HEADER HORMONE RECEPTOR 13-DEC-19 6TPK
TITLE CRYSTAL STRUCTURE OF THE HUMAN OXYTOCIN RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXYTOCIN RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OT-R;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: OXTR;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS EUKARYOTIC, PROTEIN, HORMONE RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.WALTENSPUEHL,J.SCHOEPPE,J.EHRENMANN,L.KUMMER,A.PLUECKTHUN
REVDAT 3 02-SEP-20 6TPK 1 JRNL
REVDAT 2 19-AUG-20 6TPK 1 TITLE
REVDAT 1 05-AUG-20 6TPK 0
JRNL AUTH Y.WALTENSPUHL,J.SCHOPPE,J.EHRENMANN,L.KUMMER,A.PLUCKTHUN
JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN OXYTOCIN RECEPTOR.
JRNL REF SCI ADV V. 6 B5419 2020
JRNL REFN ESSN 2375-2548
JRNL PMID 32832646
JRNL DOI 10.1126/SCIADV.ABB5419
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 14602
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.252
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.330
REMARK 3 FREE R VALUE TEST SET COUNT : 632
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 29.8400 - 5.4633 1.00 2923 119 0.2333 0.2506
REMARK 3 2 5.4633 - 4.3407 1.00 2805 134 0.2205 0.2169
REMARK 3 3 4.3407 - 3.7932 1.00 2774 137 0.2457 0.2546
REMARK 3 4 3.7932 - 3.4470 1.00 2705 132 0.3035 0.3396
REMARK 3 5 3.4470 - 3.2002 0.99 2763 110 0.3560 0.3879
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.470
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 100.8
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 : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3397 -4.7867 95.9716
REMARK 3 T TENSOR
REMARK 3 T11: 0.8463 T22: 0.7631
REMARK 3 T33: 0.6253 T12: -0.0644
REMARK 3 T13: -0.1016 T23: -0.0439
REMARK 3 L TENSOR
REMARK 3 L11: 1.4834 L22: 1.3284
REMARK 3 L33: 4.2439 L12: -0.4247
REMARK 3 L13: -1.7558 L23: 1.1086
REMARK 3 S TENSOR
REMARK 3 S11: 0.1516 S12: -0.4108 S13: 0.1207
REMARK 3 S21: 0.5507 S22: -0.1271 S23: -0.2768
REMARK 3 S31: -0.2222 S32: -0.1177 S33: 0.0003
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 6TPK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-DEC-19.
REMARK 100 THE DEPOSITION ID IS D_1292105269.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-19
REMARK 200 TEMPERATURE (KELVIN) : 104.15
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14739
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 47.590
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 32.10
REMARK 200 R MERGE (I) : 0.48900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 32.90
REMARK 200 R MERGE FOR SHELL (I) : 5.35900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PROTEIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ADA, PEG400, NAH2PO4, TCEP, LIPIDIC
REMARK 280 CUBIC PHASE, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 141.74300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 141.74300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 38.49350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.42900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 38.49350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.42900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 141.74300
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 38.49350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 39.42900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 141.74300
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 38.49350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 39.42900
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 THR A 66
REMARK 465 THR A 67
REMARK 465 ARG A 68
REMARK 465 GLN A 69
REMARK 465 LYS A 70
REMARK 465 LEU A 231
REMARK 465 ARG A 232
REMARK 465 LEU A 233
REMARK 465 LYS A 234
REMARK 465 THR A 235
REMARK 465 ALA A 236
REMARK 465 ALA A 237
REMARK 465 ALA A 238
REMARK 465 ALA A 239
REMARK 465 ALA A 240
REMARK 465 ALA A 241
REMARK 465 GLU A 242
REMARK 465 ALA A 243
REMARK 465 PRO A 244
REMARK 465 GLU A 245
REMARK 465 GLY A 246
REMARK 465 ALA A 247
REMARK 465 ALA A 248
REMARK 465 ALA A 249
REMARK 465 GLY A 250
REMARK 465 ASP A 251
REMARK 465 GLY A 252
REMARK 465 GLY A 253
REMARK 465 ARG A 254
REMARK 465 VAL A 255
REMARK 465 ALA A 256
REMARK 465 LEU A 257
REMARK 465 ALA A 258
REMARK 465 ARG A 259
REMARK 465 VAL A 260
REMARK 465 SER A 261
REMARK 465 SER A 262
REMARK 465 VAL A 263
REMARK 465 LYS A 264
REMARK 465 CYS A 346
REMARK 465 CYS A 347
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 ARG A 178 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 337 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS A 338 CG ND1 CD2 CE1 NE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 N ILE A 266 C SER A 536 1.32
REMARK 500 C LEU A 265 N GLY A 339 1.34
REMARK 500 N ILE A 266 CA SER A 536 1.64
REMARK 500 N ILE A 266 O SER A 536 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 72 -5.16 84.05
REMARK 500 ALA A 181 71.13 -155.14
REMARK 500 TYR A 209 -66.09 -131.70
REMARK 500 LYS A 306 52.87 38.57
REMARK 500 ALA A 310 -62.07 -104.93
REMARK 500 ASP A 341 70.36 57.26
REMARK 500 GLN A 385 -82.86 -125.64
REMARK 500 PRO A 458 34.30 -84.23
REMARK 500 LEU A 521 -5.60 77.16
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 NU2 A 1501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1503
DBREF 6TPK A 35 356 UNP P30559 OXYR_HUMAN 35 356
SEQADV 6TPK HIS A 65 UNP P30559 ARG 65 CONFLICT
SEQADV 6TPK LEU A 120 UNP P30559 VAL 120 CONFLICT
SEQADV 6TPK ALA A 153 UNP P30559 ASP 153 CONFLICT
SEQADV 6TPK VAL A 167 UNP P30559 ALA 167 CONFLICT
SEQADV 6TPK ARG A 193 UNP P30559 GLN 193 CONFLICT
SEQADV 6TPK THR A 218 UNP P30559 ALA 218 CONFLICT
SEQADV 6TPK ALA A 224 UNP P30559 SER 224 CONFLICT
SEQADV 6TPK CYS A 322 UNP P30559 SER 322 CONFLICT
SEQADV 6TPK LYS A 325 UNP P30559 ASN 325 CONFLICT
SEQADV 6TPK MET A 333 UNP P30559 THR 333 CONFLICT
SEQADV 6TPK GLY A 339 UNP P30559 GLU 339 CONFLICT
SEQADV 6TPK ILE A 340 UNP P30559 LEU 340 CONFLICT
SEQADV 6TPK ASP A 341 UNP P30559 VAL 341 CONFLICT
SEQADV 6TPK YCM A 342 UNP P30559 GLN 342 CONFLICT
SEQADV 6TPK SER A 343 UNP P30559 ARG 343 CONFLICT
SEQADV 6TPK TRP A 345 UNP P30559 LEU 345 CONFLICT
SEQADV 6TPK ASN A 348 UNP P30559 SER 348 CONFLICT
SEQADV 6TPK GLU A 349 UNP P30559 ALA 349 CONFLICT
SEQADV 6TPK THR A 353 UNP P30559 LYS 353 CONFLICT
SEQADV 6TPK SER A 355 UNP P30559 ARG 355 CONFLICT
SEQADV 6TPK ASP A 357 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 358 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ARG A 359 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 360 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 361 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 362 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 363 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 364 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 365 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 366 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PHE A 367 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 368 UNP P30559 EXPRESSION TAG
SEQADV 6TPK MET A 369 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ASP A 370 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 371 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 372 UNP P30559 EXPRESSION TAG
SEQADV 6TPK VAL A 373 UNP P30559 EXPRESSION TAG
SEQADV 6TPK THR A 374 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PHE A 375 UNP P30559 EXPRESSION TAG
SEQADV 6TPK MET A 376 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PHE A 377 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 378 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 379 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ARG A 380 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PHE A 381 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ASP A 382 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ARG A 383 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 384 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLN A 385 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 386 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 387 UNP P30559 EXPRESSION TAG
SEQADV 6TPK VAL A 388 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ASP A 389 UNP P30559 EXPRESSION TAG
SEQADV 6TPK VAL A 390 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 391 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 392 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 393 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ALA A 394 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 395 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 396 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 397 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 398 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 399 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 400 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 401 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 402 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 403 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PHE A 404 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLN A 405 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 406 UNP P30559 EXPRESSION TAG
SEQADV 6TPK MET A 407 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ARG A 408 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PHE A 409 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 410 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 411 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 412 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 413 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 414 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 415 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ASP A 416 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PRO A 417 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 418 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 419 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 420 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 421 UNP P30559 EXPRESSION TAG
SEQADV 6TPK TRP A 422 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ALA A 423 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ARG A 424 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 425 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 426 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 427 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 428 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 429 UNP P30559 EXPRESSION TAG
SEQADV 6TPK HIS A 430 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 431 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ASN A 432 UNP P30559 EXPRESSION TAG
SEQADV 6TPK VAL A 433 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 434 UNP P30559 EXPRESSION TAG
SEQADV 6TPK VAL A 435 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 436 UNP P30559 EXPRESSION TAG
SEQADV 6TPK THR A 437 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 438 UNP P30559 EXPRESSION TAG
SEQADV 6TPK MET A 439 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 440 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 441 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ARG A 442 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 443 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PHE A 444 UNP P30559 EXPRESSION TAG
SEQADV 6TPK VAL A 445 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ARG A 446 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 447 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 448 UNP P30559 EXPRESSION TAG
SEQADV 6TPK TYR A 449 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 450 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 451 UNP P30559 EXPRESSION TAG
SEQADV 6TPK VAL A 452 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ASP A 453 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PHE A 454 UNP P30559 EXPRESSION TAG
SEQADV 6TPK VAL A 455 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 456 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 457 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PRO A 458 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 459 UNP P30559 EXPRESSION TAG
SEQADV 6TPK TYR A 460 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PHE A 461 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 462 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PRO A 463 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PHE A 464 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 465 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 466 UNP P30559 EXPRESSION TAG
SEQADV 6TPK VAL A 467 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ALA A 468 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 469 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 470 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ALA A 471 UNP P30559 EXPRESSION TAG
SEQADV 6TPK MET A 472 UNP P30559 EXPRESSION TAG
SEQADV 6TPK CYS A 473 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 474 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 475 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ALA A 476 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 477 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PRO A 478 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 479 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ALA A 480 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 481 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ALA A 482 UNP P30559 EXPRESSION TAG
SEQADV 6TPK VAL A 483 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 484 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 485 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 486 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ARG A 487 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ASP A 488 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 489 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 490 UNP P30559 EXPRESSION TAG
SEQADV 6TPK THR A 491 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ASN A 492 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 493 UNP P30559 EXPRESSION TAG
SEQADV 6TPK THR A 494 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 495 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 496 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 497 UNP P30559 EXPRESSION TAG
SEQADV 6TPK VAL A 498 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 499 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ALA A 500 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 501 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ASP A 502 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PRO A 503 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLY A 504 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 505 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 506 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ALA A 507 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ASN A 508 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ALA A 509 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ILE A 510 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 511 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 512 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ALA A 513 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 514 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 515 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 516 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 517 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ARG A 518 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 519 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ASP A 520 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LEU A 521 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 522 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 523 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PHE A 524 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ARG A 525 UNP P30559 EXPRESSION TAG
SEQADV 6TPK GLU A 526 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ASN A 527 UNP P30559 EXPRESSION TAG
SEQADV 6TPK CYS A 528 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 529 UNP P30559 EXPRESSION TAG
SEQADV 6TPK LYS A 530 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ARG A 531 UNP P30559 EXPRESSION TAG
SEQADV 6TPK ALA A 532 UNP P30559 EXPRESSION TAG
SEQADV 6TPK MET A 533 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 534 UNP P30559 EXPRESSION TAG
SEQADV 6TPK PHE A 535 UNP P30559 EXPRESSION TAG
SEQADV 6TPK SER A 536 UNP P30559 EXPRESSION TAG
SEQRES 1 A 502 ASN GLU ALA LEU ALA ARG VAL GLU VAL ALA VAL LEU CYS
SEQRES 2 A 502 LEU ILE LEU LEU LEU ALA LEU SER GLY ASN ALA CYS VAL
SEQRES 3 A 502 LEU LEU ALA LEU HIS THR THR ARG GLN LYS HIS SER ARG
SEQRES 4 A 502 LEU PHE PHE PHE MET LYS HIS LEU SER ILE ALA ASP LEU
SEQRES 5 A 502 VAL VAL ALA VAL PHE GLN VAL LEU PRO GLN LEU LEU TRP
SEQRES 6 A 502 ASP ILE THR PHE ARG PHE TYR GLY PRO ASP LEU LEU CYS
SEQRES 7 A 502 ARG LEU VAL LYS TYR LEU GLN LEU VAL GLY MET PHE ALA
SEQRES 8 A 502 SER THR TYR LEU LEU LEU LEU MET SER LEU ASP ARG CYS
SEQRES 9 A 502 LEU ALA ILE CYS GLN PRO LEU ARG SER LEU ARG ARG ARG
SEQRES 10 A 502 THR ALA ARG LEU ALA VAL LEU ALA THR TRP LEU GLY CYS
SEQRES 11 A 502 LEU VAL VAL SER ALA PRO GLN VAL HIS ILE PHE SER LEU
SEQRES 12 A 502 ARG GLU VAL ALA ASP GLY VAL PHE ASP CYS TRP ALA VAL
SEQRES 13 A 502 PHE ILE ARG PRO TRP GLY PRO LYS ALA TYR ILE THR TRP
SEQRES 14 A 502 ILE THR LEU ALA VAL TYR ILE VAL PRO VAL ILE VAL LEU
SEQRES 15 A 502 ALA THR CYS TYR GLY LEU ILE ALA PHE LYS ILE TRP GLN
SEQRES 16 A 502 ASN LEU ARG LEU LYS THR ALA ALA ALA ALA ALA ALA GLU
SEQRES 17 A 502 ALA PRO GLU GLY ALA ALA ALA GLY ASP GLY GLY ARG VAL
SEQRES 18 A 502 ALA LEU ALA ARG VAL SER SER VAL LYS LEU ILE SER LYS
SEQRES 19 A 502 ALA LYS ILE ARG THR VAL LYS MET THR PHE ILE ILE VAL
SEQRES 20 A 502 LEU ALA PHE ILE VAL CYS TRP THR PRO PHE PHE PHE VAL
SEQRES 21 A 502 GLN MET TRP SER VAL TRP ASP ALA ASN ALA PRO LYS GLU
SEQRES 22 A 502 ALA SER ALA PHE ILE ILE VAL MET LEU LEU ALA SER LEU
SEQRES 23 A 502 ASN CYS CYS CYS LYS PRO TRP ILE TYR MET LEU PHE MET
SEQRES 24 A 502 GLY HIS LEU PHE HIS GLY ILE ASP YCM SER PHE TRP CYS
SEQRES 25 A 502 CYS ASN GLU SER TYR LEU THR GLY SER ARG ASP GLU ARG
SEQRES 26 A 502 LYS LYS SER LEU LEU SER LYS PHE GLY MET ASP GLU GLY
SEQRES 27 A 502 VAL THR PHE MET PHE ILE GLY ARG PHE ASP ARG GLY GLN
SEQRES 28 A 502 LYS GLY VAL ASP VAL LEU LEU LYS ALA ILE GLU ILE LEU
SEQRES 29 A 502 SER SER LYS LYS GLU PHE GLN GLU MET ARG PHE ILE ILE
SEQRES 30 A 502 ILE GLY LYS GLY ASP PRO GLU LEU GLU GLY TRP ALA ARG
SEQRES 31 A 502 SER LEU GLU GLU LYS HIS GLY ASN VAL LYS VAL ILE THR
SEQRES 32 A 502 GLU MET LEU SER ARG GLU PHE VAL ARG GLU LEU TYR GLY
SEQRES 33 A 502 SER VAL ASP PHE VAL ILE ILE PRO SER TYR PHE GLU PRO
SEQRES 34 A 502 PHE GLY LEU VAL ALA LEU GLU ALA MET CYS LEU GLY ALA
SEQRES 35 A 502 ILE PRO ILE ALA SER ALA VAL GLY GLY LEU ARG ASP ILE
SEQRES 36 A 502 ILE THR ASN GLU THR GLY ILE LEU VAL LYS ALA GLY ASP
SEQRES 37 A 502 PRO GLY GLU LEU ALA ASN ALA ILE LEU LYS ALA LEU GLU
SEQRES 38 A 502 LEU SER ARG SER ASP LEU SER LYS PHE ARG GLU ASN CYS
SEQRES 39 A 502 LYS LYS ARG ALA MET SER PHE SER
HET YCM A 342 10
HET NU2 A1501 36
HET CLR A1502 28
HET PEG A1503 7
HETNAM YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE
HETNAM NU2 (3~{R},6~{R})-6-[(2~{S})-BUTAN-2-YL]-3-(2,3-DIHYDRO-
HETNAM 2 NU2 1~{H}-INDEN-2-YL)-1-[(1~{R})-1-(2-METHYL-1,3-OXAZOL-4-
HETNAM 3 NU2 YL)-2-MORPHOLIN-4-YL-2-OXIDANYLIDENE-ETHYL]PIPERAZINE-
HETNAM 4 NU2 2,5-DIONE
HETNAM CLR CHOLESTEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN YCM CYSTEINE-S-ACETAMIDE
FORMUL 1 YCM C5 H10 N2 O3 S
FORMUL 2 NU2 C27 H34 N4 O5
FORMUL 3 CLR C27 H46 O
FORMUL 4 PEG C4 H10 O3
HELIX 1 AA1 ASN A 35 LEU A 64 1 30
HELIX 2 AA2 ARG A 73 THR A 102 1 30
HELIX 3 AA3 PRO A 108 GLN A 143 1 36
HELIX 4 AA4 ARG A 149 ILE A 174 1 26
HELIX 5 AA5 TRP A 195 TYR A 209 1 15
HELIX 6 AA6 TYR A 209 GLN A 229 1 21
HELIX 7 AA7 SER A 267 VAL A 299 1 33
HELIX 8 AA8 LYS A 306 MET A 333 1 28
HELIX 9 AA9 GLY A 334 PHE A 337 5 4
HELIX 10 AB1 ASN A 348 LEU A 352 5 5
HELIX 11 AB2 SER A 355 PHE A 367 1 13
HELIX 12 AB3 GLY A 387 SER A 400 1 14
HELIX 13 AB4 GLU A 403 GLN A 405 5 3
HELIX 14 AB5 ASP A 416 HIS A 430 1 15
HELIX 15 AB6 SER A 441 VAL A 452 1 12
HELIX 16 AB7 GLY A 465 LEU A 474 1 10
HELIX 17 AB8 GLY A 484 ILE A 490 1 7
HELIX 18 AB9 ASP A 502 SER A 517 1 16
HELIX 19 AC1 LEU A 521 PHE A 535 1 15
SHEET 1 AA1 2 PHE A 175 GLU A 179 0
SHEET 2 AA1 2 PHE A 185 ALA A 189 -1 O TRP A 188 N SER A 176
SHEET 1 AA2 6 VAL A 433 ILE A 436 0
SHEET 2 AA2 6 MET A 407 ILE A 412 1 N ILE A 411 O LYS A 434
SHEET 3 AA2 6 VAL A 373 ILE A 378 1 N VAL A 373 O ARG A 408
SHEET 4 AA2 6 PHE A 454 ILE A 457 1 O PHE A 454 N MET A 376
SHEET 5 AA2 6 ILE A 477 SER A 481 1 O ILE A 479 N VAL A 455
SHEET 6 AA2 6 ILE A 496 VAL A 498 1 O ILE A 496 N ALA A 480
SSBOND 1 CYS A 112 CYS A 187 1555 1555 1.86
LINK C ASP A 341 N YCM A 342 1555 1555 1.32
LINK C YCM A 342 N SER A 343 1555 1555 1.33
SITE 1 AC1 10 GLN A 92 LYS A 116 GLN A 119 MET A 123
SITE 2 AC1 10 GLN A 171 ILE A 201 TRP A 288 PHE A 291
SITE 3 AC1 10 GLN A 295 ALA A 318
SITE 1 AC2 4 PHE A 191 ILE A 192 TYR A 200 TRP A 203
SITE 1 AC3 5 GLU A 349 GLY A 354 ARG A 359 ARG A 383
SITE 2 AC3 5 LYS A 393
CRYST1 76.987 78.858 283.486 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012989 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012681 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003528 0.00000
ATOM 1 N ASN A 35 6.044 17.303 137.190 1.00184.64 N
ANISOU 1 N ASN A 35 28947 26072 15134 -4418 -1204 -6553 N
ATOM 2 CA ASN A 35 5.813 16.732 135.869 1.00182.68 C
ANISOU 2 CA ASN A 35 28638 25653 15118 -4296 -1175 -6322 C
ATOM 3 C ASN A 35 4.587 17.350 135.208 1.00183.96 C
ANISOU 3 C ASN A 35 29083 25357 15454 -4220 -792 -6256 C
ATOM 4 O ASN A 35 4.057 16.806 134.239 1.00178.40 O
ANISOU 4 O ASN A 35 28383 24505 14895 -4056 -738 -6028 O
ATOM 5 CB ASN A 35 5.645 15.215 135.958 1.00181.11 C
ANISOU 5 CB ASN A 35 28316 25729 14767 -4021 -1443 -6007 C
ATOM 6 CG ASN A 35 6.710 14.466 135.185 1.00181.86 C
ANISOU 6 CG ASN A 35 28105 26024 14969 -4025 -1712 -5923 C
ATOM 7 OD1 ASN A 35 7.365 15.025 134.304 1.00181.30 O
ANISOU 7 OD1 ASN A 35 27924 25819 15144 -4212 -1652 -6054 O
ATOM 8 ND2 ASN A 35 6.890 13.192 135.511 1.00181.74 N
ANISOU 8 ND2 ASN A 35 27963 26324 14767 -3809 -1996 -5697 N
ATOM 9 N GLU A 36 4.135 18.487 135.743 1.00191.11 N
ANISOU 9 N GLU A 36 30229 26049 16336 -4324 -525 -6455 N
ATOM 10 CA GLU A 36 3.007 19.184 135.134 1.00191.77 C
ANISOU 10 CA GLU A 36 30592 25695 16576 -4223 -148 -6408 C
ATOM 11 C GLU A 36 3.334 19.627 133.717 1.00194.70 C
ANISOU 11 C GLU A 36 30952 25764 17261 -4301 4 -6415 C
ATOM 12 O GLU A 36 2.447 19.667 132.856 1.00193.76 O
ANISOU 12 O GLU A 36 30979 25358 17285 -4113 218 -6255 O
ATOM 13 CB GLU A 36 2.608 20.388 135.993 1.00189.79 C
ANISOU 13 CB GLU A 36 30600 25274 16239 -4331 108 -6640 C
ATOM 14 CG GLU A 36 1.401 21.181 135.487 1.00183.80 C
ANISOU 14 CG GLU A 36 30151 24074 15610 -4183 512 -6596 C
ATOM 15 CD GLU A 36 1.753 22.186 134.399 1.00182.13 C
ANISOU 15 CD GLU A 36 30045 23478 15680 -4318 766 -6708 C
ATOM 16 OE1 GLU A 36 1.066 22.199 133.355 1.00178.08 O
ANISOU 16 OE1 GLU A 36 29635 22689 15339 -4119 954 -6542 O
ATOM 17 OE2 GLU A 36 2.723 22.953 134.583 1.00184.75 O
ANISOU 17 OE2 GLU A 36 30354 23788 16053 -4619 786 -6961 O
ATOM 18 N ALA A 37 4.600 19.960 133.453 1.00198.07 N
ANISOU 18 N ALA A 37 31202 26263 17792 -4566 -99 -6598 N
ATOM 19 CA ALA A 37 4.991 20.308 132.095 1.00197.26 C
ANISOU 19 CA ALA A 37 31075 25890 17986 -4647 35 -6596 C
ATOM 20 C ALA A 37 4.853 19.118 131.157 1.00196.90 C
ANISOU 20 C ALA A 37 30861 25925 18028 -4438 -137 -6307 C
ATOM 21 O ALA A 37 4.515 19.291 129.982 1.00199.73 O
ANISOU 21 O ALA A 37 31306 25976 18605 -4359 50 -6207 O
ATOM 22 CB ALA A 37 6.425 20.841 132.078 1.00200.64 C
ANISOU 22 CB ALA A 37 31313 26427 18494 -4994 -48 -6859 C
ATOM 23 N LEU A 38 5.079 17.901 131.660 1.00190.05 N
ANISOU 23 N LEU A 38 29773 25457 16982 -4330 -480 -6160 N
ATOM 24 CA LEU A 38 4.904 16.721 130.820 1.00179.15 C
ANISOU 24 CA LEU A 38 28250 24150 15667 -4130 -635 -5872 C
ATOM 25 C LEU A 38 3.436 16.517 130.464 1.00169.98 C
ANISOU 25 C LEU A 38 27316 22751 14517 -3862 -416 -5655 C
ATOM 26 O LEU A 38 3.101 16.236 129.306 1.00169.55 O
ANISOU 26 O LEU A 38 27264 22513 14642 -3746 -335 -5496 O
ATOM 27 CB LEU A 38 5.468 15.487 131.528 1.00176.15 C
ANISOU 27 CB LEU A 38 27620 24239 15068 -4054 -1029 -5755 C
ATOM 28 CG LEU A 38 5.654 14.200 130.716 1.00168.42 C
ANISOU 28 CG LEU A 38 26441 23401 14149 -3894 -1248 -5479 C
ATOM 29 CD1 LEU A 38 6.866 13.431 131.217 1.00170.74 C
ANISOU 29 CD1 LEU A 38 26432 24138 14304 -3924 -1631 -5489 C
ATOM 30 CD2 LEU A 38 4.413 13.326 130.789 1.00161.30 C
ANISOU 30 CD2 LEU A 38 25679 22471 13138 -3617 -1204 -5189 C
ATOM 31 N ALA A 39 2.542 16.676 131.443 1.00163.70 N
ANISOU 31 N ALA A 39 26704 21967 13530 -3757 -311 -5656 N
ATOM 32 CA ALA A 39 1.119 16.565 131.153 1.00158.64 C
ANISOU 32 CA ALA A 39 26257 21122 12895 -3501 -81 -5475 C
ATOM 33 C ALA A 39 0.656 17.672 130.217 1.00165.81 C
ANISOU 33 C ALA A 39 27375 21597 14028 -3477 274 -5550 C
ATOM 34 O ALA A 39 -0.209 17.442 129.363 1.00166.82 O
ANISOU 34 O ALA A 39 27574 21555 14256 -3254 421 -5373 O
ATOM 35 CB ALA A 39 0.314 16.592 132.453 1.00155.09 C
ANISOU 35 CB ALA A 39 25949 20784 12194 -3411 -28 -5488 C
ATOM 36 N ARG A 40 1.235 18.868 130.342 1.00170.90 N
ANISOU 36 N ARG A 40 28124 22060 14749 -3694 422 -5808 N
ATOM 37 CA ARG A 40 0.853 19.962 129.456 1.00173.47 C
ANISOU 37 CA ARG A 40 28685 21945 15282 -3655 781 -5867 C
ATOM 38 C ARG A 40 1.340 19.714 128.035 1.00173.23 C
ANISOU 38 C ARG A 40 28545 21782 15491 -3655 764 -5772 C
ATOM 39 O ARG A 40 0.627 20.007 127.069 1.00174.66 O
ANISOU 39 O ARG A 40 28884 21665 15815 -3450 1004 -5663 O
ATOM 40 CB ARG A 40 1.395 21.287 129.994 1.00176.56 C
ANISOU 40 CB ARG A 40 29232 22167 15687 -3912 959 -6162 C
ATOM 41 CG ARG A 40 0.551 22.500 129.626 1.00174.80 C
ANISOU 41 CG ARG A 40 29361 21491 15564 -3784 1389 -6205 C
ATOM 42 CD ARG A 40 0.937 23.719 130.457 1.00174.84 C
ANISOU 42 CD ARG A 40 29546 21367 15519 -4033 1562 -6486 C
ATOM 43 NE ARG A 40 0.078 24.870 130.182 1.00174.54 N
ANISOU 43 NE ARG A 40 29869 20893 15555 -3875 1982 -6506 N
ATOM 44 CZ ARG A 40 0.152 26.032 130.825 1.00177.94 C
ANISOU 44 CZ ARG A 40 30533 21130 15947 -4034 2212 -6720 C
ATOM 45 NH1 ARG A 40 1.047 26.203 131.788 1.00181.97 N
ANISOU 45 NH1 ARG A 40 30938 21859 16342 -4371 2061 -6950 N
ATOM 46 NH2 ARG A 40 -0.671 27.024 130.507 1.00177.09 N
ANISOU 46 NH2 ARG A 40 30761 20620 15906 -3841 2595 -6701 N
ATOM 47 N VAL A 41 2.544 19.162 127.885 1.00173.47 N
ANISOU 47 N VAL A 41 28299 22047 15564 -3860 479 -5808 N
ATOM 48 CA VAL A 41 3.020 18.791 126.559 1.00168.49 C
ANISOU 48 CA VAL A 41 27538 21329 15153 -3857 433 -5704 C
ATOM 49 C VAL A 41 2.156 17.682 125.973 1.00160.32 C
ANISOU 49 C VAL A 41 26455 20356 14102 -3559 358 -5407 C
ATOM 50 O VAL A 41 1.870 17.669 124.771 1.00155.34 O
ANISOU 50 O VAL A 41 25823 19504 13695 -3397 481 -5254 O
ATOM 51 CB VAL A 41 4.504 18.394 126.626 1.00167.35 C
ANISOU 51 CB VAL A 41 27072 21476 15038 -4128 127 -5811 C
ATOM 52 CG1 VAL A 41 4.940 17.740 125.331 1.00161.75 C
ANISOU 52 CG1 VAL A 41 26186 20746 14526 -4094 25 -5664 C
ATOM 53 CG2 VAL A 41 5.355 19.619 126.915 1.00173.12 C
ANISOU 53 CG2 VAL A 41 27856 22085 15837 -4440 269 -6117 C
ATOM 54 N GLU A 42 1.679 16.765 126.820 1.00160.35 N
ANISOU 54 N GLU A 42 26382 20656 13887 -3441 172 -5277 N
ATOM 55 CA GLU A 42 0.811 15.701 126.326 1.00157.29 C
ANISOU 55 CA GLU A 42 25868 20334 13561 -3124 116 -4937 C
ATOM 56 C GLU A 42 -0.524 16.261 125.850 1.00155.09 C
ANISOU 56 C GLU A 42 25796 19766 13367 -2852 453 -4850 C
ATOM 57 O GLU A 42 -1.030 15.873 124.787 1.00153.94 O
ANISOU 57 O GLU A 42 25533 19525 13434 -2611 507 -4617 O
ATOM 58 CB GLU A 42 0.605 14.654 127.421 1.00163.13 C
ANISOU 58 CB GLU A 42 26518 21431 14031 -3078 -118 -4831 C
ATOM 59 CG GLU A 42 -0.266 13.480 127.012 1.00169.19 C
ANISOU 59 CG GLU A 42 27140 22281 14864 -2781 -166 -4484 C
ATOM 60 CD GLU A 42 -1.670 13.573 127.575 1.00175.40 C
ANISOU 60 CD GLU A 42 28114 23030 15501 -2597 47 -4436 C
ATOM 61 OE1 GLU A 42 -1.890 14.401 128.485 1.00180.54 O
ANISOU 61 OE1 GLU A 42 29004 23641 15950 -2697 180 -4660 O
ATOM 62 OE2 GLU A 42 -2.550 12.819 127.105 1.00175.73 O
ANISOU 62 OE2 GLU A 42 28055 23092 15622 -2363 91 -4191 O
ATOM 63 N VAL A 43 -1.096 17.195 126.611 1.00152.76 N
ANISOU 63 N VAL A 43 25804 19341 12898 -2877 685 -5046 N
ATOM 64 CA VAL A 43 -2.352 17.812 126.202 1.00145.43 C
ANISOU 64 CA VAL A 43 25081 18154 12024 -2590 1017 -4983 C
ATOM 65 C VAL A 43 -2.161 18.636 124.936 1.00142.82 C
ANISOU 65 C VAL A 43 24843 17466 11958 -2530 1234 -4995 C
ATOM 66 O VAL A 43 -3.035 18.666 124.063 1.00141.82 O
ANISOU 66 O VAL A 43 24718 17198 11969 -2209 1400 -4812 O
ATOM 67 CB VAL A 43 -2.925 18.659 127.352 1.00145.00 C
ANISOU 67 CB VAL A 43 25280 18044 11770 -2605 1208 -5164 C
ATOM 68 CG1 VAL A 43 -4.156 19.418 126.893 1.00145.25 C
ANISOU 68 CG1 VAL A 43 25536 17802 11852 -2290 1567 -5121 C
ATOM 69 CG2 VAL A 43 -3.262 17.771 128.529 1.00143.46 C
ANISOU 69 CG2 VAL A 43 24976 18199 11333 -2602 1011 -5097 C
ATOM 70 N ALA A 44 -1.012 19.303 124.803 1.00140.75 N
ANISOU 70 N ALA A 44 24653 17066 11760 -2837 1240 -5215 N
ATOM 71 CA ALA A 44 -0.763 20.086 123.598 1.00134.94 C
ANISOU 71 CA ALA A 44 24035 15968 11268 -2802 1466 -5227 C
ATOM 72 C ALA A 44 -0.606 19.186 122.380 1.00134.23 C
ANISOU 72 C ALA A 44 23628 15946 11428 -2636 1303 -4943 C
ATOM 73 O ALA A 44 -1.092 19.512 121.288 1.00131.89 O
ANISOU 73 O ALA A 44 23399 15404 11310 -2385 1503 -4807 O
ATOM 74 CB ALA A 44 0.476 20.961 123.788 1.00134.84 C
ANISOU 74 CB ALA A 44 24085 15828 11321 -3185 1502 -5497 C
ATOM 75 N VAL A 45 0.046 18.035 122.554 1.00132.20 N
ANISOU 75 N VAL A 45 23034 16026 11170 -2751 946 -4844 N
ATOM 76 CA VAL A 45 0.179 17.091 121.452 1.00124.46 C
ANISOU 76 CA VAL A 45 21751 15123 10414 -2595 786 -4572 C
ATOM 77 C VAL A 45 -1.186 16.552 121.056 1.00119.78 C
ANISOU 77 C VAL A 45 21107 14560 9843 -2204 865 -4308 C
ATOM 78 O VAL A 45 -1.500 16.435 119.866 1.00107.04 O
ANISOU 78 O VAL A 45 19410 12826 8435 -1986 942 -4131 O
ATOM 79 CB VAL A 45 1.150 15.959 121.831 1.00117.71 C
ANISOU 79 CB VAL A 45 20576 14628 9520 -2779 397 -4526 C
ATOM 80 CG1 VAL A 45 0.949 14.759 120.921 1.00107.10 C
ANISOU 80 CG1 VAL A 45 18939 13405 8350 -2556 236 -4205 C
ATOM 81 CG2 VAL A 45 2.587 16.449 121.753 1.00112.59 C
ANISOU 81 CG2 VAL A 45 19887 13960 8932 -3133 321 -4763 C
ATOM 82 N LEU A 46 -2.032 16.244 122.043 1.00115.31 N
ANISOU 82 N LEU A 46 20587 14168 9056 -2115 859 -4293 N
ATOM 83 CA LEU A 46 -3.365 15.740 121.726 1.00113.03 C
ANISOU 83 CA LEU A 46 20229 13946 8771 -1771 950 -4078 C
ATOM 84 C LEU A 46 -4.224 16.801 121.048 1.00111.04 C
ANISOU 84 C LEU A 46 20200 13401 8589 -1505 1296 -4095 C
ATOM 85 O LEU A 46 -5.004 16.485 120.143 1.00109.87 O
ANISOU 85 O LEU A 46 19927 13261 8557 -1208 1366 -3903 O
ATOM 86 CB LEU A 46 -4.052 15.225 122.990 1.00120.82 C
ANISOU 86 CB LEU A 46 21235 15181 9492 -1764 893 -4082 C
ATOM 87 CG LEU A 46 -4.214 13.706 123.046 1.00122.06 C
ANISOU 87 CG LEU A 46 21102 15641 9632 -1716 651 -3852 C
ATOM 88 CD1 LEU A 46 -2.855 13.047 122.999 1.00119.82 C
ANISOU 88 CD1 LEU A 46 20639 15479 9410 -1944 349 -3831 C
ATOM 89 CD2 LEU A 46 -4.976 13.280 124.291 1.00126.91 C
ANISOU 89 CD2 LEU A 46 21784 16465 9971 -1703 650 -3861 C
ATOM 90 N CYS A 47 -4.083 18.067 121.449 1.00115.41 N
ANISOU 90 N CYS A 47 21091 13697 9063 -1598 1524 -4328 N
ATOM 91 CA CYS A 47 -4.870 19.120 120.816 1.00115.27 C
ANISOU 91 CA CYS A 47 21333 13375 9091 -1309 1875 -4338 C
ATOM 92 C CYS A 47 -4.414 19.362 119.383 1.00113.85 C
ANISOU 92 C CYS A 47 21120 12969 9168 -1221 1940 -4238 C
ATOM 93 O CYS A 47 -5.248 19.499 118.477 1.00110.17 O
ANISOU 93 O CYS A 47 20655 12421 8784 -854 2099 -4082 O
ATOM 94 CB CYS A 47 -4.788 20.411 121.634 1.00116.15 C
ANISOU 94 CB CYS A 47 21856 13234 9043 -1445 2126 -4620 C
ATOM 95 SG CYS A 47 -5.614 20.353 123.247 1.00135.99 S
ANISOU 95 SG CYS A 47 24478 15962 11232 -1455 2142 -4738 S
ATOM 96 N LEU A 48 -3.097 19.400 119.152 1.00116.91 N
ANISOU 96 N LEU A 48 21465 13280 9675 -1546 1816 -4330 N
ATOM 97 CA LEU A 48 -2.612 19.515 117.783 1.00124.44 C
ANISOU 97 CA LEU A 48 22364 14041 10876 -1484 1861 -4224 C
ATOM 98 C LEU A 48 -3.062 18.325 116.951 1.00114.63 C
ANISOU 98 C LEU A 48 20756 13036 9760 -1239 1673 -3931 C
ATOM 99 O LEU A 48 -3.484 18.489 115.800 1.00111.32 O
ANISOU 99 O LEU A 48 20335 12482 9480 -956 1807 -3783 O
ATOM 100 CB LEU A 48 -1.087 19.621 117.766 1.00135.51 C
ANISOU 100 CB LEU A 48 23724 15390 12373 -1910 1732 -4387 C
ATOM 101 CG LEU A 48 -0.466 21.002 117.565 1.00146.16 C
ANISOU 101 CG LEU A 48 25445 16328 13760 -2102 2033 -4626 C
ATOM 102 CD1 LEU A 48 1.049 20.916 117.627 1.00149.83 C
ANISOU 102 CD1 LEU A 48 25776 16847 14306 -2559 1860 -4804 C
ATOM 103 CD2 LEU A 48 -0.911 21.579 116.236 1.00145.89 C
ANISOU 103 CD2 LEU A 48 25580 15964 13888 -1780 2310 -4479 C
ATOM 104 N ILE A 49 -3.024 17.125 117.535 1.00116.57 N
ANISOU 104 N ILE A 49 20712 13637 9943 -1333 1378 -3846 N
ATOM 105 CA ILE A 49 -3.413 15.929 116.800 1.00112.22 C
ANISOU 105 CA ILE A 49 19825 13309 9506 -1146 1208 -3586 C
ATOM 106 C ILE A 49 -4.884 15.991 116.430 1.00108.78 C
ANISOU 106 C ILE A 49 19400 12906 9026 -746 1396 -3464 C
ATOM 107 O ILE A 49 -5.262 15.685 115.298 1.00107.39 O
ANISOU 107 O ILE A 49 19071 12740 8994 -509 1419 -3293 O
ATOM 108 CB ILE A 49 -3.087 14.667 117.621 1.00100.39 C
ANISOU 108 CB ILE A 49 18078 12152 7914 -1331 892 -3531 C
ATOM 109 CG1 ILE A 49 -1.602 14.325 117.507 1.00100.10 C
ANISOU 109 CG1 ILE A 49 17903 12147 7983 -1634 658 -3575 C
ATOM 110 CG2 ILE A 49 -3.942 13.493 117.172 1.00 97.77 C
ANISOU 110 CG2 ILE A 49 17477 12051 7618 -1105 803 -3290 C
ATOM 111 CD1 ILE A 49 -1.200 13.117 118.317 1.00 99.46 C
ANISOU 111 CD1 ILE A 49 17609 12392 7788 -1778 350 -3513 C
ATOM 112 N LEU A 50 -5.732 16.437 117.357 1.00110.27 N
ANISOU 112 N LEU A 50 19767 13125 9006 -657 1543 -3563 N
ATOM 113 CA LEU A 50 -7.154 16.536 117.054 1.00111.49 C
ANISOU 113 CA LEU A 50 19912 13353 9098 -265 1729 -3471 C
ATOM 114 C LEU A 50 -7.410 17.573 115.970 1.00103.61 C
ANISOU 114 C LEU A 50 19104 12062 8199 27 1994 -3451 C
ATOM 115 O LEU A 50 -8.179 17.326 115.030 1.00102.35 O
ANISOU 115 O LEU A 50 18788 11995 8104 358 2047 -3294 O
ATOM 116 CB LEU A 50 -7.933 16.878 118.325 1.00119.57 C
ANISOU 116 CB LEU A 50 21105 14458 9869 -243 1846 -3603 C
ATOM 117 CG LEU A 50 -9.438 17.104 118.188 1.00122.58 C
ANISOU 117 CG LEU A 50 21487 14942 10146 162 2062 -3553 C
ATOM 118 CD1 LEU A 50 -10.110 15.888 117.580 1.00120.61 C
ANISOU 118 CD1 LEU A 50 20846 15021 9960 312 1927 -3357 C
ATOM 119 CD2 LEU A 50 -10.044 17.422 119.542 1.00120.87 C
ANISOU 119 CD2 LEU A 50 21446 14802 9679 127 2164 -3702 C
ATOM 120 N LEU A 51 -6.727 18.719 116.052 1.00105.85 N
ANISOU 120 N LEU A 51 19732 11994 8493 -99 2165 -3613 N
ATOM 121 CA LEU A 51 -6.943 19.777 115.072 1.00114.94 C
ANISOU 121 CA LEU A 51 21140 12816 9715 187 2457 -3593 C
ATOM 122 C LEU A 51 -6.528 19.300 113.687 1.00106.90 C
ANISOU 122 C LEU A 51 19910 11786 8921 280 2365 -3409 C
ATOM 123 O LEU A 51 -7.331 19.310 112.744 1.00107.60 O
ANISOU 123 O LEU A 51 19931 11913 9037 681 2469 -3257 O
ATOM 124 CB LEU A 51 -6.147 21.026 115.457 1.00118.82 C
ANISOU 124 CB LEU A 51 22061 12905 10179 -44 2670 -3820 C
ATOM 125 CG LEU A 51 -5.892 22.029 114.324 1.00117.52 C
ANISOU 125 CG LEU A 51 22186 12330 10137 127 2948 -3798 C
ATOM 126 CD1 LEU A 51 -7.175 22.727 113.891 1.00112.82 C
ANISOU 126 CD1 LEU A 51 21797 11632 9437 674 3247 -3709 C
ATOM 127 CD2 LEU A 51 -4.829 23.042 114.722 1.00114.19 C
ANISOU 127 CD2 LEU A 51 22135 11533 9719 -247 3116 -4048 C
ATOM 128 N LEU A 52 -5.270 18.866 113.542 1.00106.46 N
ANISOU 128 N LEU A 52 19732 11703 9016 -77 2165 -3427 N
ATOM 129 CA LEU A 52 -4.832 18.464 112.212 1.00101.33 C
ANISOU 129 CA LEU A 52 18902 11018 8580 4 2096 -3261 C
ATOM 130 C LEU A 52 -5.509 17.184 111.737 1.00 98.31 C
ANISOU 130 C LEU A 52 18103 11011 8240 180 1882 -3053 C
ATOM 131 O LEU A 52 -5.718 17.034 110.533 1.00111.33 O
ANISOU 131 O LEU A 52 19630 12655 10014 411 1902 -2898 O
ATOM 132 CB LEU A 52 -3.306 18.360 112.125 1.00101.04 C
ANISOU 132 CB LEU A 52 18837 10858 8697 -412 1958 -3346 C
ATOM 133 CG LEU A 52 -2.503 17.373 112.960 1.00110.12 C
ANISOU 133 CG LEU A 52 19888 12166 9788 -851 1721 -3498 C
ATOM 134 CD1 LEU A 52 -2.548 15.994 112.354 1.00108.08 C
ANISOU 134 CD1 LEU A 52 19225 12305 9536 -880 1391 -3345 C
ATOM 135 CD2 LEU A 52 -1.070 17.846 113.185 1.00110.19 C
ANISOU 135 CD2 LEU A 52 19979 11968 9918 -1220 1713 -3654 C
ATOM 136 N ALA A 53 -5.921 16.293 112.644 1.00 97.55 N
ANISOU 136 N ALA A 53 17807 11231 8027 86 1705 -3050 N
ATOM 137 CA ALA A 53 -6.663 15.112 112.226 1.00 95.10 C
ANISOU 137 CA ALA A 53 17134 11260 7741 239 1552 -2873 C
ATOM 138 C ALA A 53 -8.007 15.462 111.613 1.00 95.59 C
ANISOU 138 C ALA A 53 17191 11392 7736 692 1758 -2800 C
ATOM 139 O ALA A 53 -8.300 15.077 110.474 1.00108.73 O
ANISOU 139 O ALA A 53 18658 13146 9509 907 1740 -2656 O
ATOM 140 CB ALA A 53 -6.856 14.190 113.431 1.00 94.75 C
ANISOU 140 CB ALA A 53 16942 11502 7555 40 1371 -2899 C
ATOM 141 N LEU A 54 -8.820 16.234 112.339 1.00 97.97 N
ANISOU 141 N LEU A 54 17712 11664 7849 857 1960 -2908 N
ATOM 142 CA LEU A 54 -10.117 16.617 111.802 1.00 98.88 C
ANISOU 142 CA LEU A 54 17814 11881 7873 1326 2160 -2852 C
ATOM 143 C LEU A 54 -9.954 17.408 110.513 1.00115.14 C
ANISOU 143 C LEU A 54 20026 13680 10041 1606 2324 -2775 C
ATOM 144 O LEU A 54 -10.621 17.115 109.511 1.00121.97 O
ANISOU 144 O LEU A 54 20685 14723 10936 1931 2336 -2644 O
ATOM 145 CB LEU A 54 -10.895 17.427 112.841 1.00127.16 C
ANISOU 145 CB LEU A 54 21650 15435 11232 1454 2368 -2994 C
ATOM 146 CG LEU A 54 -11.964 16.677 113.645 1.00120.05 C
ANISOU 146 CG LEU A 54 20515 14933 10166 1496 2314 -3009 C
ATOM 147 CD1 LEU A 54 -11.425 15.370 114.213 1.00119.09 C
ANISOU 147 CD1 LEU A 54 20137 15024 10088 1095 2026 -2980 C
ATOM 148 CD2 LEU A 54 -12.526 17.557 114.756 1.00104.62 C
ANISOU 148 CD2 LEU A 54 18854 12900 7997 1569 2521 -3170 C
ATOM 149 N SER A 55 -9.006 18.351 110.485 1.00106.93 N
ANISOU 149 N SER A 55 19336 12227 9063 1457 2447 -2859 N
ATOM 150 CA SER A 55 -8.877 19.205 109.311 1.00113.67 C
ANISOU 150 CA SER A 55 20409 12785 9996 1735 2654 -2789 C
ATOM 151 C SER A 55 -8.408 18.413 108.095 1.00105.12 C
ANISOU 151 C SER A 55 19034 11794 9112 1725 2478 -2624 C
ATOM 152 O SER A 55 -9.015 18.498 107.023 1.00104.92 O
ANISOU 152 O SER A 55 18943 11828 9095 2118 2563 -2491 O
ATOM 153 CB SER A 55 -7.927 20.365 109.609 1.00121.86 C
ANISOU 153 CB SER A 55 21906 13344 11053 1515 2852 -2941 C
ATOM 154 OG SER A 55 -6.667 19.894 110.037 1.00123.25 O
ANISOU 154 OG SER A 55 21993 13486 11350 994 2639 -3026 O
ATOM 155 N GLY A 56 -7.343 17.618 108.238 1.00103.85 N
ANISOU 155 N GLY A 56 18689 11670 9100 1297 2228 -2630 N
ATOM 156 CA GLY A 56 -6.810 16.910 107.088 1.00107.90 C
ANISOU 156 CA GLY A 56 18953 12236 9807 1272 2076 -2484 C
ATOM 157 C GLY A 56 -7.703 15.784 106.611 1.00110.81 C
ANISOU 157 C GLY A 56 18910 13023 10170 1474 1922 -2342 C
ATOM 158 O GLY A 56 -7.836 15.560 105.404 1.00112.09 O
ANISOU 158 O GLY A 56 18931 13235 10424 1691 1918 -2209 O
ATOM 159 N ASN A 57 -8.350 15.072 107.538 1.00111.10 N
ANISOU 159 N ASN A 57 18756 13369 10087 1400 1810 -2378 N
ATOM 160 CA ASN A 57 -9.261 14.025 107.101 1.00114.86 C
ANISOU 160 CA ASN A 57 18851 14245 10544 1566 1702 -2272 C
ATOM 161 C ASN A 57 -10.493 14.615 106.425 1.00118.87 C
ANISOU 161 C ASN A 57 19365 14868 10933 2075 1907 -2235 C
ATOM 162 O ASN A 57 -10.981 14.061 105.432 1.00120.35 O
ANISOU 162 O ASN A 57 19278 15290 11159 2283 1859 -2130 O
ATOM 163 CB ASN A 57 -9.644 13.126 108.277 1.00116.58 C
ANISOU 163 CB ASN A 57 18895 14747 10655 1342 1566 -2327 C
ATOM 164 CG ASN A 57 -8.582 12.077 108.573 1.00114.42 C
ANISOU 164 CG ASN A 57 18471 14498 10506 927 1305 -2293 C
ATOM 165 OD1 ASN A 57 -8.484 11.066 107.875 1.00106.23 O
ANISOU 165 OD1 ASN A 57 17155 13625 9584 887 1160 -2179 O
ATOM 166 ND2 ASN A 57 -7.779 12.316 109.609 1.00116.91 N
ANISOU 166 ND2 ASN A 57 18974 14661 10787 629 1247 -2397 N
ATOM 167 N ALA A 58 -10.994 15.756 106.914 1.00121.31 N
ANISOU 167 N ALA A 58 19986 15021 11085 2299 2142 -2325 N
ATOM 168 CA ALA A 58 -12.087 16.409 106.203 1.00123.77 C
ANISOU 168 CA ALA A 58 20331 15427 11270 2840 2347 -2280 C
ATOM 169 C ALA A 58 -11.635 16.913 104.838 1.00131.66 C
ANISOU 169 C ALA A 58 21451 16193 12382 3066 2430 -2161 C
ATOM 170 O ALA A 58 -12.403 16.867 103.867 1.00134.61 O
ANISOU 170 O ALA A 58 21659 16782 12703 3473 2475 -2067 O
ATOM 171 CB ALA A 58 -12.646 17.559 107.038 1.00118.00 C
ANISOU 171 CB ALA A 58 19953 14537 10344 3043 2598 -2397 C
ATOM 172 N CYS A 59 -10.388 17.385 104.737 1.00130.43 N
ANISOU 172 N CYS A 59 21573 15616 12370 2802 2455 -2174 N
ATOM 173 CA CYS A 59 -9.879 17.831 103.445 1.00128.13 C
ANISOU 173 CA CYS A 59 21414 15079 12192 2975 2546 -2062 C
ATOM 174 C CYS A 59 -9.786 16.672 102.467 1.00125.41 C
ANISOU 174 C CYS A 59 20646 15020 11984 2947 2318 -1931 C
ATOM 175 O CYS A 59 -10.045 16.837 101.270 1.00127.36 O
ANISOU 175 O CYS A 59 20863 15289 12240 3288 2386 -1813 O
ATOM 176 CB CYS A 59 -8.511 18.494 103.610 1.00134.61 C
ANISOU 176 CB CYS A 59 22588 15413 13145 2622 2621 -2133 C
ATOM 177 SG CYS A 59 -8.540 20.084 104.471 1.00148.21 S
ANISOU 177 SG CYS A 59 24905 16697 14712 2687 2972 -2292 S
ATOM 178 N VAL A 60 -9.436 15.484 102.962 1.00124.02 N
ANISOU 178 N VAL A 60 20155 15067 11901 2557 2054 -1949 N
ATOM 179 CA VAL A 60 -9.397 14.320 102.085 1.00114.81 C
ANISOU 179 CA VAL A 60 18594 14174 10856 2517 1851 -1836 C
ATOM 180 C VAL A 60 -10.806 13.919 101.673 1.00112.95 C
ANISOU 180 C VAL A 60 18064 14379 10474 2893 1865 -1801 C
ATOM 181 O VAL A 60 -11.062 13.632 100.499 1.00106.68 O
ANISOU 181 O VAL A 60 17080 13739 9713 3124 1842 -1701 O
ATOM 182 CB VAL A 60 -8.653 13.156 102.761 1.00103.29 C
ANISOU 182 CB VAL A 60 16914 12814 9517 2022 1590 -1861 C
ATOM 183 CG1 VAL A 60 -8.763 11.903 101.911 1.00 97.98 C
ANISOU 183 CG1 VAL A 60 15843 12437 8947 1998 1407 -1753 C
ATOM 184 CG2 VAL A 60 -7.193 13.519 102.976 1.00102.87 C
ANISOU 184 CG2 VAL A 60 17090 12383 9613 1673 1557 -1900 C
ATOM 185 N LEU A 61 -11.750 13.922 102.619 1.00115.23 N
ANISOU 185 N LEU A 61 18303 14895 10585 2963 1912 -1896 N
ATOM 186 CA LEU A 61 -13.115 13.528 102.284 1.00114.64 C
ANISOU 186 CA LEU A 61 17911 15291 10357 3296 1930 -1897 C
ATOM 187 C LEU A 61 -13.768 14.497 101.306 1.00113.14 C
ANISOU 187 C LEU A 61 17839 15101 10047 3869 2127 -1838 C
ATOM 188 O LEU A 61 -14.610 14.084 100.502 1.00115.33 O
ANISOU 188 O LEU A 61 17802 15771 10249 4161 2100 -1802 O
ATOM 189 CB LEU A 61 -13.969 13.415 103.546 1.00119.15 C
ANISOU 189 CB LEU A 61 18426 16090 10754 3248 1967 -2025 C
ATOM 190 CG LEU A 61 -14.145 12.003 104.102 1.00121.79 C
ANISOU 190 CG LEU A 61 18406 16753 11116 2882 1775 -2061 C
ATOM 191 CD1 LEU A 61 -12.861 11.536 104.743 1.00121.13 C
ANISOU 191 CD1 LEU A 61 18442 16392 11192 2386 1617 -2051 C
ATOM 192 CD2 LEU A 61 -15.292 11.954 105.096 1.00124.88 C
ANISOU 192 CD2 LEU A 61 18703 17448 11296 2952 1861 -2185 C
ATOM 193 N LEU A 62 -13.403 15.779 101.355 1.00112.00 N
ANISOU 193 N LEU A 62 18153 14534 9869 4045 2335 -1833 N
ATOM 194 CA LEU A 62 -13.968 16.725 100.400 1.00112.86 C
ANISOU 194 CA LEU A 62 18431 14602 9848 4626 2541 -1754 C
ATOM 195 C LEU A 62 -13.243 16.675 99.063 1.00125.30 C
ANISOU 195 C LEU A 62 20024 16012 11571 4681 2507 -1613 C
ATOM 196 O LEU A 62 -13.874 16.803 98.008 1.00136.60 O
ANISOU 196 O LEU A 62 21345 17653 12905 5135 2558 -1524 O
ATOM 197 CB LEU A 62 -13.924 18.143 100.970 1.00107.95 C
ANISOU 197 CB LEU A 62 18342 13562 9112 4817 2822 -1802 C
ATOM 198 CG LEU A 62 -15.014 18.480 101.985 1.00119.34 C
ANISOU 198 CG LEU A 62 19794 15220 10331 5018 2933 -1919 C
ATOM 199 CD1 LEU A 62 -14.894 19.920 102.460 1.00129.65 C
ANISOU 199 CD1 LEU A 62 21674 16058 11530 5213 3236 -1962 C
ATOM 200 CD2 LEU A 62 -16.376 18.229 101.370 1.00120.45 C
ANISOU 200 CD2 LEU A 62 19578 15905 10283 5529 2937 -1890 C
ATOM 201 N ALA A 63 -11.922 16.489 99.088 1.00123.23 N
ANISOU 201 N ALA A 63 19889 15401 11533 4232 2422 -1598 N
ATOM 202 CA ALA A 63 -11.143 16.559 97.858 1.00125.13 C
ANISOU 202 CA ALA A 63 20200 15426 11916 4266 2424 -1472 C
ATOM 203 C ALA A 63 -11.475 15.419 96.902 1.00123.75 C
ANISOU 203 C ALA A 63 19549 15680 11792 4321 2220 -1392 C
ATOM 204 O ALA A 63 -11.358 15.586 95.683 1.00123.42 O
ANISOU 204 O ALA A 63 19523 15599 11770 4578 2262 -1276 O
ATOM 205 CB ALA A 63 -9.652 16.570 98.193 1.00122.18 C
ANISOU 205 CB ALA A 63 20027 14630 11766 3740 2373 -1505 C
ATOM 206 N LEU A 64 -11.890 14.263 97.424 1.00124.07 N
ANISOU 206 N LEU A 64 19182 16118 11842 4078 2016 -1456 N
ATOM 207 CA LEU A 64 -12.242 13.116 96.596 1.00128.15 C
ANISOU 207 CA LEU A 64 19243 17050 12400 4080 1837 -1411 C
ATOM 208 C LEU A 64 -13.718 12.745 96.711 1.00136.14 C
ANISOU 208 C LEU A 64 19914 18615 13198 4360 1835 -1484 C
ATOM 209 O LEU A 64 -14.101 11.629 96.344 1.00141.66 O
ANISOU 209 O LEU A 64 20196 19710 13918 4248 1682 -1502 O
ATOM 210 CB LEU A 64 -11.357 11.915 96.941 1.00125.85 C
ANISOU 210 CB LEU A 64 18749 16745 12323 3513 1606 -1421 C
ATOM 211 CG LEU A 64 -11.249 11.397 98.379 1.00126.21 C
ANISOU 211 CG LEU A 64 18761 16816 12376 3110 1514 -1528 C
ATOM 212 CD1 LEU A 64 -12.426 10.517 98.769 1.00125.18 C
ANISOU 212 CD1 LEU A 64 18261 17191 12113 3124 1451 -1605 C
ATOM 213 CD2 LEU A 64 -9.941 10.647 98.569 1.00123.32 C
ANISOU 213 CD2 LEU A 64 18378 16243 12237 2619 1333 -1499 C
ATOM 214 N HIS A 65 -14.548 13.655 97.218 1.00134.82 N
ANISOU 214 N HIS A 65 19916 18488 12820 4709 2014 -1541 N
ATOM 215 CA HIS A 65 -15.964 13.383 97.461 1.00132.02 C
ANISOU 215 CA HIS A 65 19237 18679 12247 4969 2029 -1639 C
ATOM 216 C HIS A 65 -16.678 12.789 96.250 1.00125.74 C
ANISOU 216 C HIS A 65 18028 18370 11378 5248 1953 -1612 C
ATOM 217 O HIS A 65 -17.441 11.832 96.382 1.00122.17 O
ANISOU 217 O HIS A 65 17143 18410 10867 5135 1851 -1715 O
ATOM 218 CB HIS A 65 -16.686 14.659 97.891 1.00140.57 C
ANISOU 218 CB HIS A 65 20614 19693 13104 5432 2267 -1673 C
ATOM 219 CG HIS A 65 -18.153 14.471 98.116 1.00148.74 C
ANISOU 219 CG HIS A 65 21306 21312 13897 5741 2297 -1784 C
ATOM 220 ND1 HIS A 65 -18.655 13.733 99.167 1.00148.16 N
ANISOU 220 ND1 HIS A 65 20980 21521 13791 5427 2226 -1926 N
ATOM 221 CD2 HIS A 65 -19.227 14.912 97.420 1.00152.69 C
ANISOU 221 CD2 HIS A 65 21624 22144 14247 6249 2343 -1740 C
ATOM 222 CE1 HIS A 65 -19.975 13.734 99.112 1.00150.83 C
ANISOU 222 CE1 HIS A 65 21016 22378 13917 5774 2277 -2012 C
ATOM 223 NE2 HIS A 65 -20.347 14.443 98.061 1.00154.67 N
ANISOU 223 NE2 HIS A 65 21498 22873 14394 6209 2296 -1869 N
ATOM 224 N HIS A 71 -5.447 1.658 89.304 1.00136.45 N
ANISOU 224 N HIS A 71 17973 18569 15303 1507 240 -817 N
ATOM 225 CA HIS A 71 -6.622 0.762 89.471 1.00139.36 C
ANISOU 225 CA HIS A 71 18086 19332 15531 1484 241 -914 C
ATOM 226 C HIS A 71 -7.898 1.581 89.689 1.00143.49 C
ANISOU 226 C HIS A 71 18593 20103 15822 1812 357 -995 C
ATOM 227 O HIS A 71 -8.965 1.102 89.255 1.00150.05 O
ANISOU 227 O HIS A 71 19173 21319 16519 1977 391 -1066 O
ATOM 228 CB HIS A 71 -6.392 -0.225 90.611 1.00141.51 C
ANISOU 228 CB HIS A 71 18356 19579 15833 1134 169 -949 C
ATOM 229 CG HIS A 71 -7.636 -0.921 91.046 1.00143.45 C
ANISOU 229 CG HIS A 71 18375 20200 15930 1068 206 -1064 C
ATOM 230 ND1 HIS A 71 -7.866 -1.261 92.356 1.00144.30 N
ANISOU 230 ND1 HIS A 71 18525 20350 15953 886 215 -1127 N
ATOM 231 CD2 HIS A 71 -8.710 -1.343 90.354 1.00143.72 C
ANISOU 231 CD2 HIS A 71 18133 20602 15873 1147 249 -1144 C
ATOM 232 CE1 HIS A 71 -9.027 -1.858 92.452 1.00145.42 C
ANISOU 232 CE1 HIS A 71 18432 20853 15966 843 276 -1242 C
ATOM 233 NE2 HIS A 71 -9.565 -1.914 91.241 1.00144.27 N
ANISOU 233 NE2 HIS A 71 18079 20923 15815 991 295 -1264 N
ATOM 234 N SER A 72 -7.779 2.699 90.420 1.00136.66 N
ANISOU 234 N SER A 72 17986 19034 14904 1901 420 -997 N
ATOM 235 CA SER A 72 -8.799 3.755 90.691 1.00129.15 C
ANISOU 235 CA SER A 72 17122 18205 13746 2252 550 -1050 C
ATOM 236 C SER A 72 -9.755 3.460 91.847 1.00115.57 C
ANISOU 236 C SER A 72 15287 16759 11866 2184 572 -1175 C
ATOM 237 O SER A 72 -10.535 4.359 92.171 1.00113.18 O
ANISOU 237 O SER A 72 15058 16559 11387 2471 683 -1226 O
ATOM 238 CB SER A 72 -9.539 4.231 89.455 1.00134.63 C
ANISOU 238 CB SER A 72 17690 19155 14308 2677 625 -1038 C
ATOM 239 OG SER A 72 -10.533 3.296 89.061 1.00134.31 O
ANISOU 239 OG SER A 72 17270 19572 14190 2646 577 -1124 O
ATOM 240 N ARG A 73 -9.708 2.284 92.463 1.00108.91 N
ANISOU 240 N ARG A 73 14286 16026 11068 1829 490 -1223 N
ATOM 241 CA ARG A 73 -10.622 2.091 93.618 1.00105.87 C
ANISOU 241 CA ARG A 73 13875 15807 10546 1718 529 -1332 C
ATOM 242 C ARG A 73 -9.967 2.719 94.841 1.00 97.69 C
ANISOU 242 C ARG A 73 13158 14419 9542 1594 523 -1306 C
ATOM 243 O ARG A 73 -10.613 2.867 95.862 1.00 94.84 O
ANISOU 243 O ARG A 73 12832 14148 9053 1535 568 -1390 O
ATOM 244 CB ARG A 73 -10.844 0.610 93.920 1.00107.04 C
ANISOU 244 CB ARG A 73 13798 16156 10716 1370 475 -1389 C
ATOM 245 CG ARG A 73 -11.853 -0.052 93.001 1.00111.93 C
ANISOU 245 CG ARG A 73 14068 17207 11254 1443 510 -1479 C
ATOM 246 CD ARG A 73 -13.037 0.871 92.886 1.00120.04 C
ANISOU 246 CD ARG A 73 14946 18619 12047 1778 621 -1602 C
ATOM 247 NE ARG A 73 -13.687 0.658 91.611 1.00128.02 N
ANISOU 247 NE ARG A 73 15652 20004 12985 1976 633 -1660 N
ATOM 248 CZ ARG A 73 -13.145 0.987 90.452 1.00132.97 C
ANISOU 248 CZ ARG A 73 16315 20574 13634 2290 619 -1571 C
ATOM 249 NH1 ARG A 73 -11.945 1.537 90.422 1.00133.01 N
ANISOU 249 NH1 ARG A 73 16656 20141 13741 2417 611 -1425 N
ATOM 250 NH2 ARG A 73 -13.798 0.766 89.327 1.00136.04 N
ANISOU 250 NH2 ARG A 73 16407 21349 13932 2466 622 -1636 N
ATOM 251 N LEU A 74 -8.710 3.099 94.682 1.00 98.25 N
ANISOU 251 N LEU A 74 13449 14109 9774 1540 474 -1208 N
ATOM 252 CA LEU A 74 -7.921 3.637 95.778 1.00 89.77 C
ANISOU 252 CA LEU A 74 12659 12712 8740 1377 455 -1204 C
ATOM 253 C LEU A 74 -8.576 4.863 96.403 1.00 99.89 C
ANISOU 253 C LEU A 74 14130 13976 9849 1610 595 -1276 C
ATOM 254 O LEU A 74 -8.445 5.082 97.608 1.00100.44 O
ANISOU 254 O LEU A 74 14349 13948 9865 1452 593 -1330 O
ATOM 255 CB LEU A 74 -6.525 3.990 95.256 1.00 82.13 C
ANISOU 255 CB LEU A 74 11856 11385 7964 1309 406 -1112 C
ATOM 256 CG LEU A 74 -5.483 4.645 96.155 1.00 85.52 C
ANISOU 256 CG LEU A 74 12475 11516 8502 1009 314 -1106 C
ATOM 257 CD1 LEU A 74 -5.134 3.720 97.292 1.00 95.87 C
ANISOU 257 CD1 LEU A 74 14094 12566 9765 1111 431 -1153 C
ATOM 258 CD2 LEU A 74 -4.244 5.018 95.362 1.00 84.36 C
ANISOU 258 CD2 LEU A 74 12260 11499 8293 752 222 -1147 C
ATOM 259 N PHE A 75 -9.329 5.639 95.616 1.00101.06 N
ANISOU 259 N PHE A 75 14273 14238 9887 2003 722 -1279 N
ATOM 260 CA PHE A 75 -10.016 6.806 96.164 1.00108.99 C
ANISOU 260 CA PHE A 75 15468 15230 10712 2272 876 -1344 C
ATOM 261 C PHE A 75 -11.143 6.366 97.093 1.00113.94 C
ANISOU 261 C PHE A 75 15925 16200 11165 2240 897 -1459 C
ATOM 262 O PHE A 75 -11.330 6.944 98.170 1.00118.08 O
ANISOU 262 O PHE A 75 16638 16636 11592 2226 966 -1525 O
ATOM 263 CB PHE A 75 -10.569 7.696 95.054 1.00105.46 C
ANISOU 263 CB PHE A 75 15057 14843 10168 2750 1009 -1303 C
ATOM 264 CG PHE A 75 -9.521 8.234 94.134 1.00110.65 C
ANISOU 264 CG PHE A 75 15922 15144 10975 2802 1030 -1190 C
ATOM 265 CD1 PHE A 75 -8.794 9.360 94.479 1.00115.24 C
ANISOU 265 CD1 PHE A 75 16900 15294 11590 2813 1144 -1176 C
ATOM 266 CD2 PHE A 75 -9.263 7.619 92.921 1.00112.99 C
ANISOU 266 CD2 PHE A 75 16025 15534 11373 2823 954 -1113 C
ATOM 267 CE1 PHE A 75 -7.825 9.864 93.631 1.00120.10 C
ANISOU 267 CE1 PHE A 75 17715 15575 12340 2833 1192 -1086 C
ATOM 268 CE2 PHE A 75 -8.297 8.117 92.067 1.00113.97 C
ANISOU 268 CE2 PHE A 75 16345 15329 11630 2865 989 -1011 C
ATOM 269 CZ PHE A 75 -7.577 9.241 92.423 1.00118.57 C
ANISOU 269 CZ PHE A 75 17323 15480 12248 2865 1113 -999 C
ATOM 270 N PHE A 76 -11.903 5.344 96.695 1.00105.16 N
ANISOU 270 N PHE A 76 14461 15484 10010 2208 853 -1500 N
ATOM 271 CA PHE A 76 -12.990 4.850 97.537 1.00 92.51 C
ANISOU 271 CA PHE A 76 12676 14227 8244 2140 893 -1627 C
ATOM 272 C PHE A 76 -12.449 4.241 98.826 1.00 86.70 C
ANISOU 272 C PHE A 76 12055 13328 7558 1724 822 -1643 C
ATOM 273 O PHE A 76 -12.986 4.484 99.923 1.00 97.21 O
ANISOU 273 O PHE A 76 13462 14722 8751 1696 890 -1729 O
ATOM 274 CB PHE A 76 -13.813 3.837 96.735 1.00 90.23 C
ANISOU 274 CB PHE A 76 11983 14386 7913 2142 874 -1686 C
ATOM 275 CG PHE A 76 -14.815 3.068 97.546 1.00 82.09 C
ANISOU 275 CG PHE A 76 10735 13711 6744 1964 918 -1829 C
ATOM 276 CD1 PHE A 76 -16.009 3.650 97.934 1.00 88.79 C
ANISOU 276 CD1 PHE A 76 11495 14868 7372 2224 1046 -1953 C
ATOM 277 CD2 PHE A 76 -14.575 1.748 97.889 1.00 75.74 C
ANISOU 277 CD2 PHE A 76 9820 12937 6022 1544 852 -1843 C
ATOM 278 CE1 PHE A 76 -16.938 2.936 98.670 1.00 91.14 C
ANISOU 278 CE1 PHE A 76 11582 15505 7541 2037 1106 -2100 C
ATOM 279 CE2 PHE A 76 -15.498 1.029 98.624 1.00 81.40 C
ANISOU 279 CE2 PHE A 76 10363 13960 6606 1356 926 -1980 C
ATOM 280 CZ PHE A 76 -16.680 1.624 99.017 1.00 86.08 C
ANISOU 280 CZ PHE A 76 10852 14869 6986 1588 1053 -2116 C
ATOM 281 N PHE A 77 -11.361 3.471 98.717 1.00 81.24 N
ANISOU 281 N PHE A 77 11388 12427 7052 1420 686 -1556 N
ATOM 282 CA PHE A 77 -10.735 2.923 99.915 1.00 85.19 C
ANISOU 282 CA PHE A 77 12021 12763 7584 1066 606 -1551 C
ATOM 283 C PHE A 77 -10.146 4.026 100.791 1.00 92.55 C
ANISOU 283 C PHE A 77 13283 13387 8493 1082 626 -1559 C
ATOM 284 O PHE A 77 -10.218 3.946 102.022 1.00 94.45 O
ANISOU 284 O PHE A 77 13633 13612 8640 917 626 -1614 O
ATOM 285 CB PHE A 77 -9.672 1.896 99.523 1.00 80.37 C
ANISOU 285 CB PHE A 77 11362 12009 7165 796 458 -1449 C
ATOM 286 CG PHE A 77 -10.244 0.655 98.894 1.00 77.20 C
ANISOU 286 CG PHE A 77 10668 11893 6774 699 454 -1462 C
ATOM 287 CD1 PHE A 77 -11.285 -0.023 99.503 1.00 75.85 C
ANISOU 287 CD1 PHE A 77 10353 12013 6453 590 533 -1566 C
ATOM 288 CD2 PHE A 77 -9.759 0.180 97.686 1.00 84.79 C
ANISOU 288 CD2 PHE A 77 11501 12831 7885 703 391 -1387 C
ATOM 289 CE1 PHE A 77 -11.826 -1.158 98.929 1.00 77.81 C
ANISOU 289 CE1 PHE A 77 10340 12520 6704 464 558 -1606 C
ATOM 290 CE2 PHE A 77 -10.298 -0.959 97.105 1.00 89.90 C
ANISOU 290 CE2 PHE A 77 11887 13737 8533 594 405 -1421 C
ATOM 291 CZ PHE A 77 -11.332 -1.628 97.730 1.00 84.45 C
ANISOU 291 CZ PHE A 77 11060 13332 7694 464 493 -1537 C
ATOM 292 N MET A 78 -9.605 5.087 100.175 1.00 94.06 N
ANISOU 292 N MET A 78 13650 13335 8754 1278 665 -1517 N
ATOM 293 CA MET A 78 -9.132 6.235 100.943 1.00 95.67 C
ANISOU 293 CA MET A 78 14182 13247 8923 1295 726 -1555 C
ATOM 294 C MET A 78 -10.274 6.900 101.689 1.00 92.93 C
ANISOU 294 C MET A 78 13901 13052 8358 1496 877 -1661 C
ATOM 295 O MET A 78 -10.119 7.312 102.844 1.00 92.42 O
ANISOU 295 O MET A 78 14040 12860 8216 1373 900 -1728 O
ATOM 296 CB MET A 78 -8.481 7.262 100.014 1.00 97.02 C
ANISOU 296 CB MET A 78 14538 13132 9193 1487 793 -1499 C
ATOM 297 CG MET A 78 -7.062 6.986 99.574 1.00 94.54 C
ANISOU 297 CG MET A 78 14268 12558 9094 1251 667 -1423 C
ATOM 298 SD MET A 78 -6.679 8.064 98.179 1.00 99.28 S
ANISOU 298 SD MET A 78 15027 12912 9781 1543 798 -1353 S
ATOM 299 CE MET A 78 -4.965 8.465 98.490 1.00 95.85 C
ANISOU 299 CE MET A 78 14833 12060 9525 1211 738 -1362 C
ATOM 300 N LYS A 79 -11.434 7.000 101.042 1.00 91.54 N
ANISOU 300 N LYS A 79 13538 13173 8069 1810 979 -1686 N
ATOM 301 CA LYS A 79 -12.581 7.656 101.656 1.00 93.40 C
ANISOU 301 CA LYS A 79 13808 13593 8089 2052 1133 -1790 C
ATOM 302 C LYS A 79 -13.028 6.898 102.893 1.00 95.32 C
ANISOU 302 C LYS A 79 13965 14020 8232 1780 1105 -1877 C
ATOM 303 O LYS A 79 -13.189 7.478 103.974 1.00 94.26 O
ANISOU 303 O LYS A 79 14033 13799 7983 1762 1178 -1950 O
ATOM 304 CB LYS A 79 -13.718 7.754 100.638 1.00 92.13 C
ANISOU 304 CB LYS A 79 13395 13791 7818 2445 1221 -1805 C
ATOM 305 CG LYS A 79 -14.981 8.442 101.130 1.00 91.85 C
ANISOU 305 CG LYS A 79 13350 14005 7544 2763 1386 -1915 C
ATOM 306 CD LYS A 79 -15.987 8.568 99.989 1.00 94.24 C
ANISOU 306 CD LYS A 79 13386 14689 7733 3191 1452 -1925 C
ATOM 307 CE LYS A 79 -17.299 9.191 100.442 1.00 98.31 C
ANISOU 307 CE LYS A 79 13839 15518 7995 3540 1612 -2043 C
ATOM 308 NZ LYS A 79 -18.254 9.328 99.305 1.00102.26 N
ANISOU 308 NZ LYS A 79 14057 16437 8361 3991 1661 -2059 N
ATOM 309 N HIS A 80 -13.200 5.582 102.759 1.00 92.86 N
ANISOU 309 N HIS A 80 13379 13943 7961 1551 1012 -1870 N
ATOM 310 CA HIS A 80 -13.647 4.814 103.917 1.00 95.34 C
ANISOU 310 CA HIS A 80 13637 14418 8168 1288 1014 -1945 C
ATOM 311 C HIS A 80 -12.574 4.745 105.002 1.00 95.23 C
ANISOU 311 C HIS A 80 13894 14086 8204 982 915 -1910 C
ATOM 312 O HIS A 80 -12.894 4.781 106.199 1.00 88.16 O
ANISOU 312 O HIS A 80 13106 13221 7169 872 960 -1984 O
ATOM 313 CB HIS A 80 -14.097 3.424 103.479 1.00 93.22 C
ANISOU 313 CB HIS A 80 13044 14451 7924 1107 976 -1954 C
ATOM 314 CG HIS A 80 -15.494 3.401 102.944 1.00 97.09 C
ANISOU 314 CG HIS A 80 13231 15387 8272 1344 1101 -2067 C
ATOM 315 ND1 HIS A 80 -16.585 3.082 103.725 1.00 97.10 N
ANISOU 315 ND1 HIS A 80 13099 15702 8092 1284 1215 -2205 N
ATOM 316 CD2 HIS A 80 -15.983 3.691 101.716 1.00 98.62 C
ANISOU 316 CD2 HIS A 80 13221 15792 8459 1654 1133 -2074 C
ATOM 317 CE1 HIS A 80 -17.683 3.158 102.995 1.00102.97 C
ANISOU 317 CE1 HIS A 80 13541 16854 8728 1537 1306 -2305 C
ATOM 318 NE2 HIS A 80 -17.346 3.525 101.772 1.00102.58 N
ANISOU 318 NE2 HIS A 80 13444 16757 8774 1777 1251 -2224 N
ATOM 319 N LEU A 81 -11.294 4.678 104.617 1.00 97.98 N
ANISOU 319 N LEU A 81 14348 14146 8734 852 781 -1808 N
ATOM 320 CA LEU A 81 -10.241 4.629 105.625 1.00 93.31 C
ANISOU 320 CA LEU A 81 13982 13302 8171 579 671 -1791 C
ATOM 321 C LEU A 81 -10.158 5.937 106.401 1.00 89.80 C
ANISOU 321 C LEU A 81 13826 12668 7627 673 760 -1875 C
ATOM 322 O LEU A 81 -9.972 5.930 107.624 1.00 90.67 O
ANISOU 322 O LEU A 81 14086 12729 7634 492 736 -1929 O
ATOM 323 CB LEU A 81 -8.899 4.303 104.968 1.00 91.51 C
ANISOU 323 CB LEU A 81 13766 12848 8154 440 513 -1681 C
ATOM 324 CG LEU A 81 -7.663 4.396 105.867 1.00 94.43 C
ANISOU 324 CG LEU A 81 14348 12976 8557 193 384 -1675 C
ATOM 325 CD1 LEU A 81 -7.793 3.497 107.094 1.00 98.23 C
ANISOU 325 CD1 LEU A 81 14841 13575 8907 -33 322 -1686 C
ATOM 326 CD2 LEU A 81 -6.405 4.061 105.081 1.00 86.27 C
ANISOU 326 CD2 LEU A 81 13275 11771 7734 86 238 -1576 C
ATOM 327 N SER A 82 -10.300 7.071 105.713 1.00 90.73 N
ANISOU 327 N SER A 82 14044 12671 7759 961 878 -1889 N
ATOM 328 CA SER A 82 -10.322 8.345 106.416 1.00 93.54 C
ANISOU 328 CA SER A 82 14701 12833 8008 1066 1007 -1981 C
ATOM 329 C SER A 82 -11.584 8.504 107.255 1.00 96.42 C
ANISOU 329 C SER A 82 15049 13435 8151 1190 1141 -2084 C
ATOM 330 O SER A 82 -11.549 9.170 108.292 1.00 99.97 O
ANISOU 330 O SER A 82 15738 13759 8487 1142 1208 -2174 O
ATOM 331 CB SER A 82 -10.175 9.499 105.428 1.00104.36 C
ANISOU 331 CB SER A 82 16224 13990 9438 1363 1133 -1958 C
ATOM 332 OG SER A 82 -8.874 9.530 104.869 1.00110.90 O
ANISOU 332 OG SER A 82 17131 14545 10460 1200 1033 -1891 O
ATOM 333 N ILE A 83 -12.696 7.884 106.848 1.00100.49 N
ANISOU 333 N ILE A 83 15275 14310 8598 1329 1187 -2090 N
ATOM 334 CA ILE A 83 -13.879 7.886 107.707 1.00100.16 C
ANISOU 334 CA ILE A 83 15177 14535 8344 1398 1310 -2202 C
ATOM 335 C ILE A 83 -13.593 7.138 109.002 1.00 96.28 C
ANISOU 335 C ILE A 83 14747 14040 7792 1027 1228 -2231 C
ATOM 336 O ILE A 83 -13.943 7.596 110.100 1.00 95.76 O
ANISOU 336 O ILE A 83 14848 13968 7568 1009 1314 -2326 O
ATOM 337 CB ILE A 83 -15.085 7.277 106.966 1.00 97.94 C
ANISOU 337 CB ILE A 83 14527 14685 8002 1578 1370 -2227 C
ATOM 338 CG1 ILE A 83 -15.600 8.241 105.899 1.00 98.39 C
ANISOU 338 CG1 ILE A 83 14555 14796 8033 2040 1486 -2221 C
ATOM 339 CG2 ILE A 83 -16.196 6.916 107.946 1.00 87.39 C
ANISOU 339 CG2 ILE A 83 13076 13661 6465 1523 1474 -2352 C
ATOM 340 CD1 ILE A 83 -16.754 7.689 105.094 1.00 95.46 C
ANISOU 340 CD1 ILE A 83 13786 14897 7586 2238 1529 -2264 C
ATOM 341 N ALA A 84 -12.934 5.982 108.895 1.00 96.42 N
ANISOU 341 N ALA A 84 14654 14055 7925 741 1066 -2145 N
ATOM 342 CA ALA A 84 -12.606 5.218 110.095 1.00 99.01 C
ANISOU 342 CA ALA A 84 15067 14372 8179 418 987 -2149 C
ATOM 343 C ALA A 84 -11.618 5.976 110.974 1.00102.44 C
ANISOU 343 C ALA A 84 15820 14507 8595 306 923 -2174 C
ATOM 344 O ALA A 84 -11.751 5.993 112.204 1.00108.02 O
ANISOU 344 O ALA A 84 16672 15230 9143 177 944 -2241 O
ATOM 345 CB ALA A 84 -12.045 3.850 109.709 1.00 97.18 C
ANISOU 345 CB ALA A 84 14681 14170 8072 180 839 -2035 C
ATOM 346 N ASP A 85 -10.636 6.637 110.358 1.00 99.74 N
ANISOU 346 N ASP A 85 15592 13902 8405 345 859 -2135 N
ATOM 347 CA ASP A 85 -9.672 7.411 111.132 1.00101.29 C
ANISOU 347 CA ASP A 85 16073 13830 8583 213 812 -2193 C
ATOM 348 C ASP A 85 -10.306 8.639 111.775 1.00 93.89 C
ANISOU 348 C ASP A 85 15357 12832 7485 380 1003 -2329 C
ATOM 349 O ASP A 85 -9.883 9.052 112.857 1.00 91.53 O
ANISOU 349 O ASP A 85 15279 12417 7082 223 990 -2417 O
ATOM 350 CB ASP A 85 -8.489 7.811 110.253 1.00107.79 C
ANISOU 350 CB ASP A 85 16948 14397 9610 190 726 -2140 C
ATOM 351 CG ASP A 85 -7.438 6.720 110.164 1.00110.93 C
ANISOU 351 CG ASP A 85 17230 14788 10131 -66 500 -2039 C
ATOM 352 OD1 ASP A 85 -7.267 5.980 111.157 1.00112.45 O
ANISOU 352 OD1 ASP A 85 17434 15073 10220 -267 397 -2036 O
ATOM 353 OD2 ASP A 85 -6.787 6.601 109.103 1.00108.24 O
ANISOU 353 OD2 ASP A 85 16797 14350 9979 -49 433 -1958 O
ATOM 354 N LEU A 86 -11.324 9.226 111.144 1.00 89.34 N
ANISOU 354 N LEU A 86 14728 12347 6869 709 1183 -2352 N
ATOM 355 CA LEU A 86 -12.015 10.350 111.770 1.00 93.79 C
ANISOU 355 CA LEU A 86 15506 12866 7263 904 1384 -2475 C
ATOM 356 C LEU A 86 -12.874 9.886 112.939 1.00 95.92 C
ANISOU 356 C LEU A 86 15733 13382 7330 820 1428 -2553 C
ATOM 357 O LEU A 86 -12.962 10.577 113.963 1.00 97.08 O
ANISOU 357 O LEU A 86 16118 13436 7330 793 1517 -2665 O
ATOM 358 CB LEU A 86 -12.867 11.088 110.738 1.00 99.78 C
ANISOU 358 CB LEU A 86 16217 13678 8017 1333 1563 -2466 C
ATOM 359 CG LEU A 86 -13.335 12.482 111.160 1.00110.04 C
ANISOU 359 CG LEU A 86 17817 14822 9173 1592 1791 -2574 C
ATOM 360 CD1 LEU A 86 -12.170 13.462 111.140 1.00113.11 C
ANISOU 360 CD1 LEU A 86 18558 14767 9652 1500 1818 -2598 C
ATOM 361 CD2 LEU A 86 -14.472 12.968 110.275 1.00108.11 C
ANISOU 361 CD2 LEU A 86 17460 14759 8858 2070 1965 -2558 C
ATOM 362 N VAL A 87 -13.512 8.718 112.809 1.00100.28 N
ANISOU 362 N VAL A 87 15994 14243 7865 759 1385 -2507 N
ATOM 363 CA VAL A 87 -14.246 8.154 113.940 1.00113.81 C
ANISOU 363 CA VAL A 87 17677 16178 9390 624 1434 -2577 C
ATOM 364 C VAL A 87 -13.288 7.845 115.083 1.00118.52 C
ANISOU 364 C VAL A 87 18481 16614 9938 292 1296 -2576 C
ATOM 365 O VAL A 87 -13.602 8.066 116.263 1.00 92.96 O
ANISOU 365 O VAL A 87 15400 13406 6513 219 1364 -2670 O
ATOM 366 CB VAL A 87 -15.026 6.900 113.496 1.00 90.36 C
ANISOU 366 CB VAL A 87 14363 13545 6423 577 1433 -2535 C
ATOM 367 CG1 VAL A 87 -15.454 6.066 114.700 1.00105.25 C
ANISOU 367 CG1 VAL A 87 16255 15595 8140 328 1457 -2579 C
ATOM 368 CG2 VAL A 87 -16.234 7.295 112.660 1.00 91.30 C
ANISOU 368 CG2 VAL A 87 14260 13927 6503 926 1597 -2592 C
ATOM 369 N VAL A 88 -12.080 7.420 114.754 1.00109.91 N
ANISOU 369 N VAL A 88 17395 15362 9004 106 1098 -2476 N
ATOM 370 CA VAL A 88 -11.115 7.099 115.840 1.00108.60 C
ANISOU 370 CA VAL A 88 17413 15066 8785 -174 944 -2478 C
ATOM 371 C VAL A 88 -10.732 8.385 116.547 1.00103.42 C
ANISOU 371 C VAL A 88 17050 14198 8047 -157 1006 -2613 C
ATOM 372 O VAL A 88 -10.717 8.385 117.746 1.00 96.57 O
ANISOU 372 O VAL A 88 16353 13342 6998 -293 1006 -2698 O
ATOM 373 CB VAL A 88 -9.841 6.428 115.312 1.00108.81 C
ANISOU 373 CB VAL A 88 17360 14983 9001 -331 724 -2352 C
ATOM 374 CG1 VAL A 88 -8.659 6.759 116.196 1.00102.42 C
ANISOU 374 CG1 VAL A 88 16742 14042 8129 -565 560 -2382 C
ATOM 375 CG2 VAL A 88 -10.006 4.927 115.209 1.00109.56 C
ANISOU 375 CG2 VAL A 88 17224 15270 9134 -407 669 -2229 C
ATOM 376 N ALA A 89 -10.426 9.443 115.815 1.00109.85 N
ANISOU 376 N ALA A 89 17945 14810 8982 12 1083 -2642 N
ATOM 377 CA ALA A 89 -9.995 10.670 116.507 1.00110.25 C
ANISOU 377 CA ALA A 89 18306 14618 8968 9 1176 -2783 C
ATOM 378 C ALA A 89 -11.134 11.194 117.372 1.00108.14 C
ANISOU 378 C ALA A 89 18177 14442 8470 116 1363 -2906 C
ATOM 379 O ALA A 89 -10.903 11.525 118.535 1.00104.94 O
ANISOU 379 O ALA A 89 17975 13981 7916 -62 1349 -3016 O
ATOM 380 CB ALA A 89 -9.597 11.684 115.476 1.00109.72 C
ANISOU 380 CB ALA A 89 18322 14312 9054 218 1291 -2781 C
ATOM 381 N VAL A 90 -12.341 11.188 116.832 1.00112.90 N
ANISOU 381 N VAL A 90 18641 15231 9026 397 1527 -2894 N
ATOM 382 CA VAL A 90 -13.475 11.749 117.603 1.00111.33 C
ANISOU 382 CA VAL A 90 18530 15165 8606 525 1715 -3010 C
ATOM 383 C VAL A 90 -13.662 10.948 118.874 1.00 98.84 C
ANISOU 383 C VAL A 90 16958 13730 6866 235 1619 -3035 C
ATOM 384 O VAL A 90 -13.602 11.525 119.925 1.00100.31 O
ANISOU 384 O VAL A 90 17398 13787 6930 74 1607 -3138 O
ATOM 385 CB VAL A 90 -14.771 11.711 116.792 1.00105.40 C
ANISOU 385 CB VAL A 90 17531 14690 7828 852 1869 -2987 C
ATOM 386 CG1 VAL A 90 -15.968 11.805 117.707 1.00101.11 C
ANISOU 386 CG1 VAL A 90 17043 14326 7047 965 2059 -3114 C
ATOM 387 CG2 VAL A 90 -14.809 12.815 115.761 1.00 98.84 C
ANISOU 387 CG2 VAL A 90 16731 13711 7112 1191 1977 -2957 C
ATOM 388 N PHE A 91 -13.795 9.643 118.760 1.00108.46 N
ANISOU 388 N PHE A 91 17919 15205 8087 148 1547 -2940 N
ATOM 389 CA PHE A 91 -14.163 8.882 119.946 1.00 98.39 C
ANISOU 389 CA PHE A 91 16659 14107 6616 -49 1541 -2966 C
ATOM 390 C PHE A 91 -12.972 8.403 120.762 1.00114.24 C
ANISOU 390 C PHE A 91 18820 15999 8585 -359 1329 -2930 C
ATOM 391 O PHE A 91 -13.177 7.832 121.839 1.00114.25 O
ANISOU 391 O PHE A 91 18891 16119 8397 -516 1322 -2945 O
ATOM 392 CB PHE A 91 -15.044 7.695 119.554 1.00 97.47 C
ANISOU 392 CB PHE A 91 16241 14290 6504 -54 1577 -2891 C
ATOM 393 CG PHE A 91 -16.442 8.089 119.171 1.00 98.66 C
ANISOU 393 CG PHE A 91 16225 14670 6592 228 1804 -2976 C
ATOM 394 CD1 PHE A 91 -16.761 8.374 117.854 1.00111.22 C
ANISOU 394 CD1 PHE A 91 17617 16312 8330 490 1844 -2943 C
ATOM 395 CD2 PHE A 91 -17.434 8.189 120.132 1.00100.82 C
ANISOU 395 CD2 PHE A 91 16535 15130 6644 246 1978 -3094 C
ATOM 396 CE1 PHE A 91 -18.047 8.743 117.500 1.00109.97 C
ANISOU 396 CE1 PHE A 91 17283 16413 8089 785 2041 -3028 C
ATOM 397 CE2 PHE A 91 -18.721 8.559 119.786 1.00103.93 C
ANISOU 397 CE2 PHE A 91 16746 15776 6967 524 2185 -3186 C
ATOM 398 CZ PHE A 91 -19.027 8.837 118.468 1.00114.21 C
ANISOU 398 CZ PHE A 91 17834 17152 8407 804 2210 -3154 C
ATOM 399 N GLN A 92 -11.742 8.608 120.298 1.00108.69 N
ANISOU 399 N GLN A 92 18168 15090 8040 -442 1160 -2887 N
ATOM 400 CA GLN A 92 -10.567 8.306 121.097 1.00105.16 C
ANISOU 400 CA GLN A 92 17857 14566 7533 -703 953 -2882 C
ATOM 401 C GLN A 92 -9.847 9.559 121.568 1.00101.80 C
ANISOU 401 C GLN A 92 17689 13925 7066 -756 960 -3041 C
ATOM 402 O GLN A 92 -9.562 9.687 122.761 1.00101.56 O
ANISOU 402 O GLN A 92 17839 13912 6838 -912 917 -3137 O
ATOM 403 CB GLN A 92 -9.607 7.408 120.297 1.00111.81 C
ANISOU 403 CB GLN A 92 18530 15384 8570 -804 735 -2724 C
ATOM 404 CG GLN A 92 -8.120 7.642 120.552 1.00118.99 C
ANISOU 404 CG GLN A 92 19548 16147 9516 -986 523 -2751 C
ATOM 405 CD GLN A 92 -7.669 7.222 121.939 1.00123.09 C
ANISOU 405 CD GLN A 92 20210 16761 9798 -1179 396 -2783 C
ATOM 406 OE1 GLN A 92 -8.379 6.514 122.653 1.00127.27 O
ANISOU 406 OE1 GLN A 92 20756 17450 10152 -1196 446 -2740 O
ATOM 407 NE2 GLN A 92 -6.476 7.661 122.326 1.00122.72 N
ANISOU 407 NE2 GLN A 92 20266 16631 9731 -1329 236 -2869 N
ATOM 408 N VAL A 93 -9.533 10.492 120.668 1.00103.44 N
ANISOU 408 N VAL A 93 17934 13924 7443 -639 1025 -3081 N
ATOM 409 CA VAL A 93 -8.767 11.659 121.072 1.00107.30 C
ANISOU 409 CA VAL A 93 18685 14182 7903 -736 1053 -3248 C
ATOM 410 C VAL A 93 -9.621 12.598 121.916 1.00114.29 C
ANISOU 410 C VAL A 93 19805 15034 8585 -634 1286 -3411 C
ATOM 411 O VAL A 93 -9.175 13.074 122.967 1.00116.24 O
ANISOU 411 O VAL A 93 20270 15225 8672 -813 1272 -3563 O
ATOM 412 CB VAL A 93 -8.194 12.370 119.834 1.00104.28 C
ANISOU 412 CB VAL A 93 18309 13556 7758 -649 1092 -3239 C
ATOM 413 CG1 VAL A 93 -7.645 13.728 120.216 1.00110.04 C
ANISOU 413 CG1 VAL A 93 19350 14017 8443 -731 1213 -3442 C
ATOM 414 CG2 VAL A 93 -7.112 11.516 119.191 1.00 99.44 C
ANISOU 414 CG2 VAL A 93 17495 12962 7325 -806 841 -3113 C
ATOM 415 N LEU A 94 -10.848 12.904 121.468 1.00117.21 N
ANISOU 415 N LEU A 94 20131 15454 8948 -337 1506 -3395 N
ATOM 416 CA LEU A 94 -11.660 13.851 122.230 1.00122.17 C
ANISOU 416 CA LEU A 94 20990 16044 9385 -207 1744 -3552 C
ATOM 417 C LEU A 94 -11.955 13.364 123.646 1.00121.96 C
ANISOU 417 C LEU A 94 21024 16207 9109 -380 1709 -3616 C
ATOM 418 O LEU A 94 -11.700 14.122 124.599 1.00128.54 O
ANISOU 418 O LEU A 94 22128 16926 9785 -490 1770 -3783 O
ATOM 419 CB LEU A 94 -12.942 14.166 121.446 1.00123.75 C
ANISOU 419 CB LEU A 94 21084 16324 9612 181 1969 -3513 C
ATOM 420 CG LEU A 94 -13.834 15.310 121.929 1.00118.90 C
ANISOU 420 CG LEU A 94 20707 15640 8831 421 2255 -3661 C
ATOM 421 CD1 LEU A 94 -13.088 16.633 121.875 1.00114.94 C
ANISOU 421 CD1 LEU A 94 20560 14748 8365 414 2368 -3785 C
ATOM 422 CD2 LEU A 94 -15.107 15.375 121.098 1.00117.21 C
ANISOU 422 CD2 LEU A 94 20300 15603 8631 828 2431 -3599 C
ATOM 423 N PRO A 95 -12.459 12.141 123.868 1.00118.21 N
ANISOU 423 N PRO A 95 20333 16005 8575 -427 1629 -3501 N
ATOM 424 CA PRO A 95 -12.617 11.666 125.254 1.00119.95 C
ANISOU 424 CA PRO A 95 20654 16378 8543 -610 1597 -3552 C
ATOM 425 C PRO A 95 -11.321 11.596 126.041 1.00118.71 C
ANISOU 425 C PRO A 95 20652 16143 8309 -901 1378 -3600 C
ATOM 426 O PRO A 95 -11.331 11.879 127.243 1.00125.87 O
ANISOU 426 O PRO A 95 21763 17079 8982 -1016 1404 -3726 O
ATOM 427 CB PRO A 95 -13.232 10.274 125.074 1.00116.06 C
ANISOU 427 CB PRO A 95 19898 16148 8052 -623 1552 -3393 C
ATOM 428 CG PRO A 95 -13.920 10.336 123.764 1.00112.11 C
ANISOU 428 CG PRO A 95 19169 15686 7741 -369 1662 -3327 C
ATOM 429 CD PRO A 95 -13.024 11.173 122.913 1.00111.88 C
ANISOU 429 CD PRO A 95 19213 15389 7909 -311 1605 -3335 C
ATOM 430 N GLN A 96 -10.194 11.248 125.407 1.00106.50 N
ANISOU 430 N GLN A 96 19007 14519 6938 -1018 1161 -3515 N
ATOM 431 CA GLN A 96 -8.935 11.205 126.148 1.00107.41 C
ANISOU 431 CA GLN A 96 19235 14612 6963 -1280 941 -3581 C
ATOM 432 C GLN A 96 -8.470 12.602 126.526 1.00133.91 C
ANISOU 432 C GLN A 96 22850 17759 10269 -1352 1035 -3816 C
ATOM 433 O GLN A 96 -7.946 12.810 127.626 1.00141.76 O
ANISOU 433 O GLN A 96 24008 18794 11058 -1547 956 -3955 O
ATOM 434 CB GLN A 96 -7.863 10.481 125.336 1.00105.25 C
ANISOU 434 CB GLN A 96 18766 14332 6891 -1369 695 -3439 C
ATOM 435 CG GLN A 96 -7.672 9.022 125.723 1.00104.97 C
ANISOU 435 CG GLN A 96 18603 14512 6769 -1456 500 -3265 C
ATOM 436 CD GLN A 96 -6.909 8.860 127.023 1.00106.43 C
ANISOU 436 CD GLN A 96 18938 14803 6697 -1652 328 -3342 C
ATOM 437 OE1 GLN A 96 -6.246 9.790 127.484 1.00124.73 O
ANISOU 437 OE1 GLN A 96 21403 17042 8948 -1770 298 -3534 O
ATOM 438 NE2 GLN A 96 -6.994 7.676 127.620 1.00115.77 N
ANISOU 438 NE2 GLN A 96 20095 16169 7724 -1687 223 -3198 N
ATOM 439 N LEU A 97 -8.672 13.575 125.635 1.00121.83 N
ANISOU 439 N LEU A 97 21378 16004 8908 -1194 1220 -3869 N
ATOM 440 CA LEU A 97 -8.357 14.956 125.979 1.00122.74 C
ANISOU 440 CA LEU A 97 21789 15878 8968 -1255 1375 -4102 C
ATOM 441 C LEU A 97 -9.237 15.441 127.124 1.00126.29 C
ANISOU 441 C LEU A 97 22456 16375 9153 -1210 1563 -4242 C
ATOM 442 O LEU A 97 -8.772 16.152 128.024 1.00130.06 O
ANISOU 442 O LEU A 97 23176 16772 9471 -1395 1589 -4451 O
ATOM 443 CB LEU A 97 -8.536 15.843 124.745 1.00124.48 C
ANISOU 443 CB LEU A 97 22059 15830 9407 -1041 1576 -4097 C
ATOM 444 CG LEU A 97 -7.938 17.247 124.729 1.00130.78 C
ANISOU 444 CG LEU A 97 23170 16296 10226 -1128 1744 -4313 C
ATOM 445 CD1 LEU A 97 -6.439 17.191 124.960 1.00130.51 C
ANISOU 445 CD1 LEU A 97 23129 16235 10225 -1497 1519 -4418 C
ATOM 446 CD2 LEU A 97 -8.251 17.920 123.401 1.00131.43 C
ANISOU 446 CD2 LEU A 97 23292 16129 10516 -851 1951 -4244 C
ATOM 447 N LEU A 98 -10.511 15.040 127.123 1.00132.21 N
ANISOU 447 N LEU A 98 23109 17279 9843 -980 1697 -4145 N
ATOM 448 CA LEU A 98 -11.396 15.446 128.208 1.00132.22 C
ANISOU 448 CA LEU A 98 23298 17348 9590 -927 1884 -4275 C
ATOM 449 C LEU A 98 -11.014 14.767 129.519 1.00128.88 C
ANISOU 449 C LEU A 98 22921 17123 8925 -1189 1707 -4310 C
ATOM 450 O LEU A 98 -11.125 15.370 130.593 1.00120.24 O
ANISOU 450 O LEU A 98 21973 16019 7696 -1245 1773 -4444 O
ATOM 451 CB LEU A 98 -12.852 15.154 127.846 1.00129.33 C
ANISOU 451 CB LEU A 98 22778 17141 9220 -622 2074 -4175 C
ATOM 452 CG LEU A 98 -13.427 15.882 126.626 1.00115.61 C
ANISOU 452 CG LEU A 98 21004 15258 7665 -286 2275 -4145 C
ATOM 453 CD1 LEU A 98 -14.948 15.894 126.679 1.00116.47 C
ANISOU 453 CD1 LEU A 98 21025 15562 7667 15 2506 -4140 C
ATOM 454 CD2 LEU A 98 -12.880 17.298 126.488 1.00117.48 C
ANISOU 454 CD2 LEU A 98 21563 15135 7939 -265 2423 -4306 C
ATOM 455 N TRP A 99 -10.565 13.512 129.455 1.00127.50 N
ANISOU 455 N TRP A 99 22534 17133 8778 -1305 1458 -4137 N
ATOM 456 CA TRP A 99 -10.133 12.835 130.675 1.00140.93 C
ANISOU 456 CA TRP A 99 24294 19021 10234 -1519 1280 -4147 C
ATOM 457 C TRP A 99 -8.864 13.463 131.230 1.00152.89 C
ANISOU 457 C TRP A 99 25914 20452 11724 -1738 1116 -4301 C
ATOM 458 O TRP A 99 -8.698 13.574 132.452 1.00164.30 O
ANISOU 458 O TRP A 99 27436 21996 12993 -1843 1059 -4383 O
ATOM 459 CB TRP A 99 -9.914 11.345 130.419 1.00141.95 C
ANISOU 459 CB TRP A 99 24193 19338 10403 -1558 1069 -3908 C
ATOM 460 CG TRP A 99 -9.528 10.583 131.656 1.00149.90 C
ANISOU 460 CG TRP A 99 25274 20537 11144 -1721 899 -3881 C
ATOM 461 CD1 TRP A 99 -10.371 9.953 132.528 1.00146.62 C
ANISOU 461 CD1 TRP A 99 24865 20286 10556 -1684 979 -3806 C
ATOM 462 CD2 TRP A 99 -8.201 10.380 132.164 1.00156.56 C
ANISOU 462 CD2 TRP A 99 26129 21440 11918 -1902 615 -3900 C
ATOM 463 NE1 TRP A 99 -9.652 9.364 133.540 1.00146.60 N
ANISOU 463 NE1 TRP A 99 24908 20419 10375 -1812 768 -3762 N
ATOM 464 CE2 TRP A 99 -8.319 9.613 133.342 1.00153.14 C
ANISOU 464 CE2 TRP A 99 25726 21204 11256 -1934 534 -3820 C
ATOM 465 CE3 TRP A 99 -6.926 10.768 131.736 1.00160.39 C
ANISOU 465 CE3 TRP A 99 26588 21847 12507 -2034 428 -3984 C
ATOM 466 CZ2 TRP A 99 -7.212 9.226 134.097 1.00155.82 C
ANISOU 466 CZ2 TRP A 99 26073 21681 11452 -2057 262 -3813 C
ATOM 467 CZ3 TRP A 99 -5.827 10.384 132.489 1.00163.21 C
ANISOU 467 CZ3 TRP A 99 26917 22364 12732 -2179 153 -3994 C
ATOM 468 CH2 TRP A 99 -5.979 9.621 133.656 1.00159.41 C
ANISOU 468 CH2 TRP A 99 26469 22093 12007 -2171 67 -3905 C
ATOM 469 N ASP A 100 -7.955 13.882 130.347 1.00150.60 N
ANISOU 469 N ASP A 100 25619 19995 11608 -1816 1046 -4353 N
ATOM 470 CA ASP A 100 -6.771 14.596 130.809 1.00154.24 C
ANISOU 470 CA ASP A 100 26156 20383 12066 -2043 926 -4538 C
ATOM 471 C ASP A 100 -7.126 15.975 131.346 1.00158.55 C
ANISOU 471 C ASP A 100 26916 20736 12588 -2025 1171 -4749 C
ATOM 472 O ASP A 100 -6.398 16.516 132.186 1.00163.98 O
ANISOU 472 O ASP A 100 27678 21432 13194 -2223 1096 -4923 O
ATOM 473 CB ASP A 100 -5.744 14.695 129.683 1.00153.05 C
ANISOU 473 CB ASP A 100 25929 20099 12123 -2143 816 -4547 C
ATOM 474 CG ASP A 100 -4.958 13.411 129.507 1.00150.64 C
ANISOU 474 CG ASP A 100 25361 20017 11860 -2215 489 -4357 C
ATOM 475 OD1 ASP A 100 -4.315 12.968 130.481 1.00151.23 O
ANISOU 475 OD1 ASP A 100 25443 20305 11710 -2380 277 -4406 O
ATOM 476 OD2 ASP A 100 -4.993 12.834 128.402 1.00148.84 O
ANISOU 476 OD2 ASP A 100 24923 19756 11873 -2089 447 -4158 O
ATOM 477 N ILE A 101 -8.236 16.555 130.887 1.00156.71 N
ANISOU 477 N ILE A 101 26778 20346 12417 -1779 1464 -4740 N
ATOM 478 CA ILE A 101 -8.705 17.823 131.434 1.00153.39 C
ANISOU 478 CA ILE A 101 26577 19743 11961 -1718 1718 -4917 C
ATOM 479 C ILE A 101 -9.394 17.562 132.767 1.00151.32 C
ANISOU 479 C ILE A 101 26335 19691 11469 -1704 1730 -4930 C
ATOM 480 O ILE A 101 -8.912 17.990 133.822 1.00151.88 O
ANISOU 480 O ILE A 101 26505 19787 11413 -1884 1675 -5082 O
ATOM 481 CB ILE A 101 -9.639 18.553 130.452 1.00147.43 C
ANISOU 481 CB ILE A 101 25912 18759 11346 -1407 2026 -4889 C
ATOM 482 CG1 ILE A 101 -8.839 19.096 129.263 1.00144.79 C
ANISOU 482 CG1 ILE A 101 25631 18151 11234 -1441 2053 -4915 C
ATOM 483 CG2 ILE A 101 -10.374 19.687 131.155 1.00150.51 C
ANISOU 483 CG2 ILE A 101 26515 19011 11660 -1284 2297 -5030 C
ATOM 484 CD1 ILE A 101 -9.660 19.908 128.286 1.00146.11 C
ANISOU 484 CD1 ILE A 101 25915 18069 11531 -1102 2360 -4880 C
ATOM 485 N THR A 102 -10.520 16.855 132.737 1.00151.52 N
ANISOU 485 N THR A 102 26259 19878 11433 -1501 1808 -4780 N
ATOM 486 CA THR A 102 -11.217 16.448 133.949 1.00159.26 C
ANISOU 486 CA THR A 102 27240 21074 12198 -1491 1824 -4769 C
ATOM 487 C THR A 102 -11.144 14.932 134.067 1.00157.19 C
ANISOU 487 C THR A 102 26790 21078 11855 -1554 1608 -4571 C
ATOM 488 O THR A 102 -11.618 14.207 133.185 1.00154.33 O
ANISOU 488 O THR A 102 26280 20775 11585 -1433 1629 -4414 O
ATOM 489 CB THR A 102 -12.668 16.931 133.951 1.00165.38 C
ANISOU 489 CB THR A 102 28053 21831 12954 -1211 2132 -4780 C
ATOM 490 OG1 THR A 102 -13.381 16.288 135.013 1.00169.16 O
ANISOU 490 OG1 THR A 102 28487 22553 13232 -1211 2137 -4737 O
ATOM 491 CG2 THR A 102 -13.350 16.640 132.618 1.00164.79 C
ANISOU 491 CG2 THR A 102 27832 21745 13035 -967 2244 -4646 C
ATOM 492 N PHE A 103 -10.536 14.459 135.154 1.00150.75 N
ANISOU 492 N PHE A 103 25992 20425 10862 -1734 1409 -4580 N
ATOM 493 CA PHE A 103 -10.311 13.030 135.323 1.00133.12 C
ANISOU 493 CA PHE A 103 23623 18417 8541 -1791 1199 -4382 C
ATOM 494 C PHE A 103 -11.605 12.260 135.554 1.00138.49 C
ANISOU 494 C PHE A 103 24242 19244 9135 -1651 1355 -4245 C
ATOM 495 O PHE A 103 -11.633 11.045 135.330 1.00147.18 O
ANISOU 495 O PHE A 103 25224 20478 10218 -1663 1254 -4055 O
ATOM 496 CB PHE A 103 -9.318 12.803 136.463 1.00128.71 C
ANISOU 496 CB PHE A 103 23113 18001 7791 -1976 956 -4432 C
ATOM 497 CG PHE A 103 -7.974 13.441 136.225 1.00128.35 C
ANISOU 497 CG PHE A 103 23072 17866 7828 -2145 782 -4578 C
ATOM 498 CD1 PHE A 103 -6.917 12.697 135.727 1.00134.18 C
ANISOU 498 CD1 PHE A 103 23672 18693 8620 -2237 512 -4480 C
ATOM 499 CD2 PHE A 103 -7.772 14.789 136.488 1.00132.58 C
ANISOU 499 CD2 PHE A 103 23749 18232 8393 -2216 905 -4821 C
ATOM 500 CE1 PHE A 103 -5.683 13.281 135.503 1.00138.09 C
ANISOU 500 CE1 PHE A 103 24138 19135 9195 -2406 359 -4633 C
ATOM 501 CE2 PHE A 103 -6.542 15.380 136.265 1.00134.99 C
ANISOU 501 CE2 PHE A 103 24047 18461 8783 -2404 770 -4976 C
ATOM 502 CZ PHE A 103 -5.495 14.624 135.773 1.00138.12 C
ANISOU 502 CZ PHE A 103 24274 18973 9232 -2502 493 -4888 C
ATOM 503 N ARG A 104 -12.664 12.928 136.004 1.00134.32 N
ANISOU 503 N ARG A 104 23788 18697 8550 -1527 1608 -4342 N
ATOM 504 CA ARG A 104 -13.980 12.306 136.057 1.00136.17 C
ANISOU 504 CA ARG A 104 23925 19078 8734 -1388 1793 -4241 C
ATOM 505 C ARG A 104 -14.491 12.035 134.645 1.00142.92 C
ANISOU 505 C ARG A 104 24607 19911 9785 -1241 1888 -4149 C
ATOM 506 O ARG A 104 -14.280 12.834 133.728 1.00134.88 O
ANISOU 506 O ARG A 104 23602 18716 8931 -1151 1939 -4217 O
ATOM 507 CB ARG A 104 -14.959 13.205 136.812 1.00135.69 C
ANISOU 507 CB ARG A 104 23969 19011 8576 -1270 2042 -4390 C
ATOM 508 CG ARG A 104 -14.451 13.665 138.168 1.00148.22 C
ANISOU 508 CG ARG A 104 25741 20601 9975 -1409 1967 -4515 C
ATOM 509 CD ARG A 104 -15.293 14.797 138.729 1.00158.50 C
ANISOU 509 CD ARG A 104 27169 21835 11221 -1285 2223 -4689 C
ATOM 510 NE ARG A 104 -16.667 14.390 139.008 1.00166.18 N
ANISOU 510 NE ARG A 104 28051 22975 12113 -1137 2430 -4635 N
ATOM 511 CZ ARG A 104 -17.581 15.188 139.548 1.00174.23 C
ANISOU 511 CZ ARG A 104 29145 23994 13062 -1001 2663 -4763 C
ATOM 512 NH1 ARG A 104 -18.810 14.742 139.771 1.00180.04 N
ANISOU 512 NH1 ARG A 104 29763 24918 13726 -878 2842 -4718 N
ATOM 513 NH2 ARG A 104 -17.264 16.435 139.867 1.00174.21 N
ANISOU 513 NH2 ARG A 104 29331 23802 13058 -996 2726 -4942 N
ATOM 514 N PHE A 105 -15.154 10.889 134.465 1.00145.21 N
ANISOU 514 N PHE A 105 24741 20379 10053 -1223 1921 -3995 N
ATOM 515 CA PHE A 105 -15.664 10.541 133.141 1.00120.21 C
ANISOU 515 CA PHE A 105 21382 17237 7057 -1097 2007 -3915 C
ATOM 516 C PHE A 105 -16.799 11.461 132.709 1.00135.27 C
ANISOU 516 C PHE A 105 23236 19141 9020 -840 2285 -4029 C
ATOM 517 O PHE A 105 -16.896 11.817 131.528 1.00139.69 O
ANISOU 517 O PHE A 105 23711 19625 9740 -684 2343 -4030 O
ATOM 518 CB PHE A 105 -16.133 9.090 133.120 1.00119.18 C
ANISOU 518 CB PHE A 105 21096 17304 6881 -1169 2001 -3744 C
ATOM 519 CG PHE A 105 -16.893 8.722 131.885 1.00130.00 C
ANISOU 519 CG PHE A 105 22235 18760 8398 -1044 2132 -3693 C
ATOM 520 CD1 PHE A 105 -16.273 8.739 130.648 1.00114.82 C
ANISOU 520 CD1 PHE A 105 20240 16731 6656 -1016 2028 -3646 C
ATOM 521 CD2 PHE A 105 -18.227 8.362 131.958 1.00125.92 C
ANISOU 521 CD2 PHE A 105 21556 18451 7837 -958 2361 -3704 C
ATOM 522 CE1 PHE A 105 -16.968 8.407 129.507 1.00113.21 C
ANISOU 522 CE1 PHE A 105 19746 16623 6646 -868 2118 -3577 C
ATOM 523 CE2 PHE A 105 -18.926 8.027 130.818 1.00120.32 C
ANISOU 523 CE2 PHE A 105 20595 17867 7254 -847 2476 -3679 C
ATOM 524 CZ PHE A 105 -18.294 8.051 129.592 1.00114.11 C
ANISOU 524 CZ PHE A 105 19711 16973 6673 -797 2351 -3614 C
ATOM 525 N TYR A 106 -17.659 11.862 133.648 1.00131.89 N
ANISOU 525 N TYR A 106 22859 18801 8453 -768 2458 -4123 N
ATOM 526 CA TYR A 106 -18.818 12.713 133.374 1.00137.08 C
ANISOU 526 CA TYR A 106 23456 19498 9131 -491 2727 -4233 C
ATOM 527 C TYR A 106 -19.708 12.109 132.280 1.00146.02 C
ANISOU 527 C TYR A 106 24301 20820 10358 -332 2841 -4158 C
ATOM 528 O TYR A 106 -19.795 12.617 131.159 1.00147.83 O
ANISOU 528 O TYR A 106 24460 20980 10728 -130 2900 -4171 O
ATOM 529 CB TYR A 106 -18.381 14.127 132.979 1.00137.04 C
ANISOU 529 CB TYR A 106 23624 19221 9224 -353 2778 -4357 C
ATOM 530 CG TYR A 106 -18.043 15.035 134.133 1.00136.85 C
ANISOU 530 CG TYR A 106 23853 19059 9086 -433 2796 -4500 C
ATOM 531 CD1 TYR A 106 -19.046 15.585 134.923 1.00136.22 C
ANISOU 531 CD1 TYR A 106 23812 19064 8882 -295 3007 -4605 C
ATOM 532 CD2 TYR A 106 -16.725 15.365 134.418 1.00136.93 C
ANISOU 532 CD2 TYR A 106 24047 18870 9109 -649 2606 -4546 C
ATOM 533 CE1 TYR A 106 -18.745 16.424 135.971 1.00139.60 C
ANISOU 533 CE1 TYR A 106 24476 19362 9202 -375 3031 -4743 C
ATOM 534 CE2 TYR A 106 -16.414 16.204 135.465 1.00138.68 C
ANISOU 534 CE2 TYR A 106 24486 18983 9221 -739 2627 -4697 C
ATOM 535 CZ TYR A 106 -17.428 16.731 136.237 1.00140.56 C
ANISOU 535 CZ TYR A 106 24780 19289 9339 -602 2842 -4792 C
ATOM 536 OH TYR A 106 -17.126 17.568 137.281 1.00144.60 O
ANISOU 536 OH TYR A 106 25513 19690 9738 -698 2871 -4949 O
ATOM 537 N GLY A 107 -20.372 11.006 132.630 1.00147.19 N
ANISOU 537 N GLY A 107 24288 21214 10424 -429 2880 -4084 N
ATOM 538 CA GLY A 107 -21.319 10.402 131.719 1.00143.69 C
ANISOU 538 CA GLY A 107 23543 21001 10052 -311 3009 -4046 C
ATOM 539 C GLY A 107 -22.032 9.158 132.220 1.00141.55 C
ANISOU 539 C GLY A 107 23116 20976 9691 -470 3074 -3976 C
ATOM 540 O GLY A 107 -21.612 8.501 133.179 1.00137.55 O
ANISOU 540 O GLY A 107 22751 20436 9074 -699 2981 -3904 O
ATOM 541 N PRO A 108 -23.140 8.819 131.558 1.00144.16 N
ANISOU 541 N PRO A 108 23147 21561 10066 -342 3247 -4000 N
ATOM 542 CA PRO A 108 -23.870 7.586 131.878 1.00148.22 C
ANISOU 542 CA PRO A 108 23488 22299 10530 -517 3339 -3941 C
ATOM 543 C PRO A 108 -23.060 6.335 131.575 1.00150.26 C
ANISOU 543 C PRO A 108 23753 22486 10854 -792 3171 -3773 C
ATOM 544 O PRO A 108 -22.204 6.318 130.689 1.00151.29 O
ANISOU 544 O PRO A 108 23886 22487 11110 -799 3008 -3707 O
ATOM 545 CB PRO A 108 -25.112 7.668 130.985 1.00144.12 C
ANISOU 545 CB PRO A 108 22613 22064 10083 -292 3535 -4025 C
ATOM 546 CG PRO A 108 -25.262 9.116 130.668 1.00139.78 C
ANISOU 546 CG PRO A 108 22116 21459 9537 56 3597 -4146 C
ATOM 547 CD PRO A 108 -23.867 9.652 130.584 1.00140.42 C
ANISOU 547 CD PRO A 108 22486 21196 9670 -5 3392 -4101 C
ATOM 548 N ASP A 109 -23.334 5.280 132.344 1.00154.84 N
ANISOU 548 N ASP A 109 24357 23139 11338 -1013 3224 -3698 N
ATOM 549 CA ASP A 109 -22.596 4.031 132.181 1.00166.82 C
ANISOU 549 CA ASP A 109 25925 24573 12888 -1262 3090 -3526 C
ATOM 550 C ASP A 109 -22.780 3.443 130.786 1.00180.95 C
ANISOU 550 C ASP A 109 27425 26467 14862 -1265 3103 -3492 C
ATOM 551 O ASP A 109 -21.826 2.923 130.191 1.00184.94 O
ANISOU 551 O ASP A 109 27979 26838 15453 -1367 2925 -3370 O
ATOM 552 CB ASP A 109 -23.047 3.030 133.246 1.00168.44 C
ANISOU 552 CB ASP A 109 26217 24836 12945 -1470 3210 -3462 C
ATOM 553 CG ASP A 109 -22.279 1.725 133.193 1.00165.11 C
ANISOU 553 CG ASP A 109 25908 24300 12526 -1702 3096 -3270 C
ATOM 554 OD1 ASP A 109 -21.135 1.719 132.693 1.00161.96 O
ANISOU 554 OD1 ASP A 109 25603 23740 12195 -1707 2864 -3176 O
ATOM 555 OD2 ASP A 109 -22.828 0.698 133.648 1.00166.22 O
ANISOU 555 OD2 ASP A 109 26053 24504 12597 -1876 3252 -3212 O
ATOM 556 N LEU A 110 -24.000 3.512 130.246 1.00185.94 N
ANISOU 556 N LEU A 110 27740 27356 15552 -1149 3306 -3603 N
ATOM 557 CA LEU A 110 -24.215 3.029 128.886 1.00180.39 C
ANISOU 557 CA LEU A 110 26725 26790 15026 -1135 3313 -3593 C
ATOM 558 C LEU A 110 -23.505 3.914 127.871 1.00170.87 C
ANISOU 558 C LEU A 110 25507 25481 13937 -925 3160 -3607 C
ATOM 559 O LEU A 110 -22.976 3.420 126.868 1.00168.30 O
ANISOU 559 O LEU A 110 25073 25128 13745 -982 3050 -3531 O
ATOM 560 CB LEU A 110 -25.711 2.936 128.576 1.00183.89 C
ANISOU 560 CB LEU A 110 26802 27568 15499 -1044 3553 -3722 C
ATOM 561 CG LEU A 110 -26.461 1.758 129.211 1.00188.63 C
ANISOU 561 CG LEU A 110 27338 28291 16042 -1320 3729 -3709 C
ATOM 562 CD1 LEU A 110 -26.969 2.103 130.609 1.00187.78 C
ANISOU 562 CD1 LEU A 110 27415 28185 15747 -1324 3858 -3766 C
ATOM 563 CD2 LEU A 110 -27.599 1.276 128.317 1.00189.74 C
ANISOU 563 CD2 LEU A 110 27034 28752 16306 -1321 3891 -3806 C
ATOM 564 N LEU A 111 -23.462 5.223 128.127 1.00158.17 N
ANISOU 564 N LEU A 111 24030 23792 12276 -688 3165 -3703 N
ATOM 565 CA LEU A 111 -22.663 6.114 127.293 1.00146.59 C
ANISOU 565 CA LEU A 111 22628 22143 10928 -504 3024 -3700 C
ATOM 566 C LEU A 111 -21.197 5.735 127.484 1.00136.51 C
ANISOU 566 C LEU A 111 21578 20551 9739 -686 2745 -3534 C
ATOM 567 O LEU A 111 -20.410 5.779 126.529 1.00133.35 O
ANISOU 567 O LEU A 111 21090 20014 9563 -615 2573 -3436 O
ATOM 568 CB LEU A 111 -22.926 7.563 127.714 1.00147.85 C
ANISOU 568 CB LEU A 111 22950 22235 10991 -240 3125 -3842 C
ATOM 569 CG LEU A 111 -22.261 8.733 126.990 1.00143.91 C
ANISOU 569 CG LEU A 111 22541 21484 10654 21 3017 -3831 C
ATOM 570 CD1 LEU A 111 -23.203 9.924 126.942 1.00146.96 C
ANISOU 570 CD1 LEU A 111 22909 21970 10961 382 3239 -3989 C
ATOM 571 CD2 LEU A 111 -20.966 9.125 127.674 1.00140.37 C
ANISOU 571 CD2 LEU A 111 22460 20690 10183 -135 2834 -3792 C
ATOM 572 N CYS A 112 -20.834 5.289 128.688 1.00131.91 N
ANISOU 572 N CYS A 112 21269 19880 8970 -918 2699 -3498 N
ATOM 573 CA CYS A 112 -19.478 4.810 128.935 1.00130.17 C
ANISOU 573 CA CYS A 112 21241 19422 8796 -1081 2430 -3344 C
ATOM 574 C CYS A 112 -19.129 3.649 128.005 1.00126.94 C
ANISOU 574 C CYS A 112 20647 19033 8552 -1203 2336 -3179 C
ATOM 575 O CYS A 112 -18.143 3.692 127.249 1.00118.18 O
ANISOU 575 O CYS A 112 19513 17755 7635 -1188 2115 -3065 O
ATOM 576 CB CYS A 112 -19.333 4.432 130.412 1.00128.00 C
ANISOU 576 CB CYS A 112 21259 19103 8272 -1260 2410 -3328 C
ATOM 577 SG CYS A 112 -17.659 3.957 130.817 1.00131.07 S
ANISOU 577 SG CYS A 112 21830 19338 8631 -1486 2139 -3120 S
ATOM 578 N ARG A 113 -19.959 2.605 128.050 1.00126.26 N
ANISOU 578 N ARG A 113 20438 19148 8388 -1339 2520 -3177 N
ATOM 579 CA ARG A 113 -19.746 1.459 127.181 1.00124.23 C
ANISOU 579 CA ARG A 113 20025 18905 8273 -1476 2474 -3038 C
ATOM 580 C ARG A 113 -19.799 1.759 125.690 1.00125.53 C
ANISOU 580 C ARG A 113 19872 19109 8714 -1297 2417 -3040 C
ATOM 581 O ARG A 113 -19.048 1.170 124.903 1.00129.21 O
ANISOU 581 O ARG A 113 20272 19460 9361 -1345 2252 -2899 O
ATOM 582 CB ARG A 113 -20.819 0.445 127.566 1.00119.03 C
ANISOU 582 CB ARG A 113 19296 18464 7465 -1673 2742 -3082 C
ATOM 583 CG ARG A 113 -20.905 0.131 129.051 1.00121.00 C
ANISOU 583 CG ARG A 113 19815 18655 7506 -1798 2804 -3044 C
ATOM 584 CD ARG A 113 -22.273 -0.445 129.391 1.00124.31 C
ANISOU 584 CD ARG A 113 20057 19290 7885 -1890 3091 -3120 C
ATOM 585 NE ARG A 113 -22.350 -0.918 130.771 1.00130.37 N
ANISOU 585 NE ARG A 113 21088 19985 8460 -2029 3165 -3060 N
ATOM 586 CZ ARG A 113 -23.461 -1.369 131.345 1.00138.98 C
ANISOU 586 CZ ARG A 113 22100 21224 9481 -2133 3418 -3124 C
ATOM 587 NH1 ARG A 113 -24.595 -1.403 130.659 1.00142.46 N
ANISOU 587 NH1 ARG A 113 22182 21914 10032 -2113 3608 -3260 N
ATOM 588 NH2 ARG A 113 -23.440 -1.781 132.607 1.00141.45 N
ANISOU 588 NH2 ARG A 113 22686 21450 9609 -2251 3478 -3058 N
ATOM 589 N LEU A 114 -20.649 2.710 125.288 1.00127.26 N
ANISOU 589 N LEU A 114 19907 19489 8958 -1063 2548 -3193 N
ATOM 590 CA LEU A 114 -20.718 3.084 123.880 1.00119.96 C
ANISOU 590 CA LEU A 114 18700 18612 8267 -847 2497 -3193 C
ATOM 591 C LEU A 114 -19.421 3.737 123.426 1.00112.51 C
ANISOU 591 C LEU A 114 17898 17358 7493 -744 2245 -3090 C
ATOM 592 O LEU A 114 -18.931 3.455 122.326 1.00108.65 O
ANISOU 592 O LEU A 114 17254 16810 7218 -709 2117 -2993 O
ATOM 593 CB LEU A 114 -21.907 4.021 123.645 1.00119.05 C
ANISOU 593 CB LEU A 114 18391 18744 8098 -568 2699 -3375 C
ATOM 594 CG LEU A 114 -22.538 4.178 122.254 1.00106.75 C
ANISOU 594 CG LEU A 114 16453 17408 6697 -333 2743 -3418 C
ATOM 595 CD1 LEU A 114 -23.843 4.951 122.374 1.00109.25 C
ANISOU 595 CD1 LEU A 114 16604 18033 6873 -73 2976 -3611 C
ATOM 596 CD2 LEU A 114 -21.615 4.878 121.271 1.00104.69 C
ANISOU 596 CD2 LEU A 114 16222 16902 6651 -124 2547 -3318 C
ATOM 597 N VAL A 115 -18.827 4.579 124.273 1.00104.79 N
ANISOU 597 N VAL A 115 17215 16185 6416 -720 2178 -3123 N
ATOM 598 CA VAL A 115 -17.575 5.229 123.897 1.00103.38 C
ANISOU 598 CA VAL A 115 17171 15722 6386 -663 1959 -3058 C
ATOM 599 C VAL A 115 -16.467 4.196 123.719 1.00101.56 C
ANISOU 599 C VAL A 115 16969 15365 6254 -873 1734 -2882 C
ATOM 600 O VAL A 115 -15.746 4.202 122.712 1.00 99.56 O
ANISOU 600 O VAL A 115 16615 14992 6222 -821 1584 -2794 O
ATOM 601 CB VAL A 115 -17.192 6.301 124.933 1.00110.74 C
ANISOU 601 CB VAL A 115 18417 16494 7165 -642 1955 -3162 C
ATOM 602 CG1 VAL A 115 -15.739 6.714 124.764 1.00107.49 C
ANISOU 602 CG1 VAL A 115 18163 15804 6874 -695 1715 -3104 C
ATOM 603 CG2 VAL A 115 -18.103 7.510 124.793 1.00111.76 C
ANISOU 603 CG2 VAL A 115 18526 16679 7257 -360 2163 -3319 C
ATOM 604 N LYS A 116 -16.316 3.286 124.686 1.00128.14 N
ANISOU 604 N LYS A 116 20484 18756 9448 -1094 1716 -2821 N
ATOM 605 CA LYS A 116 -15.235 2.307 124.568 1.00120.50 C
ANISOU 605 CA LYS A 116 19569 17666 8548 -1252 1505 -2644 C
ATOM 606 C LYS A 116 -15.475 1.344 123.405 1.00113.15 C
ANISOU 606 C LYS A 116 18375 16809 7809 -1275 1525 -2544 C
ATOM 607 O LYS A 116 -14.530 0.955 122.696 1.00114.34 O
ANISOU 607 O LYS A 116 18480 16829 8136 -1293 1336 -2415 O
ATOM 608 CB LYS A 116 -15.064 1.548 125.882 1.00116.78 C
ANISOU 608 CB LYS A 116 19348 17205 7817 -1443 1502 -2590 C
ATOM 609 CG LYS A 116 -14.929 2.451 127.101 1.00104.77 C
ANISOU 609 CG LYS A 116 18085 15649 6074 -1436 1500 -2708 C
ATOM 610 CD LYS A 116 -13.794 3.458 126.949 1.00104.20 C
ANISOU 610 CD LYS A 116 18094 15397 6099 -1367 1286 -2745 C
ATOM 611 CE LYS A 116 -12.434 2.779 126.924 1.00103.24 C
ANISOU 611 CE LYS A 116 18035 15172 6020 -1469 1009 -2591 C
ATOM 612 NZ LYS A 116 -11.320 3.765 126.986 1.00103.31 N
ANISOU 612 NZ LYS A 116 18134 15043 6077 -1452 815 -2668 N
ATOM 613 N TYR A 117 -16.740 0.978 123.170 1.00108.42 N
ANISOU 613 N TYR A 117 17585 16434 7176 -1278 1758 -2620 N
ATOM 614 CA TYR A 117 -17.065 0.095 122.058 1.00105.52 C
ANISOU 614 CA TYR A 117 16950 16168 6974 -1318 1801 -2563 C
ATOM 615 C TYR A 117 -16.761 0.759 120.724 1.00102.73 C
ANISOU 615 C TYR A 117 16388 15773 6873 -1108 1692 -2558 C
ATOM 616 O TYR A 117 -16.218 0.118 119.819 1.00105.54 O
ANISOU 616 O TYR A 117 16629 16063 7410 -1148 1579 -2443 O
ATOM 617 CB TYR A 117 -18.538 -0.314 122.146 1.00103.98 C
ANISOU 617 CB TYR A 117 16571 16271 6664 -1377 2089 -2695 C
ATOM 618 CG TYR A 117 -19.089 -0.987 120.910 1.00103.20 C
ANISOU 618 CG TYR A 117 16137 16348 6728 -1395 2167 -2706 C
ATOM 619 CD1 TYR A 117 -18.903 -2.343 120.694 1.00 99.89 C
ANISOU 619 CD1 TYR A 117 15714 15897 6343 -1633 2186 -2601 C
ATOM 620 CD2 TYR A 117 -19.812 -0.270 119.968 1.00107.30 C
ANISOU 620 CD2 TYR A 117 16353 17073 7345 -1163 2231 -2827 C
ATOM 621 CE1 TYR A 117 -19.406 -2.966 119.568 1.00103.42 C
ANISOU 621 CE1 TYR A 117 15855 16511 6930 -1676 2266 -2634 C
ATOM 622 CE2 TYR A 117 -20.319 -0.883 118.837 1.00107.06 C
ANISOU 622 CE2 TYR A 117 15997 17241 7441 -1180 2292 -2854 C
ATOM 623 CZ TYR A 117 -20.113 -2.232 118.643 1.00105.98 C
ANISOU 623 CZ TYR A 117 15853 17070 7346 -1455 2310 -2767 C
ATOM 624 OH TYR A 117 -20.617 -2.847 117.520 1.00106.95 O
ANISOU 624 OH TYR A 117 15653 17396 7588 -1498 2380 -2816 O
ATOM 625 N LEU A 118 -17.083 2.049 120.586 1.00101.45 N
ANISOU 625 N LEU A 118 16201 15628 6718 -874 1736 -2676 N
ATOM 626 CA LEU A 118 -16.756 2.753 119.352 1.00 95.47 C
ANISOU 626 CA LEU A 118 15298 14798 6179 -653 1649 -2660 C
ATOM 627 C LEU A 118 -15.256 2.948 119.192 1.00 93.92 C
ANISOU 627 C LEU A 118 15269 14299 6118 -695 1401 -2542 C
ATOM 628 O LEU A 118 -14.759 2.980 118.063 1.00 92.11 O
ANISOU 628 O LEU A 118 14908 13991 6100 -612 1298 -2471 O
ATOM 629 CB LEU A 118 -17.486 4.093 119.294 1.00101.68 C
ANISOU 629 CB LEU A 118 16067 15654 6912 -367 1787 -2807 C
ATOM 630 CG LEU A 118 -18.704 4.084 118.367 1.00104.60 C
ANISOU 630 CG LEU A 118 16097 16336 7312 -171 1952 -2889 C
ATOM 631 CD1 LEU A 118 -19.674 2.985 118.762 1.00107.62 C
ANISOU 631 CD1 LEU A 118 16313 17014 7564 -372 2108 -2948 C
ATOM 632 CD2 LEU A 118 -19.403 5.426 118.365 1.00106.85 C
ANISOU 632 CD2 LEU A 118 16395 16686 7516 162 2093 -3020 C
ATOM 633 N GLN A 119 -14.515 3.046 120.298 1.00 94.75 N
ANISOU 633 N GLN A 119 15647 14258 6095 -828 1301 -2529 N
ATOM 634 CA GLN A 119 -13.060 3.109 120.193 1.00 93.57 C
ANISOU 634 CA GLN A 119 15620 13876 6056 -896 1057 -2433 C
ATOM 635 C GLN A 119 -12.500 1.825 119.594 1.00 91.82 C
ANISOU 635 C GLN A 119 15285 13643 5961 -1021 930 -2265 C
ATOM 636 O GLN A 119 -11.694 1.860 118.651 1.00 90.48 O
ANISOU 636 O GLN A 119 15025 13352 6000 -980 787 -2189 O
ATOM 637 CB GLN A 119 -12.444 3.367 121.567 1.00118.79 C
ANISOU 637 CB GLN A 119 19103 16984 9047 -1021 973 -2470 C
ATOM 638 CG GLN A 119 -12.115 4.817 121.843 1.00117.70 C
ANISOU 638 CG GLN A 119 19123 16707 8890 -925 972 -2608 C
ATOM 639 CD GLN A 119 -11.540 5.021 123.231 1.00115.74 C
ANISOU 639 CD GLN A 119 19143 16415 8419 -1069 889 -2667 C
ATOM 640 OE1 GLN A 119 -11.988 4.404 124.197 1.00 99.40 O
ANISOU 640 OE1 GLN A 119 17165 14466 6135 -1168 947 -2658 O
ATOM 641 NE2 GLN A 119 -10.534 5.880 123.335 1.00114.75 N
ANISOU 641 NE2 GLN A 119 19146 16123 8331 -1095 762 -2737 N
ATOM 642 N LEU A 120 -12.915 0.674 120.131 1.00 92.46 N
ANISOU 642 N LEU A 120 15387 13832 5912 -1178 1001 -2206 N
ATOM 643 CA LEU A 120 -12.445 -0.584 119.551 1.00 91.06 C
ANISOU 643 CA LEU A 120 15130 13623 5846 -1289 917 -2047 C
ATOM 644 C LEU A 120 -12.951 -0.770 118.121 1.00110.20 C
ANISOU 644 C LEU A 120 17255 16133 8485 -1205 986 -2048 C
ATOM 645 O LEU A 120 -12.228 -1.307 117.268 1.00 87.70 O
ANISOU 645 O LEU A 120 14318 13189 5815 -1221 857 -1930 O
ATOM 646 CB LEU A 120 -12.859 -1.771 120.417 1.00 98.98 C
ANISOU 646 CB LEU A 120 16261 14697 6649 -1474 1029 -1989 C
ATOM 647 CG LEU A 120 -12.231 -3.102 119.986 1.00103.21 C
ANISOU 647 CG LEU A 120 16799 15147 7267 -1588 947 -1808 C
ATOM 648 CD1 LEU A 120 -10.710 -2.995 119.946 1.00 90.48 C
ANISOU 648 CD1 LEU A 120 15288 13353 5736 -1546 658 -1690 C
ATOM 649 CD2 LEU A 120 -12.669 -4.242 120.892 1.00104.52 C
ANISOU 649 CD2 LEU A 120 17153 15348 7213 -1766 1100 -1748 C
ATOM 650 N VAL A 121 -14.176 -0.311 117.835 1.00100.23 N
ANISOU 650 N VAL A 121 15823 15066 7194 -1098 1184 -2185 N
ATOM 651 CA VAL A 121 -14.709 -0.402 116.480 1.00 92.47 C
ANISOU 651 CA VAL A 121 14536 14215 6384 -989 1244 -2206 C
ATOM 652 C VAL A 121 -13.861 0.420 115.524 1.00 90.26 C
ANISOU 652 C VAL A 121 14215 13766 6312 -809 1082 -2161 C
ATOM 653 O VAL A 121 -13.570 -0.011 114.403 1.00 93.96 O
ANISOU 653 O VAL A 121 14513 14223 6966 -788 1017 -2087 O
ATOM 654 CB VAL A 121 -16.183 0.051 116.455 1.00 97.89 C
ANISOU 654 CB VAL A 121 15042 15191 6963 -868 1479 -2380 C
ATOM 655 CG1 VAL A 121 -16.570 0.556 115.071 1.00 99.46 C
ANISOU 655 CG1 VAL A 121 14958 15511 7320 -631 1495 -2422 C
ATOM 656 CG2 VAL A 121 -17.102 -1.079 116.879 1.00103.60 C
ANISOU 656 CG2 VAL A 121 15686 16127 7548 -1088 1668 -2427 C
ATOM 657 N GLY A 122 -13.412 1.596 115.968 1.00 87.82 N
ANISOU 657 N GLY A 122 14085 13312 5973 -696 1027 -2211 N
ATOM 658 CA GLY A 122 -12.599 2.431 115.105 1.00 86.56 C
ANISOU 658 CA GLY A 122 13923 12967 6001 -548 908 -2182 C
ATOM 659 C GLY A 122 -11.213 1.861 114.891 1.00 85.03 C
ANISOU 659 C GLY A 122 13786 12580 5941 -691 685 -2044 C
ATOM 660 O GLY A 122 -10.665 1.937 113.786 1.00 99.88 O
ANISOU 660 O GLY A 122 15553 14372 8025 -619 600 -1981 O
ATOM 661 N MET A 123 -10.639 1.253 115.931 1.00 85.66 N
ANISOU 661 N MET A 123 14037 12611 5899 -879 589 -1992 N
ATOM 662 CA MET A 123 -9.350 0.591 115.756 1.00 84.49 C
ANISOU 662 CA MET A 123 13922 12325 5855 -990 374 -1856 C
ATOM 663 C MET A 123 -9.452 -0.517 114.714 1.00101.10 C
ANISOU 663 C MET A 123 15825 14478 8112 -1018 377 -1741 C
ATOM 664 O MET A 123 -8.684 -0.549 113.737 1.00100.81 O
ANISOU 664 O MET A 123 15688 14338 8279 -978 257 -1668 O
ATOM 665 CB MET A 123 -8.859 0.023 117.088 1.00 85.87 C
ANISOU 665 CB MET A 123 14313 12487 5826 -1147 286 -1812 C
ATOM 666 CG MET A 123 -8.445 1.067 118.109 1.00113.15 C
ANISOU 666 CG MET A 123 17973 15881 9137 -1152 232 -1925 C
ATOM 667 SD MET A 123 -7.821 0.328 119.633 1.00 89.30 S
ANISOU 667 SD MET A 123 15194 12887 5849 -1309 105 -1863 S
ATOM 668 CE MET A 123 -6.428 -0.600 119.000 1.00 89.64 C
ANISOU 668 CE MET A 123 15164 12847 6049 -1344 -144 -1682 C
ATOM 669 N PHE A 124 -10.435 -1.409 114.881 1.00 93.59 N
ANISOU 669 N PHE A 124 14811 13688 7062 -1099 535 -1741 N
ATOM 670 CA PHE A 124 -10.592 -2.513 113.940 1.00 90.22 C
ANISOU 670 CA PHE A 124 14208 13309 6761 -1160 567 -1656 C
ATOM 671 C PHE A 124 -10.911 -2.005 112.541 1.00 88.11 C
ANISOU 671 C PHE A 124 13688 13102 6687 -998 596 -1700 C
ATOM 672 O PHE A 124 -10.414 -2.548 111.546 1.00 84.95 O
ANISOU 672 O PHE A 124 13166 12647 6464 -1005 519 -1610 O
ATOM 673 CB PHE A 124 -11.688 -3.461 114.420 1.00 99.66 C
ANISOU 673 CB PHE A 124 15393 14677 7798 -1307 777 -1691 C
ATOM 674 CG PHE A 124 -11.177 -4.666 115.147 1.00104.56 C
ANISOU 674 CG PHE A 124 16218 15197 8315 -1490 748 -1558 C
ATOM 675 CD1 PHE A 124 -10.629 -5.731 114.449 1.00103.76 C
ANISOU 675 CD1 PHE A 124 16080 15004 8341 -1563 696 -1424 C
ATOM 676 CD2 PHE A 124 -11.253 -4.741 116.526 1.00106.63 C
ANISOU 676 CD2 PHE A 124 16728 15450 8337 -1569 785 -1561 C
ATOM 677 CE1 PHE A 124 -10.161 -6.844 115.118 1.00105.79 C
ANISOU 677 CE1 PHE A 124 16560 15149 8485 -1693 688 -1287 C
ATOM 678 CE2 PHE A 124 -10.787 -5.849 117.199 1.00110.18 C
ANISOU 678 CE2 PHE A 124 17397 15802 8665 -1700 769 -1422 C
ATOM 679 CZ PHE A 124 -10.239 -6.901 116.495 1.00110.83 C
ANISOU 679 CZ PHE A 124 17456 15780 8872 -1752 724 -1280 C
ATOM 680 N ALA A 125 -11.702 -0.934 112.449 1.00 90.29 N
ANISOU 680 N ALA A 125 13898 13487 6922 -826 707 -1833 N
ATOM 681 CA ALA A 125 -12.129 -0.435 111.151 1.00 80.67 C
ANISOU 681 CA ALA A 125 12449 12358 5843 -627 753 -1873 C
ATOM 682 C ALA A 125 -10.963 0.164 110.387 1.00 93.02 C
ANISOU 682 C ALA A 125 14050 13690 7602 -528 586 -1794 C
ATOM 683 O ALA A 125 -10.738 -0.173 109.221 1.00103.14 O
ANISOU 683 O ALA A 125 15166 14971 9052 -484 543 -1732 O
ATOM 684 CB ALA A 125 -13.240 0.598 111.334 1.00 82.25 C
ANISOU 684 CB ALA A 125 12605 12729 5918 -424 918 -2025 C
ATOM 685 N SER A 126 -10.190 1.038 111.037 1.00 85.08 N
ANISOU 685 N SER A 126 13264 12491 6572 -514 500 -1808 N
ATOM 686 CA SER A 126 -9.056 1.642 110.348 1.00 89.43 C
ANISOU 686 CA SER A 126 13855 12820 7303 -456 365 -1756 C
ATOM 687 C SER A 126 -8.029 0.587 109.959 1.00 86.66 C
ANISOU 687 C SER A 126 13453 12384 7089 -608 195 -1617 C
ATOM 688 O SER A 126 -7.508 0.606 108.835 1.00 75.52 O
ANISOU 688 O SER A 126 11931 10894 5870 -545 134 -1557 O
ATOM 689 CB SER A 126 -8.418 2.725 111.222 1.00 93.32 C
ANISOU 689 CB SER A 126 14595 13137 7724 -467 322 -1830 C
ATOM 690 OG SER A 126 -7.536 2.168 112.181 1.00 92.32 O
ANISOU 690 OG SER A 126 14600 12950 7529 -674 169 -1786 O
ATOM 691 N THR A 127 -7.780 -0.389 110.842 1.00 82.97 N
ANISOU 691 N THR A 127 13071 11937 6516 -790 134 -1558 N
ATOM 692 CA THR A 127 -6.760 -1.386 110.534 1.00 81.73 C
ANISOU 692 CA THR A 127 12893 11691 6471 -900 -24 -1417 C
ATOM 693 C THR A 127 -7.188 -2.279 109.373 1.00 88.91 C
ANISOU 693 C THR A 127 13591 12680 7512 -892 40 -1353 C
ATOM 694 O THR A 127 -6.434 -2.467 108.408 1.00 96.29 O
ANISOU 694 O THR A 127 14431 13520 8636 -867 -61 -1275 O
ATOM 695 CB THR A 127 -6.455 -2.220 111.778 1.00 82.81 C
ANISOU 695 CB THR A 127 13203 11832 6428 -1053 -83 -1357 C
ATOM 696 OG1 THR A 127 -5.940 -1.368 112.807 1.00 96.18 O
ANISOU 696 OG1 THR A 127 15078 13468 7998 -1065 -166 -1428 O
ATOM 697 CG2 THR A 127 -5.430 -3.293 111.465 1.00 76.55 C
ANISOU 697 CG2 THR A 127 12401 10954 5731 -1124 -234 -1200 C
ATOM 698 N TYR A 128 -8.408 -2.821 109.429 1.00 89.58 N
ANISOU 698 N TYR A 128 13589 12952 7497 -926 216 -1404 N
ATOM 699 CA TYR A 128 -8.851 -3.704 108.355 1.00 88.55 C
ANISOU 699 CA TYR A 128 13250 12922 7474 -953 289 -1374 C
ATOM 700 C TYR A 128 -9.117 -2.948 107.058 1.00 86.42 C
ANISOU 700 C TYR A 128 12776 12710 7350 -757 310 -1423 C
ATOM 701 O TYR A 128 -9.007 -3.531 105.975 1.00 83.73 O
ANISOU 701 O TYR A 128 12273 12390 7151 -759 298 -1374 O
ATOM 702 CB TYR A 128 -10.078 -4.500 108.804 1.00 86.25 C
ANISOU 702 CB TYR A 128 12914 12835 7022 -1081 489 -1445 C
ATOM 703 CG TYR A 128 -9.718 -5.696 109.667 1.00 90.19 C
ANISOU 703 CG TYR A 128 13606 13243 7420 -1290 489 -1344 C
ATOM 704 CD1 TYR A 128 -8.401 -5.925 110.050 1.00 89.69 C
ANISOU 704 CD1 TYR A 128 13724 12965 7390 -1309 296 -1203 C
ATOM 705 CD2 TYR A 128 -10.687 -6.604 110.083 1.00 96.34 C
ANISOU 705 CD2 TYR A 128 14390 14156 8058 -1459 692 -1393 C
ATOM 706 CE1 TYR A 128 -8.056 -7.016 110.829 1.00 91.92 C
ANISOU 706 CE1 TYR A 128 14206 13164 7556 -1448 297 -1093 C
ATOM 707 CE2 TYR A 128 -10.350 -7.700 110.864 1.00 99.31 C
ANISOU 707 CE2 TYR A 128 14992 14414 8325 -1631 718 -1285 C
ATOM 708 CZ TYR A 128 -9.033 -7.898 111.233 1.00 98.24 C
ANISOU 708 CZ TYR A 128 15053 14060 8215 -1603 516 -1124 C
ATOM 709 OH TYR A 128 -8.687 -8.981 112.007 1.00101.38 O
ANISOU 709 OH TYR A 128 15697 14342 8480 -1724 544 -1000 O
ATOM 710 N LEU A 129 -9.432 -1.653 107.127 1.00 92.57 N
ANISOU 710 N LEU A 129 13580 13502 8089 -575 348 -1514 N
ATOM 711 CA LEU A 129 -9.585 -0.887 105.897 1.00 73.41 C
ANISOU 711 CA LEU A 129 11007 11100 5785 -351 370 -1537 C
ATOM 712 C LEU A 129 -8.238 -0.626 105.238 1.00 73.43 C
ANISOU 712 C LEU A 129 11065 10851 5984 -334 211 -1435 C
ATOM 713 O LEU A 129 -8.122 -0.681 104.006 1.00 70.80 O
ANISOU 713 O LEU A 129 10582 10523 5794 -237 200 -1396 O
ATOM 714 CB LEU A 129 -10.318 0.422 106.181 1.00 80.08 C
ANISOU 714 CB LEU A 129 11905 12007 6513 -133 484 -1654 C
ATOM 715 CG LEU A 129 -11.817 0.412 105.871 1.00 83.93 C
ANISOU 715 CG LEU A 129 12177 12830 6882 5 660 -1767 C
ATOM 716 CD1 LEU A 129 -12.488 -0.836 106.420 1.00 87.13 C
ANISOU 716 CD1 LEU A 129 12486 13438 7182 -232 735 -1803 C
ATOM 717 CD2 LEU A 129 -12.475 1.652 106.433 1.00 84.23 C
ANISOU 717 CD2 LEU A 129 12319 12912 6773 219 774 -1874 C
ATOM 718 N LEU A 130 -7.199 -0.362 106.036 1.00 72.13 N
ANISOU 718 N LEU A 130 11103 10485 5820 -434 88 -1402 N
ATOM 719 CA LEU A 130 -5.863 -0.306 105.455 1.00 70.92 C
ANISOU 719 CA LEU A 130 10970 10127 5850 -464 -66 -1316 C
ATOM 720 C LEU A 130 -5.465 -1.655 104.875 1.00 80.17 C
ANISOU 720 C LEU A 130 12016 11317 7131 -577 -141 -1200 C
ATOM 721 O LEU A 130 -4.818 -1.713 103.822 1.00 83.89 O
ANISOU 721 O LEU A 130 12392 11700 7781 -536 -205 -1137 O
ATOM 722 CB LEU A 130 -4.844 0.155 106.494 1.00 71.75 C
ANISOU 722 CB LEU A 130 11281 10074 5908 -572 -188 -1331 C
ATOM 723 CG LEU A 130 -3.415 0.332 105.975 1.00 70.91 C
ANISOU 723 CG LEU A 130 11181 9784 5978 -618 -343 -1277 C
ATOM 724 CD1 LEU A 130 -3.384 1.303 104.801 1.00 80.56 C
ANISOU 724 CD1 LEU A 130 12360 10904 7346 -458 -267 -1304 C
ATOM 725 CD2 LEU A 130 -2.486 0.794 107.087 1.00 72.19 C
ANISOU 725 CD2 LEU A 130 11516 9854 6059 -741 -461 -1331 C
ATOM 726 N LEU A 131 -5.893 -2.748 105.517 1.00 70.08 N
ANISOU 726 N LEU A 131 10747 10141 5739 -716 -109 -1173 N
ATOM 727 CA LEU A 131 -5.635 -4.075 104.966 1.00 72.88 C
ANISOU 727 CA LEU A 131 11013 10498 6181 -821 -136 -1069 C
ATOM 728 C LEU A 131 -6.305 -4.244 103.610 1.00 75.57 C
ANISOU 728 C LEU A 131 11124 10961 6631 -738 -39 -1094 C
ATOM 729 O LEU A 131 -5.703 -4.766 102.666 1.00 78.32 O
ANISOU 729 O LEU A 131 11380 11239 7140 -747 -102 -1014 O
ATOM 730 CB LEU A 131 -6.133 -5.151 105.931 1.00 70.26 C
ANISOU 730 CB LEU A 131 10777 10240 5680 -983 -61 -1049 C
ATOM 731 CG LEU A 131 -5.171 -5.671 106.994 1.00 81.76 C
ANISOU 731 CG LEU A 131 12446 11565 7054 -1083 -192 -949 C
ATOM 732 CD1 LEU A 131 -5.856 -6.719 107.846 1.00 79.22 C
ANISOU 732 CD1 LEU A 131 12242 11311 6547 -1224 -63 -929 C
ATOM 733 CD2 LEU A 131 -3.945 -6.252 106.334 1.00 83.41 C
ANISOU 733 CD2 LEU A 131 12627 11633 7431 -1083 -346 -817 C
ATOM 734 N LEU A 132 -7.561 -3.807 103.500 1.00 78.76 N
ANISOU 734 N LEU A 132 11420 11571 6934 -646 113 -1214 N
ATOM 735 CA LEU A 132 -8.283 -3.963 102.243 1.00 74.28 C
ANISOU 735 CA LEU A 132 10608 11183 6432 -552 202 -1259 C
ATOM 736 C LEU A 132 -7.669 -3.105 101.145 1.00 76.37 C
ANISOU 736 C LEU A 132 10824 11337 6857 -356 127 -1221 C
ATOM 737 O LEU A 132 -7.553 -3.546 99.996 1.00 74.59 O
ANISOU 737 O LEU A 132 10441 11143 6754 -330 117 -1185 O
ATOM 738 CB LEU A 132 -9.761 -3.620 102.441 1.00 72.98 C
ANISOU 738 CB LEU A 132 10322 11310 6097 -469 374 -1411 C
ATOM 739 CG LEU A 132 -10.670 -3.688 101.213 1.00 78.87 C
ANISOU 739 CG LEU A 132 10779 12330 6859 -342 469 -1494 C
ATOM 740 CD1 LEU A 132 -10.500 -5.009 100.475 1.00 90.58 C
ANISOU 740 CD1 LEU A 132 12132 13841 8441 -529 469 -1454 C
ATOM 741 CD2 LEU A 132 -12.124 -3.487 101.615 1.00 78.27 C
ANISOU 741 CD2 LEU A 132 10567 12588 6583 -288 637 -1659 C
ATOM 742 N MET A 133 -7.228 -1.893 101.488 1.00 79.24 N
ANISOU 742 N MET A 133 11339 11550 7218 -233 88 -1232 N
ATOM 743 CA MET A 133 -6.591 -1.042 100.487 1.00 80.16 C
ANISOU 743 CA MET A 133 11455 11521 7480 -64 46 -1195 C
ATOM 744 C MET A 133 -5.275 -1.642 100.009 1.00 72.96 C
ANISOU 744 C MET A 133 10549 10416 6755 -190 -99 -1079 C
ATOM 745 O MET A 133 -4.976 -1.634 98.805 1.00 64.36 O
ANISOU 745 O MET A 133 9353 9296 5806 -103 -111 -1034 O
ATOM 746 CB MET A 133 -6.365 0.356 101.063 1.00 89.46 C
ANISOU 746 CB MET A 133 12839 12546 8605 50 67 -1247 C
ATOM 747 CG MET A 133 -5.446 1.227 100.227 1.00 92.52 C
ANISOU 747 CG MET A 133 13302 12705 9146 159 34 -1205 C
ATOM 748 SD MET A 133 -5.080 2.808 101.012 1.00 92.05 S
ANISOU 748 SD MET A 133 13534 12418 9021 225 89 -1287 S
ATOM 749 CE MET A 133 -6.718 3.517 101.124 1.00 70.60 C
ANISOU 749 CE MET A 133 10807 9915 6103 505 287 -1382 C
ATOM 750 N SER A 134 -4.484 -2.187 100.937 1.00 75.26 N
ANISOU 750 N SER A 134 10961 10597 7038 -378 -208 -1030 N
ATOM 751 CA SER A 134 -3.214 -2.791 100.556 1.00 80.89 C
ANISOU 751 CA SER A 134 11668 11155 7911 -477 -351 -922 C
ATOM 752 C SER A 134 -3.422 -4.047 99.720 1.00 77.93 C
ANISOU 752 C SER A 134 11132 10865 7612 -531 -330 -857 C
ATOM 753 O SER A 134 -2.701 -4.272 98.742 1.00 67.73 O
ANISOU 753 O SER A 134 9761 9485 6488 -512 -391 -789 O
ATOM 754 CB SER A 134 -2.401 -3.111 101.806 1.00 80.96 C
ANISOU 754 CB SER A 134 11834 11077 7851 -627 -475 -889 C
ATOM 755 OG SER A 134 -3.072 -4.068 102.605 1.00 84.12 O
ANISOU 755 OG SER A 134 12269 11592 8101 -730 -424 -878 O
ATOM 756 N LEU A 135 -4.416 -4.867 100.071 1.00 82.44 N
ANISOU 756 N LEU A 135 11658 11605 8059 -612 -227 -891 N
ATOM 757 CA LEU A 135 -4.724 -6.030 99.248 1.00 89.31 C
ANISOU 757 CA LEU A 135 12383 12562 8989 -688 -169 -862 C
ATOM 758 C LEU A 135 -5.225 -5.617 97.871 1.00 79.69 C
ANISOU 758 C LEU A 135 10962 11465 7852 -533 -108 -911 C
ATOM 759 O LEU A 135 -4.956 -6.306 96.879 1.00 77.15 O
ANISOU 759 O LEU A 135 10526 11138 7652 -561 -117 -866 O
ATOM 760 CB LEU A 135 -5.760 -6.913 99.940 1.00 97.69 C
ANISOU 760 CB LEU A 135 13448 13784 9885 -836 -32 -920 C
ATOM 761 CG LEU A 135 -6.138 -8.191 99.185 1.00105.45 C
ANISOU 761 CG LEU A 135 14305 14851 10909 -967 64 -918 C
ATOM 762 CD1 LEU A 135 -5.280 -9.361 99.640 1.00108.31 C
ANISOU 762 CD1 LEU A 135 14837 15017 11299 -1124 16 -787 C
ATOM 763 CD2 LEU A 135 -7.618 -8.511 99.327 1.00108.89 C
ANISOU 763 CD2 LEU A 135 14619 15564 11188 -1050 260 -1069 C
ATOM 764 N ASP A 136 -5.926 -4.488 97.807 1.00 71.98 N
ANISOU 764 N ASP A 136 9951 10599 6799 -350 -42 -1001 N
ATOM 765 CA ASP A 136 -6.387 -3.976 96.494 1.00 69.18 C
ANISOU 765 CA ASP A 136 9427 10366 6493 -147 9 -1035 C
ATOM 766 C ASP A 136 -5.182 -3.581 95.646 1.00 69.87 C
ANISOU 766 C ASP A 136 9555 10221 6770 -73 -91 -935 C
ATOM 767 O ASP A 136 -5.153 -3.932 94.482 1.00 75.11 O
ANISOU 767 O ASP A 136 10076 10931 7531 -19 -87 -909 O
ATOM 768 CB ASP A 136 -7.235 -2.724 96.636 1.00 67.64 C
ANISOU 768 CB ASP A 136 9230 10317 6152 79 106 -1136 C
ATOM 769 CG ASP A 136 -7.263 -1.957 95.340 1.00 72.84 C
ANISOU 769 CG ASP A 136 9834 10977 6864 362 129 -1126 C
ATOM 770 OD1 ASP A 136 -7.317 -2.597 94.310 1.00 80.82 O
ANISOU 770 OD1 ASP A 136 10672 12088 7946 403 129 -1108 O
ATOM 771 OD2 ASP A 136 -7.202 -0.739 95.379 1.00 84.68 O
ANISOU 771 OD2 ASP A 136 11483 12369 8321 549 161 -1137 O
ATOM 772 N ARG A 137 -4.211 -2.884 96.224 1.00 71.64 N
ANISOU 772 N ARG A 137 9969 10207 7044 -85 -175 -893 N
ATOM 773 CA ARG A 137 -3.009 -2.537 95.467 1.00 68.31 C
ANISOU 773 CA ARG A 137 9583 9568 6805 -56 -258 -815 C
ATOM 774 C ARG A 137 -2.220 -3.785 95.086 1.00 63.94 C
ANISOU 774 C ARG A 137 8954 8957 6384 -216 -351 -723 C
ATOM 775 O ARG A 137 -1.633 -3.847 93.998 1.00 64.22 O
ANISOU 775 O ARG A 137 8915 8917 6568 -170 -377 -669 O
ATOM 776 CB ARG A 137 -2.139 -1.575 96.274 1.00 76.24 C
ANISOU 776 CB ARG A 137 10791 10357 7819 -84 -318 -824 C
ATOM 777 CG ARG A 137 -2.892 -0.357 96.793 1.00 80.85 C
ANISOU 777 CG ARG A 137 11497 10962 8259 63 -208 -917 C
ATOM 778 CD ARG A 137 -2.600 0.898 95.988 1.00 81.53 C
ANISOU 778 CD ARG A 137 11675 10891 8412 250 -135 -923 C
ATOM 779 NE ARG A 137 -2.795 0.718 94.552 1.00 77.59 N
ANISOU 779 NE ARG A 137 11029 10455 7996 401 -94 -871 N
ATOM 780 CZ ARG A 137 -3.974 0.768 93.940 1.00 72.18 C
ANISOU 780 CZ ARG A 137 10219 9998 7208 611 7 -900 C
ATOM 781 NH1 ARG A 137 -5.084 0.977 94.634 1.00 68.81 N
ANISOU 781 NH1 ARG A 137 9785 9761 6598 693 85 -984 N
ATOM 782 NH2 ARG A 137 -4.044 0.602 92.627 1.00 71.46 N
ANISOU 782 NH2 ARG A 137 9996 9971 7185 744 30 -855 N
ATOM 783 N CYS A 138 -2.230 -4.803 95.949 1.00 70.11 N
ANISOU 783 N CYS A 138 9767 9767 7103 -389 -384 -701 N
ATOM 784 CA CYS A 138 -1.519 -6.038 95.642 1.00 80.89 C
ANISOU 784 CA CYS A 138 11095 11064 8574 -517 -451 -606 C
ATOM 785 C CYS A 138 -2.154 -6.768 94.466 1.00 84.88 C
ANISOU 785 C CYS A 138 11421 11703 9125 -506 -359 -619 C
ATOM 786 O CYS A 138 -1.445 -7.310 93.612 1.00 90.10 O
ANISOU 786 O CYS A 138 12022 12278 9934 -524 -403 -547 O
ATOM 787 CB CYS A 138 -1.476 -6.935 96.878 1.00 79.56 C
ANISOU 787 CB CYS A 138 11049 10887 8293 -674 -476 -573 C
ATOM 788 SG CYS A 138 -0.699 -8.538 96.609 1.00 79.29 S
ANISOU 788 SG CYS A 138 11021 10752 8351 -798 -522 -445 S
ATOM 789 N LEU A 139 -3.488 -6.792 94.400 1.00 84.68 N
ANISOU 789 N LEU A 139 11295 11911 8968 -480 -229 -723 N
ATOM 790 CA LEU A 139 -4.137 -7.402 93.243 1.00 85.58 C
ANISOU 790 CA LEU A 139 11209 12201 9106 -473 -141 -769 C
ATOM 791 C LEU A 139 -3.968 -6.550 91.989 1.00 88.09 C
ANISOU 791 C LEU A 139 11426 12527 9516 -259 -156 -763 C
ATOM 792 O LEU A 139 -3.856 -7.096 90.886 1.00 95.41 O
ANISOU 792 O LEU A 139 12225 13494 10533 -259 -145 -748 O
ATOM 793 CB LEU A 139 -5.620 -7.662 93.534 1.00 89.82 C
ANISOU 793 CB LEU A 139 11632 13036 9459 -516 4 -911 C
ATOM 794 CG LEU A 139 -6.634 -6.517 93.584 1.00 94.96 C
ANISOU 794 CG LEU A 139 12205 13904 9971 -309 70 -1022 C
ATOM 795 CD1 LEU A 139 -7.264 -6.241 92.218 1.00 95.07 C
ANISOU 795 CD1 LEU A 139 11988 14152 9981 -123 121 -1089 C
ATOM 796 CD2 LEU A 139 -7.703 -6.825 94.613 1.00 97.17 C
ANISOU 796 CD2 LEU A 139 12477 14380 10064 -427 180 -1134 C
ATOM 797 N ALA A 140 -3.942 -5.221 92.134 1.00 80.50 N
ANISOU 797 N ALA A 140 10544 11516 8524 -74 -165 -775 N
ATOM 798 CA ALA A 140 -3.732 -4.356 90.980 1.00 73.70 C
ANISOU 798 CA ALA A 140 9644 10622 7736 145 -157 -753 C
ATOM 799 C ALA A 140 -2.321 -4.494 90.422 1.00 68.75 C
ANISOU 799 C ALA A 140 9073 9735 7314 89 -252 -642 C
ATOM 800 O ALA A 140 -2.106 -4.255 89.229 1.00 64.29 O
ANISOU 800 O ALA A 140 8439 9156 6833 214 -236 -612 O
ATOM 801 CB ALA A 140 -4.027 -2.903 91.355 1.00 70.47 C
ANISOU 801 CB ALA A 140 9363 10178 7234 352 -110 -789 C
ATOM 802 N ILE A 141 -1.351 -4.863 91.259 1.00 56.49 N
ANISOU 802 N ILE A 141 7638 7995 5832 -84 -351 -584 N
ATOM 803 CA ILE A 141 0.016 -5.076 90.789 1.00 55.57 C
ANISOU 803 CA ILE A 141 7544 7668 5902 -144 -447 -492 C
ATOM 804 C ILE A 141 0.173 -6.486 90.232 1.00 83.11 C
ANISOU 804 C ILE A 141 10918 11193 9466 -258 -460 -442 C
ATOM 805 O ILE A 141 0.595 -6.665 89.085 1.00 76.14 O
ANISOU 805 O ILE A 141 9949 10274 8708 -214 -459 -403 O
ATOM 806 CB ILE A 141 1.041 -4.815 91.907 1.00 63.69 C
ANISOU 806 CB ILE A 141 8724 8521 6955 -254 -557 -465 C
ATOM 807 CG1 ILE A 141 1.191 -3.315 92.162 1.00 68.48 C
ANISOU 807 CG1 ILE A 141 9458 9025 7537 -157 -529 -519 C
ATOM 808 CG2 ILE A 141 2.399 -5.419 91.554 1.00 58.78 C
ANISOU 808 CG2 ILE A 141 8075 7752 6505 -343 -667 -378 C
ATOM 809 CD1 ILE A 141 1.770 -2.549 90.987 1.00 56.34 C
ANISOU 809 CD1 ILE A 141 7919 7356 6133 -46 -489 -498 C
ATOM 810 N CYS A 142 -0.155 -7.497 91.043 1.00 80.05 N
ANISOU 810 N CYS A 142 10555 10863 8997 -408 -456 -444 N
ATOM 811 CA CYS A 142 0.052 -8.884 90.632 1.00 85.12 C
ANISOU 811 CA CYS A 142 11144 11494 9703 -532 -444 -394 C
ATOM 812 C CYS A 142 -0.818 -9.254 89.437 1.00 84.72 C
ANISOU 812 C CYS A 142 10917 11626 9647 -503 -331 -462 C
ATOM 813 O CYS A 142 -0.402 -10.041 88.578 1.00 85.01 O
ANISOU 813 O CYS A 142 10889 11617 9793 -549 -325 -421 O
ATOM 814 CB CYS A 142 -0.230 -9.824 91.804 1.00 87.20 C
ANISOU 814 CB CYS A 142 11519 11764 9849 -691 -421 -385 C
ATOM 815 SG CYS A 142 0.867 -9.581 93.222 1.00 98.47 S
ANISOU 815 SG CYS A 142 13145 13015 11255 -718 -573 -301 S
ATOM 816 N GLN A 143 -2.024 -8.697 89.360 1.00 77.18 N
ANISOU 816 N GLN A 143 9872 10899 8555 -417 -243 -574 N
ATOM 817 CA GLN A 143 -2.970 -8.976 88.279 1.00 74.95 C
ANISOU 817 CA GLN A 143 9387 10867 8224 -374 -142 -670 C
ATOM 818 C GLN A 143 -3.537 -7.659 87.761 1.00 81.63 C
ANISOU 818 C GLN A 143 10163 11856 8999 -111 -122 -722 C
ATOM 819 O GLN A 143 -4.686 -7.310 88.050 1.00 79.45 O
ANISOU 819 O GLN A 143 9806 11828 8553 -39 -47 -832 O
ATOM 820 CB GLN A 143 -4.081 -9.913 88.754 1.00 79.25 C
ANISOU 820 CB GLN A 143 9861 11627 8623 -555 -23 -786 C
ATOM 821 CG GLN A 143 -3.564 -11.224 89.335 1.00 95.62 C
ANISOU 821 CG GLN A 143 12065 13523 10742 -799 -8 -723 C
ATOM 822 CD GLN A 143 -4.674 -12.139 89.822 1.00109.72 C
ANISOU 822 CD GLN A 143 13818 15494 12378 -1009 152 -848 C
ATOM 823 OE1 GLN A 143 -5.790 -12.111 89.301 1.00117.29 O
ANISOU 823 OE1 GLN A 143 14574 16758 13233 -1012 256 -1006 O
ATOM 824 NE2 GLN A 143 -4.373 -12.954 90.832 1.00113.21 N
ANISOU 824 NE2 GLN A 143 14459 15764 12793 -1183 180 -786 N
ATOM 825 N PRO A 144 -2.747 -6.901 86.995 1.00 82.65 N
ANISOU 825 N PRO A 144 10330 11830 9243 48 -174 -643 N
ATOM 826 CA PRO A 144 -3.232 -5.599 86.502 1.00 74.21 C
ANISOU 826 CA PRO A 144 9253 10851 8092 331 -131 -671 C
ATOM 827 C PRO A 144 -4.495 -5.696 85.662 1.00 64.87 C
ANISOU 827 C PRO A 144 7848 10039 6761 473 -46 -781 C
ATOM 828 O PRO A 144 -5.312 -4.765 85.677 1.00 73.41 O
ANISOU 828 O PRO A 144 8910 11291 7692 708 7 -837 O
ATOM 829 CB PRO A 144 -2.047 -5.071 85.682 1.00 74.05 C
ANISOU 829 CB PRO A 144 9320 10573 8241 418 -177 -562 C
ATOM 830 CG PRO A 144 -1.266 -6.291 85.315 1.00 71.65 C
ANISOU 830 CG PRO A 144 8961 10174 8090 215 -230 -508 C
ATOM 831 CD PRO A 144 -1.416 -7.236 86.465 1.00 82.15 C
ANISOU 831 CD PRO A 144 10319 11514 9379 -14 -251 -529 C
ATOM 832 N LEU A 145 -4.679 -6.787 84.914 1.00 66.60 N
ANISOU 832 N LEU A 145 7895 10403 7008 346 -26 -824 N
ATOM 833 CA LEU A 145 -5.849 -6.898 84.049 1.00 81.25 C
ANISOU 833 CA LEU A 145 9504 12657 8709 469 47 -955 C
ATOM 834 C LEU A 145 -7.118 -7.141 84.857 1.00 89.31 C
ANISOU 834 C LEU A 145 10404 13991 9538 394 122 -1112 C
ATOM 835 O LEU A 145 -8.156 -6.521 84.598 1.00 91.82 O
ANISOU 835 O LEU A 145 10572 14638 9676 620 170 -1215 O
ATOM 836 CB LEU A 145 -5.631 -8.011 83.025 1.00 76.53 C
ANISOU 836 CB LEU A 145 8764 12117 8196 320 57 -977 C
ATOM 837 CG LEU A 145 -4.488 -7.802 82.030 1.00 67.58 C
ANISOU 837 CG LEU A 145 7707 10734 7236 413 0 -842 C
ATOM 838 CD1 LEU A 145 -4.261 -9.046 81.188 1.00 63.52 C
ANISOU 838 CD1 LEU A 145 7072 10256 6807 223 19 -871 C
ATOM 839 CD2 LEU A 145 -4.768 -6.601 81.144 1.00 69.37 C
ANISOU 839 CD2 LEU A 145 7908 11075 7375 776 12 -824 C
ATOM 840 N ARG A 146 -7.059 -8.045 85.831 1.00 96.56 N
ANISOU 840 N ARG A 146 11386 14822 10480 91 141 -1132 N
ATOM 841 CA ARG A 146 -8.216 -8.374 86.654 1.00101.36 C
ANISOU 841 CA ARG A 146 11897 15704 10913 -31 235 -1286 C
ATOM 842 C ARG A 146 -8.265 -7.431 87.851 1.00102.62 C
ANISOU 842 C ARG A 146 12231 15753 11007 71 215 -1248 C
ATOM 843 O ARG A 146 -7.306 -7.352 88.626 1.00109.16 O
ANISOU 843 O ARG A 146 13296 16236 11944 -16 145 -1122 O
ATOM 844 CB ARG A 146 -8.155 -9.836 87.099 1.00103.30 C
ANISOU 844 CB ARG A 146 12165 15886 11197 -410 301 -1324 C
ATOM 845 CG ARG A 146 -8.500 -10.822 85.986 1.00110.67 C
ANISOU 845 CG ARG A 146 12889 17026 12137 -546 375 -1435 C
ATOM 846 CD ARG A 146 -7.422 -11.881 85.776 1.00115.94 C
ANISOU 846 CD ARG A 146 13703 17360 12988 -764 361 -1321 C
ATOM 847 NE ARG A 146 -7.556 -13.011 86.691 1.00124.23 N
ANISOU 847 NE ARG A 146 14874 18313 14014 -1089 470 -1355 N
ATOM 848 CZ ARG A 146 -6.953 -14.184 86.521 1.00132.19 C
ANISOU 848 CZ ARG A 146 15993 19106 15128 -1310 521 -1306 C
ATOM 849 NH1 ARG A 146 -6.177 -14.384 85.464 1.00132.49 N
ANISOU 849 NH1 ARG A 146 16008 19020 15311 -1250 464 -1230 N
ATOM 850 NH2 ARG A 146 -7.130 -15.159 87.405 1.00136.20 N
ANISOU 850 NH2 ARG A 146 16652 19510 15587 -1582 646 -1329 N
ATOM 851 N SER A 147 -9.387 -6.733 88.013 1.00100.82 N
ANISOU 851 N SER A 147 11878 15840 10589 258 277 -1368 N
ATOM 852 CA SER A 147 -9.490 -5.695 89.027 1.00102.52 C
ANISOU 852 CA SER A 147 12261 15962 10729 402 271 -1341 C
ATOM 853 C SER A 147 -10.907 -5.658 89.582 1.00106.12 C
ANISOU 853 C SER A 147 12545 16814 10963 420 379 -1522 C
ATOM 854 O SER A 147 -11.864 -6.062 88.915 1.00111.06 O
ANISOU 854 O SER A 147 12883 17841 11472 437 447 -1675 O
ATOM 855 CB SER A 147 -9.097 -4.327 88.460 1.00102.57 C
ANISOU 855 CB SER A 147 12375 15841 10756 764 229 -1246 C
ATOM 856 OG SER A 147 -9.749 -4.080 87.228 1.00104.49 O
ANISOU 856 OG SER A 147 12401 16392 10908 1019 261 -1306 O
ATOM 857 N LEU A 148 -11.025 -5.164 90.813 1.00102.74 N
ANISOU 857 N LEU A 148 12282 16286 10467 412 396 -1518 N
ATOM 858 CA LEU A 148 -12.280 -5.236 91.551 1.00100.40 C
ANISOU 858 CA LEU A 148 11849 16328 9969 373 508 -1688 C
ATOM 859 C LEU A 148 -13.370 -4.382 90.912 1.00 94.13 C
ANISOU 859 C LEU A 148 10825 15946 8994 737 560 -1806 C
ATOM 860 O LEU A 148 -13.119 -3.274 90.430 1.00 94.47 O
ANISOU 860 O LEU A 148 10958 15900 9038 1087 519 -1719 O
ATOM 861 CB LEU A 148 -12.065 -4.789 92.997 1.00104.84 C
ANISOU 861 CB LEU A 148 12670 16662 10500 313 507 -1642 C
ATOM 862 CG LEU A 148 -11.098 -5.598 93.861 1.00101.09 C
ANISOU 862 CG LEU A 148 12429 15832 10147 -15 457 -1534 C
ATOM 863 CD1 LEU A 148 -10.874 -4.911 95.199 1.00101.43 C
ANISOU 863 CD1 LEU A 148 12723 15682 10136 -3 439 -1493 C
ATOM 864 CD2 LEU A 148 -11.625 -7.007 94.067 1.00104.55 C
ANISOU 864 CD2 LEU A 148 12754 16430 10542 -351 560 -1634 C
ATOM 865 N ARG A 149 -14.591 -4.910 90.919 1.00 91.42 N
ANISOU 865 N ARG A 149 10189 16063 8483 656 664 -2012 N
ATOM 866 CA ARG A 149 -15.783 -4.148 90.584 1.00 94.65 C
ANISOU 866 CA ARG A 149 10351 16939 8671 1000 723 -2155 C
ATOM 867 C ARG A 149 -16.186 -3.251 91.752 1.00103.93 C
ANISOU 867 C ARG A 149 11678 18083 9729 1146 772 -2165 C
ATOM 868 O ARG A 149 -15.850 -3.510 92.911 1.00105.97 O
ANISOU 868 O ARG A 149 12147 18083 10035 889 788 -2128 O
ATOM 869 CB ARG A 149 -16.940 -5.083 90.232 1.00 90.92 C
ANISOU 869 CB ARG A 149 9480 17012 8054 819 823 -2406 C
ATOM 870 CG ARG A 149 -16.614 -6.111 89.170 1.00 92.42 C
ANISOU 870 CG ARG A 149 9521 17245 8349 607 801 -2432 C
ATOM 871 CD ARG A 149 -17.763 -7.089 89.010 1.00102.04 C
ANISOU 871 CD ARG A 149 10366 18985 9417 343 931 -2716 C
ATOM 872 NE ARG A 149 -18.984 -6.434 88.554 1.00109.84 N
ANISOU 872 NE ARG A 149 11001 20573 10160 681 962 -2904 N
ATOM 873 CZ ARG A 149 -19.437 -6.489 87.307 1.00109.07 C
ANISOU 873 CZ ARG A 149 10583 20893 9966 855 935 -3019 C
ATOM 874 NH1 ARG A 149 -20.558 -5.862 86.980 1.00115.00 N
ANISOU 874 NH1 ARG A 149 11009 22219 10466 1200 957 -3188 N
ATOM 875 NH2 ARG A 149 -18.773 -7.179 86.389 1.00101.21 N
ANISOU 875 NH2 ARG A 149 9588 19758 9112 699 886 -2969 N
ATOM 876 N ARG A 150 -16.911 -2.174 91.432 1.00108.44 N
ANISOU 876 N ARG A 150 12150 18922 10130 1588 800 -2210 N
ATOM 877 CA ARG A 150 -17.435 -1.308 92.486 1.00110.86 C
ANISOU 877 CA ARG A 150 12576 19247 10299 1758 870 -2244 C
ATOM 878 C ARG A 150 -18.389 -2.062 93.406 1.00114.26 C
ANISOU 878 C ARG A 150 12817 19995 10602 1462 980 -2444 C
ATOM 879 O ARG A 150 -18.408 -1.817 94.621 1.00118.29 O
ANISOU 879 O ARG A 150 13524 20339 11081 1366 1027 -2438 O
ATOM 880 CB ARG A 150 -18.145 -0.103 91.869 1.00112.22 C
ANISOU 880 CB ARG A 150 12654 19700 10285 2321 901 -2267 C
ATOM 881 CG ARG A 150 -17.227 0.868 91.140 1.00112.60 C
ANISOU 881 CG ARG A 150 12979 19371 10433 2648 837 -2059 C
ATOM 882 CD ARG A 150 -17.710 1.124 89.721 1.00116.97 C
ANISOU 882 CD ARG A 150 13288 20286 10869 3035 824 -2082 C
ATOM 883 NE ARG A 150 -17.324 0.052 88.809 1.00116.41 N
ANISOU 883 NE ARG A 150 13030 20277 10923 2775 749 -2091 N
ATOM 884 CZ ARG A 150 -17.753 -0.054 87.556 1.00113.62 C
ANISOU 884 CZ ARG A 150 12403 20296 10470 3003 725 -2146 C
ATOM 885 NH1 ARG A 150 -18.593 0.845 87.063 1.00115.76 N
ANISOU 885 NH1 ARG A 150 12549 20930 10504 3525 763 -2189 N
ATOM 886 NH2 ARG A 150 -17.345 -1.062 86.799 1.00112.89 N
ANISOU 886 NH2 ARG A 150 12169 20224 10502 2727 667 -2160 N
ATOM 887 N ARG A 151 -19.159 -3.004 92.855 1.00113.64 N
ANISOU 887 N ARG A 151 12368 20363 10446 1287 1034 -2632 N
ATOM 888 CA ARG A 151 -20.044 -3.819 93.681 1.00108.41 C
ANISOU 888 CA ARG A 151 11528 19993 9669 945 1170 -2840 C
ATOM 889 C ARG A 151 -19.243 -4.616 94.701 1.00 95.12 C
ANISOU 889 C ARG A 151 10155 17849 8137 492 1183 -2741 C
ATOM 890 O ARG A 151 -19.568 -4.626 95.895 1.00 95.02 O
ANISOU 890 O ARG A 151 10254 17804 8046 346 1271 -2789 O
ATOM 891 CB ARG A 151 -20.866 -4.761 92.797 1.00118.61 C
ANISOU 891 CB ARG A 151 12381 21812 10874 780 1235 -3070 C
ATOM 892 CG ARG A 151 -21.873 -4.084 91.879 1.00127.65 C
ANISOU 892 CG ARG A 151 13146 23548 11807 1223 1233 -3220 C
ATOM 893 CD ARG A 151 -22.231 -4.995 90.711 1.00126.80 C
ANISOU 893 CD ARG A 151 12674 23802 11700 1061 1221 -3370 C
ATOM 894 NE ARG A 151 -23.627 -4.872 90.296 1.00130.22 N
ANISOU 894 NE ARG A 151 12696 24740 12042 1195 1172 -3529 N
ATOM 895 CZ ARG A 151 -24.580 -5.737 90.631 1.00132.88 C
ANISOU 895 CZ ARG A 151 12765 25371 12354 814 1245 -3748 C
ATOM 896 NH1 ARG A 151 -24.282 -6.785 91.385 1.00135.67 N
ANISOU 896 NH1 ARG A 151 13249 25522 12777 286 1393 -3814 N
ATOM 897 NH2 ARG A 151 -25.826 -5.557 90.211 1.00132.17 N
ANISOU 897 NH2 ARG A 151 12295 25772 12151 960 1171 -3904 N
ATOM 898 N THR A 152 -18.170 -5.272 94.247 1.00 87.68 N
ANISOU 898 N THR A 152 9365 16549 7399 292 1096 -2594 N
ATOM 899 CA THR A 152 -17.336 -6.058 95.150 1.00 86.19 C
ANISOU 899 CA THR A 152 9480 15928 7342 -90 1097 -2480 C
ATOM 900 C THR A 152 -16.647 -5.178 96.185 1.00 84.69 C
ANISOU 900 C THR A 152 9649 15343 7186 31 1026 -2316 C
ATOM 901 O THR A 152 -16.474 -5.591 97.339 1.00 88.66 O
ANISOU 901 O THR A 152 10355 15655 7676 -224 1070 -2293 O
ATOM 902 CB THR A 152 -16.300 -6.847 94.342 1.00 84.63 C
ANISOU 902 CB THR A 152 9358 15449 7350 -257 1009 -2351 C
ATOM 903 OG1 THR A 152 -16.973 -7.697 93.403 1.00 89.00 O
ANISOU 903 OG1 THR A 152 9580 16376 7859 -401 1091 -2528 O
ATOM 904 CG2 THR A 152 -15.425 -7.698 95.253 1.00 72.98 C
ANISOU 904 CG2 THR A 152 8196 13544 5989 -609 1009 -2224 C
ATOM 905 N ALA A 153 -16.287 -3.948 95.807 1.00 83.40 N
ANISOU 905 N ALA A 153 9578 15063 7047 417 932 -2213 N
ATOM 906 CA ALA A 153 -15.627 -3.053 96.751 1.00 83.82 C
ANISOU 906 CA ALA A 153 9973 14747 7128 517 879 -2084 C
ATOM 907 C ALA A 153 -16.581 -2.628 97.861 1.00 82.85 C
ANISOU 907 C ALA A 153 9850 14822 6807 553 997 -2212 C
ATOM 908 O ALA A 153 -16.236 -2.697 99.050 1.00 76.83 O
ANISOU 908 O ALA A 153 9333 13821 6040 367 1004 -2169 O
ATOM 909 CB ALA A 153 -15.071 -1.834 96.017 1.00 85.85 C
ANISOU 909 CB ALA A 153 10344 14828 7449 905 795 -1964 C
ATOM 910 N ARG A 154 -17.797 -2.205 97.494 1.00 78.58 N
ANISOU 910 N ARG A 154 9025 14744 6088 801 1092 -2376 N
ATOM 911 CA ARG A 154 -18.775 -1.842 98.516 1.00 89.79 C
ANISOU 911 CA ARG A 154 10410 16394 7311 839 1218 -2516 C
ATOM 912 C ARG A 154 -19.122 -3.046 99.382 1.00 94.34 C
ANISOU 912 C ARG A 154 10951 17048 7847 377 1322 -2619 C
ATOM 913 O ARG A 154 -19.316 -2.917 100.600 1.00 97.75 O
ANISOU 913 O ARG A 154 11548 17404 8190 270 1393 -2645 O
ATOM 914 CB ARG A 154 -20.041 -1.278 97.871 1.00 83.23 C
ANISOU 914 CB ARG A 154 9229 16110 6285 1200 1299 -2687 C
ATOM 915 CG ARG A 154 -19.824 -0.174 96.849 1.00 92.29 C
ANISOU 915 CG ARG A 154 10397 17231 7440 1694 1224 -2587 C
ATOM 916 CD ARG A 154 -21.127 0.135 96.118 1.00103.21 C
ANISOU 916 CD ARG A 154 11375 19236 8603 2041 1296 -2769 C
ATOM 917 NE ARG A 154 -20.949 0.227 94.669 1.00115.40 N
ANISOU 917 NE ARG A 154 12765 20899 10182 2290 1213 -2718 N
ATOM 918 CZ ARG A 154 -21.950 0.213 93.793 1.00122.01 C
ANISOU 918 CZ ARG A 154 13197 22317 10843 2541 1242 -2878 C
ATOM 919 NH1 ARG A 154 -23.201 0.105 94.217 1.00129.17 N
ANISOU 919 NH1 ARG A 154 13809 23670 11601 2533 1320 -3068 N
ATOM 920 NH2 ARG A 154 -21.702 0.301 92.492 1.00116.91 N
ANISOU 920 NH2 ARG A 154 12447 21749 10226 2769 1159 -2816 N
ATOM 921 N LEU A 155 -19.156 -4.234 98.773 1.00 98.32 N
ANISOU 921 N LEU A 155 11274 17671 8413 90 1346 -2675 N
ATOM 922 CA LEU A 155 -19.483 -5.447 99.512 1.00 95.95 C
ANISOU 922 CA LEU A 155 10971 17415 8069 -365 1482 -2774 C
ATOM 923 C LEU A 155 -18.431 -5.733 100.573 1.00 83.48 C
ANISOU 923 C LEU A 155 9815 15318 6586 -586 1429 -2587 C
ATOM 924 O LEU A 155 -18.755 -5.947 101.749 1.00 85.07 O
ANISOU 924 O LEU A 155 10151 15496 6676 -771 1535 -2632 O
ATOM 925 CB LEU A 155 -19.598 -6.616 98.530 1.00100.74 C
ANISOU 925 CB LEU A 155 11344 18193 8740 -617 1525 -2859 C
ATOM 926 CG LEU A 155 -20.389 -7.869 98.900 1.00 95.52 C
ANISOU 926 CG LEU A 155 10539 17770 7983 -1061 1738 -3061 C
ATOM 927 CD1 LEU A 155 -21.882 -7.601 98.823 1.00 97.75 C
ANISOU 927 CD1 LEU A 155 10418 18678 8046 -977 1885 -3350 C
ATOM 928 CD2 LEU A 155 -19.999 -9.020 97.984 1.00 85.83 C
ANISOU 928 CD2 LEU A 155 9241 16486 6882 -1331 1749 -3063 C
ATOM 929 N ALA A 156 -17.155 -5.709 100.176 1.00 77.83 N
ANISOU 929 N ALA A 156 9308 14203 6062 -552 1261 -2378 N
ATOM 930 CA ALA A 156 -16.081 -5.988 101.122 1.00 76.61 C
ANISOU 930 CA ALA A 156 9528 13594 5987 -732 1185 -2202 C
ATOM 931 C ALA A 156 -16.008 -4.926 102.210 1.00 97.70 C
ANISOU 931 C ALA A 156 12418 16135 8567 -571 1159 -2170 C
ATOM 932 O ALA A 156 -15.740 -5.242 103.377 1.00 77.47 O
ANISOU 932 O ALA A 156 10098 13387 5950 -766 1181 -2125 O
ATOM 933 CB ALA A 156 -14.745 -6.088 100.384 1.00 74.20 C
ANISOU 933 CB ALA A 156 9350 12943 5900 -695 1006 -2008 C
ATOM 934 N VAL A 157 -16.290 -3.668 101.861 1.00 94.29 N
ANISOU 934 N VAL A 157 11919 15807 8101 -210 1129 -2199 N
ATOM 935 CA VAL A 157 -16.220 -2.607 102.860 1.00 89.15 C
ANISOU 935 CA VAL A 157 11496 15016 7363 -55 1122 -2181 C
ATOM 936 C VAL A 157 -17.310 -2.788 103.910 1.00 91.44 C
ANISOU 936 C VAL A 157 11739 15560 7444 -174 1293 -2338 C
ATOM 937 O VAL A 157 -17.042 -2.760 105.121 1.00 98.36 O
ANISOU 937 O VAL A 157 12873 16245 8257 -309 1303 -2303 O
ATOM 938 CB VAL A 157 -16.307 -1.229 102.183 1.00 78.39 C
ANISOU 938 CB VAL A 157 10103 13683 6000 376 1088 -2175 C
ATOM 939 CG1 VAL A 157 -16.746 -0.174 103.178 1.00 80.03 C
ANISOU 939 CG1 VAL A 157 10467 13887 6054 552 1162 -2234 C
ATOM 940 CG2 VAL A 157 -14.961 -0.860 101.578 1.00 76.29 C
ANISOU 940 CG2 VAL A 157 10023 13028 5935 450 925 -1996 C
ATOM 941 N LEU A 158 -18.554 -2.999 103.470 1.00 90.08 N
ANISOU 941 N LEU A 158 11227 15846 7152 -134 1434 -2524 N
ATOM 942 CA LEU A 158 -19.627 -3.170 104.443 1.00 95.24 C
ANISOU 942 CA LEU A 158 11811 16771 7605 -259 1615 -2694 C
ATOM 943 C LEU A 158 -19.441 -4.443 105.260 1.00 99.33 C
ANISOU 943 C LEU A 158 12477 17151 8111 -712 1695 -2680 C
ATOM 944 O LEU A 158 -19.773 -4.469 106.455 1.00103.63 O
ANISOU 944 O LEU A 158 13174 17681 8518 -843 1798 -2725 O
ATOM 945 CB LEU A 158 -20.985 -3.167 103.749 1.00 95.32 C
ANISOU 945 CB LEU A 158 11384 17351 7483 -131 1749 -2921 C
ATOM 946 CG LEU A 158 -22.062 -2.406 104.526 1.00101.01 C
ANISOU 946 CG LEU A 158 12024 18369 7987 48 1887 -3080 C
ATOM 947 CD1 LEU A 158 -21.687 -0.933 104.665 1.00102.05 C
ANISOU 947 CD1 LEU A 158 12369 18290 8114 473 1797 -2974 C
ATOM 948 CD2 LEU A 158 -23.425 -2.560 103.871 1.00 98.46 C
ANISOU 948 CD2 LEU A 158 11221 18675 7515 139 2022 -3330 C
ATOM 949 N ALA A 159 -18.880 -5.495 104.653 1.00 96.25 N
ANISOU 949 N ALA A 159 12080 16635 7857 -943 1657 -2607 N
ATOM 950 CA ALA A 159 -18.613 -6.708 105.415 1.00 98.68 C
ANISOU 950 CA ALA A 159 12591 16754 8148 -1342 1744 -2564 C
ATOM 951 C ALA A 159 -17.569 -6.459 106.494 1.00 95.66 C
ANISOU 951 C ALA A 159 12623 15943 7779 -1355 1625 -2372 C
ATOM 952 O ALA A 159 -17.729 -6.914 107.633 1.00 96.91 O
ANISOU 952 O ALA A 159 12980 16032 7809 -1566 1733 -2378 O
ATOM 953 CB ALA A 159 -18.169 -7.832 104.481 1.00 82.31 C
ANISOU 953 CB ALA A 159 10450 14604 6220 -1548 1733 -2515 C
ATOM 954 N THR A 160 -16.510 -5.711 106.171 1.00 92.23 N
ANISOU 954 N THR A 160 12320 15237 7485 -1133 1409 -2214 N
ATOM 955 CA THR A 160 -15.519 -5.403 107.195 1.00 93.77 C
ANISOU 955 CA THR A 160 12873 15079 7677 -1143 1286 -2064 C
ATOM 956 C THR A 160 -16.104 -4.535 108.301 1.00 94.66 C
ANISOU 956 C THR A 160 13087 15272 7606 -1050 1360 -2154 C
ATOM 957 O THR A 160 -15.747 -4.711 109.470 1.00 99.86 O
ANISOU 957 O THR A 160 14019 15756 8169 -1186 1356 -2096 O
ATOM 958 CB THR A 160 -14.304 -4.716 106.578 1.00102.29 C
ANISOU 958 CB THR A 160 14039 15886 8940 -944 1061 -1915 C
ATOM 959 OG1 THR A 160 -14.726 -3.568 105.831 1.00110.31 O
ANISOU 959 OG1 THR A 160 14881 17053 9977 -632 1052 -1990 O
ATOM 960 CG2 THR A 160 -13.569 -5.674 105.661 1.00102.98 C
ANISOU 960 CG2 THR A 160 14079 15845 9202 -1063 981 -1805 C
ATOM 961 N TRP A 161 -17.023 -3.623 107.969 1.00 94.28 N
ANISOU 961 N TRP A 161 12829 15502 7491 -808 1436 -2297 N
ATOM 962 CA TRP A 161 -17.621 -2.800 109.020 1.00 98.15 C
ANISOU 962 CA TRP A 161 13419 16073 7801 -708 1526 -2391 C
ATOM 963 C TRP A 161 -18.480 -3.646 109.956 1.00 99.53 C
ANISOU 963 C TRP A 161 13592 16428 7795 -989 1727 -2502 C
ATOM 964 O TRP A 161 -18.394 -3.519 111.188 1.00 94.06 O
ANISOU 964 O TRP A 161 13153 15614 6973 -1076 1759 -2488 O
ATOM 965 CB TRP A 161 -18.452 -1.669 108.413 1.00 94.53 C
ANISOU 965 CB TRP A 161 12737 15884 7296 -347 1579 -2515 C
ATOM 966 CG TRP A 161 -17.639 -0.528 107.887 1.00 89.28 C
ANISOU 966 CG TRP A 161 12197 14975 6751 -46 1427 -2410 C
ATOM 967 CD1 TRP A 161 -17.312 -0.291 106.587 1.00 97.10 C
ANISOU 967 CD1 TRP A 161 13049 15956 7889 145 1338 -2353 C
ATOM 968 CD2 TRP A 161 -17.056 0.539 108.647 1.00 86.64 C
ANISOU 968 CD2 TRP A 161 12166 14364 6389 83 1369 -2361 C
ATOM 969 NE1 TRP A 161 -16.559 0.852 106.486 1.00 99.85 N
ANISOU 969 NE1 TRP A 161 13609 16023 8308 378 1243 -2267 N
ATOM 970 CE2 TRP A 161 -16.387 1.381 107.737 1.00 91.10 C
ANISOU 970 CE2 TRP A 161 12771 14746 7096 334 1262 -2279 C
ATOM 971 CE3 TRP A 161 -17.033 0.862 110.007 1.00 85.50 C
ANISOU 971 CE3 TRP A 161 12273 14108 6106 -3 1408 -2389 C
ATOM 972 CZ2 TRP A 161 -15.702 2.526 108.142 1.00 94.07 C
ANISOU 972 CZ2 TRP A 161 13433 14826 7486 478 1210 -2238 C
ATOM 973 CZ3 TRP A 161 -16.353 1.999 110.407 1.00 85.51 C
ANISOU 973 CZ3 TRP A 161 12541 13833 6117 148 1338 -2351 C
ATOM 974 CH2 TRP A 161 -15.696 2.817 109.478 1.00 93.99 C
ANISOU 974 CH2 TRP A 161 13652 14721 7340 375 1248 -2282 C
ATOM 975 N LEU A 162 -19.315 -4.521 109.388 1.00105.57 N
ANISOU 975 N LEU A 162 14081 17492 8540 -1150 1877 -2625 N
ATOM 976 CA LEU A 162 -20.143 -5.374 110.234 1.00107.79 C
ANISOU 976 CA LEU A 162 14366 17938 8650 -1457 2105 -2747 C
ATOM 977 C LEU A 162 -19.284 -6.320 111.066 1.00106.42 C
ANISOU 977 C LEU A 162 14560 17402 8474 -1747 2086 -2582 C
ATOM 978 O LEU A 162 -19.599 -6.598 112.233 1.00116.82 O
ANISOU 978 O LEU A 162 16071 18696 9621 -1919 2221 -2610 O
ATOM 979 CB LEU A 162 -21.139 -6.163 109.380 1.00111.17 C
ANISOU 979 CB LEU A 162 14417 18757 9066 -1612 2278 -2933 C
ATOM 980 CG LEU A 162 -22.522 -5.542 109.160 1.00111.82 C
ANISOU 980 CG LEU A 162 14124 19356 9007 -1440 2424 -3185 C
ATOM 981 CD1 LEU A 162 -22.425 -4.203 108.449 1.00110.85 C
ANISOU 981 CD1 LEU A 162 13880 19299 8940 -964 2263 -3159 C
ATOM 982 CD2 LEU A 162 -23.410 -6.496 108.378 1.00105.94 C
ANISOU 982 CD2 LEU A 162 13006 19005 8239 -1670 2596 -3387 C
ATOM 983 N GLY A 163 -18.164 -6.782 110.501 1.00103.50 N
ANISOU 983 N GLY A 163 14303 16743 8279 -1775 1918 -2401 N
ATOM 984 CA GLY A 163 -17.283 -7.649 111.262 1.00 86.68 C
ANISOU 984 CA GLY A 163 12528 14276 6133 -1988 1883 -2227 C
ATOM 985 C GLY A 163 -16.593 -6.915 112.392 1.00115.06 C
ANISOU 985 C GLY A 163 16432 17644 9642 -1875 1748 -2122 C
ATOM 986 O GLY A 163 -16.421 -7.464 113.481 1.00118.41 O
ANISOU 986 O GLY A 163 17138 17930 9921 -2044 1809 -2058 O
ATOM 987 N CYS A 164 -16.218 -5.654 112.162 1.00107.42 N
ANISOU 987 N CYS A 164 15429 16641 8746 -1592 1581 -2114 N
ATOM 988 CA CYS A 164 -15.622 -4.868 113.236 1.00103.23 C
ANISOU 988 CA CYS A 164 15176 15923 8122 -1503 1468 -2056 C
ATOM 989 C CYS A 164 -16.624 -4.619 114.357 1.00100.15 C
ANISOU 989 C CYS A 164 14850 15707 7496 -1557 1660 -2194 C
ATOM 990 O CYS A 164 -16.264 -4.676 115.540 1.00119.38 O
ANISOU 990 O CYS A 164 17576 17997 9787 -1643 1644 -2137 O
ATOM 991 CB CYS A 164 -15.081 -3.547 112.687 1.00105.06 C
ANISOU 991 CB CYS A 164 15365 16074 8482 -1213 1295 -2046 C
ATOM 992 SG CYS A 164 -13.683 -3.722 111.549 1.00107.20 S
ANISOU 992 SG CYS A 164 15619 16092 9021 -1156 1053 -1872 S
ATOM 993 N LEU A 165 -17.897 -4.400 114.012 1.00 92.24 N
ANISOU 993 N LEU A 165 13570 15041 6438 -1511 1848 -2381 N
ATOM 994 CA LEU A 165 -18.908 -4.230 115.056 1.00 92.05 C
ANISOU 994 CA LEU A 165 13581 15209 6185 -1576 2053 -2527 C
ATOM 995 C LEU A 165 -19.079 -5.512 115.865 1.00129.10 C
ANISOU 995 C LEU A 165 18453 19858 10743 -1922 2216 -2500 C
ATOM 996 O LEU A 165 -19.062 -5.489 117.106 1.00 94.85 O
ANISOU 996 O LEU A 165 14385 15431 6223 -2004 2270 -2483 O
ATOM 997 CB LEU A 165 -20.243 -3.804 114.441 1.00 93.94 C
ANISOU 997 CB LEU A 165 13439 15866 6386 -1445 2222 -2745 C
ATOM 998 CG LEU A 165 -20.291 -2.531 113.592 1.00 92.52 C
ANISOU 998 CG LEU A 165 13079 15773 6303 -1058 2114 -2782 C
ATOM 999 CD1 LEU A 165 -21.730 -2.080 113.382 1.00104.28 C
ANISOU 999 CD1 LEU A 165 14239 17716 7666 -905 2309 -3010 C
ATOM 1000 CD2 LEU A 165 -19.462 -1.418 114.201 1.00 91.97 C
ANISOU 1000 CD2 LEU A 165 13305 15407 6232 -866 1961 -2691 C
ATOM 1001 N VAL A 166 -19.216 -6.649 115.177 1.00114.29 N
ANISOU 1001 N VAL A 166 16459 18023 8943 -2129 2307 -2493 N
ATOM 1002 CA VAL A 166 -19.415 -7.911 115.884 1.00117.80 C
ANISOU 1002 CA VAL A 166 17107 18398 9254 -2466 2507 -2469 C
ATOM 1003 C VAL A 166 -18.190 -8.271 116.716 1.00117.96 C
ANISOU 1003 C VAL A 166 17558 18030 9233 -2501 2355 -2232 C
ATOM 1004 O VAL A 166 -18.315 -8.860 117.797 1.00120.50 O
ANISOU 1004 O VAL A 166 18160 18265 9358 -2681 2498 -2197 O
ATOM 1005 CB VAL A 166 -19.772 -9.024 114.878 1.00112.95 C
ANISOU 1005 CB VAL A 166 16287 17886 8742 -2685 2648 -2523 C
ATOM 1006 CG1 VAL A 166 -19.873 -10.373 115.576 1.00117.02 C
ANISOU 1006 CG1 VAL A 166 17080 18258 9125 -3042 2879 -2479 C
ATOM 1007 CG2 VAL A 166 -21.077 -8.692 114.173 1.00113.61 C
ANISOU 1007 CG2 VAL A 166 15920 18429 8816 -2660 2809 -2790 C
ATOM 1008 N VAL A 167 -16.994 -7.906 116.251 1.00122.71 N
ANISOU 1008 N VAL A 167 18216 18409 9998 -2318 2069 -2072 N
ATOM 1009 CA VAL A 167 -15.783 -8.241 116.992 1.00119.13 C
ANISOU 1009 CA VAL A 167 18129 17640 9497 -2324 1901 -1858 C
ATOM 1010 C VAL A 167 -15.589 -7.316 118.192 1.00114.13 C
ANISOU 1010 C VAL A 167 17703 16969 8692 -2211 1818 -1866 C
ATOM 1011 O VAL A 167 -15.087 -7.747 119.237 1.00 93.95 O
ANISOU 1011 O VAL A 167 15474 14255 5967 -2284 1796 -1750 O
ATOM 1012 CB VAL A 167 -14.573 -8.221 116.043 1.00 89.28 C
ANISOU 1012 CB VAL A 167 14303 13670 5950 -2189 1635 -1707 C
ATOM 1013 CG1 VAL A 167 -13.290 -8.237 116.825 1.00 89.15 C
ANISOU 1013 CG1 VAL A 167 14603 13396 5873 -2126 1415 -1520 C
ATOM 1014 CG2 VAL A 167 -14.621 -9.427 115.116 1.00 88.76 C
ANISOU 1014 CG2 VAL A 167 14144 13576 6005 -2349 1735 -1662 C
ATOM 1015 N SER A 168 -15.996 -6.053 118.085 1.00106.82 N
ANISOU 1015 N SER A 168 16610 16189 7788 -2026 1783 -2004 N
ATOM 1016 CA SER A 168 -15.926 -5.144 119.220 1.00102.92 C
ANISOU 1016 CA SER A 168 16311 15671 7123 -1937 1740 -2044 C
ATOM 1017 C SER A 168 -17.102 -5.307 120.171 1.00103.43 C
ANISOU 1017 C SER A 168 16431 15920 6949 -2072 2015 -2179 C
ATOM 1018 O SER A 168 -17.125 -4.647 121.213 1.00 97.63 O
ANISOU 1018 O SER A 168 15880 15172 6042 -2022 2010 -2220 O
ATOM 1019 CB SER A 168 -15.842 -3.696 118.736 1.00 92.72 C
ANISOU 1019 CB SER A 168 14868 14417 5946 -1675 1617 -2133 C
ATOM 1020 OG SER A 168 -14.743 -3.510 117.859 1.00 90.48 O
ANISOU 1020 OG SER A 168 14540 13958 5881 -1567 1381 -2018 O
ATOM 1021 N ALA A 169 -18.056 -6.179 119.839 1.00110.67 N
ANISOU 1021 N ALA A 169 17194 17010 7846 -2258 2263 -2262 N
ATOM 1022 CA ALA A 169 -19.193 -6.429 120.725 1.00110.63 C
ANISOU 1022 CA ALA A 169 17231 17192 7611 -2426 2555 -2403 C
ATOM 1023 C ALA A 169 -18.813 -6.711 122.179 1.00120.09 C
ANISOU 1023 C ALA A 169 18850 18214 8567 -2527 2575 -2303 C
ATOM 1024 O ALA A 169 -19.507 -6.192 123.069 1.00127.54 O
ANISOU 1024 O ALA A 169 19851 19288 9320 -2528 2712 -2427 O
ATOM 1025 CB ALA A 169 -20.037 -7.589 120.168 1.00113.83 C
ANISOU 1025 CB ALA A 169 17461 17756 8033 -2688 2819 -2486 C
ATOM 1026 N PRO A 170 -17.792 -7.513 122.502 1.00123.29 N
ANISOU 1026 N PRO A 170 19556 18348 8943 -2597 2459 -2089 N
ATOM 1027 CA PRO A 170 -17.455 -7.704 123.929 1.00103.37 C
ANISOU 1027 CA PRO A 170 17435 15690 6150 -2651 2470 -1996 C
ATOM 1028 C PRO A 170 -17.113 -6.414 124.657 1.00107.05 C
ANISOU 1028 C PRO A 170 17982 16163 6528 -2456 2293 -2044 C
ATOM 1029 O PRO A 170 -17.276 -6.348 125.887 1.00108.01 O
ANISOU 1029 O PRO A 170 18365 16281 6392 -2505 2373 -2055 O
ATOM 1030 CB PRO A 170 -16.246 -8.655 123.874 1.00102.69 C
ANISOU 1030 CB PRO A 170 17599 15330 6090 -2667 2309 -1744 C
ATOM 1031 CG PRO A 170 -16.421 -9.397 122.612 1.00116.39 C
ANISOU 1031 CG PRO A 170 19107 17071 8045 -2759 2385 -1738 C
ATOM 1032 CD PRO A 170 -17.006 -8.413 121.642 1.00122.03 C
ANISOU 1032 CD PRO A 170 19397 18011 8957 -2640 2354 -1925 C
ATOM 1033 N GLN A 171 -16.613 -5.405 123.939 1.00108.33 N
ANISOU 1033 N GLN A 171 17952 16319 6889 -2246 2068 -2074 N
ATOM 1034 CA GLN A 171 -16.142 -4.181 124.577 1.00109.68 C
ANISOU 1034 CA GLN A 171 18232 16452 6991 -2081 1898 -2122 C
ATOM 1035 C GLN A 171 -17.237 -3.485 125.377 1.00117.35 C
ANISOU 1035 C GLN A 171 19210 17604 7773 -2076 2110 -2312 C
ATOM 1036 O GLN A 171 -16.946 -2.869 126.410 1.00116.16 O
ANISOU 1036 O GLN A 171 19287 17406 7443 -2033 2047 -2336 O
ATOM 1037 CB GLN A 171 -15.583 -3.223 123.524 1.00104.32 C
ANISOU 1037 CB GLN A 171 17334 15732 6572 -1879 1690 -2146 C
ATOM 1038 CG GLN A 171 -14.760 -2.070 124.076 1.00104.43 C
ANISOU 1038 CG GLN A 171 17499 15636 6544 -1743 1483 -2172 C
ATOM 1039 CD GLN A 171 -13.309 -2.447 124.312 1.00105.38 C
ANISOU 1039 CD GLN A 171 17807 15567 6666 -1761 1211 -2003 C
ATOM 1040 OE1 GLN A 171 -12.965 -3.627 124.398 1.00 99.24 O
ANISOU 1040 OE1 GLN A 171 17132 14729 5846 -1864 1197 -1847 O
ATOM 1041 NE2 GLN A 171 -12.446 -1.442 124.408 1.00111.63 N
ANISOU 1041 NE2 GLN A 171 18645 16271 7499 -1656 1005 -2042 N
ATOM 1042 N VAL A 172 -18.492 -3.566 124.928 1.00120.94 N
ANISOU 1042 N VAL A 172 19409 18289 8254 -2118 2361 -2461 N
ATOM 1043 CA VAL A 172 -19.565 -2.890 125.654 1.00121.32 C
ANISOU 1043 CA VAL A 172 19436 18537 8123 -2093 2571 -2652 C
ATOM 1044 C VAL A 172 -19.776 -3.513 127.030 1.00122.26 C
ANISOU 1044 C VAL A 172 19878 18630 7947 -2289 2726 -2625 C
ATOM 1045 O VAL A 172 -20.125 -2.813 127.988 1.00123.43 O
ANISOU 1045 O VAL A 172 20138 18823 7937 -2229 2782 -2715 O
ATOM 1046 CB VAL A 172 -20.861 -2.892 124.818 1.00119.52 C
ANISOU 1046 CB VAL A 172 18817 18615 7978 -2084 2800 -2829 C
ATOM 1047 CG1 VAL A 172 -21.325 -4.303 124.546 1.00114.69 C
ANISOU 1047 CG1 VAL A 172 18140 18077 7362 -2362 2995 -2806 C
ATOM 1048 CG2 VAL A 172 -21.957 -2.115 125.522 1.00125.31 C
ANISOU 1048 CG2 VAL A 172 19501 19580 8531 -2015 3010 -3035 C
ATOM 1049 N HIS A 173 -19.557 -4.824 127.163 1.00124.64 N
ANISOU 1049 N HIS A 173 20337 18827 8192 -2499 2794 -2485 N
ATOM 1050 CA HIS A 173 -19.743 -5.479 128.453 1.00131.75 C
ANISOU 1050 CA HIS A 173 21522 19649 8887 -2632 2924 -2408 C
ATOM 1051 C HIS A 173 -18.491 -5.369 129.313 1.00136.23 C
ANISOU 1051 C HIS A 173 22465 20004 9292 -2561 2678 -2246 C
ATOM 1052 O HIS A 173 -18.592 -5.159 130.528 1.00138.72 O
ANISOU 1052 O HIS A 173 22977 20303 9428 -2545 2707 -2245 O
ATOM 1053 CB HIS A 173 -20.114 -6.949 128.253 1.00132.47 C
ANISOU 1053 CB HIS A 173 21638 19694 9001 -2871 3137 -2322 C
ATOM 1054 CG HIS A 173 -20.114 -7.749 129.520 1.00132.11 C
ANISOU 1054 CG HIS A 173 21943 19503 8751 -2993 3257 -2196 C
ATOM 1055 ND1 HIS A 173 -18.972 -8.313 130.046 1.00130.07 N
ANISOU 1055 ND1 HIS A 173 22060 19002 8357 -2970 3095 -1968 N
ATOM 1056 CD2 HIS A 173 -21.120 -8.082 130.363 1.00131.46 C
ANISOU 1056 CD2 HIS A 173 21893 19488 8569 -3124 3526 -2263 C
ATOM 1057 CE1 HIS A 173 -19.273 -8.957 131.160 1.00129.04 C
ANISOU 1057 CE1 HIS A 173 22192 18791 8046 -3067 3263 -1894 C
ATOM 1058 NE2 HIS A 173 -20.571 -8.833 131.374 1.00131.67 N
ANISOU 1058 NE2 HIS A 173 22330 19298 8402 -3178 3531 -2072 N
ATOM 1059 N ILE A 174 -17.310 -5.507 128.703 1.00135.67 N
ANISOU 1059 N ILE A 174 22456 19782 9311 -2496 2418 -2106 N
ATOM 1060 CA ILE A 174 -16.081 -5.579 129.494 1.00132.81 C
ANISOU 1060 CA ILE A 174 22416 19250 8794 -2427 2171 -1943 C
ATOM 1061 C ILE A 174 -15.808 -4.272 130.237 1.00133.89 C
ANISOU 1061 C ILE A 174 22618 19429 8827 -2292 2020 -2060 C
ATOM 1062 O ILE A 174 -15.246 -4.288 131.340 1.00139.88 O
ANISOU 1062 O ILE A 174 23645 20129 9373 -2266 1909 -1988 O
ATOM 1063 CB ILE A 174 -14.897 -5.993 128.601 1.00124.18 C
ANISOU 1063 CB ILE A 174 21272 18000 7912 -2346 1902 -1765 C
ATOM 1064 CG1 ILE A 174 -13.648 -6.216 129.456 1.00112.86 C
ANISOU 1064 CG1 ILE A 174 20153 16444 6286 -2265 1651 -1600 C
ATOM 1065 CG2 ILE A 174 -14.639 -4.943 127.541 1.00125.39 C
ANISOU 1065 CG2 ILE A 174 21094 18184 8366 -2200 1728 -1861 C
ATOM 1066 CD1 ILE A 174 -12.533 -6.912 128.731 1.00107.59 C
ANISOU 1066 CD1 ILE A 174 19381 15674 5826 -2132 1324 -1487 C
ATOM 1067 N PHE A 175 -16.202 -3.133 129.672 1.00129.45 N
ANISOU 1067 N PHE A 175 21795 18957 8433 -2182 2014 -2235 N
ATOM 1068 CA PHE A 175 -16.011 -1.841 130.319 1.00123.40 C
ANISOU 1068 CA PHE A 175 21103 18207 7578 -2065 1913 -2369 C
ATOM 1069 C PHE A 175 -17.304 -1.360 130.965 1.00117.67 C
ANISOU 1069 C PHE A 175 20322 17632 6754 -2062 2180 -2534 C
ATOM 1070 O PHE A 175 -18.394 -1.552 130.419 1.00112.73 O
ANISOU 1070 O PHE A 175 19461 17149 6223 -2089 2409 -2618 O
ATOM 1071 CB PHE A 175 -15.510 -0.805 129.308 1.00124.49 C
ANISOU 1071 CB PHE A 175 21014 18293 7993 -1899 1728 -2433 C
ATOM 1072 CG PHE A 175 -14.020 -0.829 129.105 1.00126.22 C
ANISOU 1072 CG PHE A 175 21304 18354 8298 -1858 1400 -2304 C
ATOM 1073 CD1 PHE A 175 -13.395 -1.968 128.630 1.00121.83 C
ANISOU 1073 CD1 PHE A 175 20744 17721 7825 -1909 1296 -2108 C
ATOM 1074 CD2 PHE A 175 -13.246 0.285 129.384 1.00129.82 C
ANISOU 1074 CD2 PHE A 175 21830 18747 8749 -1776 1211 -2394 C
ATOM 1075 CE1 PHE A 175 -12.029 -2.002 128.441 1.00117.32 C
ANISOU 1075 CE1 PHE A 175 20212 17038 7326 -1856 996 -1997 C
ATOM 1076 CE2 PHE A 175 -11.874 0.258 129.197 1.00130.71 C
ANISOU 1076 CE2 PHE A 175 21974 18756 8936 -1758 916 -2301 C
ATOM 1077 CZ PHE A 175 -11.266 -0.888 128.722 1.00122.79 C
ANISOU 1077 CZ PHE A 175 20940 17702 8011 -1786 801 -2100 C
ATOM 1078 N SER A 176 -17.171 -0.725 132.128 1.00118.96 N
ANISOU 1078 N SER A 176 20667 17778 6753 -2013 2136 -2584 N
ATOM 1079 CA SER A 176 -18.323 -0.269 132.893 1.00127.14 C
ANISOU 1079 CA SER A 176 21668 18941 7698 -1991 2368 -2723 C
ATOM 1080 C SER A 176 -17.901 0.888 133.788 1.00128.14 C
ANISOU 1080 C SER A 176 21955 19024 7709 -1887 2248 -2821 C
ATOM 1081 O SER A 176 -16.720 1.053 134.107 1.00131.06 O
ANISOU 1081 O SER A 176 22499 19280 8018 -1881 1996 -2759 O
ATOM 1082 CB SER A 176 -18.929 -1.406 133.728 1.00132.28 C
ANISOU 1082 CB SER A 176 22434 19625 8202 -2143 2563 -2629 C
ATOM 1083 OG SER A 176 -17.949 -2.052 134.525 1.00137.44 O
ANISOU 1083 OG SER A 176 23388 20145 8687 -2193 2401 -2453 O
ATOM 1084 N LEU A 177 -18.882 1.694 134.186 1.00134.93 N
ANISOU 1084 N LEU A 177 22742 19989 8536 -1804 2434 -2988 N
ATOM 1085 CA LEU A 177 -18.606 2.804 135.088 1.00139.35 C
ANISOU 1085 CA LEU A 177 23462 20505 8979 -1718 2364 -3101 C
ATOM 1086 C LEU A 177 -18.136 2.288 136.441 1.00138.95 C
ANISOU 1086 C LEU A 177 23677 20422 8695 -1816 2287 -3006 C
ATOM 1087 O LEU A 177 -18.620 1.267 136.937 1.00124.78 O
ANISOU 1087 O LEU A 177 21938 18677 6796 -1921 2424 -2904 O
ATOM 1088 CB LEU A 177 -19.847 3.675 135.270 1.00135.88 C
ANISOU 1088 CB LEU A 177 22900 20193 8537 -1594 2607 -3287 C
ATOM 1089 CG LEU A 177 -19.883 4.990 134.492 1.00121.86 C
ANISOU 1089 CG LEU A 177 21019 18383 6898 -1398 2602 -3439 C
ATOM 1090 CD1 LEU A 177 -21.075 5.816 134.933 1.00124.04 C
ANISOU 1090 CD1 LEU A 177 21228 18787 7114 -1248 2841 -3607 C
ATOM 1091 CD2 LEU A 177 -18.590 5.763 134.684 1.00121.47 C
ANISOU 1091 CD2 LEU A 177 21171 18140 6841 -1390 2355 -3459 C
ATOM 1092 N ARG A 178 -17.187 3.006 137.040 1.00129.82 N
ANISOU 1092 N ARG A 178 22687 19188 7450 -1783 2078 -3047 N
ATOM 1093 CA ARG A 178 -16.681 2.653 138.357 1.00138.91 C
ANISOU 1093 CA ARG A 178 24080 20342 8356 -1841 1982 -2977 C
ATOM 1094 C ARG A 178 -16.208 3.919 139.054 1.00145.53 C
ANISOU 1094 C ARG A 178 25023 21158 9113 -1784 1870 -3143 C
ATOM 1095 O ARG A 178 -15.683 4.838 138.418 1.00146.24 O
ANISOU 1095 O ARG A 178 25052 21170 9343 -1732 1757 -3251 O
ATOM 1096 CB ARG A 178 -15.537 1.637 138.274 1.00143.75 C
ANISOU 1096 CB ARG A 178 24801 20900 8919 -1898 1749 -2771 C
ATOM 1097 N GLU A 179 -16.393 3.953 140.370 1.00153.05 N
ANISOU 1097 N GLU A 179 26146 22171 9836 -1805 1915 -3168 N
ATOM 1098 CA GLU A 179 -16.051 5.120 141.170 1.00153.03 C
ANISOU 1098 CA GLU A 179 26252 22160 9731 -1772 1842 -3343 C
ATOM 1099 C GLU A 179 -14.623 5.019 141.693 1.00156.45 C
ANISOU 1099 C GLU A 179 26822 22592 10031 -1814 1528 -3297 C
ATOM 1100 O GLU A 179 -14.222 3.991 142.244 1.00155.53 O
ANISOU 1100 O GLU A 179 26817 22534 9745 -1845 1435 -3126 O
ATOM 1101 CB GLU A 179 -17.026 5.264 142.336 1.00152.23 C
ANISOU 1101 CB GLU A 179 26252 22148 9442 -1768 2059 -3413 C
ATOM 1102 CG GLU A 179 -16.668 6.359 143.320 1.00161.01 C
ANISOU 1102 CG GLU A 179 27506 23259 10411 -1750 1991 -3588 C
ATOM 1103 CD GLU A 179 -17.656 6.448 144.474 1.00166.30 C
ANISOU 1103 CD GLU A 179 28278 24020 10890 -1744 2212 -3649 C
ATOM 1104 OE1 GLU A 179 -18.711 7.099 144.311 1.00168.21 O
ANISOU 1104 OE1 GLU A 179 28428 24274 11209 -1670 2447 -3778 O
ATOM 1105 OE2 GLU A 179 -17.376 5.858 145.542 1.00167.05 O
ANISOU 1105 OE2 GLU A 179 28544 24183 10746 -1798 2153 -3566 O
ATOM 1106 N VAL A 180 -13.869 6.100 141.533 1.00161.76 N
ANISOU 1106 N VAL A 180 27486 23205 10769 -1808 1377 -3456 N
ATOM 1107 CA VAL A 180 -12.501 6.180 142.023 1.00165.04 C
ANISOU 1107 CA VAL A 180 27986 23661 11062 -1853 1075 -3468 C
ATOM 1108 C VAL A 180 -12.423 6.898 143.367 1.00166.58 C
ANISOU 1108 C VAL A 180 28333 23932 11029 -1871 1067 -3626 C
ATOM 1109 O VAL A 180 -11.620 6.524 144.223 1.00172.36 O
ANISOU 1109 O VAL A 180 29164 24785 11538 -1891 869 -3584 O
ATOM 1110 CB VAL A 180 -11.608 6.866 140.968 1.00163.55 C
ANISOU 1110 CB VAL A 180 27681 23366 11093 -1873 908 -3559 C
ATOM 1111 CG1 VAL A 180 -10.214 7.125 141.524 1.00166.33 C
ANISOU 1111 CG1 VAL A 180 28085 23795 11317 -1935 606 -3630 C
ATOM 1112 CG2 VAL A 180 -11.533 6.009 139.720 1.00155.58 C
ANISOU 1112 CG2 VAL A 180 26535 22306 10274 -1857 876 -3381 C
ATOM 1113 N ALA A 181 -13.268 7.919 143.561 1.00171.56 N
ANISOU 1113 N ALA A 181 28984 24506 11695 -1848 1283 -3810 N
ATOM 1114 CA ALA A 181 -13.199 8.694 144.821 1.00178.87 C
ANISOU 1114 CA ALA A 181 30053 25479 12429 -1877 1268 -3992 C
ATOM 1115 C ALA A 181 -14.505 9.399 145.218 1.00183.14 C
ANISOU 1115 C ALA A 181 30637 25985 12963 -1820 1576 -4121 C
ATOM 1116 O ALA A 181 -14.539 10.626 145.202 1.00185.47 O
ANISOU 1116 O ALA A 181 30960 26179 13329 -1808 1652 -4328 O
ATOM 1117 CB ALA A 181 -12.065 9.673 144.718 1.00183.58 C
ANISOU 1117 CB ALA A 181 30640 26006 13106 -1943 1081 -4180 C
ATOM 1118 N ASP A 182 -15.515 8.645 145.639 1.00182.90 N
ANISOU 1118 N ASP A 182 30620 26037 12838 -1786 1764 -4003 N
ATOM 1119 CA ASP A 182 -16.768 9.227 146.198 1.00181.70 C
ANISOU 1119 CA ASP A 182 30507 25906 12626 -1730 2047 -4114 C
ATOM 1120 C ASP A 182 -17.420 10.255 145.281 1.00182.59 C
ANISOU 1120 C ASP A 182 30514 25900 12963 -1630 2223 -4270 C
ATOM 1121 O ASP A 182 -17.430 11.438 145.652 1.00172.91 O
ANISOU 1121 O ASP A 182 29374 24592 11733 -1612 2248 -4466 O
ATOM 1122 CB ASP A 182 -16.560 9.843 147.582 1.00174.76 C
ANISOU 1122 CB ASP A 182 29820 25094 11486 -1770 2006 -4239 C
ATOM 1123 CG ASP A 182 -17.813 9.777 148.436 1.00174.84 C
ANISOU 1123 CG ASP A 182 29896 25181 11355 -1730 2279 -4271 C
ATOM 1124 OD1 ASP A 182 -18.335 10.840 148.796 1.00176.22 O
ANISOU 1124 OD1 ASP A 182 30026 25304 11627 -1648 2498 -4418 O
ATOM 1125 OD2 ASP A 182 -18.256 8.662 148.724 1.00176.06 O
ANISOU 1125 OD2 ASP A 182 30151 25449 11295 -1769 2282 -4145 O
ATOM 1126 N GLY A 183 -17.911 9.814 144.126 1.00186.55 N
ANISOU 1126 N GLY A 183 30837 26397 13648 -1557 2355 -4186 N
ATOM 1127 CA GLY A 183 -18.598 10.712 143.177 1.00174.69 C
ANISOU 1127 CA GLY A 183 29215 24809 12351 -1417 2519 -4304 C
ATOM 1128 C GLY A 183 -17.802 10.834 141.898 1.00157.85 C
ANISOU 1128 C GLY A 183 26993 22542 10443 -1406 2372 -4284 C
ATOM 1129 O GLY A 183 -18.384 11.148 140.852 1.00158.00 O
ANISOU 1129 O GLY A 183 26890 22502 10640 -1265 2513 -4336 O
ATOM 1130 N VAL A 184 -16.492 10.645 142.001 1.00157.83 N
ANISOU 1130 N VAL A 184 27039 22503 10425 -1535 2096 -4212 N
ATOM 1131 CA VAL A 184 -15.678 10.677 140.792 1.00134.83 C
ANISOU 1131 CA VAL A 184 24033 19476 7720 -1546 1942 -4173 C
ATOM 1132 C VAL A 184 -15.825 9.333 140.089 1.00149.64 C
ANISOU 1132 C VAL A 184 25761 21432 9664 -1560 1906 -3953 C
ATOM 1133 O VAL A 184 -15.542 8.285 140.676 1.00146.12 O
ANISOU 1133 O VAL A 184 25363 21084 9072 -1648 1801 -3807 O
ATOM 1134 CB VAL A 184 -14.207 10.972 141.122 1.00135.46 C
ANISOU 1134 CB VAL A 184 24217 19503 7750 -1681 1661 -4230 C
ATOM 1135 CG1 VAL A 184 -13.324 10.723 139.909 1.00133.59 C
ANISOU 1135 CG1 VAL A 184 23866 19181 7711 -1713 1482 -4154 C
ATOM 1136 CG2 VAL A 184 -14.054 12.402 141.627 1.00137.79 C
ANISOU 1136 CG2 VAL A 184 24651 19685 8020 -1688 1726 -4475 C
ATOM 1137 N PHE A 185 -16.268 9.359 138.835 1.00146.33 N
ANISOU 1137 N PHE A 185 25175 20968 9456 -1466 2003 -3930 N
ATOM 1138 CA PHE A 185 -16.491 8.146 138.064 1.00143.53 C
ANISOU 1138 CA PHE A 185 24665 20685 9185 -1486 2000 -3744 C
ATOM 1139 C PHE A 185 -15.575 8.107 136.850 1.00151.50 C
ANISOU 1139 C PHE A 185 25591 21583 10390 -1498 1819 -3691 C
ATOM 1140 O PHE A 185 -15.142 9.147 136.345 1.00145.16 O
ANISOU 1140 O PHE A 185 24807 20642 9704 -1447 1787 -3816 O
ATOM 1141 CB PHE A 185 -17.947 8.039 137.589 1.00137.71 C
ANISOU 1141 CB PHE A 185 23752 20055 8516 -1366 2287 -3762 C
ATOM 1142 CG PHE A 185 -18.939 7.854 138.698 1.00140.86 C
ANISOU 1142 CG PHE A 185 24197 20589 8732 -1369 2481 -3793 C
ATOM 1143 CD1 PHE A 185 -18.857 6.761 139.544 1.00143.82 C
ANISOU 1143 CD1 PHE A 185 24666 21039 8940 -1509 2446 -3658 C
ATOM 1144 CD2 PHE A 185 -19.968 8.762 138.880 1.00140.96 C
ANISOU 1144 CD2 PHE A 185 24170 20655 8736 -1218 2711 -3953 C
ATOM 1145 CE1 PHE A 185 -19.774 6.585 140.560 1.00133.84 C
ANISOU 1145 CE1 PHE A 185 23457 19889 7508 -1522 2640 -3688 C
ATOM 1146 CE2 PHE A 185 -20.889 8.591 139.893 1.00141.41 C
ANISOU 1146 CE2 PHE A 185 24260 20844 8625 -1224 2893 -3988 C
ATOM 1147 CZ PHE A 185 -20.792 7.501 140.734 1.00139.03 C
ANISOU 1147 CZ PHE A 185 24053 20607 8163 -1388 2860 -3857 C
ATOM 1148 N ASP A 186 -15.291 6.894 136.378 1.00166.25 N
ANISOU 1148 N ASP A 186 27380 23496 12292 -1569 1719 -3504 N
ATOM 1149 CA ASP A 186 -14.680 6.741 135.066 1.00172.80 C
ANISOU 1149 CA ASP A 186 28090 24241 13325 -1563 1597 -3441 C
ATOM 1150 C ASP A 186 -15.029 5.374 134.498 1.00169.18 C
ANISOU 1150 C ASP A 186 27506 23866 12910 -1606 1632 -3253 C
ATOM 1151 O ASP A 186 -15.429 4.458 135.225 1.00168.73 O
ANISOU 1151 O ASP A 186 27500 23902 12707 -1674 1699 -3151 O
ATOM 1152 CB ASP A 186 -13.155 6.959 135.100 1.00182.44 C
ANISOU 1152 CB ASP A 186 29402 25368 14549 -1650 1296 -3442 C
ATOM 1153 CG ASP A 186 -12.407 5.875 135.864 1.00192.72 C
ANISOU 1153 CG ASP A 186 30792 26758 15676 -1752 1093 -3284 C
ATOM 1154 OD1 ASP A 186 -13.051 5.003 136.484 1.00197.29 O
ANISOU 1154 OD1 ASP A 186 31411 27433 16116 -1766 1202 -3173 O
ATOM 1155 OD2 ASP A 186 -11.154 5.906 135.843 1.00196.02 O
ANISOU 1155 OD2 ASP A 186 31239 27151 16088 -1810 831 -3274 O
ATOM 1156 N CYS A 187 -14.894 5.255 133.180 1.00157.09 N
ANISOU 1156 N CYS A 187 25820 22288 11578 -1572 1607 -3214 N
ATOM 1157 CA CYS A 187 -14.943 3.942 132.558 1.00145.03 C
ANISOU 1157 CA CYS A 187 24188 20811 10106 -1643 1596 -3036 C
ATOM 1158 C CYS A 187 -13.814 3.090 133.112 1.00144.17 C
ANISOU 1158 C CYS A 187 24233 20669 9878 -1751 1353 -2875 C
ATOM 1159 O CYS A 187 -12.698 3.574 133.314 1.00141.05 O
ANISOU 1159 O CYS A 187 23927 20205 9461 -1762 1120 -2905 O
ATOM 1160 CB CYS A 187 -14.786 4.058 131.045 1.00139.96 C
ANISOU 1160 CB CYS A 187 23339 20112 9727 -1572 1560 -3019 C
ATOM 1161 SG CYS A 187 -16.139 4.788 130.140 1.00138.14 S
ANISOU 1161 SG CYS A 187 22856 19967 9665 -1382 1833 -3152 S
ATOM 1162 N TRP A 188 -14.092 1.811 133.348 1.00148.26 N
ANISOU 1162 N TRP A 188 24779 21242 10313 -1826 1416 -2710 N
ATOM 1163 CA TRP A 188 -13.018 0.922 133.761 1.00150.25 C
ANISOU 1163 CA TRP A 188 25183 21460 10444 -1879 1193 -2532 C
ATOM 1164 C TRP A 188 -13.300 -0.493 133.283 1.00142.83 C
ANISOU 1164 C TRP A 188 24224 20516 9530 -1946 1289 -2340 C
ATOM 1165 O TRP A 188 -14.454 -0.919 133.190 1.00143.81 O
ANISOU 1165 O TRP A 188 24270 20697 9676 -1993 1561 -2351 O
ATOM 1166 CB TRP A 188 -12.812 0.933 135.280 1.00159.41 C
ANISOU 1166 CB TRP A 188 26559 22671 11339 -1886 1147 -2528 C
ATOM 1167 CG TRP A 188 -11.358 0.827 135.637 1.00167.17 C
ANISOU 1167 CG TRP A 188 27652 23647 12219 -1872 819 -2456 C
ATOM 1168 CD1 TRP A 188 -10.467 -0.094 135.165 1.00167.27 C
ANISOU 1168 CD1 TRP A 188 27678 23631 12245 -1867 632 -2271 C
ATOM 1169 CD2 TRP A 188 -10.622 1.680 136.522 1.00172.68 C
ANISOU 1169 CD2 TRP A 188 28437 24392 12781 -1855 640 -2582 C
ATOM 1170 NE1 TRP A 188 -9.225 0.129 135.704 1.00171.46 N
ANISOU 1170 NE1 TRP A 188 28279 24215 12652 -1831 337 -2274 N
ATOM 1171 CE2 TRP A 188 -9.293 1.211 136.542 1.00175.40 C
ANISOU 1171 CE2 TRP A 188 28817 24769 13058 -1837 337 -2472 C
ATOM 1172 CE3 TRP A 188 -10.958 2.791 137.302 1.00174.49 C
ANISOU 1172 CE3 TRP A 188 28713 24652 12935 -1853 711 -2785 C
ATOM 1173 CZ2 TRP A 188 -8.300 1.815 137.312 1.00177.04 C
ANISOU 1173 CZ2 TRP A 188 29075 25069 13123 -1830 101 -2576 C
ATOM 1174 CZ3 TRP A 188 -9.970 3.389 138.063 1.00175.78 C
ANISOU 1174 CZ3 TRP A 188 28953 24873 12962 -1861 488 -2885 C
ATOM 1175 CH2 TRP A 188 -8.658 2.900 138.063 1.00176.21 C
ANISOU 1175 CH2 TRP A 188 29013 24989 12950 -1856 185 -2788 C
ATOM 1176 N ALA A 189 -12.225 -1.212 132.976 1.00138.48 N
ANISOU 1176 N ALA A 189 23738 19901 8975 -1951 1069 -2175 N
ATOM 1177 CA ALA A 189 -12.318 -2.593 132.535 1.00123.54 C
ANISOU 1177 CA ALA A 189 21876 17967 7098 -2009 1147 -1977 C
ATOM 1178 C ALA A 189 -12.431 -3.533 133.726 1.00122.57 C
ANISOU 1178 C ALA A 189 22003 17844 6724 -2034 1229 -1832 C
ATOM 1179 O ALA A 189 -11.764 -3.346 134.747 1.00118.01 O
ANISOU 1179 O ALA A 189 21595 17296 5948 -1970 1063 -1807 O
ATOM 1180 CB ALA A 189 -11.095 -2.967 131.694 1.00116.31 C
ANISOU 1180 CB ALA A 189 20862 16960 6369 -1941 868 -1833 C
ATOM 1181 N VAL A 190 -13.262 -4.559 133.580 1.00125.43 N
ANISOU 1181 N VAL A 190 22388 18179 7092 -2131 1492 -1741 N
ATOM 1182 CA VAL A 190 -13.353 -5.635 134.556 1.00134.36 C
ANISOU 1182 CA VAL A 190 23788 19263 8001 -2162 1604 -1571 C
ATOM 1183 C VAL A 190 -13.154 -6.955 133.824 1.00131.71 C
ANISOU 1183 C VAL A 190 23515 18800 7728 -2216 1669 -1372 C
ATOM 1184 O VAL A 190 -13.680 -7.150 132.722 1.00116.30 O
ANISOU 1184 O VAL A 190 21361 16839 5988 -2310 1806 -1421 O
ATOM 1185 CB VAL A 190 -14.700 -5.608 135.316 1.00121.24 C
ANISOU 1185 CB VAL A 190 22140 17669 6258 -2258 1930 -1674 C
ATOM 1186 CG1 VAL A 190 -14.875 -4.280 136.039 1.00122.15 C
ANISOU 1186 CG1 VAL A 190 22211 17895 6307 -2188 1871 -1869 C
ATOM 1187 CG2 VAL A 190 -15.864 -5.831 134.368 1.00126.77 C
ANISOU 1187 CG2 VAL A 190 22592 18408 7165 -2390 2214 -1772 C
ATOM 1188 N PHE A 191 -12.379 -7.853 134.426 1.00134.31 N
ANISOU 1188 N PHE A 191 24124 19039 7870 -2141 1572 -1152 N
ATOM 1189 CA PHE A 191 -12.033 -9.121 133.804 1.00132.47 C
ANISOU 1189 CA PHE A 191 24005 18652 7676 -2156 1618 -940 C
ATOM 1190 C PHE A 191 -12.514 -10.277 134.668 1.00130.08 C
ANISOU 1190 C PHE A 191 24003 18238 7183 -2210 1883 -784 C
ATOM 1191 O PHE A 191 -12.607 -10.161 135.893 1.00138.08 O
ANISOU 1191 O PHE A 191 25197 19295 7973 -2159 1902 -772 O
ATOM 1192 CB PHE A 191 -10.524 -9.224 133.565 1.00118.77 C
ANISOU 1192 CB PHE A 191 22336 16886 5905 -1970 1248 -790 C
ATOM 1193 CG PHE A 191 -10.022 -8.321 132.474 1.00115.55 C
ANISOU 1193 CG PHE A 191 21630 16535 5739 -1948 1019 -918 C
ATOM 1194 CD1 PHE A 191 -10.262 -8.623 131.143 1.00126.94 C
ANISOU 1194 CD1 PHE A 191 22806 17899 7527 -2003 1092 -911 C
ATOM 1195 CD2 PHE A 191 -9.305 -7.175 132.777 1.00115.34 C
ANISOU 1195 CD2 PHE A 191 21502 16626 5698 -1848 731 -1043 C
ATOM 1196 CE1 PHE A 191 -9.794 -7.803 130.137 1.00115.16 C
ANISOU 1196 CE1 PHE A 191 20966 16436 6353 -1940 880 -1007 C
ATOM 1197 CE2 PHE A 191 -8.836 -6.347 131.773 1.00130.48 C
ANISOU 1197 CE2 PHE A 191 23079 18556 7940 -1808 537 -1150 C
ATOM 1198 CZ PHE A 191 -9.085 -6.660 130.449 1.00110.02 C
ANISOU 1198 CZ PHE A 191 20237 15877 5687 -1843 612 -1123 C
ATOM 1199 N ILE A 192 -12.825 -11.394 134.006 1.00131.53 N
ANISOU 1199 N ILE A 192 24244 18268 7463 -2322 2102 -670 N
ATOM 1200 CA ILE A 192 -13.545 -12.482 134.662 1.00149.58 C
ANISOU 1200 CA ILE A 192 26788 20421 9626 -2440 2442 -568 C
ATOM 1201 C ILE A 192 -12.706 -13.123 135.761 1.00173.29 C
ANISOU 1201 C ILE A 192 30178 23323 12340 -2243 2331 -327 C
ATOM 1202 O ILE A 192 -13.221 -13.456 136.837 1.00164.02 O
ANISOU 1202 O ILE A 192 29227 22119 10975 -2276 2524 -294 O
ATOM 1203 CB ILE A 192 -13.994 -13.521 133.617 1.00124.61 C
ANISOU 1203 CB ILE A 192 23591 17104 6652 -2620 2700 -521 C
ATOM 1204 CG1 ILE A 192 -15.204 -13.002 132.841 1.00122.94 C
ANISOU 1204 CG1 ILE A 192 22998 17041 6671 -2845 2911 -788 C
ATOM 1205 CG2 ILE A 192 -14.300 -14.860 134.275 1.00128.05 C
ANISOU 1205 CG2 ILE A 192 24391 17318 6942 -2695 2997 -345 C
ATOM 1206 CD1 ILE A 192 -16.420 -12.758 133.701 1.00125.28 C
ANISOU 1206 CD1 ILE A 192 23268 17442 6891 -2985 3182 -945 C
ATOM 1207 N ARG A 193 -11.399 -13.261 135.536 1.00182.27 N
ANISOU 1207 N ARG A 193 31387 24435 13434 -2019 2009 -165 N
ATOM 1208 CA ARG A 193 -10.585 -14.135 136.377 1.00189.95 C
ANISOU 1208 CA ARG A 193 32719 25303 14149 -1802 1929 99 C
ATOM 1209 C ARG A 193 -9.102 -13.877 136.120 1.00190.63 C
ANISOU 1209 C ARG A 193 32754 25475 14200 -1530 1490 203 C
ATOM 1210 O ARG A 193 -8.773 -12.969 135.351 1.00190.78 O
ANISOU 1210 O ARG A 193 32474 25619 14396 -1545 1268 53 O
ATOM 1211 CB ARG A 193 -10.981 -15.587 136.111 1.00194.41 C
ANISOU 1211 CB ARG A 193 33536 25589 14741 -1895 2265 278 C
ATOM 1212 CG ARG A 193 -11.711 -16.236 137.276 1.00200.22 C
ANISOU 1212 CG ARG A 193 34587 26220 15269 -1963 2576 342 C
ATOM 1213 CD ARG A 193 -11.651 -17.745 137.177 1.00201.91 C
ANISOU 1213 CD ARG A 193 35142 26122 15453 -1956 2824 579 C
ATOM 1214 NE ARG A 193 -12.968 -18.344 136.991 1.00201.54 N
ANISOU 1214 NE ARG A 193 35125 25922 15528 -2294 3286 476 N
ATOM 1215 CZ ARG A 193 -13.179 -19.484 136.342 1.00198.47 C
ANISOU 1215 CZ ARG A 193 34880 25268 15263 -2421 3551 570 C
ATOM 1216 NH1 ARG A 193 -12.158 -20.138 135.806 1.00195.02 N
ANISOU 1216 NH1 ARG A 193 34579 24675 14844 -2214 3402 784 N
ATOM 1217 NH2 ARG A 193 -14.409 -19.962 136.220 1.00198.96 N
ANISOU 1217 NH2 ARG A 193 34933 25227 15434 -2759 3967 434 N
ATOM 1218 N PRO A 194 -8.168 -14.613 136.757 1.00213.79 N
ANISOU 1218 N PRO A 194 35956 28366 16908 -1268 1347 447 N
ATOM 1219 CA PRO A 194 -6.742 -14.291 136.539 1.00131.69 C
ANISOU 1219 CA PRO A 194 25448 18112 6475 -1003 906 514 C
ATOM 1220 C PRO A 194 -6.308 -14.322 135.086 1.00161.75 C
ANISOU 1220 C PRO A 194 29045 21854 10559 -1027 793 514 C
ATOM 1221 O PRO A 194 -5.448 -13.521 134.695 1.00158.33 O
ANISOU 1221 O PRO A 194 28372 21592 10192 -930 442 426 O
ATOM 1222 CB PRO A 194 -6.013 -15.362 137.375 1.00135.57 C
ANISOU 1222 CB PRO A 194 26281 18539 6691 -717 866 804 C
ATOM 1223 CG PRO A 194 -7.037 -16.414 137.657 1.00137.64 C
ANISOU 1223 CG PRO A 194 26850 18527 6920 -861 1321 912 C
ATOM 1224 CD PRO A 194 -8.303 -15.662 137.789 1.00136.61 C
ANISOU 1224 CD PRO A 194 26575 18450 6880 -1173 1551 656 C
ATOM 1225 N TRP A 195 -6.865 -15.221 134.274 1.00143.47 N
ANISOU 1225 N TRP A 195 26808 19298 8406 -1165 1085 597 N
ATOM 1226 CA TRP A 195 -6.513 -15.232 132.857 1.00140.26 C
ANISOU 1226 CA TRP A 195 26193 18834 8264 -1204 992 586 C
ATOM 1227 C TRP A 195 -7.113 -14.045 132.113 1.00137.15 C
ANISOU 1227 C TRP A 195 25436 18574 8101 -1431 976 295 C
ATOM 1228 O TRP A 195 -6.587 -13.643 131.068 1.00139.92 O
ANISOU 1228 O TRP A 195 25457 18957 8749 -1399 767 241 O
ATOM 1229 CB TRP A 195 -6.969 -16.538 132.210 1.00140.89 C
ANISOU 1229 CB TRP A 195 26457 18623 8450 -1308 1332 738 C
ATOM 1230 CG TRP A 195 -8.402 -16.857 132.502 1.00140.32 C
ANISOU 1230 CG TRP A 195 26470 18448 8398 -1601 1776 637 C
ATOM 1231 CD1 TRP A 195 -8.877 -17.584 133.553 1.00142.93 C
ANISOU 1231 CD1 TRP A 195 27122 18654 8529 -1608 2032 740 C
ATOM 1232 CD2 TRP A 195 -9.550 -16.458 131.738 1.00140.31 C
ANISOU 1232 CD2 TRP A 195 26203 18481 8627 -1926 2016 399 C
ATOM 1233 NE1 TRP A 195 -10.247 -17.668 133.491 1.00143.55 N
ANISOU 1233 NE1 TRP A 195 27150 18684 8710 -1937 2417 574 N
ATOM 1234 CE2 TRP A 195 -10.685 -16.985 132.387 1.00141.32 C
ANISOU 1234 CE2 TRP A 195 26491 18515 8688 -2128 2409 360 C
ATOM 1235 CE3 TRP A 195 -9.728 -15.711 130.569 1.00135.97 C
ANISOU 1235 CE3 TRP A 195 25285 18047 8330 -2055 1936 211 C
ATOM 1236 CZ2 TRP A 195 -11.979 -16.788 131.907 1.00142.54 C
ANISOU 1236 CZ2 TRP A 195 26416 18721 9023 -2449 2711 129 C
ATOM 1237 CZ3 TRP A 195 -11.014 -15.515 130.095 1.00132.52 C
ANISOU 1237 CZ3 TRP A 195 24629 17660 8062 -2352 2237 -8 C
ATOM 1238 CH2 TRP A 195 -12.122 -16.053 130.761 1.00137.79 C
ANISOU 1238 CH2 TRP A 195 25430 18264 8660 -2544 2614 -52 C
ATOM 1239 N GLY A 196 -8.197 -13.474 132.641 1.00132.30 N
ANISOU 1239 N GLY A 196 24765 18035 7469 -1617 1183 108 N
ATOM 1240 CA GLY A 196 -9.012 -12.497 131.953 1.00126.07 C
ANISOU 1240 CA GLY A 196 23651 17351 6900 -1827 1260 -160 C
ATOM 1241 C GLY A 196 -8.255 -11.412 131.212 1.00121.58 C
ANISOU 1241 C GLY A 196 22684 16908 6604 -1728 904 -284 C
ATOM 1242 O GLY A 196 -8.350 -11.293 129.983 1.00112.51 O
ANISOU 1242 O GLY A 196 21219 15722 5809 -1784 899 -343 O
ATOM 1243 N PRO A 197 -7.527 -10.564 131.952 1.00125.40 N
ANISOU 1243 N PRO A 197 23172 17548 6928 -1594 616 -345 N
ATOM 1244 CA PRO A 197 -6.797 -9.476 131.279 1.00127.66 C
ANISOU 1244 CA PRO A 197 23091 17940 7474 -1530 304 -487 C
ATOM 1245 C PRO A 197 -5.801 -9.961 130.246 1.00133.17 C
ANISOU 1245 C PRO A 197 23628 18562 8408 -1408 101 -348 C
ATOM 1246 O PRO A 197 -5.725 -9.393 129.146 1.00109.14 O
ANISOU 1246 O PRO A 197 20243 15513 5712 -1447 26 -455 O
ATOM 1247 CB PRO A 197 -6.096 -8.754 132.439 1.00126.36 C
ANISOU 1247 CB PRO A 197 23044 17952 7013 -1420 55 -552 C
ATOM 1248 CG PRO A 197 -6.758 -9.253 133.695 1.00119.15 C
ANISOU 1248 CG PRO A 197 22494 17039 5739 -1445 276 -488 C
ATOM 1249 CD PRO A 197 -7.234 -10.626 133.392 1.00119.61 C
ANISOU 1249 CD PRO A 197 22746 16897 5803 -1481 553 -280 C
ATOM 1250 N LYS A 198 -5.077 -11.046 130.545 1.00136.93 N
ANISOU 1250 N LYS A 198 24358 18971 8698 -1246 33 -102 N
ATOM 1251 CA LYS A 198 -4.084 -11.539 129.596 1.00142.95 C
ANISOU 1251 CA LYS A 198 24975 19670 9669 -1106 -162 35 C
ATOM 1252 C LYS A 198 -4.760 -12.075 128.342 1.00136.30 C
ANISOU 1252 C LYS A 198 23984 18645 9157 -1250 76 52 C
ATOM 1253 O LYS A 198 -4.270 -11.861 127.226 1.00129.10 O
ANISOU 1253 O LYS A 198 22772 17717 8564 -1225 -67 27 O
ATOM 1254 CB LYS A 198 -3.192 -12.601 130.254 1.00152.66 C
ANISOU 1254 CB LYS A 198 26538 20875 10590 -859 -271 303 C
ATOM 1255 CG LYS A 198 -3.691 -14.043 130.190 1.00157.36 C
ANISOU 1255 CG LYS A 198 27475 21221 11095 -867 50 532 C
ATOM 1256 CD LYS A 198 -2.999 -14.931 131.221 1.00159.97 C
ANISOU 1256 CD LYS A 198 28236 21542 11003 -598 -14 785 C
ATOM 1257 CE LYS A 198 -3.385 -16.398 131.044 1.00160.29 C
ANISOU 1257 CE LYS A 198 28648 21282 10973 -593 323 1026 C
ATOM 1258 NZ LYS A 198 -2.798 -17.278 132.098 1.00164.12 N
ANISOU 1258 NZ LYS A 198 29472 21735 11152 -297 300 1275 N
ATOM 1259 N ALA A 199 -5.935 -12.690 128.498 1.00155.65 N
ANISOU 1259 N ALA A 199 26620 20981 11539 -1424 451 62 N
ATOM 1260 CA ALA A 199 -6.629 -13.252 127.349 1.00108.79 C
ANISOU 1260 CA ALA A 199 20542 14904 5888 -1587 696 54 C
ATOM 1261 C ALA A 199 -7.184 -12.153 126.455 1.00113.45 C
ANISOU 1261 C ALA A 199 20700 15604 6801 -1711 682 -192 C
ATOM 1262 O ALA A 199 -7.004 -12.187 125.233 1.00115.56 O
ANISOU 1262 O ALA A 199 20701 15826 7382 -1719 633 -203 O
ATOM 1263 CB ALA A 199 -7.742 -14.187 127.821 1.00110.93 C
ANISOU 1263 CB ALA A 199 21125 15049 5974 -1771 1119 99 C
ATOM 1264 N TYR A 200 -7.853 -11.159 127.045 1.00111.05 N
ANISOU 1264 N TYR A 200 20335 15444 6416 -1789 728 -387 N
ATOM 1265 CA TYR A 200 -8.419 -10.102 126.212 1.00111.18 C
ANISOU 1265 CA TYR A 200 19971 15557 6714 -1866 736 -610 C
ATOM 1266 C TYR A 200 -7.329 -9.282 125.535 1.00101.53 C
ANISOU 1266 C TYR A 200 18493 14369 5714 -1723 393 -642 C
ATOM 1267 O TYR A 200 -7.483 -8.882 124.372 1.00102.71 O
ANISOU 1267 O TYR A 200 18337 14516 6171 -1745 385 -726 O
ATOM 1268 CB TYR A 200 -9.333 -9.201 127.038 1.00116.66 C
ANISOU 1268 CB TYR A 200 20683 16389 7254 -1948 866 -806 C
ATOM 1269 CG TYR A 200 -10.300 -8.385 126.206 1.00117.14 C
ANISOU 1269 CG TYR A 200 20406 16544 7558 -2032 999 -1021 C
ATOM 1270 CD1 TYR A 200 -11.305 -9.004 125.475 1.00122.01 C
ANISOU 1270 CD1 TYR A 200 20896 17161 8302 -2179 1280 -1058 C
ATOM 1271 CD2 TYR A 200 -10.214 -6.996 126.157 1.00114.45 C
ANISOU 1271 CD2 TYR A 200 19882 16301 7303 -1957 856 -1194 C
ATOM 1272 CE1 TYR A 200 -12.195 -8.269 124.718 1.00124.23 C
ANISOU 1272 CE1 TYR A 200 20852 17574 8776 -2217 1390 -1254 C
ATOM 1273 CE2 TYR A 200 -11.104 -6.251 125.401 1.00117.46 C
ANISOU 1273 CE2 TYR A 200 19979 16770 7881 -1983 985 -1374 C
ATOM 1274 CZ TYR A 200 -12.092 -6.896 124.685 1.00124.89 C
ANISOU 1274 CZ TYR A 200 20775 17746 8932 -2097 1240 -1399 C
ATOM 1275 OH TYR A 200 -12.984 -6.175 123.926 1.00128.77 O
ANISOU 1275 OH TYR A 200 20966 18369 9593 -2088 1358 -1578 O
ATOM 1276 N ILE A 201 -6.202 -9.053 126.218 1.00102.70 N
ANISOU 1276 N ILE A 201 18755 14562 5703 -1578 112 -579 N
ATOM 1277 CA ILE A 201 -5.144 -8.262 125.598 1.00101.01 C
ANISOU 1277 CA ILE A 201 18292 14393 5694 -1477 -196 -635 C
ATOM 1278 C ILE A 201 -4.468 -9.053 124.487 1.00104.27 C
ANISOU 1278 C ILE A 201 18584 14696 6339 -1408 -280 -479 C
ATOM 1279 O ILE A 201 -4.178 -8.511 123.412 1.00106.34 O
ANISOU 1279 O ILE A 201 18556 14947 6903 -1403 -378 -553 O
ATOM 1280 CB ILE A 201 -4.141 -7.777 126.659 1.00109.81 C
ANISOU 1280 CB ILE A 201 19530 15635 6558 -1366 -470 -650 C
ATOM 1281 CG1 ILE A 201 -4.842 -6.816 127.620 1.00112.13 C
ANISOU 1281 CG1 ILE A 201 19907 16032 6666 -1452 -381 -842 C
ATOM 1282 CG2 ILE A 201 -2.945 -7.097 126.006 1.00101.69 C
ANISOU 1282 CG2 ILE A 201 18245 14659 5734 -1288 -777 -709 C
ATOM 1283 CD1 ILE A 201 -5.825 -5.886 126.930 1.00108.58 C
ANISOU 1283 CD1 ILE A 201 19232 15568 6456 -1563 -206 -1042 C
ATOM 1284 N THR A 202 -4.230 -10.352 124.709 1.00101.98 N
ANISOU 1284 N THR A 202 18533 14307 5907 -1348 -221 -260 N
ATOM 1285 CA THR A 202 -3.657 -11.172 123.649 1.00104.44 C
ANISOU 1285 CA THR A 202 18754 14495 6432 -1282 -266 -111 C
ATOM 1286 C THR A 202 -4.598 -11.251 122.455 1.00102.05 C
ANISOU 1286 C THR A 202 18235 14114 6426 -1441 -37 -192 C
ATOM 1287 O THR A 202 -4.157 -11.226 121.300 1.00 95.95 O
ANISOU 1287 O THR A 202 17222 13298 5938 -1410 -132 -184 O
ATOM 1288 CB THR A 202 -3.349 -12.573 124.179 1.00109.17 C
ANISOU 1288 CB THR A 202 19712 14975 6794 -1180 -190 141 C
ATOM 1289 OG1 THR A 202 -2.481 -12.477 125.316 1.00118.23 O
ANISOU 1289 OG1 THR A 202 21050 16241 7631 -998 -419 214 O
ATOM 1290 CG2 THR A 202 -2.678 -13.420 123.105 1.00105.47 C
ANISOU 1290 CG2 THR A 202 19167 14370 6537 -1090 -241 298 C
ATOM 1291 N TRP A 203 -5.908 -11.285 122.714 1.00103.61 N
ANISOU 1291 N TRP A 203 18491 14322 6555 -1612 262 -290 N
ATOM 1292 CA TRP A 203 -6.871 -11.365 121.624 1.00 95.61 C
ANISOU 1292 CA TRP A 203 17246 13292 5788 -1763 483 -392 C
ATOM 1293 C TRP A 203 -6.883 -10.080 120.809 1.00100.92 C
ANISOU 1293 C TRP A 203 17556 14070 6718 -1733 349 -572 C
ATOM 1294 O TRP A 203 -6.848 -10.117 119.573 1.00103.78 O
ANISOU 1294 O TRP A 203 17674 14403 7353 -1737 340 -585 O
ATOM 1295 CB TRP A 203 -8.266 -11.669 122.175 1.00 97.20 C
ANISOU 1295 CB TRP A 203 17575 13530 5827 -1955 835 -481 C
ATOM 1296 CG TRP A 203 -9.377 -11.030 121.388 1.00 95.64 C
ANISOU 1296 CG TRP A 203 17054 13462 5824 -2076 997 -697 C
ATOM 1297 CD1 TRP A 203 -10.082 -9.911 121.730 1.00 95.69 C
ANISOU 1297 CD1 TRP A 203 16933 13631 5795 -2088 1033 -893 C
ATOM 1298 CD2 TRP A 203 -9.904 -11.464 120.125 1.00108.57 C
ANISOU 1298 CD2 TRP A 203 18453 15097 7703 -2177 1142 -744 C
ATOM 1299 NE1 TRP A 203 -11.016 -9.625 120.764 1.00 94.33 N
ANISOU 1299 NE1 TRP A 203 16453 13571 5818 -2163 1186 -1048 N
ATOM 1300 CE2 TRP A 203 -10.927 -10.562 119.768 1.00108.95 C
ANISOU 1300 CE2 TRP A 203 18221 15337 7837 -2227 1249 -967 C
ATOM 1301 CE3 TRP A 203 -9.613 -12.527 119.264 1.00 93.38 C
ANISOU 1301 CE3 TRP A 203 16528 13036 5917 -2222 1196 -624 C
ATOM 1302 CZ2 TRP A 203 -11.660 -10.690 118.591 1.00 92.00 C
ANISOU 1302 CZ2 TRP A 203 15776 13282 5896 -2312 1391 -1076 C
ATOM 1303 CZ3 TRP A 203 -10.344 -12.652 118.092 1.00 91.97 C
ANISOU 1303 CZ3 TRP A 203 16060 12930 5954 -2338 1346 -743 C
ATOM 1304 CH2 TRP A 203 -11.355 -11.738 117.768 1.00 91.32 C
ANISOU 1304 CH2 TRP A 203 15684 13073 5941 -2379 1433 -969 C
ATOM 1305 N ILE A 204 -6.911 -8.928 121.484 1.00101.90 N
ANISOU 1305 N ILE A 204 17663 14307 6750 -1698 253 -708 N
ATOM 1306 CA ILE A 204 -6.944 -7.667 120.751 1.00103.05 C
ANISOU 1306 CA ILE A 204 17518 14518 7119 -1659 161 -876 C
ATOM 1307 C ILE A 204 -5.651 -7.468 119.970 1.00 90.06 C
ANISOU 1307 C ILE A 204 15726 12811 5680 -1545 -115 -810 C
ATOM 1308 O ILE A 204 -5.676 -7.047 118.806 1.00 87.91 O
ANISOU 1308 O ILE A 204 15202 12524 5678 -1527 -130 -868 O
ATOM 1309 CB ILE A 204 -7.228 -6.494 121.708 1.00 92.90 C
ANISOU 1309 CB ILE A 204 16292 13335 5669 -1651 144 -1039 C
ATOM 1310 CG1 ILE A 204 -8.661 -6.576 122.237 1.00 94.18 C
ANISOU 1310 CG1 ILE A 204 16523 13581 5680 -1764 448 -1137 C
ATOM 1311 CG2 ILE A 204 -7.006 -5.163 121.004 1.00 94.53 C
ANISOU 1311 CG2 ILE A 204 16264 13562 6091 -1582 31 -1190 C
ATOM 1312 CD1 ILE A 204 -9.718 -6.479 121.154 1.00100.16 C
ANISOU 1312 CD1 ILE A 204 17010 14400 6645 -1813 650 -1243 C
ATOM 1313 N THR A 205 -4.504 -7.815 120.569 1.00 91.23 N
ANISOU 1313 N THR A 205 16026 12940 5698 -1459 -331 -687 N
ATOM 1314 CA THR A 205 -3.240 -7.663 119.855 1.00 89.98 C
ANISOU 1314 CA THR A 205 15710 12751 5726 -1358 -590 -637 C
ATOM 1315 C THR A 205 -3.180 -8.585 118.644 1.00 97.29 C
ANISOU 1315 C THR A 205 16520 13567 6880 -1352 -530 -512 C
ATOM 1316 O THR A 205 -2.817 -8.151 117.544 1.00 97.36 O
ANISOU 1316 O THR A 205 16286 13549 7158 -1327 -613 -554 O
ATOM 1317 CB THR A 205 -2.065 -7.939 120.794 1.00 92.04 C
ANISOU 1317 CB THR A 205 16140 13068 5765 -1250 -830 -537 C
ATOM 1318 OG1 THR A 205 -1.967 -6.894 121.768 1.00106.03 O
ANISOU 1318 OG1 THR A 205 17965 14960 7360 -1267 -923 -693 O
ATOM 1319 CG2 THR A 205 -0.762 -8.022 120.012 1.00 91.00 C
ANISOU 1319 CG2 THR A 205 15833 12924 5819 -1146 -1077 -470 C
ATOM 1320 N LEU A 206 -3.581 -9.850 118.818 1.00 94.14 N
ANISOU 1320 N LEU A 206 16309 13089 6371 -1387 -359 -368 N
ATOM 1321 CA LEU A 206 -3.571 -10.809 117.721 1.00 90.22 C
ANISOU 1321 CA LEU A 206 15737 12474 6069 -1403 -271 -258 C
ATOM 1322 C LEU A 206 -4.517 -10.399 116.603 1.00 87.11 C
ANISOU 1322 C LEU A 206 15074 12105 5918 -1509 -108 -400 C
ATOM 1323 O LEU A 206 -4.240 -10.664 115.427 1.00 86.57 O
ANISOU 1323 O LEU A 206 14826 11978 6089 -1492 -133 -366 O
ATOM 1324 CB LEU A 206 -3.950 -12.189 118.260 1.00 94.04 C
ANISOU 1324 CB LEU A 206 16531 12850 6350 -1451 -62 -101 C
ATOM 1325 CG LEU A 206 -4.159 -13.370 117.314 1.00103.99 C
ANISOU 1325 CG LEU A 206 17799 13959 7751 -1515 118 3 C
ATOM 1326 CD1 LEU A 206 -2.855 -13.745 116.637 1.00106.98 C
ANISOU 1326 CD1 LEU A 206 18114 14256 8277 -1347 -110 149 C
ATOM 1327 CD2 LEU A 206 -4.724 -14.554 118.082 1.00112.75 C
ANISOU 1327 CD2 LEU A 206 19277 14953 8610 -1602 387 118 C
ATOM 1328 N ALA A 207 -5.629 -9.751 116.945 1.00 86.11 N
ANISOU 1328 N ALA A 207 14911 12084 5722 -1599 56 -562 N
ATOM 1329 CA ALA A 207 -6.644 -9.451 115.948 1.00 84.60 C
ANISOU 1329 CA ALA A 207 14467 11963 5714 -1674 229 -698 C
ATOM 1330 C ALA A 207 -6.391 -8.145 115.200 1.00 82.76 C
ANISOU 1330 C ALA A 207 13977 11781 5685 -1571 84 -818 C
ATOM 1331 O ALA A 207 -6.577 -8.100 113.980 1.00 97.67 O
ANISOU 1331 O ALA A 207 15637 13677 7796 -1557 115 -848 O
ATOM 1332 CB ALA A 207 -8.023 -9.423 116.609 1.00 99.16 C
ANISOU 1332 CB ALA A 207 16371 13923 7381 -1803 498 -823 C
ATOM 1333 N VAL A 208 -5.982 -7.071 115.884 1.00 93.89 N
ANISOU 1333 N VAL A 208 15434 13222 7017 -1502 -58 -894 N
ATOM 1334 CA VAL A 208 -5.723 -5.808 115.193 1.00 94.13 C
ANISOU 1334 CA VAL A 208 15272 13262 7231 -1413 -160 -1009 C
ATOM 1335 C VAL A 208 -4.258 -5.614 114.844 1.00 96.40 C
ANISOU 1335 C VAL A 208 15522 13459 7648 -1341 -422 -938 C
ATOM 1336 O VAL A 208 -3.907 -4.576 114.266 1.00100.99 O
ANISOU 1336 O VAL A 208 15972 14018 8383 -1284 -500 -1029 O
ATOM 1337 CB VAL A 208 -6.216 -4.582 115.991 1.00 89.75 C
ANISOU 1337 CB VAL A 208 14777 12782 6542 -1393 -119 -1174 C
ATOM 1338 CG1 VAL A 208 -7.693 -4.666 116.265 1.00 91.91 C
ANISOU 1338 CG1 VAL A 208 15045 13178 6699 -1448 144 -1267 C
ATOM 1339 CG2 VAL A 208 -5.448 -4.439 117.266 1.00 88.47 C
ANISOU 1339 CG2 VAL A 208 14836 12611 6168 -1406 -270 -1157 C
ATOM 1340 N TYR A 209 -3.387 -6.567 115.170 1.00100.02 N
ANISOU 1340 N TYR A 209 16095 13869 8040 -1334 -547 -783 N
ATOM 1341 CA TYR A 209 -1.976 -6.359 114.878 1.00102.05 C
ANISOU 1341 CA TYR A 209 16285 14086 8405 -1261 -802 -736 C
ATOM 1342 C TYR A 209 -1.360 -7.565 114.183 1.00 98.54 C
ANISOU 1342 C TYR A 209 15808 13562 8069 -1221 -853 -557 C
ATOM 1343 O TYR A 209 -0.976 -7.477 113.013 1.00 90.65 O
ANISOU 1343 O TYR A 209 14617 12510 7318 -1192 -898 -547 O
ATOM 1344 CB TYR A 209 -1.205 -6.036 116.159 1.00 83.42 C
ANISOU 1344 CB TYR A 209 14086 11796 5814 -1242 -979 -756 C
ATOM 1345 CG TYR A 209 0.212 -5.578 115.904 1.00 91.77 C
ANISOU 1345 CG TYR A 209 15028 12867 6974 -1191 -1239 -773 C
ATOM 1346 CD1 TYR A 209 0.504 -4.233 115.710 1.00 90.78 C
ANISOU 1346 CD1 TYR A 209 14795 12749 6950 -1226 -1297 -953 C
ATOM 1347 CD2 TYR A 209 1.258 -6.491 115.846 1.00 89.71 C
ANISOU 1347 CD2 TYR A 209 14769 12614 6702 -1109 -1407 -618 C
ATOM 1348 CE1 TYR A 209 1.799 -3.808 115.469 1.00 87.81 C
ANISOU 1348 CE1 TYR A 209 14302 12396 6666 -1219 -1511 -996 C
ATOM 1349 CE2 TYR A 209 2.555 -6.077 115.605 1.00 92.85 C
ANISOU 1349 CE2 TYR A 209 15026 13065 7189 -1070 -1641 -655 C
ATOM 1350 CZ TYR A 209 2.820 -4.734 115.418 1.00 92.91 C
ANISOU 1350 CZ TYR A 209 14912 13089 7301 -1145 -1690 -853 C
ATOM 1351 OH TYR A 209 4.110 -4.316 115.179 1.00 93.30 O
ANISOU 1351 OH TYR A 209 14812 13202 7437 -1144 -1900 -916 O
ATOM 1352 N ILE A 210 -1.277 -8.695 114.888 1.00100.31 N
ANISOU 1352 N ILE A 210 16244 13766 8103 -1211 -828 -410 N
ATOM 1353 CA ILE A 210 -0.491 -9.828 114.401 1.00101.91 C
ANISOU 1353 CA ILE A 210 16470 13881 8371 -1136 -898 -226 C
ATOM 1354 C ILE A 210 -1.001 -10.294 113.042 1.00100.41 C
ANISOU 1354 C ILE A 210 16119 13604 8429 -1188 -744 -210 C
ATOM 1355 O ILE A 210 -0.243 -10.369 112.068 1.00 98.94 O
ANISOU 1355 O ILE A 210 15770 13369 8455 -1128 -857 -166 O
ATOM 1356 CB ILE A 210 -0.505 -10.970 115.428 1.00108.47 C
ANISOU 1356 CB ILE A 210 17614 14678 8922 -1102 -837 -66 C
ATOM 1357 CG1 ILE A 210 0.140 -10.508 116.730 1.00115.20 C
ANISOU 1357 CG1 ILE A 210 18606 15651 9515 -1020 -1028 -79 C
ATOM 1358 CG2 ILE A 210 0.211 -12.193 114.880 1.00109.09 C
ANISOU 1358 CG2 ILE A 210 17749 14637 9062 -1003 -866 133 C
ATOM 1359 CD1 ILE A 210 0.143 -11.567 117.802 1.00117.67 C
ANISOU 1359 CD1 ILE A 210 19256 15936 9515 -951 -971 88 C
ATOM 1360 N VAL A 211 -2.294 -10.610 112.955 1.00 97.18 N
ANISOU 1360 N VAL A 211 15740 13197 7988 -1310 -482 -260 N
ATOM 1361 CA VAL A 211 -2.880 -10.954 111.659 1.00 87.48 C
ANISOU 1361 CA VAL A 211 14325 11936 6978 -1376 -332 -287 C
ATOM 1362 C VAL A 211 -2.775 -9.800 110.664 1.00 87.82 C
ANISOU 1362 C VAL A 211 14084 12031 7254 -1326 -423 -410 C
ATOM 1363 O VAL A 211 -2.297 -10.028 109.539 1.00 91.11 O
ANISOU 1363 O VAL A 211 14346 12388 7884 -1289 -474 -365 O
ATOM 1364 CB VAL A 211 -4.324 -11.453 111.847 1.00 81.91 C
ANISOU 1364 CB VAL A 211 13681 11276 6164 -1536 -29 -356 C
ATOM 1365 CG1 VAL A 211 -4.999 -11.658 110.499 1.00 78.19 C
ANISOU 1365 CG1 VAL A 211 12970 10837 5903 -1610 116 -430 C
ATOM 1366 CG2 VAL A 211 -4.344 -12.735 112.666 1.00 83.61 C
ANISOU 1366 CG2 VAL A 211 14216 11385 6168 -1594 97 -213 C
ATOM 1367 N PRO A 212 -3.191 -8.565 110.992 1.00 89.50 N
ANISOU 1367 N PRO A 212 14237 12336 7433 -1314 -430 -560 N
ATOM 1368 CA PRO A 212 -3.026 -7.478 110.009 1.00 89.89 C
ANISOU 1368 CA PRO A 212 14062 12396 7695 -1245 -496 -658 C
ATOM 1369 C PRO A 212 -1.589 -7.236 109.579 1.00 83.90 C
ANISOU 1369 C PRO A 212 13240 11553 7083 -1168 -728 -597 C
ATOM 1370 O PRO A 212 -1.349 -6.959 108.396 1.00 71.99 O
ANISOU 1370 O PRO A 212 11551 10006 5796 -1127 -748 -609 O
ATOM 1371 CB PRO A 212 -3.611 -6.263 110.742 1.00 88.96 C
ANISOU 1371 CB PRO A 212 13984 12361 7457 -1234 -456 -812 C
ATOM 1372 CG PRO A 212 -4.592 -6.842 111.682 1.00 80.96 C
ANISOU 1372 CG PRO A 212 13121 11422 6219 -1323 -285 -822 C
ATOM 1373 CD PRO A 212 -3.969 -8.113 112.159 1.00 77.71 C
ANISOU 1373 CD PRO A 212 12884 10931 5711 -1362 -335 -654 C
ATOM 1374 N VAL A 213 -0.621 -7.366 110.487 1.00 80.16 N
ANISOU 1374 N VAL A 213 12900 11072 6483 -1146 -901 -538 N
ATOM 1375 CA VAL A 213 0.763 -7.097 110.111 1.00 81.53 C
ANISOU 1375 CA VAL A 213 12979 11213 6786 -1085 -1123 -509 C
ATOM 1376 C VAL A 213 1.291 -8.199 109.204 1.00 73.62 C
ANISOU 1376 C VAL A 213 11906 10134 5932 -1042 -1148 -358 C
ATOM 1377 O VAL A 213 1.978 -7.930 108.212 1.00 72.29 O
ANISOU 1377 O VAL A 213 11566 9923 5979 -1006 -1232 -361 O
ATOM 1378 CB VAL A 213 1.640 -6.911 111.365 1.00 80.13 C
ANISOU 1378 CB VAL A 213 12933 11108 6405 -1064 -1311 -513 C
ATOM 1379 CG1 VAL A 213 3.116 -6.975 111.008 1.00 76.70 C
ANISOU 1379 CG1 VAL A 213 12383 10682 6077 -1001 -1540 -467 C
ATOM 1380 CG2 VAL A 213 1.328 -5.582 112.033 1.00 83.04 C
ANISOU 1380 CG2 VAL A 213 13336 11532 6683 -1117 -1303 -697 C
ATOM 1381 N ILE A 214 0.951 -9.455 109.506 1.00 87.66 N
ANISOU 1381 N ILE A 214 13833 11878 7596 -1051 -1050 -228 N
ATOM 1382 CA ILE A 214 1.367 -10.556 108.645 1.00 83.11 C
ANISOU 1382 CA ILE A 214 13223 11204 7150 -1014 -1037 -88 C
ATOM 1383 C ILE A 214 0.747 -10.410 107.261 1.00 80.30 C
ANISOU 1383 C ILE A 214 12663 10819 7029 -1063 -905 -150 C
ATOM 1384 O ILE A 214 1.408 -10.642 106.242 1.00 79.74 O
ANISOU 1384 O ILE A 214 12457 10688 7155 -1015 -969 -98 O
ATOM 1385 CB ILE A 214 1.003 -11.908 109.293 1.00 84.70 C
ANISOU 1385 CB ILE A 214 13679 11342 7160 -1029 -903 53 C
ATOM 1386 CG1 ILE A 214 1.894 -12.186 110.507 1.00 84.47 C
ANISOU 1386 CG1 ILE A 214 13849 11344 6900 -913 -1073 157 C
ATOM 1387 CG2 ILE A 214 1.107 -13.046 108.284 1.00 82.23 C
ANISOU 1387 CG2 ILE A 214 13350 10902 6991 -1027 -806 169 C
ATOM 1388 CD1 ILE A 214 3.364 -12.329 110.170 1.00 86.06 C
ANISOU 1388 CD1 ILE A 214 13952 11553 7192 -760 -1316 245 C
ATOM 1389 N VAL A 215 -0.512 -9.967 107.196 1.00 84.97 N
ANISOU 1389 N VAL A 215 13215 11477 7594 -1143 -727 -271 N
ATOM 1390 CA VAL A 215 -1.170 -9.848 105.897 1.00 69.48 C
ANISOU 1390 CA VAL A 215 11047 9533 5818 -1166 -604 -337 C
ATOM 1391 C VAL A 215 -0.595 -8.679 105.103 1.00 76.15 C
ANISOU 1391 C VAL A 215 11710 10374 6850 -1079 -728 -406 C
ATOM 1392 O VAL A 215 -0.400 -8.777 103.885 1.00 66.64 O
ANISOU 1392 O VAL A 215 10347 9133 5839 -1048 -724 -390 O
ATOM 1393 CB VAL A 215 -2.694 -9.728 106.077 1.00 69.91 C
ANISOU 1393 CB VAL A 215 11088 9710 5766 -1254 -380 -459 C
ATOM 1394 CG1 VAL A 215 -3.369 -9.449 104.743 1.00 68.42 C
ANISOU 1394 CG1 VAL A 215 10656 9598 5743 -1242 -278 -548 C
ATOM 1395 CG2 VAL A 215 -3.246 -11.002 106.690 1.00 71.37 C
ANISOU 1395 CG2 VAL A 215 11455 9873 5788 -1378 -214 -395 C
ATOM 1396 N LEU A 216 -0.299 -7.563 105.778 1.00 79.65 N
ANISOU 1396 N LEU A 216 12192 10841 7230 -1048 -825 -489 N
ATOM 1397 CA LEU A 216 0.320 -6.427 105.099 1.00 74.15 C
ANISOU 1397 CA LEU A 216 11371 10106 6698 -987 -916 -560 C
ATOM 1398 C LEU A 216 1.702 -6.788 104.575 1.00 74.52 C
ANISOU 1398 C LEU A 216 11348 10073 6892 -958 -1086 -468 C
ATOM 1399 O LEU A 216 2.066 -6.427 103.446 1.00 75.94 O
ANISOU 1399 O LEU A 216 11382 10200 7273 -921 -1097 -479 O
ATOM 1400 CB LEU A 216 0.417 -5.235 106.054 1.00 75.07 C
ANISOU 1400 CB LEU A 216 11583 10246 6695 -992 -967 -679 C
ATOM 1401 CG LEU A 216 -0.852 -4.473 106.437 1.00 74.54 C
ANISOU 1401 CG LEU A 216 11562 10248 6511 -983 -802 -801 C
ATOM 1402 CD1 LEU A 216 -0.549 -3.425 107.495 1.00 72.67 C
ANISOU 1402 CD1 LEU A 216 11457 10009 6144 -1003 -866 -910 C
ATOM 1403 CD2 LEU A 216 -1.467 -3.826 105.220 1.00 80.88 C
ANISOU 1403 CD2 LEU A 216 12219 11049 7464 -895 -683 -861 C
ATOM 1404 N ALA A 217 2.484 -7.513 105.381 1.00 76.84 N
ANISOU 1404 N ALA A 217 11745 10372 7077 -958 -1215 -375 N
ATOM 1405 CA ALA A 217 3.804 -7.938 104.937 1.00 77.61 C
ANISOU 1405 CA ALA A 217 11762 10430 7294 -907 -1379 -287 C
ATOM 1406 C ALA A 217 3.699 -8.896 103.763 1.00 85.64 C
ANISOU 1406 C ALA A 217 12693 11372 8474 -883 -1296 -184 C
ATOM 1407 O ALA A 217 4.469 -8.794 102.806 1.00 90.59 O
ANISOU 1407 O ALA A 217 13174 11953 9294 -847 -1366 -168 O
ATOM 1408 CB ALA A 217 4.566 -8.586 106.093 1.00 77.97 C
ANISOU 1408 CB ALA A 217 11946 10532 7149 -866 -1529 -200 C
ATOM 1409 N THR A 218 2.719 -9.804 103.793 1.00 83.39 N
ANISOU 1409 N THR A 218 12497 11076 8112 -923 -1128 -131 N
ATOM 1410 CA THR A 218 2.547 -10.723 102.675 1.00 82.00 C
ANISOU 1410 CA THR A 218 12246 10831 8079 -929 -1025 -59 C
ATOM 1411 C THR A 218 2.161 -9.977 101.407 1.00 79.83 C
ANISOU 1411 C THR A 218 11766 10571 7997 -927 -962 -154 C
ATOM 1412 O THR A 218 2.711 -10.246 100.334 1.00 80.54 O
ANISOU 1412 O THR A 218 11734 10600 8267 -892 -989 -108 O
ATOM 1413 CB THR A 218 1.496 -11.781 103.015 1.00 78.12 C
ANISOU 1413 CB THR A 218 11901 10333 7449 -1017 -824 -22 C
ATOM 1414 OG1 THR A 218 2.083 -12.800 103.835 1.00 84.01 O
ANISOU 1414 OG1 THR A 218 12858 11006 8054 -980 -867 124 O
ATOM 1415 CG2 THR A 218 0.934 -12.414 101.748 1.00 66.41 C
ANISOU 1415 CG2 THR A 218 10298 8822 6112 -1073 -666 -28 C
ATOM 1416 N CYS A 219 1.262 -8.998 101.520 1.00 79.32 N
ANISOU 1416 N CYS A 219 11668 10586 7884 -941 -880 -282 N
ATOM 1417 CA CYS A 219 0.820 -8.271 100.336 1.00 76.35 C
ANISOU 1417 CA CYS A 219 11120 10235 7654 -896 -807 -363 C
ATOM 1418 C CYS A 219 1.959 -7.462 99.730 1.00 76.97 C
ANISOU 1418 C CYS A 219 11115 10229 7902 -830 -942 -365 C
ATOM 1419 O CYS A 219 2.220 -7.547 98.523 1.00 85.90 O
ANISOU 1419 O CYS A 219 12116 11318 9204 -790 -929 -340 O
ATOM 1420 CB CYS A 219 -0.362 -7.361 100.681 1.00 74.89 C
ANISOU 1420 CB CYS A 219 10938 10161 7354 -881 -689 -494 C
ATOM 1421 SG CYS A 219 -1.986 -8.162 100.617 1.00 79.27 S
ANISOU 1421 SG CYS A 219 11454 10877 7788 -957 -464 -548 S
ATOM 1422 N TYR A 220 2.669 -6.683 100.549 1.00 71.49 N
ANISOU 1422 N TYR A 220 10494 9514 7156 -834 -1063 -406 N
ATOM 1423 CA TYR A 220 3.724 -5.856 99.973 1.00 75.47 C
ANISOU 1423 CA TYR A 220 10917 9941 7817 -810 -1159 -440 C
ATOM 1424 C TYR A 220 4.969 -6.655 99.601 1.00 77.43 C
ANISOU 1424 C TYR A 220 11092 10147 8181 -807 -1295 -337 C
ATOM 1425 O TYR A 220 5.677 -6.273 98.663 1.00 81.65 O
ANISOU 1425 O TYR A 220 11511 10618 8893 -789 -1324 -347 O
ATOM 1426 CB TYR A 220 4.057 -4.700 100.915 1.00 76.28 C
ANISOU 1426 CB TYR A 220 11112 10044 7826 -847 -1220 -554 C
ATOM 1427 CG TYR A 220 3.036 -3.596 100.781 1.00 75.84 C
ANISOU 1427 CG TYR A 220 11100 9981 7733 -805 -1066 -664 C
ATOM 1428 CD1 TYR A 220 3.183 -2.596 99.829 1.00 77.20 C
ANISOU 1428 CD1 TYR A 220 11230 10059 8045 -750 -1000 -721 C
ATOM 1429 CD2 TYR A 220 1.894 -3.586 101.565 1.00 76.18 C
ANISOU 1429 CD2 TYR A 220 11237 10111 7596 -800 -970 -704 C
ATOM 1430 CE1 TYR A 220 2.235 -1.601 99.686 1.00 76.29 C
ANISOU 1430 CE1 TYR A 220 11177 9932 7876 -663 -847 -806 C
ATOM 1431 CE2 TYR A 220 0.946 -2.596 101.431 1.00 76.80 C
ANISOU 1431 CE2 TYR A 220 11347 10202 7630 -725 -826 -801 C
ATOM 1432 CZ TYR A 220 1.121 -1.607 100.492 1.00 76.22 C
ANISOU 1432 CZ TYR A 220 11244 10031 7686 -641 -767 -846 C
ATOM 1433 OH TYR A 220 0.172 -0.626 100.363 1.00 76.59 O
ANISOU 1433 OH TYR A 220 11347 10087 7668 -521 -615 -929 O
ATOM 1434 N GLY A 221 5.222 -7.793 100.251 1.00 77.70 N
ANISOU 1434 N GLY A 221 11197 10209 8116 -808 -1359 -233 N
ATOM 1435 CA GLY A 221 6.281 -8.664 99.780 1.00 78.12 C
ANISOU 1435 CA GLY A 221 11182 10226 8276 -764 -1461 -122 C
ATOM 1436 C GLY A 221 5.927 -9.329 98.467 1.00 74.70 C
ANISOU 1436 C GLY A 221 10658 9726 7999 -745 -1344 -61 C
ATOM 1437 O GLY A 221 6.785 -9.495 97.600 1.00 78.97 O
ANISOU 1437 O GLY A 221 11081 10218 8707 -708 -1401 -21 O
ATOM 1438 N LEU A 222 4.653 -9.695 98.288 1.00 76.11 N
ANISOU 1438 N LEU A 222 10876 9922 8120 -779 -1173 -72 N
ATOM 1439 CA LEU A 222 4.210 -10.208 96.998 1.00 74.53 C
ANISOU 1439 CA LEU A 222 10569 9695 8055 -779 -1052 -52 C
ATOM 1440 C LEU A 222 4.307 -9.137 95.922 1.00 76.85 C
ANISOU 1440 C LEU A 222 10713 9979 8507 -733 -1043 -128 C
ATOM 1441 O LEU A 222 4.627 -9.442 94.770 1.00 68.85 O
ANISOU 1441 O LEU A 222 9589 8921 7650 -704 -1023 -93 O
ATOM 1442 CB LEU A 222 2.774 -10.722 97.108 1.00 65.24 C
ANISOU 1442 CB LEU A 222 9440 8590 6758 -849 -867 -90 C
ATOM 1443 CG LEU A 222 2.498 -12.183 96.751 1.00 71.01 C
ANISOU 1443 CG LEU A 222 10215 9277 7487 -912 -752 -14 C
ATOM 1444 CD1 LEU A 222 3.425 -13.111 97.518 1.00 60.94 C
ANISOU 1444 CD1 LEU A 222 9107 7897 6150 -886 -840 126 C
ATOM 1445 CD2 LEU A 222 1.043 -12.525 97.031 1.00 60.31 C
ANISOU 1445 CD2 LEU A 222 8900 8026 5989 -1023 -557 -97 C
ATOM 1446 N ILE A 223 4.068 -7.876 96.286 1.00 77.55 N
ANISOU 1446 N ILE A 223 10821 10094 8549 -718 -1044 -229 N
ATOM 1447 CA ILE A 223 4.195 -6.789 95.319 1.00 57.76 C
ANISOU 1447 CA ILE A 223 8227 7546 6173 -658 -1012 -292 C
ATOM 1448 C ILE A 223 5.654 -6.599 94.918 1.00 72.08 C
ANISOU 1448 C ILE A 223 9979 9263 8144 -664 -1134 -263 C
ATOM 1449 O ILE A 223 5.977 -6.471 93.732 1.00 79.91 O
ANISOU 1449 O ILE A 223 10870 10198 9294 -623 -1101 -248 O
ATOM 1450 CB ILE A 223 3.592 -5.488 95.883 1.00 58.46 C
ANISOU 1450 CB ILE A 223 8397 7657 6157 -632 -957 -405 C
ATOM 1451 CG1 ILE A 223 2.073 -5.598 96.022 1.00 58.54 C
ANISOU 1451 CG1 ILE A 223 8418 7796 6028 -599 -815 -449 C
ATOM 1452 CG2 ILE A 223 3.943 -4.306 94.998 1.00 58.10 C
ANISOU 1452 CG2 ILE A 223 8323 7518 6236 -564 -916 -458 C
ATOM 1453 CD1 ILE A 223 1.430 -4.326 96.545 1.00 69.45 C
ANISOU 1453 CD1 ILE A 223 9886 9201 7298 -539 -747 -556 C
ATOM 1454 N ALA A 224 6.558 -6.579 95.901 1.00 71.50 N
ANISOU 1454 N ALA A 224 9954 9195 8019 -713 -1277 -265 N
ATOM 1455 CA ALA A 224 7.976 -6.434 95.583 1.00 82.58 C
ANISOU 1455 CA ALA A 224 11265 10555 9558 -730 -1398 -261 C
ATOM 1456 C ALA A 224 8.496 -7.627 94.789 1.00 86.94 C
ANISOU 1456 C ALA A 224 11720 11085 10228 -686 -1427 -140 C
ATOM 1457 O ALA A 224 9.330 -7.455 93.892 1.00 89.50 O
ANISOU 1457 O ALA A 224 11927 11357 10720 -678 -1449 -139 O
ATOM 1458 CB ALA A 224 8.783 -6.252 96.868 1.00 90.63 C
ANISOU 1458 CB ALA A 224 12328 11645 10460 -784 -1556 -304 C
ATOM 1459 N PHE A 225 7.985 -8.831 95.071 1.00 90.17 N
ANISOU 1459 N PHE A 225 12192 11518 10550 -663 -1401 -43 N
ATOM 1460 CA PHE A 225 8.360 -10.005 94.291 1.00 90.64 C
ANISOU 1460 CA PHE A 225 12196 11531 10713 -620 -1391 70 C
ATOM 1461 C PHE A 225 7.856 -9.890 92.860 1.00 91.03 C
ANISOU 1461 C PHE A 225 12145 11534 10906 -611 -1258 52 C
ATOM 1462 O PHE A 225 8.593 -10.167 91.912 1.00 94.40 O
ANISOU 1462 O PHE A 225 12468 11907 11491 -580 -1275 94 O
ATOM 1463 CB PHE A 225 7.803 -11.276 94.944 1.00 96.91 C
ANISOU 1463 CB PHE A 225 13131 12329 11361 -617 -1343 164 C
ATOM 1464 CG PHE A 225 8.662 -11.835 96.047 1.00109.71 C
ANISOU 1464 CG PHE A 225 14845 13978 12863 -562 -1489 244 C
ATOM 1465 CD1 PHE A 225 8.196 -12.869 96.848 1.00112.58 C
ANISOU 1465 CD1 PHE A 225 15395 14325 13055 -549 -1438 335 C
ATOM 1466 CD2 PHE A 225 9.931 -11.334 96.284 1.00112.68 C
ANISOU 1466 CD2 PHE A 225 15122 14408 13282 -520 -1668 221 C
ATOM 1467 CE1 PHE A 225 8.979 -13.390 97.863 1.00115.76 C
ANISOU 1467 CE1 PHE A 225 15902 14761 13319 -455 -1571 424 C
ATOM 1468 CE2 PHE A 225 10.718 -11.849 97.298 1.00114.29 C
ANISOU 1468 CE2 PHE A 225 15389 14687 13349 -438 -1818 289 C
ATOM 1469 CZ PHE A 225 10.243 -12.878 98.087 1.00116.50 C
ANISOU 1469 CZ PHE A 225 15872 14946 13446 -385 -1774 401 C
ATOM 1470 N LYS A 226 6.598 -9.478 92.686 1.00 92.05 N
ANISOU 1470 N LYS A 226 12297 11707 10971 -625 -1126 -13 N
ATOM 1471 CA LYS A 226 6.039 -9.341 91.347 1.00 90.53 C
ANISOU 1471 CA LYS A 226 12001 11516 10879 -590 -1006 -38 C
ATOM 1472 C LYS A 226 6.764 -8.270 90.547 1.00 90.67 C
ANISOU 1472 C LYS A 226 11942 11466 11041 -544 -1029 -74 C
ATOM 1473 O LYS A 226 6.922 -8.405 89.328 1.00 96.62 O
ANISOU 1473 O LYS A 226 12602 12186 11924 -504 -978 -52 O
ATOM 1474 CB LYS A 226 4.547 -9.023 91.449 1.00 96.62 C
ANISOU 1474 CB LYS A 226 12794 12401 11517 -587 -875 -117 C
ATOM 1475 CG LYS A 226 3.904 -8.478 90.182 1.00 98.57 C
ANISOU 1475 CG LYS A 226 12930 12699 11821 -504 -767 -169 C
ATOM 1476 CD LYS A 226 3.885 -9.500 89.054 1.00100.37 C
ANISOU 1476 CD LYS A 226 13055 12937 12144 -516 -712 -127 C
ATOM 1477 CE LYS A 226 2.855 -9.110 88.006 1.00102.04 C
ANISOU 1477 CE LYS A 226 13155 13285 12331 -433 -592 -200 C
ATOM 1478 NZ LYS A 226 3.055 -9.813 86.713 1.00102.59 N
ANISOU 1478 NZ LYS A 226 13112 13352 12515 -428 -551 -172 N
ATOM 1479 N ILE A 227 7.238 -7.218 91.214 1.00 97.64 N
ANISOU 1479 N ILE A 227 12877 12321 11901 -563 -1091 -137 N
ATOM 1480 CA ILE A 227 7.975 -6.175 90.512 1.00 96.73 C
ANISOU 1480 CA ILE A 227 12722 12114 11917 -552 -1080 -185 C
ATOM 1481 C ILE A 227 9.364 -6.674 90.134 1.00111.66 C
ANISOU 1481 C ILE A 227 14509 13959 13958 -585 -1183 -137 C
ATOM 1482 O ILE A 227 9.695 -6.789 88.951 1.00118.51 O
ANISOU 1482 O ILE A 227 15290 14771 14968 -551 -1134 -106 O
ATOM 1483 CB ILE A 227 8.041 -4.891 91.355 1.00 88.61 C
ANISOU 1483 CB ILE A 227 11801 11058 10811 -593 -1085 -292 C
ATOM 1484 CG1 ILE A 227 6.638 -4.316 91.549 1.00 83.28 C
ANISOU 1484 CG1 ILE A 227 11221 10427 9996 -520 -960 -339 C
ATOM 1485 CG2 ILE A 227 8.928 -3.862 90.675 1.00 88.87 C
ANISOU 1485 CG2 ILE A 227 11819 10966 10980 -620 -1049 -352 C
ATOM 1486 CD1 ILE A 227 6.551 -3.270 92.642 1.00 87.79 C
ANISOU 1486 CD1 ILE A 227 11929 10977 10449 -563 -961 -440 C
ATOM 1487 N TRP A 228 10.190 -7.005 91.129 1.00124.74 N
ANISOU 1487 N TRP A 228 16165 15661 15571 -636 -1329 -131 N
ATOM 1488 CA TRP A 228 11.581 -7.330 90.828 1.00141.94 C
ANISOU 1488 CA TRP A 228 18218 17834 17878 -650 -1435 -108 C
ATOM 1489 C TRP A 228 11.714 -8.622 90.029 1.00148.70 C
ANISOU 1489 C TRP A 228 19005 18673 18820 -578 -1425 15 C
ATOM 1490 O TRP A 228 12.494 -8.684 89.071 1.00156.99 O
ANISOU 1490 O TRP A 228 19940 19678 20031 -566 -1419 29 O
ATOM 1491 CB TRP A 228 12.387 -7.437 92.117 1.00152.04 C
ANISOU 1491 CB TRP A 228 19495 19217 19055 -687 -1607 -134 C
ATOM 1492 CG TRP A 228 13.815 -7.768 91.868 1.00157.82 C
ANISOU 1492 CG TRP A 228 20067 19998 19897 -683 -1726 -126 C
ATOM 1493 CD1 TRP A 228 14.423 -8.978 92.046 1.00158.48 C
ANISOU 1493 CD1 TRP A 228 20097 20150 19967 -586 -1834 -16 C
ATOM 1494 CD2 TRP A 228 14.820 -6.880 91.372 1.00161.90 C
ANISOU 1494 CD2 TRP A 228 20459 20506 20550 -773 -1733 -239 C
ATOM 1495 NE1 TRP A 228 15.750 -8.892 91.700 1.00161.35 N
ANISOU 1495 NE1 TRP A 228 20281 20578 20448 -592 -1926 -55 N
ATOM 1496 CE2 TRP A 228 16.018 -7.615 91.282 1.00164.03 C
ANISOU 1496 CE2 TRP A 228 20564 20875 20884 -727 -1863 -201 C
ATOM 1497 CE3 TRP A 228 14.823 -5.531 90.998 1.00161.20 C
ANISOU 1497 CE3 TRP A 228 20397 20327 20527 -887 -1623 -372 C
ATOM 1498 CZ2 TRP A 228 17.208 -7.047 90.836 1.00165.96 C
ANISOU 1498 CZ2 TRP A 228 20637 21161 21261 -815 -1893 -309 C
ATOM 1499 CZ3 TRP A 228 16.005 -4.969 90.556 1.00161.42 C
ANISOU 1499 CZ3 TRP A 228 20288 20359 20686 -990 -1634 -474 C
ATOM 1500 CH2 TRP A 228 17.182 -5.726 90.478 1.00164.05 C
ANISOU 1500 CH2 TRP A 228 20424 20821 21086 -965 -1771 -450 C
ATOM 1501 N GLN A 229 10.951 -9.652 90.387 1.00147.00 N
ANISOU 1501 N GLN A 229 18873 18482 18499 -542 -1399 96 N
ATOM 1502 CA GLN A 229 11.162 -10.991 89.853 1.00145.72 C
ANISOU 1502 CA GLN A 229 18687 18287 18393 -487 -1384 209 C
ATOM 1503 C GLN A 229 10.644 -11.120 88.425 1.00130.68 C
ANISOU 1503 C GLN A 229 16720 16325 16607 -478 -1242 212 C
ATOM 1504 O GLN A 229 11.434 -11.257 87.484 1.00133.26 O
ANISOU 1504 O GLN A 229 16940 16603 17089 -450 -1245 236 O
ATOM 1505 CB GLN A 229 10.486 -12.028 90.756 1.00153.07 C
ANISOU 1505 CB GLN A 229 19769 19237 19154 -477 -1366 282 C
ATOM 1506 CG GLN A 229 11.005 -13.446 90.577 1.00157.99 C
ANISOU 1506 CG GLN A 229 20425 19804 19800 -405 -1371 409 C
ATOM 1507 CD GLN A 229 12.345 -13.656 91.252 1.00160.08 C
ANISOU 1507 CD GLN A 229 20658 20116 20049 -312 -1550 463 C
ATOM 1508 OE1 GLN A 229 12.582 -13.158 92.353 1.00160.95 O
ANISOU 1508 OE1 GLN A 229 20799 20319 20037 -313 -1667 427 O
ATOM 1509 NE2 GLN A 229 13.233 -14.388 90.591 1.00161.82 N
ANISOU 1509 NE2 GLN A 229 20805 20296 20384 -221 -1574 540 N
ATOM 1510 N ASN A 230 9.322 -11.076 88.252 1.00119.58 N
ANISOU 1510 N ASN A 230 15366 14949 15118 -498 -1117 178 N
ATOM 1511 CA ASN A 230 8.694 -11.389 86.973 1.00113.38 C
ANISOU 1511 CA ASN A 230 14517 14160 14401 -484 -985 174 C
ATOM 1512 C ASN A 230 8.157 -10.160 86.244 1.00117.09 C
ANISOU 1512 C ASN A 230 14939 14657 14891 -447 -910 92 C
ATOM 1513 O ASN A 230 7.304 -10.297 85.363 1.00120.40 O
ANISOU 1513 O ASN A 230 15311 15135 15299 -418 -799 67 O
ATOM 1514 CB ASN A 230 7.586 -12.423 87.168 1.00106.31 C
ANISOU 1514 CB ASN A 230 13691 13315 13386 -534 -880 182 C
ATOM 1515 CG ASN A 230 8.092 -13.840 87.009 1.00 92.33 C
ANISOU 1515 CG ASN A 230 11960 11463 11659 -544 -867 277 C
ATOM 1516 OD1 ASN A 230 8.543 -14.226 85.932 1.00 81.46 O
ANISOU 1516 OD1 ASN A 230 10502 10033 10415 -519 -834 304 O
ATOM 1517 ND2 ASN A 230 8.030 -14.621 88.081 1.00 53.29 N
ANISOU 1517 ND2 ASN A 230 7161 6494 6593 -569 -879 334 N
ATOM 1518 N LEU A 265 8.628 -8.965 86.590 1.00120.52 N
ANISOU 1518 N LEU A 265 15394 15056 15340 -440 -958 44 N
ATOM 1519 CA LEU A 265 8.314 -7.771 85.803 1.00132.82 C
ANISOU 1519 CA LEU A 265 16948 16591 16928 -376 -867 -14 C
ATOM 1520 C LEU A 265 9.552 -6.900 85.616 1.00140.86 C
ANISOU 1520 C LEU A 265 17955 17493 18072 -404 -905 -38 C
ATOM 1521 O LEU A 265 10.225 -6.977 84.587 1.00147.27 O
ANISOU 1521 O LEU A 265 18690 18241 19025 -389 -878 -11 O
ATOM 1522 CB LEU A 265 7.199 -6.949 86.454 1.00139.35 C
ANISOU 1522 CB LEU A 265 17868 17487 17591 -341 -810 -84 C
ATOM 1523 CG LEU A 265 5.757 -7.432 86.284 1.00142.56 C
ANISOU 1523 CG LEU A 265 18251 18046 17868 -296 -718 -104 C
ATOM 1524 CD1 LEU A 265 4.793 -6.366 86.775 1.00145.33 C
ANISOU 1524 CD1 LEU A 265 18680 18465 18072 -220 -655 -181 C
ATOM 1525 CD2 LEU A 265 5.460 -7.798 84.835 1.00141.97 C
ANISOU 1525 CD2 LEU A 265 18067 18017 17858 -225 -634 -90 C
ATOM 1526 N ILE A 266 4.710 -1.460 82.591 1.00 97.72 N
ANISOU 1526 N ILE A 266 12941 12079 12107 498 -162 -188 N
ATOM 1527 CA ILE A 266 4.225 -1.215 83.942 1.00 92.76 C
ANISOU 1527 CA ILE A 266 12384 11496 11365 446 -197 -249 C
ATOM 1528 C ILE A 266 3.924 0.273 84.109 1.00 96.00 C
ANISOU 1528 C ILE A 266 13021 11778 11677 600 -60 -284 C
ATOM 1529 O ILE A 266 4.611 1.127 83.545 1.00110.05 O
ANISOU 1529 O ILE A 266 14945 13339 13530 632 41 -269 O
ATOM 1530 CB ILE A 266 5.238 -1.720 84.994 1.00 76.34 C
ANISOU 1530 CB ILE A 266 10290 9332 9385 185 -335 -264 C
ATOM 1531 CG1 ILE A 266 4.570 -1.884 86.361 1.00 72.16 C
ANISOU 1531 CG1 ILE A 266 9789 8915 8715 127 -392 -315 C
ATOM 1532 CG2 ILE A 266 6.438 -0.792 85.086 1.00 69.43 C
ANISOU 1532 CG2 ILE A 266 9544 8216 8620 87 -307 -292 C
ATOM 1533 CD1 ILE A 266 5.474 -2.511 87.407 1.00 78.93 C
ANISOU 1533 CD1 ILE A 266 10625 9737 9630 -92 -540 -319 C
ATOM 1534 N SER A 267 2.876 0.582 84.867 1.00 84.10 N
ANISOU 1534 N SER A 267 11559 10398 9997 698 -35 -333 N
ATOM 1535 CA SER A 267 2.446 1.962 85.041 1.00 84.59 C
ANISOU 1535 CA SER A 267 11854 10347 9940 884 114 -364 C
ATOM 1536 C SER A 267 3.282 2.646 86.112 1.00 86.57 C
ANISOU 1536 C SER A 267 12288 10367 10239 684 112 -427 C
ATOM 1537 O SER A 267 3.442 2.118 87.216 1.00 99.52 O
ANISOU 1537 O SER A 267 13866 12069 11876 488 -14 -472 O
ATOM 1538 CB SER A 267 0.965 2.014 85.417 1.00 85.33 C
ANISOU 1538 CB SER A 267 11905 10698 9820 1085 146 -402 C
ATOM 1539 OG SER A 267 0.177 1.285 84.493 1.00 95.69 O
ANISOU 1539 OG SER A 267 13003 12281 11073 1232 134 -377 O
ATOM 1540 N LYS A 268 3.827 3.820 85.781 1.00 83.62 N
ANISOU 1540 N LYS A 268 12148 9726 9897 726 264 -438 N
ATOM 1541 CA LYS A 268 4.466 4.639 86.805 1.00 86.75 C
ANISOU 1541 CA LYS A 268 12741 9916 10304 542 300 -534 C
ATOM 1542 C LYS A 268 3.451 5.161 87.819 1.00 83.59 C
ANISOU 1542 C LYS A 268 12462 9585 9712 650 344 -595 C
ATOM 1543 O LYS A 268 3.762 5.264 89.009 1.00 84.80 O
ANISOU 1543 O LYS A 268 12664 9708 9849 449 280 -682 O
ATOM 1544 CB LYS A 268 5.219 5.806 86.159 1.00 93.02 C
ANISOU 1544 CB LYS A 268 13789 10389 11167 548 500 -548 C
ATOM 1545 CG LYS A 268 6.298 5.416 85.144 1.00 99.29 C
ANISOU 1545 CG LYS A 268 14482 11093 12152 429 485 -500 C
ATOM 1546 CD LYS A 268 7.621 5.065 85.819 1.00 98.52 C
ANISOU 1546 CD LYS A 268 14279 10945 12207 63 354 -587 C
ATOM 1547 CE LYS A 268 8.808 5.353 84.903 1.00100.07 C
ANISOU 1547 CE LYS A 268 14504 10943 12574 -65 449 -591 C
ATOM 1548 NZ LYS A 268 8.638 4.724 83.561 1.00 99.05 N
ANISOU 1548 NZ LYS A 268 14248 10883 12502 110 453 -461 N
ATOM 1549 N ALA A 269 2.226 5.462 87.379 1.00 83.03 N
ANISOU 1549 N ALA A 269 12425 9639 9485 974 446 -555 N
ATOM 1550 CA ALA A 269 1.232 6.022 88.293 1.00 83.62 C
ANISOU 1550 CA ALA A 269 12617 9786 9370 1107 508 -617 C
ATOM 1551 C ALA A 269 0.700 4.968 89.261 1.00 94.21 C
ANISOU 1551 C ALA A 269 13735 11406 10655 974 333 -653 C
ATOM 1552 O ALA A 269 0.494 5.250 90.452 1.00 96.33 O
ANISOU 1552 O ALA A 269 14096 11669 10835 886 323 -732 O
ATOM 1553 CB ALA A 269 0.089 6.650 87.493 1.00 78.18 C
ANISOU 1553 CB ALA A 269 12007 9184 8513 1530 669 -566 C
ATOM 1554 N LYS A 270 0.470 3.748 88.769 1.00 98.90 N
ANISOU 1554 N LYS A 270 14055 12232 11291 949 211 -601 N
ATOM 1555 CA LYS A 270 0.007 2.676 89.643 1.00 95.86 C
ANISOU 1555 CA LYS A 270 13488 12080 10854 800 74 -631 C
ATOM 1556 C LYS A 270 1.044 2.357 90.713 1.00 95.35 C
ANISOU 1556 C LYS A 270 13460 11892 10878 486 -54 -663 C
ATOM 1557 O LYS A 270 0.703 2.171 91.889 1.00104.16 O
ANISOU 1557 O LYS A 270 14594 13091 11893 389 -105 -717 O
ATOM 1558 CB LYS A 270 -0.315 1.435 88.806 1.00 95.34 C
ANISOU 1558 CB LYS A 270 13155 12241 10831 805 1 -577 C
ATOM 1559 CG LYS A 270 -0.835 0.234 89.585 1.00 99.81 C
ANISOU 1559 CG LYS A 270 13552 13031 11339 642 -101 -606 C
ATOM 1560 CD LYS A 270 -1.051 -0.959 88.661 1.00 99.93 C
ANISOU 1560 CD LYS A 270 13333 13227 11408 618 -142 -568 C
ATOM 1561 CE LYS A 270 0.238 -1.339 87.945 1.00101.06 C
ANISOU 1561 CE LYS A 270 13460 13181 11759 502 -210 -489 C
ATOM 1562 NZ LYS A 270 0.075 -2.544 87.082 1.00 98.24 N
ANISOU 1562 NZ LYS A 270 12895 12976 11454 460 -241 -458 N
ATOM 1563 N ILE A 271 2.324 2.322 90.333 1.00 82.30 N
ANISOU 1563 N ILE A 271 11816 10056 9399 334 -104 -637 N
ATOM 1564 CA ILE A 271 3.360 2.085 91.332 1.00 80.69 C
ANISOU 1564 CA ILE A 271 11627 9774 9258 62 -234 -680 C
ATOM 1565 C ILE A 271 3.526 3.294 92.248 1.00 99.49 C
ANISOU 1565 C ILE A 271 14243 11999 11561 9 -156 -789 C
ATOM 1566 O ILE A 271 3.921 3.140 93.408 1.00108.82 O
ANISOU 1566 O ILE A 271 15441 13204 12703 -177 -262 -853 O
ATOM 1567 CB ILE A 271 4.688 1.673 90.666 1.00 79.33 C
ANISOU 1567 CB ILE A 271 11360 9496 9285 -82 -312 -639 C
ATOM 1568 CG1 ILE A 271 5.298 2.822 89.868 1.00 81.12 C
ANISOU 1568 CG1 ILE A 271 11740 9482 9598 -45 -161 -663 C
ATOM 1569 CG2 ILE A 271 4.472 0.464 89.772 1.00 81.79 C
ANISOU 1569 CG2 ILE A 271 11461 9952 9664 -28 -373 -538 C
ATOM 1570 CD1 ILE A 271 6.559 2.443 89.115 1.00 87.89 C
ANISOU 1570 CD1 ILE A 271 12488 10252 10652 -181 -216 -632 C
ATOM 1571 N ARG A 272 3.205 4.505 91.776 1.00 96.57 N
ANISOU 1571 N ARG A 272 14074 11470 11150 179 39 -815 N
ATOM 1572 CA ARG A 272 3.206 5.648 92.689 1.00 93.34 C
ANISOU 1572 CA ARG A 272 13917 10906 10643 137 144 -929 C
ATOM 1573 C ARG A 272 2.153 5.474 93.777 1.00 91.20 C
ANISOU 1573 C ARG A 272 13647 10818 10188 191 113 -968 C
ATOM 1574 O ARG A 272 2.423 5.713 94.963 1.00 95.89 O
ANISOU 1574 O ARG A 272 14331 11385 10718 20 67 -1064 O
ATOM 1575 CB ARG A 272 2.952 6.953 91.931 1.00103.47 C
ANISOU 1575 CB ARG A 272 15458 11960 11895 352 394 -933 C
ATOM 1576 CG ARG A 272 4.085 7.447 91.046 1.00116.74 C
ANISOU 1576 CG ARG A 272 17231 13386 13739 255 485 -930 C
ATOM 1577 CD ARG A 272 5.336 7.811 91.819 1.00124.40 C
ANISOU 1577 CD ARG A 272 18274 14199 14791 -96 452 -1066 C
ATOM 1578 NE ARG A 272 6.339 8.391 90.930 1.00127.83 N
ANISOU 1578 NE ARG A 272 18813 14385 15371 -192 585 -1083 N
ATOM 1579 CZ ARG A 272 7.601 8.624 91.272 1.00131.04 C
ANISOU 1579 CZ ARG A 272 19224 14681 15886 -518 563 -1208 C
ATOM 1580 NH1 ARG A 272 8.025 8.322 92.491 1.00132.32 N
ANISOU 1580 NH1 ARG A 272 19288 14972 16016 -756 394 -1321 N
ATOM 1581 NH2 ARG A 272 8.440 9.156 90.392 1.00130.43 N
ANISOU 1581 NH2 ARG A 272 19241 14380 15935 -605 714 -1229 N
ATOM 1582 N THR A 273 0.944 5.056 93.390 1.00 90.48 N
ANISOU 1582 N THR A 273 13443 10935 9999 422 140 -908 N
ATOM 1583 CA THR A 273 -0.102 4.834 94.387 1.00 89.75 C
ANISOU 1583 CA THR A 273 13328 11042 9731 464 125 -953 C
ATOM 1584 C THR A 273 0.268 3.689 95.324 1.00 64.30 C
ANISOU 1584 C THR A 273 9963 7950 6519 205 -69 -956 C
ATOM 1585 O THR A 273 -0.019 3.737 96.530 1.00 68.09 O
ANISOU 1585 O THR A 273 10513 8484 6873 120 -95 -1024 O
ATOM 1586 CB THR A 273 -1.443 4.550 93.705 1.00 91.41 C
ANISOU 1586 CB THR A 273 13400 11497 9835 744 194 -910 C
ATOM 1587 OG1 THR A 273 -1.370 3.315 92.978 1.00 63.16 O
ANISOU 1587 OG1 THR A 273 9564 8081 6351 686 83 -834 O
ATOM 1588 CG2 THR A 273 -1.805 5.678 92.753 1.00 93.22 C
ANISOU 1588 CG2 THR A 273 13784 11611 10024 1058 384 -888 C
ATOM 1589 N VAL A 274 0.934 2.662 94.793 1.00 62.81 N
ANISOU 1589 N VAL A 274 9596 7801 6470 89 -196 -878 N
ATOM 1590 CA VAL A 274 1.361 1.555 95.641 1.00 81.18 C
ANISOU 1590 CA VAL A 274 11820 10226 8796 -123 -369 -861 C
ATOM 1591 C VAL A 274 2.413 2.019 96.642 1.00 81.62 C
ANISOU 1591 C VAL A 274 12001 10154 8856 -321 -451 -937 C
ATOM 1592 O VAL A 274 2.387 1.625 97.813 1.00 88.76 O
ANISOU 1592 O VAL A 274 12927 11149 9650 -435 -543 -967 O
ATOM 1593 CB VAL A 274 1.870 0.390 94.773 1.00 71.07 C
ANISOU 1593 CB VAL A 274 10345 8995 7662 -173 -465 -757 C
ATOM 1594 CG1 VAL A 274 2.748 -0.541 95.590 1.00 70.32 C
ANISOU 1594 CG1 VAL A 274 10204 8922 7593 -378 -641 -730 C
ATOM 1595 CG2 VAL A 274 0.694 -0.369 94.180 1.00 68.81 C
ANISOU 1595 CG2 VAL A 274 9913 8913 7320 -48 -409 -715 C
ATOM 1596 N LYS A 275 3.334 2.883 96.211 1.00 77.95 N
ANISOU 1596 N LYS A 275 11626 9491 8502 -370 -408 -982 N
ATOM 1597 CA LYS A 275 4.354 3.386 97.126 1.00 87.09 C
ANISOU 1597 CA LYS A 275 12878 10556 9655 -583 -477 -1092 C
ATOM 1598 C LYS A 275 3.747 4.288 98.196 1.00 86.70 C
ANISOU 1598 C LYS A 275 13034 10479 9429 -579 -386 -1209 C
ATOM 1599 O LYS A 275 4.180 4.267 99.357 1.00 85.96 O
ANISOU 1599 O LYS A 275 12978 10433 9249 -749 -490 -1292 O
ATOM 1600 CB LYS A 275 5.439 4.121 96.339 1.00 95.12 C
ANISOU 1600 CB LYS A 275 13938 11369 10833 -664 -414 -1137 C
ATOM 1601 CG LYS A 275 6.704 4.400 97.133 1.00109.12 C
ANISOU 1601 CG LYS A 275 15724 13109 12629 -930 -517 -1266 C
ATOM 1602 CD LYS A 275 7.900 4.606 96.213 1.00117.43 C
ANISOU 1602 CD LYS A 275 16707 14037 13873 -1042 -503 -1287 C
ATOM 1603 CE LYS A 275 7.700 5.801 95.294 1.00122.29 C
ANISOU 1603 CE LYS A 275 17528 14394 14543 -952 -243 -1317 C
ATOM 1604 NZ LYS A 275 8.888 6.032 94.426 1.00122.05 N
ANISOU 1604 NZ LYS A 275 17447 14232 14694 -1090 -204 -1349 N
ATOM 1605 N MET A 276 2.722 5.066 97.837 1.00 73.33 N
ANISOU 1605 N MET A 276 11473 8725 7663 -367 -194 -1216 N
ATOM 1606 CA MET A 276 2.052 5.891 98.839 1.00 70.02 C
ANISOU 1606 CA MET A 276 11255 8283 7067 -335 -92 -1323 C
ATOM 1607 C MET A 276 1.358 5.025 99.884 1.00 77.27 C
ANISOU 1607 C MET A 276 12086 9436 7836 -364 -203 -1310 C
ATOM 1608 O MET A 276 1.483 5.261 101.095 1.00 82.85 O
ANISOU 1608 O MET A 276 12898 10158 8422 -496 -244 -1406 O
ATOM 1609 CB MET A 276 1.047 6.824 98.167 1.00 69.79 C
ANISOU 1609 CB MET A 276 11375 8166 6978 -45 139 -1315 C
ATOM 1610 CG MET A 276 0.165 7.584 99.147 1.00 78.52 C
ANISOU 1610 CG MET A 276 12674 9275 7887 43 259 -1410 C
ATOM 1611 SD MET A 276 -1.303 8.245 98.347 1.00 86.36 S
ANISOU 1611 SD MET A 276 13744 10302 8767 474 486 -1361 S
ATOM 1612 CE MET A 276 -1.881 6.771 97.518 1.00 88.05 C
ANISOU 1612 CE MET A 276 13590 10834 9030 564 350 -1226 C
ATOM 1613 N THR A 277 0.635 3.996 99.432 1.00 77.62 N
ANISOU 1613 N THR A 277 11944 9668 7879 -258 -242 -1201 N
ATOM 1614 CA THR A 277 -0.012 3.098 100.383 1.00 67.30 C
ANISOU 1614 CA THR A 277 10570 8570 6433 -310 -319 -1188 C
ATOM 1615 C THR A 277 1.014 2.334 101.215 1.00 77.45 C
ANISOU 1615 C THR A 277 11819 9882 7726 -541 -517 -1176 C
ATOM 1616 O THR A 277 0.757 2.017 102.384 1.00 80.38 O
ANISOU 1616 O THR A 277 12244 10354 7942 -620 -570 -1206 O
ATOM 1617 CB THR A 277 -0.944 2.137 99.649 1.00 65.97 C
ANISOU 1617 CB THR A 277 10209 8590 6269 -187 -294 -1096 C
ATOM 1618 OG1 THR A 277 -0.199 1.405 98.666 1.00 77.36 O
ANISOU 1618 OG1 THR A 277 11503 10002 7889 -230 -382 -1000 O
ATOM 1619 CG2 THR A 277 -2.069 2.901 98.964 1.00 66.41 C
ANISOU 1619 CG2 THR A 277 10279 8690 6263 78 -111 -1122 C
ATOM 1620 N PHE A 278 2.188 2.051 100.644 1.00 66.67 N
ANISOU 1620 N PHE A 278 10368 8440 6525 -634 -625 -1134 N
ATOM 1621 CA PHE A 278 3.243 1.404 101.417 1.00 85.41 C
ANISOU 1621 CA PHE A 278 12699 10864 8890 -813 -821 -1129 C
ATOM 1622 C PHE A 278 3.771 2.320 102.513 1.00 85.72 C
ANISOU 1622 C PHE A 278 12890 10856 8823 -948 -847 -1281 C
ATOM 1623 O PHE A 278 4.048 1.865 103.630 1.00 83.53 O
ANISOU 1623 O PHE A 278 12629 10696 8413 -1047 -980 -1299 O
ATOM 1624 CB PHE A 278 4.385 0.971 100.499 1.00 77.18 C
ANISOU 1624 CB PHE A 278 11511 9769 8046 -863 -918 -1066 C
ATOM 1625 CG PHE A 278 5.515 0.302 101.223 1.00 79.60 C
ANISOU 1625 CG PHE A 278 11749 10161 8335 -1004 -1127 -1059 C
ATOM 1626 CD1 PHE A 278 6.816 0.757 101.087 1.00 77.81 C
ANISOU 1626 CD1 PHE A 278 11473 9881 8210 -1127 -1208 -1138 C
ATOM 1627 CD2 PHE A 278 5.269 -0.773 102.063 1.00 79.77 C
ANISOU 1627 CD2 PHE A 278 11761 10328 8220 -1006 -1232 -979 C
ATOM 1628 CE1 PHE A 278 7.855 0.139 101.764 1.00 79.68 C
ANISOU 1628 CE1 PHE A 278 11619 10250 8408 -1225 -1413 -1141 C
ATOM 1629 CE2 PHE A 278 6.300 -1.392 102.743 1.00 76.99 C
ANISOU 1629 CE2 PHE A 278 11358 10072 7821 -1084 -1426 -959 C
ATOM 1630 CZ PHE A 278 7.594 -0.937 102.593 1.00 79.50 C
ANISOU 1630 CZ PHE A 278 11594 10376 8235 -1182 -1529 -1042 C
ATOM 1631 N ILE A 279 3.912 3.615 102.218 1.00 89.72 N
ANISOU 1631 N ILE A 279 13528 11191 9372 -951 -710 -1396 N
ATOM 1632 CA ILE A 279 4.314 4.549 103.268 1.00 88.45 C
ANISOU 1632 CA ILE A 279 13532 10977 9097 -1099 -701 -1569 C
ATOM 1633 C ILE A 279 3.232 4.631 104.335 1.00 86.27 C
ANISOU 1633 C ILE A 279 13382 10793 8605 -1041 -649 -1602 C
ATOM 1634 O ILE A 279 3.531 4.763 105.530 1.00 84.34 O
ANISOU 1634 O ILE A 279 13215 10616 8214 -1177 -732 -1703 O
ATOM 1635 CB ILE A 279 4.642 5.933 102.668 1.00 86.65 C
ANISOU 1635 CB ILE A 279 13461 10502 8959 -1122 -514 -1688 C
ATOM 1636 CG1 ILE A 279 6.071 5.947 102.125 1.00 81.34 C
ANISOU 1636 CG1 ILE A 279 12679 9770 8457 -1298 -599 -1729 C
ATOM 1637 CG2 ILE A 279 4.488 7.034 103.703 1.00 84.45 C
ANISOU 1637 CG2 ILE A 279 13422 10141 8526 -1213 -410 -1870 C
ATOM 1638 CD1 ILE A 279 7.121 5.674 103.182 1.00 76.78 C
ANISOU 1638 CD1 ILE A 279 12020 9344 7807 -1532 -805 -1839 C
ATOM 1639 N ILE A 280 1.966 4.501 103.935 1.00 87.31 N
ANISOU 1639 N ILE A 280 13516 10957 8700 -841 -519 -1526 N
ATOM 1640 CA ILE A 280 0.886 4.486 104.922 1.00 85.41 C
ANISOU 1640 CA ILE A 280 13367 10831 8253 -785 -462 -1558 C
ATOM 1641 C ILE A 280 1.008 3.267 105.832 1.00 85.15 C
ANISOU 1641 C ILE A 280 13253 10987 8113 -892 -638 -1494 C
ATOM 1642 O ILE A 280 0.830 3.361 107.054 1.00 74.13 O
ANISOU 1642 O ILE A 280 11971 9663 6533 -965 -664 -1566 O
ATOM 1643 CB ILE A 280 -0.480 4.525 104.216 1.00 72.09 C
ANISOU 1643 CB ILE A 280 11647 9194 6549 -543 -291 -1500 C
ATOM 1644 CG1 ILE A 280 -0.616 5.800 103.390 1.00 72.67 C
ANISOU 1644 CG1 ILE A 280 11851 9071 6690 -390 -103 -1553 C
ATOM 1645 CG2 ILE A 280 -1.605 4.429 105.225 1.00 72.99 C
ANISOU 1645 CG2 ILE A 280 11825 9457 6452 -497 -227 -1541 C
ATOM 1646 CD1 ILE A 280 -1.595 5.661 102.265 1.00 89.26 C
ANISOU 1646 CD1 ILE A 280 13842 11244 8827 -130 12 -1463 C
ATOM 1647 N VAL A 281 1.324 2.107 105.252 1.00 83.64 N
ANISOU 1647 N VAL A 281 12887 10868 8024 -893 -748 -1355 N
ATOM 1648 CA VAL A 281 1.488 0.897 106.056 1.00 95.64 C
ANISOU 1648 CA VAL A 281 14367 12534 9437 -970 -894 -1272 C
ATOM 1649 C VAL A 281 2.692 1.027 106.986 1.00104.01 C
ANISOU 1649 C VAL A 281 15476 13617 10427 -1119 -1072 -1341 C
ATOM 1650 O VAL A 281 2.659 0.575 108.141 1.00 73.99 O
ANISOU 1650 O VAL A 281 11748 9932 6434 -1170 -1156 -1339 O
ATOM 1651 CB VAL A 281 1.602 -0.334 105.137 1.00 69.54 C
ANISOU 1651 CB VAL A 281 10891 9266 6264 -929 -945 -1112 C
ATOM 1652 CG1 VAL A 281 2.166 -1.528 105.893 1.00 69.97 C
ANISOU 1652 CG1 VAL A 281 10940 9418 6229 -1002 -1108 -1017 C
ATOM 1653 CG2 VAL A 281 0.243 -0.674 104.536 1.00 69.77 C
ANISOU 1653 CG2 VAL A 281 10863 9358 6289 -811 -780 -1068 C
ATOM 1654 N LEU A 282 3.763 1.665 106.509 1.00 92.28 N
ANISOU 1654 N LEU A 282 13946 12036 9078 -1194 -1125 -1414 N
ATOM 1655 CA LEU A 282 4.928 1.872 107.362 1.00 86.74 C
ANISOU 1655 CA LEU A 282 13253 11401 8301 -1350 -1293 -1519 C
ATOM 1656 C LEU A 282 4.592 2.791 108.528 1.00 87.39 C
ANISOU 1656 C LEU A 282 13527 11493 8186 -1428 -1236 -1687 C
ATOM 1657 O LEU A 282 5.043 2.564 109.658 1.00 95.66 O
ANISOU 1657 O LEU A 282 14606 12686 9055 -1516 -1381 -1738 O
ATOM 1658 CB LEU A 282 6.083 2.445 106.542 1.00 86.38 C
ANISOU 1658 CB LEU A 282 13110 11259 8450 -1442 -1323 -1596 C
ATOM 1659 CG LEU A 282 7.433 1.741 106.677 1.00 88.38 C
ANISOU 1659 CG LEU A 282 13192 11657 8732 -1525 -1558 -1576 C
ATOM 1660 CD1 LEU A 282 7.289 0.259 106.367 1.00 82.97 C
ANISOU 1660 CD1 LEU A 282 12395 11060 8070 -1390 -1652 -1352 C
ATOM 1661 CD2 LEU A 282 8.461 2.389 105.763 1.00 89.17 C
ANISOU 1661 CD2 LEU A 282 13187 11656 9037 -1630 -1543 -1671 C
ATOM 1662 N ALA A 283 3.770 3.813 108.279 1.00 84.17 N
ANISOU 1662 N ALA A 283 13254 10938 7788 -1374 -1021 -1769 N
ATOM 1663 CA ALA A 283 3.332 4.677 109.368 1.00 87.69 C
ANISOU 1663 CA ALA A 283 13902 11375 8040 -1430 -938 -1925 C
ATOM 1664 C ALA A 283 2.459 3.913 110.354 1.00 91.19 C
ANISOU 1664 C ALA A 283 14393 11983 8272 -1373 -965 -1854 C
ATOM 1665 O ALA A 283 2.584 4.092 111.571 1.00 81.04 O
ANISOU 1665 O ALA A 283 13218 10787 6786 -1469 -1027 -1953 O
ATOM 1666 CB ALA A 283 2.586 5.889 108.810 1.00 83.64 C
ANISOU 1666 CB ALA A 283 13542 10656 7581 -1335 -679 -2007 C
ATOM 1667 N PHE A 284 1.606 3.018 109.849 1.00 92.03 N
ANISOU 1667 N PHE A 284 14416 12139 8413 -1235 -917 -1691 N
ATOM 1668 CA PHE A 284 0.762 2.225 110.737 1.00 84.25 C
ANISOU 1668 CA PHE A 284 13482 11300 7231 -1205 -912 -1625 C
ATOM 1669 C PHE A 284 1.610 1.361 111.658 1.00 84.70 C
ANISOU 1669 C PHE A 284 13536 11491 7154 -1300 -1128 -1575 C
ATOM 1670 O PHE A 284 1.387 1.323 112.875 1.00 96.83 O
ANISOU 1670 O PHE A 284 15206 13125 8460 -1344 -1154 -1621 O
ATOM 1671 CB PHE A 284 -0.195 1.353 109.919 1.00 85.74 C
ANISOU 1671 CB PHE A 284 13557 11526 7495 -1080 -812 -1480 C
ATOM 1672 CG PHE A 284 -0.896 0.286 110.727 1.00 87.53 C
ANISOU 1672 CG PHE A 284 13821 11894 7540 -1090 -806 -1396 C
ATOM 1673 CD1 PHE A 284 -2.112 0.549 111.337 1.00 90.06 C
ANISOU 1673 CD1 PHE A 284 14238 12282 7700 -1054 -643 -1459 C
ATOM 1674 CD2 PHE A 284 -0.346 -0.983 110.863 1.00 76.03 C
ANISOU 1674 CD2 PHE A 284 12322 10498 6069 -1130 -942 -1254 C
ATOM 1675 CE1 PHE A 284 -2.760 -0.428 112.077 1.00 87.83 C
ANISOU 1675 CE1 PHE A 284 14005 12120 7247 -1088 -608 -1392 C
ATOM 1676 CE2 PHE A 284 -0.987 -1.960 111.603 1.00 76.64 C
ANISOU 1676 CE2 PHE A 284 12480 10672 5969 -1146 -900 -1173 C
ATOM 1677 CZ PHE A 284 -2.196 -1.683 112.209 1.00 80.22 C
ANISOU 1677 CZ PHE A 284 13026 11187 6267 -1141 -729 -1247 C
ATOM 1678 N ILE A 285 2.594 0.658 111.091 1.00 84.04 N
ANISOU 1678 N ILE A 285 13308 11425 7199 -1310 -1284 -1476 N
ATOM 1679 CA ILE A 285 3.391 -0.243 111.917 1.00 89.54 C
ANISOU 1679 CA ILE A 285 14000 12269 7751 -1343 -1492 -1405 C
ATOM 1680 C ILE A 285 4.247 0.550 112.900 1.00 91.05 C
ANISOU 1680 C ILE A 285 14252 12544 7800 -1465 -1621 -1583 C
ATOM 1681 O ILE A 285 4.323 0.203 114.085 1.00 83.31 O
ANISOU 1681 O ILE A 285 13371 11709 6574 -1481 -1719 -1586 O
ATOM 1682 CB ILE A 285 4.228 -1.205 111.045 1.00 92.75 C
ANISOU 1682 CB ILE A 285 14235 12682 8326 -1294 -1619 -1255 C
ATOM 1683 CG1 ILE A 285 5.310 -0.476 110.242 1.00 98.52 C
ANISOU 1683 CG1 ILE A 285 14823 13352 9260 -1360 -1688 -1352 C
ATOM 1684 CG2 ILE A 285 3.324 -2.001 110.110 1.00 92.09 C
ANISOU 1684 CG2 ILE A 285 14101 12524 8365 -1199 -1476 -1102 C
ATOM 1685 CD1 ILE A 285 6.710 -0.610 110.824 1.00 99.52 C
ANISOU 1685 CD1 ILE A 285 14867 13635 9311 -1428 -1929 -1406 C
ATOM 1686 N VAL A 286 4.852 1.658 112.452 1.00 86.39 N
ANISOU 1686 N VAL A 286 13619 11864 7341 -1564 -1601 -1748 N
ATOM 1687 CA VAL A 286 5.701 2.433 113.355 1.00 93.95 C
ANISOU 1687 CA VAL A 286 14619 12916 8162 -1721 -1711 -1955 C
ATOM 1688 C VAL A 286 4.876 3.075 114.465 1.00 97.78 C
ANISOU 1688 C VAL A 286 15322 13410 8421 -1759 -1603 -2076 C
ATOM 1689 O VAL A 286 5.381 3.289 115.574 1.00105.42 O
ANISOU 1689 O VAL A 286 16348 14530 9177 -1861 -1725 -2202 O
ATOM 1690 CB VAL A 286 6.519 3.483 112.575 1.00 92.85 C
ANISOU 1690 CB VAL A 286 14404 12653 8223 -1855 -1671 -2122 C
ATOM 1691 CG1 VAL A 286 5.656 4.663 112.156 1.00 88.26 C
ANISOU 1691 CG1 VAL A 286 13986 11830 7719 -1856 -1398 -2225 C
ATOM 1692 CG2 VAL A 286 7.708 3.956 113.405 1.00 87.47 C
ANISOU 1692 CG2 VAL A 286 13681 12141 7414 -2047 -1840 -2333 C
ATOM 1693 N CYS A 287 3.601 3.380 114.207 1.00 97.34 N
ANISOU 1693 N CYS A 287 15379 13218 8389 -1668 -1377 -2047 N
ATOM 1694 CA CYS A 287 2.792 4.027 115.233 1.00 99.87 C
ANISOU 1694 CA CYS A 287 15905 13542 8497 -1692 -1256 -2168 C
ATOM 1695 C CYS A 287 2.198 3.024 116.212 1.00102.28 C
ANISOU 1695 C CYS A 287 16281 14012 8569 -1630 -1307 -2048 C
ATOM 1696 O CYS A 287 2.067 3.326 117.404 1.00113.10 O
ANISOU 1696 O CYS A 287 17801 15473 9699 -1693 -1321 -2154 O
ATOM 1697 CB CYS A 287 1.681 4.853 114.586 1.00 85.54 C
ANISOU 1697 CB CYS A 287 14180 11537 6784 -1595 -985 -2203 C
ATOM 1698 SG CYS A 287 2.244 6.346 113.734 1.00 93.72 S
ANISOU 1698 SG CYS A 287 15265 12329 8017 -1671 -852 -2384 S
ATOM 1699 N TRP A 288 1.822 1.833 115.738 1.00 93.13 N
ANISOU 1699 N TRP A 288 15038 12882 7467 -1519 -1315 -1834 N
ATOM 1700 CA TRP A 288 1.110 0.891 116.592 1.00 94.63 C
ANISOU 1700 CA TRP A 288 15333 13184 7440 -1469 -1298 -1718 C
ATOM 1701 C TRP A 288 1.994 -0.171 117.228 1.00 97.73 C
ANISOU 1701 C TRP A 288 15721 13729 7685 -1461 -1523 -1599 C
ATOM 1702 O TRP A 288 1.578 -0.771 118.225 1.00 90.67 O
ANISOU 1702 O TRP A 288 14976 12930 6546 -1438 -1520 -1536 O
ATOM 1703 CB TRP A 288 -0.017 0.208 115.808 1.00 91.44 C
ANISOU 1703 CB TRP A 288 14877 12722 7144 -1368 -1120 -1576 C
ATOM 1704 CG TRP A 288 -1.122 1.155 115.441 1.00 93.41 C
ANISOU 1704 CG TRP A 288 15154 12887 7451 -1325 -889 -1685 C
ATOM 1705 CD1 TRP A 288 -1.242 1.860 114.280 1.00 97.60 C
ANISOU 1705 CD1 TRP A 288 15586 13293 8206 -1264 -792 -1725 C
ATOM 1706 CD2 TRP A 288 -2.254 1.515 116.246 1.00101.39 C
ANISOU 1706 CD2 TRP A 288 16307 13943 8273 -1311 -720 -1765 C
ATOM 1707 NE1 TRP A 288 -2.378 2.630 114.307 1.00 98.22 N
ANISOU 1707 NE1 TRP A 288 15737 13343 8240 -1187 -579 -1818 N
ATOM 1708 CE2 TRP A 288 -3.019 2.437 115.502 1.00 99.44 C
ANISOU 1708 CE2 TRP A 288 16028 13606 8149 -1219 -531 -1850 C
ATOM 1709 CE3 TRP A 288 -2.696 1.148 117.522 1.00103.29 C
ANISOU 1709 CE3 TRP A 288 16706 14296 8244 -1353 -703 -1770 C
ATOM 1710 CZ2 TRP A 288 -4.199 2.994 115.988 1.00103.46 C
ANISOU 1710 CZ2 TRP A 288 16638 14149 8524 -1159 -333 -1945 C
ATOM 1711 CZ3 TRP A 288 -3.871 1.702 118.003 1.00102.93 C
ANISOU 1711 CZ3 TRP A 288 16761 14274 8075 -1323 -499 -1870 C
ATOM 1712 CH2 TRP A 288 -4.608 2.614 117.237 1.00106.27 C
ANISOU 1712 CH2 TRP A 288 17129 14621 8630 -1222 -320 -1959 C
ATOM 1713 N THR A 289 3.192 -0.428 116.699 1.00105.32 N
ANISOU 1713 N THR A 289 16526 14721 8770 -1461 -1709 -1564 N
ATOM 1714 CA THR A 289 4.067 -1.419 117.322 1.00107.66 C
ANISOU 1714 CA THR A 289 16818 15187 8902 -1405 -1929 -1448 C
ATOM 1715 C THR A 289 4.408 -1.094 118.774 1.00108.99 C
ANISOU 1715 C THR A 289 17119 15540 8753 -1455 -2052 -1566 C
ATOM 1716 O THR A 289 4.281 -1.995 119.624 1.00116.86 O
ANISOU 1716 O THR A 289 18251 16645 9506 -1366 -2106 -1434 O
ATOM 1717 CB THR A 289 5.336 -1.587 116.477 1.00111.17 C
ANISOU 1717 CB THR A 289 17041 15660 9540 -1393 -2106 -1426 C
ATOM 1718 OG1 THR A 289 4.994 -2.120 115.194 1.00113.19 O
ANISOU 1718 OG1 THR A 289 17194 15759 10055 -1326 -1999 -1282 O
ATOM 1719 CG2 THR A 289 6.320 -2.522 117.162 1.00113.80 C
ANISOU 1719 CG2 THR A 289 17358 16204 9677 -1297 -2350 -1320 C
ATOM 1720 N PRO A 290 4.843 0.126 119.137 1.00110.39 N
ANISOU 1720 N PRO A 290 17286 15759 8899 -1596 -2089 -1813 N
ATOM 1721 CA PRO A 290 5.097 0.389 120.564 1.00111.23 C
ANISOU 1721 CA PRO A 290 17524 16064 8675 -1649 -2201 -1936 C
ATOM 1722 C PRO A 290 3.868 0.183 121.432 1.00 95.96 C
ANISOU 1722 C PRO A 290 15830 14105 6523 -1610 -2039 -1884 C
ATOM 1723 O PRO A 290 3.979 -0.305 122.565 1.00104.92 O
ANISOU 1723 O PRO A 290 17098 15413 7353 -1565 -2141 -1845 O
ATOM 1724 CB PRO A 290 5.573 1.847 120.584 1.00 96.58 C
ANISOU 1724 CB PRO A 290 15626 14192 6878 -1845 -2191 -2237 C
ATOM 1725 CG PRO A 290 6.011 2.134 119.192 1.00 98.36 C
ANISOU 1725 CG PRO A 290 15663 14264 7447 -1876 -2155 -2242 C
ATOM 1726 CD PRO A 290 5.112 1.323 118.317 1.00102.11 C
ANISOU 1726 CD PRO A 290 16134 14573 8089 -1722 -2013 -2000 C
ATOM 1727 N PHE A 291 2.687 0.509 120.903 1.00 94.12 N
ANISOU 1727 N PHE A 291 15652 13678 6431 -1612 -1782 -1879 N
ATOM 1728 CA PHE A 291 1.465 0.427 121.695 1.00 94.73 C
ANISOU 1728 CA PHE A 291 15935 13744 6312 -1594 -1602 -1864 C
ATOM 1729 C PHE A 291 1.181 -1.008 122.120 1.00 94.99 C
ANISOU 1729 C PHE A 291 16066 13846 6181 -1484 -1617 -1626 C
ATOM 1730 O PHE A 291 0.990 -1.294 123.309 1.00 97.13 O
ANISOU 1730 O PHE A 291 16526 14231 6147 -1474 -1634 -1613 O
ATOM 1731 CB PHE A 291 0.293 0.995 120.887 1.00110.38 C
ANISOU 1731 CB PHE A 291 17905 15541 8495 -1585 -1331 -1901 C
ATOM 1732 CG PHE A 291 -1.024 0.958 121.606 1.00107.48 C
ANISOU 1732 CG PHE A 291 17710 15181 7945 -1568 -1124 -1906 C
ATOM 1733 CD1 PHE A 291 -1.425 2.018 122.402 1.00102.16 C
ANISOU 1733 CD1 PHE A 291 17181 14513 7123 -1632 -1030 -2104 C
ATOM 1734 CD2 PHE A 291 -1.871 -0.133 121.479 1.00108.51 C
ANISOU 1734 CD2 PHE A 291 17863 15313 8053 -1502 -1002 -1728 C
ATOM 1735 CE1 PHE A 291 -2.639 1.987 123.064 1.00 95.78 C
ANISOU 1735 CE1 PHE A 291 16520 13727 6146 -1611 -832 -2116 C
ATOM 1736 CE2 PHE A 291 -3.084 -0.169 122.140 1.00107.61 C
ANISOU 1736 CE2 PHE A 291 17890 15226 7769 -1507 -796 -1751 C
ATOM 1737 CZ PHE A 291 -3.468 0.893 122.932 1.00 94.92 C
ANISOU 1737 CZ PHE A 291 16410 13639 6015 -1552 -717 -1942 C
ATOM 1738 N PHE A 292 1.167 -1.929 121.159 1.00101.07 N
ANISOU 1738 N PHE A 292 16731 14533 7139 -1404 -1597 -1438 N
ATOM 1739 CA PHE A 292 0.854 -3.312 121.488 1.00113.42 C
ANISOU 1739 CA PHE A 292 18424 16114 8557 -1312 -1563 -1213 C
ATOM 1740 C PHE A 292 2.029 -4.036 122.127 1.00123.91 C
ANISOU 1740 C PHE A 292 19798 17596 9687 -1213 -1818 -1104 C
ATOM 1741 O PHE A 292 1.810 -4.949 122.925 1.00121.35 O
ANISOU 1741 O PHE A 292 19681 17316 9109 -1132 -1796 -956 O
ATOM 1742 CB PHE A 292 0.339 -4.027 120.240 1.00 90.84 C
ANISOU 1742 CB PHE A 292 15453 13105 5958 -1279 -1418 -1071 C
ATOM 1743 CG PHE A 292 -1.006 -3.532 119.814 1.00 89.49 C
ANISOU 1743 CG PHE A 292 15262 12844 5895 -1339 -1152 -1157 C
ATOM 1744 CD1 PHE A 292 -2.155 -4.093 120.339 1.00 90.11 C
ANISOU 1744 CD1 PHE A 292 15496 12928 5816 -1361 -941 -1108 C
ATOM 1745 CD2 PHE A 292 -1.122 -2.459 118.949 1.00 87.96 C
ANISOU 1745 CD2 PHE A 292 14906 12579 5936 -1364 -1104 -1299 C
ATOM 1746 CE1 PHE A 292 -3.393 -3.622 119.979 1.00 89.20 C
ANISOU 1746 CE1 PHE A 292 15329 12783 5780 -1402 -705 -1206 C
ATOM 1747 CE2 PHE A 292 -2.362 -1.984 118.584 1.00 87.07 C
ANISOU 1747 CE2 PHE A 292 14770 12419 5892 -1373 -868 -1377 C
ATOM 1748 CZ PHE A 292 -3.495 -2.560 119.106 1.00 87.70 C
ANISOU 1748 CZ PHE A 292 14964 12544 5815 -1389 -677 -1338 C
ATOM 1749 N PHE A 293 3.264 -3.608 121.859 1.00124.59 N
ANISOU 1749 N PHE A 293 19703 17781 9855 -1211 -2050 -1187 N
ATOM 1750 CA PHE A 293 4.392 -4.132 122.622 1.00131.11 C
ANISOU 1750 CA PHE A 293 20550 18826 10439 -1099 -2314 -1127 C
ATOM 1751 C PHE A 293 4.220 -3.824 124.104 1.00139.96 C
ANISOU 1751 C PHE A 293 21879 20113 11188 -1119 -2351 -1220 C
ATOM 1752 O PHE A 293 4.336 -4.713 124.962 1.00153.30 O
ANISOU 1752 O PHE A 293 23755 21912 12582 -977 -2416 -1064 O
ATOM 1753 CB PHE A 293 5.692 -3.531 122.082 1.00130.50 C
ANISOU 1753 CB PHE A 293 20201 18865 10519 -1136 -2540 -1264 C
ATOM 1754 CG PHE A 293 6.933 -3.961 122.819 1.00139.09 C
ANISOU 1754 CG PHE A 293 21247 20246 11357 -1012 -2836 -1241 C
ATOM 1755 CD1 PHE A 293 6.996 -5.175 123.487 1.00142.09 C
ANISOU 1755 CD1 PHE A 293 21809 20711 11469 -796 -2897 -1007 C
ATOM 1756 CD2 PHE A 293 8.045 -3.138 122.835 1.00141.79 C
ANISOU 1756 CD2 PHE A 293 21365 20789 11718 -1106 -3044 -1464 C
ATOM 1757 CE1 PHE A 293 8.145 -5.552 124.160 1.00144.28 C
ANISOU 1757 CE1 PHE A 293 22039 21290 11490 -635 -3180 -984 C
ATOM 1758 CE2 PHE A 293 9.194 -3.510 123.502 1.00144.38 C
ANISOU 1758 CE2 PHE A 293 21611 21445 11801 -981 -3330 -1468 C
ATOM 1759 CZ PHE A 293 9.245 -4.718 124.165 1.00144.52 C
ANISOU 1759 CZ PHE A 293 21804 21567 11540 -723 -3408 -1220 C
ATOM 1760 N VAL A 294 3.887 -2.572 124.422 1.00132.76 N
ANISOU 1760 N VAL A 294 20967 19202 10273 -1285 -2285 -1468 N
ATOM 1761 CA VAL A 294 3.739 -2.189 125.819 1.00126.54 C
ANISOU 1761 CA VAL A 294 20371 18575 9133 -1321 -2317 -1584 C
ATOM 1762 C VAL A 294 2.518 -2.854 126.439 1.00118.35 C
ANISOU 1762 C VAL A 294 19607 17449 7910 -1271 -2097 -1438 C
ATOM 1763 O VAL A 294 2.576 -3.349 127.570 1.00116.02 O
ANISOU 1763 O VAL A 294 19517 17299 7267 -1189 -2159 -1369 O
ATOM 1764 CB VAL A 294 3.675 -0.659 125.939 1.00120.37 C
ANISOU 1764 CB VAL A 294 19540 17784 8412 -1522 -2270 -1898 C
ATOM 1765 CG1 VAL A 294 3.159 -0.270 127.304 1.00120.93 C
ANISOU 1765 CG1 VAL A 294 19846 17960 8142 -1572 -2219 -2012 C
ATOM 1766 CG2 VAL A 294 5.052 -0.069 125.707 1.00118.86 C
ANISOU 1766 CG2 VAL A 294 19120 17752 8289 -1599 -2512 -2071 C
ATOM 1767 N GLN A 295 1.395 -2.883 125.716 1.00116.12 N
ANISOU 1767 N GLN A 295 19330 16948 7843 -1319 -1829 -1396 N
ATOM 1768 CA GLN A 295 0.201 -3.509 126.272 1.00116.43 C
ANISOU 1768 CA GLN A 295 19605 16919 7714 -1305 -1594 -1285 C
ATOM 1769 C GLN A 295 0.387 -5.007 126.477 1.00120.66 C
ANISOU 1769 C GLN A 295 20292 17456 8098 -1157 -1616 -1007 C
ATOM 1770 O GLN A 295 -0.171 -5.569 127.426 1.00122.38 O
ANISOU 1770 O GLN A 295 20777 17694 8029 -1128 -1505 -919 O
ATOM 1771 CB GLN A 295 -1.005 -3.235 125.373 1.00118.91 C
ANISOU 1771 CB GLN A 295 19841 17047 8292 -1384 -1313 -1320 C
ATOM 1772 CG GLN A 295 -2.056 -2.337 126.008 1.00125.83 C
ANISOU 1772 CG GLN A 295 20828 17921 9060 -1479 -1115 -1500 C
ATOM 1773 CD GLN A 295 -1.518 -0.960 126.355 1.00131.30 C
ANISOU 1773 CD GLN A 295 21478 18678 9733 -1555 -1230 -1749 C
ATOM 1774 OE1 GLN A 295 -2.063 -0.360 127.410 1.00134.58 O
ANISOU 1774 OE1 GLN A 295 21408 18778 10036 -1575 -1383 -1825 O
ATOM 1775 NE2 GLN A 295 -0.623 -0.443 125.686 1.00132.18 N
ANISOU 1775 NE2 GLN A 295 22070 19153 9910 -1613 -1139 -1888 N
ATOM 1776 N MET A 296 1.167 -5.669 125.615 1.00122.32 N
ANISOU 1776 N MET A 296 20360 17632 8485 -1058 -1742 -866 N
ATOM 1777 CA MET A 296 1.476 -7.077 125.832 1.00123.00 C
ANISOU 1777 CA MET A 296 20619 17707 8410 -886 -1769 -598 C
ATOM 1778 C MET A 296 2.385 -7.257 127.038 1.00128.25 C
ANISOU 1778 C MET A 296 21426 18607 8696 -738 -2010 -564 C
ATOM 1779 O MET A 296 2.247 -8.231 127.787 1.00129.04 O
ANISOU 1779 O MET A 296 21813 18710 8507 -603 -1958 -371 O
ATOM 1780 CB MET A 296 2.127 -7.663 124.580 1.00111.90 C
ANISOU 1780 CB MET A 296 19015 16210 7293 -806 -1845 -471 C
ATOM 1781 CG MET A 296 1.851 -9.137 124.372 1.00111.27 C
ANISOU 1781 CG MET A 296 19131 15978 7171 -692 -1698 -199 C
ATOM 1782 SD MET A 296 0.112 -9.453 124.029 1.00112.95 S
ANISOU 1782 SD MET A 296 19463 15965 7487 -877 -1276 -192 S
ATOM 1783 CE MET A 296 0.152 -11.229 123.813 1.00114.46 C
ANISOU 1783 CE MET A 296 19902 15980 7608 -748 -1139 120 C
ATOM 1784 N TRP A 297 3.323 -6.329 127.238 1.00129.17 N
ANISOU 1784 N TRP A 297 21351 18933 8794 -762 -2267 -758 N
ATOM 1785 CA TRP A 297 4.178 -6.398 128.417 1.00137.38 C
ANISOU 1785 CA TRP A 297 22488 20259 9449 -628 -2513 -768 C
ATOM 1786 C TRP A 297 3.384 -6.170 129.697 1.00134.13 C
ANISOU 1786 C TRP A 297 22365 19897 8702 -680 -2390 -824 C
ATOM 1787 O TRP A 297 3.724 -6.725 130.749 1.00130.96 O
ANISOU 1787 O TRP A 297 22178 19667 7916 -514 -2498 -719 O
ATOM 1788 CB TRP A 297 5.306 -5.371 128.298 1.00145.82 C
ANISOU 1788 CB TRP A 297 23257 21560 10590 -700 -2790 -1015 C
ATOM 1789 CG TRP A 297 6.419 -5.570 129.283 1.00153.68 C
ANISOU 1789 CG TRP A 297 24261 22914 11217 -531 -3098 -1025 C
ATOM 1790 CD1 TRP A 297 6.696 -6.704 129.985 1.00158.64 C
ANISOU 1790 CD1 TRP A 297 25109 23655 11514 -254 -3180 -779 C
ATOM 1791 CD2 TRP A 297 7.406 -4.605 129.676 1.00157.78 C
ANISOU 1791 CD2 TRP A 297 24559 23746 11644 -620 -3357 -1303 C
ATOM 1792 NE1 TRP A 297 7.790 -6.509 130.792 1.00162.87 N
ANISOU 1792 NE1 TRP A 297 25555 24583 11743 -135 -3495 -880 N
ATOM 1793 CE2 TRP A 297 8.246 -5.229 130.621 1.00163.64 C
ANISOU 1793 CE2 TRP A 297 25367 24824 11984 -375 -3611 -1215 C
ATOM 1794 CE3 TRP A 297 7.660 -3.276 129.322 1.00158.19 C
ANISOU 1794 CE3 TRP A 297 24377 23827 11902 -885 -3384 -1625 C
ATOM 1795 CZ2 TRP A 297 9.322 -4.571 131.216 1.00167.88 C
ANISOU 1795 CZ2 TRP A 297 25702 25765 12319 -401 -3907 -1458 C
ATOM 1796 CZ3 TRP A 297 8.730 -2.624 129.913 1.00162.68 C
ANISOU 1796 CZ3 TRP A 297 24772 24757 12282 -942 -3652 -1870 C
ATOM 1797 CH2 TRP A 297 9.547 -3.273 130.850 1.00167.19 C
ANISOU 1797 CH2 TRP A 297 25371 25700 12451 -708 -3919 -1796 C
ATOM 1798 N SER A 298 2.318 -5.372 129.621 1.00133.69 N
ANISOU 1798 N SER A 298 22323 19699 8772 -889 -2158 -985 N
ATOM 1799 CA SER A 298 1.590 -4.970 130.819 1.00134.39 C
ANISOU 1799 CA SER A 298 22654 19850 8560 -961 -2043 -1084 C
ATOM 1800 C SER A 298 0.863 -6.133 131.485 1.00136.89 C
ANISOU 1800 C SER A 298 23317 20083 8612 -854 -1851 -842 C
ATOM 1801 O SER A 298 0.643 -6.103 132.702 1.00139.52 O
ANISOU 1801 O SER A 298 23895 20536 8581 -831 -1838 -862 O
ATOM 1802 CB SER A 298 0.600 -3.859 130.472 1.00134.15 C
ANISOU 1802 CB SER A 298 22544 19677 8748 -1180 -1821 -1305 C
ATOM 1803 OG SER A 298 -0.338 -3.671 131.515 1.00133.79 O
ANISOU 1803 OG SER A 298 22753 19644 8439 -1240 -1638 -1361 O
ATOM 1804 N VAL A 299 0.475 -7.155 130.723 1.00135.32 N
ANISOU 1804 N VAL A 299 23163 19675 8577 -802 -1685 -624 N
ATOM 1805 CA VAL A 299 -0.378 -8.220 131.238 1.00134.01 C
ANISOU 1805 CA VAL A 299 23342 19374 8201 -761 -1424 -419 C
ATOM 1806 C VAL A 299 0.352 -9.555 131.322 1.00138.59 C
ANISOU 1806 C VAL A 299 24107 19938 8613 -510 -1512 -124 C
ATOM 1807 O VAL A 299 -0.291 -10.594 131.511 1.00140.27 O
ANISOU 1807 O VAL A 299 24618 19975 8702 -478 -1262 76 O
ATOM 1808 CB VAL A 299 -1.668 -8.353 130.411 1.00119.84 C
ANISOU 1808 CB VAL A 299 21508 17338 6689 -943 -1075 -430 C
ATOM 1809 CG1 VAL A 299 -2.455 -7.053 130.443 1.00118.69 C
ANISOU 1809 CG1 VAL A 299 21221 17219 6655 -1138 -969 -706 C
ATOM 1810 CG2 VAL A 299 -1.351 -8.758 128.981 1.00109.82 C
ANISOU 1810 CG2 VAL A 299 19999 15931 5797 -926 -1095 -346 C
ATOM 1811 N TRP A 300 1.672 -9.563 131.193 1.00139.11 N
ANISOU 1811 N TRP A 300 24014 20184 8658 -329 -1845 -96 N
ATOM 1812 CA TRP A 300 2.424 -10.810 131.188 1.00143.32 C
ANISOU 1812 CA TRP A 300 24704 20708 9041 -44 -1937 189 C
ATOM 1813 C TRP A 300 3.525 -10.776 132.246 1.00163.19 C
ANISOU 1813 C TRP A 300 27284 23562 11157 202 -2265 204 C
ATOM 1814 O TRP A 300 3.641 -9.829 133.028 1.00173.34 O
ANISOU 1814 O TRP A 300 28514 25079 12270 120 -2399 -13 O
ATOM 1815 CB TRP A 300 2.968 -11.105 129.788 1.00137.93 C
ANISOU 1815 CB TRP A 300 23743 19916 8748 -12 -2005 250 C
ATOM 1816 CG TRP A 300 1.899 -11.658 128.884 1.00131.07 C
ANISOU 1816 CG TRP A 300 22928 18713 8158 -168 -1655 333 C
ATOM 1817 CD1 TRP A 300 1.386 -11.079 127.758 1.00120.01 C
ANISOU 1817 CD1 TRP A 300 21241 17190 7169 -385 -1548 186 C
ATOM 1818 CD2 TRP A 300 1.187 -12.890 129.059 1.00130.70 C
ANISOU 1818 CD2 TRP A 300 23252 18432 7977 -129 -1354 565 C
ATOM 1819 NE1 TRP A 300 0.411 -11.882 127.214 1.00112.26 N
ANISOU 1819 NE1 TRP A 300 20393 15947 6314 -483 -1219 301 N
ATOM 1820 CE2 TRP A 300 0.270 -12.999 127.995 1.00116.48 C
ANISOU 1820 CE2 TRP A 300 21333 16398 6526 -351 -1083 525 C
ATOM 1821 CE3 TRP A 300 1.242 -13.915 130.010 1.00137.99 C
ANISOU 1821 CE3 TRP A 300 24609 19318 8504 73 -1273 800 C
ATOM 1822 CZ2 TRP A 300 -0.584 -14.091 127.854 1.00112.47 C
ANISOU 1822 CZ2 TRP A 300 21106 15633 5993 -415 -732 685 C
ATOM 1823 CZ3 TRP A 300 0.395 -14.999 129.868 1.00134.04 C
ANISOU 1823 CZ3 TRP A 300 24426 18520 7984 16 -905 978 C
ATOM 1824 CH2 TRP A 300 -0.505 -15.079 128.798 1.00124.01 C
ANISOU 1824 CH2 TRP A 300 23010 17032 7077 -245 -636 908 C
ATOM 1825 N ASP A 301 4.337 -11.839 132.251 1.00175.04 N
ANISOU 1825 N ASP A 301 28906 25100 12500 518 -2387 459 N
ATOM 1826 CA ASP A 301 5.061 -12.233 133.457 1.00185.85 C
ANISOU 1826 CA ASP A 301 30394 26741 13479 804 -2562 569 C
ATOM 1827 C ASP A 301 6.022 -11.153 133.939 1.00190.67 C
ANISOU 1827 C ASP A 301 30667 27779 14000 795 -2924 306 C
ATOM 1828 O ASP A 301 6.152 -10.927 135.148 1.00192.28 O
ANISOU 1828 O ASP A 301 30913 28224 13920 847 -2992 255 O
ATOM 1829 CB ASP A 301 5.818 -13.535 133.196 1.00187.54 C
ANISOU 1829 CB ASP A 301 30701 26908 13649 1155 -2611 885 C
ATOM 1830 CG ASP A 301 6.656 -13.969 134.379 1.00191.38 C
ANISOU 1830 CG ASP A 301 31227 27692 13798 1468 -2792 1009 C
ATOM 1831 OD1 ASP A 301 6.074 -14.218 135.457 1.00193.32 O
ANISOU 1831 OD1 ASP A 301 31747 27911 13795 1482 -2622 1081 O
ATOM 1832 OD2 ASP A 301 7.895 -14.059 134.229 1.00191.63 O
ANISOU 1832 OD2 ASP A 301 31004 27993 13812 1695 -3101 1028 O
ATOM 1833 N ALA A 302 6.693 -10.465 133.022 1.00190.88 N
ANISOU 1833 N ALA A 302 30358 27906 14261 708 -3147 122 N
ATOM 1834 CA ALA A 302 7.601 -9.401 133.422 1.00187.53 C
ANISOU 1834 CA ALA A 302 29599 27882 13774 643 -3461 -167 C
ATOM 1835 C ALA A 302 6.791 -8.131 133.639 1.00180.03 C
ANISOU 1835 C ALA A 302 28635 26878 12888 285 -3345 -474 C
ATOM 1836 O ALA A 302 6.135 -7.641 132.714 1.00178.40 O
ANISOU 1836 O ALA A 302 28309 26402 13071 38 -3156 -570 O
ATOM 1837 CB ALA A 302 8.688 -9.198 132.369 1.00186.33 C
ANISOU 1837 CB ALA A 302 29076 27858 13864 682 -3721 -252 C
ATOM 1838 N ASN A 303 6.829 -7.597 134.857 1.00178.38 N
ANISOU 1838 N ASN A 303 28436 26926 12416 249 -3400 -617 N
ATOM 1839 CA ASN A 303 5.998 -6.454 135.229 1.00180.82 C
ANISOU 1839 CA ASN A 303 28773 27176 12756 -57 -3251 -891 C
ATOM 1840 C ASN A 303 6.897 -5.300 135.666 1.00184.46 C
ANISOU 1840 C ASN A 303 28931 28010 13144 -182 -3519 -1233 C
ATOM 1841 O ASN A 303 7.440 -5.306 136.776 1.00184.97 O
ANISOU 1841 O ASN A 303 28966 28421 12894 -80 -3669 -1266 O
ATOM 1842 CB ASN A 303 5.005 -6.833 136.324 1.00182.12 C
ANISOU 1842 CB ASN A 303 29267 27257 12675 -25 -2999 -773 C
ATOM 1843 CG ASN A 303 3.857 -5.849 136.426 1.00179.87 C
ANISOU 1843 CG ASN A 303 29046 26792 12506 -326 -2752 -996 C
ATOM 1844 OD1 ASN A 303 3.971 -4.701 135.993 1.00178.50 O
ANISOU 1844 OD1 ASN A 303 28661 26636 12524 -549 -2811 -1281 O
ATOM 1845 ND2 ASN A 303 2.742 -6.293 136.989 1.00179.16 N
ANISOU 1845 ND2 ASN A 303 29246 26517 12310 -334 -2454 -867 N
ATOM 1846 N ALA A 304 6.960 -4.265 134.824 1.00185.12 N
ANISOU 1846 N ALA A 304 28794 28021 13522 -431 -3561 -1487 N
ATOM 1847 CA ALA A 304 7.729 -3.024 135.082 1.00193.24 C
ANISOU 1847 CA ALA A 304 29552 29323 14547 -632 -3738 -1866 C
ATOM 1848 C ALA A 304 6.972 -1.888 134.388 1.00194.72 C
ANISOU 1848 C ALA A 304 29758 29210 15016 -973 -3492 -2095 C
ATOM 1849 O ALA A 304 7.452 -1.411 133.344 1.00192.62 O
ANISOU 1849 O ALA A 304 29278 28789 15120 -1136 -3464 -2198 O
ATOM 1850 CB ALA A 304 9.124 -3.173 134.533 1.00196.11 C
ANISOU 1850 CB ALA A 304 29567 29937 15009 -597 -4049 -1955 C
ATOM 1851 N PRO A 305 5.835 -1.413 134.941 1.00196.91 N
ANISOU 1851 N PRO A 305 30243 29394 15182 -1051 -3274 -2164 N
ATOM 1852 CA PRO A 305 4.985 -0.440 134.241 1.00195.03 C
ANISOU 1852 CA PRO A 305 30064 28836 15203 -1314 -2986 -2320 C
ATOM 1853 C PRO A 305 5.454 0.976 133.867 1.00195.16 C
ANISOU 1853 C PRO A 305 29827 28825 15498 -1570 -3029 -2631 C
ATOM 1854 O PRO A 305 5.393 1.219 132.673 1.00196.93 O
ANISOU 1854 O PRO A 305 29922 28820 16083 -1634 -2942 -2590 O
ATOM 1855 CB PRO A 305 3.797 -0.261 135.204 1.00196.72 C
ANISOU 1855 CB PRO A 305 30471 29101 15174 -1325 -2844 -2414 C
ATOM 1856 CG PRO A 305 3.834 -1.486 136.089 1.00199.59 C
ANISOU 1856 CG PRO A 305 30984 29659 15190 -1044 -2939 -2154 C
ATOM 1857 CD PRO A 305 5.307 -1.786 136.250 1.00200.99 C
ANISOU 1857 CD PRO A 305 30947 30107 15315 -881 -3271 -2088 C
ATOM 1858 N LYS A 306 6.038 1.754 134.797 1.00201.82 N
ANISOU 1858 N LYS A 306 30563 29869 16250 -1684 -3126 -2934 N
ATOM 1859 CA LYS A 306 6.434 3.177 134.547 1.00201.93 C
ANISOU 1859 CA LYS A 306 30368 29829 16528 -1947 -3124 -3253 C
ATOM 1860 C LYS A 306 5.338 3.814 133.682 1.00213.01 C
ANISOU 1860 C LYS A 306 31883 30828 18223 -2121 -2797 -3294 C
ATOM 1861 O LYS A 306 5.667 4.356 132.610 1.00206.67 O
ANISOU 1861 O LYS A 306 30946 29865 17717 -2247 -2757 -3351 O
ATOM 1862 CB LYS A 306 7.784 3.234 133.826 1.00190.25 C
ANISOU 1862 CB LYS A 306 28583 28513 15189 -1940 -3376 -3259 C
ATOM 1863 CG LYS A 306 8.332 4.633 133.577 1.00183.81 C
ANISOU 1863 CG LYS A 306 27517 27766 14555 -2191 -3442 -3622 C
ATOM 1864 CD LYS A 306 9.771 4.639 133.107 1.00180.24 C
ANISOU 1864 CD LYS A 306 26772 27374 14337 -2213 -3597 -3596 C
ATOM 1865 CE LYS A 306 9.936 4.125 131.692 1.00180.96 C
ANISOU 1865 CE LYS A 306 26591 27599 14566 -2443 -3696 -3950 C
ATOM 1866 NZ LYS A 306 11.319 4.319 131.195 1.00169.30 N
ANISOU 1866 NZ LYS A 306 24865 26044 13418 -2553 -3715 -3973 N
ATOM 1867 N GLU A 307 4.087 3.700 134.140 1.00223.83 N
ANISOU 1867 N GLU A 307 33500 32047 19499 -2107 -2555 -3267 N
ATOM 1868 CA GLU A 307 2.903 4.025 133.347 1.00218.53 C
ANISOU 1868 CA GLU A 307 32952 31020 19058 -2178 -2242 -3233 C
ATOM 1869 C GLU A 307 3.013 5.382 132.658 1.00208.97 C
ANISOU 1869 C GLU A 307 31655 29628 18118 -2399 -2122 -3514 C
ATOM 1870 O GLU A 307 2.536 5.549 131.529 1.00205.13 O
ANISOU 1870 O GLU A 307 31112 28871 17959 -2396 -1950 -3450 O
ATOM 1871 CB GLU A 307 1.670 4.005 134.250 1.00224.21 C
ANISOU 1871 CB GLU A 307 33919 31664 19608 -2119 -2010 -3186 C
ATOM 1872 CG GLU A 307 1.265 2.631 134.747 1.00229.49 C
ANISOU 1872 CG GLU A 307 34732 32406 20056 -1913 -2020 -2876 C
ATOM 1873 CD GLU A 307 -0.002 2.674 135.582 1.00233.67 C
ANISOU 1873 CD GLU A 307 35487 32851 20448 -1886 -1756 -2852 C
ATOM 1874 OE1 GLU A 307 -0.417 3.787 135.974 1.00236.69 O
ANISOU 1874 OE1 GLU A 307 35905 33173 20852 -2003 -1617 -3088 O
ATOM 1875 OE2 GLU A 307 -0.584 1.596 135.839 1.00234.38 O
ANISOU 1875 OE2 GLU A 307 35721 32923 20409 -1752 -1671 -2601 O
ATOM 1876 N ALA A 308 3.646 6.363 133.307 1.00196.12 N
ANISOU 1876 N ALA A 308 29967 28117 16432 -2540 -2185 -3803 N
ATOM 1877 CA ALA A 308 3.653 7.710 132.742 1.00184.55 C
ANISOU 1877 CA ALA A 308 28486 26427 15209 -2753 -2010 -4072 C
ATOM 1878 C ALA A 308 4.611 7.807 131.561 1.00170.70 C
ANISOU 1878 C ALA A 308 26504 24647 13709 -2858 -2124 -4118 C
ATOM 1879 O ALA A 308 4.249 8.318 130.495 1.00165.09 O
ANISOU 1879 O ALA A 308 25808 23643 13274 -2923 -1930 -4141 O
ATOM 1880 CB ALA A 308 4.015 8.732 133.819 1.00187.44 C
ANISOU 1880 CB ALA A 308 28883 26899 15438 -2892 -2012 -4372 C
ATOM 1881 N SER A 309 5.838 7.314 131.731 1.00164.42 N
ANISOU 1881 N SER A 309 25481 24160 12832 -2846 -2431 -4125 N
ATOM 1882 CA SER A 309 6.820 7.363 130.656 1.00155.99 C
ANISOU 1882 CA SER A 309 24164 23106 12000 -2945 -2550 -4176 C
ATOM 1883 C SER A 309 6.482 6.435 129.495 1.00146.09 C
ANISOU 1883 C SER A 309 22831 21675 11001 -2753 -2519 -3848 C
ATOM 1884 O SER A 309 6.956 6.673 128.380 1.00147.01 O
ANISOU 1884 O SER A 309 22766 21658 11432 -2815 -2501 -3868 O
ATOM 1885 CB SER A 309 8.201 7.021 131.204 1.00161.03 C
ANISOU 1885 CB SER A 309 24540 24153 12491 -2926 -2888 -4255 C
ATOM 1886 OG SER A 309 8.586 7.945 132.210 1.00164.42 O
ANISOU 1886 OG SER A 309 24972 24706 12793 -3069 -2900 -4549 O
ATOM 1887 N ALA A 310 5.690 5.385 129.723 1.00140.62 N
ANISOU 1887 N ALA A 310 22256 20962 10210 -2515 -2492 -3545 N
ATOM 1888 CA ALA A 310 5.427 4.383 128.693 1.00129.89 C
ANISOU 1888 CA ALA A 310 20800 19456 9097 -2317 -2468 -3225 C
ATOM 1889 C ALA A 310 4.035 4.519 128.088 1.00128.81 C
ANISOU 1889 C ALA A 310 20801 18974 9168 -2263 -2145 -3111 C
ATOM 1890 O ALA A 310 3.899 4.743 126.878 1.00134.40 O
ANISOU 1890 O ALA A 310 21395 19456 10213 -2265 -2028 -3072 O
ATOM 1891 CB ALA A 310 5.612 2.973 129.267 1.00125.19 C
ANISOU 1891 CB ALA A 310 20231 19084 8253 -2085 -2658 -2954 C
ATOM 1892 N PHE A 311 2.996 4.356 128.912 1.00126.45 N
ANISOU 1892 N PHE A 311 20735 18656 8654 -2204 -2002 -3056 N
ATOM 1893 CA PHE A 311 1.636 4.304 128.389 1.00125.41 C
ANISOU 1893 CA PHE A 311 20699 18266 8683 -2124 -1710 -2933 C
ATOM 1894 C PHE A 311 1.268 5.607 127.694 1.00126.78 C
ANISOU 1894 C PHE A 311 20872 18197 9101 -2232 -1496 -3132 C
ATOM 1895 O PHE A 311 0.655 5.593 126.618 1.00130.97 O
ANISOU 1895 O PHE A 311 21335 18520 9908 -2151 -1331 -3027 O
ATOM 1896 CB PHE A 311 0.650 4.004 129.522 1.00132.87 C
ANISOU 1896 CB PHE A 311 21892 19268 9323 -2072 -1589 -2887 C
ATOM 1897 CG PHE A 311 0.662 2.569 129.990 1.00142.12 C
ANISOU 1897 CG PHE A 311 23123 20584 10294 -1919 -1699 -2618 C
ATOM 1898 CD1 PHE A 311 1.853 1.880 130.163 1.00144.65 C
ANISOU 1898 CD1 PHE A 311 23343 21115 10502 -1853 -1993 -2534 C
ATOM 1899 CD2 PHE A 311 -0.526 1.916 130.281 1.00144.60 C
ANISOU 1899 CD2 PHE A 311 23604 20825 10514 -1835 -1491 -2458 C
ATOM 1900 CE1 PHE A 311 1.860 0.566 130.597 1.00142.65 C
ANISOU 1900 CE1 PHE A 311 23191 20964 10046 -1680 -2069 -2272 C
ATOM 1901 CE2 PHE A 311 -0.526 0.602 130.719 1.00144.37 C
ANISOU 1901 CE2 PHE A 311 23678 20888 10290 -1706 -1552 -2211 C
ATOM 1902 CZ PHE A 311 0.668 -0.073 130.876 1.00141.66 C
ANISOU 1902 CZ PHE A 311 23270 20722 9833 -1615 -1838 -2108 C
ATOM 1903 N ILE A 312 1.695 6.739 128.259 1.00125.14 N
ANISOU 1903 N ILE A 312 20743 18015 8790 -2411 -1495 -3424 N
ATOM 1904 CA ILE A 312 1.379 8.027 127.651 1.00126.81 C
ANISOU 1904 CA ILE A 312 21011 17964 9209 -2506 -1263 -3617 C
ATOM 1905 C ILE A 312 2.013 8.131 126.274 1.00127.93 C
ANISOU 1905 C ILE A 312 20946 17964 9697 -2517 -1289 -3580 C
ATOM 1906 O ILE A 312 1.358 8.520 125.302 1.00130.79 O
ANISOU 1906 O ILE A 312 21314 18073 10305 -2438 -1075 -3532 O
ATOM 1907 CB ILE A 312 1.832 9.178 128.569 1.00129.66 C
ANISOU 1907 CB ILE A 312 21517 18376 9373 -2728 -1254 -3957 C
ATOM 1908 CG1 ILE A 312 0.967 9.236 129.832 1.00124.16 C
ANISOU 1908 CG1 ILE A 312 21060 17758 8356 -2702 -1157 -4001 C
ATOM 1909 CG2 ILE A 312 1.802 10.505 127.823 1.00134.04 C
ANISOU 1909 CG2 ILE A 312 22136 18632 10160 -2844 -1024 -4162 C
ATOM 1910 CD1 ILE A 312 -0.464 9.662 129.581 1.00120.78 C
ANISOU 1910 CD1 ILE A 312 20793 17083 8013 -2579 -827 -3961 C
ATOM 1911 N ILE A 313 3.273 7.717 126.152 1.00128.01 N
ANISOU 1911 N ILE A 313 20760 18157 9721 -2590 -1554 -3586 N
ATOM 1912 CA ILE A 313 3.992 7.880 124.892 1.00130.29 C
ANISOU 1912 CA ILE A 313 20850 18327 10327 -2631 -1580 -3581 C
ATOM 1913 C ILE A 313 3.412 6.967 123.816 1.00122.52 C
ANISOU 1913 C ILE A 313 19758 17219 9576 -2414 -1527 -3275 C
ATOM 1914 O ILE A 313 3.191 7.387 122.667 1.00121.61 O
ANISOU 1914 O ILE A 313 19595 16867 9745 -2387 -1372 -3253 O
ATOM 1915 CB ILE A 313 5.492 7.619 125.107 1.00137.04 C
ANISOU 1915 CB ILE A 313 21496 19461 11111 -2757 -1885 -3679 C
ATOM 1916 CG1 ILE A 313 6.132 8.800 125.830 1.00139.90 C
ANISOU 1916 CG1 ILE A 313 21929 19900 11327 -3037 -1885 -4053 C
ATOM 1917 CG2 ILE A 313 6.188 7.351 123.786 1.00138.48 C
ANISOU 1917 CG2 ILE A 313 21438 19566 11612 -2740 -1945 -3585 C
ATOM 1918 CD1 ILE A 313 7.624 8.680 125.962 1.00141.88 C
ANISOU 1918 CD1 ILE A 313 21932 20457 11518 -3189 -2168 -4203 C
ATOM 1919 N VAL A 314 3.172 5.699 124.165 1.00117.65 N
ANISOU 1919 N VAL A 314 19114 16757 8829 -2260 -1646 -3038 N
ATOM 1920 CA VAL A 314 2.646 4.770 123.171 1.00114.63 C
ANISOU 1920 CA VAL A 314 18632 16269 8654 -2084 -1589 -2765 C
ATOM 1921 C VAL A 314 1.238 5.181 122.746 1.00113.85 C
ANISOU 1921 C VAL A 314 18645 15953 8661 -2002 -1287 -2738 C
ATOM 1922 O VAL A 314 0.865 5.049 121.568 1.00112.72 O
ANISOU 1922 O VAL A 314 18395 15657 8776 -1909 -1180 -2626 O
ATOM 1923 CB VAL A 314 2.707 3.322 123.699 1.00113.60 C
ANISOU 1923 CB VAL A 314 18494 16329 8340 -1952 -1750 -2529 C
ATOM 1924 CG1 VAL A 314 4.148 2.940 124.018 1.00102.46 C
ANISOU 1924 CG1 VAL A 314 16945 15158 6826 -1982 -2059 -2551 C
ATOM 1925 CG2 VAL A 314 1.814 3.128 124.919 1.00102.29 C
ANISOU 1925 CG2 VAL A 314 17294 14973 6599 -1921 -1661 -2516 C
ATOM 1926 N MET A 315 0.447 5.727 123.680 1.00111.76 N
ANISOU 1926 N MET A 315 18587 15690 8188 -2025 -1144 -2855 N
ATOM 1927 CA MET A 315 -0.864 6.248 123.310 1.00110.90 C
ANISOU 1927 CA MET A 315 18570 15406 8161 -1930 -855 -2862 C
ATOM 1928 C MET A 315 -0.734 7.456 122.392 1.00110.60 C
ANISOU 1928 C MET A 315 18527 15140 8357 -1957 -712 -3007 C
ATOM 1929 O MET A 315 -1.542 7.636 121.472 1.00106.92 O
ANISOU 1929 O MET A 315 18030 14525 8071 -1816 -525 -2935 O
ATOM 1930 CB MET A 315 -1.657 6.607 124.567 1.00116.17 C
ANISOU 1930 CB MET A 315 19462 16135 8540 -1949 -735 -2972 C
ATOM 1931 CG MET A 315 -3.073 7.070 124.288 1.00119.47 C
ANISOU 1931 CG MET A 315 19961 16425 9007 -1821 -437 -2979 C
ATOM 1932 SD MET A 315 -3.214 8.842 123.974 1.00124.54 S
ANISOU 1932 SD MET A 315 20747 16824 9749 -1843 -216 -3234 S
ATOM 1933 CE MET A 315 -3.635 9.448 125.604 1.00123.95 C
ANISOU 1933 CE MET A 315 20945 16829 9320 -1934 -132 -3434 C
ATOM 1934 N LEU A 316 0.292 8.283 122.614 1.00114.02 N
ANISOU 1934 N LEU A 316 18994 15550 8780 -2139 -791 -3216 N
ATOM 1935 CA LEU A 316 0.503 9.436 121.745 1.00113.21 C
ANISOU 1935 CA LEU A 316 18925 15197 8891 -2186 -631 -3356 C
ATOM 1936 C LEU A 316 0.793 8.990 120.321 1.00 98.06 C
ANISOU 1936 C LEU A 316 16799 13187 7273 -2095 -662 -3188 C
ATOM 1937 O LEU A 316 0.250 9.551 119.364 1.00112.50 O
ANISOU 1937 O LEU A 316 18658 14799 9287 -1979 -457 -3167 O
ATOM 1938 CB LEU A 316 1.653 10.305 122.266 1.00119.13 C
ANISOU 1938 CB LEU A 316 19735 15959 9568 -2451 -710 -3632 C
ATOM 1939 CG LEU A 316 1.591 10.982 123.640 1.00106.64 C
ANISOU 1939 CG LEU A 316 18370 14455 7693 -2599 -677 -3868 C
ATOM 1940 CD1 LEU A 316 2.785 11.905 123.846 1.00109.22 C
ANISOU 1940 CD1 LEU A 316 18719 14771 8007 -2891 -724 -4166 C
ATOM 1941 CD2 LEU A 316 0.289 11.728 123.845 1.00107.00 C
ANISOU 1941 CD2 LEU A 316 18662 14310 7683 -2477 -371 -3914 C
ATOM 1942 N LEU A 317 1.613 7.948 120.162 1.00101.43 N
ANISOU 1942 N LEU A 317 17021 13783 7735 -2118 -912 -3056 N
ATOM 1943 CA LEU A 317 1.918 7.470 118.812 1.00 97.08 C
ANISOU 1943 CA LEU A 317 16270 13151 7464 -2034 -945 -2897 C
ATOM 1944 C LEU A 317 0.689 6.852 118.149 1.00 93.47 C
ANISOU 1944 C LEU A 317 15778 12641 7097 -1810 -804 -2685 C
ATOM 1945 O LEU A 317 0.414 7.095 116.955 1.00 90.55 O
ANISOU 1945 O LEU A 317 15341 12109 6954 -1707 -679 -2625 O
ATOM 1946 CB LEU A 317 3.062 6.457 118.859 1.00 95.96 C
ANISOU 1946 CB LEU A 317 15925 13216 7318 -2088 -1240 -2804 C
ATOM 1947 CG LEU A 317 4.388 6.934 119.452 1.00100.10 C
ANISOU 1947 CG LEU A 317 16409 13875 7749 -2309 -1418 -3021 C
ATOM 1948 CD1 LEU A 317 5.444 5.847 119.330 1.00 96.90 C
ANISOU 1948 CD1 LEU A 317 15770 13693 7354 -2292 -1705 -2896 C
ATOM 1949 CD2 LEU A 317 4.847 8.213 118.775 1.00105.19 C
ANISOU 1949 CD2 LEU A 317 17087 14303 8577 -2465 -1271 -3233 C
ATOM 1950 N ALA A 318 -0.063 6.051 118.911 1.00 97.37 N
ANISOU 1950 N ALA A 318 16314 13282 7402 -1739 -814 -2581 N
ATOM 1951 CA ALA A 318 -1.245 5.410 118.348 1.00102.04 C
ANISOU 1951 CA ALA A 318 16850 13864 8058 -1565 -672 -2411 C
ATOM 1952 C ALA A 318 -2.285 6.442 117.935 1.00110.41 C
ANISOU 1952 C ALA A 318 18004 14775 9172 -1449 -402 -2502 C
ATOM 1953 O ALA A 318 -2.990 6.257 116.936 1.00119.16 O
ANISOU 1953 O ALA A 318 19004 15839 10433 -1295 -283 -2399 O
ATOM 1954 CB ALA A 318 -1.829 4.420 119.355 1.00102.44 C
ANISOU 1954 CB ALA A 318 16961 14092 7869 -1550 -703 -2313 C
ATOM 1955 N SER A 319 -2.396 7.537 118.690 1.00107.15 N
ANISOU 1955 N SER A 319 17794 14295 8624 -1508 -298 -2698 N
ATOM 1956 CA SER A 319 -3.246 8.641 118.262 1.00106.02 C
ANISOU 1956 CA SER A 319 17770 13981 8530 -1370 -33 -2790 C
ATOM 1957 C SER A 319 -2.666 9.364 117.052 1.00102.78 C
ANISOU 1957 C SER A 319 17333 13353 8367 -1344 22 -2815 C
ATOM 1958 O SER A 319 -3.420 9.861 116.207 1.00 99.77 O
ANISOU 1958 O SER A 319 16967 12851 8089 -1143 218 -2786 O
ATOM 1959 CB SER A 319 -3.449 9.620 119.420 1.00107.89 C
ANISOU 1959 CB SER A 319 18264 14179 8550 -1448 76 -3000 C
ATOM 1960 OG SER A 319 -3.924 8.954 120.578 1.00107.57 O
ANISOU 1960 OG SER A 319 18263 14340 8266 -1482 24 -2978 O
ATOM 1961 N LEU A 320 -1.335 9.432 116.954 1.00104.54 N
ANISOU 1961 N LEU A 320 17512 13538 8672 -1537 -142 -2873 N
ATOM 1962 CA LEU A 320 -0.694 10.168 115.869 1.00105.64 C
ANISOU 1962 CA LEU A 320 17650 13455 9033 -1554 -71 -2918 C
ATOM 1963 C LEU A 320 -0.932 9.522 114.511 1.00101.88 C
ANISOU 1963 C LEU A 320 16971 12962 8777 -1376 -73 -2712 C
ATOM 1964 O LEU A 320 -0.933 10.219 113.492 1.00104.62 O
ANISOU 1964 O LEU A 320 17359 13105 9287 -1281 76 -2717 O
ATOM 1965 CB LEU A 320 0.806 10.286 116.145 1.00104.71 C
ANISOU 1965 CB LEU A 320 17491 13358 8937 -1830 -257 -3047 C
ATOM 1966 CG LEU A 320 1.683 10.975 115.098 1.00107.78 C
ANISOU 1966 CG LEU A 320 17867 13533 9552 -1917 -197 -3116 C
ATOM 1967 CD1 LEU A 320 1.246 12.417 114.888 1.00112.38 C
ANISOU 1967 CD1 LEU A 320 18738 13814 10146 -1878 115 -3269 C
ATOM 1968 CD2 LEU A 320 3.144 10.908 115.510 1.00107.09 C
ANISOU 1968 CD2 LEU A 320 17678 13559 9452 -2208 -410 -3257 C
ATOM 1969 N ASN A 321 -1.112 8.200 114.476 1.00 99.25 N
ANISOU 1969 N ASN A 321 16439 12830 8441 -1333 -226 -2534 N
ATOM 1970 CA ASN A 321 -1.243 7.504 113.187 1.00101.16 C
ANISOU 1970 CA ASN A 321 16476 13071 8890 -1198 -242 -2353 C
ATOM 1971 C ASN A 321 -2.416 8.038 112.352 1.00109.59 C
ANISOU 1971 C ASN A 321 17573 14050 10017 -945 -1 -2321 C
ATOM 1972 O ASN A 321 -2.286 8.288 111.132 1.00117.18 O
ANISOU 1972 O ASN A 321 18470 14886 11167 -838 62 -2265 O
ATOM 1973 CB ASN A 321 -1.413 6.004 113.447 1.00 96.39 C
ANISOU 1973 CB ASN A 321 15706 12686 8231 -1200 -400 -2185 C
ATOM 1974 CG ASN A 321 -2.116 5.280 112.313 1.00 90.76 C
ANISOU 1974 CG ASN A 321 14814 12007 7662 -1032 -339 -2020 C
ATOM 1975 OD1 ASN A 321 -1.479 4.832 111.359 1.00 84.18 O
ANISOU 1975 OD1 ASN A 321 13832 11137 7016 -1033 -428 -1925 O
ATOM 1976 ND2 ASN A 321 -3.435 5.141 112.423 1.00 90.36 N
ANISOU 1976 ND2 ASN A 321 14766 12050 7515 -896 -185 -2000 N
ATOM 1977 N CYS A 322 -3.580 8.200 112.994 1.00109.16 N
ANISOU 1977 N CYS A 322 17606 14080 9789 -831 136 -2357 N
ATOM 1978 CA CYS A 322 -4.800 8.525 112.264 1.00112.98 C
ANISOU 1978 CA CYS A 322 18066 14569 10294 -555 344 -2319 C
ATOM 1979 C CYS A 322 -4.720 9.893 111.606 1.00120.37 C
ANISOU 1979 C CYS A 322 19182 15246 11308 -422 530 -2403 C
ATOM 1980 O CYS A 322 -5.275 10.094 110.521 1.00122.39 O
ANISOU 1980 O CYS A 322 19374 15471 11658 -180 650 -2329 O
ATOM 1981 CB CYS A 322 -6.006 8.461 113.205 1.00114.88 C
ANISOU 1981 CB CYS A 322 18362 14976 10313 -476 455 -2366 C
ATOM 1982 SG CYS A 322 -6.085 9.824 114.397 1.00115.64 S
ANISOU 1982 SG CYS A 322 18795 14928 10214 -516 601 -2582 S
ATOM 1983 N CYS A 323 -4.050 10.847 112.251 1.00124.53 N
ANISOU 1983 N CYS A 323 19949 15587 11781 -573 572 -2562 N
ATOM 1984 CA CYS A 323 -3.806 12.138 111.626 1.00121.60 C
ANISOU 1984 CA CYS A 323 19795 14917 11490 -490 771 -2647 C
ATOM 1985 C CYS A 323 -2.598 12.116 110.704 1.00123.33 C
ANISOU 1985 C CYS A 323 19946 14988 11927 -624 682 -2614 C
ATOM 1986 O CYS A 323 -2.470 12.997 109.847 1.00115.17 O
ANISOU 1986 O CYS A 323 19058 13707 10995 -514 860 -2630 O
ATOM 1987 CB CYS A 323 -3.614 13.213 112.698 1.00111.93 C
ANISOU 1987 CB CYS A 323 18881 13535 10112 -626 892 -2860 C
ATOM 1988 SG CYS A 323 -2.114 13.045 113.696 1.00103.91 S
ANISOU 1988 SG CYS A 323 17874 12546 9062 -1072 662 -3012 S
ATOM 1989 N CYS A 324 -1.703 11.143 110.874 1.00126.08 N
ANISOU 1989 N CYS A 324 20089 15479 12335 -849 424 -2568 N
ATOM 1990 CA CYS A 324 -0.551 11.041 109.991 1.00131.65 C
ANISOU 1990 CA CYS A 324 20694 16080 13249 -974 332 -2537 C
ATOM 1991 C CYS A 324 -0.957 10.674 108.570 1.00128.26 C
ANISOU 1991 C CYS A 324 20113 15634 12986 -737 380 -2358 C
ATOM 1992 O CYS A 324 -0.282 11.072 107.615 1.00127.70 O
ANISOU 1992 O CYS A 324 20059 15379 13083 -752 430 -2349 O
ATOM 1993 CB CYS A 324 0.438 10.018 110.550 1.00141.17 C
ANISOU 1993 CB CYS A 324 21702 17483 14455 -1222 38 -2521 C
ATOM 1994 SG CYS A 324 1.899 9.755 109.523 1.00150.92 S
ANISOU 1994 SG CYS A 324 22760 18646 15936 -1379 -99 -2489 S
ATOM 1995 N LYS A 325 -2.039 9.912 108.408 1.00118.15 N
ANISOU 1995 N LYS A 325 18681 14556 11657 -533 372 -2228 N
ATOM 1996 CA LYS A 325 -2.416 9.483 107.053 1.00102.04 C
ANISOU 1996 CA LYS A 325 16465 12546 9761 -321 399 -2073 C
ATOM 1997 C LYS A 325 -2.641 10.627 106.051 1.00 97.28 C
ANISOU 1997 C LYS A 325 16034 11705 9225 -93 633 -2081 C
ATOM 1998 O LYS A 325 -2.048 10.586 104.952 1.00 94.80 O
ANISOU 1998 O LYS A 325 15653 11283 9085 -75 623 -2007 O
ATOM 1999 CB LYS A 325 -3.660 8.589 107.125 1.00 96.92 C
ANISOU 1999 CB LYS A 325 15634 12175 9015 -157 389 -1979 C
ATOM 2000 CG LYS A 325 -3.402 7.107 106.935 1.00 95.40 C
ANISOU 2000 CG LYS A 325 15174 12178 8896 -271 185 -1850 C
ATOM 2001 CD LYS A 325 -2.929 6.454 108.220 1.00 96.24 C
ANISOU 2001 CD LYS A 325 15291 12386 8889 -514 19 -1881 C
ATOM 2002 CE LYS A 325 -3.374 5.001 108.286 1.00 90.27 C
ANISOU 2002 CE LYS A 325 14334 11859 8105 -536 -83 -1757 C
ATOM 2003 NZ LYS A 325 -2.847 4.294 109.485 1.00 94.97 N
ANISOU 2003 NZ LYS A 325 14964 12541 8577 -740 -244 -1757 N
ATOM 2004 N PRO A 326 -3.478 11.641 106.332 1.00101.96 N
ANISOU 2004 N PRO A 326 16857 12202 9679 108 857 -2159 N
ATOM 2005 CA PRO A 326 -3.767 12.655 105.298 1.00 99.75 C
ANISOU 2005 CA PRO A 326 16758 11699 9443 390 1094 -2134 C
ATOM 2006 C PRO A 326 -2.552 13.409 104.783 1.00 97.33 C
ANISOU 2006 C PRO A 326 16643 11057 9281 228 1166 -2188 C
ATOM 2007 O PRO A 326 -2.540 13.820 103.613 1.00 88.71 O
ANISOU 2007 O PRO A 326 15613 9809 8283 426 1296 -2107 O
ATOM 2008 CB PRO A 326 -4.754 13.597 106.000 1.00106.38 C
ANISOU 2008 CB PRO A 326 17848 12492 10079 596 1312 -2231 C
ATOM 2009 CG PRO A 326 -5.369 12.771 107.075 1.00107.94 C
ANISOU 2009 CG PRO A 326 17878 12996 10139 510 1178 -2254 C
ATOM 2010 CD PRO A 326 -4.270 11.876 107.551 1.00107.77 C
ANISOU 2010 CD PRO A 326 17706 13039 10203 129 919 -2258 C
ATOM 2011 N TRP A 327 -1.550 13.654 105.628 1.00106.90 N
ANISOU 2011 N TRP A 327 17960 12159 10497 -126 1102 -2337 N
ATOM 2012 CA TRP A 327 -0.365 14.355 105.146 1.00115.61 C
ANISOU 2012 CA TRP A 327 19223 12966 11738 -326 1184 -2420 C
ATOM 2013 C TRP A 327 0.369 13.520 104.108 1.00121.06 C
ANISOU 2013 C TRP A 327 19644 13721 12633 -390 1020 -2290 C
ATOM 2014 O TRP A 327 0.899 14.061 103.132 1.00124.48 O
ANISOU 2014 O TRP A 327 20185 13916 13196 -372 1154 -2274 O
ATOM 2015 CB TRP A 327 0.586 14.683 106.295 1.00118.47 C
ANISOU 2015 CB TRP A 327 19690 13273 12049 -724 1122 -2634 C
ATOM 2016 CG TRP A 327 -0.055 15.151 107.556 1.00122.99 C
ANISOU 2016 CG TRP A 327 20449 13875 12407 -728 1197 -2766 C
ATOM 2017 CD1 TRP A 327 -1.298 15.698 107.711 1.00123.93 C
ANISOU 2017 CD1 TRP A 327 20750 13955 12381 -414 1399 -2746 C
ATOM 2018 CD2 TRP A 327 0.531 15.108 108.857 1.00126.35 C
ANISOU 2018 CD2 TRP A 327 20889 14397 12723 -1057 1067 -2944 C
ATOM 2019 NE1 TRP A 327 -1.518 15.995 109.033 1.00127.84 N
ANISOU 2019 NE1 TRP A 327 21382 14497 12694 -541 1412 -2901 N
ATOM 2020 CE2 TRP A 327 -0.408 15.643 109.757 1.00129.73 C
ANISOU 2020 CE2 TRP A 327 21526 14819 12947 -938 1208 -3024 C
ATOM 2021 CE3 TRP A 327 1.764 14.669 109.349 1.00127.15 C
ANISOU 2021 CE3 TRP A 327 20834 14613 12863 -1424 841 -3047 C
ATOM 2022 CZ2 TRP A 327 -0.153 15.749 111.118 1.00130.68 C
ANISOU 2022 CZ2 TRP A 327 21718 15029 12904 -1188 1132 -3203 C
ATOM 2023 CZ3 TRP A 327 2.015 14.776 110.702 1.00127.07 C
ANISOU 2023 CZ3 TRP A 327 20885 14717 12680 -1656 756 -3226 C
ATOM 2024 CH2 TRP A 327 1.061 15.313 111.572 1.00128.46 C
ANISOU 2024 CH2 TRP A 327 21284 14868 12655 -1546 903 -3302 C
ATOM 2025 N ILE A 328 0.393 12.198 104.295 1.00106.28 N
ANISOU 2025 N ILE A 328 17440 12155 10786 -458 750 -2193 N
ATOM 2026 CA ILE A 328 0.986 11.317 103.295 1.00 91.67 C
ANISOU 2026 CA ILE A 328 15329 10380 9121 -485 599 -2058 C
ATOM 2027 C ILE A 328 0.179 11.376 102.009 1.00 89.27 C
ANISOU 2027 C ILE A 328 15003 10048 8869 -134 734 -1907 C
ATOM 2028 O ILE A 328 0.739 11.397 100.900 1.00 87.28 O
ANISOU 2028 O ILE A 328 14713 9675 8774 -113 762 -1837 O
ATOM 2029 CB ILE A 328 1.072 9.882 103.844 1.00 87.16 C
ANISOU 2029 CB ILE A 328 14455 10126 8535 -603 312 -1983 C
ATOM 2030 CG1 ILE A 328 1.950 9.840 105.096 1.00 83.83 C
ANISOU 2030 CG1 ILE A 328 14054 9756 8039 -922 164 -2130 C
ATOM 2031 CG2 ILE A 328 1.599 8.934 102.784 1.00 76.34 C
ANISOU 2031 CG2 ILE A 328 12827 8828 7350 -604 175 -1838 C
ATOM 2032 CD1 ILE A 328 1.860 8.534 105.855 1.00 79.57 C
ANISOU 2032 CD1 ILE A 328 13300 9513 7420 -988 -79 -2054 C
ATOM 2033 N TYR A 329 -1.149 11.464 102.140 1.00 89.22 N
ANISOU 2033 N TYR A 329 15023 10163 8714 154 831 -1866 N
ATOM 2034 CA TYR A 329 -1.989 11.601 100.953 1.00 89.71 C
ANISOU 2034 CA TYR A 329 15058 10243 8784 526 963 -1741 C
ATOM 2035 C TYR A 329 -1.618 12.847 100.160 1.00 94.23 C
ANISOU 2035 C TYR A 329 15938 10458 9407 647 1210 -1758 C
ATOM 2036 O TYR A 329 -1.328 12.774 98.960 1.00 89.80 O
ANISOU 2036 O TYR A 329 15326 9825 8970 752 1238 -1654 O
ATOM 2037 CB TYR A 329 -3.464 11.662 101.349 1.00 89.28 C
ANISOU 2037 CB TYR A 329 14994 10396 8533 817 1049 -1736 C
ATOM 2038 CG TYR A 329 -4.067 10.333 101.718 1.00 86.15 C
ANISOU 2038 CG TYR A 329 14268 10372 8094 771 856 -1683 C
ATOM 2039 CD1 TYR A 329 -3.372 9.154 101.512 1.00 78.71 C
ANISOU 2039 CD1 TYR A 329 13075 9544 7287 544 635 -1613 C
ATOM 2040 CD2 TYR A 329 -5.340 10.258 102.264 1.00 90.72 C
ANISOU 2040 CD2 TYR A 329 14799 11182 8489 956 916 -1710 C
ATOM 2041 CE1 TYR A 329 -3.927 7.940 101.841 1.00 81.53 C
ANISOU 2041 CE1 TYR A 329 13178 10203 7597 494 497 -1566 C
ATOM 2042 CE2 TYR A 329 -5.901 9.045 102.600 1.00 92.24 C
ANISOU 2042 CE2 TYR A 329 14710 11699 8637 883 774 -1677 C
ATOM 2043 CZ TYR A 329 -5.189 7.888 102.387 1.00 91.27 C
ANISOU 2043 CZ TYR A 329 14377 11652 8650 647 573 -1602 C
ATOM 2044 OH TYR A 329 -5.741 6.671 102.719 1.00 98.03 O
ANISOU 2044 OH TYR A 329 14997 12794 9456 563 467 -1570 O
ATOM 2045 N MET A 330 -1.605 14.000 100.826 1.00103.74 N
ANISOU 2045 N MET A 330 17487 11418 10511 626 1408 -1891 N
ATOM 2046 CA MET A 330 -1.342 15.249 100.120 1.00106.60 C
ANISOU 2046 CA MET A 330 18209 11399 10895 756 1696 -1910 C
ATOM 2047 C MET A 330 0.118 15.398 99.713 1.00102.82 C
ANISOU 2047 C MET A 330 17779 10683 10605 415 1687 -1966 C
ATOM 2048 O MET A 330 0.417 16.191 98.813 1.00111.50 O
ANISOU 2048 O MET A 330 19122 11482 11762 519 1912 -1940 O
ATOM 2049 CB MET A 330 -1.786 16.445 100.965 1.00120.15 C
ANISOU 2049 CB MET A 330 20313 12901 12439 830 1943 -2047 C
ATOM 2050 CG MET A 330 -3.269 16.423 101.322 1.00130.71 C
ANISOU 2050 CG MET A 330 21617 14469 13576 1205 1988 -2001 C
ATOM 2051 SD MET A 330 -4.314 15.716 100.025 1.00135.94 S
ANISOU 2051 SD MET A 330 21978 15442 14231 1668 1934 -1783 S
ATOM 2052 CE MET A 330 -4.176 16.952 98.734 1.00137.96 C
ANISOU 2052 CE MET A 330 22617 15301 14499 2001 2257 -1704 C
ATOM 2053 N LEU A 331 1.034 14.665 100.349 1.00101.81 N
ANISOU 2053 N LEU A 331 17429 10690 10563 23 1443 -2044 N
ATOM 2054 CA LEU A 331 2.426 14.692 99.919 1.00102.06 C
ANISOU 2054 CA LEU A 331 17436 10568 10776 -296 1410 -2104 C
ATOM 2055 C LEU A 331 2.604 13.923 98.619 1.00102.47 C
ANISOU 2055 C LEU A 331 17243 10705 10984 -172 1315 -1922 C
ATOM 2056 O LEU A 331 3.227 14.420 97.672 1.00100.16 O
ANISOU 2056 O LEU A 331 17078 10169 10810 -190 1465 -1907 O
ATOM 2057 CB LEU A 331 3.322 14.112 101.019 1.00 95.94 C
ANISOU 2057 CB LEU A 331 16472 9967 10016 -708 1162 -2243 C
ATOM 2058 CG LEU A 331 4.839 14.008 100.816 1.00 95.34 C
ANISOU 2058 CG LEU A 331 16289 9831 10105 -1083 1073 -2345 C
ATOM 2059 CD1 LEU A 331 5.537 14.110 102.161 1.00100.41 C
ANISOU 2059 CD1 LEU A 331 16923 10564 10666 -1447 956 -2567 C
ATOM 2060 CD2 LEU A 331 5.247 12.711 100.120 1.00 92.80 C
ANISOU 2060 CD2 LEU A 331 15582 9744 9933 -1080 816 -2185 C
ATOM 2061 N PHE A 332 2.062 12.704 98.553 1.00 98.64 N
ANISOU 2061 N PHE A 332 16422 10559 10499 -60 1083 -1789 N
ATOM 2062 CA PHE A 332 2.224 11.914 97.339 1.00 99.20 C
ANISOU 2062 CA PHE A 332 16254 10723 10713 42 989 -1629 C
ATOM 2063 C PHE A 332 1.411 12.456 96.173 1.00102.62 C
ANISOU 2063 C PHE A 332 16827 11053 11112 446 1203 -1506 C
ATOM 2064 O PHE A 332 1.752 12.182 95.017 1.00100.45 O
ANISOU 2064 O PHE A 332 16459 10746 10960 515 1203 -1400 O
ATOM 2065 CB PHE A 332 1.849 10.458 97.602 1.00 94.41 C
ANISOU 2065 CB PHE A 332 15279 10489 10104 34 712 -1536 C
ATOM 2066 CG PHE A 332 3.004 9.614 98.046 1.00 90.29 C
ANISOU 2066 CG PHE A 332 14544 10066 9694 -312 472 -1574 C
ATOM 2067 CD1 PHE A 332 3.338 9.524 99.384 1.00 88.90 C
ANISOU 2067 CD1 PHE A 332 14375 9972 9433 -550 353 -1698 C
ATOM 2068 CD2 PHE A 332 3.766 8.922 97.120 1.00 91.52 C
ANISOU 2068 CD2 PHE A 332 14499 10246 10029 -379 366 -1486 C
ATOM 2069 CE1 PHE A 332 4.409 8.749 99.794 1.00 93.94 C
ANISOU 2069 CE1 PHE A 332 14813 10732 10147 -823 124 -1728 C
ATOM 2070 CE2 PHE A 332 4.837 8.146 97.523 1.00 90.50 C
ANISOU 2070 CE2 PHE A 332 14171 10226 9989 -658 146 -1517 C
ATOM 2071 CZ PHE A 332 5.159 8.060 98.863 1.00 93.28 C
ANISOU 2071 CZ PHE A 332 14524 10677 10242 -868 21 -1636 C
ATOM 2072 N MET A 333 0.362 13.230 96.439 1.00106.95 N
ANISOU 2072 N MET A 333 17599 11555 11481 733 1388 -1518 N
ATOM 2073 CA MET A 333 -0.596 13.608 95.404 1.00104.72 C
ANISOU 2073 CA MET A 333 17400 11272 11117 1192 1556 -1387 C
ATOM 2074 C MET A 333 -0.755 15.124 95.354 1.00122.20 C
ANISOU 2074 C MET A 333 20090 13114 13225 1381 1896 -1438 C
ATOM 2075 O MET A 333 -1.544 15.710 96.100 1.00118.74 O
ANISOU 2075 O MET A 333 19831 12671 12614 1541 2013 -1499 O
ATOM 2076 CB MET A 333 -1.934 12.904 95.633 1.00 95.28 C
ANISOU 2076 CB MET A 333 15955 10471 9777 1453 1445 -1328 C
ATOM 2077 CG MET A 333 -1.893 11.420 95.300 1.00 95.37 C
ANISOU 2077 CG MET A 333 15534 10813 9889 1342 1174 -1246 C
ATOM 2078 SD MET A 333 -3.443 10.568 95.639 1.00106.76 S
ANISOU 2078 SD MET A 333 16682 12724 11159 1570 1074 -1218 S
ATOM 2079 CE MET A 333 -3.135 8.985 94.856 1.00 98.74 C
ANISOU 2079 CE MET A 333 15250 11968 10300 1426 833 -1116 C
ATOM 2080 N GLY A 334 -0.002 15.748 94.452 1.00139.70 N
ANISOU 2080 N GLY A 334 22527 15009 15542 1365 2074 -1411 N
ATOM 2081 CA GLY A 334 -0.355 17.043 93.918 1.00148.33 C
ANISOU 2081 CA GLY A 334 24069 15764 16524 1689 2427 -1381 C
ATOM 2082 C GLY A 334 -1.379 16.925 92.822 1.00154.02 C
ANISOU 2082 C GLY A 334 24721 16658 17140 2222 2471 -1192 C
ATOM 2083 O GLY A 334 -1.785 17.917 92.210 1.00159.50 O
ANISOU 2083 O GLY A 334 25773 17114 17714 2593 2757 -1124 O
ATOM 2084 N HIS A 335 -1.790 15.683 92.565 1.00153.88 N
ANISOU 2084 N HIS A 335 24244 17069 17157 2261 2190 -1112 N
ATOM 2085 CA HIS A 335 -2.877 15.368 91.652 1.00151.39 C
ANISOU 2085 CA HIS A 335 23756 17045 16720 2735 2174 -967 C
ATOM 2086 C HIS A 335 -4.202 15.947 92.127 1.00147.12 C
ANISOU 2086 C HIS A 335 23334 16638 15927 3146 2299 -979 C
ATOM 2087 O HIS A 335 -5.136 16.073 91.327 1.00146.77 O
ANISOU 2087 O HIS A 335 23252 16781 15732 3628 2367 -872 O
ATOM 2088 CB HIS A 335 -2.963 13.845 91.527 1.00153.00 C
ANISOU 2088 CB HIS A 335 23436 17675 17020 2575 1846 -932 C
ATOM 2089 CG HIS A 335 -3.800 13.361 90.388 1.00159.20 C
ANISOU 2089 CG HIS A 335 23988 18771 17728 2961 1804 -803 C
ATOM 2090 ND1 HIS A 335 -5.151 13.119 90.508 1.00160.56 N
ANISOU 2090 ND1 HIS A 335 23968 19332 17705 3291 1768 -798 N
ATOM 2091 CD2 HIS A 335 -3.470 13.036 89.116 1.00160.71 C
ANISOU 2091 CD2 HIS A 335 24082 18975 18004 3053 1784 -691 C
ATOM 2092 CE1 HIS A 335 -5.621 12.683 89.353 1.00161.87 C
ANISOU 2092 CE1 HIS A 335 23923 19751 17831 3570 1725 -698 C
ATOM 2093 NE2 HIS A 335 -4.621 12.623 88.491 1.00160.95 N
ANISOU 2093 NE2 HIS A 335 23869 19404 17881 3437 1733 -625 N
ATOM 2094 N LEU A 336 -4.309 16.287 93.408 1.00141.51 N
ANISOU 2094 N LEU A 336 22748 15864 15154 2978 2327 -1113 N
ATOM 2095 CA LEU A 336 -5.548 16.766 94.004 1.00135.05 C
ANISOU 2095 CA LEU A 336 22015 15196 14101 3331 2433 -1144 C
ATOM 2096 C LEU A 336 -5.299 18.023 94.832 1.00136.85 C
ANISOU 2096 C LEU A 336 22736 15004 14257 3274 2696 -1258 C
ATOM 2097 O LEU A 336 -5.919 18.239 95.877 1.00135.80 O
ANISOU 2097 O LEU A 336 22648 14959 13991 3300 2719 -1355 O
ATOM 2098 CB LEU A 336 -6.196 15.664 94.841 1.00122.13 C
ANISOU 2098 CB LEU A 336 19951 14022 12430 3191 2171 -1203 C
ATOM 2099 CG LEU A 336 -7.647 15.801 95.309 1.00116.59 C
ANISOU 2099 CG LEU A 336 19173 13640 11488 3567 2220 -1230 C
ATOM 2100 CD1 LEU A 336 -8.510 16.439 94.232 1.00116.11 C
ANISOU 2100 CD1 LEU A 336 19212 13649 11255 4178 2401 -1115 C
ATOM 2101 CD2 LEU A 336 -8.199 14.440 95.709 1.00113.84 C
ANISOU 2101 CD2 LEU A 336 18326 13786 11144 3405 1949 -1259 C
ATOM 2102 N PHE A 337 -4.373 18.871 94.390 1.00137.15 N
ANISOU 2102 N PHE A 337 23160 14571 14379 3171 2915 -1261 N
ATOM 2103 CA PHE A 337 -4.219 20.171 95.026 1.00139.84 C
ANISOU 2103 CA PHE A 337 24025 14478 14629 3163 3227 -1371 C
ATOM 2104 C PHE A 337 -5.461 21.019 94.769 1.00136.84 C
ANISOU 2104 C PHE A 337 23911 14090 13991 3802 3477 -1286 C
ATOM 2105 O PHE A 337 -5.977 21.067 93.648 1.00138.90 O
ANISOU 2105 O PHE A 337 24157 14446 14173 4257 3537 -1121 O
ATOM 2106 CB PHE A 337 -2.969 20.879 94.503 1.00143.25 C
ANISOU 2106 CB PHE A 337 24820 14405 15205 2904 3441 -1400 C
ATOM 2107 N HIS A 338 -5.935 21.697 95.810 1.00134.43 N
ANISOU 2107 N HIS A 338 23853 13684 13540 3853 3624 -1402 N
ATOM 2108 CA HIS A 338 -7.177 22.465 95.716 1.00122.61 C
ANISOU 2108 CA HIS A 338 22585 12224 11778 4479 3850 -1335 C
ATOM 2109 C HIS A 338 -7.280 23.535 96.801 1.00117.96 C
ANISOU 2109 C HIS A 338 22453 11299 11069 4442 4116 -1483 C
ATOM 2110 O HIS A 338 -8.158 24.399 96.752 1.00109.81 O
ANISOU 2110 O HIS A 338 21562 10258 9903 4834 4260 -1351 O
ATOM 2111 CB HIS A 338 -8.387 21.530 95.797 1.00113.71 C
ANISOU 2111 CB HIS A 338 20940 11732 10535 4761 3594 -1288 C
ATOM 2112 N GLY A 339 9.810 -5.916 86.486 1.00144.87 N
ANISOU 2112 N GLY A 339 18545 17970 18530 -454 -936 -109 N
ATOM 2113 CA GLY A 339 10.921 -5.060 86.866 1.00140.19 C
ANISOU 2113 CA GLY A 339 17963 17301 18001 -547 -983 -180 C
ATOM 2114 C GLY A 339 11.924 -4.929 85.745 1.00132.39 C
ANISOU 2114 C GLY A 339 16884 16224 17194 -564 -947 -172 C
ATOM 2115 O GLY A 339 13.126 -5.109 85.933 1.00135.25 O
ANISOU 2115 O GLY A 339 17148 16593 17647 -651 -1042 -193 O
ATOM 2116 N ILE A 340 11.400 -4.624 84.558 1.00121.24 N
ANISOU 2116 N ILE A 340 15496 14750 15821 -468 -806 -146 N
ATOM 2117 CA ILE A 340 12.235 -4.498 83.371 1.00107.29 C
ANISOU 2117 CA ILE A 340 13660 12888 14216 -472 -742 -130 C
ATOM 2118 C ILE A 340 13.241 -3.364 83.516 1.00101.93 C
ANISOU 2118 C ILE A 340 13029 12093 13608 -596 -700 -232 C
ATOM 2119 O ILE A 340 14.331 -3.413 82.932 1.00106.55 O
ANISOU 2119 O ILE A 340 13516 12631 14338 -671 -696 -247 O
ATOM 2120 CB ILE A 340 11.332 -4.318 82.136 1.00100.30 C
ANISOU 2120 CB ILE A 340 12818 11979 13313 -319 -593 -84 C
ATOM 2121 CG1 ILE A 340 12.151 -4.298 80.845 1.00 81.77 C
ANISOU 2121 CG1 ILE A 340 10409 9537 11123 -314 -519 -56 C
ATOM 2122 CG2 ILE A 340 10.494 -3.057 82.281 1.00107.20 C
ANISOU 2122 CG2 ILE A 340 13870 12798 14063 -234 -470 -133 C
ATOM 2123 CD1 ILE A 340 11.300 -4.177 79.611 1.00 64.68 C
ANISOU 2123 CD1 ILE A 340 8280 7376 8919 -145 -386 -7 C
ATOM 2124 N ASP A 341 12.911 -2.318 84.291 1.00 88.55 N
ANISOU 2124 N ASP A 341 11483 10354 11809 -637 -658 -317 N
ATOM 2125 CA ASP A 341 13.750 -1.092 84.470 1.00 84.12 C
ANISOU 2125 CA ASP A 341 11010 9657 11294 -781 -570 -440 C
ATOM 2126 C ASP A 341 13.982 -0.492 83.095 1.00 81.76 C
ANISOU 2126 C ASP A 341 10774 9189 11101 -743 -380 -424 C
ATOM 2127 O ASP A 341 15.108 -0.462 82.643 1.00 81.81 O
ANISOU 2127 O ASP A 341 10675 9157 11253 -857 -370 -456 O
ATOM 2128 CB ASP A 341 15.059 -1.322 85.224 1.00 84.99 C
ANISOU 2128 CB ASP A 341 10960 9858 11474 -973 -723 -527 C
ATOM 2129 CG ASP A 341 15.815 -0.046 85.494 1.00 84.75 C
ANISOU 2129 CG ASP A 341 11013 9719 11470 -1174 -626 -699 C
ATOM 2130 OD1 ASP A 341 15.174 0.993 85.538 1.00 86.14 O
ANISOU 2130 OD1 ASP A 341 11417 9721 11589 -1158 -439 -742 O
ATOM 2131 OD2 ASP A 341 17.029 -0.115 85.654 1.00 85.35 O
ANISOU 2131 OD2 ASP A 341 10927 9890 11614 -1345 -726 -800 O
HETATM 2132 N YCM A 342 12.924 0.058 82.528 1.00 79.58 N
ANISOU 2132 N YCM A 342 10672 8826 10737 -567 -225 -377 N
HETATM 2133 CA YCM A 342 12.947 0.528 81.119 1.00 83.26 C
ANISOU 2133 CA YCM A 342 11223 9147 11266 -462 -38 -326 C
HETATM 2134 CB YCM A 342 11.529 0.623 80.598 1.00 88.96 C
ANISOU 2134 CB YCM A 342 12049 9910 11843 -189 45 -238 C
HETATM 2135 SG YCM A 342 11.354 0.709 78.802 1.00 92.73 S
ANISOU 2135 SG YCM A 342 12564 10316 12353 13 209 -136 S
HETATM 2136 CD YCM A 342 9.702 -0.012 78.563 1.00 89.82 C
ANISOU 2136 CD YCM A 342 12117 10204 11805 283 150 -56 C
HETATM 2137 CE YCM A 342 8.620 0.771 79.280 1.00 94.24 C
ANISOU 2137 CE YCM A 342 12838 10793 12176 424 204 -87 C
HETATM 2138 OZ1 YCM A 342 8.548 0.760 80.504 1.00 92.40 O
ANISOU 2138 OZ1 YCM A 342 12606 10595 11906 306 115 -148 O
HETATM 2139 NZ2 YCM A 342 7.789 1.436 78.510 1.00 97.93 N
ANISOU 2139 NZ2 YCM A 342 13441 11256 12511 694 351 -42 N
HETATM 2140 C YCM A 342 13.696 1.864 81.033 1.00 80.96 C
ANISOU 2140 C YCM A 342 11122 8619 11021 -600 152 -432 C
HETATM 2141 O YCM A 342 13.848 2.436 79.954 1.00 79.20 O
ANISOU 2141 O YCM A 342 11023 8228 10840 -537 343 -402 O
ATOM 2142 N SER A 343 14.166 2.344 82.181 1.00 79.00 N
ANISOU 2142 N SER A 343 10905 8357 10754 -799 109 -565 N
ATOM 2143 CA SER A 343 15.030 3.517 82.232 1.00 80.19 C
ANISOU 2143 CA SER A 343 11210 8300 10958 -1009 286 -709 C
ATOM 2144 C SER A 343 16.421 3.148 81.732 1.00 79.35 C
ANISOU 2144 C SER A 343 10897 8214 11036 -1210 257 -764 C
ATOM 2145 O SER A 343 17.216 4.018 81.375 1.00 79.92 O
ANISOU 2145 O SER A 343 11074 8107 11185 -1390 446 -875 O
ATOM 2146 CB SER A 343 15.110 4.079 83.655 1.00 80.45 C
ANISOU 2146 CB SER A 343 11313 8351 10902 -1183 237 -860 C
ATOM 2147 OG SER A 343 15.753 3.171 84.536 1.00 81.14 O
ANISOU 2147 OG SER A 343 11126 8683 11021 -1326 -25 -910 O
ATOM 2148 N PHE A 344 16.706 1.846 81.718 1.00 78.20 N
ANISOU 2148 N PHE A 344 10467 8289 10958 -1181 36 -693 N
ATOM 2149 CA PHE A 344 17.994 1.321 81.286 1.00 75.12 C
ANISOU 2149 CA PHE A 344 9839 7969 10733 -1330 -23 -734 C
ATOM 2150 C PHE A 344 17.933 0.658 79.918 1.00 83.49 C
ANISOU 2150 C PHE A 344 10832 9006 11885 -1171 25 -590 C
ATOM 2151 O PHE A 344 18.733 0.984 79.036 1.00 85.95 O
ANISOU 2151 O PHE A 344 11134 9206 12318 -1263 167 -625 O
ATOM 2152 CB PHE A 344 18.527 0.321 82.326 1.00 61.11 C
ANISOU 2152 CB PHE A 344 7797 6464 8958 -1402 -306 -766 C
ATOM 2153 CG PHE A 344 19.853 -0.293 81.959 1.00 70.11 C
ANISOU 2153 CG PHE A 344 8663 7722 10251 -1516 -388 -808 C
ATOM 2154 CD1 PHE A 344 21.041 0.295 82.362 1.00 82.79 C
ANISOU 2154 CD1 PHE A 344 10163 9376 11917 -1781 -374 -1007 C
ATOM 2155 CD2 PHE A 344 19.913 -1.463 81.218 1.00 69.75 C
ANISOU 2155 CD2 PHE A 344 8460 7757 10283 -1363 -471 -665 C
ATOM 2156 CE1 PHE A 344 22.262 -0.271 82.027 1.00 85.78 C
ANISOU 2156 CE1 PHE A 344 10260 9905 12428 -1870 -451 -1058 C
ATOM 2157 CE2 PHE A 344 21.129 -2.029 80.878 1.00 60.80 C
ANISOU 2157 CE2 PHE A 344 7076 6739 9286 -1441 -540 -702 C
ATOM 2158 CZ PHE A 344 22.304 -1.432 81.283 1.00 63.18 C
ANISOU 2158 CZ PHE A 344 7250 7111 9642 -1685 -535 -897 C
ATOM 2159 N TRP A 345 17.000 -0.272 79.718 1.00 76.42 N
ANISOU 2159 N TRP A 345 9890 8218 10928 -951 -79 -443 N
ATOM 2160 CA TRP A 345 16.932 -1.057 78.485 1.00 65.04 C
ANISOU 2160 CA TRP A 345 8358 6792 9562 -812 -59 -320 C
ATOM 2161 C TRP A 345 16.111 -0.298 77.454 1.00 68.03 C
ANISOU 2161 C TRP A 345 8967 7007 9874 -639 161 -253 C
ATOM 2162 O TRP A 345 14.883 -0.392 77.414 1.00 65.16 O
ANISOU 2162 O TRP A 345 8690 6696 9373 -438 159 -176 O
ATOM 2163 CB TRP A 345 16.336 -2.434 78.749 1.00 70.42 C
ANISOU 2163 CB TRP A 345 8889 7668 10200 -685 -251 -217 C
ATOM 2164 CG TRP A 345 17.053 -3.235 79.791 1.00 77.16 C
ANISOU 2164 CG TRP A 345 9553 8681 11083 -795 -464 -253 C
ATOM 2165 CD1 TRP A 345 16.731 -3.330 81.111 1.00 78.76 C
ANISOU 2165 CD1 TRP A 345 9768 8985 11171 -826 -599 -287 C
ATOM 2166 CD2 TRP A 345 18.205 -4.067 79.599 1.00 78.55 C
ANISOU 2166 CD2 TRP A 345 9506 8945 11393 -856 -565 -253 C
ATOM 2167 NE1 TRP A 345 17.611 -4.164 81.756 1.00 71.41 N
ANISOU 2167 NE1 TRP A 345 8646 8205 10283 -890 -781 -301 N
ATOM 2168 CE2 TRP A 345 18.526 -4.629 80.850 1.00 70.63 C
ANISOU 2168 CE2 TRP A 345 8395 8105 10335 -900 -765 -281 C
ATOM 2169 CE3 TRP A 345 18.996 -4.388 78.493 1.00 79.40 C
ANISOU 2169 CE3 TRP A 345 9499 9019 11651 -862 -502 -231 C
ATOM 2170 CZ2 TRP A 345 19.606 -5.492 81.026 1.00 56.40 C
ANISOU 2170 CZ2 TRP A 345 6374 6442 8615 -922 -907 -282 C
ATOM 2171 CZ3 TRP A 345 20.066 -5.246 78.669 1.00 74.46 C
ANISOU 2171 CZ3 TRP A 345 8645 8527 11120 -902 -638 -240 C
ATOM 2172 CH2 TRP A 345 20.361 -5.787 79.926 1.00 71.31 C
ANISOU 2172 CH2 TRP A 345 8142 8298 10655 -919 -841 -263 C
ATOM 2173 N ASN A 348 16.800 0.475 76.617 1.00 77.42 N
ANISOU 2173 N ASN A 348 10258 8010 11148 -711 360 -288 N
ATOM 2174 CA ASN A 348 16.209 1.037 75.411 1.00 83.34 C
ANISOU 2174 CA ASN A 348 11214 8610 11841 -515 573 -200 C
ATOM 2175 C ASN A 348 17.336 1.452 74.478 1.00 75.85 C
ANISOU 2175 C ASN A 348 10290 7494 11037 -651 751 -238 C
ATOM 2176 O ASN A 348 18.468 1.689 74.907 1.00 59.82 O
ANISOU 2176 O ASN A 348 8174 5432 9124 -919 756 -369 O
ATOM 2177 CB ASN A 348 15.276 2.219 75.716 1.00 77.50 C
ANISOU 2177 CB ASN A 348 10787 7729 10930 -388 728 -205 C
ATOM 2178 CG ASN A 348 15.965 3.333 76.476 1.00 80.80 C
ANISOU 2178 CG ASN A 348 11368 7962 11371 -627 851 -355 C
ATOM 2179 OD1 ASN A 348 16.934 3.101 77.197 1.00 84.03 O
ANISOU 2179 OD1 ASN A 348 11601 8440 11886 -892 739 -475 O
ATOM 2180 ND2 ASN A 348 15.459 4.553 76.324 1.00 86.37 N
ANISOU 2180 ND2 ASN A 348 12416 8439 11960 -527 1090 -357 N
ATOM 2181 N GLU A 349 17.003 1.548 73.189 1.00 73.15 N
ANISOU 2181 N GLU A 349 10058 7066 10671 -465 902 -132 N
ATOM 2182 CA GLU A 349 17.987 1.898 72.172 1.00 79.88 C
ANISOU 2182 CA GLU A 349 10952 7752 11646 -571 1094 -150 C
ATOM 2183 C GLU A 349 18.463 3.338 72.284 1.00 76.39 C
ANISOU 2183 C GLU A 349 10800 7026 11199 -731 1364 -255 C
ATOM 2184 O GLU A 349 19.456 3.691 71.640 1.00 65.03 O
ANISOU 2184 O GLU A 349 9388 5442 9878 -902 1539 -313 O
ATOM 2185 CB GLU A 349 17.415 1.659 70.775 1.00 93.20 C
ANISOU 2185 CB GLU A 349 12712 9425 13275 -305 1192 -4 C
ATOM 2186 CG GLU A 349 18.194 0.645 69.956 1.00104.86 C
ANISOU 2186 CG GLU A 349 13939 10997 14907 -363 1129 22 C
ATOM 2187 CD GLU A 349 17.748 0.595 68.508 1.00116.47 C
ANISOU 2187 CD GLU A 349 15516 12426 16311 -128 1267 145 C
ATOM 2188 OE1 GLU A 349 16.837 1.365 68.137 1.00122.98 O
ANISOU 2188 OE1 GLU A 349 16607 13162 16958 101 1408 215 O
ATOM 2189 OE2 GLU A 349 18.313 -0.214 67.740 1.00117.56 O
ANISOU 2189 OE2 GLU A 349 15474 12630 16562 -156 1236 171 O
ATOM 2190 N SER A 350 17.777 4.171 73.071 1.00 79.46 N
ANISOU 2190 N SER A 350 11417 7324 11450 -687 1420 -287 N
ATOM 2191 CA SER A 350 18.156 5.575 73.176 1.00 81.99 C
ANISOU 2191 CA SER A 350 12067 7337 11748 -837 1713 -390 C
ATOM 2192 C SER A 350 19.569 5.742 73.719 1.00 88.75 C
ANISOU 2192 C SER A 350 12772 8176 12773 -1260 1727 -596 C
ATOM 2193 O SER A 350 20.251 6.715 73.380 1.00102.44 O
ANISOU 2193 O SER A 350 14722 9651 14549 -1456 2016 -698 O
ATOM 2194 CB SER A 350 17.160 6.318 74.067 1.00 85.35 C
ANISOU 2194 CB SER A 350 12737 7697 11995 -715 1743 -398 C
ATOM 2195 OG SER A 350 15.826 5.982 73.727 1.00 86.57 O
ANISOU 2195 OG SER A 350 12935 7971 11988 -327 1667 -231 O
ATOM 2196 N TYR A 351 20.022 4.821 74.573 1.00 77.62 N
ANISOU 2196 N TYR A 351 11000 7047 11445 -1403 1432 -670 N
ATOM 2197 CA TYR A 351 21.399 4.866 75.053 1.00 83.52 C
ANISOU 2197 CA TYR A 351 11536 7859 12339 -1778 1411 -874 C
ATOM 2198 C TYR A 351 22.415 4.443 73.997 1.00 81.86 C
ANISOU 2198 C TYR A 351 11147 7661 12294 -1875 1480 -879 C
ATOM 2199 O TYR A 351 23.584 4.831 74.093 1.00 85.66 O
ANISOU 2199 O TYR A 351 11532 8125 12888 -2198 1583 -1068 O
ATOM 2200 CB TYR A 351 21.549 3.995 76.301 1.00 66.78 C
ANISOU 2200 CB TYR A 351 9092 6059 10223 -1847 1066 -936 C
ATOM 2201 CG TYR A 351 20.959 4.630 77.536 1.00 67.52 C
ANISOU 2201 CG TYR A 351 9343 6133 10178 -1888 1034 -1017 C
ATOM 2202 CD1 TYR A 351 19.680 4.310 77.961 1.00 65.72 C
ANISOU 2202 CD1 TYR A 351 9195 5970 9805 -1617 903 -880 C
ATOM 2203 CD2 TYR A 351 21.677 5.567 78.266 1.00 78.71 C
ANISOU 2203 CD2 TYR A 351 10830 7474 11604 -2214 1150 -1248 C
ATOM 2204 CE1 TYR A 351 19.133 4.897 79.084 1.00 66.47 C
ANISOU 2204 CE1 TYR A 351 9438 6047 9770 -1649 883 -956 C
ATOM 2205 CE2 TYR A 351 21.139 6.160 79.393 1.00 71.01 C
ANISOU 2205 CE2 TYR A 351 10012 6474 10496 -2256 1130 -1330 C
ATOM 2206 CZ TYR A 351 19.866 5.822 79.797 1.00 74.79 C
ANISOU 2206 CZ TYR A 351 10573 7010 10834 -1963 995 -1176 C
ATOM 2207 OH TYR A 351 19.319 6.407 80.916 1.00 75.65 O
ANISOU 2207 OH TYR A 351 10840 7097 10808 -1997 982 -1257 O
ATOM 2208 N LEU A 352 22.010 3.654 73.007 1.00 76.11 N
ANISOU 2208 N LEU A 352 10359 6982 11578 -1618 1432 -695 N
ATOM 2209 CA LEU A 352 22.949 3.148 72.015 1.00 79.58 C
ANISOU 2209 CA LEU A 352 10612 7452 12172 -1693 1482 -694 C
ATOM 2210 C LEU A 352 23.280 4.202 70.962 1.00 84.58 C
ANISOU 2210 C LEU A 352 11549 7766 12821 -1767 1862 -711 C
ATOM 2211 O LEU A 352 22.462 5.065 70.631 1.00 81.50 O
ANISOU 2211 O LEU A 352 11540 7133 12294 -1605 2072 -629 O
ATOM 2212 CB LEU A 352 22.389 1.889 71.356 1.00 76.07 C
ANISOU 2212 CB LEU A 352 10003 7173 11726 -1405 1299 -503 C
ATOM 2213 CG LEU A 352 22.147 0.775 72.376 1.00 67.39 C
ANISOU 2213 CG LEU A 352 8626 6365 10615 -1350 953 -486 C
ATOM 2214 CD1 LEU A 352 21.706 -0.487 71.684 1.00 68.69 C
ANISOU 2214 CD1 LEU A 352 8640 6668 10790 -1116 813 -325 C
ATOM 2215 CD2 LEU A 352 23.393 0.519 73.212 1.00 66.75 C
ANISOU 2215 CD2 LEU A 352 8252 6457 10652 -1622 818 -659 C
ATOM 2216 N THR A 353 24.496 4.112 70.426 1.00 92.60 N
ANISOU 2216 N THR A 353 12398 8789 13997 -1998 1961 -816 N
ATOM 2217 CA THR A 353 25.019 5.085 69.476 1.00 71.56 C
ANISOU 2217 CA THR A 353 10002 5821 11365 -2137 2346 -864 C
ATOM 2218 C THR A 353 24.995 4.527 68.058 1.00 71.99 C
ANISOU 2218 C THR A 353 10048 5847 11456 -1932 2416 -698 C
ATOM 2219 O THR A 353 25.367 3.374 67.826 1.00 72.66 O
ANISOU 2219 O THR A 353 9786 6178 11645 -1887 2201 -662 O
ATOM 2220 CB THR A 353 26.451 5.480 69.846 1.00 74.32 C
ANISOU 2220 CB THR A 353 10173 6201 11863 -2588 2451 -1135 C
ATOM 2221 OG1 THR A 353 27.353 4.448 69.433 1.00 77.15 O
ANISOU 2221 OG1 THR A 353 10121 6812 12380 -2644 2300 -1158 O
ATOM 2222 CG2 THR A 353 26.573 5.668 71.350 1.00 78.86 C
ANISOU 2222 CG2 THR A 353 10619 6935 12411 -2786 2275 -1313 C
ATOM 2223 N GLY A 354 24.568 5.358 67.111 1.00 79.38 N
ANISOU 2223 N GLY A 354 11388 6478 12294 -1797 2730 -597 N
ATOM 2224 CA GLY A 354 24.630 5.003 65.708 1.00 85.35 C
ANISOU 2224 CA GLY A 354 12181 7180 13069 -1630 2848 -460 C
ATOM 2225 C GLY A 354 23.512 4.073 65.281 1.00 88.89 C
ANISOU 2225 C GLY A 354 12561 7804 13408 -1223 2622 -244 C
ATOM 2226 O GLY A 354 22.623 3.705 66.051 1.00 88.92 O
ANISOU 2226 O GLY A 354 12502 7966 13319 -1061 2385 -194 O
ATOM 2227 N SER A 355 23.563 3.692 64.008 1.00 91.18 N
ANISOU 2227 N SER A 355 12865 8074 13705 -1072 2713 -130 N
ATOM 2228 CA SER A 355 22.617 2.722 63.480 1.00 88.49 C
ANISOU 2228 CA SER A 355 12421 7931 13270 -727 2511 43 C
ATOM 2229 C SER A 355 22.970 1.323 63.971 1.00 85.46 C
ANISOU 2229 C SER A 355 11581 7863 13027 -799 2176 4 C
ATOM 2230 O SER A 355 24.125 1.026 64.288 1.00 92.42 O
ANISOU 2230 O SER A 355 12212 8812 14090 -1071 2135 -128 O
ATOM 2231 CB SER A 355 22.610 2.748 61.955 1.00 86.90 C
ANISOU 2231 CB SER A 355 12377 7620 13020 -554 2718 163 C
ATOM 2232 OG SER A 355 23.846 2.294 61.441 1.00 77.32 O
ANISOU 2232 OG SER A 355 10946 6427 12007 -785 2771 82 O
ATOM 2233 N ARG A 356 21.955 0.460 64.042 1.00 79.70 N
ANISOU 2233 N ARG A 356 10749 7335 12199 -546 1946 115 N
ATOM 2234 CA ARG A 356 22.166 -0.883 64.572 1.00 73.73 C
ANISOU 2234 CA ARG A 356 9619 6847 11549 -587 1647 94 C
ATOM 2235 C ARG A 356 23.143 -1.689 63.722 1.00 71.48 C
ANISOU 2235 C ARG A 356 9113 6620 11427 -662 1661 85 C
ATOM 2236 O ARG A 356 23.899 -2.512 64.257 1.00 74.01 O
ANISOU 2236 O ARG A 356 9132 7100 11890 -796 1487 15 O
ATOM 2237 CB ARG A 356 20.821 -1.602 64.685 1.00 71.39 C
ANISOU 2237 CB ARG A 356 9299 6725 11099 -317 1456 206 C
ATOM 2238 CG ARG A 356 20.876 -3.111 64.537 1.00 65.60 C
ANISOU 2238 CG ARG A 356 8270 6213 10441 -276 1245 238 C
ATOM 2239 CD ARG A 356 19.623 -3.747 65.104 1.00 66.91 C
ANISOU 2239 CD ARG A 356 8398 6558 10467 -108 1048 292 C
ATOM 2240 NE ARG A 356 19.858 -4.318 66.427 1.00 74.90 N
ANISOU 2240 NE ARG A 356 9226 7687 11544 -238 833 231 N
ATOM 2241 CZ ARG A 356 18.907 -4.838 67.195 1.00 68.85 C
ANISOU 2241 CZ ARG A 356 8425 7064 10672 -153 664 255 C
ATOM 2242 NH1 ARG A 356 17.651 -4.851 66.774 1.00 68.21 N
ANISOU 2242 NH1 ARG A 356 8449 7050 10418 50 680 320 N
ATOM 2243 NH2 ARG A 356 19.210 -5.342 68.383 1.00 65.26 N
ANISOU 2243 NH2 ARG A 356 7825 6701 10269 -266 484 207 N
ATOM 2244 N ASP A 357 23.155 -1.462 62.407 1.00 74.01 N
ANISOU 2244 N ASP A 357 9585 6818 11716 -560 1869 158 N
ATOM 2245 CA ASP A 357 24.051 -2.225 61.543 1.00 80.40 C
ANISOU 2245 CA ASP A 357 10196 7680 12673 -621 1897 150 C
ATOM 2246 C ASP A 357 25.510 -1.955 61.891 1.00 88.41 C
ANISOU 2246 C ASP A 357 11048 8660 13884 -942 1972 -10 C
ATOM 2247 O ASP A 357 26.357 -2.858 61.824 1.00 91.25 O
ANISOU 2247 O ASP A 357 11106 9169 14396 -1025 1867 -58 O
ATOM 2248 CB ASP A 357 23.762 -1.888 60.080 1.00 89.06 C
ANISOU 2248 CB ASP A 357 11524 8639 13674 -451 2130 254 C
ATOM 2249 CG ASP A 357 24.421 -2.852 59.112 1.00104.08 C
ANISOU 2249 CG ASP A 357 13225 10625 15694 -453 2132 268 C
ATOM 2250 OD1 ASP A 357 24.972 -3.881 59.564 1.00110.21 O
ANISOU 2250 OD1 ASP A 357 13687 11575 16614 -542 1937 216 O
ATOM 2251 OD2 ASP A 357 24.385 -2.581 57.894 1.00107.86 O
ANISOU 2251 OD2 ASP A 357 13877 10995 16111 -348 2337 337 O
ATOM 2252 N GLU A 358 25.818 -0.721 62.294 1.00 98.85 N
ANISOU 2252 N GLU A 358 12561 9800 15196 -1127 2159 -107 N
ATOM 2253 CA GLU A 358 27.180 -0.405 62.707 1.00100.94 C
ANISOU 2253 CA GLU A 358 12650 10071 15632 -1470 2234 -299 C
ATOM 2254 C GLU A 358 27.564 -1.168 63.969 1.00 93.21 C
ANISOU 2254 C GLU A 358 11315 9366 14736 -1566 1920 -395 C
ATOM 2255 O GLU A 358 28.674 -1.707 64.061 1.00 98.50 O
ANISOU 2255 O GLU A 358 11667 10199 15560 -1721 1854 -504 O
ATOM 2256 CB GLU A 358 27.323 1.099 62.931 1.00108.04 C
ANISOU 2256 CB GLU A 358 13863 10704 16482 -1668 2518 -400 C
ATOM 2257 CG GLU A 358 27.026 1.949 61.707 1.00109.87 C
ANISOU 2257 CG GLU A 358 14498 10632 16614 -1566 2868 -301 C
ATOM 2258 CD GLU A 358 26.925 3.421 62.048 1.00107.68 C
ANISOU 2258 CD GLU A 358 14606 10057 16249 -1707 3151 -373 C
ATOM 2259 OE1 GLU A 358 26.617 3.732 63.219 1.00105.70 O
ANISOU 2259 OE1 GLU A 358 14358 9844 15958 -1777 3029 -447 O
ATOM 2260 OE2 GLU A 358 27.161 4.265 61.157 1.00107.66 O
ANISOU 2260 OE2 GLU A 358 14924 9771 16211 -1750 3509 -358 O
ATOM 2261 N ARG A 359 26.653 -1.241 64.945 1.00 76.12 N
ANISOU 2261 N ARG A 359 9197 7268 12457 -1454 1725 -352 N
ATOM 2262 CA ARG A 359 26.948 -1.983 66.165 1.00 73.17 C
ANISOU 2262 CA ARG A 359 8520 7150 12131 -1512 1428 -423 C
ATOM 2263 C ARG A 359 27.119 -3.466 65.873 1.00 67.97 C
ANISOU 2263 C ARG A 359 7585 6695 11544 -1356 1226 -338 C
ATOM 2264 O ARG A 359 27.972 -4.133 66.471 1.00 68.78 O
ANISOU 2264 O ARG A 359 7382 7006 11747 -1437 1058 -421 O
ATOM 2265 CB ARG A 359 25.839 -1.763 67.197 1.00 74.65 C
ANISOU 2265 CB ARG A 359 8850 7348 12165 -1409 1285 -380 C
ATOM 2266 CG ARG A 359 25.814 -0.366 67.790 1.00 80.19 C
ANISOU 2266 CG ARG A 359 9788 7876 12806 -1593 1452 -497 C
ATOM 2267 CD ARG A 359 24.537 0.376 67.438 1.00 78.97 C
ANISOU 2267 CD ARG A 359 10024 7509 12474 -1387 1597 -371 C
ATOM 2268 NE ARG A 359 23.354 -0.263 68.002 1.00 75.34 N
ANISOU 2268 NE ARG A 359 9551 7188 11888 -1147 1362 -255 N
ATOM 2269 CZ ARG A 359 22.120 0.216 67.882 1.00 76.85 C
ANISOU 2269 CZ ARG A 359 10015 7281 11902 -929 1423 -150 C
ATOM 2270 NH1 ARG A 359 21.904 1.343 67.218 1.00 74.27 N
ANISOU 2270 NH1 ARG A 359 10023 6699 11496 -886 1709 -126 N
ATOM 2271 NH2 ARG A 359 21.099 -0.433 68.423 1.00 82.66 N
ANISOU 2271 NH2 ARG A 359 10696 8179 12531 -744 1209 -70 N
ATOM 2272 N LYS A 360 26.348 -3.993 64.918 1.00 63.73 N
ANISOU 2272 N LYS A 360 7158 6108 10947 -1125 1253 -181 N
ATOM 2273 CA LYS A 360 26.473 -5.409 64.589 1.00 63.28 C
ANISOU 2273 CA LYS A 360 6878 6213 10951 -987 1094 -107 C
ATOM 2274 C LYS A 360 27.811 -5.701 63.920 1.00 70.28 C
ANISOU 2274 C LYS A 360 7553 7140 12012 -1105 1186 -183 C
ATOM 2275 O LYS A 360 28.501 -6.665 64.278 1.00 73.56 O
ANISOU 2275 O LYS A 360 7686 7741 12522 -1096 1022 -211 O
ATOM 2276 CB LYS A 360 25.320 -5.853 63.691 1.00 61.39 C
ANISOU 2276 CB LYS A 360 6804 5925 10594 -743 1120 47 C
ATOM 2277 CG LYS A 360 25.604 -7.167 62.984 1.00 65.26 C
ANISOU 2277 CG LYS A 360 7115 6518 11164 -640 1057 104 C
ATOM 2278 CD LYS A 360 24.446 -8.143 63.069 1.00 72.16 C
ANISOU 2278 CD LYS A 360 8013 7483 11921 -444 904 207 C
ATOM 2279 CE LYS A 360 23.686 -8.216 61.755 1.00 72.79 C
ANISOU 2279 CE LYS A 360 8246 7507 11904 -291 1038 291 C
ATOM 2280 NZ LYS A 360 22.999 -9.530 61.589 1.00 71.72 N
ANISOU 2280 NZ LYS A 360 8038 7494 11717 -158 912 350 N
ATOM 2281 N LYS A 361 28.199 -4.873 62.946 1.00 71.35 N
ANISOU 2281 N LYS A 361 7829 7101 12180 -1203 1461 -215 N
ATOM 2282 CA LYS A 361 29.480 -5.093 62.288 1.00 78.84 C
ANISOU 2282 CA LYS A 361 8571 8092 13292 -1335 1573 -302 C
ATOM 2283 C LYS A 361 30.632 -4.907 63.268 1.00 82.23 C
ANISOU 2283 C LYS A 361 8723 8688 13832 -1576 1497 -494 C
ATOM 2284 O LYS A 361 31.625 -5.643 63.222 1.00 86.62 O
ANISOU 2284 O LYS A 361 8966 9431 14514 -1605 1422 -559 O
ATOM 2285 CB LYS A 361 29.627 -4.149 61.091 1.00 89.43 C
ANISOU 2285 CB LYS A 361 10159 9193 14628 -1409 1912 -301 C
ATOM 2286 CG LYS A 361 30.831 -4.447 60.204 1.00 97.97 C
ANISOU 2286 CG LYS A 361 11050 10307 15867 -1521 2057 -373 C
ATOM 2287 CD LYS A 361 30.920 -3.469 59.036 1.00 99.21 C
ANISOU 2287 CD LYS A 361 11498 10200 15995 -1594 2417 -363 C
ATOM 2288 CE LYS A 361 31.945 -3.930 58.003 1.00 97.78 C
ANISOU 2288 CE LYS A 361 11143 10056 15954 -1657 2558 -403 C
ATOM 2289 NZ LYS A 361 33.335 -3.976 58.543 1.00 96.09 N
ANISOU 2289 NZ LYS A 361 10573 10022 15914 -1926 2543 -613 N
ATOM 2290 N SER A 362 30.489 -3.966 64.206 1.00 82.47 N
ANISOU 2290 N SER A 362 8852 8680 13803 -1734 1501 -592 N
ATOM 2291 CA SER A 362 31.539 -3.755 65.195 1.00 80.65 C
ANISOU 2291 CA SER A 362 8345 8647 13653 -1975 1417 -800 C
ATOM 2292 C SER A 362 31.669 -4.950 66.129 1.00 76.53 C
ANISOU 2292 C SER A 362 7522 8421 13134 -1826 1073 -775 C
ATOM 2293 O SER A 362 32.783 -5.398 66.416 1.00 78.62 O
ANISOU 2293 O SER A 362 7444 8930 13498 -1903 981 -896 O
ATOM 2294 CB SER A 362 31.259 -2.482 65.992 1.00 84.59 C
ANISOU 2294 CB SER A 362 9051 9023 14068 -2178 1509 -914 C
ATOM 2295 OG SER A 362 32.266 -2.262 66.965 1.00 90.40 O
ANISOU 2295 OG SER A 362 9503 9982 14863 -2431 1423 -1141 O
ATOM 2296 N LEU A 363 30.543 -5.496 66.596 1.00 76.41 N
ANISOU 2296 N LEU A 363 7633 8398 13002 -1600 890 -618 N
ATOM 2297 CA LEU A 363 30.604 -6.661 67.474 1.00 75.97 C
ANISOU 2297 CA LEU A 363 7349 8585 12930 -1441 591 -573 C
ATOM 2298 C LEU A 363 31.168 -7.875 66.747 1.00 81.55 C
ANISOU 2298 C LEU A 363 7855 9395 13736 -1281 549 -503 C
ATOM 2299 O LEU A 363 31.948 -8.648 67.322 1.00 86.03 O
ANISOU 2299 O LEU A 363 8136 10204 14347 -1223 373 -545 O
ATOM 2300 CB LEU A 363 29.212 -6.973 68.019 1.00 70.15 C
ANISOU 2300 CB LEU A 363 6825 7786 12042 -1255 453 -423 C
ATOM 2301 CG LEU A 363 29.063 -8.285 68.785 1.00 77.40 C
ANISOU 2301 CG LEU A 363 7595 8891 12922 -1057 183 -335 C
ATOM 2302 CD1 LEU A 363 29.814 -8.224 70.108 1.00 83.92 C
ANISOU 2302 CD1 LEU A 363 8197 9954 13736 -1148 -2 -464 C
ATOM 2303 CD2 LEU A 363 27.593 -8.603 68.999 1.00 58.32 C
ANISOU 2303 CD2 LEU A 363 5418 6376 10363 -892 118 -186 C
ATOM 2304 N LEU A 364 30.788 -8.060 65.480 1.00 83.35 N
ANISOU 2304 N LEU A 364 8234 9450 13986 -1189 713 -395 N
ATOM 2305 CA LEU A 364 31.323 -9.185 64.726 1.00 85.18 C
ANISOU 2305 CA LEU A 364 8297 9756 14310 -1046 701 -337 C
ATOM 2306 C LEU A 364 32.816 -9.027 64.472 1.00 91.36 C
ANISOU 2306 C LEU A 364 8789 10681 15241 -1202 783 -497 C
ATOM 2307 O LEU A 364 33.544 -10.025 64.434 1.00 96.16 O
ANISOU 2307 O LEU A 364 9147 11466 15922 -1080 683 -493 O
ATOM 2308 CB LEU A 364 30.553 -9.350 63.415 1.00 82.68 C
ANISOU 2308 CB LEU A 364 8212 9236 13965 -930 865 -205 C
ATOM 2309 CG LEU A 364 29.116 -9.851 63.589 1.00 72.79 C
ANISOU 2309 CG LEU A 364 7171 7920 12567 -742 759 -55 C
ATOM 2310 CD1 LEU A 364 28.418 -9.987 62.246 1.00 72.60 C
ANISOU 2310 CD1 LEU A 364 7338 7747 12498 -635 920 45 C
ATOM 2311 CD2 LEU A 364 29.099 -11.174 64.337 1.00 59.22 C
ANISOU 2311 CD2 LEU A 364 5307 6354 10840 -583 528 5 C
ATOM 2312 N SER A 365 33.293 -7.791 64.302 1.00 98.87 N
ANISOU 2312 N SER A 365 9774 11560 16231 -1472 980 -647 N
ATOM 2313 CA SER A 365 34.734 -7.571 64.265 1.00108.73 C
ANISOU 2313 CA SER A 365 10707 12996 17610 -1670 1050 -847 C
ATOM 2314 C SER A 365 35.379 -7.849 65.617 1.00108.35 C
ANISOU 2314 C SER A 365 10344 13275 17550 -1692 794 -971 C
ATOM 2315 O SER A 365 36.525 -8.312 65.674 1.00110.31 O
ANISOU 2315 O SER A 365 10237 13790 17886 -1701 736 -1084 O
ATOM 2316 CB SER A 365 35.038 -6.144 63.809 1.00115.72 C
ANISOU 2316 CB SER A 365 11740 13704 18526 -1989 1353 -994 C
ATOM 2317 OG SER A 365 34.695 -5.973 62.446 1.00117.56 O
ANISOU 2317 OG SER A 365 12219 13676 18772 -1945 1602 -886 O
ATOM 2318 N LYS A 366 34.661 -7.577 66.710 1.00108.08 N
ANISOU 2318 N LYS A 366 10427 13245 17393 -1686 638 -953 N
ATOM 2319 CA LYS A 366 35.189 -7.898 68.032 1.00107.37 C
ANISOU 2319 CA LYS A 366 10058 13478 17259 -1670 376 -1053 C
ATOM 2320 C LYS A 366 35.343 -9.399 68.213 1.00105.00 C
ANISOU 2320 C LYS A 366 9580 13361 16952 -1336 151 -915 C
ATOM 2321 O LYS A 366 36.260 -9.851 68.909 1.00107.87 O
ANISOU 2321 O LYS A 366 9612 14055 17319 -1283 -23 -1012 O
ATOM 2322 CB LYS A 366 34.279 -7.347 69.135 1.00107.95 C
ANISOU 2322 CB LYS A 366 10333 13493 17189 -1711 262 -1042 C
ATOM 2323 CG LYS A 366 34.038 -5.849 69.116 1.00106.59 C
ANISOU 2323 CG LYS A 366 10386 13117 16997 -2017 484 -1172 C
ATOM 2324 CD LYS A 366 35.311 -5.042 69.266 1.00110.62 C
ANISOU 2324 CD LYS A 366 10644 13799 17590 -2356 601 -1461 C
ATOM 2325 CE LYS A 366 34.993 -3.553 69.254 1.00111.60 C
ANISOU 2325 CE LYS A 366 11062 13661 17682 -2663 859 -1583 C
ATOM 2326 NZ LYS A 366 36.217 -2.713 69.341 1.00110.88 N
ANISOU 2326 NZ LYS A 366 10750 13710 17670 -3051 1023 -1893 N
ATOM 2327 N PHE A 367 34.462 -10.186 67.597 1.00102.58 N
ANISOU 2327 N PHE A 367 9496 12856 16625 -1105 160 -696 N
ATOM 2328 CA PHE A 367 34.497 -11.636 67.729 1.00104.56 C
ANISOU 2328 CA PHE A 367 9654 13217 16859 -789 -11 -552 C
ATOM 2329 C PHE A 367 35.128 -12.330 66.526 1.00114.57 C
ANISOU 2329 C PHE A 367 10811 14468 18252 -686 116 -516 C
ATOM 2330 O PHE A 367 35.123 -13.564 66.467 1.00112.38 O
ANISOU 2330 O PHE A 367 10505 14229 17966 -416 20 -387 O
ATOM 2331 CB PHE A 367 33.088 -12.173 67.979 1.00 97.36 C
ANISOU 2331 CB PHE A 367 9052 12117 15825 -614 -90 -353 C
ATOM 2332 CG PHE A 367 32.537 -11.810 69.329 1.00 97.70 C
ANISOU 2332 CG PHE A 367 9165 12224 15731 -645 -262 -369 C
ATOM 2333 CD1 PHE A 367 33.375 -11.343 70.331 1.00103.31 C
ANISOU 2333 CD1 PHE A 367 9634 13195 16423 -759 -388 -534 C
ATOM 2334 CD2 PHE A 367 31.184 -11.935 69.599 1.00 92.81 C
ANISOU 2334 CD2 PHE A 367 8839 11431 14995 -568 -296 -233 C
ATOM 2335 CE1 PHE A 367 32.876 -11.007 71.573 1.00102.35 C
ANISOU 2335 CE1 PHE A 367 9583 13138 16167 -790 -543 -554 C
ATOM 2336 CE2 PHE A 367 30.679 -11.603 70.842 1.00 92.26 C
ANISOU 2336 CE2 PHE A 367 8836 11421 14797 -597 -444 -250 C
ATOM 2337 CZ PHE A 367 31.527 -11.137 71.829 1.00 97.00 C
ANISOU 2337 CZ PHE A 367 9215 12262 15380 -705 -568 -405 C
ATOM 2338 N GLY A 368 35.670 -11.575 65.576 1.00126.55 N
ANISOU 2338 N GLY A 368 12288 15917 19878 -895 347 -629 N
ATOM 2339 CA GLY A 368 36.394 -12.170 64.465 1.00128.97 C
ANISOU 2339 CA GLY A 368 12459 16237 20306 -817 476 -621 C
ATOM 2340 C GLY A 368 35.553 -12.950 63.477 1.00129.35 C
ANISOU 2340 C GLY A 368 12761 16041 20344 -626 560 -424 C
ATOM 2341 O GLY A 368 36.003 -13.987 62.975 1.00131.26 O
ANISOU 2341 O GLY A 368 12890 16338 20645 -434 556 -365 O
ATOM 2342 N MET A 369 34.335 -12.490 63.194 1.00114.13 N
ANISOU 2342 N MET A 369 11169 13863 18333 -665 636 -331 N
ATOM 2343 CA MET A 369 33.423 -13.206 62.312 1.00104.42 C
ANISOU 2343 CA MET A 369 10173 12439 17064 -498 703 -167 C
ATOM 2344 C MET A 369 32.948 -12.298 61.184 1.00101.22 C
ANISOU 2344 C MET A 369 9995 11811 16652 -631 949 -163 C
ATOM 2345 O MET A 369 32.742 -11.097 61.386 1.00 95.75 O
ANISOU 2345 O MET A 369 9417 11042 15923 -813 1031 -230 O
ATOM 2346 CB MET A 369 32.221 -13.745 63.099 1.00 96.51 C
ANISOU 2346 CB MET A 369 9359 11389 15921 -354 530 -39 C
ATOM 2347 CG MET A 369 32.618 -14.521 64.347 1.00 95.56 C
ANISOU 2347 CG MET A 369 9066 11470 15771 -217 292 -31 C
ATOM 2348 SD MET A 369 31.263 -15.438 65.103 1.00 86.75 S
ANISOU 2348 SD MET A 369 8192 10272 14497 -31 136 132 S
ATOM 2349 CE MET A 369 30.745 -14.332 66.411 1.00 87.82 C
ANISOU 2349 CE MET A 369 8387 10458 14522 -183 10 69 C
ATOM 2350 N ASP A 370 32.769 -12.881 59.999 1.00103.28 N
ANISOU 2350 N ASP A 370 10341 11965 16934 -525 1075 -83 N
ATOM 2351 CA ASP A 370 32.229 -12.145 58.865 1.00105.77 C
ANISOU 2351 CA ASP A 370 10898 12082 17210 -593 1301 -54 C
ATOM 2352 C ASP A 370 30.756 -11.817 59.096 1.00 99.46 C
ANISOU 2352 C ASP A 370 10383 11167 16240 -536 1254 40 C
ATOM 2353 O ASP A 370 30.058 -12.486 59.862 1.00 97.47 O
ANISOU 2353 O ASP A 370 10154 10970 15911 -420 1066 105 O
ATOM 2354 CB ASP A 370 32.385 -12.938 57.567 1.00117.21 C
ANISOU 2354 CB ASP A 370 12354 13477 18704 -479 1430 2 C
ATOM 2355 CG ASP A 370 33.828 -13.278 57.258 1.00125.38 C
ANISOU 2355 CG ASP A 370 13102 14634 19904 -517 1493 -93 C
ATOM 2356 OD1 ASP A 370 34.060 -14.274 56.539 1.00126.53 O
ANISOU 2356 OD1 ASP A 370 13195 14784 20096 -376 1528 -45 O
ATOM 2357 OD2 ASP A 370 34.727 -12.561 57.745 1.00129.31 O
ANISOU 2357 OD2 ASP A 370 13418 15235 20479 -691 1512 -227 O
ATOM 2358 N GLU A 371 30.290 -10.762 58.428 1.00 97.46 N
ANISOU 2358 N GLU A 371 10356 10758 15917 -609 1439 47 N
ATOM 2359 CA GLU A 371 28.923 -10.296 58.631 1.00 95.09 C
ANISOU 2359 CA GLU A 371 10315 10373 15441 -540 1409 124 C
ATOM 2360 C GLU A 371 27.913 -11.384 58.288 1.00 99.79 C
ANISOU 2360 C GLU A 371 10979 10999 15937 -343 1316 231 C
ATOM 2361 O GLU A 371 28.064 -12.115 57.305 1.00103.17 O
ANISOU 2361 O GLU A 371 11382 11422 16397 -266 1392 261 O
ATOM 2362 CB GLU A 371 28.643 -9.055 57.782 1.00 95.47 C
ANISOU 2362 CB GLU A 371 10617 10244 15415 -595 1653 131 C
ATOM 2363 CG GLU A 371 28.927 -7.733 58.474 1.00104.01 C
ANISOU 2363 CG GLU A 371 11776 11245 16497 -783 1731 42 C
ATOM 2364 CD GLU A 371 28.291 -6.555 57.755 1.00110.71 C
ANISOU 2364 CD GLU A 371 12968 11886 17213 -766 1964 90 C
ATOM 2365 OE1 GLU A 371 27.697 -6.763 56.675 1.00111.85 O
ANISOU 2365 OE1 GLU A 371 13260 11978 17262 -600 2055 190 O
ATOM 2366 OE2 GLU A 371 28.381 -5.422 58.273 1.00111.90 O
ANISOU 2366 OE2 GLU A 371 13251 11926 17340 -909 2062 25 O
ATOM 2367 N GLY A 372 26.879 -11.480 59.112 1.00100.80 N
ANISOU 2367 N GLY A 372 11194 11165 15942 -280 1165 272 N
ATOM 2368 CA GLY A 372 25.821 -12.454 58.913 1.00 96.27 C
ANISOU 2368 CA GLY A 372 10686 10634 15256 -134 1086 344 C
ATOM 2369 C GLY A 372 24.799 -12.300 60.016 1.00 96.25 C
ANISOU 2369 C GLY A 372 10766 10680 15126 -112 933 363 C
ATOM 2370 O GLY A 372 25.034 -11.623 61.023 1.00108.82 O
ANISOU 2370 O GLY A 372 12336 12277 16732 -198 863 324 O
ATOM 2371 N VAL A 373 23.647 -12.944 59.809 1.00 79.36 N
ANISOU 2371 N VAL A 373 8714 8587 12852 -9 892 407 N
ATOM 2372 CA VAL A 373 22.571 -12.865 60.790 1.00 74.34 C
ANISOU 2372 CA VAL A 373 8152 8012 12080 13 762 419 C
ATOM 2373 C VAL A 373 23.042 -13.478 62.096 1.00 79.13 C
ANISOU 2373 C VAL A 373 8639 8666 12761 -29 593 410 C
ATOM 2374 O VAL A 373 23.529 -14.612 62.119 1.00 79.89 O
ANISOU 2374 O VAL A 373 8636 8782 12935 4 551 424 O
ATOM 2375 CB VAL A 373 21.323 -13.582 60.261 1.00 61.86 C
ANISOU 2375 CB VAL A 373 6648 6509 10347 106 763 438 C
ATOM 2376 CG1 VAL A 373 20.124 -13.287 61.143 1.00 61.75 C
ANISOU 2376 CG1 VAL A 373 6716 6575 10173 127 663 436 C
ATOM 2377 CG2 VAL A 373 21.062 -13.187 58.821 1.00 63.58 C
ANISOU 2377 CG2 VAL A 373 6950 6714 10493 176 926 446 C
ATOM 2378 N THR A 374 22.837 -12.766 63.199 1.00 74.63 N
ANISOU 2378 N THR A 374 8098 8114 12145 -80 501 391 N
ATOM 2379 CA THR A 374 23.401 -13.154 64.485 1.00 71.12 C
ANISOU 2379 CA THR A 374 7538 7729 11756 -115 339 378 C
ATOM 2380 C THR A 374 22.310 -13.693 65.399 1.00 69.32 C
ANISOU 2380 C THR A 374 7390 7557 11392 -70 214 411 C
ATOM 2381 O THR A 374 21.277 -13.042 65.595 1.00 79.37 O
ANISOU 2381 O THR A 374 8788 8837 12532 -70 219 408 O
ATOM 2382 CB THR A 374 24.109 -11.975 65.152 1.00 71.83 C
ANISOU 2382 CB THR A 374 7583 7813 11895 -236 327 307 C
ATOM 2383 OG1 THR A 374 25.181 -11.528 64.314 1.00 72.87 O
ANISOU 2383 OG1 THR A 374 7632 7897 12158 -308 465 258 O
ATOM 2384 CG2 THR A 374 24.674 -12.393 66.500 1.00 72.59 C
ANISOU 2384 CG2 THR A 374 7544 8017 12019 -255 141 285 C
ATOM 2385 N PHE A 375 22.552 -14.872 65.963 1.00 53.24 N
ANISOU 2385 N PHE A 375 5293 5557 9380 -23 117 444 N
ATOM 2386 CA PHE A 375 21.675 -15.486 66.949 1.00 49.06 C
ANISOU 2386 CA PHE A 375 4845 5066 8730 3 11 475 C
ATOM 2387 C PHE A 375 22.432 -15.501 68.271 1.00 50.10 C
ANISOU 2387 C PHE A 375 4891 5253 8891 0 -143 475 C
ATOM 2388 O PHE A 375 23.311 -16.340 68.492 1.00 54.94 O
ANISOU 2388 O PHE A 375 5408 5887 9579 71 -195 505 O
ATOM 2389 CB PHE A 375 21.256 -16.882 66.505 1.00 48.76 C
ANISOU 2389 CB PHE A 375 4857 5001 8667 63 57 514 C
ATOM 2390 CG PHE A 375 20.449 -16.887 65.244 1.00 65.04 C
ANISOU 2390 CG PHE A 375 6985 7054 10672 58 195 491 C
ATOM 2391 CD1 PHE A 375 19.068 -16.873 65.292 1.00 67.49 C
ANISOU 2391 CD1 PHE A 375 7396 7426 10820 38 208 466 C
ATOM 2392 CD2 PHE A 375 21.073 -16.882 64.007 1.00 65.56 C
ANISOU 2392 CD2 PHE A 375 6998 7078 10834 77 311 483 C
ATOM 2393 CE1 PHE A 375 18.323 -16.869 64.129 1.00 71.56 C
ANISOU 2393 CE1 PHE A 375 7945 7986 11258 49 321 429 C
ATOM 2394 CE2 PHE A 375 20.331 -16.876 62.842 1.00 68.31 C
ANISOU 2394 CE2 PHE A 375 7405 7445 11107 87 430 458 C
ATOM 2395 CZ PHE A 375 18.954 -16.871 62.905 1.00 71.70 C
ANISOU 2395 CZ PHE A 375 7920 7959 11361 78 428 429 C
ATOM 2396 N MET A 376 22.140 -14.515 69.110 1.00 67.04 N
ANISOU 2396 N MET A 376 7068 7435 10970 -68 -210 437 N
ATOM 2397 CA MET A 376 22.595 -14.506 70.486 1.00 51.06 C
ANISOU 2397 CA MET A 376 4986 5492 8923 -74 -370 428 C
ATOM 2398 C MET A 376 21.761 -15.480 71.308 1.00 50.67 C
ANISOU 2398 C MET A 376 5050 5454 8748 -6 -448 495 C
ATOM 2399 O MET A 376 20.601 -15.750 70.997 1.00 49.55 O
ANISOU 2399 O MET A 376 5040 5274 8514 -9 -380 513 O
ATOM 2400 CB MET A 376 22.487 -13.094 71.062 1.00 63.23 C
ANISOU 2400 CB MET A 376 6548 7052 10424 -189 -391 350 C
ATOM 2401 CG MET A 376 22.927 -12.945 72.503 1.00 59.86 C
ANISOU 2401 CG MET A 376 6057 6733 9954 -215 -558 317 C
ATOM 2402 SD MET A 376 22.529 -11.312 73.145 1.00 62.38 S
ANISOU 2402 SD MET A 376 6461 7040 10199 -364 -548 217 S
ATOM 2403 CE MET A 376 23.056 -11.493 74.846 1.00 72.02 C
ANISOU 2403 CE MET A 376 7589 8425 11351 -373 -767 182 C
ATOM 2404 N PHE A 377 22.381 -16.035 72.340 1.00 62.96 N
ANISOU 2404 N PHE A 377 6553 7077 10291 59 -582 525 N
ATOM 2405 CA PHE A 377 21.677 -16.753 73.389 1.00 64.10 C
ANISOU 2405 CA PHE A 377 6829 7229 10297 111 -659 585 C
ATOM 2406 C PHE A 377 22.334 -16.397 74.710 1.00 59.96 C
ANISOU 2406 C PHE A 377 6227 6826 9729 127 -831 567 C
ATOM 2407 O PHE A 377 23.559 -16.274 74.786 1.00 54.67 O
ANISOU 2407 O PHE A 377 5377 6251 9145 163 -900 536 O
ATOM 2408 CB PHE A 377 21.701 -18.273 73.192 1.00 52.30 C
ANISOU 2408 CB PHE A 377 5414 5662 8798 233 -614 677 C
ATOM 2409 CG PHE A 377 21.431 -19.043 74.457 1.00 76.79 C
ANISOU 2409 CG PHE A 377 8641 8769 11765 313 -702 749 C
ATOM 2410 CD1 PHE A 377 20.136 -19.215 74.918 1.00 80.08 C
ANISOU 2410 CD1 PHE A 377 9240 9145 12043 243 -664 756 C
ATOM 2411 CD2 PHE A 377 22.476 -19.571 75.201 1.00 75.99 C
ANISOU 2411 CD2 PHE A 377 8476 8735 11663 469 -820 806 C
ATOM 2412 CE1 PHE A 377 19.888 -19.910 76.092 1.00 53.32 C
ANISOU 2412 CE1 PHE A 377 5993 5746 8521 309 -724 825 C
ATOM 2413 CE2 PHE A 377 22.233 -20.261 76.373 1.00 56.05 C
ANISOU 2413 CE2 PHE A 377 6097 6209 8991 568 -892 887 C
ATOM 2414 CZ PHE A 377 20.938 -20.432 76.817 1.00 55.16 C
ANISOU 2414 CZ PHE A 377 6192 6021 8746 478 -836 899 C
ATOM 2415 N ILE A 378 21.518 -16.262 75.751 1.00 56.96 N
ANISOU 2415 N ILE A 378 5971 6468 9204 101 -899 576 N
ATOM 2416 CA ILE A 378 21.993 -15.810 77.050 1.00 61.25 C
ANISOU 2416 CA ILE A 378 6456 7140 9675 101 -1063 544 C
ATOM 2417 C ILE A 378 21.230 -16.551 78.138 1.00 62.41 C
ANISOU 2417 C ILE A 378 6779 7280 9653 168 -1123 624 C
ATOM 2418 O ILE A 378 20.066 -16.925 77.966 1.00 66.13 O
ANISOU 2418 O ILE A 378 7419 7655 10052 135 -1024 657 O
ATOM 2419 CB ILE A 378 21.848 -14.275 77.189 1.00 65.47 C
ANISOU 2419 CB ILE A 378 6955 7708 10213 -64 -1062 424 C
ATOM 2420 CG1 ILE A 378 22.580 -13.758 78.429 1.00 68.88 C
ANISOU 2420 CG1 ILE A 378 7283 8300 10589 -91 -1228 355 C
ATOM 2421 CG2 ILE A 378 20.378 -13.860 77.181 1.00 68.12 C
ANISOU 2421 CG2 ILE A 378 7476 7962 10444 -130 -981 424 C
ATOM 2422 CD1 ILE A 378 22.607 -12.250 78.521 1.00 75.65 C
ANISOU 2422 CD1 ILE A 378 8112 9168 11463 -274 -1199 217 C
ATOM 2423 N GLY A 379 21.902 -16.764 79.264 1.00 63.22 N
ANISOU 2423 N GLY A 379 6836 7505 9679 261 -1280 645 N
ATOM 2424 CA GLY A 379 21.354 -17.546 80.351 1.00 77.88 C
ANISOU 2424 CA GLY A 379 8875 9352 11363 353 -1334 736 C
ATOM 2425 C GLY A 379 22.259 -18.700 80.724 1.00 86.99 C
ANISOU 2425 C GLY A 379 10022 10546 12486 583 -1405 845 C
ATOM 2426 O GLY A 379 23.028 -19.196 79.894 1.00 89.74 O
ANISOU 2426 O GLY A 379 10268 10874 12954 679 -1361 870 O
ATOM 2427 N ARG A 380 22.172 -19.137 81.976 1.00 90.34 N
ANISOU 2427 N ARG A 380 10565 11025 12734 695 -1508 914 N
ATOM 2428 CA ARG A 380 23.058 -20.177 82.474 1.00100.25 C
ANISOU 2428 CA ARG A 380 11834 12340 13919 966 -1588 1030 C
ATOM 2429 C ARG A 380 22.770 -21.554 81.885 1.00 98.79 C
ANISOU 2429 C ARG A 380 11868 11926 13743 1082 -1411 1161 C
ATOM 2430 O ARG A 380 21.653 -21.854 81.454 1.00 90.49 O
ANISOU 2430 O ARG A 380 11010 10690 12683 942 -1245 1168 O
ATOM 2431 CB ARG A 380 22.986 -20.255 83.999 1.00115.08 C
ANISOU 2431 CB ARG A 380 13815 14333 15576 1067 -1736 1077 C
ATOM 2432 CG ARG A 380 21.643 -20.694 84.556 1.00122.19 C
ANISOU 2432 CG ARG A 380 15038 15060 16328 1002 -1628 1148 C
ATOM 2433 CD ARG A 380 21.647 -20.660 86.076 1.00132.05 C
ANISOU 2433 CD ARG A 380 16379 16441 17353 1100 -1780 1187 C
ATOM 2434 NE ARG A 380 20.371 -21.087 86.644 1.00138.54 N
ANISOU 2434 NE ARG A 380 17513 17098 18027 1026 -1660 1250 N
ATOM 2435 CZ ARG A 380 19.337 -20.279 86.852 1.00141.92 C
ANISOU 2435 CZ ARG A 380 17980 17514 18430 793 -1623 1154 C
ATOM 2436 NH1 ARG A 380 19.424 -18.994 86.535 1.00138.65 N
ANISOU 2436 NH1 ARG A 380 17344 17212 18123 626 -1688 1005 N
ATOM 2437 NH2 ARG A 380 18.214 -20.754 87.378 1.00144.40 N
ANISOU 2437 NH2 ARG A 380 18564 17699 18602 731 -1505 1205 N
ATOM 2438 N PHE A 381 23.832 -22.342 81.813 1.00105.61 N
ANISOU 2438 N PHE A 381 12693 12817 14616 1340 -1440 1252 N
ATOM 2439 CA PHE A 381 23.706 -23.698 81.249 1.00108.49 C
ANISOU 2439 CA PHE A 381 13281 12952 14988 1475 -1258 1376 C
ATOM 2440 C PHE A 381 23.156 -24.657 82.291 1.00116.87 C
ANISOU 2440 C PHE A 381 14687 13885 15832 1613 -1213 1519 C
ATOM 2441 O PHE A 381 23.712 -24.757 83.378 1.00127.17 O
ANISOU 2441 O PHE A 381 16003 15335 16982 1824 -1370 1589 O
ATOM 2442 CB PHE A 381 25.083 -24.184 80.817 1.00105.64 C
ANISOU 2442 CB PHE A 381 12749 12669 14720 1724 -1294 1419 C
ATOM 2443 CG PHE A 381 25.721 -23.377 79.722 1.00100.59 C
ANISOU 2443 CG PHE A 381 11768 12164 14286 1592 -1329 1277 C
ATOM 2444 CD1 PHE A 381 25.409 -23.605 78.398 1.00 98.23 C
ANISOU 2444 CD1 PHE A 381 11463 11706 14153 1478 -1151 1244 C
ATOM 2445 CD2 PHE A 381 26.648 -22.404 80.014 1.00100.58 C
ANISOU 2445 CD2 PHE A 381 11461 12451 14303 1571 -1525 1166 C
ATOM 2446 CE1 PHE A 381 26.014 -22.884 77.390 1.00 95.71 C
ANISOU 2446 CE1 PHE A 381 10861 11494 14012 1359 -1162 1121 C
ATOM 2447 CE2 PHE A 381 27.248 -21.675 79.004 1.00 96.55 C
ANISOU 2447 CE2 PHE A 381 10665 12042 13978 1425 -1522 1028 C
ATOM 2448 CZ PHE A 381 26.931 -21.920 77.696 1.00 93.24 C
ANISOU 2448 CZ PHE A 381 10262 11443 13720 1327 -1337 1015 C
ATOM 2449 N ASP A 382 22.061 -25.315 81.941 1.00115.67 N
ANISOU 2449 N ASP A 382 14819 13474 15657 1489 -988 1551 N
ATOM 2450 CA ASP A 382 21.427 -26.349 82.789 1.00122.24 C
ANISOU 2450 CA ASP A 382 16032 14119 16294 1596 -869 1687 C
ATOM 2451 C ASP A 382 20.469 -27.194 81.952 1.00119.91 C
ANISOU 2451 C ASP A 382 15976 13545 16041 1412 -579 1672 C
ATOM 2452 O ASP A 382 20.014 -26.709 80.913 1.00118.66 O
ANISOU 2452 O ASP A 382 15687 13390 16010 1153 -510 1538 O
ATOM 2453 CB ASP A 382 20.768 -25.723 84.012 1.00132.13 C
ANISOU 2453 CB ASP A 382 17378 15459 17365 1515 -968 1679 C
ATOM 2454 CG ASP A 382 19.699 -24.735 83.609 1.00139.36 C
ANISOU 2454 CG ASP A 382 18105 16487 18357 1200 -1015 1509 C
ATOM 2455 OD1 ASP A 382 19.237 -24.841 82.465 1.00142.25 O
ANISOU 2455 OD1 ASP A 382 18350 16810 18889 1019 -918 1410 O
ATOM 2456 OD2 ASP A 382 19.350 -23.872 84.434 1.00142.38 O
ANISOU 2456 OD2 ASP A 382 18469 17005 18622 1151 -1148 1478 O
ATOM 2457 N ARG A 383 20.160 -28.409 82.398 1.00123.91 N
ANISOU 2457 N ARG A 383 16841 13816 16424 1552 -402 1804 N
ATOM 2458 CA ARG A 383 19.251 -29.278 81.609 1.00120.38 C
ANISOU 2458 CA ARG A 383 16663 13093 15984 1357 -98 1776 C
ATOM 2459 C ARG A 383 17.862 -29.209 82.233 1.00116.52 C
ANISOU 2459 C ARG A 383 16355 12561 15356 1094 -6 1715 C
ATOM 2460 O ARG A 383 17.756 -29.355 83.449 1.00116.24 O
ANISOU 2460 O ARG A 383 16473 12549 15143 1188 -77 1799 O
ATOM 2461 CB ARG A 383 19.776 -30.716 81.542 1.00121.25 C
ANISOU 2461 CB ARG A 383 17115 12936 16016 1615 90 1938 C
ATOM 2462 CG ARG A 383 18.943 -31.657 80.681 1.00115.25 C
ANISOU 2462 CG ARG A 383 16664 11866 15259 1401 441 1895 C
ATOM 2463 CD ARG A 383 19.432 -31.916 79.268 1.00105.70 C
ANISOU 2463 CD ARG A 383 15311 10602 14249 1364 539 1823 C
ATOM 2464 NE ARG A 383 20.788 -32.433 79.161 1.00 99.62 N
ANISOU 2464 NE ARG A 383 14524 9803 13524 1746 488 1960 N
ATOM 2465 CZ ARG A 383 21.337 -32.875 78.034 1.00 90.91 C
ANISOU 2465 CZ ARG A 383 13354 8615 12571 1788 594 1934 C
ATOM 2466 NH1 ARG A 383 20.644 -32.874 76.911 1.00 78.82 N
ANISOU 2466 NH1 ARG A 383 11773 7022 11155 1469 754 1776 N
ATOM 2467 NH2 ARG A 383 22.577 -33.319 78.032 1.00 91.86 N
ANISOU 2467 NH2 ARG A 383 13450 8735 12717 2162 540 2061 N
ATOM 2468 N GLY A 384 16.848 -28.992 81.405 1.00112.74 N
ANISOU 2468 N GLY A 384 15850 12041 14946 773 153 1564 N
ATOM 2469 CA GLY A 384 15.472 -28.920 81.913 1.00106.57 C
ANISOU 2469 CA GLY A 384 15207 11247 14037 506 261 1478 C
ATOM 2470 C GLY A 384 15.097 -27.525 82.347 1.00100.97 C
ANISOU 2470 C GLY A 384 14249 10799 13316 392 52 1384 C
ATOM 2471 O GLY A 384 14.000 -27.368 82.873 1.00104.55 O
ANISOU 2471 O GLY A 384 14810 11268 13647 201 124 1320 O
ATOM 2472 N GLN A 385 15.965 -26.538 82.154 1.00 95.96 N
ANISOU 2472 N GLN A 385 13296 10365 12801 493 -187 1366 N
ATOM 2473 CA GLN A 385 15.532 -25.179 82.559 1.00 93.12 C
ANISOU 2473 CA GLN A 385 12723 10225 12431 379 -361 1268 C
ATOM 2474 C GLN A 385 15.661 -24.184 81.410 1.00 88.44 C
ANISOU 2474 C GLN A 385 11821 9760 12021 277 -417 1144 C
ATOM 2475 O GLN A 385 14.676 -23.935 80.740 1.00 83.39 O
ANISOU 2475 O GLN A 385 11145 9132 11407 73 -296 1027 O
ATOM 2476 CB GLN A 385 16.308 -24.683 83.772 1.00 97.64 C
ANISOU 2476 CB GLN A 385 13240 10934 12924 584 -601 1353 C
ATOM 2477 CG GLN A 385 15.922 -25.361 85.070 1.00103.06 C
ANISOU 2477 CG GLN A 385 14231 11543 13385 664 -570 1461 C
ATOM 2478 CD GLN A 385 16.275 -24.476 86.236 1.00108.99 C
ANISOU 2478 CD GLN A 385 14883 12500 14028 750 -813 1470 C
ATOM 2479 OE1 GLN A 385 16.831 -23.398 86.067 1.00109.93 O
ANISOU 2479 OE1 GLN A 385 14712 12812 14245 704 -987 1372 O
ATOM 2480 NE2 GLN A 385 15.949 -24.926 87.433 1.00110.60 N
ANISOU 2480 NE2 GLN A 385 15346 12656 14019 869 -811 1582 N
ATOM 2481 N LYS A 386 16.853 -23.647 81.202 1.00 87.43 N
ANISOU 2481 N LYS A 386 11471 9742 12008 421 -592 1163 N
ATOM 2482 CA LYS A 386 17.027 -22.615 80.189 1.00 78.80 C
ANISOU 2482 CA LYS A 386 10108 8756 11075 331 -638 1053 C
ATOM 2483 C LYS A 386 17.080 -23.173 78.773 1.00 91.68 C
ANISOU 2483 C LYS A 386 11713 10283 12838 300 -480 1029 C
ATOM 2484 O LYS A 386 16.978 -22.395 77.817 1.00 97.61 O
ANISOU 2484 O LYS A 386 12285 11103 13699 206 -473 936 O
ATOM 2485 CB LYS A 386 18.286 -21.798 80.483 1.00 75.47 C
ANISOU 2485 CB LYS A 386 9461 8488 10728 458 -851 1058 C
ATOM 2486 CG LYS A 386 18.152 -20.914 81.714 1.00 76.71 C
ANISOU 2486 CG LYS A 386 9592 8786 10767 430 -1012 1028 C
ATOM 2487 CD LYS A 386 16.838 -20.143 81.693 1.00 71.48 C
ANISOU 2487 CD LYS A 386 8960 8142 10055 220 -948 926 C
ATOM 2488 CE LYS A 386 16.631 -19.360 82.978 1.00 71.97 C
ANISOU 2488 CE LYS A 386 9037 8323 9987 194 -1085 899 C
ATOM 2489 NZ LYS A 386 15.301 -18.691 82.999 1.00 69.79 N
ANISOU 2489 NZ LYS A 386 8806 8066 9645 19 -1009 806 N
ATOM 2490 N GLY A 387 17.236 -24.484 78.610 1.00 88.05 N
ANISOU 2490 N GLY A 387 11445 9650 12360 384 -341 1111 N
ATOM 2491 CA GLY A 387 17.106 -25.075 77.294 1.00 80.90 C
ANISOU 2491 CA GLY A 387 10548 8636 11557 320 -163 1069 C
ATOM 2492 C GLY A 387 18.285 -24.892 76.368 1.00 73.26 C
ANISOU 2492 C GLY A 387 9376 7696 10764 446 -216 1081 C
ATOM 2493 O GLY A 387 18.128 -25.048 75.153 1.00 72.02 O
ANISOU 2493 O GLY A 387 9170 7493 10701 364 -90 1017 O
ATOM 2494 N VAL A 388 19.467 -24.560 76.897 1.00 70.35 N
ANISOU 2494 N VAL A 388 8875 7423 10434 637 -395 1148 N
ATOM 2495 CA VAL A 388 20.645 -24.443 76.047 1.00 57.68 C
ANISOU 2495 CA VAL A 388 7064 5859 8993 754 -433 1149 C
ATOM 2496 C VAL A 388 20.974 -25.769 75.379 1.00105.49 C
ANISOU 2496 C VAL A 388 13270 11727 15086 875 -262 1220 C
ATOM 2497 O VAL A 388 21.596 -25.789 74.312 1.00 96.71 O
ANISOU 2497 O VAL A 388 12019 10608 14117 906 -215 1193 O
ATOM 2498 CB VAL A 388 21.851 -23.918 76.855 1.00 58.99 C
ANISOU 2498 CB VAL A 388 7044 6205 9167 931 -656 1186 C
ATOM 2499 CG1 VAL A 388 22.231 -24.896 77.952 1.00 61.40 C
ANISOU 2499 CG1 VAL A 388 7533 6469 9326 1170 -700 1326 C
ATOM 2500 CG2 VAL A 388 23.029 -23.645 75.928 1.00 59.22 C
ANISOU 2500 CG2 VAL A 388 6817 6312 9373 1008 -685 1152 C
ATOM 2501 N ASP A 389 20.569 -26.889 75.981 1.00 96.09 N
ANISOU 2501 N ASP A 389 12381 10365 13762 940 -147 1310 N
ATOM 2502 CA ASP A 389 20.731 -28.174 75.314 1.00 95.13 C
ANISOU 2502 CA ASP A 389 12459 10021 13665 1025 64 1365 C
ATOM 2503 C ASP A 389 19.952 -28.210 74.007 1.00 90.29 C
ANISOU 2503 C ASP A 389 11833 9342 13133 780 246 1234 C
ATOM 2504 O ASP A 389 20.429 -28.756 73.005 1.00 89.40 O
ANISOU 2504 O ASP A 389 11712 9133 13123 832 364 1231 O
ATOM 2505 CB ASP A 389 20.264 -29.295 76.240 1.00 97.16 C
ANISOU 2505 CB ASP A 389 13096 10077 13743 1096 194 1472 C
ATOM 2506 CG ASP A 389 18.838 -29.093 76.713 1.00100.84 C
ANISOU 2506 CG ASP A 389 13699 10528 14086 820 268 1390 C
ATOM 2507 OD1 ASP A 389 18.318 -27.970 76.559 1.00103.04 O
ANISOU 2507 OD1 ASP A 389 13759 10992 14400 635 162 1273 O
ATOM 2508 OD2 ASP A 389 18.231 -30.053 77.224 1.00108.16 O
ANISOU 2508 OD2 ASP A 389 14963 11256 14876 789 448 1438 O
ATOM 2509 N VAL A 390 18.762 -27.602 73.988 1.00 85.61 N
ANISOU 2509 N VAL A 390 11221 8823 12484 523 266 1120 N
ATOM 2510 CA VAL A 390 17.977 -27.548 72.761 1.00 71.88 C
ANISOU 2510 CA VAL A 390 9434 7084 10792 304 415 981 C
ATOM 2511 C VAL A 390 18.683 -26.694 71.719 1.00 68.42 C
ANISOU 2511 C VAL A 390 8709 6772 10516 336 330 935 C
ATOM 2512 O VAL A 390 18.686 -27.023 70.528 1.00 73.80 O
ANISOU 2512 O VAL A 390 9366 7403 11273 283 463 875 O
ATOM 2513 CB VAL A 390 16.560 -27.026 73.057 1.00 55.78 C
ANISOU 2513 CB VAL A 390 7409 5151 8633 61 434 866 C
ATOM 2514 CG1 VAL A 390 15.710 -27.052 71.799 1.00 54.79 C
ANISOU 2514 CG1 VAL A 390 7227 5069 8522 -145 587 711 C
ATOM 2515 CG2 VAL A 390 15.915 -27.844 74.161 1.00 72.62 C
ANISOU 2515 CG2 VAL A 390 9832 7158 10603 18 530 910 C
ATOM 2516 N LEU A 391 19.334 -25.612 72.151 1.00 62.72 N
ANISOU 2516 N LEU A 391 7779 6208 9845 417 122 956 N
ATOM 2517 CA LEU A 391 20.046 -24.771 71.196 1.00 58.14 C
ANISOU 2517 CA LEU A 391 6948 5729 9415 431 67 909 C
ATOM 2518 C LEU A 391 21.271 -25.481 70.637 1.00 55.55 C
ANISOU 2518 C LEU A 391 6580 5320 9205 614 109 973 C
ATOM 2519 O LEU A 391 21.540 -25.406 69.435 1.00 67.96 O
ANISOU 2519 O LEU A 391 8052 6882 10886 584 194 922 O
ATOM 2520 CB LEU A 391 20.451 -23.450 71.845 1.00 56.08 C
ANISOU 2520 CB LEU A 391 6496 5639 9171 441 -135 896 C
ATOM 2521 CG LEU A 391 21.390 -22.625 70.964 1.00 57.61 C
ANISOU 2521 CG LEU A 391 6450 5914 9523 460 -172 853 C
ATOM 2522 CD1 LEU A 391 20.699 -22.216 69.670 1.00 51.78 C
ANISOU 2522 CD1 LEU A 391 5685 5170 8817 319 -44 764 C
ATOM 2523 CD2 LEU A 391 21.911 -21.419 71.708 1.00 69.59 C
ANISOU 2523 CD2 LEU A 391 7803 7583 11055 455 -348 828 C
ATOM 2524 N LEU A 392 22.028 -26.170 71.489 1.00 57.45 N
ANISOU 2524 N LEU A 392 6898 5514 9415 824 53 1088 N
ATOM 2525 CA LEU A 392 23.209 -26.875 71.002 1.00 80.57 C
ANISOU 2525 CA LEU A 392 9785 8386 12443 1039 93 1153 C
ATOM 2526 C LEU A 392 22.824 -28.031 70.087 1.00 77.60 C
ANISOU 2526 C LEU A 392 9620 7789 12075 1008 340 1148 C
ATOM 2527 O LEU A 392 23.494 -28.282 69.076 1.00 59.70 O
ANISOU 2527 O LEU A 392 7266 5488 9928 1073 420 1134 O
ATOM 2528 CB LEU A 392 24.046 -27.364 72.184 1.00 61.30 C
ANISOU 2528 CB LEU A 392 7391 5973 9929 1313 -29 1282 C
ATOM 2529 CG LEU A 392 24.617 -26.236 73.046 1.00 61.32 C
ANISOU 2529 CG LEU A 392 7145 6228 9926 1347 -280 1262 C
ATOM 2530 CD1 LEU A 392 25.300 -26.784 74.289 1.00 63.82 C
ANISOU 2530 CD1 LEU A 392 7525 6603 10123 1629 -406 1386 C
ATOM 2531 CD2 LEU A 392 25.571 -25.366 72.237 1.00 60.91 C
ANISOU 2531 CD2 LEU A 392 6760 6338 10045 1328 -346 1176 C
ATOM 2532 N LYS A 393 21.729 -28.729 70.405 1.00 70.44 N
ANISOU 2532 N LYS A 393 8990 6735 11039 886 479 1143 N
ATOM 2533 CA LYS A 393 21.254 -29.786 69.520 1.00 68.51 C
ANISOU 2533 CA LYS A 393 8952 6286 10791 797 737 1100 C
ATOM 2534 C LYS A 393 20.758 -29.214 68.198 1.00 71.94 C
ANISOU 2534 C LYS A 393 9224 6808 11302 582 801 951 C
ATOM 2535 O LYS A 393 20.974 -29.811 67.139 1.00 71.30 O
ANISOU 2535 O LYS A 393 9176 6626 11288 577 960 913 O
ATOM 2536 CB LYS A 393 20.148 -30.588 70.205 1.00 69.03 C
ANISOU 2536 CB LYS A 393 9344 6193 10691 667 888 1097 C
ATOM 2537 CG LYS A 393 20.595 -31.427 71.391 1.00 73.41 C
ANISOU 2537 CG LYS A 393 10154 6596 11143 902 893 1262 C
ATOM 2538 CD LYS A 393 19.390 -32.036 72.090 1.00 83.19 C
ANISOU 2538 CD LYS A 393 11710 7688 12210 719 1053 1240 C
ATOM 2539 CE LYS A 393 19.759 -32.634 73.433 1.00 94.77 C
ANISOU 2539 CE LYS A 393 13430 9035 13543 960 1027 1416 C
ATOM 2540 NZ LYS A 393 18.539 -33.067 74.168 1.00 97.53 N
ANISOU 2540 NZ LYS A 393 14074 9262 13723 748 1180 1384 N
ATOM 2541 N ALA A 394 20.104 -28.048 68.233 1.00 76.56 N
ANISOU 2541 N ALA A 394 9642 7583 11863 424 684 868 N
ATOM 2542 CA ALA A 394 19.700 -27.397 66.993 1.00 54.74 C
ANISOU 2542 CA ALA A 394 6720 4927 9151 274 728 744 C
ATOM 2543 C ALA A 394 20.899 -26.938 66.176 1.00 54.61 C
ANISOU 2543 C ALA A 394 6495 4956 9297 402 679 765 C
ATOM 2544 O ALA A 394 20.851 -26.977 64.946 1.00 58.03 O
ANISOU 2544 O ALA A 394 6878 5387 9783 338 792 692 O
ATOM 2545 CB ALA A 394 18.781 -26.217 67.296 1.00 53.09 C
ANISOU 2545 CB ALA A 394 6402 4907 8864 130 614 670 C
ATOM 2546 N ILE A 395 21.979 -26.508 66.832 1.00 65.25 N
ANISOU 2546 N ILE A 395 7712 6364 10717 574 519 852 N
ATOM 2547 CA ILE A 395 23.196 -26.156 66.105 1.00 69.05 C
ANISOU 2547 CA ILE A 395 7986 6897 11355 686 492 859 C
ATOM 2548 C ILE A 395 23.820 -27.400 65.486 1.00 77.97 C
ANISOU 2548 C ILE A 395 9217 7865 12543 823 648 901 C
ATOM 2549 O ILE A 395 24.348 -27.357 64.370 1.00 82.62 O
ANISOU 2549 O ILE A 395 9698 8453 13240 833 729 862 O
ATOM 2550 CB ILE A 395 24.179 -25.414 67.033 1.00 77.71 C
ANISOU 2550 CB ILE A 395 8895 8135 12495 813 286 910 C
ATOM 2551 CG1 ILE A 395 23.601 -24.054 67.443 1.00 54.56 C
ANISOU 2551 CG1 ILE A 395 5864 5344 9521 656 163 848 C
ATOM 2552 CG2 ILE A 395 25.549 -25.234 66.372 1.00 56.98 C
ANISOU 2552 CG2 ILE A 395 6049 5574 10028 936 276 908 C
ATOM 2553 CD1 ILE A 395 24.488 -23.255 68.377 1.00 57.01 C
ANISOU 2553 CD1 ILE A 395 5994 5807 9862 730 -29 863 C
ATOM 2554 N GLU A 396 23.737 -28.537 66.183 1.00 80.63 N
ANISOU 2554 N GLU A 396 9791 8047 12798 933 713 983 N
ATOM 2555 CA GLU A 396 24.183 -29.794 65.588 1.00 84.26 C
ANISOU 2555 CA GLU A 396 10411 8312 13293 1060 902 1020 C
ATOM 2556 C GLU A 396 23.318 -30.173 64.392 1.00 80.79 C
ANISOU 2556 C GLU A 396 10077 7776 12842 841 1113 900 C
ATOM 2557 O GLU A 396 23.820 -30.695 63.389 1.00 88.62 O
ANISOU 2557 O GLU A 396 11072 8682 13917 893 1251 878 O
ATOM 2558 CB GLU A 396 24.162 -30.910 66.635 1.00 97.16 C
ANISOU 2558 CB GLU A 396 12336 9768 14812 1222 956 1139 C
ATOM 2559 CG GLU A 396 25.275 -30.841 67.674 1.00111.96 C
ANISOU 2559 CG GLU A 396 14116 11738 16686 1529 770 1272 C
ATOM 2560 CD GLU A 396 26.653 -31.062 67.074 1.00120.27 C
ANISOU 2560 CD GLU A 396 14996 12833 17870 1778 767 1311 C
ATOM 2561 OE1 GLU A 396 27.648 -30.612 67.684 1.00122.95 O
ANISOU 2561 OE1 GLU A 396 15112 13368 18236 1980 574 1363 O
ATOM 2562 OE2 GLU A 396 26.741 -31.682 65.992 1.00122.17 O
ANISOU 2562 OE2 GLU A 396 15310 12930 18178 1764 961 1275 O
ATOM 2563 N ILE A 397 22.016 -29.897 64.476 1.00 68.99 N
ANISOU 2563 N ILE A 397 8653 6323 11237 598 1138 807 N
ATOM 2564 CA ILE A 397 21.112 -30.180 63.366 1.00 72.21 C
ANISOU 2564 CA ILE A 397 9122 6708 11605 376 1319 663 C
ATOM 2565 C ILE A 397 21.430 -29.285 62.174 1.00 71.55 C
ANISOU 2565 C ILE A 397 8790 6777 11619 345 1283 594 C
ATOM 2566 O ILE A 397 21.413 -29.731 61.021 1.00 82.84 O
ANISOU 2566 O ILE A 397 10242 8157 13075 289 1441 517 O
ATOM 2567 CB ILE A 397 19.650 -30.016 63.825 1.00 56.80 C
ANISOU 2567 CB ILE A 397 7259 4827 9495 138 1332 568 C
ATOM 2568 CG1 ILE A 397 19.265 -31.106 64.828 1.00 63.98 C
ANISOU 2568 CG1 ILE A 397 8474 5538 10297 131 1444 618 C
ATOM 2569 CG2 ILE A 397 18.703 -30.025 62.638 1.00 56.13 C
ANISOU 2569 CG2 ILE A 397 7146 4827 9353 -91 1470 390 C
ATOM 2570 CD1 ILE A 397 17.889 -30.911 65.443 1.00 60.27 C
ANISOU 2570 CD1 ILE A 397 8074 5155 9671 -102 1450 524 C
ATOM 2571 N LEU A 398 21.757 -28.020 62.435 1.00 64.65 N
ANISOU 2571 N LEU A 398 7696 6077 10792 381 1092 620 N
ATOM 2572 CA LEU A 398 22.057 -27.063 61.378 1.00 63.70 C
ANISOU 2572 CA LEU A 398 7369 6083 10749 353 1072 566 C
ATOM 2573 C LEU A 398 23.479 -27.180 60.851 1.00 68.78 C
ANISOU 2573 C LEU A 398 7894 6684 11555 522 1090 620 C
ATOM 2574 O LEU A 398 23.783 -26.584 59.813 1.00 64.00 O
ANISOU 2574 O LEU A 398 7154 6145 11017 494 1127 572 O
ATOM 2575 CB LEU A 398 21.822 -25.635 61.875 1.00 64.57 C
ANISOU 2575 CB LEU A 398 7329 6367 10837 309 896 563 C
ATOM 2576 CG LEU A 398 20.408 -25.302 62.351 1.00 68.45 C
ANISOU 2576 CG LEU A 398 7895 6946 11165 157 865 501 C
ATOM 2577 CD1 LEU A 398 20.327 -23.855 62.801 1.00 63.95 C
ANISOU 2577 CD1 LEU A 398 7190 6523 10585 148 707 509 C
ATOM 2578 CD2 LEU A 398 19.391 -25.589 61.262 1.00 72.53 C
ANISOU 2578 CD2 LEU A 398 8462 7512 11586 13 1012 376 C
ATOM 2579 N SER A 399 24.351 -27.920 61.541 1.00 81.42 N
ANISOU 2579 N SER A 399 9540 8190 13207 711 1069 719 N
ATOM 2580 CA SER A 399 25.727 -28.059 61.078 1.00 97.54 C
ANISOU 2580 CA SER A 399 11439 10226 15395 892 1084 761 C
ATOM 2581 C SER A 399 25.799 -28.708 59.703 1.00114.04 C
ANISOU 2581 C SER A 399 13587 12211 17531 866 1292 701 C
ATOM 2582 O SER A 399 26.686 -28.379 58.908 1.00114.29 O
ANISOU 2582 O SER A 399 13449 12294 17683 926 1318 687 O
ATOM 2583 CB SER A 399 26.535 -28.881 62.087 1.00100.46 C
ANISOU 2583 CB SER A 399 11872 10527 15770 1141 1033 880 C
ATOM 2584 OG SER A 399 26.257 -28.490 63.421 1.00100.78 O
ANISOU 2584 OG SER A 399 11922 10645 15726 1153 861 932 O
ATOM 2585 N SER A 400 24.875 -29.618 59.397 1.00127.77 N
ANISOU 2585 N SER A 400 15563 13812 19172 757 1454 651 N
ATOM 2586 CA SER A 400 24.901 -30.325 58.124 1.00131.70 C
ANISOU 2586 CA SER A 400 16139 14206 19696 719 1665 578 C
ATOM 2587 C SER A 400 24.237 -29.563 56.980 1.00127.29 C
ANISOU 2587 C SER A 400 15479 13782 19103 525 1702 453 C
ATOM 2588 O SER A 400 24.381 -29.982 55.825 1.00129.80 O
ANISOU 2588 O SER A 400 15820 14052 19448 500 1860 387 O
ATOM 2589 CB SER A 400 24.231 -31.693 58.280 1.00136.91 C
ANISOU 2589 CB SER A 400 17115 14650 20256 666 1852 554 C
ATOM 2590 OG SER A 400 22.921 -31.557 58.803 1.00136.34 O
ANISOU 2590 OG SER A 400 17144 14624 20037 457 1831 488 O
ATOM 2591 N LYS A 401 23.519 -28.475 57.257 1.00112.69 N
ANISOU 2591 N LYS A 401 13534 12102 17182 408 1568 423 N
ATOM 2592 CA LYS A 401 22.717 -27.805 56.240 1.00 98.96 C
ANISOU 2592 CA LYS A 401 11736 10503 15362 256 1606 311 C
ATOM 2593 C LYS A 401 23.501 -26.712 55.519 1.00 98.51 C
ANISOU 2593 C LYS A 401 11482 10543 15403 317 1564 330 C
ATOM 2594 O LYS A 401 24.483 -26.169 56.033 1.00 90.46 O
ANISOU 2594 O LYS A 401 10335 9534 14503 425 1461 411 O
ATOM 2595 CB LYS A 401 21.442 -27.227 56.855 1.00 84.39 C
ANISOU 2595 CB LYS A 401 9910 8793 13361 121 1509 264 C
ATOM 2596 CG LYS A 401 20.417 -28.306 57.164 1.00 80.41 C
ANISOU 2596 CG LYS A 401 9603 8222 12727 -15 1616 185 C
ATOM 2597 CD LYS A 401 19.187 -27.760 57.856 1.00 79.09 C
ANISOU 2597 CD LYS A 401 9434 8209 12407 -143 1520 132 C
ATOM 2598 CE LYS A 401 18.193 -28.879 58.132 1.00 84.29 C
ANISOU 2598 CE LYS A 401 10286 8804 12938 -315 1659 29 C
ATOM 2599 NZ LYS A 401 18.829 -30.032 58.834 1.00 86.84 N
ANISOU 2599 NZ LYS A 401 10810 8857 13329 -237 1747 120 N
ATOM 2600 N LYS A 402 23.053 -26.404 54.298 1.00103.16 N
ANISOU 2600 N LYS A 402 12054 11213 15927 238 1658 243 N
ATOM 2601 CA LYS A 402 23.817 -25.536 53.405 1.00100.95 C
ANISOU 2601 CA LYS A 402 11639 10986 15732 290 1681 256 C
ATOM 2602 C LYS A 402 23.855 -24.099 53.903 1.00 97.30 C
ANISOU 2602 C LYS A 402 11068 10630 15271 293 1540 302 C
ATOM 2603 O LYS A 402 24.773 -23.348 53.559 1.00 96.30 O
ANISOU 2603 O LYS A 402 10829 10508 15254 338 1549 334 O
ATOM 2604 CB LYS A 402 23.234 -25.583 51.987 1.00103.83 C
ANISOU 2604 CB LYS A 402 12041 11420 15990 219 1819 155 C
ATOM 2605 CG LYS A 402 23.320 -26.937 51.270 1.00108.87 C
ANISOU 2605 CG LYS A 402 12786 11945 16634 198 1995 86 C
ATOM 2606 CD LYS A 402 22.260 -27.938 51.742 1.00105.24 C
ANISOU 2606 CD LYS A 402 12484 11455 16048 77 2035 6 C
ATOM 2607 CE LYS A 402 20.874 -27.310 51.809 1.00 98.43 C
ANISOU 2607 CE LYS A 402 11607 10804 14986 -48 1959 -79 C
ATOM 2608 NZ LYS A 402 19.876 -28.232 52.421 1.00 94.19 N
ANISOU 2608 NZ LYS A 402 11206 10249 14333 -193 2001 -168 N
ATOM 2609 N GLU A 403 22.865 -23.696 54.686 1.00 94.22 N
ANISOU 2609 N GLU A 403 10721 10321 14759 233 1431 295 N
ATOM 2610 CA GLU A 403 22.708 -22.306 55.092 1.00 92.12 C
ANISOU 2610 CA GLU A 403 10392 10148 14463 228 1322 324 C
ATOM 2611 C GLU A 403 23.498 -21.942 56.343 1.00 89.06 C
ANISOU 2611 C GLU A 403 9925 9724 14189 269 1186 397 C
ATOM 2612 O GLU A 403 23.478 -20.774 56.746 1.00 90.36 O
ANISOU 2612 O GLU A 403 10046 9946 14343 250 1108 413 O
ATOM 2613 CB GLU A 403 21.225 -21.990 55.318 1.00 96.26 C
ANISOU 2613 CB GLU A 403 10988 10803 14784 160 1271 272 C
ATOM 2614 CG GLU A 403 20.339 -22.181 54.092 1.00101.63 C
ANISOU 2614 CG GLU A 403 11711 11594 15308 123 1382 176 C
ATOM 2615 CD GLU A 403 19.845 -23.606 53.943 1.00105.84 C
ANISOU 2615 CD GLU A 403 12323 12101 15792 39 1468 91 C
ATOM 2616 OE1 GLU A 403 20.441 -24.508 54.569 1.00111.05 O
ANISOU 2616 OE1 GLU A 403 13027 12602 16566 44 1479 131 O
ATOM 2617 OE2 GLU A 403 18.857 -23.823 53.208 1.00106.92 O
ANISOU 2617 OE2 GLU A 403 12484 12381 15761 -30 1533 -22 O
ATOM 2618 N PHE A 404 24.184 -22.904 56.967 1.00 86.23 N
ANISOU 2618 N PHE A 404 9558 9280 13926 334 1163 438 N
ATOM 2619 CA PHE A 404 24.733 -22.687 58.304 1.00 81.79 C
ANISOU 2619 CA PHE A 404 8929 8728 13421 384 1010 498 C
ATOM 2620 C PHE A 404 25.787 -21.585 58.334 1.00 85.96 C
ANISOU 2620 C PHE A 404 9281 9311 14068 392 965 503 C
ATOM 2621 O PHE A 404 25.945 -20.911 59.358 1.00 87.15 O
ANISOU 2621 O PHE A 404 9370 9521 14222 377 832 518 O
ATOM 2622 CB PHE A 404 25.316 -23.993 58.845 1.00 80.67 C
ANISOU 2622 CB PHE A 404 8825 8490 13334 501 1012 550 C
ATOM 2623 CG PHE A 404 25.819 -23.899 60.259 1.00 76.19 C
ANISOU 2623 CG PHE A 404 8199 7960 12790 583 846 614 C
ATOM 2624 CD1 PHE A 404 24.943 -23.980 61.329 1.00 78.56 C
ANISOU 2624 CD1 PHE A 404 8616 8266 12968 546 750 636 C
ATOM 2625 CD2 PHE A 404 27.171 -23.745 60.517 1.00 72.50 C
ANISOU 2625 CD2 PHE A 404 7548 7547 12452 699 786 641 C
ATOM 2626 CE1 PHE A 404 25.404 -23.901 62.629 1.00 80.88 C
ANISOU 2626 CE1 PHE A 404 8863 8606 13263 631 594 695 C
ATOM 2627 CE2 PHE A 404 27.638 -23.666 61.814 1.00 72.38 C
ANISOU 2627 CE2 PHE A 404 7460 7607 12432 785 621 686 C
ATOM 2628 CZ PHE A 404 26.754 -23.743 62.871 1.00 79.86 C
ANISOU 2628 CZ PHE A 404 8545 8547 13252 756 523 719 C
ATOM 2629 N GLN A 405 26.513 -21.379 57.235 1.00 88.18 N
ANISOU 2629 N GLN A 405 9484 9578 14443 398 1088 478 N
ATOM 2630 CA GLN A 405 27.547 -20.351 57.226 1.00 95.49 C
ANISOU 2630 CA GLN A 405 10245 10554 15484 370 1081 460 C
ATOM 2631 C GLN A 405 26.988 -18.953 56.992 1.00 88.13 C
ANISOU 2631 C GLN A 405 9364 9645 14477 261 1102 434 C
ATOM 2632 O GLN A 405 27.730 -17.975 57.137 1.00 86.54 O
ANISOU 2632 O GLN A 405 9062 9467 14354 199 1108 407 O
ATOM 2633 CB GLN A 405 28.611 -20.663 56.170 1.00110.35 C
ANISOU 2633 CB GLN A 405 12022 12408 17496 413 1224 438 C
ATOM 2634 CG GLN A 405 28.171 -20.424 54.737 1.00122.95 C
ANISOU 2634 CG GLN A 405 13716 13958 19042 366 1396 410 C
ATOM 2635 CD GLN A 405 27.301 -21.541 54.197 1.00127.45 C
ANISOU 2635 CD GLN A 405 14435 14477 19511 401 1458 409 C
ATOM 2636 OE1 GLN A 405 26.931 -22.462 54.925 1.00126.22 O
ANISOU 2636 OE1 GLN A 405 14343 14294 19320 443 1388 431 O
ATOM 2637 NE2 GLN A 405 26.976 -21.468 52.910 1.00130.88 N
ANISOU 2637 NE2 GLN A 405 14939 14901 19890 377 1604 374 N
ATOM 2638 N GLU A 406 25.709 -18.833 56.638 1.00 82.72 N
ANISOU 2638 N GLU A 406 8836 8960 13633 240 1126 433 N
ATOM 2639 CA GLU A 406 25.075 -17.527 56.527 1.00 78.87 C
ANISOU 2639 CA GLU A 406 8427 8497 13044 187 1140 425 C
ATOM 2640 C GLU A 406 24.745 -16.923 57.884 1.00 83.25 C
ANISOU 2640 C GLU A 406 8985 9088 13556 149 988 434 C
ATOM 2641 O GLU A 406 24.408 -15.735 57.951 1.00 86.19 O
ANISOU 2641 O GLU A 406 9423 9462 13865 109 1003 427 O
ATOM 2642 CB GLU A 406 23.798 -17.625 55.684 1.00 77.21 C
ANISOU 2642 CB GLU A 406 8357 8327 12652 213 1206 413 C
ATOM 2643 CG GLU A 406 24.039 -17.603 54.178 1.00 83.63 C
ANISOU 2643 CG GLU A 406 9195 9117 13462 240 1380 398 C
ATOM 2644 CD GLU A 406 22.751 -17.610 53.369 1.00 87.48 C
ANISOU 2644 CD GLU A 406 9801 9701 13738 280 1428 372 C
ATOM 2645 OE1 GLU A 406 22.256 -18.708 53.040 1.00 86.11 O
ANISOU 2645 OE1 GLU A 406 9638 9570 13508 278 1441 329 O
ATOM 2646 OE2 GLU A 406 22.231 -16.515 53.064 1.00 86.70 O
ANISOU 2646 OE2 GLU A 406 9786 9641 13514 319 1459 387 O
ATOM 2647 N MET A 407 24.839 -17.702 58.959 1.00 80.50 N
ANISOU 2647 N MET A 407 8591 8762 13233 172 854 452 N
ATOM 2648 CA MET A 407 24.429 -17.272 60.286 1.00 74.04 C
ANISOU 2648 CA MET A 407 7791 7989 12354 142 704 460 C
ATOM 2649 C MET A 407 25.573 -17.429 61.280 1.00 65.18 C
ANISOU 2649 C MET A 407 6515 6898 11351 154 592 463 C
ATOM 2650 O MET A 407 26.414 -18.324 61.156 1.00 65.46 O
ANISOU 2650 O MET A 407 6455 6931 11486 230 599 478 O
ATOM 2651 CB MET A 407 23.207 -18.071 60.760 1.00 70.57 C
ANISOU 2651 CB MET A 407 7470 7571 11773 163 644 477 C
ATOM 2652 CG MET A 407 23.472 -19.562 60.905 1.00 71.33 C
ANISOU 2652 CG MET A 407 7569 7623 11910 225 642 504 C
ATOM 2653 SD MET A 407 21.983 -20.565 61.084 1.00 71.88 S
ANISOU 2653 SD MET A 407 7809 7694 11808 195 659 490 S
ATOM 2654 CE MET A 407 21.323 -20.509 59.423 1.00 73.62 C
ANISOU 2654 CE MET A 407 8068 7948 11956 162 823 423 C
ATOM 2655 N ARG A 408 25.600 -16.527 62.257 1.00 57.64 N
ANISOU 2655 N ARG A 408 5535 5991 10374 90 491 441 N
ATOM 2656 CA ARG A 408 26.524 -16.545 63.378 1.00 64.97 C
ANISOU 2656 CA ARG A 408 6312 7003 11371 94 353 425 C
ATOM 2657 C ARG A 408 25.768 -16.881 64.656 1.00 66.26 C
ANISOU 2657 C ARG A 408 6559 7202 11415 127 198 464 C
ATOM 2658 O ARG A 408 24.585 -16.558 64.796 1.00 65.83 O
ANISOU 2658 O ARG A 408 6656 7121 11235 89 198 473 O
ATOM 2659 CB ARG A 408 27.214 -15.188 63.541 1.00 71.23 C
ANISOU 2659 CB ARG A 408 7008 7832 12225 -40 373 341 C
ATOM 2660 CG ARG A 408 27.825 -14.647 62.267 1.00 77.74 C
ANISOU 2660 CG ARG A 408 7795 8597 13146 -105 563 297 C
ATOM 2661 CD ARG A 408 29.040 -15.452 61.867 1.00 84.77 C
ANISOU 2661 CD ARG A 408 8486 9544 14178 -42 586 281 C
ATOM 2662 NE ARG A 408 29.625 -14.964 60.626 1.00 89.93 N
ANISOU 2662 NE ARG A 408 9109 10139 14922 -114 784 236 N
ATOM 2663 CZ ARG A 408 29.315 -15.435 59.425 1.00 88.55 C
ANISOU 2663 CZ ARG A 408 9029 9875 14741 -52 920 280 C
ATOM 2664 NH1 ARG A 408 28.425 -16.410 59.302 1.00 80.55 N
ANISOU 2664 NH1 ARG A 408 8137 8827 13640 63 883 353 N
ATOM 2665 NH2 ARG A 408 29.898 -14.931 58.347 1.00 93.45 N
ANISOU 2665 NH2 ARG A 408 9628 10444 15436 -119 1105 239 N
ATOM 2666 N PHE A 409 26.466 -17.512 65.599 1.00 70.12 N
ANISOU 2666 N PHE A 409 6945 7767 11931 210 68 485 N
ATOM 2667 CA PHE A 409 25.890 -17.875 66.889 1.00 65.69 C
ANISOU 2667 CA PHE A 409 6467 7241 11251 254 -77 529 C
ATOM 2668 C PHE A 409 26.779 -17.349 68.005 1.00 54.97 C
ANISOU 2668 C PHE A 409 4944 6029 9913 246 -231 484 C
ATOM 2669 O PHE A 409 27.975 -17.657 68.047 1.00 80.62 O
ANISOU 2669 O PHE A 409 8002 9377 13253 323 -270 466 O
ATOM 2670 CB PHE A 409 25.722 -19.392 67.014 1.00 63.42 C
ANISOU 2670 CB PHE A 409 6276 6894 10928 404 -77 617 C
ATOM 2671 CG PHE A 409 24.541 -19.927 66.265 1.00 52.43 C
ANISOU 2671 CG PHE A 409 5074 5385 9462 370 52 636 C
ATOM 2672 CD1 PHE A 409 23.275 -19.861 66.818 1.00 59.92 C
ANISOU 2672 CD1 PHE A 409 6178 6323 10266 305 26 639 C
ATOM 2673 CD2 PHE A 409 24.690 -20.488 65.006 1.00 52.36 C
ANISOU 2673 CD2 PHE A 409 5075 5300 9521 393 202 632 C
ATOM 2674 CE1 PHE A 409 22.181 -20.341 66.134 1.00 68.85 C
ANISOU 2674 CE1 PHE A 409 7448 7394 11316 255 143 625 C
ATOM 2675 CE2 PHE A 409 23.597 -20.973 64.316 1.00 51.36 C
ANISOU 2675 CE2 PHE A 409 5103 5101 9309 343 317 621 C
ATOM 2676 CZ PHE A 409 22.340 -20.899 64.881 1.00 50.45 C
ANISOU 2676 CZ PHE A 409 5120 5003 9047 270 286 611 C
ATOM 2677 N ILE A 410 26.198 -16.552 68.898 1.00 54.54 N
ANISOU 2677 N ILE A 410 4950 6009 9762 154 -316 455 N
ATOM 2678 CA ILE A 410 26.848 -16.149 70.140 1.00 67.60 C
ANISOU 2678 CA ILE A 410 6474 7818 11392 142 -481 406 C
ATOM 2679 C ILE A 410 26.137 -16.864 71.280 1.00 67.25 C
ANISOU 2679 C ILE A 410 6568 7784 11200 243 -606 490 C
ATOM 2680 O ILE A 410 24.902 -16.902 71.320 1.00 59.14 O
ANISOU 2680 O ILE A 410 5739 6656 10074 206 -565 528 O
ATOM 2681 CB ILE A 410 26.817 -14.622 70.337 1.00 65.48 C
ANISOU 2681 CB ILE A 410 6182 7572 11123 -57 -464 291 C
ATOM 2682 CG1 ILE A 410 27.278 -13.910 69.060 1.00 71.60 C
ANISOU 2682 CG1 ILE A 410 6905 8276 12023 -168 -282 224 C
ATOM 2683 CG2 ILE A 410 27.692 -14.223 71.518 1.00 57.90 C
ANISOU 2683 CG2 ILE A 410 5042 6808 10150 -94 -625 204 C
ATOM 2684 CD1 ILE A 410 27.355 -12.395 69.175 1.00 76.51 C
ANISOU 2684 CD1 ILE A 410 7541 8881 12650 -370 -217 107 C
ATOM 2685 N ILE A 411 26.907 -17.439 72.198 1.00 57.57 N
ANISOU 2685 N ILE A 411 5236 6693 9945 379 -752 515 N
ATOM 2686 CA ILE A 411 26.357 -18.109 73.372 1.00 57.83 C
ANISOU 2686 CA ILE A 411 5412 6737 9823 490 -867 602 C
ATOM 2687 C ILE A 411 27.000 -17.493 74.605 1.00 83.20 C
ANISOU 2687 C ILE A 411 8476 10163 12974 481 -1053 533 C
ATOM 2688 O ILE A 411 28.221 -17.304 74.641 1.00 84.95 O
ANISOU 2688 O ILE A 411 8446 10562 13267 515 -1121 461 O
ATOM 2689 CB ILE A 411 26.588 -19.632 73.325 1.00 58.77 C
ANISOU 2689 CB ILE A 411 5611 6796 9921 723 -849 729 C
ATOM 2690 CG1 ILE A 411 25.799 -20.270 72.173 1.00 57.21 C
ANISOU 2690 CG1 ILE A 411 5589 6386 9761 696 -655 774 C
ATOM 2691 CG2 ILE A 411 26.197 -20.276 74.649 1.00 64.53 C
ANISOU 2691 CG2 ILE A 411 6497 7544 10477 852 -964 820 C
ATOM 2692 CD1 ILE A 411 26.546 -20.349 70.847 1.00 63.73 C
ANISOU 2692 CD1 ILE A 411 6280 7185 10748 706 -535 742 C
ATOM 2693 N ILE A 412 26.183 -17.169 75.606 1.00 76.04 N
ANISOU 2693 N ILE A 412 7706 9258 11927 427 -1132 540 N
ATOM 2694 CA ILE A 412 26.653 -16.528 76.826 1.00 78.62 C
ANISOU 2694 CA ILE A 412 7914 9787 12169 397 -1306 463 C
ATOM 2695 C ILE A 412 26.034 -17.249 78.013 1.00 76.15 C
ANISOU 2695 C ILE A 412 7785 9478 11671 532 -1412 571 C
ATOM 2696 O ILE A 412 24.849 -17.603 77.989 1.00 70.55 O
ANISOU 2696 O ILE A 412 7319 8595 10890 510 -1327 647 O
ATOM 2697 CB ILE A 412 26.301 -15.021 76.860 1.00 78.42 C
ANISOU 2697 CB ILE A 412 7879 9756 12159 138 -1272 323 C
ATOM 2698 CG1 ILE A 412 26.838 -14.301 75.618 1.00 74.54 C
ANISOU 2698 CG1 ILE A 412 7263 9217 11841 -1 -1124 228 C
ATOM 2699 CG2 ILE A 412 26.850 -14.362 78.120 1.00 76.78 C
ANISOU 2699 CG2 ILE A 412 7540 9769 11862 82 -1444 216 C
ATOM 2700 CD1 ILE A 412 25.792 -14.047 74.548 1.00 75.27 C
ANISOU 2700 CD1 ILE A 412 7549 9082 11968 -75 -937 267 C
ATOM 2701 N GLY A 413 26.831 -17.465 79.044 1.00 83.74 N
ANISOU 2701 N GLY A 413 8625 10653 12539 670 -1590 569 N
ATOM 2702 CA GLY A 413 26.341 -18.099 80.249 1.00 88.62 C
ANISOU 2702 CA GLY A 413 9426 11287 12960 813 -1693 674 C
ATOM 2703 C GLY A 413 27.475 -18.757 81.002 1.00 90.54 C
ANISOU 2703 C GLY A 413 9522 11764 13114 1080 -1863 717 C
ATOM 2704 O GLY A 413 28.633 -18.735 80.585 1.00 84.65 O
ANISOU 2704 O GLY A 413 8508 11189 12464 1152 -1905 653 O
ATOM 2705 N LYS A 414 27.157 -19.363 82.129 1.00 97.14 N
ANISOU 2705 N LYS A 414 10541 12619 13749 1240 -1954 825 N
ATOM 2706 CA LYS A 414 28.178 -20.078 82.922 1.00103.16 C
ANISOU 2706 CA LYS A 414 11227 13598 14371 1559 -2117 901 C
ATOM 2707 C LYS A 414 27.426 -21.193 83.626 1.00107.50 C
ANISOU 2707 C LYS A 414 12142 13980 14724 1744 -2088 1092 C
ATOM 2708 O LYS A 414 26.309 -20.946 84.055 1.00110.62 O
ANISOU 2708 O LYS A 414 12750 14242 15040 1578 -2042 1097 O
ATOM 2709 CB LYS A 414 28.809 -19.136 83.948 1.00105.94 C
ANISOU 2709 CB LYS A 414 11302 14314 14636 1513 -2339 745 C
ATOM 2710 CG LYS A 414 29.870 -19.758 84.848 1.00109.05 C
ANISOU 2710 CG LYS A 414 11570 15010 14853 1871 -2537 805 C
ATOM 2711 CD LYS A 414 31.237 -19.860 84.202 1.00107.20 C
ANISOU 2711 CD LYS A 414 11046 14945 14739 2051 -2550 779 C
ATOM 2712 CE LYS A 414 32.063 -21.048 84.652 1.00106.69 C
ANISOU 2712 CE LYS A 414 10813 15249 14475 2436 -2768 820 C
ATOM 2713 NZ LYS A 414 33.443 -20.986 84.116 1.00104.10 N
ANISOU 2713 NZ LYS A 414 10172 15127 14255 2631 -2784 782 N
ATOM 2714 N GLY A 415 27.999 -22.379 83.731 1.00108.05 N
ANISOU 2714 N GLY A 415 12295 14051 14708 2092 -2096 1246 N
ATOM 2715 CA GLY A 415 27.210 -23.391 84.437 1.00108.38 C
ANISOU 2715 CA GLY A 415 12726 13899 14555 2278 -2030 1436 C
ATOM 2716 C GLY A 415 27.767 -24.781 84.326 1.00110.05 C
ANISOU 2716 C GLY A 415 13086 14028 14698 2670 -1971 1620 C
ATOM 2717 O GLY A 415 28.949 -24.975 84.562 1.00116.23 O
ANISOU 2717 O GLY A 415 13688 15082 15392 2982 -2135 1650 O
ATOM 2718 N ASP A 416 26.917 -25.705 83.922 1.00105.86 N
ANISOU 2718 N ASP A 416 12890 13136 14195 2663 -1727 1737 N
ATOM 2719 CA ASP A 416 27.301 -27.113 83.928 1.00112.59 C
ANISOU 2719 CA ASP A 416 13992 13835 14951 3036 -1621 1931 C
ATOM 2720 C ASP A 416 28.526 -27.348 83.048 1.00120.37 C
ANISOU 2720 C ASP A 416 14704 14946 16083 3239 -1642 1914 C
ATOM 2721 O ASP A 416 28.570 -26.866 81.910 1.00122.53 O
ANISOU 2721 O ASP A 416 14782 15187 16588 3007 -1566 1791 O
ATOM 2722 CB ASP A 416 26.133 -27.976 83.456 1.00107.75 C
ANISOU 2722 CB ASP A 416 13804 12791 14346 2906 -1321 2018 C
ATOM 2723 CG ASP A 416 26.570 -29.357 83.019 1.00107.24 C
ANISOU 2723 CG ASP A 416 13980 12507 14260 3223 -1144 2181 C
ATOM 2724 OD1 ASP A 416 26.921 -29.522 81.832 1.00108.36 O
ANISOU 2724 OD1 ASP A 416 14002 12575 14595 3191 -1038 2135 O
ATOM 2725 OD2 ASP A 416 26.581 -30.274 83.865 1.00110.00 O
ANISOU 2725 OD2 ASP A 416 14656 12749 14389 3517 -1102 2357 O
ATOM 2726 N PRO A 417 29.547 -28.051 83.549 1.00125.04 N
ANISOU 2726 N PRO A 417 15268 15705 16537 3682 -1746 2032 N
ATOM 2727 CA PRO A 417 30.749 -28.301 82.734 1.00125.64 C
ANISOU 2727 CA PRO A 417 15063 15931 16742 3902 -1766 2011 C
ATOM 2728 C PRO A 417 30.507 -29.033 81.425 1.00121.67 C
ANISOU 2728 C PRO A 417 14733 15079 16418 3855 -1488 2054 C
ATOM 2729 O PRO A 417 31.210 -28.756 80.447 1.00120.67 O
ANISOU 2729 O PRO A 417 14304 15057 16486 3816 -1481 1953 O
ATOM 2730 CB PRO A 417 31.637 -29.117 83.678 1.00133.94 C
ANISOU 2730 CB PRO A 417 16165 17182 17546 4444 -1899 2172 C
ATOM 2731 CG PRO A 417 31.196 -28.717 85.048 1.00135.58 C
ANISOU 2731 CG PRO A 417 16467 17526 17523 4428 -2064 2188 C
ATOM 2732 CD PRO A 417 29.713 -28.506 84.939 1.00130.70 C
ANISOU 2732 CD PRO A 417 16160 16545 16955 4014 -1880 2173 C
ATOM 2733 N GLU A 418 29.548 -29.963 81.360 1.00121.22 N
ANISOU 2733 N GLU A 418 15148 14614 16295 3841 -1245 2188 N
ATOM 2734 CA GLU A 418 29.415 -30.780 80.154 1.00122.47 C
ANISOU 2734 CA GLU A 418 15481 14454 16597 3830 -975 2225 C
ATOM 2735 C GLU A 418 28.877 -29.963 78.985 1.00114.81 C
ANISOU 2735 C GLU A 418 14326 13424 15873 3378 -890 2041 C
ATOM 2736 O GLU A 418 29.439 -29.994 77.884 1.00112.46 O
ANISOU 2736 O GLU A 418 13846 13129 15756 3375 -820 1982 O
ATOM 2737 CB GLU A 418 28.514 -31.989 80.414 1.00132.08 C
ANISOU 2737 CB GLU A 418 17267 15250 17667 3897 -713 2390 C
ATOM 2738 CG GLU A 418 28.526 -32.996 79.264 1.00139.06 C
ANISOU 2738 CG GLU A 418 18362 15808 18665 3947 -423 2436 C
ATOM 2739 CD GLU A 418 27.147 -33.540 78.917 1.00141.52 C
ANISOU 2739 CD GLU A 418 19090 15710 18972 3628 -121 2429 C
ATOM 2740 OE1 GLU A 418 26.252 -33.502 79.788 1.00145.15 O
ANISOU 2740 OE1 GLU A 418 19785 16086 19280 3494 -104 2456 O
ATOM 2741 OE2 GLU A 418 26.964 -34.002 77.767 1.00138.88 O
ANISOU 2741 OE2 GLU A 418 18834 15153 18780 3502 103 2381 O
ATOM 2742 N LEU A 419 27.781 -29.233 79.203 1.00108.35 N
ANISOU 2742 N LEU A 419 13560 12555 15051 3012 -889 1952 N
ATOM 2743 CA LEU A 419 27.246 -28.385 78.143 1.00 99.38 C
ANISOU 2743 CA LEU A 419 12254 11389 14118 2620 -820 1785 C
ATOM 2744 C LEU A 419 28.207 -27.258 77.788 1.00 94.07 C
ANISOU 2744 C LEU A 419 11111 11039 13592 2563 -1005 1643 C
ATOM 2745 O LEU A 419 28.289 -26.858 76.621 1.00 94.48 O
ANISOU 2745 O LEU A 419 11001 11063 13833 2384 -918 1540 O
ATOM 2746 CB LEU A 419 25.886 -27.822 78.556 1.00 90.24 C
ANISOU 2746 CB LEU A 419 11245 10145 12895 2290 -792 1725 C
ATOM 2747 CG LEU A 419 24.784 -28.865 78.755 1.00 70.35 C
ANISOU 2747 CG LEU A 419 9180 7300 10251 2248 -563 1820 C
ATOM 2748 CD1 LEU A 419 23.483 -28.209 79.192 1.00 68.24 C
ANISOU 2748 CD1 LEU A 419 8997 7012 9918 1923 -554 1737 C
ATOM 2749 CD2 LEU A 419 24.585 -29.681 77.483 1.00 79.34 C
ANISOU 2749 CD2 LEU A 419 10458 8181 11509 2191 -302 1814 C
ATOM 2750 N GLU A 420 28.957 -26.755 78.771 1.00 86.58 N
ANISOU 2750 N GLU A 420 9945 10404 12548 2710 -1247 1626 N
ATOM 2751 CA GLU A 420 29.947 -25.718 78.497 1.00 86.71 C
ANISOU 2751 CA GLU A 420 9510 10744 12693 2640 -1406 1467 C
ATOM 2752 C GLU A 420 31.077 -26.248 77.621 1.00 86.41 C
ANISOU 2752 C GLU A 420 9283 10771 12777 2861 -1357 1475 C
ATOM 2753 O GLU A 420 31.512 -25.575 76.678 1.00 88.25 O
ANISOU 2753 O GLU A 420 9244 11086 13200 2682 -1328 1338 O
ATOM 2754 CB GLU A 420 30.488 -25.172 79.819 1.00100.60 C
ANISOU 2754 CB GLU A 420 11087 12846 14292 2750 -1670 1432 C
ATOM 2755 CG GLU A 420 31.848 -24.505 79.742 1.00113.71 C
ANISOU 2755 CG GLU A 420 12276 14902 16027 2807 -1842 1287 C
ATOM 2756 CD GLU A 420 32.367 -24.114 81.115 1.00121.97 C
ANISOU 2756 CD GLU A 420 13155 16312 16876 2941 -2104 1247 C
ATOM 2757 OE1 GLU A 420 31.535 -23.915 82.028 1.00122.22 O
ANISOU 2757 OE1 GLU A 420 13398 16281 16758 2856 -2155 1283 O
ATOM 2758 OE2 GLU A 420 33.601 -24.018 81.287 1.00126.11 O
ANISOU 2758 OE2 GLU A 420 13329 17205 17384 3133 -2259 1171 O
ATOM 2759 N GLY A 421 31.536 -27.472 77.887 1.00 86.82 N
ANISOU 2759 N GLY A 421 9502 10768 12716 3259 -1325 1640 N
ATOM 2760 CA GLY A 421 32.563 -28.060 77.047 1.00 88.79 C
ANISOU 2760 CA GLY A 421 9600 11064 13074 3499 -1260 1658 C
ATOM 2761 C GLY A 421 32.046 -28.435 75.675 1.00 84.56 C
ANISOU 2761 C GLY A 421 9223 10193 12713 3320 -992 1651 C
ATOM 2762 O GLY A 421 32.781 -28.358 74.686 1.00 90.95 O
ANISOU 2762 O GLY A 421 9800 11069 13687 3329 -938 1579 O
ATOM 2763 N TRP A 422 30.774 -28.828 75.589 1.00 76.71 N
ANISOU 2763 N TRP A 422 8611 8857 11677 3141 -820 1710 N
ATOM 2764 CA TRP A 422 30.165 -29.075 74.287 1.00 78.82 C
ANISOU 2764 CA TRP A 422 9010 8845 12094 2919 -576 1669 C
ATOM 2765 C TRP A 422 30.098 -27.790 73.469 1.00 86.15 C
ANISOU 2765 C TRP A 422 9633 9898 13202 2568 -607 1485 C
ATOM 2766 O TRP A 422 30.394 -27.789 72.267 1.00 93.58 O
ANISOU 2766 O TRP A 422 10468 10784 14303 2499 -482 1424 O
ATOM 2767 CB TRP A 422 28.772 -29.677 74.486 1.00 80.74 C
ANISOU 2767 CB TRP A 422 9691 8758 12230 2768 -399 1735 C
ATOM 2768 CG TRP A 422 28.002 -30.010 73.231 1.00 81.02 C
ANISOU 2768 CG TRP A 422 9883 8522 12378 2526 -144 1678 C
ATOM 2769 CD1 TRP A 422 28.443 -29.937 71.939 1.00 80.31 C
ANISOU 2769 CD1 TRP A 422 9628 8422 12466 2469 -47 1601 C
ATOM 2770 CD2 TRP A 422 26.648 -30.474 73.163 1.00 81.96 C
ANISOU 2770 CD2 TRP A 422 10349 8370 12423 2302 47 1678 C
ATOM 2771 NE1 TRP A 422 27.447 -30.321 71.074 1.00 79.70 N
ANISOU 2771 NE1 TRP A 422 9770 8092 12421 2233 181 1554 N
ATOM 2772 CE2 TRP A 422 26.335 -30.658 71.801 1.00 80.18 C
ANISOU 2772 CE2 TRP A 422 10135 8000 12330 2120 243 1591 C
ATOM 2773 CE3 TRP A 422 25.670 -30.753 74.124 1.00 81.02 C
ANISOU 2773 CE3 TRP A 422 10521 8131 12131 2228 79 1730 C
ATOM 2774 CZ2 TRP A 422 25.087 -31.107 71.375 1.00 79.53 C
ANISOU 2774 CZ2 TRP A 422 10322 7689 12206 1863 458 1540 C
ATOM 2775 CZ3 TRP A 422 24.431 -31.198 73.699 1.00 83.96 C
ANISOU 2775 CZ3 TRP A 422 11164 8264 12473 1962 306 1680 C
ATOM 2776 CH2 TRP A 422 24.150 -31.371 72.337 1.00 83.25 C
ANISOU 2776 CH2 TRP A 422 11057 8063 12513 1780 488 1578 C
ATOM 2777 N ALA A 423 29.736 -26.678 74.112 1.00 82.55 N
ANISOU 2777 N ALA A 423 9051 9603 12712 2356 -761 1397 N
ATOM 2778 CA ALA A 423 29.714 -25.399 73.412 1.00 74.62 C
ANISOU 2778 CA ALA A 423 7789 8704 11859 2045 -778 1231 C
ATOM 2779 C ALA A 423 31.117 -24.966 72.999 1.00 76.23 C
ANISOU 2779 C ALA A 423 7607 9167 12190 2132 -858 1141 C
ATOM 2780 O ALA A 423 31.299 -24.376 71.927 1.00 78.09 O
ANISOU 2780 O ALA A 423 7687 9396 12587 1945 -765 1035 O
ATOM 2781 CB ALA A 423 29.059 -24.334 74.290 1.00 75.48 C
ANISOU 2781 CB ALA A 423 7878 8916 11886 1828 -913 1161 C
ATOM 2782 N ARG A 424 32.124 -25.258 73.828 1.00 74.53 N
ANISOU 2782 N ARG A 424 7228 9198 11891 2420 -1022 1176 N
ATOM 2783 CA ARG A 424 33.494 -24.945 73.429 1.00 81.37 C
ANISOU 2783 CA ARG A 424 7700 10349 12869 2513 -1089 1073 C
ATOM 2784 C ARG A 424 33.934 -25.798 72.244 1.00 91.41 C
ANISOU 2784 C ARG A 424 8995 11473 14262 2660 -902 1121 C
ATOM 2785 O ARG A 424 34.643 -25.314 71.353 1.00 95.76 O
ANISOU 2785 O ARG A 424 9274 12135 14976 2560 -852 1002 O
ATOM 2786 CB ARG A 424 34.454 -25.139 74.601 1.00 85.94 C
ANISOU 2786 CB ARG A 424 8081 11272 13300 2824 -1317 1093 C
ATOM 2787 CG ARG A 424 34.309 -24.127 75.722 1.00 92.31 C
ANISOU 2787 CG ARG A 424 8763 12311 14001 2661 -1520 993 C
ATOM 2788 CD ARG A 424 35.595 -24.038 76.522 1.00107.37 C
ANISOU 2788 CD ARG A 424 10306 14676 15814 2907 -1747 925 C
ATOM 2789 NE ARG A 424 35.359 -23.664 77.913 1.00116.90 N
ANISOU 2789 NE ARG A 424 11529 16065 16821 2921 -1951 917 N
ATOM 2790 CZ ARG A 424 36.325 -23.425 78.796 1.00125.67 C
ANISOU 2790 CZ ARG A 424 12322 17620 17809 3089 -2180 830 C
ATOM 2791 NH1 ARG A 424 37.596 -23.512 78.432 1.00128.46 N
ANISOU 2791 NH1 ARG A 424 12294 18294 18222 3257 -2233 735 N
ATOM 2792 NH2 ARG A 424 36.020 -23.093 80.042 1.00127.53 N
ANISOU 2792 NH2 ARG A 424 12604 18002 17851 3088 -2355 824 N
ATOM 2793 N SER A 425 33.518 -27.067 72.213 1.00 95.36 N
ANISOU 2793 N SER A 425 9838 11711 14684 2885 -778 1288 N
ATOM 2794 CA SER A 425 33.833 -27.911 71.066 1.00102.97 C
ANISOU 2794 CA SER A 425 10871 12495 15756 3007 -574 1330 C
ATOM 2795 C SER A 425 33.122 -27.423 69.815 1.00103.35 C
ANISOU 2795 C SER A 425 10968 12341 15958 2646 -394 1236 C
ATOM 2796 O SER A 425 33.651 -27.560 68.708 1.00105.27 O
ANISOU 2796 O SER A 425 11098 12558 16342 2649 -266 1190 O
ATOM 2797 CB SER A 425 33.457 -29.365 71.353 1.00112.56 C
ANISOU 2797 CB SER A 425 12497 13433 16837 3298 -449 1521 C
ATOM 2798 OG SER A 425 32.063 -29.577 71.197 1.00113.80 O
ANISOU 2798 OG SER A 425 13019 13263 16957 3051 -295 1551 O
ATOM 2799 N LEU A 426 31.925 -26.855 69.971 1.00 96.04 N
ANISOU 2799 N LEU A 426 10209 11289 14993 2351 -381 1206 N
ATOM 2800 CA LEU A 426 31.238 -26.271 68.824 1.00 83.39 C
ANISOU 2800 CA LEU A 426 8630 9548 13507 2031 -233 1112 C
ATOM 2801 C LEU A 426 31.949 -25.017 68.331 1.00 85.09 C
ANISOU 2801 C LEU A 426 8490 9980 13861 1855 -289 962 C
ATOM 2802 O LEU A 426 32.084 -24.812 67.119 1.00 87.29 O
ANISOU 2802 O LEU A 426 8704 10194 14270 1738 -144 898 O
ATOM 2803 CB LEU A 426 29.784 -25.964 69.180 1.00 73.89 C
ANISOU 2803 CB LEU A 426 7674 8198 12204 1795 -215 1113 C
ATOM 2804 CG LEU A 426 28.758 -27.049 68.846 1.00 75.83 C
ANISOU 2804 CG LEU A 426 8287 8145 12380 1784 -23 1188 C
ATOM 2805 CD1 LEU A 426 27.371 -26.612 69.280 1.00 75.31 C
ANISOU 2805 CD1 LEU A 426 8396 8009 12208 1541 -27 1161 C
ATOM 2806 CD2 LEU A 426 28.781 -27.363 67.358 1.00 78.65 C
ANISOU 2806 CD2 LEU A 426 8655 8369 12861 1712 180 1140 C
ATOM 2807 N GLU A 427 32.421 -24.171 69.253 1.00 89.00 N
ANISOU 2807 N GLU A 427 8762 10731 14321 1825 -483 895 N
ATOM 2808 CA GLU A 427 33.174 -22.985 68.851 1.00 90.90 C
ANISOU 2808 CA GLU A 427 8674 11176 14687 1638 -512 734 C
ATOM 2809 C GLU A 427 34.495 -23.345 68.183 1.00 93.71 C
ANISOU 2809 C GLU A 427 8765 11678 15162 1803 -467 693 C
ATOM 2810 O GLU A 427 34.929 -22.647 67.260 1.00 96.70 O
ANISOU 2810 O GLU A 427 8966 12095 15681 1620 -367 575 O
ATOM 2811 CB GLU A 427 33.433 -22.080 70.055 1.00 93.54 C
ANISOU 2811 CB GLU A 427 8831 11766 14944 1563 -720 651 C
ATOM 2812 CG GLU A 427 34.220 -20.822 69.708 1.00 93.22 C
ANISOU 2812 CG GLU A 427 8466 11927 15024 1329 -724 459 C
ATOM 2813 CD GLU A 427 34.593 -19.992 70.917 1.00 92.98 C
ANISOU 2813 CD GLU A 427 8242 12175 14913 1251 -924 349 C
ATOM 2814 OE1 GLU A 427 34.178 -20.350 72.037 1.00 93.42 O
ANISOU 2814 OE1 GLU A 427 8422 12265 14809 1384 -1071 433 O
ATOM 2815 OE2 GLU A 427 35.308 -18.980 70.746 1.00 91.31 O
ANISOU 2815 OE2 GLU A 427 7761 12145 14788 1043 -919 170 O
ATOM 2816 N GLU A 428 35.146 -24.425 68.623 1.00 97.33 N
ANISOU 2816 N GLU A 428 9205 12217 15557 2159 -525 791 N
ATOM 2817 CA GLU A 428 36.361 -24.871 67.949 1.00106.31 C
ANISOU 2817 CA GLU A 428 10100 13493 16799 2354 -469 759 C
ATOM 2818 C GLU A 428 36.046 -25.499 66.597 1.00106.19 C
ANISOU 2818 C GLU A 428 10275 13186 16888 2336 -223 806 C
ATOM 2819 O GLU A 428 36.799 -25.322 65.634 1.00104.03 O
ANISOU 2819 O GLU A 428 9793 12980 16755 2301 -118 720 O
ATOM 2820 CB GLU A 428 37.118 -25.858 68.836 1.00116.59 C
ANISOU 2820 CB GLU A 428 11347 14973 17977 2791 -602 863 C
ATOM 2821 CG GLU A 428 38.378 -26.420 68.202 1.00130.21 C
ANISOU 2821 CG GLU A 428 12821 16864 19790 3054 -547 841 C
ATOM 2822 CD GLU A 428 38.738 -27.786 68.750 1.00143.57 C
ANISOU 2822 CD GLU A 428 14659 18548 21344 3549 -578 1017 C
ATOM 2823 OE1 GLU A 428 37.972 -28.306 69.593 1.00147.84 O
ANISOU 2823 OE1 GLU A 428 15525 18925 21723 3663 -623 1160 O
ATOM 2824 OE2 GLU A 428 39.779 -28.338 68.332 1.00146.85 O
ANISOU 2824 OE2 GLU A 428 14880 19113 21805 3831 -541 1015 O
ATOM 2825 N LYS A 429 34.941 -26.243 66.513 1.00107.62 N
ANISOU 2825 N LYS A 429 10847 13051 16994 2347 -119 927 N
ATOM 2826 CA LYS A 429 34.536 -26.896 65.275 1.00104.31 C
ANISOU 2826 CA LYS A 429 10632 12355 16647 2313 118 958 C
ATOM 2827 C LYS A 429 34.061 -25.908 64.217 1.00101.53 C
ANISOU 2827 C LYS A 429 10238 11937 16401 1959 229 841 C
ATOM 2828 O LYS A 429 34.115 -26.225 63.023 1.00107.07 O
ANISOU 2828 O LYS A 429 10982 12508 17192 1929 413 823 O
ATOM 2829 CB LYS A 429 33.426 -27.908 65.570 1.00107.16 C
ANISOU 2829 CB LYS A 429 11418 12420 16877 2376 203 1088 C
ATOM 2830 CG LYS A 429 33.705 -29.325 65.084 1.00116.37 C
ANISOU 2830 CG LYS A 429 12786 13390 18041 2648 376 1187 C
ATOM 2831 CD LYS A 429 33.129 -29.564 63.694 1.00116.69 C
ANISOU 2831 CD LYS A 429 12979 13194 18165 2454 615 1138 C
ATOM 2832 CE LYS A 429 33.165 -31.038 63.324 1.00111.85 C
ANISOU 2832 CE LYS A 429 12653 12325 17520 2686 813 1233 C
ATOM 2833 NZ LYS A 429 32.468 -31.305 62.038 1.00 99.22 N
ANISOU 2833 NZ LYS A 429 11225 10500 15973 2467 1045 1167 N
ATOM 2834 N HIS A 430 33.591 -24.729 64.622 1.00 96.18 N
ANISOU 2834 N HIS A 430 9499 11341 15703 1709 133 767 N
ATOM 2835 CA HIS A 430 33.010 -23.768 63.694 1.00 90.10 C
ANISOU 2835 CA HIS A 430 8749 10487 14997 1405 245 679 C
ATOM 2836 C HIS A 430 33.426 -22.365 64.097 1.00 83.40 C
ANISOU 2836 C HIS A 430 7660 9843 14186 1214 140 559 C
ATOM 2837 O HIS A 430 33.271 -21.979 65.258 1.00 82.26 O
ANISOU 2837 O HIS A 430 7491 9810 13953 1200 -28 556 O
ATOM 2838 CB HIS A 430 31.481 -23.876 63.677 1.00 86.87 C
ANISOU 2838 CB HIS A 430 8662 9866 14479 1272 297 728 C
ATOM 2839 CG HIS A 430 30.977 -25.273 63.505 1.00 87.45 C
ANISOU 2839 CG HIS A 430 9002 9736 14490 1422 403 827 C
ATOM 2840 ND1 HIS A 430 31.371 -26.081 62.461 1.00 89.29 N
ANISOU 2840 ND1 HIS A 430 9269 9859 14797 1519 574 836 N
ATOM 2841 CD2 HIS A 430 30.114 -26.008 64.245 1.00 88.67 C
ANISOU 2841 CD2 HIS A 430 9417 9763 14509 1474 386 910 C
ATOM 2842 CE1 HIS A 430 30.771 -27.253 62.564 1.00 89.84 C
ANISOU 2842 CE1 HIS A 430 9620 9734 14782 1619 663 917 C
ATOM 2843 NE2 HIS A 430 30.002 -27.235 63.637 1.00 91.76 N
ANISOU 2843 NE2 HIS A 430 10007 9960 14897 1588 558 962 N
ATOM 2844 N GLY A 431 33.928 -21.594 63.134 1.00 81.07 N
ANISOU 2844 N GLY A 431 7210 9579 14012 1051 259 454 N
ATOM 2845 CA GLY A 431 34.384 -20.255 63.449 1.00 89.54 C
ANISOU 2845 CA GLY A 431 8076 10819 15125 841 205 321 C
ATOM 2846 C GLY A 431 33.291 -19.221 63.605 1.00 91.51 C
ANISOU 2846 C GLY A 431 8508 10956 15304 605 212 302 C
ATOM 2847 O GLY A 431 33.565 -18.125 64.103 1.00 89.82 O
ANISOU 2847 O GLY A 431 8172 10860 15097 433 158 197 O
ATOM 2848 N ASN A 432 32.063 -19.542 63.192 1.00 88.38 N
ANISOU 2848 N ASN A 432 8400 10349 14833 595 284 388 N
ATOM 2849 CA ASN A 432 30.938 -18.631 63.353 1.00 82.08 C
ANISOU 2849 CA ASN A 432 7781 9463 13945 418 286 379 C
ATOM 2850 C ASN A 432 30.305 -18.701 64.738 1.00 86.45 C
ANISOU 2850 C ASN A 432 8420 10060 14369 452 104 422 C
ATOM 2851 O ASN A 432 29.424 -17.888 65.036 1.00 93.32 O
ANISOU 2851 O ASN A 432 9415 10884 15157 317 89 407 O
ATOM 2852 CB ASN A 432 29.876 -18.914 62.285 1.00 75.83 C
ANISOU 2852 CB ASN A 432 7224 8482 13107 395 437 431 C
ATOM 2853 CG ASN A 432 29.306 -20.312 62.384 1.00 72.93 C
ANISOU 2853 CG ASN A 432 7013 8027 12672 552 428 525 C
ATOM 2854 OD1 ASN A 432 29.873 -21.181 63.047 1.00 83.47 O
ANISOU 2854 OD1 ASN A 432 8293 9409 14014 718 344 573 O
ATOM 2855 ND2 ASN A 432 28.182 -20.541 61.714 1.00 61.34 N
ANISOU 2855 ND2 ASN A 432 5748 6434 11124 503 529 546 N
ATOM 2856 N VAL A 433 30.706 -19.652 65.572 1.00 83.70 N
ANISOU 2856 N VAL A 433 8024 9791 13985 645 -22 483 N
ATOM 2857 CA VAL A 433 30.232 -19.732 66.948 1.00 75.06 C
ANISOU 2857 CA VAL A 433 7006 8754 12760 691 -194 526 C
ATOM 2858 C VAL A 433 31.233 -19.032 67.856 1.00 71.90 C
ANISOU 2858 C VAL A 433 6342 8600 12376 668 -347 431 C
ATOM 2859 O VAL A 433 32.451 -19.163 67.682 1.00 73.60 O
ANISOU 2859 O VAL A 433 6305 8977 12681 746 -361 375 O
ATOM 2860 CB VAL A 433 30.018 -21.200 67.371 1.00 71.84 C
ANISOU 2860 CB VAL A 433 6750 8275 12273 930 -225 657 C
ATOM 2861 CG1 VAL A 433 29.525 -21.282 68.808 1.00 68.01 C
ANISOU 2861 CG1 VAL A 433 6362 7841 11636 980 -391 707 C
ATOM 2862 CG2 VAL A 433 29.039 -21.893 66.428 1.00 64.18 C
ANISOU 2862 CG2 VAL A 433 6027 7073 11285 908 -51 712 C
ATOM 2863 N LYS A 434 30.719 -18.271 68.820 1.00 69.75 N
ANISOU 2863 N LYS A 434 6116 8377 12008 552 -459 397 N
ATOM 2864 CA LYS A 434 31.538 -17.652 69.857 1.00 78.39 C
ANISOU 2864 CA LYS A 434 6982 9723 13082 517 -621 295 C
ATOM 2865 C LYS A 434 30.867 -17.889 71.200 1.00 78.30 C
ANISOU 2865 C LYS A 434 7107 9742 12900 595 -788 363 C
ATOM 2866 O LYS A 434 29.735 -17.443 71.421 1.00 86.75 O
ANISOU 2866 O LYS A 434 8391 10677 13893 473 -768 384 O
ATOM 2867 CB LYS A 434 31.733 -16.152 69.607 1.00 88.82 C
ANISOU 2867 CB LYS A 434 8205 11074 14468 225 -550 133 C
ATOM 2868 CG LYS A 434 32.690 -15.478 70.586 1.00 98.01 C
ANISOU 2868 CG LYS A 434 9098 12522 15618 142 -694 -18 C
ATOM 2869 CD LYS A 434 34.109 -16.011 70.445 1.00102.25 C
ANISOU 2869 CD LYS A 434 9304 13309 16236 277 -740 -81 C
ATOM 2870 CE LYS A 434 35.039 -15.378 71.470 1.00 98.15 C
ANISOU 2870 CE LYS A 434 8484 13132 15678 192 -899 -257 C
ATOM 2871 NZ LYS A 434 36.448 -15.839 71.326 1.00 96.06 N
ANISOU 2871 NZ LYS A 434 7850 13170 15480 327 -947 -343 N
ATOM 2872 N VAL A 435 31.558 -18.598 72.086 1.00 77.82 N
ANISOU 2872 N VAL A 435 6928 9870 12770 816 -948 401 N
ATOM 2873 CA VAL A 435 31.053 -18.912 73.417 1.00 78.13 C
ANISOU 2873 CA VAL A 435 7097 9958 12631 925 -1109 475 C
ATOM 2874 C VAL A 435 31.742 -18.009 74.429 1.00 79.86 C
ANISOU 2874 C VAL A 435 7075 10470 12799 837 -1284 332 C
ATOM 2875 O VAL A 435 32.945 -17.734 74.321 1.00 89.85 O
ANISOU 2875 O VAL A 435 8023 11978 14137 837 -1328 210 O
ATOM 2876 CB VAL A 435 31.271 -20.402 73.749 1.00 77.00 C
ANISOU 2876 CB VAL A 435 7047 9804 12406 1270 -1154 637 C
ATOM 2877 CG1 VAL A 435 30.670 -20.752 75.102 1.00 67.43 C
ANISOU 2877 CG1 VAL A 435 6020 8609 10994 1382 -1293 729 C
ATOM 2878 CG2 VAL A 435 30.671 -21.274 72.655 1.00 73.44 C
ANISOU 2878 CG2 VAL A 435 6824 9063 12018 1317 -952 744 C
ATOM 2879 N ILE A 436 30.979 -17.542 75.415 1.00 74.75 N
ANISOU 2879 N ILE A 436 6566 9817 12019 748 -1376 330 N
ATOM 2880 CA ILE A 436 31.476 -16.657 76.461 1.00 89.12 C
ANISOU 2880 CA ILE A 436 8196 11901 13764 639 -1538 184 C
ATOM 2881 C ILE A 436 31.026 -17.213 77.804 1.00 92.49 C
ANISOU 2881 C ILE A 436 8766 12394 13982 819 -1709 288 C
ATOM 2882 O ILE A 436 29.897 -17.698 77.936 1.00 86.72 O
ANISOU 2882 O ILE A 436 8346 11431 13174 862 -1657 428 O
ATOM 2883 CB ILE A 436 30.970 -15.210 76.267 1.00 92.49 C
ANISOU 2883 CB ILE A 436 8668 12234 14242 288 -1443 41 C
ATOM 2884 CG1 ILE A 436 31.356 -14.689 74.882 1.00 87.98 C
ANISOU 2884 CG1 ILE A 436 8008 11558 13861 124 -1242 -41 C
ATOM 2885 CG2 ILE A 436 31.531 -14.286 77.338 1.00 92.83 C
ANISOU 2885 CG2 ILE A 436 8517 12546 14208 143 -1590 -138 C
ATOM 2886 CD1 ILE A 436 30.819 -13.309 74.579 1.00 83.71 C
ANISOU 2886 CD1 ILE A 436 7574 10874 13359 -184 -1107 -155 C
ATOM 2887 N THR A 437 31.909 -17.144 78.802 1.00101.53 N
ANISOU 2887 N THR A 437 9680 13873 15023 920 -1909 211 N
ATOM 2888 CA THR A 437 31.627 -17.712 80.113 1.00108.90 C
ANISOU 2888 CA THR A 437 10740 14904 15735 1131 -2082 316 C
ATOM 2889 C THR A 437 31.854 -16.756 81.277 1.00114.18 C
ANISOU 2889 C THR A 437 11261 15844 16279 989 -2256 155 C
ATOM 2890 O THR A 437 31.437 -17.074 82.396 1.00114.20 O
ANISOU 2890 O THR A 437 11409 15899 16083 1122 -2387 237 O
ATOM 2891 CB THR A 437 32.470 -18.977 80.341 1.00114.74 C
ANISOU 2891 CB THR A 437 11394 15807 16395 1539 -2180 441 C
ATOM 2892 OG1 THR A 437 33.835 -18.715 79.987 1.00121.70 O
ANISOU 2892 OG1 THR A 437 11868 17005 17369 1562 -2237 288 O
ATOM 2893 CG2 THR A 437 31.943 -20.122 79.491 1.00112.43 C
ANISOU 2893 CG2 THR A 437 11375 15182 16162 1708 -2002 640 C
ATOM 2894 N GLU A 438 32.494 -15.612 81.060 1.00121.98 N
ANISOU 2894 N GLU A 438 11982 16998 17366 714 -2247 -77 N
ATOM 2895 CA GLU A 438 32.739 -14.664 82.135 1.00131.33 C
ANISOU 2895 CA GLU A 438 13024 18442 18433 541 -2393 -263 C
ATOM 2896 C GLU A 438 31.461 -13.916 82.502 1.00128.64 C
ANISOU 2896 C GLU A 438 12987 17847 18042 316 -2324 -258 C
ATOM 2897 O GLU A 438 30.545 -13.764 81.687 1.00118.82 O
ANISOU 2897 O GLU A 438 11983 16262 16902 205 -2135 -181 O
ATOM 2898 CB GLU A 438 33.827 -13.667 81.733 1.00140.26 C
ANISOU 2898 CB GLU A 438 13790 19811 19693 276 -2363 -538 C
ATOM 2899 CG GLU A 438 33.301 -12.415 81.055 1.00144.56 C
ANISOU 2899 CG GLU A 438 14453 20095 20380 -122 -2147 -665 C
ATOM 2900 CD GLU A 438 34.393 -11.598 80.396 1.00150.39 C
ANISOU 2900 CD GLU A 438 14873 20996 21272 -380 -2048 -913 C
ATOM 2901 OE1 GLU A 438 35.162 -12.171 79.594 1.00153.34 O
ANISOU 2901 OE1 GLU A 438 15053 21448 21759 -256 -2005 -897 O
ATOM 2902 OE2 GLU A 438 34.486 -10.386 80.684 1.00151.57 O
ANISOU 2902 OE2 GLU A 438 14976 21188 21425 -714 -1995 -1133 O
ATOM 2903 N MET A 439 31.394 -13.473 83.756 1.00134.25 N
ANISOU 2903 N MET A 439 13684 18749 18576 270 -2483 -341 N
ATOM 2904 CA MET A 439 30.318 -12.582 84.167 1.00129.51 C
ANISOU 2904 CA MET A 439 13327 17955 17926 33 -2419 -381 C
ATOM 2905 C MET A 439 30.441 -11.256 83.426 1.00129.77 C
ANISOU 2905 C MET A 439 13293 17889 18125 -332 -2244 -584 C
ATOM 2906 O MET A 439 31.538 -10.707 83.280 1.00139.17 O
ANISOU 2906 O MET A 439 14180 19311 19385 -481 -2256 -790 O
ATOM 2907 CB MET A 439 30.365 -12.359 85.680 1.00129.03 C
ANISOU 2907 CB MET A 439 13238 18153 17636 55 -2629 -452 C
ATOM 2908 CG MET A 439 29.067 -11.836 86.279 1.00126.63 C
ANISOU 2908 CG MET A 439 13253 17629 17231 -76 -2583 -418 C
ATOM 2909 SD MET A 439 27.670 -12.931 85.956 1.00123.28 S
ANISOU 2909 SD MET A 439 13226 16834 16782 132 -2472 -114 S
ATOM 2910 CE MET A 439 28.319 -14.491 86.552 1.00128.03 C
ANISOU 2910 CE MET A 439 13779 17634 17232 556 -2650 67 C
ATOM 2911 N LEU A 440 29.310 -10.734 82.960 1.00116.70 N
ANISOU 2911 N LEU A 440 11926 15896 16520 -474 -2068 -532 N
ATOM 2912 CA LEU A 440 29.300 -9.563 82.096 1.00 95.97 C
ANISOU 2912 CA LEU A 440 9318 13102 14046 -769 -1857 -675 C
ATOM 2913 C LEU A 440 28.438 -8.452 82.680 1.00 89.88 C
ANISOU 2913 C LEU A 440 8765 12196 13190 -979 -1796 -759 C
ATOM 2914 O LEU A 440 27.416 -8.706 83.325 1.00 87.82 O
ANISOU 2914 O LEU A 440 8728 11844 12797 -879 -1850 -639 O
ATOM 2915 CB LEU A 440 28.793 -9.911 80.692 1.00 83.37 C
ANISOU 2915 CB LEU A 440 7869 11209 12599 -713 -1658 -531 C
ATOM 2916 CG LEU A 440 29.822 -10.547 79.757 1.00 79.10 C
ANISOU 2916 CG LEU A 440 7096 10756 12204 -619 -1626 -523 C
ATOM 2917 CD1 LEU A 440 29.290 -10.612 78.331 1.00 66.22 C
ANISOU 2917 CD1 LEU A 440 5624 8822 10714 -628 -1402 -423 C
ATOM 2918 CD2 LEU A 440 31.138 -9.782 79.813 1.00 86.65 C
ANISOU 2918 CD2 LEU A 440 7727 11969 13228 -825 -1636 -774 C
ATOM 2919 N SER A 441 28.869 -7.217 82.434 1.00 87.87 N
ANISOU 2919 N SER A 441 8453 11922 13013 -1276 -1663 -972 N
ATOM 2920 CA SER A 441 28.103 -6.043 82.821 1.00 82.40 C
ANISOU 2920 CA SER A 441 7994 11056 12259 -1486 -1553 -1064 C
ATOM 2921 C SER A 441 26.801 -5.970 82.036 1.00 76.60 C
ANISOU 2921 C SER A 441 7587 9964 11555 -1412 -1375 -890 C
ATOM 2922 O SER A 441 26.728 -6.357 80.866 1.00 78.03 O
ANISOU 2922 O SER A 441 7792 9999 11858 -1329 -1254 -782 O
ATOM 2923 CB SER A 441 28.918 -4.768 82.597 1.00 79.91 C
ANISOU 2923 CB SER A 441 7573 10759 12028 -1830 -1400 -1335 C
ATOM 2924 OG SER A 441 29.329 -4.646 81.243 1.00 77.78 O
ANISOU 2924 OG SER A 441 7269 10342 11943 -1890 -1198 -1333 O
ATOM 2925 N ARG A 442 25.762 -5.464 82.703 1.00 74.80 N
ANISOU 2925 N ARG A 442 7602 9620 11200 -1436 -1363 -872 N
ATOM 2926 CA ARG A 442 24.460 -5.346 82.057 1.00 75.70 C
ANISOU 2926 CA ARG A 442 8005 9448 11309 -1350 -1209 -725 C
ATOM 2927 C ARG A 442 24.495 -4.366 80.891 1.00 84.50 C
ANISOU 2927 C ARG A 442 9226 10332 12548 -1492 -944 -786 C
ATOM 2928 O ARG A 442 23.702 -4.496 79.953 1.00 87.43 O
ANISOU 2928 O ARG A 442 9759 10509 12950 -1373 -814 -650 O
ATOM 2929 CB ARG A 442 23.402 -4.934 83.080 1.00 78.42 C
ANISOU 2929 CB ARG A 442 8564 9749 11482 -1348 -1247 -718 C
ATOM 2930 CG ARG A 442 23.693 -3.627 83.794 1.00 96.33 C
ANISOU 2930 CG ARG A 442 10873 12029 13700 -1597 -1197 -935 C
ATOM 2931 CD ARG A 442 22.547 -3.242 84.716 1.00104.64 C
ANISOU 2931 CD ARG A 442 12161 13016 14583 -1570 -1215 -913 C
ATOM 2932 NE ARG A 442 22.862 -2.053 85.500 1.00111.04 N
ANISOU 2932 NE ARG A 442 13015 13844 15330 -1811 -1174 -1132 N
ATOM 2933 CZ ARG A 442 22.052 -1.520 86.408 1.00115.59 C
ANISOU 2933 CZ ARG A 442 13785 14377 15757 -1833 -1178 -1163 C
ATOM 2934 NH1 ARG A 442 22.427 -0.437 87.077 1.00120.29 N
ANISOU 2934 NH1 ARG A 442 14421 14983 16301 -2074 -1123 -1382 N
ATOM 2935 NH2 ARG A 442 20.870 -2.069 86.647 1.00114.82 N
ANISOU 2935 NH2 ARG A 442 13838 14230 15559 -1629 -1223 -990 N
ATOM 2936 N GLU A 443 25.397 -3.378 80.928 1.00 88.55 N
ANISOU 2936 N GLU A 443 9658 10868 13120 -1747 -850 -996 N
ATOM 2937 CA GLU A 443 25.557 -2.486 79.782 1.00 87.67 C
ANISOU 2937 CA GLU A 443 9664 10521 13125 -1885 -571 -1052 C
ATOM 2938 C GLU A 443 26.098 -3.235 78.568 1.00 87.69 C
ANISOU 2938 C GLU A 443 9519 10522 13277 -1788 -525 -961 C
ATOM 2939 O GLU A 443 25.704 -2.956 77.427 1.00 88.76 O
ANISOU 2939 O GLU A 443 9822 10428 13475 -1750 -320 -882 O
ATOM 2940 CB GLU A 443 26.474 -1.317 80.150 1.00 89.16 C
ANISOU 2940 CB GLU A 443 9797 10739 13340 -2220 -461 -1322 C
ATOM 2941 CG GLU A 443 26.002 -0.490 81.341 1.00 94.88 C
ANISOU 2941 CG GLU A 443 10681 11454 13917 -2344 -483 -1439 C
ATOM 2942 CD GLU A 443 26.390 -1.101 82.677 1.00 98.91 C
ANISOU 2942 CD GLU A 443 10955 12308 14318 -2327 -783 -1504 C
ATOM 2943 OE1 GLU A 443 27.423 -1.800 82.735 1.00100.69 O
ANISOU 2943 OE1 GLU A 443 10853 12808 14595 -2319 -935 -1555 O
ATOM 2944 OE2 GLU A 443 25.660 -0.886 83.668 1.00 97.82 O
ANISOU 2944 OE2 GLU A 443 10963 12175 14030 -2301 -865 -1501 O
ATOM 2945 N PHE A 444 26.944 -4.218 78.822 1.00 85.92 N
ANISOU 2945 N PHE A 444 8992 10559 13096 -1723 -712 -967 N
ATOM 2946 CA PHE A 444 27.394 -5.027 77.676 1.00 81.62 C
ANISOU 2946 CA PHE A 444 8313 10018 12681 -1595 -682 -865 C
ATOM 2947 C PHE A 444 26.171 -5.763 77.134 1.00 76.83 C
ANISOU 2947 C PHE A 444 7891 9261 12041 -1336 -681 -626 C
ATOM 2948 O PHE A 444 25.860 -5.663 75.953 1.00 80.85 O
ANISOU 2948 O PHE A 444 8450 9628 12641 -1273 -537 -543 O
ATOM 2949 CB PHE A 444 28.434 -6.031 78.157 1.00 84.76 C
ANISOU 2949 CB PHE A 444 8358 10745 13101 -1532 -895 -914 C
ATOM 2950 CG PHE A 444 29.316 -6.558 77.062 1.00 91.21 C
ANISOU 2950 CG PHE A 444 8979 11600 14076 -1487 -826 -898 C
ATOM 2951 CD1 PHE A 444 28.921 -6.462 75.747 1.00 93.97 C
ANISOU 2951 CD1 PHE A 444 9477 11695 14533 -1499 -595 -830 C
ATOM 2952 CD2 PHE A 444 30.517 -7.167 77.347 1.00 96.47 C
ANISOU 2952 CD2 PHE A 444 9310 12577 14768 -1410 -994 -952 C
ATOM 2953 CE1 PHE A 444 29.718 -6.948 74.730 1.00 93.22 C
ANISOU 2953 CE1 PHE A 444 9204 11637 14577 -1460 -527 -819 C
ATOM 2954 CE2 PHE A 444 31.310 -7.664 76.330 1.00 99.69 C
ANISOU 2954 CE2 PHE A 444 9531 13031 15317 -1356 -927 -942 C
ATOM 2955 CZ PHE A 444 30.905 -7.557 75.026 1.00 98.68 C
ANISOU 2955 CZ PHE A 444 9558 12630 15305 -1394 -689 -878 C
ATOM 2956 N VAL A 445 25.398 -6.370 78.025 1.00 71.58 N
ANISOU 2956 N VAL A 445 7329 8633 11235 -1201 -828 -529 N
ATOM 2957 CA VAL A 445 24.230 -7.109 77.561 1.00 72.11 C
ANISOU 2957 CA VAL A 445 7568 8575 11255 -997 -811 -337 C
ATOM 2958 C VAL A 445 23.288 -6.196 76.786 1.00 71.82 C
ANISOU 2958 C VAL A 445 7783 8303 11202 -1026 -597 -316 C
ATOM 2959 O VAL A 445 22.638 -6.630 75.827 1.00 77.22 O
ANISOU 2959 O VAL A 445 8557 8884 11900 -894 -511 -196 O
ATOM 2960 CB VAL A 445 23.526 -7.787 78.754 1.00 67.54 C
ANISOU 2960 CB VAL A 445 7045 8096 10519 -876 -997 -259 C
ATOM 2961 CG1 VAL A 445 22.225 -8.438 78.318 1.00 64.92 C
ANISOU 2961 CG1 VAL A 445 6898 7644 10126 -718 -949 -99 C
ATOM 2962 CG2 VAL A 445 24.443 -8.822 79.394 1.00 64.82 C
ANISOU 2962 CG2 VAL A 445 6481 7977 10171 -779 -1196 -243 C
ATOM 2963 N ARG A 446 23.216 -4.916 77.163 1.00 60.79 N
ANISOU 2963 N ARG A 446 6510 6823 9764 -1187 -500 -437 N
ATOM 2964 CA ARG A 446 22.409 -3.970 76.401 1.00 58.61 C
ANISOU 2964 CA ARG A 446 6495 6316 9460 -1180 -277 -414 C
ATOM 2965 C ARG A 446 22.998 -3.749 75.015 1.00 61.98 C
ANISOU 2965 C ARG A 446 6911 6620 10021 -1213 -84 -413 C
ATOM 2966 O ARG A 446 22.265 -3.708 74.019 1.00 57.13 O
ANISOU 2966 O ARG A 446 6451 5868 9385 -1078 49 -305 O
ATOM 2967 CB ARG A 446 22.298 -2.642 77.157 1.00 64.52 C
ANISOU 2967 CB ARG A 446 7406 6978 10132 -1346 -193 -550 C
ATOM 2968 CG ARG A 446 21.223 -1.710 76.612 1.00 69.18 C
ANISOU 2968 CG ARG A 446 8314 7336 10637 -1266 17 -498 C
ATOM 2969 CD ARG A 446 21.713 -0.272 76.467 1.00 77.20 C
ANISOU 2969 CD ARG A 446 9501 8156 11677 -1472 254 -643 C
ATOM 2970 NE ARG A 446 21.550 0.502 77.694 1.00 80.65 N
ANISOU 2970 NE ARG A 446 10040 8591 12013 -1604 230 -768 N
ATOM 2971 CZ ARG A 446 22.555 0.965 78.431 1.00 77.82 C
ANISOU 2971 CZ ARG A 446 9568 8306 11695 -1875 211 -967 C
ATOM 2972 NH1 ARG A 446 22.303 1.663 79.529 1.00 73.07 N
ANISOU 2972 NH1 ARG A 446 9081 7700 10984 -1987 196 -1081 N
ATOM 2973 NH2 ARG A 446 23.810 0.743 78.066 1.00 79.87 N
ANISOU 2973 NH2 ARG A 446 9589 8662 12096 -2039 213 -1067 N
ATOM 2974 N GLU A 447 24.326 -3.638 74.930 1.00 63.87 N
ANISOU 2974 N GLU A 447 6952 6931 10387 -1387 -68 -539 N
ATOM 2975 CA GLU A 447 24.973 -3.511 73.628 1.00 68.76 C
ANISOU 2975 CA GLU A 447 7540 7447 11138 -1430 119 -544 C
ATOM 2976 C GLU A 447 24.739 -4.753 72.777 1.00 71.87 C
ANISOU 2976 C GLU A 447 7853 7880 11575 -1213 63 -381 C
ATOM 2977 O GLU A 447 24.531 -4.656 71.561 1.00 75.71 O
ANISOU 2977 O GLU A 447 8445 8223 12097 -1148 234 -311 O
ATOM 2978 CB GLU A 447 26.471 -3.263 73.814 1.00 78.50 C
ANISOU 2978 CB GLU A 447 8525 8808 12493 -1670 128 -733 C
ATOM 2979 CG GLU A 447 26.954 -1.887 73.377 1.00 95.28 C
ANISOU 2979 CG GLU A 447 10791 10744 14666 -1925 410 -887 C
ATOM 2980 CD GLU A 447 26.817 -1.668 71.882 1.00113.84 C
ANISOU 2980 CD GLU A 447 13308 12867 17078 -1862 660 -794 C
ATOM 2981 OE1 GLU A 447 25.887 -0.942 71.470 1.00120.60 O
ANISOU 2981 OE1 GLU A 447 14493 13485 17842 -1782 832 -715 O
ATOM 2982 OE2 GLU A 447 27.633 -2.231 71.120 1.00118.95 O
ANISOU 2982 OE2 GLU A 447 13758 13585 17852 -1872 685 -797 O
ATOM 2983 N LEU A 448 24.734 -5.931 73.407 1.00 70.51 N
ANISOU 2983 N LEU A 448 7518 7891 11382 -1093 -165 -317 N
ATOM 2984 CA LEU A 448 24.501 -7.163 72.659 1.00 65.98 C
ANISOU 2984 CA LEU A 448 6889 7337 10841 -902 -202 -175 C
ATOM 2985 C LEU A 448 23.068 -7.237 72.146 1.00 64.31 C
ANISOU 2985 C LEU A 448 6908 7006 10522 -753 -133 -52 C
ATOM 2986 O LEU A 448 22.839 -7.589 70.984 1.00 62.47 O
ANISOU 2986 O LEU A 448 6711 6702 10322 -661 -26 23 O
ATOM 2987 CB LEU A 448 24.823 -8.373 73.534 1.00 60.98 C
ANISOU 2987 CB LEU A 448 6077 6900 10192 -802 -435 -135 C
ATOM 2988 CG LEU A 448 26.309 -8.583 73.817 1.00 62.72 C
ANISOU 2988 CG LEU A 448 6013 7301 10517 -877 -518 -241 C
ATOM 2989 CD1 LEU A 448 26.507 -9.589 74.937 1.00 71.51 C
ANISOU 2989 CD1 LEU A 448 7000 8615 11557 -745 -758 -198 C
ATOM 2990 CD2 LEU A 448 27.017 -9.036 72.553 1.00 60.16 C
ANISOU 2990 CD2 LEU A 448 5572 6947 10338 -842 -404 -219 C
ATOM 2991 N TYR A 449 22.093 -6.896 72.993 1.00 63.47 N
ANISOU 2991 N TYR A 449 6945 6899 10274 -728 -192 -41 N
ATOM 2992 CA TYR A 449 20.707 -6.873 72.543 1.00 52.50 C
ANISOU 2992 CA TYR A 449 5744 5440 8762 -587 -125 50 C
ATOM 2993 C TYR A 449 20.498 -5.837 71.450 1.00 52.72 C
ANISOU 2993 C TYR A 449 5941 5304 8787 -578 102 48 C
ATOM 2994 O TYR A 449 19.660 -6.032 70.563 1.00 53.57 O
ANISOU 2994 O TYR A 449 6141 5386 8828 -430 179 130 O
ATOM 2995 CB TYR A 449 19.773 -6.592 73.719 1.00 64.20 C
ANISOU 2995 CB TYR A 449 7336 6965 10091 -571 -219 43 C
ATOM 2996 CG TYR A 449 19.633 -7.721 74.707 1.00 68.21 C
ANISOU 2996 CG TYR A 449 7744 7619 10553 -530 -419 82 C
ATOM 2997 CD1 TYR A 449 19.899 -9.031 74.344 1.00 69.53 C
ANISOU 2997 CD1 TYR A 449 7794 7846 10780 -451 -481 156 C
ATOM 2998 CD2 TYR A 449 19.222 -7.472 76.009 1.00 75.34 C
ANISOU 2998 CD2 TYR A 449 8701 8583 11343 -563 -528 48 C
ATOM 2999 CE1 TYR A 449 19.764 -10.062 75.253 1.00 74.54 C
ANISOU 2999 CE1 TYR A 449 8387 8580 11356 -399 -634 203 C
ATOM 3000 CE2 TYR A 449 19.083 -8.494 76.922 1.00 68.62 C
ANISOU 3000 CE2 TYR A 449 7793 7850 10432 -516 -693 95 C
ATOM 3001 CZ TYR A 449 19.357 -9.785 76.542 1.00 67.49 C
ANISOU 3001 CZ TYR A 449 7553 7746 10343 -430 -739 176 C
ATOM 3002 OH TYR A 449 19.220 -10.799 77.459 1.00 68.53 O
ANISOU 3002 OH TYR A 449 7675 7964 10400 -370 -875 233 O
ATOM 3003 N GLY A 450 21.247 -4.736 71.494 1.00 59.16 N
ANISOU 3003 N GLY A 450 6806 6014 9659 -735 222 -53 N
ATOM 3004 CA GLY A 450 21.158 -3.725 70.460 1.00 64.81 C
ANISOU 3004 CA GLY A 450 7720 6537 10366 -726 470 -50 C
ATOM 3005 C GLY A 450 21.974 -3.993 69.216 1.00 66.67 C
ANISOU 3005 C GLY A 450 7875 6723 10733 -745 593 -35 C
ATOM 3006 O GLY A 450 21.841 -3.251 68.237 1.00 58.50 O
ANISOU 3006 O GLY A 450 7027 5524 9674 -706 811 -9 O
ATOM 3007 N SER A 451 22.809 -5.029 69.225 1.00 67.33 N
ANISOU 3007 N SER A 451 7699 6940 10941 -784 469 -46 N
ATOM 3008 CA SER A 451 23.627 -5.381 68.071 1.00 61.24 C
ANISOU 3008 CA SER A 451 6828 6140 10301 -798 579 -37 C
ATOM 3009 C SER A 451 23.152 -6.627 67.340 1.00 59.38 C
ANISOU 3009 C SER A 451 6528 5977 10058 -611 515 82 C
ATOM 3010 O SER A 451 23.128 -6.638 66.107 1.00 63.09 O
ANISOU 3010 O SER A 451 7059 6369 10545 -545 664 129 O
ATOM 3011 CB SER A 451 25.084 -5.580 68.504 1.00 57.05 C
ANISOU 3011 CB SER A 451 6035 5717 9925 -981 518 -159 C
ATOM 3012 OG SER A 451 25.580 -4.425 69.160 1.00 62.12 O
ANISOU 3012 OG SER A 451 6719 6309 10573 -1197 592 -304 O
ATOM 3013 N VAL A 452 22.775 -7.680 68.071 1.00 63.70 N
ANISOU 3013 N VAL A 452 6970 6664 10569 -533 312 125 N
ATOM 3014 CA VAL A 452 22.390 -8.937 67.439 1.00 60.94 C
ANISOU 3014 CA VAL A 452 6566 6372 10217 -392 270 214 C
ATOM 3015 C VAL A 452 21.044 -8.782 66.737 1.00 70.57 C
ANISOU 3015 C VAL A 452 7968 7557 11287 -257 353 281 C
ATOM 3016 O VAL A 452 20.212 -7.941 67.105 1.00 74.15 O
ANISOU 3016 O VAL A 452 8577 7983 11611 -229 376 278 O
ATOM 3017 CB VAL A 452 22.353 -10.081 68.471 1.00 53.85 C
ANISOU 3017 CB VAL A 452 5549 5605 9308 -354 62 240 C
ATOM 3018 CG1 VAL A 452 23.677 -10.161 69.221 1.00 52.65 C
ANISOU 3018 CG1 VAL A 452 5201 5534 9269 -450 -37 169 C
ATOM 3019 CG2 VAL A 452 21.181 -9.915 69.435 1.00 50.38 C
ANISOU 3019 CG2 VAL A 452 5234 5202 8707 -321 -29 257 C
ATOM 3020 N ASP A 453 20.840 -9.587 65.691 1.00 70.70 N
ANISOU 3020 N ASP A 453 7960 7594 11310 -164 403 332 N
ATOM 3021 CA ASP A 453 19.562 -9.579 64.987 1.00 71.97 C
ANISOU 3021 CA ASP A 453 8249 7786 11310 -28 463 377 C
ATOM 3022 C ASP A 453 18.506 -10.401 65.714 1.00 63.92 C
ANISOU 3022 C ASP A 453 7215 6896 10174 19 326 389 C
ATOM 3023 O ASP A 453 17.328 -10.024 65.731 1.00 62.76 O
ANISOU 3023 O ASP A 453 7170 6814 9860 104 337 393 O
ATOM 3024 CB ASP A 453 19.741 -10.096 63.559 1.00 80.55 C
ANISOU 3024 CB ASP A 453 9312 8862 12431 36 578 405 C
ATOM 3025 CG ASP A 453 20.210 -9.020 62.607 1.00 87.82 C
ANISOU 3025 CG ASP A 453 10341 9655 13372 41 769 407 C
ATOM 3026 OD1 ASP A 453 20.434 -7.880 63.066 1.00 92.44 O
ANISOU 3026 OD1 ASP A 453 11029 10141 13954 -20 826 381 O
ATOM 3027 OD2 ASP A 453 20.354 -9.314 61.402 1.00 84.47 O
ANISOU 3027 OD2 ASP A 453 9918 9218 12961 100 878 431 O
ATOM 3028 N PHE A 454 18.901 -11.519 66.322 1.00 62.10 N
ANISOU 3028 N PHE A 454 6868 6708 10018 -26 210 394 N
ATOM 3029 CA PHE A 454 17.958 -12.407 66.984 1.00 46.94 C
ANISOU 3029 CA PHE A 454 4958 4886 7992 -5 113 403 C
ATOM 3030 C PHE A 454 18.538 -12.889 68.304 1.00 47.34 C
ANISOU 3030 C PHE A 454 4948 4943 8098 -63 -31 409 C
ATOM 3031 O PHE A 454 19.750 -13.068 68.442 1.00 71.78 O
ANISOU 3031 O PHE A 454 7939 8004 11331 -95 -64 410 O
ATOM 3032 CB PHE A 454 17.605 -13.624 66.116 1.00 46.50 C
ANISOU 3032 CB PHE A 454 4872 4871 7924 32 163 414 C
ATOM 3033 CG PHE A 454 16.912 -13.271 64.836 1.00 62.80 C
ANISOU 3033 CG PHE A 454 6985 6982 9895 107 286 400 C
ATOM 3034 CD1 PHE A 454 15.532 -13.295 64.749 1.00 56.53 C
ANISOU 3034 CD1 PHE A 454 6236 6329 8913 157 291 367 C
ATOM 3035 CD2 PHE A 454 17.642 -12.909 63.718 1.00 62.50 C
ANISOU 3035 CD2 PHE A 454 6937 6870 9942 135 399 413 C
ATOM 3036 CE1 PHE A 454 14.892 -12.962 63.567 1.00 45.95 C
ANISOU 3036 CE1 PHE A 454 4923 5077 7457 257 391 349 C
ATOM 3037 CE2 PHE A 454 17.009 -12.575 62.536 1.00 46.61 C
ANISOU 3037 CE2 PHE A 454 4980 4911 7817 229 510 408 C
ATOM 3038 CZ PHE A 454 15.635 -12.603 62.460 1.00 46.31 C
ANISOU 3038 CZ PHE A 454 4979 5036 7579 302 498 377 C
ATOM 3039 N VAL A 455 17.652 -13.086 69.274 1.00 47.01 N
ANISOU 3039 N VAL A 455 4965 4965 7932 -67 -114 408 N
ATOM 3040 CA VAL A 455 17.989 -13.713 70.544 1.00 47.46 C
ANISOU 3040 CA VAL A 455 4996 5041 7994 -94 -248 427 C
ATOM 3041 C VAL A 455 17.154 -14.977 70.674 1.00 47.06 C
ANISOU 3041 C VAL A 455 5000 5024 7857 -77 -246 452 C
ATOM 3042 O VAL A 455 15.968 -14.987 70.330 1.00 46.44 O
ANISOU 3042 O VAL A 455 4981 5005 7657 -79 -184 422 O
ATOM 3043 CB VAL A 455 17.759 -12.766 71.742 1.00 47.74 C
ANISOU 3043 CB VAL A 455 5079 5108 7953 -138 -336 395 C
ATOM 3044 CG1 VAL A 455 16.290 -12.374 71.851 1.00 47.02 C
ANISOU 3044 CG1 VAL A 455 5100 5073 7691 -118 -301 376 C
ATOM 3045 CG2 VAL A 455 18.256 -13.404 73.033 1.00 61.48 C
ANISOU 3045 CG2 VAL A 455 6786 6883 9690 -149 -482 418 C
ATOM 3046 N ILE A 456 17.779 -16.046 71.154 1.00 50.67 N
ANISOU 3046 N ILE A 456 5440 5448 8367 -57 -300 500 N
ATOM 3047 CA ILE A 456 17.131 -17.341 71.310 1.00 60.62 C
ANISOU 3047 CA ILE A 456 6789 6692 9552 -57 -263 525 C
ATOM 3048 C ILE A 456 16.889 -17.578 72.792 1.00 66.95 C
ANISOU 3048 C ILE A 456 7670 7512 10256 -64 -369 555 C
ATOM 3049 O ILE A 456 17.799 -17.412 73.616 1.00 68.04 O
ANISOU 3049 O ILE A 456 7763 7654 10435 -20 -487 589 O
ATOM 3050 CB ILE A 456 17.973 -18.468 70.689 1.00 48.35 C
ANISOU 3050 CB ILE A 456 5211 5049 8109 0 -207 572 C
ATOM 3051 CG1 ILE A 456 18.524 -18.019 69.333 1.00 48.03 C
ANISOU 3051 CG1 ILE A 456 5070 4994 8185 13 -124 545 C
ATOM 3052 CG2 ILE A 456 17.135 -19.721 70.533 1.00 48.43 C
ANISOU 3052 CG2 ILE A 456 5350 5016 8036 -33 -103 570 C
ATOM 3053 CD1 ILE A 456 19.360 -19.062 68.629 1.00 48.69 C
ANISOU 3053 CD1 ILE A 456 5123 4994 8382 75 -55 582 C
ATOM 3054 N ILE A 457 15.663 -17.963 73.126 1.00 57.52 N
ANISOU 3054 N ILE A 457 6584 6350 8921 -122 -324 529 N
ATOM 3055 CA ILE A 457 15.254 -18.237 74.499 1.00 48.49 C
ANISOU 3055 CA ILE A 457 5546 5220 7661 -141 -395 554 C
ATOM 3056 C ILE A 457 14.578 -19.603 74.499 1.00 57.03 C
ANISOU 3056 C ILE A 457 6763 6240 8664 -188 -278 563 C
ATOM 3057 O ILE A 457 13.339 -19.690 74.525 1.00 48.65 O
ANISOU 3057 O ILE A 457 5758 5246 7479 -288 -200 492 O
ATOM 3058 CB ILE A 457 14.330 -17.137 75.043 1.00 47.91 C
ANISOU 3058 CB ILE A 457 5480 5252 7472 -194 -434 492 C
ATOM 3059 CG1 ILE A 457 14.860 -15.752 74.654 1.00 47.52 C
ANISOU 3059 CG1 ILE A 457 5329 5227 7500 -169 -476 462 C
ATOM 3060 CG2 ILE A 457 14.203 -17.246 76.554 1.00 48.62 C
ANISOU 3060 CG2 ILE A 457 5662 5354 7458 -202 -532 523 C
ATOM 3061 CD1 ILE A 457 13.891 -14.619 74.915 1.00 47.04 C
ANISOU 3061 CD1 ILE A 457 5298 5250 7325 -191 -473 400 C
ATOM 3062 N PRO A 458 15.349 -20.692 74.440 1.00 56.88 N
ANISOU 3062 N PRO A 458 6805 6099 8709 -119 -245 639 N
ATOM 3063 CA PRO A 458 14.750 -22.030 74.351 1.00 58.49 C
ANISOU 3063 CA PRO A 458 7180 6202 8843 -179 -89 640 C
ATOM 3064 C PRO A 458 14.362 -22.606 75.703 1.00 67.12 C
ANISOU 3064 C PRO A 458 8460 7243 9798 -190 -98 692 C
ATOM 3065 O PRO A 458 14.451 -23.820 75.912 1.00 75.62 O
ANISOU 3065 O PRO A 458 9723 8168 10840 -170 11 751 O
ATOM 3066 CB PRO A 458 15.863 -22.856 73.701 1.00 53.31 C
ANISOU 3066 CB PRO A 458 6527 5413 8316 -64 -42 711 C
ATOM 3067 CG PRO A 458 17.119 -22.194 74.159 1.00 51.75 C
ANISOU 3067 CG PRO A 458 6198 5257 8209 83 -219 781 C
ATOM 3068 CD PRO A 458 16.815 -20.727 74.294 1.00 51.78 C
ANISOU 3068 CD PRO A 458 6065 5406 8204 16 -323 711 C
ATOM 3069 N SER A 459 13.929 -21.748 76.623 1.00 57.34 N
ANISOU 3069 N SER A 459 7201 6114 8472 -218 -209 673 N
ATOM 3070 CA SER A 459 13.664 -22.181 77.988 1.00 64.00 C
ANISOU 3070 CA SER A 459 8222 6918 9178 -212 -234 731 C
ATOM 3071 C SER A 459 12.501 -23.165 78.049 1.00 66.32 C
ANISOU 3071 C SER A 459 8706 7146 9347 -367 -34 681 C
ATOM 3072 O SER A 459 11.476 -22.984 77.387 1.00 60.47 O
ANISOU 3072 O SER A 459 7903 6503 8572 -522 68 551 O
ATOM 3073 CB SER A 459 13.365 -20.972 78.873 1.00 58.81 C
ANISOU 3073 CB SER A 459 7493 6403 8450 -229 -381 699 C
ATOM 3074 OG SER A 459 14.383 -19.992 78.764 1.00 60.15 O
ANISOU 3074 OG SER A 459 7487 6636 8733 -135 -536 711 O
ATOM 3075 N TYR A 460 12.671 -24.219 78.854 1.00 68.31 N
ANISOU 3075 N TYR A 460 9196 7240 9518 -322 33 777 N
ATOM 3076 CA TYR A 460 11.558 -25.113 79.154 1.00 69.87 C
ANISOU 3076 CA TYR A 460 9614 7359 9576 -499 241 723 C
ATOM 3077 C TYR A 460 10.500 -24.430 80.011 1.00 73.00 C
ANISOU 3077 C TYR A 460 9999 7906 9832 -625 207 646 C
ATOM 3078 O TYR A 460 9.318 -24.784 79.935 1.00 77.50 O
ANISOU 3078 O TYR A 460 10632 8514 10300 -833 377 525 O
ATOM 3079 CB TYR A 460 12.056 -26.366 79.874 1.00 71.08 C
ANISOU 3079 CB TYR A 460 10074 7274 9661 -393 338 866 C
ATOM 3080 CG TYR A 460 12.916 -27.286 79.041 1.00 68.30 C
ANISOU 3080 CG TYR A 460 9792 6741 9417 -278 437 935 C
ATOM 3081 CD1 TYR A 460 14.298 -27.151 79.025 1.00 72.90 C
ANISOU 3081 CD1 TYR A 460 10284 7312 10104 -12 274 1062 C
ATOM 3082 CD2 TYR A 460 12.349 -28.304 78.286 1.00 61.06 C
ANISOU 3082 CD2 TYR A 460 9030 5677 8492 -441 703 858 C
ATOM 3083 CE1 TYR A 460 15.090 -27.998 78.274 1.00 70.24 C
ANISOU 3083 CE1 TYR A 460 10009 6817 9862 115 370 1125 C
ATOM 3084 CE2 TYR A 460 13.133 -29.156 77.532 1.00 60.51 C
ANISOU 3084 CE2 TYR A 460 9046 5427 8518 -330 808 919 C
ATOM 3085 CZ TYR A 460 14.503 -28.996 77.529 1.00 64.15 C
ANISOU 3085 CZ TYR A 460 9416 5874 9083 -38 639 1060 C
ATOM 3086 OH TYR A 460 15.298 -29.834 76.783 1.00 71.69 O
ANISOU 3086 OH TYR A 460 10448 6659 10130 94 746 1120 O
ATOM 3087 N PHE A 461 10.901 -23.452 80.821 1.00 68.72 N
ANISOU 3087 N PHE A 461 9370 7464 9277 -513 -2 696 N
ATOM 3088 CA PHE A 461 10.028 -22.890 81.842 1.00 72.24 C
ANISOU 3088 CA PHE A 461 9850 8022 9576 -599 -37 648 C
ATOM 3089 C PHE A 461 10.376 -21.423 82.042 1.00 73.31 C
ANISOU 3089 C PHE A 461 9777 8318 9758 -516 -253 631 C
ATOM 3090 O PHE A 461 11.541 -21.083 82.267 1.00 73.13 O
ANISOU 3090 O PHE A 461 9695 8279 9814 -359 -412 718 O
ATOM 3091 CB PHE A 461 10.172 -23.677 83.153 1.00 82.25 C
ANISOU 3091 CB PHE A 461 11394 9154 10704 -545 -12 767 C
ATOM 3092 CG PHE A 461 9.624 -22.972 84.365 1.00 91.70 C
ANISOU 3092 CG PHE A 461 12618 10465 11758 -577 -103 750 C
ATOM 3093 CD1 PHE A 461 10.482 -22.414 85.301 1.00 90.72 C
ANISOU 3093 CD1 PHE A 461 12481 10379 11610 -406 -314 846 C
ATOM 3094 CD2 PHE A 461 8.258 -22.889 84.582 1.00 96.85 C
ANISOU 3094 CD2 PHE A 461 13301 11207 12292 -782 28 623 C
ATOM 3095 CE1 PHE A 461 9.988 -21.772 86.423 1.00 90.80 C
ANISOU 3095 CE1 PHE A 461 12527 10491 11482 -439 -392 824 C
ATOM 3096 CE2 PHE A 461 7.757 -22.248 85.705 1.00 94.10 C
ANISOU 3096 CE2 PHE A 461 12984 10962 11810 -805 -46 606 C
ATOM 3097 CZ PHE A 461 8.624 -21.690 86.625 1.00 89.55 C
ANISOU 3097 CZ PHE A 461 12415 10398 11213 -634 -254 710 C
ATOM 3098 N GLU A 462 9.365 -20.565 81.962 1.00 77.83 N
ANISOU 3098 N GLU A 462 10244 9054 10274 -623 -244 509 N
ATOM 3099 CA GLU A 462 9.548 -19.134 82.157 1.00 83.58 C
ANISOU 3099 CA GLU A 462 10820 9910 11029 -559 -407 480 C
ATOM 3100 C GLU A 462 8.258 -18.515 82.675 1.00 88.22 C
ANISOU 3100 C GLU A 462 11403 10645 11470 -659 -371 374 C
ATOM 3101 O GLU A 462 7.290 -18.374 81.916 1.00 84.69 O
ANISOU 3101 O GLU A 462 10866 10318 10994 -742 -265 260 O
ATOM 3102 CB GLU A 462 9.971 -18.451 80.855 1.00 80.89 C
ANISOU 3102 CB GLU A 462 10286 9609 10840 -510 -431 441 C
ATOM 3103 CG GLU A 462 11.477 -18.289 80.678 1.00 86.67 C
ANISOU 3103 CG GLU A 462 10951 10259 11721 -379 -554 531 C
ATOM 3104 CD GLU A 462 12.048 -17.112 81.459 1.00100.09 C
ANISOU 3104 CD GLU A 462 12587 12019 13422 -324 -722 533 C
ATOM 3105 OE1 GLU A 462 11.300 -16.479 82.235 1.00104.87 O
ANISOU 3105 OE1 GLU A 462 13233 12703 13908 -372 -745 483 O
ATOM 3106 OE2 GLU A 462 13.251 -16.815 81.289 1.00106.60 O
ANISOU 3106 OE2 GLU A 462 13317 12820 14365 -244 -820 569 O
ATOM 3107 N PRO A 463 8.198 -18.151 83.959 1.00 89.89 N
ANISOU 3107 N PRO A 463 11704 10877 11575 -646 -456 402 N
ATOM 3108 CA PRO A 463 6.984 -17.482 84.460 1.00 87.34 C
ANISOU 3108 CA PRO A 463 11367 10704 11113 -726 -421 296 C
ATOM 3109 C PRO A 463 6.686 -16.170 83.740 1.00 82.66 C
ANISOU 3109 C PRO A 463 10595 10247 10565 -677 -462 209 C
ATOM 3110 O PRO A 463 5.565 -15.974 83.255 1.00 75.28 O
ANISOU 3110 O PRO A 463 9583 9461 9557 -730 -361 99 O
ATOM 3111 CB PRO A 463 7.291 -17.288 85.949 1.00 88.17 C
ANISOU 3111 CB PRO A 463 11604 10780 11115 -691 -531 362 C
ATOM 3112 CG PRO A 463 8.791 -17.291 86.030 1.00 88.36 C
ANISOU 3112 CG PRO A 463 11616 10705 11252 -557 -681 473 C
ATOM 3113 CD PRO A 463 9.253 -18.248 84.983 1.00 86.70 C
ANISOU 3113 CD PRO A 463 11393 10388 11161 -539 -598 520 C
ATOM 3114 N PHE A 464 7.671 -15.276 83.632 1.00 84.33 N
ANISOU 3114 N PHE A 464 10741 10416 10884 -571 -593 251 N
ATOM 3115 CA PHE A 464 7.608 -14.123 82.741 1.00 90.76 C
ANISOU 3115 CA PHE A 464 11425 11295 11763 -505 -600 193 C
ATOM 3116 C PHE A 464 9.003 -13.962 82.164 1.00 84.01 C
ANISOU 3116 C PHE A 464 10511 10324 11085 -437 -677 260 C
ATOM 3117 O PHE A 464 9.977 -13.918 82.919 1.00 85.31 O
ANISOU 3117 O PHE A 464 10707 10421 11285 -415 -792 316 O
ATOM 3118 CB PHE A 464 7.164 -12.847 83.467 1.00 99.80 C
ANISOU 3118 CB PHE A 464 12588 12516 12815 -473 -648 138 C
ATOM 3119 CG PHE A 464 6.021 -12.127 82.797 1.00103.80 C
ANISOU 3119 CG PHE A 464 13023 13172 13245 -427 -556 43 C
ATOM 3120 CD1 PHE A 464 4.711 -12.495 83.056 1.00105.85 C
ANISOU 3120 CD1 PHE A 464 13276 13592 13349 -484 -466 -36 C
ATOM 3121 CD2 PHE A 464 6.255 -11.081 81.921 1.00100.93 C
ANISOU 3121 CD2 PHE A 464 12599 12801 12947 -317 -549 30 C
ATOM 3122 CE1 PHE A 464 3.661 -11.845 82.448 1.00101.01 C
ANISOU 3122 CE1 PHE A 464 12570 13165 12644 -410 -392 -130 C
ATOM 3123 CE2 PHE A 464 5.209 -10.428 81.312 1.00101.10 C
ANISOU 3123 CE2 PHE A 464 12567 12975 12871 -225 -467 -44 C
ATOM 3124 CZ PHE A 464 3.910 -10.811 81.577 1.00100.24 C
ANISOU 3124 CZ PHE A 464 12423 13062 12602 -259 -399 -126 C
ATOM 3125 N GLY A 465 9.103 -13.902 80.839 1.00 81.28 N
ANISOU 3125 N GLY A 465 10070 9976 10838 -404 -612 244 N
ATOM 3126 CA GLY A 465 10.401 -13.890 80.193 1.00 82.28 C
ANISOU 3126 CA GLY A 465 10132 9996 11135 -354 -658 301 C
ATOM 3127 C GLY A 465 11.040 -12.519 80.147 1.00 81.81 C
ANISOU 3127 C GLY A 465 10030 9913 11141 -312 -718 279 C
ATOM 3128 O GLY A 465 10.911 -11.801 79.151 1.00 86.55 O
ANISOU 3128 O GLY A 465 10583 10517 11784 -267 -648 247 O
ATOM 3129 N LEU A 466 11.724 -12.137 81.228 1.00 75.20 N
ANISOU 3129 N LEU A 466 9222 9053 10298 -329 -833 288 N
ATOM 3130 CA LEU A 466 12.345 -10.818 81.280 1.00 69.16 C
ANISOU 3130 CA LEU A 466 8432 8257 9587 -331 -868 240 C
ATOM 3131 C LEU A 466 13.450 -10.670 80.244 1.00 72.62 C
ANISOU 3131 C LEU A 466 8770 8622 10202 -319 -848 251 C
ATOM 3132 O LEU A 466 13.687 -9.564 79.746 1.00 81.86 O
ANISOU 3132 O LEU A 466 9936 9743 11422 -324 -793 203 O
ATOM 3133 CB LEU A 466 12.896 -10.547 82.676 1.00 68.31 C
ANISOU 3133 CB LEU A 466 8358 8172 9426 -375 -1001 225 C
ATOM 3134 CG LEU A 466 11.942 -9.848 83.643 1.00 73.88 C
ANISOU 3134 CG LEU A 466 9171 8928 9971 -399 -1001 170 C
ATOM 3135 CD1 LEU A 466 10.771 -10.748 83.991 1.00 83.91 C
ANISOU 3135 CD1 LEU A 466 10511 10264 11108 -394 -959 198 C
ATOM 3136 CD2 LEU A 466 12.679 -9.401 84.896 1.00 75.95 C
ANISOU 3136 CD2 LEU A 466 9451 9214 10191 -453 -1133 134 C
ATOM 3137 N VAL A 467 14.139 -11.762 79.909 1.00 63.17 N
ANISOU 3137 N VAL A 467 7505 7403 9092 -299 -875 314 N
ATOM 3138 CA VAL A 467 15.148 -11.687 78.859 1.00 58.87 C
ANISOU 3138 CA VAL A 467 6853 6800 8714 -286 -842 320 C
ATOM 3139 C VAL A 467 14.499 -11.320 77.534 1.00 48.32 C
ANISOU 3139 C VAL A 467 5525 5436 7398 -254 -696 304 C
ATOM 3140 O VAL A 467 15.068 -10.557 76.739 1.00 55.98 O
ANISOU 3140 O VAL A 467 6458 6346 8464 -255 -635 280 O
ATOM 3141 CB VAL A 467 15.926 -13.018 78.763 1.00 64.60 C
ANISOU 3141 CB VAL A 467 7518 7512 9513 -240 -887 396 C
ATOM 3142 CG1 VAL A 467 16.882 -12.993 77.584 1.00 56.68 C
ANISOU 3142 CG1 VAL A 467 6397 6459 8679 -223 -835 397 C
ATOM 3143 CG2 VAL A 467 16.679 -13.297 80.059 1.00 76.51 C
ANISOU 3143 CG2 VAL A 467 9012 9076 10980 -226 -1043 417 C
ATOM 3144 N ALA A 468 13.277 -11.804 77.297 1.00 47.65 N
ANISOU 3144 N ALA A 468 5491 5409 7204 -229 -631 307 N
ATOM 3145 CA ALA A 468 12.553 -11.410 76.095 1.00 47.00 C
ANISOU 3145 CA ALA A 468 5405 5354 7098 -173 -508 281 C
ATOM 3146 C ALA A 468 12.218 -9.926 76.118 1.00 47.19 C
ANISOU 3146 C ALA A 468 5495 5370 7063 -130 -467 237 C
ATOM 3147 O ALA A 468 12.396 -9.230 75.114 1.00 49.80 O
ANISOU 3147 O ALA A 468 5833 5651 7438 -71 -375 234 O
ATOM 3148 CB ALA A 468 11.278 -12.238 75.952 1.00 46.62 C
ANISOU 3148 CB ALA A 468 5368 5422 6921 -172 -453 261 C
ATOM 3149 N LEU A 469 11.760 -9.414 77.264 1.00 72.97 N
ANISOU 3149 N LEU A 469 8833 8669 10223 -152 -519 206 N
ATOM 3150 CA LEU A 469 11.416 -7.998 77.346 1.00 47.98 C
ANISOU 3150 CA LEU A 469 5766 5474 6992 -101 -461 163 C
ATOM 3151 C LEU A 469 12.644 -7.122 77.157 1.00 48.67 C
ANISOU 3151 C LEU A 469 5871 5411 7210 -153 -438 148 C
ATOM 3152 O LEU A 469 12.570 -6.066 76.518 1.00 49.04 O
ANISOU 3152 O LEU A 469 6008 5376 7248 -91 -318 132 O
ATOM 3153 CB LEU A 469 10.751 -7.696 78.687 1.00 48.38 C
ANISOU 3153 CB LEU A 469 5893 5585 6906 -127 -521 126 C
ATOM 3154 CG LEU A 469 9.374 -8.304 78.946 1.00 48.04 C
ANISOU 3154 CG LEU A 469 5845 5703 6704 -89 -510 111 C
ATOM 3155 CD1 LEU A 469 8.808 -7.777 80.258 1.00 64.40 C
ANISOU 3155 CD1 LEU A 469 8007 7817 8645 -111 -552 69 C
ATOM 3156 CD2 LEU A 469 8.432 -8.017 77.788 1.00 47.78 C
ANISOU 3156 CD2 LEU A 469 5793 5770 6593 49 -394 94 C
ATOM 3157 N GLU A 470 13.793 -7.561 77.670 1.00 49.10 N
ANISOU 3157 N GLU A 470 5841 5436 7378 -261 -539 148 N
ATOM 3158 CA GLU A 470 15.002 -6.760 77.537 1.00 50.06 C
ANISOU 3158 CA GLU A 470 5946 5452 7623 -348 -513 100 C
ATOM 3159 C GLU A 470 15.494 -6.757 76.100 1.00 49.82 C
ANISOU 3159 C GLU A 470 5873 5345 7712 -313 -396 128 C
ATOM 3160 O GLU A 470 15.811 -5.700 75.545 1.00 96.16 O
ANISOU 3160 O GLU A 470 11824 11096 13618 -330 -267 93 O
ATOM 3161 CB GLU A 470 16.089 -7.288 78.467 1.00 62.33 C
ANISOU 3161 CB GLU A 470 7380 7058 9244 -452 -667 79 C
ATOM 3162 CG GLU A 470 15.761 -7.186 79.936 1.00 70.86 C
ANISOU 3162 CG GLU A 470 8511 8213 10200 -494 -783 45 C
ATOM 3163 CD GLU A 470 16.853 -7.771 80.804 1.00 81.25 C
ANISOU 3163 CD GLU A 470 9698 9618 11556 -555 -947 31 C
ATOM 3164 OE1 GLU A 470 16.814 -7.550 82.033 1.00 86.20 O
ANISOU 3164 OE1 GLU A 470 10358 10313 12081 -603 -1048 -14 O
ATOM 3165 OE2 GLU A 470 17.749 -8.451 80.257 1.00 83.99 O
ANISOU 3165 OE2 GLU A 470 9909 9980 12022 -540 -974 63 O
ATOM 3166 N ALA A 471 15.564 -7.935 75.477 1.00 56.38 N
ANISOU 3166 N ALA A 471 6599 6225 8596 -269 -421 189 N
ATOM 3167 CA ALA A 471 16.045 -7.988 74.104 1.00 57.37 C
ANISOU 3167 CA ALA A 471 6682 6285 8830 -236 -310 213 C
ATOM 3168 C ALA A 471 15.087 -7.286 73.147 1.00 48.52 C
ANISOU 3168 C ALA A 471 5685 5139 7612 -114 -162 227 C
ATOM 3169 O ALA A 471 15.527 -6.620 72.204 1.00 48.95 O
ANISOU 3169 O ALA A 471 5786 5089 7725 -95 -31 228 O
ATOM 3170 CB ALA A 471 16.271 -9.438 73.690 1.00 48.25 C
ANISOU 3170 CB ALA A 471 5407 5185 7740 -211 -359 269 C
ATOM 3171 N MET A 472 13.776 -7.407 73.375 1.00 47.99 N
ANISOU 3171 N MET A 472 5671 5180 7381 -21 -173 234 N
ATOM 3172 CA MET A 472 12.814 -6.695 72.541 1.00 48.01 C
ANISOU 3172 CA MET A 472 5777 5208 7256 137 -47 242 C
ATOM 3173 C MET A 472 12.869 -5.189 72.772 1.00 79.80 C
ANISOU 3173 C MET A 472 9981 9102 11239 168 50 218 C
ATOM 3174 O MET A 472 12.582 -4.412 71.853 1.00 49.57 O
ANISOU 3174 O MET A 472 6272 5214 7348 307 196 242 O
ATOM 3175 CB MET A 472 11.405 -7.237 72.793 1.00 47.48 C
ANISOU 3175 CB MET A 472 5685 5338 7017 221 -88 231 C
ATOM 3176 CG MET A 472 11.206 -8.674 72.314 1.00 46.72 C
ANISOU 3176 CG MET A 472 5452 5357 6942 189 -124 239 C
ATOM 3177 SD MET A 472 9.765 -9.506 73.020 1.00 46.45 S
ANISOU 3177 SD MET A 472 5372 5545 6732 178 -177 189 S
ATOM 3178 CE MET A 472 8.433 -8.564 72.286 1.00 46.92 C
ANISOU 3178 CE MET A 472 5467 5780 6581 391 -81 151 C
ATOM 3179 N CYS A 473 13.236 -4.755 73.982 1.00 71.48 N
ANISOU 3179 N CYS A 473 8966 7994 10201 46 -14 169 N
ATOM 3180 CA CYS A 473 13.411 -3.326 74.220 1.00 61.29 C
ANISOU 3180 CA CYS A 473 7864 6542 8880 36 103 127 C
ATOM 3181 C CYS A 473 14.577 -2.760 73.417 1.00 65.04 C
ANISOU 3181 C CYS A 473 8379 6834 9498 -48 237 115 C
ATOM 3182 O CYS A 473 14.559 -1.580 73.051 1.00 79.58 O
ANISOU 3182 O CYS A 473 10429 8511 11298 -2 416 104 O
ATOM 3183 CB CYS A 473 13.601 -3.059 75.713 1.00 67.66 C
ANISOU 3183 CB CYS A 473 8687 7351 9671 -105 0 55 C
ATOM 3184 SG CYS A 473 12.065 -2.735 76.604 1.00 87.74 S
ANISOU 3184 SG CYS A 473 11342 10005 11990 28 -27 47 S
ATOM 3185 N LEU A 474 15.585 -3.579 73.127 1.00 58.92 N
ANISOU 3185 N LEU A 474 7423 6079 8884 -165 173 114 N
ATOM 3186 CA LEU A 474 16.723 -3.175 72.313 1.00 70.20 C
ANISOU 3186 CA LEU A 474 8852 7363 10457 -260 302 92 C
ATOM 3187 C LEU A 474 16.558 -3.561 70.847 1.00 73.69 C
ANISOU 3187 C LEU A 474 9287 7802 10912 -120 402 173 C
ATOM 3188 O LEU A 474 17.509 -3.430 70.068 1.00 83.88 O
ANISOU 3188 O LEU A 474 10553 8989 12327 -194 507 164 O
ATOM 3189 CB LEU A 474 18.014 -3.766 72.882 1.00 66.29 C
ANISOU 3189 CB LEU A 474 8145 6918 10126 -461 177 28 C
ATOM 3190 CG LEU A 474 18.642 -3.071 74.099 1.00 57.09 C
ANISOU 3190 CG LEU A 474 6983 5732 8976 -654 131 -93 C
ATOM 3191 CD1 LEU A 474 18.905 -1.611 73.788 1.00 57.39 C
ANISOU 3191 CD1 LEU A 474 7237 5556 9012 -740 362 -166 C
ATOM 3192 CD2 LEU A 474 17.801 -3.203 75.366 1.00 53.77 C
ANISOU 3192 CD2 LEU A 474 6595 5417 8420 -620 -16 -97 C
ATOM 3193 N GLY A 475 15.376 -4.035 70.458 1.00 50.74 N
ANISOU 3193 N GLY A 475 6387 5023 7868 71 374 237 N
ATOM 3194 CA GLY A 475 15.083 -4.361 69.080 1.00 50.33 C
ANISOU 3194 CA GLY A 475 6332 5002 7788 218 464 301 C
ATOM 3195 C GLY A 475 15.457 -5.757 68.633 1.00 64.17 C
ANISOU 3195 C GLY A 475 7873 6861 9646 173 370 319 C
ATOM 3196 O GLY A 475 15.234 -6.089 67.462 1.00 64.82 O
ANISOU 3196 O GLY A 475 7943 6981 9703 281 444 359 O
ATOM 3197 N ALA A 476 16.032 -6.578 69.507 1.00 76.42 N
ANISOU 3197 N ALA A 476 9274 8460 11303 31 221 293 N
ATOM 3198 CA ALA A 476 16.326 -7.957 69.143 1.00 48.15 C
ANISOU 3198 CA ALA A 476 5527 4961 7806 12 147 318 C
ATOM 3199 C ALA A 476 15.030 -8.732 68.932 1.00 47.23 C
ANISOU 3199 C ALA A 476 5398 5003 7543 120 114 336 C
ATOM 3200 O ALA A 476 14.031 -8.509 69.622 1.00 47.09 O
ANISOU 3200 O ALA A 476 5435 5074 7382 163 70 319 O
ATOM 3201 CB ALA A 476 17.177 -8.629 70.219 1.00 48.32 C
ANISOU 3201 CB ALA A 476 5420 5001 7937 -118 -2 297 C
ATOM 3202 N ILE A 477 15.040 -9.633 67.959 1.00 46.78 N
ANISOU 3202 N ILE A 477 5264 4994 7518 151 148 355 N
ATOM 3203 CA ILE A 477 13.882 -10.459 67.629 1.00 63.65 C
ANISOU 3203 CA ILE A 477 7366 7299 9521 214 137 341 C
ATOM 3204 C ILE A 477 14.023 -11.783 68.372 1.00 61.44 C
ANISOU 3204 C ILE A 477 7002 7047 9296 105 36 336 C
ATOM 3205 O ILE A 477 15.030 -12.484 68.177 1.00 63.45 O
ANISOU 3205 O ILE A 477 7190 7217 9700 51 27 362 O
ATOM 3206 CB ILE A 477 13.761 -10.682 66.115 1.00 58.35 C
ANISOU 3206 CB ILE A 477 6674 6670 8828 302 248 347 C
ATOM 3207 CG1 ILE A 477 13.789 -9.339 65.383 1.00 57.46 C
ANISOU 3207 CG1 ILE A 477 6684 6488 8659 429 368 374 C
ATOM 3208 CG2 ILE A 477 12.484 -11.444 65.788 1.00 62.73 C
ANISOU 3208 CG2 ILE A 477 7175 7441 9216 346 243 296 C
ATOM 3209 CD1 ILE A 477 14.349 -9.422 63.988 1.00 72.72 C
ANISOU 3209 CD1 ILE A 477 8613 8369 10650 477 486 400 C
ATOM 3210 N PRO A 478 13.081 -12.146 69.243 1.00 52.29 N
ANISOU 3210 N PRO A 478 5857 5996 8015 81 -28 308 N
ATOM 3211 CA PRO A 478 13.245 -13.371 70.033 1.00 50.27 C
ANISOU 3211 CA PRO A 478 5572 5730 7798 -16 -100 316 C
ATOM 3212 C PRO A 478 12.614 -14.597 69.389 1.00 60.28 C
ANISOU 3212 C PRO A 478 6808 7078 9015 -48 -35 282 C
ATOM 3213 O PRO A 478 11.422 -14.605 69.066 1.00 61.33 O
ANISOU 3213 O PRO A 478 6932 7375 8994 -33 11 214 O
ATOM 3214 CB PRO A 478 12.554 -13.015 71.354 1.00 49.31 C
ANISOU 3214 CB PRO A 478 5508 5667 7560 -43 -179 297 C
ATOM 3215 CG PRO A 478 11.454 -12.084 70.939 1.00 51.25 C
ANISOU 3215 CG PRO A 478 5783 6038 7653 51 -121 251 C
ATOM 3216 CD PRO A 478 11.933 -11.344 69.702 1.00 52.60 C
ANISOU 3216 CD PRO A 478 5958 6150 7878 146 -32 272 C
ATOM 3217 N ILE A 479 13.428 -15.627 69.179 1.00 65.87 N
ANISOU 3217 N ILE A 479 7496 7684 9847 -89 -23 316 N
ATOM 3218 CA ILE A 479 12.959 -16.974 68.887 1.00 63.56 C
ANISOU 3218 CA ILE A 479 7216 7417 9518 -158 47 281 C
ATOM 3219 C ILE A 479 12.951 -17.710 70.219 1.00 67.84 C
ANISOU 3219 C ILE A 479 7836 7899 10039 -223 -13 312 C
ATOM 3220 O ILE A 479 14.009 -18.062 70.751 1.00 65.95 O
ANISOU 3220 O ILE A 479 7616 7532 9911 -197 -72 391 O
ATOM 3221 CB ILE A 479 13.855 -17.680 67.862 1.00 45.99 C
ANISOU 3221 CB ILE A 479 4957 5089 7429 -144 119 307 C
ATOM 3222 CG1 ILE A 479 14.354 -16.689 66.806 1.00 45.72 C
ANISOU 3222 CG1 ILE A 479 4862 5053 7457 -60 152 316 C
ATOM 3223 CG2 ILE A 479 13.102 -18.812 67.200 1.00 58.48 C
ANISOU 3223 CG2 ILE A 479 6556 6727 8936 -222 236 230 C
ATOM 3224 CD1 ILE A 479 15.402 -17.261 65.882 1.00 48.65 C
ANISOU 3224 CD1 ILE A 479 5192 5315 7979 -42 218 347 C
ATOM 3225 N ALA A 480 11.767 -17.930 70.781 1.00 46.39 N
ANISOU 3225 N ALA A 480 5165 5292 7168 -296 6 249 N
ATOM 3226 CA ALA A 480 11.670 -18.409 72.149 1.00 64.80 C
ANISOU 3226 CA ALA A 480 7597 7572 9452 -350 -46 283 C
ATOM 3227 C ALA A 480 10.623 -19.504 72.244 1.00 61.19 C
ANISOU 3227 C ALA A 480 7213 7163 8873 -483 72 205 C
ATOM 3228 O ALA A 480 9.705 -19.591 71.426 1.00 58.45 O
ANISOU 3228 O ALA A 480 6803 6966 8439 -544 166 92 O
ATOM 3229 CB ALA A 480 11.334 -17.271 73.117 1.00 72.80 C
ANISOU 3229 CB ALA A 480 8613 8659 10389 -321 -151 282 C
ATOM 3230 N SER A 481 10.788 -20.348 73.258 1.00 68.79 N
ANISOU 3230 N SER A 481 8314 8005 9817 -529 75 259 N
ATOM 3231 CA SER A 481 9.854 -21.439 73.490 1.00 49.23 C
ANISOU 3231 CA SER A 481 5951 5531 7223 -686 219 185 C
ATOM 3232 C SER A 481 8.481 -20.899 73.865 1.00 49.15 C
ANISOU 3232 C SER A 481 5891 5741 7044 -780 232 64 C
ATOM 3233 O SER A 481 8.363 -19.898 74.574 1.00 77.21 O
ANISOU 3233 O SER A 481 9411 9367 10558 -712 113 88 O
ATOM 3234 CB SER A 481 10.369 -22.362 74.590 1.00 50.35 C
ANISOU 3234 CB SER A 481 6294 5474 7364 -683 227 292 C
ATOM 3235 OG SER A 481 11.656 -22.862 74.285 1.00 66.09 O
ANISOU 3235 OG SER A 481 8321 7290 9499 -559 209 406 O
ATOM 3236 N ALA A 482 7.437 -21.575 73.387 1.00 49.83 N
ANISOU 3236 N ALA A 482 5966 5945 7023 -943 386 -81 N
ATOM 3237 CA ALA A 482 6.055 -21.169 73.646 1.00 50.10 C
ANISOU 3237 CA ALA A 482 5917 6239 6881 -1039 417 -226 C
ATOM 3238 C ALA A 482 5.595 -21.749 74.985 1.00 63.90 C
ANISOU 3238 C ALA A 482 7830 7918 8531 -1168 469 -224 C
ATOM 3239 O ALA A 482 4.795 -22.685 75.060 1.00 73.57 O
ANISOU 3239 O ALA A 482 9122 9175 9655 -1375 641 -343 O
ATOM 3240 CB ALA A 482 5.152 -21.611 72.501 1.00 50.69 C
ANISOU 3240 CB ALA A 482 5867 6525 6869 -1166 557 -412 C
ATOM 3241 N VAL A 483 6.119 -21.162 76.061 1.00 50.73 N
ANISOU 3241 N VAL A 483 6234 6156 6884 -1055 329 -96 N
ATOM 3242 CA VAL A 483 5.862 -21.643 77.415 1.00 51.72 C
ANISOU 3242 CA VAL A 483 6542 6191 6917 -1138 359 -60 C
ATOM 3243 C VAL A 483 5.687 -20.448 78.342 1.00 64.37 C
ANISOU 3243 C VAL A 483 8099 7898 8461 -1042 204 -31 C
ATOM 3244 O VAL A 483 6.596 -19.619 78.471 1.00 62.44 O
ANISOU 3244 O VAL A 483 7817 7595 8313 -878 44 74 O
ATOM 3245 CB VAL A 483 6.987 -22.559 77.934 1.00 58.45 C
ANISOU 3245 CB VAL A 483 7610 6744 7853 -1081 364 104 C
ATOM 3246 CG1 VAL A 483 6.822 -23.966 77.380 1.00 85.07 C
ANISOU 3246 CG1 VAL A 483 11119 9983 11221 -1230 586 55 C
ATOM 3247 CG2 VAL A 483 8.365 -21.996 77.582 1.00 51.50 C
ANISOU 3247 CG2 VAL A 483 6652 5774 7141 -869 197 236 C
ATOM 3248 N GLY A 484 4.528 -20.362 78.986 1.00 72.61 N
ANISOU 3248 N GLY A 484 9147 9098 9344 -1160 266 -137 N
ATOM 3249 CA GLY A 484 4.337 -19.407 80.066 1.00 69.69 C
ANISOU 3249 CA GLY A 484 8786 8792 8901 -1087 146 -107 C
ATOM 3250 C GLY A 484 4.511 -17.973 79.613 1.00 62.61 C
ANISOU 3250 C GLY A 484 7726 8014 8051 -914 7 -105 C
ATOM 3251 O GLY A 484 3.849 -17.495 78.678 1.00 75.05 O
ANISOU 3251 O GLY A 484 9139 9789 9589 -885 42 -210 O
ATOM 3252 N GLY A 485 5.415 -17.268 80.296 1.00 49.89 N
ANISOU 3252 N GLY A 485 6168 6284 6505 -792 -143 11 N
ATOM 3253 CA GLY A 485 5.599 -15.856 80.021 1.00 49.05 C
ANISOU 3253 CA GLY A 485 5959 6247 6432 -647 -245 11 C
ATOM 3254 C GLY A 485 6.061 -15.579 78.607 1.00 69.41 C
ANISOU 3254 C GLY A 485 8420 8823 9127 -561 -235 13 C
ATOM 3255 O GLY A 485 5.687 -14.564 78.019 1.00 81.33 O
ANISOU 3255 O GLY A 485 9839 10453 10608 -457 -241 -33 O
ATOM 3256 N LEU A 486 6.886 -16.465 78.044 1.00 72.26 N
ANISOU 3256 N LEU A 486 8800 9043 9612 -584 -211 72 N
ATOM 3257 CA LEU A 486 7.264 -16.312 76.645 1.00 47.66 C
ANISOU 3257 CA LEU A 486 5578 5933 6598 -517 -180 65 C
ATOM 3258 C LEU A 486 6.059 -16.478 75.728 1.00 47.82 C
ANISOU 3258 C LEU A 486 5491 6175 6504 -560 -65 -70 C
ATOM 3259 O LEU A 486 5.945 -15.780 74.714 1.00 85.64 O
ANISOU 3259 O LEU A 486 10176 11067 11296 -450 -59 -100 O
ATOM 3260 CB LEU A 486 8.358 -17.318 76.290 1.00 47.78 C
ANISOU 3260 CB LEU A 486 5639 5756 6758 -534 -166 149 C
ATOM 3261 CG LEU A 486 9.692 -17.171 77.022 1.00 47.89 C
ANISOU 3261 CG LEU A 486 5710 5601 6886 -460 -292 273 C
ATOM 3262 CD1 LEU A 486 10.658 -18.266 76.595 1.00 48.29 C
ANISOU 3262 CD1 LEU A 486 5796 5496 7058 -447 -260 348 C
ATOM 3263 CD2 LEU A 486 10.297 -15.794 76.792 1.00 47.30 C
ANISOU 3263 CD2 LEU A 486 5551 5534 6886 -360 -384 286 C
ATOM 3264 N ARG A 487 5.140 -17.384 76.073 1.00 59.00 N
ANISOU 3264 N ARG A 487 6932 7682 7804 -718 36 -162 N
ATOM 3265 CA ARG A 487 3.919 -17.518 75.286 1.00 63.75 C
ANISOU 3265 CA ARG A 487 7395 8558 8271 -778 142 -328 C
ATOM 3266 C ARG A 487 3.041 -16.280 75.404 1.00 66.37 C
ANISOU 3266 C ARG A 487 7619 9133 8465 -649 92 -393 C
ATOM 3267 O ARG A 487 2.334 -15.932 74.452 1.00 70.69 O
ANISOU 3267 O ARG A 487 8014 9926 8918 -575 129 -495 O
ATOM 3268 CB ARG A 487 3.138 -18.761 75.718 1.00 70.72 C
ANISOU 3268 CB ARG A 487 8333 9483 9054 -1017 285 -437 C
ATOM 3269 CG ARG A 487 2.052 -19.174 74.730 1.00 82.75 C
ANISOU 3269 CG ARG A 487 9690 11294 10457 -1130 414 -638 C
ATOM 3270 CD ARG A 487 1.002 -20.086 75.352 1.00 98.97 C
ANISOU 3270 CD ARG A 487 11776 13460 12369 -1391 569 -792 C
ATOM 3271 NE ARG A 487 1.588 -21.116 76.205 1.00107.10 N
ANISOU 3271 NE ARG A 487 13059 14169 13466 -1529 642 -696 N
ATOM 3272 CZ ARG A 487 1.462 -21.141 77.527 1.00110.66 C
ANISOU 3272 CZ ARG A 487 13657 14527 13861 -1574 634 -641 C
ATOM 3273 NH1 ARG A 487 0.764 -20.198 78.143 1.00106.64 N
ANISOU 3273 NH1 ARG A 487 13056 14220 13241 -1510 558 -684 N
ATOM 3274 NH2 ARG A 487 2.027 -22.111 78.234 1.00110.91 N
ANISOU 3274 NH2 ARG A 487 13940 14265 13935 -1663 708 -538 N
ATOM 3275 N ASP A 488 3.080 -15.600 76.551 1.00 76.84 N
ANISOU 3275 N ASP A 488 9028 10402 9764 -601 12 -336 N
ATOM 3276 CA ASP A 488 2.270 -14.395 76.707 1.00 77.89 C
ANISOU 3276 CA ASP A 488 9089 10742 9764 -456 -22 -390 C
ATOM 3277 C ASP A 488 2.879 -13.202 75.979 1.00 66.57 C
ANISOU 3277 C ASP A 488 7645 9251 8399 -231 -84 -311 C
ATOM 3278 O ASP A 488 2.155 -12.421 75.351 1.00 52.95 O
ANISOU 3278 O ASP A 488 5826 7737 6555 -69 -62 -371 O
ATOM 3279 CB ASP A 488 2.088 -14.057 78.188 1.00 79.03 C
ANISOU 3279 CB ASP A 488 9342 10836 9848 -489 -71 -365 C
ATOM 3280 CG ASP A 488 1.707 -15.259 79.017 1.00 92.24 C
ANISOU 3280 CG ASP A 488 11089 12489 11468 -716 4 -409 C
ATOM 3281 OD1 ASP A 488 2.409 -15.538 80.012 1.00 98.81 O
ANISOU 3281 OD1 ASP A 488 12081 13104 12358 -766 -48 -305 O
ATOM 3282 OD2 ASP A 488 0.720 -15.937 78.661 1.00 96.85 O
ANISOU 3282 OD2 ASP A 488 11576 13281 11943 -846 124 -553 O
ATOM 3283 N ILE A 489 4.201 -13.046 76.055 1.00 84.42 N
ANISOU 3283 N ILE A 489 10002 11236 10836 -212 -150 -183 N
ATOM 3284 CA ILE A 489 4.850 -11.849 75.532 1.00 47.44 C
ANISOU 3284 CA ILE A 489 5346 6458 6222 -35 -185 -113 C
ATOM 3285 C ILE A 489 4.915 -11.884 74.010 1.00 77.93 C
ANISOU 3285 C ILE A 489 9119 10385 10106 57 -123 -124 C
ATOM 3286 O ILE A 489 4.461 -10.957 73.332 1.00 68.57 O
ANISOU 3286 O ILE A 489 7907 9319 8827 242 -92 -141 O
ATOM 3287 CB ILE A 489 6.255 -11.701 76.148 1.00 47.03 C
ANISOU 3287 CB ILE A 489 5398 6126 6343 -78 -268 -3 C
ATOM 3288 CG1 ILE A 489 6.165 -11.476 77.662 1.00 47.36 C
ANISOU 3288 CG1 ILE A 489 5532 6131 6332 -138 -338 3 C
ATOM 3289 CG2 ILE A 489 7.029 -10.577 75.466 1.00 51.75 C
ANISOU 3289 CG2 ILE A 489 6026 6605 7031 54 -266 50 C
ATOM 3290 CD1 ILE A 489 7.506 -11.538 78.370 1.00 47.30 C
ANISOU 3290 CD1 ILE A 489 5596 5910 6466 -196 -434 88 C
ATOM 3291 N ILE A 490 5.483 -12.952 73.448 1.00 84.39 N
ANISOU 3291 N ILE A 490 9906 11122 11036 -54 -97 -111 N
ATOM 3292 CA ILE A 490 5.720 -13.006 72.010 1.00 46.88 C
ANISOU 3292 CA ILE A 490 5085 6403 6324 23 -42 -113 C
ATOM 3293 C ILE A 490 4.403 -13.209 71.270 1.00 47.61 C
ANISOU 3293 C ILE A 490 5042 6826 6223 60 27 -249 C
ATOM 3294 O ILE A 490 3.506 -13.929 71.730 1.00 63.47 O
ANISOU 3294 O ILE A 490 6990 9004 8123 -76 59 -358 O
ATOM 3295 CB ILE A 490 6.736 -14.115 71.683 1.00 46.50 C
ANISOU 3295 CB ILE A 490 5052 6167 6450 -103 -27 -64 C
ATOM 3296 CG1 ILE A 490 8.014 -13.882 72.484 1.00 46.12 C
ANISOU 3296 CG1 ILE A 490 5101 5856 6567 -119 -112 53 C
ATOM 3297 CG2 ILE A 490 7.037 -14.158 70.197 1.00 46.40 C
ANISOU 3297 CG2 ILE A 490 4973 6176 6480 -28 35 -67 C
ATOM 3298 CD1 ILE A 490 9.181 -14.713 72.031 1.00 55.54 C
ANISOU 3298 CD1 ILE A 490 6297 6870 7937 -171 -104 118 C
ATOM 3299 N THR A 491 4.282 -12.566 70.112 1.00 71.25 N
ANISOU 3299 N THR A 491 7984 9928 9160 245 59 -251 N
ATOM 3300 CA THR A 491 3.133 -12.692 69.229 1.00 72.93 C
ANISOU 3300 CA THR A 491 8039 10498 9173 321 111 -383 C
ATOM 3301 C THR A 491 3.637 -12.989 67.822 1.00 70.23 C
ANISOU 3301 C THR A 491 7655 10145 8884 366 160 -372 C
ATOM 3302 O THR A 491 4.845 -13.014 67.565 1.00 59.23 O
ANISOU 3302 O THR A 491 6358 8465 7684 348 159 -258 O
ATOM 3303 CB THR A 491 2.266 -11.425 69.241 1.00 66.70 C
ANISOU 3303 CB THR A 491 7233 9921 8187 585 99 -399 C
ATOM 3304 OG1 THR A 491 3.019 -10.325 68.717 1.00 49.41 O
ANISOU 3304 OG1 THR A 491 5177 7541 6057 800 105 -265 O
ATOM 3305 CG2 THR A 491 1.810 -11.096 70.658 1.00 57.19 C
ANISOU 3305 CG2 THR A 491 6081 8713 6935 540 57 -410 C
ATOM 3306 N ASN A 492 2.699 -13.225 66.901 1.00 79.67 N
ANISOU 3306 N ASN A 492 8692 11681 9896 424 204 -504 N
ATOM 3307 CA ASN A 492 3.084 -13.559 65.534 1.00 87.34 C
ANISOU 3307 CA ASN A 492 9616 12678 10890 462 254 -511 C
ATOM 3308 C ASN A 492 3.821 -12.409 64.857 1.00 84.52 C
ANISOU 3308 C ASN A 492 9376 12160 10575 720 255 -361 C
ATOM 3309 O ASN A 492 4.708 -12.643 64.028 1.00 80.19 O
ANISOU 3309 O ASN A 492 8868 11445 10153 709 294 -300 O
ATOM 3310 CB ASN A 492 1.844 -13.953 64.730 1.00 93.67 C
ANISOU 3310 CB ASN A 492 10205 13936 11448 482 292 -707 C
ATOM 3311 CG ASN A 492 2.180 -14.764 63.495 1.00100.85 C
ANISOU 3311 CG ASN A 492 11051 14878 12388 404 356 -764 C
ATOM 3312 OD1 ASN A 492 2.967 -14.337 62.651 1.00104.33 O
ANISOU 3312 OD1 ASN A 492 11569 15170 12902 553 367 -651 O
ATOM 3313 ND2 ASN A 492 1.585 -15.947 63.387 1.00107.40 N
ANISOU 3313 ND2 ASN A 492 11752 15896 13158 153 416 -951 N
ATOM 3314 N GLU A 493 3.477 -11.168 65.198 1.00 78.88 N
ANISOU 3314 N GLU A 493 8737 11479 9755 948 232 -302 N
ATOM 3315 CA GLU A 493 4.132 -10.007 64.611 1.00 67.51 C
ANISOU 3315 CA GLU A 493 7455 9856 8339 1187 270 -162 C
ATOM 3316 C GLU A 493 5.423 -9.620 65.320 1.00 64.70 C
ANISOU 3316 C GLU A 493 7277 9075 8230 1084 262 -30 C
ATOM 3317 O GLU A 493 6.171 -8.791 64.793 1.00 68.12 O
ANISOU 3317 O GLU A 493 7853 9306 8725 1211 322 75 O
ATOM 3318 CB GLU A 493 3.182 -8.803 64.612 1.00 71.79 C
ANISOU 3318 CB GLU A 493 8035 10605 8637 1505 279 -157 C
ATOM 3319 CG GLU A 493 1.903 -8.999 63.807 1.00 91.85 C
ANISOU 3319 CG GLU A 493 10376 13630 10893 1674 280 -292 C
ATOM 3320 CD GLU A 493 0.903 -9.914 64.494 1.00 99.96 C
ANISOU 3320 CD GLU A 493 11188 14960 11832 1471 231 -473 C
ATOM 3321 OE1 GLU A 493 0.946 -10.019 65.740 1.00 99.75 O
ANISOU 3321 OE1 GLU A 493 11209 14791 11900 1304 196 -469 O
ATOM 3322 OE2 GLU A 493 0.087 -10.540 63.784 1.00104.53 O
ANISOU 3322 OE2 GLU A 493 11552 15923 12240 1464 237 -631 O
ATOM 3323 N THR A 494 5.699 -10.181 66.496 1.00 70.71 N
ANISOU 3323 N THR A 494 8038 9711 9119 859 199 -41 N
ATOM 3324 CA THR A 494 6.843 -9.758 67.289 1.00 66.60 C
ANISOU 3324 CA THR A 494 7655 8852 8797 772 172 60 C
ATOM 3325 C THR A 494 7.935 -10.809 67.425 1.00 74.30 C
ANISOU 3325 C THR A 494 8603 9630 9996 549 146 87 C
ATOM 3326 O THR A 494 8.995 -10.498 67.979 1.00 86.36 O
ANISOU 3326 O THR A 494 10211 10912 11689 482 118 159 O
ATOM 3327 CB THR A 494 6.384 -9.333 68.690 1.00 60.15 C
ANISOU 3327 CB THR A 494 6890 8038 7928 741 110 46 C
ATOM 3328 OG1 THR A 494 5.621 -10.391 69.282 1.00 63.11 O
ANISOU 3328 OG1 THR A 494 7144 8594 8239 588 67 -51 O
ATOM 3329 CG2 THR A 494 5.527 -8.082 68.611 1.00 65.07 C
ANISOU 3329 CG2 THR A 494 7584 8788 8350 1000 150 46 C
ATOM 3330 N GLY A 495 7.720 -12.028 66.953 1.00 76.19 N
ANISOU 3330 N GLY A 495 8733 9978 10239 438 161 22 N
ATOM 3331 CA GLY A 495 8.729 -13.054 67.121 1.00 66.45 C
ANISOU 3331 CA GLY A 495 7497 8550 9202 262 149 55 C
ATOM 3332 C GLY A 495 8.191 -14.421 66.764 1.00 67.27 C
ANISOU 3332 C GLY A 495 7512 8787 9262 128 191 -42 C
ATOM 3333 O GLY A 495 7.041 -14.580 66.344 1.00 82.01 O
ANISOU 3333 O GLY A 495 9289 10926 10946 147 227 -155 O
ATOM 3334 N ILE A 496 9.056 -15.414 66.950 1.00 53.85 N
ANISOU 3334 N ILE A 496 5838 6898 7725 -8 196 -5 N
ATOM 3335 CA ILE A 496 8.786 -16.794 66.569 1.00 55.21 C
ANISOU 3335 CA ILE A 496 5976 7114 7889 -154 271 -86 C
ATOM 3336 C ILE A 496 8.675 -17.611 67.851 1.00 46.56 C
ANISOU 3336 C ILE A 496 4952 5932 6807 -307 250 -87 C
ATOM 3337 O ILE A 496 9.688 -17.954 68.470 1.00 63.55 O
ANISOU 3337 O ILE A 496 7185 7856 9106 -329 210 14 O
ATOM 3338 CB ILE A 496 9.877 -17.354 65.648 1.00 58.35 C
ANISOU 3338 CB ILE A 496 6379 7342 8448 -158 327 -36 C
ATOM 3339 CG1 ILE A 496 10.142 -16.399 64.481 1.00 50.90 C
ANISOU 3339 CG1 ILE A 496 5398 6442 7499 5 351 -8 C
ATOM 3340 CG2 ILE A 496 9.496 -18.743 65.149 1.00 56.08 C
ANISOU 3340 CG2 ILE A 496 6077 7100 8130 -310 434 -140 C
ATOM 3341 CD1 ILE A 496 11.318 -16.803 63.607 1.00 46.03 C
ANISOU 3341 CD1 ILE A 496 4787 5650 7053 9 407 48 C
ATOM 3342 N LEU A 497 7.447 -17.921 68.260 1.00 47.14 N
ANISOU 3342 N LEU A 497 4996 6203 6713 -403 283 -205 N
ATOM 3343 CA LEU A 497 7.245 -18.904 69.314 1.00 47.64 C
ANISOU 3343 CA LEU A 497 5153 6180 6768 -575 313 -223 C
ATOM 3344 C LEU A 497 7.467 -20.274 68.681 1.00 77.28 C
ANISOU 3344 C LEU A 497 8961 9816 10583 -717 439 -259 C
ATOM 3345 O LEU A 497 7.268 -20.468 67.479 1.00 75.82 O
ANISOU 3345 O LEU A 497 8698 9735 10376 -737 521 -346 O
ATOM 3346 CB LEU A 497 5.820 -18.830 69.858 1.00 48.32 C
ANISOU 3346 CB LEU A 497 5186 6521 6651 -661 338 -359 C
ATOM 3347 CG LEU A 497 5.570 -17.720 70.878 1.00 47.95 C
ANISOU 3347 CG LEU A 497 5154 6516 6548 -557 226 -307 C
ATOM 3348 CD1 LEU A 497 4.132 -17.755 71.370 1.00 51.15 C
ANISOU 3348 CD1 LEU A 497 5491 7196 6749 -647 269 -457 C
ATOM 3349 CD2 LEU A 497 6.545 -17.831 72.042 1.00 47.60 C
ANISOU 3349 CD2 LEU A 497 5259 6194 6631 -569 150 -165 C
ATOM 3350 N VAL A 498 7.887 -21.231 69.504 1.00 62.78 N
ANISOU 3350 N VAL A 498 7280 7760 8813 -803 464 -191 N
ATOM 3351 CA VAL A 498 8.194 -22.576 69.083 1.00 63.02 C
ANISOU 3351 CA VAL A 498 7419 7610 8914 -907 599 -195 C
ATOM 3352 C VAL A 498 8.001 -23.511 70.256 1.00 74.68 C
ANISOU 3352 C VAL A 498 9081 8966 10329 -1058 685 -200 C
ATOM 3353 O VAL A 498 8.072 -23.074 71.408 1.00 78.78 O
ANISOU 3353 O VAL A 498 9661 9458 10814 -1025 595 -130 O
ATOM 3354 CB VAL A 498 9.590 -22.684 68.418 1.00 54.47 C
ANISOU 3354 CB VAL A 498 6369 6296 8030 -755 543 -38 C
ATOM 3355 CG1 VAL A 498 9.681 -21.846 67.147 1.00 60.39 C
ANISOU 3355 CG1 VAL A 498 7310 6783 8852 -752 562 80 C
ATOM 3356 CG2 VAL A 498 10.679 -22.303 69.404 1.00 49.09 C
ANISOU 3356 CG2 VAL A 498 5622 5629 7400 -759 641 -97 C
ATOM 3357 N LYS A 499 7.687 -24.776 69.980 1.00 71.73 N
ANISOU 3357 N LYS A 499 8813 8515 9926 -1233 878 -292 N
ATOM 3358 CA LYS A 499 7.525 -25.746 71.056 1.00 60.28 C
ANISOU 3358 CA LYS A 499 7594 6897 8414 -1381 1007 -288 C
ATOM 3359 C LYS A 499 8.759 -25.976 71.920 1.00 53.38 C
ANISOU 3359 C LYS A 499 6899 5729 7653 -1207 926 -64 C
ATOM 3360 O LYS A 499 9.871 -26.138 71.407 1.00 53.15 O
ANISOU 3360 O LYS A 499 6877 5550 7766 -1059 894 43 O
ATOM 3361 CB LYS A 499 7.103 -27.049 70.377 1.00 79.47 C
ANISOU 3361 CB LYS A 499 10135 9259 10803 -1607 1263 -434 C
ATOM 3362 CG LYS A 499 7.198 -28.273 71.275 1.00 86.13 C
ANISOU 3362 CG LYS A 499 11301 9805 11618 -1720 1439 -382 C
ATOM 3363 CD LYS A 499 6.791 -29.545 70.551 1.00 89.01 C
ANISOU 3363 CD LYS A 499 11802 10074 11942 -1967 1727 -543 C
ATOM 3364 CE LYS A 499 5.284 -29.619 70.370 1.00 96.61 C
ANISOU 3364 CE LYS A 499 12645 11335 12728 -2276 1861 -821 C
ATOM 3365 NZ LYS A 499 4.865 -30.910 69.754 1.00101.66 N
ANISOU 3365 NZ LYS A 499 13436 11874 13315 -2569 2171 -1009 N
ATOM 3366 N ALA A 500 8.558 -26.014 73.236 1.00 53.91 N
ANISOU 3366 N ALA A 500 7103 5737 7643 -1217 896 0 N
ATOM 3367 CA ALA A 500 9.674 -26.179 74.159 1.00 54.25 C
ANISOU 3367 CA ALA A 500 7300 5557 7755 -1027 797 206 C
ATOM 3368 C ALA A 500 10.300 -27.560 74.023 1.00 65.82 C
ANISOU 3368 C ALA A 500 9012 6732 9263 -1013 970 280 C
ATOM 3369 O ALA A 500 9.604 -28.560 73.826 1.00 78.13 O
ANISOU 3369 O ALA A 500 10737 8207 10743 -1217 1208 174 O
ATOM 3370 CB ALA A 500 9.211 -25.962 75.598 1.00 54.70 C
ANISOU 3370 CB ALA A 500 7466 5630 7687 -1049 743 246 C
ATOM 3371 N GLY A 501 11.624 -27.612 74.135 1.00 61.79 N
ANISOU 3371 N GLY A 501 8530 6076 8871 -770 861 452 N
ATOM 3372 CA GLY A 501 12.316 -28.881 74.197 1.00 69.85 C
ANISOU 3372 CA GLY A 501 9812 6812 9916 -684 1009 557 C
ATOM 3373 C GLY A 501 12.461 -29.618 72.887 1.00 71.73 C
ANISOU 3373 C GLY A 501 10066 6953 10234 -749 1189 481 C
ATOM 3374 O GLY A 501 12.791 -30.808 72.905 1.00 72.54 O
ANISOU 3374 O GLY A 501 10438 6794 10329 -722 1378 539 O
ATOM 3375 N ASP A 502 12.237 -28.961 71.753 1.00 74.94 N
ANISOU 3375 N ASP A 502 10215 7553 10705 -819 1149 358 N
ATOM 3376 CA ASP A 502 12.295 -29.622 70.449 1.00 71.13 C
ANISOU 3376 CA ASP A 502 9734 7009 10283 -900 1322 263 C
ATOM 3377 C ASP A 502 13.425 -29.003 69.647 1.00 72.30 C
ANISOU 3377 C ASP A 502 9677 7196 10599 -690 1175 341 C
ATOM 3378 O ASP A 502 13.246 -27.934 69.034 1.00 73.21 O
ANISOU 3378 O ASP A 502 9537 7537 10744 -696 1052 275 O
ATOM 3379 CB ASP A 502 10.967 -29.488 69.704 1.00 67.63 C
ANISOU 3379 CB ASP A 502 9169 6789 9738 -1180 1432 25 C
ATOM 3380 CG ASP A 502 10.873 -30.404 68.486 1.00 66.26 C
ANISOU 3380 CG ASP A 502 9051 6540 9585 -1318 1657 -104 C
ATOM 3381 OD1 ASP A 502 11.893 -30.596 67.789 1.00 64.20 O
ANISOU 3381 OD1 ASP A 502 8781 6154 9457 -1158 1651 -21 O
ATOM 3382 OD2 ASP A 502 9.770 -30.932 68.222 1.00 65.13 O
ANISOU 3382 OD2 ASP A 502 8952 6477 9317 -1600 1847 -306 O
ATOM 3383 N PRO A 503 14.608 -29.619 69.637 1.00 68.74 N
ANISOU 3383 N PRO A 503 9334 6535 10251 -489 1191 483 N
ATOM 3384 CA PRO A 503 15.713 -29.080 68.826 1.00 69.71 C
ANISOU 3384 CA PRO A 503 9249 6702 10535 -308 1075 539 C
ATOM 3385 C PRO A 503 15.390 -28.968 67.350 1.00 63.42 C
ANISOU 3385 C PRO A 503 8316 6001 9779 -433 1171 394 C
ATOM 3386 O PRO A 503 15.877 -28.048 66.683 1.00 53.98 O
ANISOU 3386 O PRO A 503 6893 4939 8677 -351 1049 397 O
ATOM 3387 CB PRO A 503 16.856 -30.063 69.092 1.00 73.01 C
ANISOU 3387 CB PRO A 503 9849 6873 11019 -87 1134 692 C
ATOM 3388 CG PRO A 503 16.492 -30.748 70.378 1.00 71.52 C
ANISOU 3388 CG PRO A 503 9940 6539 10695 -82 1193 768 C
ATOM 3389 CD PRO A 503 15.002 -30.821 70.388 1.00 67.77 C
ANISOU 3389 CD PRO A 503 9533 6130 10087 -396 1325 602 C
ATOM 3390 N GLY A 504 14.582 -29.883 66.807 1.00 56.25 N
ANISOU 3390 N GLY A 504 7550 5032 8791 -638 1399 258 N
ATOM 3391 CA GLY A 504 14.236 -29.784 65.399 1.00 55.73 C
ANISOU 3391 CA GLY A 504 7345 5093 8736 -756 1484 105 C
ATOM 3392 C GLY A 504 13.328 -28.605 65.108 1.00 80.28 C
ANISOU 3392 C GLY A 504 10214 8525 11763 -849 1362 -11 C
ATOM 3393 O GLY A 504 13.485 -27.923 64.090 1.00 82.82 O
ANISOU 3393 O GLY A 504 10346 8994 12127 -803 1308 -51 O
ATOM 3394 N GLU A 505 12.390 -28.323 66.013 1.00 75.40 N
ANISOU 3394 N GLU A 505 9611 8020 11017 -958 1321 -56 N
ATOM 3395 CA GLU A 505 11.550 -27.145 65.836 1.00 69.23 C
ANISOU 3395 CA GLU A 505 8608 7551 10146 -996 1196 -149 C
ATOM 3396 C GLU A 505 12.358 -25.865 66.006 1.00 64.07 C
ANISOU 3396 C GLU A 505 7803 6947 9595 -773 974 -9 C
ATOM 3397 O GLU A 505 12.130 -24.881 65.293 1.00 56.62 O
ANISOU 3397 O GLU A 505 6679 6200 8632 -730 900 -57 O
ATOM 3398 CB GLU A 505 10.373 -27.183 66.809 1.00 78.12 C
ANISOU 3398 CB GLU A 505 9787 8786 11110 -1160 1218 -235 C
ATOM 3399 CG GLU A 505 9.279 -26.190 66.469 1.00 92.92 C
ANISOU 3399 CG GLU A 505 11439 11015 12853 -1217 1143 -376 C
ATOM 3400 CD GLU A 505 7.912 -26.636 66.942 1.00108.07 C
ANISOU 3400 CD GLU A 505 13388 13087 14587 -1463 1260 -554 C
ATOM 3401 OE1 GLU A 505 7.029 -25.768 67.107 1.00110.33 O
ANISOU 3401 OE1 GLU A 505 13509 13659 14752 -1469 1170 -637 O
ATOM 3402 OE2 GLU A 505 7.720 -27.855 67.144 1.00115.33 O
ANISOU 3402 OE2 GLU A 505 14503 13839 15477 -1650 1460 -618 O
ATOM 3403 N LEU A 506 13.323 -25.863 66.929 1.00 64.58 N
ANISOU 3403 N LEU A 506 7944 6838 9755 -629 876 157 N
ATOM 3404 CA LEU A 506 14.196 -24.703 67.069 1.00 50.24 C
ANISOU 3404 CA LEU A 506 5982 5064 8044 -452 687 264 C
ATOM 3405 C LEU A 506 15.057 -24.509 65.828 1.00 67.41 C
ANISOU 3405 C LEU A 506 8044 7219 10350 -361 709 276 C
ATOM 3406 O LEU A 506 15.321 -23.372 65.420 1.00 70.29 O
ANISOU 3406 O LEU A 506 8259 7690 10756 -290 614 286 O
ATOM 3407 CB LEU A 506 15.072 -24.856 68.315 1.00 56.66 C
ANISOU 3407 CB LEU A 506 6882 5733 8912 -324 582 414 C
ATOM 3408 CG LEU A 506 15.701 -23.587 68.895 1.00 49.99 C
ANISOU 3408 CG LEU A 506 5897 4972 8125 -206 378 487 C
ATOM 3409 CD1 LEU A 506 15.943 -23.761 70.372 1.00 82.79 C
ANISOU 3409 CD1 LEU A 506 10154 9066 12235 -146 278 581 C
ATOM 3410 CD2 LEU A 506 17.003 -23.240 68.213 1.00 49.91 C
ANISOU 3410 CD2 LEU A 506 5756 4925 8282 -73 333 544 C
ATOM 3411 N ALA A 507 15.488 -25.605 65.200 1.00 70.56 N
ANISOU 3411 N ALA A 507 8533 7469 10807 -367 853 272 N
ATOM 3412 CA ALA A 507 16.264 -25.484 63.972 1.00 75.27 C
ANISOU 3412 CA ALA A 507 9028 8050 11520 -291 892 273 C
ATOM 3413 C ALA A 507 15.407 -24.948 62.835 1.00 78.68 C
ANISOU 3413 C ALA A 507 9350 8682 11863 -382 942 138 C
ATOM 3414 O ALA A 507 15.857 -24.100 62.052 1.00 82.00 O
ANISOU 3414 O ALA A 507 9642 9173 12343 -297 899 153 O
ATOM 3415 CB ALA A 507 16.869 -26.838 63.605 1.00 75.78 C
ANISOU 3415 CB ALA A 507 9237 7901 11654 -268 1051 295 C
ATOM 3416 N ASN A 508 14.158 -25.415 62.744 1.00 80.73 N
ANISOU 3416 N ASN A 508 9658 9051 11965 -553 1037 -2 N
ATOM 3417 CA ASN A 508 13.247 -24.882 61.739 1.00 82.94 C
ANISOU 3417 CA ASN A 508 9809 9584 12119 -616 1063 -142 C
ATOM 3418 C ASN A 508 12.980 -23.402 61.980 1.00 69.77 C
ANISOU 3418 C ASN A 508 8013 8093 10403 -510 904 -105 C
ATOM 3419 O ASN A 508 12.877 -22.617 61.030 1.00 59.13 O
ANISOU 3419 O ASN A 508 6559 6891 9018 -434 891 -133 O
ATOM 3420 CB ASN A 508 11.934 -25.669 61.753 1.00 95.47 C
ANISOU 3420 CB ASN A 508 11444 11298 13531 -838 1189 -324 C
ATOM 3421 CG ASN A 508 12.123 -27.131 61.399 1.00105.76 C
ANISOU 3421 CG ASN A 508 12908 12410 14866 -969 1392 -386 C
ATOM 3422 OD1 ASN A 508 13.248 -27.616 61.278 1.00110.53 O
ANISOU 3422 OD1 ASN A 508 13603 12770 15624 -865 1429 -271 O
ATOM 3423 ND2 ASN A 508 11.014 -27.846 61.237 1.00111.76 N
ANISOU 3423 ND2 ASN A 508 13705 13285 15473 -1203 1538 -581 N
ATOM 3424 N ALA A 509 12.901 -22.996 63.249 1.00 67.73 N
ANISOU 3424 N ALA A 509 7788 7809 10137 -491 792 -35 N
ATOM 3425 CA ALA A 509 12.684 -21.588 63.561 1.00 59.50 C
ANISOU 3425 CA ALA A 509 6656 6899 9051 -391 658 2 C
ATOM 3426 C ALA A 509 13.902 -20.741 63.208 1.00 50.78 C
ANISOU 3426 C ALA A 509 5502 5692 8101 -242 595 117 C
ATOM 3427 O ALA A 509 13.757 -19.612 62.725 1.00 50.55 O
ANISOU 3427 O ALA A 509 5408 5770 8030 -155 563 118 O
ATOM 3428 CB ALA A 509 12.324 -21.432 65.036 1.00 59.01 C
ANISOU 3428 CB ALA A 509 6654 6826 8942 -423 566 37 C
ATOM 3429 N ILE A 510 15.109 -21.266 63.431 1.00 47.36 N
ANISOU 3429 N ILE A 510 5103 5057 7836 -205 592 209 N
ATOM 3430 CA ILE A 510 16.308 -20.523 63.047 1.00 59.64 C
ANISOU 3430 CA ILE A 510 6585 6536 9541 -95 553 289 C
ATOM 3431 C ILE A 510 16.382 -20.387 61.531 1.00 66.57 C
ANISOU 3431 C ILE A 510 7413 7459 10423 -67 661 244 C
ATOM 3432 O ILE A 510 16.774 -19.337 61.001 1.00 76.37 O
ANISOU 3432 O ILE A 510 8602 8720 11697 7 654 272 O
ATOM 3433 CB ILE A 510 17.573 -21.196 63.618 1.00 53.10 C
ANISOU 3433 CB ILE A 510 5770 5531 8873 -45 523 381 C
ATOM 3434 CG1 ILE A 510 17.577 -21.143 65.149 1.00 51.14 C
ANISOU 3434 CG1 ILE A 510 5568 5262 8602 -40 396 436 C
ATOM 3435 CG2 ILE A 510 18.833 -20.538 63.063 1.00 49.19 C
ANISOU 3435 CG2 ILE A 510 5167 4987 8534 40 512 430 C
ATOM 3436 CD1 ILE A 510 18.894 -21.572 65.776 1.00 48.89 C
ANISOU 3436 CD1 ILE A 510 5265 4860 8450 58 332 531 C
ATOM 3437 N LEU A 511 15.973 -21.431 60.805 1.00 61.85 N
ANISOU 3437 N LEU A 511 6848 6876 9778 -136 779 166 N
ATOM 3438 CA LEU A 511 15.947 -21.329 59.350 1.00 55.90 C
ANISOU 3438 CA LEU A 511 6049 6194 8999 -111 881 111 C
ATOM 3439 C LEU A 511 14.901 -20.323 58.882 1.00 61.93 C
ANISOU 3439 C LEU A 511 6765 7188 9579 -73 860 49 C
ATOM 3440 O LEU A 511 15.147 -19.557 57.941 1.00 65.41 O
ANISOU 3440 O LEU A 511 7173 7670 10008 25 893 67 O
ATOM 3441 CB LEU A 511 15.691 -22.701 58.729 1.00 60.91 C
ANISOU 3441 CB LEU A 511 6735 6801 9607 -214 1019 18 C
ATOM 3442 CG LEU A 511 16.911 -23.615 58.624 1.00 60.95 C
ANISOU 3442 CG LEU A 511 6791 6572 9794 -184 1088 85 C
ATOM 3443 CD1 LEU A 511 16.511 -24.979 58.088 1.00 70.06 C
ANISOU 3443 CD1 LEU A 511 8041 7681 10899 -303 1251 -21 C
ATOM 3444 CD2 LEU A 511 17.971 -22.975 57.739 1.00 53.98 C
ANISOU 3444 CD2 LEU A 511 5825 5649 9037 -70 1103 145 C
ATOM 3445 N LYS A 512 13.740 -20.287 59.544 1.00 65.72 N
ANISOU 3445 N LYS A 512 7246 7822 9901 -131 812 -19 N
ATOM 3446 CA LYS A 512 12.734 -19.288 59.195 1.00 65.05 C
ANISOU 3446 CA LYS A 512 7108 7983 9624 -50 781 -72 C
ATOM 3447 C LYS A 512 13.229 -17.879 59.495 1.00 60.96 C
ANISOU 3447 C LYS A 512 6609 7400 9153 93 707 44 C
ATOM 3448 O LYS A 512 12.926 -16.940 58.751 1.00 60.03 O
ANISOU 3448 O LYS A 512 6485 7395 8927 226 729 49 O
ATOM 3449 CB LYS A 512 11.430 -19.562 59.951 1.00 70.97 C
ANISOU 3449 CB LYS A 512 7838 8923 10203 -147 747 -178 C
ATOM 3450 CG LYS A 512 10.183 -19.594 59.075 1.00 84.10 C
ANISOU 3450 CG LYS A 512 9406 10918 11630 -151 796 -338 C
ATOM 3451 CD LYS A 512 9.895 -18.251 58.419 1.00 91.70 C
ANISOU 3451 CD LYS A 512 10326 12049 12465 73 757 -302 C
ATOM 3452 CE LYS A 512 8.619 -18.313 57.589 1.00 95.88 C
ANISOU 3452 CE LYS A 512 10735 12967 12727 102 787 -470 C
ATOM 3453 NZ LYS A 512 8.354 -17.031 56.879 1.00 90.30 N
ANISOU 3453 NZ LYS A 512 10017 12424 11870 372 762 -417 N
ATOM 3454 N ALA A 513 14.010 -17.716 60.565 1.00 65.76 N
ANISOU 3454 N ALA A 513 7252 7824 9909 71 633 134 N
ATOM 3455 CA ALA A 513 14.576 -16.406 60.863 1.00 59.81 C
ANISOU 3455 CA ALA A 513 6524 6990 9213 165 586 221 C
ATOM 3456 C ALA A 513 15.588 -15.994 59.804 1.00 46.37 C
ANISOU 3456 C ALA A 513 4820 5177 7621 229 673 270 C
ATOM 3457 O ALA A 513 15.638 -14.825 59.401 1.00 55.02 O
ANISOU 3457 O ALA A 513 5962 6269 8673 328 709 305 O
ATOM 3458 CB ALA A 513 15.219 -16.417 62.250 1.00 53.73 C
ANISOU 3458 CB ALA A 513 5768 6081 8566 106 483 280 C
ATOM 3459 N LEU A 514 16.395 -16.945 59.330 1.00 56.16 N
ANISOU 3459 N LEU A 514 6025 6316 8997 178 728 272 N
ATOM 3460 CA LEU A 514 17.331 -16.623 58.259 1.00 57.02 C
ANISOU 3460 CA LEU A 514 6124 6335 9206 229 828 306 C
ATOM 3461 C LEU A 514 16.592 -16.255 56.980 1.00 51.97 C
ANISOU 3461 C LEU A 514 5512 5839 8394 320 921 266 C
ATOM 3462 O LEU A 514 17.030 -15.374 56.231 1.00 49.67 O
ANISOU 3462 O LEU A 514 5265 5499 8108 406 1001 310 O
ATOM 3463 CB LEU A 514 18.281 -17.794 58.013 1.00 63.37 C
ANISOU 3463 CB LEU A 514 6882 7020 10176 175 873 310 C
ATOM 3464 CG LEU A 514 19.208 -17.611 56.808 1.00 65.94 C
ANISOU 3464 CG LEU A 514 7186 7270 10600 217 995 329 C
ATOM 3465 CD1 LEU A 514 20.153 -16.437 57.035 1.00 59.78 C
ANISOU 3465 CD1 LEU A 514 6393 6388 9932 235 995 387 C
ATOM 3466 CD2 LEU A 514 19.976 -18.884 56.498 1.00 63.02 C
ANISOU 3466 CD2 LEU A 514 6774 6805 10364 185 1051 321 C
ATOM 3467 N GLU A 515 15.458 -16.910 56.724 1.00 65.06 N
ANISOU 3467 N GLU A 515 7148 7688 9883 301 920 174 N
ATOM 3468 CA GLU A 515 14.660 -16.563 55.552 1.00 76.83 C
ANISOU 3468 CA GLU A 515 8641 9380 11170 410 986 121 C
ATOM 3469 C GLU A 515 14.056 -15.170 55.689 1.00 71.59 C
ANISOU 3469 C GLU A 515 8038 8811 10352 570 955 165 C
ATOM 3470 O GLU A 515 13.995 -14.412 54.714 1.00 80.41 O
ANISOU 3470 O GLU A 515 9213 9978 11360 725 1033 196 O
ATOM 3471 CB GLU A 515 13.563 -17.604 55.340 1.00 96.77 C
ANISOU 3471 CB GLU A 515 11099 12131 13539 324 988 -22 C
ATOM 3472 CG GLU A 515 12.736 -17.385 54.089 1.00112.48 C
ANISOU 3472 CG GLU A 515 13053 14389 15295 436 1045 -105 C
ATOM 3473 CD GLU A 515 11.481 -18.235 54.069 1.00126.61 C
ANISOU 3473 CD GLU A 515 14745 16465 16895 329 1033 -282 C
ATOM 3474 OE1 GLU A 515 10.857 -18.399 55.140 1.00127.31 O
ANISOU 3474 OE1 GLU A 515 14810 16609 16954 242 961 -322 O
ATOM 3475 OE2 GLU A 515 11.125 -18.744 52.983 1.00137.49 O
ANISOU 3475 OE2 GLU A 515 16068 18021 18150 318 1106 -394 O
ATOM 3476 N LEU A 516 13.616 -14.815 56.898 1.00 59.86 N
ANISOU 3476 N LEU A 516 6561 7337 8845 549 855 174 N
ATOM 3477 CA LEU A 516 13.073 -13.486 57.148 1.00 50.27 C
ANISOU 3477 CA LEU A 516 5428 6181 7491 708 836 220 C
ATOM 3478 C LEU A 516 14.146 -12.407 57.124 1.00 52.18 C
ANISOU 3478 C LEU A 516 5790 6173 7866 757 901 331 C
ATOM 3479 O LEU A 516 13.820 -11.231 56.927 1.00 60.14 O
ANISOU 3479 O LEU A 516 6918 7188 8745 921 949 380 O
ATOM 3480 CB LEU A 516 12.342 -13.458 58.490 1.00 47.43 C
ANISOU 3480 CB LEU A 516 5046 5895 7080 654 720 190 C
ATOM 3481 CG LEU A 516 10.823 -13.296 58.434 1.00 68.39 C
ANISOU 3481 CG LEU A 516 7652 8874 9461 761 685 102 C
ATOM 3482 CD1 LEU A 516 10.216 -14.359 57.536 1.00 75.81 C
ANISOU 3482 CD1 LEU A 516 8471 10046 10288 709 720 -24 C
ATOM 3483 CD2 LEU A 516 10.221 -13.362 59.828 1.00 47.58 C
ANISOU 3483 CD2 LEU A 516 4993 6282 6802 676 583 70 C
ATOM 3484 N SER A 517 15.414 -12.784 57.305 1.00 52.67 N
ANISOU 3484 N SER A 517 5824 6019 8169 622 917 363 N
ATOM 3485 CA SER A 517 16.498 -11.809 57.361 1.00 64.56 C
ANISOU 3485 CA SER A 517 7416 7301 9813 615 989 435 C
ATOM 3486 C SER A 517 16.663 -11.035 56.061 1.00 79.07 C
ANISOU 3486 C SER A 517 9371 9100 11571 752 1152 479 C
ATOM 3487 O SER A 517 17.240 -9.942 56.073 1.00 89.93 O
ANISOU 3487 O SER A 517 10875 10304 12990 771 1247 532 O
ATOM 3488 CB SER A 517 17.813 -12.506 57.712 1.00 75.33 C
ANISOU 3488 CB SER A 517 8678 8508 11435 454 971 437 C
ATOM 3489 OG SER A 517 18.248 -13.358 56.663 1.00 84.95 O
ANISOU 3489 OG SER A 517 9838 9727 12712 444 1049 422 O
ATOM 3490 N ARG A 518 16.183 -11.572 54.942 1.00 79.32 N
ANISOU 3490 N ARG A 518 9376 9283 11479 840 1200 451 N
ATOM 3491 CA ARG A 518 16.347 -10.917 53.650 1.00 82.79 C
ANISOU 3491 CA ARG A 518 9938 9695 11823 988 1359 499 C
ATOM 3492 C ARG A 518 15.358 -9.778 53.428 1.00 82.13 C
ANISOU 3492 C ARG A 518 10014 9716 11474 1229 1396 543 C
ATOM 3493 O ARG A 518 15.427 -9.116 52.387 1.00 84.86 O
ANISOU 3493 O ARG A 518 10507 10033 11704 1394 1540 602 O
ATOM 3494 CB ARG A 518 16.243 -11.955 52.530 1.00 85.26 C
ANISOU 3494 CB ARG A 518 10159 10146 12092 993 1394 443 C
ATOM 3495 CG ARG A 518 17.339 -13.006 52.622 1.00 85.89 C
ANISOU 3495 CG ARG A 518 10118 10084 12431 795 1396 416 C
ATOM 3496 CD ARG A 518 17.296 -14.014 51.489 1.00 89.86 C
ANISOU 3496 CD ARG A 518 10556 10691 12896 791 1457 355 C
ATOM 3497 NE ARG A 518 18.446 -14.912 51.552 1.00 88.87 N
ANISOU 3497 NE ARG A 518 10344 10401 13022 639 1482 345 N
ATOM 3498 CZ ARG A 518 18.497 -16.009 52.301 1.00 78.75 C
ANISOU 3498 CZ ARG A 518 8962 9112 11847 512 1393 297 C
ATOM 3499 NH1 ARG A 518 17.457 -16.352 53.048 1.00 77.04 N
ANISOU 3499 NH1 ARG A 518 8719 9037 11515 486 1280 245 N
ATOM 3500 NH2 ARG A 518 19.589 -16.763 52.301 1.00 77.09 N
ANISOU 3500 NH2 ARG A 518 8689 8753 11849 425 1428 302 N
ATOM 3501 N SER A 519 14.428 -9.565 54.355 1.00 77.65 N
ANISOU 3501 N SER A 519 9431 9278 10795 1273 1279 520 N
ATOM 3502 CA SER A 519 13.558 -8.400 54.370 1.00 78.83 C
ANISOU 3502 CA SER A 519 9741 9503 10708 1518 1311 569 C
ATOM 3503 C SER A 519 14.195 -7.279 55.198 1.00 89.11 C
ANISOU 3503 C SER A 519 11219 10514 12124 1473 1375 639 C
ATOM 3504 O SER A 519 15.239 -7.453 55.831 1.00 89.87 O
ANISOU 3504 O SER A 519 11270 10405 12473 1241 1365 629 O
ATOM 3505 CB SER A 519 12.178 -8.779 54.913 1.00 79.69 C
ANISOU 3505 CB SER A 519 9722 9932 10623 1589 1161 488 C
ATOM 3506 OG SER A 519 11.593 -9.811 54.131 1.00 75.22 O
ANISOU 3506 OG SER A 519 8990 9647 9944 1593 1122 392 O
ATOM 3507 N ASP A 520 13.530 -6.130 55.211 1.00 99.14 N
ANISOU 3507 N ASP A 520 12696 11781 13191 1709 1450 702 N
ATOM 3508 CA ASP A 520 14.134 -4.956 55.884 1.00110.41 C
ANISOU 3508 CA ASP A 520 14334 12916 14700 1668 1549 756 C
ATOM 3509 C ASP A 520 14.315 -5.192 57.373 1.00117.06 C
ANISOU 3509 C ASP A 520 15065 13735 15678 1467 1396 696 C
ATOM 3510 O ASP A 520 15.266 -4.597 57.902 1.00125.77 O
ANISOU 3510 O ASP A 520 16252 14588 16946 1300 1449 698 O
ATOM 3511 CB ASP A 520 13.336 -3.676 55.689 1.00111.84 C
ANISOU 3511 CB ASP A 520 14789 13103 14603 2001 1672 840 C
ATOM 3512 CG ASP A 520 14.142 -2.490 56.156 1.00116.00 C
ANISOU 3512 CG ASP A 520 15605 13268 15202 1960 1853 898 C
ATOM 3513 OD1 ASP A 520 15.365 -2.631 56.233 1.00113.62 O
ANISOU 3513 OD1 ASP A 520 15287 12724 15158 1673 1914 870 O
ATOM 3514 OD2 ASP A 520 13.542 -1.456 56.446 1.00122.22 O
ANISOU 3514 OD2 ASP A 520 16637 14023 15777 2216 1946 963 O
ATOM 3515 N LEU A 521 13.291 -5.764 58.021 1.00 92.46 N
ANISOU 3515 N LEU A 521 11766 10886 12479 1475 1216 632 N
ATOM 3516 CA LEU A 521 13.221 -6.189 59.452 1.00 73.70 C
ANISOU 3516 CA LEU A 521 9267 8516 10219 1282 1061 574 C
ATOM 3517 C LEU A 521 13.012 -5.022 60.414 1.00 73.85 C
ANISOU 3517 C LEU A 521 9452 8417 10190 1322 1076 594 C
ATOM 3518 O LEU A 521 12.809 -5.293 61.576 1.00 72.87 O
ANISOU 3518 O LEU A 521 9239 8350 10099 1212 940 546 O
ATOM 3519 CB LEU A 521 14.467 -6.968 59.880 1.00 62.78 C
ANISOU 3519 CB LEU A 521 7760 6968 9127 1000 1024 549 C
ATOM 3520 CG LEU A 521 14.594 -8.402 59.393 1.00 55.47 C
ANISOU 3520 CG LEU A 521 6625 6171 8279 900 947 502 C
ATOM 3521 CD1 LEU A 521 15.616 -9.131 60.229 1.00 53.52 C
ANISOU 3521 CD1 LEU A 521 6264 5775 8295 664 886 485 C
ATOM 3522 CD2 LEU A 521 13.263 -9.108 59.473 1.00 53.64 C
ANISOU 3522 CD2 LEU A 521 6276 6219 7887 942 822 437 C
ATOM 3523 N SER A 522 13.024 -3.780 59.957 1.00 80.53 N
ANISOU 3523 N SER A 522 10560 9085 10952 1474 1254 664 N
ATOM 3524 CA SER A 522 12.861 -2.639 60.884 1.00 83.37 C
ANISOU 3524 CA SER A 522 11109 9293 11276 1493 1297 674 C
ATOM 3525 C SER A 522 11.467 -2.706 61.484 1.00 75.88 C
ANISOU 3525 C SER A 522 10126 8594 10110 1677 1180 653 C
ATOM 3526 O SER A 522 11.282 -2.222 62.590 1.00 75.04 O
ANISOU 3526 O SER A 522 10063 8431 10019 1607 1130 624 O
ATOM 3527 CB SER A 522 13.122 -1.337 60.212 1.00 88.57 C
ANISOU 3527 CB SER A 522 12103 9692 11858 1642 1552 756 C
ATOM 3528 OG SER A 522 12.741 -1.405 58.852 1.00 93.19 O
ANISOU 3528 OG SER A 522 12777 10421 12211 1963 1633 827 O
ATOM 3529 N LYS A 523 10.513 -3.224 60.725 1.00 76.71 N
ANISOU 3529 N LYS A 523 10139 9002 10005 1905 1139 652 N
ATOM 3530 CA LYS A 523 9.162 -3.259 61.272 1.00 70.29 C
ANISOU 3530 CA LYS A 523 9245 8482 8981 2069 1027 607 C
ATOM 3531 C LYS A 523 9.074 -4.237 62.436 1.00 77.88 C
ANISOU 3531 C LYS A 523 9978 9540 10072 1798 842 512 C
ATOM 3532 O LYS A 523 8.397 -3.968 63.436 1.00 80.68 O
ANISOU 3532 O LYS A 523 10334 9972 10347 1821 774 478 O
ATOM 3533 CB LYS A 523 8.162 -3.639 60.179 1.00 68.97 C
ANISOU 3533 CB LYS A 523 8968 8674 8565 2330 1009 591 C
ATOM 3534 CG LYS A 523 8.326 -2.880 58.870 1.00 84.82 C
ANISOU 3534 CG LYS A 523 11189 10606 10435 2607 1187 694 C
ATOM 3535 CD LYS A 523 7.861 -1.441 58.979 1.00 92.77 C
ANISOU 3535 CD LYS A 523 12503 11505 11239 2928 1322 786 C
ATOM 3536 CE LYS A 523 7.859 -0.779 57.613 1.00 93.46 C
ANISOU 3536 CE LYS A 523 12813 11564 11134 3255 1501 897 C
ATOM 3537 NZ LYS A 523 7.286 0.592 57.672 1.00 93.53 N
ANISOU 3537 NZ LYS A 523 13151 11483 10904 3628 1647 998 N
ATOM 3538 N PHE A 524 9.790 -5.363 62.341 1.00 81.15 N
ANISOU 3538 N PHE A 524 10218 9933 10684 1549 775 474 N
ATOM 3539 CA PHE A 524 9.808 -6.318 63.444 1.00 64.00 C
ANISOU 3539 CA PHE A 524 7872 7812 8632 1305 622 403 C
ATOM 3540 C PHE A 524 10.417 -5.823 64.747 1.00 67.15 C
ANISOU 3540 C PHE A 524 8371 7968 9175 1153 602 417 C
ATOM 3541 O PHE A 524 9.884 -6.095 65.828 1.00 76.43 O
ANISOU 3541 O PHE A 524 9490 9216 10335 1069 492 372 O
ATOM 3542 CB PHE A 524 10.490 -7.616 63.011 1.00 55.96 C
ANISOU 3542 CB PHE A 524 6687 6791 7782 1109 582 374 C
ATOM 3543 CG PHE A 524 9.558 -8.609 62.381 1.00 65.73 C
ANISOU 3543 CG PHE A 524 7758 8336 8882 1148 541 297 C
ATOM 3544 CD1 PHE A 524 9.096 -9.703 63.098 1.00 74.00 C
ANISOU 3544 CD1 PHE A 524 8652 9521 9942 977 438 212 C
ATOM 3545 CD2 PHE A 524 9.136 -8.446 61.074 1.00 71.35 C
ANISOU 3545 CD2 PHE A 524 8473 9203 9434 1346 621 300 C
ATOM 3546 CE1 PHE A 524 8.232 -10.615 62.518 1.00 74.02 C
ANISOU 3546 CE1 PHE A 524 8504 9807 9813 971 426 111 C
ATOM 3547 CE2 PHE A 524 8.275 -9.352 60.489 1.00 73.41 C
ANISOU 3547 CE2 PHE A 524 8560 9778 9553 1358 586 199 C
ATOM 3548 CZ PHE A 524 7.821 -10.438 61.211 1.00 74.64 C
ANISOU 3548 CZ PHE A 524 8558 10066 9734 1154 495 94 C
ATOM 3549 N ARG A 525 11.490 -5.061 64.621 1.00 61.40 N
ANISOU 3549 N ARG A 525 7793 6963 8575 1106 716 467 N
ATOM 3550 CA ARG A 525 12.176 -4.495 65.794 1.00 50.34 C
ANISOU 3550 CA ARG A 525 6474 5355 7299 939 704 451 C
ATOM 3551 C ARG A 525 11.288 -3.446 66.454 1.00 63.82 C
ANISOU 3551 C ARG A 525 8344 7073 8832 1083 728 450 C
ATOM 3552 O ARG A 525 11.155 -3.454 67.657 1.00 72.54 O
ANISOU 3552 O ARG A 525 9423 8173 9963 962 629 405 O
ATOM 3553 CB ARG A 525 13.508 -3.958 65.295 1.00 51.84 C
ANISOU 3553 CB ARG A 525 6785 5265 7648 837 852 476 C
ATOM 3554 CG ARG A 525 14.205 -4.943 64.375 1.00 50.92 C
ANISOU 3554 CG ARG A 525 6571 5135 7640 802 903 499 C
ATOM 3555 CD ARG A 525 15.693 -4.755 64.486 1.00 71.98 C
ANISOU 3555 CD ARG A 525 8981 7920 10449 635 740 460 C
ATOM 3556 NE ARG A 525 16.430 -5.992 64.446 1.00 74.47 N
ANISOU 3556 NE ARG A 525 9216 8082 10996 413 728 434 N
ATOM 3557 CZ ARG A 525 17.080 -6.404 63.391 1.00 72.25 C
ANISOU 3557 CZ ARG A 525 8877 7723 10853 351 807 443 C
ATOM 3558 NH1 ARG A 525 17.084 -5.671 62.300 1.00 77.05 N
ANISOU 3558 NH1 ARG A 525 9517 8369 11389 489 907 484 N
ATOM 3559 NH2 ARG A 525 17.739 -7.535 63.426 1.00 74.51 N
ANISOU 3559 NH2 ARG A 525 9058 7915 11336 159 785 403 N
ATOM 3560 N GLU A 526 10.657 -2.607 65.663 1.00 67.90 N
ANISOU 3560 N GLU A 526 9036 7610 9152 1364 860 501 N
ATOM 3561 CA GLU A 526 9.795 -1.556 66.193 1.00 79.36 C
ANISOU 3561 CA GLU A 526 10652 9080 10419 1544 895 504 C
ATOM 3562 C GLU A 526 8.600 -2.240 66.846 1.00 76.82 C
ANISOU 3562 C GLU A 526 10141 9082 9965 1594 729 445 C
ATOM 3563 O GLU A 526 8.119 -1.775 67.888 1.00 81.45 O
ANISOU 3563 O GLU A 526 10789 9673 10485 1604 696 415 O
ATOM 3564 CB GLU A 526 9.342 -0.502 65.186 1.00102.49 C
ANISOU 3564 CB GLU A 526 13832 11961 13148 1882 1086 588 C
ATOM 3565 CG GLU A 526 10.458 0.456 64.801 1.00121.69 C
ANISOU 3565 CG GLU A 526 16535 14011 15691 1815 1301 638 C
ATOM 3566 CD GLU A 526 9.954 1.729 64.148 1.00140.97 C
ANISOU 3566 CD GLU A 526 19322 16333 17908 2163 1524 731 C
ATOM 3567 OE1 GLU A 526 8.827 1.722 63.609 1.00148.57 O
ANISOU 3567 OE1 GLU A 526 20269 17559 18623 2503 1501 772 O
ATOM 3568 OE2 GLU A 526 10.689 2.740 64.181 1.00146.38 O
ANISOU 3568 OE2 GLU A 526 20300 16666 18653 2098 1731 755 O
ATOM 3569 N ASN A 527 8.115 -3.348 66.272 1.00 67.28 N
ANISOU 3569 N ASN A 527 8705 8143 8715 1604 638 412 N
ATOM 3570 CA ASN A 527 7.042 -4.091 66.926 1.00 58.77 C
ANISOU 3570 CA ASN A 527 7436 7368 7526 1588 501 329 C
ATOM 3571 C ASN A 527 7.513 -4.692 68.245 1.00 58.37 C
ANISOU 3571 C ASN A 527 7308 7227 7645 1291 382 285 C
ATOM 3572 O ASN A 527 6.781 -4.668 69.242 1.00 58.20 O
ANISOU 3572 O ASN A 527 7261 7319 7533 1281 313 236 O
ATOM 3573 CB ASN A 527 6.515 -5.182 65.995 1.00 60.00 C
ANISOU 3573 CB ASN A 527 7374 7813 7610 1612 457 279 C
ATOM 3574 CG ASN A 527 5.515 -4.657 64.984 1.00 52.41 C
ANISOU 3574 CG ASN A 527 6429 7106 6378 1959 525 285 C
ATOM 3575 OD1 ASN A 527 4.807 -3.686 65.242 1.00 53.64 O
ANISOU 3575 OD1 ASN A 527 6706 7321 6352 2203 567 306 O
ATOM 3576 ND2 ASN A 527 5.442 -5.309 63.830 1.00 52.47 N
ANISOU 3576 ND2 ASN A 527 6314 7281 6342 2000 536 264 N
ATOM 3577 N CYS A 528 8.746 -5.206 68.278 1.00 52.05 N
ANISOU 3577 N CYS A 528 6473 6229 7075 1065 359 303 N
ATOM 3578 CA CYS A 528 9.293 -5.715 69.531 1.00 48.63 C
ANISOU 3578 CA CYS A 528 5982 5711 6784 821 244 274 C
ATOM 3579 C CYS A 528 9.430 -4.602 70.559 1.00 64.48 C
ANISOU 3579 C CYS A 528 8156 7566 8779 810 261 270 C
ATOM 3580 O CYS A 528 9.105 -4.790 71.739 1.00 71.79 O
ANISOU 3580 O CYS A 528 9053 8545 9678 719 164 229 O
ATOM 3581 CB CYS A 528 10.651 -6.372 69.285 1.00 64.31 C
ANISOU 3581 CB CYS A 528 7898 7535 9002 632 224 296 C
ATOM 3582 SG CYS A 528 10.615 -7.802 68.184 1.00 69.34 S
ANISOU 3582 SG CYS A 528 8356 8314 9676 609 212 290 S
ATOM 3583 N LYS A 529 9.871 -3.421 70.117 1.00 67.57 N
ANISOU 3583 N LYS A 529 8743 7759 9173 900 403 308 N
ATOM 3584 CA LYS A 529 10.015 -2.297 71.038 1.00 65.25 C
ANISOU 3584 CA LYS A 529 8638 7294 8861 875 453 289 C
ATOM 3585 C LYS A 529 8.672 -1.912 71.639 1.00 55.92 C
ANISOU 3585 C LYS A 529 7507 6278 7462 1054 435 267 C
ATOM 3586 O LYS A 529 8.534 -1.791 72.864 1.00 56.87 O
ANISOU 3586 O LYS A 529 7642 6393 7573 950 361 220 O
ATOM 3587 CB LYS A 529 10.622 -1.092 70.320 1.00 78.72 C
ANISOU 3587 CB LYS A 529 10584 8741 10584 950 659 328 C
ATOM 3588 CG LYS A 529 12.071 -1.228 69.905 1.00 85.40 C
ANISOU 3588 CG LYS A 529 11400 9395 11653 736 706 324 C
ATOM 3589 CD LYS A 529 12.480 -0.015 69.079 1.00 82.36 C
ANISOU 3589 CD LYS A 529 11287 8759 11248 827 952 363 C
ATOM 3590 CE LYS A 529 13.936 -0.074 68.654 1.00 80.14 C
ANISOU 3590 CE LYS A 529 10970 8294 11185 593 1025 338 C
ATOM 3591 NZ LYS A 529 14.869 -0.001 69.809 1.00 75.87 N
ANISOU 3591 NZ LYS A 529 10360 7670 10798 292 952 236 N
ATOM 3592 N LYS A 530 7.665 -1.713 70.785 1.00 53.99 N
ANISOU 3592 N LYS A 530 7281 6206 7028 1335 500 297 N
ATOM 3593 CA LYS A 530 6.370 -1.267 71.281 1.00 63.51 C
ANISOU 3593 CA LYS A 530 8524 7599 8009 1542 495 271 C
ATOM 3594 C LYS A 530 5.696 -2.329 72.141 1.00 67.32 C
ANISOU 3594 C LYS A 530 8778 8336 8465 1409 330 194 C
ATOM 3595 O LYS A 530 5.027 -1.988 73.122 1.00 68.99 O
ANISOU 3595 O LYS A 530 9025 8616 8572 1438 302 151 O
ATOM 3596 CB LYS A 530 5.475 -0.851 70.114 1.00 74.25 C
ANISOU 3596 CB LYS A 530 9926 9136 9151 1903 593 313 C
ATOM 3597 CG LYS A 530 5.856 0.502 69.516 1.00 87.31 C
ANISOU 3597 CG LYS A 530 11903 10515 10756 2107 799 400 C
ATOM 3598 CD LYS A 530 4.795 1.017 68.554 1.00 97.11 C
ANISOU 3598 CD LYS A 530 13212 11964 11719 2538 888 451 C
ATOM 3599 CE LYS A 530 5.165 2.393 68.010 1.00101.57 C
ANISOU 3599 CE LYS A 530 14161 12213 12217 2762 1125 553 C
ATOM 3600 NZ LYS A 530 4.136 2.958 67.089 1.00103.49 N
ANISOU 3600 NZ LYS A 530 14503 12660 12157 3243 1218 622 N
ATOM 3601 N ARG A 531 5.907 -3.614 71.835 1.00 76.33 N
ANISOU 3601 N ARG A 531 9708 9592 9702 1247 239 172 N
ATOM 3602 CA ARG A 531 5.326 -4.672 72.657 1.00 50.10 C
ANISOU 3602 CA ARG A 531 6207 6470 6357 1092 116 100 C
ATOM 3603 C ARG A 531 5.967 -4.710 74.040 1.00 69.39 C
ANISOU 3603 C ARG A 531 8705 8739 8919 870 36 91 C
ATOM 3604 O ARG A 531 5.268 -4.768 75.064 1.00 49.84 O
ANISOU 3604 O ARG A 531 6216 6373 6347 839 -16 41 O
ATOM 3605 CB ARG A 531 5.488 -6.019 71.951 1.00 49.20 C
ANISOU 3605 CB ARG A 531 5904 6468 6320 968 73 81 C
ATOM 3606 CG ARG A 531 4.865 -7.200 72.678 1.00 80.16 C
ANISOU 3606 CG ARG A 531 9671 10576 10208 795 -12 2 C
ATOM 3607 CD ARG A 531 3.346 -7.112 72.701 1.00 67.88 C
ANISOU 3607 CD ARG A 531 8022 9359 8411 938 5 -90 C
ATOM 3608 NE ARG A 531 2.741 -8.349 73.186 1.00 49.35 N
ANISOU 3608 NE ARG A 531 5523 7197 6031 740 -36 -185 N
ATOM 3609 CZ ARG A 531 1.453 -8.489 73.484 1.00 50.18 C
ANISOU 3609 CZ ARG A 531 5514 7612 5941 776 -27 -297 C
ATOM 3610 NH1 ARG A 531 0.619 -7.466 73.356 1.00 67.25 N
ANISOU 3610 NH1 ARG A 531 7682 9952 7917 1038 5 -320 N
ATOM 3611 NH2 ARG A 531 0.997 -9.654 73.918 1.00 80.07 N
ANISOU 3611 NH2 ARG A 531 9185 11527 9710 552 -34 -390 N
ATOM 3612 N ALA A 532 7.304 -4.658 74.091 1.00 57.96 N
ANISOU 3612 N ALA A 532 7310 7042 7669 718 28 131 N
ATOM 3613 CA ALA A 532 7.984 -4.669 75.380 1.00 59.01 C
ANISOU 3613 CA ALA A 532 7478 7045 7897 521 -60 113 C
ATOM 3614 C ALA A 532 7.651 -3.434 76.206 1.00 61.98 C
ANISOU 3614 C ALA A 532 8031 7345 8172 586 -14 84 C
ATOM 3615 O ALA A 532 7.556 -3.522 77.436 1.00 68.30 O
ANISOU 3615 O ALA A 532 8840 8162 8949 475 -97 45 O
ATOM 3616 CB ALA A 532 9.493 -4.780 75.174 1.00 61.65 C
ANISOU 3616 CB ALA A 532 7803 7175 8446 366 -72 140 C
ATOM 3617 N MET A 533 7.461 -2.279 75.560 1.00 61.02 N
ANISOU 3617 N MET A 533 8075 7132 7977 776 131 106 N
ATOM 3618 CA MET A 533 7.078 -1.091 76.315 1.00 65.65 C
ANISOU 3618 CA MET A 533 8863 7628 8453 857 203 78 C
ATOM 3619 C MET A 533 5.637 -1.183 76.802 1.00 64.62 C
ANISOU 3619 C MET A 533 8685 7751 8114 1013 171 43 C
ATOM 3620 O MET A 533 5.321 -0.729 77.908 1.00 66.38 O
ANISOU 3620 O MET A 533 8994 7959 8268 983 155 -2 O
ATOM 3621 CB MET A 533 7.290 0.169 75.474 1.00 74.20 C
ANISOU 3621 CB MET A 533 10182 8506 9503 1034 400 120 C
ATOM 3622 CG MET A 533 8.745 0.439 75.122 1.00 75.20 C
ANISOU 3622 CG MET A 533 10379 8364 9831 844 465 127 C
ATOM 3623 SD MET A 533 9.066 2.171 74.750 1.00 93.15 S
ANISOU 3623 SD MET A 533 13029 10305 12058 956 735 139 S
ATOM 3624 CE MET A 533 7.653 2.555 73.720 1.00 90.50 C
ANISOU 3624 CE MET A 533 12792 10128 11467 1411 846 229 C
ATOM 3625 N SER A 534 4.750 -1.776 75.996 1.00 62.73 N
ANISOU 3625 N SER A 534 8298 7771 7768 1168 166 48 N
ATOM 3626 CA SER A 534 3.365 -1.940 76.420 1.00 52.84 C
ANISOU 3626 CA SER A 534 6953 6811 6312 1296 139 -10 C
ATOM 3627 C SER A 534 3.251 -2.898 77.594 1.00 59.42 C
ANISOU 3627 C SER A 534 7662 7734 7182 1048 11 -69 C
ATOM 3628 O SER A 534 2.334 -2.767 78.414 1.00 55.39 O
ANISOU 3628 O SER A 534 7143 7376 6528 1089 -1 -127 O
ATOM 3629 CB SER A 534 2.511 -2.441 75.256 1.00 63.55 C
ANISOU 3629 CB SER A 534 8139 8463 7543 1481 157 -21 C
ATOM 3630 OG SER A 534 2.755 -3.815 75.005 1.00 59.96 O
ANISOU 3630 OG SER A 534 7479 8107 7194 1267 71 -47 O
ATOM 3631 N PHE A 535 4.173 -3.857 77.700 1.00 67.14 N
ANISOU 3631 N PHE A 535 8556 8616 8337 805 -75 -50 N
ATOM 3632 CA PHE A 535 4.125 -4.771 78.833 1.00 64.26 C
ANISOU 3632 CA PHE A 535 8117 8307 7991 592 -182 -87 C
ATOM 3633 C PHE A 535 4.507 -4.101 80.144 1.00 80.63 C
ANISOU 3633 C PHE A 535 10337 10229 10071 505 -219 -100 C
ATOM 3634 O PHE A 535 4.242 -4.666 81.210 1.00 71.66 O
ANISOU 3634 O PHE A 535 9172 9162 8892 377 -293 -132 O
ATOM 3635 CB PHE A 535 5.020 -5.983 78.576 1.00 61.97 C
ANISOU 3635 CB PHE A 535 7725 7951 7871 402 -252 -50 C
ATOM 3636 CG PHE A 535 4.254 -7.216 78.206 1.00 62.61 C
ANISOU 3636 CG PHE A 535 7644 8252 7892 353 -254 -90 C
ATOM 3637 CD1 PHE A 535 4.018 -7.536 76.880 1.00 66.86 C
ANISOU 3637 CD1 PHE A 535 8078 8901 8424 441 -197 -96 C
ATOM 3638 CD2 PHE A 535 3.737 -8.037 79.189 1.00 49.06 C
ANISOU 3638 CD2 PHE A 535 5892 6635 6112 210 -296 -134 C
ATOM 3639 CE1 PHE A 535 3.296 -8.668 76.545 1.00 75.18 C
ANISOU 3639 CE1 PHE A 535 8982 10167 9414 363 -182 -162 C
ATOM 3640 CE2 PHE A 535 3.014 -9.164 78.859 1.00 67.23 C
ANISOU 3640 CE2 PHE A 535 8066 9125 8355 130 -263 -193 C
ATOM 3641 CZ PHE A 535 2.794 -9.481 77.537 1.00 71.51 C
ANISOU 3641 CZ PHE A 535 8491 9783 8895 195 -206 -216 C
ATOM 3642 N SER A 536 5.112 -2.920 80.095 1.00109.05 N
ANISOU 3642 N SER A 536 14104 13621 13711 561 -154 -84 N
ATOM 3643 CA SER A 536 5.427 -2.178 81.306 1.00104.13 C
ANISOU 3643 CA SER A 536 13626 12863 13074 473 -172 -123 C
ATOM 3644 C SER A 536 4.562 -0.926 81.391 1.00103.99 C
ANISOU 3644 C SER A 536 13777 12842 12891 690 -46 -151 C
ATOM 3645 O SER A 536 3.350 -0.984 81.179 1.00106.17 O
ANISOU 3645 O SER A 536 13996 13338 13007 874 -11 -166 O
ATOM 3646 CB SER A 536 6.909 -1.813 81.336 1.00106.96 C
ANISOU 3646 CB SER A 536 14054 12976 13612 313 -183 -116 C
ATOM 3647 OG SER A 536 7.701 -2.930 80.977 1.00114.50 O
ANISOU 3647 OG SER A 536 14847 13946 14714 182 -278 -77 O
TER 3648 SER A 536
HETATM 3649 C10 NU2 A1501 -7.986 3.454 123.750 1.00101.42 C
ANISOU 3649 C10 NU2 A1501 17450 14463 6622 -1417 190 -2397 C
HETATM 3650 C13 NU2 A1501 -6.549 3.112 123.586 1.00 96.53 C
ANISOU 3650 C13 NU2 A1501 16803 13800 6073 -1486 -83 -2319 C
HETATM 3651 C15 NU2 A1501 -7.835 2.495 126.192 1.00116.19 C
ANISOU 3651 C15 NU2 A1501 19682 16522 7943 -1584 107 -2360 C
HETATM 3652 C17 NU2 A1501 -6.306 3.670 122.139 1.00103.35 C
ANISOU 3652 C17 NU2 A1501 17479 14529 7259 -1405 -77 -2328 C
HETATM 3653 C20 NU2 A1501 -6.709 0.808 127.728 1.00133.36 C
ANISOU 3653 C20 NU2 A1501 22108 18842 9718 -1676 -167 -2137 C
HETATM 3654 C21 NU2 A1501 -7.701 -1.119 123.314 1.00 94.96 C
ANISOU 3654 C21 NU2 A1501 16525 13778 5777 -1541 59 -1774 C
HETATM 3655 C22 NU2 A1501 -5.797 -0.967 124.880 1.00106.75 C
ANISOU 3655 C22 NU2 A1501 18288 15310 6963 -1577 -330 -1763 C
HETATM 3656 C24 NU2 A1501 -5.056 4.239 121.407 1.00102.22 C
ANISOU 3656 C24 NU2 A1501 17261 14261 7319 -1433 -245 -2363 C
HETATM 3657 C26 NU2 A1501 -6.456 -0.636 128.049 1.00136.81 C
ANISOU 3657 C26 NU2 A1501 22637 19326 10017 -1671 -230 -1913 C
HETATM 3658 C28 NU2 A1501 -5.184 4.727 119.939 1.00 91.65 C
ANISOU 3658 C28 NU2 A1501 15763 12786 6275 -1321 -159 -2353 C
HETATM 3659 C11 NU2 A1501 -8.724 2.838 124.957 1.00112.73 C
ANISOU 3659 C11 NU2 A1501 19039 16031 7762 -1477 295 -2382 C
HETATM 3660 C12 NU2 A1501 -8.078 0.062 125.553 1.00111.20 C
ANISOU 3660 C12 NU2 A1501 18940 15940 7370 -1599 121 -2003 C
HETATM 3661 C14 NU2 A1501 -8.604 3.027 122.392 1.00100.25 C
ANISOU 3661 C14 NU2 A1501 17063 14309 6719 -1315 294 -2302 C
HETATM 3662 C16 NU2 A1501 -7.076 -0.241 124.406 1.00105.35 C
ANISOU 3662 C16 NU2 A1501 18017 15114 6898 -1561 -71 -1895 C
HETATM 3663 C18 NU2 A1501 -7.624 3.600 121.428 1.00102.08 C
ANISOU 3663 C18 NU2 A1501 17199 14397 7190 -1281 156 -2308 C
HETATM 3664 C19 NU2 A1501 -9.432 0.403 124.904 1.00108.27 C
ANISOU 3664 C19 NU2 A1501 18423 15593 7120 -1552 391 -2088 C
HETATM 3665 C23 NU2 A1501 -7.362 1.398 129.033 1.00138.60 C
ANISOU 3665 C23 NU2 A1501 22995 19585 10083 -1721 -37 -2287 C
HETATM 3666 C25 NU2 A1501 -7.769 4.086 119.955 1.00 91.47 C
ANISOU 3666 C25 NU2 A1501 15669 12956 6128 -1144 220 -2303 C
HETATM 3667 C27 NU2 A1501 -7.944 -2.575 123.864 1.00 95.93 C
ANISOU 3667 C27 NU2 A1501 16791 13937 5722 -1608 126 -1604 C
HETATM 3668 C29 NU2 A1501 -6.533 4.652 119.214 1.00 90.57 C
ANISOU 3668 C29 NU2 A1501 15519 12677 6215 -1160 65 -2314 C
HETATM 3669 C30 NU2 A1501 -7.229 1.933 131.568 1.00153.02 C
ANISOU 3669 C30 NU2 A1501 25253 21593 11294 -1814 -81 -2462 C
HETATM 3670 C31 NU2 A1501 -5.324 0.907 130.612 1.00145.67 C
ANISOU 3670 C31 NU2 A1501 24125 20663 10560 -1759 -498 -2229 C
HETATM 3671 C32 NU2 A1501 -7.362 -1.620 128.302 1.00136.51 C
ANISOU 3671 C32 NU2 A1501 22699 19302 9867 -1691 -29 -1794 C
HETATM 3672 C33 NU2 A1501 -6.257 2.783 132.398 1.00160.51 C
ANISOU 3672 C33 NU2 A1501 26308 22617 12062 -1874 -283 -2635 C
HETATM 3673 C34 NU2 A1501 -4.371 1.967 131.185 1.00155.73 C
ANISOU 3673 C34 NU2 A1501 25428 22013 11728 -1823 -693 -2440 C
HETATM 3674 C35 NU2 A1501 -5.366 -2.441 128.517 1.00140.61 C
ANISOU 3674 C35 NU2 A1501 23276 19856 10295 -1613 -451 -1599 C
HETATM 3675 C36 NU2 A1501 -4.184 -3.413 128.770 1.00142.75 C
ANISOU 3675 C36 NU2 A1501 23626 20173 10438 -1522 -695 -1405 C
HETATM 3676 N06 NU2 A1501 -7.533 1.093 126.515 1.00119.29 N
ANISOU 3676 N06 NU2 A1501 20122 16981 8223 -1624 15 -2161 N
HETATM 3677 N07 NU2 A1501 -9.727 1.817 124.587 1.00113.18 N
ANISOU 3677 N07 NU2 A1501 18987 16175 7840 -1464 461 -2271 N
HETATM 3678 N08 NU2 A1501 -6.650 1.409 130.342 1.00140.80 N
ANISOU 3678 N08 NU2 A1501 23489 19971 10039 -1768 -201 -2321 N
HETATM 3679 N09 NU2 A1501 -5.240 -1.151 128.202 1.00139.33 N
ANISOU 3679 N09 NU2 A1501 22980 19681 10278 -1640 -489 -1803 N
HETATM 3680 O01 NU2 A1501 -7.456 3.380 126.892 1.00116.65 O
ANISOU 3680 O01 NU2 A1501 19872 16573 7878 -1623 56 -2511 O
HETATM 3681 O02 NU2 A1501 -10.236 -0.434 124.633 1.00100.52 O
ANISOU 3681 O02 NU2 A1501 17376 14669 6149 -1578 551 -2017 O
HETATM 3682 O03 NU2 A1501 -8.463 1.846 128.995 1.00140.90 O
ANISOU 3682 O03 NU2 A1501 23278 19868 10389 -1708 199 -2381 O
HETATM 3683 O04 NU2 A1501 -5.055 3.101 131.707 1.00161.69 O
ANISOU 3683 O04 NU2 A1501 26291 22741 12403 -1887 -520 -2666 O
HETATM 3684 O05 NU2 A1501 -6.688 -2.729 128.575 1.00138.67 O
ANISOU 3684 O05 NU2 A1501 23086 19583 10020 -1664 -153 -1598 O
HETATM 3685 C1 CLR A1502 -14.615 -12.635 127.936 1.00118.86 C
ANISOU 3685 C1 CLR A1502 21475 16625 7059 -2930 2629 -980 C
HETATM 3686 C2 CLR A1502 -14.584 -11.730 129.171 1.00120.70 C
ANISOU 3686 C2 CLR A1502 21852 16964 7045 -2829 2528 -1037 C
HETATM 3687 C3 CLR A1502 -13.198 -11.636 129.762 1.00113.83 C
ANISOU 3687 C3 CLR A1502 21217 15994 6038 -2587 2181 -842 C
HETATM 3688 C4 CLR A1502 -12.206 -11.173 128.712 1.00117.01 C
ANISOU 3688 C4 CLR A1502 21330 16386 6743 -2416 1834 -811 C
HETATM 3689 C5 CLR A1502 -12.260 -12.040 127.473 1.00118.90 C
ANISOU 3689 C5 CLR A1502 21425 16514 7238 -2498 1935 -745 C
HETATM 3690 C6 CLR A1502 -11.176 -12.662 127.031 1.00119.94 C
ANISOU 3690 C6 CLR A1502 21633 16492 7446 -2365 1744 -544 C
HETATM 3691 C7 CLR A1502 -11.106 -13.422 125.746 1.00115.75 C
ANISOU 3691 C7 CLR A1502 20946 15847 7185 -2426 1808 -486 C
HETATM 3692 C8 CLR A1502 -12.310 -13.126 124.859 1.00111.63 C
ANISOU 3692 C8 CLR A1502 20067 15462 6883 -2626 2032 -715 C
HETATM 3693 C9 CLR A1502 -13.605 -13.232 125.686 1.00115.24 C
ANISOU 3693 C9 CLR A1502 20649 16017 7120 -2842 2390 -854 C
HETATM 3694 C10 CLR A1502 -13.638 -12.178 126.830 1.00116.39 C
ANISOU 3694 C10 CLR A1502 20874 16294 7055 -2739 2275 -934 C
HETATM 3695 C11 CLR A1502 -14.854 -13.157 124.790 1.00113.22 C
ANISOU 3695 C11 CLR A1502 20032 15934 7052 -3053 2647 -1087 C
HETATM 3696 C12 CLR A1502 -14.805 -14.090 123.573 1.00108.08 C
ANISOU 3696 C12 CLR A1502 19261 15182 6624 -3163 2740 -1042 C
HETATM 3697 C13 CLR A1502 -13.551 -13.841 122.726 1.00109.24 C
ANISOU 3697 C13 CLR A1502 19271 15230 7003 -2926 2369 -907 C
HETATM 3698 C14 CLR A1502 -12.374 -14.094 123.688 1.00108.52 C
ANISOU 3698 C14 CLR A1502 19574 14954 6704 -2737 2163 -665 C
HETATM 3699 C15 CLR A1502 -11.134 -14.273 122.816 1.00111.21 C
ANISOU 3699 C15 CLR A1502 19830 15168 7257 -2550 1870 -507 C
HETATM 3700 C16 CLR A1502 -11.692 -14.602 121.421 1.00115.51 C
ANISOU 3700 C16 CLR A1502 20062 15739 8088 -2700 2015 -611 C
HETATM 3701 C17 CLR A1502 -13.212 -14.863 121.595 1.00115.51 C
ANISOU 3701 C17 CLR A1502 20022 15867 7998 -2991 2418 -808 C
HETATM 3702 C18 CLR A1502 -13.528 -12.402 122.179 1.00107.85 C
ANISOU 3702 C18 CLR A1502 18698 15256 7023 -2766 2124 -1063 C
HETATM 3703 C19 CLR A1502 -14.065 -10.793 126.310 1.00116.79 C
ANISOU 3703 C19 CLR A1502 20511 16563 7302 -2678 2165 -1166 C
HETATM 3704 C20 CLR A1502 -13.959 -14.847 120.239 1.00111.27 C
ANISOU 3704 C20 CLR A1502 19068 15482 7729 -3133 2538 -994 C
HETATM 3705 C21 CLR A1502 -15.452 -14.546 120.360 1.00115.16 C
ANISOU 3705 C21 CLR A1502 19353 16243 8158 -3348 2831 -1263 C
HETATM 3706 C22 CLR A1502 -13.787 -16.171 119.470 1.00104.28 C
ANISOU 3706 C22 CLR A1502 18282 14400 6939 -3279 2702 -895 C
HETATM 3707 C23 CLR A1502 -12.399 -16.508 118.958 1.00100.41 C
ANISOU 3707 C23 CLR A1502 17883 13686 6581 -3065 2426 -662 C
HETATM 3708 C24 CLR A1502 -12.379 -17.178 117.601 1.00110.68 C
ANISOU 3708 C24 CLR A1502 18998 14929 8127 -3163 2496 -678 C
HETATM 3709 C25 CLR A1502 -12.255 -16.239 116.394 1.00107.07 C
ANISOU 3709 C25 CLR A1502 18061 14658 7963 -3040 2258 -796 C
HETATM 3710 C26 CLR A1502 -13.585 -15.598 116.027 1.00106.91 C
ANISOU 3710 C26 CLR A1502 17674 14960 7987 -3185 2421 -1084 C
HETATM 3711 C27 CLR A1502 -11.644 -16.946 115.193 1.00 98.34 C
ANISOU 3711 C27 CLR A1502 16878 13408 7080 -3031 2211 -707 C
HETATM 3712 O1 CLR A1502 -13.196 -10.724 130.869 1.00115.18 O
ANISOU 3712 O1 CLR A1502 21472 16285 6007 -2503 2080 -926 O
HETATM 3713 C1 PEG A1503 17.000 -0.243 64.380 1.00 76.76 C
ANISOU 3713 C1 PEG A1503 10585 7452 11127 459 1542 444 C
HETATM 3714 O1 PEG A1503 16.723 -0.768 65.686 1.00 59.27 O
ANISOU 3714 O1 PEG A1503 8191 5391 8937 359 1310 384 O
HETATM 3715 C2 PEG A1503 17.036 1.282 64.430 1.00 91.09 C
ANISOU 3715 C2 PEG A1503 12768 8985 12857 485 1799 444 C
HETATM 3716 O2 PEG A1503 18.243 1.713 65.054 1.00 93.59 O
ANISOU 3716 O2 PEG A1503 13076 9127 13357 146 1871 323 O
HETATM 3717 C3 PEG A1503 18.119 3.030 65.588 1.00 92.08 C
ANISOU 3717 C3 PEG A1503 13203 8701 13082 118 2059 285 C
HETATM 3718 C4 PEG A1503 19.485 3.495 66.075 1.00 83.67 C
ANISOU 3718 C4 PEG A1503 12116 7464 12209 -277 2170 127 C
HETATM 3719 O4 PEG A1503 19.461 3.705 67.493 1.00 63.61 O
ANISOU 3719 O4 PEG A1503 9520 4966 9681 -443 2042 14 O
CONECT 577 1161
CONECT 1161 577
CONECT 2126 2132
CONECT 2132 2126 2133
CONECT 2133 2132 2134 2140
CONECT 2134 2133 2135
CONECT 2135 2134 2136
CONECT 2136 2135 2137
CONECT 2137 2136 2138 2139
CONECT 2138 2137
CONECT 2139 2137
CONECT 2140 2133 2141 2142
CONECT 2141 2140
CONECT 2142 2140
CONECT 3649 3650 3659 3661
CONECT 3650 3649 3652
CONECT 3651 3659 3676 3680
CONECT 3652 3650 3656 3663
CONECT 3653 3657 3665 3676
CONECT 3654 3662 3667
CONECT 3655 3662
CONECT 3656 3652 3658
CONECT 3657 3653 3671 3679
CONECT 3658 3656 3668
CONECT 3659 3649 3651 3677
CONECT 3660 3662 3664 3676
CONECT 3661 3649 3663
CONECT 3662 3654 3655 3660
CONECT 3663 3652 3661 3666
CONECT 3664 3660 3677 3681
CONECT 3665 3653 3678 3682
CONECT 3666 3663 3668
CONECT 3667 3654
CONECT 3668 3658 3666
CONECT 3669 3672 3678
CONECT 3670 3673 3678
CONECT 3671 3657 3684
CONECT 3672 3669 3683
CONECT 3673 3670 3683
CONECT 3674 3675 3679 3684
CONECT 3675 3674
CONECT 3676 3651 3653 3660
CONECT 3677 3659 3664
CONECT 3678 3665 3669 3670
CONECT 3679 3657 3674
CONECT 3680 3651
CONECT 3681 3664
CONECT 3682 3665
CONECT 3683 3672 3673
CONECT 3684 3671 3674
CONECT 3685 3686 3694
CONECT 3686 3685 3687
CONECT 3687 3686 3688 3712
CONECT 3688 3687 3689
CONECT 3689 3688 3690 3694
CONECT 3690 3689 3691
CONECT 3691 3690 3692
CONECT 3692 3691 3693 3698
CONECT 3693 3692 3694 3695
CONECT 3694 3685 3689 3693 3703
CONECT 3695 3693 3696
CONECT 3696 3695 3697
CONECT 3697 3696 3698 3701 3702
CONECT 3698 3692 3697 3699
CONECT 3699 3698 3700
CONECT 3700 3699 3701
CONECT 3701 3697 3700 3704
CONECT 3702 3697
CONECT 3703 3694
CONECT 3704 3701 3705 3706
CONECT 3705 3704
CONECT 3706 3704 3707
CONECT 3707 3706 3708
CONECT 3708 3707 3709
CONECT 3709 3708 3710 3711
CONECT 3710 3709
CONECT 3711 3709
CONECT 3712 3687
CONECT 3713 3714 3715
CONECT 3714 3713
CONECT 3715 3713 3716
CONECT 3716 3715 3717
CONECT 3717 3716 3718
CONECT 3718 3717 3719
CONECT 3719 3718
MASTER 336 0 4 19 8 0 6 6 3718 1 85 39
END