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*** Apo AMPK ***elNémo ID: 260711175133601569Job options:ID = 260711175133601569 JOBID = Apo AMPK USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER Apo AMPK HEADER TRANSFERASE 18-NOV-13 4CFH TITLE STRUCTURE OF AN ACTIVE FORM OF MAMMALIAN AMPK COMPND MOL_ID: 1; COMPND 2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 13-481; COMPND 5 SYNONYM: AMPK SUBUNIT ALPHA-1; COMPND 6 EC: 2.7.11.1; COMPND 7 ENGINEERED: YES; COMPND 8 OTHER_DETAILS: PROTEASE RECOGNITION SITES WERE ENGINEERED INTO THE COMPND 9 ALPHA SUBUNIT AT BOTH ENDS OF A LARGE FLEXIBLE LOOP IN THE C-TERMINAL COMPND 10 REGION (RESIDUES 470 TO 524), RESIDUES 471 TO 523 WERE REMOVED FROM COMPND 11 THE PROTEIN, RESIDUES 523 TO 548 ARE GIVEN AS CHAIN C; COMPND 12 MOL_ID: 2; COMPND 13 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2; COMPND 14 CHAIN: B; COMPND 15 FRAGMENT: RESIDUES 187-272; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 3; COMPND 18 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1; COMPND 19 CHAIN: C; COMPND 20 FRAGMENT: RESIDUES 535-559; COMPND 21 SYNONYM: AMPK SUBUNIT ALPHA-1; COMPND 22 EC: 2.7.11.1; COMPND 23 ENGINEERED: YES; COMPND 24 OTHER_DETAILS: PROTEASE RECOGNITION SITES WERE ENGINEERED INTO THE COMPND 25 SUBUNIT ALPHA AT BOTH ENDS OF A LARGE FLEXIBLE LOOP IN THE C-TERMINAL COMPND 26 REGION (RESIDUES 470 AND 524), RESIDUES 471 TO 523 WERE REMOVED FROM COMPND 27 THE PROTEIN, RESIDUES 2 TO 470 ARE GIVEN AS CHAIN A; COMPND 28 MOL_ID: 4; COMPND 29 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1; COMPND 30 CHAIN: E; COMPND 31 SYNONYM: AMPK SUBUNIT ALPHA-1, AMPK GAMMA1, AMPK SUBUNIT GAMMA-1, COMPND 32 AMPKG; COMPND 33 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 15 ORGANISM_COMMON: NORWAY RAT; SOURCE 16 ORGANISM_TAXID: 10116; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 21 ORGANISM_COMMON: NORWAY RAT; SOURCE 22 ORGANISM_TAXID: 10116; SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS TRANSFERASE, TRANSFERASE PHOSPHORYLATION, ACTIVE FORM, NUCLEOTIDE- KEYWDS 2 BINDING, STAUROSPORINE-BINDING, SERINE/THREONINE-PROTEIN KINASE EXPDTA X-RAY DIFFRACTION AUTHOR B.XIAO,M.J.SANDERS,E.UNDERWOOD,R.HEATH,F.MAYER,D.CARMENA,C.JING, AUTHOR 2 P.A.WALKER,J.F.ECCLESTON,L.F.HAIRE,P.SAIU,S.A.HOWELL,R.AASLAND, AUTHOR 3 S.R.MARTIN,D.CARLING,S.J.GAMBLIN REVDAT 5 13-NOV-24 4CFH 1 REMARK REVDAT 4 20-DEC-23 4CFH 1 REMARK REVDAT 3 08-MAY-19 4CFH 1 REMARK LINK REVDAT 2 08-JAN-14 4CFH 1 REMARK REVDAT 1 25-DEC-13 4CFH 0 SPRSDE 25-DEC-13 4CFH 2Y94 JRNL AUTH B.XIAO,M.J.SANDERS,E.UNDERWOOD,R.HEATH,F.MAYER,D.CARMENA, JRNL AUTH 2 C.JING,P.A.WALKER,J.F.ECCLESTON,L.F.HAIRE,P.SAIU,S.A.HOWELL, JRNL AUTH 3 R.AASLAND,S.R.MARTIN,D.CARLING,S.J.GAMBLIN JRNL TITL STRUCTURE OF MAMMALIAN AMPK AND ITS REGULATION BY ADP JRNL REF NATURE V. 472 230 2011 JRNL REFN ISSN 0028-0836 JRNL PMID 21399626 JRNL DOI 10.1038/NATURE09932 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH B.XIAO,M.J.SANDERS,D.CARMENA,N.J.BRIGHT,L.F.HAIRE, REMARK 1 AUTH 2 E.UNDERWOOD,B.R.PATEL,R.B.HEATH,P.A.WALKER,S.HALLEN, REMARK 1 AUTH 3 F.GIORDANETTO,S.R.MARTIN,D.CARLING,S.J.GAMBLIN REMARK 1 TITL STRUCTURAL BASIS OF AMPK REGULATION BY SMALL MOLECULE REMARK 1 TITL 2 ACTIVATORS. REMARK 1 REF NAT.COMMUN. V. 4 3017 2013 REMARK 1 REFN ESSN 2041-1723 REMARK 1 PMID 24352254 REMARK 1 DOI 10.1038/NCOMMS4017 REMARK 2 REMARK 2 RESOLUTION. 3.24 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.24 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.53 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1 REMARK 3 NUMBER OF REFLECTIONS : 19619 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.234 REMARK 3 R VALUE (WORKING SET) : 0.233 REMARK 3 FREE R VALUE : 0.268 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 989 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 29.5333 - 6.1817 0.85 2601 132 0.2094 0.2439 REMARK 3 2 6.1817 - 4.9139 0.93 2679 134 0.2348 0.2903 REMARK 3 3 4.9139 - 4.2949 0.93 2637 154 0.2104 0.2440 REMARK 3 4 4.2949 - 3.9032 0.94 2679 131 0.2311 0.2708 REMARK 3 5 3.9032 - 3.6239 0.95 2669 140 0.2662 0.2823 REMARK 3 6 3.6239 - 3.4106 0.96 2682 152 0.2893 0.2967 REMARK 3 7 3.4106 - 3.2400 0.96 2683 146 0.3412 0.3568 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 4CFH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-NOV-13. REMARK 100 THE DEPOSITION ID IS D_1290058999. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-JUL-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18662 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.240 REMARK 200 RESOLUTION RANGE LOW (A) : 29.530 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3 REMARK 200 DATA REDUNDANCY : 4.500 REMARK 200 R MERGE (I) : 0.07000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.24 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.44 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8 REMARK 200 DATA REDUNDANCY IN SHELL : 4.50 REMARK 200 R MERGE FOR SHELL (I) : 0.51000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE, PHASER REMARK 200 STARTING MODEL: PDB ENTRIES 2V8Q AND 2H6D REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN BY THE HANGING REMARK 280 DROP METHOD WITH RESERVOIR SOLUTION CONTAINING 8% ISOPROPANOL REMARK 280 AND 5% MPD AS PRECIPITANT IN 0.1M TRIS AT PH 7.5 AT 18 DEGREES., REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-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 70.94800 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 66.95850 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 66.95850 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 35.47400 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 66.95850 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 66.95850 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 106.42200 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 66.95850 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.95850 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 35.47400 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 66.95850 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.95850 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 106.42200 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 70.94800 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 13440 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 40040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.5 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A -18 REMARK 465 SER A -17 REMARK 465 HIS A -16 REMARK 465 HIS A -15 REMARK 465 HIS A -14 REMARK 465 HIS A -13 REMARK 465 HIS A -12 REMARK 465 HIS A -11 REMARK 465 SER A -10 REMARK 465 SER A -9 REMARK 465 GLY A -8 REMARK 465 LEU A -7 REMARK 465 GLU A -6 REMARK 465 VAL A -5 REMARK 465 LEU A -4 REMARK 465 PHE A -3 REMARK 465 GLN A -2 REMARK 465 GLY A -1 REMARK 465 PRO A 0 REMARK 465 MET A 1 REMARK 465 ALA A 2 REMARK 465 GLU A 3 REMARK 465 LYS A 4 REMARK 465 GLN A 5 REMARK 465 LYS A 6 REMARK 465 HIS A 7 REMARK 465 ASP A 8 REMARK 465 GLY A 9 REMARK 465 PRO A 281 REMARK 465 SER A 282 REMARK 465 TYR A 283 REMARK 465 SER A 284 REMARK 465 SER A 285 REMARK 465 THR A 286 REMARK 465 MET A 287 REMARK 465 ILE A 288 REMARK 465 ASP A 289 REMARK 465 ASP A 290 REMARK 465 GLU A 291 REMARK 465 ALA A 292 REMARK 465 LEU A 293 REMARK 465 LYS A 294 REMARK 465 GLU A 295 REMARK 465 VAL A 296 REMARK 465 CYS A 297 REMARK 465 GLU A 298 REMARK 465 LYS A 299 REMARK 465 PHE A 300 REMARK 465 GLU A 301 REMARK 465 CYS A 302 REMARK 465 SER A 303 REMARK 465 GLU A 304 REMARK 465 GLU A 305 REMARK 465 GLU A 306 REMARK 465 VAL A 307 REMARK 465 LEU A 308 REMARK 465 SER A 309 REMARK 465 CYS A 310 REMARK 465 LEU A 311 REMARK 465 TYR A 312 REMARK 465 ASN A 313 REMARK 465 ARG A 314 REMARK 465 ASN A 315 REMARK 465 HIS A 316 REMARK 465 GLN A 317 REMARK 465 ASP A 318 REMARK 465 PRO A 319 REMARK 465 LEU A 320 REMARK 465 ARG A 375 REMARK 465 HIS A 376 REMARK 465 TPO A 377 REMARK 465 LEU A 378 REMARK 465 ASP A 379 REMARK 465 GLU A 380 REMARK 465 LEU A 381 REMARK 465 ASN A 382 REMARK 465 PRO A 383 REMARK 465 GLN A 384 REMARK 465 LYS A 385 REMARK 465 SER A 386 REMARK 465 LYS A 387 REMARK 465 HIS A 388 REMARK 465 GLN A 389 REMARK 465 GLY A 390 REMARK 465 VAL A 391 REMARK 465 ARG A 392 REMARK 465 LYS A 393 REMARK 465 LEU A 471 REMARK 465 GLU A 472 REMARK 465 VAL A 473 REMARK 465 LEU A 474 REMARK 465 MET B 186 REMARK 465 GLY B 187 REMARK 465 PRO B 188 REMARK 465 TYR B 189 REMARK 465 GLY B 190 REMARK 465 GLN B 191 REMARK 465 GLU B 192 REMARK 465 MET B 193 REMARK 465 TYR B 194 REMARK 465 ALA B 195 REMARK 465 PHE B 196 REMARK 465 ARG B 197 REMARK 465 SER B 198 REMARK 465 GLU B 199 REMARK 465 GLU B 200 REMARK 465 ARG B 201 REMARK 465 PHE B 202 REMARK 465 ILE B 272 REMARK 465 PHE C 522 REMARK 465 GLN C 523 REMARK 465 VAL C 524 REMARK 465 ALA C 525 REMARK 465 PRO C 526 REMARK 465 ARG C 527 REMARK 465 MET E 1 REMARK 465 GLU E 2 REMARK 465 SER E 3 REMARK 465 VAL E 4 REMARK 465 ALA E 5 REMARK 465 ALA E 6 REMARK 465 GLU E 7 REMARK 465 SER E 8 REMARK 465 ALA E 9 REMARK 465 PRO E 10 REMARK 465 ALA E 11 REMARK 465 PRO E 12 REMARK 465 GLU E 13 REMARK 465 ASN E 14 REMARK 465 GLU E 15 REMARK 465 HIS E 16 REMARK 465 SER E 17 REMARK 465 GLN E 18 REMARK 465 GLU E 19 REMARK 465 THR E 20 REMARK 465 PRO E 21 REMARK 465 GLU E 22 REMARK 465 SER E 23 REMARK 465 GLY E 325 REMARK 465 GLY E 326 REMARK 465 GLU E 327 REMARK 465 LYS E 328 REMARK 465 LYS E 329 REMARK 465 PRO E 330 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 VAL A 322 CG1 CG2 REMARK 470 TYR A 324 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 HIS A 325 CG ND1 CD2 CE1 NE2 REMARK 470 LEU A 326 CG CD1 CD2 REMARK 470 ILE A 327 CG1 CG2 CD1 REMARK 470 ILE A 328 CG1 CG2 CD1 REMARK 470 ASP A 329 CG OD1 OD2 REMARK 470 ASN A 330 CG OD1 ND2 REMARK 470 ARG A 331 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 332 CG CD NE CZ NH1 NH2 REMARK 470 ILE A 333 CG1 CG2 CD1 REMARK 470 MET A 334 CG SD CE REMARK 470 ASN A 335 CG OD1 ND2 REMARK 470 GLU A 336 CG CD OE1 OE2 REMARK 470 LYS A 338 CG CD CE NZ REMARK 470 ASP A 339 CG OD1 OD2 REMARK 470 LYS E 99 CG CD CE NZ REMARK 470 PHE E 182 CG CD1 CD2 CE1 CE2 CZ 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 PHE A 27 -31.27 -172.35 REMARK 500 CYS A 106 -65.90 58.89 REMARK 500 ASN A 108 175.83 59.55 REMARK 500 ARG A 110 -143.57 51.76 REMARK 500 HIS A 150 31.08 -94.07 REMARK 500 MET A 151 51.49 39.08 REMARK 500 ALA A 156 -79.88 -117.21 REMARK 500 ARG A 171 -122.51 66.12 REMARK 500 TPO A 172 -57.66 65.90 REMARK 500 SER A 173 86.06 60.99 REMARK 500 TYR A 179 -5.25 62.96 REMARK 500 GLN A 235 -103.76 51.25 REMARK 500 PHE A 277 159.40 68.29 REMARK 500 VAL A 322 50.52 -115.01 REMARK 500 ALA A 337 74.88 -104.24 REMARK 500 ARG A 363 40.81 -140.60 REMARK 500 ARG A 373 50.79 -142.86 REMARK 500 PRO A 439 30.25 -76.28 REMARK 500 VAL A 440 -54.71 -135.35 REMARK 500 VAL A 454 -65.10 -101.83 REMARK 500 ARG A 457 28.16 -152.71 REMARK 500 ASN B 239 -19.10 71.46 REMARK 500 ASP B 248 -97.58 56.78 REMARK 500 SER B 249 18.04 -154.70 REMARK 500 LYS B 260 -102.06 52.02 REMARK 500 SER E 26 82.69 99.98 REMARK 500 VAL E 27 -40.17 -156.55 REMARK 500 SER E 44 108.69 -160.14 REMARK 500 TYR E 97 31.55 -97.69 REMARK 500 HIS E 111 119.05 -160.99 REMARK 500 SER E 124 30.77 -166.38 REMARK 500 SER E 159 -37.53 64.18 REMARK 500 PHE E 178 40.58 -99.35 REMARK 500 PRO E 183 42.22 -88.92 REMARK 500 SER E 269 -123.67 52.80 REMARK 500 TYR E 271 58.34 -100.19 REMARK 500 PHE E 272 -9.31 -145.61 REMARK 500 GLU E 273 3.42 55.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP E 1325 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP E 1326 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STU A 1550 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4CFE RELATED DB: PDB REMARK 900 STRUCTURE OF FULL LENGTH HUMAN AMPK IN COMPLEX WITH A SMALL REMARK 900 MOLECULE ACTIVATOR, A BENZIMIDAZOLE DERIVATIVE ( 991) REMARK 900 RELATED ID: 4CFF RELATED DB: PDB REMARK 900 STRUCTURE OF FULL LENGTH HUMAN AMPK IN COMPLEX WITH A SMALL REMARK 900 MOLECULE ACTIVATOR, A THIENOPYRIDONE DERIVATIVE ( A-769662) REMARK 999 REMARK 999 SEQUENCE REMARK 999 U40819 IN PUBMED. THE 19 RESIDUES (MSHHHHHHSSGLEVLFQGP)AT REMARK 999 THE N-TERMINAL ARE EXPRESSION TAG. RESIDUES 471 TO 523 ARE REMARK 999 REMOVED TO FAVOUR CRYSTALLIZATION, THE 6 RESIDUES (LEVLFQ) REMARK 999 ARE EXPRESSION TAG AT THIS SITE. REMARK 999 M AT THE N-TERMINAL IS EXPRESSION TAG. DBREF 4CFH A 2 470 UNP P54645 AAPK1_RAT 13 481 DBREF 4CFH C 524 548 UNP P54645 AAPK1_RAT 535 559 DBREF 4CFH B 187 272 UNP O43741 AAKB2_HUMAN 187 272 DBREF 4CFH E 1 330 UNP P80385 AAKG1_RAT 1 330 SEQADV 4CFH MET A -18 UNP P54645 EXPRESSION TAG SEQADV 4CFH SER A -17 UNP P54645 EXPRESSION TAG SEQADV 4CFH HIS A -16 UNP P54645 EXPRESSION TAG SEQADV 4CFH HIS A -15 UNP P54645 EXPRESSION TAG SEQADV 4CFH HIS A -14 UNP P54645 EXPRESSION TAG SEQADV 4CFH HIS A -13 UNP P54645 EXPRESSION TAG SEQADV 4CFH HIS A -12 UNP P54645 EXPRESSION TAG SEQADV 4CFH HIS A -11 UNP P54645 EXPRESSION TAG SEQADV 4CFH SER A -10 UNP P54645 EXPRESSION TAG SEQADV 4CFH SER A -9 UNP P54645 EXPRESSION TAG SEQADV 4CFH GLY A -8 UNP P54645 EXPRESSION TAG SEQADV 4CFH LEU A -7 UNP P54645 EXPRESSION TAG SEQADV 4CFH GLU A -6 UNP P54645 EXPRESSION TAG SEQADV 4CFH VAL A -5 UNP P54645 EXPRESSION TAG SEQADV 4CFH LEU A -4 UNP P54645 EXPRESSION TAG SEQADV 4CFH PHE A -3 UNP P54645 EXPRESSION TAG SEQADV 4CFH GLN A -2 UNP P54645 EXPRESSION TAG SEQADV 4CFH GLY A -1 UNP P54645 EXPRESSION TAG SEQADV 4CFH PRO A 0 UNP P54645 EXPRESSION TAG SEQADV 4CFH MET A 1 UNP P54645 EXPRESSION TAG SEQADV 4CFH LEU A 471 UNP P54645 SEE REMARK 999 SEQADV 4CFH GLU A 472 UNP P54645 SEE REMARK 999 SEQADV 4CFH VAL A 473 UNP P54645 SEE REMARK 999 SEQADV 4CFH LEU A 474 UNP P54645 SEE REMARK 999 SEQADV 4CFH PHE C 522 UNP P54645 SEE REMARK 999 SEQADV 4CFH GLN C 523 UNP P54645 SEE REMARK 999 SEQADV 4CFH MET B 186 UNP O43741 EXPRESSION TAG SEQRES 1 A 493 MET SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU SEQRES 2 A 493 VAL LEU PHE GLN GLY PRO MET ALA GLU LYS GLN LYS HIS SEQRES 3 A 493 ASP GLY ARG VAL LYS ILE GLY HIS TYR ILE LEU GLY ASP SEQRES 4 A 493 THR LEU GLY VAL GLY THR PHE GLY LYS VAL LYS VAL GLY SEQRES 5 A 493 LYS HIS GLU LEU THR GLY HIS LYS VAL ALA VAL LYS ILE SEQRES 6 A 493 LEU ASN ARG GLN LYS ILE ARG SER LEU ASP VAL VAL GLY SEQRES 7 A 493 LYS ILE ARG ARG GLU ILE GLN ASN LEU LYS LEU PHE ARG SEQRES 8 A 493 HIS PRO HIS ILE ILE LYS LEU TYR GLN VAL ILE SER THR SEQRES 9 A 493 PRO SER ASP ILE PHE MET VAL MET GLU TYR VAL SER GLY SEQRES 10 A 493 GLY GLU LEU PHE ASP TYR ILE CYS LYS ASN GLY ARG LEU SEQRES 11 A 493 ASP GLU LYS GLU SER ARG ARG LEU PHE GLN GLN ILE LEU SEQRES 12 A 493 SER GLY VAL ASP TYR CYS HIS ARG HIS MET VAL VAL HIS SEQRES 13 A 493 ARG ASP LEU LYS PRO GLU ASN VAL LEU LEU ASP ALA HIS SEQRES 14 A 493 MET ASN ALA LYS ILE ALA ASP PHE GLY LEU SER ASN MET SEQRES 15 A 493 MET SER ASP GLY GLU PHE LEU ARG TPO SER CYS GLY SER SEQRES 16 A 493 PRO ASN TYR ALA ALA PRO GLU VAL ILE SER GLY ARG LEU SEQRES 17 A 493 TYR ALA GLY PRO GLU VAL ASP ILE TRP SER SER GLY VAL SEQRES 18 A 493 ILE LEU TYR ALA LEU LEU CYS GLY THR LEU PRO PHE ASP SEQRES 19 A 493 ASP ASP HIS VAL PRO THR LEU PHE LYS LYS ILE CYS ASP SEQRES 20 A 493 GLY ILE PHE TYR THR PRO GLN TYR LEU ASN PRO SER VAL SEQRES 21 A 493 ILE SER LEU LEU LYS HIS MET LEU GLN VAL ASP PRO MET SEQRES 22 A 493 LYS ARG ALA THR ILE LYS ASP ILE ARG GLU HIS GLU TRP SEQRES 23 A 493 PHE LYS GLN ASP LEU PRO LYS TYR LEU PHE PRO GLU ASP SEQRES 24 A 493 PRO SER TYR SER SER THR MET ILE ASP ASP GLU ALA LEU SEQRES 25 A 493 LYS GLU VAL CYS GLU LYS PHE GLU CYS SER GLU GLU GLU SEQRES 26 A 493 VAL LEU SER CYS LEU TYR ASN ARG ASN HIS GLN ASP PRO SEQRES 27 A 493 LEU ALA VAL ALA TYR HIS LEU ILE ILE ASP ASN ARG ARG SEQRES 28 A 493 ILE MET ASN GLU ALA LYS ASP PHE TYR LEU ALA THR SER SEQRES 29 A 493 PRO PRO ASP SER PHE LEU ASP ASP HIS HIS LEU THR ARG SEQRES 30 A 493 PRO HIS PRO GLU ARG VAL PRO PHE LEU VAL ALA GLU THR SEQRES 31 A 493 PRO ARG ALA ARG HIS TPO LEU ASP GLU LEU ASN PRO GLN SEQRES 32 A 493 LYS SER LYS HIS GLN GLY VAL ARG LYS ALA LYS TRP HIS SEQRES 33 A 493 LEU GLY ILE ARG SER GLN SER ARG PRO ASN ASP ILE MET SEQRES 34 A 493 ALA GLU VAL CYS ARG ALA ILE LYS GLN LEU ASP TYR GLU SEQRES 35 A 493 TRP LYS VAL VAL ASN PRO TYR TYR LEU ARG VAL ARG ARG SEQRES 36 A 493 LYS ASN PRO VAL THR SER THR PHE SER LYS MET SER LEU SEQRES 37 A 493 GLN LEU TYR GLN VAL ASP SER ARG THR TYR LEU LEU ASP SEQRES 38 A 493 PHE ARG SER ILE ASP ASP GLU ILE LEU GLU VAL LEU SEQRES 1 B 87 MET GLY PRO TYR GLY GLN GLU MET TYR ALA PHE ARG SER SEQRES 2 B 87 GLU GLU ARG PHE LYS SER PRO PRO ILE LEU PRO PRO HIS SEQRES 3 B 87 LEU LEU GLN VAL ILE LEU ASN LYS ASP THR ASN ILE SER SEQRES 4 B 87 CYS ASP PRO ALA LEU LEU PRO GLU PRO ASN HIS VAL MET SEQRES 5 B 87 LEU ASN HIS LEU TYR ALA LEU SER ILE LYS ASP SER VAL SEQRES 6 B 87 MET VAL LEU SER ALA THR HIS ARG TYR LYS LYS LYS TYR SEQRES 7 B 87 VAL THR THR LEU LEU TYR LYS PRO ILE SEQRES 1 C 27 PHE GLN VAL ALA PRO ARG PRO GLY SER HIS THR ILE GLU SEQRES 2 C 27 PHE PHE GLU MET CYS ALA ASN LEU ILE LYS ILE LEU ALA SEQRES 3 C 27 GLN SEQRES 1 E 330 MET GLU SER VAL ALA ALA GLU SER ALA PRO ALA PRO GLU SEQRES 2 E 330 ASN GLU HIS SER GLN GLU THR PRO GLU SER ASN SER SER SEQRES 3 E 330 VAL TYR THR THR PHE MET LYS SER HIS ARG CYS TYR ASP SEQRES 4 E 330 LEU ILE PRO THR SER SER LYS LEU VAL VAL PHE ASP THR SEQRES 5 E 330 SER LEU GLN VAL LYS LYS ALA PHE PHE ALA LEU VAL THR SEQRES 6 E 330 ASN GLY VAL ARG ALA ALA PRO LEU TRP ASP SER LYS LYS SEQRES 7 E 330 GLN SER PHE VAL GLY MET LEU THR ILE THR ASP PHE ILE SEQRES 8 E 330 ASN ILE LEU HIS ARG TYR TYR LYS SER ALA LEU VAL GLN SEQRES 9 E 330 ILE TYR GLU LEU GLU GLU HIS LYS ILE GLU THR TRP ARG SEQRES 10 E 330 GLU VAL TYR LEU GLN ASP SER PHE LYS PRO LEU VAL CYS SEQRES 11 E 330 ILE SER PRO ASN ALA SER LEU PHE ASP ALA VAL SER SER SEQRES 12 E 330 LEU ILE ARG ASN LYS ILE HIS ARG LEU PRO VAL ILE ASP SEQRES 13 E 330 PRO GLU SER GLY ASN THR LEU TYR ILE LEU THR HIS LYS SEQRES 14 E 330 ARG ILE LEU LYS PHE LEU LYS LEU PHE ILE THR GLU PHE SEQRES 15 E 330 PRO LYS PRO GLU PHE MET SER LYS SER LEU GLU GLU LEU SEQRES 16 E 330 GLN ILE GLY THR TYR ALA ASN ILE ALA MET VAL ARG THR SEQRES 17 E 330 THR THR PRO VAL TYR VAL ALA LEU GLY ILE PHE VAL GLN SEQRES 18 E 330 HIS ARG VAL SER ALA LEU PRO VAL VAL ASP GLU LYS GLY SEQRES 19 E 330 ARG VAL VAL ASP ILE TYR SER LYS PHE ASP VAL ILE ASN SEQRES 20 E 330 LEU ALA ALA GLU LYS THR TYR ASN ASN LEU ASP VAL SER SEQRES 21 E 330 VAL THR LYS ALA LEU GLN HIS ARG SER HIS TYR PHE GLU SEQRES 22 E 330 GLY VAL LEU LYS CYS TYR LEU HIS GLU THR LEU GLU ALA SEQRES 23 E 330 ILE ILE ASN ARG LEU VAL GLU ALA GLU VAL HIS ARG LEU SEQRES 24 E 330 VAL VAL VAL ASP GLU HIS ASP VAL VAL LYS GLY ILE VAL SEQRES 25 E 330 SER LEU SER ASP ILE LEU GLN ALA LEU VAL LEU THR GLY SEQRES 26 E 330 GLY GLU LYS LYS PRO MODRES 4CFH TPO A 172 THR PHOSPHOTHREONINE HET TPO A 172 11 HET STU A1550 35 HET AMP E1325 23 HET AMP E1326 23 HETNAM TPO PHOSPHOTHREONINE HETNAM STU STAUROSPORINE HETNAM AMP ADENOSINE MONOPHOSPHATE HETSYN TPO PHOSPHONOTHREONINE FORMUL 1 TPO C4 H10 N O6 P FORMUL 5 STU C28 H26 N4 O3 FORMUL 6 AMP 2(C10 H14 N5 O7 P) HELIX 1 1 ARG A 49 ARG A 53 1 5 HELIX 2 2 VAL A 57 LEU A 70 1 14 HELIX 3 3 ASP A 112 HIS A 133 1 22 HELIX 4 4 ALA A 181 SER A 186 1 6 HELIX 5 5 GLY A 192 GLY A 210 1 19 HELIX 6 6 HIS A 218 ASP A 228 1 11 HELIX 7 7 ASN A 238 LEU A 249 1 12 HELIX 8 8 THR A 258 GLU A 264 1 7 HELIX 9 9 HIS A 265 GLN A 270 1 6 HELIX 10 10 ALA A 323 ALA A 337 1 15 HELIX 11 11 LYS A 338 TYR A 341 5 4 HELIX 12 12 HIS A 360 ARG A 363 5 4 HELIX 13 13 VAL A 364 THR A 371 1 8 HELIX 14 14 ARG A 405 GLN A 419 1 15 HELIX 15 15 PRO B 209 GLN B 214 5 6 HELIX 16 16 ASN B 234 LEU B 238 5 5 HELIX 17 17 SER C 530 ALA C 547 1 18 HELIX 18 18 VAL E 27 HIS E 35 1 9 HELIX 19 19 CYS E 37 LEU E 40 5 4 HELIX 20 20 GLN E 55 GLY E 67 1 13 HELIX 21 21 THR E 86 TYR E 97 1 12 HELIX 22 22 ILE E 105 GLU E 110 1 6 HELIX 23 23 LYS E 112 ARG E 117 1 6 HELIX 24 24 SER E 136 LYS E 148 1 13 HELIX 25 25 THR E 167 PHE E 178 1 12 HELIX 26 26 GLU E 186 LYS E 190 5 5 HELIX 27 27 SER E 191 GLN E 196 1 6 HELIX 28 28 PRO E 211 HIS E 222 1 12 HELIX 29 29 PHE E 243 VAL E 245 5 3 HELIX 30 30 ILE E 246 GLU E 251 1 6 HELIX 31 31 SER E 260 LEU E 265 1 6 HELIX 32 32 THR E 283 ALA E 294 1 12 HELIX 33 33 LEU E 314 LEU E 323 1 10 SHEET 1 AA 6 LYS A 12 ILE A 13 0 SHEET 2 AA 6 TYR A 16 GLY A 23 -1 O TYR A 16 N ILE A 13 SHEET 3 AA 6 VAL A 30 HIS A 35 -1 O VAL A 30 N LEU A 22 SHEET 4 AA 6 LYS A 41 ASN A 48 -1 O VAL A 42 N GLY A 33 SHEET 5 AA 6 ASP A 88 GLU A 94 -1 O ILE A 89 N LEU A 47 SHEET 6 AA 6 LEU A 79 SER A 84 -1 N TYR A 80 O VAL A 92 SHEET 1 AB 2 VAL A 135 VAL A 136 0 SHEET 2 AB 2 ASN A 162 MET A 163 -1 O ASN A 162 N VAL A 136 SHEET 1 AC 2 VAL A 145 LEU A 147 0 SHEET 2 AC 2 ALA A 153 ILE A 155 -1 O LYS A 154 N LEU A 146 SHEET 1 AD 7 HIS A 397 LEU A 398 0 SHEET 2 AD 7 TYR B 242 ALA B 243 -1 O ALA B 243 N HIS A 397 SHEET 3 AD 7 MET B 251 TYR B 259 -1 O SER B 254 N TYR B 242 SHEET 4 AD 7 LYS B 262 LYS B 270 -1 O LYS B 262 N TYR B 259 SHEET 5 AD 7 SER E 44 ASP E 51 1 O SER E 45 N THR B 265 SHEET 6 AD 7 ALA E 71 ASP E 75 1 O PRO E 72 N PHE E 50 SHEET 7 AD 7 SER E 80 LEU E 85 -1 O SER E 80 N ASP E 75 SHEET 1 AE 5 ILE A 400 SER A 402 0 SHEET 2 AE 5 TYR A 459 ILE A 466 -1 O TYR A 459 N SER A 402 SHEET 3 AE 5 PHE A 444 GLN A 453 -1 O LYS A 446 N ILE A 466 SHEET 4 AE 5 TYR A 431 LYS A 437 -1 O LEU A 432 N LEU A 449 SHEET 5 AE 5 VAL A 426 ASN A 428 -1 N VAL A 427 O TYR A 431 SHEET 1 EA 2 LEU E 152 ILE E 155 0 SHEET 2 EA 2 THR E 162 LEU E 166 -1 N LEU E 163 O VAL E 154 SHEET 1 EB 3 VAL E 206 ARG E 207 0 SHEET 2 EB 3 ALA E 226 VAL E 230 1 O PRO E 228 N VAL E 206 SHEET 3 EB 3 VAL E 236 SER E 241 -1 N VAL E 237 O VAL E 229 SHEET 1 EC 3 LYS E 277 CYS E 278 0 SHEET 2 EC 3 ARG E 298 VAL E 302 1 O VAL E 300 N CYS E 278 SHEET 3 EC 3 VAL E 308 SER E 313 -1 N LYS E 309 O VAL E 301 LINK C ARG A 171 N TPO A 172 1555 1555 1.34 LINK C TPO A 172 N SER A 173 1555 1555 1.33 CISPEP 1 GLU A 279 ASP A 280 0 0.41 CISPEP 2 SER E 100 ALA E 101 0 -3.28 SITE 1 AC1 12 ARG E 69 LYS E 169 ILE E 239 SER E 241 SITE 2 AC1 12 PHE E 243 ASP E 244 ARG E 268 VAL E 275 SITE 3 AC1 12 LEU E 276 VAL E 296 HIS E 297 ARG E 298 SITE 1 AC2 12 HIS E 150 THR E 199 ILE E 203 ALA E 204 SITE 2 AC2 12 VAL E 224 SER E 225 ALA E 226 HIS E 297 SITE 3 AC2 12 ILE E 311 SER E 313 SER E 315 ASP E 316 SITE 1 AC3 16 LEU A 22 GLY A 23 VAL A 24 GLY A 25 SITE 2 AC3 16 ALA A 43 LYS A 45 MET A 93 GLU A 94 SITE 3 AC3 16 TYR A 95 VAL A 96 GLY A 99 GLU A 100 SITE 4 AC3 16 GLU A 143 ASN A 144 LEU A 146 ASP A 157 CRYST1 133.917 133.917 141.896 90.00 90.00 90.00 P 41 21 2 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.007467 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007467 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007047 0.00000 ATOM 1 N ARG A 10 -49.005 82.919 -14.973 1.00146.06 N ANISOU 1 N ARG A 10 19452 14558 21487 1555 -3082 -36 N ATOM 2 CA ARG A 10 -48.571 81.594 -14.548 1.00140.99 C ANISOU 2 CA ARG A 10 18639 14437 20493 1322 -2915 -213 C ATOM 3 C ARG A 10 -48.332 80.683 -15.747 1.00136.83 C ANISOU 3 C ARG A 10 18116 14289 19583 1266 -2935 135 C ATOM 4 O ARG A 10 -49.117 80.673 -16.695 1.00138.14 O ANISOU 4 O ARG A 10 18284 14530 19674 1530 -3117 323 O ATOM 5 CB ARG A 10 -49.609 80.963 -13.617 1.00142.01 C ANISOU 5 CB ARG A 10 18491 14852 20614 1520 -2859 -637 C ATOM 6 CG ARG A 10 -49.955 81.807 -12.400 1.00147.47 C ANISOU 6 CG ARG A 10 19185 15265 21584 1693 -2817 -1038 C ATOM 7 CD ARG A 10 -50.906 81.070 -11.468 1.00148.67 C ANISOU 7 CD ARG A 10 19016 15814 21659 1900 -2671 -1369 C ATOM 8 NE ARG A 10 -50.280 79.902 -10.853 1.00146.57 N ANISOU 8 NE ARG A 10 18621 15975 21093 1627 -2466 -1457 N ATOM 9 CZ ARG A 10 -49.668 79.915 -9.673 1.00147.60 C ANISOU 9 CZ ARG A 10 18782 16179 21122 1538 -2313 -1748 C ATOM 10 NH1 ARG A 10 -49.599 81.039 -8.972 1.00151.45 N ANISOU 10 NH1 ARG A 10 19438 16320 21784 1688 -2366 -2049 N ATOM 11 NH2 ARG A 10 -49.126 78.805 -9.191 1.00144.89 N ANISOU 11 NH2 ARG A 10 18312 16243 20497 1325 -2133 -1755 N ATOM 12 N VAL A 11 -47.244 79.919 -15.701 1.00131.68 N ANISOU 12 N VAL A 11 17469 13894 18670 962 -2768 192 N ATOM 13 CA VAL A 11 -46.937 78.960 -16.757 1.00127.26 C ANISOU 13 CA VAL A 11 16935 13719 17698 951 -2765 440 C ATOM 14 C VAL A 11 -47.277 77.536 -16.325 1.00118.25 C ANISOU 14 C VAL A 11 15583 12983 16365 921 -2718 122 C ATOM 15 O VAL A 11 -46.847 77.076 -15.269 1.00114.37 O ANISOU 15 O VAL A 11 14974 12584 15897 732 -2540 -110 O ATOM 16 CB VAL A 11 -45.457 79.037 -17.192 1.00128.83 C ANISOU 16 CB VAL A 11 17271 13948 17732 689 -2589 800 C ATOM 17 CG1 VAL A 11 -45.244 80.205 -18.146 1.00134.34 C ANISOU 17 CG1 VAL A 11 18170 14329 18545 771 -2646 1308 C ATOM 18 CG2 VAL A 11 -44.546 79.153 -15.978 1.00127.45 C ANISOU 18 CG2 VAL A 11 17015 13668 17742 363 -2424 593 C ATOM 19 N LYS A 12 -48.061 76.845 -17.145 1.00114.97 N ANISOU 19 N LYS A 12 15112 12791 15779 1116 -2905 120 N ATOM 20 CA LYS A 12 -48.477 75.485 -16.827 1.00109.14 C ANISOU 20 CA LYS A 12 14156 12345 14966 1071 -2905 -156 C ATOM 21 C LYS A 12 -47.853 74.473 -17.777 1.00104.44 C ANISOU 21 C LYS A 12 13688 12025 13970 1043 -2935 -61 C ATOM 22 O LYS A 12 -47.617 74.764 -18.949 1.00106.50 O ANISOU 22 O LYS A 12 14167 12344 13954 1197 -3056 196 O ATOM 23 CB LYS A 12 -50.003 75.357 -16.869 1.00112.26 C ANISOU 23 CB LYS A 12 14305 12755 15594 1295 -3148 -335 C ATOM 24 CG LYS A 12 -50.610 75.608 -18.243 1.00116.67 C ANISOU 24 CG LYS A 12 14968 13349 16014 1565 -3497 -168 C ATOM 25 CD LYS A 12 -51.953 74.909 -18.411 1.00118.24 C ANISOU 25 CD LYS A 12 14846 13692 16388 1702 -3791 -396 C ATOM 26 CE LYS A 12 -52.991 75.446 -17.442 1.00119.52 C ANISOU 26 CE LYS A 12 14683 13722 17007 1806 -3745 -531 C ATOM 27 NZ LYS A 12 -54.336 74.861 -17.703 1.00121.56 N ANISOU 27 NZ LYS A 12 14553 14130 17504 1937 -4051 -680 N ATOM 28 N ILE A 13 -47.584 73.282 -17.256 1.00 98.82 N ANISOU 28 N ILE A 13 12849 11489 13208 887 -2812 -258 N ATOM 29 CA ILE A 13 -47.123 72.170 -18.074 1.00 95.57 C ANISOU 29 CA ILE A 13 12549 11308 12457 911 -2863 -270 C ATOM 30 C ILE A 13 -48.209 71.105 -18.053 1.00 93.74 C ANISOU 30 C ILE A 13 12093 11118 12405 948 -3093 -574 C ATOM 31 O ILE A 13 -48.405 70.425 -17.046 1.00 92.25 O ANISOU 31 O ILE A 13 11665 10912 12474 785 -2950 -730 O ATOM 32 CB ILE A 13 -45.786 71.585 -17.565 1.00 92.05 C ANISOU 32 CB ILE A 13 12146 10983 11846 708 -2540 -218 C ATOM 33 CG1 ILE A 13 -44.626 72.535 -17.870 1.00 93.69 C ANISOU 33 CG1 ILE A 13 12539 11180 11880 654 -2358 131 C ATOM 34 CG2 ILE A 13 -45.503 70.246 -18.219 1.00 91.91 C ANISOU 34 CG2 ILE A 13 12204 11164 11555 779 -2595 -335 C ATOM 35 CD1 ILE A 13 -44.451 73.655 -16.868 1.00 94.59 C ANISOU 35 CD1 ILE A 13 12577 11045 12317 481 -2241 174 C ATOM 36 N GLY A 14 -48.928 70.979 -19.163 1.00 94.58 N ANISOU 36 N GLY A 14 12257 11284 12395 1165 -3466 -635 N ATOM 37 CA GLY A 14 -50.074 70.094 -19.218 1.00 95.39 C ANISOU 37 CA GLY A 14 12094 11378 12773 1175 -3775 -930 C ATOM 38 C GLY A 14 -51.143 70.561 -18.250 1.00 95.29 C ANISOU 38 C GLY A 14 11703 11235 13269 1127 -3747 -969 C ATOM 39 O GLY A 14 -51.792 71.581 -18.476 1.00 98.95 O ANISOU 39 O GLY A 14 12134 11641 13822 1313 -3890 -876 O ATOM 40 N HIS A 15 -51.320 69.820 -17.163 1.00 92.36 N ANISOU 40 N HIS A 15 11041 10833 13219 919 -3533 -1075 N ATOM 41 CA HIS A 15 -52.279 70.197 -16.132 1.00 92.18 C ANISOU 41 CA HIS A 15 10631 10761 13632 913 -3413 -1084 C ATOM 42 C HIS A 15 -51.559 70.553 -14.836 1.00 88.26 C ANISOU 42 C HIS A 15 10154 10272 13109 807 -2949 -1005 C ATOM 43 O HIS A 15 -52.175 70.660 -13.776 1.00 87.56 O ANISOU 43 O HIS A 15 9760 10211 13297 816 -2749 -1026 O ATOM 44 CB HIS A 15 -53.283 69.069 -15.895 1.00 94.59 C ANISOU 44 CB HIS A 15 10497 11067 14376 793 -3548 -1220 C ATOM 45 CG HIS A 15 -54.090 68.718 -17.102 1.00 99.47 C ANISOU 45 CG HIS A 15 11043 11674 15078 887 -4092 -1374 C ATOM 46 ND1 HIS A 15 -53.562 68.037 -18.183 1.00101.20 N ANISOU 46 ND1 HIS A 15 11571 11905 14974 902 -4380 -1519 N ATOM 47 CD2 HIS A 15 -55.386 68.955 -17.412 1.00103.45 C ANISOU 47 CD2 HIS A 15 11193 12187 15926 1006 -4434 -1432 C ATOM 48 CE1 HIS A 15 -54.496 67.871 -19.096 1.00105.22 C ANISOU 48 CE1 HIS A 15 11947 12430 15602 1020 -4907 -1695 C ATOM 49 NE2 HIS A 15 -55.618 68.419 -18.654 1.00106.63 N ANISOU 49 NE2 HIS A 15 11699 12607 16210 1067 -4961 -1630 N ATOM 50 N TYR A 16 -50.245 70.733 -14.935 1.00 85.90 N ANISOU 50 N TYR A 16 10197 9986 12455 731 -2788 -914 N ATOM 51 CA TYR A 16 -49.427 71.107 -13.789 1.00 82.60 C ANISOU 51 CA TYR A 16 9823 9591 11971 626 -2429 -874 C ATOM 52 C TYR A 16 -49.087 72.590 -13.802 1.00 86.55 C ANISOU 52 C TYR A 16 10536 9937 12411 715 -2423 -803 C ATOM 53 O TYR A 16 -48.223 73.030 -14.560 1.00 87.44 O ANISOU 53 O TYR A 16 10931 9994 12297 687 -2469 -645 O ATOM 54 CB TYR A 16 -48.133 70.292 -13.760 1.00 76.56 C ANISOU 54 CB TYR A 16 9222 8937 10931 455 -2256 -813 C ATOM 55 CG TYR A 16 -48.288 68.909 -13.175 1.00 73.38 C ANISOU 55 CG TYR A 16 8595 8624 10664 343 -2133 -864 C ATOM 56 CD1 TYR A 16 -48.530 68.734 -11.819 1.00 72.30 C ANISOU 56 CD1 TYR A 16 8207 8575 10688 300 -1858 -858 C ATOM 57 CD2 TYR A 16 -48.194 67.777 -13.976 1.00 71.50 C ANISOU 57 CD2 TYR A 16 8408 8368 10390 310 -2289 -911 C ATOM 58 CE1 TYR A 16 -48.671 67.472 -11.276 1.00 70.91 C ANISOU 58 CE1 TYR A 16 7813 8457 10672 201 -1714 -810 C ATOM 59 CE2 TYR A 16 -48.332 66.510 -13.441 1.00 69.90 C ANISOU 59 CE2 TYR A 16 8005 8153 10401 195 -2185 -930 C ATOM 60 CZ TYR A 16 -48.571 66.364 -12.091 1.00 69.00 C ANISOU 60 CZ TYR A 16 7618 8114 10485 127 -1882 -836 C ATOM 61 OH TYR A 16 -48.710 65.106 -11.552 1.00 67.56 O ANISOU 61 OH TYR A 16 7224 7898 10549 15 -1748 -761 O ATOM 62 N ILE A 17 -49.768 73.358 -12.959 1.00 89.70 N ANISOU 62 N ILE A 17 10789 10254 13039 838 -2354 -907 N ATOM 63 CA ILE A 17 -49.464 74.776 -12.813 1.00 93.19 C ANISOU 63 CA ILE A 17 11437 10456 13515 921 -2360 -896 C ATOM 64 C ILE A 17 -48.319 74.974 -11.818 1.00 93.94 C ANISOU 64 C ILE A 17 11640 10567 13485 743 -2128 -968 C ATOM 65 O ILE A 17 -48.359 74.463 -10.698 1.00 93.23 O ANISOU 65 O ILE A 17 11378 10674 13372 724 -1924 -1118 O ATOM 66 CB ILE A 17 -50.708 75.585 -12.384 1.00 96.12 C ANISOU 66 CB ILE A 17 11633 10703 14183 1206 -2416 -1030 C ATOM 67 CG1 ILE A 17 -51.405 74.913 -11.200 1.00 97.48 C ANISOU 67 CG1 ILE A 17 11447 11123 14469 1262 -2188 -1194 C ATOM 68 CG2 ILE A 17 -51.684 75.712 -13.543 1.00 97.47 C ANISOU 68 CG2 ILE A 17 11739 10818 14477 1401 -2728 -917 C ATOM 69 CD1 ILE A 17 -52.644 75.637 -10.722 1.00101.67 C ANISOU 69 CD1 ILE A 17 11749 11609 15271 1598 -2182 -1317 C ATOM 70 N LEU A 18 -47.290 75.703 -12.240 1.00 95.47 N ANISOU 70 N LEU A 18 12095 10576 13604 616 -2168 -831 N ATOM 71 CA LEU A 18 -46.113 75.918 -11.404 1.00 95.11 C ANISOU 71 CA LEU A 18 12122 10540 13477 408 -2024 -899 C ATOM 72 C LEU A 18 -46.328 77.049 -10.407 1.00 99.00 C ANISOU 72 C LEU A 18 12652 10794 14171 510 -2045 -1176 C ATOM 73 O LEU A 18 -46.884 78.095 -10.746 1.00102.33 O ANISOU 73 O LEU A 18 13179 10870 14834 671 -2196 -1185 O ATOM 74 CB LEU A 18 -44.884 76.206 -12.267 1.00 94.24 C ANISOU 74 CB LEU A 18 12202 10336 13269 197 -2051 -601 C ATOM 75 CG LEU A 18 -44.491 75.124 -13.272 1.00 91.55 C ANISOU 75 CG LEU A 18 11876 10260 12647 156 -2012 -362 C ATOM 76 CD1 LEU A 18 -43.199 75.502 -13.979 1.00 91.66 C ANISOU 76 CD1 LEU A 18 12033 10244 12550 -16 -1959 -31 C ATOM 77 CD2 LEU A 18 -44.361 73.774 -12.584 1.00 88.83 C ANISOU 77 CD2 LEU A 18 11361 10242 12147 102 -1853 -503 C ATOM 78 N GLY A 19 -45.876 76.837 -9.176 1.00 98.29 N ANISOU 78 N GLY A 19 12494 10889 13962 455 -1910 -1416 N ATOM 79 CA GLY A 19 -46.061 77.816 -8.124 1.00100.25 C ANISOU 79 CA GLY A 19 12801 10966 14323 606 -1947 -1779 C ATOM 80 C GLY A 19 -44.786 78.155 -7.380 1.00 99.60 C ANISOU 80 C GLY A 19 12817 10868 14160 378 -1986 -1947 C ATOM 81 O GLY A 19 -43.841 78.686 -7.963 1.00 99.82 O ANISOU 81 O GLY A 19 12969 10627 14331 108 -2117 -1777 O ATOM 82 N ASP A 20 -44.766 77.835 -6.089 1.00100.49 N ANISOU 82 N ASP A 20 12842 11301 14037 498 -1874 -2254 N ATOM 83 CA ASP A 20 -43.674 78.221 -5.200 1.00103.46 C ANISOU 83 CA ASP A 20 13295 11704 14310 346 -1980 -2523 C ATOM 84 C ASP A 20 -42.312 77.705 -5.645 1.00102.01 C ANISOU 84 C ASP A 20 13067 11638 14056 -46 -1995 -2228 C ATOM 85 O ASP A 20 -42.100 76.500 -5.768 1.00100.16 O ANISOU 85 O ASP A 20 12687 11796 13574 -93 -1802 -1979 O ATOM 86 CB ASP A 20 -43.963 77.763 -3.768 1.00106.01 C ANISOU 86 CB ASP A 20 13519 12497 14262 623 -1825 -2848 C ATOM 87 CG ASP A 20 -45.103 78.534 -3.127 1.00113.14 C ANISOU 87 CG ASP A 20 14482 13293 15214 1057 -1820 -3230 C ATOM 88 OD1 ASP A 20 -45.994 79.007 -3.865 1.00115.10 O ANISOU 88 OD1 ASP A 20 14753 13214 15765 1189 -1850 -3140 O ATOM 89 OD2 ASP A 20 -45.107 78.672 -1.885 1.00116.85 O ANISOU 89 OD2 ASP A 20 14975 14037 15386 1311 -1787 -3624 O ATOM 90 N THR A 21 -41.394 78.634 -5.889 1.00104.00 N ANISOU 90 N THR A 21 13423 11519 14575 -321 -2222 -2241 N ATOM 91 CA THR A 21 -40.012 78.292 -6.190 1.00101.92 C ANISOU 91 CA THR A 21 13057 11383 14284 -688 -2237 -1973 C ATOM 92 C THR A 21 -39.356 77.740 -4.934 1.00101.52 C ANISOU 92 C THR A 21 12881 11789 13901 -687 -2237 -2241 C ATOM 93 O THR A 21 -39.431 78.352 -3.869 1.00104.35 O ANISOU 93 O THR A 21 13310 12114 14224 -566 -2412 -2723 O ATOM 94 CB THR A 21 -39.222 79.523 -6.675 1.00104.25 C ANISOU 94 CB THR A 21 13431 11135 15044 -1009 -2486 -1893 C ATOM 95 OG1 THR A 21 -39.751 79.967 -7.932 1.00104.61 O ANISOU 95 OG1 THR A 21 13591 10812 15344 -984 -2456 -1527 O ATOM 96 CG2 THR A 21 -37.747 79.186 -6.841 1.00102.85 C ANISOU 96 CG2 THR A 21 13060 11155 14864 -1386 -2487 -1618 C ATOM 97 N LEU A 22 -38.719 76.580 -5.052 1.00 99.00 N ANISOU 97 N LEU A 22 12394 11909 13313 -775 -2053 -1945 N ATOM 98 CA LEU A 22 -38.121 75.941 -3.888 1.00101.44 C ANISOU 98 CA LEU A 22 12570 12708 13264 -723 -2035 -2121 C ATOM 99 C LEU A 22 -36.728 75.386 -4.167 1.00102.11 C ANISOU 99 C LEU A 22 12464 13031 13301 -1006 -2027 -1812 C ATOM 100 O LEU A 22 -36.095 74.814 -3.281 1.00101.93 O ANISOU 100 O LEU A 22 12303 13441 12983 -969 -2033 -1894 O ATOM 101 CB LEU A 22 -39.039 74.838 -3.348 1.00100.31 C ANISOU 101 CB LEU A 22 12373 12979 12761 -379 -1746 -2096 C ATOM 102 CG LEU A 22 -38.992 73.435 -3.961 1.00 97.13 C ANISOU 102 CG LEU A 22 11845 12838 12223 -382 -1469 -1651 C ATOM 103 CD1 LEU A 22 -39.908 72.508 -3.191 1.00 96.22 C ANISOU 103 CD1 LEU A 22 11646 13061 11854 -73 -1218 -1649 C ATOM 104 CD2 LEU A 22 -39.370 73.435 -5.426 1.00 96.16 C ANISOU 104 CD2 LEU A 22 11793 12387 12358 -475 -1435 -1366 C ATOM 105 N GLY A 23 -36.243 75.574 -5.390 1.00104.17 N ANISOU 105 N GLY A 23 12704 13048 13830 -1249 -2002 -1433 N ATOM 106 CA GLY A 23 -34.973 74.993 -5.785 1.00106.39 C ANISOU 106 CA GLY A 23 12768 13592 14063 -1462 -1924 -1077 C ATOM 107 C GLY A 23 -33.891 75.954 -6.242 1.00112.33 C ANISOU 107 C GLY A 23 13395 14070 15217 -1851 -2113 -916 C ATOM 108 O GLY A 23 -34.097 76.757 -7.150 1.00114.18 O ANISOU 108 O GLY A 23 13732 13862 15788 -1977 -2138 -724 O ATOM 109 N VAL A 24 -32.728 75.858 -5.605 1.00117.20 N ANISOU 109 N VAL A 24 13754 14960 15818 -2041 -2248 -954 N ATOM 110 CA VAL A 24 -31.546 76.603 -6.019 1.00123.45 C ANISOU 110 CA VAL A 24 14303 15563 17039 -2460 -2405 -719 C ATOM 111 C VAL A 24 -31.104 76.121 -7.398 1.00119.97 C ANISOU 111 C VAL A 24 13755 15216 16612 -2506 -2064 -70 C ATOM 112 O VAL A 24 -30.788 76.919 -8.281 1.00119.53 O ANISOU 112 O VAL A 24 13654 14813 16950 -2750 -2057 270 O ATOM 113 CB VAL A 24 -30.385 76.401 -5.016 1.00129.74 C ANISOU 113 CB VAL A 24 14774 16751 17770 -2616 -2630 -887 C ATOM 114 CG1 VAL A 24 -29.135 77.141 -5.475 1.00135.52 C ANISOU 114 CG1 VAL A 24 15161 17296 19036 -3095 -2790 -590 C ATOM 115 CG2 VAL A 24 -30.799 76.851 -3.621 1.00132.52 C ANISOU 115 CG2 VAL A 24 15264 17093 17993 -2495 -2986 -1575 C ATOM 116 N GLY A 25 -31.095 74.803 -7.565 1.00119.08 N ANISOU 116 N GLY A 25 13614 15572 16060 -2235 -1775 105 N ATOM 117 CA GLY A 25 -30.726 74.166 -8.815 1.00122.16 C ANISOU 117 CA GLY A 25 13949 16132 16335 -2158 -1442 630 C ATOM 118 C GLY A 25 -29.225 74.057 -8.963 1.00131.98 C ANISOU 118 C GLY A 25 14779 17678 17690 -2377 -1378 989 C ATOM 119 O GLY A 25 -28.474 74.591 -8.148 1.00135.95 O ANISOU 119 O GLY A 25 15016 18197 18441 -2657 -1649 836 O ATOM 120 N THR A 26 -28.782 73.354 -10.000 1.00136.85 N ANISOU 120 N THR A 26 15322 18558 18116 -2224 -1036 1447 N ATOM 121 CA THR A 26 -27.371 73.349 -10.351 1.00143.76 C ANISOU 121 CA THR A 26 15761 19726 19135 -2407 -905 1892 C ATOM 122 C THR A 26 -27.072 74.679 -11.042 1.00146.80 C ANISOU 122 C THR A 26 16035 19712 20029 -2778 -954 2231 C ATOM 123 O THR A 26 -25.922 75.113 -11.125 1.00150.70 O ANISOU 123 O THR A 26 16089 20301 20871 -3094 -952 2576 O ATOM 124 CB THR A 26 -27.005 72.152 -11.255 1.00146.03 C ANISOU 124 CB THR A 26 16026 20450 19010 -2038 -487 2258 C ATOM 125 OG1 THR A 26 -25.589 71.937 -11.221 1.00149.65 O ANISOU 125 OG1 THR A 26 15986 21318 19555 -2145 -369 2605 O ATOM 126 CG2 THR A 26 -27.454 72.391 -12.692 1.00147.54 C ANISOU 126 CG2 THR A 26 16461 20481 19116 -1894 -241 2600 C ATOM 127 N PHE A 27 -28.141 75.315 -11.519 1.00144.82 N ANISOU 127 N PHE A 27 16163 19003 19859 -2734 -1001 2158 N ATOM 128 CA PHE A 27 -28.113 76.664 -12.071 1.00148.33 C ANISOU 128 CA PHE A 27 16594 18934 20830 -3055 -1089 2440 C ATOM 129 C PHE A 27 -29.556 77.097 -12.326 1.00142.61 C ANISOU 129 C PHE A 27 16357 17766 20062 -2860 -1186 2195 C ATOM 130 O PHE A 27 -29.891 78.278 -12.232 1.00144.61 O ANISOU 130 O PHE A 27 16704 17453 20786 -3089 -1420 2126 O ATOM 131 CB PHE A 27 -27.314 76.717 -13.379 1.00155.63 C ANISOU 131 CB PHE A 27 17295 20052 21783 -3076 -702 3220 C ATOM 132 CG PHE A 27 -28.168 76.643 -14.614 1.00158.82 C ANISOU 132 CG PHE A 27 18086 20396 21863 -2725 -454 3492 C ATOM 133 CD1 PHE A 27 -28.588 75.420 -15.109 1.00156.77 C ANISOU 133 CD1 PHE A 27 18055 20556 20954 -2236 -222 3419 C ATOM 134 CD2 PHE A 27 -28.558 77.797 -15.274 1.00163.74 C ANISOU 134 CD2 PHE A 27 18849 20522 22844 -2868 -489 3806 C ATOM 135 CE1 PHE A 27 -29.380 75.351 -16.237 1.00156.76 C ANISOU 135 CE1 PHE A 27 18408 20525 20627 -1899 -71 3604 C ATOM 136 CE2 PHE A 27 -29.349 77.732 -16.399 1.00163.63 C ANISOU 136 CE2 PHE A 27 19186 20507 22477 -2503 -302 4056 C ATOM 137 CZ PHE A 27 -29.760 76.510 -16.882 1.00159.67 C ANISOU 137 CZ PHE A 27 18905 20474 21290 -2019 -112 3930 C ATOM 138 N GLY A 28 -30.404 76.121 -12.645 1.00136.01 N ANISOU 138 N GLY A 28 15808 17170 18700 -2430 -1024 2059 N ATOM 139 CA GLY A 28 -31.773 76.383 -13.049 1.00129.92 C ANISOU 139 CA GLY A 28 15438 16075 17850 -2198 -1088 1895 C ATOM 140 C GLY A 28 -32.785 76.129 -11.950 1.00123.47 C ANISOU 140 C GLY A 28 14804 15174 16937 -2054 -1306 1253 C ATOM 141 O GLY A 28 -32.711 75.122 -11.245 1.00121.23 O ANISOU 141 O GLY A 28 14450 15257 16354 -1921 -1264 1007 O ATOM 142 N LYS A 29 -33.739 77.048 -11.822 1.00117.63 N ANISOU 142 N LYS A 29 14287 13956 16452 -2048 -1512 1028 N ATOM 143 CA LYS A 29 -34.733 77.010 -10.753 1.00108.96 C ANISOU 143 CA LYS A 29 13335 12763 15301 -1891 -1697 443 C ATOM 144 C LYS A 29 -35.542 75.717 -10.731 1.00 98.05 C ANISOU 144 C LYS A 29 12048 11741 13466 -1541 -1538 301 C ATOM 145 O LYS A 29 -35.840 75.135 -11.773 1.00 94.12 O ANISOU 145 O LYS A 29 11644 11361 12755 -1358 -1377 563 O ATOM 146 CB LYS A 29 -35.686 78.205 -10.871 1.00109.74 C ANISOU 146 CB LYS A 29 13665 12285 15746 -1858 -1894 300 C ATOM 147 CG LYS A 29 -35.014 79.566 -10.795 1.00114.53 C ANISOU 147 CG LYS A 29 14209 12382 16927 -2219 -2105 385 C ATOM 148 CD LYS A 29 -36.039 80.691 -10.887 1.00117.96 C ANISOU 148 CD LYS A 29 14908 12201 17710 -2112 -2298 221 C ATOM 149 CE LYS A 29 -35.384 82.062 -10.784 1.00124.98 C ANISOU 149 CE LYS A 29 15752 12463 19273 -2489 -2542 287 C ATOM 150 NZ LYS A 29 -34.455 82.335 -11.918 1.00128.38 N ANISOU 150 NZ LYS A 29 16012 12825 19941 -2766 -2365 1044 N ATOM 151 N VAL A 30 -35.887 75.272 -9.528 1.00 92.01 N ANISOU 151 N VAL A 30 11251 11146 12561 -1442 -1597 -112 N ATOM 152 CA VAL A 30 -36.807 74.158 -9.354 1.00 86.02 C ANISOU 152 CA VAL A 30 10554 10629 11501 -1144 -1464 -245 C ATOM 153 C VAL A 30 -38.056 74.657 -8.644 1.00 82.28 C ANISOU 153 C VAL A 30 10195 9945 11121 -978 -1586 -629 C ATOM 154 O VAL A 30 -37.973 75.257 -7.574 1.00 82.66 O ANISOU 154 O VAL A 30 10224 9944 11239 -1014 -1728 -957 O ATOM 155 CB VAL A 30 -36.180 73.012 -8.538 1.00 86.09 C ANISOU 155 CB VAL A 30 10386 11096 11226 -1102 -1339 -286 C ATOM 156 CG1 VAL A 30 -37.232 71.973 -8.179 1.00 83.01 C ANISOU 156 CG1 VAL A 30 10039 10860 10642 -829 -1215 -417 C ATOM 157 CG2 VAL A 30 -35.032 72.377 -9.306 1.00 87.46 C ANISOU 157 CG2 VAL A 30 10434 11514 11283 -1175 -1177 98 C ATOM 158 N LYS A 31 -39.212 74.423 -9.256 1.00 79.15 N ANISOU 158 N LYS A 31 9908 9449 10719 -769 -1547 -604 N ATOM 159 CA LYS A 31 -40.479 74.845 -8.678 1.00 78.21 C ANISOU 159 CA LYS A 31 9844 9171 10701 -563 -1621 -914 C ATOM 160 C LYS A 31 -41.356 73.643 -8.352 1.00 75.43 C ANISOU 160 C LYS A 31 9388 9104 10168 -350 -1460 -964 C ATOM 161 O LYS A 31 -41.069 72.519 -8.766 1.00 73.29 O ANISOU 161 O LYS A 31 9057 9051 9739 -362 -1334 -766 O ATOM 162 CB LYS A 31 -41.223 75.775 -9.636 1.00 79.92 C ANISOU 162 CB LYS A 31 10217 8977 11173 -492 -1754 -823 C ATOM 163 CG LYS A 31 -40.496 77.069 -9.961 1.00 83.91 C ANISOU 163 CG LYS A 31 10823 9090 11971 -705 -1908 -716 C ATOM 164 CD LYS A 31 -41.339 77.929 -10.887 1.00 87.68 C ANISOU 164 CD LYS A 31 11462 9165 12685 -568 -2023 -572 C ATOM 165 CE LYS A 31 -40.565 79.119 -11.425 1.00 92.68 C ANISOU 165 CE LYS A 31 12186 9368 13658 -802 -2134 -306 C ATOM 166 NZ LYS A 31 -41.344 79.821 -12.486 1.00 95.36 N ANISOU 166 NZ LYS A 31 12692 9371 14171 -624 -2213 -40 N ATOM 167 N VAL A 32 -42.427 73.886 -7.605 1.00 75.42 N ANISOU 167 N VAL A 32 9351 9082 10225 -144 -1456 -1218 N ATOM 168 CA VAL A 32 -43.400 72.847 -7.313 1.00 72.64 C ANISOU 168 CA VAL A 32 8839 8951 9810 38 -1291 -1202 C ATOM 169 C VAL A 32 -44.499 72.880 -8.361 1.00 73.40 C ANISOU 169 C VAL A 32 8941 8832 10115 139 -1385 -1117 C ATOM 170 O VAL A 32 -45.014 73.945 -8.695 1.00 75.79 O ANISOU 170 O VAL A 32 9340 8853 10602 225 -1537 -1200 O ATOM 171 CB VAL A 32 -44.039 73.033 -5.927 1.00 72.82 C ANISOU 171 CB VAL A 32 8756 9155 9758 258 -1181 -1466 C ATOM 172 CG1 VAL A 32 -45.021 71.908 -5.640 1.00 71.51 C ANISOU 172 CG1 VAL A 32 8353 9221 9594 409 -962 -1336 C ATOM 173 CG2 VAL A 32 -42.973 73.089 -4.856 1.00 73.15 C ANISOU 173 CG2 VAL A 32 8810 9447 9535 204 -1158 -1605 C ATOM 174 N GLY A 33 -44.845 71.713 -8.887 1.00 73.19 N ANISOU 174 N GLY A 33 8811 8918 10080 139 -1330 -961 N ATOM 175 CA GLY A 33 -45.947 71.601 -9.819 1.00 75.60 C ANISOU 175 CA GLY A 33 9074 9072 10577 241 -1476 -924 C ATOM 176 C GLY A 33 -47.187 71.116 -9.100 1.00 77.91 C ANISOU 176 C GLY A 33 9076 9472 11053 383 -1369 -996 C ATOM 177 O GLY A 33 -47.109 70.230 -8.252 1.00 77.39 O ANISOU 177 O GLY A 33 8841 9629 10933 363 -1150 -947 O ATOM 178 N LYS A 34 -48.330 71.704 -9.431 1.00 81.47 N ANISOU 178 N LYS A 34 9438 9780 11737 545 -1507 -1062 N ATOM 179 CA LYS A 34 -49.599 71.321 -8.822 1.00 84.22 C ANISOU 179 CA LYS A 34 9431 10247 12321 694 -1394 -1082 C ATOM 180 C LYS A 34 -50.606 70.944 -9.898 1.00 84.75 C ANISOU 180 C LYS A 34 9339 10194 12670 710 -1647 -1025 C ATOM 181 O LYS A 34 -50.926 71.754 -10.767 1.00 87.21 O ANISOU 181 O LYS A 34 9777 10323 13037 813 -1906 -1059 O ATOM 182 CB LYS A 34 -50.151 72.468 -7.979 1.00 87.97 C ANISOU 182 CB LYS A 34 9866 10722 12836 953 -1309 -1263 C ATOM 183 CG LYS A 34 -51.496 72.183 -7.331 1.00 90.97 C ANISOU 183 CG LYS A 34 9829 11285 13448 1167 -1134 -1242 C ATOM 184 CD LYS A 34 -51.341 71.909 -5.845 1.00 92.04 C ANISOU 184 CD LYS A 34 9838 11765 13370 1285 -757 -1261 C ATOM 185 CE LYS A 34 -52.680 71.984 -5.129 1.00 95.70 C ANISOU 185 CE LYS A 34 9896 12442 14024 1596 -526 -1234 C ATOM 186 NZ LYS A 34 -53.348 73.297 -5.346 1.00 98.43 N ANISOU 186 NZ LYS A 34 10305 12598 14497 1893 -681 -1464 N ATOM 187 N HIS A 35 -51.103 69.714 -9.841 1.00 83.70 N ANISOU 187 N HIS A 35 8918 10145 12737 610 -1599 -930 N ATOM 188 CA HIS A 35 -52.068 69.247 -10.826 1.00 85.65 C ANISOU 188 CA HIS A 35 8970 10274 13297 593 -1908 -930 C ATOM 189 C HIS A 35 -53.390 69.996 -10.678 1.00 87.58 C ANISOU 189 C HIS A 35 8906 10529 13842 817 -1972 -964 C ATOM 190 O HIS A 35 -54.071 69.875 -9.662 1.00 87.86 O ANISOU 190 O HIS A 35 8579 10729 14076 904 -1694 -899 O ATOM 191 CB HIS A 35 -52.288 67.740 -10.694 1.00 88.06 C ANISOU 191 CB HIS A 35 9008 10592 13858 396 -1855 -832 C ATOM 192 CG HIS A 35 -52.848 67.105 -11.927 1.00 91.28 C ANISOU 192 CG HIS A 35 9352 10822 14507 313 -2285 -921 C ATOM 193 ND1 HIS A 35 -54.202 66.992 -12.159 1.00 95.76 N ANISOU 193 ND1 HIS A 35 9495 11347 15540 336 -2504 -938 N ATOM 194 CD2 HIS A 35 -52.235 66.556 -13.002 1.00 91.38 C ANISOU 194 CD2 HIS A 35 9666 10714 14340 239 -2564 -1030 C ATOM 195 CE1 HIS A 35 -54.399 66.396 -13.321 1.00 97.78 C ANISOU 195 CE1 HIS A 35 9805 11447 15900 256 -2951 -1087 C ATOM 196 NE2 HIS A 35 -53.222 66.121 -13.853 1.00 95.70 N ANISOU 196 NE2 HIS A 35 10005 11139 15217 221 -2984 -1159 N ATOM 197 N GLU A 36 -53.747 70.767 -11.701 1.00 89.89 N ANISOU 197 N GLU A 36 9328 10676 14148 950 -2318 -1030 N ATOM 198 CA GLU A 36 -54.931 71.622 -11.648 1.00 95.96 C ANISOU 198 CA GLU A 36 9837 11439 15185 1224 -2407 -1058 C ATOM 199 C GLU A 36 -56.225 70.842 -11.417 1.00 99.01 C ANISOU 199 C GLU A 36 9617 11951 16050 1210 -2418 -991 C ATOM 200 O GLU A 36 -57.227 71.408 -10.981 1.00103.56 O ANISOU 200 O GLU A 36 9850 12618 16880 1456 -2340 -974 O ATOM 201 CB GLU A 36 -55.046 72.463 -12.924 1.00 99.30 C ANISOU 201 CB GLU A 36 10514 11685 15528 1376 -2818 -1078 C ATOM 202 CG GLU A 36 -55.267 71.648 -14.192 1.00101.58 C ANISOU 202 CG GLU A 36 10790 11964 15842 1268 -3238 -1086 C ATOM 203 CD GLU A 36 -55.477 72.516 -15.422 1.00104.37 C ANISOU 203 CD GLU A 36 11377 12226 16054 1500 -3636 -1057 C ATOM 204 OE1 GLU A 36 -55.192 73.731 -15.351 1.00105.11 O ANISOU 204 OE1 GLU A 36 11720 12190 16025 1684 -3553 -981 O ATOM 205 OE2 GLU A 36 -55.928 71.984 -16.459 1.00105.95 O ANISOU 205 OE2 GLU A 36 11516 12471 16271 1511 -4052 -1110 O ATOM 206 N LEU A 37 -56.196 69.544 -11.701 1.00 96.19 N ANISOU 206 N LEU A 37 9109 11580 15860 929 -2513 -946 N ATOM 207 CA LEU A 37 -57.379 68.703 -11.564 1.00 96.67 C ANISOU 207 CA LEU A 37 8553 11691 16487 828 -2570 -850 C ATOM 208 C LEU A 37 -57.441 67.979 -10.224 1.00 95.91 C ANISOU 208 C LEU A 37 8116 11759 16567 723 -2053 -628 C ATOM 209 O LEU A 37 -58.528 67.729 -9.701 1.00 98.70 O ANISOU 209 O LEU A 37 7878 12243 17381 754 -1905 -454 O ATOM 210 CB LEU A 37 -57.431 67.676 -12.695 1.00 96.15 C ANISOU 210 CB LEU A 37 8489 11440 16604 579 -3044 -956 C ATOM 211 CG LEU A 37 -58.308 67.983 -13.909 1.00 98.79 C ANISOU 211 CG LEU A 37 8700 11718 17118 693 -3635 -1106 C ATOM 212 CD1 LEU A 37 -58.073 69.393 -14.417 1.00 97.84 C ANISOU 212 CD1 LEU A 37 8973 11623 16577 1024 -3746 -1153 C ATOM 213 CD2 LEU A 37 -58.038 66.970 -15.006 1.00 99.07 C ANISOU 213 CD2 LEU A 37 8910 11582 17150 485 -4109 -1308 C ATOM 214 N THR A 38 -56.278 67.631 -9.676 1.00 92.57 N ANISOU 214 N THR A 38 8034 11362 15776 617 -1768 -588 N ATOM 215 CA THR A 38 -56.220 66.788 -8.480 1.00 92.56 C ANISOU 215 CA THR A 38 7755 11528 15885 520 -1297 -322 C ATOM 216 C THR A 38 -55.240 67.269 -7.413 1.00 89.12 C ANISOU 216 C THR A 38 7638 11318 14904 677 -882 -310 C ATOM 217 O THR A 38 -55.084 66.628 -6.374 1.00 89.15 O ANISOU 217 O THR A 38 7468 11526 14879 658 -475 -68 O ATOM 218 CB THR A 38 -55.839 65.345 -8.835 1.00 91.54 C ANISOU 218 CB THR A 38 7610 11181 15989 172 -1404 -226 C ATOM 219 OG1 THR A 38 -54.517 65.324 -9.390 1.00 87.43 O ANISOU 219 OG1 THR A 38 7683 10543 14993 114 -1542 -401 O ATOM 220 CG2 THR A 38 -56.823 64.762 -9.832 1.00 94.22 C ANISOU 220 CG2 THR A 38 7610 11275 16916 -9 -1875 -297 C ATOM 221 N GLY A 39 -54.568 68.382 -7.676 1.00 87.50 N ANISOU 221 N GLY A 39 7890 11072 14283 827 -1007 -555 N ATOM 222 CA GLY A 39 -53.651 68.952 -6.706 1.00 86.96 C ANISOU 222 CA GLY A 39 8116 11188 13734 966 -714 -624 C ATOM 223 C GLY A 39 -52.417 68.114 -6.434 1.00 85.27 C ANISOU 223 C GLY A 39 8136 11018 13246 756 -586 -527 C ATOM 224 O GLY A 39 -51.687 68.377 -5.477 1.00 86.39 O ANISOU 224 O GLY A 39 8436 11382 13008 860 -337 -550 O ATOM 225 N HIS A 40 -52.182 67.106 -7.269 1.00 82.94 N ANISOU 225 N HIS A 40 7863 10519 13132 496 -783 -446 N ATOM 226 CA HIS A 40 -51.002 66.261 -7.130 1.00 80.75 C ANISOU 226 CA HIS A 40 7804 10250 12625 334 -681 -349 C ATOM 227 C HIS A 40 -49.737 67.096 -7.277 1.00 78.01 C ANISOU 227 C HIS A 40 7917 9929 11795 364 -752 -526 C ATOM 228 O HIS A 40 -49.611 67.886 -8.210 1.00 76.81 O ANISOU 228 O HIS A 40 7998 9604 11582 373 -1035 -693 O ATOM 229 CB HIS A 40 -51.019 65.143 -8.172 1.00 81.21 C ANISOU 229 CB HIS A 40 7858 10020 12977 107 -948 -324 C ATOM 230 CG HIS A 40 -49.857 64.201 -8.069 1.00 78.88 C ANISOU 230 CG HIS A 40 7773 9705 12494 -8 -837 -221 C ATOM 231 ND1 HIS A 40 -48.795 64.230 -8.947 1.00 74.62 N ANISOU 231 ND1 HIS A 40 7633 9068 11650 -43 -1035 -368 N ATOM 232 CD2 HIS A 40 -49.597 63.198 -7.197 1.00 78.80 C ANISOU 232 CD2 HIS A 40 7609 9773 12559 -60 -529 55 C ATOM 233 CE1 HIS A 40 -47.930 63.287 -8.619 1.00 72.90 C ANISOU 233 CE1 HIS A 40 7492 8868 11339 -101 -865 -224 C ATOM 234 NE2 HIS A 40 -48.392 62.647 -7.560 1.00 75.10 N ANISOU 234 NE2 HIS A 40 7453 9233 11849 -114 -571 37 N ATOM 235 N LYS A 41 -48.804 66.925 -6.348 1.00 78.90 N ANISOU 235 N LYS A 41 8128 10267 11585 380 -499 -452 N ATOM 236 CA LYS A 41 -47.588 67.728 -6.353 1.00 80.20 C ANISOU 236 CA LYS A 41 8643 10470 11358 375 -571 -607 C ATOM 237 C LYS A 41 -46.392 67.021 -6.983 1.00 78.78 C ANISOU 237 C LYS A 41 8671 10232 11029 203 -642 -523 C ATOM 238 O LYS A 41 -46.057 65.889 -6.629 1.00 79.63 O ANISOU 238 O LYS A 41 8690 10427 11140 156 -478 -333 O ATOM 239 CB LYS A 41 -47.240 68.209 -4.940 1.00 83.44 C ANISOU 239 CB LYS A 41 9044 11204 11455 540 -330 -664 C ATOM 240 CG LYS A 41 -47.761 69.601 -4.613 1.00 87.13 C ANISOU 240 CG LYS A 41 9567 11652 11887 744 -395 -941 C ATOM 241 CD LYS A 41 -49.012 69.549 -3.754 1.00 92.27 C ANISOU 241 CD LYS A 41 9890 12520 12648 1007 -138 -891 C ATOM 242 CE LYS A 41 -48.681 69.104 -2.341 1.00 95.92 C ANISOU 242 CE LYS A 41 10259 13430 12756 1173 204 -786 C ATOM 243 NZ LYS A 41 -47.719 70.034 -1.679 1.00 97.35 N ANISOU 243 NZ LYS A 41 10741 13744 12506 1281 115 -1112 N ATOM 244 N VAL A 42 -45.754 67.707 -7.924 1.00 76.26 N ANISOU 244 N VAL A 42 8620 9767 10590 140 -865 -629 N ATOM 245 CA VAL A 42 -44.520 67.227 -8.527 1.00 72.35 C ANISOU 245 CA VAL A 42 8316 9278 9895 33 -895 -545 C ATOM 246 C VAL A 42 -43.438 68.295 -8.405 1.00 72.97 C ANISOU 246 C VAL A 42 8573 9422 9731 -17 -927 -598 C ATOM 247 O VAL A 42 -43.730 69.458 -8.124 1.00 75.46 O ANISOU 247 O VAL A 42 8926 9664 10082 19 -1003 -743 O ATOM 248 CB VAL A 42 -44.716 66.871 -10.010 1.00 67.43 C ANISOU 248 CB VAL A 42 7822 8439 9358 13 -1129 -557 C ATOM 249 CG1 VAL A 42 -45.667 65.699 -10.149 1.00 67.14 C ANISOU 249 CG1 VAL A 42 7593 8282 9634 10 -1166 -544 C ATOM 250 CG2 VAL A 42 -45.225 68.077 -10.783 1.00 66.05 C ANISOU 250 CG2 VAL A 42 7764 8110 9223 66 -1357 -655 C ATOM 251 N ALA A 43 -42.189 67.894 -8.612 1.00 70.82 N ANISOU 251 N ALA A 43 8386 9264 9260 -98 -877 -480 N ATOM 252 CA ALA A 43 -41.077 68.830 -8.595 1.00 70.19 C ANISOU 252 CA ALA A 43 8407 9231 9031 -204 -926 -480 C ATOM 253 C ALA A 43 -40.531 69.021 -10.005 1.00 72.82 C ANISOU 253 C ALA A 43 8902 9444 9324 -257 -1023 -341 C ATOM 254 O ALA A 43 -40.144 68.058 -10.667 1.00 73.75 O ANISOU 254 O ALA A 43 9056 9633 9333 -208 -966 -222 O ATOM 255 CB ALA A 43 -39.996 68.338 -7.672 1.00 67.41 C ANISOU 255 CB ALA A 43 7956 9180 8476 -237 -783 -408 C ATOM 256 N VAL A 44 -40.502 70.269 -10.460 1.00 73.40 N ANISOU 256 N VAL A 44 9080 9331 9476 -321 -1158 -344 N ATOM 257 CA VAL A 44 -40.096 70.570 -11.826 1.00 73.17 C ANISOU 257 CA VAL A 44 9202 9217 9382 -327 -1219 -138 C ATOM 258 C VAL A 44 -38.792 71.359 -11.881 1.00 73.62 C ANISOU 258 C VAL A 44 9246 9305 9422 -513 -1179 54 C ATOM 259 O VAL A 44 -38.702 72.466 -11.351 1.00 74.56 O ANISOU 259 O VAL A 44 9349 9243 9736 -650 -1276 -22 O ATOM 260 CB VAL A 44 -41.193 71.354 -12.571 1.00 74.53 C ANISOU 260 CB VAL A 44 9496 9119 9702 -226 -1409 -174 C ATOM 261 CG1 VAL A 44 -40.785 71.605 -14.015 1.00 75.67 C ANISOU 261 CG1 VAL A 44 9813 9247 9691 -170 -1452 95 C ATOM 262 CG2 VAL A 44 -42.510 70.601 -12.511 1.00 74.13 C ANISOU 262 CG2 VAL A 44 9375 9045 9745 -75 -1481 -356 C ATOM 263 N LYS A 45 -37.787 70.776 -12.527 1.00 73.56 N ANISOU 263 N LYS A 45 9226 9512 9213 -510 -1043 297 N ATOM 264 CA LYS A 45 -36.514 71.449 -12.758 1.00 74.35 C ANISOU 264 CA LYS A 45 9241 9676 9335 -695 -974 574 C ATOM 265 C LYS A 45 -36.564 72.174 -14.100 1.00 75.76 C ANISOU 265 C LYS A 45 9570 9710 9506 -652 -988 872 C ATOM 266 O LYS A 45 -36.723 71.548 -15.149 1.00 72.69 O ANISOU 266 O LYS A 45 9315 9457 8845 -420 -925 991 O ATOM 267 CB LYS A 45 -35.370 70.437 -12.747 1.00 74.08 C ANISOU 267 CB LYS A 45 9062 10010 9075 -659 -771 735 C ATOM 268 CG LYS A 45 -33.980 71.043 -12.707 1.00 75.73 C ANISOU 268 CG LYS A 45 9054 10350 9368 -886 -693 1021 C ATOM 269 CD LYS A 45 -32.930 69.948 -12.694 1.00 75.75 C ANISOU 269 CD LYS A 45 8887 10758 9138 -776 -480 1177 C ATOM 270 CE LYS A 45 -31.624 70.438 -12.106 1.00 80.68 C ANISOU 270 CE LYS A 45 9176 11558 9921 -1043 -467 1353 C ATOM 271 NZ LYS A 45 -30.640 69.330 -11.970 1.00 83.20 N ANISOU 271 NZ LYS A 45 9293 12300 10020 -888 -269 1495 N ATOM 272 N ILE A 46 -36.429 73.495 -14.058 1.00 80.84 N ANISOU 272 N ILE A 46 10203 10068 10443 -852 -1085 991 N ATOM 273 CA ILE A 46 -36.609 74.326 -15.245 1.00 84.16 C ANISOU 273 CA ILE A 46 10775 10300 10904 -798 -1102 1333 C ATOM 274 C ILE A 46 -35.285 74.761 -15.852 1.00 90.96 C ANISOU 274 C ILE A 46 11496 11274 11791 -965 -910 1845 C ATOM 275 O ILE A 46 -34.444 75.354 -15.177 1.00 94.55 O ANISOU 275 O ILE A 46 11732 11629 12564 -1288 -923 1907 O ATOM 276 CB ILE A 46 -37.439 75.574 -14.927 1.00 82.13 C ANISOU 276 CB ILE A 46 10613 9561 11030 -875 -1327 1201 C ATOM 277 CG1 ILE A 46 -38.736 75.172 -14.225 1.00 78.74 C ANISOU 277 CG1 ILE A 46 10245 9073 10600 -698 -1473 722 C ATOM 278 CG2 ILE A 46 -37.719 76.355 -16.199 1.00 84.83 C ANISOU 278 CG2 ILE A 46 11129 9713 11391 -759 -1344 1610 C ATOM 279 CD1 ILE A 46 -39.468 76.324 -13.598 1.00 80.92 C ANISOU 279 CD1 ILE A 46 10575 8921 11249 -733 -1669 494 C ATOM 280 N LEU A 47 -35.110 74.462 -17.134 1.00 94.15 N ANISOU 280 N LEU A 47 12007 11911 11856 -728 -740 2212 N ATOM 281 CA LEU A 47 -33.876 74.775 -17.840 1.00 97.54 C ANISOU 281 CA LEU A 47 12271 12541 12248 -815 -473 2792 C ATOM 282 C LEU A 47 -34.200 75.450 -19.165 1.00101.38 C ANISOU 282 C LEU A 47 12959 12964 12598 -617 -413 3257 C ATOM 283 O LEU A 47 -34.462 74.776 -20.160 1.00101.34 O ANISOU 283 O LEU A 47 13151 13284 12070 -219 -321 3334 O ATOM 284 CB LEU A 47 -33.083 73.494 -18.104 1.00 95.25 C ANISOU 284 CB LEU A 47 11883 12788 11520 -603 -216 2837 C ATOM 285 CG LEU A 47 -33.021 72.476 -16.964 1.00 89.92 C ANISOU 285 CG LEU A 47 11097 12239 10829 -632 -275 2366 C ATOM 286 CD1 LEU A 47 -32.439 71.166 -17.453 1.00 89.39 C ANISOU 286 CD1 LEU A 47 11023 12631 10311 -310 -37 2409 C ATOM 287 CD2 LEU A 47 -32.214 73.024 -15.799 1.00 91.62 C ANISOU 287 CD2 LEU A 47 10985 12366 11459 -1043 -332 2346 C ATOM 288 N ASN A 48 -34.194 76.779 -19.180 1.00105.80 N ANISOU 288 N ASN A 48 13486 13092 13621 -867 -486 3558 N ATOM 289 CA ASN A 48 -34.464 77.507 -20.414 1.00112.30 C ANISOU 289 CA ASN A 48 14490 13840 14340 -671 -411 4105 C ATOM 290 C ASN A 48 -33.285 77.410 -21.371 1.00117.66 C ANISOU 290 C ASN A 48 15005 14952 14746 -599 0 4804 C ATOM 291 O ASN A 48 -32.130 77.391 -20.947 1.00119.38 O ANISOU 291 O ASN A 48 14872 15292 15195 -899 190 5005 O ATOM 292 CB ASN A 48 -34.831 78.970 -20.139 1.00116.96 C ANISOU 292 CB ASN A 48 15104 13761 15576 -942 -608 4255 C ATOM 293 CG ASN A 48 -33.663 79.780 -19.610 1.00122.77 C ANISOU 293 CG ASN A 48 15499 14224 16923 -1456 -525 4573 C ATOM 294 OD1 ASN A 48 -32.811 79.264 -18.886 1.00123.47 O ANISOU 294 OD1 ASN A 48 15309 14535 17070 -1687 -463 4393 O ATOM 295 ND2 ASN A 48 -33.619 81.058 -19.969 1.00127.00 N ANISOU 295 ND2 ASN A 48 16040 14253 17961 -1641 -550 5059 N ATOM 296 N ARG A 49 -33.585 77.341 -22.663 1.00120.79 N ANISOU 296 N ARG A 49 15639 15631 14625 -167 134 5180 N ATOM 297 CA ARG A 49 -32.556 77.165 -23.679 1.00125.14 C ANISOU 297 CA ARG A 49 16070 16708 14772 34 579 5859 C ATOM 298 C ARG A 49 -31.670 78.400 -23.815 1.00131.62 C ANISOU 298 C ARG A 49 16580 17272 16155 -357 813 6665 C ATOM 299 O ARG A 49 -30.542 78.312 -24.299 1.00135.29 O ANISOU 299 O ARG A 49 16760 18145 16500 -358 1232 7261 O ATOM 300 CB ARG A 49 -33.194 76.814 -25.023 1.00126.70 C ANISOU 300 CB ARG A 49 16646 17299 14194 662 620 6012 C ATOM 301 CG ARG A 49 -34.065 75.572 -24.973 1.00120.73 C ANISOU 301 CG ARG A 49 16172 16750 12951 1023 343 5215 C ATOM 302 CD ARG A 49 -34.721 75.297 -26.314 1.00124.38 C ANISOU 302 CD ARG A 49 17014 17585 12660 1642 287 5305 C ATOM 303 NE ARG A 49 -35.559 74.105 -26.265 1.00121.59 N ANISOU 303 NE ARG A 49 16897 17357 11944 1934 -39 4509 N ATOM 304 CZ ARG A 49 -35.102 72.868 -26.428 1.00122.94 C ANISOU 304 CZ ARG A 49 17107 17943 11661 2201 80 4196 C ATOM 305 NH1 ARG A 49 -33.813 72.662 -26.658 1.00126.85 N ANISOU 305 NH1 ARG A 49 17409 18836 11953 2258 543 4617 N ATOM 306 NH2 ARG A 49 -35.934 71.838 -26.367 1.00120.58 N ANISOU 306 NH2 ARG A 49 17018 17641 11157 2415 -266 3475 N ATOM 307 N GLN A 50 -32.184 79.546 -23.381 1.00132.99 N ANISOU 307 N GLN A 50 16790 16751 16989 -682 546 6687 N ATOM 308 CA GLN A 50 -31.431 80.795 -23.433 1.00140.06 C ANISOU 308 CA GLN A 50 17397 17233 18587 -1121 692 7415 C ATOM 309 C GLN A 50 -30.174 80.753 -22.568 1.00140.91 C ANISOU 309 C GLN A 50 16994 17344 19200 -1645 792 7429 C ATOM 310 O GLN A 50 -29.162 81.370 -22.902 1.00147.46 O ANISOU 310 O GLN A 50 17451 18156 20419 -1935 1081 8191 O ATOM 311 CB GLN A 50 -32.313 81.971 -23.006 1.00140.98 C ANISOU 311 CB GLN A 50 17697 16507 19361 -1340 310 7275 C ATOM 312 CG GLN A 50 -33.330 82.412 -24.050 1.00143.01 C ANISOU 312 CG GLN A 50 18351 16692 19294 -881 266 7603 C ATOM 313 CD GLN A 50 -32.713 83.259 -25.148 1.00150.22 C ANISOU 313 CD GLN A 50 19166 17611 20300 -860 641 8734 C ATOM 314 OE1 GLN A 50 -31.508 83.510 -25.152 1.00153.89 O ANISOU 314 OE1 GLN A 50 19225 18133 21113 -1217 962 9302 O ATOM 315 NE2 GLN A 50 -33.541 83.709 -26.083 1.00153.03 N ANISOU 315 NE2 GLN A 50 19860 17926 20357 -432 607 9112 N ATOM 316 N LYS A 51 -30.241 80.025 -21.458 1.00134.53 N ANISOU 316 N LYS A 51 16138 16579 18400 -1762 548 6625 N ATOM 317 CA LYS A 51 -29.126 79.970 -20.518 1.00134.28 C ANISOU 317 CA LYS A 51 15627 16562 18830 -2237 546 6542 C ATOM 318 C LYS A 51 -28.149 78.829 -20.794 1.00133.08 C ANISOU 318 C LYS A 51 15203 17200 18162 -2027 924 6711 C ATOM 319 O LYS A 51 -26.940 79.048 -20.871 1.00137.23 O ANISOU 319 O LYS A 51 15240 17911 18990 -2304 1185 7261 O ATOM 320 CB LYS A 51 -29.635 79.888 -19.076 1.00129.01 C ANISOU 320 CB LYS A 51 15025 15533 18461 -2465 79 5631 C ATOM 321 CG LYS A 51 -30.062 81.223 -18.487 1.00132.21 C ANISOU 321 CG LYS A 51 15492 15096 19645 -2850 -291 5490 C ATOM 322 CD LYS A 51 -30.223 81.130 -16.977 1.00128.89 C ANISOU 322 CD LYS A 51 15034 14451 19489 -3084 -699 4633 C ATOM 323 CE LYS A 51 -30.402 82.505 -16.353 1.00133.43 C ANISOU 323 CE LYS A 51 15624 14181 20893 -3487 -1075 4471 C ATOM 324 NZ LYS A 51 -30.418 82.436 -14.866 1.00131.46 N ANISOU 324 NZ LYS A 51 15321 13794 20836 -3682 -1469 3634 N ATOM 325 N ILE A 52 -28.672 77.615 -20.936 1.00127.89 N ANISOU 325 N ILE A 52 14837 16980 16777 -1536 943 6242 N ATOM 326 CA ILE A 52 -27.824 76.439 -21.118 1.00126.90 C ANISOU 326 CA ILE A 52 14509 17550 16158 -1268 1264 6285 C ATOM 327 C ILE A 52 -26.996 76.502 -22.394 1.00133.17 C ANISOU 327 C ILE A 52 15127 18845 16625 -1010 1796 7156 C ATOM 328 O ILE A 52 -25.826 76.127 -22.397 1.00136.12 O ANISOU 328 O ILE A 52 15062 19664 16995 -1047 2118 7490 O ATOM 329 CB ILE A 52 -28.637 75.125 -21.106 1.00120.01 C ANISOU 329 CB ILE A 52 14033 16947 14617 -769 1154 5606 C ATOM 330 CG1 ILE A 52 -29.928 75.284 -21.909 1.00119.29 C ANISOU 330 CG1 ILE A 52 14455 16693 14175 -412 1002 5496 C ATOM 331 CG2 ILE A 52 -28.951 74.701 -19.682 1.00113.61 C ANISOU 331 CG2 ILE A 52 13192 15900 14074 -1007 798 4863 C ATOM 332 CD1 ILE A 52 -30.780 74.037 -21.932 1.00114.60 C ANISOU 332 CD1 ILE A 52 14216 16290 13036 21 836 4828 C ATOM 333 N ARG A 53 -27.607 76.981 -23.472 1.00136.43 N ANISOU 333 N ARG A 53 15864 19229 16744 -712 1897 7548 N ATOM 334 CA ARG A 53 -26.934 77.053 -24.764 1.00143.58 C ANISOU 334 CA ARG A 53 16663 20678 17214 -364 2436 8414 C ATOM 335 C ARG A 53 -25.709 77.965 -24.708 1.00150.87 C ANISOU 335 C ARG A 53 16960 21528 18838 -878 2741 9265 C ATOM 336 O ARG A 53 -24.725 77.739 -25.413 1.00157.12 O ANISOU 336 O ARG A 53 17461 22846 19391 -631 3157 9644 O ATOM 337 CB ARG A 53 -27.904 77.536 -25.844 1.00145.57 C ANISOU 337 CB ARG A 53 17394 20864 17051 35 2417 8689 C ATOM 338 CG ARG A 53 -27.327 77.537 -27.247 1.00152.00 C ANISOU 338 CG ARG A 53 18186 22281 17285 530 2917 9355 C ATOM 339 CD ARG A 53 -27.788 78.760 -28.017 1.00156.90 C ANISOU 339 CD ARG A 53 18963 22551 18099 525 2901 9872 C ATOM 340 NE ARG A 53 -27.482 79.992 -27.295 1.00158.27 N ANISOU 340 NE ARG A 53 18788 21998 19351 -210 2785 10234 N ATOM 341 CZ ARG A 53 -26.317 80.628 -27.361 1.00164.54 C ANISOU 341 CZ ARG A 53 19050 22758 20710 -562 3061 10757 C ATOM 342 NH1 ARG A 53 -25.338 80.151 -28.118 1.00168.86 N ANISOU 342 NH1 ARG A 53 19330 23994 20835 -224 3509 11051 N ATOM 343 NH2 ARG A 53 -26.128 81.743 -26.667 1.00167.10 N ANISOU 343 NH2 ARG A 53 19102 22337 22050 -1233 2856 10954 N ATOM 344 N SER A 54 -25.775 78.987 -23.858 1.00150.70 N ANISOU 344 N SER A 54 16757 20759 19742 -1538 2397 9209 N ATOM 345 CA SER A 54 -24.687 79.950 -23.710 1.00157.81 C ANISOU 345 CA SER A 54 17070 21413 21478 -2094 2522 9801 C ATOM 346 C SER A 54 -23.392 79.278 -23.257 1.00161.20 C ANISOU 346 C SER A 54 16929 22342 21979 -2210 2703 9757 C ATOM 347 O SER A 54 -22.295 79.750 -23.564 1.00169.47 O ANISOU 347 O SER A 54 17495 23499 23398 -2371 2924 10230 O ATOM 348 CB SER A 54 -25.080 81.055 -22.727 1.00155.76 C ANISOU 348 CB SER A 54 16770 20201 22211 -2786 2027 9615 C ATOM 349 OG SER A 54 -24.052 82.021 -22.603 1.00163.29 O ANISOU 349 OG SER A 54 17210 20847 23986 -3276 2037 9973 O ATOM 350 N LEU A 55 -23.528 78.175 -22.528 1.00155.34 N ANISOU 350 N LEU A 55 16237 21900 20884 -2098 2592 9190 N ATOM 351 CA LEU A 55 -22.377 77.408 -22.066 1.00155.51 C ANISOU 351 CA LEU A 55 15750 22438 20898 -2120 2746 9113 C ATOM 352 C LEU A 55 -22.151 76.201 -22.974 1.00153.04 C ANISOU 352 C LEU A 55 15611 22920 19616 -1321 3171 9111 C ATOM 353 O LEU A 55 -22.695 76.130 -24.075 1.00153.39 O ANISOU 353 O LEU A 55 16085 23136 19061 -801 3366 9257 O ATOM 354 CB LEU A 55 -22.596 76.940 -20.625 1.00150.20 C ANISOU 354 CB LEU A 55 15077 21543 20450 -2391 2247 8232 C ATOM 355 CG LEU A 55 -23.115 77.981 -19.630 1.00150.27 C ANISOU 355 CG LEU A 55 15144 20709 21244 -2999 1669 7818 C ATOM 356 CD1 LEU A 55 -23.284 77.370 -18.246 1.00144.49 C ANISOU 356 CD1 LEU A 55 14442 19921 20536 -3106 1221 6907 C ATOM 357 CD2 LEU A 55 -22.194 79.191 -19.577 1.00159.12 C ANISOU 357 CD2 LEU A 55 15671 21480 23307 -3660 1678 8484 C ATOM 358 N ASP A 56 -21.343 75.256 -22.507 1.00150.91 N ANISOU 358 N ASP A 56 15019 23117 19205 -1197 3271 8895 N ATOM 359 CA ASP A 56 -21.155 73.996 -23.215 1.00150.41 C ANISOU 359 CA ASP A 56 15159 23717 18274 -421 3596 8734 C ATOM 360 C ASP A 56 -21.663 72.858 -22.335 1.00141.42 C ANISOU 360 C ASP A 56 14239 22679 16814 -282 3395 8055 C ATOM 361 O ASP A 56 -21.067 71.781 -22.269 1.00139.95 O ANISOU 361 O ASP A 56 13941 22951 16284 112 3556 7840 O ATOM 362 CB ASP A 56 -19.684 73.791 -23.583 1.00158.80 C ANISOU 362 CB ASP A 56 15662 25264 19411 -261 3941 9129 C ATOM 363 CG ASP A 56 -19.493 72.721 -24.639 1.00162.28 C ANISOU 363 CG ASP A 56 16358 26319 18983 605 4306 9060 C ATOM 364 OD1 ASP A 56 -20.500 72.314 -25.258 1.00159.90 O ANISOU 364 OD1 ASP A 56 16677 26037 18041 1061 4286 8754 O ATOM 365 OD2 ASP A 56 -18.340 72.284 -24.846 1.00167.37 O ANISOU 365 OD2 ASP A 56 16587 27410 19597 839 4576 9283 O ATOM 366 N VAL A 57 -22.775 73.119 -21.656 1.00135.03 N ANISOU 366 N VAL A 57 13838 21252 16213 -534 2872 7428 N ATOM 367 CA VAL A 57 -23.375 72.162 -20.738 1.00125.88 C ANISOU 367 CA VAL A 57 12967 19967 14895 -419 2509 6556 C ATOM 368 C VAL A 57 -24.487 71.360 -21.408 1.00121.79 C ANISOU 368 C VAL A 57 13125 19477 13674 173 2462 6106 C ATOM 369 O VAL A 57 -25.303 70.735 -20.732 1.00115.80 O ANISOU 369 O VAL A 57 12682 18462 12856 221 2116 5406 O ATOM 370 CB VAL A 57 -23.950 72.873 -19.498 1.00120.90 C ANISOU 370 CB VAL A 57 12351 18682 14903 -1013 1963 6092 C ATOM 371 CG1 VAL A 57 -22.847 73.591 -18.739 1.00124.91 C ANISOU 371 CG1 VAL A 57 12195 19138 16127 -1609 1897 6398 C ATOM 372 CG2 VAL A 57 -25.037 73.854 -19.907 1.00119.88 C ANISOU 372 CG2 VAL A 57 12623 18015 14908 -1135 1762 6100 C ATOM 373 N VAL A 58 -24.512 71.384 -22.737 1.00125.22 N ANISOU 373 N VAL A 58 13759 20239 13581 627 2802 6524 N ATOM 374 CA VAL A 58 -25.520 70.660 -23.506 1.00122.13 C ANISOU 374 CA VAL A 58 13996 19913 12495 1216 2716 6099 C ATOM 375 C VAL A 58 -25.442 69.155 -23.253 1.00117.85 C ANISOU 375 C VAL A 58 13599 19618 11562 1648 2707 5518 C ATOM 376 O VAL A 58 -26.465 68.483 -23.139 1.00112.05 O ANISOU 376 O VAL A 58 13316 18632 10626 1843 2377 4862 O ATOM 377 CB VAL A 58 -25.399 70.956 -25.022 1.00128.90 C ANISOU 377 CB VAL A 58 15013 21203 12759 1701 3111 6703 C ATOM 378 CG1 VAL A 58 -23.951 70.817 -25.491 1.00135.52 C ANISOU 378 CG1 VAL A 58 15361 22594 13536 1883 3629 7250 C ATOM 379 CG2 VAL A 58 -26.331 70.058 -25.829 1.00109.42 C ANISOU 379 CG2 VAL A 58 13182 18887 9505 2376 2972 6170 C ATOM 380 N GLY A 59 -24.222 68.638 -23.148 1.00120.83 N ANISOU 380 N GLY A 59 13557 20457 11896 1785 3065 5787 N ATOM 381 CA GLY A 59 -24.008 67.227 -22.889 1.00118.60 C ANISOU 381 CA GLY A 59 13371 20386 11306 2215 3092 5310 C ATOM 382 C GLY A 59 -24.020 66.920 -21.405 1.00112.55 C ANISOU 382 C GLY A 59 12405 19288 11072 1790 2762 4898 C ATOM 383 O GLY A 59 -24.262 65.783 -21.000 1.00107.92 O ANISOU 383 O GLY A 59 12022 18648 10336 2062 2638 4386 O ATOM 384 N LYS A 60 -23.763 67.942 -20.594 1.00114.18 N ANISOU 384 N LYS A 60 12221 19259 11901 1137 2610 5128 N ATOM 385 CA LYS A 60 -23.727 67.788 -19.143 1.00112.22 C ANISOU 385 CA LYS A 60 11764 18761 12111 740 2282 4765 C ATOM 386 C LYS A 60 -25.106 67.460 -18.582 1.00108.26 C ANISOU 386 C LYS A 60 11757 17763 11613 706 1859 4088 C ATOM 387 O LYS A 60 -25.258 66.513 -17.810 1.00106.28 O ANISOU 387 O LYS A 60 11570 17468 11343 819 1725 3681 O ATOM 388 CB LYS A 60 -23.174 69.050 -18.476 1.00115.33 C ANISOU 388 CB LYS A 60 11665 18996 13160 65 2155 5104 C ATOM 389 CG LYS A 60 -21.771 69.432 -18.925 1.00123.88 C ANISOU 389 CG LYS A 60 12130 20548 14392 -4 2557 5839 C ATOM 390 CD LYS A 60 -20.747 68.378 -18.534 1.00125.17 C ANISOU 390 CD LYS A 60 11919 21219 14421 282 2754 5853 C ATOM 391 CE LYS A 60 -19.349 68.777 -18.980 1.00130.97 C ANISOU 391 CE LYS A 60 11953 22463 15348 211 3173 6626 C ATOM 392 NZ LYS A 60 -18.323 67.800 -18.525 1.00131.58 N ANISOU 392 NZ LYS A 60 11601 23045 15349 492 3337 6651 N ATOM 393 N ILE A 61 -26.108 68.247 -18.966 1.00108.35 N ANISOU 393 N ILE A 61 12087 17408 11673 561 1667 4019 N ATOM 394 CA ILE A 61 -27.477 67.987 -18.532 1.00104.35 C ANISOU 394 CA ILE A 61 12001 16461 11186 547 1292 3427 C ATOM 395 C ILE A 61 -28.072 66.811 -19.299 1.00104.61 C ANISOU 395 C ILE A 61 12463 16578 10707 1111 1320 3099 C ATOM 396 O ILE A 61 -28.969 66.130 -18.806 1.00100.96 O ANISOU 396 O ILE A 61 12246 15832 10281 1158 1061 2595 O ATOM 397 CB ILE A 61 -28.386 69.227 -18.665 1.00103.76 C ANISOU 397 CB ILE A 61 12098 15959 11365 238 1052 3449 C ATOM 398 CG1 ILE A 61 -28.323 69.793 -20.081 1.00110.07 C ANISOU 398 CG1 ILE A 61 13027 16922 11874 461 1280 3925 C ATOM 399 CG2 ILE A 61 -27.991 70.291 -17.653 1.00104.36 C ANISOU 399 CG2 ILE A 61 11819 15797 12036 -341 894 3561 C ATOM 400 CD1 ILE A 61 -29.142 71.057 -20.261 1.00111.99 C ANISOU 400 CD1 ILE A 61 13422 16732 12396 192 1064 4036 C ATOM 401 N ARG A 62 -27.566 66.577 -20.506 1.00109.42 N ANISOU 401 N ARG A 62 13147 17576 10850 1548 1633 3386 N ATOM 402 CA ARG A 62 -27.906 65.374 -21.253 1.00110.32 C ANISOU 402 CA ARG A 62 13652 17817 10449 2145 1657 3029 C ATOM 403 C ARG A 62 -27.434 64.162 -20.460 1.00107.38 C ANISOU 403 C ARG A 62 13161 17483 10153 2283 1691 2755 C ATOM 404 O ARG A 62 -28.134 63.154 -20.366 1.00104.82 O ANISOU 404 O ARG A 62 13155 16916 9758 2511 1487 2248 O ATOM 405 CB ARG A 62 -27.241 65.394 -22.630 1.00118.25 C ANISOU 405 CB ARG A 62 14711 19341 10876 2647 2045 3429 C ATOM 406 CG ARG A 62 -27.228 64.049 -23.341 1.00122.40 C ANISOU 406 CG ARG A 62 15580 20087 10839 3345 2123 3045 C ATOM 407 CD ARG A 62 -28.612 63.654 -23.821 1.00122.17 C ANISOU 407 CD ARG A 62 16105 19712 10602 3542 1699 2450 C ATOM 408 NE ARG A 62 -28.904 64.180 -25.151 1.00127.31 N ANISOU 408 NE ARG A 62 17040 20635 10696 3896 1752 2637 N ATOM 409 CZ ARG A 62 -28.722 63.499 -26.278 1.00132.91 C ANISOU 409 CZ ARG A 62 18067 21735 10697 4600 1890 2495 C ATOM 410 NH1 ARG A 62 -28.250 62.260 -26.238 1.00134.43 N ANISOU 410 NH1 ARG A 62 18339 22025 10714 5015 1984 2136 N ATOM 411 NH2 ARG A 62 -29.014 64.055 -27.446 1.00137.50 N ANISOU 411 NH2 ARG A 62 18906 22613 10724 4933 1926 2705 N ATOM 412 N ARG A 63 -26.243 64.280 -19.883 1.00108.15 N ANISOU 412 N ARG A 63 12774 17870 10447 2131 1932 3121 N ATOM 413 CA ARG A 63 -25.664 63.225 -19.060 1.00107.41 C ANISOU 413 CA ARG A 63 12502 17861 10449 2265 1980 2964 C ATOM 414 C ARG A 63 -26.476 62.994 -17.790 1.00100.07 C ANISOU 414 C ARG A 63 11638 16480 9906 1925 1609 2563 C ATOM 415 O ARG A 63 -26.671 61.855 -17.368 1.00 98.49 O ANISOU 415 O ARG A 63 11576 16147 9700 2158 1547 2255 O ATOM 416 CB ARG A 63 -24.220 63.573 -18.699 1.00112.88 C ANISOU 416 CB ARG A 63 12586 19000 11304 2130 2271 3488 C ATOM 417 CG ARG A 63 -23.551 62.593 -17.752 1.00114.48 C ANISOU 417 CG ARG A 63 12538 19331 11628 2257 2298 3394 C ATOM 418 CD ARG A 63 -22.122 63.018 -17.462 1.00120.21 C ANISOU 418 CD ARG A 63 12596 20543 12535 2112 2545 3931 C ATOM 419 NE ARG A 63 -22.063 64.303 -16.772 1.00120.80 N ANISOU 419 NE ARG A 63 12337 20483 13077 1424 2322 4117 N ATOM 420 CZ ARG A 63 -20.945 64.995 -16.576 1.00125.40 C ANISOU 420 CZ ARG A 63 12304 21394 13947 1133 2447 4598 C ATOM 421 NH1 ARG A 63 -19.787 64.528 -17.024 1.00130.01 N ANISOU 421 NH1 ARG A 63 12497 22524 14377 1487 2842 4996 N ATOM 422 NH2 ARG A 63 -20.985 66.155 -15.936 1.00125.52 N ANISOU 422 NH2 ARG A 63 12076 21180 14437 497 2165 4668 N ATOM 423 N GLU A 64 -26.943 64.079 -17.181 1.00 96.43 N ANISOU 423 N GLU A 64 11076 15777 9785 1401 1383 2590 N ATOM 424 CA GLU A 64 -27.746 63.983 -15.968 1.00 91.04 C ANISOU 424 CA GLU A 64 10443 14733 9416 1110 1069 2242 C ATOM 425 C GLU A 64 -29.050 63.245 -16.241 1.00 88.61 C ANISOU 425 C GLU A 64 10590 14055 9022 1314 874 1797 C ATOM 426 O GLU A 64 -29.420 62.331 -15.507 1.00 87.41 O ANISOU 426 O GLU A 64 10497 13727 8989 1376 779 1546 O ATOM 427 CB GLU A 64 -28.041 65.372 -15.394 1.00 90.31 C ANISOU 427 CB GLU A 64 10204 14445 9664 581 862 2309 C ATOM 428 CG GLU A 64 -28.921 65.343 -14.149 1.00 87.67 C ANISOU 428 CG GLU A 64 9933 13799 9580 346 571 1943 C ATOM 429 CD GLU A 64 -29.229 66.727 -13.603 1.00 88.05 C ANISOU 429 CD GLU A 64 9883 13632 9942 -104 351 1931 C ATOM 430 OE1 GLU A 64 -28.653 67.712 -14.112 1.00 90.92 O ANISOU 430 OE1 GLU A 64 10084 14045 10415 -297 410 2244 O ATOM 431 OE2 GLU A 64 -30.048 66.826 -12.662 1.00 85.47 O ANISOU 431 OE2 GLU A 64 9635 13073 9767 -245 132 1620 O ATOM 432 N ILE A 65 -29.739 63.646 -17.304 1.00 89.04 N ANISOU 432 N ILE A 65 10939 13998 8893 1417 804 1735 N ATOM 433 CA ILE A 65 -31.010 63.032 -17.673 1.00 85.53 C ANISOU 433 CA ILE A 65 10887 13210 8401 1584 554 1300 C ATOM 434 C ILE A 65 -30.830 61.563 -18.053 1.00 88.01 C ANISOU 434 C ILE A 65 11391 13539 8508 2050 621 1059 C ATOM 435 O ILE A 65 -31.645 60.719 -17.683 1.00 88.10 O ANISOU 435 O ILE A 65 11565 13194 8715 2076 414 702 O ATOM 436 CB ILE A 65 -31.699 63.802 -18.819 1.00 83.70 C ANISOU 436 CB ILE A 65 10915 12931 7955 1652 436 1308 C ATOM 437 CG1 ILE A 65 -31.991 65.239 -18.388 1.00 80.53 C ANISOU 437 CG1 ILE A 65 10357 12391 7849 1200 336 1515 C ATOM 438 CG2 ILE A 65 -32.992 63.121 -19.228 1.00 83.21 C ANISOU 438 CG2 ILE A 65 11209 12542 7864 1828 116 826 C ATOM 439 CD1 ILE A 65 -32.681 66.062 -19.446 1.00 82.42 C ANISOU 439 CD1 ILE A 65 10834 12564 7916 1273 217 1593 C ATOM 440 N GLN A 66 -29.754 61.264 -18.776 1.00 90.46 N ANISOU 440 N GLN A 66 11663 14246 8462 2425 922 1270 N ATOM 441 CA GLN A 66 -29.447 59.894 -19.181 1.00 93.29 C ANISOU 441 CA GLN A 66 12217 14624 8606 2943 1009 1028 C ATOM 442 C GLN A 66 -29.330 58.947 -17.990 1.00 89.96 C ANISOU 442 C GLN A 66 11655 13980 8547 2878 983 924 C ATOM 443 O GLN A 66 -29.892 57.851 -18.002 1.00 90.17 O ANISOU 443 O GLN A 66 11939 13644 8677 3089 826 554 O ATOM 444 CB GLN A 66 -28.156 59.858 -19.999 1.00100.76 C ANISOU 444 CB GLN A 66 13047 16126 9112 3370 1415 1358 C ATOM 445 CG GLN A 66 -28.369 59.684 -21.493 1.00107.91 C ANISOU 445 CG GLN A 66 14352 17196 9453 3892 1441 1185 C ATOM 446 CD GLN A 66 -28.882 58.301 -21.853 1.00111.45 C ANISOU 446 CD GLN A 66 15223 17330 9795 4346 1231 579 C ATOM 447 OE1 GLN A 66 -28.109 57.350 -21.962 1.00115.20 O ANISOU 447 OE1 GLN A 66 15713 17940 10118 4802 1444 512 O ATOM 448 NE2 GLN A 66 -30.193 58.184 -22.039 1.00110.57 N ANISOU 448 NE2 GLN A 66 15436 16767 9807 4225 793 127 N ATOM 449 N ASN A 67 -28.598 59.377 -16.966 1.00 87.48 N ANISOU 449 N ASN A 67 10927 13874 8440 2588 1116 1263 N ATOM 450 CA ASN A 67 -28.403 58.573 -15.765 1.00 86.59 C ANISOU 450 CA ASN A 67 10646 13642 8611 2549 1111 1258 C ATOM 451 C ASN A 67 -29.701 58.364 -14.999 1.00 84.93 C ANISOU 451 C ASN A 67 10579 12939 8751 2266 820 986 C ATOM 452 O ASN A 67 -30.030 57.250 -14.595 1.00 86.72 O ANISOU 452 O ASN A 67 10915 12862 9171 2418 770 829 O ATOM 453 CB ASN A 67 -27.379 59.233 -14.840 1.00 87.45 C ANISOU 453 CB ASN A 67 10267 14141 8821 2284 1244 1657 C ATOM 454 CG ASN A 67 -26.016 59.383 -15.485 1.00 93.90 C ANISOU 454 CG ASN A 67 10818 15479 9380 2541 1567 2008 C ATOM 455 OD1 ASN A 67 -25.661 58.635 -16.396 1.00 99.40 O ANISOU 455 OD1 ASN A 67 11689 16288 9792 3049 1760 1957 O ATOM 456 ND2 ASN A 67 -25.240 60.351 -15.009 1.00 93.89 N ANISOU 456 ND2 ASN A 67 10374 15805 9497 2203 1622 2359 N ATOM 457 N LEU A 68 -30.436 59.453 -14.812 1.00 83.50 N ANISOU 457 N LEU A 68 10377 12669 8681 1868 647 966 N ATOM 458 CA LEU A 68 -31.619 59.457 -13.965 1.00 82.27 C ANISOU 458 CA LEU A 68 10257 12145 8854 1581 423 784 C ATOM 459 C LEU A 68 -32.823 58.808 -14.640 1.00 85.04 C ANISOU 459 C LEU A 68 10942 12055 9313 1696 202 417 C ATOM 460 O LEU A 68 -33.760 58.385 -13.965 1.00 86.09 O ANISOU 460 O LEU A 68 11076 11852 9782 1542 63 289 O ATOM 461 CB LEU A 68 -31.953 60.895 -13.564 1.00 80.92 C ANISOU 461 CB LEU A 68 9947 12037 8763 1173 316 862 C ATOM 462 CG LEU A 68 -32.917 61.119 -12.400 1.00 79.96 C ANISOU 462 CG LEU A 68 9752 11698 8932 888 163 755 C ATOM 463 CD1 LEU A 68 -32.403 60.439 -11.139 1.00 81.37 C ANISOU 463 CD1 LEU A 68 9714 12016 9187 915 277 901 C ATOM 464 CD2 LEU A 68 -33.117 62.609 -12.169 1.00 78.27 C ANISOU 464 CD2 LEU A 68 9443 11536 8762 565 55 785 C ATOM 465 N LYS A 69 -32.790 58.724 -15.967 1.00 88.37 N ANISOU 465 N LYS A 69 11623 12507 9448 1978 165 259 N ATOM 466 CA LYS A 69 -33.939 58.256 -16.743 1.00 90.62 C ANISOU 466 CA LYS A 69 12224 12408 9799 2082 -135 -149 C ATOM 467 C LYS A 69 -34.348 56.819 -16.419 1.00 91.34 C ANISOU 467 C LYS A 69 12415 12059 10229 2210 -241 -395 C ATOM 468 O LYS A 69 -35.536 56.492 -16.405 1.00 90.98 O ANISOU 468 O LYS A 69 12455 11590 10524 2063 -529 -662 O ATOM 469 CB LYS A 69 -33.673 58.395 -18.247 1.00 96.07 C ANISOU 469 CB LYS A 69 13196 13310 9997 2457 -151 -276 C ATOM 470 CG LYS A 69 -34.892 58.121 -19.120 1.00100.72 C ANISOU 470 CG LYS A 69 14105 13571 10592 2555 -551 -732 C ATOM 471 CD LYS A 69 -34.547 58.164 -20.603 1.00106.94 C ANISOU 471 CD LYS A 69 15208 14652 10773 3031 -560 -871 C ATOM 472 CE LYS A 69 -35.776 57.897 -21.467 1.00109.80 C ANISOU 472 CE LYS A 69 15885 14720 11112 3144 -1042 -1377 C ATOM 473 NZ LYS A 69 -35.454 57.854 -22.923 1.00114.54 N ANISOU 473 NZ LYS A 69 16842 15660 11019 3699 -1077 -1559 N ATOM 474 N LEU A 70 -33.369 55.962 -16.156 1.00 92.69 N ANISOU 474 N LEU A 70 12546 12309 10362 2482 -12 -277 N ATOM 475 CA LEU A 70 -33.661 54.553 -15.922 1.00 95.68 C ANISOU 475 CA LEU A 70 13047 12205 11102 2646 -99 -478 C ATOM 476 C LEU A 70 -33.541 54.152 -14.453 1.00 93.73 C ANISOU 476 C LEU A 70 12511 11869 11233 2447 60 -143 C ATOM 477 O LEU A 70 -33.540 52.965 -14.127 1.00 97.36 O ANISOU 477 O LEU A 70 13025 11958 12011 2608 72 -165 O ATOM 478 CB LEU A 70 -32.766 53.665 -16.794 1.00100.74 C ANISOU 478 CB LEU A 70 13929 12896 11452 3214 9 -649 C ATOM 479 CG LEU A 70 -32.877 53.856 -18.311 1.00102.82 C ANISOU 479 CG LEU A 70 14540 13276 11251 3545 -145 -1021 C ATOM 480 CD1 LEU A 70 -32.055 52.809 -19.047 1.00107.37 C ANISOU 480 CD1 LEU A 70 15375 13858 11562 4180 -32 -1249 C ATOM 481 CD2 LEU A 70 -34.328 53.817 -18.765 1.00103.14 C ANISOU 481 CD2 LEU A 70 14791 12859 11538 3350 -613 -1458 C ATOM 482 N PHE A 71 -33.445 55.138 -13.569 1.00 88.71 N ANISOU 482 N PHE A 71 11586 11562 10557 2124 168 164 N ATOM 483 CA PHE A 71 -33.368 54.860 -12.139 1.00 85.40 C ANISOU 483 CA PHE A 71 10901 11158 10387 1972 306 483 C ATOM 484 C PHE A 71 -34.749 54.646 -11.545 1.00 84.13 C ANISOU 484 C PHE A 71 10707 10574 10683 1685 150 426 C ATOM 485 O PHE A 71 -35.697 55.345 -11.890 1.00 83.74 O ANISOU 485 O PHE A 71 10695 10426 10694 1455 -45 231 O ATOM 486 CB PHE A 71 -32.666 55.994 -11.388 1.00 81.54 C ANISOU 486 CB PHE A 71 10122 11217 9641 1780 443 774 C ATOM 487 CG PHE A 71 -31.170 55.950 -11.478 1.00 81.13 C ANISOU 487 CG PHE A 71 9932 11608 9286 2034 657 995 C ATOM 488 CD1 PHE A 71 -30.537 55.031 -12.295 1.00 83.48 C ANISOU 488 CD1 PHE A 71 10391 11847 9481 2463 758 923 C ATOM 489 CD2 PHE A 71 -30.396 56.823 -10.733 1.00 79.46 C ANISOU 489 CD2 PHE A 71 9405 11872 8912 1862 738 1255 C ATOM 490 CE1 PHE A 71 -29.163 54.991 -12.377 1.00 85.17 C ANISOU 490 CE1 PHE A 71 10418 12513 9431 2730 986 1162 C ATOM 491 CE2 PHE A 71 -29.020 56.787 -10.809 1.00 81.13 C ANISOU 491 CE2 PHE A 71 9408 12513 8906 2072 916 1486 C ATOM 492 CZ PHE A 71 -28.403 55.869 -11.631 1.00 84.10 C ANISOU 492 CZ PHE A 71 9909 12868 9178 2513 1066 1469 C ATOM 493 N ARG A 72 -34.850 53.674 -10.647 1.00 85.67 N ANISOU 493 N ARG A 72 10800 10537 11214 1720 258 649 N ATOM 494 CA ARG A 72 -36.086 53.427 -9.924 1.00 87.38 C ANISOU 494 CA ARG A 72 10894 10411 11896 1452 198 730 C ATOM 495 C ARG A 72 -35.759 52.813 -8.568 1.00 88.32 C ANISOU 495 C ARG A 72 10795 10617 12145 1506 458 1203 C ATOM 496 O ARG A 72 -35.628 51.596 -8.440 1.00 92.40 O ANISOU 496 O ARG A 72 11361 10760 12986 1689 525 1343 O ATOM 497 CB ARG A 72 -37.005 52.510 -10.728 1.00 95.13 C ANISOU 497 CB ARG A 72 12067 10722 13358 1450 -57 413 C ATOM 498 CG ARG A 72 -38.479 52.725 -10.436 1.00100.64 C ANISOU 498 CG ARG A 72 12604 11140 14496 1092 -212 381 C ATOM 499 CD ARG A 72 -39.355 52.219 -11.572 1.00107.56 C ANISOU 499 CD ARG A 72 13670 11461 15736 1052 -600 -82 C ATOM 500 NE ARG A 72 -40.639 52.916 -11.609 1.00109.23 N ANISOU 500 NE ARG A 72 13715 11618 16172 731 -802 -193 N ATOM 501 CZ ARG A 72 -41.544 52.766 -12.570 1.00112.97 C ANISOU 501 CZ ARG A 72 14286 11719 16920 647 -1207 -611 C ATOM 502 NH1 ARG A 72 -41.311 51.938 -13.579 1.00116.32 N ANISOU 502 NH1 ARG A 72 15017 11780 17399 867 -1471 -1011 N ATOM 503 NH2 ARG A 72 -42.683 53.444 -12.522 1.00113.31 N ANISOU 503 NH2 ARG A 72 14116 11771 17166 377 -1369 -657 N ATOM 504 N HIS A 73 -35.617 53.668 -7.561 1.00 85.02 N ANISOU 504 N HIS A 73 10152 10691 11462 1379 588 1442 N ATOM 505 CA HIS A 73 -35.208 53.235 -6.231 1.00 85.03 C ANISOU 505 CA HIS A 73 9948 10935 11427 1487 827 1904 C ATOM 506 C HIS A 73 -35.974 54.013 -5.165 1.00 83.81 C ANISOU 506 C HIS A 73 9586 11058 11201 1270 891 2052 C ATOM 507 O HIS A 73 -36.234 55.205 -5.334 1.00 83.37 O ANISOU 507 O HIS A 73 9521 11227 10927 1088 769 1802 O ATOM 508 CB HIS A 73 -33.700 53.438 -6.057 1.00 84.53 C ANISOU 508 CB HIS A 73 9821 11391 10904 1723 922 2032 C ATOM 509 CG HIS A 73 -33.147 52.844 -4.799 1.00 87.24 C ANISOU 509 CG HIS A 73 9975 12001 11170 1924 1125 2506 C ATOM 510 ND1 HIS A 73 -33.232 53.477 -3.577 1.00 87.02 N ANISOU 510 ND1 HIS A 73 9740 12448 10874 1844 1190 2719 N ATOM 511 CD2 HIS A 73 -32.503 51.675 -4.572 1.00 90.95 C ANISOU 511 CD2 HIS A 73 10447 12344 11767 2249 1268 2811 C ATOM 512 CE1 HIS A 73 -32.665 52.723 -2.652 1.00 90.16 C ANISOU 512 CE1 HIS A 73 10013 13047 11196 2112 1359 3157 C ATOM 513 NE2 HIS A 73 -32.214 51.624 -3.230 1.00 92.53 N ANISOU 513 NE2 HIS A 73 10428 12970 11760 2353 1417 3246 N ATOM 514 N PRO A 74 -36.344 53.336 -4.066 1.00 84.09 N ANISOU 514 N PRO A 74 9458 11076 11417 1328 1099 2478 N ATOM 515 CA PRO A 74 -37.107 53.919 -2.956 1.00 83.58 C ANISOU 515 CA PRO A 74 9188 11319 11248 1219 1227 2671 C ATOM 516 C PRO A 74 -36.481 55.176 -2.356 1.00 82.62 C ANISOU 516 C PRO A 74 9005 11872 10516 1235 1186 2550 C ATOM 517 O PRO A 74 -37.195 55.988 -1.769 1.00 83.41 O ANISOU 517 O PRO A 74 9011 12194 10485 1133 1201 2485 O ATOM 518 CB PRO A 74 -37.099 52.803 -1.912 1.00 88.05 C ANISOU 518 CB PRO A 74 9612 11865 11978 1414 1512 3263 C ATOM 519 CG PRO A 74 -37.009 51.561 -2.706 1.00 91.06 C ANISOU 519 CG PRO A 74 10131 11585 12884 1475 1473 3295 C ATOM 520 CD PRO A 74 -36.145 51.887 -3.888 1.00 87.90 C ANISOU 520 CD PRO A 74 9955 11175 12266 1532 1243 2825 C ATOM 521 N HIS A 75 -35.171 55.334 -2.495 1.00 81.76 N ANISOU 521 N HIS A 75 8926 12070 10069 1371 1121 2507 N ATOM 522 CA HIS A 75 -34.479 56.449 -1.861 1.00 79.76 C ANISOU 522 CA HIS A 75 8574 12420 9310 1363 1030 2397 C ATOM 523 C HIS A 75 -33.738 57.325 -2.862 1.00 77.45 C ANISOU 523 C HIS A 75 8356 12178 8893 1225 815 2042 C ATOM 524 O HIS A 75 -32.762 57.991 -2.522 1.00 78.17 O ANISOU 524 O HIS A 75 8332 12710 8659 1231 717 2000 O ATOM 525 CB HIS A 75 -33.538 55.935 -0.772 1.00 80.91 C ANISOU 525 CB HIS A 75 8568 13037 9138 1651 1147 2776 C ATOM 526 CG HIS A 75 -34.235 55.143 0.289 1.00 83.58 C ANISOU 526 CG HIS A 75 8819 13397 9541 1820 1401 3223 C ATOM 527 ND1 HIS A 75 -34.070 53.782 0.431 1.00 87.09 N ANISOU 527 ND1 HIS A 75 9250 13594 10245 2042 1601 3679 N ATOM 528 CD2 HIS A 75 -35.122 55.516 1.241 1.00 84.53 C ANISOU 528 CD2 HIS A 75 8853 13747 9516 1822 1519 3324 C ATOM 529 CE1 HIS A 75 -34.814 53.354 1.436 1.00 90.08 C ANISOU 529 CE1 HIS A 75 9520 14051 10656 2144 1842 4098 C ATOM 530 NE2 HIS A 75 -35.463 54.386 1.943 1.00 88.70 N ANISOU 530 NE2 HIS A 75 9292 14204 10205 2029 1813 3893 N ATOM 531 N ILE A 76 -34.213 57.313 -4.102 1.00 75.79 N ANISOU 531 N ILE A 76 8319 11524 8955 1104 734 1809 N ATOM 532 CA ILE A 76 -33.718 58.219 -5.127 1.00 74.62 C ANISOU 532 CA ILE A 76 8250 11407 8693 973 571 1528 C ATOM 533 C ILE A 76 -34.905 58.890 -5.800 1.00 74.10 C ANISOU 533 C ILE A 76 8323 11013 8819 757 435 1240 C ATOM 534 O ILE A 76 -35.840 58.214 -6.236 1.00 75.41 O ANISOU 534 O ILE A 76 8586 10766 9298 757 433 1197 O ATOM 535 CB ILE A 76 -32.892 57.485 -6.197 1.00 74.88 C ANISOU 535 CB ILE A 76 8385 11311 8755 1160 611 1549 C ATOM 536 CG1 ILE A 76 -31.739 56.712 -5.555 1.00 76.71 C ANISOU 536 CG1 ILE A 76 8456 11848 8843 1431 756 1866 C ATOM 537 CG2 ILE A 76 -32.360 58.473 -7.226 1.00 74.10 C ANISOU 537 CG2 ILE A 76 8333 11324 8498 1048 503 1356 C ATOM 538 CD1 ILE A 76 -30.913 55.920 -6.546 1.00 78.18 C ANISOU 538 CD1 ILE A 76 8731 11925 9048 1703 836 1889 C ATOM 539 N ILE A 77 -34.872 60.218 -5.871 1.00 72.63 N ANISOU 539 N ILE A 77 8126 10985 8486 573 294 1045 N ATOM 540 CA ILE A 77 -35.943 60.976 -6.507 1.00 73.07 C ANISOU 540 CA ILE A 77 8301 10759 8701 404 151 795 C ATOM 541 C ILE A 77 -36.134 60.519 -7.950 1.00 73.86 C ANISOU 541 C ILE A 77 8598 10525 8941 449 79 686 C ATOM 542 O ILE A 77 -35.186 60.506 -8.740 1.00 73.47 O ANISOU 542 O ILE A 77 8616 10571 8729 533 88 707 O ATOM 543 CB ILE A 77 -35.662 62.491 -6.481 1.00 73.63 C ANISOU 543 CB ILE A 77 8356 10998 8623 224 2 628 C ATOM 544 CG1 ILE A 77 -35.560 62.996 -5.040 1.00 73.65 C ANISOU 544 CG1 ILE A 77 8206 11324 8455 215 4 619 C ATOM 545 CG2 ILE A 77 -36.751 63.249 -7.233 1.00 72.64 C ANISOU 545 CG2 ILE A 77 8368 10559 8673 103 -145 410 C ATOM 546 CD1 ILE A 77 -36.883 63.012 -4.309 1.00 74.22 C ANISOU 546 CD1 ILE A 77 8262 11317 8622 253 61 557 C ATOM 547 N LYS A 78 -37.362 60.133 -8.280 1.00 74.50 N ANISOU 547 N LYS A 78 8748 10246 9312 417 2 569 N ATOM 548 CA LYS A 78 -37.670 59.612 -9.605 1.00 75.24 C ANISOU 548 CA LYS A 78 9044 10014 9528 490 -137 393 C ATOM 549 C LYS A 78 -37.821 60.738 -10.617 1.00 73.35 C ANISOU 549 C LYS A 78 8943 9787 9138 419 -317 206 C ATOM 550 O LYS A 78 -38.334 61.808 -10.295 1.00 71.67 O ANISOU 550 O LYS A 78 8667 9624 8942 263 -386 157 O ATOM 551 CB LYS A 78 -38.952 58.778 -9.563 1.00 77.14 C ANISOU 551 CB LYS A 78 9256 9848 10207 445 -216 329 C ATOM 552 CG LYS A 78 -38.933 57.672 -8.521 1.00 81.74 C ANISOU 552 CG LYS A 78 9681 10364 11012 501 -8 610 C ATOM 553 CD LYS A 78 -40.302 57.026 -8.369 1.00 86.73 C ANISOU 553 CD LYS A 78 10190 10589 12173 377 -67 620 C ATOM 554 CE LYS A 78 -40.298 55.959 -7.280 1.00 90.32 C ANISOU 554 CE LYS A 78 10463 10972 12882 428 191 1014 C ATOM 555 NZ LYS A 78 -39.380 54.825 -7.597 1.00 92.47 N ANISOU 555 NZ LYS A 78 10886 11051 13197 632 235 1089 N ATOM 556 N LEU A 79 -37.357 60.492 -11.837 1.00 73.35 N ANISOU 556 N LEU A 79 9144 9753 8974 578 -379 117 N ATOM 557 CA LEU A 79 -37.605 61.403 -12.946 1.00 71.24 C ANISOU 557 CA LEU A 79 9037 9482 8550 572 -546 -10 C ATOM 558 C LEU A 79 -38.792 60.883 -13.745 1.00 73.95 C ANISOU 558 C LEU A 79 9531 9481 9087 632 -811 -287 C ATOM 559 O LEU A 79 -38.659 59.943 -14.531 1.00 77.53 O ANISOU 559 O LEU A 79 10164 9802 9492 845 -889 -443 O ATOM 560 CB LEU A 79 -36.376 61.514 -13.848 1.00 69.59 C ANISOU 560 CB LEU A 79 8942 9533 7967 762 -432 100 C ATOM 561 CG LEU A 79 -36.559 62.342 -15.123 1.00 69.17 C ANISOU 561 CG LEU A 79 9081 9517 7684 830 -563 52 C ATOM 562 CD1 LEU A 79 -36.785 63.809 -14.794 1.00 68.22 C ANISOU 562 CD1 LEU A 79 8855 9433 7633 567 -606 173 C ATOM 563 CD2 LEU A 79 -35.375 62.176 -16.056 1.00 71.20 C ANISOU 563 CD2 LEU A 79 9438 10067 7547 1103 -383 199 C ATOM 564 N TYR A 80 -39.955 61.488 -13.535 1.00 72.51 N ANISOU 564 N TYR A 80 9261 9152 9136 464 -976 -377 N ATOM 565 CA TYR A 80 -41.167 61.031 -14.199 1.00 74.34 C ANISOU 565 CA TYR A 80 9551 9070 9626 480 -1278 -638 C ATOM 566 C TYR A 80 -41.123 61.309 -15.699 1.00 76.70 C ANISOU 566 C TYR A 80 10134 9406 9603 682 -1512 -821 C ATOM 567 O TYR A 80 -41.315 60.403 -16.511 1.00 79.34 O ANISOU 567 O TYR A 80 10641 9568 9937 856 -1718 -1077 O ATOM 568 CB TYR A 80 -42.403 61.683 -13.576 1.00 74.22 C ANISOU 568 CB TYR A 80 9311 8955 9935 285 -1370 -646 C ATOM 569 CG TYR A 80 -42.689 61.258 -12.150 1.00 73.40 C ANISOU 569 CG TYR A 80 8922 8831 10137 149 -1143 -471 C ATOM 570 CD1 TYR A 80 -42.247 60.037 -11.662 1.00 74.48 C ANISOU 570 CD1 TYR A 80 9012 8880 10406 182 -981 -353 C ATOM 571 CD2 TYR A 80 -43.407 62.083 -11.294 1.00 72.43 C ANISOU 571 CD2 TYR A 80 8584 8790 10143 39 -1075 -402 C ATOM 572 CE1 TYR A 80 -42.511 59.654 -10.358 1.00 75.93 C ANISOU 572 CE1 TYR A 80 8935 9091 10823 98 -744 -112 C ATOM 573 CE2 TYR A 80 -43.675 61.709 -9.995 1.00 72.45 C ANISOU 573 CE2 TYR A 80 8333 8858 10337 -19 -831 -211 C ATOM 574 CZ TYR A 80 -43.227 60.497 -9.531 1.00 75.67 C ANISOU 574 CZ TYR A 80 8691 9210 10852 5 -660 -37 C ATOM 575 OH TYR A 80 -43.500 60.132 -8.232 1.00 78.85 O ANISOU 575 OH TYR A 80 8838 9720 11401 -16 -388 229 O ATOM 576 N GLN A 81 -40.865 62.560 -16.064 1.00 77.58 N ANISOU 576 N GLN A 81 10303 9734 9438 680 -1489 -688 N ATOM 577 CA GLN A 81 -40.860 62.955 -17.470 1.00 82.96 C ANISOU 577 CA GLN A 81 11247 10516 9757 905 -1677 -768 C ATOM 578 C GLN A 81 -39.868 64.067 -17.776 1.00 81.79 C ANISOU 578 C GLN A 81 11155 10671 9252 933 -1459 -441 C ATOM 579 O GLN A 81 -39.282 64.663 -16.875 1.00 80.55 O ANISOU 579 O GLN A 81 10817 10598 9189 728 -1233 -211 O ATOM 580 CB GLN A 81 -42.256 63.404 -17.903 1.00 88.01 C ANISOU 580 CB GLN A 81 11878 10977 10583 875 -2045 -956 C ATOM 581 CG GLN A 81 -43.158 62.286 -18.384 1.00 94.30 C ANISOU 581 CG GLN A 81 12715 11513 11602 953 -2400 -1336 C ATOM 582 CD GLN A 81 -44.479 62.805 -18.910 1.00 98.50 C ANISOU 582 CD GLN A 81 13196 11938 12291 946 -2803 -1505 C ATOM 583 OE1 GLN A 81 -44.905 63.907 -18.563 1.00 97.51 O ANISOU 583 OE1 GLN A 81 12935 11860 12254 838 -2768 -1326 O ATOM 584 NE2 GLN A 81 -45.132 62.016 -19.758 1.00103.10 N ANISOU 584 NE2 GLN A 81 13885 12367 12923 1083 -3221 -1879 N ATOM 585 N VAL A 82 -39.692 64.339 -19.064 1.00 83.34 N ANISOU 585 N VAL A 82 11593 11031 9042 1195 -1545 -416 N ATOM 586 CA VAL A 82 -38.900 65.475 -19.517 1.00 83.48 C ANISOU 586 CA VAL A 82 11644 11303 8773 1217 -1349 -27 C ATOM 587 C VAL A 82 -39.544 66.099 -20.758 1.00 85.51 C ANISOU 587 C VAL A 82 12128 11614 8747 1443 -1591 -14 C ATOM 588 O VAL A 82 -39.527 65.523 -21.847 1.00 88.66 O ANISOU 588 O VAL A 82 12776 12180 8731 1805 -1706 -160 O ATOM 589 CB VAL A 82 -37.419 65.094 -19.761 1.00 84.65 C ANISOU 589 CB VAL A 82 11798 11779 8585 1378 -997 211 C ATOM 590 CG1 VAL A 82 -37.312 63.738 -20.438 1.00 87.77 C ANISOU 590 CG1 VAL A 82 12408 12233 8709 1750 -1056 -95 C ATOM 591 CG2 VAL A 82 -36.705 66.173 -20.562 1.00 86.53 C ANISOU 591 CG2 VAL A 82 12075 12295 8507 1457 -809 657 C ATOM 592 N ILE A 83 -40.133 67.275 -20.570 1.00 84.11 N ANISOU 592 N ILE A 83 11878 11297 8784 1270 -1686 143 N ATOM 593 CA ILE A 83 -40.889 67.944 -21.621 1.00 87.22 C ANISOU 593 CA ILE A 83 12457 11712 8972 1483 -1950 191 C ATOM 594 C ILE A 83 -40.127 69.146 -22.167 1.00 90.01 C ANISOU 594 C ILE A 83 12867 12232 9099 1519 -1718 734 C ATOM 595 O ILE A 83 -39.621 69.969 -21.404 1.00 89.68 O ANISOU 595 O ILE A 83 12643 12066 9366 1214 -1511 1006 O ATOM 596 CB ILE A 83 -42.278 68.407 -21.109 1.00 88.20 C ANISOU 596 CB ILE A 83 12447 11518 9546 1324 -2260 -6 C ATOM 597 CG1 ILE A 83 -43.219 67.213 -20.926 1.00 86.83 C ANISOU 597 CG1 ILE A 83 12208 11196 9588 1338 -2552 -490 C ATOM 598 CG2 ILE A 83 -42.903 69.412 -22.064 1.00 91.85 C ANISOU 598 CG2 ILE A 83 13058 12005 9837 1527 -2483 177 C ATOM 599 CD1 ILE A 83 -43.115 66.541 -19.576 1.00 83.16 C ANISOU 599 CD1 ILE A 83 11492 10566 9540 1052 -2370 -610 C ATOM 600 N SER A 84 -40.047 69.244 -23.490 1.00 93.27 N ANISOU 600 N SER A 84 13531 12927 8981 1900 -1764 899 N ATOM 601 CA SER A 84 -39.366 70.361 -24.132 1.00 95.05 C ANISOU 601 CA SER A 84 13804 13324 8987 1967 -1516 1517 C ATOM 602 C SER A 84 -40.343 71.325 -24.796 1.00 97.76 C ANISOU 602 C SER A 84 14284 13560 9299 2115 -1796 1678 C ATOM 603 O SER A 84 -41.350 70.912 -25.369 1.00 99.28 O ANISOU 603 O SER A 84 14636 13790 9295 2385 -2186 1333 O ATOM 604 CB SER A 84 -38.362 69.854 -25.171 1.00 99.29 C ANISOU 604 CB SER A 84 14505 14363 8857 2361 -1242 1748 C ATOM 605 OG SER A 84 -37.320 69.112 -24.565 1.00 98.70 O ANISOU 605 OG SER A 84 14264 14401 8836 2244 -931 1706 O ATOM 606 N THR A 85 -40.034 72.613 -24.701 1.00 99.20 N ANISOU 606 N THR A 85 14388 13583 9723 1934 -1622 2205 N ATOM 607 CA THR A 85 -40.744 73.646 -25.441 1.00102.17 C ANISOU 607 CA THR A 85 14908 13872 10039 2126 -1809 2524 C ATOM 608 C THR A 85 -39.714 74.289 -26.364 1.00108.34 C ANISOU 608 C THR A 85 15771 14948 10444 2294 -1437 3272 C ATOM 609 O THR A 85 -38.522 74.008 -26.241 1.00109.63 O ANISOU 609 O THR A 85 15811 15322 10521 2186 -1049 3497 O ATOM 610 CB THR A 85 -41.335 74.708 -24.493 1.00 98.53 C ANISOU 610 CB THR A 85 14282 12862 10292 1777 -1924 2542 C ATOM 611 OG1 THR A 85 -40.284 75.526 -23.967 1.00 97.84 O ANISOU 611 OG1 THR A 85 14035 12582 10556 1425 -1581 2979 O ATOM 612 CG2 THR A 85 -42.085 74.048 -23.348 1.00 93.48 C ANISOU 612 CG2 THR A 85 13473 11991 10055 1560 -2135 1891 C ATOM 613 N PRO A 86 -40.155 75.142 -27.303 1.00112.98 N ANISOU 613 N PRO A 86 16538 15582 10805 2583 -1532 3713 N ATOM 614 CA PRO A 86 -39.138 75.827 -28.108 1.00118.86 C ANISOU 614 CA PRO A 86 17310 16590 11262 2709 -1105 4551 C ATOM 615 C PRO A 86 -38.293 76.804 -27.287 1.00118.21 C ANISOU 615 C PRO A 86 16931 16082 11901 2158 -788 5019 C ATOM 616 O PRO A 86 -37.291 77.315 -27.788 1.00122.84 O ANISOU 616 O PRO A 86 17430 16846 12397 2146 -379 5749 O ATOM 617 CB PRO A 86 -39.970 76.588 -29.144 1.00124.68 C ANISOU 617 CB PRO A 86 18297 17386 11692 3122 -1331 4918 C ATOM 618 CG PRO A 86 -41.237 75.817 -29.245 1.00108.20 C ANISOU 618 CG PRO A 86 16361 15353 9397 3382 -1880 4160 C ATOM 619 CD PRO A 86 -41.508 75.323 -27.858 1.00114.60 C ANISOU 619 CD PRO A 86 16931 15746 10867 2905 -2007 3509 C ATOM 620 N SER A 87 -38.688 77.049 -26.040 1.00113.29 N ANISOU 620 N SER A 87 16139 14920 11985 1721 -982 4600 N ATOM 621 CA SER A 87 -38.002 78.019 -25.192 1.00112.84 C ANISOU 621 CA SER A 87 15827 14391 12655 1198 -803 4908 C ATOM 622 C SER A 87 -37.261 77.390 -24.009 1.00108.55 C ANISOU 622 C SER A 87 15011 13824 12408 797 -691 4507 C ATOM 623 O SER A 87 -36.154 77.813 -23.673 1.00111.31 O ANISOU 623 O SER A 87 15109 14104 13078 454 -419 4879 O ATOM 624 CB SER A 87 -38.991 79.075 -24.690 1.00112.67 C ANISOU 624 CB SER A 87 15850 13728 13232 1059 -1119 4807 C ATOM 625 OG SER A 87 -40.102 78.473 -24.046 1.00107.63 O ANISOU 625 OG SER A 87 15250 12997 12647 1122 -1474 4042 O ATOM 626 N ASP A 88 -37.868 76.388 -23.379 1.00103.12 N ANISOU 626 N ASP A 88 14345 13196 11639 838 -909 3784 N ATOM 627 CA ASP A 88 -37.297 75.797 -22.168 1.00 99.09 C ANISOU 627 CA ASP A 88 13593 12654 11403 498 -837 3401 C ATOM 628 C ASP A 88 -37.452 74.279 -22.086 1.00 94.21 C ANISOU 628 C ASP A 88 13023 12393 10381 713 -876 2890 C ATOM 629 O ASP A 88 -38.213 73.677 -22.843 1.00 94.76 O ANISOU 629 O ASP A 88 13317 12646 10040 1087 -1056 2682 O ATOM 630 CB ASP A 88 -37.909 76.444 -20.922 1.00 99.12 C ANISOU 630 CB ASP A 88 13501 12122 12039 171 -1077 3034 C ATOM 631 CG ASP A 88 -39.076 77.356 -21.252 1.00104.43 C ANISOU 631 CG ASP A 88 14355 12428 12897 321 -1343 3067 C ATOM 632 OD1 ASP A 88 -40.205 76.845 -21.421 1.00103.06 O ANISOU 632 OD1 ASP A 88 14306 12318 12532 593 -1591 2694 O ATOM 633 OD2 ASP A 88 -38.863 78.584 -21.341 1.00109.61 O ANISOU 633 OD2 ASP A 88 15003 12708 13935 165 -1317 3480 O ATOM 634 N ILE A 89 -36.719 73.672 -21.155 1.00 90.31 N ANISOU 634 N ILE A 89 12309 11969 10034 476 -737 2690 N ATOM 635 CA ILE A 89 -36.790 72.233 -20.912 1.00 85.84 C ANISOU 635 CA ILE A 89 11763 11647 9206 637 -756 2235 C ATOM 636 C ILE A 89 -37.223 71.962 -19.471 1.00 82.51 C ANISOU 636 C ILE A 89 11183 10962 9205 357 -902 1772 C ATOM 637 O ILE A 89 -36.648 72.512 -18.531 1.00 83.18 O ANISOU 637 O ILE A 89 11054 10906 9644 24 -828 1834 O ATOM 638 CB ILE A 89 -35.435 71.537 -21.187 1.00 83.55 C ANISOU 638 CB ILE A 89 11356 11787 8604 729 -400 2473 C ATOM 639 CG1 ILE A 89 -35.050 71.679 -22.661 1.00 87.78 C ANISOU 639 CG1 ILE A 89 12062 12687 8605 1111 -206 2929 C ATOM 640 CG2 ILE A 89 -35.494 70.068 -20.798 1.00 78.38 C ANISOU 640 CG2 ILE A 89 10723 11276 7783 881 -433 1993 C ATOM 641 CD1 ILE A 89 -33.789 70.932 -23.042 1.00 89.72 C ANISOU 641 CD1 ILE A 89 12196 13420 8473 1315 176 3154 C ATOM 642 N PHE A 90 -38.238 71.118 -19.301 1.00 79.09 N ANISOU 642 N PHE A 90 10841 10478 8734 502 -1119 1317 N ATOM 643 CA PHE A 90 -38.794 70.839 -17.978 1.00 74.99 C ANISOU 643 CA PHE A 90 10166 9753 8574 296 -1222 939 C ATOM 644 C PHE A 90 -38.542 69.405 -17.515 1.00 73.01 C ANISOU 644 C PHE A 90 9847 9673 8220 352 -1139 688 C ATOM 645 O PHE A 90 -38.998 68.452 -18.145 1.00 73.60 O ANISOU 645 O PHE A 90 10060 9812 8093 593 -1246 491 O ATOM 646 CB PHE A 90 -40.300 71.118 -17.960 1.00 74.47 C ANISOU 646 CB PHE A 90 10165 9427 8703 370 -1523 679 C ATOM 647 CG PHE A 90 -40.661 72.547 -18.258 1.00 76.93 C ANISOU 647 CG PHE A 90 10541 9497 9192 342 -1625 903 C ATOM 648 CD1 PHE A 90 -40.675 73.498 -17.250 1.00 77.03 C ANISOU 648 CD1 PHE A 90 10434 9227 9608 99 -1624 870 C ATOM 649 CD2 PHE A 90 -40.995 72.937 -19.545 1.00 79.72 C ANISOU 649 CD2 PHE A 90 11095 9897 9299 597 -1739 1136 C ATOM 650 CE1 PHE A 90 -41.008 74.814 -17.521 1.00 79.12 C ANISOU 650 CE1 PHE A 90 10778 9182 10101 90 -1731 1066 C ATOM 651 CE2 PHE A 90 -41.330 74.251 -19.822 1.00 81.97 C ANISOU 651 CE2 PHE A 90 11444 9918 9781 595 -1825 1401 C ATOM 652 CZ PHE A 90 -41.336 75.190 -18.808 1.00 81.76 C ANISOU 652 CZ PHE A 90 11298 9534 10234 331 -1820 1365 C ATOM 653 N MET A 91 -37.825 69.260 -16.404 1.00 70.94 N ANISOU 653 N MET A 91 9377 9460 8115 139 -981 685 N ATOM 654 CA MET A 91 -37.618 67.952 -15.792 1.00 69.46 C ANISOU 654 CA MET A 91 9106 9393 7893 190 -894 498 C ATOM 655 C MET A 91 -38.634 67.719 -14.678 1.00 67.95 C ANISOU 655 C MET A 91 8809 9009 8002 85 -1010 214 C ATOM 656 O MET A 91 -38.508 68.276 -13.589 1.00 67.28 O ANISOU 656 O MET A 91 8569 8899 8094 -103 -973 197 O ATOM 657 CB MET A 91 -36.197 67.830 -15.239 1.00 70.08 C ANISOU 657 CB MET A 91 8992 9719 7915 81 -648 709 C ATOM 658 CG MET A 91 -35.111 67.770 -16.306 1.00 73.67 C ANISOU 658 CG MET A 91 9482 10452 8058 242 -448 1030 C ATOM 659 SD MET A 91 -33.454 67.692 -15.595 1.00106.73 S ANISOU 659 SD MET A 91 13332 14957 12265 91 -182 1307 S ATOM 660 CE MET A 91 -33.653 66.348 -14.426 1.00 62.64 C ANISOU 660 CE MET A 91 7678 9383 6741 158 -193 999 C ATOM 661 N VAL A 92 -39.641 66.897 -14.959 1.00 68.61 N ANISOU 661 N VAL A 92 8957 8968 8142 219 -1158 -9 N ATOM 662 CA VAL A 92 -40.697 66.612 -13.990 1.00 67.01 C ANISOU 662 CA VAL A 92 8601 8607 8254 137 -1228 -205 C ATOM 663 C VAL A 92 -40.304 65.465 -13.060 1.00 67.17 C ANISOU 663 C VAL A 92 8481 8712 8330 117 -1047 -209 C ATOM 664 O VAL A 92 -40.193 64.315 -13.487 1.00 66.12 O ANISOU 664 O VAL A 92 8412 8549 8162 241 -1046 -259 O ATOM 665 CB VAL A 92 -42.024 66.263 -14.689 1.00 65.17 C ANISOU 665 CB VAL A 92 8420 8178 8164 246 -1498 -407 C ATOM 666 CG1 VAL A 92 -43.176 66.338 -13.701 1.00 63.50 C ANISOU 666 CG1 VAL A 92 7976 7829 8323 149 -1535 -521 C ATOM 667 CG2 VAL A 92 -42.264 67.198 -15.860 1.00 66.02 C ANISOU 667 CG2 VAL A 92 8715 8262 8108 360 -1688 -355 C ATOM 668 N MET A 93 -40.102 65.785 -11.787 1.00 67.99 N ANISOU 668 N MET A 93 8411 8912 8510 -6 -912 -164 N ATOM 669 CA MET A 93 -39.639 64.798 -10.821 1.00 69.78 C ANISOU 669 CA MET A 93 8499 9277 8737 7 -722 -89 C ATOM 670 C MET A 93 -40.617 64.606 -9.667 1.00 72.43 C ANISOU 670 C MET A 93 8648 9577 9294 -23 -666 -134 C ATOM 671 O MET A 93 -41.586 65.346 -9.525 1.00 71.99 O ANISOU 671 O MET A 93 8549 9420 9386 -52 -762 -248 O ATOM 672 CB MET A 93 -38.268 65.198 -10.272 1.00 69.81 C ANISOU 672 CB MET A 93 8434 9561 8531 -54 -586 59 C ATOM 673 CG MET A 93 -37.167 65.229 -11.312 1.00 71.26 C ANISOU 673 CG MET A 93 8715 9856 8504 -4 -548 202 C ATOM 674 SD MET A 93 -35.719 66.140 -10.743 1.00 79.81 S ANISOU 674 SD MET A 93 9622 11223 9477 -174 -470 382 S ATOM 675 CE MET A 93 -36.429 67.767 -10.505 1.00 93.61 C ANISOU 675 CE MET A 93 11403 12746 11418 -378 -667 238 C ATOM 676 N GLU A 94 -40.339 63.601 -8.845 1.00 76.93 N ANISOU 676 N GLU A 94 9096 10255 9879 22 -484 -1 N ATOM 677 CA GLU A 94 -41.140 63.297 -7.668 1.00 81.50 C ANISOU 677 CA GLU A 94 9468 10881 10616 35 -346 66 C ATOM 678 C GLU A 94 -40.942 64.351 -6.585 1.00 82.34 C ANISOU 678 C GLU A 94 9505 11265 10516 34 -286 19 C ATOM 679 O GLU A 94 -39.811 64.681 -6.231 1.00 80.91 O ANISOU 679 O GLU A 94 9351 11316 10075 22 -268 43 O ATOM 680 CB GLU A 94 -40.750 61.921 -7.128 1.00 86.09 C ANISOU 680 CB GLU A 94 9961 11505 11246 114 -150 302 C ATOM 681 CG GLU A 94 -41.289 61.606 -5.748 1.00 91.25 C ANISOU 681 CG GLU A 94 10385 12328 11958 168 78 499 C ATOM 682 CD GLU A 94 -40.611 60.400 -5.129 1.00 95.74 C ANISOU 682 CD GLU A 94 10887 12996 12495 277 289 810 C ATOM 683 OE1 GLU A 94 -39.552 59.982 -5.647 1.00 94.96 O ANISOU 683 OE1 GLU A 94 10916 12895 12269 327 256 830 O ATOM 684 OE2 GLU A 94 -41.135 59.870 -4.127 1.00100.39 O ANISOU 684 OE2 GLU A 94 11282 13678 13183 345 510 1073 O ATOM 685 N TYR A 95 -42.043 64.875 -6.056 1.00 86.58 N ANISOU 685 N TYR A 95 9936 11783 11177 67 -273 -74 N ATOM 686 CA TYR A 95 -41.971 65.887 -5.007 1.00 89.22 C ANISOU 686 CA TYR A 95 10241 12361 11299 131 -241 -206 C ATOM 687 C TYR A 95 -42.066 65.285 -3.611 1.00 91.71 C ANISOU 687 C TYR A 95 10378 13018 11450 292 21 -40 C ATOM 688 O TYR A 95 -42.896 64.415 -3.350 1.00 92.07 O ANISOU 688 O TYR A 95 10248 13034 11699 354 207 174 O ATOM 689 CB TYR A 95 -43.062 66.943 -5.186 1.00 89.50 C ANISOU 689 CB TYR A 95 10283 12222 11500 164 -360 -426 C ATOM 690 CG TYR A 95 -43.212 67.856 -3.991 1.00 91.49 C ANISOU 690 CG TYR A 95 10507 12704 11551 313 -307 -617 C ATOM 691 CD1 TYR A 95 -42.272 68.842 -3.724 1.00 92.12 C ANISOU 691 CD1 TYR A 95 10738 12841 11424 263 -466 -832 C ATOM 692 CD2 TYR A 95 -44.292 67.731 -3.127 1.00 93.73 C ANISOU 692 CD2 TYR A 95 10599 13152 11864 519 -103 -592 C ATOM 693 CE1 TYR A 95 -42.404 69.679 -2.631 1.00 93.94 C ANISOU 693 CE1 TYR A 95 10982 13254 11457 431 -478 -1101 C ATOM 694 CE2 TYR A 95 -44.434 68.564 -2.032 1.00 95.90 C ANISOU 694 CE2 TYR A 95 10882 13678 11878 738 -49 -818 C ATOM 695 CZ TYR A 95 -43.487 69.536 -1.789 1.00 95.21 C ANISOU 695 CZ TYR A 95 11001 13614 11562 702 -263 -1114 C ATOM 696 OH TYR A 95 -43.623 70.365 -0.702 1.00 97.28 O ANISOU 696 OH TYR A 95 11309 14099 11554 949 -267 -1429 O ATOM 697 N VAL A 96 -41.206 65.762 -2.718 1.00 94.09 N ANISOU 697 N VAL A 96 10710 13650 11392 361 20 -121 N ATOM 698 CA VAL A 96 -41.235 65.349 -1.321 1.00 97.70 C ANISOU 698 CA VAL A 96 11030 14530 11562 584 249 22 C ATOM 699 C VAL A 96 -41.148 66.576 -0.418 1.00 99.30 C ANISOU 699 C VAL A 96 11298 14993 11439 720 140 -331 C ATOM 700 O VAL A 96 -40.380 67.499 -0.686 1.00 99.42 O ANISOU 700 O VAL A 96 11453 14927 11396 584 -136 -612 O ATOM 701 CB VAL A 96 -40.092 64.361 -0.988 1.00 98.56 C ANISOU 701 CB VAL A 96 11101 14878 11468 616 339 306 C ATOM 702 CG1 VAL A 96 -40.344 63.015 -1.652 1.00 98.28 C ANISOU 702 CG1 VAL A 96 11004 14563 11774 564 484 642 C ATOM 703 CG2 VAL A 96 -38.739 64.929 -1.410 1.00 96.72 C ANISOU 703 CG2 VAL A 96 10980 14680 11091 468 86 137 C ATOM 704 N SER A 97 -41.949 66.589 0.642 1.00100.90 N ANISOU 704 N SER A 97 11393 15495 11450 1000 356 -314 N ATOM 705 CA SER A 97 -41.977 67.724 1.558 1.00103.96 C ANISOU 705 CA SER A 97 11874 16142 11486 1215 249 -722 C ATOM 706 C SER A 97 -41.149 67.450 2.809 1.00109.67 C ANISOU 706 C SER A 97 12582 17439 11648 1443 295 -691 C ATOM 707 O SER A 97 -41.227 66.369 3.392 1.00112.33 O ANISOU 707 O SER A 97 12765 18093 11821 1613 600 -259 O ATOM 708 CB SER A 97 -43.416 68.065 1.943 1.00104.63 C ANISOU 708 CB SER A 97 11859 16261 11634 1474 460 -784 C ATOM 709 OG SER A 97 -44.045 66.966 2.578 1.00106.45 O ANISOU 709 OG SER A 97 11840 16798 11810 1669 873 -316 O ATOM 710 N GLY A 98 -40.361 68.437 3.220 1.00112.27 N ANISOU 710 N GLY A 98 13063 17888 11707 1449 -35 -1140 N ATOM 711 CA GLY A 98 -39.497 68.288 4.375 1.00116.78 C ANISOU 711 CA GLY A 98 13626 19031 11714 1669 -101 -1195 C ATOM 712 C GLY A 98 -38.129 68.871 4.094 1.00116.97 C ANISOU 712 C GLY A 98 13719 18963 11761 1382 -545 -1474 C ATOM 713 O GLY A 98 -37.381 69.208 5.012 1.00121.27 O ANISOU 713 O GLY A 98 14284 19913 11879 1522 -783 -1743 O ATOM 714 N GLY A 99 -37.805 68.988 2.811 1.00111.48 N ANISOU 714 N GLY A 99 13034 17759 11564 988 -663 -1396 N ATOM 715 CA GLY A 99 -36.553 69.584 2.388 1.00109.09 C ANISOU 715 CA GLY A 99 12733 17318 11397 668 -1037 -1575 C ATOM 716 C GLY A 99 -35.359 68.701 2.672 1.00105.93 C ANISOU 716 C GLY A 99 12156 17317 10773 660 -1043 -1275 C ATOM 717 O GLY A 99 -35.495 67.486 2.818 1.00102.86 O ANISOU 717 O GLY A 99 11675 17150 10256 838 -724 -834 O ATOM 718 N GLU A 100 -34.184 69.318 2.747 1.00107.97 N ANISOU 718 N GLU A 100 12344 17642 11040 450 -1418 -1497 N ATOM 719 CA GLU A 100 -32.953 68.590 3.021 1.00108.92 C ANISOU 719 CA GLU A 100 12244 18174 10967 450 -1477 -1234 C ATOM 720 C GLU A 100 -32.935 68.120 4.465 1.00113.33 C ANISOU 720 C GLU A 100 12770 19388 10901 873 -1454 -1253 C ATOM 721 O GLU A 100 -33.625 68.683 5.315 1.00117.47 O ANISOU 721 O GLU A 100 13442 20074 11116 1122 -1511 -1617 O ATOM 722 CB GLU A 100 -31.731 69.475 2.773 1.00110.13 C ANISOU 722 CB GLU A 100 12257 18241 11346 90 -1920 -1475 C ATOM 723 CG GLU A 100 -31.780 70.280 1.490 1.00107.04 C ANISOU 723 CG GLU A 100 11920 17213 11536 -311 -1986 -1506 C ATOM 724 CD GLU A 100 -32.080 71.740 1.739 1.00108.37 C ANISOU 724 CD GLU A 100 12243 17043 11889 -456 -2351 -2071 C ATOM 725 OE1 GLU A 100 -33.102 72.033 2.394 1.00109.36 O ANISOU 725 OE1 GLU A 100 12584 17177 11790 -175 -2316 -2385 O ATOM 726 OE2 GLU A 100 -31.288 72.593 1.285 1.00109.34 O ANISOU 726 OE2 GLU A 100 12257 16880 12409 -840 -2663 -2182 O ATOM 727 N LEU A 101 -32.141 67.091 4.744 1.00112.65 N ANISOU 727 N LEU A 101 13427 16487 12888 1415 340 -1212 N ATOM 728 CA LEU A 101 -31.927 66.677 6.123 1.00112.49 C ANISOU 728 CA LEU A 101 13603 16657 12481 1340 432 -1345 C ATOM 729 C LEU A 101 -30.869 67.580 6.744 1.00112.39 C ANISOU 729 C LEU A 101 13692 16700 12311 1264 400 -1627 C ATOM 730 O LEU A 101 -30.555 67.474 7.928 1.00112.85 O ANISOU 730 O LEU A 101 13932 16932 12014 1194 446 -1792 O ATOM 731 CB LEU A 101 -31.531 65.200 6.225 1.00111.18 C ANISOU 731 CB LEU A 101 13548 16685 12012 1338 255 -1136 C ATOM 732 CG LEU A 101 -30.058 64.813 6.108 1.00109.40 C ANISOU 732 CG LEU A 101 13409 16603 11553 1312 -45 -1109 C ATOM 733 CD1 LEU A 101 -29.859 63.357 6.496 1.00108.86 C ANISOU 733 CD1 LEU A 101 13461 16714 11186 1321 -134 -904 C ATOM 734 CD2 LEU A 101 -29.566 65.052 4.706 1.00106.93 C ANISOU 734 CD2 LEU A 101 12956 16150 11524 1342 -227 -1009 C ATOM 735 N PHE A 102 -30.326 68.474 5.922 1.00112.58 N ANISOU 735 N PHE A 102 13601 16571 12601 1279 326 -1689 N ATOM 736 CA PHE A 102 -29.449 69.535 6.392 1.00116.40 C ANISOU 736 CA PHE A 102 14121 17042 13064 1201 353 -2003 C ATOM 737 C PHE A 102 -30.237 70.432 7.338 1.00121.56 C ANISOU 737 C PHE A 102 14799 17620 13768 1150 700 -2265 C ATOM 738 O PHE A 102 -29.679 71.035 8.254 1.00125.18 O ANISOU 738 O PHE A 102 15361 18158 14043 1043 765 -2582 O ATOM 739 CB PHE A 102 -28.922 70.345 5.204 1.00114.98 C ANISOU 739 CB PHE A 102 13800 16641 13248 1245 293 -1985 C ATOM 740 CG PHE A 102 -27.928 71.409 5.580 1.00116.61 C ANISOU 740 CG PHE A 102 14010 16799 13495 1157 330 -2321 C ATOM 741 CD1 PHE A 102 -26.581 71.107 5.698 1.00115.94 C ANISOU 741 CD1 PHE A 102 13975 16856 13223 1092 76 -2410 C ATOM 742 CD2 PHE A 102 -28.339 72.714 5.800 1.00118.18 C ANISOU 742 CD2 PHE A 102 14139 16795 13967 1136 632 -2558 C ATOM 743 CE1 PHE A 102 -25.663 72.084 6.039 1.00117.38 C ANISOU 743 CE1 PHE A 102 14127 16989 13483 998 106 -2754 C ATOM 744 CE2 PHE A 102 -27.426 73.695 6.142 1.00119.36 C ANISOU 744 CE2 PHE A 102 14278 16887 14187 1038 693 -2900 C ATOM 745 CZ PHE A 102 -26.087 73.380 6.261 1.00119.00 C ANISOU 745 CZ PHE A 102 14271 16994 13949 964 421 -3011 C ATOM 746 N ASP A 103 -31.544 70.511 7.105 1.00122.02 N ANISOU 746 N ASP A 103 14751 17519 14094 1219 927 -2146 N ATOM 747 CA ASP A 103 -32.440 71.257 7.977 1.00124.37 C ANISOU 747 CA ASP A 103 15057 17706 14491 1174 1310 -2366 C ATOM 748 C ASP A 103 -33.043 70.337 9.035 1.00125.08 C ANISOU 748 C ASP A 103 15325 17966 14236 1131 1437 -2350 C ATOM 749 O ASP A 103 -33.739 70.795 9.941 1.00127.41 O ANISOU 749 O ASP A 103 15688 18196 14527 1071 1783 -2550 O ATOM 750 CB ASP A 103 -33.544 71.935 7.163 1.00124.92 C ANISOU 750 CB ASP A 103 14882 17473 15110 1283 1510 -2251 C ATOM 751 CG ASP A 103 -33.000 72.935 6.159 1.00123.68 C ANISOU 751 CG ASP A 103 14585 17117 15291 1342 1443 -2251 C ATOM 752 OD1 ASP A 103 -31.957 73.561 6.444 1.00123.18 O ANISOU 752 OD1 ASP A 103 14597 17075 15130 1255 1423 -2494 O ATOM 753 OD2 ASP A 103 -33.615 73.095 5.084 1.00123.35 O ANISOU 753 OD2 ASP A 103 14360 16895 15614 1477 1413 -2010 O ATOM 754 N TYR A 104 -32.777 69.038 8.909 1.00123.81 N ANISOU 754 N TYR A 104 15246 17996 13800 1163 1194 -2109 N ATOM 755 CA TYR A 104 -33.152 68.073 9.940 1.00126.31 C ANISOU 755 CA TYR A 104 15774 18486 13734 1131 1305 -2069 C ATOM 756 C TYR A 104 -32.098 68.128 11.039 1.00132.03 C ANISOU 756 C TYR A 104 16766 19461 13940 1033 1200 -2291 C ATOM 757 O TYR A 104 -32.341 67.721 12.174 1.00135.80 O ANISOU 757 O TYR A 104 17486 20078 14033 987 1358 -2358 O ATOM 758 CB TYR A 104 -33.254 66.661 9.361 1.00121.44 C ANISOU 758 CB TYR A 104 15130 17954 13057 1207 1110 -1721 C ATOM 759 CG TYR A 104 -33.857 65.633 10.294 1.00120.57 C ANISOU 759 CG TYR A 104 15208 17951 12651 1200 1301 -1630 C ATOM 760 CD1 TYR A 104 -34.705 66.009 11.328 1.00122.19 C ANISOU 760 CD1 TYR A 104 15533 18089 12803 1149 1702 -1810 C ATOM 761 CD2 TYR A 104 -33.573 64.283 10.140 1.00118.72 C ANISOU 761 CD2 TYR A 104 15041 17858 12208 1243 1123 -1364 C ATOM 762 CE1 TYR A 104 -35.253 65.067 12.179 1.00123.08 C ANISOU 762 CE1 TYR A 104 15847 18272 12645 1147 1922 -1718 C ATOM 763 CE2 TYR A 104 -34.115 63.336 10.985 1.00119.34 C ANISOU 763 CE2 TYR A 104 15304 18007 12033 1248 1338 -1262 C ATOM 764 CZ TYR A 104 -34.954 63.732 12.002 1.00121.28 C ANISOU 764 CZ TYR A 104 15685 18183 12213 1203 1739 -1436 C ATOM 765 OH TYR A 104 -35.493 62.787 12.843 1.00122.75 O ANISOU 765 OH TYR A 104 16083 18413 12145 1212 1996 -1325 O ATOM 766 N ILE A 105 -30.919 68.630 10.683 1.00133.65 N ANISOU 766 N ILE A 105 16925 19719 14136 1004 930 -2406 N ATOM 767 CA ILE A 105 -29.940 69.063 11.670 1.00139.28 C ANISOU 767 CA ILE A 105 17822 20632 14467 894 833 -2715 C ATOM 768 C ILE A 105 -30.339 70.500 12.005 1.00146.65 C ANISOU 768 C ILE A 105 18706 21373 15642 805 1165 -3074 C ATOM 769 O ILE A 105 -31.387 70.959 11.547 1.00147.57 O ANISOU 769 O ILE A 105 18666 21224 16179 851 1455 -3022 O ATOM 770 CB ILE A 105 -28.500 68.990 11.123 1.00136.43 C ANISOU 770 CB ILE A 105 17387 20377 14072 894 419 -2708 C ATOM 771 CG1 ILE A 105 -28.339 67.780 10.200 1.00132.19 C ANISOU 771 CG1 ILE A 105 16773 19866 13587 1004 174 -2303 C ATOM 772 CG2 ILE A 105 -27.489 68.901 12.261 1.00139.90 C ANISOU 772 CG2 ILE A 105 18035 21121 13999 805 210 -2936 C ATOM 773 CD1 ILE A 105 -28.458 66.444 10.907 1.00131.79 C ANISOU 773 CD1 ILE A 105 16926 20044 13106 1041 106 -2086 C ATOM 774 N CYS A 106 -29.532 71.209 12.791 1.00153.04 N ANISOU 774 N CYS A 106 19630 22305 16214 677 1129 -3443 N ATOM 775 CA CYS A 106 -29.929 72.507 13.349 1.00159.70 C ANISOU 775 CA CYS A 106 20475 22984 17219 561 1503 -3834 C ATOM 776 C CYS A 106 -31.192 72.333 14.192 1.00166.53 C ANISOU 776 C CYS A 106 21506 23803 17964 538 1913 -3848 C ATOM 777 O CYS A 106 -31.166 72.520 15.409 1.00171.57 O ANISOU 777 O CYS A 106 22409 24589 18192 412 2068 -4133 O ATOM 778 CB CYS A 106 -30.136 73.564 12.256 1.00157.34 C ANISOU 778 CB CYS A 106 19874 22331 17578 607 1655 -3853 C ATOM 779 SG CYS A 106 -28.716 73.815 11.166 1.00158.91 S ANISOU 779 SG CYS A 106 19885 22507 17985 637 1265 -3827 S ATOM 780 N LYS A 107 -32.296 71.980 13.538 1.00167.09 N ANISOU 780 N LYS A 107 21424 23664 18400 656 2092 -3553 N ATOM 781 CA LYS A 107 -33.459 71.448 14.233 1.00170.56 C ANISOU 781 CA LYS A 107 22004 24069 18730 660 2434 -3477 C ATOM 782 C LYS A 107 -33.025 70.119 14.841 1.00171.80 C ANISOU 782 C LYS A 107 22440 24554 18281 678 2194 -3294 C ATOM 783 O LYS A 107 -32.120 69.468 14.318 1.00170.07 O ANISOU 783 O LYS A 107 22187 24508 17926 739 1766 -3101 O ATOM 784 CB LYS A 107 -34.617 71.240 13.255 1.00168.43 C ANISOU 784 CB LYS A 107 21450 23523 19023 794 2583 -3180 C ATOM 785 CG LYS A 107 -35.966 71.003 13.917 1.00170.27 C ANISOU 785 CG LYS A 107 21745 23613 19338 785 3044 -3174 C ATOM 786 CD LYS A 107 -37.079 70.888 12.885 1.00167.27 C ANISOU 786 CD LYS A 107 21016 22956 19582 918 3142 -2912 C ATOM 787 CE LYS A 107 -38.446 70.803 13.546 1.00168.68 C ANISOU 787 CE LYS A 107 21201 22935 19954 899 3650 -2954 C ATOM 788 NZ LYS A 107 -38.563 69.619 14.442 1.00169.28 N ANISOU 788 NZ LYS A 107 21589 23203 19526 865 3733 -2872 N ATOM 789 N ASN A 108 -33.654 69.727 15.947 1.00176.36 N ANISOU 789 N ASN A 108 23300 25197 18510 629 2495 -3348 N ATOM 790 CA ASN A 108 -33.223 68.560 16.722 1.00178.82 C ANISOU 790 CA ASN A 108 23939 25822 18181 648 2318 -3193 C ATOM 791 C ASN A 108 -31.788 68.682 17.241 1.00183.22 C ANISOU 791 C ASN A 108 24676 26710 18230 582 1907 -3376 C ATOM 792 O ASN A 108 -31.086 69.650 16.946 1.00183.98 O ANISOU 792 O ASN A 108 24620 26784 18500 510 1759 -3638 O ATOM 793 CB ASN A 108 -33.397 67.257 15.929 1.00175.27 C ANISOU 793 CB ASN A 108 23370 25381 17842 799 2125 -2736 C ATOM 794 CG ASN A 108 -34.843 66.807 15.851 1.00175.78 C ANISOU 794 CG ASN A 108 23365 25204 18217 849 2545 -2570 C ATOM 795 OD1 ASN A 108 -35.587 67.220 14.962 1.00174.29 O ANISOU 795 OD1 ASN A 108 22849 24743 18629 890 2671 -2525 O ATOM 796 ND2 ASN A 108 -35.245 65.949 16.781 1.00178.52 N ANISOU 796 ND2 ASN A 108 24018 25643 18167 854 2766 -2471 N ATOM 797 N GLY A 109 -31.359 67.699 18.024 1.00189.21 N ANISOU 797 N GLY A 109 25746 27766 18380 613 1730 -3235 N ATOM 798 CA GLY A 109 -30.011 67.691 18.561 1.00188.09 C ANISOU 798 CA GLY A 109 25762 27967 17737 570 1289 -3376 C ATOM 799 C GLY A 109 -29.212 66.534 18.000 1.00181.53 C ANISOU 799 C GLY A 109 24857 27305 16811 712 830 -2989 C ATOM 800 O GLY A 109 -29.286 65.419 18.520 1.00183.05 O ANISOU 800 O GLY A 109 25289 27661 16599 801 795 -2710 O ATOM 801 N ARG A 110 -28.446 66.809 16.945 1.00171.55 N ANISOU 801 N ARG A 110 23268 25978 15936 733 514 -2972 N ATOM 802 CA ARG A 110 -27.746 65.773 16.193 1.00162.03 C ANISOU 802 CA ARG A 110 21931 24852 14781 860 133 -2607 C ATOM 803 C ARG A 110 -28.748 64.694 15.807 1.00155.56 C ANISOU 803 C ARG A 110 21112 23899 14096 974 358 -2207 C ATOM 804 O ARG A 110 -29.905 64.990 15.515 1.00154.20 O ANISOU 804 O ARG A 110 20849 23473 14265 964 738 -2215 O ATOM 805 CB ARG A 110 -26.606 65.166 17.018 1.00162.10 C ANISOU 805 CB ARG A 110 22153 25232 14204 884 -276 -2577 C ATOM 806 CG ARG A 110 -25.720 66.185 17.718 1.00162.69 C ANISOU 806 CG ARG A 110 22286 25493 14034 748 -479 -3033 C ATOM 807 CD ARG A 110 -24.638 65.501 18.543 1.00163.56 C ANISOU 807 CD ARG A 110 22596 25995 13554 794 -934 -2970 C ATOM 808 NE ARG A 110 -25.192 64.583 19.537 1.00165.49 N ANISOU 808 NE ARG A 110 23236 26417 13226 873 -796 -2737 N ATOM 809 CZ ARG A 110 -25.291 64.853 20.835 1.00170.80 C ANISOU 809 CZ ARG A 110 24284 27317 13296 798 -721 -2969 C ATOM 810 NH1 ARG A 110 -24.868 66.018 21.307 1.00174.04 N ANISOU 810 NH1 ARG A 110 24704 27818 13605 627 -785 -3472 N ATOM 811 NH2 ARG A 110 -25.810 63.956 21.663 1.00173.39 N ANISOU 811 NH2 ARG A 110 24991 27772 13116 889 -560 -2707 N ATOM 812 N LEU A 111 -28.303 63.444 15.820 1.00150.40 N ANISOU 812 N LEU A 111 20540 23403 13201 1082 130 -1869 N ATOM 813 CA LEU A 111 -29.208 62.313 15.668 1.00144.27 C ANISOU 813 CA LEU A 111 19811 22527 12478 1178 368 -1513 C ATOM 814 C LEU A 111 -28.725 61.141 16.509 1.00141.30 C ANISOU 814 C LEU A 111 19729 22410 11549 1271 224 -1254 C ATOM 815 O LEU A 111 -27.524 60.960 16.709 1.00141.66 O ANISOU 815 O LEU A 111 19810 22688 11326 1301 -192 -1233 O ATOM 816 CB LEU A 111 -29.336 61.891 14.203 1.00140.28 C ANISOU 816 CB LEU A 111 18963 21812 12523 1236 287 -1276 C ATOM 817 CG LEU A 111 -30.505 62.446 13.383 1.00138.15 C ANISOU 817 CG LEU A 111 18453 21232 12806 1211 594 -1329 C ATOM 818 CD1 LEU A 111 -31.744 62.631 14.251 1.00141.73 C ANISOU 818 CD1 LEU A 111 19074 21591 13188 1177 1068 -1434 C ATOM 819 CD2 LEU A 111 -30.131 63.735 12.667 1.00136.61 C ANISOU 819 CD2 LEU A 111 18027 20915 12964 1150 480 -1582 C ATOM 820 N ASP A 112 -29.670 60.349 17.002 1.00138.93 N ANISOU 820 N ASP A 112 19629 22052 11105 1326 582 -1051 N ATOM 821 CA ASP A 112 -29.347 59.169 17.790 1.00139.79 C ANISOU 821 CA ASP A 112 20041 22365 10708 1440 519 -749 C ATOM 822 C ASP A 112 -28.657 58.139 16.909 1.00137.77 C ANISOU 822 C ASP A 112 19576 22114 10658 1549 215 -399 C ATOM 823 O ASP A 112 -28.668 58.253 15.684 1.00134.25 O ANISOU 823 O ASP A 112 18781 21482 10746 1527 140 -382 O ATOM 824 CB ASP A 112 -30.623 58.559 18.370 1.00139.64 C ANISOU 824 CB ASP A 112 20250 22203 10603 1471 1060 -606 C ATOM 825 CG ASP A 112 -31.686 59.600 18.667 1.00140.53 C ANISOU 825 CG ASP A 112 20384 22127 10881 1346 1492 -941 C ATOM 826 OD1 ASP A 112 -32.364 60.041 17.715 1.00136.73 O ANISOU 826 OD1 ASP A 112 19561 21378 11010 1301 1638 -1017 O ATOM 827 OD2 ASP A 112 -31.848 59.971 19.849 1.00144.93 O ANISOU 827 OD2 ASP A 112 21306 22799 10960 1294 1690 -1123 O ATOM 828 N GLU A 113 -28.059 57.129 17.531 1.00140.90 N ANISOU 828 N GLU A 113 20195 22712 10627 1671 54 -112 N ATOM 829 CA GLU A 113 -27.537 55.999 16.778 1.00138.26 C ANISOU 829 CA GLU A 113 19686 22341 10506 1781 -135 257 C ATOM 830 C GLU A 113 -28.701 55.287 16.100 1.00136.74 C ANISOU 830 C GLU A 113 19366 21853 10737 1791 286 449 C ATOM 831 O GLU A 113 -28.542 54.683 15.043 1.00133.63 O ANISOU 831 O GLU A 113 18703 21323 10746 1813 202 631 O ATOM 832 CB GLU A 113 -26.779 55.029 17.688 1.00140.78 C ANISOU 832 CB GLU A 113 20290 22915 10284 1932 -335 559 C ATOM 833 CG GLU A 113 -25.515 55.603 18.306 1.00142.99 C ANISOU 833 CG GLU A 113 20650 23516 10162 1934 -839 389 C ATOM 834 CD GLU A 113 -24.694 54.553 19.029 1.00146.51 C ANISOU 834 CD GLU A 113 21312 24207 10147 2116 -1108 750 C ATOM 835 OE1 GLU A 113 -24.460 53.473 18.445 1.00144.02 O ANISOU 835 OE1 GLU A 113 20855 23786 10081 2229 -1130 1122 O ATOM 836 OE2 GLU A 113 -24.279 54.809 20.180 1.00151.86 O ANISOU 836 OE2 GLU A 113 22303 25184 10213 2147 -1299 663 O ATOM 837 N LYS A 114 -29.875 55.371 16.719 1.00139.23 N ANISOU 837 N LYS A 114 19870 22062 10970 1764 749 384 N ATOM 838 CA LYS A 114 -31.091 54.804 16.152 1.00137.61 C ANISOU 838 CA LYS A 114 19518 21565 11204 1756 1174 503 C ATOM 839 C LYS A 114 -31.461 55.492 14.844 1.00133.12 C ANISOU 839 C LYS A 114 18532 20789 11258 1660 1122 321 C ATOM 840 O LYS A 114 -31.780 54.835 13.853 1.00130.78 O ANISOU 840 O LYS A 114 17985 20324 11382 1669 1162 480 O ATOM 841 CB LYS A 114 -32.257 54.937 17.137 1.00141.69 C ANISOU 841 CB LYS A 114 20308 21988 11540 1732 1700 411 C ATOM 842 CG LYS A 114 -32.631 53.655 17.870 1.00144.89 C ANISOU 842 CG LYS A 114 21007 22371 11673 1846 2032 744 C ATOM 843 CD LYS A 114 -33.963 53.818 18.594 1.00148.27 C ANISOU 843 CD LYS A 114 21629 22608 12098 1799 2640 626 C ATOM 844 CE LYS A 114 -34.403 52.533 19.282 1.00151.01 C ANISOU 844 CE LYS A 114 22270 22881 12225 1914 3046 963 C ATOM 845 NZ LYS A 114 -33.537 52.183 20.441 1.00154.86 N ANISOU 845 NZ LYS A 114 23235 23668 11936 2033 2886 1147 N ATOM 846 N GLU A 115 -31.408 56.820 14.844 1.00132.54 N ANISOU 846 N GLU A 115 18397 20729 11233 1569 1037 -15 N ATOM 847 CA GLU A 115 -31.927 57.600 13.727 1.00130.10 C ANISOU 847 CA GLU A 115 17736 20205 11491 1494 1053 -185 C ATOM 848 C GLU A 115 -30.891 57.890 12.643 1.00126.19 C ANISOU 848 C GLU A 115 16991 19739 11217 1485 612 -192 C ATOM 849 O GLU A 115 -31.174 57.739 11.454 1.00123.00 O ANISOU 849 O GLU A 115 16310 19166 11258 1477 578 -118 O ATOM 850 CB GLU A 115 -32.547 58.907 14.232 1.00132.64 C ANISOU 850 CB GLU A 115 18101 20459 11839 1406 1278 -532 C ATOM 851 CG GLU A 115 -33.626 59.469 13.321 1.00131.01 C ANISOU 851 CG GLU A 115 17571 19968 12240 1365 1484 -632 C ATOM 852 CD GLU A 115 -34.843 58.564 13.229 1.00130.83 C ANISOU 852 CD GLU A 115 17486 19756 12466 1395 1856 -459 C ATOM 853 OE1 GLU A 115 -35.079 57.775 14.171 1.00133.29 O ANISOU 853 OE1 GLU A 115 18075 20118 12451 1428 2108 -336 O ATOM 854 OE2 GLU A 115 -35.569 58.647 12.216 1.00128.34 O ANISOU 854 OE2 GLU A 115 16846 19240 12677 1387 1899 -450 O ATOM 855 N SER A 116 -29.697 58.308 13.053 1.00126.12 N ANISOU 855 N SER A 116 17084 19939 10898 1481 283 -293 N ATOM 856 CA SER A 116 -28.637 58.651 12.108 1.00121.02 C ANISOU 856 CA SER A 116 16213 19299 10470 1465 -100 -330 C ATOM 857 C SER A 116 -28.236 57.452 11.260 1.00116.73 C ANISOU 857 C SER A 116 15541 18711 10102 1528 -239 -5 C ATOM 858 O SER A 116 -27.860 57.601 10.098 1.00113.54 O ANISOU 858 O SER A 116 14900 18189 10051 1502 -404 2 O ATOM 859 CB SER A 116 -27.413 59.198 12.842 1.00122.89 C ANISOU 859 CB SER A 116 16575 19777 10341 1448 -421 -505 C ATOM 860 OG SER A 116 -26.899 58.237 13.746 1.00125.47 O ANISOU 860 OG SER A 116 17142 20326 10203 1536 -535 -293 O ATOM 861 N ARG A 117 -28.320 56.264 11.847 1.00116.76 N ANISOU 861 N ARG A 117 15717 18792 9855 1609 -141 264 N ATOM 862 CA ARG A 117 -27.986 55.037 11.136 1.00113.83 C ANISOU 862 CA ARG A 117 15236 18359 9655 1665 -209 576 C ATOM 863 C ARG A 117 -29.070 54.664 10.132 1.00110.99 C ANISOU 863 C ARG A 117 14674 17753 9746 1624 47 638 C ATOM 864 O ARG A 117 -28.769 54.256 9.011 1.00107.70 O ANISOU 864 O ARG A 117 14055 17229 9638 1604 -74 736 O ATOM 865 CB ARG A 117 -27.755 53.894 12.124 1.00115.84 C ANISOU 865 CB ARG A 117 15744 18754 9515 1779 -150 861 C ATOM 866 CG ARG A 117 -27.587 52.532 11.483 1.00113.64 C ANISOU 866 CG ARG A 117 15363 18370 9445 1837 -113 1196 C ATOM 867 CD ARG A 117 -26.768 51.618 12.375 1.00116.11 C ANISOU 867 CD ARG A 117 15890 18862 9365 1975 -232 1482 C ATOM 868 NE ARG A 117 -27.175 51.703 13.776 1.00119.50 N ANISOU 868 NE ARG A 117 16669 19448 9288 2038 -65 1482 N ATOM 869 CZ ARG A 117 -26.540 51.106 14.781 1.00120.81 C ANISOU 869 CZ ARG A 117 17096 19817 8989 2175 -182 1710 C ATOM 870 NH1 ARG A 117 -25.460 50.373 14.545 1.00119.70 N ANISOU 870 NH1 ARG A 117 16868 19738 8876 2271 -473 1963 N ATOM 871 NH2 ARG A 117 -26.983 51.243 16.023 1.00123.86 N ANISOU 871 NH2 ARG A 117 17839 20339 8883 2220 -2 1691 N ATOM 872 N ARG A 118 -30.328 54.813 10.540 1.00112.84 N ANISOU 872 N ARG A 118 14960 17893 10020 1605 403 561 N ATOM 873 CA ARG A 118 -31.465 54.500 9.679 1.00111.35 C ANISOU 873 CA ARG A 118 14555 17481 10272 1565 640 586 C ATOM 874 C ARG A 118 -31.406 55.286 8.375 1.00108.54 C ANISOU 874 C ARG A 118 13921 17015 10302 1502 432 446 C ATOM 875 O ARG A 118 -31.629 54.733 7.299 1.00107.06 O ANISOU 875 O ARG A 118 13541 16709 10429 1477 404 545 O ATOM 876 CB ARG A 118 -32.783 54.791 10.398 1.00113.74 C ANISOU 876 CB ARG A 118 14931 17688 10597 1549 1046 467 C ATOM 877 CG ARG A 118 -34.017 54.421 9.587 1.00113.37 C ANISOU 877 CG ARG A 118 14628 17413 11036 1512 1285 480 C ATOM 878 CD ARG A 118 -35.287 54.929 10.245 1.00116.71 C ANISOU 878 CD ARG A 118 15070 17709 11564 1490 1677 316 C ATOM 879 NE ARG A 118 -35.314 56.387 10.306 1.00118.01 N ANISOU 879 NE ARG A 118 15197 17876 11767 1454 1596 53 N ATOM 880 CZ ARG A 118 -35.851 57.165 9.370 1.00116.25 C ANISOU 880 CZ ARG A 118 14682 17511 11976 1423 1529 -78 C ATOM 881 NH1 ARG A 118 -36.412 56.624 8.298 1.00114.24 N ANISOU 881 NH1 ARG A 118 14156 17131 12119 1415 1496 14 N ATOM 882 NH2 ARG A 118 -35.828 58.483 9.509 1.00116.45 N ANISOU 882 NH2 ARG A 118 14690 17521 12034 1401 1497 -301 N ATOM 883 N LEU A 119 -31.103 56.576 8.481 1.00108.12 N ANISOU 883 N LEU A 119 13867 17000 10214 1475 300 213 N ATOM 884 CA LEU A 119 -30.960 57.433 7.309 1.00104.80 C ANISOU 884 CA LEU A 119 13224 16469 10126 1435 116 93 C ATOM 885 C LEU A 119 -29.736 57.042 6.491 1.00102.03 C ANISOU 885 C LEU A 119 12814 16148 9805 1433 -194 210 C ATOM 886 O LEU A 119 -29.797 56.958 5.265 1.00 99.83 O ANISOU 886 O LEU A 119 12363 15743 9823 1407 -278 258 O ATOM 887 CB LEU A 119 -30.856 58.900 7.723 1.00105.65 C ANISOU 887 CB LEU A 119 13358 16589 10195 1408 100 -186 C ATOM 888 CG LEU A 119 -32.120 59.525 8.312 1.00108.24 C ANISOU 888 CG LEU A 119 13692 16822 10611 1395 433 -342 C ATOM 889 CD1 LEU A 119 -31.895 61.001 8.612 1.00109.06 C ANISOU 889 CD1 LEU A 119 13804 16913 10719 1357 422 -628 C ATOM 890 CD2 LEU A 119 -33.297 59.334 7.366 1.00106.99 C ANISOU 890 CD2 LEU A 119 13290 16466 10898 1401 569 -271 C ATOM 891 N PHE A 120 -28.626 56.806 7.182 1.00102.14 N ANISOU 891 N PHE A 120 12974 16326 9508 1461 -364 250 N ATOM 892 CA PHE A 120 -27.387 56.403 6.535 1.00100.53 C ANISOU 892 CA PHE A 120 12707 16137 9354 1463 -637 359 C ATOM 893 C PHE A 120 -27.583 55.117 5.737 1.00 98.56 C ANISOU 893 C PHE A 120 12373 15784 9290 1464 -568 610 C ATOM 894 O PHE A 120 -27.012 54.953 4.659 1.00 96.58 O ANISOU 894 O PHE A 120 12001 15436 9260 1428 -706 658 O ATOM 895 CB PHE A 120 -26.283 56.219 7.577 1.00104.04 C ANISOU 895 CB PHE A 120 13307 16791 9432 1512 -826 385 C ATOM 896 CG PHE A 120 -24.943 55.895 6.989 1.00104.69 C ANISOU 896 CG PHE A 120 13292 16872 9615 1517 -1107 472 C ATOM 897 CD1 PHE A 120 -24.147 56.896 6.459 1.00105.11 C ANISOU 897 CD1 PHE A 120 13230 16875 9832 1466 -1304 267 C ATOM 898 CD2 PHE A 120 -24.477 54.593 6.969 1.00106.40 C ANISOU 898 CD2 PHE A 120 13522 17106 9800 1573 -1138 758 C ATOM 899 CE1 PHE A 120 -22.910 56.603 5.915 1.00105.48 C ANISOU 899 CE1 PHE A 120 13173 16885 10018 1464 -1526 334 C ATOM 900 CE2 PHE A 120 -23.242 54.293 6.427 1.00107.31 C ANISOU 900 CE2 PHE A 120 13526 17188 10057 1575 -1369 835 C ATOM 901 CZ PHE A 120 -22.457 55.301 5.900 1.00106.41 C ANISOU 901 CZ PHE A 120 13294 17021 10115 1517 -1563 617 C ATOM 902 N GLN A 121 -28.400 54.213 6.270 1.00 99.04 N ANISOU 902 N GLN A 121 12509 15850 9272 1495 -320 754 N ATOM 903 CA GLN A 121 -28.694 52.953 5.599 1.00 97.08 C ANISOU 903 CA GLN A 121 12176 15491 9219 1481 -197 963 C ATOM 904 C GLN A 121 -29.426 53.195 4.286 1.00 94.09 C ANISOU 904 C GLN A 121 11590 14945 9213 1401 -174 877 C ATOM 905 O GLN A 121 -29.024 52.692 3.237 1.00 92.82 O ANISOU 905 O GLN A 121 11328 14698 9241 1352 -267 954 O ATOM 906 CB GLN A 121 -29.531 52.048 6.503 1.00100.30 C ANISOU 906 CB GLN A 121 12704 15908 9495 1529 124 1103 C ATOM 907 CG GLN A 121 -28.759 51.436 7.657 1.00104.95 C ANISOU 907 CG GLN A 121 13521 16655 9701 1631 100 1288 C ATOM 908 CD GLN A 121 -29.667 50.815 8.702 1.00110.48 C ANISOU 908 CD GLN A 121 14402 17358 10216 1689 462 1396 C ATOM 909 OE1 GLN A 121 -30.890 50.940 8.633 1.00111.59 O ANISOU 909 OE1 GLN A 121 14482 17377 10541 1643 743 1294 O ATOM 910 NE2 GLN A 121 -29.070 50.141 9.679 1.00113.45 N ANISOU 910 NE2 GLN A 121 15002 17865 10239 1799 465 1613 N ATOM 911 N GLN A 122 -30.500 53.973 4.354 1.00 93.95 N ANISOU 911 N GLN A 122 11515 14881 9299 1388 -51 715 N ATOM 912 CA GLN A 122 -31.307 54.273 3.178 1.00 91.77 C ANISOU 912 CA GLN A 122 11036 14468 9364 1334 -59 639 C ATOM 913 C GLN A 122 -30.508 55.045 2.136 1.00 89.14 C ANISOU 913 C GLN A 122 10644 14096 9128 1309 -333 574 C ATOM 914 O GLN A 122 -30.568 54.738 0.945 1.00 86.99 O ANISOU 914 O GLN A 122 10266 13734 9053 1258 -413 616 O ATOM 915 CB GLN A 122 -32.547 55.070 3.578 1.00 92.75 C ANISOU 915 CB GLN A 122 11095 14544 9600 1348 117 484 C ATOM 916 CG GLN A 122 -33.446 54.348 4.562 1.00 96.02 C ANISOU 916 CG GLN A 122 11569 14951 9964 1366 451 531 C ATOM 917 CD GLN A 122 -34.629 55.190 4.985 1.00 99.65 C ANISOU 917 CD GLN A 122 11954 15332 10575 1374 656 361 C ATOM 918 OE1 GLN A 122 -34.688 56.386 4.698 1.00 99.84 O ANISOU 918 OE1 GLN A 122 11905 15328 10702 1380 543 214 O ATOM 919 NE2 GLN A 122 -35.582 54.569 5.670 1.00102.44 N ANISOU 919 NE2 GLN A 122 12320 15624 10980 1377 995 384 N ATOM 920 N ILE A 123 -29.764 56.048 2.592 1.00 88.76 N ANISOU 920 N ILE A 123 10677 14109 8939 1337 -456 457 N ATOM 921 CA ILE A 123 -28.921 56.838 1.705 1.00 87.14 C ANISOU 921 CA ILE A 123 10433 13841 8837 1318 -668 387 C ATOM 922 C ILE A 123 -27.914 55.951 0.988 1.00 87.20 C ANISOU 922 C ILE A 123 10446 13816 8869 1280 -789 532 C ATOM 923 O ILE A 123 -27.769 56.026 -0.233 1.00 87.69 O ANISOU 923 O ILE A 123 10447 13761 9112 1236 -868 546 O ATOM 924 CB ILE A 123 -28.169 57.942 2.469 1.00 87.98 C ANISOU 924 CB ILE A 123 10617 14016 8793 1341 -753 215 C ATOM 925 CG1 ILE A 123 -29.144 59.023 2.939 1.00 89.47 C ANISOU 925 CG1 ILE A 123 10782 14180 9032 1360 -609 38 C ATOM 926 CG2 ILE A 123 -27.095 58.560 1.591 1.00 86.28 C ANISOU 926 CG2 ILE A 123 10367 13712 8704 1317 -940 160 C ATOM 927 CD1 ILE A 123 -28.491 60.121 3.750 1.00 90.68 C ANISOU 927 CD1 ILE A 123 11013 14397 9043 1360 -651 -175 C ATOM 928 N LEU A 124 -27.232 55.101 1.750 1.00 87.02 N ANISOU 928 N LEU A 124 10508 13891 8666 1302 -790 650 N ATOM 929 CA LEU A 124 -26.228 54.205 1.190 1.00 86.11 C ANISOU 929 CA LEU A 124 10383 13727 8608 1273 -873 800 C ATOM 930 C LEU A 124 -26.849 53.231 0.191 1.00 84.84 C ANISOU 930 C LEU A 124 10147 13449 8638 1205 -754 911 C ATOM 931 O LEU A 124 -26.233 52.891 -0.820 1.00 82.81 O ANISOU 931 O LEU A 124 9859 13081 8523 1142 -813 957 O ATOM 932 CB LEU A 124 -25.508 53.439 2.301 1.00 88.84 C ANISOU 932 CB LEU A 124 10821 14204 8731 1337 -890 939 C ATOM 933 CG LEU A 124 -24.243 52.680 1.888 1.00 88.89 C ANISOU 933 CG LEU A 124 10795 14155 8825 1328 -1001 1085 C ATOM 934 CD1 LEU A 124 -23.169 53.644 1.400 1.00 87.84 C ANISOU 934 CD1 LEU A 124 10613 13966 8796 1300 -1209 935 C ATOM 935 CD2 LEU A 124 -23.723 51.829 3.032 1.00 90.57 C ANISOU 935 CD2 LEU A 124 11090 14503 8819 1423 -1013 1272 C ATOM 936 N SER A 125 -28.071 52.791 0.482 1.00 86.22 N ANISOU 936 N SER A 125 10293 13639 8830 1207 -568 932 N ATOM 937 CA SER A 125 -28.798 51.882 -0.398 1.00 85.23 C ANISOU 937 CA SER A 125 10070 13413 8902 1129 -449 989 C ATOM 938 C SER A 125 -28.934 52.466 -1.799 1.00 83.26 C ANISOU 938 C SER A 125 9746 13067 8824 1060 -589 892 C ATOM 939 O SER A 125 -28.789 51.758 -2.796 1.00 81.30 O ANISOU 939 O SER A 125 9467 12732 8693 971 -587 938 O ATOM 940 CB SER A 125 -30.183 51.575 0.180 1.00 85.36 C ANISOU 940 CB SER A 125 10030 13445 8958 1143 -226 969 C ATOM 941 OG SER A 125 -30.939 50.766 -0.705 1.00 84.07 O ANISOU 941 OG SER A 125 9736 13188 9020 1052 -129 977 O ATOM 942 N GLY A 126 -29.205 53.766 -1.863 1.00 83.98 N ANISOU 942 N GLY A 126 9823 13165 8918 1104 -693 760 N ATOM 943 CA GLY A 126 -29.332 54.461 -3.129 1.00 83.60 C ANISOU 943 CA GLY A 126 9738 13029 8999 1073 -831 695 C ATOM 944 C GLY A 126 -27.988 54.642 -3.803 1.00 82.82 C ANISOU 944 C GLY A 126 9731 12850 8886 1040 -947 717 C ATOM 945 O GLY A 126 -27.875 54.518 -5.023 1.00 81.39 O ANISOU 945 O GLY A 126 9567 12572 8787 973 -1003 731 O ATOM 946 N VAL A 127 -26.968 54.941 -3.004 1.00 84.23 N ANISOU 946 N VAL A 127 9972 13066 8964 1083 -980 707 N ATOM 947 CA VAL A 127 -25.609 55.074 -3.513 1.00 86.19 C ANISOU 947 CA VAL A 127 10278 13219 9252 1052 -1065 715 C ATOM 948 C VAL A 127 -25.178 53.769 -4.173 1.00 87.52 C ANISOU 948 C VAL A 127 10454 13308 9493 963 -1001 846 C ATOM 949 O VAL A 127 -24.609 53.769 -5.267 1.00 86.95 O ANISOU 949 O VAL A 127 10425 13091 9521 892 -1018 847 O ATOM 950 CB VAL A 127 -24.614 55.430 -2.389 1.00 87.69 C ANISOU 950 CB VAL A 127 10490 13490 9336 1109 -1131 672 C ATOM 951 CG1 VAL A 127 -23.199 55.519 -2.937 1.00 86.76 C ANISOU 951 CG1 VAL A 127 10385 13246 9333 1072 -1208 667 C ATOM 952 CG2 VAL A 127 -25.006 56.737 -1.724 1.00 88.44 C ANISOU 952 CG2 VAL A 127 10585 13652 9367 1173 -1162 504 C ATOM 953 N ASP A 128 -25.465 52.660 -3.499 1.00 89.16 N ANISOU 953 N ASP A 128 10633 13589 9655 965 -889 957 N ATOM 954 CA ASP A 128 -25.203 51.331 -4.035 1.00 88.59 C ANISOU 954 CA ASP A 128 10550 13428 9682 878 -772 1081 C ATOM 955 C ASP A 128 -25.909 51.151 -5.371 1.00 85.82 C ANISOU 955 C ASP A 128 10188 12984 9435 766 -743 1027 C ATOM 956 O ASP A 128 -25.300 50.733 -6.354 1.00 85.28 O ANISOU 956 O ASP A 128 10165 12781 9458 666 -715 1044 O ATOM 957 CB ASP A 128 -25.679 50.264 -3.049 1.00 91.69 C ANISOU 957 CB ASP A 128 10912 13905 10020 915 -612 1207 C ATOM 958 CG ASP A 128 -25.431 48.854 -3.548 1.00 93.09 C ANISOU 958 CG ASP A 128 11064 13967 10340 825 -442 1336 C ATOM 959 OD1 ASP A 128 -24.332 48.594 -4.086 1.00 92.11 O ANISOU 959 OD1 ASP A 128 10958 13724 10317 779 -461 1385 O ATOM 960 OD2 ASP A 128 -26.338 48.007 -3.404 1.00 94.19 O ANISOU 960 OD2 ASP A 128 11154 14111 10525 795 -259 1377 O ATOM 961 N TYR A 129 -27.195 51.486 -5.392 1.00 84.69 N ANISOU 961 N TYR A 129 9985 12914 9281 782 -754 952 N ATOM 962 CA TYR A 129 -28.022 51.367 -6.586 1.00 82.64 C ANISOU 962 CA TYR A 129 9693 12610 9098 689 -783 887 C ATOM 963 C TYR A 129 -27.433 52.150 -7.756 1.00 80.43 C ANISOU 963 C TYR A 129 9525 12228 8806 658 -919 842 C ATOM 964 O TYR A 129 -27.475 51.697 -8.900 1.00 80.10 O ANISOU 964 O TYR A 129 9534 12110 8789 544 -919 827 O ATOM 965 CB TYR A 129 -29.445 51.848 -6.288 1.00 82.64 C ANISOU 965 CB TYR A 129 9574 12704 9122 747 -814 808 C ATOM 966 CG TYR A 129 -30.435 51.602 -7.405 1.00 82.56 C ANISOU 966 CG TYR A 129 9483 12682 9202 659 -879 737 C ATOM 967 CD1 TYR A 129 -31.050 50.366 -7.553 1.00 82.57 C ANISOU 967 CD1 TYR A 129 9383 12680 9308 550 -742 722 C ATOM 968 CD2 TYR A 129 -30.765 52.608 -8.305 1.00 83.31 C ANISOU 968 CD2 TYR A 129 9600 12771 9283 690 -1080 681 C ATOM 969 CE1 TYR A 129 -31.959 50.135 -8.568 1.00 83.77 C ANISOU 969 CE1 TYR A 129 9443 12843 9543 457 -834 621 C ATOM 970 CE2 TYR A 129 -31.673 52.386 -9.325 1.00 84.41 C ANISOU 970 CE2 TYR A 129 9667 12931 9476 619 -1193 619 C ATOM 971 CZ TYR A 129 -32.267 51.147 -9.452 1.00 84.69 C ANISOU 971 CZ TYR A 129 9586 12983 9609 495 -1084 572 C ATOM 972 OH TYR A 129 -33.172 50.918 -10.465 1.00 86.20 O ANISOU 972 OH TYR A 129 9686 13212 9852 411 -1227 474 O ATOM 973 N CYS A 130 -26.879 53.322 -7.464 1.00 78.35 N ANISOU 973 N CYS A 130 9315 11955 8502 754 -1011 812 N ATOM 974 CA CYS A 130 -26.273 54.152 -8.496 1.00 76.90 C ANISOU 974 CA CYS A 130 9255 11643 8322 742 -1092 781 C ATOM 975 C CYS A 130 -25.026 53.495 -9.068 1.00 75.37 C ANISOU 975 C CYS A 130 9161 11297 8180 640 -1002 826 C ATOM 976 O CYS A 130 -24.836 53.458 -10.285 1.00 74.44 O ANISOU 976 O CYS A 130 9166 11057 8061 554 -991 818 O ATOM 977 CB CYS A 130 -25.925 55.534 -7.940 1.00 77.39 C ANISOU 977 CB CYS A 130 9327 11701 8377 863 -1159 720 C ATOM 978 SG CYS A 130 -27.343 56.616 -7.686 1.00105.53 S ANISOU 978 SG CYS A 130 12798 15360 11938 980 -1243 658 S ATOM 979 N HIS A 131 -24.181 52.976 -8.181 1.00 75.49 N ANISOU 979 N HIS A 131 9128 11314 8240 653 -932 878 N ATOM 980 CA HIS A 131 -22.916 52.368 -8.581 1.00 75.53 C ANISOU 980 CA HIS A 131 9184 11153 8361 572 -833 928 C ATOM 981 C HIS A 131 -23.136 51.056 -9.327 1.00 78.44 C ANISOU 981 C HIS A 131 9572 11451 8783 428 -686 978 C ATOM 982 O HIS A 131 -22.349 50.691 -10.204 1.00 80.15 O ANISOU 982 O HIS A 131 9879 11480 9094 320 -578 983 O ATOM 983 CB HIS A 131 -22.022 52.135 -7.365 1.00 73.67 C ANISOU 983 CB HIS A 131 8858 10962 8171 647 -838 987 C ATOM 984 CG HIS A 131 -21.628 53.391 -6.647 1.00 72.20 C ANISOU 984 CG HIS A 131 8653 10835 7945 757 -975 893 C ATOM 985 ND1 HIS A 131 -20.862 53.383 -5.506 1.00 71.66 N ANISOU 985 ND1 HIS A 131 8507 10848 7873 832 -1044 910 N ATOM 986 CD2 HIS A 131 -21.901 54.691 -6.916 1.00 71.44 C ANISOU 986 CD2 HIS A 131 8602 10724 7819 801 -1050 774 C ATOM 987 CE1 HIS A 131 -20.677 54.630 -5.095 1.00 71.72 C ANISOU 987 CE1 HIS A 131 8509 10894 7847 898 -1154 770 C ATOM 988 NE2 HIS A 131 -21.297 55.437 -5.931 1.00 71.73 N ANISOU 988 NE2 HIS A 131 8581 10823 7851 883 -1137 693 N ATOM 989 N ARG A 132 -24.206 50.351 -8.973 1.00 78.50 N ANISOU 989 N ARG A 132 9490 11587 8751 417 -650 997 N ATOM 990 CA ARG A 132 -24.569 49.119 -9.661 1.00 79.44 C ANISOU 990 CA ARG A 132 9604 11644 8937 266 -496 1005 C ATOM 991 C ARG A 132 -24.974 49.412 -11.101 1.00 76.74 C ANISOU 991 C ARG A 132 9386 11243 8528 153 -556 898 C ATOM 992 O ARG A 132 -24.846 48.561 -11.979 1.00 76.98 O ANISOU 992 O ARG A 132 9480 11165 8603 -9 -424 869 O ATOM 993 CB ARG A 132 -25.703 48.402 -8.924 1.00 84.99 C ANISOU 993 CB ARG A 132 10165 12484 9644 283 -428 1022 C ATOM 994 CG ARG A 132 -25.299 47.807 -7.583 1.00 90.16 C ANISOU 994 CG ARG A 132 10743 13179 10334 380 -315 1164 C ATOM 995 CD ARG A 132 -26.499 47.227 -6.848 1.00 96.35 C ANISOU 995 CD ARG A 132 11416 14075 11118 408 -208 1178 C ATOM 996 NE ARG A 132 -26.389 45.781 -6.672 1.00102.45 N ANISOU 996 NE ARG A 132 12137 14759 12032 340 56 1285 N ATOM 997 CZ ARG A 132 -25.831 45.195 -5.616 1.00107.18 C ANISOU 997 CZ ARG A 132 12725 15358 12642 440 176 1467 C ATOM 998 NH1 ARG A 132 -25.325 45.929 -4.633 1.00108.31 N ANISOU 998 NH1 ARG A 132 12908 15611 12633 600 27 1537 N ATOM 999 NH2 ARG A 132 -25.777 43.872 -5.542 1.00109.46 N ANISOU 999 NH2 ARG A 132 12965 15536 13091 383 447 1579 N ATOM 1000 N HIS A 133 -25.460 50.625 -11.337 1.00 75.86 N ANISOU 1000 N HIS A 133 9319 11202 8302 242 -748 844 N ATOM 1001 CA HIS A 133 -25.844 51.041 -12.679 1.00 76.96 C ANISOU 1001 CA HIS A 133 9604 11306 8333 174 -847 776 C ATOM 1002 C HIS A 133 -24.743 51.864 -13.327 1.00 76.25 C ANISOU 1002 C HIS A 133 9714 11037 8218 186 -833 788 C ATOM 1003 O HIS A 133 -24.994 52.606 -14.276 1.00 77.83 O ANISOU 1003 O HIS A 133 10072 11209 8292 195 -936 764 O ATOM 1004 CB HIS A 133 -27.148 51.840 -12.648 1.00 78.03 C ANISOU 1004 CB HIS A 133 9658 11607 8385 278 -1061 734 C ATOM 1005 CG HIS A 133 -28.333 51.041 -12.203 1.00 79.52 C ANISOU 1005 CG HIS A 133 9643 11936 8635 245 -1055 691 C ATOM 1006 ND1 HIS A 133 -28.434 50.500 -10.939 1.00 79.97 N ANISOU 1006 ND1 HIS A 133 9545 12047 8793 291 -924 731 N ATOM 1007 CD2 HIS A 133 -29.465 50.686 -12.855 1.00 81.52 C ANISOU 1007 CD2 HIS A 133 9820 12278 8874 171 -1156 604 C ATOM 1008 CE1 HIS A 133 -29.577 49.849 -10.831 1.00 81.07 C ANISOU 1008 CE1 HIS A 133 9524 12275 9003 243 -901 671 C ATOM 1009 NE2 HIS A 133 -30.223 49.947 -11.980 1.00 82.64 N ANISOU 1009 NE2 HIS A 133 9746 12502 9154 165 -1053 579 N ATOM 1010 N MET A 134 -23.528 51.724 -12.804 1.00 73.79 N ANISOU 1010 N MET A 134 9393 10600 8044 193 -701 832 N ATOM 1011 CA MET A 134 -22.356 52.410 -13.342 1.00 71.70 C ANISOU 1011 CA MET A 134 9286 10123 7835 191 -631 826 C ATOM 1012 C MET A 134 -22.520 53.927 -13.331 1.00 69.74 C ANISOU 1012 C MET A 134 9090 9890 7517 336 -773 801 C ATOM 1013 O MET A 134 -22.018 54.625 -14.210 1.00 68.87 O ANISOU 1013 O MET A 134 9172 9607 7389 329 -725 789 O ATOM 1014 CB MET A 134 -22.048 51.914 -14.758 1.00 71.33 C ANISOU 1014 CB MET A 134 9461 9895 7747 19 -488 800 C ATOM 1015 CG MET A 134 -21.842 50.416 -14.841 1.00 70.45 C ANISOU 1015 CG MET A 134 9298 9725 7746 -144 -295 806 C ATOM 1016 SD MET A 134 -20.453 49.875 -13.831 1.00106.95 S ANISOU 1016 SD MET A 134 13756 14204 12675 -115 -124 891 S ATOM 1017 CE MET A 134 -19.075 50.545 -14.759 1.00 61.81 C ANISOU 1017 CE MET A 134 8243 8158 7085 -170 36 852 C ATOM 1018 N VAL A 135 -23.230 54.433 -12.330 1.00 68.69 N ANISOU 1018 N VAL A 135 8797 9944 7358 468 -912 794 N ATOM 1019 CA VAL A 135 -23.449 55.866 -12.212 1.00 69.37 C ANISOU 1019 CA VAL A 135 8902 10037 7417 608 -1016 763 C ATOM 1020 C VAL A 135 -22.928 56.387 -10.885 1.00 70.09 C ANISOU 1020 C VAL A 135 8849 10176 7607 705 -1026 719 C ATOM 1021 O VAL A 135 -23.495 56.108 -9.831 1.00 71.05 O ANISOU 1021 O VAL A 135 8819 10480 7698 753 -1079 717 O ATOM 1022 CB VAL A 135 -24.940 56.226 -12.331 1.00 68.67 C ANISOU 1022 CB VAL A 135 8759 10118 7213 681 -1178 768 C ATOM 1023 CG1 VAL A 135 -25.154 57.703 -12.031 1.00 68.75 C ANISOU 1023 CG1 VAL A 135 8754 10118 7249 839 -1248 747 C ATOM 1024 CG2 VAL A 135 -25.460 55.877 -13.712 1.00 69.46 C ANISOU 1024 CG2 VAL A 135 9015 10194 7182 594 -1228 793 C ATOM 1025 N VAL A 136 -21.839 57.141 -10.937 1.00 69.99 N ANISOU 1025 N VAL A 136 8889 9992 7711 726 -963 669 N ATOM 1026 CA VAL A 136 -21.340 57.798 -9.742 1.00 71.27 C ANISOU 1026 CA VAL A 136 8917 10207 7957 811 -1001 583 C ATOM 1027 C VAL A 136 -22.044 59.147 -9.602 1.00 76.75 C ANISOU 1027 C VAL A 136 9609 10933 8620 927 -1059 519 C ATOM 1028 O VAL A 136 -22.458 59.748 -10.595 1.00 78.92 O ANISOU 1028 O VAL A 136 10013 11106 8869 955 -1046 555 O ATOM 1029 CB VAL A 136 -19.808 57.968 -9.783 1.00 68.89 C ANISOU 1029 CB VAL A 136 8618 9698 7857 770 -905 523 C ATOM 1030 CG1 VAL A 136 -19.410 59.055 -10.767 1.00 68.49 C ANISOU 1030 CG1 VAL A 136 8722 9401 7899 781 -798 473 C ATOM 1031 CG2 VAL A 136 -19.276 58.283 -8.406 1.00 69.49 C ANISOU 1031 CG2 VAL A 136 8520 9890 7994 832 -993 425 C ATOM 1032 N HIS A 137 -22.205 59.610 -8.368 1.00 78.05 N ANISOU 1032 N HIS A 137 9638 11238 8781 1000 -1115 431 N ATOM 1033 CA HIS A 137 -22.892 60.868 -8.111 1.00 79.29 C ANISOU 1033 CA HIS A 137 9769 11413 8946 1104 -1132 355 C ATOM 1034 C HIS A 137 -22.002 61.818 -7.324 1.00 86.66 C ANISOU 1034 C HIS A 137 10639 12288 9999 1132 -1096 183 C ATOM 1035 O HIS A 137 -21.958 61.760 -6.098 1.00 91.74 O ANISOU 1035 O HIS A 137 11174 13096 10586 1144 -1150 91 O ATOM 1036 CB HIS A 137 -24.185 60.608 -7.334 1.00 74.54 C ANISOU 1036 CB HIS A 137 9059 11034 8230 1152 -1198 373 C ATOM 1037 CG HIS A 137 -24.844 61.851 -6.813 1.00 71.55 C ANISOU 1037 CG HIS A 137 8617 10671 7897 1254 -1183 275 C ATOM 1038 ND1 HIS A 137 -24.370 62.543 -5.723 1.00 69.97 N ANISOU 1038 ND1 HIS A 137 8354 10503 7726 1275 -1148 111 N ATOM 1039 CD2 HIS A 137 -25.951 62.510 -7.229 1.00 72.11 C ANISOU 1039 CD2 HIS A 137 8668 10724 8006 1337 -1193 314 C ATOM 1040 CE1 HIS A 137 -25.151 63.587 -5.493 1.00 71.07 C ANISOU 1040 CE1 HIS A 137 8447 10625 7931 1357 -1098 43 C ATOM 1041 NE2 HIS A 137 -26.116 63.587 -6.390 1.00 71.95 N ANISOU 1041 NE2 HIS A 137 8574 10700 8065 1406 -1125 179 N ATOM 1042 N ARG A 138 -21.296 62.702 -8.016 1.00 87.03 N ANISOU 1042 N ARG A 138 10762 12098 10207 1139 -995 127 N ATOM 1043 CA ARG A 138 -20.503 63.704 -7.317 1.00 86.25 C ANISOU 1043 CA ARG A 138 10580 11924 10267 1155 -944 -78 C ATOM 1044 C ARG A 138 -21.444 64.724 -6.677 1.00 89.99 C ANISOU 1044 C ARG A 138 10992 12479 10720 1245 -933 -170 C ATOM 1045 O ARG A 138 -22.626 64.781 -7.024 1.00 92.93 O ANISOU 1045 O ARG A 138 11394 12904 11011 1309 -950 -51 O ATOM 1046 CB ARG A 138 -19.500 64.374 -8.259 1.00 83.21 C ANISOU 1046 CB ARG A 138 10289 11219 10109 1134 -781 -123 C ATOM 1047 CG ARG A 138 -18.271 63.516 -8.586 1.00 78.90 C ANISOU 1047 CG ARG A 138 9749 10556 9675 1030 -750 -110 C ATOM 1048 CD ARG A 138 -18.540 62.486 -9.681 1.00 72.91 C ANISOU 1048 CD ARG A 138 9149 9751 8801 978 -724 99 C ATOM 1049 NE ARG A 138 -18.732 63.110 -10.988 1.00 70.97 N ANISOU 1049 NE ARG A 138 9120 9275 8569 1004 -577 181 N ATOM 1050 CZ ARG A 138 -17.769 63.281 -11.890 1.00 68.89 C ANISOU 1050 CZ ARG A 138 8994 8708 8472 950 -377 175 C ATOM 1051 NH1 ARG A 138 -16.534 62.870 -11.634 1.00 68.28 N ANISOU 1051 NH1 ARG A 138 8819 8510 8616 861 -306 78 N ATOM 1052 NH2 ARG A 138 -18.040 63.862 -13.052 1.00 67.81 N ANISOU 1052 NH2 ARG A 138 9098 8379 8288 992 -243 275 N ATOM 1053 N ASP A 139 -20.921 65.508 -5.737 1.00 90.50 N ANISOU 1053 N ASP A 139 10956 12551 10877 1241 -905 -396 N ATOM 1054 CA ASP A 139 -21.726 66.449 -4.949 1.00 91.12 C ANISOU 1054 CA ASP A 139 10967 12705 10950 1302 -859 -526 C ATOM 1055 C ASP A 139 -22.787 65.722 -4.122 1.00 85.43 C ANISOU 1055 C ASP A 139 10205 12259 9996 1317 -957 -462 C ATOM 1056 O ASP A 139 -23.965 66.072 -4.147 1.00 81.97 O ANISOU 1056 O ASP A 139 9752 11844 9550 1386 -911 -408 O ATOM 1057 CB ASP A 139 -22.368 67.522 -5.837 1.00 95.12 C ANISOU 1057 CB ASP A 139 11533 12997 11611 1398 -711 -463 C ATOM 1058 CG ASP A 139 -22.765 68.764 -5.061 1.00100.32 C ANISOU 1058 CG ASP A 139 12101 13626 12391 1444 -583 -661 C ATOM 1059 OD1 ASP A 139 -22.161 69.023 -3.996 1.00102.39 O ANISOU 1059 OD1 ASP A 139 12277 13968 12658 1376 -582 -913 O ATOM 1060 OD2 ASP A 139 -23.678 69.485 -5.518 1.00102.04 O ANISOU 1060 OD2 ASP A 139 12329 13737 12703 1549 -487 -570 O ATOM 1061 N LEU A 140 -22.345 64.709 -3.386 1.00 84.53 N ANISOU 1061 N LEU A 140 10065 12332 9719 1259 -1077 -459 N ATOM 1062 CA LEU A 140 -23.223 63.912 -2.542 1.00 81.81 C ANISOU 1062 CA LEU A 140 9705 12229 9150 1270 -1132 -391 C ATOM 1063 C LEU A 140 -23.213 64.465 -1.117 1.00 80.68 C ANISOU 1063 C LEU A 140 9523 12238 8894 1266 -1124 -612 C ATOM 1064 O LEU A 140 -22.496 63.966 -0.252 1.00 79.20 O ANISOU 1064 O LEU A 140 9331 12207 8554 1229 -1235 -673 O ATOM 1065 CB LEU A 140 -22.752 62.456 -2.554 1.00 81.31 C ANISOU 1065 CB LEU A 140 9661 12267 8965 1224 -1236 -231 C ATOM 1066 CG LEU A 140 -23.668 61.367 -1.993 1.00 81.51 C ANISOU 1066 CG LEU A 140 9690 12487 8792 1234 -1248 -92 C ATOM 1067 CD1 LEU A 140 -24.952 61.273 -2.801 1.00 80.75 C ANISOU 1067 CD1 LEU A 140 9592 12341 8749 1262 -1184 28 C ATOM 1068 CD2 LEU A 140 -22.949 60.022 -1.962 1.00 80.13 C ANISOU 1068 CD2 LEU A 140 9526 12372 8547 1193 -1321 54 C ATOM 1069 N LYS A 141 -24.008 65.503 -0.882 1.00 82.52 N ANISOU 1069 N LYS A 141 9732 12422 9200 1305 -992 -730 N ATOM 1070 CA LYS A 141 -24.022 66.187 0.410 1.00 86.30 C ANISOU 1070 CA LYS A 141 10194 13014 9584 1281 -939 -984 C ATOM 1071 C LYS A 141 -25.434 66.226 1.005 1.00 90.23 C ANISOU 1071 C LYS A 141 10695 13596 9993 1320 -809 -966 C ATOM 1072 O LYS A 141 -26.416 66.039 0.284 1.00 91.74 O ANISOU 1072 O LYS A 141 10856 13711 10290 1378 -757 -787 O ATOM 1073 CB LYS A 141 -23.466 67.607 0.253 1.00 85.22 C ANISOU 1073 CB LYS A 141 10008 12680 9691 1267 -827 -1224 C ATOM 1074 CG LYS A 141 -24.214 68.451 -0.763 1.00 84.75 C ANISOU 1074 CG LYS A 141 9929 12375 9898 1347 -659 -1136 C ATOM 1075 CD LYS A 141 -23.579 69.820 -0.926 1.00 86.66 C ANISOU 1075 CD LYS A 141 10129 12389 10411 1337 -504 -1360 C ATOM 1076 CE LYS A 141 -24.330 70.654 -1.952 1.00 87.13 C ANISOU 1076 CE LYS A 141 10184 12192 10728 1448 -333 -1222 C ATOM 1077 NZ LYS A 141 -23.685 71.976 -2.183 1.00 88.97 N ANISOU 1077 NZ LYS A 141 10385 12158 11261 1448 -130 -1416 N ATOM 1078 N PRO A 142 -25.541 66.453 2.328 1.00 91.47 N ANISOU 1078 N PRO A 142 10887 13909 9957 1283 -757 -1162 N ATOM 1079 CA PRO A 142 -26.830 66.572 3.023 1.00 91.56 C ANISOU 1079 CA PRO A 142 10911 13972 9906 1306 -574 -1186 C ATOM 1080 C PRO A 142 -27.817 67.575 2.412 1.00 91.65 C ANISOU 1080 C PRO A 142 10821 13761 10242 1368 -380 -1194 C ATOM 1081 O PRO A 142 -29.002 67.522 2.738 1.00 92.77 O ANISOU 1081 O PRO A 142 10932 13905 10413 1400 -230 -1158 O ATOM 1082 CB PRO A 142 -26.433 67.022 4.440 1.00 93.83 C ANISOU 1082 CB PRO A 142 11281 14415 9955 1234 -535 -1475 C ATOM 1083 CG PRO A 142 -24.923 67.089 4.459 1.00 94.02 C ANISOU 1083 CG PRO A 142 11304 14490 9931 1180 -747 -1596 C ATOM 1084 CD PRO A 142 -24.435 66.315 3.287 1.00 91.99 C ANISOU 1084 CD PRO A 142 11001 14149 9800 1216 -898 -1336 C ATOM 1085 N GLU A 143 -27.343 68.474 1.555 1.00 90.96 N ANISOU 1085 N GLU A 143 10678 13467 10415 1392 -366 -1232 N ATOM 1086 CA GLU A 143 -28.236 69.392 0.853 1.00 91.36 C ANISOU 1086 CA GLU A 143 10633 13294 10786 1483 -204 -1179 C ATOM 1087 C GLU A 143 -28.878 68.731 -0.369 1.00 88.19 C ANISOU 1087 C GLU A 143 10195 12841 10472 1569 -321 -862 C ATOM 1088 O GLU A 143 -29.903 69.193 -0.865 1.00 87.84 O ANISOU 1088 O GLU A 143 10056 12672 10649 1663 -239 -762 O ATOM 1089 CB GLU A 143 -27.504 70.673 0.443 1.00 93.14 C ANISOU 1089 CB GLU A 143 10831 13294 11262 1489 -100 -1334 C ATOM 1090 CG GLU A 143 -27.438 71.738 1.528 1.00 96.24 C ANISOU 1090 CG GLU A 143 11202 13656 11711 1424 117 -1677 C ATOM 1091 CD GLU A 143 -26.138 71.708 2.309 1.00 97.28 C ANISOU 1091 CD GLU A 143 11391 13924 11646 1296 17 -1945 C ATOM 1092 OE1 GLU A 143 -25.476 70.651 2.329 1.00 95.35 O ANISOU 1092 OE1 GLU A 143 11206 13858 11165 1262 -224 -1845 O ATOM 1093 OE2 GLU A 143 -25.776 72.745 2.903 1.00100.42 O ANISOU 1093 OE2 GLU A 143 11760 14246 12149 1227 178 -2263 O ATOM 1094 N ASN A 144 -28.269 67.652 -0.851 1.00 86.19 N ANISOU 1094 N ASN A 144 10009 12683 10056 1534 -515 -714 N ATOM 1095 CA ASN A 144 -28.811 66.911 -1.986 1.00 84.25 C ANISOU 1095 CA ASN A 144 9748 12416 9848 1583 -636 -450 C ATOM 1096 C ASN A 144 -29.629 65.702 -1.546 1.00 82.53 C ANISOU 1096 C ASN A 144 9501 12377 9480 1559 -671 -352 C ATOM 1097 O ASN A 144 -30.155 64.957 -2.371 1.00 81.07 O ANISOU 1097 O ASN A 144 9284 12201 9317 1576 -771 -168 O ATOM 1098 CB ASN A 144 -27.694 66.479 -2.940 1.00 83.87 C ANISOU 1098 CB ASN A 144 9795 12312 9759 1548 -774 -351 C ATOM 1099 CG ASN A 144 -27.076 67.648 -3.683 1.00 84.76 C ANISOU 1099 CG ASN A 144 9939 12187 10077 1592 -702 -395 C ATOM 1100 OD1 ASN A 144 -27.732 68.661 -3.930 1.00 85.62 O ANISOU 1100 OD1 ASN A 144 9995 12153 10382 1684 -587 -395 O ATOM 1101 ND2 ASN A 144 -25.806 67.513 -4.044 1.00 84.34 N ANISOU 1101 ND2 ASN A 144 9966 12067 10012 1532 -743 -425 N ATOM 1102 N VAL A 145 -29.725 65.512 -0.236 1.00 82.92 N ANISOU 1102 N VAL A 145 9573 12562 9371 1514 -573 -486 N ATOM 1103 CA VAL A 145 -30.542 64.446 0.325 1.00 81.70 C ANISOU 1103 CA VAL A 145 9405 12545 9093 1497 -532 -406 C ATOM 1104 C VAL A 145 -31.820 65.044 0.905 1.00 83.59 C ANISOU 1104 C VAL A 145 9542 12729 9488 1539 -319 -491 C ATOM 1105 O VAL A 145 -31.775 65.824 1.856 1.00 84.44 O ANISOU 1105 O VAL A 145 9688 12833 9564 1521 -158 -690 O ATOM 1106 CB VAL A 145 -29.786 63.678 1.424 1.00 79.13 C ANISOU 1106 CB VAL A 145 9211 12409 8445 1430 -550 -456 C ATOM 1107 CG1 VAL A 145 -30.686 62.634 2.060 1.00 79.58 C ANISOU 1107 CG1 VAL A 145 9275 12573 8388 1424 -439 -366 C ATOM 1108 CG2 VAL A 145 -28.536 63.036 0.857 1.00 76.37 C ANISOU 1108 CG2 VAL A 145 8923 12090 8003 1393 -748 -361 C ATOM 1109 N LEU A 146 -32.957 64.681 0.323 1.00 83.46 N ANISOU 1109 N LEU A 146 9386 12662 9662 1587 -313 -358 N ATOM 1110 CA LEU A 146 -34.234 65.242 0.740 1.00 77.26 C ANISOU 1110 CA LEU A 146 8456 11785 9115 1637 -107 -424 C ATOM 1111 C LEU A 146 -35.071 64.224 1.503 1.00 97.71 C ANISOU 1111 C LEU A 146 11023 14462 11641 1599 40 -408 C ATOM 1112 O LEU A 146 -34.863 63.018 1.382 1.00 96.78 O ANISOU 1112 O LEU A 146 10957 14455 11358 1555 -51 -292 O ATOM 1113 CB LEU A 146 -34.999 65.754 -0.476 1.00 77.51 C ANISOU 1113 CB LEU A 146 8300 11666 9484 1741 -206 -298 C ATOM 1114 CG LEU A 146 -34.235 66.784 -1.307 1.00 77.04 C ANISOU 1114 CG LEU A 146 8285 11483 9503 1799 -308 -280 C ATOM 1115 CD1 LEU A 146 -34.819 66.868 -2.694 1.00 84.37 C ANISOU 1115 CD1 LEU A 146 9097 12324 10635 1902 -496 -78 C ATOM 1116 CD2 LEU A 146 -34.262 68.146 -0.637 1.00 78.86 C ANISOU 1116 CD2 LEU A 146 8492 11574 9897 1830 -74 -464 C ATOM 1117 N LEU A 147 -36.017 64.723 2.293 1.00 99.93 N ANISOU 1117 N LEU A 147 11226 14663 12079 1614 308 -527 N ATOM 1118 CA LEU A 147 -36.868 63.871 3.116 1.00101.70 C ANISOU 1118 CA LEU A 147 11440 14925 12276 1578 529 -534 C ATOM 1119 C LEU A 147 -38.332 64.027 2.728 1.00106.00 C ANISOU 1119 C LEU A 147 11700 15309 13266 1638 641 -507 C ATOM 1120 O LEU A 147 -38.790 65.136 2.454 1.00108.63 O ANISOU 1120 O LEU A 147 11883 15488 13902 1709 687 -559 O ATOM 1121 CB LEU A 147 -36.699 64.223 4.596 1.00101.93 C ANISOU 1121 CB LEU A 147 11664 14997 12068 1523 807 -726 C ATOM 1122 CG LEU A 147 -35.670 63.455 5.429 1.00100.37 C ANISOU 1122 CG LEU A 147 11748 15009 11378 1458 763 -727 C ATOM 1123 CD1 LEU A 147 -34.311 63.426 4.754 1.00 98.22 C ANISOU 1123 CD1 LEU A 147 11545 14832 10942 1452 428 -665 C ATOM 1124 CD2 LEU A 147 -35.562 64.071 6.815 1.00102.11 C ANISOU 1124 CD2 LEU A 147 12165 15271 11362 1407 1013 -951 C ATOM 1125 N ASP A 148 -39.065 62.918 2.706 1.00106.67 N ANISOU 1125 N ASP A 148 11689 15414 13425 1614 694 -428 N ATOM 1126 CA ASP A 148 -40.501 62.977 2.457 1.00109.24 C ANISOU 1126 CA ASP A 148 11710 15588 14210 1661 814 -432 C ATOM 1127 C ASP A 148 -41.262 63.192 3.761 1.00112.03 C ANISOU 1127 C ASP A 148 12076 15833 14658 1634 1258 -587 C ATOM 1128 O ASP A 148 -40.660 63.464 4.800 1.00112.51 O ANISOU 1128 O ASP A 148 12402 15947 14399 1585 1445 -700 O ATOM 1129 CB ASP A 148 -40.997 61.720 1.731 1.00109.53 C ANISOU 1129 CB ASP A 148 11592 15671 14354 1634 672 -311 C ATOM 1130 CG ASP A 148 -40.577 60.434 2.419 1.00109.13 C ANISOU 1130 CG ASP A 148 11746 15738 13979 1542 807 -280 C ATOM 1131 OD1 ASP A 148 -40.208 60.479 3.610 1.00110.37 O ANISOU 1131 OD1 ASP A 148 12140 15931 13867 1512 1055 -352 O ATOM 1132 OD2 ASP A 148 -40.625 59.370 1.765 1.00107.83 O ANISOU 1132 OD2 ASP A 148 11513 15628 13828 1501 671 -182 O ATOM 1133 N ALA A 149 -42.584 63.069 3.701 1.00114.52 N ANISOU 1133 N ALA A 149 12105 15992 15416 1660 1427 -606 N ATOM 1134 CA ALA A 149 -43.422 63.272 4.875 1.00118.77 C ANISOU 1134 CA ALA A 149 12635 16377 16114 1631 1902 -759 C ATOM 1135 C ALA A 149 -43.117 62.238 5.951 1.00119.89 C ANISOU 1135 C ALA A 149 13079 16623 15851 1539 2158 -775 C ATOM 1136 O ALA A 149 -43.201 62.521 7.145 1.00122.08 O ANISOU 1136 O ALA A 149 13560 16852 15974 1496 2529 -910 O ATOM 1137 CB ALA A 149 -44.891 63.220 4.491 1.00121.78 C ANISOU 1137 CB ALA A 149 12603 16555 17111 1679 2013 -767 C ATOM 1138 N HIS A 150 -42.752 61.039 5.515 1.00119.22 N ANISOU 1138 N HIS A 150 13038 16675 15586 1511 1968 -631 N ATOM 1139 CA HIS A 150 -42.473 59.942 6.429 1.00122.03 C ANISOU 1139 CA HIS A 150 13666 17118 15583 1448 2198 -592 C ATOM 1140 C HIS A 150 -40.982 59.868 6.748 1.00121.42 C ANISOU 1140 C HIS A 150 13947 17267 14919 1432 1996 -535 C ATOM 1141 O HIS A 150 -40.447 58.789 7.004 1.00121.09 O ANISOU 1141 O HIS A 150 14090 17348 14569 1407 1985 -411 O ATOM 1142 CB HIS A 150 -42.956 58.627 5.818 1.00122.85 C ANISOU 1142 CB HIS A 150 13591 17211 15877 1423 2158 -474 C ATOM 1143 CG HIS A 150 -44.212 58.766 5.014 1.00125.41 C ANISOU 1143 CG HIS A 150 13473 17362 16816 1447 2134 -521 C ATOM 1144 ND1 HIS A 150 -45.465 58.802 5.588 1.00128.51 N ANISOU 1144 ND1 HIS A 150 13672 17534 17621 1441 2538 -638 N ATOM 1145 CD2 HIS A 150 -44.407 58.889 3.680 1.00124.51 C ANISOU 1145 CD2 HIS A 150 13069 17263 16976 1481 1742 -470 C ATOM 1146 CE1 HIS A 150 -46.378 58.936 4.642 1.00129.14 C ANISOU 1146 CE1 HIS A 150 13326 17508 18235 1474 2370 -659 C ATOM 1147 NE2 HIS A 150 -45.762 58.991 3.475 1.00126.65 N ANISOU 1147 NE2 HIS A 150 12959 17346 17818 1502 1873 -554 N ATOM 1148 N MET A 151 -40.333 61.032 6.741 1.00121.48 N ANISOU 1148 N MET A 151 14029 17312 14818 1449 1851 -631 N ATOM 1149 CA MET A 151 -38.888 61.181 6.968 1.00118.69 C ANISOU 1149 CA MET A 151 13955 17157 13985 1433 1621 -622 C ATOM 1150 C MET A 151 -37.991 60.103 6.338 1.00113.86 C ANISOU 1150 C MET A 151 13407 16700 13152 1428 1315 -425 C ATOM 1151 O MET A 151 -37.145 59.510 7.009 1.00112.91 O ANISOU 1151 O MET A 151 13549 16737 12616 1410 1296 -366 O ATOM 1152 CB MET A 151 -38.564 61.389 8.460 1.00121.38 C ANISOU 1152 CB MET A 151 14627 17577 13914 1390 1888 -755 C ATOM 1153 CG MET A 151 -38.981 60.261 9.396 1.00123.54 C ANISOU 1153 CG MET A 151 15088 17875 13976 1372 2200 -676 C ATOM 1154 SD MET A 151 -38.398 60.519 11.085 1.00201.96 S ANISOU 1154 SD MET A 151 25484 27958 23295 1331 2428 -811 S ATOM 1155 CE MET A 151 -38.932 59.001 11.871 1.00 97.27 C ANISOU 1155 CE MET A 151 12424 14693 9842 1345 2776 -623 C ATOM 1156 N ASN A 152 -38.179 59.864 5.043 1.00110.78 N ANISOU 1156 N ASN A 152 12781 16264 13047 1446 1075 -322 N ATOM 1157 CA ASN A 152 -37.318 58.952 4.295 1.00107.56 C ANISOU 1157 CA ASN A 152 12417 15969 12481 1427 798 -158 C ATOM 1158 C ASN A 152 -36.386 59.704 3.353 1.00103.87 C ANISOU 1158 C ASN A 152 11938 15529 11998 1445 457 -153 C ATOM 1159 O ASN A 152 -36.824 60.558 2.581 1.00104.93 O ANISOU 1159 O ASN A 152 11894 15557 12418 1486 360 -192 O ATOM 1160 CB ASN A 152 -38.147 57.933 3.512 1.00108.53 C ANISOU 1160 CB ASN A 152 12322 16025 12889 1406 800 -59 C ATOM 1161 CG ASN A 152 -38.848 56.937 4.413 1.00111.94 C ANISOU 1161 CG ASN A 152 12795 16421 13318 1379 1160 -37 C ATOM 1162 OD1 ASN A 152 -38.316 56.537 5.449 1.00112.18 O ANISOU 1162 OD1 ASN A 152 13094 16536 12994 1377 1320 3 O ATOM 1163 ND2 ASN A 152 -40.052 56.531 4.022 1.00114.07 N ANISOU 1163 ND2 ASN A 152 12796 16558 13988 1363 1290 -61 N ATOM 1164 N ALA A 153 -35.100 59.378 3.422 1.00 99.40 N ANISOU 1164 N ALA A 153 11562 15091 11116 1423 288 -94 N ATOM 1165 CA ALA A 153 -34.083 60.077 2.645 1.00 94.38 C ANISOU 1165 CA ALA A 153 10944 14460 10458 1431 17 -105 C ATOM 1166 C ALA A 153 -34.168 59.749 1.159 1.00 90.79 C ANISOU 1166 C ALA A 153 10345 13942 10211 1430 -194 17 C ATOM 1167 O ALA A 153 -34.271 58.585 0.779 1.00 90.46 O ANISOU 1167 O ALA A 153 10276 13928 10164 1390 -219 136 O ATOM 1168 CB ALA A 153 -32.700 59.749 3.180 1.00 93.20 C ANISOU 1168 CB ALA A 153 11004 14451 9957 1406 -95 -85 C ATOM 1169 N LYS A 154 -34.122 60.783 0.324 1.00 88.17 N ANISOU 1169 N LYS A 154 9934 13516 10051 1473 -330 -17 N ATOM 1170 CA LYS A 154 -34.150 60.601 -1.123 1.00 84.00 C ANISOU 1170 CA LYS A 154 9319 12935 9663 1478 -546 97 C ATOM 1171 C LYS A 154 -33.077 61.434 -1.823 1.00 79.73 C ANISOU 1171 C LYS A 154 8875 12338 9080 1499 -709 96 C ATOM 1172 O LYS A 154 -33.120 62.664 -1.800 1.00 79.74 O ANISOU 1172 O LYS A 154 8852 12247 9198 1563 -677 14 O ATOM 1173 CB LYS A 154 -35.536 60.927 -1.684 1.00 85.10 C ANISOU 1173 CB LYS A 154 9226 12985 10123 1536 -546 104 C ATOM 1174 CG LYS A 154 -36.577 59.843 -1.436 1.00 87.32 C ANISOU 1174 CG LYS A 154 9367 13293 10518 1493 -427 121 C ATOM 1175 CD LYS A 154 -37.783 60.025 -2.348 1.00 91.09 C ANISOU 1175 CD LYS A 154 9579 13697 11334 1541 -541 141 C ATOM 1176 CE LYS A 154 -38.688 58.797 -2.355 1.00 93.16 C ANISOU 1176 CE LYS A 154 9678 13981 11739 1472 -463 141 C ATOM 1177 NZ LYS A 154 -39.442 58.631 -1.082 1.00 95.99 N ANISOU 1177 NZ LYS A 154 9975 14292 12207 1468 -116 51 N ATOM 1178 N ILE A 155 -32.117 60.749 -2.439 1.00 76.12 N ANISOU 1178 N ILE A 155 8523 11911 8488 1442 -845 184 N ATOM 1179 CA ILE A 155 -31.011 61.394 -3.142 1.00 74.62 C ANISOU 1179 CA ILE A 155 8437 11640 8274 1448 -962 185 C ATOM 1180 C ILE A 155 -31.523 62.157 -4.359 1.00 74.49 C ANISOU 1180 C ILE A 155 8363 11498 8443 1519 -1061 245 C ATOM 1181 O ILE A 155 -32.342 61.639 -5.118 1.00 74.65 O ANISOU 1181 O ILE A 155 8297 11529 8535 1520 -1153 338 O ATOM 1182 CB ILE A 155 -29.969 60.358 -3.580 1.00 75.68 C ANISOU 1182 CB ILE A 155 8680 11806 8269 1363 -1049 274 C ATOM 1183 CG1 ILE A 155 -29.536 59.515 -2.378 1.00 77.61 C ANISOU 1183 CG1 ILE A 155 8974 12183 8333 1321 -970 264 C ATOM 1184 CG2 ILE A 155 -28.778 61.038 -4.230 1.00 75.41 C ANISOU 1184 CG2 ILE A 155 8751 11656 8246 1361 -1121 256 C ATOM 1185 CD1 ILE A 155 -28.595 58.385 -2.723 1.00 77.64 C ANISOU 1185 CD1 ILE A 155 9049 12202 8248 1250 -1027 375 C ATOM 1186 N ALA A 156 -31.032 63.381 -4.548 1.00 75.49 N ANISOU 1186 N ALA A 156 8536 11502 8645 1579 -1045 192 N ATOM 1187 CA ALA A 156 -31.663 64.310 -5.487 1.00 78.78 C ANISOU 1187 CA ALA A 156 8894 11786 9251 1689 -1100 264 C ATOM 1188 C ALA A 156 -30.827 64.763 -6.690 1.00 80.52 C ANISOU 1188 C ALA A 156 9266 11871 9459 1713 -1186 354 C ATOM 1189 O ALA A 156 -31.012 64.264 -7.800 1.00 83.35 O ANISOU 1189 O ALA A 156 9673 12229 9766 1709 -1334 492 O ATOM 1190 CB ALA A 156 -32.205 65.525 -4.738 1.00 80.39 C ANISOU 1190 CB ALA A 156 8994 11908 9644 1776 -937 150 C ATOM 1191 N ASP A 157 -29.935 65.726 -6.476 1.00 79.36 N ANISOU 1191 N ASP A 157 9195 11595 9361 1733 -1075 260 N ATOM 1192 CA ASP A 157 -29.313 66.434 -7.595 1.00 78.97 C ANISOU 1192 CA ASP A 157 9282 11355 9366 1788 -1085 344 C ATOM 1193 C ASP A 157 -28.167 65.667 -8.243 1.00 74.83 C ANISOU 1193 C ASP A 157 8930 10810 8694 1682 -1135 386 C ATOM 1194 O ASP A 157 -27.114 65.477 -7.638 1.00 73.73 O ANISOU 1194 O ASP A 157 8823 10673 8518 1596 -1069 263 O ATOM 1195 CB ASP A 157 -28.842 67.825 -7.162 1.00 82.78 C ANISOU 1195 CB ASP A 157 9761 11665 10028 1848 -896 210 C ATOM 1196 CG ASP A 157 -28.471 68.707 -8.340 1.00 86.50 C ANISOU 1196 CG ASP A 157 10362 11898 10607 1944 -853 330 C ATOM 1197 OD1 ASP A 157 -28.895 68.399 -9.473 1.00 87.62 O ANISOU 1197 OD1 ASP A 157 10586 12029 10676 1999 -995 538 O ATOM 1198 OD2 ASP A 157 -27.762 69.713 -8.134 1.00 89.08 O ANISOU 1198 OD2 ASP A 157 10717 12043 11085 1963 -668 210 O ATOM 1199 N PHE A 158 -28.380 65.242 -9.485 1.00 73.66 N ANISOU 1199 N PHE A 158 8887 10634 8466 1689 -1255 554 N ATOM 1200 CA PHE A 158 -27.380 64.482 -10.228 1.00 72.90 C ANISOU 1200 CA PHE A 158 8969 10487 8243 1580 -1268 599 C ATOM 1201 C PHE A 158 -26.696 65.326 -11.296 1.00 74.84 C ANISOU 1201 C PHE A 158 9417 10487 8529 1634 -1186 671 C ATOM 1202 O PHE A 158 -26.236 64.802 -12.312 1.00 74.85 O ANISOU 1202 O PHE A 158 9606 10419 8413 1572 -1205 762 O ATOM 1203 CB PHE A 158 -28.016 63.247 -10.871 1.00 72.46 C ANISOU 1203 CB PHE A 158 8926 10571 8036 1508 -1423 704 C ATOM 1204 CG PHE A 158 -28.174 62.090 -9.930 1.00 70.69 C ANISOU 1204 CG PHE A 158 8568 10529 7762 1406 -1429 636 C ATOM 1205 CD1 PHE A 158 -29.213 62.060 -9.018 1.00 70.62 C ANISOU 1205 CD1 PHE A 158 8364 10657 7810 1450 -1439 590 C ATOM 1206 CD2 PHE A 158 -27.280 61.033 -9.955 1.00 68.98 C ANISOU 1206 CD2 PHE A 158 8426 10322 7463 1272 -1390 629 C ATOM 1207 CE1 PHE A 158 -29.356 60.999 -8.147 1.00 70.37 C ANISOU 1207 CE1 PHE A 158 8241 10771 7724 1367 -1404 547 C ATOM 1208 CE2 PHE A 158 -27.418 59.970 -9.089 1.00 68.40 C ANISOU 1208 CE2 PHE A 158 8242 10397 7349 1199 -1373 600 C ATOM 1209 CZ PHE A 158 -28.457 59.953 -8.183 1.00 69.66 C ANISOU 1209 CZ PHE A 158 8235 10696 7536 1249 -1376 563 C ATOM 1210 N GLY A 159 -26.628 66.633 -11.062 1.00 76.25 N ANISOU 1210 N GLY A 159 9572 10516 8884 1746 -1058 625 N ATOM 1211 CA GLY A 159 -26.024 67.546 -12.014 1.00 77.25 C ANISOU 1211 CA GLY A 159 9894 10375 9084 1819 -926 701 C ATOM 1212 C GLY A 159 -24.548 67.282 -12.246 1.00 76.87 C ANISOU 1212 C GLY A 159 9988 10168 9052 1697 -780 619 C ATOM 1213 O GLY A 159 -24.027 67.535 -13.332 1.00 78.42 O ANISOU 1213 O GLY A 159 10412 10153 9231 1712 -680 722 O ATOM 1214 N LEU A 160 -23.873 66.764 -11.225 1.00 75.63 N ANISOU 1214 N LEU A 160 9699 10104 8933 1580 -765 438 N ATOM 1215 CA LEU A 160 -22.436 66.535 -11.300 1.00 75.76 C ANISOU 1215 CA LEU A 160 9784 9965 9038 1468 -637 336 C ATOM 1216 C LEU A 160 -22.112 65.053 -11.404 1.00 75.84 C ANISOU 1216 C LEU A 160 9813 10101 8901 1332 -737 380 C ATOM 1217 O LEU A 160 -20.948 64.659 -11.373 1.00 74.51 O ANISOU 1217 O LEU A 160 9658 9825 8827 1233 -651 303 O ATOM 1218 CB LEU A 160 -21.736 67.155 -10.090 1.00 76.69 C ANISOU 1218 CB LEU A 160 9725 10067 9347 1444 -550 87 C ATOM 1219 CG LEU A 160 -21.908 68.673 -10.008 1.00 79.77 C ANISOU 1219 CG LEU A 160 10093 10276 9941 1556 -381 8 C ATOM 1220 CD1 LEU A 160 -21.308 69.257 -8.740 1.00 80.53 C ANISOU 1220 CD1 LEU A 160 10002 10391 10203 1508 -312 -287 C ATOM 1221 CD2 LEU A 160 -21.300 69.323 -11.236 1.00 81.50 C ANISOU 1221 CD2 LEU A 160 10522 10155 10288 1599 -174 100 C ATOM 1222 N SER A 161 -23.152 64.238 -11.535 1.00 78.51 N ANISOU 1222 N SER A 161 10132 10649 9049 1329 -903 496 N ATOM 1223 CA SER A 161 -22.989 62.801 -11.706 1.00 77.85 C ANISOU 1223 CA SER A 161 10067 10671 8840 1200 -968 546 C ATOM 1224 C SER A 161 -22.276 62.489 -13.015 1.00 77.93 C ANISOU 1224 C SER A 161 10319 10470 8821 1123 -861 626 C ATOM 1225 O SER A 161 -22.170 63.339 -13.898 1.00 78.83 O ANISOU 1225 O SER A 161 10617 10389 8948 1188 -768 684 O ATOM 1226 CB SER A 161 -24.352 62.107 -11.693 1.00 77.30 C ANISOU 1226 CB SER A 161 9923 10837 8612 1212 -1139 633 C ATOM 1227 OG SER A 161 -25.145 62.521 -12.794 1.00 76.49 O ANISOU 1227 OG SER A 161 9947 10694 8420 1285 -1212 757 O ATOM 1228 N ASN A 162 -21.791 61.260 -13.133 1.00 77.79 N ANISOU 1228 N ASN A 162 10315 10475 8766 985 -844 635 N ATOM 1229 CA ASN A 162 -21.143 60.811 -14.355 1.00 79.78 C ANISOU 1229 CA ASN A 162 10805 10523 8983 881 -709 694 C ATOM 1230 C ASN A 162 -21.203 59.294 -14.470 1.00 77.62 C ANISOU 1230 C ASN A 162 10512 10357 8624 736 -734 724 C ATOM 1231 O ASN A 162 -21.035 58.580 -13.483 1.00 75.54 O ANISOU 1231 O ASN A 162 10047 10220 8435 701 -769 684 O ATOM 1232 CB ASN A 162 -19.693 61.292 -14.402 1.00 83.39 C ANISOU 1232 CB ASN A 162 11308 10691 9685 848 -484 606 C ATOM 1233 CG ASN A 162 -19.051 61.084 -15.761 1.00 86.74 C ANISOU 1233 CG ASN A 162 12026 10843 10088 756 -278 665 C ATOM 1234 OD1 ASN A 162 -19.734 61.012 -16.781 1.00 88.67 O ANISOU 1234 OD1 ASN A 162 12499 11099 10092 757 -312 777 O ATOM 1235 ND2 ASN A 162 -17.727 60.988 -15.779 1.00 87.34 N ANISOU 1235 ND2 ASN A 162 12100 10668 10418 672 -61 581 N ATOM 1236 N MET A 163 -21.453 58.804 -15.677 1.00 78.58 N ANISOU 1236 N MET A 163 10855 10423 8579 652 -707 794 N ATOM 1237 CA MET A 163 -21.565 57.369 -15.894 1.00 79.34 C ANISOU 1237 CA MET A 163 10942 10596 8607 495 -695 801 C ATOM 1238 C MET A 163 -20.179 56.735 -15.972 1.00 77.85 C ANISOU 1238 C MET A 163 10785 10177 8617 365 -454 764 C ATOM 1239 O MET A 163 -19.353 57.125 -16.795 1.00 77.74 O ANISOU 1239 O MET A 163 10984 9894 8660 324 -262 758 O ATOM 1240 CB MET A 163 -22.380 57.080 -17.161 1.00 81.42 C ANISOU 1240 CB MET A 163 11430 10903 8604 434 -769 853 C ATOM 1241 CG MET A 163 -22.929 55.659 -17.248 1.00 81.17 C ANISOU 1241 CG MET A 163 11323 11023 8494 281 -808 826 C ATOM 1242 SD MET A 163 -21.875 54.527 -18.179 1.00212.48 S ANISOU 1242 SD MET A 163 28168 27412 25152 41 -516 789 S ATOM 1243 CE MET A 163 -22.101 55.134 -19.851 1.00 81.99 C ANISOU 1243 CE MET A 163 12067 10778 8306 15 -523 821 C ATOM 1244 N MET A 164 -19.926 55.765 -15.097 1.00 76.48 N ANISOU 1244 N MET A 164 10397 10093 8570 312 -448 751 N ATOM 1245 CA MET A 164 -18.647 55.064 -15.062 1.00 74.50 C ANISOU 1245 CA MET A 164 10115 9631 8559 205 -238 735 C ATOM 1246 C MET A 164 -18.523 54.086 -16.228 1.00 77.96 C ANISOU 1246 C MET A 164 10756 9923 8942 20 -50 750 C ATOM 1247 O MET A 164 -19.442 53.318 -16.505 1.00 78.54 O ANISOU 1247 O MET A 164 10848 10157 8837 -52 -118 765 O ATOM 1248 CB MET A 164 -18.493 54.315 -13.736 1.00 69.68 C ANISOU 1248 CB MET A 164 9217 9179 8079 233 -310 754 C ATOM 1249 CG MET A 164 -18.343 55.215 -12.520 1.00 67.62 C ANISOU 1249 CG MET A 164 8773 9038 7883 387 -463 708 C ATOM 1250 SD MET A 164 -19.179 54.571 -11.057 1.00113.23 S ANISOU 1250 SD MET A 164 14314 15156 13551 467 -646 758 S ATOM 1251 CE MET A 164 -18.591 52.882 -11.039 1.00104.26 C ANISOU 1251 CE MET A 164 13108 13947 12558 347 -493 861 C ATOM 1252 N SER A 165 -17.385 54.123 -16.912 1.00 80.00 N ANISOU 1252 N SER A 165 11164 9862 9372 -69 207 723 N ATOM 1253 CA SER A 165 -17.125 53.194 -18.004 1.00 82.57 C ANISOU 1253 CA SER A 165 11700 10004 9668 -267 445 713 C ATOM 1254 C SER A 165 -15.946 52.307 -17.626 1.00 83.21 C ANISOU 1254 C SER A 165 11616 9876 10124 -359 675 709 C ATOM 1255 O SER A 165 -14.975 52.785 -17.042 1.00 83.93 O ANISOU 1255 O SER A 165 11556 9828 10505 -285 718 693 O ATOM 1256 CB SER A 165 -16.837 53.956 -19.298 1.00 85.62 C ANISOU 1256 CB SER A 165 12460 10149 9924 -306 613 694 C ATOM 1257 OG SER A 165 -16.824 53.082 -20.413 1.00 88.31 O ANISOU 1257 OG SER A 165 13056 10365 10135 -508 816 668 O ATOM 1258 N ASP A 166 -16.032 51.019 -17.949 1.00 84.71 N ANISOU 1258 N ASP A 166 11813 10037 10335 -519 822 717 N ATOM 1259 CA ASP A 166 -15.007 50.064 -17.530 1.00 87.57 C ANISOU 1259 CA ASP A 166 11982 10207 11084 -591 1038 745 C ATOM 1260 C ASP A 166 -13.666 50.319 -18.202 1.00 86.40 C ANISOU 1260 C ASP A 166 11951 9642 11233 -674 1358 695 C ATOM 1261 O ASP A 166 -13.581 50.437 -19.424 1.00 85.68 O ANISOU 1261 O ASP A 166 12190 9346 11019 -807 1582 635 O ATOM 1262 CB ASP A 166 -15.435 48.616 -17.789 1.00 94.29 C ANISOU 1262 CB ASP A 166 12820 11084 11922 -755 1180 759 C ATOM 1263 CG ASP A 166 -16.912 48.481 -18.074 1.00100.93 C ANISOU 1263 CG ASP A 166 13756 12222 12369 -779 982 726 C ATOM 1264 OD1 ASP A 166 -17.703 49.320 -17.594 1.00104.37 O ANISOU 1264 OD1 ASP A 166 14143 12916 12598 -620 678 743 O ATOM 1265 OD2 ASP A 166 -17.281 47.525 -18.787 1.00102.98 O ANISOU 1265 OD2 ASP A 166 14125 12447 12555 -967 1142 668 O ATOM 1266 N GLY A 167 -12.619 50.386 -17.387 1.00 87.58 N ANISOU 1266 N GLY A 167 11831 9666 11780 -596 1382 716 N ATOM 1267 CA GLY A 167 -11.277 50.625 -17.880 1.00 90.53 C ANISOU 1267 CA GLY A 167 12238 9621 12538 -664 1691 656 C ATOM 1268 C GLY A 167 -10.950 52.103 -17.933 1.00 94.28 C ANISOU 1268 C GLY A 167 12785 10012 13024 -554 1637 576 C ATOM 1269 O GLY A 167 -9.874 52.495 -18.379 1.00 97.80 O ANISOU 1269 O GLY A 167 13274 10089 13798 -603 1911 503 O ATOM 1270 N GLU A 168 -11.879 52.928 -17.463 1.00 92.92 N ANISOU 1270 N GLU A 168 12616 10158 12533 -407 1315 584 N ATOM 1271 CA GLU A 168 -11.725 54.371 -17.572 1.00 94.30 C ANISOU 1271 CA GLU A 168 12882 10255 12693 -301 1286 512 C ATOM 1272 C GLU A 168 -11.909 55.086 -16.233 1.00 92.14 C ANISOU 1272 C GLU A 168 12310 10252 12446 -118 950 485 C ATOM 1273 O GLU A 168 -12.798 54.749 -15.448 1.00 90.70 O ANISOU 1273 O GLU A 168 11995 10425 12040 -45 671 547 O ATOM 1274 CB GLU A 168 -12.689 54.923 -18.627 1.00 98.87 C ANISOU 1274 CB GLU A 168 13852 10881 12833 -310 1294 536 C ATOM 1275 CG GLU A 168 -12.575 56.419 -18.872 1.00105.36 C ANISOU 1275 CG GLU A 168 14812 11580 13639 -192 1322 493 C ATOM 1276 CD GLU A 168 -13.051 56.816 -20.255 1.00111.25 C ANISOU 1276 CD GLU A 168 16020 12204 14045 -233 1476 542 C ATOM 1277 OE1 GLU A 168 -12.712 56.105 -21.226 1.00114.76 O ANISOU 1277 OE1 GLU A 168 16713 12433 14458 -403 1753 542 O ATOM 1278 OE2 GLU A 168 -13.766 57.834 -20.370 1.00112.08 O ANISOU 1278 OE2 GLU A 168 16247 12428 13910 -93 1325 586 O ATOM 1279 N PHE A 169 -11.050 56.070 -15.981 1.00 91.96 N ANISOU 1279 N PHE A 169 12189 10042 12711 -57 1007 373 N ATOM 1280 CA PHE A 169 -11.123 56.886 -14.773 1.00 90.91 C ANISOU 1280 CA PHE A 169 11798 10133 12613 94 722 297 C ATOM 1281 C PHE A 169 -11.795 58.224 -15.089 1.00 90.55 C ANISOU 1281 C PHE A 169 11942 10114 12347 188 694 254 C ATOM 1282 O PHE A 169 -12.157 58.469 -16.235 1.00 90.42 O ANISOU 1282 O PHE A 169 12255 9951 12149 149 873 308 O ATOM 1283 CB PHE A 169 -9.726 57.088 -14.186 1.00 93.01 C ANISOU 1283 CB PHE A 169 11773 10189 13379 96 776 168 C ATOM 1284 CG PHE A 169 -9.033 55.805 -13.806 1.00 93.04 C ANISOU 1284 CG PHE A 169 11551 10159 13642 36 782 239 C ATOM 1285 CD1 PHE A 169 -8.337 55.071 -14.752 1.00 93.17 C ANISOU 1285 CD1 PHE A 169 11668 9819 13913 -109 1131 272 C ATOM 1286 CD2 PHE A 169 -9.076 55.338 -12.503 1.00 93.42 C ANISOU 1286 CD2 PHE A 169 11298 10517 13680 129 460 284 C ATOM 1287 CE1 PHE A 169 -7.697 53.896 -14.408 1.00 93.39 C ANISOU 1287 CE1 PHE A 169 11468 9786 14228 -155 1163 353 C ATOM 1288 CE2 PHE A 169 -8.434 54.161 -12.150 1.00 93.79 C ANISOU 1288 CE2 PHE A 169 11135 10521 13980 101 468 387 C ATOM 1289 CZ PHE A 169 -7.745 53.440 -13.105 1.00 93.98 C ANISOU 1289 CZ PHE A 169 11229 10174 14304 -39 822 424 C ATOM 1290 N LEU A 170 -11.958 59.091 -14.093 1.00 92.14 N ANISOU 1290 N LEU A 170 11951 10497 12562 311 480 160 N ATOM 1291 CA LEU A 170 -12.845 60.243 -14.264 1.00 96.80 C ANISOU 1291 CA LEU A 170 12692 11168 12918 417 426 152 C ATOM 1292 C LEU A 170 -12.210 61.637 -14.167 1.00104.77 C ANISOU 1292 C LEU A 170 13660 11951 14197 477 559 -15 C ATOM 1293 O LEU A 170 -12.294 62.420 -15.112 1.00109.20 O ANISOU 1293 O LEU A 170 14481 12277 14735 499 782 9 O ATOM 1294 CB LEU A 170 -14.023 60.146 -13.295 1.00 92.87 C ANISOU 1294 CB LEU A 170 12066 11099 12121 513 94 198 C ATOM 1295 CG LEU A 170 -14.970 58.958 -13.471 1.00 88.59 C ANISOU 1295 CG LEU A 170 11591 10788 11281 470 -21 358 C ATOM 1296 CD1 LEU A 170 -16.146 59.057 -12.513 1.00 86.29 C ANISOU 1296 CD1 LEU A 170 11174 10869 10744 574 -296 381 C ATOM 1297 CD2 LEU A 170 -15.457 58.848 -14.907 1.00 88.06 C ANISOU 1297 CD2 LEU A 170 11858 10586 11014 410 129 459 C ATOM 1298 N ARG A 171 -11.608 61.948 -13.019 1.00106.49 N ANISOU 1298 N ARG A 171 13560 12247 14656 507 423 -186 N ATOM 1299 CA ARG A 171 -11.083 63.299 -12.711 1.00109.41 C ANISOU 1299 CA ARG A 171 13828 12448 15296 557 519 -398 C ATOM 1300 C ARG A 171 -12.194 64.358 -12.589 1.00107.99 C ANISOU 1300 C ARG A 171 13751 12412 14867 678 453 -389 C ATOM 1301 O ARG A 171 -13.100 64.189 -11.753 1.00106.36 O ANISOU 1301 O ARG A 171 13448 12571 14394 739 175 -357 O ATOM 1302 CB ARG A 171 -10.035 63.739 -13.730 1.00112.65 C ANISOU 1302 CB ARG A 171 14367 12365 16072 487 921 -468 C ATOM 1303 CG ARG A 171 -9.007 64.742 -13.215 1.00116.72 C ANISOU 1303 CG ARG A 171 14638 12657 17052 485 1033 -751 C ATOM 1304 CD ARG A 171 -7.832 64.893 -14.182 1.00120.31 C ANISOU 1304 CD ARG A 171 15179 12591 17943 392 1463 -822 C ATOM 1305 NE ARG A 171 -6.862 65.881 -13.708 1.00124.51 N ANISOU 1305 NE ARG A 171 15450 12888 18972 382 1589 -1124 N ATOM 1306 CZ ARG A 171 -5.701 66.138 -14.306 1.00128.20 C ANISOU 1306 CZ ARG A 171 15892 12880 19940 299 1968 -1259 C ATOM 1307 NH1 ARG A 171 -5.369 65.472 -15.403 1.00128.53 N ANISOU 1307 NH1 ARG A 171 16183 12630 20023 219 2269 -1106 N ATOM 1308 NH2 ARG A 171 -4.871 67.053 -13.812 1.00130.81 N ANISOU 1308 NH2 ARG A 171 15944 13011 20745 283 2066 -1567 N HETATM 1309 N TPO A 172 -12.118 65.421 -13.400 1.00109.59 N ANISOU 1309 N TPO A 172 14149 12311 15180 718 732 -407 N HETATM 1310 CA TPO A 172 -13.055 66.500 -13.376 1.00113.08 C ANISOU 1310 CA TPO A 172 14680 12815 15469 845 723 -385 C HETATM 1311 CB TPO A 172 -14.451 66.047 -13.709 1.00109.63 C ANISOU 1311 CB TPO A 172 14419 12652 14584 912 532 -142 C HETATM 1312 CG2 TPO A 172 -15.454 67.146 -13.450 1.00107.85 C ANISOU 1312 CG2 TPO A 172 14201 12523 14253 1057 481 -129 C HETATM 1313 OG1 TPO A 172 -14.488 65.725 -15.083 1.00110.35 O ANISOU 1313 OG1 TPO A 172 14841 12542 14543 884 712 44 O HETATM 1314 P TPO A 172 -15.663 64.804 -15.598 1.00 78.08 P ANISOU 1314 P TPO A 172 10925 8724 10020 887 503 271 P HETATM 1315 O1P TPO A 172 -16.790 65.682 -16.059 1.00 78.42 O ANISOU 1315 O1P TPO A 172 11136 8819 9842 1041 453 411 O HETATM 1316 O2P TPO A 172 -16.117 63.940 -14.454 1.00 77.34 O ANISOU 1316 O2P TPO A 172 10555 9006 9825 862 197 236 O HETATM 1317 O3P TPO A 172 -15.173 63.953 -16.735 1.00 78.06 O ANISOU 1317 O3P TPO A 172 11179 8526 9955 762 684 368 O HETATM 1318 C TPO A 172 -13.014 67.300 -12.083 1.00118.14 C ANISOU 1318 C TPO A 172 15027 13604 16257 887 592 -626 C HETATM 1319 O TPO A 172 -12.784 68.488 -12.132 1.00121.76 O ANISOU 1319 O TPO A 172 15480 13841 16943 931 797 -763 O ATOM 1320 N SER A 173 -13.226 66.645 -10.944 1.00117.82 N ANISOU 1320 N SER A 173 14762 13923 16082 869 277 -682 N ATOM 1321 CA SER A 173 -13.204 67.287 -9.632 1.00118.15 C ANISOU 1321 CA SER A 173 14547 14152 16192 890 124 -927 C ATOM 1322 C SER A 173 -14.285 68.365 -9.552 1.00115.00 C ANISOU 1322 C SER A 173 14227 13799 15669 1000 174 -922 C ATOM 1323 O SER A 173 -14.002 69.535 -9.798 1.00114.59 O ANISOU 1323 O SER A 173 14190 13477 15871 1030 419 -1055 O ATOM 1324 CB SER A 173 -11.836 67.904 -9.354 1.00123.20 C ANISOU 1324 CB SER A 173 14987 14537 17287 818 263 -1225 C ATOM 1325 OG SER A 173 -10.790 66.998 -9.612 1.00126.40 O ANISOU 1325 OG SER A 173 15316 14819 17893 726 272 -1213 O ATOM 1326 N CYS A 174 -15.510 67.983 -9.192 1.00113.45 N ANISOU 1326 N CYS A 174 14063 13916 15125 1063 -30 -775 N ATOM 1327 CA CYS A 174 -16.643 68.902 -9.295 1.00114.65 C ANISOU 1327 CA CYS A 174 14297 14084 15181 1180 29 -715 C ATOM 1328 C CYS A 174 -17.422 69.100 -7.995 1.00114.46 C ANISOU 1328 C CYS A 174 14105 14373 15012 1210 -149 -837 C ATOM 1329 O CYS A 174 -18.272 69.989 -7.911 1.00116.63 O ANISOU 1329 O CYS A 174 14393 14633 15287 1301 -69 -838 O ATOM 1330 CB CYS A 174 -17.590 68.432 -10.395 1.00115.12 C ANISOU 1330 CB CYS A 174 14594 14155 14992 1248 10 -393 C ATOM 1331 SG CYS A 174 -17.789 66.641 -10.502 1.00 92.63 S ANISOU 1331 SG CYS A 174 11774 11561 11858 1162 -224 -214 S ATOM 1332 N GLY A 175 -17.120 68.289 -6.984 1.00111.90 N ANISOU 1332 N GLY A 175 13632 14314 14571 1138 -369 -931 N ATOM 1333 CA GLY A 175 -17.854 68.315 -5.728 1.00110.80 C ANISOU 1333 CA GLY A 175 13381 14486 14233 1155 -528 -1031 C ATOM 1334 C GLY A 175 -17.814 69.625 -4.962 1.00111.28 C ANISOU 1334 C GLY A 175 13330 14498 14451 1159 -416 -1327 C ATOM 1335 O GLY A 175 -17.335 70.644 -5.453 1.00112.81 O ANISOU 1335 O GLY A 175 13528 14395 14941 1165 -186 -1446 O ATOM 1336 N SER A 176 -18.338 69.589 -3.743 1.00110.94 N ANISOU 1336 N SER A 176 13204 14739 14211 1149 -546 -1452 N ATOM 1337 CA SER A 176 -18.348 70.751 -2.862 1.00113.43 C ANISOU 1337 CA SER A 176 13417 15048 14635 1126 -442 -1772 C ATOM 1338 C SER A 176 -16.953 70.964 -2.269 1.00114.81 C ANISOU 1338 C SER A 176 13441 15204 14980 1014 -505 -2093 C ATOM 1339 O SER A 176 -16.098 70.088 -2.394 1.00116.32 O ANISOU 1339 O SER A 176 13594 15435 15169 970 -667 -2035 O ATOM 1340 CB SER A 176 -19.386 70.547 -1.754 1.00114.15 C ANISOU 1340 CB SER A 176 13501 15449 14421 1140 -545 -1798 C ATOM 1341 OG SER A 176 -20.675 70.356 -2.307 1.00113.61 O ANISOU 1341 OG SER A 176 13525 15382 14260 1241 -491 -1522 O ATOM 1342 N PRO A 177 -16.705 72.135 -1.647 1.00113.94 N ANISOU 1342 N PRO A 177 13223 15016 15051 963 -371 -2446 N ATOM 1343 CA PRO A 177 -15.423 72.325 -0.954 1.00112.31 C ANISOU 1343 CA PRO A 177 12838 14839 14996 843 -481 -2800 C ATOM 1344 C PRO A 177 -15.223 71.266 0.127 1.00108.61 C ANISOU 1344 C PRO A 177 12326 14779 14162 804 -856 -2812 C ATOM 1345 O PRO A 177 -14.161 70.652 0.197 1.00108.30 O ANISOU 1345 O PRO A 177 12177 14777 14193 757 -1053 -2847 O ATOM 1346 CB PRO A 177 -15.559 73.720 -0.332 1.00116.27 C ANISOU 1346 CB PRO A 177 13256 15251 15670 792 -270 -3178 C ATOM 1347 CG PRO A 177 -17.028 74.041 -0.382 1.00116.90 C ANISOU 1347 CG PRO A 177 13470 15353 15595 889 -112 -2999 C ATOM 1348 CD PRO A 177 -17.528 73.356 -1.609 1.00114.70 C ANISOU 1348 CD PRO A 177 13338 14967 15277 1008 -98 -2549 C ATOM 1349 N ASN A 178 -16.237 71.055 0.959 1.00106.25 N ANISOU 1349 N ASN A 178 12114 14762 13493 832 -935 -2770 N ATOM 1350 CA ASN A 178 -16.246 69.908 1.854 1.00103.49 C ANISOU 1350 CA ASN A 178 11792 14785 12744 831 -1252 -2672 C ATOM 1351 C ASN A 178 -16.874 68.736 1.110 1.00100.23 C ANISOU 1351 C ASN A 178 11504 14395 12185 921 -1283 -2226 C ATOM 1352 O ASN A 178 -17.214 68.863 -0.066 1.00 99.73 O ANISOU 1352 O ASN A 178 11501 14078 12312 970 -1097 -2034 O ATOM 1353 CB ASN A 178 -17.026 70.214 3.134 1.00104.15 C ANISOU 1353 CB ASN A 178 11939 15143 12488 809 -1277 -2848 C ATOM 1354 CG ASN A 178 -16.818 71.636 3.621 1.00105.86 C ANISOU 1354 CG ASN A 178 12069 15256 12899 718 -1105 -3290 C ATOM 1355 OD1 ASN A 178 -16.988 72.594 2.867 1.00105.13 O ANISOU 1355 OD1 ASN A 178 11945 14840 13160 728 -807 -3347 O ATOM 1356 ND2 ASN A 178 -16.442 71.780 4.885 1.00108.62 N ANISOU 1356 ND2 ASN A 178 12386 15874 13012 627 -1286 -3607 N ATOM 1357 N TYR A 179 -17.012 67.597 1.784 1.00 97.41 N ANISOU 1357 N TYR A 179 11193 14333 11486 943 -1512 -2066 N ATOM 1358 CA TYR A 179 -17.602 66.389 1.192 1.00 90.11 C ANISOU 1358 CA TYR A 179 10369 13444 10423 1010 -1536 -1673 C ATOM 1359 C TYR A 179 -16.818 65.812 0.006 1.00 86.51 C ANISOU 1359 C TYR A 179 9879 12762 10227 1005 -1528 -1492 C ATOM 1360 O TYR A 179 -17.160 64.748 -0.503 1.00 85.25 O ANISOU 1360 O TYR A 179 9792 12624 9973 1038 -1548 -1197 O ATOM 1361 CB TYR A 179 -19.065 66.617 0.787 1.00 85.65 C ANISOU 1361 CB TYR A 179 9918 12830 9795 1070 -1335 -1523 C ATOM 1362 CG TYR A 179 -19.907 67.313 1.831 1.00 86.32 C ANISOU 1362 CG TYR A 179 10036 13061 9703 1069 -1256 -1713 C ATOM 1363 CD1 TYR A 179 -20.414 66.618 2.920 1.00 86.33 C ANISOU 1363 CD1 TYR A 179 10112 13355 9333 1078 -1357 -1671 C ATOM 1364 CD2 TYR A 179 -20.211 68.662 1.717 1.00 88.16 C ANISOU 1364 CD2 TYR A 179 10235 13111 10150 1059 -1039 -1927 C ATOM 1365 CE1 TYR A 179 -21.186 67.251 3.876 1.00 88.58 C ANISOU 1365 CE1 TYR A 179 10452 13752 9454 1063 -1241 -1857 C ATOM 1366 CE2 TYR A 179 -20.985 69.304 2.665 1.00 90.18 C ANISOU 1366 CE2 TYR A 179 10519 13471 10274 1044 -924 -2115 C ATOM 1367 CZ TYR A 179 -21.472 68.594 3.743 1.00 90.29 C ANISOU 1367 CZ TYR A 179 10620 13779 9906 1039 -1023 -2088 C ATOM 1368 OH TYR A 179 -22.244 69.233 4.688 1.00 91.73 O ANISOU 1368 OH TYR A 179 10853 14043 9956 1012 -866 -2288 O ATOM 1369 N ALA A 180 -15.770 66.506 -0.427 1.00 86.08 N ANISOU 1369 N ALA A 180 9716 12474 10516 953 -1468 -1687 N ATOM 1370 CA ALA A 180 -14.987 66.065 -1.576 1.00 84.75 C ANISOU 1370 CA ALA A 180 9531 12042 10628 935 -1399 -1545 C ATOM 1371 C ALA A 180 -13.753 65.283 -1.146 1.00 86.17 C ANISOU 1371 C ALA A 180 9554 12298 10890 897 -1625 -1575 C ATOM 1372 O ALA A 180 -13.003 65.722 -0.274 1.00 89.40 O ANISOU 1372 O ALA A 180 9804 12807 11357 858 -1782 -1853 O ATOM 1373 CB ALA A 180 -14.586 67.254 -2.430 1.00 85.26 C ANISOU 1373 CB ALA A 180 9581 11742 11070 909 -1136 -1708 C ATOM 1374 N ALA A 181 -13.549 64.126 -1.767 1.00 84.04 N ANISOU 1374 N ALA A 181 9317 11976 10638 908 -1642 -1296 N ATOM 1375 CA ALA A 181 -12.407 63.270 -1.465 1.00 83.65 C ANISOU 1375 CA ALA A 181 9105 11964 10715 891 -1837 -1266 C ATOM 1376 C ALA A 181 -11.093 63.973 -1.800 1.00 83.26 C ANISOU 1376 C ALA A 181 8865 11635 11135 820 -1779 -1526 C ATOM 1377 O ALA A 181 -11.053 64.824 -2.687 1.00 82.20 O ANISOU 1377 O ALA A 181 8785 11192 11257 785 -1504 -1621 O ATOM 1378 CB ALA A 181 -12.525 61.955 -2.226 1.00 82.06 C ANISOU 1378 CB ALA A 181 8986 11692 10499 904 -1778 -919 C ATOM 1379 N PRO A 182 -10.012 63.626 -1.083 1.00 84.70 N ANISOU 1379 N PRO A 182 8818 11917 11448 807 -2036 -1638 N ATOM 1380 CA PRO A 182 -8.711 64.271 -1.295 1.00 86.20 C ANISOU 1380 CA PRO A 182 8769 11845 12138 733 -2002 -1925 C ATOM 1381 C PRO A 182 -8.167 64.108 -2.712 1.00 84.91 C ANISOU 1381 C PRO A 182 8630 11233 12398 687 -1679 -1815 C ATOM 1382 O PRO A 182 -7.544 65.035 -3.227 1.00 85.72 O ANISOU 1382 O PRO A 182 8652 11016 12900 622 -1460 -2053 O ATOM 1383 CB PRO A 182 -7.798 63.566 -0.284 1.00 88.81 C ANISOU 1383 CB PRO A 182 8853 12418 12473 756 -2399 -1960 C ATOM 1384 CG PRO A 182 -8.514 62.312 0.086 1.00 87.99 C ANISOU 1384 CG PRO A 182 8897 12596 11941 849 -2547 -1587 C ATOM 1385 CD PRO A 182 -9.962 62.652 0.019 1.00 86.14 C ANISOU 1385 CD PRO A 182 8942 12467 11321 871 -2380 -1509 C ATOM 1386 N GLU A 183 -8.398 62.955 -3.332 1.00 83.70 N ANISOU 1386 N GLU A 183 8598 11040 12163 711 -1618 -1472 N ATOM 1387 CA GLU A 183 -7.924 62.723 -4.695 1.00 83.95 C ANISOU 1387 CA GLU A 183 8701 10652 12546 653 -1288 -1364 C ATOM 1388 C GLU A 183 -8.665 63.608 -5.690 1.00 81.88 C ANISOU 1388 C GLU A 183 8703 10164 12244 640 -951 -1365 C ATOM 1389 O GLU A 183 -8.189 63.855 -6.799 1.00 80.71 O ANISOU 1389 O GLU A 183 8636 9622 12407 587 -632 -1366 O ATOM 1390 CB GLU A 183 -8.065 61.251 -5.087 1.00 83.95 C ANISOU 1390 CB GLU A 183 8779 10677 12440 666 -1290 -1016 C ATOM 1391 CG GLU A 183 -9.486 60.711 -5.040 1.00 84.11 C ANISOU 1391 CG GLU A 183 9045 10961 11950 722 -1323 -766 C ATOM 1392 CD GLU A 183 -9.890 60.234 -3.657 1.00 87.39 C ANISOU 1392 CD GLU A 183 9381 11814 12012 804 -1670 -715 C ATOM 1393 OE1 GLU A 183 -9.280 60.689 -2.666 1.00 90.40 O ANISOU 1393 OE1 GLU A 183 9562 12345 12441 823 -1909 -929 O ATOM 1394 OE2 GLU A 183 -10.815 59.398 -3.563 1.00 86.70 O ANISOU 1394 OE2 GLU A 183 9436 11913 11592 847 -1693 -470 O ATOM 1395 N VAL A 184 -9.836 64.082 -5.280 1.00 81.90 N ANISOU 1395 N VAL A 184 8845 10407 11866 699 -1013 -1354 N ATOM 1396 CA VAL A 184 -10.634 64.984 -6.096 1.00 81.26 C ANISOU 1396 CA VAL A 184 8993 10152 11731 719 -742 -1337 C ATOM 1397 C VAL A 184 -10.111 66.412 -5.983 1.00 85.56 C ANISOU 1397 C VAL A 184 9431 10487 12592 693 -589 -1670 C ATOM 1398 O VAL A 184 -9.877 67.077 -6.993 1.00 86.35 O ANISOU 1398 O VAL A 184 9644 10214 12950 677 -259 -1691 O ATOM 1399 CB VAL A 184 -12.115 64.940 -5.682 1.00 77.05 C ANISOU 1399 CB VAL A 184 8609 9935 10729 796 -856 -1198 C ATOM 1400 CG1 VAL A 184 -12.863 66.151 -6.213 1.00 76.47 C ANISOU 1400 CG1 VAL A 184 8689 9710 10656 839 -631 -1246 C ATOM 1401 CG2 VAL A 184 -12.752 63.652 -6.161 1.00 73.68 C ANISOU 1401 CG2 VAL A 184 8332 9615 10050 810 -895 -868 C ATOM 1402 N ILE A 185 -9.918 66.874 -4.752 1.00 87.79 N ANISOU 1402 N ILE A 185 9507 11000 12849 685 -812 -1936 N ATOM 1403 CA ILE A 185 -9.430 68.229 -4.523 1.00 90.44 C ANISOU 1403 CA ILE A 185 9710 11154 13499 641 -668 -2304 C ATOM 1404 C ILE A 185 -8.003 68.398 -5.048 1.00 93.42 C ANISOU 1404 C ILE A 185 9904 11154 14438 558 -503 -2481 C ATOM 1405 O ILE A 185 -7.595 69.499 -5.412 1.00 94.97 O ANISOU 1405 O ILE A 185 10059 11028 14995 520 -214 -2716 O ATOM 1406 CB ILE A 185 -9.527 68.641 -3.027 1.00 89.84 C ANISOU 1406 CB ILE A 185 9458 11437 13239 626 -961 -2590 C ATOM 1407 CG1 ILE A 185 -8.452 67.953 -2.185 1.00 91.95 C ANISOU 1407 CG1 ILE A 185 9453 11892 13594 582 -1312 -2719 C ATOM 1408 CG2 ILE A 185 -10.911 68.341 -2.473 1.00 88.97 C ANISOU 1408 CG2 ILE A 185 9529 11683 12593 703 -1097 -2403 C ATOM 1409 CD1 ILE A 185 -7.357 68.887 -1.721 1.00 95.72 C ANISOU 1409 CD1 ILE A 185 9637 12240 14491 488 -1327 -3178 C ATOM 1410 N SER A 186 -7.255 67.300 -5.105 1.00 94.81 N ANISOU 1410 N SER A 186 9963 11338 14723 533 -650 -2363 N ATOM 1411 CA SER A 186 -5.889 67.338 -5.613 1.00 97.65 C ANISOU 1411 CA SER A 186 10123 11318 15662 453 -483 -2516 C ATOM 1412 C SER A 186 -5.864 67.140 -7.126 1.00 97.40 C ANISOU 1412 C SER A 186 10350 10866 15792 440 -61 -2282 C ATOM 1413 O SER A 186 -4.800 66.976 -7.724 1.00 99.61 O ANISOU 1413 O SER A 186 10521 10786 16541 371 145 -2343 O ATOM 1414 CB SER A 186 -5.021 66.289 -4.917 1.00 98.92 C ANISOU 1414 CB SER A 186 9997 11661 15927 438 -839 -2510 C ATOM 1415 OG SER A 186 -5.551 64.989 -5.096 1.00 97.22 O ANISOU 1415 OG SER A 186 9939 11624 15376 493 -952 -2121 O ATOM 1416 N GLY A 187 -7.046 67.153 -7.733 1.00 94.97 N ANISOU 1416 N GLY A 187 10385 10607 15092 505 64 -2023 N ATOM 1417 CA GLY A 187 -7.176 67.079 -9.177 1.00 93.61 C ANISOU 1417 CA GLY A 187 10520 10076 14970 501 448 -1803 C ATOM 1418 C GLY A 187 -6.593 65.823 -9.788 1.00 91.89 C ANISOU 1418 C GLY A 187 10324 9729 14859 441 495 -1609 C ATOM 1419 O GLY A 187 -6.056 65.853 -10.895 1.00 91.05 O ANISOU 1419 O GLY A 187 10368 9205 15024 387 868 -1565 O ATOM 1420 N ARG A 188 -6.697 64.714 -9.065 1.00 92.18 N ANISOU 1420 N ARG A 188 10227 10106 14690 452 148 -1489 N ATOM 1421 CA ARG A 188 -6.165 63.444 -9.539 1.00 92.32 C ANISOU 1421 CA ARG A 188 10234 10013 14830 398 190 -1300 C ATOM 1422 C ARG A 188 -7.295 62.539 -10.019 1.00 88.27 C ANISOU 1422 C ARG A 188 10016 9690 13832 424 165 -969 C ATOM 1423 O ARG A 188 -8.403 62.584 -9.485 1.00 88.54 O ANISOU 1423 O ARG A 188 10131 10079 13432 500 -54 -888 O ATOM 1424 CB ARG A 188 -5.358 62.763 -8.434 1.00 95.48 C ANISOU 1424 CB ARG A 188 10250 10614 15414 400 -156 -1380 C ATOM 1425 CG ARG A 188 -4.454 61.650 -8.923 1.00 99.53 C ANISOU 1425 CG ARG A 188 10658 10889 16270 337 -43 -1251 C ATOM 1426 CD ARG A 188 -3.271 61.478 -7.992 1.00104.74 C ANISOU 1426 CD ARG A 188 10868 11583 17347 338 -307 -1433 C ATOM 1427 NE ARG A 188 -2.614 62.756 -7.731 1.00109.15 N ANISOU 1427 NE ARG A 188 11227 11981 18264 306 -264 -1808 N ATOM 1428 CZ ARG A 188 -1.419 62.881 -7.164 1.00114.25 C ANISOU 1428 CZ ARG A 188 11461 12539 19411 278 -414 -2054 C ATOM 1429 NH1 ARG A 188 -0.738 61.802 -6.802 1.00115.81 N ANISOU 1429 NH1 ARG A 188 11402 12792 19809 296 -631 -1932 N ATOM 1430 NH2 ARG A 188 -0.901 64.086 -6.965 1.00116.93 N ANISOU 1430 NH2 ARG A 188 11627 12723 20080 232 -344 -2427 N ATOM 1431 N LEU A 189 -7.017 61.726 -11.033 1.00 84.13 N ANISOU 1431 N LEU A 189 9648 8914 13405 350 411 -802 N ATOM 1432 CA LEU A 189 -8.034 60.840 -11.591 1.00 80.41 C ANISOU 1432 CA LEU A 189 9450 8592 12510 347 413 -526 C ATOM 1433 C LEU A 189 -8.397 59.692 -10.649 1.00 77.47 C ANISOU 1433 C LEU A 189 8914 8601 11919 383 80 -385 C ATOM 1434 O LEU A 189 -7.561 59.208 -9.886 1.00 76.73 O ANISOU 1434 O LEU A 189 8524 8553 12078 387 -80 -431 O ATOM 1435 CB LEU A 189 -7.625 60.315 -12.973 1.00 81.12 C ANISOU 1435 CB LEU A 189 9780 8291 12748 235 802 -419 C ATOM 1436 CG LEU A 189 -6.144 60.263 -13.356 1.00 84.10 C ANISOU 1436 CG LEU A 189 10007 8225 13722 140 1088 -551 C ATOM 1437 CD1 LEU A 189 -5.362 59.335 -12.439 1.00 87.55 C ANISOU 1437 CD1 LEU A 189 10054 8769 14444 135 860 -557 C ATOM 1438 CD2 LEU A 189 -5.997 59.831 -14.806 1.00 82.77 C ANISOU 1438 CD2 LEU A 189 10179 7684 13585 24 1519 -437 C ATOM 1439 N TYR A 190 -9.656 59.266 -10.716 1.00 75.34 N ANISOU 1439 N TYR A 190 8836 8597 11192 417 -18 -207 N ATOM 1440 CA TYR A 190 -10.183 58.246 -9.817 1.00 73.28 C ANISOU 1440 CA TYR A 190 8460 8696 10686 463 -291 -62 C ATOM 1441 C TYR A 190 -11.154 57.320 -10.533 1.00 72.41 C ANISOU 1441 C TYR A 190 8583 8652 10278 420 -204 153 C ATOM 1442 O TYR A 190 -11.581 57.598 -11.651 1.00 72.95 O ANISOU 1442 O TYR A 190 8918 8557 10243 369 0 181 O ATOM 1443 CB TYR A 190 -10.898 58.902 -8.639 1.00 73.14 C ANISOU 1443 CB TYR A 190 8354 9042 10394 573 -585 -145 C ATOM 1444 CG TYR A 190 -11.907 59.950 -9.052 1.00 72.99 C ANISOU 1444 CG TYR A 190 8544 9047 10143 612 -518 -189 C ATOM 1445 CD1 TYR A 190 -13.203 59.598 -9.413 1.00 71.27 C ANISOU 1445 CD1 TYR A 190 8521 8994 9564 633 -534 -22 C ATOM 1446 CD2 TYR A 190 -11.562 61.296 -9.079 1.00 73.84 C ANISOU 1446 CD2 TYR A 190 8631 8998 10427 631 -433 -400 C ATOM 1447 CE1 TYR A 190 -14.126 60.560 -9.787 1.00 70.19 C ANISOU 1447 CE1 TYR A 190 8545 8874 9248 687 -495 -42 C ATOM 1448 CE2 TYR A 190 -12.477 62.261 -9.451 1.00 72.45 C ANISOU 1448 CE2 TYR A 190 8635 8823 10072 686 -357 -412 C ATOM 1449 CZ TYR A 190 -13.756 61.889 -9.804 1.00 70.83 C ANISOU 1449 CZ TYR A 190 8613 8791 9508 722 -402 -221 C ATOM 1450 OH TYR A 190 -14.662 62.853 -10.174 1.00 65.81 O ANISOU 1450 OH TYR A 190 8127 8150 8727 795 -348 -213 O ATOM 1451 N ALA A 191 -11.515 56.228 -9.867 1.00 73.49 N ANISOU 1451 N ALA A 191 8621 9034 10268 443 -362 300 N ATOM 1452 CA ALA A 191 -12.444 55.257 -10.430 1.00 73.45 C ANISOU 1452 CA ALA A 191 8789 9105 10015 390 -284 475 C ATOM 1453 C ALA A 191 -13.878 55.782 -10.428 1.00 74.23 C ANISOU 1453 C ALA A 191 9041 9446 9717 447 -397 485 C ATOM 1454 O ALA A 191 -14.563 55.737 -11.453 1.00 75.16 O ANISOU 1454 O ALA A 191 9383 9498 9674 388 -275 532 O ATOM 1455 CB ALA A 191 -12.356 53.942 -9.676 1.00 72.61 C ANISOU 1455 CB ALA A 191 8513 9149 9925 406 -375 630 C ATOM 1456 N GLY A 192 -14.322 56.284 -9.277 1.00 73.81 N ANISOU 1456 N GLY A 192 8863 9669 9513 560 -631 435 N ATOM 1457 CA GLY A 192 -15.676 56.790 -9.133 1.00 71.82 C ANISOU 1457 CA GLY A 192 8708 9638 8944 624 -731 439 C ATOM 1458 C GLY A 192 -16.292 56.574 -7.758 1.00 71.05 C ANISOU 1458 C GLY A 192 8474 9875 8646 717 -943 461 C ATOM 1459 O GLY A 192 -16.528 57.538 -7.026 1.00 68.63 O ANISOU 1459 O GLY A 192 8119 9697 8262 794 -1059 337 O ATOM 1460 N PRO A 193 -16.562 55.304 -7.401 1.00 72.39 N ANISOU 1460 N PRO A 193 8600 10172 8734 705 -960 617 N ATOM 1461 CA PRO A 193 -17.230 54.938 -6.144 1.00 71.51 C ANISOU 1461 CA PRO A 193 8407 10361 8403 793 -1108 676 C ATOM 1462 C PRO A 193 -16.512 55.405 -4.879 1.00 70.60 C ANISOU 1462 C PRO A 193 8151 10384 8291 879 -1295 584 C ATOM 1463 O PRO A 193 -17.182 55.859 -3.952 1.00 69.90 O ANISOU 1463 O PRO A 193 8061 10523 7977 953 -1409 528 O ATOM 1464 CB PRO A 193 -17.247 53.408 -6.194 1.00 73.03 C ANISOU 1464 CB PRO A 193 8575 10553 8618 751 -1018 872 C ATOM 1465 CG PRO A 193 -17.221 53.082 -7.638 1.00 73.27 C ANISOU 1465 CG PRO A 193 8727 10342 8772 623 -821 889 C ATOM 1466 CD PRO A 193 -16.344 54.127 -8.260 1.00 73.50 C ANISOU 1466 CD PRO A 193 8794 10150 8983 598 -785 748 C ATOM 1467 N GLU A 194 -15.187 55.286 -4.836 1.00 71.23 N ANISOU 1467 N GLU A 194 8109 10327 8627 864 -1326 557 N ATOM 1468 CA GLU A 194 -14.421 55.671 -3.648 1.00 74.65 C ANISOU 1468 CA GLU A 194 8386 10908 9070 939 -1551 454 C ATOM 1469 C GLU A 194 -14.619 57.142 -3.291 1.00 73.42 C ANISOU 1469 C GLU A 194 8239 10816 8841 960 -1626 199 C ATOM 1470 O GLU A 194 -14.619 57.515 -2.117 1.00 73.47 O ANISOU 1470 O GLU A 194 8184 11058 8674 1024 -1818 98 O ATOM 1471 CB GLU A 194 -12.928 55.370 -3.823 1.00 78.47 C ANISOU 1471 CB GLU A 194 8698 11191 9927 911 -1570 444 C ATOM 1472 CG GLU A 194 -12.573 54.599 -5.083 1.00 79.82 C ANISOU 1472 CG GLU A 194 8914 11051 10365 811 -1312 568 C ATOM 1473 CD GLU A 194 -12.554 55.477 -6.317 1.00 80.33 C ANISOU 1473 CD GLU A 194 9112 10838 10573 719 -1100 425 C ATOM 1474 OE1 GLU A 194 -11.541 56.174 -6.539 1.00 82.39 O ANISOU 1474 OE1 GLU A 194 9277 10888 11138 690 -1065 261 O ATOM 1475 OE2 GLU A 194 -13.555 55.470 -7.062 1.00 78.87 O ANISOU 1475 OE2 GLU A 194 9126 10643 10200 680 -969 478 O ATOM 1476 N VAL A 195 -14.787 57.969 -4.316 1.00 72.31 N ANISOU 1476 N VAL A 195 8190 10456 8827 906 -1458 97 N ATOM 1477 CA VAL A 195 -15.096 59.377 -4.129 1.00 72.45 C ANISOU 1477 CA VAL A 195 8230 10485 8814 927 -1462 -124 C ATOM 1478 C VAL A 195 -16.465 59.536 -3.481 1.00 70.75 C ANISOU 1478 C VAL A 195 8096 10526 8259 988 -1510 -98 C ATOM 1479 O VAL A 195 -16.668 60.411 -2.640 1.00 72.02 O ANISOU 1479 O VAL A 195 8224 10821 8320 1024 -1587 -278 O ATOM 1480 CB VAL A 195 -15.067 60.128 -5.468 1.00 72.92 C ANISOU 1480 CB VAL A 195 8405 10230 9071 879 -1237 -173 C ATOM 1481 CG1 VAL A 195 -15.568 61.558 -5.299 1.00 74.82 C ANISOU 1481 CG1 VAL A 195 8675 10469 9282 919 -1202 -361 C ATOM 1482 CG2 VAL A 195 -13.660 60.110 -6.034 1.00 73.18 C ANISOU 1482 CG2 VAL A 195 8353 9970 9480 812 -1140 -241 C ATOM 1483 N ASP A 196 -17.401 58.676 -3.867 1.00 69.12 N ANISOU 1483 N ASP A 196 7986 10374 7902 989 -1444 106 N ATOM 1484 CA ASP A 196 -18.732 58.695 -3.276 1.00 70.68 C ANISOU 1484 CA ASP A 196 8238 10787 7830 1042 -1460 141 C ATOM 1485 C ASP A 196 -18.722 58.212 -1.831 1.00 73.43 C ANISOU 1485 C ASP A 196 8535 11405 7958 1098 -1600 157 C ATOM 1486 O ASP A 196 -19.445 58.741 -0.989 1.00 72.97 O ANISOU 1486 O ASP A 196 8504 11517 7705 1142 -1624 64 O ATOM 1487 CB ASP A 196 -19.706 57.862 -4.108 1.00 70.92 C ANISOU 1487 CB ASP A 196 8355 10791 7802 1016 -1352 329 C ATOM 1488 CG ASP A 196 -20.579 58.717 -4.993 1.00 71.37 C ANISOU 1488 CG ASP A 196 8493 10747 7878 1021 -1273 288 C ATOM 1489 OD1 ASP A 196 -20.644 59.932 -4.728 1.00 73.69 O ANISOU 1489 OD1 ASP A 196 8774 11022 8202 1065 -1278 133 O ATOM 1490 OD2 ASP A 196 -21.200 58.184 -5.938 1.00 69.55 O ANISOU 1490 OD2 ASP A 196 8334 10456 7635 983 -1210 408 O ATOM 1491 N ILE A 197 -17.903 57.202 -1.552 1.00 77.31 N ANISOU 1491 N ILE A 197 8966 11925 8483 1101 -1676 286 N ATOM 1492 CA ILE A 197 -17.764 56.686 -0.196 1.00 82.53 C ANISOU 1492 CA ILE A 197 9603 12842 8913 1174 -1829 341 C ATOM 1493 C ILE A 197 -17.277 57.782 0.745 1.00 87.60 C ANISOU 1493 C ILE A 197 10197 13613 9473 1196 -1998 83 C ATOM 1494 O ILE A 197 -17.823 57.965 1.834 1.00 90.62 O ANISOU 1494 O ILE A 197 10645 14229 9557 1245 -2061 31 O ATOM 1495 CB ILE A 197 -16.779 55.502 -0.138 1.00 83.69 C ANISOU 1495 CB ILE A 197 9664 12959 9176 1191 -1898 536 C ATOM 1496 CG1 ILE A 197 -17.181 54.417 -1.140 1.00 80.63 C ANISOU 1496 CG1 ILE A 197 9318 12409 8908 1140 -1692 754 C ATOM 1497 CG2 ILE A 197 -16.709 54.934 1.276 1.00 86.87 C ANISOU 1497 CG2 ILE A 197 10074 13641 9291 1295 -2066 642 C ATOM 1498 CD1 ILE A 197 -18.567 53.860 -0.913 1.00 79.52 C ANISOU 1498 CD1 ILE A 197 9283 12395 8535 1161 -1568 877 C ATOM 1499 N TRP A 198 -16.254 58.512 0.310 1.00 88.97 N ANISOU 1499 N TRP A 198 10261 13620 9923 1148 -2045 -97 N ATOM 1500 CA TRP A 198 -15.670 59.584 1.109 1.00 92.38 C ANISOU 1500 CA TRP A 198 10613 14144 10343 1143 -2198 -393 C ATOM 1501 C TRP A 198 -16.704 60.653 1.444 1.00 91.32 C ANISOU 1501 C TRP A 198 10577 14081 10040 1140 -2097 -576 C ATOM 1502 O TRP A 198 -16.714 61.191 2.550 1.00 93.96 O ANISOU 1502 O TRP A 198 10916 14620 10165 1149 -2213 -767 O ATOM 1503 CB TRP A 198 -14.490 60.215 0.369 1.00 95.00 C ANISOU 1503 CB TRP A 198 10798 14208 11088 1078 -2185 -567 C ATOM 1504 CG TRP A 198 -13.566 60.986 1.259 1.00102.12 C ANISOU 1504 CG TRP A 198 11549 15212 12039 1063 -2397 -866 C ATOM 1505 CD1 TRP A 198 -12.399 60.540 1.815 1.00106.45 C ANISOU 1505 CD1 TRP A 198 11922 15842 12682 1079 -2653 -889 C ATOM 1506 CD2 TRP A 198 -13.728 62.338 1.701 1.00105.62 C ANISOU 1506 CD2 TRP A 198 11984 15685 12460 1024 -2378 -1201 C ATOM 1507 NE1 TRP A 198 -11.826 61.532 2.573 1.00109.91 N ANISOU 1507 NE1 TRP A 198 12240 16381 13141 1044 -2822 -1239 N ATOM 1508 CE2 TRP A 198 -12.622 62.646 2.519 1.00110.67 C ANISOU 1508 CE2 TRP A 198 12443 16438 13167 1001 -2636 -1446 C ATOM 1509 CE3 TRP A 198 -14.700 63.320 1.484 1.00105.58 C ANISOU 1509 CE3 TRP A 198 12092 15614 12410 1007 -2164 -1322 C ATOM 1510 CZ2 TRP A 198 -12.463 63.892 3.120 1.00114.73 C ANISOU 1510 CZ2 TRP A 198 12897 17003 13693 941 -2669 -1835 C ATOM 1511 CZ3 TRP A 198 -14.542 64.555 2.084 1.00109.00 C ANISOU 1511 CZ3 TRP A 198 12467 16075 12874 959 -2169 -1681 C ATOM 1512 CH2 TRP A 198 -13.431 64.832 2.889 1.00113.62 C ANISOU 1512 CH2 TRP A 198 12882 16774 13515 916 -2410 -1949 C ATOM 1513 N SER A 199 -17.572 60.953 0.483 1.00 87.43 N ANISOU 1513 N SER A 199 10161 13415 9641 1125 -1880 -519 N ATOM 1514 CA SER A 199 -18.630 61.934 0.681 1.00 86.10 C ANISOU 1514 CA SER A 199 10063 13272 9381 1135 -1754 -655 C ATOM 1515 C SER A 199 -19.653 61.420 1.681 1.00 84.51 C ANISOU 1515 C SER A 199 9954 13325 8828 1183 -1759 -568 C ATOM 1516 O SER A 199 -20.219 62.187 2.454 1.00 84.37 O ANISOU 1516 O SER A 199 9977 13412 8668 1187 -1714 -745 O ATOM 1517 CB SER A 199 -19.323 62.256 -0.645 1.00 86.20 C ANISOU 1517 CB SER A 199 10127 13047 9580 1132 -1558 -563 C ATOM 1518 OG SER A 199 -18.436 62.889 -1.549 1.00 87.43 O ANISOU 1518 OG SER A 199 10238 12939 10043 1093 -1497 -656 O ATOM 1519 N SER A 200 -19.896 60.116 1.655 1.00 83.66 N ANISOU 1519 N SER A 200 9888 13293 8606 1212 -1773 -301 N ATOM 1520 CA SER A 200 -20.840 59.510 2.580 1.00 84.22 C ANISOU 1520 CA SER A 200 10059 13573 8368 1261 -1731 -193 C ATOM 1521 C SER A 200 -20.217 59.433 3.964 1.00 87.68 C ANISOU 1521 C SER A 200 10533 14258 8523 1293 -1913 -274 C ATOM 1522 O SER A 200 -20.910 59.528 4.976 1.00 90.10 O ANISOU 1522 O SER A 200 10956 14743 8534 1320 -1867 -321 O ATOM 1523 CB SER A 200 -21.238 58.115 2.099 1.00 82.97 C ANISOU 1523 CB SER A 200 9924 13389 8211 1279 -1657 111 C ATOM 1524 OG SER A 200 -21.849 58.177 0.822 1.00 81.56 O ANISOU 1524 OG SER A 200 9725 13012 8252 1240 -1521 165 O ATOM 1525 N GLY A 201 -18.898 59.268 3.994 1.00 88.74 N ANISOU 1525 N GLY A 201 10568 14397 8751 1289 -2122 -296 N ATOM 1526 CA GLY A 201 -18.161 59.181 5.240 1.00 92.40 C ANISOU 1526 CA GLY A 201 11043 15111 8953 1326 -2367 -371 C ATOM 1527 C GLY A 201 -18.268 60.446 6.066 1.00 95.83 C ANISOU 1527 C GLY A 201 11515 15667 9229 1282 -2403 -724 C ATOM 1528 O GLY A 201 -18.353 60.392 7.293 1.00 99.84 O ANISOU 1528 O GLY A 201 12143 16437 9354 1313 -2512 -781 O ATOM 1529 N VAL A 202 -18.262 61.592 5.394 1.00 94.77 N ANISOU 1529 N VAL A 202 11295 15330 9382 1209 -2288 -962 N ATOM 1530 CA VAL A 202 -18.389 62.871 6.079 1.00 96.42 C ANISOU 1530 CA VAL A 202 11523 15603 9511 1150 -2261 -1326 C ATOM 1531 C VAL A 202 -19.855 63.206 6.346 1.00 95.80 C ANISOU 1531 C VAL A 202 11590 15537 9272 1157 -1995 -1330 C ATOM 1532 O VAL A 202 -20.164 64.029 7.207 1.00 97.87 O ANISOU 1532 O VAL A 202 11922 15904 9360 1114 -1939 -1594 O ATOM 1533 CB VAL A 202 -17.712 64.014 5.293 1.00 95.71 C ANISOU 1533 CB VAL A 202 11267 15258 9840 1074 -2210 -1588 C ATOM 1534 CG1 VAL A 202 -16.220 63.768 5.181 1.00 96.93 C ANISOU 1534 CG1 VAL A 202 11249 15393 10185 1054 -2463 -1642 C ATOM 1535 CG2 VAL A 202 -18.313 64.135 3.920 1.00 92.69 C ANISOU 1535 CG2 VAL A 202 10876 14578 9765 1084 -1963 -1430 C ATOM 1536 N ILE A 203 -20.755 62.564 5.606 1.00 93.53 N ANISOU 1536 N ILE A 203 11337 15134 9067 1202 -1823 -1056 N ATOM 1537 CA ILE A 203 -22.186 62.716 5.844 1.00 95.15 C ANISOU 1537 CA ILE A 203 11645 15341 9168 1219 -1576 -1029 C ATOM 1538 C ILE A 203 -22.568 62.052 7.159 1.00 98.55 C ANISOU 1538 C ILE A 203 12250 16035 9158 1253 -1585 -968 C ATOM 1539 O ILE A 203 -23.290 62.629 7.975 1.00101.62 O ANISOU 1539 O ILE A 203 12749 16498 9366 1232 -1430 -1137 O ATOM 1540 CB ILE A 203 -23.024 62.107 4.704 1.00 93.34 C ANISOU 1540 CB ILE A 203 11379 14936 9150 1253 -1428 -760 C ATOM 1541 CG1 ILE A 203 -23.042 63.048 3.499 1.00 93.05 C ANISOU 1541 CG1 ILE A 203 11231 14635 9487 1231 -1346 -842 C ATOM 1542 CG2 ILE A 203 -24.449 61.835 5.167 1.00 93.24 C ANISOU 1542 CG2 ILE A 203 11455 14974 8997 1284 -1212 -681 C ATOM 1543 CD1 ILE A 203 -23.967 62.602 2.379 1.00 90.64 C ANISOU 1543 CD1 ILE A 203 10901 14181 9356 1263 -1229 -614 C ATOM 1544 N LEU A 204 -22.065 60.839 7.361 1.00 97.85 N ANISOU 1544 N LEU A 204 12201 16070 8907 1310 -1742 -719 N ATOM 1545 CA LEU A 204 -22.332 60.080 8.576 1.00 99.10 C ANISOU 1545 CA LEU A 204 12556 16472 8627 1368 -1752 -600 C ATOM 1546 C LEU A 204 -21.824 60.828 9.806 1.00101.40 C ANISOU 1546 C LEU A 204 12955 16990 8582 1335 -1903 -890 C ATOM 1547 O LEU A 204 -22.362 60.681 10.903 1.00103.73 O ANISOU 1547 O LEU A 204 13470 17465 8478 1356 -1816 -902 O ATOM 1548 CB LEU A 204 -21.688 58.695 8.485 1.00 98.52 C ANISOU 1548 CB LEU A 204 12476 16460 8497 1449 -1910 -267 C ATOM 1549 CG LEU A 204 -21.969 57.701 9.612 1.00101.35 C ANISOU 1549 CG LEU A 204 13052 17035 8422 1543 -1891 -48 C ATOM 1550 CD1 LEU A 204 -23.463 57.583 9.867 1.00101.44 C ANISOU 1550 CD1 LEU A 204 13205 16996 8341 1544 -1524 -1 C ATOM 1551 CD2 LEU A 204 -21.374 56.344 9.273 1.00100.56 C ANISOU 1551 CD2 LEU A 204 12898 16918 8390 1628 -1993 309 C ATOM 1552 N TYR A 205 -20.791 61.638 9.608 1.00101.22 N ANISOU 1552 N TYR A 205 12784 16947 8727 1274 -2110 -1143 N ATOM 1553 CA TYR A 205 -20.227 62.445 10.682 1.00106.09 C ANISOU 1553 CA TYR A 205 13464 17774 9072 1214 -2279 -1485 C ATOM 1554 C TYR A 205 -21.219 63.515 11.126 1.00107.92 C ANISOU 1554 C TYR A 205 13804 17966 9237 1133 -1982 -1770 C ATOM 1555 O TYR A 205 -21.476 63.678 12.317 1.00111.86 O ANISOU 1555 O TYR A 205 14513 18680 9308 1110 -1964 -1916 O ATOM 1556 CB TYR A 205 -18.917 63.092 10.224 1.00105.83 C ANISOU 1556 CB TYR A 205 13193 17672 9346 1152 -2529 -1717 C ATOM 1557 CG TYR A 205 -18.116 63.745 11.330 1.00109.53 C ANISOU 1557 CG TYR A 205 13684 18391 9541 1087 -2792 -2075 C ATOM 1558 CD1 TYR A 205 -18.331 65.071 11.682 1.00111.33 C ANISOU 1558 CD1 TYR A 205 13918 18589 9794 963 -2652 -2504 C ATOM 1559 CD2 TYR A 205 -17.136 63.037 12.015 1.00111.97 C ANISOU 1559 CD2 TYR A 205 13996 18965 9582 1149 -3186 -1990 C ATOM 1560 CE1 TYR A 205 -17.598 65.673 12.688 1.00116.30 C ANISOU 1560 CE1 TYR A 205 14563 19457 10168 880 -2896 -2875 C ATOM 1561 CE2 TYR A 205 -16.396 63.631 13.022 1.00116.68 C ANISOU 1561 CE2 TYR A 205 14604 19820 9910 1085 -3475 -2338 C ATOM 1562 CZ TYR A 205 -16.631 64.949 13.356 1.00118.30 C ANISOU 1562 CZ TYR A 205 14821 20000 10126 939 -3328 -2798 C ATOM 1563 OH TYR A 205 -15.900 65.546 14.359 1.00121.52 O ANISOU 1563 OH TYR A 205 15238 20674 10260 852 -3617 -3188 O ATOM 1564 N ALA A 206 -21.779 64.235 10.158 1.00104.83 N ANISOU 1564 N ALA A 206 13276 17288 9268 1095 -1740 -1838 N ATOM 1565 CA ALA A 206 -22.726 65.308 10.443 1.00105.62 C ANISOU 1565 CA ALA A 206 13428 17289 9414 1028 -1427 -2093 C ATOM 1566 C ALA A 206 -24.014 64.769 11.058 1.00107.29 C ANISOU 1566 C ALA A 206 13842 17558 9364 1069 -1164 -1936 C ATOM 1567 O ALA A 206 -24.695 65.462 11.812 1.00110.40 O ANISOU 1567 O ALA A 206 14359 17967 9621 1009 -929 -2166 O ATOM 1568 CB ALA A 206 -23.031 66.087 9.177 1.00102.36 C ANISOU 1568 CB ALA A 206 12815 16544 9534 1015 -1246 -2123 C ATOM 1569 N LEU A 207 -24.340 63.525 10.731 1.00105.30 N ANISOU 1569 N LEU A 207 13621 17314 9075 1164 -1169 -1559 N ATOM 1570 CA LEU A 207 -25.538 62.883 11.257 1.00105.65 C ANISOU 1570 CA LEU A 207 13838 17381 8922 1207 -895 -1389 C ATOM 1571 C LEU A 207 -25.336 62.464 12.707 1.00110.12 C ANISOU 1571 C LEU A 207 14695 18240 8905 1219 -953 -1413 C ATOM 1572 O LEU A 207 -26.294 62.348 13.470 1.00112.81 O ANISOU 1572 O LEU A 207 15239 18606 9018 1220 -663 -1413 O ATOM 1573 CB LEU A 207 -25.904 61.667 10.404 1.00102.14 C ANISOU 1573 CB LEU A 207 13316 16836 8659 1292 -869 -1000 C ATOM 1574 CG LEU A 207 -26.895 61.877 9.257 1.00 98.62 C ANISOU 1574 CG LEU A 207 12685 16115 8671 1293 -653 -931 C ATOM 1575 CD1 LEU A 207 -26.747 63.254 8.627 1.00 97.22 C ANISOU 1575 CD1 LEU A 207 12346 15770 8822 1236 -647 -1188 C ATOM 1576 CD2 LEU A 207 -26.710 60.790 8.210 1.00 95.74 C ANISOU 1576 CD2 LEU A 207 12203 15673 8501 1343 -762 -618 C ATOM 1577 N LEU A 208 -24.082 62.243 13.083 1.00111.21 N ANISOU 1577 N LEU A 208 14855 18592 8807 1234 -1328 -1433 N ATOM 1578 CA LEU A 208 -23.752 61.787 14.427 1.00114.27 C ANISOU 1578 CA LEU A 208 15530 19294 8595 1268 -1465 -1420 C ATOM 1579 C LEU A 208 -23.255 62.924 15.311 1.00119.49 C ANISOU 1579 C LEU A 208 16280 20127 8993 1153 -1583 -1866 C ATOM 1580 O LEU A 208 -23.412 62.883 16.530 1.00124.63 O ANISOU 1580 O LEU A 208 17234 21008 9110 1142 -1557 -1955 O ATOM 1581 CB LEU A 208 -22.697 60.681 14.365 1.00111.92 C ANISOU 1581 CB LEU A 208 15198 19150 8176 1381 -1837 -1117 C ATOM 1582 CG LEU A 208 -23.163 59.338 13.803 1.00107.82 C ANISOU 1582 CG LEU A 208 14667 18514 7787 1497 -1702 -661 C ATOM 1583 CD1 LEU A 208 -21.977 58.517 13.336 1.00105.66 C ANISOU 1583 CD1 LEU A 208 14236 18286 7626 1579 -2056 -421 C ATOM 1584 CD2 LEU A 208 -23.956 58.580 14.851 1.00110.53 C ANISOU 1584 CD2 LEU A 208 15344 18983 7669 1573 -1470 -465 C ATOM 1585 N CYS A 209 -22.659 63.939 14.693 1.00118.33 N ANISOU 1585 N CYS A 209 15882 19860 9218 1059 -1690 -2158 N ATOM 1586 CA CYS A 209 -22.032 65.022 15.442 1.00121.47 C ANISOU 1586 CA CYS A 209 16310 20407 9434 931 -1828 -2623 C ATOM 1587 C CYS A 209 -22.805 66.331 15.333 1.00121.16 C ANISOU 1587 C CYS A 209 16228 20145 9662 801 -1444 -2976 C ATOM 1588 O CYS A 209 -22.859 67.108 16.285 1.00124.97 O ANISOU 1588 O CYS A 209 16869 20752 9863 684 -1365 -3347 O ATOM 1589 CB CYS A 209 -20.590 65.224 14.972 1.00120.95 C ANISOU 1589 CB CYS A 209 15979 20379 9599 912 -2248 -2740 C ATOM 1590 SG CYS A 209 -19.636 63.694 14.877 1.00112.32 S ANISOU 1590 SG CYS A 209 14851 19469 8357 1078 -2678 -2290 S ATOM 1591 N GLY A 210 -23.401 66.569 14.171 1.00117.30 N ANISOU 1591 N GLY A 210 15529 19327 9714 824 -1206 -2858 N ATOM 1592 CA GLY A 210 -24.123 67.803 13.928 1.00117.39 C ANISOU 1592 CA GLY A 210 15454 19085 10064 732 -843 -3138 C ATOM 1593 C GLY A 210 -23.241 68.841 13.264 1.00116.64 C ANISOU 1593 C GLY A 210 15099 18837 10381 655 -951 -3420 C ATOM 1594 O GLY A 210 -23.686 69.944 12.955 1.00115.96 O ANISOU 1594 O GLY A 210 14907 18509 10643 588 -659 -3650 O ATOM 1595 N THR A 211 -21.980 68.483 13.046 1.00117.94 N ANISOU 1595 N THR A 211 15149 19122 10539 670 -1349 -3397 N ATOM 1596 CA THR A 211 -21.023 69.383 12.412 1.00118.87 C ANISOU 1596 CA THR A 211 15011 19080 11074 596 -1450 -3663 C ATOM 1597 C THR A 211 -20.171 68.661 11.371 1.00117.01 C ANISOU 1597 C THR A 211 14585 18764 11111 684 -1714 -3376 C ATOM 1598 O THR A 211 -20.280 67.448 11.196 1.00115.16 O ANISOU 1598 O THR A 211 14414 18618 10723 796 -1838 -2985 O ATOM 1599 CB THR A 211 -20.092 70.042 13.448 1.00123.07 C ANISOU 1599 CB THR A 211 15565 19845 11352 457 -1667 -4133 C ATOM 1600 OG1 THR A 211 -19.511 69.031 14.281 1.00124.99 O ANISOU 1600 OG1 THR A 211 15958 20460 11073 508 -2058 -4003 O ATOM 1601 CG2 THR A 211 -20.865 71.027 14.313 1.00125.81 C ANISOU 1601 CG2 THR A 211 16070 20192 11539 329 -1332 -4507 C ATOM 1602 N LEU A 212 -19.322 69.419 10.684 1.00117.68 N ANISOU 1602 N LEU A 212 14438 18653 11623 626 -1757 -3584 N ATOM 1603 CA LEU A 212 -18.441 68.871 9.659 1.00116.68 C ANISOU 1603 CA LEU A 212 14126 18399 11810 687 -1954 -3365 C ATOM 1604 C LEU A 212 -17.105 68.438 10.256 1.00123.30 C ANISOU 1604 C LEU A 212 14885 19486 12477 664 -2390 -3476 C ATOM 1605 O LEU A 212 -16.638 69.029 11.229 1.00130.14 O ANISOU 1605 O LEU A 212 15760 20548 13139 563 -2533 -3860 O ATOM 1606 CB LEU A 212 -18.198 69.910 8.562 1.00112.92 C ANISOU 1606 CB LEU A 212 13450 17543 11912 645 -1734 -3515 C ATOM 1607 CG LEU A 212 -19.408 70.338 7.733 1.00109.55 C ANISOU 1607 CG LEU A 212 13056 16834 11736 700 -1348 -3350 C ATOM 1608 CD1 LEU A 212 -19.035 71.466 6.789 1.00107.91 C ANISOU 1608 CD1 LEU A 212 12677 16264 12060 666 -1139 -3522 C ATOM 1609 CD2 LEU A 212 -19.957 69.154 6.961 1.00106.46 C ANISOU 1609 CD2 LEU A 212 12720 16417 11311 827 -1374 -2861 C ATOM 1610 N PRO A 213 -16.487 67.399 9.673 1.00121.53 N ANISOU 1610 N PRO A 213 14572 19253 12349 756 -2607 -3149 N ATOM 1611 CA PRO A 213 -15.163 66.945 10.114 1.00123.62 C ANISOU 1611 CA PRO A 213 14707 19715 12548 757 -3036 -3214 C ATOM 1612 C PRO A 213 -14.035 67.785 9.516 1.00124.98 C ANISOU 1612 C PRO A 213 14583 19661 13243 662 -3086 -3532 C ATOM 1613 O PRO A 213 -12.986 67.932 10.141 1.00128.30 O ANISOU 1613 O PRO A 213 14860 20254 13636 607 -3416 -3798 O ATOM 1614 CB PRO A 213 -15.096 65.515 9.579 1.00120.49 C ANISOU 1614 CB PRO A 213 14323 19317 12142 895 -3144 -2708 C ATOM 1615 CG PRO A 213 -15.946 65.544 8.361 1.00115.88 C ANISOU 1615 CG PRO A 213 13753 18406 11870 920 -2777 -2491 C ATOM 1616 CD PRO A 213 -17.065 66.507 8.653 1.00116.60 C ANISOU 1616 CD PRO A 213 13976 18455 11871 865 -2466 -2692 C ATOM 1617 N PHE A 214 -14.254 68.327 8.321 1.00122.43 N ANISOU 1617 N PHE A 214 14171 18952 13395 648 -2761 -3503 N ATOM 1618 CA PHE A 214 -13.255 69.162 7.664 1.00124.45 C ANISOU 1618 CA PHE A 214 14169 18927 14191 561 -2715 -3789 C ATOM 1619 C PHE A 214 -13.848 70.502 7.249 1.00126.18 C ANISOU 1619 C PHE A 214 14391 18859 14690 488 -2299 -4040 C ATOM 1620 O PHE A 214 -14.505 70.600 6.212 1.00123.64 O ANISOU 1620 O PHE A 214 14126 18256 14596 549 -1996 -3801 O ATOM 1621 CB PHE A 214 -12.683 68.454 6.435 1.00120.26 C ANISOU 1621 CB PHE A 214 13518 18137 14041 629 -2706 -3472 C ATOM 1622 CG PHE A 214 -12.112 67.096 6.726 1.00119.57 C ANISOU 1622 CG PHE A 214 13404 18271 13757 714 -3064 -3183 C ATOM 1623 CD1 PHE A 214 -11.036 66.952 7.584 1.00122.75 C ANISOU 1623 CD1 PHE A 214 13642 18909 14088 687 -3465 -3388 C ATOM 1624 CD2 PHE A 214 -12.657 65.963 6.147 1.00114.96 C ANISOU 1624 CD2 PHE A 214 12946 17656 13076 823 -3001 -2710 C ATOM 1625 CE1 PHE A 214 -10.511 65.701 7.853 1.00122.71 C ANISOU 1625 CE1 PHE A 214 13601 19094 13929 790 -3792 -3087 C ATOM 1626 CE2 PHE A 214 -12.135 64.711 6.412 1.00114.09 C ANISOU 1626 CE2 PHE A 214 12805 17719 12824 908 -3287 -2431 C ATOM 1627 CZ PHE A 214 -11.062 64.580 7.266 1.00118.20 C ANISOU 1627 CZ PHE A 214 13164 18463 13285 902 -3680 -2600 C ATOM 1628 N ASP A 215 -13.613 71.532 8.056 1.00129.86 N ANISOU 1628 N ASP A 215 14799 19399 15144 360 -2288 -4523 N ATOM 1629 CA ASP A 215 -14.126 72.864 7.755 1.00129.12 C ANISOU 1629 CA ASP A 215 14692 19018 15352 287 -1867 -4788 C ATOM 1630 C ASP A 215 -13.123 73.950 8.132 1.00132.72 C ANISOU 1630 C ASP A 215 14921 19397 16109 123 -1879 -5357 C ATOM 1631 O ASP A 215 -12.403 73.826 9.121 1.00135.78 O ANISOU 1631 O ASP A 215 15237 20092 16262 39 -2235 -5641 O ATOM 1632 CB ASP A 215 -15.460 73.102 8.466 1.00129.36 C ANISOU 1632 CB ASP A 215 14957 19192 15003 290 -1670 -4789 C ATOM 1633 CG ASP A 215 -16.219 74.288 7.901 1.00128.19 C ANISOU 1633 CG ASP A 215 14802 18687 15217 271 -1184 -4901 C ATOM 1634 OD1 ASP A 215 -16.102 74.547 6.684 1.00125.64 O ANISOU 1634 OD1 ASP A 215 14387 18011 15341 332 -985 -4737 O ATOM 1635 OD2 ASP A 215 -16.937 74.959 8.672 1.00130.29 O ANISOU 1635 OD2 ASP A 215 15166 19017 15321 201 -987 -5142 O ATOM 1636 N ASP A 216 -13.085 75.011 7.331 1.00133.29 N ANISOU 1636 N ASP A 216 14882 19055 16706 83 -1489 -5518 N ATOM 1637 CA ASP A 216 -12.208 76.149 7.578 1.00139.30 C ANISOU 1637 CA ASP A 216 15413 19667 17850 -82 -1401 -6080 C ATOM 1638 C ASP A 216 -12.652 77.325 6.718 1.00141.87 C ANISOU 1638 C ASP A 216 15714 19515 18673 -85 -844 -6150 C ATOM 1639 O ASP A 216 -12.917 77.163 5.527 1.00139.43 O ANISOU 1639 O ASP A 216 15453 18906 18618 42 -629 -5768 O ATOM 1640 CB ASP A 216 -10.755 75.789 7.254 1.00139.97 C ANISOU 1640 CB ASP A 216 15229 19693 18259 -114 -1682 -6171 C ATOM 1641 CG ASP A 216 -9.759 76.786 7.829 1.00145.61 C ANISOU 1641 CG ASP A 216 15671 20371 19283 -308 -1718 -6820 C ATOM 1642 OD1 ASP A 216 -10.177 77.881 8.262 1.00147.97 O ANISOU 1642 OD1 ASP A 216 15989 20597 19636 -423 -1431 -7198 O ATOM 1643 OD2 ASP A 216 -8.549 76.475 7.842 1.00147.40 O ANISOU 1643 OD2 ASP A 216 15645 20628 19734 -352 -2025 -6967 O ATOM 1644 N ASP A 217 -12.735 78.506 7.326 1.00147.90 N ANISOU 1644 N ASP A 217 16417 20211 19568 -229 -607 -6637 N ATOM 1645 CA ASP A 217 -13.099 79.719 6.601 1.00149.25 C ANISOU 1645 CA ASP A 217 16546 19909 20252 -231 -50 -6736 C ATOM 1646 C ASP A 217 -12.098 79.995 5.487 1.00147.74 C ANISOU 1646 C ASP A 217 16161 19308 20667 -217 100 -6732 C ATOM 1647 O ASP A 217 -12.474 80.373 4.377 1.00144.67 O ANISOU 1647 O ASP A 217 15830 18522 20615 -102 480 -6457 O ATOM 1648 CB ASP A 217 -13.166 80.916 7.551 1.00155.85 C ANISOU 1648 CB ASP A 217 17312 20745 21159 -422 172 -7335 C ATOM 1649 CG ASP A 217 -14.301 80.805 8.548 1.00158.00 C ANISOU 1649 CG ASP A 217 17815 21329 20888 -437 166 -7335 C ATOM 1650 OD1 ASP A 217 -15.372 80.282 8.176 1.00155.39 O ANISOU 1650 OD1 ASP A 217 17682 21006 20355 -273 248 -6854 O ATOM 1651 OD2 ASP A 217 -14.121 81.243 9.704 1.00162.73 O ANISOU 1651 OD2 ASP A 217 18401 22162 21269 -620 88 -7833 O ATOM 1652 N HIS A 218 -10.820 79.803 5.793 1.00150.58 N ANISOU 1652 N HIS A 218 16291 19759 21165 -331 -199 -7036 N ATOM 1653 CA HIS A 218 -9.768 79.941 4.797 1.00151.76 C ANISOU 1653 CA HIS A 218 16241 19522 21901 -329 -72 -7047 C ATOM 1654 C HIS A 218 -9.711 78.667 3.961 1.00147.74 C ANISOU 1654 C HIS A 218 15839 19037 21260 -166 -280 -6470 C ATOM 1655 O HIS A 218 -9.248 77.626 4.428 1.00148.09 O ANISOU 1655 O HIS A 218 15840 19421 21008 -161 -752 -6381 O ATOM 1656 CB HIS A 218 -8.422 80.199 5.477 1.00157.53 C ANISOU 1656 CB HIS A 218 16641 20338 22876 -519 -328 -7616 C ATOM 1657 CG HIS A 218 -7.452 80.960 4.627 1.00160.21 C ANISOU 1657 CG HIS A 218 16733 20158 23983 -582 23 -7852 C ATOM 1658 ND1 HIS A 218 -6.637 80.350 3.698 1.00158.33 N ANISOU 1658 ND1 HIS A 218 16396 19692 24072 -514 -17 -7607 N ATOM 1659 CD2 HIS A 218 -7.165 82.282 4.569 1.00164.08 C ANISOU 1659 CD2 HIS A 218 17058 20283 25001 -712 465 -8318 C ATOM 1660 CE1 HIS A 218 -5.892 81.264 3.103 1.00160.95 C ANISOU 1660 CE1 HIS A 218 16522 19537 25093 -596 389 -7907 C ATOM 1661 NE2 HIS A 218 -6.192 82.444 3.613 1.00164.42 N ANISOU 1661 NE2 HIS A 218 16913 19883 25675 -713 686 -8338 N ATOM 1662 N VAL A 219 -10.193 78.756 2.726 1.00144.21 N ANISOU 1662 N VAL A 219 15540 18225 21027 -30 81 -6077 N ATOM 1663 CA VAL A 219 -10.313 77.586 1.852 1.00139.22 C ANISOU 1663 CA VAL A 219 15056 17598 20245 118 -55 -5524 C ATOM 1664 C VAL A 219 -9.012 76.828 1.522 1.00137.41 C ANISOU 1664 C VAL A 219 14640 17321 20248 85 -294 -5516 C ATOM 1665 O VAL A 219 -9.007 75.600 1.555 1.00134.59 O ANISOU 1665 O VAL A 219 14346 17218 19573 152 -633 -5197 O ATOM 1666 CB VAL A 219 -11.100 77.904 0.554 1.00178.16 C ANISOU 1666 CB VAL A 219 20203 22151 25339 265 375 -5124 C ATOM 1667 CG1 VAL A 219 -12.458 77.218 0.578 1.00174.88 C ANISOU 1667 CG1 VAL A 219 20041 21997 24407 399 261 -4692 C ATOM 1668 CG2 VAL A 219 -11.256 79.407 0.377 1.00180.57 C ANISOU 1668 CG2 VAL A 219 20462 22081 26064 231 868 -5408 C ATOM 1669 N PRO A 220 -7.914 77.542 1.195 1.00138.94 N ANISOU 1669 N PRO A 220 14592 17163 21034 -17 -92 -5864 N ATOM 1670 CA PRO A 220 -6.683 76.788 0.924 1.00137.52 C ANISOU 1670 CA PRO A 220 14205 16929 21117 -49 -320 -5863 C ATOM 1671 C PRO A 220 -6.220 75.963 2.121 1.00137.01 C ANISOU 1671 C PRO A 220 13976 17372 20708 -101 -927 -6001 C ATOM 1672 O PRO A 220 -5.679 74.874 1.940 1.00135.43 O ANISOU 1672 O PRO A 220 13717 17265 20476 -51 -1209 -5757 O ATOM 1673 CB PRO A 220 -5.662 77.886 0.619 1.00141.85 C ANISOU 1673 CB PRO A 220 14485 17032 22380 -177 20 -6325 C ATOM 1674 CG PRO A 220 -6.472 79.018 0.118 1.00142.54 C ANISOU 1674 CG PRO A 220 14753 16798 22609 -140 558 -6322 C ATOM 1675 CD PRO A 220 -7.740 78.979 0.914 1.00142.08 C ANISOU 1675 CD PRO A 220 14895 17140 21948 -93 400 -6221 C ATOM 1676 N THR A 221 -6.441 76.472 3.328 1.00138.32 N ANISOU 1676 N THR A 221 14087 17859 20611 -195 -1113 -6378 N ATOM 1677 CA THR A 221 -6.070 75.745 4.535 1.00138.05 C ANISOU 1677 CA THR A 221 13944 18341 20168 -230 -1705 -6502 C ATOM 1678 C THR A 221 -7.104 74.668 4.864 1.00132.82 C ANISOU 1678 C THR A 221 13591 18063 18811 -90 -1942 -6018 C ATOM 1679 O THR A 221 -6.871 73.816 5.718 1.00133.94 O ANISOU 1679 O THR A 221 13709 18623 18561 -68 -2423 -5966 O ATOM 1680 CB THR A 221 -5.890 76.691 5.739 1.00142.53 C ANISOU 1680 CB THR A 221 14364 19124 20667 -402 -1822 -7121 C ATOM 1681 OG1 THR A 221 -7.146 77.292 6.072 1.00142.03 O ANISOU 1681 OG1 THR A 221 14570 19133 20260 -398 -1560 -7123 O ATOM 1682 CG2 THR A 221 -4.883 77.783 5.411 1.00144.74 C ANISOU 1682 CG2 THR A 221 14313 18995 21687 -555 -1548 -7636 C ATOM 1683 N LEU A 222 -8.243 74.715 4.177 1.00127.14 N ANISOU 1683 N LEU A 222 13155 17192 17961 12 -1598 -5662 N ATOM 1684 CA LEU A 222 -9.291 73.712 4.339 1.00123.21 C ANISOU 1684 CA LEU A 222 12939 16990 16887 143 -1747 -5197 C ATOM 1685 C LEU A 222 -8.957 72.448 3.553 1.00120.04 C ANISOU 1685 C LEU A 222 12555 16537 16517 252 -1882 -4737 C ATOM 1686 O LEU A 222 -9.126 71.333 4.049 1.00120.53 O ANISOU 1686 O LEU A 222 12696 16936 16165 323 -2217 -4474 O ATOM 1687 CB LEU A 222 -10.643 74.275 3.889 1.00120.60 C ANISOU 1687 CB LEU A 222 12859 16506 16458 207 -1340 -5019 C ATOM 1688 CG LEU A 222 -11.774 73.298 3.548 1.00117.13 C ANISOU 1688 CG LEU A 222 12688 16200 15614 356 -1358 -4481 C ATOM 1689 CD1 LEU A 222 -12.155 72.447 4.747 1.00118.78 C ANISOU 1689 CD1 LEU A 222 12997 16904 15230 373 -1733 -4413 C ATOM 1690 CD2 LEU A 222 -12.990 74.048 3.017 1.00114.27 C ANISOU 1690 CD2 LEU A 222 12500 15626 15290 415 -948 -4362 C ATOM 1691 N PHE A 223 -8.480 72.628 2.325 1.00116.42 N ANISOU 1691 N PHE A 223 12039 15638 16557 260 -1587 -4644 N ATOM 1692 CA PHE A 223 -8.073 71.502 1.494 1.00110.70 C ANISOU 1692 CA PHE A 223 11326 14805 15932 335 -1651 -4254 C ATOM 1693 C PHE A 223 -6.865 70.796 2.081 1.00108.53 C ANISOU 1693 C PHE A 223 10775 14702 15759 299 -2067 -4370 C ATOM 1694 O PHE A 223 -6.602 69.633 1.778 1.00104.17 O ANISOU 1694 O PHE A 223 10227 14194 15160 370 -2228 -4033 O ATOM 1695 CB PHE A 223 -7.768 71.964 0.073 1.00111.26 C ANISOU 1695 CB PHE A 223 11418 14339 16515 335 -1202 -4178 C ATOM 1696 CG PHE A 223 -8.969 72.474 -0.659 1.00111.22 C ANISOU 1696 CG PHE A 223 11702 14165 16393 411 -834 -3955 C ATOM 1697 CD1 PHE A 223 -9.946 71.602 -1.109 1.00108.80 C ANISOU 1697 CD1 PHE A 223 11650 13979 15710 522 -860 -3496 C ATOM 1698 CD2 PHE A 223 -9.124 73.825 -0.896 1.00114.29 C ANISOU 1698 CD2 PHE A 223 12088 14267 17070 377 -464 -4208 C ATOM 1699 CE1 PHE A 223 -11.052 72.073 -1.781 1.00107.51 C ANISOU 1699 CE1 PHE A 223 11720 13674 15453 602 -568 -3293 C ATOM 1700 CE2 PHE A 223 -10.227 74.302 -1.564 1.00113.03 C ANISOU 1700 CE2 PHE A 223 12175 13951 16819 471 -149 -3976 C ATOM 1701 CZ PHE A 223 -11.192 73.426 -2.008 1.00109.70 C ANISOU 1701 CZ PHE A 223 11994 13674 16014 586 -224 -3518 C ATOM 1702 N LYS A 224 -6.123 71.510 2.917 1.00111.94 N ANISOU 1702 N LYS A 224 10951 15225 16354 188 -2240 -4858 N ATOM 1703 CA LYS A 224 -5.024 70.889 3.633 1.00114.48 C ANISOU 1703 CA LYS A 224 10987 15776 16734 165 -2714 -4991 C ATOM 1704 C LYS A 224 -5.571 69.996 4.739 1.00112.73 C ANISOU 1704 C LYS A 224 10913 16100 15817 249 -3156 -4788 C ATOM 1705 O LYS A 224 -5.071 68.898 4.951 1.00113.21 O ANISOU 1705 O LYS A 224 10888 16336 15791 327 -3496 -4547 O ATOM 1706 CB LYS A 224 -4.079 71.941 4.212 1.00120.48 C ANISOU 1706 CB LYS A 224 11414 16489 17873 10 -2796 -5610 C ATOM 1707 CG LYS A 224 -2.821 71.361 4.838 1.00125.21 C ANISOU 1707 CG LYS A 224 11654 17282 18639 -12 -3305 -5771 C ATOM 1708 CD LYS A 224 -2.932 71.285 6.354 1.00129.27 C ANISOU 1708 CD LYS A 224 12164 18372 18583 -29 -3827 -5984 C ATOM 1709 CE LYS A 224 -2.451 72.566 7.025 1.00133.67 C ANISOU 1709 CE LYS A 224 12489 18948 19352 -215 -3856 -6668 C ATOM 1710 NZ LYS A 224 -3.350 73.729 6.795 1.00131.79 N ANISOU 1710 NZ LYS A 224 12459 18503 19112 -296 -3342 -6864 N ATOM 1711 N LYS A 225 -6.605 70.462 5.435 1.00110.55 N ANISOU 1711 N LYS A 225 10867 16069 15066 239 -3116 -4872 N ATOM 1712 CA LYS A 225 -7.199 69.701 6.533 1.00110.00 C ANISOU 1712 CA LYS A 225 10986 16500 14311 313 -3472 -4698 C ATOM 1713 C LYS A 225 -7.804 68.395 6.032 1.00100.96 C ANISOU 1713 C LYS A 225 10049 15389 12922 467 -3460 -4098 C ATOM 1714 O LYS A 225 -8.005 67.451 6.800 1.00101.76 O ANISOU 1714 O LYS A 225 10255 15853 12555 557 -3777 -3866 O ATOM 1715 CB LYS A 225 -8.280 70.523 7.239 1.00110.26 C ANISOU 1715 CB LYS A 225 11249 16703 13943 260 -3313 -4906 C ATOM 1716 CG LYS A 225 -7.766 71.721 8.008 1.00109.89 C ANISOU 1716 CG LYS A 225 11026 16715 14013 92 -3369 -5532 C ATOM 1717 CD LYS A 225 -8.911 72.481 8.641 1.00110.41 C ANISOU 1717 CD LYS A 225 11342 16908 13701 38 -3143 -5706 C ATOM 1718 CE LYS A 225 -8.405 73.648 9.451 1.00117.93 C ANISOU 1718 CE LYS A 225 12128 17929 14752 -151 -3185 -6362 C ATOM 1719 NZ LYS A 225 -9.551 74.357 10.066 1.00115.82 N ANISOU 1719 NZ LYS A 225 12117 17760 14130 -210 -2919 -6524 N ATOM 1720 N ILE A 226 -8.104 68.353 4.738 1.00107.76 N ANISOU 1720 N ILE A 226 10982 15867 14096 495 -3077 -3854 N ATOM 1721 CA ILE A 226 -8.706 67.175 4.126 1.00104.46 C ANISOU 1721 CA ILE A 226 10754 15437 13499 615 -3014 -3326 C ATOM 1722 C ILE A 226 -7.676 66.108 3.753 1.00104.23 C ANISOU 1722 C ILE A 226 10539 15333 13732 660 -3208 -3107 C ATOM 1723 O ILE A 226 -7.773 64.961 4.195 1.00104.07 O ANISOU 1723 O ILE A 226 10575 15565 13402 757 -3456 -2798 O ATOM 1724 CB ILE A 226 -9.531 67.560 2.880 1.00101.16 C ANISOU 1724 CB ILE A 226 10517 14665 13253 624 -2544 -3154 C ATOM 1725 CG1 ILE A 226 -10.650 68.529 3.270 1.00100.97 C ANISOU 1725 CG1 ILE A 226 10667 14713 12984 604 -2348 -3315 C ATOM 1726 CG2 ILE A 226 -10.110 66.324 2.204 1.00 86.44 C ANISOU 1726 CG2 ILE A 226 8829 12789 11226 723 -2490 -2652 C ATOM 1727 CD1 ILE A 226 -11.394 69.115 2.098 1.00 98.29 C ANISOU 1727 CD1 ILE A 226 10469 14023 12854 625 -1916 -3189 C ATOM 1728 N CYS A 227 -6.692 66.492 2.944 1.00105.76 N ANISOU 1728 N CYS A 227 10508 15151 14524 592 -3058 -3265 N ATOM 1729 CA CYS A 227 -5.672 65.562 2.463 1.00108.41 C ANISOU 1729 CA CYS A 227 10643 15331 15219 621 -3164 -3079 C ATOM 1730 C CYS A 227 -4.879 64.918 3.594 1.00113.37 C ANISOU 1730 C CYS A 227 11044 16310 15722 669 -3695 -3118 C ATOM 1731 O CYS A 227 -4.258 63.870 3.418 1.00112.77 O ANISOU 1731 O CYS A 227 10836 16202 15807 738 -3844 -2854 O ATOM 1732 CB CYS A 227 -4.741 66.253 1.465 1.00109.62 C ANISOU 1732 CB CYS A 227 10591 14989 16070 523 -2864 -3307 C ATOM 1733 SG CYS A 227 -5.430 66.386 -0.203 1.00 90.38 S ANISOU 1733 SG CYS A 227 8448 12086 13807 520 -2267 -3039 S ATOM 1734 N ASP A 228 -4.903 65.554 4.758 1.00118.84 N ANISOU 1734 N ASP A 228 11695 17336 16122 634 -3977 -3446 N ATOM 1735 CA ASP A 228 -4.350 64.945 5.959 1.00124.87 C ANISOU 1735 CA ASP A 228 12320 18518 16605 701 -4528 -3452 C ATOM 1736 C ASP A 228 -5.467 64.192 6.677 1.00124.45 C ANISOU 1736 C ASP A 228 12615 18851 15818 820 -4641 -3108 C ATOM 1737 O ASP A 228 -6.472 64.780 7.070 1.00124.02 O ANISOU 1737 O ASP A 228 12816 18939 15366 787 -4499 -3215 O ATOM 1738 CB ASP A 228 -3.739 66.007 6.867 1.00132.06 C ANISOU 1738 CB ASP A 228 13015 19605 17556 587 -4795 -4019 C ATOM 1739 CG ASP A 228 -2.648 66.806 6.168 1.00135.90 C ANISOU 1739 CG ASP A 228 13137 19675 18823 459 -4636 -4396 C ATOM 1740 OD1 ASP A 228 -2.779 67.077 4.945 1.00133.75 O ANISOU 1740 OD1 ASP A 228 12914 18945 18960 422 -4146 -4316 O ATOM 1741 OD2 ASP A 228 -1.650 67.156 6.837 1.00141.12 O ANISOU 1741 OD2 ASP A 228 13464 20463 19693 396 -4998 -4776 O ATOM 1742 N GLY A 229 -5.300 62.886 6.844 1.00125.77 N ANISOU 1742 N GLY A 229 12789 19158 15839 959 -4858 -2692 N ATOM 1743 CA GLY A 229 -6.354 62.067 7.413 1.00127.31 C ANISOU 1743 CA GLY A 229 13318 19653 15399 1079 -4892 -2324 C ATOM 1744 C GLY A 229 -6.465 62.201 8.917 1.00135.64 C ANISOU 1744 C GLY A 229 14473 21202 15860 1117 -5295 -2473 C ATOM 1745 O GLY A 229 -6.191 61.252 9.655 1.00139.53 O ANISOU 1745 O GLY A 229 14979 21981 16055 1256 -5648 -2208 O ATOM 1746 N ILE A 230 -6.867 63.383 9.376 1.00137.52 N ANISOU 1746 N ILE A 230 14799 21534 15919 995 -5227 -2894 N ATOM 1747 CA ILE A 230 -7.077 63.607 10.803 1.00141.16 C ANISOU 1747 CA ILE A 230 15415 22461 15759 1002 -5556 -3081 C ATOM 1748 C ILE A 230 -8.425 64.276 11.085 1.00137.87 C ANISOU 1748 C ILE A 230 15345 22105 14934 935 -5217 -3194 C ATOM 1749 O ILE A 230 -8.803 65.243 10.423 1.00133.18 O ANISOU 1749 O ILE A 230 14736 21224 14641 816 -4842 -3433 O ATOM 1750 CB ILE A 230 -5.909 64.432 11.433 1.00155.79 C ANISOU 1750 CB ILE A 230 16953 24450 17789 894 -5950 -3609 C ATOM 1751 CG1 ILE A 230 -5.973 64.371 12.958 1.00160.51 C ANISOU 1751 CG1 ILE A 230 17724 25590 17673 929 -6394 -3729 C ATOM 1752 CG2 ILE A 230 -5.850 65.879 10.865 1.00166.15 C ANISOU 1752 CG2 ILE A 230 18124 25445 19560 692 -5614 -4121 C ATOM 1753 CD1 ILE A 230 -5.896 62.983 13.508 1.00161.70 C ANISOU 1753 CD1 ILE A 230 17993 26024 17420 1146 -6728 -3217 C ATOM 1754 N PHE A 231 -9.146 63.729 12.059 1.00140.89 N ANISOU 1754 N PHE A 231 16041 22840 14650 1025 -5328 -2998 N ATOM 1755 CA PHE A 231 -10.418 64.276 12.517 1.00141.40 C ANISOU 1755 CA PHE A 231 16439 22995 14291 970 -5028 -3104 C ATOM 1756 C PHE A 231 -10.726 63.757 13.918 1.00147.65 C ANISOU 1756 C PHE A 231 17524 24252 14324 1053 -5304 -3009 C ATOM 1757 O PHE A 231 -10.269 62.679 14.304 1.00151.62 O ANISOU 1757 O PHE A 231 18037 24956 14615 1207 -5629 -2671 O ATOM 1758 CB PHE A 231 -11.560 63.949 11.545 1.00134.27 C ANISOU 1758 CB PHE A 231 15695 21799 13522 1010 -4538 -2764 C ATOM 1759 CG PHE A 231 -11.789 62.476 11.329 1.00131.14 C ANISOU 1759 CG PHE A 231 15398 21429 13000 1179 -4560 -2200 C ATOM 1760 CD1 PHE A 231 -12.653 61.765 12.148 1.00131.75 C ANISOU 1760 CD1 PHE A 231 15796 21762 12501 1280 -4537 -1935 C ATOM 1761 CD2 PHE A 231 -11.162 61.810 10.288 1.00127.82 C ANISOU 1761 CD2 PHE A 231 14758 20746 13061 1229 -4551 -1946 C ATOM 1762 CE1 PHE A 231 -12.873 60.413 11.941 1.00129.60 C ANISOU 1762 CE1 PHE A 231 15605 21484 12155 1431 -4512 -1426 C ATOM 1763 CE2 PHE A 231 -11.378 60.461 10.078 1.00125.51 C ANISOU 1763 CE2 PHE A 231 14548 20454 12687 1369 -4531 -1450 C ATOM 1764 CZ PHE A 231 -12.231 59.762 10.906 1.00126.23 C ANISOU 1764 CZ PHE A 231 14941 20800 12221 1472 -4513 -1190 C ATOM 1765 N TYR A 232 -11.493 64.527 14.682 1.00148.74 N ANISOU 1765 N TYR A 232 17913 24545 14056 955 -5154 -3300 N ATOM 1766 CA TYR A 232 -11.765 64.180 16.072 1.00153.22 C ANISOU 1766 CA TYR A 232 18804 25554 13860 1010 -5389 -3275 C ATOM 1767 C TYR A 232 -13.141 63.554 16.271 1.00150.05 C ANISOU 1767 C TYR A 232 18793 25164 13056 1100 -5020 -2906 C ATOM 1768 O TYR A 232 -14.153 64.077 15.804 1.00146.50 O ANISOU 1768 O TYR A 232 18432 24473 12759 1025 -4549 -2968 O ATOM 1769 CB TYR A 232 -11.600 65.414 16.964 1.00158.92 C ANISOU 1769 CB TYR A 232 19566 26478 14337 824 -5494 -3890 C ATOM 1770 CG TYR A 232 -10.184 65.619 17.459 1.00164.90 C ANISOU 1770 CG TYR A 232 20050 27465 15141 784 -6069 -4194 C ATOM 1771 CD1 TYR A 232 -9.393 64.537 17.825 1.00167.47 C ANISOU 1771 CD1 TYR A 232 20346 27896 15387 921 -6455 -3770 C ATOM 1772 CD2 TYR A 232 -9.637 66.893 17.558 1.00167.67 C ANISOU 1772 CD2 TYR A 232 20182 27762 15763 570 -6104 -4812 C ATOM 1773 CE1 TYR A 232 -8.100 64.718 18.279 1.00172.47 C ANISOU 1773 CE1 TYR A 232 20733 28606 16193 852 -6895 -3952 C ATOM 1774 CE2 TYR A 232 -8.343 67.084 18.010 1.00172.47 C ANISOU 1774 CE2 TYR A 232 20544 28435 16552 493 -6525 -5008 C ATOM 1775 CZ TYR A 232 -7.579 65.995 18.368 1.00175.06 C ANISOU 1775 CZ TYR A 232 20841 28892 16783 637 -6934 -4575 C ATOM 1776 OH TYR A 232 -6.292 66.181 18.819 1.00180.47 O ANISOU 1776 OH TYR A 232 21257 29652 17660 564 -7369 -4768 O ATOM 1777 N THR A 233 -13.160 62.424 16.969 1.00151.83 N ANISOU 1777 N THR A 233 19234 25658 12795 1272 -5234 -2515 N ATOM 1778 CA THR A 233 -14.399 61.752 17.337 1.00150.54 C ANISOU 1778 CA THR A 233 19458 25534 12208 1364 -4899 -2173 C ATOM 1779 C THR A 233 -14.612 61.907 18.839 1.00156.40 C ANISOU 1779 C THR A 233 20579 26685 12161 1358 -5053 -2333 C ATOM 1780 O THR A 233 -14.042 61.159 19.635 1.00160.25 O ANISOU 1780 O THR A 233 21200 27319 12369 1436 -5354 -2060 O ATOM 1781 CB THR A 233 -14.351 60.266 16.963 1.00148.26 C ANISOU 1781 CB THR A 233 19170 25194 11967 1574 -4933 -1563 C ATOM 1782 OG1 THR A 233 -13.255 59.638 17.639 1.00152.90 O ANISOU 1782 OG1 THR A 233 19712 26047 12334 1690 -5454 -1412 O ATOM 1783 CG2 THR A 233 -14.167 60.113 15.463 1.00142.04 C ANISOU 1783 CG2 THR A 233 18045 23999 11925 1558 -4754 -1430 C ATOM 1784 N PRO A 234 -15.434 62.892 19.230 1.00157.01 N ANISOU 1784 N PRO A 234 20851 26744 12063 1197 -4724 -2705 N ATOM 1785 CA PRO A 234 -15.502 63.356 20.619 1.00164.04 C ANISOU 1785 CA PRO A 234 22079 27913 12336 1096 -4817 -2979 C ATOM 1786 C PRO A 234 -16.474 62.599 21.524 1.00167.08 C ANISOU 1786 C PRO A 234 22966 28398 12117 1184 -4564 -2637 C ATOM 1787 O PRO A 234 -17.605 62.311 21.132 1.00163.83 O ANISOU 1787 O PRO A 234 22681 27880 11686 1258 -4123 -2461 O ATOM 1788 CB PRO A 234 -15.967 64.804 20.462 1.00162.80 C ANISOU 1788 CB PRO A 234 21857 27657 12343 882 -4516 -3574 C ATOM 1789 CG PRO A 234 -16.842 64.768 19.252 1.00155.65 C ANISOU 1789 CG PRO A 234 20814 26304 12022 897 -4014 -3351 C ATOM 1790 CD PRO A 234 -16.272 63.710 18.335 1.00151.92 C ANISOU 1790 CD PRO A 234 20093 25709 11919 1066 -4212 -2885 C ATOM 1791 N GLN A 235 -15.997 62.278 22.726 1.00173.52 N ANISOU 1791 N GLN A 235 24060 29412 12458 1174 -4850 -2550 N ATOM 1792 CA GLN A 235 -16.833 61.854 23.851 1.00176.97 C ANISOU 1792 CA GLN A 235 25040 29961 12241 1195 -4615 -2368 C ATOM 1793 C GLN A 235 -17.822 60.720 23.568 1.00173.78 C ANISOU 1793 C GLN A 235 24824 29439 11765 1390 -4230 -1838 C ATOM 1794 O GLN A 235 -17.446 59.551 23.485 1.00173.60 O ANISOU 1794 O GLN A 235 24784 29405 11772 1565 -4402 -1341 O ATOM 1795 CB GLN A 235 -17.591 63.062 24.413 1.00179.12 C ANISOU 1795 CB GLN A 235 25546 30260 12252 985 -4276 -2899 C ATOM 1796 CG GLN A 235 -17.917 62.968 25.895 1.00186.56 C ANISOU 1796 CG GLN A 235 27049 31375 12460 918 -4227 -2898 C ATOM 1797 CD GLN A 235 -16.774 63.439 26.774 1.00194.26 C ANISOU 1797 CD GLN A 235 28056 32564 13190 781 -4756 -3172 C ATOM 1798 OE1 GLN A 235 -15.982 64.293 26.376 1.00194.80 O ANISOU 1798 OE1 GLN A 235 27749 32628 13638 658 -5011 -3575 O ATOM 1799 NE2 GLN A 235 -16.683 62.882 27.976 1.00200.55 N ANISOU 1799 NE2 GLN A 235 29300 33546 13354 795 -4917 -2958 N ATOM 1800 N TYR A 236 -19.090 61.095 23.427 1.00171.42 N ANISOU 1800 N TYR A 236 24688 29041 11404 1351 -3686 -1968 N ATOM 1801 CA TYR A 236 -20.209 60.158 23.348 1.00169.97 C ANISOU 1801 CA TYR A 236 24741 28746 11094 1503 -3233 -1544 C ATOM 1802 C TYR A 236 -20.136 59.188 22.175 1.00164.17 C ANISOU 1802 C TYR A 236 23697 27853 10829 1690 -3238 -1107 C ATOM 1803 O TYR A 236 -20.755 58.124 22.209 1.00163.84 O ANISOU 1803 O TYR A 236 23834 27729 10687 1841 -2976 -661 O ATOM 1804 CB TYR A 236 -21.522 60.938 23.252 1.00168.03 C ANISOU 1804 CB TYR A 236 24617 28388 10838 1403 -2648 -1848 C ATOM 1805 CG TYR A 236 -21.683 61.663 21.934 1.00161.62 C ANISOU 1805 CG TYR A 236 23339 27208 10862 1286 -2480 -2040 C ATOM 1806 CD1 TYR A 236 -21.029 62.866 21.699 1.00161.01 C ANISOU 1806 CD1 TYR A 236 23002 27134 11040 1116 -2683 -2531 C ATOM 1807 CD2 TYR A 236 -22.473 61.137 20.920 1.00156.00 C ANISOU 1807 CD2 TYR A 236 22450 26145 10678 1349 -2123 -1728 C ATOM 1808 CE1 TYR A 236 -21.164 63.527 20.498 1.00155.75 C ANISOU 1808 CE1 TYR A 236 21944 26121 11114 1029 -2513 -2672 C ATOM 1809 CE2 TYR A 236 -22.613 61.792 19.715 1.00150.88 C ANISOU 1809 CE2 TYR A 236 21409 25180 10739 1258 -1996 -1878 C ATOM 1810 CZ TYR A 236 -21.957 62.987 19.511 1.00150.66 C ANISOU 1810 CZ TYR A 236 21159 25152 10933 1108 -2183 -2332 C ATOM 1811 OH TYR A 236 -22.092 63.644 18.313 1.00145.77 O ANISOU 1811 OH TYR A 236 20181 24205 11000 1037 -2036 -2450 O ATOM 1812 N LEU A 237 -19.396 59.569 21.138 1.00160.07 N ANISOU 1812 N LEU A 237 22717 27242 10860 1658 -3490 -1247 N ATOM 1813 CA LEU A 237 -19.359 58.809 19.892 1.00153.02 C ANISOU 1813 CA LEU A 237 21505 26053 10582 1749 -3414 -886 C ATOM 1814 C LEU A 237 -18.992 57.343 20.114 1.00150.84 C ANISOU 1814 C LEU A 237 21329 25890 10092 1984 -3589 -329 C ATOM 1815 O LEU A 237 -17.888 57.025 20.557 1.00151.91 O ANISOU 1815 O LEU A 237 21415 26139 10165 2017 -4033 -231 O ATOM 1816 CB LEU A 237 -18.404 59.464 18.891 1.00152.21 C ANISOU 1816 CB LEU A 237 20933 25816 11086 1656 -3691 -1131 C ATOM 1817 CG LEU A 237 -18.904 59.508 17.446 1.00146.47 C ANISOU 1817 CG LEU A 237 19911 24667 11073 1610 -3361 -1050 C ATOM 1818 CD1 LEU A 237 -20.304 60.099 17.386 1.00145.55 C ANISOU 1818 CD1 LEU A 237 19939 24356 11006 1507 -2826 -1203 C ATOM 1819 CD2 LEU A 237 -17.954 60.307 16.574 1.00145.05 C ANISOU 1819 CD2 LEU A 237 19330 24353 11430 1505 -3594 -1340 C ATOM 1820 N ASN A 238 -19.943 56.463 19.813 1.00147.41 N ANISOU 1820 N ASN A 238 21008 25244 9758 2070 -3157 43 N ATOM 1821 CA ASN A 238 -19.790 55.025 20.017 1.00148.41 C ANISOU 1821 CA ASN A 238 21256 25416 9718 2293 -3192 595 C ATOM 1822 C ASN A 238 -18.596 54.456 19.256 1.00148.15 C ANISOU 1822 C ASN A 238 20841 25312 10136 2370 -3582 806 C ATOM 1823 O ASN A 238 -18.403 54.766 18.083 1.00145.41 O ANISOU 1823 O ASN A 238 20126 24741 10381 2286 -3567 687 O ATOM 1824 CB ASN A 238 -21.077 54.303 19.607 1.00143.42 C ANISOU 1824 CB ASN A 238 20723 24486 9286 2323 -2593 875 C ATOM 1825 CG ASN A 238 -21.037 52.819 19.906 1.00143.52 C ANISOU 1825 CG ASN A 238 20901 24516 9115 2550 -2534 1439 C ATOM 1826 OD1 ASN A 238 -20.760 52.005 19.027 1.00139.73 O ANISOU 1826 OD1 ASN A 238 20155 23841 9095 2620 -2530 1728 O ATOM 1827 ND2 ASN A 238 -21.312 52.458 21.155 1.00147.93 N ANISOU 1827 ND2 ASN A 238 21888 25188 9129 2601 -2433 1580 N ATOM 1828 N PRO A 239 -17.789 53.619 19.928 1.00152.20 N ANISOU 1828 N PRO A 239 21438 25891 10499 2474 -3874 1119 N ATOM 1829 CA PRO A 239 -16.557 53.067 19.351 1.00150.84 C ANISOU 1829 CA PRO A 239 20909 25654 10751 2552 -4258 1316 C ATOM 1830 C PRO A 239 -16.781 52.266 18.068 1.00145.44 C ANISOU 1830 C PRO A 239 19963 24723 10573 2646 -4012 1617 C ATOM 1831 O PRO A 239 -15.892 52.228 17.216 1.00142.67 O ANISOU 1831 O PRO A 239 19234 24277 10696 2648 -4252 1613 O ATOM 1832 CB PRO A 239 -16.027 52.151 20.463 1.00157.25 C ANISOU 1832 CB PRO A 239 21964 26575 11210 2679 -4484 1677 C ATOM 1833 CG PRO A 239 -17.207 51.881 21.342 1.00159.59 C ANISOU 1833 CG PRO A 239 22746 26913 10978 2705 -4070 1802 C ATOM 1834 CD PRO A 239 -18.012 53.137 21.301 1.00157.60 C ANISOU 1834 CD PRO A 239 22574 26709 10598 2528 -3842 1315 C ATOM 1835 N SER A 240 -17.947 51.643 17.931 1.00142.39 N ANISOU 1835 N SER A 240 19773 24229 10100 2713 -3524 1861 N ATOM 1836 CA SER A 240 -18.230 50.810 16.766 1.00136.99 C ANISOU 1836 CA SER A 240 18862 23213 9976 2733 -3224 2132 C ATOM 1837 C SER A 240 -18.329 51.626 15.481 1.00129.83 C ANISOU 1837 C SER A 240 17621 22041 9669 2524 -3127 1792 C ATOM 1838 O SER A 240 -17.935 51.159 14.413 1.00128.14 O ANISOU 1838 O SER A 240 17117 21588 9981 2510 -3107 1920 O ATOM 1839 CB SER A 240 -19.510 49.996 16.975 1.00136.88 C ANISOU 1839 CB SER A 240 19123 23059 9826 2790 -2674 2410 C ATOM 1840 OG SER A 240 -19.761 49.145 15.869 1.00133.06 O ANISOU 1840 OG SER A 240 18411 22245 9900 2783 -2389 2644 O ATOM 1841 N VAL A 241 -18.848 52.845 15.585 1.00126.80 N ANISOU 1841 N VAL A 241 17291 21686 9200 2364 -3048 1365 N ATOM 1842 CA VAL A 241 -19.051 53.682 14.406 1.00120.41 C ANISOU 1842 CA VAL A 241 16207 20619 8923 2185 -2922 1063 C ATOM 1843 C VAL A 241 -17.815 54.518 14.067 1.00120.39 C ANISOU 1843 C VAL A 241 15924 20659 9158 2110 -3338 769 C ATOM 1844 O VAL A 241 -17.626 54.926 12.920 1.00116.08 O ANISOU 1844 O VAL A 241 15108 19865 9132 2004 -3285 630 O ATOM 1845 CB VAL A 241 -20.292 54.593 14.557 1.00118.46 C ANISOU 1845 CB VAL A 241 16116 20317 8578 2055 -2570 766 C ATOM 1846 CG1 VAL A 241 -20.016 55.730 15.531 1.00121.22 C ANISOU 1846 CG1 VAL A 241 16606 20923 8528 1985 -2783 379 C ATOM 1847 CG2 VAL A 241 -20.723 55.136 13.200 1.00113.69 C ANISOU 1847 CG2 VAL A 241 15245 19397 8555 1918 -2364 600 C ATOM 1848 N ILE A 242 -16.970 54.759 15.066 1.00125.33 N ANISOU 1848 N ILE A 242 16621 21597 9403 2166 -3748 671 N ATOM 1849 CA ILE A 242 -15.728 55.495 14.855 1.00125.66 C ANISOU 1849 CA ILE A 242 16373 21691 9683 2100 -4164 378 C ATOM 1850 C ILE A 242 -14.802 54.703 13.935 1.00123.76 C ANISOU 1850 C ILE A 242 15811 21255 9956 2169 -4305 640 C ATOM 1851 O ILE A 242 -14.119 55.271 13.082 1.00121.13 O ANISOU 1851 O ILE A 242 15170 20739 10113 2065 -4398 419 O ATOM 1852 CB ILE A 242 -15.010 55.794 16.187 1.00131.04 C ANISOU 1852 CB ILE A 242 17191 22781 9817 2156 -4620 231 C ATOM 1853 CG1 ILE A 242 -15.905 56.639 17.096 1.00133.35 C ANISOU 1853 CG1 ILE A 242 17821 23249 9597 2059 -4443 -76 C ATOM 1854 CG2 ILE A 242 -13.692 56.509 15.940 1.00131.79 C ANISOU 1854 CG2 ILE A 242 16932 22911 10232 2081 -5056 -92 C ATOM 1855 CD1 ILE A 242 -15.270 56.997 18.422 1.00139.56 C ANISOU 1855 CD1 ILE A 242 18790 24365 9874 2044 -4833 -260 C ATOM 1856 N SER A 243 -14.799 53.385 14.109 1.00124.80 N ANISOU 1856 N SER A 243 16024 21398 9994 2342 -4274 1116 N ATOM 1857 CA SER A 243 -14.014 52.500 13.257 1.00122.58 C ANISOU 1857 CA SER A 243 15460 20903 10214 2411 -4333 1403 C ATOM 1858 C SER A 243 -14.529 52.531 11.822 1.00116.04 C ANISOU 1858 C SER A 243 14476 19681 9933 2273 -3935 1366 C ATOM 1859 O SER A 243 -13.780 52.282 10.877 1.00114.23 O ANISOU 1859 O SER A 243 13965 19222 10216 2245 -3972 1415 O ATOM 1860 CB SER A 243 -14.045 51.069 13.797 1.00125.11 C ANISOU 1860 CB SER A 243 15931 21297 10307 2630 -4308 1936 C ATOM 1861 OG SER A 243 -15.373 50.579 13.861 1.00123.84 O ANISOU 1861 OG SER A 243 16049 21054 9951 2640 -3837 2116 O ATOM 1862 N LEU A 244 -15.813 52.840 11.665 1.00112.72 N ANISOU 1862 N LEU A 244 14243 19184 9402 2188 -3556 1277 N ATOM 1863 CA LEU A 244 -16.414 52.947 10.342 1.00106.82 C ANISOU 1863 CA LEU A 244 13374 18103 9109 2060 -3211 1224 C ATOM 1864 C LEU A 244 -16.032 54.265 9.681 1.00104.40 C ANISOU 1864 C LEU A 244 12880 17684 9102 1904 -3294 806 C ATOM 1865 O LEU A 244 -15.769 54.313 8.481 1.00101.81 O ANISOU 1865 O LEU A 244 12358 17080 9246 1824 -3190 781 O ATOM 1866 CB LEU A 244 -17.936 52.818 10.423 1.00104.56 C ANISOU 1866 CB LEU A 244 13319 17775 8636 2035 -2801 1275 C ATOM 1867 CG LEU A 244 -18.686 52.953 9.095 1.00 98.80 C ANISOU 1867 CG LEU A 244 12474 16737 8328 1909 -2477 1213 C ATOM 1868 CD1 LEU A 244 -18.169 51.944 8.074 1.00 95.47 C ANISOU 1868 CD1 LEU A 244 11870 16086 8321 1918 -2421 1469 C ATOM 1869 CD2 LEU A 244 -20.186 52.795 9.306 1.00 97.70 C ANISOU 1869 CD2 LEU A 244 12529 16576 8017 1897 -2107 1257 C ATOM 1870 N LEU A 245 -15.999 55.332 10.472 1.00106.22 N ANISOU 1870 N LEU A 245 13189 18119 9053 1858 -3454 474 N ATOM 1871 CA LEU A 245 -15.647 56.652 9.960 1.00106.19 C ANISOU 1871 CA LEU A 245 13017 18003 9328 1713 -3502 57 C ATOM 1872 C LEU A 245 -14.186 56.723 9.517 1.00107.62 C ANISOU 1872 C LEU A 245 12897 18101 9894 1702 -3801 -18 C ATOM 1873 O LEU A 245 -13.885 57.220 8.431 1.00105.11 O ANISOU 1873 O LEU A 245 12391 17503 10045 1602 -3690 -162 O ATOM 1874 CB LEU A 245 -15.942 57.728 11.006 1.00109.13 C ANISOU 1874 CB LEU A 245 13546 18613 9307 1656 -3579 -297 C ATOM 1875 CG LEU A 245 -17.417 57.912 11.360 1.00107.30 C ANISOU 1875 CG LEU A 245 13581 18400 8787 1635 -3222 -305 C ATOM 1876 CD1 LEU A 245 -17.585 59.012 12.396 1.00110.64 C ANISOU 1876 CD1 LEU A 245 14152 19037 8848 1560 -3284 -689 C ATOM 1877 CD2 LEU A 245 -18.226 58.217 10.110 1.00101.74 C ANISOU 1877 CD2 LEU A 245 12785 17368 8503 1554 -2869 -320 C ATOM 1878 N LYS A 246 -13.287 56.222 10.363 1.00111.49 N ANISOU 1878 N LYS A 246 13343 18824 10192 1812 -4174 88 N ATOM 1879 CA LYS A 246 -11.863 56.159 10.036 1.00112.62 C ANISOU 1879 CA LYS A 246 13164 18891 10733 1821 -4481 44 C ATOM 1880 C LYS A 246 -11.638 55.314 8.786 1.00109.91 C ANISOU 1880 C LYS A 246 12660 18199 10902 1827 -4262 326 C ATOM 1881 O LYS A 246 -10.670 55.515 8.052 1.00110.84 O ANISOU 1881 O LYS A 246 12502 18099 11515 1770 -4333 216 O ATOM 1882 CB LYS A 246 -11.062 55.575 11.206 1.00116.80 C ANISOU 1882 CB LYS A 246 13688 19755 10937 1976 -4935 193 C ATOM 1883 CG LYS A 246 -10.911 56.498 12.407 1.00120.63 C ANISOU 1883 CG LYS A 246 14274 20597 10962 1945 -5252 -165 C ATOM 1884 CD LYS A 246 -9.763 57.483 12.227 1.00121.31 C ANISOU 1884 CD LYS A 246 14024 20643 11424 1830 -5542 -600 C ATOM 1885 CE LYS A 246 -9.660 58.425 13.419 1.00124.46 C ANISOU 1885 CE LYS A 246 14530 21403 11358 1770 -5841 -1007 C ATOM 1886 NZ LYS A 246 -8.651 59.504 13.223 1.00124.56 N ANISOU 1886 NZ LYS A 246 14204 21348 11773 1626 -6063 -1502 N ATOM 1887 N HIS A 247 -12.543 54.368 8.553 1.00105.99 N ANISOU 1887 N HIS A 247 12342 17637 10294 1884 -3971 668 N ATOM 1888 CA HIS A 247 -12.462 53.480 7.404 1.00100.45 C ANISOU 1888 CA HIS A 247 11528 16616 10022 1875 -3724 931 C ATOM 1889 C HIS A 247 -12.997 54.176 6.154 1.00 95.37 C ANISOU 1889 C HIS A 247 10868 15678 9691 1712 -3403 729 C ATOM 1890 O HIS A 247 -12.358 54.154 5.102 1.00 92.69 O ANISOU 1890 O HIS A 247 10347 15051 9821 1640 -3321 705 O ATOM 1891 CB HIS A 247 -13.249 52.196 7.682 1.00 99.31 C ANISOU 1891 CB HIS A 247 11575 16517 9641 1990 -3524 1347 C ATOM 1892 CG HIS A 247 -12.850 51.038 6.819 1.00 97.42 C ANISOU 1892 CG HIS A 247 11193 16009 9812 2015 -3361 1658 C ATOM 1893 ND1 HIS A 247 -11.908 51.141 5.819 1.00 95.78 N ANISOU 1893 ND1 HIS A 247 10728 15525 10137 1932 -3367 1574 N ATOM 1894 CD2 HIS A 247 -13.267 49.750 6.811 1.00 97.20 C ANISOU 1894 CD2 HIS A 247 11250 15923 9759 2104 -3147 2041 C ATOM 1895 CE1 HIS A 247 -11.762 49.968 5.231 1.00 94.48 C ANISOU 1895 CE1 HIS A 247 10500 15150 10248 1962 -3168 1885 C ATOM 1896 NE2 HIS A 247 -12.576 49.106 5.813 1.00 95.24 N ANISOU 1896 NE2 HIS A 247 10791 15373 10022 2065 -3034 2171 N ATOM 1897 N MET A 248 -14.165 54.801 6.280 1.00 95.29 N ANISOU 1897 N MET A 248 11054 15731 9422 1660 -3216 591 N ATOM 1898 CA MET A 248 -14.797 55.490 5.155 1.00 94.23 C ANISOU 1898 CA MET A 248 10924 15345 9533 1532 -2932 429 C ATOM 1899 C MET A 248 -14.042 56.754 4.757 1.00 96.78 C ANISOU 1899 C MET A 248 11088 15544 10138 1434 -3024 67 C ATOM 1900 O MET A 248 -14.145 57.217 3.619 1.00 95.64 O ANISOU 1900 O MET A 248 10904 15126 10311 1344 -2816 -21 O ATOM 1901 CB MET A 248 -16.252 55.839 5.477 1.00 92.73 C ANISOU 1901 CB MET A 248 10953 15255 9027 1520 -2722 384 C ATOM 1902 CG MET A 248 -17.164 54.638 5.643 1.00 92.56 C ANISOU 1902 CG MET A 248 11076 15274 8816 1591 -2530 715 C ATOM 1903 SD MET A 248 -18.883 55.120 5.900 1.00 96.38 S ANISOU 1903 SD MET A 248 11762 15813 9045 1562 -2247 626 S ATOM 1904 CE MET A 248 -19.271 55.838 4.308 1.00171.60 C ANISOU 1904 CE MET A 248 21180 25031 18991 1438 -2059 478 C ATOM 1905 N LEU A 249 -13.289 57.314 5.699 1.00 98.92 N ANISOU 1905 N LEU A 249 11280 16017 10288 1452 -3327 -148 N ATOM 1906 CA LEU A 249 -12.517 58.520 5.433 1.00 98.11 C ANISOU 1906 CA LEU A 249 11002 15794 10479 1353 -3407 -527 C ATOM 1907 C LEU A 249 -11.024 58.239 5.410 1.00100.20 C ANISOU 1907 C LEU A 249 10993 16003 11076 1370 -3675 -547 C ATOM 1908 O LEU A 249 -10.244 58.940 6.050 1.00104.38 O ANISOU 1908 O LEU A 249 11377 16657 11627 1345 -3946 -842 O ATOM 1909 CB LEU A 249 -12.831 59.604 6.462 1.00100.50 C ANISOU 1909 CB LEU A 249 11391 16340 10456 1318 -3518 -865 C ATOM 1910 CG LEU A 249 -14.270 60.114 6.449 1.00 99.49 C ANISOU 1910 CG LEU A 249 11489 16215 10097 1287 -3220 -908 C ATOM 1911 CD1 LEU A 249 -14.413 61.331 7.346 1.00101.60 C ANISOU 1911 CD1 LEU A 249 11805 16652 10148 1222 -3285 -1304 C ATOM 1912 CD2 LEU A 249 -14.706 60.428 5.026 1.00 96.49 C ANISOU 1912 CD2 LEU A 249 11084 15482 10096 1224 -2898 -880 C ATOM 1913 N GLN A 250 -10.630 57.205 4.677 1.00 98.44 N ANISOU 1913 N GLN A 250 10685 15583 11136 1405 -3592 -250 N ATOM 1914 CA GLN A 250 -9.218 56.919 4.484 1.00100.21 C ANISOU 1914 CA GLN A 250 10615 15674 11785 1415 -3786 -258 C ATOM 1915 C GLN A 250 -8.679 57.719 3.309 1.00 99.72 C ANISOU 1915 C GLN A 250 10406 15225 12257 1279 -3567 -500 C ATOM 1916 O GLN A 250 -9.202 57.631 2.199 1.00 96.78 O ANISOU 1916 O GLN A 250 10148 14585 12038 1218 -3217 -403 O ATOM 1917 CB GLN A 250 -8.984 55.426 4.264 1.00 98.42 C ANISOU 1917 CB GLN A 250 10352 15380 11662 1513 -3760 173 C ATOM 1918 CG GLN A 250 -8.844 54.635 5.548 1.00101.19 C ANISOU 1918 CG GLN A 250 10728 16085 11635 1681 -4093 403 C ATOM 1919 CD GLN A 250 -7.664 55.095 6.383 1.00105.88 C ANISOU 1919 CD GLN A 250 11076 16864 12290 1721 -4554 187 C ATOM 1920 OE1 GLN A 250 -6.669 55.594 5.854 1.00105.86 O ANISOU 1920 OE1 GLN A 250 10793 16641 12789 1641 -4608 -41 O ATOM 1921 NE2 GLN A 250 -7.771 54.933 7.697 1.00110.32 N ANISOU 1921 NE2 GLN A 250 11747 17829 12340 1843 -4886 247 N ATOM 1922 N VAL A 251 -7.639 58.505 3.563 1.00103.44 N ANISOU 1922 N VAL A 251 10631 15667 13002 1232 -3772 -825 N ATOM 1923 CA VAL A 251 -7.028 59.322 2.523 1.00103.82 C ANISOU 1923 CA VAL A 251 10534 15324 13590 1107 -3541 -1078 C ATOM 1924 C VAL A 251 -6.469 58.454 1.401 1.00103.77 C ANISOU 1924 C VAL A 251 10437 14954 14037 1093 -3318 -835 C ATOM 1925 O VAL A 251 -6.540 58.822 0.230 1.00102.39 O ANISOU 1925 O VAL A 251 10326 14425 14151 998 -2959 -884 O ATOM 1926 CB VAL A 251 -5.930 60.235 3.091 1.00108.34 C ANISOU 1926 CB VAL A 251 10811 15928 14424 1056 -3811 -1490 C ATOM 1927 CG1 VAL A 251 -6.547 61.499 3.680 1.00108.66 C ANISOU 1927 CG1 VAL A 251 10969 16143 14172 992 -3817 -1845 C ATOM 1928 CG2 VAL A 251 -5.110 59.490 4.135 1.00113.69 C ANISOU 1928 CG2 VAL A 251 11278 16894 15024 1166 -4290 -1398 C ATOM 1929 N ASP A 252 -5.922 57.297 1.760 1.00106.05 N ANISOU 1929 N ASP A 252 10592 15322 14378 1190 -3515 -563 N ATOM 1930 CA ASP A 252 -5.499 56.324 0.761 1.00105.78 C ANISOU 1930 CA ASP A 252 10495 14952 14743 1177 -3268 -301 C ATOM 1931 C ASP A 252 -6.723 55.594 0.227 1.00103.04 C ANISOU 1931 C ASP A 252 10465 14599 14087 1181 -2976 1 C ATOM 1932 O ASP A 252 -7.376 54.856 0.963 1.00104.33 O ANISOU 1932 O ASP A 252 10751 15049 13840 1287 -3101 242 O ATOM 1933 CB ASP A 252 -4.513 55.322 1.357 1.00109.92 C ANISOU 1933 CB ASP A 252 10748 15550 15467 1293 -3566 -96 C ATOM 1934 CG ASP A 252 -4.084 54.263 0.357 1.00109.74 C ANISOU 1934 CG ASP A 252 10654 15156 15885 1272 -3270 178 C ATOM 1935 OD1 ASP A 252 -3.787 54.621 -0.803 1.00106.80 O ANISOU 1935 OD1 ASP A 252 10274 14383 15924 1137 -2920 47 O ATOM 1936 OD2 ASP A 252 -4.052 53.072 0.730 1.00112.32 O ANISOU 1936 OD2 ASP A 252 10952 15581 16145 1391 -3358 527 O ATOM 1937 N PRO A 253 -7.037 55.799 -1.062 1.00 99.85 N ANISOU 1937 N PRO A 253 10197 13862 13878 1065 -2581 -20 N ATOM 1938 CA PRO A 253 -8.249 55.252 -1.682 1.00 96.57 C ANISOU 1938 CA PRO A 253 10072 13434 13185 1044 -2311 201 C ATOM 1939 C PRO A 253 -8.266 53.726 -1.730 1.00 95.86 C ANISOU 1939 C PRO A 253 9978 13333 13112 1097 -2251 564 C ATOM 1940 O PRO A 253 -9.340 53.131 -1.824 1.00 93.80 O ANISOU 1940 O PRO A 253 9924 13174 12541 1108 -2119 754 O ATOM 1941 CB PRO A 253 -8.205 55.828 -3.102 1.00 94.55 C ANISOU 1941 CB PRO A 253 9916 12789 13222 908 -1947 75 C ATOM 1942 CG PRO A 253 -6.767 56.121 -3.347 1.00 95.76 C ANISOU 1942 CG PRO A 253 9800 12662 13922 863 -1949 -94 C ATOM 1943 CD PRO A 253 -6.221 56.558 -2.025 1.00 99.04 C ANISOU 1943 CD PRO A 253 9984 13365 14283 947 -2365 -261 C ATOM 1944 N MET A 254 -7.094 53.104 -1.658 1.00 97.13 N ANISOU 1944 N MET A 254 9884 13353 13667 1129 -2332 653 N ATOM 1945 CA MET A 254 -7.008 51.650 -1.725 1.00 96.80 C ANISOU 1945 CA MET A 254 9808 13251 13719 1182 -2238 1004 C ATOM 1946 C MET A 254 -7.345 50.996 -0.389 1.00 97.75 C ANISOU 1946 C MET A 254 9932 13762 13448 1359 -2537 1234 C ATOM 1947 O MET A 254 -7.834 49.869 -0.355 1.00 98.07 O ANISOU 1947 O MET A 254 10062 13824 13378 1412 -2401 1541 O ATOM 1948 CB MET A 254 -5.625 51.210 -2.208 1.00 99.59 C ANISOU 1948 CB MET A 254 9875 13261 14704 1155 -2170 1032 C ATOM 1949 CG MET A 254 -5.208 51.839 -3.530 1.00 99.28 C ANISOU 1949 CG MET A 254 9857 12798 15067 979 -1826 808 C ATOM 1950 SD MET A 254 -6.477 51.715 -4.809 1.00116.06 S ANISOU 1950 SD MET A 254 12386 14773 16937 835 -1380 857 S ATOM 1951 CE MET A 254 -6.582 49.941 -5.020 1.00 75.92 C ANISOU 1951 CE MET A 254 7301 9595 11949 847 -1176 1234 C ATOM 1952 N LYS A 255 -7.087 51.701 0.708 1.00 99.27 N ANISOU 1952 N LYS A 255 10041 14253 13423 1447 -2924 1079 N ATOM 1953 CA LYS A 255 -7.446 51.193 2.029 1.00101.79 C ANISOU 1953 CA LYS A 255 10422 14967 13285 1619 -3214 1284 C ATOM 1954 C LYS A 255 -8.819 51.711 2.457 1.00 99.03 C ANISOU 1954 C LYS A 255 10380 14880 12365 1610 -3168 1205 C ATOM 1955 O LYS A 255 -9.376 51.267 3.462 1.00 99.69 O ANISOU 1955 O LYS A 255 10600 15267 12012 1736 -3303 1385 O ATOM 1956 CB LYS A 255 -6.381 51.557 3.071 1.00107.92 C ANISOU 1956 CB LYS A 255 10949 15957 14098 1726 -3695 1173 C ATOM 1957 CG LYS A 255 -6.484 50.753 4.370 1.00113.36 C ANISOU 1957 CG LYS A 255 11687 17012 14374 1935 -4003 1477 C ATOM 1958 CD LYS A 255 -5.362 51.078 5.350 1.00119.52 C ANISOU 1958 CD LYS A 255 12205 18017 15192 2044 -4532 1367 C ATOM 1959 CE LYS A 255 -5.470 50.219 6.607 1.00123.42 C ANISOU 1959 CE LYS A 255 12790 18872 15230 2274 -4836 1721 C ATOM 1960 NZ LYS A 255 -4.352 50.454 7.565 1.00127.88 N ANISOU 1960 NZ LYS A 255 13093 19685 15810 2396 -5409 1639 N ATOM 1961 N ARG A 256 -9.365 52.647 1.683 1.00 95.76 N ANISOU 1961 N ARG A 256 10078 14331 11974 1469 -2956 949 N ATOM 1962 CA ARG A 256 -10.669 53.226 1.990 1.00 93.04 C ANISOU 1962 CA ARG A 256 9989 14188 11174 1453 -2886 855 C ATOM 1963 C ARG A 256 -11.766 52.180 1.866 1.00 92.88 C ANISOU 1963 C ARG A 256 10163 14197 10930 1484 -2648 1156 C ATOM 1964 O ARG A 256 -11.700 51.300 1.009 1.00 92.56 O ANISOU 1964 O ARG A 256 10101 13917 11152 1441 -2411 1344 O ATOM 1965 CB ARG A 256 -10.968 54.418 1.079 1.00 88.02 C ANISOU 1965 CB ARG A 256 9407 13358 10678 1312 -2697 555 C ATOM 1966 CG ARG A 256 -12.231 55.185 1.454 1.00 85.05 C ANISOU 1966 CG ARG A 256 9244 13176 9895 1304 -2648 424 C ATOM 1967 CD ARG A 256 -12.461 56.347 0.510 1.00 82.10 C ANISOU 1967 CD ARG A 256 8908 12583 9702 1190 -2458 169 C ATOM 1968 NE ARG A 256 -11.297 57.224 0.454 1.00 84.35 N ANISOU 1968 NE ARG A 256 9000 12740 10309 1144 -2573 -105 N ATOM 1969 CZ ARG A 256 -11.128 58.189 -0.444 1.00 84.54 C ANISOU 1969 CZ ARG A 256 9017 12496 10607 1052 -2387 -316 C ATOM 1970 NH1 ARG A 256 -12.049 58.405 -1.374 1.00 82.31 N ANISOU 1970 NH1 ARG A 256 8923 12069 10282 1007 -2116 -265 N ATOM 1971 NH2 ARG A 256 -10.034 58.936 -0.414 1.00 87.36 N ANISOU 1971 NH2 ARG A 256 9176 12724 11291 1009 -2471 -577 N ATOM 1972 N ALA A 257 -12.771 52.283 2.730 1.00 93.52 N ANISOU 1972 N ALA A 257 10432 14557 10546 1546 -2685 1179 N ATOM 1973 CA ALA A 257 -13.842 51.299 2.786 1.00 94.03 C ANISOU 1973 CA ALA A 257 10665 14663 10400 1584 -2459 1446 C ATOM 1974 C ALA A 257 -14.632 51.220 1.485 1.00 93.31 C ANISOU 1974 C ALA A 257 10645 14325 10485 1449 -2119 1424 C ATOM 1975 O ALA A 257 -14.758 52.204 0.757 1.00 92.90 O ANISOU 1975 O ALA A 257 10602 14154 10543 1347 -2065 1183 O ATOM 1976 CB ALA A 257 -14.773 51.599 3.953 1.00 94.84 C ANISOU 1976 CB ALA A 257 10960 15081 9995 1662 -2530 1422 C ATOM 1977 N THR A 258 -15.153 50.032 1.199 1.00 93.62 N ANISOU 1977 N THR A 258 10736 14287 10548 1454 -1891 1680 N ATOM 1978 CA THR A 258 -16.045 49.832 0.069 1.00 91.90 C ANISOU 1978 CA THR A 258 10598 13886 10432 1326 -1594 1661 C ATOM 1979 C THR A 258 -17.435 49.543 0.613 1.00 94.84 C ANISOU 1979 C THR A 258 11120 14430 10485 1364 -1470 1734 C ATOM 1980 O THR A 258 -17.592 49.300 1.808 1.00 98.49 O ANISOU 1980 O THR A 258 11640 15108 10672 1489 -1562 1847 O ATOM 1981 CB THR A 258 -15.589 48.651 -0.796 1.00 90.63 C ANISOU 1981 CB THR A 258 10363 13465 10607 1264 -1378 1851 C ATOM 1982 OG1 THR A 258 -15.713 47.436 -0.047 1.00 92.50 O ANISOU 1982 OG1 THR A 258 10600 13782 10764 1373 -1313 2145 O ATOM 1983 CG2 THR A 258 -14.139 48.831 -1.219 1.00 90.99 C ANISOU 1983 CG2 THR A 258 10240 13316 11015 1239 -1473 1801 C ATOM 1984 N ILE A 259 -18.441 49.572 -0.255 1.00 94.74 N ANISOU 1984 N ILE A 259 11171 14317 10510 1257 -1263 1665 N ATOM 1985 CA ILE A 259 -19.807 49.261 0.159 1.00 95.88 C ANISOU 1985 CA ILE A 259 11416 14580 10435 1277 -1111 1713 C ATOM 1986 C ILE A 259 -19.865 47.848 0.728 1.00 98.46 C ANISOU 1986 C ILE A 259 11751 14918 10741 1351 -959 2003 C ATOM 1987 O ILE A 259 -20.541 47.593 1.726 1.00100.70 O ANISOU 1987 O ILE A 259 12127 15363 10770 1445 -905 2097 O ATOM 1988 CB ILE A 259 -20.804 49.417 -1.007 1.00 95.05 C ANISOU 1988 CB ILE A 259 11332 14346 10437 1144 -941 1595 C ATOM 1989 CG1 ILE A 259 -20.931 50.893 -1.390 1.00 95.73 C ANISOU 1989 CG1 ILE A 259 11436 14440 10496 1113 -1076 1343 C ATOM 1990 CG2 ILE A 259 -22.168 48.849 -0.636 1.00 94.98 C ANISOU 1990 CG2 ILE A 259 11372 14417 10301 1155 -751 1658 C ATOM 1991 CD1 ILE A 259 -21.970 51.167 -2.450 1.00 95.27 C ANISOU 1991 CD1 ILE A 259 11405 14294 10500 1016 -967 1243 C ATOM 1992 N LYS A 260 -19.131 46.942 0.091 1.00 99.29 N ANISOU 1992 N LYS A 260 11766 14828 11131 1309 -857 2147 N ATOM 1993 CA LYS A 260 -18.945 45.590 0.598 1.00103.15 C ANISOU 1993 CA LYS A 260 12237 15285 11670 1395 -704 2451 C ATOM 1994 C LYS A 260 -18.405 45.622 2.029 1.00106.52 C ANISOU 1994 C LYS A 260 12699 15937 11835 1594 -929 2607 C ATOM 1995 O LYS A 260 -18.853 44.864 2.890 1.00108.64 O ANISOU 1995 O LYS A 260 13058 16299 11921 1709 -810 2830 O ATOM 1996 CB LYS A 260 -17.989 44.825 -0.322 1.00105.77 C ANISOU 1996 CB LYS A 260 12441 15347 12401 1317 -589 2548 C ATOM 1997 CG LYS A 260 -17.374 43.567 0.274 1.00111.19 C ANISOU 1997 CG LYS A 260 13063 15977 13208 1442 -493 2886 C ATOM 1998 CD LYS A 260 -18.306 42.371 0.179 1.00112.22 C ANISOU 1998 CD LYS A 260 13237 16010 13392 1410 -113 3047 C ATOM 1999 CE LYS A 260 -17.549 41.080 0.446 1.00114.20 C ANISOU 1999 CE LYS A 260 13395 16107 13887 1508 48 3385 C ATOM 2000 NZ LYS A 260 -18.449 39.895 0.448 1.00114.53 N ANISOU 2000 NZ LYS A 260 13477 16038 14003 1484 459 3543 N ATOM 2001 N ASP A 261 -17.454 46.518 2.280 1.00107.12 N ANISOU 2001 N ASP A 261 12714 16099 11885 1631 -1251 2479 N ATOM 2002 CA ASP A 261 -16.836 46.640 3.597 1.00109.22 C ANISOU 2002 CA ASP A 261 13007 16608 11885 1808 -1535 2586 C ATOM 2003 C ASP A 261 -17.759 47.302 4.615 1.00108.53 C ANISOU 2003 C ASP A 261 13114 16789 11334 1866 -1591 2482 C ATOM 2004 O ASP A 261 -17.548 47.184 5.821 1.00111.37 O ANISOU 2004 O ASP A 261 13572 17374 11371 2018 -1756 2613 O ATOM 2005 CB ASP A 261 -15.522 47.421 3.508 1.00109.57 C ANISOU 2005 CB ASP A 261 12889 16651 12091 1806 -1866 2428 C ATOM 2006 CG ASP A 261 -14.467 46.697 2.699 1.00109.47 C ANISOU 2006 CG ASP A 261 12676 16366 12553 1775 -1808 2561 C ATOM 2007 OD1 ASP A 261 -14.508 45.450 2.649 1.00110.05 O ANISOU 2007 OD1 ASP A 261 12734 16324 12754 1824 -1596 2856 O ATOM 2008 OD2 ASP A 261 -13.595 47.373 2.113 1.00109.11 O ANISOU 2008 OD2 ASP A 261 12484 16195 12778 1699 -1938 2365 O ATOM 2009 N ILE A 262 -18.777 48.003 4.129 1.00105.37 N ANISOU 2009 N ILE A 262 12774 16361 10901 1747 -1452 2250 N ATOM 2010 CA ILE A 262 -19.713 48.682 5.017 1.00106.94 C ANISOU 2010 CA ILE A 262 13143 16769 10722 1782 -1449 2124 C ATOM 2011 C ILE A 262 -20.918 47.797 5.338 1.00107.84 C ANISOU 2011 C ILE A 262 13385 16870 10721 1812 -1112 2302 C ATOM 2012 O ILE A 262 -21.404 47.790 6.467 1.00110.33 O ANISOU 2012 O ILE A 262 13876 17363 10681 1911 -1077 2364 O ATOM 2013 CB ILE A 262 -20.183 50.031 4.429 1.00105.08 C ANISOU 2013 CB ILE A 262 12885 16504 10536 1657 -1482 1774 C ATOM 2014 CG1 ILE A 262 -18.980 50.912 4.086 1.00103.26 C ANISOU 2014 CG1 ILE A 262 12525 16246 10465 1621 -1761 1585 C ATOM 2015 CG2 ILE A 262 -21.087 50.757 5.410 1.00106.78 C ANISOU 2015 CG2 ILE A 262 13263 16914 10394 1692 -1458 1635 C ATOM 2016 CD1 ILE A 262 -19.347 52.225 3.436 1.00100.09 C ANISOU 2016 CD1 ILE A 262 12101 15775 10155 1513 -1761 1271 C ATOM 2017 N ARG A 263 -21.388 47.046 4.346 1.00106.64 N ANISOU 2017 N ARG A 263 13149 16496 10872 1717 -847 2370 N ATOM 2018 CA ARG A 263 -22.525 46.145 4.533 1.00107.42 C ANISOU 2018 CA ARG A 263 13323 16539 10952 1724 -492 2511 C ATOM 2019 C ARG A 263 -22.233 45.065 5.570 1.00110.55 C ANISOU 2019 C ARG A 263 13827 16997 11179 1894 -399 2857 C ATOM 2020 O ARG A 263 -23.141 44.567 6.238 1.00110.84 O ANISOU 2020 O ARG A 263 14001 17058 11054 1951 -132 2970 O ATOM 2021 CB ARG A 263 -22.918 45.481 3.211 1.00105.58 C ANISOU 2021 CB ARG A 263 12954 16056 11105 1573 -256 2495 C ATOM 2022 CG ARG A 263 -23.610 46.398 2.223 1.00104.04 C ANISOU 2022 CG ARG A 263 12695 15805 11029 1422 -280 2194 C ATOM 2023 CD ARG A 263 -24.831 45.718 1.618 1.00105.16 C ANISOU 2023 CD ARG A 263 12789 15818 11350 1317 31 2171 C ATOM 2024 NE ARG A 263 -24.494 44.480 0.919 1.00106.39 N ANISOU 2024 NE ARG A 263 12862 15781 11781 1247 226 2320 N ATOM 2025 CZ ARG A 263 -24.297 44.389 -0.393 1.00106.04 C ANISOU 2025 CZ ARG A 263 12724 15578 11990 1092 232 2209 C ATOM 2026 NH1 ARG A 263 -24.404 45.467 -1.161 1.00104.66 N ANISOU 2026 NH1 ARG A 263 12533 15417 11815 1010 40 1977 N ATOM 2027 NH2 ARG A 263 -23.994 43.219 -0.939 1.00106.92 N ANISOU 2027 NH2 ARG A 263 12772 15505 12349 1020 451 2335 N ATOM 2028 N GLU A 264 -20.961 44.705 5.694 1.00113.16 N ANISOU 2028 N GLU A 264 14092 17335 11569 1982 -607 3033 N ATOM 2029 CA GLU A 264 -20.549 43.643 6.602 1.00118.16 C ANISOU 2029 CA GLU A 264 14810 18013 12071 2170 -550 3411 C ATOM 2030 C GLU A 264 -20.005 44.199 7.912 1.00121.75 C ANISOU 2030 C GLU A 264 15419 18771 12069 2339 -889 3457 C ATOM 2031 O GLU A 264 -19.625 43.446 8.806 1.00124.61 O ANISOU 2031 O GLU A 264 15890 19223 12232 2527 -912 3784 O ATOM 2032 CB GLU A 264 -19.521 42.738 5.925 1.00118.61 C ANISOU 2032 CB GLU A 264 14675 17864 12527 2177 -539 3620 C ATOM 2033 CG GLU A 264 -20.087 41.989 4.731 1.00117.34 C ANISOU 2033 CG GLU A 264 14401 17407 12777 2009 -156 3597 C ATOM 2034 CD GLU A 264 -19.014 41.423 3.828 1.00117.28 C ANISOU 2034 CD GLU A 264 14190 17169 13202 1953 -158 3683 C ATOM 2035 OE1 GLU A 264 -17.841 41.830 3.966 1.00118.44 O ANISOU 2035 OE1 GLU A 264 14246 17372 13384 2021 -488 3697 O ATOM 2036 OE2 GLU A 264 -19.347 40.571 2.978 1.00116.46 O ANISOU 2036 OE2 GLU A 264 14009 16815 13423 1832 185 3718 O ATOM 2037 N HIS A 265 -19.976 45.522 8.016 1.00122.36 N ANISOU 2037 N HIS A 265 15512 19004 11975 2270 -1149 3126 N ATOM 2038 CA HIS A 265 -19.556 46.184 9.242 1.00126.82 C ANISOU 2038 CA HIS A 265 16233 19875 12078 2391 -1471 3084 C ATOM 2039 C HIS A 265 -20.615 45.953 10.311 1.00132.27 C ANISOU 2039 C HIS A 265 17227 20694 12338 2478 -1224 3190 C ATOM 2040 O HIS A 265 -21.811 46.024 10.032 1.00127.79 O ANISOU 2040 O HIS A 265 16711 20014 11831 2379 -884 3076 O ATOM 2041 CB HIS A 265 -19.360 47.679 8.996 1.00124.87 C ANISOU 2041 CB HIS A 265 15913 19714 11815 2264 -1732 2661 C ATOM 2042 CG HIS A 265 -18.615 48.381 10.088 1.00127.79 C ANISOU 2042 CG HIS A 265 16374 20385 11796 2356 -2131 2564 C ATOM 2043 ND1 HIS A 265 -19.248 48.982 11.153 1.00130.09 N ANISOU 2043 ND1 HIS A 265 16923 20906 11599 2383 -2131 2435 N ATOM 2044 CD2 HIS A 265 -17.289 48.582 10.275 1.00129.52 C ANISOU 2044 CD2 HIS A 265 16449 20711 12053 2415 -2544 2552 C ATOM 2045 CE1 HIS A 265 -18.345 49.522 11.952 1.00133.12 C ANISOU 2045 CE1 HIS A 265 17336 21545 11698 2449 -2542 2338 C ATOM 2046 NE2 HIS A 265 -17.148 49.294 11.442 1.00132.74 N ANISOU 2046 NE2 HIS A 265 17029 21433 11975 2473 -2814 2406 N ATOM 2047 N GLU A 266 -20.175 45.670 11.532 1.00144.38 N ANISOU 2047 N GLU A 266 18961 22457 13442 2666 -1394 3409 N ATOM 2048 CA GLU A 266 -21.091 45.297 12.608 1.00149.25 C ANISOU 2048 CA GLU A 266 19912 23173 13623 2772 -1116 3570 C ATOM 2049 C GLU A 266 -22.034 46.418 13.035 1.00147.44 C ANISOU 2049 C GLU A 266 19856 23054 13110 2664 -1028 3215 C ATOM 2050 O GLU A 266 -23.135 46.159 13.521 1.00149.27 O ANISOU 2050 O GLU A 266 20304 23244 13169 2676 -639 3267 O ATOM 2051 CB GLU A 266 -20.319 44.758 13.814 1.00157.50 C ANISOU 2051 CB GLU A 266 21164 24455 14223 3014 -1356 3909 C ATOM 2052 CG GLU A 266 -19.847 43.331 13.627 1.00161.94 C ANISOU 2052 CG GLU A 266 21644 24852 15036 3167 -1226 4376 C ATOM 2053 CD GLU A 266 -20.977 42.407 13.212 1.00163.22 C ANISOU 2053 CD GLU A 266 21843 24721 15453 3124 -617 4528 C ATOM 2054 OE1 GLU A 266 -21.831 42.090 14.067 1.00167.00 O ANISOU 2054 OE1 GLU A 266 22628 25236 15588 3210 -302 4665 O ATOM 2055 OE2 GLU A 266 -21.014 42.002 12.030 1.00160.29 O ANISOU 2055 OE2 GLU A 266 21198 24074 15629 2995 -439 4492 O ATOM 2056 N TRP A 267 -21.604 47.661 12.849 1.00139.97 N ANISOU 2056 N TRP A 267 18804 22223 12157 2555 -1352 2851 N ATOM 2057 CA TRP A 267 -22.433 48.804 13.204 1.00132.08 C ANISOU 2057 CA TRP A 267 17937 21304 10945 2444 -1263 2494 C ATOM 2058 C TRP A 267 -23.567 48.976 12.200 1.00124.11 C ANISOU 2058 C TRP A 267 16782 20025 10350 2289 -897 2333 C ATOM 2059 O TRP A 267 -24.691 49.299 12.572 1.00123.26 O ANISOU 2059 O TRP A 267 16820 19892 10122 2244 -597 2209 O ATOM 2060 CB TRP A 267 -21.588 50.078 13.280 1.00128.83 C ANISOU 2060 CB TRP A 267 17433 21068 10448 2373 -1697 2146 C ATOM 2061 CG TRP A 267 -22.333 51.275 13.794 1.00125.74 C ANISOU 2061 CG TRP A 267 17195 20771 9810 2268 -1607 1780 C ATOM 2062 CD1 TRP A 267 -22.549 51.607 15.099 1.00128.23 C ANISOU 2062 CD1 TRP A 267 17836 21328 9558 2319 -1616 1713 C ATOM 2063 CD2 TRP A 267 -22.950 52.304 13.011 1.00122.03 C ANISOU 2063 CD2 TRP A 267 16566 20141 9658 2098 -1477 1434 C ATOM 2064 NE1 TRP A 267 -23.265 52.777 15.178 1.00127.28 N ANISOU 2064 NE1 TRP A 267 17755 21189 9415 2176 -1472 1329 N ATOM 2065 CE2 TRP A 267 -23.525 53.225 13.909 1.00123.91 C ANISOU 2065 CE2 TRP A 267 17022 20516 9542 2051 -1390 1167 C ATOM 2066 CE3 TRP A 267 -23.074 52.536 11.636 1.00117.72 C ANISOU 2066 CE3 TRP A 267 15730 19348 9652 1987 -1420 1335 C ATOM 2067 CZ2 TRP A 267 -24.212 54.359 13.479 1.00123.02 C ANISOU 2067 CZ2 TRP A 267 16815 20283 9646 1906 -1240 819 C ATOM 2068 CZ3 TRP A 267 -23.757 53.662 11.211 1.00115.97 C ANISOU 2068 CZ3 TRP A 267 15434 19027 9601 1859 -1301 1009 C ATOM 2069 CH2 TRP A 267 -24.316 54.559 12.129 1.00118.95 C ANISOU 2069 CH2 TRP A 267 16002 19528 9666 1824 -1209 762 C ATOM 2070 N PHE A 268 -23.267 48.739 10.927 1.00118.47 N ANISOU 2070 N PHE A 268 15779 19106 10126 2208 -925 2336 N ATOM 2071 CA PHE A 268 -24.235 48.946 9.854 1.00114.13 C ANISOU 2071 CA PHE A 268 15068 18326 9971 2059 -663 2171 C ATOM 2072 C PHE A 268 -25.252 47.808 9.766 1.00116.54 C ANISOU 2072 C PHE A 268 15413 18460 10408 2075 -222 2388 C ATOM 2073 O PHE A 268 -26.365 47.997 9.275 1.00115.82 O ANISOU 2073 O PHE A 268 15250 18226 10530 1972 38 2239 O ATOM 2074 CB PHE A 268 -23.508 49.117 8.518 1.00108.21 C ANISOU 2074 CB PHE A 268 14038 17428 9650 1961 -853 2086 C ATOM 2075 CG PHE A 268 -24.400 49.548 7.388 1.00102.71 C ANISOU 2075 CG PHE A 268 13189 16538 9298 1812 -679 1884 C ATOM 2076 CD1 PHE A 268 -24.728 50.883 7.218 1.00100.81 C ANISOU 2076 CD1 PHE A 268 12918 16323 9062 1732 -765 1567 C ATOM 2077 CD2 PHE A 268 -24.901 48.619 6.490 1.00100.53 C ANISOU 2077 CD2 PHE A 268 12796 16055 9345 1753 -438 2008 C ATOM 2078 CE1 PHE A 268 -25.545 51.285 6.179 1.00 98.02 C ANISOU 2078 CE1 PHE A 268 12425 15802 9016 1622 -639 1414 C ATOM 2079 CE2 PHE A 268 -25.719 49.014 5.447 1.00 98.30 C ANISOU 2079 CE2 PHE A 268 12376 15625 9348 1623 -330 1822 C ATOM 2080 CZ PHE A 268 -26.042 50.349 5.292 1.00 97.02 C ANISOU 2080 CZ PHE A 268 12188 15500 9174 1570 -444 1543 C ATOM 2081 N LYS A 269 -24.866 46.629 10.243 1.00120.21 N ANISOU 2081 N LYS A 269 15974 18927 10775 2208 -137 2740 N ATOM 2082 CA LYS A 269 -25.753 45.469 10.228 1.00122.12 C ANISOU 2082 CA LYS A 269 16254 18983 11161 2230 320 2959 C ATOM 2083 C LYS A 269 -26.891 45.605 11.235 1.00126.09 C ANISOU 2083 C LYS A 269 17010 19527 11369 2266 648 2927 C ATOM 2084 O LYS A 269 -27.929 44.957 11.101 1.00126.13 O ANISOU 2084 O LYS A 269 17004 19342 11576 2232 1078 2979 O ATOM 2085 CB LYS A 269 -24.970 44.189 10.529 1.00124.04 C ANISOU 2085 CB LYS A 269 16544 19201 11386 2385 348 3373 C ATOM 2086 CG LYS A 269 -24.161 43.638 9.368 1.00120.55 C ANISOU 2086 CG LYS A 269 15824 18590 11390 2325 241 3450 C ATOM 2087 CD LYS A 269 -23.410 42.380 9.790 1.00121.46 C ANISOU 2087 CD LYS A 269 15985 18666 11500 2501 298 3883 C ATOM 2088 CE LYS A 269 -22.744 41.701 8.607 1.00117.25 C ANISOU 2088 CE LYS A 269 15174 17902 11473 2422 308 3959 C ATOM 2089 NZ LYS A 269 -21.921 40.534 9.022 1.00119.12 N ANISOU 2089 NZ LYS A 269 15425 18085 11750 2607 349 4391 N ATOM 2090 N GLN A 270 -26.687 46.446 12.244 1.00130.15 N ANISOU 2090 N GLN A 270 17751 20278 11422 2324 463 2821 N ATOM 2091 CA GLN A 270 -27.623 46.546 13.360 1.00135.01 C ANISOU 2091 CA GLN A 270 18671 20942 11684 2372 786 2813 C ATOM 2092 C GLN A 270 -29.014 47.024 12.945 1.00134.00 C ANISOU 2092 C GLN A 270 18438 20627 11848 2225 1135 2542 C ATOM 2093 O GLN A 270 -29.230 48.214 12.711 1.00132.37 O ANISOU 2093 O GLN A 270 18145 20462 11686 2118 994 2212 O ATOM 2094 CB GLN A 270 -27.056 47.442 14.465 1.00138.89 C ANISOU 2094 CB GLN A 270 19427 21738 11606 2435 485 2700 C ATOM 2095 CG GLN A 270 -27.890 47.455 15.739 1.00143.59 C ANISOU 2095 CG GLN A 270 20412 22396 11750 2497 833 2727 C ATOM 2096 CD GLN A 270 -27.203 48.176 16.884 1.00147.17 C ANISOU 2096 CD GLN A 270 21166 23182 11570 2565 509 2644 C ATOM 2097 OE1 GLN A 270 -26.061 48.621 16.758 1.00147.11 O ANISOU 2097 OE1 GLN A 270 21050 23363 11481 2575 4 2574 O ATOM 2098 NE2 GLN A 270 -27.897 48.292 18.011 1.00150.25 N ANISOU 2098 NE2 GLN A 270 21938 23636 11513 2603 812 2632 N ATOM 2099 N ASP A 271 -29.943 46.076 12.857 1.00135.57 N ANISOU 2099 N ASP A 271 18626 20606 12279 2226 1600 2685 N ATOM 2100 CA ASP A 271 -31.351 46.359 12.589 1.00136.30 C ANISOU 2100 CA ASP A 271 18610 20504 12675 2106 1976 2459 C ATOM 2101 C ASP A 271 -31.589 47.146 11.304 1.00133.39 C ANISOU 2101 C ASP A 271 17882 20055 12746 1945 1772 2159 C ATOM 2102 O ASP A 271 -32.242 48.189 11.321 1.00132.61 O ANISOU 2102 O ASP A 271 17740 19953 12694 1869 1790 1878 O ATOM 2103 CB ASP A 271 -31.994 47.083 13.776 1.00140.72 C ANISOU 2103 CB ASP A 271 19466 21146 12856 2129 2182 2322 C ATOM 2104 CG ASP A 271 -32.003 46.240 15.035 1.00147.09 C ANISOU 2104 CG ASP A 271 20670 21993 13224 2288 2482 2629 C ATOM 2105 OD1 ASP A 271 -31.073 45.425 15.216 1.00148.57 O ANISOU 2105 OD1 ASP A 271 20954 22270 13227 2420 2323 2950 O ATOM 2106 OD2 ASP A 271 -32.941 46.392 15.845 1.00150.71 O ANISOU 2106 OD2 ASP A 271 21350 22379 13532 2288 2892 2561 O ATOM 2107 N LEU A 272 -31.061 46.646 10.193 1.00132.43 N ANISOU 2107 N LEU A 272 17518 19857 12943 1897 1596 2227 N ATOM 2108 CA LEU A 272 -31.328 47.255 8.896 1.00131.07 C ANISOU 2108 CA LEU A 272 17033 19594 13173 1752 1429 1980 C ATOM 2109 C LEU A 272 -32.365 46.436 8.130 1.00132.74 C ANISOU 2109 C LEU A 272 17028 19569 13839 1660 1756 1971 C ATOM 2110 O LEU A 272 -32.337 45.205 8.162 1.00135.32 O ANISOU 2110 O LEU A 272 17368 19787 14258 1689 1996 2194 O ATOM 2111 CB LEU A 272 -30.039 47.420 8.077 1.00126.60 C ANISOU 2111 CB LEU A 272 16351 19097 12656 1734 1002 2001 C ATOM 2112 CG LEU A 272 -29.499 46.265 7.227 1.00123.14 C ANISOU 2112 CG LEU A 272 15772 18532 12483 1710 1012 2199 C ATOM 2113 CD1 LEU A 272 -28.332 46.741 6.377 1.00118.60 C ANISOU 2113 CD1 LEU A 272 15077 18001 11986 1668 608 2140 C ATOM 2114 CD2 LEU A 272 -29.084 45.083 8.088 1.00126.01 C ANISOU 2114 CD2 LEU A 272 16317 18903 12660 1849 1200 2544 C ATOM 2115 N PRO A 273 -33.303 47.122 7.460 1.00131.89 N ANISOU 2115 N PRO A 273 16708 19375 14031 1551 1772 1708 N ATOM 2116 CA PRO A 273 -34.338 46.453 6.664 1.00130.89 C ANISOU 2116 CA PRO A 273 16328 19043 14360 1446 2022 1641 C ATOM 2117 C PRO A 273 -33.733 45.591 5.557 1.00129.57 C ANISOU 2117 C PRO A 273 16005 18809 14416 1375 1902 1735 C ATOM 2118 O PRO A 273 -32.807 46.020 4.868 1.00127.76 O ANISOU 2118 O PRO A 273 15740 18662 14143 1351 1537 1714 O ATOM 2119 CB PRO A 273 -35.123 47.621 6.067 1.00129.20 C ANISOU 2119 CB PRO A 273 15911 18812 14366 1368 1883 1347 C ATOM 2120 CG PRO A 273 -34.914 48.740 7.024 1.00129.85 C ANISOU 2120 CG PRO A 273 16199 19032 14106 1443 1800 1271 C ATOM 2121 CD PRO A 273 -33.506 48.580 7.512 1.00130.34 C ANISOU 2121 CD PRO A 273 16494 19264 13766 1529 1576 1456 C ATOM 2122 N LYS A 274 -34.260 44.382 5.397 1.00129.79 N ANISOU 2122 N LYS A 274 15946 18667 14702 1331 2246 1823 N ATOM 2123 CA LYS A 274 -33.704 43.419 4.456 1.00128.20 C ANISOU 2123 CA LYS A 274 15620 18375 14715 1253 2218 1915 C ATOM 2124 C LYS A 274 -34.059 43.761 3.008 1.00125.29 C ANISOU 2124 C LYS A 274 14980 17964 14661 1087 1998 1667 C ATOM 2125 O LYS A 274 -33.433 43.257 2.077 1.00123.51 O ANISOU 2125 O LYS A 274 14676 17694 14559 1001 1883 1693 O ATOM 2126 CB LYS A 274 -34.179 42.003 4.806 1.00130.58 C ANISOU 2126 CB LYS A 274 15918 18486 15208 1254 2709 2076 C ATOM 2127 CG LYS A 274 -33.350 40.876 4.196 1.00130.34 C ANISOU 2127 CG LYS A 274 15841 18356 15325 1215 2753 2253 C ATOM 2128 CD LYS A 274 -31.927 40.850 4.739 1.00128.88 C ANISOU 2128 CD LYS A 274 15874 18297 14798 1367 2539 2532 C ATOM 2129 CE LYS A 274 -31.170 39.624 4.245 1.00126.09 C ANISOU 2129 CE LYS A 274 15463 17795 14650 1343 2670 2739 C ATOM 2130 NZ LYS A 274 -29.752 39.617 4.695 1.00124.45 N ANISOU 2130 NZ LYS A 274 15412 17700 14173 1494 2422 3007 N ATOM 2131 N TYR A 275 -35.052 44.625 2.820 1.00125.95 N ANISOU 2131 N TYR A 275 14930 18058 14869 1045 1942 1432 N ATOM 2132 CA TYR A 275 -35.501 44.974 1.473 1.00125.57 C ANISOU 2132 CA TYR A 275 14631 17984 15094 908 1714 1211 C ATOM 2133 C TYR A 275 -34.484 45.841 0.727 1.00122.66 C ANISOU 2133 C TYR A 275 14314 17733 14556 906 1272 1189 C ATOM 2134 O TYR A 275 -34.546 45.972 -0.495 1.00119.61 O ANISOU 2134 O TYR A 275 13788 17329 14329 797 1067 1065 O ATOM 2135 CB TYR A 275 -36.889 45.632 1.495 1.00128.84 C ANISOU 2135 CB TYR A 275 14856 18362 15735 886 1777 991 C ATOM 2136 CG TYR A 275 -36.898 47.110 1.826 1.00131.01 C ANISOU 2136 CG TYR A 275 15194 18751 15834 973 1544 905 C ATOM 2137 CD1 TYR A 275 -36.975 47.548 3.141 1.00133.74 C ANISOU 2137 CD1 TYR A 275 15730 19132 15953 1085 1726 954 C ATOM 2138 CD2 TYR A 275 -36.853 48.068 0.819 1.00130.76 C ANISOU 2138 CD2 TYR A 275 15043 18778 15860 940 1169 770 C ATOM 2139 CE1 TYR A 275 -36.992 48.899 3.446 1.00134.69 C ANISOU 2139 CE1 TYR A 275 15901 19338 15939 1145 1551 846 C ATOM 2140 CE2 TYR A 275 -36.869 49.420 1.115 1.00131.58 C ANISOU 2140 CE2 TYR A 275 15192 18954 15847 1020 1000 692 C ATOM 2141 CZ TYR A 275 -36.938 49.830 2.430 1.00133.48 C ANISOU 2141 CZ TYR A 275 15602 19222 15894 1114 1198 717 C ATOM 2142 OH TYR A 275 -36.954 51.173 2.728 1.00133.47 O ANISOU 2142 OH TYR A 275 15639 19275 15798 1175 1064 612 O ATOM 2143 N LEU A 276 -33.552 46.433 1.468 1.00123.98 N ANISOU 2143 N LEU A 276 14692 18017 14399 1023 1135 1299 N ATOM 2144 CA LEU A 276 -32.431 47.134 0.858 1.00124.26 C ANISOU 2144 CA LEU A 276 14784 18130 14300 1024 773 1293 C ATOM 2145 C LEU A 276 -31.423 46.093 0.394 1.00128.21 C ANISOU 2145 C LEU A 276 15315 18566 14832 979 788 1455 C ATOM 2146 O LEU A 276 -31.309 45.033 1.012 1.00133.15 O ANISOU 2146 O LEU A 276 15998 19138 15455 1016 1049 1634 O ATOM 2147 CB LEU A 276 -31.767 48.069 1.869 1.00121.98 C ANISOU 2147 CB LEU A 276 14680 17980 13686 1151 635 1325 C ATOM 2148 CG LEU A 276 -32.663 49.032 2.648 1.00121.08 C ANISOU 2148 CG LEU A 276 14587 17918 13502 1207 705 1187 C ATOM 2149 CD1 LEU A 276 -31.829 49.877 3.596 1.00120.06 C ANISOU 2149 CD1 LEU A 276 14657 17935 13026 1306 556 1195 C ATOM 2150 CD2 LEU A 276 -33.458 49.913 1.703 1.00120.18 C ANISOU 2150 CD2 LEU A 276 14278 17758 13628 1144 565 979 C ATOM 2151 N PHE A 277 -30.713 46.387 -0.695 1.00126.30 N ANISOU 2151 N PHE A 277 15042 18306 14640 904 543 1401 N ATOM 2152 CA PHE A 277 -29.664 45.505 -1.217 1.00125.08 C ANISOU 2152 CA PHE A 277 14913 18063 14549 850 562 1535 C ATOM 2153 C PHE A 277 -30.241 44.191 -1.785 1.00127.79 C ANISOU 2153 C PHE A 277 15137 18257 15158 720 847 1539 C ATOM 2154 O PHE A 277 -31.369 43.828 -1.457 1.00126.99 O ANISOU 2154 O PHE A 277 14950 18129 15171 704 1067 1483 O ATOM 2155 CB PHE A 277 -28.588 45.279 -0.142 1.00125.39 C ANISOU 2155 CB PHE A 277 15097 18161 14385 992 561 1759 C ATOM 2156 CG PHE A 277 -28.014 46.555 0.406 1.00124.85 C ANISOU 2156 CG PHE A 277 15126 18243 14070 1093 278 1705 C ATOM 2157 CD1 PHE A 277 -27.239 47.379 -0.394 1.00123.49 C ANISOU 2157 CD1 PHE A 277 14940 18063 13919 1050 10 1599 C ATOM 2158 CD2 PHE A 277 -28.255 46.936 1.715 1.00126.91 C ANISOU 2158 CD2 PHE A 277 15503 18637 14081 1221 310 1742 C ATOM 2159 CE1 PHE A 277 -26.712 48.557 0.103 1.00123.48 C ANISOU 2159 CE1 PHE A 277 15007 18177 13733 1130 -220 1520 C ATOM 2160 CE2 PHE A 277 -27.729 48.113 2.218 1.00126.89 C ANISOU 2160 CE2 PHE A 277 15582 18771 13858 1291 61 1652 C ATOM 2161 CZ PHE A 277 -26.958 48.924 1.411 1.00125.02 C ANISOU 2161 CZ PHE A 277 15299 18518 13684 1244 -203 1534 C ATOM 2162 N PRO A 278 -29.483 43.491 -2.659 1.00131.63 N ANISOU 2162 N PRO A 278 15610 18627 15776 613 868 1580 N ATOM 2163 CA PRO A 278 -29.991 42.326 -3.403 1.00136.26 C ANISOU 2163 CA PRO A 278 16076 19063 16635 448 1125 1522 C ATOM 2164 C PRO A 278 -30.854 41.332 -2.621 1.00140.58 C ANISOU 2164 C PRO A 278 16554 19537 17324 467 1511 1591 C ATOM 2165 O PRO A 278 -31.980 41.058 -3.036 1.00140.43 O ANISOU 2165 O PRO A 278 16381 19473 17503 352 1634 1406 O ATOM 2166 CB PRO A 278 -28.708 41.633 -3.899 1.00135.64 C ANISOU 2166 CB PRO A 278 16050 18855 16631 394 1173 1654 C ATOM 2167 CG PRO A 278 -27.564 42.356 -3.229 1.00134.48 C ANISOU 2167 CG PRO A 278 16030 18798 16267 559 949 1809 C ATOM 2168 CD PRO A 278 -28.073 43.737 -3.000 1.00132.47 C ANISOU 2168 CD PRO A 278 15804 18713 15814 628 681 1664 C ATOM 2169 N GLU A 279 -30.341 40.806 -1.514 1.00146.46 N ANISOU 2169 N GLU A 279 17407 20264 17976 615 1697 1854 N ATOM 2170 CA GLU A 279 -31.049 39.764 -0.775 1.00152.81 C ANISOU 2170 CA GLU A 279 18181 20957 18921 645 2128 1962 C ATOM 2171 C GLU A 279 -31.610 40.265 0.558 1.00156.65 C ANISOU 2171 C GLU A 279 18780 21553 19186 819 2195 2038 C ATOM 2172 O GLU A 279 -30.904 40.914 1.330 1.00155.94 O ANISOU 2172 O GLU A 279 18862 21607 18782 975 1994 2176 O ATOM 2173 CB GLU A 279 -30.128 38.563 -0.558 1.00155.26 C ANISOU 2173 CB GLU A 279 18544 21118 19329 685 2380 2240 C ATOM 2174 CG GLU A 279 -29.592 37.981 -1.854 1.00155.83 C ANISOU 2174 CG GLU A 279 18514 21043 19652 493 2393 2151 C ATOM 2175 CD GLU A 279 -28.347 37.146 -1.649 1.00158.39 C ANISOU 2175 CD GLU A 279 18899 21239 20042 566 2526 2447 C ATOM 2176 OE1 GLU A 279 -28.039 36.811 -0.485 1.00160.74 O ANISOU 2176 OE1 GLU A 279 19302 21553 20218 769 2651 2742 O ATOM 2177 OE2 GLU A 279 -27.672 36.832 -2.652 1.00158.25 O ANISOU 2177 OE2 GLU A 279 18829 21099 20198 425 2509 2390 O ATOM 2178 N ASP A 280 -32.881 39.965 0.822 1.00160.86 N ANISOU 2178 N ASP A 280 19215 22010 19895 779 2489 1928 N ATOM 2179 CA ASP A 280 -33.711 39.190 -0.098 1.00163.86 C ANISOU 2179 CA ASP A 280 19360 22227 20671 580 2706 1728 C ATOM 2180 C ASP A 280 -34.483 40.088 -1.064 1.00164.34 C ANISOU 2180 C ASP A 280 19243 22372 20828 450 2402 1397 C ATOM 2181 O ASP A 280 -34.966 41.158 -0.688 1.00164.87 O ANISOU 2181 O ASP A 280 19321 22561 20762 529 2220 1311 O ATOM 2182 CB ASP A 280 -34.682 38.290 0.674 1.00167.03 C ANISOU 2182 CB ASP A 280 19713 22466 21286 598 3223 1772 C ATOM 2183 CG ASP A 280 -35.777 39.074 1.374 1.00168.42 C ANISOU 2183 CG ASP A 280 19870 22701 21420 663 3263 1644 C ATOM 2184 OD1 ASP A 280 -36.813 39.352 0.734 1.00168.82 O ANISOU 2184 OD1 ASP A 280 19680 22728 21736 531 3221 1352 O ATOM 2185 OD2 ASP A 280 -35.606 39.406 2.565 1.00169.37 O ANISOU 2185 OD2 ASP A 280 20215 22891 21249 844 3338 1831 O ATOM 2186 N ALA A 321 -45.594 33.041 -18.989 1.00147.09 N ANISOU 2186 N ALA A 321 17732 15685 22472 -1517 1623 -1779 N ATOM 2187 CA ALA A 321 -44.303 33.718 -18.930 1.00143.13 C ANISOU 2187 CA ALA A 321 17707 15010 21668 -1434 1500 -2324 C ATOM 2188 C ALA A 321 -43.963 34.145 -17.504 1.00143.80 C ANISOU 2188 C ALA A 321 17481 16107 21051 -959 1688 -2451 C ATOM 2189 O ALA A 321 -43.694 35.319 -17.245 1.00143.29 O ANISOU 2189 O ALA A 321 17642 16174 20628 -614 1478 -3145 O ATOM 2190 CB ALA A 321 -44.294 34.921 -19.861 1.00141.26 C ANISOU 2190 CB ALA A 321 17980 14634 21057 -1242 951 -2667 C ATOM 2191 N VAL A 322 -43.974 33.183 -16.585 1.00144.19 N ANISOU 2191 N VAL A 322 17023 16852 20911 -954 2023 -1766 N ATOM 2192 CA VAL A 322 -43.699 33.460 -15.177 1.00145.42 C ANISOU 2192 CA VAL A 322 16820 18071 20362 -513 2237 -1799 C ATOM 2193 C VAL A 322 -42.417 32.779 -14.704 1.00141.83 C ANISOU 2193 C VAL A 322 16476 17639 19775 -686 2360 -1470 C ATOM 2194 O VAL A 322 -42.407 32.097 -13.679 1.00144.85 O ANISOU 2194 O VAL A 322 16378 18808 19851 -627 2628 -900 O ATOM 2195 CB VAL A 322 -44.865 33.010 -14.276 1.00151.48 C ANISOU 2195 CB VAL A 322 16772 19926 20858 -310 2539 -1244 C ATOM 2196 N ALA A 323 -41.339 32.972 -15.457 1.00135.39 N ANISOU 2196 N ALA A 323 16265 16003 19173 -912 2145 -1813 N ATOM 2197 CA ALA A 323 -40.046 32.393 -15.111 1.00132.08 C ANISOU 2197 CA ALA A 323 15985 15549 18652 -1056 2221 -1590 C ATOM 2198 C ALA A 323 -39.209 33.366 -14.286 1.00133.92 C ANISOU 2198 C ALA A 323 16370 16232 18280 -686 2172 -2117 C ATOM 2199 O ALA A 323 -38.121 33.023 -13.822 1.00132.85 O ANISOU 2199 O ALA A 323 16313 16197 17965 -735 2240 -1978 O ATOM 2200 CB ALA A 323 -39.297 31.981 -16.368 1.00124.92 C ANISOU 2200 CB ALA A 323 15570 13632 18264 -1486 2028 -1639 C ATOM 2201 N TYR A 324 -39.723 34.580 -14.110 1.00136.71 N ANISOU 2201 N TYR A 324 16778 16825 18342 -296 1994 -2740 N ATOM 2202 CA TYR A 324 -39.041 35.596 -13.317 1.00138.48 C ANISOU 2202 CA TYR A 324 17171 17441 18004 113 1831 -3298 C ATOM 2203 C TYR A 324 -39.010 35.196 -11.847 1.00141.91 C ANISOU 2203 C TYR A 324 17090 18965 17866 460 2166 -2955 C ATOM 2204 O TYR A 324 -38.110 35.585 -11.105 1.00143.77 O ANISOU 2204 O TYR A 324 17455 19499 17674 681 2109 -3181 O ATOM 2205 CB TYR A 324 -39.724 36.955 -13.480 1.00140.59 C ANISOU 2205 CB TYR A 324 17609 17669 18141 503 1452 -4070 C ATOM 2206 N HIS A 325 -40.000 34.411 -11.434 1.00142.32 N ANISOU 2206 N HIS A 325 16539 19636 17900 474 2490 -2366 N ATOM 2207 CA HIS A 325 -40.040 33.879 -10.078 1.00143.55 C ANISOU 2207 CA HIS A 325 16125 20908 17510 701 2827 -1881 C ATOM 2208 C HIS A 325 -39.119 32.668 -9.965 1.00138.48 C ANISOU 2208 C HIS A 325 15496 20035 17084 242 2974 -1171 C ATOM 2209 O HIS A 325 -38.953 32.098 -8.886 1.00142.03 O ANISOU 2209 O HIS A 325 15534 21291 17141 311 3210 -670 O ATOM 2210 CB HIS A 325 -41.471 33.499 -9.693 1.00148.59 C ANISOU 2210 CB HIS A 325 16047 22388 18022 827 3082 -1433 C ATOM 2211 N LEU A 326 -38.522 32.283 -11.089 1.00131.05 N ANISOU 2211 N LEU A 326 15019 18018 16755 -208 2801 -1151 N ATOM 2212 CA LEU A 326 -37.588 31.162 -11.131 1.00128.39 C ANISOU 2212 CA LEU A 326 14756 17337 16688 -591 2846 -606 C ATOM 2213 C LEU A 326 -36.174 31.636 -11.459 1.00122.84 C ANISOU 2213 C LEU A 326 14614 16095 15965 -627 2656 -1107 C ATOM 2214 O LEU A 326 -35.191 31.005 -11.071 1.00122.07 O ANISOU 2214 O LEU A 326 14541 16010 15830 -746 2703 -823 O ATOM 2215 CB LEU A 326 -38.042 30.121 -12.156 1.00126.88 C ANISOU 2215 CB LEU A 326 14567 16417 17223 -1057 2776 -109 C ATOM 2216 N ILE A 327 -36.080 32.748 -12.181 1.00119.35 N ANISOU 2216 N ILE A 327 14600 15192 15554 -551 2401 -1819 N ATOM 2217 CA ILE A 327 -34.788 33.342 -12.501 1.00115.01 C ANISOU 2217 CA ILE A 327 14543 14220 14937 -622 2171 -2271 C ATOM 2218 C ILE A 327 -34.255 34.120 -11.302 1.00119.10 C ANISOU 2218 C ILE A 327 15045 15398 14809 -208 2136 -2573 C ATOM 2219 O ILE A 327 -33.047 34.296 -11.152 1.00118.33 O ANISOU 2219 O ILE A 327 15209 15181 14572 -267 2023 -2706 O ATOM 2220 CB ILE A 327 -34.880 34.282 -13.718 1.00110.05 C ANISOU 2220 CB ILE A 327 14375 12870 14571 -770 1824 -2847 C ATOM 2221 N ILE A 328 -35.165 34.585 -10.453 1.00123.43 N ANISOU 2221 N ILE A 328 15268 16684 14947 238 2215 -2695 N ATOM 2222 CA ILE A 328 -34.786 35.276 -9.227 1.00125.93 C ANISOU 2222 CA ILE A 328 15523 17727 14597 722 2171 -2999 C ATOM 2223 C ILE A 328 -34.485 34.262 -8.130 1.00128.27 C ANISOU 2223 C ILE A 328 15386 18748 14604 734 2539 -2339 C ATOM 2224 O ILE A 328 -33.771 34.560 -7.173 1.00131.12 O ANISOU 2224 O ILE A 328 15762 19581 14477 1002 2521 -2464 O ATOM 2225 CB ILE A 328 -35.895 36.228 -8.746 1.00129.79 C ANISOU 2225 CB ILE A 328 15809 18811 14693 1298 2067 -3495 C ATOM 2226 N ASP A 329 -35.038 33.062 -8.276 1.00127.30 N ANISOU 2226 N ASP A 329 14888 18679 14799 420 2812 -1610 N ATOM 2227 CA ASP A 329 -34.794 31.984 -7.327 1.00128.97 C ANISOU 2227 CA ASP A 329 14686 19491 14827 319 3082 -862 C ATOM 2228 C ASP A 329 -33.464 31.299 -7.624 1.00124.54 C ANISOU 2228 C ASP A 329 14438 18295 14588 -42 2999 -649 C ATOM 2229 O ASP A 329 -32.720 30.944 -6.709 1.00126.79 O ANISOU 2229 O ASP A 329 14615 18995 14565 8 3080 -388 O ATOM 2230 CB ASP A 329 -35.934 30.963 -7.365 1.00131.19 C ANISOU 2230 CB ASP A 329 14435 20052 15360 76 3291 -98 C ATOM 2231 N ASN A 330 -33.172 31.118 -8.909 1.00118.45 N ANISOU 2231 N ASN A 330 14033 16560 14411 -381 2828 -782 N ATOM 2232 CA ASN A 330 -31.922 30.498 -9.334 1.00112.54 C ANISOU 2232 CA ASN A 330 13560 15232 13968 -669 2727 -676 C ATOM 2233 C ASN A 330 -30.712 31.351 -8.967 1.00112.17 C ANISOU 2233 C ASN A 330 13837 15244 13539 -498 2594 -1170 C ATOM 2234 O ASN A 330 -29.652 30.825 -8.638 1.00112.20 O ANISOU 2234 O ASN A 330 13881 15226 13526 -591 2596 -972 O ATOM 2235 CB ASN A 330 -31.939 30.224 -10.839 1.00105.64 C ANISOU 2235 CB ASN A 330 12978 13431 13728 -1002 2566 -799 C ATOM 2236 N ARG A 331 -30.882 32.670 -9.017 1.00112.52 N ANISOU 2236 N ARG A 331 14112 15340 13298 -247 2418 -1804 N ATOM 2237 CA ARG A 331 -29.803 33.602 -8.701 1.00112.07 C ANISOU 2237 CA ARG A 331 14393 15289 12899 -104 2179 -2275 C ATOM 2238 C ARG A 331 -29.387 33.520 -7.233 1.00116.33 C ANISOU 2238 C ARG A 331 14710 16603 12887 209 2306 -2103 C ATOM 2239 O ARG A 331 -28.205 33.630 -6.906 1.00114.94 O ANISOU 2239 O ARG A 331 14724 16387 12560 181 2195 -2170 O ATOM 2240 CB ARG A 331 -30.210 35.035 -9.053 1.00111.25 C ANISOU 2240 CB ARG A 331 14594 15021 12655 103 1833 -2971 C ATOM 2241 N ARG A 332 -30.365 33.328 -6.353 1.00121.18 N ANISOU 2241 N ARG A 332 14892 17979 13174 498 2537 -1864 N ATOM 2242 CA ARG A 332 -30.099 33.224 -4.923 1.00125.44 C ANISOU 2242 CA ARG A 332 15160 19383 13120 807 2680 -1666 C ATOM 2243 C ARG A 332 -29.261 31.987 -4.614 1.00126.79 C ANISOU 2243 C ARG A 332 15199 19507 13468 477 2833 -1003 C ATOM 2244 O ARG A 332 -28.460 31.984 -3.679 1.00129.22 O ANISOU 2244 O ARG A 332 15499 20203 13397 615 2834 -936 O ATOM 2245 CB ARG A 332 -31.409 33.185 -4.132 1.00129.31 C ANISOU 2245 CB ARG A 332 15113 20824 13195 1146 2926 -1476 C ATOM 2246 N ILE A 333 -29.449 30.940 -5.410 1.00125.44 N ANISOU 2246 N ILE A 333 14944 18822 13894 61 2902 -538 N ATOM 2247 CA ILE A 333 -28.706 29.699 -5.231 1.00125.85 C ANISOU 2247 CA ILE A 333 14893 18711 14215 -239 2939 62 C ATOM 2248 C ILE A 333 -27.274 29.837 -5.737 1.00122.72 C ANISOU 2248 C ILE A 333 14916 17709 14002 -362 2740 -267 C ATOM 2249 O ILE A 333 -26.394 29.064 -5.355 1.00124.01 O ANISOU 2249 O ILE A 333 15036 17843 14239 -480 2722 66 O ATOM 2250 CB ILE A 333 -29.386 28.524 -5.958 1.00125.36 C ANISOU 2250 CB ILE A 333 14633 18224 14772 -604 2958 625 C ATOM 2251 N MET A 334 -27.047 30.825 -6.597 1.00118.84 N ANISOU 2251 N MET A 334 14804 16771 13579 -351 2560 -896 N ATOM 2252 CA MET A 334 -25.719 31.079 -7.145 1.00115.12 C ANISOU 2252 CA MET A 334 14680 15837 13223 -501 2360 -1200 C ATOM 2253 C MET A 334 -24.850 31.832 -6.144 1.00116.65 C ANISOU 2253 C MET A 334 14994 16443 12884 -262 2252 -1428 C ATOM 2254 O MET A 334 -23.700 31.463 -5.902 1.00115.38 O ANISOU 2254 O MET A 334 14882 16236 12720 -352 2206 -1308 O ATOM 2255 CB MET A 334 -25.818 31.865 -8.454 1.00111.29 C ANISOU 2255 CB MET A 334 14524 14775 12986 -659 2160 -1697 C ATOM 2256 N ASN A 335 -25.410 32.888 -5.562 1.00119.46 N ANISOU 2256 N ASN A 335 15397 17198 12794 77 2170 -1785 N ATOM 2257 CA ASN A 335 -24.699 33.684 -4.570 1.00121.51 C ANISOU 2257 CA ASN A 335 15798 17846 12524 369 1991 -2055 C ATOM 2258 C ASN A 335 -24.503 32.927 -3.259 1.00125.53 C ANISOU 2258 C ASN A 335 15980 19023 12695 527 2227 -1578 C ATOM 2259 O ASN A 335 -23.608 33.248 -2.478 1.00127.44 O ANISOU 2259 O ASN A 335 16336 19494 12591 674 2099 -1669 O ATOM 2260 CB ASN A 335 -25.436 35.001 -4.315 1.00123.32 C ANISOU 2260 CB ASN A 335 16171 18306 12378 773 1753 -2636 C ATOM 2261 N GLU A 336 -25.344 31.923 -3.024 1.00127.14 N ANISOU 2261 N GLU A 336 15773 19534 13002 460 2528 -1026 N ATOM 2262 CA GLU A 336 -25.259 31.111 -1.813 1.00129.21 C ANISOU 2262 CA GLU A 336 15673 20462 12959 521 2726 -450 C ATOM 2263 C GLU A 336 -23.970 30.295 -1.788 1.00125.94 C ANISOU 2263 C GLU A 336 15349 19688 12814 246 2655 -141 C ATOM 2264 O GLU A 336 -23.276 30.242 -0.772 1.00127.69 O ANISOU 2264 O GLU A 336 15532 20316 12669 371 2641 -6 O ATOM 2265 CB GLU A 336 -26.472 30.185 -1.701 1.00131.33 C ANISOU 2265 CB GLU A 336 15463 21090 13348 396 2983 171 C ATOM 2266 N ALA A 337 -23.657 29.660 -2.911 1.00121.19 N ANISOU 2266 N ALA A 337 14859 18345 12842 -94 2590 -60 N ATOM 2267 CA ALA A 337 -22.411 28.918 -3.050 1.00119.11 C ANISOU 2267 CA ALA A 337 14680 17706 12871 -299 2477 117 C ATOM 2268 C ALA A 337 -21.427 29.713 -3.902 1.00112.61 C ANISOU 2268 C ALA A 337 14238 16406 12143 -355 2274 -460 C ATOM 2269 O ALA A 337 -21.196 29.391 -5.067 1.00109.26 O ANISOU 2269 O ALA A 337 13910 15423 12179 -577 2208 -566 O ATOM 2270 CB ALA A 337 -22.670 27.554 -3.665 1.00119.89 C ANISOU 2270 CB ALA A 337 14598 17375 13581 -585 2476 604 C ATOM 2271 N LYS A 338 -20.852 30.755 -3.308 1.00110.46 N ANISOU 2271 N LYS A 338 14163 16396 11410 -160 2140 -812 N ATOM 2272 CA LYS A 338 -19.954 31.656 -4.022 1.00103.65 C ANISOU 2272 CA LYS A 338 13642 15168 10573 -264 1876 -1292 C ATOM 2273 C LYS A 338 -18.638 30.982 -4.393 1.00102.54 C ANISOU 2273 C LYS A 338 13500 14759 10701 -486 1813 -1163 C ATOM 2274 O LYS A 338 -17.951 31.415 -5.318 1.00101.05 O ANISOU 2274 O LYS A 338 13485 14255 10653 -682 1645 -1446 O ATOM 2275 CB LYS A 338 -19.684 32.913 -3.190 1.00102.68 C ANISOU 2275 CB LYS A 338 13737 15372 9904 9 1641 -1655 C ATOM 2276 N ASP A 339 -18.295 29.914 -3.677 1.00103.91 N ANISOU 2276 N ASP A 339 13447 15101 10931 -460 1922 -721 N ATOM 2277 CA ASP A 339 -17.046 29.191 -3.914 1.00102.12 C ANISOU 2277 CA ASP A 339 13180 14664 10955 -592 1833 -617 C ATOM 2278 C ASP A 339 -17.003 28.556 -5.304 1.00 98.40 C ANISOU 2278 C ASP A 339 12677 13699 11013 -783 1821 -702 C ATOM 2279 O ASP A 339 -15.960 28.081 -5.751 1.00 98.38 O ANISOU 2279 O ASP A 339 12633 13541 11207 -849 1722 -759 O ATOM 2280 CB ASP A 339 -16.838 28.120 -2.839 1.00104.30 C ANISOU 2280 CB ASP A 339 13225 15174 11229 -522 1885 -99 C ATOM 2281 N PHE A 340 -18.145 28.562 -5.980 1.00 95.82 N ANISOU 2281 N PHE A 340 12352 13167 10888 -837 1907 -740 N ATOM 2282 CA PHE A 340 -18.289 27.942 -7.288 1.00 92.63 C ANISOU 2282 CA PHE A 340 11927 12297 10971 -982 1883 -826 C ATOM 2283 C PHE A 340 -18.020 28.949 -8.403 1.00 88.86 C ANISOU 2283 C PHE A 340 11659 11664 10439 -1133 1797 -1311 C ATOM 2284 O PHE A 340 -17.632 28.575 -9.511 1.00 86.52 O ANISOU 2284 O PHE A 340 11344 11108 10420 -1248 1744 -1474 O ATOM 2285 CB PHE A 340 -19.702 27.366 -7.413 1.00 93.74 C ANISOU 2285 CB PHE A 340 11949 12286 11382 -997 1987 -544 C ATOM 2286 CG PHE A 340 -19.973 26.670 -8.716 1.00 93.22 C ANISOU 2286 CG PHE A 340 11883 11697 11840 -1115 1915 -620 C ATOM 2287 CD1 PHE A 340 -19.507 25.386 -8.944 1.00 94.68 C ANISOU 2287 CD1 PHE A 340 11940 11596 12439 -1095 1763 -423 C ATOM 2288 CD2 PHE A 340 -20.724 27.289 -9.701 1.00 92.02 C ANISOU 2288 CD2 PHE A 340 11870 11319 11775 -1217 1946 -909 C ATOM 2289 CE1 PHE A 340 -19.768 24.741 -10.139 1.00 94.16 C ANISOU 2289 CE1 PHE A 340 11892 11046 12841 -1137 1638 -551 C ATOM 2290 CE2 PHE A 340 -20.989 26.650 -10.897 1.00 91.31 C ANISOU 2290 CE2 PHE A 340 11791 10762 12142 -1305 1865 -995 C ATOM 2291 CZ PHE A 340 -20.515 25.371 -11.114 1.00 92.27 C ANISOU 2291 CZ PHE A 340 11788 10619 12651 -1246 1710 -830 C ATOM 2292 N TYR A 341 -18.219 30.230 -8.101 1.00 88.94 N ANISOU 2292 N TYR A 341 11862 11856 10074 -1126 1730 -1539 N ATOM 2293 CA TYR A 341 -18.078 31.286 -9.101 1.00 87.63 C ANISOU 2293 CA TYR A 341 11915 11527 9853 -1335 1555 -1929 C ATOM 2294 C TYR A 341 -16.873 32.188 -8.854 1.00 87.68 C ANISOU 2294 C TYR A 341 12054 11736 9522 -1431 1311 -2092 C ATOM 2295 O TYR A 341 -16.349 32.798 -9.786 1.00 86.68 O ANISOU 2295 O TYR A 341 12026 11523 9387 -1704 1124 -2297 O ATOM 2296 CB TYR A 341 -19.351 32.135 -9.174 1.00 88.80 C ANISOU 2296 CB TYR A 341 12223 11593 9924 -1291 1520 -2103 C ATOM 2297 CG TYR A 341 -20.535 31.411 -9.771 1.00 90.70 C ANISOU 2297 CG TYR A 341 12350 11572 10541 -1300 1706 -1976 C ATOM 2298 CD1 TYR A 341 -20.688 31.312 -11.149 1.00 90.44 C ANISOU 2298 CD1 TYR A 341 12379 11155 10828 -1530 1665 -2139 C ATOM 2299 CD2 TYR A 341 -21.499 30.826 -8.959 1.00 92.71 C ANISOU 2299 CD2 TYR A 341 12411 12006 10810 -1101 1900 -1658 C ATOM 2300 CE1 TYR A 341 -21.767 30.650 -11.701 1.00 90.66 C ANISOU 2300 CE1 TYR A 341 12326 10898 11224 -1540 1787 -2018 C ATOM 2301 CE2 TYR A 341 -22.582 30.164 -9.503 1.00 93.52 C ANISOU 2301 CE2 TYR A 341 12393 11863 11278 -1151 2019 -1481 C ATOM 2302 CZ TYR A 341 -22.709 30.079 -10.874 1.00 93.21 C ANISOU 2302 CZ TYR A 341 12464 11355 11596 -1361 1950 -1676 C ATOM 2303 OH TYR A 341 -23.784 29.421 -11.423 1.00 95.53 O ANISOU 2303 OH TYR A 341 12662 11359 12276 -1412 2024 -1498 O ATOM 2304 N LEU A 342 -16.441 32.276 -7.601 1.00 89.64 N ANISOU 2304 N LEU A 342 12293 12283 9482 -1236 1284 -1961 N ATOM 2305 CA LEU A 342 -15.329 33.150 -7.244 1.00 90.55 C ANISOU 2305 CA LEU A 342 12551 12572 9282 -1319 995 -2079 C ATOM 2306 C LEU A 342 -14.246 32.452 -6.430 1.00 94.38 C ANISOU 2306 C LEU A 342 12866 13303 9691 -1219 1051 -1838 C ATOM 2307 O LEU A 342 -14.532 31.582 -5.604 1.00 95.99 O ANISOU 2307 O LEU A 342 12915 13624 9932 -999 1253 -1572 O ATOM 2308 CB LEU A 342 -15.833 34.375 -6.480 1.00 90.34 C ANISOU 2308 CB LEU A 342 12795 12637 8895 -1152 738 -2285 C ATOM 2309 CG LEU A 342 -16.306 35.551 -7.333 1.00 88.24 C ANISOU 2309 CG LEU A 342 12800 12096 8632 -1346 408 -2616 C ATOM 2310 CD1 LEU A 342 -16.675 36.738 -6.457 1.00 91.53 C ANISOU 2310 CD1 LEU A 342 13498 12589 8691 -1086 35 -2882 C ATOM 2311 CD2 LEU A 342 -15.240 35.935 -8.346 1.00 86.02 C ANISOU 2311 CD2 LEU A 342 12556 11706 8420 -1797 153 -2642 C ATOM 2312 N ALA A 343 -13.000 32.851 -6.667 1.00 95.57 N ANISOU 2312 N ALA A 343 13027 13552 9732 -1416 836 -1896 N ATOM 2313 CA ALA A 343 -11.871 32.348 -5.896 1.00 97.41 C ANISOU 2313 CA ALA A 343 13117 14023 9873 -1331 828 -1704 C ATOM 2314 C ALA A 343 -11.719 33.152 -4.613 1.00 97.80 C ANISOU 2314 C ALA A 343 13373 14261 9525 -1169 616 -1694 C ATOM 2315 O ALA A 343 -11.603 34.376 -4.649 1.00 97.37 O ANISOU 2315 O ALA A 343 13574 14177 9244 -1281 266 -1893 O ATOM 2316 CB ALA A 343 -10.595 32.417 -6.716 1.00 97.65 C ANISOU 2316 CB ALA A 343 13005 14169 9930 -1603 692 -1756 C ATOM 2317 N THR A 344 -11.727 32.459 -3.479 1.00 99.45 N ANISOU 2317 N THR A 344 13480 14655 9651 -905 769 -1457 N ATOM 2318 CA THR A 344 -11.583 33.115 -2.187 1.00102.20 C ANISOU 2318 CA THR A 344 14003 15249 9579 -689 585 -1456 C ATOM 2319 C THR A 344 -10.132 33.510 -1.936 1.00101.73 C ANISOU 2319 C THR A 344 13993 15278 9381 -826 288 -1437 C ATOM 2320 O THR A 344 -9.228 33.095 -2.663 1.00 98.45 O ANISOU 2320 O THR A 344 13395 14828 9183 -1057 296 -1375 O ATOM 2321 CB THR A 344 -12.068 32.215 -1.032 1.00106.50 C ANISOU 2321 CB THR A 344 14383 16054 10029 -402 847 -1143 C ATOM 2322 OG1 THR A 344 -11.209 31.074 -0.914 1.00107.21 O ANISOU 2322 OG1 THR A 344 14236 16139 10360 -465 946 -842 O ATOM 2323 CG2 THR A 344 -13.497 31.750 -1.281 1.00107.46 C ANISOU 2323 CG2 THR A 344 14386 16146 10297 -317 1130 -1067 C ATOM 2324 N SER A 345 -9.917 34.316 -0.903 1.00105.04 N ANISOU 2324 N SER A 345 14641 15852 9418 -656 5 -1505 N ATOM 2325 CA SER A 345 -8.576 34.752 -0.543 1.00107.95 C ANISOU 2325 CA SER A 345 15080 16295 9641 -786 -336 -1453 C ATOM 2326 C SER A 345 -7.959 33.810 0.486 1.00110.39 C ANISOU 2326 C SER A 345 15209 16833 9903 -607 -165 -1154 C ATOM 2327 O SER A 345 -8.631 33.383 1.425 1.00113.96 O ANISOU 2327 O SER A 345 15639 17469 10192 -309 28 -1036 O ATOM 2328 CB SER A 345 -8.606 36.183 -0.001 1.00109.59 C ANISOU 2328 CB SER A 345 15683 16467 9490 -698 -865 -1708 C ATOM 2329 OG SER A 345 -9.128 37.083 -0.964 1.00108.37 O ANISOU 2329 OG SER A 345 15717 16042 9415 -901 -1127 -1968 O ATOM 2330 N PRO A 346 -6.673 33.480 0.306 1.00109.85 N ANISOU 2330 N PRO A 346 14977 16801 9960 -802 -253 -1009 N ATOM 2331 CA PRO A 346 -5.966 32.584 1.225 1.00109.48 C ANISOU 2331 CA PRO A 346 14763 16920 9915 -659 -160 -731 C ATOM 2332 C PRO A 346 -5.705 33.260 2.565 1.00111.68 C ANISOU 2332 C PRO A 346 15298 17370 9767 -461 -438 -711 C ATOM 2333 O PRO A 346 -5.608 34.487 2.613 1.00111.69 O ANISOU 2333 O PRO A 346 15593 17319 9527 -502 -830 -930 O ATOM 2334 CB PRO A 346 -4.644 32.320 0.500 1.00109.97 C ANISOU 2334 CB PRO A 346 14587 17005 10193 -919 -255 -682 C ATOM 2335 CG PRO A 346 -4.437 33.528 -0.343 1.00109.80 C ANISOU 2335 CG PRO A 346 14711 16935 10074 -1228 -559 -877 C ATOM 2336 CD PRO A 346 -5.805 33.949 -0.789 1.00108.35 C ANISOU 2336 CD PRO A 346 14716 16558 9893 -1182 -467 -1083 C ATOM 2337 N PRO A 347 -5.603 32.467 3.644 1.00112.31 N ANISOU 2337 N PRO A 347 15279 17638 9756 -248 -298 -447 N ATOM 2338 CA PRO A 347 -5.306 32.957 4.996 1.00116.11 C ANISOU 2338 CA PRO A 347 15972 18343 9801 -24 -538 -407 C ATOM 2339 C PRO A 347 -4.062 33.844 5.031 1.00117.18 C ANISOU 2339 C PRO A 347 16286 18398 9839 -192 -1015 -496 C ATOM 2340 O PRO A 347 -3.141 33.645 4.238 1.00115.90 O ANISOU 2340 O PRO A 347 15938 18135 9966 -491 -1067 -427 O ATOM 2341 CB PRO A 347 -5.077 31.667 5.796 1.00117.28 C ANISOU 2341 CB PRO A 347 15874 18655 10032 69 -305 -6 C ATOM 2342 CG PRO A 347 -4.954 30.570 4.777 1.00114.93 C ANISOU 2342 CG PRO A 347 15258 18133 10278 -123 -68 122 C ATOM 2343 CD PRO A 347 -5.787 31.008 3.627 1.00112.24 C ANISOU 2343 CD PRO A 347 14952 17622 10071 -221 44 -148 C ATOM 2344 N ASP A 348 -4.038 34.808 5.947 1.00121.14 N ANISOU 2344 N ASP A 348 17122 18986 9921 13 -1392 -646 N ATOM 2345 CA ASP A 348 -3.022 35.857 5.924 1.00123.73 C ANISOU 2345 CA ASP A 348 17687 19165 10160 -176 -1976 -739 C ATOM 2346 C ASP A 348 -1.729 35.539 6.675 1.00125.51 C ANISOU 2346 C ASP A 348 17847 19486 10355 -227 -2147 -469 C ATOM 2347 O ASP A 348 -0.645 35.900 6.215 1.00126.23 O ANISOU 2347 O ASP A 348 17895 19480 10588 -560 -2464 -381 O ATOM 2348 CB ASP A 348 -3.604 37.184 6.427 1.00127.00 C ANISOU 2348 CB ASP A 348 18556 19516 10184 84 -2465 -1107 C ATOM 2349 CG ASP A 348 -4.983 37.024 7.037 1.00128.73 C ANISOU 2349 CG ASP A 348 18812 19993 10106 554 -2158 -1290 C ATOM 2350 OD1 ASP A 348 -5.310 35.910 7.497 1.00128.97 O ANISOU 2350 OD1 ASP A 348 18559 20311 10132 683 -1647 -1022 O ATOM 2351 OD2 ASP A 348 -5.740 38.017 7.057 1.00130.28 O ANISOU 2351 OD2 ASP A 348 19302 20128 10072 790 -2471 -1689 O ATOM 2352 N SER A 349 -1.840 34.877 7.823 1.00126.29 N ANISOU 2352 N SER A 349 17915 19816 10253 73 -1959 -305 N ATOM 2353 CA SER A 349 -0.680 34.662 8.689 1.00127.87 C ANISOU 2353 CA SER A 349 18114 20093 10379 67 -2179 -70 C ATOM 2354 C SER A 349 0.453 33.913 7.991 1.00126.50 C ANISOU 2354 C SER A 349 17577 19844 10643 -270 -2089 174 C ATOM 2355 O SER A 349 0.245 32.853 7.399 1.00125.97 O ANISOU 2355 O SER A 349 17175 19778 10911 -321 -1675 284 O ATOM 2356 CB SER A 349 -1.080 33.936 9.977 1.00129.27 C ANISOU 2356 CB SER A 349 18268 20575 10275 407 -1948 121 C ATOM 2357 OG SER A 349 0.030 33.803 10.849 1.00129.83 O ANISOU 2357 OG SER A 349 18379 20693 10257 405 -2207 333 O ATOM 2358 N PHE A 350 1.649 34.485 8.059 1.00125.73 N ANISOU 2358 N PHE A 350 17536 19701 10534 -477 -2526 242 N ATOM 2359 CA PHE A 350 2.831 33.874 7.469 1.00123.76 C ANISOU 2359 CA PHE A 350 16896 19501 10624 -755 -2488 447 C ATOM 2360 C PHE A 350 3.825 33.523 8.567 1.00127.49 C ANISOU 2360 C PHE A 350 17364 20053 11025 -666 -2680 687 C ATOM 2361 O PHE A 350 5.009 33.311 8.302 1.00129.52 O ANISOU 2361 O PHE A 350 17355 20384 11474 -877 -2816 844 O ATOM 2362 CB PHE A 350 3.478 34.828 6.468 1.00121.42 C ANISOU 2362 CB PHE A 350 16564 19181 10390 -1168 -2847 403 C ATOM 2363 CG PHE A 350 2.554 35.271 5.373 1.00119.12 C ANISOU 2363 CG PHE A 350 16306 18793 10160 -1302 -2732 182 C ATOM 2364 CD1 PHE A 350 1.733 34.359 4.730 1.00116.06 C ANISOU 2364 CD1 PHE A 350 15684 18415 9997 -1191 -2185 95 C ATOM 2365 CD2 PHE A 350 2.497 36.603 4.993 1.00119.79 C ANISOU 2365 CD2 PHE A 350 16679 18733 10103 -1553 -3242 75 C ATOM 2366 CE1 PHE A 350 0.879 34.764 3.721 1.00113.61 C ANISOU 2366 CE1 PHE A 350 15414 18003 9751 -1318 -2089 -105 C ATOM 2367 CE2 PHE A 350 1.643 37.016 3.986 1.00117.06 C ANISOU 2367 CE2 PHE A 350 16376 18273 9829 -1695 -3176 -118 C ATOM 2368 CZ PHE A 350 0.833 36.096 3.349 1.00113.90 C ANISOU 2368 CZ PHE A 350 15730 17914 9633 -1572 -2568 -215 C ATOM 2369 N LEU A 351 3.333 33.469 9.801 1.00127.27 N ANISOU 2369 N LEU A 351 17602 20067 10686 -346 -2692 717 N ATOM 2370 CA LEU A 351 4.174 33.165 10.954 1.00127.20 C ANISOU 2370 CA LEU A 351 17640 20129 10560 -244 -2894 950 C ATOM 2371 C LEU A 351 3.830 31.814 11.569 1.00125.39 C ANISOU 2371 C LEU A 351 17208 20009 10425 -54 -2506 1189 C ATOM 2372 O LEU A 351 4.449 31.390 12.544 1.00103.99 O ANISOU 2372 O LEU A 351 14510 17360 7643 24 -2638 1423 O ATOM 2373 CB LEU A 351 4.055 34.270 12.004 1.00129.47 C ANISOU 2373 CB LEU A 351 18419 20425 10348 -36 -3351 819 C ATOM 2374 CG LEU A 351 5.269 35.192 12.123 1.00131.36 C ANISOU 2374 CG LEU A 351 18831 20525 10556 -255 -3987 862 C ATOM 2375 CD1 LEU A 351 6.429 34.453 12.765 1.00133.15 C ANISOU 2375 CD1 LEU A 351 18861 20814 10914 -309 -4039 1188 C ATOM 2376 CD2 LEU A 351 5.669 35.728 10.758 1.00129.81 C ANISOU 2376 CD2 LEU A 351 18462 20216 10645 -683 -4135 825 C ATOM 2377 N ASP A 352 2.840 31.141 10.992 1.00122.68 N ANISOU 2377 N ASP A 352 16684 19666 10261 -12 -2082 1164 N ATOM 2378 CA ASP A 352 2.434 29.821 11.462 1.00122.89 C ANISOU 2378 CA ASP A 352 16502 19751 10441 94 -1791 1457 C ATOM 2379 C ASP A 352 3.474 28.753 11.134 1.00122.63 C ANISOU 2379 C ASP A 352 16118 19566 10908 -25 -1820 1636 C ATOM 2380 O ASP A 352 3.978 28.686 10.012 1.00121.42 O ANISOU 2380 O ASP A 352 15727 19314 11091 -164 -1799 1469 O ATOM 2381 CB ASP A 352 1.072 29.438 10.877 1.00121.84 C ANISOU 2381 CB ASP A 352 16274 19627 10394 141 -1404 1406 C ATOM 2382 CG ASP A 352 0.892 29.920 9.451 1.00119.74 C ANISOU 2382 CG ASP A 352 15943 19192 10362 -13 -1321 1085 C ATOM 2383 OD1 ASP A 352 1.904 30.055 8.732 1.00119.53 O ANISOU 2383 OD1 ASP A 352 15772 19067 10578 -197 -1474 997 O ATOM 2384 OD2 ASP A 352 -0.264 30.167 9.049 1.00119.11 O ANISOU 2384 OD2 ASP A 352 15930 19129 10199 42 -1107 938 O ATOM 2385 N ASP A 353 3.792 27.924 12.123 1.00124.62 N ANISOU 2385 N ASP A 353 16324 19843 11183 49 -1898 1964 N ATOM 2386 CA ASP A 353 4.757 26.844 11.943 1.00125.56 C ANISOU 2386 CA ASP A 353 16127 19791 11791 2 -2006 2113 C ATOM 2387 C ASP A 353 4.225 25.785 10.982 1.00127.27 C ANISOU 2387 C ASP A 353 16045 19814 12500 8 -1785 2081 C ATOM 2388 O ASP A 353 4.926 25.355 10.065 1.00128.62 O ANISOU 2388 O ASP A 353 15923 19870 13077 0 -1829 1897 O ATOM 2389 CB ASP A 353 5.116 26.210 13.290 1.00126.29 C ANISOU 2389 CB ASP A 353 16280 19913 11790 61 -2203 2503 C ATOM 2390 CG ASP A 353 5.998 27.107 14.140 1.00126.51 C ANISOU 2390 CG ASP A 353 16556 20064 11448 67 -2515 2508 C ATOM 2391 OD1 ASP A 353 6.005 28.334 13.907 1.00124.65 O ANISOU 2391 OD1 ASP A 353 16537 19909 10916 46 -2595 2246 O ATOM 2392 OD2 ASP A 353 6.685 26.584 15.042 1.00128.79 O ANISOU 2392 OD2 ASP A 353 16838 20331 11763 81 -2742 2785 O ATOM 2393 N HIS A 354 2.982 25.367 11.197 1.00127.45 N ANISOU 2393 N HIS A 354 16121 19840 12463 40 -1576 2258 N ATOM 2394 CA HIS A 354 2.329 24.414 10.308 1.00125.79 C ANISOU 2394 CA HIS A 354 15680 19397 12717 37 -1422 2250 C ATOM 2395 C HIS A 354 0.962 24.930 9.887 1.00120.85 C ANISOU 2395 C HIS A 354 15172 18873 11874 22 -1105 2146 C ATOM 2396 O HIS A 354 0.247 25.536 10.683 1.00119.71 O ANISOU 2396 O HIS A 354 15240 19010 11233 58 -1009 2261 O ATOM 2397 CB HIS A 354 2.189 23.046 10.981 1.00131.86 C ANISOU 2397 CB HIS A 354 16326 19989 13787 35 -1593 2705 C ATOM 2398 CG HIS A 354 3.479 22.299 11.115 1.00136.99 C ANISOU 2398 CG HIS A 354 16801 20423 14826 88 -1948 2737 C ATOM 2399 ND1 HIS A 354 4.513 22.734 11.918 1.00139.71 N ANISOU 2399 ND1 HIS A 354 17237 20908 14939 92 -2152 2791 N ATOM 2400 CD2 HIS A 354 3.905 21.145 10.550 1.00139.69 C ANISOU 2400 CD2 HIS A 354 16881 20412 15782 176 -2183 2690 C ATOM 2401 CE1 HIS A 354 5.517 21.881 11.841 1.00142.31 C ANISOU 2401 CE1 HIS A 354 17346 21006 15721 165 -2462 2791 C ATOM 2402 NE2 HIS A 354 5.174 20.906 11.017 1.00142.54 N ANISOU 2402 NE2 HIS A 354 17158 20736 16265 244 -2502 2703 N ATOM 2403 N HIS A 355 0.604 24.690 8.630 1.00118.53 N ANISOU 2403 N HIS A 355 14720 18382 11933 3 -958 1899 N ATOM 2404 CA HIS A 355 -0.699 25.097 8.120 1.00116.66 C ANISOU 2404 CA HIS A 355 14569 18190 11566 -19 -672 1794 C ATOM 2405 C HIS A 355 -1.429 23.912 7.498 1.00114.77 C ANISOU 2405 C HIS A 355 14124 17663 11819 -32 -604 1934 C ATOM 2406 O HIS A 355 -1.003 23.371 6.479 1.00112.54 O ANISOU 2406 O HIS A 355 13650 17117 11993 2 -671 1701 O ATOM 2407 CB HIS A 355 -0.552 26.230 7.101 1.00115.76 C ANISOU 2407 CB HIS A 355 14532 18111 11342 -74 -592 1332 C ATOM 2408 CG HIS A 355 -1.859 26.754 6.590 1.00115.91 C ANISOU 2408 CG HIS A 355 14668 18153 11220 -87 -342 1187 C ATOM 2409 ND1 HIS A 355 -2.911 27.065 7.423 1.00117.08 N ANISOU 2409 ND1 HIS A 355 14983 18527 10976 -3 -220 1348 N ATOM 2410 CD2 HIS A 355 -2.282 27.023 5.332 1.00114.82 C ANISOU 2410 CD2 HIS A 355 14481 17883 11262 -161 -199 887 C ATOM 2411 CE1 HIS A 355 -3.928 27.501 6.700 1.00115.79 C ANISOU 2411 CE1 HIS A 355 14869 18340 10787 -12 -20 1141 C ATOM 2412 NE2 HIS A 355 -3.572 27.485 5.429 1.00114.33 N ANISOU 2412 NE2 HIS A 355 14577 17902 10960 -126 -12 872 N ATOM 2413 N LEU A 356 -2.529 23.511 8.125 1.00116.70 N ANISOU 2413 N LEU A 356 14390 18002 11948 -72 -507 2323 N ATOM 2414 CA LEU A 356 -3.313 22.383 7.642 1.00 99.33 C ANISOU 2414 CA LEU A 356 12017 15504 10221 -135 -525 2557 C ATOM 2415 C LEU A 356 -4.566 22.843 6.904 1.00120.78 C ANISOU 2415 C LEU A 356 14769 18264 12858 -166 -214 2402 C ATOM 2416 O LEU A 356 -5.331 23.666 7.406 1.00 96.57 O ANISOU 2416 O LEU A 356 11829 15584 9279 -155 8 2434 O ATOM 2417 CB LEU A 356 -3.664 21.436 8.795 1.00103.81 C ANISOU 2417 CB LEU A 356 12510 16139 10793 -247 -712 3229 C ATOM 2418 CG LEU A 356 -4.205 22.032 10.099 1.00119.95 C ANISOU 2418 CG LEU A 356 14657 18780 12137 -278 -557 3567 C ATOM 2419 CD1 LEU A 356 -5.726 22.108 10.093 1.00120.74 C ANISOU 2419 CD1 LEU A 356 14689 19177 12010 -351 -276 3796 C ATOM 2420 CD2 LEU A 356 -3.714 21.229 11.294 1.00110.51 C ANISOU 2420 CD2 LEU A 356 13399 17662 10926 -382 -866 4131 C ATOM 2421 N THR A 357 -4.760 22.307 5.703 1.00119.44 N ANISOU 2421 N THR A 357 14483 17708 13192 -165 -228 2194 N ATOM 2422 CA THR A 357 -5.883 22.684 4.852 1.00116.44 C ANISOU 2422 CA THR A 357 14133 17293 12817 -202 36 2016 C ATOM 2423 C THR A 357 -6.064 21.663 3.733 1.00117.16 C ANISOU 2423 C THR A 357 14068 16887 13559 -190 -104 1928 C ATOM 2424 O THR A 357 -5.124 20.955 3.372 1.00119.57 O ANISOU 2424 O THR A 357 14256 16918 14258 -81 -382 1783 O ATOM 2425 CB THR A 357 -5.680 24.086 4.246 1.00111.11 C ANISOU 2425 CB THR A 357 13619 16794 11803 -170 233 1486 C ATOM 2426 OG1 THR A 357 -6.603 24.283 3.168 1.00108.27 O ANISOU 2426 OG1 THR A 357 13264 16280 11593 -211 422 1259 O ATOM 2427 CG2 THR A 357 -4.258 24.239 3.726 1.00109.79 C ANISOU 2427 CG2 THR A 357 13393 16554 11770 -130 69 1146 C ATOM 2428 N ARG A 358 -7.273 21.590 3.188 1.00114.64 N ANISOU 2428 N ARG A 358 13746 16464 13348 -265 55 1984 N ATOM 2429 CA ARG A 358 -7.589 20.615 2.151 1.00113.77 C ANISOU 2429 CA ARG A 358 13523 15848 13855 -242 -126 1915 C ATOM 2430 C ARG A 358 -7.373 21.184 0.752 1.00108.36 C ANISOU 2430 C ARG A 358 12857 15064 13249 -146 29 1272 C ATOM 2431 O ARG A 358 -8.121 22.053 0.309 1.00105.97 O ANISOU 2431 O ARG A 358 12660 14901 12702 -224 325 1098 O ATOM 2432 CB ARG A 358 -9.031 20.129 2.303 1.00117.79 C ANISOU 2432 CB ARG A 358 13994 16281 14482 -413 -92 2396 C ATOM 2433 CG ARG A 358 -9.462 19.121 1.253 1.00120.99 C ANISOU 2433 CG ARG A 358 14323 16098 15551 -398 -354 2356 C ATOM 2434 CD ARG A 358 -8.530 17.923 1.227 1.00127.68 C ANISOU 2434 CD ARG A 358 15080 16496 16936 -262 -896 2383 C ATOM 2435 NE ARG A 358 -9.001 16.888 0.313 1.00132.48 N ANISOU 2435 NE ARG A 358 15643 16492 18200 -206 -1267 2356 N ATOM 2436 CZ ARG A 358 -9.697 15.822 0.692 1.00139.33 C ANISOU 2436 CZ ARG A 358 16463 16996 19480 -389 -1694 2976 C ATOM 2437 NH1 ARG A 358 -10.001 15.645 1.971 1.00143.51 N ANISOU 2437 NH1 ARG A 358 16940 17801 19786 -665 -1753 3703 N ATOM 2438 NH2 ARG A 358 -10.087 14.930 -0.208 1.00141.81 N ANISOU 2438 NH2 ARG A 358 16774 16691 20417 -309 -2107 2893 N ATOM 2439 N PRO A 359 -6.347 20.687 0.046 1.00106.81 N ANISOU 2439 N PRO A 359 12534 14672 13377 33 -195 915 N ATOM 2440 CA PRO A 359 -6.020 21.186 -1.292 1.00103.01 C ANISOU 2440 CA PRO A 359 12002 14230 12908 115 -60 328 C ATOM 2441 C PRO A 359 -6.938 20.610 -2.362 1.00102.39 C ANISOU 2441 C PRO A 359 11903 13767 13235 154 -90 199 C ATOM 2442 O PRO A 359 -7.326 19.445 -2.283 1.00105.29 O ANISOU 2442 O PRO A 359 12224 13710 14071 224 -407 447 O ATOM 2443 CB PRO A 359 -4.596 20.676 -1.504 1.00 88.35 C ANISOU 2443 CB PRO A 359 9936 12406 11226 347 -325 45 C ATOM 2444 CG PRO A 359 -4.550 19.410 -0.729 1.00 92.38 C ANISOU 2444 CG PRO A 359 10404 12554 12142 446 -730 425 C ATOM 2445 CD PRO A 359 -5.417 19.631 0.482 1.00110.27 C ANISOU 2445 CD PRO A 359 12839 14902 14156 187 -615 1034 C ATOM 2446 N HIS A 360 -7.282 21.431 -3.348 1.00 82.44 N ANISOU 2446 N HIS A 360 9426 11359 10539 85 178 -160 N ATOM 2447 CA HIS A 360 -8.056 20.986 -4.498 1.00 81.77 C ANISOU 2447 CA HIS A 360 9328 10934 10807 134 156 -362 C ATOM 2448 C HIS A 360 -7.252 19.918 -5.231 1.00 84.63 C ANISOU 2448 C HIS A 360 9486 11072 11599 463 -197 -705 C ATOM 2449 O HIS A 360 -6.056 20.088 -5.462 1.00 87.90 O ANISOU 2449 O HIS A 360 9727 11811 11860 617 -226 -1043 O ATOM 2450 CB HIS A 360 -8.334 22.177 -5.415 1.00 81.00 C ANISOU 2450 CB HIS A 360 9311 11079 10388 -15 481 -716 C ATOM 2451 CG HIS A 360 -9.312 21.892 -6.510 1.00 81.53 C ANISOU 2451 CG HIS A 360 9413 10815 10751 -16 508 -877 C ATOM 2452 ND1 HIS A 360 -8.977 21.181 -7.642 1.00 84.17 N ANISOU 2452 ND1 HIS A 360 9600 10970 11411 215 325 -1274 N ATOM 2453 CD2 HIS A 360 -10.612 22.241 -6.655 1.00 80.57 C ANISOU 2453 CD2 HIS A 360 9450 10532 10632 -193 680 -722 C ATOM 2454 CE1 HIS A 360 -10.032 21.093 -8.431 1.00 83.49 C ANISOU 2454 CE1 HIS A 360 9610 10579 11531 157 372 -1334 C ATOM 2455 NE2 HIS A 360 -11.037 21.729 -7.857 1.00 81.30 N ANISOU 2455 NE2 HIS A 360 9512 10299 11078 -106 593 -987 N ATOM 2456 N PRO A 361 -7.903 18.804 -5.592 1.00 86.83 N ANISOU 2456 N PRO A 361 9767 10809 12414 591 -516 -626 N ATOM 2457 CA PRO A 361 -7.207 17.653 -6.175 1.00 90.66 C ANISOU 2457 CA PRO A 361 10086 10997 13365 994 -991 -974 C ATOM 2458 C PRO A 361 -6.525 17.977 -7.500 1.00 97.94 C ANISOU 2458 C PRO A 361 10825 12249 14139 1244 -870 -1694 C ATOM 2459 O PRO A 361 -5.540 17.333 -7.860 1.00 93.37 O ANISOU 2459 O PRO A 361 10021 11737 13718 1642 -1172 -2102 O ATOM 2460 CB PRO A 361 -8.336 16.642 -6.401 1.00 92.64 C ANISOU 2460 CB PRO A 361 10449 10563 14185 996 -1356 -713 C ATOM 2461 CG PRO A 361 -9.566 17.468 -6.501 1.00 88.74 C ANISOU 2461 CG PRO A 361 10116 10146 13456 637 -923 -467 C ATOM 2462 CD PRO A 361 -9.360 18.599 -5.546 1.00 86.20 C ANISOU 2462 CD PRO A 361 9839 10377 12537 381 -493 -233 C ATOM 2463 N GLU A 362 -7.042 18.973 -8.208 1.00 95.19 N ANISOU 2463 N GLU A 362 10546 12155 13465 1017 -454 -1845 N ATOM 2464 CA GLU A 362 -6.538 19.303 -9.533 1.00 97.75 C ANISOU 2464 CA GLU A 362 10679 12855 13607 1178 -331 -2454 C ATOM 2465 C GLU A 362 -5.426 20.351 -9.472 1.00 99.66 C ANISOU 2465 C GLU A 362 10736 13852 13278 1041 -56 -2595 C ATOM 2466 O GLU A 362 -5.040 20.922 -10.491 1.00100.62 O ANISOU 2466 O GLU A 362 10677 14455 13100 1017 122 -2971 O ATOM 2467 CB GLU A 362 -7.685 19.770 -10.432 1.00 94.52 C ANISOU 2467 CB GLU A 362 10437 12289 13188 972 -107 -2523 C ATOM 2468 CG GLU A 362 -7.485 19.478 -11.907 1.00 96.87 C ANISOU 2468 CG GLU A 362 10555 12708 13542 1259 -180 -3132 C ATOM 2469 CD GLU A 362 -8.777 19.554 -12.690 1.00 96.43 C ANISOU 2469 CD GLU A 362 10712 12256 13668 1114 -105 -3139 C ATOM 2470 OE1 GLU A 362 -9.820 19.117 -12.158 1.00 97.36 O ANISOU 2470 OE1 GLU A 362 11061 11781 14152 999 -234 -2719 O ATOM 2471 OE2 GLU A 362 -8.753 20.051 -13.836 1.00 96.05 O ANISOU 2471 OE2 GLU A 362 10580 12531 13384 1091 72 -3529 O ATOM 2472 N ARG A 363 -4.909 20.597 -8.273 1.00 99.86 N ANISOU 2472 N ARG A 363 10796 14001 13145 923 -56 -2253 N ATOM 2473 CA ARG A 363 -3.774 21.499 -8.115 1.00100.75 C ANISOU 2473 CA ARG A 363 10731 14776 12773 792 101 -2330 C ATOM 2474 C ARG A 363 -2.783 20.989 -7.075 1.00107.71 C ANISOU 2474 C ARG A 363 11494 15711 13721 972 -136 -2178 C ATOM 2475 O ARG A 363 -2.246 21.760 -6.283 1.00108.88 O ANISOU 2475 O ARG A 363 11681 16161 13526 746 -34 -1942 O ATOM 2476 CB ARG A 363 -4.236 22.917 -7.774 1.00 94.90 C ANISOU 2476 CB ARG A 363 10240 14220 11598 314 404 -2061 C ATOM 2477 CG ARG A 363 -5.036 23.033 -6.494 1.00 79.49 C ANISOU 2477 CG ARG A 363 8610 11920 9671 160 426 -1571 C ATOM 2478 CD ARG A 363 -5.677 24.403 -6.377 1.00 76.06 C ANISOU 2478 CD ARG A 363 8435 11622 8844 -204 664 -1452 C ATOM 2479 NE ARG A 363 -4.706 25.481 -6.512 1.00 85.43 N ANISOU 2479 NE ARG A 363 9544 13314 9601 -411 687 -1562 N ATOM 2480 CZ ARG A 363 -4.989 26.765 -6.316 1.00 84.32 C ANISOU 2480 CZ ARG A 363 9638 13297 9105 -720 749 -1476 C ATOM 2481 NH1 ARG A 363 -6.217 27.125 -5.973 1.00 81.84 N ANISOU 2481 NH1 ARG A 363 9622 12691 8780 -795 844 -1342 N ATOM 2482 NH2 ARG A 363 -4.046 27.687 -6.458 1.00 85.07 N ANISOU 2482 NH2 ARG A 363 9651 13814 8855 -949 663 -1519 N ATOM 2483 N VAL A 364 -2.538 19.684 -7.089 1.00113.43 N ANISOU 2483 N VAL A 364 12088 16100 14908 1392 -516 -2329 N ATOM 2484 CA VAL A 364 -1.571 19.077 -6.178 1.00119.28 C ANISOU 2484 CA VAL A 364 12703 16838 15780 1603 -820 -2227 C ATOM 2485 C VAL A 364 -0.155 18.925 -6.763 1.00126.10 C ANISOU 2485 C VAL A 364 13114 18291 16506 1957 -924 -2738 C ATOM 2486 O VAL A 364 0.821 19.245 -6.083 1.00129.12 O ANISOU 2486 O VAL A 364 13362 19033 16663 1907 -929 -2622 O ATOM 2487 CB VAL A 364 -2.085 17.733 -5.604 1.00121.72 C ANISOU 2487 CB VAL A 364 13155 16390 16703 1816 -1302 -1989 C ATOM 2488 CG1 VAL A 364 -1.011 17.059 -4.761 1.00101.83 C ANISOU 2488 CG1 VAL A 364 10490 13847 14352 2058 -1690 -1935 C ATOM 2489 CG2 VAL A 364 -3.345 17.961 -4.786 1.00119.18 C ANISOU 2489 CG2 VAL A 364 13190 15693 16400 1409 -1168 -1360 C ATOM 2490 N PRO A 365 -0.029 18.440 -8.017 1.00129.39 N ANISOU 2490 N PRO A 365 13269 18866 17029 2334 -1015 -3313 N ATOM 2491 CA PRO A 365 1.328 18.331 -8.570 1.00134.58 C ANISOU 2491 CA PRO A 365 13411 20258 17465 2702 -1082 -3814 C ATOM 2492 C PRO A 365 2.064 19.670 -8.661 1.00135.97 C ANISOU 2492 C PRO A 365 13371 21308 16983 2289 -674 -3704 C ATOM 2493 O PRO A 365 3.249 19.724 -8.331 1.00138.77 O ANISOU 2493 O PRO A 365 13398 22175 17153 2400 -748 -3758 O ATOM 2494 CB PRO A 365 1.087 17.763 -9.970 1.00135.75 C ANISOU 2494 CB PRO A 365 13353 20494 17731 3131 -1179 -4439 C ATOM 2495 CG PRO A 365 -0.183 17.012 -9.851 1.00133.94 C ANISOU 2495 CG PRO A 365 13548 19281 18063 3168 -1441 -4268 C ATOM 2496 CD PRO A 365 -1.024 17.825 -8.916 1.00128.87 C ANISOU 2496 CD PRO A 365 13321 18334 17308 2524 -1138 -3556 C ATOM 2497 N PHE A 366 1.382 20.725 -9.098 1.00135.33 N ANISOU 2497 N PHE A 366 13468 21370 16580 1807 -314 -3531 N ATOM 2498 CA PHE A 366 2.006 22.042 -9.179 1.00137.90 C ANISOU 2498 CA PHE A 366 13640 22431 16324 1338 -45 -3351 C ATOM 2499 C PHE A 366 2.349 22.535 -7.781 1.00140.42 C ANISOU 2499 C PHE A 366 14188 22603 16562 1056 -92 -2854 C ATOM 2500 O PHE A 366 3.333 23.248 -7.582 1.00142.35 O ANISOU 2500 O PHE A 366 14204 23445 16437 838 -65 -2732 O ATOM 2501 CB PHE A 366 1.080 23.054 -9.857 1.00133.61 C ANISOU 2501 CB PHE A 366 13328 21907 15532 864 237 -3239 C ATOM 2502 CG PHE A 366 0.095 22.440 -10.807 1.00133.25 C ANISOU 2502 CG PHE A 366 13369 21495 15764 1093 252 -3556 C ATOM 2503 CD1 PHE A 366 0.494 21.999 -12.057 1.00136.13 C ANISOU 2503 CD1 PHE A 366 13309 22377 16037 1437 240 -4091 C ATOM 2504 CD2 PHE A 366 -1.238 22.320 -10.454 1.00129.80 C ANISOU 2504 CD2 PHE A 366 13418 20251 15648 973 268 -3319 C ATOM 2505 CE1 PHE A 366 -0.416 21.439 -12.933 1.00135.92 C ANISOU 2505 CE1 PHE A 366 13394 21980 16271 1664 210 -4400 C ATOM 2506 CE2 PHE A 366 -2.153 21.763 -11.325 1.00129.40 C ANISOU 2506 CE2 PHE A 366 13458 19830 15879 1157 245 -3576 C ATOM 2507 CZ PHE A 366 -1.743 21.322 -12.567 1.00132.31 C ANISOU 2507 CZ PHE A 366 13453 20631 16188 1505 200 -4125 C ATOM 2508 N LEU A 367 1.522 22.144 -6.817 1.00141.22 N ANISOU 2508 N LEU A 367 14723 21942 16992 1052 -187 -2545 N ATOM 2509 CA LEU A 367 1.677 22.559 -5.429 1.00141.90 C ANISOU 2509 CA LEU A 367 15073 21856 16986 820 -236 -2075 C ATOM 2510 C LEU A 367 2.865 21.871 -4.759 1.00146.70 C ANISOU 2510 C LEU A 367 15423 22594 17722 1119 -514 -2096 C ATOM 2511 O LEU A 367 3.778 22.531 -4.265 1.00145.95 O ANISOU 2511 O LEU A 367 15218 22917 17318 935 -517 -1937 O ATOM 2512 CB LEU A 367 0.384 22.264 -4.659 1.00140.91 C ANISOU 2512 CB LEU A 367 15409 21007 17123 745 -242 -1731 C ATOM 2513 CG LEU A 367 0.213 22.642 -3.183 1.00141.39 C ANISOU 2513 CG LEU A 367 15793 20873 17056 533 -267 -1233 C ATOM 2514 CD1 LEU A 367 0.713 21.539 -2.252 1.00145.54 C ANISOU 2514 CD1 LEU A 367 16263 21125 17911 801 -593 -1065 C ATOM 2515 CD2 LEU A 367 0.893 23.968 -2.872 1.00141.08 C ANISOU 2515 CD2 LEU A 367 15784 21311 16511 211 -172 -1126 C ATOM 2516 N VAL A 368 2.849 20.542 -4.757 1.00152.20 N ANISOU 2516 N VAL A 368 16034 22893 18902 1579 -811 -2292 N ATOM 2517 CA VAL A 368 3.824 19.751 -4.010 1.00159.95 C ANISOU 2517 CA VAL A 368 16839 23825 20108 1893 -1167 -2294 C ATOM 2518 C VAL A 368 5.256 19.865 -4.547 1.00169.45 C ANISOU 2518 C VAL A 368 17485 25833 21064 2118 -1196 -2676 C ATOM 2519 O VAL A 368 6.210 19.463 -3.880 1.00174.24 O ANISOU 2519 O VAL A 368 17917 26523 21763 2316 -1454 -2655 O ATOM 2520 CB VAL A 368 3.407 18.261 -3.965 1.00160.21 C ANISOU 2520 CB VAL A 368 16932 23158 20780 2338 -1609 -2428 C ATOM 2521 CG1 VAL A 368 3.825 17.549 -5.244 1.00163.15 C ANISOU 2521 CG1 VAL A 368 16896 23773 21319 2884 -1785 -3131 C ATOM 2522 CG2 VAL A 368 3.996 17.570 -2.742 1.00162.66 C ANISOU 2522 CG2 VAL A 368 17292 23146 21364 2463 -2015 -2153 C ATOM 2523 N ALA A 369 5.407 20.423 -5.744 1.00172.89 N ANISOU 2523 N ALA A 369 17614 26913 21163 2067 -939 -2996 N ATOM 2524 CA ALA A 369 6.720 20.525 -6.373 1.00179.03 C ANISOU 2524 CA ALA A 369 17762 28628 21635 2272 -938 -3346 C ATOM 2525 C ALA A 369 7.379 21.884 -6.147 1.00180.30 C ANISOU 2525 C ALA A 369 17814 29448 21242 1701 -719 -2971 C ATOM 2526 O ALA A 369 8.590 21.969 -5.946 1.00184.14 O ANISOU 2526 O ALA A 369 17887 30536 21541 1765 -818 -2983 O ATOM 2527 CB ALA A 369 6.620 20.223 -7.863 1.00180.32 C ANISOU 2527 CB ALA A 369 17546 29260 21708 2596 -844 -3927 C ATOM 2528 N GLU A 370 6.578 22.944 -6.180 1.00177.40 N ANISOU 2528 N GLU A 370 17820 28946 20637 1146 -484 -2637 N ATOM 2529 CA GLU A 370 7.101 24.302 -6.048 1.00178.00 C ANISOU 2529 CA GLU A 370 17854 29557 20223 562 -390 -2270 C ATOM 2530 C GLU A 370 7.077 24.823 -4.611 1.00177.07 C ANISOU 2530 C GLU A 370 18202 28966 20108 277 -521 -1774 C ATOM 2531 O GLU A 370 7.734 25.816 -4.296 1.00178.84 O ANISOU 2531 O GLU A 370 18388 29571 19991 -130 -586 -1469 O ATOM 2532 CB GLU A 370 6.338 25.264 -6.968 1.00174.30 C ANISOU 2532 CB GLU A 370 17509 29251 19466 116 -166 -2220 C ATOM 2533 CG GLU A 370 6.941 25.434 -8.360 1.00175.89 C ANISOU 2533 CG GLU A 370 17080 30434 19316 96 -43 -2509 C ATOM 2534 CD GLU A 370 6.645 24.270 -9.291 1.00175.46 C ANISOU 2534 CD GLU A 370 16765 30402 19498 707 13 -3104 C ATOM 2535 OE1 GLU A 370 5.961 23.315 -8.866 1.00173.55 O ANISOU 2535 OE1 GLU A 370 16853 29335 19752 1111 -96 -3257 O ATOM 2536 OE2 GLU A 370 7.095 24.314 -10.456 1.00177.53 O ANISOU 2536 OE2 GLU A 370 16483 31536 19436 777 126 -3405 O ATOM 2537 N THR A 371 6.325 24.155 -3.742 1.00174.32 N ANISOU 2537 N THR A 371 18281 27823 20128 480 -598 -1673 N ATOM 2538 CA THR A 371 6.185 24.608 -2.356 1.00170.58 C ANISOU 2538 CA THR A 371 18258 26947 19608 254 -705 -1226 C ATOM 2539 C THR A 371 6.858 23.808 -1.212 1.00171.16 C ANISOU 2539 C THR A 371 18324 26788 19923 526 -971 -1090 C ATOM 2540 O THR A 371 6.880 24.297 -0.081 1.00168.16 O ANISOU 2540 O THR A 371 18275 26207 19410 319 -1062 -719 O ATOM 2541 CB THR A 371 4.691 24.801 -1.986 1.00154.92 C ANISOU 2541 CB THR A 371 16831 24330 17702 120 -574 -1045 C ATOM 2542 OG1 THR A 371 4.554 25.915 -1.095 1.00152.81 O ANISOU 2542 OG1 THR A 371 16944 24003 17113 -236 -608 -695 O ATOM 2543 CG2 THR A 371 4.128 23.547 -1.324 1.00155.87 C ANISOU 2543 CG2 THR A 371 17112 23842 18269 461 -691 -985 C ATOM 2544 N PRO A 372 7.414 22.602 -1.480 1.00175.31 N ANISOU 2544 N PRO A 372 18486 27334 20792 1005 -1147 -1404 N ATOM 2545 CA PRO A 372 7.775 21.815 -0.292 1.00177.81 C ANISOU 2545 CA PRO A 372 18922 27236 21403 1217 -1454 -1209 C ATOM 2546 C PRO A 372 8.913 22.421 0.529 1.00178.08 C ANISOU 2546 C PRO A 372 18870 27615 21176 1032 -1583 -952 C ATOM 2547 O PRO A 372 8.904 22.317 1.756 1.00177.57 O ANISOU 2547 O PRO A 372 19122 27169 21178 971 -1753 -603 O ATOM 2548 CB PRO A 372 8.207 20.474 -0.886 1.00182.77 C ANISOU 2548 CB PRO A 372 19154 27831 22459 1797 -1708 -1676 C ATOM 2549 CG PRO A 372 8.760 20.826 -2.207 1.00184.30 C ANISOU 2549 CG PRO A 372 18835 28812 22379 1882 -1521 -2107 C ATOM 2550 CD PRO A 372 7.928 21.971 -2.712 1.00179.38 C ANISOU 2550 CD PRO A 372 18450 28311 21394 1391 -1154 -1939 C ATOM 2551 N ARG A 373 9.873 23.049 -0.143 1.00178.65 N ANISOU 2551 N ARG A 373 18504 28437 20938 920 -1522 -1089 N ATOM 2552 CA ARG A 373 10.966 23.735 0.536 1.00178.80 C ANISOU 2552 CA ARG A 373 18418 28824 20694 679 -1672 -806 C ATOM 2553 C ARG A 373 11.344 25.014 -0.203 1.00179.33 C ANISOU 2553 C ARG A 373 18269 29585 20284 217 -1536 -712 C ATOM 2554 O ARG A 373 12.514 25.249 -0.502 1.00182.90 O ANISOU 2554 O ARG A 373 18207 30746 20540 159 -1625 -718 O ATOM 2555 CB ARG A 373 12.182 22.816 0.681 1.00181.32 C ANISOU 2555 CB ARG A 373 18248 29409 21238 1103 -1934 -1018 C ATOM 2556 CG ARG A 373 12.066 21.811 1.818 1.00180.61 C ANISOU 2556 CG ARG A 373 18453 28593 21577 1388 -2230 -900 C ATOM 2557 CD ARG A 373 11.896 22.521 3.154 1.00177.41 C ANISOU 2557 CD ARG A 373 18575 27840 20991 1001 -2296 -354 C ATOM 2558 NE ARG A 373 11.587 21.594 4.240 1.00177.92 N ANISOU 2558 NE ARG A 373 18955 27234 21412 1192 -2552 -157 N ATOM 2559 CZ ARG A 373 11.421 21.958 5.507 1.00176.55 C ANISOU 2559 CZ ARG A 373 19220 26758 21103 956 -2648 293 C ATOM 2560 NH1 ARG A 373 11.537 23.232 5.854 1.00174.47 N ANISOU 2560 NH1 ARG A 373 19168 26734 20387 576 -2551 534 N ATOM 2561 NH2 ARG A 373 11.140 21.047 6.429 1.00177.83 N ANISOU 2561 NH2 ARG A 373 19608 26388 21571 1099 -2896 509 N ATOM 2562 N ALA A 374 10.340 25.837 -0.493 1.00175.36 N ANISOU 2562 N ALA A 374 18143 28888 19598 -129 -1363 -597 N ATOM 2563 CA ALA A 374 10.553 27.097 -1.195 1.00174.53 C ANISOU 2563 CA ALA A 374 17911 29328 19074 -640 -1326 -448 C ATOM 2564 C ALA A 374 9.566 28.161 -0.727 1.00170.37 C ANISOU 2564 C ALA A 374 18043 28307 18384 -1035 -1352 -171 C ATOM 2565 O ALA A 374 8.871 28.775 -1.536 1.00168.21 O ANISOU 2565 O ALA A 374 17862 28084 17967 -1290 -1225 -222 O ATOM 2566 CB ALA A 374 10.443 26.892 -2.697 1.00174.86 C ANISOU 2566 CB ALA A 374 17484 29914 19040 -568 -1091 -802 C ATOM 2567 N ALA A 394 7.230 34.794 -10.863 1.00 96.89 N ANISOU 2567 N ALA A 394 14323 13216 9276 4836 2470 -802 N ATOM 2568 CA ALA A 394 7.214 35.871 -11.847 1.00 94.54 C ANISOU 2568 CA ALA A 394 13459 13214 9246 4394 2457 -914 C ATOM 2569 C ALA A 394 6.108 36.879 -11.554 1.00 94.83 C ANISOU 2569 C ALA A 394 13566 13047 9420 3877 2566 -928 C ATOM 2570 O ALA A 394 4.975 36.501 -11.252 1.00 95.84 O ANISOU 2570 O ALA A 394 14112 12720 9581 3761 2833 -863 O ATOM 2571 CB ALA A 394 7.056 35.307 -13.250 1.00 91.33 C ANISOU 2571 CB ALA A 394 12949 12749 9003 4385 2663 -975 C ATOM 2572 N LYS A 395 6.442 38.163 -11.640 1.00 93.86 N ANISOU 2572 N LYS A 395 13017 13246 9399 3572 2366 -997 N ATOM 2573 CA LYS A 395 5.460 39.219 -11.434 1.00 91.48 C ANISOU 2573 CA LYS A 395 12762 12758 9240 3130 2454 -1030 C ATOM 2574 C LYS A 395 4.881 39.695 -12.755 1.00 87.28 C ANISOU 2574 C LYS A 395 11918 12215 9031 2745 2604 -1060 C ATOM 2575 O LYS A 395 5.529 39.610 -13.798 1.00 85.84 O ANISOU 2575 O LYS A 395 11378 12312 8925 2758 2559 -1076 O ATOM 2576 CB LYS A 395 6.067 40.407 -10.686 1.00 94.75 C ANISOU 2576 CB LYS A 395 13009 13423 9571 3003 2110 -1103 C ATOM 2577 CG LYS A 395 6.238 40.195 -9.195 1.00 99.72 C ANISOU 2577 CG LYS A 395 14104 13958 9829 3304 1957 -1095 C ATOM 2578 CD LYS A 395 6.216 41.526 -8.457 1.00102.53 C ANISOU 2578 CD LYS A 395 14495 14340 10121 3055 1709 -1218 C ATOM 2579 CE LYS A 395 7.184 42.527 -9.075 1.00104.37 C ANISOU 2579 CE LYS A 395 14107 14966 10583 2762 1333 -1300 C ATOM 2580 NZ LYS A 395 7.111 43.858 -8.406 1.00105.98 N ANISOU 2580 NZ LYS A 395 14410 15102 10758 2476 1059 -1446 N ATOM 2581 N TRP A 396 3.657 40.202 -12.696 1.00 86.49 N ANISOU 2581 N TRP A 396 11958 11804 9099 2437 2792 -1054 N ATOM 2582 CA TRP A 396 2.993 40.735 -13.874 1.00 85.13 C ANISOU 2582 CA TRP A 396 11526 11594 9227 2076 2883 -1069 C ATOM 2583 C TRP A 396 3.072 42.257 -13.903 1.00 84.09 C ANISOU 2583 C TRP A 396 11113 11614 9223 1751 2717 -1108 C ATOM 2584 O TRP A 396 2.619 42.933 -12.983 1.00 82.02 O ANISOU 2584 O TRP A 396 11036 11190 8940 1679 2714 -1136 O ATOM 2585 CB TRP A 396 1.537 40.272 -13.918 1.00 84.40 C ANISOU 2585 CB TRP A 396 11697 11054 9317 1945 3172 -1015 C ATOM 2586 CG TRP A 396 1.387 38.831 -14.277 1.00 82.82 C ANISOU 2586 CG TRP A 396 11739 10642 9087 2141 3301 -983 C ATOM 2587 CD1 TRP A 396 1.356 37.771 -13.421 1.00 85.09 C ANISOU 2587 CD1 TRP A 396 12441 10686 9203 2428 3424 -905 C ATOM 2588 CD2 TRP A 396 1.248 38.289 -15.592 1.00 80.17 C ANISOU 2588 CD2 TRP A 396 11320 10271 8872 2073 3299 -1033 C ATOM 2589 NE1 TRP A 396 1.205 36.601 -14.122 1.00 70.68 N ANISOU 2589 NE1 TRP A 396 10790 8638 7428 2523 3491 -909 N ATOM 2590 CE2 TRP A 396 1.136 36.893 -15.459 1.00 69.11 C ANISOU 2590 CE2 TRP A 396 10301 8565 7392 2315 3404 -1010 C ATOM 2591 CE3 TRP A 396 1.205 38.850 -16.872 1.00 76.53 C ANISOU 2591 CE3 TRP A 396 10553 9982 8543 1841 3208 -1093 C ATOM 2592 CZ2 TRP A 396 0.986 36.051 -16.553 1.00 69.90 C ANISOU 2592 CZ2 TRP A 396 10504 8509 7544 2331 3393 -1090 C ATOM 2593 CZ3 TRP A 396 1.058 38.012 -17.956 1.00 75.38 C ANISOU 2593 CZ3 TRP A 396 10512 9726 8401 1880 3210 -1161 C ATOM 2594 CH2 TRP A 396 0.948 36.629 -17.791 1.00 76.87 C ANISOU 2594 CH2 TRP A 396 11101 9592 8515 2121 3289 -1181 C ATOM 2595 N HIS A 397 3.658 42.787 -14.969 1.00 86.99 N ANISOU 2595 N HIS A 397 11075 12272 9705 1571 2597 -1104 N ATOM 2596 CA HIS A 397 3.825 44.224 -15.112 1.00 90.32 C ANISOU 2596 CA HIS A 397 11234 12807 10276 1230 2422 -1109 C ATOM 2597 C HIS A 397 2.585 44.834 -15.741 1.00 87.25 C ANISOU 2597 C HIS A 397 10868 12144 10141 938 2561 -1081 C ATOM 2598 O HIS A 397 1.833 44.156 -16.437 1.00 86.69 O ANISOU 2598 O HIS A 397 10865 11921 10152 950 2736 -1052 O ATOM 2599 CB HIS A 397 5.036 44.537 -15.993 1.00 96.75 C ANISOU 2599 CB HIS A 397 11579 14067 11115 1146 2272 -1052 C ATOM 2600 CG HIS A 397 6.211 43.640 -15.750 1.00103.99 C ANISOU 2600 CG HIS A 397 12370 15307 11833 1513 2194 -1049 C ATOM 2601 ND1 HIS A 397 6.502 43.109 -14.513 1.00107.05 N ANISOU 2601 ND1 HIS A 397 13010 15645 12019 1817 2075 -1101 N ATOM 2602 CD2 HIS A 397 7.165 43.178 -16.594 1.00107.11 C ANISOU 2602 CD2 HIS A 397 12420 16089 12188 1674 2231 -986 C ATOM 2603 CE1 HIS A 397 7.587 42.359 -14.603 1.00110.58 C ANISOU 2603 CE1 HIS A 397 13248 16425 12343 2152 2001 -1071 C ATOM 2604 NE2 HIS A 397 8.009 42.385 -15.854 1.00110.81 N ANISOU 2604 NE2 HIS A 397 12895 16731 12478 2083 2117 -1006 N ATOM 2605 N LEU A 398 2.377 46.120 -15.494 1.00 86.09 N ANISOU 2605 N LEU A 398 10673 11912 10126 686 2442 -1098 N ATOM 2606 CA LEU A 398 1.313 46.859 -16.151 1.00 81.50 C ANISOU 2606 CA LEU A 398 10056 11103 9807 435 2522 -1051 C ATOM 2607 C LEU A 398 1.892 47.631 -17.326 1.00 78.69 C ANISOU 2607 C LEU A 398 9365 10976 9558 163 2376 -955 C ATOM 2608 O LEU A 398 2.627 48.600 -17.135 1.00 77.95 O ANISOU 2608 O LEU A 398 9131 10992 9494 -24 2172 -945 O ATOM 2609 CB LEU A 398 0.654 47.825 -15.172 1.00 81.80 C ANISOU 2609 CB LEU A 398 10312 10848 9920 382 2516 -1122 C ATOM 2610 CG LEU A 398 -0.283 48.843 -15.817 1.00 81.00 C ANISOU 2610 CG LEU A 398 10131 10530 10117 149 2534 -1066 C ATOM 2611 CD1 LEU A 398 -1.573 48.178 -16.270 1.00 79.59 C ANISOU 2611 CD1 LEU A 398 9959 10159 10122 203 2779 -1000 C ATOM 2612 CD2 LEU A 398 -0.553 49.992 -14.866 1.00 83.10 C ANISOU 2612 CD2 LEU A 398 10616 10546 10414 127 2466 -1167 C ATOM 2613 N GLY A 399 1.562 47.199 -18.539 1.00 78.45 N ANISOU 2613 N GLY A 399 9236 11001 9571 127 2472 -876 N ATOM 2614 CA GLY A 399 2.088 47.826 -19.738 1.00 81.44 C ANISOU 2614 CA GLY A 399 9350 11614 9979 -94 2397 -744 C ATOM 2615 C GLY A 399 3.603 47.801 -19.744 1.00 86.29 C ANISOU 2615 C GLY A 399 9686 12650 10451 -68 2324 -699 C ATOM 2616 O GLY A 399 4.213 46.795 -19.382 1.00 89.15 O ANISOU 2616 O GLY A 399 10046 13192 10634 226 2373 -766 O ATOM 2617 N ILE A 400 4.216 48.908 -20.151 1.00 87.34 N ANISOU 2617 N ILE A 400 9562 12932 10692 -377 2205 -563 N ATOM 2618 CA ILE A 400 5.668 49.032 -20.095 1.00 90.24 C ANISOU 2618 CA ILE A 400 9555 13717 11016 -423 2119 -484 C ATOM 2619 C ILE A 400 6.086 50.368 -19.489 1.00 91.62 C ANISOU 2619 C ILE A 400 9613 13800 11397 -793 1844 -451 C ATOM 2620 O ILE A 400 5.341 51.346 -19.549 1.00 90.61 O ANISOU 2620 O ILE A 400 9666 13324 11436 -1044 1772 -429 O ATOM 2621 CB ILE A 400 6.315 48.877 -21.484 1.00 91.72 C ANISOU 2621 CB ILE A 400 9439 14295 11116 -453 2305 -284 C ATOM 2622 CG1 ILE A 400 5.770 49.930 -22.448 1.00 91.76 C ANISOU 2622 CG1 ILE A 400 9471 14150 11243 -809 2318 -98 C ATOM 2623 CG2 ILE A 400 6.082 47.477 -22.030 1.00 90.33 C ANISOU 2623 CG2 ILE A 400 9430 14205 10688 -42 2531 -370 C ATOM 2624 CD1 ILE A 400 6.397 49.871 -23.820 1.00 94.49 C ANISOU 2624 CD1 ILE A 400 9580 14883 11437 -840 2537 134 C ATOM 2625 N ARG A 401 7.280 50.401 -18.904 1.00 94.32 N ANISOU 2625 N ARG A 401 9659 14435 11743 -817 1656 -455 N ATOM 2626 CA ARG A 401 7.797 51.618 -18.287 1.00 96.61 C ANISOU 2626 CA ARG A 401 9841 14627 12240 -1206 1313 -451 C ATOM 2627 C ARG A 401 9.209 51.955 -18.759 1.00 98.54 C ANISOU 2627 C ARG A 401 9468 15340 12631 -1473 1223 -233 C ATOM 2628 O ARG A 401 9.988 51.068 -19.107 1.00 98.84 O ANISOU 2628 O ARG A 401 9150 15843 12560 -1216 1379 -155 O ATOM 2629 CB ARG A 401 7.759 51.509 -16.761 1.00 98.59 C ANISOU 2629 CB ARG A 401 10397 14678 12385 -1032 1038 -716 C ATOM 2630 CG ARG A 401 8.202 50.165 -16.224 1.00100.73 C ANISOU 2630 CG ARG A 401 10648 15222 12403 -560 1084 -808 C ATOM 2631 CD ARG A 401 7.260 49.682 -15.134 1.00100.50 C ANISOU 2631 CD ARG A 401 11203 14823 12161 -241 1115 -1026 C ATOM 2632 NE ARG A 401 7.370 50.468 -13.909 1.00103.32 N ANISOU 2632 NE ARG A 401 11823 14953 12480 -349 750 -1202 N ATOM 2633 CZ ARG A 401 6.527 50.376 -12.883 1.00102.70 C ANISOU 2633 CZ ARG A 401 12303 14517 12203 -123 785 -1384 C ATOM 2634 NH1 ARG A 401 5.500 49.538 -12.937 1.00 98.80 N ANISOU 2634 NH1 ARG A 401 12087 13851 11601 170 1174 -1377 N ATOM 2635 NH2 ARG A 401 6.707 51.126 -11.805 1.00106.44 N ANISOU 2635 NH2 ARG A 401 13067 14793 12581 -197 433 -1569 N ATOM 2636 N SER A 402 9.522 53.248 -18.773 1.00100.51 N ANISOU 2636 N SER A 402 9589 15448 13153 -1985 984 -122 N ATOM 2637 CA SER A 402 10.851 53.725 -19.142 1.00106.17 C ANISOU 2637 CA SER A 402 9667 16572 14101 -2350 875 126 C ATOM 2638 C SER A 402 11.269 54.882 -18.239 1.00111.31 C ANISOU 2638 C SER A 402 10320 16950 15023 -2817 356 45 C ATOM 2639 O SER A 402 10.516 55.294 -17.357 1.00110.19 O ANISOU 2639 O SER A 402 10735 16305 14828 -2794 116 -224 O ATOM 2640 CB SER A 402 10.879 54.170 -20.606 1.00105.89 C ANISOU 2640 CB SER A 402 9405 16675 14155 -2616 1218 487 C ATOM 2641 OG SER A 402 12.163 54.651 -20.969 1.00110.93 O ANISOU 2641 OG SER A 402 9376 17722 15050 -3002 1181 781 O ATOM 2642 N GLN A 403 12.471 55.403 -18.464 1.00116.91 N ANISOU 2642 N GLN A 403 10410 17984 16026 -3242 187 276 N ATOM 2643 CA GLN A 403 12.965 56.534 -17.690 1.00122.05 C ANISOU 2643 CA GLN A 403 11033 18358 16983 -3773 -372 208 C ATOM 2644 C GLN A 403 13.331 57.701 -18.604 1.00124.50 C ANISOU 2644 C GLN A 403 11041 18588 17677 -4443 -332 585 C ATOM 2645 O GLN A 403 13.973 58.661 -18.178 1.00128.72 O ANISOU 2645 O GLN A 403 11400 18951 18557 -5002 -786 617 O ATOM 2646 CB GLN A 403 14.168 56.116 -16.845 1.00129.63 C ANISOU 2646 CB GLN A 403 11496 19742 18016 -3736 -778 118 C ATOM 2647 CG GLN A 403 13.887 54.956 -15.901 1.00129.28 C ANISOU 2647 CG GLN A 403 11785 19768 17568 -3064 -839 -210 C ATOM 2648 CD GLN A 403 15.114 54.524 -15.120 1.00137.63 C ANISOU 2648 CD GLN A 403 12331 21277 18686 -2981 -1278 -266 C ATOM 2649 OE1 GLN A 403 16.045 55.304 -14.924 1.00146.01 O ANISOU 2649 OE1 GLN A 403 12917 22446 20114 -3504 -1723 -173 O ATOM 2650 NE2 GLN A 403 15.123 53.272 -14.676 1.00136.05 N ANISOU 2650 NE2 GLN A 403 12216 21327 18147 -2329 -1183 -402 N ATOM 2651 N SER A 404 12.911 57.609 -19.862 1.00122.33 N ANISOU 2651 N SER A 404 10746 18409 17324 -4396 192 875 N ATOM 2652 CA SER A 404 13.195 58.644 -20.850 1.00126.57 C ANISOU 2652 CA SER A 404 11054 18879 18157 -4982 323 1302 C ATOM 2653 C SER A 404 12.327 59.875 -20.622 1.00125.80 C ANISOU 2653 C SER A 404 11605 17985 18207 -5323 50 1221 C ATOM 2654 O SER A 404 11.362 59.831 -19.861 1.00121.70 O ANISOU 2654 O SER A 404 11714 17014 17510 -5013 -119 844 O ATOM 2655 CB SER A 404 12.957 58.105 -22.262 1.00125.45 C ANISOU 2655 CB SER A 404 10802 19085 17777 -4739 963 1619 C ATOM 2656 OG SER A 404 13.624 56.870 -22.460 1.00126.42 O ANISOU 2656 OG SER A 404 10451 19885 17699 -4292 1254 1631 O ATOM 2657 N ARG A 405 12.677 60.974 -21.285 1.00130.88 N ANISOU 2657 N ARG A 405 12098 18448 19181 -5942 36 1598 N ATOM 2658 CA ARG A 405 11.861 62.183 -21.249 1.00132.12 C ANISOU 2658 CA ARG A 405 12891 17817 19490 -6244 -180 1583 C ATOM 2659 C ARG A 405 10.505 61.898 -21.887 1.00126.57 C ANISOU 2659 C ARG A 405 12730 16898 18462 -5764 184 1560 C ATOM 2660 O ARG A 405 10.439 61.304 -22.963 1.00125.71 O ANISOU 2660 O ARG A 405 12421 17202 18143 -5558 650 1831 O ATOM 2661 CB ARG A 405 12.566 63.330 -21.975 1.00139.34 C ANISOU 2661 CB ARG A 405 13513 18606 20824 -7012 -207 2078 C ATOM 2662 CG ARG A 405 13.115 64.413 -21.056 1.00145.21 C ANISOU 2662 CG ARG A 405 14316 18853 22003 -7637 -856 1951 C ATOM 2663 CD ARG A 405 13.982 63.828 -19.953 1.00147.02 C ANISOU 2663 CD ARG A 405 14133 19451 22279 -7587 -1259 1628 C ATOM 2664 NE ARG A 405 14.644 64.867 -19.171 1.00154.72 N ANISOU 2664 NE ARG A 405 15101 19994 23691 -8266 -1940 1532 N ATOM 2665 CZ ARG A 405 15.890 65.282 -19.382 1.00162.60 C ANISOU 2665 CZ ARG A 405 15369 21266 25144 -8893 -2096 1855 C ATOM 2666 NH1 ARG A 405 16.615 64.743 -20.352 1.00164.04 N ANISOU 2666 NH1 ARG A 405 14827 22158 25345 -8777 -1522 2257 N ATOM 2667 NH2 ARG A 405 16.413 66.235 -18.622 1.00169.51 N ANISOU 2667 NH2 ARG A 405 16396 21659 26353 -9342 -2712 1645 N ATOM 2668 N PRO A 406 9.420 62.328 -21.222 1.00123.61 N ANISOU 2668 N PRO A 406 13042 15881 18045 -5570 -42 1232 N ATOM 2669 CA PRO A 406 8.040 61.972 -21.579 1.00117.43 C ANISOU 2669 CA PRO A 406 12731 14891 16997 -5055 224 1133 C ATOM 2670 C PRO A 406 7.678 62.275 -23.031 1.00119.06 C ANISOU 2670 C PRO A 406 12948 15117 17173 -5149 553 1579 C ATOM 2671 O PRO A 406 7.079 61.431 -23.695 1.00115.85 O ANISOU 2671 O PRO A 406 12565 14981 16473 -4728 878 1607 O ATOM 2672 CB PRO A 406 7.196 62.827 -20.626 1.00116.80 C ANISOU 2672 CB PRO A 406 13302 14052 17024 -5014 -122 803 C ATOM 2673 CG PRO A 406 8.102 63.920 -20.176 1.00123.83 C ANISOU 2673 CG PRO A 406 14150 14637 18261 -5640 -556 847 C ATOM 2674 CD PRO A 406 9.461 63.307 -20.123 1.00126.75 C ANISOU 2674 CD PRO A 406 13808 15673 18679 -5868 -583 955 C ATOM 2675 N ASN A 407 8.040 63.456 -23.517 1.00124.88 N ANISOU 2675 N ASN A 407 13706 15549 18195 -5702 444 1929 N ATOM 2676 CA ASN A 407 7.720 63.829 -24.888 1.00126.27 C ANISOU 2676 CA ASN A 407 13963 15711 18304 -5798 737 2396 C ATOM 2677 C ASN A 407 8.641 63.147 -25.894 1.00127.08 C ANISOU 2677 C ASN A 407 13485 16571 18228 -5867 1163 2774 C ATOM 2678 O ASN A 407 8.300 63.011 -27.070 1.00125.95 O ANISOU 2678 O ASN A 407 13429 16592 17834 -5737 1492 3089 O ATOM 2679 CB ASN A 407 7.754 65.347 -25.060 1.00133.50 C ANISOU 2679 CB ASN A 407 15176 15974 19576 -6354 492 2679 C ATOM 2680 CG ASN A 407 6.572 65.867 -25.855 1.00133.68 C ANISOU 2680 CG ASN A 407 15737 15555 19500 -6145 571 2867 C ATOM 2681 OD1 ASN A 407 6.702 66.215 -27.028 1.00137.54 O ANISOU 2681 OD1 ASN A 407 16205 16128 19927 -6349 800 3370 O ATOM 2682 ND2 ASN A 407 5.407 65.912 -25.218 1.00129.75 N ANISOU 2682 ND2 ASN A 407 15716 14606 18976 -5707 390 2480 N ATOM 2683 N ASP A 408 9.810 62.718 -25.424 1.00129.60 N ANISOU 2683 N ASP A 408 13224 17361 18659 -6036 1148 2736 N ATOM 2684 CA ASP A 408 10.735 61.954 -26.253 1.00132.09 C ANISOU 2684 CA ASP A 408 12930 18456 18802 -5994 1596 3044 C ATOM 2685 C ASP A 408 10.237 60.523 -26.420 1.00127.23 C ANISOU 2685 C ASP A 408 12371 18248 17724 -5269 1870 2770 C ATOM 2686 O ASP A 408 10.561 59.853 -27.400 1.00128.66 O ANISOU 2686 O ASP A 408 12317 18960 17609 -5060 2313 3004 O ATOM 2687 CB ASP A 408 12.141 61.956 -25.651 1.00136.10 C ANISOU 2687 CB ASP A 408 12729 19345 19638 -6374 1457 3094 C ATOM 2688 CG ASP A 408 12.833 63.295 -25.793 1.00143.84 C ANISOU 2688 CG ASP A 408 13518 20034 21101 -7193 1277 3498 C ATOM 2689 OD1 ASP A 408 12.462 64.065 -26.705 1.00145.70 O ANISOU 2689 OD1 ASP A 408 14089 19947 21325 -7375 1457 3848 O ATOM 2690 OD2 ASP A 408 13.754 63.575 -24.996 1.00148.48 O ANISOU 2690 OD2 ASP A 408 13707 20651 22057 -7540 928 3394 O ATOM 2691 N ILE A 409 9.451 60.062 -25.453 1.00121.68 N ANISOU 2691 N ILE A 409 12015 17270 16949 -4887 1617 2276 N ATOM 2692 CA ILE A 409 8.842 58.741 -25.530 1.00115.26 C ANISOU 2692 CA ILE A 409 11333 16712 15749 -4244 1826 2004 C ATOM 2693 C ILE A 409 7.757 58.729 -26.597 1.00113.52 C ANISOU 2693 C ILE A 409 11539 16320 15272 -4033 2020 2137 C ATOM 2694 O ILE A 409 7.757 57.877 -27.485 1.00112.82 O ANISOU 2694 O ILE A 409 11396 16636 14833 -3727 2349 2224 O ATOM 2695 CB ILE A 409 8.227 58.316 -24.182 1.00109.62 C ANISOU 2695 CB ILE A 409 10901 15705 15045 -3931 1531 1493 C ATOM 2696 CG1 ILE A 409 9.320 58.153 -23.124 1.00113.28 C ANISOU 2696 CG1 ILE A 409 10971 16400 15671 -4053 1293 1333 C ATOM 2697 CG2 ILE A 409 7.441 57.024 -24.339 1.00102.02 C ANISOU 2697 CG2 ILE A 409 10135 14897 13731 -3333 1749 1261 C ATOM 2698 CD1 ILE A 409 8.807 57.680 -21.780 1.00110.20 C ANISOU 2698 CD1 ILE A 409 10898 15768 15203 -3712 1032 859 C ATOM 2699 N MET A 410 6.842 59.691 -26.504 1.00113.87 N ANISOU 2699 N MET A 410 12029 15751 15486 -4176 1784 2142 N ATOM 2700 CA MET A 410 5.725 59.808 -27.438 1.00113.79 C ANISOU 2700 CA MET A 410 12428 15519 15287 -3979 1859 2269 C ATOM 2701 C MET A 410 6.196 59.926 -28.882 1.00120.41 C ANISOU 2701 C MET A 410 13164 16701 15884 -4122 2178 2753 C ATOM 2702 O MET A 410 5.505 59.499 -29.807 1.00120.95 O ANISOU 2702 O MET A 410 13487 16849 15618 -3827 2308 2821 O ATOM 2703 CB MET A 410 4.850 61.010 -27.077 1.00113.15 C ANISOU 2703 CB MET A 410 12779 14716 15498 -4138 1542 2258 C ATOM 2704 CG MET A 410 4.157 60.909 -25.726 1.00109.49 C ANISOU 2704 CG MET A 410 12528 13882 15193 -3896 1291 1779 C ATOM 2705 SD MET A 410 2.842 59.673 -25.680 1.00 99.72 S ANISOU 2705 SD MET A 410 11466 12709 13713 -3258 1397 1454 S ATOM 2706 CE MET A 410 3.693 58.273 -24.955 1.00106.77 C ANISOU 2706 CE MET A 410 12006 14144 14419 -3048 1544 1168 C ATOM 2707 N ALA A 411 7.375 60.511 -29.067 1.00125.33 N ANISOU 2707 N ALA A 411 13417 17529 16672 -4583 2296 3098 N ATOM 2708 CA ALA A 411 7.956 60.654 -30.393 1.00128.40 C ANISOU 2708 CA ALA A 411 13672 18292 16821 -4738 2686 3613 C ATOM 2709 C ALA A 411 8.334 59.293 -30.969 1.00126.51 C ANISOU 2709 C ALA A 411 13209 18735 16123 -4280 3082 3539 C ATOM 2710 O ALA A 411 8.208 59.062 -32.171 1.00127.35 O ANISOU 2710 O ALA A 411 13495 19083 15807 -4109 3386 3797 O ATOM 2711 CB ALA A 411 9.172 61.567 -30.340 1.00134.80 C ANISOU 2711 CB ALA A 411 14048 19175 17996 -5381 2743 4013 C ATOM 2712 N GLU A 412 8.786 58.391 -30.105 1.00125.19 N ANISOU 2712 N GLU A 412 12710 18849 16006 -4048 3062 3177 N ATOM 2713 CA GLU A 412 9.278 57.095 -30.555 1.00128.42 C ANISOU 2713 CA GLU A 412 12893 19879 16022 -3592 3434 3092 C ATOM 2714 C GLU A 412 8.174 56.048 -30.684 1.00125.47 C ANISOU 2714 C GLU A 412 12987 19397 15291 -3028 3376 2705 C ATOM 2715 O GLU A 412 8.306 55.095 -31.452 1.00127.08 O ANISOU 2715 O GLU A 412 13238 19990 15056 -2636 3682 2682 O ATOM 2716 CB GLU A 412 10.380 56.578 -29.629 1.00130.33 C ANISOU 2716 CB GLU A 412 12531 20501 16486 -3577 3441 2933 C ATOM 2717 CG GLU A 412 11.239 55.493 -30.260 1.00134.42 C ANISOU 2717 CG GLU A 412 12685 21730 16659 -3180 3920 3002 C ATOM 2718 CD GLU A 412 12.082 54.747 -29.246 1.00135.42 C ANISOU 2718 CD GLU A 412 12303 22184 16967 -2986 3845 2747 C ATOM 2719 OE1 GLU A 412 11.754 54.802 -28.041 1.00131.29 O ANISOU 2719 OE1 GLU A 412 11873 21307 16704 -3030 3404 2414 O ATOM 2720 OE2 GLU A 412 13.074 54.106 -29.656 1.00140.28 O ANISOU 2720 OE2 GLU A 412 12469 23382 17448 -2736 4220 2869 O ATOM 2721 N VAL A 413 7.091 56.217 -29.933 1.00121.44 N ANISOU 2721 N VAL A 413 12820 18348 14973 -2984 2992 2401 N ATOM 2722 CA VAL A 413 5.982 55.273 -30.010 1.00115.68 C ANISOU 2722 CA VAL A 413 12478 17477 13998 -2527 2908 2063 C ATOM 2723 C VAL A 413 5.206 55.450 -31.312 1.00115.44 C ANISOU 2723 C VAL A 413 12857 17359 13646 -2451 2943 2269 C ATOM 2724 O VAL A 413 4.632 54.497 -31.834 1.00112.57 O ANISOU 2724 O VAL A 413 12750 17079 12942 -2076 2970 2081 O ATOM 2725 CB VAL A 413 5.031 55.371 -28.794 1.00111.46 C ANISOU 2725 CB VAL A 413 12135 16432 13783 -2481 2547 1707 C ATOM 2726 CG1 VAL A 413 5.799 55.148 -27.501 1.00110.41 C ANISOU 2726 CG1 VAL A 413 11682 16392 13876 -2513 2477 1491 C ATOM 2727 CG2 VAL A 413 4.314 56.708 -28.769 1.00111.75 C ANISOU 2727 CG2 VAL A 413 12420 15940 14099 -2785 2293 1867 C ATOM 2728 N CYS A 414 5.203 56.670 -31.840 1.00119.62 N ANISOU 2728 N CYS A 414 13478 17697 14274 -2813 2907 2662 N ATOM 2729 CA CYS A 414 4.551 56.945 -33.114 1.00122.81 C ANISOU 2729 CA CYS A 414 14294 18031 14335 -2748 2915 2922 C ATOM 2730 C CYS A 414 5.396 56.407 -34.258 1.00127.07 C ANISOU 2730 C CYS A 414 14782 19154 14346 -2606 3363 3169 C ATOM 2731 O CYS A 414 4.869 55.989 -35.289 1.00128.49 O ANISOU 2731 O CYS A 414 15358 19417 14046 -2331 3394 3198 O ATOM 2732 CB CYS A 414 4.320 58.445 -33.291 1.00126.32 C ANISOU 2732 CB CYS A 414 14900 18049 15048 -3161 2743 3303 C ATOM 2733 SG CYS A 414 3.174 59.155 -32.095 1.00117.47 S ANISOU 2733 SG CYS A 414 13959 16195 14478 -3216 2245 3014 S ATOM 2734 N ARG A 415 6.711 56.427 -34.066 1.00130.25 N ANISOU 2734 N ARG A 415 14689 19966 14833 -2780 3704 3345 N ATOM 2735 CA ARG A 415 7.633 55.846 -35.031 1.00136.02 C ANISOU 2735 CA ARG A 415 15278 21319 15085 -2582 4225 3566 C ATOM 2736 C ARG A 415 7.360 54.354 -35.160 1.00132.63 C ANISOU 2736 C ARG A 415 15037 21110 14248 -1983 4284 3122 C ATOM 2737 O ARG A 415 7.316 53.813 -36.264 1.00137.13 O ANISOU 2737 O ARG A 415 15932 21939 14230 -1661 4525 3180 O ATOM 2738 CB ARG A 415 9.081 56.077 -34.597 1.00142.12 C ANISOU 2738 CB ARG A 415 15343 22503 16152 -2864 4544 3797 C ATOM 2739 CG ARG A 415 10.112 55.460 -35.530 1.00150.83 C ANISOU 2739 CG ARG A 415 16207 24297 16805 -2602 5161 4032 C ATOM 2740 CD ARG A 415 11.473 55.373 -34.863 1.00156.97 C ANISOU 2740 CD ARG A 415 16301 25311 18030 -2688 5282 3975 C ATOM 2741 NE ARG A 415 11.409 54.637 -33.604 1.00154.67 N ANISOU 2741 NE ARG A 415 15752 25032 17983 -2511 5015 3541 N ATOM 2742 CZ ARG A 415 11.487 53.314 -33.507 1.00155.28 C ANISOU 2742 CZ ARG A 415 15865 25356 17778 -1923 5124 3169 C ATOM 2743 NH1 ARG A 415 11.632 52.573 -34.598 1.00159.09 N ANISOU 2743 NH1 ARG A 415 16644 26073 17728 -1462 5474 3143 N ATOM 2744 NH2 ARG A 415 11.418 52.730 -32.318 1.00151.69 N ANISOU 2744 NH2 ARG A 415 15206 24874 17553 -1789 4869 2814 N ATOM 2745 N ALA A 416 7.167 53.695 -34.022 1.00124.71 N ANISOU 2745 N ALA A 416 13884 19965 13535 -1833 4053 2680 N ATOM 2746 CA ALA A 416 6.849 52.274 -34.005 1.00119.54 C ANISOU 2746 CA ALA A 416 13440 19406 12575 -1305 4056 2246 C ATOM 2747 C ALA A 416 5.482 52.019 -34.632 1.00116.84 C ANISOU 2747 C ALA A 416 13721 18703 11968 -1131 3749 2075 C ATOM 2748 O ALA A 416 5.268 50.997 -35.283 1.00117.12 O ANISOU 2748 O ALA A 416 14088 18870 11544 -730 3817 1863 O ATOM 2749 CB ALA A 416 6.888 51.743 -32.584 1.00113.94 C ANISOU 2749 CB ALA A 416 12469 18558 12263 -1233 3857 1874 C ATOM 2750 N ILE A 417 4.561 52.955 -34.430 1.00114.31 N ANISOU 2750 N ILE A 417 13560 17916 11956 -1424 3382 2160 N ATOM 2751 CA ILE A 417 3.217 52.843 -34.986 1.00112.85 C ANISOU 2751 CA ILE A 417 13873 17387 11617 -1297 3022 2038 C ATOM 2752 C ILE A 417 3.227 53.071 -36.495 1.00119.24 C ANISOU 2752 C ILE A 417 15069 18392 11845 -1223 3143 2350 C ATOM 2753 O ILE A 417 2.566 52.355 -37.249 1.00120.95 O ANISOU 2753 O ILE A 417 15721 18590 11644 -929 2980 2165 O ATOM 2754 CB ILE A 417 2.240 53.824 -34.301 1.00108.22 C ANISOU 2754 CB ILE A 417 13300 16260 11561 -1570 2617 2058 C ATOM 2755 CG1 ILE A 417 1.862 53.309 -32.912 1.00101.89 C ANISOU 2755 CG1 ILE A 417 12299 15225 11191 -1504 2458 1657 C ATOM 2756 CG2 ILE A 417 0.987 54.005 -35.129 1.00108.45 C ANISOU 2756 CG2 ILE A 417 13767 16007 11431 -1483 2259 2093 C ATOM 2757 CD1 ILE A 417 0.830 54.158 -32.207 1.00 98.87 C ANISOU 2757 CD1 ILE A 417 11953 14323 11291 -1671 2114 1629 C ATOM 2758 N LYS A 418 3.992 54.065 -36.932 1.00123.59 N ANISOU 2758 N LYS A 418 15485 19117 12356 -1505 3419 2832 N ATOM 2759 CA LYS A 418 4.132 54.358 -38.352 1.00128.88 C ANISOU 2759 CA LYS A 418 16536 20011 12423 -1442 3621 3208 C ATOM 2760 C LYS A 418 4.844 53.200 -39.047 1.00132.86 C ANISOU 2760 C LYS A 418 17143 21041 12297 -1008 4046 3077 C ATOM 2761 O LYS A 418 4.635 52.948 -40.234 1.00137.24 O ANISOU 2761 O LYS A 418 18213 21741 12190 -753 4109 3161 O ATOM 2762 CB LYS A 418 4.915 55.661 -38.546 1.00131.76 C ANISOU 2762 CB LYS A 418 16670 20443 12950 -1890 3899 3799 C ATOM 2763 CG LYS A 418 4.407 56.556 -39.672 1.00134.78 C ANISOU 2763 CG LYS A 418 17561 20658 12993 -1995 3800 4248 C ATOM 2764 CD LYS A 418 4.817 56.042 -41.044 1.00139.04 C ANISOU 2764 CD LYS A 418 18485 21674 12672 -1669 4197 4443 C ATOM 2765 CE LYS A 418 4.332 56.966 -42.153 1.00142.29 C ANISOU 2765 CE LYS A 418 19453 21915 12695 -1765 4084 4933 C ATOM 2766 NZ LYS A 418 4.899 58.338 -42.028 1.00144.45 N ANISOU 2766 NZ LYS A 418 19479 22047 13356 -2305 4282 5527 N ATOM 2767 N GLN A 419 5.676 52.490 -38.291 1.00132.72 N ANISOU 2767 N GLN A 419 16671 21293 12462 -884 4315 2855 N ATOM 2768 CA GLN A 419 6.462 51.385 -38.828 1.00137.31 C ANISOU 2768 CA GLN A 419 17293 22374 12507 -414 4766 2718 C ATOM 2769 C GLN A 419 5.607 50.136 -39.032 1.00135.69 C ANISOU 2769 C GLN A 419 17617 21975 11962 35 4459 2185 C ATOM 2770 O GLN A 419 6.010 49.201 -39.725 1.00139.57 O ANISOU 2770 O GLN A 419 18389 22774 11869 493 4748 2028 O ATOM 2771 CB GLN A 419 7.637 51.076 -37.896 1.00137.50 C ANISOU 2771 CB GLN A 419 16611 22732 12899 -411 5104 2678 C ATOM 2772 CG GLN A 419 8.736 50.237 -38.519 1.00143.62 C ANISOU 2772 CG GLN A 419 17287 24079 13202 42 5688 2683 C ATOM 2773 CD GLN A 419 9.946 50.110 -37.616 1.00145.40 C ANISOU 2773 CD GLN A 419 16789 24463 13994 -23 5851 2632 C ATOM 2774 OE1 GLN A 419 9.917 50.526 -36.458 1.00140.62 O ANISOU 2774 OE1 GLN A 419 15746 23734 13949 -344 5618 2628 O ATOM 2775 NE2 GLN A 419 11.022 49.540 -38.145 1.00152.63 N ANISOU 2775 NE2 GLN A 419 17581 25666 14747 291 6229 2597 N ATOM 2776 N LEU A 420 4.423 50.126 -38.430 1.00130.87 N ANISOU 2776 N LEU A 420 17149 20840 11735 -97 3880 1911 N ATOM 2777 CA LEU A 420 3.528 48.980 -38.534 1.00130.62 C ANISOU 2777 CA LEU A 420 17564 20555 11510 224 3523 1422 C ATOM 2778 C LEU A 420 2.290 49.285 -39.369 1.00133.94 C ANISOU 2778 C LEU A 420 18529 20655 11709 170 3023 1436 C ATOM 2779 O LEU A 420 1.383 48.457 -39.463 1.00133.75 O ANISOU 2779 O LEU A 420 18853 20353 11615 336 2610 1052 O ATOM 2780 CB LEU A 420 3.116 48.494 -37.144 1.00124.76 C ANISOU 2780 CB LEU A 420 16521 19488 11393 160 3269 1068 C ATOM 2781 CG LEU A 420 3.754 47.183 -36.687 1.00125.83 C ANISOU 2781 CG LEU A 420 16587 19792 11429 543 3505 720 C ATOM 2782 CD1 LEU A 420 3.367 46.047 -37.623 1.00129.22 C ANISOU 2782 CD1 LEU A 420 17656 20179 11264 955 3405 399 C ATOM 2783 CD2 LEU A 420 5.262 47.324 -36.618 1.00129.03 C ANISOU 2783 CD2 LEU A 420 16539 20738 11749 637 4083 961 C ATOM 2784 N ASP A 421 2.266 50.473 -39.970 1.00137.12 N ANISOU 2784 N ASP A 421 18994 21083 12021 -74 3036 1896 N ATOM 2785 CA ASP A 421 1.148 50.917 -40.802 1.00137.84 C ANISOU 2785 CA ASP A 421 19583 20896 11895 -114 2538 1990 C ATOM 2786 C ASP A 421 -0.161 50.940 -40.014 1.00128.76 C ANISOU 2786 C ASP A 421 18324 19224 11376 -270 1920 1727 C ATOM 2787 O ASP A 421 -1.143 50.309 -40.405 1.00126.96 O ANISOU 2787 O ASP A 421 18450 18781 11009 -122 1445 1440 O ATOM 2788 CB ASP A 421 1.012 50.034 -42.050 1.00145.05 C ANISOU 2788 CB ASP A 421 21179 21980 11955 296 2481 1803 C ATOM 2789 CG ASP A 421 0.163 50.672 -43.135 1.00150.33 C ANISOU 2789 CG ASP A 421 22393 22496 12229 271 2046 2036 C ATOM 2790 OD1 ASP A 421 -0.504 51.691 -42.857 1.00149.35 O ANISOU 2790 OD1 ASP A 421 22105 22067 12575 -34 1712 2286 O ATOM 2791 OD2 ASP A 421 0.158 50.148 -44.269 1.00155.94 O ANISOU 2791 OD2 ASP A 421 23737 23382 12133 596 2020 1960 O ATOM 2792 N TYR A 422 -0.166 51.665 -38.900 1.00123.55 N ANISOU 2792 N TYR A 422 17167 18364 11413 -568 1930 1825 N ATOM 2793 CA TYR A 422 -1.367 51.793 -38.082 1.00119.18 C ANISOU 2793 CA TYR A 422 16458 17345 11481 -691 1449 1625 C ATOM 2794 C TYR A 422 -1.968 53.186 -38.217 1.00119.44 C ANISOU 2794 C TYR A 422 16495 17099 11787 -927 1187 1996 C ATOM 2795 O TYR A 422 -1.261 54.156 -38.485 1.00121.36 O ANISOU 2795 O TYR A 422 16712 17451 11948 -1107 1451 2408 O ATOM 2796 CB TYR A 422 -1.068 51.513 -36.606 1.00114.34 C ANISOU 2796 CB TYR A 422 15360 16649 11437 -777 1622 1398 C ATOM 2797 CG TYR A 422 -0.762 50.069 -36.264 1.00112.66 C ANISOU 2797 CG TYR A 422 15150 16567 11088 -519 1763 989 C ATOM 2798 CD1 TYR A 422 -0.654 49.100 -37.253 1.00115.74 C ANISOU 2798 CD1 TYR A 422 15965 17142 10868 -224 1773 818 C ATOM 2799 CD2 TYR A 422 -0.577 49.679 -34.943 1.00107.86 C ANISOU 2799 CD2 TYR A 422 14184 15868 10932 -544 1876 772 C ATOM 2800 CE1 TYR A 422 -0.367 47.786 -36.937 1.00114.36 C ANISOU 2800 CE1 TYR A 422 15850 17020 10581 35 1892 443 C ATOM 2801 CE2 TYR A 422 -0.297 48.367 -34.618 1.00106.45 C ANISOU 2801 CE2 TYR A 422 14050 15763 10634 -291 1996 432 C ATOM 2802 CZ TYR A 422 -0.195 47.424 -35.618 1.00109.97 C ANISOU 2802 CZ TYR A 422 14914 16356 10515 -4 2003 268 C ATOM 2803 OH TYR A 422 0.086 46.116 -35.300 1.00109.85 O ANISOU 2803 OH TYR A 422 14999 16350 10388 273 2112 -75 O ATOM 2804 N GLU A 423 -3.278 53.276 -38.024 1.00118.74 N ANISOU 2804 N GLU A 423 16422 16635 12058 -922 673 1863 N ATOM 2805 CA GLU A 423 -3.970 54.556 -38.063 1.00120.88 C ANISOU 2805 CA GLU A 423 16688 16586 12654 -1067 384 2178 C ATOM 2806 C GLU A 423 -4.108 55.109 -36.650 1.00117.39 C ANISOU 2806 C GLU A 423 15803 15853 12944 -1234 454 2111 C ATOM 2807 O GLU A 423 -4.919 54.627 -35.864 1.00114.72 O ANISOU 2807 O GLU A 423 15249 15309 13032 -1166 265 1803 O ATOM 2808 CB GLU A 423 -5.351 54.394 -38.699 1.00123.30 C ANISOU 2808 CB GLU A 423 17222 16673 12952 -919 -241 2096 C ATOM 2809 CG GLU A 423 -5.326 53.795 -40.095 1.00128.84 C ANISOU 2809 CG GLU A 423 18459 17621 12874 -726 -415 2098 C ATOM 2810 CD GLU A 423 -6.716 53.507 -40.628 1.00132.29 C ANISOU 2810 CD GLU A 423 19068 17837 13358 -605 -1135 1950 C ATOM 2811 OE1 GLU A 423 -7.700 53.837 -39.933 1.00130.39 O ANISOU 2811 OE1 GLU A 423 18464 17278 13800 -666 -1451 1899 O ATOM 2812 OE2 GLU A 423 -6.823 52.948 -41.741 1.00137.24 O ANISOU 2812 OE2 GLU A 423 20188 18617 13339 -437 -1392 1882 O ATOM 2813 N TRP A 424 -3.310 56.122 -36.329 1.00118.60 N ANISOU 2813 N TRP A 424 15847 15982 13234 -1460 730 2406 N ATOM 2814 CA TRP A 424 -3.325 56.706 -34.994 1.00116.75 C ANISOU 2814 CA TRP A 424 15284 15458 13616 -1611 790 2323 C ATOM 2815 C TRP A 424 -3.948 58.098 -34.990 1.00117.03 C ANISOU 2815 C TRP A 424 15421 15058 13986 -1711 537 2616 C ATOM 2816 O TRP A 424 -3.842 58.838 -35.968 1.00121.37 O ANISOU 2816 O TRP A 424 16260 15587 14269 -1779 468 3012 O ATOM 2817 CB TRP A 424 -1.907 56.764 -34.424 1.00120.25 C ANISOU 2817 CB TRP A 424 15496 16145 14049 -1817 1236 2365 C ATOM 2818 CG TRP A 424 -0.933 57.481 -35.309 1.00128.76 C ANISOU 2818 CG TRP A 424 16699 17433 14792 -2026 1479 2823 C ATOM 2819 CD1 TRP A 424 -0.174 56.935 -36.301 1.00133.23 C ANISOU 2819 CD1 TRP A 424 17389 18460 14773 -1948 1766 2964 C ATOM 2820 CD2 TRP A 424 -0.613 58.879 -35.280 1.00134.31 C ANISOU 2820 CD2 TRP A 424 17431 17873 15727 -2349 1492 3221 C ATOM 2821 NE1 TRP A 424 0.600 57.904 -36.892 1.00139.28 N ANISOU 2821 NE1 TRP A 424 18215 19308 15397 -2216 2000 3463 N ATOM 2822 CE2 TRP A 424 0.349 59.102 -36.287 1.00140.29 C ANISOU 2822 CE2 TRP A 424 18291 18973 16038 -2494 1814 3633 C ATOM 2823 CE3 TRP A 424 -1.047 59.956 -34.506 1.00135.40 C ANISOU 2823 CE3 TRP A 424 17553 17495 16397 -2515 1277 3268 C ATOM 2824 CZ2 TRP A 424 0.883 60.368 -36.534 1.00145.85 C ANISOU 2824 CZ2 TRP A 424 19055 19504 16859 -2864 1916 4125 C ATOM 2825 CZ3 TRP A 424 -0.514 61.210 -34.756 1.00140.44 C ANISOU 2825 CZ3 TRP A 424 18302 17921 17136 -2857 1334 3712 C ATOM 2826 CH2 TRP A 424 0.441 61.405 -35.761 1.00145.42 C ANISOU 2826 CH2 TRP A 424 19008 18887 17358 -3059 1646 4151 C ATOM 2827 N LYS A 425 -4.601 58.445 -33.885 1.00113.27 N ANISOU 2827 N LYS A 425 14746 14221 14071 -1682 421 2430 N ATOM 2828 CA LYS A 425 -5.208 59.764 -33.727 1.00114.50 C ANISOU 2828 CA LYS A 425 15005 13904 14595 -1710 199 2656 C ATOM 2829 C LYS A 425 -4.912 60.343 -32.344 1.00110.76 C ANISOU 2829 C LYS A 425 14359 13143 14581 -1832 356 2505 C ATOM 2830 O LYS A 425 -5.158 59.697 -31.325 1.00107.25 O ANISOU 2830 O LYS A 425 13683 12704 14364 -1715 442 2139 O ATOM 2831 CB LYS A 425 -6.719 59.699 -33.971 1.00116.43 C ANISOU 2831 CB LYS A 425 15252 13928 15058 -1414 -223 2589 C ATOM 2832 CG LYS A 425 -7.102 59.370 -35.410 1.00121.67 C ANISOU 2832 CG LYS A 425 16181 14790 15260 -1298 -519 2772 C ATOM 2833 CD LYS A 425 -8.609 59.240 -35.577 1.00124.27 C ANISOU 2833 CD LYS A 425 16410 14925 15882 -1027 -1006 2681 C ATOM 2834 CE LYS A 425 -8.984 58.888 -37.012 1.00128.59 C ANISOU 2834 CE LYS A 425 17268 15666 15926 -915 -1395 2831 C ATOM 2835 NZ LYS A 425 -8.614 59.966 -37.973 1.00133.07 N ANISOU 2835 NZ LYS A 425 18270 16153 16138 -963 -1468 3325 N ATOM 2836 N VAL A 426 -4.384 61.563 -32.316 1.00111.98 N ANISOU 2836 N VAL A 426 14676 13021 14849 -2073 379 2795 N ATOM 2837 CA VAL A 426 -3.978 62.202 -31.068 1.00109.83 C ANISOU 2837 CA VAL A 426 14333 12441 14955 -2231 475 2648 C ATOM 2838 C VAL A 426 -5.131 62.904 -30.358 1.00111.55 C ANISOU 2838 C VAL A 426 14637 12119 15628 -1976 255 2518 C ATOM 2839 O VAL A 426 -5.774 63.790 -30.922 1.00116.95 O ANISOU 2839 O VAL A 426 15557 12456 16422 -1880 17 2786 O ATOM 2840 CB VAL A 426 -2.846 63.224 -31.303 1.00110.76 C ANISOU 2840 CB VAL A 426 14593 12444 15046 -2666 572 3007 C ATOM 2841 CG1 VAL A 426 -2.659 64.108 -30.081 1.00110.61 C ANISOU 2841 CG1 VAL A 426 14624 11945 15456 -2817 518 2853 C ATOM 2842 CG2 VAL A 426 -1.550 62.512 -31.653 1.00110.09 C ANISOU 2842 CG2 VAL A 426 14289 12932 14608 -2909 891 3080 C ATOM 2843 N VAL A 427 -5.385 62.504 -29.116 1.00107.25 N ANISOU 2843 N VAL A 427 13917 11508 15325 -1825 357 2121 N ATOM 2844 CA VAL A 427 -6.379 63.170 -28.284 1.00106.54 C ANISOU 2844 CA VAL A 427 13901 10928 15652 -1543 251 1968 C ATOM 2845 C VAL A 427 -5.679 64.125 -27.321 1.00106.01 C ANISOU 2845 C VAL A 427 14046 10474 15760 -1746 298 1885 C ATOM 2846 O VAL A 427 -6.112 65.261 -27.126 1.00108.59 O ANISOU 2846 O VAL A 427 14653 10259 16349 -1656 146 1965 O ATOM 2847 CB VAL A 427 -7.221 62.155 -27.492 1.00102.81 C ANISOU 2847 CB VAL A 427 13140 10598 15324 -1213 368 1601 C ATOM 2848 CG1 VAL A 427 -8.245 62.872 -26.624 1.00103.59 C ANISOU 2848 CG1 VAL A 427 13294 10223 15842 -870 342 1465 C ATOM 2849 CG2 VAL A 427 -7.906 61.185 -28.441 1.00101.83 C ANISOU 2849 CG2 VAL A 427 12814 10810 15066 -1075 250 1659 C ATOM 2850 N ASN A 428 -4.593 63.645 -26.723 1.00102.60 N ANISOU 2850 N ASN A 428 13495 10308 15181 -2005 474 1713 N ATOM 2851 CA ASN A 428 -3.740 64.455 -25.864 1.00104.05 C ANISOU 2851 CA ASN A 428 13860 10185 15489 -2287 449 1624 C ATOM 2852 C ASN A 428 -2.291 64.260 -26.288 1.00104.67 C ANISOU 2852 C ASN A 428 13776 10646 15348 -2768 533 1813 C ATOM 2853 O ASN A 428 -1.989 63.330 -27.034 1.00103.52 O ANISOU 2853 O ASN A 428 13383 11032 14918 -2778 683 1919 O ATOM 2854 CB ASN A 428 -3.907 64.049 -24.397 1.00102.39 C ANISOU 2854 CB ASN A 428 13628 9914 15363 -2062 552 1157 C ATOM 2855 CG ASN A 428 -5.302 64.311 -23.872 1.00104.63 C ANISOU 2855 CG ASN A 428 14038 9825 15891 -1567 553 984 C ATOM 2856 OD1 ASN A 428 -6.122 63.398 -23.774 1.00101.95 O ANISOU 2856 OD1 ASN A 428 13456 9728 15553 -1242 696 856 O ATOM 2857 ND2 ASN A 428 -5.579 65.563 -23.526 1.00110.02 N ANISOU 2857 ND2 ASN A 428 15094 9901 16806 -1505 402 987 N ATOM 2858 N PRO A 429 -1.384 65.136 -25.824 1.00107.20 N ANISOU 2858 N PRO A 429 14227 10693 15812 -3164 434 1856 N ATOM 2859 CA PRO A 429 0.040 64.905 -26.094 1.00107.63 C ANISOU 2859 CA PRO A 429 14002 11163 15728 -3629 537 2029 C ATOM 2860 C PRO A 429 0.550 63.602 -25.477 1.00104.57 C ANISOU 2860 C PRO A 429 13250 11334 15147 -3505 710 1713 C ATOM 2861 O PRO A 429 1.654 63.171 -25.805 1.00106.88 O ANISOU 2861 O PRO A 429 13220 12092 15296 -3773 845 1856 O ATOM 2862 CB PRO A 429 0.718 66.105 -25.428 1.00110.89 C ANISOU 2862 CB PRO A 429 14629 11070 16433 -4055 309 2038 C ATOM 2863 CG PRO A 429 -0.311 67.175 -25.464 1.00113.22 C ANISOU 2863 CG PRO A 429 15409 10658 16952 -3869 114 2090 C ATOM 2864 CD PRO A 429 -1.622 66.473 -25.250 1.00110.28 C ANISOU 2864 CD PRO A 429 15036 10350 16513 -3235 200 1823 C ATOM 2865 N TYR A 430 -0.241 62.988 -24.601 1.00100.75 N ANISOU 2865 N TYR A 430 12814 10801 14667 -3087 731 1320 N ATOM 2866 CA TYR A 430 0.140 61.730 -23.970 1.00 98.07 C ANISOU 2866 CA TYR A 430 12203 10922 14137 -2922 888 1033 C ATOM 2867 C TYR A 430 -1.005 60.721 -24.003 1.00 96.46 C ANISOU 2867 C TYR A 430 11972 10843 13837 -2449 1031 861 C ATOM 2868 O TYR A 430 -1.162 59.912 -23.089 1.00 95.18 O ANISOU 2868 O TYR A 430 11757 10792 13616 -2209 1130 552 O ATOM 2869 CB TYR A 430 0.594 61.973 -22.530 1.00 98.60 C ANISOU 2869 CB TYR A 430 12374 10788 14303 -2973 755 698 C ATOM 2870 CG TYR A 430 1.737 62.956 -22.417 1.00103.11 C ANISOU 2870 CG TYR A 430 12946 11202 15030 -3503 535 837 C ATOM 2871 CD1 TYR A 430 3.044 62.560 -22.665 1.00104.27 C ANISOU 2871 CD1 TYR A 430 12679 11841 15099 -3833 578 984 C ATOM 2872 CD2 TYR A 430 1.509 64.282 -22.075 1.00106.84 C ANISOU 2872 CD2 TYR A 430 13818 11017 15759 -3675 279 831 C ATOM 2873 CE1 TYR A 430 4.092 63.454 -22.569 1.00109.97 C ANISOU 2873 CE1 TYR A 430 13318 12431 16035 -4378 363 1143 C ATOM 2874 CE2 TYR A 430 2.550 65.185 -21.976 1.00111.96 C ANISOU 2874 CE2 TYR A 430 14475 11467 16597 -4228 35 965 C ATOM 2875 CZ TYR A 430 3.840 64.766 -22.224 1.00113.81 C ANISOU 2875 CZ TYR A 430 14227 12225 16791 -4609 72 1132 C ATOM 2876 OH TYR A 430 4.884 65.659 -22.128 1.00119.50 O ANISOU 2876 OH TYR A 430 14873 12762 17770 -5220 -184 1295 O ATOM 2877 N TYR A 431 -1.797 60.773 -25.070 1.00 97.15 N ANISOU 2877 N TYR A 431 12100 10903 13910 -2337 1019 1083 N ATOM 2878 CA TYR A 431 -2.965 59.911 -25.214 1.00 94.59 C ANISOU 2878 CA TYR A 431 11717 10654 13570 -1953 1080 957 C ATOM 2879 C TYR A 431 -3.293 59.744 -26.694 1.00 94.88 C ANISOU 2879 C TYR A 431 11737 10869 13443 -1954 1019 1251 C ATOM 2880 O TYR A 431 -3.640 60.710 -27.375 1.00 97.50 O ANISOU 2880 O TYR A 431 12248 10932 13864 -2020 853 1522 O ATOM 2881 CB TYR A 431 -4.158 60.518 -24.471 1.00 97.23 C ANISOU 2881 CB TYR A 431 12221 10501 14221 -1672 1010 807 C ATOM 2882 CG TYR A 431 -5.439 59.707 -24.510 1.00 97.82 C ANISOU 2882 CG TYR A 431 12148 10629 14390 -1308 1074 699 C ATOM 2883 CD1 TYR A 431 -5.424 58.339 -24.758 1.00 96.32 C ANISOU 2883 CD1 TYR A 431 11743 10847 14007 -1249 1193 612 C ATOM 2884 CD2 TYR A 431 -6.666 60.315 -24.276 1.00100.15 C ANISOU 2884 CD2 TYR A 431 12503 10544 15004 -1024 1012 689 C ATOM 2885 CE1 TYR A 431 -6.600 57.606 -24.788 1.00 96.10 C ANISOU 2885 CE1 TYR A 431 11557 10828 14127 -992 1217 529 C ATOM 2886 CE2 TYR A 431 -7.842 59.592 -24.303 1.00 99.68 C ANISOU 2886 CE2 TYR A 431 12213 10552 15107 -735 1066 624 C ATOM 2887 CZ TYR A 431 -7.805 58.240 -24.558 1.00 98.07 C ANISOU 2887 CZ TYR A 431 11791 10738 14734 -757 1154 548 C ATOM 2888 OH TYR A 431 -8.979 57.525 -24.582 1.00 99.10 O ANISOU 2888 OH TYR A 431 11670 10900 15083 -540 1174 498 O ATOM 2889 N LEU A 432 -3.182 58.514 -27.186 1.00 92.43 N ANISOU 2889 N LEU A 432 11270 10987 12862 -1859 1131 1190 N ATOM 2890 CA LEU A 432 -3.462 58.228 -28.588 1.00 92.72 C ANISOU 2890 CA LEU A 432 11360 11220 12649 -1828 1050 1415 C ATOM 2891 C LEU A 432 -4.660 57.298 -28.747 1.00 91.94 C ANISOU 2891 C LEU A 432 11203 11137 12593 -1535 948 1236 C ATOM 2892 O LEU A 432 -5.127 56.693 -27.783 1.00 89.21 O ANISOU 2892 O LEU A 432 10728 10727 12441 -1376 1032 958 O ATOM 2893 CB LEU A 432 -2.237 57.623 -29.282 1.00 92.24 C ANISOU 2893 CB LEU A 432 11227 11648 12174 -1976 1248 1527 C ATOM 2894 CG LEU A 432 -1.082 58.556 -29.658 1.00 94.96 C ANISOU 2894 CG LEU A 432 11578 12060 12443 -2329 1342 1860 C ATOM 2895 CD1 LEU A 432 -0.238 58.927 -28.444 1.00 94.64 C ANISOU 2895 CD1 LEU A 432 11375 11943 12643 -2536 1406 1726 C ATOM 2896 CD2 LEU A 432 -0.220 57.929 -30.745 1.00 95.78 C ANISOU 2896 CD2 LEU A 432 11628 12679 12083 -2365 1566 2050 C ATOM 2897 N ARG A 433 -5.151 57.198 -29.977 1.00 95.35 N ANISOU 2897 N ARG A 433 11744 11647 12839 -1482 753 1416 N ATOM 2898 CA ARG A 433 -6.251 56.306 -30.304 1.00 96.70 C ANISOU 2898 CA ARG A 433 11847 11841 13052 -1270 568 1267 C ATOM 2899 C ARG A 433 -5.890 55.541 -31.573 1.00100.01 C ANISOU 2899 C ARG A 433 12430 12607 12963 -1275 504 1333 C ATOM 2900 O ARG A 433 -6.364 55.869 -32.660 1.00103.34 O ANISOU 2900 O ARG A 433 13038 13008 13219 -1242 225 1540 O ATOM 2901 CB ARG A 433 -7.534 57.106 -30.520 1.00100.00 C ANISOU 2901 CB ARG A 433 12264 11914 13819 -1134 251 1402 C ATOM 2902 CG ARG A 433 -8.807 56.304 -30.328 1.00102.49 C ANISOU 2902 CG ARG A 433 12341 12173 14426 -939 87 1206 C ATOM 2903 CD ARG A 433 -9.221 56.270 -28.865 1.00103.34 C ANISOU 2903 CD ARG A 433 12213 12083 14967 -829 329 990 C ATOM 2904 NE ARG A 433 -9.869 57.513 -28.453 1.00108.11 N ANISOU 2904 NE ARG A 433 12803 12321 15954 -688 263 1109 N ATOM 2905 CZ ARG A 433 -11.185 57.706 -28.464 1.00112.15 C ANISOU 2905 CZ ARG A 433 13089 12648 16874 -462 75 1147 C ATOM 2906 NH1 ARG A 433 -11.997 56.735 -28.862 1.00112.63 N ANISOU 2906 NH1 ARG A 433 12892 12857 17044 -420 -103 1080 N ATOM 2907 NH2 ARG A 433 -11.689 58.870 -28.074 1.00114.95 N ANISOU 2907 NH2 ARG A 433 13467 12656 17555 -272 49 1249 N ATOM 2908 N VAL A 434 -5.044 54.525 -31.426 1.00 99.59 N ANISOU 2908 N VAL A 434 12345 12862 12631 -1275 756 1151 N ATOM 2909 CA VAL A 434 -4.488 53.801 -32.570 1.00101.53 C ANISOU 2909 CA VAL A 434 12799 13456 12323 -1232 787 1186 C ATOM 2910 C VAL A 434 -5.415 52.698 -33.090 1.00100.88 C ANISOU 2910 C VAL A 434 12821 13363 12146 -1066 508 962 C ATOM 2911 O VAL A 434 -6.003 51.946 -32.314 1.00 97.14 O ANISOU 2911 O VAL A 434 12176 12756 11979 -1005 483 697 O ATOM 2912 CB VAL A 434 -3.090 53.230 -32.239 1.00101.38 C ANISOU 2912 CB VAL A 434 12695 13781 12043 -1253 1192 1106 C ATOM 2913 CG1 VAL A 434 -3.117 52.506 -30.908 1.00 98.58 C ANISOU 2913 CG1 VAL A 434 12122 13351 11984 -1181 1321 788 C ATOM 2914 CG2 VAL A 434 -2.587 52.320 -33.351 1.00103.21 C ANISOU 2914 CG2 VAL A 434 13160 14368 11688 -1107 1277 1079 C ATOM 2915 N ARG A 435 -5.534 52.618 -34.413 1.00105.61 N ANISOU 2915 N ARG A 435 13730 14090 12307 -1010 288 1084 N ATOM 2916 CA ARG A 435 -6.461 51.705 -35.071 1.00107.97 C ANISOU 2916 CA ARG A 435 14193 14339 12494 -892 -105 884 C ATOM 2917 C ARG A 435 -5.738 50.835 -36.100 1.00110.63 C ANISOU 2917 C ARG A 435 14926 14988 12121 -764 -29 793 C ATOM 2918 O ARG A 435 -4.928 51.332 -36.884 1.00112.69 O ANISOU 2918 O ARG A 435 15421 15494 11901 -748 158 1047 O ATOM 2919 CB ARG A 435 -7.571 52.514 -35.746 1.00112.20 C ANISOU 2919 CB ARG A 435 14792 14665 13176 -890 -602 1096 C ATOM 2920 CG ARG A 435 -8.487 51.726 -36.659 1.00117.43 C ANISOU 2920 CG ARG A 435 15661 15298 13658 -802 -1128 938 C ATOM 2921 CD ARG A 435 -9.475 52.658 -37.349 1.00123.13 C ANISOU 2921 CD ARG A 435 16427 15850 14506 -770 -1645 1203 C ATOM 2922 NE ARG A 435 -10.836 52.505 -36.839 1.00123.96 N ANISOU 2922 NE ARG A 435 16125 15692 15284 -772 -2029 1079 N ATOM 2923 CZ ARG A 435 -11.855 53.283 -37.187 1.00126.38 C ANISOU 2923 CZ ARG A 435 16308 15821 15887 -704 -2493 1286 C ATOM 2924 NH1 ARG A 435 -11.668 54.280 -38.043 1.00129.29 N ANISOU 2924 NH1 ARG A 435 17006 16209 15909 -631 -2651 1631 N ATOM 2925 NH2 ARG A 435 -13.060 53.070 -36.676 1.00126.36 N ANISOU 2925 NH2 ARG A 435 15839 15628 16546 -697 -2782 1179 N ATOM 2926 N ARG A 436 -6.031 49.537 -36.091 1.00111.05 N ANISOU 2926 N ARG A 436 15077 15013 12105 -663 -148 440 N ATOM 2927 CA ARG A 436 -5.400 48.606 -37.023 1.00114.01 C ANISOU 2927 CA ARG A 436 15896 15630 11791 -475 -83 282 C ATOM 2928 C ARG A 436 -6.426 47.797 -37.811 1.00116.10 C ANISOU 2928 C ARG A 436 16490 15715 11909 -418 -663 37 C ATOM 2929 O ARG A 436 -7.468 47.413 -37.282 1.00114.71 O ANISOU 2929 O ARG A 436 16078 15237 12268 -535 -996 -134 O ATOM 2930 CB ARG A 436 -4.452 47.657 -36.282 1.00113.12 C ANISOU 2930 CB ARG A 436 15695 15656 11629 -359 374 45 C ATOM 2931 CG ARG A 436 -3.565 46.826 -37.201 1.00119.10 C ANISOU 2931 CG ARG A 436 16901 16709 11642 -84 578 -85 C ATOM 2932 CD ARG A 436 -4.057 45.395 -37.378 1.00122.99 C ANISOU 2932 CD ARG A 436 17722 16994 12012 63 305 -516 C ATOM 2933 NE ARG A 436 -3.709 44.546 -36.242 1.00122.67 N ANISOU 2933 NE ARG A 436 17459 16860 12291 116 577 -743 N ATOM 2934 CZ ARG A 436 -4.573 44.139 -35.318 1.00123.35 C ANISOU 2934 CZ ARG A 436 17307 16588 12974 -50 377 -893 C ATOM 2935 NH1 ARG A 436 -5.848 44.496 -35.396 1.00125.30 N ANISOU 2935 NH1 ARG A 436 17434 16560 13614 -279 -93 -854 N ATOM 2936 NH2 ARG A 436 -4.164 43.369 -34.319 1.00121.41 N ANISOU 2936 NH2 ARG A 436 16931 16269 12932 30 658 -1058 N ATOM 2937 N LYS A 437 -6.120 47.543 -39.079 1.00120.08 N ANISOU 2937 N LYS A 437 17541 16406 11677 -245 -782 26 N ATOM 2938 CA LYS A 437 -6.956 46.693 -39.918 1.00123.44 C ANISOU 2938 CA LYS A 437 18391 16666 11847 -179 -1379 -259 C ATOM 2939 C LYS A 437 -6.359 45.292 -39.996 1.00123.78 C ANISOU 2939 C LYS A 437 18789 16742 11501 23 -1194 -660 C ATOM 2940 O LYS A 437 -5.256 45.109 -40.511 1.00126.06 O ANISOU 2940 O LYS A 437 19413 17347 11137 281 -763 -646 O ATOM 2941 CB LYS A 437 -7.087 47.287 -41.322 1.00128.48 C ANISOU 2941 CB LYS A 437 19534 17447 11834 -69 -1707 -45 C ATOM 2942 CG LYS A 437 -7.841 46.408 -42.310 1.00133.10 C ANISOU 2942 CG LYS A 437 20671 17884 12018 23 -2385 -369 C ATOM 2943 CD LYS A 437 -7.860 47.033 -43.696 1.00139.07 C ANISOU 2943 CD LYS A 437 22008 18821 12013 181 -2674 -132 C ATOM 2944 CE LYS A 437 -8.601 46.160 -44.694 1.00145.49 C ANISOU 2944 CE LYS A 437 23438 19475 12368 280 -3431 -491 C ATOM 2945 NZ LYS A 437 -8.637 46.779 -46.049 1.00152.25 N ANISOU 2945 NZ LYS A 437 24932 20512 12403 470 -3742 -249 N ATOM 2946 N ASN A 438 -7.088 44.310 -39.472 1.00121.43 N ANISOU 2946 N ASN A 438 18408 16105 11626 -83 -1494 -996 N ATOM 2947 CA ASN A 438 -6.642 42.919 -39.488 1.00121.72 C ANISOU 2947 CA ASN A 438 18828 16055 11365 104 -1385 -1399 C ATOM 2948 C ASN A 438 -6.541 42.384 -40.914 1.00128.32 C ANISOU 2948 C ASN A 438 20465 16951 11339 354 -1700 -1613 C ATOM 2949 O ASN A 438 -7.549 42.264 -41.608 1.00133.25 O ANISOU 2949 O ASN A 438 21348 17352 11927 233 -2410 -1732 O ATOM 2950 CB ASN A 438 -7.589 42.052 -38.653 1.00119.52 C ANISOU 2950 CB ASN A 438 18302 15326 11784 -137 -1698 -1658 C ATOM 2951 CG ASN A 438 -7.144 40.600 -38.570 1.00120.06 C ANISOU 2951 CG ASN A 438 18794 15213 11609 45 -1590 -2061 C ATOM 2952 OD1 ASN A 438 -5.991 40.271 -38.845 1.00120.55 O ANISOU 2952 OD1 ASN A 438 19197 15527 11079 400 -1140 -2136 O ATOM 2953 ND2 ASN A 438 -8.064 39.724 -38.181 1.00120.39 N ANISOU 2953 ND2 ASN A 438 18801 14802 12141 -192 -1990 -2304 N ATOM 2954 N PRO A 439 -5.316 42.056 -41.355 1.00128.86 N ANISOU 2954 N PRO A 439 20930 17333 10698 729 -1177 -1665 N ATOM 2955 CA PRO A 439 -5.060 41.628 -42.736 1.00135.68 C ANISOU 2955 CA PRO A 439 22630 18317 10605 1060 -1343 -1849 C ATOM 2956 C PRO A 439 -5.492 40.190 -43.023 1.00140.04 C ANISOU 2956 C PRO A 439 23766 18465 10975 1164 -1793 -2405 C ATOM 2957 O PRO A 439 -4.882 39.532 -43.866 1.00144.48 O ANISOU 2957 O PRO A 439 25053 19128 10714 1572 -1675 -2657 O ATOM 2958 CB PRO A 439 -3.541 41.748 -42.854 1.00135.40 C ANISOU 2958 CB PRO A 439 22653 18771 10020 1438 -484 -1688 C ATOM 2959 CG PRO A 439 -3.049 41.509 -41.471 1.00129.23 C ANISOU 2959 CG PRO A 439 21242 17963 9898 1363 -28 -1687 C ATOM 2960 CD PRO A 439 -4.076 42.124 -40.561 1.00124.43 C ANISOU 2960 CD PRO A 439 20018 17067 10194 888 -381 -1533 C ATOM 2961 N VAL A 440 -6.524 39.714 -42.334 1.00139.21 N ANISOU 2961 N VAL A 440 23366 17895 11630 803 -2282 -2586 N ATOM 2962 CA VAL A 440 -7.048 38.371 -42.563 1.00143.20 C ANISOU 2962 CA VAL A 440 24402 17924 12084 793 -2794 -3096 C ATOM 2963 C VAL A 440 -8.573 38.376 -42.623 1.00142.85 C ANISOU 2963 C VAL A 440 24164 17476 12637 316 -3696 -3161 C ATOM 2964 O VAL A 440 -9.168 37.911 -43.596 1.00149.63 O ANISOU 2964 O VAL A 440 25627 18112 13113 301 -4412 -3451 O ATOM 2965 CB VAL A 440 -6.577 37.381 -41.477 1.00141.87 C ANISOU 2965 CB VAL A 440 24078 17523 12305 850 -2365 -3299 C ATOM 2966 CG1 VAL A 440 -7.355 36.078 -41.567 1.00146.73 C ANISOU 2966 CG1 VAL A 440 25145 17517 13089 691 -2985 -3771 C ATOM 2967 CG2 VAL A 440 -5.083 37.122 -41.604 1.00142.32 C ANISOU 2967 CG2 VAL A 440 24433 17950 11691 1404 -1592 -3328 C ATOM 2968 N THR A 441 -9.202 38.909 -41.581 1.00135.59 N ANISOU 2968 N THR A 441 22392 16474 12653 -58 -3665 -2892 N ATOM 2969 CA THR A 441 -10.658 38.971 -41.519 1.00136.89 C ANISOU 2969 CA THR A 441 22191 16307 13514 -507 -4438 -2892 C ATOM 2970 C THR A 441 -11.177 40.381 -41.796 1.00138.77 C ANISOU 2970 C THR A 441 22003 16811 13911 -603 -4647 -2471 C ATOM 2971 O THR A 441 -12.382 40.628 -41.727 1.00141.86 O ANISOU 2971 O THR A 441 21964 17007 14930 -928 -5252 -2395 O ATOM 2972 CB THR A 441 -11.189 38.492 -40.153 1.00129.93 C ANISOU 2972 CB THR A 441 20647 15093 13628 -852 -4289 -2887 C ATOM 2973 OG1 THR A 441 -10.628 39.297 -39.108 1.00123.04 O ANISOU 2973 OG1 THR A 441 19165 14500 13085 -795 -3539 -2534 O ATOM 2974 CG2 THR A 441 -10.822 37.035 -39.917 1.00130.03 C ANISOU 2974 CG2 THR A 441 21139 14737 13529 -788 -4198 -3294 C ATOM 2975 N SER A 442 -10.259 41.293 -42.110 1.00137.91 N ANISOU 2975 N SER A 442 22003 17137 13260 -315 -4139 -2182 N ATOM 2976 CA SER A 442 -10.597 42.684 -42.413 1.00138.00 C ANISOU 2976 CA SER A 442 21718 17377 13338 -356 -4270 -1749 C ATOM 2977 C SER A 442 -11.416 43.345 -41.307 1.00133.53 C ANISOU 2977 C SER A 442 20240 16678 13819 -665 -4269 -1491 C ATOM 2978 O SER A 442 -12.361 44.085 -41.579 1.00136.01 O ANISOU 2978 O SER A 442 20273 16949 14456 -793 -4788 -1284 O ATOM 2979 CB SER A 442 -11.330 42.789 -43.754 1.00145.64 C ANISOU 2979 CB SER A 442 23211 18305 13822 -328 -5133 -1813 C ATOM 2980 OG SER A 442 -10.516 42.330 -44.819 1.00149.93 O ANISOU 2980 OG SER A 442 24669 19019 13280 29 -5056 -2014 O ATOM 2981 N THR A 443 -11.049 43.070 -40.060 1.00127.10 N ANISOU 2981 N THR A 443 18986 15802 13504 -737 -3682 -1504 N ATOM 2982 CA THR A 443 -11.750 43.640 -38.917 1.00123.43 C ANISOU 2982 CA THR A 443 17710 15217 13970 -972 -3569 -1283 C ATOM 2983 C THR A 443 -10.912 44.714 -38.232 1.00120.13 C ANISOU 2983 C THR A 443 16993 15062 13588 -856 -2868 -953 C ATOM 2984 O THR A 443 -9.707 44.550 -38.044 1.00119.24 O ANISOU 2984 O THR A 443 17094 15153 13060 -678 -2294 -978 O ATOM 2985 CB THR A 443 -12.145 42.557 -37.894 1.00120.57 C ANISOU 2985 CB THR A 443 17054 14532 14226 -1184 -3475 -1517 C ATOM 2986 OG1 THR A 443 -10.996 41.774 -37.551 1.00117.27 O ANISOU 2986 OG1 THR A 443 16985 14162 13410 -994 -2920 -1711 O ATOM 2987 CG2 THR A 443 -13.211 41.646 -38.477 1.00127.46 C ANISOU 2987 CG2 THR A 443 18073 15070 15287 -1422 -4270 -1791 C ATOM 2988 N PHE A 444 -11.559 45.815 -37.866 1.00119.02 N ANISOU 2988 N PHE A 444 16355 14904 13965 -949 -2947 -649 N ATOM 2989 CA PHE A 444 -10.876 46.929 -37.220 1.00114.26 C ANISOU 2989 CA PHE A 444 15496 14469 13447 -879 -2382 -344 C ATOM 2990 C PHE A 444 -10.813 46.734 -35.709 1.00110.52 C ANISOU 2990 C PHE A 444 14538 13877 13576 -964 -1896 -392 C ATOM 2991 O PHE A 444 -11.836 46.763 -35.027 1.00110.30 O ANISOU 2991 O PHE A 444 14040 13632 14237 -1099 -2039 -375 O ATOM 2992 CB PHE A 444 -11.575 48.252 -37.550 1.00114.22 C ANISOU 2992 CB PHE A 444 15280 14446 13674 -883 -2697 -1 C ATOM 2993 CG PHE A 444 -11.298 48.762 -38.940 1.00116.71 C ANISOU 2993 CG PHE A 444 16135 14940 13270 -748 -2993 169 C ATOM 2994 CD1 PHE A 444 -11.755 48.076 -40.054 1.00121.34 C ANISOU 2994 CD1 PHE A 444 17161 15508 13433 -713 -3604 -20 C ATOM 2995 CD2 PHE A 444 -10.596 49.939 -39.130 1.00115.60 C ANISOU 2995 CD2 PHE A 444 16097 14960 12865 -668 -2677 529 C ATOM 2996 CE1 PHE A 444 -11.504 48.548 -41.330 1.00125.63 C ANISOU 2996 CE1 PHE A 444 18272 16226 13234 -552 -3861 151 C ATOM 2997 CE2 PHE A 444 -10.343 50.419 -40.402 1.00120.05 C ANISOU 2997 CE2 PHE A 444 17187 15686 12739 -543 -2898 741 C ATOM 2998 CZ PHE A 444 -10.798 49.722 -41.504 1.00125.05 C ANISOU 2998 CZ PHE A 444 18289 16334 12889 -460 -3478 555 C ATOM 2999 N SER A 445 -9.607 46.527 -35.191 1.00109.18 N ANISOU 2999 N SER A 445 14481 13872 13131 -865 -1317 -437 N ATOM 3000 CA SER A 445 -9.405 46.408 -33.752 1.00107.05 C ANISOU 3000 CA SER A 445 13838 13520 13316 -905 -851 -465 C ATOM 3001 C SER A 445 -8.772 47.681 -33.203 1.00105.69 C ANISOU 3001 C SER A 445 13468 13487 13203 -874 -474 -198 C ATOM 3002 O SER A 445 -7.789 48.183 -33.749 1.00105.42 O ANISOU 3002 O SER A 445 13662 13701 12691 -801 -296 -62 O ATOM 3003 CB SER A 445 -8.540 45.189 -33.421 1.00106.72 C ANISOU 3003 CB SER A 445 14041 13521 12989 -805 -532 -725 C ATOM 3004 OG SER A 445 -8.108 44.531 -34.599 1.00110.65 O ANISOU 3004 OG SER A 445 15066 14130 12846 -673 -720 -886 O ATOM 3005 N LYS A 446 -9.344 48.203 -32.123 1.00106.03 N ANISOU 3005 N LYS A 446 13097 13353 13835 -935 -345 -120 N ATOM 3006 CA LYS A 446 -8.897 49.470 -31.557 1.00106.02 C ANISOU 3006 CA LYS A 446 12948 13387 13947 -922 -73 100 C ATOM 3007 C LYS A 446 -8.261 49.300 -30.182 1.00102.83 C ANISOU 3007 C LYS A 446 12394 12980 13697 -901 404 4 C ATOM 3008 O LYS A 446 -8.505 48.311 -29.488 1.00101.86 O ANISOU 3008 O LYS A 446 12190 12762 13749 -890 524 -185 O ATOM 3009 CB LYS A 446 -10.066 50.456 -31.470 1.00109.12 C ANISOU 3009 CB LYS A 446 13060 13560 14840 -932 -334 281 C ATOM 3010 CG LYS A 446 -10.656 50.847 -32.816 1.00115.15 C ANISOU 3010 CG LYS A 446 13980 14333 15440 -923 -859 433 C ATOM 3011 CD LYS A 446 -11.871 51.748 -32.647 1.00118.16 C ANISOU 3011 CD LYS A 446 14020 14489 16387 -873 -1129 609 C ATOM 3012 CE LYS A 446 -12.978 51.044 -31.873 1.00118.92 C ANISOU 3012 CE LYS A 446 13665 14419 17099 -902 -1169 458 C ATOM 3013 NZ LYS A 446 -14.191 51.897 -31.713 1.00121.34 N ANISOU 3013 NZ LYS A 446 13561 14547 17995 -795 -1398 639 N ATOM 3014 N MET A 447 -7.442 50.277 -29.801 1.00101.65 N ANISOU 3014 N MET A 447 12235 12914 13473 -909 644 149 N ATOM 3015 CA MET A 447 -6.822 50.305 -28.482 1.00 98.29 C ANISOU 3015 CA MET A 447 11694 12481 13172 -888 1017 66 C ATOM 3016 C MET A 447 -6.320 51.710 -28.147 1.00 98.35 C ANISOU 3016 C MET A 447 11672 12453 13246 -955 1108 251 C ATOM 3017 O MET A 447 -6.011 52.498 -29.043 1.00 99.68 O ANISOU 3017 O MET A 447 11955 12690 13228 -1036 981 466 O ATOM 3018 CB MET A 447 -5.677 49.293 -28.399 1.00 96.02 C ANISOU 3018 CB MET A 447 11543 12445 12496 -824 1250 -84 C ATOM 3019 CG MET A 447 -4.461 49.645 -29.224 1.00 95.57 C ANISOU 3019 CG MET A 447 11624 12707 11982 -843 1332 50 C ATOM 3020 SD MET A 447 -3.032 48.678 -28.717 1.00101.78 S ANISOU 3020 SD MET A 447 12423 13797 12452 -702 1682 -104 S ATOM 3021 CE MET A 447 -1.779 49.289 -29.842 1.00 69.40 C ANISOU 3021 CE MET A 447 8374 10100 7893 -745 1808 140 C ATOM 3022 N SER A 448 -6.246 52.021 -26.855 1.00 97.00 N ANISOU 3022 N SER A 448 11394 12143 13319 -926 1320 172 N ATOM 3023 CA SER A 448 -5.823 53.348 -26.410 1.00 97.92 C ANISOU 3023 CA SER A 448 11534 12137 13534 -1004 1361 295 C ATOM 3024 C SER A 448 -4.493 53.340 -25.659 1.00 97.23 C ANISOU 3024 C SER A 448 11469 12216 13258 -1073 1577 220 C ATOM 3025 O SER A 448 -4.301 52.573 -24.715 1.00 96.78 O ANISOU 3025 O SER A 448 11382 12200 13192 -967 1751 24 O ATOM 3026 CB SER A 448 -6.900 53.995 -25.539 1.00 97.92 C ANISOU 3026 CB SER A 448 11446 11783 13977 -884 1365 263 C ATOM 3027 OG SER A 448 -7.979 54.465 -26.326 1.00100.45 O ANISOU 3027 OG SER A 448 11703 11946 14517 -836 1103 416 O ATOM 3028 N LEU A 449 -3.586 54.214 -26.082 1.00 97.33 N ANISOU 3028 N LEU A 449 11525 12317 13139 -1263 1545 404 N ATOM 3029 CA LEU A 449 -2.291 54.363 -25.433 1.00 95.42 C ANISOU 3029 CA LEU A 449 11229 12242 12784 -1384 1677 370 C ATOM 3030 C LEU A 449 -2.271 55.624 -24.577 1.00 96.07 C ANISOU 3030 C LEU A 449 11385 11990 13127 -1504 1599 378 C ATOM 3031 O LEU A 449 -2.400 56.735 -25.090 1.00 98.52 O ANISOU 3031 O LEU A 449 11788 12094 13553 -1663 1460 588 O ATOM 3032 CB LEU A 449 -1.177 54.430 -26.477 1.00 97.65 C ANISOU 3032 CB LEU A 449 11455 12881 12766 -1556 1726 591 C ATOM 3033 CG LEU A 449 -0.497 53.128 -26.908 1.00 97.68 C ANISOU 3033 CG LEU A 449 11385 13306 12422 -1409 1899 508 C ATOM 3034 CD1 LEU A 449 -1.505 52.012 -27.127 1.00 96.86 C ANISOU 3034 CD1 LEU A 449 11398 13132 12274 -1167 1857 322 C ATOM 3035 CD2 LEU A 449 0.316 53.365 -28.171 1.00100.46 C ANISOU 3035 CD2 LEU A 449 11720 13983 12469 -1532 1986 785 C ATOM 3036 N GLN A 450 -2.116 55.446 -23.270 1.00 94.15 N ANISOU 3036 N GLN A 450 11163 11663 12948 -1411 1675 144 N ATOM 3037 CA GLN A 450 -2.048 56.570 -22.345 1.00 94.54 C ANISOU 3037 CA GLN A 450 11367 11369 13184 -1491 1580 78 C ATOM 3038 C GLN A 450 -0.757 56.515 -21.539 1.00 93.02 C ANISOU 3038 C GLN A 450 11131 11352 12860 -1629 1560 -36 C ATOM 3039 O GLN A 450 -0.438 55.492 -20.935 1.00 92.82 O ANISOU 3039 O GLN A 450 11041 11557 12669 -1460 1674 -206 O ATOM 3040 CB GLN A 450 -3.253 56.563 -21.402 1.00 93.87 C ANISOU 3040 CB GLN A 450 11421 10955 13290 -1191 1664 -117 C ATOM 3041 CG GLN A 450 -3.180 57.598 -20.290 1.00 95.60 C ANISOU 3041 CG GLN A 450 11899 10805 13619 -1181 1595 -266 C ATOM 3042 CD GLN A 450 -3.362 59.016 -20.789 1.00 98.36 C ANISOU 3042 CD GLN A 450 12406 10788 14180 -1341 1393 -97 C ATOM 3043 OE1 GLN A 450 -4.368 59.338 -21.421 1.00 99.92 O ANISOU 3043 OE1 GLN A 450 12596 10805 14563 -1210 1374 40 O ATOM 3044 NE2 GLN A 450 -2.388 59.873 -20.506 1.00 99.69 N ANISOU 3044 NE2 GLN A 450 12716 10822 14341 -1632 1208 -95 N ATOM 3045 N LEU A 451 -0.016 57.617 -21.530 1.00 92.29 N ANISOU 3045 N LEU A 451 11074 11131 12860 -1945 1381 70 N ATOM 3046 CA LEU A 451 1.235 57.678 -20.785 1.00 91.43 C ANISOU 3046 CA LEU A 451 10871 11182 12686 -2133 1271 -26 C ATOM 3047 C LEU A 451 1.007 58.197 -19.370 1.00 90.74 C ANISOU 3047 C LEU A 451 11103 10711 12664 -2036 1128 -321 C ATOM 3048 O LEU A 451 0.284 59.172 -19.165 1.00 92.34 O ANISOU 3048 O LEU A 451 11601 10440 13044 -2022 1041 -354 O ATOM 3049 CB LEU A 451 2.251 58.560 -21.509 1.00 94.57 C ANISOU 3049 CB LEU A 451 11097 11655 13180 -2598 1135 261 C ATOM 3050 CG LEU A 451 3.680 58.473 -20.973 1.00 95.99 C ANISOU 3050 CG LEU A 451 11004 12135 13334 -2840 1009 226 C ATOM 3051 CD1 LEU A 451 4.230 57.073 -21.183 1.00 93.40 C ANISOU 3051 CD1 LEU A 451 10348 12385 12754 -2606 1225 208 C ATOM 3052 CD2 LEU A 451 4.571 59.509 -21.632 1.00101.06 C ANISOU 3052 CD2 LEU A 451 11458 12770 14169 -3371 881 550 C ATOM 3053 N TYR A 452 1.625 57.538 -18.396 1.00 88.21 N ANISOU 3053 N TYR A 452 10762 10589 12166 -1924 1101 -537 N ATOM 3054 CA TYR A 452 1.499 57.942 -17.001 1.00 89.14 C ANISOU 3054 CA TYR A 452 11249 10383 12236 -1794 957 -839 C ATOM 3055 C TYR A 452 2.860 58.223 -16.380 1.00 91.95 C ANISOU 3055 C TYR A 452 11528 10869 12538 -2074 619 -928 C ATOM 3056 O TYR A 452 3.896 58.026 -17.011 1.00 92.74 O ANISOU 3056 O TYR A 452 11205 11357 12673 -2350 550 -733 O ATOM 3057 CB TYR A 452 0.789 56.858 -16.188 1.00 87.10 C ANISOU 3057 CB TYR A 452 11143 10184 11768 -1328 1216 -1039 C ATOM 3058 CG TYR A 452 -0.677 56.688 -16.507 1.00 86.03 C ANISOU 3058 CG TYR A 452 11089 9843 11755 -1056 1509 -995 C ATOM 3059 CD1 TYR A 452 -1.631 57.521 -15.939 1.00 87.74 C ANISOU 3059 CD1 TYR A 452 11642 9600 12095 -879 1551 -1114 C ATOM 3060 CD2 TYR A 452 -1.110 55.686 -17.367 1.00 83.94 C ANISOU 3060 CD2 TYR A 452 10556 9841 11494 -961 1726 -845 C ATOM 3061 CE1 TYR A 452 -2.974 57.367 -16.222 1.00 87.11 C ANISOU 3061 CE1 TYR A 452 11536 9374 12189 -620 1815 -1048 C ATOM 3062 CE2 TYR A 452 -2.452 55.523 -17.655 1.00 83.15 C ANISOU 3062 CE2 TYR A 452 10466 9566 11563 -755 1930 -798 C ATOM 3063 CZ TYR A 452 -3.379 56.367 -17.081 1.00 85.38 C ANISOU 3063 CZ TYR A 452 10989 9437 12014 -588 1980 -882 C ATOM 3064 OH TYR A 452 -4.715 56.208 -17.367 1.00 86.49 O ANISOU 3064 OH TYR A 452 11038 9443 12380 -374 2180 -810 O ATOM 3065 N GLN A 453 2.845 58.684 -15.134 1.00 93.83 N ANISOU 3065 N GLN A 453 12174 10793 12685 -1987 403 -1225 N ATOM 3066 CA GLN A 453 4.068 58.874 -14.368 1.00 97.05 C ANISOU 3066 CA GLN A 453 12550 11309 13016 -2216 -4 -1368 C ATOM 3067 C GLN A 453 4.004 58.051 -13.086 1.00 96.59 C ANISOU 3067 C GLN A 453 12777 11333 12588 -1790 4 -1664 C ATOM 3068 O GLN A 453 3.044 58.153 -12.324 1.00 95.75 O ANISOU 3068 O GLN A 453 13169 10884 12326 -1442 155 -1873 O ATOM 3069 CB GLN A 453 4.278 60.353 -14.043 1.00102.01 C ANISOU 3069 CB GLN A 453 13503 11414 13843 -2581 -411 -1469 C ATOM 3070 CG GLN A 453 5.544 60.636 -13.249 1.00106.72 C ANISOU 3070 CG GLN A 453 14059 12083 14408 -2891 -939 -1633 C ATOM 3071 CD GLN A 453 5.819 62.117 -13.091 1.00111.66 C ANISOU 3071 CD GLN A 453 14985 12148 15293 -3356 -1387 -1705 C ATOM 3072 OE1 GLN A 453 5.156 62.953 -13.704 1.00112.46 O ANISOU 3072 OE1 GLN A 453 15283 11827 15619 -3465 -1279 -1575 O ATOM 3073 NE2 GLN A 453 6.804 62.451 -12.265 1.00116.28 N ANISOU 3073 NE2 GLN A 453 15626 12697 15857 -3635 -1935 -1911 N ATOM 3074 N VAL A 454 5.023 57.230 -12.855 1.00 98.03 N ANISOU 3074 N VAL A 454 12644 11981 12622 -1784 -133 -1655 N ATOM 3075 CA VAL A 454 5.059 56.374 -11.674 1.00 98.43 C ANISOU 3075 CA VAL A 454 12977 12138 12284 -1367 -147 -1886 C ATOM 3076 C VAL A 454 5.977 56.938 -10.594 1.00104.93 C ANISOU 3076 C VAL A 454 14021 12875 12972 -1519 -730 -2136 C ATOM 3077 O VAL A 454 5.523 57.303 -9.510 1.00106.54 O ANISOU 3077 O VAL A 454 14856 12713 12913 -1297 -845 -2430 O ATOM 3078 CB VAL A 454 5.517 54.948 -12.022 1.00 94.50 C ANISOU 3078 CB VAL A 454 12063 12185 11658 -1142 64 -1732 C ATOM 3079 CG1 VAL A 454 5.638 54.110 -10.760 1.00 94.66 C ANISOU 3079 CG1 VAL A 454 12420 12283 11264 -719 1 -1935 C ATOM 3080 CG2 VAL A 454 4.549 54.311 -13.000 1.00 89.02 C ANISOU 3080 CG2 VAL A 454 11245 11526 11051 -976 581 -1542 C ATOM 3081 N ASP A 455 7.271 56.999 -10.897 1.00109.33 N ANISOU 3081 N ASP A 455 14053 13784 13704 -1886 -1100 -2018 N ATOM 3082 CA ASP A 455 8.254 57.534 -9.964 1.00116.28 C ANISOU 3082 CA ASP A 455 15033 14621 14526 -2114 -1760 -2236 C ATOM 3083 C ASP A 455 8.465 59.019 -10.212 1.00122.52 C ANISOU 3083 C ASP A 455 15890 14985 15678 -2697 -2129 -2252 C ATOM 3084 O ASP A 455 7.704 59.651 -10.943 1.00119.94 O ANISOU 3084 O ASP A 455 15669 14330 15572 -2823 -1847 -2127 O ATOM 3085 CB ASP A 455 9.591 56.798 -10.101 1.00117.46 C ANISOU 3085 CB ASP A 455 14492 15404 14733 -2205 -2005 -2083 C ATOM 3086 CG ASP A 455 9.506 55.341 -9.682 1.00115.84 C ANISOU 3086 CG ASP A 455 14319 15554 14141 -1601 -1746 -2099 C ATOM 3087 OD1 ASP A 455 9.611 55.066 -8.468 1.00118.97 O ANISOU 3087 OD1 ASP A 455 15161 15889 14153 -1301 -2036 -2353 O ATOM 3088 OD2 ASP A 455 9.339 54.470 -10.564 1.00111.24 O ANISOU 3088 OD2 ASP A 455 13368 15283 13614 -1420 -1268 -1857 O ATOM 3089 N SER A 456 9.507 59.570 -9.599 1.00131.96 N ANISOU 3089 N SER A 456 17029 16163 16947 -3061 -2799 -2398 N ATOM 3090 CA SER A 456 9.882 60.958 -9.826 1.00137.81 C ANISOU 3090 CA SER A 456 17794 16481 18086 -3709 -3229 -2393 C ATOM 3091 C SER A 456 10.758 61.060 -11.069 1.00137.29 C ANISOU 3091 C SER A 456 16821 16821 18521 -4254 -3171 -1937 C ATOM 3092 O SER A 456 11.131 62.153 -11.493 1.00140.80 O ANISOU 3092 O SER A 456 17153 16968 19376 -4871 -3440 -1807 O ATOM 3093 CB SER A 456 10.616 61.520 -8.607 1.00145.97 C ANISOU 3093 CB SER A 456 19183 17282 18998 -3913 -4040 -2767 C ATOM 3094 OG SER A 456 11.719 60.704 -8.253 1.00147.97 O ANISOU 3094 OG SER A 456 18895 18147 19181 -3893 -4371 -2733 O ATOM 3095 N ARG A 457 11.077 59.908 -11.650 1.00133.41 N ANISOU 3095 N ARG A 457 15720 16991 17979 -4005 -2787 -1685 N ATOM 3096 CA ARG A 457 11.927 59.842 -12.832 1.00135.00 C ANISOU 3096 CA ARG A 457 15046 17677 18573 -4405 -2622 -1240 C ATOM 3097 C ARG A 457 11.618 58.602 -13.673 1.00128.97 C ANISOU 3097 C ARG A 457 13948 17421 17634 -3933 -1952 -1010 C ATOM 3098 O ARG A 457 12.487 58.084 -14.374 1.00130.90 O ANISOU 3098 O ARG A 457 13454 18250 18031 -4019 -1801 -717 O ATOM 3099 CB ARG A 457 13.404 59.867 -12.424 1.00142.88 C ANISOU 3099 CB ARG A 457 15417 19076 19797 -4774 -3199 -1208 C ATOM 3100 CG ARG A 457 13.719 59.035 -11.186 1.00144.98 C ANISOU 3100 CG ARG A 457 15854 19561 19670 -4306 -3559 -1539 C ATOM 3101 CD ARG A 457 14.479 57.761 -11.529 1.00145.11 C ANISOU 3101 CD ARG A 457 15123 20370 19644 -3972 -3330 -1317 C ATOM 3102 NE ARG A 457 15.924 57.974 -11.577 1.00153.19 N ANISOU 3102 NE ARG A 457 15285 21843 21076 -4434 -3804 -1136 N ATOM 3103 CZ ARG A 457 16.613 58.212 -12.689 1.00155.44 C ANISOU 3103 CZ ARG A 457 14739 22497 21825 -4870 -3566 -707 C ATOM 3104 NH1 ARG A 457 15.992 58.271 -13.859 1.00150.62 N ANISOU 3104 NH1 ARG A 457 14122 21840 21266 -4886 -2890 -429 N ATOM 3105 NH2 ARG A 457 17.926 58.391 -12.631 1.00163.10 N ANISOU 3105 NH2 ARG A 457 14871 23898 23202 -5284 -4005 -537 N ATOM 3106 N THR A 458 10.374 58.135 -13.598 1.00122.18 N ANISOU 3106 N THR A 458 13635 16322 16465 -3433 -1553 -1147 N ATOM 3107 CA THR A 458 9.941 56.959 -14.350 1.00115.15 C ANISOU 3107 CA THR A 458 12551 15801 15398 -2994 -970 -981 C ATOM 3108 C THR A 458 8.505 57.116 -14.849 1.00109.67 C ANISOU 3108 C THR A 458 12320 14703 14648 -2810 -553 -972 C ATOM 3109 O THR A 458 7.609 57.480 -14.085 1.00108.28 O ANISOU 3109 O THR A 458 12756 14045 14342 -2629 -605 -1229 O ATOM 3110 CB THR A 458 10.036 55.679 -13.495 1.00112.72 C ANISOU 3110 CB THR A 458 12340 15776 14713 -2424 -954 -1179 C ATOM 3111 OG1 THR A 458 11.375 55.522 -13.008 1.00118.08 O ANISOU 3111 OG1 THR A 458 12559 16853 15453 -2547 -1398 -1184 O ATOM 3112 CG2 THR A 458 9.648 54.456 -14.311 1.00107.59 C ANISOU 3112 CG2 THR A 458 11512 15453 13915 -2013 -392 -1015 C ATOM 3113 N TYR A 459 8.291 56.837 -16.132 1.00106.08 N ANISOU 3113 N TYR A 459 11566 14462 14278 -2829 -145 -674 N ATOM 3114 CA TYR A 459 6.965 56.941 -16.732 1.00100.10 C ANISOU 3114 CA TYR A 459 11154 13378 13499 -2665 198 -630 C ATOM 3115 C TYR A 459 6.426 55.573 -17.143 1.00 94.41 C ANISOU 3115 C TYR A 459 10390 12943 12538 -2191 615 -612 C ATOM 3116 O TYR A 459 7.191 54.626 -17.317 1.00 93.88 O ANISOU 3116 O TYR A 459 9964 13356 12350 -2036 703 -552 O ATOM 3117 CB TYR A 459 6.992 57.886 -17.935 1.00101.89 C ANISOU 3117 CB TYR A 459 11208 13504 14002 -3102 263 -299 C ATOM 3118 CG TYR A 459 7.332 59.319 -17.582 1.00108.54 C ANISOU 3118 CG TYR A 459 12202 13912 15126 -3602 -143 -304 C ATOM 3119 CD1 TYR A 459 6.355 60.189 -17.110 1.00109.15 C ANISOU 3119 CD1 TYR A 459 12878 13339 15256 -3563 -262 -488 C ATOM 3120 CD2 TYR A 459 8.628 59.802 -17.716 1.00113.32 C ANISOU 3120 CD2 TYR A 459 12346 14739 15971 -4111 -409 -122 C ATOM 3121 CE1 TYR A 459 6.660 61.500 -16.785 1.00113.37 C ANISOU 3121 CE1 TYR A 459 13636 13397 16042 -4007 -661 -522 C ATOM 3122 CE2 TYR A 459 8.941 61.111 -17.394 1.00117.62 C ANISOU 3122 CE2 TYR A 459 13058 14821 16810 -4628 -825 -130 C ATOM 3123 CZ TYR A 459 7.953 61.954 -16.930 1.00117.82 C ANISOU 3123 CZ TYR A 459 13771 14145 16850 -4568 -963 -345 C ATOM 3124 OH TYR A 459 8.258 63.257 -16.607 1.00123.91 O ANISOU 3124 OH TYR A 459 14793 14380 17907 -5068 -1402 -381 O ATOM 3125 N LEU A 460 5.107 55.480 -17.298 1.00 90.41 N ANISOU 3125 N LEU A 460 10241 12120 11992 -1960 851 -665 N ATOM 3126 CA LEU A 460 4.443 54.219 -17.623 1.00 84.14 C ANISOU 3126 CA LEU A 460 9469 11487 11014 -1558 1196 -674 C ATOM 3127 C LEU A 460 3.530 54.379 -18.837 1.00 81.59 C ANISOU 3127 C LEU A 460 9156 11048 10796 -1600 1413 -487 C ATOM 3128 O LEU A 460 2.639 55.228 -18.844 1.00 81.32 O ANISOU 3128 O LEU A 460 9372 10603 10923 -1670 1379 -491 O ATOM 3129 CB LEU A 460 3.628 53.734 -16.418 1.00 80.70 C ANISOU 3129 CB LEU A 460 9453 10791 10418 -1187 1258 -939 C ATOM 3130 CG LEU A 460 3.117 52.289 -16.308 1.00 76.85 C ANISOU 3130 CG LEU A 460 9035 10433 9733 -778 1553 -987 C ATOM 3131 CD1 LEU A 460 1.928 52.001 -17.221 1.00 74.02 C ANISOU 3131 CD1 LEU A 460 8702 9935 9488 -713 1823 -884 C ATOM 3132 CD2 LEU A 460 4.234 51.299 -16.562 1.00 77.25 C ANISOU 3132 CD2 LEU A 460 8767 10961 9624 -671 1552 -928 C ATOM 3133 N LEU A 461 3.753 53.559 -19.859 1.00 80.24 N ANISOU 3133 N LEU A 461 8742 11233 10513 -1520 1616 -336 N ATOM 3134 CA LEU A 461 2.879 53.540 -21.027 1.00 79.02 C ANISOU 3134 CA LEU A 461 8641 11000 10384 -1512 1773 -184 C ATOM 3135 C LEU A 461 1.797 52.481 -20.856 1.00 78.04 C ANISOU 3135 C LEU A 461 8715 10758 10177 -1158 1939 -337 C ATOM 3136 O LEU A 461 2.093 51.289 -20.752 1.00 78.13 O ANISOU 3136 O LEU A 461 8683 11003 10000 -917 2062 -422 O ATOM 3137 CB LEU A 461 3.677 53.270 -22.303 1.00 79.52 C ANISOU 3137 CB LEU A 461 8407 11490 10316 -1612 1901 59 C ATOM 3138 CG LEU A 461 2.859 53.159 -23.594 1.00 76.80 C ANISOU 3138 CG LEU A 461 8174 11108 9898 -1575 2020 208 C ATOM 3139 CD1 LEU A 461 2.157 54.472 -23.907 1.00 77.54 C ANISOU 3139 CD1 LEU A 461 8428 10816 10216 -1826 1872 361 C ATOM 3140 CD2 LEU A 461 3.733 52.724 -24.762 1.00 77.42 C ANISOU 3140 CD2 LEU A 461 8028 11655 9733 -1578 2206 411 C ATOM 3141 N ASP A 462 0.543 52.920 -20.831 1.00 78.75 N ANISOU 3141 N ASP A 462 9008 10473 10442 -1129 1940 -357 N ATOM 3142 CA ASP A 462 -0.577 52.021 -20.571 1.00 78.91 C ANISOU 3142 CA ASP A 462 9160 10342 10479 -858 2092 -475 C ATOM 3143 C ASP A 462 -1.323 51.616 -21.838 1.00 80.02 C ANISOU 3143 C ASP A 462 9252 10507 10646 -852 2118 -358 C ATOM 3144 O ASP A 462 -1.644 52.456 -22.679 1.00 82.02 O ANISOU 3144 O ASP A 462 9488 10672 11005 -1013 2004 -194 O ATOM 3145 CB ASP A 462 -1.551 52.658 -19.582 1.00 79.18 C ANISOU 3145 CB ASP A 462 9399 9972 10713 -768 2109 -584 C ATOM 3146 CG ASP A 462 -2.786 51.813 -19.362 1.00 78.77 C ANISOU 3146 CG ASP A 462 9398 9772 10760 -538 2308 -642 C ATOM 3147 OD1 ASP A 462 -2.659 50.570 -19.334 1.00 78.45 O ANISOU 3147 OD1 ASP A 462 9341 9894 10574 -410 2427 -689 O ATOM 3148 OD2 ASP A 462 -3.883 52.394 -19.223 1.00 79.21 O ANISOU 3148 OD2 ASP A 462 9493 9537 11065 -483 2347 -625 O ATOM 3149 N PHE A 463 -1.610 50.323 -21.954 1.00 79.05 N ANISOU 3149 N PHE A 463 9152 10467 10415 -664 2233 -445 N ATOM 3150 CA PHE A 463 -2.316 49.786 -23.111 1.00 78.60 C ANISOU 3150 CA PHE A 463 9100 10413 10352 -656 2192 -388 C ATOM 3151 C PHE A 463 -3.738 49.404 -22.730 1.00 77.63 C ANISOU 3151 C PHE A 463 9014 9979 10502 -570 2220 -455 C ATOM 3152 O PHE A 463 -3.949 48.503 -21.925 1.00 76.03 O ANISOU 3152 O PHE A 463 8873 9704 10311 -427 2375 -573 O ATOM 3153 CB PHE A 463 -1.593 48.557 -23.659 1.00 78.74 C ANISOU 3153 CB PHE A 463 9145 10717 10056 -523 2267 -448 C ATOM 3154 CG PHE A 463 -0.192 48.828 -24.122 1.00 80.17 C ANISOU 3154 CG PHE A 463 9202 11274 9987 -571 2302 -349 C ATOM 3155 CD1 PHE A 463 0.839 48.987 -23.210 1.00 80.78 C ANISOU 3155 CD1 PHE A 463 9155 11509 10030 -555 2350 -380 C ATOM 3156 CD2 PHE A 463 0.098 48.901 -25.473 1.00 82.36 C ANISOU 3156 CD2 PHE A 463 9472 11766 10054 -625 2289 -211 C ATOM 3157 CE1 PHE A 463 2.127 49.230 -23.637 1.00 83.35 C ANISOU 3157 CE1 PHE A 463 9259 12212 10196 -624 2388 -258 C ATOM 3158 CE2 PHE A 463 1.385 49.140 -25.906 1.00 84.90 C ANISOU 3158 CE2 PHE A 463 9622 12470 10166 -666 2399 -76 C ATOM 3159 CZ PHE A 463 2.402 49.306 -24.987 1.00 85.27 C ANISOU 3159 CZ PHE A 463 9453 12685 10261 -681 2452 -90 C ATOM 3160 N ARG A 464 -4.712 50.094 -23.310 1.00 81.65 N ANISOU 3160 N ARG A 464 9463 10309 11250 -655 2076 -348 N ATOM 3161 CA ARG A 464 -6.112 49.816 -23.028 1.00 86.57 C ANISOU 3161 CA ARG A 464 10007 10672 12214 -590 2096 -370 C ATOM 3162 C ARG A 464 -6.767 49.219 -24.266 1.00 90.64 C ANISOU 3162 C ARG A 464 10479 11206 12755 -654 1871 -330 C ATOM 3163 O ARG A 464 -6.273 49.391 -25.374 1.00 90.29 O ANISOU 3163 O ARG A 464 10513 11334 12460 -727 1693 -257 O ATOM 3164 CB ARG A 464 -6.830 51.099 -22.608 1.00 89.09 C ANISOU 3164 CB ARG A 464 10258 10747 12846 -573 2079 -291 C ATOM 3165 CG ARG A 464 -8.139 50.871 -21.877 1.00 92.09 C ANISOU 3165 CG ARG A 464 10496 10894 13602 -438 2240 -315 C ATOM 3166 CD ARG A 464 -8.628 52.141 -21.195 1.00 97.23 C ANISOU 3166 CD ARG A 464 11146 11308 14487 -316 2316 -285 C ATOM 3167 NE ARG A 464 -9.221 53.103 -22.122 1.00102.00 N ANISOU 3167 NE ARG A 464 11644 11801 15309 -350 2047 -127 N ATOM 3168 CZ ARG A 464 -8.620 54.212 -22.543 1.00103.75 C ANISOU 3168 CZ ARG A 464 12022 11976 15424 -435 1867 -41 C ATOM 3169 NH1 ARG A 464 -7.397 54.511 -22.123 1.00102.54 N ANISOU 3169 NH1 ARG A 464 12078 11894 14988 -536 1913 -108 N ATOM 3170 NH2 ARG A 464 -9.245 55.025 -23.385 1.00106.37 N ANISOU 3170 NH2 ARG A 464 12290 12174 15951 -431 1619 134 N ATOM 3171 N SER A 465 -7.873 48.510 -24.076 1.00 95.79 N ANISOU 3171 N SER A 465 11016 11679 13701 -638 1874 -370 N ATOM 3172 CA SER A 465 -8.586 47.907 -25.194 1.00101.75 C ANISOU 3172 CA SER A 465 11734 12406 14520 -731 1574 -364 C ATOM 3173 C SER A 465 -9.948 48.561 -25.403 1.00109.75 C ANISOU 3173 C SER A 465 12464 13233 16003 -768 1379 -238 C ATOM 3174 O SER A 465 -10.659 48.863 -24.444 1.00110.25 O ANISOU 3174 O SER A 465 12313 13136 16441 -694 1592 -202 O ATOM 3175 CB SER A 465 -8.753 46.404 -24.973 1.00100.61 C ANISOU 3175 CB SER A 465 11664 12185 14377 -739 1647 -507 C ATOM 3176 OG SER A 465 -9.524 45.825 -26.010 1.00102.45 O ANISOU 3176 OG SER A 465 11882 12336 14710 -864 1289 -533 O ATOM 3177 N ILE A 466 -10.307 48.779 -26.664 1.00116.88 N ANISOU 3177 N ILE A 466 13372 14173 16863 -843 979 -163 N ATOM 3178 CA ILE A 466 -11.582 49.402 -26.991 1.00124.68 C ANISOU 3178 CA ILE A 466 14063 15012 18298 -847 709 -25 C ATOM 3179 C ILE A 466 -12.480 48.466 -27.785 1.00132.49 C ANISOU 3179 C ILE A 466 14935 15947 19459 -981 322 -75 C ATOM 3180 O ILE A 466 -12.138 48.056 -28.894 1.00134.88 O ANISOU 3180 O ILE A 466 15512 16353 19383 -1048 -2 -134 O ATOM 3181 CB ILE A 466 -11.395 50.691 -27.809 1.00126.68 C ANISOU 3181 CB ILE A 466 14418 15307 18406 -810 464 157 C ATOM 3182 CG1 ILE A 466 -10.573 51.712 -27.024 1.00124.08 C ANISOU 3182 CG1 ILE A 466 14203 14961 17982 -736 781 207 C ATOM 3183 CG2 ILE A 466 -12.746 51.278 -28.186 1.00131.37 C ANISOU 3183 CG2 ILE A 466 14696 15747 19471 -757 134 307 C ATOM 3184 CD1 ILE A 466 -10.462 53.047 -27.718 1.00125.69 C ANISOU 3184 CD1 ILE A 466 14519 15115 18122 -725 565 424 C ATOM 3185 N ASP A 467 -13.631 48.132 -27.211 1.00138.26 N ANISOU 3185 N ASP A 467 15263 16512 20760 -1023 357 -49 N ATOM 3186 CA ASP A 467 -14.636 47.354 -27.920 1.00145.90 C ANISOU 3186 CA ASP A 467 16021 17390 22026 -1207 -84 -73 C ATOM 3187 C ASP A 467 -15.543 48.302 -28.692 1.00151.83 C ANISOU 3187 C ASP A 467 16490 18137 23061 -1159 -541 104 C ATOM 3188 O ASP A 467 -15.759 49.441 -28.276 1.00151.48 O ANISOU 3188 O ASP A 467 16261 18074 23221 -967 -381 262 O ATOM 3189 CB ASP A 467 -15.457 46.512 -26.943 1.00149.27 C ANISOU 3189 CB ASP A 467 16073 17646 22995 -1322 185 -78 C ATOM 3190 CG ASP A 467 -16.451 45.606 -27.646 1.00156.10 C ANISOU 3190 CG ASP A 467 16702 18385 24223 -1598 -308 -112 C ATOM 3191 OD1 ASP A 467 -16.139 45.132 -28.759 1.00158.04 O ANISOU 3191 OD1 ASP A 467 17305 18652 24091 -1705 -784 -255 O ATOM 3192 OD2 ASP A 467 -17.544 45.369 -27.087 1.00159.68 O ANISOU 3192 OD2 ASP A 467 16616 18718 25338 -1712 -220 6 O ATOM 3193 N ASP A 468 -16.067 47.835 -29.820 1.00158.24 N ANISOU 3193 N ASP A 468 17313 18944 23866 -1310 -1145 67 N ATOM 3194 CA ASP A 468 -16.947 48.656 -30.643 1.00164.41 C ANISOU 3194 CA ASP A 468 17847 19732 24890 -1248 -1680 242 C ATOM 3195 C ASP A 468 -18.195 47.902 -31.095 1.00170.36 C ANISOU 3195 C ASP A 468 18182 20389 26159 -1470 -2222 219 C ATOM 3196 O ASP A 468 -18.126 47.011 -31.941 1.00172.00 O ANISOU 3196 O ASP A 468 18686 20576 26092 -1668 -2673 43 O ATOM 3197 CB ASP A 468 -16.191 49.211 -31.855 1.00165.73 C ANISOU 3197 CB ASP A 468 18559 20038 24374 -1165 -2020 277 C ATOM 3198 CG ASP A 468 -15.256 48.193 -32.480 1.00165.72 C ANISOU 3198 CG ASP A 468 19125 20126 23716 -1278 -2078 44 C ATOM 3199 OD1 ASP A 468 -15.315 47.006 -32.095 1.00165.77 O ANISOU 3199 OD1 ASP A 468 19115 20037 23834 -1438 -1985 -160 O ATOM 3200 OD2 ASP A 468 -14.462 48.581 -33.362 1.00165.71 O ANISOU 3200 OD2 ASP A 468 19603 20279 23082 -1188 -2193 80 O ATOM 3201 N GLU A 469 -19.337 48.267 -30.521 1.00173.76 N ANISOU 3201 N GLU A 469 17918 20756 27348 -1428 -2180 393 N ATOM 3202 CA GLU A 469 -20.611 47.688 -30.926 1.00180.65 C ANISOU 3202 CA GLU A 469 18241 21559 28839 -1660 -2726 425 C ATOM 3203 C GLU A 469 -21.295 48.603 -31.935 1.00185.39 C ANISOU 3203 C GLU A 469 18655 22233 29553 -1503 -3413 596 C ATOM 3204 O GLU A 469 -21.292 49.824 -31.777 1.00184.21 O ANISOU 3204 O GLU A 469 18435 22125 29430 -1168 -3251 790 O ATOM 3205 CB GLU A 469 -21.519 47.473 -29.714 1.00182.85 C ANISOU 3205 CB GLU A 469 17769 21763 29943 -1707 -2249 558 C ATOM 3206 CG GLU A 469 -22.772 46.665 -30.020 1.00190.52 C ANISOU 3206 CG GLU A 469 18099 22655 31633 -2054 -2753 598 C ATOM 3207 CD GLU A 469 -23.812 46.759 -28.921 1.00194.39 C ANISOU 3207 CD GLU A 469 17707 23138 33014 -2026 -2263 834 C ATOM 3208 OE1 GLU A 469 -24.069 47.883 -28.440 1.00194.59 O ANISOU 3208 OE1 GLU A 469 17437 23256 33241 -1623 -1928 1022 O ATOM 3209 OE2 GLU A 469 -24.371 45.710 -28.537 1.00197.78 O ANISOU 3209 OE2 GLU A 469 17757 23452 33938 -2399 -2190 843 O ATOM 3210 N ILE A 470 -21.877 48.010 -32.972 1.00190.55 N ANISOU 3210 N ILE A 470 19274 22869 30257 -1736 -4217 519 N ATOM 3211 CA ILE A 470 -22.538 48.778 -34.021 1.00194.74 C ANISOU 3211 CA ILE A 470 19678 23473 30841 -1586 -4985 678 C ATOM 3212 C ILE A 470 -24.056 48.650 -33.932 1.00201.04 C ANISOU 3212 C ILE A 470 19513 24249 32622 -1704 -5416 826 C ATOM 3213 O ILE A 470 -24.707 49.366 -33.171 1.00201.23 O ANISOU 3213 O ILE A 470 18871 24303 33284 -1467 -5059 1062 O ATOM 3214 CB ILE A 470 -22.072 48.332 -35.420 1.00195.89 C ANISOU 3214 CB ILE A 470 20564 23648 30218 -1705 -5704 490 C ATOM 3215 CG1 ILE A 470 -20.544 48.366 -35.509 1.00189.04 C ANISOU 3215 CG1 ILE A 470 20571 22844 28410 -1593 -5212 362 C ATOM 3216 CG2 ILE A 470 -22.701 49.204 -36.496 1.00200.65 C ANISOU 3216 CG2 ILE A 470 21121 24332 30785 -1501 -6501 689 C ATOM 3217 CD1 ILE A 470 -19.994 47.861 -36.826 1.00191.11 C ANISOU 3217 CD1 ILE A 470 21622 23155 27834 -1654 -5772 164 C TER 3218 ILE A 470 ATOM 3219 N LYS B 203 1.739 71.397 -17.853 1.00139.26 N ANISOU 3219 N LYS B 203 23063 15491 14359 -4116 2383 810 N ATOM 3220 CA LYS B 203 1.065 70.176 -18.277 1.00134.42 C ANISOU 3220 CA LYS B 203 21855 15463 13756 -3873 2218 965 C ATOM 3221 C LYS B 203 2.014 68.986 -18.319 1.00130.87 C ANISOU 3221 C LYS B 203 20335 15209 14181 -4354 2331 372 C ATOM 3222 O LYS B 203 2.858 68.878 -19.207 1.00134.68 O ANISOU 3222 O LYS B 203 20717 15562 14893 -5104 2873 -72 O ATOM 3223 CB LYS B 203 0.406 70.368 -19.644 1.00138.17 C ANISOU 3223 CB LYS B 203 23011 16011 13477 -3976 2555 1276 C ATOM 3224 CG LYS B 203 -0.960 71.027 -19.589 1.00138.29 C ANISOU 3224 CG LYS B 203 23807 16129 12607 -3173 2199 1923 C ATOM 3225 CD LYS B 203 -2.002 70.100 -18.983 1.00132.17 C ANISOU 3225 CD LYS B 203 22370 16007 11840 -2450 1641 2189 C ATOM 3226 CE LYS B 203 -3.388 70.722 -19.048 1.00131.48 C ANISOU 3226 CE LYS B 203 22980 16119 10857 -1661 1310 2727 C ATOM 3227 NZ LYS B 203 -4.447 69.791 -18.576 1.00126.07 N ANISOU 3227 NZ LYS B 203 21638 16139 10122 -1057 854 2916 N ATOM 3228 N SER B 204 1.863 68.097 -17.345 1.00124.56 N ANISOU 3228 N SER B 204 18774 14710 13842 -3913 1808 343 N ATOM 3229 CA SER B 204 2.639 66.868 -17.282 1.00124.00 C ANISOU 3229 CA SER B 204 17710 14835 14570 -4199 1776 -187 C ATOM 3230 C SER B 204 1.689 65.689 -17.458 1.00121.75 C ANISOU 3230 C SER B 204 17034 15083 14142 -3811 1506 124 C ATOM 3231 O SER B 204 0.509 65.794 -17.121 1.00121.19 O ANISOU 3231 O SER B 204 17279 15251 13518 -3209 1180 677 O ATOM 3232 CB SER B 204 3.354 66.777 -15.932 1.00123.58 C ANISOU 3232 CB SER B 204 17161 14613 15182 -4016 1352 -535 C ATOM 3233 OG SER B 204 4.031 65.543 -15.778 1.00122.98 O ANISOU 3233 OG SER B 204 16161 14716 15848 -4148 1197 -1040 O ATOM 3234 N PRO B 205 2.190 64.568 -18.008 1.00117.35 N ANISOU 3234 N PRO B 205 15789 14731 14067 -4172 1659 -270 N ATOM 3235 CA PRO B 205 1.372 63.353 -18.090 1.00110.43 C ANISOU 3235 CA PRO B 205 14503 14338 13117 -3850 1400 -35 C ATOM 3236 C PRO B 205 0.859 62.955 -16.709 1.00106.97 C ANISOU 3236 C PRO B 205 13862 14011 12769 -3205 745 186 C ATOM 3237 O PRO B 205 1.614 63.020 -15.738 1.00107.93 O ANISOU 3237 O PRO B 205 13734 13860 13414 -3143 465 -122 O ATOM 3238 CB PRO B 205 2.348 62.301 -18.637 1.00110.07 C ANISOU 3238 CB PRO B 205 13704 14347 13772 -4367 1619 -656 C ATOM 3239 CG PRO B 205 3.714 62.907 -18.495 1.00113.73 C ANISOU 3239 CG PRO B 205 14032 14391 14789 -4847 1851 -1282 C ATOM 3240 CD PRO B 205 3.511 64.377 -18.625 1.00118.19 C ANISOU 3240 CD PRO B 205 15474 14654 14781 -4919 2109 -987 C ATOM 3241 N PRO B 206 -0.418 62.557 -16.626 1.00101.85 N ANISOU 3241 N PRO B 206 13335 13776 11589 -2751 512 683 N ATOM 3242 CA PRO B 206 -1.110 62.333 -15.352 1.00 98.59 C ANISOU 3242 CA PRO B 206 12891 13498 11072 -2165 -50 959 C ATOM 3243 C PRO B 206 -0.472 61.229 -14.517 1.00 97.53 C ANISOU 3243 C PRO B 206 12141 13291 11625 -2147 -415 608 C ATOM 3244 O PRO B 206 0.069 60.271 -15.065 1.00 97.52 O ANISOU 3244 O PRO B 206 11661 13345 12046 -2470 -282 261 O ATOM 3245 CB PRO B 206 -2.521 61.927 -15.788 1.00 74.32 C ANISOU 3245 CB PRO B 206 9946 10976 7316 -1874 -69 1406 C ATOM 3246 CG PRO B 206 -2.354 61.395 -17.164 1.00 75.35 C ANISOU 3246 CG PRO B 206 9897 11277 7456 -2331 385 1254 C ATOM 3247 CD PRO B 206 -1.260 62.207 -17.781 1.00101.12 C ANISOU 3247 CD PRO B 206 13361 14091 10971 -2821 795 942 C ATOM 3248 N ILE B 207 -0.533 61.382 -13.198 1.00 74.23 N ANISOU 3248 N ILE B 207 9248 10194 8763 -1752 -892 688 N ATOM 3249 CA ILE B 207 0.004 60.389 -12.281 1.00 83.90 C ANISOU 3249 CA ILE B 207 10033 11295 10551 -1642 -1331 396 C ATOM 3250 C ILE B 207 -0.806 59.105 -12.418 1.00 81.49 C ANISOU 3250 C ILE B 207 9536 11381 10045 -1551 -1447 576 C ATOM 3251 O ILE B 207 -2.028 59.148 -12.560 1.00 80.77 O ANISOU 3251 O ILE B 207 9706 11684 9301 -1355 -1402 1020 O ATOM 3252 CB ILE B 207 -0.039 60.889 -10.818 1.00 72.88 C ANISOU 3252 CB ILE B 207 8857 9672 9163 -1215 -1825 513 C ATOM 3253 CG1 ILE B 207 0.668 62.239 -10.682 1.00 75.49 C ANISOU 3253 CG1 ILE B 207 9435 9628 9619 -1315 -1680 362 C ATOM 3254 CG2 ILE B 207 0.587 59.875 -9.878 1.00 72.81 C ANISOU 3254 CG2 ILE B 207 8483 9469 9714 -1082 -2320 188 C ATOM 3255 CD1 ILE B 207 -0.273 63.434 -10.698 1.00 77.86 C ANISOU 3255 CD1 ILE B 207 10373 10011 9201 -1072 -1564 865 C ATOM 3256 N LEU B 208 -0.120 57.966 -12.392 1.00 80.53 N ANISOU 3256 N LEU B 208 8962 11160 10476 -1696 -1593 186 N ATOM 3257 CA LEU B 208 -0.776 56.671 -12.533 1.00 77.47 C ANISOU 3257 CA LEU B 208 8424 11076 9936 -1673 -1683 302 C ATOM 3258 C LEU B 208 -1.657 56.364 -11.329 1.00 76.23 C ANISOU 3258 C LEU B 208 8549 11010 9406 -1269 -2134 649 C ATOM 3259 O LEU B 208 -1.183 56.352 -10.193 1.00 77.61 O ANISOU 3259 O LEU B 208 8783 10841 9866 -1033 -2585 526 O ATOM 3260 CB LEU B 208 0.260 55.559 -12.709 1.00 78.47 C ANISOU 3260 CB LEU B 208 8061 10988 10768 -1875 -1793 -243 C ATOM 3261 CG LEU B 208 -0.288 54.137 -12.864 1.00 75.18 C ANISOU 3261 CG LEU B 208 7527 10798 10242 -1891 -1888 -178 C ATOM 3262 CD1 LEU B 208 -0.902 53.943 -14.240 1.00 73.32 C ANISOU 3262 CD1 LEU B 208 7201 11005 9653 -2220 -1341 -29 C ATOM 3263 CD2 LEU B 208 0.798 53.107 -12.612 1.00 71.87 C ANISOU 3263 CD2 LEU B 208 6736 10030 10543 -1905 -2213 -732 C ATOM 3264 N PRO B 209 -2.949 56.113 -11.579 1.00 74.39 N ANISOU 3264 N PRO B 209 8490 11262 8514 -1208 -2003 1046 N ATOM 3265 CA PRO B 209 -3.911 55.758 -10.531 1.00 73.39 C ANISOU 3265 CA PRO B 209 8623 11314 7948 -924 -2336 1339 C ATOM 3266 C PRO B 209 -3.588 54.403 -9.907 1.00 74.48 C ANISOU 3266 C PRO B 209 8672 11234 8392 -955 -2685 1143 C ATOM 3267 O PRO B 209 -3.312 53.446 -10.629 1.00 75.38 O ANISOU 3267 O PRO B 209 8520 11384 8738 -1211 -2539 935 O ATOM 3268 CB PRO B 209 -5.240 55.696 -11.286 1.00 72.75 C ANISOU 3268 CB PRO B 209 8605 11878 7160 -967 -2002 1652 C ATOM 3269 CG PRO B 209 -4.857 55.436 -12.698 1.00 74.61 C ANISOU 3269 CG PRO B 209 8553 12215 7582 -1318 -1575 1479 C ATOM 3270 CD PRO B 209 -3.574 56.162 -12.909 1.00 65.06 C ANISOU 3270 CD PRO B 209 7258 10520 6942 -1434 -1509 1190 C ATOM 3271 N PRO B 210 -3.626 54.327 -8.570 1.00 75.71 N ANISOU 3271 N PRO B 210 9108 11141 8519 -687 -3153 1206 N ATOM 3272 CA PRO B 210 -3.244 53.149 -7.782 1.00 79.36 C ANISOU 3272 CA PRO B 210 9659 11260 9235 -644 -3588 1026 C ATOM 3273 C PRO B 210 -4.076 51.904 -8.078 1.00 80.95 C ANISOU 3273 C PRO B 210 9933 11768 9057 -860 -3465 1139 C ATOM 3274 O PRO B 210 -3.664 50.803 -7.716 1.00 82.69 O ANISOU 3274 O PRO B 210 10241 11662 9514 -885 -3762 946 O ATOM 3275 CB PRO B 210 -3.488 53.602 -6.338 1.00 79.70 C ANISOU 3275 CB PRO B 210 10119 11102 9061 -323 -4020 1207 C ATOM 3276 CG PRO B 210 -3.423 55.088 -6.389 1.00 78.85 C ANISOU 3276 CG PRO B 210 9998 11044 8918 -182 -3872 1309 C ATOM 3277 CD PRO B 210 -4.013 55.457 -7.710 1.00 76.23 C ANISOU 3277 CD PRO B 210 9485 11197 8283 -388 -3311 1451 C ATOM 3278 N HIS B 211 -5.229 52.076 -8.715 1.00 81.99 N ANISOU 3278 N HIS B 211 10054 12509 8588 -998 -3053 1416 N ATOM 3279 CA HIS B 211 -6.113 50.952 -9.012 1.00 83.89 C ANISOU 3279 CA HIS B 211 10347 13119 8409 -1252 -2877 1499 C ATOM 3280 C HIS B 211 -5.454 49.946 -9.952 1.00 83.03 C ANISOU 3280 C HIS B 211 9930 12880 8736 -1526 -2732 1210 C ATOM 3281 O HIS B 211 -5.638 48.737 -9.810 1.00 83.26 O ANISOU 3281 O HIS B 211 10101 12846 8687 -1691 -2817 1148 O ATOM 3282 CB HIS B 211 -7.421 51.447 -9.631 1.00 85.80 C ANISOU 3282 CB HIS B 211 10532 14109 7960 -1316 -2455 1764 C ATOM 3283 CG HIS B 211 -8.166 52.426 -8.778 1.00 87.58 C ANISOU 3283 CG HIS B 211 11037 14306 7934 -946 -2418 1867 C ATOM 3284 ND1 HIS B 211 -7.765 53.734 -8.626 1.00 88.19 N ANISOU 3284 ND1 HIS B 211 11147 14237 8126 -676 -2512 1934 N ATOM 3285 CD2 HIS B 211 -9.288 52.284 -8.034 1.00 88.55 C ANISOU 3285 CD2 HIS B 211 11411 14425 7810 -802 -2245 1809 C ATOM 3286 CE1 HIS B 211 -8.609 54.360 -7.823 1.00 88.94 C ANISOU 3286 CE1 HIS B 211 11521 14223 8051 -354 -2412 1899 C ATOM 3287 NE2 HIS B 211 -9.542 53.503 -7.451 1.00 89.10 N ANISOU 3287 NE2 HIS B 211 11648 14339 7867 -436 -2265 1814 N ATOM 3288 N LEU B 212 -4.683 50.455 -10.907 1.00 82.49 N ANISOU 3288 N LEU B 212 9478 12758 9107 -1598 -2498 1015 N ATOM 3289 CA LEU B 212 -4.044 49.609 -11.906 1.00 83.88 C ANISOU 3289 CA LEU B 212 9295 12865 9710 -1876 -2305 699 C ATOM 3290 C LEU B 212 -2.881 48.815 -11.327 1.00 87.74 C ANISOU 3290 C LEU B 212 9760 12722 10855 -1769 -2772 302 C ATOM 3291 O LEU B 212 -2.348 47.917 -11.977 1.00 90.69 O ANISOU 3291 O LEU B 212 9875 12988 11595 -1951 -2711 -10 O ATOM 3292 CB LEU B 212 -3.555 50.449 -13.085 1.00 82.86 C ANISOU 3292 CB LEU B 212 8802 12864 9817 -2035 -1884 573 C ATOM 3293 CG LEU B 212 -4.609 51.181 -13.913 1.00 79.89 C ANISOU 3293 CG LEU B 212 8458 13086 8809 -2117 -1425 909 C ATOM 3294 CD1 LEU B 212 -3.964 51.843 -15.122 1.00 79.49 C ANISOU 3294 CD1 LEU B 212 8147 13037 9019 -2339 -1018 736 C ATOM 3295 CD2 LEU B 212 -5.709 50.225 -14.338 1.00 78.82 C ANISOU 3295 CD2 LEU B 212 8320 13467 8162 -2305 -1217 1063 C ATOM 3296 N LEU B 213 -2.486 49.149 -10.103 1.00 87.70 N ANISOU 3296 N LEU B 213 10027 12302 10991 -1442 -3266 286 N ATOM 3297 CA LEU B 213 -1.371 48.468 -9.455 1.00 90.22 C ANISOU 3297 CA LEU B 213 10364 12005 11912 -1237 -3809 -124 C ATOM 3298 C LEU B 213 -1.834 47.286 -8.610 1.00 90.96 C ANISOU 3298 C LEU B 213 10993 11875 11694 -1164 -4190 -8 C ATOM 3299 O LEU B 213 -1.114 46.827 -7.720 1.00 93.40 O ANISOU 3299 O LEU B 213 11549 11621 12319 -875 -4776 -243 O ATOM 3300 CB LEU B 213 -0.559 49.447 -8.608 1.00 91.54 C ANISOU 3300 CB LEU B 213 10534 11801 12445 -912 -4175 -278 C ATOM 3301 CG LEU B 213 0.077 50.585 -9.404 1.00 71.62 C ANISOU 3301 CG LEU B 213 7547 9389 10275 -1038 -3805 -479 C ATOM 3302 CD1 LEU B 213 1.074 51.339 -8.544 1.00 73.60 C ANISOU 3302 CD1 LEU B 213 7755 9211 10997 -750 -4208 -772 C ATOM 3303 CD2 LEU B 213 0.739 50.043 -10.659 1.00 72.93 C ANISOU 3303 CD2 LEU B 213 7191 9623 10895 -1349 -3478 -898 C ATOM 3304 N GLN B 214 -3.041 46.804 -8.892 1.00 89.33 N ANISOU 3304 N GLN B 214 10999 12107 10835 -1437 -3856 325 N ATOM 3305 CA GLN B 214 -3.557 45.602 -8.252 1.00 91.48 C ANISOU 3305 CA GLN B 214 11828 12197 10732 -1510 -4092 419 C ATOM 3306 C GLN B 214 -3.763 44.503 -9.288 1.00 88.93 C ANISOU 3306 C GLN B 214 11337 12067 10384 -1864 -3759 301 C ATOM 3307 O GLN B 214 -4.812 44.428 -9.930 1.00 87.58 O ANISOU 3307 O GLN B 214 11091 12496 9690 -2193 -3255 534 O ATOM 3308 CB GLN B 214 -4.864 45.890 -7.512 1.00 93.74 C ANISOU 3308 CB GLN B 214 12575 12835 10205 -1588 -3989 853 C ATOM 3309 CG GLN B 214 -4.695 46.732 -6.255 1.00 97.84 C ANISOU 3309 CG GLN B 214 13414 13065 10694 -1235 -4409 968 C ATOM 3310 CD GLN B 214 -5.696 46.363 -5.175 1.00101.78 C ANISOU 3310 CD GLN B 214 14598 13601 10472 -1325 -4534 1245 C ATOM 3311 OE1 GLN B 214 -6.553 45.500 -5.375 1.00102.75 O ANISOU 3311 OE1 GLN B 214 14937 13986 10117 -1671 -4234 1329 O ATOM 3312 NE2 GLN B 214 -5.586 47.010 -4.018 1.00103.17 N ANISOU 3312 NE2 GLN B 214 15003 13487 10710 -984 -4659 1275 N ATOM 3313 N VAL B 215 -2.753 43.653 -9.443 1.00 88.14 N ANISOU 3313 N VAL B 215 11163 11473 10854 -1771 -4063 -102 N ATOM 3314 CA VAL B 215 -2.774 42.617 -10.469 1.00 85.92 C ANISOU 3314 CA VAL B 215 10677 11314 10654 -2079 -3775 -282 C ATOM 3315 C VAL B 215 -3.347 41.306 -9.934 1.00 87.86 C ANISOU 3315 C VAL B 215 11621 11319 10444 -2220 -3956 -179 C ATOM 3316 O VAL B 215 -2.788 40.706 -9.017 1.00 91.82 O ANISOU 3316 O VAL B 215 12639 11153 11097 -1934 -4560 -329 O ATOM 3317 CB VAL B 215 -1.362 42.361 -11.024 1.00 84.33 C ANISOU 3317 CB VAL B 215 9976 10737 11328 -1917 -3977 -851 C ATOM 3318 CG1 VAL B 215 -1.430 41.465 -12.251 1.00 85.17 C ANISOU 3318 CG1 VAL B 215 9766 11077 11520 -2275 -3573 -1031 C ATOM 3319 CG2 VAL B 215 -0.688 43.677 -11.364 1.00 80.22 C ANISOU 3319 CG2 VAL B 215 8878 10352 11252 -1813 -3836 -1008 C ATOM 3320 N ILE B 216 -4.457 40.861 -10.517 1.00 84.64 N ANISOU 3320 N ILE B 216 11263 11443 9452 -2667 -3434 51 N ATOM 3321 CA ILE B 216 -5.127 39.646 -10.060 1.00 85.56 C ANISOU 3321 CA ILE B 216 12086 11389 9033 -2924 -3490 153 C ATOM 3322 C ILE B 216 -4.282 38.395 -10.279 1.00 90.32 C ANISOU 3322 C ILE B 216 12867 11384 10067 -2864 -3806 -213 C ATOM 3323 O ILE B 216 -4.460 37.388 -9.591 1.00 93.99 O ANISOU 3323 O ILE B 216 14122 11379 10210 -2916 -4100 -191 O ATOM 3324 CB ILE B 216 -6.499 39.454 -10.743 1.00 80.94 C ANISOU 3324 CB ILE B 216 11410 11598 7746 -3463 -2804 393 C ATOM 3325 CG1 ILE B 216 -6.382 39.666 -12.250 1.00 76.44 C ANISOU 3325 CG1 ILE B 216 10027 11541 7477 -3637 -2301 258 C ATOM 3326 CG2 ILE B 216 -7.532 40.404 -10.160 1.00 79.11 C ANISOU 3326 CG2 ILE B 216 11279 11878 6902 -3497 -2624 732 C ATOM 3327 CD1 ILE B 216 -7.710 39.679 -12.954 1.00 73.55 C ANISOU 3327 CD1 ILE B 216 9475 12030 6441 -4079 -1662 464 C ATOM 3328 N LEU B 217 -3.362 38.462 -11.235 1.00 90.30 N ANISOU 3328 N LEU B 217 12167 11376 10767 -2761 -3745 -574 N ATOM 3329 CA LEU B 217 -2.518 37.317 -11.560 1.00 93.15 C ANISOU 3329 CA LEU B 217 12575 11219 11597 -2666 -4035 -999 C ATOM 3330 C LEU B 217 -1.297 37.232 -10.653 1.00 96.53 C ANISOU 3330 C LEU B 217 13241 10845 12592 -2061 -4861 -1352 C ATOM 3331 O LEU B 217 -0.730 36.156 -10.463 1.00100.01 O ANISOU 3331 O LEU B 217 14066 10688 13244 -1861 -5313 -1657 O ATOM 3332 CB LEU B 217 -2.093 37.364 -13.026 1.00 91.39 C ANISOU 3332 CB LEU B 217 11471 11389 11862 -2867 -3572 -1297 C ATOM 3333 CG LEU B 217 -3.238 37.299 -14.034 1.00 87.69 C ANISOU 3333 CG LEU B 217 10766 11696 10856 -3436 -2797 -1016 C ATOM 3334 CD1 LEU B 217 -2.687 37.278 -15.440 1.00 79.31 C ANISOU 3334 CD1 LEU B 217 8907 10920 10306 -3613 -2404 -1350 C ATOM 3335 CD2 LEU B 217 -4.102 36.078 -13.776 1.00 81.35 C ANISOU 3335 CD2 LEU B 217 10666 10814 9430 -3760 -2732 -852 C ATOM 3336 N ASN B 218 -0.890 38.371 -10.101 1.00 74.17 N ANISOU 3336 N ASN B 218 7788 11069 9325 -611 -2771 792 N ATOM 3337 CA ASN B 218 0.175 38.394 -9.107 1.00 78.67 C ANISOU 3337 CA ASN B 218 8224 11828 9840 -825 -3056 1072 C ATOM 3338 C ASN B 218 -0.367 37.964 -7.754 1.00 81.20 C ANISOU 3338 C ASN B 218 8733 12254 9865 -1061 -3197 1109 C ATOM 3339 O ASN B 218 0.362 37.437 -6.917 1.00 84.66 O ANISOU 3339 O ASN B 218 9051 12853 10262 -1200 -3455 1447 O ATOM 3340 CB ASN B 218 0.814 39.782 -9.018 1.00 80.73 C ANISOU 3340 CB ASN B 218 8459 12192 10020 -1062 -3149 995 C ATOM 3341 CG ASN B 218 1.710 40.090 -10.204 1.00 81.26 C ANISOU 3341 CG ASN B 218 8289 12201 10384 -879 -3073 1060 C ATOM 3342 OD1 ASN B 218 2.276 39.185 -10.817 1.00 82.92 O ANISOU 3342 OD1 ASN B 218 8273 12352 10879 -641 -3022 1265 O ATOM 3343 ND2 ASN B 218 1.846 41.370 -10.531 1.00 79.86 N ANISOU 3343 ND2 ASN B 218 8172 12013 10157 -1007 -3023 875 N ATOM 3344 N LYS B 219 -1.659 38.197 -7.549 1.00 81.74 N ANISOU 3344 N LYS B 219 9085 12235 9737 -1123 -3029 780 N ATOM 3345 CA LYS B 219 -2.353 37.694 -6.372 1.00 87.18 C ANISOU 3345 CA LYS B 219 9997 12985 10142 -1345 -3085 753 C ATOM 3346 C LYS B 219 -2.513 36.184 -6.502 1.00 88.54 C ANISOU 3346 C LYS B 219 10113 13081 10447 -1100 -3057 966 C ATOM 3347 O LYS B 219 -2.757 35.671 -7.595 1.00 88.07 O ANISOU 3347 O LYS B 219 9971 12857 10634 -774 -2846 915 O ATOM 3348 CB LYS B 219 -3.729 38.356 -6.234 1.00 88.94 C ANISOU 3348 CB LYS B 219 10499 13091 10203 -1444 -2843 315 C ATOM 3349 CG LYS B 219 -3.800 39.508 -5.228 1.00 93.12 C ANISOU 3349 CG LYS B 219 11224 13702 10456 -1888 -2859 110 C ATOM 3350 CD LYS B 219 -3.598 40.874 -5.884 1.00 92.34 C ANISOU 3350 CD LYS B 219 11078 13511 10497 -1877 -2734 -76 C ATOM 3351 CE LYS B 219 -2.135 41.313 -5.868 1.00 91.70 C ANISOU 3351 CE LYS B 219 10811 13604 10425 -2019 -2971 169 C ATOM 3352 NZ LYS B 219 -1.942 42.632 -6.540 1.00 87.99 N ANISOU 3352 NZ LYS B 219 10319 13020 10092 -2012 -2822 -17 N ATOM 3353 N ASP B 220 -2.373 35.469 -5.393 1.00 91.37 N ANISOU 3353 N ASP B 220 10532 13556 10628 -1292 -3253 1209 N ATOM 3354 CA ASP B 220 -2.490 34.017 -5.426 1.00 92.62 C ANISOU 3354 CA ASP B 220 10648 13606 10936 -1070 -3208 1445 C ATOM 3355 C ASP B 220 -3.793 33.548 -4.788 1.00 88.82 C ANISOU 3355 C ASP B 220 10498 13074 10176 -1198 -3075 1211 C ATOM 3356 O ASP B 220 -4.222 34.079 -3.764 1.00 88.80 O ANISOU 3356 O ASP B 220 10729 13200 9813 -1575 -3161 1064 O ATOM 3357 CB ASP B 220 -1.291 33.362 -4.741 1.00101.26 C ANISOU 3357 CB ASP B 220 11508 14838 12129 -1129 -3536 2007 C ATOM 3358 CG ASP B 220 -1.085 31.927 -5.181 1.00105.90 C ANISOU 3358 CG ASP B 220 11930 15217 13091 -770 -3411 2306 C ATOM 3359 OD1 ASP B 220 -1.454 31.597 -6.329 1.00104.08 O ANISOU 3359 OD1 ASP B 220 11679 14755 13113 -459 -3066 2089 O ATOM 3360 OD2 ASP B 220 -0.553 31.129 -4.381 1.00111.53 O ANISOU 3360 OD2 ASP B 220 12538 15992 13848 -824 -3643 2771 O ATOM 3361 N THR B 221 -4.414 32.547 -5.404 1.00 86.04 N ANISOU 3361 N THR B 221 10174 12530 9986 -922 -2830 1153 N ATOM 3362 CA THR B 221 -5.702 32.038 -4.945 1.00 84.79 C ANISOU 3362 CA THR B 221 10310 12309 9598 -1018 -2660 903 C ATOM 3363 C THR B 221 -5.558 31.016 -3.822 1.00 87.85 C ANISOU 3363 C THR B 221 10805 12741 9834 -1178 -2825 1228 C ATOM 3364 O THR B 221 -4.457 30.547 -3.527 1.00 91.38 O ANISOU 3364 O THR B 221 11048 13241 10429 -1145 -3067 1707 O ATOM 3365 CB THR B 221 -6.488 31.382 -6.095 1.00 82.78 C ANISOU 3365 CB THR B 221 10059 11857 9538 -712 -2315 685 C ATOM 3366 OG1 THR B 221 -5.720 30.304 -6.645 1.00 85.08 O ANISOU 3366 OG1 THR B 221 10162 12014 10153 -451 -2253 1003 O ATOM 3367 CG2 THR B 221 -6.790 32.396 -7.188 1.00 80.36 C ANISOU 3367 CG2 THR B 221 9670 11534 9329 -601 -2178 389 C ATOM 3368 N ASN B 222 -6.685 30.680 -3.201 1.00 86.57 N ANISOU 3368 N ASN B 222 10945 12553 9394 -1356 -2695 989 N ATOM 3369 CA ASN B 222 -6.722 29.667 -2.156 1.00 88.49 C ANISOU 3369 CA ASN B 222 11348 12819 9454 -1532 -2818 1270 C ATOM 3370 C ASN B 222 -6.493 28.288 -2.764 1.00 88.74 C ANISOU 3370 C ASN B 222 11250 12627 9841 -1165 -2671 1547 C ATOM 3371 O ASN B 222 -6.932 28.019 -3.880 1.00 87.89 O ANISOU 3371 O ASN B 222 11091 12339 9964 -876 -2351 1306 O ATOM 3372 CB ASN B 222 -8.065 29.717 -1.427 1.00 87.66 C ANISOU 3372 CB ASN B 222 11618 12721 8970 -1831 -2647 867 C ATOM 3373 CG ASN B 222 -8.026 29.030 -0.078 1.00 92.94 C ANISOU 3373 CG ASN B 222 12513 13491 9308 -2185 -2848 1145 C ATOM 3374 OD1 ASN B 222 -7.560 27.898 0.045 1.00 96.27 O ANISOU 3374 OD1 ASN B 222 12866 13837 9873 -2042 -2943 1583 O ATOM 3375 ND2 ASN B 222 -8.513 29.720 0.947 1.00 94.72 N ANISOU 3375 ND2 ASN B 222 13018 13872 9098 -2673 -2890 901 N ATOM 3376 N ILE B 223 -5.804 27.416 -2.036 1.00 90.04 N ANISOU 3376 N ILE B 223 11361 12796 10055 -1201 -2890 2068 N ATOM 3377 CA ILE B 223 -5.456 26.105 -2.572 1.00 90.10 C ANISOU 3377 CA ILE B 223 11216 12530 10487 -839 -2710 2381 C ATOM 3378 C ILE B 223 -6.654 25.164 -2.621 1.00 88.86 C ANISOU 3378 C ILE B 223 11359 12172 10231 -813 -2355 2108 C ATOM 3379 O ILE B 223 -6.620 24.144 -3.304 1.00 89.61 O ANISOU 3379 O ILE B 223 11385 11989 10673 -519 -2056 2190 O ATOM 3380 CB ILE B 223 -4.326 25.437 -1.768 1.00 95.57 C ANISOU 3380 CB ILE B 223 11706 13260 11347 -854 -3060 3109 C ATOM 3381 CG1 ILE B 223 -4.877 24.789 -0.498 1.00 98.17 C ANISOU 3381 CG1 ILE B 223 12354 13650 11295 -1175 -3203 3284 C ATOM 3382 CG2 ILE B 223 -3.239 26.448 -1.439 1.00 98.10 C ANISOU 3382 CG2 ILE B 223 11768 13876 11629 -1022 -3483 3374 C ATOM 3383 CD1 ILE B 223 -3.884 23.887 0.189 1.00104.41 C ANISOU 3383 CD1 ILE B 223 12935 14421 12317 -1136 -3514 4077 C ATOM 3384 N SER B 224 -7.712 25.507 -1.895 1.00 86.94 N ANISOU 3384 N SER B 224 11452 12057 9525 -1146 -2348 1761 N ATOM 3385 CA SER B 224 -8.909 24.677 -1.865 1.00 84.40 C ANISOU 3385 CA SER B 224 11419 11579 9070 -1172 -2019 1471 C ATOM 3386 C SER B 224 -9.808 24.989 -3.053 1.00 80.17 C ANISOU 3386 C SER B 224 10879 10968 8612 -1007 -1652 924 C ATOM 3387 O SER B 224 -10.595 24.150 -3.483 1.00 80.64 O ANISOU 3387 O SER B 224 11069 10864 8706 -924 -1318 717 O ATOM 3388 CB SER B 224 -9.671 24.872 -0.554 1.00 85.79 C ANISOU 3388 CB SER B 224 11950 11918 8729 -1631 -2137 1327 C ATOM 3389 OG SER B 224 -10.026 26.229 -0.366 1.00 84.76 O ANISOU 3389 OG SER B 224 11870 11988 8347 -1875 -2202 949 O ATOM 3390 N CYS B 225 -9.676 26.199 -3.584 1.00 79.61 N ANISOU 3390 N CYS B 225 10655 11030 8563 -985 -1725 716 N ATOM 3391 CA CYS B 225 -10.479 26.633 -4.721 1.00 78.65 C ANISOU 3391 CA CYS B 225 10491 10883 8511 -854 -1451 271 C ATOM 3392 C CYS B 225 -10.034 25.973 -6.022 1.00 79.77 C ANISOU 3392 C CYS B 225 10441 10850 9018 -535 -1220 351 C ATOM 3393 O CYS B 225 -8.935 25.429 -6.109 1.00 82.92 O ANISOU 3393 O CYS B 225 10675 11132 9700 -369 -1275 745 O ATOM 3394 CB CYS B 225 -10.418 28.157 -4.864 1.00 77.13 C ANISOU 3394 CB CYS B 225 10191 10855 8261 -930 -1601 82 C ATOM 3395 SG CYS B 225 -11.116 29.074 -3.470 1.00175.66 S ANISOU 3395 SG CYS B 225 22924 23490 20329 -1362 -1721 -160 S ATOM 3396 N ASP B 226 -10.900 26.022 -7.029 1.00 78.26 N ANISOU 3396 N ASP B 226 10263 10646 8827 -482 -947 -19 N ATOM 3397 CA ASP B 226 -10.556 25.535 -8.357 1.00 79.09 C ANISOU 3397 CA ASP B 226 10225 10619 9208 -276 -689 -25 C ATOM 3398 C ASP B 226 -9.404 26.367 -8.903 1.00 80.04 C ANISOU 3398 C ASP B 226 10077 10782 9555 -139 -864 161 C ATOM 3399 O ASP B 226 -9.439 27.597 -8.839 1.00 80.35 O ANISOU 3399 O ASP B 226 10052 10993 9485 -207 -1079 64 O ATOM 3400 CB ASP B 226 -11.771 25.626 -9.285 1.00 77.57 C ANISOU 3400 CB ASP B 226 10095 10499 8878 -343 -439 -450 C ATOM 3401 CG ASP B 226 -11.510 25.034 -10.662 1.00 79.00 C ANISOU 3401 CG ASP B 226 10192 10567 9257 -241 -127 -500 C ATOM 3402 OD1 ASP B 226 -10.587 25.499 -11.367 1.00 77.95 O ANISOU 3402 OD1 ASP B 226 9864 10421 9332 -121 -173 -373 O ATOM 3403 OD2 ASP B 226 -12.239 24.096 -11.041 1.00 81.49 O ANISOU 3403 OD2 ASP B 226 10656 10807 9501 -323 196 -693 O ATOM 3404 N PRO B 227 -8.378 25.695 -9.444 1.00 80.79 N ANISOU 3404 N PRO B 227 10009 10689 9998 50 -732 422 N ATOM 3405 CA PRO B 227 -7.169 26.336 -9.977 1.00 80.98 C ANISOU 3405 CA PRO B 227 9756 10724 10289 184 -856 620 C ATOM 3406 C PRO B 227 -7.448 27.411 -11.032 1.00 79.67 C ANISOU 3406 C PRO B 227 9529 10700 10043 155 -837 328 C ATOM 3407 O PRO B 227 -6.606 28.285 -11.246 1.00 80.48 O ANISOU 3407 O PRO B 227 9444 10875 10258 200 -1022 446 O ATOM 3408 CB PRO B 227 -6.409 25.168 -10.611 1.00 80.28 C ANISOU 3408 CB PRO B 227 9548 10338 10618 378 -521 817 C ATOM 3409 CG PRO B 227 -6.866 23.979 -9.864 1.00 81.26 C ANISOU 3409 CG PRO B 227 9857 10297 10721 363 -386 919 C ATOM 3410 CD PRO B 227 -8.298 24.226 -9.514 1.00 80.08 C ANISOU 3410 CD PRO B 227 9990 10325 10113 143 -409 548 C ATOM 3411 N ALA B 228 -8.612 27.352 -11.673 1.00 77.18 N ANISOU 3411 N ALA B 228 9356 10435 9532 62 -633 -19 N ATOM 3412 CA ALA B 228 -8.925 28.269 -12.765 1.00 76.15 C ANISOU 3412 CA ALA B 228 9155 10442 9336 23 -620 -232 C ATOM 3413 C ALA B 228 -9.637 29.543 -12.305 1.00 74.36 C ANISOU 3413 C ALA B 228 8945 10411 8897 -71 -884 -370 C ATOM 3414 O ALA B 228 -9.718 30.517 -13.054 1.00 72.68 O ANISOU 3414 O ALA B 228 8633 10299 8681 -76 -950 -450 O ATOM 3415 CB ALA B 228 -9.745 27.557 -13.831 1.00 76.30 C ANISOU 3415 CB ALA B 228 9275 10446 9271 -67 -273 -486 C ATOM 3416 N LEU B 229 -10.142 29.536 -11.076 1.00 73.94 N ANISOU 3416 N LEU B 229 9023 10386 8685 -162 -1004 -393 N ATOM 3417 CA LEU B 229 -10.909 30.668 -10.564 1.00 72.06 C ANISOU 3417 CA LEU B 229 8819 10274 8288 -275 -1154 -571 C ATOM 3418 C LEU B 229 -10.033 31.849 -10.151 1.00 71.76 C ANISOU 3418 C LEU B 229 8679 10283 8304 -288 -1407 -437 C ATOM 3419 O LEU B 229 -8.869 31.681 -9.780 1.00 72.73 O ANISOU 3419 O LEU B 229 8733 10380 8520 -258 -1543 -171 O ATOM 3420 CB LEU B 229 -11.777 30.240 -9.380 1.00 71.83 C ANISOU 3420 CB LEU B 229 8996 10244 8051 -430 -1130 -694 C ATOM 3421 CG LEU B 229 -12.747 29.085 -9.610 1.00 70.11 C ANISOU 3421 CG LEU B 229 8910 9986 7742 -464 -870 -859 C ATOM 3422 CD1 LEU B 229 -13.651 28.904 -8.402 1.00 70.06 C ANISOU 3422 CD1 LEU B 229 9109 9992 7519 -650 -852 -1016 C ATOM 3423 CD2 LEU B 229 -13.563 29.309 -10.867 1.00 68.56 C ANISOU 3423 CD2 LEU B 229 8613 9880 7557 -446 -728 -1065 C ATOM 3424 N LEU B 230 -10.617 33.042 -10.211 1.00 69.97 N ANISOU 3424 N LEU B 230 8427 10117 8043 -342 -1454 -613 N ATOM 3425 CA LEU B 230 -9.940 34.268 -9.809 1.00 69.27 C ANISOU 3425 CA LEU B 230 8279 10055 7987 -403 -1635 -553 C ATOM 3426 C LEU B 230 -10.887 35.132 -8.987 1.00 70.85 C ANISOU 3426 C LEU B 230 8588 10251 8080 -570 -1603 -796 C ATOM 3427 O LEU B 230 -12.104 35.002 -9.108 1.00 69.54 O ANISOU 3427 O LEU B 230 8458 10069 7894 -570 -1447 -1003 O ATOM 3428 CB LEU B 230 -9.466 35.041 -11.040 1.00 66.94 C ANISOU 3428 CB LEU B 230 7802 9765 7868 -271 -1651 -501 C ATOM 3429 CG LEU B 230 -8.299 34.430 -11.808 1.00 56.27 C ANISOU 3429 CG LEU B 230 6326 8391 6662 -146 -1651 -280 C ATOM 3430 CD1 LEU B 230 -7.972 35.277 -13.014 1.00 55.60 C ANISOU 3430 CD1 LEU B 230 6105 8321 6699 -76 -1646 -273 C ATOM 3431 CD2 LEU B 230 -7.090 34.296 -10.901 1.00 62.82 C ANISOU 3431 CD2 LEU B 230 7116 9226 7526 -189 -1830 -36 C ATOM 3432 N PRO B 231 -10.332 36.016 -8.143 1.00 75.04 N ANISOU 3432 N PRO B 231 9166 10791 8553 -742 -1721 -783 N ATOM 3433 CA PRO B 231 -11.162 36.956 -7.386 1.00 77.92 C ANISOU 3433 CA PRO B 231 9643 11100 8863 -934 -1607 -1054 C ATOM 3434 C PRO B 231 -11.893 37.906 -8.324 1.00 79.48 C ANISOU 3434 C PRO B 231 9687 11210 9303 -771 -1475 -1186 C ATOM 3435 O PRO B 231 -11.499 38.059 -9.479 1.00 79.21 O ANISOU 3435 O PRO B 231 9483 11195 9419 -572 -1538 -1039 O ATOM 3436 CB PRO B 231 -10.139 37.742 -6.560 1.00 78.98 C ANISOU 3436 CB PRO B 231 9839 11276 8894 -1174 -1754 -980 C ATOM 3437 CG PRO B 231 -8.938 36.874 -6.502 1.00 79.25 C ANISOU 3437 CG PRO B 231 9816 11427 8868 -1145 -1987 -639 C ATOM 3438 CD PRO B 231 -8.905 36.150 -7.806 1.00 77.07 C ANISOU 3438 CD PRO B 231 9371 11115 8798 -808 -1938 -524 C ATOM 3439 N GLU B 232 -12.948 38.541 -7.832 1.00 81.89 N ANISOU 3439 N GLU B 232 10040 11409 9666 -868 -1283 -1443 N ATOM 3440 CA GLU B 232 -13.697 39.477 -8.653 1.00 84.04 C ANISOU 3440 CA GLU B 232 10120 11574 10236 -698 -1164 -1506 C ATOM 3441 C GLU B 232 -12.908 40.768 -8.826 1.00 84.27 C ANISOU 3441 C GLU B 232 10095 11510 10416 -703 -1201 -1440 C ATOM 3442 O GLU B 232 -12.507 41.391 -7.844 1.00 86.58 O ANISOU 3442 O GLU B 232 10538 11730 10627 -947 -1142 -1561 O ATOM 3443 CB GLU B 232 -15.061 39.766 -8.031 1.00 88.09 C ANISOU 3443 CB GLU B 232 10656 11958 10855 -782 -899 -1789 C ATOM 3444 CG GLU B 232 -15.995 40.542 -8.937 1.00 90.16 C ANISOU 3444 CG GLU B 232 10647 12120 11492 -562 -793 -1779 C ATOM 3445 CD GLU B 232 -17.344 40.777 -8.300 1.00 94.16 C ANISOU 3445 CD GLU B 232 11121 12478 12178 -627 -499 -2048 C ATOM 3446 OE1 GLU B 232 -17.465 40.550 -7.077 1.00 95.26 O ANISOU 3446 OE1 GLU B 232 11501 12561 12133 -893 -340 -2295 O ATOM 3447 OE2 GLU B 232 -18.281 41.181 -9.020 1.00 96.52 O ANISOU 3447 OE2 GLU B 232 11141 12724 12808 -434 -428 -1997 O ATOM 3448 N PRO B 233 -12.669 41.164 -10.085 1.00 83.06 N ANISOU 3448 N PRO B 233 9746 11366 10448 -481 -1290 -1253 N ATOM 3449 CA PRO B 233 -11.944 42.399 -10.399 1.00 84.24 C ANISOU 3449 CA PRO B 233 9838 11411 10758 -469 -1313 -1175 C ATOM 3450 C PRO B 233 -12.875 43.604 -10.398 1.00 86.28 C ANISOU 3450 C PRO B 233 10007 11430 11346 -420 -1088 -1295 C ATOM 3451 O PRO B 233 -14.082 43.435 -10.579 1.00 88.19 O ANISOU 3451 O PRO B 233 10133 11632 11744 -313 -974 -1353 O ATOM 3452 CB PRO B 233 -11.444 42.142 -11.819 1.00 81.91 C ANISOU 3452 CB PRO B 233 9384 11232 10506 -267 -1483 -918 C ATOM 3453 CG PRO B 233 -12.503 41.268 -12.421 1.00 79.96 C ANISOU 3453 CG PRO B 233 9049 11082 10250 -153 -1460 -912 C ATOM 3454 CD PRO B 233 -13.012 40.397 -11.297 1.00 80.12 C ANISOU 3454 CD PRO B 233 9226 11123 10093 -285 -1369 -1105 C ATOM 3455 N ASN B 234 -12.333 44.799 -10.189 1.00 86.49 N ANISOU 3455 N ASN B 234 10069 11286 11508 -504 -1001 -1326 N ATOM 3456 CA ASN B 234 -13.129 46.006 -10.376 1.00 89.49 C ANISOU 3456 CA ASN B 234 10325 11377 12301 -403 -756 -1379 C ATOM 3457 C ASN B 234 -13.116 46.418 -11.844 1.00 86.89 C ANISOU 3457 C ASN B 234 9757 11058 12201 -126 -908 -1062 C ATOM 3458 O ASN B 234 -12.200 46.060 -12.585 1.00 83.86 O ANISOU 3458 O ASN B 234 9369 10863 11633 -90 -1149 -868 O ATOM 3459 CB ASN B 234 -12.679 47.146 -9.452 1.00 94.70 C ANISOU 3459 CB ASN B 234 11158 11794 13031 -656 -508 -1593 C ATOM 3460 CG ASN B 234 -11.215 47.498 -9.618 1.00 98.25 C ANISOU 3460 CG ASN B 234 11694 12340 13296 -775 -689 -1475 C ATOM 3461 OD1 ASN B 234 -10.705 47.598 -10.733 1.00 99.03 O ANISOU 3461 OD1 ASN B 234 11652 12512 13462 -574 -885 -1212 O ATOM 3462 ND2 ASN B 234 -10.528 47.691 -8.497 1.00100.87 N ANISOU 3462 ND2 ASN B 234 12260 12693 13374 -1146 -623 -1669 N ATOM 3463 N HIS B 235 -14.136 47.161 -12.261 1.00 87.51 N ANISOU 3463 N HIS B 235 9627 10931 12693 53 -758 -991 N ATOM 3464 CA HIS B 235 -14.343 47.450 -13.676 1.00 86.02 C ANISOU 3464 CA HIS B 235 9191 10796 12697 287 -942 -633 C ATOM 3465 C HIS B 235 -13.187 48.218 -14.307 1.00 85.38 C ANISOU 3465 C HIS B 235 9157 10673 12611 284 -1049 -455 C ATOM 3466 O HIS B 235 -13.020 48.214 -15.526 1.00 86.08 O ANISOU 3466 O HIS B 235 9119 10896 12690 395 -1264 -156 O ATOM 3467 CB HIS B 235 -15.654 48.215 -13.883 1.00 88.29 C ANISOU 3467 CB HIS B 235 9201 10842 13504 479 -762 -534 C ATOM 3468 CG HIS B 235 -15.631 49.613 -13.348 1.00 91.19 C ANISOU 3468 CG HIS B 235 9585 10774 14290 479 -429 -629 C ATOM 3469 ND1 HIS B 235 -15.052 50.662 -14.031 1.00 92.81 N ANISOU 3469 ND1 HIS B 235 9746 10810 14708 564 -453 -394 N ATOM 3470 CD2 HIS B 235 -16.113 50.135 -12.197 1.00 93.58 C ANISOU 3470 CD2 HIS B 235 9967 10751 14840 371 -14 -958 C ATOM 3471 CE1 HIS B 235 -15.177 51.769 -13.322 1.00 95.82 C ANISOU 3471 CE1 HIS B 235 10175 10763 15469 525 -57 -570 C ATOM 3472 NE2 HIS B 235 -15.819 51.477 -12.204 1.00 96.76 N ANISOU 3472 NE2 HIS B 235 10371 10777 15617 396 230 -927 N ATOM 3473 N VAL B 236 -12.379 48.860 -13.473 1.00 84.53 N ANISOU 3473 N VAL B 236 9248 10399 12473 105 -892 -652 N ATOM 3474 CA VAL B 236 -11.373 49.790 -13.967 1.00 82.59 C ANISOU 3474 CA VAL B 236 9043 10054 12285 83 -923 -520 C ATOM 3475 C VAL B 236 -10.065 49.120 -14.411 1.00 77.63 C ANISOU 3475 C VAL B 236 8502 9722 11272 -8 -1199 -428 C ATOM 3476 O VAL B 236 -9.255 49.736 -15.101 1.00 76.58 O ANISOU 3476 O VAL B 236 8366 9564 11168 -5 -1269 -274 O ATOM 3477 CB VAL B 236 -11.108 50.912 -12.937 1.00 84.44 C ANISOU 3477 CB VAL B 236 9441 9956 12685 -111 -585 -780 C ATOM 3478 CG1 VAL B 236 -9.895 50.590 -12.083 1.00 83.28 C ANISOU 3478 CG1 VAL B 236 9540 9984 12119 -435 -649 -979 C ATOM 3479 CG2 VAL B 236 -10.944 52.242 -13.645 1.00 86.69 C ANISOU 3479 CG2 VAL B 236 9649 9950 13340 2 -472 -591 C ATOM 3480 N MET B 237 -9.867 47.860 -14.032 1.00 75.42 N ANISOU 3480 N MET B 237 8287 9698 10671 -83 -1328 -512 N ATOM 3481 CA MET B 237 -8.670 47.127 -14.447 1.00 74.38 C ANISOU 3481 CA MET B 237 8189 9810 10261 -137 -1544 -409 C ATOM 3482 C MET B 237 -8.903 46.393 -15.769 1.00 73.90 C ANISOU 3482 C MET B 237 7998 9929 10150 15 -1698 -193 C ATOM 3483 O MET B 237 -7.970 45.847 -16.366 1.00 73.00 O ANISOU 3483 O MET B 237 7887 9971 9876 -12 -1816 -97 O ATOM 3484 CB MET B 237 -8.232 46.129 -13.371 1.00 72.51 C ANISOU 3484 CB MET B 237 8076 9730 9745 -301 -1593 -557 C ATOM 3485 CG MET B 237 -8.965 44.794 -13.423 1.00 70.68 C ANISOU 3485 CG MET B 237 7817 9650 9386 -215 -1642 -562 C ATOM 3486 SD MET B 237 -8.242 43.560 -12.325 1.00173.51 S ANISOU 3486 SD MET B 237 20971 22850 22106 -384 -1741 -623 S ATOM 3487 CE MET B 237 -8.478 44.335 -10.726 1.00 72.38 C ANISOU 3487 CE MET B 237 8348 9911 9241 -670 -1589 -881 C ATOM 3488 N LEU B 238 -10.156 46.386 -16.213 1.00 73.14 N ANISOU 3488 N LEU B 238 7779 9813 10197 143 -1675 -122 N ATOM 3489 CA LEU B 238 -10.543 45.690 -17.433 1.00 69.15 C ANISOU 3489 CA LEU B 238 7164 9517 9591 204 -1815 70 C ATOM 3490 C LEU B 238 -9.904 46.328 -18.656 1.00 68.00 C ANISOU 3490 C LEU B 238 6976 9391 9470 202 -1919 314 C ATOM 3491 O LEU B 238 -9.633 47.526 -18.660 1.00 68.68 O ANISOU 3491 O LEU B 238 7056 9275 9766 228 -1873 385 O ATOM 3492 CB LEU B 238 -12.064 45.693 -17.579 1.00 68.76 C ANISOU 3492 CB LEU B 238 6951 9464 9711 306 -1792 127 C ATOM 3493 CG LEU B 238 -12.841 45.054 -16.429 1.00 66.98 C ANISOU 3493 CG LEU B 238 6767 9215 9466 289 -1659 -131 C ATOM 3494 CD1 LEU B 238 -14.333 45.262 -16.616 1.00 68.42 C ANISOU 3494 CD1 LEU B 238 6728 9366 9903 401 -1616 -55 C ATOM 3495 CD2 LEU B 238 -12.514 43.577 -16.331 1.00 65.34 C ANISOU 3495 CD2 LEU B 238 6679 9237 8909 197 -1713 -236 C ATOM 3496 N ASN B 239 -9.654 45.510 -19.677 1.00 67.63 N ANISOU 3496 N ASN B 239 6925 9574 9198 135 -2023 420 N ATOM 3497 CA ASN B 239 -9.080 45.947 -20.957 1.00 68.69 C ANISOU 3497 CA ASN B 239 7048 9772 9281 64 -2113 642 C ATOM 3498 C ASN B 239 -7.600 46.345 -20.930 1.00 69.04 C ANISOU 3498 C ASN B 239 7192 9737 9303 -5 -2076 597 C ATOM 3499 O ASN B 239 -6.942 46.379 -21.972 1.00 68.81 O ANISOU 3499 O ASN B 239 7188 9792 9166 -110 -2111 717 O ATOM 3500 CB ASN B 239 -9.924 47.056 -21.588 1.00 69.80 C ANISOU 3500 CB ASN B 239 7047 9824 9649 139 -2195 921 C ATOM 3501 CG ASN B 239 -11.360 46.647 -21.772 1.00 72.20 C ANISOU 3501 CG ASN B 239 7188 10256 9989 188 -2267 1023 C ATOM 3502 OD1 ASN B 239 -11.795 45.626 -21.240 1.00 71.26 O ANISOU 3502 OD1 ASN B 239 7087 10248 9739 173 -2216 825 O ATOM 3503 ND2 ASN B 239 -12.112 47.441 -22.526 1.00 76.37 N ANISOU 3503 ND2 ASN B 239 7536 10774 10708 239 -2393 1361 N ATOM 3504 N HIS B 240 -7.080 46.638 -19.744 1.00 68.23 N ANISOU 3504 N HIS B 240 7146 9493 9284 11 -1998 422 N ATOM 3505 CA HIS B 240 -5.688 47.042 -19.611 1.00 67.83 C ANISOU 3505 CA HIS B 240 7155 9397 9220 -80 -1979 385 C ATOM 3506 C HIS B 240 -4.759 45.853 -19.800 1.00 67.37 C ANISOU 3506 C HIS B 240 7100 9509 8988 -145 -1986 338 C ATOM 3507 O HIS B 240 -5.063 44.742 -19.365 1.00 68.56 O ANISOU 3507 O HIS B 240 7249 9751 9049 -118 -1973 253 O ATOM 3508 CB HIS B 240 -5.447 47.714 -18.261 1.00 69.06 C ANISOU 3508 CB HIS B 240 7373 9392 9475 -119 -1902 218 C ATOM 3509 CG HIS B 240 -6.163 49.019 -18.105 1.00 71.73 C ANISOU 3509 CG HIS B 240 7714 9476 10064 -69 -1798 242 C ATOM 3510 ND1 HIS B 240 -5.597 50.225 -18.456 1.00 72.55 N ANISOU 3510 ND1 HIS B 240 7851 9409 10307 -114 -1741 320 N ATOM 3511 CD2 HIS B 240 -7.403 49.306 -17.641 1.00 73.06 C ANISOU 3511 CD2 HIS B 240 7844 9498 10419 29 -1699 201 C ATOM 3512 CE1 HIS B 240 -6.456 51.200 -18.212 1.00 74.70 C ANISOU 3512 CE1 HIS B 240 8106 9413 10862 -33 -1598 339 C ATOM 3513 NE2 HIS B 240 -7.560 50.668 -17.719 1.00 74.50 N ANISOU 3513 NE2 HIS B 240 8021 9396 10889 60 -1566 267 N ATOM 3514 N LEU B 241 -3.626 46.099 -20.452 1.00 66.82 N ANISOU 3514 N LEU B 241 7026 9454 8910 -230 -1975 396 N ATOM 3515 CA LEU B 241 -2.685 45.044 -20.807 1.00 66.32 C ANISOU 3515 CA LEU B 241 6924 9501 8773 -282 -1920 372 C ATOM 3516 C LEU B 241 -1.642 44.800 -19.725 1.00 68.29 C ANISOU 3516 C LEU B 241 7113 9749 9085 -294 -1937 308 C ATOM 3517 O LEU B 241 -0.968 45.728 -19.280 1.00 69.71 O ANISOU 3517 O LEU B 241 7286 9874 9326 -365 -1975 303 O ATOM 3518 CB LEU B 241 -1.974 45.396 -22.112 1.00 66.30 C ANISOU 3518 CB LEU B 241 6931 9514 8747 -400 -1864 461 C ATOM 3519 CG LEU B 241 -0.888 44.418 -22.557 1.00 67.04 C ANISOU 3519 CG LEU B 241 6966 9664 8842 -469 -1723 414 C ATOM 3520 CD1 LEU B 241 -1.511 43.197 -23.215 1.00 68.17 C ANISOU 3520 CD1 LEU B 241 7148 9896 8857 -505 -1603 374 C ATOM 3521 CD2 LEU B 241 0.107 45.089 -23.487 1.00 67.99 C ANISOU 3521 CD2 LEU B 241 7092 9756 8986 -613 -1649 458 C ATOM 3522 N TYR B 242 -1.506 43.543 -19.318 1.00 68.76 N ANISOU 3522 N TYR B 242 7121 9876 9128 -247 -1910 282 N ATOM 3523 CA TYR B 242 -0.475 43.149 -18.366 1.00 71.82 C ANISOU 3523 CA TYR B 242 7400 10297 9590 -263 -1966 310 C ATOM 3524 C TYR B 242 0.493 42.163 -19.004 1.00 74.75 C ANISOU 3524 C TYR B 242 7631 10683 10088 -235 -1839 378 C ATOM 3525 O TYR B 242 0.120 41.406 -19.900 1.00 76.90 O ANISOU 3525 O TYR B 242 7940 10940 10340 -211 -1673 344 O ATOM 3526 CB TYR B 242 -1.103 42.549 -17.111 1.00 71.36 C ANISOU 3526 CB TYR B 242 7384 10271 9458 -232 -2045 272 C ATOM 3527 CG TYR B 242 -1.854 43.565 -16.287 1.00 70.73 C ANISOU 3527 CG TYR B 242 7429 10144 9302 -304 -2108 169 C ATOM 3528 CD1 TYR B 242 -3.131 43.970 -16.647 1.00 68.56 C ANISOU 3528 CD1 TYR B 242 7247 9792 9010 -243 -2046 95 C ATOM 3529 CD2 TYR B 242 -1.280 44.128 -15.156 1.00 71.83 C ANISOU 3529 CD2 TYR B 242 7579 10311 9401 -463 -2206 148 C ATOM 3530 CE1 TYR B 242 -3.816 44.903 -15.901 1.00 68.99 C ANISOU 3530 CE1 TYR B 242 7392 9743 9079 -296 -2028 -11 C ATOM 3531 CE2 TYR B 242 -1.958 45.061 -14.404 1.00 71.84 C ANISOU 3531 CE2 TYR B 242 7722 10228 9346 -576 -2177 4 C ATOM 3532 CZ TYR B 242 -3.226 45.444 -14.780 1.00 70.98 C ANISOU 3532 CZ TYR B 242 7694 9986 9290 -471 -2061 -83 C ATOM 3533 OH TYR B 242 -3.910 46.375 -14.034 1.00 72.98 O ANISOU 3533 OH TYR B 242 8064 10095 9569 -569 -1960 -239 O ATOM 3534 N ALA B 243 1.738 42.169 -18.546 1.00 75.40 N ANISOU 3534 N ALA B 243 7539 10791 10317 -265 -1893 472 N ATOM 3535 CA ALA B 243 2.744 41.319 -19.163 1.00 78.94 C ANISOU 3535 CA ALA B 243 7802 11205 10986 -222 -1723 546 C ATOM 3536 C ALA B 243 3.770 40.785 -18.173 1.00 84.03 C ANISOU 3536 C ALA B 243 8193 11898 11836 -181 -1838 729 C ATOM 3537 O ALA B 243 4.009 41.376 -17.121 1.00 84.90 O ANISOU 3537 O ALA B 243 8270 12119 11868 -273 -2083 798 O ATOM 3538 CB ALA B 243 3.435 42.063 -20.294 1.00 79.00 C ANISOU 3538 CB ALA B 243 7793 11177 11045 -328 -1597 509 C ATOM 3539 N LEU B 244 4.368 39.652 -18.522 1.00 88.47 N ANISOU 3539 N LEU B 244 8569 12374 12670 -69 -1645 822 N ATOM 3540 CA LEU B 244 5.469 39.100 -17.754 1.00 95.29 C ANISOU 3540 CA LEU B 244 9110 13269 13828 -4 -1745 1078 C ATOM 3541 C LEU B 244 6.776 39.674 -18.268 1.00103.85 C ANISOU 3541 C LEU B 244 9952 14363 15145 -74 -1692 1135 C ATOM 3542 O LEU B 244 6.818 40.277 -19.342 1.00104.00 O ANISOU 3542 O LEU B 244 10081 14323 15109 -160 -1507 957 O ATOM 3543 CB LEU B 244 5.502 37.579 -17.886 1.00 94.99 C ANISOU 3543 CB LEU B 244 8952 13068 14073 182 -1504 1178 C ATOM 3544 CG LEU B 244 4.495 36.781 -17.063 1.00 93.42 C ANISOU 3544 CG LEU B 244 8905 12868 13722 260 -1590 1211 C ATOM 3545 CD1 LEU B 244 4.720 35.294 -17.264 1.00 96.02 C ANISOU 3545 CD1 LEU B 244 9092 12984 14407 443 -1293 1328 C ATOM 3546 CD2 LEU B 244 4.613 37.145 -15.597 1.00 94.31 C ANISOU 3546 CD2 LEU B 244 8963 13175 13695 181 -2005 1411 C ATOM 3547 N SER B 245 7.841 39.488 -17.498 1.00112.23 N ANISOU 3547 N SER B 245 10671 15515 16458 -60 -1867 1406 N ATOM 3548 CA SER B 245 9.169 39.853 -17.957 1.00120.37 C ANISOU 3548 CA SER B 245 11392 16554 17788 -111 -1793 1488 C ATOM 3549 C SER B 245 9.509 38.974 -19.150 1.00126.51 C ANISOU 3549 C SER B 245 12061 17074 18931 26 -1324 1415 C ATOM 3550 O SER B 245 9.404 37.750 -19.075 1.00127.72 O ANISOU 3550 O SER B 245 12108 17072 19346 212 -1147 1523 O ATOM 3551 CB SER B 245 10.194 39.651 -16.842 1.00124.92 C ANISOU 3551 CB SER B 245 11561 17306 18598 -121 -2100 1861 C ATOM 3552 OG SER B 245 9.817 40.351 -15.670 1.00125.17 O ANISOU 3552 OG SER B 245 11739 17584 18235 -322 -2500 1905 O ATOM 3553 N ILE B 246 9.895 39.600 -20.256 1.00131.77 N ANISOU 3553 N ILE B 246 12784 17678 19606 -97 -1086 1215 N ATOM 3554 CA ILE B 246 10.236 38.861 -21.467 1.00138.80 C ANISOU 3554 CA ILE B 246 13619 18321 20797 -60 -578 1082 C ATOM 3555 C ILE B 246 11.442 37.945 -21.248 1.00147.58 C ANISOU 3555 C ILE B 246 14226 19298 22550 115 -402 1335 C ATOM 3556 O ILE B 246 12.555 38.405 -20.992 1.00150.64 O ANISOU 3556 O ILE B 246 14264 19780 23193 83 -526 1503 O ATOM 3557 CB ILE B 246 10.482 39.809 -22.664 1.00138.82 C ANISOU 3557 CB ILE B 246 13794 18309 20643 -292 -378 832 C ATOM 3558 CG1 ILE B 246 11.135 39.051 -23.822 1.00141.12 C ANISOU 3558 CG1 ILE B 246 13967 18350 21302 -319 188 698 C ATOM 3559 CG2 ILE B 246 11.329 41.007 -22.243 1.00140.05 C ANISOU 3559 CG2 ILE B 246 13790 18644 20778 -417 -662 919 C ATOM 3560 CD1 ILE B 246 11.428 39.915 -25.028 1.00140.89 C ANISOU 3560 CD1 ILE B 246 14124 18308 21100 -599 407 459 C ATOM 3561 N LYS B 247 11.203 36.640 -21.334 1.00152.65 N ANISOU 3561 N LYS B 247 14812 19709 23478 298 -103 1379 N ATOM 3562 CA LYS B 247 12.259 35.654 -21.141 1.00159.95 C ANISOU 3562 CA LYS B 247 15234 20430 25108 515 122 1659 C ATOM 3563 C LYS B 247 12.389 34.769 -22.376 1.00164.79 C ANISOU 3563 C LYS B 247 15879 20665 26070 525 841 1409 C ATOM 3564 O LYS B 247 11.401 34.502 -23.061 1.00162.02 O ANISOU 3564 O LYS B 247 15958 20227 25377 406 1098 1096 O ATOM 3565 CB LYS B 247 11.981 34.804 -19.897 1.00162.20 C ANISOU 3565 CB LYS B 247 15366 20739 25526 739 -163 2025 C ATOM 3566 CG LYS B 247 13.149 33.930 -19.462 1.00169.07 C ANISOU 3566 CG LYS B 247 15627 21446 27167 987 -73 2462 C ATOM 3567 CD LYS B 247 12.826 33.162 -18.191 1.00172.54 C ANISOU 3567 CD LYS B 247 15948 21940 27668 1171 -422 2877 C ATOM 3568 CE LYS B 247 13.995 32.288 -17.758 1.00180.73 C ANISOU 3568 CE LYS B 247 16329 22810 29532 1437 -364 3404 C ATOM 3569 NZ LYS B 247 14.334 31.257 -18.778 1.00184.94 N ANISOU 3569 NZ LYS B 247 16713 22831 30727 1632 403 3277 N ATOM 3570 N ASP B 248 13.614 34.323 -22.649 1.00174.16 N ANISOU 3570 N ASP B 248 16598 21633 27943 635 1180 1545 N ATOM 3571 CA ASP B 248 13.924 33.535 -23.840 1.00176.24 C ANISOU 3571 CA ASP B 248 16855 21494 28614 598 1959 1275 C ATOM 3572 C ASP B 248 13.523 34.281 -25.108 1.00171.44 C ANISOU 3572 C ASP B 248 16715 20934 27491 219 2212 793 C ATOM 3573 O ASP B 248 14.259 35.138 -25.594 1.00174.41 O ANISOU 3573 O ASP B 248 17001 21392 27875 48 2232 703 O ATOM 3574 CB ASP B 248 13.250 32.161 -23.788 1.00178.49 C ANISOU 3574 CB ASP B 248 17253 21474 29092 762 2320 1266 C ATOM 3575 CG ASP B 248 13.574 31.402 -22.518 1.00182.31 C ANISOU 3575 CG ASP B 248 17304 21905 30060 1130 2040 1796 C ATOM 3576 OD1 ASP B 248 14.694 30.857 -22.418 1.00187.43 O ANISOU 3576 OD1 ASP B 248 17399 22311 31504 1346 2284 2085 O ATOM 3577 OD2 ASP B 248 12.706 31.345 -21.622 1.00180.24 O ANISOU 3577 OD2 ASP B 248 17242 21841 29398 1192 1582 1944 O ATOM 3578 N SER B 249 12.349 33.953 -25.634 1.00162.64 N ANISOU 3578 N SER B 249 16093 19786 25915 63 2387 510 N ATOM 3579 CA SER B 249 11.828 34.620 -26.821 1.00152.88 C ANISOU 3579 CA SER B 249 15322 18642 24123 -334 2561 118 C ATOM 3580 C SER B 249 10.309 34.539 -26.853 1.00136.38 C ANISOU 3580 C SER B 249 13717 16705 21394 -446 2375 -17 C ATOM 3581 O SER B 249 9.686 34.734 -27.896 1.00133.63 O ANISOU 3581 O SER B 249 13767 16405 20602 -790 2588 -316 O ATOM 3582 CB SER B 249 12.417 34.004 -28.091 1.00160.00 C ANISOU 3582 CB SER B 249 16234 19205 25352 -560 3373 -198 C ATOM 3583 OG SER B 249 13.813 34.235 -28.169 1.00164.29 O ANISOU 3583 OG SER B 249 16327 19624 26473 -493 3558 -105 O ATOM 3584 N VAL B 250 9.719 34.249 -25.700 1.00123.62 N ANISOU 3584 N VAL B 250 12054 15185 19730 -184 1969 222 N ATOM 3585 CA VAL B 250 8.272 34.137 -25.590 1.00112.09 C ANISOU 3585 CA VAL B 250 10994 13872 17722 -256 1776 118 C ATOM 3586 C VAL B 250 7.683 35.285 -24.772 1.00103.75 C ANISOU 3586 C VAL B 250 10039 13155 16226 -217 1089 263 C ATOM 3587 O VAL B 250 8.064 35.507 -23.623 1.00104.73 O ANISOU 3587 O VAL B 250 9909 13369 16514 -3 702 540 O ATOM 3588 CB VAL B 250 7.852 32.782 -24.982 1.00109.96 C ANISOU 3588 CB VAL B 250 10674 13401 17703 -35 1951 209 C ATOM 3589 CG1 VAL B 250 8.715 32.442 -23.775 1.00112.11 C ANISOU 3589 CG1 VAL B 250 10476 13597 18524 328 1728 620 C ATOM 3590 CG2 VAL B 250 6.375 32.792 -24.616 1.00105.62 C ANISOU 3590 CG2 VAL B 250 10482 13056 16592 -81 1642 146 C ATOM 3591 N MET B 251 6.758 36.019 -25.381 1.00 95.58 N ANISOU 3591 N MET B 251 9370 12302 14643 -455 958 85 N ATOM 3592 CA MET B 251 6.093 37.122 -24.704 1.00 87.09 C ANISOU 3592 CA MET B 251 8414 11485 13190 -429 400 187 C ATOM 3593 C MET B 251 4.809 36.638 -24.051 1.00 81.46 C ANISOU 3593 C MET B 251 7878 10845 12228 -333 215 199 C ATOM 3594 O MET B 251 4.048 35.884 -24.652 1.00 82.42 O ANISOU 3594 O MET B 251 8204 10917 12196 -444 479 37 O ATOM 3595 CB MET B 251 5.791 38.250 -25.689 1.00 85.29 C ANISOU 3595 CB MET B 251 8440 11390 12576 -708 343 54 C ATOM 3596 CG MET B 251 5.065 39.422 -25.064 1.00 82.79 C ANISOU 3596 CG MET B 251 8244 11272 11939 -674 -153 153 C ATOM 3597 SD MET B 251 5.404 40.984 -25.893 1.00114.71 S ANISOU 3597 SD MET B 251 12411 15398 15775 -909 -256 131 S ATOM 3598 CE MET B 251 5.848 41.994 -24.481 1.00111.07 C ANISOU 3598 CE MET B 251 11770 15015 15418 -737 -681 301 C ATOM 3599 N VAL B 252 4.570 37.065 -22.817 1.00 77.44 N ANISOU 3599 N VAL B 252 7301 10460 11663 -172 -216 372 N ATOM 3600 CA VAL B 252 3.397 36.614 -22.082 1.00 75.28 C ANISOU 3600 CA VAL B 252 7178 10245 11178 -85 -382 378 C ATOM 3601 C VAL B 252 2.473 37.780 -21.737 1.00 74.01 C ANISOU 3601 C VAL B 252 7204 10276 10640 -145 -755 355 C ATOM 3602 O VAL B 252 2.605 38.402 -20.684 1.00 74.02 O ANISOU 3602 O VAL B 252 7132 10361 10633 -77 -1071 474 O ATOM 3603 CB VAL B 252 3.792 35.867 -20.793 1.00 74.64 C ANISOU 3603 CB VAL B 252 6875 10111 11376 138 -510 605 C ATOM 3604 CG1 VAL B 252 2.662 34.957 -20.350 1.00 72.21 C ANISOU 3604 CG1 VAL B 252 6742 9777 10916 200 -481 559 C ATOM 3605 CG2 VAL B 252 5.063 35.059 -21.015 1.00 77.17 C ANISOU 3605 CG2 VAL B 252 6880 10221 12219 245 -201 730 C ATOM 3606 N LEU B 253 1.535 38.069 -22.633 1.00 73.17 N ANISOU 3606 N LEU B 253 7330 10234 10235 -300 -698 214 N ATOM 3607 CA LEU B 253 0.599 39.169 -22.438 1.00 71.21 C ANISOU 3607 CA LEU B 253 7224 10119 9713 -335 -998 220 C ATOM 3608 C LEU B 253 -0.631 38.722 -21.660 1.00 72.24 C ANISOU 3608 C LEU B 253 7450 10299 9699 -247 -1120 195 C ATOM 3609 O LEU B 253 -0.955 37.535 -21.621 1.00 74.96 O ANISOU 3609 O LEU B 253 7821 10600 10060 -218 -940 140 O ATOM 3610 CB LEU B 253 0.173 39.746 -23.788 1.00 68.74 C ANISOU 3610 CB LEU B 253 7071 9874 9175 -551 -926 160 C ATOM 3611 CG LEU B 253 1.306 40.273 -24.667 1.00 68.45 C ANISOU 3611 CG LEU B 253 6990 9791 9228 -696 -783 158 C ATOM 3612 CD1 LEU B 253 0.780 40.695 -26.027 1.00 67.66 C ANISOU 3612 CD1 LEU B 253 7086 9783 8841 -968 -717 126 C ATOM 3613 CD2 LEU B 253 2.009 41.428 -23.976 1.00 68.32 C ANISOU 3613 CD2 LEU B 253 6861 9766 9331 -615 -1018 260 C ATOM 3614 N SER B 254 -1.317 39.683 -21.052 1.00 69.49 N ANISOU 3614 N SER B 254 7158 10017 9229 -218 -1381 219 N ATOM 3615 CA SER B 254 -2.511 39.393 -20.269 1.00 66.19 C ANISOU 3615 CA SER B 254 6822 9638 8690 -151 -1481 173 C ATOM 3616 C SER B 254 -3.445 40.591 -20.161 1.00 65.56 C ANISOU 3616 C SER B 254 6810 9596 8504 -164 -1660 173 C ATOM 3617 O SER B 254 -3.004 41.738 -20.080 1.00 64.22 O ANISOU 3617 O SER B 254 6617 9389 8395 -181 -1762 223 O ATOM 3618 CB SER B 254 -2.128 38.926 -18.866 1.00 65.52 C ANISOU 3618 CB SER B 254 6666 9520 8708 -48 -1575 222 C ATOM 3619 OG SER B 254 -3.215 39.078 -17.971 1.00 64.15 O ANISOU 3619 OG SER B 254 6593 9380 8402 -29 -1700 160 O ATOM 3620 N ALA B 255 -4.743 40.306 -20.157 1.00 65.95 N ANISOU 3620 N ALA B 255 6927 9700 8429 -157 -1670 119 N ATOM 3621 CA ALA B 255 -5.761 41.317 -19.912 1.00 65.88 C ANISOU 3621 CA ALA B 255 6933 9688 8411 -127 -1804 134 C ATOM 3622 C ALA B 255 -7.008 40.647 -19.359 1.00 66.45 C ANISOU 3622 C ALA B 255 7039 9804 8406 -88 -1791 41 C ATOM 3623 O ALA B 255 -7.205 39.445 -19.531 1.00 65.88 O ANISOU 3623 O ALA B 255 7004 9794 8233 -121 -1678 -22 O ATOM 3624 CB ALA B 255 -6.085 42.072 -21.185 1.00 66.21 C ANISOU 3624 CB ALA B 255 6965 9781 8410 -207 -1842 255 C ATOM 3625 N THR B 256 -7.844 41.426 -18.686 1.00 68.05 N ANISOU 3625 N THR B 256 7229 9948 8679 -32 -1863 16 N ATOM 3626 CA THR B 256 -9.104 40.914 -18.168 1.00 66.00 C ANISOU 3626 CA THR B 256 6980 9723 8373 -6 -1834 -85 C ATOM 3627 C THR B 256 -10.254 41.564 -18.914 1.00 66.41 C ANISOU 3627 C THR B 256 6928 9824 8482 8 -1891 17 C ATOM 3628 O THR B 256 -10.328 42.787 -19.019 1.00 66.29 O ANISOU 3628 O THR B 256 6843 9699 8644 62 -1946 122 O ATOM 3629 CB THR B 256 -9.257 41.186 -16.664 1.00 64.84 C ANISOU 3629 CB THR B 256 6890 9458 8288 17 -1823 -219 C ATOM 3630 OG1 THR B 256 -8.124 40.660 -15.963 1.00 63.90 O ANISOU 3630 OG1 THR B 256 6835 9331 8112 -23 -1836 -232 O ATOM 3631 CG2 THR B 256 -10.523 40.539 -16.135 1.00 63.45 C ANISOU 3631 CG2 THR B 256 6736 9314 8057 21 -1756 -351 C ATOM 3632 N HIS B 257 -11.146 40.739 -19.445 1.00 68.44 N ANISOU 3632 N HIS B 257 7159 10244 8601 -54 -1873 8 N ATOM 3633 CA HIS B 257 -12.283 41.246 -20.195 1.00 73.39 C ANISOU 3633 CA HIS B 257 7634 10978 9274 -67 -1973 167 C ATOM 3634 C HIS B 257 -13.578 40.725 -19.600 1.00 76.00 C ANISOU 3634 C HIS B 257 7901 11360 9614 -45 -1929 50 C ATOM 3635 O HIS B 257 -13.601 39.650 -19.000 1.00 77.74 O ANISOU 3635 O HIS B 257 8242 11605 9691 -86 -1813 -149 O ATOM 3636 CB HIS B 257 -12.166 40.848 -21.663 1.00 74.18 C ANISOU 3636 CB HIS B 257 7736 11304 9145 -263 -2024 311 C ATOM 3637 CG HIS B 257 -10.931 41.369 -22.326 1.00 75.08 C ANISOU 3637 CG HIS B 257 7913 11364 9248 -315 -2038 412 C ATOM 3638 ND1 HIS B 257 -10.901 42.567 -23.007 1.00 76.51 N ANISOU 3638 ND1 HIS B 257 8010 11524 9535 -313 -2181 659 N ATOM 3639 CD2 HIS B 257 -9.677 40.864 -22.397 1.00 74.59 C ANISOU 3639 CD2 HIS B 257 7975 11252 9116 -369 -1911 309 C ATOM 3640 CE1 HIS B 257 -9.684 42.772 -23.478 1.00 76.30 C ANISOU 3640 CE1 HIS B 257 8080 11450 9460 -389 -2138 673 C ATOM 3641 NE2 HIS B 257 -8.922 41.754 -23.121 1.00 75.12 N ANISOU 3641 NE2 HIS B 257 8038 11283 9219 -419 -1970 459 N ATOM 3642 N ARG B 258 -14.654 41.489 -19.753 1.00 75.84 N ANISOU 3642 N ARG B 258 7675 11342 9798 25 -2009 192 N ATOM 3643 CA ARG B 258 -15.936 41.065 -19.221 1.00 75.46 C ANISOU 3643 CA ARG B 258 7522 11345 9806 43 -1953 84 C ATOM 3644 C ARG B 258 -16.875 40.589 -20.320 1.00 74.57 C ANISOU 3644 C ARG B 258 7246 11548 9538 -106 -2080 255 C ATOM 3645 O ARG B 258 -16.801 41.039 -21.461 1.00 74.32 O ANISOU 3645 O ARG B 258 7114 11663 9462 -191 -2253 540 O ATOM 3646 CB ARG B 258 -16.592 42.178 -18.399 1.00 80.42 C ANISOU 3646 CB ARG B 258 7995 11717 10845 224 -1886 83 C ATOM 3647 CG ARG B 258 -17.314 43.240 -19.209 1.00 87.78 C ANISOU 3647 CG ARG B 258 8621 12645 12087 321 -2024 429 C ATOM 3648 CD ARG B 258 -18.609 43.652 -18.520 1.00 93.84 C ANISOU 3648 CD ARG B 258 9145 13266 13243 457 -1902 393 C ATOM 3649 NE ARG B 258 -18.381 44.148 -17.165 1.00 97.74 N ANISOU 3649 NE ARG B 258 9776 13407 13954 538 -1632 98 N ATOM 3650 CZ ARG B 258 -18.583 45.407 -16.785 1.00104.49 C ANISOU 3650 CZ ARG B 258 10503 13925 15274 687 -1483 152 C ATOM 3651 NH1 ARG B 258 -19.031 46.299 -17.658 1.00109.45 N ANISOU 3651 NH1 ARG B 258 10832 14505 16249 829 -1602 540 N ATOM 3652 NH2 ARG B 258 -18.349 45.772 -15.531 1.00104.94 N ANISOU 3652 NH2 ARG B 258 10738 13686 15450 666 -1198 -171 N ATOM 3653 N TYR B 259 -17.747 39.656 -19.961 1.00 75.35 N ANISOU 3653 N TYR B 259 7335 11772 9521 -184 -1995 82 N ATOM 3654 CA TYR B 259 -18.814 39.206 -20.841 1.00 77.07 C ANISOU 3654 CA TYR B 259 7370 12321 9593 -366 -2112 222 C ATOM 3655 C TYR B 259 -20.107 39.213 -20.043 1.00 77.67 C ANISOU 3655 C TYR B 259 7241 12365 9904 -269 -2046 127 C ATOM 3656 O TYR B 259 -20.270 38.425 -19.110 1.00 74.66 O ANISOU 3656 O TYR B 259 7017 11909 9439 -281 -1848 -190 O ATOM 3657 CB TYR B 259 -18.528 37.804 -21.381 1.00 75.55 C ANISOU 3657 CB TYR B 259 7403 12357 8945 -653 -2015 56 C ATOM 3658 CG TYR B 259 -19.613 37.288 -22.291 1.00 77.24 C ANISOU 3658 CG TYR B 259 7458 12958 8931 -934 -2123 170 C ATOM 3659 CD1 TYR B 259 -19.768 37.799 -23.569 1.00 79.21 C ANISOU 3659 CD1 TYR B 259 7548 13475 9073 -1123 -2372 519 C ATOM 3660 CD2 TYR B 259 -20.487 36.298 -21.868 1.00 78.44 C ANISOU 3660 CD2 TYR B 259 7622 13232 8950 -1052 -1989 -58 C ATOM 3661 CE1 TYR B 259 -20.763 37.339 -24.406 1.00 82.97 C ANISOU 3661 CE1 TYR B 259 7866 14364 9294 -1449 -2509 655 C ATOM 3662 CE2 TYR B 259 -21.487 35.828 -22.700 1.00 81.38 C ANISOU 3662 CE2 TYR B 259 7836 13999 9086 -1361 -2096 43 C ATOM 3663 CZ TYR B 259 -21.619 36.353 -23.968 1.00 84.04 C ANISOU 3663 CZ TYR B 259 8002 14632 9300 -1571 -2369 408 C ATOM 3664 OH TYR B 259 -22.609 35.896 -24.805 1.00 88.15 O ANISOU 3664 OH TYR B 259 8353 15602 9539 -1946 -2514 541 O ATOM 3665 N LYS B 260 -21.019 40.107 -20.417 1.00 82.22 N ANISOU 3665 N LYS B 260 7452 12986 10800 -177 -2202 424 N ATOM 3666 CA LYS B 260 -22.207 40.385 -19.619 1.00 85.52 C ANISOU 3666 CA LYS B 260 7609 13292 11592 -31 -2099 359 C ATOM 3667 C LYS B 260 -21.797 40.695 -18.184 1.00 86.15 C ANISOU 3667 C LYS B 260 7886 12961 11887 145 -1816 27 C ATOM 3668 O LYS B 260 -21.327 41.793 -17.887 1.00 88.32 O ANISOU 3668 O LYS B 260 8144 12939 12475 321 -1771 101 O ATOM 3669 CB LYS B 260 -23.195 39.215 -19.646 1.00 84.53 C ANISOU 3669 CB LYS B 260 7430 13468 11219 -242 -2064 206 C ATOM 3670 CG LYS B 260 -23.831 38.938 -20.996 1.00 86.61 C ANISOU 3670 CG LYS B 260 7456 14192 11261 -495 -2344 533 C ATOM 3671 CD LYS B 260 -25.065 38.064 -20.826 1.00 89.09 C ANISOU 3671 CD LYS B 260 7611 14763 11477 -668 -2289 391 C ATOM 3672 CE LYS B 260 -25.693 37.698 -22.161 1.00 93.78 C ANISOU 3672 CE LYS B 260 7987 15883 11764 -1018 -2578 703 C ATOM 3673 NZ LYS B 260 -24.825 36.772 -22.939 1.00 93.31 N ANISOU 3673 NZ LYS B 260 8321 16036 11097 -1371 -2555 579 N ATOM 3674 N LYS B 261 -21.963 39.715 -17.302 1.00 84.09 N ANISOU 3674 N LYS B 261 7836 12692 11424 51 -1619 -337 N ATOM 3675 CA LYS B 261 -21.566 39.869 -15.908 1.00 82.41 C ANISOU 3675 CA LYS B 261 7856 12150 11305 119 -1369 -657 C ATOM 3676 C LYS B 261 -20.605 38.765 -15.476 1.00 77.99 C ANISOU 3676 C LYS B 261 7697 11627 10308 -20 -1310 -884 C ATOM 3677 O LYS B 261 -20.509 38.435 -14.294 1.00 76.38 O ANISOU 3677 O LYS B 261 7708 11266 10048 -62 -1126 -1160 O ATOM 3678 CB LYS B 261 -22.793 39.913 -14.995 1.00 85.39 C ANISOU 3678 CB LYS B 261 8080 12407 11958 146 -1142 -869 C ATOM 3679 CG LYS B 261 -23.603 41.193 -15.122 1.00 90.34 C ANISOU 3679 CG LYS B 261 8297 12849 13180 346 -1106 -660 C ATOM 3680 CD LYS B 261 -24.784 41.204 -14.168 1.00 94.46 C ANISOU 3680 CD LYS B 261 8662 13211 14018 361 -808 -915 C ATOM 3681 CE LYS B 261 -25.583 42.491 -14.298 1.00100.71 C ANISOU 3681 CE LYS B 261 8997 13756 15512 594 -718 -683 C ATOM 3682 NZ LYS B 261 -26.102 42.693 -15.681 1.00104.44 N ANISOU 3682 NZ LYS B 261 9040 14523 16120 675 -1072 -169 N ATOM 3683 N LYS B 262 -19.898 38.198 -16.447 1.00 76.54 N ANISOU 3683 N LYS B 262 7608 11643 9832 -111 -1453 -748 N ATOM 3684 CA LYS B 262 -18.864 37.210 -16.169 1.00 74.36 C ANISOU 3684 CA LYS B 262 7658 11356 9238 -202 -1384 -892 C ATOM 3685 C LYS B 262 -17.513 37.756 -16.611 1.00 75.14 C ANISOU 3685 C LYS B 262 7834 11376 9340 -142 -1489 -730 C ATOM 3686 O LYS B 262 -17.408 38.400 -17.655 1.00 77.41 O ANISOU 3686 O LYS B 262 7970 11752 9690 -129 -1637 -493 O ATOM 3687 CB LYS B 262 -19.157 35.890 -16.886 1.00 72.44 C ANISOU 3687 CB LYS B 262 7487 11369 8669 -397 -1350 -939 C ATOM 3688 CG LYS B 262 -20.438 35.205 -16.442 1.00 72.83 C ANISOU 3688 CG LYS B 262 7487 11519 8668 -495 -1228 -1127 C ATOM 3689 CD LYS B 262 -20.439 34.943 -14.948 1.00 71.19 C ANISOU 3689 CD LYS B 262 7476 11081 8491 -456 -1046 -1387 C ATOM 3690 CE LYS B 262 -21.727 34.277 -14.499 1.00 71.78 C ANISOU 3690 CE LYS B 262 7511 11244 8519 -572 -896 -1597 C ATOM 3691 NZ LYS B 262 -21.908 32.937 -15.123 1.00 71.59 N ANISOU 3691 NZ LYS B 262 7608 11435 8158 -777 -826 -1665 N ATOM 3692 N TYR B 263 -16.482 37.502 -15.814 1.00 73.29 N ANISOU 3692 N TYR B 263 7823 10990 9034 -128 -1426 -836 N ATOM 3693 CA TYR B 263 -15.146 37.984 -16.138 1.00 70.98 C ANISOU 3693 CA TYR B 263 7584 10625 8760 -83 -1512 -699 C ATOM 3694 C TYR B 263 -14.208 36.849 -16.525 1.00 68.93 C ANISOU 3694 C TYR B 263 7478 10428 8285 -157 -1464 -697 C ATOM 3695 O TYR B 263 -14.301 35.738 -15.998 1.00 67.78 O ANISOU 3695 O TYR B 263 7468 10281 8003 -212 -1343 -828 O ATOM 3696 CB TYR B 263 -14.560 38.773 -14.968 1.00 71.33 C ANISOU 3696 CB TYR B 263 7711 10452 8940 -31 -1494 -770 C ATOM 3697 CG TYR B 263 -15.374 39.984 -14.585 1.00 74.22 C ANISOU 3697 CG TYR B 263 7939 10674 9589 35 -1449 -799 C ATOM 3698 CD1 TYR B 263 -15.296 41.156 -15.321 1.00 76.37 C ANISOU 3698 CD1 TYR B 263 8043 10881 10092 132 -1528 -603 C ATOM 3699 CD2 TYR B 263 -16.225 39.954 -13.490 1.00 76.90 C ANISOU 3699 CD2 TYR B 263 8317 10909 9994 -7 -1287 -1022 C ATOM 3700 CE1 TYR B 263 -16.040 42.267 -14.976 1.00 79.33 C ANISOU 3700 CE1 TYR B 263 8270 11060 10812 218 -1432 -610 C ATOM 3701 CE2 TYR B 263 -16.973 41.061 -13.136 1.00 80.30 C ANISOU 3701 CE2 TYR B 263 8604 11149 10756 55 -1165 -1070 C ATOM 3702 CZ TYR B 263 -16.876 42.214 -13.884 1.00 81.26 C ANISOU 3702 CZ TYR B 263 8537 11177 11159 184 -1230 -854 C ATOM 3703 OH TYR B 263 -17.616 43.318 -13.538 1.00 85.03 O ANISOU 3703 OH TYR B 263 8853 11405 12049 271 -1057 -882 O ATOM 3704 N VAL B 264 -13.303 37.142 -17.451 1.00 69.05 N ANISOU 3704 N VAL B 264 7466 10469 8301 -161 -1526 -544 N ATOM 3705 CA VAL B 264 -12.307 36.171 -17.885 1.00 69.37 C ANISOU 3705 CA VAL B 264 7617 10513 8226 -221 -1421 -541 C ATOM 3706 C VAL B 264 -10.953 36.834 -18.115 1.00 66.52 C ANISOU 3706 C VAL B 264 7235 10060 7980 -164 -1487 -410 C ATOM 3707 O VAL B 264 -10.832 37.780 -18.895 1.00 66.84 O ANISOU 3707 O VAL B 264 7187 10136 8071 -173 -1587 -287 O ATOM 3708 CB VAL B 264 -12.762 35.410 -19.156 1.00 70.00 C ANISOU 3708 CB VAL B 264 7706 10779 8112 -406 -1320 -551 C ATOM 3709 CG1 VAL B 264 -13.362 36.369 -20.173 1.00 72.00 C ANISOU 3709 CG1 VAL B 264 7803 11199 8353 -478 -1489 -391 C ATOM 3710 CG2 VAL B 264 -11.606 34.619 -19.755 1.00 68.57 C ANISOU 3710 CG2 VAL B 264 7627 10539 7888 -478 -1138 -555 C ATOM 3711 N THR B 265 -9.937 36.338 -17.420 1.00 64.10 N ANISOU 3711 N THR B 265 6994 9638 7725 -112 -1440 -411 N ATOM 3712 CA THR B 265 -8.592 36.876 -17.556 1.00 65.08 C ANISOU 3712 CA THR B 265 7066 9688 7973 -70 -1497 -288 C ATOM 3713 C THR B 265 -7.769 36.009 -18.504 1.00 62.33 C ANISOU 3713 C THR B 265 6720 9328 7635 -119 -1316 -256 C ATOM 3714 O THR B 265 -7.227 34.977 -18.109 1.00 61.35 O ANISOU 3714 O THR B 265 6621 9112 7576 -80 -1182 -254 O ATOM 3715 CB THR B 265 -7.890 36.976 -16.192 1.00 67.88 C ANISOU 3715 CB THR B 265 7437 9950 8403 -17 -1588 -257 C ATOM 3716 OG1 THR B 265 -8.764 37.614 -15.250 1.00 67.83 O ANISOU 3716 OG1 THR B 265 7478 9933 8362 -35 -1665 -357 O ATOM 3717 CG2 THR B 265 -6.595 37.769 -16.309 1.00 67.83 C ANISOU 3717 CG2 THR B 265 7342 9906 8525 -3 -1683 -129 C ATOM 3718 N THR B 266 -7.682 36.441 -19.757 1.00 61.36 N ANISOU 3718 N THR B 266 6570 9280 7465 -220 -1290 -221 N ATOM 3719 CA THR B 266 -7.017 35.668 -20.797 1.00 61.08 C ANISOU 3719 CA THR B 266 6565 9227 7414 -341 -1046 -245 C ATOM 3720 C THR B 266 -5.504 35.853 -20.771 1.00 59.50 C ANISOU 3720 C THR B 266 6277 8892 7438 -266 -1003 -155 C ATOM 3721 O THR B 266 -5.003 36.969 -20.641 1.00 58.41 O ANISOU 3721 O THR B 266 6065 8753 7375 -219 -1188 -60 O ATOM 3722 CB THR B 266 -7.537 36.055 -22.190 1.00 63.39 C ANISOU 3722 CB THR B 266 6889 9691 7505 -566 -1038 -240 C ATOM 3723 OG1 THR B 266 -8.968 36.128 -22.164 1.00 63.96 O ANISOU 3723 OG1 THR B 266 6967 9926 7409 -622 -1158 -259 O ATOM 3724 CG2 THR B 266 -7.092 35.032 -23.225 1.00 65.16 C ANISOU 3724 CG2 THR B 266 7208 9905 7644 -787 -696 -348 C ATOM 3725 N LEU B 267 -4.784 34.744 -20.893 1.00 61.36 N ANISOU 3725 N LEU B 267 6504 8995 7813 -258 -730 -181 N ATOM 3726 CA LEU B 267 -3.327 34.769 -20.941 1.00 64.02 C ANISOU 3726 CA LEU B 267 6701 9195 8429 -184 -643 -80 C ATOM 3727 C LEU B 267 -2.852 34.243 -22.287 1.00 68.40 C ANISOU 3727 C LEU B 267 7293 9684 9012 -365 -271 -184 C ATOM 3728 O LEU B 267 -3.384 33.256 -22.799 1.00 70.42 O ANISOU 3728 O LEU B 267 7676 9914 9165 -502 20 -331 O ATOM 3729 CB LEU B 267 -2.727 33.927 -19.812 1.00 62.84 C ANISOU 3729 CB LEU B 267 6445 8896 8533 5 -621 38 C ATOM 3730 CG LEU B 267 -2.599 34.543 -18.416 1.00 59.38 C ANISOU 3730 CG LEU B 267 5935 8514 8114 124 -983 187 C ATOM 3731 CD1 LEU B 267 -3.948 34.922 -17.833 1.00 59.00 C ANISOU 3731 CD1 LEU B 267 6042 8585 7792 85 -1163 81 C ATOM 3732 CD2 LEU B 267 -1.892 33.573 -17.495 1.00 60.96 C ANISOU 3732 CD2 LEU B 267 6011 8588 8563 262 -957 373 C ATOM 3733 N LEU B 268 -1.852 34.902 -22.862 1.00 69.45 N ANISOU 3733 N LEU B 268 7334 9787 9268 -408 -245 -135 N ATOM 3734 CA LEU B 268 -1.342 34.507 -24.169 1.00 70.94 C ANISOU 3734 CA LEU B 268 7578 9906 9471 -637 144 -263 C ATOM 3735 C LEU B 268 0.177 34.367 -24.188 1.00 71.90 C ANISOU 3735 C LEU B 268 7490 9821 10008 -537 350 -197 C ATOM 3736 O LEU B 268 0.907 35.289 -23.821 1.00 71.49 O ANISOU 3736 O LEU B 268 7285 9797 10082 -433 106 -58 O ATOM 3737 CB LEU B 268 -1.796 35.497 -25.246 1.00 70.57 C ANISOU 3737 CB LEU B 268 7664 10062 9088 -905 26 -295 C ATOM 3738 CG LEU B 268 -1.264 35.236 -26.657 1.00 73.15 C ANISOU 3738 CG LEU B 268 8093 10356 9344 -1241 416 -440 C ATOM 3739 CD1 LEU B 268 -1.692 33.861 -27.149 1.00 74.14 C ANISOU 3739 CD1 LEU B 268 8369 10415 9386 -1449 856 -653 C ATOM 3740 CD2 LEU B 268 -1.711 36.322 -27.625 1.00 66.35 C ANISOU 3740 CD2 LEU B 268 7360 9727 8124 -1517 209 -389 C ATOM 3741 N TYR B 269 0.643 33.200 -24.614 1.00 72.40 N ANISOU 3741 N TYR B 269 7535 9662 10312 -580 833 -303 N ATOM 3742 CA TYR B 269 2.061 32.974 -24.847 1.00 74.73 C ANISOU 3742 CA TYR B 269 7602 9727 11064 -512 1130 -259 C ATOM 3743 C TYR B 269 2.319 33.099 -26.341 1.00 76.22 C ANISOU 3743 C TYR B 269 7942 9898 11119 -878 1518 -491 C ATOM 3744 O TYR B 269 1.623 32.489 -27.150 1.00 77.33 O ANISOU 3744 O TYR B 269 8332 10052 10996 -1170 1830 -714 O ATOM 3745 CB TYR B 269 2.476 31.587 -24.349 1.00 78.09 C ANISOU 3745 CB TYR B 269 7879 9848 11945 -310 1486 -206 C ATOM 3746 CG TYR B 269 2.512 31.456 -22.841 1.00 77.95 C ANISOU 3746 CG TYR B 269 7671 9839 12110 27 1099 91 C ATOM 3747 CD1 TYR B 269 1.342 31.482 -22.091 1.00 75.96 C ANISOU 3747 CD1 TYR B 269 7594 9758 11511 60 775 102 C ATOM 3748 CD2 TYR B 269 3.716 31.295 -22.169 1.00 74.03 C ANISOU 3748 CD2 TYR B 269 6808 9192 12126 277 1059 373 C ATOM 3749 CE1 TYR B 269 1.371 31.362 -20.716 1.00 68.97 C ANISOU 3749 CE1 TYR B 269 6575 8892 10737 295 439 357 C ATOM 3750 CE2 TYR B 269 3.754 31.172 -20.793 1.00 73.79 C ANISOU 3750 CE2 TYR B 269 6619 9216 12203 511 672 678 C ATOM 3751 CZ TYR B 269 2.579 31.206 -20.074 1.00 71.23 C ANISOU 3751 CZ TYR B 269 6525 9059 11479 501 374 654 C ATOM 3752 OH TYR B 269 2.613 31.084 -18.706 1.00 96.80 O ANISOU 3752 OH TYR B 269 9645 12362 14773 665 7 942 O ATOM 3753 N LYS B 270 3.315 33.895 -26.709 1.00 73.18 N ANISOU 3753 N LYS B 270 7422 9503 10881 -913 1503 -448 N ATOM 3754 CA LYS B 270 3.569 34.180 -28.113 1.00 76.45 C ANISOU 3754 CA LYS B 270 8009 9932 11107 -1310 1827 -658 C ATOM 3755 C LYS B 270 5.055 34.393 -28.390 1.00 78.42 C ANISOU 3755 C LYS B 270 8009 9987 11798 -1280 2085 -649 C ATOM 3756 O LYS B 270 5.686 35.257 -27.779 1.00 76.49 O ANISOU 3756 O LYS B 270 7546 9809 11709 -1080 1729 -450 O ATOM 3757 CB LYS B 270 2.769 35.409 -28.543 1.00 76.11 C ANISOU 3757 CB LYS B 270 8182 10214 10523 -1518 1398 -619 C ATOM 3758 CG LYS B 270 3.003 35.853 -29.977 1.00 81.50 C ANISOU 3758 CG LYS B 270 9066 10965 10935 -1974 1640 -775 C ATOM 3759 CD LYS B 270 2.204 37.110 -30.291 1.00 82.51 C ANISOU 3759 CD LYS B 270 9359 11398 10592 -2121 1153 -633 C ATOM 3760 CE LYS B 270 2.406 37.557 -31.729 1.00 87.01 C ANISOU 3760 CE LYS B 270 10153 12065 10840 -2621 1352 -737 C ATOM 3761 NZ LYS B 270 1.584 38.758 -32.054 1.00 87.32 N ANISOU 3761 NZ LYS B 270 10331 12386 10461 -2750 862 -522 N ATOM 3762 N PRO B 271 5.618 33.595 -29.312 1.00 81.61 N ANISOU 3762 N PRO B 271 8446 10145 12417 -1510 2743 -885 N ATOM 3763 CA PRO B 271 7.020 33.700 -29.730 1.00 84.78 C ANISOU 3763 CA PRO B 271 8606 10327 13281 -1529 3106 -927 C ATOM 3764 C PRO B 271 7.354 35.085 -30.272 1.00 85.01 C ANISOU 3764 C PRO B 271 8708 10571 13019 -1739 2836 -917 C ATOM 3765 O PRO B 271 6.665 35.539 -31.185 1.00 85.82 O ANISOU 3765 O PRO B 271 9166 10870 12570 -2133 2810 -1056 O ATOM 3766 CB PRO B 271 7.122 32.664 -30.852 1.00 88.30 C ANISOU 3766 CB PRO B 271 9238 10511 13801 -1895 3908 -1282 C ATOM 3767 CG PRO B 271 6.072 31.662 -30.525 1.00 87.65 C ANISOU 3767 CG PRO B 271 9325 10400 13576 -1859 3986 -1335 C ATOM 3768 CD PRO B 271 4.938 32.453 -29.948 1.00 83.33 C ANISOU 3768 CD PRO B 271 8925 10250 12488 -1779 3243 -1150 C TER 3769 PRO B 271 ATOM 3770 N PRO C 528 -14.565 34.186 -36.541 1.00108.48 N ANISOU 3770 N PRO C 528 12720 17633 10864 599 -3291 960 N ATOM 3771 CA PRO C 528 -13.818 35.173 -37.328 1.00107.98 C ANISOU 3771 CA PRO C 528 12831 17127 11070 1020 -2969 1131 C ATOM 3772 C PRO C 528 -12.721 35.850 -36.511 1.00102.24 C ANISOU 3772 C PRO C 528 12066 15744 11035 1395 -2551 842 C ATOM 3773 O PRO C 528 -12.507 37.053 -36.653 1.00102.42 O ANISOU 3773 O PRO C 528 11960 15531 11426 1850 -2273 1001 O ATOM 3774 CB PRO C 528 -14.895 36.190 -37.715 1.00112.12 C ANISOU 3774 CB PRO C 528 12869 18158 11573 1366 -3106 1663 C ATOM 3775 CG PRO C 528 -16.146 35.385 -37.784 1.00115.78 C ANISOU 3775 CG PRO C 528 13094 19440 11455 906 -3601 1853 C ATOM 3776 CD PRO C 528 -16.022 34.344 -36.697 1.00112.92 C ANISOU 3776 CD PRO C 528 12835 18929 11140 521 -3625 1331 C ATOM 3777 N GLY C 529 -12.039 35.080 -35.669 1.00 97.01 N ANISOU 3777 N GLY C 529 11523 14815 10522 1169 -2501 453 N ATOM 3778 CA GLY C 529 -10.954 35.605 -34.860 1.00 92.38 C ANISOU 3778 CA GLY C 529 10876 13713 10511 1384 -2170 204 C ATOM 3779 C GLY C 529 -11.431 36.188 -33.546 1.00 88.95 C ANISOU 3779 C GLY C 529 9975 13432 10390 1481 -2169 89 C ATOM 3780 O GLY C 529 -12.530 36.728 -33.463 1.00 92.15 O ANISOU 3780 O GLY C 529 10053 14211 10748 1639 -2255 295 O ATOM 3781 N SER C 530 -10.601 36.079 -32.515 1.00 84.41 N ANISOU 3781 N SER C 530 9362 12581 10131 1367 -2046 -209 N ATOM 3782 CA SER C 530 -10.938 36.605 -31.198 1.00 85.04 C ANISOU 3782 CA SER C 530 9096 12751 10463 1340 -1991 -379 C ATOM 3783 C SER C 530 -10.550 38.072 -31.067 1.00 85.39 C ANISOU 3783 C SER C 530 9078 12447 10919 1657 -1538 -378 C ATOM 3784 O SER C 530 -9.415 38.447 -31.348 1.00 86.72 O ANISOU 3784 O SER C 530 9444 12203 11304 1718 -1279 -438 O ATOM 3785 CB SER C 530 -10.247 35.790 -30.104 1.00 85.59 C ANISOU 3785 CB SER C 530 9164 12752 10603 969 -2106 -663 C ATOM 3786 OG SER C 530 -10.418 36.395 -28.835 1.00 87.05 O ANISOU 3786 OG SER C 530 9093 12974 11007 858 -2001 -856 O ATOM 3787 N HIS C 531 -11.498 38.894 -30.631 1.00 85.43 N ANISOU 3787 N HIS C 531 8822 12597 11039 1849 -1385 -305 N ATOM 3788 CA HIS C 531 -11.257 40.320 -30.442 1.00 86.92 C ANISOU 3788 CA HIS C 531 9022 12397 11608 2140 -843 -313 C ATOM 3789 C HIS C 531 -10.152 40.558 -29.416 1.00 80.53 C ANISOU 3789 C HIS C 531 8318 11250 11030 1799 -610 -701 C ATOM 3790 O HIS C 531 -9.306 41.439 -29.586 1.00 78.19 O ANISOU 3790 O HIS C 531 8209 10531 10967 1885 -204 -760 O ATOM 3791 CB HIS C 531 -12.547 41.016 -30.001 1.00 94.79 C ANISOU 3791 CB HIS C 531 9711 13592 12711 2396 -651 -160 C ATOM 3792 CG HIS C 531 -12.403 42.486 -29.781 1.00102.80 C ANISOU 3792 CG HIS C 531 10811 14130 14120 2710 30 -161 C ATOM 3793 ND1 HIS C 531 -11.932 43.348 -30.756 1.00107.58 N ANISOU 3793 ND1 HIS C 531 11644 14360 14871 3096 366 62 N ATOM 3794 CD2 HIS C 531 -12.672 43.262 -28.705 1.00106.01 C ANISOU 3794 CD2 HIS C 531 11178 14319 14783 2667 512 -372 C ATOM 3795 CE1 HIS C 531 -11.917 44.576 -30.287 1.00111.01 C ANISOU 3795 CE1 HIS C 531 12180 14358 15642 3291 1031 -6 C ATOM 3796 NE2 HIS C 531 -12.363 44.556 -29.039 1.00110.54 N ANISOU 3796 NE2 HIS C 531 11978 14370 15653 3023 1158 -279 N ATOM 3797 N THR C 532 -10.164 39.753 -28.359 1.00 77.35 N ANISOU 3797 N THR C 532 7793 11076 10521 1362 -888 -940 N ATOM 3798 CA THR C 532 -9.194 39.873 -27.278 1.00 74.41 C ANISOU 3798 CA THR C 532 7456 10529 10286 928 -771 -1250 C ATOM 3799 C THR C 532 -7.789 39.492 -27.729 1.00 74.59 C ANISOU 3799 C THR C 532 7611 10355 10373 828 -839 -1231 C ATOM 3800 O THR C 532 -6.824 40.189 -27.422 1.00 76.14 O ANISOU 3800 O THR C 532 7873 10291 10766 661 -546 -1355 O ATOM 3801 CB THR C 532 -9.598 39.008 -26.074 1.00 70.68 C ANISOU 3801 CB THR C 532 6817 10401 9636 474 -1109 -1442 C ATOM 3802 OG1 THR C 532 -10.806 39.527 -25.502 1.00 71.11 O ANISOU 3802 OG1 THR C 532 6738 10582 9698 530 -919 -1502 O ATOM 3803 CG2 THR C 532 -8.502 39.009 -25.024 1.00 70.43 C ANISOU 3803 CG2 THR C 532 6800 10284 9675 -47 -1091 -1676 C ATOM 3804 N ILE C 533 -7.674 38.389 -28.461 1.00 74.43 N ANISOU 3804 N ILE C 533 7644 10455 10183 901 -1177 -1069 N ATOM 3805 CA ILE C 533 -6.375 37.948 -28.960 1.00 74.39 C ANISOU 3805 CA ILE C 533 7751 10229 10284 877 -1167 -1002 C ATOM 3806 C ILE C 533 -5.808 38.948 -29.967 1.00 76.20 C ANISOU 3806 C ILE C 533 8173 10080 10698 1192 -761 -912 C ATOM 3807 O ILE C 533 -4.609 39.227 -29.964 1.00 76.88 O ANISOU 3807 O ILE C 533 8276 9933 11003 1097 -560 -946 O ATOM 3808 CB ILE C 533 -6.448 36.547 -29.603 1.00 73.22 C ANISOU 3808 CB ILE C 533 7728 10191 9901 898 -1478 -857 C ATOM 3809 CG1 ILE C 533 -6.970 35.523 -28.595 1.00 71.15 C ANISOU 3809 CG1 ILE C 533 7322 10267 9444 569 -1851 -945 C ATOM 3810 CG2 ILE C 533 -5.079 36.122 -30.112 1.00 73.91 C ANISOU 3810 CG2 ILE C 533 7926 9981 10176 934 -1344 -757 C ATOM 3811 CD1 ILE C 533 -6.099 35.382 -27.361 1.00 70.01 C ANISOU 3811 CD1 ILE C 533 6966 10156 9481 220 -1916 -1040 C ATOM 3812 N GLU C 534 -6.676 39.486 -30.822 1.00 77.36 N ANISOU 3812 N GLU C 534 8438 10204 10750 1554 -649 -757 N ATOM 3813 CA GLU C 534 -6.281 40.517 -31.780 1.00 79.08 C ANISOU 3813 CA GLU C 534 8874 10056 11117 1878 -246 -642 C ATOM 3814 C GLU C 534 -5.686 41.721 -31.058 1.00 80.66 C ANISOU 3814 C GLU C 534 9073 9967 11606 1762 202 -844 C ATOM 3815 O GLU C 534 -4.734 42.339 -31.536 1.00 81.74 O ANISOU 3815 O GLU C 534 9386 9760 11913 1807 534 -858 O ATOM 3816 CB GLU C 534 -7.479 40.963 -32.618 1.00 82.57 C ANISOU 3816 CB GLU C 534 9361 10612 11400 2277 -232 -363 C ATOM 3817 CG GLU C 534 -7.950 39.952 -33.648 1.00 84.29 C ANISOU 3817 CG GLU C 534 9692 11088 11245 2317 -606 -132 C ATOM 3818 CD GLU C 534 -9.224 40.392 -34.346 1.00 89.47 C ANISOU 3818 CD GLU C 534 10272 12022 11700 2633 -684 223 C ATOM 3819 OE1 GLU C 534 -9.647 41.553 -34.147 1.00 92.17 O ANISOU 3819 OE1 GLU C 534 10493 12253 12275 2946 -362 335 O ATOM 3820 OE2 GLU C 534 -9.805 39.575 -35.092 1.00 90.55 O ANISOU 3820 OE2 GLU C 534 10473 12498 11435 2546 -1040 422 O ATOM 3821 N PHE C 535 -6.259 42.045 -29.903 1.00 80.72 N ANISOU 3821 N PHE C 535 8925 10108 11636 1552 250 -1022 N ATOM 3822 CA PHE C 535 -5.752 43.122 -29.061 1.00 80.46 C ANISOU 3822 CA PHE C 535 8967 9814 11792 1278 711 -1276 C ATOM 3823 C PHE C 535 -4.353 42.791 -28.562 1.00 79.40 C ANISOU 3823 C PHE C 535 8762 9690 11715 785 617 -1427 C ATOM 3824 O PHE C 535 -3.474 43.651 -28.536 1.00 82.60 O ANISOU 3824 O PHE C 535 9306 9819 12260 607 1009 -1541 O ATOM 3825 CB PHE C 535 -6.694 43.359 -27.882 1.00 78.86 C ANISOU 3825 CB PHE C 535 8652 9763 11547 1074 785 -1456 C ATOM 3826 CG PHE C 535 -6.103 44.200 -26.788 1.00 79.10 C ANISOU 3826 CG PHE C 535 8809 9588 11659 549 1204 -1792 C ATOM 3827 CD1 PHE C 535 -5.829 45.540 -26.996 1.00 83.03 C ANISOU 3827 CD1 PHE C 535 9623 9603 12323 636 1888 -1874 C ATOM 3828 CD2 PHE C 535 -5.841 43.653 -25.543 1.00 77.04 C ANISOU 3828 CD2 PHE C 535 8397 9616 11258 -90 934 -2021 C ATOM 3829 CE1 PHE C 535 -5.292 46.317 -25.986 1.00 85.53 C ANISOU 3829 CE1 PHE C 535 10138 9725 12634 29 2322 -2221 C ATOM 3830 CE2 PHE C 535 -5.307 44.425 -24.530 1.00 79.21 C ANISOU 3830 CE2 PHE C 535 8828 9755 11513 -707 1306 -2332 C ATOM 3831 CZ PHE C 535 -5.032 45.757 -24.752 1.00 83.70 C ANISOU 3831 CZ PHE C 535 9748 9837 12216 -680 2016 -2454 C ATOM 3832 N PHE C 536 -4.156 41.537 -28.169 1.00 75.15 N ANISOU 3832 N PHE C 536 7994 9493 11066 561 110 -1387 N ATOM 3833 CA PHE C 536 -2.853 41.069 -27.720 1.00 73.93 C ANISOU 3833 CA PHE C 536 7659 9436 10994 161 -41 -1391 C ATOM 3834 C PHE C 536 -1.873 41.066 -28.884 1.00 73.94 C ANISOU 3834 C PHE C 536 7754 9172 11165 435 124 -1213 C ATOM 3835 O PHE C 536 -0.733 41.505 -28.753 1.00 74.73 O ANISOU 3835 O PHE C 536 7781 9185 11428 181 321 -1237 O ATOM 3836 CB PHE C 536 -2.963 39.656 -27.146 1.00 71.56 C ANISOU 3836 CB PHE C 536 7115 9512 10562 -18 -581 -1298 C ATOM 3837 CG PHE C 536 -3.616 39.595 -25.797 1.00 70.70 C ANISOU 3837 CG PHE C 536 6883 9696 10286 -450 -759 -1493 C ATOM 3838 CD1 PHE C 536 -3.476 40.635 -24.897 1.00 72.13 C ANISOU 3838 CD1 PHE C 536 7107 9833 10466 -891 -460 -1743 C ATOM 3839 CD2 PHE C 536 -4.358 38.487 -25.424 1.00 69.29 C ANISOU 3839 CD2 PHE C 536 6603 9810 9915 -477 -1180 -1448 C ATOM 3840 CE1 PHE C 536 -4.071 40.575 -23.656 1.00 72.45 C ANISOU 3840 CE1 PHE C 536 7095 10110 10321 -1346 -573 -1946 C ATOM 3841 CE2 PHE C 536 -4.957 38.422 -24.183 1.00 68.97 C ANISOU 3841 CE2 PHE C 536 6474 10027 9707 -899 -1324 -1639 C ATOM 3842 CZ PHE C 536 -4.813 39.467 -23.298 1.00 70.16 C ANISOU 3842 CZ PHE C 536 6670 10125 9862 -1334 -1019 -1888 C ATOM 3843 N GLU C 537 -2.337 40.560 -30.021 1.00 74.81 N ANISOU 3843 N GLU C 537 8034 9184 11204 895 51 -1034 N ATOM 3844 CA GLU C 537 -1.525 40.449 -31.223 1.00 78.69 C ANISOU 3844 CA GLU C 537 8692 9392 11814 1160 237 -873 C ATOM 3845 C GLU C 537 -0.979 41.815 -31.610 1.00 82.17 C ANISOU 3845 C GLU C 537 9316 9483 12421 1207 742 -954 C ATOM 3846 O GLU C 537 0.182 41.945 -31.998 1.00 82.94 O ANISOU 3846 O GLU C 537 9407 9401 12707 1150 954 -914 O ATOM 3847 CB GLU C 537 -2.372 39.892 -32.368 1.00 82.67 C ANISOU 3847 CB GLU C 537 9458 9858 12094 1547 121 -707 C ATOM 3848 CG GLU C 537 -1.593 39.129 -33.422 1.00 86.92 C ANISOU 3848 CG GLU C 537 10181 10179 12666 1695 196 -549 C ATOM 3849 CD GLU C 537 -1.605 37.635 -33.177 1.00 88.99 C ANISOU 3849 CD GLU C 537 10366 10622 12824 1583 -121 -470 C ATOM 3850 OE1 GLU C 537 -0.893 37.172 -32.259 1.00 91.17 O ANISOU 3850 OE1 GLU C 537 10322 11025 13293 1359 -231 -458 O ATOM 3851 OE2 GLU C 537 -2.329 36.922 -33.904 1.00 88.63 O ANISOU 3851 OE2 GLU C 537 10595 10603 12478 1688 -248 -394 O ATOM 3852 N MET C 538 -1.830 42.830 -31.489 1.00 85.21 N ANISOU 3852 N MET C 538 9867 9758 12751 1319 981 -1052 N ATOM 3853 CA MET C 538 -1.470 44.199 -31.839 1.00 88.04 C ANISOU 3853 CA MET C 538 10493 9716 13244 1387 1544 -1132 C ATOM 3854 C MET C 538 -0.423 44.763 -30.885 1.00 92.40 C ANISOU 3854 C MET C 538 10938 10255 13914 808 1768 -1369 C ATOM 3855 O MET C 538 0.555 45.373 -31.316 1.00 96.33 O ANISOU 3855 O MET C 538 11562 10497 14543 717 2116 -1401 O ATOM 3856 CB MET C 538 -2.712 45.092 -31.831 1.00 87.35 C ANISOU 3856 CB MET C 538 10590 9495 13104 1688 1805 -1119 C ATOM 3857 CG MET C 538 -2.485 46.484 -32.398 1.00 89.88 C ANISOU 3857 CG MET C 538 11281 9312 13557 1893 2454 -1126 C ATOM 3858 SD MET C 538 -3.932 47.546 -32.225 1.00140.60 S ANISOU 3858 SD MET C 538 17868 15542 20013 2307 2870 -1031 S ATOM 3859 CE MET C 538 -5.235 46.422 -32.714 1.00 97.32 C ANISOU 3859 CE MET C 538 12092 10561 14324 2712 2216 -675 C ATOM 3860 N CYS C 539 -0.636 44.555 -29.588 1.00 92.52 N ANISOU 3860 N CYS C 539 10732 10581 13843 352 1561 -1532 N ATOM 3861 CA CYS C 539 0.282 45.050 -28.566 1.00 94.70 C ANISOU 3861 CA CYS C 539 10899 10958 14125 -353 1708 -1744 C ATOM 3862 C CYS C 539 1.675 44.447 -28.710 1.00 95.24 C ANISOU 3862 C CYS C 539 10640 11224 14324 -586 1500 -1579 C ATOM 3863 O CYS C 539 2.676 45.121 -28.478 1.00 97.72 O ANISOU 3863 O CYS C 539 10926 11515 14689 -1039 1766 -1671 O ATOM 3864 CB CYS C 539 -0.264 44.760 -27.166 1.00 94.31 C ANISOU 3864 CB CYS C 539 10679 11263 13893 -839 1448 -1911 C ATOM 3865 SG CYS C 539 -1.737 45.702 -26.714 1.00 99.12 S ANISOU 3865 SG CYS C 539 11646 11606 14410 -707 1887 -2146 S ATOM 3866 N ALA C 540 1.732 43.177 -29.094 1.00 94.30 N ANISOU 3866 N ALA C 540 10275 11296 14260 -288 1071 -1315 N ATOM 3867 CA ALA C 540 3.005 42.486 -29.259 1.00 96.58 C ANISOU 3867 CA ALA C 540 10205 11746 14747 -389 926 -1070 C ATOM 3868 C ALA C 540 3.849 43.149 -30.342 1.00 99.99 C ANISOU 3868 C ALA C 540 10819 11801 15370 -195 1387 -1037 C ATOM 3869 O ALA C 540 5.054 43.335 -30.174 1.00103.86 O ANISOU 3869 O ALA C 540 11030 12413 16020 -539 1493 -959 O ATOM 3870 CB ALA C 540 2.776 41.018 -29.585 1.00 93.97 C ANISOU 3870 CB ALA C 540 9719 11540 14446 -20 533 -803 C ATOM 3871 N ASN C 541 3.203 43.511 -31.447 1.00 99.09 N ANISOU 3871 N ASN C 541 11156 11272 15222 325 1649 -1065 N ATOM 3872 CA ASN C 541 3.887 44.145 -32.569 1.00100.60 C ANISOU 3872 CA ASN C 541 11611 11056 15556 540 2107 -1039 C ATOM 3873 C ASN C 541 4.494 45.488 -32.186 1.00103.56 C ANISOU 3873 C ASN C 541 12100 11293 15954 94 2555 -1269 C ATOM 3874 O ASN C 541 5.543 45.878 -32.701 1.00107.21 O ANISOU 3874 O ASN C 541 12565 11597 16574 -7 2870 -1245 O ATOM 3875 CB ASN C 541 2.927 44.328 -33.745 1.00 99.01 C ANISOU 3875 CB ASN C 541 11894 10495 15232 1126 2253 -988 C ATOM 3876 CG ASN C 541 2.235 43.038 -34.136 1.00 97.38 C ANISOU 3876 CG ASN C 541 11659 10443 14898 1444 1836 -801 C ATOM 3877 OD1 ASN C 541 2.701 41.944 -33.813 1.00 96.12 O ANISOU 3877 OD1 ASN C 541 11189 10511 14822 1339 1557 -681 O ATOM 3878 ND2 ASN C 541 1.114 43.159 -34.838 1.00 96.97 N ANISOU 3878 ND2 ASN C 541 11935 10280 14631 1813 1811 -739 N ATOM 3879 N LEU C 542 3.826 46.189 -31.277 1.00101.66 N ANISOU 3879 N LEU C 542 11990 11094 15543 -210 2638 -1508 N ATOM 3880 CA LEU C 542 4.278 47.499 -30.830 1.00102.75 C ANISOU 3880 CA LEU C 542 12365 11046 15630 -724 3150 -1784 C ATOM 3881 C LEU C 542 5.456 47.369 -29.871 1.00102.62 C ANISOU 3881 C LEU C 542 11891 11495 15604 -1533 2983 -1809 C ATOM 3882 O LEU C 542 6.473 48.048 -30.026 1.00104.64 O ANISOU 3882 O LEU C 542 12170 11682 15908 -1917 3328 -1877 O ATOM 3883 CB LEU C 542 3.132 48.248 -30.149 1.00103.79 C ANISOU 3883 CB LEU C 542 12840 11011 15585 -790 3390 -2027 C ATOM 3884 CG LEU C 542 2.894 49.697 -30.576 1.00107.67 C ANISOU 3884 CG LEU C 542 13944 10890 16074 -674 4163 -2211 C ATOM 3885 CD1 LEU C 542 1.792 50.322 -29.738 1.00109.23 C ANISOU 3885 CD1 LEU C 542 14420 10932 16149 -754 4454 -2417 C ATOM 3886 CD2 LEU C 542 4.171 50.513 -30.480 1.00111.96 C ANISOU 3886 CD2 LEU C 542 14610 11319 16610 -1311 4597 -2404 C ATOM 3887 N ILE C 543 5.310 46.492 -28.882 1.00100.38 N ANISOU 3887 N ILE C 543 11178 11728 15235 -1821 2439 -1719 N ATOM 3888 CA ILE C 543 6.340 46.291 -27.867 1.00102.69 C ANISOU 3888 CA ILE C 543 10959 12589 15470 -2627 2173 -1646 C ATOM 3889 C ILE C 543 7.615 45.710 -28.474 1.00104.40 C ANISOU 3889 C ILE C 543 10688 12996 15984 -2520 2061 -1278 C ATOM 3890 O ILE C 543 8.721 46.031 -28.039 1.00107.90 O ANISOU 3890 O ILE C 543 10782 13788 16428 -3172 2091 -1209 O ATOM 3891 CB ILE C 543 5.837 45.385 -26.725 1.00100.38 C ANISOU 3891 CB ILE C 543 10321 12803 15015 -2889 1581 -1561 C ATOM 3892 CG1 ILE C 543 4.559 45.960 -26.116 1.00 99.01 C ANISOU 3892 CG1 ILE C 543 10619 12421 14578 -2988 1761 -1929 C ATOM 3893 CG2 ILE C 543 6.898 45.238 -25.649 1.00104.72 C ANISOU 3893 CG2 ILE C 543 10325 14011 15453 -3787 1271 -1415 C ATOM 3894 CD1 ILE C 543 3.963 45.105 -25.025 1.00 97.30 C ANISOU 3894 CD1 ILE C 543 10139 12654 14178 -3243 1223 -1890 C ATOM 3895 N LYS C 544 7.449 44.864 -29.488 1.00102.23 N ANISOU 3895 N LYS C 544 10400 12496 15947 -1731 1972 -1033 N ATOM 3896 CA LYS C 544 8.579 44.277 -30.200 1.00104.31 C ANISOU 3896 CA LYS C 544 10276 12807 16550 -1502 2001 -681 C ATOM 3897 C LYS C 544 9.557 45.357 -30.648 1.00110.14 C ANISOU 3897 C LYS C 544 11109 13374 17365 -1818 2514 -797 C ATOM 3898 O LYS C 544 10.770 45.191 -30.541 1.00115.23 O ANISOU 3898 O LYS C 544 11207 14361 18212 -2125 2495 -534 O ATOM 3899 CB LYS C 544 8.093 43.474 -31.409 1.00100.40 C ANISOU 3899 CB LYS C 544 10043 11895 16211 -646 2043 -534 C ATOM 3900 CG LYS C 544 9.207 42.823 -32.215 1.00102.66 C ANISOU 3900 CG LYS C 544 10020 12112 16875 -353 2202 -186 C ATOM 3901 CD LYS C 544 8.647 41.986 -33.356 1.00100.56 C ANISOU 3901 CD LYS C 544 10133 11408 16665 372 2283 -92 C ATOM 3902 CE LYS C 544 9.753 41.281 -34.126 1.00102.62 C ANISOU 3902 CE LYS C 544 10140 11526 17326 663 2552 246 C ATOM 3903 NZ LYS C 544 9.210 40.351 -35.158 1.00100.45 N ANISOU 3903 NZ LYS C 544 10303 10823 17040 1249 2662 318 N ATOM 3904 N ILE C 545 9.019 46.470 -31.135 1.00111.13 N ANISOU 3904 N ILE C 545 11909 12983 17333 -1743 2992 -1156 N ATOM 3905 CA ILE C 545 9.844 47.599 -31.543 1.00116.67 C ANISOU 3905 CA ILE C 545 12830 13448 18049 -2083 3548 -1329 C ATOM 3906 C ILE C 545 10.356 48.373 -30.335 1.00122.44 C ANISOU 3906 C ILE C 545 13409 14586 18527 -3117 3592 -1533 C ATOM 3907 O ILE C 545 11.550 48.651 -30.221 1.00127.27 O ANISOU 3907 O ILE C 545 13659 15502 19196 -3674 3698 -1443 O ATOM 3908 CB ILE C 545 9.063 48.566 -32.447 1.00115.64 C ANISOU 3908 CB ILE C 545 13527 12588 17823 -1645 4093 -1603 C ATOM 3909 CG1 ILE C 545 8.577 47.844 -33.703 1.00112.10 C ANISOU 3909 CG1 ILE C 545 13270 11792 17530 -747 4038 -1389 C ATOM 3910 CG2 ILE C 545 9.926 49.765 -32.815 1.00119.23 C ANISOU 3910 CG2 ILE C 545 14275 12762 18265 -2050 4718 -1806 C ATOM 3911 CD1 ILE C 545 7.883 48.749 -34.683 1.00112.31 C ANISOU 3911 CD1 ILE C 545 14038 11176 17460 -298 4518 -1535 C ATOM 3912 N LEU C 546 9.442 48.716 -29.433 1.00122.90 N ANISOU 3912 N LEU C 546 13752 14665 18280 -3422 3534 -1803 N ATOM 3913 CA LEU C 546 9.770 49.540 -28.275 1.00129.15 C ANISOU 3913 CA LEU C 546 14593 15753 18726 -4497 3672 -2082 C ATOM 3914 C LEU C 546 10.752 48.863 -27.322 1.00133.66 C ANISOU 3914 C LEU C 546 14322 17215 19249 -5240 3100 -1769 C ATOM 3915 O LEU C 546 11.771 49.449 -26.955 1.00138.97 O ANISOU 3915 O LEU C 546 14792 18233 19775 -6099 3242 -1797 O ATOM 3916 CB LEU C 546 8.496 49.938 -27.530 1.00128.42 C ANISOU 3916 CB LEU C 546 15011 15437 18344 -4595 3780 -2422 C ATOM 3917 CG LEU C 546 7.478 50.722 -28.359 1.00126.97 C ANISOU 3917 CG LEU C 546 15610 14422 18211 -3887 4382 -2652 C ATOM 3918 CD1 LEU C 546 6.260 51.072 -27.522 1.00127.09 C ANISOU 3918 CD1 LEU C 546 16022 14266 18000 -3990 4527 -2928 C ATOM 3919 CD2 LEU C 546 8.112 51.975 -28.943 1.00131.59 C ANISOU 3919 CD2 LEU C 546 16700 14526 18773 -4133 5140 -2880 C ATOM 3920 N ALA C 547 10.440 47.634 -26.919 1.00132.81 N ANISOU 3920 N ALA C 547 13717 17503 19241 -4935 2456 -1436 N ATOM 3921 CA ALA C 547 11.314 46.885 -26.022 1.00138.77 C ANISOU 3921 CA ALA C 547 13615 19127 19984 -5527 1865 -1013 C ATOM 3922 C ALA C 547 12.663 46.617 -26.681 1.00144.31 C ANISOU 3922 C ALA C 547 13696 20076 21060 -5430 1890 -576 C ATOM 3923 O ALA C 547 12.735 46.292 -27.867 1.00141.47 O ANISOU 3923 O ALA C 547 13419 19251 21083 -4567 2124 -448 O ATOM 3924 CB ALA C 547 10.656 45.581 -25.593 1.00135.28 C ANISOU 3924 CB ALA C 547 12843 18937 19619 -5076 1246 -716 C ATOM 3925 N GLN C 548 13.730 46.763 -25.904 1.00153.25 N ANISOU 3925 N GLN C 548 14199 21970 22059 -6363 1665 -332 N ATOM 3926 CA GLN C 548 15.082 46.627 -26.428 1.00160.03 C ANISOU 3926 CA GLN C 548 14377 23156 23270 -6387 1728 112 C ATOM 3927 C GLN C 548 15.866 45.580 -25.644 1.00164.94 C ANISOU 3927 C GLN C 548 14165 24457 24048 -6308 1022 799 C ATOM 3928 O GLN C 548 15.283 44.756 -24.937 1.00163.04 O ANISOU 3928 O GLN C 548 13858 24377 23714 -6094 535 934 O ATOM 3929 CB GLN C 548 15.799 47.978 -26.376 1.00166.56 C ANISOU 3929 CB GLN C 548 15585 23918 23783 -7102 2128 -184 C ATOM 3930 CG GLN C 548 15.011 49.112 -27.017 1.00164.57 C ANISOU 3930 CG GLN C 548 16336 22838 23354 -7145 2922 -924 C ATOM 3931 CD GLN C 548 15.451 50.481 -26.536 1.00171.29 C ANISOU 3931 CD GLN C 548 17780 23645 23657 -7919 3203 -1271 C ATOM 3932 OE1 GLN C 548 14.644 51.406 -26.439 1.00170.38 O ANISOU 3932 OE1 GLN C 548 18566 22966 23203 -8082 3685 -1843 O ATOM 3933 NE2 GLN C 548 16.737 50.617 -26.232 1.00178.42 N ANISOU 3933 NE2 GLN C 548 18179 25120 24491 -8371 2957 -925 N TER 3934 GLN C 548 END If you find results from this site helpful for your 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