233 CA PHE B 88 -29.230 43.903 42.958 1.00 20.04 C ANISOU 3233 CA PHE B 88 2373 2738 2502 118 166 -96 C ATOM 3234 C PHE B 88 -29.930 43.083 44.029 1.00 20.90 C ANISOU 3234 C PHE B 88 2481 2858 2602 105 178 -108 C ATOM 3235 O PHE B 88 -30.350 43.634 45.053 1.00 18.43 O ANISOU 3235 O PHE B 88 2171 2541 2290 116 190 -116 O ATOM 3236 CB PHE B 88 -30.253 44.406 41.941 1.00 23.43 C ANISOU 3236 CB PHE B 88 2776 3192 2936 135 164 -87 C ATOM 3237 CG PHE B 88 -29.718 45.470 41.040 1.00 25.04 C ANISOU 3237 CG PHE B 88 2980 3385 3150 156 157 -71 C ATOM 3238 CD1 PHE B 88 -29.375 46.707 41.553 1.00 22.62 C ANISOU 3238 CD1 PHE B 88 2684 3052 2860 174 164 -69 C ATOM 3239 CD2 PHE B 88 -29.550 45.235 39.685 1.00 22.65 C ANISOU 3239 CD2 PHE B 88 2668 3096 2841 159 146 -58 C ATOM 3240 CE1 PHE B 88 -28.876 47.698 40.734 1.00 30.21 C ANISOU 3240 CE1 PHE B 88 3645 3999 3836 193 162 -52 C ATOM 3241 CE2 PHE B 88 -29.057 46.227 38.853 1.00 20.28 C ANISOU 3241 CE2 PHE B 88 2369 2786 2551 182 144 -39 C ATOM 3242 CZ PHE B 88 -28.717 47.459 39.381 1.00 25.64 C ANISOU 3242 CZ PHE B 88 3057 3436 3250 198 153 -34 C ATOM 3243 N GLY B 89 -30.088 41.785 43.805 1.00 22.34 N ANISOU 3243 N GLY B 89 2659 3053 2777 84 179 -111 N ATOM 3244 CA GLY B 89 -30.716 40.938 44.793 1.00 20.63 C ANISOU 3244 CA GLY B 89 2440 2842 2554 71 196 -118 C ATOM 3245 C GLY B 89 -29.785 40.623 45.940 1.00 22.47 C ANISOU 3245 C GLY B 89 2702 3055 2778 66 201 -121 C ATOM 3246 O GLY B 89 -30.206 40.618 47.099 1.00 19.61 O ANISOU 3246 O GLY B 89 2346 2695 2411 70 216 -126 O ATOM 3247 N GLY B 90 -28.518 40.345 45.630 1.00 18.44 N ANISOU 3247 N GLY B 90 2210 2530 2267 58 189 -117 N ATOM 3248 CA GLY B 90 -27.580 39.931 46.656 1.00 23.61 C ANISOU 3248 CA GLY B 90 2890 3169 2911 53 192 -119 C ATOM 3249 C GLY B 90 -26.544 40.942 47.100 1.00 20.19 C ANISOU 3249 C GLY B 90 2476 2716 2480 67 181 -124 C ATOM 3250 O GLY B 90 -26.331 41.114 48.304 1.00 17.53 O ANISOU 3250 O GLY B 90 2154 2375 2133 74 186 -132 O ATOM 3251 N PHE B 91 -25.900 41.629 46.148 1.00 17.99 N ANISOU 3251 N PHE B 91 2195 2425 2214 72 167 -119 N ATOM 3252 CA PHE B 91 -24.742 42.457 46.483 1.00 18.51 C ANISOU 3252 CA PHE B 91 2277 2468 2287 81 157 -124 C ATOM 3253 C PHE B 91 -25.127 43.717 47.239 1.00 20.15 C ANISOU 3253 C PHE B 91 2485 2670 2502 101 161 -136 C ATOM 3254 O PHE B 91 -24.289 44.277 47.960 1.00 18.01 O ANISOU 3254 O PHE B 91 2228 2382 2234 107 155 -149 O ATOM 3255 CB PHE B 91 -23.957 42.837 45.223 1.00 19.43 C ANISOU 3255 CB PHE B 91 2390 2572 2419 81 145 -113 C ATOM 3256 CG PHE B 91 -23.150 41.709 44.633 1.00 19.38 C ANISOU 3256 CG PHE B 91 2392 2565 2408 63 138 -105 C ATOM 3257 CD1 PHE B 91 -23.290 40.414 45.096 1.00 18.20 C ANISOU 3257 CD1 PHE B 91 2248 2426 2243 48 144 -106 C ATOM 3258 CD2 PHE B 91 -22.240 41.956 43.616 1.00 22.62 C ANISOU 3258 CD2 PHE B 91 2803 2962 2830 64 128 -95 C ATOM 3259 CE1 PHE B 91 -22.547 39.388 44.558 1.00 20.88 C ANISOU 3259 CE1 PHE B 91 2593 2761 2580 32 140 -100 C ATOM 3260 CE2 PHE B 91 -21.492 40.934 43.071 1.00 20.89 C ANISOU 3260 CE2 PHE B 91 2590 2741 2606 48 124 -88 C ATOM 3261 CZ PHE B 91 -21.648 39.645 43.543 1.00 19.78 C ANISOU 3261 CZ PHE B 91 2454 2610 2450 32 129 -92 C ATOM 3262 N THR B 92 -26.368 44.178 47.085 1.00 22.71 N ANISOU 3262 N THR B 92 2792 3008 2830 111 171 -135 N ATOM 3263 CA THR B 92 -26.832 45.317 47.865 1.00 17.82 C ANISOU 3263 CA THR B 92 2172 2384 2216 130 178 -148 C ATOM 3264 C THR B 92 -26.859 45.003 49.355 1.00 22.11 C ANISOU 3264 C THR B 92 2730 2932 2740 131 186 -163 C ATOM 3265 O THR B 92 -26.587 45.886 50.178 1.00 20.53 O ANISOU 3265 O THR B 92 2539 2720 2543 145 185 -181 O ATOM 3266 CB THR B 92 -28.215 45.761 47.371 1.00 19.07 C ANISOU 3266 CB THR B 92 2306 2558 2380 142 188 -141 C ATOM 3267 OG1 THR B 92 -29.095 44.632 47.281 1.00 19.51 O ANISOU 3267 OG1 THR B 92 2351 2640 2423 128 196 -136 O ATOM 3268 CG2 THR B 92 -28.099 46.401 46.000 1.00 17.94 C ANISOU 3268 CG2 THR B 92 2150 2409 2256 149 180 -126 C ATOM 3269 N THR B 93 -27.175 43.757 49.727 1.00 17.89 N ANISOU 3269 N THR B 93 2198 2414 2186 118 194 -158 N ATOM 3270 CA THR B 93 -27.140 43.388 51.139 1.00 21.05 C ANISOU 3270 CA THR B 93 2614 2820 2564 122 203 -169 C ATOM 3271 C THR B 93 -25.705 43.237 51.636 1.00 17.93 C ANISOU 3271 C THR B 93 2240 2411 2160 120 189 -177 C ATOM 3272 O THR B 93 -25.392 43.646 52.758 1.00 22.57 O ANISOU 3272 O THR B 93 2841 2998 2735 133 188 -194 O ATOM 3273 CB THR B 93 -27.945 42.104 51.384 1.00 21.22 C ANISOU 3273 CB THR B 93 2631 2862 2572 111 221 -157 C ATOM 3274 OG1 THR B 93 -29.349 42.382 51.282 1.00 21.51 O ANISOU 3274 OG1 THR B 93 2646 2913 2614 117 236 -156 O ATOM 3275 CG2 THR B 93 -27.661 41.540 52.769 1.00 18.16 C ANISOU 3275 CG2 THR B 93 2262 2479 2157 116 231 -162 C ATOM 3276 N THR B 94 -24.812 42.673 50.814 1.00 18.71 N ANISOU 3276 N THR B 94 2342 2500 2266 105 176 -166 N ATOM 3277 CA THR B 94 -23.418 42.540 51.234 1.00 19.97 C ANISOU 3277 CA THR B 94 2519 2647 2421 104 162 -173 C ATOM 3278 C THR B 94 -22.813 43.898 51.565 1.00 21.86 C ANISOU 3278 C THR B 94 2762 2869 2674 118 149 -194 C ATOM 3279 O THR B 94 -22.128 44.054 52.581 1.00 20.70 O ANISOU 3279 O THR B 94 2629 2721 2516 126 142 -212 O ATOM 3280 CB THR B 94 -22.577 41.859 50.155 1.00 19.74 C ANISOU 3280 CB THR B 94 2490 2608 2401 86 151 -158 C ATOM 3281 OG1 THR B 94 -23.324 40.800 49.542 1.00 21.47 O ANISOU 3281 OG1 THR B 94 2700 2840 2616 72 162 -142 O ATOM 3282 CG2 THR B 94 -21.294 41.294 50.778 1.00 17.38 C ANISOU 3282 CG2 THR B 94 2210 2303 2091 83 140 -162 C ATOM 3283 N LEU B 95 -23.055 44.894 50.709 1.00 17.75 N ANISOU 3283 N LEU B 95 2228 2336 2181 123 148 -193 N ATOM 3284 CA LEU B 95 -22.483 46.218 50.927 1.00 19.65 C ANISOU 3284 CA LEU B 95 2469 2553 2443 135 139 -212 C ATOM 3285 C LEU B 95 -23.000 46.828 52.222 1.00 22.21 C ANISOU 3285 C LEU B 95 2798 2885 2755 152 146 -237 C ATOM 3286 O LEU B 95 -22.224 47.331 53.042 1.00 19.08 O ANISOU 3286 O LEU B 95 2412 2479 2359 159 135 -262 O ATOM 3287 CB LEU B 95 -22.799 47.118 49.731 1.00 19.31 C ANISOU 3287 CB LEU B 95 2410 2495 2432 139 142 -200 C ATOM 3288 CG LEU B 95 -22.552 48.623 49.846 1.00 22.43 C ANISOU 3288 CG LEU B 95 2800 2864 2857 154 141 -217 C ATOM 3289 CD1 LEU B 95 -21.077 48.949 49.941 1.00 21.38 C ANISOU 3289 CD1 LEU B 95 2675 2706 2743 149 126 -231 C ATOM 3290 CD2 LEU B 95 -23.186 49.329 48.659 1.00 18.06 C ANISOU 3290 CD2 LEU B 95 2229 2303 2328 162 150 -197 C ATOM 3291 N TYR B 96 -24.316 46.766 52.431 1.00 21.99 N ANISOU 3291 N TYR B 96 2763 2876 2717 159 163 -232 N ATOM 3292 CA TYR B 96 -24.914 47.332 53.633 1.00 18.49 C ANISOU 3292 CA TYR B 96 2324 2441 2260 177 172 -254 C ATOM 3293 C TYR B 96 -24.408 46.628 54.885 1.00 20.15 C ANISOU 3293 C TYR B 96 2554 2667 2436 179 169 -267 C ATOM 3294 O TYR B 96 -24.120 47.276 55.897 1.00 18.79 O ANISOU 3294 O TYR B 96 2391 2495 2255 194 164 -295 O ATOM 3295 CB TYR B 96 -26.433 47.230 53.543 1.00 18.57 C ANISOU 3295 CB TYR B 96 2320 2470 2264 182 193 -242 C ATOM 3296 CG TYR B 96 -27.168 48.064 54.553 1.00 21.22 C ANISOU 3296 CG TYR B 96 2656 2811 2594 203 206 -263 C ATOM 3297 CD1 TYR B 96 -27.459 49.392 54.293 1.00 26.50 C ANISOU 3297 CD1 TYR B 96 3316 3463 3292 217 208 -274 C ATOM 3298 CD2 TYR B 96 -27.577 47.525 55.766 1.00 29.51 C ANISOU 3298 CD2 TYR B 96 3718 3884 3610 211 218 -271 C ATOM 3299 CE1 TYR B 96 -28.138 50.160 55.209 1.00 31.83 C ANISOU 3299 CE1 TYR B 96 3991 4141 3962 236 220 -295 C ATOM 3300 CE2 TYR B 96 -28.253 48.286 56.691 1.00 24.09 C ANISOU 3300 CE2 TYR B 96 3032 3204 2917 232 230 -291 C ATOM 3301 CZ TYR B 96 -28.530 49.604 56.409 1.00 27.65 C ANISOU 3301 CZ TYR B 96 3473 3637 3397 244 230 -305 C ATOM 3302 OH TYR B 96 -29.208 50.379 57.321 1.00 36.27 O ANISOU 3302 OH TYR B 96 4565 4733 4482 265 244 -327 O ATOM 3303 N THR B 97 -24.301 45.298 54.828 1.00 18.43 N ANISOU 3303 N THR B 97 2342 2464 2197 166 172 -247 N ATOM 3304 CA THR B 97 -23.777 44.516 55.943 1.00 18.52 C ANISOU 3304 CA THR B 97 2371 2491 2174 171 171 -252 C ATOM 3305 C THR B 97 -22.326 44.880 56.236 1.00 18.53 C ANISOU 3305 C THR B 97 2383 2478 2178 173 146 -273 C ATOM 3306 O THR B 97 -21.913 44.950 57.400 1.00 18.74 O ANISOU 3306 O THR B 97 2423 2517 2180 188 140 -294 O ATOM 3307 CB THR B 97 -23.906 43.026 55.610 1.00 18.36 C ANISOU 3307 CB THR B 97 2353 2482 2141 155 181 -222 C ATOM 3308 OG1 THR B 97 -25.295 42.681 55.484 1.00 18.41 O ANISOU 3308 OG1 THR B 97 2347 2502 2146 153 205 -208 O ATOM 3309 CG2 THR B 97 -23.244 42.153 56.666 1.00 18.45 C ANISOU 3309 CG2 THR B 97 2384 2508 2118 161 180 -222 C ATOM 3310 N SER B 98 -21.535 45.108 55.185 1.00 18.33 N ANISOU 3310 N SER B 98 2351 2430 2184 159 131 -268 N ATOM 3311 CA SER B 98 -20.116 45.388 55.363 1.00 18.71 C ANISOU 3311 CA SER B 98 2405 2463 2239 158 108 -286 C ATOM 3312 C SER B 98 -19.879 46.798 55.898 1.00 18.58 C ANISOU 3312 C SER B 98 2386 2434 2241 173 99 -322 C ATOM 3313 O SER B 98 -18.855 47.048 56.542 1.00 23.33 O ANISOU 3313 O SER B 98 2994 3031 2840 177 80 -349 O ATOM 3314 CB SER B 98 -19.376 45.166 54.044 1.00 19.98 C ANISOU 3314 CB SER B 98 2560 2604 2430 140 99 -266 C ATOM 3315 OG SER B 98 -19.420 43.799 53.659 1.00 18.85 O ANISOU 3315 OG SER B 98 2420 2472 2269 126 106 -238 O ATOM 3316 N LEU B 99 -20.807 47.726 55.645 1.00 18.67 N ANISOU 3316 N LEU B 99 2387 2436 2272 180 112 -327 N ATOM 3317 CA LEU B 99 -20.680 49.081 56.182 1.00 18.94 C ANISOU 3317 CA LEU B 99 2417 2454 2326 194 106 -363 C ATOM 3318 C LEU B 99 -20.875 49.112 57.696 1.00 23.29 C ANISOU 3318 C LEU B 99 2981 3030 2840 213 106 -393 C ATOM 3319 O LEU B 99 -20.214 49.889 58.399 1.00 20.53 O ANISOU 3319 O LEU B 99 2633 2672 2496 222 91 -432 O ATOM 3320 CB LEU B 99 -21.687 50.018 55.513 1.00 21.40 C ANISOU 3320 CB LEU B 99 2714 2751 2668 199 123 -356 C ATOM 3321 CG LEU B 99 -21.504 50.384 54.035 1.00 20.91 C ANISOU 3321 CG LEU B 99 2637 2661 2646 188 124 -332 C ATOM 3322 CD1 LEU B 99 -22.740 51.104 53.540 1.00 18.86 C ANISOU 3322 CD1 LEU B 99 2365 2398 2403 198 143 -321 C ATOM 3323 CD2 LEU B 99 -20.267 51.243 53.828 1.00 18.86 C ANISOU 3323 CD2 LEU B 99 2374 2367 2425 185 109 -352 C ATOM 3324 N HIS B 100 -21.792 48.299 58.219 1.00 23.51 N ANISOU 3324 N HIS B 100 3016 3087 2829 219 123 -377 N ATOM 3325 CA HIS B 100 -22.075 48.316 59.650 1.00 22.00 C ANISOU 3325 CA HIS B 100 2837 2922 2598 241 126 -401 C ATOM 3326 C HIS B 100 -21.325 47.247 60.428 1.00 22.25 C ANISOU 3326 C HIS B 100 2885 2979 2588 245 116 -399 C ATOM 3327 O HIS B 100 -21.218 47.358 61.656 1.00 23.10 O ANISOU 3327 O HIS B 100 3005 3110 2662 266 112 -425 O ATOM 3328 CB HIS B 100 -23.580 48.154 59.905 1.00 20.17 C ANISOU 3328 CB HIS B 100 2604 2710 2350 251 155 -386 C ATOM 3329 CG HIS B 100 -24.411 49.260 59.338 1.00 22.93 C ANISOU 3329 CG HIS B 100 2937 3040 2735 254 166 -391 C ATOM 3330 ND1 HIS B 100 -24.652 49.392 57.987 1.00 26.18 N ANISOU 3330 ND1 HIS B 100 3332 3431 3182 238 170 -365 N ATOM 3331 CD2 HIS B 100 -25.054 50.290 59.938 1.00 20.07 C ANISOU 3331 CD2 HIS B 100 2572 2676 2377 273 176 -417 C ATOM 3332 CE1 HIS B 100 -25.407 50.457 57.779 1.00 24.24 C ANISOU 3332 CE1 HIS B 100 3076 3173 2963 248 181 -374 C ATOM 3333 NE2 HIS B 100 -25.667 51.017 58.947 1.00 26.34 N ANISOU 3333 NE2 HIS B 100 3349 3449 3212 269 185 -406 N ATOM 3334 N GLY B 101 -20.802 46.231 59.753 1.00 25.09 N ANISOU 3334 N GLY B 101 3246 3337 2949 227 112 -368 N ATOM 3335 CA GLY B 101 -20.064 45.176 60.409 1.00 23.99 C ANISOU 3335 CA GLY B 101 3123 3219 2774 231 104 -361 C ATOM 3336 C GLY B 101 -20.886 44.005 60.900 1.00 20.61 C ANISOU 3336 C GLY B 101 2704 2819 2307 237 129 -330 C ATOM 3337 O GLY B 101 -20.367 43.205 61.685 1.00 19.50 O ANISOU 3337 O GLY B 101 2578 2700 2130 248 126 -325 O ATOM 3338 N TYR B 102 -22.144 43.878 60.477 1.00 19.31 N ANISOU 3338 N TYR B 102 2532 2655 2151 231 155 -310 N ATOM 3339 CA TYR B 102 -22.970 42.724 60.830 1.00 21.89 C ANISOU 3339 CA TYR B 102 2864 3003 2451 233 183 -278 C ATOM 3340 C TYR B 102 -24.260 42.779 60.019 1.00 20.41 C ANISOU 3340 C TYR B 102 2659 2808 2288 221 206 -260 C ATOM 3341 O TYR B 102 -24.586 43.794 59.399 1.00 19.76 O ANISOU 3341 O TYR B 102 2563 2709 2236 217 201 -273 O ATOM 3342 CB TYR B 102 -23.269 42.661 62.338 1.00 21.31 C ANISOU 3342 CB TYR B 102 2806 2961 2331 263 195 -290 C ATOM 3343 CG TYR B 102 -24.260 43.686 62.860 1.00 22.77 C ANISOU 3343 CG TYR B 102 2986 3152 2513 280 208 -312 C ATOM 3344 CD1 TYR B 102 -23.927 45.029 62.940 1.00 25.15 C ANISOU 3344 CD1 TYR B 102 3283 3441 2832 288 188 -352 C ATOM 3345 CD2 TYR B 102 -25.518 43.297 63.307 1.00 22.94 C ANISOU 3345 CD2 TYR B 102 3007 3192 2518 290 241 -294 C ATOM 3346 CE1 TYR B 102 -24.829 45.960 63.428 1.00 29.71 C ANISOU 3346 CE1 TYR B 102 3857 4023 3409 305 200 -374 C ATOM 3347 CE2 TYR B 102 -26.423 44.219 63.789 1.00 24.61 C ANISOU 3347 CE2 TYR B 102 3214 3410 2728 307 254 -314 C ATOM 3348 CZ TYR B 102 -26.074 45.548 63.849 1.00 26.36 C ANISOU 3348 CZ TYR B 102 3432 3618 2965 315 233 -354 C ATOM 3349 OH TYR B 102 -26.975 46.468 64.336 1.00 28.93 O ANISOU 3349 OH TYR B 102 3754 3949 3290 333 247 -375 O ATOM 3350 N PHE B 103 -24.991 41.666 60.032 1.00 19.21 N ANISOU 3350 N PHE B 103 2507 2668 2125 214 232 -230 N ATOM 3351 CA PHE B 103 -26.245 41.558 59.286 1.00 21.96 C ANISOU 3351 CA PHE B 103 2835 3013 2496 202 253 -213 C ATOM 3352 C PHE B 103 -27.328 42.313 60.045 1.00 20.15 C ANISOU 3352 C PHE B 103 2603 2798 2257 222 271 -226 C ATOM 3353 O PHE B 103 -28.086 41.747 60.834 1.00 23.12 O ANISOU 3353 O PHE B 103 2982 3193 2610 233 298 -214 O ATOM 3354 CB PHE B 103 -26.618 40.098 59.056 1.00 19.40 C ANISOU 3354 CB PHE B 103 2508 2694 2168 186 274 -179 C ATOM 3355 CG PHE B 103 -25.969 39.497 57.841 1.00 22.34 C ANISOU 3355 CG PHE B 103 2874 3048 2564 160 260 -166 C ATOM 3356 CD1 PHE B 103 -26.557 39.624 56.590 1.00 19.30 C ANISOU 3356 CD1 PHE B 103 2468 2652 2212 142 260 -160 C ATOM 3357 CD2 PHE B 103 -24.763 38.823 57.942 1.00 21.44 C ANISOU 3357 CD2 PHE B 103 2776 2930 2439 157 247 -160 C ATOM 3358 CE1 PHE B 103 -25.955 39.087 55.467 1.00 19.96 C ANISOU 3358 CE1 PHE B 103 2547 2722 2315 120 247 -149 C ATOM 3359 CE2 PHE B 103 -24.158 38.279 56.826 1.00 20.36 C ANISOU 3359 CE2 PHE B 103 2634 2778 2326 134 235 -148 C ATOM 3360 CZ PHE B 103 -24.756 38.410 55.585 1.00 21.23 C ANISOU 3360 CZ PHE B 103 2723 2876 2466 116 236 -143 C ATOM 3361 N VAL B 104 -27.392 43.623 59.791 1.00 22.36 N ANISOU 3361 N VAL B 104 2874 3065 2557 229 258 -251 N ATOM 3362 CA VAL B 104 -28.408 44.472 60.407 1.00 22.04 C ANISOU 3362 CA VAL B 104 2828 3034 2512 249 274 -266 C ATOM 3363 C VAL B 104 -29.804 43.957 60.078 1.00 26.64 C ANISOU 3363 C VAL B 104 3394 3626 3104 242 304 -241 C ATOM 3364 O VAL B 104 -30.706 43.968 60.928 1.00 24.28 O ANISOU 3364 O VAL B 104 3094 3345 2785 259 329 -242 O ATOM 3365 CB VAL B 104 -28.224 45.930 59.946 1.00 29.21 C ANISOU 3365 CB VAL B 104 3727 3920 3450 253 257 -293 C ATOM 3366 CG1 VAL B 104 -29.349 46.808 60.470 1.00 26.71 C ANISOU 3366 CG1 VAL B 104 3403 3611 3134 273 276 -307 C ATOM 3367 CG2 VAL B 104 -26.880 46.462 60.389 1.00 25.28 C ANISOU 3367 CG2 VAL B 104 3244 3413 2948 260 229 -322 C ATOM 3368 N PHE B 105 -30.006 43.498 58.844 1.00 23.62 N ANISOU 3368 N PHE B 105 2994 3233 2749 218 302 -221 N ATOM 3369 CA PHE B 105 -31.295 42.963 58.430 1.00 23.40 C ANISOU 3369 CA PHE B 105 2944 3213 2732 209 327 -201 C ATOM 3370 C PHE B 105 -31.497 41.516 58.869 1.00 28.37 C ANISOU 3370 C PHE B 105 3580 3856 3345 200 350 -177 C ATOM 3371 O PHE B 105 -32.505 40.902 58.493 1.00 25.13 O ANISOU 3371 O PHE B 105 3149 3451 2948 188 371 -160 O ATOM 3372 CB PHE B 105 -31.452 43.081 56.910 1.00 27.32 C ANISOU 3372 CB PHE B 105 3418 3696 3264 189 314 -192 C ATOM 3373 CG PHE B 105 -32.882 43.087 56.450 1.00 31.64 C ANISOU 3373 CG PHE B 105 3938 4253 3829 186 333 -183 C ATOM 3374 CD1 PHE B 105 -33.898 43.445 57.322 1.00 29.84 C ANISOU 3374 CD1 PHE B 105 3705 4039 3592 204 357 -188 C ATOM 3375 CD2 PHE B 105 -33.214 42.717 55.155 1.00 26.13 C ANISOU 3375 CD2 PHE B 105 3218 3554 3157 166 327 -170 C ATOM 3376 CE1 PHE B 105 -35.222 43.448 56.905 1.00 37.65 C ANISOU 3376 CE1 PHE B 105 4667 5039 4600 202 375 -179 C ATOM 3377 CE2 PHE B 105 -34.533 42.717 54.733 1.00 30.89 C ANISOU 3377 CE2 PHE B 105 3792 4168 3775 165 342 -164 C ATOM 3378 CZ PHE B 105 -35.538 43.081 55.609 1.00 30.37 C ANISOU 3378 CZ PHE B 105 3721 4115 3703 182 366 -168 C ATOM 3379 N GLY B 106 -30.555 40.957 59.629 1.00 24.40 N ANISOU 3379 N GLY B 106 3101 3357 2814 206 346 -175 N ATOM 3380 CA GLY B 106 -30.737 39.682 60.281 1.00 21.35 C ANISOU 3380 CA GLY B 106 2722 2983 2407 206 372 -152 C ATOM 3381 C GLY B 106 -30.779 38.495 59.341 1.00 19.59 C ANISOU 3381 C GLY B 106 2488 2750 2207 176 378 -128 C ATOM 3382 O GLY B 106 -30.260 38.530 58.219 1.00 22.32 O ANISOU 3382 O GLY B 106 2825 3079 2575 157 355 -130 O ATOM 3383 N PRO B 107 -31.406 37.409 59.798 1.00 22.99 N ANISOU 3383 N PRO B 107 2916 3188 2632 173 412 -104 N ATOM 3384 CA PRO B 107 -31.439 36.177 58.989 1.00 19.56 C ANISOU 3384 CA PRO B 107 2469 2741 2221 145 421 -84 C ATOM 3385 C PRO B 107 -32.059 36.360 57.613 1.00 20.59 C ANISOU 3385 C PRO B 107 2570 2862 2390 121 411 -90 C ATOM 3386 O PRO B 107 -31.637 35.686 56.664 1.00 23.42 O ANISOU 3386 O PRO B 107 2922 3209 2768 98 400 -84 O ATOM 3387 CB PRO B 107 -32.266 35.213 59.856 1.00 20.48 C ANISOU 3387 CB PRO B 107 2585 2867 2329 150 466 -60 C ATOM 3388 CG PRO B 107 -32.134 35.738 61.257 1.00 23.30 C ANISOU 3388 CG PRO B 107 2966 3244 2645 184 474 -65 C ATOM 3389 CD PRO B 107 -31.998 37.225 61.139 1.00 20.17 C ANISOU 3389 CD PRO B 107 2569 2850 2246 197 445 -96 C ATOM 3390 N THR B 108 -33.049 37.247 57.473 1.00 20.86 N ANISOU 3390 N THR B 108 2585 2905 2435 128 414 -101 N ATOM 3391 CA THR B 108 -33.592 37.548 56.149 1.00 24.47 C ANISOU 3391 CA THR B 108 3014 3358 2926 111 400 -108 C ATOM 3392 C THR B 108 -32.521 38.114 55.226 1.00 22.14 C ANISOU 3392 C THR B 108 2726 3051 2637 105 362 -118 C ATOM 3393 O THR B 108 -32.450 37.753 54.043 1.00 21.66 O ANISOU 3393 O THR B 108 2650 2984 2597 85 350 -116 O ATOM 3394 CB THR B 108 -34.753 38.532 56.270 1.00 28.03 C ANISOU 3394 CB THR B 108 3445 3820 3383 125 409 -118 C ATOM 3395 OG1 THR B 108 -35.829 37.913 56.983 1.00 22.25 O ANISOU 3395 OG1 THR B 108 2702 3100 2652 127 447 -106 O ATOM 3396 CG2 THR B 108 -35.239 38.965 54.893 1.00 25.82 C ANISOU 3396 CG2 THR B 108 3137 3540 3134 113 391 -124 C ATOM 3397 N GLY B 109 -31.692 39.019 55.744 1.00 21.01 N ANISOU 3397 N GLY B 109 2603 2903 2475 124 345 -131 N ATOM 3398 CA GLY B 109 -30.624 39.578 54.938 1.00 19.20 C ANISOU 3398 CA GLY B 109 2381 2660 2256 120 312 -140 C ATOM 3399 C GLY B 109 -29.587 38.542 54.560 1.00 23.17 C ANISOU 3399 C GLY B 109 2895 3152 2756 102 303 -129 C ATOM 3400 O GLY B 109 -29.043 38.573 53.453 1.00 18.32 O ANISOU 3400 O GLY B 109 2276 2527 2159 89 282 -129 O ATOM 3401 N CYS B 110 -29.298 37.611 55.477 1.00 20.05 N ANISOU 3401 N CYS B 110 2517 2761 2341 104 319 -118 N ATOM 3402 CA CYS B 110 -28.397 36.503 55.176 1.00 18.51 C ANISOU 3402 CA CYS B 110 2332 2555 2144 88 315 -104 C ATOM 3403 C CYS B 110 -28.966 35.611 54.077 1.00 21.98 C ANISOU 3403 C CYS B 110 2750 2991 2612 62 323 -94 C ATOM 3404 O CYS B 110 -28.231 35.175 53.182 1.00 20.95 O ANISOU 3404 O CYS B 110 2619 2848 2492 46 307 -92 O ATOM 3405 CB CYS B 110 -28.132 35.702 56.456 1.00 21.24 C ANISOU 3405 CB CYS B 110 2699 2909 2463 100 336 -91 C ATOM 3406 SG CYS B 110 -27.031 34.260 56.324 1.00 21.66 S ANISOU 3406 SG CYS B 110 2766 2949 2512 86 336 -71 S ATOM 3407 N ASN B 111 -30.276 35.341 54.121 1.00 19.42 N ANISOU 3407 N ASN B 111 2404 2676 2299 57 348 -91 N ATOM 3408 CA ASN B 111 -30.911 34.531 53.084 1.00 20.56 C ANISOU 3408 CA ASN B 111 2524 2818 2471 32 354 -87 C ATOM 3409 C ASN B 111 -30.826 35.209 51.722 1.00 18.46 C ANISOU 3409 C ASN B 111 2242 2551 2222 24 325 -99 C ATOM 3410 O ASN B 111 -30.627 34.541 50.702 1.00 20.35 O ANISOU 3410 O ASN B 111 2472 2785 2477 4 317 -99 O ATOM 3411 CB ASN B 111 -32.373 34.249 53.440 1.00 18.85 C ANISOU 3411 CB ASN B 111 2284 2613 2266 29 386 -84 C ATOM 3412 CG ASN B 111 -32.525 33.216 54.541 1.00 23.98 C ANISOU 3412 CG ASN B 111 2944 3261 2907 31 421 -65 C ATOM 3413 OD1 ASN B 111 -31.599 32.469 54.846 1.00 22.99 O ANISOU 3413 OD1 ASN B 111 2840 3125 2771 28 424 -53 O ATOM 3414 ND2 ASN B 111 -33.710 33.162 55.137 1.00 24.89 N ANISOU 3414 ND2 ASN B 111 3044 3386 3027 36 452 -61 N ATOM 3415 N LEU B 112 -30.996 36.531 51.679 1.00 18.37 N ANISOU 3415 N LEU B 112 2227 2544 2207 42 311 -110 N ATOM 3416 CA LEU B 112 -30.862 37.238 50.405 1.00 20.69 C ANISOU 3416 CA LEU B 112 2508 2837 2515 40 286 -117 C ATOM 3417 C LEU B 112 -29.432 37.175 49.878 1.00 24.12 C ANISOU 3417 C LEU B 112 2961 3256 2947 35 263 -116 C ATOM 3418 O LEU B 112 -29.216 36.944 48.684 1.00 21.92 O ANISOU 3418 O LEU B 112 2672 2976 2680 22 249 -115 O ATOM 3419 CB LEU B 112 -31.313 38.692 50.559 1.00 24.19 C ANISOU 3419 CB LEU B 112 2947 3287 2959 62 280 -126 C ATOM 3420 CG LEU B 112 -32.813 38.980 50.657 1.00 18.91 C ANISOU 3420 CG LEU B 112 2251 2634 2298 68 297 -129 C ATOM 3421 CD1 LEU B 112 -33.048 40.324 51.325 1.00 26.10 C ANISOU 3421 CD1 LEU B 112 3167 3546 3203 94 297 -137 C ATOM 3422 CD2 LEU B 112 -33.463 38.951 49.278 1.00 24.12 C ANISOU 3422 CD2 LEU B 112 2881 3306 2978 58 286 -130 C ATOM 3423 N GLU B 113 -28.440 37.378 50.750 1.00 21.13 N ANISOU 3423 N GLU B 113 2609 2868 2551 45 258 -116 N ATOM 3424 CA GLU B 113 -27.051 37.396 50.294 1.00 17.70 C ANISOU 3424 CA GLU B 113 2191 2419 2117 42 236 -115 C ATOM 3425 C GLU B 113 -26.621 36.032 49.770 1.00 21.52 C ANISOU 3425 C GLU B 113 2675 2896 2604 20 239 -105 C ATOM 3426 O GLU B 113 -26.008 35.932 48.699 1.00 21.26 O ANISOU 3426 O GLU B 113 2640 2856 2582 10 223 -104 O ATOM 3427 CB GLU B 113 -26.139 37.853 51.434 1.00 26.36 C ANISOU 3427 CB GLU B 113 3312 3509 3194 58 230 -121 C ATOM 3428 CG GLU B 113 -24.921 38.634 50.991 1.00 21.75 C ANISOU 3428 CG GLU B 113 2737 2909 2617 62 204 -128 C ATOM 3429 CD GLU B 113 -23.726 37.752 50.675 1.00 23.65 C ANISOU 3429 CD GLU B 113 2991 3139 2857 50 195 -120 C ATOM 3430 OE1 GLU B 113 -23.687 36.599 51.152 1.00 26.28 O ANISOU 3430 OE1 GLU B 113 3331 3476 3178 42 209 -110 O ATOM 3431 OE2 GLU B 113 -22.819 38.222 49.955 1.00 26.04 O ANISOU 3431 OE2 GLU B 113 3295 3428 3171 48 176 -122 O ATOM 3432 N GLY B 114 -26.952 34.968 50.499 1.00 20.21 N ANISOU 3432 N GLY B 114 2514 2733 2432 14 262 -96 N ATOM 3433 CA GLY B 114 -26.592 33.620 50.099 1.00 18.89 C ANISOU 3433 CA GLY B 114 2348 2558 2273 -7 270 -86 C ATOM 3434 C GLY B 114 -27.365 33.047 48.927 1.00 18.24 C ANISOU 3434 C GLY B 114 2240 2479 2213 -27 273 -90 C ATOM 3435 O GLY B 114 -26.767 32.392 48.068 1.00 19.87 O ANISOU 3435 O GLY B 114 2445 2676 2427 -42 264 -89 O ATOM 3436 N PHE B 115 -28.683 33.272 48.871 1.00 17.86 N ANISOU 3436 N PHE B 115 2167 2444 2173 -28 285 -96 N ATOM 3437 CA PHE B 115 -29.500 32.652 47.826 1.00 19.67 C ANISOU 3437 CA PHE B 115 2368 2681 2425 -48 287 -103 C ATOM 3438 C PHE B 115 -29.090 33.132 46.439 1.00 20.06 C ANISOU 3438 C PHE B 115 2410 2734 2479 -50 258 -111 C ATOM 3439 O PHE B 115 -28.933 32.327 45.512 1.00 19.65 O ANISOU 3439 O PHE B 115 2349 2680 2438 -67 254 -116 O ATOM 3440 CB PHE B 115 -30.988 32.932 48.067 1.00 24.86 C ANISOU 3440 CB PHE B 115 3000 3356 3091 -45 303 -109 C ATOM 3441 CG PHE B 115 -31.885 32.502 46.927 1.00 23.84 C ANISOU 3441 CG PHE B 115 2836 3238 2984 -62 300 -122 C ATOM 3442 CD1 PHE B 115 -32.258 31.175 46.782 1.00 20.60 C ANISOU 3442 CD1 PHE B 115 2412 2822 2594 -87 319 -124 C ATOM 3443 CD2 PHE B 115 -32.358 33.428 46.006 1.00 22.13 C ANISOU 3443 CD2 PHE B 115 2600 3040 2770 -53 279 -132 C ATOM 3444 CE1 PHE B 115 -33.080 30.776 45.734 1.00 25.80 C ANISOU 3444 CE1 PHE B 115 3036 3494 3273 -103 314 -142 C ATOM 3445 CE2 PHE B 115 -33.183 33.035 44.958 1.00 18.37 C ANISOU 3445 CE2 PHE B 115 2090 2580 2311 -67 274 -146 C ATOM 3446 CZ PHE B 115 -33.543 31.708 44.826 1.00 18.52 C ANISOU 3446 CZ PHE B 115 2094 2594 2349 -93 290 -153 C ATOM 3447 N PHE B 116 -28.915 34.444 46.270 1.00 22.51 N ANISOU 3447 N PHE B 116 2723 3048 2781 -30 241 -113 N ATOM 3448 CA PHE B 116 -28.660 34.958 44.926 1.00 19.11 C ANISOU 3448 CA PHE B 116 2282 2623 2354 -28 217 -117 C ATOM 3449 C PHE B 116 -27.244 34.647 44.458 1.00 20.00 C ANISOU 3449 C PHE B 116 2416 2720 2464 -34 203 -112 C ATOM 3450 O PHE B 116 -27.003 34.558 43.248 1.00 17.71 O ANISOU 3450 O PHE B 116 2117 2434 2178 -38 189 -114 O ATOM 3451 CB PHE B 116 -28.943 36.459 44.869 1.00 19.79 C ANISOU 3451 CB PHE B 116 2365 2717 2439 -5 207 -118 C ATOM 3452 CG PHE B 116 -30.410 36.788 44.751 1.00 21.75 C ANISOU 3452 CG PHE B 116 2584 2987 2694 0 214 -124 C ATOM 3453 CD1 PHE B 116 -31.065 36.636 43.539 1.00 20.98 C ANISOU 3453 CD1 PHE B 116 2459 2908 2604 -4 205 -130 C ATOM 3454 CD2 PHE B 116 -31.131 37.236 45.845 1.00 23.75 C ANISOU 3454 CD2 PHE B 116 2836 3243 2945 12 231 -124 C ATOM 3455 CE1 PHE B 116 -32.411 36.927 43.420 1.00 29.74 C ANISOU 3455 CE1 PHE B 116 3540 4040 3721 1 210 -136 C ATOM 3456 CE2 PHE B 116 -32.481 37.532 45.734 1.00 27.64 C ANISOU 3456 CE2 PHE B 116 3300 3755 3446 17 239 -130 C ATOM 3457 CZ PHE B 116 -33.122 37.374 44.514 1.00 24.94 C ANISOU 3457 CZ PHE B 116 2930 3433 3114 11 228 -136 C ATOM 3458 N ALA B 117 -26.299 34.480 45.387 1.00 19.44 N ANISOU 3458 N ALA B 117 2370 2632 2384 -31 207 -105 N ATOM 3459 CA ALA B 117 -24.949 34.079 44.997 1.00 18.43 C ANISOU 3459 CA ALA B 117 2260 2487 2254 -37 196 -99 C ATOM 3460 C ALA B 117 -24.871 32.586 44.701 1.00 20.70 C ANISOU 3460 C ALA B 117 2546 2771 2549 -59 207 -98 C ATOM 3461 O ALA B 117 -24.122 32.168 43.810 1.00 24.70 O ANISOU 3461 O ALA B 117 3055 3270 3059 -68 196 -98 O ATOM 3462 CB ALA B 117 -23.948 34.465 46.088 1.00 23.47 C ANISOU 3462 CB ALA B 117 2924 3112 2881 -25 193 -94 C ATOM 3463 N THR B 118 -25.631 31.769 45.435 1.00 20.30 N ANISOU 3463 N THR B 118 2489 2721 2502 -68 230 -97 N ATOM 3464 CA THR B 118 -25.694 30.342 45.123 1.00 18.94 C ANISOU 3464 CA THR B 118 2312 2542 2343 -90 244 -98 C ATOM 3465 C THR B 118 -26.459 30.099 43.830 1.00 21.74 C ANISOU 3465 C THR B 118 2638 2910 2712 -104 238 -114 C ATOM 3466 O THR B 118 -26.077 29.241 43.025 1.00 19.60 O ANISOU 3466 O THR B 118 2364 2632 2449 -120 235 -120 O ATOM 3467 CB THR B 118 -26.349 29.579 46.276 1.00 21.67 C ANISOU 3467 CB THR B 118 2658 2884 2692 -95 276 -91 C ATOM 3468 OG1 THR B 118 -25.612 29.807 47.480 1.00 23.28 O ANISOU 3468 OG1 THR B 118 2888 3080 2877 -78 280 -76 O ATOM 3469 CG2 THR B 118 -26.380 28.088 45.984 1.00 23.35 C ANISOU 3469 CG2 THR B 118 2865 3083 2924 -118 294 -91 C ATOM 3470 N LEU B 119 -27.547 30.840 43.621 1.00 23.52 N ANISOU 3470 N LEU B 119 2842 3156 2939 -97 234 -123 N ATOM 3471 CA LEU B 119 -28.309 30.720 42.384 1.00 20.91 C ANISOU 3471 CA LEU B 119 2482 2843 2618 -106 224 -140 C ATOM 3472 C LEU B 119 -27.465 31.109 41.179 1.00 17.44 C ANISOU 3472 C LEU B 119 2047 2408 2171 -100 198 -141 C ATOM 3473 O LEU B 119 -27.367 30.354 40.205 1.00 22.09 O ANISOU 3473 O LEU B 119 2627 3001 2767 -114 192 -153 O ATOM 3474 CB LEU B 119 -29.562 31.591 42.461 1.00 22.90 C ANISOU 3474 CB LEU B 119 2711 3118 2872 -94 223 -146 C ATOM 3475 CG LEU B 119 -30.379 31.710 41.174 1.00 21.44 C ANISOU 3475 CG LEU B 119 2494 2960 2693 -96 208 -163 C ATOM 3476 CD1 LEU B 119 -31.038 30.381 40.838 1.00 23.44 C ANISOU 3476 CD1 LEU B 119 2724 3216 2967 -123 220 -181 C ATOM 3477 CD2 LEU B 119 -31.415 32.821 41.314 1.00 21.82 C ANISOU 3477 CD2 LEU B 119 2523 3029 2738 -77 205 -163 C ATOM 3478 N GLY B 120 -26.830 32.282 41.236 1.00 18.98 N ANISOU 3478 N GLY B 120 2258 2601 2353 -78 184 -130 N ATOM 3479 CA GLY B 120 -26.057 32.755 40.098 1.00 19.03 C ANISOU 3479 CA GLY B 120 2268 2610 2353 -70 164 -127 C ATOM 3480 C GLY B 120 -24.845 31.892 39.795 1.00 20.22 C ANISOU 3480 C GLY B 120 2437 2742 2504 -82 162 -124 C ATOM 3481 O GLY B 120 -24.478 31.712 38.631 1.00 19.82 O ANISOU 3481 O GLY B 120 2382 2698 2451 -84 150 -128 O ATOM 3482 N GLY B 121 -24.192 31.369 40.834 1.00 20.51 N ANISOU 3482 N GLY B 121 2495 2757 2542 -88 174 -116 N ATOM 3483 CA GLY B 121 -23.037 30.513 40.613 1.00 16.83 C ANISOU 3483 CA GLY B 121 2045 2272 2077 -98 175 -111 C ATOM 3484 C GLY B 121 -23.397 29.200 39.943 1.00 19.77 C ANISOU 3484 C GLY B 121 2404 2646 2461 -121 183 -125 C ATOM 3485 O GLY B 121 -22.677 28.726 39.058 1.00 20.63 O ANISOU 3485 O GLY B 121 2516 2750 2570 -126 175 -128 O ATOM 3486 N GLU B 122 -24.523 28.604 40.339 1.00 19.39 N ANISOU 3486 N GLU B 122 2339 2604 2425 -133 200 -135 N ATOM 3487 CA GLU B 122 -24.940 27.335 39.750 1.00 18.54 C ANISOU 3487 CA GLU B 122 2215 2495 2334 -156 209 -152 C ATOM 3488 C GLU B 122 -25.509 27.500 38.345 1.00 21.25 C ANISOU 3488 C GLU B 122 2533 2865 2676 -158 191 -174 C ATOM 3489 O GLU B 122 -25.420 26.566 37.540 1.00 21.80 O ANISOU 3489 O GLU B 122 2594 2934 2756 -174 190 -191 O ATOM 3490 CB GLU B 122 -25.954 26.640 40.660 1.00 17.53 C ANISOU 3490 CB GLU B 122 2074 2362 2224 -170 236 -155 C ATOM 3491 CG GLU B 122 -25.315 25.955 41.870 1.00 18.52 C ANISOU 3491 CG GLU B 122 2223 2460 2352 -173 260 -135 C ATOM 3492 CD GLU B 122 -24.440 24.768 41.484 1.00 21.97 C ANISOU 3492 CD GLU B 122 2671 2875 2800 -188 267 -135 C ATOM 3493 OE1 GLU B 122 -24.787 24.052 40.525 1.00 20.09 O ANISOU 3493 OE1 GLU B 122 2414 2639 2579 -206 266 -157 O ATOM 3494 OE2 GLU B 122 -23.401 24.546 42.139 1.00 22.14 O ANISOU 3494 OE2 GLU B 122 2719 2877 2814 -181 273 -115 O ATOM 3495 N ILE B 123 -26.089 28.659 38.024 1.00 17.42 N ANISOU 3495 N ILE B 123 2036 2404 2180 -140 175 -174 N ATOM 3496 CA ILE B 123 -26.486 28.919 36.642 1.00 17.52 C ANISOU 3496 CA ILE B 123 2027 2445 2185 -134 155 -190 C ATOM 3497 C ILE B 123 -25.258 28.926 35.742 1.00 18.23 C ANISOU 3497 C ILE B 123 2134 2530 2262 -127 141 -185 C ATOM 3498 O ILE B 123 -25.279 28.393 34.623 1.00 23.32 O ANISOU 3498 O ILE B 123 2767 3189 2904 -133 132 -203 O ATOM 3499 CB ILE B 123 -27.270 30.242 36.542 1.00 19.20 C ANISOU 3499 CB ILE B 123 2226 2684 2387 -111 143 -186 C ATOM 3500 CG1 ILE B 123 -28.653 30.101 37.186 1.00 20.50 C ANISOU 3500 CG1 ILE B 123 2365 2858 2564 -119 156 -197 C ATOM 3501 CG2 ILE B 123 -27.400 30.687 35.089 1.00 17.88 C ANISOU 3501 CG2 ILE B 123 2042 2546 2204 -97 120 -195 C ATOM 3502 CD1 ILE B 123 -29.431 31.399 37.258 1.00 24.74 C ANISOU 3502 CD1 ILE B 123 2890 3418 3093 -96 148 -190 C ATOM 3503 N ALA B 124 -24.165 29.526 36.222 1.00 17.13 N ANISOU 3503 N ALA B 124 2022 2371 2115 -115 141 -161 N ATOM 3504 CA ALA B 124 -22.924 29.547 35.458 1.00 16.98 C ANISOU 3504 CA ALA B 124 2020 2344 2088 -109 131 -153 C ATOM 3505 C ALA B 124 -22.345 28.147 35.288 1.00 17.04 C ANISOU 3505 C ALA B 124 2036 2334 2106 -130 140 -163 C ATOM 3506 O ALA B 124 -21.831 27.811 34.217 1.00 19.37 O ANISOU 3506 O ALA B 124 2330 2635 2395 -130 132 -170 O ATOM 3507 CB ALA B 124 -21.913 30.475 36.131 1.00 16.76 C ANISOU 3507 CB ALA B 124 2017 2296 2056 -93 129 -128 C ATOM 3508 N LEU B 125 -22.400 27.319 36.331 1.00 20.41 N ANISOU 3508 N LEU B 125 2468 2739 2547 -147 160 -162 N ATOM 3509 CA LEU B 125 -21.829 25.978 36.222 1.00 20.87 C ANISOU 3509 CA LEU B 125 2534 2777 2619 -166 172 -168 C ATOM 3510 C LEU B 125 -22.630 25.106 35.261 1.00 19.40 C ANISOU 3510 C LEU B 125 2322 2606 2443 -183 172 -200 C ATOM 3511 O LEU B 125 -22.057 24.401 34.421 1.00 22.84 O ANISOU 3511 O LEU B 125 2760 3038 2880 -191 169 -212 O ATOM 3512 CB LEU B 125 -21.746 25.320 37.599 1.00 20.68 C ANISOU 3512 CB LEU B 125 2523 2727 2609 -176 196 -156 C ATOM 3513 CG LEU B 125 -21.238 23.872 37.575 1.00 23.42 C ANISOU 3513 CG LEU B 125 2876 3049 2973 -196 213 -160 C ATOM 3514 CD1 LEU B 125 -19.901 23.761 36.854 1.00 21.10 C ANISOU 3514 CD1 LEU B 125 2600 2746 2672 -191 203 -155 C ATOM 3515 CD2 LEU B 125 -21.140 23.299 38.977 1.00 20.69 C ANISOU 3515 CD2 LEU B 125 2544 2680 2639 -201 239 -142 C ATOM 3516 N TRP B 126 -23.958 25.123 35.372 1.00 17.49 N ANISOU 3516 N TRP B 126 2054 2382 2210 -190 175 -216 N ATOM 3517 CA TRP B 126 -24.742 24.302 34.461 1.00 17.77 C ANISOU 3517 CA TRP B 126 2061 2433 2256 -207 172 -251 C ATOM 3518 C TRP B 126 -24.771 24.890 33.058 1.00 21.09 C ANISOU 3518 C TRP B 126 2470 2888 2654 -191 145 -265 C ATOM 3519 O TRP B 126 -24.983 24.147 32.093 1.00 21.80 O ANISOU 3519 O TRP B 126 2544 2992 2748 -202 139 -295 O ATOM 3520 CB TRP B 126 -26.156 24.102 35.018 1.00 18.01 C ANISOU 3520 CB TRP B 126 2064 2472 2307 -220 184 -266 C ATOM 3521 CG TRP B 126 -26.179 23.172 36.210 1.00 20.14 C ANISOU 3521 CG TRP B 126 2342 2707 2603 -239 217 -256 C ATOM 3522 CD1 TRP B 126 -26.270 23.524 37.532 1.00 18.15 C ANISOU 3522 CD1 TRP B 126 2103 2441 2352 -232 234 -230 C ATOM 3523 CD2 TRP B 126 -26.094 21.741 36.185 1.00 19.29 C ANISOU 3523 CD2 TRP B 126 2230 2574 2525 -265 238 -272 C ATOM 3524 NE1 TRP B 126 -26.256 22.401 38.322 1.00 18.10 N ANISOU 3524 NE1 TRP B 126 2102 2404 2372 -251 265 -226 N ATOM 3525 CE2 TRP B 126 -26.150 21.294 37.520 1.00 21.29 C ANISOU 3525 CE2 TRP B 126 2494 2798 2795 -272 269 -250 C ATOM 3526 CE3 TRP B 126 -25.989 20.794 35.160 1.00 23.74 C ANISOU 3526 CE3 TRP B 126 2781 3136 3102 -282 235 -303 C ATOM 3527 CZ2 TRP B 126 -26.100 19.942 37.856 1.00 22.50 C ANISOU 3527 CZ2 TRP B 126 2648 2920 2982 -294 299 -255 C ATOM 3528 CZ3 TRP B 126 -25.937 19.454 35.497 1.00 22.50 C ANISOU 3528 CZ3 TRP B 126 2623 2946 2980 -307 263 -311 C ATOM 3529 CH2 TRP B 126 -25.991 19.041 36.832 1.00 20.09 C ANISOU 3529 CH2 TRP B 126 2329 2610 2694 -313 296 -286 C ATOM 3530 N SER B 127 -24.520 26.194 32.914 1.00 20.06 N ANISOU 3530 N SER B 127 2348 2772 2500 -164 130 -244 N ATOM 3531 CA SER B 127 -24.369 26.755 31.573 1.00 21.01 C ANISOU 3531 CA SER B 127 2462 2924 2596 -145 107 -249 C ATOM 3532 C SER B 127 -23.119 26.213 30.887 1.00 20.14 C ANISOU 3532 C SER B 127 2372 2801 2480 -146 106 -248 C ATOM 3533 O SER B 127 -23.137 25.943 29.680 1.00 19.05 O ANISOU 3533 O SER B 127 2223 2686 2328 -142 93 -268 O ATOM 3534 CB SER B 127 -24.333 28.281 31.631 1.00 17.87 C ANISOU 3534 CB SER B 127 2071 2540 2180 -115 96 -222 C ATOM 3535 OG SER B 127 -25.587 28.796 32.055 1.00 19.22 O ANISOU 3535 OG SER B 127 2220 2729 2355 -111 95 -228 O ATOM 3536 N LEU B 128 -22.022 26.048 31.637 1.00 18.85 N ANISOU 3536 N LEU B 128 2237 2601 2324 -149 119 -225 N ATOM 3537 CA LEU B 128 -20.820 25.443 31.067 1.00 17.51 C ANISOU 3537 CA LEU B 128 2085 2416 2153 -152 120 -223 C ATOM 3538 C LEU B 128 -21.059 23.988 30.675 1.00 19.60 C ANISOU 3538 C LEU B 128 2338 2674 2433 -177 129 -255 C ATOM 3539 O LEU B 128 -20.444 23.495 29.724 1.00 19.31 O ANISOU 3539 O LEU B 128 2306 2641 2390 -177 124 -267 O ATOM 3540 CB LEU B 128 -19.652 25.539 32.056 1.00 18.85 C ANISOU 3540 CB LEU B 128 2283 2548 2329 -151 132 -192 C ATOM 3541 CG LEU B 128 -19.206 26.913 32.568 1.00 19.83 C ANISOU 3541 CG LEU B 128 2421 2669 2443 -128 125 -162 C ATOM 3542 CD1 LEU B 128 -18.156 26.754 33.673 1.00 25.19 C ANISOU 3542 CD1 LEU B 128 3125 3313 3133 -132 137 -140 C ATOM 3543 CD2 LEU B 128 -18.671 27.792 31.450 1.00 26.00 C ANISOU 3543 CD2 LEU B 128 3204 3468 3205 -105 110 -152 C ATOM 3544 N VAL B 129 -21.935 23.283 31.398 1.00 20.62 N ANISOU 3544 N VAL B 129 2453 2794 2587 -199 144 -270 N ATOM 3545 CA VAL B 129 -22.337 21.944 30.970 1.00 18.15 C ANISOU 3545 CA VAL B 129 2124 2476 2296 -224 153 -306 C ATOM 3546 C VAL B 129 -23.064 22.012 29.631 1.00 19.19 C ANISOU 3546 C VAL B 129 2229 2651 2413 -219 131 -342 C ATOM 3547 O VAL B 129 -22.815 21.204 28.727 1.00 21.82 O ANISOU 3547 O VAL B 129 2557 2988 2747 -228 128 -370 O ATOM 3548 CB VAL B 129 -23.200 21.274 32.058 1.00 19.72 C ANISOU 3548 CB VAL B 129 2310 2655 2527 -247 176 -312 C ATOM 3549 CG1 VAL B 129 -23.795 19.971 31.548 1.00 20.79 C ANISOU 3549 CG1 VAL B 129 2422 2787 2691 -275 186 -354 C ATOM 3550 CG2 VAL B 129 -22.372 21.021 33.297 1.00 17.84 C ANISOU 3550 CG2 VAL B 129 2101 2377 2301 -250 198 -278 C ATOM 3551 N VAL B 130 -23.961 22.989 29.474 1.00 19.22 N ANISOU 3551 N VAL B 130 2213 2689 2400 -204 114 -342 N ATOM 3552 CA VAL B 130 -24.694 23.133 28.218 1.00 19.86 C ANISOU 3552 CA VAL B 130 2266 2816 2462 -194 91 -375 C ATOM 3553 C VAL B 130 -23.740 23.431 27.068 1.00 21.47 C ANISOU 3553 C VAL B 130 2486 3038 2634 -172 76 -369 C ATOM 3554 O VAL B 130 -23.855 22.849 25.982 1.00 22.64 O ANISOU 3554 O VAL B 130 2620 3209 2773 -173 64 -404 O ATOM 3555 CB VAL B 130 -25.776 24.221 28.350 1.00 20.19 C ANISOU 3555 CB VAL B 130 2288 2891 2492 -177 78 -369 C ATOM 3556 CG1 VAL B 130 -26.427 24.501 27.000 1.00 20.94 C ANISOU 3556 CG1 VAL B 130 2356 3039 2560 -160 51 -397 C ATOM 3557 CG2 VAL B 130 -26.825 23.806 29.376 1.00 23.71 C ANISOU 3557 CG2 VAL B 130 2714 3323 2970 -201 94 -380 C ATOM 3558 N LEU B 131 -22.783 24.339 27.283 1.00 20.92 N ANISOU 3558 N LEU B 131 2444 2956 2549 -150 76 -328 N ATOM 3559 CA LEU B 131 -21.846 24.688 26.217 1.00 19.96 C ANISOU 3559 CA LEU B 131 2337 2849 2399 -127 66 -317 C ATOM 3560 C LEU B 131 -20.900 23.541 25.886 1.00 19.48 C ANISOU 3560 C LEU B 131 2291 2764 2348 -143 76 -331 C ATOM 3561 O LEU B 131 -20.477 23.405 24.733 1.00 23.42 O ANISOU 3561 O LEU B 131 2790 3283 2824 -130 66 -342 O ATOM 3562 CB LEU B 131 -21.049 25.934 26.603 1.00 20.17 C ANISOU 3562 CB LEU B 131 2388 2863 2414 -103 67 -270 C ATOM 3563 CG LEU B 131 -21.847 27.239 26.638 1.00 22.38 C ANISOU 3563 CG LEU B 131 2654 3170 2679 -79 55 -254 C ATOM 3564 CD1 LEU B 131 -21.035 28.338 27.284 1.00 23.17 C ANISOU 3564 CD1 LEU B 131 2778 3246 2780 -62 62 -210 C ATOM 3565 CD2 LEU B 131 -22.265 27.639 25.232 1.00 21.36 C ANISOU 3565 CD2 LEU B 131 2508 3091 2517 -53 36 -266 C ATOM 3566 N ALA B 132 -20.535 22.725 26.876 1.00 18.01 N ANISOU 3566 N ALA B 132 2116 2534 2192 -168 97 -327 N ATOM 3567 CA ALA B 132 -19.641 21.603 26.605 1.00 21.32 C ANISOU 3567 CA ALA B 132 2550 2928 2625 -182 110 -338 C ATOM 3568 C ALA B 132 -20.321 20.561 25.728 1.00 21.32 C ANISOU 3568 C ALA B 132 2525 2946 2630 -199 105 -391 C ATOM 3569 O ALA B 132 -19.701 20.007 24.812 1.00 24.52 O ANISOU 3569 O ALA B 132 2936 3355 3026 -196 103 -408 O ATOM 3570 CB ALA B 132 -19.166 20.980 27.921 1.00 21.20 C ANISOU 3570 CB ALA B 132 2551 2862 2641 -203 134 -320 C ATOM 3571 N ILE B 133 -21.596 20.281 25.998 1.00 21.08 N ANISOU 3571 N ILE B 133 2466 2927 2617 -216 104 -418 N ATOM 3572 CA ILE B 133 -22.372 19.389 25.140 1.00 20.23 C ANISOU 3572 CA ILE B 133 2329 2841 2517 -231 96 -474 C ATOM 3573 C ILE B 133 -22.529 19.993 23.751 1.00 26.10 C ANISOU 3573 C ILE B 133 3061 3640 3216 -203 67 -491 C ATOM 3574 O ILE B 133 -22.434 19.287 22.742 1.00 22.98 O ANISOU 3574 O ILE B 133 2656 3261 2813 -205 59 -529 O ATOM 3575 CB ILE B 133 -23.738 19.087 25.788 1.00 19.89 C ANISOU 3575 CB ILE B 133 2255 2799 2504 -254 102 -497 C ATOM 3576 CG1 ILE B 133 -23.550 18.303 27.094 1.00 20.49 C ANISOU 3576 CG1 ILE B 133 2342 2819 2624 -281 135 -482 C ATOM 3577 CG2 ILE B 133 -24.662 18.355 24.820 1.00 22.27 C ANISOU 3577 CG2 ILE B 133 2518 3130 2811 -267 88 -559 C ATOM 3578 CD1 ILE B 133 -24.806 18.185 27.922 1.00 22.29 C ANISOU 3578 CD1 ILE B 133 2544 3043 2882 -300 146 -492 C ATOM 3579 N GLU B 134 -22.782 21.304 23.675 1.00 28.70 N ANISOU 3579 N GLU B 134 3390 4000 3517 -174 51 -463 N ATOM 3580 CA GLU B 134 -22.950 21.950 22.373 1.00 23.21 C ANISOU 3580 CA GLU B 134 2684 3359 2776 -142 26 -472 C ATOM 3581 C GLU B 134 -21.674 21.859 21.544 1.00 27.38 C ANISOU 3581 C GLU B 134 3237 3885 3280 -124 27 -461 C ATOM 3582 O GLU B 134 -21.721 21.547 20.347 1.00 26.79 O ANISOU 3582 O GLU B 134 3152 3846 3179 -113 12 -493 O ATOM 3583 CB GLU B 134 -23.368 23.411 22.553 1.00 23.49 C ANISOU 3583 CB GLU B 134 2717 3419 2789 -112 14 -436 C ATOM 3584 CG GLU B 134 -23.722 24.138 21.252 1.00 26.57 C ANISOU 3584 CG GLU B 134 3093 3870 3132 -75 -12 -443 C ATOM 3585 CD GLU B 134 -22.603 25.030 20.720 1.00 25.21 C ANISOU 3585 CD GLU B 134 2950 3701 2929 -40 -11 -398 C ATOM 3586 OE1 GLU B 134 -21.534 25.107 21.360 1.00 24.66 O ANISOU 3586 OE1 GLU B 134 2910 3586 2875 -46 8 -365 O ATOM 3587 OE2 GLU B 134 -22.800 25.663 19.655 1.00 21.11 O ANISOU 3587 OE2 GLU B 134 2421 3230 2368 -6 -28 -397 O ATOM 3588 N ARG B 135 -20.520 22.134 22.166 1.00 21.91 N ANISOU 3588 N ARG B 135 2578 3152 2596 -122 44 -417 N ATOM 3589 CA ARG B 135 -19.245 22.024 21.461 1.00 26.44 C ANISOU 3589 CA ARG B 135 3175 3719 3152 -107 48 -403 C ATOM 3590 C ARG B 135 -18.984 20.594 21.004 1.00 29.10 C ANISOU 3590 C ARG B 135 3510 4043 3503 -130 56 -446 C ATOM 3591 O ARG B 135 -18.523 20.367 19.877 1.00 28.69 O ANISOU 3591 O ARG B 135 3461 4014 3425 -114 49 -462 O ATOM 3592 CB ARG B 135 -18.103 22.508 22.356 1.00 24.23 C ANISOU 3592 CB ARG B 135 2927 3395 2886 -104 66 -352 C ATOM 3593 CG ARG B 135 -18.054 24.011 22.594 1.00 22.37 C ANISOU 3593 CG ARG B 135 2697 3168 2633 -76 60 -308 C ATOM 3594 CD ARG B 135 -17.725 24.777 21.312 1.00 24.98 C ANISOU 3594 CD ARG B 135 3030 3538 2923 -39 48 -295 C ATOM 3595 NE ARG B 135 -18.924 25.080 20.539 1.00 23.87 N ANISOU 3595 NE ARG B 135 2862 3452 2755 -23 27 -320 N ATOM 3596 CZ ARG B 135 -18.923 25.524 19.289 1.00 25.33 C ANISOU 3596 CZ ARG B 135 3043 3683 2900 10 14 -321 C ATOM 3597 NH1 ARG B 135 -17.797 25.729 18.628 1.00 21.03 N ANISOU 3597 NH1 ARG B 135 2519 3134 2336 31 22 -297 N ATOM 3598 NH2 ARG B 135 -20.083 25.774 18.691 1.00 19.73 N ANISOU 3598 NH2 ARG B 135 2306 3024 2166 24 -6 -345 N ATOM 3599 N TYR B 136 -19.260 19.619 21.872 1.00 23.33 N ANISOU 3599 N TYR B 136 2774 3275 2815 -165 72 -464 N ATOM 3600 CA TYR B 136 -19.039 18.220 21.524 1.00 26.50 C ANISOU 3600 CA TYR B 136 3173 3658 3239 -189 83 -505 C ATOM 3601 C TYR B 136 -19.890 17.805 20.332 1.00 31.27 C ANISOU 3601 C TYR B 136 3747 4310 3824 -188 62 -564 C ATOM 3602 O TYR B 136 -19.404 17.127 19.418 1.00 29.32 O ANISOU 3602 O TYR B 136 3503 4071 3568 -185 61 -593 O ATOM 3603 CB TYR B 136 -19.331 17.332 22.737 1.00 27.74 C ANISOU 3603 CB TYR B 136 3327 3766 3447 -226 107 -510 C ATOM 3604 CG TYR B 136 -19.489 15.864 22.405 1.00 30.42 C ANISOU 3604 CG TYR B 136 3653 4088 3818 -255 118 -562 C ATOM 3605 CD1 TYR B 136 -18.432 15.132 21.878 1.00 37.71 C ANISOU 3605 CD1 TYR B 136 4595 4991 4742 -255 129 -569 C ATOM 3606 CD2 TYR B 136 -20.691 15.208 22.627 1.00 34.25 C ANISOU 3606 CD2 TYR B 136 4106 4573 4335 -282 121 -604 C ATOM 3607 CE1 TYR B 136 -18.571 13.789 21.573 1.00 34.67 C ANISOU 3607 CE1 TYR B 136 4197 4587 4388 -281 142 -617 C ATOM 3608 CE2 TYR B 136 -20.838 13.866 22.330 1.00 39.50 C ANISOU 3608 CE2 TYR B 136 4757 5217 5034 -310 134 -653 C ATOM 3609 CZ TYR B 136 -19.773 13.164 21.801 1.00 37.94 C ANISOU 3609 CZ TYR B 136 4580 5000 4836 -309 144 -660 C ATOM 3610 OH TYR B 136 -19.908 11.830 21.499 1.00 39.59 O ANISOU 3610 OH TYR B 136 4775 5186 5082 -336 158 -710 O ATOM 3611 N VAL B 137 -21.165 18.200 20.322 1.00 24.85 N ANISOU 3611 N VAL B 137 2904 3531 3007 -187 44 -584 N ATOM 3612 CA VAL B 137 -22.035 17.854 19.202 1.00 25.95 C ANISOU 3612 CA VAL B 137 3011 3722 3128 -184 21 -642 C ATOM 3613 C VAL B 137 -21.576 18.555 17.927 1.00 34.24 C ANISOU 3613 C VAL B 137 4069 4822 4119 -142 0 -636 C ATOM 3614 O VAL B 137 -21.536 17.948 16.851 1.00 25.58 O ANISOU 3614 O VAL B 137 2963 3754 3003 -136 -12 -680 O ATOM 3615 CB VAL B 137 -23.500 18.187 19.538 1.00 31.66 C ANISOU 3615 CB VAL B 137 3698 4472 3861 -192 7 -661 C ATOM 3616 CG1 VAL B 137 -24.378 18.004 18.317 1.00 37.07 C ANISOU 3616 CG1 VAL B 137 4347 5218 4519 -182 -23 -720 C ATOM 3617 CG2 VAL B 137 -23.994 17.317 20.682 1.00 32.55 C ANISOU 3617 CG2 VAL B 137 3800 4535 4034 -235 31 -674 C ATOM 3618 N VAL B 138 -21.213 19.836 18.029 1.00 29.45 N ANISOU 3618 N VAL B 138 3480 4227 3484 -110 -4 -580 N ATOM 3619 CA VAL B 138 -20.881 20.629 16.849 1.00 29.21 C ANISOU 3619 CA VAL B 138 3455 4246 3397 -66 -21 -567 C ATOM 3620 C VAL B 138 -19.563 20.172 16.228 1.00 32.61 C ANISOU 3620 C VAL B 138 3913 4662 3815 -57 -8 -561 C ATOM 3621 O VAL B 138 -19.449 20.047 15.001 1.00 33.44 O ANISOU 3621 O VAL B 138 4015 4811 3882 -33 -22 -585 O ATOM 3622 CB VAL B 138 -20.844 22.124 17.217 1.00 24.22 C ANISOU 3622 CB VAL B 138 2833 3622 2747 -36 -22 -506 C ATOM 3623 CG1 VAL B 138 -20.087 22.919 16.166 1.00 36.46 C ANISOU 3623 CG1 VAL B 138 4400 5204 4247 9 -28 -476 C ATOM 3624 CG2 VAL B 138 -22.253 22.667 17.385 1.00 26.91 C ANISOU 3624 CG2 VAL B 138 3142 3998 3083 -32 -41 -519 C ATOM 3625 N VAL B 139 -18.552 19.917 17.053 1.00 32.19 N ANISOU 3625 N VAL B 139 3887 4550 3793 -74 18 -528 N ATOM 3626 CA VAL B 139 -17.210 19.644 16.548 1.00 32.93 C ANISOU 3626 CA VAL B 139 4009 4627 3877 -62 31 -513 C ATOM 3627 C VAL B 139 -17.012 18.164 16.240 1.00 36.65 C ANISOU 3627 C VAL B 139 4477 5079 4369 -89 40 -565 C ATOM 3628 O VAL B 139 -16.437 17.814 15.208 1.00 34.94 O ANISOU 3628 O VAL B 139 4268 4882 4126 -73 38 -582 O ATOM 3629 CB VAL B 139 -16.161 20.154 17.555 1.00 29.66 C ANISOU 3629 CB VAL B 139 3625 4161 3485 -64 53 -452 C ATOM 3630 CG1 VAL B 139 -14.757 19.782 17.096 1.00 42.00 C ANISOU 3630 CG1 VAL B 139 5214 5702 5043 -55 69 -437 C ATOM 3631 CG2 VAL B 139 -16.281 21.658 17.722 1.00 26.76 C ANISOU 3631 CG2 VAL B 139 3260 3811 3096 -35 46 -404 C ATOM 3632 N CYS B 140 -17.468 17.279 17.124 1.00 35.47 N ANISOU 3632 N CYS B 140 4317 4892 4268 -129 52 -589 N ATOM 3633 CA CYS B 140 -17.292 15.846 16.928 1.00 29.49 C ANISOU 3633 CA CYS B 140 3556 4110 3541 -157 64 -637 C ATOM 3634 C CYS B 140 -18.399 15.213 16.101 1.00 37.58 C ANISOU 3634 C CYS B 140 4545 5175 4559 -166 44 -709 C ATOM 3635 O CYS B 140 -18.236 14.071 15.661 1.00 39.72 O ANISOU 3635 O CYS B 140 4812 5434 4847 -184 51 -756 O ATOM 3636 CB CYS B 140 -17.205 15.134 18.281 1.00 36.50 C ANISOU 3636 CB CYS B 140 4449 4931 4487 -195 91 -626 C ATOM 3637 SG CYS B 140 -15.727 15.551 19.225 1.00 36.00 S ANISOU 3637 SG CYS B 140 4428 4816 4436 -188 115 -552 S ATOM 3638 N LYS B 141 -19.511 15.918 15.896 1.00 38.16 N ANISOU 3638 N LYS B 141 4593 5297 4610 -154 19 -720 N ATOM 3639 CA LYS B 141 -20.668 15.472 15.125 1.00 37.79 C ANISOU 3639 CA LYS B 141 4507 5298 4555 -159 -6 -789 C ATOM 3640 C LYS B 141 -21.049 14.025 15.425 1.00 41.90 C ANISOU 3640 C LYS B 141 5009 5781 5132 -205 8 -847 C ATOM 3641 O LYS B 141 -21.133 13.204 14.501 1.00 40.77 O ANISOU 3641 O LYS B 141 4852 5657 4983 -209 0 -907 O ATOM 3642 CB LYS B 141 -20.402 15.658 13.631 1.00 37.18 C ANISOU 3642 CB LYS B 141 4430 5280 4417 -122 -28 -812 C ATOM 3643 CG LYS B 141 -20.311 17.121 13.228 1.00 36.22 C ANISOU 3643 CG LYS B 141 4318 5204 4239 -74 -43 -760 C ATOM 3644 CD LYS B 141 -19.521 17.309 11.951 1.00 36.72 C ANISOU 3644 CD LYS B 141 4398 5307 4247 -34 -50 -759 C ATOM 3645 CE LYS B 141 -19.079 18.756 11.796 1.00 45.93 C ANISOU 3645 CE LYS B 141 5584 6496 5372 11 -52 -689 C ATOM 3646 NZ LYS B 141 -18.225 19.200 12.938 1.00 38.18 N ANISOU 3646 NZ LYS B 141 4632 5451 4425 0 -24 -624 N ATOM 3647 N PRO B 142 -21.308 13.672 16.694 1.00 41.73 N ANISOU 3647 N PRO B 142 4986 5705 5165 -239 31 -831 N ATOM 3648 CA PRO B 142 -21.614 12.278 17.023 1.00 44.00 C ANISOU 3648 CA PRO B 142 5256 5950 5512 -283 51 -880 C ATOM 3649 C PRO B 142 -23.068 11.913 16.741 1.00 46.27 C ANISOU 3649 C PRO B 142 5495 6269 5817 -302 32 -946 C ATOM 3650 O PRO B 142 -23.338 11.235 15.751 1.00 50.20 O ANISOU 3650 O PRO B 142 5971 6793 6308 -306 17 -1012 O ATOM 3651 CB PRO B 142 -21.323 12.215 18.518 1.00 45.35 C ANISOU 3651 CB PRO B 142 5446 6055 5729 -304 84 -828 C ATOM 3652 CG PRO B 142 -21.720 13.562 18.998 1.00 41.03 C ANISOU 3652 CG PRO B 142 4900 5534 5155 -282 70 -781 C ATOM 3653 CD PRO B 142 -21.397 14.535 17.886 1.00 40.17 C ANISOU 3653 CD PRO B 142 4799 5484 4979 -239 41 -770 C ATOM 3654 N ARG B 147 -28.329 18.396 14.772 1.00 47.38 N ANISOU 3654 N ARG B 147 5505 6777 5720 -126 -150 -905 N ATOM 3655 CA ARG B 147 -27.566 19.615 15.005 1.00 46.10 C ANISOU 3655 CA ARG B 147 5380 6610 5525 -91 -141 -826 C ATOM 3656 C ARG B 147 -28.103 20.394 16.203 1.00 49.77 C ANISOU 3656 C ARG B 147 5843 7051 6016 -98 -130 -782 C ATOM 3657 O ARG B 147 -29.314 20.560 16.359 1.00 52.26 O ANISOU 3657 O ARG B 147 6121 7393 6342 -103 -145 -805 O ATOM 3658 CB ARG B 147 -27.585 20.500 13.756 1.00 54.62 C ANISOU 3658 CB ARG B 147 6458 7765 6533 -35 -171 -819 C ATOM 3659 N PHE B 148 -27.190 20.867 17.049 1.00 40.89 N ANISOU 3659 N PHE B 148 4758 5876 4903 -97 -104 -719 N ATOM 3660 CA PHE B 148 -27.554 21.718 18.177 1.00 44.04 C ANISOU 3660 CA PHE B 148 5160 6252 5321 -98 -93 -673 C ATOM 3661 C PHE B 148 -27.967 23.083 17.644 1.00 46.00 C ANISOU 3661 C PHE B 148 5401 6555 5520 -51 -115 -643 C ATOM 3662 O PHE B 148 -27.124 23.856 17.177 1.00 43.07 O ANISOU 3662 O PHE B 148 5058 6193 5113 -16 -115 -601 O ATOM 3663 CB PHE B 148 -26.379 21.837 19.143 1.00 37.32 C ANISOU 3663 CB PHE B 148 4353 5336 4491 -108 -62 -619 C ATOM 3664 CG PHE B 148 -26.774 22.177 20.555 1.00 39.29 C ANISOU 3664 CG PHE B 148 4603 5547 4777 -126 -44 -589 C ATOM 3665 CD1 PHE B 148 -27.107 23.474 20.907 1.00 34.26 C ANISOU 3665 CD1 PHE B 148 3969 4926 4124 -100 -49 -547 C ATOM 3666 CD2 PHE B 148 -26.783 21.200 21.538 1.00 35.54 C ANISOU 3666 CD2 PHE B 148 4130 5020 4354 -168 -19 -600 C ATOM 3667 CE1 PHE B 148 -27.453 23.787 22.210 1.00 33.07 C ANISOU 3667 CE1 PHE B 148 3821 4741 4005 -116 -32 -521 C ATOM 3668 CE2 PHE B 148 -27.129 21.508 22.841 1.00 41.21 C ANISOU 3668 CE2 PHE B 148 4852 5706 5103 -182 -1 -571 C ATOM 3669 CZ PHE B 148 -27.466 22.802 23.177 1.00 37.26 C ANISOU 3669 CZ PHE B 148 4353 5223 4583 -156 -8 -533 C ATOM 3670 N GLY B 149 -29.267 23.378 17.696 1.00 45.31 N ANISOU 3670 N GLY B 149 5276 6503 5436 -49 -132 -664 N ATOM 3671 CA GLY B 149 -29.808 24.597 17.160 1.00 40.45 C ANISOU 3671 CA GLY B 149 4649 5944 4778 -4 -154 -641 C ATOM 3672 C GLY B 149 -30.370 25.522 18.220 1.00 36.29 C ANISOU 3672 C GLY B 149 4119 5399 4270 -2 -144 -600 C ATOM 3673 O GLY B 149 -30.046 25.430 19.412 1.00 41.16 O ANISOU 3673 O GLY B 149 4755 5957 4926 -29 -118 -575 O ATOM 3674 N GLU B 150 -31.234 26.434 17.773 1.00 39.37 N ANISOU 3674 N GLU B 150 4485 5844 4631 32 -166 -594 N ATOM 3675 CA GLU B 150 -31.794 27.453 18.654 1.00 38.27 C ANISOU 3675 CA GLU B 150 4342 5694 4504 42 -158 -554 C ATOM 3676 C GLU B 150 -32.641 26.834 19.758 1.00 33.74 C ANISOU 3676 C GLU B 150 3746 5089 3985 -3 -146 -580 C ATOM 3677 O GLU B 150 -32.568 27.260 20.917 1.00 36.21 O ANISOU 3677 O GLU B 150 4074 5358 4325 -14 -124 -544 O ATOM 3678 CB GLU B 150 -32.620 28.437 17.828 1.00 42.60 C ANISOU 3678 CB GLU B 150 4864 6312 5010 89 -186 -548 C ATOM 3679 CG GLU B 150 -32.893 29.760 18.498 1.00 42.88 C ANISOU 3679 CG GLU B 150 4907 6339 5047 113 -176 -493 C ATOM 3680 CD GLU B 150 -32.869 30.906 17.509 1.00 40.80 C ANISOU 3680 CD GLU B 150 4645 6128 4730 173 -192 -459 C ATOM 3681 OE1 GLU B 150 -32.595 30.658 16.316 1.00 46.66 O ANISOU 3681 OE1 GLU B 150 5384 6913 5430 196 -210 -476 O ATOM 3682 OE2 GLU B 150 -33.118 32.057 17.925 1.00 47.03 O ANISOU 3682 OE2 GLU B 150 5437 6913 5518 197 -185 -414 O ATOM 3683 N ASN B 151 -33.457 25.832 19.417 1.00 40.10 N ANISOU 3683 N ASN B 151 4513 5917 4808 -28 -160 -643 N ATOM 3684 CA ASN B 151 -34.330 25.210 20.410 1.00 38.77 C ANISOU 3684 CA ASN B 151 4318 5720 4694 -70 -146 -668 C ATOM 3685 C ASN B 151 -33.525 24.566 21.532 1.00 35.40 C ANISOU 3685 C ASN B 151 3923 5216 4309 -107 -110 -649 C ATOM 3686 O ASN B 151 -33.876 24.696 22.711 1.00 31.53 O ANISOU 3686 O ASN B 151 3435 4691 3854 -126 -88 -629 O ATOM 3687 CB ASN B 151 -35.232 24.166 19.747 1.00 35.22 C ANISOU 3687 CB ASN B 151 3820 5304 4258 -92 -167 -744 C ATOM 3688 CG ASN B 151 -36.286 24.780 18.842 1.00 30.83 C ANISOU 3688 CG ASN B 151 3222 4826 3666 -57 -204 -767 C ATOM 3689 OD1 ASN B 151 -36.710 25.923 19.030 1.00 33.41 O ANISOU 3689 OD1 ASN B 151 3546 5175 3975 -26 -209 -728 O ATOM 3690 ND2 ASN B 151 -36.732 24.009 17.863 1.00 31.44 N ANISOU 3690 ND2 ASN B 151 3264 4947 3734 -62 -230 -832 N ATOM 3691 N HIS B 152 -32.447 23.859 21.184 1.00 31.44 N ANISOU 3691 N HIS B 152 3450 4691 3805 -117 -102 -656 N ATOM 3692 CA HIS B 152 -31.641 23.193 22.202 1.00 37.52 C ANISOU 3692 CA HIS B 152 4250 5391 4614 -150 -68 -637 C ATOM 3693 C HIS B 152 -30.971 24.204 23.122 1.00 34.27 C ANISOU 3693 C HIS B 152 3877 4946 4197 -134 -50 -570 C ATOM 3694 O HIS B 152 -30.855 23.973 24.332 1.00 35.32 O ANISOU 3694 O HIS B 152 4024 5031 4367 -158 -23 -551 O ATOM 3695 CB HIS B 152 -30.591 22.297 21.547 1.00 40.97 C ANISOU 3695 CB HIS B 152 4708 5813 5045 -159 -65 -656 C ATOM 3696 CG HIS B 152 -31.141 21.397 20.487 1.00 40.62 C ANISOU 3696 CG HIS B 152 4628 5806 4998 -169 -86 -725 C ATOM 3697 ND1 HIS B 152 -31.276 21.791 19.173 1.00 38.14 N ANISOU 3697 ND1 HIS B 152 4302 5557 4634 -134 -119 -745 N ATOM 3698 CD2 HIS B 152 -31.588 20.121 20.545 1.00 40.63 C ANISOU 3698 CD2 HIS B 152 4605 5790 5044 -209 -79 -780 C ATOM 3699 CE1 HIS B 152 -31.783 20.797 18.468 1.00 47.01 C ANISOU 3699 CE1 HIS B 152 5392 6702 5766 -153 -134 -813 C ATOM 3700 NE2 HIS B 152 -31.980 19.771 19.276 1.00 47.69 N ANISOU 3700 NE2 HIS B 152 5470 6738 5912 -200 -109 -836 N ATOM 3701 N ALA B 153 -30.505 25.323 22.563 1.00 32.29 N ANISOU 3701 N ALA B 153 3644 4722 3903 -93 -63 -535 N ATOM 3702 CA ALA B 153 -29.889 26.358 23.385 1.00 30.93 C ANISOU 3702 CA ALA B 153 3504 4519 3728 -77 -48 -475 C ATOM 3703 C ALA B 153 -30.890 26.937 24.375 1.00 29.09 C ANISOU 3703 C ALA B 153 3254 4282 3515 -80 -41 -463 C ATOM 3704 O ALA B 153 -30.585 27.094 25.561 1.00 31.53 O ANISOU 3704 O ALA B 153 3584 4547 3849 -93 -18 -434 O ATOM 3705 CB ALA B 153 -29.309 27.458 22.495 1.00 27.96 C ANISOU 3705 CB ALA B 153 3145 4175 3305 -31 -62 -441 C ATOM 3706 N ILE B 154 -32.104 27.240 23.911 1.00 31.83 N ANISOU 3706 N ILE B 154 3562 4678 3854 -68 -61 -486 N ATOM 3707 CA ILE B 154 -33.108 27.810 24.805 1.00 28.11 C ANISOU 3707 CA ILE B 154 3072 4206 3402 -70 -54 -475 C ATOM 3708 C ILE B 154 -33.574 26.772 25.821 1.00 31.65 C ANISOU 3708 C ILE B 154 3508 4616 3901 -115 -32 -499 C ATOM 3709 O ILE B 154 -33.795 27.089 26.998 1.00 27.83 O ANISOU 3709 O ILE B 154 3032 4103 3440 -123 -11 -474 O ATOM 3710 CB ILE B 154 -34.281 28.387 23.993 1.00 30.17 C ANISOU 3710 CB ILE B 154 3291 4531 3640 -43 -83 -494 C ATOM 3711 CG1 ILE B 154 -33.788 29.522 23.094 1.00 33.15 C ANISOU 3711 CG1 ILE B 154 3684 4942 3968 7 -99 -460 C ATOM 3712 CG2 ILE B 154 -35.382 28.885 24.921 1.00 37.11 C ANISOU 3712 CG2 ILE B 154 4148 5410 4544 -46 -74 -487 C ATOM 3713 CD1 ILE B 154 -34.893 30.244 22.360 1.00 34.46 C ANISOU 3713 CD1 ILE B 154 3813 5173 4108 41 -126 -469 C ATOM 3714 N MET B 155 -33.737 25.519 25.387 1.00 28.06 N ANISOU 3714 N MET B 155 3034 4163 3465 -144 -34 -547 N ATOM 3715 CA MET B 155 -34.030 24.452 26.339 1.00 29.74 C ANISOU 3715 CA MET B 155 3239 4332 3730 -187 -7 -565 C ATOM 3716 C MET B 155 -32.929 24.344 27.384 1.00 28.80 C ANISOU 3716 C MET B 155 3166 4153 3624 -198 24 -524 C ATOM 3717 O MET B 155 -33.204 24.112 28.568 1.00 24.34 O ANISOU 3717 O MET B 155 2603 3552 3091 -217 50 -511 O ATOM 3718 CB MET B 155 -34.210 23.124 25.606 1.00 33.68 C ANISOU 3718 CB MET B 155 3713 4837 4248 -215 -12 -624 C ATOM 3719 CG MET B 155 -34.166 21.905 26.512 1.00 37.15 C ANISOU 3719 CG MET B 155 4154 5221 4742 -259 22 -637 C ATOM 3720 SD MET B 155 -35.169 20.544 25.884 1.00 54.28 S ANISOU 3720 SD MET B 155 6268 7403 6952 -296 16 -716 S ATOM 3721 CE MET B 155 -34.703 20.574 24.153 1.00 35.50 C ANISOU 3721 CE MET B 155 3886 5078 4522 -270 -25 -750 C ATOM 3722 N GLY B 156 -31.675 24.513 26.964 1.00 24.65 N ANISOU 3722 N GLY B 156 2677 3618 3072 -183 20 -502 N ATOM 3723 CA GLY B 156 -30.581 24.529 27.914 1.00 25.13 C ANISOU 3723 CA GLY B 156 2779 3627 3141 -188 45 -461 C ATOM 3724 C GLY B 156 -30.656 25.685 28.888 1.00 24.25 C ANISOU 3724 C GLY B 156 2684 3506 3025 -170 53 -417 C ATOM 3725 O GLY B 156 -30.248 25.550 30.044 1.00 21.53 O ANISOU 3725 O GLY B 156 2361 3119 2699 -182 78 -393 O ATOM 3726 N VAL B 157 -31.169 26.836 28.444 1.00 19.71 N ANISOU 3726 N VAL B 157 2097 2970 2423 -139 33 -406 N ATOM 3727 CA VAL B 157 -31.266 27.989 29.338 1.00 23.46 C ANISOU 3727 CA VAL B 157 2584 3435 2894 -120 41 -367 C ATOM 3728 C VAL B 157 -32.243 27.702 30.474 1.00 23.94 C ANISOU 3728 C VAL B 157 2627 3481 2989 -142 61 -374 C ATOM 3729 O VAL B 157 -31.935 27.932 31.648 1.00 20.11 O ANISOU 3729 O VAL B 157 2165 2962 2516 -146 82 -346 O ATOM 3730 CB VAL B 157 -31.668 29.254 28.560 1.00 24.99 C ANISOU 3730 CB VAL B 157 2766 3673 3055 -81 18 -355 C ATOM 3731 CG1 VAL B 157 -32.239 30.301 29.518 1.00 23.83 C ANISOU 3731 CG1 VAL B 157 2619 3522 2915 -68 27 -327 C ATOM 3732 CG2 VAL B 157 -30.475 29.823 27.810 1.00 26.00 C ANISOU 3732 CG2 VAL B 157 2923 3803 3153 -55 9 -329 C ATOM 3733 N ALA B 158 -33.436 27.198 30.142 1.00 21.91 N ANISOU 3733 N ALA B 158 2327 3250 2747 -155 54 -411 N ATOM 3734 CA ALA B 158 -34.393 26.822 31.177 1.00 21.79 C ANISOU 3734 CA ALA B 158 2293 3220 2768 -177 77 -419 C ATOM 3735 C ALA B 158 -33.847 25.710 32.059 1.00 21.08 C ANISOU 3735 C ALA B 158 2222 3079 2710 -210 108 -417 C ATOM 3736 O ALA B 158 -34.132 25.670 33.259 1.00 21.98 O ANISOU 3736 O ALA B 158 2340 3166 2844 -219 134 -399 O ATOM 3737 CB ALA B 158 -35.715 26.392 30.543 1.00 31.03 C ANISOU 3737 CB ALA B 158 3410 4428 3953 -188 63 -464 C ATOM 3738 N PHE B 159 -33.060 24.805 31.481 1.00 23.21 N ANISOU 3738 N PHE B 159 2502 3335 2981 -224 106 -433 N ATOM 3739 CA PHE B 159 -32.458 23.729 32.260 1.00 22.98 C ANISOU 3739 CA PHE B 159 2492 3256 2981 -252 137 -428 C ATOM 3740 C PHE B 159 -31.540 24.275 33.349 1.00 20.25 C ANISOU 3740 C PHE B 159 2191 2878 2626 -240 154 -380 C ATOM 3741 O PHE B 159 -31.507 23.737 34.460 1.00 19.20 O ANISOU 3741 O PHE B 159 2068 2709 2517 -256 183 -366 O ATOM 3742 CB PHE B 159 -31.712 22.784 31.314 1.00 23.86 C ANISOU 3742 CB PHE B 159 2610 3362 3093 -265 130 -454 C ATOM 3743 CG PHE B 159 -30.810 21.799 32.002 1.00 20.79 C ANISOU 3743 CG PHE B 159 2249 2922 2728 -286 159 -441 C ATOM 3744 CD1 PHE B 159 -31.324 20.648 32.578 1.00 26.10 C ANISOU 3744 CD1 PHE B 159 2905 3565 3447 -318 188 -459 C ATOM 3745 CD2 PHE B 159 -29.440 22.002 32.029 1.00 21.96 C ANISOU 3745 CD2 PHE B 159 2438 3051 2854 -273 158 -411 C ATOM 3746 CE1 PHE B 159 -30.495 19.735 33.194 1.00 23.21 C ANISOU 3746 CE1 PHE B 159 2565 3152 3102 -335 216 -444 C ATOM 3747 CE2 PHE B 159 -28.603 21.087 32.646 1.00 27.31 C ANISOU 3747 CE2 PHE B 159 3141 3684 3553 -290 184 -399 C ATOM 3748 CZ PHE B 159 -29.134 19.955 33.228 1.00 23.98 C ANISOU 3748 CZ PHE B 159 2703 3233 3174 -320 213 -414 C ATOM 3749 N THR B 160 -30.792 25.349 33.061 1.00 18.96 N ANISOU 3749 N THR B 160 2051 2725 2427 -210 136 -353 N ATOM 3750 CA THR B 160 -29.861 25.863 34.066 1.00 22.00 C ANISOU 3750 CA THR B 160 2475 3079 2804 -200 149 -312 C ATOM 3751 C THR B 160 -30.597 26.421 35.283 1.00 22.93 C ANISOU 3751 C THR B 160 2590 3192 2931 -195 165 -295 C ATOM 3752 O THR B 160 -30.129 26.261 36.417 1.00 23.89 O ANISOU 3752 O THR B 160 2736 3282 3060 -200 187 -272 O ATOM 3753 CB THR B 160 -28.931 26.927 33.468 1.00 23.12 C ANISOU 3753 CB THR B 160 2640 3233 2912 -170 127 -290 C ATOM 3754 OG1 THR B 160 -29.679 28.090 33.083 1.00 22.46 O ANISOU 3754 OG1 THR B 160 2539 3184 2811 -145 110 -287 O ATOM 3755 CG2 THR B 160 -28.185 26.372 32.264 1.00 19.69 C ANISOU 3755 CG2 THR B 160 2211 2805 2467 -172 114 -306 C ATOM 3756 N TRP B 161 -31.749 27.074 35.074 1.00 19.15 N ANISOU 3756 N TRP B 161 2081 2745 2450 -185 155 -306 N ATOM 3757 CA TRP B 161 -32.506 27.632 36.198 1.00 19.10 C ANISOU 3757 CA TRP B 161 2070 2736 2452 -180 171 -290 C ATOM 3758 C TRP B 161 -33.130 26.537 37.057 1.00 20.07 C ANISOU 3758 C TRP B 161 2179 2836 2610 -208 203 -300 C ATOM 3759 O TRP B 161 -33.217 26.676 38.285 1.00 19.14 O ANISOU 3759 O TRP B 161 2075 2699 2499 -207 226 -278 O ATOM 3760 CB TRP B 161 -33.592 28.584 35.693 1.00 22.64 C ANISOU 3760 CB TRP B 161 2487 3224 2890 -160 153 -299 C ATOM 3761 CG TRP B 161 -33.084 29.927 35.269 1.00 29.78 C ANISOU 3761 CG TRP B 161 3408 4144 3764 -127 132 -277 C ATOM 3762 CD1 TRP B 161 -32.558 30.261 34.049 1.00 24.16 C ANISOU 3762 CD1 TRP B 161 2698 3452 3028 -111 107 -279 C ATOM 3763 CD2 TRP B 161 -33.056 31.121 36.058 1.00 20.59 C ANISOU 3763 CD2 TRP B 161 2260 2974 2589 -104 137 -249 C ATOM 3764 NE1 TRP B 161 -32.201 31.585 34.038 1.00 24.62 N ANISOU 3764 NE1 TRP B 161 2773 3516 3066 -80 98 -252 N ATOM 3765 CE2 TRP B 161 -32.496 32.137 35.258 1.00 26.39 C ANISOU 3765 CE2 TRP B 161 3005 3723 3299 -76 115 -234 C ATOM 3766 CE3 TRP B 161 -33.448 31.431 37.365 1.00 27.16 C ANISOU 3766 CE3 TRP B 161 3098 3790 3432 -103 158 -235 C ATOM 3767 CZ2 TRP B 161 -32.320 33.440 35.721 1.00 26.78 C ANISOU 3767 CZ2 TRP B 161 3070 3768 3338 -49 115 -209 C ATOM 3768 CZ3 TRP B 161 -33.269 32.725 37.823 1.00 24.01 C ANISOU 3768 CZ3 TRP B 161 2715 3390 3019 -76 156 -212 C ATOM 3769 CH2 TRP B 161 -32.715 33.713 37.001 1.00 28.60 C ANISOU 3769 CH2 TRP B 161 3305 3982 3579 -51 134 -200 C ATOM 3770 N VAL B 162 -33.591 25.454 36.428 1.00 19.30 N ANISOU 3770 N VAL B 162 2054 2742 2537 -233 204 -333 N ATOM 3771 CA VAL B 162 -34.180 24.343 37.173 1.00 19.54 C ANISOU 3771 CA VAL B 162 2070 2747 2608 -262 238 -343 C ATOM 3772 C VAL B 162 -33.141 23.705 38.086 1.00 20.69 C ANISOU 3772 C VAL B 162 2253 2848 2758 -270 265 -316 C ATOM 3773 O VAL B 162 -33.400 23.447 39.266 1.00 23.63 O ANISOU 3773 O VAL B 162 2632 3199 3147 -275 296 -297 O ATOM 3774 CB VAL B 162 -34.790 23.313 36.205 1.00 22.62 C ANISOU 3774 CB VAL B 162 2422 3148 3026 -288 233 -389 C ATOM 3775 CG1 VAL B 162 -35.083 22.008 36.928 1.00 25.19 C ANISOU 3775 CG1 VAL B 162 2738 3436 3398 -321 272 -396 C ATOM 3776 CG2 VAL B 162 -36.054 23.871 35.566 1.00 20.62 C ANISOU 3776 CG2 VAL B 162 2124 2939 2772 -282 211 -416 C ATOM 3777 N MET B 163 -31.946 23.440 37.552 1.00 21.82 N ANISOU 3777 N MET B 163 2423 2981 2888 -269 253 -313 N ATOM 3778 CA MET B 163 -30.910 22.807 38.362 1.00 20.53 C ANISOU 3778 CA MET B 163 2294 2777 2729 -274 277 -287 C ATOM 3779 C MET B 163 -30.384 23.760 39.429 1.00 19.97 C ANISOU 3779 C MET B 163 2255 2699 2632 -249 281 -249 C ATOM 3780 O MET B 163 -30.129 23.345 40.564 1.00 19.98 O ANISOU 3780 O MET B 163 2275 2675 2642 -252 309 -226 O ATOM 3781 CB MET B 163 -29.779 22.303 37.470 1.00 22.86 C ANISOU 3781 CB MET B 163 2606 3063 3016 -278 263 -295 C ATOM 3782 CG MET B 163 -30.212 21.265 36.442 1.00 19.14 C ANISOU 3782 CG MET B 163 2105 2596 2571 -303 260 -337 C ATOM 3783 SD MET B 163 -31.036 19.818 37.150 1.00 25.13 S ANISOU 3783 SD MET B 163 2840 3321 3386 -338 304 -352 S ATOM 3784 CE MET B 163 -29.698 19.077 38.073 1.00 24.60 C ANISOU 3784 CE MET B 163 2818 3205 3324 -340 334 -315 C ATOM 3785 N ALA B 164 -30.226 25.042 39.090 1.00 18.50 N ANISOU 3785 N ALA B 164 2076 2538 2416 -224 254 -242 N ATOM 3786 CA ALA B 164 -29.699 25.998 40.059 1.00 18.30 C ANISOU 3786 CA ALA B 164 2079 2506 2369 -201 255 -210 C ATOM 3787 C ALA B 164 -30.680 26.230 41.202 1.00 19.92 C ANISOU 3787 C ALA B 164 2275 2712 2583 -199 278 -201 C ATOM 3788 O ALA B 164 -30.268 26.362 42.359 1.00 18.33 O ANISOU 3788 O ALA B 164 2098 2494 2373 -189 294 -177 O ATOM 3789 CB ALA B 164 -29.357 27.317 39.369 1.00 18.57 C ANISOU 3789 CB ALA B 164 2119 2563 2375 -176 223 -206 C ATOM 3790 N LEU B 165 -31.979 26.299 40.895 1.00 18.68 N ANISOU 3790 N LEU B 165 2080 2576 2440 -205 278 -221 N ATOM 3791 CA LEU B 165 -32.987 26.413 41.945 1.00 18.87 C ANISOU 3791 CA LEU B 165 2092 2600 2476 -204 304 -214 C ATOM 3792 C LEU B 165 -33.058 25.145 42.786 1.00 19.06 C ANISOU 3792 C LEU B 165 2119 2594 2528 -225 342 -207 C ATOM 3793 O LEU B 165 -33.352 25.216 43.983 1.00 21.37 O ANISOU 3793 O LEU B 165 2421 2878 2822 -218 369 -186 O ATOM 3794 CB LEU B 165 -34.357 26.728 41.337 1.00 20.12 C ANISOU 3794 CB LEU B 165 2207 2790 2649 -207 295 -238 C ATOM 3795 CG LEU B 165 -34.606 28.163 40.855 1.00 22.92 C ANISOU 3795 CG LEU B 165 2556 3175 2977 -179 266 -237 C ATOM 3796 CD1 LEU B 165 -35.780 28.227 39.894 1.00 26.66 C ANISOU 3796 CD1 LEU B 165 2984 3683 3463 -184 250 -266 C ATOM 3797 CD2 LEU B 165 -34.843 29.094 42.033 1.00 22.52 C ANISOU 3797 CD2 LEU B 165 2520 3123 2915 -158 279 -214 C ATOM 3798 N ALA B 166 -32.787 23.983 42.188 1.00 19.14 N ANISOU 3798 N ALA B 166 2123 2589 2561 -249 348 -222 N ATOM 3799 CA ALA B 166 -32.763 22.738 42.949 1.00 19.33 C ANISOU 3799 CA ALA B 166 2151 2580 2614 -268 388 -213 C ATOM 3800 C ALA B 166 -31.643 22.709 43.978 1.00 19.12 C ANISOU 3800 C ALA B 166 2168 2530 2566 -252 402 -176 C ATOM 3801 O ALA B 166 -31.690 21.894 44.904 1.00 19.81 O ANISOU 3801 O ALA B 166 2262 2592 2670 -259 439 -158 O ATOM 3802 CB ALA B 166 -32.626 21.546 42.003 1.00 19.48 C ANISOU 3802 CB ALA B 166 2154 2585 2663 -296 389 -240 C ATOM 3803 N CYS B 167 -30.635 23.569 43.827 1.00 20.22 N ANISOU 3803 N CYS B 167 2336 2678 2671 -232 373 -165 N ATOM 3804 CA CYS B 167 -29.543 23.726 44.780 1.00 19.78 C ANISOU 3804 CA CYS B 167 2319 2605 2590 -214 379 -134 C ATOM 3805 C CYS B 167 -29.738 24.912 45.719 1.00 23.03 C ANISOU 3805 C CYS B 167 2742 3032 2975 -187 376 -118 C ATOM 3806 O CYS B 167 -29.516 24.779 46.927 1.00 22.13 O ANISOU 3806 O CYS B 167 2650 2908 2852 -176 399 -95 O ATOM 3807 CB CYS B 167 -28.215 23.882 44.025 1.00 19.75 C ANISOU 3807 CB CYS B 167 2337 2598 2569 -208 351 -135 C ATOM 3808 SG CYS B 167 -26.723 23.968 45.061 1.00 22.33 S ANISOU 3808 SG CYS B 167 2710 2907 2870 -188 354 -101 S ATOM 3809 N ALA B 168 -30.157 26.072 45.197 1.00 18.42 N ANISOU 3809 N ALA B 168 2147 2474 2378 -175 350 -131 N ATOM 3810 CA ALA B 168 -30.222 27.286 46.009 1.00 18.38 C ANISOU 3810 CA ALA B 168 2154 2481 2348 -149 344 -118 C ATOM 3811 C ALA B 168 -31.461 27.358 46.901 1.00 20.16 C ANISOU 3811 C ALA B 168 2363 2714 2582 -146 372 -115 C ATOM 3812 O ALA B 168 -31.421 28.023 47.941 1.00 21.52 O ANISOU 3812 O ALA B 168 2552 2889 2734 -125 379 -100 O ATOM 3813 CB ALA B 168 -30.172 28.524 45.111 1.00 20.28 C ANISOU 3813 CB ALA B 168 2389 2743 2575 -135 309 -130 C ATOM 3814 N ALA B 169 -32.570 26.720 46.509 1.00 23.32 N ANISOU 3814 N ALA B 169 2729 3118 3013 -166 387 -130 N ATOM 3815 CA ALA B 169 -33.861 26.894 47.180 1.00 20.20 C ANISOU 3815 CA ALA B 169 2312 2734 2630 -164 411 -129 C ATOM 3816 C ALA B 169 -34.053 26.092 48.474 1.00 22.32 C ANISOU 3816 C ALA B 169 2591 2983 2908 -165 456 -107 C ATOM 3817 O ALA B 169 -34.626 26.633 49.428 1.00 19.48 O ANISOU 3817 O ALA B 169 2233 2632 2537 -148 473 -95 O ATOM 3818 CB ALA B 169 -35.002 26.573 46.213 1.00 20.59 C ANISOU 3818 CB ALA B 169 2315 2796 2711 -184 408 -157 C ATOM 3819 N PRO B 170 -33.661 24.818 48.556 1.00 19.75 N ANISOU 3819 N PRO B 170 2271 2632 2602 -183 479 -99 N ATOM 3820 CA PRO B 170 -33.959 24.034 49.780 1.00 21.09 C ANISOU 3820 CA PRO B 170 2447 2784 2782 -182 526 -74 C ATOM 3821 C PRO B 170 -33.408 24.662 51.054 1.00 19.66 C ANISOU 3821 C PRO B 170 2301 2607 2560 -150 533 -46 C ATOM 3822 O PRO B 170 -34.065 24.568 52.100 1.00 19.92 O ANISOU 3822 O PRO B 170 2333 2640 2593 -140 568 -29 O ATOM 3823 CB PRO B 170 -33.309 22.673 49.493 1.00 21.31 C ANISOU 3823 CB PRO B 170 2480 2782 2834 -204 542 -70 C ATOM 3824 CG PRO B 170 -33.403 22.548 48.010 1.00 21.71 C ANISOU 3824 CG PRO B 170 2506 2838 2905 -226 512 -104 C ATOM 3825 CD PRO B 170 -33.161 23.938 47.477 1.00 19.50 C ANISOU 3825 CD PRO B 170 2232 2587 2591 -207 468 -116 C ATOM 3826 N PRO B 171 -32.222 25.298 51.044 1.00 19.61 N ANISOU 3826 N PRO B 171 2326 2604 2519 -132 502 -42 N ATOM 3827 CA PRO B 171 -31.776 25.986 52.274 1.00 21.68 C ANISOU 3827 CA PRO B 171 2619 2875 2742 -100 506 -22 C ATOM 3828 C PRO B 171 -32.685 27.122 52.717 1.00 19.39 C ANISOU 3828 C PRO B 171 2319 2609 2440 -83 504 -29 C ATOM 3829 O PRO B 171 -32.577 27.565 53.867 1.00 22.25 O ANISOU 3829 O PRO B 171 2702 2979 2773 -57 516 -14 O ATOM 3830 CB PRO B 171 -30.374 26.493 51.911 1.00 21.94 C ANISOU 3830 CB PRO B 171 2679 2908 2749 -91 467 -25 C ATOM 3831 CG PRO B 171 -29.900 25.535 50.886 1.00 23.53 C ANISOU 3831 CG PRO B 171 2873 3090 2975 -116 461 -32 C ATOM 3832 CD PRO B 171 -31.114 25.209 50.070 1.00 19.05 C ANISOU 3832 CD PRO B 171 2267 2527 2444 -140 469 -52 C ATOM 3833 N LEU B 172 -33.567 27.619 51.848 1.00 19.39 N ANISOU 3833 N LEU B 172 2288 2622 2459 -94 490 -51 N ATOM 3834 CA LEU B 172 -34.581 28.571 52.279 1.00 20.46 C ANISOU 3834 CA LEU B 172 2409 2778 2589 -78 494 -56 C ATOM 3835 C LEU B 172 -35.728 27.912 53.039 1.00 19.91 C ANISOU 3835 C LEU B 172 2320 2706 2540 -83 541 -45 C ATOM 3836 O LEU B 172 -36.402 28.593 53.816 1.00 23.78 O ANISOU 3836 O LEU B 172 2808 3210 3018 -64 555 -40 O ATOM 3837 CB LEU B 172 -35.161 29.331 51.079 1.00 19.43 C ANISOU 3837 CB LEU B 172 2249 2663 2471 -85 464 -82 C ATOM 3838 CG LEU B 172 -34.293 30.312 50.282 1.00 22.04 C ANISOU 3838 CG LEU B 172 2592 3000 2782 -75 419 -93 C ATOM 3839 CD1 LEU B 172 -35.059 30.809 49.059 1.00 21.26 C ANISOU 3839 CD1 LEU B 172 2459 2919 2700 -83 397 -114 C ATOM 3840 CD2 LEU B 172 -33.850 31.486 51.146 1.00 27.77 C ANISOU 3840 CD2 LEU B 172 3344 3732 3474 -45 410 -86 C ATOM 3841 N VAL B 173 -35.978 26.616 52.826 1.00 20.10 N ANISOU 3841 N VAL B 173 2328 2711 2598 -108 568 -41 N ATOM 3842 CA VAL B 173 -37.224 26.004 53.285 1.00 20.50 C ANISOU 3842 CA VAL B 173 2351 2758 2681 -119 612 -35 C ATOM 3843 C VAL B 173 -37.007 24.727 54.092 1.00 20.74 C ANISOU 3843 C VAL B 173 2394 2763 2725 -124 658 -6 C ATOM 3844 O VAL B 173 -37.897 23.869 54.151 1.00 21.08 O ANISOU 3844 O VAL B 173 2409 2793 2809 -144 696 -4 O ATOM 3845 CB VAL B 173 -38.169 25.721 52.100 1.00 20.61 C ANISOU 3845 CB VAL B 173 2318 2776 2739 -149 603 -64 C ATOM 3846 CG1 VAL B 173 -38.683 27.027 51.507 1.00 23.24 C ANISOU 3846 CG1 VAL B 173 2633 3137 3060 -137 568 -86 C ATOM 3847 CG2 VAL B 173 -37.473 24.890 51.042 1.00 20.48 C ANISOU 3847 CG2 VAL B 173 2298 2742 2741 -174 586 -78 C ATOM 3848 N GLY B 174 -35.838 24.578 54.711 1.00 20.61 N ANISOU 3848 N GLY B 174 2418 2738 2674 -106 657 15 N ATOM 3849 CA GLY B 174 -35.647 23.559 55.726 1.00 20.88 C ANISOU 3849 CA GLY B 174 2469 2753 2711 -100 704 50 C ATOM 3850 C GLY B 174 -34.719 22.400 55.412 1.00 20.84 C ANISOU 3850 C GLY B 174 2477 2720 2721 -115 710 61 C ATOM 3851 O GLY B 174 -34.674 21.449 56.199 1.00 21.12 O ANISOU 3851 O GLY B 174 2523 2737 2765 -111 755 92 O ATOM 3852 N TRP B 175 -33.996 22.423 54.294 1.00 20.52 N ANISOU 3852 N TRP B 175 2438 2676 2685 -132 670 38 N ATOM 3853 CA TRP B 175 -32.920 21.468 54.039 1.00 20.44 C ANISOU 3853 CA TRP B 175 2446 2640 2681 -141 671 49 C ATOM 3854 C TRP B 175 -31.624 22.264 53.989 1.00 20.84 C ANISOU 3854 C TRP B 175 2530 2704 2685 -120 627 48 C ATOM 3855 O TRP B 175 -31.434 23.086 53.087 1.00 20.67 O ANISOU 3855 O TRP B 175 2502 2696 2657 -124 584 21 O ATOM 3856 CB TRP B 175 -33.144 20.688 52.744 1.00 23.54 C ANISOU 3856 CB TRP B 175 2809 3014 3122 -179 665 22 C ATOM 3857 CG TRP B 175 -32.341 19.416 52.664 1.00 23.01 C ANISOU 3857 CG TRP B 175 2754 2914 3074 -191 685 37 C ATOM 3858 CD1 TRP B 175 -31.752 18.747 53.703 1.00 23.28 C ANISOU 3858 CD1 TRP B 175 2816 2931 3097 -173 720 77 C ATOM 3859 CD2 TRP B 175 -32.038 18.665 51.483 1.00 20.46 C ANISOU 3859 CD2 TRP B 175 2417 2571 2785 -221 673 14 C ATOM 3860 NE1 TRP B 175 -31.103 17.626 53.238 1.00 20.95 N ANISOU 3860 NE1 TRP B 175 2525 2605 2829 -191 730 80 N ATOM 3861 CE2 TRP B 175 -31.267 17.553 51.878 1.00 22.63 C ANISOU 3861 CE2 TRP B 175 2712 2815 3071 -222 703 40 C ATOM 3862 CE3 TRP B 175 -32.348 18.823 50.129 1.00 22.89 C ANISOU 3862 CE3 TRP B 175 2696 2887 3114 -246 641 -28 C ATOM 3863 CZ2 TRP B 175 -30.796 16.608 50.966 1.00 21.93 C ANISOU 3863 CZ2 TRP B 175 2617 2701 3016 -247 701 25 C ATOM 3864 CZ3 TRP B 175 -31.878 17.885 49.227 1.00 25.48 C ANISOU 3864 CZ3 TRP B 175 3018 3192 3471 -271 638 -44 C ATOM 3865 CH2 TRP B 175 -31.112 16.792 49.650 1.00 23.06 C ANISOU 3865 CH2 TRP B 175 2732 2852 3178 -272 669 -18 C ATOM 3866 N SER B 176 -30.736 22.011 54.954 1.00 20.08 N ANISOU 3866 N SER B 176 2468 2604 2559 -95 639 78 N ATOM 3867 CA SER B 176 -29.607 22.887 55.254 1.00 19.80 C ANISOU 3867 CA SER B 176 2463 2584 2475 -69 602 79 C ATOM 3868 C SER B 176 -30.107 24.293 55.565 1.00 21.03 C ANISOU 3868 C SER B 176 2617 2769 2604 -50 581 64 C ATOM 3869 O SER B 176 -31.294 24.487 55.845 1.00 24.90 O ANISOU 3869 O SER B 176 3087 3268 3106 -51 603 62 O ATOM 3870 CB SER B 176 -28.590 22.916 54.110 1.00 25.44 C ANISOU 3870 CB SER B 176 3181 3290 3194 -84 561 61 C ATOM 3871 OG SER B 176 -27.440 23.656 54.494 1.00 23.50 O ANISOU 3871 OG SER B 176 2965 3057 2906 -58 530 64 O ATOM 3872 N ARG B 177 -29.207 25.271 55.547 1.00 22.89 N ANISOU 3872 N ARG B 177 2872 3018 2806 -33 541 54 N ATOM 3873 CA ARG B 177 -29.550 26.656 55.843 1.00 19.39 C ANISOU 3873 CA ARG B 177 2429 2599 2338 -14 520 38 C ATOM 3874 C ARG B 177 -28.396 27.528 55.376 1.00 19.05 C ANISOU 3874 C ARG B 177 2402 2561 2275 -6 473 22 C ATOM 3875 O ARG B 177 -27.276 27.050 55.186 1.00 19.44 O ANISOU 3875 O ARG B 177 2468 2599 2320 -8 460 29 O ATOM 3876 CB ARG B 177 -29.822 26.874 57.339 1.00 20.17 C ANISOU 3876 CB ARG B 177 2545 2714 2404 18 546 57 C ATOM 3877 CG ARG B 177 -28.667 26.474 58.265 1.00 21.94 C ANISOU 3877 CG ARG B 177 2804 2939 2594 42 549 80 C ATOM 3878 CD ARG B 177 -29.054 26.617 59.740 1.00 23.88 C ANISOU 3878 CD ARG B 177 3064 3204 2805 76 579 99 C ATOM 3879 NE ARG B 177 -28.004 26.157 60.644 1.00 24.42 N ANISOU 3879 NE ARG B 177 3164 3278 2838 102 583 122 N ATOM 3880 CZ ARG B 177 -28.030 26.297 61.964 1.00 27.00 C ANISOU 3880 CZ ARG B 177 3510 3625 3123 138 601 139 C ATOM 3881 NH1 ARG B 177 -29.045 26.881 62.578 1.00 23.57 N ANISOU 3881 NH1 ARG B 177 3070 3209 2679 152 620 135 N ATOM 3882 NH2 ARG B 177 -27.005 25.848 62.686 1.00 23.83 N ANISOU 3882 NH2 ARG B 177 3136 3231 2689 162 601 159 N ATOM 3883 N TYR B 178 -28.687 28.809 55.177 1.00 22.12 N ANISOU 3883 N TYR B 178 2784 2965 2655 3 448 1 N ATOM 3884 CA TYR B 178 -27.649 29.787 54.888 1.00 18.66 C ANISOU 3884 CA TYR B 178 2361 2531 2199 13 407 -14 C ATOM 3885 C TYR B 178 -27.167 30.396 56.198 1.00 18.78 C ANISOU 3885 C TYR B 178 2401 2560 2175 46 405 -10 C ATOM 3886 O TYR B 178 -27.969 30.711 57.083 1.00 19.10 O ANISOU 3886 O TYR B 178 2441 2615 2202 62 425 -7 O ATOM 3887 CB TYR B 178 -28.157 30.877 53.941 1.00 18.51 C ANISOU 3887 CB TYR B 178 2320 2518 2193 7 382 -37 C ATOM 3888 CG TYR B 178 -28.437 30.375 52.540 1.00 18.38 C ANISOU 3888 CG TYR B 178 2282 2493 2210 -21 375 -45 C ATOM 3889 CD1 TYR B 178 -27.402 29.952 51.714 1.00 18.47 C ANISOU 3889 CD1 TYR B 178 2300 2491 2228 -34 356 -46 C ATOM 3890 CD2 TYR B 178 -29.736 30.319 52.043 1.00 19.54 C ANISOU 3890 CD2 TYR B 178 2398 2646 2380 -34 387 -53 C ATOM 3891 CE1 TYR B 178 -27.652 29.490 50.426 1.00 21.58 C ANISOU 3891 CE1 TYR B 178 2673 2879 2648 -58 349 -56 C ATOM 3892 CE2 TYR B 178 -29.994 29.858 50.761 1.00 22.78 C ANISOU 3892 CE2 TYR B 178 2784 3052 2817 -59 379 -64 C ATOM 3893 CZ TYR B 178 -28.949 29.445 49.955 1.00 22.26 C ANISOU 3893 CZ TYR B 178 2728 2974 2755 -70 359 -66 C ATOM 3894 OH TYR B 178 -29.203 28.979 48.680 1.00 20.55 O ANISOU 3894 OH TYR B 178 2489 2756 2562 -92 350 -80 O ATOM 3895 N ILE B 179 -25.852 30.544 56.321 1.00 18.64 N ANISOU 3895 N ILE B 179 2404 2539 2139 55 380 -11 N ATOM 3896 CA ILE B 179 -25.251 30.932 57.595 1.00 18.79 C ANISOU 3896 CA ILE B 179 2447 2573 2119 86 376 -9 C ATOM 3897 C ILE B 179 -24.078 31.867 57.307 1.00 18.57 C ANISOU 3897 C ILE B 179 2429 2544 2082 93 334 -30 C ATOM 3898 O ILE B 179 -23.401 31.706 56.282 1.00 21.75 O ANISOU 3898 O ILE B 179 2828 2931 2505 74 314 -33 O ATOM 3899 CB ILE B 179 -24.841 29.678 58.393 1.00 19.03 C ANISOU 3899 CB ILE B 179 2495 2602 2133 95 403 21 C ATOM 3900 CG1 ILE B 179 -24.764 29.955 59.899 1.00 20.83 C ANISOU 3900 CG1 ILE B 179 2744 2854 2317 132 413 27 C ATOM 3901 CG2 ILE B 179 -23.527 29.096 57.880 1.00 20.43 C ANISOU 3901 CG2 ILE B 179 2683 2765 2315 87 384 27 C ATOM 3902 CD1 ILE B 179 -24.494 28.704 60.720 1.00 19.55 C ANISOU 3902 CD1 ILE B 179 2597 2693 2138 145 445 62 C ATOM 3903 N PRO B 180 -23.820 32.873 58.142 1.00 20.88 N ANISOU 3903 N PRO B 180 2733 2852 2349 118 319 -46 N ATOM 3904 CA PRO B 180 -22.689 33.772 57.876 1.00 18.50 C ANISOU 3904 CA PRO B 180 2438 2546 2045 122 280 -68 C ATOM 3905 C PRO B 180 -21.352 33.051 57.996 1.00 19.58 C ANISOU 3905 C PRO B 180 2590 2678 2171 124 268 -58 C ATOM 3906 O PRO B 180 -21.210 32.081 58.747 1.00 20.92 O ANISOU 3906 O PRO B 180 2773 2855 2321 135 288 -36 O ATOM 3907 CB PRO B 180 -22.836 34.860 58.948 1.00 18.72 C ANISOU 3907 CB PRO B 180 2473 2593 2045 150 273 -90 C ATOM 3908 CG PRO B 180 -24.254 34.751 59.435 1.00 20.75 C ANISOU 3908 CG PRO B 180 2723 2863 2298 156 307 -81 C ATOM 3909 CD PRO B 180 -24.605 33.305 59.314 1.00 18.97 C ANISOU 3909 CD PRO B 180 2496 2632 2081 143 338 -49 C ATOM 3910 N GLU B 181 -20.367 33.535 57.236 1.00 20.93 N ANISOU 3910 N GLU B 181 2759 2836 2358 115 236 -72 N ATOM 3911 CA GLU B 181 -19.048 32.915 57.158 1.00 19.87 C ANISOU 3911 CA GLU B 181 2636 2694 2219 114 222 -63 C ATOM 3912 C GLU B 181 -17.956 33.964 57.332 1.00 18.10 C ANISOU 3912 C GLU B 181 2416 2471 1990 126 186 -90 C ATOM 3913 O GLU B 181 -18.172 35.157 57.113 1.00 20.25 O ANISOU 3913 O GLU B 181 2679 2741 2274 127 171 -114 O ATOM 3914 CB GLU B 181 -18.821 32.187 55.821 1.00 22.37 C ANISOU 3914 CB GLU B 181 2943 2988 2569 86 222 -51 C ATOM 3915 CG GLU B 181 -19.885 31.158 55.443 1.00 24.74 C ANISOU 3915 CG GLU B 181 3234 3283 2884 68 256 -31 C ATOM 3916 CD GLU B 181 -19.446 30.278 54.281 1.00 25.28 C ANISOU 3916 CD GLU B 181 3296 3330 2978 44 256 -21 C ATOM 3917 OE1 GLU B 181 -18.740 29.277 54.529 1.00 20.89 O ANISOU 3917 OE1 GLU B 181 2752 2769 2418 45 264 -3 O ATOM 3918 OE2 GLU B 181 -19.787 30.593 53.120 1.00 24.09 O ANISOU 3918 OE2 GLU B 181 3129 3171 2853 25 247 -31 O ATOM 3919 N GLY B 182 -16.768 33.498 57.724 1.00 20.97 N ANISOU 3919 N GLY B 182 2792 2837 2340 135 172 -85 N ATOM 3920 CA GLY B 182 -15.592 34.341 57.802 1.00 18.12 C ANISOU 3920 CA GLY B 182 2432 2475 1980 143 137 -110 C ATOM 3921 C GLY B 182 -15.689 35.442 58.834 1.00 19.27 C ANISOU 3921 C GLY B 182 2580 2639 2103 167 124 -140 C ATOM 3922 O GLY B 182 -15.894 35.168 60.022 1.00 20.20 O ANISOU 3922 O GLY B 182 2711 2783 2183 191 134 -137 O ATOM 3923 N MET B 183 -15.539 36.689 58.392 1.00 18.29 N ANISOU 3923 N MET B 183 2445 2503 2002 161 103 -169 N ATOM 3924 CA MET B 183 -15.781 37.868 59.222 1.00 22.02 C ANISOU 3924 CA MET B 183 2917 2988 2462 180 93 -202 C ATOM 3925 C MET B 183 -17.296 38.138 59.457 1.00 22.42 C ANISOU 3925 C MET B 183 2965 3047 2506 185 119 -200 C ATOM 3926 O MET B 183 -17.631 39.159 60.077 1.00 19.60 O ANISOU 3926 O MET B 183 2607 2698 2141 200 113 -228 O ATOM 3927 CB MET B 183 -15.107 39.095 58.600 1.00 19.58 C ANISOU 3927 CB MET B 183 2595 2656 2188 172 66 -232 C ATOM 3928 CG MET B 183 -13.583 39.045 58.675 1.00 23.75 C ANISOU 3928 CG MET B 183 3123 3180 2719 173 37 -244 C ATOM 3929 SD MET B 183 -12.722 40.326 57.731 1.00 23.46 S ANISOU 3929 SD MET B 183 3069 3110 2736 158 12 -272 S ATOM 3930 CE MET B 183 -13.464 41.808 58.404 1.00 24.80 C ANISOU 3930 CE MET B 183 3233 3282 2907 172 9 -311 C ATOM 3931 N GLN B 184 -18.144 37.228 58.963 1.00 19.65 N ANISOU 3931 N GLN B 184 2612 2693 2161 171 147 -168 N ATOM 3932 CA GLN B 184 -19.595 37.189 59.179 1.00 18.59 C ANISOU 3932 CA GLN B 184 2474 2569 2022 173 176 -160 C ATOM 3933 C GLN B 184 -20.351 38.221 58.350 1.00 18.47 C ANISOU 3933 C GLN B 184 2440 2538 2038 162 174 -174 C ATOM 3934 O GLN B 184 -21.499 38.543 58.671 1.00 23.44 O ANISOU 3934 O GLN B 184 3065 3178 2663 169 193 -176 O ATOM 3935 CB GLN B 184 -19.969 37.353 60.658 1.00 18.96 C ANISOU 3935 CB GLN B 184 2533 2644 2026 204 186 -168 C ATOM 3936 CG GLN B 184 -19.230 36.409 61.614 1.00 23.39 C ANISOU 3936 CG GLN B 184 3113 3225 2549 223 188 -153 C ATOM 3937 CD GLN B 184 -19.598 34.945 61.424 1.00 22.46 C ANISOU 3937 CD GLN B 184 2999 3105 2431 213 220 -111 C ATOM 3938 OE1 GLN B 184 -20.648 34.495 61.877 1.00 21.38 O ANISOU 3938 OE1 GLN B 184 2862 2978 2282 220 253 -93 O ATOM 3939 NE2 GLN B 184 -18.725 34.194 60.758 1.00 18.92 N ANISOU 3939 NE2 GLN B 184 2551 2640 1997 198 211 -96 N ATOM 3940 N CYS B 185 -19.752 38.759 57.288 1.00 20.12 N ANISOU 3940 N CYS B 185 2639 2725 2280 146 154 -182 N ATOM 3941 CA CYS B 185 -20.429 39.731 56.437 1.00 21.09 C ANISOU 3941 CA CYS B 185 2746 2835 2434 138 153 -191 C ATOM 3942 C CYS B 185 -20.858 39.146 55.093 1.00 24.26 C ANISOU 3942 C CYS B 185 3133 3224 2859 114 162 -169 C ATOM 3943 O CYS B 185 -21.234 39.903 54.192 1.00 23.51 O ANISOU 3943 O CYS B 185 3024 3118 2791 108 158 -173 O ATOM 3944 CB CYS B 185 -19.542 40.962 56.233 1.00 19.50 C ANISOU 3944 CB CYS B 185 2541 2617 2253 141 127 -219 C ATOM 3945 SG CYS B 185 -19.401 42.011 57.721 1.00 23.04 S ANISOU 3945 SG CYS B 185 2998 3078 2678 170 116 -257 S ATOM 3946 N SER B 186 -20.816 37.821 54.939 1.00 20.68 N ANISOU 3946 N SER B 186 2685 2774 2400 103 175 -145 N ATOM 3947 CA SER B 186 -21.399 37.149 53.783 1.00 18.95 C ANISOU 3947 CA SER B 186 2451 2548 2201 81 186 -127 C ATOM 3948 C SER B 186 -21.923 35.794 54.237 1.00 22.23 C ANISOU 3948 C SER B 186 2872 2974 2603 76 212 -107 C ATOM 3949 O SER B 186 -21.557 35.298 55.305 1.00 22.80 O ANISOU 3949 O SER B 186 2959 3054 2649 89 219 -101 O ATOM 3950 CB SER B 186 -20.391 36.990 52.642 1.00 25.74 C ANISOU 3950 CB SER B 186 3309 3389 3081 65 168 -123 C ATOM 3951 OG SER B 186 -19.299 36.179 53.036 1.00 22.86 O ANISOU 3951 OG SER B 186 2959 3022 2704 65 162 -115 O ATOM 3952 N CYS B 187 -22.786 35.190 53.416 1.00 23.61 N ANISOU 3952 N CYS B 187 3031 3146 2795 58 228 -95 N ATOM 3953 CA CYS B 187 -23.478 33.968 53.810 1.00 22.72 C ANISOU 3953 CA CYS B 187 2916 3038 2676 51 258 -77 C ATOM 3954 C CYS B 187 -23.298 32.859 52.781 1.00 19.87 C ANISOU 3954 C CYS B 187 2549 2665 2337 27 262 -65 C ATOM 3955 O CYS B 187 -23.168 33.109 51.580 1.00 24.90 O ANISOU 3955 O CYS B 187 3174 3295 2994 13 246 -71 O ATOM 3956 CB CYS B 187 -24.977 34.227 54.044 1.00 20.63 C ANISOU 3956 CB CYS B 187 2637 2787 2416 54 280 -79 C ATOM 3957 SG CYS B 187 -25.278 35.008 55.639 1.00 22.31 S ANISOU 3957 SG CYS B 187 2863 3018 2596 85 288 -87 S ATOM 3958 N GLY B 188 -23.303 31.623 53.276 1.00 20.82 N ANISOU 3958 N GLY B 188 2676 2783 2452 22 286 -46 N ATOM 3959 CA GLY B 188 -23.158 30.441 52.445 1.00 20.63 C ANISOU 3959 CA GLY B 188 2645 2744 2447 -1 295 -36 C ATOM 3960 C GLY B 188 -23.855 29.239 53.049 1.00 22.74 C ANISOU 3960 C GLY B 188 2911 3010 2718 -6 332 -17 C ATOM 3961 O GLY B 188 -24.654 29.390 53.976 1.00 22.86 O ANISOU 3961 O GLY B 188 2927 3037 2721 8 353 -12 O ATOM 3962 N ILE B 189 -23.564 28.044 52.544 1.00 19.23 N ANISOU 3962 N ILE B 189 2466 2550 2291 -24 344 -6 N ATOM 3963 CA ILE B 189 -24.160 26.820 53.071 1.00 21.51 C ANISOU 3963 CA ILE B 189 2753 2831 2589 -30 384 14 C ATOM 3964 C ILE B 189 -23.501 26.467 54.404 1.00 23.45 C ANISOU 3964 C ILE B 189 3024 3080 2805 -5 398 36 C ATOM 3965 O ILE B 189 -22.327 26.774 54.640 1.00 18.92 O ANISOU 3965 O ILE B 189 2470 2509 2211 10 374 37 O ATOM 3966 CB ILE B 189 -24.026 25.692 52.026 1.00 21.15 C ANISOU 3966 CB ILE B 189 2696 2764 2576 -58 392 14 C ATOM 3967 CG1 ILE B 189 -24.870 26.020 50.792 1.00 22.86 C ANISOU 3967 CG1 ILE B 189 2884 2984 2818 -80 380 -10 C ATOM 3968 CG2 ILE B 189 -24.445 24.345 52.580 1.00 18.43 C ANISOU 3968 CG2 ILE B 189 2351 2405 2246 -65 435 36 C ATOM 3969 CD1 ILE B 189 -26.358 26.092 51.088 1.00 22.62 C ANISOU 3969 CD1 ILE B 189 2832 2964 2800 -84 404 -13 C ATOM 3970 N ASP B 190 -24.265 25.845 55.305 1.00 24.29 N ANISOU 3970 N ASP B 190 3131 3188 2908 2 436 56 N ATOM 3971 CA ASP B 190 -23.771 25.508 56.642 1.00 20.31 C ANISOU 3971 CA ASP B 190 2652 2694 2372 31 453 80 C ATOM 3972 C ASP B 190 -22.897 24.261 56.551 1.00 19.29 C ANISOU 3972 C ASP B 190 2534 2544 2251 26 466 103 C ATOM 3973 O ASP B 190 -23.394 23.133 56.568 1.00 19.72 O ANISOU 3973 O ASP B 190 2582 2580 2329 14 504 123 O ATOM 3974 CB ASP B 190 -24.934 25.307 57.614 1.00 21.76 C ANISOU 3974 CB ASP B 190 2831 2886 2549 43 494 96 C ATOM 3975 CG ASP B 190 -24.474 25.092 59.058 1.00 22.70 C ANISOU 3975 CG ASP B 190 2977 3021 2627 80 510 122 C ATOM 3976 OD1 ASP B 190 -23.256 24.957 59.294 1.00 19.46 O ANISOU 3976 OD1 ASP B 190 2587 2613 2195 94 491 129 O ATOM 3977 OD2 ASP B 190 -25.338 25.061 59.963 1.00 24.44 O ANISOU 3977 OD2 ASP B 190 3198 3254 2834 96 542 136 O ATOM 3978 N TYR B 191 -21.583 24.466 56.458 1.00 21.75 N ANISOU 3978 N TYR B 191 2862 2856 2546 36 435 101 N ATOM 3979 CA TYR B 191 -20.601 23.391 56.534 1.00 20.29 C ANISOU 3979 CA TYR B 191 2691 2656 2363 38 444 124 C ATOM 3980 C TYR B 191 -20.112 23.150 57.952 1.00 22.43 C ANISOU 3980 C TYR B 191 2986 2943 2594 75 457 150 C ATOM 3981 O TYR B 191 -19.277 22.263 58.166 1.00 24.27 O ANISOU 3981 O TYR B 191 3232 3166 2824 84 466 174 O ATOM 3982 CB TYR B 191 -19.385 23.706 55.655 1.00 23.95 C ANISOU 3982 CB TYR B 191 3158 3112 2831 30 403 108 C ATOM 3983 CG TYR B 191 -19.705 24.404 54.359 1.00 21.72 C ANISOU 3983 CG TYR B 191 2855 2824 2573 4 379 78 C ATOM 3984 CD1 TYR B 191 -20.243 23.706 53.287 1.00 22.45 C ANISOU 3984 CD1 TYR B 191 2930 2898 2704 -26 392 73 C ATOM 3985 CD2 TYR B 191 -19.455 25.762 54.198 1.00 24.35 C ANISOU 3985 CD2 TYR B 191 3188 3172 2893 12 343 54 C ATOM 3986 CE1 TYR B 191 -20.533 24.338 52.095 1.00 23.75 C ANISOU 3986 CE1 TYR B 191 3076 3061 2885 -45 369 46 C ATOM 3987 CE2 TYR B 191 -19.746 26.405 53.000 1.00 22.55 C ANISOU 3987 CE2 TYR B 191 2942 2940 2686 -8 323 30 C ATOM 3988 CZ TYR B 191 -20.288 25.684 51.956 1.00 22.99 C ANISOU 3988 CZ TYR B 191 2981 2981 2774 -35 335 28 C ATOM 3989 OH TYR B 191 -20.589 26.303 50.757 1.00 26.25 O ANISOU 3989 OH TYR B 191 3376 3394 3204 -51 315 6 O ATOM 3990 N TYR B 192 -20.622 23.908 58.921 1.00 20.75 N ANISOU 3990 N TYR B 192 2778 2756 2349 99 459 148 N ATOM 3991 CA TYR B 192 -19.971 24.070 60.211 1.00 19.48 C ANISOU 3991 CA TYR B 192 2640 2622 2140 140 455 161 C ATOM 3992 C TYR B 192 -20.604 23.260 61.333 1.00 23.87 C ANISOU 3992 C TYR B 192 3205 3184 2679 162 504 198 C ATOM 3993 O TYR B 192 -19.883 22.813 62.230 1.00 22.20 O ANISOU 3993 O TYR B 192 3015 2987 2435 194 511 223 O ATOM 3994 CB TYR B 192 -19.973 25.553 60.602 1.00 23.19 C ANISOU 3994 CB TYR B 192 3112 3119 2581 156 421 129 C ATOM 3995 CG TYR B 192 -19.352 26.459 59.558 1.00 20.87 C ANISOU 3995 CG TYR B 192 2808 2817 2304 137 375 95 C ATOM 3996 CD1 TYR B 192 -20.088 26.908 58.471 1.00 18.80 C ANISOU 3996 CD1 TYR B 192 2526 2541 2077 107 370 75 C ATOM 3997 CD2 TYR B 192 -18.033 26.866 59.665 1.00 21.46 C ANISOU 3997 CD2 TYR B 192 2893 2898 2361 150 339 84 C ATOM 3998 CE1 TYR B 192 -19.526 27.734 57.512 1.00 22.57 C ANISOU 3998 CE1 TYR B 192 2995 3012 2570 93 332 48 C ATOM 3999 CE2 TYR B 192 -17.461 27.693 58.714 1.00 21.31 C ANISOU 3999 CE2 TYR B 192 2865 2870 2361 133 301 55 C ATOM 4000 CZ TYR B 192 -18.211 28.124 57.641 1.00 26.62 C ANISOU 4000 CZ TYR B 192 3519 3528 3067 106 299 39 C ATOM 4001 OH TYR B 192 -17.641 28.942 56.690 1.00 24.19 O ANISOU 4001 OH TYR B 192 3203 3211 2778 92 265 15 O ATOM 4002 N THR B 193 -21.924 23.065 61.314 1.00 21.65 N ANISOU 4002 N THR B 193 2909 2896 2420 149 540 204 N ATOM 4003 CA THR B 193 -22.645 22.451 62.419 1.00 26.21 C ANISOU 4003 CA THR B 193 3495 3483 2982 172 590 238 C ATOM 4004 C THR B 193 -23.475 21.279 61.921 1.00 31.55 C ANISOU 4004 C THR B 193 4154 4125 3710 144 637 259 C ATOM 4005 O THR B 193 -23.898 21.262 60.762 1.00 27.61 O ANISOU 4005 O THR B 193 3632 3604 3255 105 629 237 O ATOM 4006 CB THR B 193 -23.577 23.459 63.114 1.00 29.14 C ANISOU 4006 CB THR B 193 3863 3882 3328 189 592 223 C ATOM 4007 OG1 THR B 193 -24.763 23.634 62.329 1.00 30.45 O ANISOU 4007 OG1 THR B 193 4002 4032 3536 156 604 207 O ATOM 4008 CG2 THR B 193 -22.891 24.810 63.288 1.00 22.70 C ANISOU 4008 CG2 THR B 193 3057 3093 2476 207 539 188 C ATOM 4009 N PRO B 194 -23.731 20.283 62.778 1.00 30.74 N ANISOU 4009 N PRO B 194 4060 4017 3603 162 688 302 N ATOM 4010 CA PRO B 194 -24.575 19.154 62.361 1.00 31.28 C ANISOU 4010 CA PRO B 194 4110 4049 3725 134 738 322 C ATOM 4011 C PRO B 194 -26.041 19.535 62.200 1.00 32.01 C ANISOU 4011 C PRO B 194 4176 4141 3843 115 758 306 C ATOM 4012 O PRO B 194 -26.669 19.170 61.201 1.00 32.11 O ANISOU 4012 O PRO B 194 4162 4128 3910 76 766 290 O ATOM 4013 CB PRO B 194 -24.381 18.132 63.491 1.00 41.90 C ANISOU 4013 CB PRO B 194 5474 5392 5052 167 787 375 C ATOM 4014 CG PRO B 194 -23.158 18.589 64.242 1.00 36.61 C ANISOU 4014 CG PRO B 194 4834 4755 4320 209 754 381 C ATOM 4015 CD PRO B 194 -23.148 20.073 64.113 1.00 31.45 C ANISOU 4015 CD PRO B 194 4178 4132 3639 210 702 336 C ATOM 4016 N HIS B 195 -26.591 20.251 63.186 1.00 28.88 N ANISOU 4016 N HIS B 195 3787 3776 3410 145 766 310 N ATOM 4017 CA HIS B 195 -27.951 20.793 63.161 1.00 31.18 C ANISOU 4017 CA HIS B 195 4056 4074 3718 133 782 294 C ATOM 4018 C HIS B 195 -28.977 19.832 62.568 1.00 30.87 C ANISOU 4018 C HIS B 195 3986 4000 3744 97 826 302 C ATOM 4019 O HIS B 195 -29.514 20.091 61.485 1.00 29.76 O ANISOU 4019 O HIS B 195 3818 3848 3643 61 808 268 O ATOM 4020 CB HIS B 195 -28.009 22.119 62.415 1.00 26.94 C ANISOU 4020 CB HIS B 195 3507 3552 3177 120 727 245 C ATOM 4021 CG HIS B 195 -29.191 22.951 62.799 1.00 25.07 C ANISOU 4021 CG HIS B 195 3256 3335 2934 126 738 233 C ATOM 4022 ND1 HIS B 195 -30.320 23.048 62.018 1.00 24.59 N ANISOU 4022 ND1 HIS B 195 3162 3262 2919 94 746 214 N ATOM 4023 CD2 HIS B 195 -29.439 23.684 63.911 1.00 31.47 C ANISOU 4023 CD2 HIS B 195 4081 4177 3698 163 743 237 C ATOM 4024 CE1 HIS B 195 -31.202 23.828 62.617 1.00 29.80 C ANISOU 4024 CE1 HIS B 195 3816 3944 3562 111 756 208 C ATOM 4025 NE2 HIS B 195 -30.691 24.229 63.767 1.00 26.54 N ANISOU 4025 NE2 HIS B 195 3433 3558 3094 152 755 221 N ATOM 4026 N GLU B 196 -29.225 18.713 63.254 1.00 28.73 N ANISOU 4026 N GLU B 196 3720 3712 3486 107 884 346 N ATOM 4027 CA GLU B 196 -30.015 17.624 62.684 1.00 28.47 C ANISOU 4027 CA GLU B 196 3658 3638 3521 71 929 354 C ATOM 4028 C GLU B 196 -31.412 18.064 62.257 1.00 27.31 C ANISOU 4028 C GLU B 196 3475 3492 3410 45 938 328 C ATOM 4029 O GLU B 196 -32.004 17.445 61.368 1.00 27.17 O ANISOU 4029 O GLU B 196 3426 3443 3453 5 951 313 O ATOM 4030 CB GLU B 196 -30.113 16.476 63.691 1.00 30.72 C ANISOU 4030 CB GLU B 196 3955 3907 3810 94 996 411 C ATOM 4031 CG GLU B 196 -28.837 15.647 63.834 1.00 35.76 C ANISOU 4031 CG GLU B 196 4620 4531 4437 109 997 440 C ATOM 4032 CD GLU B 196 -27.767 16.327 64.672 1.00 43.23 C ANISOU 4032 CD GLU B 196 5602 5517 5305 156 963 449 C ATOM 4033 OE1 GLU B 196 -27.935 17.520 65.014 1.00 42.01 O ANISOU 4033 OE1 GLU B 196 5453 5400 5108 173 931 426 O ATOM 4034 OE2 GLU B 196 -26.758 15.660 64.992 1.00 42.27 O ANISOU 4034 OE2 GLU B 196 5504 5390 5167 176 968 479 O ATOM 4035 N GLU B 197 -31.953 19.122 62.867 1.00 26.67 N ANISOU 4035 N GLU B 197 3396 3444 3292 68 929 319 N ATOM 4036 CA GLU B 197 -33.291 19.582 62.503 1.00 24.15 C ANISOU 4036 CA GLU B 197 3042 3127 3005 46 937 295 C ATOM 4037 C GLU B 197 -33.392 19.927 61.018 1.00 30.64 C ANISOU 4037 C GLU B 197 3837 3941 3865 5 892 248 C ATOM 4038 O GLU B 197 -34.470 19.811 60.426 1.00 24.44 O ANISOU 4038 O GLU B 197 3014 3145 3126 -24 906 229 O ATOM 4039 CB GLU B 197 -33.672 20.796 63.349 1.00 28.05 C ANISOU 4039 CB GLU B 197 3547 3662 3449 80 927 290 C ATOM 4040 CG GLU B 197 -35.106 21.272 63.178 1.00 32.53 C ANISOU 4040 CG GLU B 197 4079 4234 4045 65 943 272 C ATOM 4041 CD GLU B 197 -35.433 22.454 64.074 1.00 43.56 C ANISOU 4041 CD GLU B 197 5489 5669 5391 102 935 267 C ATOM 4042 OE1 GLU B 197 -34.516 22.943 64.773 1.00 41.01 O ANISOU 4042 OE1 GLU B 197 5202 5370 5010 137 913 273 O ATOM 4043 OE2 GLU B 197 -36.604 22.892 64.080 1.00 50.39 O ANISOU 4043 OE2 GLU B 197 6329 6543 6276 96 951 256 O ATOM 4044 N THR B 198 -32.290 20.348 60.401 1.00 24.56 N ANISOU 4044 N THR B 198 3083 3176 3073 4 839 228 N ATOM 4045 CA THR B 198 -32.279 20.688 58.984 1.00 24.78 C ANISOU 4045 CA THR B 198 3088 3199 3129 -31 795 185 C ATOM 4046 C THR B 198 -31.549 19.663 58.123 1.00 23.67 C ANISOU 4046 C THR B 198 2947 3027 3021 -57 792 184 C ATOM 4047 O THR B 198 -31.411 19.878 56.913 1.00 25.90 O ANISOU 4047 O THR B 198 3213 3305 3323 -83 754 150 O ATOM 4048 CB THR B 198 -31.665 22.079 58.779 1.00 20.92 C ANISOU 4048 CB THR B 198 2614 2738 2596 -15 737 159 C ATOM 4049 OG1 THR B 198 -30.484 22.212 59.582 1.00 27.11 O ANISOU 4049 OG1 THR B 198 3437 3534 3331 18 725 178 O ATOM 4050 CG2 THR B 198 -32.665 23.163 59.168 1.00 20.99 C ANISOU 4050 CG2 THR B 198 2611 2774 2591 -2 735 146 C ATOM 4051 N ASN B 199 -31.091 18.554 58.708 1.00 23.78 N ANISOU 4051 N ASN B 199 2977 3018 3041 -49 830 221 N ATOM 4052 CA ASN B 199 -30.430 17.477 57.969 1.00 26.08 C ANISOU 4052 CA ASN B 199 3266 3275 3366 -73 834 222 C ATOM 4053 C ASN B 199 -29.269 18.019 57.138 1.00 25.13 C ANISOU 4053 C ASN B 199 3161 3164 3225 -76 774 197 C ATOM 4054 O ASN B 199 -29.169 17.794 55.930 1.00 21.02 O ANISOU 4054 O ASN B 199 2622 2628 2736 -107 753 168 O ATOM 4055 CB ASN B 199 -31.433 16.724 57.093 1.00 25.35 C ANISOU 4055 CB ASN B 199 3133 3155 3344 -116 858 202 C ATOM 4056 CG ASN B 199 -32.502 16.030 57.908 1.00 30.53 C ANISOU 4056 CG ASN B 199 3773 3795 4031 -115 924 230 C ATOM 4057 OD1 ASN B 199 -33.648 16.473 57.956 1.00 35.68 O ANISOU 4057 OD1 ASN B 199 4399 4459 4698 -122 934 217 O ATOM 4058 ND2 ASN B 199 -32.131 14.936 58.559 1.00 31.60 N ANISOU 4058 ND2 ASN B 199 3925 3904 4179 -105 971 272 N ATOM 4059 N ASN B 200 -28.384 18.753 57.815 1.00 22.87 N ANISOU 4059 N ASN B 200 2905 2902 2881 -41 748 208 N ATOM 4060 CA ASN B 200 -27.310 19.465 57.131 1.00 20.50 C ANISOU 4060 CA ASN B 200 2618 2614 2558 -40 691 184 C ATOM 4061 C ASN B 200 -26.415 18.517 56.344 1.00 20.23 C ANISOU 4061 C ASN B 200 2587 2550 2549 -59 686 185 C ATOM 4062 O ASN B 200 -26.027 18.821 55.210 1.00 20.59 O ANISOU 4062 O ASN B 200 2625 2594 2606 -79 648 155 O ATOM 4063 CB ASN B 200 -26.478 20.246 58.146 1.00 24.30 C ANISOU 4063 CB ASN B 200 3132 3124 2979 1 670 197 C ATOM 4064 CG ASN B 200 -27.133 21.535 58.561 1.00 27.12 C ANISOU 4064 CG ASN B 200 3485 3512 3308 16 654 179 C ATOM 4065 OD1 ASN B 200 -28.262 21.837 58.157 1.00 22.77 O ANISOU 4065 OD1 ASN B 200 2908 2962 2782 -1 661 162 O ATOM 4066 ND2 ASN B 200 -26.428 22.312 59.374 1.00 20.21 N ANISOU 4066 ND2 ASN B 200 2635 2662 2381 51 631 182 N ATOM 4067 N GLU B 201 -26.071 17.369 56.933 1.00 21.98 N ANISOU 4067 N GLU B 201 2822 2750 2780 -51 727 221 N ATOM 4068 CA GLU B 201 -25.041 16.515 56.349 1.00 22.85 C ANISOU 4068 CA GLU B 201 2941 2834 2906 -62 722 227 C ATOM 4069 C GLU B 201 -25.454 15.996 54.978 1.00 22.99 C ANISOU 4069 C GLU B 201 2930 2826 2979 -106 720 195 C ATOM 4070 O GLU B 201 -24.645 15.986 54.043 1.00 25.40 O ANISOU 4070 O GLU B 201 3237 3124 3288 -118 687 175 O ATOM 4071 CB GLU B 201 -24.725 15.350 57.289 1.00 23.75 C ANISOU 4071 CB GLU B 201 3073 2928 3024 -42 772 275 C ATOM 4072 CG GLU B 201 -23.562 14.478 56.839 1.00 24.84 C ANISOU 4072 CG GLU B 201 3223 3040 3175 -47 770 286 C ATOM 4073 CD GLU B 201 -23.311 13.305 57.767 1.00 33.42 C ANISOU 4073 CD GLU B 201 4326 4104 4267 -26 823 337 C ATOM 4074 OE1 GLU B 201 -24.290 12.639 58.171 1.00 35.91 O ANISOU 4074 OE1 GLU B 201 4628 4401 4615 -32 876 356 O ATOM 4075 OE2 GLU B 201 -22.132 13.055 58.105 1.00 38.25 O ANISOU 4075 OE2 GLU B 201 4962 4718 4852 -1 814 360 O ATOM 4076 N SER B 202 -26.709 15.567 54.837 1.00 26.15 N ANISOU 4076 N SER B 202 3300 3212 3421 -128 753 188 N ATOM 4077 CA SER B 202 -27.153 15.029 53.558 1.00 21.05 C ANISOU 4077 CA SER B 202 2625 2545 2829 -170 751 153 C ATOM 4078 C SER B 202 -27.138 16.090 52.463 1.00 21.68 C ANISOU 4078 C SER B 202 2693 2650 2896 -182 694 109 C ATOM 4079 O SER B 202 -26.824 15.774 51.309 1.00 20.99 O ANISOU 4079 O SER B 202 2594 2550 2832 -206 673 82 O ATOM 4080 CB SER B 202 -28.545 14.408 53.701 1.00 24.44 C ANISOU 4080 CB SER B 202 3021 2956 3307 -191 798 152 C ATOM 4081 OG SER B 202 -29.453 15.298 54.319 1.00 21.06 O ANISOU 4081 OG SER B 202 2586 2557 2859 -177 800 153 O ATOM 4082 N PHE B 203 -27.447 17.349 52.797 1.00 20.03 N ANISOU 4082 N PHE B 203 2486 2475 2651 -164 668 102 N ATOM 4083 CA PHE B 203 -27.466 18.378 51.763 1.00 21.45 C ANISOU 4083 CA PHE B 203 2654 2677 2820 -173 618 64 C ATOM 4084 C PHE B 203 -26.067 18.679 51.229 1.00 21.01 C ANISOU 4084 C PHE B 203 2621 2624 2740 -165 577 60 C ATOM 4085 O PHE B 203 -25.902 18.910 50.025 1.00 22.11 O ANISOU 4085 O PHE B 203 2748 2765 2889 -183 546 30 O ATOM 4086 CB PHE B 203 -28.124 19.663 52.266 1.00 22.09 C ANISOU 4086 CB PHE B 203 2732 2790 2871 -154 603 59 C ATOM 4087 CG PHE B 203 -28.185 20.733 51.216 1.00 19.33 C ANISOU 4087 CG PHE B 203 2369 2462 2513 -161 555 24 C ATOM 4088 CD1 PHE B 203 -27.137 21.625 51.055 1.00 20.98 C ANISOU 4088 CD1 PHE B 203 2601 2686 2686 -143 514 21 C ATOM 4089 CD2 PHE B 203 -29.259 20.806 50.348 1.00 20.09 C ANISOU 4089 CD2 PHE B 203 2430 2565 2640 -184 551 -5 C ATOM 4090 CE1 PHE B 203 -27.167 22.584 50.058 1.00 22.39 C ANISOU 4090 CE1 PHE B 203 2767 2881 2859 -148 474 -7 C ATOM 4091 CE2 PHE B 203 -29.301 21.768 49.356 1.00 22.98 C ANISOU 4091 CE2 PHE B 203 2784 2951 2995 -187 508 -34 C ATOM 4092 CZ PHE B 203 -28.256 22.660 49.213 1.00 24.84 C ANISOU 4092 CZ PHE B 203 3044 3199 3196 -168 471 -33 C ATOM 4093 N VAL B 204 -25.053 18.723 52.101 1.00 21.24 N ANISOU 4093 N VAL B 204 2682 2654 2735 -138 577 88 N ATOM 4094 CA VAL B 204 -23.698 19.013 51.626 1.00 19.70 C ANISOU 4094 CA VAL B 204 2506 2460 2518 -130 540 84 C ATOM 4095 C VAL B 204 -23.226 17.920 50.676 1.00 20.75 C ANISOU 4095 C VAL B 204 2634 2564 2687 -155 546 78 C ATOM 4096 O VAL B 204 -22.621 18.197 49.632 1.00 19.60 O ANISOU 4096 O VAL B 204 2486 2420 2541 -165 512 56 O ATOM 4097 CB VAL B 204 -22.728 19.188 52.811 1.00 23.30 C ANISOU 4097 CB VAL B 204 2995 2925 2933 -95 539 115 C ATOM 4098 CG1 VAL B 204 -21.322 19.455 52.299 1.00 20.50 C ANISOU 4098 CG1 VAL B 204 2656 2570 2562 -89 502 110 C ATOM 4099 CG2 VAL B 204 -23.184 20.322 53.721 1.00 21.56 C ANISOU 4099 CG2 VAL B 204 2780 2735 2677 -70 531 116 C ATOM 4100 N AILE B 205 -23.491 16.659 51.023 0.26 21.90 N ANISOU 4100 N AILE B 205 2777 2682 2864 -164 591 97 N ATOM 4101 N BILE B 205 -23.488 16.659 51.028 0.74 21.89 N ANISOU 4101 N BILE B 205 2775 2681 2862 -164 591 97 N ATOM 4102 CA AILE B 205 -23.136 15.556 50.136 0.26 21.95 C ANISOU 4102 CA AILE B 205 2775 2656 2908 -189 602 87 C ATOM 4103 CA BILE B 205 -23.143 15.549 50.145 0.74 21.97 C ANISOU 4103 CA BILE B 205 2777 2659 2911 -189 602 88 C ATOM 4104 C AILE B 205 -23.899 15.667 48.822 0.26 20.92 C ANISOU 4104 C AILE B 205 2613 2529 2808 -221 585 43 C ATOM 4105 C BILE B 205 -23.899 15.668 48.827 0.74 20.88 C ANISOU 4105 C BILE B 205 2608 2524 2802 -220 585 43 C ATOM 4106 O AILE B 205 -23.337 15.457 47.740 0.26 22.08 O ANISOU 4106 O AILE B 205 2756 2668 2964 -235 563 21 O ATOM 4107 O BILE B 205 -23.328 15.472 47.746 0.74 22.11 O ANISOU 4107 O BILE B 205 2761 2672 2968 -235 562 21 O ATOM 4108 CB AILE B 205 -23.392 14.207 50.833 0.26 21.06 C ANISOU 4108 CB AILE B 205 2663 2511 2829 -192 659 118 C ATOM 4109 CB BILE B 205 -23.421 14.207 50.849 0.74 21.04 C ANISOU 4109 CB BILE B 205 2660 2507 2826 -192 660 118 C ATOM 4110 CG1AILE B 205 -22.647 14.154 52.169 0.26 22.41 C ANISOU 4110 CG1AILE B 205 2867 2686 2963 -154 674 164 C ATOM 4111 CG1BILE B 205 -22.545 14.076 52.100 0.74 22.59 C ANISOU 4111 CG1BILE B 205 2890 2706 2988 -155 674 164 C ATOM 4112 CG2AILE B 205 -22.964 13.056 49.938 0.26 21.95 C ANISOU 4112 CG2AILE B 205 2769 2587 2983 -217 671 106 C ATOM 4113 CG2BILE B 205 -23.184 13.044 49.901 0.74 21.39 C ANISOU 4113 CG2BILE B 205 2694 2517 2918 -220 674 103 C ATOM 4114 CD1AILE B 205 -21.149 14.300 52.037 0.26 21.70 C ANISOU 4114 CD1AILE B 205 2802 2600 2844 -137 643 172 C ATOM 4115 CD1BILE B 205 -22.787 12.803 52.896 0.74 20.80 C ANISOU 4115 CD1BILE B 205 2666 2447 2789 -152 734 201 C ATOM 4116 N TYR B 206 -25.189 16.000 48.896 1.00 20.31 N ANISOU 4116 N TYR B 206 2511 2464 2743 -230 594 29 N ATOM 4117 CA TYR B 206 -25.977 16.204 47.683 1.00 23.41 C ANISOU 4117 CA TYR B 206 2870 2865 3158 -257 574 -14 C ATOM 4118 C TYR B 206 -25.435 17.363 46.851 1.00 21.92 C ANISOU 4118 C TYR B 206 2687 2705 2936 -248 520 -35 C ATOM 4119 O TYR B 206 -25.283 17.242 45.630 1.00 22.10 O ANISOU 4119 O TYR B 206 2697 2729 2971 -265 498 -64 O ATOM 4120 CB TYR B 206 -27.443 16.435 48.065 1.00 23.99 C ANISOU 4120 CB TYR B 206 2917 2950 3249 -264 594 -21 C ATOM 4121 CG TYR B 206 -28.266 17.193 47.047 1.00 21.44 C ANISOU 4121 CG TYR B 206 2564 2654 2930 -277 561 -62 C ATOM 4122 CD1 TYR B 206 -28.793 16.555 45.935 1.00 22.19 C ANISOU 4122 CD1 TYR B 206 2627 2741 3064 -308 560 -99 C ATOM 4123 CD2 TYR B 206 -28.542 18.544 47.220 1.00 27.58 C ANISOU 4123 CD2 TYR B 206 3343 3466 3672 -258 533 -64 C ATOM 4124 CE1 TYR B 206 -29.565 17.246 45.016 1.00 24.50 C ANISOU 4124 CE1 TYR B 206 2890 3062 3356 -317 529 -135 C ATOM 4125 CE2 TYR B 206 -29.301 19.242 46.302 1.00 21.97 C ANISOU 4125 CE2 TYR B 206 2604 2780 2964 -267 505 -98 C ATOM 4126 CZ TYR B 206 -29.808 18.590 45.203 1.00 26.04 C ANISOU 4126 CZ TYR B 206 3088 3291 3514 -295 502 -132 C ATOM 4127 OH TYR B 206 -30.571 19.288 44.294 1.00 23.84 O ANISOU 4127 OH TYR B 206 2780 3042 3235 -301 473 -165 O ATOM 4128 N MET B 207 -25.106 18.485 47.496 1.00 18.90 N ANISOU 4128 N MET B 207 2324 2347 2512 -221 500 -20 N ATOM 4129 CA MET B 207 -24.608 19.641 46.756 1.00 21.13 C ANISOU 4129 CA MET B 207 2610 2653 2767 -212 453 -37 C ATOM 4130 C MET B 207 -23.296 19.333 46.040 1.00 23.01 C ANISOU 4130 C MET B 207 2864 2878 3000 -213 433 -38 C ATOM 4131 O MET B 207 -23.121 19.691 44.869 1.00 21.66 O ANISOU 4131 O MET B 207 2684 2718 2829 -221 404 -63 O ATOM 4132 CB MET B 207 -24.434 20.830 47.702 1.00 21.11 C ANISOU 4132 CB MET B 207 2625 2671 2724 -182 439 -21 C ATOM 4133 CG MET B 207 -24.060 22.128 46.992 1.00 25.11 C ANISOU 4133 CG MET B 207 3133 3201 3207 -173 394 -38 C ATOM 4134 SD MET B 207 -23.588 23.415 48.162 1.00 26.61 S ANISOU 4134 SD MET B 207 3347 3409 3355 -138 379 -21 S ATOM 4135 CE MET B 207 -22.122 22.684 48.873 1.00 23.98 C ANISOU 4135 CE MET B 207 3046 3057 3008 -125 387 7 C ATOM 4136 N PHE B 208 -22.362 18.660 46.717 1.00 20.50 N ANISOU 4136 N PHE B 208 2571 2540 2678 -203 450 -11 N ATOM 4137 CA PHE B 208 -21.062 18.413 46.102 1.00 22.98 C ANISOU 4137 CA PHE B 208 2900 2843 2987 -202 432 -10 C ATOM 4138 C PHE B 208 -21.131 17.348 45.013 1.00 23.61 C ANISOU 4138 C PHE B 208 2965 2902 3104 -230 442 -32 C ATOM 4139 O PHE B 208 -20.321 17.369 44.081 1.00 25.12 O ANISOU 4139 O PHE B 208 3161 3093 3292 -233 419 -44 O ATOM 4140 CB PHE B 208 -20.039 18.013 47.162 1.00 22.54 C ANISOU 4140 CB PHE B 208 2874 2775 2916 -181 446 25 C ATOM 4141 CG PHE B 208 -19.266 19.177 47.732 1.00 23.57 C ANISOU 4141 CG PHE B 208 3023 2926 3005 -153 416 36 C ATOM 4142 CD1 PHE B 208 -18.180 19.700 47.053 1.00 29.41 C ANISOU 4142 CD1 PHE B 208 3772 3670 3732 -148 383 28 C ATOM 4143 CD2 PHE B 208 -19.621 19.738 48.944 1.00 25.50 C ANISOU 4143 CD2 PHE B 208 3276 3187 3226 -132 423 52 C ATOM 4144 CE1 PHE B 208 -17.467 20.763 47.568 1.00 30.68 C ANISOU 4144 CE1 PHE B 208 3948 3849 3862 -125 356 34 C ATOM 4145 CE2 PHE B 208 -18.911 20.804 49.464 1.00 25.93 C ANISOU 4145 CE2 PHE B 208 3347 3261 3245 -107 395 56 C ATOM 4146 CZ PHE B 208 -17.832 21.314 48.776 1.00 25.09 C ANISOU 4146 CZ PHE B 208 3247 3156 3131 -105 362 47 C ATOM 4147 N VAL B 209 -22.066 16.406 45.114 1.00 18.52 N ANISOU 4147 N VAL B 209 2302 2241 2496 -250 476 -37 N ATOM 4148 CA VAL B 209 -22.103 15.303 44.161 1.00 21.41 C ANISOU 4148 CA VAL B 209 2653 2583 2899 -276 488 -60 C ATOM 4149 C VAL B 209 -22.880 15.688 42.910 1.00 19.81 C ANISOU 4149 C VAL B 209 2420 2401 2705 -295 463 -104 C ATOM 4150 O VAL B 209 -22.388 15.543 41.786 1.00 25.04 O ANISOU 4150 O VAL B 209 3080 3064 3370 -303 443 -127 O ATOM 4151 CB VAL B 209 -22.693 14.043 44.824 1.00 25.20 C ANISOU 4151 CB VAL B 209 3124 3030 3420 -290 540 -47 C ATOM 4152 CG1 VAL B 209 -23.130 13.048 43.764 1.00 25.47 C ANISOU 4152 CG1 VAL B 209 3133 3044 3502 -323 551 -83 C ATOM 4153 CG2 VAL B 209 -21.664 13.416 45.747 1.00 20.66 C ANISOU 4153 CG2 VAL B 209 2579 2431 2839 -272 564 -5 C ATOM 4154 N AVAL B 210 -24.102 16.193 43.095 0.85 20.27 N ANISOU 4154 N AVAL B 210 2456 2479 2767 -299 465 -115 N ATOM 4155 N BVAL B 210 -24.096 16.202 43.064 0.15 20.45 N ANISOU 4155 N BVAL B 210 2478 2501 2789 -299 464 -116 N ATOM 4156 CA AVAL B 210 -24.983 16.531 41.978 0.85 21.36 C ANISOU 4156 CA AVAL B 210 2562 2640 2914 -314 442 -157 C ATOM 4157 CA BVAL B 210 -24.889 16.488 41.874 0.15 21.31 C ANISOU 4157 CA BVAL B 210 2556 2632 2907 -315 440 -158 C ATOM 4158 C AVAL B 210 -24.581 17.861 41.352 0.85 22.37 C ANISOU 4158 C AVAL B 210 2697 2802 3001 -296 397 -163 C ATOM 4159 C BVAL B 210 -24.693 17.907 41.349 0.15 22.28 C ANISOU 4159 C BVAL B 210 2683 2792 2989 -296 396 -164 C ATOM 4160 O AVAL B 210 -24.618 18.021 40.128 0.85 22.46 O ANISOU 4160 O AVAL B 210 2695 2830 3010 -303 371 -193 O ATOM 4161 O BVAL B 210 -24.989 18.164 40.174 0.15 21.84 O ANISOU 4161 O BVAL B 210 2609 2757 2933 -304 371 -196 O ATOM 4162 CB AVAL B 210 -26.452 16.553 42.453 0.85 19.13 C ANISOU 4162 CB AVAL B 210 2251 2364 2653 -324 462 -165 C ATOM 4163 CB BVAL B 210 -26.387 16.229 42.116 0.15 19.82 C ANISOU 4163 CB BVAL B 210 2334 2447 2750 -332 463 -174 C ATOM 4164 CG1AVAL B 210 -27.378 17.066 41.349 0.85 21.62 C ANISOU 4164 CG1AVAL B 210 2532 2712 2972 -336 434 -207 C ATOM 4165 CG1BVAL B 210 -26.600 14.859 42.745 0.15 19.55 C ANISOU 4165 CG1BVAL B 210 2296 2372 2761 -350 512 -163 C ATOM 4166 CG2AVAL B 210 -26.895 15.176 42.916 0.85 19.51 C ANISOU 4166 CG2AVAL B 210 2288 2376 2750 -346 510 -162 C ATOM 4167 CG2BVAL B 210 -26.974 17.317 42.968 0.15 20.26 C ANISOU 4167 CG2BVAL B 210 2392 2526 2781 -312 459 -156 C ATOM 4168 N HIS B 211 -24.202 18.837 42.175 1.00 21.05 N ANISOU 4168 N HIS B 211 2551 2646 2801 -270 387 -136 N ATOM 4169 CA HIS B 211 -23.970 20.202 41.717 1.00 19.98 C ANISOU 4169 CA HIS B 211 2420 2540 2632 -252 349 -139 C ATOM 4170 C HIS B 211 -22.500 20.616 41.734 1.00 19.16 C ANISOU 4170 C HIS B 211 2347 2432 2503 -234 331 -120 C ATOM 4171 O HIS B 211 -22.214 21.818 41.691 1.00 19.64 O ANISOU 4171 O HIS B 211 2415 2510 2536 -215 306 -115 O ATOM 4172 CB HIS B 211 -24.804 21.181 42.551 1.00 21.18 C ANISOU 4172 CB HIS B 211 2566 2711 2769 -238 350 -130 C ATOM 4173 CG HIS B 211 -26.283 20.985 42.411 1.00 21.39 C ANISOU 4173 CG HIS B 211 2558 2749 2820 -253 362 -151 C ATOM 4174 ND1 HIS B 211 -26.960 21.231 41.234 1.00 19.30 N ANISOU 4174 ND1 HIS B 211 2265 2506 2560 -263 341 -184 N ATOM 4175 CD2 HIS B 211 -27.217 20.570 43.301 1.00 18.57 C ANISOU 4175 CD2 HIS B 211 2190 2384 2483 -260 394 -144 C ATOM 4176 CE1 HIS B 211 -28.245 20.968 41.404 1.00 18.99 C ANISOU 4176 CE1 HIS B 211 2196 2473 2545 -276 357 -198 C ATOM 4177 NE2 HIS B 211 -28.426 20.562 42.649 1.00 18.78 N ANISOU 4177 NE2 HIS B 211 2179 2427 2530 -276 392 -174 N ATOM 4178 N PHE B 212 -21.565 19.679 41.915 1.00 21.63 N ANISOU 4178 N PHE B 212 2678 2717 2824 -237 346 -107 N ATOM 4179 CA PHE B 212 -20.163 19.962 41.615 1.00 17.76 C ANISOU 4179 CA PHE B 212 2210 2223 2315 -224 326 -96 C ATOM 4180 C PHE B 212 -19.519 18.889 40.731 1.00 21.62 C ANISOU 4180 C PHE B 212 2700 2691 2823 -239 332 -107 C ATOM 4181 O PHE B 212 -19.030 19.181 39.633 1.00 17.87 O ANISOU 4181 O PHE B 212 2224 2227 2341 -239 308 -122 O ATOM 4182 CB PHE B 212 -19.392 20.141 42.931 1.00 21.80 C ANISOU 4182 CB PHE B 212 2748 2725 2810 -204 334 -62 C ATOM 4183 CG PHE B 212 -17.947 20.539 42.760 1.00 19.55 C ANISOU 4183 CG PHE B 212 2484 2437 2506 -189 313 -50 C ATOM 4184 CD1 PHE B 212 -17.601 21.691 42.074 1.00 21.88 C ANISOU 4184 CD1 PHE B 212 2778 2750 2784 -179 281 -59 C ATOM 4185 CD2 PHE B 212 -16.939 19.776 43.326 1.00 24.71 C ANISOU 4185 CD2 PHE B 212 3157 3068 3161 -183 326 -28 C ATOM 4186 CE1 PHE B 212 -16.278 22.056 41.933 1.00 29.49 C ANISOU 4186 CE1 PHE B 212 3760 3710 3736 -166 264 -48 C ATOM 4187 CE2 PHE B 212 -15.616 20.136 43.188 1.00 27.21 C ANISOU 4187 CE2 PHE B 212 3492 3384 3465 -169 307 -18 C ATOM 4188 CZ PHE B 212 -15.284 21.277 42.495 1.00 32.69 C ANISOU 4188 CZ PHE B 212 4183 4094 4144 -162 276 -29 C ATOM 4189 N ILE B 213 -19.562 17.634 41.186 1.00 18.13 N ANISOU 4189 N ILE B 213 2260 2222 2408 -252 365 -100 N ATOM 4190 CA AILE B 213 -18.779 16.572 40.559 0.67 20.51 C ANISOU 4190 CA AILE B 213 2566 2498 2728 -264 374 -105 C ATOM 4191 CA BILE B 213 -18.776 16.575 40.558 0.34 20.52 C ANISOU 4191 CA BILE B 213 2568 2500 2730 -263 374 -105 C ATOM 4192 C ILE B 213 -19.415 16.117 39.253 1.00 18.76 C ANISOU 4192 C ILE B 213 2319 2282 2527 -286 369 -147 C ATOM 4193 O ILE B 213 -18.741 15.997 38.225 1.00 20.23 O ANISOU 4193 O ILE B 213 2509 2470 2710 -288 353 -162 O ATOM 4194 CB AILE B 213 -18.605 15.396 41.536 0.67 23.04 C ANISOU 4194 CB AILE B 213 2897 2784 3072 -267 414 -81 C ATOM 4195 CB BILE B 213 -18.590 15.401 41.536 0.34 22.33 C ANISOU 4195 CB BILE B 213 2808 2695 2982 -267 414 -81 C ATOM 4196 CG1AILE B 213 -17.715 15.805 42.716 0.67 20.04 C ANISOU 4196 CG1AILE B 213 2545 2403 2665 -240 414 -41 C ATOM 4197 CG1BILE B 213 -17.768 15.842 42.751 0.34 19.41 C ANISOU 4197 CG1BILE B 213 2465 2324 2585 -240 414 -41 C ATOM 4198 CG2AILE B 213 -18.035 14.187 40.814 0.67 21.91 C ANISOU 4198 CG2AILE B 213 2755 2613 2958 -283 429 -92 C ATOM 4199 CG2BILE B 213 -17.926 14.229 40.837 0.34 21.90 C ANISOU 4199 CG2BILE B 213 2756 2611 2954 -281 427 -90 C ATOM 4200 CD1AILE B 213 -17.587 14.737 43.773 0.67 24.89 C ANISOU 4200 CD1AILE B 213 3171 2989 3298 -237 454 -11 C ATOM 4201 CD1BILE B 213 -16.356 16.261 42.415 0.34 23.27 C ANISOU 4201 CD1BILE B 213 2974 2816 3052 -224 388 -32 C ATOM 4202 N ILE B 214 -20.720 15.843 39.273 1.00 25.43 N ANISOU 4202 N ILE B 214 3137 3130 3394 -303 382 -167 N ATOM 4203 CA ILE B 214 -21.397 15.397 38.054 1.00 20.23 C ANISOU 4203 CA ILE B 214 2451 2480 2756 -325 375 -211 C ATOM 4204 C ILE B 214 -21.262 16.413 36.924 1.00 18.30 C ANISOU 4204 C ILE B 214 2202 2273 2480 -314 334 -230 C ATOM 4205 O ILE B 214 -20.929 16.008 35.798 1.00 23.19 O ANISOU 4205 O ILE B 214 2815 2894 3101 -321 323 -256 O ATOM 4206 CB ILE B 214 -22.857 15.025 38.368 1.00 21.05 C ANISOU 4206 CB ILE B 214 2524 2584 2890 -344 396 -229 C ATOM 4207 CG1 ILE B 214 -22.906 13.699 39.132 1.00 19.01 C ANISOU 4207 CG1 ILE B 214 2268 2282 2674 -360 442 -217 C ATOM 4208 CG2 ILE B 214 -23.681 14.926 37.087 1.00 22.37 C ANISOU 4208 CG2 ILE B 214 2658 2773 3069 -362 378 -280 C ATOM 4209 CD1 ILE B 214 -24.291 13.333 39.651 1.00 20.33 C ANISOU 4209 CD1 ILE B 214 2406 2443 2875 -378 470 -227 C ATOM 4210 N PRO B 215 -21.477 17.721 37.139 1.00 18.01 N ANISOU 4210 N PRO B 215 2167 2265 2413 -294 312 -218 N ATOM 4211 CA PRO B 215 -21.195 18.677 36.051 1.00 17.84 C ANISOU 4211 CA PRO B 215 2144 2274 2361 -280 276 -230 C ATOM 4212 C PRO B 215 -19.758 18.644 35.555 1.00 19.36 C ANISOU 4212 C PRO B 215 2360 2456 2539 -270 266 -218 C ATOM 4213 O PRO B 215 -19.533 18.718 34.340 1.00 23.71 O ANISOU 4213 O PRO B 215 2905 3023 3080 -268 248 -239 O ATOM 4214 CB PRO B 215 -21.534 20.036 36.680 1.00 25.78 C ANISOU 4214 CB PRO B 215 3152 3301 3342 -260 262 -210 C ATOM 4215 CG PRO B 215 -22.474 19.730 37.783 1.00 17.84 C ANISOU 4215 CG PRO B 215 2137 2286 2356 -269 288 -204 C ATOM 4216 CD PRO B 215 -22.058 18.397 38.317 1.00 17.98 C ANISOU 4216 CD PRO B 215 2164 2266 2400 -284 320 -196 C ATOM 4217 N LEU B 216 -18.772 18.533 36.453 1.00 20.58 N ANISOU 4217 N LEU B 216 2542 2587 2692 -261 278 -185 N ATOM 4218 CA LEU B 216 -17.378 18.525 36.010 1.00 20.80 C ANISOU 4218 CA LEU B 216 2591 2604 2709 -250 269 -173 C ATOM 4219 C LEU B 216 -17.069 17.280 35.185 1.00 20.36 C ANISOU 4219 C LEU B 216 2532 2532 2674 -267 281 -195 C ATOM 4220 O LEU B 216 -16.356 17.356 34.174 1.00 21.38 O ANISOU 4220 O LEU B 216 2665 2667 2792 -261 266 -204 O ATOM 4221 CB LEU B 216 -16.433 18.627 37.210 1.00 22.24 C ANISOU 4221 CB LEU B 216 2799 2767 2886 -236 278 -136 C ATOM 4222 CG LEU B 216 -16.197 20.024 37.797 1.00 21.65 C ANISOU 4222 CG LEU B 216 2734 2709 2785 -214 259 -115 C ATOM 4223 CD1 LEU B 216 -15.019 20.010 38.763 1.00 23.23 C ANISOU 4223 CD1 LEU B 216 2958 2889 2978 -200 264 -84 C ATOM 4224 CD2 LEU B 216 -15.977 21.055 36.699 1.00 25.90 C ANISOU 4224 CD2 LEU B 216 3268 3271 3304 -203 230 -124 C ATOM 4225 N ILE B 217 -17.609 16.129 35.591 1.00 21.02 N ANISOU 4225 N ILE B 217 2606 2591 2790 -287 309 -205 N ATOM 4226 CA ILE B 217 -17.425 14.900 34.822 1.00 24.31 C ANISOU 4226 CA ILE B 217 3016 2988 3233 -306 323 -231 C ATOM 4227 C ILE B 217 -17.932 15.077 33.394 1.00 20.25 C ANISOU 4227 C ILE B 217 2481 2504 2710 -311 300 -273 C ATOM 4228 O ILE B 217 -17.291 14.635 32.432 1.00 21.05 O ANISOU 4228 O ILE B 217 2585 2603 2809 -313 295 -290 O ATOM 4229 CB ILE B 217 -18.123 13.723 35.530 1.00 23.97 C ANISOU 4229 CB ILE B 217 2962 2913 3231 -328 360 -235 C ATOM 4230 CG1 ILE B 217 -17.417 13.406 36.849 1.00 23.24 C ANISOU 4230 CG1 ILE B 217 2894 2791 3144 -318 385 -190 C ATOM 4231 CG2 ILE B 217 -18.168 12.497 34.626 1.00 23.72 C ANISOU 4231 CG2 ILE B 217 2917 2862 3232 -350 373 -272 C ATOM 4232 CD1 ILE B 217 -17.999 12.209 37.576 1.00 33.66 C ANISOU 4232 CD1 ILE B 217 4206 4076 4506 -336 427 -187 C ATOM 4233 N VAL B 218 -19.090 15.723 33.233 1.00 19.09 N ANISOU 4233 N VAL B 218 2310 2387 2555 -313 286 -291 N ATOM 4234 CA VAL B 218 -19.660 15.926 31.900 1.00 18.85 C ANISOU 4234 CA VAL B 218 2258 2393 2513 -315 262 -331 C ATOM 4235 C VAL B 218 -18.773 16.844 31.067 1.00 18.05 C ANISOU 4235 C VAL B 218 2171 2315 2372 -290 234 -321 C ATOM 4236 O VAL B 218 -18.523 16.588 29.882 1.00 19.23 O ANISOU 4236 O VAL B 218 2315 2478 2511 -288 222 -347 O ATOM 4237 CB VAL B 218 -21.093 16.478 32.009 1.00 18.88 C ANISOU 4237 CB VAL B 218 2233 2425 2517 -319 253 -348 C ATOM 4238 CG1 VAL B 218 -21.566 17.009 30.661 1.00 21.00 C ANISOU 4238 CG1 VAL B 218 2480 2739 2760 -310 221 -382 C ATOM 4239 CG2 VAL B 218 -22.036 15.399 32.514 1.00 19.06 C ANISOU 4239 CG2 VAL B 218 2234 2425 2584 -347 281 -369 C ATOM 4240 N ILE B 219 -18.306 17.941 31.667 1.00 18.71 N ANISOU 4240 N ILE B 219 2272 2403 2433 -268 225 -283 N ATOM 4241 CA ILE B 219 -17.499 18.915 30.931 1.00 21.04 C ANISOU 4241 CA ILE B 219 2580 2720 2696 -244 202 -270 C ATOM 4242 C ILE B 219 -16.215 18.268 30.428 1.00 18.70 C ANISOU 4242 C ILE B 219 2302 2403 2401 -242 209 -266 C ATOM 4243 O ILE B 219 -15.853 18.383 29.251 1.00 20.32 O ANISOU 4243 O ILE B 219 2506 2627 2588 -233 195 -280 O ATOM 4244 CB ILE B 219 -17.199 20.137 31.817 1.00 23.29 C ANISOU 4244 CB ILE B 219 2880 3006 2965 -224 195 -231 C ATOM 4245 CG1 ILE B 219 -18.497 20.853 32.200 1.00 21.66 C ANISOU 4245 CG1 ILE B 219 2653 2823 2754 -223 188 -236 C ATOM 4246 CG2 ILE B 219 -16.226 21.074 31.115 1.00 23.17 C ANISOU 4246 CG2 ILE B 219 2877 3003 2922 -200 177 -214 C ATOM 4247 CD1 ILE B 219 -18.299 21.989 33.157 1.00 26.43 C ANISOU 4247 CD1 ILE B 219 3271 3426 3346 -206 184 -204 C ATOM 4248 N PHE B 220 -15.507 17.572 31.313 1.00 23.30 N ANISOU 4248 N PHE B 220 2902 2947 3004 -250 230 -245 N ATOM 4249 CA PHE B 220 -14.235 16.993 30.919 1.00 25.33 C ANISOU 4249 CA PHE B 220 3178 3184 3264 -247 237 -238 C ATOM 4250 C PHE B 220 -14.400 15.757 30.043 1.00 21.02 C ANISOU 4250 C PHE B 220 2620 2630 2736 -265 248 -276 C ATOM 4251 O PHE B 220 -13.467 15.410 29.311 1.00 25.11 O ANISOU 4251 O PHE B 220 3150 3142 3250 -259 248 -279 O ATOM 4252 CB PHE B 220 -13.400 16.700 32.165 1.00 24.40 C ANISOU 4252 CB PHE B 220 3080 3030 3160 -245 255 -202 C ATOM 4253 CG PHE B 220 -12.781 17.934 32.756 1.00 27.62 C ANISOU 4253 CG PHE B 220 3502 3445 3546 -223 241 -168 C ATOM 4254 CD1 PHE B 220 -11.653 18.498 32.179 1.00 33.87 C ANISOU 4254 CD1 PHE B 220 4306 4241 4322 -206 228 -154 C ATOM 4255 CD2 PHE B 220 -13.349 18.560 33.849 1.00 27.81 C ANISOU 4255 CD2 PHE B 220 3526 3474 3568 -219 240 -151 C ATOM 4256 CE1 PHE B 220 -11.085 19.645 32.701 1.00 35.89 C ANISOU 4256 CE1 PHE B 220 4572 4500 4563 -187 215 -126 C ATOM 4257 CE2 PHE B 220 -12.781 19.709 34.382 1.00 33.88 C ANISOU 4257 CE2 PHE B 220 4306 4249 4318 -200 226 -125 C ATOM 4258 CZ PHE B 220 -11.648 20.250 33.805 1.00 34.51 C ANISOU 4258 CZ PHE B 220 4397 4330 4387 -185 213 -113 C ATOM 4259 N PHE B 221 -15.562 15.098 30.077 1.00 21.20 N ANISOU 4259 N PHE B 221 2621 2653 2781 -286 257 -308 N ATOM 4260 CA PHE B 221 -15.841 14.069 29.080 1.00 25.22 C ANISOU 4260 CA PHE B 221 3114 3161 3306 -303 262 -353 C ATOM 4261 C PHE B 221 -15.923 14.684 27.689 1.00 22.60 C ANISOU 4261 C PHE B 221 2773 2874 2940 -288 232 -379 C ATOM 4262 O PHE B 221 -15.281 14.208 26.746 1.00 21.51 O ANISOU 4262 O PHE B 221 2640 2736 2795 -285 231 -397 O ATOM 4263 CB PHE B 221 -17.139 13.330 29.415 1.00 20.51 C ANISOU 4263 CB PHE B 221 2492 2557 2745 -330 276 -384 C ATOM 4264 CG PHE B 221 -17.534 12.292 28.389 1.00 31.79 C ANISOU 4264 CG PHE B 221 3899 3986 4193 -349 280 -439 C ATOM 4265 CD1 PHE B 221 -17.055 10.993 28.477 1.00 34.21 C ANISOU 4265 CD1 PHE B 221 4212 4250 4537 -367 308 -449 C ATOM 4266 CD2 PHE B 221 -18.380 12.616 27.336 1.00 26.11 C ANISOU 4266 CD2 PHE B 221 3154 3310 3455 -349 254 -482 C ATOM 4267 CE1 PHE B 221 -17.407 10.044 27.537 1.00 35.55 C ANISOU 4267 CE1 PHE B 221 4362 4417 4727 -385 311 -503 C ATOM 4268 CE2 PHE B 221 -18.738 11.670 26.395 1.00 25.88 C ANISOU 4268 CE2 PHE B 221 3105 3285 3444 -366 254 -537 C ATOM 4269 CZ PHE B 221 -18.251 10.383 26.493 1.00 31.56 C ANISOU 4269 CZ PHE B 221 3830 3958 4202 -385 283 -550 C ATOM 4270 N CYS B 222 -16.717 15.749 27.546 1.00 21.88 N ANISOU 4270 N CYS B 222 2668 2820 2824 -276 210 -379 N ATOM 4271 CA CYS B 222 -16.864 16.392 26.244 1.00 25.92 C ANISOU 4271 CA CYS B 222 3170 3378 3299 -258 183 -399 C ATOM 4272 C CYS B 222 -15.538 16.966 25.767 1.00 26.60 C ANISOU 4272 C CYS B 222 3282 3466 3359 -233 177 -369 C ATOM 4273 O CYS B 222 -15.203 16.880 24.579 1.00 31.40 O ANISOU 4273 O CYS B 222 3889 4096 3946 -221 167 -388 O ATOM 4274 CB CYS B 222 -17.931 17.484 26.315 1.00 23.09 C ANISOU 4274 CB CYS B 222 2793 3057 2921 -247 163 -397 C ATOM 4275 SG CYS B 222 -19.591 16.898 26.724 1.00 23.29 S ANISOU 4275 SG CYS B 222 2784 3088 2978 -275 168 -436 S ATOM 4276 N TYR B 223 -14.767 17.555 26.680 1.00 21.52 N ANISOU 4276 N TYR B 223 2660 2801 2716 -223 184 -323 N ATOM 4277 CA TYR B 223 -13.451 18.064 26.314 1.00 28.21 C ANISOU 4277 CA TYR B 223 3529 3644 3545 -201 180 -294 C ATOM 4278 C TYR B 223 -12.525 16.936 25.881 1.00 28.13 C ANISOU 4278 C TYR B 223 3530 3609 3549 -209 196 -304 C ATOM 4279 O TYR B 223 -11.808 17.061 24.879 1.00 25.45 O ANISOU 4279 O TYR B 223 3198 3282 3189 -193 190 -306 O ATOM 4280 CB TYR B 223 -12.845 18.833 27.483 1.00 27.42 C ANISOU 4280 CB TYR B 223 3446 3523 3449 -193 184 -248 C ATOM 4281 CG TYR B 223 -11.514 19.450 27.154 1.00 29.47 C ANISOU 4281 CG TYR B 223 3725 3778 3694 -171 181 -217 C ATOM 4282 CD1 TYR B 223 -11.397 20.375 26.126 1.00 32.91 C ANISOU 4282 CD1 TYR B 223 4158 4245 4100 -148 165 -214 C ATOM 4283 CD2 TYR B 223 -10.376 19.111 27.867 1.00 32.12 C ANISOU 4283 CD2 TYR B 223 4080 4078 4047 -173 194 -192 C ATOM 4284 CE1 TYR B 223 -10.182 20.945 25.819 1.00 42.14 C ANISOU 4284 CE1 TYR B 223 5343 5408 5261 -129 166 -185 C ATOM 4285 CE2 TYR B 223 -9.157 19.671 27.567 1.00 36.61 C ANISOU 4285 CE2 TYR B 223 4663 4642 4606 -154 192 -166 C ATOM 4286 CZ TYR B 223 -9.067 20.589 26.545 1.00 41.57 C ANISOU 4286 CZ TYR B 223 5287 5299 5209 -133 179 -162 C ATOM 4287 OH TYR B 223 -7.855 21.155 26.240 1.00 47.34 O ANISOU 4287 OH TYR B 223 6030 6022 5935 -115 180 -135 O ATOM 4288 N GLY B 224 -12.532 15.824 26.621 1.00 24.89 N ANISOU 4288 N GLY B 224 3122 3161 3173 -232 218 -311 N ATOM 4289 CA GLY B 224 -11.688 14.698 26.258 1.00 22.99 C ANISOU 4289 CA GLY B 224 2892 2894 2950 -240 236 -321 C ATOM 4290 C GLY B 224 -11.999 14.169 24.872 1.00 30.93 C ANISOU 4290 C GLY B 224 3884 3923 3946 -242 229 -369 C ATOM 4291 O GLY B 224 -11.094 13.817 24.112 1.00 34.72 O ANISOU 4291 O GLY B 224 4375 4399 4418 -233 232 -373 O ATOM 4292 N GLN B 225 -13.286 14.111 24.523 1.00 26.57 N ANISOU 4292 N GLN B 225 3306 3398 3392 -253 217 -407 N ATOM 4293 CA GLN B 225 -13.673 13.738 23.169 1.00 29.57 C ANISOU 4293 CA GLN B 225 3670 3810 3756 -252 205 -457 C ATOM 4294 C GLN B 225 -13.206 14.766 22.147 1.00 30.90 C ANISOU 4294 C GLN B 225 3845 4019 3875 -218 183 -445 C ATOM 4295 O GLN B 225 -12.883 14.402 21.012 1.00 38.83 O ANISOU 4295 O GLN B 225 4850 5043 4862 -209 179 -472 O ATOM 4296 CB GLN B 225 -15.188 13.553 23.094 1.00 27.34 C ANISOU 4296 CB GLN B 225 3356 3550 3484 -269 195 -500 C ATOM 4297 CG GLN B 225 -15.700 12.344 23.865 1.00 31.08 C ANISOU 4297 CG GLN B 225 3818 3981 4009 -304 221 -521 C ATOM 4298 CD GLN B 225 -15.345 11.026 23.196 1.00 35.20 C ANISOU 4298 CD GLN B 225 4337 4481 4554 -319 236 -562 C ATOM 4299 OE1 GLN B 225 -14.605 10.214 23.749 1.00 41.68 O ANISOU 4299 OE1 GLN B 225 5176 5255 5408 -330 264 -546 O ATOM 4300 NE2 GLN B 225 -15.877 10.809 22.002 1.00 36.71 N ANISOU 4300 NE2 GLN B 225 4508 4709 4730 -319 218 -616 N ATOM 4301 N LEU B 226 -13.169 16.048 22.522 1.00 29.64 N ANISOU 4301 N LEU B 226 3692 3875 3695 -199 171 -405 N ATOM 4302 CA LEU B 226 -12.664 17.079 21.616 1.00 31.57 C ANISOU 4302 CA LEU B 226 3945 4155 3898 -165 156 -386 C ATOM 4303 C LEU B 226 -11.181 16.887 21.318 1.00 31.68 C ANISOU 4303 C LEU B 226 3982 4146 3909 -154 169 -362 C ATOM 4304 O LEU B 226 -10.747 17.029 20.170 1.00 40.37 O ANISOU 4304 O LEU B 226 5087 5273 4981 -133 163 -369 O ATOM 4305 CB LEU B 226 -12.888 18.469 22.213 1.00 37.00 C ANISOU 4305 CB LEU B 226 4633 4854 4572 -149 145 -345 C ATOM 4306 CG LEU B 226 -14.257 19.137 22.112 1.00 36.81 C ANISOU 4306 CG LEU B 226 4586 4869 4532 -145 125 -360 C ATOM 4307 CD1 LEU B 226 -14.102 20.639 22.309 1.00 39.41 C ANISOU 4307 CD1 LEU B 226 4921 5212 4840 -118 116 -316 C ATOM 4308 CD2 LEU B 226 -14.890 18.836 20.775 1.00 35.02 C ANISOU 4308 CD2 LEU B 226 4339 4688 4279 -137 109 -406 C ATOM 4309 N VAL B 227 -10.385 16.591 22.347 1.00 30.03 N ANISOU 4309 N VAL B 227 3790 3891 3730 -164 187 -332 N ATOM 4310 CA VAL B 227 -8.935 16.561 22.186 1.00 33.18 C ANISOU 4310 CA VAL B 227 4211 4268 4129 -151 199 -304 C ATOM 4311 C VAL B 227 -8.496 15.320 21.419 1.00 39.10 C ANISOU 4311 C VAL B 227 4963 5007 4887 -159 212 -337 C ATOM 4312 O VAL B 227 -7.653 15.401 20.518 1.00 39.86 O ANISOU 4312 O VAL B 227 5068 5112 4963 -140 214 -332 O ATOM 4313 CB VAL B 227 -8.248 16.654 23.560 1.00 33.37 C ANISOU 4313 CB VAL B 227 4249 4250 4181 -158 212 -263 C ATOM 4314 CG1 VAL B 227 -6.770 16.316 23.438 1.00 31.54 C ANISOU 4314 CG1 VAL B 227 4036 3991 3956 -150 226 -241 C ATOM 4315 CG2 VAL B 227 -8.430 18.045 24.149 1.00 35.65 C ANISOU 4315 CG2 VAL B 227 4537 4551 4456 -145 198 -230 C ATOM 4316 N PHE B 228 -9.041 14.157 21.762 1.00 34.76 N ANISOU 4316 N PHE B 228 4404 4435 4368 -186 224 -370 N ATOM 4317 CA PHE B 228 -8.659 12.912 21.093 1.00 40.78 C ANISOU 4317 CA PHE B 228 5168 5182 5143 -196 239 -405 C ATOM 4318 C PHE B 228 -9.602 12.566 19.942 1.00 51.46 C ANISOU 4318 C PHE B 228 6501 6575 6478 -198 225 -463 C ATOM 4319 O PHE B 228 -10.082 11.439 19.829 1.00 58.03 O ANISOU 4319 O PHE B 228 7320 7392 7336 -222 234 -508 O ATOM 4320 CB PHE B 228 -8.597 11.779 22.111 1.00 44.84 C ANISOU 4320 CB PHE B 228 5686 5645 5707 -224 264 -406 C ATOM 4321 N THR B 229 -9.844 13.529 19.055 1.00 59.55 N ANISOU 4321 N THR B 229 7519 7650 7457 -173 202 -464 N ATOM 4322 CA THR B 229 -10.680 13.314 17.875 1.00 61.61 C ANISOU 4322 CA THR B 229 7761 7958 7692 -168 184 -518 C ATOM 4323 C THR B 229 -10.585 14.502 16.921 1.00 67.48 C ANISOU 4323 C THR B 229 8506 8754 8380 -130 164 -501 C ATOM 4324 O THR B 229 -11.122 15.578 17.194 1.00 68.67 O ANISOU 4324 O THR B 229 8650 8927 8513 -118 149 -477 O ATOM 4325 CB THR B 229 -12.160 13.089 18.245 1.00 57.55 C ANISOU 4325 CB THR B 229 7218 7454 7194 -192 173 -555 C ATOM 4326 N GLN B 244 -15.423 26.808 10.549 1.00 40.49 N ANISOU 4326 N GLN B 244 5011 5853 4522 264 6 -271 N ATOM 4327 CA GLN B 244 -14.168 26.187 10.972 1.00 48.97 C ANISOU 4327 CA GLN B 244 6108 6868 5629 238 30 -262 C ATOM 4328 C GLN B 244 -13.337 27.166 11.793 1.00 41.90 C ANISOU 4328 C GLN B 244 5232 5921 4767 239 53 -197 C ATOM 4329 O GLN B 244 -13.016 26.907 12.954 1.00 41.48 O ANISOU 4329 O GLN B 244 5186 5813 4762 202 62 -193 O ATOM 4330 CB GLN B 244 -13.368 25.701 9.761 1.00 51.63 C ANISOU 4330 CB GLN B 244 6458 7230 5929 264 38 -270 C ATOM 4331 N LYS B 245 -12.969 28.287 11.171 1.00 44.30 N ANISOU 4331 N LYS B 245 5543 6244 5044 284 64 -147 N ATOM 4332 CA LYS B 245 -12.350 29.372 11.924 1.00 41.62 C ANISOU 4332 CA LYS B 245 5217 5860 4739 287 84 -88 C ATOM 4333 C LYS B 245 -13.361 30.029 12.853 1.00 34.95 C ANISOU 4333 C LYS B 245 4357 5009 3915 275 71 -84 C ATOM 4334 O LYS B 245 -13.021 30.422 13.975 1.00 35.07 O ANISOU 4334 O LYS B 245 4378 4972 3973 253 82 -61 O ATOM 4335 CB LYS B 245 -11.744 30.397 10.965 1.00 42.19 C ANISOU 4335 CB LYS B 245 5299 5952 4780 339 102 -36 C ATOM 4336 CG LYS B 245 -10.953 31.500 11.648 1.00 52.73 C ANISOU 4336 CG LYS B 245 6646 7235 6154 342 126 24 C ATOM 4337 CD LYS B 245 -10.379 32.474 10.632 1.00 48.09 C ANISOU 4337 CD LYS B 245 6066 6667 5539 394 148 77 C ATOM 4338 N ALA B 246 -14.611 30.154 12.402 1.00 38.84 N ANISOU 4338 N ALA B 246 4827 5555 4375 291 48 -108 N ATOM 4339 CA ALA B 246 -15.660 30.698 13.258 1.00 37.39 C ANISOU 4339 CA ALA B 246 4627 5369 4210 279 36 -109 C ATOM 4340 C ALA B 246 -16.015 29.742 14.388 1.00 34.83 C ANISOU 4340 C ALA B 246 4296 5009 3926 226 29 -149 C ATOM 4341 O ALA B 246 -16.343 30.187 15.493 1.00 29.63 O ANISOU 4341 O ALA B 246 3636 4320 3301 207 31 -136 O ATOM 4342 CB ALA B 246 -16.900 31.027 12.429 1.00 32.91 C ANISOU 4342 CB ALA B 246 4036 4872 3597 312 12 -125 C ATOM 4343 N GLU B 247 -15.971 28.432 14.132 1.00 34.03 N ANISOU 4343 N GLU B 247 4193 4913 3823 202 22 -198 N ATOM 4344 CA GLU B 247 -16.204 27.474 15.206 1.00 35.16 C ANISOU 4344 CA GLU B 247 4333 5018 4010 152 22 -231 C ATOM 4345 C GLU B 247 -15.028 27.422 16.171 1.00 31.45 C ANISOU 4345 C GLU B 247 3887 4481 3581 129 45 -201 C ATOM 4346 O GLU B 247 -15.225 27.239 17.378 1.00 27.32 O ANISOU 4346 O GLU B 247 3364 3920 3096 97 48 -204 O ATOM 4347 CB GLU B 247 -16.481 26.081 14.638 1.00 34.63 C ANISOU 4347 CB GLU B 247 4254 4969 3932 133 11 -292 C ATOM 4348 CG GLU B 247 -17.777 25.951 13.849 1.00 38.07 C ANISOU 4348 CG GLU B 247 4660 5470 4334 147 -16 -335 C ATOM 4349 CD GLU B 247 -19.031 26.147 14.692 1.00 37.81 C ANISOU 4349 CD GLU B 247 4603 5440 4323 127 -29 -350 C ATOM 4350 OE1 GLU B 247 -18.925 26.403 15.911 1.00 35.87 O ANISOU 4350 OE1 GLU B 247 4366 5146 4118 104 -17 -326 O ATOM 4351 OE2 GLU B 247 -20.137 26.039 14.123 1.00 39.92 O ANISOU 4351 OE2 GLU B 247 4842 5759 4566 137 -53 -387 O ATOM 4352 N LYS B 248 -13.806 27.581 15.660 1.00 30.10 N ANISOU 4352 N LYS B 248 3736 4296 3402 147 61 -172 N ATOM 4353 CA LYS B 248 -12.633 27.566 16.527 1.00 29.25 C ANISOU 4353 CA LYS B 248 3650 4129 3334 128 82 -144 C ATOM 4354 C LYS B 248 -12.669 28.722 17.523 1.00 24.54 C ANISOU 4354 C LYS B 248 3055 3505 2763 129 87 -104 C ATOM 4355 O LYS B 248 -12.309 28.552 18.693 1.00 23.62 O ANISOU 4355 O LYS B 248 2947 3344 2685 101 94 -99 O ATOM 4356 CB LYS B 248 -11.361 27.613 15.679 1.00 28.22 C ANISOU 4356 CB LYS B 248 3538 3995 3190 151 99 -119 C ATOM 4357 CG LYS B 248 -10.180 26.847 16.258 1.00 30.70 C ANISOU 4357 CG LYS B 248 3870 4257 3539 124 116 -117 C ATOM 4358 CD LYS B 248 -8.954 27.018 15.375 1.00 31.86 C ANISOU 4358 CD LYS B 248 4031 4401 3671 151 134 -89 C ATOM 4359 CE LYS B 248 -8.621 28.496 15.219 1.00 35.76 C ANISOU 4359 CE LYS B 248 4529 4896 4162 183 145 -35 C ATOM 4360 NZ LYS B 248 -7.788 28.775 14.014 1.00 39.81 N ANISOU 4360 NZ LYS B 248 5052 5427 4648 220 161 -9 N ATOM 4361 N GLU B 249 -13.117 29.902 17.083 1.00 24.13 N ANISOU 4361 N GLU B 249 2997 3482 2691 163 83 -77 N ATOM 4362 CA GLU B 249 -13.182 31.052 17.982 1.00 23.43 C ANISOU 4362 CA GLU B 249 2909 3367 2627 165 89 -42 C ATOM 4363 C GLU B 249 -14.139 30.808 19.145 1.00 23.51 C ANISOU 4363 C GLU B 249 2907 3365 2660 134 77 -66 C ATOM 4364 O GLU B 249 -13.918 31.323 20.246 1.00 22.78 O ANISOU 4364 O GLU B 249 2820 3234 2599 121 84 -47 O ATOM 4365 CB GLU B 249 -13.600 32.308 17.213 1.00 25.59 C ANISOU 4365 CB GLU B 249 3175 3675 2873 210 88 -10 C ATOM 4366 CG GLU B 249 -13.521 33.594 18.037 1.00 27.56 C ANISOU 4366 CG GLU B 249 3426 3893 3152 216 98 29 C ATOM 4367 CD GLU B 249 -14.398 34.710 17.490 1.00 27.11 C ANISOU 4367 CD GLU B 249 3356 3874 3071 254 94 51 C ATOM 4368 OE1 GLU B 249 -15.521 34.415 17.025 1.00 30.70 O ANISOU 4368 OE1 GLU B 249 3793 4376 3496 262 75 23 O ATOM 4369 OE2 GLU B 249 -13.967 35.883 17.525 1.00 26.92 O ANISOU 4369 OE2 GLU B 249 3337 3830 3060 277 110 95 O ATOM 4370 N VAL B 250 -15.209 30.044 18.921 1.00 19.40 N ANISOU 4370 N VAL B 250 2369 2878 2125 123 60 -109 N ATOM 4371 CA VAL B 250 -16.150 29.747 19.997 1.00 24.97 C ANISOU 4371 CA VAL B 250 3062 3572 2853 94 52 -132 C ATOM 4372 C VAL B 250 -15.583 28.696 20.942 1.00 23.88 C ANISOU 4372 C VAL B 250 2935 3388 2749 54 62 -148 C ATOM 4373 O VAL B 250 -15.686 28.825 22.167 1.00 18.26 O ANISOU 4373 O VAL B 250 2227 2645 2067 34 67 -141 O ATOM 4374 CB VAL B 250 -17.509 29.314 19.418 1.00 22.47 C ANISOU 4374 CB VAL B 250 2718 3306 2513 95 32 -174 C ATOM 4375 CG1 VAL B 250 -18.487 28.984 20.550 1.00 22.63 C ANISOU 4375 CG1 VAL B 250 2724 3313 2561 63 27 -196 C ATOM 4376 CG2 VAL B 250 -18.066 30.412 18.528 1.00 22.72 C ANISOU 4376 CG2 VAL B 250 2738 3385 2508 138 22 -154 C ATOM 4377 N THR B 251 -14.994 27.628 20.397 1.00 18.77 N ANISOU 4377 N THR B 251 2295 2738 2098 44 66 -169 N ATOM 4378 CA THR B 251 -14.378 26.625 21.260 1.00 21.88 C ANISOU 4378 CA THR B 251 2700 3087 2524 10 78 -179 C ATOM 4379 C THR B 251 -13.287 27.248 22.124 1.00 21.44 C ANISOU 4379 C THR B 251 2665 2988 2494 10 92 -138 C ATOM 4380 O THR B 251 -13.125 26.885 23.294 1.00 17.93 O ANISOU 4380 O THR B 251 2227 2508 2078 -15 99 -137 O ATOM 4381 CB THR B 251 -13.810 25.475 20.426 1.00 21.90 C ANISOU 4381 CB THR B 251 2708 3093 2519 4 82 -205 C ATOM 4382 OG1 THR B 251 -14.811 24.997 19.516 1.00 23.96 O ANISOU 4382 OG1 THR B 251 2948 3400 2754 8 67 -247 O ATOM 4383 CG2 THR B 251 -13.379 24.327 21.329 1.00 19.27 C ANISOU 4383 CG2 THR B 251 2385 2716 2222 -32 95 -220 C ATOM 4384 N ARG B 252 -12.541 28.204 21.573 1.00 20.35 N ANISOU 4384 N ARG B 252 2536 2852 2344 38 98 -103 N ATOM 4385 CA ARG B 252 -11.486 28.837 22.353 1.00 21.11 C ANISOU 4385 CA ARG B 252 2649 2907 2467 38 110 -67 C ATOM 4386 C ARG B 252 -12.047 29.633 23.525 1.00 18.51 C ANISOU 4386 C ARG B 252 2314 2562 2156 32 106 -56 C ATOM 4387 O ARG B 252 -11.441 29.663 24.600 1.00 22.16 O ANISOU 4387 O ARG B 252 2786 2987 2645 17 112 -45 O ATOM 4388 CB ARG B 252 -10.633 29.718 21.452 1.00 17.56 C ANISOU 4388 CB ARG B 252 2206 2462 2005 70 119 -33 C ATOM 4389 CG ARG B 252 -9.764 28.895 20.524 1.00 22.85 C ANISOU 4389 CG ARG B 252 2885 3134 2662 74 127 -40 C ATOM 4390 CD ARG B 252 -9.039 29.760 19.530 1.00 25.88 C ANISOU 4390 CD ARG B 252 3275 3529 3031 110 138 -5 C ATOM 4391 NE ARG B 252 -8.009 28.999 18.837 1.00 22.25 N ANISOU 4391 NE ARG B 252 2826 3062 2565 112 150 -7 N ATOM 4392 CZ ARG B 252 -7.058 29.540 18.090 1.00 25.89 C ANISOU 4392 CZ ARG B 252 3295 3521 3021 138 166 26 C ATOM 4393 NH1 ARG B 252 -6.985 30.849 17.904 1.00 24.41 N ANISOU 4393 NH1 ARG B 252 3106 3336 2835 164 174 63 N ATOM 4394 NH2 ARG B 252 -6.155 28.748 17.519 1.00 29.49 N ANISOU 4394 NH2 ARG B 252 3761 3971 3473 137 178 20 N ATOM 4395 N MET B 253 -13.192 30.295 23.335 1.00 19.14 N ANISOU 4395 N MET B 253 2379 2673 2221 45 96 -60 N ATOM 4396 CA MET B 253 -13.781 31.077 24.419 1.00 20.90 C ANISOU 4396 CA MET B 253 2597 2884 2461 41 93 -50 C ATOM 4397 C MET B 253 -14.337 30.177 25.515 1.00 19.99 C ANISOU 4397 C MET B 253 2478 2754 2363 8 91 -77 C ATOM 4398 O MET B 253 -14.212 30.492 26.703 1.00 21.47 O ANISOU 4398 O MET B 253 2672 2914 2572 -3 95 -67 O ATOM 4399 CB MET B 253 -14.872 32.002 23.876 1.00 17.43 C ANISOU 4399 CB MET B 253 2140 2482 2000 66 84 -46 C ATOM 4400 CG MET B 253 -15.536 32.872 24.952 1.00 19.75 C ANISOU 4400 CG MET B 253 2428 2764 2310 64 82 -37 C ATOM 4401 SD MET B 253 -16.759 34.041 24.319 1.00 21.20 S ANISOU 4401 SD MET B 253 2592 2991 2473 97 73 -27 S ATOM 4402 CE MET B 253 -17.766 34.255 25.784 1.00 17.22 C ANISOU 4402 CE MET B 253 2078 2473 1990 77 70 -39 C ATOM 4403 N VAL B 254 -14.952 29.052 25.135 1.00 21.41 N ANISOU 4403 N VAL B 254 2648 2952 2534 -7 86 -111 N ATOM 4404 CA VAL B 254 -15.507 28.138 26.128 1.00 20.49 C ANISOU 4404 CA VAL B 254 2528 2821 2437 -38 89 -134 C ATOM 4405 C VAL B 254 -14.404 27.537 26.989 1.00 24.88 C ANISOU 4405 C VAL B 254 3104 3333 3017 -56 102 -124 C ATOM 4406 O VAL B 254 -14.598 27.306 28.189 1.00 19.52 O ANISOU 4406 O VAL B 254 2427 2632 2357 -73 108 -124 O ATOM 4407 CB VAL B 254 -16.348 27.048 25.436 1.00 23.41 C ANISOU 4407 CB VAL B 254 2880 3216 2797 -51 83 -175 C ATOM 4408 CG1 VAL B 254 -16.827 26.020 26.454 1.00 26.19 C ANISOU 4408 CG1 VAL B 254 3229 3547 3176 -84 91 -196 C ATOM 4409 CG2 VAL B 254 -17.529 27.681 24.723 1.00 21.92 C ANISOU 4409 CG2 VAL B 254 2668 3074 2584 -32 67 -186 C ATOM 4410 N ILE B 255 -13.233 27.279 26.403 1.00 23.43 N ANISOU 4410 N ILE B 255 2933 3137 2831 -50 108 -114 N ATOM 4411 CA ILE B 255 -12.106 26.772 27.183 1.00 23.08 C ANISOU 4411 CA ILE B 255 2907 3053 2809 -63 120 -102 C ATOM 4412 C ILE B 255 -11.708 27.772 28.264 1.00 19.61 C ANISOU 4412 C ILE B 255 2475 2592 2384 -58 120 -74 C ATOM 4413 O ILE B 255 -11.476 27.397 29.420 1.00 21.87 O ANISOU 4413 O ILE B 255 2769 2853 2688 -73 125 -72 O ATOM 4414 CB ILE B 255 -10.926 26.442 26.247 1.00 21.15 C ANISOU 4414 CB ILE B 255 2673 2803 2559 -54 126 -94 C ATOM 4415 CG1 ILE B 255 -11.267 25.233 25.376 1.00 21.38 C ANISOU 4415 CG1 ILE B 255 2697 2849 2579 -64 127 -127 C ATOM 4416 CG2 ILE B 255 -9.653 26.195 27.047 1.00 22.60 C ANISOU 4416 CG2 ILE B 255 2874 2947 2766 -62 136 -75 C ATOM 4417 CD1 ILE B 255 -10.203 24.885 24.359 1.00 26.30 C ANISOU 4417 CD1 ILE B 255 3329 3470 3192 -53 134 -123 C ATOM 4418 N ILE B 256 -11.626 29.058 27.910 1.00 16.95 N ANISOU 4418 N ILE B 256 2136 2264 2040 -35 116 -54 N ATOM 4419 CA ILE B 256 -11.250 30.080 28.883 1.00 17.92 C ANISOU 4419 CA ILE B 256 2264 2365 2179 -30 116 -32 C ATOM 4420 C ILE B 256 -12.354 30.273 29.921 1.00 17.67 C ANISOU 4420 C ILE B 256 2225 2338 2151 -39 111 -43 C ATOM 4421 O ILE B 256 -12.079 30.539 31.098 1.00 19.70 O ANISOU 4421 O ILE B 256 2489 2573 2423 -45 112 -36 O ATOM 4422 CB ILE B 256 -10.907 31.399 28.163 1.00 17.68 C ANISOU 4422 CB ILE B 256 2231 2340 2144 -3 115 -8 C ATOM 4423 CG1 ILE B 256 -9.727 31.189 27.207 1.00 22.21 C ANISOU 4423 CG1 ILE B 256 2814 2908 2717 7 123 5 C ATOM 4424 CG2 ILE B 256 -10.591 32.505 29.156 1.00 22.56 C ANISOU 4424 CG2 ILE B 256 2853 2936 2784 2 116 9 C ATOM 4425 CD1 ILE B 256 -8.475 30.669 27.877 1.00 17.08 C ANISOU 4425 CD1 ILE B 256 2177 2224 2090 -7 130 11 C ATOM 4426 N MET B 257 -13.617 30.148 29.505 1.00 16.31 N ANISOU 4426 N MET B 257 2038 2196 1965 -39 106 -60 N ATOM 4427 CA MET B 257 -14.722 30.254 30.455 1.00 16.33 C ANISOU 4427 CA MET B 257 2030 2202 1971 -48 104 -71 C ATOM 4428 C MET B 257 -14.648 29.168 31.523 1.00 21.13 C ANISOU 4428 C MET B 257 2646 2789 2594 -72 112 -81 C ATOM 4429 O MET B 257 -14.967 29.413 32.693 1.00 18.10 O ANISOU 4429 O MET B 257 2265 2395 2218 -77 115 -78 O ATOM 4430 CB MET B 257 -16.065 30.176 29.728 1.00 19.96 C ANISOU 4430 CB MET B 257 2470 2699 2414 -45 96 -91 C ATOM 4431 CG MET B 257 -16.388 31.380 28.867 1.00 17.16 C ANISOU 4431 CG MET B 257 2106 2371 2045 -16 88 -77 C ATOM 4432 SD MET B 257 -17.948 31.146 28.005 1.00 23.38 S ANISOU 4432 SD MET B 257 2866 3206 2810 -12 77 -104 S ATOM 4433 CE MET B 257 -19.114 31.214 29.356 1.00 16.91 C ANISOU 4433 CE MET B 257 2036 2383 2007 -28 79 -115 C ATOM 4434 N VAL B 258 -14.266 27.951 31.138 1.00 20.29 N ANISOU 4434 N VAL B 258 2544 2677 2490 -87 118 -94 N ATOM 4435 CA VAL B 258 -14.149 26.893 32.134 1.00 18.83 C ANISOU 4435 CA VAL B 258 2366 2468 2319 -107 130 -100 C ATOM 4436 C VAL B 258 -12.959 27.154 33.051 1.00 20.57 C ANISOU 4436 C VAL B 258 2606 2661 2551 -104 133 -77 C ATOM 4437 O VAL B 258 -13.067 27.020 34.277 1.00 19.54 O ANISOU 4437 O VAL B 258 2481 2517 2428 -110 139 -73 O ATOM 4438 CB VAL B 258 -14.056 25.519 31.452 1.00 20.00 C ANISOU 4438 CB VAL B 258 2512 2614 2471 -123 138 -119 C ATOM 4439 CG1 VAL B 258 -13.698 24.448 32.482 1.00 21.78 C ANISOU 4439 CG1 VAL B 258 2749 2811 2716 -141 154 -118 C ATOM 4440 CG2 VAL B 258 -15.370 25.185 30.774 1.00 18.60 C ANISOU 4440 CG2 VAL B 258 2313 2466 2287 -130 134 -148 C ATOM 4441 N ILE B 259 -11.817 27.556 32.476 1.00 18.06 N ANISOU 4441 N ILE B 259 2296 2334 2232 -92 130 -62 N ATOM 4442 CA ILE B 259 -10.630 27.854 33.279 1.00 19.12 C ANISOU 4442 CA ILE B 259 2444 2442 2378 -88 131 -44 C ATOM 4443 C ILE B 259 -10.922 28.967 34.277 1.00 19.34 C ANISOU 4443 C ILE B 259 2470 2469 2408 -80 124 -36 C ATOM 4444 O ILE B 259 -10.560 28.874 35.456 1.00 18.24 O ANISOU 4444 O ILE B 259 2340 2314 2276 -83 126 -31 O ATOM 4445 CB ILE B 259 -9.443 28.219 32.370 1.00 17.02 C ANISOU 4445 CB ILE B 259 2183 2169 2114 -76 130 -30 C ATOM 4446 CG1 ILE B 259 -8.918 26.979 31.654 1.00 21.27 C ANISOU 4446 CG1 ILE B 259 2726 2702 2652 -84 138 -37 C ATOM 4447 CG2 ILE B 259 -8.324 28.877 33.186 1.00 18.81 C ANISOU 4447 CG2 ILE B 259 2418 2373 2356 -69 127 -12 C ATOM 4448 CD1 ILE B 259 -7.847 27.286 30.628 1.00 22.13 C ANISOU 4448 CD1 ILE B 259 2839 2808 2761 -71 139 -24 C ATOM 4449 N ALA B 260 -11.580 30.036 33.820 1.00 21.42 N ANISOU 4449 N ALA B 260 2724 2749 2665 -67 118 -35 N ATOM 4450 CA ALA B 260 -11.911 31.142 34.715 1.00 24.71 C ANISOU 4450 CA ALA B 260 3139 3165 3086 -58 112 -30 C ATOM 4451 C ALA B 260 -12.827 30.683 35.843 1.00 18.35 C ANISOU 4451 C ALA B 260 2332 2362 2278 -69 116 -41 C ATOM 4452 O ALA B 260 -12.683 31.123 36.991 1.00 20.30 O ANISOU 4452 O ALA B 260 2586 2600 2530 -66 115 -38 O ATOM 4453 CB ALA B 260 -12.558 32.278 33.923 1.00 19.76 C ANISOU 4453 CB ALA B 260 2499 2554 2453 -42 107 -26 C ATOM 4454 N PHE B 261 -13.778 29.799 35.531 1.00 20.04 N ANISOU 4454 N PHE B 261 2538 2590 2486 -81 122 -55 N ATOM 4455 CA PHE B 261 -14.668 29.264 36.557 1.00 20.12 C ANISOU 4455 CA PHE B 261 2546 2603 2497 -92 130 -64 C ATOM 4456 C PHE B 261 -13.889 28.476 37.605 1.00 22.64 C ANISOU 4456 C PHE B 261 2880 2899 2821 -100 139 -57 C ATOM 4457 O PHE B 261 -14.173 28.574 38.804 1.00 21.93 O ANISOU 4457 O PHE B 261 2795 2806 2730 -99 143 -54 O ATOM 4458 CB PHE B 261 -15.745 28.389 35.905 1.00 19.99 C ANISOU 4458 CB PHE B 261 2514 2603 2478 -106 136 -82 C ATOM 4459 CG PHE B 261 -16.753 27.820 36.875 1.00 18.74 C ANISOU 4459 CG PHE B 261 2350 2446 2324 -118 148 -91 C ATOM 4460 CD1 PHE B 261 -16.521 26.610 37.505 1.00 16.30 C ANISOU 4460 CD1 PHE B 261 2049 2118 2025 -133 164 -91 C ATOM 4461 CD2 PHE B 261 -17.940 28.488 37.135 1.00 20.24 C ANISOU 4461 CD2 PHE B 261 2525 2654 2510 -114 146 -97 C ATOM 4462 CE1 PHE B 261 -17.446 26.081 38.394 1.00 21.56 C ANISOU 4462 CE1 PHE B 261 2710 2785 2698 -143 180 -95 C ATOM 4463 CE2 PHE B 261 -18.871 27.964 38.029 1.00 23.28 C ANISOU 4463 CE2 PHE B 261 2904 3039 2902 -124 161 -103 C ATOM 4464 CZ PHE B 261 -18.620 26.758 38.655 1.00 20.52 C ANISOU 4464 CZ PHE B 261 2564 2671 2562 -139 178 -102 C ATOM 4465 N LEU B 262 -12.915 27.671 37.173 1.00 18.33 N ANISOU 4465 N LEU B 262 2344 2340 2282 -105 142 -53 N ATOM 4466 CA LEU B 262 -12.126 26.904 38.133 1.00 20.57 C ANISOU 4466 CA LEU B 262 2642 2604 2571 -109 151 -43 C ATOM 4467 C LEU B 262 -11.290 27.820 39.020 1.00 24.22 C ANISOU 4467 C LEU B 262 3113 3057 3031 -95 140 -31 C ATOM 4468 O LEU B 262 -11.200 27.605 40.234 1.00 20.41 O ANISOU 4468 O LEU B 262 2639 2570 2546 -93 144 -26 O ATOM 4469 CB LEU B 262 -11.236 25.897 37.408 1.00 17.81 C ANISOU 4469 CB LEU B 262 2299 2241 2229 -117 157 -42 C ATOM 4470 CG LEU B 262 -12.008 24.746 36.766 1.00 27.50 C ANISOU 4470 CG LEU B 262 3517 3472 3460 -134 170 -58 C ATOM 4471 CD1 LEU B 262 -11.112 23.926 35.838 1.00 27.01 C ANISOU 4471 CD1 LEU B 262 3459 3398 3404 -138 174 -60 C ATOM 4472 CD2 LEU B 262 -12.620 23.866 37.838 1.00 25.00 C ANISOU 4472 CD2 LEU B 262 3202 3147 3150 -144 188 -58 C ATOM 4473 N ILE B 263 -10.679 28.853 38.433 1.00 21.68 N ANISOU 4473 N ILE B 263 2789 2735 2713 -84 128 -27 N ATOM 4474 CA ILE B 263 -9.908 29.812 39.222 1.00 24.97 C ANISOU 4474 CA ILE B 263 3211 3143 3134 -72 117 -21 C ATOM 4475 C ILE B 263 -10.796 30.487 40.262 1.00 21.48 C ANISOU 4475 C ILE B 263 2766 2710 2684 -66 114 -28 C ATOM 4476 O ILE B 263 -10.373 30.739 41.396 1.00 23.50 O ANISOU 4476 O ILE B 263 3029 2961 2937 -59 110 -27 O ATOM 4477 CB ILE B 263 -9.242 30.845 38.294 1.00 20.21 C ANISOU 4477 CB ILE B 263 2603 2536 2541 -62 108 -16 C ATOM 4478 CG1 ILE B 263 -8.138 30.197 37.462 1.00 26.45 C ANISOU 4478 CG1 ILE B 263 3398 3314 3339 -65 111 -8 C ATOM 4479 CG2 ILE B 263 -8.700 32.022 39.085 1.00 19.80 C ANISOU 4479 CG2 ILE B 263 2551 2474 2498 -51 97 -15 C ATOM 4480 CD1 ILE B 263 -7.665 31.057 36.311 1.00 23.13 C ANISOU 4480 CD1 ILE B 263 2971 2892 2927 -56 108 0 C ATOM 4481 N CYS B 264 -12.040 30.789 39.891 1.00 21.54 N ANISOU 4481 N CYS B 264 2763 2734 2686 -68 118 -35 N ATOM 4482 CA CYS B 264 -12.915 31.565 40.763 1.00 21.55 C ANISOU 4482 CA CYS B 264 2761 2745 2682 -60 116 -41 C ATOM 4483 C CYS B 264 -13.460 30.730 41.917 1.00 18.31 C ANISOU 4483 C CYS B 264 2357 2338 2262 -66 128 -42 C ATOM 4484 O CYS B 264 -13.592 31.228 43.040 1.00 24.41 O ANISOU 4484 O CYS B 264 3134 3113 3028 -56 126 -44 O ATOM 4485 CB CYS B 264 -14.057 32.162 39.937 1.00 20.13 C ANISOU 4485 CB CYS B 264 2566 2582 2501 -58 116 -47 C ATOM 4486 SG CYS B 264 -15.252 33.150 40.849 1.00 27.34 S ANISOU 4486 SG CYS B 264 3472 3508 3408 -48 116 -54 S ATOM 4487 N TRP B 265 -13.795 29.463 41.668 1.00 20.29 N ANISOU 4487 N TRP B 265 2607 2589 2513 -80 142 -42 N ATOM 4488 CA TRP B 265 -14.571 28.693 42.631 1.00 19.32 C ANISOU 4488 CA TRP B 265 2486 2469 2385 -85 158 -42 C ATOM 4489 C TRP B 265 -13.810 27.569 43.320 1.00 24.52 C ANISOU 4489 C TRP B 265 3160 3115 3043 -88 170 -30 C ATOM 4490 O TRP B 265 -14.262 27.106 44.373 1.00 24.83 O ANISOU 4490 O TRP B 265 3204 3155 3075 -86 184 -24 O ATOM 4491 CB TRP B 265 -15.824 28.103 41.957 1.00 21.11 C ANISOU 4491 CB TRP B 265 2698 2707 2617 -100 171 -52 C ATOM 4492 CG TRP B 265 -16.880 29.132 41.663 1.00 22.11 C ANISOU 4492 CG TRP B 265 2809 2852 2741 -94 164 -61 C ATOM 4493 CD1 TRP B 265 -17.107 29.759 40.466 1.00 21.95 C ANISOU 4493 CD1 TRP B 265 2776 2842 2722 -92 152 -68 C ATOM 4494 CD2 TRP B 265 -17.842 29.669 42.583 1.00 20.74 C ANISOU 4494 CD2 TRP B 265 2631 2690 2562 -87 169 -64 C ATOM 4495 NE1 TRP B 265 -18.154 30.642 40.586 1.00 24.06 N ANISOU 4495 NE1 TRP B 265 3030 3126 2986 -84 149 -74 N ATOM 4496 CE2 TRP B 265 -18.618 30.609 41.876 1.00 22.69 C ANISOU 4496 CE2 TRP B 265 2862 2952 2808 -82 160 -72 C ATOM 4497 CE3 TRP B 265 -18.122 29.445 43.935 1.00 22.86 C ANISOU 4497 CE3 TRP B 265 2908 2957 2823 -83 182 -59 C ATOM 4498 CZ2 TRP B 265 -19.657 31.323 42.475 1.00 19.26 C ANISOU 4498 CZ2 TRP B 265 2418 2530 2370 -74 163 -77 C ATOM 4499 CZ3 TRP B 265 -19.152 30.159 44.529 1.00 21.68 C ANISOU 4499 CZ3 TRP B 265 2750 2821 2667 -75 186 -64 C ATOM 4500 CH2 TRP B 265 -19.910 31.081 43.794 1.00 22.60 C ANISOU 4500 CH2 TRP B 265 2849 2950 2786 -71 176 -73 C ATOM 4501 N LEU B 266 -12.688 27.108 42.765 1.00 19.60 N ANISOU 4501 N LEU B 266 2542 2477 2426 -90 166 -24 N ATOM 4502 CA LEU B 266 -11.954 26.023 43.415 1.00 20.23 C ANISOU 4502 CA LEU B 266 2636 2544 2506 -90 177 -11 C ATOM 4503 C LEU B 266 -11.430 26.397 44.795 1.00 24.91 C ANISOU 4503 C LEU B 266 3240 3139 3084 -73 171 -2 C ATOM 4504 O LEU B 266 -11.574 25.579 45.719 1.00 21.06 O ANISOU 4504 O LEU B 266 2761 2651 2590 -69 188 9 O ATOM 4505 CB LEU B 266 -10.829 25.522 42.503 1.00 27.08 C ANISOU 4505 CB LEU B 266 3507 3397 3386 -95 173 -7 C ATOM 4506 CG LEU B 266 -11.248 24.550 41.392 1.00 25.96 C ANISOU 4506 CG LEU B 266 3357 3250 3256 -113 187 -14 C ATOM 4507 CD1 LEU B 266 -10.026 24.028 40.651 1.00 23.93 C ANISOU 4507 CD1 LEU B 266 3107 2978 3009 -115 185 -9 C ATOM 4508 CD2 LEU B 266 -12.073 23.392 41.943 1.00 32.23 C ANISOU 4508 CD2 LEU B 266 4151 4039 4055 -124 212 -12 C ATOM 4509 N PRO B 267 -10.819 27.570 45.019 1.00 22.28 N ANISOU 4509 N PRO B 267 2908 2811 2748 -60 150 -7 N ATOM 4510 CA PRO B 267 -10.405 27.898 46.392 1.00 25.84 C ANISOU 4510 CA PRO B 267 3368 3268 3182 -42 143 -4 C ATOM 4511 C PRO B 267 -11.548 27.857 47.394 1.00 23.52 C ANISOU 4511 C PRO B 267 3077 2988 2873 -36 157 -4 C ATOM 4512 O PRO B 267 -11.378 27.333 48.504 1.00 22.64 O ANISOU 4512 O PRO B 267 2977 2882 2745 -24 165 7 O ATOM 4513 CB PRO B 267 -9.826 29.313 46.249 1.00 24.85 C ANISOU 4513 CB PRO B 267 3238 3143 3061 -33 118 -17 C ATOM 4514 CG PRO B 267 -9.402 29.409 44.844 1.00 21.64 C ANISOU 4514 CG PRO B 267 2824 2725 2674 -44 114 -17 C ATOM 4515 CD PRO B 267 -10.430 28.634 44.074 1.00 25.40 C ANISOU 4515 CD PRO B 267 3295 3204 3154 -59 132 -16 C ATOM 4516 N TYR B 268 -12.723 28.371 47.027 1.00 21.68 N ANISOU 4516 N TYR B 268 2832 2763 2642 -43 161 -14 N ATOM 4517 CA TYR B 268 -13.860 28.315 47.941 1.00 24.33 C ANISOU 4517 CA TYR B 268 3167 3111 2964 -38 177 -14 C ATOM 4518 C TYR B 268 -14.320 26.879 48.164 1.00 20.23 C ANISOU 4518 C TYR B 268 2652 2587 2448 -47 206 1 C ATOM 4519 O TYR B 268 -14.607 26.485 49.299 1.00 19.02 O ANISOU 4519 O TYR B 268 2507 2440 2280 -36 222 12 O ATOM 4520 CB TYR B 268 -15.011 29.173 47.414 1.00 21.54 C ANISOU 4520 CB TYR B 268 2799 2768 2617 -43 175 -28 C ATOM 4521 CG TYR B 268 -16.231 29.150 48.308 1.00 20.14 C ANISOU 4521 CG TYR B 268 2620 2604 2429 -38 193 -28 C ATOM 4522 CD1 TYR B 268 -16.322 29.990 49.408 1.00 23.33 C ANISOU 4522 CD1 TYR B 268 3030 3020 2814 -19 187 -33 C ATOM 4523 CD2 TYR B 268 -17.289 28.282 48.056 1.00 19.69 C ANISOU 4523 CD2 TYR B 268 2553 2548 2381 -53 217 -25 C ATOM 4524 CE1 TYR B 268 -17.429 29.967 50.233 1.00 18.58 C ANISOU 4524 CE1 TYR B 268 2426 2431 2201 -13 206 -32 C ATOM 4525 CE2 TYR B 268 -18.402 28.258 48.878 1.00 24.32 C ANISOU 4525 CE2 TYR B 268 3135 3145 2960 -48 236 -23 C ATOM 4526 CZ TYR B 268 -18.464 29.103 49.961 1.00 19.98 C ANISOU 4526 CZ TYR B 268 2594 2608 2389 -28 231 -26 C ATOM 4527 OH TYR B 268 -19.568 29.081 50.781 1.00 26.75 O ANISOU 4527 OH TYR B 268 3448 3478 3239 -22 252 -23 O ATOM 4528 N ALA B 269 -14.381 26.084 47.092 1.00 21.84 N ANISOU 4528 N ALA B 269 2849 2779 2672 -66 214 1 N ATOM 4529 CA ALA B 269 -14.818 24.695 47.204 1.00 25.59 C ANISOU 4529 CA ALA B 269 3324 3243 3157 -78 244 12 C ATOM 4530 C ALA B 269 -13.895 23.885 48.110 1.00 22.24 C ANISOU 4530 C ALA B 269 2917 2809 2723 -65 254 34 C ATOM 4531 O ALA B 269 -14.362 23.051 48.896 1.00 21.43 O ANISOU 4531 O ALA B 269 2820 2705 2619 -62 281 50 O ATOM 4532 CB ALA B 269 -14.890 24.060 45.815 1.00 29.37 C ANISOU 4532 CB ALA B 269 3791 3709 3658 -100 247 3 C ATOM 4533 N GLY B 270 -12.583 24.097 47.996 1.00 22.62 N ANISOU 4533 N GLY B 270 2974 2853 2766 -56 234 37 N ATOM 4534 CA GLY B 270 -11.648 23.346 48.822 1.00 24.53 C ANISOU 4534 CA GLY B 270 3232 3090 3000 -42 241 58 C ATOM 4535 C GLY B 270 -11.762 23.684 50.297 1.00 19.83 C ANISOU 4535 C GLY B 270 2646 2512 2375 -17 242 67 C ATOM 4536 O GLY B 270 -11.775 22.794 51.151 1.00 23.94 O ANISOU 4536 O GLY B 270 3178 3032 2886 -6 265 90 O ATOM 4537 N VAL B 271 -11.847 24.977 50.617 1.00 17.55 N ANISOU 4537 N VAL B 271 2355 2241 2072 -6 219 50 N ATOM 4538 CA VAL B 271 -11.942 25.382 52.018 1.00 18.63 C ANISOU 4538 CA VAL B 271 2502 2399 2179 19 217 54 C ATOM 4539 C VAL B 271 -13.264 24.925 52.628 1.00 19.71 C ANISOU 4539 C VAL B 271 2638 2541 2308 20 250 64 C ATOM 4540 O VAL B 271 -13.312 24.493 53.788 1.00 19.84 O ANISOU 4540 O VAL B 271 2667 2570 2302 40 265 82 O ATOM 4541 CB VAL B 271 -11.750 26.904 52.143 1.00 18.87 C ANISOU 4541 CB VAL B 271 2527 2442 2200 28 186 29 C ATOM 4542 CG1 VAL B 271 -12.028 27.361 53.567 1.00 17.34 C ANISOU 4542 CG1 VAL B 271 2343 2273 1974 54 185 27 C ATOM 4543 CG2 VAL B 271 -10.337 27.282 51.736 1.00 25.38 C ANISOU 4543 CG2 VAL B 271 3352 3260 3032 31 158 22 C ATOM 4544 N ALA B 272 -14.359 25.030 51.871 1.00 20.10 N ANISOU 4544 N ALA B 272 2673 2586 2377 -1 260 54 N ATOM 4545 CA ALA B 272 -15.650 24.563 52.373 1.00 18.64 C ANISOU 4545 CA ALA B 272 2484 2405 2193 -4 292 62 C ATOM 4546 C ALA B 272 -15.614 23.072 52.670 1.00 20.27 C ANISOU 4546 C ALA B 272 2697 2595 2407 -6 327 90 C ATOM 4547 O ALA B 272 -16.100 22.627 53.717 1.00 23.86 O ANISOU 4547 O ALA B 272 3159 3057 2848 9 354 109 O ATOM 4548 CB ALA B 272 -16.756 24.877 51.365 1.00 22.63 C ANISOU 4548 CB ALA B 272 2969 2907 2722 -28 295 44 C ATOM 4549 N PHE B 273 -15.039 22.282 51.763 1.00 18.83 N ANISOU 4549 N PHE B 273 2513 2392 2250 -23 329 93 N ATOM 4550 CA PHE B 273 -14.968 20.843 51.990 1.00 26.20 C ANISOU 4550 CA PHE B 273 3453 3305 3196 -26 364 119 C ATOM 4551 C PHE B 273 -14.035 20.513 53.149 1.00 22.21 C ANISOU 4551 C PHE B 273 2969 2808 2664 5 367 145 C ATOM 4552 O PHE B 273 -14.294 19.574 53.911 1.00 18.27 O ANISOU 4552 O PHE B 273 2477 2302 2162 16 402 174 O ATOM 4553 CB PHE B 273 -14.528 20.128 50.713 1.00 28.78 C ANISOU 4553 CB PHE B 273 3773 3608 3556 -50 363 112 C ATOM 4554 CG PHE B 273 -14.600 18.631 50.806 1.00 34.03 C ANISOU 4554 CG PHE B 273 4440 4247 4244 -58 403 134 C ATOM 4555 CD1 PHE B 273 -15.824 17.979 50.744 1.00 29.75 C ANISOU 4555 CD1 PHE B 273 3884 3692 3726 -76 437 134 C ATOM 4556 CD2 PHE B 273 -13.446 17.875 50.955 1.00 33.21 C ANISOU 4556 CD2 PHE B 273 4350 4129 4139 -47 407 155 C ATOM 4557 CE1 PHE B 273 -15.896 16.598 50.833 1.00 32.09 C ANISOU 4557 CE1 PHE B 273 4182 3961 4050 -83 476 154 C ATOM 4558 CE2 PHE B 273 -13.509 16.494 51.044 1.00 34.67 C ANISOU 4558 CE2 PHE B 273 4538 4286 4348 -53 446 177 C ATOM 4559 CZ PHE B 273 -14.736 15.854 50.984 1.00 34.56 C ANISOU 4559 CZ PHE B 273 4511 4259 4362 -71 482 176 C ATOM 4560 N TYR B 274 -12.945 21.271 53.302 1.00 24.20 N ANISOU 4560 N TYR B 274 3228 3073 2895 22 331 138 N ATOM 4561 CA TYR B 274 -12.051 21.040 54.434 1.00 20.85 C ANISOU 4561 CA TYR B 274 2821 2662 2439 54 329 160 C ATOM 4562 C TYR B 274 -12.763 21.287 55.758 1.00 22.86 C ANISOU 4562 C TYR B 274 3084 2941 2662 79 344 170 C ATOM 4563 O TYR B 274 -12.606 20.516 56.714 1.00 20.31 O ANISOU 4563 O TYR B 274 2773 2623 2320 103 368 201 O ATOM 4564 CB TYR B 274 -10.810 21.932 54.329 1.00 24.41 C ANISOU 4564 CB TYR B 274 3274 3125 2877 65 285 143 C ATOM 4565 CG TYR B 274 -9.904 21.796 55.530 1.00 26.04 C ANISOU 4565 CG TYR B 274 3496 3351 3049 101 277 160 C ATOM 4566 CD1 TYR B 274 -8.914 20.826 55.566 1.00 25.80 C ANISOU 4566 CD1 TYR B 274 3472 3308 3021 110 284 184 C ATOM 4567 CD2 TYR B 274 -10.059 22.620 56.644 1.00 27.73 C ANISOU 4567 CD2 TYR B 274 3715 3596 3225 127 264 152 C ATOM 4568 CE1 TYR B 274 -8.099 20.684 56.672 1.00 29.76 C ANISOU 4568 CE1 TYR B 274 3987 3833 3489 146 276 201 C ATOM 4569 CE2 TYR B 274 -9.250 22.486 57.752 1.00 31.93 C ANISOU 4569 CE2 TYR B 274 4259 4150 3721 162 255 166 C ATOM 4570 CZ TYR B 274 -8.271 21.520 57.761 1.00 31.06 C ANISOU 4570 CZ TYR B 274 4156 4031 3614 172 261 191 C ATOM 4571 OH TYR B 274 -7.461 21.388 58.863 1.00 36.00 O ANISOU 4571 OH TYR B 274 4794 4684 4202 210 250 205 O ATOM 4572 N ILE B 275 -13.535 22.371 55.837 1.00 20.84 N ANISOU 4572 N ILE B 275 2820 2701 2397 77 331 147 N ATOM 4573 CA ILE B 275 -14.271 22.681 57.058 1.00 20.81 C ANISOU 4573 CA ILE B 275 2823 2722 2362 101 346 154 C ATOM 4574 C ILE B 275 -15.290 21.591 57.355 1.00 19.60 C ANISOU 4574 C ILE B 275 2669 2556 2222 96 396 182 C ATOM 4575 O ILE B 275 -15.448 21.165 58.506 1.00 19.11 O ANISOU 4575 O ILE B 275 2620 2508 2133 124 421 209 O ATOM 4576 CB ILE B 275 -14.933 24.067 56.934 1.00 23.33 C ANISOU 4576 CB ILE B 275 3131 3056 2676 96 323 121 C ATOM 4577 CG1 ILE B 275 -13.860 25.151 56.799 1.00 18.21 C ANISOU 4577 CG1 ILE B 275 2485 2419 2017 104 276 95 C ATOM 4578 CG2 ILE B 275 -15.866 24.329 58.117 1.00 21.03 C ANISOU 4578 CG2 ILE B 275 2846 2788 2356 119 343 128 C ATOM 4579 CD1 ILE B 275 -14.404 26.562 56.683 1.00 21.11 C ANISOU 4579 CD1 ILE B 275 2842 2798 2382 102 254 62 C ATOM 4580 N PHE B 276 -15.991 21.118 56.320 1.00 20.41 N ANISOU 4580 N PHE B 276 2755 2633 2366 62 413 176 N ATOM 4581 CA PHE B 276 -17.042 20.124 56.515 1.00 22.95 C ANISOU 4581 CA PHE B 276 3071 2939 2708 53 462 198 C ATOM 4582 C PHE B 276 -16.487 18.828 57.086 1.00 21.94 C ANISOU 4582 C PHE B 276 2958 2797 2581 68 495 237 C ATOM 4583 O PHE B 276 -17.166 18.155 57.868 1.00 21.57 O ANISOU 4583 O PHE B 276 2914 2747 2533 79 538 265 O ATOM 4584 CB PHE B 276 -17.759 19.866 55.186 1.00 20.15 C ANISOU 4584 CB PHE B 276 2695 2561 2401 12 468 177 C ATOM 4585 CG PHE B 276 -18.765 18.741 55.233 1.00 19.54 C ANISOU 4585 CG PHE B 276 2607 2462 2357 -3 518 195 C ATOM 4586 CD1 PHE B 276 -19.970 18.892 55.904 1.00 23.64 C ANISOU 4586 CD1 PHE B 276 3118 2991 2873 1 545 200 C ATOM 4587 CD2 PHE B 276 -18.515 17.547 54.575 1.00 19.07 C ANISOU 4587 CD2 PHE B 276 2543 2369 2334 -23 540 204 C ATOM 4588 CE1 PHE B 276 -20.903 17.866 55.933 1.00 21.03 C ANISOU 4588 CE1 PHE B 276 2776 2638 2578 -14 594 216 C ATOM 4589 CE2 PHE B 276 -19.443 16.515 54.599 1.00 23.33 C ANISOU 4589 CE2 PHE B 276 3071 2885 2910 -40 587 217 C ATOM 4590 CZ PHE B 276 -20.639 16.675 55.281 1.00 22.16 C ANISOU 4590 CZ PHE B 276 2913 2745 2760 -36 615 223 C ATOM 4591 N THR B 277 -15.261 18.469 56.716 1.00 19.45 N ANISOU 4591 N THR B 277 2651 2472 2268 70 477 242 N ATOM 4592 CA THR B 277 -14.612 17.265 57.208 1.00 19.33 C ANISOU 4592 CA THR B 277 2649 2442 2252 87 505 280 C ATOM 4593 C THR B 277 -13.764 17.518 58.452 1.00 21.93 C ANISOU 4593 C THR B 277 2999 2803 2531 133 492 300 C ATOM 4594 O THR B 277 -13.127 16.584 58.949 1.00 20.17 O ANISOU 4594 O THR B 277 2790 2574 2302 153 513 336 O ATOM 4595 CB THR B 277 -13.750 16.640 56.099 1.00 21.52 C ANISOU 4595 CB THR B 277 2923 2690 2562 66 496 275 C ATOM 4596 OG1 THR B 277 -12.904 17.635 55.508 1.00 18.78 O ANISOU 4596 OG1 THR B 277 2575 2357 2206 62 445 245 O ATOM 4597 CG2 THR B 277 -14.635 16.048 55.011 1.00 19.06 C ANISOU 4597 CG2 THR B 277 2593 2348 2303 25 519 261 C ATOM 4598 N HIS B 278 -13.729 18.752 58.953 1.00 19.45 N ANISOU 4598 N HIS B 278 2688 2523 2180 149 459 278 N ATOM 4599 CA HIS B 278 -12.960 19.110 60.146 1.00 23.79 C ANISOU 4599 CA HIS B 278 3254 3108 2677 193 441 289 C ATOM 4600 C HIS B 278 -13.757 20.079 61.015 1.00 20.66 C ANISOU 4600 C HIS B 278 2860 2745 2246 212 437 276 C ATOM 4601 O HIS B 278 -13.258 21.119 61.444 1.00 26.77 O ANISOU 4601 O HIS B 278 3637 3548 2987 230 398 252 O ATOM 4602 CB HIS B 278 -11.604 19.703 59.767 1.00 24.64 C ANISOU 4602 CB HIS B 278 3363 3224 2777 197 391 267 C ATOM 4603 CG HIS B 278 -10.756 18.789 58.937 1.00 26.00 C ANISOU 4603 CG HIS B 278 3533 3365 2980 181 394 280 C ATOM 4604 ND1 HIS B 278 -10.995 18.561 57.597 1.00 19.02 N ANISOU 4604 ND1 HIS B 278 2636 2448 2144 141 397 264 N ATOM 4605 CD2 HIS B 278 -9.672 18.044 59.256 1.00 22.20 C ANISOU 4605 CD2 HIS B 278 3062 2883 2490 203 395 306 C ATOM 4606 CE1 HIS B 278 -10.099 17.711 57.130 1.00 19.00 C ANISOU 4606 CE1 HIS B 278 2636 2424 2160 137 401 280 C ATOM 4607 NE2 HIS B 278 -9.279 17.388 58.114 1.00 19.26 N ANISOU 4607 NE2 HIS B 278 2683 2475 2161 174 400 306 N ATOM 4608 N GLN B 279 -15.027 19.763 61.256 1.00 21.24 N ANISOU 4608 N GLN B 279 2929 2811 2330 205 478 289 N ATOM 4609 CA GLN B 279 -15.879 20.666 62.018 1.00 20.10 C ANISOU 4609 CA GLN B 279 2786 2697 2156 221 477 276 C ATOM 4610 C GLN B 279 -15.345 20.863 63.432 1.00 26.57 C ANISOU 4610 C GLN B 279 3624 3555 2914 272 472 292 C ATOM 4611 O GLN B 279 -14.962 19.904 64.112 1.00 21.82 O ANISOU 4611 O GLN B 279 3037 2957 2296 299 498 332 O ATOM 4612 CB GLN B 279 -17.311 20.130 62.070 1.00 26.54 C ANISOU 4612 CB GLN B 279 3592 3496 2996 207 528 293 C ATOM 4613 CG GLN B 279 -18.030 20.134 60.733 1.00 23.64 C ANISOU 4613 CG GLN B 279 3201 3098 2683 159 530 270 C ATOM 4614 CD GLN B 279 -19.448 19.620 60.845 1.00 24.79 C ANISOU 4614 CD GLN B 279 3334 3231 2855 146 579 284 C ATOM 4615 OE1 GLN B 279 -19.809 18.971 61.825 1.00 31.23 O ANISOU 4615 OE1 GLN B 279 4159 4050 3655 169 621 320 O ATOM 4616 NE2 GLN B 279 -20.262 19.912 59.842 1.00 29.91 N ANISOU 4616 NE2 GLN B 279 3960 3864 3542 109 575 256 N ATOM 4617 N GLY B 280 -15.321 22.121 63.869 1.00 23.67 N ANISOU 4617 N GLY B 280 3258 3221 2515 287 436 258 N ATOM 4618 CA GLY B 280 -14.817 22.475 65.179 1.00 27.30 C ANISOU 4618 CA GLY B 280 3736 3724 2915 335 423 262 C ATOM 4619 C GLY B 280 -13.321 22.678 65.266 1.00 25.15 C ANISOU 4619 C GLY B 280 3468 3466 2621 352 379 250 C ATOM 4620 O GLY B 280 -12.823 22.998 66.354 1.00 27.10 O ANISOU 4620 O GLY B 280 3728 3753 2816 394 362 249 O ATOM 4621 N SER B 281 -12.589 22.507 64.165 1.00 24.87 N ANISOU 4621 N SER B 281 3424 3402 2625 322 358 240 N ATOM 4622 CA SER B 281 -11.141 22.653 64.186 1.00 25.26 C ANISOU 4622 CA SER B 281 3476 3463 2660 336 318 230 C ATOM 4623 C SER B 281 -10.746 24.126 64.299 1.00 27.61 C ANISOU 4623 C SER B 281 3766 3784 2941 340 266 179 C ATOM 4624 O SER B 281 -11.578 25.038 64.237 1.00 25.13 O ANISOU 4624 O SER B 281 3445 3473 2630 329 262 151 O ATOM 4625 CB SER B 281 -10.517 22.024 62.939 1.00 25.77 C ANISOU 4625 CB SER B 281 3531 3487 2773 303 315 236 C ATOM 4626 OG SER B 281 -11.020 22.616 61.752 1.00 23.57 O ANISOU 4626 OG SER B 281 3235 3182 2537 260 305 205 O ATOM 4627 N ASP B 282 -9.443 24.348 64.460 1.00 26.60 N ANISOU 4627 N ASP B 282 3638 3671 2799 356 227 165 N ATOM 4628 CA ASP B 282 -8.893 25.662 64.791 1.00 28.91 C ANISOU 4628 CA ASP B 282 3924 3990 3072 366 178 117 C ATOM 4629 C ASP B 282 -8.650 26.459 63.513 1.00 29.27 C ANISOU 4629 C ASP B 282 3952 4004 3167 325 151 82 C ATOM 4630 O ASP B 282 -7.601 26.329 62.879 1.00 38.36 O ANISOU 4630 O ASP B 282 5095 5140 4341 313 129 78 O ATOM 4631 CB ASP B 282 -7.602 25.500 65.586 1.00 31.49 C ANISOU 4631 CB ASP B 282 4256 4347 3360 404 150 118 C ATOM 4632 CG ASP B 282 -7.124 26.800 66.198 1.00 34.06 C ANISOU 4632 CG ASP B 282 4576 4707 3660 422 102 67 C ATOM 4633 OD1 ASP B 282 -7.963 27.697 66.425 1.00 37.13 O ANISOU 4633 OD1 ASP B 282 4963 5104 4042 419 102 40 O ATOM 4634 OD2 ASP B 282 -5.907 26.924 66.450 1.00 36.75 O ANISOU 4634 OD2 ASP B 282 4911 5065 3987 439 66 53 O ATOM 4635 N PHE B 283 -9.614 27.301 63.136 1.00 24.33 N ANISOU 4635 N PHE B 283 3318 3369 2559 304 154 58 N ATOM 4636 CA PHE B 283 -9.422 28.256 62.052 1.00 25.80 C ANISOU 4636 CA PHE B 283 3487 3531 2786 271 127 23 C ATOM 4637 C PHE B 283 -10.049 29.588 62.446 1.00 27.55 C ANISOU 4637 C PHE B 283 3703 3768 2998 276 112 -16 C ATOM 4638 O PHE B 283 -10.942 29.649 63.293 1.00 19.92 O ANISOU 4638 O PHE B 283 2746 2823 2001 295 131 -12 O ATOM 4639 CB PHE B 283 -10.000 27.742 60.712 1.00 26.56 C ANISOU 4639 CB PHE B 283 3575 3587 2930 231 151 39 C ATOM 4640 CG PHE B 283 -11.458 27.377 60.768 1.00 24.05 C ANISOU 4640 CG PHE B 283 3259 3264 2614 224 191 56 C ATOM 4641 CD1 PHE B 283 -12.436 28.332 60.539 1.00 24.44 C ANISOU 4641 CD1 PHE B 283 3300 3314 2674 211 190 32 C ATOM 4642 CD2 PHE B 283 -11.850 26.074 61.045 1.00 25.09 C ANISOU 4642 CD2 PHE B 283 3401 3392 2741 229 231 98 C ATOM 4643 CE1 PHE B 283 -13.782 27.998 60.595 1.00 26.13 C ANISOU 4643 CE1 PHE B 283 3512 3524 2891 204 227 47 C ATOM 4644 CE2 PHE B 283 -13.194 25.732 61.100 1.00 26.42 C ANISOU 4644 CE2 PHE B 283 3568 3555 2916 221 270 113 C ATOM 4645 CZ PHE B 283 -14.160 26.695 60.877 1.00 26.79 C ANISOU 4645 CZ PHE B 283 3605 3604 2972 208 267 87 C ATOM 4646 N GLY B 284 -9.561 30.665 61.826 1.00 21.26 N ANISOU 4646 N GLY B 284 2892 2958 2228 259 78 -53 N ATOM 4647 CA GLY B 284 -10.014 31.998 62.153 1.00 21.14 C ANISOU 4647 CA GLY B 284 2871 2953 2209 263 62 -93 C ATOM 4648 C GLY B 284 -10.926 32.594 61.099 1.00 21.20 C ANISOU 4648 C GLY B 284 2866 2932 2257 231 72 -102 C ATOM 4649 O GLY B 284 -11.242 31.955 60.090 1.00 21.43 O ANISOU 4649 O GLY B 284 2891 2935 2316 205 92 -78 O ATOM 4650 N PRO B 285 -11.357 33.844 61.312 1.00 20.64 N ANISOU 4650 N PRO B 285 2788 2866 2187 233 59 -137 N ATOM 4651 CA PRO B 285 -12.290 34.473 60.358 1.00 20.47 C ANISOU 4651 CA PRO B 285 2755 2821 2203 207 70 -144 C ATOM 4652 C PRO B 285 -11.704 34.688 58.973 1.00 22.43 C ANISOU 4652 C PRO B 285 2989 3035 2498 178 57 -146 C ATOM 4653 O PRO B 285 -12.445 34.636 57.982 1.00 25.68 O ANISOU 4653 O PRO B 285 3393 3426 2937 155 74 -135 O ATOM 4654 CB PRO B 285 -12.633 35.817 61.023 1.00 21.50 C ANISOU 4654 CB PRO B 285 2882 2964 2323 222 55 -184 C ATOM 4655 CG PRO B 285 -12.039 35.769 62.401 1.00 27.34 C ANISOU 4655 CG PRO B 285 3634 3739 3016 257 40 -197 C ATOM 4656 CD PRO B 285 -10.908 34.791 62.343 1.00 28.26 C ANISOU 4656 CD PRO B 285 3754 3856 3126 259 31 -176 C ATOM 4657 N ILE B 286 -10.401 34.954 58.868 1.00 21.15 N ANISOU 4657 N ILE B 286 2822 2868 2346 179 28 -162 N ATOM 4658 CA ILE B 286 -9.814 35.239 57.565 1.00 23.51 C ANISOU 4658 CA ILE B 286 3107 3134 2690 153 17 -164 C ATOM 4659 C ILE B 286 -9.752 33.987 56.696 1.00 27.56 C ANISOU 4659 C ILE B 286 3623 3632 3215 135 36 -126 C ATOM 4660 O ILE B 286 -9.678 34.088 55.463 1.00 20.95 O ANISOU 4660 O ILE B 286 2776 2770 2414 112 38 -122 O ATOM 4661 CB ILE B 286 -8.428 35.886 57.762 1.00 20.61 C ANISOU 4661 CB ILE B 286 2732 2766 2334 159 -18 -192 C ATOM 4662 CG1 ILE B 286 -8.558 37.152 58.612 1.00 22.77 C ANISOU 4662 CG1 ILE B 286 3000 3052 2598 175 -36 -234 C ATOM 4663 CG2 ILE B 286 -7.791 36.247 56.430 1.00 26.46 C ANISOU 4663 CG2 ILE B 286 3458 3472 3122 134 -26 -192 C ATOM 4664 CD1 ILE B 286 -9.488 38.201 58.011 1.00 29.18 C ANISOU 4664 CD1 ILE B 286 3803 3845 3438 161 -28 -248 C ATOM 4665 N PHE B 287 -9.844 32.807 57.309 1.00 24.09 N ANISOU 4665 N PHE B 287 3197 3208 2747 147 54 -100 N ATOM 4666 CA PHE B 287 -9.694 31.552 56.576 1.00 25.94 C ANISOU 4666 CA PHE B 287 3435 3427 2995 132 73 -67 C ATOM 4667 C PHE B 287 -10.718 31.437 55.448 1.00 23.56 C ANISOU 4667 C PHE B 287 3126 3106 2721 106 94 -58 C ATOM 4668 O PHE B 287 -10.380 31.065 54.316 1.00 22.74 O ANISOU 4668 O PHE B 287 3015 2979 2644 85 95 -48 O ATOM 4669 CB PHE B 287 -9.817 30.390 57.564 1.00 24.77 C ANISOU 4669 CB PHE B 287 3303 3298 2811 153 94 -39 C ATOM 4670 CG PHE B 287 -9.574 29.034 56.967 1.00 28.06 C ANISOU 4670 CG PHE B 287 3723 3697 3241 140 115 -5 C ATOM 4671 CD1 PHE B 287 -8.426 28.774 56.238 1.00 27.62 C ANISOU 4671 CD1 PHE B 287 3663 3625 3207 130 99 -3 C ATOM 4672 CD2 PHE B 287 -10.474 28.002 57.183 1.00 23.31 C ANISOU 4672 CD2 PHE B 287 3129 3095 2632 140 152 24 C ATOM 4673 CE1 PHE B 287 -8.202 27.518 55.706 1.00 34.32 C ANISOU 4673 CE1 PHE B 287 4516 4456 4068 120 120 26 C ATOM 4674 CE2 PHE B 287 -10.251 26.743 56.658 1.00 26.89 C ANISOU 4674 CE2 PHE B 287 3586 3530 3101 129 173 52 C ATOM 4675 CZ PHE B 287 -9.114 26.501 55.918 1.00 27.60 C ANISOU 4675 CZ PHE B 287 3673 3604 3211 119 156 53 C ATOM 4676 N MET B 288 -11.976 31.768 55.730 1.00 19.57 N ANISOU 4676 N MET B 288 2619 2609 2208 107 110 -61 N ATOM 4677 CA MET B 288 -13.008 31.702 54.703 1.00 23.24 C ANISOU 4677 CA MET B 288 3074 3059 2697 84 128 -55 C ATOM 4678 C MET B 288 -13.331 33.058 54.085 1.00 18.76 C ANISOU 4678 C MET B 288 2493 2485 2151 76 113 -80 C ATOM 4679 O MET B 288 -13.932 33.097 53.008 1.00 24.02 O ANISOU 4679 O MET B 288 3148 3138 2840 57 121 -77 O ATOM 4680 CB MET B 288 -14.284 31.072 55.285 1.00 24.19 C ANISOU 4680 CB MET B 288 3198 3191 2801 88 161 -40 C ATOM 4681 CG MET B 288 -15.389 30.771 54.275 1.00 19.95 C ANISOU 4681 CG MET B 288 2648 2641 2289 63 181 -33 C ATOM 4682 SD MET B 288 -14.821 29.955 52.771 1.00 22.52 S ANISOU 4682 SD MET B 288 2967 2942 2648 36 181 -22 S ATOM 4683 CE MET B 288 -15.654 28.377 52.899 1.00 22.41 C ANISOU 4683 CE MET B 288 2956 2924 2636 26 221 5 C ATOM 4684 N THR B 289 -12.926 34.164 54.723 1.00 21.14 N ANISOU 4684 N THR B 289 2794 2793 2444 92 92 -106 N ATOM 4685 CA THR B 289 -13.291 35.491 54.228 1.00 21.01 C ANISOU 4685 CA THR B 289 2765 2768 2450 87 81 -128 C ATOM 4686 C THR B 289 -12.744 35.738 52.821 1.00 21.62 C ANISOU 4686 C THR B 289 2830 2820 2563 68 72 -126 C ATOM 4687 O THR B 289 -13.476 36.167 51.922 1.00 22.05 O ANISOU 4687 O THR B 289 2875 2867 2638 56 79 -125 O ATOM 4688 CB THR B 289 -12.787 36.569 55.198 1.00 17.58 C ANISOU 4688 CB THR B 289 2332 2343 2005 107 59 -159 C ATOM 4689 OG1 THR B 289 -13.472 36.460 56.449 1.00 19.42 O ANISOU 4689 OG1 THR B 289 2575 2602 2202 127 70 -162 O ATOM 4690 CG2 THR B 289 -13.019 37.965 54.639 1.00 17.65 C ANISOU 4690 CG2 THR B 289 2327 2336 2043 102 49 -182 C ATOM 4691 N AILE B 290 -11.456 35.476 52.617 0.66 22.03 N ANISOU 4691 N AILE B 290 2884 2863 2623 66 56 -124 N ATOM 4692 N BILE B 290 -11.460 35.471 52.613 0.35 22.04 N ANISOU 4692 N BILE B 290 2885 2864 2625 66 57 -124 N ATOM 4693 CA AILE B 290 -10.791 35.753 51.342 0.66 22.63 C ANISOU 4693 CA AILE B 290 2950 2915 2733 50 48 -122 C ATOM 4694 CA BILE B 290 -10.810 35.764 51.337 0.35 22.82 C ANISOU 4694 CA BILE B 290 2974 2940 2758 50 48 -122 C ATOM 4695 C AILE B 290 -11.347 34.888 50.210 0.66 23.51 C ANISOU 4695 C AILE B 290 3059 3020 2854 32 67 -99 C ATOM 4696 C BILE B 290 -11.344 34.887 50.204 0.35 23.49 C ANISOU 4696 C BILE B 290 3056 3017 2851 32 67 -98 C ATOM 4697 O AILE B 290 -11.660 35.432 49.140 0.66 22.10 O ANISOU 4697 O AILE B 290 2870 2831 2697 23 68 -99 O ATOM 4698 O BILE B 290 -11.645 35.423 49.127 0.35 22.31 O ANISOU 4698 O BILE B 290 2896 2857 2724 23 68 -98 O ATOM 4699 CB AILE B 290 -9.267 35.591 51.466 0.66 24.88 C ANISOU 4699 CB AILE B 290 3236 3193 3024 53 29 -125 C ATOM 4700 CB BILE B 290 -9.284 35.656 51.474 0.35 24.84 C ANISOU 4700 CB BILE B 290 3230 3188 3020 53 28 -126 C ATOM 4701 CG1AILE B 290 -8.748 36.365 52.680 0.66 24.53 C ANISOU 4701 CG1AILE B 290 3192 3160 2968 72 8 -152 C ATOM 4702 CG1BILE B 290 -8.833 36.497 52.669 0.35 24.51 C ANISOU 4702 CG1BILE B 290 3189 3157 2967 72 8 -154 C ATOM 4703 CG2AILE B 290 -8.581 36.085 50.203 0.66 26.67 C ANISOU 4703 CG2AILE B 290 3451 3395 3288 40 22 -124 C ATOM 4704 CG2BILE B 290 -8.602 36.130 50.202 0.35 26.63 C ANISOU 4704 CG2BILE B 290 3445 3390 3283 40 22 -124 C ATOM 4705 CD1AILE B 290 -9.006 37.855 52.607 0.66 25.38 C ANISOU 4705 CD1AILE B 290 3289 3259 3097 73 -1 -179 C ATOM 4706 CD1BILE B 290 -7.354 36.545 52.863 0.35 26.73 C ANISOU 4706 CD1BILE B 290 3467 3433 3257 76 -14 -164 C ATOM 4707 N PRO B 291 -11.471 33.560 50.362 1.00 22.50 N ANISOU 4707 N PRO B 291 2939 2897 2711 28 82 -79 N ATOM 4708 CA PRO B 291 -12.084 32.772 49.274 1.00 21.32 C ANISOU 4708 CA PRO B 291 2786 2742 2573 10 100 -64 C ATOM 4709 C PRO B 291 -13.528 33.145 49.007 1.00 22.06 C ANISOU 4709 C PRO B 291 2870 2843 2668 6 112 -68 C ATOM 4710 O PRO B 291 -13.979 33.069 47.857 1.00 19.15 O ANISOU 4710 O PRO B 291 2491 2470 2315 -8 117 -64 O ATOM 4711 CB PRO B 291 -11.965 31.321 49.763 1.00 26.35 C ANISOU 4711 CB PRO B 291 3434 3382 3195 9 116 -45 C ATOM 4712 CG PRO B 291 -10.935 31.353 50.833 1.00 22.93 C ANISOU 4712 CG PRO B 291 3012 2956 2746 27 102 -47 C ATOM 4713 CD PRO B 291 -11.072 32.676 51.476 1.00 21.52 C ANISOU 4713 CD PRO B 291 2830 2786 2561 41 86 -70 C ATOM 4714 N ALA B 292 -14.270 33.541 50.044 1.00 19.35 N ANISOU 4714 N ALA B 292 2530 2515 2308 18 118 -75 N ATOM 4715 CA ALA B 292 -15.672 33.892 49.861 1.00 22.48 C ANISOU 4715 CA ALA B 292 2916 2920 2706 16 130 -79 C ATOM 4716 C ALA B 292 -15.820 35.157 49.025 1.00 22.20 C ANISOU 4716 C ALA B 292 2867 2877 2689 15 118 -91 C ATOM 4717 O ALA B 292 -16.631 35.202 48.092 1.00 25.90 O ANISOU 4717 O ALA B 292 3324 3348 3170 6 125 -88 O ATOM 4718 CB ALA B 292 -16.353 34.053 51.222 1.00 16.95 C ANISOU 4718 CB ALA B 292 2222 2237 1981 32 140 -84 C ATOM 4719 N PHE B 293 -15.041 36.196 49.336 1.00 20.60 N ANISOU 4719 N PHE B 293 2667 2668 2493 26 100 -105 N ATOM 4720 CA PHE B 293 -15.190 37.453 48.610 1.00 21.15 C ANISOU 4720 CA PHE B 293 2724 2728 2585 28 92 -114 C ATOM 4721 C PHE B 293 -14.487 37.426 47.254 1.00 23.11 C ANISOU 4721 C PHE B 293 2966 2960 2855 18 86 -104 C ATOM 4722 O PHE B 293 -14.891 38.156 46.343 1.00 20.22 O ANISOU 4722 O PHE B 293 2589 2590 2506 18 86 -102 O ATOM 4723 CB PHE B 293 -14.698 38.620 49.471 1.00 23.99 C ANISOU 4723 CB PHE B 293 3085 3082 2947 43 78 -136 C ATOM 4724 CG PHE B 293 -15.754 39.167 50.408 1.00 23.77 C ANISOU 4724 CG PHE B 293 3057 3069 2904 56 85 -149 C ATOM 4725 CD1 PHE B 293 -16.091 38.491 51.572 1.00 25.08 C ANISOU 4725 CD1 PHE B 293 3235 3255 3041 64 94 -150 C ATOM 4726 CD2 PHE B 293 -16.424 40.345 50.108 1.00 21.92 C ANISOU 4726 CD2 PHE B 293 2812 2830 2686 62 87 -159 C ATOM 4727 CE1 PHE B 293 -17.067 38.982 52.422 1.00 21.32 C ANISOU 4727 CE1 PHE B 293 2759 2793 2550 77 103 -161 C ATOM 4728 CE2 PHE B 293 -17.399 40.844 50.958 1.00 22.58 C ANISOU 4728 CE2 PHE B 293 2895 2926 2757 74 95 -172 C ATOM 4729 CZ PHE B 293 -17.720 40.162 52.114 1.00 20.00 C ANISOU 4729 CZ PHE B 293 2579 2619 2399 82 103 -173 C ATOM 4730 N PHE B 294 -13.449 36.599 47.094 1.00 20.38 N ANISOU 4730 N PHE B 294 2627 2607 2509 10 81 -96 N ATOM 4731 CA PHE B 294 -12.873 36.404 45.767 1.00 25.64 C ANISOU 4731 CA PHE B 294 3289 3261 3194 1 80 -84 C ATOM 4732 C PHE B 294 -13.878 35.765 44.816 1.00 22.66 C ANISOU 4732 C PHE B 294 2904 2894 2814 -10 93 -74 C ATOM 4733 O PHE B 294 -13.881 36.070 43.616 1.00 24.43 O ANISOU 4733 O PHE B 294 3119 3113 3050 -12 92 -68 O ATOM 4734 CB PHE B 294 -11.605 35.552 45.856 1.00 24.69 C ANISOU 4734 CB PHE B 294 3177 3132 3073 -4 74 -77 C ATOM 4735 CG PHE B 294 -10.902 35.363 44.532 1.00 27.47 C ANISOU 4735 CG PHE B 294 3524 3470 3443 -13 73 -66 C ATOM 4736 CD1 PHE B 294 -10.294 36.433 43.897 1.00 29.20 C ANISOU 4736 CD1 PHE B 294 3736 3675 3686 -8 65 -67 C ATOM 4737 CD2 PHE B 294 -10.843 34.114 43.934 1.00 23.20 C ANISOU 4737 CD2 PHE B 294 2988 2931 2897 -24 82 -53 C ATOM 4738 CE1 PHE B 294 -9.647 36.265 42.682 1.00 29.10 C ANISOU 4738 CE1 PHE B 294 3719 3650 3687 -14 66 -54 C ATOM 4739 CE2 PHE B 294 -10.194 33.936 42.718 1.00 27.94 C ANISOU 4739 CE2 PHE B 294 3585 3521 3512 -30 82 -44 C ATOM 4740 CZ PHE B 294 -9.595 35.015 42.093 1.00 30.42 C ANISOU 4740 CZ PHE B 294 3891 3823 3846 -24 74 -43 C ATOM 4741 N ALA B 295 -14.735 34.878 45.332 1.00 23.00 N ANISOU 4741 N ALA B 295 2950 2950 2840 -15 106 -72 N ATOM 4742 CA ALA B 295 -15.720 34.206 44.491 1.00 21.12 C ANISOU 4742 CA ALA B 295 2702 2722 2602 -26 118 -67 C ATOM 4743 C ALA B 295 -16.765 35.173 43.951 1.00 23.15 C ANISOU 4743 C ALA B 295 2943 2989 2863 -20 118 -72 C ATOM 4744 O ALA B 295 -17.356 34.919 42.891 1.00 20.77 O ANISOU 4744 O ALA B 295 2630 2696 2566 -27 121 -70 O ATOM 4745 CB ALA B 295 -16.403 33.084 45.276 1.00 20.23 C ANISOU 4745 CB ALA B 295 2593 2618 2476 -33 135 -65 C ATOM 4746 N LYS B 296 -17.006 36.282 44.651 1.00 16.39 N ANISOU 4746 N LYS B 296 2087 2134 2008 -7 114 -80 N ATOM 4747 CA LYS B 296 -18.039 37.217 44.220 1.00 22.55 C ANISOU 4747 CA LYS B 296 2853 2923 2794 1 116 -84 C ATOM 4748 C LYS B 296 -17.678 37.951 42.931 1.00 22.19 C ANISOU 4748 C LYS B 296 2798 2869 2763 6 108 -77 C ATOM 4749 O LYS B 296 -18.551 38.613 42.357 1.00 20.27 O ANISOU 4749 O LYS B 296 2542 2637 2524 14 110 -76 O ATOM 4750 CB LYS B 296 -18.348 38.210 45.349 1.00 20.39 C ANISOU 4750 CB LYS B 296 2581 2648 2517 16 115 -96 C ATOM 4751 CG LYS B 296 -19.008 37.548 46.564 1.00 23.57 C ANISOU 4751 CG LYS B 296 2990 3065 2901 15 127 -100 C ATOM 4752 CD LYS B 296 -19.424 38.560 47.635 1.00 21.67 C ANISOU 4752 CD LYS B 296 2752 2828 2656 32 128 -114 C ATOM 4753 CE LYS B 296 -19.639 37.886 49.000 1.00 19.72 C ANISOU 4753 CE LYS B 296 2517 2592 2385 36 138 -117 C ATOM 4754 NZ LYS B 296 -20.662 36.851 48.959 1.00 27.88 N ANISOU 4754 NZ LYS B 296 3544 3639 3411 25 157 -107 N ATOM 4755 N THR B 297 -16.436 37.835 42.443 1.00 21.81 N ANISOU 4755 N THR B 297 2756 2805 2724 3 101 -70 N ATOM 4756 CA THR B 297 -16.130 38.345 41.110 1.00 22.26 C ANISOU 4756 CA THR B 297 2806 2858 2794 8 98 -60 C ATOM 4757 C THR B 297 -16.866 37.591 40.014 1.00 21.17 C ANISOU 4757 C THR B 297 2658 2740 2646 1 102 -54 C ATOM 4758 O THR B 297 -16.778 37.993 38.852 1.00 20.86 O ANISOU 4758 O THR B 297 2611 2703 2611 9 100 -44 O ATOM 4759 CB THR B 297 -14.635 38.269 40.799 1.00 19.66 C ANISOU 4759 CB THR B 297 2485 2508 2477 5 92 -53 C ATOM 4760 OG1 THR B 297 -14.217 36.899 40.771 1.00 22.82 O ANISOU 4760 OG1 THR B 297 2893 2911 2867 -9 93 -51 O ATOM 4761 CG2 THR B 297 -13.827 39.032 41.817 1.00 25.37 C ANISOU 4761 CG2 THR B 297 3215 3213 3213 11 84 -62 C ATOM 4762 N SER B 298 -17.562 36.503 40.354 1.00 21.54 N ANISOU 4762 N SER B 298 2704 2800 2679 -12 108 -61 N ATOM 4763 CA SER B 298 -18.285 35.721 39.358 1.00 20.74 C ANISOU 4763 CA SER B 298 2591 2718 2571 -20 112 -62 C ATOM 4764 C SER B 298 -19.350 36.546 38.645 1.00 21.49 C ANISOU 4764 C SER B 298 2667 2833 2665 -7 110 -62 C ATOM 4765 O SER B 298 -19.706 36.244 37.499 1.00 24.03 O ANISOU 4765 O SER B 298 2978 3172 2981 -7 107 -61 O ATOM 4766 CB SER B 298 -18.914 34.501 40.028 1.00 20.58 C ANISOU 4766 CB SER B 298 2571 2705 2544 -37 122 -71 C ATOM 4767 OG SER B 298 -19.659 34.885 41.180 1.00 19.47 O ANISOU 4767 OG SER B 298 2429 2568 2400 -32 128 -76 O ATOM 4768 N ALA B 299 -19.873 37.581 39.300 1.00 17.89 N ANISOU 4768 N ALA B 299 2208 2377 2213 6 111 -63 N ATOM 4769 CA ALA B 299 -20.905 38.404 38.686 1.00 17.51 C ANISOU 4769 CA ALA B 299 2142 2347 2164 21 110 -61 C ATOM 4770 C ALA B 299 -20.394 39.278 37.542 1.00 22.26 C ANISOU 4770 C ALA B 299 2741 2946 2772 39 105 -45 C ATOM 4771 O ALA B 299 -21.215 39.835 36.805 1.00 24.78 O ANISOU 4771 O ALA B 299 3044 3284 3088 54 104 -40 O ATOM 4772 CB ALA B 299 -21.562 39.293 39.746 1.00 23.10 C ANISOU 4772 CB ALA B 299 2848 3053 2877 32 115 -66 C ATOM 4773 N VAL B 300 -19.079 39.409 37.355 1.00 24.95 N ANISOU 4773 N VAL B 300 3094 3263 3122 39 103 -36 N ATOM 4774 CA VAL B 300 -18.520 40.422 36.470 1.00 22.20 C ANISOU 4774 CA VAL B 300 2744 2905 2785 57 103 -18 C ATOM 4775 C VAL B 300 -17.743 39.826 35.300 1.00 21.49 C ANISOU 4775 C VAL B 300 2657 2818 2689 55 101 -8 C ATOM 4776 O VAL B 300 -17.807 40.354 34.184 1.00 23.19 O ANISOU 4776 O VAL B 300 2864 3044 2902 73 103 8 O ATOM 4777 CB VAL B 300 -17.639 41.418 37.256 1.00 25.36 C ANISOU 4777 CB VAL B 300 3154 3273 3209 63 105 -16 C ATOM 4778 CG1 VAL B 300 -17.009 42.444 36.311 1.00 26.84 C ANISOU 4778 CG1 VAL B 300 3338 3446 3415 82 109 4 C ATOM 4779 CG2 VAL B 300 -18.466 42.120 38.323 1.00 26.77 C ANISOU 4779 CG2 VAL B 300 3328 3450 3392 69 107 -28 C ATOM 4780 N TYR B 301 -16.990 38.740 35.520 1.00 20.26 N ANISOU 4780 N TYR B 301 2513 2655 2531 36 100 -14 N ATOM 4781 CA TYR B 301 -15.915 38.407 34.583 1.00 23.31 C ANISOU 4781 CA TYR B 301 2906 3034 2919 36 100 -3 C ATOM 4782 C TYR B 301 -16.394 37.805 33.261 1.00 24.23 C ANISOU 4782 C TYR B 301 3013 3180 3015 40 98 -1 C ATOM 4783 O TYR B 301 -15.668 37.891 32.264 1.00 18.81 O ANISOU 4783 O TYR B 301 2328 2491 2326 50 100 13 O ATOM 4784 CB TYR B 301 -14.901 37.462 35.243 1.00 21.69 C ANISOU 4784 CB TYR B 301 2715 2808 2717 17 99 -10 C ATOM 4785 CG TYR B 301 -15.349 36.031 35.392 1.00 19.28 C ANISOU 4785 CG TYR B 301 2411 2517 2397 -2 99 -24 C ATOM 4786 CD1 TYR B 301 -15.237 35.126 34.340 1.00 22.33 C ANISOU 4786 CD1 TYR B 301 2796 2916 2773 -8 99 -25 C ATOM 4787 CD2 TYR B 301 -15.857 35.572 36.594 1.00 18.41 C ANISOU 4787 CD2 TYR B 301 2303 2406 2285 -14 101 -37 C ATOM 4788 CE1 TYR B 301 -15.650 33.814 34.478 1.00 21.75 C ANISOU 4788 CE1 TYR B 301 2721 2851 2691 -27 102 -41 C ATOM 4789 CE2 TYR B 301 -16.265 34.265 36.744 1.00 18.69 C ANISOU 4789 CE2 TYR B 301 2339 2450 2312 -32 105 -48 C ATOM 4790 CZ TYR B 301 -16.160 33.389 35.686 1.00 21.00 C ANISOU 4790 CZ TYR B 301 2629 2752 2599 -39 106 -51 C ATOM 4791 OH TYR B 301 -16.567 32.083 35.833 1.00 23.03 O ANISOU 4791 OH TYR B 301 2884 3013 2852 -58 112 -64 O ATOM 4792 N ASN B 302 -17.562 37.158 33.221 1.00 25.49 N ANISOU 4792 N ASN B 302 3160 3365 3158 33 95 -17 N ATOM 4793 CA ASN B 302 -17.971 36.497 31.979 1.00 23.44 C ANISOU 4793 CA ASN B 302 2891 3135 2879 35 91 -22 C ATOM 4794 C ASN B 302 -18.183 37.462 30.817 1.00 18.01 C ANISOU 4794 C ASN B 302 2193 2467 2182 64 89 -4 C ATOM 4795 O ASN B 302 -17.716 37.158 29.708 1.00 21.40 O ANISOU 4795 O ASN B 302 2624 2908 2599 72 88 2 O ATOM 4796 CB ASN B 302 -19.210 35.629 32.219 1.00 23.33 C ANISOU 4796 CB ASN B 302 2864 3146 2856 20 88 -47 C ATOM 4797 CG ASN B 302 -18.865 34.290 32.832 1.00 22.21 C ANISOU 4797 CG ASN B 302 2731 2989 2718 -8 92 -62 C ATOM 4798 OD1 ASN B 302 -18.161 33.483 32.225 1.00 21.50 O ANISOU 4798 OD1 ASN B 302 2648 2896 2626 -16 92 -65 O ATOM 4799 ND2 ASN B 302 -19.358 34.045 34.046 1.00 25.91 N ANISOU 4799 ND2 ASN B 302 3201 3450 3196 -22 97 -71 N ATOM 4800 N PRO B 303 -18.868 38.601 30.967 1.00 22.78 N ANISOU 4800 N PRO B 303 2789 3077 2791 83 91 6 N ATOM 4801 CA PRO B 303 -18.927 39.554 29.844 1.00 20.31 C ANISOU 4801 CA PRO B 303 2469 2779 2470 115 92 29 C ATOM 4802 C PRO B 303 -17.567 40.128 29.443 1.00 21.08 C ANISOU 4802 C PRO B 303 2579 2848 2582 126 102 55 C ATOM 4803 O PRO B 303 -17.414 40.553 28.290 1.00 23.02 O ANISOU 4803 O PRO B 303 2822 3109 2817 151 106 75 O ATOM 4804 CB PRO B 303 -19.872 40.650 30.357 1.00 19.59 C ANISOU 4804 CB PRO B 303 2366 2690 2387 131 95 34 C ATOM 4805 CG PRO B 303 -20.690 39.984 31.398 1.00 25.22 C ANISOU 4805 CG PRO B 303 3074 3408 3100 107 90 8 C ATOM 4806 CD PRO B 303 -19.759 39.014 32.065 1.00 17.68 C ANISOU 4806 CD PRO B 303 2136 2428 2153 80 91 -4 C ATOM 4807 N VAL B 304 -16.581 40.153 30.348 1.00 21.89 N ANISOU 4807 N VAL B 304 2697 2912 2710 111 107 54 N ATOM 4808 CA VAL B 304 -15.250 40.649 29.990 1.00 21.46 C ANISOU 4808 CA VAL B 304 2652 2829 2673 119 117 76 C ATOM 4809 C VAL B 304 -14.554 39.675 29.047 1.00 20.15 C ANISOU 4809 C VAL B 304 2493 2673 2492 114 116 78 C ATOM 4810 O VAL B 304 -13.883 40.086 28.094 1.00 22.01 O ANISOU 4810 O VAL B 304 2730 2906 2727 133 126 101 O ATOM 4811 CB VAL B 304 -14.403 40.913 31.250 1.00 21.56 C ANISOU 4811 CB VAL B 304 2675 2800 2716 102 119 70 C ATOM 4812 CG1 VAL B 304 -12.983 41.338 30.866 1.00 20.12 C ANISOU 4812 CG1 VAL B 304 2500 2588 2557 108 129 90 C ATOM 4813 CG2 VAL B 304 -15.047 41.973 32.113 1.00 16.66 C ANISOU 4813 CG2 VAL B 304 2048 2169 2112 110 120 67 C ATOM 4814 N ILE B 305 -14.693 38.374 29.305 1.00 20.76 N ANISOU 4814 N ILE B 305 2573 2761 2555 91 108 53 N ATOM 4815 CA ILE B 305 -14.201 37.362 28.372 1.00 19.90 C ANISOU 4815 CA ILE B 305 2468 2665 2429 87 108 50 C ATOM 4816 C ILE B 305 -14.923 37.484 27.037 1.00 21.56 C ANISOU 4816 C ILE B 305 2666 2916 2610 110 105 55 C ATOM 4817 O ILE B 305 -14.312 37.389 25.965 1.00 17.83 O ANISOU 4817 O ILE B 305 2197 2452 2124 125 110 69 O ATOM 4818 CB ILE B 305 -14.386 35.958 28.979 1.00 18.49 C ANISOU 4818 CB ILE B 305 2293 2488 2245 56 101 21 C ATOM 4819 CG1 ILE B 305 -13.678 35.850 30.337 1.00 17.36 C ANISOU 4819 CG1 ILE B 305 2161 2307 2126 37 103 18 C ATOM 4820 CG2 ILE B 305 -13.956 34.874 27.990 1.00 19.39 C ANISOU 4820 CG2 ILE B 305 2410 2615 2342 52 101 13 C ATOM 4821 CD1 ILE B 305 -13.900 34.522 31.031 1.00 20.57 C ANISOU 4821 CD1 ILE B 305 2572 2714 2530 11 101 -6 C ATOM 4822 N TYR B 306 -16.240 37.685 27.096 1.00 18.77 N ANISOU 4822 N TYR B 306 2298 2590 2243 116 97 44 N ATOM 4823 CA TYR B 306 -17.084 37.772 25.908 1.00 20.30 C ANISOU 4823 CA TYR B 306 2476 2830 2406 140 90 45 C ATOM 4824 C TYR B 306 -16.612 38.875 24.969 1.00 20.20 C ANISOU 4824 C TYR B 306 2465 2820 2390 176 101 82 C ATOM 4825 O TYR B 306 -16.542 38.679 23.748 1.00 23.71 O ANISOU 4825 O TYR B 306 2907 3294 2806 197 100 89 O ATOM 4826 CB TYR B 306 -18.519 38.027 26.371 1.00 17.59 C ANISOU 4826 CB TYR B 306 2116 2510 2059 141 81 31 C ATOM 4827 CG TYR B 306 -19.626 37.789 25.381 1.00 17.99 C ANISOU 4827 CG TYR B 306 2146 2612 2076 157 68 18 C ATOM 4828 CD1 TYR B 306 -19.415 37.090 24.195 1.00 18.94 C ANISOU 4828 CD1 TYR B 306 2265 2763 2170 164 62 10 C ATOM 4829 CD2 TYR B 306 -20.898 38.277 25.639 1.00 19.69 C ANISOU 4829 CD2 TYR B 306 2343 2851 2289 166 62 12 C ATOM 4830 CE1 TYR B 306 -20.457 36.878 23.303 1.00 19.62 C ANISOU 4830 CE1 TYR B 306 2330 2901 2224 180 48 -6 C ATOM 4831 CE2 TYR B 306 -21.933 38.077 24.761 1.00 18.03 C ANISOU 4831 CE2 TYR B 306 2110 2691 2049 181 48 -2 C ATOM 4832 CZ TYR B 306 -21.714 37.378 23.596 1.00 18.19 C ANISOU 4832 CZ TYR B 306 2128 2742 2041 189 40 -12 C ATOM 4833 OH TYR B 306 -22.765 37.185 22.728 1.00 21.63 O ANISOU 4833 OH TYR B 306 2540 3232 2446 205 23 -30 O ATOM 4834 N ILE B 307 -16.289 40.043 25.526 1.00 21.81 N ANISOU 4834 N ILE B 307 2673 2993 2622 186 113 106 N ATOM 4835 CA ILE B 307 -15.808 41.168 24.732 1.00 21.49 C ANISOU 4835 CA ILE B 307 2634 2947 2586 221 129 145 C ATOM 4836 C ILE B 307 -14.436 40.867 24.141 1.00 21.60 C ANISOU 4836 C ILE B 307 2662 2942 2605 221 140 160 C ATOM 4837 O ILE B 307 -14.149 41.223 22.994 1.00 24.93 O ANISOU 4837 O ILE B 307 3083 3379 3010 251 151 187 O ATOM 4838 CB ILE B 307 -15.781 42.443 25.596 1.00 21.82 C ANISOU 4838 CB ILE B 307 2675 2952 2665 226 140 162 C ATOM 4839 CG1 ILE B 307 -17.195 42.826 26.035 1.00 23.77 C ANISOU 4839 CG1 ILE B 307 2906 3220 2904 232 130 150 C ATOM 4840 CG2 ILE B 307 -15.113 43.590 24.847 1.00 26.36 C ANISOU 4840 CG2 ILE B 307 3251 3510 3254 259 161 204 C ATOM 4841 CD1 ILE B 307 -17.232 43.923 27.080 1.00 31.95 C ANISOU 4841 CD1 ILE B 307 3943 4220 3978 232 140 157 C ATOM 4842 N AMET B 308 -13.568 40.213 24.915 0.45 20.91 N ANISOU 4842 N AMET B 308 2585 2821 2537 190 140 146 N ATOM 4843 N BMET B 308 -13.567 40.213 24.913 0.55 20.87 N ANISOU 4843 N BMET B 308 2580 2817 2533 190 140 146 N ATOM 4844 CA AMET B 308 -12.202 39.954 24.471 0.45 23.02 C ANISOU 4844 CA AMET B 308 2864 3067 2815 189 152 160 C ATOM 4845 CA BMET B 308 -12.201 39.959 24.466 0.55 23.02 C ANISOU 4845 CA BMET B 308 2864 3067 2815 189 152 160 C ATOM 4846 C AMET B 308 -12.110 38.820 23.454 0.45 22.83 C ANISOU 4846 C AMET B 308 2843 3075 2756 190 146 148 C ATOM 4847 C BMET B 308 -12.103 38.814 23.461 0.55 22.83 C ANISOU 4847 C BMET B 308 2843 3075 2756 190 146 148 C ATOM 4848 O AMET B 308 -11.177 38.803 22.645 0.45 22.40 O ANISOU 4848 O AMET B 308 2795 3016 2699 203 160 168 O ATOM 4849 O BMET B 308 -11.158 38.782 22.667 0.55 22.40 O ANISOU 4849 O BMET B 308 2796 3015 2699 202 159 168 O ATOM 4850 CB AMET B 308 -11.311 39.632 25.672 0.45 22.79 C ANISOU 4850 CB AMET B 308 2845 2995 2820 158 151 147 C ATOM 4851 CB BMET B 308 -11.301 39.662 25.668 0.55 22.79 C ANISOU 4851 CB BMET B 308 2844 2994 2820 158 152 148 C ATOM 4852 CG AMET B 308 -10.986 40.822 26.553 0.45 23.02 C ANISOU 4852 CG AMET B 308 2873 2985 2888 159 159 160 C ATOM 4853 CG BMET B 308 -11.114 40.837 26.608 0.55 23.02 C ANISOU 4853 CG BMET B 308 2872 2987 2887 159 158 158 C ATOM 4854 SD AMET B 308 -10.083 40.324 28.034 0.45 33.75 S ANISOU 4854 SD AMET B 308 4242 4304 4279 123 152 137 S ATOM 4855 SD BMET B 308 -10.164 42.180 25.876 0.55 32.51 S ANISOU 4855 SD BMET B 308 4073 4161 4119 188 184 202 S ATOM 4856 CE AMET B 308 -8.835 39.256 27.319 0.45 25.29 C ANISOU 4856 CE AMET B 308 3180 3228 3201 116 158 141 C ATOM 4857 CE BMET B 308 -8.628 41.341 25.488 0.55 22.05 C ANISOU 4857 CE BMET B 308 2759 2818 2802 176 191 206 C ATOM 4858 N MET B 309 -13.040 37.863 23.477 1.00 17.58 N ANISOU 4858 N MET B 309 2171 2442 2065 176 129 116 N ATOM 4859 CA MET B 309 -12.893 36.647 22.680 1.00 23.88 C ANISOU 4859 CA MET B 309 2972 3265 2836 170 124 96 C ATOM 4860 C MET B 309 -14.029 36.360 21.698 1.00 23.90 C ANISOU 4860 C MET B 309 2961 3324 2796 188 110 81 C ATOM 4861 O MET B 309 -14.124 35.225 21.212 1.00 23.57 O ANISOU 4861 O MET B 309 2918 3304 2734 177 102 53 O ATOM 4862 CB MET B 309 -12.714 35.441 23.607 1.00 19.93 C ANISOU 4862 CB MET B 309 2478 2746 2349 130 116 64 C ATOM 4863 CG MET B 309 -11.557 35.591 24.580 1.00 20.42 C ANISOU 4863 CG MET B 309 2554 2758 2448 113 126 75 C ATOM 4864 SD MET B 309 -11.158 34.071 25.442 1.00 21.91 S ANISOU 4864 SD MET B 309 2752 2927 2648 74 121 45 S ATOM 4865 CE MET B 309 -10.292 33.161 24.165 1.00 19.23 C ANISOU 4865 CE MET B 309 2420 2598 2290 80 128 44 C ATOM 4866 N ASN B 310 -14.899 37.321 21.392 1.00 23.97 N ANISOU 4866 N ASN B 310 2957 3357 2793 215 108 96 N ATOM 4867 CA ASN B 310 -15.916 37.108 20.355 1.00 25.47 C ANISOU 4867 CA ASN B 310 3131 3606 2940 238 94 83 C ATOM 4868 C ASN B 310 -16.007 38.380 19.516 1.00 27.47 C ANISOU 4868 C ASN B 310 3381 3878 3179 285 105 125 C ATOM 4869 O ASN B 310 -16.578 39.384 19.955 1.00 18.71 O ANISOU 4869 O ASN B 310 2263 2762 2083 297 108 142 O ATOM 4870 CB ASN B 310 -17.271 36.726 20.946 1.00 24.42 C ANISOU 4870 CB ASN B 310 2980 3494 2803 220 75 48 C ATOM 4871 CG ASN B 310 -18.272 36.294 19.879 1.00 24.67 C ANISOU 4871 CG ASN B 310 2993 3588 2792 238 57 25 C ATOM 4872 OD1 ASN B 310 -18.994 37.118 19.324 1.00 24.05 O ANISOU 4872 OD1 ASN B 310 2901 3543 2693 272 53 41 O ATOM 4873 ND2 ASN B 310 -18.312 34.998 19.585 1.00 19.09 N ANISOU 4873 ND2 ASN B 310 2284 2897 2073 216 46 -14 N ATOM 4874 N LYS B 311 -15.443 38.320 18.303 1.00 27.01 N ANISOU 4874 N LYS B 311 3328 3842 3093 312 113 142 N ATOM 4875 CA LYS B 311 -15.305 39.510 17.470 1.00 25.22 C ANISOU 4875 CA LYS B 311 3102 3627 2855 360 130 190 C ATOM 4876 C LYS B 311 -16.659 40.086 17.077 1.00 25.81 C ANISOU 4876 C LYS B 311 3156 3749 2901 390 117 192 C ATOM 4877 O LYS B 311 -16.853 41.307 17.105 1.00 28.71 O ANISOU 4877 O LYS B 311 3520 4108 3280 418 130 229 O ATOM 4878 CB LYS B 311 -14.480 39.172 16.228 1.00 26.89 C ANISOU 4878 CB LYS B 311 3322 3858 3036 384 140 204 C ATOM 4879 CG LYS B 311 -14.607 40.170 15.088 1.00 20.87 C ANISOU 4879 CG LYS B 311 2556 3128 2244 440 155 249 C ATOM 4880 CD LYS B 311 -13.747 39.754 13.907 1.00 37.48 C ANISOU 4880 CD LYS B 311 4672 5252 4317 464 167 262 C ATOM 4881 N GLN B 312 -17.606 39.221 16.704 1.00 27.80 N ANISOU 4881 N GLN B 312 3394 4052 3118 385 91 151 N ATOM 4882 CA GLN B 312 -18.919 39.691 16.273 1.00 23.94 C ANISOU 4882 CA GLN B 312 2882 3614 2599 415 76 149 C ATOM 4883 C GLN B 312 -19.620 40.458 17.382 1.00 23.87 C ANISOU 4883 C GLN B 312 2864 3580 2625 404 76 155 C ATOM 4884 O GLN B 312 -20.140 41.556 17.161 1.00 22.82 O ANISOU 4884 O GLN B 312 2723 3461 2488 440 82 187 O ATOM 4885 CB GLN B 312 -19.772 38.508 15.820 1.00 30.58 C ANISOU 4885 CB GLN B 312 3706 4509 3404 403 46 96 C ATOM 4886 CG GLN B 312 -21.216 38.851 15.512 1.00 29.55 C ANISOU 4886 CG GLN B 312 3548 4433 3247 427 25 84 C ATOM 4887 CD GLN B 312 -21.982 37.657 14.979 1.00 35.24 C ANISOU 4887 CD GLN B 312 4249 5206 3933 416 -4 28 C ATOM 4888 OE1 GLN B 312 -22.394 37.637 13.818 1.00 36.63 O ANISOU 4888 OE1 GLN B 312 4413 5443 4061 453 -17 23 O ATOM 4889 NE2 GLN B 312 -22.169 36.649 15.822 1.00 24.92 N ANISOU 4889 NE2 GLN B 312 2938 3876 2653 365 -13 -17 N ATOM 4890 N PHE B 313 -19.631 39.901 18.593 1.00 22.69 N ANISOU 4890 N PHE B 313 2718 3395 2509 357 71 125 N ATOM 4891 CA PHE B 313 -20.266 40.599 19.705 1.00 21.70 C ANISOU 4891 CA PHE B 313 2585 3244 2416 347 72 128 C ATOM 4892 C PHE B 313 -19.543 41.903 20.029 1.00 23.02 C ANISOU 4892 C PHE B 313 2765 3366 2616 365 98 175 C ATOM 4893 O PHE B 313 -20.187 42.925 20.302 1.00 21.02 O ANISOU 4893 O PHE B 313 2502 3111 2373 384 103 195 O ATOM 4894 CB PHE B 313 -20.323 39.692 20.936 1.00 21.10 C ANISOU 4894 CB PHE B 313 2512 3139 2367 295 64 89 C ATOM 4895 CG PHE B 313 -20.896 40.365 22.150 1.00 23.48 C ANISOU 4895 CG PHE B 313 2808 3413 2700 284 67 91 C ATOM 4896 CD1 PHE B 313 -22.267 40.480 22.309 1.00 23.99 C ANISOU 4896 CD1 PHE B 313 2850 3510 2755 289 54 74 C ATOM 4897 CD2 PHE B 313 -20.065 40.908 23.115 1.00 19.19 C ANISOU 4897 CD2 PHE B 313 2282 2814 2197 270 84 107 C ATOM 4898 CE1 PHE B 313 -22.800 41.109 23.421 1.00 26.09 C ANISOU 4898 CE1 PHE B 313 3111 3752 3049 280 58 75 C ATOM 4899 CE2 PHE B 313 -20.591 41.539 24.225 1.00 20.78 C ANISOU 4899 CE2 PHE B 313 2479 2992 2425 261 87 106 C ATOM 4900 CZ PHE B 313 -21.957 41.641 24.378 1.00 23.95 C ANISOU 4900 CZ PHE B 313 2860 3426 2815 267 75 91 C ATOM 4901 N ARG B 314 -18.207 41.886 20.008 1.00 20.92 N ANISOU 4901 N ARG B 314 2518 3061 2368 357 116 193 N ATOM 4902 CA ARG B 314 -17.442 43.091 20.321 1.00 26.02 C ANISOU 4902 CA ARG B 314 3174 3660 3052 371 142 235 C ATOM 4903 C ARG B 314 -17.730 44.203 19.319 1.00 23.49 C ANISOU 4903 C ARG B 314 2847 3363 2715 424 156 279 C ATOM 4904 O ARG B 314 -17.802 45.381 19.686 1.00 22.94 O ANISOU 4904 O ARG B 314 2775 3266 2675 440 173 308 O ATOM 4905 CB ARG B 314 -15.946 42.763 20.355 1.00 27.72 C ANISOU 4905 CB ARG B 314 3409 3834 3289 354 157 243 C ATOM 4906 CG ARG B 314 -15.029 43.976 20.441 1.00 33.11 C ANISOU 4906 CG ARG B 314 4099 4470 4011 371 186 287 C ATOM 4907 CD ARG B 314 -13.567 43.579 20.674 1.00 32.81 C ANISOU 4907 CD ARG B 314 4077 4389 4001 348 198 289 C ATOM 4908 NE ARG B 314 -12.930 42.967 19.510 1.00 30.78 N ANISOU 4908 NE ARG B 314 3827 4155 3714 362 204 299 N ATOM 4909 CZ ARG B 314 -12.617 41.680 19.411 1.00 30.08 C ANISOU 4909 CZ ARG B 314 3744 4078 3606 338 190 268 C ATOM 4910 NH1 ARG B 314 -12.913 40.819 20.371 1.00 31.69 N ANISOU 4910 NH1 ARG B 314 3948 4274 3817 299 171 227 N ATOM 4911 NH2 ARG B 314 -11.985 41.247 18.325 1.00 34.88 N ANISOU 4911 NH2 ARG B 314 4360 4705 4189 356 199 280 N ATOM 4912 N ASN B 315 -17.898 43.850 18.045 1.00 26.40 N ANISOU 4912 N ASN B 315 3212 3784 3036 454 151 285 N ATOM 4913 CA ASN B 315 -18.247 44.859 17.052 1.00 29.58 C ANISOU 4913 CA ASN B 315 3608 4216 3416 510 164 330 C ATOM 4914 C ASN B 315 -19.666 45.377 17.258 1.00 28.33 C ANISOU 4914 C ASN B 315 3428 4089 3248 526 150 325 C ATOM 4915 O ASN B 315 -19.925 46.573 17.074 1.00 29.30 O ANISOU 4915 O ASN B 315 3546 4207 3380 563 168 366 O ATOM 4916 CB ASN B 315 -18.068 44.294 15.645 1.00 26.87 C ANISOU 4916 CB ASN B 315 3266 3926 3019 540 160 335 C ATOM 4917 CG ASN B 315 -16.610 44.099 15.287 1.00 27.98 C ANISOU 4917 CG ASN B 315 3426 4034 3170 536 183 355 C ATOM 4918 OD1 ASN B 315 -15.721 44.595 15.980 1.00 28.16 O ANISOU 4918 OD1 ASN B 315 3461 3996 3245 519 204 373 O ATOM 4919 ND2 ASN B 315 -16.356 43.386 14.198 1.00 25.65 N ANISOU 4919 ND2 ASN B 315 3135 3781 2830 553 178 350 N ATOM 4920 N CYS B 316 -20.598 44.497 17.638 1.00 31.29 N ANISOU 4920 N CYS B 316 3790 4494 3606 500 120 276 N ATOM 4921 CA CYS B 316 -21.962 44.944 17.907 1.00 29.20 C ANISOU 4921 CA CYS B 316 3502 4257 3335 513 106 268 C ATOM 4922 C CYS B 316 -21.997 45.941 19.058 1.00 24.62 C ANISOU 4922 C CYS B 316 2925 3623 2807 503 123 284 C ATOM 4923 O CYS B 316 -22.741 46.925 19.010 1.00 27.01 O ANISOU 4923 O CYS B 316 3215 3936 3112 534 129 308 O ATOM 4924 CB CYS B 316 -22.873 43.751 18.207 1.00 23.25 C ANISOU 4924 CB CYS B 316 2732 3538 2562 480 74 210 C ATOM 4925 SG CYS B 316 -23.242 42.701 16.778 1.00 30.73 S ANISOU 4925 SG CYS B 316 3667 4563 3444 499 49 183 S ATOM 4926 N MET B 317 -21.200 45.702 20.103 1.00 25.68 N ANISOU 4926 N MET B 317 3075 3701 2982 461 131 270 N ATOM 4927 CA MET B 317 -21.172 46.620 21.237 1.00 27.89 C ANISOU 4927 CA MET B 317 3357 3928 3310 450 145 280 C ATOM 4928 C MET B 317 -20.626 47.985 20.836 1.00 30.90 C ANISOU 4928 C MET B 317 3744 4281 3715 488 176 334 C ATOM 4929 O MET B 317 -21.152 49.022 21.259 1.00 33.78 O ANISOU 4929 O MET B 317 4102 4630 4104 504 187 351 O ATOM 4930 CB MET B 317 -20.340 46.030 22.376 1.00 22.87 C ANISOU 4930 CB MET B 317 2737 3243 2709 400 145 253 C ATOM 4931 CG MET B 317 -20.312 46.895 23.631 1.00 33.94 C ANISOU 4931 CG MET B 317 4142 4595 4159 387 157 255 C ATOM 4932 SD MET B 317 -19.230 46.208 24.894 1.00 42.51 S ANISOU 4932 SD MET B 317 5246 5627 5278 335 156 226 S ATOM 4933 CE MET B 317 -17.800 45.789 23.903 1.00 43.04 C ANISOU 4933 CE MET B 317 5328 5685 5339 339 167 246 C ATOM 4934 N VAL B 318 -19.562 48.008 20.031 1.00 29.42 N ANISOU 4934 N VAL B 318 3570 4085 3524 503 193 362 N ATOM 4935 CA VAL B 318 -19.019 49.281 19.561 1.00 31.48 C ANISOU 4935 CA VAL B 318 3835 4318 3809 541 227 417 C ATOM 4936 C VAL B 318 -20.049 50.012 18.710 1.00 33.27 C ANISOU 4936 C VAL B 318 4046 4591 4005 594 230 448 C ATOM 4937 O VAL B 318 -20.234 51.228 18.839 1.00 36.47 O ANISOU 4937 O VAL B 318 4446 4971 4440 620 253 482 O ATOM 4938 CB VAL B 318 -17.701 49.056 18.795 1.00 38.30 C ANISOU 4938 CB VAL B 318 4713 5167 4671 547 245 440 C ATOM 4939 CG1 VAL B 318 -17.252 50.338 18.128 1.00 30.57 C ANISOU 4939 CG1 VAL B 318 3736 4166 3713 592 283 501 C ATOM 4940 CG2 VAL B 318 -16.621 48.541 19.742 1.00 29.32 C ANISOU 4940 CG2 VAL B 318 3590 3976 3574 497 246 415 C ATOM 4941 N THR B 319 -20.750 49.277 17.841 1.00 33.32 N ANISOU 4941 N THR B 319 4042 4666 3953 611 206 434 N ATOM 4942 CA THR B 319 -21.823 49.872 17.048 1.00 31.05 C ANISOU 4942 CA THR B 319 3736 4431 3629 662 203 459 C ATOM 4943 C THR B 319 -22.938 50.414 17.937 1.00 33.26 C ANISOU 4943 C THR B 319 4001 4707 3931 658 195 446 C ATOM 4944 O THR B 319 -23.460 51.509 17.695 1.00 34.07 O ANISOU 4944 O THR B 319 4093 4813 4039 699 211 484 O ATOM 4945 CB THR B 319 -22.370 48.836 16.063 1.00 27.43 C ANISOU 4945 CB THR B 319 3268 4050 3104 675 173 434 C ATOM 4946 OG1 THR B 319 -21.320 48.417 15.182 1.00 35.35 O ANISOU 4946 OG1 THR B 319 4286 5058 4086 685 184 449 O ATOM 4947 CG2 THR B 319 -23.523 49.410 15.243 1.00 34.29 C ANISOU 4947 CG2 THR B 319 4116 4981 3933 730 166 456 C ATOM 4948 N THR B 320 -23.319 49.659 18.970 1.00 32.37 N ANISOU 4948 N THR B 320 3884 4586 3830 609 173 394 N ATOM 4949 CA THR B 320 -24.359 50.112 19.892 1.00 31.58 C ANISOU 4949 CA THR B 320 3769 4480 3750 602 166 379 C ATOM 4950 C THR B 320 -23.879 51.281 20.745 1.00 37.00 C ANISOU 4950 C THR B 320 4466 5098 4496 600 196 404 C ATOM 4951 O THR B 320 -24.608 52.263 20.929 1.00 39.68 O ANISOU 4951 O THR B 320 4793 5434 4850 626 206 424 O ATOM 4952 CB THR B 320 -24.809 48.950 20.778 1.00 33.10 C ANISOU 4952 CB THR B 320 3957 4680 3941 550 138 320 C ATOM 4953 OG1 THR B 320 -25.777 48.160 20.077 1.00 31.72 O ANISOU 4953 OG1 THR B 320 3761 4574 3716 560 109 295 O ATOM 4954 CG2 THR B 320 -25.412 49.454 22.092 1.00 30.05 C ANISOU 4954 CG2 THR B 320 3565 4260 3593 530 141 305 C ATOM 4955 N LEU B 321 -22.653 51.197 21.265 1.00 37.04 N ANISOU 4955 N LEU B 321 4490 5046 4537 570 210 402 N ATOM 4956 CA LEU B 321 -22.129 52.248 22.130 1.00 38.22 C ANISOU 4956 CA LEU B 321 4647 5128 4746 563 236 417 C ATOM 4957 C LEU B 321 -21.833 53.532 21.360 1.00 40.18 C ANISOU 4957 C LEU B 321 4896 5359 5012 612 271 477 C ATOM 4958 O LEU B 321 -21.994 54.630 21.905 1.00 43.13 O ANISOU 4958 O LEU B 321 5266 5693 5429 623 291 493 O ATOM 4959 CB LEU B 321 -20.871 51.749 22.836 1.00 41.59 C ANISOU 4959 CB LEU B 321 5092 5505 5204 518 239 396 C ATOM 4960 CG LEU B 321 -20.834 51.845 24.358 1.00 43.28 C ANISOU 4960 CG LEU B 321 5311 5674 5460 479 235 362 C ATOM 4961 CD1 LEU B 321 -22.139 51.353 24.950 1.00 41.83 C ANISOU 4961 CD1 LEU B 321 5114 5526 5253 466 210 327 C ATOM 4962 CD2 LEU B 321 -19.662 51.038 24.900 1.00 43.52 C ANISOU 4962 CD2 LEU B 321 5357 5673 5505 436 230 337 C ATOM 4963 N CYS B 322 -21.403 53.424 20.110 1.00 42.13 N ANISOU 4963 N CYS B 322 5145 5633 5228 644 280 510 N ATOM 4964 CA CYS B 322 -21.073 54.605 19.321 1.00 42.32 C ANISOU 4964 CA CYS B 322 5171 5641 5269 694 317 572 C ATOM 4965 C CYS B 322 -22.064 54.808 18.181 1.00 48.79 C ANISOU 4965 C CYS B 322 5976 6530 6034 750 312 601 C ATOM 4966 O CYS B 322 -21.670 55.109 17.053 1.00 51.51 O ANISOU 4966 O CYS B 322 6323 6891 6357 792 332 647 O ATOM 4967 CB CYS B 322 -19.654 54.497 18.767 1.00 44.38 C ANISOU 4967 CB CYS B 322 5447 5872 5541 692 339 596 C ATOM 4968 SG CYS B 322 -18.393 54.241 20.029 1.00 54.89 S ANISOU 4968 SG CYS B 322 6793 7127 6934 630 343 562 S TER 4969 CYS B 322 HETATM 4970 C1 NAG C 1 10.521 22.277 0.378 1.00 25.65 C ANISOU 4970 C1 NAG C 1 3451 3608 2687 561 623 188 C HETATM 4971 C2 NAG C 1 9.032 22.361 0.760 1.00 25.41 C ANISOU 4971 C2 NAG C 1 3414 3608 2634 545 578 150 C HETATM 4972 C3 NAG C 1 8.209 21.314 -0.007 1.00 24.01 C ANISOU 4972 C3 NAG C 1 3242 3484 2396 552 556 80 C HETATM 4973 C4 NAG C 1 8.507 21.337 -1.500 1.00 28.84 C ANISOU 4973 C4 NAG C 1 3865 4151 2942 609 580 88 C HETATM 4974 C5 NAG C 1 10.012 21.249 -1.727 1.00 30.03 C ANISOU 4974 C5 NAG C 1 4024 4265 3122 621 626 128 C HETATM 4975 C6 NAG C 1 10.413 21.340 -3.184 1.00 26.56 C ANISOU 4975 C6 NAG C 1 3597 3877 2618 680 657 144 C HETATM 4976 C7 NAG C 1 8.282 23.072 2.996 1.00 24.79 C ANISOU 4976 C7 NAG C 1 3315 3464 2640 476 537 159 C HETATM 4977 C8 NAG C 1 8.189 22.692 4.444 1.00 30.26 C ANISOU 4977 C8 NAG C 1 4001 4106 3392 422 516 140 C HETATM 4978 N2 NAG C 1 8.864 22.175 2.193 1.00 28.02 N ANISOU 4978 N2 NAG C 1 3735 3886 3026 491 555 137 N HETATM 4979 O3 NAG C 1 6.823 21.561 0.198 1.00 25.36 O ANISOU 4979 O3 NAG C 1 3404 3689 2541 545 517 52 O HETATM 4980 O4 NAG C 1 7.875 20.217 -2.114 1.00 26.46 O ANISOU 4980 O4 NAG C 1 3568 3892 2593 610 559 14 O HETATM 4981 O5 NAG C 1 10.659 22.332 -1.047 1.00 25.28 O ANISOU 4981 O5 NAG C 1 3414 3615 2574 615 646 196 O HETATM 4982 O6 NAG C 1 10.040 22.585 -3.759 1.00 28.05 O ANISOU 4982 O6 NAG C 1 3784 4104 2768 725 666 194 O HETATM 4983 O7 NAG C 1 7.859 24.144 2.577 1.00 33.12 O ANISOU 4983 O7 NAG C 1 4368 4549 3669 507 541 193 O HETATM 4984 C1 NAG C 2 6.960 20.582 -3.177 1.00 30.04 C ANISOU 4984 C1 NAG C 2 4022 4425 2966 656 545 1 C HETATM 4985 C2 NAG C 2 6.644 19.311 -3.968 1.00 29.42 C ANISOU 4985 C2 NAG C 2 3949 4388 2841 661 532 -77 C HETATM 4986 C3 NAG C 2 5.668 19.624 -5.097 1.00 35.55 C ANISOU 4986 C3 NAG C 2 4724 5254 3529 710 513 -98 C HETATM 4987 C4 NAG C 2 4.422 20.293 -4.533 1.00 32.66 C ANISOU 4987 C4 NAG C 2 4342 4904 3162 696 476 -100 C HETATM 4988 C5 NAG C 2 4.819 21.527 -3.727 1.00 36.09 C ANISOU 4988 C5 NAG C 2 4774 5291 3648 690 494 -19 C HETATM 4989 C6 NAG C 2 3.644 22.196 -3.051 1.00 38.28 C ANISOU 4989 C6 NAG C 2 5036 5577 3932 674 459 -19 C HETATM 4990 C7 NAG C 2 8.409 17.612 -3.958 1.00 32.52 C ANISOU 4990 C7 NAG C 2 4358 4713 3286 635 573 -107 C HETATM 4991 C8 NAG C 2 9.663 17.126 -4.612 1.00 28.67 C ANISOU 4991 C8 NAG C 2 3884 4213 2796 658 614 -94 C HETATM 4992 N2 NAG C 2 7.857 18.705 -4.491 1.00 33.24 N ANISOU 4992 N2 NAG C 2 4446 4854 3328 675 569 -72 N HETATM 4993 O3 NAG C 2 5.320 18.425 -5.779 1.00 36.68 O ANISOU 4993 O3 NAG C 2 4870 5435 3631 712 497 -178 O HETATM 4994 O4 NAG C 2 3.538 20.666 -5.585 1.00 43.03 O ANISOU 4994 O4 NAG C 2 5653 6304 4393 746 458 -114 O HETATM 4995 O5 NAG C 2 5.743 21.159 -2.688 1.00 29.36 O ANISOU 4995 O5 NAG C 2 3923 4358 2875 644 509 -6 O HETATM 4996 O6 NAG C 2 2.800 21.243 -2.419 1.00 38.02 O ANISOU 4996 O6 NAG C 2 4993 5538 3917 626 421 -92 O HETATM 4997 O7 NAG C 2 7.918 17.043 -2.988 1.00 30.08 O ANISOU 4997 O7 NAG C 2 4040 4369 3020 585 547 -144 O HETATM 4998 C1 NAG D 1 -20.024 34.625 75.224 1.00 29.84 C ANISOU 4998 C1 NAG D 1 4107 4446 2784 644 304 -115 C HETATM 4999 C2 NAG D 1 -21.522 34.565 74.857 1.00 30.25 C ANISOU 4999 C2 NAG D 1 4151 4474 2869 623 353 -91 C HETATM 5000 C3 NAG D 1 -22.315 35.636 75.614 1.00 31.65 C ANISOU 5000 C3 NAG D 1 4331 4677 3019 647 357 -128 C HETATM 5001 C4 NAG D 1 -22.004 35.624 77.106 1.00 36.36 C ANISOU 5001 C4 NAG D 1 4950 5333 3533 708 356 -134 C HETATM 5002 C5 NAG D 1 -20.497 35.696 77.316 1.00 29.13 C ANISOU 5002 C5 NAG D 1 4039 4437 2592 722 304 -161 C HETATM 5003 C6 NAG D 1 -20.075 35.638 78.768 1.00 33.90 C ANISOU 5003 C6 NAG D 1 4664 5105 3109 785 297 -168 C HETATM 5004 C7 NAG D 1 -22.218 33.781 72.631 1.00 29.93 C ANISOU 5004 C7 NAG D 1 4081 4348 2944 538 380 -50 C HETATM 5005 C8 NAG D 1 -22.343 34.134 71.179 1.00 32.63 C ANISOU 5005 C8 NAG D 1 4399 4643 3355 486 364 -65 C HETATM 5006 N2 NAG D 1 -21.706 34.728 73.423 1.00 32.01 N ANISOU 5006 N2 NAG D 1 4352 4645 3166 568 346 -96 N HETATM 5007 O3 NAG D 1 -23.708 35.419 75.411 1.00 32.41 O ANISOU 5007 O3 NAG D 1 4419 4756 3139 635 408 -99 O HETATM 5008 O4 NAG D 1 -22.613 36.757 77.717 1.00 35.06 O ANISOU 5008 O4 NAG D 1 4786 5190 3347 728 353 -180 O HETATM 5009 O5 NAG D 1 -19.873 34.591 76.648 1.00 34.61 O ANISOU 5009 O5 NAG D 1 4732 5108 3311 701 307 -117 O HETATM 5010 O6 NAG D 1 -20.615 34.509 79.442 1.00 28.81 O ANISOU 5010 O6 NAG D 1 4038 4484 2426 817 350 -104 O HETATM 5011 O7 NAG D 1 -22.559 32.686 73.066 1.00 36.40 O ANISOU 5011 O7 NAG D 1 4909 5175 3745 552 422 -1 O HETATM 5012 C1 NAG D 2 -23.613 36.376 78.691 1.00 40.25 C ANISOU 5012 C1 NAG D 2 5457 5878 3958 765 404 -147 C HETATM 5013 C2 NAG D 2 -23.991 37.620 79.498 1.00 42.69 C ANISOU 5013 C2 NAG D 2 5770 6218 4232 794 392 -204 C HETATM 5014 C3 NAG D 2 -25.072 37.278 80.517 1.00 48.48 C ANISOU 5014 C3 NAG D 2 6519 6986 4917 835 448 -171 C HETATM 5015 C4 NAG D 2 -26.261 36.620 79.829 1.00 49.26 C ANISOU 5015 C4 NAG D 2 6605 7044 5068 803 503 -118 C HETATM 5016 C5 NAG D 2 -25.800 35.428 78.994 1.00 42.12 C ANISOU 5016 C5 NAG D 2 5695 6107 4202 771 510 -68 C HETATM 5017 C6 NAG D 2 -26.916 34.824 78.174 1.00 47.16 C ANISOU 5017 C6 NAG D 2 6316 6701 4900 732 559 -24 C HETATM 5018 C7 NAG D 2 -22.147 39.228 79.659 1.00 46.07 C ANISOU 5018 C7 NAG D 2 6192 6665 4646 801 286 -317 C HETATM 5019 C8 NAG D 2 -20.980 39.699 80.474 1.00 43.85 C ANISOU 5019 C8 NAG D 2 5920 6429 4314 836 235 -369 C HETATM 5020 N2 NAG D 2 -22.829 38.193 80.158 1.00 45.41 N ANISOU 5020 N2 NAG D 2 6123 6600 4530 824 339 -255 N HETATM 5021 O3 NAG D 2 -25.495 38.468 81.173 1.00 46.54 O ANISOU 5021 O3 NAG D 2 6275 6764 4644 859 437 -226 O HETATM 5022 O4 NAG D 2 -27.198 36.175 80.803 1.00 57.23 O ANISOU 5022 O4 NAG D 2 7627 8084 6033 842 559 -80 O HETATM 5023 O5 NAG D 2 -24.784 35.837 78.066 1.00 41.80 O ANISOU 5023 O5 NAG D 2 5643 6039 4200 736 455 -103 O HETATM 5024 O6 NAG D 2 -27.804 35.826 77.698 1.00 54.02 O ANISOU 5024 O6 NAG D 2 7166 7550 5808 709 558 -59 O HETATM 5025 O7 NAG D 2 -22.457 39.760 78.598 1.00 44.25 O ANISOU 5025 O7 NAG D 2 5943 6387 4484 755 281 -331 O HETATM 5026 C ACE A 401 17.478 35.083 4.692 1.00 44.41 C ANISOU 5026 C ACE A 401 5661 5517 5697 568 899 793 C HETATM 5027 O ACE A 401 18.476 34.694 5.297 1.00 45.15 O ANISOU 5027 O ACE A 401 5741 5569 5844 539 900 784 O HETATM 5028 CH3 ACE A 401 17.561 36.132 3.625 1.00 44.20 C ANISOU 5028 CH3 ACE A 401 5633 5500 5660 619 950 857 C HETATM 5029 C1 RET A 402 10.698 31.974 30.908 1.00 22.62 C ANISOU 5029 C1 RET A 402 2827 2572 3194 -3 182 166 C HETATM 5030 C2 RET A 402 11.358 32.538 32.168 1.00 24.09 C ANISOU 5030 C2 RET A 402 2995 2745 3413 -8 160 150 C HETATM 5031 C3 RET A 402 11.872 31.480 33.075 1.00 23.37 C ANISOU 5031 C3 RET A 402 2906 2660 3313 -12 144 140 C HETATM 5032 C4 RET A 402 10.716 30.608 33.541 1.00 23.82 C ANISOU 5032 C4 RET A 402 2987 2740 3325 -16 135 130 C HETATM 5033 C5 RET A 402 9.774 30.217 32.438 1.00 22.09 C ANISOU 5033 C5 RET A 402 2785 2534 3076 -14 154 139 C HETATM 5034 C6 RET A 402 9.906 30.708 31.185 1.00 25.20 C ANISOU 5034 C6 RET A 402 3176 2921 3479 -7 175 156 C HETATM 5035 C7 RET A 402 9.284 30.119 30.011 1.00 23.95 C ANISOU 5035 C7 RET A 402 3032 2777 3290 -3 193 164 C HETATM 5036 C8 RET A 402 8.888 28.827 29.815 1.00 19.74 C ANISOU 5036 C8 RET A 402 2516 2257 2727 -6 197 158 C HETATM 5037 C9 RET A 402 8.684 28.205 28.584 1.00 17.32 C ANISOU 5037 C9 RET A 402 2220 1960 2400 0 216 165 C HETATM 5038 C10 RET A 402 8.504 26.815 28.503 1.00 23.94 C ANISOU 5038 C10 RET A 402 3072 2806 3218 -6 219 156 C HETATM 5039 C11 RET A 402 9.159 25.918 27.682 1.00 22.20 C ANISOU 5039 C11 RET A 402 2857 2582 2996 -1 237 162 C HETATM 5040 C12 RET A 402 9.061 24.542 27.678 1.00 20.20 C ANISOU 5040 C12 RET A 402 2616 2330 2729 -7 242 151 C HETATM 5041 C13 RET A 402 9.908 23.610 27.048 1.00 21.53 C ANISOU 5041 C13 RET A 402 2788 2489 2902 -2 260 156 C HETATM 5042 C14 RET A 402 9.600 22.253 26.949 1.00 25.11 C ANISOU 5042 C14 RET A 402 3255 2944 3340 -8 267 143 C HETATM 5043 C15 RET A 402 10.431 21.301 26.370 1.00 22.13 C ANISOU 5043 C15 RET A 402 2882 2556 2970 -4 285 147 C HETATM 5044 C16 RET A 402 9.782 33.057 30.315 1.00 23.65 C ANISOU 5044 C16 RET A 402 2958 2706 3321 3 192 172 C HETATM 5045 C17 RET A 402 11.808 31.674 29.889 1.00 32.72 C ANISOU 5045 C17 RET A 402 4100 3838 4494 5 206 187 C HETATM 5046 C18 RET A 402 8.708 29.264 32.906 1.00 24.23 C ANISOU 5046 C18 RET A 402 3075 2824 3307 -20 147 128 C HETATM 5047 C19 RET A 402 8.638 28.977 27.321 1.00 23.98 C ANISOU 5047 C19 RET A 402 3060 2808 3243 13 234 180 C HETATM 5048 C20 RET A 402 11.190 24.121 26.502 1.00 23.05 C ANISOU 5048 C20 RET A 402 2969 2667 3121 10 272 177 C HETATM 5049 C1 NAG A 403 21.175 34.020 7.013 1.00 35.85 C ANISOU 5049 C1 NAG A 403 4517 4279 4825 467 906 767 C HETATM 5050 C2 NAG A 403 20.831 35.406 7.556 1.00 39.02 C ANISOU 5050 C2 NAG A 403 4900 4652 5273 460 906 789 C HETATM 5051 C3 NAG A 403 21.803 36.441 6.997 1.00 47.11 C ANISOU 5051 C3 NAG A 403 5904 5641 6354 482 965 849 C HETATM 5052 C4 NAG A 403 23.237 36.033 7.302 1.00 47.16 C ANISOU 5052 C4 NAG A 403 5888 5607 6423 464 981 849 C HETATM 5053 C5 NAG A 403 23.504 34.621 6.786 1.00 45.51 C ANISOU 5053 C5 NAG A 403 5699 5430 6161 472 977 827 C HETATM 5054 C6 NAG A 403 24.867 34.098 7.177 1.00 45.30 C ANISOU 5054 C6 NAG A 403 5651 5366 6193 452 987 823 C HETATM 5055 C7 NAG A 403 18.753 36.639 7.978 1.00 39.74 C ANISOU 5055 C7 NAG A 403 5002 4770 5328 463 870 784 C HETATM 5056 C8 NAG A 403 17.350 36.898 7.523 1.00 35.86 C ANISOU 5056 C8 NAG A 403 4530 4327 4769 486 855 782 C HETATM 5057 N2 NAG A 403 19.458 35.771 7.245 1.00 38.25 N ANISOU 5057 N2 NAG A 403 4821 4595 5116 478 890 787 N HETATM 5058 O3 NAG A 403 21.530 37.721 7.556 1.00 45.40 O ANISOU 5058 O3 NAG A 403 5669 5392 6189 473 967 866 O HETATM 5059 O4 NAG A 403 24.144 36.941 6.686 1.00 51.21 O ANISOU 5059 O4 NAG A 403 6381 6088 6989 486 1040 906 O HETATM 5060 O5 NAG A 403 22.541 33.704 7.330 1.00 39.93 O ANISOU 5060 O5 NAG A 403 5014 4755 5403 451 922 772 O HETATM 5061 O6 NAG A 403 25.150 34.365 8.544 1.00 49.13 O ANISOU 5061 O6 NAG A 403 6111 5810 6745 409 955 798 O HETATM 5062 O7 NAG A 403 19.225 37.187 8.970 1.00 46.62 O ANISOU 5062 O7 NAG A 403 5850 5594 6271 432 862 780 O HETATM 5063 O1 DAO A 404 22.900 25.129 22.193 1.00 41.41 O ANISOU 5063 O1 DAO A 404 5162 4836 5738 100 448 354 O HETATM 5064 O2 DAO A 404 23.526 27.152 22.867 1.00 42.82 O ANISOU 5064 O2 DAO A 404 5296 4987 5985 92 439 366 O HETATM 5065 C1 DAO A 404 23.427 25.914 23.006 1.00 39.51 C ANISOU 5065 C1 DAO A 404 4895 4579 5538 92 433 354 C HETATM 5066 C2 DAO A 404 24.022 25.328 24.299 1.00 37.76 C ANISOU 5066 C2 DAO A 404 4660 4350 5337 82 404 340 C HETATM 5067 C3 DAO A 404 23.362 25.739 25.605 1.00 39.00 C ANISOU 5067 C3 DAO A 404 4814 4514 5490 68 365 318 C HETATM 5068 C4 DAO A 404 23.709 24.800 26.753 1.00 36.24 C ANISOU 5068 C4 DAO A 404 4462 4167 5139 64 340 305 C HETATM 5069 C5 DAO A 404 22.506 24.411 27.600 1.00 33.37 C ANISOU 5069 C5 DAO A 404 4121 3822 4735 55 313 284 C HETATM 5070 C6 DAO A 404 22.697 23.090 28.331 1.00 33.73 C ANISOU 5070 C6 DAO A 404 4176 3872 4766 57 302 279 C HETATM 5071 C7 DAO A 404 23.728 23.141 29.451 1.00 35.94 C ANISOU 5071 C7 DAO A 404 4430 4147 5080 59 278 276 C HETATM 5072 C8 DAO A 404 24.013 21.767 30.043 1.00 34.11 C ANISOU 5072 C8 DAO A 404 4207 3919 4834 66 274 277 C HETATM 5073 C9 DAO A 404 24.841 21.781 31.325 1.00 35.66 C ANISOU 5073 C9 DAO A 404 4379 4118 5053 70 244 273 C HETATM 5074 C10 DAO A 404 25.156 20.377 31.827 1.00 28.93 C ANISOU 5074 C10 DAO A 404 3537 3268 4187 82 244 280 C HETATM 5075 C11 DAO A 404 25.293 20.282 33.341 1.00 31.20 C ANISOU 5075 C11 DAO A 404 3815 3571 4470 88 208 271 C HETATM 5076 C18 OLC A 405 23.542 31.736 38.317 1.00 45.06 C ANISOU 5076 C18 OLC A 405 5402 5337 6381 6 6 62 C HETATM 5077 C10 OLC A 405 24.777 30.828 29.257 1.00 48.31 C ANISOU 5077 C10 OLC A 405 5860 5638 6856 26 275 265 C HETATM 5078 C9 OLC A 405 23.663 31.314 28.777 1.00 49.28 C ANISOU 5078 C9 OLC A 405 6005 5766 6952 25 285 270 C HETATM 5079 C17 OLC A 405 23.919 30.483 37.566 1.00 41.56 C ANISOU 5079 C17 OLC A 405 4975 4894 5922 15 31 95 C HETATM 5080 C11 OLC A 405 25.188 30.882 30.695 1.00 46.52 C ANISOU 5080 C11 OLC A 405 5612 5416 6646 18 234 236 C HETATM 5081 C8 OLC A 405 23.155 31.099 27.386 1.00 46.79 C ANISOU 5081 C8 OLC A 405 5714 5455 6608 36 322 296 C HETATM 5082 C24 OLC A 405 24.376 30.275 16.735 1.00 49.91 C ANISOU 5082 C24 OLC A 405 6190 5874 6898 190 638 516 C HETATM 5083 C16 OLC A 405 23.737 30.563 36.074 1.00 40.18 C ANISOU 5083 C16 OLC A 405 4813 4696 5758 10 74 124 C HETATM 5084 C12 OLC A 405 24.267 30.103 31.578 1.00 46.72 C ANISOU 5084 C12 OLC A 405 5666 5471 6616 18 204 219 C HETATM 5085 C7 OLC A 405 23.248 32.323 26.533 1.00 47.17 C ANISOU 5085 C7 OLC A 405 5749 5483 6691 40 352 316 C HETATM 5086 C15 OLC A 405 24.060 29.267 35.378 1.00 40.86 C ANISOU 5086 C15 OLC A 405 4916 4784 5825 20 97 152 C HETATM 5087 C13 OLC A 405 24.612 30.147 33.057 1.00 45.19 C ANISOU 5087 C13 OLC A 405 5452 5287 6430 15 162 190 C HETATM 5088 C6 OLC A 405 22.823 32.094 25.091 1.00 45.11 C ANISOU 5088 C6 OLC A 405 5512 5229 6397 56 390 345 C HETATM 5089 C14 OLC A 405 23.743 29.252 33.905 1.00 43.55 C ANISOU 5089 C14 OLC A 405 5274 5109 6165 18 138 179 C HETATM 5090 C5 OLC A 405 23.357 33.112 24.117 1.00 45.92 C ANISOU 5090 C5 OLC A 405 5597 5309 6543 66 429 375 C HETATM 5091 C4 OLC A 405 23.130 32.729 22.680 1.00 46.06 C ANISOU 5091 C4 OLC A 405 5637 5338 6525 87 467 404 C HETATM 5092 C3 OLC A 405 24.093 33.354 21.684 1.00 44.98 C ANISOU 5092 C3 OLC A 405 5480 5177 6433 101 512 439 C HETATM 5093 C2 OLC A 405 24.269 32.471 20.494 1.00 46.61 C ANISOU 5093 C2 OLC A 405 5707 5399 6603 121 543 461 C HETATM 5094 C21 OLC A 405 25.394 32.554 17.104 1.00 48.08 C ANISOU 5094 C21 OLC A 405 5902 5584 6782 183 663 552 C HETATM 5095 C1 OLC A 405 25.135 33.038 19.408 1.00 48.35 C ANISOU 5095 C1 OLC A 405 5911 5599 6860 139 592 500 C HETATM 5096 C22 OLC A 405 25.360 31.314 16.240 1.00 50.28 C ANISOU 5096 C22 OLC A 405 6208 5890 7004 201 676 553 C HETATM 5097 O19 OLC A 405 25.599 34.147 19.375 1.00 47.15 O ANISOU 5097 O19 OLC A 405 5732 5418 6763 138 610 516 O HETATM 5098 O25 OLC A 405 24.380 29.107 15.917 1.00 48.53 O ANISOU 5098 O25 OLC A 405 6040 5723 6678 205 652 514 O HETATM 5099 O23 OLC A 405 25.040 31.689 14.902 1.00 50.40 O ANISOU 5099 O23 OLC A 405 6239 5921 6989 230 716 586 O HETATM 5100 O20 OLC A 405 25.361 32.115 18.478 1.00 52.28 O ANISOU 5100 O20 OLC A 405 6428 6114 7324 156 615 514 O HETATM 5101 C10 OLC A 406 -3.807 22.608 43.551 1.00 51.12 C ANISOU 5101 C10 OLC A 406 6598 6373 6453 -56 165 65 C HETATM 5102 C9 OLC A 406 -3.180 22.107 44.582 1.00 50.97 C ANISOU 5102 C9 OLC A 406 6587 6353 6425 -42 167 80 C HETATM 5103 C11 OLC A 406 -4.348 21.780 42.428 1.00 50.91 C ANISOU 5103 C11 OLC A 406 6569 6334 6440 -75 185 60 C HETATM 5104 C8 OLC A 406 -2.794 22.816 45.842 1.00 51.83 C ANISOU 5104 C8 OLC A 406 6698 6479 6515 -21 148 81 C HETATM 5105 C12 OLC A 406 -4.998 22.581 41.345 1.00 48.82 C ANISOU 5105 C12 OLC A 406 6294 6077 6178 -86 177 42 C HETATM 5106 C7 OLC A 406 -2.142 21.901 46.830 1.00 51.18 C ANISOU 5106 C7 OLC A 406 6627 6398 6423 -3 155 102 C HETATM 5107 C15 OLC A 406 -7.071 21.687 38.172 1.00 60.86 C ANISOU 5107 C15 OLC A 406 7797 7609 7719 -127 200 0 C HETATM 5108 C13 OLC A 406 -5.681 21.734 40.287 1.00 49.04 C ANISOU 5108 C13 OLC A 406 6318 6100 6216 -104 194 32 C HETATM 5109 C6 OLC A 406 -2.109 22.425 48.260 1.00 51.34 C ANISOU 5109 C6 OLC A 406 6651 6441 6416 20 141 103 C HETATM 5110 C14 OLC A 406 -6.313 22.525 39.172 1.00 50.13 C ANISOU 5110 C14 OLC A 406 6445 6251 6353 -110 185 15 C HETATM 5111 C5 OLC A 406 -3.472 22.725 48.836 1.00 55.61 C ANISOU 5111 C5 OLC A 406 7194 6995 6940 19 151 97 C HETATM 5112 C4 OLC A 406 -3.469 23.004 50.317 1.00 57.01 C ANISOU 5112 C4 OLC A 406 7378 7197 7087 45 142 101 C HETATM 5113 C3 OLC A 406 -3.234 21.778 51.183 1.00 60.23 C ANISOU 5113 C3 OLC A 406 7799 7607 7480 64 163 131 C HETATM 5114 C2 OLC A 406 -4.434 20.884 51.251 1.00 67.50 C ANISOU 5114 C2 OLC A 406 8727 8519 8402 55 200 146 C HETATM 5115 C1 OLC A 406 -4.205 19.638 52.060 1.00 70.57 C ANISOU 5115 C1 OLC A 406 9128 8905 8780 74 227 180 C HETATM 5116 O19 OLC A 406 -3.457 18.747 51.755 1.00 74.62 O ANISOU 5116 O19 OLC A 406 9644 9401 9306 75 237 197 O HETATM 5117 O20 OLC A 406 -4.926 19.635 53.177 1.00 62.60 O ANISOU 5117 O20 OLC A 406 8127 7915 7744 92 239 190 O HETATM 5118 C10 OLC A 407 15.990 39.148 28.109 1.00 29.25 C ANISOU 5118 C10 OLC A 407 3512 3217 4384 23 308 264 C HETATM 5119 C9 OLC A 407 15.459 40.135 28.786 1.00 26.53 C ANISOU 5119 C9 OLC A 407 3159 2863 4059 17 296 246 C HETATM 5120 C11 OLC A 407 17.347 38.559 28.336 1.00 24.81 C ANISOU 5120 C11 OLC A 407 2930 2643 3852 17 305 260 C HETATM 5121 C8 OLC A 407 14.082 40.692 28.599 1.00 23.58 C ANISOU 5121 C8 OLC A 407 2803 2502 3654 25 298 250 C HETATM 5122 C12 OLC A 407 17.297 37.140 28.814 1.00 29.45 C ANISOU 5122 C12 OLC A 407 3537 3260 4392 13 280 244 C HETATM 5123 C7 OLC A 407 14.066 42.163 28.331 1.00 25.69 C ANISOU 5123 C7 OLC A 407 3051 2736 3973 30 322 262 C HETATM 5124 C13 OLC A 407 18.654 36.541 29.142 1.00 33.07 C ANISOU 5124 C13 OLC A 407 3977 3708 4882 8 274 239 C HETATM 5125 C10 OLC A 408 19.621 15.889 25.351 1.00 46.66 C ANISOU 5125 C10 OLC A 408 5961 5525 6243 61 401 237 C HETATM 5126 C9 OLC A 408 20.552 15.221 24.719 1.00 44.98 C ANISOU 5126 C9 OLC A 408 5747 5299 6045 73 425 246 C HETATM 5127 C11 OLC A 408 19.572 16.214 26.812 1.00 42.39 C ANISOU 5127 C11 OLC A 408 5411 4984 5712 56 372 241 C HETATM 5128 C8 OLC A 408 20.437 14.754 23.301 1.00 44.75 C ANISOU 5128 C8 OLC A 408 5732 5273 6000 79 453 236 C HETATM 5129 C12 OLC A 408 20.730 17.029 27.297 1.00 40.39 C ANISOU 5129 C12 OLC A 408 5131 4725 5491 63 360 258 C HETATM 5130 C7 OLC A 408 21.478 15.316 22.384 1.00 45.24 C ANISOU 5130 C7 OLC A 408 5780 5331 6077 94 473 254 C HETATM 5131 C13 OLC A 408 20.659 17.376 28.774 1.00 37.17 C ANISOU 5131 C13 OLC A 408 4713 4322 5087 60 329 258 C HETATM 5132 C6 OLC A 408 21.308 14.904 20.928 1.00 44.00 C ANISOU 5132 C6 OLC A 408 5638 5182 5897 104 501 244 C HETATM 5133 C14 OLC A 408 21.847 18.152 29.286 1.00 37.11 C ANISOU 5133 C14 OLC A 408 4676 4309 5115 66 315 270 C HETATM 5134 C5 OLC A 408 22.400 15.394 20.007 1.00 42.14 C ANISOU 5134 C5 OLC A 408 5390 4944 5678 122 525 266 C HETATM 5135 C10 OLC A 409 23.945 22.803 46.027 1.00 23.94 C ANISOU 5135 C10 OLC A 409 2829 2899 3367 179 -126 121 C HETATM 5136 C9 OLC A 409 23.675 21.958 46.988 1.00 33.13 C ANISOU 5136 C9 OLC A 409 4011 4091 4488 204 -134 135 C HETATM 5137 C11 OLC A 409 23.864 22.522 44.559 1.00 25.19 C ANISOU 5137 C11 OLC A 409 2999 3019 3552 159 -86 141 C HETATM 5138 C8 OLC A 409 23.865 22.239 48.446 1.00 21.58 C ANISOU 5138 C8 OLC A 409 2534 2670 2995 229 -176 114 C HETATM 5139 C12 OLC A 409 24.365 23.652 43.715 1.00 27.64 C ANISOU 5139 C12 OLC A 409 3283 3306 3914 137 -84 124 C HETATM 5140 C7 OLC A 409 23.599 21.059 49.324 1.00 30.61 C ANISOU 5140 C7 OLC A 409 3702 3840 4089 261 -172 142 C HETATM 5141 C13 OLC A 409 24.220 23.423 42.220 1.00 18.44 C ANISOU 5141 C13 OLC A 409 2131 2106 2769 120 -43 144 C HETATM 5142 C6 OLC A 409 23.803 21.349 50.805 1.00 30.75 C ANISOU 5142 C6 OLC A 409 3707 3906 4072 291 -215 122 C HETATM 5143 C5 OLC A 409 23.348 20.257 51.735 1.00 31.79 C ANISOU 5143 C5 OLC A 409 3866 4066 4148 324 -208 153 C HETATM 5144 C4 OLC A 409 23.239 20.700 53.170 1.00 31.88 C ANISOU 5144 C4 OLC A 409 3870 4127 4115 352 -248 130 C HETATM 5145 C3 OLC A 409 22.620 19.672 54.098 1.00 39.32 C ANISOU 5145 C3 OLC A 409 4844 5097 5000 386 -236 164 C HETATM 5146 C2 OLC A 409 22.411 20.205 55.479 1.00 41.80 C ANISOU 5146 C2 OLC A 409 5153 5463 5267 414 -275 139 C HETATM 5147 C1 PLM A 410 12.847 2.269 54.084 1.00 51.54 C ANISOU 5147 C1 PLM A 410 6776 6272 6536 469 485 743 C HETATM 5148 O2 PLM A 410 12.632 1.274 54.834 1.00 58.93 O ANISOU 5148 O2 PLM A 410 7726 7197 7468 501 527 793 O HETATM 5149 C2 PLM A 410 13.415 1.959 52.661 1.00 49.28 C ANISOU 5149 C2 PLM A 410 6481 5942 6302 436 493 720 C HETATM 5150 C3 PLM A 410 14.479 2.920 52.137 1.00 59.71 C ANISOU 5150 C3 PLM A 410 7781 7287 7620 429 439 686 C HETATM 5151 C4 PLM A 410 15.103 2.467 50.811 1.00 54.13 C ANISOU 5151 C4 PLM A 410 7067 6537 6963 404 453 673 C HETATM 5152 C5 PLM A 410 15.837 3.564 50.045 1.00 59.36 C ANISOU 5152 C5 PLM A 410 7709 7216 7629 384 406 630 C HETATM 5153 C6 PLM A 410 16.543 3.046 48.781 1.00 55.02 C ANISOU 5153 C6 PLM A 410 7152 6626 7125 366 423 622 C HETATM 5154 C7 PLM A 410 17.258 4.133 47.972 1.00 56.16 C ANISOU 5154 C7 PLM A 410 7277 6785 7277 346 381 583 C HETATM 5155 C8 PLM A 410 17.842 3.628 46.647 1.00 60.31 C ANISOU 5155 C8 PLM A 410 7797 7270 7846 326 402 573 C HETATM 5156 C9 PLM A 410 17.584 4.571 45.464 1.00 63.32 C ANISOU 5156 C9 PLM A 410 8172 7648 8240 284 385 526 C HETATM 5157 CA PLM A 410 18.097 4.039 44.119 1.00 50.52 C ANISOU 5157 CA PLM A 410 6549 5989 6659 267 408 516 C HETATM 5158 CB PLM A 410 17.780 4.958 42.927 1.00 53.32 C ANISOU 5158 CB PLM A 410 6897 6341 7021 228 394 472 C HETATM 5159 C8 OLC A 411 24.826 34.859 45.779 1.00 42.48 C ANISOU 5159 C8 OLC A 411 4941 5127 6072 27 -240 -187 C HETATM 5160 C7 OLC A 411 24.839 34.109 47.074 1.00 42.48 C ANISOU 5160 C7 OLC A 411 4949 5177 6015 52 -278 -201 C HETATM 5161 C6 OLC A 411 26.170 34.160 47.814 1.00 43.59 C ANISOU 5161 C6 OLC A 411 5044 5336 6184 63 -316 -232 C HETATM 5162 C5 OLC A 411 26.548 35.519 48.347 1.00 42.61 C ANISOU 5162 C5 OLC A 411 4878 5204 6109 51 -344 -290 C HETATM 5163 C4 OLC A 411 25.731 35.968 49.533 1.00 48.98 C ANISOU 5163 C4 OLC A 411 5695 6044 6871 60 -377 -330 C HETATM 5164 C3 OLC A 411 25.905 35.104 50.771 1.00 46.23 C ANISOU 5164 C3 OLC A 411 5352 5753 6459 92 -415 -339 C HETATM 5165 C2 OLC A 411 24.927 35.444 51.854 1.00 49.55 C ANISOU 5165 C2 OLC A 411 5793 6208 6827 104 -440 -370 C HETATM 5166 C1 OLC A 411 25.020 34.537 53.049 1.00 53.87 C ANISOU 5166 C1 OLC A 411 6350 6814 7303 140 -474 -371 C HETATM 5167 O19 OLC A 411 24.264 33.451 52.907 1.00 57.64 O ANISOU 5167 O19 OLC A 411 6873 7303 7724 153 -449 -321 O HETATM 5168 O20 OLC A 411 25.688 34.752 54.025 1.00 53.02 O ANISOU 5168 O20 OLC A 411 6212 6741 7192 157 -517 -413 O HETATM 5169 C18 OLC A 412 -7.432 25.212 37.172 1.00 46.19 C ANISOU 5169 C18 OLC A 412 5920 5788 5842 -104 154 -9 C HETATM 5170 C10 OLC A 412 -6.140 26.285 46.422 1.00 44.99 C ANISOU 5170 C10 OLC A 412 5813 5658 5621 -26 123 28 C HETATM 5171 C9 OLC A 412 -6.647 25.390 47.228 1.00 54.22 C ANISOU 5171 C9 OLC A 412 6992 6833 6778 -22 142 40 C HETATM 5172 C17 OLC A 412 -6.732 26.283 37.974 1.00 40.68 C ANISOU 5172 C17 OLC A 412 5225 5087 5145 -91 140 1 C HETATM 5173 C11 OLC A 412 -5.690 26.040 45.015 1.00 44.63 C ANISOU 5173 C11 OLC A 412 5763 5598 5598 -41 125 28 C HETATM 5174 C8 OLC A 412 -7.194 25.655 48.597 1.00 50.04 C ANISOU 5174 C8 OLC A 412 6468 6322 6223 -6 143 40 C HETATM 5175 C24 OLC A 412 -5.736 27.131 58.230 1.00 47.99 C ANISOU 5175 C24 OLC A 412 6264 6244 5726 195 77 33 C HETATM 5176 C16 OLC A 412 -7.009 26.252 39.454 1.00 42.69 C ANISOU 5176 C16 OLC A 412 5485 5342 5393 -88 140 3 C HETATM 5177 C12 OLC A 412 -6.457 26.859 44.027 1.00 44.34 C ANISOU 5177 C12 OLC A 412 5715 5563 5569 -51 122 15 C HETATM 5178 C7 OLC A 412 -7.358 24.408 49.408 1.00 48.45 C ANISOU 5178 C7 OLC A 412 6279 6121 6009 2 167 63 C HETATM 5179 C15 OLC A 412 -6.428 27.444 40.173 1.00 42.13 C ANISOU 5179 C15 OLC A 412 5414 5271 5322 -74 122 6 C HETATM 5180 C13 OLC A 412 -6.088 26.637 42.570 1.00 40.83 C ANISOU 5180 C13 OLC A 412 5266 5108 5142 -62 125 16 C HETATM 5181 C6 OLC A 412 -7.703 24.653 50.870 1.00 44.43 C ANISOU 5181 C6 OLC A 412 5778 5634 5470 25 168 67 C HETATM 5182 C14 OLC A 412 -6.817 27.564 41.625 1.00 41.85 C ANISOU 5182 C14 OLC A 412 5383 5243 5275 -67 120 5 C HETATM 5183 C5 OLC A 412 -7.281 23.535 51.789 1.00 45.99 C ANISOU 5183 C5 OLC A 412 5989 5834 5651 44 185 94 C HETATM 5184 C4 OLC A 412 -7.432 23.848 53.256 1.00 45.63 C ANISOU 5184 C4 OLC A 412 5952 5815 5570 72 182 97 C HETATM 5185 C3 OLC A 412 -6.323 23.277 54.124 1.00 45.70 C ANISOU 5185 C3 OLC A 412 5972 5834 5558 99 176 116 C HETATM 5186 C2 OLC A 412 -6.519 23.568 55.580 1.00 46.31 C ANISOU 5186 C2 OLC A 412 6058 5944 5595 131 174 119 C HETATM 5187 C21 OLC A 412 -6.261 24.661 58.025 1.00 50.12 C ANISOU 5187 C21 OLC A 412 6552 6491 6001 192 143 104 C HETATM 5188 C1 OLC A 412 -5.332 23.193 56.425 1.00 48.51 C ANISOU 5188 C1 OLC A 412 6344 6238 5849 161 160 133 C HETATM 5189 C22 OLC A 412 -5.832 25.793 58.933 1.00 49.64 C ANISOU 5189 C22 OLC A 412 6489 6462 5909 216 107 74 C HETATM 5190 O19 OLC A 412 -4.684 22.188 56.293 1.00 46.79 O ANISOU 5190 O19 OLC A 412 6132 6009 5639 166 172 158 O HETATM 5191 O25 OLC A 412 -5.673 28.210 59.159 1.00 48.31 O ANISOU 5191 O25 OLC A 412 6303 6312 5740 216 51 2 O HETATM 5192 O23 OLC A 412 -6.720 25.875 60.047 1.00 48.27 O ANISOU 5192 O23 OLC A 412 6327 6316 5698 239 122 78 O HETATM 5193 O20 OLC A 412 -5.100 24.088 57.384 1.00 49.74 O ANISOU 5193 O20 OLC A 412 6501 6425 5974 186 134 114 O HETATM 5194 C10 OLC A 413 -6.732 34.725 28.965 1.00 37.40 C ANISOU 5194 C10 OLC A 413 4746 4733 4730 32 138 78 C HETATM 5195 C9 OLC A 413 -6.496 34.738 27.681 1.00 33.77 C ANISOU 5195 C9 OLC A 413 4286 4287 4259 47 147 92 C HETATM 5196 C11 OLC A 413 -6.340 33.632 29.908 1.00 34.41 C ANISOU 5196 C11 OLC A 413 4375 4342 4357 9 132 62 C HETATM 5197 C8 OLC A 413 -6.967 35.794 26.731 1.00 33.80 C ANISOU 5197 C8 OLC A 413 4282 4308 4254 74 154 112 C HETATM 5198 C12 OLC A 413 -6.645 33.960 31.335 1.00 37.31 C ANISOU 5198 C12 OLC A 413 4742 4697 4735 -1 123 52 C HETATM 5199 C7 OLC A 413 -6.568 35.524 25.316 1.00 39.65 C ANISOU 5199 C7 OLC A 413 5025 5065 4976 92 165 126 C HETATM 5200 C13 OLC A 413 -6.268 32.869 32.319 1.00 32.94 C ANISOU 5200 C13 OLC A 413 4198 4134 4184 -20 119 39 C HETATM 5201 C6 OLC A 413 -7.230 36.439 24.296 1.00 30.62 C ANISOU 5201 C6 OLC A 413 3873 3948 3814 123 171 146 C HETATM 5202 C14 OLC A 413 -6.421 33.269 33.765 1.00 30.48 C ANISOU 5202 C14 OLC A 413 3887 3812 3882 -25 111 31 C HETATM 5203 C5 OLC A 413 -6.987 36.036 22.863 1.00 33.23 C ANISOU 5203 C5 OLC A 413 4206 4305 4115 143 180 155 C HETATM 5204 C4 OLC A 413 -7.836 36.778 21.865 1.00 31.76 C ANISOU 5204 C4 OLC A 413 4012 4155 3901 176 183 172 C HETATM 5205 C3 OLC A 413 -7.772 36.224 20.455 1.00 33.06 C ANISOU 5205 C3 OLC A 413 4179 4356 4026 197 188 174 C HETATM 5206 C2 OLC A 413 -8.703 36.929 19.518 1.00 39.17 C ANISOU 5206 C2 OLC A 413 4944 5172 4768 233 187 189 C HETATM 5207 C ACE B 401 -13.197 21.853 71.160 1.00 29.27 C ANISOU 5207 C ACE B 401 4068 4170 2885 578 440 353 C HETATM 5208 O ACE B 401 -12.255 22.006 70.385 1.00 36.42 O ANISOU 5208 O ACE B 401 4964 5059 3816 556 401 330 O HETATM 5209 CH3 ACE B 401 -13.094 20.986 72.378 1.00 30.52 C ANISOU 5209 CH3 ACE B 401 4247 4360 2990 635 475 406 C HETATM 5210 C1 RET B 402 -20.118 24.745 44.669 1.00 27.29 C ANISOU 5210 C1 RET B 402 3452 3492 3426 -139 274 -51 C HETATM 5211 C2 RET B 402 -19.430 24.199 43.416 1.00 29.62 C ANISOU 5211 C2 RET B 402 3745 3777 3732 -152 264 -60 C HETATM 5212 C3 RET B 402 -18.816 25.259 42.582 1.00 29.12 C ANISOU 5212 C3 RET B 402 3683 3724 3658 -142 234 -66 C HETATM 5213 C4 RET B 402 -19.911 26.195 42.093 1.00 26.38 C ANISOU 5213 C4 RET B 402 3316 3399 3308 -140 223 -81 C HETATM 5214 C5 RET B 402 -20.865 26.611 43.177 1.00 24.21 C ANISOU 5214 C5 RET B 402 3036 3134 3028 -133 235 -78 C HETATM 5215 C6 RET B 402 -20.801 26.079 44.419 1.00 24.07 C ANISOU 5215 C6 RET B 402 3031 3105 3008 -130 255 -63 C HETATM 5216 C7 RET B 402 -21.417 26.682 45.590 1.00 25.77 C ANISOU 5216 C7 RET B 402 3249 3331 3211 -116 264 -57 C HETATM 5217 C8 RET B 402 -21.724 27.993 45.811 1.00 24.33 C ANISOU 5217 C8 RET B 402 3065 3164 3016 -100 249 -62 C HETATM 5218 C9 RET B 402 -22.072 28.595 47.020 1.00 22.29 C ANISOU 5218 C9 RET B 402 2814 2914 2743 -83 255 -56 C HETATM 5219 C10 RET B 402 -22.236 29.991 47.097 1.00 27.67 C ANISOU 5219 C10 RET B 402 3492 3607 3413 -67 238 -64 C HETATM 5220 C11 RET B 402 -21.639 30.884 47.970 1.00 19.86 C ANISOU 5220 C11 RET B 402 2520 2620 2407 -46 227 -62 C HETATM 5221 C12 RET B 402 -21.757 32.264 47.969 1.00 24.79 C ANISOU 5221 C12 RET B 402 3140 3251 3027 -32 210 -72 C HETATM 5222 C13 RET B 402 -20.926 33.218 48.587 1.00 24.27 C ANISOU 5222 C13 RET B 402 3089 3182 2950 -14 194 -76 C HETATM 5223 C14 RET B 402 -21.232 34.583 48.624 1.00 26.67 C ANISOU 5223 C14 RET B 402 3387 3491 3254 -1 183 -87 C HETATM 5224 C15 RET B 402 -20.424 35.554 49.212 1.00 26.14 C ANISOU 5224 C15 RET B 402 3331 3418 3181 15 168 -96 C HETATM 5225 C16 RET B 402 -21.142 23.701 45.142 1.00 22.68 C ANISOU 5225 C16 RET B 402 2857 2901 2860 -153 308 -50 C HETATM 5226 C17 RET B 402 -19.054 24.900 45.767 1.00 31.33 C ANISOU 5226 C17 RET B 402 3989 3995 3918 -120 273 -31 C HETATM 5227 C18 RET B 402 -21.863 27.631 42.701 1.00 21.86 C ANISOU 5227 C18 RET B 402 2719 2858 2727 -127 223 -91 C HETATM 5228 C19 RET B 402 -22.298 27.807 48.260 1.00 22.60 C ANISOU 5228 C19 RET B 402 2863 2948 2776 -80 283 -41 C HETATM 5229 C20 RET B 402 -19.658 32.723 49.184 1.00 20.95 C ANISOU 5229 C20 RET B 402 2689 2752 2519 -10 189 -68 C HETATM 5230 C1 NAG B 403 -9.398 22.799 68.393 1.00 28.78 C ANISOU 5230 C1 NAG B 403 3966 4058 2911 503 282 256 C HETATM 5231 C2 NAG B 403 -9.717 21.373 67.937 1.00 33.01 C ANISOU 5231 C2 NAG B 403 4506 4555 3480 489 334 312 C HETATM 5232 C3 NAG B 403 -8.758 20.392 68.606 1.00 39.79 C ANISOU 5232 C3 NAG B 403 5378 5432 4308 531 342 354 C HETATM 5233 C4 NAG B 403 -7.318 20.788 68.306 1.00 40.07 C ANISOU 5233 C4 NAG B 403 5405 5478 4343 532 286 325 C HETATM 5234 C5 NAG B 403 -7.072 22.241 68.713 1.00 37.42 C ANISOU 5234 C5 NAG B 403 5062 5179 3977 541 233 266 C HETATM 5235 C6 NAG B 403 -5.704 22.740 68.309 1.00 34.04 C ANISOU 5235 C6 NAG B 403 4621 4755 3559 536 177 232 C HETATM 5236 C7 NAG B 403 -11.853 20.296 67.386 1.00 31.50 C ANISOU 5236 C7 NAG B 403 4314 4310 3345 450 428 358 C HETATM 5237 C8 NAG B 403 -13.260 20.036 67.829 1.00 28.42 C ANISOU 5237 C8 NAG B 403 3927 3917 2955 452 479 381 C HETATM 5238 N2 NAG B 403 -11.099 21.021 68.221 1.00 31.30 N ANISOU 5238 N2 NAG B 403 4295 4330 3266 487 387 337 N HETATM 5239 O3 NAG B 403 -9.008 19.065 68.157 1.00 30.68 O ANISOU 5239 O3 NAG B 403 4228 4238 3190 517 392 404 O HETATM 5240 O4 NAG B 403 -6.418 19.942 69.012 1.00 39.61 O ANISOU 5240 O4 NAG B 403 5358 5443 4251 576 289 363 O HETATM 5241 O5 NAG B 403 -8.030 23.107 68.082 1.00 35.20 O ANISOU 5241 O5 NAG B 403 4771 4876 3728 502 232 232 O HETATM 5242 O6 NAG B 403 -5.398 22.379 66.970 1.00 39.75 O ANISOU 5242 O6 NAG B 403 5332 5427 4344 491 180 234 O HETATM 5243 O7 NAG B 403 -11.417 19.870 66.319 1.00 35.22 O ANISOU 5243 O7 NAG B 403 4776 4744 3864 416 423 357 O HETATM 5244 C10 OLC B 404 -33.971 34.670 31.031 1.00 40.79 C ANISOU 5244 C10 OLC B 404 4757 5694 5048 23 32 -240 C HETATM 5245 C9 OLC B 404 -33.176 34.165 30.125 1.00 40.56 C ANISOU 5245 C9 OLC B 404 4738 5669 5004 21 21 -246 C HETATM 5246 C11 OLC B 404 -34.343 34.084 32.356 1.00 41.90 C ANISOU 5246 C11 OLC B 404 4897 5804 5218 -7 55 -248 C HETATM 5247 C8 OLC B 404 -32.929 34.828 28.806 1.00 39.97 C ANISOU 5247 C8 OLC B 404 4661 5630 4897 56 1 -236 C HETATM 5248 C12 OLC B 404 -35.257 34.973 33.139 1.00 42.10 C ANISOU 5248 C12 OLC B 404 4910 5833 5252 7 64 -237 C HETATM 5249 C7 OLC B 404 -33.353 34.006 27.630 1.00 46.96 C ANISOU 5249 C7 OLC B 404 5519 6558 5768 53 -20 -271 C HETATM 5250 C15 OLC B 404 -37.048 34.765 36.591 1.00 43.99 C ANISOU 5250 C15 OLC B 404 5137 6026 5549 -26 128 -236 C HETATM 5251 C13 OLC B 404 -35.660 34.426 34.498 1.00 42.07 C ANISOU 5251 C13 OLC B 404 4908 5802 5275 -19 90 -242 C HETATM 5252 C6 OLC B 404 -33.886 34.828 26.464 1.00 44.59 C ANISOU 5252 C6 OLC B 404 5196 6310 5434 94 -43 -265 C HETATM 5253 C14 OLC B 404 -36.592 35.328 35.269 1.00 41.71 C ANISOU 5253 C14 OLC B 404 4849 5762 5237 -3 100 -231 C HETATM 5254 C5 OLC B 404 -34.082 34.050 25.189 1.00 45.49 C ANISOU 5254 C5 OLC B 404 5288 6470 5526 96 -66 -300 C HETATM 5255 C4 OLC B 404 -34.853 34.793 24.123 1.00 51.01 C ANISOU 5255 C4 OLC B 404 5959 7231 6191 138 -90 -299 C HETATM 5256 C3 OLC B 404 -34.396 36.224 23.898 1.00 53.20 C ANISOU 5256 C3 OLC B 404 6257 7508 6448 183 -85 -246 C HETATM 5257 C2 OLC B 404 -35.119 36.895 22.766 1.00 53.67 C ANISOU 5257 C2 OLC B 404 6288 7631 6471 229 -108 -242 C HETATM 5258 C21 OLC B 404 -35.975 38.075 20.612 1.00 54.47 C ANISOU 5258 C21 OLC B 404 6353 7846 6499 320 -146 -223 C HETATM 5259 C1 OLC B 404 -34.823 38.369 22.670 1.00 54.43 C ANISOU 5259 C1 OLC B 404 6402 7723 6556 274 -98 -186 C HETATM 5260 C22 OLC B 404 -36.452 38.930 19.460 1.00 45.83 C ANISOU 5260 C22 OLC B 404 5240 6814 5360 379 -164 -202 C HETATM 5261 O19 OLC B 404 -34.161 38.979 23.467 1.00 56.26 O ANISOU 5261 O19 OLC B 404 6664 7905 6808 271 -76 -154 O HETATM 5262 O20 OLC B 404 -35.363 38.939 21.594 1.00 57.52 O ANISOU 5262 O20 OLC B 404 6772 8172 6911 319 -117 -178 O HETATM 5263 C8 OLC B 405 -6.179 22.244 30.605 1.00 42.99 C ANISOU 5263 C8 OLC B 405 5507 5392 5435 -119 183 -54 C HETATM 5264 C7 OLC B 405 -5.967 22.745 29.213 1.00 37.41 C ANISOU 5264 C7 OLC B 405 4796 4704 4713 -106 179 -56 C HETATM 5265 C6 OLC B 405 -5.212 21.781 28.308 1.00 36.76 C ANISOU 5265 C6 OLC B 405 4719 4614 4633 -107 190 -64 C HETATM 5266 C5 OLC B 405 -5.050 22.278 26.895 1.00 36.33 C ANISOU 5266 C5 OLC B 405 4661 4582 4560 -90 187 -66 C HETATM 5267 C4 OLC B 405 -4.360 21.314 25.962 1.00 40.91 C ANISOU 5267 C4 OLC B 405 5248 5158 5140 -90 199 -76 C HETATM 5268 C3 OLC B 405 -4.425 21.721 24.499 1.00 37.77 C ANISOU 5268 C3 OLC B 405 4846 4790 4716 -71 196 -82 C HETATM 5269 C2 OLC B 405 -5.830 21.764 23.989 1.00 46.34 C ANISOU 5269 C2 OLC B 405 5917 5909 5779 -73 185 -111 C HETATM 5270 C1 OLC B 405 -5.971 22.431 22.652 1.00 43.36 C ANISOU 5270 C1 OLC B 405 5535 5568 5370 -49 179 -111 C HETATM 5271 O19 OLC B 405 -5.201 21.854 21.737 1.00 44.55 O ANISOU 5271 O19 OLC B 405 5693 5720 5515 -41 189 -116 O HETATM 5272 O20 OLC B 405 -6.686 23.371 22.418 1.00 50.77 O ANISOU 5272 O20 OLC B 405 6464 6533 6292 -35 168 -106 O HETATM 5273 C10 OLC B 406 -4.442 38.481 41.428 1.00 52.14 C ANISOU 5273 C10 OLC B 406 6612 6480 6719 -7 42 -48 C HETATM 5274 C9 OLC B 406 -4.592 37.193 41.610 1.00 48.13 C ANISOU 5274 C9 OLC B 406 6116 5988 6185 -13 43 -43 C HETATM 5275 C11 OLC B 406 -4.420 39.185 40.107 1.00 52.18 C ANISOU 5275 C11 OLC B 406 6608 6470 6746 -4 55 -31 C HETATM 5276 C8 OLC B 406 -4.502 36.486 42.927 1.00 44.07 C ANISOU 5276 C8 OLC B 406 5610 5486 5648 -12 32 -55 C HETATM 5277 C24 OLC B 406 -7.737 31.758 52.920 1.00 37.21 C ANISOU 5277 C24 OLC B 406 4832 4780 4526 71 47 -66 C HETATM 5278 C7 OLC B 406 -5.732 35.711 43.285 1.00 39.52 C ANISOU 5278 C7 OLC B 406 5045 4932 5040 -14 41 -53 C HETATM 5279 C6 OLC B 406 -5.650 35.023 44.642 1.00 42.83 C ANISOU 5279 C6 OLC B 406 5473 5364 5436 -10 34 -61 C HETATM 5280 C5 OLC B 406 -6.905 34.293 45.058 1.00 41.54 C ANISOU 5280 C5 OLC B 406 5319 5220 5245 -12 46 -58 C HETATM 5281 C4 OLC B 406 -6.863 33.758 46.471 1.00 42.79 C ANISOU 5281 C4 OLC B 406 5487 5392 5379 -3 42 -62 C HETATM 5282 C3 OLC B 406 -8.184 33.194 46.964 1.00 39.16 C ANISOU 5282 C3 OLC B 406 5035 4950 4895 -3 58 -59 C HETATM 5283 C2 OLC B 406 -8.204 32.984 48.444 1.00 36.94 C ANISOU 5283 C2 OLC B 406 4763 4684 4588 11 54 -65 C HETATM 5284 C21 OLC B 406 -7.191 30.431 50.826 1.00 40.88 C ANISOU 5284 C21 OLC B 406 5293 5209 5031 38 65 -35 C HETATM 5285 C1 OLC B 406 -7.453 31.769 48.904 1.00 38.85 C ANISOU 5285 C1 OLC B 406 5016 4928 4818 14 57 -50 C HETATM 5286 C22 OLC B 406 -7.001 30.580 52.320 1.00 40.56 C ANISOU 5286 C22 OLC B 406 5260 5191 4959 63 55 -42 C HETATM 5287 O19 OLC B 406 -6.968 30.934 48.188 1.00 41.84 O ANISOU 5287 O19 OLC B 406 5396 5296 5206 5 64 -35 O HETATM 5288 O25 OLC B 406 -7.078 32.987 52.632 1.00 43.90 O ANISOU 5288 O25 OLC B 406 5668 5618 5395 70 22 -91 O HETATM 5289 O23 OLC B 406 -7.413 29.378 52.969 1.00 42.46 O ANISOU 5289 O23 OLC B 406 5514 5442 5176 71 78 -18 O HETATM 5290 O20 OLC B 406 -7.362 31.735 50.230 1.00 40.93 O ANISOU 5290 O20 OLC B 406 5287 5208 5057 32 52 -55 O HETATM 5291 C18 OLC B 407 -8.464 40.337 42.919 1.00 57.53 C ANISOU 5291 C18 OLC B 407 7294 7201 7365 12 49 -80 C HETATM 5292 C10 OLC B 407 -10.177 41.616 50.727 1.00 49.18 C ANISOU 5292 C10 OLC B 407 6264 6216 6205 63 4 -213 C HETATM 5293 C9 OLC B 407 -10.356 42.035 51.955 1.00 42.72 C ANISOU 5293 C9 OLC B 407 5450 5412 5370 77 -4 -239 C HETATM 5294 C17 OLC B 407 -9.278 39.980 44.141 1.00 51.22 C ANISOU 5294 C17 OLC B 407 6502 6421 6536 14 45 -95 C HETATM 5295 C11 OLC B 407 -11.029 41.951 49.543 1.00 39.33 C ANISOU 5295 C11 OLC B 407 5009 4958 4976 56 20 -194 C HETATM 5296 C8 OLC B 407 -9.518 41.596 53.114 1.00 46.50 C ANISOU 5296 C8 OLC B 407 5936 5907 5823 87 -22 -256 C HETATM 5297 C16 OLC B 407 -8.443 39.505 45.301 1.00 48.81 C ANISOU 5297 C16 OLC B 407 6205 6119 6222 14 32 -109 C HETATM 5298 C12 OLC B 407 -11.735 40.762 48.972 1.00 38.86 C ANISOU 5298 C12 OLC B 407 4957 4914 4896 48 36 -167 C HETATM 5299 C7 OLC B 407 -10.020 42.064 54.444 1.00 42.32 C ANISOU 5299 C7 OLC B 407 5412 5400 5268 106 -27 -284 C HETATM 5300 C15 OLC B 407 -9.228 39.064 46.515 1.00 40.70 C ANISOU 5300 C15 OLC B 407 5187 5114 5162 19 32 -120 C HETATM 5301 C13 OLC B 407 -10.825 39.704 48.372 1.00 39.53 C ANISOU 5301 C13 OLC B 407 5046 4994 4981 37 34 -148 C HETATM 5302 C6 OLC B 407 -9.266 41.453 55.617 1.00 42.56 C ANISOU 5302 C6 OLC B 407 5452 5455 5263 121 -44 -296 C HETATM 5303 C14 OLC B 407 -10.084 40.142 47.132 1.00 38.08 C ANISOU 5303 C14 OLC B 407 4851 4786 4831 29 32 -138 C HETATM 5304 C5 OLC B 407 -7.771 41.631 55.532 1.00 48.09 C ANISOU 5304 C5 OLC B 407 6142 6142 5986 117 -69 -312 C HETATM 5305 C4 OLC B 407 -6.988 40.843 56.553 1.00 46.08 C ANISOU 5305 C4 OLC B 407 5896 5916 5695 133 -86 -317 C HETATM 5306 C3 OLC B 407 -5.481 40.945 56.387 1.00 60.64 C ANISOU 5306 C3 OLC B 407 7727 7748 7565 128 -110 -331 C HETATM 5307 C2 OLC B 407 -4.737 40.050 57.329 1.00 51.65 C ANISOU 5307 C2 OLC B 407 6596 6640 6388 146 -126 -330 C HETATM 5308 C1 PLM B 408 -17.527 53.849 21.519 1.00 47.32 C ANISOU 5308 C1 PLM B 408 5844 6106 6027 565 335 513 C HETATM 5309 O2 PLM B 408 -17.482 55.112 21.557 1.00 48.62 O ANISOU 5309 O2 PLM B 408 6005 6233 6234 590 365 547 O HETATM 5310 C2 PLM B 408 -17.053 53.094 22.810 1.00 54.57 C ANISOU 5310 C2 PLM B 408 6771 6995 6968 506 314 460 C HETATM 5311 C3 PLM B 408 -16.182 53.913 23.765 1.00 51.54 C ANISOU 5311 C3 PLM B 408 6391 6537 6654 486 334 457 C HETATM 5312 C4 PLM B 408 -15.740 53.153 25.028 1.00 49.88 C ANISOU 5312 C4 PLM B 408 6188 6305 6459 433 311 405 C HETATM 5313 C5 PLM B 408 -14.978 54.033 26.033 1.00 49.54 C ANISOU 5313 C5 PLM B 408 6145 6194 6484 415 328 396 C HETATM 5314 C6 PLM B 408 -14.306 53.257 27.178 1.00 54.84 C ANISOU 5314 C6 PLM B 408 6825 6844 7167 367 306 349 C HETATM 5315 C10 OLC B 409 -14.511 17.849 46.719 1.00 64.53 C ANISOU 5315 C10 OLC B 409 8265 8068 8186 -134 381 68 C HETATM 5316 C9 OLC B 409 -15.115 16.755 46.326 1.00 64.08 C ANISOU 5316 C9 OLC B 409 8197 7989 8160 -154 411 64 C HETATM 5317 C11 OLC B 409 -13.734 18.764 45.825 1.00 62.72 C ANISOU 5317 C11 OLC B 409 8035 7849 7946 -132 343 51 C HETATM 5318 C8 OLC B 409 -15.836 15.774 47.197 1.00 61.02 C ANISOU 5318 C8 OLC B 409 7809 7585 7790 -156 454 84 C HETATM 5319 C12 OLC B 409 -13.179 19.966 46.524 1.00 59.21 C ANISOU 5319 C12 OLC B 409 7600 7425 7470 -108 316 57 C HETATM 5320 C7 OLC B 409 -15.272 14.390 47.113 1.00 67.43 C ANISOU 5320 C7 OLC B 409 8628 8363 8629 -162 484 99 C HETATM 5321 C13 OLC B 409 -12.347 20.868 45.630 1.00 57.93 C ANISOU 5321 C13 OLC B 409 7438 7270 7304 -107 281 43 C HETATM 5322 O HOH A 501 9.775 31.949 63.180 1.00 42.20 O ANISOU 5322 O HOH A 501 5316 5724 4996 378 -403 -297 O HETATM 5323 O HOH A 502 -3.742 38.250 19.503 1.00 27.83 O ANISOU 5323 O HOH A 502 3527 3590 3455 238 267 288 O HETATM 5324 O HOH A 503 6.956 31.031 57.985 1.00 29.58 O ANISOU 5324 O HOH A 503 3766 3928 3544 235 -241 -166 O HETATM 5325 O HOH A 504 2.167 21.113 8.821 1.00 30.03 O ANISOU 5325 O HOH A 504 3928 4078 3406 246 337 -61 O HETATM 5326 O HOH A 505 17.296 29.604 3.691 1.00 30.60 O ANISOU 5326 O HOH A 505 3978 3881 3769 547 827 616 O HETATM 5327 O HOH A 506 16.650 30.491 10.546 1.00 27.59 O ANISOU 5327 O HOH A 506 3530 3324 3629 340 667 524 O HETATM 5328 O HOH A 507 0.504 14.386 26.725 1.00 16.79 O ANISOU 5328 O HOH A 507 2244 1931 2204 -128 304 -77 O HETATM 5329 O HOH A 508 -3.647 20.981 58.146 1.00 43.45 O ANISOU 5329 O HOH A 508 5729 5620 5162 228 182 205 O HETATM 5330 O HOH A 509 6.137 19.372 28.158 1.00 23.04 O ANISOU 5330 O HOH A 509 3025 2702 3027 -50 262 78 O HETATM 5331 O HOH A 510 0.399 14.784 12.497 1.00 34.36 O ANISOU 5331 O HOH A 510 4463 4478 4114 47 306 -284 O HETATM 5332 O HOH A 511 2.331 26.334 15.327 1.00 27.01 O ANISOU 5332 O HOH A 511 3509 3511 3241 164 308 116 O HETATM 5333 O HOH A 512 18.046 27.948 10.410 1.00 28.09 O ANISOU 5333 O HOH A 512 3605 3379 3687 324 671 483 O HETATM 5334 O HOH A 513 10.694 25.745 0.680 1.00 29.47 O ANISOU 5334 O HOH A 513 3915 4071 3211 605 659 342 O HETATM 5335 O HOH A 514 -9.593 33.204 20.411 1.00 29.90 O ANISOU 5335 O HOH A 514 3772 4021 3567 151 144 73 O HETATM 5336 O HOH A 515 12.758 7.876 15.367 1.00 24.88 O ANISOU 5336 O HOH A 515 3339 2860 3253 44 546 -106 O HETATM 5337 O HOH A 516 12.280 41.001 17.461 1.00 35.93 O ANISOU 5337 O HOH A 516 4465 4188 5000 246 572 559 O HETATM 5338 O HOH A 517 11.951 26.066 15.337 1.00 21.24 O ANISOU 5338 O HOH A 517 2768 2563 2740 183 455 281 O HETATM 5339 O HOH A 518 3.793 31.107 9.850 1.00 23.44 O ANISOU 5339 O HOH A 518 3058 3161 2688 376 426 321 O HETATM 5340 O HOH A 519 17.561 25.335 17.165 1.00 20.62 O ANISOU 5340 O HOH A 519 2638 2340 2856 158 501 341 O HETATM 5341 O HOH A 520 11.064 23.144 23.323 1.00 25.88 O ANISOU 5341 O HOH A 520 3348 3052 3434 34 321 177 O HETATM 5342 O HOH A 521 17.166 32.847 58.023 1.00 25.47 O ANISOU 5342 O HOH A 521 3003 3419 3256 254 -464 -334 O HETATM 5343 O HOH A 522 21.000 17.430 13.837 1.00 37.90 O ANISOU 5343 O HOH A 522 4892 4514 4993 200 615 269 O HETATM 5344 O HOH A 523 7.111 22.771 39.171 1.00 30.78 O ANISOU 5344 O HOH A 523 3976 3700 4021 -19 120 115 O HETATM 5345 O HOH A 524 5.371 19.005 4.541 1.00 28.99 O ANISOU 5345 O HOH A 524 3839 4002 3174 349 430 -81 O HETATM 5346 O HOH A 525 -7.550 17.751 18.582 1.00 36.45 O ANISOU 5346 O HOH A 525 4635 4770 4444 -73 184 -302 O HETATM 5347 O HOH A 526 19.183 10.903 8.678 1.00 26.53 O ANISOU 5347 O HOH A 526 3554 3160 3367 246 694 45 O HETATM 5348 O HOH A 527 10.585 19.961 40.586 1.00 21.13 O ANISOU 5348 O HOH A 527 2750 2456 2822 24 126 165 O HETATM 5349 O HOH A 528 -0.849 26.915 19.913 1.00 18.42 O ANISOU 5349 O HOH A 528 2399 2388 2213 73 231 65 O HETATM 5350 O HOH A 529 14.274 23.502 54.775 1.00 25.91 O ANISOU 5350 O HOH A 529 3270 3390 3184 278 -187 66 O HETATM 5351 O HOH A 530 13.547 7.863 18.654 1.00 20.74 O ANISOU 5351 O HOH A 530 2805 2266 2810 19 532 -31 O HETATM 5352 O HOH A 531 4.917 34.889 20.224 1.00 20.26 O ANISOU 5352 O HOH A 531 2584 2443 2671 158 335 308 O HETATM 5353 O HOH A 532 18.516 23.749 54.466 1.00 21.75 O ANISOU 5353 O HOH A 532 2650 2870 2742 300 -259 38 O HETATM 5354 O HOH A 533 14.755 39.601 14.570 1.00 26.69 O ANISOU 5354 O HOH A 533 3302 3030 3807 301 663 634 O HETATM 5355 O HOH A 534 18.777 22.359 2.203 1.00 38.53 O ANISOU 5355 O HOH A 534 5047 4936 4656 522 813 399 O HETATM 5356 O HOH A 535 13.591 25.773 42.055 1.00 19.81 O ANISOU 5356 O HOH A 535 2479 2310 2736 35 6 94 O HETATM 5357 O HOH A 536 -2.723 30.591 19.461 1.00 24.29 O ANISOU 5357 O HOH A 536 3120 3179 2932 128 220 120 O HETATM 5358 O HOH A 537 13.816 20.943 21.130 1.00 21.75 O ANISOU 5358 O HOH A 537 2834 2504 2927 63 387 194 O HETATM 5359 O HOH A 538 5.556 19.334 51.294 1.00 25.43 O ANISOU 5359 O HOH A 538 3368 3183 3111 153 87 199 O HETATM 5360 O HOH A 539 18.644 19.545 56.669 1.00 31.16 O ANISOU 5360 O HOH A 539 3904 4130 3803 420 -212 178 O HETATM 5361 O HOH A 540 10.033 18.158 1.045 1.00 29.55 O ANISOU 5361 O HOH A 540 3956 4075 3198 471 574 -3 O HETATM 5362 O HOH A 541 -3.340 41.383 14.494 1.00 39.73 O ANISOU 5362 O HOH A 541 5032 5170 4893 421 375 466 O HETATM 5363 O HOH A 542 2.965 13.680 18.837 1.00 24.08 O ANISOU 5363 O HOH A 542 3180 2944 3027 -48 342 -157 O HETATM 5364 O HOH A 543 17.745 25.570 29.605 1.00 21.53 O ANISOU 5364 O HOH A 543 2675 2381 3125 22 243 225 O HETATM 5365 O HOH A 544 13.453 20.444 59.400 1.00 22.13 O ANISOU 5365 O HOH A 544 2857 3056 2494 438 -173 168 O HETATM 5366 O HOH A 545 9.282 20.823 57.145 1.00 21.79 O ANISOU 5366 O HOH A 545 2871 2909 2500 325 -68 172 O HETATM 5367 O HOH A 546 20.428 24.729 9.932 1.00 26.87 O ANISOU 5367 O HOH A 546 3462 3200 3547 319 704 447 O HETATM 5368 O HOH A 547 5.078 35.028 10.031 1.00 24.76 O ANISOU 5368 O HOH A 547 3202 3247 2960 425 500 473 O HETATM 5369 O HOH A 548 8.457 24.668 14.265 1.00 17.91 O ANISOU 5369 O HOH A 548 2374 2245 2187 183 411 191 O HETATM 5370 O HOH A 549 11.860 25.239 37.516 1.00 24.47 O ANISOU 5370 O HOH A 549 3106 2857 3335 -3 96 126 O HETATM 5371 O HOH A 550 13.503 33.151 13.299 1.00 26.61 O ANISOU 5371 O HOH A 550 3387 3190 3535 290 577 497 O HETATM 5372 O HOH A 551 15.073 6.993 16.353 1.00 24.65 O ANISOU 5372 O HOH A 551 3310 2762 3293 54 581 -49 O HETATM 5373 O HOH A 552 4.360 40.311 15.457 1.00 27.73 O ANISOU 5373 O HOH A 552 3510 3418 3609 335 476 513 O HETATM 5374 O HOH A 553 23.067 34.968 10.418 1.00 35.17 O ANISOU 5374 O HOH A 553 4351 4051 4961 361 862 736 O HETATM 5375 O HOH A 554 14.328 27.563 3.085 1.00 23.81 O ANISOU 5375 O HOH A 554 3158 3146 2741 546 736 483 O HETATM 5376 O HOH A 555 14.202 26.185 16.891 1.00 20.23 O ANISOU 5376 O HOH A 555 2614 2359 2713 158 462 308 O HETATM 5377 O HOH A 556 8.262 28.239 55.690 1.00 22.59 O ANISOU 5377 O HOH A 556 2891 2981 2710 212 -185 -61 O HETATM 5378 O HOH A 557 12.911 14.479 4.417 1.00 31.06 O ANISOU 5378 O HOH A 557 4146 4036 3620 332 602 -46 O HETATM 5379 O HOH A 558 10.202 23.300 39.011 1.00 25.75 O ANISOU 5379 O HOH A 558 3306 3043 3436 -1 101 128 O HETATM 5380 O HOH A 559 19.255 16.507 4.503 1.00 30.62 O ANISOU 5380 O HOH A 559 4065 3840 3727 395 751 198 O HETATM 5381 O HOH A 560 22.554 22.356 14.756 1.00 24.49 O ANISOU 5381 O HOH A 560 3118 2777 3411 209 620 388 O HETATM 5382 O HOH A 561 -0.937 29.042 13.670 1.00 37.12 O ANISOU 5382 O HOH A 561 4769 4915 4419 238 281 137 O HETATM 5383 O HOH A 562 7.925 36.306 17.417 1.00 19.15 O ANISOU 5383 O HOH A 562 2429 2262 2587 227 439 420 O HETATM 5384 O HOH A 563 13.456 18.565 19.768 1.00 26.31 O ANISOU 5384 O HOH A 563 3438 3093 3466 65 413 153 O HETATM 5385 O HOH A 564 0.733 23.923 18.254 1.00 22.24 O ANISOU 5385 O HOH A 564 2904 2868 2680 69 260 24 O HETATM 5386 O HOH A 565 -4.150 17.745 16.078 1.00 24.51 O ANISOU 5386 O HOH A 565 3163 3260 2888 -8 220 -258 O HETATM 5387 O HOH A 566 6.132 25.958 4.031 1.00 33.05 O ANISOU 5387 O HOH A 566 4337 4534 3688 483 497 220 O HETATM 5388 O HOH A 567 -8.211 23.432 60.953 1.00 40.44 O ANISOU 5388 O HOH A 567 5362 5320 4683 260 216 164 O HETATM 5389 O HOH A 568 20.799 27.305 6.913 1.00 39.69 O ANISOU 5389 O HOH A 568 5085 4867 5130 421 806 563 O HETATM 5390 O HOH A 569 -2.029 24.882 13.663 1.00 22.53 O ANISOU 5390 O HOH A 569 2927 3094 2541 170 244 -14 O HETATM 5391 O HOH A 570 20.470 24.827 6.553 1.00 29.92 O ANISOU 5391 O HOH A 570 3879 3664 3824 413 782 486 O HETATM 5392 O HOH A 571 14.047 34.152 2.867 1.00 52.68 O ANISOU 5392 O HOH A 571 6766 6746 6505 638 837 734 O HETATM 5393 O HOH A 572 22.350 33.461 14.739 1.00 33.79 O ANISOU 5393 O HOH A 572 4163 3853 4824 241 697 589 O HETATM 5394 O HOH A 573 -0.897 21.029 10.536 1.00 34.31 O ANISOU 5394 O HOH A 573 4440 4637 3959 186 270 -130 O HETATM 5395 O HOH A 574 2.205 42.220 18.443 1.00 26.03 O ANISOU 5395 O HOH A 574 3273 3160 3456 288 420 466 O HETATM 5396 O HOH A 575 -0.720 36.177 10.112 1.00 27.79 O ANISOU 5396 O HOH A 575 3571 3790 3199 460 395 409 O HETATM 5397 O HOH A 576 13.624 18.077 -3.665 1.00 28.63 O ANISOU 5397 O HOH A 576 3884 4049 2946 656 732 83 O HETATM 5398 O HOH A 577 20.593 12.800 8.288 1.00 48.63 O ANISOU 5398 O HOH A 577 6335 5961 6179 281 719 132 O HETATM 5399 O HOH A 578 11.262 30.621 5.075 1.00 34.78 O ANISOU 5399 O HOH A 578 4521 4535 4158 517 662 508 O HETATM 5400 O HOH A 579 5.723 19.218 30.953 1.00 29.93 O ANISOU 5400 O HOH A 579 3898 3563 3910 -61 240 87 O HETATM 5401 O HOH A 580 21.396 6.436 13.232 1.00 27.93 O ANISOU 5401 O HOH A 580 3720 3134 3758 168 709 47 O HETATM 5402 O HOH A 581 7.675 38.525 16.647 1.00 36.96 O ANISOU 5402 O HOH A 581 4669 4502 4870 268 480 482 O HETATM 5403 O HOH A 582 2.318 41.291 15.846 1.00 30.50 O ANISOU 5403 O HOH A 582 3858 3800 3932 347 451 506 O HETATM 5404 O HOH A 583 11.954 28.035 2.128 1.00 33.38 O ANISOU 5404 O HOH A 583 4383 4460 3838 586 698 457 O HETATM 5405 O HOH A 584 18.797 14.609 3.380 1.00 27.25 O ANISOU 5405 O HOH A 584 3664 3447 3244 405 755 116 O HETATM 5406 O HOH A 585 -0.812 26.204 15.289 1.00 28.73 O ANISOU 5406 O HOH A 585 3713 3805 3397 156 259 52 O HETATM 5407 O HOH A 586 2.556 22.430 5.395 1.00 32.82 O ANISOU 5407 O HOH A 586 4293 4552 3626 370 372 -15 O HETATM 5408 O HOH A 587 4.247 24.365 3.789 1.00 40.06 O ANISOU 5408 O HOH A 587 5223 5487 4510 461 438 107 O HETATM 5409 O HOH A 588 22.599 22.550 10.435 1.00 42.16 O ANISOU 5409 O HOH A 588 5392 5086 5542 302 722 429 O HETATM 5410 O HOH B 501 -11.954 34.694 73.686 1.00 30.03 O ANISOU 5410 O HOH B 501 4096 4468 2847 618 38 -229 O HETATM 5411 O HOH B 502 -28.679 35.964 66.764 1.00 30.71 O ANISOU 5411 O HOH B 502 4034 4273 3363 331 460 -74 O HETATM 5412 O HOH B 503 -30.288 42.393 48.739 1.00 18.08 O ANISOU 5412 O HOH B 503 2168 2489 2212 104 225 -139 O HETATM 5413 O HOH B 504 -4.393 25.026 66.362 1.00 44.29 O ANISOU 5413 O HOH B 504 5873 6014 4940 460 77 116 O HETATM 5414 O HOH B 505 -24.816 37.514 47.261 1.00 22.61 O ANISOU 5414 O HOH B 505 2811 3012 2766 21 185 -109 O HETATM 5415 O HOH B 506 -21.558 49.480 62.868 1.00 31.73 O ANISOU 5415 O HOH B 506 4094 4197 3763 297 106 -501 O HETATM 5416 O HOH B 507 -21.383 36.070 18.091 1.00 27.59 O ANISOU 5416 O HOH B 507 3300 4107 3076 286 6 -29 O HETATM 5417 O HOH B 508 -17.126 31.091 33.591 1.00 23.79 O ANISOU 5417 O HOH B 508 2962 3145 2934 -62 107 -81 O HETATM 5418 O HOH B 509 -23.885 25.701 17.384 1.00 30.45 O ANISOU 5418 O HOH B 509 3563 4526 3480 40 -72 -450 O HETATM 5419 O HOH B 510 -37.814 39.463 57.083 1.00 32.62 O ANISOU 5419 O HOH B 510 3979 4434 3983 150 464 -121 O HETATM 5420 O HOH B 511 -15.429 49.775 59.161 1.00 23.75 O ANISOU 5420 O HOH B 511 3043 3056 2925 206 1 -506 O HETATM 5421 O HOH B 512 -25.280 37.945 70.841 1.00 29.82 O ANISOU 5421 O HOH B 512 4004 4272 3054 470 365 -175 O HETATM 5422 O HOH B 513 -13.194 31.637 58.462 1.00 18.25 O ANISOU 5422 O HOH B 513 2475 2497 1962 159 137 -57 O HETATM 5423 O HOH B 514 -25.339 37.316 24.092 1.00 25.37 O ANISOU 5423 O HOH B 514 2970 3733 2939 187 8 -68 O HETATM 5424 O HOH B 515 -12.420 18.595 64.296 1.00 31.24 O ANISOU 5424 O HOH B 515 4250 4149 3470 335 477 373 O HETATM 5425 O HOH B 516 -26.693 25.774 65.611 1.00 25.39 O ANISOU 5425 O HOH B 516 3382 3484 2781 252 641 204 O HETATM 5426 O HOH B 517 -17.152 48.965 56.950 1.00 25.39 O ANISOU 5426 O HOH B 517 3245 3251 3152 183 46 -414 O HETATM 5427 O HOH B 518 -25.845 21.938 65.702 1.00 30.00 O ANISOU 5427 O HOH B 518 3981 4006 3411 244 737 316 O HETATM 5428 O HOH B 519 -23.513 34.169 36.457 1.00 33.65 O ANISOU 5428 O HOH B 519 4134 4469 4183 -35 113 -106 O HETATM 5429 O HOH B 520 -17.398 36.086 16.324 1.00 26.38 O ANISOU 5429 O HOH B 520 3215 3901 2908 323 59 49 O HETATM 5430 O HOH B 521 -20.147 37.036 34.921 1.00 20.20 O ANISOU 5430 O HOH B 521 2469 2722 2484 20 96 -48 O HETATM 5431 O HOH B 522 -33.347 26.140 56.181 1.00 22.08 O ANISOU 5431 O HOH B 522 2694 2947 2747 -38 607 39 O HETATM 5432 O HOH B 523 -13.374 24.033 17.498 1.00 25.61 O ANISOU 5432 O HOH B 523 3175 3632 2925 32 75 -265 O HETATM 5433 O HOH B 524 -18.780 30.565 60.084 1.00 18.85 O ANISOU 5433 O HOH B 524 2550 2606 2007 169 277 -4 O HETATM 5434 O HOH B 525 -19.951 27.003 70.838 1.00 29.96 O ANISOU 5434 O HOH B 525 4102 4255 3027 489 480 189 O HETATM 5435 O HOH B 526 -13.843 26.414 64.625 1.00 21.09 O ANISOU 5435 O HOH B 526 2927 2976 2113 321 284 119 O HETATM 5436 O HOH B 527 -12.749 28.797 65.085 1.00 25.74 O ANISOU 5436 O HOH B 527 3507 3600 2672 339 198 33 O HETATM 5437 O HOH B 528 -10.276 32.369 65.502 1.00 28.69 O ANISOU 5437 O HOH B 528 3855 4009 3038 356 55 -115 O HETATM 5438 O HOH B 529 -20.088 30.990 74.533 1.00 36.02 O ANISOU 5438 O HOH B 529 4902 5187 3599 626 399 48 O HETATM 5439 O HOH B 530 -10.536 32.442 69.034 1.00 27.12 O ANISOU 5439 O HOH B 530 3691 3928 2685 468 55 -127 O HETATM 5440 O HOH B 531 -34.589 18.744 55.972 1.00 28.38 O ANISOU 5440 O HOH B 531 3427 3588 3767 -153 827 119 O HETATM 5441 O HOH B 532 -12.118 33.372 21.066 1.00 26.55 O ANISOU 5441 O HOH B 532 3322 3642 3124 142 114 35 O HETATM 5442 O HOH B 533 -22.191 32.108 61.374 1.00 19.31 O ANISOU 5442 O HOH B 533 2592 2699 2046 192 328 -24 O HETATM 5443 O HOH B 534 -31.564 27.344 61.571 1.00 32.95 O ANISOU 5443 O HOH B 534 4196 4388 3934 112 648 112 O HETATM 5444 O HOH B 535 -28.518 30.463 59.940 1.00 24.78 O ANISOU 5444 O HOH B 535 3192 3367 2858 118 482 24 O HETATM 5445 O HOH B 536 -22.889 20.539 58.287 1.00 21.92 O ANISOU 5445 O HOH B 536 2891 2834 2603 43 590 206 O HETATM 5446 O HOH B 537 -25.659 21.775 55.502 1.00 20.56 O ANISOU 5446 O HOH B 537 2636 2654 2521 -41 564 118 O HETATM 5447 O HOH B 538 -18.245 44.090 68.946 1.00 37.54 O ANISOU 5447 O HOH B 538 4934 5164 4163 419 61 -482 O HETATM 5448 O HOH B 539 -16.491 33.264 20.790 1.00 24.84 O ANISOU 5448 O HOH B 539 3045 3544 2851 150 63 -37 O HETATM 5449 O HOH B 540 -31.453 29.785 55.636 1.00 19.33 O ANISOU 5449 O HOH B 540 2387 2638 2319 9 484 -12 O HETATM 5450 O HOH B 541 -16.482 30.600 58.639 1.00 23.26 O ANISOU 5450 O HOH B 541 3105 3134 2597 146 221 -18 O HETATM 5451 O HOH B 542 -20.525 33.644 36.799 1.00 22.71 O ANISOU 5451 O HOH B 542 2797 3028 2803 -43 114 -85 O HETATM 5452 O HOH B 543 -20.552 38.921 74.528 1.00 34.82 O ANISOU 5452 O HOH B 543 4699 5045 3486 605 220 -296 O HETATM 5453 O HOH B 544 -30.201 32.917 57.264 1.00 21.63 O ANISOU 5453 O HOH B 544 2728 2964 2527 80 428 -41 O HETATM 5454 O HOH B 545 -31.295 43.211 14.336 1.00 32.81 O ANISOU 5454 O HOH B 545 3734 5201 3533 646 -96 84 O HETATM 5455 O HOH B 546 -27.883 43.395 56.465 1.00 18.83 O ANISOU 5455 O HOH B 546 2382 2582 2188 178 248 -213 O HETATM 5456 O HOH B 547 -11.372 46.023 66.293 1.00 30.63 O ANISOU 5456 O HOH B 547 3984 4172 3482 331 -122 -612 O HETATM 5457 O HOH B 548 -17.294 24.046 62.590 1.00 25.25 O ANISOU 5457 O HOH B 548 3424 3408 2762 230 418 188 O HETATM 5458 O HOH B 549 -16.400 29.314 72.509 1.00 25.29 O ANISOU 5458 O HOH B 549 3532 3770 2306 574 315 72 O HETATM 5459 O HOH B 550 -18.695 31.943 37.818 1.00 17.85 O ANISOU 5459 O HOH B 550 2216 2371 2197 -68 125 -80 O HETATM 5460 O HOH B 551 -12.708 31.291 45.912 1.00 25.66 O ANISOU 5460 O HOH B 551 3317 3271 3162 -34 122 -42 O HETATM 5461 O HOH B 552 -7.113 30.731 60.197 1.00 27.24 O ANISOU 5461 O HOH B 552 3628 3676 3047 228 28 -68 O HETATM 5462 O HOH B 553 -16.662 36.244 54.351 1.00 25.10 O ANISOU 5462 O HOH B 553 3270 3305 2963 88 125 -130 O HETATM 5463 O HOH B 554 -19.915 33.412 52.199 1.00 24.94 O ANISOU 5463 O HOH B 554 3219 3281 2976 32 201 -74 O HETATM 5464 O HOH B 555 -28.327 14.665 57.174 1.00 31.61 O ANISOU 5464 O HOH B 555 3991 3894 4126 -98 867 259 O HETATM 5465 O HOH B 556 -22.643 28.642 19.740 1.00 25.58 O ANISOU 5465 O HOH B 556 3004 3816 2900 66 -29 -296 O HETATM 5466 O HOH B 557 -7.831 21.856 64.858 1.00 33.84 O ANISOU 5466 O HOH B 557 4574 4581 3703 394 259 250 O HETATM 5467 O HOH B 558 -16.248 17.074 60.757 1.00 25.53 O ANISOU 5467 O HOH B 558 3464 3284 2954 172 586 354 O HETATM 5468 O HOH B 559 -32.653 32.061 61.728 1.00 28.73 O ANISOU 5468 O HOH B 559 3650 3913 3352 156 565 16 O HETATM 5469 O HOH B 560 -17.166 38.452 55.768 1.00 23.79 O ANISOU 5469 O HOH B 560 3103 3153 2783 120 110 -179 O HETATM 5470 O HOH B 561 -34.671 39.035 59.544 1.00 20.62 O ANISOU 5470 O HOH B 561 2557 2906 2372 184 450 -120 O HETATM 5471 O HOH B 562 -26.533 16.374 60.045 1.00 32.01 O ANISOU 5471 O HOH B 562 4129 4029 4003 22 832 322 O HETATM 5472 O HOH B 563 -3.257 29.717 17.486 1.00 32.35 O ANISOU 5472 O HOH B 563 4143 4263 3887 156 222 99 O HETATM 5473 O HOH B 564 -8.013 34.765 60.770 1.00 24.17 O ANISOU 5473 O HOH B 564 3213 3297 2675 228 -26 -189 O HETATM 5474 O HOH B 565 -11.468 40.356 71.261 1.00 33.53 O ANISOU 5474 O HOH B 565 4455 4789 3496 499 -82 -470 O HETATM 5475 O HOH B 566 -31.518 35.903 64.945 1.00 36.50 O ANISOU 5475 O HOH B 566 4702 4971 4194 275 509 -57 O HETATM 5476 O HOH B 567 -17.771 42.585 71.345 1.00 33.25 O ANISOU 5476 O HOH B 567 4430 4718 3486 492 66 -464 O HETATM 5477 O HOH B 568 -28.574 42.194 13.564 1.00 45.22 O ANISOU 5477 O HOH B 568 5370 6721 5092 624 -69 96 O HETATM 5478 O HOH B 569 -31.376 20.679 65.629 1.00 30.85 O ANISOU 5478 O HOH B 569 3990 4058 3672 176 925 353 O HETATM 5479 O HOH B 570 -9.840 30.070 68.131 1.00 35.53 O ANISOU 5479 O HOH B 570 4764 4959 3775 453 92 -36 O HETATM 5480 O HOH B 571 -25.108 37.528 44.653 1.00 23.65 O ANISOU 5480 O HOH B 571 2913 3153 2918 10 168 -104 O HETATM 5481 O HOH B 572 -11.958 37.595 19.464 1.00 27.68 O ANISOU 5481 O HOH B 572 3458 3800 3261 256 151 162 O HETATM 5482 O HOH B 573 -26.707 11.655 56.067 1.00 31.14 O ANISOU 5482 O HOH B 573 3938 3736 4156 -135 915 285 O HETATM 5483 O HOH B 574 -22.948 18.120 58.584 1.00 40.19 O ANISOU 5483 O HOH B 574 5207 5100 4963 34 669 262 O HETATM 5484 O HOH B 575 -28.825 15.325 60.035 1.00 32.36 O ANISOU 5484 O HOH B 575 4124 4036 4135 -16 921 332 O HETATM 5485 O HOH B 576 -31.264 30.708 60.306 1.00 44.14 O ANISOU 5485 O HOH B 576 5604 5831 5336 116 540 26 O HETATM 5486 O HOH B 577 -19.150 28.946 73.556 1.00 27.67 O ANISOU 5486 O HOH B 577 3844 4084 2584 598 420 122 O HETATM 5487 O HOH B 578 -12.347 42.592 71.956 1.00 31.35 O ANISOU 5487 O HOH B 578 4169 4514 3227 510 -96 -564 O HETATM 5488 O HOH B 579 -1.998 27.299 17.516 1.00 26.03 O ANISOU 5488 O HOH B 579 3358 3434 3100 121 231 57 O HETATM 5489 O HOH B 580 -34.025 26.807 58.471 1.00 32.14 O ANISOU 5489 O HOH B 580 3992 4249 3971 15 652 68 O HETATM 5490 O HOH B 581 -32.849 29.188 58.265 1.00 29.97 O ANISOU 5490 O HOH B 581 3744 4003 3639 46 569 29 O HETATM 5491 O HOH B 582 -8.482 34.979 65.502 1.00 35.88 O ANISOU 5491 O HOH B 582 4734 4921 3978 352 -41 -230 O HETATM 5492 O HOH B 583 -21.332 36.830 81.984 1.00 44.26 O ANISOU 5492 O HOH B 583 6016 6551 4251 916 327 -218 O CONECT 1 5026 CONECT 13 5049 CONECT 114 4970 CONECT 923 1474 CONECT 1474 923 CONECT 2277 5043 CONECT 2490 5147 CONECT 2492 5207 CONECT 2504 5230 CONECT 2605 4998 CONECT 3406 3957 CONECT 3957 3406 CONECT 4754 5224 CONECT 4968 5308 CONECT 4970 114 4971 4981 CONECT 4971 4970 4972 4978 CONECT 4972 4971 4973 4979 CONECT 4973 4972 4974 4980 CONECT 4974 4973 4975 4981 CONECT 4975 4974 4982 CONECT 4976 4977 4978 4983 CONECT 4977 4976 CONECT 4978 4971 4976 CONECT 4979 4972 CONECT 4980 4973 4984 CONECT 4981 4970 4974 CONECT 4982 4975 CONECT 4983 4976 CONECT 4984 4980 4985 4995 CONECT 4985 4984 4986 4992 CONECT 4986 4985 4987 4993 CONECT 4987 4986 4988 4994 CONECT 4988 4987 4989 4995 CONECT 4989 4988 4996 CONECT 4990 4991 4992 4997 CONECT 4991 4990 CONECT 4992 4985 4990 CONECT 4993 4986 CONECT 4994 4987 CONECT 4995 4984 4988 CONECT 4996 4989 CONECT 4997 4990 CONECT 4998 2605 4999 5009 CONECT 4999 4998 5000 5006 CONECT 5000 4999 5001 5007 CONECT 5001 5000 5002 5008 CONECT 5002 5001 5003 5009 CONECT 5003 5002 5010 CONECT 5004 5005 5006 5011 CONECT 5005 5004 CONECT 5006 4999 5004 CONECT 5007 5000 CONECT 5008 5001 5012 CONECT 5009 4998 5002 CONECT 5010 5003 CONECT 5011 5004 CONECT 5012 5008 5013 5023 CONECT 5013 5012 5014 5020 CONECT 5014 5013 5015 5021 CONECT 5015 5014 5016 5022 CONECT 5016 5015 5017 5023 CONECT 5017 5016 5024 CONECT 5018 5019 5020 5025 CONECT 5019 5018 CONECT 5020 5013 5018 CONECT 5021 5014 CONECT 5022 5015 CONECT 5023 5012 5016 CONECT 5024 5017 CONECT 5025 5018 CONECT 5026 1 5027 5028 CONECT 5027 5026 CONECT 5028 5026 CONECT 5029 5030 5034 5044 5045 CONECT 5030 5029 5031 CONECT 5031 5030 5032 CONECT 5032 5031 5033 CONECT 5033 5032 5034 5046 CONECT 5034 5029 5033 5035 CONECT 5035 5034 5036 CONECT 5036 5035 5037 CONECT 5037 5036 5038 5047 CONECT 5038 5037 5039 CONECT 5039 5038 5040 CONECT 5040 5039 5041 CONECT 5041 5040 5042 5048 CONECT 5042 5041 5043 CONECT 5043 2277 5042 CONECT 5044 5029 CONECT 5045 5029 CONECT 5046 5033 CONECT 5047 5037 CONECT 5048 5041 CONECT 5049 13 5050 5060 CONECT 5050 5049 5051 5057 CONECT 5051 5050 5052 5058 CONECT 5052 5051 5053 5059 CONECT 5053 5052 5054 5060 CONECT 5054 5053 5061 CONECT 5055 5056 5057 5062 CONECT 5056 5055 CONECT 5057 5050 5055 CONECT 5058 5051 CONECT 5059 5052 CONECT 5060 5049 5053 CONECT 5061 5054 CONECT 5062 5055 CONECT 5063 5065 CONECT 5064 5065 CONECT 5065 5063 5064 5066 CONECT 5066 5065 5067 CONECT 5067 5066 5068 CONECT 5068 5067 5069 CONECT 5069 5068 5070 CONECT 5070 5069 5071 CONECT 5071 5070 5072 CONECT 5072 5071 5073 CONECT 5073 5072 5074 CONECT 5074 5073 5075 CONECT 5075 5074 CONECT 5076 5079 CONECT 5077 5078 5080 CONECT 5078 5077 5081 CONECT 5079 5076 5083 CONECT 5080 5077 5084 CONECT 5081 5078 5085 CONECT 5082 5096 5098 CONECT 5083 5079 5086 CONECT 5084 5080 5087 CONECT 5085 5081 5088 CONECT 5086 5083 5089 CONECT 5087 5084 5089 CONECT 5088 5085 5090 CONECT 5089 5086 5087 CONECT 5090 5088 5091 CONECT 5091 5090 5092 CONECT 5092 5091 5093 CONECT 5093 5092 5095 CONECT 5094 5096 5100 CONECT 5095 5093 5097 5100 CONECT 5096 5082 5094 5099 CONECT 5097 5095 CONECT 5098 5082 CONECT 5099 5096 CONECT 5100 5094 5095 CONECT 5101 5102 5103 CONECT 5102 5101 5104 CONECT 5103 5101 5105 CONECT 5104 5102 5106 CONECT 5105 5103 5108 CONECT 5106 5104 5109 CONECT 5107 5110 CONECT 5108 5105 5110 CONECT 5109 5106 5111 CONECT 5110 5107 5108 CONECT 5111 5109 5112 CONECT 5112 5111 5113 CONECT 5113 5112 5114 CONECT 5114 5113 5115 CONECT 5115 5114 5116 5117 CONECT 5116 5115 CONECT 5117 5115 CONECT 5118 5119 5120 CONECT 5119 5118 5121 CONECT 5120 5118 5122 CONECT 5121 5119 5123 CONECT 5122 5120 5124 CONECT 5123 5121 CONECT 5124 5122 CONECT 5125 5126 5127 CONECT 5126 5125 5128 CONECT 5127 5125 5129 CONECT 5128 5126 5130 CONECT 5129 5127 5131 CONECT 5130 5128 5132 CONECT 5131 5129 5133 CONECT 5132 5130 5134 CONECT 5133 5131 CONECT 5134 5132 CONECT 5135 5136 5137 CONECT 5136 5135 5138 CONECT 5137 5135 5139 CONECT 5138 5136 5140 CONECT 5139 5137 5141 CONECT 5140 5138 5142 CONECT 5141 5139 CONECT 5142 5140 5143 CONECT 5143 5142 5144 CONECT 5144 5143 5145 CONECT 5145 5144 5146 CONECT 5146 5145 CONECT 5147 2490 5148 5149 CONECT 5148 5147 CONECT 5149 5147 5150 CONECT 5150 5149 5151 CONECT 5151 5150 5152 CONECT 5152 5151 5153 CONECT 5153 5152 5154 CONECT 5154 5153 5155 CONECT 5155 5154 5156 CONECT 5156 5155 5157 CONECT 5157 5156 5158 CONECT 5158 5157 CONECT 5159 5160 CONECT 5160 5159 5161 CONECT 5161 5160 5162 CONECT 5162 5161 5163 CONECT 5163 5162 5164 CONECT 5164 5163 5165 CONECT 5165 5164 5166 CONECT 5166 5165 5167 5168 CONECT 5167 5166 CONECT 5168 5166 CONECT 5169 5172 CONECT 5170 5171 5173 CONECT 5171 5170 5174 CONECT 5172 5169 5176 CONECT 5173 5170 5177 CONECT 5174 5171 5178 CONECT 5175 5189 5191 CONECT 5176 5172 5179 CONECT 5177 5173 5180 CONECT 5178 5174 5181 CONECT 5179 5176 5182 CONECT 5180 5177 5182 CONECT 5181 5178 5183 CONECT 5182 5179 5180 CONECT 5183 5181 5184 CONECT 5184 5183 5185 CONECT 5185 5184 5186 CONECT 5186 5185 5188 CONECT 5187 5189 5193 CONECT 5188 5186 5190 5193 CONECT 5189 5175 5187 5192 CONECT 5190 5188 CONECT 5191 5175 CONECT 5192 5189 CONECT 5193 5187 5188 CONECT 5194 5195 5196 CONECT 5195 5194 5197 CONECT 5196 5194 5198 CONECT 5197 5195 5199 CONECT 5198 5196 5200 CONECT 5199 5197 5201 CONECT 5200 5198 5202 CONECT 5201 5199 5203 CONECT 5202 5200 CONECT 5203 5201 5204 CONECT 5204 5203 5205 CONECT 5205 5204 5206 CONECT 5206 5205 CONECT 5207 2492 5208 5209 CONECT 5208 5207 CONECT 5209 5207 CONECT 5210 5211 5215 5225 5226 CONECT 5211 5210 5212 CONECT 5212 5211 5213 CONECT 5213 5212 5214 CONECT 5214 5213 5215 5227 CONECT 5215 5210 5214 5216 CONECT 5216 5215 5217 CONECT 5217 5216 5218 CONECT 5218 5217 5219 5228 CONECT 5219 5218 5220 CONECT 5220 5219 5221 CONECT 5221 5220 5222 CONECT 5222 5221 5223 5229 CONECT 5223 5222 5224 CONECT 5224 4754 5223 CONECT 5225 5210 CONECT 5226 5210 CONECT 5227 5214 CONECT 5228 5218 CONECT 5229 5222 CONECT 5230 2504 5231 5241 CONECT 5231 5230 5232 5238 CONECT 5232 5231 5233 5239 CONECT 5233 5232 5234 5240 CONECT 5234 5233 5235 5241 CONECT 5235 5234 5242 CONECT 5236 5237 5238 5243 CONECT 5237 5236 CONECT 5238 5231 5236 CONECT 5239 5232 CONECT 5240 5233 CONECT 5241 5230 5234 CONECT 5242 5235 CONECT 5243 5236 CONECT 5244 5245 5246 CONECT 5245 5244 5247 CONECT 5246 5244 5248 CONECT 5247 5245 5249 CONECT 5248 5246 5251 CONECT 5249 5247 5252 CONECT 5250 5253 CONECT 5251 5248 5253 CONECT 5252 5249 5254 CONECT 5253 5250 5251 CONECT 5254 5252 5255 CONECT 5255 5254 5256 CONECT 5256 5255 5257 CONECT 5257 5256 5259 CONECT 5258 5260 5262 CONECT 5259 5257 5261 5262 CONECT 5260 5258 CONECT 5261 5259 CONECT 5262 5258 5259 CONECT 5263 5264 CONECT 5264 5263 5265 CONECT 5265 5264 5266 CONECT 5266 5265 5267 CONECT 5267 5266 5268 CONECT 5268 5267 5269 CONECT 5269 5268 5270 CONECT 5270 5269 5271 5272 CONECT 5271 5270 CONECT 5272 5270 CONECT 5273 5274 5275 CONECT 5274 5273 5276 CONECT 5275 5273 CONECT 5276 5274 5278 CONECT 5277 5286 5288 CONECT 5278 5276 5279 CONECT 5279 5278 5280 CONECT 5280 5279 5281 CONECT 5281 5280 5282 CONECT 5282 5281 5283 CONECT 5283 5282 5285 CONECT 5284 5286 5290 CONECT 5285 5283 5287 5290 CONECT 5286 5277 5284 5289 CONECT 5287 5285 CONECT 5288 5277 CONECT 5289 5286 CONECT 5290 5284 5285 CONECT 5291 5294 CONECT 5292 5293 5295 CONECT 5293 5292 5296 CONECT 5294 5291 5297 CONECT 5295 5292 5298 CONECT 5296 5293 5299 CONECT 5297 5294 5300 CONECT 5298 5295 5301 CONECT 5299 5296 5302 CONECT 5300 5297 5303 CONECT 5301 5298 5303 CONECT 5302 5299 5304 CONECT 5303 5300 5301 CONECT 5304 5302 5305 CONECT 5305 5304 5306 CONECT 5306 5305 5307 CONECT 5307 5306 CONECT 5308 4968 5309 5310 CONECT 5309 5308 CONECT 5310 5308 5311 CONECT 5311 5310 5312 CONECT 5312 5311 5313 CONECT 5313 5312 5314 CONECT 5314 5313 CONECT 5315 5316 5317 CONECT 5316 5315 5318 CONECT 5317 5315 5319 CONECT 5318 5316 5320 CONECT 5319 5317 5321 CONECT 5320 5318 CONECT 5321 5319 MASTER 407 0 26 28 8 0 0 6 5329 2 366 54 END