HEADER MEMBRANE PROTEIN 16-DEC-19 6TQ4
TITLE CRYSTAL STRUCTURE OF THE OREXIN-1 RECEPTOR IN COMPLEX WITH COMPOUND 16
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OREXIN RECEPTOR TYPE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: OX1R,HYPOCRETIN RECEPTOR TYPE 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: COMPOUND 16 BOUND IN THE ORTHOSTERIC SITE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HCRTR1;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS 7TM, GPCR, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.RAPPAS,A.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL,M.CONGREVE,
AUTHOR 2 R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY,A.JAZAYERI,
AUTHOR 3 F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL,B.G.TEHAN,M.WEIR,
AUTHOR 4 J.A.CHRISTOPHER
REVDAT 4 29-JUL-20 6TQ4 1 COMPND REMARK HETNAM SITE
REVDAT 3 11-MAR-20 6TQ4 1 JRNL
REVDAT 2 29-JAN-20 6TQ4 1 JRNL
REVDAT 1 01-JAN-20 6TQ4 0
JRNL AUTH M.RAPPAS,A.A.E.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL,
JRNL AUTH 2 M.CONGREVE,R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY,
JRNL AUTH 3 A.JAZAYERI,F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL,
JRNL AUTH 4 B.G.TEHAN,M.WEIR,J.A.CHRISTOPHER
JRNL TITL COMPARISON OF OREXIN 1 AND OREXIN 2 LIGAND BINDING MODES
JRNL TITL 2 USING X-RAY CRYSTALLOGRAPHY AND COMPUTATIONAL ANALYSIS.
JRNL REF J.MED.CHEM. V. 63 1528 2020
JRNL REFN ISSN 0022-2623
JRNL PMID 31860301
JRNL DOI 10.1021/ACS.JMEDCHEM.9B01787
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 77.1
REMARK 3 NUMBER OF REFLECTIONS : 38396
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 1896
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 34.6930 - 5.5337 1.00 3404 207 0.2391 0.2377
REMARK 3 2 5.5337 - 4.3951 1.00 3403 175 0.1921 0.2183
REMARK 3 3 4.3951 - 3.8403 1.00 3414 156 0.1843 0.2221
REMARK 3 4 3.8403 - 3.4895 1.00 3341 188 0.1823 0.2256
REMARK 3 5 3.4895 - 3.2396 1.00 3362 196 0.2020 0.2493
REMARK 3 6 3.2396 - 3.0487 1.00 3417 162 0.2141 0.2216
REMARK 3 7 3.0487 - 2.8961 0.99 3353 158 0.2183 0.2418
REMARK 3 8 2.8961 - 2.7701 0.90 3034 170 0.2197 0.2827
REMARK 3 9 2.7701 - 2.6635 0.77 2593 135 0.2283 0.2810
REMARK 3 10 2.6635 - 2.5716 0.64 2161 116 0.2469 0.2612
REMARK 3 11 2.5716 - 2.4913 0.54 1813 88 0.2734 0.2981
REMARK 3 12 2.4913 - 2.4201 0.43 1468 64 0.2594 0.2808
REMARK 3 13 2.4201 - 2.3564 0.30 1011 55 0.2692 0.3281
REMARK 3 14 2.3564 - 2.2990 0.21 726 26 0.2615 0.3449
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.860
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 83.75
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 : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 26:375)
REMARK 3 ORIGIN FOR THE GROUP (A): 37.4729 -4.5263 230.1843
REMARK 3 T TENSOR
REMARK 3 T11: 0.2073 T22: 0.4433
REMARK 3 T33: 0.5893 T12: -0.0152
REMARK 3 T13: -0.0781 T23: -0.1061
REMARK 3 L TENSOR
REMARK 3 L11: 0.2204 L22: 3.8584
REMARK 3 L33: 4.2427 L12: -0.1545
REMARK 3 L13: -1.4037 L23: 2.0349
REMARK 3 S TENSOR
REMARK 3 S11: 0.0478 S12: -0.3641 S13: 0.3711
REMARK 3 S21: 0.2064 S22: 0.3573 S23: -0.6049
REMARK 3 S31: -0.1987 S32: 0.6165 S33: -0.1524
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 45:378)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.1131 -26.6732 205.4664
REMARK 3 T TENSOR
REMARK 3 T11: 0.4561 T22: 0.3616
REMARK 3 T33: 0.2875 T12: 0.0354
REMARK 3 T13: 0.0013 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 2.8897 L22: 5.0721
REMARK 3 L33: 2.5809 L12: -0.2130
REMARK 3 L13: -0.4479 L23: 0.6618
REMARK 3 S TENSOR
REMARK 3 S11: 0.0180 S12: 0.2715 S13: -0.0976
REMARK 3 S21: -0.7334 S22: 0.1254 S23: -0.1154
REMARK 3 S31: 0.1255 S32: 0.0784 S33: -0.0748
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 6TQ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-19.
REMARK 100 THE DEPOSITION ID IS D_1292105888.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 3.0-6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38396
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.290
REMARK 200 RESOLUTION RANGE LOW (A) : 34.693
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 77.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6TO7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRISODIUM CITRATE 50MM SODIUM
REMARK 280 CHLORIDE 50MM LITHIUM SULPHATE 15-34% PEG400, PH 4.8, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 284K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 72.94600
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 ALA A 25
REMARK 465 LEU A 189
REMARK 465 PRO A 190
REMARK 465 GLU A 191
REMARK 465 LEU A 192
REMARK 465 ALA A 193
REMARK 465 ALA A 194
REMARK 465 ARG A 195
REMARK 465 THR A 196
REMARK 465 ARG A 197
REMARK 465 ALA A 198
REMARK 465 GLY A 244
REMARK 465 ARG A 245
REMARK 465 GLN A 246
REMARK 465 ILE A 247
REMARK 465 PRO A 248
REMARK 465 GLY A 249
REMARK 465 THR A 250
REMARK 465 THR A 251
REMARK 465 SER A 252
REMARK 465 ALA A 253
REMARK 465 LEU A 254
REMARK 465 VAL A 255
REMARK 465 ARG A 256
REMARK 465 ASN A 257
REMARK 465 TRP A 258
REMARK 465 LYS A 259
REMARK 465 ARG A 260
REMARK 465 PRO A 261
REMARK 465 SER A 262
REMARK 465 ASP A 263
REMARK 465 GLN A 264
REMARK 465 LEU A 265
REMARK 465 GLY A 266
REMARK 465 ASP A 267
REMARK 465 LEU A 268
REMARK 465 GLU A 269
REMARK 465 GLN A 270
REMARK 465 GLY A 271
REMARK 465 LEU A 272
REMARK 465 SER A 273
REMARK 465 GLY A 274
REMARK 465 GLU A 275
REMARK 465 PRO A 276
REMARK 465 GLN A 277
REMARK 465 PRO A 278
REMARK 465 ARG A 279
REMARK 465 ALA A 280
REMARK 465 ARG A 281
REMARK 465 ALA A 282
REMARK 465 PHE A 283
REMARK 465 LEU A 284
REMARK 465 ALA A 285
REMARK 465 GLU A 286
REMARK 465 TRP A 376
REMARK 465 LEU A 377
REMARK 465 PRO A 378
REMARK 465 GLY A 379
REMARK 465 LEU A 380
REMARK 465 ALA A 381
REMARK 465 ALA A 382
REMARK 465 ALA A 383
REMARK 465 HIS A 384
REMARK 465 HIS A 385
REMARK 465 HIS A 386
REMARK 465 HIS A 387
REMARK 465 HIS A 388
REMARK 465 HIS A 389
REMARK 465 HIS A 390
REMARK 465 HIS A 391
REMARK 465 HIS A 392
REMARK 465 ALA B 25
REMARK 465 ALA B 26
REMARK 465 SER B 27
REMARK 465 GLU B 28
REMARK 465 ASP B 29
REMARK 465 GLU B 30
REMARK 465 PHE B 31
REMARK 465 LEU B 32
REMARK 465 ARG B 33
REMARK 465 TYR B 34
REMARK 465 LEU B 35
REMARK 465 TRP B 36
REMARK 465 ARG B 37
REMARK 465 ASP B 38
REMARK 465 TYR B 39
REMARK 465 LEU B 40
REMARK 465 TYR B 41
REMARK 465 PRO B 42
REMARK 465 LYS B 43
REMARK 465 GLN B 44
REMARK 465 ALA B 253
REMARK 465 LEU B 254
REMARK 465 VAL B 255
REMARK 465 ARG B 256
REMARK 465 ASN B 257
REMARK 465 TRP B 258
REMARK 465 LYS B 259
REMARK 465 ARG B 260
REMARK 465 PRO B 261
REMARK 465 SER B 262
REMARK 465 ASP B 263
REMARK 465 GLN B 264
REMARK 465 LEU B 265
REMARK 465 GLY B 266
REMARK 465 ASP B 267
REMARK 465 LEU B 268
REMARK 465 GLU B 269
REMARK 465 GLN B 270
REMARK 465 GLY B 271
REMARK 465 LEU B 272
REMARK 465 SER B 273
REMARK 465 GLY B 274
REMARK 465 GLU B 275
REMARK 465 PRO B 276
REMARK 465 GLN B 277
REMARK 465 PRO B 278
REMARK 465 ARG B 279
REMARK 465 ALA B 280
REMARK 465 ARG B 281
REMARK 465 ALA B 282
REMARK 465 PHE B 283
REMARK 465 LEU B 284
REMARK 465 ALA B 330
REMARK 465 SER B 331
REMARK 465 ASP B 332
REMARK 465 GLY B 379
REMARK 465 LEU B 380
REMARK 465 ALA B 381
REMARK 465 ALA B 382
REMARK 465 ALA B 383
REMARK 465 HIS B 384
REMARK 465 HIS B 385
REMARK 465 HIS B 386
REMARK 465 HIS B 387
REMARK 465 HIS B 388
REMARK 465 HIS B 389
REMARK 465 HIS B 390
REMARK 465 HIS B 391
REMARK 465 HIS B 392
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 ND2 ASN A 318 O01 NV8 A 401 2.16
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 TYR A 39 -55.25 -138.47
REMARK 500 TYR A 224 -72.88 -132.60
REMARK 500 TYR B 224 -67.92 -138.75
REMARK 500 TRP B 376 -75.48 -93.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 SOG A 408
REMARK 610 SOG A 409
REMARK 610 SOG A 411
REMARK 610 SOG A 412
REMARK 610 SOG B 405
REMARK 610 SOG B 406
REMARK 610 SOG B 407
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 413 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 92 OD1
REMARK 620 2 TYR A 311 OH 121.5
REMARK 620 N 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6TO7 RELATED DB: PDB
REMARK 900 RELATED ID: 6TOD RELATED DB: PDB
REMARK 900 RELATED ID: 6TOS RELATED DB: PDB
REMARK 900 RELATED ID: 6TOT RELATED DB: PDB
REMARK 900 RELATED ID: 6TP6 RELATED DB: PDB
REMARK 900 RELATED ID: 6TP3 RELATED DB: PDB
REMARK 900 RELATED ID: 6TP4 RELATED DB: PDB
DBREF 6TQ4 A 28 380 UNP O43613 OX1R_HUMAN 28 380
DBREF 6TQ4 B 28 380 UNP O43613 OX1R_HUMAN 28 380
SEQADV 6TQ4 ALA A 25 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 ALA A 26 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 SER A 27 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 ALA A 46 UNP O43613 GLU 46 ENGINEERED MUTATION
SEQADV 6TQ4 LEU A 85 UNP O43613 ILE 85 ENGINEERED MUTATION
SEQADV 6TQ4 ALA A 95 UNP O43613 VAL 95 ENGINEERED MUTATION
SEQADV 6TQ4 LEU A 162 UNP O43613 ARG 162 ENGINEERED MUTATION
SEQADV 6TQ4 ALA A 194 UNP O43613 ASN 194 ENGINEERED MUTATION
SEQADV 6TQ4 ALA A 198 UNP O43613 LEU 198 ENGINEERED MUTATION
SEQADV 6TQ4 ALA A 211 UNP O43613 TYR 211 ENGINEERED MUTATION
SEQADV 6TQ4 VAL A 304 UNP O43613 LEU 304 ENGINEERED MUTATION
SEQADV 6TQ4 ALA A 339 UNP O43613 CYS 339 ENGINEERED MUTATION
SEQADV 6TQ4 TRP A 375 UNP O43613 CYS 375 ENGINEERED MUTATION
SEQADV 6TQ4 TRP A 376 UNP O43613 CYS 376 ENGINEERED MUTATION
SEQADV 6TQ4 ALA A 381 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 ALA A 382 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 ALA A 383 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS A 384 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS A 385 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS A 386 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS A 387 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS A 388 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS A 389 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS A 390 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS A 391 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS A 392 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 ALA B 25 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 ALA B 26 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 SER B 27 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 ALA B 46 UNP O43613 GLU 46 ENGINEERED MUTATION
SEQADV 6TQ4 LEU B 85 UNP O43613 ILE 85 ENGINEERED MUTATION
SEQADV 6TQ4 ALA B 95 UNP O43613 VAL 95 ENGINEERED MUTATION
SEQADV 6TQ4 LEU B 162 UNP O43613 ARG 162 ENGINEERED MUTATION
SEQADV 6TQ4 ALA B 194 UNP O43613 ASN 194 ENGINEERED MUTATION
SEQADV 6TQ4 ALA B 198 UNP O43613 LEU 198 ENGINEERED MUTATION
SEQADV 6TQ4 ALA B 211 UNP O43613 TYR 211 ENGINEERED MUTATION
SEQADV 6TQ4 VAL B 304 UNP O43613 LEU 304 ENGINEERED MUTATION
SEQADV 6TQ4 ALA B 339 UNP O43613 CYS 339 ENGINEERED MUTATION
SEQADV 6TQ4 TRP B 375 UNP O43613 CYS 375 ENGINEERED MUTATION
SEQADV 6TQ4 TRP B 376 UNP O43613 CYS 376 ENGINEERED MUTATION
SEQADV 6TQ4 ALA B 381 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 ALA B 382 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 ALA B 383 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS B 384 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS B 385 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS B 386 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS B 387 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS B 388 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS B 389 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS B 390 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS B 391 UNP O43613 EXPRESSION TAG
SEQADV 6TQ4 HIS B 392 UNP O43613 EXPRESSION TAG
SEQRES 1 A 368 ALA ALA SER GLU ASP GLU PHE LEU ARG TYR LEU TRP ARG
SEQRES 2 A 368 ASP TYR LEU TYR PRO LYS GLN TYR ALA TRP VAL LEU ILE
SEQRES 3 A 368 ALA ALA TYR VAL ALA VAL PHE VAL VAL ALA LEU VAL GLY
SEQRES 4 A 368 ASN THR LEU VAL CYS LEU ALA VAL TRP ARG ASN HIS HIS
SEQRES 5 A 368 MET ARG THR VAL THR ASN TYR PHE LEU VAL ASN LEU SER
SEQRES 6 A 368 LEU ALA ASP VAL LEU ALA THR ALA ILE CYS LEU PRO ALA
SEQRES 7 A 368 SER LEU LEU VAL ASP ILE THR GLU SER TRP LEU PHE GLY
SEQRES 8 A 368 HIS ALA LEU CYS LYS VAL ILE PRO TYR LEU GLN ALA VAL
SEQRES 9 A 368 SER VAL SER VAL ALA VAL LEU THR LEU SER PHE ILE ALA
SEQRES 10 A 368 LEU ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU LEU PHE
SEQRES 11 A 368 LYS SER THR ALA ARG ARG ALA LEU GLY SER ILE LEU GLY
SEQRES 12 A 368 ILE TRP ALA VAL SER LEU ALA ILE MET VAL PRO GLN ALA
SEQRES 13 A 368 ALA VAL MET GLU CYS SER SER VAL LEU PRO GLU LEU ALA
SEQRES 14 A 368 ALA ARG THR ARG ALA PHE SER VAL CYS ASP GLU ARG TRP
SEQRES 15 A 368 ALA ASP ASP LEU ALA PRO LYS ILE TYR HIS SER CYS PHE
SEQRES 16 A 368 PHE ILE VAL THR TYR LEU ALA PRO LEU GLY LEU MET ALA
SEQRES 17 A 368 MET ALA TYR PHE GLN ILE PHE ARG LYS LEU TRP GLY ARG
SEQRES 18 A 368 GLN ILE PRO GLY THR THR SER ALA LEU VAL ARG ASN TRP
SEQRES 19 A 368 LYS ARG PRO SER ASP GLN LEU GLY ASP LEU GLU GLN GLY
SEQRES 20 A 368 LEU SER GLY GLU PRO GLN PRO ARG ALA ARG ALA PHE LEU
SEQRES 21 A 368 ALA GLU VAL LYS GLN MET ARG ALA ARG ARG LYS THR ALA
SEQRES 22 A 368 LYS MET LEU MET VAL VAL VAL LEU VAL PHE ALA LEU CYS
SEQRES 23 A 368 TYR LEU PRO ILE SER VAL LEU ASN VAL LEU LYS ARG VAL
SEQRES 24 A 368 PHE GLY MET PHE ARG GLN ALA SER ASP ARG GLU ALA VAL
SEQRES 25 A 368 TYR ALA ALA PHE THR PHE SER HIS TRP LEU VAL TYR ALA
SEQRES 26 A 368 ASN SER ALA ALA ASN PRO ILE ILE TYR ASN PHE LEU SER
SEQRES 27 A 368 GLY LYS PHE ARG GLU GLN PHE LYS ALA ALA PHE SER TRP
SEQRES 28 A 368 TRP LEU PRO GLY LEU ALA ALA ALA HIS HIS HIS HIS HIS
SEQRES 29 A 368 HIS HIS HIS HIS
SEQRES 1 B 368 ALA ALA SER GLU ASP GLU PHE LEU ARG TYR LEU TRP ARG
SEQRES 2 B 368 ASP TYR LEU TYR PRO LYS GLN TYR ALA TRP VAL LEU ILE
SEQRES 3 B 368 ALA ALA TYR VAL ALA VAL PHE VAL VAL ALA LEU VAL GLY
SEQRES 4 B 368 ASN THR LEU VAL CYS LEU ALA VAL TRP ARG ASN HIS HIS
SEQRES 5 B 368 MET ARG THR VAL THR ASN TYR PHE LEU VAL ASN LEU SER
SEQRES 6 B 368 LEU ALA ASP VAL LEU ALA THR ALA ILE CYS LEU PRO ALA
SEQRES 7 B 368 SER LEU LEU VAL ASP ILE THR GLU SER TRP LEU PHE GLY
SEQRES 8 B 368 HIS ALA LEU CYS LYS VAL ILE PRO TYR LEU GLN ALA VAL
SEQRES 9 B 368 SER VAL SER VAL ALA VAL LEU THR LEU SER PHE ILE ALA
SEQRES 10 B 368 LEU ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU LEU PHE
SEQRES 11 B 368 LYS SER THR ALA ARG ARG ALA LEU GLY SER ILE LEU GLY
SEQRES 12 B 368 ILE TRP ALA VAL SER LEU ALA ILE MET VAL PRO GLN ALA
SEQRES 13 B 368 ALA VAL MET GLU CYS SER SER VAL LEU PRO GLU LEU ALA
SEQRES 14 B 368 ALA ARG THR ARG ALA PHE SER VAL CYS ASP GLU ARG TRP
SEQRES 15 B 368 ALA ASP ASP LEU ALA PRO LYS ILE TYR HIS SER CYS PHE
SEQRES 16 B 368 PHE ILE VAL THR TYR LEU ALA PRO LEU GLY LEU MET ALA
SEQRES 17 B 368 MET ALA TYR PHE GLN ILE PHE ARG LYS LEU TRP GLY ARG
SEQRES 18 B 368 GLN ILE PRO GLY THR THR SER ALA LEU VAL ARG ASN TRP
SEQRES 19 B 368 LYS ARG PRO SER ASP GLN LEU GLY ASP LEU GLU GLN GLY
SEQRES 20 B 368 LEU SER GLY GLU PRO GLN PRO ARG ALA ARG ALA PHE LEU
SEQRES 21 B 368 ALA GLU VAL LYS GLN MET ARG ALA ARG ARG LYS THR ALA
SEQRES 22 B 368 LYS MET LEU MET VAL VAL VAL LEU VAL PHE ALA LEU CYS
SEQRES 23 B 368 TYR LEU PRO ILE SER VAL LEU ASN VAL LEU LYS ARG VAL
SEQRES 24 B 368 PHE GLY MET PHE ARG GLN ALA SER ASP ARG GLU ALA VAL
SEQRES 25 B 368 TYR ALA ALA PHE THR PHE SER HIS TRP LEU VAL TYR ALA
SEQRES 26 B 368 ASN SER ALA ALA ASN PRO ILE ILE TYR ASN PHE LEU SER
SEQRES 27 B 368 GLY LYS PHE ARG GLU GLN PHE LYS ALA ALA PHE SER TRP
SEQRES 28 B 368 TRP LEU PRO GLY LEU ALA ALA ALA HIS HIS HIS HIS HIS
SEQRES 29 B 368 HIS HIS HIS HIS
HET NV8 A 401 51
HET SO4 A 402 5
HET SO4 A 403 5
HET PGW A 404 51
HET SOG A 405 20
HET SOG A 406 20
HET SOG A 407 20
HET SOG A 408 13
HET SOG A 409 14
HET SOG A 410 20
HET SOG A 411 5
HET SOG A 412 4
HET NA A 413 1
HET NV8 B 401 51
HET SO4 B 402 5
HET SO4 B 403 5
HET PGW B 404 51
HET SOG B 405 14
HET SOG B 406 13
HET SOG B 407 5
HET SOG B 408 20
HET SOG B 409 20
HETNAM NV8 2-[1-(PHENYLSULFONYL)-1,8-DIAZASPIRO[4.5]DECAN-8-YL]-1,
HETNAM 2 NV8 3-BENZOXAZOLE
HETNAM SO4 SULFATE ION
HETNAM PGW (1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)
HETNAM 2 PGW PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL (9Z)-
HETNAM 3 PGW OCTADEC-9-ENOATE
HETNAM SOG OCTYL 1-THIO-BETA-D-GLUCOPYRANOSIDE
HETNAM NA SODIUM ION
HETSYN PGW 1-PALMITOYL-2-OLEOYL-SN-GLYCERO-3-[PHOSPHO-(1-
HETSYN 2 PGW GLYCEROL)]; PHOSPHATIDYLGLYCEROL
HETSYN SOG 1-S-OCTYL-BETA-D-THIOGLUCOSIDE
FORMUL 3 NV8 2(C21 H23 N3 O3 S)
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 6 PGW 2(C40 H77 O10 P)
FORMUL 7 SOG 13(C14 H28 O5 S)
FORMUL 15 NA NA 1+
FORMUL 25 HOH *42(H2 O)
HELIX 1 AA1 SER A 27 TYR A 39 1 13
HELIX 2 AA2 TYR A 39 ASN A 74 1 36
HELIX 3 AA3 HIS A 75 ARG A 78 5 4
HELIX 4 AA4 THR A 79 GLU A 110 1 32
HELIX 5 AA5 PHE A 114 CYS A 149 1 36
HELIX 6 AA6 THR A 157 MET A 176 1 20
HELIX 7 AA7 MET A 176 VAL A 182 1 7
HELIX 8 AA8 ASP A 209 TYR A 224 1 16
HELIX 9 AA9 TYR A 224 TRP A 243 1 20
HELIX 10 AB1 LYS A 288 VAL A 323 1 36
HELIX 11 AB2 ASP A 332 SER A 362 1 31
HELIX 12 AB3 SER A 362 TRP A 375 1 14
HELIX 13 AB4 ALA B 46 ASN B 74 1 29
HELIX 14 AB5 HIS B 75 ARG B 78 5 4
HELIX 15 AB6 THR B 79 ILE B 98 1 20
HELIX 16 AB7 ILE B 98 GLU B 110 1 13
HELIX 17 AB8 PHE B 114 CYS B 149 1 36
HELIX 18 AB9 THR B 157 MET B 176 1 20
HELIX 19 AC1 MET B 176 VAL B 182 1 7
HELIX 20 AC2 GLU B 191 ARG B 195 5 5
HELIX 21 AC3 ASP B 209 TYR B 224 1 16
HELIX 22 AC4 TYR B 224 GLY B 244 1 21
HELIX 23 AC5 THR B 251 VAL B 323 1 41
HELIX 24 AC6 GLU B 334 SER B 362 1 29
HELIX 25 AC7 SER B 362 TRP B 376 1 15
SHEET 1 AA1 2 MET A 183 SER A 186 0
SHEET 2 AA1 2 VAL A 201 GLU A 204 -1 O ASP A 203 N GLU A 184
SHEET 1 AA2 2 MET B 183 SER B 187 0
SHEET 2 AA2 2 SER B 200 GLU B 204 -1 O ASP B 203 N GLU B 184
SSBOND 1 CYS A 119 CYS A 202 1555 1555 2.04
SSBOND 2 CYS B 119 CYS B 202 1555 1555 2.04
LINK OD1 ASP A 92 NA NA A 413 1555 1555 2.99
LINK OH TYR A 311 NA NA A 413 1555 1555 2.81
CRYST1 59.339 145.892 71.341 90.00 112.33 90.00 P 1 21 1 4
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 0.016852 0.000000 0.006923 0.00000
SCALE2 0.000000 0.006854 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015154 0.00000
ATOM 1 N ALA A 26 9.668 20.415 265.136 1.00156.37 N
ANISOU 1 N ALA A 26 24733 14676 20004 -474 6598 -2150 N
ATOM 2 CA ALA A 26 8.919 19.282 265.671 1.00158.90 C
ANISOU 2 CA ALA A 26 24961 15019 20395 -600 6759 -2237 C
ATOM 3 C ALA A 26 9.225 18.000 264.900 1.00157.98 C
ANISOU 3 C ALA A 26 24562 15124 20341 -597 6502 -2280 C
ATOM 4 O ALA A 26 9.822 17.071 265.444 1.00160.50 O
ANISOU 4 O ALA A 26 25091 15452 20442 -805 6390 -2261 O
ATOM 5 CB ALA A 26 7.432 19.575 265.639 1.00162.65 C
ANISOU 5 CB ALA A 26 25158 15462 21179 -446 7089 -2340 C
ATOM 6 N SER A 27 8.809 17.954 263.633 1.00156.25 N
ANISOU 6 N SER A 27 23877 15088 20402 -342 6402 -2334 N
ATOM 7 CA SER A 27 9.046 16.792 262.774 1.00151.25 C
ANISOU 7 CA SER A 27 22941 14676 19850 -319 6169 -2376 C
ATOM 8 C SER A 27 10.449 16.862 262.163 1.00149.08 C
ANISOU 8 C SER A 27 22769 14468 19407 -312 5799 -2281 C
ATOM 9 O SER A 27 10.642 16.873 260.949 1.00144.98 O
ANISOU 9 O SER A 27 21945 14105 19035 -117 5601 -2277 O
ATOM 10 CB SER A 27 7.975 16.707 261.694 1.00148.54 C
ANISOU 10 CB SER A 27 22042 14526 19870 -45 6211 -2482 C
ATOM 11 OG SER A 27 6.722 16.346 262.243 1.00148.21 O
ANISOU 11 OG SER A 27 21849 14467 19995 -100 6523 -2613 O
ATOM 12 N GLU A 28 11.448 16.913 263.045 1.00150.46 N
ANISOU 12 N GLU A 28 23380 14526 19261 -530 5700 -2212 N
ATOM 13 CA GLU A 28 12.826 17.005 262.581 1.00146.03 C
ANISOU 13 CA GLU A 28 22921 14028 18535 -557 5347 -2152 C
ATOM 14 C GLU A 28 13.264 15.750 261.832 1.00141.18 C
ANISOU 14 C GLU A 28 22077 13609 17957 -551 5084 -2180 C
ATOM 15 O GLU A 28 14.083 15.841 260.911 1.00141.54 O
ANISOU 15 O GLU A 28 22002 13755 18021 -475 4818 -2156 O
ATOM 16 CB GLU A 28 13.762 17.268 263.760 1.00148.34 C
ANISOU 16 CB GLU A 28 23698 14189 18477 -787 5275 -2105 C
ATOM 17 CG GLU A 28 15.213 17.448 263.350 1.00148.62 C
ANISOU 17 CG GLU A 28 23823 14293 18354 -837 4910 -2080 C
ATOM 18 CD GLU A 28 16.036 18.144 264.417 1.00152.89 C
ANISOU 18 CD GLU A 28 24799 14702 18592 -1024 4867 -2056 C
ATOM 19 OE1 GLU A 28 15.626 18.119 265.598 1.00155.59 O
ANISOU 19 OE1 GLU A 28 25420 14913 18783 -1140 5063 -2045 O
ATOM 20 OE2 GLU A 28 17.088 18.723 264.073 1.00153.72 O
ANISOU 20 OE2 GLU A 28 24964 14833 18610 -1067 4649 -2057 O
ATOM 21 N ASP A 29 12.747 14.578 262.211 1.00137.24 N
ANISOU 21 N ASP A 29 21533 13153 17459 -644 5169 -2228 N
ATOM 22 CA ASP A 29 13.168 13.345 261.550 1.00130.92 C
ANISOU 22 CA ASP A 29 20552 12526 16665 -649 4934 -2248 C
ATOM 23 C ASP A 29 12.698 13.301 260.100 1.00123.19 C
ANISOU 23 C ASP A 29 19076 11725 16005 -422 4891 -2289 C
ATOM 24 O ASP A 29 13.429 12.837 259.216 1.00125.00 O
ANISOU 24 O ASP A 29 19158 12089 16245 -371 4618 -2273 O
ATOM 25 CB ASP A 29 12.644 12.131 262.317 1.00132.20 C
ANISOU 25 CB ASP A 29 20820 12671 16740 -811 5079 -2285 C
ATOM 26 CG ASP A 29 12.945 10.817 261.607 1.00130.10 C
ANISOU 26 CG ASP A 29 20366 12578 16487 -811 4877 -2305 C
ATOM 27 OD1 ASP A 29 14.138 10.517 261.389 1.00129.38 O
ANISOU 27 OD1 ASP A 29 20394 12543 16220 -821 4540 -2255 O
ATOM 28 OD2 ASP A 29 11.988 10.087 261.275 1.00130.70 O
ANISOU 28 OD2 ASP A 29 20170 12737 16753 -809 5057 -2384 O
ATOM 29 N GLU A 30 11.484 13.787 259.831 1.00118.92 N
ANISOU 29 N GLU A 30 18263 11197 15726 -270 5143 -2346 N
ATOM 30 CA GLU A 30 11.009 13.838 258.452 1.00116.31 C
ANISOU 30 CA GLU A 30 17449 11061 15685 -8 5070 -2382 C
ATOM 31 C GLU A 30 11.835 14.816 257.628 1.00114.10 C
ANISOU 31 C GLU A 30 17184 10775 15394 157 4856 -2289 C
ATOM 32 O GLU A 30 12.165 14.544 256.464 1.00110.20 O
ANISOU 32 O GLU A 30 16425 10438 15008 296 4647 -2273 O
ATOM 33 CB GLU A 30 9.532 14.227 258.428 1.00122.52 C
ANISOU 33 CB GLU A 30 17940 11879 16731 148 5349 -2475 C
ATOM 34 CG GLU A 30 8.963 14.462 257.040 1.00127.51 C
ANISOU 34 CG GLU A 30 18068 12735 17643 477 5242 -2506 C
ATOM 35 CD GLU A 30 7.510 14.901 257.082 1.00136.95 C
ANISOU 35 CD GLU A 30 18965 13990 19078 657 5476 -2617 C
ATOM 36 OE1 GLU A 30 7.029 15.485 256.087 1.00138.21 O
ANISOU 36 OE1 GLU A 30 18791 14303 19422 990 5377 -2622 O
ATOM 37 OE2 GLU A 30 6.851 14.668 258.118 1.00140.76 O
ANISOU 37 OE2 GLU A 30 19559 14367 19555 474 5749 -2702 O
ATOM 38 N PHE A 31 12.212 15.944 258.233 1.00105.87 N
ANISOU 38 N PHE A 31 16476 9543 14207 119 4917 -2227 N
ATOM 39 CA PHE A 31 13.067 16.897 257.540 1.00105.18 C
ANISOU 39 CA PHE A 31 16470 9420 14075 217 4743 -2144 C
ATOM 40 C PHE A 31 14.422 16.281 257.230 1.00105.50 C
ANISOU 40 C PHE A 31 16600 9525 13962 68 4431 -2120 C
ATOM 41 O PHE A 31 14.971 16.489 256.145 1.00 99.05 O
ANISOU 41 O PHE A 31 15640 8779 13214 183 4248 -2084 O
ATOM 42 CB PHE A 31 13.232 18.159 258.386 1.00107.60 C
ANISOU 42 CB PHE A 31 17153 9505 14223 146 4895 -2094 C
ATOM 43 CG PHE A 31 14.315 19.077 257.902 1.00101.10 C
ANISOU 43 CG PHE A 31 16511 8619 13283 140 4731 -2021 C
ATOM 44 CD1 PHE A 31 14.075 19.963 256.865 1.00103.93 C
ANISOU 44 CD1 PHE A 31 16734 8977 13778 402 4736 -1969 C
ATOM 45 CD2 PHE A 31 15.570 19.062 258.488 1.00 99.22 C
ANISOU 45 CD2 PHE A 31 16582 8328 12789 -128 4567 -2015 C
ATOM 46 CE1 PHE A 31 15.068 20.813 256.416 1.00 98.38 C
ANISOU 46 CE1 PHE A 31 16228 8197 12954 363 4622 -1907 C
ATOM 47 CE2 PHE A 31 16.567 19.912 258.043 1.00105.11 C
ANISOU 47 CE2 PHE A 31 17472 9026 13439 -174 4439 -1978 C
ATOM 48 CZ PHE A 31 16.315 20.787 257.005 1.00101.12 C
ANISOU 48 CZ PHE A 31 16857 8497 13069 55 4488 -1921 C
ATOM 49 N LEU A 32 14.964 15.493 258.162 1.00110.94 N
ANISOU 49 N LEU A 32 17524 10190 14438 -177 4359 -2142 N
ATOM 50 CA LEU A 32 16.252 14.851 257.923 1.00109.14 C
ANISOU 50 CA LEU A 32 17368 10041 14059 -302 4034 -2138 C
ATOM 51 C LEU A 32 16.150 13.792 256.833 1.00103.22 C
ANISOU 51 C LEU A 32 16258 9481 13480 -194 3899 -2161 C
ATOM 52 O LEU A 32 17.061 13.651 256.009 1.00103.95 O
ANISOU 52 O LEU A 32 16266 9653 13575 -181 3651 -2146 O
ATOM 53 CB LEU A 32 16.778 14.249 259.223 1.00115.51 C
ANISOU 53 CB LEU A 32 18524 10787 14577 -536 3966 -2151 C
ATOM 54 CG LEU A 32 17.246 15.282 260.244 1.00121.27 C
ANISOU 54 CG LEU A 32 19632 11353 15093 -670 4013 -2130 C
ATOM 55 CD1 LEU A 32 16.804 14.894 261.642 1.00127.43 C
ANISOU 55 CD1 LEU A 32 20702 12027 15690 -807 4177 -2132 C
ATOM 56 CD2 LEU A 32 18.758 15.423 260.177 1.00119.30 C
ANISOU 56 CD2 LEU A 32 19525 11141 14661 -793 3678 -2147 C
ATOM 57 N ARG A 33 15.040 13.054 256.794 1.00100.72 N
ANISOU 57 N ARG A 33 15712 9244 13314 -130 4073 -2207 N
ATOM 58 CA ARG A 33 14.865 12.080 255.724 1.00 95.69 C
ANISOU 58 CA ARG A 33 14706 8803 12848 -30 3966 -2236 C
ATOM 59 C ARG A 33 14.809 12.765 254.365 1.00 91.24 C
ANISOU 59 C ARG A 33 13834 8327 12506 223 3890 -2199 C
ATOM 60 O ARG A 33 15.440 12.306 253.399 1.00 82.86 O
ANISOU 60 O ARG A 33 12580 7419 11483 260 3633 -2147 O
ATOM 61 CB ARG A 33 13.598 11.263 255.964 1.00106.31 C
ANISOU 61 CB ARG A 33 15842 10227 14323 -35 4200 -2318 C
ATOM 62 CG ARG A 33 13.628 10.420 257.223 1.00118.11 C
ANISOU 62 CG ARG A 33 17663 11630 15585 -283 4284 -2339 C
ATOM 63 CD ARG A 33 12.501 9.399 257.225 1.00126.04 C
ANISOU 63 CD ARG A 33 18430 12734 16726 -327 4494 -2432 C
ATOM 64 NE ARG A 33 12.710 8.352 258.221 1.00133.79 N
ANISOU 64 NE ARG A 33 19746 13636 17452 -561 4525 -2428 N
ATOM 65 CZ ARG A 33 13.418 7.246 258.007 1.00131.48 C
ANISOU 65 CZ ARG A 33 19529 13418 17011 -631 4314 -2402 C
ATOM 66 NH1 ARG A 33 13.992 7.042 256.829 1.00128.73 N
ANISOU 66 NH1 ARG A 33 18927 13224 16761 -511 4071 -2390 N
ATOM 67 NH2 ARG A 33 13.554 6.344 258.971 1.00134.90 N
ANISOU 67 NH2 ARG A 33 20306 13762 17187 -809 4348 -2379 N
ATOM 68 N TYR A 34 14.062 13.870 254.270 1.00 93.28 N
ANISOU 68 N TYR A 34 14032 8525 12884 402 4059 -2181 N
ATOM 69 CA TYR A 34 13.982 14.580 252.998 1.00 86.62 C
ANISOU 69 CA TYR A 34 12950 7751 12209 678 3971 -2121 C
ATOM 70 C TYR A 34 15.309 15.239 252.636 1.00 78.33 C
ANISOU 70 C TYR A 34 12148 6595 11018 614 3785 -2044 C
ATOM 71 O TYR A 34 15.665 15.315 251.456 1.00 74.25 O
ANISOU 71 O TYR A 34 11431 6202 10580 744 3582 -1961 O
ATOM 72 CB TYR A 34 12.847 15.601 253.034 1.00 90.65 C
ANISOU 72 CB TYR A 34 13374 8221 12848 910 4176 -2120 C
ATOM 73 CG TYR A 34 11.507 14.948 252.800 1.00102.22 C
ANISOU 73 CG TYR A 34 14410 9886 14541 1054 4281 -2216 C
ATOM 74 CD1 TYR A 34 11.220 14.342 251.582 1.00108.44 C
ANISOU 74 CD1 TYR A 34 14769 10922 15513 1238 4115 -2225 C
ATOM 75 CD2 TYR A 34 10.537 14.914 253.795 1.00110.65 C
ANISOU 75 CD2 TYR A 34 15494 10909 15639 981 4543 -2308 C
ATOM 76 CE1 TYR A 34 10.005 13.727 251.356 1.00115.84 C
ANISOU 76 CE1 TYR A 34 15283 12080 16650 1338 4185 -2335 C
ATOM 77 CE2 TYR A 34 9.313 14.301 253.578 1.00117.89 C
ANISOU 77 CE2 TYR A 34 15994 12029 16772 1076 4640 -2427 C
ATOM 78 CZ TYR A 34 9.054 13.709 252.355 1.00121.01 C
ANISOU 78 CZ TYR A 34 15945 12693 17338 1250 4450 -2446 C
ATOM 79 OH TYR A 34 7.842 13.098 252.129 1.00123.86 O
ANISOU 79 OH TYR A 34 15870 13288 17903 1318 4522 -2584 O
ATOM 80 N LEU A 35 16.060 15.718 253.633 1.00 77.23 N
ANISOU 80 N LEU A 35 12406 6288 10649 383 3796 -2041 N
ATOM 81 CA LEU A 35 17.383 16.270 253.354 1.00 81.62 C
ANISOU 81 CA LEU A 35 13173 6774 11067 259 3615 -2007 C
ATOM 82 C LEU A 35 18.327 15.193 252.836 1.00 79.84 C
ANISOU 82 C LEU A 35 12778 6751 10805 137 3286 -1987 C
ATOM 83 O LEU A 35 19.162 15.453 251.961 1.00 77.51 O
ANISOU 83 O LEU A 35 12401 6536 10513 129 3080 -1923 O
ATOM 84 CB LEU A 35 17.956 16.921 254.613 1.00 88.00 C
ANISOU 84 CB LEU A 35 14387 7420 11630 16 3666 -2023 C
ATOM 85 CG LEU A 35 19.389 17.447 254.520 1.00 91.37 C
ANISOU 85 CG LEU A 35 15020 7803 11895 -181 3478 -2034 C
ATOM 86 CD1 LEU A 35 19.462 18.745 253.718 1.00 91.33 C
ANISOU 86 CD1 LEU A 35 15061 7699 11941 -64 3565 -1970 C
ATOM 87 CD2 LEU A 35 19.984 17.638 255.909 1.00 89.12 C
ANISOU 87 CD2 LEU A 35 15075 7433 11353 -446 3462 -2083 C
ATOM 88 N TRP A 36 18.194 13.970 253.346 1.00 79.15 N
ANISOU 88 N TRP A 36 12634 6766 10674 39 3229 -2028 N
ATOM 89 CA TRP A 36 19.034 12.884 252.859 1.00 69.72 C
ANISOU 89 CA TRP A 36 11262 5793 9434 -50 2900 -1985 C
ATOM 90 C TRP A 36 18.666 12.511 251.429 1.00 75.79 C
ANISOU 90 C TRP A 36 11594 6783 10420 144 2781 -1894 C
ATOM 91 O TRP A 36 19.541 12.356 250.568 1.00 71.45 O
ANISOU 91 O TRP A 36 10908 6368 9874 125 2524 -1826 O
ATOM 92 CB TRP A 36 18.909 11.671 253.780 1.00 76.28 C
ANISOU 92 CB TRP A 36 12211 6637 10134 -178 2904 -2049 C
ATOM 93 CG TRP A 36 19.480 10.437 253.177 1.00 83.25 C
ANISOU 93 CG TRP A 36 12878 7753 11002 -203 2612 -1999 C
ATOM 94 CD1 TRP A 36 18.798 9.450 252.524 1.00 80.32 C
ANISOU 94 CD1 TRP A 36 12196 7552 10769 -114 2612 -1970 C
ATOM 95 CD2 TRP A 36 20.862 10.062 253.143 1.00 84.46 C
ANISOU 95 CD2 TRP A 36 13096 7999 10997 -322 2279 -1984 C
ATOM 96 NE1 TRP A 36 19.669 8.479 252.094 1.00 72.36 N
ANISOU 96 NE1 TRP A 36 11095 6715 9685 -168 2314 -1920 N
ATOM 97 CE2 TRP A 36 20.942 8.831 252.462 1.00 80.58 C
ANISOU 97 CE2 TRP A 36 12349 7718 10552 -280 2101 -1929 C
ATOM 98 CE3 TRP A 36 22.037 10.645 253.626 1.00 83.32 C
ANISOU 98 CE3 TRP A 36 13186 7792 10681 -461 2118 -2033 C
ATOM 99 CZ2 TRP A 36 22.150 8.171 252.253 1.00 86.81 C
ANISOU 99 CZ2 TRP A 36 13115 8647 11224 -345 1771 -1911 C
ATOM 100 CZ3 TRP A 36 23.237 9.989 253.417 1.00 85.87 C
ANISOU 100 CZ3 TRP A 36 13446 8281 10902 -533 1775 -2037 C
ATOM 101 CH2 TRP A 36 23.284 8.765 252.736 1.00 87.39 C
ANISOU 101 CH2 TRP A 36 13385 8673 11146 -460 1606 -1970 C
ATOM 102 N ARG A 37 17.370 12.363 251.153 1.00 76.40 N
ANISOU 102 N ARG A 37 11441 6907 10680 328 2968 -1910 N
ATOM 103 CA ARG A 37 16.959 11.961 249.811 1.00 77.95 C
ANISOU 103 CA ARG A 37 11221 7328 11069 519 2835 -1840 C
ATOM 104 C ARG A 37 17.245 13.049 248.779 1.00 79.12 C
ANISOU 104 C ARG A 37 11336 7446 11280 692 2758 -1749 C
ATOM 105 O ARG A 37 17.703 12.755 247.669 1.00 68.12 O
ANISOU 105 O ARG A 37 9743 6206 9935 743 2531 -1663 O
ATOM 106 CB ARG A 37 15.475 11.606 249.809 1.00 87.41 C
ANISOU 106 CB ARG A 37 12158 8601 12453 673 3053 -1922 C
ATOM 107 CG ARG A 37 14.846 11.620 248.427 1.00 93.05 C
ANISOU 107 CG ARG A 37 12460 9516 13379 941 2948 -1873 C
ATOM 108 CD ARG A 37 13.335 11.607 248.529 1.00105.53 C
ANISOU 108 CD ARG A 37 13781 11157 15160 1121 3191 -1999 C
ATOM 109 NE ARG A 37 12.841 10.376 249.138 1.00112.89 N
ANISOU 109 NE ARG A 37 14611 12179 16105 934 3312 -2119 N
ATOM 110 CZ ARG A 37 11.579 10.186 249.510 1.00120.66 C
ANISOU 110 CZ ARG A 37 15396 13201 17246 989 3586 -2285 C
ATOM 111 NH1 ARG A 37 10.684 11.151 249.340 1.00123.33 N
ANISOU 111 NH1 ARG A 37 15589 13518 17753 1260 3738 -2345 N
ATOM 112 NH2 ARG A 37 11.212 9.033 250.055 1.00119.88 N
ANISOU 112 NH2 ARG A 37 15258 13158 17134 774 3724 -2403 N
ATOM 113 N ASP A 38 16.982 14.311 249.124 1.00 77.91 N
ANISOU 113 N ASP A 38 11418 7074 11112 781 2965 -1767 N
ATOM 114 CA ASP A 38 17.011 15.398 248.154 1.00 77.57 C
ANISOU 114 CA ASP A 38 11398 6958 11118 995 2958 -1688 C
ATOM 115 C ASP A 38 18.375 16.045 247.985 1.00 76.70 C
ANISOU 115 C ASP A 38 11561 6730 10852 812 2851 -1647 C
ATOM 116 O ASP A 38 18.608 16.692 246.958 1.00 78.97 O
ANISOU 116 O ASP A 38 11861 6983 11162 948 2801 -1570 O
ATOM 117 CB ASP A 38 16.002 16.481 248.548 1.00 76.49 C
ANISOU 117 CB ASP A 38 11403 6624 11036 1219 3258 -1731 C
ATOM 118 CG ASP A 38 14.565 16.061 248.299 1.00 85.08 C
ANISOU 118 CG ASP A 38 12123 7866 12338 1489 3350 -1786 C
ATOM 119 OD1 ASP A 38 14.344 14.938 247.795 1.00 87.51 O
ANISOU 119 OD1 ASP A 38 12079 8428 12744 1481 3187 -1790 O
ATOM 120 OD2 ASP A 38 13.659 16.864 248.605 1.00 93.54 O
ANISOU 120 OD2 ASP A 38 13249 8816 13477 1702 3582 -1835 O
ATOM 121 N TYR A 39 19.280 15.891 248.947 1.00 74.31 N
ANISOU 121 N TYR A 39 11484 6365 10384 508 2819 -1713 N
ATOM 122 CA TYR A 39 20.559 16.577 248.845 1.00 76.65 C
ANISOU 122 CA TYR A 39 12014 6563 10547 309 2742 -1723 C
ATOM 123 C TYR A 39 21.727 15.696 249.269 1.00 74.88 C
ANISOU 123 C TYR A 39 11763 6480 10207 23 2495 -1780 C
ATOM 124 O TYR A 39 22.681 15.516 248.506 1.00 69.76 O
ANISOU 124 O TYR A 39 11000 5946 9560 -66 2294 -1760 O
ATOM 125 CB TYR A 39 20.545 17.855 249.682 1.00 81.91 C
ANISOU 125 CB TYR A 39 13092 6934 11096 244 3007 -1787 C
ATOM 126 CG TYR A 39 21.914 18.466 249.834 1.00 83.80 C
ANISOU 126 CG TYR A 39 13580 7083 11177 -47 2946 -1855 C
ATOM 127 CD1 TYR A 39 22.504 19.162 248.788 1.00 85.21 C
ANISOU 127 CD1 TYR A 39 13800 7210 11365 -42 2934 -1817 C
ATOM 128 CD2 TYR A 39 22.622 18.337 251.020 1.00 82.10 C
ANISOU 128 CD2 TYR A 39 13565 6834 10795 -334 2905 -1977 C
ATOM 129 CE1 TYR A 39 23.757 19.717 248.919 1.00 84.03 C
ANISOU 129 CE1 TYR A 39 13852 6989 11087 -345 2910 -1918 C
ATOM 130 CE2 TYR A 39 23.873 18.888 251.162 1.00 84.32 C
ANISOU 130 CE2 TYR A 39 14025 7067 10945 -613 2837 -2078 C
ATOM 131 CZ TYR A 39 24.437 19.578 250.110 1.00 84.90 C
ANISOU 131 CZ TYR A 39 14101 7101 11054 -633 2854 -2059 C
ATOM 132 OH TYR A 39 25.687 20.129 250.248 1.00 83.80 O
ANISOU 132 OH TYR A 39 14117 6923 10799 -948 2819 -2198 O
ATOM 133 N LEU A 40 21.677 15.148 250.484 1.00 74.08 N
ANISOU 133 N LEU A 40 11786 6364 9997 -109 2510 -1859 N
ATOM 134 CA LEU A 40 22.835 14.427 251.007 1.00 77.38 C
ANISOU 134 CA LEU A 40 12243 6892 10265 -346 2259 -1930 C
ATOM 135 C LEU A 40 23.151 13.195 250.166 1.00 77.93 C
ANISOU 135 C LEU A 40 11969 7227 10413 -303 1993 -1865 C
ATOM 136 O LEU A 40 24.281 13.029 249.685 1.00 75.69 O
ANISOU 136 O LEU A 40 11591 7064 10103 -416 1768 -1881 O
ATOM 137 CB LEU A 40 22.592 14.038 252.464 1.00 82.27 C
ANISOU 137 CB LEU A 40 13120 7416 10724 -450 2334 -2017 C
ATOM 138 CG LEU A 40 22.627 15.196 253.465 1.00 81.73 C
ANISOU 138 CG LEU A 40 13453 7083 10519 -568 2549 -2106 C
ATOM 139 CD1 LEU A 40 22.196 14.738 254.851 1.00 83.64 C
ANISOU 139 CD1 LEU A 40 13968 7208 10603 -640 2656 -2180 C
ATOM 140 CD2 LEU A 40 24.016 15.809 253.510 1.00 80.27 C
ANISOU 140 CD2 LEU A 40 13396 6895 10207 -795 2387 -2196 C
ATOM 141 N TYR A 41 22.164 12.325 249.968 1.00 75.69 N
ANISOU 141 N TYR A 41 11488 7039 10230 -150 2032 -1807 N
ATOM 142 CA TYR A 41 22.416 11.112 249.196 1.00 71.64 C
ANISOU 142 CA TYR A 41 10680 6764 9777 -118 1801 -1746 C
ATOM 143 C TYR A 41 22.851 11.399 247.767 1.00 70.85 C
ANISOU 143 C TYR A 41 10354 6763 9803 -45 1679 -1663 C
ATOM 144 O TYR A 41 23.843 10.799 247.319 1.00 75.04 O
ANISOU 144 O TYR A 41 10763 7440 10307 -135 1443 -1656 O
ATOM 145 CB TYR A 41 21.184 10.206 249.212 1.00 69.64 C
ANISOU 145 CB TYR A 41 10265 6582 9615 8 1913 -1723 C
ATOM 146 CG TYR A 41 21.369 8.996 248.320 1.00 79.95 C
ANISOU 146 CG TYR A 41 11278 8119 10982 42 1703 -1656 C
ATOM 147 CD1 TYR A 41 22.131 7.912 248.738 1.00 76.77 C
ANISOU 147 CD1 TYR A 41 10934 7805 10432 -79 1512 -1676 C
ATOM 148 CD2 TYR A 41 20.812 8.950 247.048 1.00 81.04 C
ANISOU 148 CD2 TYR A 41 11107 8379 11306 209 1684 -1574 C
ATOM 149 CE1 TYR A 41 22.321 6.811 247.923 1.00 71.36 C
ANISOU 149 CE1 TYR A 41 10009 7312 9791 -46 1338 -1611 C
ATOM 150 CE2 TYR A 41 20.994 7.855 246.226 1.00 68.65 C
ANISOU 150 CE2 TYR A 41 9293 7009 9782 224 1502 -1514 C
ATOM 151 CZ TYR A 41 21.750 6.786 246.667 1.00 73.89 C
ANISOU 151 CZ TYR A 41 10022 7747 10304 90 1343 -1530 C
ATOM 152 OH TYR A 41 21.931 5.692 245.846 1.00 78.06 O
ANISOU 152 OH TYR A 41 10333 8459 10869 109 1181 -1468 O
ATOM 153 N PRO A 42 22.156 12.231 246.984 1.00 74.56 N
ANISOU 153 N PRO A 42 10769 7160 10401 135 1823 -1600 N
ATOM 154 CA PRO A 42 22.646 12.499 245.619 1.00 71.18 C
ANISOU 154 CA PRO A 42 10199 6793 10054 197 1710 -1522 C
ATOM 155 C PRO A 42 24.043 13.090 245.583 1.00 76.72 C
ANISOU 155 C PRO A 42 11054 7436 10659 -22 1633 -1582 C
ATOM 156 O PRO A 42 24.835 12.766 244.689 1.00 74.08 O
ANISOU 156 O PRO A 42 10568 7218 10360 -76 1470 -1555 O
ATOM 157 CB PRO A 42 21.608 13.479 245.058 1.00 78.91 C
ANISOU 157 CB PRO A 42 11211 7641 11131 453 1907 -1465 C
ATOM 158 CG PRO A 42 20.388 13.282 245.899 1.00 84.68 C
ANISOU 158 CG PRO A 42 11925 8348 11902 561 2077 -1507 C
ATOM 159 CD PRO A 42 20.885 12.921 247.267 1.00 80.53 C
ANISOU 159 CD PRO A 42 11594 7775 11228 316 2090 -1604 C
ATOM 160 N LYS A 43 24.382 13.925 246.567 1.00 78.31 N
ANISOU 160 N LYS A 43 11547 7465 10741 -172 1756 -1684 N
ATOM 161 CA LYS A 43 25.708 14.532 246.580 1.00 80.09 C
ANISOU 161 CA LYS A 43 11900 7649 10882 -416 1702 -1787 C
ATOM 162 C LYS A 43 26.777 13.481 246.847 1.00 77.39 C
ANISOU 162 C LYS A 43 11393 7526 10484 -586 1415 -1864 C
ATOM 163 O LYS A 43 27.800 13.433 246.151 1.00 74.93 O
ANISOU 163 O LYS A 43 10953 7314 10204 -705 1284 -1906 O
ATOM 164 CB LYS A 43 25.758 15.646 247.628 1.00 82.82 C
ANISOU 164 CB LYS A 43 12605 7762 11099 -548 1905 -1894 C
ATOM 165 CG LYS A 43 26.776 16.742 247.355 1.00 99.55 C
ANISOU 165 CG LYS A 43 14906 9756 13161 -763 1984 -1996 C
ATOM 166 CD LYS A 43 26.103 18.017 246.866 1.00112.75 C
ANISOU 166 CD LYS A 43 16832 11159 14849 -622 2286 -1929 C
ATOM 167 CE LYS A 43 27.064 19.199 246.893 1.00122.13 C
ANISOU 167 CE LYS A 43 18309 12162 15932 -891 2439 -2066 C
ATOM 168 NZ LYS A 43 26.397 20.471 246.497 1.00128.62 N
ANISOU 168 NZ LYS A 43 19465 12677 16728 -736 2759 -1997 N
ATOM 169 N GLN A 44 26.541 12.603 247.827 1.00 76.60 N
ANISOU 169 N GLN A 44 11308 7498 10300 -584 1323 -1890 N
ATOM 170 CA GLN A 44 27.497 11.534 248.094 1.00 74.62 C
ANISOU 170 CA GLN A 44 10929 7451 9974 -682 1031 -1955 C
ATOM 171 C GLN A 44 27.590 10.566 246.920 1.00 77.67 C
ANISOU 171 C GLN A 44 10993 8032 10485 -575 876 -1848 C
ATOM 172 O GLN A 44 28.674 10.056 246.604 1.00 75.80 O
ANISOU 172 O GLN A 44 10601 7957 10241 -663 655 -1904 O
ATOM 173 CB GLN A 44 27.099 10.798 249.373 1.00 82.54 C
ANISOU 173 CB GLN A 44 12099 8439 10824 -668 998 -1988 C
ATOM 174 CG GLN A 44 27.650 9.393 249.492 1.00 89.83 C
ANISOU 174 CG GLN A 44 12897 9562 11671 -648 718 -1993 C
ATOM 175 CD GLN A 44 27.244 8.731 250.792 1.00103.09 C
ANISOU 175 CD GLN A 44 14840 11173 13158 -633 720 -2030 C
ATOM 176 OE1 GLN A 44 27.311 9.342 251.860 1.00108.85 O
ANISOU 176 OE1 GLN A 44 15864 11754 13741 -729 789 -2129 O
ATOM 177 NE2 GLN A 44 26.810 7.477 250.709 1.00108.69 N
ANISOU 177 NE2 GLN A 44 15482 11967 13848 -523 664 -1954 N
ATOM 178 N TYR A 45 26.467 10.323 246.242 1.00 79.01 N
ANISOU 178 N TYR A 45 11049 8197 10775 -382 989 -1709 N
ATOM 179 CA TYR A 45 26.466 9.409 245.107 1.00 69.67 C
ANISOU 179 CA TYR A 45 9581 7189 9701 -284 854 -1606 C
ATOM 180 C TYR A 45 27.316 9.968 243.976 1.00 69.94 C
ANISOU 180 C TYR A 45 9520 7238 9816 -345 813 -1602 C
ATOM 181 O TYR A 45 28.169 9.268 243.416 1.00 67.32 O
ANISOU 181 O TYR A 45 9005 7064 9508 -401 627 -1609 O
ATOM 182 CB TYR A 45 25.019 9.168 244.659 1.00 61.93 C
ANISOU 182 CB TYR A 45 8500 6202 8831 -74 992 -1492 C
ATOM 183 CG TYR A 45 24.819 8.304 243.425 1.00 61.90 C
ANISOU 183 CG TYR A 45 8216 6364 8940 38 878 -1383 C
ATOM 184 CD1 TYR A 45 25.156 8.771 242.161 1.00 69.71 C
ANISOU 184 CD1 TYR A 45 9111 7356 10019 80 849 -1320 C
ATOM 185 CD2 TYR A 45 24.239 7.043 243.519 1.00 61.04 C
ANISOU 185 CD2 TYR A 45 7975 6385 8833 92 827 -1350 C
ATOM 186 CE1 TYR A 45 24.957 8.000 241.034 1.00 66.66 C
ANISOU 186 CE1 TYR A 45 8499 7109 9721 179 746 -1222 C
ATOM 187 CE2 TYR A 45 24.039 6.260 242.391 1.00 66.20 C
ANISOU 187 CE2 TYR A 45 8386 7186 9579 176 732 -1260 C
ATOM 188 CZ TYR A 45 24.398 6.746 241.151 1.00 73.26 C
ANISOU 188 CZ TYR A 45 9182 8091 10562 225 680 -1193 C
ATOM 189 OH TYR A 45 24.201 5.979 240.024 1.00 74.23 O
ANISOU 189 OH TYR A 45 9091 8350 10763 306 583 -1103 O
ATOM 190 N ALA A 46 27.121 11.250 243.653 1.00 68.49 N
ANISOU 190 N ALA A 46 9491 6871 9663 -340 1008 -1601 N
ATOM 191 CA ALA A 46 27.925 11.868 242.605 1.00 75.40 C
ANISOU 191 CA ALA A 46 10351 7708 10589 -424 1025 -1613 C
ATOM 192 C ALA A 46 29.395 11.919 242.996 1.00 82.01 C
ANISOU 192 C ALA A 46 11175 8617 11367 -697 908 -1790 C
ATOM 193 O ALA A 46 30.275 11.723 242.146 1.00 80.28 O
ANISOU 193 O ALA A 46 10803 8490 11211 -790 824 -1821 O
ATOM 194 CB ALA A 46 27.403 13.272 242.300 1.00 74.17 C
ANISOU 194 CB ALA A 46 10451 7296 10433 -356 1286 -1586 C
ATOM 195 N TRP A 47 29.685 12.149 244.280 1.00 82.85 N
ANISOU 195 N TRP A 47 11429 8696 11355 -828 893 -1924 N
ATOM 196 CA TRP A 47 31.082 12.212 244.689 1.00 79.46 C
ANISOU 196 CA TRP A 47 10954 8369 10871 -1079 751 -2129 C
ATOM 197 C TRP A 47 31.760 10.862 244.511 1.00 80.04 C
ANISOU 197 C TRP A 47 10737 8709 10965 -1053 455 -2142 C
ATOM 198 O TRP A 47 32.848 10.776 243.928 1.00 79.71 O
ANISOU 198 O TRP A 47 10509 8789 10986 -1185 355 -2249 O
ATOM 199 CB TRP A 47 31.199 12.678 246.141 1.00 85.00 C
ANISOU 199 CB TRP A 47 11889 8993 11415 -1203 764 -2272 C
ATOM 200 CG TRP A 47 32.626 12.898 246.561 1.00 99.87 C
ANISOU 200 CG TRP A 47 13713 10990 13241 -1468 615 -2522 C
ATOM 201 CD1 TRP A 47 33.318 14.074 246.530 1.00104.96 C
ANISOU 201 CD1 TRP A 47 14474 11529 13878 -1723 769 -2697 C
ATOM 202 CD2 TRP A 47 33.539 11.909 247.055 1.00107.27 C
ANISOU 202 CD2 TRP A 47 14455 12182 14122 -1500 282 -2649 C
ATOM 203 NE1 TRP A 47 34.601 13.881 246.982 1.00110.97 N
ANISOU 203 NE1 TRP A 47 15076 12488 14600 -1931 547 -2946 N
ATOM 204 CE2 TRP A 47 34.763 12.560 247.310 1.00113.96 C
ANISOU 204 CE2 TRP A 47 15257 13094 14946 -1774 228 -2917 C
ATOM 205 CE3 TRP A 47 33.439 10.537 247.312 1.00108.62 C
ANISOU 205 CE3 TRP A 47 14500 12524 14245 -1316 31 -2572 C
ATOM 206 CZ2 TRP A 47 35.877 11.886 247.809 1.00116.74 C
ANISOU 206 CZ2 TRP A 47 15403 13707 15245 -1837 -103 -3118 C
ATOM 207 CZ3 TRP A 47 34.547 9.871 247.807 1.00107.56 C
ANISOU 207 CZ3 TRP A 47 14219 12616 14035 -1361 -286 -2747 C
ATOM 208 CH2 TRP A 47 35.748 10.545 248.050 1.00110.72 C
ANISOU 208 CH2 TRP A 47 14538 13105 14428 -1605 -368 -3020 C
ATOM 209 N VAL A 48 31.129 9.791 245.006 1.00 69.14 N
ANISOU 209 N VAL A 48 9330 7411 9530 -885 333 -2046 N
ATOM 210 CA VAL A 48 31.735 8.468 244.878 1.00 72.76 C
ANISOU 210 CA VAL A 48 9570 8099 9979 -831 63 -2048 C
ATOM 211 C VAL A 48 31.866 8.087 243.411 1.00 75.29 C
ANISOU 211 C VAL A 48 9649 8501 10457 -777 57 -1942 C
ATOM 212 O VAL A 48 32.874 7.503 242.993 1.00 74.83 O
ANISOU 212 O VAL A 48 9381 8614 10437 -827 -121 -2013 O
ATOM 213 CB VAL A 48 30.921 7.422 245.662 1.00 67.42 C
ANISOU 213 CB VAL A 48 8987 7441 9187 -669 -4 -1958 C
ATOM 214 CG1 VAL A 48 31.498 6.031 245.434 1.00 70.71 C
ANISOU 214 CG1 VAL A 48 9224 8066 9577 -585 -260 -1941 C
ATOM 215 CG2 VAL A 48 30.909 7.766 247.140 1.00 70.77 C
ANISOU 215 CG2 VAL A 48 9691 7770 9428 -734 -7 -2076 C
ATOM 216 N LEU A 49 30.878 8.455 242.595 1.00 72.99 N
ANISOU 216 N LEU A 49 9389 8088 10257 -667 249 -1785 N
ATOM 217 CA LEU A 49 30.923 8.087 241.185 1.00 67.66 C
ANISOU 217 CA LEU A 49 8529 7472 9708 -603 240 -1675 C
ATOM 218 C LEU A 49 32.090 8.768 240.480 1.00 63.63 C
ANISOU 218 C LEU A 49 7964 6949 9264 -793 276 -1796 C
ATOM 219 O LEU A 49 32.919 8.106 239.833 1.00 69.26 O
ANISOU 219 O LEU A 49 8465 7810 10040 -838 148 -1826 O
ATOM 220 CB LEU A 49 29.590 8.452 240.529 1.00 67.91 C
ANISOU 220 CB LEU A 49 8632 7372 9800 -423 418 -1506 C
ATOM 221 CG LEU A 49 29.320 8.099 239.068 1.00 76.55 C
ANISOU 221 CG LEU A 49 9587 8501 10999 -309 415 -1367 C
ATOM 222 CD1 LEU A 49 27.885 7.624 238.909 1.00 81.42 C
ANISOU 222 CD1 LEU A 49 10162 9132 11642 -86 446 -1226 C
ATOM 223 CD2 LEU A 49 29.577 9.303 238.183 1.00 76.44 C
ANISOU 223 CD2 LEU A 49 9710 8309 11026 -357 583 -1371 C
ATOM 224 N ILE A 50 32.183 10.094 240.611 1.00 68.66 N
ANISOU 224 N ILE A 50 8804 7398 9885 -921 476 -1880 N
ATOM 225 CA ILE A 50 33.237 10.828 239.917 1.00 73.09 C
ANISOU 225 CA ILE A 50 9356 7911 10505 -1141 577 -2017 C
ATOM 226 C ILE A 50 34.607 10.426 240.448 1.00 81.11 C
ANISOU 226 C ILE A 50 10163 9134 11520 -1342 385 -2251 C
ATOM 227 O ILE A 50 35.579 10.332 239.687 1.00 82.40 O
ANISOU 227 O ILE A 50 10148 9382 11777 -1480 373 -2356 O
ATOM 228 CB ILE A 50 32.998 12.344 240.037 1.00 71.50 C
ANISOU 228 CB ILE A 50 9477 7435 10255 -1242 863 -2068 C
ATOM 229 CG1 ILE A 50 31.656 12.715 239.402 1.00 69.40 C
ANISOU 229 CG1 ILE A 50 9395 6980 9993 -983 1023 -1842 C
ATOM 230 CG2 ILE A 50 34.138 13.124 239.384 1.00 60.55 C
ANISOU 230 CG2 ILE A 50 8120 5974 8911 -1522 1015 -2246 C
ATOM 231 CD1 ILE A 50 31.216 14.140 239.677 1.00 69.47 C
ANISOU 231 CD1 ILE A 50 9767 6702 9925 -1004 1298 -1863 C
ATOM 232 N ALA A 51 34.707 10.150 241.751 1.00 82.46 N
ANISOU 232 N ALA A 51 10352 9399 11582 -1347 223 -2347 N
ATOM 233 CA ALA A 51 36.002 9.779 242.305 1.00 75.55 C
ANISOU 233 CA ALA A 51 9273 8743 10691 -1496 -4 -2590 C
ATOM 234 C ALA A 51 36.437 8.403 241.817 1.00 76.84 C
ANISOU 234 C ALA A 51 9145 9141 10912 -1360 -247 -2543 C
ATOM 235 O ALA A 51 37.603 8.211 241.447 1.00 79.91 O
ANISOU 235 O ALA A 51 9282 9695 11386 -1484 -349 -2721 O
ATOM 236 CB ALA A 51 35.952 9.822 243.831 1.00 72.94 C
ANISOU 236 CB ALA A 51 9089 8433 10191 -1502 -136 -2697 C
ATOM 237 N ALA A 52 35.515 7.436 241.784 1.00 67.91 N
ANISOU 237 N ALA A 52 8040 8023 9740 -1112 -321 -2318 N
ATOM 238 CA ALA A 52 35.882 6.115 241.294 1.00 57.62 C
ANISOU 238 CA ALA A 52 6507 6914 8473 -980 -524 -2259 C
ATOM 239 C ALA A 52 36.304 6.180 239.834 1.00 65.30 C
ANISOU 239 C ALA A 52 7305 7891 9614 -1048 -415 -2230 C
ATOM 240 O ALA A 52 37.315 5.578 239.441 1.00 73.18 O
ANISOU 240 O ALA A 52 8054 9067 10682 -1082 -554 -2337 O
ATOM 241 CB ALA A 52 34.715 5.143 241.479 1.00 47.32 C
ANISOU 241 CB ALA A 52 5306 5588 7086 -742 -560 -2031 C
ATOM 242 N TYR A 53 35.578 6.958 239.024 1.00 66.52 N
ANISOU 242 N TYR A 53 7607 7840 9827 -1064 -160 -2100 N
ATOM 243 CA TYR A 53 35.937 7.049 237.613 1.00 65.70 C
ANISOU 243 CA TYR A 53 7409 7701 9853 -1125 -39 -2064 C
ATOM 244 C TYR A 53 37.283 7.744 237.417 1.00 69.64 C
ANISOU 244 C TYR A 53 7798 8228 10434 -1408 36 -2333 C
ATOM 245 O TYR A 53 38.108 7.279 236.625 1.00 73.51 O
ANISOU 245 O TYR A 53 8073 8827 11033 -1473 8 -2400 O
ATOM 246 CB TYR A 53 34.840 7.766 236.828 1.00 66.81 C
ANISOU 246 CB TYR A 53 7783 7600 10001 -1043 197 -1873 C
ATOM 247 CG TYR A 53 33.852 6.846 236.133 1.00 67.78 C
ANISOU 247 CG TYR A 53 7870 7749 10135 -802 140 -1627 C
ATOM 248 CD1 TYR A 53 32.666 6.476 236.753 1.00 70.85 C
ANISOU 248 CD1 TYR A 53 8331 8137 10453 -615 95 -1496 C
ATOM 249 CD2 TYR A 53 34.103 6.357 234.852 1.00 65.92 C
ANISOU 249 CD2 TYR A 53 7530 7537 9979 -784 148 -1546 C
ATOM 250 CE1 TYR A 53 31.757 5.642 236.123 1.00 66.98 C
ANISOU 250 CE1 TYR A 53 7783 7688 9977 -428 54 -1309 C
ATOM 251 CE2 TYR A 53 33.202 5.523 234.214 1.00 67.55 C
ANISOU 251 CE2 TYR A 53 7705 7776 10186 -585 91 -1341 C
ATOM 252 CZ TYR A 53 32.028 5.171 234.853 1.00 73.20 C
ANISOU 252 CZ TYR A 53 8467 8510 10837 -413 41 -1231 C
ATOM 253 OH TYR A 53 31.118 4.346 234.225 1.00 68.03 O
ANISOU 253 OH TYR A 53 7757 7905 10188 -244 -5 -1062 O
ATOM 254 N VAL A 54 37.538 8.841 238.137 1.00 67.80 N
ANISOU 254 N VAL A 54 7704 7901 10156 -1596 147 -2509 N
ATOM 255 CA VAL A 54 38.797 9.560 237.953 1.00 72.83 C
ANISOU 255 CA VAL A 54 8233 8563 10876 -1911 256 -2804 C
ATOM 256 C VAL A 54 39.976 8.716 238.422 1.00 80.06 C
ANISOU 256 C VAL A 54 8776 9801 11840 -1954 -32 -3032 C
ATOM 257 O VAL A 54 41.043 8.694 237.784 1.00 82.12 O
ANISOU 257 O VAL A 54 8796 10169 12238 -2132 7 -3229 O
ATOM 258 CB VAL A 54 38.749 10.910 238.690 1.00 67.77 C
ANISOU 258 CB VAL A 54 7852 7744 10153 -2112 447 -2950 C
ATOM 259 CG1 VAL A 54 40.098 11.613 238.610 1.00 70.98 C
ANISOU 259 CG1 VAL A 54 8123 8203 10642 -2483 563 -3307 C
ATOM 260 CG2 VAL A 54 37.648 11.789 238.121 1.00 67.75 C
ANISOU 260 CG2 VAL A 54 8228 7411 10102 -2037 743 -2735 C
ATOM 261 N ALA A 55 39.805 8.001 239.537 1.00 78.94 N
ANISOU 261 N ALA A 55 8596 9816 11582 -1777 -322 -3020 N
ATOM 262 CA ALA A 55 40.887 7.167 240.041 1.00 75.31 C
ANISOU 262 CA ALA A 55 7814 9664 11135 -1750 -638 -3232 C
ATOM 263 C ALA A 55 41.203 6.061 239.050 1.00 73.89 C
ANISOU 263 C ALA A 55 7392 9615 11066 -1611 -723 -3138 C
ATOM 264 O ALA A 55 42.372 5.818 238.715 1.00 74.48 O
ANISOU 264 O ALA A 55 7211 9873 11214 -1654 -770 -3272 O
ATOM 265 CB ALA A 55 40.509 6.581 241.403 1.00 67.73 C
ANISOU 265 CB ALA A 55 6964 8791 9980 -1544 -919 -3198 C
ATOM 266 N VAL A 56 40.165 5.392 238.543 1.00 66.06 N
ANISOU 266 N VAL A 56 6542 8522 10037 -1388 -694 -2816 N
ATOM 267 CA VAL A 56 40.400 4.337 237.565 1.00 65.62 C
ANISOU 267 CA VAL A 56 6296 8565 10070 -1264 -753 -2709 C
ATOM 268 C VAL A 56 41.034 4.917 236.306 1.00 63.38 C
ANISOU 268 C VAL A 56 5903 8211 9967 -1490 -503 -2802 C
ATOM 269 O VAL A 56 41.918 4.303 235.701 1.00 73.13 O
ANISOU 269 O VAL A 56 6906 9594 11287 -1477 -546 -2861 O
ATOM 270 CB VAL A 56 39.089 3.587 237.267 1.00 67.55 C
ANISOU 270 CB VAL A 56 6731 8704 10230 -1019 -744 -2366 C
ATOM 271 CG1 VAL A 56 39.123 2.997 235.878 1.00 78.42 C
ANISOU 271 CG1 VAL A 56 8007 10069 11718 -981 -658 -2230 C
ATOM 272 CG2 VAL A 56 38.875 2.487 238.298 1.00 61.35 C
ANISOU 272 CG2 VAL A 56 5970 8055 9285 -786 -1023 -2316 C
ATOM 273 N PHE A 57 40.649 6.142 235.936 1.00 66.99 N
ANISOU 273 N PHE A 57 6593 8423 10439 -1670 -206 -2791 N
ATOM 274 CA PHE A 57 41.176 6.758 234.721 1.00 71.76 C
ANISOU 274 CA PHE A 57 7190 8896 11178 -1894 81 -2870 C
ATOM 275 C PHE A 57 42.678 6.967 234.828 1.00 75.57 C
ANISOU 275 C PHE A 57 7448 9570 11696 -2046 91 -3122 C
ATOM 276 O PHE A 57 43.450 6.494 233.981 1.00 76.42 O
ANISOU 276 O PHE A 57 7393 9764 11879 -2039 138 -3133 O
ATOM 277 CB PHE A 57 40.448 8.088 234.478 1.00 71.90 C
ANISOU 277 CB PHE A 57 7593 8590 11136 -2009 393 -2794 C
ATOM 278 CG PHE A 57 40.894 8.846 233.248 1.00 68.43 C
ANISOU 278 CG PHE A 57 7272 7943 10786 -2241 735 -2865 C
ATOM 279 CD1 PHE A 57 40.427 8.503 231.988 1.00 69.05 C
ANISOU 279 CD1 PHE A 57 7472 7883 10882 -2122 843 -2635 C
ATOM 280 CD2 PHE A 57 41.735 9.941 233.363 1.00 79.86 C
ANISOU 280 CD2 PHE A 57 8788 9340 12214 -2505 958 -3084 C
ATOM 281 CE1 PHE A 57 40.821 9.214 230.865 1.00 60.92 C
ANISOU 281 CE1 PHE A 57 6623 6623 9901 -2329 1174 -2697 C
ATOM 282 CE2 PHE A 57 42.131 10.654 232.239 1.00 79.88 C
ANISOU 282 CE2 PHE A 57 8978 9149 12222 -2662 1298 -3095 C
ATOM 283 CZ PHE A 57 41.674 10.287 230.990 1.00 68.71 C
ANISOU 283 CZ PHE A 57 7694 7564 10848 -2577 1407 -2906 C
ATOM 284 N VAL A 58 43.116 7.646 235.890 1.00 80.34 N
ANISOU 284 N VAL A 58 8052 10245 12229 -2157 48 -3312 N
ATOM 285 CA VAL A 58 44.538 7.951 236.008 1.00 87.53 C
ANISOU 285 CA VAL A 58 8752 11336 13170 -2295 78 -3555 C
ATOM 286 C VAL A 58 45.344 6.681 236.241 1.00 80.22 C
ANISOU 286 C VAL A 58 7505 10715 12261 -2074 -230 -3591 C
ATOM 287 O VAL A 58 46.422 6.502 235.657 1.00 83.53 O
ANISOU 287 O VAL A 58 7716 11251 12769 -2119 -163 -3716 O
ATOM 288 CB VAL A 58 44.780 8.990 237.117 1.00 94.67 C
ANISOU 288 CB VAL A 58 9739 12243 13987 -2471 98 -3750 C
ATOM 289 CG1 VAL A 58 44.139 10.316 236.744 1.00 90.09 C
ANISOU 289 CG1 VAL A 58 9519 11331 13380 -2692 466 -3720 C
ATOM 290 CG2 VAL A 58 44.237 8.486 238.439 1.00 98.67 C
ANISOU 290 CG2 VAL A 58 10265 12854 14372 -2289 -238 -3719 C
ATOM 291 N VAL A 59 44.836 5.770 237.080 1.00 77.60 N
ANISOU 291 N VAL A 59 7156 10496 11831 -1822 -554 -3486 N
ATOM 292 CA VAL A 59 45.585 4.551 237.361 1.00 76.00 C
ANISOU 292 CA VAL A 59 6716 10552 11607 -1579 -842 -3508 C
ATOM 293 C VAL A 59 45.736 3.714 236.100 1.00 84.53 C
ANISOU 293 C VAL A 59 7707 11626 12785 -1482 -761 -3370 C
ATOM 294 O VAL A 59 46.814 3.174 235.826 1.00 86.20 O
ANISOU 294 O VAL A 59 7696 12003 13052 -1421 -815 -3478 O
ATOM 295 CB VAL A 59 44.911 3.753 238.492 1.00 72.09 C
ANISOU 295 CB VAL A 59 6311 10130 10948 -1320 -1173 -3406 C
ATOM 296 CG1 VAL A 59 45.451 2.334 238.525 1.00 74.29 C
ANISOU 296 CG1 VAL A 59 6436 10604 11185 -1023 -1425 -3352 C
ATOM 297 CG2 VAL A 59 45.142 4.439 239.827 1.00 71.86 C
ANISOU 297 CG2 VAL A 59 6331 10164 10808 -1397 -1302 -3594 C
ATOM 298 N ALA A 60 44.678 3.623 235.289 1.00 81.65 N
ANISOU 298 N ALA A 60 7515 11061 12446 -1474 -622 -3146 N
ATOM 299 CA ALA A 60 44.759 2.823 234.077 1.00 71.55 C
ANISOU 299 CA ALA A 60 6182 9760 11243 -1391 -546 -3003 C
ATOM 300 C ALA A 60 45.729 3.448 233.089 1.00 77.47 C
ANISOU 300 C ALA A 60 6852 10464 12118 -1613 -263 -3156 C
ATOM 301 O ALA A 60 46.618 2.768 232.562 1.00 79.79 O
ANISOU 301 O ALA A 60 6965 10878 12472 -1549 -279 -3210 O
ATOM 302 CB ALA A 60 43.369 2.668 233.460 1.00 64.38 C
ANISOU 302 CB ALA A 60 5479 8647 10336 -1343 -465 -2744 C
ATOM 303 N LEU A 61 45.612 4.762 232.862 1.00 77.08 N
ANISOU 303 N LEU A 61 6958 10232 12099 -1879 14 -3246 N
ATOM 304 CA LEU A 61 46.516 5.401 231.914 1.00 84.30 C
ANISOU 304 CA LEU A 61 7845 11077 13110 -2104 323 -3404 C
ATOM 305 C LEU A 61 47.967 5.183 232.327 1.00 84.98 C
ANISOU 305 C LEU A 61 7615 11427 13246 -2114 226 -3678 C
ATOM 306 O LEU A 61 48.788 4.698 231.533 1.00 89.63 O
ANISOU 306 O LEU A 61 8050 12080 13927 -2108 302 -3749 O
ATOM 307 CB LEU A 61 46.194 6.894 231.793 1.00 85.04 C
ANISOU 307 CB LEU A 61 8207 10924 13180 -2377 640 -3472 C
ATOM 308 CG LEU A 61 44.970 7.268 230.948 1.00 88.57 C
ANISOU 308 CG LEU A 61 9003 11046 13605 -2401 844 -3234 C
ATOM 309 CD1 LEU A 61 44.807 8.782 230.858 1.00 90.07 C
ANISOU 309 CD1 LEU A 61 9508 10976 13739 -2652 1178 -3315 C
ATOM 310 CD2 LEU A 61 45.081 6.664 229.560 1.00 79.05 C
ANISOU 310 CD2 LEU A 61 7811 9758 12466 -2363 973 -3115 C
ATOM 311 N VAL A 62 48.287 5.477 233.589 1.00 87.82 N
ANISOU 311 N VAL A 62 7875 11947 13548 -2113 40 -3839 N
ATOM 312 CA VAL A 62 49.674 5.407 234.032 1.00 90.69 C
ANISOU 312 CA VAL A 62 7932 12562 13964 -2137 -49 -4135 C
ATOM 313 C VAL A 62 50.180 3.971 233.998 1.00 90.62 C
ANISOU 313 C VAL A 62 7700 12758 13974 -1844 -318 -4093 C
ATOM 314 O VAL A 62 51.270 3.696 233.481 1.00 94.87 O
ANISOU 314 O VAL A 62 8012 13413 14621 -1866 -255 -4273 O
ATOM 315 CB VAL A 62 49.817 6.021 235.435 1.00 89.30 C
ANISOU 315 CB VAL A 62 7725 12503 13702 -2188 -214 -4302 C
ATOM 316 CG1 VAL A 62 51.192 5.703 236.009 1.00 93.07 C
ANISOU 316 CG1 VAL A 62 7854 13282 14226 -2136 -399 -4594 C
ATOM 317 CG2 VAL A 62 49.598 7.522 235.377 1.00 88.73 C
ANISOU 317 CG2 VAL A 62 7861 12230 13620 -2518 112 -4399 C
ATOM 318 N GLY A 63 49.401 3.029 234.535 1.00 81.86 N
ANISOU 318 N GLY A 63 6669 11682 12751 -1566 -603 -3866 N
ATOM 319 CA GLY A 63 49.889 1.666 234.641 1.00 82.16 C
ANISOU 319 CA GLY A 63 6544 11904 12768 -1271 -861 -3830 C
ATOM 320 C GLY A 63 50.042 0.984 233.298 1.00 87.41 C
ANISOU 320 C GLY A 63 7183 12499 13529 -1240 -707 -3719 C
ATOM 321 O GLY A 63 50.985 0.218 233.087 1.00 92.77 O
ANISOU 321 O GLY A 63 7653 13333 14263 -1116 -790 -3824 O
ATOM 322 N ASN A 64 49.131 1.252 232.362 1.00 91.77 N
ANISOU 322 N ASN A 64 7953 12814 14102 -1347 -480 -3514 N
ATOM 323 CA ASN A 64 49.274 0.641 231.048 1.00 88.25 C
ANISOU 323 CA ASN A 64 7505 12287 13740 -1335 -323 -3412 C
ATOM 324 C ASN A 64 50.422 1.272 230.271 1.00 90.88 C
ANISOU 324 C ASN A 64 7695 12614 14222 -1572 -46 -3676 C
ATOM 325 O ASN A 64 51.191 0.566 229.593 1.00 99.91 O
ANISOU 325 O ASN A 64 8687 13826 15449 -1515 -15 -3736 O
ATOM 326 CB ASN A 64 47.954 0.736 230.285 1.00 80.17 C
ANISOU 326 CB ASN A 64 6760 11013 12686 -1369 -179 -3126 C
ATOM 327 CG ASN A 64 46.898 -0.202 230.845 1.00 80.35 C
ANISOU 327 CG ASN A 64 6890 11060 12579 -1106 -440 -2869 C
ATOM 328 OD1 ASN A 64 46.928 -1.406 230.594 1.00 80.26 O
ANISOU 328 OD1 ASN A 64 6843 11118 12534 -899 -568 -2740 O
ATOM 329 ND2 ASN A 64 45.963 0.346 231.611 1.00 88.34 N
ANISOU 329 ND2 ASN A 64 8047 12005 13511 -1121 -501 -2805 N
ATOM 330 N THR A 65 50.589 2.595 230.388 1.00 90.36 N
ANISOU 330 N THR A 65 7681 12468 14186 -1844 172 -3856 N
ATOM 331 CA THR A 65 51.758 3.204 229.775 1.00 92.30 C
ANISOU 331 CA THR A 65 7785 12726 14560 -2077 446 -4153 C
ATOM 332 C THR A 65 53.035 2.625 230.364 1.00 87.16 C
ANISOU 332 C THR A 65 6765 12378 13974 -1963 238 -4420 C
ATOM 333 O THR A 65 54.014 2.412 229.638 1.00 92.40 O
ANISOU 333 O THR A 65 7251 13094 14764 -2027 382 -4606 O
ATOM 334 CB THR A 65 51.706 4.721 229.958 1.00100.80 C
ANISOU 334 CB THR A 65 9004 13670 15624 -2382 711 -4308 C
ATOM 335 OG1 THR A 65 51.364 5.023 231.315 1.00109.96 O
ANISOU 335 OG1 THR A 65 10153 14939 16687 -2328 472 -4325 O
ATOM 336 CG2 THR A 65 50.652 5.331 229.045 1.00 92.77 C
ANISOU 336 CG2 THR A 65 8369 12318 14562 -2510 997 -4083 C
ATOM 337 N LEU A 66 53.022 2.304 231.662 1.00 87.81 N
ANISOU 337 N LEU A 66 6741 12657 13965 -1775 -109 -4440 N
ATOM 338 CA LEU A 66 54.185 1.678 232.285 1.00 86.94 C
ANISOU 338 CA LEU A 66 6297 12841 13897 -1617 -351 -4682 C
ATOM 339 C LEU A 66 54.394 0.250 231.795 1.00 78.06 C
ANISOU 339 C LEU A 66 5088 11786 12787 -1340 -502 -4551 C
ATOM 340 O LEU A 66 55.531 -0.203 231.677 1.00 79.22 O
ANISOU 340 O LEU A 66 4954 12113 13033 -1278 -550 -4782 O
ATOM 341 CB LEU A 66 54.050 1.699 233.805 1.00 89.95 C
ANISOU 341 CB LEU A 66 6643 13387 14147 -1470 -688 -4720 C
ATOM 342 CG LEU A 66 54.095 3.067 234.480 1.00 93.26 C
ANISOU 342 CG LEU A 66 7087 13795 14553 -1738 -580 -4914 C
ATOM 343 CD1 LEU A 66 54.207 2.896 235.987 1.00 95.28 C
ANISOU 343 CD1 LEU A 66 7262 14255 14685 -1560 -955 -4994 C
ATOM 344 CD2 LEU A 66 55.249 3.901 233.938 1.00102.27 C
ANISOU 344 CD2 LEU A 66 8017 14984 15855 -2035 -281 -5276 C
ATOM 345 N VAL A 67 53.319 -0.487 231.523 1.00 83.70 N
ANISOU 345 N VAL A 67 6036 12365 13400 -1171 -576 -4197 N
ATOM 346 CA VAL A 67 53.488 -1.839 230.990 1.00 81.19 C
ANISOU 346 CA VAL A 67 5671 12093 13086 -929 -683 -4063 C
ATOM 347 C VAL A 67 54.221 -1.777 229.653 1.00 80.06 C
ANISOU 347 C VAL A 67 5423 11879 13117 -1104 -379 -4186 C
ATOM 348 O VAL A 67 55.214 -2.493 229.412 1.00 76.18 O
ANISOU 348 O VAL A 67 4697 11537 12712 -996 -435 -4341 O
ATOM 349 CB VAL A 67 52.119 -2.534 230.856 1.00 78.28 C
ANISOU 349 CB VAL A 67 5594 11571 12577 -765 -764 -3668 C
ATOM 350 CG1 VAL A 67 52.248 -3.872 230.138 1.00 74.65 C
ANISOU 350 CG1 VAL A 67 5119 11124 12120 -559 -812 -3519 C
ATOM 351 CG2 VAL A 67 51.481 -2.726 232.227 1.00 79.07 C
ANISOU 351 CG2 VAL A 67 5797 11748 12498 -570 -1068 -3575 C
ATOM 352 N CYS A 68 53.763 -0.878 228.777 1.00 83.08 N
ANISOU 352 N CYS A 68 5993 12023 13550 -1381 -42 -4139 N
ATOM 353 CA CYS A 68 54.416 -0.738 227.479 1.00 90.70 C
ANISOU 353 CA CYS A 68 6915 12881 14665 -1570 285 -4263 C
ATOM 354 C CYS A 68 55.862 -0.277 227.634 1.00 97.69 C
ANISOU 354 C CYS A 68 7480 13944 15693 -1711 373 -4696 C
ATOM 355 O CYS A 68 56.768 -0.820 226.989 1.00 96.08 O
ANISOU 355 O CYS A 68 7083 13808 15614 -1698 448 -4851 O
ATOM 356 CB CYS A 68 53.625 0.231 226.599 1.00 90.44 C
ANISOU 356 CB CYS A 68 7199 12539 14625 -1829 633 -4141 C
ATOM 357 SG CYS A 68 51.899 -0.247 226.332 1.00 86.02 S
ANISOU 357 SG CYS A 68 6989 11775 13919 -1680 546 -3666 S
ATOM 358 N LEU A 69 56.107 0.701 228.512 1.00 99.23 N
ANISOU 358 N LEU A 69 7601 14227 15875 -1848 361 -4910 N
ATOM 359 CA LEU A 69 57.472 1.180 228.709 1.00107.41 C
ANISOU 359 CA LEU A 69 8312 15451 17047 -1998 446 -5352 C
ATOM 360 C LEU A 69 58.366 0.092 229.284 1.00101.28 C
ANISOU 360 C LEU A 69 7192 14980 16310 -1710 108 -5495 C
ATOM 361 O LEU A 69 59.548 -0.004 228.932 1.00 94.69 O
ANISOU 361 O LEU A 69 6065 14281 15632 -1773 201 -5817 O
ATOM 362 CB LEU A 69 57.468 2.398 229.631 1.00114.91 C
ANISOU 362 CB LEU A 69 9265 16445 17951 -2189 474 -5532 C
ATOM 363 CG LEU A 69 57.177 3.743 228.970 1.00122.41 C
ANISOU 363 CG LEU A 69 10466 17132 18912 -2560 919 -5585 C
ATOM 364 CD1 LEU A 69 56.752 4.762 230.015 1.00126.02 C
ANISOU 364 CD1 LEU A 69 11021 17597 19266 -2678 877 -5623 C
ATOM 365 CD2 LEU A 69 58.405 4.226 228.217 1.00130.80 C
ANISOU 365 CD2 LEU A 69 11342 18214 20141 -2822 1266 -5977 C
ATOM 366 N ALA A 70 57.817 -0.749 230.159 1.00 97.60 N
ANISOU 366 N ALA A 70 6772 14616 15697 -1385 -275 -5270 N
ATOM 367 CA ALA A 70 58.623 -1.778 230.795 1.00 99.19 C
ANISOU 367 CA ALA A 70 6696 15096 15897 -1074 -614 -5396 C
ATOM 368 C ALA A 70 59.107 -2.777 229.764 1.00112.47 C
ANISOU 368 C ALA A 70 8283 16770 17682 -968 -541 -5369 C
ATOM 369 O ALA A 70 60.288 -3.145 229.745 1.00119.41 O
ANISOU 369 O ALA A 70 8830 17856 18684 -901 -598 -5666 O
ATOM 370 CB ALA A 70 57.815 -2.478 231.888 1.00 85.44 C
ANISOU 370 CB ALA A 70 5114 13408 13940 -748 -999 -5131 C
ATOM 371 N VAL A 71 58.215 -3.208 228.870 1.00103.20 N
ANISOU 371 N VAL A 71 7386 15359 16464 -961 -406 -5029 N
ATOM 372 CA VAL A 71 58.702 -4.149 227.865 1.00101.71 C
ANISOU 372 CA VAL A 71 7110 15158 16377 -877 -321 -5010 C
ATOM 373 C VAL A 71 59.476 -3.464 226.740 1.00 97.92 C
ANISOU 373 C VAL A 71 6521 14580 16104 -1209 86 -5276 C
ATOM 374 O VAL A 71 60.193 -4.147 226.000 1.00 98.23 O
ANISOU 374 O VAL A 71 6402 14656 16266 -1164 164 -5371 O
ATOM 375 CB VAL A 71 57.567 -5.002 227.281 1.00 99.55 C
ANISOU 375 CB VAL A 71 7148 14690 15986 -732 -332 -4571 C
ATOM 376 CG1 VAL A 71 56.952 -5.872 228.370 1.00 91.82 C
ANISOU 376 CG1 VAL A 71 6267 13820 14802 -379 -723 -4347 C
ATOM 377 CG2 VAL A 71 56.531 -4.120 226.633 1.00 97.91 C
ANISOU 377 CG2 VAL A 71 7257 14193 15752 -994 -52 -4378 C
ATOM 378 N TRP A 72 59.374 -2.136 226.587 1.00100.53 N
ANISOU 378 N TRP A 72 6948 14778 16471 -1542 368 -5411 N
ATOM 379 CA TRP A 72 60.179 -1.468 225.561 1.00103.69 C
ANISOU 379 CA TRP A 72 7272 15075 17052 -1863 782 -5704 C
ATOM 380 C TRP A 72 61.602 -1.182 226.027 1.00104.42 C
ANISOU 380 C TRP A 72 6936 15442 17297 -1934 765 -6199 C
ATOM 381 O TRP A 72 62.532 -1.236 225.216 1.00104.45 O
ANISOU 381 O TRP A 72 6760 15450 17476 -2072 1003 -6465 O
ATOM 382 CB TRP A 72 59.508 -0.165 225.108 1.00109.34 C
ANISOU 382 CB TRP A 72 8312 15507 17725 -2192 1139 -5656 C
ATOM 383 CG TRP A 72 60.442 0.833 224.429 1.00123.91 C
ANISOU 383 CG TRP A 72 10082 17277 19720 -2557 1573 -6053 C
ATOM 384 CD1 TRP A 72 61.019 1.930 225.005 1.00133.09 C
ANISOU 384 CD1 TRP A 72 11114 18536 20919 -2785 1695 -6399 C
ATOM 385 CD2 TRP A 72 60.884 0.827 223.059 1.00125.21 C
ANISOU 385 CD2 TRP A 72 10326 17244 20005 -2744 1961 -6152 C
ATOM 386 NE1 TRP A 72 61.791 2.602 224.087 1.00137.28 N
ANISOU 386 NE1 TRP A 72 11637 18944 21580 -3103 2145 -6715 N
ATOM 387 CE2 TRP A 72 61.726 1.947 222.886 1.00131.30 C
ANISOU 387 CE2 TRP A 72 11016 17997 20874 -3082 2316 -6572 C
ATOM 388 CE3 TRP A 72 60.652 -0.015 221.966 1.00126.85 C
ANISOU 388 CE3 TRP A 72 10679 17282 20238 -2666 2055 -5935 C
ATOM 389 CZ2 TRP A 72 62.337 2.246 221.666 1.00135.31 C
ANISOU 389 CZ2 TRP A 72 11601 18311 21499 -3338 2768 -6785 C
ATOM 390 CZ3 TRP A 72 61.261 0.285 220.752 1.00132.01 C
ANISOU 390 CZ3 TRP A 72 11403 17740 21012 -2918 2490 -6137 C
ATOM 391 CH2 TRP A 72 62.093 1.406 220.615 1.00137.21 C
ANISOU 391 CH2 TRP A 72 11996 18374 21762 -3247 2844 -6560 C
ATOM 392 N ARG A 73 61.797 -0.859 227.308 1.00109.82 N
ANISOU 392 N ARG A 73 7451 16353 17921 -1855 498 -6345 N
ATOM 393 CA ARG A 73 63.147 -0.622 227.809 1.00118.50 C
ANISOU 393 CA ARG A 73 8115 17746 19162 -1903 448 -6833 C
ATOM 394 C ARG A 73 63.882 -1.925 228.096 1.00126.76 C
ANISOU 394 C ARG A 73 8849 19059 20254 -1543 108 -6904 C
ATOM 395 O ARG A 73 65.065 -2.058 227.765 1.00137.72 O
ANISOU 395 O ARG A 73 9889 20609 21829 -1595 193 -7275 O
ATOM 396 CB ARG A 73 63.103 0.235 229.072 1.00128.23 C
ANISOU 396 CB ARG A 73 9288 19125 20310 -1958 290 -6977 C
ATOM 397 CG ARG A 73 62.690 1.674 228.852 1.00140.13 C
ANISOU 397 CG ARG A 73 11029 20416 21798 -2351 663 -7029 C
ATOM 398 CD ARG A 73 62.633 2.404 230.179 1.00153.46 C
ANISOU 398 CD ARG A 73 12650 22265 23392 -2377 468 -7150 C
ATOM 399 NE ARG A 73 62.127 3.765 230.042 1.00163.56 N
ANISOU 399 NE ARG A 73 14197 23325 24623 -2732 813 -7159 N
ATOM 400 CZ ARG A 73 61.766 4.530 231.068 1.00169.85 C
ANISOU 400 CZ ARG A 73 15059 24169 25309 -2801 709 -7173 C
ATOM 401 NH1 ARG A 73 61.850 4.064 232.307 1.00171.86 N
ANISOU 401 NH1 ARG A 73 15135 24677 25486 -2537 262 -7180 N
ATOM 402 NH2 ARG A 73 61.315 5.759 230.856 1.00171.61 N
ANISOU 402 NH2 ARG A 73 15550 24172 25483 -3127 1056 -7176 N
ATOM 403 N ASN A 74 63.199 -2.890 228.710 1.00116.92 N
ANISOU 403 N ASN A 74 7731 17858 18835 -1176 -264 -6566 N
ATOM 404 CA ASN A 74 63.810 -4.153 229.122 1.00114.98 C
ANISOU 404 CA ASN A 74 7246 17859 18581 -784 -616 -6604 C
ATOM 405 C ASN A 74 63.668 -5.148 227.976 1.00111.11 C
ANISOU 405 C ASN A 74 6858 17222 18137 -688 -494 -6377 C
ATOM 406 O ASN A 74 62.584 -5.686 227.731 1.00 98.57 O
ANISOU 406 O ASN A 74 5608 15442 16402 -569 -529 -5951 O
ATOM 407 CB ASN A 74 63.164 -4.664 230.405 1.00108.29 C
ANISOU 407 CB ASN A 74 6533 17115 17498 -439 -1052 -6376 C
ATOM 408 CG ASN A 74 63.897 -5.848 230.998 1.00107.89 C
ANISOU 408 CG ASN A 74 6244 17336 17413 -18 -1431 -6473 C
ATOM 409 OD1 ASN A 74 64.473 -6.662 230.279 1.00109.30 O
ANISOU 409 OD1 ASN A 74 6276 17555 17696 98 -1391 -6516 O
ATOM 410 ND2 ASN A 74 63.876 -5.951 232.320 1.00109.41 N
ANISOU 410 ND2 ASN A 74 6416 17707 17448 226 -1800 -6510 N
ATOM 411 N HIS A 75 64.769 -5.380 227.257 1.00111.06 N
ANISOU 411 N HIS A 75 6551 17306 18339 -755 -336 -6676 N
ATOM 412 CA HIS A 75 64.729 -6.292 226.120 1.00112.88 C
ANISOU 412 CA HIS A 75 6860 17397 18633 -689 -191 -6490 C
ATOM 413 C HIS A 75 64.480 -7.732 226.553 1.00113.41 C
ANISOU 413 C HIS A 75 6965 17575 18551 -221 -565 -6216 C
ATOM 414 O HIS A 75 63.977 -8.537 225.761 1.00109.20 O
ANISOU 414 O HIS A 75 6632 16876 17983 -132 -483 -5911 O
ATOM 415 CB HIS A 75 66.029 -6.189 225.320 1.00117.10 C
ANISOU 415 CB HIS A 75 7044 18014 19435 -870 67 -6912 C
ATOM 416 CG HIS A 75 66.131 -4.946 224.491 1.00126.04 C
ANISOU 416 CG HIS A 75 8263 18926 20699 -1351 549 -7110 C
ATOM 417 ND1 HIS A 75 65.679 -3.718 224.926 1.00128.22 N
ANISOU 417 ND1 HIS A 75 8696 19117 20905 -1600 662 -7153 N
ATOM 418 CD2 HIS A 75 66.635 -4.743 223.251 1.00129.14 C
ANISOU 418 CD2 HIS A 75 8639 19151 21276 -1625 965 -7280 C
ATOM 419 CE1 HIS A 75 65.900 -2.812 223.989 1.00128.13 C
ANISOU 419 CE1 HIS A 75 8776 18893 21017 -1997 1131 -7341 C
ATOM 420 NE2 HIS A 75 66.480 -3.409 222.963 1.00129.35 N
ANISOU 420 NE2 HIS A 75 8836 18987 21325 -2024 1324 -7425 N
ATOM 421 N HIS A 76 64.830 -8.082 227.790 1.00115.91 N
ANISOU 421 N HIS A 76 7113 18161 18768 83 -964 -6327 N
ATOM 422 CA HIS A 76 64.666 -9.454 228.251 1.00117.66 C
ANISOU 422 CA HIS A 76 7401 18480 18824 549 -1311 -6099 C
ATOM 423 C HIS A 76 63.221 -9.799 228.586 1.00109.73 C
ANISOU 423 C HIS A 76 6856 17278 17560 681 -1426 -5619 C
ATOM 424 O HIS A 76 62.912 -10.982 228.765 1.00107.90 O
ANISOU 424 O HIS A 76 6768 17054 17174 1033 -1636 -5375 O
ATOM 425 CB HIS A 76 65.560 -9.710 229.464 1.00122.08 C
ANISOU 425 CB HIS A 76 7655 19383 19347 850 -1701 -6403 C
ATOM 426 CG HIS A 76 67.019 -9.512 229.185 1.00133.12 C
ANISOU 426 CG HIS A 76 8558 21017 21004 768 -1627 -6899 C
ATOM 427 ND1 HIS A 76 67.524 -9.373 227.910 1.00129.16 N
ANISOU 427 ND1 HIS A 76 7916 20420 20741 500 -1249 -7035 N
ATOM 428 CD2 HIS A 76 68.080 -9.426 230.021 1.00134.00 C
ANISOU 428 CD2 HIS A 76 8279 21458 21175 917 -1878 -7313 C
ATOM 429 CE1 HIS A 76 68.834 -9.211 227.972 1.00126.77 C
ANISOU 429 CE1 HIS A 76 7147 20379 20642 477 -1259 -7517 C
ATOM 430 NE2 HIS A 76 69.196 -9.239 229.241 1.00138.52 N
ANISOU 430 NE2 HIS A 76 8463 22140 22029 732 -1646 -7697 N
ATOM 431 N MET A 77 62.341 -8.809 228.687 1.00103.60 N
ANISOU 431 N MET A 77 6312 16325 16726 415 -1287 -5493 N
ATOM 432 CA MET A 77 60.924 -9.055 228.910 1.00107.28 C
ANISOU 432 CA MET A 77 7198 16593 16970 498 -1355 -5058 C
ATOM 433 C MET A 77 60.129 -9.188 227.615 1.00103.27 C
ANISOU 433 C MET A 77 6945 15799 16494 322 -1042 -4761 C
ATOM 434 O MET A 77 58.902 -9.322 227.673 1.00101.80 O
ANISOU 434 O MET A 77 7096 15440 16144 353 -1060 -4413 O
ATOM 435 CB MET A 77 60.321 -7.944 229.777 1.00108.09 C
ANISOU 435 CB MET A 77 7424 16662 16982 336 -1396 -5067 C
ATOM 436 CG MET A 77 60.765 -7.994 231.230 1.00116.50 C
ANISOU 436 CG MET A 77 8351 17977 17936 579 -1770 -5254 C
ATOM 437 SD MET A 77 59.736 -6.967 232.286 1.00120.06 S
ANISOU 437 SD MET A 77 9053 18343 18223 453 -1846 -5140 S
ATOM 438 CE MET A 77 59.937 -5.381 231.487 1.00117.01 C
ANISOU 438 CE MET A 77 8567 17837 18054 -77 -1411 -5354 C
ATOM 439 N ARG A 78 60.787 -9.140 226.454 1.00102.63 N
ANISOU 439 N ARG A 78 6713 15662 16617 135 -751 -4904 N
ATOM 440 CA ARG A 78 60.091 -9.147 225.164 1.00102.39 C
ANISOU 440 CA ARG A 78 6931 15348 16626 -63 -427 -4658 C
ATOM 441 C ARG A 78 59.754 -10.584 224.754 1.00 99.27 C
ANISOU 441 C ARG A 78 6658 14918 16141 230 -520 -4364 C
ATOM 442 O ARG A 78 60.264 -11.134 223.776 1.00107.16 O
ANISOU 442 O ARG A 78 7568 15881 17268 219 -345 -4395 O
ATOM 443 CB ARG A 78 60.931 -8.443 224.106 1.00 97.52 C
ANISOU 443 CB ARG A 78 6146 14654 16252 -403 -49 -4950 C
ATOM 444 CG ARG A 78 61.181 -6.964 224.391 1.00100.30 C
ANISOU 444 CG ARG A 78 6435 14995 16680 -730 113 -5232 C
ATOM 445 CD ARG A 78 61.817 -6.258 223.198 1.00103.93 C
ANISOU 445 CD ARG A 78 6842 15298 17348 -1095 559 -5480 C
ATOM 446 NE ARG A 78 62.090 -4.847 223.469 1.00106.21 N
ANISOU 446 NE ARG A 78 7090 15570 17694 -1409 745 -5769 N
ATOM 447 CZ ARG A 78 62.612 -4.003 222.584 1.00108.37 C
ANISOU 447 CZ ARG A 78 7366 15690 18120 -1762 1162 -6026 C
ATOM 448 NH1 ARG A 78 62.917 -4.423 221.364 1.00113.08 N
ANISOU 448 NH1 ARG A 78 8003 16129 18832 -1850 1430 -6029 N
ATOM 449 NH2 ARG A 78 62.828 -2.737 222.915 1.00109.10 N
ANISOU 449 NH2 ARG A 78 7443 15774 18238 -2032 1332 -6284 N
ATOM 450 N THR A 79 58.862 -11.191 225.530 1.00 90.08 N
ANISOU 450 N THR A 79 5720 13758 14748 492 -784 -4082 N
ATOM 451 CA THR A 79 58.353 -12.530 225.269 1.00 88.09 C
ANISOU 451 CA THR A 79 5651 13454 14365 776 -872 -3777 C
ATOM 452 C THR A 79 56.991 -12.460 224.583 1.00 91.20 C
ANISOU 452 C THR A 79 6398 13579 14674 630 -689 -3426 C
ATOM 453 O THR A 79 56.337 -11.415 224.542 1.00 91.73 O
ANISOU 453 O THR A 79 6595 13514 14744 370 -564 -3391 O
ATOM 454 CB THR A 79 58.252 -13.331 226.570 1.00 85.38 C
ANISOU 454 CB THR A 79 5368 13270 13802 1174 -1266 -3710 C
ATOM 455 OG1 THR A 79 57.162 -12.832 227.356 1.00 81.44 O
ANISOU 455 OG1 THR A 79 5128 12688 13129 1137 -1371 -3540 O
ATOM 456 CG2 THR A 79 59.535 -13.192 227.369 1.00 83.27 C
ANISOU 456 CG2 THR A 79 4754 13278 13608 1303 -1473 -4088 C
ATOM 457 N VAL A 80 56.561 -13.603 224.044 1.00 85.60 N
ANISOU 457 N VAL A 80 5846 12791 13887 816 -675 -3171 N
ATOM 458 CA VAL A 80 55.265 -13.657 223.371 1.00 85.76 C
ANISOU 458 CA VAL A 80 6184 12576 13827 705 -517 -2850 C
ATOM 459 C VAL A 80 54.155 -13.220 224.319 1.00 74.31 C
ANISOU 459 C VAL A 80 4954 11088 12193 717 -684 -2694 C
ATOM 460 O VAL A 80 53.292 -12.402 223.963 1.00 69.06 O
ANISOU 460 O VAL A 80 4450 10255 11533 473 -529 -2587 O
ATOM 461 CB VAL A 80 55.014 -15.075 222.819 1.00 62.78 C
ANISOU 461 CB VAL A 80 3400 9616 10836 951 -510 -2622 C
ATOM 462 CG1 VAL A 80 53.548 -15.255 222.434 1.00 57.92 C
ANISOU 462 CG1 VAL A 80 3119 8796 10090 901 -430 -2292 C
ATOM 463 CG2 VAL A 80 55.913 -15.353 221.624 1.00 64.78 C
ANISOU 463 CG2 VAL A 80 3481 9840 11291 862 -256 -2744 C
ATOM 464 N THR A 81 54.187 -13.717 225.558 1.00 80.93 N
ANISOU 464 N THR A 81 5810 12074 12867 1004 -996 -2696 N
ATOM 465 CA THR A 81 53.140 -13.376 226.512 1.00 76.21 C
ANISOU 465 CA THR A 81 5434 11434 12086 1029 -1150 -2555 C
ATOM 466 C THR A 81 53.132 -11.883 226.796 1.00 75.58 C
ANISOU 466 C THR A 81 5275 11342 12098 736 -1075 -2718 C
ATOM 467 O THR A 81 52.075 -11.247 226.790 1.00 72.46 O
ANISOU 467 O THR A 81 5075 10805 11652 579 -1000 -2567 O
ATOM 468 CB THR A 81 53.331 -14.158 227.813 1.00 74.32 C
ANISOU 468 CB THR A 81 5246 11344 11649 1390 -1486 -2574 C
ATOM 469 OG1 THR A 81 53.264 -15.562 227.543 1.00 82.50 O
ANISOU 469 OG1 THR A 81 6415 12358 12572 1674 -1535 -2407 O
ATOM 470 CG2 THR A 81 52.246 -13.791 228.812 1.00 78.21 C
ANISOU 470 CG2 THR A 81 5984 11778 11955 1402 -1623 -2445 C
ATOM 471 N ASN A 82 54.308 -11.304 227.050 1.00 73.27 N
ANISOU 471 N ASN A 82 4696 11200 11943 666 -1090 -3042 N
ATOM 472 CA ASN A 82 54.372 -9.875 227.338 1.00 78.18 C
ANISOU 472 CA ASN A 82 5247 11811 12649 387 -999 -3222 C
ATOM 473 C ASN A 82 54.001 -9.028 226.127 1.00 82.02 C
ANISOU 473 C ASN A 82 5817 12079 13269 40 -642 -3181 C
ATOM 474 O ASN A 82 53.447 -7.937 226.289 1.00 84.68 O
ANISOU 474 O ASN A 82 6259 12315 13601 -170 -547 -3182 O
ATOM 475 CB ASN A 82 55.760 -9.500 227.856 1.00 82.03 C
ANISOU 475 CB ASN A 82 5393 12520 13255 388 -1085 -3608 C
ATOM 476 CG ASN A 82 56.014 -10.013 229.263 1.00 85.96 C
ANISOU 476 CG ASN A 82 5848 13219 13594 708 -1460 -3675 C
ATOM 477 OD1 ASN A 82 55.081 -10.328 230.006 1.00 86.06 O
ANISOU 477 OD1 ASN A 82 6114 13182 13402 866 -1632 -3459 O
ATOM 478 ND2 ASN A 82 57.283 -10.092 229.638 1.00 91.59 N
ANISOU 478 ND2 ASN A 82 6248 14155 14396 808 -1584 -3994 N
ATOM 479 N TYR A 83 54.275 -9.509 224.911 1.00 77.76 N
ANISOU 479 N TYR A 83 5260 11449 12836 -16 -434 -3143 N
ATOM 480 CA TYR A 83 53.801 -8.791 223.733 1.00 69.56 C
ANISOU 480 CA TYR A 83 4375 10165 11888 -319 -96 -3073 C
ATOM 481 C TYR A 83 52.281 -8.758 223.696 1.00 70.25 C
ANISOU 481 C TYR A 83 4781 10084 11829 -319 -107 -2744 C
ATOM 482 O TYR A 83 51.671 -7.706 223.442 1.00 74.62 O
ANISOU 482 O TYR A 83 5483 10476 12395 -548 58 -2716 O
ATOM 483 CB TYR A 83 54.353 -9.437 222.462 1.00 68.02 C
ANISOU 483 CB TYR A 83 4129 9896 11820 -356 120 -3084 C
ATOM 484 CG TYR A 83 55.717 -8.925 222.055 1.00 86.52 C
ANISOU 484 CG TYR A 83 6206 12299 14369 -532 303 -3448 C
ATOM 485 CD1 TYR A 83 56.158 -7.674 222.462 1.00 93.61 C
ANISOU 485 CD1 TYR A 83 7005 13224 15338 -750 383 -3715 C
ATOM 486 CD2 TYR A 83 56.561 -9.690 221.260 1.00 86.66 C
ANISOU 486 CD2 TYR A 83 6074 12342 14510 -487 416 -3538 C
ATOM 487 CE1 TYR A 83 57.400 -7.201 222.093 1.00 97.14 C
ANISOU 487 CE1 TYR A 83 7207 13727 15974 -928 572 -4077 C
ATOM 488 CE2 TYR A 83 57.806 -9.222 220.886 1.00 92.37 C
ANISOU 488 CE2 TYR A 83 6544 13120 15432 -660 599 -3896 C
ATOM 489 CZ TYR A 83 58.219 -7.978 221.305 1.00100.71 C
ANISOU 489 CZ TYR A 83 7503 14206 16555 -884 678 -4172 C
ATOM 490 OH TYR A 83 59.457 -7.500 220.939 1.00107.15 O
ANISOU 490 OH TYR A 83 8064 15077 17570 -1073 881 -4559 O
ATOM 491 N PHE A 84 51.645 -9.896 223.978 1.00 64.81 N
ANISOU 491 N PHE A 84 4203 9428 10992 -57 -296 -2507 N
ATOM 492 CA PHE A 84 50.189 -9.895 224.021 1.00 64.26 C
ANISOU 492 CA PHE A 84 4410 9220 10788 -51 -318 -2223 C
ATOM 493 C PHE A 84 49.670 -9.020 225.157 1.00 60.80 C
ANISOU 493 C PHE A 84 4025 8814 10261 -82 -457 -2251 C
ATOM 494 O PHE A 84 48.637 -8.354 225.014 1.00 65.78 O
ANISOU 494 O PHE A 84 4839 9296 10859 -216 -373 -2117 O
ATOM 495 CB PHE A 84 49.676 -11.328 224.147 1.00 70.37 C
ANISOU 495 CB PHE A 84 5295 10028 11416 235 -476 -1999 C
ATOM 496 CG PHE A 84 49.664 -12.080 222.847 1.00 77.19 C
ANISOU 496 CG PHE A 84 6203 10780 12347 219 -284 -1884 C
ATOM 497 CD1 PHE A 84 49.088 -11.521 221.716 1.00 76.07 C
ANISOU 497 CD1 PHE A 84 6194 10423 12287 -31 -20 -1795 C
ATOM 498 CD2 PHE A 84 50.238 -13.338 222.750 1.00 75.25 C
ANISOU 498 CD2 PHE A 84 5887 10627 12077 462 -358 -1869 C
ATOM 499 CE1 PHE A 84 49.076 -12.206 220.516 1.00 67.75 C
ANISOU 499 CE1 PHE A 84 5201 9249 11294 -58 170 -1695 C
ATOM 500 CE2 PHE A 84 50.231 -14.025 221.553 1.00 70.09 C
ANISOU 500 CE2 PHE A 84 5280 9862 11491 443 -161 -1770 C
ATOM 501 CZ PHE A 84 49.647 -13.459 220.435 1.00 68.68 C
ANISOU 501 CZ PHE A 84 5231 9466 11399 172 106 -1685 C
ATOM 502 N LEU A 85 50.374 -8.997 226.290 1.00 66.90 N
ANISOU 502 N LEU A 85 4643 9778 11000 46 -671 -2432 N
ATOM 503 CA LEU A 85 49.933 -8.154 227.396 1.00 70.38 C
ANISOU 503 CA LEU A 85 5133 10246 11360 11 -794 -2476 C
ATOM 504 C LEU A 85 50.055 -6.678 227.042 1.00 73.55 C
ANISOU 504 C LEU A 85 5503 10548 11893 -312 -564 -2630 C
ATOM 505 O LEU A 85 49.236 -5.855 227.470 1.00 73.40 O
ANISOU 505 O LEU A 85 5621 10445 11822 -412 -553 -2571 O
ATOM 506 CB LEU A 85 50.734 -8.480 228.656 1.00 69.87 C
ANISOU 506 CB LEU A 85 4915 10404 11227 224 -1074 -2657 C
ATOM 507 CG LEU A 85 50.473 -9.873 229.238 1.00 69.43 C
ANISOU 507 CG LEU A 85 4974 10418 10986 572 -1318 -2500 C
ATOM 508 CD1 LEU A 85 51.289 -10.091 230.498 1.00 65.06 C
ANISOU 508 CD1 LEU A 85 4298 10069 10353 789 -1598 -2701 C
ATOM 509 CD2 LEU A 85 48.990 -10.060 229.522 1.00 60.77 C
ANISOU 509 CD2 LEU A 85 4177 9187 9726 617 -1355 -2224 C
ATOM 510 N VAL A 86 51.063 -6.326 226.245 1.00 81.35 N
ANISOU 510 N VAL A 86 6329 11531 13049 -480 -358 -2837 N
ATOM 511 CA VAL A 86 51.170 -4.955 225.762 1.00 75.67 C
ANISOU 511 CA VAL A 86 5637 10675 12440 -799 -82 -2982 C
ATOM 512 C VAL A 86 49.999 -4.627 224.849 1.00 72.17 C
ANISOU 512 C VAL A 86 5479 9970 11971 -929 120 -2736 C
ATOM 513 O VAL A 86 49.447 -3.520 224.892 1.00 69.55 O
ANISOU 513 O VAL A 86 5290 9505 11633 -1108 248 -2737 O
ATOM 514 CB VAL A 86 52.516 -4.741 225.050 1.00 74.31 C
ANISOU 514 CB VAL A 86 5250 10538 12446 -952 125 -3271 C
ATOM 515 CG1 VAL A 86 52.580 -3.346 224.454 1.00 71.66 C
ANISOU 515 CG1 VAL A 86 5011 10019 12198 -1291 462 -3414 C
ATOM 516 CG2 VAL A 86 53.657 -4.964 226.015 1.00 83.16 C
ANISOU 516 CG2 VAL A 86 6062 11935 13600 -823 -91 -3545 C
ATOM 517 N ASN A 87 49.583 -5.588 224.020 1.00 67.15 N
ANISOU 517 N ASN A 87 4941 9256 11316 -832 148 -2524 N
ATOM 518 CA ASN A 87 48.402 -5.338 223.197 1.00 66.03 C
ANISOU 518 CA ASN A 87 5070 8877 11140 -929 306 -2287 C
ATOM 519 C ASN A 87 47.160 -5.153 224.067 1.00 68.64 C
ANISOU 519 C ASN A 87 5541 9201 11337 -838 125 -2111 C
ATOM 520 O ASN A 87 46.298 -4.310 223.777 1.00 70.09 O
ANISOU 520 O ASN A 87 5910 9208 11515 -977 253 -2024 O
ATOM 521 CB ASN A 87 48.195 -6.479 222.204 1.00 63.18 C
ANISOU 521 CB ASN A 87 4776 8451 10779 -837 355 -2102 C
ATOM 522 CG ASN A 87 47.227 -6.112 221.103 1.00 65.02 C
ANISOU 522 CG ASN A 87 5277 8418 11010 -984 575 -1914 C
ATOM 523 OD1 ASN A 87 47.354 -5.053 220.487 1.00 68.58 O
ANISOU 523 OD1 ASN A 87 5845 8691 11520 -1213 828 -2003 O
ATOM 524 ND2 ASN A 87 46.244 -6.975 220.857 1.00 60.01 N
ANISOU 524 ND2 ASN A 87 4766 7742 10292 -851 485 -1656 N
ATOM 525 N LEU A 88 47.057 -5.930 225.148 1.00 66.11 N
ANISOU 525 N LEU A 88 5152 9061 10904 -600 -165 -2066 N
ATOM 526 CA LEU A 88 45.923 -5.785 226.057 1.00 62.32 C
ANISOU 526 CA LEU A 88 4807 8577 10295 -512 -328 -1926 C
ATOM 527 C LEU A 88 45.929 -4.410 226.709 1.00 72.82 C
ANISOU 527 C LEU A 88 6130 9884 11654 -679 -285 -2083 C
ATOM 528 O LEU A 88 44.873 -3.787 226.886 1.00 74.14 O
ANISOU 528 O LEU A 88 6452 9933 11784 -737 -261 -1977 O
ATOM 529 CB LEU A 88 45.966 -6.891 227.116 1.00 56.20 C
ANISOU 529 CB LEU A 88 3995 7981 9378 -228 -620 -1881 C
ATOM 530 CG LEU A 88 44.990 -6.891 228.298 1.00 62.60 C
ANISOU 530 CG LEU A 88 4935 8814 10034 -106 -814 -1784 C
ATOM 531 CD1 LEU A 88 43.564 -6.988 227.820 1.00 53.68 C
ANISOU 531 CD1 LEU A 88 4007 7530 8858 -122 -746 -1542 C
ATOM 532 CD2 LEU A 88 45.308 -8.047 229.245 1.00 61.51 C
ANISOU 532 CD2 LEU A 88 4786 8833 9750 178 -1070 -1781 C
ATOM 533 N SER A 89 47.120 -3.911 227.044 1.00 71.50 N
ANISOU 533 N SER A 89 5777 9825 11563 -764 -264 -2351 N
ATOM 534 CA SER A 89 47.236 -2.556 227.570 1.00 77.58 C
ANISOU 534 CA SER A 89 6543 10565 12367 -959 -180 -2529 C
ATOM 535 C SER A 89 46.868 -1.512 226.525 1.00 77.95 C
ANISOU 535 C SER A 89 6760 10363 12493 -1220 148 -2515 C
ATOM 536 O SER A 89 46.316 -0.463 226.870 1.00 75.68 O
ANISOU 536 O SER A 89 6597 9968 12188 -1351 225 -2534 O
ATOM 537 CB SER A 89 48.654 -2.310 228.085 1.00 78.16 C
ANISOU 537 CB SER A 89 6363 10823 12511 -1000 -216 -2843 C
ATOM 538 OG SER A 89 48.951 -3.176 229.166 1.00 81.66 O
ANISOU 538 OG SER A 89 6686 11481 12860 -742 -535 -2863 O
ATOM 539 N LEU A 90 47.154 -1.774 225.248 1.00 70.52 N
ANISOU 539 N LEU A 90 5859 9306 11628 -1295 355 -2482 N
ATOM 540 CA LEU A 90 46.742 -0.833 224.211 1.00 73.27 C
ANISOU 540 CA LEU A 90 6444 9380 12016 -1521 674 -2445 C
ATOM 541 C LEU A 90 45.224 -0.761 224.120 1.00 74.37 C
ANISOU 541 C LEU A 90 6818 9361 12079 -1466 635 -2177 C
ATOM 542 O LEU A 90 44.644 0.326 224.011 1.00 76.61 O
ANISOU 542 O LEU A 90 7307 9451 12351 -1614 796 -2168 O
ATOM 543 CB LEU A 90 47.338 -1.234 222.861 1.00 79.63 C
ANISOU 543 CB LEU A 90 7276 10081 12897 -1595 898 -2454 C
ATOM 544 CG LEU A 90 48.849 -1.110 222.667 1.00 85.98 C
ANISOU 544 CG LEU A 90 7872 10984 13813 -1706 1032 -2756 C
ATOM 545 CD1 LEU A 90 49.239 -1.595 221.282 1.00 83.21 C
ANISOU 545 CD1 LEU A 90 7594 10497 13526 -1765 1259 -2728 C
ATOM 546 CD2 LEU A 90 49.298 0.322 222.877 1.00 84.33 C
ANISOU 546 CD2 LEU A 90 7708 10702 13631 -1953 1252 -2997 C
ATOM 547 N ALA A 91 44.562 -1.916 224.183 1.00 69.82 N
ANISOU 547 N ALA A 91 6224 8859 11445 -1250 429 -1967 N
ATOM 548 CA ALA A 91 43.103 -1.918 224.135 1.00 64.52 C
ANISOU 548 CA ALA A 91 5734 8063 10719 -1185 377 -1734 C
ATOM 549 C ALA A 91 42.509 -1.245 225.371 1.00 67.78 C
ANISOU 549 C ALA A 91 6153 8518 11082 -1164 243 -1771 C
ATOM 550 O ALA A 91 41.532 -0.482 225.274 1.00 69.12 O
ANISOU 550 O ALA A 91 6503 8504 11257 -1232 326 -1689 O
ATOM 551 CB ALA A 91 42.599 -3.352 223.992 1.00 51.36 C
ANISOU 551 CB ALA A 91 4039 6488 8989 -963 197 -1527 C
ATOM 552 N ASP A 92 43.109 -1.495 226.539 1.00 69.40 N
ANISOU 552 N ASP A 92 6186 8944 11238 -1066 41 -1900 N
ATOM 553 CA ASP A 92 42.651 -0.838 227.756 1.00 69.39 C
ANISOU 553 CA ASP A 92 6201 8980 11185 -1062 -76 -1959 C
ATOM 554 C ASP A 92 42.871 0.668 227.702 1.00 72.74 C
ANISOU 554 C ASP A 92 6712 9254 11671 -1321 154 -2128 C
ATOM 555 O ASP A 92 42.042 1.425 228.210 1.00 74.95 O
ANISOU 555 O ASP A 92 7120 9426 11932 -1370 167 -2108 O
ATOM 556 CB ASP A 92 43.362 -1.435 228.972 1.00 75.55 C
ANISOU 556 CB ASP A 92 6811 10011 11885 -906 -334 -2074 C
ATOM 557 CG ASP A 92 42.876 -2.830 229.301 1.00 78.00 C
ANISOU 557 CG ASP A 92 7134 10425 12077 -636 -560 -1891 C
ATOM 558 OD1 ASP A 92 41.850 -3.248 228.733 1.00 70.39 O
ANISOU 558 OD1 ASP A 92 6296 9355 11092 -580 -531 -1679 O
ATOM 559 OD2 ASP A 92 43.521 -3.508 230.126 1.00 86.18 O
ANISOU 559 OD2 ASP A 92 8071 11639 13035 -479 -760 -1967 O
ATOM 560 N VAL A 93 43.966 1.121 227.086 1.00 66.88 N
ANISOU 560 N VAL A 93 5926 8486 10999 -1493 360 -2301 N
ATOM 561 CA VAL A 93 44.209 2.554 226.967 1.00 70.15 C
ANISOU 561 CA VAL A 93 6480 8733 11440 -1751 627 -2461 C
ATOM 562 C VAL A 93 43.223 3.184 225.996 1.00 73.65 C
ANISOU 562 C VAL A 93 7257 8847 11878 -1846 864 -2296 C
ATOM 563 O VAL A 93 42.747 4.301 226.218 1.00 72.70 O
ANISOU 563 O VAL A 93 7359 8540 11724 -1969 1006 -2324 O
ATOM 564 CB VAL A 93 45.664 2.825 226.547 1.00 74.59 C
ANISOU 564 CB VAL A 93 6911 9359 12073 -1906 805 -2707 C
ATOM 565 CG1 VAL A 93 45.843 4.294 226.185 1.00 76.18 C
ANISOU 565 CG1 VAL A 93 7335 9337 12273 -2183 1150 -2845 C
ATOM 566 CG2 VAL A 93 46.621 2.439 227.665 1.00 76.89 C
ANISOU 566 CG2 VAL A 93 6893 9954 12370 -1820 566 -2907 C
ATOM 567 N LEU A 94 42.883 2.478 224.917 1.00 74.74 N
ANISOU 567 N LEU A 94 7474 8891 12035 -1776 908 -2116 N
ATOM 568 CA LEU A 94 41.853 2.989 224.020 1.00 74.37 C
ANISOU 568 CA LEU A 94 7781 8514 11962 -1820 1090 -1936 C
ATOM 569 C LEU A 94 40.555 3.217 224.783 1.00 72.63 C
ANISOU 569 C LEU A 94 7726 8279 11591 -1602 910 -1738 C
ATOM 570 O LEU A 94 39.994 4.327 224.779 1.00 71.82 O
ANISOU 570 O LEU A 94 7929 7955 11403 -1638 1055 -1705 O
ATOM 571 CB LEU A 94 41.642 2.013 222.859 1.00 77.39 C
ANISOU 571 CB LEU A 94 8226 8849 12329 -1707 1093 -1734 C
ATOM 572 CG LEU A 94 40.453 2.243 221.920 1.00 79.79 C
ANISOU 572 CG LEU A 94 8953 8892 12472 -1572 1156 -1444 C
ATOM 573 CD1 LEU A 94 40.601 3.560 221.172 1.00 87.88 C
ANISOU 573 CD1 LEU A 94 10360 9574 13457 -1769 1499 -1513 C
ATOM 574 CD2 LEU A 94 40.295 1.086 220.943 1.00 69.51 C
ANISOU 574 CD2 LEU A 94 7654 7607 11150 -1457 1101 -1264 C
ATOM 575 N ALA A 95 40.097 2.186 225.500 1.00 62.29 N
ANISOU 575 N ALA A 95 6227 7198 10241 -1377 611 -1624 N
ATOM 576 CA ALA A 95 38.866 2.331 226.268 1.00 56.50 C
ANISOU 576 CA ALA A 95 5627 6463 9379 -1185 462 -1460 C
ATOM 577 C ALA A 95 38.992 3.459 227.284 1.00 62.19 C
ANISOU 577 C ALA A 95 6388 7150 10090 -1301 512 -1631 C
ATOM 578 O ALA A 95 38.173 4.381 227.305 1.00 67.81 O
ANISOU 578 O ALA A 95 7380 7668 10716 -1269 616 -1545 O
ATOM 579 CB ALA A 95 38.511 1.012 226.957 1.00 47.99 C
ANISOU 579 CB ALA A 95 4352 5626 8256 -972 175 -1359 C
ATOM 580 N THR A 96 40.064 3.444 228.079 1.00 71.44 N
ANISOU 580 N THR A 96 7291 8502 11350 -1440 450 -1891 N
ATOM 581 CA THR A 96 40.194 4.386 229.184 1.00 73.96 C
ANISOU 581 CA THR A 96 7629 8826 11647 -1551 457 -2066 C
ATOM 582 C THR A 96 40.254 5.827 228.698 1.00 75.13 C
ANISOU 582 C THR A 96 8066 8689 11792 -1773 787 -2151 C
ATOM 583 O THR A 96 39.668 6.722 229.321 1.00 82.30 O
ANISOU 583 O THR A 96 9186 9474 12610 -1774 841 -2140 O
ATOM 584 CB THR A 96 41.452 4.062 229.988 1.00 75.03 C
ANISOU 584 CB THR A 96 7396 9230 11881 -1664 313 -2366 C
ATOM 585 OG1 THR A 96 41.322 2.769 230.590 1.00 83.10 O
ANISOU 585 OG1 THR A 96 8231 10487 12857 -1414 -4 -2277 O
ATOM 586 CG2 THR A 96 41.683 5.109 231.067 1.00 72.02 C
ANISOU 586 CG2 THR A 96 7053 8848 11461 -1812 337 -2569 C
ATOM 587 N ALA A 97 40.951 6.077 227.588 1.00 73.73 N
ANISOU 587 N ALA A 97 7938 8379 11697 -1965 1035 -2239 N
ATOM 588 CA ALA A 97 41.152 7.451 227.156 1.00 76.17 C
ANISOU 588 CA ALA A 97 8564 8392 11985 -2211 1388 -2358 C
ATOM 589 C ALA A 97 39.934 7.990 226.425 1.00 74.59 C
ANISOU 589 C ALA A 97 8832 7881 11628 -2034 1508 -2073 C
ATOM 590 O ALA A 97 39.529 9.136 226.661 1.00 72.98 O
ANISOU 590 O ALA A 97 8948 7455 11325 -2080 1677 -2085 O
ATOM 591 CB ALA A 97 42.391 7.553 226.266 1.00 68.79 C
ANISOU 591 CB ALA A 97 7584 7481 11072 -2372 1606 -2491 C
ATOM 592 N ILE A 98 39.317 7.196 225.556 1.00 68.12 N
ANISOU 592 N ILE A 98 8069 7044 10771 -1817 1415 -1824 N
ATOM 593 CA ILE A 98 38.240 7.698 224.715 1.00 70.05 C
ANISOU 593 CA ILE A 98 8748 7004 10865 -1636 1513 -1582 C
ATOM 594 C ILE A 98 36.871 7.434 225.329 1.00 73.63 C
ANISOU 594 C ILE A 98 9211 7545 11222 -1309 1259 -1360 C
ATOM 595 O ILE A 98 36.052 8.343 225.436 1.00 78.44 O
ANISOU 595 O ILE A 98 10126 7962 11717 -1193 1333 -1278 O
ATOM 596 CB ILE A 98 38.348 7.103 223.294 1.00 77.40 C
ANISOU 596 CB ILE A 98 9780 7834 11792 -1609 1584 -1461 C
ATOM 597 CG1 ILE A 98 39.695 7.480 222.669 1.00 72.03 C
ANISOU 597 CG1 ILE A 98 9125 7030 11213 -1962 1902 -1709 C
ATOM 598 CG2 ILE A 98 37.206 7.599 222.421 1.00 79.41 C
ANISOU 598 CG2 ILE A 98 10493 7811 11867 -1381 1635 -1217 C
ATOM 599 CD1 ILE A 98 39.998 8.966 222.730 1.00 77.16 C
ANISOU 599 CD1 ILE A 98 10116 7428 11774 -2160 2219 -1857 C
ATOM 600 N CYS A 99 36.598 6.189 225.730 1.00 70.08 N
ANISOU 600 N CYS A 99 8442 7374 10812 -1156 977 -1271 N
ATOM 601 CA CYS A 99 35.248 5.816 226.134 1.00 63.98 C
ANISOU 601 CA CYS A 99 7678 6676 9956 -866 773 -1068 C
ATOM 602 C CYS A 99 34.956 6.134 227.596 1.00 63.48 C
ANISOU 602 C CYS A 99 7525 6714 9878 -843 682 -1145 C
ATOM 603 O CYS A 99 33.813 6.467 227.931 1.00 69.10 O
ANISOU 603 O CYS A 99 8368 7373 10512 -650 640 -1025 O
ATOM 604 CB CYS A 99 35.036 4.326 225.865 1.00 63.14 C
ANISOU 604 CB CYS A 99 7330 6787 9875 -737 558 -943 C
ATOM 605 SG CYS A 99 35.625 3.801 224.236 1.00 62.46 S
ANISOU 605 SG CYS A 99 7310 6604 9816 -809 667 -886 S
ATOM 606 N LEU A 100 35.954 6.032 228.477 1.00 60.08 N
ANISOU 606 N LEU A 100 6873 6436 9520 -1026 644 -1354 N
ATOM 607 CA LEU A 100 35.686 6.213 229.903 1.00 58.34 C
ANISOU 607 CA LEU A 100 6586 6318 9264 -996 532 -1423 C
ATOM 608 C LEU A 100 35.081 7.576 230.219 1.00 66.58 C
ANISOU 608 C LEU A 100 7938 7131 10229 -997 706 -1426 C
ATOM 609 O LEU A 100 34.083 7.631 230.959 1.00 64.47 O
ANISOU 609 O LEU A 100 7722 6878 9897 -824 623 -1332 O
ATOM 610 CB LEU A 100 36.970 5.976 230.703 1.00 61.79 C
ANISOU 610 CB LEU A 100 6755 6948 9775 -1193 452 -1677 C
ATOM 611 CG LEU A 100 36.856 6.069 232.229 1.00 67.45 C
ANISOU 611 CG LEU A 100 7412 7783 10435 -1174 307 -1773 C
ATOM 612 CD1 LEU A 100 37.922 5.213 232.899 1.00 66.38 C
ANISOU 612 CD1 LEU A 100 6955 7919 10346 -1227 92 -1953 C
ATOM 613 CD2 LEU A 100 36.970 7.516 232.694 1.00 66.38 C
ANISOU 613 CD2 LEU A 100 7488 7466 10267 -1350 507 -1917 C
ATOM 614 N PRO A 101 35.631 8.700 229.745 1.00 69.25 N
ANISOU 614 N PRO A 101 8505 7243 10564 -1190 968 -1541 N
ATOM 615 CA PRO A 101 34.972 9.992 230.023 1.00 61.16 C
ANISOU 615 CA PRO A 101 7832 5969 9437 -1154 1147 -1522 C
ATOM 616 C PRO A 101 33.546 10.063 229.499 1.00 68.39 C
ANISOU 616 C PRO A 101 8956 6764 10264 -822 1114 -1266 C
ATOM 617 O PRO A 101 32.663 10.635 230.160 1.00 65.35 O
ANISOU 617 O PRO A 101 8711 6308 9812 -673 1123 -1214 O
ATOM 618 CB PRO A 101 35.887 11.008 229.328 1.00 61.83 C
ANISOU 618 CB PRO A 101 8163 5809 9521 -1430 1464 -1683 C
ATOM 619 CG PRO A 101 37.222 10.316 229.230 1.00 71.81 C
ANISOU 619 CG PRO A 101 9083 7277 10924 -1681 1425 -1884 C
ATOM 620 CD PRO A 101 36.898 8.867 229.013 1.00 73.23 C
ANISOU 620 CD PRO A 101 8974 7699 11151 -1465 1141 -1718 C
ATOM 621 N ALA A 102 33.279 9.449 228.339 1.00 72.09 N
ANISOU 621 N ALA A 102 9428 7227 10736 -692 1063 -1116 N
ATOM 622 CA ALA A 102 31.922 9.459 227.801 1.00 67.85 C
ANISOU 622 CA ALA A 102 9044 6616 10119 -362 992 -899 C
ATOM 623 C ALA A 102 30.991 8.616 228.659 1.00 67.21 C
ANISOU 623 C ALA A 102 8690 6781 10064 -174 756 -822 C
ATOM 624 O ALA A 102 29.851 9.016 228.928 1.00 69.73 O
ANISOU 624 O ALA A 102 9108 7054 10334 55 737 -738 O
ATOM 625 CB ALA A 102 31.929 8.962 226.359 1.00 63.89 C
ANISOU 625 CB ALA A 102 8614 6060 9601 -292 979 -779 C
ATOM 626 N SER A 103 31.462 7.447 229.104 1.00 67.63 N
ANISOU 626 N SER A 103 8416 7089 10192 -264 593 -862 N
ATOM 627 CA SER A 103 30.645 6.612 229.975 1.00 63.74 C
ANISOU 627 CA SER A 103 7713 6801 9704 -123 411 -809 C
ATOM 628 C SER A 103 30.349 7.319 231.291 1.00 65.44 C
ANISOU 628 C SER A 103 7993 6983 9888 -133 459 -896 C
ATOM 629 O SER A 103 29.232 7.232 231.817 1.00 63.64 O
ANISOU 629 O SER A 103 7749 6794 9639 45 413 -830 O
ATOM 630 CB SER A 103 31.358 5.282 230.221 1.00 53.43 C
ANISOU 630 CB SER A 103 6122 5731 8448 -221 253 -848 C
ATOM 631 OG SER A 103 30.699 4.520 231.218 1.00 63.42 O
ANISOU 631 OG SER A 103 7248 7160 9691 -125 117 -826 O
ATOM 632 N LEU A 104 31.319 8.074 231.807 1.00 67.36 N
ANISOU 632 N LEU A 104 8318 7146 10130 -352 572 -1060 N
ATOM 633 CA LEU A 104 31.089 8.828 233.033 1.00 64.05 C
ANISOU 633 CA LEU A 104 8003 6668 9664 -383 634 -1149 C
ATOM 634 C LEU A 104 30.021 9.894 232.821 1.00 67.07 C
ANISOU 634 C LEU A 104 8669 6827 9987 -195 785 -1057 C
ATOM 635 O LEU A 104 29.071 10.018 233.611 1.00 63.63 O
ANISOU 635 O LEU A 104 8250 6402 9527 -47 772 -1024 O
ATOM 636 CB LEU A 104 32.401 9.461 233.503 1.00 61.54 C
ANISOU 636 CB LEU A 104 7717 6312 9353 -682 730 -1369 C
ATOM 637 CG LEU A 104 32.310 10.535 234.591 1.00 67.98 C
ANISOU 637 CG LEU A 104 8728 7001 10102 -766 855 -1483 C
ATOM 638 CD1 LEU A 104 31.799 9.950 235.904 1.00 63.36 C
ANISOU 638 CD1 LEU A 104 8024 6568 9481 -682 693 -1485 C
ATOM 639 CD2 LEU A 104 33.652 11.218 234.793 1.00 62.07 C
ANISOU 639 CD2 LEU A 104 8010 6208 9366 -1096 975 -1725 C
ATOM 640 N LEU A 105 30.150 10.668 231.742 1.00 58.41 N
ANISOU 640 N LEU A 105 7820 5514 8858 -181 940 -1020 N
ATOM 641 CA LEU A 105 29.180 11.732 231.513 1.00 63.09 C
ANISOU 641 CA LEU A 105 8727 5875 9369 41 1077 -935 C
ATOM 642 C LEU A 105 27.780 11.175 231.269 1.00 74.10 C
ANISOU 642 C LEU A 105 9998 7380 10777 383 921 -777 C
ATOM 643 O LEU A 105 26.790 11.791 231.686 1.00 82.47 O
ANISOU 643 O LEU A 105 11172 8360 11803 594 970 -744 O
ATOM 644 CB LEU A 105 29.632 12.603 230.340 1.00 74.77 C
ANISOU 644 CB LEU A 105 10557 7076 10776 2 1274 -924 C
ATOM 645 CG LEU A 105 29.190 14.062 230.381 1.00 91.13 C
ANISOU 645 CG LEU A 105 13075 8827 12724 110 1507 -921 C
ATOM 646 CD1 LEU A 105 29.823 14.762 231.568 1.00 96.09 C
ANISOU 646 CD1 LEU A 105 13775 9394 13340 -159 1661 -1103 C
ATOM 647 CD2 LEU A 105 29.557 14.753 229.081 1.00 96.40 C
ANISOU 647 CD2 LEU A 105 14139 9201 13288 107 1695 -887 C
ATOM 648 N VAL A 106 27.674 10.010 230.622 1.00 69.74 N
ANISOU 648 N VAL A 106 9201 7019 10278 435 743 -697 N
ATOM 649 CA VAL A 106 26.358 9.425 230.382 1.00 67.79 C
ANISOU 649 CA VAL A 106 8799 6907 10053 722 597 -585 C
ATOM 650 C VAL A 106 25.764 8.882 231.678 1.00 65.00 C
ANISOU 650 C VAL A 106 8217 6732 9747 728 535 -635 C
ATOM 651 O VAL A 106 24.568 9.048 231.943 1.00 64.09 O
ANISOU 651 O VAL A 106 8065 6642 9645 953 529 -609 O
ATOM 652 CB VAL A 106 26.438 8.335 229.296 1.00 66.69 C
ANISOU 652 CB VAL A 106 8492 6906 9940 744 445 -497 C
ATOM 653 CG1 VAL A 106 25.142 7.539 229.251 1.00 61.21 C
ANISOU 653 CG1 VAL A 106 7561 6413 9285 970 286 -430 C
ATOM 654 CG2 VAL A 106 26.724 8.958 227.937 1.00 66.08 C
ANISOU 654 CG2 VAL A 106 8706 6612 9789 804 519 -429 C
ATOM 655 N ASP A 107 26.583 8.233 232.511 1.00 62.10 N
ANISOU 655 N ASP A 107 7708 6488 9402 493 493 -722 N
ATOM 656 CA ASP A 107 26.090 7.770 233.802 1.00 62.21 C
ANISOU 656 CA ASP A 107 7591 6623 9423 485 461 -777 C
ATOM 657 C ASP A 107 25.707 8.932 234.706 1.00 68.60 C
ANISOU 657 C ASP A 107 8603 7268 10196 519 619 -840 C
ATOM 658 O ASP A 107 24.972 8.729 235.680 1.00 70.37 O
ANISOU 658 O ASP A 107 8765 7548 10424 571 634 -872 O
ATOM 659 CB ASP A 107 27.130 6.878 234.490 1.00 65.01 C
ANISOU 659 CB ASP A 107 7813 7118 9769 260 364 -859 C
ATOM 660 CG ASP A 107 27.265 5.510 233.826 1.00 76.79 C
ANISOU 660 CG ASP A 107 9093 8794 11291 263 211 -791 C
ATOM 661 OD1 ASP A 107 26.274 5.027 233.232 1.00 68.97 O
ANISOU 661 OD1 ASP A 107 8008 7871 10326 425 171 -698 O
ATOM 662 OD2 ASP A 107 28.361 4.913 233.903 1.00 79.62 O
ANISOU 662 OD2 ASP A 107 9373 9236 11645 108 131 -843 O
ATOM 663 N ILE A 108 26.218 10.134 234.428 1.00 69.26 N
ANISOU 663 N ILE A 108 8953 7131 10233 469 764 -869 N
ATOM 664 CA ILE A 108 25.787 11.307 235.187 1.00 68.77 C
ANISOU 664 CA ILE A 108 9128 6880 10121 522 938 -917 C
ATOM 665 C ILE A 108 24.475 11.868 234.643 1.00 73.23 C
ANISOU 665 C ILE A 108 9782 7353 10688 868 988 -820 C
ATOM 666 O ILE A 108 23.516 12.076 235.396 1.00 71.33 O
ANISOU 666 O ILE A 108 9520 7117 10465 1014 1041 -837 O
ATOM 667 CB ILE A 108 26.887 12.386 235.200 1.00 66.20 C
ANISOU 667 CB ILE A 108 9086 6341 9727 300 1105 -1013 C
ATOM 668 CG1 ILE A 108 28.077 11.937 236.050 1.00 70.74 C
ANISOU 668 CG1 ILE A 108 9535 7037 10304 -20 1042 -1161 C
ATOM 669 CG2 ILE A 108 26.328 13.696 235.723 1.00 66.71 C
ANISOU 669 CG2 ILE A 108 9464 6164 9720 398 1315 -1035 C
ATOM 670 CD1 ILE A 108 29.207 12.943 236.086 1.00 74.11 C
ANISOU 670 CD1 ILE A 108 10184 7293 10682 -287 1209 -1306 C
ATOM 671 N THR A 109 24.408 12.151 233.339 1.00 70.11 N
ANISOU 671 N THR A 109 9502 6869 10269 1017 973 -729 N
ATOM 672 CA THR A 109 23.250 12.851 232.794 1.00 70.89 C
ANISOU 672 CA THR A 109 9737 6856 10340 1386 1004 -652 C
ATOM 673 C THR A 109 22.217 11.941 232.141 1.00 72.58 C
ANISOU 673 C THR A 109 9649 7297 10629 1637 802 -580 C
ATOM 674 O THR A 109 21.094 12.394 231.891 1.00 74.04 O
ANISOU 674 O THR A 109 9852 7462 10817 1974 788 -551 O
ATOM 675 CB THR A 109 23.690 13.908 231.772 1.00 78.80 C
ANISOU 675 CB THR A 109 11153 7567 11221 1453 1127 -602 C
ATOM 676 OG1 THR A 109 24.211 13.266 230.601 1.00 82.44 O
ANISOU 676 OG1 THR A 109 11562 8082 11679 1400 1012 -537 O
ATOM 677 CG2 THR A 109 24.751 14.815 232.369 1.00 79.98 C
ANISOU 677 CG2 THR A 109 11601 7492 11296 1156 1357 -705 C
ATOM 678 N GLU A 110 22.552 10.683 231.860 1.00 67.40 N
ANISOU 678 N GLU A 110 8715 6861 10031 1490 646 -565 N
ATOM 679 CA GLU A 110 21.658 9.801 231.106 1.00 59.40 C
ANISOU 679 CA GLU A 110 7435 6058 9076 1687 462 -510 C
ATOM 680 C GLU A 110 21.244 10.445 229.781 1.00 65.35 C
ANISOU 680 C GLU A 110 8390 6683 9757 1985 408 -419 C
ATOM 681 O GLU A 110 20.107 10.300 229.326 1.00 66.79 O
ANISOU 681 O GLU A 110 8420 6986 9970 2284 282 -404 O
ATOM 682 CB GLU A 110 20.425 9.422 231.932 1.00 57.96 C
ANISOU 682 CB GLU A 110 6980 6055 8988 1819 448 -579 C
ATOM 683 CG GLU A 110 20.740 8.801 233.280 1.00 65.29 C
ANISOU 683 CG GLU A 110 7783 7073 9952 1551 515 -667 C
ATOM 684 CD GLU A 110 21.577 7.547 233.166 1.00 74.48 C
ANISOU 684 CD GLU A 110 8796 8387 11117 1298 405 -654 C
ATOM 685 OE1 GLU A 110 21.682 6.994 232.052 1.00 80.92 O
ANISOU 685 OE1 GLU A 110 9531 9280 11934 1335 278 -581 O
ATOM 686 OE2 GLU A 110 22.134 7.110 234.194 1.00 78.24 O
ANISOU 686 OE2 GLU A 110 9257 8895 11577 1078 442 -716 O
ATOM 687 N SER A 111 22.177 11.165 229.161 1.00 64.68 N
ANISOU 687 N SER A 111 8660 6349 9565 1903 507 -377 N
ATOM 688 CA SER A 111 21.964 11.787 227.860 1.00 65.90 C
ANISOU 688 CA SER A 111 9112 6324 9602 2163 477 -284 C
ATOM 689 C SER A 111 23.303 11.868 227.141 1.00 67.96 C
ANISOU 689 C SER A 111 9630 6405 9785 1899 573 -258 C
ATOM 690 O SER A 111 24.362 11.631 227.729 1.00 65.70 O
ANISOU 690 O SER A 111 9285 6132 9546 1542 671 -332 O
ATOM 691 CB SER A 111 21.336 13.173 227.991 1.00 75.40 C
ANISOU 691 CB SER A 111 10657 7281 10709 2464 603 -280 C
ATOM 692 OG SER A 111 22.278 14.098 228.497 1.00 80.06 O
ANISOU 692 OG SER A 111 11595 7600 11223 2232 859 -325 O
ATOM 693 N TRP A 112 23.251 12.185 225.851 1.00 66.57 N
ANISOU 693 N TRP A 112 9739 6067 9487 2082 541 -168 N
ATOM 694 CA TRP A 112 24.440 12.214 225.008 1.00 69.91 C
ANISOU 694 CA TRP A 112 10419 6308 9836 1840 652 -149 C
ATOM 695 C TRP A 112 24.755 13.656 224.634 1.00 76.01 C
ANISOU 695 C TRP A 112 11782 6668 10431 1905 899 -144 C
ATOM 696 O TRP A 112 23.908 14.353 224.065 1.00 80.72 O
ANISOU 696 O TRP A 112 12675 7104 10890 2293 862 -66 O
ATOM 697 CB TRP A 112 24.248 11.354 223.760 1.00 62.75 C
ANISOU 697 CB TRP A 112 9438 5503 8903 1948 455 -52 C
ATOM 698 CG TRP A 112 25.499 11.199 222.969 1.00 65.50 C
ANISOU 698 CG TRP A 112 9987 5695 9205 1661 584 -48 C
ATOM 699 CD1 TRP A 112 25.831 11.862 221.823 1.00 64.50 C
ANISOU 699 CD1 TRP A 112 10353 5250 8906 1725 703 10 C
ATOM 700 CD2 TRP A 112 26.606 10.340 223.273 1.00 62.72 C
ANISOU 700 CD2 TRP A 112 9367 5486 8979 1268 625 -119 C
ATOM 701 NE1 TRP A 112 27.072 11.459 221.387 1.00 67.81 N
ANISOU 701 NE1 TRP A 112 10802 5608 9353 1368 839 -31 N
ATOM 702 CE2 TRP A 112 27.568 10.526 222.260 1.00 63.70 C
ANISOU 702 CE2 TRP A 112 9798 5382 9023 1097 781 -114 C
ATOM 703 CE3 TRP A 112 26.872 9.425 224.299 1.00 61.44 C
ANISOU 703 CE3 TRP A 112 8757 5613 8974 1062 546 -194 C
ATOM 704 CZ2 TRP A 112 28.776 9.834 222.241 1.00 62.07 C
ANISOU 704 CZ2 TRP A 112 9409 5255 8919 736 856 -192 C
ATOM 705 CZ3 TRP A 112 28.075 8.738 224.282 1.00 62.24 C
ANISOU 705 CZ3 TRP A 112 8708 5787 9153 734 594 -259 C
ATOM 706 CH2 TRP A 112 29.012 8.947 223.258 1.00 67.93 C
ANISOU 706 CH2 TRP A 112 9688 6303 9821 576 745 -264 C
ATOM 707 N LEU A 113 25.971 14.098 224.955 1.00 77.03 N
ANISOU 707 N LEU A 113 12089 6626 10553 1532 1152 -242 N
ATOM 708 CA LEU A 113 26.393 15.474 224.721 1.00 80.02 C
ANISOU 708 CA LEU A 113 13054 6591 10760 1506 1453 -272 C
ATOM 709 C LEU A 113 27.558 15.581 223.741 1.00 82.81 C
ANISOU 709 C LEU A 113 13714 6717 11035 1227 1649 -302 C
ATOM 710 O LEU A 113 28.161 16.654 223.633 1.00 91.10 O
ANISOU 710 O LEU A 113 15241 7417 11954 1079 1965 -373 O
ATOM 711 CB LEU A 113 26.760 16.137 226.053 1.00 81.84 C
ANISOU 711 CB LEU A 113 13285 6776 11035 1282 1648 -409 C
ATOM 712 CG LEU A 113 25.672 16.094 227.133 1.00 79.78 C
ANISOU 712 CG LEU A 113 12754 6706 10852 1516 1512 -401 C
ATOM 713 CD1 LEU A 113 26.250 16.413 228.502 1.00 77.66 C
ANISOU 713 CD1 LEU A 113 12401 6455 10650 1200 1669 -550 C
ATOM 714 CD2 LEU A 113 24.537 17.049 226.802 1.00 74.35 C
ANISOU 714 CD2 LEU A 113 12425 5808 10017 1988 1528 -307 C
ATOM 715 N PHE A 114 27.907 14.501 223.039 1.00 77.02 N
ANISOU 715 N PHE A 114 12731 6157 10375 1128 1503 -264 N
ATOM 716 CA PHE A 114 29.068 14.495 222.156 1.00 82.32 C
ANISOU 716 CA PHE A 114 13639 6635 11003 827 1708 -315 C
ATOM 717 C PHE A 114 28.722 14.502 220.672 1.00 84.99 C
ANISOU 717 C PHE A 114 14360 6769 11162 1075 1666 -170 C
ATOM 718 O PHE A 114 29.636 14.477 219.842 1.00 91.49 O
ANISOU 718 O PHE A 114 15356 7480 11927 820 1828 -201 O
ATOM 719 CB PHE A 114 29.960 13.286 222.454 1.00 90.16 C
ANISOU 719 CB PHE A 114 14105 7943 12208 481 1623 -405 C
ATOM 720 CG PHE A 114 30.362 13.168 223.894 1.00 95.56 C
ANISOU 720 CG PHE A 114 14416 8844 13048 249 1624 -553 C
ATOM 721 CD1 PHE A 114 29.687 12.308 224.743 1.00 98.69 C
ANISOU 721 CD1 PHE A 114 14349 9586 13564 375 1349 -516 C
ATOM 722 CD2 PHE A 114 31.414 13.912 224.400 1.00 96.99 C
ANISOU 722 CD2 PHE A 114 14731 8877 13244 -105 1905 -746 C
ATOM 723 CE1 PHE A 114 30.053 12.191 226.068 1.00 96.13 C
ANISOU 723 CE1 PHE A 114 13739 9437 13349 179 1342 -648 C
ATOM 724 CE2 PHE A 114 31.785 13.798 225.727 1.00 93.30 C
ANISOU 724 CE2 PHE A 114 13934 8616 12899 -304 1873 -892 C
ATOM 725 CZ PHE A 114 31.104 12.937 226.560 1.00 91.72 C
ANISOU 725 CZ PHE A 114 13312 8741 12796 -148 1585 -832 C
ATOM 726 N GLY A 115 27.443 14.521 220.310 1.00 83.02 N
ANISOU 726 N GLY A 115 14174 6557 10814 1546 1420 -24 N
ATOM 727 CA GLY A 115 27.048 14.644 218.923 1.00 80.70 C
ANISOU 727 CA GLY A 115 14162 6205 10296 1766 1309 106 C
ATOM 728 C GLY A 115 26.868 13.321 218.193 1.00 86.77 C
ANISOU 728 C GLY A 115 14684 7140 11145 1841 1060 187 C
ATOM 729 O GLY A 115 27.263 12.239 218.648 1.00 84.59 O
ANISOU 729 O GLY A 115 13921 7136 11084 1607 978 140 O
ATOM 730 N HIS A 116 26.264 13.438 217.005 1.00 92.17 N
ANISOU 730 N HIS A 116 15595 7811 11615 2102 901 300 N
ATOM 731 CA HIS A 116 25.834 12.270 216.242 1.00 89.18 C
ANISOU 731 CA HIS A 116 15002 7616 11267 2239 615 387 C
ATOM 732 C HIS A 116 27.002 11.396 215.797 1.00 89.36 C
ANISOU 732 C HIS A 116 14972 7597 11385 1857 750 363 C
ATOM 733 O HIS A 116 26.850 10.171 215.716 1.00 91.36 O
ANISOU 733 O HIS A 116 14830 8113 11770 1832 541 394 O
ATOM 734 CB HIS A 116 25.023 12.718 215.018 1.00 89.40 C
ANISOU 734 CB HIS A 116 15340 7616 11011 2564 445 484 C
ATOM 735 CG HIS A 116 23.810 13.535 215.352 1.00102.56 C
ANISOU 735 CG HIS A 116 17033 9354 12583 2964 291 497 C
ATOM 736 ND1 HIS A 116 23.886 14.770 215.961 1.00107.66 N
ANISOU 736 ND1 HIS A 116 17940 9822 13144 2971 511 454 N
ATOM 737 CD2 HIS A 116 22.491 13.296 215.153 1.00104.89 C
ANISOU 737 CD2 HIS A 116 17103 9894 12856 3355 -53 531 C
ATOM 738 CE1 HIS A 116 22.668 15.253 216.128 1.00107.58 C
ANISOU 738 CE1 HIS A 116 17882 9928 13066 3367 311 474 C
ATOM 739 NE2 HIS A 116 21.803 14.379 215.647 1.00106.18 N
ANISOU 739 NE2 HIS A 116 17389 10019 12934 3600 -33 509 N
ATOM 740 N ALA A 117 28.166 11.987 215.502 1.00 87.01 N
ANISOU 740 N ALA A 117 14955 7086 11017 1504 1087 285 N
ATOM 741 CA ALA A 117 29.284 11.197 214.985 1.00 77.02 C
ANISOU 741 CA ALA A 117 13609 5813 9841 1139 1225 241 C
ATOM 742 C ALA A 117 29.982 10.425 216.096 1.00 75.96 C
ANISOU 742 C ALA A 117 12991 5855 10016 834 1279 121 C
ATOM 743 O ALA A 117 30.251 9.223 215.964 1.00 80.63 O
ANISOU 743 O ALA A 117 13190 6704 10740 703 1145 132 O
ATOM 744 CB ALA A 117 30.278 12.106 214.262 1.00 79.36 C
ANISOU 744 CB ALA A 117 14303 5899 9951 870 1565 171 C
ATOM 745 N LEU A 118 30.272 11.098 217.209 1.00 75.12 N
ANISOU 745 N LEU A 118 12799 5747 9995 695 1427 -3 N
ATOM 746 CA LEU A 118 30.841 10.393 218.347 1.00 73.64 C
ANISOU 746 CA LEU A 118 12027 5894 10058 420 1386 -128 C
ATOM 747 C LEU A 118 29.875 9.362 218.910 1.00 71.60 C
ANISOU 747 C LEU A 118 11260 6038 9905 633 1019 -44 C
ATOM 748 O LEU A 118 30.332 8.365 219.480 1.00 69.20 O
ANISOU 748 O LEU A 118 10497 6022 9776 438 932 -102 O
ATOM 749 CB LEU A 118 31.282 11.391 219.419 1.00 70.05 C
ANISOU 749 CB LEU A 118 11630 5343 9643 243 1607 -284 C
ATOM 750 CG LEU A 118 32.463 12.268 218.979 1.00 71.68 C
ANISOU 750 CG LEU A 118 12257 5192 9788 -91 2023 -431 C
ATOM 751 CD1 LEU A 118 32.921 13.167 220.114 1.00 71.10 C
ANISOU 751 CD1 LEU A 118 12170 5083 9760 -306 2221 -610 C
ATOM 752 CD2 LEU A 118 33.622 11.420 218.468 1.00 62.04 C
ANISOU 752 CD2 LEU A 118 10814 4060 8700 -429 2117 -527 C
ATOM 753 N CYS A 119 28.564 9.547 218.706 1.00 76.85 N
ANISOU 753 N CYS A 119 12012 6725 10462 1030 808 78 N
ATOM 754 CA CYS A 119 27.612 8.521 219.121 1.00 70.68 C
ANISOU 754 CA CYS A 119 10753 6321 9782 1203 490 132 C
ATOM 755 C CYS A 119 27.894 7.185 218.441 1.00 72.68 C
ANISOU 755 C CYS A 119 10772 6755 10088 1086 363 181 C
ATOM 756 O CYS A 119 27.693 6.125 219.049 1.00 72.27 O
ANISOU 756 O CYS A 119 10263 7024 10170 1027 204 166 O
ATOM 757 CB CYS A 119 26.184 8.980 218.816 1.00 67.92 C
ANISOU 757 CB CYS A 119 10541 5961 9306 1656 293 224 C
ATOM 758 SG CYS A 119 24.897 7.716 219.018 1.00 77.45 S
ANISOU 758 SG CYS A 119 11194 7616 10618 1867 -81 262 S
ATOM 759 N LYS A 120 28.374 7.205 217.195 1.00 77.76 N
ANISOU 759 N LYS A 120 11757 7174 10612 1043 455 236 N
ATOM 760 CA LYS A 120 28.784 5.956 216.562 1.00 80.25 C
ANISOU 760 CA LYS A 120 11878 7633 10980 895 380 273 C
ATOM 761 C LYS A 120 30.212 5.580 216.935 1.00 72.84 C
ANISOU 761 C LYS A 120 10768 6714 10194 497 593 153 C
ATOM 762 O LYS A 120 30.498 4.408 217.206 1.00 67.63 O
ANISOU 762 O LYS A 120 9722 6315 9661 369 493 140 O
ATOM 763 CB LYS A 120 28.651 6.059 215.041 1.00 76.08 C
ANISOU 763 CB LYS A 120 11795 6861 10252 1026 378 383 C
ATOM 764 CG LYS A 120 27.223 6.010 214.533 1.00 76.61 C
ANISOU 764 CG LYS A 120 11915 7012 10182 1435 71 493 C
ATOM 765 CD LYS A 120 27.183 6.032 213.015 1.00 79.04 C
ANISOU 765 CD LYS A 120 12685 7078 10269 1555 49 596 C
ATOM 766 CE LYS A 120 25.755 5.965 212.487 1.00 85.96 C
ANISOU 766 CE LYS A 120 13584 8074 11004 1986 -302 680 C
ATOM 767 NZ LYS A 120 25.092 4.673 212.815 1.00 79.28 N
ANISOU 767 NZ LYS A 120 12159 7663 10301 1980 -570 670 N
ATOM 768 N VAL A 121 31.118 6.558 216.967 1.00 70.22 N
ANISOU 768 N VAL A 121 10718 6114 9849 302 890 46 N
ATOM 769 CA VAL A 121 32.534 6.231 217.116 1.00 63.14 C
ANISOU 769 CA VAL A 121 9663 5231 9098 -75 1100 -101 C
ATOM 770 C VAL A 121 32.819 5.639 218.494 1.00 58.05 C
ANISOU 770 C VAL A 121 8489 4921 8645 -194 990 -208 C
ATOM 771 O VAL A 121 33.419 4.562 218.610 1.00 62.38 O
ANISOU 771 O VAL A 121 8703 5681 9317 -334 929 -245 O
ATOM 772 CB VAL A 121 33.406 7.469 216.845 1.00 72.01 C
ANISOU 772 CB VAL A 121 11208 5990 10163 -287 1473 -230 C
ATOM 773 CG1 VAL A 121 34.863 7.141 217.101 1.00 68.05 C
ANISOU 773 CG1 VAL A 121 10454 5555 9848 -685 1681 -433 C
ATOM 774 CG2 VAL A 121 33.211 7.949 215.422 1.00 74.20 C
ANISOU 774 CG2 VAL A 121 12072 5900 10219 -176 1601 -121 C
ATOM 775 N ILE A 122 32.420 6.340 219.561 1.00 59.70 N
ANISOU 775 N ILE A 122 8650 5165 8867 -130 970 -262 N
ATOM 776 CA ILE A 122 32.800 5.913 220.910 1.00 63.52 C
ANISOU 776 CA ILE A 122 8709 5921 9504 -260 892 -384 C
ATOM 777 C ILE A 122 32.269 4.528 221.262 1.00 65.07 C
ANISOU 777 C ILE A 122 8520 6445 9761 -148 615 -300 C
ATOM 778 O ILE A 122 33.053 3.694 221.742 1.00 56.78 O
ANISOU 778 O ILE A 122 7164 5586 8823 -308 577 -385 O
ATOM 779 CB ILE A 122 32.394 6.981 221.937 1.00 61.87 C
ANISOU 779 CB ILE A 122 8585 5651 9270 -206 939 -448 C
ATOM 780 CG1 ILE A 122 33.246 8.238 221.722 1.00 55.30 C
ANISOU 780 CG1 ILE A 122 8109 4507 8397 -421 1267 -586 C
ATOM 781 CG2 ILE A 122 32.555 6.448 223.347 1.00 61.84 C
ANISOU 781 CG2 ILE A 122 8175 5934 9388 -282 806 -545 C
ATOM 782 CD1 ILE A 122 32.843 9.413 222.587 1.00 65.20 C
ANISOU 782 CD1 ILE A 122 9543 5637 9592 -369 1357 -641 C
ATOM 783 N PRO A 123 30.983 4.226 221.096 1.00 59.33 N
ANISOU 783 N PRO A 123 7784 5798 8962 120 424 -157 N
ATOM 784 CA PRO A 123 30.539 2.846 221.341 1.00 52.40 C
ANISOU 784 CA PRO A 123 6570 5208 8130 174 211 -98 C
ATOM 785 C PRO A 123 31.254 1.845 220.449 1.00 63.88 C
ANISOU 785 C PRO A 123 7975 6693 9604 50 220 -65 C
ATOM 786 O PRO A 123 31.550 0.719 220.882 1.00 59.94 O
ANISOU 786 O PRO A 123 7194 6409 9174 -21 130 -81 O
ATOM 787 CB PRO A 123 29.033 2.905 221.038 1.00 51.04 C
ANISOU 787 CB PRO A 123 6451 5073 7871 467 48 18 C
ATOM 788 CG PRO A 123 28.660 4.344 221.252 1.00 48.37 C
ANISOU 788 CG PRO A 123 6378 4528 7470 592 145 -4 C
ATOM 789 CD PRO A 123 29.857 5.135 220.811 1.00 56.85 C
ANISOU 789 CD PRO A 123 7742 5335 8525 389 393 -72 C
ATOM 790 N TYR A 124 31.582 2.248 219.218 1.00 58.97 N
ANISOU 790 N TYR A 124 7662 5835 8910 22 349 -22 N
ATOM 791 CA TYR A 124 32.356 1.382 218.341 1.00 58.36 C
ANISOU 791 CA TYR A 124 7569 5751 8854 -118 403 -3 C
ATOM 792 C TYR A 124 33.721 1.089 218.942 1.00 55.90 C
ANISOU 792 C TYR A 124 7025 5522 8693 -370 524 -165 C
ATOM 793 O TYR A 124 34.155 -0.066 218.991 1.00 60.11 O
ANISOU 793 O TYR A 124 7316 6232 9291 -427 453 -166 O
ATOM 794 CB TYR A 124 32.501 2.034 216.963 1.00 59.64 C
ANISOU 794 CB TYR A 124 8174 5594 8894 -117 563 54 C
ATOM 795 CG TYR A 124 33.503 1.346 216.056 1.00 58.07 C
ANISOU 795 CG TYR A 124 8008 5326 8728 -311 701 41 C
ATOM 796 CD1 TYR A 124 33.227 0.103 215.505 1.00 60.14 C
ANISOU 796 CD1 TYR A 124 8153 5729 8969 -263 557 150 C
ATOM 797 CD2 TYR A 124 34.724 1.943 215.751 1.00 61.47 C
ANISOU 797 CD2 TYR A 124 8593 5549 9216 -559 1000 -98 C
ATOM 798 CE1 TYR A 124 34.135 -0.532 214.679 1.00 57.63 C
ANISOU 798 CE1 TYR A 124 7878 5338 8681 -432 699 139 C
ATOM 799 CE2 TYR A 124 35.638 1.315 214.918 1.00 58.80 C
ANISOU 799 CE2 TYR A 124 8273 5146 8924 -738 1151 -127 C
ATOM 800 CZ TYR A 124 35.337 0.080 214.390 1.00 60.25 C
ANISOU 800 CZ TYR A 124 8346 5464 9081 -661 995 1 C
ATOM 801 OH TYR A 124 36.233 -0.552 213.566 1.00 63.45 O
ANISOU 801 OH TYR A 124 8781 5796 9531 -830 1159 -26 O
ATOM 802 N LEU A 125 34.417 2.131 219.404 1.00 55.73 N
ANISOU 802 N LEU A 125 7076 5376 8721 -515 704 -317 N
ATOM 803 CA LEU A 125 35.739 1.920 219.977 1.00 55.96 C
ANISOU 803 CA LEU A 125 6849 5510 8903 -752 800 -513 C
ATOM 804 C LEU A 125 35.670 1.119 221.267 1.00 61.65 C
ANISOU 804 C LEU A 125 7190 6542 9691 -694 580 -552 C
ATOM 805 O LEU A 125 36.578 0.335 221.555 1.00 64.67 O
ANISOU 805 O LEU A 125 7308 7089 10174 -791 550 -653 O
ATOM 806 CB LEU A 125 36.434 3.260 220.210 1.00 55.24 C
ANISOU 806 CB LEU A 125 6923 5224 8842 -944 1049 -696 C
ATOM 807 CG LEU A 125 36.923 3.934 218.925 1.00 59.23 C
ANISOU 807 CG LEU A 125 7815 5397 9291 -1085 1346 -717 C
ATOM 808 CD1 LEU A 125 37.694 5.209 219.223 1.00 63.58 C
ANISOU 808 CD1 LEU A 125 8527 5757 9876 -1329 1635 -935 C
ATOM 809 CD2 LEU A 125 37.765 2.954 218.108 1.00 67.94 C
ANISOU 809 CD2 LEU A 125 8792 6544 10478 -1214 1412 -740 C
ATOM 810 N GLN A 126 34.594 1.271 222.038 1.00 62.71 N
ANISOU 810 N GLN A 126 7310 6753 9763 -521 428 -478 N
ATOM 811 CA GLN A 126 34.456 0.473 223.251 1.00 64.68 C
ANISOU 811 CA GLN A 126 7269 7263 10045 -464 239 -506 C
ATOM 812 C GLN A 126 34.298 -1.003 222.914 1.00 59.09 C
ANISOU 812 C GLN A 126 6417 6714 9320 -391 104 -399 C
ATOM 813 O GLN A 126 34.961 -1.867 223.508 1.00 60.43 O
ANISOU 813 O GLN A 126 6368 7055 9537 -424 25 -469 O
ATOM 814 CB GLN A 126 33.260 0.968 224.067 1.00 63.14 C
ANISOU 814 CB GLN A 126 7122 7086 9784 -307 150 -454 C
ATOM 815 CG GLN A 126 32.986 0.149 225.305 1.00 62.07 C
ANISOU 815 CG GLN A 126 6757 7177 9649 -247 -18 -475 C
ATOM 816 CD GLN A 126 34.172 0.145 226.252 1.00 80.78 C
ANISOU 816 CD GLN A 126 8962 9642 12087 -387 -24 -659 C
ATOM 817 OE1 GLN A 126 34.710 1.202 226.597 1.00 77.10 O
ANISOU 817 OE1 GLN A 126 8551 9084 11658 -506 86 -795 O
ATOM 818 NE2 GLN A 126 34.599 -1.047 226.667 1.00 82.69 N
ANISOU 818 NE2 GLN A 126 9015 10070 12334 -366 -154 -676 N
ATOM 819 N ALA A 127 33.431 -1.312 221.946 1.00 54.19 N
ANISOU 819 N ALA A 127 5937 6033 8618 -283 73 -237 N
ATOM 820 CA ALA A 127 33.255 -2.705 221.551 1.00 53.18 C
ANISOU 820 CA ALA A 127 5709 6037 8460 -240 -27 -140 C
ATOM 821 C ALA A 127 34.537 -3.275 220.950 1.00 53.77 C
ANISOU 821 C ALA A 127 5729 6097 8603 -378 70 -194 C
ATOM 822 O ALA A 127 34.898 -4.429 221.223 1.00 55.09 O
ANISOU 822 O ALA A 127 5730 6419 8782 -369 -6 -194 O
ATOM 823 CB ALA A 127 32.088 -2.824 220.568 1.00 47.97 C
ANISOU 823 CB ALA A 127 5211 5317 7697 -114 -82 17 C
ATOM 824 N VAL A 128 35.248 -2.474 220.149 1.00 50.22 N
ANISOU 824 N VAL A 128 5435 5451 8196 -504 258 -253 N
ATOM 825 CA VAL A 128 36.511 -2.929 219.568 1.00 56.21 C
ANISOU 825 CA VAL A 128 6123 6189 9045 -655 390 -339 C
ATOM 826 C VAL A 128 37.528 -3.193 220.666 1.00 56.92 C
ANISOU 826 C VAL A 128 5902 6469 9256 -718 348 -528 C
ATOM 827 O VAL A 128 38.319 -4.141 220.591 1.00 62.29 O
ANISOU 827 O VAL A 128 6405 7265 9999 -736 332 -576 O
ATOM 828 CB VAL A 128 37.044 -1.894 218.558 1.00 56.61 C
ANISOU 828 CB VAL A 128 6437 5961 9112 -808 649 -396 C
ATOM 829 CG1 VAL A 128 38.530 -2.126 218.293 1.00 52.72 C
ANISOU 829 CG1 VAL A 128 5793 5471 8767 -1011 828 -576 C
ATOM 830 CG2 VAL A 128 36.255 -1.958 217.266 1.00 62.13 C
ANISOU 830 CG2 VAL A 128 7461 6477 9670 -725 670 -206 C
ATOM 831 N SER A 129 37.519 -2.361 221.708 1.00 55.60 N
ANISOU 831 N SER A 129 5673 6339 9115 -735 318 -643 N
ATOM 832 CA SER A 129 38.433 -2.571 222.820 1.00 56.12 C
ANISOU 832 CA SER A 129 5451 6600 9273 -774 235 -836 C
ATOM 833 C SER A 129 38.132 -3.883 223.521 1.00 58.27 C
ANISOU 833 C SER A 129 5576 7084 9480 -597 8 -757 C
ATOM 834 O SER A 129 39.045 -4.661 223.823 1.00 59.41 O
ANISOU 834 O SER A 129 5514 7380 9680 -579 -60 -859 O
ATOM 835 CB SER A 129 38.335 -1.400 223.796 1.00 67.07 C
ANISOU 835 CB SER A 129 6851 7964 10666 -827 242 -960 C
ATOM 836 OG SER A 129 38.797 -1.771 225.078 1.00 80.18 O
ANISOU 836 OG SER A 129 8268 9844 12352 -786 70 -1095 O
ATOM 837 N VAL A 130 36.851 -4.171 223.748 1.00 52.68 N
ANISOU 837 N VAL A 130 4986 6383 8647 -459 -98 -585 N
ATOM 838 CA VAL A 130 36.508 -5.426 224.413 1.00 52.49 C
ANISOU 838 CA VAL A 130 4883 6525 8536 -316 -267 -517 C
ATOM 839 C VAL A 130 36.926 -6.614 223.555 1.00 60.78 C
ANISOU 839 C VAL A 130 5915 7600 9578 -297 -250 -443 C
ATOM 840 O VAL A 130 37.447 -7.619 224.063 1.00 62.97 O
ANISOU 840 O VAL A 130 6083 8012 9830 -212 -347 -477 O
ATOM 841 CB VAL A 130 35.004 -5.472 224.734 1.00 58.06 C
ANISOU 841 CB VAL A 130 5712 7224 9125 -213 -333 -377 C
ATOM 842 CG1 VAL A 130 34.665 -6.787 225.430 1.00 45.94 C
ANISOU 842 CG1 VAL A 130 4145 5828 7482 -102 -457 -325 C
ATOM 843 CG2 VAL A 130 34.610 -4.280 225.585 1.00 63.47 C
ANISOU 843 CG2 VAL A 130 6427 7870 9821 -222 -331 -451 C
ATOM 844 N SER A 131 36.712 -6.515 222.239 1.00 65.47 N
ANISOU 844 N SER A 131 6650 8051 10176 -360 -124 -342 N
ATOM 845 CA SER A 131 37.047 -7.629 221.357 1.00 50.84 C
ANISOU 845 CA SER A 131 4815 6199 8304 -354 -86 -262 C
ATOM 846 C SER A 131 38.552 -7.864 221.311 1.00 51.44 C
ANISOU 846 C SER A 131 4708 6327 8510 -412 -23 -425 C
ATOM 847 O SER A 131 39.013 -9.013 221.367 1.00 53.20 O
ANISOU 847 O SER A 131 4851 6651 8713 -326 -76 -415 O
ATOM 848 CB SER A 131 36.497 -7.370 219.953 1.00 47.85 C
ANISOU 848 CB SER A 131 4660 5638 7885 -414 31 -129 C
ATOM 849 OG SER A 131 37.088 -8.255 219.013 1.00 59.51 O
ANISOU 849 OG SER A 131 6166 7079 9368 -452 116 -86 O
ATOM 850 N VAL A 132 39.334 -6.789 221.225 1.00 45.75 N
ANISOU 850 N VAL A 132 3918 5540 7923 -554 101 -593 N
ATOM 851 CA VAL A 132 40.780 -6.947 221.241 1.00 46.73 C
ANISOU 851 CA VAL A 132 3806 5748 8201 -624 166 -802 C
ATOM 852 C VAL A 132 41.237 -7.525 222.572 1.00 53.53 C
ANISOU 852 C VAL A 132 4429 6851 9060 -473 -55 -919 C
ATOM 853 O VAL A 132 42.159 -8.349 222.621 1.00 59.65 O
ANISOU 853 O VAL A 132 5069 7747 9848 -388 -97 -995 O
ATOM 854 CB VAL A 132 41.462 -5.601 220.947 1.00 53.25 C
ANISOU 854 CB VAL A 132 4614 6452 9167 -848 373 -994 C
ATOM 855 CG1 VAL A 132 42.963 -5.709 221.162 1.00 55.13 C
ANISOU 855 CG1 VAL A 132 4600 6827 9518 -901 413 -1244 C
ATOM 856 CG2 VAL A 132 41.154 -5.146 219.531 1.00 49.61 C
ANISOU 856 CG2 VAL A 132 4451 5719 8679 -976 608 -881 C
ATOM 857 N ALA A 133 40.572 -7.149 223.667 1.00 56.76 N
ANISOU 857 N ALA A 133 4864 7318 9385 -402 -203 -911 N
ATOM 858 CA ALA A 133 40.994 -7.639 224.975 1.00 50.52 C
ANISOU 858 CA ALA A 133 3959 6723 8511 -243 -413 -1005 C
ATOM 859 C ALA A 133 40.775 -9.139 225.086 1.00 50.84 C
ANISOU 859 C ALA A 133 4042 6843 8433 -40 -536 -875 C
ATOM 860 O ALA A 133 41.696 -9.897 225.429 1.00 56.92 O
ANISOU 860 O ALA A 133 4724 7738 9164 89 -624 -954 O
ATOM 861 CB ALA A 133 40.233 -6.897 226.077 1.00 47.46 C
ANISOU 861 CB ALA A 133 3621 6346 8066 -231 -516 -1021 C
ATOM 862 N VAL A 134 39.553 -9.589 224.790 1.00 50.43 N
ANISOU 862 N VAL A 134 4195 6702 8262 -7 -523 -661 N
ATOM 863 CA VAL A 134 39.261 -11.007 224.961 1.00 50.83 C
ANISOU 863 CA VAL A 134 4358 6801 8153 162 -604 -537 C
ATOM 864 C VAL A 134 40.002 -11.855 223.928 1.00 53.18 C
ANISOU 864 C VAL A 134 4626 7082 8498 175 -511 -510 C
ATOM 865 O VAL A 134 40.450 -12.963 224.245 1.00 58.64 O
ANISOU 865 O VAL A 134 5321 7854 9106 350 -595 -509 O
ATOM 866 CB VAL A 134 37.740 -11.250 224.936 1.00 50.08 C
ANISOU 866 CB VAL A 134 4495 6627 7905 156 -586 -345 C
ATOM 867 CG1 VAL A 134 37.189 -11.044 223.543 1.00 44.84 C
ANISOU 867 CG1 VAL A 134 3929 5831 7277 24 -434 -217 C
ATOM 868 CG2 VAL A 134 37.403 -12.640 225.479 1.00 60.37 C
ANISOU 868 CG2 VAL A 134 5949 7978 9013 312 -660 -259 C
ATOM 869 N LEU A 135 40.182 -11.363 222.693 1.00 58.79 N
ANISOU 869 N LEU A 135 5337 7672 9329 6 -328 -493 N
ATOM 870 CA LEU A 135 40.975 -12.132 221.735 1.00 54.96 C
ANISOU 870 CA LEU A 135 4821 7161 8900 9 -216 -487 C
ATOM 871 C LEU A 135 42.448 -12.187 222.127 1.00 55.15 C
ANISOU 871 C LEU A 135 4548 7331 9076 76 -258 -727 C
ATOM 872 O LEU A 135 43.106 -13.210 221.901 1.00 61.52 O
ANISOU 872 O LEU A 135 5305 8191 9877 208 -262 -735 O
ATOM 873 CB LEU A 135 40.818 -11.565 220.321 1.00 52.88 C
ANISOU 873 CB LEU A 135 4676 6706 8710 -194 5 -419 C
ATOM 874 CG LEU A 135 39.490 -11.844 219.604 1.00 57.70 C
ANISOU 874 CG LEU A 135 5572 7188 9162 -226 37 -183 C
ATOM 875 CD1 LEU A 135 39.458 -11.174 218.242 1.00 55.72 C
ANISOU 875 CD1 LEU A 135 5467 6738 8967 -399 232 -139 C
ATOM 876 CD2 LEU A 135 39.244 -13.342 219.456 1.00 58.82 C
ANISOU 876 CD2 LEU A 135 5830 7362 9156 -110 6 -48 C
ATOM 877 N THR A 136 42.986 -11.127 222.736 1.00 57.01 N
ANISOU 877 N THR A 136 4635 7632 9393 -3 -288 -917 N
ATOM 878 CA THR A 136 44.370 -11.197 223.191 1.00 57.49 C
ANISOU 878 CA THR A 136 4511 7845 9488 64 -342 -1123 C
ATOM 879 C THR A 136 44.520 -12.207 224.322 1.00 58.40 C
ANISOU 879 C THR A 136 4624 8122 9445 351 -591 -1117 C
ATOM 880 O THR A 136 45.493 -12.975 224.357 1.00 64.46 O
ANISOU 880 O THR A 136 5284 8993 10216 503 -642 -1198 O
ATOM 881 CB THR A 136 44.848 -9.814 223.638 1.00 58.53 C
ANISOU 881 CB THR A 136 4552 7992 9694 -102 -309 -1315 C
ATOM 882 OG1 THR A 136 44.737 -8.887 222.549 1.00 53.89 O
ANISOU 882 OG1 THR A 136 4021 7219 9235 -358 -53 -1327 O
ATOM 883 CG2 THR A 136 46.299 -9.880 224.093 1.00 53.24 C
ANISOU 883 CG2 THR A 136 3662 7488 9079 -45 -372 -1550 C
ATOM 884 N LEU A 137 43.560 -12.228 225.255 1.00 58.74 N
ANISOU 884 N LEU A 137 4806 8173 9341 438 -739 -1025 N
ATOM 885 CA LEU A 137 43.611 -13.237 226.310 1.00 58.62 C
ANISOU 885 CA LEU A 137 4866 8264 9143 719 -956 -1008 C
ATOM 886 C LEU A 137 43.475 -14.636 225.726 1.00 55.17 C
ANISOU 886 C LEU A 137 4528 7793 8639 894 -940 -875 C
ATOM 887 O LEU A 137 44.132 -15.581 226.186 1.00 55.52 O
ANISOU 887 O LEU A 137 4594 7924 8577 1143 -1062 -909 O
ATOM 888 CB LEU A 137 42.516 -12.980 227.346 1.00 57.94 C
ANISOU 888 CB LEU A 137 4943 8157 8915 755 -1078 -941 C
ATOM 889 CG LEU A 137 42.658 -11.761 228.257 1.00 55.35 C
ANISOU 889 CG LEU A 137 4546 7874 8609 655 -1142 -1084 C
ATOM 890 CD1 LEU A 137 41.382 -11.577 229.042 1.00 53.05 C
ANISOU 890 CD1 LEU A 137 4430 7529 8200 675 -1215 -992 C
ATOM 891 CD2 LEU A 137 43.835 -11.915 229.203 1.00 51.24 C
ANISOU 891 CD2 LEU A 137 3921 7508 8042 808 -1316 -1269 C
ATOM 892 N SER A 138 42.659 -14.778 224.679 1.00 56.43 N
ANISOU 892 N SER A 138 4811 7804 8828 757 -768 -706 N
ATOM 893 CA SER A 138 42.476 -16.084 224.055 1.00 45.75 C
ANISOU 893 CA SER A 138 3674 6372 7337 859 -688 -536 C
ATOM 894 C SER A 138 43.774 -16.565 223.426 1.00 48.45 C
ANISOU 894 C SER A 138 3816 6773 7821 950 -634 -653 C
ATOM 895 O SER A 138 44.173 -17.721 223.596 1.00 59.50 O
ANISOU 895 O SER A 138 5303 8207 9098 1198 -695 -625 O
ATOM 896 CB SER A 138 41.363 -16.013 223.005 1.00 47.94 C
ANISOU 896 CB SER A 138 4170 6471 7573 638 -494 -328 C
ATOM 897 OG SER A 138 40.091 -15.891 223.613 1.00 57.83 O
ANISOU 897 OG SER A 138 5618 7687 8669 604 -545 -218 O
ATOM 898 N PHE A 139 44.458 -15.681 222.701 1.00 56.70 N
ANISOU 898 N PHE A 139 4604 7819 9120 755 -500 -797 N
ATOM 899 CA PHE A 139 45.713 -16.080 222.075 1.00 56.50 C
ANISOU 899 CA PHE A 139 4383 7848 9237 806 -408 -929 C
ATOM 900 C PHE A 139 46.813 -16.331 223.101 1.00 64.29 C
ANISOU 900 C PHE A 139 5243 9031 10152 1023 -605 -1094 C
ATOM 901 O PHE A 139 47.667 -17.196 222.881 1.00 67.82 O
ANISOU 901 O PHE A 139 5621 9538 10609 1206 -606 -1142 O
ATOM 902 CB PHE A 139 46.141 -15.036 221.048 1.00 62.87 C
ANISOU 902 CB PHE A 139 5072 8561 10255 487 -161 -1025 C
ATOM 903 CG PHE A 139 45.391 -15.137 219.751 1.00 73.86 C
ANISOU 903 CG PHE A 139 6682 9723 11659 304 76 -829 C
ATOM 904 CD1 PHE A 139 44.009 -15.239 219.741 1.00 80.05 C
ANISOU 904 CD1 PHE A 139 7791 10390 12235 265 46 -581 C
ATOM 905 CD2 PHE A 139 46.066 -15.135 218.545 1.00 86.62 C
ANISOU 905 CD2 PHE A 139 8252 11230 13429 157 334 -880 C
ATOM 906 CE1 PHE A 139 43.317 -15.336 218.554 1.00 78.40 C
ANISOU 906 CE1 PHE A 139 7844 9981 11965 102 230 -392 C
ATOM 907 CE2 PHE A 139 45.379 -15.228 217.351 1.00 91.60 C
ANISOU 907 CE2 PHE A 139 9193 11628 13983 -12 537 -671 C
ATOM 908 CZ PHE A 139 44.001 -15.328 217.357 1.00 85.96 C
ANISOU 908 CZ PHE A 139 8790 10819 13052 -31 465 -428 C
ATOM 909 N ILE A 140 46.805 -15.618 224.233 1.00 69.40 N
ANISOU 909 N ILE A 140 5868 9769 10732 1019 -774 -1183 N
ATOM 910 CA ILE A 140 47.760 -15.945 225.293 1.00 65.12 C
ANISOU 910 CA ILE A 140 5237 9397 10110 1246 -989 -1332 C
ATOM 911 C ILE A 140 47.486 -17.342 225.832 1.00 64.19 C
ANISOU 911 C ILE A 140 5346 9283 9762 1592 -1144 -1201 C
ATOM 912 O ILE A 140 48.410 -18.144 226.036 1.00 69.04 O
ANISOU 912 O ILE A 140 5914 9986 10334 1832 -1236 -1277 O
ATOM 913 CB ILE A 140 47.705 -14.898 226.422 1.00 61.90 C
ANISOU 913 CB ILE A 140 4791 9059 9670 1168 -1130 -1452 C
ATOM 914 CG1 ILE A 140 48.272 -13.559 225.957 1.00 71.20 C
ANISOU 914 CG1 ILE A 140 5752 10238 11061 863 -975 -1632 C
ATOM 915 CG2 ILE A 140 48.458 -15.404 227.641 1.00 53.04 C
ANISOU 915 CG2 ILE A 140 3645 8092 8414 1448 -1391 -1580 C
ATOM 916 CD1 ILE A 140 48.083 -12.449 226.968 1.00 66.12 C
ANISOU 916 CD1 ILE A 140 5097 9634 10392 762 -1075 -1738 C
ATOM 917 N ALA A 141 46.206 -17.661 226.060 1.00 64.50 N
ANISOU 917 N ALA A 141 5657 9212 9637 1629 -1166 -1013 N
ATOM 918 CA ALA A 141 45.863 -18.992 226.541 1.00 66.64 C
ANISOU 918 CA ALA A 141 6230 9443 9646 1948 -1277 -887 C
ATOM 919 C ALA A 141 46.248 -20.052 225.520 1.00 65.93 C
ANISOU 919 C ALA A 141 6175 9299 9578 2079 -1144 -814 C
ATOM 920 O ALA A 141 46.718 -21.133 225.884 1.00 73.34 O
ANISOU 920 O ALA A 141 7277 10249 10341 2380 -1232 -797 O
ATOM 921 CB ALA A 141 44.369 -19.070 226.854 1.00 59.27 C
ANISOU 921 CB ALA A 141 5588 8391 8543 1925 -1283 -716 C
ATOM 922 N LEU A 142 46.105 -19.736 224.233 1.00 63.17 N
ANISOU 922 N LEU A 142 5688 8873 9440 1857 -920 -784 N
ATOM 923 CA LEU A 142 46.442 -20.694 223.184 1.00 63.48 C
ANISOU 923 CA LEU A 142 5810 8821 9490 1923 -739 -698 C
ATOM 924 C LEU A 142 47.941 -20.940 223.127 1.00 67.44 C
ANISOU 924 C LEU A 142 6036 9465 10124 2086 -773 -890 C
ATOM 925 O LEU A 142 48.393 -22.090 223.016 1.00 70.96 O
ANISOU 925 O LEU A 142 6607 9896 10460 2362 -776 -848 O
ATOM 926 CB LEU A 142 45.935 -20.173 221.842 1.00 61.56 C
ANISOU 926 CB LEU A 142 5598 8410 9382 1536 -447 -584 C
ATOM 927 CG LEU A 142 45.737 -21.155 220.696 1.00 67.99 C
ANISOU 927 CG LEU A 142 6679 9045 10111 1496 -213 -394 C
ATOM 928 CD1 LEU A 142 44.622 -22.126 221.042 1.00 64.59 C
ANISOU 928 CD1 LEU A 142 6709 8492 9339 1573 -227 -157 C
ATOM 929 CD2 LEU A 142 45.408 -20.393 219.425 1.00 74.76 C
ANISOU 929 CD2 LEU A 142 7518 9758 11128 1122 34 -338 C
ATOM 930 N ASP A 143 48.728 -19.865 223.215 1.00 68.88 N
ANISOU 930 N ASP A 143 5904 9766 10503 1886 -776 -1086 N
ATOM 931 CA ASP A 143 50.177 -20.003 223.182 1.00 63.17 C
ANISOU 931 CA ASP A 143 4923 9181 9897 1982 -797 -1282 C
ATOM 932 C ASP A 143 50.670 -20.800 224.380 1.00 66.16 C
ANISOU 932 C ASP A 143 5398 9674 10066 2348 -1074 -1323 C
ATOM 933 O ASP A 143 51.501 -21.705 224.232 1.00 84.14 O
ANISOU 933 O ASP A 143 7645 11996 12329 2592 -1093 -1364 O
ATOM 934 CB ASP A 143 50.814 -18.611 223.127 1.00 72.77 C
ANISOU 934 CB ASP A 143 5834 10484 11330 1679 -745 -1503 C
ATOM 935 CG ASP A 143 52.314 -18.635 223.338 1.00 87.02 C
ANISOU 935 CG ASP A 143 7345 12469 13251 1778 -815 -1757 C
ATOM 936 OD1 ASP A 143 52.752 -18.697 224.509 1.00 87.77 O
ANISOU 936 OD1 ASP A 143 7400 12709 13239 1973 -1077 -1869 O
ATOM 937 OD2 ASP A 143 53.055 -18.593 222.332 1.00 93.68 O
ANISOU 937 OD2 ASP A 143 8001 13302 14291 1660 -605 -1859 O
ATOM 938 N ARG A 144 50.128 -20.516 225.570 1.00 72.56 N
ANISOU 938 N ARG A 144 6359 10513 10698 2400 -1283 -1311 N
ATOM 939 CA ARG A 144 50.523 -21.281 226.749 1.00 70.64 C
ANISOU 939 CA ARG A 144 6275 10348 10216 2750 -1544 -1355 C
ATOM 940 C ARG A 144 50.060 -22.734 226.659 1.00 73.58 C
ANISOU 940 C ARG A 144 7046 10582 10330 3041 -1529 -1152 C
ATOM 941 O ARG A 144 50.784 -23.648 227.073 1.00 75.43 O
ANISOU 941 O ARG A 144 7374 10864 10423 3358 -1655 -1199 O
ATOM 942 CB ARG A 144 49.969 -20.618 228.010 1.00 72.15 C
ANISOU 942 CB ARG A 144 6579 10571 10264 2721 -1735 -1389 C
ATOM 943 CG ARG A 144 50.470 -19.197 228.240 1.00 72.29 C
ANISOU 943 CG ARG A 144 6255 10716 10496 2459 -1757 -1604 C
ATOM 944 CD ARG A 144 51.959 -19.187 228.545 1.00 67.86 C
ANISOU 944 CD ARG A 144 5396 10353 10034 2593 -1889 -1871 C
ATOM 945 NE ARG A 144 52.770 -19.312 227.336 1.00 71.72 N
ANISOU 945 NE ARG A 144 5622 10868 10760 2508 -1693 -1939 N
ATOM 946 CZ ARG A 144 54.040 -19.700 227.328 1.00 79.00 C
ANISOU 946 CZ ARG A 144 6309 11942 11764 2682 -1769 -2135 C
ATOM 947 NH1 ARG A 144 54.640 -20.020 228.465 1.00 81.05 N
ANISOU 947 NH1 ARG A 144 6570 12348 11879 2968 -2056 -2280 N
ATOM 948 NH2 ARG A 144 54.706 -19.782 226.183 1.00 80.65 N
ANISOU 948 NH2 ARG A 144 6289 12156 12196 2581 -1557 -2195 N
ATOM 949 N TRP A 145 48.869 -22.972 226.100 1.00 76.75 N
ANISOU 949 N TRP A 145 7706 10803 10653 2942 -1368 -934 N
ATOM 950 CA TRP A 145 48.347 -24.330 226.038 1.00 72.89 C
ANISOU 950 CA TRP A 145 7671 10152 9871 3193 -1321 -738 C
ATOM 951 C TRP A 145 49.168 -25.192 225.093 1.00 70.49 C
ANISOU 951 C TRP A 145 7313 9824 9646 3337 -1183 -734 C
ATOM 952 O TRP A 145 49.461 -26.354 225.400 1.00 73.92 O
ANISOU 952 O TRP A 145 8042 10206 9839 3643 -1232 -680 O
ATOM 953 CB TRP A 145 46.881 -24.297 225.608 1.00 65.71 C
ANISOU 953 CB TRP A 145 7035 9067 8865 3032 -1166 -526 C
ATOM 954 CG TRP A 145 46.174 -25.606 225.743 1.00 64.44 C
ANISOU 954 CG TRP A 145 7441 8710 8333 3244 -1094 -314 C
ATOM 955 CD1 TRP A 145 45.747 -26.194 226.901 1.00 66.70 C
ANISOU 955 CD1 TRP A 145 8149 8926 8269 3424 -1213 -259 C
ATOM 956 CD2 TRP A 145 45.793 -26.488 224.681 1.00 62.68 C
ANISOU 956 CD2 TRP A 145 7495 8298 8022 3201 -824 -123 C
ATOM 957 NE1 TRP A 145 45.134 -27.392 226.623 1.00 66.99 N
ANISOU 957 NE1 TRP A 145 8706 8740 8006 3526 -1033 -55 N
ATOM 958 CE2 TRP A 145 45.147 -27.594 225.267 1.00 66.18 C
ANISOU 958 CE2 TRP A 145 8524 8564 8059 3379 -793 36 C
ATOM 959 CE3 TRP A 145 45.946 -26.454 223.292 1.00 61.65 C
ANISOU 959 CE3 TRP A 145 7219 8106 8099 2957 -572 -73 C
ATOM 960 CZ2 TRP A 145 44.649 -28.653 224.513 1.00 63.73 C
ANISOU 960 CZ2 TRP A 145 8631 8032 7553 3304 -518 234 C
ATOM 961 CZ3 TRP A 145 45.451 -27.507 222.544 1.00 58.41 C
ANISOU 961 CZ3 TRP A 145 7223 7479 7491 2900 -322 133 C
ATOM 962 CH2 TRP A 145 44.810 -28.591 223.156 1.00 55.40 C
ANISOU 962 CH2 TRP A 145 7398 6939 6713 3066 -297 280 C
ATOM 963 N TYR A 146 49.546 -24.646 223.934 1.00 65.41 N
ANISOU 963 N TYR A 146 6324 9202 9325 3117 -988 -796 N
ATOM 964 CA TYR A 146 50.422 -25.398 223.041 1.00 67.32 C
ANISOU 964 CA TYR A 146 6480 9426 9673 3247 -838 -820 C
ATOM 965 C TYR A 146 51.843 -25.501 223.578 1.00 81.49 C
ANISOU 965 C TYR A 146 8001 11416 11547 3440 -1011 -1038 C
ATOM 966 O TYR A 146 52.525 -26.496 223.312 1.00 84.44 O
ANISOU 966 O TYR A 146 8439 11772 11873 3695 -980 -1037 O
ATOM 967 CB TYR A 146 50.428 -24.782 221.644 1.00 68.32 C
ANISOU 967 CB TYR A 146 6346 9503 10109 2946 -549 -845 C
ATOM 968 CG TYR A 146 49.265 -25.232 220.791 1.00 68.15 C
ANISOU 968 CG TYR A 146 6689 9248 9956 2839 -320 -601 C
ATOM 969 CD1 TYR A 146 49.179 -26.543 220.335 1.00 69.03 C
ANISOU 969 CD1 TYR A 146 7193 9190 9847 3014 -175 -420 C
ATOM 970 CD2 TYR A 146 48.256 -24.351 220.442 1.00 57.27 C
ANISOU 970 CD2 TYR A 146 5379 7766 8615 2412 -208 -491 C
ATOM 971 CE1 TYR A 146 48.112 -26.960 219.556 1.00 70.98 C
ANISOU 971 CE1 TYR A 146 7867 9183 9917 2737 74 -150 C
ATOM 972 CE2 TYR A 146 47.192 -24.757 219.663 1.00 59.52 C
ANISOU 972 CE2 TYR A 146 6069 7814 8731 2169 14 -226 C
ATOM 973 CZ TYR A 146 47.122 -26.062 219.225 1.00 64.09 C
ANISOU 973 CZ TYR A 146 7014 8241 9096 2316 153 -63 C
ATOM 974 OH TYR A 146 46.057 -26.454 218.446 1.00 64.52 O
ANISOU 974 OH TYR A 146 7455 8077 8983 2048 369 174 O
ATOM 975 N ALA A 147 52.320 -24.500 224.325 1.00 82.71 N
ANISOU 975 N ALA A 147 7859 11754 11810 3332 -1189 -1234 N
ATOM 976 CA ALA A 147 53.693 -24.576 224.817 1.00 76.51 C
ANISOU 976 CA ALA A 147 6798 11175 11099 3523 -1362 -1471 C
ATOM 977 C ALA A 147 53.833 -25.611 225.927 1.00 85.31 C
ANISOU 977 C ALA A 147 8233 12307 11875 3940 -1622 -1449 C
ATOM 978 O ALA A 147 54.840 -26.327 225.991 1.00 93.16 O
ANISOU 978 O ALA A 147 9149 13390 12855 4223 -1705 -1555 O
ATOM 979 CB ALA A 147 54.160 -23.201 225.300 1.00 69.81 C
ANISOU 979 CB ALA A 147 5578 10507 10438 3282 -1465 -1708 C
ATOM 980 N ILE A 148 52.829 -25.724 226.790 1.00 85.78 N
ANISOU 980 N ILE A 148 8678 12272 11644 3989 -1737 -1317 N
ATOM 981 CA ILE A 148 52.912 -26.564 227.980 1.00 79.38 C
ANISOU 981 CA ILE A 148 8224 11467 10470 4360 -1979 -1320 C
ATOM 982 C ILE A 148 52.246 -27.916 227.766 1.00 77.98 C
ANISOU 982 C ILE A 148 8600 11061 9969 4569 -1859 -1076 C
ATOM 983 O ILE A 148 52.797 -28.951 228.139 1.00 84.30 O
ANISOU 983 O ILE A 148 9632 11858 10542 4923 -1957 -1092 O
ATOM 984 CB ILE A 148 52.298 -25.822 229.187 1.00 79.94 C
ANISOU 984 CB ILE A 148 8409 11569 10397 4288 -2166 -1361 C
ATOM 985 CG1 ILE A 148 53.134 -24.587 229.531 1.00 80.51 C
ANISOU 985 CG1 ILE A 148 7977 11873 10740 4129 -2302 -1634 C
ATOM 986 CG2 ILE A 148 52.164 -26.756 230.379 1.00 86.39 C
ANISOU 986 CG2 ILE A 148 9711 12329 10784 4660 -2365 -1333 C
ATOM 987 CD1 ILE A 148 52.433 -23.609 230.444 1.00 82.68 C
ANISOU 987 CD1 ILE A 148 8303 12155 10955 3955 -2409 -1662 C
ATOM 988 N CYS A 149 51.050 -27.927 227.177 1.00 85.89 N
ANISOU 988 N CYS A 149 9845 11865 10923 4355 -1641 -858 N
ATOM 989 CA CYS A 149 50.270 -29.155 227.087 1.00 82.49 C
ANISOU 989 CA CYS A 149 10016 11196 10131 4507 -1503 -626 C
ATOM 990 C CYS A 149 50.530 -29.946 225.809 1.00 77.60 C
ANISOU 990 C CYS A 149 9435 10462 9586 4537 -1252 -521 C
ATOM 991 O CYS A 149 50.511 -31.183 225.839 1.00 83.27 O
ANISOU 991 O CYS A 149 10603 11041 9997 4776 -1183 -406 O
ATOM 992 CB CYS A 149 48.778 -28.834 227.208 1.00 76.53 C
ANISOU 992 CB CYS A 149 9563 10277 9237 4272 -1392 -449 C
ATOM 993 SG CYS A 149 48.287 -28.339 228.873 1.00 80.54 S
ANISOU 993 SG CYS A 149 10262 10830 9511 4319 -1644 -524 S
ATOM 994 N HIS A 150 50.751 -29.274 224.680 1.00 76.28 N
ANISOU 994 N HIS A 150 8850 10334 9799 4292 -1086 -559 N
ATOM 995 CA HIS A 150 51.030 -29.949 223.411 1.00 76.75 C
ANISOU 995 CA HIS A 150 8932 10274 9954 4307 -821 -478 C
ATOM 996 C HIS A 150 52.192 -29.260 222.705 1.00 82.51 C
ANISOU 996 C HIS A 150 9044 11177 11129 4209 -779 -694 C
ATOM 997 O HIS A 150 52.022 -28.614 221.664 1.00 83.30 O
ANISOU 997 O HIS A 150 8907 11241 11503 3929 -554 -696 O
ATOM 998 CB HIS A 150 49.773 -29.986 222.540 1.00 74.32 C
ANISOU 998 CB HIS A 150 8919 9741 9580 4067 -539 -247 C
ATOM 999 CG HIS A 150 48.593 -30.607 223.224 1.00 71.32 C
ANISOU 999 CG HIS A 150 9146 9181 8772 4102 -533 -44 C
ATOM 1000 ND1 HIS A 150 48.412 -31.971 223.302 1.00 70.46 N
ANISOU 1000 ND1 HIS A 150 9597 8885 8289 4292 -421 106 N
ATOM 1001 CD2 HIS A 150 47.549 -30.052 223.883 1.00 67.36 C
ANISOU 1001 CD2 HIS A 150 8789 8650 8156 3949 -600 16 C
ATOM 1002 CE1 HIS A 150 47.302 -32.230 223.970 1.00 67.74 C
ANISOU 1002 CE1 HIS A 150 9722 8398 7620 4228 -397 239 C
ATOM 1003 NE2 HIS A 150 46.758 -31.082 224.334 1.00 69.53 N
ANISOU 1003 NE2 HIS A 150 9699 8716 8005 4031 -509 191 N
ATOM 1004 N PRO A 151 53.403 -29.410 223.235 1.00 81.44 N
ANISOU 1004 N PRO A 151 8662 11226 11057 4437 -970 -888 N
ATOM 1005 CA PRO A 151 54.575 -28.776 222.620 1.00 84.57 C
ANISOU 1005 CA PRO A 151 8478 11794 11860 4333 -907 -1112 C
ATOM 1006 C PRO A 151 54.974 -29.421 221.300 1.00 90.06 C
ANISOU 1006 C PRO A 151 9145 12364 12711 4350 -598 -1065 C
ATOM 1007 O PRO A 151 54.637 -30.568 220.997 1.00 93.12 O
ANISOU 1007 O PRO A 151 9961 12559 12860 4539 -488 -887 O
ATOM 1008 CB PRO A 151 55.673 -28.969 223.669 1.00 86.39 C
ANISOU 1008 CB PRO A 151 8546 12249 12029 4639 -1221 -1320 C
ATOM 1009 CG PRO A 151 55.265 -30.203 224.396 1.00 86.65 C
ANISOU 1009 CG PRO A 151 9149 12158 11615 4994 -1349 -1165 C
ATOM 1010 CD PRO A 151 53.755 -30.145 224.459 1.00 84.33 C
ANISOU 1010 CD PRO A 151 9286 11657 11099 4805 -1249 -927 C
ATOM 1011 N LEU A 152 55.709 -28.643 220.507 1.00 94.92 N
ANISOU 1011 N LEU A 152 9278 13081 13706 4126 -431 -1233 N
ATOM 1012 CA LEU A 152 56.371 -29.045 219.265 1.00 96.80 C
ANISOU 1012 CA LEU A 152 9371 13245 14165 4115 -119 -1263 C
ATOM 1013 C LEU A 152 55.411 -29.216 218.099 1.00 89.04 C
ANISOU 1013 C LEU A 152 8665 11994 13173 3915 228 -1069 C
ATOM 1014 O LEU A 152 55.781 -29.836 217.095 1.00 97.14 O
ANISOU 1014 O LEU A 152 9729 12889 14290 3957 507 -1048 O
ATOM 1015 CB LEU A 152 57.164 -30.342 219.430 1.00 97.73 C
ANISOU 1015 CB LEU A 152 9620 13354 14158 4535 -187 -1270 C
ATOM 1016 CG LEU A 152 58.250 -30.277 220.502 1.00 97.38 C
ANISOU 1016 CG LEU A 152 9291 13592 14119 4790 -531 -1497 C
ATOM 1017 CD1 LEU A 152 59.156 -31.494 220.433 1.00 95.16 C
ANISOU 1017 CD1 LEU A 152 9072 13311 13773 5195 -552 -1531 C
ATOM 1018 CD2 LEU A 152 59.041 -28.991 220.353 1.00 97.75 C
ANISOU 1018 CD2 LEU A 152 8748 13873 14519 4511 -519 -1764 C
ATOM 1019 N LEU A 153 54.193 -28.691 218.192 1.00 89.66 N
ANISOU 1019 N LEU A 153 8945 11986 13137 3705 225 -938 N
ATOM 1020 CA LEU A 153 53.255 -28.686 217.078 1.00 89.85 C
ANISOU 1020 CA LEU A 153 9208 11792 13140 3498 543 -781 C
ATOM 1021 C LEU A 153 53.298 -27.378 216.301 1.00 90.12 C
ANISOU 1021 C LEU A 153 8863 11855 13523 3054 733 -930 C
ATOM 1022 O LEU A 153 53.437 -27.390 215.074 1.00 88.58 O
ANISOU 1022 O LEU A 153 8709 11486 13460 2791 1078 -890 O
ATOM 1023 CB LEU A 153 51.833 -28.945 217.587 1.00 90.02 C
ANISOU 1023 CB LEU A 153 9753 11671 12780 3468 459 -504 C
ATOM 1024 CG LEU A 153 51.628 -30.257 218.343 1.00 94.91 C
ANISOU 1024 CG LEU A 153 10867 12200 12997 3836 321 -346 C
ATOM 1025 CD1 LEU A 153 50.180 -30.402 218.792 1.00 92.55 C
ANISOU 1025 CD1 LEU A 153 11070 11745 12352 3729 307 -94 C
ATOM 1026 CD2 LEU A 153 52.053 -31.439 217.485 1.00 94.30 C
ANISOU 1026 CD2 LEU A 153 11052 11947 12832 3982 573 -248 C
ATOM 1027 N PHE A 154 53.193 -26.245 216.995 1.00 81.67 N
ANISOU 1027 N PHE A 154 7548 10947 12538 2860 537 -1037 N
ATOM 1028 CA PHE A 154 53.219 -24.930 216.368 1.00 89.18 C
ANISOU 1028 CA PHE A 154 8234 11896 13754 2392 704 -1160 C
ATOM 1029 C PHE A 154 54.304 -24.098 217.032 1.00 93.01 C
ANISOU 1029 C PHE A 154 8322 12653 14366 2344 521 -1408 C
ATOM 1030 O PHE A 154 54.299 -23.930 218.255 1.00 90.59 O
ANISOU 1030 O PHE A 154 7981 12500 13939 2494 202 -1438 O
ATOM 1031 CB PHE A 154 51.856 -24.237 216.481 1.00 84.70 C
ANISOU 1031 CB PHE A 154 7892 11195 13097 2106 683 -993 C
ATOM 1032 CG PHE A 154 50.738 -24.988 215.811 1.00 82.89 C
ANISOU 1032 CG PHE A 154 8245 10677 12571 1979 852 -632 C
ATOM 1033 CD1 PHE A 154 50.430 -24.754 214.481 1.00 82.11 C
ANISOU 1033 CD1 PHE A 154 8313 10347 12537 1611 1179 -519 C
ATOM 1034 CD2 PHE A 154 49.998 -25.930 216.509 1.00 82.10 C
ANISOU 1034 CD2 PHE A 154 8546 10532 12118 2218 693 -423 C
ATOM 1035 CE1 PHE A 154 49.404 -25.444 213.859 1.00 79.46 C
ANISOU 1035 CE1 PHE A 154 8492 9771 11927 1487 1312 -214 C
ATOM 1036 CE2 PHE A 154 48.968 -26.621 215.892 1.00 79.98 C
ANISOU 1036 CE2 PHE A 154 8789 10014 11584 2065 863 -128 C
ATOM 1037 CZ PHE A 154 48.674 -26.379 214.565 1.00 76.13 C
ANISOU 1037 CZ PHE A 154 8422 9330 11175 1702 1158 -28 C
ATOM 1038 N LYS A 155 55.244 -23.601 216.233 1.00 92.08 N
ANISOU 1038 N LYS A 155 7936 12562 14488 2119 734 -1600 N
ATOM 1039 CA LYS A 155 56.244 -22.681 216.751 1.00 98.84 C
ANISOU 1039 CA LYS A 155 8419 13637 15500 2003 605 -1876 C
ATOM 1040 C LYS A 155 55.593 -21.357 217.129 1.00 92.56 C
ANISOU 1040 C LYS A 155 7614 12829 14725 1673 540 -1910 C
ATOM 1041 O LYS A 155 54.768 -20.817 216.389 1.00 88.82 O
ANISOU 1041 O LYS A 155 7311 12149 14287 1365 752 -1807 O
ATOM 1042 CB LYS A 155 57.356 -22.462 215.725 1.00102.68 C
ANISOU 1042 CB LYS A 155 8660 14114 16239 1810 888 -2090 C
ATOM 1043 CG LYS A 155 58.295 -23.652 215.577 1.00110.17 C
ANISOU 1043 CG LYS A 155 9518 15147 17195 2174 902 -2125 C
ATOM 1044 CD LYS A 155 59.501 -23.321 214.712 1.00110.95 C
ANISOU 1044 CD LYS A 155 9316 15274 17564 1973 1154 -2389 C
ATOM 1045 CE LYS A 155 60.527 -24.441 214.749 1.00113.23 C
ANISOU 1045 CE LYS A 155 9455 15695 17872 2374 1118 -2453 C
ATOM 1046 NZ LYS A 155 61.738 -24.122 213.941 1.00114.12 N
ANISOU 1046 NZ LYS A 155 9247 15850 18265 2178 1363 -2739 N
ATOM 1047 N SER A 156 55.994 -20.822 218.281 1.00 94.66 N
ANISOU 1047 N SER A 156 7698 13300 14969 1738 255 -2062 N
ATOM 1048 CA SER A 156 55.495 -19.549 218.791 1.00 92.77 C
ANISOU 1048 CA SER A 156 7445 13066 14737 1463 178 -2118 C
ATOM 1049 C SER A 156 56.687 -18.617 218.953 1.00 91.13 C
ANISOU 1049 C SER A 156 6889 13007 14731 1287 182 -2462 C
ATOM 1050 O SER A 156 57.553 -18.851 219.805 1.00 92.81 O
ANISOU 1050 O SER A 156 6884 13440 14940 1516 -52 -2636 O
ATOM 1051 CB SER A 156 54.758 -19.731 220.118 1.00105.21 C
ANISOU 1051 CB SER A 156 9183 14719 16073 1690 -157 -1991 C
ATOM 1052 OG SER A 156 55.666 -19.975 221.179 1.00109.45 O
ANISOU 1052 OG SER A 156 9540 15479 16569 1953 -437 -2163 O
ATOM 1053 N THR A 157 56.733 -17.567 218.141 1.00 88.59 N
ANISOU 1053 N THR A 157 6536 12547 14577 883 455 -2573 N
ATOM 1054 CA THR A 157 57.811 -16.592 218.183 1.00 98.75 C
ANISOU 1054 CA THR A 157 7529 13930 16063 665 521 -2922 C
ATOM 1055 C THR A 157 57.218 -15.200 218.347 1.00 94.16 C
ANISOU 1055 C THR A 157 7051 13239 15485 336 581 -2959 C
ATOM 1056 O THR A 157 56.049 -14.959 218.037 1.00 92.36 O
ANISOU 1056 O THR A 157 7116 12818 15159 216 661 -2721 O
ATOM 1057 CB THR A 157 58.681 -16.652 216.920 1.00101.14 C
ANISOU 1057 CB THR A 157 7714 14132 16584 483 865 -3083 C
ATOM 1058 OG1 THR A 157 57.894 -16.292 215.778 1.00105.61 O
ANISOU 1058 OG1 THR A 157 8578 14383 17165 184 1189 -2921 O
ATOM 1059 CG2 THR A 157 59.235 -18.056 216.724 1.00 99.03 C
ANISOU 1059 CG2 THR A 157 7359 13961 16306 830 825 -3029 C
ATOM 1060 N ALA A 158 58.038 -14.280 218.854 1.00 96.28 N
ANISOU 1060 N ALA A 158 7078 13636 15868 202 544 -3273 N
ATOM 1061 CA ALA A 158 57.565 -12.915 219.044 1.00 97.18 C
ANISOU 1061 CA ALA A 158 7295 13644 15983 -95 622 -3332 C
ATOM 1062 C ALA A 158 57.186 -12.271 217.714 1.00102.36 C
ANISOU 1062 C ALA A 158 8181 13985 16725 -446 1021 -3283 C
ATOM 1063 O ALA A 158 56.204 -11.516 217.634 1.00107.52 O
ANISOU 1063 O ALA A 158 9094 14464 17295 -613 1092 -3136 O
ATOM 1064 CB ALA A 158 58.638 -12.093 219.757 1.00101.91 C
ANISOU 1064 CB ALA A 158 7581 14437 16703 -178 549 -3717 C
ATOM 1065 N ARG A 159 57.936 -12.574 216.652 1.00107.88 N
ANISOU 1065 N ARG A 159 8815 14593 17580 -549 1291 -3400 N
ATOM 1066 CA ARG A 159 57.643 -11.963 215.360 1.00115.83 C
ANISOU 1066 CA ARG A 159 10096 15266 18650 -879 1690 -3369 C
ATOM 1067 C ARG A 159 56.309 -12.450 214.809 1.00112.36 C
ANISOU 1067 C ARG A 159 10024 14613 18054 -841 1730 -2976 C
ATOM 1068 O ARG A 159 55.576 -11.684 214.176 1.00114.18 O
ANISOU 1068 O ARG A 159 10565 14579 18239 -1074 1938 -2871 O
ATOM 1069 CB ARG A 159 58.780 -12.241 214.373 1.00130.34 C
ANISOU 1069 CB ARG A 159 11799 17041 20685 -992 1977 -3594 C
ATOM 1070 CG ARG A 159 58.927 -13.690 213.943 1.00137.30 C
ANISOU 1070 CG ARG A 159 12640 17964 21563 -742 1951 -3438 C
ATOM 1071 CD ARG A 159 60.056 -13.830 212.931 1.00147.70 C
ANISOU 1071 CD ARG A 159 13835 19194 23091 -893 2271 -3681 C
ATOM 1072 NE ARG A 159 60.119 -15.167 212.351 1.00152.09 N
ANISOU 1072 NE ARG A 159 14417 19734 23638 -681 2314 -3509 N
ATOM 1073 CZ ARG A 159 59.290 -15.607 211.410 1.00154.50 C
ANISOU 1073 CZ ARG A 159 15090 19759 23852 -738 2513 -3223 C
ATOM 1074 NH1 ARG A 159 58.328 -14.817 210.951 1.00151.87 N
ANISOU 1074 NH1 ARG A 159 15128 19149 23426 -983 2663 -3071 N
ATOM 1075 NH2 ARG A 159 59.418 -16.838 210.932 1.00155.54 N
ANISOU 1075 NH2 ARG A 159 15239 19884 23974 -536 2563 -3088 N
ATOM 1076 N ARG A 160 55.972 -13.721 215.038 1.00111.36 N
ANISOU 1076 N ARG A 160 9885 14596 17831 -538 1540 -2763 N
ATOM 1077 CA ARG A 160 54.635 -14.203 214.712 1.00111.67 C
ANISOU 1077 CA ARG A 160 10245 14472 17714 -485 1539 -2409 C
ATOM 1078 C ARG A 160 53.586 -13.666 215.678 1.00106.83 C
ANISOU 1078 C ARG A 160 9734 13909 16949 -446 1298 -2271 C
ATOM 1079 O ARG A 160 52.411 -13.556 215.306 1.00111.85 O
ANISOU 1079 O ARG A 160 10655 14359 17484 -523 1358 -2029 O
ATOM 1080 CB ARG A 160 54.638 -15.734 214.677 1.00121.91 C
ANISOU 1080 CB ARG A 160 11513 15858 18949 -166 1442 -2251 C
ATOM 1081 CG ARG A 160 55.623 -16.293 213.657 1.00129.68 C
ANISOU 1081 CG ARG A 160 12419 16771 20083 -203 1707 -2369 C
ATOM 1082 CD ARG A 160 55.774 -17.800 213.751 1.00137.52 C
ANISOU 1082 CD ARG A 160 13364 17880 21008 163 1601 -2245 C
ATOM 1083 NE ARG A 160 56.821 -18.286 212.857 1.00147.43 N
ANISOU 1083 NE ARG A 160 14509 19089 22417 138 1847 -2387 N
ATOM 1084 CZ ARG A 160 56.602 -18.789 211.646 1.00151.19 C
ANISOU 1084 CZ ARG A 160 15234 19304 22909 30 2161 -2249 C
ATOM 1085 NH1 ARG A 160 57.622 -19.200 210.903 1.00153.72 N
ANISOU 1085 NH1 ARG A 160 15442 19590 23373 9 2381 -2399 N
ATOM 1086 NH2 ARG A 160 55.364 -18.887 211.178 1.00149.03 N
ANISOU 1086 NH2 ARG A 160 15329 18792 22503 -62 2261 -1963 N
ATOM 1087 N ALA A 161 53.985 -13.323 216.905 1.00 98.98 N
ANISOU 1087 N ALA A 161 8520 13154 15934 -331 1031 -2426 N
ATOM 1088 CA ALA A 161 53.066 -12.646 217.812 1.00 93.11 C
ANISOU 1088 CA ALA A 161 7883 12435 15059 -335 841 -2329 C
ATOM 1089 C ALA A 161 52.672 -11.271 217.287 1.00 90.35 C
ANISOU 1089 C ALA A 161 7713 11864 14752 -673 1077 -2367 C
ATOM 1090 O ALA A 161 51.531 -10.840 217.484 1.00 87.31 O
ANISOU 1090 O ALA A 161 7539 11381 14253 -713 1028 -2180 O
ATOM 1091 CB ALA A 161 53.685 -12.521 219.207 1.00 92.86 C
ANISOU 1091 CB ALA A 161 7604 12681 14996 -161 536 -2510 C
ATOM 1092 N LEU A 162 53.588 -10.574 216.609 1.00 84.73 N
ANISOU 1092 N LEU A 162 6940 11059 14194 -908 1346 -2613 N
ATOM 1093 CA LEU A 162 53.215 -9.296 216.006 1.00 89.31 C
ANISOU 1093 CA LEU A 162 7766 11387 14780 -1208 1612 -2639 C
ATOM 1094 C LEU A 162 52.138 -9.482 214.940 1.00 94.16 C
ANISOU 1094 C LEU A 162 8759 11718 15301 -1278 1788 -2343 C
ATOM 1095 O LEU A 162 51.197 -8.678 214.843 1.00 97.69 O
ANISOU 1095 O LEU A 162 9467 12003 15647 -1386 1837 -2208 O
ATOM 1096 CB LEU A 162 54.444 -8.614 215.402 1.00 98.58 C
ANISOU 1096 CB LEU A 162 8842 12492 16122 -1439 1907 -2974 C
ATOM 1097 CG LEU A 162 54.166 -7.421 214.479 1.00106.43 C
ANISOU 1097 CG LEU A 162 10176 13166 17098 -1737 2268 -3001 C
ATOM 1098 CD1 LEU A 162 53.719 -6.202 215.272 1.00108.50 C
ANISOU 1098 CD1 LEU A 162 10496 13442 17288 -1826 2207 -3048 C
ATOM 1099 CD2 LEU A 162 55.386 -7.095 213.626 1.00115.67 C
ANISOU 1099 CD2 LEU A 162 11297 14228 18424 -1943 2612 -3310 C
ATOM 1100 N GLY A 163 52.240 -10.555 214.151 1.00 91.42 N
ANISOU 1100 N GLY A 163 8454 11308 14973 -1205 1877 -2231 N
ATOM 1101 CA GLY A 163 51.229 -10.801 213.140 1.00 85.65 C
ANISOU 1101 CA GLY A 163 8099 10311 14134 -1266 2033 -1946 C
ATOM 1102 C GLY A 163 49.909 -11.218 213.749 1.00 91.39 C
ANISOU 1102 C GLY A 163 8914 11095 14714 -1107 1780 -1664 C
ATOM 1103 O GLY A 163 48.839 -10.835 213.265 1.00 93.39 O
ANISOU 1103 O GLY A 163 9488 11147 14848 -1198 1843 -1454 O
ATOM 1104 N SER A 164 49.964 -12.004 214.825 1.00 85.88 N
ANISOU 1104 N SER A 164 7959 10668 14001 -852 1481 -1660 N
ATOM 1105 CA SER A 164 48.736 -12.350 215.528 1.00 79.17 C
ANISOU 1105 CA SER A 164 7189 9879 13012 -699 1240 -1429 C
ATOM 1106 C SER A 164 48.066 -11.104 216.101 1.00 78.04 C
ANISOU 1106 C SER A 164 7132 9705 12813 -813 1165 -1432 C
ATOM 1107 O SER A 164 46.838 -10.983 216.068 1.00 66.73 O
ANISOU 1107 O SER A 164 5904 8171 11281 -825 1118 -1217 O
ATOM 1108 CB SER A 164 49.030 -13.362 216.639 1.00 74.60 C
ANISOU 1108 CB SER A 164 6376 9582 12385 -376 936 -1452 C
ATOM 1109 OG SER A 164 49.648 -14.525 216.122 1.00 89.08 O
ANISOU 1109 OG SER A 164 8142 11440 14264 -237 1011 -1448 O
ATOM 1110 N ILE A 165 48.859 -10.146 216.587 1.00 81.43 N
ANISOU 1110 N ILE A 165 7417 10211 13312 -907 1174 -1682 N
ATOM 1111 CA ILE A 165 48.293 -8.919 217.143 1.00 77.84 C
ANISOU 1111 CA ILE A 165 7050 9717 12810 -1016 1135 -1701 C
ATOM 1112 C ILE A 165 47.646 -8.078 216.049 1.00 82.57 C
ANISOU 1112 C ILE A 165 7994 10003 13376 -1238 1406 -1593 C
ATOM 1113 O ILE A 165 46.546 -7.530 216.228 1.00 84.04 O
ANISOU 1113 O ILE A 165 8366 10097 13470 -1259 1350 -1439 O
ATOM 1114 CB ILE A 165 49.387 -8.133 217.885 1.00 73.97 C
ANISOU 1114 CB ILE A 165 6327 9375 12404 -1076 1112 -2012 C
ATOM 1115 CG1 ILE A 165 49.795 -8.868 219.162 1.00 69.60 C
ANISOU 1115 CG1 ILE A 165 5506 9125 11815 -817 778 -2075 C
ATOM 1116 CG2 ILE A 165 48.920 -6.717 218.175 1.00 71.65 C
ANISOU 1116 CG2 ILE A 165 6171 8973 12079 -1249 1182 -2057 C
ATOM 1117 CD1 ILE A 165 51.008 -8.275 219.842 1.00 69.79 C
ANISOU 1117 CD1 ILE A 165 5270 9316 11931 -861 742 -2398 C
ATOM 1118 N LEU A 166 48.314 -7.965 214.898 1.00 89.48 N
ANISOU 1118 N LEU A 166 8990 10703 14307 -1388 1701 -1671 N
ATOM 1119 CA LEU A 166 47.727 -7.218 213.791 1.00 85.87 C
ANISOU 1119 CA LEU A 166 8946 9931 13748 -1554 1948 -1550 C
ATOM 1120 C LEU A 166 46.437 -7.867 213.315 1.00 80.85 C
ANISOU 1120 C LEU A 166 8571 9179 12968 -1467 1862 -1215 C
ATOM 1121 O LEU A 166 45.448 -7.175 213.041 1.00 79.80 O
ANISOU 1121 O LEU A 166 8744 8876 12700 -1509 1870 -1059 O
ATOM 1122 CB LEU A 166 48.727 -7.116 212.645 1.00 85.36 C
ANISOU 1122 CB LEU A 166 8991 9706 13736 -1696 2274 -1698 C
ATOM 1123 CG LEU A 166 49.736 -5.980 212.758 1.00 94.43 C
ANISOU 1123 CG LEU A 166 10060 10842 14976 -1871 2472 -2019 C
ATOM 1124 CD1 LEU A 166 50.831 -6.128 211.713 1.00102.97 C
ANISOU 1124 CD1 LEU A 166 11178 11804 16141 -1989 2782 -2200 C
ATOM 1125 CD2 LEU A 166 49.021 -4.654 212.602 1.00 96.19 C
ANISOU 1125 CD2 LEU A 166 10621 10872 15057 -1988 2587 -1958 C
ATOM 1126 N GLY A 167 46.408 -9.200 213.256 1.00 78.32 N
ANISOU 1126 N GLY A 167 8140 8954 12665 -1333 1767 -1105 N
ATOM 1127 CA GLY A 167 45.188 -9.877 212.860 1.00 77.34 C
ANISOU 1127 CA GLY A 167 8255 8733 12398 -1262 1682 -800 C
ATOM 1128 C GLY A 167 44.087 -9.732 213.884 1.00 74.43 C
ANISOU 1128 C GLY A 167 7825 8473 11982 -1162 1420 -684 C
ATOM 1129 O GLY A 167 42.909 -9.654 213.524 1.00 76.64 O
ANISOU 1129 O GLY A 167 8415 8635 12071 -1124 1341 -458 O
ATOM 1130 N ILE A 168 44.453 -9.673 215.163 1.00 72.83 N
ANISOU 1130 N ILE A 168 7281 8522 11869 -1061 1233 -840 N
ATOM 1131 CA ILE A 168 43.472 -9.420 216.209 1.00 72.39 C
ANISOU 1131 CA ILE A 168 7236 8579 11690 -929 966 -747 C
ATOM 1132 C ILE A 168 42.814 -8.068 215.989 1.00 66.99 C
ANISOU 1132 C ILE A 168 6784 7707 10961 -1068 1049 -721 C
ATOM 1133 O ILE A 168 41.584 -7.942 216.031 1.00 60.42 O
ANISOU 1133 O ILE A 168 6171 6823 9961 -983 920 -524 O
ATOM 1134 CB ILE A 168 44.139 -9.490 217.594 1.00 72.41 C
ANISOU 1134 CB ILE A 168 6859 8860 11793 -813 773 -952 C
ATOM 1135 CG1 ILE A 168 44.501 -10.935 217.953 1.00 68.33 C
ANISOU 1135 CG1 ILE A 168 6195 8525 11243 -582 621 -922 C
ATOM 1136 CG2 ILE A 168 43.235 -8.863 218.654 1.00 71.43 C
ANISOU 1136 CG2 ILE A 168 6770 8801 11571 -748 569 -906 C
ATOM 1137 CD1 ILE A 168 45.227 -11.069 219.276 1.00 68.77 C
ANISOU 1137 CD1 ILE A 168 6008 8839 11282 -407 390 -1098 C
ATOM 1138 N TRP A 169 43.623 -7.036 215.744 1.00 65.58 N
ANISOU 1138 N TRP A 169 6592 7426 10900 -1263 1268 -927 N
ATOM 1139 CA TRP A 169 43.041 -5.720 215.510 1.00 62.40 C
ANISOU 1139 CA TRP A 169 6468 6809 10432 -1383 1377 -905 C
ATOM 1140 C TRP A 169 42.201 -5.702 214.242 1.00 70.36 C
ANISOU 1140 C TRP A 169 7911 7536 11288 -1403 1485 -673 C
ATOM 1141 O TRP A 169 41.142 -5.065 214.202 1.00 68.25 O
ANISOU 1141 O TRP A 169 7903 7155 10874 -1339 1406 -533 O
ATOM 1142 CB TRP A 169 44.135 -4.661 215.445 1.00 57.53 C
ANISOU 1142 CB TRP A 169 5843 6149 9867 -1544 1592 -1164 C
ATOM 1143 CG TRP A 169 44.587 -4.235 216.790 1.00 57.38 C
ANISOU 1143 CG TRP A 169 5513 6356 9932 -1526 1450 -1366 C
ATOM 1144 CD1 TRP A 169 45.649 -4.724 217.486 1.00 61.65 C
ANISOU 1144 CD1 TRP A 169 5706 7152 10567 -1465 1347 -1564 C
ATOM 1145 CD2 TRP A 169 43.979 -3.240 217.624 1.00 65.47 C
ANISOU 1145 CD2 TRP A 169 6576 7368 10930 -1550 1376 -1387 C
ATOM 1146 NE1 TRP A 169 45.751 -4.089 218.700 1.00 69.70 N
ANISOU 1146 NE1 TRP A 169 6565 8323 11597 -1450 1203 -1702 N
ATOM 1147 CE2 TRP A 169 44.737 -3.173 218.810 1.00 63.85 C
ANISOU 1147 CE2 TRP A 169 6048 7422 10791 -1513 1231 -1599 C
ATOM 1148 CE3 TRP A 169 42.874 -2.394 217.479 1.00 60.21 C
ANISOU 1148 CE3 TRP A 169 6212 6483 10182 -1586 1416 -1249 C
ATOM 1149 CZ2 TRP A 169 44.425 -2.297 219.847 1.00 57.40 C
ANISOU 1149 CZ2 TRP A 169 5197 6654 9957 -1532 1140 -1676 C
ATOM 1150 CZ3 TRP A 169 42.568 -1.526 218.507 1.00 64.43 C
ANISOU 1150 CZ3 TRP A 169 6695 7059 10726 -1604 1339 -1333 C
ATOM 1151 CH2 TRP A 169 43.340 -1.484 219.677 1.00 62.52 C
ANISOU 1151 CH2 TRP A 169 6125 7083 10547 -1587 1208 -1544 C
ATOM 1152 N ALA A 170 42.630 -6.422 213.207 1.00 70.67 N
ANISOU 1152 N ALA A 170 8070 7505 11275 -1413 1607 -620 N
ATOM 1153 CA ALA A 170 41.855 -6.437 211.972 1.00 58.61 C
ANISOU 1153 CA ALA A 170 6986 5747 9535 -1392 1660 -404 C
ATOM 1154 C ALA A 170 40.485 -7.065 212.201 1.00 59.35 C
ANISOU 1154 C ALA A 170 7139 5886 9524 -1234 1404 -164 C
ATOM 1155 O ALA A 170 39.449 -6.492 211.831 1.00 61.05 O
ANISOU 1155 O ALA A 170 7652 5968 9577 -1170 1332 -25 O
ATOM 1156 CB ALA A 170 42.624 -7.183 210.881 1.00 60.22 C
ANISOU 1156 CB ALA A 170 7283 5906 9690 -1420 1817 -407 C
ATOM 1157 N VAL A 171 40.460 -8.230 212.855 1.00 59.67 N
ANISOU 1157 N VAL A 171 6911 6180 9581 -1104 1217 -127 N
ATOM 1158 CA VAL A 171 39.195 -8.904 213.122 1.00 59.26 C
ANISOU 1158 CA VAL A 171 6912 6246 9359 -929 958 71 C
ATOM 1159 C VAL A 171 38.306 -8.034 213.999 1.00 63.08 C
ANISOU 1159 C VAL A 171 7370 6797 9801 -843 787 76 C
ATOM 1160 O VAL A 171 37.104 -7.888 213.739 1.00 64.32 O
ANISOU 1160 O VAL A 171 7713 6918 9809 -753 662 221 O
ATOM 1161 CB VAL A 171 39.448 -10.278 213.774 1.00 57.41 C
ANISOU 1161 CB VAL A 171 6431 6243 9139 -819 834 81 C
ATOM 1162 CG1 VAL A 171 38.135 -11.008 214.002 1.00 52.42 C
ANISOU 1162 CG1 VAL A 171 5880 5711 8325 -687 621 262 C
ATOM 1163 CG2 VAL A 171 40.390 -11.112 212.919 1.00 68.65 C
ANISOU 1163 CG2 VAL A 171 7875 7594 10616 -886 1021 65 C
ATOM 1164 N SER A 172 38.880 -7.431 215.042 1.00 60.40 N
ANISOU 1164 N SER A 172 6793 6563 9593 -865 778 -97 N
ATOM 1165 CA SER A 172 38.070 -6.655 215.973 1.00 59.39 C
ANISOU 1165 CA SER A 172 6636 6501 9427 -781 627 -97 C
ATOM 1166 C SER A 172 37.477 -5.431 215.295 1.00 61.15 C
ANISOU 1166 C SER A 172 7180 6484 9571 -812 717 -48 C
ATOM 1167 O SER A 172 36.288 -5.136 215.462 1.00 55.77 O
ANISOU 1167 O SER A 172 6604 5813 8775 -678 565 63 O
ATOM 1168 CB SER A 172 38.908 -6.250 217.187 1.00 60.40 C
ANISOU 1168 CB SER A 172 6470 6777 9704 -818 610 -309 C
ATOM 1169 OG SER A 172 39.254 -7.389 217.954 1.00 61.17 O
ANISOU 1169 OG SER A 172 6312 7106 9826 -714 463 -335 O
ATOM 1170 N LEU A 173 38.281 -4.709 214.509 1.00 58.52 N
ANISOU 1170 N LEU A 173 7025 5921 9289 -980 977 -141 N
ATOM 1171 CA LEU A 173 37.744 -3.551 213.811 1.00 57.20 C
ANISOU 1171 CA LEU A 173 7248 5479 9005 -987 1081 -87 C
ATOM 1172 C LEU A 173 36.662 -3.955 212.828 1.00 60.10 C
ANISOU 1172 C LEU A 173 7903 5757 9177 -845 964 133 C
ATOM 1173 O LEU A 173 35.694 -3.211 212.633 1.00 65.04 O
ANISOU 1173 O LEU A 173 8770 6276 9666 -712 877 221 O
ATOM 1174 CB LEU A 173 38.855 -2.800 213.082 1.00 57.50 C
ANISOU 1174 CB LEU A 173 7481 5254 9114 -1222 1431 -238 C
ATOM 1175 CG LEU A 173 39.900 -2.143 213.975 1.00 58.09 C
ANISOU 1175 CG LEU A 173 7297 5397 9379 -1397 1572 -502 C
ATOM 1176 CD1 LEU A 173 41.139 -1.809 213.162 1.00 61.92 C
ANISOU 1176 CD1 LEU A 173 7880 5786 9862 -1575 1867 -661 C
ATOM 1177 CD2 LEU A 173 39.328 -0.890 214.613 1.00 58.07 C
ANISOU 1177 CD2 LEU A 173 7430 5318 9316 -1358 1548 -529 C
ATOM 1178 N ALA A 174 36.788 -5.134 212.212 1.00 58.18 N
ANISOU 1178 N ALA A 174 7634 5563 8909 -857 948 216 N
ATOM 1179 CA ALA A 174 35.772 -5.534 211.245 1.00 53.18 C
ANISOU 1179 CA ALA A 174 7272 4854 8081 -742 828 403 C
ATOM 1180 C ALA A 174 34.461 -5.912 211.930 1.00 57.99 C
ANISOU 1180 C ALA A 174 7716 5703 8617 -548 522 494 C
ATOM 1181 O ALA A 174 33.399 -5.388 211.580 1.00 65.42 O
ANISOU 1181 O ALA A 174 8851 6587 9420 -404 389 577 O
ATOM 1182 CB ALA A 174 36.289 -6.691 210.388 1.00 57.52 C
ANISOU 1182 CB ALA A 174 7863 5375 8616 -833 921 457 C
ATOM 1183 N ILE A 175 34.512 -6.796 212.933 1.00 51.04 N
ANISOU 1183 N ILE A 175 6485 5087 7821 -534 413 462 N
ATOM 1184 CA ILE A 175 33.280 -7.408 213.427 1.00 58.90 C
ANISOU 1184 CA ILE A 175 7350 6293 8734 -396 174 540 C
ATOM 1185 C ILE A 175 32.436 -6.479 214.285 1.00 61.61 C
ANISOU 1185 C ILE A 175 7621 6705 9081 -270 46 506 C
ATOM 1186 O ILE A 175 31.279 -6.810 214.577 1.00 50.10 O
ANISOU 1186 O ILE A 175 6078 5402 7557 -155 -133 552 O
ATOM 1187 CB ILE A 175 33.565 -8.695 214.226 1.00 61.71 C
ANISOU 1187 CB ILE A 175 7434 6872 9141 -418 126 520 C
ATOM 1188 CG1 ILE A 175 34.340 -8.382 215.503 1.00 52.40 C
ANISOU 1188 CG1 ILE A 175 6008 5795 8106 -433 149 380 C
ATOM 1189 CG2 ILE A 175 34.319 -9.695 213.362 1.00 56.22 C
ANISOU 1189 CG2 ILE A 175 6818 6111 8431 -515 251 562 C
ATOM 1190 CD1 ILE A 175 34.598 -9.614 216.357 1.00 48.37 C
ANISOU 1190 CD1 ILE A 175 5285 5484 7607 -405 82 361 C
ATOM 1191 N MET A 176 32.977 -5.347 214.724 1.00 55.26 N
ANISOU 1191 N MET A 176 6842 5795 8358 -301 151 409 N
ATOM 1192 CA MET A 176 32.205 -4.382 215.492 1.00 59.00 C
ANISOU 1192 CA MET A 176 7290 6300 8827 -178 58 379 C
ATOM 1193 C MET A 176 31.597 -3.286 214.624 1.00 59.35 C
ANISOU 1193 C MET A 176 7680 6119 8751 -64 68 437 C
ATOM 1194 O MET A 176 31.012 -2.338 215.164 1.00 57.90 O
ANISOU 1194 O MET A 176 7527 5918 8556 57 18 411 O
ATOM 1195 CB MET A 176 33.072 -3.762 216.593 1.00 57.31 C
ANISOU 1195 CB MET A 176 6917 6107 8751 -270 157 230 C
ATOM 1196 CG MET A 176 33.514 -4.762 217.659 1.00 59.66 C
ANISOU 1196 CG MET A 176 6887 6646 9137 -309 88 166 C
ATOM 1197 SD MET A 176 32.128 -5.747 218.259 1.00 57.32 S
ANISOU 1197 SD MET A 176 6444 6581 8754 -164 -135 256 S
ATOM 1198 CE MET A 176 32.947 -6.854 219.410 1.00 52.73 C
ANISOU 1198 CE MET A 176 5604 6195 8236 -213 -161 176 C
ATOM 1199 N VAL A 177 31.743 -3.375 213.298 1.00 59.17 N
ANISOU 1199 N VAL A 177 7955 5906 8622 -86 136 515 N
ATOM 1200 CA VAL A 177 31.065 -2.422 212.419 1.00 61.89 C
ANISOU 1200 CA VAL A 177 8685 6029 8802 73 107 584 C
ATOM 1201 C VAL A 177 29.557 -2.454 212.614 1.00 64.13 C
ANISOU 1201 C VAL A 177 8874 6491 9002 326 -178 640 C
ATOM 1202 O VAL A 177 28.942 -1.382 212.632 1.00 65.46 O
ANISOU 1202 O VAL A 177 9220 6555 9097 514 -230 642 O
ATOM 1203 CB VAL A 177 31.496 -2.638 210.962 1.00 62.43 C
ANISOU 1203 CB VAL A 177 9117 5855 8747 2 225 657 C
ATOM 1204 CG1 VAL A 177 30.691 -1.719 210.049 1.00 59.92 C
ANISOU 1204 CG1 VAL A 177 9245 5310 8213 219 149 738 C
ATOM 1205 CG2 VAL A 177 32.986 -2.355 210.810 1.00 56.77 C
ANISOU 1205 CG2 VAL A 177 8498 4937 8134 -255 556 558 C
ATOM 1206 N PRO A 178 28.887 -3.611 212.703 1.00 55.92 N
ANISOU 1206 N PRO A 178 7580 5707 7961 348 -355 673 N
ATOM 1207 CA PRO A 178 27.426 -3.578 212.910 1.00 51.71 C
ANISOU 1207 CA PRO A 178 6914 5363 7371 571 -607 679 C
ATOM 1208 C PRO A 178 27.040 -2.808 214.159 1.00 54.65 C
ANISOU 1208 C PRO A 178 7099 5824 7841 666 -628 598 C
ATOM 1209 O PRO A 178 26.013 -2.102 214.168 1.00 64.14 O
ANISOU 1209 O PRO A 178 8336 7047 8986 903 -771 592 O
ATOM 1210 CB PRO A 178 27.058 -5.066 213.036 1.00 56.86 C
ANISOU 1210 CB PRO A 178 7284 6278 8043 475 -705 684 C
ATOM 1211 CG PRO A 178 28.176 -5.804 212.362 1.00 50.07 C
ANISOU 1211 CG PRO A 178 6553 5296 7174 271 -543 732 C
ATOM 1212 CD PRO A 178 29.406 -4.984 212.595 1.00 46.59 C
ANISOU 1212 CD PRO A 178 6235 4645 6821 170 -317 690 C
ATOM 1213 N GLN A 179 27.878 -2.882 215.194 1.00 55.46 N
ANISOU 1213 N GLN A 179 7022 5968 8083 501 -488 528 N
ATOM 1214 CA GLN A 179 27.643 -2.112 216.404 1.00 55.79 C
ANISOU 1214 CA GLN A 179 6927 6061 8208 563 -479 448 C
ATOM 1215 C GLN A 179 27.613 -0.626 216.097 1.00 62.41 C
ANISOU 1215 C GLN A 179 8086 6646 8981 696 -410 449 C
ATOM 1216 O GLN A 179 26.730 0.099 216.569 1.00 66.56 O
ANISOU 1216 O GLN A 179 8594 7203 9493 893 -497 427 O
ATOM 1217 CB GLN A 179 28.737 -2.413 217.425 1.00 57.03 C
ANISOU 1217 CB GLN A 179 6899 6273 8498 356 -345 365 C
ATOM 1218 CG GLN A 179 28.483 -1.782 218.761 1.00 51.61 C
ANISOU 1218 CG GLN A 179 6064 5661 7886 399 -347 278 C
ATOM 1219 CD GLN A 179 27.195 -2.289 219.350 1.00 56.17 C
ANISOU 1219 CD GLN A 179 6417 6465 8460 525 -508 274 C
ATOM 1220 OE1 GLN A 179 27.007 -3.502 219.482 1.00 55.48 O
ANISOU 1220 OE1 GLN A 179 6151 6553 8376 457 -566 282 O
ATOM 1221 NE2 GLN A 179 26.282 -1.374 219.679 1.00 56.56 N
ANISOU 1221 NE2 GLN A 179 6486 6504 8500 708 -562 250 N
ATOM 1222 N ALA A 180 28.577 -0.151 215.303 1.00 58.76 N
ANISOU 1222 N ALA A 180 7944 5913 8470 589 -228 466 N
ATOM 1223 CA ALA A 180 28.552 1.244 214.880 1.00 61.76 C
ANISOU 1223 CA ALA A 180 8725 5999 8743 710 -127 473 C
ATOM 1224 C ALA A 180 27.350 1.547 213.996 1.00 67.63 C
ANISOU 1224 C ALA A 180 9697 6692 9307 1026 -330 565 C
ATOM 1225 O ALA A 180 26.777 2.640 214.078 1.00 68.31 O
ANISOU 1225 O ALA A 180 9993 6650 9310 1252 -354 565 O
ATOM 1226 CB ALA A 180 29.845 1.593 214.144 1.00 55.57 C
ANISOU 1226 CB ALA A 180 8260 4918 7934 491 150 452 C
ATOM 1227 N ALA A 181 26.936 0.590 213.163 1.00 66.39 N
ANISOU 1227 N ALA A 181 9503 6643 9081 1061 -489 635 N
ATOM 1228 CA ALA A 181 25.852 0.863 212.224 1.00 61.49 C
ANISOU 1228 CA ALA A 181 9106 5984 8272 1370 -712 704 C
ATOM 1229 C ALA A 181 24.532 1.091 212.946 1.00 59.59 C
ANISOU 1229 C ALA A 181 8582 5990 8070 1638 -943 654 C
ATOM 1230 O ALA A 181 23.731 1.934 212.527 1.00 72.40 O
ANISOU 1230 O ALA A 181 10430 7520 9556 1962 -1081 672 O
ATOM 1231 CB ALA A 181 25.716 -0.282 211.220 1.00 49.79 C
ANISOU 1231 CB ALA A 181 7619 4587 6710 1316 -834 768 C
ATOM 1232 N VAL A 182 24.286 0.362 214.041 1.00 59.79 N
ANISOU 1232 N VAL A 182 8130 6317 8272 1521 -977 579 N
ATOM 1233 CA VAL A 182 22.999 0.521 214.722 1.00 57.78 C
ANISOU 1233 CA VAL A 182 7583 6303 8069 1750 -1165 507 C
ATOM 1234 C VAL A 182 22.935 1.723 215.652 1.00 61.70 C
ANISOU 1234 C VAL A 182 8131 6696 8617 1867 -1065 458 C
ATOM 1235 O VAL A 182 21.838 2.094 216.085 1.00 62.99 O
ANISOU 1235 O VAL A 182 8126 7004 8804 2114 -1207 398 O
ATOM 1236 CB VAL A 182 22.617 -0.732 215.531 1.00 57.88 C
ANISOU 1236 CB VAL A 182 7107 6659 8226 1581 -1219 432 C
ATOM 1237 CG1 VAL A 182 22.455 -1.929 214.606 1.00 57.22 C
ANISOU 1237 CG1 VAL A 182 6969 6697 8074 1490 -1333 467 C
ATOM 1238 CG2 VAL A 182 23.661 -1.015 216.594 1.00 51.91 C
ANISOU 1238 CG2 VAL A 182 6226 5895 7604 1297 -1002 403 C
ATOM 1239 N MET A 183 24.064 2.344 215.982 1.00 63.04 N
ANISOU 1239 N MET A 183 8515 6628 8808 1690 -817 462 N
ATOM 1240 CA MET A 183 24.031 3.486 216.886 1.00 59.74 C
ANISOU 1240 CA MET A 183 8169 6102 8427 1773 -703 408 C
ATOM 1241 C MET A 183 23.365 4.680 216.221 1.00 68.04 C
ANISOU 1241 C MET A 183 9611 6935 9305 2134 -768 451 C
ATOM 1242 O MET A 183 23.637 4.994 215.060 1.00 69.62 O
ANISOU 1242 O MET A 183 10229 6891 9332 2210 -754 530 O
ATOM 1243 CB MET A 183 25.443 3.866 217.328 1.00 55.84 C
ANISOU 1243 CB MET A 183 7816 5411 7990 1471 -418 374 C
ATOM 1244 CG MET A 183 26.219 2.742 217.972 1.00 53.60 C
ANISOU 1244 CG MET A 183 7185 5323 7857 1156 -366 325 C
ATOM 1245 SD MET A 183 25.273 1.958 219.287 1.00 59.94 S
ANISOU 1245 SD MET A 183 7485 6496 8793 1190 -518 257 S
ATOM 1246 CE MET A 183 25.136 3.296 220.466 1.00 62.91 C
ANISOU 1246 CE MET A 183 7927 6767 9209 1270 -402 177 C
ATOM 1247 N GLU A 184 22.511 5.372 216.973 1.00 67.54 N
ANISOU 1247 N GLU A 184 9449 6937 9276 2369 -825 397 N
ATOM 1248 CA GLU A 184 21.892 6.588 216.475 1.00 71.28 C
ANISOU 1248 CA GLU A 184 10313 7190 9578 2755 -878 432 C
ATOM 1249 C GLU A 184 21.712 7.545 217.643 1.00 69.38 C
ANISOU 1249 C GLU A 184 10057 6895 9409 2824 -743 364 C
ATOM 1250 O GLU A 184 21.548 7.125 218.794 1.00 67.40 O
ANISOU 1250 O GLU A 184 9388 6878 9341 2683 -723 281 O
ATOM 1251 CB GLU A 184 20.544 6.314 215.791 1.00 79.85 C
ANISOU 1251 CB GLU A 184 11269 8481 10591 3139 -1220 434 C
ATOM 1252 CG GLU A 184 20.585 5.222 214.728 1.00 95.82 C
ANISOU 1252 CG GLU A 184 13241 10614 12552 3053 -1381 482 C
ATOM 1253 CD GLU A 184 21.313 5.642 213.461 1.00104.06 C
ANISOU 1253 CD GLU A 184 14887 11286 13364 3069 -1302 597 C
ATOM 1254 OE1 GLU A 184 21.440 6.862 213.215 1.00106.61 O
ANISOU 1254 OE1 GLU A 184 15656 11322 13530 3201 -1170 625 O
ATOM 1255 OE2 GLU A 184 21.756 4.745 212.711 1.00104.95 O
ANISOU 1255 OE2 GLU A 184 15010 11421 13444 2874 -1324 645 O
ATOM 1256 N CYS A 185 21.755 8.839 217.329 1.00 73.67 N
ANISOU 1256 N CYS A 185 11107 7101 9784 3041 -633 401 N
ATOM 1257 CA CYS A 185 21.622 9.915 218.306 1.00 78.19 C
ANISOU 1257 CA CYS A 185 11782 7548 10378 3128 -473 348 C
ATOM 1258 C CYS A 185 20.378 10.713 217.944 1.00 80.99 C
ANISOU 1258 C CYS A 185 12257 7918 10598 3575 -643 360 C
ATOM 1259 O CYS A 185 20.388 11.480 216.975 1.00 89.72 O
ANISOU 1259 O CYS A 185 13808 8814 11466 3686 -618 422 O
ATOM 1260 CB CYS A 185 22.874 10.794 218.316 1.00 76.70 C
ANISOU 1260 CB CYS A 185 12076 6967 10100 2874 -125 353 C
ATOM 1261 SG CYS A 185 22.849 12.171 219.475 1.00 85.93 S
ANISOU 1261 SG CYS A 185 13453 7931 11265 2926 119 282 S
ATOM 1262 N SER A 186 19.310 10.527 218.712 1.00 82.58 N
ANISOU 1262 N SER A 186 12010 8425 10943 3739 -791 280 N
ATOM 1263 CA SER A 186 18.008 11.091 218.386 1.00 97.26 C
ANISOU 1263 CA SER A 186 13818 10423 12715 4073 -970 257 C
ATOM 1264 C SER A 186 17.557 12.073 219.459 1.00101.78 C
ANISOU 1264 C SER A 186 14385 10945 13341 4201 -836 196 C
ATOM 1265 O SER A 186 17.825 11.888 220.649 1.00 98.07 O
ANISOU 1265 O SER A 186 13693 10516 13055 4046 -698 132 O
ATOM 1266 CB SER A 186 16.960 9.983 218.211 1.00101.27 C
ANISOU 1266 CB SER A 186 13771 11364 13345 4134 -1254 187 C
ATOM 1267 OG SER A 186 17.013 9.056 219.282 1.00102.43 O
ANISOU 1267 OG SER A 186 13435 11744 13738 3919 -1219 104 O
ATOM 1268 N SER A 187 16.866 13.121 219.020 1.00109.16 N
ANISOU 1268 N SER A 187 15590 11787 14100 4496 -880 211 N
ATOM 1269 CA SER A 187 16.355 14.129 219.936 1.00110.81 C
ANISOU 1269 CA SER A 187 15834 11935 14334 4652 -759 160 C
ATOM 1270 C SER A 187 15.206 13.572 220.770 1.00112.14 C
ANISOU 1270 C SER A 187 15381 12480 14745 4743 -895 40 C
ATOM 1271 O SER A 187 14.463 12.688 220.336 1.00115.49 O
ANISOU 1271 O SER A 187 15416 13221 15244 4790 -1131 -8 O
ATOM 1272 CB SER A 187 15.886 15.362 219.162 1.00117.42 C
ANISOU 1272 CB SER A 187 17139 12582 14892 4972 -787 207 C
ATOM 1273 OG SER A 187 16.904 15.848 218.305 1.00123.75 O
ANISOU 1273 OG SER A 187 18533 13043 15444 4860 -638 305 O
ATOM 1274 N VAL A 188 15.070 14.099 221.983 1.00114.38 N
ANISOU 1274 N VAL A 188 15590 12722 15146 4736 -717 -22 N
ATOM 1275 CA VAL A 188 13.972 13.724 222.866 1.00118.26 C
ANISOU 1275 CA VAL A 188 15542 13529 15862 4806 -779 -151 C
ATOM 1276 C VAL A 188 13.229 14.971 223.336 1.00115.52 C
ANISOU 1276 C VAL A 188 15343 13076 15473 5083 -698 -184 C
ATOM 1277 O VAL A 188 13.838 15.917 223.837 1.00109.37 O
ANISOU 1277 O VAL A 188 14957 11992 14608 5053 -465 -146 O
ATOM 1278 CB VAL A 188 14.472 12.905 224.070 1.00116.39 C
ANISOU 1278 CB VAL A 188 14982 13394 15848 4493 -630 -223 C
ATOM 1279 CG1 VAL A 188 13.332 12.653 225.047 1.00119.61 C
ANISOU 1279 CG1 VAL A 188 14900 14081 16464 4545 -628 -366 C
ATOM 1280 CG2 VAL A 188 15.076 11.592 223.604 1.00113.19 C
ANISOU 1280 CG2 VAL A 188 14383 13137 15488 4246 -736 -202 C
ATOM 1281 N PHE A 199 16.703 17.120 224.578 1.00107.21 N
ANISOU 1281 N PHE A 199 15674 10948 14113 4498 157 -33 N
ATOM 1282 CA PHE A 199 18.055 16.583 224.680 1.00106.42 C
ANISOU 1282 CA PHE A 199 15680 10714 14039 4120 306 -21 C
ATOM 1283 C PHE A 199 18.219 15.336 223.818 1.00109.80 C
ANISOU 1283 C PHE A 199 15859 11339 14521 4057 84 14 C
ATOM 1284 O PHE A 199 17.243 14.650 223.509 1.00111.17 O
ANISOU 1284 O PHE A 199 15632 11828 14781 4238 -176 -8 O
ATOM 1285 CB PHE A 199 18.399 16.264 226.136 1.00107.66 C
ANISOU 1285 CB PHE A 199 15606 10909 14392 3893 481 -121 C
ATOM 1286 CG PHE A 199 17.496 15.241 226.768 1.00106.14 C
ANISOU 1286 CG PHE A 199 14799 11098 14430 3974 309 -208 C
ATOM 1287 CD1 PHE A 199 17.887 13.917 226.862 1.00103.39 C
ANISOU 1287 CD1 PHE A 199 14073 10993 14219 3703 213 -234 C
ATOM 1288 CD2 PHE A 199 16.258 15.605 227.272 1.00107.62 C
ANISOU 1288 CD2 PHE A 199 14757 11439 14694 4219 258 -274 C
ATOM 1289 CE1 PHE A 199 17.061 12.975 227.444 1.00104.30 C
ANISOU 1289 CE1 PHE A 199 13638 11468 14524 3697 88 -329 C
ATOM 1290 CE2 PHE A 199 15.427 14.666 227.854 1.00104.77 C
ANISOU 1290 CE2 PHE A 199 13831 11429 14550 4232 146 -380 C
ATOM 1291 CZ PHE A 199 15.830 13.350 227.939 1.00102.70 C
ANISOU 1291 CZ PHE A 199 13242 11376 14403 4012 66 -415 C
ATOM 1292 N SER A 200 19.456 15.057 223.418 1.00102.21 N
ANISOU 1292 N SER A 200 15136 10191 13507 3773 205 56 N
ATOM 1293 CA SER A 200 19.748 13.914 222.568 1.00 98.12 C
ANISOU 1293 CA SER A 200 14447 9814 13020 3690 26 98 C
ATOM 1294 C SER A 200 20.027 12.664 223.396 1.00 93.22 C
ANISOU 1294 C SER A 200 13288 9497 12634 3368 -9 26 C
ATOM 1295 O SER A 200 20.517 12.731 224.527 1.00 88.99 O
ANISOU 1295 O SER A 200 12645 8969 12199 3083 170 -45 O
ATOM 1296 CB SER A 200 20.935 14.209 221.648 1.00 94.38 C
ANISOU 1296 CB SER A 200 14464 9023 12373 3471 189 169 C
ATOM 1297 OG SER A 200 20.504 14.861 220.466 1.00101.08 O
ANISOU 1297 OG SER A 200 15651 9775 12980 3696 99 249 O
ATOM 1298 N VAL A 201 19.712 11.515 222.807 1.00 85.00 N
ANISOU 1298 N VAL A 201 11909 8730 11656 3366 -244 42 N
ATOM 1299 CA VAL A 201 20.002 10.212 223.391 1.00 78.46 C
ANISOU 1299 CA VAL A 201 10600 8203 11007 3015 -284 -12 C
ATOM 1300 C VAL A 201 20.697 9.371 222.331 1.00 73.95 C
ANISOU 1300 C VAL A 201 10063 7648 10387 2836 -365 61 C
ATOM 1301 O VAL A 201 20.230 9.298 221.188 1.00 86.04 O
ANISOU 1301 O VAL A 201 11714 9169 11809 3085 -542 125 O
ATOM 1302 CB VAL A 201 18.726 9.509 223.894 1.00 78.57 C
ANISOU 1302 CB VAL A 201 10102 8579 11171 3176 -465 -100 C
ATOM 1303 CG1 VAL A 201 18.968 8.015 224.049 1.00 87.34 C
ANISOU 1303 CG1 VAL A 201 10810 9973 12402 2859 -539 -130 C
ATOM 1304 CG2 VAL A 201 18.267 10.119 225.212 1.00 75.12 C
ANISOU 1304 CG2 VAL A 201 9572 8145 10826 3220 -321 -194 C
ATOM 1305 N CYS A 202 21.819 8.761 222.703 1.00 65.77 N
ANISOU 1305 N CYS A 202 8938 6630 9422 2423 -241 44 N
ATOM 1306 CA CYS A 202 22.562 7.862 221.831 1.00 60.35 C
ANISOU 1306 CA CYS A 202 8241 5972 8716 2216 -286 100 C
ATOM 1307 C CYS A 202 22.257 6.429 222.249 1.00 70.36 C
ANISOU 1307 C CYS A 202 9011 7598 10126 2073 -427 61 C
ATOM 1308 O CYS A 202 22.515 6.047 223.397 1.00 69.19 O
ANISOU 1308 O CYS A 202 8625 7574 10092 1865 -351 -13 O
ATOM 1309 CB CYS A 202 24.064 8.144 221.911 1.00 62.47 C
ANISOU 1309 CB CYS A 202 8742 6022 8972 1867 -44 84 C
ATOM 1310 SG CYS A 202 25.124 7.036 220.930 1.00 67.96 S
ANISOU 1310 SG CYS A 202 9408 6744 9670 1584 -51 130 S
ATOM 1311 N ASP A 203 21.708 5.644 221.326 1.00 72.01 N
ANISOU 1311 N ASP A 203 9099 7957 10305 2182 -624 104 N
ATOM 1312 CA ASP A 203 21.378 4.258 221.633 1.00 74.63 C
ANISOU 1312 CA ASP A 203 9004 8607 10746 2036 -732 61 C
ATOM 1313 C ASP A 203 21.268 3.472 220.334 1.00 65.28 C
ANISOU 1313 C ASP A 203 7832 7488 9485 2065 -894 129 C
ATOM 1314 O ASP A 203 21.236 4.038 219.237 1.00 60.21 O
ANISOU 1314 O ASP A 203 7508 6666 8702 2255 -956 204 O
ATOM 1315 CB ASP A 203 20.085 4.157 222.456 1.00 81.05 C
ANISOU 1315 CB ASP A 203 9478 9657 11659 2199 -813 -45 C
ATOM 1316 CG ASP A 203 20.013 2.877 223.281 1.00 89.79 C
ANISOU 1316 CG ASP A 203 10211 11021 12884 1943 -797 -120 C
ATOM 1317 OD1 ASP A 203 20.913 2.022 223.138 1.00 80.09 O
ANISOU 1317 OD1 ASP A 203 8982 9802 11647 1683 -761 -77 O
ATOM 1318 OD2 ASP A 203 19.063 2.730 224.080 1.00 94.49 O
ANISOU 1318 OD2 ASP A 203 10537 11795 13572 2006 -802 -230 O
ATOM 1319 N GLU A 204 21.240 2.152 220.475 1.00 56.66 N
ANISOU 1319 N GLU A 204 6434 6631 8465 1868 -946 103 N
ATOM 1320 CA GLU A 204 21.066 1.286 219.322 1.00 61.36 C
ANISOU 1320 CA GLU A 204 7010 7315 8989 1868 -1095 154 C
ATOM 1321 C GLU A 204 19.673 1.471 218.739 1.00 61.03 C
ANISOU 1321 C GLU A 204 6866 7419 8905 2200 -1327 111 C
ATOM 1322 O GLU A 204 18.686 1.565 219.474 1.00 60.17 O
ANISOU 1322 O GLU A 204 6472 7499 8892 2325 -1376 -4 O
ATOM 1323 CB GLU A 204 21.278 -0.173 219.723 1.00 63.26 C
ANISOU 1323 CB GLU A 204 6958 7771 9307 1584 -1074 122 C
ATOM 1324 CG GLU A 204 22.642 -0.458 220.321 1.00 52.57 C
ANISOU 1324 CG GLU A 204 5666 6314 7995 1296 -887 146 C
ATOM 1325 CD GLU A 204 22.757 -1.876 220.839 1.00 56.03 C
ANISOU 1325 CD GLU A 204 5849 6954 8484 1072 -871 111 C
ATOM 1326 OE1 GLU A 204 21.757 -2.622 220.745 1.00 53.72 O
ANISOU 1326 OE1 GLU A 204 5342 6872 8199 1104 -973 60 O
ATOM 1327 OE2 GLU A 204 23.841 -2.247 221.343 1.00 55.07 O
ANISOU 1327 OE2 GLU A 204 5751 6782 8390 870 -753 119 O
ATOM 1328 N ARG A 205 19.592 1.519 217.413 1.00 67.43 N
ANISOU 1328 N ARG A 205 7907 8145 9570 2348 -1472 186 N
ATOM 1329 CA ARG A 205 18.320 1.582 216.705 1.00 68.06 C
ANISOU 1329 CA ARG A 205 7884 8390 9587 2677 -1746 133 C
ATOM 1330 C ARG A 205 18.111 0.272 215.959 1.00 70.75 C
ANISOU 1330 C ARG A 205 8044 8936 9902 2530 -1885 122 C
ATOM 1331 O ARG A 205 18.971 -0.146 215.178 1.00 77.49 O
ANISOU 1331 O ARG A 205 9149 9638 10658 2364 -1836 233 O
ATOM 1332 CB ARG A 205 18.275 2.763 215.734 1.00 75.24 C
ANISOU 1332 CB ARG A 205 9265 9023 10300 3021 -1835 221 C
ATOM 1333 CG ARG A 205 16.960 2.880 214.970 1.00 93.32 C
ANISOU 1333 CG ARG A 205 11466 11509 12481 3236 -2044 165 C
ATOM 1334 CD ARG A 205 16.984 4.050 213.998 1.00110.18 C
ANISOU 1334 CD ARG A 205 14126 13354 14383 3514 -2086 255 C
ATOM 1335 NE ARG A 205 17.214 5.329 214.668 1.00124.54 N
ANISOU 1335 NE ARG A 205 16186 14936 16196 3648 -1916 274 N
ATOM 1336 CZ ARG A 205 16.249 6.109 215.147 1.00131.53 C
ANISOU 1336 CZ ARG A 205 16956 15915 17105 3873 -1951 194 C
ATOM 1337 NH1 ARG A 205 14.979 5.740 215.036 1.00137.80 N
ANISOU 1337 NH1 ARG A 205 17376 17037 17944 3986 -2148 77 N
ATOM 1338 NH2 ARG A 205 16.554 7.257 215.739 1.00129.31 N
ANISOU 1338 NH2 ARG A 205 16940 15389 16804 3974 -1776 220 N
ATOM 1339 N TRP A 206 16.970 -0.369 216.201 1.00 72.73 N
ANISOU 1339 N TRP A 206 7892 9522 10221 2508 -1976 -13 N
ATOM 1340 CA TRP A 206 16.665 -1.668 215.623 1.00 69.95 C
ANISOU 1340 CA TRP A 206 7345 9387 9845 2318 -2065 -53 C
ATOM 1341 C TRP A 206 15.324 -1.591 214.912 1.00 73.03 C
ANISOU 1341 C TRP A 206 7616 9975 10156 2488 -2251 -143 C
ATOM 1342 O TRP A 206 14.348 -1.089 215.476 1.00 80.56 O
ANISOU 1342 O TRP A 206 8368 11061 11181 2609 -2250 -254 O
ATOM 1343 CB TRP A 206 16.640 -2.755 216.702 1.00 59.70 C
ANISOU 1343 CB TRP A 206 5688 8295 8700 1993 -1907 -152 C
ATOM 1344 CG TRP A 206 17.970 -3.000 217.345 1.00 60.05 C
ANISOU 1344 CG TRP A 206 5851 8159 8804 1765 -1710 -66 C
ATOM 1345 CD1 TRP A 206 18.397 -2.535 218.556 1.00 62.23 C
ANISOU 1345 CD1 TRP A 206 6113 8353 9179 1696 -1523 -78 C
ATOM 1346 CD2 TRP A 206 19.045 -3.783 216.813 1.00 61.67 C
ANISOU 1346 CD2 TRP A 206 6252 8243 8936 1516 -1620 54 C
ATOM 1347 NE1 TRP A 206 19.676 -2.978 218.809 1.00 56.61 N
ANISOU 1347 NE1 TRP A 206 5556 7494 8459 1432 -1348 17 N
ATOM 1348 CE2 TRP A 206 20.097 -3.744 217.753 1.00 60.91 C
ANISOU 1348 CE2 TRP A 206 6222 8012 8907 1324 -1396 98 C
ATOM 1349 CE3 TRP A 206 19.223 -4.509 215.629 1.00 65.21 C
ANISOU 1349 CE3 TRP A 206 6828 8684 9266 1445 -1709 121 C
ATOM 1350 CZ2 TRP A 206 21.310 -4.402 217.544 1.00 58.44 C
ANISOU 1350 CZ2 TRP A 206 6065 7576 8562 1087 -1267 195 C
ATOM 1351 CZ3 TRP A 206 20.424 -5.161 215.426 1.00 61.45 C
ANISOU 1351 CZ3 TRP A 206 6532 8061 8755 1193 -1551 231 C
ATOM 1352 CH2 TRP A 206 21.451 -5.104 216.378 1.00 60.05 C
ANISOU 1352 CH2 TRP A 206 6385 7769 8663 1028 -1336 262 C
ATOM 1353 N ALA A 207 15.276 -2.094 213.679 1.00 74.97 N
ANISOU 1353 N ALA A 207 7989 10237 10260 2500 -2417 -106 N
ATOM 1354 CA ALA A 207 14.047 -2.045 212.896 1.00 78.28 C
ANISOU 1354 CA ALA A 207 8306 10840 10596 2671 -2626 -206 C
ATOM 1355 C ALA A 207 13.024 -3.090 213.324 1.00 81.45 C
ANISOU 1355 C ALA A 207 8233 11594 11119 2459 -2618 -393 C
ATOM 1356 O ALA A 207 11.864 -2.997 212.913 1.00 96.01 O
ANISOU 1356 O ALA A 207 9910 13625 12945 2600 -2777 -522 O
ATOM 1357 CB ALA A 207 14.363 -2.212 211.406 1.00 75.99 C
ANISOU 1357 CB ALA A 207 8356 10425 10091 2755 -2806 -108 C
ATOM 1358 N ASP A 208 13.417 -4.068 214.139 1.00 83.90 N
ANISOU 1358 N ASP A 208 8347 11985 11545 2128 -2429 -421 N
ATOM 1359 CA ASP A 208 12.513 -5.129 214.559 1.00 75.40 C
ANISOU 1359 CA ASP A 208 6893 11194 10562 1885 -2369 -599 C
ATOM 1360 C ASP A 208 12.974 -5.663 215.907 1.00 67.79 C
ANISOU 1360 C ASP A 208 5799 10227 9731 1608 -2093 -620 C
ATOM 1361 O ASP A 208 14.099 -5.413 216.347 1.00 70.16 O
ANISOU 1361 O ASP A 208 6283 10331 10044 1576 -1981 -494 O
ATOM 1362 CB ASP A 208 12.452 -6.257 213.526 1.00 78.92 C
ANISOU 1362 CB ASP A 208 7331 11750 10904 1719 -2484 -618 C
ATOM 1363 CG ASP A 208 13.736 -7.059 213.470 1.00 85.17 C
ANISOU 1363 CG ASP A 208 8295 12408 11658 1479 -2374 -488 C
ATOM 1364 OD1 ASP A 208 13.950 -7.898 214.370 1.00 87.87 O
ANISOU 1364 OD1 ASP A 208 8482 12811 12093 1192 -2163 -538 O
ATOM 1365 OD2 ASP A 208 14.538 -6.843 212.537 1.00 91.12 O
ANISOU 1365 OD2 ASP A 208 9366 12974 12280 1585 -2492 -341 O
ATOM 1366 N ASP A 209 12.078 -6.394 216.572 1.00 58.35 N
ANISOU 1366 N ASP A 209 4302 9241 8629 1413 -1980 -796 N
ATOM 1367 CA ASP A 209 12.371 -6.918 217.900 1.00 66.29 C
ANISOU 1367 CA ASP A 209 5218 10236 9734 1162 -1709 -837 C
ATOM 1368 C ASP A 209 13.273 -8.150 217.893 1.00 64.52 C
ANISOU 1368 C ASP A 209 5083 9969 9462 855 -1589 -775 C
ATOM 1369 O ASP A 209 13.866 -8.464 218.931 1.00 70.99 O
ANISOU 1369 O ASP A 209 5931 10712 10330 689 -1380 -760 O
ATOM 1370 CB ASP A 209 11.065 -7.247 218.626 1.00 79.03 C
ANISOU 1370 CB ASP A 209 6524 12054 11450 1067 -1608 -1064 C
ATOM 1371 CG ASP A 209 10.192 -6.026 218.831 1.00101.52 C
ANISOU 1371 CG ASP A 209 9260 14945 14367 1368 -1696 -1140 C
ATOM 1372 OD1 ASP A 209 10.572 -4.937 218.350 1.00108.68 O
ANISOU 1372 OD1 ASP A 209 10355 15715 15222 1656 -1840 -1011 O
ATOM 1373 OD2 ASP A 209 9.128 -6.153 219.474 1.00111.18 O
ANISOU 1373 OD2 ASP A 209 10224 16329 15690 1320 -1609 -1339 O
ATOM 1374 N LEU A 210 13.395 -8.857 216.767 1.00 58.83 N
ANISOU 1374 N LEU A 210 4421 9291 8639 783 -1716 -746 N
ATOM 1375 CA LEU A 210 14.163 -10.100 216.770 1.00 61.63 C
ANISOU 1375 CA LEU A 210 4851 9619 8947 483 -1588 -709 C
ATOM 1376 C LEU A 210 15.659 -9.849 216.611 1.00 58.46 C
ANISOU 1376 C LEU A 210 4704 8995 8511 524 -1590 -517 C
ATOM 1377 O LEU A 210 16.480 -10.519 217.260 1.00 62.33 O
ANISOU 1377 O LEU A 210 5248 9413 9022 320 -1410 -484 O
ATOM 1378 CB LEU A 210 13.655 -11.028 215.662 1.00 67.93 C
ANISOU 1378 CB LEU A 210 5603 10560 9650 361 -1708 -779 C
ATOM 1379 CG LEU A 210 14.316 -12.402 215.539 1.00 71.92 C
ANISOU 1379 CG LEU A 210 6192 11051 10083 38 -1572 -763 C
ATOM 1380 CD1 LEU A 210 14.190 -13.181 216.838 1.00 61.35 C
ANISOU 1380 CD1 LEU A 210 4776 9730 8804 -221 -1267 -866 C
ATOM 1381 CD2 LEU A 210 13.690 -13.178 214.389 1.00 64.62 C
ANISOU 1381 CD2 LEU A 210 5224 10273 9054 -65 -1709 -850 C
ATOM 1382 N ALA A 211 16.023 -8.903 215.743 1.00 57.79 N
ANISOU 1382 N ALA A 211 4800 8782 8374 790 -1788 -403 N
ATOM 1383 CA ALA A 211 17.435 -8.668 215.448 1.00 52.57 C
ANISOU 1383 CA ALA A 211 4471 7838 7664 792 -1742 -201 C
ATOM 1384 C ALA A 211 18.249 -8.342 216.684 1.00 47.28 C
ANISOU 1384 C ALA A 211 3853 7024 7087 723 -1522 -147 C
ATOM 1385 O ALA A 211 19.341 -8.914 216.842 1.00 58.89 O
ANISOU 1385 O ALA A 211 5500 8351 8526 533 -1361 -36 O
ATOM 1386 CB ALA A 211 17.568 -7.556 214.400 1.00 52.23 C
ANISOU 1386 CB ALA A 211 4690 7629 7528 1093 -1939 -91 C
ATOM 1387 N PRO A 212 17.840 -7.415 217.551 1.00 57.88 N
ANISOU 1387 N PRO A 212 5068 8387 8538 881 -1513 -220 N
ATOM 1388 CA PRO A 212 18.644 -7.165 218.757 1.00 50.18 C
ANISOU 1388 CA PRO A 212 4156 7277 7632 792 -1310 -179 C
ATOM 1389 C PRO A 212 18.810 -8.397 219.621 1.00 49.74 C
ANISOU 1389 C PRO A 212 4007 7302 7588 508 -1123 -235 C
ATOM 1390 O PRO A 212 19.890 -8.607 220.185 1.00 50.14 O
ANISOU 1390 O PRO A 212 4217 7208 7627 392 -984 -148 O
ATOM 1391 CB PRO A 212 17.858 -6.059 219.484 1.00 47.07 C
ANISOU 1391 CB PRO A 212 3607 6934 7343 1012 -1344 -283 C
ATOM 1392 CG PRO A 212 16.461 -6.169 218.959 1.00 46.66 C
ANISOU 1392 CG PRO A 212 3378 7099 7252 1093 -1457 -394 C
ATOM 1393 CD PRO A 212 16.598 -6.621 217.529 1.00 56.44 C
ANISOU 1393 CD PRO A 212 4723 8342 8379 1113 -1636 -330 C
ATOM 1394 N LYS A 213 17.794 -9.255 219.697 1.00 58.02 N
ANISOU 1394 N LYS A 213 4823 8576 8646 390 -1115 -391 N
ATOM 1395 CA LYS A 213 17.919 -10.462 220.507 1.00 56.70 C
ANISOU 1395 CA LYS A 213 4639 8449 8454 114 -905 -449 C
ATOM 1396 C LYS A 213 18.974 -11.393 219.930 1.00 55.85 C
ANISOU 1396 C LYS A 213 4782 8216 8223 -42 -848 -300 C
ATOM 1397 O LYS A 213 19.860 -11.874 220.650 1.00 58.10 O
ANISOU 1397 O LYS A 213 5220 8383 8472 -153 -694 -235 O
ATOM 1398 CB LYS A 213 16.571 -11.175 220.604 1.00 49.77 C
ANISOU 1398 CB LYS A 213 3545 7791 7574 -17 -854 -638 C
ATOM 1399 CG LYS A 213 15.478 -10.313 221.176 1.00 52.90 C
ANISOU 1399 CG LYS A 213 3780 8266 8055 127 -858 -751 C
ATOM 1400 CD LYS A 213 14.213 -11.111 221.423 1.00 52.40 C
ANISOU 1400 CD LYS A 213 3534 8379 7998 -43 -751 -953 C
ATOM 1401 CE LYS A 213 13.158 -10.246 222.086 1.00 56.10 C
ANISOU 1401 CE LYS A 213 3822 8923 8570 99 -735 -1085 C
ATOM 1402 NZ LYS A 213 12.052 -11.064 222.648 1.00 73.34 N
ANISOU 1402 NZ LYS A 213 5838 11250 10780 -108 -558 -1315 N
ATOM 1403 N ILE A 214 18.920 -11.627 218.618 1.00 52.81 N
ANISOU 1403 N ILE A 214 4456 7847 7763 -29 -981 -245 N
ATOM 1404 CA ILE A 214 19.920 -12.498 218.011 1.00 55.24 C
ANISOU 1404 CA ILE A 214 5009 8023 7956 -172 -911 -104 C
ATOM 1405 C ILE A 214 21.313 -11.882 218.126 1.00 54.33 C
ANISOU 1405 C ILE A 214 5113 7672 7856 -90 -871 60 C
ATOM 1406 O ILE A 214 22.283 -12.560 218.504 1.00 59.71 O
ANISOU 1406 O ILE A 214 5932 8255 8499 -206 -732 129 O
ATOM 1407 CB ILE A 214 19.544 -12.804 216.552 1.00 57.25 C
ANISOU 1407 CB ILE A 214 5306 8330 8117 -173 -1063 -84 C
ATOM 1408 CG1 ILE A 214 18.227 -13.582 216.505 1.00 57.89 C
ANISOU 1408 CG1 ILE A 214 5138 8672 8184 -311 -1080 -287 C
ATOM 1409 CG2 ILE A 214 20.657 -13.595 215.875 1.00 56.66 C
ANISOU 1409 CG2 ILE A 214 5514 8086 7930 -303 -973 75 C
ATOM 1410 CD1 ILE A 214 17.725 -13.835 215.102 1.00 58.78 C
ANISOU 1410 CD1 ILE A 214 5260 8873 8199 -302 -1269 -302 C
ATOM 1411 N TYR A 215 21.433 -10.581 217.846 1.00 52.08 N
ANISOU 1411 N TYR A 215 4864 7297 7626 114 -981 104 N
ATOM 1412 CA TYR A 215 22.754 -9.960 217.839 1.00 48.67 C
ANISOU 1412 CA TYR A 215 4637 6643 7212 154 -922 227 C
ATOM 1413 C TYR A 215 23.367 -9.945 219.224 1.00 46.83 C
ANISOU 1413 C TYR A 215 4365 6382 7046 102 -789 198 C
ATOM 1414 O TYR A 215 24.565 -10.195 219.374 1.00 54.25 O
ANISOU 1414 O TYR A 215 5428 7205 7980 34 -700 265 O
ATOM 1415 CB TYR A 215 22.688 -8.534 217.296 1.00 43.41 C
ANISOU 1415 CB TYR A 215 4066 5860 6568 369 -1032 263 C
ATOM 1416 CG TYR A 215 23.981 -7.774 217.502 1.00 46.01 C
ANISOU 1416 CG TYR A 215 4577 5968 6938 375 -926 338 C
ATOM 1417 CD1 TYR A 215 25.062 -7.965 216.652 1.00 49.71 C
ANISOU 1417 CD1 TYR A 215 5262 6266 7360 295 -857 438 C
ATOM 1418 CD2 TYR A 215 24.128 -6.872 218.552 1.00 52.09 C
ANISOU 1418 CD2 TYR A 215 5294 6701 7796 440 -877 288 C
ATOM 1419 CE1 TYR A 215 26.253 -7.281 216.835 1.00 52.17 C
ANISOU 1419 CE1 TYR A 215 5702 6394 7726 269 -739 464 C
ATOM 1420 CE2 TYR A 215 25.316 -6.178 218.740 1.00 49.75 C
ANISOU 1420 CE2 TYR A 215 5143 6219 7539 413 -773 323 C
ATOM 1421 CZ TYR A 215 26.374 -6.386 217.875 1.00 51.30 C
ANISOU 1421 CZ TYR A 215 5523 6266 7702 322 -702 400 C
ATOM 1422 OH TYR A 215 27.558 -5.705 218.052 1.00 54.00 O
ANISOU 1422 OH TYR A 215 5975 6443 8102 267 -578 394 O
ATOM 1423 N HIS A 216 22.570 -9.662 220.254 1.00 53.94 N
ANISOU 1423 N HIS A 216 5095 7392 8007 138 -777 84 N
ATOM 1424 CA HIS A 216 23.144 -9.594 221.589 1.00 49.93 C
ANISOU 1424 CA HIS A 216 4591 6843 7539 100 -666 54 C
ATOM 1425 C HIS A 216 23.382 -10.978 222.181 1.00 49.27 C
ANISOU 1425 C HIS A 216 4544 6802 7374 -67 -546 35 C
ATOM 1426 O HIS A 216 24.334 -11.152 222.952 1.00 49.63 O
ANISOU 1426 O HIS A 216 4684 6769 7405 -90 -480 58 O
ATOM 1427 CB HIS A 216 22.264 -8.713 222.476 1.00 48.95 C
ANISOU 1427 CB HIS A 216 4320 6781 7498 204 -673 -55 C
ATOM 1428 CG HIS A 216 22.441 -7.251 222.201 1.00 44.13 C
ANISOU 1428 CG HIS A 216 3766 6055 6948 383 -747 -17 C
ATOM 1429 ND1 HIS A 216 23.582 -6.562 222.557 1.00 46.27 N
ANISOU 1429 ND1 HIS A 216 4176 6162 7243 390 -695 34 N
ATOM 1430 CD2 HIS A 216 21.650 -6.361 221.556 1.00 46.08 C
ANISOU 1430 CD2 HIS A 216 3976 6315 7217 567 -862 -31 C
ATOM 1431 CE1 HIS A 216 23.469 -5.304 222.171 1.00 42.95 C
ANISOU 1431 CE1 HIS A 216 3828 5639 6852 543 -743 52 C
ATOM 1432 NE2 HIS A 216 22.306 -5.154 221.565 1.00 50.74 N
ANISOU 1432 NE2 HIS A 216 4728 6723 7830 675 -852 24 N
ATOM 1433 N SER A 217 22.608 -11.993 221.778 1.00 45.03 N
ANISOU 1433 N SER A 217 3963 6379 6767 -182 -520 -9 N
ATOM 1434 CA SER A 217 22.999 -13.358 222.116 1.00 46.60 C
ANISOU 1434 CA SER A 217 4291 6565 6850 -337 -386 1 C
ATOM 1435 C SER A 217 24.368 -13.689 221.529 1.00 48.68 C
ANISOU 1435 C SER A 217 4737 6693 7068 -331 -386 141 C
ATOM 1436 O SER A 217 25.254 -14.209 222.230 1.00 48.84 O
ANISOU 1436 O SER A 217 4877 6644 7036 -342 -310 167 O
ATOM 1437 CB SER A 217 21.945 -14.341 221.617 1.00 50.07 C
ANISOU 1437 CB SER A 217 4671 7137 7216 -490 -339 -81 C
ATOM 1438 OG SER A 217 20.700 -14.110 222.249 1.00 55.16 O
ANISOU 1438 OG SER A 217 5113 7924 7922 -515 -307 -251 O
ATOM 1439 N CYS A 218 24.571 -13.371 220.244 1.00 52.28 N
ANISOU 1439 N CYS A 218 5223 7105 7537 -299 -472 223 N
ATOM 1440 CA CYS A 218 25.871 -13.651 219.640 1.00 46.85 C
ANISOU 1440 CA CYS A 218 4695 6281 6823 -306 -442 337 C
ATOM 1441 C CYS A 218 26.974 -12.822 220.289 1.00 49.93 C
ANISOU 1441 C CYS A 218 5088 6576 7307 -216 -439 345 C
ATOM 1442 O CYS A 218 28.093 -13.308 220.477 1.00 49.78 O
ANISOU 1442 O CYS A 218 5146 6494 7273 -226 -382 377 O
ATOM 1443 CB CYS A 218 25.823 -13.392 218.133 1.00 45.67 C
ANISOU 1443 CB CYS A 218 4617 6075 6659 -298 -513 413 C
ATOM 1444 SG CYS A 218 24.693 -14.485 217.224 1.00 54.81 S
ANISOU 1444 SG CYS A 218 5783 7354 7689 -428 -534 391 S
ATOM 1445 N PHE A 219 26.670 -11.580 220.674 1.00 48.22 N
ANISOU 1445 N PHE A 219 4782 6356 7184 -124 -499 298 N
ATOM 1446 CA PHE A 219 27.688 -10.726 221.281 1.00 42.70 C
ANISOU 1446 CA PHE A 219 4084 5570 6570 -69 -488 281 C
ATOM 1447 C PHE A 219 28.136 -11.287 222.621 1.00 42.66 C
ANISOU 1447 C PHE A 219 4065 5608 6537 -79 -448 223 C
ATOM 1448 O PHE A 219 29.342 -11.375 222.899 1.00 43.81 O
ANISOU 1448 O PHE A 219 4236 5706 6702 -67 -434 219 O
ATOM 1449 CB PHE A 219 27.144 -9.303 221.444 1.00 43.84 C
ANISOU 1449 CB PHE A 219 4174 5688 6796 28 -541 241 C
ATOM 1450 CG PHE A 219 28.183 -8.290 221.845 1.00 45.19 C
ANISOU 1450 CG PHE A 219 4372 5748 7050 52 -511 213 C
ATOM 1451 CD1 PHE A 219 28.598 -8.182 223.166 1.00 38.65 C
ANISOU 1451 CD1 PHE A 219 3484 4952 6248 51 -495 134 C
ATOM 1452 CD2 PHE A 219 28.749 -7.453 220.900 1.00 42.13 C
ANISOU 1452 CD2 PHE A 219 4093 5215 6701 61 -487 250 C
ATOM 1453 CE1 PHE A 219 29.557 -7.254 223.532 1.00 43.24 C
ANISOU 1453 CE1 PHE A 219 4072 5450 6906 48 -471 79 C
ATOM 1454 CE2 PHE A 219 29.710 -6.519 221.263 1.00 47.04 C
ANISOU 1454 CE2 PHE A 219 4738 5733 7401 41 -426 193 C
ATOM 1455 CZ PHE A 219 30.113 -6.420 222.582 1.00 46.23 C
ANISOU 1455 CZ PHE A 219 4534 5693 7339 29 -425 100 C
ATOM 1456 N PHE A 220 27.178 -11.726 223.441 1.00 43.50 N
ANISOU 1456 N PHE A 220 4139 5804 6586 -98 -425 164 N
ATOM 1457 CA PHE A 220 27.537 -12.315 224.725 1.00 43.45 C
ANISOU 1457 CA PHE A 220 4194 5808 6507 -96 -380 113 C
ATOM 1458 C PHE A 220 28.361 -13.580 224.530 1.00 46.15 C
ANISOU 1458 C PHE A 220 4673 6123 6740 -117 -339 167 C
ATOM 1459 O PHE A 220 29.410 -13.755 225.161 1.00 51.97 O
ANISOU 1459 O PHE A 220 5461 6831 7454 -47 -362 153 O
ATOM 1460 CB PHE A 220 26.276 -12.613 225.535 1.00 45.20 C
ANISOU 1460 CB PHE A 220 4399 6101 6673 -142 -314 30 C
ATOM 1461 CG PHE A 220 26.541 -13.343 226.819 1.00 47.73 C
ANISOU 1461 CG PHE A 220 4868 6399 6870 -145 -245 -18 C
ATOM 1462 CD1 PHE A 220 27.234 -12.729 227.854 1.00 46.54 C
ANISOU 1462 CD1 PHE A 220 4742 6206 6735 -56 -295 -59 C
ATOM 1463 CD2 PHE A 220 26.081 -14.638 227.002 1.00 50.66 C
ANISOU 1463 CD2 PHE A 220 5388 6776 7085 -237 -124 -32 C
ATOM 1464 CE1 PHE A 220 27.474 -13.400 229.046 1.00 46.12 C
ANISOU 1464 CE1 PHE A 220 4873 6117 6534 -30 -254 -104 C
ATOM 1465 CE2 PHE A 220 26.315 -15.316 228.194 1.00 46.28 C
ANISOU 1465 CE2 PHE A 220 5047 6161 6375 -219 -48 -73 C
ATOM 1466 CZ PHE A 220 27.017 -14.695 229.214 1.00 43.65 C
ANISOU 1466 CZ PHE A 220 4749 5786 6049 -100 -128 -104 C
ATOM 1467 N ILE A 221 27.906 -14.478 223.652 1.00 46.55 N
ANISOU 1467 N ILE A 221 4786 6188 6714 -203 -284 220 N
ATOM 1468 CA ILE A 221 28.632 -15.735 223.511 1.00 41.96 C
ANISOU 1468 CA ILE A 221 4371 5563 6007 -213 -221 274 C
ATOM 1469 C ILE A 221 30.020 -15.534 222.912 1.00 47.60 C
ANISOU 1469 C ILE A 221 5073 6214 6797 -143 -263 327 C
ATOM 1470 O ILE A 221 30.962 -16.256 223.268 1.00 46.77 O
ANISOU 1470 O ILE A 221 5061 6083 6626 -69 -249 334 O
ATOM 1471 CB ILE A 221 27.804 -16.733 222.692 1.00 45.63 C
ANISOU 1471 CB ILE A 221 4923 6050 6365 -348 -132 307 C
ATOM 1472 CG1 ILE A 221 26.590 -17.176 223.517 1.00 45.67 C
ANISOU 1472 CG1 ILE A 221 4955 6119 6280 -442 -39 210 C
ATOM 1473 CG2 ILE A 221 28.678 -17.923 222.277 1.00 40.26 C
ANISOU 1473 CG2 ILE A 221 4438 5295 5564 -347 -57 386 C
ATOM 1474 CD1 ILE A 221 25.679 -18.140 222.807 1.00 62.62 C
ANISOU 1474 CD1 ILE A 221 7160 8309 8323 -616 65 194 C
ATOM 1475 N VAL A 222 30.193 -14.551 222.028 1.00 50.09 N
ANISOU 1475 N VAL A 222 5287 6498 7247 -154 -304 350 N
ATOM 1476 CA VAL A 222 31.456 -14.439 221.304 1.00 42.54 C
ANISOU 1476 CA VAL A 222 4330 5466 6365 -135 -289 381 C
ATOM 1477 C VAL A 222 32.489 -13.634 222.086 1.00 51.89 C
ANISOU 1477 C VAL A 222 5398 6653 7663 -57 -339 289 C
ATOM 1478 O VAL A 222 33.672 -13.997 222.122 1.00 53.16 O
ANISOU 1478 O VAL A 222 5537 6809 7854 -7 -331 260 O
ATOM 1479 CB VAL A 222 31.191 -13.835 219.911 1.00 51.01 C
ANISOU 1479 CB VAL A 222 5420 6467 7496 -202 -276 443 C
ATOM 1480 CG1 VAL A 222 32.464 -13.250 219.315 1.00 49.07 C
ANISOU 1480 CG1 VAL A 222 5157 6119 7369 -203 -230 433 C
ATOM 1481 CG2 VAL A 222 30.613 -14.890 218.990 1.00 47.31 C
ANISOU 1481 CG2 VAL A 222 5080 5992 6904 -283 -228 526 C
ATOM 1482 N THR A 223 32.086 -12.514 222.691 1.00 54.50 N
ANISOU 1482 N THR A 223 5641 6999 8065 -45 -390 226 N
ATOM 1483 CA THR A 223 33.043 -11.700 223.431 1.00 49.89 C
ANISOU 1483 CA THR A 223 4949 6422 7584 -2 -433 118 C
ATOM 1484 C THR A 223 33.199 -12.119 224.885 1.00 49.66 C
ANISOU 1484 C THR A 223 4924 6471 7474 90 -505 44 C
ATOM 1485 O THR A 223 34.097 -11.609 225.561 1.00 52.89 O
ANISOU 1485 O THR A 223 5238 6910 7949 136 -567 -64 O
ATOM 1486 CB THR A 223 32.656 -10.219 223.383 1.00 55.57 C
ANISOU 1486 CB THR A 223 5618 7091 8407 -34 -434 80 C
ATOM 1487 OG1 THR A 223 31.366 -10.046 223.975 1.00 48.74 O
ANISOU 1487 OG1 THR A 223 4770 6267 7484 -10 -464 89 O
ATOM 1488 CG2 THR A 223 32.630 -9.721 221.948 1.00 54.46 C
ANISOU 1488 CG2 THR A 223 5538 6837 8318 -98 -365 147 C
ATOM 1489 N TYR A 224 32.361 -13.021 225.390 1.00 57.38 N
ANISOU 1489 N TYR A 224 6026 7477 8300 108 -491 83 N
ATOM 1490 CA TYR A 224 32.468 -13.371 226.799 1.00 50.40 C
ANISOU 1490 CA TYR A 224 5216 6628 7306 201 -546 14 C
ATOM 1491 C TYR A 224 32.456 -14.877 227.036 1.00 53.44 C
ANISOU 1491 C TYR A 224 5809 7004 7494 258 -507 61 C
ATOM 1492 O TYR A 224 33.487 -15.466 227.373 1.00 50.40 O
ANISOU 1492 O TYR A 224 5474 6629 7047 390 -569 36 O
ATOM 1493 CB TYR A 224 31.340 -12.708 227.607 1.00 42.99 C
ANISOU 1493 CB TYR A 224 4285 5695 6356 165 -533 -27 C
ATOM 1494 CG TYR A 224 31.539 -12.878 229.097 1.00 49.97 C
ANISOU 1494 CG TYR A 224 5276 6587 7124 255 -587 -109 C
ATOM 1495 CD1 TYR A 224 32.306 -11.972 229.818 1.00 45.04 C
ANISOU 1495 CD1 TYR A 224 4561 5982 6571 312 -692 -209 C
ATOM 1496 CD2 TYR A 224 31.007 -13.973 229.772 1.00 47.75 C
ANISOU 1496 CD2 TYR A 224 5222 6280 6640 277 -524 -97 C
ATOM 1497 CE1 TYR A 224 32.516 -12.133 231.171 1.00 47.06 C
ANISOU 1497 CE1 TYR A 224 4942 6242 6698 407 -765 -288 C
ATOM 1498 CE2 TYR A 224 31.217 -14.145 231.130 1.00 47.16 C
ANISOU 1498 CE2 TYR A 224 5313 6183 6425 376 -573 -169 C
ATOM 1499 CZ TYR A 224 31.975 -13.224 231.821 1.00 53.19 C
ANISOU 1499 CZ TYR A 224 5976 6976 7259 452 -711 -260 C
ATOM 1500 OH TYR A 224 32.183 -13.384 233.172 1.00 55.87 O
ANISOU 1500 OH TYR A 224 6502 7288 7436 560 -782 -336 O
ATOM 1501 N LEU A 225 31.293 -15.511 226.879 1.00 46.26 N
ANISOU 1501 N LEU A 225 5026 6074 6475 165 -398 113 N
ATOM 1502 CA LEU A 225 31.123 -16.856 227.424 1.00 45.51 C
ANISOU 1502 CA LEU A 225 5198 5939 6152 201 -322 131 C
ATOM 1503 C LEU A 225 32.053 -17.864 226.760 1.00 51.15 C
ANISOU 1503 C LEU A 225 6016 6622 6798 278 -309 199 C
ATOM 1504 O LEU A 225 32.772 -18.593 227.447 1.00 59.13 O
ANISOU 1504 O LEU A 225 7199 7605 7664 441 -348 184 O
ATOM 1505 CB LEU A 225 29.670 -17.310 227.289 1.00 44.18 C
ANISOU 1505 CB LEU A 225 5121 5763 5901 35 -170 138 C
ATOM 1506 CG LEU A 225 29.398 -18.673 227.936 1.00 48.25 C
ANISOU 1506 CG LEU A 225 5974 6204 6157 32 -35 136 C
ATOM 1507 CD1 LEU A 225 29.602 -18.595 229.445 1.00 44.95 C
ANISOU 1507 CD1 LEU A 225 5723 5739 5617 156 -72 61 C
ATOM 1508 CD2 LEU A 225 28.006 -19.194 227.606 1.00 40.26 C
ANISOU 1508 CD2 LEU A 225 5018 5198 5081 -186 149 112 C
ATOM 1509 N ALA A 226 32.026 -17.958 225.431 1.00 47.55 N
ANISOU 1509 N ALA A 226 5486 6159 6424 178 -254 274 N
ATOM 1510 CA ALA A 226 32.842 -18.971 224.764 1.00 49.72 C
ANISOU 1510 CA ALA A 226 5879 6387 6627 241 -208 341 C
ATOM 1511 C ALA A 226 34.341 -18.785 224.970 1.00 55.92 C
ANISOU 1511 C ALA A 226 6552 7199 7497 429 -325 291 C
ATOM 1512 O ALA A 226 35.010 -19.754 225.375 1.00 65.96 O
ANISOU 1512 O ALA A 226 7991 8447 8623 599 -338 294 O
ATOM 1513 CB ALA A 226 32.499 -19.002 223.270 1.00 47.31 C
ANISOU 1513 CB ALA A 226 5526 6056 6393 82 -125 424 C
ATOM 1514 N PRO A 227 34.938 -17.623 224.686 1.00 49.37 N
ANISOU 1514 N PRO A 227 5454 6417 6889 412 -403 228 N
ATOM 1515 CA PRO A 227 36.386 -17.497 224.920 1.00 48.68 C
ANISOU 1515 CA PRO A 227 5218 6384 6895 572 -504 133 C
ATOM 1516 C PRO A 227 36.778 -17.723 226.366 1.00 55.38 C
ANISOU 1516 C PRO A 227 6133 7290 7621 776 -649 41 C
ATOM 1517 O PRO A 227 37.814 -18.344 226.632 1.00 46.09 O
ANISOU 1517 O PRO A 227 4963 6151 6397 981 -732 -11 O
ATOM 1518 CB PRO A 227 36.702 -16.069 224.444 1.00 48.18 C
ANISOU 1518 CB PRO A 227 4885 6344 7079 452 -518 59 C
ATOM 1519 CG PRO A 227 35.379 -15.365 224.367 1.00 47.67 C
ANISOU 1519 CG PRO A 227 4853 6244 7016 302 -478 111 C
ATOM 1520 CD PRO A 227 34.364 -16.418 224.062 1.00 46.06 C
ANISOU 1520 CD PRO A 227 4869 5996 6637 252 -386 230 C
ATOM 1521 N LEU A 228 35.946 -17.291 227.317 1.00 51.17 N
ANISOU 1521 N LEU A 228 5672 6756 7015 743 -683 15 N
ATOM 1522 CA LEU A 228 36.328 -17.429 228.720 1.00 51.69 C
ANISOU 1522 CA LEU A 228 5838 6857 6945 937 -830 -78 C
ATOM 1523 C LEU A 228 36.180 -18.870 229.192 1.00 54.08 C
ANISOU 1523 C LEU A 228 6517 7078 6954 1091 -790 -13 C
ATOM 1524 O LEU A 228 37.015 -19.363 229.957 1.00 56.23 O
ANISOU 1524 O LEU A 228 6895 7373 7095 1347 -933 -75 O
ATOM 1525 CB LEU A 228 35.515 -16.469 229.595 1.00 53.71 C
ANISOU 1525 CB LEU A 228 6080 7114 7213 845 -854 -132 C
ATOM 1526 CG LEU A 228 35.934 -15.000 229.444 1.00 54.45 C
ANISOU 1526 CG LEU A 228 5852 7279 7559 755 -923 -232 C
ATOM 1527 CD1 LEU A 228 35.086 -14.092 230.318 1.00 53.30 C
ANISOU 1527 CD1 LEU A 228 5727 7116 7409 676 -928 -276 C
ATOM 1528 CD2 LEU A 228 37.421 -14.813 229.771 1.00 43.74 C
ANISOU 1528 CD2 LEU A 228 4307 6030 6282 910 -1095 -378 C
ATOM 1529 N GLY A 229 35.159 -19.583 228.712 1.00 45.41 N
ANISOU 1529 N GLY A 229 5637 5882 5736 946 -597 101 N
ATOM 1530 CA GLY A 229 35.051 -20.993 229.053 1.00 49.10 C
ANISOU 1530 CA GLY A 229 6509 6239 5908 1066 -510 161 C
ATOM 1531 C GLY A 229 36.161 -21.827 228.439 1.00 54.97 C
ANISOU 1531 C GLY A 229 7284 6979 6624 1254 -537 197 C
ATOM 1532 O GLY A 229 36.725 -22.715 229.095 1.00 62.55 O
ANISOU 1532 O GLY A 229 8517 7888 7360 1518 -596 190 O
ATOM 1533 N LEU A 230 36.533 -21.523 227.190 1.00 58.36 N
ANISOU 1533 N LEU A 230 7448 7453 7274 1146 -497 229 N
ATOM 1534 CA LEU A 230 37.645 -22.245 226.577 1.00 60.95 C
ANISOU 1534 CA LEU A 230 7769 7782 7609 1323 -506 246 C
ATOM 1535 C LEU A 230 38.961 -21.927 227.279 1.00 66.54 C
ANISOU 1535 C LEU A 230 8276 8615 8392 1608 -742 101 C
ATOM 1536 O LEU A 230 39.786 -22.823 227.499 1.00 68.61 O
ANISOU 1536 O LEU A 230 8675 8873 8522 1894 -808 86 O
ATOM 1537 CB LEU A 230 37.736 -21.909 225.089 1.00 51.54 C
ANISOU 1537 CB LEU A 230 6354 6591 6638 1119 -388 299 C
ATOM 1538 CG LEU A 230 36.610 -22.429 224.196 1.00 44.99 C
ANISOU 1538 CG LEU A 230 5723 5653 5719 872 -177 435 C
ATOM 1539 CD1 LEU A 230 36.663 -21.760 222.831 1.00 47.66 C
ANISOU 1539 CD1 LEU A 230 5827 5996 6286 674 -111 467 C
ATOM 1540 CD2 LEU A 230 36.714 -23.951 224.057 1.00 45.10 C
ANISOU 1540 CD2 LEU A 230 6111 5548 5476 981 -48 523 C
ATOM 1541 N MET A 231 39.160 -20.662 227.668 1.00 65.30 N
ANISOU 1541 N MET A 231 7802 8575 8436 1545 -876 -23 N
ATOM 1542 CA MET A 231 40.358 -20.292 228.411 1.00 63.72 C
ANISOU 1542 CA MET A 231 7381 8521 8308 1787 -1116 -201 C
ATOM 1543 C MET A 231 40.390 -20.968 229.771 1.00 67.48 C
ANISOU 1543 C MET A 231 8181 8975 8483 2077 -1272 -229 C
ATOM 1544 O MET A 231 41.461 -21.345 230.256 1.00 67.66 O
ANISOU 1544 O MET A 231 8164 9090 8452 2397 -1470 -338 O
ATOM 1545 CB MET A 231 40.421 -18.775 228.590 1.00 65.40 C
ANISOU 1545 CB MET A 231 7242 8839 8769 1611 -1193 -331 C
ATOM 1546 CG MET A 231 40.735 -17.994 227.338 1.00 53.66 C
ANISOU 1546 CG MET A 231 5434 7373 7579 1381 -1068 -354 C
ATOM 1547 SD MET A 231 41.017 -16.254 227.716 1.00 58.44 S
ANISOU 1547 SD MET A 231 5684 8086 8435 1216 -1155 -542 S
ATOM 1548 CE MET A 231 39.406 -15.559 227.425 1.00 45.42 C
ANISOU 1548 CE MET A 231 4187 6299 6771 935 -994 -388 C
ATOM 1549 N ALA A 232 39.225 -21.138 230.400 1.00 65.73 N
ANISOU 1549 N ALA A 232 8294 8627 8052 1980 -1183 -144 N
ATOM 1550 CA ALA A 232 39.192 -21.822 231.685 1.00 60.25 C
ANISOU 1550 CA ALA A 232 8001 7861 7029 2243 -1292 -162 C
ATOM 1551 C ALA A 232 39.606 -23.273 231.530 1.00 61.03 C
ANISOU 1551 C ALA A 232 8455 7857 6877 2507 -1248 -82 C
ATOM 1552 O ALA A 232 40.411 -23.782 232.316 1.00 70.00 O
ANISOU 1552 O ALA A 232 9756 9015 7827 2881 -1453 -153 O
ATOM 1553 CB ALA A 232 37.798 -21.719 232.306 1.00 52.17 C
ANISOU 1553 CB ALA A 232 7276 6701 5847 2036 -1137 -101 C
ATOM 1554 N MET A 233 39.090 -23.950 230.504 1.00 66.78 N
ANISOU 1554 N MET A 233 9316 8473 7586 2335 -993 60 N
ATOM 1555 CA MET A 233 39.499 -25.336 230.306 1.00 66.27 C
ANISOU 1555 CA MET A 233 9616 8289 7274 2581 -923 141 C
ATOM 1556 C MET A 233 40.985 -25.432 229.964 1.00 60.26 C
ANISOU 1556 C MET A 233 8562 7677 6659 2889 -1116 50 C
ATOM 1557 O MET A 233 41.691 -26.325 230.465 1.00 68.25 O
ANISOU 1557 O MET A 233 9837 8655 7440 3284 -1234 32 O
ATOM 1558 CB MET A 233 38.631 -25.975 229.227 1.00 70.23 C
ANISOU 1558 CB MET A 233 10298 8648 7740 2291 -600 295 C
ATOM 1559 CG MET A 233 37.157 -26.023 229.624 1.00 72.16 C
ANISOU 1559 CG MET A 233 10832 8761 7824 2004 -399 346 C
ATOM 1560 SD MET A 233 36.094 -26.821 228.405 1.00 76.75 S
ANISOU 1560 SD MET A 233 11613 9203 8344 1649 -37 484 S
ATOM 1561 CE MET A 233 34.646 -27.149 229.404 1.00 88.44 C
ANISOU 1561 CE MET A 233 13531 10528 9544 1450 166 468 C
ATOM 1562 N ALA A 234 41.495 -24.480 229.176 1.00 59.82 N
ANISOU 1562 N ALA A 234 7964 7785 6979 2728 -1153 -31 N
ATOM 1563 CA ALA A 234 42.907 -24.508 228.805 1.00 63.02 C
ANISOU 1563 CA ALA A 234 8030 8347 7567 2975 -1301 -158 C
ATOM 1564 C ALA A 234 43.798 -24.304 230.023 1.00 65.03 C
ANISOU 1564 C ALA A 234 8197 8748 7765 3232 -1590 -349 C
ATOM 1565 O ALA A 234 44.771 -25.039 230.231 1.00 73.76 O
ANISOU 1565 O ALA A 234 9355 9895 8777 3476 -1669 -419 O
ATOM 1566 CB ALA A 234 43.192 -23.441 227.748 1.00 53.08 C
ANISOU 1566 CB ALA A 234 6249 7203 6715 2671 -1223 -226 C
ATOM 1567 N TYR A 235 43.484 -23.300 230.841 1.00 64.06 N
ANISOU 1567 N TYR A 235 7951 8697 7692 3118 -1719 -442 N
ATOM 1568 CA TYR A 235 44.291 -23.048 232.024 1.00 67.80 C
ANISOU 1568 CA TYR A 235 8370 9292 8100 3278 -1956 -628 C
ATOM 1569 C TYR A 235 44.135 -24.147 233.064 1.00 78.85 C
ANISOU 1569 C TYR A 235 10334 10554 9072 3581 -2020 -585 C
ATOM 1570 O TYR A 235 45.069 -24.400 233.831 1.00 73.33 O
ANISOU 1570 O TYR A 235 9650 9943 8271 3822 -2209 -733 O
ATOM 1571 CB TYR A 235 43.954 -21.676 232.604 1.00 56.06 C
ANISOU 1571 CB TYR A 235 6645 7891 6764 3064 -2048 -732 C
ATOM 1572 CG TYR A 235 44.655 -20.569 231.851 1.00 57.25 C
ANISOU 1572 CG TYR A 235 6235 8205 7313 2814 -2021 -865 C
ATOM 1573 CD1 TYR A 235 46.046 -20.493 231.840 1.00 62.70 C
ANISOU 1573 CD1 TYR A 235 6632 9055 8138 2899 -2120 -1048 C
ATOM 1574 CD2 TYR A 235 43.941 -19.625 231.137 1.00 50.57 C
ANISOU 1574 CD2 TYR A 235 5184 7340 6692 2495 -1878 -816 C
ATOM 1575 CE1 TYR A 235 46.700 -19.499 231.146 1.00 65.74 C
ANISOU 1575 CE1 TYR A 235 6563 9557 8858 2651 -2050 -1175 C
ATOM 1576 CE2 TYR A 235 44.586 -18.624 230.435 1.00 64.14 C
ANISOU 1576 CE2 TYR A 235 6473 9163 8735 2252 -1806 -935 C
ATOM 1577 CZ TYR A 235 45.966 -18.568 230.443 1.00 68.21 C
ANISOU 1577 CZ TYR A 235 6734 9819 9365 2322 -1880 -1113 C
ATOM 1578 OH TYR A 235 46.626 -17.576 229.751 1.00 72.50 O
ANISOU 1578 OH TYR A 235 6901 10442 10203 2070 -1776 -1242 O
ATOM 1579 N PHE A 236 42.993 -24.835 233.096 1.00 75.17 N
ANISOU 1579 N PHE A 236 10363 9860 8337 3571 -1848 -395 N
ATOM 1580 CA PHE A 236 42.889 -25.991 233.977 1.00 80.58 C
ANISOU 1580 CA PHE A 236 11651 10370 8595 3832 -1837 -359 C
ATOM 1581 C PHE A 236 43.844 -27.093 233.537 1.00 82.04 C
ANISOU 1581 C PHE A 236 11917 10561 8694 4078 -1820 -367 C
ATOM 1582 O PHE A 236 44.525 -27.714 234.369 1.00 79.97 O
ANISOU 1582 O PHE A 236 11885 10300 8200 4379 -1959 -471 O
ATOM 1583 CB PHE A 236 41.447 -26.500 234.007 1.00 82.27 C
ANISOU 1583 CB PHE A 236 12398 10313 8549 3693 -1580 -162 C
ATOM 1584 CG PHE A 236 41.257 -27.736 234.839 1.00 95.78 C
ANISOU 1584 CG PHE A 236 14784 11794 9816 3899 -1481 -137 C
ATOM 1585 CD1 PHE A 236 41.145 -27.649 236.216 1.00101.29 C
ANISOU 1585 CD1 PHE A 236 15781 12418 10285 4031 -1597 -237 C
ATOM 1586 CD2 PHE A 236 41.188 -28.986 234.244 1.00 98.19 C
ANISOU 1586 CD2 PHE A 236 15447 11931 9932 3951 -1246 -28 C
ATOM 1587 CE1 PHE A 236 40.969 -28.783 236.984 1.00 99.34 C
ANISOU 1587 CE1 PHE A 236 16179 11920 9644 4220 -1474 -239 C
ATOM 1588 CE2 PHE A 236 41.012 -30.125 235.009 1.00 94.16 C
ANISOU 1588 CE2 PHE A 236 15569 11183 9026 4125 -1117 -39 C
ATOM 1589 CZ PHE A 236 40.903 -30.023 236.380 1.00 96.65 C
ANISOU 1589 CZ PHE A 236 16179 11411 9132 4265 -1228 -149 C
ATOM 1590 N GLN A 237 43.928 -27.343 232.229 1.00 74.77 N
ANISOU 1590 N GLN A 237 10816 9639 7953 3971 -1654 -267 N
ATOM 1591 CA GLN A 237 44.899 -28.336 231.774 1.00 83.83 C
ANISOU 1591 CA GLN A 237 12007 10804 9042 4208 -1640 -283 C
ATOM 1592 C GLN A 237 46.330 -27.878 232.047 1.00 82.55 C
ANISOU 1592 C GLN A 237 11373 10904 9088 4373 -1908 -513 C
ATOM 1593 O GLN A 237 47.191 -28.687 232.422 1.00 83.79 O
ANISOU 1593 O GLN A 237 11675 11090 9071 4689 -2015 -593 O
ATOM 1594 CB GLN A 237 44.690 -28.632 230.291 1.00 77.35 C
ANISOU 1594 CB GLN A 237 11090 9914 8385 4045 -1393 -132 C
ATOM 1595 CG GLN A 237 43.359 -29.305 230.009 1.00 72.32 C
ANISOU 1595 CG GLN A 237 10985 9001 7494 3891 -1102 88 C
ATOM 1596 CD GLN A 237 43.351 -30.066 228.704 1.00 74.53 C
ANISOU 1596 CD GLN A 237 11353 9166 7800 3829 -847 232 C
ATOM 1597 OE1 GLN A 237 43.850 -29.586 227.684 1.00 75.28 O
ANISOU 1597 OE1 GLN A 237 11002 9373 8227 3749 -835 216 O
ATOM 1598 NE2 GLN A 237 42.785 -31.268 228.729 1.00 75.18 N
ANISOU 1598 NE2 GLN A 237 12030 9008 7525 3843 -611 356 N
ATOM 1599 N ILE A 238 46.593 -26.577 231.903 1.00 84.14 N
ANISOU 1599 N ILE A 238 11030 11292 9647 4156 -2008 -636 N
ATOM 1600 CA ILE A 238 47.931 -26.058 232.178 1.00 81.01 C
ANISOU 1600 CA ILE A 238 10183 11140 9457 4255 -2229 -877 C
ATOM 1601 C ILE A 238 48.273 -26.229 233.651 1.00 89.66 C
ANISOU 1601 C ILE A 238 11519 12271 10277 4533 -2480 -1015 C
ATOM 1602 O ILE A 238 49.428 -26.492 234.014 1.00 98.41 O
ANISOU 1602 O ILE A 238 12493 13525 11374 4790 -2668 -1189 O
ATOM 1603 CB ILE A 238 48.028 -24.583 231.749 1.00 76.76 C
ANISOU 1603 CB ILE A 238 9085 10755 9326 3909 -2225 -981 C
ATOM 1604 CG1 ILE A 238 47.902 -24.452 230.233 1.00 69.33 C
ANISOU 1604 CG1 ILE A 238 7897 9782 8663 3674 -1982 -881 C
ATOM 1605 CG2 ILE A 238 49.325 -23.962 232.252 1.00 82.58 C
ANISOU 1605 CG2 ILE A 238 9415 11729 10231 3980 -2444 -1254 C
ATOM 1606 CD1 ILE A 238 47.592 -23.034 229.774 1.00 62.65 C
ANISOU 1606 CD1 ILE A 238 6657 9005 8143 3294 -1908 -931 C
ATOM 1607 N PHE A 239 47.272 -26.090 234.521 1.00 88.88 N
ANISOU 1607 N PHE A 239 11791 12032 9947 4499 -2483 -948 N
ATOM 1608 CA PHE A 239 47.496 -26.282 235.948 1.00 93.22 C
ANISOU 1608 CA PHE A 239 12646 12568 10204 4771 -2698 -1072 C
ATOM 1609 C PHE A 239 47.785 -27.741 236.263 1.00 94.06 C
ANISOU 1609 C PHE A 239 13268 12539 9930 5146 -2693 -1037 C
ATOM 1610 O PHE A 239 48.680 -28.046 237.060 1.00101.06 O
ANISOU 1610 O PHE A 239 14213 13513 10672 5470 -2922 -1208 O
ATOM 1611 CB PHE A 239 46.281 -25.795 236.737 1.00 89.69 C
ANISOU 1611 CB PHE A 239 12505 11966 9607 4623 -2657 -999 C
ATOM 1612 CG PHE A 239 46.276 -26.224 238.176 1.00 91.65 C
ANISOU 1612 CG PHE A 239 13237 12103 9482 4912 -2807 -1081 C
ATOM 1613 CD1 PHE A 239 46.866 -25.435 239.147 1.00 95.76 C
ANISOU 1613 CD1 PHE A 239 13561 12771 10054 4993 -3073 -1287 C
ATOM 1614 CD2 PHE A 239 45.668 -27.410 238.560 1.00 98.03 C
ANISOU 1614 CD2 PHE A 239 14729 12634 9882 5091 -2657 -961 C
ATOM 1615 CE1 PHE A 239 46.859 -25.823 240.475 1.00101.83 C
ANISOU 1615 CE1 PHE A 239 14801 13414 10476 5275 -3213 -1365 C
ATOM 1616 CE2 PHE A 239 45.659 -27.806 239.889 1.00100.57 C
ANISOU 1616 CE2 PHE A 239 15540 12813 9857 5360 -2769 -1048 C
ATOM 1617 CZ PHE A 239 46.255 -27.011 240.847 1.00101.87 C
ANISOU 1617 CZ PHE A 239 15500 13127 10079 5465 -3060 -1245 C
ATOM 1618 N ARG A 240 47.046 -28.657 235.634 1.00 93.61 N
ANISOU 1618 N ARG A 240 13601 12266 9699 5111 -2425 -827 N
ATOM 1619 CA ARG A 240 47.329 -30.072 235.847 1.00 93.27 C
ANISOU 1619 CA ARG A 240 14076 12078 9286 5448 -2375 -796 C
ATOM 1620 C ARG A 240 48.723 -30.437 235.358 1.00 92.54 C
ANISOU 1620 C ARG A 240 13646 12188 9328 5687 -2517 -914 C
ATOM 1621 O ARG A 240 49.379 -31.307 235.942 1.00 97.75 O
ANISOU 1621 O ARG A 240 14603 12831 9705 6069 -2638 -1000 O
ATOM 1622 CB ARG A 240 46.286 -30.935 235.139 1.00 95.71 C
ANISOU 1622 CB ARG A 240 14836 12117 9413 5304 -2015 -559 C
ATOM 1623 CG ARG A 240 44.901 -30.873 235.743 1.00106.81 C
ANISOU 1623 CG ARG A 240 16705 13273 10604 5116 -1837 -458 C
ATOM 1624 CD ARG A 240 44.678 -31.999 236.735 1.00125.79 C
ANISOU 1624 CD ARG A 240 19853 15414 12528 5385 -1755 -480 C
ATOM 1625 NE ARG A 240 43.292 -32.454 236.704 1.00138.38 N
ANISOU 1625 NE ARG A 240 21955 16685 13937 5141 -1394 -334 N
ATOM 1626 CZ ARG A 240 42.859 -33.469 235.963 1.00150.12 C
ANISOU 1626 CZ ARG A 240 23773 17972 15294 5061 -1072 -213 C
ATOM 1627 NH1 ARG A 240 43.708 -34.142 235.197 1.00154.79 N
ANISOU 1627 NH1 ARG A 240 24271 18657 15885 5236 -1075 -196 N
ATOM 1628 NH2 ARG A 240 41.578 -33.813 235.990 1.00152.83 N
ANISOU 1628 NH2 ARG A 240 24524 18008 15535 4789 -733 -122 N
ATOM 1629 N LYS A 241 49.194 -29.779 234.297 1.00 92.59 N
ANISOU 1629 N LYS A 241 13044 12375 9762 5475 -2495 -934 N
ATOM 1630 CA LYS A 241 50.506 -30.117 233.754 1.00 90.03 C
ANISOU 1630 CA LYS A 241 12378 12230 9600 5675 -2592 -1052 C
ATOM 1631 C LYS A 241 51.640 -29.515 234.577 1.00 95.87 C
ANISOU 1631 C LYS A 241 12749 13228 10449 5858 -2928 -1337 C
ATOM 1632 O LYS A 241 52.666 -30.170 234.790 1.00104.22 O
ANISOU 1632 O LYS A 241 13802 14386 11409 6209 -3086 -1466 O
ATOM 1633 CB LYS A 241 50.608 -29.654 232.302 1.00 87.31 C
ANISOU 1633 CB LYS A 241 11549 11950 9674 5373 -2405 -987 C
ATOM 1634 CG LYS A 241 51.796 -30.222 231.548 1.00 98.26 C
ANISOU 1634 CG LYS A 241 12674 13451 11209 5563 -2411 -1061 C
ATOM 1635 CD LYS A 241 51.502 -31.615 231.014 1.00107.05 C
ANISOU 1635 CD LYS A 241 14291 14345 12038 5733 -2198 -862 C
ATOM 1636 CE LYS A 241 52.614 -32.091 230.091 1.00113.92 C
ANISOU 1636 CE LYS A 241 14856 15316 13114 5878 -2161 -919 C
ATOM 1637 NZ LYS A 241 52.218 -33.299 229.313 1.00117.88 N
ANISOU 1637 NZ LYS A 241 15805 15583 13400 5948 -1886 -699 N
ATOM 1638 N LEU A 242 51.481 -28.275 235.048 1.00 94.64 N
ANISOU 1638 N LEU A 242 12288 13182 10487 5631 -3038 -1446 N
ATOM 1639 CA LEU A 242 52.589 -27.591 235.708 1.00 98.60 C
ANISOU 1639 CA LEU A 242 12382 13944 11138 5747 -3330 -1735 C
ATOM 1640 C LEU A 242 52.734 -27.997 237.173 1.00107.59 C
ANISOU 1640 C LEU A 242 13937 15050 11893 6117 -3582 -1850 C
ATOM 1641 O LEU A 242 53.857 -28.107 237.677 1.00117.68 O
ANISOU 1641 O LEU A 242 15043 16512 13156 6413 -3840 -2079 O
ATOM 1642 CB LEU A 242 52.416 -26.075 235.595 1.00 94.26 C
ANISOU 1642 CB LEU A 242 11353 13518 10945 5342 -3323 -1818 C
ATOM 1643 CG LEU A 242 52.656 -25.458 234.215 1.00 90.39 C
ANISOU 1643 CG LEU A 242 10340 13115 10887 5000 -3122 -1803 C
ATOM 1644 CD1 LEU A 242 52.422 -23.954 234.243 1.00 85.25 C
ANISOU 1644 CD1 LEU A 242 9315 12556 10520 4614 -3104 -1893 C
ATOM 1645 CD2 LEU A 242 54.061 -25.780 233.723 1.00 82.99 C
ANISOU 1645 CD2 LEU A 242 9029 12372 10129 5178 -3198 -1984 C
ATOM 1646 N TRP A 243 51.623 -28.221 237.869 1.00103.59 N
ANISOU 1646 N TRP A 243 13984 14302 11073 6113 -3508 -1711 N
ATOM 1647 CA TRP A 243 51.671 -28.530 239.297 1.00102.79 C
ANISOU 1647 CA TRP A 243 14326 14126 10605 6444 -3720 -1822 C
ATOM 1648 C TRP A 243 51.369 -29.998 239.583 1.00109.26 C
ANISOU 1648 C TRP A 243 15871 14688 10954 6779 -3622 -1704 C
ATOM 1649 O TRP A 243 50.468 -30.590 238.991 1.00108.61 O
ANISOU 1649 O TRP A 243 16130 14383 10753 6637 -3324 -1477 O
ATOM 1650 CB TRP A 243 50.696 -27.638 240.070 1.00103.96 C
ANISOU 1650 CB TRP A 243 14605 14167 10726 6212 -3711 -1793 C
ATOM 1651 CG TRP A 243 51.195 -26.232 240.274 1.00110.80 C
ANISOU 1651 CG TRP A 243 14871 15285 11941 6004 -3889 -1985 C
ATOM 1652 CD1 TRP A 243 51.971 -25.782 241.302 1.00113.47 C
ANISOU 1652 CD1 TRP A 243 15086 15776 12252 6203 -4193 -2232 C
ATOM 1653 CD2 TRP A 243 50.949 -25.097 239.431 1.00106.32 C
ANISOU 1653 CD2 TRP A 243 13779 14832 11787 5555 -3757 -1955 C
ATOM 1654 NE1 TRP A 243 52.224 -24.439 241.152 1.00113.10 N
ANISOU 1654 NE1 TRP A 243 14469 15931 12573 5886 -4242 -2359 N
ATOM 1655 CE2 TRP A 243 51.609 -23.995 240.011 1.00104.56 C
ANISOU 1655 CE2 TRP A 243 13145 14822 11760 5487 -3971 -2193 C
ATOM 1656 CE3 TRP A 243 50.235 -24.907 238.245 1.00 95.72 C
ANISOU 1656 CE3 TRP A 243 12295 13421 10654 5211 -3475 -1759 C
ATOM 1657 CZ2 TRP A 243 51.578 -22.723 239.444 1.00 97.04 C
ANISOU 1657 CZ2 TRP A 243 11677 14001 11193 5078 -3885 -2240 C
ATOM 1658 CZ3 TRP A 243 50.205 -23.643 237.684 1.00 91.13 C
ANISOU 1658 CZ3 TRP A 243 11196 12972 10458 4828 -3411 -1805 C
ATOM 1659 CH2 TRP A 243 50.872 -22.567 238.284 1.00 92.28 C
ANISOU 1659 CH2 TRP A 243 10969 13315 10779 4758 -3603 -2043 C
ATOM 1660 N VAL A 287 64.473 -27.646 234.909 1.00144.04 N
ANISOU 1660 N VAL A 287 14232 21989 18507 7407 -4807 -4149 N
ATOM 1661 CA VAL A 287 63.271 -27.345 235.678 1.00135.27 C
ANISOU 1661 CA VAL A 287 13597 20673 17126 7288 -4820 -3952 C
ATOM 1662 C VAL A 287 63.202 -25.867 236.044 1.00141.90 C
ANISOU 1662 C VAL A 287 14088 21631 18195 6890 -4842 -4129 C
ATOM 1663 O VAL A 287 62.214 -25.419 236.629 1.00140.94 O
ANISOU 1663 O VAL A 287 14282 21354 17915 6729 -4829 -3984 O
ATOM 1664 CB VAL A 287 63.188 -28.205 236.946 1.00141.00 C
ANISOU 1664 CB VAL A 287 14869 21345 17359 7816 -5134 -3956 C
ATOM 1665 CG1 VAL A 287 64.266 -27.789 237.931 1.00149.05 C
ANISOU 1665 CG1 VAL A 287 15568 22673 18394 8078 -5521 -4362 C
ATOM 1666 CG2 VAL A 287 61.805 -28.094 237.576 1.00139.35 C
ANISOU 1666 CG2 VAL A 287 15237 20856 16853 7687 -5064 -3696 C
ATOM 1667 N LYS A 288 64.247 -25.102 235.716 1.00145.54 N
ANISOU 1667 N LYS A 288 13912 22363 19023 6728 -4863 -4453 N
ATOM 1668 CA LYS A 288 64.137 -23.656 235.872 1.00146.03 C
ANISOU 1668 CA LYS A 288 13656 22507 19323 6284 -4806 -4604 C
ATOM 1669 C LYS A 288 62.983 -23.132 235.031 1.00126.54 C
ANISOU 1669 C LYS A 288 11322 19784 16972 5799 -4430 -4292 C
ATOM 1670 O LYS A 288 62.245 -22.222 235.444 1.00126.54 O
ANISOU 1670 O LYS A 288 11411 19706 16964 5512 -4390 -4239 O
ATOM 1671 CB LYS A 288 65.448 -22.975 235.470 1.00126.29 C
ANISOU 1671 CB LYS A 288 10462 20315 17208 6149 -4817 -5006 C
ATOM 1672 CG LYS A 288 66.622 -23.198 236.412 1.00151.21 C
ANISOU 1672 CG LYS A 288 13387 23777 20290 6578 -5221 -5390 C
ATOM 1673 CD LYS A 288 67.876 -22.497 235.892 1.00153.93 C
ANISOU 1673 CD LYS A 288 13016 24422 21048 6388 -5179 -5803 C
ATOM 1674 CE LYS A 288 69.032 -22.622 236.870 1.00157.92 C
ANISOU 1674 CE LYS A 288 13247 25260 21494 6802 -5601 -6221 C
ATOM 1675 NZ LYS A 288 70.271 -21.972 236.363 1.00164.52 N
ANISOU 1675 NZ LYS A 288 13371 26403 22738 6615 -5550 -6657 N
ATOM 1676 N GLN A 289 62.782 -23.747 233.865 1.00111.93 N
ANISOU 1676 N GLN A 289 9518 17794 15215 5731 -4159 -4076 N
ATOM 1677 CA GLN A 289 61.684 -23.356 232.999 1.00118.39 C
ANISOU 1677 CA GLN A 289 10480 18369 16132 5312 -3810 -3779 C
ATOM 1678 C GLN A 289 60.337 -23.643 233.646 1.00122.31 C
ANISOU 1678 C GLN A 289 11568 18624 16283 5360 -3835 -3477 C
ATOM 1679 O GLN A 289 59.398 -22.859 233.485 1.00121.94 O
ANISOU 1679 O GLN A 289 11598 18441 16294 4995 -3663 -3331 O
ATOM 1680 CB GLN A 289 61.797 -24.075 231.657 1.00122.75 C
ANISOU 1680 CB GLN A 289 10985 18821 16832 5287 -3534 -3620 C
ATOM 1681 CG GLN A 289 60.850 -23.534 230.599 1.00123.71 C
ANISOU 1681 CG GLN A 289 11150 18730 17124 4827 -3161 -3376 C
ATOM 1682 CD GLN A 289 61.015 -24.223 229.261 1.00128.95 C
ANISOU 1682 CD GLN A 289 11759 19293 17943 4807 -2880 -3238 C
ATOM 1683 OE1 GLN A 289 61.195 -25.441 229.192 1.00130.51 O
ANISOU 1683 OE1 GLN A 289 12172 19443 17973 5172 -2930 -3135 O
ATOM 1684 NE2 GLN A 289 60.962 -23.444 228.185 1.00125.59 N
ANISOU 1684 NE2 GLN A 289 11072 18819 17827 4385 -2569 -3242 N
ATOM 1685 N MET A 290 60.216 -24.744 234.396 1.00123.82 N
ANISOU 1685 N MET A 290 12197 18750 16099 5808 -4038 -3392 N
ATOM 1686 CA MET A 290 58.921 -25.028 235.007 1.00119.43 C
ANISOU 1686 CA MET A 290 12228 17945 15204 5836 -4027 -3123 C
ATOM 1687 C MET A 290 58.596 -24.019 236.099 1.00114.69 C
ANISOU 1687 C MET A 290 11637 17390 14549 5713 -4190 -3241 C
ATOM 1688 O MET A 290 57.437 -23.626 236.260 1.00119.28 O
ANISOU 1688 O MET A 290 12489 17786 15046 5485 -4068 -3042 O
ATOM 1689 CB MET A 290 58.868 -26.448 235.568 1.00121.80 C
ANISOU 1689 CB MET A 290 13061 18135 15080 6339 -4173 -3019 C
ATOM 1690 CG MET A 290 57.465 -26.827 236.043 1.00120.55 C
ANISOU 1690 CG MET A 290 13550 17683 14572 6331 -4085 -2731 C
ATOM 1691 SD MET A 290 57.363 -28.348 237.005 1.00132.43 S
ANISOU 1691 SD MET A 290 15787 19029 15500 6916 -4260 -2657 S
ATOM 1692 CE MET A 290 58.349 -27.904 238.431 1.00140.11 C
ANISOU 1692 CE MET A 290 16606 20248 16384 7235 -4698 -3027 C
ATOM 1693 N ARG A 291 59.606 -23.559 236.838 1.00115.81 N
ANISOU 1693 N ARG A 291 11468 17781 14753 5855 -4459 -3574 N
ATOM 1694 CA ARG A 291 59.350 -22.553 237.864 1.00112.53 C
ANISOU 1694 CA ARG A 291 11043 17411 14302 5730 -4607 -3698 C
ATOM 1695 C ARG A 291 58.957 -21.219 237.236 1.00105.08 C
ANISOU 1695 C ARG A 291 9772 16461 13691 5176 -4359 -3688 C
ATOM 1696 O ARG A 291 57.984 -20.574 237.670 1.00105.52 O
ANISOU 1696 O ARG A 291 10034 16382 13676 4964 -4305 -3562 O
ATOM 1697 CB ARG A 291 60.581 -22.403 238.760 1.00120.03 C
ANISOU 1697 CB ARG A 291 11720 18643 15245 6025 -4958 -4077 C
ATOM 1698 CG ARG A 291 60.948 -23.669 239.541 1.00126.52 C
ANISOU 1698 CG ARG A 291 12922 19461 15689 6618 -5240 -4106 C
ATOM 1699 CD ARG A 291 62.173 -23.453 240.429 1.00144.77 C
ANISOU 1699 CD ARG A 291 14930 22070 18004 6917 -5610 -4505 C
ATOM 1700 NE ARG A 291 62.472 -24.620 241.257 1.00152.99 N
ANISOU 1700 NE ARG A 291 16391 23090 18647 7511 -5897 -4537 N
ATOM 1701 CZ ARG A 291 63.519 -24.712 242.070 1.00160.35 C
ANISOU 1701 CZ ARG A 291 17155 24264 19507 7890 -6259 -4868 C
ATOM 1702 NH1 ARG A 291 64.376 -23.705 242.168 1.00165.16 N
ANISOU 1702 NH1 ARG A 291 17161 25168 20425 7717 -6374 -5205 N
ATOM 1703 NH2 ARG A 291 63.712 -25.812 242.787 1.00168.53 N
ANISOU 1703 NH2 ARG A 291 18642 25245 20148 8446 -6502 -4876 N
ATOM 1704 N ALA A 292 59.668 -20.809 236.179 1.00103.89 N
ANISOU 1704 N ALA A 292 9142 16436 13896 4939 -4186 -3814 N
ATOM 1705 CA ALA A 292 59.289 -19.570 235.507 1.00104.98 C
ANISOU 1705 CA ALA A 292 9028 16537 14325 4418 -3918 -3802 C
ATOM 1706 C ALA A 292 57.891 -19.678 234.904 1.00104.77 C
ANISOU 1706 C ALA A 292 9354 16223 14230 4200 -3655 -3423 C
ATOM 1707 O ALA A 292 57.093 -18.729 234.971 1.00105.78 O
ANISOU 1707 O ALA A 292 9524 16256 14411 3878 -3536 -3344 O
ATOM 1708 CB ALA A 292 60.318 -19.225 234.428 1.00106.56 C
ANISOU 1708 CB ALA A 292 8710 16889 14890 4221 -3748 -4009 C
ATOM 1709 N ARG A 293 57.564 -20.845 234.339 1.00101.49 N
ANISOU 1709 N ARG A 293 9207 15670 13684 4387 -3567 -3191 N
ATOM 1710 CA ARG A 293 56.244 -21.047 233.756 1.00 91.48 C
ANISOU 1710 CA ARG A 293 8274 14142 12341 4207 -3328 -2847 C
ATOM 1711 C ARG A 293 55.160 -21.037 234.822 1.00 94.11 C
ANISOU 1711 C ARG A 293 9054 14332 12371 4275 -3437 -2704 C
ATOM 1712 O ARG A 293 54.055 -20.552 234.577 1.00 98.38 O
ANISOU 1712 O ARG A 293 9739 14714 12926 4000 -3263 -2514 O
ATOM 1713 CB ARG A 293 56.208 -22.359 232.975 1.00 84.78 C
ANISOU 1713 CB ARG A 293 7627 13183 11403 4420 -3216 -2656 C
ATOM 1714 CG ARG A 293 56.850 -22.297 231.603 1.00 89.66 C
ANISOU 1714 CG ARG A 293 7866 13848 12350 4240 -2984 -2696 C
ATOM 1715 CD ARG A 293 56.860 -23.666 230.947 1.00 92.29 C
ANISOU 1715 CD ARG A 293 8427 14070 12568 4499 -2893 -2514 C
ATOM 1716 NE ARG A 293 57.200 -23.592 229.530 1.00 90.62 N
ANISOU 1716 NE ARG A 293 7925 13842 12666 4283 -2609 -2493 N
ATOM 1717 CZ ARG A 293 57.462 -24.651 228.771 1.00 94.33 C
ANISOU 1717 CZ ARG A 293 8475 14242 13126 4472 -2492 -2385 C
ATOM 1718 NH1 ARG A 293 57.764 -24.490 227.489 1.00 97.87 N
ANISOU 1718 NH1 ARG A 293 8656 14664 13867 4255 -2213 -2380 N
ATOM 1719 NH2 ARG A 293 57.425 -25.869 229.296 1.00 83.49 N
ANISOU 1719 NH2 ARG A 293 7480 12809 11434 4882 -2637 -2288 N
ATOM 1720 N ARG A 294 55.456 -21.558 236.015 1.00 90.05 N
ANISOU 1720 N ARG A 294 8773 13867 11575 4648 -3723 -2804 N
ATOM 1721 CA ARG A 294 54.472 -21.502 237.090 1.00 92.98 C
ANISOU 1721 CA ARG A 294 9581 14090 11655 4711 -3817 -2695 C
ATOM 1722 C ARG A 294 54.193 -20.064 237.487 1.00 95.22 C
ANISOU 1722 C ARG A 294 9646 14427 12106 4379 -3814 -2795 C
ATOM 1723 O ARG A 294 53.033 -19.674 237.667 1.00 92.75 O
ANISOU 1723 O ARG A 294 9574 13948 11720 4190 -3707 -2618 O
ATOM 1724 CB ARG A 294 54.955 -22.297 238.302 1.00103.37 C
ANISOU 1724 CB ARG A 294 11200 15442 12634 5190 -4124 -2814 C
ATOM 1725 CG ARG A 294 54.866 -23.800 238.152 1.00105.79 C
ANISOU 1725 CG ARG A 294 11936 15609 12649 5545 -4110 -2656 C
ATOM 1726 CD ARG A 294 55.273 -24.493 239.442 1.00106.78 C
ANISOU 1726 CD ARG A 294 12424 15742 12407 6023 -4411 -2783 C
ATOM 1727 NE ARG A 294 55.203 -25.946 239.332 1.00112.81 N
ANISOU 1727 NE ARG A 294 13656 16352 12854 6377 -4380 -2642 N
ATOM 1728 CZ ARG A 294 55.473 -26.781 240.330 1.00119.81 C
ANISOU 1728 CZ ARG A 294 14978 17185 13360 6832 -4595 -2714 C
ATOM 1729 NH1 ARG A 294 55.828 -26.303 241.516 1.00124.14 N
ANISOU 1729 NH1 ARG A 294 15534 17824 13809 6996 -4874 -2924 N
ATOM 1730 NH2 ARG A 294 55.386 -28.093 240.145 1.00118.99 N
ANISOU 1730 NH2 ARG A 294 15326 16923 12961 7129 -4523 -2579 N
ATOM 1731 N LYS A 295 55.240 -19.246 237.596 1.00 95.67 N
ANISOU 1731 N LYS A 295 9243 14713 12393 4293 -3916 -3087 N
ATOM 1732 CA LYS A 295 55.000 -17.848 237.944 1.00 96.08 C
ANISOU 1732 CA LYS A 295 9102 14807 12599 3964 -3889 -3188 C
ATOM 1733 C LYS A 295 54.128 -17.173 236.891 1.00 90.44 C
ANISOU 1733 C LYS A 295 8322 13951 12088 3533 -3558 -2996 C
ATOM 1734 O LYS A 295 53.093 -16.562 237.210 1.00 86.78 O
ANISOU 1734 O LYS A 295 8045 13358 11571 3345 -3489 -2867 O
ATOM 1735 CB LYS A 295 56.329 -17.106 238.117 1.00 98.60 C
ANISOU 1735 CB LYS A 295 8926 15398 13141 3922 -4016 -3554 C
ATOM 1736 CG LYS A 295 57.098 -17.508 239.367 1.00108.89 C
ANISOU 1736 CG LYS A 295 10283 16853 14235 4330 -4384 -3777 C
ATOM 1737 CD LYS A 295 58.021 -16.398 239.844 1.00114.11 C
ANISOU 1737 CD LYS A 295 10509 17756 15090 4198 -4512 -4129 C
ATOM 1738 CE LYS A 295 59.469 -16.671 239.482 1.00115.08 C
ANISOU 1738 CE LYS A 295 10200 18139 15388 4348 -4613 -4429 C
ATOM 1739 NZ LYS A 295 60.386 -15.718 240.176 1.00126.73 N
ANISOU 1739 NZ LYS A 295 11293 19865 16992 4289 -4793 -4806 N
ATOM 1740 N THR A 296 54.508 -17.312 235.616 1.00 95.37 N
ANISOU 1740 N THR A 296 8706 14591 12940 3390 -3350 -2973 N
ATOM 1741 CA THR A 296 53.769 -16.613 234.569 1.00 95.44 C
ANISOU 1741 CA THR A 296 8645 14469 13149 2989 -3039 -2818 C
ATOM 1742 C THR A 296 52.345 -17.147 234.426 1.00 93.35 C
ANISOU 1742 C THR A 296 8804 13970 12695 2989 -2931 -2485 C
ATOM 1743 O THR A 296 51.410 -16.378 234.168 1.00 88.41 O
ANISOU 1743 O THR A 296 8226 13229 12137 2701 -2771 -2364 O
ATOM 1744 CB THR A 296 54.519 -16.707 233.238 1.00 99.13 C
ANISOU 1744 CB THR A 296 8798 14985 13881 2858 -2837 -2874 C
ATOM 1745 OG1 THR A 296 53.766 -16.033 232.222 1.00105.42 O
ANISOU 1745 OG1 THR A 296 9577 15633 14844 2486 -2537 -2721 O
ATOM 1746 CG2 THR A 296 54.725 -18.160 232.829 1.00109.69 C
ANISOU 1746 CG2 THR A 296 10288 16291 15099 3173 -2860 -2750 C
ATOM 1747 N ALA A 297 52.150 -18.456 234.612 1.00 91.50 N
ANISOU 1747 N ALA A 297 8894 13661 12213 3316 -3013 -2346 N
ATOM 1748 CA ALA A 297 50.817 -19.032 234.473 1.00 75.22 C
ANISOU 1748 CA ALA A 297 7246 11376 9958 3321 -2897 -2052 C
ATOM 1749 C ALA A 297 49.915 -18.619 235.624 1.00 76.00 C
ANISOU 1749 C ALA A 297 7632 11392 9854 3322 -3004 -2012 C
ATOM 1750 O ALA A 297 48.720 -18.375 235.423 1.00 83.53 O
ANISOU 1750 O ALA A 297 8765 12194 10779 3140 -2859 -1826 O
ATOM 1751 CB ALA A 297 50.908 -20.557 234.385 1.00 70.37 C
ANISOU 1751 CB ALA A 297 6944 10687 9106 3671 -2932 -1932 C
ATOM 1752 N LYS A 298 50.461 -18.534 236.839 1.00 82.07 N
ANISOU 1752 N LYS A 298 8448 12257 10478 3536 -3260 -2193 N
ATOM 1753 CA LYS A 298 49.666 -18.034 237.951 1.00 84.65 C
ANISOU 1753 CA LYS A 298 9030 12503 10629 3522 -3357 -2176 C
ATOM 1754 C LYS A 298 49.217 -16.605 237.679 1.00 90.16 C
ANISOU 1754 C LYS A 298 9465 13216 11577 3116 -3223 -2199 C
ATOM 1755 O LYS A 298 48.043 -16.254 237.889 1.00 96.94 O
ANISOU 1755 O LYS A 298 10539 13932 12361 2978 -3142 -2053 O
ATOM 1756 CB LYS A 298 50.490 -18.125 239.239 1.00 96.03 C
ANISOU 1756 CB LYS A 298 10527 14060 11900 3823 -3662 -2397 C
ATOM 1757 CG LYS A 298 49.749 -17.805 240.524 1.00106.47 C
ANISOU 1757 CG LYS A 298 12194 15276 12985 3884 -3789 -2383 C
ATOM 1758 CD LYS A 298 50.677 -17.910 241.740 1.00122.64 C
ANISOU 1758 CD LYS A 298 14282 17445 14872 4201 -4104 -2617 C
ATOM 1759 CE LYS A 298 51.123 -19.349 241.999 1.00132.08 C
ANISOU 1759 CE LYS A 298 15804 18595 15787 4644 -4231 -2603 C
ATOM 1760 NZ LYS A 298 51.966 -19.472 243.229 1.00135.74 N
ANISOU 1760 NZ LYS A 298 16348 19162 16067 4988 -4556 -2833 N
ATOM 1761 N MET A 299 50.118 -15.787 237.125 1.00 86.11 N
ANISOU 1761 N MET A 299 8500 12860 11358 2914 -3171 -2381 N
ATOM 1762 CA MET A 299 49.747 -14.412 236.802 1.00 78.79 C
ANISOU 1762 CA MET A 299 7357 11925 10654 2525 -3013 -2410 C
ATOM 1763 C MET A 299 48.639 -14.373 235.752 1.00 78.83 C
ANISOU 1763 C MET A 299 7456 11758 10737 2297 -2746 -2160 C
ATOM 1764 O MET A 299 47.646 -13.648 235.899 1.00 76.14 O
ANISOU 1764 O MET A 299 7212 11317 10399 2104 -2665 -2072 O
ATOM 1765 CB MET A 299 50.981 -13.645 236.323 1.00 74.09 C
ANISOU 1765 CB MET A 299 6306 11506 10338 2356 -2971 -2664 C
ATOM 1766 CG MET A 299 50.754 -12.156 236.111 1.00 78.98 C
ANISOU 1766 CG MET A 299 6735 12114 11159 1971 -2810 -2739 C
ATOM 1767 SD MET A 299 52.207 -11.362 235.402 1.00 87.61 S
ANISOU 1767 SD MET A 299 7339 13384 12566 1760 -2702 -3045 S
ATOM 1768 CE MET A 299 52.231 -12.115 233.779 1.00 85.22 C
ANISOU 1768 CE MET A 299 6993 12990 12397 1705 -2452 -2880 C
ATOM 1769 N LEU A 300 48.795 -15.149 234.676 1.00 76.38 N
ANISOU 1769 N LEU A 300 7114 11416 10492 2326 -2613 -2053 N
ATOM 1770 CA LEU A 300 47.801 -15.128 233.606 1.00 69.62 C
ANISOU 1770 CA LEU A 300 6328 10406 9717 2117 -2366 -1830 C
ATOM 1771 C LEU A 300 46.448 -15.665 234.064 1.00 76.94 C
ANISOU 1771 C LEU A 300 7653 11176 10402 2213 -2381 -1617 C
ATOM 1772 O LEU A 300 45.402 -15.153 233.635 1.00 71.14 O
ANISOU 1772 O LEU A 300 6965 10335 9731 1995 -2230 -1486 O
ATOM 1773 CB LEU A 300 48.325 -15.911 232.401 1.00 64.42 C
ANISOU 1773 CB LEU A 300 5564 9748 9166 2153 -2233 -1774 C
ATOM 1774 CG LEU A 300 49.573 -15.319 231.732 1.00 69.31 C
ANISOU 1774 CG LEU A 300 5783 10499 10055 2006 -2155 -1985 C
ATOM 1775 CD1 LEU A 300 50.184 -16.306 230.753 1.00 66.96 C
ANISOU 1775 CD1 LEU A 300 5414 10210 9819 2125 -2067 -1945 C
ATOM 1776 CD2 LEU A 300 49.243 -14.002 231.028 1.00 64.04 C
ANISOU 1776 CD2 LEU A 300 4954 9771 9608 1614 -1933 -2001 C
ATOM 1777 N MET A 301 46.436 -16.673 234.941 1.00 80.13 N
ANISOU 1777 N MET A 301 8369 11557 10520 2539 -2555 -1590 N
ATOM 1778 CA MET A 301 45.165 -17.151 235.474 1.00 74.00 C
ANISOU 1778 CA MET A 301 8016 10615 9485 2626 -2555 -1413 C
ATOM 1779 C MET A 301 44.479 -16.069 236.299 1.00 73.45 C
ANISOU 1779 C MET A 301 7972 10525 9409 2473 -2604 -1460 C
ATOM 1780 O MET A 301 43.259 -15.876 236.190 1.00 71.47 O
ANISOU 1780 O MET A 301 7881 10153 9123 2348 -2498 -1317 O
ATOM 1781 CB MET A 301 45.381 -18.409 236.318 1.00 75.51 C
ANISOU 1781 CB MET A 301 8602 10753 9333 3012 -2711 -1397 C
ATOM 1782 CG MET A 301 45.954 -19.599 235.564 1.00 79.93 C
ANISOU 1782 CG MET A 301 9211 11307 9853 3198 -2656 -1334 C
ATOM 1783 SD MET A 301 46.344 -20.989 236.654 1.00 89.64 S
ANISOU 1783 SD MET A 301 10936 12465 10656 3670 -2840 -1351 S
ATOM 1784 CE MET A 301 47.030 -22.169 235.493 1.00 89.10 C
ANISOU 1784 CE MET A 301 10829 12404 10622 3817 -2729 -1279 C
ATOM 1785 N VAL A 302 45.250 -15.323 237.101 1.00 74.73 N
ANISOU 1785 N VAL A 302 7966 10812 9616 2477 -2762 -1670 N
ATOM 1786 CA VAL A 302 44.643 -14.221 237.847 1.00 70.79 C
ANISOU 1786 CA VAL A 302 7479 10293 9125 2316 -2797 -1723 C
ATOM 1787 C VAL A 302 44.061 -13.191 236.889 1.00 74.08 C
ANISOU 1787 C VAL A 302 7658 10679 9811 1953 -2571 -1669 C
ATOM 1788 O VAL A 302 42.967 -12.651 237.116 1.00 74.21 O
ANISOU 1788 O VAL A 302 7793 10599 9804 1825 -2518 -1593 O
ATOM 1789 CB VAL A 302 45.670 -13.572 238.790 1.00 69.36 C
ANISOU 1789 CB VAL A 302 7132 10262 8961 2369 -2996 -1973 C
ATOM 1790 CG1 VAL A 302 45.051 -12.354 239.454 1.00 59.64 C
ANISOU 1790 CG1 VAL A 302 5899 9004 7758 2168 -3006 -2029 C
ATOM 1791 CG2 VAL A 302 46.159 -14.567 239.830 1.00 59.22 C
ANISOU 1791 CG2 VAL A 302 6132 8987 7381 2756 -3235 -2029 C
ATOM 1792 N VAL A 303 44.774 -12.912 235.795 1.00 69.49 N
ANISOU 1792 N VAL A 303 6762 10163 9477 1793 -2430 -1712 N
ATOM 1793 CA VAL A 303 44.297 -11.899 234.859 1.00 65.88 C
ANISOU 1793 CA VAL A 303 6127 9650 9255 1460 -2203 -1668 C
ATOM 1794 C VAL A 303 42.980 -12.334 234.239 1.00 63.72 C
ANISOU 1794 C VAL A 303 6045 9227 8939 1417 -2065 -1434 C
ATOM 1795 O VAL A 303 42.030 -11.546 234.142 1.00 71.43 O
ANISOU 1795 O VAL A 303 7037 10121 9980 1229 -1966 -1378 O
ATOM 1796 CB VAL A 303 45.361 -11.620 233.782 1.00 66.69 C
ANISOU 1796 CB VAL A 303 5921 9824 9593 1317 -2066 -1764 C
ATOM 1797 CG1 VAL A 303 44.832 -10.623 232.764 1.00 63.11 C
ANISOU 1797 CG1 VAL A 303 5367 9272 9341 995 -1815 -1705 C
ATOM 1798 CG2 VAL A 303 46.641 -11.105 234.420 1.00 68.86 C
ANISOU 1798 CG2 VAL A 303 5974 10262 9926 1340 -2199 -2031 C
ATOM 1799 N VAL A 304 42.894 -13.602 233.832 1.00 64.62 N
ANISOU 1799 N VAL A 304 6311 9304 8937 1601 -2060 -1304 N
ATOM 1800 CA VAL A 304 41.672 -14.087 233.197 1.00 59.22 C
ANISOU 1800 CA VAL A 304 5801 8489 8210 1564 -1930 -1098 C
ATOM 1801 C VAL A 304 40.513 -14.076 234.184 1.00 62.98 C
ANISOU 1801 C VAL A 304 6579 8870 8481 1608 -1982 -1030 C
ATOM 1802 O VAL A 304 39.380 -13.723 233.830 1.00 68.49 O
ANISOU 1802 O VAL A 304 7379 9439 9205 1388 -1774 -894 O
ATOM 1803 CB VAL A 304 41.893 -15.492 232.613 1.00 55.19 C
ANISOU 1803 CB VAL A 304 5429 7950 7591 1764 -1906 -985 C
ATOM 1804 CG1 VAL A 304 40.613 -15.991 231.956 1.00 55.78 C
ANISOU 1804 CG1 VAL A 304 5742 7860 7591 1657 -1704 -761 C
ATOM 1805 CG2 VAL A 304 43.047 -15.479 231.626 1.00 62.18 C
ANISOU 1805 CG2 VAL A 304 6029 8915 8684 1697 -1821 -1055 C
ATOM 1806 N LEU A 305 40.775 -14.439 235.442 1.00 70.04 N
ANISOU 1806 N LEU A 305 7678 9793 9143 1851 -2201 -1111 N
ATOM 1807 CA LEU A 305 39.700 -14.457 236.430 1.00 68.67 C
ANISOU 1807 CA LEU A 305 7889 9468 8734 1833 -2155 -1031 C
ATOM 1808 C LEU A 305 39.175 -13.050 236.697 1.00 71.13 C
ANISOU 1808 C LEU A 305 8058 9769 9199 1572 -2087 -1091 C
ATOM 1809 O LEU A 305 37.958 -12.822 236.746 1.00 69.28 O
ANISOU 1809 O LEU A 305 8002 9392 8928 1403 -1889 -972 O
ATOM 1810 CB LEU A 305 40.196 -15.100 237.723 1.00 74.23 C
ANISOU 1810 CB LEU A 305 8884 10186 9133 2166 -2415 -1118 C
ATOM 1811 CG LEU A 305 39.252 -15.010 238.921 1.00 80.92 C
ANISOU 1811 CG LEU A 305 10149 10872 9725 2152 -2381 -1083 C
ATOM 1812 CD1 LEU A 305 38.035 -15.901 238.716 1.00 79.68 C
ANISOU 1812 CD1 LEU A 305 10394 10496 9387 2075 -2098 -877 C
ATOM 1813 CD2 LEU A 305 39.990 -15.406 240.183 1.00 77.20 C
ANISOU 1813 CD2 LEU A 305 9921 10439 8973 2494 -2695 -1213 C
ATOM 1814 N VAL A 306 40.083 -12.089 236.885 1.00 72.71 N
ANISOU 1814 N VAL A 306 7933 10121 9572 1535 -2240 -1293 N
ATOM 1815 CA VAL A 306 39.628 -10.727 237.133 1.00 68.48 C
ANISOU 1815 CA VAL A 306 7297 9556 9168 1289 -2156 -1353 C
ATOM 1816 C VAL A 306 38.905 -10.177 235.912 1.00 65.43 C
ANISOU 1816 C VAL A 306 6785 9080 8994 1025 -1879 -1223 C
ATOM 1817 O VAL A 306 37.951 -9.403 236.046 1.00 56.76 O
ANISOU 1817 O VAL A 306 5767 7875 7923 859 -1735 -1167 O
ATOM 1818 CB VAL A 306 40.799 -9.825 237.554 1.00 63.49 C
ANISOU 1818 CB VAL A 306 6367 9093 8666 1264 -2335 -1611 C
ATOM 1819 CG1 VAL A 306 40.307 -8.404 237.779 1.00 63.92 C
ANISOU 1819 CG1 VAL A 306 6348 9094 8843 1006 -2234 -1676 C
ATOM 1820 CG2 VAL A 306 41.456 -10.365 238.812 1.00 60.91 C
ANISOU 1820 CG2 VAL A 306 6221 8829 8091 1528 -2590 -1720 C
ATOM 1821 N PHE A 307 39.312 -10.579 234.708 1.00 64.75 N
ANISOU 1821 N PHE A 307 6528 9028 9047 1002 -1800 -1173 N
ATOM 1822 CA PHE A 307 38.575 -10.154 233.523 1.00 57.19 C
ANISOU 1822 CA PHE A 307 5515 7968 8245 785 -1555 -1036 C
ATOM 1823 C PHE A 307 37.151 -10.692 233.553 1.00 58.64 C
ANISOU 1823 C PHE A 307 5992 8013 8277 767 -1415 -839 C
ATOM 1824 O PHE A 307 36.182 -9.948 233.339 1.00 54.57 O
ANISOU 1824 O PHE A 307 5496 7413 7827 609 -1271 -775 O
ATOM 1825 CB PHE A 307 39.300 -10.627 232.263 1.00 55.23 C
ANISOU 1825 CB PHE A 307 5083 7764 8137 778 -1497 -1017 C
ATOM 1826 CG PHE A 307 38.708 -10.100 230.984 1.00 55.89 C
ANISOU 1826 CG PHE A 307 5119 7740 8376 563 -1270 -900 C
ATOM 1827 CD1 PHE A 307 37.630 -10.731 230.386 1.00 56.99 C
ANISOU 1827 CD1 PHE A 307 5451 7773 8428 540 -1139 -695 C
ATOM 1828 CD2 PHE A 307 39.235 -8.972 230.377 1.00 60.68 C
ANISOU 1828 CD2 PHE A 307 5511 8346 9198 383 -1184 -1010 C
ATOM 1829 CE1 PHE A 307 37.090 -10.244 229.212 1.00 49.17 C
ANISOU 1829 CE1 PHE A 307 4431 6693 7557 375 -970 -597 C
ATOM 1830 CE2 PHE A 307 38.696 -8.481 229.202 1.00 48.84 C
ANISOU 1830 CE2 PHE A 307 4033 6721 7803 217 -985 -899 C
ATOM 1831 CZ PHE A 307 37.624 -9.116 228.623 1.00 46.46 C
ANISOU 1831 CZ PHE A 307 3916 6329 7407 231 -899 -690 C
ATOM 1832 N ALA A 308 37.005 -11.992 233.821 1.00 56.30 N
ANISOU 1832 N ALA A 308 5929 7692 7771 931 -1445 -757 N
ATOM 1833 CA ALA A 308 35.673 -12.585 233.816 1.00 47.98 C
ANISOU 1833 CA ALA A 308 5143 6512 6575 878 -1278 -604 C
ATOM 1834 C ALA A 308 34.789 -11.938 234.871 1.00 52.80 C
ANISOU 1834 C ALA A 308 5899 7055 7110 816 -1242 -636 C
ATOM 1835 O ALA A 308 33.604 -11.677 234.625 1.00 62.50 O
ANISOU 1835 O ALA A 308 7168 8209 8371 673 -1068 -561 O
ATOM 1836 CB ALA A 308 35.770 -14.095 234.049 1.00 43.58 C
ANISOU 1836 CB ALA A 308 4871 5915 5771 1060 -1297 -536 C
ATOM 1837 N LEU A 309 35.367 -11.606 236.029 1.00 57.45 N
ANISOU 1837 N LEU A 309 6543 7675 7609 923 -1411 -767 N
ATOM 1838 CA LEU A 309 34.579 -10.977 237.085 1.00 62.65 C
ANISOU 1838 CA LEU A 309 7367 8252 8186 863 -1366 -805 C
ATOM 1839 C LEU A 309 34.186 -9.554 236.707 1.00 53.42 C
ANISOU 1839 C LEU A 309 5968 7080 7248 669 -1270 -832 C
ATOM 1840 O LEU A 309 33.020 -9.167 236.842 1.00 61.23 O
ANISOU 1840 O LEU A 309 7039 7979 8245 564 -1107 -781 O
ATOM 1841 CB LEU A 309 35.357 -10.993 238.400 1.00 72.97 C
ANISOU 1841 CB LEU A 309 8821 9589 9315 1036 -1590 -943 C
ATOM 1842 CG LEU A 309 35.370 -12.334 239.129 1.00 73.79 C
ANISOU 1842 CG LEU A 309 9322 9619 9098 1252 -1650 -906 C
ATOM 1843 CD1 LEU A 309 36.291 -12.279 240.335 1.00 70.84 C
ANISOU 1843 CD1 LEU A 309 9072 9296 8547 1464 -1931 -1057 C
ATOM 1844 CD2 LEU A 309 33.959 -12.702 239.558 1.00 72.05 C
ANISOU 1844 CD2 LEU A 309 9439 9216 8720 1150 -1403 -813 C
ATOM 1845 N CYS A 310 35.142 -8.764 236.207 1.00 53.68 N
ANISOU 1845 N CYS A 310 5721 7205 7471 622 -1353 -923 N
ATOM 1846 CA CYS A 310 34.843 -7.377 235.868 1.00 51.22 C
ANISOU 1846 CA CYS A 310 5256 6859 7348 448 -1247 -955 C
ATOM 1847 C CYS A 310 33.821 -7.270 234.746 1.00 54.73 C
ANISOU 1847 C CYS A 310 5668 7231 7898 347 -1052 -805 C
ATOM 1848 O CYS A 310 33.047 -6.305 234.708 1.00 55.76 O
ANISOU 1848 O CYS A 310 5793 7288 8105 256 -938 -792 O
ATOM 1849 CB CYS A 310 36.125 -6.638 235.474 1.00 52.84 C
ANISOU 1849 CB CYS A 310 5194 7158 7724 388 -1332 -1102 C
ATOM 1850 SG CYS A 310 37.285 -6.337 236.820 1.00 68.52 S
ANISOU 1850 SG CYS A 310 7141 9263 9629 468 -1581 -1343 S
ATOM 1851 N TYR A 311 33.801 -8.233 233.821 1.00 52.01 N
ANISOU 1851 N TYR A 311 5309 6905 7549 376 -1019 -698 N
ATOM 1852 CA TYR A 311 32.897 -8.143 232.679 1.00 45.04 C
ANISOU 1852 CA TYR A 311 4385 5971 6758 288 -868 -573 C
ATOM 1853 C TYR A 311 31.602 -8.927 232.854 1.00 49.88 C
ANISOU 1853 C TYR A 311 5160 6545 7246 292 -766 -482 C
ATOM 1854 O TYR A 311 30.691 -8.771 232.034 1.00 56.04 O
ANISOU 1854 O TYR A 311 5889 7305 8098 226 -661 -405 O
ATOM 1855 CB TYR A 311 33.607 -8.613 231.401 1.00 45.31 C
ANISOU 1855 CB TYR A 311 4300 6038 6878 277 -866 -520 C
ATOM 1856 CG TYR A 311 34.519 -7.572 230.776 1.00 48.72 C
ANISOU 1856 CG TYR A 311 4550 6470 7492 191 -861 -603 C
ATOM 1857 CD1 TYR A 311 35.820 -7.394 231.229 1.00 50.02 C
ANISOU 1857 CD1 TYR A 311 4591 6716 7700 212 -972 -760 C
ATOM 1858 CD2 TYR A 311 34.077 -6.772 229.728 1.00 50.93 C
ANISOU 1858 CD2 TYR A 311 4798 6665 7890 90 -738 -542 C
ATOM 1859 CE1 TYR A 311 36.657 -6.441 230.658 1.00 48.14 C
ANISOU 1859 CE1 TYR A 311 4185 6473 7634 90 -922 -871 C
ATOM 1860 CE2 TYR A 311 34.905 -5.826 229.147 1.00 52.02 C
ANISOU 1860 CE2 TYR A 311 4832 6764 8171 -11 -685 -626 C
ATOM 1861 CZ TYR A 311 36.195 -5.664 229.616 1.00 56.37 C
ANISOU 1861 CZ TYR A 311 5246 7394 8778 -32 -759 -799 C
ATOM 1862 OH TYR A 311 37.016 -4.718 229.043 1.00 59.61 O
ANISOU 1862 OH TYR A 311 5553 7760 9337 -175 -665 -916 O
ATOM 1863 N LEU A 312 31.493 -9.775 233.878 1.00 48.98 N
ANISOU 1863 N LEU A 312 5252 6418 6939 367 -789 -503 N
ATOM 1864 CA LEU A 312 30.243 -10.507 234.071 1.00 48.26 C
ANISOU 1864 CA LEU A 312 5327 6277 6732 326 -641 -450 C
ATOM 1865 C LEU A 312 29.039 -9.595 234.269 1.00 48.85 C
ANISOU 1865 C LEU A 312 5346 6319 6895 237 -519 -474 C
ATOM 1866 O LEU A 312 28.012 -9.810 233.600 1.00 53.49 O
ANISOU 1866 O LEU A 312 5874 6920 7529 166 -401 -428 O
ATOM 1867 CB LEU A 312 30.399 -11.476 235.247 1.00 57.53 C
ANISOU 1867 CB LEU A 312 6805 7399 7653 420 -661 -486 C
ATOM 1868 CG LEU A 312 29.181 -12.349 235.548 1.00 62.42 C
ANISOU 1868 CG LEU A 312 7651 7942 8124 346 -460 -462 C
ATOM 1869 CD1 LEU A 312 28.941 -13.329 234.415 1.00 55.91 C
ANISOU 1869 CD1 LEU A 312 6805 7144 7294 293 -377 -370 C
ATOM 1870 CD2 LEU A 312 29.365 -13.072 236.872 1.00 67.86 C
ANISOU 1870 CD2 LEU A 312 8717 8531 8538 444 -464 -512 C
ATOM 1871 N PRO A 313 29.067 -8.602 235.164 1.00 49.31 N
ANISOU 1871 N PRO A 313 5418 6340 6976 244 -541 -557 N
ATOM 1872 CA PRO A 313 27.832 -7.827 235.404 1.00 47.27 C
ANISOU 1872 CA PRO A 313 5126 6042 6791 183 -402 -583 C
ATOM 1873 C PRO A 313 27.286 -7.138 234.163 1.00 54.86 C
ANISOU 1873 C PRO A 313 5868 7038 7940 154 -365 -528 C
ATOM 1874 O PRO A 313 26.088 -7.256 233.873 1.00 56.88 O
ANISOU 1874 O PRO A 313 6068 7314 8231 124 -253 -521 O
ATOM 1875 CB PRO A 313 28.260 -6.818 236.484 1.00 46.63 C
ANISOU 1875 CB PRO A 313 5110 5907 6701 203 -453 -677 C
ATOM 1876 CG PRO A 313 29.420 -7.476 237.184 1.00 44.69 C
ANISOU 1876 CG PRO A 313 5011 5673 6295 278 -606 -718 C
ATOM 1877 CD PRO A 313 30.146 -8.240 236.104 1.00 45.44 C
ANISOU 1877 CD PRO A 313 4997 5847 6423 312 -688 -647 C
ATOM 1878 N ILE A 314 28.127 -6.430 233.408 1.00 51.36 N
ANISOU 1878 N ILE A 314 5308 6599 7609 166 -452 -504 N
ATOM 1879 CA ILE A 314 27.611 -5.708 232.246 1.00 49.94 C
ANISOU 1879 CA ILE A 314 4993 6414 7568 165 -418 -448 C
ATOM 1880 C ILE A 314 27.138 -6.686 231.177 1.00 50.61 C
ANISOU 1880 C ILE A 314 5025 6561 7643 150 -404 -364 C
ATOM 1881 O ILE A 314 26.117 -6.455 230.515 1.00 58.38 O
ANISOU 1881 O ILE A 314 5924 7570 8688 164 -363 -339 O
ATOM 1882 CB ILE A 314 28.674 -4.737 231.699 1.00 51.35 C
ANISOU 1882 CB ILE A 314 5123 6545 7844 154 -472 -456 C
ATOM 1883 CG1 ILE A 314 28.080 -3.852 230.602 1.00 46.76 C
ANISOU 1883 CG1 ILE A 314 4491 5909 7365 181 -424 -399 C
ATOM 1884 CG2 ILE A 314 29.884 -5.504 231.161 1.00 36.70 C
ANISOU 1884 CG2 ILE A 314 3238 4732 5975 132 -550 -437 C
ATOM 1885 CD1 ILE A 314 26.981 -2.918 231.091 1.00 57.80 C
ANISOU 1885 CD1 ILE A 314 5904 7261 8795 241 -354 -432 C
ATOM 1886 N SER A 315 27.846 -7.809 231.010 1.00 51.48 N
ANISOU 1886 N SER A 315 5191 6702 7667 134 -444 -329 N
ATOM 1887 CA SER A 315 27.439 -8.782 229.998 1.00 47.26 C
ANISOU 1887 CA SER A 315 4636 6214 7106 101 -416 -251 C
ATOM 1888 C SER A 315 26.084 -9.391 230.333 1.00 50.44 C
ANISOU 1888 C SER A 315 5058 6660 7448 51 -306 -285 C
ATOM 1889 O SER A 315 25.207 -9.505 229.457 1.00 59.20 O
ANISOU 1889 O SER A 315 6062 7827 8605 21 -278 -265 O
ATOM 1890 CB SER A 315 28.508 -9.870 229.859 1.00 50.98 C
ANISOU 1890 CB SER A 315 5195 6693 7484 108 -462 -213 C
ATOM 1891 OG SER A 315 29.743 -9.314 229.424 1.00 54.90 O
ANISOU 1891 OG SER A 315 5619 7171 8069 133 -544 -212 O
ATOM 1892 N VAL A 316 25.875 -9.746 231.606 1.00 53.86 N
ANISOU 1892 N VAL A 316 5628 7064 7772 37 -237 -358 N
ATOM 1893 CA VAL A 316 24.592 -10.315 232.006 1.00 52.90 C
ANISOU 1893 CA VAL A 316 5535 6968 7596 -46 -80 -426 C
ATOM 1894 C VAL A 316 23.483 -9.275 231.904 1.00 43.84 C
ANISOU 1894 C VAL A 316 4193 5865 6600 -34 -39 -489 C
ATOM 1895 O VAL A 316 22.369 -9.580 231.459 1.00 50.94 O
ANISOU 1895 O VAL A 316 4964 6850 7540 -93 41 -539 O
ATOM 1896 CB VAL A 316 24.685 -10.896 233.428 1.00 56.77 C
ANISOU 1896 CB VAL A 316 6284 7375 7909 -64 10 -493 C
ATOM 1897 CG1 VAL A 316 23.310 -11.345 233.908 1.00 49.09 C
ANISOU 1897 CG1 VAL A 316 5346 6408 6898 -186 227 -599 C
ATOM 1898 CG2 VAL A 316 25.676 -12.046 233.467 1.00 49.60 C
ANISOU 1898 CG2 VAL A 316 5592 6427 6826 -32 -38 -433 C
ATOM 1899 N LEU A 317 23.758 -8.034 232.321 1.00 45.80 N
ANISOU 1899 N LEU A 317 4412 6059 6930 48 -91 -504 N
ATOM 1900 CA LEU A 317 22.720 -7.008 232.264 1.00 49.17 C
ANISOU 1900 CA LEU A 317 4681 6512 7489 100 -49 -562 C
ATOM 1901 C LEU A 317 22.326 -6.710 230.826 1.00 55.48 C
ANISOU 1901 C LEU A 317 5301 7387 8393 162 -135 -506 C
ATOM 1902 O LEU A 317 21.150 -6.472 230.532 1.00 65.03 O
ANISOU 1902 O LEU A 317 6345 8683 9681 200 -103 -572 O
ATOM 1903 CB LEU A 317 23.185 -5.731 232.960 1.00 53.82 C
ANISOU 1903 CB LEU A 317 5326 7001 8122 173 -74 -581 C
ATOM 1904 CG LEU A 317 23.259 -5.712 234.484 1.00 57.00 C
ANISOU 1904 CG LEU A 317 5902 7324 8432 135 15 -665 C
ATOM 1905 CD1 LEU A 317 23.917 -4.429 234.955 1.00 48.74 C
ANISOU 1905 CD1 LEU A 317 4910 6184 7427 191 -37 -675 C
ATOM 1906 CD2 LEU A 317 21.880 -5.861 235.106 1.00 50.22 C
ANISOU 1906 CD2 LEU A 317 5006 6487 7588 93 198 -775 C
ATOM 1907 N ASN A 318 23.287 -6.751 229.901 1.00 57.62 N
ANISOU 1907 N ASN A 318 5605 7629 8658 179 -246 -398 N
ATOM 1908 CA ASN A 318 22.919 -6.486 228.517 1.00 59.53 C
ANISOU 1908 CA ASN A 318 5739 7916 8965 243 -329 -340 C
ATOM 1909 C ASN A 318 22.177 -7.654 227.896 1.00 54.64 C
ANISOU 1909 C ASN A 318 5035 7422 8304 162 -312 -355 C
ATOM 1910 O ASN A 318 21.280 -7.441 227.076 1.00 51.88 O
ANISOU 1910 O ASN A 318 4541 7162 8011 224 -367 -376 O
ATOM 1911 CB ASN A 318 24.144 -6.115 227.691 1.00 52.93 C
ANISOU 1911 CB ASN A 318 4992 6985 8135 265 -413 -235 C
ATOM 1912 CG ASN A 318 24.350 -4.614 227.628 1.00 87.37 C
ANISOU 1912 CG ASN A 318 9391 11235 12570 370 -432 -232 C
ATOM 1913 OD1 ASN A 318 23.822 -3.941 226.744 1.00103.17 O
ANISOU 1913 OD1 ASN A 318 11390 13205 14605 472 -483 -189 O
ATOM 1914 ND2 ASN A 318 25.106 -4.075 228.582 1.00 93.95 N
ANISOU 1914 ND2 ASN A 318 10293 11997 13408 350 -389 -284 N
ATOM 1915 N VAL A 319 22.495 -8.889 228.285 1.00 49.26 N
ANISOU 1915 N VAL A 319 4455 6749 7512 33 -237 -356 N
ATOM 1916 CA VAL A 319 21.655 -9.988 227.818 1.00 51.34 C
ANISOU 1916 CA VAL A 319 4654 7125 7727 -80 -176 -402 C
ATOM 1917 C VAL A 319 20.236 -9.832 228.356 1.00 54.26 C
ANISOU 1917 C VAL A 319 4854 7601 8161 -108 -74 -566 C
ATOM 1918 O VAL A 319 19.255 -9.993 227.618 1.00 59.32 O
ANISOU 1918 O VAL A 319 5301 8382 8855 -124 -96 -638 O
ATOM 1919 CB VAL A 319 22.264 -11.346 228.206 1.00 48.88 C
ANISOU 1919 CB VAL A 319 4547 6768 7256 -207 -81 -376 C
ATOM 1920 CG1 VAL A 319 21.226 -12.432 228.054 1.00 43.13 C
ANISOU 1920 CG1 VAL A 319 3785 6138 6465 -368 53 -472 C
ATOM 1921 CG2 VAL A 319 23.461 -11.641 227.324 1.00 45.21 C
ANISOU 1921 CG2 VAL A 319 4177 6246 6754 -178 -183 -235 C
ATOM 1922 N LEU A 320 20.102 -9.489 229.641 1.00 51.77 N
ANISOU 1922 N LEU A 320 4598 7227 7847 -112 38 -644 N
ATOM 1923 CA LEU A 320 18.770 -9.379 230.232 1.00 58.70 C
ANISOU 1923 CA LEU A 320 5314 8194 8794 -156 178 -823 C
ATOM 1924 C LEU A 320 17.978 -8.244 229.601 1.00 65.33 C
ANISOU 1924 C LEU A 320 5890 9134 9800 18 63 -865 C
ATOM 1925 O LEU A 320 16.766 -8.363 229.386 1.00 69.35 O
ANISOU 1925 O LEU A 320 6154 9804 10393 -1 106 -1017 O
ATOM 1926 CB LEU A 320 18.881 -9.156 231.740 1.00 65.68 C
ANISOU 1926 CB LEU A 320 6365 8958 9632 -184 327 -886 C
ATOM 1927 CG LEU A 320 19.495 -10.245 232.615 1.00 63.43 C
ANISOU 1927 CG LEU A 320 6392 8557 9150 -319 456 -876 C
ATOM 1928 CD1 LEU A 320 19.498 -9.791 234.064 1.00 55.55 C
ANISOU 1928 CD1 LEU A 320 5564 7436 8109 -313 575 -947 C
ATOM 1929 CD2 LEU A 320 18.727 -11.552 232.471 1.00 63.01 C
ANISOU 1929 CD2 LEU A 320 6353 8572 9016 -519 637 -979 C
ATOM 1930 N LYS A 321 18.649 -7.135 229.292 1.00 53.72 N
ANISOU 1930 N LYS A 321 4472 7568 8372 194 -80 -748 N
ATOM 1931 CA LYS A 321 17.962 -5.995 228.700 1.00 57.05 C
ANISOU 1931 CA LYS A 321 4719 8043 8914 404 -192 -772 C
ATOM 1932 C LYS A 321 17.605 -6.266 227.243 1.00 56.63 C
ANISOU 1932 C LYS A 321 4539 8112 8867 463 -354 -742 C
ATOM 1933 O LYS A 321 16.443 -6.141 226.844 1.00 59.94 O
ANISOU 1933 O LYS A 321 4757 8684 9335 541 -397 -845 O
ATOM 1934 CB LYS A 321 18.845 -4.752 228.829 1.00 57.85 C
ANISOU 1934 CB LYS A 321 4989 7965 9024 547 -255 -661 C
ATOM 1935 CG LYS A 321 18.338 -3.522 228.110 1.00 62.37 C
ANISOU 1935 CG LYS A 321 5489 8533 9675 797 -373 -649 C
ATOM 1936 CD LYS A 321 19.425 -2.448 228.062 1.00 60.05 C
ANISOU 1936 CD LYS A 321 5435 8027 9355 879 -404 -528 C
ATOM 1937 CE LYS A 321 18.914 -1.194 227.372 1.00 73.81 C
ANISOU 1937 CE LYS A 321 7188 9719 11137 1148 -497 -510 C
ATOM 1938 NZ LYS A 321 19.936 -0.111 227.362 1.00 94.02 N
ANISOU 1938 NZ LYS A 321 10018 12046 13659 1194 -474 -415 N
ATOM 1939 N ARG A 322 18.582 -6.702 226.445 1.00 59.74 N
ANISOU 1939 N ARG A 322 5092 8433 9174 414 -436 -593 N
ATOM 1940 CA ARG A 322 18.377 -6.777 225.005 1.00 51.99 C
ANISOU 1940 CA ARG A 322 4057 7519 8176 493 -604 -540 C
ATOM 1941 C ARG A 322 17.699 -8.068 224.575 1.00 52.27 C
ANISOU 1941 C ARG A 322 3956 7733 8174 324 -581 -629 C
ATOM 1942 O ARG A 322 16.950 -8.068 223.592 1.00 58.52 O
ANISOU 1942 O ARG A 322 4666 8634 8935 392 -701 -642 O
ATOM 1943 CB ARG A 322 19.710 -6.633 224.280 1.00 54.06 C
ANISOU 1943 CB ARG A 322 4565 7609 8367 502 -671 -354 C
ATOM 1944 CG ARG A 322 20.381 -5.284 224.452 1.00 48.75 C
ANISOU 1944 CG ARG A 322 4041 6756 7726 650 -690 -282 C
ATOM 1945 CD ARG A 322 19.577 -4.167 223.806 1.00 47.07 C
ANISOU 1945 CD ARG A 322 3781 6548 7554 905 -814 -299 C
ATOM 1946 NE ARG A 322 20.311 -2.906 223.863 1.00 54.98 N
ANISOU 1946 NE ARG A 322 4999 7336 8555 1022 -798 -222 N
ATOM 1947 CZ ARG A 322 19.852 -1.745 223.404 1.00 55.84 C
ANISOU 1947 CZ ARG A 322 5178 7372 8668 1270 -876 -212 C
ATOM 1948 NH1 ARG A 322 18.652 -1.670 222.845 1.00 55.33 N
ANISOU 1948 NH1 ARG A 322 4951 7455 8617 1463 -1014 -279 N
ATOM 1949 NH2 ARG A 322 20.599 -0.654 223.500 1.00 56.78 N
ANISOU 1949 NH2 ARG A 322 5540 7267 8767 1331 -815 -150 N
ATOM 1950 N VAL A 323 17.936 -9.168 225.282 1.00 48.84 N
ANISOU 1950 N VAL A 323 3595 7292 7671 96 -408 -663 N
ATOM 1951 CA VAL A 323 17.384 -10.460 224.894 1.00 50.86 C
ANISOU 1951 CA VAL A 323 3778 7684 7865 -105 -342 -750 C
ATOM 1952 C VAL A 323 16.117 -10.802 225.669 1.00 58.11 C
ANISOU 1952 C VAL A 323 4531 8732 8817 -222 -175 -963 C
ATOM 1953 O VAL A 323 15.203 -11.415 225.118 1.00 60.64 O
ANISOU 1953 O VAL A 323 4747 9185 9107 -317 -170 -1059 O
ATOM 1954 CB VAL A 323 18.454 -11.558 225.053 1.00 52.73 C
ANISOU 1954 CB VAL A 323 4292 7790 7952 -278 -233 -635 C
ATOM 1955 CG1 VAL A 323 17.875 -12.904 224.698 1.00 54.30 C
ANISOU 1955 CG1 VAL A 323 4467 8101 8065 -505 -125 -730 C
ATOM 1956 CG2 VAL A 323 19.630 -11.243 224.159 1.00 40.61 C
ANISOU 1956 CG2 VAL A 323 2922 6127 6381 -174 -380 -433 C
ATOM 1957 N PHE A 324 16.027 -10.417 226.940 1.00 64.54 N
ANISOU 1957 N PHE A 324 5340 9494 9690 -226 -26 -1048 N
ATOM 1958 CA PHE A 324 14.858 -10.748 227.746 1.00 56.38 C
ANISOU 1958 CA PHE A 324 4192 8547 8681 -357 176 -1259 C
ATOM 1959 C PHE A 324 13.949 -9.559 228.021 1.00 64.66 C
ANISOU 1959 C PHE A 324 5071 9646 9851 -159 128 -1338 C
ATOM 1960 O PHE A 324 12.936 -9.720 228.711 1.00 67.74 O
ANISOU 1960 O PHE A 324 5347 10105 10285 -254 299 -1529 O
ATOM 1961 CB PHE A 324 15.296 -11.400 229.063 1.00 59.06 C
ANISOU 1961 CB PHE A 324 4722 8765 8952 -552 444 -1318 C
ATOM 1962 CG PHE A 324 15.932 -12.749 228.874 1.00 66.60 C
ANISOU 1962 CG PHE A 324 5942 9644 9719 -750 534 -1241 C
ATOM 1963 CD1 PHE A 324 17.303 -12.869 228.761 1.00 60.89 C
ANISOU 1963 CD1 PHE A 324 5505 8753 8877 -678 434 -1017 C
ATOM 1964 CD2 PHE A 324 15.154 -13.890 228.772 1.00 70.42 C
ANISOU 1964 CD2 PHE A 324 6382 10227 10146 -1007 726 -1410 C
ATOM 1965 CE1 PHE A 324 17.892 -14.104 228.570 1.00 64.68 C
ANISOU 1965 CE1 PHE A 324 6235 9159 9180 -822 514 -946 C
ATOM 1966 CE2 PHE A 324 15.736 -15.129 228.581 1.00 68.48 C
ANISOU 1966 CE2 PHE A 324 6425 9889 9706 -1178 825 -1333 C
ATOM 1967 CZ PHE A 324 17.107 -15.236 228.481 1.00 64.11 C
ANISOU 1967 CZ PHE A 324 6166 9161 9031 -1065 712 -1092 C
ATOM 1968 N GLY A 325 14.277 -8.374 227.513 1.00 63.36 N
ANISOU 1968 N GLY A 325 4905 9434 9733 105 -78 -1206 N
ATOM 1969 CA GLY A 325 13.346 -7.266 227.609 1.00 55.22 C
ANISOU 1969 CA GLY A 325 3723 8460 8799 314 -133 -1278 C
ATOM 1970 C GLY A 325 13.143 -6.751 229.014 1.00 63.85 C
ANISOU 1970 C GLY A 325 4800 9485 9974 311 61 -1389 C
ATOM 1971 O GLY A 325 12.081 -6.199 229.320 1.00 70.59 O
ANISOU 1971 O GLY A 325 5491 10418 10912 401 101 -1521 O
ATOM 1972 N MET A 326 14.121 -6.946 229.889 1.00 68.53 N
ANISOU 1972 N MET A 326 5554 9934 10549 206 188 -1354 N
ATOM 1973 CA MET A 326 14.018 -6.493 231.264 1.00 65.03 C
ANISOU 1973 CA MET A 326 5129 9404 10177 187 393 -1465 C
ATOM 1974 C MET A 326 14.356 -5.008 231.378 1.00 65.94 C
ANISOU 1974 C MET A 326 5279 9408 10368 455 283 -1378 C
ATOM 1975 O MET A 326 14.970 -4.409 230.490 1.00 72.52 O
ANISOU 1975 O MET A 326 6181 10192 11183 624 71 -1218 O
ATOM 1976 CB MET A 326 14.920 -7.338 232.163 1.00 61.45 C
ANISOU 1976 CB MET A 326 4996 8784 9569 -31 555 -1409 C
ATOM 1977 CG MET A 326 14.488 -8.805 232.189 1.00 81.36 C
ANISOU 1977 CG MET A 326 7519 11387 12008 -304 731 -1528 C
ATOM 1978 SD MET A 326 15.371 -9.814 233.389 1.00 88.43 S
ANISOU 1978 SD MET A 326 8882 12051 12664 -515 944 -1474 S
ATOM 1979 CE MET A 326 15.371 -8.709 234.799 1.00 86.47 C
ANISOU 1979 CE MET A 326 8758 11646 12452 -420 1053 -1515 C
ATOM 1980 N PHE A 327 13.906 -4.408 232.480 1.00 64.01 N
ANISOU 1980 N PHE A 327 5034 9101 10186 479 454 -1487 N
ATOM 1981 CA PHE A 327 14.182 -3.024 232.859 1.00 75.29 C
ANISOU 1981 CA PHE A 327 6571 10382 11652 691 418 -1417 C
ATOM 1982 C PHE A 327 13.427 -2.007 232.016 1.00 83.36 C
ANISOU 1982 C PHE A 327 7404 11496 12772 989 256 -1425 C
ATOM 1983 O PHE A 327 13.715 -0.808 232.104 1.00 85.58 O
ANISOU 1983 O PHE A 327 7777 11646 13093 1206 211 -1365 O
ATOM 1984 CB PHE A 327 15.681 -2.713 232.793 1.00 67.83 C
ANISOU 1984 CB PHE A 327 5957 9237 10579 691 307 -1197 C
ATOM 1985 CG PHE A 327 16.546 -3.812 233.331 1.00 62.15 C
ANISOU 1985 CG PHE A 327 5456 8445 9712 447 380 -1147 C
ATOM 1986 CD1 PHE A 327 16.398 -4.252 234.636 1.00 62.02 C
ANISOU 1986 CD1 PHE A 327 5573 8356 9635 287 597 -1247 C
ATOM 1987 CD2 PHE A 327 17.504 -4.410 232.530 1.00 61.64 C
ANISOU 1987 CD2 PHE A 327 5492 8371 9557 396 236 -1003 C
ATOM 1988 CE1 PHE A 327 17.188 -5.269 235.133 1.00 63.51 C
ANISOU 1988 CE1 PHE A 327 6011 8465 9657 109 646 -1200 C
ATOM 1989 CE2 PHE A 327 18.302 -5.428 233.020 1.00 61.89 C
ANISOU 1989 CE2 PHE A 327 5732 8339 9445 218 290 -961 C
ATOM 1990 CZ PHE A 327 18.144 -5.860 234.323 1.00 64.55 C
ANISOU 1990 CZ PHE A 327 6219 8603 9704 88 484 -1057 C
ATOM 1991 N ARG A 328 12.477 -2.446 231.188 1.00 86.96 N
ANISOU 1991 N ARG A 328 7692 12142 13208 997 162 -1467 N
ATOM 1992 CA ARG A 328 11.659 -1.490 230.450 1.00 89.62 C
ANISOU 1992 CA ARG A 328 7923 12553 13575 1284 5 -1456 C
ATOM 1993 C ARG A 328 10.798 -0.654 231.386 1.00 85.64 C
ANISOU 1993 C ARG A 328 7322 12041 13177 1405 154 -1592 C
ATOM 1994 O ARG A 328 10.501 0.508 231.086 1.00 93.80 O
ANISOU 1994 O ARG A 328 8367 13037 14235 1701 57 -1547 O
ATOM 1995 CB ARG A 328 10.792 -2.221 229.426 1.00 89.99 C
ANISOU 1995 CB ARG A 328 7789 12813 13592 1249 -123 -1506 C
ATOM 1996 CG ARG A 328 11.576 -2.724 228.230 1.00 89.91 C
ANISOU 1996 CG ARG A 328 7896 12793 13472 1223 -312 -1345 C
ATOM 1997 CD ARG A 328 12.290 -1.572 227.538 1.00103.60 C
ANISOU 1997 CD ARG A 328 9818 14378 15169 1502 -489 -1167 C
ATOM 1998 NE ARG A 328 11.359 -0.709 226.815 1.00121.24 N
ANISOU 1998 NE ARG A 328 11968 16683 17413 1796 -644 -1183 N
ATOM 1999 CZ ARG A 328 11.658 0.507 226.372 1.00126.36 C
ANISOU 1999 CZ ARG A 328 12792 17187 18033 2092 -757 -1070 C
ATOM 2000 NH1 ARG A 328 12.864 1.013 226.587 1.00124.52 N
ANISOU 2000 NH1 ARG A 328 12811 16729 17772 2113 -724 -947 N
ATOM 2001 NH2 ARG A 328 10.748 1.221 225.720 1.00131.49 N
ANISOU 2001 NH2 ARG A 328 13379 17904 18679 2368 -900 -1096 N
ATOM 2002 N GLN A 329 10.399 -1.221 232.521 1.00 91.31 N
ANISOU 2002 N GLN A 329 7974 12772 13946 1183 408 -1758 N
ATOM 2003 CA GLN A 329 9.623 -0.484 233.505 1.00108.19 C
ANISOU 2003 CA GLN A 329 10040 14882 16186 1265 590 -1897 C
ATOM 2004 C GLN A 329 10.509 0.499 234.262 1.00117.25 C
ANISOU 2004 C GLN A 329 11417 15786 17346 1375 672 -1817 C
ATOM 2005 O GLN A 329 11.725 0.318 234.374 1.00116.72 O
ANISOU 2005 O GLN A 329 11545 15576 17229 1286 661 -1712 O
ATOM 2006 CB GLN A 329 8.945 -1.456 234.470 1.00114.79 C
ANISOU 2006 CB GLN A 329 10781 15776 17059 961 870 -2112 C
ATOM 2007 CG GLN A 329 8.163 -2.554 233.759 1.00121.56 C
ANISOU 2007 CG GLN A 329 11441 16847 17898 800 818 -2216 C
ATOM 2008 CD GLN A 329 7.542 -3.549 234.716 1.00126.49 C
ANISOU 2008 CD GLN A 329 12028 17491 18542 471 1129 -2444 C
ATOM 2009 OE1 GLN A 329 7.504 -3.323 235.926 1.00133.84 O
ANISOU 2009 OE1 GLN A 329 13058 18285 19508 386 1388 -2535 O
ATOM 2010 NE2 GLN A 329 7.052 -4.661 234.177 1.00124.65 N
ANISOU 2010 NE2 GLN A 329 11685 17403 18272 274 1124 -2543 N
ATOM 2011 N ALA A 330 9.890 1.560 234.768 1.00123.17 N
ANISOU 2011 N ALA A 330 12143 16486 18170 1574 756 -1876 N
ATOM 2012 CA ALA A 330 10.598 2.635 235.450 1.00130.62 C
ANISOU 2012 CA ALA A 330 13321 17181 19127 1703 844 -1817 C
ATOM 2013 C ALA A 330 10.165 2.746 236.908 1.00138.98 C
ANISOU 2013 C ALA A 330 14410 18146 20251 1577 1168 -1981 C
ATOM 2014 O ALA A 330 10.095 3.840 237.475 1.00140.52 O
ANISOU 2014 O ALA A 330 14726 18186 20481 1747 1269 -1986 O
ATOM 2015 CB ALA A 330 10.388 3.963 234.725 1.00132.78 C
ANISOU 2015 CB ALA A 330 13646 17410 19396 2086 676 -1714 C
ATOM 2016 N SER A 331 9.876 1.609 237.544 1.00146.02 N
ANISOU 2016 N SER A 331 15240 19102 21140 1268 1358 -2118 N
ATOM 2017 CA SER A 331 9.430 1.641 238.935 1.00147.27 C
ANISOU 2017 CA SER A 331 15475 19147 21334 1119 1696 -2280 C
ATOM 2018 C SER A 331 10.507 2.225 239.841 1.00144.38 C
ANISOU 2018 C SER A 331 15505 18482 20871 1083 1801 -2178 C
ATOM 2019 O SER A 331 10.233 3.105 240.666 1.00151.38 O
ANISOU 2019 O SER A 331 16505 19221 21790 1164 1976 -2230 O
ATOM 2020 CB SER A 331 9.044 0.235 239.398 1.00150.73 C
ANISOU 2020 CB SER A 331 15870 19662 21737 766 1892 -2429 C
ATOM 2021 OG SER A 331 10.188 -0.588 239.525 1.00150.79 O
ANISOU 2021 OG SER A 331 16107 19567 21619 568 1906 -2346 O
ATOM 2022 N ASP A 332 11.747 1.759 239.689 1.00126.21 N
ANISOU 2022 N ASP A 332 13483 16085 18386 939 1652 -1989 N
ATOM 2023 CA ASP A 332 12.900 2.317 240.391 1.00112.74 C
ANISOU 2023 CA ASP A 332 12199 14124 16514 885 1641 -1840 C
ATOM 2024 C ASP A 332 13.988 2.561 239.345 1.00 99.14 C
ANISOU 2024 C ASP A 332 10560 12393 14717 974 1339 -1629 C
ATOM 2025 O ASP A 332 14.999 1.856 239.286 1.00 94.01 O
ANISOU 2025 O ASP A 332 10077 11713 13928 809 1234 -1526 O
ATOM 2026 CB ASP A 332 13.378 1.396 241.519 1.00112.05 C
ANISOU 2026 CB ASP A 332 12403 13914 16257 584 1802 -1870 C
ATOM 2027 CG ASP A 332 14.278 2.110 242.517 1.00102.76 C
ANISOU 2027 CG ASP A 332 11630 12484 14929 543 1835 -1792 C
ATOM 2028 OD1 ASP A 332 14.680 3.261 242.245 1.00 96.59 O
ANISOU 2028 OD1 ASP A 332 10910 11621 14168 709 1728 -1699 O
ATOM 2029 OD2 ASP A 332 14.578 1.519 243.578 1.00 99.43 O
ANISOU 2029 OD2 ASP A 332 11490 11936 14352 341 1972 -1833 O
ATOM 2030 N ARG A 333 13.765 3.576 238.507 1.00 92.51 N
ANISOU 2030 N ARG A 333 9618 11569 13963 1252 1213 -1575 N
ATOM 2031 CA ARG A 333 14.682 3.840 237.406 1.00 85.81 C
ANISOU 2031 CA ARG A 333 8855 10700 13050 1339 963 -1395 C
ATOM 2032 C ARG A 333 16.090 4.109 237.917 1.00 81.52 C
ANISOU 2032 C ARG A 333 8671 9953 12350 1182 942 -1277 C
ATOM 2033 O ARG A 333 17.077 3.738 237.265 1.00 82.02 O
ANISOU 2033 O ARG A 333 8806 10022 12337 1106 777 -1160 O
ATOM 2034 CB ARG A 333 14.166 5.023 236.583 1.00 90.20 C
ANISOU 2034 CB ARG A 333 9341 11245 13687 1685 873 -1367 C
ATOM 2035 CG ARG A 333 14.969 5.338 235.330 1.00 98.67 C
ANISOU 2035 CG ARG A 333 10526 12276 14687 1792 644 -1196 C
ATOM 2036 CD ARG A 333 14.461 6.597 234.634 1.00109.61 C
ANISOU 2036 CD ARG A 333 11947 13592 16105 2161 580 -1167 C
ATOM 2037 NE ARG A 333 13.124 6.430 234.066 1.00120.93 N
ANISOU 2037 NE ARG A 333 13019 15256 17674 2411 503 -1287 N
ATOM 2038 CZ ARG A 333 12.562 7.286 233.216 1.00125.44 C
ANISOU 2038 CZ ARG A 333 13569 15829 18264 2791 374 -1270 C
ATOM 2039 NH1 ARG A 333 13.223 8.369 232.829 1.00126.08 N
ANISOU 2039 NH1 ARG A 333 14020 15660 18225 2946 343 -1126 N
ATOM 2040 NH2 ARG A 333 11.341 7.059 232.746 1.00128.44 N
ANISOU 2040 NH2 ARG A 333 13669 16455 18679 2927 288 -1330 N
ATOM 2041 N GLU A 334 16.203 4.721 239.098 1.00 75.77 N
ANISOU 2041 N GLU A 334 8160 9053 11575 1124 1111 -1325 N
ATOM 2042 CA GLU A 334 17.517 4.957 239.681 1.00 70.84 C
ANISOU 2042 CA GLU A 334 7852 8263 10802 961 1082 -1254 C
ATOM 2043 C GLU A 334 18.229 3.654 240.030 1.00 65.84 C
ANISOU 2043 C GLU A 334 7271 7690 10055 729 1019 -1245 C
ATOM 2044 O GLU A 334 19.460 3.594 239.966 1.00 68.78 O
ANISOU 2044 O GLU A 334 7796 8014 10325 631 886 -1170 O
ATOM 2045 CB GLU A 334 17.389 5.848 240.918 1.00 66.55 C
ANISOU 2045 CB GLU A 334 7537 7529 10220 943 1280 -1326 C
ATOM 2046 CG GLU A 334 17.114 7.308 240.593 1.00 76.16 C
ANISOU 2046 CG GLU A 334 8827 8619 11493 1168 1327 -1300 C
ATOM 2047 CD GLU A 334 18.139 7.892 239.633 1.00 87.30 C
ANISOU 2047 CD GLU A 334 10361 9960 12849 1204 1163 -1173 C
ATOM 2048 OE1 GLU A 334 17.798 8.840 238.890 1.00 86.61 O
ANISOU 2048 OE1 GLU A 334 10296 9807 12804 1438 1158 -1129 O
ATOM 2049 OE2 GLU A 334 19.284 7.395 239.616 1.00 92.18 O
ANISOU 2049 OE2 GLU A 334 11065 10583 13374 1006 1048 -1127 O
ATOM 2050 N ALA A 335 17.493 2.599 240.386 1.00 63.50 N
ANISOU 2050 N ALA A 335 6860 7496 9769 640 1121 -1334 N
ATOM 2051 CA ALA A 335 18.160 1.334 240.688 1.00 64.51 C
ANISOU 2051 CA ALA A 335 7098 7656 9759 449 1070 -1318 C
ATOM 2052 C ALA A 335 18.777 0.725 239.432 1.00 62.85 C
ANISOU 2052 C ALA A 335 6755 7573 9552 461 850 -1204 C
ATOM 2053 O ALA A 335 19.913 0.229 239.463 1.00 67.87 O
ANISOU 2053 O ALA A 335 7533 8188 10067 368 721 -1135 O
ATOM 2054 CB ALA A 335 17.175 0.364 241.339 1.00 67.01 C
ANISOU 2054 CB ALA A 335 7374 8017 10068 333 1282 -1453 C
ATOM 2055 N VAL A 336 18.053 0.777 238.311 1.00 63.40 N
ANISOU 2055 N VAL A 336 6554 7778 9756 590 797 -1192 N
ATOM 2056 CA VAL A 336 18.616 0.317 237.046 1.00 66.02 C
ANISOU 2056 CA VAL A 336 6789 8209 10089 610 596 -1079 C
ATOM 2057 C VAL A 336 19.816 1.172 236.657 1.00 61.07 C
ANISOU 2057 C VAL A 336 6317 7464 9422 651 463 -966 C
ATOM 2058 O VAL A 336 20.843 0.656 236.188 1.00 64.58 O
ANISOU 2058 O VAL A 336 6812 7924 9802 571 334 -886 O
ATOM 2059 CB VAL A 336 17.537 0.332 235.946 1.00 66.01 C
ANISOU 2059 CB VAL A 336 6489 8367 10224 764 551 -1104 C
ATOM 2060 CG1 VAL A 336 18.119 -0.180 234.637 1.00 65.20 C
ANISOU 2060 CG1 VAL A 336 6327 8346 10100 772 353 -985 C
ATOM 2061 CG2 VAL A 336 16.327 -0.492 236.364 1.00 66.33 C
ANISOU 2061 CG2 VAL A 336 6335 8542 10324 685 712 -1266 C
ATOM 2062 N TYR A 337 19.719 2.490 236.866 1.00 54.41 N
ANISOU 2062 N TYR A 337 5563 6494 8616 765 519 -974 N
ATOM 2063 CA TYR A 337 20.843 3.357 236.530 1.00 57.69 C
ANISOU 2063 CA TYR A 337 6152 6778 8990 765 441 -898 C
ATOM 2064 C TYR A 337 22.066 3.031 237.381 1.00 59.85 C
ANISOU 2064 C TYR A 337 6597 6995 9147 568 412 -915 C
ATOM 2065 O TYR A 337 23.190 2.997 236.873 1.00 66.18 O
ANISOU 2065 O TYR A 337 7440 7788 9916 498 297 -865 O
ATOM 2066 CB TYR A 337 20.454 4.827 236.702 1.00 64.97 C
ANISOU 2066 CB TYR A 337 7190 7547 9949 913 546 -916 C
ATOM 2067 CG TYR A 337 19.498 5.371 235.657 1.00 74.28 C
ANISOU 2067 CG TYR A 337 8244 8759 11220 1174 518 -885 C
ATOM 2068 CD1 TYR A 337 19.423 4.811 234.385 1.00 80.75 C
ANISOU 2068 CD1 TYR A 337 8915 9701 12065 1245 365 -814 C
ATOM 2069 CD2 TYR A 337 18.675 6.458 235.943 1.00 71.86 C
ANISOU 2069 CD2 TYR A 337 7987 8356 10959 1372 635 -930 C
ATOM 2070 CE1 TYR A 337 18.552 5.316 233.433 1.00 83.12 C
ANISOU 2070 CE1 TYR A 337 9123 10036 12424 1515 303 -794 C
ATOM 2071 CE2 TYR A 337 17.804 6.967 235.000 1.00 73.49 C
ANISOU 2071 CE2 TYR A 337 8091 8598 11232 1663 579 -910 C
ATOM 2072 CZ TYR A 337 17.744 6.396 233.747 1.00 86.24 C
ANISOU 2072 CZ TYR A 337 9563 10345 12861 1739 399 -845 C
ATOM 2073 OH TYR A 337 16.875 6.904 232.807 1.00 86.38 O
ANISOU 2073 OH TYR A 337 9496 10404 12921 2057 308 -834 O
ATOM 2074 N ALA A 338 21.866 2.750 238.672 1.00 59.07 N
ANISOU 2074 N ALA A 338 6601 6864 8979 481 511 -1000 N
ATOM 2075 CA ALA A 338 22.998 2.435 239.539 1.00 59.03 C
ANISOU 2075 CA ALA A 338 6776 6814 8837 332 447 -1031 C
ATOM 2076 C ALA A 338 23.631 1.100 239.166 1.00 58.99 C
ANISOU 2076 C ALA A 338 6711 6933 8770 266 304 -988 C
ATOM 2077 O ALA A 338 24.864 0.966 239.164 1.00 66.34 O
ANISOU 2077 O ALA A 338 7698 7872 9637 200 167 -983 O
ATOM 2078 CB ALA A 338 22.556 2.426 241.000 1.00 53.82 C
ANISOU 2078 CB ALA A 338 6296 6066 8088 276 589 -1129 C
ATOM 2079 N ALA A 339 22.809 0.104 238.825 1.00 51.97 N
ANISOU 2079 N ALA A 339 5701 6147 7900 282 342 -973 N
ATOM 2080 CA ALA A 339 23.366 -1.192 238.448 1.00 52.26 C
ANISOU 2080 CA ALA A 339 5716 6280 7860 225 232 -927 C
ATOM 2081 C ALA A 339 24.191 -1.074 237.172 1.00 53.89 C
ANISOU 2081 C ALA A 339 5802 6540 8132 252 79 -835 C
ATOM 2082 O ALA A 339 25.351 -1.515 237.114 1.00 62.90 O
ANISOU 2082 O ALA A 339 6989 7703 9207 203 -48 -817 O
ATOM 2083 CB ALA A 339 22.238 -2.213 238.276 1.00 42.15 C
ANISOU 2083 CB ALA A 339 4339 5088 6590 207 341 -947 C
ATOM 2084 N PHE A 340 23.620 -0.437 236.144 1.00 52.89 N
ANISOU 2084 N PHE A 340 5537 6427 8131 344 92 -788 N
ATOM 2085 CA PHE A 340 24.356 -0.286 234.896 1.00 56.09 C
ANISOU 2085 CA PHE A 340 5881 6848 8584 362 -21 -703 C
ATOM 2086 C PHE A 340 25.594 0.588 235.069 1.00 55.80 C
ANISOU 2086 C PHE A 340 5957 6709 8535 304 -59 -726 C
ATOM 2087 O PHE A 340 26.633 0.323 234.447 1.00 64.06 O
ANISOU 2087 O PHE A 340 6979 7779 9581 246 -149 -698 O
ATOM 2088 CB PHE A 340 23.431 0.277 233.818 1.00 53.95 C
ANISOU 2088 CB PHE A 340 5499 6588 8414 502 -7 -654 C
ATOM 2089 CG PHE A 340 22.582 -0.768 233.155 1.00 54.03 C
ANISOU 2089 CG PHE A 340 5340 6744 8444 526 -33 -632 C
ATOM 2090 CD1 PHE A 340 21.318 -1.070 233.635 1.00 56.69 C
ANISOU 2090 CD1 PHE A 340 5568 7159 8813 554 65 -715 C
ATOM 2091 CD2 PHE A 340 23.056 -1.456 232.050 1.00 56.25 C
ANISOU 2091 CD2 PHE A 340 5572 7086 8714 501 -136 -549 C
ATOM 2092 CE1 PHE A 340 20.541 -2.040 233.021 1.00 55.12 C
ANISOU 2092 CE1 PHE A 340 5198 7111 8635 541 53 -729 C
ATOM 2093 CE2 PHE A 340 22.284 -2.423 231.432 1.00 52.91 C
ANISOU 2093 CE2 PHE A 340 5006 6798 8297 501 -157 -540 C
ATOM 2094 CZ PHE A 340 21.025 -2.715 231.918 1.00 52.09 C
ANISOU 2094 CZ PHE A 340 4779 6785 8226 514 -65 -638 C
ATOM 2095 N THR A 341 25.520 1.603 235.934 1.00 58.22 N
ANISOU 2095 N THR A 341 6382 6906 8832 300 25 -796 N
ATOM 2096 CA THR A 341 26.666 2.473 236.160 1.00 58.63 C
ANISOU 2096 CA THR A 341 6540 6865 8869 208 11 -853 C
ATOM 2097 C THR A 341 27.806 1.717 236.825 1.00 57.91 C
ANISOU 2097 C THR A 341 6458 6851 8694 96 -113 -920 C
ATOM 2098 O THR A 341 28.971 1.842 236.422 1.00 60.17 O
ANISOU 2098 O THR A 341 6706 7156 9002 14 -187 -956 O
ATOM 2099 CB THR A 341 26.242 3.662 237.019 1.00 54.65 C
ANISOU 2099 CB THR A 341 6187 6222 8356 221 142 -919 C
ATOM 2100 OG1 THR A 341 25.289 4.451 236.297 1.00 54.60 O
ANISOU 2100 OG1 THR A 341 6181 6139 8424 370 238 -860 O
ATOM 2101 CG2 THR A 341 27.448 4.515 237.384 1.00 56.98 C
ANISOU 2101 CG2 THR A 341 6600 6430 8621 82 140 -1013 C
ATOM 2102 N PHE A 342 27.489 0.913 237.844 1.00 53.37 N
ANISOU 2102 N PHE A 342 5944 6318 8016 100 -131 -952 N
ATOM 2103 CA PHE A 342 28.538 0.122 238.471 1.00 60.59 C
ANISOU 2103 CA PHE A 342 6898 7305 8819 51 -279 -1012 C
ATOM 2104 C PHE A 342 29.138 -0.880 237.493 1.00 57.42 C
ANISOU 2104 C PHE A 342 6359 7019 8440 66 -392 -947 C
ATOM 2105 O PHE A 342 30.348 -1.128 237.531 1.00 59.83 O
ANISOU 2105 O PHE A 342 6623 7389 8721 34 -528 -1008 O
ATOM 2106 CB PHE A 342 27.996 -0.583 239.715 1.00 58.14 C
ANISOU 2106 CB PHE A 342 6758 6976 8356 73 -255 -1047 C
ATOM 2107 CG PHE A 342 29.015 -1.433 240.416 1.00 71.81 C
ANISOU 2107 CG PHE A 342 8587 8768 9931 77 -431 -1107 C
ATOM 2108 CD1 PHE A 342 29.946 -0.864 241.272 1.00 73.57 C
ANISOU 2108 CD1 PHE A 342 8895 8978 10082 37 -543 -1231 C
ATOM 2109 CD2 PHE A 342 29.043 -2.805 240.221 1.00 73.36 C
ANISOU 2109 CD2 PHE A 342 8801 9035 10038 134 -492 -1049 C
ATOM 2110 CE1 PHE A 342 30.888 -1.649 241.918 1.00 69.09 C
ANISOU 2110 CE1 PHE A 342 8410 8485 9358 87 -745 -1301 C
ATOM 2111 CE2 PHE A 342 29.979 -3.592 240.862 1.00 68.83 C
ANISOU 2111 CE2 PHE A 342 8347 8508 9298 190 -668 -1102 C
ATOM 2112 CZ PHE A 342 30.903 -3.014 241.711 1.00 68.49 C
ANISOU 2112 CZ PHE A 342 8368 8468 9186 183 -812 -1230 C
ATOM 2113 N SER A 343 28.326 -1.438 236.586 1.00 60.30 N
ANISOU 2113 N SER A 343 6639 7418 8856 116 -338 -838 N
ATOM 2114 CA SER A 343 28.877 -2.396 235.624 1.00 56.01 C
ANISOU 2114 CA SER A 343 5991 6965 8324 122 -427 -770 C
ATOM 2115 C SER A 343 29.832 -1.720 234.637 1.00 61.50 C
ANISOU 2115 C SER A 343 6586 7650 9133 74 -459 -773 C
ATOM 2116 O SER A 343 30.936 -2.232 234.368 1.00 65.27 O
ANISOU 2116 O SER A 343 6996 8196 9609 46 -559 -802 O
ATOM 2117 CB SER A 343 27.735 -3.094 234.888 1.00 56.09 C
ANISOU 2117 CB SER A 343 5944 7014 8355 164 -356 -672 C
ATOM 2118 OG SER A 343 26.773 -3.590 235.811 1.00 55.10 O
ANISOU 2118 OG SER A 343 5912 6882 8142 171 -269 -703 O
ATOM 2119 N HIS A 344 29.438 -0.555 234.112 1.00 60.85 N
ANISOU 2119 N HIS A 344 6513 7468 9141 69 -359 -758 N
ATOM 2120 CA HIS A 344 30.343 0.212 233.262 1.00 65.04 C
ANISOU 2120 CA HIS A 344 7017 7939 9756 -5 -337 -783 C
ATOM 2121 C HIS A 344 31.647 0.499 233.996 1.00 60.64 C
ANISOU 2121 C HIS A 344 6443 7409 9190 -119 -398 -939 C
ATOM 2122 O HIS A 344 32.751 0.302 233.457 1.00 72.68 O
ANISOU 2122 O HIS A 344 7863 8984 10766 -194 -442 -995 O
ATOM 2123 CB HIS A 344 29.676 1.526 232.844 1.00 61.30 C
ANISOU 2123 CB HIS A 344 6647 7312 9331 27 -202 -756 C
ATOM 2124 CG HIS A 344 28.367 1.351 232.141 1.00 66.66 C
ANISOU 2124 CG HIS A 344 7316 7989 10024 171 -175 -634 C
ATOM 2125 ND1 HIS A 344 27.329 2.253 232.263 1.00 63.95 N
ANISOU 2125 ND1 HIS A 344 7050 7554 9692 283 -88 -620 N
ATOM 2126 CD2 HIS A 344 27.928 0.380 231.305 1.00 62.49 C
ANISOU 2126 CD2 HIS A 344 6694 7551 9499 228 -232 -538 C
ATOM 2127 CE1 HIS A 344 26.308 1.844 231.532 1.00 62.85 C
ANISOU 2127 CE1 HIS A 344 6838 7472 9573 413 -112 -534 C
ATOM 2128 NE2 HIS A 344 26.645 0.711 230.941 1.00 65.92 N
ANISOU 2128 NE2 HIS A 344 7127 7969 9952 367 -196 -485 N
ATOM 2129 N TRP A 345 31.534 0.956 235.246 1.00 58.54 N
ANISOU 2129 N TRP A 345 6267 7118 8858 -134 -401 -1031 N
ATOM 2130 CA TRP A 345 32.737 1.275 235.994 1.00 62.00 C
ANISOU 2130 CA TRP A 345 6679 7601 9277 -241 -484 -1207 C
ATOM 2131 C TRP A 345 33.599 0.044 236.214 1.00 58.89 C
ANISOU 2131 C TRP A 345 6171 7375 8832 -200 -675 -1251 C
ATOM 2132 O TRP A 345 34.823 0.159 236.253 1.00 60.15 O
ANISOU 2132 O TRP A 345 6205 7618 9032 -280 -763 -1401 O
ATOM 2133 CB TRP A 345 32.381 1.913 237.332 1.00 59.98 C
ANISOU 2133 CB TRP A 345 6578 7282 8932 -256 -463 -1290 C
ATOM 2134 CG TRP A 345 33.597 2.142 238.153 1.00 64.42 C
ANISOU 2134 CG TRP A 345 7105 7918 9454 -359 -587 -1488 C
ATOM 2135 CD1 TRP A 345 34.459 3.189 238.055 1.00 64.67 C
ANISOU 2135 CD1 TRP A 345 7096 7918 9558 -529 -533 -1646 C
ATOM 2136 CD2 TRP A 345 34.117 1.287 239.176 1.00 61.61 C
ANISOU 2136 CD2 TRP A 345 6755 7687 8966 -295 -796 -1573 C
ATOM 2137 NE1 TRP A 345 35.475 3.054 238.967 1.00 70.77 N
ANISOU 2137 NE1 TRP A 345 7801 8818 10270 -585 -710 -1842 N
ATOM 2138 CE2 TRP A 345 35.291 1.890 239.665 1.00 67.62 C
ANISOU 2138 CE2 TRP A 345 7439 8517 9738 -419 -892 -1793 C
ATOM 2139 CE3 TRP A 345 33.701 0.075 239.730 1.00 59.51 C
ANISOU 2139 CE3 TRP A 345 6581 7473 8559 -144 -904 -1496 C
ATOM 2140 CZ2 TRP A 345 36.052 1.324 240.686 1.00 65.78 C
ANISOU 2140 CZ2 TRP A 345 7198 8420 9375 -360 -1135 -1935 C
ATOM 2141 CZ3 TRP A 345 34.459 -0.486 240.743 1.00 59.05 C
ANISOU 2141 CZ3 TRP A 345 6572 7513 8352 -81 -1119 -1618 C
ATOM 2142 CH2 TRP A 345 35.620 0.137 241.209 1.00 60.80 C
ANISOU 2142 CH2 TRP A 345 6695 7819 8586 -171 -1254 -1834 C
ATOM 2143 N LEU A 346 32.993 -1.137 236.365 1.00 52.75 N
ANISOU 2143 N LEU A 346 5436 6647 7960 -74 -733 -1141 N
ATOM 2144 CA LEU A 346 33.805 -2.341 236.526 1.00 56.66 C
ANISOU 2144 CA LEU A 346 5869 7277 8381 2 -908 -1170 C
ATOM 2145 C LEU A 346 34.600 -2.634 235.261 1.00 56.30 C
ANISOU 2145 C LEU A 346 5636 7295 8462 -30 -915 -1155 C
ATOM 2146 O LEU A 346 35.782 -3.019 235.323 1.00 64.85 O
ANISOU 2146 O LEU A 346 6586 8497 9559 -19 -1051 -1272 O
ATOM 2147 CB LEU A 346 32.923 -3.536 236.878 1.00 59.56 C
ANISOU 2147 CB LEU A 346 6383 7644 8603 123 -914 -1051 C
ATOM 2148 CG LEU A 346 32.649 -3.802 238.353 1.00 64.52 C
ANISOU 2148 CG LEU A 346 7230 8243 9040 186 -971 -1109 C
ATOM 2149 CD1 LEU A 346 31.903 -5.113 238.490 1.00 68.28 C
ANISOU 2149 CD1 LEU A 346 7868 8703 9371 278 -936 -1001 C
ATOM 2150 CD2 LEU A 346 33.942 -3.821 239.160 1.00 60.04 C
ANISOU 2150 CD2 LEU A 346 6653 7768 8393 226 -1189 -1273 C
ATOM 2151 N VAL A 347 33.980 -2.420 234.097 1.00 52.18 N
ANISOU 2151 N VAL A 347 5100 6694 8032 -63 -771 -1026 N
ATOM 2152 CA VAL A 347 34.723 -2.602 232.852 1.00 58.62 C
ANISOU 2152 CA VAL A 347 5780 7533 8962 -115 -744 -1014 C
ATOM 2153 C VAL A 347 35.942 -1.692 232.841 1.00 65.33 C
ANISOU 2153 C VAL A 347 6508 8395 9919 -258 -730 -1208 C
ATOM 2154 O VAL A 347 37.062 -2.123 232.542 1.00 64.79 O
ANISOU 2154 O VAL A 347 6270 8433 9914 -283 -798 -1312 O
ATOM 2155 CB VAL A 347 33.829 -2.351 231.627 1.00 62.51 C
ANISOU 2155 CB VAL A 347 6327 7913 9510 -124 -598 -855 C
ATOM 2156 CG1 VAL A 347 34.701 -2.252 230.372 1.00 50.27 C
ANISOU 2156 CG1 VAL A 347 4688 6338 8073 -214 -532 -869 C
ATOM 2157 CG2 VAL A 347 32.823 -3.468 231.472 1.00 55.49 C
ANISOU 2157 CG2 VAL A 347 5490 7060 8533 -13 -622 -704 C
ATOM 2158 N TYR A 348 35.749 -0.416 233.179 1.00 69.27 N
ANISOU 2158 N TYR A 348 7088 8786 10445 -361 -627 -1280 N
ATOM 2159 CA TYR A 348 36.915 0.472 233.169 1.00 60.73 C
ANISOU 2159 CA TYR A 348 5900 7710 9463 -543 -579 -1496 C
ATOM 2160 C TYR A 348 37.910 0.141 234.277 1.00 69.65 C
ANISOU 2160 C TYR A 348 6882 9025 10558 -537 -784 -1704 C
ATOM 2161 O TYR A 348 39.116 0.354 234.104 1.00 75.05 O
ANISOU 2161 O TYR A 348 7364 9805 11347 -660 -801 -1910 O
ATOM 2162 CB TYR A 348 36.472 1.932 233.234 1.00 59.23 C
ANISOU 2162 CB TYR A 348 5881 7334 9288 -662 -391 -1526 C
ATOM 2163 CG TYR A 348 35.719 2.283 231.986 1.00 57.74 C
ANISOU 2163 CG TYR A 348 5833 6972 9134 -642 -214 -1351 C
ATOM 2164 CD1 TYR A 348 36.375 2.357 230.759 1.00 60.48 C
ANISOU 2164 CD1 TYR A 348 6142 7264 9575 -746 -96 -1367 C
ATOM 2165 CD2 TYR A 348 34.347 2.458 232.013 1.00 47.84 C
ANISOU 2165 CD2 TYR A 348 4746 5618 7811 -502 -175 -1180 C
ATOM 2166 CE1 TYR A 348 35.683 2.638 229.596 1.00 57.78 C
ANISOU 2166 CE1 TYR A 348 5974 6751 9230 -702 42 -1202 C
ATOM 2167 CE2 TYR A 348 33.643 2.739 230.856 1.00 54.53 C
ANISOU 2167 CE2 TYR A 348 5718 6328 8673 -441 -58 -1030 C
ATOM 2168 CZ TYR A 348 34.319 2.830 229.652 1.00 55.59 C
ANISOU 2168 CZ TYR A 348 5857 6391 8873 -535 40 -1035 C
ATOM 2169 OH TYR A 348 33.623 3.120 228.504 1.00 63.06 O
ANISOU 2169 OH TYR A 348 6975 7184 9801 -455 137 -886 O
ATOM 2170 N ALA A 349 37.435 -0.393 235.402 1.00 67.18 N
ANISOU 2170 N ALA A 349 6668 8764 10091 -392 -939 -1670 N
ATOM 2171 CA ALA A 349 38.325 -0.752 236.501 1.00 60.92 C
ANISOU 2171 CA ALA A 349 5785 8139 9221 -337 -1174 -1860 C
ATOM 2172 C ALA A 349 39.251 -1.895 236.126 1.00 64.14 C
ANISOU 2172 C ALA A 349 5992 8724 9654 -221 -1337 -1904 C
ATOM 2173 O ALA A 349 40.345 -2.015 236.688 1.00 74.80 O
ANISOU 2173 O ALA A 349 7166 10247 11008 -197 -1528 -2125 O
ATOM 2174 CB ALA A 349 37.505 -1.131 237.734 1.00 51.56 C
ANISOU 2174 CB ALA A 349 4837 6923 7831 -193 -1276 -1787 C
ATOM 2175 N ASN A 350 38.827 -2.755 235.199 1.00 70.20 N
ANISOU 2175 N ASN A 350 6781 9458 10432 -133 -1275 -1709 N
ATOM 2176 CA ASN A 350 39.706 -3.850 234.790 1.00 63.97 C
ANISOU 2176 CA ASN A 350 5821 8818 9666 -12 -1405 -1743 C
ATOM 2177 C ASN A 350 41.011 -3.326 234.183 1.00 66.53 C
ANISOU 2177 C ASN A 350 5919 9216 10145 -158 -1329 -1920 C
ATOM 2178 O ASN A 350 42.093 -3.904 234.402 1.00 72.62 O
ANISOU 2178 O ASN A 350 6589 10129 10874 -55 -1442 -2014 O
ATOM 2179 CB ASN A 350 38.974 -4.748 233.795 1.00 56.28 C
ANISOU 2179 CB ASN A 350 4946 7764 8672 63 -1299 -1495 C
ATOM 2180 CG ASN A 350 39.775 -5.964 233.417 1.00 61.98 C
ANISOU 2180 CG ASN A 350 5551 8611 9386 211 -1413 -1502 C
ATOM 2181 OD1 ASN A 350 40.001 -6.849 234.243 1.00 63.06 O
ANISOU 2181 OD1 ASN A 350 5763 8837 9361 416 -1605 -1518 O
ATOM 2182 ND2 ASN A 350 40.210 -6.024 232.160 1.00 54.34 N
ANISOU 2182 ND2 ASN A 350 4499 7612 8535 121 -1252 -1453 N
ATOM 2183 N SER A 351 40.936 -2.217 233.437 1.00 60.84 N
ANISOU 2183 N SER A 351 5168 8373 9576 -393 -1103 -1958 N
ATOM 2184 CA SER A 351 42.138 -1.639 232.845 1.00 61.82 C
ANISOU 2184 CA SER A 351 5148 8524 9815 -559 -963 -2122 C
ATOM 2185 C SER A 351 43.105 -1.135 233.904 1.00 67.81 C
ANISOU 2185 C SER A 351 5799 9424 10543 -598 -1078 -2370 C
ATOM 2186 O SER A 351 44.323 -1.210 233.714 1.00 73.17 O
ANISOU 2186 O SER A 351 6308 10219 11276 -625 -1070 -2522 O
ATOM 2187 CB SER A 351 41.769 -0.496 231.895 1.00 67.61 C
ANISOU 2187 CB SER A 351 5947 9055 10686 -806 -677 -2120 C
ATOM 2188 OG SER A 351 41.066 -0.973 230.760 1.00 78.01 O
ANISOU 2188 OG SER A 351 7344 10252 12046 -772 -570 -1910 O
ATOM 2189 N ALA A 352 42.588 -0.603 235.014 1.00 68.83 N
ANISOU 2189 N ALA A 352 6017 9545 10592 -609 -1182 -2429 N
ATOM 2190 CA ALA A 352 43.463 -0.222 236.116 1.00 69.52 C
ANISOU 2190 CA ALA A 352 6016 9776 10621 -623 -1329 -2659 C
ATOM 2191 C ALA A 352 43.974 -1.444 236.867 1.00 66.15 C
ANISOU 2191 C ALA A 352 5550 9530 10052 -334 -1622 -2663 C
ATOM 2192 O ALA A 352 45.081 -1.420 237.414 1.00 72.27 O
ANISOU 2192 O ALA A 352 6179 10467 10814 -303 -1744 -2858 O
ATOM 2193 CB ALA A 352 42.726 0.721 237.067 1.00 66.16 C
ANISOU 2193 CB ALA A 352 5740 9262 10136 -731 -1344 -2723 C
ATOM 2194 N ALA A 353 43.180 -2.515 236.906 1.00 63.25 N
ANISOU 2194 N ALA A 353 5327 9132 9572 -116 -1730 -2459 N
ATOM 2195 CA ALA A 353 43.562 -3.694 237.675 1.00 65.23 C
ANISOU 2195 CA ALA A 353 5623 9512 9649 178 -1996 -2454 C
ATOM 2196 C ALA A 353 44.742 -4.419 237.044 1.00 71.29 C
ANISOU 2196 C ALA A 353 6207 10402 10479 270 -2005 -2503 C
ATOM 2197 O ALA A 353 45.640 -4.883 237.755 1.00 79.58 O
ANISOU 2197 O ALA A 353 7190 11602 11446 443 -2209 -2637 O
ATOM 2198 CB ALA A 353 42.368 -4.643 237.805 1.00 59.16 C
ANISOU 2198 CB ALA A 353 5093 8651 8732 364 -2065 -2232 C
ATOM 2199 N ASN A 354 44.766 -4.525 235.717 1.00 67.20 N
ANISOU 2199 N ASN A 354 5615 9815 10103 166 -1790 -2406 N
ATOM 2200 CA ASN A 354 45.771 -5.389 235.093 1.00 69.09 C
ANISOU 2200 CA ASN A 354 5711 10154 10388 279 -1802 -2434 C
ATOM 2201 C ASN A 354 47.205 -4.988 235.428 1.00 76.52 C
ANISOU 2201 C ASN A 354 6402 11266 11407 244 -1866 -2721 C
ATOM 2202 O ASN A 354 47.985 -5.862 235.858 1.00 77.44 O
ANISOU 2202 O ASN A 354 6449 11525 11450 478 -2062 -2797 O
ATOM 2203 CB ASN A 354 45.540 -5.435 233.579 1.00 63.48 C
ANISOU 2203 CB ASN A 354 4981 9321 9816 139 -1543 -2298 C
ATOM 2204 CG ASN A 354 44.309 -6.230 233.211 1.00 69.73 C
ANISOU 2204 CG ASN A 354 5984 9993 10517 244 -1526 -2023 C
ATOM 2205 OD1 ASN A 354 43.979 -7.210 233.877 1.00 71.18 O
ANISOU 2205 OD1 ASN A 354 6303 10213 10530 480 -1707 -1937 O
ATOM 2206 ND2 ASN A 354 43.608 -5.805 232.166 1.00 67.96 N
ANISOU 2206 ND2 ASN A 354 5809 9618 10394 74 -1306 -1895 N
ATOM 2207 N PRO A 355 47.622 -3.727 235.274 1.00 74.52 N
ANISOU 2207 N PRO A 355 6013 11007 11293 -28 -1710 -2901 N
ATOM 2208 CA PRO A 355 49.001 -3.375 235.641 1.00 77.23 C
ANISOU 2208 CA PRO A 355 6097 11534 11712 -64 -1775 -3203 C
ATOM 2209 C PRO A 355 49.322 -3.657 237.095 1.00 77.87 C
ANISOU 2209 C PRO A 355 6181 11772 11634 150 -2097 -3321 C
ATOM 2210 O PRO A 355 50.451 -4.054 237.403 1.00 88.97 O
ANISOU 2210 O PRO A 355 7388 13363 13052 285 -2249 -3515 O
ATOM 2211 CB PRO A 355 49.077 -1.870 235.334 1.00 82.64 C
ANISOU 2211 CB PRO A 355 6725 12139 12535 -420 -1523 -3349 C
ATOM 2212 CG PRO A 355 48.001 -1.639 234.327 1.00 79.36 C
ANISOU 2212 CG PRO A 355 6499 11493 12163 -551 -1282 -3116 C
ATOM 2213 CD PRO A 355 46.897 -2.580 234.700 1.00 74.32 C
ANISOU 2213 CD PRO A 355 6069 10804 11365 -314 -1452 -2854 C
ATOM 2214 N ILE A 356 48.360 -3.480 238.004 1.00 80.30 N
ANISOU 2214 N ILE A 356 6717 12007 11785 198 -2213 -3222 N
ATOM 2215 CA ILE A 356 48.614 -3.799 239.403 1.00 87.76 C
ANISOU 2215 CA ILE A 356 7723 13076 12545 420 -2528 -3322 C
ATOM 2216 C ILE A 356 48.856 -5.296 239.563 1.00 87.51 C
ANISOU 2216 C ILE A 356 7768 13108 12372 788 -2735 -3233 C
ATOM 2217 O ILE A 356 49.710 -5.727 240.362 1.00 87.87 O
ANISOU 2217 O ILE A 356 7746 13314 12326 1006 -2982 -3394 O
ATOM 2218 CB ILE A 356 47.424 -3.302 240.253 1.00 76.15 C
ANISOU 2218 CB ILE A 356 6527 11477 10929 378 -2575 -3223 C
ATOM 2219 CG1 ILE A 356 47.219 -1.797 240.039 1.00 68.55 C
ANISOU 2219 CG1 ILE A 356 5505 10434 10106 11 -2346 -3321 C
ATOM 2220 CG2 ILE A 356 47.623 -3.627 241.725 1.00 77.35 C
ANISOU 2220 CG2 ILE A 356 6808 11725 10856 610 -2899 -3317 C
ATOM 2221 CD1 ILE A 356 45.931 -1.249 240.624 1.00 70.23 C
ANISOU 2221 CD1 ILE A 356 5987 10485 10214 -68 -2331 -3214 C
ATOM 2222 N ILE A 357 48.157 -6.108 238.764 1.00 88.37 N
ANISOU 2222 N ILE A 357 8020 13094 12463 862 -2630 -2988 N
ATOM 2223 CA ILE A 357 48.354 -7.550 238.810 1.00 85.64 C
ANISOU 2223 CA ILE A 357 7780 12782 11976 1194 -2784 -2893 C
ATOM 2224 C ILE A 357 49.759 -7.902 238.355 1.00 78.89 C
ANISOU 2224 C ILE A 357 6631 12096 11247 1264 -2813 -3079 C
ATOM 2225 O ILE A 357 50.437 -8.729 238.975 1.00 79.41 O
ANISOU 2225 O ILE A 357 6703 12281 11187 1562 -3049 -3167 O
ATOM 2226 CB ILE A 357 47.284 -8.257 237.957 1.00 75.15 C
ANISOU 2226 CB ILE A 357 6654 11283 10617 1209 -2630 -2601 C
ATOM 2227 CG1 ILE A 357 45.884 -7.885 238.450 1.00 73.85 C
ANISOU 2227 CG1 ILE A 357 6754 10967 10338 1145 -2610 -2453 C
ATOM 2228 CG2 ILE A 357 47.488 -9.772 237.976 1.00 72.84 C
ANISOU 2228 CG2 ILE A 357 6505 11008 10162 1543 -2764 -2504 C
ATOM 2229 CD1 ILE A 357 44.764 -8.538 237.675 1.00 68.77 C
ANISOU 2229 CD1 ILE A 357 6294 10169 9665 1154 -2469 -2188 C
ATOM 2230 N TYR A 358 50.233 -7.268 237.277 1.00 79.50 N
ANISOU 2230 N TYR A 358 6459 12181 11567 998 -2571 -3158 N
ATOM 2231 CA TYR A 358 51.614 -7.520 236.866 1.00 80.06 C
ANISOU 2231 CA TYR A 358 6225 12422 11773 1044 -2588 -3377 C
ATOM 2232 C TYR A 358 52.602 -7.036 237.918 1.00 85.62 C
ANISOU 2232 C TYR A 358 6731 13332 12470 1097 -2801 -3689 C
ATOM 2233 O TYR A 358 53.658 -7.653 238.115 1.00 86.45 O
ANISOU 2233 O TYR A 358 6655 13613 12577 1311 -2970 -3867 O
ATOM 2234 CB TYR A 358 51.928 -6.846 235.530 1.00 77.69 C
ANISOU 2234 CB TYR A 358 5726 12067 11724 726 -2264 -3427 C
ATOM 2235 CG TYR A 358 50.872 -6.991 234.458 1.00 75.91 C
ANISOU 2235 CG TYR A 358 5692 11624 11524 605 -2028 -3138 C
ATOM 2236 CD1 TYR A 358 50.030 -8.093 234.414 1.00 68.99 C
ANISOU 2236 CD1 TYR A 358 5065 10657 10490 821 -2101 -2869 C
ATOM 2237 CD2 TYR A 358 50.728 -6.016 233.481 1.00 72.36 C
ANISOU 2237 CD2 TYR A 358 5189 11056 11250 276 -1726 -3150 C
ATOM 2238 CE1 TYR A 358 49.066 -8.212 233.431 1.00 66.73 C
ANISOU 2238 CE1 TYR A 358 4931 10190 10232 707 -1894 -2622 C
ATOM 2239 CE2 TYR A 358 49.772 -6.127 232.498 1.00 72.85 C
ANISOU 2239 CE2 TYR A 358 5426 10923 11330 181 -1527 -2898 C
ATOM 2240 CZ TYR A 358 48.942 -7.222 232.475 1.00 70.60 C
ANISOU 2240 CZ TYR A 358 5350 10574 10900 393 -1619 -2637 C
ATOM 2241 OH TYR A 358 47.984 -7.320 231.489 1.00 61.79 O
ANISOU 2241 OH TYR A 358 4390 9279 9807 295 -1428 -2402 O
ATOM 2242 N ASN A 359 52.286 -5.933 238.595 1.00 89.64 N
ANISOU 2242 N ASN A 359 7264 13826 12969 908 -2798 -3771 N
ATOM 2243 CA ASN A 359 53.209 -5.398 239.587 1.00 89.93 C
ANISOU 2243 CA ASN A 359 7106 14061 13001 928 -2993 -4077 C
ATOM 2244 C ASN A 359 53.370 -6.334 240.774 1.00 96.71 C
ANISOU 2244 C ASN A 359 8112 15018 13617 1331 -3363 -4089 C
ATOM 2245 O ASN A 359 54.453 -6.400 241.366 1.00108.11 O
ANISOU 2245 O ASN A 359 9341 16674 15063 1472 -3573 -4355 O
ATOM 2246 CB ASN A 359 52.737 -4.026 240.068 1.00 88.20 C
ANISOU 2246 CB ASN A 359 6929 13781 12801 629 -2899 -4139 C
ATOM 2247 CG ASN A 359 53.699 -3.399 241.052 1.00 95.08 C
ANISOU 2247 CG ASN A 359 7589 14863 13674 609 -3083 -4468 C
ATOM 2248 OD1 ASN A 359 54.660 -2.739 240.658 1.00104.68 O
ANISOU 2248 OD1 ASN A 359 8489 16202 15081 404 -2959 -4733 O
ATOM 2249 ND2 ASN A 359 53.451 -3.607 242.341 1.00 92.91 N
ANISOU 2249 ND2 ASN A 359 7498 14625 13178 819 -3377 -4463 N
ATOM 2250 N PHE A 360 52.316 -7.060 241.142 1.00 92.96 N
ANISOU 2250 N PHE A 360 8011 14386 12923 1526 -3446 -3819 N
ATOM 2251 CA PHE A 360 52.442 -7.961 242.284 1.00 95.14 C
ANISOU 2251 CA PHE A 360 8500 14715 12933 1922 -3779 -3829 C
ATOM 2252 C PHE A 360 52.781 -9.401 241.916 1.00 99.26 C
ANISOU 2252 C PHE A 360 9095 15251 13368 2260 -3866 -3744 C
ATOM 2253 O PHE A 360 53.332 -10.115 242.759 1.00106.62 O
ANISOU 2253 O PHE A 360 10112 16278 14119 2608 -4149 -3844 O
ATOM 2254 CB PHE A 360 51.166 -7.941 243.132 1.00 94.75 C
ANISOU 2254 CB PHE A 360 8873 14481 12644 1972 -3844 -3628 C
ATOM 2255 CG PHE A 360 50.991 -6.675 243.915 1.00103.92 C
ANISOU 2255 CG PHE A 360 10013 15658 13811 1743 -3870 -3755 C
ATOM 2256 CD1 PHE A 360 51.848 -6.367 244.961 1.00106.61 C
ANISOU 2256 CD1 PHE A 360 10251 16174 14084 1843 -4125 -4010 C
ATOM 2257 CD2 PHE A 360 49.977 -5.787 243.601 1.00 99.80 C
ANISOU 2257 CD2 PHE A 360 9579 14979 13359 1430 -3641 -3630 C
ATOM 2258 CE1 PHE A 360 51.694 -5.199 245.681 1.00102.11 C
ANISOU 2258 CE1 PHE A 360 9675 15614 13508 1613 -4142 -4128 C
ATOM 2259 CE2 PHE A 360 49.816 -4.618 244.319 1.00 99.66 C
ANISOU 2259 CE2 PHE A 360 9565 14965 13337 1212 -3652 -3752 C
ATOM 2260 CZ PHE A 360 50.676 -4.323 245.360 1.00101.88 C
ANISOU 2260 CZ PHE A 360 9752 15414 13542 1292 -3898 -3996 C
ATOM 2261 N LEU A 361 52.480 -9.852 240.699 1.00 96.53 N
ANISOU 2261 N LEU A 361 8737 14807 13132 2178 -3635 -3568 N
ATOM 2262 CA LEU A 361 52.727 -11.239 240.318 1.00 87.72 C
ANISOU 2262 CA LEU A 361 7724 13685 11920 2484 -3696 -3469 C
ATOM 2263 C LEU A 361 53.857 -11.411 239.311 1.00 79.77 C
ANISOU 2263 C LEU A 361 6339 12824 11147 2442 -3602 -3625 C
ATOM 2264 O LEU A 361 54.084 -12.533 238.844 1.00 80.78 O
ANISOU 2264 O LEU A 361 6529 12944 11221 2669 -3620 -3540 O
ATOM 2265 CB LEU A 361 51.443 -11.872 239.767 1.00 84.91 C
ANISOU 2265 CB LEU A 361 7709 13096 11458 2477 -3530 -3127 C
ATOM 2266 CG LEU A 361 50.329 -12.053 240.802 1.00 80.10 C
ANISOU 2266 CG LEU A 361 7536 12331 10566 2606 -3643 -2970 C
ATOM 2267 CD1 LEU A 361 49.065 -12.585 240.162 1.00 80.42 C
ANISOU 2267 CD1 LEU A 361 7863 12159 10536 2555 -3451 -2665 C
ATOM 2268 CD2 LEU A 361 50.794 -12.973 241.927 1.00 84.67 C
ANISOU 2268 CD2 LEU A 361 8355 12955 10862 3033 -3950 -3048 C
ATOM 2269 N SER A 362 54.568 -10.341 238.957 1.00 86.26 N
ANISOU 2269 N SER A 362 6789 13766 12219 2155 -3486 -3857 N
ATOM 2270 CA SER A 362 55.724 -10.420 238.065 1.00 94.04 C
ANISOU 2270 CA SER A 362 7399 14896 13434 2099 -3391 -4056 C
ATOM 2271 C SER A 362 56.851 -9.580 238.652 1.00103.71 C
ANISOU 2271 C SER A 362 8267 16358 14781 2028 -3511 -4443 C
ATOM 2272 O SER A 362 56.725 -8.356 238.756 1.00104.13 O
ANISOU 2272 O SER A 362 8221 16402 14941 1709 -3385 -4544 O
ATOM 2273 CB SER A 362 55.372 -9.937 236.658 1.00 90.38 C
ANISOU 2273 CB SER A 362 6857 14294 13191 1743 -3015 -3938 C
ATOM 2274 OG SER A 362 56.543 -9.615 235.924 1.00 96.68 O
ANISOU 2274 OG SER A 362 7266 15232 14237 1600 -2892 -4204 O
ATOM 2275 N GLY A 363 57.958 -10.227 239.021 1.00114.73 N
ANISOU 2275 N GLY A 363 9466 17968 16159 2323 -3750 -4673 N
ATOM 2276 CA GLY A 363 59.077 -9.479 239.566 1.00 99.09 C
ANISOU 2276 CA GLY A 363 7110 16239 14299 2265 -3877 -5071 C
ATOM 2277 C GLY A 363 59.698 -8.536 238.554 1.00 99.87 C
ANISOU 2277 C GLY A 363 6837 16392 14718 1861 -3565 -5280 C
ATOM 2278 O GLY A 363 60.196 -7.468 238.917 1.00120.68 O
ANISOU 2278 O GLY A 363 9236 19151 17467 1635 -3544 -5555 O
ATOM 2279 N LYS A 364 59.655 -8.901 237.271 1.00 97.55 N
ANISOU 2279 N LYS A 364 6512 15989 14562 1753 -3304 -5155 N
ATOM 2280 CA LYS A 364 60.255 -8.060 236.238 1.00119.74 C
ANISOU 2280 CA LYS A 364 9014 18818 17664 1375 -2979 -5358 C
ATOM 2281 C LYS A 364 59.424 -6.802 235.990 1.00107.25 C
ANISOU 2281 C LYS A 364 7570 17044 16137 962 -2698 -5260 C
ATOM 2282 O LYS A 364 59.961 -5.681 235.947 1.00106.89 O
ANISOU 2282 O LYS A 364 7295 17069 16249 660 -2546 -5537 O
ATOM 2283 CB LYS A 364 60.434 -8.884 234.960 1.00110.20 C
ANISOU 2283 CB LYS A 364 7771 17534 16566 1404 -2793 -5243 C
ATOM 2284 CG LYS A 364 61.534 -9.942 235.106 1.00118.91 C
ANISOU 2284 CG LYS A 364 8640 18866 17675 1768 -3032 -5437 C
ATOM 2285 CD LYS A 364 61.383 -11.114 234.151 1.00123.28 C
ANISOU 2285 CD LYS A 364 9308 19310 18221 1931 -2943 -5200 C
ATOM 2286 CE LYS A 364 62.486 -12.140 234.395 1.00129.26 C
ANISOU 2286 CE LYS A 364 9842 20302 18968 2323 -3201 -5404 C
ATOM 2287 NZ LYS A 364 62.336 -13.365 233.560 1.00127.51 N
ANISOU 2287 NZ LYS A 364 9758 19976 18712 2521 -3133 -5163 N
ATOM 2288 N PHE A 365 58.105 -6.961 235.854 1.00 89.35 N
ANISOU 2288 N PHE A 365 5684 14535 13731 949 -2626 -4880 N
ATOM 2289 CA PHE A 365 57.248 -5.787 235.756 1.00 86.21 C
ANISOU 2289 CA PHE A 365 5440 13959 13355 607 -2402 -4783 C
ATOM 2290 C PHE A 365 57.359 -4.938 237.012 1.00 99.52 C
ANISOU 2290 C PHE A 365 7084 15761 14970 562 -2575 -4971 C
ATOM 2291 O PHE A 365 57.366 -3.704 236.940 1.00102.23 O
ANISOU 2291 O PHE A 365 7358 16068 15417 224 -2374 -5107 O
ATOM 2292 CB PHE A 365 55.791 -6.200 235.543 1.00 89.51 C
ANISOU 2292 CB PHE A 365 6259 14129 13620 655 -2350 -4362 C
ATOM 2293 CG PHE A 365 55.407 -6.392 234.103 1.00 83.21 C
ANISOU 2293 CG PHE A 365 5531 13147 12936 500 -2046 -4172 C
ATOM 2294 CD1 PHE A 365 55.308 -5.308 233.247 1.00 76.10 C
ANISOU 2294 CD1 PHE A 365 4596 12118 12202 125 -1710 -4222 C
ATOM 2295 CD2 PHE A 365 55.109 -7.656 233.617 1.00 85.10 C
ANISOU 2295 CD2 PHE A 365 5905 13329 13100 735 -2091 -3940 C
ATOM 2296 CE1 PHE A 365 54.944 -5.484 231.924 1.00 77.79 C
ANISOU 2296 CE1 PHE A 365 4903 12150 12504 -4 -1439 -4050 C
ATOM 2297 CE2 PHE A 365 54.739 -7.844 232.295 1.00 72.19 C
ANISOU 2297 CE2 PHE A 365 4340 11526 11562 593 -1820 -3763 C
ATOM 2298 CZ PHE A 365 54.656 -6.757 231.446 1.00 75.10 C
ANISOU 2298 CZ PHE A 365 4671 11768 12096 228 -1501 -3818 C
ATOM 2299 N ARG A 366 57.462 -5.584 238.176 1.00 90.60 N
ANISOU 2299 N ARG A 366 6015 14760 13649 902 -2941 -4989 N
ATOM 2300 CA ARG A 366 57.557 -4.833 239.422 1.00 97.00 C
ANISOU 2300 CA ARG A 366 6806 15678 14371 876 -3132 -5161 C
ATOM 2301 C ARG A 366 58.844 -4.030 239.477 1.00104.38 C
ANISOU 2301 C ARG A 366 7318 16844 15498 691 -3098 -5595 C
ATOM 2302 O ARG A 366 58.851 -2.883 239.939 1.00105.81 O
ANISOU 2302 O ARG A 366 7446 17045 15710 428 -3032 -5747 O
ATOM 2303 CB ARG A 366 57.456 -5.788 240.611 1.00103.11 C
ANISOU 2303 CB ARG A 366 7765 16529 14882 1311 -3535 -5097 C
ATOM 2304 CG ARG A 366 57.880 -5.203 241.950 1.00 98.57 C
ANISOU 2304 CG ARG A 366 7115 16123 14213 1357 -3802 -5340 C
ATOM 2305 CD ARG A 366 57.410 -6.111 243.072 1.00113.26 C
ANISOU 2305 CD ARG A 366 9312 17958 15765 1768 -4151 -5186 C
ATOM 2306 NE ARG A 366 57.666 -7.515 242.758 1.00130.49 N
ANISOU 2306 NE ARG A 366 11559 20155 17867 2141 -4271 -5092 N
ATOM 2307 CZ ARG A 366 56.907 -8.524 243.174 1.00140.24 C
ANISOU 2307 CZ ARG A 366 13200 21244 18842 2456 -4415 -4827 C
ATOM 2308 NH1 ARG A 366 55.834 -8.287 243.918 1.00138.58 N
ANISOU 2308 NH1 ARG A 366 13355 20865 18436 2441 -4457 -4636 N
ATOM 2309 NH2 ARG A 366 57.214 -9.771 242.839 1.00145.05 N
ANISOU 2309 NH2 ARG A 366 13866 21868 19380 2779 -4501 -4761 N
ATOM 2310 N GLU A 367 59.936 -4.593 238.958 1.00110.96 N
ANISOU 2310 N GLU A 367 7843 17848 16468 803 -3117 -5808 N
ATOM 2311 CA GLU A 367 61.198 -3.863 238.930 1.00114.52 C
ANISOU 2311 CA GLU A 367 7860 18530 17122 614 -3060 -6256 C
ATOM 2312 C GLU A 367 61.104 -2.650 238.015 1.00109.60 C
ANISOU 2312 C GLU A 367 7182 17767 16695 121 -2615 -6329 C
ATOM 2313 O GLU A 367 61.524 -1.544 238.384 1.00110.50 O
ANISOU 2313 O GLU A 367 7130 17969 16885 -148 -2529 -6605 O
ATOM 2314 CB GLU A 367 62.330 -4.785 238.477 1.00123.01 C
ANISOU 2314 CB GLU A 367 8623 19805 18312 845 -3155 -6465 C
ATOM 2315 CG GLU A 367 62.857 -5.726 239.551 1.00128.90 C
ANISOU 2315 CG GLU A 367 9312 20775 18889 1320 -3619 -6567 C
ATOM 2316 CD GLU A 367 64.043 -6.554 239.073 1.00135.93 C
ANISOU 2316 CD GLU A 367 9857 21878 19911 1539 -3702 -6812 C
ATOM 2317 OE1 GLU A 367 63.914 -7.249 238.040 1.00132.73 O
ANISOU 2317 OE1 GLU A 367 9511 21351 19570 1571 -3530 -6633 O
ATOM 2318 OE2 GLU A 367 65.107 -6.502 239.726 1.00140.62 O
ANISOU 2318 OE2 GLU A 367 10113 22767 20548 1679 -3942 -7193 O
ATOM 2319 N GLN A 368 60.549 -2.832 236.814 1.00112.82 N
ANISOU 2319 N GLN A 368 7751 17944 17171 -3 -2319 -6087 N
ATOM 2320 CA GLN A 368 60.450 -1.691 235.907 1.00116.82 C
ANISOU 2320 CA GLN A 368 8259 18287 17840 -451 -1884 -6154 C
ATOM 2321 C GLN A 368 59.508 -0.620 236.458 1.00116.19 C
ANISOU 2321 C GLN A 368 8437 18054 17656 -672 -1804 -6031 C
ATOM 2322 O GLN A 368 59.761 0.582 236.301 1.00112.00 O
ANISOU 2322 O GLN A 368 7833 17494 17227 -1029 -1541 -6243 O
ATOM 2323 CB GLN A 368 60.012 -2.159 234.519 1.00116.70 C
ANISOU 2323 CB GLN A 368 8397 18047 17897 -508 -1610 -5907 C
ATOM 2324 CG GLN A 368 61.056 -3.015 233.802 1.00118.23 C
ANISOU 2324 CG GLN A 368 8309 18376 18238 -378 -1604 -6080 C
ATOM 2325 CD GLN A 368 62.310 -2.240 233.410 1.00111.37 C
ANISOU 2325 CD GLN A 368 7064 17651 17601 -657 -1380 -6548 C
ATOM 2326 OE1 GLN A 368 62.489 -1.874 232.249 1.00108.64 O
ANISOU 2326 OE1 GLN A 368 6709 17160 17410 -927 -1006 -6606 O
ATOM 2327 NE2 GLN A 368 63.187 -2.003 234.377 1.00130.49 N
ANISOU 2327 NE2 GLN A 368 9182 20358 20041 -591 -1604 -6898 N
ATOM 2328 N PHE A 369 58.434 -1.031 237.141 1.00110.38 N
ANISOU 2328 N PHE A 369 8012 17217 16709 -467 -2019 -5709 N
ATOM 2329 CA PHE A 369 57.541 -0.053 237.760 1.00108.17 C
ANISOU 2329 CA PHE A 369 7970 16803 16325 -655 -1971 -5606 C
ATOM 2330 C PHE A 369 58.232 0.690 238.901 1.00114.32 C
ANISOU 2330 C PHE A 369 8556 17795 17086 -729 -2137 -5933 C
ATOM 2331 O PHE A 369 57.997 1.890 239.105 1.00112.94 O
ANISOU 2331 O PHE A 369 8446 17542 16924 -1043 -1956 -6015 O
ATOM 2332 CB PHE A 369 56.271 -0.743 238.264 1.00104.92 C
ANISOU 2332 CB PHE A 369 7921 16249 15695 -405 -2171 -5218 C
ATOM 2333 CG PHE A 369 55.416 -1.336 237.174 1.00 92.09 C
ANISOU 2333 CG PHE A 369 6514 14399 14076 -377 -1990 -4883 C
ATOM 2334 CD1 PHE A 369 55.529 -0.905 235.862 1.00 93.97 C
ANISOU 2334 CD1 PHE A 369 6710 14505 14488 -639 -1623 -4894 C
ATOM 2335 CD2 PHE A 369 54.493 -2.327 237.469 1.00 90.64 C
ANISOU 2335 CD2 PHE A 369 6597 14131 13713 -91 -2180 -4567 C
ATOM 2336 CE1 PHE A 369 54.738 -1.455 234.862 1.00 91.45 C
ANISOU 2336 CE1 PHE A 369 6596 13984 14168 -610 -1474 -4589 C
ATOM 2337 CE2 PHE A 369 53.696 -2.880 236.475 1.00 87.99 C
ANISOU 2337 CE2 PHE A 369 6450 13601 13381 -74 -2018 -4270 C
ATOM 2338 CZ PHE A 369 53.819 -2.442 235.170 1.00 86.42 C
ANISOU 2338 CZ PHE A 369 6193 13283 13361 -330 -1676 -4277 C
ATOM 2339 N LYS A 370 59.089 -0.004 239.656 1.00119.12 N
ANISOU 2339 N LYS A 370 8937 18668 17654 -439 -2483 -6128 N
ATOM 2340 CA LYS A 370 59.857 0.666 240.700 1.00120.67 C
ANISOU 2340 CA LYS A 370 8911 19095 17843 -504 -2658 -6474 C
ATOM 2341 C LYS A 370 60.812 1.686 240.101 1.00119.77 C
ANISOU 2341 C LYS A 370 8478 19070 17961 -888 -2339 -6853 C
ATOM 2342 O LYS A 370 60.977 2.789 240.635 1.00113.15 O
ANISOU 2342 O LYS A 370 7588 18273 17129 -1160 -2264 -7058 O
ATOM 2343 CB LYS A 370 60.633 -0.363 241.525 1.00117.04 C
ANISOU 2343 CB LYS A 370 8267 18905 17296 -80 -3098 -6620 C
ATOM 2344 CG LYS A 370 60.091 -0.607 242.921 1.00116.04 C
ANISOU 2344 CG LYS A 370 8385 18800 16906 176 -3477 -6498 C
ATOM 2345 CD LYS A 370 60.911 -1.663 243.645 1.00125.39 C
ANISOU 2345 CD LYS A 370 9415 20235 17993 625 -3900 -6651 C
ATOM 2346 CE LYS A 370 62.372 -1.253 243.754 1.00141.59 C
ANISOU 2346 CE LYS A 370 10966 22608 20225 545 -3957 -7144 C
ATOM 2347 NZ LYS A 370 63.187 -2.270 244.480 1.00149.72 N
ANISOU 2347 NZ LYS A 370 11841 23893 21154 1014 -4393 -7313 N
ATOM 2348 N ALA A 371 61.430 1.340 238.970 1.00120.57 N
ANISOU 2348 N ALA A 371 8384 19183 18244 -931 -2126 -6953 N
ATOM 2349 CA ALA A 371 62.297 2.294 238.288 1.00121.58 C
ANISOU 2349 CA ALA A 371 8246 19359 18588 -1316 -1766 -7317 C
ATOM 2350 C ALA A 371 61.510 3.490 237.774 1.00121.83 C
ANISOU 2350 C ALA A 371 8561 19101 18626 -1723 -1352 -7195 C
ATOM 2351 O ALA A 371 62.020 4.616 237.769 1.00126.83 O
ANISOU 2351 O ALA A 371 9072 19768 19349 -2074 -1102 -7500 O
ATOM 2352 CB ALA A 371 63.033 1.609 237.139 1.00116.96 C
ANISOU 2352 CB ALA A 371 7444 18811 18185 -1270 -1611 -7425 C
ATOM 2353 N ALA A 372 60.264 3.270 237.354 1.00119.33 N
ANISOU 2353 N ALA A 372 8634 18501 18207 -1676 -1272 -6764 N
ATOM 2354 CA ALA A 372 59.441 4.381 236.886 1.00116.49 C
ANISOU 2354 CA ALA A 372 8574 17855 17833 -2022 -900 -6632 C
ATOM 2355 C ALA A 372 59.076 5.314 238.033 1.00118.67 C
ANISOU 2355 C ALA A 372 8964 18143 17984 -2156 -990 -6681 C
ATOM 2356 O ALA A 372 59.198 6.538 237.916 1.00122.72 O
ANISOU 2356 O ALA A 372 9515 18574 18539 -2524 -679 -6858 O
ATOM 2357 CB ALA A 372 58.180 3.852 236.201 1.00110.82 C
ANISOU 2357 CB ALA A 372 8220 16854 17034 -1906 -834 -6170 C
ATOM 2358 N PHE A 373 58.629 4.750 239.156 1.00118.03 N
ANISOU 2358 N PHE A 373 8966 18149 17733 -1867 -1402 -6530 N
ATOM 2359 CA PHE A 373 58.254 5.588 240.291 1.00119.58 C
ANISOU 2359 CA PHE A 373 9294 18345 17795 -1987 -1508 -6568 C
ATOM 2360 C PHE A 373 59.459 6.298 240.897 1.00130.54 C
ANISOU 2360 C PHE A 373 10347 19993 19260 -2172 -1535 -7029 C
ATOM 2361 O PHE A 373 59.327 7.426 241.388 1.00127.57 O
ANISOU 2361 O PHE A 373 10066 19566 18841 -2462 -1405 -7143 O
ATOM 2362 CB PHE A 373 57.526 4.746 241.337 1.00117.71 C
ANISOU 2362 CB PHE A 373 9248 18131 17346 -1623 -1939 -6313 C
ATOM 2363 CG PHE A 373 56.202 4.225 240.861 1.00118.87 C
ANISOU 2363 CG PHE A 373 9751 18011 17402 -1496 -1887 -5878 C
ATOM 2364 CD1 PHE A 373 55.354 5.042 240.131 1.00115.98 C
ANISOU 2364 CD1 PHE A 373 9636 17364 17066 -1775 -1522 -5715 C
ATOM 2365 CD2 PHE A 373 55.817 2.919 241.111 1.00119.05 C
ANISOU 2365 CD2 PHE A 373 9867 18061 17307 -1097 -2188 -5645 C
ATOM 2366 CE1 PHE A 373 54.139 4.577 239.676 1.00112.07 C
ANISOU 2366 CE1 PHE A 373 9441 16642 16500 -1660 -1480 -5341 C
ATOM 2367 CE2 PHE A 373 54.601 2.445 240.656 1.00117.81 C
ANISOU 2367 CE2 PHE A 373 10020 17670 17071 -1001 -2124 -5270 C
ATOM 2368 CZ PHE A 373 53.760 3.277 239.937 1.00114.06 C
ANISOU 2368 CZ PHE A 373 9755 16939 16645 -1283 -1780 -5123 C
ATOM 2369 N SER A 374 60.636 5.668 240.873 1.00141.10 N
ANISOU 2369 N SER A 374 11291 21611 20709 -2013 -1696 -7311 N
ATOM 2370 CA SER A 374 61.826 6.333 241.395 1.00150.29 C
ANISOU 2370 CA SER A 374 12091 23047 21964 -2195 -1714 -7788 C
ATOM 2371 C SER A 374 62.228 7.531 240.544 1.00159.55 C
ANISOU 2371 C SER A 374 13205 24122 23296 -2677 -1188 -8036 C
ATOM 2372 O SER A 374 62.766 8.511 241.072 1.00166.88 O
ANISOU 2372 O SER A 374 14000 25164 24244 -2956 -1101 -8358 O
ATOM 2373 CB SER A 374 62.979 5.335 241.494 1.00152.99 C
ANISOU 2373 CB SER A 374 12016 23713 22399 -1892 -2004 -8045 C
ATOM 2374 OG SER A 374 62.602 4.207 242.264 1.00149.37 O
ANISOU 2374 OG SER A 374 11669 23321 21765 -1429 -2469 -7810 O
ATOM 2375 N TRP A 375 61.963 7.483 239.241 1.00163.85 N
ANISOU 2375 N TRP A 375 13875 24443 23937 -2786 -825 -7895 N
ATOM 2376 CA TRP A 375 62.321 8.576 238.342 1.00174.81 C
ANISOU 2376 CA TRP A 375 15270 25699 25452 -3229 -289 -8120 C
ATOM 2377 C TRP A 375 61.320 9.719 238.460 1.00181.45 C
ANISOU 2377 C TRP A 375 16532 26249 26164 -3512 -26 -7934 C
ATOM 2378 O TRP A 375 61.492 10.625 239.275 1.00189.90 O
ANISOU 2378 O TRP A 375 17592 27386 27176 -3725 -14 -8131 O
ATOM 2379 CB TRP A 375 62.399 8.080 236.895 1.00177.68 C
ANISOU 2379 CB TRP A 375 15655 25910 25945 -3227 -3 -8034 C
ATOM 2380 CG TRP A 375 62.125 9.144 235.873 1.00181.47 C
ANISOU 2380 CG TRP A 375 16403 26089 26460 -3628 568 -8042 C
ATOM 2381 CD1 TRP A 375 63.040 9.942 235.248 1.00185.18 C
ANISOU 2381 CD1 TRP A 375 16723 26573 27064 -3985 991 -8441 C
ATOM 2382 CD2 TRP A 375 60.843 9.520 235.353 1.00180.91 C
ANISOU 2382 CD2 TRP A 375 16819 25647 26272 -3701 787 -7643 C
ATOM 2383 NE1 TRP A 375 62.406 10.794 234.374 1.00184.66 N
ANISOU 2383 NE1 TRP A 375 17059 26153 26952 -4268 1468 -8300 N
ATOM 2384 CE2 TRP A 375 61.057 10.555 234.421 1.00182.88 C
ANISOU 2384 CE2 TRP A 375 17220 25691 26575 -4091 1339 -7810 C
ATOM 2385 CE3 TRP A 375 59.535 9.084 235.590 1.00173.59 C
ANISOU 2385 CE3 TRP A 375 16219 24544 25194 -3472 577 -7177 C
ATOM 2386 CZ2 TRP A 375 60.012 11.158 233.725 1.00180.08 C
ANISOU 2386 CZ2 TRP A 375 17343 24960 26119 -4232 1664 -7511 C
ATOM 2387 CZ3 TRP A 375 58.500 9.683 234.899 1.00167.77 C
ANISOU 2387 CZ3 TRP A 375 15913 23451 24380 -3626 894 -6901 C
ATOM 2388 CH2 TRP A 375 58.744 10.709 233.978 1.00172.41 C
ANISOU 2388 CH2 TRP A 375 16655 23838 25015 -3990 1423 -7060 C
TER 2389 TRP A 375
ATOM 2390 N TYR B 45 15.590 -46.959 200.582 1.00115.20 N
ANISOU 2390 N TYR B 45 15145 11697 16928 -2585 -2812 -2341 N
ATOM 2391 CA TYR B 45 16.277 -45.763 201.058 1.00113.87 C
ANISOU 2391 CA TYR B 45 14981 11805 16481 -2315 -2647 -2075 C
ATOM 2392 C TYR B 45 17.766 -46.036 201.276 1.00107.94 C
ANISOU 2392 C TYR B 45 14581 10983 15449 -2101 -2348 -1991 C
ATOM 2393 O TYR B 45 18.600 -45.150 201.089 1.00 99.05 O
ANISOU 2393 O TYR B 45 13589 10076 13971 -1871 -2305 -1899 O
ATOM 2394 CB TYR B 45 15.627 -45.257 202.353 1.00117.87 C
ANISOU 2394 CB TYR B 45 15111 12378 17297 -2351 -2439 -1804 C
ATOM 2395 CG TYR B 45 16.100 -43.890 202.813 1.00116.01 C
ANISOU 2395 CG TYR B 45 14825 12439 16814 -2102 -2328 -1564 C
ATOM 2396 CD1 TYR B 45 15.904 -42.762 202.025 1.00119.13 C
ANISOU 2396 CD1 TYR B 45 15180 13104 16982 -1992 -2613 -1601 C
ATOM 2397 CD2 TYR B 45 16.718 -43.726 204.048 1.00114.40 C
ANISOU 2397 CD2 TYR B 45 14627 12232 16607 -1981 -1952 -1301 C
ATOM 2398 CE1 TYR B 45 16.329 -41.510 202.446 1.00118.93 C
ANISOU 2398 CE1 TYR B 45 15115 13316 16758 -1778 -2503 -1388 C
ATOM 2399 CE2 TYR B 45 17.145 -42.480 204.478 1.00113.70 C
ANISOU 2399 CE2 TYR B 45 14493 12399 16307 -1771 -1861 -1109 C
ATOM 2400 CZ TYR B 45 16.948 -41.376 203.673 1.00113.06 C
ANISOU 2400 CZ TYR B 45 14364 12563 16030 -1676 -2125 -1157 C
ATOM 2401 OH TYR B 45 17.371 -40.134 204.093 1.00100.11 O
ANISOU 2401 OH TYR B 45 12688 11146 14205 -1479 -2025 -975 O
ATOM 2402 N ALA B 46 18.095 -47.271 201.668 1.00113.56 N
ANISOU 2402 N ALA B 46 15431 11373 16344 -2178 -2143 -2025 N
ATOM 2403 CA ALA B 46 19.481 -47.600 201.997 1.00105.42 C
ANISOU 2403 CA ALA B 46 14685 10251 15118 -1962 -1857 -1931 C
ATOM 2404 C ALA B 46 20.386 -47.541 200.771 1.00105.43 C
ANISOU 2404 C ALA B 46 15018 10315 14725 -1814 -1967 -2148 C
ATOM 2405 O ALA B 46 21.515 -47.033 200.845 1.00103.71 O
ANISOU 2405 O ALA B 46 14944 10227 14233 -1571 -1800 -2042 O
ATOM 2406 CB ALA B 46 19.545 -48.984 202.644 1.00 99.36 C
ANISOU 2406 CB ALA B 46 14000 9090 14663 -2074 -1639 -1919 C
ATOM 2407 N TRP B 47 19.910 -48.052 199.633 1.00111.57 N
ANISOU 2407 N TRP B 47 15921 11001 15468 -1964 -2240 -2464 N
ATOM 2408 CA TRP B 47 20.729 -48.047 198.426 1.00110.98 C
ANISOU 2408 CA TRP B 47 16202 10976 14991 -1835 -2320 -2690 C
ATOM 2409 C TRP B 47 21.022 -46.626 197.971 1.00106.81 C
ANISOU 2409 C TRP B 47 15684 10822 14079 -1660 -2414 -2591 C
ATOM 2410 O TRP B 47 22.157 -46.303 197.597 1.00108.64 O
ANISOU 2410 O TRP B 47 16154 11142 13983 -1452 -2257 -2588 O
ATOM 2411 CB TRP B 47 20.023 -48.829 197.318 1.00121.83 C
ANISOU 2411 CB TRP B 47 17713 12191 16386 -2050 -2633 -3060 C
ATOM 2412 CG TRP B 47 20.721 -48.769 195.994 1.00136.27 C
ANISOU 2412 CG TRP B 47 19892 14137 17747 -1919 -2687 -3282 C
ATOM 2413 CD1 TRP B 47 21.707 -49.602 195.550 1.00141.59 C
ANISOU 2413 CD1 TRP B 47 20875 14637 18286 -1816 -2465 -3443 C
ATOM 2414 CD2 TRP B 47 20.483 -47.830 194.934 1.00143.13 C
ANISOU 2414 CD2 TRP B 47 20820 15338 18225 -1861 -2935 -3339 C
ATOM 2415 NE1 TRP B 47 22.100 -49.239 194.284 1.00146.47 N
ANISOU 2415 NE1 TRP B 47 21733 15466 18454 -1713 -2537 -3606 N
ATOM 2416 CE2 TRP B 47 21.364 -48.155 193.883 1.00147.75 C
ANISOU 2416 CE2 TRP B 47 21766 15935 18437 -1738 -2827 -3533 C
ATOM 2417 CE3 TRP B 47 19.612 -46.747 194.774 1.00142.00 C
ANISOU 2417 CE3 TRP B 47 20457 15474 18022 -1887 -3223 -3231 C
ATOM 2418 CZ2 TRP B 47 21.400 -47.437 192.689 1.00149.53 C
ANISOU 2418 CZ2 TRP B 47 22162 16438 18213 -1656 -2987 -3605 C
ATOM 2419 CZ3 TRP B 47 19.650 -46.035 193.587 1.00143.34 C
ANISOU 2419 CZ3 TRP B 47 20803 15911 17750 -1787 -3404 -3296 C
ATOM 2420 CH2 TRP B 47 20.538 -46.384 192.561 1.00146.72 C
ANISOU 2420 CH2 TRP B 47 21614 16341 17791 -1680 -3281 -3474 C
ATOM 2421 N VAL B 48 20.013 -45.753 198.025 1.00106.83 N
ANISOU 2421 N VAL B 48 15414 11032 14144 -1737 -2649 -2503 N
ATOM 2422 CA VAL B 48 20.216 -44.360 197.648 1.00104.04 C
ANISOU 2422 CA VAL B 48 15065 11007 13459 -1572 -2740 -2382 C
ATOM 2423 C VAL B 48 21.215 -43.701 198.582 1.00 95.14 C
ANISOU 2423 C VAL B 48 13897 9985 12267 -1359 -2389 -2099 C
ATOM 2424 O VAL B 48 22.033 -42.880 198.152 1.00 94.96 O
ANISOU 2424 O VAL B 48 14036 10143 11902 -1179 -2323 -2048 O
ATOM 2425 CB VAL B 48 18.870 -43.612 197.642 1.00104.56 C
ANISOU 2425 CB VAL B 48 14805 11238 13684 -1686 -3060 -2331 C
ATOM 2426 CG1 VAL B 48 19.077 -42.139 197.320 1.00104.57 C
ANISOU 2426 CG1 VAL B 48 14820 11547 13366 -1499 -3140 -2176 C
ATOM 2427 CG2 VAL B 48 17.908 -44.252 196.656 1.00108.17 C
ANISOU 2427 CG2 VAL B 48 15293 11604 14203 -1896 -3461 -2637 C
ATOM 2428 N LEU B 49 21.204 -44.083 199.859 1.00 91.87 N
ANISOU 2428 N LEU B 49 13287 9448 12170 -1382 -2153 -1920 N
ATOM 2429 CA LEU B 49 22.131 -43.490 200.815 1.00 85.40 C
ANISOU 2429 CA LEU B 49 12425 8729 11293 -1185 -1855 -1664 C
ATOM 2430 C LEU B 49 23.563 -43.900 200.507 1.00 88.37 C
ANISOU 2430 C LEU B 49 13095 9029 11454 -1011 -1645 -1730 C
ATOM 2431 O LEU B 49 24.471 -43.056 200.476 1.00 87.94 O
ANISOU 2431 O LEU B 49 13098 9153 11162 -826 -1522 -1634 O
ATOM 2432 CB LEU B 49 21.741 -43.902 202.233 1.00 85.51 C
ANISOU 2432 CB LEU B 49 12210 8616 11665 -1255 -1667 -1467 C
ATOM 2433 CG LEU B 49 22.380 -43.159 203.404 1.00 87.41 C
ANISOU 2433 CG LEU B 49 12345 8990 11875 -1084 -1420 -1187 C
ATOM 2434 CD1 LEU B 49 22.029 -41.682 203.344 1.00 82.05 C
ANISOU 2434 CD1 LEU B 49 11500 8610 11063 -1024 -1527 -1084 C
ATOM 2435 CD2 LEU B 49 21.916 -43.773 204.715 1.00 88.05 C
ANISOU 2435 CD2 LEU B 49 12271 8907 12279 -1177 -1240 -1017 C
ATOM 2436 N ILE B 50 23.785 -45.194 200.257 1.00 95.15 N
ANISOU 2436 N ILE B 50 14130 9607 12415 -1069 -1595 -1907 N
ATOM 2437 CA ILE B 50 25.139 -45.643 199.942 1.00 92.81 C
ANISOU 2437 CA ILE B 50 14092 9217 11954 -888 -1384 -1991 C
ATOM 2438 C ILE B 50 25.623 -45.007 198.647 1.00 88.41 C
ANISOU 2438 C ILE B 50 13758 8839 10993 -804 -1460 -2154 C
ATOM 2439 O ILE B 50 26.786 -44.597 198.533 1.00 83.60 O
ANISOU 2439 O ILE B 50 13253 8322 10189 -611 -1254 -2115 O
ATOM 2440 CB ILE B 50 25.200 -47.180 199.860 1.00 90.13 C
ANISOU 2440 CB ILE B 50 13912 8510 11823 -966 -1324 -2171 C
ATOM 2441 CG1 ILE B 50 24.742 -47.806 201.176 1.00 92.80 C
ANISOU 2441 CG1 ILE B 50 14061 8650 12547 -1051 -1215 -1972 C
ATOM 2442 CG2 ILE B 50 26.613 -47.637 199.515 1.00 83.45 C
ANISOU 2442 CG2 ILE B 50 13312 7561 10835 -753 -1094 -2271 C
ATOM 2443 CD1 ILE B 50 24.829 -49.318 201.183 1.00 96.05 C
ANISOU 2443 CD1 ILE B 50 14639 8659 13196 -1121 -1132 -2115 C
ATOM 2444 N ALA B 51 24.735 -44.891 197.656 1.00 82.70 N
ANISOU 2444 N ALA B 51 13113 8171 10139 -949 -1758 -2334 N
ATOM 2445 CA ALA B 51 25.154 -44.326 196.379 1.00 81.32 C
ANISOU 2445 CA ALA B 51 13212 8154 9532 -873 -1833 -2483 C
ATOM 2446 C ALA B 51 25.483 -42.846 196.512 1.00 85.94 C
ANISOU 2446 C ALA B 51 13704 9037 9912 -737 -1783 -2252 C
ATOM 2447 O ALA B 51 26.483 -42.376 195.955 1.00 88.00 O
ANISOU 2447 O ALA B 51 14165 9397 9875 -591 -1611 -2268 O
ATOM 2448 CB ALA B 51 24.071 -44.548 195.325 1.00 84.87 C
ANISOU 2448 CB ALA B 51 13778 8596 9873 -1056 -2216 -2722 C
ATOM 2449 N ALA B 52 24.673 -42.100 197.266 1.00 83.08 N
ANISOU 2449 N ALA B 52 13036 8804 9725 -786 -1901 -2041 N
ATOM 2450 CA ALA B 52 24.958 -40.684 197.451 1.00 69.96 C
ANISOU 2450 CA ALA B 52 11284 7394 7902 -661 -1849 -1825 C
ATOM 2451 C ALA B 52 26.262 -40.485 198.205 1.00 74.96 C
ANISOU 2451 C ALA B 52 11890 8040 8551 -489 -1489 -1682 C
ATOM 2452 O ALA B 52 27.067 -39.613 197.845 1.00 79.09 O
ANISOU 2452 O ALA B 52 12510 8712 8828 -363 -1362 -1624 O
ATOM 2453 CB ALA B 52 23.801 -40.009 198.185 1.00 62.75 C
ANISOU 2453 CB ALA B 52 10036 6586 7222 -742 -2026 -1648 C
ATOM 2454 N TYR B 53 26.517 -41.315 199.221 1.00 77.28 N
ANISOU 2454 N TYR B 53 12062 8167 9134 -483 -1327 -1628 N
ATOM 2455 CA TYR B 53 27.762 -41.177 199.967 1.00 71.60 C
ANISOU 2455 CA TYR B 53 11301 7460 8445 -308 -1033 -1501 C
ATOM 2456 C TYR B 53 28.969 -41.506 199.097 1.00 71.19 C
ANISOU 2456 C TYR B 53 11506 7360 8185 -186 -852 -1671 C
ATOM 2457 O TYR B 53 29.978 -40.797 199.143 1.00 73.43 O
ANISOU 2457 O TYR B 53 11780 7768 8351 -44 -662 -1596 O
ATOM 2458 CB TYR B 53 27.737 -42.065 201.212 1.00 71.76 C
ANISOU 2458 CB TYR B 53 11176 7295 8796 -315 -929 -1398 C
ATOM 2459 CG TYR B 53 27.343 -41.347 202.484 1.00 73.34 C
ANISOU 2459 CG TYR B 53 11106 7613 9147 -312 -909 -1141 C
ATOM 2460 CD1 TYR B 53 26.017 -41.294 202.894 1.00 78.07 C
ANISOU 2460 CD1 TYR B 53 11532 8210 9922 -475 -1061 -1076 C
ATOM 2461 CD2 TYR B 53 28.299 -40.729 203.281 1.00 74.38 C
ANISOU 2461 CD2 TYR B 53 11150 7855 9255 -150 -732 -980 C
ATOM 2462 CE1 TYR B 53 25.653 -40.636 204.061 1.00 73.61 C
ANISOU 2462 CE1 TYR B 53 10737 7749 9482 -468 -1006 -856 C
ATOM 2463 CE2 TYR B 53 27.947 -40.074 204.449 1.00 70.38 C
ANISOU 2463 CE2 TYR B 53 10431 7455 8857 -146 -711 -768 C
ATOM 2464 CZ TYR B 53 26.623 -40.031 204.834 1.00 71.00 C
ANISOU 2464 CZ TYR B 53 10365 7527 9085 -302 -832 -706 C
ATOM 2465 OH TYR B 53 26.274 -39.377 205.997 1.00 71.04 O
ANISOU 2465 OH TYR B 53 10177 7634 9183 -293 -775 -510 O
ATOM 2466 N VAL B 54 28.881 -42.558 198.279 1.00 74.43 N
ANISOU 2466 N VAL B 54 12142 7584 8555 -245 -896 -1916 N
ATOM 2467 CA VAL B 54 30.027 -42.937 197.455 1.00 77.26 C
ANISOU 2467 CA VAL B 54 12750 7878 8725 -122 -683 -2099 C
ATOM 2468 C VAL B 54 30.282 -41.898 196.368 1.00 75.13 C
ANISOU 2468 C VAL B 54 12661 7824 8061 -92 -680 -2141 C
ATOM 2469 O VAL B 54 31.439 -41.568 196.062 1.00 72.45 O
ANISOU 2469 O VAL B 54 12404 7543 7581 47 -413 -2157 O
ATOM 2470 CB VAL B 54 29.816 -44.338 196.858 1.00 81.56 C
ANISOU 2470 CB VAL B 54 13515 8149 9326 -198 -727 -2374 C
ATOM 2471 CG1 VAL B 54 30.941 -44.670 195.895 1.00 83.28 C
ANISOU 2471 CG1 VAL B 54 14012 8309 9320 -68 -491 -2593 C
ATOM 2472 CG2 VAL B 54 29.734 -45.375 197.966 1.00 82.18 C
ANISOU 2472 CG2 VAL B 54 13443 7978 9803 -205 -673 -2302 C
ATOM 2473 N ALA B 55 29.215 -41.361 195.769 1.00 78.44 N
ANISOU 2473 N ALA B 55 13141 8358 8306 -219 -971 -2152 N
ATOM 2474 CA ALA B 55 29.396 -40.326 194.760 1.00 73.19 C
ANISOU 2474 CA ALA B 55 12679 7887 7242 -185 -985 -2151 C
ATOM 2475 C ALA B 55 30.018 -39.078 195.369 1.00 78.74 C
ANISOU 2475 C ALA B 55 13195 8772 7951 -77 -806 -1896 C
ATOM 2476 O ALA B 55 30.954 -38.501 194.799 1.00 85.75 O
ANISOU 2476 O ALA B 55 14235 9745 8603 16 -577 -1897 O
ATOM 2477 CB ALA B 55 28.059 -39.994 194.101 1.00 71.37 C
ANISOU 2477 CB ALA B 55 12523 7738 6858 -324 -1388 -2187 C
ATOM 2478 N VAL B 56 29.538 -38.666 196.546 1.00 72.26 N
ANISOU 2478 N VAL B 56 12047 8000 7407 -94 -882 -1686 N
ATOM 2479 CA VAL B 56 30.116 -37.497 197.197 1.00 67.93 C
ANISOU 2479 CA VAL B 56 11318 7607 6884 -1 -725 -1466 C
ATOM 2480 C VAL B 56 31.565 -37.764 197.577 1.00 71.48 C
ANISOU 2480 C VAL B 56 11730 8009 7420 135 -382 -1480 C
ATOM 2481 O VAL B 56 32.422 -36.884 197.460 1.00 72.13 O
ANISOU 2481 O VAL B 56 11805 8205 7396 214 -184 -1408 O
ATOM 2482 CB VAL B 56 29.270 -37.099 198.420 1.00 61.26 C
ANISOU 2482 CB VAL B 56 10150 6809 6316 -48 -868 -1269 C
ATOM 2483 CG1 VAL B 56 30.088 -36.239 199.376 1.00 65.35 C
ANISOU 2483 CG1 VAL B 56 10466 7429 6933 59 -660 -1084 C
ATOM 2484 CG2 VAL B 56 28.014 -36.365 197.973 1.00 53.69 C
ANISOU 2484 CG2 VAL B 56 9184 5956 5259 -140 -1171 -1218 C
ATOM 2485 N PHE B 57 31.871 -38.997 197.979 1.00 72.77 N
ANISOU 2485 N PHE B 57 11871 7988 7791 164 -308 -1582 N
ATOM 2486 CA PHE B 57 33.231 -39.348 198.374 1.00 72.67 C
ANISOU 2486 CA PHE B 57 11792 7914 7906 317 -15 -1602 C
ATOM 2487 C PHE B 57 34.190 -39.202 197.198 1.00 73.32 C
ANISOU 2487 C PHE B 57 12105 8021 7733 385 222 -1761 C
ATOM 2488 O PHE B 57 35.201 -38.485 197.281 1.00 71.30 O
ANISOU 2488 O PHE B 57 11757 7867 7466 479 454 -1699 O
ATOM 2489 CB PHE B 57 33.217 -40.782 198.913 1.00 74.57 C
ANISOU 2489 CB PHE B 57 12010 7914 8408 338 -20 -1683 C
ATOM 2490 CG PHE B 57 34.546 -41.295 199.395 1.00 70.78 C
ANISOU 2490 CG PHE B 57 11441 7341 8110 522 233 -1701 C
ATOM 2491 CD1 PHE B 57 35.045 -40.924 200.633 1.00 67.91 C
ANISOU 2491 CD1 PHE B 57 10807 7042 7953 620 277 -1505 C
ATOM 2492 CD2 PHE B 57 35.264 -42.204 198.634 1.00 68.13 C
ANISOU 2492 CD2 PHE B 57 11292 6841 7754 604 408 -1928 C
ATOM 2493 CE1 PHE B 57 36.255 -41.420 201.083 1.00 67.04 C
ANISOU 2493 CE1 PHE B 57 10596 6847 8031 803 462 -1524 C
ATOM 2494 CE2 PHE B 57 36.473 -42.703 199.079 1.00 67.70 C
ANISOU 2494 CE2 PHE B 57 11123 6690 7910 794 627 -1949 C
ATOM 2495 CZ PHE B 57 36.968 -42.312 200.305 1.00 66.03 C
ANISOU 2495 CZ PHE B 57 10622 6554 7913 897 637 -1742 C
ATOM 2496 N VAL B 58 33.856 -39.838 196.073 1.00 69.24 N
ANISOU 2496 N VAL B 58 11894 7413 7000 326 171 -1977 N
ATOM 2497 CA VAL B 58 34.736 -39.793 194.911 1.00 74.22 C
ANISOU 2497 CA VAL B 58 12792 8054 7354 388 431 -2148 C
ATOM 2498 C VAL B 58 34.859 -38.365 194.391 1.00 82.09 C
ANISOU 2498 C VAL B 58 13857 9266 8069 369 490 -2016 C
ATOM 2499 O VAL B 58 35.966 -37.873 194.127 1.00 85.01 O
ANISOU 2499 O VAL B 58 14231 9692 8375 453 815 -2014 O
ATOM 2500 CB VAL B 58 34.223 -40.750 193.821 1.00 75.27 C
ANISOU 2500 CB VAL B 58 13280 8047 7271 314 325 -2420 C
ATOM 2501 CG1 VAL B 58 35.140 -40.720 192.601 1.00 75.16 C
ANISOU 2501 CG1 VAL B 58 13583 8043 6932 382 633 -2609 C
ATOM 2502 CG2 VAL B 58 34.102 -42.159 194.376 1.00 77.89 C
ANISOU 2502 CG2 VAL B 58 13545 8128 7921 324 281 -2541 C
ATOM 2503 N VAL B 59 33.726 -37.668 194.257 1.00 77.36 N
ANISOU 2503 N VAL B 59 13296 8774 7324 260 185 -1899 N
ATOM 2504 CA VAL B 59 33.763 -36.329 193.682 1.00 71.26 C
ANISOU 2504 CA VAL B 59 12638 8173 6266 248 221 -1764 C
ATOM 2505 C VAL B 59 34.541 -35.381 194.582 1.00 77.47 C
ANISOU 2505 C VAL B 59 13123 9053 7261 314 427 -1563 C
ATOM 2506 O VAL B 59 35.350 -34.580 194.103 1.00 76.33 O
ANISOU 2506 O VAL B 59 13061 8982 6960 347 689 -1520 O
ATOM 2507 CB VAL B 59 32.335 -35.818 193.422 1.00 68.27 C
ANISOU 2507 CB VAL B 59 12329 7873 5739 143 -189 -1675 C
ATOM 2508 CG1 VAL B 59 32.372 -34.365 192.991 1.00 64.16 C
ANISOU 2508 CG1 VAL B 59 11903 7506 4972 153 -160 -1488 C
ATOM 2509 CG2 VAL B 59 31.659 -36.665 192.363 1.00 72.67 C
ANISOU 2509 CG2 VAL B 59 13217 8353 6042 70 -405 -1904 C
ATOM 2510 N ALA B 60 34.341 -35.469 195.899 1.00 74.15 N
ANISOU 2510 N ALA B 60 12358 8621 7193 328 326 -1445 N
ATOM 2511 CA ALA B 60 35.038 -34.554 196.791 1.00 67.53 C
ANISOU 2511 CA ALA B 60 11241 7875 6544 383 480 -1276 C
ATOM 2512 C ALA B 60 36.535 -34.818 196.787 1.00 72.23 C
ANISOU 2512 C ALA B 60 11766 8432 7245 489 844 -1369 C
ATOM 2513 O ALA B 60 37.331 -33.876 196.681 1.00 79.02 O
ANISOU 2513 O ALA B 60 12566 9378 8078 508 1068 -1303 O
ATOM 2514 CB ALA B 60 34.469 -34.660 198.204 1.00 55.38 C
ANISOU 2514 CB ALA B 60 9391 6332 5317 377 288 -1145 C
ATOM 2515 N LEU B 61 36.943 -36.090 196.856 1.00 78.06 N
ANISOU 2515 N LEU B 61 12507 9029 8124 560 917 -1532 N
ATOM 2516 CA LEU B 61 38.373 -36.377 196.839 1.00 74.11 C
ANISOU 2516 CA LEU B 61 11906 8485 7766 684 1259 -1634 C
ATOM 2517 C LEU B 61 39.013 -35.863 195.555 1.00 74.36 C
ANISOU 2517 C LEU B 61 12183 8564 7504 671 1559 -1727 C
ATOM 2518 O LEU B 61 40.002 -35.114 195.591 1.00 81.20 O
ANISOU 2518 O LEU B 61 12907 9504 8442 705 1833 -1684 O
ATOM 2519 CB LEU B 61 38.613 -37.881 196.992 1.00 71.30 C
ANISOU 2519 CB LEU B 61 11559 7936 7594 777 1278 -1802 C
ATOM 2520 CG LEU B 61 38.256 -38.483 198.351 1.00 76.07 C
ANISOU 2520 CG LEU B 61 11918 8463 8520 817 1061 -1695 C
ATOM 2521 CD1 LEU B 61 38.749 -39.909 198.428 1.00 71.81 C
ANISOU 2521 CD1 LEU B 61 11400 7706 8179 938 1144 -1854 C
ATOM 2522 CD2 LEU B 61 38.860 -37.645 199.464 1.00 69.36 C
ANISOU 2522 CD2 LEU B 61 10730 7739 7883 877 1088 -1516 C
ATOM 2523 N VAL B 62 38.435 -36.223 194.403 1.00 71.53 N
ANISOU 2523 N VAL B 62 12209 8165 6804 610 1511 -1856 N
ATOM 2524 CA VAL B 62 39.046 -35.847 193.133 1.00 69.93 C
ANISOU 2524 CA VAL B 62 12306 7994 6271 603 1825 -1955 C
ATOM 2525 C VAL B 62 39.059 -34.332 192.971 1.00 74.11 C
ANISOU 2525 C VAL B 62 12844 8674 6640 534 1884 -1744 C
ATOM 2526 O VAL B 62 40.084 -33.743 192.602 1.00 84.28 O
ANISOU 2526 O VAL B 62 14125 9998 7901 552 2260 -1740 O
ATOM 2527 CB VAL B 62 38.317 -36.542 191.967 1.00 70.83 C
ANISOU 2527 CB VAL B 62 12834 8048 6029 544 1687 -2124 C
ATOM 2528 CG1 VAL B 62 38.906 -36.108 190.627 1.00 74.80 C
ANISOU 2528 CG1 VAL B 62 13535 8636 6251 517 1939 -2132 C
ATOM 2529 CG2 VAL B 62 38.397 -38.054 192.124 1.00 70.16 C
ANISOU 2529 CG2 VAL B 62 12730 7781 6146 608 1664 -2343 C
ATOM 2530 N GLY B 63 37.945 -33.668 193.290 1.00 66.99 N
ANISOU 2530 N GLY B 63 11934 7848 5673 454 1532 -1564 N
ATOM 2531 CA GLY B 63 37.861 -32.243 193.038 1.00 62.98 C
ANISOU 2531 CA GLY B 63 11488 7450 4993 396 1570 -1365 C
ATOM 2532 C GLY B 63 38.748 -31.428 193.953 1.00 71.27 C
ANISOU 2532 C GLY B 63 12168 8547 6365 418 1776 -1239 C
ATOM 2533 O GLY B 63 39.362 -30.450 193.523 1.00 82.81 O
ANISOU 2533 O GLY B 63 13690 10050 7725 385 2043 -1157 O
ATOM 2534 N ASN B 64 38.868 -31.832 195.214 1.00 67.34 N
ANISOU 2534 N ASN B 64 11297 8035 6255 469 1664 -1229 N
ATOM 2535 CA ASN B 64 39.722 -31.054 196.098 1.00 68.63 C
ANISOU 2535 CA ASN B 64 11111 8251 6715 487 1822 -1133 C
ATOM 2536 C ASN B 64 41.201 -31.317 195.832 1.00 73.39 C
ANISOU 2536 C ASN B 64 11604 8819 7461 552 2240 -1274 C
ATOM 2537 O ASN B 64 42.022 -30.382 195.918 1.00 78.06 O
ANISOU 2537 O ASN B 64 12040 9458 8163 520 2485 -1214 O
ATOM 2538 CB ASN B 64 39.329 -31.319 197.550 1.00 64.95 C
ANISOU 2538 CB ASN B 64 10316 7793 6568 524 1545 -1063 C
ATOM 2539 CG ASN B 64 37.966 -30.738 197.881 1.00 67.81 C
ANISOU 2539 CG ASN B 64 10721 8205 6838 450 1204 -904 C
ATOM 2540 OD1 ASN B 64 37.837 -29.537 198.141 1.00 69.75 O
ANISOU 2540 OD1 ASN B 64 10897 8519 7088 402 1189 -757 O
ATOM 2541 ND2 ASN B 64 36.935 -31.580 197.838 1.00 63.05 N
ANISOU 2541 ND2 ASN B 64 10229 7554 6172 437 939 -943 N
ATOM 2542 N THR B 65 41.562 -32.548 195.444 1.00 67.14 N
ANISOU 2542 N THR B 65 10894 7936 6682 636 2348 -1471 N
ATOM 2543 CA THR B 65 42.930 -32.763 194.995 1.00 75.91 C
ANISOU 2543 CA THR B 65 11927 9010 7906 703 2786 -1621 C
ATOM 2544 C THR B 65 43.226 -31.931 193.754 1.00 84.80 C
ANISOU 2544 C THR B 65 13357 10170 8695 612 3116 -1608 C
ATOM 2545 O THR B 65 44.328 -31.388 193.610 1.00 88.69 O
ANISOU 2545 O THR B 65 13656 10689 9354 596 3445 -1602 O
ATOM 2546 CB THR B 65 43.167 -34.246 194.712 1.00 81.93 C
ANISOU 2546 CB THR B 65 12769 9642 8719 821 2846 -1847 C
ATOM 2547 OG1 THR B 65 42.740 -35.029 195.832 1.00 79.94 O
ANISOU 2547 OG1 THR B 65 12301 9335 8739 894 2518 -1823 O
ATOM 2548 CG2 THR B 65 44.650 -34.512 194.454 1.00 77.87 C
ANISOU 2548 CG2 THR B 65 12058 9092 8438 918 3276 -1997 C
ATOM 2549 N LEU B 66 42.245 -31.798 192.856 1.00 88.41 N
ANISOU 2549 N LEU B 66 14225 10640 8728 535 2947 -1559 N
ATOM 2550 CA LEU B 66 42.445 -30.961 191.678 1.00 82.93 C
ANISOU 2550 CA LEU B 66 13767 9991 7750 438 3127 -1459 C
ATOM 2551 C LEU B 66 42.564 -29.488 192.039 1.00 80.10 C
ANISOU 2551 C LEU B 66 13305 9689 7438 355 3207 -1246 C
ATOM 2552 O LEU B 66 43.298 -28.753 191.377 1.00 74.49 O
ANISOU 2552 O LEU B 66 12625 8985 6695 289 3502 -1177 O
ATOM 2553 CB LEU B 66 41.311 -31.170 190.680 1.00 73.81 C
ANISOU 2553 CB LEU B 66 13045 8841 6157 392 2852 -1445 C
ATOM 2554 CG LEU B 66 41.288 -32.564 190.058 1.00 71.46 C
ANISOU 2554 CG LEU B 66 12895 8476 5781 447 2825 -1674 C
ATOM 2555 CD1 LEU B 66 40.241 -32.634 188.961 1.00 82.94 C
ANISOU 2555 CD1 LEU B 66 14764 9950 6799 386 2560 -1662 C
ATOM 2556 CD2 LEU B 66 42.668 -32.932 189.521 1.00 73.52 C
ANISOU 2556 CD2 LEU B 66 13057 8704 6173 494 3263 -1804 C
ATOM 2557 N VAL B 67 41.863 -29.038 193.081 1.00 78.00 N
ANISOU 2557 N VAL B 67 12900 9455 7282 350 2937 -1133 N
ATOM 2558 CA VAL B 67 42.005 -27.648 193.513 1.00 75.81 C
ANISOU 2558 CA VAL B 67 12467 9217 7121 269 2983 -934 C
ATOM 2559 C VAL B 67 43.433 -27.391 193.979 1.00 74.14 C
ANISOU 2559 C VAL B 67 11879 8999 7292 268 3357 -1000 C
ATOM 2560 O VAL B 67 44.075 -26.399 193.592 1.00 73.55 O
ANISOU 2560 O VAL B 67 11809 8915 7223 176 3661 -917 O
ATOM 2561 CB VAL B 67 40.982 -27.323 194.619 1.00 72.06 C
ANISOU 2561 CB VAL B 67 11794 8784 6803 267 2525 -796 C
ATOM 2562 CG1 VAL B 67 41.262 -25.954 195.218 1.00 61.67 C
ANISOU 2562 CG1 VAL B 67 10269 7488 5676 194 2590 -632 C
ATOM 2563 CG2 VAL B 67 39.563 -27.397 194.075 1.00 74.45 C
ANISOU 2563 CG2 VAL B 67 12438 9095 6754 253 2169 -720 C
ATOM 2564 N CYS B 68 43.965 -28.306 194.795 1.00 77.75 N
ANISOU 2564 N CYS B 68 11988 9450 8101 370 3317 -1146 N
ATOM 2565 CA CYS B 68 45.347 -28.149 195.243 1.00 79.32 C
ANISOU 2565 CA CYS B 68 11788 9649 8700 388 3632 -1233 C
ATOM 2566 C CYS B 68 46.319 -28.206 194.067 1.00 81.07 C
ANISOU 2566 C CYS B 68 12111 9837 8855 355 4045 -1313 C
ATOM 2567 O CYS B 68 47.244 -27.386 193.972 1.00 87.45 O
ANISOU 2567 O CYS B 68 12722 10647 9857 269 4312 -1272 O
ATOM 2568 CB CYS B 68 45.687 -29.219 196.281 1.00 71.96 C
ANISOU 2568 CB CYS B 68 10494 8712 8137 534 3449 -1359 C
ATOM 2569 SG CYS B 68 44.695 -29.114 197.796 1.00 74.67 S
ANISOU 2569 SG CYS B 68 10631 9109 8632 553 2893 -1215 S
ATOM 2570 N LEU B 69 46.102 -29.137 193.136 1.00 79.90 N
ANISOU 2570 N LEU B 69 12255 9654 8450 406 4046 -1410 N
ATOM 2571 CA LEU B 69 46.993 -29.251 191.987 1.00 85.28 C
ANISOU 2571 CA LEU B 69 13032 10308 9065 378 4389 -1475 C
ATOM 2572 C LEU B 69 46.926 -28.016 191.103 1.00 85.15 C
ANISOU 2572 C LEU B 69 13283 10292 8778 227 4549 -1294 C
ATOM 2573 O LEU B 69 47.939 -27.613 190.520 1.00 85.49 O
ANISOU 2573 O LEU B 69 13260 10309 8914 166 4905 -1299 O
ATOM 2574 CB LEU B 69 46.642 -30.495 191.176 1.00 94.54 C
ANISOU 2574 CB LEU B 69 14497 11439 9985 460 4327 -1625 C
ATOM 2575 CG LEU B 69 47.237 -31.813 191.672 1.00 97.86 C
ANISOU 2575 CG LEU B 69 14647 11810 10726 619 4342 -1837 C
ATOM 2576 CD1 LEU B 69 46.407 -32.995 191.196 1.00102.14 C
ANISOU 2576 CD1 LEU B 69 15508 12293 11008 686 4131 -1963 C
ATOM 2577 CD2 LEU B 69 48.677 -31.943 191.189 1.00105.30 C
ANISOU 2577 CD2 LEU B 69 15374 12733 11902 644 4746 -1942 C
ATOM 2578 N ALA B 70 45.751 -27.396 191.007 1.00 81.35 N
ANISOU 2578 N ALA B 70 13101 9828 7980 172 4286 -1128 N
ATOM 2579 CA ALA B 70 45.605 -26.213 190.174 1.00 80.17 C
ANISOU 2579 CA ALA B 70 13235 9658 7569 51 4397 -933 C
ATOM 2580 C ALA B 70 46.372 -25.044 190.765 1.00 86.24 C
ANISOU 2580 C ALA B 70 13696 10405 8666 -49 4615 -829 C
ATOM 2581 O ALA B 70 47.118 -24.358 190.058 1.00 94.14 O
ANISOU 2581 O ALA B 70 14750 11352 9667 -142 4938 -770 O
ATOM 2582 CB ALA B 70 44.126 -25.864 190.017 1.00 77.05 C
ANISOU 2582 CB ALA B 70 13192 9283 6801 43 4005 -778 C
ATOM 2583 N VAL B 71 46.213 -24.805 192.070 1.00 87.66 N
ANISOU 2583 N VAL B 71 13551 10618 9139 -36 4448 -818 N
ATOM 2584 CA VAL B 71 46.964 -23.695 192.653 1.00 86.20 C
ANISOU 2584 CA VAL B 71 13051 10406 9294 -144 4639 -746 C
ATOM 2585 C VAL B 71 48.465 -23.971 192.616 1.00 99.22 C
ANISOU 2585 C VAL B 71 14339 12038 11321 -155 4982 -902 C
ATOM 2586 O VAL B 71 49.265 -23.040 192.452 1.00104.50 O
ANISOU 2586 O VAL B 71 14879 12651 12176 -281 5249 -847 O
ATOM 2587 CB VAL B 71 46.484 -23.385 194.080 1.00 80.03 C
ANISOU 2587 CB VAL B 71 11992 9670 8746 -128 4381 -719 C
ATOM 2588 CG1 VAL B 71 47.227 -22.171 194.634 1.00 79.78 C
ANISOU 2588 CG1 VAL B 71 11652 9600 9063 -262 4560 -657 C
ATOM 2589 CG2 VAL B 71 44.989 -23.134 194.086 1.00 78.03 C
ANISOU 2589 CG2 VAL B 71 12094 9431 8124 -111 4044 -564 C
ATOM 2590 N TRP B 72 48.879 -25.238 192.746 1.00 98.35 N
ANISOU 2590 N TRP B 72 14062 11960 11348 -22 4976 -1098 N
ATOM 2591 CA TRP B 72 50.310 -25.542 192.723 1.00 99.31 C
ANISOU 2591 CA TRP B 72 13816 12065 11851 -10 5276 -1247 C
ATOM 2592 C TRP B 72 50.902 -25.373 191.328 1.00102.00 C
ANISOU 2592 C TRP B 72 14418 12344 11996 -85 5648 -1237 C
ATOM 2593 O TRP B 72 52.023 -24.872 191.180 1.00103.59 O
ANISOU 2593 O TRP B 72 14378 12503 12478 -171 5963 -1263 O
ATOM 2594 CB TRP B 72 50.551 -26.963 193.241 1.00105.64 C
ANISOU 2594 CB TRP B 72 14386 12899 12854 178 5148 -1447 C
ATOM 2595 CG TRP B 72 51.912 -27.530 192.920 1.00113.00 C
ANISOU 2595 CG TRP B 72 15040 13807 14089 230 5445 -1610 C
ATOM 2596 CD1 TRP B 72 53.101 -27.198 193.506 1.00113.92 C
ANISOU 2596 CD1 TRP B 72 14664 13929 14692 206 5586 -1675 C
ATOM 2597 CD2 TRP B 72 52.212 -28.546 191.954 1.00118.84 C
ANISOU 2597 CD2 TRP B 72 15969 14511 14674 318 5622 -1739 C
ATOM 2598 NE1 TRP B 72 54.122 -27.937 192.957 1.00122.64 N
ANISOU 2598 NE1 TRP B 72 15635 15003 15960 280 5846 -1826 N
ATOM 2599 CE2 TRP B 72 53.603 -28.772 192.001 1.00124.89 C
ANISOU 2599 CE2 TRP B 72 16337 15260 15855 352 5889 -1870 C
ATOM 2600 CE3 TRP B 72 51.441 -29.283 191.050 1.00122.55 C
ANISOU 2600 CE3 TRP B 72 16902 14959 14703 370 5570 -1769 C
ATOM 2601 CZ2 TRP B 72 54.239 -29.701 191.178 1.00131.38 C
ANISOU 2601 CZ2 TRP B 72 17217 16041 16661 443 6132 -2023 C
ATOM 2602 CZ3 TRP B 72 52.074 -30.206 190.233 1.00129.55 C
ANISOU 2602 CZ3 TRP B 72 17853 15804 15566 452 5804 -1931 C
ATOM 2603 CH2 TRP B 72 53.459 -30.406 190.303 1.00133.63 C
ANISOU 2603 CH2 TRP B 72 17973 16301 16498 492 6095 -2053 C
ATOM 2604 N ARG B 73 50.165 -25.780 190.294 1.00104.15 N
ANISOU 2604 N ARG B 73 15179 12604 11787 -58 5611 -1207 N
ATOM 2605 CA ARG B 73 50.719 -25.786 188.945 1.00105.46 C
ANISOU 2605 CA ARG B 73 15616 12716 11737 -105 5963 -1222 C
ATOM 2606 C ARG B 73 50.760 -24.388 188.337 1.00110.58 C
ANISOU 2606 C ARG B 73 16484 13297 12232 -272 6158 -1015 C
ATOM 2607 O ARG B 73 51.686 -24.065 187.585 1.00120.08 O
ANISOU 2607 O ARG B 73 17704 14437 13484 -349 6553 -1026 O
ATOM 2608 CB ARG B 73 49.907 -26.725 188.056 1.00100.83 C
ANISOU 2608 CB ARG B 73 15480 12143 10687 -16 5823 -1279 C
ATOM 2609 CG ARG B 73 50.609 -27.141 186.789 1.00104.95 C
ANISOU 2609 CG ARG B 73 16215 12623 11038 -17 6187 -1375 C
ATOM 2610 CD ARG B 73 49.600 -27.527 185.728 1.00103.77 C
ANISOU 2610 CD ARG B 73 16631 12480 10317 8 6026 -1353 C
ATOM 2611 NE ARG B 73 50.237 -28.052 184.528 1.00111.91 N
ANISOU 2611 NE ARG B 73 17884 13476 11160 22 6366 -1474 N
ATOM 2612 CZ ARG B 73 49.618 -28.194 183.362 1.00113.70 C
ANISOU 2612 CZ ARG B 73 18630 13701 10871 16 6331 -1451 C
ATOM 2613 NH1 ARG B 73 48.346 -27.834 183.241 1.00111.01 N
ANISOU 2613 NH1 ARG B 73 18615 13390 10174 -1 5946 -1306 N
ATOM 2614 NH2 ARG B 73 50.269 -28.687 182.316 1.00111.95 N
ANISOU 2614 NH2 ARG B 73 18595 13448 10493 31 6671 -1578 N
ATOM 2615 N ASN B 74 49.773 -23.550 188.649 1.00108.42 N
ANISOU 2615 N ASN B 74 16385 13023 11786 -323 5896 -826 N
ATOM 2616 CA ASN B 74 49.639 -22.223 188.056 1.00108.30 C
ANISOU 2616 CA ASN B 74 16637 12923 11588 -459 6028 -607 C
ATOM 2617 C ASN B 74 50.102 -21.182 189.071 1.00109.69 C
ANISOU 2617 C ASN B 74 16422 13057 12197 -568 6076 -543 C
ATOM 2618 O ASN B 74 49.419 -20.932 190.069 1.00111.37 O
ANISOU 2618 O ASN B 74 16501 13309 12504 -551 5766 -491 O
ATOM 2619 CB ASN B 74 48.195 -21.975 187.625 1.00105.35 C
ANISOU 2619 CB ASN B 74 16745 12562 10722 -428 5683 -434 C
ATOM 2620 CG ASN B 74 48.032 -20.692 186.835 1.00102.53 C
ANISOU 2620 CG ASN B 74 16729 12103 10127 -535 5812 -201 C
ATOM 2621 OD1 ASN B 74 48.754 -19.718 187.049 1.00100.98 O
ANISOU 2621 OD1 ASN B 74 16347 11817 10202 -655 6067 -128 O
ATOM 2622 ND2 ASN B 74 47.077 -20.686 185.912 1.00102.92 N
ANISOU 2622 ND2 ASN B 74 17274 12155 9675 -491 5619 -86 N
ATOM 2623 N HIS B 75 51.268 -20.583 188.817 1.00111.22 N
ANISOU 2623 N HIS B 75 16431 13168 12661 -686 6467 -559 N
ATOM 2624 CA HIS B 75 51.831 -19.629 189.766 1.00105.59 C
ANISOU 2624 CA HIS B 75 15311 12406 12405 -805 6520 -537 C
ATOM 2625 C HIS B 75 51.008 -18.347 189.861 1.00105.32 C
ANISOU 2625 C HIS B 75 15518 12289 12209 -898 6383 -300 C
ATOM 2626 O HIS B 75 50.983 -17.714 190.923 1.00 99.49 O
ANISOU 2626 O HIS B 75 14480 11540 11783 -957 6249 -284 O
ATOM 2627 CB HIS B 75 53.279 -19.318 189.389 1.00113.96 C
ANISOU 2627 CB HIS B 75 16123 13382 13796 -918 6973 -624 C
ATOM 2628 CG HIS B 75 54.232 -20.429 189.700 1.00119.86 C
ANISOU 2628 CG HIS B 75 16456 14204 14881 -827 7067 -871 C
ATOM 2629 ND1 HIS B 75 53.959 -21.747 189.406 1.00121.32 N
ANISOU 2629 ND1 HIS B 75 16756 14475 14863 -659 6966 -990 N
ATOM 2630 CD2 HIS B 75 55.452 -20.420 190.289 1.00123.68 C
ANISOU 2630 CD2 HIS B 75 16406 14682 15907 -871 7230 -1025 C
ATOM 2631 CE1 HIS B 75 54.970 -22.503 189.795 1.00123.42 C
ANISOU 2631 CE1 HIS B 75 16585 14778 15530 -592 7075 -1196 C
ATOM 2632 NE2 HIS B 75 55.890 -21.722 190.334 1.00125.30 N
ANISOU 2632 NE2 HIS B 75 16417 14968 16223 -714 7224 -1219 N
ATOM 2633 N HIS B 76 50.329 -17.948 188.781 1.00109.98 N
ANISOU 2633 N HIS B 76 16644 12819 12323 -903 6397 -119 N
ATOM 2634 CA HIS B 76 49.521 -16.733 188.832 1.00107.52 C
ANISOU 2634 CA HIS B 76 16576 12417 11860 -965 6248 120 C
ATOM 2635 C HIS B 76 48.280 -16.892 189.705 1.00101.00 C
ANISOU 2635 C HIS B 76 15756 11676 10943 -868 5774 171 C
ATOM 2636 O HIS B 76 47.729 -15.887 190.166 1.00100.37 O
ANISOU 2636 O HIS B 76 15712 11524 10900 -917 5630 330 O
ATOM 2637 CB HIS B 76 49.118 -16.297 187.421 1.00114.63 C
ANISOU 2637 CB HIS B 76 18051 13235 12269 -970 6354 305 C
ATOM 2638 CG HIS B 76 50.271 -15.867 186.568 1.00124.09 C
ANISOU 2638 CG HIS B 76 19288 14318 13544 -1090 6853 301 C
ATOM 2639 ND1 HIS B 76 51.121 -16.765 185.957 1.00127.27 N
ANISOU 2639 ND1 HIS B 76 19641 14761 13954 -1070 7143 127 N
ATOM 2640 CD2 HIS B 76 50.717 -14.635 186.225 1.00126.54 C
ANISOU 2640 CD2 HIS B 76 19683 14461 13935 -1231 7128 448 C
ATOM 2641 CE1 HIS B 76 52.038 -16.105 185.273 1.00128.95 C
ANISOU 2641 CE1 HIS B 76 19905 14846 14246 -1197 7583 168 C
ATOM 2642 NE2 HIS B 76 51.815 -14.811 185.419 1.00131.45 N
ANISOU 2642 NE2 HIS B 76 20306 15032 14607 -1300 7584 363 N
ATOM 2643 N MET B 77 47.834 -18.125 189.944 1.00100.85 N
ANISOU 2643 N MET B 77 15705 11795 10818 -731 5540 38 N
ATOM 2644 CA MET B 77 46.680 -18.389 190.796 1.00 93.18 C
ANISOU 2644 CA MET B 77 14725 10908 9773 -638 5107 67 C
ATOM 2645 C MET B 77 47.017 -18.370 192.279 1.00 89.94 C
ANISOU 2645 C MET B 77 13798 10542 9833 -657 5034 -44 C
ATOM 2646 O MET B 77 46.110 -18.525 193.103 1.00 93.61 O
ANISOU 2646 O MET B 77 14226 11071 10270 -589 4707 -21 O
ATOM 2647 CB MET B 77 46.053 -19.741 190.444 1.00 94.88 C
ANISOU 2647 CB MET B 77 15124 11235 9691 -492 4884 -43 C
ATOM 2648 CG MET B 77 45.387 -19.787 189.079 1.00103.76 C
ANISOU 2648 CG MET B 77 16789 12338 10297 -457 4818 67 C
ATOM 2649 SD MET B 77 44.475 -21.323 188.829 1.00 97.44 S
ANISOU 2649 SD MET B 77 16179 11659 9186 -303 4468 -80 S
ATOM 2650 CE MET B 77 43.471 -21.346 190.316 1.00 92.18 C
ANISOU 2650 CE MET B 77 15279 11058 8687 -247 4041 -54 C
ATOM 2651 N ARG B 78 48.289 -18.198 192.640 1.00 87.64 N
ANISOU 2651 N ARG B 78 13102 10222 9974 -744 5315 -171 N
ATOM 2652 CA ARG B 78 48.716 -18.239 194.039 1.00 83.34 C
ANISOU 2652 CA ARG B 78 12032 9734 9900 -755 5221 -307 C
ATOM 2653 C ARG B 78 48.407 -16.899 194.713 1.00 91.88 C
ANISOU 2653 C ARG B 78 13048 10726 11136 -877 5152 -171 C
ATOM 2654 O ARG B 78 49.288 -16.117 195.077 1.00 96.94 O
ANISOU 2654 O ARG B 78 13392 11288 12154 -1013 5333 -213 O
ATOM 2655 CB ARG B 78 50.195 -18.587 194.127 1.00 85.45 C
ANISOU 2655 CB ARG B 78 11877 10006 10584 -791 5495 -505 C
ATOM 2656 CG ARG B 78 50.522 -19.995 193.655 1.00 84.67 C
ANISOU 2656 CG ARG B 78 11780 9989 10400 -649 5542 -663 C
ATOM 2657 CD ARG B 78 52.017 -20.268 193.672 1.00 81.21 C
ANISOU 2657 CD ARG B 78 10928 9541 10387 -678 5823 -843 C
ATOM 2658 NE ARG B 78 52.299 -21.687 193.474 1.00 87.85 N
ANISOU 2658 NE ARG B 78 11703 10458 11216 -513 5817 -1011 N
ATOM 2659 CZ ARG B 78 53.512 -22.197 193.290 1.00 99.35 C
ANISOU 2659 CZ ARG B 78 12866 11911 12973 -491 6056 -1172 C
ATOM 2660 NH1 ARG B 78 54.577 -21.404 193.269 1.00108.97 N
ANISOU 2660 NH1 ARG B 78 13816 13058 14529 -634 6323 -1195 N
ATOM 2661 NH2 ARG B 78 53.660 -23.504 193.120 1.00 99.05 N
ANISOU 2661 NH2 ARG B 78 12801 11926 12906 -324 6027 -1317 N
ATOM 2662 N THR B 79 47.113 -16.645 194.872 1.00 82.31 N
ANISOU 2662 N THR B 79 12122 9518 9634 -824 4870 -13 N
ATOM 2663 CA THR B 79 46.604 -15.465 195.555 1.00 72.57 C
ANISOU 2663 CA THR B 79 10867 8194 8513 -910 4756 125 C
ATOM 2664 C THR B 79 46.229 -15.810 196.992 1.00 75.44 C
ANISOU 2664 C THR B 79 10872 8668 9123 -838 4393 10 C
ATOM 2665 O THR B 79 46.159 -16.978 197.382 1.00 78.05 O
ANISOU 2665 O THR B 79 11047 9142 9468 -702 4182 -134 O
ATOM 2666 CB THR B 79 45.397 -14.889 194.810 1.00 74.85 C
ANISOU 2666 CB THR B 79 11683 8402 8355 -869 4595 385 C
ATOM 2667 OG1 THR B 79 44.306 -15.817 194.871 1.00 74.25 O
ANISOU 2667 OG1 THR B 79 11794 8452 7967 -711 4267 392 O
ATOM 2668 CG2 THR B 79 45.750 -14.637 193.360 1.00 73.55 C
ANISOU 2668 CG2 THR B 79 11867 8147 7930 -900 4837 480 C
ATOM 2669 N VAL B 80 45.988 -14.767 197.790 1.00 72.61 N
ANISOU 2669 N VAL B 80 10380 8230 8978 -912 4240 69 N
ATOM 2670 CA VAL B 80 45.537 -14.979 199.163 1.00 73.02 C
ANISOU 2670 CA VAL B 80 10128 8382 9233 -826 3797 -32 C
ATOM 2671 C VAL B 80 44.241 -15.788 199.175 1.00 69.44 C
ANISOU 2671 C VAL B 80 9900 8034 8452 -644 3403 34 C
ATOM 2672 O VAL B 80 44.101 -16.773 199.917 1.00 68.45 O
ANISOU 2672 O VAL B 80 9564 8045 8398 -528 3141 -96 O
ATOM 2673 CB VAL B 80 45.367 -13.624 199.877 1.00 62.51 C
ANISOU 2673 CB VAL B 80 8708 6922 8123 -937 3722 28 C
ATOM 2674 CG1 VAL B 80 44.652 -13.803 201.205 1.00 59.56 C
ANISOU 2674 CG1 VAL B 80 8132 6649 7850 -829 3259 -47 C
ATOM 2675 CG2 VAL B 80 46.724 -12.952 200.077 1.00 62.20 C
ANISOU 2675 CG2 VAL B 80 8345 6790 8497 -1133 4065 -96 C
ATOM 2676 N THR B 81 43.293 -15.412 198.312 1.00 71.53 N
ANISOU 2676 N THR B 81 10598 8225 8354 -616 3359 239 N
ATOM 2677 CA THR B 81 42.004 -16.096 198.286 1.00 64.99 C
ANISOU 2677 CA THR B 81 9963 7486 7246 -462 2971 298 C
ATOM 2678 C THR B 81 42.170 -17.559 197.907 1.00 62.63 C
ANISOU 2678 C THR B 81 9681 7311 6805 -370 2963 165 C
ATOM 2679 O THR B 81 41.580 -18.446 198.533 1.00 67.39 O
ANISOU 2679 O THR B 81 10169 8020 7418 -260 2645 89 O
ATOM 2680 CB THR B 81 41.056 -15.404 197.303 1.00 65.42 C
ANISOU 2680 CB THR B 81 10478 7435 6942 -445 2927 539 C
ATOM 2681 OG1 THR B 81 40.845 -14.046 197.703 1.00 71.61 O
ANISOU 2681 OG1 THR B 81 11249 8074 7884 -511 2920 665 O
ATOM 2682 CG2 THR B 81 39.720 -16.134 197.248 1.00 64.35 C
ANISOU 2682 CG2 THR B 81 10499 7395 6555 -295 2508 578 C
ATOM 2683 N ASN B 82 42.973 -17.834 196.875 1.00 69.20 N
ANISOU 2683 N ASN B 82 10668 8117 7508 -417 3337 132 N
ATOM 2684 CA ASN B 82 43.154 -19.215 196.440 1.00 74.24 C
ANISOU 2684 CA ASN B 82 11351 8847 8009 -324 3361 -12 C
ATOM 2685 C ASN B 82 43.912 -20.047 197.471 1.00 80.00 C
ANISOU 2685 C ASN B 82 11615 9664 9116 -273 3315 -225 C
ATOM 2686 O ASN B 82 43.650 -21.248 197.608 1.00 77.74 O
ANISOU 2686 O ASN B 82 11307 9454 8777 -155 3135 -330 O
ATOM 2687 CB ASN B 82 43.854 -19.246 195.084 1.00 72.84 C
ANISOU 2687 CB ASN B 82 11471 8613 7594 -384 3815 -5 C
ATOM 2688 CG ASN B 82 42.947 -18.784 193.958 1.00 81.33 C
ANISOU 2688 CG ASN B 82 13096 9627 8178 -383 3774 202 C
ATOM 2689 OD1 ASN B 82 41.721 -18.792 194.095 1.00 79.52 O
ANISOU 2689 OD1 ASN B 82 13015 9424 7774 -303 3358 300 O
ATOM 2690 ND2 ASN B 82 43.542 -18.381 192.839 1.00 89.69 N
ANISOU 2690 ND2 ASN B 82 14365 10605 9110 -450 4059 258 N
ATOM 2691 N TYR B 83 44.831 -19.435 198.223 1.00 71.24 N
ANISOU 2691 N TYR B 83 10136 8537 8397 -357 3451 -292 N
ATOM 2692 CA TYR B 83 45.486 -20.171 199.300 1.00 69.27 C
ANISOU 2692 CA TYR B 83 9443 8376 8500 -287 3329 -480 C
ATOM 2693 C TYR B 83 44.485 -20.549 200.384 1.00 67.89 C
ANISOU 2693 C TYR B 83 9194 8276 8324 -181 2848 -460 C
ATOM 2694 O TYR B 83 44.476 -21.691 200.875 1.00 62.31 O
ANISOU 2694 O TYR B 83 8356 7645 7675 -57 2669 -564 O
ATOM 2695 CB TYR B 83 46.630 -19.338 199.882 1.00 74.98 C
ANISOU 2695 CB TYR B 83 9784 9065 9640 -411 3528 -562 C
ATOM 2696 CG TYR B 83 47.914 -19.416 199.078 1.00 76.62 C
ANISOU 2696 CG TYR B 83 9889 9230 9991 -486 4020 -664 C
ATOM 2697 CD1 TYR B 83 48.157 -20.486 198.229 1.00 82.53 C
ANISOU 2697 CD1 TYR B 83 10781 10004 10572 -393 4210 -740 C
ATOM 2698 CD2 TYR B 83 48.884 -18.430 199.179 1.00 82.26 C
ANISOU 2698 CD2 TYR B 83 10356 9869 11031 -657 4311 -701 C
ATOM 2699 CE1 TYR B 83 49.325 -20.567 197.503 1.00 88.11 C
ANISOU 2699 CE1 TYR B 83 11386 10670 11423 -452 4646 -838 C
ATOM 2700 CE2 TYR B 83 50.055 -18.503 198.453 1.00 88.77 C
ANISOU 2700 CE2 TYR B 83 11062 10649 12017 -728 4735 -791 C
ATOM 2701 CZ TYR B 83 50.271 -19.573 197.617 1.00 94.63 C
ANISOU 2701 CZ TYR B 83 11954 11424 12577 -613 4843 -847 C
ATOM 2702 OH TYR B 83 51.436 -19.652 196.889 1.00101.60 O
ANISOU 2702 OH TYR B 83 12732 12256 13615 -665 5154 -923 O
ATOM 2703 N PHE B 84 43.605 -19.616 200.749 1.00 68.82 N
ANISOU 2703 N PHE B 84 9413 8360 8376 -223 2653 -322 N
ATOM 2704 CA PHE B 84 42.574 -19.961 201.720 1.00 64.13 C
ANISOU 2704 CA PHE B 84 8771 7834 7762 -128 2242 -299 C
ATOM 2705 C PHE B 84 41.653 -21.050 201.176 1.00 61.70 C
ANISOU 2705 C PHE B 84 8714 7563 7166 -23 2072 -270 C
ATOM 2706 O PHE B 84 41.227 -21.943 201.918 1.00 64.97 O
ANISOU 2706 O PHE B 84 9019 8043 7623 72 1820 -322 O
ATOM 2707 CB PHE B 84 41.781 -18.712 202.103 1.00 64.29 C
ANISOU 2707 CB PHE B 84 8863 7792 7770 -186 2108 -164 C
ATOM 2708 CG PHE B 84 42.473 -17.834 203.114 1.00 60.13 C
ANISOU 2708 CG PHE B 84 8031 7244 7571 -269 2134 -239 C
ATOM 2709 CD1 PHE B 84 42.962 -18.366 204.298 1.00 56.29 C
ANISOU 2709 CD1 PHE B 84 7215 6856 7317 -218 1974 -389 C
ATOM 2710 CD2 PHE B 84 42.626 -16.474 202.884 1.00 61.49 C
ANISOU 2710 CD2 PHE B 84 8264 7286 7812 -398 2304 -160 C
ATOM 2711 CE1 PHE B 84 43.588 -17.562 205.235 1.00 55.94 C
ANISOU 2711 CE1 PHE B 84 6901 6799 7554 -298 1960 -481 C
ATOM 2712 CE2 PHE B 84 43.254 -15.658 203.815 1.00 56.56 C
ANISOU 2712 CE2 PHE B 84 7361 6627 7500 -491 2316 -257 C
ATOM 2713 CZ PHE B 84 43.738 -16.205 204.992 1.00 63.31 C
ANISOU 2713 CZ PHE B 84 7882 7600 8572 -443 2132 -429 C
ATOM 2714 N LEU B 85 41.341 -21.003 199.877 1.00 59.36 N
ANISOU 2714 N LEU B 85 8770 7216 6566 -44 2207 -190 N
ATOM 2715 CA LEU B 85 40.482 -22.036 199.306 1.00 64.04 C
ANISOU 2715 CA LEU B 85 9607 7840 6887 40 2029 -192 C
ATOM 2716 C LEU B 85 41.167 -23.397 199.304 1.00 77.12 C
ANISOU 2716 C LEU B 85 11149 9531 8620 115 2108 -371 C
ATOM 2717 O LEU B 85 40.502 -24.428 199.473 1.00 85.62 O
ANISOU 2717 O LEU B 85 12269 10634 9629 195 1876 -414 O
ATOM 2718 CB LEU B 85 40.050 -21.651 197.890 1.00 66.79 C
ANISOU 2718 CB LEU B 85 10385 8131 6860 4 2136 -78 C
ATOM 2719 CG LEU B 85 39.156 -20.410 197.768 1.00 68.92 C
ANISOU 2719 CG LEU B 85 10828 8345 7015 -31 1998 125 C
ATOM 2720 CD1 LEU B 85 38.842 -20.108 196.309 1.00 73.39 C
ANISOU 2720 CD1 LEU B 85 11855 8854 7178 -47 2100 246 C
ATOM 2721 CD2 LEU B 85 37.875 -20.574 198.571 1.00 71.38 C
ANISOU 2721 CD2 LEU B 85 11050 8702 7369 39 1577 168 C
ATOM 2722 N VAL B 86 42.490 -23.424 199.135 1.00 74.48 N
ANISOU 2722 N VAL B 86 10654 9184 8462 91 2439 -479 N
ATOM 2723 CA VAL B 86 43.218 -24.682 199.269 1.00 70.92 C
ANISOU 2723 CA VAL B 86 10038 8754 8156 189 2509 -655 C
ATOM 2724 C VAL B 86 43.131 -25.196 200.701 1.00 68.75 C
ANISOU 2724 C VAL B 86 9443 8531 8148 276 2208 -697 C
ATOM 2725 O VAL B 86 43.031 -26.407 200.939 1.00 65.00 O
ANISOU 2725 O VAL B 86 8940 8058 7699 386 2081 -778 O
ATOM 2726 CB VAL B 86 44.679 -24.507 198.819 1.00 69.47 C
ANISOU 2726 CB VAL B 86 9695 8543 8157 149 2943 -767 C
ATOM 2727 CG1 VAL B 86 45.493 -25.756 199.147 1.00 61.18 C
ANISOU 2727 CG1 VAL B 86 8396 7507 7342 281 2987 -954 C
ATOM 2728 CG2 VAL B 86 44.747 -24.199 197.326 1.00 66.62 C
ANISOU 2728 CG2 VAL B 86 9718 8124 7470 76 3278 -727 C
ATOM 2729 N ASN B 87 43.154 -24.289 201.680 1.00 63.59 N
ANISOU 2729 N ASN B 87 8572 7908 7680 227 2091 -641 N
ATOM 2730 CA ASN B 87 42.968 -24.736 203.059 1.00 55.45 C
ANISOU 2730 CA ASN B 87 7301 6934 6834 310 1791 -663 C
ATOM 2731 C ASN B 87 41.568 -25.313 203.262 1.00 57.10 C
ANISOU 2731 C ASN B 87 7705 7148 6843 358 1493 -577 C
ATOM 2732 O ASN B 87 41.385 -26.312 203.976 1.00 58.78 O
ANISOU 2732 O ASN B 87 7832 7376 7126 456 1309 -612 O
ATOM 2733 CB ASN B 87 43.222 -23.577 204.021 1.00 63.18 C
ANISOU 2733 CB ASN B 87 8052 7943 8011 238 1728 -638 C
ATOM 2734 CG ASN B 87 43.466 -24.041 205.445 1.00 63.61 C
ANISOU 2734 CG ASN B 87 7828 8066 8277 330 1481 -700 C
ATOM 2735 OD1 ASN B 87 44.236 -24.973 205.684 1.00 68.14 O
ANISOU 2735 OD1 ASN B 87 8229 8656 9003 434 1485 -804 O
ATOM 2736 ND2 ASN B 87 42.805 -23.395 206.398 1.00 52.54 N
ANISOU 2736 ND2 ASN B 87 6396 6695 6872 304 1264 -635 N
ATOM 2737 N LEU B 88 40.566 -24.707 202.622 1.00 57.08 N
ANISOU 2737 N LEU B 88 7963 7122 6601 292 1446 -460 N
ATOM 2738 CA LEU B 88 39.211 -25.246 202.713 1.00 53.02 C
ANISOU 2738 CA LEU B 88 7605 6610 5929 324 1172 -393 C
ATOM 2739 C LEU B 88 39.140 -26.628 202.077 1.00 57.86 C
ANISOU 2739 C LEU B 88 8360 7189 6434 386 1170 -484 C
ATOM 2740 O LEU B 88 38.437 -27.517 202.572 1.00 62.78 O
ANISOU 2740 O LEU B 88 8979 7805 7071 434 957 -488 O
ATOM 2741 CB LEU B 88 38.219 -24.285 202.049 1.00 54.31 C
ANISOU 2741 CB LEU B 88 8002 6753 5881 257 1110 -257 C
ATOM 2742 CG LEU B 88 36.745 -24.704 201.943 1.00 56.10 C
ANISOU 2742 CG LEU B 88 8380 6981 5955 276 826 -190 C
ATOM 2743 CD1 LEU B 88 36.092 -24.826 203.320 1.00 50.24 C
ANISOU 2743 CD1 LEU B 88 7425 6275 5388 306 607 -161 C
ATOM 2744 CD2 LEU B 88 35.963 -23.725 201.073 1.00 55.83 C
ANISOU 2744 CD2 LEU B 88 8583 6918 5710 233 780 -61 C
ATOM 2745 N SER B 89 39.891 -26.833 200.992 1.00 55.42 N
ANISOU 2745 N SER B 89 8185 6845 6027 380 1432 -566 N
ATOM 2746 CA SER B 89 39.959 -28.155 200.379 1.00 62.58 C
ANISOU 2746 CA SER B 89 9230 7702 6846 445 1466 -689 C
ATOM 2747 C SER B 89 40.652 -29.169 201.282 1.00 70.21 C
ANISOU 2747 C SER B 89 9936 8651 8089 556 1443 -790 C
ATOM 2748 O SER B 89 40.280 -30.348 201.287 1.00 67.36 O
ANISOU 2748 O SER B 89 9651 8229 7712 620 1329 -851 O
ATOM 2749 CB SER B 89 40.678 -28.076 199.032 1.00 60.43 C
ANISOU 2749 CB SER B 89 9169 7396 6396 418 1799 -766 C
ATOM 2750 OG SER B 89 39.822 -27.552 198.032 1.00 61.70 O
ANISOU 2750 OG SER B 89 9679 7552 6213 346 1752 -677 O
ATOM 2751 N LEU B 90 41.663 -28.741 202.042 1.00 68.06 N
ANISOU 2751 N LEU B 90 9361 8419 8081 583 1536 -810 N
ATOM 2752 CA LEU B 90 42.298 -29.668 202.976 1.00 62.71 C
ANISOU 2752 CA LEU B 90 8435 7728 7663 713 1460 -885 C
ATOM 2753 C LEU B 90 41.330 -30.079 204.078 1.00 61.88 C
ANISOU 2753 C LEU B 90 8309 7631 7573 746 1129 -789 C
ATOM 2754 O LEU B 90 41.255 -31.258 204.444 1.00 61.55 O
ANISOU 2754 O LEU B 90 8265 7522 7599 847 1026 -822 O
ATOM 2755 CB LEU B 90 43.555 -29.045 203.581 1.00 55.27 C
ANISOU 2755 CB LEU B 90 7155 6842 7005 731 1580 -933 C
ATOM 2756 CG LEU B 90 44.726 -28.772 202.641 1.00 67.48 C
ANISOU 2756 CG LEU B 90 8638 8370 8633 707 1957 -1048 C
ATOM 2757 CD1 LEU B 90 45.882 -28.163 203.417 1.00 67.82 C
ANISOU 2757 CD1 LEU B 90 8283 8469 9016 711 2014 -1103 C
ATOM 2758 CD2 LEU B 90 45.149 -30.051 201.948 1.00 71.26 C
ANISOU 2758 CD2 LEU B 90 9196 8764 9114 824 2109 -1185 C
ATOM 2759 N ALA B 91 40.567 -29.121 204.607 1.00 58.79 N
ANISOU 2759 N ALA B 91 7913 7303 7121 663 984 -668 N
ATOM 2760 CA ALA B 91 39.569 -29.468 205.615 1.00 56.99 C
ANISOU 2760 CA ALA B 91 7681 7081 6891 681 717 -575 C
ATOM 2761 C ALA B 91 38.498 -30.390 205.036 1.00 67.40 C
ANISOU 2761 C ALA B 91 9233 8321 8056 665 619 -566 C
ATOM 2762 O ALA B 91 38.057 -31.347 205.694 1.00 67.45 O
ANISOU 2762 O ALA B 91 9233 8274 8122 716 476 -545 O
ATOM 2763 CB ALA B 91 38.939 -28.195 206.178 1.00 49.80 C
ANISOU 2763 CB ALA B 91 6729 6244 5949 596 623 -469 C
ATOM 2764 N ASP B 92 38.081 -30.131 203.793 1.00 65.81 N
ANISOU 2764 N ASP B 92 9250 8102 7653 591 692 -584 N
ATOM 2765 CA ASP B 92 37.081 -30.983 203.164 1.00 63.88 C
ANISOU 2765 CA ASP B 92 9224 7785 7263 563 571 -606 C
ATOM 2766 C ASP B 92 37.616 -32.390 202.935 1.00 64.94 C
ANISOU 2766 C ASP B 92 9401 7808 7463 647 639 -737 C
ATOM 2767 O ASP B 92 36.881 -33.367 203.095 1.00 67.43 O
ANISOU 2767 O ASP B 92 9793 8037 7792 646 493 -749 O
ATOM 2768 CB ASP B 92 36.618 -30.360 201.847 1.00 71.00 C
ANISOU 2768 CB ASP B 92 10373 8701 7903 480 610 -604 C
ATOM 2769 CG ASP B 92 35.748 -29.138 202.055 1.00 71.09 C
ANISOU 2769 CG ASP B 92 10373 8782 7855 411 478 -458 C
ATOM 2770 OD1 ASP B 92 35.395 -28.862 203.222 1.00 60.44 O
ANISOU 2770 OD1 ASP B 92 8832 7468 6663 417 361 -379 O
ATOM 2771 OD2 ASP B 92 35.423 -28.455 201.059 1.00 80.99 O
ANISOU 2771 OD2 ASP B 92 11827 10048 8899 360 495 -422 O
ATOM 2772 N VAL B 93 38.895 -32.520 202.576 1.00 65.86 N
ANISOU 2772 N VAL B 93 9459 7911 7653 721 872 -843 N
ATOM 2773 CA VAL B 93 39.465 -33.851 202.382 1.00 66.34 C
ANISOU 2773 CA VAL B 93 9546 7848 7812 829 953 -978 C
ATOM 2774 C VAL B 93 39.609 -34.574 203.716 1.00 66.64 C
ANISOU 2774 C VAL B 93 9389 7839 8092 935 806 -925 C
ATOM 2775 O VAL B 93 39.424 -35.795 203.800 1.00 66.17 O
ANISOU 2775 O VAL B 93 9406 7639 8096 998 747 -972 O
ATOM 2776 CB VAL B 93 40.808 -33.763 201.638 1.00 66.77 C
ANISOU 2776 CB VAL B 93 9560 7900 7909 890 1272 -1113 C
ATOM 2777 CG1 VAL B 93 41.579 -35.069 201.786 1.00 64.57 C
ANISOU 2777 CG1 VAL B 93 9208 7492 7835 1048 1348 -1243 C
ATOM 2778 CG2 VAL B 93 40.571 -33.459 200.171 1.00 69.59 C
ANISOU 2778 CG2 VAL B 93 10222 8256 7963 798 1431 -1182 C
ATOM 2779 N LEU B 94 39.925 -33.837 204.781 1.00 64.64 N
ANISOU 2779 N LEU B 94 8906 7689 7964 956 737 -824 N
ATOM 2780 CA LEU B 94 39.980 -34.461 206.096 1.00 65.64 C
ANISOU 2780 CA LEU B 94 8896 7783 8262 1059 571 -749 C
ATOM 2781 C LEU B 94 38.622 -35.037 206.466 1.00 67.56 C
ANISOU 2781 C LEU B 94 9290 7954 8426 993 385 -652 C
ATOM 2782 O LEU B 94 38.517 -36.197 206.879 1.00 72.89 O
ANISOU 2782 O LEU B 94 10009 8492 9194 1069 319 -642 O
ATOM 2783 CB LEU B 94 40.438 -33.451 207.147 1.00 64.28 C
ANISOU 2783 CB LEU B 94 8491 7751 8183 1071 506 -671 C
ATOM 2784 CG LEU B 94 40.412 -33.960 208.593 1.00 68.82 C
ANISOU 2784 CG LEU B 94 8967 8314 8866 1174 306 -570 C
ATOM 2785 CD1 LEU B 94 41.390 -35.115 208.791 1.00 65.67 C
ANISOU 2785 CD1 LEU B 94 8489 7804 8657 1363 317 -632 C
ATOM 2786 CD2 LEU B 94 40.698 -32.833 209.587 1.00 71.56 C
ANISOU 2786 CD2 LEU B 94 9131 8813 9245 1158 218 -513 C
ATOM 2787 N ALA B 95 37.562 -34.242 206.301 1.00 63.30 N
ANISOU 2787 N ALA B 95 8824 7489 7737 852 309 -580 N
ATOM 2788 CA ALA B 95 36.230 -34.751 206.620 1.00 58.57 C
ANISOU 2788 CA ALA B 95 8326 6826 7103 773 150 -501 C
ATOM 2789 C ALA B 95 35.793 -35.865 205.667 1.00 65.29 C
ANISOU 2789 C ALA B 95 9376 7520 7910 740 152 -609 C
ATOM 2790 O ALA B 95 35.094 -36.795 206.085 1.00 69.92 O
ANISOU 2790 O ALA B 95 10016 7982 8569 716 53 -575 O
ATOM 2791 CB ALA B 95 35.214 -33.607 206.608 1.00 50.67 C
ANISOU 2791 CB ALA B 95 7323 5939 5989 647 68 -415 C
ATOM 2792 N THR B 96 36.207 -35.808 204.398 1.00 64.25 N
ANISOU 2792 N THR B 96 9372 7382 7660 730 275 -747 N
ATOM 2793 CA THR B 96 35.717 -36.764 203.408 1.00 67.93 C
ANISOU 2793 CA THR B 96 10062 7708 8041 681 259 -879 C
ATOM 2794 C THR B 96 36.388 -38.125 203.545 1.00 72.34 C
ANISOU 2794 C THR B 96 10646 8080 8760 801 335 -975 C
ATOM 2795 O THR B 96 35.727 -39.162 203.410 1.00 64.75 O
ANISOU 2795 O THR B 96 9816 6952 7835 757 251 -1028 O
ATOM 2796 CB THR B 96 35.938 -36.223 201.994 1.00 64.56 C
ANISOU 2796 CB THR B 96 9812 7339 7379 636 376 -995 C
ATOM 2797 OG1 THR B 96 35.152 -35.041 201.796 1.00 64.55 O
ANISOU 2797 OG1 THR B 96 9826 7475 7225 530 269 -892 O
ATOM 2798 CG2 THR B 96 35.546 -37.268 200.955 1.00 72.13 C
ANISOU 2798 CG2 THR B 96 11030 8152 8226 596 357 -1170 C
ATOM 2799 N ALA B 97 37.699 -38.142 203.798 1.00 67.71 N
ANISOU 2799 N ALA B 97 9925 7504 8300 954 490 -1008 N
ATOM 2800 CA ALA B 97 38.430 -39.403 203.819 1.00 70.45 C
ANISOU 2800 CA ALA B 97 10290 7659 8817 1101 575 -1111 C
ATOM 2801 C ALA B 97 38.195 -40.174 205.112 1.00 70.66 C
ANISOU 2801 C ALA B 97 10240 7570 9036 1173 425 -970 C
ATOM 2802 O ALA B 97 38.014 -41.397 205.083 1.00 66.83 O
ANISOU 2802 O ALA B 97 9879 6863 8651 1212 409 -1019 O
ATOM 2803 CB ALA B 97 39.924 -39.142 203.619 1.00 69.92 C
ANISOU 2803 CB ALA B 97 10068 7644 8855 1252 791 -1200 C
ATOM 2804 N ILE B 98 38.181 -39.481 206.246 1.00 62.87 N
ANISOU 2804 N ILE B 98 9080 6718 8091 1187 324 -796 N
ATOM 2805 CA ILE B 98 38.117 -40.119 207.556 1.00 65.57 C
ANISOU 2805 CA ILE B 98 9368 6970 8576 1278 200 -641 C
ATOM 2806 C ILE B 98 36.693 -40.164 208.091 1.00 68.73 C
ANISOU 2806 C ILE B 98 9855 7347 8911 1118 67 -503 C
ATOM 2807 O ILE B 98 36.210 -41.215 208.512 1.00 72.98 O
ANISOU 2807 O ILE B 98 10498 7690 9541 1117 19 -443 O
ATOM 2808 CB ILE B 98 39.059 -39.397 208.545 1.00 70.12 C
ANISOU 2808 CB ILE B 98 9712 7704 9226 1407 165 -551 C
ATOM 2809 CG1 ILE B 98 40.489 -39.375 208.003 1.00 72.21 C
ANISOU 2809 CG1 ILE B 98 9837 7985 9615 1559 311 -701 C
ATOM 2810 CG2 ILE B 98 39.003 -40.066 209.909 1.00 75.98 C
ANISOU 2810 CG2 ILE B 98 10448 8357 10064 1516 20 -377 C
ATOM 2811 CD1 ILE B 98 41.061 -40.739 207.737 1.00 76.38 C
ANISOU 2811 CD1 ILE B 98 10428 8279 10316 1725 375 -792 C
ATOM 2812 N CYS B 99 36.008 -39.023 208.093 1.00 61.35 N
ANISOU 2812 N CYS B 99 8870 6598 7842 981 22 -450 N
ATOM 2813 CA CYS B 99 34.716 -38.943 208.761 1.00 57.43 C
ANISOU 2813 CA CYS B 99 8395 6104 7323 846 -83 -313 C
ATOM 2814 C CYS B 99 33.589 -39.510 207.907 1.00 60.96 C
ANISOU 2814 C CYS B 99 8984 6427 7749 683 -122 -393 C
ATOM 2815 O CYS B 99 32.682 -40.162 208.434 1.00 70.91 O
ANISOU 2815 O CYS B 99 10284 7563 9093 597 -176 -310 O
ATOM 2816 CB CYS B 99 34.430 -37.491 209.137 1.00 56.83 C
ANISOU 2816 CB CYS B 99 8191 6257 7143 784 -115 -236 C
ATOM 2817 SG CYS B 99 35.727 -36.793 210.180 1.00 64.76 S
ANISOU 2817 SG CYS B 99 9020 7406 8180 950 -105 -174 S
ATOM 2818 N LEU B 100 33.623 -39.272 206.598 1.00 64.94 N
ANISOU 2818 N LEU B 100 9572 6962 8142 631 -95 -555 N
ATOM 2819 CA LEU B 100 32.495 -39.660 205.754 1.00 65.13 C
ANISOU 2819 CA LEU B 100 9725 6902 8120 465 -186 -647 C
ATOM 2820 C LEU B 100 32.197 -41.150 205.811 1.00 68.25 C
ANISOU 2820 C LEU B 100 10238 7027 8668 441 -198 -699 C
ATOM 2821 O LEU B 100 31.019 -41.514 205.982 1.00 65.32 O
ANISOU 2821 O LEU B 100 9874 6573 8372 285 -299 -666 O
ATOM 2822 CB LEU B 100 32.751 -39.201 204.316 1.00 56.42 C
ANISOU 2822 CB LEU B 100 8744 5873 6820 442 -156 -816 C
ATOM 2823 CG LEU B 100 31.654 -39.511 203.294 1.00 59.64 C
ANISOU 2823 CG LEU B 100 9308 6221 7133 281 -296 -941 C
ATOM 2824 CD1 LEU B 100 31.723 -38.547 202.124 1.00 59.64 C
ANISOU 2824 CD1 LEU B 100 9412 6376 6871 256 -304 -1019 C
ATOM 2825 CD2 LEU B 100 31.758 -40.954 202.800 1.00 55.63 C
ANISOU 2825 CD2 LEU B 100 8974 5464 6701 278 -272 -1113 C
ATOM 2826 N PRO B 101 33.171 -42.052 205.644 1.00 68.64 N
ANISOU 2826 N PRO B 101 10372 6913 8794 580 -94 -790 N
ATOM 2827 CA PRO B 101 32.847 -43.485 205.753 1.00 63.76 C
ANISOU 2827 CA PRO B 101 9881 5997 8346 555 -102 -829 C
ATOM 2828 C PRO B 101 32.263 -43.863 207.102 1.00 71.66 C
ANISOU 2828 C PRO B 101 10817 6908 9502 524 -141 -606 C
ATOM 2829 O PRO B 101 31.349 -44.698 207.178 1.00 74.40 O
ANISOU 2829 O PRO B 101 11243 7054 9974 382 -181 -605 O
ATOM 2830 CB PRO B 101 34.198 -44.169 205.500 1.00 51.74 C
ANISOU 2830 CB PRO B 101 8419 4344 6894 768 38 -937 C
ATOM 2831 CG PRO B 101 35.053 -43.130 204.825 1.00 63.82 C
ANISOU 2831 CG PRO B 101 9884 6105 8260 844 128 -1024 C
ATOM 2832 CD PRO B 101 34.601 -41.819 205.374 1.00 62.98 C
ANISOU 2832 CD PRO B 101 9621 6258 8051 767 47 -861 C
ATOM 2833 N ALA B 102 32.746 -43.236 208.177 1.00 69.25 N
ANISOU 2833 N ALA B 102 10380 6748 9185 640 -124 -421 N
ATOM 2834 CA ALA B 102 32.224 -43.547 209.503 1.00 65.80 C
ANISOU 2834 CA ALA B 102 9920 6238 8841 620 -139 -196 C
ATOM 2835 C ALA B 102 30.775 -43.102 209.624 1.00 69.62 C
ANISOU 2835 C ALA B 102 10346 6792 9316 388 -193 -140 C
ATOM 2836 O ALA B 102 29.920 -43.842 210.130 1.00 79.98 O
ANISOU 2836 O ALA B 102 11703 7925 10762 269 -179 -52 O
ATOM 2837 CB ALA B 102 33.085 -42.876 210.579 1.00 56.14 C
ANISOU 2837 CB ALA B 102 8586 5183 7560 797 -135 -37 C
ATOM 2838 N SER B 103 30.481 -41.895 209.140 1.00 61.90 N
ANISOU 2838 N SER B 103 9259 6059 8202 324 -244 -192 N
ATOM 2839 CA SER B 103 29.115 -41.393 209.178 1.00 66.74 C
ANISOU 2839 CA SER B 103 9778 6748 8832 128 -309 -155 C
ATOM 2840 C SER B 103 28.188 -42.255 208.335 1.00 71.23 C
ANISOU 2840 C SER B 103 10421 7130 9514 -52 -381 -296 C
ATOM 2841 O SER B 103 27.037 -42.489 208.720 1.00 74.77 O
ANISOU 2841 O SER B 103 10797 7509 10104 -220 -402 -235 O
ATOM 2842 CB SER B 103 29.093 -39.939 208.706 1.00 68.47 C
ANISOU 2842 CB SER B 103 9888 7239 8889 128 -364 -190 C
ATOM 2843 OG SER B 103 27.780 -39.408 208.708 1.00 79.75 O
ANISOU 2843 OG SER B 103 11202 8741 10359 -33 -442 -160 O
ATOM 2844 N LEU B 104 28.685 -42.783 207.216 1.00 70.26 N
ANISOU 2844 N LEU B 104 10440 6909 9345 -26 -407 -496 N
ATOM 2845 CA LEU B 104 27.863 -43.671 206.400 1.00 68.13 C
ANISOU 2845 CA LEU B 104 10264 6444 9176 -200 -497 -664 C
ATOM 2846 C LEU B 104 27.537 -44.952 207.154 1.00 69.56 C
ANISOU 2846 C LEU B 104 10502 6325 9604 -263 -423 -586 C
ATOM 2847 O LEU B 104 26.370 -45.370 207.233 1.00 67.48 O
ANISOU 2847 O LEU B 104 10185 5944 9511 -473 -476 -591 O
ATOM 2848 CB LEU B 104 28.580 -43.993 205.086 1.00 73.35 C
ANISOU 2848 CB LEU B 104 11111 7055 9702 -138 -511 -909 C
ATOM 2849 CG LEU B 104 28.021 -45.204 204.331 1.00 76.59 C
ANISOU 2849 CG LEU B 104 11678 7196 10227 -283 -582 -1115 C
ATOM 2850 CD1 LEU B 104 26.624 -44.911 203.805 1.00 77.03 C
ANISOU 2850 CD1 LEU B 104 11654 7314 10300 -518 -792 -1195 C
ATOM 2851 CD2 LEU B 104 28.945 -45.637 203.206 1.00 70.83 C
ANISOU 2851 CD2 LEU B 104 11169 6388 9355 -178 -533 -1354 C
ATOM 2852 N LEU B 105 28.563 -45.592 207.719 1.00 70.03 N
ANISOU 2852 N LEU B 105 10662 6242 9703 -80 -300 -508 N
ATOM 2853 CA LEU B 105 28.318 -46.852 208.410 1.00 72.92 C
ANISOU 2853 CA LEU B 105 11126 6285 10294 -122 -221 -414 C
ATOM 2854 C LEU B 105 27.408 -46.654 209.615 1.00 68.35 C
ANISOU 2854 C LEU B 105 10432 5729 9810 -239 -170 -171 C
ATOM 2855 O LEU B 105 26.581 -47.523 209.915 1.00 69.48 O
ANISOU 2855 O LEU B 105 10611 5624 10163 -410 -123 -129 O
ATOM 2856 CB LEU B 105 29.641 -47.490 208.830 1.00 64.49 C
ANISOU 2856 CB LEU B 105 10183 5072 9247 137 -123 -352 C
ATOM 2857 CG LEU B 105 29.584 -48.965 209.227 1.00 73.27 C
ANISOU 2857 CG LEU B 105 11468 5780 10591 131 -46 -299 C
ATOM 2858 CD1 LEU B 105 29.272 -49.825 208.015 1.00 80.87 C
ANISOU 2858 CD1 LEU B 105 12563 6504 11658 0 -82 -585 C
ATOM 2859 CD2 LEU B 105 30.898 -49.381 209.865 1.00 86.28 C
ANISOU 2859 CD2 LEU B 105 13197 7333 12251 433 21 -177 C
ATOM 2860 N VAL B 106 27.516 -45.509 210.293 1.00 65.05 N
ANISOU 2860 N VAL B 106 9876 5593 9245 -164 -158 -23 N
ATOM 2861 CA VAL B 106 26.661 -45.259 211.450 1.00 67.53 C
ANISOU 2861 CA VAL B 106 10094 5943 9621 -266 -75 194 C
ATOM 2862 C VAL B 106 25.224 -45.016 211.008 1.00 75.63 C
ANISOU 2862 C VAL B 106 10959 6999 10777 -531 -133 109 C
ATOM 2863 O VAL B 106 24.279 -45.573 211.579 1.00 76.45 O
ANISOU 2863 O VAL B 106 11027 6941 11081 -706 -40 203 O
ATOM 2864 CB VAL B 106 27.198 -44.082 212.281 1.00 68.03 C
ANISOU 2864 CB VAL B 106 10070 6295 9484 -108 -51 342 C
ATOM 2865 CG1 VAL B 106 26.163 -43.652 213.309 1.00 62.82 C
ANISOU 2865 CG1 VAL B 106 9302 5706 8862 -235 47 518 C
ATOM 2866 CG2 VAL B 106 28.501 -44.465 212.961 1.00 72.21 C
ANISOU 2866 CG2 VAL B 106 10735 6766 9936 141 -12 456 C
ATOM 2867 N ASP B 107 25.033 -44.188 209.976 1.00 79.41 N
ANISOU 2867 N ASP B 107 11336 7679 11157 -564 -287 -66 N
ATOM 2868 CA ASP B 107 23.678 -43.902 209.520 1.00 78.26 C
ANISOU 2868 CA ASP B 107 11011 7578 11145 -790 -393 -153 C
ATOM 2869 C ASP B 107 22.987 -45.153 209.002 1.00 82.06 C
ANISOU 2869 C ASP B 107 11547 7762 11870 -995 -436 -291 C
ATOM 2870 O ASP B 107 21.756 -45.253 209.070 1.00 87.31 O
ANISOU 2870 O ASP B 107 12037 8380 12756 -1215 -465 -305 O
ATOM 2871 CB ASP B 107 23.696 -42.816 208.444 1.00 75.96 C
ANISOU 2871 CB ASP B 107 10651 7540 10672 -756 -581 -304 C
ATOM 2872 CG ASP B 107 23.871 -41.419 209.024 1.00 89.54 C
ANISOU 2872 CG ASP B 107 12237 9544 12240 -638 -544 -166 C
ATOM 2873 OD1 ASP B 107 23.639 -41.235 210.240 1.00 87.44 O
ANISOU 2873 OD1 ASP B 107 11889 9300 12035 -631 -395 21 O
ATOM 2874 OD2 ASP B 107 24.228 -40.498 208.257 1.00 91.18 O
ANISOU 2874 OD2 ASP B 107 12442 9941 12261 -557 -654 -248 O
ATOM 2875 N ILE B 108 23.748 -46.116 208.479 1.00 79.15 N
ANISOU 2875 N ILE B 108 11402 7179 11491 -931 -437 -408 N
ATOM 2876 CA ILE B 108 23.115 -47.338 207.987 1.00 90.99 C
ANISOU 2876 CA ILE B 108 12973 8364 13235 -1135 -477 -562 C
ATOM 2877 C ILE B 108 22.857 -48.322 209.122 1.00 93.20 C
ANISOU 2877 C ILE B 108 13304 8351 13758 -1210 -266 -363 C
ATOM 2878 O ILE B 108 21.739 -48.825 209.282 1.00 90.18 O
ANISOU 2878 O ILE B 108 12811 7803 13649 -1464 -241 -370 O
ATOM 2879 CB ILE B 108 23.955 -47.978 206.869 1.00 93.49 C
ANISOU 2879 CB ILE B 108 13526 8546 13448 -1046 -557 -806 C
ATOM 2880 CG1 ILE B 108 23.833 -47.151 205.589 1.00 98.52 C
ANISOU 2880 CG1 ILE B 108 14136 9426 13869 -1059 -780 -1029 C
ATOM 2881 CG2 ILE B 108 23.511 -49.418 206.630 1.00 93.95 C
ANISOU 2881 CG2 ILE B 108 13710 8205 13780 -1226 -544 -938 C
ATOM 2882 CD1 ILE B 108 24.640 -47.693 204.437 1.00106.75 C
ANISOU 2882 CD1 ILE B 108 15433 10364 14764 -975 -830 -1286 C
ATOM 2883 N THR B 109 23.882 -48.634 209.913 1.00 88.73 N
ANISOU 2883 N THR B 109 12905 7703 13106 -995 -113 -180 N
ATOM 2884 CA THR B 109 23.750 -49.640 210.960 1.00 81.77 C
ANISOU 2884 CA THR B 109 12141 6513 12416 -1036 87 32 C
ATOM 2885 C THR B 109 23.193 -49.090 212.267 1.00 86.64 C
ANISOU 2885 C THR B 109 12638 7252 13027 -1075 250 316 C
ATOM 2886 O THR B 109 22.797 -49.879 213.132 1.00 90.44 O
ANISOU 2886 O THR B 109 13207 7478 13678 -1171 439 504 O
ATOM 2887 CB THR B 109 25.108 -50.299 211.228 1.00 72.95 C
ANISOU 2887 CB THR B 109 11278 5228 11213 -763 150 108 C
ATOM 2888 OG1 THR B 109 26.007 -49.327 211.771 1.00 72.01 O
ANISOU 2888 OG1 THR B 109 11125 5409 10828 -509 148 246 O
ATOM 2889 CG2 THR B 109 25.692 -50.843 209.938 1.00 66.40 C
ANISOU 2889 CG2 THR B 109 10573 4269 10387 -711 34 -190 C
ATOM 2890 N GLU B 110 23.141 -47.768 212.429 1.00 90.16 N
ANISOU 2890 N GLU B 110 12906 8066 13283 -1007 201 351 N
ATOM 2891 CA GLU B 110 22.683 -47.145 213.673 1.00 89.35 C
ANISOU 2891 CA GLU B 110 12707 8105 13136 -1019 370 596 C
ATOM 2892 C GLU B 110 23.464 -47.655 214.883 1.00 89.39 C
ANISOU 2892 C GLU B 110 12952 7980 13033 -841 538 867 C
ATOM 2893 O GLU B 110 22.952 -47.680 216.005 1.00 99.74 O
ANISOU 2893 O GLU B 110 14282 9257 14359 -903 739 1093 O
ATOM 2894 CB GLU B 110 21.179 -47.353 213.878 1.00100.29 C
ANISOU 2894 CB GLU B 110 13900 9391 14814 -1326 478 609 C
ATOM 2895 CG GLU B 110 20.308 -46.709 212.810 1.00111.26 C
ANISOU 2895 CG GLU B 110 15013 10949 16313 -1485 275 365 C
ATOM 2896 CD GLU B 110 18.826 -46.819 213.117 1.00122.54 C
ANISOU 2896 CD GLU B 110 16186 12306 18070 -1775 385 383 C
ATOM 2897 OE1 GLU B 110 18.397 -46.331 214.185 1.00125.23 O
ANISOU 2897 OE1 GLU B 110 16429 12744 18410 -1786 604 581 O
ATOM 2898 OE2 GLU B 110 18.092 -47.401 212.291 1.00131.75 O
ANISOU 2898 OE2 GLU B 110 17243 13315 19501 -1995 258 184 O
ATOM 2899 N SER B 111 24.721 -48.044 214.669 1.00 86.93 N
ANISOU 2899 N SER B 111 12828 7598 12601 -607 457 846 N
ATOM 2900 CA SER B 111 25.579 -48.506 215.751 1.00 87.61 C
ANISOU 2900 CA SER B 111 13143 7573 12573 -394 551 1096 C
ATOM 2901 C SER B 111 27.018 -48.124 215.436 1.00 84.44 C
ANISOU 2901 C SER B 111 12784 7326 11974 -93 397 1021 C
ATOM 2902 O SER B 111 27.385 -47.905 214.277 1.00 81.57 O
ANISOU 2902 O SER B 111 12343 7038 11611 -68 266 774 O
ATOM 2903 CB SER B 111 25.462 -50.020 215.970 1.00 88.88 C
ANISOU 2903 CB SER B 111 13533 7283 12956 -457 669 1194 C
ATOM 2904 OG SER B 111 26.047 -50.739 214.899 1.00 83.94 O
ANISOU 2904 OG SER B 111 12986 6465 12443 -398 551 974 O
ATOM 2905 N TRP B 112 27.828 -48.022 216.487 1.00 75.50 N
ANISOU 2905 N TRP B 112 11773 6246 10669 132 415 1236 N
ATOM 2906 CA TRP B 112 29.238 -47.680 216.357 1.00 68.92 C
ANISOU 2906 CA TRP B 112 10947 5554 9686 425 272 1185 C
ATOM 2907 C TRP B 112 30.071 -48.953 216.441 1.00 72.94 C
ANISOU 2907 C TRP B 112 11674 5732 10309 610 263 1250 C
ATOM 2908 O TRP B 112 30.013 -49.672 217.444 1.00 84.56 O
ANISOU 2908 O TRP B 112 13347 6992 11790 659 345 1505 O
ATOM 2909 CB TRP B 112 29.661 -46.684 217.435 1.00 65.94 C
ANISOU 2909 CB TRP B 112 10536 5465 9052 570 246 1348 C
ATOM 2910 CG TRP B 112 31.052 -46.186 217.246 1.00 68.03 C
ANISOU 2910 CG TRP B 112 10740 5908 9202 835 87 1262 C
ATOM 2911 CD1 TRP B 112 32.181 -46.656 217.856 1.00 62.45 C
ANISOU 2911 CD1 TRP B 112 10154 5124 8451 1107 3 1381 C
ATOM 2912 CD2 TRP B 112 31.474 -45.125 216.377 1.00 61.83 C
ANISOU 2912 CD2 TRP B 112 9742 5396 8354 853 -4 1039 C
ATOM 2913 NE1 TRP B 112 33.279 -45.947 217.425 1.00 67.61 N
ANISOU 2913 NE1 TRP B 112 10646 5995 9048 1282 -130 1228 N
ATOM 2914 CE2 TRP B 112 32.872 -45.002 216.518 1.00 64.09 C
ANISOU 2914 CE2 TRP B 112 10009 5760 8583 1122 -117 1023 C
ATOM 2915 CE3 TRP B 112 30.806 -44.269 215.496 1.00 66.48 C
ANISOU 2915 CE3 TRP B 112 10160 6163 8938 673 -4 861 C
ATOM 2916 CZ2 TRP B 112 33.614 -44.058 215.809 1.00 60.48 C
ANISOU 2916 CZ2 TRP B 112 9363 5542 8075 1190 -190 833 C
ATOM 2917 CZ3 TRP B 112 31.546 -43.329 214.792 1.00 63.18 C
ANISOU 2917 CZ3 TRP B 112 9595 5975 8434 756 -87 693 C
ATOM 2918 CH2 TRP B 112 32.935 -43.233 214.953 1.00 63.51 C
ANISOU 2918 CH2 TRP B 112 9619 6081 8431 1001 -159 679 C
ATOM 2919 N LEU B 113 30.847 -49.221 215.390 1.00 67.22 N
ANISOU 2919 N LEU B 113 10922 4953 9666 721 177 1025 N
ATOM 2920 CA LEU B 113 31.617 -50.454 215.278 1.00 73.64 C
ANISOU 2920 CA LEU B 113 11918 5424 10637 902 175 1034 C
ATOM 2921 C LEU B 113 33.127 -50.229 215.300 1.00 77.58 C
ANISOU 2921 C LEU B 113 12370 6040 11066 1243 58 1003 C
ATOM 2922 O LEU B 113 33.881 -51.190 215.101 1.00 79.58 O
ANISOU 2922 O LEU B 113 12739 6024 11475 1432 48 979 O
ATOM 2923 CB LEU B 113 31.216 -51.198 213.999 1.00 72.27 C
ANISOU 2923 CB LEU B 113 11777 5009 10673 742 208 768 C
ATOM 2924 CG LEU B 113 29.729 -51.535 213.836 1.00 75.87 C
ANISOU 2924 CG LEU B 113 12244 5316 11269 388 296 749 C
ATOM 2925 CD1 LEU B 113 29.421 -51.933 212.399 1.00 73.07 C
ANISOU 2925 CD1 LEU B 113 11876 4836 11053 234 257 411 C
ATOM 2926 CD2 LEU B 113 29.308 -52.650 214.794 1.00 78.80 C
ANISOU 2926 CD2 LEU B 113 12835 5309 11796 339 432 1012 C
ATOM 2927 N PHE B 114 33.593 -48.994 215.521 1.00 67.13 N
ANISOU 2927 N PHE B 114 10865 5097 9546 1324 -28 991 N
ATOM 2928 CA PHE B 114 35.010 -48.657 215.402 1.00 75.19 C
ANISOU 2928 CA PHE B 114 11769 6259 10539 1611 -138 912 C
ATOM 2929 C PHE B 114 35.766 -48.626 216.732 1.00 83.51 C
ANISOU 2929 C PHE B 114 12873 7363 11493 1862 -254 1164 C
ATOM 2930 O PHE B 114 36.968 -48.343 216.731 1.00 91.81 O
ANISOU 2930 O PHE B 114 13794 8537 12554 2106 -371 1102 O
ATOM 2931 CB PHE B 114 35.178 -47.301 214.703 1.00 81.17 C
ANISOU 2931 CB PHE B 114 12284 7387 11170 1543 -166 711 C
ATOM 2932 CG PHE B 114 34.448 -47.188 213.392 1.00 87.21 C
ANISOU 2932 CG PHE B 114 13015 8147 11974 1312 -93 472 C
ATOM 2933 CD1 PHE B 114 34.874 -47.890 212.278 1.00 89.97 C
ANISOU 2933 CD1 PHE B 114 13414 8313 12459 1356 -49 251 C
ATOM 2934 CD2 PHE B 114 33.349 -46.352 213.272 1.00 85.45 C
ANISOU 2934 CD2 PHE B 114 12714 8109 11643 1064 -78 460 C
ATOM 2935 CE1 PHE B 114 34.205 -47.771 211.072 1.00 90.71 C
ANISOU 2935 CE1 PHE B 114 13509 8415 12542 1147 -11 24 C
ATOM 2936 CE2 PHE B 114 32.678 -46.229 212.070 1.00 80.02 C
ANISOU 2936 CE2 PHE B 114 12000 7428 10976 868 -60 246 C
ATOM 2937 CZ PHE B 114 33.107 -46.940 210.970 1.00 84.97 C
ANISOU 2937 CZ PHE B 114 12705 7879 11699 905 -36 29 C
ATOM 2938 N GLY B 115 35.110 -48.898 217.857 1.00 77.77 N
ANISOU 2938 N GLY B 115 12331 6550 10667 1808 -226 1438 N
ATOM 2939 CA GLY B 115 35.765 -48.867 219.150 1.00 84.61 C
ANISOU 2939 CA GLY B 115 13296 7470 11382 2044 -359 1686 C
ATOM 2940 C GLY B 115 35.786 -47.480 219.779 1.00 83.87 C
ANISOU 2940 C GLY B 115 13062 7781 11025 2019 -439 1704 C
ATOM 2941 O GLY B 115 35.364 -46.484 219.193 1.00 76.76 O
ANISOU 2941 O GLY B 115 11968 7120 10076 1838 -389 1527 O
ATOM 2942 N HIS B 116 36.303 -47.422 221.012 1.00 88.13 N
ANISOU 2942 N HIS B 116 13720 8383 11382 2216 -579 1922 N
ATOM 2943 CA HIS B 116 36.231 -46.193 221.804 1.00 88.01 C
ANISOU 2943 CA HIS B 116 13636 8716 11088 2185 -650 1958 C
ATOM 2944 C HIS B 116 37.159 -45.104 221.263 1.00 92.46 C
ANISOU 2944 C HIS B 116 13879 9584 11667 2265 -792 1710 C
ATOM 2945 O HIS B 116 36.769 -43.927 221.174 1.00 94.03 O
ANISOU 2945 O HIS B 116 13931 10052 11746 2106 -754 1599 O
ATOM 2946 CB HIS B 116 36.576 -46.494 223.267 1.00 95.19 C
ANISOU 2946 CB HIS B 116 14802 9599 11768 2386 -786 2250 C
ATOM 2947 CG HIS B 116 35.670 -47.492 223.923 1.00108.97 C
ANISOU 2947 CG HIS B 116 16851 11077 13477 2268 -610 2508 C
ATOM 2948 ND1 HIS B 116 35.691 -48.837 223.617 1.00116.26 N
ANISOU 2948 ND1 HIS B 116 17877 11655 14641 2287 -549 2570 N
ATOM 2949 CD2 HIS B 116 34.731 -47.342 224.888 1.00112.91 C
ANISOU 2949 CD2 HIS B 116 17531 11623 13747 2101 -461 2694 C
ATOM 2950 CE1 HIS B 116 34.798 -49.470 224.359 1.00115.96 C
ANISOU 2950 CE1 HIS B 116 18067 11459 14531 2129 -378 2792 C
ATOM 2951 NE2 HIS B 116 34.203 -48.586 225.139 1.00113.84 N
ANISOU 2951 NE2 HIS B 116 17848 11428 13978 2015 -311 2870 N
ATOM 2952 N ALA B 117 38.391 -45.474 220.904 1.00 91.52 N
ANISOU 2952 N ALA B 117 13641 9414 11718 2511 -940 1619 N
ATOM 2953 CA ALA B 117 39.381 -44.478 220.506 1.00 79.44 C
ANISOU 2953 CA ALA B 117 11798 8160 10227 2596 -1064 1401 C
ATOM 2954 C ALA B 117 38.918 -43.709 219.279 1.00 74.52 C
ANISOU 2954 C ALA B 117 10983 7663 9670 2357 -892 1155 C
ATOM 2955 O ALA B 117 38.961 -42.474 219.247 1.00 73.97 O
ANISOU 2955 O ALA B 117 10740 7870 9495 2266 -911 1047 O
ATOM 2956 CB ALA B 117 40.724 -45.158 220.244 1.00 75.52 C
ANISOU 2956 CB ALA B 117 11185 7544 9967 2898 -1209 1339 C
ATOM 2957 N LEU B 118 38.461 -44.425 218.253 1.00 71.28 N
ANISOU 2957 N LEU B 118 10620 7038 9424 2254 -731 1065 N
ATOM 2958 CA LEU B 118 37.910 -43.757 217.084 1.00 71.08 C
ANISOU 2958 CA LEU B 118 10467 7120 9421 2026 -587 853 C
ATOM 2959 C LEU B 118 36.610 -43.028 217.402 1.00 67.83 C
ANISOU 2959 C LEU B 118 10103 6835 8833 1771 -509 922 C
ATOM 2960 O LEU B 118 36.308 -42.025 216.748 1.00 65.08 O
ANISOU 2960 O LEU B 118 9608 6679 8441 1623 -460 776 O
ATOM 2961 CB LEU B 118 37.718 -44.765 215.951 1.00 73.51 C
ANISOU 2961 CB LEU B 118 10850 7159 9922 1981 -463 728 C
ATOM 2962 CG LEU B 118 39.028 -45.401 215.464 1.00 70.38 C
ANISOU 2962 CG LEU B 118 10372 6641 9729 2238 -496 609 C
ATOM 2963 CD1 LEU B 118 38.778 -46.354 214.310 1.00 67.20 C
ANISOU 2963 CD1 LEU B 118 10073 5969 9493 2179 -352 453 C
ATOM 2964 CD2 LEU B 118 40.050 -44.335 215.075 1.00 67.67 C
ANISOU 2964 CD2 LEU B 118 9744 6574 9393 2317 -531 436 C
ATOM 2965 N CYS B 119 35.858 -43.485 218.407 1.00 68.76 N
ANISOU 2965 N CYS B 119 10423 6847 8855 1727 -485 1148 N
ATOM 2966 CA CYS B 119 34.683 -42.737 218.845 1.00 73.86 C
ANISOU 2966 CA CYS B 119 11086 7629 9348 1509 -392 1214 C
ATOM 2967 C CYS B 119 35.061 -41.356 219.362 1.00 72.34 C
ANISOU 2967 C CYS B 119 10751 7760 8977 1541 -481 1173 C
ATOM 2968 O CYS B 119 34.277 -40.408 219.241 1.00 64.24 O
ANISOU 2968 O CYS B 119 9639 6892 7876 1365 -402 1117 O
ATOM 2969 CB CYS B 119 33.930 -43.520 219.924 1.00 74.89 C
ANISOU 2969 CB CYS B 119 11472 7577 9404 1473 -313 1477 C
ATOM 2970 SG CYS B 119 32.631 -42.585 220.782 1.00 77.74 S
ANISOU 2970 SG CYS B 119 11856 8120 9562 1258 -172 1582 S
ATOM 2971 N LYS B 120 36.247 -41.213 219.948 1.00 73.25 N
ANISOU 2971 N LYS B 120 10829 7964 9037 1766 -655 1191 N
ATOM 2972 CA LYS B 120 36.685 -39.852 220.253 1.00 69.40 C
ANISOU 2972 CA LYS B 120 10173 7772 8424 1774 -746 1093 C
ATOM 2973 C LYS B 120 37.299 -39.165 219.034 1.00 70.30 C
ANISOU 2973 C LYS B 120 10029 7998 8686 1747 -736 847 C
ATOM 2974 O LYS B 120 37.014 -37.993 218.774 1.00 70.93 O
ANISOU 2974 O LYS B 120 9982 8263 8705 1616 -693 743 O
ATOM 2975 CB LYS B 120 37.671 -39.848 221.422 1.00 66.69 C
ANISOU 2975 CB LYS B 120 9875 7508 7955 2004 -968 1190 C
ATOM 2976 CG LYS B 120 37.001 -40.035 222.780 1.00 69.30 C
ANISOU 2976 CG LYS B 120 10483 7824 8025 2001 -966 1426 C
ATOM 2977 CD LYS B 120 37.982 -39.872 223.934 1.00 66.28 C
ANISOU 2977 CD LYS B 120 10160 7560 7464 2228 -1231 1501 C
ATOM 2978 CE LYS B 120 37.339 -40.228 225.268 1.00 69.72 C
ANISOU 2978 CE LYS B 120 10943 7948 7598 2243 -1210 1761 C
ATOM 2979 NZ LYS B 120 36.241 -39.302 225.647 1.00 71.06 N
ANISOU 2979 NZ LYS B 120 11161 8263 7575 2023 -1021 1749 N
ATOM 2980 N VAL B 121 38.120 -39.881 218.263 1.00 72.54 N
ANISOU 2980 N VAL B 121 10246 8153 9163 1870 -752 757 N
ATOM 2981 CA VAL B 121 38.933 -39.227 217.239 1.00 61.65 C
ANISOU 2981 CA VAL B 121 8628 6888 7908 1878 -728 534 C
ATOM 2982 C VAL B 121 38.070 -38.716 216.091 1.00 59.37 C
ANISOU 2982 C VAL B 121 8319 6626 7614 1650 -559 415 C
ATOM 2983 O VAL B 121 38.180 -37.554 215.682 1.00 59.86 O
ANISOU 2983 O VAL B 121 8235 6870 7639 1562 -528 303 O
ATOM 2984 CB VAL B 121 40.029 -40.180 216.732 1.00 65.79 C
ANISOU 2984 CB VAL B 121 9090 7257 8650 2083 -754 461 C
ATOM 2985 CG1 VAL B 121 40.634 -39.649 215.443 1.00 66.28 C
ANISOU 2985 CG1 VAL B 121 8950 7393 8840 2043 -633 226 C
ATOM 2986 CG2 VAL B 121 41.110 -40.372 217.786 1.00 64.97 C
ANISOU 2986 CG2 VAL B 121 8921 7188 8575 2336 -975 541 C
ATOM 2987 N ILE B 122 37.235 -39.584 215.525 1.00 60.26 N
ANISOU 2987 N ILE B 122 8579 6544 7772 1554 -462 434 N
ATOM 2988 CA ILE B 122 36.484 -39.210 214.331 1.00 59.64 C
ANISOU 2988 CA ILE B 122 8488 6480 7691 1361 -348 306 C
ATOM 2989 C ILE B 122 35.522 -38.057 214.580 1.00 57.40 C
ANISOU 2989 C ILE B 122 8164 6373 7272 1189 -333 341 C
ATOM 2990 O ILE B 122 35.517 -37.106 213.784 1.00 60.05 O
ANISOU 2990 O ILE B 122 8400 6839 7579 1106 -295 222 O
ATOM 2991 CB ILE B 122 35.791 -40.450 213.741 1.00 56.37 C
ANISOU 2991 CB ILE B 122 8240 5809 7370 1291 -283 301 C
ATOM 2992 CG1 ILE B 122 36.858 -41.476 213.353 1.00 58.81 C
ANISOU 2992 CG1 ILE B 122 8573 5938 7832 1481 -277 227 C
ATOM 2993 CG2 ILE B 122 34.937 -40.078 212.552 1.00 52.11 C
ANISOU 2993 CG2 ILE B 122 7703 5295 6804 1091 -216 168 C
ATOM 2994 CD1 ILE B 122 36.310 -42.773 212.805 1.00 65.01 C
ANISOU 2994 CD1 ILE B 122 9539 6432 8730 1430 -215 200 C
ATOM 2995 N PRO B 123 34.684 -38.072 215.616 1.00 61.68 N
ANISOU 2995 N PRO B 123 8789 6914 7733 1132 -342 500 N
ATOM 2996 CA PRO B 123 33.868 -36.879 215.878 1.00 57.91 C
ANISOU 2996 CA PRO B 123 8245 6611 7149 997 -314 511 C
ATOM 2997 C PRO B 123 34.712 -35.643 216.116 1.00 56.60 C
ANISOU 2997 C PRO B 123 7937 6655 6914 1062 -370 439 C
ATOM 2998 O PRO B 123 34.345 -34.545 215.670 1.00 55.93 O
ANISOU 2998 O PRO B 123 7760 6693 6796 959 -334 366 O
ATOM 2999 CB PRO B 123 33.057 -37.277 217.126 1.00 60.43 C
ANISOU 2999 CB PRO B 123 8693 6874 7394 967 -283 700 C
ATOM 3000 CG PRO B 123 33.069 -38.780 217.114 1.00 65.47 C
ANISOU 3000 CG PRO B 123 9482 7260 8133 1012 -268 781 C
ATOM 3001 CD PRO B 123 34.395 -39.166 216.553 1.00 70.18 C
ANISOU 3001 CD PRO B 123 10036 7816 8812 1184 -347 679 C
ATOM 3002 N TYR B 124 35.868 -35.810 216.753 1.00 60.47 N
ANISOU 3002 N TYR B 124 8399 7175 7404 1235 -469 450 N
ATOM 3003 CA TYR B 124 36.776 -34.691 216.961 1.00 56.65 C
ANISOU 3003 CA TYR B 124 7753 6875 6896 1287 -538 355 C
ATOM 3004 C TYR B 124 37.261 -34.136 215.630 1.00 61.64 C
ANISOU 3004 C TYR B 124 8244 7544 7631 1236 -460 186 C
ATOM 3005 O TYR B 124 37.229 -32.921 215.400 1.00 62.29 O
ANISOU 3005 O TYR B 124 8230 7757 7682 1149 -426 114 O
ATOM 3006 CB TYR B 124 37.959 -35.147 217.819 1.00 56.60 C
ANISOU 3006 CB TYR B 124 7722 6877 6908 1493 -696 386 C
ATOM 3007 CG TYR B 124 39.106 -34.164 217.891 1.00 58.67 C
ANISOU 3007 CG TYR B 124 7768 7305 7220 1551 -785 249 C
ATOM 3008 CD1 TYR B 124 38.999 -33.001 218.643 1.00 58.53 C
ANISOU 3008 CD1 TYR B 124 7710 7452 7079 1492 -842 227 C
ATOM 3009 CD2 TYR B 124 40.301 -34.405 217.221 1.00 52.48 C
ANISOU 3009 CD2 TYR B 124 6810 6501 6629 1658 -799 127 C
ATOM 3010 CE1 TYR B 124 40.043 -32.100 218.721 1.00 55.90 C
ANISOU 3010 CE1 TYR B 124 7169 7252 6819 1521 -928 85 C
ATOM 3011 CE2 TYR B 124 41.358 -33.506 217.296 1.00 55.40 C
ANISOU 3011 CE2 TYR B 124 6947 7014 7089 1690 -867 -7 C
ATOM 3012 CZ TYR B 124 41.219 -32.354 218.046 1.00 56.93 C
ANISOU 3012 CZ TYR B 124 7106 7363 7164 1613 -941 -28 C
ATOM 3013 OH TYR B 124 42.256 -31.452 218.131 1.00 52.26 O
ANISOU 3013 OH TYR B 124 6275 6896 6687 1620 -1013 -177 O
ATOM 3014 N LEU B 125 37.719 -35.015 214.738 1.00 61.55 N
ANISOU 3014 N LEU B 125 8242 7405 7737 1292 -411 123 N
ATOM 3015 CA LEU B 125 38.218 -34.545 213.454 1.00 56.49 C
ANISOU 3015 CA LEU B 125 7505 6795 7163 1249 -302 -34 C
ATOM 3016 C LEU B 125 37.109 -33.909 212.630 1.00 52.67 C
ANISOU 3016 C LEU B 125 7091 6336 6586 1064 -219 -50 C
ATOM 3017 O LEU B 125 37.364 -32.962 211.881 1.00 65.50 O
ANISOU 3017 O LEU B 125 8646 8046 8196 1000 -144 -137 O
ATOM 3018 CB LEU B 125 38.875 -35.694 212.686 1.00 49.03 C
ANISOU 3018 CB LEU B 125 6587 5694 6347 1354 -243 -111 C
ATOM 3019 CG LEU B 125 40.215 -36.206 213.232 1.00 55.66 C
ANISOU 3019 CG LEU B 125 7296 6513 7338 1569 -319 -132 C
ATOM 3020 CD1 LEU B 125 40.741 -37.357 212.391 1.00 56.01 C
ANISOU 3020 CD1 LEU B 125 7377 6377 7529 1676 -228 -222 C
ATOM 3021 CD2 LEU B 125 41.237 -35.081 213.307 1.00 54.19 C
ANISOU 3021 CD2 LEU B 125 6868 6504 7216 1589 -324 -233 C
ATOM 3022 N GLN B 126 35.870 -34.388 212.775 1.00 57.19 N
ANISOU 3022 N GLN B 126 7793 6828 7107 976 -235 40 N
ATOM 3023 CA GLN B 126 34.763 -33.748 212.073 1.00 55.43 C
ANISOU 3023 CA GLN B 126 7604 6639 6818 817 -202 28 C
ATOM 3024 C GLN B 126 34.528 -32.331 212.587 1.00 53.50 C
ANISOU 3024 C GLN B 126 7265 6552 6509 767 -211 55 C
ATOM 3025 O GLN B 126 34.360 -31.389 211.792 1.00 55.87 O
ANISOU 3025 O GLN B 126 7539 6914 6775 693 -172 2 O
ATOM 3026 CB GLN B 126 33.501 -34.593 212.221 1.00 62.27 C
ANISOU 3026 CB GLN B 126 8578 7383 7697 730 -223 108 C
ATOM 3027 CG GLN B 126 32.241 -33.932 211.692 1.00 72.58 C
ANISOU 3027 CG GLN B 126 9878 8732 8968 577 -231 108 C
ATOM 3028 CD GLN B 126 32.372 -33.507 210.242 1.00 94.11 C
ANISOU 3028 CD GLN B 126 12631 11481 11646 533 -221 -13 C
ATOM 3029 OE1 GLN B 126 31.950 -32.412 209.863 1.00103.23 O
ANISOU 3029 OE1 GLN B 126 13745 12734 12742 474 -232 -15 O
ATOM 3030 NE2 GLN B 126 32.950 -34.377 209.418 1.00101.10 N
ANISOU 3030 NE2 GLN B 126 13607 12262 12545 570 -191 -110 N
ATOM 3031 N ALA B 127 34.522 -32.156 213.912 1.00 49.78 N
ANISOU 3031 N ALA B 127 6769 6135 6009 812 -260 138 N
ATOM 3032 CA ALA B 127 34.327 -30.816 214.456 1.00 42.65 C
ANISOU 3032 CA ALA B 127 5790 5366 5048 771 -261 138 C
ATOM 3033 C ALA B 127 35.464 -29.891 214.043 1.00 47.27 C
ANISOU 3033 C ALA B 127 6257 6035 5668 796 -244 26 C
ATOM 3034 O ALA B 127 35.235 -28.724 213.694 1.00 52.36 O
ANISOU 3034 O ALA B 127 6858 6740 6298 719 -201 -9 O
ATOM 3035 CB ALA B 127 34.211 -30.881 215.979 1.00 43.37 C
ANISOU 3035 CB ALA B 127 5914 5499 5066 824 -312 227 C
ATOM 3036 N VAL B 128 36.695 -30.408 214.047 1.00 47.00 N
ANISOU 3036 N VAL B 128 6161 5990 5707 903 -269 -31 N
ATOM 3037 CA VAL B 128 37.842 -29.609 213.626 1.00 52.47 C
ANISOU 3037 CA VAL B 128 6705 6751 6480 914 -226 -149 C
ATOM 3038 C VAL B 128 37.714 -29.224 212.161 1.00 58.02 C
ANISOU 3038 C VAL B 128 7439 7420 7184 822 -84 -205 C
ATOM 3039 O VAL B 128 38.063 -28.106 211.762 1.00 53.02 O
ANISOU 3039 O VAL B 128 6735 6840 6569 757 -8 -260 O
ATOM 3040 CB VAL B 128 39.151 -30.380 213.878 1.00 50.11 C
ANISOU 3040 CB VAL B 128 6301 6436 6304 1061 -279 -203 C
ATOM 3041 CG1 VAL B 128 40.316 -29.660 213.208 1.00 51.43 C
ANISOU 3041 CG1 VAL B 128 6284 6652 6604 1050 -183 -342 C
ATOM 3042 CG2 VAL B 128 39.399 -30.557 215.362 1.00 48.83 C
ANISOU 3042 CG2 VAL B 128 6119 6327 6107 1164 -456 -145 C
ATOM 3043 N SER B 129 37.211 -30.145 211.338 1.00 58.38 N
ANISOU 3043 N SER B 129 7614 7368 7201 812 -49 -194 N
ATOM 3044 CA SER B 129 37.052 -29.853 209.923 1.00 61.97 C
ANISOU 3044 CA SER B 129 8150 7794 7602 733 64 -247 C
ATOM 3045 C SER B 129 36.068 -28.714 209.724 1.00 55.73 C
ANISOU 3045 C SER B 129 7402 7050 6721 623 53 -190 C
ATOM 3046 O SER B 129 36.323 -27.787 208.941 1.00 55.32 O
ANISOU 3046 O SER B 129 7360 7021 6636 568 147 -220 O
ATOM 3047 CB SER B 129 36.586 -31.114 209.195 1.00 65.15 C
ANISOU 3047 CB SER B 129 8704 8077 7972 740 64 -262 C
ATOM 3048 OG SER B 129 36.356 -30.866 207.822 1.00 74.62 O
ANISOU 3048 OG SER B 129 10027 9256 9070 666 147 -318 O
ATOM 3049 N VAL B 130 34.966 -28.731 210.476 1.00 52.14 N
ANISOU 3049 N VAL B 130 6967 6601 6241 596 -47 -103 N
ATOM 3050 CA VAL B 130 33.988 -27.655 210.345 1.00 48.31 C
ANISOU 3050 CA VAL B 130 6496 6151 5709 515 -64 -52 C
ATOM 3051 C VAL B 130 34.583 -26.330 210.805 1.00 50.97 C
ANISOU 3051 C VAL B 130 6732 6558 6076 509 -18 -74 C
ATOM 3052 O VAL B 130 34.375 -25.282 210.172 1.00 50.10 O
ANISOU 3052 O VAL B 130 6645 6447 5941 454 29 -67 O
ATOM 3053 CB VAL B 130 32.709 -27.994 211.129 1.00 51.31 C
ANISOU 3053 CB VAL B 130 6882 6519 6096 492 -146 33 C
ATOM 3054 CG1 VAL B 130 31.646 -26.928 210.868 1.00 42.41 C
ANISOU 3054 CG1 VAL B 130 5744 5414 4957 428 -167 75 C
ATOM 3055 CG2 VAL B 130 32.211 -29.377 210.752 1.00 56.17 C
ANISOU 3055 CG2 VAL B 130 7583 7040 6721 479 -187 42 C
ATOM 3056 N SER B 131 35.327 -26.347 211.914 1.00 55.20 N
ANISOU 3056 N SER B 131 7165 7143 6665 566 -45 -104 N
ATOM 3057 CA SER B 131 35.902 -25.103 212.415 1.00 48.73 C
ANISOU 3057 CA SER B 131 6243 6382 5890 545 -20 -155 C
ATOM 3058 C SER B 131 36.899 -24.527 211.419 1.00 53.70 C
ANISOU 3058 C SER B 131 6828 6994 6580 506 104 -228 C
ATOM 3059 O SER B 131 36.870 -23.328 211.118 1.00 46.47 O
ANISOU 3059 O SER B 131 5908 6069 5681 435 175 -234 O
ATOM 3060 CB SER B 131 36.569 -25.340 213.770 1.00 49.25 C
ANISOU 3060 CB SER B 131 6220 6511 5983 618 -113 -190 C
ATOM 3061 OG SER B 131 37.434 -24.268 214.107 1.00 52.29 O
ANISOU 3061 OG SER B 131 6482 6944 6443 591 -102 -287 O
ATOM 3062 N VAL B 132 37.772 -25.375 210.871 1.00 47.56 N
ANISOU 3062 N VAL B 132 6026 6197 5846 552 158 -281 N
ATOM 3063 CA VAL B 132 38.764 -24.888 209.919 1.00 46.22 C
ANISOU 3063 CA VAL B 132 5809 6010 5743 510 328 -355 C
ATOM 3064 C VAL B 132 38.078 -24.324 208.686 1.00 49.99 C
ANISOU 3064 C VAL B 132 6464 6432 6096 428 429 -296 C
ATOM 3065 O VAL B 132 38.478 -23.277 208.163 1.00 55.04 O
ANISOU 3065 O VAL B 132 7102 7052 6760 354 564 -304 O
ATOM 3066 CB VAL B 132 39.751 -26.011 209.548 1.00 43.44 C
ANISOU 3066 CB VAL B 132 5397 5638 5470 594 388 -433 C
ATOM 3067 CG1 VAL B 132 40.727 -25.520 208.492 1.00 46.73 C
ANISOU 3067 CG1 VAL B 132 5768 6031 5956 540 620 -512 C
ATOM 3068 CG2 VAL B 132 40.489 -26.493 210.784 1.00 48.26 C
ANISOU 3068 CG2 VAL B 132 5827 6300 6211 698 251 -479 C
ATOM 3069 N ALA B 133 36.996 -24.968 208.235 1.00 49.01 N
ANISOU 3069 N ALA B 133 6502 6278 5843 436 350 -229 N
ATOM 3070 CA ALA B 133 36.337 -24.497 207.022 1.00 54.21 C
ANISOU 3070 CA ALA B 133 7346 6891 6359 376 396 -172 C
ATOM 3071 C ALA B 133 35.676 -23.142 207.244 1.00 52.28 C
ANISOU 3071 C ALA B 133 7106 6643 6114 327 365 -93 C
ATOM 3072 O ALA B 133 35.876 -22.201 206.460 1.00 59.17 O
ANISOU 3072 O ALA B 133 8064 7473 6943 275 479 -60 O
ATOM 3073 CB ALA B 133 35.313 -25.530 206.547 1.00 43.70 C
ANISOU 3073 CB ALA B 133 6158 5530 4915 391 274 -143 C
ATOM 3074 N VAL B 134 34.885 -23.015 208.313 1.00 55.17 N
ANISOU 3074 N VAL B 134 7394 7038 6530 346 232 -58 N
ATOM 3075 CA VAL B 134 34.193 -21.745 208.501 1.00 54.61 C
ANISOU 3075 CA VAL B 134 7328 6944 6477 317 212 5 C
ATOM 3076 C VAL B 134 35.182 -20.630 208.831 1.00 52.62 C
ANISOU 3076 C VAL B 134 6987 6678 6328 275 334 -49 C
ATOM 3077 O VAL B 134 34.985 -19.481 208.413 1.00 50.32 O
ANISOU 3077 O VAL B 134 6757 6318 6043 234 395 1 O
ATOM 3078 CB VAL B 134 33.090 -21.879 209.567 1.00 55.87 C
ANISOU 3078 CB VAL B 134 7421 7133 6672 349 82 39 C
ATOM 3079 CG1 VAL B 134 33.690 -22.014 210.952 1.00 58.29 C
ANISOU 3079 CG1 VAL B 134 7597 7500 7051 376 77 -31 C
ATOM 3080 CG2 VAL B 134 32.122 -20.700 209.493 1.00 60.69 C
ANISOU 3080 CG2 VAL B 134 8055 7699 7306 342 56 109 C
ATOM 3081 N LEU B 135 36.270 -20.934 209.552 1.00 52.09 N
ANISOU 3081 N LEU B 135 6771 6661 6359 283 363 -152 N
ATOM 3082 CA LEU B 135 37.257 -19.895 209.832 1.00 49.95 C
ANISOU 3082 CA LEU B 135 6386 6371 6221 221 467 -230 C
ATOM 3083 C LEU B 135 37.998 -19.482 208.567 1.00 54.58 C
ANISOU 3083 C LEU B 135 7036 6888 6815 151 671 -224 C
ATOM 3084 O LEU B 135 38.323 -18.302 208.385 1.00 63.03 O
ANISOU 3084 O LEU B 135 8102 7883 7963 68 790 -224 O
ATOM 3085 CB LEU B 135 38.241 -20.367 210.900 1.00 57.34 C
ANISOU 3085 CB LEU B 135 7129 7388 7269 256 404 -352 C
ATOM 3086 CG LEU B 135 37.736 -20.405 212.341 1.00 60.88 C
ANISOU 3086 CG LEU B 135 7530 7900 7700 306 236 -372 C
ATOM 3087 CD1 LEU B 135 38.837 -20.909 213.267 1.00 57.04 C
ANISOU 3087 CD1 LEU B 135 6879 7496 7298 355 144 -485 C
ATOM 3088 CD2 LEU B 135 37.257 -19.030 212.789 1.00 60.34 C
ANISOU 3088 CD2 LEU B 135 7475 7787 7664 248 250 -384 C
ATOM 3089 N THR B 136 38.256 -20.435 207.668 1.00 53.23 N
ANISOU 3089 N THR B 136 6944 6724 6557 177 737 -220 N
ATOM 3090 CA THR B 136 38.898 -20.094 206.406 1.00 51.94 C
ANISOU 3090 CA THR B 136 6884 6494 6355 112 968 -207 C
ATOM 3091 C THR B 136 38.004 -19.176 205.590 1.00 58.98 C
ANISOU 3091 C THR B 136 8011 7299 7100 72 988 -65 C
ATOM 3092 O THR B 136 38.467 -18.186 205.008 1.00 61.73 O
ANISOU 3092 O THR B 136 8425 7560 7471 -10 1177 -27 O
ATOM 3093 CB THR B 136 39.213 -21.370 205.622 1.00 54.52 C
ANISOU 3093 CB THR B 136 7287 6844 6585 164 1028 -246 C
ATOM 3094 OG1 THR B 136 40.118 -22.182 206.380 1.00 56.05 O
ANISOU 3094 OG1 THR B 136 7251 7098 6946 224 1007 -369 O
ATOM 3095 CG2 THR B 136 39.835 -21.036 204.275 1.00 50.56 C
ANISOU 3095 CG2 THR B 136 6935 6276 5998 98 1304 -233 C
ATOM 3096 N LEU B 137 36.706 -19.488 205.545 1.00 51.64 N
ANISOU 3096 N LEU B 137 7203 6382 6035 133 791 21 N
ATOM 3097 CA LEU B 137 35.779 -18.615 204.830 1.00 51.98 C
ANISOU 3097 CA LEU B 137 7449 6345 5958 125 755 162 C
ATOM 3098 C LEU B 137 35.718 -17.235 205.470 1.00 51.19 C
ANISOU 3098 C LEU B 137 7275 6169 6008 89 783 191 C
ATOM 3099 O LEU B 137 35.670 -16.215 204.768 1.00 61.37 O
ANISOU 3099 O LEU B 137 8717 7342 7259 50 884 293 O
ATOM 3100 CB LEU B 137 34.389 -19.252 204.783 1.00 49.23 C
ANISOU 3100 CB LEU B 137 7174 6033 5498 199 510 223 C
ATOM 3101 CG LEU B 137 34.266 -20.492 203.902 1.00 50.81 C
ANISOU 3101 CG LEU B 137 7514 6269 5523 220 467 200 C
ATOM 3102 CD1 LEU B 137 32.863 -21.073 204.022 1.00 48.73 C
ANISOU 3102 CD1 LEU B 137 7265 6034 5218 269 207 239 C
ATOM 3103 CD2 LEU B 137 34.573 -20.125 202.460 1.00 47.68 C
ANISOU 3103 CD2 LEU B 137 7386 5812 4920 189 603 263 C
ATOM 3104 N SER B 138 35.750 -17.179 206.803 1.00 50.26 N
ANISOU 3104 N SER B 138 6947 6100 6050 101 702 100 N
ATOM 3105 CA SER B 138 35.732 -15.888 207.479 1.00 51.60 C
ANISOU 3105 CA SER B 138 7051 6189 6368 63 732 89 C
ATOM 3106 C SER B 138 36.971 -15.071 207.137 1.00 59.47 C
ANISOU 3106 C SER B 138 8021 7095 7481 -53 962 45 C
ATOM 3107 O SER B 138 36.890 -13.853 206.946 1.00 54.88 O
ANISOU 3107 O SER B 138 7515 6371 6965 -105 1051 104 O
ATOM 3108 CB SER B 138 35.632 -16.093 208.990 1.00 53.54 C
ANISOU 3108 CB SER B 138 7103 6521 6720 96 607 -26 C
ATOM 3109 OG SER B 138 34.586 -16.994 209.309 1.00 59.80 O
ANISOU 3109 OG SER B 138 7907 7394 7420 184 442 14 O
ATOM 3110 N PHE B 139 38.128 -15.726 207.037 1.00 56.57 N
ANISOU 3110 N PHE B 139 7537 6792 7165 -94 1073 -58 N
ATOM 3111 CA PHE B 139 39.342 -14.984 206.720 1.00 51.91 C
ANISOU 3111 CA PHE B 139 6875 6115 6732 -222 1317 -115 C
ATOM 3112 C PHE B 139 39.371 -14.554 205.260 1.00 63.17 C
ANISOU 3112 C PHE B 139 8559 7422 8021 -274 1534 31 C
ATOM 3113 O PHE B 139 39.889 -13.476 204.943 1.00 57.35 O
ANISOU 3113 O PHE B 139 7855 6542 7394 -389 1740 61 O
ATOM 3114 CB PHE B 139 40.573 -15.808 207.085 1.00 55.47 C
ANISOU 3114 CB PHE B 139 7080 6672 7322 -236 1368 -279 C
ATOM 3115 CG PHE B 139 40.919 -15.746 208.544 1.00 72.66 C
ANISOU 3115 CG PHE B 139 9003 8926 9680 -229 1200 -433 C
ATOM 3116 CD1 PHE B 139 39.918 -15.750 209.506 1.00 71.19 C
ANISOU 3116 CD1 PHE B 139 8843 8785 9422 -149 969 -420 C
ATOM 3117 CD2 PHE B 139 42.238 -15.683 208.956 1.00 86.78 C
ANISOU 3117 CD2 PHE B 139 10526 10741 11705 -300 1270 -597 C
ATOM 3118 CE1 PHE B 139 40.224 -15.689 210.852 1.00 63.85 C
ANISOU 3118 CE1 PHE B 139 7730 7928 8603 -139 816 -562 C
ATOM 3119 CE2 PHE B 139 42.553 -15.622 210.302 1.00 94.93 C
ANISOU 3119 CE2 PHE B 139 11349 11851 12870 -286 1072 -745 C
ATOM 3120 CZ PHE B 139 41.543 -15.625 211.250 1.00 84.83 C
ANISOU 3120 CZ PHE B 139 10148 10618 11464 -204 846 -724 C
ATOM 3121 N ILE B 140 38.797 -15.355 204.360 1.00 66.69 N
ANISOU 3121 N ILE B 140 9213 7912 8216 -198 1491 126 N
ATOM 3122 CA ILE B 140 38.647 -14.899 202.981 1.00 57.76 C
ANISOU 3122 CA ILE B 140 8394 6670 6884 -229 1655 286 C
ATOM 3123 C ILE B 140 37.773 -13.655 202.937 1.00 58.94 C
ANISOU 3123 C ILE B 140 8699 6675 7022 -221 1584 440 C
ATOM 3124 O ILE B 140 38.079 -12.681 202.233 1.00 64.31 O
ANISOU 3124 O ILE B 140 9553 7195 7687 -300 1792 553 O
ATOM 3125 CB ILE B 140 38.055 -16.013 202.101 1.00 50.28 C
ANISOU 3125 CB ILE B 140 7656 5804 5644 -138 1555 335 C
ATOM 3126 CG1 ILE B 140 39.007 -17.204 202.022 1.00 58.73 C
ANISOU 3126 CG1 ILE B 140 8599 6977 6739 -139 1673 181 C
ATOM 3127 CG2 ILE B 140 37.721 -15.469 200.712 1.00 52.43 C
ANISOU 3127 CG2 ILE B 140 8307 5967 5647 -150 1662 517 C
ATOM 3128 CD1 ILE B 140 38.423 -18.379 201.276 1.00 56.74 C
ANISOU 3128 CD1 ILE B 140 8542 6793 6224 -54 1560 190 C
ATOM 3129 N ALA B 141 36.677 -13.662 203.702 1.00 62.12 N
ANISOU 3129 N ALA B 141 9039 7116 7447 -123 1308 450 N
ATOM 3130 CA ALA B 141 35.791 -12.503 203.729 1.00 57.69 C
ANISOU 3130 CA ALA B 141 8596 6410 6914 -86 1228 583 C
ATOM 3131 C ALA B 141 36.494 -11.286 204.314 1.00 56.98 C
ANISOU 3131 C ALA B 141 8399 6172 7079 -196 1402 529 C
ATOM 3132 O ALA B 141 36.341 -10.169 203.810 1.00 65.36 O
ANISOU 3132 O ALA B 141 9641 7037 8155 -223 1504 667 O
ATOM 3133 CB ALA B 141 34.531 -12.829 204.527 1.00 50.01 C
ANISOU 3133 CB ALA B 141 7523 5519 5960 39 933 572 C
ATOM 3134 N LEU B 142 37.298 -11.489 205.361 1.00 56.87 N
ANISOU 3134 N LEU B 142 8102 6237 7269 -263 1429 328 N
ATOM 3135 CA LEU B 142 38.007 -10.371 205.977 1.00 59.62 C
ANISOU 3135 CA LEU B 142 8326 6449 7880 -386 1568 233 C
ATOM 3136 C LEU B 142 39.050 -9.796 205.027 1.00 68.01 C
ANISOU 3136 C LEU B 142 9480 7365 8995 -538 1893 287 C
ATOM 3137 O LEU B 142 39.216 -8.571 204.934 1.00 67.41 O
ANISOU 3137 O LEU B 142 9478 7074 9062 -632 2041 337 O
ATOM 3138 CB LEU B 142 38.660 -10.833 207.281 1.00 56.69 C
ANISOU 3138 CB LEU B 142 7636 6220 7683 -415 1478 -6 C
ATOM 3139 CG LEU B 142 39.222 -9.783 208.240 1.00 65.99 C
ANISOU 3139 CG LEU B 142 8648 7292 9132 -527 1520 -165 C
ATOM 3140 CD1 LEU B 142 38.102 -8.957 208.859 1.00 57.28 C
ANISOU 3140 CD1 LEU B 142 7632 6087 8047 -451 1388 -134 C
ATOM 3141 CD2 LEU B 142 40.045 -10.463 209.322 1.00 68.24 C
ANISOU 3141 CD2 LEU B 142 8639 7754 9535 -549 1411 -395 C
ATOM 3142 N ASP B 143 39.736 -10.668 204.286 1.00 75.78 N
ANISOU 3142 N ASP B 143 10476 8448 9870 -565 2031 280 N
ATOM 3143 CA ASP B 143 40.733 -10.208 203.328 1.00 72.92 C
ANISOU 3143 CA ASP B 143 10208 7956 9544 -713 2392 332 C
ATOM 3144 C ASP B 143 40.081 -9.424 202.200 1.00 75.09 C
ANISOU 3144 C ASP B 143 10885 8042 9605 -698 2493 598 C
ATOM 3145 O ASP B 143 40.539 -8.327 201.855 1.00 72.25 O
ANISOU 3145 O ASP B 143 10622 7462 9367 -829 2744 677 O
ATOM 3146 CB ASP B 143 41.512 -11.409 202.790 1.00 70.11 C
ANISOU 3146 CB ASP B 143 9784 7755 9100 -714 2522 255 C
ATOM 3147 CG ASP B 143 42.451 -11.045 201.658 1.00 76.72 C
ANISOU 3147 CG ASP B 143 10755 8469 9925 -855 2941 323 C
ATOM 3148 OD1 ASP B 143 43.488 -10.406 201.929 1.00 84.45 O
ANISOU 3148 OD1 ASP B 143 11521 9353 11212 -1022 3176 221 O
ATOM 3149 OD2 ASP B 143 42.150 -11.403 200.497 1.00 76.73 O
ANISOU 3149 OD2 ASP B 143 11080 8467 9608 -806 3039 473 O
ATOM 3150 N ARG B 144 38.985 -9.946 201.641 1.00 70.89 N
ANISOU 3150 N ARG B 144 10592 7578 8765 -539 2281 740 N
ATOM 3151 CA ARG B 144 38.284 -9.207 200.594 1.00 71.44 C
ANISOU 3151 CA ARG B 144 11058 7476 8610 -493 2308 1004 C
ATOM 3152 C ARG B 144 37.719 -7.897 201.126 1.00 70.27 C
ANISOU 3152 C ARG B 144 10928 7119 8652 -480 2236 1083 C
ATOM 3153 O ARG B 144 37.712 -6.882 200.419 1.00 72.58 O
ANISOU 3153 O ARG B 144 11491 7177 8908 -520 2402 1277 O
ATOM 3154 CB ARG B 144 37.163 -10.063 200.005 1.00 65.82 C
ANISOU 3154 CB ARG B 144 10549 6897 7563 -317 2022 1106 C
ATOM 3155 CG ARG B 144 37.629 -11.358 199.359 1.00 59.82 C
ANISOU 3155 CG ARG B 144 9832 6312 6585 -319 2091 1029 C
ATOM 3156 CD ARG B 144 38.411 -11.072 198.088 1.00 64.38 C
ANISOU 3156 CD ARG B 144 10713 6781 6968 -418 2456 1148 C
ATOM 3157 NE ARG B 144 39.785 -10.659 198.362 1.00 63.82 N
ANISOU 3157 NE ARG B 144 10432 6636 7181 -600 2833 1035 N
ATOM 3158 CZ ARG B 144 40.499 -9.874 197.563 1.00 69.96 C
ANISOU 3158 CZ ARG B 144 11414 7233 7934 -734 3214 1156 C
ATOM 3159 NH1 ARG B 144 39.959 -9.401 196.448 1.00 70.78 N
ANISOU 3159 NH1 ARG B 144 11979 7210 7702 -690 3258 1413 N
ATOM 3160 NH2 ARG B 144 41.743 -9.543 197.884 1.00 64.73 N
ANISOU 3160 NH2 ARG B 144 10495 6508 7589 -913 3546 1025 N
ATOM 3161 N TRP B 145 37.272 -7.891 202.382 1.00 69.44 N
ANISOU 3161 N TRP B 145 10555 7080 8750 -425 2011 933 N
ATOM 3162 CA TRP B 145 36.621 -6.710 202.931 1.00 62.92 C
ANISOU 3162 CA TRP B 145 9747 6057 8101 -385 1930 983 C
ATOM 3163 C TRP B 145 37.625 -5.588 203.147 1.00 56.94 C
ANISOU 3163 C TRP B 145 8940 5071 7623 -578 2223 928 C
ATOM 3164 O TRP B 145 37.374 -4.436 202.777 1.00 65.19 O
ANISOU 3164 O TRP B 145 10197 5844 8727 -589 2320 1090 O
ATOM 3165 CB TRP B 145 35.915 -7.084 204.236 1.00 62.66 C
ANISOU 3165 CB TRP B 145 9451 6170 8187 -281 1651 813 C
ATOM 3166 CG TRP B 145 35.041 -6.016 204.817 1.00 55.73 C
ANISOU 3166 CG TRP B 145 8592 5114 7469 -196 1545 848 C
ATOM 3167 CD1 TRP B 145 33.801 -5.643 204.383 1.00 63.44 C
ANISOU 3167 CD1 TRP B 145 9752 5998 8354 -23 1374 1040 C
ATOM 3168 CD2 TRP B 145 35.328 -5.199 205.960 1.00 54.55 C
ANISOU 3168 CD2 TRP B 145 8261 4854 7610 -268 1593 667 C
ATOM 3169 NE1 TRP B 145 33.306 -4.631 205.175 1.00 65.34 N
ANISOU 3169 NE1 TRP B 145 9932 6065 8830 26 1341 995 N
ATOM 3170 CE2 TRP B 145 34.223 -4.344 206.153 1.00 58.04 C
ANISOU 3170 CE2 TRP B 145 8801 5126 8128 -128 1479 760 C
ATOM 3171 CE3 TRP B 145 36.415 -5.101 206.834 1.00 63.81 C
ANISOU 3171 CE3 TRP B 145 9197 6054 8993 -433 1705 423 C
ATOM 3172 CZ2 TRP B 145 34.173 -3.403 207.185 1.00 55.96 C
ANISOU 3172 CZ2 TRP B 145 8428 4707 8126 -152 1504 607 C
ATOM 3173 CZ3 TRP B 145 36.365 -4.164 207.858 1.00 65.13 C
ANISOU 3173 CZ3 TRP B 145 9264 6080 9404 -468 1699 268 C
ATOM 3174 CH2 TRP B 145 35.253 -3.328 208.023 1.00 56.38 C
ANISOU 3174 CH2 TRP B 145 8280 4792 8350 -330 1614 357 C
ATOM 3175 N TYR B 146 38.777 -5.905 203.739 1.00 57.53 N
ANISOU 3175 N TYR B 146 8728 5239 7894 -732 2358 700 N
ATOM 3176 CA TYR B 146 39.816 -4.888 203.856 1.00 61.35 C
ANISOU 3176 CA TYR B 146 9137 5504 8670 -948 2648 630 C
ATOM 3177 C TYR B 146 40.395 -4.503 202.500 1.00 75.39 C
ANISOU 3177 C TYR B 146 11191 7108 10345 -1063 3002 838 C
ATOM 3178 O TYR B 146 40.818 -3.357 202.319 1.00 82.38 O
ANISOU 3178 O TYR B 146 12166 7711 11425 -1210 3245 900 O
ATOM 3179 CB TYR B 146 40.920 -5.357 204.804 1.00 58.33 C
ANISOU 3179 CB TYR B 146 8349 5277 8536 -1079 2670 324 C
ATOM 3180 CG TYR B 146 40.573 -5.124 206.256 1.00 66.69 C
ANISOU 3180 CG TYR B 146 9183 6381 9774 -1038 2414 113 C
ATOM 3181 CD1 TYR B 146 40.547 -3.840 206.779 1.00 61.83 C
ANISOU 3181 CD1 TYR B 146 8573 5515 9404 -1126 2464 56 C
ATOM 3182 CD2 TYR B 146 40.257 -6.183 207.099 1.00 59.23 C
ANISOU 3182 CD2 TYR B 146 8053 5714 8739 -911 2138 -27 C
ATOM 3183 CE1 TYR B 146 40.220 -3.611 208.103 1.00 62.10 C
ANISOU 3183 CE1 TYR B 146 8438 5588 9569 -1086 2246 -155 C
ATOM 3184 CE2 TYR B 146 39.929 -5.960 208.426 1.00 62.11 C
ANISOU 3184 CE2 TYR B 146 8258 6120 9223 -872 1928 -213 C
ATOM 3185 CZ TYR B 146 39.914 -4.674 208.920 1.00 60.12 C
ANISOU 3185 CZ TYR B 146 8020 5632 9193 -958 1983 -285 C
ATOM 3186 OH TYR B 146 39.590 -4.448 210.236 1.00 62.23 O
ANISOU 3186 OH TYR B 146 8158 5940 9547 -918 1790 -490 O
ATOM 3187 N ALA B 147 40.428 -5.426 201.533 1.00 73.56 N
ANISOU 3187 N ALA B 147 11119 7025 9806 -1006 3055 945 N
ATOM 3188 CA ALA B 147 41.004 -5.081 200.237 1.00 69.28 C
ANISOU 3188 CA ALA B 147 10875 6324 9123 -1118 3427 1140 C
ATOM 3189 C ALA B 147 40.093 -4.176 199.418 1.00 75.05 C
ANISOU 3189 C ALA B 147 12059 6813 9644 -1025 3409 1462 C
ATOM 3190 O ALA B 147 40.585 -3.332 198.661 1.00 78.19 O
ANISOU 3190 O ALA B 147 12698 6961 10048 -1154 3741 1631 O
ATOM 3191 CB ALA B 147 41.321 -6.352 199.449 1.00 70.60 C
ANISOU 3191 CB ALA B 147 11105 6720 9001 -1078 3499 1134 C
ATOM 3192 N ILE B 148 38.779 -4.321 199.554 1.00 77.21 N
ANISOU 3192 N ILE B 148 12443 7146 9747 -799 3027 1554 N
ATOM 3193 CA ILE B 148 37.833 -3.637 198.680 1.00 74.90 C
ANISOU 3193 CA ILE B 148 12582 6660 9216 -661 2942 1872 C
ATOM 3194 C ILE B 148 37.174 -2.450 199.371 1.00 78.65 C
ANISOU 3194 C ILE B 148 13038 6890 9957 -601 2815 1915 C
ATOM 3195 O ILE B 148 36.963 -1.408 198.750 1.00 84.75 O
ANISOU 3195 O ILE B 148 14114 7382 10704 -586 2913 2150 O
ATOM 3196 CB ILE B 148 36.776 -4.639 198.168 1.00 75.63 C
ANISOU 3196 CB ILE B 148 12824 6981 8930 -439 2592 1957 C
ATOM 3197 CG1 ILE B 148 37.459 -5.821 197.480 1.00 74.43 C
ANISOU 3197 CG1 ILE B 148 12710 7050 8520 -500 2738 1889 C
ATOM 3198 CG2 ILE B 148 35.807 -3.964 197.213 1.00 82.26 C
ANISOU 3198 CG2 ILE B 148 14110 7636 9509 -279 2456 2289 C
ATOM 3199 CD1 ILE B 148 36.496 -6.884 197.013 1.00 67.70 C
ANISOU 3199 CD1 ILE B 148 11986 6421 7318 -311 2393 1926 C
ATOM 3200 N CYS B 149 36.791 -2.629 200.628 1.00 77.31 N
ANISOU 3200 N CYS B 149 12515 6830 10030 -551 2587 1681 N
ATOM 3201 CA CYS B 149 36.067 -1.551 201.339 1.00 74.62 C
ANISOU 3201 CA CYS B 149 12151 6271 9931 -465 2455 1690 C
ATOM 3202 C CYS B 149 37.004 -0.651 202.145 1.00 82.60 C
ANISOU 3202 C CYS B 149 12960 7080 11343 -674 2685 1498 C
ATOM 3203 O CYS B 149 36.684 0.527 202.278 1.00 86.18 O
ANISOU 3203 O CYS B 149 13525 7227 11992 -654 2715 1570 O
ATOM 3204 CB CYS B 149 34.980 -2.144 202.222 1.00 77.39 C
ANISOU 3204 CB CYS B 149 12278 6844 10285 -265 2071 1558 C
ATOM 3205 SG CYS B 149 33.738 -3.055 201.277 1.00 72.35 S
ANISOU 3205 SG CYS B 149 11845 6400 9245 -14 1739 1770 S
ATOM 3206 N HIS B 150 38.053 -1.205 202.753 1.00 83.05 N
ANISOU 3206 N HIS B 150 12718 7289 11549 -867 2829 1242 N
ATOM 3207 CA HIS B 150 39.003 -0.417 203.587 1.00 77.41 C
ANISOU 3207 CA HIS B 150 11780 6402 11230 -1086 3014 1022 C
ATOM 3208 C HIS B 150 40.419 -0.762 203.135 1.00 77.24 C
ANISOU 3208 C HIS B 150 11647 6408 11292 -1337 3353 949 C
ATOM 3209 O HIS B 150 41.140 -1.417 203.886 1.00 80.09 O
ANISOU 3209 O HIS B 150 11649 6976 11806 -1443 3339 673 O
ATOM 3210 CB HIS B 150 38.757 -0.664 205.080 1.00 72.00 C
ANISOU 3210 CB HIS B 150 10751 5895 10710 -1033 2745 711 C
ATOM 3211 CG HIS B 150 37.348 -0.401 205.487 1.00 67.24 C
ANISOU 3211 CG HIS B 150 10241 5270 10037 -784 2460 780 C
ATOM 3212 ND1 HIS B 150 36.910 0.837 205.864 1.00 72.48 N
ANISOU 3212 ND1 HIS B 150 11048 5605 10888 -740 2481 845 N
ATOM 3213 CD2 HIS B 150 36.260 -1.193 205.472 1.00 68.10 C
ANISOU 3213 CD2 HIS B 150 10313 5627 9934 -565 2167 800 C
ATOM 3214 CE1 HIS B 150 35.623 0.786 206.113 1.00 70.05 C
ANISOU 3214 CE1 HIS B 150 10764 5357 10494 -492 2214 891 C
ATOM 3215 NE2 HIS B 150 35.202 -0.443 205.875 1.00 63.34 N
ANISOU 3215 NE2 HIS B 150 9801 4858 9406 -393 2023 866 N
ATOM 3216 N PRO B 151 40.859 -0.236 201.978 1.00 80.74 N
ANISOU 3216 N PRO B 151 12399 6632 11645 -1433 3675 1200 N
ATOM 3217 CA PRO B 151 42.113 -0.635 201.333 1.00 91.39 C
ANISOU 3217 CA PRO B 151 13682 8113 12929 -1587 3966 1173 C
ATOM 3218 C PRO B 151 43.520 -0.511 201.933 1.00101.54 C
ANISOU 3218 C PRO B 151 14534 9438 14608 -1834 4148 858 C
ATOM 3219 O PRO B 151 44.302 -1.389 201.656 1.00119.83 O
ANISOU 3219 O PRO B 151 16656 11972 16903 -1900 4264 745 O
ATOM 3220 CB PRO B 151 42.101 0.168 200.028 1.00 85.17 C
ANISOU 3220 CB PRO B 151 13257 7151 11953 -1572 4144 1439 C
ATOM 3221 CG PRO B 151 40.650 0.464 199.801 1.00 88.48 C
ANISOU 3221 CG PRO B 151 13992 7450 12176 -1338 3867 1676 C
ATOM 3222 CD PRO B 151 40.133 0.743 201.189 1.00 83.93 C
ANISOU 3222 CD PRO B 151 13188 6805 11895 -1305 3653 1495 C
ATOM 3223 N LEU B 152 43.853 0.547 202.665 1.00 83.69 N
ANISOU 3223 N LEU B 152 12102 6987 12709 -1963 4158 697 N
ATOM 3224 CA LEU B 152 45.281 0.622 203.071 1.00 96.52 C
ANISOU 3224 CA LEU B 152 13363 8624 14688 -2202 4353 437 C
ATOM 3225 C LEU B 152 45.533 0.328 204.551 1.00 99.55 C
ANISOU 3225 C LEU B 152 13317 9106 15400 -2290 4145 76 C
ATOM 3226 O LEU B 152 46.664 0.559 204.982 1.00106.76 O
ANISOU 3226 O LEU B 152 13918 10000 16647 -2477 4231 -164 O
ATOM 3227 CB LEU B 152 45.838 1.978 202.640 1.00107.43 C
ANISOU 3227 CB LEU B 152 14872 9713 16235 -2325 4573 515 C
ATOM 3228 CG LEU B 152 45.771 2.226 201.133 1.00109.26 C
ANISOU 3228 CG LEU B 152 15461 9870 16183 -2298 4841 818 C
ATOM 3229 CD1 LEU B 152 46.129 3.661 200.793 1.00113.02 C
ANISOU 3229 CD1 LEU B 152 16030 10047 16867 -2449 5083 876 C
ATOM 3230 CD2 LEU B 152 46.665 1.255 200.381 1.00103.72 C
ANISOU 3230 CD2 LEU B 152 14629 9408 15373 -2345 5034 765 C
ATOM 3231 N LEU B 153 44.533 -0.125 205.304 1.00 95.20 N
ANISOU 3231 N LEU B 153 12737 8709 14725 -2121 3815 13 N
ATOM 3232 CA LEU B 153 44.772 -0.416 206.743 1.00 86.70 C
ANISOU 3232 CA LEU B 153 11276 7800 13864 -2143 3536 -345 C
ATOM 3233 C LEU B 153 45.688 -1.626 206.968 1.00 91.05 C
ANISOU 3233 C LEU B 153 11462 8671 14462 -2185 3503 -541 C
ATOM 3234 O LEU B 153 46.644 -1.481 207.740 1.00 88.51 O
ANISOU 3234 O LEU B 153 10778 8366 14486 -2370 3511 -823 O
ATOM 3235 CB LEU B 153 43.426 -0.645 207.430 1.00 79.96 C
ANISOU 3235 CB LEU B 153 10518 7074 12788 -1878 3146 -351 C
ATOM 3236 CG LEU B 153 42.295 0.264 206.970 1.00 78.68 C
ANISOU 3236 CG LEU B 153 10725 6621 12550 -1766 3152 -121 C
ATOM 3237 CD1 LEU B 153 41.185 0.286 208.002 1.00 76.56 C
ANISOU 3237 CD1 LEU B 153 10452 6466 12172 -1541 2796 -211 C
ATOM 3238 CD2 LEU B 153 42.810 1.668 206.724 1.00 76.85 C
ANISOU 3238 CD2 LEU B 153 10553 5977 12669 -1996 3419 -145 C
ATOM 3239 N PHE B 154 45.456 -2.745 206.271 1.00 88.01 N
ANISOU 3239 N PHE B 154 11160 8527 13753 -2016 3461 -404 N
ATOM 3240 CA PHE B 154 46.214 -3.960 206.544 1.00 90.88 C
ANISOU 3240 CA PHE B 154 11194 9199 14137 -1993 3378 -583 C
ATOM 3241 C PHE B 154 46.720 -4.567 205.246 1.00 97.27 C
ANISOU 3241 C PHE B 154 12101 10047 14812 -2019 3704 -419 C
ATOM 3242 O PHE B 154 45.938 -4.791 204.315 1.00 94.59 O
ANISOU 3242 O PHE B 154 12133 9690 14116 -1887 3758 -154 O
ATOM 3243 CB PHE B 154 45.362 -4.988 207.297 1.00 79.67 C
ANISOU 3243 CB PHE B 154 9751 8068 12452 -1735 2959 -631 C
ATOM 3244 CG PHE B 154 44.914 -4.523 208.650 1.00 77.75 C
ANISOU 3244 CG PHE B 154 9408 7827 12308 -1700 2653 -818 C
ATOM 3245 CD1 PHE B 154 45.755 -4.629 209.745 1.00 72.94 C
ANISOU 3245 CD1 PHE B 154 8432 7331 11952 -1790 2494 -1130 C
ATOM 3246 CD2 PHE B 154 43.651 -3.982 208.828 1.00 77.51 C
ANISOU 3246 CD2 PHE B 154 9651 7685 12115 -1568 2521 -693 C
ATOM 3247 CE1 PHE B 154 45.349 -4.198 210.993 1.00 78.16 C
ANISOU 3247 CE1 PHE B 154 9044 7997 12658 -1758 2219 -1315 C
ATOM 3248 CE2 PHE B 154 43.235 -3.552 210.073 1.00 79.64 C
ANISOU 3248 CE2 PHE B 154 9845 7951 12462 -1532 2279 -881 C
ATOM 3249 CZ PHE B 154 44.085 -3.659 211.158 1.00 77.16 C
ANISOU 3249 CZ PHE B 154 9206 7753 12357 -1631 2133 -1194 C
ATOM 3250 N LYS B 155 48.023 -4.839 205.191 1.00 93.98 N
ANISOU 3250 N LYS B 155 11344 9683 14681 -2183 3916 -592 N
ATOM 3251 CA LYS B 155 48.612 -5.513 204.043 1.00 96.45 C
ANISOU 3251 CA LYS B 155 11703 10053 14889 -2204 4254 -487 C
ATOM 3252 C LYS B 155 48.317 -7.007 204.092 1.00 94.69 C
ANISOU 3252 C LYS B 155 11439 10149 14391 -1963 4011 -513 C
ATOM 3253 O LYS B 155 48.473 -7.648 205.137 1.00100.38 O
ANISOU 3253 O LYS B 155 11847 11072 15219 -1875 3687 -727 O
ATOM 3254 CB LYS B 155 50.121 -5.274 204.002 1.00101.08 C
ANISOU 3254 CB LYS B 155 11925 10617 15864 -2383 4480 -687 C
ATOM 3255 CG LYS B 155 50.506 -3.845 203.662 1.00112.03 C
ANISOU 3255 CG LYS B 155 13428 11715 17422 -2547 4695 -635 C
ATOM 3256 CD LYS B 155 52.008 -3.700 203.455 1.00121.24 C
ANISOU 3256 CD LYS B 155 14264 12875 18925 -2689 4919 -812 C
ATOM 3257 CE LYS B 155 52.362 -2.293 203.000 1.00120.06 C
ANISOU 3257 CE LYS B 155 14262 12428 18925 -2858 5178 -733 C
ATOM 3258 NZ LYS B 155 53.821 -2.121 202.765 1.00126.77 N
ANISOU 3258 NZ LYS B 155 14790 13253 20122 -3011 5424 -900 N
ATOM 3259 N SER B 156 47.919 -7.566 202.952 1.00 95.79 N
ANISOU 3259 N SER B 156 11910 10318 14169 -1860 4172 -299 N
ATOM 3260 CA SER B 156 47.618 -8.986 202.825 1.00 87.98 C
ANISOU 3260 CA SER B 156 10932 9589 12909 -1646 3987 -312 C
ATOM 3261 C SER B 156 48.568 -9.591 201.804 1.00 91.19 C
ANISOU 3261 C SER B 156 11304 10028 13317 -1706 4392 -318 C
ATOM 3262 O SER B 156 48.529 -9.228 200.624 1.00102.25 O
ANISOU 3262 O SER B 156 13048 11284 14518 -1772 4741 -119 O
ATOM 3263 CB SER B 156 46.165 -9.212 202.405 1.00 96.64 C
ANISOU 3263 CB SER B 156 12467 10706 13547 -1450 3764 -81 C
ATOM 3264 OG SER B 156 45.957 -8.824 201.058 1.00103.11 O
ANISOU 3264 OG SER B 156 13701 11370 14106 -1488 4071 166 O
ATOM 3265 N THR B 157 49.418 -10.506 202.256 1.00 91.23 N
ANISOU 3265 N THR B 157 10908 10215 13541 -1671 4350 -544 N
ATOM 3266 CA THR B 157 50.349 -11.209 201.391 1.00 91.71 C
ANISOU 3266 CA THR B 157 10884 10325 13635 -1687 4703 -594 C
ATOM 3267 C THR B 157 50.143 -12.710 201.545 1.00 95.88 C
ANISOU 3267 C THR B 157 11347 11090 13994 -1457 4478 -674 C
ATOM 3268 O THR B 157 49.624 -13.184 202.558 1.00 98.05 O
ANISOU 3268 O THR B 157 11503 11499 14252 -1312 4029 -748 O
ATOM 3269 CB THR B 157 51.802 -10.847 201.721 1.00 92.52 C
ANISOU 3269 CB THR B 157 10542 10393 14219 -1823 4808 -812 C
ATOM 3270 OG1 THR B 157 52.106 -11.273 203.056 1.00 90.37 O
ANISOU 3270 OG1 THR B 157 9802 10277 14255 -1783 4481 -1051 O
ATOM 3271 CG2 THR B 157 52.019 -9.340 201.612 1.00 94.39 C
ANISOU 3271 CG2 THR B 157 10861 10381 14621 -2027 4964 -751 C
ATOM 3272 N ALA B 158 50.545 -13.465 200.523 1.00101.91 N
ANISOU 3272 N ALA B 158 12229 11889 14605 -1405 4753 -657 N
ATOM 3273 CA ALA B 158 50.453 -14.916 200.632 1.00 95.77 C
ANISOU 3273 CA ALA B 158 11373 11302 13712 -1197 4593 -754 C
ATOM 3274 C ALA B 158 51.299 -15.437 201.786 1.00105.26 C
ANISOU 3274 C ALA B 158 12014 12634 15345 -1147 4376 -1008 C
ATOM 3275 O ALA B 158 50.913 -16.407 202.457 1.00108.69 O
ANISOU 3275 O ALA B 158 12376 13215 15704 -950 4001 -1067 O
ATOM 3276 CB ALA B 158 50.878 -15.566 199.316 1.00 83.03 C
ANISOU 3276 CB ALA B 158 9985 9677 11884 -1149 4891 -721 C
ATOM 3277 N ARG B 159 52.441 -14.795 202.044 1.00116.27 N
ANISOU 3277 N ARG B 159 13056 13963 17158 -1298 4500 -1140 N
ATOM 3278 CA ARG B 159 53.306 -15.232 203.132 1.00116.89 C
ANISOU 3278 CA ARG B 159 12603 14163 17647 -1246 4252 -1380 C
ATOM 3279 C ARG B 159 52.609 -15.098 204.480 1.00117.60 C
ANISOU 3279 C ARG B 159 12575 14342 17765 -1193 3797 -1430 C
ATOM 3280 O ARG B 159 52.751 -15.966 205.349 1.00127.58 O
ANISOU 3280 O ARG B 159 13599 15761 19112 -1021 3447 -1554 O
ATOM 3281 CB ARG B 159 54.602 -14.424 203.106 1.00127.15 C
ANISOU 3281 CB ARG B 159 13608 15352 19350 -1428 4419 -1498 C
ATOM 3282 CG ARG B 159 55.602 -14.793 204.183 1.00134.04 C
ANISOU 3282 CG ARG B 159 13938 16341 20651 -1379 4138 -1746 C
ATOM 3283 CD ARG B 159 56.784 -13.838 204.162 1.00145.67 C
ANISOU 3283 CD ARG B 159 15146 17685 22515 -1583 4303 -1861 C
ATOM 3284 NE ARG B 159 56.383 -12.467 204.468 1.00149.42 N
ANISOU 3284 NE ARG B 159 15733 18013 23026 -1783 4298 -1817 N
ATOM 3285 CZ ARG B 159 56.400 -11.942 205.689 1.00149.97 C
ANISOU 3285 CZ ARG B 159 15557 18110 23313 -1838 3956 -1962 C
ATOM 3286 NH1 ARG B 159 56.018 -10.686 205.881 1.00146.49 N
ANISOU 3286 NH1 ARG B 159 15255 17508 22897 -2018 3983 -1922 N
ATOM 3287 NH2 ARG B 159 56.801 -12.675 206.719 1.00152.11 N
ANISOU 3287 NH2 ARG B 159 15468 18564 23763 -1700 3570 -2147 N
ATOM 3288 N ARG B 160 51.846 -14.021 204.673 1.00105.12 N
ANISOU 3288 N ARG B 160 11238 12648 16057 -1303 3715 -1312 N
ATOM 3289 CA ARG B 160 51.040 -13.880 205.879 1.00102.30 C
ANISOU 3289 CA ARG B 160 10905 12358 15607 -1216 3227 -1326 C
ATOM 3290 C ARG B 160 49.794 -14.757 205.854 1.00 99.79 C
ANISOU 3290 C ARG B 160 10935 12138 14844 -993 2968 -1174 C
ATOM 3291 O ARG B 160 49.290 -15.135 206.921 1.00100.13 O
ANISOU 3291 O ARG B 160 10927 12293 14823 -864 2563 -1219 O
ATOM 3292 CB ARG B 160 50.655 -12.413 206.077 1.00103.88 C
ANISOU 3292 CB ARG B 160 11238 12378 15853 -1402 3258 -1268 C
ATOM 3293 CG ARG B 160 51.848 -11.476 206.139 1.00118.80 C
ANISOU 3293 CG ARG B 160 12782 14141 18215 -1658 3513 -1428 C
ATOM 3294 CD ARG B 160 51.415 -10.023 206.197 1.00127.76 C
ANISOU 3294 CD ARG B 160 14110 15050 19383 -1845 3588 -1350 C
ATOM 3295 NE ARG B 160 50.523 -9.766 207.324 1.00132.86 N
ANISOU 3295 NE ARG B 160 14839 15738 19902 -1751 3144 -1380 N
ATOM 3296 CZ ARG B 160 50.933 -9.397 208.533 1.00136.98 C
ANISOU 3296 CZ ARG B 160 15054 16298 20694 -1811 2868 -1613 C
ATOM 3297 NH1 ARG B 160 52.228 -9.240 208.777 1.00141.67 N
ANISOU 3297 NH1 ARG B 160 15203 16895 21731 -1968 2955 -1841 N
ATOM 3298 NH2 ARG B 160 50.048 -9.184 209.499 1.00134.89 N
ANISOU 3298 NH2 ARG B 160 14924 16071 20259 -1715 2506 -1630 N
ATOM 3299 N ALA B 161 49.295 -15.100 204.663 1.00 97.33 N
ANISOU 3299 N ALA B 161 10979 11783 14219 -951 3193 -1004 N
ATOM 3300 CA ALA B 161 48.197 -16.056 204.580 1.00 94.46 C
ANISOU 3300 CA ALA B 161 10900 11513 13477 -750 2950 -892 C
ATOM 3301 C ALA B 161 48.623 -17.433 205.071 1.00 93.94 C
ANISOU 3301 C ALA B 161 10598 11606 13491 -574 2769 -1027 C
ATOM 3302 O ALA B 161 47.815 -18.153 205.666 1.00 92.24 O
ANISOU 3302 O ALA B 161 10475 11481 13092 -418 2436 -992 O
ATOM 3303 CB ALA B 161 47.675 -16.144 203.146 1.00 90.88 C
ANISOU 3303 CB ALA B 161 10871 10981 12678 -751 3218 -710 C
ATOM 3304 N LEU B 162 49.889 -17.809 204.860 1.00 90.86 N
ANISOU 3304 N LEU B 162 9889 11237 13398 -593 2990 -1180 N
ATOM 3305 CA LEU B 162 50.362 -19.075 205.416 1.00 90.98 C
ANISOU 3305 CA LEU B 162 9648 11382 13538 -405 2792 -1311 C
ATOM 3306 C LEU B 162 50.289 -19.066 206.938 1.00 86.36 C
ANISOU 3306 C LEU B 162 8834 10894 13084 -337 2341 -1394 C
ATOM 3307 O LEU B 162 49.875 -20.056 207.560 1.00 86.80 O
ANISOU 3307 O LEU B 162 8916 11044 13019 -148 2035 -1386 O
ATOM 3308 CB LEU B 162 51.793 -19.356 204.960 1.00101.04 C
ANISOU 3308 CB LEU B 162 10565 12651 15174 -435 3117 -1476 C
ATOM 3309 CG LEU B 162 52.523 -20.459 205.740 1.00108.55 C
ANISOU 3309 CG LEU B 162 11139 13720 16384 -241 2880 -1640 C
ATOM 3310 CD1 LEU B 162 51.988 -21.841 205.380 1.00105.55 C
ANISOU 3310 CD1 LEU B 162 10994 13375 15736 -20 2808 -1582 C
ATOM 3311 CD2 LEU B 162 54.032 -20.391 205.527 1.00112.16 C
ANISOU 3311 CD2 LEU B 162 11121 14169 17325 -304 3165 -1835 C
ATOM 3312 N GLY B 163 50.650 -17.940 207.556 1.00 78.29 N
ANISOU 3312 N GLY B 163 7620 9838 12289 -495 2296 -1473 N
ATOM 3313 CA GLY B 163 50.572 -17.864 209.002 1.00 77.72 C
ANISOU 3313 CA GLY B 163 7373 9859 12296 -437 1867 -1566 C
ATOM 3314 C GLY B 163 49.140 -17.858 209.494 1.00 82.30 C
ANISOU 3314 C GLY B 163 8308 10458 12503 -359 1602 -1417 C
ATOM 3315 O GLY B 163 48.820 -18.485 210.507 1.00 85.26 O
ANISOU 3315 O GLY B 163 8660 10942 12792 -211 1253 -1437 O
ATOM 3316 N SER B 164 48.248 -17.195 208.755 1.00 75.49 N
ANISOU 3316 N SER B 164 7786 9485 11412 -446 1773 -1255 N
ATOM 3317 CA SER B 164 46.841 -17.235 209.133 1.00 70.56 C
ANISOU 3317 CA SER B 164 7471 8875 10464 -362 1545 -1115 C
ATOM 3318 C SER B 164 46.280 -18.648 209.035 1.00 68.74 C
ANISOU 3318 C SER B 164 7376 8734 10007 -168 1409 -1039 C
ATOM 3319 O SER B 164 45.476 -19.056 209.879 1.00 67.53 O
ANISOU 3319 O SER B 164 7310 8649 9699 -60 1126 -998 O
ATOM 3320 CB SER B 164 46.028 -16.277 208.260 1.00 71.75 C
ANISOU 3320 CB SER B 164 7941 8881 10441 -471 1745 -950 C
ATOM 3321 OG SER B 164 46.447 -14.938 208.449 1.00 74.51 O
ANISOU 3321 OG SER B 164 8193 9114 11005 -651 1856 -1011 O
ATOM 3322 N ILE B 165 46.717 -19.422 208.041 1.00 69.54 N
ANISOU 3322 N ILE B 165 7497 8826 10099 -125 1624 -1032 N
ATOM 3323 CA ILE B 165 46.226 -20.789 207.894 1.00 69.02 C
ANISOU 3323 CA ILE B 165 7567 8815 9844 48 1510 -980 C
ATOM 3324 C ILE B 165 46.743 -21.675 209.023 1.00 78.47 C
ANISOU 3324 C ILE B 165 8510 10114 11191 197 1238 -1084 C
ATOM 3325 O ILE B 165 45.994 -22.480 209.603 1.00 72.66 O
ANISOU 3325 O ILE B 165 7898 9424 10286 326 995 -1017 O
ATOM 3326 CB ILE B 165 46.624 -21.334 206.512 1.00 65.00 C
ANISOU 3326 CB ILE B 165 7160 8252 9284 51 1834 -974 C
ATOM 3327 CG1 ILE B 165 45.875 -20.563 205.421 1.00 61.82 C
ANISOU 3327 CG1 ILE B 165 7104 7753 8632 -65 2037 -828 C
ATOM 3328 CG2 ILE B 165 46.364 -22.838 206.423 1.00 59.56 C
ANISOU 3328 CG2 ILE B 165 6553 7602 8477 231 1722 -974 C
ATOM 3329 CD1 ILE B 165 46.428 -20.761 204.026 1.00 63.76 C
ANISOU 3329 CD1 ILE B 165 7471 7936 8818 -107 2421 -833 C
ATOM 3330 N LEU B 166 48.026 -21.533 209.367 1.00 82.06 N
ANISOU 3330 N LEU B 166 8604 10600 11973 180 1267 -1243 N
ATOM 3331 CA LEU B 166 48.560 -22.291 210.492 1.00 76.08 C
ANISOU 3331 CA LEU B 166 7605 9943 11361 337 961 -1335 C
ATOM 3332 C LEU B 166 47.825 -21.946 211.778 1.00 69.71 C
ANISOU 3332 C LEU B 166 6880 9198 10409 355 619 -1299 C
ATOM 3333 O LEU B 166 47.490 -22.836 212.573 1.00 69.18 O
ANISOU 3333 O LEU B 166 6868 9192 10226 517 353 -1256 O
ATOM 3334 CB LEU B 166 50.054 -22.015 210.643 1.00 81.58 C
ANISOU 3334 CB LEU B 166 7862 10664 12470 299 1026 -1528 C
ATOM 3335 CG LEU B 166 50.987 -22.868 209.790 1.00 90.11 C
ANISOU 3335 CG LEU B 166 8762 11721 13756 385 1273 -1603 C
ATOM 3336 CD1 LEU B 166 52.403 -22.321 209.842 1.00 95.94 C
ANISOU 3336 CD1 LEU B 166 9036 12471 14946 295 1395 -1797 C
ATOM 3337 CD2 LEU B 166 50.947 -24.301 210.284 1.00 88.23 C
ANISOU 3337 CD2 LEU B 166 8522 11529 13473 642 1023 -1584 C
ATOM 3338 N GLY B 167 47.515 -20.661 211.975 1.00 63.67 N
ANISOU 3338 N GLY B 167 6160 8400 9633 191 645 -1308 N
ATOM 3339 CA GLY B 167 46.785 -20.270 213.167 1.00 60.16 C
ANISOU 3339 CA GLY B 167 5816 8007 9037 205 362 -1292 C
ATOM 3340 C GLY B 167 45.362 -20.781 213.168 1.00 64.75 C
ANISOU 3340 C GLY B 167 6737 8580 9285 285 297 -1112 C
ATOM 3341 O GLY B 167 44.817 -21.104 214.227 1.00 68.24 O
ANISOU 3341 O GLY B 167 7258 9090 9582 376 49 -1083 O
ATOM 3342 N ILE B 168 44.744 -20.877 211.989 1.00 57.62 N
ANISOU 3342 N ILE B 168 6041 7596 8254 251 519 -993 N
ATOM 3343 CA ILE B 168 43.405 -21.444 211.915 1.00 56.56 C
ANISOU 3343 CA ILE B 168 6190 7454 7846 320 446 -838 C
ATOM 3344 C ILE B 168 43.429 -22.894 212.363 1.00 61.59 C
ANISOU 3344 C ILE B 168 6823 8146 8434 490 283 -817 C
ATOM 3345 O ILE B 168 42.568 -23.337 213.134 1.00 57.85 O
ANISOU 3345 O ILE B 168 6480 7701 7797 560 105 -737 O
ATOM 3346 CB ILE B 168 42.842 -21.307 210.489 1.00 61.17 C
ANISOU 3346 CB ILE B 168 6987 7946 8308 255 680 -734 C
ATOM 3347 CG1 ILE B 168 42.445 -19.858 210.210 1.00 60.39 C
ANISOU 3347 CG1 ILE B 168 6975 7770 8200 114 790 -696 C
ATOM 3348 CG2 ILE B 168 41.654 -22.246 210.284 1.00 60.07 C
ANISOU 3348 CG2 ILE B 168 7081 7804 7938 342 587 -608 C
ATOM 3349 CD1 ILE B 168 41.972 -19.627 208.804 1.00 52.40 C
ANISOU 3349 CD1 ILE B 168 6194 6666 7051 58 1000 -581 C
ATOM 3350 N TRP B 169 44.429 -23.652 211.911 1.00 59.33 N
ANISOU 3350 N TRP B 169 6385 7857 8302 560 359 -888 N
ATOM 3351 CA TRP B 169 44.511 -25.041 212.348 1.00 55.49 C
ANISOU 3351 CA TRP B 169 5897 7390 7796 737 201 -863 C
ATOM 3352 C TRP B 169 44.794 -25.137 213.841 1.00 61.80 C
ANISOU 3352 C TRP B 169 6579 8278 8624 830 -98 -895 C
ATOM 3353 O TRP B 169 44.232 -25.993 214.528 1.00 60.36 O
ANISOU 3353 O TRP B 169 6533 8105 8298 947 -272 -800 O
ATOM 3354 CB TRP B 169 45.573 -25.788 211.551 1.00 56.08 C
ANISOU 3354 CB TRP B 169 5817 7430 8063 812 359 -950 C
ATOM 3355 CG TRP B 169 45.064 -26.213 210.235 1.00 58.91 C
ANISOU 3355 CG TRP B 169 6395 7701 8287 782 589 -896 C
ATOM 3356 CD1 TRP B 169 45.215 -25.560 209.052 1.00 56.06 C
ANISOU 3356 CD1 TRP B 169 6089 7293 7919 655 877 -917 C
ATOM 3357 CD2 TRP B 169 44.278 -27.377 209.957 1.00 64.70 C
ANISOU 3357 CD2 TRP B 169 7355 8375 8854 873 544 -812 C
ATOM 3358 NE1 TRP B 169 44.585 -26.252 208.046 1.00 55.23 N
ANISOU 3358 NE1 TRP B 169 6242 7120 7624 672 993 -861 N
ATOM 3359 CE2 TRP B 169 44.003 -27.373 208.576 1.00 58.04 C
ANISOU 3359 CE2 TRP B 169 6692 7463 7898 798 788 -809 C
ATOM 3360 CE3 TRP B 169 43.789 -28.427 210.740 1.00 58.24 C
ANISOU 3360 CE3 TRP B 169 6618 7542 7968 1002 326 -740 C
ATOM 3361 CZ2 TRP B 169 43.261 -28.377 207.960 1.00 54.75 C
ANISOU 3361 CZ2 TRP B 169 6514 6972 7317 843 795 -764 C
ATOM 3362 CZ3 TRP B 169 43.054 -29.425 210.127 1.00 52.77 C
ANISOU 3362 CZ3 TRP B 169 6151 6757 7143 1037 362 -683 C
ATOM 3363 CH2 TRP B 169 42.795 -29.392 208.751 1.00 53.90 C
ANISOU 3363 CH2 TRP B 169 6451 6840 7188 955 581 -709 C
ATOM 3364 N ALA B 170 45.637 -24.248 214.370 1.00 59.17 N
ANISOU 3364 N ALA B 170 6013 8004 8465 770 -163 -1027 N
ATOM 3365 CA ALA B 170 45.954 -24.312 215.794 1.00 56.76 C
ANISOU 3365 CA ALA B 170 5615 7794 8156 861 -481 -1075 C
ATOM 3366 C ALA B 170 44.718 -24.023 216.638 1.00 61.72 C
ANISOU 3366 C ALA B 170 6509 8447 8495 841 -603 -973 C
ATOM 3367 O ALA B 170 44.394 -24.768 217.578 1.00 66.88 O
ANISOU 3367 O ALA B 170 7279 9142 8991 972 -811 -897 O
ATOM 3368 CB ALA B 170 47.077 -23.327 216.121 1.00 55.86 C
ANISOU 3368 CB ALA B 170 5191 7733 8301 771 -532 -1269 C
ATOM 3369 N VAL B 171 43.984 -22.966 216.283 1.00 56.87 N
ANISOU 3369 N VAL B 171 6007 7792 7809 685 -452 -959 N
ATOM 3370 CA VAL B 171 42.772 -22.624 217.017 1.00 58.53 C
ANISOU 3370 CA VAL B 171 6445 8015 7780 667 -522 -876 C
ATOM 3371 C VAL B 171 41.761 -23.758 216.920 1.00 51.11 C
ANISOU 3371 C VAL B 171 5724 7044 6651 759 -518 -702 C
ATOM 3372 O VAL B 171 41.191 -24.188 217.930 1.00 50.25 O
ANISOU 3372 O VAL B 171 5749 6975 6368 834 -661 -632 O
ATOM 3373 CB VAL B 171 42.181 -21.301 216.499 1.00 53.44 C
ANISOU 3373 CB VAL B 171 5863 7303 7139 503 -344 -888 C
ATOM 3374 CG1 VAL B 171 40.821 -21.049 217.121 1.00 50.72 C
ANISOU 3374 CG1 VAL B 171 5740 6957 6573 503 -377 -797 C
ATOM 3375 CG2 VAL B 171 43.131 -20.137 216.792 1.00 49.54 C
ANISOU 3375 CG2 VAL B 171 5166 6817 6840 392 -359 -1071 C
ATOM 3376 N SER B 172 41.523 -24.260 215.700 1.00 48.24 N
ANISOU 3376 N SER B 172 5412 6602 6314 745 -346 -636 N
ATOM 3377 CA SER B 172 40.501 -25.284 215.512 1.00 46.62 C
ANISOU 3377 CA SER B 172 5407 6346 5959 800 -337 -491 C
ATOM 3378 C SER B 172 40.848 -26.555 216.267 1.00 53.82 C
ANISOU 3378 C SER B 172 6329 7271 6850 959 -501 -447 C
ATOM 3379 O SER B 172 39.971 -27.202 216.849 1.00 53.14 O
ANISOU 3379 O SER B 172 6415 7165 6610 1003 -562 -327 O
ATOM 3380 CB SER B 172 40.334 -25.595 214.021 1.00 46.47 C
ANISOU 3380 CB SER B 172 5442 6242 5971 756 -148 -465 C
ATOM 3381 OG SER B 172 39.772 -24.493 213.327 1.00 59.68 O
ANISOU 3381 OG SER B 172 7175 7888 7614 625 -16 -456 O
ATOM 3382 N LEU B 173 42.126 -26.931 216.275 1.00 59.46 N
ANISOU 3382 N LEU B 173 6855 8004 7732 1052 -566 -537 N
ATOM 3383 CA LEU B 173 42.520 -28.113 217.022 1.00 56.89 C
ANISOU 3383 CA LEU B 173 6540 7674 7399 1231 -749 -483 C
ATOM 3384 C LEU B 173 42.339 -27.908 218.518 1.00 62.98 C
ANISOU 3384 C LEU B 173 7387 8534 8007 1282 -975 -448 C
ATOM 3385 O LEU B 173 41.991 -28.860 219.229 1.00 60.07 O
ANISOU 3385 O LEU B 173 7182 8138 7505 1399 -1090 -319 O
ATOM 3386 CB LEU B 173 43.970 -28.480 216.686 1.00 57.60 C
ANISOU 3386 CB LEU B 173 6369 7766 7748 1336 -778 -602 C
ATOM 3387 CG LEU B 173 44.210 -28.980 215.253 1.00 57.56 C
ANISOU 3387 CG LEU B 173 6331 7661 7878 1325 -536 -635 C
ATOM 3388 CD1 LEU B 173 45.684 -28.929 214.886 1.00 55.10 C
ANISOU 3388 CD1 LEU B 173 5701 7370 7864 1385 -497 -792 C
ATOM 3389 CD2 LEU B 173 43.679 -30.399 215.087 1.00 57.84 C
ANISOU 3389 CD2 LEU B 173 6560 7578 7839 1440 -541 -517 C
ATOM 3390 N ALA B 174 42.531 -26.679 219.011 1.00 65.33 N
ANISOU 3390 N ALA B 174 7601 8923 8297 1191 -1025 -559 N
ATOM 3391 CA ALA B 174 42.382 -26.451 220.447 1.00 60.58 C
ANISOU 3391 CA ALA B 174 7103 8412 7504 1239 -1239 -551 C
ATOM 3392 C ALA B 174 40.915 -26.444 220.869 1.00 55.87 C
ANISOU 3392 C ALA B 174 6785 7791 6651 1188 -1147 -413 C
ATOM 3393 O ALA B 174 40.529 -27.145 221.811 1.00 59.84 O
ANISOU 3393 O ALA B 174 7477 8304 6956 1285 -1255 -295 O
ATOM 3394 CB ALA B 174 43.060 -25.138 220.848 1.00 62.75 C
ANISOU 3394 CB ALA B 174 7203 8777 7861 1149 -1326 -746 C
ATOM 3395 N ILE B 175 40.073 -25.671 220.180 1.00 56.19 N
ANISOU 3395 N ILE B 175 6857 7792 6701 1040 -941 -418 N
ATOM 3396 CA ILE B 175 38.730 -25.423 220.701 1.00 62.85 C
ANISOU 3396 CA ILE B 175 7905 8628 7347 987 -858 -328 C
ATOM 3397 C ILE B 175 37.806 -26.625 220.580 1.00 58.40 C
ANISOU 3397 C ILE B 175 7510 7983 6697 1028 -785 -144 C
ATOM 3398 O ILE B 175 36.733 -26.626 221.193 1.00 58.29 O
ANISOU 3398 O ILE B 175 7656 7965 6527 1000 -719 -56 O
ATOM 3399 CB ILE B 175 38.073 -24.198 220.026 1.00 59.71 C
ANISOU 3399 CB ILE B 175 7475 8200 7012 839 -682 -384 C
ATOM 3400 CG1 ILE B 175 37.831 -24.440 218.537 1.00 52.66 C
ANISOU 3400 CG1 ILE B 175 6540 7215 6252 784 -527 -335 C
ATOM 3401 CG2 ILE B 175 38.927 -22.949 220.223 1.00 56.60 C
ANISOU 3401 CG2 ILE B 175 6933 7854 6716 776 -734 -568 C
ATOM 3402 CD1 ILE B 175 37.171 -23.241 217.839 1.00 44.82 C
ANISOU 3402 CD1 ILE B 175 5541 6179 5309 661 -379 -362 C
ATOM 3403 N MET B 176 38.173 -27.636 219.796 1.00 53.30 N
ANISOU 3403 N MET B 176 6826 7259 6165 1083 -775 -96 N
ATOM 3404 CA MET B 176 37.348 -28.827 219.645 1.00 49.40 C
ANISOU 3404 CA MET B 176 6488 6659 5622 1107 -711 61 C
ATOM 3405 C MET B 176 37.731 -29.959 220.593 1.00 52.92 C
ANISOU 3405 C MET B 176 7051 7079 5976 1260 -856 169 C
ATOM 3406 O MET B 176 37.075 -31.008 220.572 1.00 60.27 O
ANISOU 3406 O MET B 176 8129 7896 6876 1276 -797 309 O
ATOM 3407 CB MET B 176 37.390 -29.314 218.199 1.00 46.95 C
ANISOU 3407 CB MET B 176 6116 6250 5471 1072 -603 44 C
ATOM 3408 CG MET B 176 36.754 -28.318 217.226 1.00 56.95 C
ANISOU 3408 CG MET B 176 7340 7521 6780 926 -462 -11 C
ATOM 3409 SD MET B 176 35.109 -27.822 217.794 1.00 61.84 S
ANISOU 3409 SD MET B 176 8078 8146 7272 830 -386 79 S
ATOM 3410 CE MET B 176 34.736 -26.439 216.718 1.00 56.27 C
ANISOU 3410 CE MET B 176 7287 7450 6645 710 -282 -1 C
ATOM 3411 N VAL B 177 38.766 -29.774 221.422 1.00 61.46 N
ANISOU 3411 N VAL B 177 8077 8254 7021 1372 -1056 110 N
ATOM 3412 CA VAL B 177 39.096 -30.784 222.434 1.00 63.58 C
ANISOU 3412 CA VAL B 177 8496 8501 7162 1539 -1228 237 C
ATOM 3413 C VAL B 177 37.901 -31.081 223.329 1.00 68.48 C
ANISOU 3413 C VAL B 177 9397 9092 7532 1507 -1144 405 C
ATOM 3414 O VAL B 177 37.643 -32.264 223.612 1.00 70.69 O
ANISOU 3414 O VAL B 177 9851 9253 7756 1587 -1143 578 O
ATOM 3415 CB VAL B 177 40.351 -30.364 223.212 1.00 60.71 C
ANISOU 3415 CB VAL B 177 8016 8266 6787 1658 -1499 125 C
ATOM 3416 CG1 VAL B 177 40.632 -31.343 224.342 1.00 66.00 C
ANISOU 3416 CG1 VAL B 177 8883 8919 7275 1850 -1713 279 C
ATOM 3417 CG2 VAL B 177 41.551 -30.291 222.280 1.00 50.93 C
ANISOU 3417 CG2 VAL B 177 6470 7028 5853 1696 -1544 -26 C
ATOM 3418 N PRO B 178 37.147 -30.096 223.825 1.00 63.85 N
ANISOU 3418 N PRO B 178 8872 8591 6799 1396 -1052 366 N
ATOM 3419 CA PRO B 178 35.974 -30.430 224.646 1.00 56.73 C
ANISOU 3419 CA PRO B 178 8223 7652 5678 1360 -916 525 C
ATOM 3420 C PRO B 178 34.995 -31.331 223.919 1.00 51.92 C
ANISOU 3420 C PRO B 178 7661 6881 5186 1282 -718 658 C
ATOM 3421 O PRO B 178 34.318 -32.142 224.564 1.00 63.92 O
ANISOU 3421 O PRO B 178 9393 8314 6578 1290 -632 834 O
ATOM 3422 CB PRO B 178 35.360 -29.054 224.957 1.00 55.09 C
ANISOU 3422 CB PRO B 178 7994 7551 5385 1241 -809 404 C
ATOM 3423 CG PRO B 178 36.495 -28.086 224.814 1.00 50.38 C
ANISOU 3423 CG PRO B 178 7205 7064 4873 1260 -984 199 C
ATOM 3424 CD PRO B 178 37.357 -28.642 223.719 1.00 54.62 C
ANISOU 3424 CD PRO B 178 7548 7539 5665 1303 -1052 173 C
ATOM 3425 N GLN B 179 34.890 -31.208 222.594 1.00 51.99 N
ANISOU 3425 N GLN B 179 7488 6838 5427 1197 -640 576 N
ATOM 3426 CA GLN B 179 34.052 -32.134 221.841 1.00 51.30 C
ANISOU 3426 CA GLN B 179 7439 6592 5462 1123 -500 672 C
ATOM 3427 C GLN B 179 34.538 -33.570 221.982 1.00 58.69 C
ANISOU 3427 C GLN B 179 8497 7385 6419 1246 -576 798 C
ATOM 3428 O GLN B 179 33.730 -34.495 222.129 1.00 65.47 O
ANISOU 3428 O GLN B 179 9504 8098 7274 1203 -464 944 O
ATOM 3429 CB GLN B 179 34.037 -31.743 220.369 1.00 60.16 C
ANISOU 3429 CB GLN B 179 8374 7697 6787 1035 -450 545 C
ATOM 3430 CG GLN B 179 33.144 -32.620 219.537 1.00 62.65 C
ANISOU 3430 CG GLN B 179 8725 7859 7222 945 -339 606 C
ATOM 3431 CD GLN B 179 31.708 -32.486 219.965 1.00 65.22 C
ANISOU 3431 CD GLN B 179 9109 8166 7507 821 -191 691 C
ATOM 3432 OE1 GLN B 179 31.213 -31.374 220.138 1.00 64.08 O
ANISOU 3432 OE1 GLN B 179 8894 8127 7327 759 -135 636 O
ATOM 3433 NE2 GLN B 179 31.034 -33.612 220.170 1.00 62.54 N
ANISOU 3433 NE2 GLN B 179 8890 7678 7196 783 -112 822 N
ATOM 3434 N ALA B 180 35.856 -33.780 221.922 1.00 53.81 N
ANISOU 3434 N ALA B 180 7803 6789 5855 1399 -759 740 N
ATOM 3435 CA ALA B 180 36.389 -35.130 222.055 1.00 60.33 C
ANISOU 3435 CA ALA B 180 8736 7460 6726 1550 -847 857 C
ATOM 3436 C ALA B 180 36.272 -35.650 223.481 1.00 66.60 C
ANISOU 3436 C ALA B 180 9789 8233 7282 1652 -920 1052 C
ATOM 3437 O ALA B 180 36.127 -36.860 223.687 1.00 70.22 O
ANISOU 3437 O ALA B 180 10427 8506 7748 1722 -904 1222 O
ATOM 3438 CB ALA B 180 37.846 -35.170 221.591 1.00 57.14 C
ANISOU 3438 CB ALA B 180 8141 7089 6483 1702 -1018 730 C
ATOM 3439 N ALA B 181 36.351 -34.765 224.476 1.00 62.92 N
ANISOU 3439 N ALA B 181 9374 7942 6593 1666 -998 1031 N
ATOM 3440 CA ALA B 181 36.285 -35.231 225.859 1.00 57.74 C
ANISOU 3440 CA ALA B 181 9010 7277 5650 1774 -1074 1218 C
ATOM 3441 C ALA B 181 34.915 -35.798 226.212 1.00 60.49 C
ANISOU 3441 C ALA B 181 9594 7492 5897 1649 -806 1408 C
ATOM 3442 O ALA B 181 34.826 -36.714 227.036 1.00 67.89 O
ANISOU 3442 O ALA B 181 10809 8314 6673 1740 -813 1625 O
ATOM 3443 CB ALA B 181 36.650 -34.104 226.825 1.00 47.06 C
ANISOU 3443 CB ALA B 181 7680 6148 4055 1805 -1216 1118 C
ATOM 3444 N VAL B 182 33.837 -35.270 225.617 1.00 60.28 N
ANISOU 3444 N VAL B 182 9459 7471 5975 1443 -567 1338 N
ATOM 3445 CA VAL B 182 32.495 -35.741 225.958 1.00 60.26 C
ANISOU 3445 CA VAL B 182 9623 7350 5924 1305 -295 1497 C
ATOM 3446 C VAL B 182 32.075 -36.977 225.178 1.00 66.65 C
ANISOU 3446 C VAL B 182 10443 7912 6970 1246 -193 1594 C
ATOM 3447 O VAL B 182 31.037 -37.577 225.500 1.00 66.19 O
ANISOU 3447 O VAL B 182 10528 7715 6907 1130 29 1746 O
ATOM 3448 CB VAL B 182 31.435 -34.642 225.743 1.00 56.64 C
ANISOU 3448 CB VAL B 182 9023 6998 5500 1120 -91 1380 C
ATOM 3449 CG1 VAL B 182 31.716 -33.451 226.642 1.00 61.61 C
ANISOU 3449 CG1 VAL B 182 9690 7838 5882 1166 -151 1284 C
ATOM 3450 CG2 VAL B 182 31.387 -34.226 224.285 1.00 49.28 C
ANISOU 3450 CG2 VAL B 182 7798 6068 4859 1028 -102 1206 C
ATOM 3451 N MET B 183 32.829 -37.376 224.158 1.00 65.03 N
ANISOU 3451 N MET B 183 10089 7638 6981 1310 -327 1498 N
ATOM 3452 CA MET B 183 32.445 -38.551 223.392 1.00 66.25 C
ANISOU 3452 CA MET B 183 10271 7544 7358 1250 -236 1558 C
ATOM 3453 C MET B 183 32.694 -39.807 224.213 1.00 68.47 C
ANISOU 3453 C MET B 183 10838 7623 7556 1381 -261 1795 C
ATOM 3454 O MET B 183 33.784 -40.001 224.761 1.00 78.80 O
ANISOU 3454 O MET B 183 12229 8960 8753 1601 -474 1846 O
ATOM 3455 CB MET B 183 33.212 -38.606 222.075 1.00 59.77 C
ANISOU 3455 CB MET B 183 9240 6705 6765 1293 -350 1371 C
ATOM 3456 CG MET B 183 33.028 -37.369 221.217 1.00 53.17 C
ANISOU 3456 CG MET B 183 8159 6051 5994 1175 -329 1161 C
ATOM 3457 SD MET B 183 31.290 -36.982 220.916 1.00 60.62 S
ANISOU 3457 SD MET B 183 9054 6983 6995 912 -101 1162 S
ATOM 3458 CE MET B 183 30.792 -38.430 219.992 1.00 57.86 C
ANISOU 3458 CE MET B 183 8757 6348 6882 824 -33 1190 C
ATOM 3459 N GLU B 184 31.690 -40.678 224.276 1.00 72.71 N
ANISOU 3459 N GLU B 184 11519 7941 8168 1245 -50 1942 N
ATOM 3460 CA GLU B 184 31.800 -41.949 224.972 1.00 76.70 C
ANISOU 3460 CA GLU B 184 12324 8198 8622 1344 -30 2192 C
ATOM 3461 C GLU B 184 31.032 -42.997 224.182 1.00 76.16 C
ANISOU 3461 C GLU B 184 12261 7834 8842 1181 142 2216 C
ATOM 3462 O GLU B 184 30.044 -42.692 223.503 1.00 69.04 O
ANISOU 3462 O GLU B 184 11189 6944 8100 951 298 2099 O
ATOM 3463 CB GLU B 184 31.263 -41.870 226.409 1.00 83.87 C
ANISOU 3463 CB GLU B 184 13514 9136 9214 1334 103 2418 C
ATOM 3464 CG GLU B 184 31.881 -40.760 227.254 1.00 91.41 C
ANISOU 3464 CG GLU B 184 14487 10390 9854 1464 -61 2367 C
ATOM 3465 CD GLU B 184 33.354 -40.985 227.542 1.00 92.22 C
ANISOU 3465 CD GLU B 184 14645 10530 9866 1754 -409 2382 C
ATOM 3466 OE1 GLU B 184 33.799 -42.152 227.503 1.00 91.97 O
ANISOU 3466 OE1 GLU B 184 14755 10262 9929 1888 -486 2529 O
ATOM 3467 OE2 GLU B 184 34.065 -39.991 227.810 1.00 92.52 O
ANISOU 3467 OE2 GLU B 184 14568 10821 9763 1848 -609 2239 O
ATOM 3468 N CYS B 185 31.505 -44.236 224.276 1.00 85.20 N
ANISOU 3468 N CYS B 185 13603 8706 10065 1309 93 2361 N
ATOM 3469 CA CYS B 185 30.953 -45.361 223.533 1.00 83.97 C
ANISOU 3469 CA CYS B 185 13481 8225 10200 1177 226 2370 C
ATOM 3470 C CYS B 185 30.381 -46.358 224.527 1.00 79.10 C
ANISOU 3470 C CYS B 185 13202 7335 9517 1141 410 2682 C
ATOM 3471 O CYS B 185 31.117 -46.897 225.361 1.00 84.58 O
ANISOU 3471 O CYS B 185 14153 7934 10048 1367 301 2890 O
ATOM 3472 CB CYS B 185 32.027 -46.014 222.659 1.00 87.76 C
ANISOU 3472 CB CYS B 185 13904 8565 10877 1360 40 2249 C
ATOM 3473 SG CYS B 185 31.408 -47.234 221.492 1.00 94.22 S
ANISOU 3473 SG CYS B 185 14727 9008 12066 1184 176 2157 S
ATOM 3474 N SER B 186 29.077 -46.612 224.433 1.00 79.74 N
ANISOU 3474 N SER B 186 13277 7284 9737 856 685 2717 N
ATOM 3475 CA SER B 186 28.400 -47.458 225.408 1.00 92.49 C
ANISOU 3475 CA SER B 186 15205 8643 11293 773 930 3020 C
ATOM 3476 C SER B 186 27.417 -48.380 224.703 1.00 95.35 C
ANISOU 3476 C SER B 186 15523 8681 12025 504 1141 2992 C
ATOM 3477 O SER B 186 26.914 -48.076 223.620 1.00 94.02 O
ANISOU 3477 O SER B 186 15057 8568 12098 325 1134 2734 O
ATOM 3478 CB SER B 186 27.669 -46.624 226.470 1.00100.15 C
ANISOU 3478 CB SER B 186 16212 9849 11993 667 1120 3116 C
ATOM 3479 OG SER B 186 26.684 -45.794 225.879 1.00101.75 O
ANISOU 3479 OG SER B 186 16117 10199 12343 429 1268 2927 O
ATOM 3480 N SER B 187 27.154 -49.520 225.329 1.00100.84 N
ANISOU 3480 N SER B 187 16400 9141 12773 447 1253 3175 N
ATOM 3481 CA SER B 187 26.264 -50.529 224.776 1.00105.71 C
ANISOU 3481 CA SER B 187 16989 9428 13749 187 1436 3153 C
ATOM 3482 C SER B 187 24.867 -50.428 225.385 1.00103.89 C
ANISOU 3482 C SER B 187 16715 9208 13552 -113 1769 3243 C
ATOM 3483 O SER B 187 24.665 -49.853 226.457 1.00101.80 O
ANISOU 3483 O SER B 187 16529 9156 12996 -89 1880 3377 O
ATOM 3484 CB SER B 187 26.837 -51.930 224.996 1.00109.18 C
ANISOU 3484 CB SER B 187 17638 9568 14279 303 1356 3283 C
ATOM 3485 OG SER B 187 26.070 -52.904 224.311 1.00112.46 O
ANISOU 3485 OG SER B 187 18013 9651 15066 58 1495 3214 O
ATOM 3486 N VAL B 188 23.897 -51.027 224.687 1.00107.40 N
ANISOU 3486 N VAL B 188 17021 9416 14369 -401 1925 3146 N
ATOM 3487 CA VAL B 188 22.510 -50.962 225.136 1.00109.76 C
ANISOU 3487 CA VAL B 188 17204 9718 14782 -706 2245 3192 C
ATOM 3488 C VAL B 188 22.375 -51.533 226.539 1.00114.21 C
ANISOU 3488 C VAL B 188 18034 10239 15123 -680 2420 3473 C
ATOM 3489 O VAL B 188 21.566 -51.049 227.341 1.00112.42 O
ANISOU 3489 O VAL B 188 17774 10161 14779 -806 2673 3552 O
ATOM 3490 CB VAL B 188 21.598 -51.708 224.140 1.00113.81 C
ANISOU 3490 CB VAL B 188 17519 9956 15766 -1011 2324 3026 C
ATOM 3491 CG1 VAL B 188 20.139 -51.603 224.565 1.00120.93 C
ANISOU 3491 CG1 VAL B 188 18234 10882 16831 -1327 2644 3047 C
ATOM 3492 CG2 VAL B 188 21.792 -51.174 222.725 1.00113.67 C
ANISOU 3492 CG2 VAL B 188 17272 9973 15945 -1027 2123 2734 C
ATOM 3493 N LEU B 189 23.180 -52.538 226.870 1.00116.48 N
ANISOU 3493 N LEU B 189 18589 10327 15343 -506 2291 3625 N
ATOM 3494 CA LEU B 189 23.209 -53.132 228.195 1.00124.00 C
ANISOU 3494 CA LEU B 189 19836 11221 16058 -447 2415 3910 C
ATOM 3495 C LEU B 189 24.648 -53.210 228.679 1.00127.36 C
ANISOU 3495 C LEU B 189 20495 11718 16177 -76 2111 4027 C
ATOM 3496 O LEU B 189 25.575 -53.334 227.871 1.00119.24 O
ANISOU 3496 O LEU B 189 19416 10640 15250 105 1835 3904 O
ATOM 3497 CB LEU B 189 22.573 -54.528 228.191 1.00127.92 C
ANISOU 3497 CB LEU B 189 20426 11329 16850 -651 2592 4013 C
ATOM 3498 CG LEU B 189 21.055 -54.544 227.975 1.00119.26 C
ANISOU 3498 CG LEU B 189 19095 10165 16052 -1036 2918 3927 C
ATOM 3499 CD1 LEU B 189 20.561 -55.947 227.652 1.00117.17 C
ANISOU 3499 CD1 LEU B 189 18879 9491 16150 -1237 3018 3959 C
ATOM 3500 CD2 LEU B 189 20.333 -53.993 229.197 1.00119.37 C
ANISOU 3500 CD2 LEU B 189 19164 10378 15811 -1114 3219 4082 C
ATOM 3501 N PRO B 190 24.863 -53.131 229.997 1.00138.24 N
ANISOU 3501 N PRO B 190 22119 13219 17186 46 2150 4250 N
ATOM 3502 CA PRO B 190 26.213 -52.802 230.491 1.00134.86 C
ANISOU 3502 CA PRO B 190 21836 12977 16430 399 1821 4309 C
ATOM 3503 C PRO B 190 27.314 -53.761 230.069 1.00129.57 C
ANISOU 3503 C PRO B 190 21249 12078 15903 625 1536 4341 C
ATOM 3504 O PRO B 190 28.409 -53.301 229.718 1.00126.91 O
ANISOU 3504 O PRO B 190 20830 11896 15496 877 1226 4228 O
ATOM 3505 CB PRO B 190 26.025 -52.803 232.017 1.00135.72 C
ANISOU 3505 CB PRO B 190 22229 13184 16157 428 1959 4557 C
ATOM 3506 CG PRO B 190 24.766 -53.576 232.264 1.00133.31 C
ANISOU 3506 CG PRO B 190 21983 12629 16040 128 2347 4679 C
ATOM 3507 CD PRO B 190 23.893 -53.328 231.086 1.00132.33 C
ANISOU 3507 CD PRO B 190 21520 12451 16308 -134 2491 4441 C
ATOM 3508 N GLU B 191 27.057 -55.064 230.034 1.00118.36 N
ANISOU 3508 N GLU B 191 19966 10289 14715 540 1636 4471 N
ATOM 3509 CA GLU B 191 28.095 -56.029 229.694 1.00119.06 C
ANISOU 3509 CA GLU B 191 20143 10137 14957 768 1381 4509 C
ATOM 3510 C GLU B 191 27.986 -56.517 228.262 1.00107.42 C
ANISOU 3510 C GLU B 191 18474 8419 13922 665 1362 4275 C
ATOM 3511 O GLU B 191 28.760 -57.390 227.854 1.00 95.53 O
ANISOU 3511 O GLU B 191 17022 6671 12602 833 1187 4271 O
ATOM 3512 CB GLU B 191 28.066 -57.234 230.643 1.00132.06 C
ANISOU 3512 CB GLU B 191 22113 11505 16558 793 1463 4822 C
ATOM 3513 CG GLU B 191 28.388 -56.903 232.091 1.00141.33 C
ANISOU 3513 CG GLU B 191 23537 12893 17270 950 1425 5067 C
ATOM 3514 CD GLU B 191 27.263 -56.145 232.761 1.00150.86 C
ANISOU 3514 CD GLU B 191 24758 14305 18258 711 1746 5096 C
ATOM 3515 OE1 GLU B 191 26.207 -55.985 232.116 1.00153.61 O
ANISOU 3515 OE1 GLU B 191 24908 14601 18854 419 2003 4951 O
ATOM 3516 OE2 GLU B 191 27.429 -55.706 233.917 1.00155.99 O
ANISOU 3516 OE2 GLU B 191 25604 15167 18499 814 1740 5249 O
ATOM 3517 N LEU B 192 27.036 -55.982 227.498 1.00104.45 N
ANISOU 3517 N LEU B 192 17872 8093 13720 394 1535 4070 N
ATOM 3518 CA LEU B 192 26.842 -56.453 226.135 1.00106.57 C
ANISOU 3518 CA LEU B 192 17972 8126 14393 266 1517 3827 C
ATOM 3519 C LEU B 192 28.074 -56.184 225.285 1.00108.83 C
ANISOU 3519 C LEU B 192 18153 8483 14715 547 1209 3633 C
ATOM 3520 O LEU B 192 28.429 -56.990 224.417 1.00109.06 O
ANISOU 3520 O LEU B 192 18165 8243 15029 584 1122 3500 O
ATOM 3521 CB LEU B 192 25.614 -55.776 225.534 1.00 99.21 C
ANISOU 3521 CB LEU B 192 16793 7288 13613 -67 1725 3640 C
ATOM 3522 CG LEU B 192 25.007 -56.420 224.293 1.00 97.74 C
ANISOU 3522 CG LEU B 192 16456 6820 13861 -308 1769 3407 C
ATOM 3523 CD1 LEU B 192 24.906 -57.918 224.495 1.00 92.58 C
ANISOU 3523 CD1 LEU B 192 16003 5762 13412 -365 1834 3541 C
ATOM 3524 CD2 LEU B 192 23.640 -55.823 224.014 1.00 95.44 C
ANISOU 3524 CD2 LEU B 192 15922 6629 13714 -661 1993 3284 C
ATOM 3525 N ALA B 193 28.777 -55.083 225.564 1.00 99.14 N
ANISOU 3525 N ALA B 193 16859 7611 13197 756 1045 3610 N
ATOM 3526 CA ALA B 193 29.941 -54.716 224.766 1.00101.42 C
ANISOU 3526 CA ALA B 193 17013 8000 13522 1017 773 3412 C
ATOM 3527 C ALA B 193 31.041 -55.763 224.863 1.00108.77 C
ANISOU 3527 C ALA B 193 18065 8711 14552 1291 580 3494 C
ATOM 3528 O ALA B 193 31.888 -55.844 223.969 1.00101.02 O
ANISOU 3528 O ALA B 193 16958 7689 13737 1465 412 3296 O
ATOM 3529 CB ALA B 193 30.466 -53.345 225.203 1.00 77.81 C
ANISOU 3529 CB ALA B 193 13933 5436 10194 1177 634 3391 C
ATOM 3530 N ALA B 194 31.032 -56.579 225.916 1.00 88.55 N
ANISOU 3530 N ALA B 194 15742 5996 11905 1332 615 3780 N
ATOM 3531 CA ALA B 194 32.000 -57.657 226.046 1.00110.06 C
ANISOU 3531 CA ALA B 194 18586 8472 14758 1584 441 3884 C
ATOM 3532 C ALA B 194 31.777 -58.763 225.024 1.00115.06 C
ANISOU 3532 C ALA B 194 19213 8697 15808 1480 516 3744 C
ATOM 3533 O ALA B 194 32.640 -59.637 224.888 1.00132.41 O
ANISOU 3533 O ALA B 194 21466 10667 18177 1703 369 3768 O
ATOM 3534 CB ALA B 194 31.957 -58.238 227.462 1.00 97.01 C
ANISOU 3534 CB ALA B 194 17222 6748 12890 1638 470 4245 C
ATOM 3535 N ARG B 195 30.641 -58.762 224.325 1.00105.11 N
ANISOU 3535 N ARG B 195 17878 7332 14726 1146 732 3591 N
ATOM 3536 CA ARG B 195 30.347 -59.789 223.334 1.00103.56 C
ANISOU 3536 CA ARG B 195 17679 6754 14917 1011 794 3420 C
ATOM 3537 C ARG B 195 30.307 -59.278 221.901 1.00 90.11 C
ANISOU 3537 C ARG B 195 15742 5109 13387 934 761 3038 C
ATOM 3538 O ARG B 195 30.685 -60.018 220.991 1.00 91.55 O
ANISOU 3538 O ARG B 195 15909 5037 13837 985 700 2841 O
ATOM 3539 CB ARG B 195 29.009 -60.469 223.652 1.00104.12 C
ANISOU 3539 CB ARG B 195 17867 6582 15113 653 1063 3540 C
ATOM 3540 CG ARG B 195 28.914 -61.008 225.067 1.00101.63 C
ANISOU 3540 CG ARG B 195 17814 6186 14614 693 1146 3926 C
ATOM 3541 CD ARG B 195 27.548 -61.607 225.337 1.00104.77 C
ANISOU 3541 CD ARG B 195 18296 6361 15151 319 1448 4024 C
ATOM 3542 NE ARG B 195 27.332 -62.838 224.585 1.00107.82 N
ANISOU 3542 NE ARG B 195 18728 6310 15928 196 1477 3913 N
ATOM 3543 CZ ARG B 195 26.197 -63.529 224.597 1.00111.02 C
ANISOU 3543 CZ ARG B 195 19178 6458 16546 -142 1715 3942 C
ATOM 3544 NH1 ARG B 195 25.171 -63.109 225.322 1.00111.60 N
ANISOU 3544 NH1 ARG B 195 19239 6673 16491 -386 1964 4084 N
ATOM 3545 NH2 ARG B 195 26.086 -64.641 223.882 1.00113.92 N
ANISOU 3545 NH2 ARG B 195 19593 6426 17264 -238 1709 3816 N
ATOM 3546 N THR B 196 29.857 -58.047 221.671 1.00 85.92 N
ANISOU 3546 N THR B 196 15043 4897 12706 813 803 2921 N
ATOM 3547 CA THR B 196 29.732 -57.534 220.314 1.00 82.50 C
ANISOU 3547 CA THR B 196 14412 4517 12417 718 779 2567 C
ATOM 3548 C THR B 196 29.651 -56.016 220.361 1.00 93.69 C
ANISOU 3548 C THR B 196 15672 6346 13580 719 760 2518 C
ATOM 3549 O THR B 196 29.308 -55.425 221.388 1.00 86.71 O
ANISOU 3549 O THR B 196 14823 5672 12452 689 828 2733 O
ATOM 3550 CB THR B 196 28.500 -58.107 219.606 1.00 93.76 C
ANISOU 3550 CB THR B 196 15805 5690 14129 339 942 2411 C
ATOM 3551 OG1 THR B 196 28.402 -57.556 218.288 1.00 96.35 O
ANISOU 3551 OG1 THR B 196 15955 6093 14562 251 890 2057 O
ATOM 3552 CG2 THR B 196 27.235 -57.761 220.381 1.00 88.36 C
ANISOU 3552 CG2 THR B 196 15103 5098 13371 43 1154 2586 C
ATOM 3553 N ARG B 197 29.991 -55.392 219.233 1.00 88.19 N
ANISOU 3553 N ARG B 197 14818 5759 12931 761 672 2225 N
ATOM 3554 CA ARG B 197 29.801 -53.963 219.035 1.00 81.91 C
ANISOU 3554 CA ARG B 197 13870 5308 11946 722 661 2132 C
ATOM 3555 C ARG B 197 28.527 -53.641 218.269 1.00 80.46 C
ANISOU 3555 C ARG B 197 13521 5140 11911 349 781 1935 C
ATOM 3556 O ARG B 197 28.272 -52.466 217.983 1.00 81.10 O
ANISOU 3556 O ARG B 197 13353 5609 11853 274 720 1795 O
ATOM 3557 CB ARG B 197 31.006 -53.365 218.306 1.00 85.06 C
ANISOU 3557 CB ARG B 197 14133 5914 12273 992 458 1915 C
ATOM 3558 CG ARG B 197 32.259 -53.308 219.155 1.00 98.36 C
ANISOU 3558 CG ARG B 197 15884 7705 13785 1360 299 2096 C
ATOM 3559 CD ARG B 197 33.455 -52.833 218.349 1.00102.14 C
ANISOU 3559 CD ARG B 197 16187 8353 14269 1608 127 1853 C
ATOM 3560 NE ARG B 197 34.649 -52.714 219.180 1.00107.17 N
ANISOU 3560 NE ARG B 197 16818 9127 14775 1943 -56 2004 N
ATOM 3561 CZ ARG B 197 35.864 -52.463 218.708 1.00106.02 C
ANISOU 3561 CZ ARG B 197 16514 9096 14674 2208 -207 1841 C
ATOM 3562 NH1 ARG B 197 36.053 -52.309 217.404 1.00 94.91 N
ANISOU 3562 NH1 ARG B 197 14951 7704 13408 2166 -172 1521 N
ATOM 3563 NH2 ARG B 197 36.893 -52.370 219.540 1.00112.45 N
ANISOU 3563 NH2 ARG B 197 17266 10063 15399 2473 -394 1973 N
ATOM 3564 N ALA B 198 27.722 -54.652 217.935 1.00 75.79 N
ANISOU 3564 N ALA B 198 12999 4194 11604 105 907 1894 N
ATOM 3565 CA ALA B 198 26.540 -54.429 217.110 1.00 77.74 C
ANISOU 3565 CA ALA B 198 13046 4453 12037 -252 966 1664 C
ATOM 3566 C ALA B 198 25.527 -53.516 217.786 1.00 80.02 C
ANISOU 3566 C ALA B 198 13167 5016 12221 -453 1090 1785 C
ATOM 3567 O ALA B 198 24.717 -52.891 217.094 1.00 82.71 O
ANISOU 3567 O ALA B 198 13239 5546 12639 -677 1053 1567 O
ATOM 3568 CB ALA B 198 25.882 -55.768 216.760 1.00 75.43 C
ANISOU 3568 CB ALA B 198 12838 3745 12077 -480 1050 1599 C
ATOM 3569 N PHE B 199 25.545 -53.433 219.116 1.00 83.81 N
ANISOU 3569 N PHE B 199 13809 5514 12523 -371 1234 2123 N
ATOM 3570 CA PHE B 199 24.605 -52.608 219.865 1.00 81.83 C
ANISOU 3570 CA PHE B 199 13430 5500 12163 -545 1401 2249 C
ATOM 3571 C PHE B 199 25.288 -51.446 220.581 1.00 84.88 C
ANISOU 3571 C PHE B 199 13797 6295 12160 -298 1307 2349 C
ATOM 3572 O PHE B 199 24.742 -50.918 221.553 1.00 88.00 O
ANISOU 3572 O PHE B 199 14207 6834 12394 -363 1479 2534 O
ATOM 3573 CB PHE B 199 23.832 -53.472 220.859 1.00 86.62 C
ANISOU 3573 CB PHE B 199 14159 5913 12838 -714 1630 2492 C
ATOM 3574 CG PHE B 199 23.284 -54.736 220.256 1.00 84.87 C
ANISOU 3574 CG PHE B 199 13943 5329 12976 -933 1665 2382 C
ATOM 3575 CD1 PHE B 199 22.052 -54.740 219.627 1.00 90.64 C
ANISOU 3575 CD1 PHE B 199 14430 6003 14005 -1289 1756 2196 C
ATOM 3576 CD2 PHE B 199 24.009 -55.912 220.304 1.00 82.35 C
ANISOU 3576 CD2 PHE B 199 13852 4727 12709 -779 1584 2450 C
ATOM 3577 CE1 PHE B 199 21.549 -55.895 219.064 1.00 93.15 C
ANISOU 3577 CE1 PHE B 199 14753 5998 14643 -1497 1760 2072 C
ATOM 3578 CE2 PHE B 199 23.510 -57.076 219.744 1.00 92.64 C
ANISOU 3578 CE2 PHE B 199 15175 5685 14339 -982 1613 2337 C
ATOM 3579 CZ PHE B 199 22.278 -57.066 219.124 1.00 96.33 C
ANISOU 3579 CZ PHE B 199 15417 6107 15079 -1347 1698 2143 C
ATOM 3580 N SER B 200 26.488 -51.067 220.147 1.00 80.39 N
ANISOU 3580 N SER B 200 13202 5899 11444 -20 1055 2225 N
ATOM 3581 CA SER B 200 27.208 -49.935 220.715 1.00 73.37 C
ANISOU 3581 CA SER B 200 12263 5395 10220 202 931 2271 C
ATOM 3582 C SER B 200 26.804 -48.627 220.048 1.00 77.59 C
ANISOU 3582 C SER B 200 12463 6303 10714 90 859 2026 C
ATOM 3583 O SER B 200 26.392 -48.595 218.884 1.00 78.19 O
ANISOU 3583 O SER B 200 12349 6372 10988 -64 802 1774 O
ATOM 3584 CB SER B 200 28.721 -50.134 220.597 1.00 78.16 C
ANISOU 3584 CB SER B 200 12966 6003 10730 551 701 2254 C
ATOM 3585 OG SER B 200 29.163 -51.147 221.491 1.00 86.75 O
ANISOU 3585 OG SER B 200 14383 6794 11783 717 740 2542 O
ATOM 3586 N VAL B 201 26.947 -47.541 220.800 1.00 75.10 N
ANISOU 3586 N VAL B 201 12099 6308 10128 179 849 2101 N
ATOM 3587 CA VAL B 201 26.633 -46.202 220.322 1.00 67.29 C
ANISOU 3587 CA VAL B 201 10819 5669 9077 108 785 1904 C
ATOM 3588 C VAL B 201 27.719 -45.250 220.799 1.00 69.06 C
ANISOU 3588 C VAL B 201 11044 6189 9009 364 626 1913 C
ATOM 3589 O VAL B 201 28.152 -45.309 221.956 1.00 78.74 O
ANISOU 3589 O VAL B 201 12473 7428 10015 513 644 2126 O
ATOM 3590 CB VAL B 201 25.244 -45.738 220.811 1.00 68.60 C
ANISOU 3590 CB VAL B 201 10872 5906 9288 -141 1013 1965 C
ATOM 3591 CG1 VAL B 201 25.019 -44.271 220.476 1.00 67.39 C
ANISOU 3591 CG1 VAL B 201 10445 6114 9047 -159 937 1792 C
ATOM 3592 CG2 VAL B 201 24.159 -46.606 220.202 1.00 76.45 C
ANISOU 3592 CG2 VAL B 201 11793 6625 10630 -421 1140 1906 C
ATOM 3593 N CYS B 202 28.160 -44.380 219.894 1.00 70.11 N
ANISOU 3593 N CYS B 202 10957 6546 9134 408 464 1679 N
ATOM 3594 CA CYS B 202 29.108 -43.317 220.193 1.00 72.11 C
ANISOU 3594 CA CYS B 202 11145 7093 9162 602 318 1636 C
ATOM 3595 C CYS B 202 28.325 -42.017 220.303 1.00 71.85 C
ANISOU 3595 C CYS B 202 10926 7325 9049 470 384 1567 C
ATOM 3596 O CYS B 202 27.694 -41.587 219.333 1.00 66.70 O
ANISOU 3596 O CYS B 202 10075 6730 8539 319 381 1397 O
ATOM 3597 CB CYS B 202 30.172 -43.226 219.098 1.00 73.78 C
ANISOU 3597 CB CYS B 202 11243 7350 9441 736 134 1428 C
ATOM 3598 SG CYS B 202 31.413 -41.915 219.293 1.00 72.32 S
ANISOU 3598 SG CYS B 202 10923 7504 9053 945 -43 1336 S
ATOM 3599 N ASP B 203 28.344 -41.401 221.478 1.00 73.75 N
ANISOU 3599 N ASP B 203 11246 7717 9059 533 436 1696 N
ATOM 3600 CA ASP B 203 27.585 -40.170 221.645 1.00 69.46 C
ANISOU 3600 CA ASP B 203 10536 7401 8454 422 522 1625 C
ATOM 3601 C ASP B 203 28.182 -39.362 222.784 1.00 61.22 C
ANISOU 3601 C ASP B 203 9593 6562 7107 575 483 1694 C
ATOM 3602 O ASP B 203 29.031 -39.841 223.538 1.00 68.44 O
ANISOU 3602 O ASP B 203 10719 7435 7852 749 395 1824 O
ATOM 3603 CB ASP B 203 26.099 -40.449 221.894 1.00 81.55 C
ANISOU 3603 CB ASP B 203 12039 8822 10124 189 777 1705 C
ATOM 3604 CG ASP B 203 25.230 -39.234 221.621 1.00 95.41 C
ANISOU 3604 CG ASP B 203 13538 10780 11935 67 839 1572 C
ATOM 3605 OD1 ASP B 203 25.731 -38.279 220.992 1.00 95.59 O
ANISOU 3605 OD1 ASP B 203 13412 10987 11919 140 673 1408 O
ATOM 3606 OD2 ASP B 203 24.051 -39.227 222.039 1.00102.32 O
ANISOU 3606 OD2 ASP B 203 14355 11616 12907 -97 1065 1634 O
ATOM 3607 N GLU B 204 27.754 -38.108 222.864 1.00 58.09 N
ANISOU 3607 N GLU B 204 9040 6382 6649 517 526 1589 N
ATOM 3608 CA GLU B 204 28.170 -37.232 223.946 1.00 51.79 C
ANISOU 3608 CA GLU B 204 8334 5780 5564 630 506 1616 C
ATOM 3609 C GLU B 204 27.561 -37.692 225.267 1.00 58.70 C
ANISOU 3609 C GLU B 204 9467 6582 6252 604 722 1835 C
ATOM 3610 O GLU B 204 26.380 -38.050 225.336 1.00 64.15 O
ANISOU 3610 O GLU B 204 10143 7157 7072 427 975 1909 O
ATOM 3611 CB GLU B 204 27.751 -35.799 223.619 1.00 46.55 C
ANISOU 3611 CB GLU B 204 7440 5323 4924 561 528 1438 C
ATOM 3612 CG GLU B 204 28.117 -35.413 222.194 1.00 51.40 C
ANISOU 3612 CG GLU B 204 7822 5973 5734 547 369 1250 C
ATOM 3613 CD GLU B 204 27.667 -34.010 221.826 1.00 58.79 C
ANISOU 3613 CD GLU B 204 8553 7079 6706 485 388 1100 C
ATOM 3614 OE1 GLU B 204 26.923 -33.392 222.629 1.00 53.98 O
ANISOU 3614 OE1 GLU B 204 7950 6542 6016 439 547 1128 O
ATOM 3615 OE2 GLU B 204 28.060 -33.527 220.734 1.00 52.94 O
ANISOU 3615 OE2 GLU B 204 7659 6386 6071 490 259 958 O
ATOM 3616 N ARG B 205 28.370 -37.672 226.324 1.00 63.73 N
ANISOU 3616 N ARG B 205 10344 7289 6582 777 623 1937 N
ATOM 3617 CA ARG B 205 27.933 -38.054 227.665 1.00 70.11 C
ANISOU 3617 CA ARG B 205 11468 8046 7126 781 818 2159 C
ATOM 3618 C ARG B 205 28.047 -36.834 228.568 1.00 72.67 C
ANISOU 3618 C ARG B 205 11848 8620 7142 841 818 2083 C
ATOM 3619 O ARG B 205 29.156 -36.403 228.899 1.00 73.65 O
ANISOU 3619 O ARG B 205 12031 8886 7068 1017 548 2020 O
ATOM 3620 CB ARG B 205 28.758 -39.218 228.211 1.00 69.42 C
ANISOU 3620 CB ARG B 205 11688 7794 6896 952 684 2374 C
ATOM 3621 CG ARG B 205 28.262 -39.734 229.554 1.00 81.05 C
ANISOU 3621 CG ARG B 205 13544 9177 8076 950 909 2644 C
ATOM 3622 CD ARG B 205 29.028 -40.963 230.022 1.00 94.51 C
ANISOU 3622 CD ARG B 205 15532 10691 9687 1115 757 2860 C
ATOM 3623 NE ARG B 205 28.896 -42.087 229.100 1.00102.03 N
ANISOU 3623 NE ARG B 205 16440 11345 10981 1060 792 2925 N
ATOM 3624 CZ ARG B 205 29.200 -43.344 229.411 1.00114.59 C
ANISOU 3624 CZ ARG B 205 18200 12718 12623 1117 746 3086 C
ATOM 3625 NH1 ARG B 205 29.643 -43.636 230.626 1.00117.24 N
ANISOU 3625 NH1 ARG B 205 18762 13105 12677 1234 659 3222 N
ATOM 3626 NH2 ARG B 205 29.054 -44.310 228.512 1.00114.85 N
ANISOU 3626 NH2 ARG B 205 18183 12468 12986 1055 785 3107 N
ATOM 3627 N TRP B 206 26.905 -36.279 228.962 1.00 73.72 N
ANISOU 3627 N TRP B 206 11950 8803 7256 693 1121 2072 N
ATOM 3628 CA TRP B 206 26.853 -35.079 229.782 1.00 72.48 C
ANISOU 3628 CA TRP B 206 11845 8864 6831 730 1172 1970 C
ATOM 3629 C TRP B 206 26.478 -35.428 231.213 1.00 78.71 C
ANISOU 3629 C TRP B 206 13024 9627 7254 748 1406 2175 C
ATOM 3630 O TRP B 206 25.579 -36.240 231.449 1.00 93.77 O
ANISOU 3630 O TRP B 206 15039 11360 9232 623 1712 2358 O
ATOM 3631 CB TRP B 206 25.853 -34.077 229.210 1.00 67.73 C
ANISOU 3631 CB TRP B 206 10924 8341 6469 577 1358 1787 C
ATOM 3632 CG TRP B 206 26.225 -33.636 227.844 1.00 66.86 C
ANISOU 3632 CG TRP B 206 10482 8265 6655 567 1130 1598 C
ATOM 3633 CD1 TRP B 206 25.739 -34.119 226.664 1.00 66.00 C
ANISOU 3633 CD1 TRP B 206 10144 8031 6900 452 1136 1574 C
ATOM 3634 CD2 TRP B 206 27.186 -32.633 227.505 1.00 64.92 C
ANISOU 3634 CD2 TRP B 206 10117 8184 6365 672 866 1406 C
ATOM 3635 NE1 TRP B 206 26.333 -33.469 225.609 1.00 57.55 N
ANISOU 3635 NE1 TRP B 206 8848 7044 5972 488 903 1391 N
ATOM 3636 CE2 TRP B 206 27.224 -32.550 226.100 1.00 61.48 C
ANISOU 3636 CE2 TRP B 206 9400 7713 6248 617 751 1292 C
ATOM 3637 CE3 TRP B 206 28.009 -31.787 228.254 1.00 65.75 C
ANISOU 3637 CE3 TRP B 206 10331 8457 6192 796 717 1312 C
ATOM 3638 CZ2 TRP B 206 28.056 -31.659 225.428 1.00 63.29 C
ANISOU 3638 CZ2 TRP B 206 9461 8058 6527 678 532 1110 C
ATOM 3639 CZ3 TRP B 206 28.838 -30.908 227.588 1.00 59.86 C
ANISOU 3639 CZ3 TRP B 206 9388 7820 5536 845 484 1115 C
ATOM 3640 CH2 TRP B 206 28.856 -30.850 226.188 1.00 62.85 C
ANISOU 3640 CH2 TRP B 206 9494 8151 6237 785 412 1027 C
ATOM 3641 N ALA B 207 27.158 -34.791 232.165 1.00 82.12 N
ANISOU 3641 N ALA B 207 13677 10233 7293 893 1269 2136 N
ATOM 3642 CA ALA B 207 26.898 -35.030 233.578 1.00 81.20 C
ANISOU 3642 CA ALA B 207 13903 10128 6821 906 1432 2271 C
ATOM 3643 C ALA B 207 25.637 -34.335 234.078 1.00 85.65 C
ANISOU 3643 C ALA B 207 14435 10746 7361 753 1852 2207 C
ATOM 3644 O ALA B 207 25.181 -34.643 235.184 1.00 89.30 O
ANISOU 3644 O ALA B 207 15112 11191 7624 713 2050 2303 O
ATOM 3645 CB ALA B 207 28.100 -34.582 234.413 1.00 80.95 C
ANISOU 3645 CB ALA B 207 14032 10275 6452 1088 1069 2180 C
ATOM 3646 N ASP B 208 25.064 -33.418 233.299 1.00 85.09 N
ANISOU 3646 N ASP B 208 14077 10737 7515 672 1987 2039 N
ATOM 3647 CA ASP B 208 23.852 -32.720 233.708 1.00 86.16 C
ANISOU 3647 CA ASP B 208 14140 10917 7680 545 2400 1964 C
ATOM 3648 C ASP B 208 23.130 -32.213 232.466 1.00 78.45 C
ANISOU 3648 C ASP B 208 12671 9921 7215 416 2450 1794 C
ATOM 3649 O ASP B 208 23.644 -32.286 231.348 1.00 74.83 O
ANISOU 3649 O ASP B 208 11968 9441 7021 429 2152 1717 O
ATOM 3650 CB ASP B 208 24.166 -31.574 234.678 1.00 94.60 C
ANISOU 3650 CB ASP B 208 15342 12191 8410 635 2349 1776 C
ATOM 3651 CG ASP B 208 25.070 -30.524 234.068 1.00 98.08 C
ANISOU 3651 CG ASP B 208 15620 12780 8865 740 2007 1541 C
ATOM 3652 OD1 ASP B 208 24.584 -29.733 233.234 1.00 94.85 O
ANISOU 3652 OD1 ASP B 208 14844 12392 8804 663 2055 1361 O
ATOM 3653 OD2 ASP B 208 26.267 -30.488 234.425 1.00105.34 O
ANISOU 3653 OD2 ASP B 208 16726 13788 9510 889 1653 1518 O
ATOM 3654 N ASP B 209 21.903 -31.727 232.681 1.00 83.91 N
ANISOU 3654 N ASP B 209 13222 10614 8044 295 2839 1741 N
ATOM 3655 CA ASP B 209 21.069 -31.224 231.594 1.00 85.82 C
ANISOU 3655 CA ASP B 209 12997 10837 8775 182 2895 1591 C
ATOM 3656 C ASP B 209 21.483 -29.845 231.088 1.00 84.17 C
ANISOU 3656 C ASP B 209 12574 10782 8625 269 2664 1331 C
ATOM 3657 O ASP B 209 21.099 -29.473 229.974 1.00 83.74 O
ANISOU 3657 O ASP B 209 12154 10709 8955 214 2575 1220 O
ATOM 3658 CB ASP B 209 19.604 -31.163 232.040 1.00 96.17 C
ANISOU 3658 CB ASP B 209 14197 12091 10252 38 3396 1619 C
ATOM 3659 CG ASP B 209 19.072 -32.507 232.496 1.00110.51 C
ANISOU 3659 CG ASP B 209 16197 13724 12069 -87 3684 1881 C
ATOM 3660 OD1 ASP B 209 19.576 -33.544 232.016 1.00116.21 O
ANISOU 3660 OD1 ASP B 209 16984 14316 12853 -100 3475 2018 O
ATOM 3661 OD2 ASP B 209 18.145 -32.526 233.333 1.00116.59 O
ANISOU 3661 OD2 ASP B 209 16993 14475 12833 -173 4047 1903 O
ATOM 3662 N LEU B 210 22.237 -29.074 231.871 1.00 72.84 N
ANISOU 3662 N LEU B 210 11368 9488 6819 398 2560 1230 N
ATOM 3663 CA LEU B 210 22.528 -27.694 231.496 1.00 69.25 C
ANISOU 3663 CA LEU B 210 10724 9151 6437 459 2402 977 C
ATOM 3664 C LEU B 210 23.762 -27.563 230.612 1.00 67.62 C
ANISOU 3664 C LEU B 210 10421 8981 6290 534 1950 900 C
ATOM 3665 O LEU B 210 23.792 -26.708 229.713 1.00 70.18 O
ANISOU 3665 O LEU B 210 10467 9329 6868 529 1824 741 O
ATOM 3666 CB LEU B 210 22.702 -26.839 232.754 1.00 71.88 C
ANISOU 3666 CB LEU B 210 11336 9606 6369 543 2522 862 C
ATOM 3667 CG LEU B 210 22.958 -25.342 232.574 1.00 76.12 C
ANISOU 3667 CG LEU B 210 11727 10240 6955 600 2410 586 C
ATOM 3668 CD1 LEU B 210 21.867 -24.715 231.728 1.00 74.63 C
ANISOU 3668 CD1 LEU B 210 11142 9990 7226 528 2590 495 C
ATOM 3669 CD2 LEU B 210 23.037 -24.653 233.930 1.00 75.55 C
ANISOU 3669 CD2 LEU B 210 11982 10268 6457 668 2565 470 C
ATOM 3670 N ALA B 211 24.791 -28.366 230.879 1.00 67.79 N
ANISOU 3670 N ALA B 211 10674 9003 6082 612 1716 1014 N
ATOM 3671 CA ALA B 211 26.023 -28.276 230.099 1.00 60.19 C
ANISOU 3671 CA ALA B 211 9608 8076 5187 688 1315 934 C
ATOM 3672 C ALA B 211 25.797 -28.525 228.619 1.00 66.78 C
ANISOU 3672 C ALA B 211 10117 8819 6438 611 1235 924 C
ATOM 3673 O ALA B 211 26.342 -27.764 227.802 1.00 67.52 O
ANISOU 3673 O ALA B 211 10016 8962 6678 633 1035 770 O
ATOM 3674 CB ALA B 211 27.068 -29.241 230.665 1.00 58.27 C
ANISOU 3674 CB ALA B 211 9649 7827 4665 800 1095 1078 C
ATOM 3675 N PRO B 212 25.082 -29.574 228.197 1.00 67.81 N
ANISOU 3675 N PRO B 212 10194 8809 6761 518 1367 1077 N
ATOM 3676 CA PRO B 212 24.833 -29.731 226.754 1.00 56.57 C
ANISOU 3676 CA PRO B 212 8474 7310 5712 442 1268 1034 C
ATOM 3677 C PRO B 212 24.099 -28.554 226.137 1.00 52.66 C
ANISOU 3677 C PRO B 212 7699 6863 5446 391 1333 875 C
ATOM 3678 O PRO B 212 24.418 -28.157 225.009 1.00 60.46 O
ANISOU 3678 O PRO B 212 8497 7857 6618 394 1138 779 O
ATOM 3679 CB PRO B 212 24.002 -31.025 226.681 1.00 58.05 C
ANISOU 3679 CB PRO B 212 8682 7330 6044 328 1449 1213 C
ATOM 3680 CG PRO B 212 23.450 -31.207 228.060 1.00 57.76 C
ANISOU 3680 CG PRO B 212 8886 7291 5770 314 1749 1332 C
ATOM 3681 CD PRO B 212 24.484 -30.661 228.987 1.00 65.55 C
ANISOU 3681 CD PRO B 212 10129 8416 6363 468 1610 1290 C
ATOM 3682 N LYS B 213 23.164 -27.941 226.862 1.00 54.26 N
ANISOU 3682 N LYS B 213 7888 7097 5631 360 1607 845 N
ATOM 3683 CA LYS B 213 22.447 -26.809 226.287 1.00 63.74 C
ANISOU 3683 CA LYS B 213 8816 8325 7080 338 1661 700 C
ATOM 3684 C LYS B 213 23.379 -25.623 226.088 1.00 59.38 C
ANISOU 3684 C LYS B 213 8258 7866 6438 435 1450 534 C
ATOM 3685 O LYS B 213 23.403 -25.013 225.008 1.00 63.09 O
ANISOU 3685 O LYS B 213 8518 8325 7129 433 1305 450 O
ATOM 3686 CB LYS B 213 21.262 -26.426 227.174 1.00 72.61 C
ANISOU 3686 CB LYS B 213 9917 9449 8221 301 2031 691 C
ATOM 3687 CG LYS B 213 20.243 -27.535 227.357 1.00 74.42 C
ANISOU 3687 CG LYS B 213 10109 9570 8595 176 2289 849 C
ATOM 3688 CD LYS B 213 19.018 -27.054 228.119 1.00 74.19 C
ANISOU 3688 CD LYS B 213 9995 9544 8651 134 2691 818 C
ATOM 3689 CE LYS B 213 17.969 -28.153 228.214 1.00 78.53 C
ANISOU 3689 CE LYS B 213 10456 9969 9413 -20 2967 968 C
ATOM 3690 NZ LYS B 213 16.708 -27.667 228.830 1.00 84.38 N
ANISOU 3690 NZ LYS B 213 11038 10708 10316 -69 3386 922 N
ATOM 3691 N ILE B 214 24.195 -25.318 227.098 1.00 53.99 N
ANISOU 3691 N ILE B 214 7818 7268 5427 515 1414 488 N
ATOM 3692 CA ILE B 214 25.132 -24.207 226.960 1.00 59.78 C
ANISOU 3692 CA ILE B 214 8540 8077 6099 585 1212 314 C
ATOM 3693 C ILE B 214 26.143 -24.501 225.860 1.00 52.93 C
ANISOU 3693 C ILE B 214 7576 7194 5340 596 915 316 C
ATOM 3694 O ILE B 214 26.416 -23.653 224.997 1.00 57.80 O
ANISOU 3694 O ILE B 214 8030 7809 6123 594 802 206 O
ATOM 3695 CB ILE B 214 25.837 -23.919 228.297 1.00 58.38 C
ANISOU 3695 CB ILE B 214 8646 7996 5538 660 1195 249 C
ATOM 3696 CG1 ILE B 214 24.840 -23.424 229.345 1.00 59.04 C
ANISOU 3696 CG1 ILE B 214 8838 8097 5499 653 1527 206 C
ATOM 3697 CG2 ILE B 214 26.956 -22.892 228.096 1.00 57.79 C
ANISOU 3697 CG2 ILE B 214 8538 7985 5436 709 945 59 C
ATOM 3698 CD1 ILE B 214 25.492 -23.056 230.661 1.00 64.76 C
ANISOU 3698 CD1 ILE B 214 9878 8922 5804 727 1502 114 C
ATOM 3699 N TYR B 215 26.701 -25.713 225.861 1.00 56.43 N
ANISOU 3699 N TYR B 215 8131 7613 5698 611 805 445 N
ATOM 3700 CA TYR B 215 27.743 -26.032 224.897 1.00 51.26 C
ANISOU 3700 CA TYR B 215 7397 6945 5134 636 550 431 C
ATOM 3701 C TYR B 215 27.209 -25.991 223.480 1.00 57.32 C
ANISOU 3701 C TYR B 215 7937 7638 6202 564 541 426 C
ATOM 3702 O TYR B 215 27.872 -25.469 222.583 1.00 59.70 O
ANISOU 3702 O TYR B 215 8131 7951 6602 574 393 338 O
ATOM 3703 CB TYR B 215 28.348 -27.403 225.184 1.00 52.51 C
ANISOU 3703 CB TYR B 215 7717 7064 5171 684 454 575 C
ATOM 3704 CG TYR B 215 29.287 -27.859 224.092 1.00 53.83 C
ANISOU 3704 CG TYR B 215 7778 7194 5479 711 241 559 C
ATOM 3705 CD1 TYR B 215 30.625 -27.471 224.093 1.00 56.49 C
ANISOU 3705 CD1 TYR B 215 8101 7607 5754 796 27 455 C
ATOM 3706 CD2 TYR B 215 28.835 -28.654 223.044 1.00 51.37 C
ANISOU 3706 CD2 TYR B 215 7372 6770 5377 647 262 627 C
ATOM 3707 CE1 TYR B 215 31.492 -27.878 223.094 1.00 46.86 C
ANISOU 3707 CE1 TYR B 215 6772 6352 4680 823 -122 430 C
ATOM 3708 CE2 TYR B 215 29.692 -29.065 222.038 1.00 51.24 C
ANISOU 3708 CE2 TYR B 215 7281 6717 5471 676 100 594 C
ATOM 3709 CZ TYR B 215 31.018 -28.675 222.065 1.00 52.96 C
ANISOU 3709 CZ TYR B 215 7483 7012 5629 768 -73 500 C
ATOM 3710 OH TYR B 215 31.864 -29.083 221.056 1.00 50.14 O
ANISOU 3710 OH TYR B 215 7040 6615 5398 798 -190 460 O
ATOM 3711 N HIS B 216 26.013 -26.521 223.249 1.00 55.34 N
ANISOU 3711 N HIS B 216 7616 7311 6101 485 697 515 N
ATOM 3712 CA HIS B 216 25.535 -26.547 221.878 1.00 47.21 C
ANISOU 3712 CA HIS B 216 6387 6216 5332 423 634 502 C
ATOM 3713 C HIS B 216 25.012 -25.189 221.430 1.00 50.42 C
ANISOU 3713 C HIS B 216 6630 6649 5878 422 658 395 C
ATOM 3714 O HIS B 216 25.147 -24.849 220.249 1.00 51.94 O
ANISOU 3714 O HIS B 216 6712 6819 6204 413 524 356 O
ATOM 3715 CB HIS B 216 24.507 -27.662 221.712 1.00 51.73 C
ANISOU 3715 CB HIS B 216 6919 6688 6049 328 745 618 C
ATOM 3716 CG HIS B 216 25.132 -29.017 221.588 1.00 54.02 C
ANISOU 3716 CG HIS B 216 7341 6901 6284 327 658 714 C
ATOM 3717 ND1 HIS B 216 25.646 -29.491 220.400 1.00 52.85 N
ANISOU 3717 ND1 HIS B 216 7146 6700 6236 321 480 686 N
ATOM 3718 CD2 HIS B 216 25.361 -29.983 222.509 1.00 53.70 C
ANISOU 3718 CD2 HIS B 216 7500 6813 6090 346 729 837 C
ATOM 3719 CE1 HIS B 216 26.138 -30.702 220.591 1.00 53.81 C
ANISOU 3719 CE1 HIS B 216 7409 6736 6299 338 450 776 C
ATOM 3720 NE2 HIS B 216 25.988 -31.020 221.862 1.00 56.85 N
ANISOU 3720 NE2 HIS B 216 7949 7119 6532 357 588 880 N
ATOM 3721 N SER B 217 24.500 -24.360 222.345 1.00 52.45 N
ANISOU 3721 N SER B 217 6895 6945 6087 445 824 343 N
ATOM 3722 CA SER B 217 24.242 -22.975 221.968 1.00 48.71 C
ANISOU 3722 CA SER B 217 6295 6477 5737 475 824 230 C
ATOM 3723 C SER B 217 25.531 -22.301 221.505 1.00 55.06 C
ANISOU 3723 C SER B 217 7142 7309 6471 515 635 141 C
ATOM 3724 O SER B 217 25.571 -21.678 220.433 1.00 53.56 O
ANISOU 3724 O SER B 217 6844 7080 6428 513 540 111 O
ATOM 3725 CB SER B 217 23.620 -22.212 223.140 1.00 49.27 C
ANISOU 3725 CB SER B 217 6399 6575 5747 506 1050 162 C
ATOM 3726 OG SER B 217 22.392 -22.796 223.541 1.00 56.50 O
ANISOU 3726 OG SER B 217 7245 7458 6763 457 1271 242 O
ATOM 3727 N CYS B 218 26.610 -22.445 222.288 1.00 55.38 N
ANISOU 3727 N CYS B 218 7339 7413 6289 551 574 103 N
ATOM 3728 CA CYS B 218 27.876 -21.823 221.903 1.00 51.28 C
ANISOU 3728 CA CYS B 218 6823 6919 5742 574 407 2 C
ATOM 3729 C CYS B 218 28.404 -22.401 220.598 1.00 51.72 C
ANISOU 3729 C CYS B 218 6809 6937 5905 551 269 55 C
ATOM 3730 O CYS B 218 28.943 -21.670 219.758 1.00 48.17 O
ANISOU 3730 O CYS B 218 6293 6466 5545 541 199 -8 O
ATOM 3731 CB CYS B 218 28.916 -21.997 223.011 1.00 39.51 C
ANISOU 3731 CB CYS B 218 5488 5512 4013 620 329 -52 C
ATOM 3732 SG CYS B 218 28.545 -21.130 224.559 1.00 59.43 S
ANISOU 3732 SG CYS B 218 8152 8091 6337 651 470 -167 S
ATOM 3733 N PHE B 219 28.245 -23.709 220.400 1.00 48.32 N
ANISOU 3733 N PHE B 219 6408 6483 5467 538 250 166 N
ATOM 3734 CA PHE B 219 28.780 -24.339 219.201 1.00 45.51 C
ANISOU 3734 CA PHE B 219 6016 6087 5191 523 133 194 C
ATOM 3735 C PHE B 219 28.062 -23.828 217.965 1.00 47.55 C
ANISOU 3735 C PHE B 219 6164 6290 5615 477 129 194 C
ATOM 3736 O PHE B 219 28.695 -23.525 216.944 1.00 47.79 O
ANISOU 3736 O PHE B 219 6173 6303 5681 473 50 160 O
ATOM 3737 CB PHE B 219 28.653 -25.860 219.322 1.00 43.60 C
ANISOU 3737 CB PHE B 219 5846 5800 4918 518 127 303 C
ATOM 3738 CG PHE B 219 29.303 -26.619 218.202 1.00 46.46 C
ANISOU 3738 CG PHE B 219 6199 6111 5341 517 19 308 C
ATOM 3739 CD1 PHE B 219 28.638 -26.815 217.004 1.00 46.56 C
ANISOU 3739 CD1 PHE B 219 6149 6060 5482 454 4 320 C
ATOM 3740 CD2 PHE B 219 30.577 -27.143 218.351 1.00 52.52 C
ANISOU 3740 CD2 PHE B 219 7021 6896 6039 587 -73 290 C
ATOM 3741 CE1 PHE B 219 29.234 -27.520 215.973 1.00 49.25 C
ANISOU 3741 CE1 PHE B 219 6513 6350 5848 453 -76 304 C
ATOM 3742 CE2 PHE B 219 31.178 -27.848 217.322 1.00 49.50 C
ANISOU 3742 CE2 PHE B 219 6629 6456 5723 596 -137 277 C
ATOM 3743 CZ PHE B 219 30.506 -28.033 216.134 1.00 46.91 C
ANISOU 3743 CZ PHE B 219 6270 6062 5492 525 -125 280 C
ATOM 3744 N PHE B 220 26.741 -23.668 218.062 1.00 46.14 N
ANISOU 3744 N PHE B 220 5913 6083 5537 449 217 233 N
ATOM 3745 CA PHE B 220 25.974 -23.150 216.938 1.00 39.21 C
ANISOU 3745 CA PHE B 220 4924 5155 4818 427 173 240 C
ATOM 3746 C PHE B 220 26.345 -21.701 216.652 1.00 42.61 C
ANISOU 3746 C PHE B 220 5339 5581 5271 465 161 170 C
ATOM 3747 O PHE B 220 26.551 -21.322 215.492 1.00 48.73 O
ANISOU 3747 O PHE B 220 6109 6317 6088 460 72 177 O
ATOM 3748 CB PHE B 220 24.480 -23.293 217.236 1.00 42.21 C
ANISOU 3748 CB PHE B 220 5186 5509 5343 399 267 284 C
ATOM 3749 CG PHE B 220 23.589 -22.622 216.236 1.00 46.49 C
ANISOU 3749 CG PHE B 220 5590 6007 6068 404 192 288 C
ATOM 3750 CD1 PHE B 220 23.513 -23.085 214.930 1.00 47.88 C
ANISOU 3750 CD1 PHE B 220 5757 6149 6287 371 24 316 C
ATOM 3751 CD2 PHE B 220 22.792 -21.554 216.614 1.00 45.53 C
ANISOU 3751 CD2 PHE B 220 5357 5872 6071 453 281 260 C
ATOM 3752 CE1 PHE B 220 22.682 -22.472 214.009 1.00 53.69 C
ANISOU 3752 CE1 PHE B 220 6385 6849 7165 391 -87 330 C
ATOM 3753 CE2 PHE B 220 21.954 -20.935 215.698 1.00 52.43 C
ANISOU 3753 CE2 PHE B 220 6097 6697 7128 484 182 277 C
ATOM 3754 CZ PHE B 220 21.900 -21.396 214.392 1.00 50.72 C
ANISOU 3754 CZ PHE B 220 5883 6458 6933 454 -19 319 C
ATOM 3755 N ILE B 221 26.468 -20.876 217.699 1.00 46.68 N
ANISOU 3755 N ILE B 221 5871 6122 5743 498 257 100 N
ATOM 3756 CA ILE B 221 26.771 -19.462 217.473 1.00 45.51 C
ANISOU 3756 CA ILE B 221 5711 5934 5646 523 261 26 C
ATOM 3757 C ILE B 221 28.168 -19.295 216.885 1.00 52.99 C
ANISOU 3757 C ILE B 221 6716 6883 6533 501 176 -15 C
ATOM 3758 O ILE B 221 28.389 -18.468 215.990 1.00 53.65 O
ANISOU 3758 O ILE B 221 6796 6900 6688 494 153 -17 O
ATOM 3759 CB ILE B 221 26.620 -18.659 218.778 1.00 47.93 C
ANISOU 3759 CB ILE B 221 6039 6257 5914 556 388 -72 C
ATOM 3760 CG1 ILE B 221 25.154 -18.620 219.223 1.00 48.88 C
ANISOU 3760 CG1 ILE B 221 6071 6357 6144 582 523 -42 C
ATOM 3761 CG2 ILE B 221 27.197 -17.259 218.605 1.00 45.49 C
ANISOU 3761 CG2 ILE B 221 5742 5883 5657 566 386 -172 C
ATOM 3762 CD1 ILE B 221 24.226 -18.042 218.193 1.00 61.01 C
ANISOU 3762 CD1 ILE B 221 7472 7806 7901 610 485 8 C
ATOM 3763 N VAL B 222 29.126 -20.098 217.351 1.00 49.63 N
ANISOU 3763 N VAL B 222 6344 6525 5989 495 136 -39 N
ATOM 3764 CA VAL B 222 30.519 -19.858 216.992 1.00 54.40 C
ANISOU 3764 CA VAL B 222 6958 7138 6573 478 79 -107 C
ATOM 3765 C VAL B 222 30.892 -20.498 215.654 1.00 55.30 C
ANISOU 3765 C VAL B 222 7075 7223 6712 455 31 -46 C
ATOM 3766 O VAL B 222 31.692 -19.930 214.900 1.00 46.98 O
ANISOU 3766 O VAL B 222 6017 6136 5698 427 40 -82 O
ATOM 3767 CB VAL B 222 31.433 -20.350 218.125 1.00 51.65 C
ANISOU 3767 CB VAL B 222 6642 6876 6105 503 31 -174 C
ATOM 3768 CG1 VAL B 222 32.873 -20.395 217.660 1.00 44.83 C
ANISOU 3768 CG1 VAL B 222 5736 6028 5270 489 -40 -240 C
ATOM 3769 CG2 VAL B 222 31.288 -19.442 219.349 1.00 49.20 C
ANISOU 3769 CG2 VAL B 222 6362 6592 5738 516 75 -278 C
ATOM 3770 N THR B 223 30.355 -21.679 215.335 1.00 44.94 N
ANISOU 3770 N THR B 223 5784 5914 5379 460 -3 35 N
ATOM 3771 CA THR B 223 30.691 -22.340 214.083 1.00 43.28 C
ANISOU 3771 CA THR B 223 5605 5671 5168 441 -46 67 C
ATOM 3772 C THR B 223 29.709 -22.056 212.955 1.00 42.11 C
ANISOU 3772 C THR B 223 5473 5465 5063 418 -75 130 C
ATOM 3773 O THR B 223 29.965 -22.476 211.821 1.00 51.00 O
ANISOU 3773 O THR B 223 6662 6563 6153 400 -111 145 O
ATOM 3774 CB THR B 223 30.793 -23.859 214.286 1.00 51.40 C
ANISOU 3774 CB THR B 223 6667 6711 6153 457 -85 99 C
ATOM 3775 OG1 THR B 223 29.495 -24.392 214.544 1.00 50.04 O
ANISOU 3775 OG1 THR B 223 6488 6515 6009 438 -84 170 O
ATOM 3776 CG2 THR B 223 31.694 -24.176 215.470 1.00 52.28 C
ANISOU 3776 CG2 THR B 223 6777 6879 6206 506 -95 59 C
ATOM 3777 N TYR B 224 28.607 -21.359 213.217 1.00 53.59 N
ANISOU 3777 N TYR B 224 6874 6897 6590 428 -67 161 N
ATOM 3778 CA TYR B 224 27.638 -21.155 212.146 1.00 44.74 C
ANISOU 3778 CA TYR B 224 5753 5725 5522 426 -145 226 C
ATOM 3779 C TYR B 224 27.059 -19.745 212.117 1.00 49.00 C
ANISOU 3779 C TYR B 224 6254 6211 6153 466 -128 243 C
ATOM 3780 O TYR B 224 27.306 -18.988 211.173 1.00 55.05 O
ANISOU 3780 O TYR B 224 7094 6918 6903 474 -155 276 O
ATOM 3781 CB TYR B 224 26.502 -22.178 212.254 1.00 39.98 C
ANISOU 3781 CB TYR B 224 5083 5127 4979 406 -202 265 C
ATOM 3782 CG TYR B 224 25.548 -22.118 211.078 1.00 49.38 C
ANISOU 3782 CG TYR B 224 6259 6276 6225 402 -342 314 C
ATOM 3783 CD1 TYR B 224 25.758 -22.902 209.947 1.00 42.09 C
ANISOU 3783 CD1 TYR B 224 5440 5340 5213 367 -451 315 C
ATOM 3784 CD2 TYR B 224 24.456 -21.256 211.087 1.00 47.59 C
ANISOU 3784 CD2 TYR B 224 5922 6022 6139 445 -378 349 C
ATOM 3785 CE1 TYR B 224 24.894 -22.835 208.865 1.00 42.80 C
ANISOU 3785 CE1 TYR B 224 5540 5401 5321 367 -620 349 C
ATOM 3786 CE2 TYR B 224 23.593 -21.185 210.014 1.00 52.19 C
ANISOU 3786 CE2 TYR B 224 6484 6573 6774 458 -554 395 C
ATOM 3787 CZ TYR B 224 23.818 -21.975 208.906 1.00 55.41 C
ANISOU 3787 CZ TYR B 224 7013 6979 7060 415 -688 395 C
ATOM 3788 OH TYR B 224 22.958 -21.907 207.839 1.00 58.94 O
ANISOU 3788 OH TYR B 224 7461 7404 7531 431 -902 430 O
ATOM 3789 N LEU B 225 26.268 -19.384 213.125 1.00 47.55 N
ANISOU 3789 N LEU B 225 5968 6032 6066 496 -67 227 N
ATOM 3790 CA LEU B 225 25.451 -18.179 212.999 1.00 48.69 C
ANISOU 3790 CA LEU B 225 6054 6104 6343 556 -63 249 C
ATOM 3791 C LEU B 225 26.310 -16.920 212.934 1.00 44.04 C
ANISOU 3791 C LEU B 225 5545 5446 5743 567 0 211 C
ATOM 3792 O LEU B 225 26.180 -16.117 212.003 1.00 49.03 O
ANISOU 3792 O LEU B 225 6231 5985 6412 598 -49 275 O
ATOM 3793 CB LEU B 225 24.452 -18.090 214.154 1.00 52.13 C
ANISOU 3793 CB LEU B 225 6356 6555 6895 590 36 217 C
ATOM 3794 CG LEU B 225 23.437 -16.950 214.048 1.00 52.11 C
ANISOU 3794 CG LEU B 225 6253 6466 7081 676 43 233 C
ATOM 3795 CD1 LEU B 225 22.558 -17.107 212.812 1.00 47.28 C
ANISOU 3795 CD1 LEU B 225 5579 5818 6568 706 -143 332 C
ATOM 3796 CD2 LEU B 225 22.582 -16.874 215.309 1.00 50.16 C
ANISOU 3796 CD2 LEU B 225 5877 6239 6944 707 205 175 C
ATOM 3797 N ALA B 226 27.185 -16.715 213.924 1.00 47.81 N
ANISOU 3797 N ALA B 226 6039 5956 6171 541 101 108 N
ATOM 3798 CA ALA B 226 27.964 -15.477 213.941 1.00 51.84 C
ANISOU 3798 CA ALA B 226 6603 6382 6714 529 166 48 C
ATOM 3799 C ALA B 226 28.890 -15.329 212.742 1.00 44.22 C
ANISOU 3799 C ALA B 226 5733 5368 5699 479 146 96 C
ATOM 3800 O ALA B 226 28.846 -14.277 212.080 1.00 52.22 O
ANISOU 3800 O ALA B 226 6809 6255 6777 490 169 146 O
ATOM 3801 CB ALA B 226 28.757 -15.379 215.248 1.00 44.19 C
ANISOU 3801 CB ALA B 226 5625 5472 5694 500 238 -96 C
ATOM 3802 N PRO B 227 29.756 -16.294 212.422 1.00 50.87 N
ANISOU 3802 N PRO B 227 6602 6289 6437 428 126 86 N
ATOM 3803 CA PRO B 227 30.629 -16.104 211.251 1.00 53.91 C
ANISOU 3803 CA PRO B 227 7084 6622 6778 379 158 124 C
ATOM 3804 C PRO B 227 29.872 -15.934 209.949 1.00 56.34 C
ANISOU 3804 C PRO B 227 7501 6857 7046 412 91 263 C
ATOM 3805 O PRO B 227 30.260 -15.102 209.121 1.00 57.53 O
ANISOU 3805 O PRO B 227 7767 6905 7188 391 150 321 O
ATOM 3806 CB PRO B 227 31.504 -17.372 211.247 1.00 50.49 C
ANISOU 3806 CB PRO B 227 6634 6293 6256 347 149 76 C
ATOM 3807 CG PRO B 227 30.818 -18.347 212.157 1.00 44.74 C
ANISOU 3807 CG PRO B 227 5837 5654 5507 387 76 65 C
ATOM 3808 CD PRO B 227 30.066 -17.527 213.162 1.00 49.02 C
ANISOU 3808 CD PRO B 227 6321 6176 6127 421 100 36 C
ATOM 3809 N LEU B 228 28.766 -16.660 209.763 1.00 56.90 N
ANISOU 3809 N LEU B 228 7545 6973 7100 460 -38 320 N
ATOM 3810 CA LEU B 228 28.025 -16.538 208.513 1.00 56.00 C
ANISOU 3810 CA LEU B 228 7537 6804 6935 499 -159 441 C
ATOM 3811 C LEU B 228 27.262 -15.224 208.430 1.00 54.28 C
ANISOU 3811 C LEU B 228 7322 6466 6837 576 -184 516 C
ATOM 3812 O LEU B 228 27.140 -14.654 207.343 1.00 57.04 O
ANISOU 3812 O LEU B 228 7823 6725 7125 607 -240 630 O
ATOM 3813 CB LEU B 228 27.072 -17.718 208.341 1.00 57.21 C
ANISOU 3813 CB LEU B 228 7632 7035 7071 513 -314 455 C
ATOM 3814 CG LEU B 228 27.767 -19.052 208.077 1.00 53.87 C
ANISOU 3814 CG LEU B 228 7260 6688 6520 451 -309 402 C
ATOM 3815 CD1 LEU B 228 26.756 -20.180 208.091 1.00 55.92 C
ANISOU 3815 CD1 LEU B 228 7443 6996 6810 447 -450 400 C
ATOM 3816 CD2 LEU B 228 28.518 -19.028 206.752 1.00 55.47 C
ANISOU 3816 CD2 LEU B 228 7668 6858 6550 425 -292 436 C
ATOM 3817 N GLY B 229 26.761 -14.711 209.554 1.00 49.10 N
ANISOU 3817 N GLY B 229 6521 5793 6341 617 -134 457 N
ATOM 3818 CA GLY B 229 26.122 -13.407 209.517 1.00 48.23 C
ANISOU 3818 CA GLY B 229 6411 5540 6374 705 -134 513 C
ATOM 3819 C GLY B 229 27.116 -12.287 209.270 1.00 54.72 C
ANISOU 3819 C GLY B 229 7372 6225 7195 664 -1 520 C
ATOM 3820 O GLY B 229 26.856 -11.368 208.479 1.00 57.28 O
ANISOU 3820 O GLY B 229 7818 6398 7547 722 -30 642 O
ATOM 3821 N LEU B 230 28.286 -12.365 209.907 1.00 50.82 N
ANISOU 3821 N LEU B 230 6864 5770 6674 561 139 396 N
ATOM 3822 CA LEU B 230 29.316 -11.372 209.631 1.00 50.91 C
ANISOU 3822 CA LEU B 230 6982 5646 6715 489 279 387 C
ATOM 3823 C LEU B 230 29.777 -11.454 208.182 1.00 53.29 C
ANISOU 3823 C LEU B 230 7473 5901 6873 453 287 526 C
ATOM 3824 O LEU B 230 29.997 -10.424 207.533 1.00 61.57 O
ANISOU 3824 O LEU B 230 8670 6775 7948 444 366 623 O
ATOM 3825 CB LEU B 230 30.493 -11.565 210.586 1.00 51.47 C
ANISOU 3825 CB LEU B 230 6961 5791 6803 381 389 208 C
ATOM 3826 CG LEU B 230 30.206 -11.138 212.023 1.00 52.03 C
ANISOU 3826 CG LEU B 230 6913 5868 6986 406 413 58 C
ATOM 3827 CD1 LEU B 230 31.281 -11.639 212.964 1.00 45.84 C
ANISOU 3827 CD1 LEU B 230 6044 5209 6165 320 443 -113 C
ATOM 3828 CD2 LEU B 230 30.095 -9.609 212.083 1.00 42.47 C
ANISOU 3828 CD2 LEU B 230 5759 4438 5939 417 503 47 C
ATOM 3829 N MET B 231 29.890 -12.675 207.645 1.00 52.66 N
ANISOU 3829 N MET B 231 7416 5961 6630 435 216 542 N
ATOM 3830 CA MET B 231 30.275 -12.843 206.248 1.00 60.62 C
ANISOU 3830 CA MET B 231 8636 6938 7458 407 233 659 C
ATOM 3831 C MET B 231 29.209 -12.296 205.309 1.00 61.93 C
ANISOU 3831 C MET B 231 8962 7002 7566 514 82 841 C
ATOM 3832 O MET B 231 29.531 -11.676 204.288 1.00 66.86 O
ANISOU 3832 O MET B 231 9818 7506 8080 504 145 973 O
ATOM 3833 CB MET B 231 30.529 -14.321 205.953 1.00 59.31 C
ANISOU 3833 CB MET B 231 8459 6935 7140 378 180 606 C
ATOM 3834 CG MET B 231 31.861 -14.851 206.454 1.00 48.45 C
ANISOU 3834 CG MET B 231 6987 5636 5787 282 338 465 C
ATOM 3835 SD MET B 231 32.177 -16.519 205.858 1.00 59.48 S
ANISOU 3835 SD MET B 231 8421 7169 7009 270 296 422 S
ATOM 3836 CE MET B 231 31.793 -17.517 207.295 1.00 49.49 C
ANISOU 3836 CE MET B 231 6923 6031 5848 303 182 308 C
ATOM 3837 N ALA B 232 27.934 -12.502 205.645 1.00 55.68 N
ANISOU 3837 N ALA B 232 8048 6251 6855 622 -116 856 N
ATOM 3838 CA ALA B 232 26.870 -11.971 204.805 1.00 53.38 C
ANISOU 3838 CA ALA B 232 7869 5867 6546 747 -306 1021 C
ATOM 3839 C ALA B 232 26.924 -10.455 204.766 1.00 59.88 C
ANISOU 3839 C ALA B 232 8792 6471 7491 797 -211 1117 C
ATOM 3840 O ALA B 232 26.815 -9.848 203.694 1.00 64.89 O
ANISOU 3840 O ALA B 232 9667 6976 8010 851 -264 1296 O
ATOM 3841 CB ALA B 232 25.509 -12.447 205.316 1.00 50.48 C
ANISOU 3841 CB ALA B 232 7278 5582 6321 846 -515 991 C
ATOM 3842 N MET B 233 27.119 -9.819 205.924 1.00 62.36 N
ANISOU 3842 N MET B 233 8948 6723 8021 779 -68 1001 N
ATOM 3843 CA MET B 233 27.187 -8.361 205.927 1.00 62.03 C
ANISOU 3843 CA MET B 233 9005 6439 8125 818 36 1072 C
ATOM 3844 C MET B 233 28.430 -7.859 205.198 1.00 65.20 C
ANISOU 3844 C MET B 233 9639 6718 8415 691 238 1140 C
ATOM 3845 O MET B 233 28.369 -6.861 204.459 1.00 63.88 O
ANISOU 3845 O MET B 233 9689 6336 8245 736 269 1313 O
ATOM 3846 CB MET B 233 27.136 -7.851 207.361 1.00 61.61 C
ANISOU 3846 CB MET B 233 8744 6350 8313 816 148 893 C
ATOM 3847 CG MET B 233 25.784 -8.117 208.012 1.00 62.02 C
ANISOU 3847 CG MET B 233 8586 6475 8505 959 -1 854 C
ATOM 3848 SD MET B 233 25.670 -7.484 209.692 1.00 68.06 S
ANISOU 3848 SD MET B 233 9157 7194 9509 968 163 634 S
ATOM 3849 CE MET B 233 26.696 -8.677 210.559 1.00 56.46 C
ANISOU 3849 CE MET B 233 7595 5969 7889 796 250 443 C
ATOM 3850 N ALA B 234 29.553 -8.564 205.349 1.00 63.89 N
ANISOU 3850 N ALA B 234 9434 6680 8163 537 382 1018 N
ATOM 3851 CA ALA B 234 30.770 -8.154 204.661 1.00 56.38 C
ANISOU 3851 CA ALA B 234 8663 5622 7138 400 612 1066 C
ATOM 3852 C ALA B 234 30.578 -8.208 203.154 1.00 64.48 C
ANISOU 3852 C ALA B 234 9998 6598 7903 444 563 1291 C
ATOM 3853 O ALA B 234 30.935 -7.268 202.433 1.00 64.14 O
ANISOU 3853 O ALA B 234 10195 6348 7827 416 707 1446 O
ATOM 3854 CB ALA B 234 31.938 -9.045 205.085 1.00 48.03 C
ANISOU 3854 CB ALA B 234 7458 4733 6057 253 746 882 C
ATOM 3855 N TYR B 235 29.999 -9.304 202.659 1.00 62.11 N
ANISOU 3855 N TYR B 235 9720 6477 7404 510 359 1313 N
ATOM 3856 CA TYR B 235 29.787 -9.425 201.221 1.00 60.70 C
ANISOU 3856 CA TYR B 235 9864 6271 6929 556 278 1506 C
ATOM 3857 C TYR B 235 28.693 -8.491 200.721 1.00 60.49 C
ANISOU 3857 C TYR B 235 9998 6077 6909 726 76 1718 C
ATOM 3858 O TYR B 235 28.730 -8.075 199.561 1.00 71.32 O
ANISOU 3858 O TYR B 235 11711 7336 8052 758 74 1922 O
ATOM 3859 CB TYR B 235 29.503 -10.881 200.848 1.00 60.41 C
ANISOU 3859 CB TYR B 235 9807 6462 6686 567 104 1435 C
ATOM 3860 CG TYR B 235 30.769 -11.714 200.844 1.00 59.05 C
ANISOU 3860 CG TYR B 235 9606 6400 6430 417 339 1292 C
ATOM 3861 CD1 TYR B 235 31.794 -11.447 199.942 1.00 55.67 C
ANISOU 3861 CD1 TYR B 235 9429 5893 5832 320 602 1363 C
ATOM 3862 CD2 TYR B 235 30.948 -12.753 201.748 1.00 53.29 C
ANISOU 3862 CD2 TYR B 235 8602 5842 5805 379 316 1094 C
ATOM 3863 CE1 TYR B 235 32.958 -12.193 199.938 1.00 62.92 C
ANISOU 3863 CE1 TYR B 235 10284 6905 6717 197 832 1220 C
ATOM 3864 CE2 TYR B 235 32.107 -13.504 201.751 1.00 50.61 C
ANISOU 3864 CE2 TYR B 235 8219 5590 5421 269 514 966 C
ATOM 3865 CZ TYR B 235 33.109 -13.218 200.843 1.00 60.59 C
ANISOU 3865 CZ TYR B 235 9696 6779 6547 182 771 1020 C
ATOM 3866 OH TYR B 235 34.267 -13.962 200.840 1.00 70.60 O
ANISOU 3866 OH TYR B 235 10885 8129 7809 87 982 882 O
ATOM 3867 N PHE B 236 27.733 -8.117 201.569 1.00 62.21 N
ANISOU 3867 N PHE B 236 9988 6265 7384 845 -83 1680 N
ATOM 3868 CA PHE B 236 26.785 -7.087 201.152 1.00 63.13 C
ANISOU 3868 CA PHE B 236 10233 6186 7569 1023 -252 1880 C
ATOM 3869 C PHE B 236 27.503 -5.767 200.909 1.00 72.80 C
ANISOU 3869 C PHE B 236 11684 7125 8850 977 2 2009 C
ATOM 3870 O PHE B 236 27.265 -5.091 199.896 1.00 77.09 O
ANISOU 3870 O PHE B 236 12548 7495 9249 1068 -60 2256 O
ATOM 3871 CB PHE B 236 25.682 -6.917 202.201 1.00 63.48 C
ANISOU 3871 CB PHE B 236 9951 6242 7927 1158 -413 1784 C
ATOM 3872 CG PHE B 236 24.657 -5.876 201.845 1.00 77.05 C
ANISOU 3872 CG PHE B 236 11747 7753 9774 1372 -599 1973 C
ATOM 3873 CD1 PHE B 236 23.621 -6.173 200.977 1.00 82.04 C
ANISOU 3873 CD1 PHE B 236 12450 8435 10285 1536 -952 2120 C
ATOM 3874 CD2 PHE B 236 24.723 -4.602 202.385 1.00 91.10 C
ANISOU 3874 CD2 PHE B 236 13525 9277 11812 1417 -441 1993 C
ATOM 3875 CE1 PHE B 236 22.676 -5.217 200.644 1.00 88.72 C
ANISOU 3875 CE1 PHE B 236 13353 9087 11270 1760 -1156 2302 C
ATOM 3876 CE2 PHE B 236 23.778 -3.642 202.059 1.00 88.69 C
ANISOU 3876 CE2 PHE B 236 13291 8757 11651 1639 -615 2173 C
ATOM 3877 CZ PHE B 236 22.753 -3.952 201.187 1.00 91.03 C
ANISOU 3877 CZ PHE B 236 13644 9113 11831 1820 -979 2335 C
ATOM 3878 N GLN B 237 28.418 -5.397 201.811 1.00 74.21 N
ANISOU 3878 N GLN B 237 11718 7246 9231 826 286 1845 N
ATOM 3879 CA GLN B 237 29.182 -4.169 201.586 1.00 77.58 C
ANISOU 3879 CA GLN B 237 12348 7385 9746 742 555 1947 C
ATOM 3880 C GLN B 237 30.091 -4.292 200.364 1.00 81.71 C
ANISOU 3880 C GLN B 237 13202 7874 9968 621 742 2098 C
ATOM 3881 O GLN B 237 30.231 -3.338 199.584 1.00 81.45 O
ANISOU 3881 O GLN B 237 13488 7585 9873 634 854 2327 O
ATOM 3882 CB GLN B 237 29.992 -3.818 202.834 1.00 76.58 C
ANISOU 3882 CB GLN B 237 11970 7219 9906 587 791 1700 C
ATOM 3883 CG GLN B 237 29.138 -3.358 204.005 1.00 72.35 C
ANISOU 3883 CG GLN B 237 11190 6637 9662 709 677 1571 C
ATOM 3884 CD GLN B 237 29.930 -2.570 205.026 1.00 72.68 C
ANISOU 3884 CD GLN B 237 11108 6533 9974 567 916 1375 C
ATOM 3885 OE1 GLN B 237 31.087 -2.884 205.308 1.00 73.83 O
ANISOU 3885 OE1 GLN B 237 11175 6760 10117 366 1099 1224 O
ATOM 3886 NE2 GLN B 237 29.316 -1.526 205.575 1.00 73.27 N
ANISOU 3886 NE2 GLN B 237 11160 6381 10299 675 908 1363 N
ATOM 3887 N ILE B 238 30.692 -5.469 200.162 1.00 79.37 N
ANISOU 3887 N ILE B 238 12855 7823 9479 512 792 1982 N
ATOM 3888 CA ILE B 238 31.558 -5.668 199.002 1.00 77.67 C
ANISOU 3888 CA ILE B 238 12951 7593 8969 401 1005 2100 C
ATOM 3889 C ILE B 238 30.755 -5.546 197.714 1.00 83.86 C
ANISOU 3889 C ILE B 238 14126 8317 9419 559 795 2380 C
ATOM 3890 O ILE B 238 31.241 -5.019 196.705 1.00 90.92 O
ANISOU 3890 O ILE B 238 15399 9049 10098 513 987 2586 O
ATOM 3891 CB ILE B 238 32.268 -7.031 199.090 1.00 72.76 C
ANISOU 3891 CB ILE B 238 12170 7246 8229 286 1077 1896 C
ATOM 3892 CG1 ILE B 238 33.288 -7.036 200.229 1.00 63.61 C
ANISOU 3892 CG1 ILE B 238 10675 6119 7375 120 1308 1648 C
ATOM 3893 CG2 ILE B 238 32.923 -7.384 197.758 1.00 68.79 C
ANISOU 3893 CG2 ILE B 238 12017 6754 7367 214 1261 2018 C
ATOM 3894 CD1 ILE B 238 33.879 -8.406 200.513 1.00 60.99 C
ANISOU 3894 CD1 ILE B 238 10134 6054 6986 50 1326 1438 C
ATOM 3895 N PHE B 239 29.507 -6.021 197.733 1.00 82.83 N
ANISOU 3895 N PHE B 239 13916 8313 9244 746 393 2393 N
ATOM 3896 CA PHE B 239 28.645 -5.920 196.562 1.00 83.04 C
ANISOU 3896 CA PHE B 239 14286 8299 8966 918 111 2642 C
ATOM 3897 C PHE B 239 28.268 -4.473 196.286 1.00 85.93 C
ANISOU 3897 C PHE B 239 14796 8392 9461 1017 98 2856 C
ATOM 3898 O PHE B 239 28.315 -4.018 195.134 1.00 84.61 O
ANISOU 3898 O PHE B 239 14897 8183 9068 1021 96 3026 O
ATOM 3899 CB PHE B 239 27.395 -6.779 196.770 1.00 84.34 C
ANISOU 3899 CB PHE B 239 14227 8675 9142 1073 -329 2556 C
ATOM 3900 CG PHE B 239 26.284 -6.489 195.804 1.00 86.72 C
ANISOU 3900 CG PHE B 239 14697 8965 9288 1261 -700 2748 C
ATOM 3901 CD1 PHE B 239 26.265 -7.081 194.554 1.00 84.99 C
ANISOU 3901 CD1 PHE B 239 14700 8901 8690 1237 -816 2785 C
ATOM 3902 CD2 PHE B 239 25.249 -5.636 196.152 1.00 90.74 C
ANISOU 3902 CD2 PHE B 239 15057 9345 10076 1446 -923 2838 C
ATOM 3903 CE1 PHE B 239 25.241 -6.819 193.660 1.00 85.24 C
ANISOU 3903 CE1 PHE B 239 14815 8962 8609 1389 -1162 2918 C
ATOM 3904 CE2 PHE B 239 24.223 -5.370 195.261 1.00 95.77 C
ANISOU 3904 CE2 PHE B 239 15749 10013 10624 1602 -1263 2980 C
ATOM 3905 CZ PHE B 239 24.220 -5.963 194.014 1.00 92.25 C
ANISOU 3905 CZ PHE B 239 15536 9729 9786 1572 -1390 3023 C
ATOM 3906 N ARG B 240 27.936 -3.722 197.341 1.00 86.48 N
ANISOU 3906 N ARG B 240 14670 8280 9909 1089 110 2826 N
ATOM 3907 CA ARG B 240 27.635 -2.308 197.147 1.00 84.31 C
ANISOU 3907 CA ARG B 240 14487 7737 9811 1167 121 2993 C
ATOM 3908 C ARG B 240 28.832 -1.567 196.571 1.00 84.69 C
ANISOU 3908 C ARG B 240 14775 7617 9786 968 509 3079 C
ATOM 3909 O ARG B 240 28.663 -0.660 195.748 1.00 82.10 O
ANISOU 3909 O ARG B 240 14666 7135 9392 1016 487 3286 O
ATOM 3910 CB ARG B 240 27.215 -1.668 198.472 1.00 85.66 C
ANISOU 3910 CB ARG B 240 14394 7729 10422 1257 132 2889 C
ATOM 3911 CG ARG B 240 25.884 -2.144 199.034 1.00 95.60 C
ANISOU 3911 CG ARG B 240 15349 9140 11833 1469 -245 2801 C
ATOM 3912 CD ARG B 240 24.768 -1.153 198.735 1.00118.19 C
ANISOU 3912 CD ARG B 240 18231 11817 14858 1707 -497 2984 C
ATOM 3913 NE ARG B 240 23.794 -1.085 199.822 1.00129.52 N
ANISOU 3913 NE ARG B 240 19331 13229 16650 1891 -652 2854 N
ATOM 3914 CZ ARG B 240 23.781 -0.138 200.757 1.00135.54 C
ANISOU 3914 CZ ARG B 240 19950 13770 17781 1918 -476 2763 C
ATOM 3915 NH1 ARG B 240 24.687 0.830 200.734 1.00136.21 N
ANISOU 3915 NH1 ARG B 240 20240 13585 17928 1788 -166 2815 N
ATOM 3916 NH2 ARG B 240 22.860 -0.156 201.712 1.00136.76 N
ANISOU 3916 NH2 ARG B 240 19737 13976 18250 2056 -596 2598 N
ATOM 3917 N LYS B 241 30.047 -1.960 196.963 1.00 85.43 N
ANISOU 3917 N LYS B 241 14819 7740 9898 743 867 2925 N
ATOM 3918 CA LYS B 241 31.231 -1.261 196.474 1.00 78.30 C
ANISOU 3918 CA LYS B 241 14084 6682 8984 534 1262 2976 C
ATOM 3919 C LYS B 241 31.566 -1.639 195.034 1.00 85.21 C
ANISOU 3919 C LYS B 241 15259 7682 9433 493 1305 3106 C
ATOM 3920 O LYS B 241 31.904 -0.767 194.226 1.00 91.29 O
ANISOU 3920 O LYS B 241 16269 8290 10127 447 1459 3274 O
ATOM 3921 CB LYS B 241 32.425 -1.553 197.384 1.00 76.21 C
ANISOU 3921 CB LYS B 241 13604 6417 8935 300 1624 2745 C
ATOM 3922 CG LYS B 241 33.661 -0.707 197.109 1.00 81.59 C
ANISOU 3922 CG LYS B 241 14358 6913 9731 67 2043 2750 C
ATOM 3923 CD LYS B 241 33.593 0.628 197.840 1.00 84.30 C
ANISOU 3923 CD LYS B 241 14614 6949 10467 51 2114 2741 C
ATOM 3924 CE LYS B 241 34.959 1.296 197.907 1.00 91.01 C
ANISOU 3924 CE LYS B 241 15418 7640 11522 -228 2543 2651 C
ATOM 3925 NZ LYS B 241 34.943 2.533 198.746 1.00 99.99 N
ANISOU 3925 NZ LYS B 241 16440 8484 13066 -267 2605 2583 N
ATOM 3926 N LEU B 242 31.489 -2.929 194.695 1.00 86.50 N
ANISOU 3926 N LEU B 242 15426 8124 9316 507 1180 3020 N
ATOM 3927 CA LEU B 242 31.930 -3.366 193.373 1.00 87.26 C
ANISOU 3927 CA LEU B 242 15804 8341 9011 452 1270 3090 C
ATOM 3928 C LEU B 242 30.887 -3.098 192.293 1.00 93.65 C
ANISOU 3928 C LEU B 242 16866 9165 9552 642 920 3303 C
ATOM 3929 O LEU B 242 31.238 -2.675 191.186 1.00107.88 O
ANISOU 3929 O LEU B 242 18975 10905 11108 607 1052 3454 O
ATOM 3930 CB LEU B 242 32.292 -4.850 193.402 1.00 86.60 C
ANISOU 3930 CB LEU B 242 15632 8531 8740 388 1286 2891 C
ATOM 3931 CG LEU B 242 33.605 -5.201 194.106 1.00 81.22 C
ANISOU 3931 CG LEU B 242 14754 7859 8246 169 1703 2695 C
ATOM 3932 CD1 LEU B 242 33.843 -6.699 194.079 1.00 83.10 C
ANISOU 3932 CD1 LEU B 242 14917 8365 8293 141 1679 2515 C
ATOM 3933 CD2 LEU B 242 34.770 -4.468 193.472 1.00 69.69 C
ANISOU 3933 CD2 LEU B 242 13440 6251 6789 -9 2137 2749 C
ATOM 3934 N TRP B 243 29.608 -3.349 192.575 1.00 93.24 N
ANISOU 3934 N TRP B 243 16681 9196 9548 844 476 3314 N
ATOM 3935 CA TRP B 243 28.565 -3.148 191.577 1.00 89.92 C
ANISOU 3935 CA TRP B 243 16449 8811 8907 1030 107 3498 C
ATOM 3936 C TRP B 243 27.852 -1.809 191.709 1.00 97.93 C
ANISOU 3936 C TRP B 243 17465 9575 10167 1178 -30 3700 C
ATOM 3937 O TRP B 243 26.954 -1.522 190.912 1.00107.75 O
ANISOU 3937 O TRP B 243 18847 10825 11266 1348 -344 3875 O
ATOM 3938 CB TRP B 243 27.557 -4.297 191.628 1.00 84.90 C
ANISOU 3938 CB TRP B 243 15648 8436 8174 1158 -317 3379 C
ATOM 3939 CG TRP B 243 28.075 -5.538 190.965 1.00 90.47 C
ANISOU 3939 CG TRP B 243 16479 9372 8522 1050 -255 3240 C
ATOM 3940 CD1 TRP B 243 27.921 -5.894 189.656 1.00 94.90 C
ANISOU 3940 CD1 TRP B 243 17333 10043 8683 1078 -378 3304 C
ATOM 3941 CD2 TRP B 243 28.852 -6.577 191.574 1.00 87.78 C
ANISOU 3941 CD2 TRP B 243 15988 9168 8198 904 -45 3008 C
ATOM 3942 NE1 TRP B 243 28.544 -7.095 189.416 1.00 97.48 N
ANISOU 3942 NE1 TRP B 243 17695 10556 8789 957 -251 3110 N
ATOM 3943 CE2 TRP B 243 29.123 -7.536 190.577 1.00 91.74 C
ANISOU 3943 CE2 TRP B 243 16692 9849 8318 852 -47 2933 C
ATOM 3944 CE3 TRP B 243 29.339 -6.794 192.867 1.00 81.40 C
ANISOU 3944 CE3 TRP B 243 14899 8339 7690 818 141 2854 C
ATOM 3945 CZ2 TRP B 243 29.859 -8.694 190.832 1.00 88.98 C
ANISOU 3945 CZ2 TRP B 243 16257 9651 7899 725 136 2713 C
ATOM 3946 CZ3 TRP B 243 30.069 -7.944 193.119 1.00 78.87 C
ANISOU 3946 CZ3 TRP B 243 14499 8182 7285 691 310 2652 C
ATOM 3947 CH2 TRP B 243 30.322 -8.878 192.106 1.00 82.42 C
ANISOU 3947 CH2 TRP B 243 15139 8803 7372 649 308 2583 C
ATOM 3948 N GLY B 244 28.220 -0.989 192.692 1.00100.58 N
ANISOU 3948 N GLY B 244 17648 9686 10881 1121 192 3671 N
ATOM 3949 CA GLY B 244 27.737 0.372 192.735 1.00108.70 C
ANISOU 3949 CA GLY B 244 18723 10433 12147 1236 135 3861 C
ATOM 3950 C GLY B 244 28.529 1.286 191.816 1.00116.30 C
ANISOU 3950 C GLY B 244 20032 11196 12959 1123 428 4057 C
ATOM 3951 O GLY B 244 29.592 0.936 191.304 1.00117.80 O
ANISOU 3951 O GLY B 244 20388 11448 12923 932 748 4017 O
ATOM 3952 N ARG B 245 27.991 2.485 191.607 1.00123.71 N
ANISOU 3952 N ARG B 245 21075 11883 14046 1251 327 4273 N
ATOM 3953 CA ARG B 245 28.696 3.477 190.807 1.00136.30 C
ANISOU 3953 CA ARG B 245 23003 13246 15541 1149 609 4480 C
ATOM 3954 C ARG B 245 29.987 3.888 191.506 1.00141.82 C
ANISOU 3954 C ARG B 245 23621 13778 16487 886 1099 4334 C
ATOM 3955 O ARG B 245 30.041 3.993 192.734 1.00138.33 O
ANISOU 3955 O ARG B 245 22877 13264 16416 849 1155 4143 O
ATOM 3956 CB ARG B 245 27.805 4.699 190.564 1.00143.06 C
ANISOU 3956 CB ARG B 245 23958 13839 16557 1353 383 4739 C
ATOM 3957 CG ARG B 245 26.674 4.465 189.569 1.00148.49 C
ANISOU 3957 CG ARG B 245 24794 14668 16957 1597 -63 4938 C
ATOM 3958 CD ARG B 245 25.952 5.769 189.232 1.00157.61 C
ANISOU 3958 CD ARG B 245 26081 15531 18272 1788 -235 5228 C
ATOM 3959 NE ARG B 245 25.079 5.636 188.067 1.00164.01 N
ANISOU 3959 NE ARG B 245 27107 16463 18745 1994 -607 5453 N
ATOM 3960 CZ ARG B 245 24.415 6.646 187.511 1.00169.49 C
ANISOU 3960 CZ ARG B 245 27972 16944 19482 2185 -799 5747 C
ATOM 3961 NH1 ARG B 245 24.521 7.868 188.012 1.00170.16 N
ANISOU 3961 NH1 ARG B 245 28041 16667 19945 2193 -647 5850 N
ATOM 3962 NH2 ARG B 245 23.645 6.434 186.451 1.00174.38 N
ANISOU 3962 NH2 ARG B 245 28784 17706 19768 2370 -1150 5931 N
ATOM 3963 N GLN B 246 31.032 4.118 190.717 1.00155.17 N
ANISOU 3963 N GLN B 246 25572 15408 17978 701 1460 4410 N
ATOM 3964 CA GLN B 246 32.349 4.458 191.237 1.00154.70 C
ANISOU 3964 CA GLN B 246 25421 15213 18146 428 1945 4263 C
ATOM 3965 C GLN B 246 32.655 5.931 190.988 1.00152.53 C
ANISOU 3965 C GLN B 246 25335 14569 18048 370 2154 4456 C
ATOM 3966 O GLN B 246 31.852 6.680 190.426 1.00157.11 O
ANISOU 3966 O GLN B 246 26130 14994 18570 550 1925 4715 O
ATOM 3967 CB GLN B 246 33.425 3.562 190.620 1.00164.03 C
ANISOU 3967 CB GLN B 246 26691 16600 19033 238 2255 4162 C
ATOM 3968 CG GLN B 246 33.548 2.203 191.288 1.00167.69 C
ANISOU 3968 CG GLN B 246 26869 17360 19487 204 2198 3885 C
ATOM 3969 CD GLN B 246 34.872 1.529 190.993 1.00173.92 C
ANISOU 3969 CD GLN B 246 27651 18274 20157 -28 2609 3732 C
ATOM 3970 OE1 GLN B 246 35.479 1.758 189.946 1.00180.88 O
ANISOU 3970 OE1 GLN B 246 28812 19110 20804 -111 2856 3853 O
ATOM 3971 NE2 GLN B 246 35.332 0.699 191.922 1.00171.50 N
ANISOU 3971 NE2 GLN B 246 27018 18118 20028 -127 2694 3464 N
ATOM 3972 N ILE B 247 33.849 6.337 191.407 1.00147.30 N
ANISOU 3972 N ILE B 247 24580 13766 17620 111 2591 4323 N
ATOM 3973 CA ILE B 247 34.265 7.738 191.386 1.00144.88 C
ANISOU 3973 CA ILE B 247 24393 13089 17564 12 2832 4446 C
ATOM 3974 C ILE B 247 34.328 8.226 189.943 1.00151.23 C
ANISOU 3974 C ILE B 247 25648 13796 18018 39 2912 4771 C
ATOM 3975 O ILE B 247 34.674 7.450 189.039 1.00152.93 O
ANISOU 3975 O ILE B 247 26044 14227 17837 5 2997 4807 O
ATOM 3976 CB ILE B 247 35.614 7.914 192.102 1.00142.32 C
ANISOU 3976 CB ILE B 247 23835 12683 17558 -297 3285 4196 C
ATOM 3977 CG1 ILE B 247 35.546 7.290 193.499 1.00135.56 C
ANISOU 3977 CG1 ILE B 247 22550 11963 16994 -317 3184 3869 C
ATOM 3978 CG2 ILE B 247 35.990 9.385 192.182 1.00149.97 C
ANISOU 3978 CG2 ILE B 247 24898 13253 18830 -406 3512 4295 C
ATOM 3979 CD1 ILE B 247 36.894 7.061 194.136 1.00132.08 C
ANISOU 3979 CD1 ILE B 247 21832 11556 16795 -613 3574 3585 C
ATOM 3980 N PRO B 248 33.994 9.493 189.680 1.00151.19 N
ANISOU 3980 N PRO B 248 25849 13459 18139 107 2889 5011 N
ATOM 3981 CA PRO B 248 33.917 9.956 188.283 1.00156.59 C
ANISOU 3981 CA PRO B 248 26993 14046 18458 166 2917 5354 C
ATOM 3982 C PRO B 248 35.211 9.815 187.501 1.00159.50 C
ANISOU 3982 C PRO B 248 27556 14436 18609 -85 3407 5360 C
ATOM 3983 O PRO B 248 35.158 9.617 186.278 1.00165.09 O
ANISOU 3983 O PRO B 248 28631 15223 18873 -27 3407 5571 O
ATOM 3984 CB PRO B 248 33.504 11.428 188.434 1.00159.68 C
ANISOU 3984 CB PRO B 248 27498 14025 19150 241 2870 5561 C
ATOM 3985 CG PRO B 248 32.780 11.479 189.735 1.00153.31 C
ANISOU 3985 CG PRO B 248 26315 13189 18747 359 2595 5363 C
ATOM 3986 CD PRO B 248 33.492 10.501 190.627 1.00147.72 C
ANISOU 3986 CD PRO B 248 25247 12728 18154 177 2770 4989 C
ATOM 3987 N GLY B 249 36.368 9.924 188.147 1.00152.65 N
ANISOU 3987 N GLY B 249 26453 13499 18047 -358 3824 5128 N
ATOM 3988 CA GLY B 249 37.632 9.838 187.430 1.00149.41 C
ANISOU 3988 CA GLY B 249 26186 13091 17492 -600 4317 5120 C
ATOM 3989 C GLY B 249 38.373 8.525 187.600 1.00140.41 C
ANISOU 3989 C GLY B 249 24806 12286 16259 -728 4482 4828 C
ATOM 3990 O GLY B 249 39.550 8.521 187.971 1.00136.64 O
ANISOU 3990 O GLY B 249 24110 11777 16030 -982 4891 4624 O
ATOM 3991 N THR B 250 37.699 7.408 187.335 1.00135.66 N
ANISOU 3991 N THR B 250 24226 11998 15320 -553 4161 4797 N
ATOM 3992 CA THR B 250 38.323 6.100 187.491 1.00133.08 C
ANISOU 3992 CA THR B 250 23681 11984 14898 -651 4285 4523 C
ATOM 3993 C THR B 250 39.388 5.863 186.423 1.00137.55 C
ANISOU 3993 C THR B 250 24478 12586 15199 -813 4723 4553 C
ATOM 3994 O THR B 250 39.223 6.240 185.260 1.00144.13 O
ANISOU 3994 O THR B 250 25745 13339 15681 -750 4761 4820 O
ATOM 3995 CB THR B 250 37.265 4.999 187.425 1.00129.44 C
ANISOU 3995 CB THR B 250 23214 11827 14141 -419 3815 4493 C
ATOM 3996 OG1 THR B 250 36.233 5.268 188.383 1.00127.49 O
ANISOU 3996 OG1 THR B 250 22757 11530 14153 -256 3420 4478 O
ATOM 3997 CG2 THR B 250 37.888 3.645 187.733 1.00124.64 C
ANISOU 3997 CG2 THR B 250 22351 11520 13488 -517 3930 4193 C
ATOM 3998 N THR B 251 40.489 5.237 186.831 1.00133.47 N
ANISOU 3998 N THR B 251 23664 12186 14863 -1016 5057 4274 N
ATOM 3999 CA THR B 251 41.577 4.852 185.941 1.00133.87 C
ANISOU 3999 CA THR B 251 23850 12295 14718 -1173 5497 4239 C
ATOM 4000 C THR B 251 41.295 3.496 185.293 1.00123.46 C
ANISOU 4000 C THR B 251 22655 11304 12950 -1049 5335 4174 C
ATOM 4001 O THR B 251 40.521 2.684 185.803 1.00123.27 O
ANISOU 4001 O THR B 251 22472 11492 12872 -900 4943 4065 O
ATOM 4002 CB THR B 251 42.905 4.809 186.705 1.00143.47 C
ANISOU 4002 CB THR B 251 24640 13480 16390 -1442 5916 3952 C
ATOM 4003 OG1 THR B 251 43.178 6.105 187.253 1.00149.93 O
ANISOU 4003 OG1 THR B 251 25363 13980 17623 -1571 6065 4001 O
ATOM 4004 CG2 THR B 251 44.049 4.413 185.785 1.00153.30 C
ANISOU 4004 CG2 THR B 251 25995 14775 17475 -1597 6389 3907 C
ATOM 4005 N SER B 252 41.937 3.264 184.144 1.00128.59 N
ANISOU 4005 N SER B 252 23600 11981 13277 -1114 5652 4239 N
ATOM 4006 CA SER B 252 41.777 1.989 183.450 1.00130.87 C
ANISOU 4006 CA SER B 252 24030 12559 13136 -1015 5544 4156 C
ATOM 4007 C SER B 252 42.297 0.827 184.290 1.00133.28 C
ANISOU 4007 C SER B 252 23882 13096 13664 -1086 5585 3802 C
ATOM 4008 O SER B 252 41.710 -0.267 184.293 1.00132.33 O
ANISOU 4008 O SER B 252 23736 13227 13316 -949 5275 3695 O
ATOM 4009 CB SER B 252 42.504 2.039 182.107 1.00138.18 C
ANISOU 4009 CB SER B 252 25351 13437 13716 -1097 5948 4272 C
ATOM 4010 OG SER B 252 43.888 2.294 182.295 1.00141.20 O
ANISOU 4010 OG SER B 252 25513 13700 14435 -1350 6504 4132 O
ATOM 4011 N ALA B 285 43.383 1.052 185.034 1.00134.30 N
ANISOU 4011 N ALA B 285 23634 13138 14256 -1299 5947 3613 N
ATOM 4012 CA ALA B 285 43.932 -0.023 185.850 1.00125.33 C
ANISOU 4012 CA ALA B 285 22051 12212 13355 -1365 5988 3283 C
ATOM 4013 C ALA B 285 42.925 -0.473 186.897 1.00124.74 C
ANISOU 4013 C ALA B 285 21742 12273 13380 -1218 5497 3198 C
ATOM 4014 O ALA B 285 42.707 -1.678 187.088 1.00124.81 O
ANISOU 4014 O ALA B 285 21625 12533 13265 -1138 5314 3033 O
ATOM 4015 CB ALA B 285 45.235 0.429 186.512 1.00123.10 C
ANISOU 4015 CB ALA B 285 21380 11796 13595 -1617 6418 3102 C
ATOM 4016 N GLU B 286 42.271 0.481 187.564 1.00131.85 N
ANISOU 4016 N GLU B 286 22597 13001 14500 -1176 5282 3313 N
ATOM 4017 CA GLU B 286 41.274 0.107 188.555 1.00137.01 C
ANISOU 4017 CA GLU B 286 23040 13764 15253 -1030 4832 3243 C
ATOM 4018 C GLU B 286 40.008 -0.462 187.926 1.00139.63 C
ANISOU 4018 C GLU B 286 23667 14255 15133 -782 4386 3385 C
ATOM 4019 O GLU B 286 39.311 -1.237 188.583 1.00133.96 O
ANISOU 4019 O GLU B 286 22764 13713 14422 -666 4046 3271 O
ATOM 4020 CB GLU B 286 40.946 1.291 189.469 1.00 98.51 C
ANISOU 4020 CB GLU B 286 18021 8643 10766 -1050 4741 3303 C
ATOM 4021 CG GLU B 286 40.805 2.635 188.797 1.00112.43 C
ANISOU 4021 CG GLU B 286 20115 10114 12489 -1051 4837 3585 C
ATOM 4022 CD GLU B 286 40.931 3.771 189.795 1.00113.96 C
ANISOU 4022 CD GLU B 286 20085 10041 13173 -1150 4893 3555 C
ATOM 4023 OE1 GLU B 286 41.394 3.511 190.926 1.00112.79 O
ANISOU 4023 OE1 GLU B 286 19518 9941 13397 -1264 4943 3288 O
ATOM 4024 OE2 GLU B 286 40.572 4.917 189.454 1.00120.68 O
ANISOU 4024 OE2 GLU B 286 21182 10631 14040 -1114 4879 3790 O
ATOM 4025 N VAL B 287 39.705 -0.135 186.668 1.00103.29 N
ANISOU 4025 N VAL B 287 19510 9599 10136 -702 4372 3622 N
ATOM 4026 CA VAL B 287 38.558 -0.773 186.024 1.00119.13 C
ANISOU 4026 CA VAL B 287 21769 11783 11714 -477 3931 3721 C
ATOM 4027 C VAL B 287 38.841 -2.251 185.762 1.00119.56 C
ANISOU 4027 C VAL B 287 21768 12122 11539 -479 3942 3499 C
ATOM 4028 O VAL B 287 37.992 -3.120 186.021 1.00121.91 O
ANISOU 4028 O VAL B 287 21985 12618 11717 -337 3546 3415 O
ATOM 4029 CB VAL B 287 38.177 -0.025 184.734 1.00121.14 C
ANISOU 4029 CB VAL B 287 22522 11906 11599 -391 3901 4031 C
ATOM 4030 CG1 VAL B 287 37.114 -0.798 183.968 1.00121.48 C
ANISOU 4030 CG1 VAL B 287 22815 12160 11182 -178 3458 4093 C
ATOM 4031 CG2 VAL B 287 37.680 1.374 185.062 1.00118.26 C
ANISOU 4031 CG2 VAL B 287 22202 11261 11471 -344 3799 4258 C
ATOM 4032 N LYS B 288 40.043 -2.568 185.268 1.00113.15 N
ANISOU 4032 N LYS B 288 20979 11323 10689 -642 4400 3391 N
ATOM 4033 CA LYS B 288 40.398 -3.976 185.105 1.00111.41 C
ANISOU 4033 CA LYS B 288 20669 11351 10312 -648 4441 3156 C
ATOM 4034 C LYS B 288 40.426 -4.682 186.458 1.00111.16 C
ANISOU 4034 C LYS B 288 20155 11447 10632 -668 4320 2909 C
ATOM 4035 O LYS B 288 39.956 -5.826 186.595 1.00105.74 O
ANISOU 4035 O LYS B 288 19397 10979 9799 -571 4059 2770 O
ATOM 4036 CB LYS B 288 41.752 -4.092 184.400 1.00115.73 C
ANISOU 4036 CB LYS B 288 21285 11858 10828 -820 4993 3080 C
ATOM 4037 CG LYS B 288 41.787 -3.449 183.011 1.00133.45 C
ANISOU 4037 CG LYS B 288 24043 13977 12686 -809 5157 3326 C
ATOM 4038 CD LYS B 288 43.168 -3.548 182.366 1.00135.28 C
ANISOU 4038 CD LYS B 288 24320 14157 12924 -988 5743 3242 C
ATOM 4039 CE LYS B 288 43.149 -3.044 180.930 1.00139.31 C
ANISOU 4039 CE LYS B 288 25387 14562 12982 -965 5900 3487 C
ATOM 4040 NZ LYS B 288 44.444 -3.267 180.226 1.00148.37 N
ANISOU 4040 NZ LYS B 288 26601 15676 14097 -1126 6476 3395 N
ATOM 4041 N GLN B 289 40.913 -3.977 187.485 1.00110.13 N
ANISOU 4041 N GLN B 289 19703 11174 10968 -792 4483 2858 N
ATOM 4042 CA GLN B 289 40.920 -4.523 188.837 1.00100.97 C
ANISOU 4042 CA GLN B 289 18098 10116 10151 -813 4364 2642 C
ATOM 4043 C GLN B 289 39.505 -4.840 189.306 1.00 96.24 C
ANISOU 4043 C GLN B 289 17506 9616 9445 -612 3827 2693 C
ATOM 4044 O GLN B 289 39.254 -5.911 189.877 1.00 91.92 O
ANISOU 4044 O GLN B 289 16755 9265 8904 -560 3642 2522 O
ATOM 4045 CB GLN B 289 41.602 -3.514 189.767 1.00106.39 C
ANISOU 4045 CB GLN B 289 18488 10597 11338 -980 4603 2599 C
ATOM 4046 CG GLN B 289 41.752 -3.911 191.224 1.00103.10 C
ANISOU 4046 CG GLN B 289 17600 10254 11319 -1032 4526 2371 C
ATOM 4047 CD GLN B 289 42.338 -2.781 192.060 1.00108.62 C
ANISOU 4047 CD GLN B 289 18047 10727 12496 -1196 4722 2331 C
ATOM 4048 OE1 GLN B 289 41.924 -1.625 191.940 1.00112.67 O
ANISOU 4048 OE1 GLN B 289 18738 11019 13051 -1179 4680 2519 O
ATOM 4049 NE2 GLN B 289 43.319 -3.107 192.897 1.00107.71 N
ANISOU 4049 NE2 GLN B 289 17508 10663 12754 -1355 4926 2075 N
ATOM 4050 N MET B 290 38.559 -3.934 189.038 1.00 93.48 N
ANISOU 4050 N MET B 290 17386 9131 9000 -490 3571 2932 N
ATOM 4051 CA MET B 290 37.182 -4.133 189.471 1.00 91.59 C
ANISOU 4051 CA MET B 290 17124 8968 8708 -289 3056 2986 C
ATOM 4052 C MET B 290 36.524 -5.299 188.745 1.00 88.15 C
ANISOU 4052 C MET B 290 16859 8775 7861 -153 2760 2950 C
ATOM 4053 O MET B 290 35.756 -6.052 189.349 1.00 89.37 O
ANISOU 4053 O MET B 290 16842 9081 8035 -47 2419 2851 O
ATOM 4054 CB MET B 290 36.374 -2.855 189.256 1.00 96.72 C
ANISOU 4054 CB MET B 290 17969 9402 9376 -180 2863 3252 C
ATOM 4055 CG MET B 290 34.948 -2.934 189.786 1.00100.57 C
ANISOU 4055 CG MET B 290 18374 9943 9896 35 2339 3303 C
ATOM 4056 SD MET B 290 33.952 -1.504 189.321 1.00113.56 S
ANISOU 4056 SD MET B 290 20269 11345 11535 200 2088 3629 S
ATOM 4057 CE MET B 290 34.010 -1.626 187.534 1.00120.43 C
ANISOU 4057 CE MET B 290 21630 12274 11853 237 2117 3809 C
ATOM 4058 N ARG B 291 36.808 -5.476 187.453 1.00 90.48 N
ANISOU 4058 N ARG B 291 17491 9102 7785 -159 2887 3017 N
ATOM 4059 CA ARG B 291 36.188 -6.599 186.752 1.00 94.81 C
ANISOU 4059 CA ARG B 291 18202 9872 7950 -40 2597 2953 C
ATOM 4060 C ARG B 291 36.704 -7.938 187.284 1.00 95.14 C
ANISOU 4060 C ARG B 291 17979 10108 8062 -106 2684 2664 C
ATOM 4061 O ARG B 291 35.914 -8.870 187.541 1.00 94.73 O
ANISOU 4061 O ARG B 291 17839 10229 7924 1 2322 2559 O
ATOM 4062 CB ARG B 291 36.418 -6.460 185.245 1.00102.31 C
ANISOU 4062 CB ARG B 291 19597 10799 8478 -37 2734 3083 C
ATOM 4063 CG ARG B 291 35.596 -5.328 184.612 1.00106.89 C
ANISOU 4063 CG ARG B 291 20482 11227 8904 84 2510 3387 C
ATOM 4064 CD ARG B 291 36.106 -4.933 183.230 1.00120.01 C
ANISOU 4064 CD ARG B 291 22590 12807 10202 44 2777 3542 C
ATOM 4065 NE ARG B 291 35.218 -3.981 182.564 1.00131.47 N
ANISOU 4065 NE ARG B 291 24357 14138 11459 187 2503 3840 N
ATOM 4066 CZ ARG B 291 35.545 -3.287 181.477 1.00140.18 C
ANISOU 4066 CZ ARG B 291 25868 15106 12287 166 2716 4050 C
ATOM 4067 NH1 ARG B 291 36.746 -3.429 180.935 1.00145.39 N
ANISOU 4067 NH1 ARG B 291 26662 15733 12846 0 3224 3987 N
ATOM 4068 NH2 ARG B 291 34.674 -2.446 180.934 1.00146.35 N
ANISOU 4068 NH2 ARG B 291 26920 15781 12907 314 2427 4328 N
ATOM 4069 N ALA B 292 38.019 -8.038 187.516 1.00 83.22 N
ANISOU 4069 N ALA B 292 16306 8564 6749 -280 3155 2529 N
ATOM 4070 CA ALA B 292 38.539 -9.279 188.088 1.00 79.74 C
ANISOU 4070 CA ALA B 292 15583 8296 6417 -330 3241 2259 C
ATOM 4071 C ALA B 292 37.965 -9.527 189.483 1.00 93.04 C
ANISOU 4071 C ALA B 292 16920 10038 8394 -285 2971 2174 C
ATOM 4072 O ALA B 292 37.568 -10.658 189.820 1.00 91.27 O
ANISOU 4072 O ALA B 292 16578 9993 8108 -219 2749 2022 O
ATOM 4073 CB ALA B 292 40.067 -9.234 188.131 1.00 81.00 C
ANISOU 4073 CB ALA B 292 15577 8396 6803 -518 3787 2132 C
ATOM 4074 N ARG B 293 37.887 -8.473 190.300 1.00 89.39 N
ANISOU 4074 N ARG B 293 16304 9412 8248 -318 2987 2269 N
ATOM 4075 CA ARG B 293 37.334 -8.627 191.638 1.00 79.90 C
ANISOU 4075 CA ARG B 293 14794 8242 7321 -274 2751 2197 C
ATOM 4076 C ARG B 293 35.860 -9.002 191.599 1.00 80.03 C
ANISOU 4076 C ARG B 293 14909 8359 7142 -73 2223 2269 C
ATOM 4077 O ARG B 293 35.387 -9.709 192.489 1.00 75.97 O
ANISOU 4077 O ARG B 293 14171 7958 6737 -19 2004 2154 O
ATOM 4078 CB ARG B 293 37.532 -7.342 192.440 1.00 81.79 C
ANISOU 4078 CB ARG B 293 14881 8257 7939 -350 2880 2278 C
ATOM 4079 CG ARG B 293 38.946 -7.137 192.942 1.00 83.85 C
ANISOU 4079 CG ARG B 293 14876 8449 8534 -567 3338 2126 C
ATOM 4080 CD ARG B 293 39.101 -5.747 193.524 1.00 90.42 C
ANISOU 4080 CD ARG B 293 15616 9029 9712 -650 3451 2209 C
ATOM 4081 NE ARG B 293 40.328 -5.603 194.299 1.00 93.21 N
ANISOU 4081 NE ARG B 293 15612 9333 10470 -859 3798 2014 N
ATOM 4082 CZ ARG B 293 40.767 -4.444 194.778 1.00 94.94 C
ANISOU 4082 CZ ARG B 293 15707 9330 11034 -986 3969 2022 C
ATOM 4083 NH1 ARG B 293 40.081 -3.331 194.550 1.00 95.60 N
ANISOU 4083 NH1 ARG B 293 16017 9208 11097 -915 3848 2231 N
ATOM 4084 NH2 ARG B 293 41.893 -4.397 195.477 1.00 98.38 N
ANISOU 4084 NH2 ARG B 293 15779 9748 11852 -1181 4241 1809 N
ATOM 4085 N ARG B 294 35.122 -8.545 190.585 1.00 84.03 N
ANISOU 4085 N ARG B 294 15728 8825 7373 39 2007 2454 N
ATOM 4086 CA ARG B 294 33.729 -8.955 190.460 1.00 76.73 C
ANISOU 4086 CA ARG B 294 14854 8013 6288 225 1486 2497 C
ATOM 4087 C ARG B 294 33.632 -10.452 190.226 1.00 76.01 C
ANISOU 4087 C ARG B 294 14743 8153 5984 241 1353 2299 C
ATOM 4088 O ARG B 294 32.834 -11.141 190.878 1.00 70.26 O
ANISOU 4088 O ARG B 294 13827 7542 5326 324 1022 2207 O
ATOM 4089 CB ARG B 294 33.049 -8.194 189.323 1.00 75.58 C
ANISOU 4089 CB ARG B 294 15045 7787 5886 335 1295 2726 C
ATOM 4090 CG ARG B 294 32.849 -6.715 189.580 1.00 76.58 C
ANISOU 4090 CG ARG B 294 15190 7672 6233 364 1324 2939 C
ATOM 4091 CD ARG B 294 31.987 -6.080 188.498 1.00 90.25 C
ANISOU 4091 CD ARG B 294 17238 9349 7706 510 1050 3172 C
ATOM 4092 NE ARG B 294 31.723 -4.670 188.770 1.00 95.71 N
ANISOU 4092 NE ARG B 294 17941 9793 8631 558 1054 3380 N
ATOM 4093 CZ ARG B 294 30.867 -3.925 188.078 1.00100.99 C
ANISOU 4093 CZ ARG B 294 18822 10374 9175 711 787 3609 C
ATOM 4094 NH1 ARG B 294 30.188 -4.456 187.072 1.00111.47 N
ANISOU 4094 NH1 ARG B 294 20364 11853 10137 825 483 3655 N
ATOM 4095 NH2 ARG B 294 30.687 -2.649 188.393 1.00 99.20 N
ANISOU 4095 NH2 ARG B 294 18591 9901 9199 751 816 3787 N
ATOM 4096 N LYS B 295 34.462 -10.983 189.325 1.00 80.86 N
ANISOU 4096 N LYS B 295 15540 8823 6359 157 1623 2219 N
ATOM 4097 CA LYS B 295 34.441 -12.430 189.119 1.00 84.19 C
ANISOU 4097 CA LYS B 295 15942 9441 6607 167 1526 2007 C
ATOM 4098 C LYS B 295 34.714 -13.165 190.432 1.00 86.67 C
ANISOU 4098 C LYS B 295 15886 9835 7211 123 1566 1820 C
ATOM 4099 O LYS B 295 33.935 -14.044 190.853 1.00 92.22 O
ANISOU 4099 O LYS B 295 16468 10667 7904 200 1230 1715 O
ATOM 4100 CB LYS B 295 35.456 -12.825 188.043 1.00 92.54 C
ANISOU 4100 CB LYS B 295 17226 10514 7420 77 1888 1935 C
ATOM 4101 CG LYS B 295 35.148 -12.263 186.657 1.00108.38 C
ANISOU 4101 CG LYS B 295 19649 12463 9065 129 1832 2113 C
ATOM 4102 CD LYS B 295 36.109 -12.799 185.602 1.00116.51 C
ANISOU 4102 CD LYS B 295 20912 13522 9835 49 2186 2018 C
ATOM 4103 CE LYS B 295 35.686 -12.384 184.201 1.00121.28 C
ANISOU 4103 CE LYS B 295 21968 14092 10021 115 2082 2186 C
ATOM 4104 NZ LYS B 295 36.528 -13.018 183.147 1.00123.56 N
ANISOU 4104 NZ LYS B 295 22506 14418 10022 50 2404 2078 N
ATOM 4105 N THR B 296 35.792 -12.780 191.124 1.00 86.50 N
ANISOU 4105 N THR B 296 15664 9731 7471 -5 1964 1777 N
ATOM 4106 CA THR B 296 36.165 -13.518 192.331 1.00 75.35 C
ANISOU 4106 CA THR B 296 13908 8404 6316 -50 2032 1593 C
ATOM 4107 C THR B 296 35.106 -13.390 193.421 1.00 70.17 C
ANISOU 4107 C THR B 296 13043 7761 5858 46 1653 1624 C
ATOM 4108 O THR B 296 34.778 -14.375 194.097 1.00 72.91 O
ANISOU 4108 O THR B 296 13099 8263 6340 84 1432 1434 O
ATOM 4109 CB THR B 296 37.515 -13.044 192.863 1.00 69.40 C
ANISOU 4109 CB THR B 296 12937 7561 5873 -212 2510 1531 C
ATOM 4110 OG1 THR B 296 38.547 -13.426 191.948 1.00 72.32 O
ANISOU 4110 OG1 THR B 296 13403 7952 6123 -292 2853 1438 O
ATOM 4111 CG2 THR B 296 37.795 -13.680 194.220 1.00 57.63 C
ANISOU 4111 CG2 THR B 296 10967 6178 4750 -235 2466 1312 C
ATOM 4112 N ALA B 297 34.566 -12.182 193.620 1.00 70.32 N
ANISOU 4112 N ALA B 297 13108 7622 5987 90 1552 1820 N
ATOM 4113 CA ALA B 297 33.584 -11.972 194.677 1.00 70.78 C
ANISOU 4113 CA ALA B 297 12851 7698 6343 188 1195 1794 C
ATOM 4114 C ALA B 297 32.285 -12.711 194.400 1.00 75.53 C
ANISOU 4114 C ALA B 297 13510 8430 6757 337 724 1794 C
ATOM 4115 O ALA B 297 31.660 -13.221 195.339 1.00 74.60 O
ANISOU 4115 O ALA B 297 13044 8418 6881 384 478 1659 O
ATOM 4116 CB ALA B 297 33.321 -10.478 194.866 1.00 62.01 C
ANISOU 4116 CB ALA B 297 11805 6360 5395 214 1219 1999 C
ATOM 4117 N LYS B 298 31.869 -12.804 193.133 1.00 77.57 N
ANISOU 4117 N LYS B 298 14157 8695 6621 400 588 1915 N
ATOM 4118 CA LYS B 298 30.694 -13.610 192.823 1.00 72.01 C
ANISOU 4118 CA LYS B 298 13450 8132 5776 515 127 1861 C
ATOM 4119 C LYS B 298 30.935 -15.060 193.210 1.00 70.91 C
ANISOU 4119 C LYS B 298 13155 8160 5629 462 121 1618 C
ATOM 4120 O LYS B 298 30.088 -15.702 193.853 1.00 74.05 O
ANISOU 4120 O LYS B 298 13268 8660 6208 513 -194 1503 O
ATOM 4121 CB LYS B 298 30.356 -13.493 191.336 1.00 81.43 C
ANISOU 4121 CB LYS B 298 14965 9342 6634 559 -2 1945 C
ATOM 4122 CG LYS B 298 29.116 -14.261 190.892 1.00 83.47 C
ANISOU 4122 CG LYS B 298 15217 9736 6761 661 -489 1881 C
ATOM 4123 CD LYS B 298 28.653 -13.777 189.515 1.00 91.76 C
ANISOU 4123 CD LYS B 298 16584 10765 7514 731 -649 2022 C
ATOM 4124 CE LYS B 298 28.652 -14.901 188.490 1.00 98.49 C
ANISOU 4124 CE LYS B 298 17639 11751 8031 701 -736 1868 C
ATOM 4125 NZ LYS B 298 28.428 -14.386 187.101 1.00105.29 N
ANISOU 4125 NZ LYS B 298 18868 12583 8554 755 -817 2011 N
ATOM 4126 N MET B 299 32.121 -15.579 192.877 1.00 69.85 N
ANISOU 4126 N MET B 299 13111 8053 5375 350 495 1506 N
ATOM 4127 CA MET B 299 32.403 -16.970 193.221 1.00 61.25 C
ANISOU 4127 CA MET B 299 11812 7110 4349 307 499 1247 C
ATOM 4128 C MET B 299 32.366 -17.185 194.730 1.00 66.12 C
ANISOU 4128 C MET B 299 11914 7774 5434 292 451 1116 C
ATOM 4129 O MET B 299 31.761 -18.152 195.218 1.00 74.10 O
ANISOU 4129 O MET B 299 12720 8890 6546 321 205 978 O
ATOM 4130 CB MET B 299 33.759 -17.386 192.656 1.00 57.77 C
ANISOU 4130 CB MET B 299 11525 6671 3756 206 950 1149 C
ATOM 4131 CG MET B 299 34.094 -18.850 192.871 1.00 61.18 C
ANISOU 4131 CG MET B 299 11791 7225 4230 184 966 887 C
ATOM 4132 SD MET B 299 35.725 -19.247 192.220 1.00 80.94 S
ANISOU 4132 SD MET B 299 14433 9712 6609 87 1536 766 S
ATOM 4133 CE MET B 299 36.761 -18.405 193.418 1.00 73.82 C
ANISOU 4133 CE MET B 299 13090 8745 6212 -1 1853 767 C
ATOM 4134 N LEU B 300 33.001 -16.287 195.487 1.00 67.47 N
ANISOU 4134 N LEU B 300 11888 7861 5888 240 687 1154 N
ATOM 4135 CA LEU B 300 33.045 -16.456 196.939 1.00 62.74 C
ANISOU 4135 CA LEU B 300 10839 7311 5689 225 652 1023 C
ATOM 4136 C LEU B 300 31.667 -16.313 197.576 1.00 58.80 C
ANISOU 4136 C LEU B 300 10175 6832 5334 325 271 1066 C
ATOM 4137 O LEU B 300 31.356 -17.027 198.538 1.00 63.58 O
ANISOU 4137 O LEU B 300 10480 7530 6146 334 147 932 O
ATOM 4138 CB LEU B 300 34.027 -15.459 197.553 1.00 64.36 C
ANISOU 4138 CB LEU B 300 10894 7414 6148 139 967 1038 C
ATOM 4139 CG LEU B 300 35.486 -15.599 197.107 1.00 71.10 C
ANISOU 4139 CG LEU B 300 11803 8249 6964 23 1384 965 C
ATOM 4140 CD1 LEU B 300 36.344 -14.525 197.753 1.00 72.96 C
ANISOU 4140 CD1 LEU B 300 11856 8368 7498 -79 1650 973 C
ATOM 4141 CD2 LEU B 300 36.028 -16.989 197.419 1.00 69.44 C
ANISOU 4141 CD2 LEU B 300 11398 8181 6805 14 1419 744 C
ATOM 4142 N MET B 301 30.822 -15.418 197.055 1.00 59.99 N
ANISOU 4142 N MET B 301 10516 6892 5387 409 91 1257 N
ATOM 4143 CA MET B 301 29.466 -15.325 197.582 1.00 59.71 C
ANISOU 4143 CA MET B 301 10300 6877 5511 517 -269 1287 C
ATOM 4144 C MET B 301 28.706 -16.621 197.345 1.00 65.25 C
ANISOU 4144 C MET B 301 10964 7718 6109 542 -556 1175 C
ATOM 4145 O MET B 301 27.964 -17.084 198.223 1.00 62.09 O
ANISOU 4145 O MET B 301 10259 7384 5946 566 -735 1087 O
ATOM 4146 CB MET B 301 28.729 -14.150 196.944 1.00 64.36 C
ANISOU 4146 CB MET B 301 11113 7330 6012 626 -429 1519 C
ATOM 4147 CG MET B 301 29.372 -12.800 197.197 1.00 70.26 C
ANISOU 4147 CG MET B 301 11904 7896 6897 598 -154 1638 C
ATOM 4148 SD MET B 301 28.555 -11.460 196.311 1.00 83.64 S
ANISOU 4148 SD MET B 301 13931 9390 8458 748 -336 1944 S
ATOM 4149 CE MET B 301 29.541 -10.063 196.837 1.00 84.60 C
ANISOU 4149 CE MET B 301 14045 9281 8819 659 71 2018 C
ATOM 4150 N VAL B 302 28.903 -17.244 196.180 1.00 66.15 N
ANISOU 4150 N VAL B 302 11392 7869 5872 525 -579 1164 N
ATOM 4151 CA VAL B 302 28.227 -18.516 195.945 1.00 63.39 C
ANISOU 4151 CA VAL B 302 11013 7633 5439 529 -849 1027 C
ATOM 4152 C VAL B 302 28.744 -19.583 196.903 1.00 70.23 C
ANISOU 4152 C VAL B 302 11584 8575 6524 450 -707 823 C
ATOM 4153 O VAL B 302 27.968 -20.394 197.427 1.00 73.00 O
ANISOU 4153 O VAL B 302 11718 8989 7030 453 -924 724 O
ATOM 4154 CB VAL B 302 28.383 -18.957 194.481 1.00 65.83 C
ANISOU 4154 CB VAL B 302 11760 7958 5295 525 -894 1031 C
ATOM 4155 CG1 VAL B 302 27.745 -20.328 194.278 1.00 58.39 C
ANISOU 4155 CG1 VAL B 302 10778 7116 4292 507 -1166 850 C
ATOM 4156 CG2 VAL B 302 27.746 -17.933 193.551 1.00 60.55 C
ANISOU 4156 CG2 VAL B 302 11408 7214 4383 625 -1099 1258 C
ATOM 4157 N VAL B 303 30.054 -19.590 197.167 1.00 64.75 N
ANISOU 4157 N VAL B 303 10870 7867 5867 381 -341 763 N
ATOM 4158 CA VAL B 303 30.602 -20.602 198.070 1.00 58.54 C
ANISOU 4158 CA VAL B 303 9818 7143 5282 331 -227 585 C
ATOM 4159 C VAL B 303 30.019 -20.435 199.465 1.00 61.49 C
ANISOU 4159 C VAL B 303 9830 7536 5996 352 -335 577 C
ATOM 4160 O VAL B 303 29.622 -21.413 200.114 1.00 60.74 O
ANISOU 4160 O VAL B 303 9545 7498 6034 344 -448 472 O
ATOM 4161 CB VAL B 303 32.141 -20.536 198.104 1.00 52.76 C
ANISOU 4161 CB VAL B 303 9092 6391 4565 269 168 524 C
ATOM 4162 CG1 VAL B 303 32.686 -21.458 199.201 1.00 48.71 C
ANISOU 4162 CG1 VAL B 303 8271 5935 4302 249 244 363 C
ATOM 4163 CG2 VAL B 303 32.731 -20.911 196.761 1.00 59.09 C
ANISOU 4163 CG2 VAL B 303 10244 7181 5028 245 324 498 C
ATOM 4164 N VAL B 304 29.947 -19.193 199.944 1.00 63.52 N
ANISOU 4164 N VAL B 304 10009 7732 6393 376 -285 687 N
ATOM 4165 CA VAL B 304 29.435 -18.959 201.289 1.00 62.89 C
ANISOU 4165 CA VAL B 304 9614 7668 6615 399 -349 666 C
ATOM 4166 C VAL B 304 27.957 -19.309 201.370 1.00 61.03 C
ANISOU 4166 C VAL B 304 9281 7464 6442 457 -666 685 C
ATOM 4167 O VAL B 304 27.496 -19.879 202.365 1.00 60.58 O
ANISOU 4167 O VAL B 304 8976 7459 6584 450 -722 609 O
ATOM 4168 CB VAL B 304 29.689 -17.503 201.712 1.00 61.40 C
ANISOU 4168 CB VAL B 304 9390 7382 6558 412 -216 759 C
ATOM 4169 CG1 VAL B 304 28.985 -17.210 203.022 1.00 54.51 C
ANISOU 4169 CG1 VAL B 304 8233 6519 5958 451 -297 730 C
ATOM 4170 CG2 VAL B 304 31.177 -17.244 201.826 1.00 64.30 C
ANISOU 4170 CG2 VAL B 304 9769 7721 6940 327 102 704 C
ATOM 4171 N LEU B 305 27.190 -18.997 200.323 1.00 62.42 N
ANISOU 4171 N LEU B 305 9651 7611 6455 513 -882 787 N
ATOM 4172 CA LEU B 305 25.768 -19.320 200.353 1.00 61.20 C
ANISOU 4172 CA LEU B 305 9362 7490 6402 565 -1208 791 C
ATOM 4173 C LEU B 305 25.545 -20.828 200.361 1.00 66.08 C
ANISOU 4173 C LEU B 305 9912 8187 7008 496 -1309 641 C
ATOM 4174 O LEU B 305 24.705 -21.338 201.116 1.00 67.57 O
ANISOU 4174 O LEU B 305 9839 8408 7427 486 -1427 586 O
ATOM 4175 CB LEU B 305 25.065 -18.676 199.162 1.00 68.04 C
ANISOU 4175 CB LEU B 305 10464 8310 7078 653 -1459 931 C
ATOM 4176 CG LEU B 305 23.569 -18.935 199.005 1.00 75.42 C
ANISOU 4176 CG LEU B 305 11253 9279 8125 718 -1848 935 C
ATOM 4177 CD1 LEU B 305 22.777 -18.272 200.123 1.00 77.76 C
ANISOU 4177 CD1 LEU B 305 11203 9546 8797 786 -1869 968 C
ATOM 4178 CD2 LEU B 305 23.105 -18.429 197.648 1.00 72.74 C
ANISOU 4178 CD2 LEU B 305 11221 8903 7511 809 -2119 1068 C
ATOM 4179 N VAL B 306 26.298 -21.564 199.536 1.00 67.25 N
ANISOU 4179 N VAL B 306 10300 8350 6903 443 -1235 569 N
ATOM 4180 CA VAL B 306 26.151 -23.015 199.520 1.00 62.63 C
ANISOU 4180 CA VAL B 306 9674 7806 6315 376 -1314 414 C
ATOM 4181 C VAL B 306 26.589 -23.621 200.843 1.00 55.89 C
ANISOU 4181 C VAL B 306 8558 6968 5709 333 -1127 332 C
ATOM 4182 O VAL B 306 26.009 -24.612 201.298 1.00 61.80 O
ANISOU 4182 O VAL B 306 9156 7729 6598 290 -1230 248 O
ATOM 4183 CB VAL B 306 26.929 -23.620 198.341 1.00 64.67 C
ANISOU 4183 CB VAL B 306 10268 8061 6242 343 -1241 339 C
ATOM 4184 CG1 VAL B 306 26.911 -25.135 198.422 1.00 57.54 C
ANISOU 4184 CG1 VAL B 306 9322 7169 5372 275 -1280 160 C
ATOM 4185 CG2 VAL B 306 26.328 -23.144 197.021 1.00 61.20 C
ANISOU 4185 CG2 VAL B 306 10128 7616 5511 389 -1483 420 C
ATOM 4186 N PHE B 307 27.600 -23.035 201.490 1.00 61.21 N
ANISOU 4186 N PHE B 307 9180 7634 6444 341 -862 356 N
ATOM 4187 CA PHE B 307 28.026 -23.533 202.794 1.00 53.28 C
ANISOU 4187 CA PHE B 307 7947 6651 5647 319 -719 290 C
ATOM 4188 C PHE B 307 26.946 -23.306 203.844 1.00 54.44 C
ANISOU 4188 C PHE B 307 7841 6811 6033 335 -826 328 C
ATOM 4189 O PHE B 307 26.628 -24.212 204.632 1.00 60.31 O
ANISOU 4189 O PHE B 307 8434 7569 6913 302 -837 272 O
ATOM 4190 CB PHE B 307 29.332 -22.843 203.188 1.00 49.23 C
ANISOU 4190 CB PHE B 307 7428 6131 5145 323 -454 296 C
ATOM 4191 CG PHE B 307 29.925 -23.330 204.481 1.00 51.11 C
ANISOU 4191 CG PHE B 307 7464 6400 5555 315 -334 226 C
ATOM 4192 CD1 PHE B 307 29.487 -22.827 205.696 1.00 47.96 C
ANISOU 4192 CD1 PHE B 307 6869 6018 5335 333 -343 255 C
ATOM 4193 CD2 PHE B 307 30.943 -24.274 204.478 1.00 53.18 C
ANISOU 4193 CD2 PHE B 307 7747 6670 5791 304 -212 129 C
ATOM 4194 CE1 PHE B 307 30.038 -23.268 206.884 1.00 47.87 C
ANISOU 4194 CE1 PHE B 307 6714 6040 5432 335 -254 199 C
ATOM 4195 CE2 PHE B 307 31.505 -24.714 205.663 1.00 50.02 C
ANISOU 4195 CE2 PHE B 307 7175 6294 5534 319 -138 81 C
ATOM 4196 CZ PHE B 307 31.050 -24.211 206.868 1.00 53.47 C
ANISOU 4196 CZ PHE B 307 7448 6759 6110 332 -170 121 C
ATOM 4197 N ALA B 308 26.347 -22.110 203.846 1.00 53.60 N
ANISOU 4197 N ALA B 308 7697 6685 5985 390 -890 427 N
ATOM 4198 CA ALA B 308 25.272 -21.829 204.788 1.00 53.56 C
ANISOU 4198 CA ALA B 308 7445 6685 6219 417 -965 453 C
ATOM 4199 C ALA B 308 24.109 -22.785 204.580 1.00 51.72 C
ANISOU 4199 C ALA B 308 7113 6470 6071 384 -1183 415 C
ATOM 4200 O ALA B 308 23.546 -23.316 205.547 1.00 58.19 O
ANISOU 4200 O ALA B 308 7720 7303 7086 351 -1156 380 O
ATOM 4201 CB ALA B 308 24.810 -20.378 204.630 1.00 43.92 C
ANISOU 4201 CB ALA B 308 6222 5414 5051 503 -1011 561 C
ATOM 4202 N LEU B 309 23.772 -23.062 203.320 1.00 55.40 N
ANISOU 4202 N LEU B 309 7741 6929 6379 379 -1393 412 N
ATOM 4203 CA LEU B 309 22.660 -23.963 203.046 1.00 59.26 C
ANISOU 4203 CA LEU B 309 8124 7426 6965 329 -1634 351 C
ATOM 4204 C LEU B 309 22.984 -25.394 203.454 1.00 58.66 C
ANISOU 4204 C LEU B 309 8022 7343 6922 226 -1544 235 C
ATOM 4205 O LEU B 309 22.144 -26.077 204.049 1.00 60.17 O
ANISOU 4205 O LEU B 309 8003 7524 7335 164 -1598 196 O
ATOM 4206 CB LEU B 309 22.291 -23.898 201.566 1.00 59.49 C
ANISOU 4206 CB LEU B 309 8371 7454 6777 352 -1911 359 C
ATOM 4207 CG LEU B 309 21.512 -22.658 201.129 1.00 66.07 C
ANISOU 4207 CG LEU B 309 9189 8276 7638 467 -2110 487 C
ATOM 4208 CD1 LEU B 309 21.482 -22.559 199.615 1.00 62.55 C
ANISOU 4208 CD1 LEU B 309 9065 7830 6871 502 -2351 515 C
ATOM 4209 CD2 LEU B 309 20.097 -22.720 201.685 1.00 71.01 C
ANISOU 4209 CD2 LEU B 309 9462 8912 8606 477 -2299 475 C
ATOM 4210 N CYS B 310 24.191 -25.873 203.137 1.00 57.42 N
ANISOU 4210 N CYS B 310 8072 7177 6569 208 -1393 183 N
ATOM 4211 CA CYS B 310 24.539 -27.249 203.473 1.00 56.86 C
ANISOU 4211 CA CYS B 310 7997 7071 6536 133 -1315 78 C
ATOM 4212 C CYS B 310 24.593 -27.475 204.977 1.00 62.35 C
ANISOU 4212 C CYS B 310 8479 7764 7446 124 -1140 105 C
ATOM 4213 O CYS B 310 24.250 -28.568 205.444 1.00 65.23 O
ANISOU 4213 O CYS B 310 8765 8081 7937 54 -1139 57 O
ATOM 4214 CB CYS B 310 25.875 -27.635 202.838 1.00 52.49 C
ANISOU 4214 CB CYS B 310 7690 6501 5753 144 -1168 13 C
ATOM 4215 SG CYS B 310 25.820 -27.868 201.061 1.00 64.25 S
ANISOU 4215 SG CYS B 310 9499 7979 6936 130 -1346 -62 S
ATOM 4216 N TYR B 311 25.026 -26.478 205.751 1.00 58.13 N
ANISOU 4216 N TYR B 311 7874 7269 6945 187 -990 178 N
ATOM 4217 CA TYR B 311 25.158 -26.675 207.190 1.00 46.57 C
ANISOU 4217 CA TYR B 311 6258 5813 5624 186 -828 197 C
ATOM 4218 C TYR B 311 23.943 -26.224 207.991 1.00 51.54 C
ANISOU 4218 C TYR B 311 6666 6455 6461 183 -850 249 C
ATOM 4219 O TYR B 311 23.896 -26.482 209.200 1.00 57.35 O
ANISOU 4219 O TYR B 311 7298 7195 7296 172 -709 266 O
ATOM 4220 CB TYR B 311 26.410 -25.965 207.719 1.00 45.65 C
ANISOU 4220 CB TYR B 311 6185 5731 5429 248 -647 212 C
ATOM 4221 CG TYR B 311 27.706 -26.670 207.370 1.00 50.40 C
ANISOU 4221 CG TYR B 311 6926 6318 5906 253 -558 148 C
ATOM 4222 CD1 TYR B 311 28.243 -26.581 206.093 1.00 52.46 C
ANISOU 4222 CD1 TYR B 311 7364 6566 6003 255 -574 111 C
ATOM 4223 CD2 TYR B 311 28.399 -27.413 208.320 1.00 44.92 C
ANISOU 4223 CD2 TYR B 311 6194 5619 5256 268 -452 126 C
ATOM 4224 CE1 TYR B 311 29.431 -27.220 205.767 1.00 43.83 C
ANISOU 4224 CE1 TYR B 311 6376 5455 4824 269 -458 38 C
ATOM 4225 CE2 TYR B 311 29.592 -28.050 208.002 1.00 48.66 C
ANISOU 4225 CE2 TYR B 311 6761 6070 5656 296 -375 62 C
ATOM 4226 CZ TYR B 311 30.101 -27.947 206.724 1.00 47.37 C
ANISOU 4226 CZ TYR B 311 6744 5895 5362 294 -364 9 C
ATOM 4227 OH TYR B 311 31.278 -28.580 206.405 1.00 66.67 O
ANISOU 4227 OH TYR B 311 9260 8313 7761 330 -255 -69 O
ATOM 4228 N LEU B 312 22.970 -25.550 207.368 1.00 57.64 N
ANISOU 4228 N LEU B 312 7368 7232 7300 202 -1017 277 N
ATOM 4229 CA LEU B 312 21.780 -25.157 208.120 1.00 54.32 C
ANISOU 4229 CA LEU B 312 6699 6817 7122 208 -1018 311 C
ATOM 4230 C LEU B 312 21.017 -26.339 208.705 1.00 57.67 C
ANISOU 4230 C LEU B 312 6973 7211 7730 103 -995 278 C
ATOM 4231 O LEU B 312 20.708 -26.310 209.910 1.00 62.96 O
ANISOU 4231 O LEU B 312 7504 7885 8533 96 -813 306 O
ATOM 4232 CB LEU B 312 20.862 -24.316 207.228 1.00 58.15 C
ANISOU 4232 CB LEU B 312 7121 7302 7671 266 -1244 344 C
ATOM 4233 CG LEU B 312 19.579 -23.840 207.913 1.00 57.69 C
ANISOU 4233 CG LEU B 312 6765 7243 7911 294 -1248 368 C
ATOM 4234 CD1 LEU B 312 19.897 -22.818 209.005 1.00 64.46 C
ANISOU 4234 CD1 LEU B 312 7575 8108 8808 374 -1010 404 C
ATOM 4235 CD2 LEU B 312 18.601 -23.279 206.900 1.00 52.38 C
ANISOU 4235 CD2 LEU B 312 6010 6562 7329 357 -1543 393 C
ATOM 4236 N PRO B 313 20.668 -27.381 207.942 1.00 52.92 N
ANISOU 4236 N PRO B 313 6400 6564 7143 13 -1154 217 N
ATOM 4237 CA PRO B 313 19.806 -28.433 208.513 1.00 59.82 C
ANISOU 4237 CA PRO B 313 7102 7381 8247 -109 -1120 191 C
ATOM 4238 C PRO B 313 20.385 -29.116 209.740 1.00 61.07 C
ANISOU 4238 C PRO B 313 7302 7505 8398 -139 -853 226 C
ATOM 4239 O PRO B 313 19.676 -29.289 210.740 1.00 65.51 O
ANISOU 4239 O PRO B 313 7694 8049 9148 -188 -703 265 O
ATOM 4240 CB PRO B 313 19.648 -29.418 207.346 1.00 64.58 C
ANISOU 4240 CB PRO B 313 7803 7925 8810 -200 -1347 93 C
ATOM 4241 CG PRO B 313 19.858 -28.590 206.120 1.00 61.10 C
ANISOU 4241 CG PRO B 313 7505 7539 8173 -113 -1560 84 C
ATOM 4242 CD PRO B 313 20.920 -27.589 206.506 1.00 56.71 C
ANISOU 4242 CD PRO B 313 7070 7036 7442 8 -1375 162 C
ATOM 4243 N ILE B 314 21.677 -29.450 209.722 1.00 57.70 N
ANISOU 4243 N ILE B 314 7097 7071 7755 -99 -781 220 N
ATOM 4244 CA ILE B 314 22.240 -30.199 210.840 1.00 54.17 C
ANISOU 4244 CA ILE B 314 6709 6582 7292 -110 -577 262 C
ATOM 4245 C ILE B 314 22.472 -29.285 212.033 1.00 57.38 C
ANISOU 4245 C ILE B 314 7069 7067 7667 -28 -399 331 C
ATOM 4246 O ILE B 314 22.274 -29.689 213.184 1.00 58.01 O
ANISOU 4246 O ILE B 314 7120 7124 7796 -53 -229 388 O
ATOM 4247 CB ILE B 314 23.531 -30.917 210.410 1.00 55.85 C
ANISOU 4247 CB ILE B 314 7145 6753 7323 -76 -581 221 C
ATOM 4248 CG1 ILE B 314 24.010 -31.857 211.522 1.00 51.10 C
ANISOU 4248 CG1 ILE B 314 6607 6081 6728 -76 -416 279 C
ATOM 4249 CG2 ILE B 314 24.617 -29.911 210.052 1.00 51.71 C
ANISOU 4249 CG2 ILE B 314 6719 6318 6609 37 -577 210 C
ATOM 4250 CD1 ILE B 314 22.996 -32.932 211.915 1.00 52.36 C
ANISOU 4250 CD1 ILE B 314 6694 6117 7085 -208 -373 306 C
ATOM 4251 N SER B 315 22.869 -28.034 211.781 1.00 52.26 N
ANISOU 4251 N SER B 315 6431 6498 6926 64 -428 324 N
ATOM 4252 CA SER B 315 23.006 -27.069 212.868 1.00 57.52 C
ANISOU 4252 CA SER B 315 7052 7228 7575 134 -275 358 C
ATOM 4253 C SER B 315 21.676 -26.855 213.577 1.00 58.10 C
ANISOU 4253 C SER B 315 6924 7297 7854 99 -181 386 C
ATOM 4254 O SER B 315 21.595 -26.913 214.813 1.00 64.23 O
ANISOU 4254 O SER B 315 7692 8087 8627 101 14 420 O
ATOM 4255 CB SER B 315 23.537 -25.743 212.319 1.00 54.69 C
ANISOU 4255 CB SER B 315 6731 6918 7129 219 -332 337 C
ATOM 4256 OG SER B 315 24.771 -25.938 211.651 1.00 54.40 O
ANISOU 4256 OG SER B 315 6862 6884 6925 240 -376 307 O
ATOM 4257 N VAL B 316 20.613 -26.625 212.801 1.00 56.84 N
ANISOU 4257 N VAL B 316 6602 7121 7874 71 -318 369 N
ATOM 4258 CA VAL B 316 19.298 -26.405 213.391 1.00 60.83 C
ANISOU 4258 CA VAL B 316 6861 7620 8633 43 -225 382 C
ATOM 4259 C VAL B 316 18.826 -27.649 214.130 1.00 58.53 C
ANISOU 4259 C VAL B 316 6523 7267 8449 -82 -71 409 C
ATOM 4260 O VAL B 316 18.292 -27.562 215.244 1.00 65.41 O
ANISOU 4260 O VAL B 316 7300 8141 9411 -97 166 443 O
ATOM 4261 CB VAL B 316 18.291 -25.983 212.304 1.00 62.19 C
ANISOU 4261 CB VAL B 316 6847 7784 9000 48 -460 353 C
ATOM 4262 CG1 VAL B 316 16.870 -26.061 212.838 1.00 60.26 C
ANISOU 4262 CG1 VAL B 316 6291 7518 9087 -6 -370 350 C
ATOM 4263 CG2 VAL B 316 18.606 -24.576 211.807 1.00 63.15 C
ANISOU 4263 CG2 VAL B 316 7015 7942 9037 188 -555 361 C
ATOM 4264 N LEU B 317 19.024 -28.829 213.533 1.00 56.87 N
ANISOU 4264 N LEU B 317 6399 6986 8225 -176 -179 395 N
ATOM 4265 CA LEU B 317 18.552 -30.052 214.171 1.00 64.45 C
ANISOU 4265 CA LEU B 317 7327 7848 9311 -308 -29 431 C
ATOM 4266 C LEU B 317 19.275 -30.300 215.486 1.00 65.28 C
ANISOU 4266 C LEU B 317 7612 7955 9237 -271 223 517 C
ATOM 4267 O LEU B 317 18.654 -30.694 216.479 1.00 67.37 O
ANISOU 4267 O LEU B 317 7821 8177 9601 -340 455 581 O
ATOM 4268 CB LEU B 317 18.736 -31.244 213.228 1.00 66.99 C
ANISOU 4268 CB LEU B 317 7741 8067 9643 -407 -204 382 C
ATOM 4269 CG LEU B 317 17.813 -31.346 212.010 1.00 70.84 C
ANISOU 4269 CG LEU B 317 8057 8531 10330 -489 -468 286 C
ATOM 4270 CD1 LEU B 317 18.211 -32.532 211.144 1.00 67.51 C
ANISOU 4270 CD1 LEU B 317 7798 8001 9853 -576 -622 213 C
ATOM 4271 CD2 LEU B 317 16.360 -31.468 212.443 1.00 67.47 C
ANISOU 4271 CD2 LEU B 317 7308 8067 10262 -606 -386 286 C
ATOM 4272 N ASN B 318 20.589 -30.071 215.520 1.00 64.33 N
ANISOU 4272 N ASN B 318 7709 7883 8850 -162 181 519 N
ATOM 4273 CA ASN B 318 21.320 -30.303 216.758 1.00 71.03 C
ANISOU 4273 CA ASN B 318 8736 8743 9512 -109 362 595 C
ATOM 4274 C ASN B 318 21.005 -29.260 217.819 1.00 71.24 C
ANISOU 4274 C ASN B 318 8710 8860 9499 -49 545 609 C
ATOM 4275 O ASN B 318 21.025 -29.578 219.012 1.00 72.41 O
ANISOU 4275 O ASN B 318 8963 9001 9547 -51 749 684 O
ATOM 4276 CB ASN B 318 22.817 -30.361 216.482 1.00 75.94 C
ANISOU 4276 CB ASN B 318 9559 9393 9904 -8 243 575 C
ATOM 4277 CG ASN B 318 23.300 -31.773 216.282 1.00 89.93 C
ANISOU 4277 CG ASN B 318 11471 11041 11656 -45 207 608 C
ATOM 4278 OD1 ASN B 318 23.702 -32.442 217.232 1.00 92.89 O
ANISOU 4278 OD1 ASN B 318 11814 11332 12147 -121 88 556 O
ATOM 4279 ND2 ASN B 318 23.279 -32.236 215.038 1.00100.62 N
ANISOU 4279 ND2 ASN B 318 12996 12374 12863 16 299 691 N
ATOM 4280 N VAL B 319 20.709 -28.020 217.426 1.00 63.01 N
ANISOU 4280 N VAL B 319 7531 7890 8519 9 485 540 N
ATOM 4281 CA VAL B 319 20.244 -27.067 218.428 1.00 59.96 C
ANISOU 4281 CA VAL B 319 7079 7563 8139 60 685 532 C
ATOM 4282 C VAL B 319 18.891 -27.498 218.981 1.00 68.50 C
ANISOU 4282 C VAL B 319 7983 8593 9451 -39 898 571 C
ATOM 4283 O VAL B 319 18.647 -27.419 220.190 1.00 79.21 O
ANISOU 4283 O VAL B 319 9391 9966 10739 -35 1164 606 O
ATOM 4284 CB VAL B 319 20.190 -25.644 217.848 1.00 56.14 C
ANISOU 4284 CB VAL B 319 6489 7132 7710 153 577 453 C
ATOM 4285 CG1 VAL B 319 19.181 -24.808 218.619 1.00 46.55 C
ANISOU 4285 CG1 VAL B 319 5110 5933 6643 184 785 427 C
ATOM 4286 CG2 VAL B 319 21.565 -25.006 217.912 1.00 51.61 C
ANISOU 4286 CG2 VAL B 319 6108 6614 6888 245 503 414 C
ATOM 4287 N LEU B 320 17.994 -27.971 218.111 1.00 65.64 N
ANISOU 4287 N LEU B 320 7410 8166 9362 -136 793 558 N
ATOM 4288 CA LEU B 320 16.680 -28.407 218.574 1.00 69.16 C
ANISOU 4288 CA LEU B 320 7634 8555 10091 -252 1001 582 C
ATOM 4289 C LEU B 320 16.778 -29.627 219.479 1.00 73.66 C
ANISOU 4289 C LEU B 320 8371 9041 10578 -358 1229 688 C
ATOM 4290 O LEU B 320 15.973 -29.781 220.404 1.00 79.10 O
ANISOU 4290 O LEU B 320 8977 9700 11378 -426 1537 735 O
ATOM 4291 CB LEU B 320 15.774 -28.706 217.378 1.00 75.38 C
ANISOU 4291 CB LEU B 320 8150 9289 11201 -343 780 526 C
ATOM 4292 CG LEU B 320 15.478 -27.540 216.426 1.00 78.75 C
ANISOU 4292 CG LEU B 320 8404 9780 11736 -234 535 448 C
ATOM 4293 CD1 LEU B 320 14.630 -28.001 215.247 1.00 78.91 C
ANISOU 4293 CD1 LEU B 320 8194 9752 12036 -327 266 394 C
ATOM 4294 CD2 LEU B 320 14.789 -26.398 217.160 1.00 70.08 C
ANISOU 4294 CD2 LEU B 320 7121 8730 10775 -140 738 426 C
ATOM 4295 N LYS B 321 17.751 -30.502 219.227 1.00 78.44 N
ANISOU 4295 N LYS B 321 9215 9593 10994 -366 1100 732 N
ATOM 4296 CA LYS B 321 17.912 -31.707 220.033 1.00 71.07 C
ANISOU 4296 CA LYS B 321 8477 8551 9978 -447 1289 855 C
ATOM 4297 C LYS B 321 18.604 -31.409 221.361 1.00 74.05 C
ANISOU 4297 C LYS B 321 9116 8996 10025 -340 1483 934 C
ATOM 4298 O LYS B 321 18.124 -31.815 222.426 1.00 76.49 O
ANISOU 4298 O LYS B 321 9502 9257 10304 -399 1783 1036 O
ATOM 4299 CB LYS B 321 18.702 -32.742 219.231 1.00 58.07 C
ANISOU 4299 CB LYS B 321 6984 6804 8275 -471 1066 862 C
ATOM 4300 CG LYS B 321 19.150 -33.961 219.997 1.00 58.07 C
ANISOU 4300 CG LYS B 321 7244 6671 8150 -507 1209 1003 C
ATOM 4301 CD LYS B 321 20.102 -34.785 219.140 1.00 64.42 C
ANISOU 4301 CD LYS B 321 8200 7386 8890 -479 967 979 C
ATOM 4302 CE LYS B 321 20.477 -36.087 219.817 1.00 70.33 C
ANISOU 4302 CE LYS B 321 9199 7960 9564 -508 1091 1127 C
ATOM 4303 NZ LYS B 321 21.442 -36.864 218.993 1.00 77.29 N
ANISOU 4303 NZ LYS B 321 10222 8743 10403 -455 870 1088 N
ATOM 4304 N ARG B 322 19.723 -30.681 221.312 1.00 71.08 N
ANISOU 4304 N ARG B 322 8882 8729 9394 -187 1316 884 N
ATOM 4305 CA ARG B 322 20.576 -30.516 222.482 1.00 65.47 C
ANISOU 4305 CA ARG B 322 8449 8085 8344 -81 1413 941 C
ATOM 4306 C ARG B 322 20.115 -29.393 223.392 1.00 67.52 C
ANISOU 4306 C ARG B 322 8676 8448 8531 -30 1624 891 C
ATOM 4307 O ARG B 322 20.302 -29.473 224.610 1.00 75.04 O
ANISOU 4307 O ARG B 322 9851 9427 9235 5 1816 959 O
ATOM 4308 CB ARG B 322 22.011 -30.242 222.047 1.00 61.12 C
ANISOU 4308 CB ARG B 322 8032 7600 7590 47 1137 885 C
ATOM 4309 CG ARG B 322 22.632 -31.347 221.225 1.00 60.96 C
ANISOU 4309 CG ARG B 322 8078 7476 7607 27 951 919 C
ATOM 4310 CD ARG B 322 22.797 -32.589 222.056 1.00 52.09 C
ANISOU 4310 CD ARG B 322 7179 6237 6376 8 1070 1077 C
ATOM 4311 NE ARG B 322 23.455 -33.659 221.316 1.00 61.98 N
ANISOU 4311 NE ARG B 322 8511 7366 7672 10 900 1099 N
ATOM 4312 CZ ARG B 322 23.810 -34.824 221.851 1.00 65.42 C
ANISOU 4312 CZ ARG B 322 9162 7666 8028 22 948 1239 C
ATOM 4313 NH1 ARG B 322 23.575 -35.063 223.137 1.00 66.65 N
ANISOU 4313 NH1 ARG B 322 9498 7802 8024 27 1157 1386 N
ATOM 4314 NH2 ARG B 322 24.406 -35.745 221.105 1.00 63.27 N
ANISOU 4314 NH2 ARG B 322 8947 7267 7826 37 795 1235 N
ATOM 4315 N VAL B 323 19.555 -28.328 222.830 1.00 65.32 N
ANISOU 4315 N VAL B 323 8151 8223 8446 -11 1586 771 N
ATOM 4316 CA VAL B 323 19.154 -27.169 223.612 1.00 72.70 C
ANISOU 4316 CA VAL B 323 9048 9239 9337 56 1780 695 C
ATOM 4317 C VAL B 323 17.670 -27.198 223.949 1.00 75.01 C
ANISOU 4317 C VAL B 323 9110 9483 9907 -35 2082 707 C
ATOM 4318 O VAL B 323 17.275 -26.776 225.036 1.00 83.82 O
ANISOU 4318 O VAL B 323 10289 10633 10926 -11 2382 696 O
ATOM 4319 CB VAL B 323 19.532 -25.873 222.868 1.00 68.33 C
ANISOU 4319 CB VAL B 323 8384 8751 8827 158 1568 559 C
ATOM 4320 CG1 VAL B 323 19.289 -24.671 223.759 1.00 63.23 C
ANISOU 4320 CG1 VAL B 323 7750 8168 8108 242 1765 463 C
ATOM 4321 CG2 VAL B 323 20.984 -25.930 222.428 1.00 60.50 C
ANISOU 4321 CG2 VAL B 323 7575 7794 7617 222 1293 545 C
ATOM 4322 N PHE B 324 16.839 -27.703 223.041 1.00 74.56 N
ANISOU 4322 N PHE B 324 8782 9347 10200 -142 2013 716 N
ATOM 4323 CA PHE B 324 15.400 -27.732 223.249 1.00 75.92 C
ANISOU 4323 CA PHE B 324 8660 9472 10715 -238 2276 709 C
ATOM 4324 C PHE B 324 14.863 -29.119 223.570 1.00 86.09 C
ANISOU 4324 C PHE B 324 9957 10637 12115 -417 2475 834 C
ATOM 4325 O PHE B 324 13.649 -29.273 223.740 1.00 87.48 O
ANISOU 4325 O PHE B 324 9861 10759 12619 -528 2718 831 O
ATOM 4326 CB PHE B 324 14.687 -27.163 222.022 1.00 74.46 C
ANISOU 4326 CB PHE B 324 8106 9285 10902 -230 2044 609 C
ATOM 4327 CG PHE B 324 15.004 -25.722 221.774 1.00 76.54 C
ANISOU 4327 CG PHE B 324 8341 9631 11109 -58 1912 503 C
ATOM 4328 CD1 PHE B 324 14.248 -24.724 222.365 1.00 77.46 C
ANISOU 4328 CD1 PHE B 324 8292 9773 11367 18 2148 428 C
ATOM 4329 CD2 PHE B 324 16.075 -25.362 220.977 1.00 73.71 C
ANISOU 4329 CD2 PHE B 324 8132 9309 10566 25 1584 477 C
ATOM 4330 CE1 PHE B 324 14.545 -23.395 222.151 1.00 74.09 C
ANISOU 4330 CE1 PHE B 324 7857 9388 10904 175 2035 332 C
ATOM 4331 CE2 PHE B 324 16.376 -24.033 220.759 1.00 72.41 C
ANISOU 4331 CE2 PHE B 324 7957 9192 10365 166 1486 390 C
ATOM 4332 CZ PHE B 324 15.607 -23.049 221.346 1.00 74.28 C
ANISOU 4332 CZ PHE B 324 8038 9436 10748 242 1702 319 C
ATOM 4333 N GLY B 325 15.725 -30.128 223.648 1.00 88.88 N
ANISOU 4333 N GLY B 325 10603 10932 12237 -448 2386 942 N
ATOM 4334 CA GLY B 325 15.274 -31.440 224.075 1.00 85.15 C
ANISOU 4334 CA GLY B 325 10194 10310 11847 -615 2609 1080 C
ATOM 4335 C GLY B 325 14.244 -32.067 223.166 1.00 87.02 C
ANISOU 4335 C GLY B 325 10083 10431 12551 -794 2556 1045 C
ATOM 4336 O GLY B 325 13.435 -32.878 223.625 1.00103.94 O
ANISOU 4336 O GLY B 325 12154 12446 14892 -964 2846 1128 O
ATOM 4337 N MET B 326 14.245 -31.705 221.886 1.00 85.16 N
ANISOU 4337 N MET B 326 9636 10230 12493 -766 2192 921 N
ATOM 4338 CA MET B 326 13.314 -32.268 220.922 1.00 84.33 C
ANISOU 4338 CA MET B 326 9202 10026 12812 -928 2060 859 C
ATOM 4339 C MET B 326 13.797 -33.625 220.412 1.00 83.66 C
ANISOU 4339 C MET B 326 9295 9788 12703 -1045 1908 911 C
ATOM 4340 O MET B 326 14.954 -34.016 220.595 1.00 79.71 O
ANISOU 4340 O MET B 326 9147 9272 11866 -962 1836 984 O
ATOM 4341 CB MET B 326 13.108 -31.314 219.747 1.00 83.96 C
ANISOU 4341 CB MET B 326 8898 10079 12923 -836 1707 711 C
ATOM 4342 CG MET B 326 12.329 -30.058 220.095 1.00 95.58 C
ANISOU 4342 CG MET B 326 10102 11653 14561 -740 1850 644 C
ATOM 4343 SD MET B 326 12.042 -28.996 218.664 1.00104.83 S
ANISOU 4343 SD MET B 326 10995 12907 15930 -619 1407 505 S
ATOM 4344 CE MET B 326 11.144 -30.116 217.591 1.00106.82 C
ANISOU 4344 CE MET B 326 10959 13045 16585 -832 1171 452 C
ATOM 4345 N PHE B 327 12.878 -34.351 219.776 1.00 87.62 N
ANISOU 4345 N PHE B 327 9532 10165 13596 -1238 1857 860 N
ATOM 4346 CA PHE B 327 13.127 -35.621 219.090 1.00 91.46 C
ANISOU 4346 CA PHE B 327 10122 10477 14151 -1374 1684 860 C
ATOM 4347 C PHE B 327 13.315 -36.791 220.046 1.00101.77 C
ANISOU 4347 C PHE B 327 11695 11596 15379 -1485 1999 1033 C
ATOM 4348 O PHE B 327 13.726 -37.873 219.600 1.00107.58 O
ANISOU 4348 O PHE B 327 12594 12161 16119 -1566 1876 1050 O
ATOM 4349 CB PHE B 327 14.354 -35.535 218.173 1.00 88.29 C
ANISOU 4349 CB PHE B 327 9956 10130 13459 -1226 1304 800 C
ATOM 4350 CG PHE B 327 14.355 -34.331 217.266 1.00 83.68 C
ANISOU 4350 CG PHE B 327 9203 9723 12870 -1093 1007 665 C
ATOM 4351 CD1 PHE B 327 13.213 -33.970 216.567 1.00 79.88 C
ANISOU 4351 CD1 PHE B 327 8338 9264 12747 -1170 868 550 C
ATOM 4352 CD2 PHE B 327 15.493 -33.555 217.126 1.00 71.98 C
ANISOU 4352 CD2 PHE B 327 7940 8372 11037 -889 864 661 C
ATOM 4353 CE1 PHE B 327 13.210 -32.861 215.738 1.00 72.43 C
ANISOU 4353 CE1 PHE B 327 7272 8465 11784 -1030 584 454 C
ATOM 4354 CE2 PHE B 327 15.497 -32.444 216.299 1.00 74.58 C
ANISOU 4354 CE2 PHE B 327 8144 8836 11358 -772 617 561 C
ATOM 4355 CZ PHE B 327 14.353 -32.097 215.604 1.00 75.74 C
ANISOU 4355 CZ PHE B 327 7946 8996 11834 -834 474 468 C
ATOM 4356 N ARG B 328 13.045 -36.618 221.341 1.00110.11 N
ANISOU 4356 N ARG B 328 12828 12665 16345 -1484 2406 1166 N
ATOM 4357 CA ARG B 328 13.213 -37.718 222.285 1.00118.04 C
ANISOU 4357 CA ARG B 328 14131 13481 17240 -1581 2717 1364 C
ATOM 4358 C ARG B 328 12.112 -38.768 222.179 1.00129.12 C
ANISOU 4358 C ARG B 328 15316 14648 19095 -1875 2913 1382 C
ATOM 4359 O ARG B 328 12.341 -39.923 222.556 1.00132.32 O
ANISOU 4359 O ARG B 328 15980 14830 19467 -1980 3063 1529 O
ATOM 4360 CB ARG B 328 13.291 -37.168 223.710 1.00120.53 C
ANISOU 4360 CB ARG B 328 14646 13892 17260 -1482 3094 1501 C
ATOM 4361 CG ARG B 328 14.658 -36.586 224.063 1.00120.99 C
ANISOU 4361 CG ARG B 328 15064 14104 16804 -1220 2922 1535 C
ATOM 4362 CD ARG B 328 14.590 -35.627 225.246 1.00125.81 C
ANISOU 4362 CD ARG B 328 15775 14873 17153 -1105 3211 1574 C
ATOM 4363 NE ARG B 328 15.920 -35.304 225.758 1.00129.09 N
ANISOU 4363 NE ARG B 328 16577 15398 17071 -888 3065 1626 N
ATOM 4364 CZ ARG B 328 16.168 -34.372 226.674 1.00132.17 C
ANISOU 4364 CZ ARG B 328 17114 15950 17154 -750 3202 1618 C
ATOM 4365 NH1 ARG B 328 15.174 -33.656 227.181 1.00131.85 N
ANISOU 4365 NH1 ARG B 328 16878 15975 17244 -794 3519 1562 N
ATOM 4366 NH2 ARG B 328 17.412 -34.154 227.080 1.00133.68 N
ANISOU 4366 NH2 ARG B 328 17636 16233 16923 -566 3018 1650 N
ATOM 4367 N GLN B 329 10.942 -38.412 221.657 1.00140.08 N
ANISOU 4367 N GLN B 329 16230 16067 20927 -2008 2900 1233 N
ATOM 4368 CA GLN B 329 9.818 -39.345 221.605 1.00151.45 C
ANISOU 4368 CA GLN B 329 17402 17288 22856 -2311 3104 1228 C
ATOM 4369 C GLN B 329 9.953 -40.330 220.447 1.00155.19 C
ANISOU 4369 C GLN B 329 17859 17584 23523 -2447 2747 1121 C
ATOM 4370 O GLN B 329 10.677 -40.079 219.484 1.00157.06 O
ANISOU 4370 O GLN B 329 18175 17912 23587 -2306 2314 1003 O
ATOM 4371 CB GLN B 329 8.496 -38.582 221.494 1.00162.54 C
ANISOU 4371 CB GLN B 329 18257 18796 24704 -2394 3207 1091 C
ATOM 4372 CG GLN B 329 8.107 -37.819 222.752 1.00171.32 C
ANISOU 4372 CG GLN B 329 19398 20051 25644 -2278 3613 1165 C
ATOM 4373 CD GLN B 329 6.909 -36.914 222.535 1.00177.87 C
ANISOU 4373 CD GLN B 329 19726 21027 26830 -2255 3595 988 C
ATOM 4374 OE1 GLN B 329 6.675 -36.433 221.425 1.00177.56 O
ANISOU 4374 OE1 GLN B 329 19356 21059 27048 -2232 3215 824 O
ATOM 4375 NE2 GLN B 329 6.141 -36.681 223.594 1.00184.20 N
ANISOU 4375 NE2 GLN B 329 20485 21865 27637 -2247 3990 1020 N
ATOM 4376 N ARG B 333 10.000 -41.684 214.915 1.00109.71 N
ANISOU 4376 N ARG B 333 11703 11659 18324 -2686 914 287 N
ATOM 4377 CA ARG B 333 11.443 -41.882 214.884 1.00107.45 C
ANISOU 4377 CA ARG B 333 11902 11365 17559 -2485 847 367 C
ATOM 4378 C ARG B 333 11.960 -41.941 213.451 1.00102.86 C
ANISOU 4378 C ARG B 333 11415 10818 16847 -2422 372 158 C
ATOM 4379 O ARG B 333 13.081 -41.513 213.168 1.00 96.18 O
ANISOU 4379 O ARG B 333 10849 10095 15599 -2191 233 173 O
ATOM 4380 CB ARG B 333 11.828 -43.160 215.637 1.00115.45 C
ANISOU 4380 CB ARG B 333 13223 12084 18560 -2595 1151 528 C
ATOM 4381 CG ARG B 333 11.538 -43.114 217.131 1.00128.30 C
ANISOU 4381 CG ARG B 333 14884 13679 20186 -2621 1650 774 C
ATOM 4382 CD ARG B 333 12.012 -44.377 217.843 1.00138.25 C
ANISOU 4382 CD ARG B 333 16513 14633 21382 -2699 1922 966 C
ATOM 4383 NE ARG B 333 11.785 -44.302 219.285 1.00147.39 N
ANISOU 4383 NE ARG B 333 17767 15772 22464 -2707 2402 1220 N
ATOM 4384 CZ ARG B 333 12.158 -45.235 220.156 1.00152.86 C
ANISOU 4384 CZ ARG B 333 18815 16221 23044 -2742 2699 1451 C
ATOM 4385 NH1 ARG B 333 12.782 -46.328 219.738 1.00156.17 N
ANISOU 4385 NH1 ARG B 333 19505 16379 23452 -2766 2567 1458 N
ATOM 4386 NH2 ARG B 333 11.908 -45.075 221.448 1.00154.19 N
ANISOU 4386 NH2 ARG B 333 19094 16435 23055 -2715 3094 1661 N
ATOM 4387 N GLU B 334 11.136 -42.471 212.544 1.00105.15 N
ANISOU 4387 N GLU B 334 11471 11001 17481 -2636 129 -46 N
ATOM 4388 CA GLU B 334 11.574 -42.644 211.163 1.00106.02 C
ANISOU 4388 CA GLU B 334 11713 11122 17449 -2599 -312 -260 C
ATOM 4389 C GLU B 334 11.873 -41.303 210.503 1.00101.70 C
ANISOU 4389 C GLU B 334 11133 10884 16624 -2358 -600 -313 C
ATOM 4390 O GLU B 334 12.931 -41.125 209.887 1.00103.18 O
ANISOU 4390 O GLU B 334 11630 11142 16431 -2180 -774 -348 O
ATOM 4391 CB GLU B 334 10.517 -43.418 210.376 1.00112.38 C
ANISOU 4391 CB GLU B 334 12250 11760 18688 -2890 -537 -486 C
ATOM 4392 CG GLU B 334 10.491 -44.904 210.691 1.00122.01 C
ANISOU 4392 CG GLU B 334 13615 12617 20126 -3127 -329 -479 C
ATOM 4393 CD GLU B 334 9.285 -45.608 210.102 1.00136.29 C
ANISOU 4393 CD GLU B 334 15098 14270 22417 -3442 -499 -699 C
ATOM 4394 OE1 GLU B 334 8.197 -44.992 210.060 1.00140.60 O
ANISOU 4394 OE1 GLU B 334 15242 15008 23172 -3474 -570 -748 O
ATOM 4395 OE2 GLU B 334 9.424 -46.776 209.679 1.00143.09 O
ANISOU 4395 OE2 GLU B 334 16169 14897 23302 -3572 -552 -810 O
ATOM 4396 N ALA B 335 10.958 -40.337 210.631 1.00102.39 N
ANISOU 4396 N ALA B 335 10845 11145 16912 -2344 -633 -314 N
ATOM 4397 CA ALA B 335 11.199 -39.031 210.028 1.00 98.29 C
ANISOU 4397 CA ALA B 335 10304 10890 16149 -2111 -897 -343 C
ATOM 4398 C ALA B 335 12.403 -38.338 210.651 1.00 91.45 C
ANISOU 4398 C ALA B 335 9748 10148 14851 -1858 -700 -172 C
ATOM 4399 O ALA B 335 13.161 -37.661 209.946 1.00 88.11 O
ANISOU 4399 O ALA B 335 9511 9865 14101 -1672 -921 -205 O
ATOM 4400 CB ALA B 335 9.953 -38.151 210.162 1.00 93.52 C
ANISOU 4400 CB ALA B 335 9223 10419 15893 -2129 -939 -363 C
ATOM 4401 N VAL B 336 12.620 -38.527 211.955 1.00 95.89 N
ANISOU 4401 N VAL B 336 10386 10651 15396 -1857 -289 9 N
ATOM 4402 CA VAL B 336 13.741 -37.878 212.625 1.00 97.74 C
ANISOU 4402 CA VAL B 336 10896 11006 15237 -1626 -123 157 C
ATOM 4403 C VAL B 336 15.062 -38.412 212.092 1.00 95.72 C
ANISOU 4403 C VAL B 336 11031 10693 14647 -1529 -248 133 C
ATOM 4404 O VAL B 336 15.974 -37.645 211.756 1.00 91.72 O
ANISOU 4404 O VAL B 336 10690 10337 13823 -1329 -363 133 O
ATOM 4405 CB VAL B 336 13.638 -38.075 214.148 1.00 94.03 C
ANISOU 4405 CB VAL B 336 10453 10474 14801 -1656 326 348 C
ATOM 4406 CG1 VAL B 336 14.946 -37.675 214.822 1.00 88.32 C
ANISOU 4406 CG1 VAL B 336 10071 9838 13647 -1435 450 482 C
ATOM 4407 CG2 VAL B 336 12.471 -37.283 214.711 1.00 91.32 C
ANISOU 4407 CG2 VAL B 336 9732 10228 14735 -1697 493 366 C
ATOM 4408 N TYR B 337 15.194 -39.738 212.027 1.00 96.88 N
ANISOU 4408 N TYR B 337 11323 10603 14883 -1669 -204 111 N
ATOM 4409 CA TYR B 337 16.415 -40.316 211.487 1.00103.81 C
ANISOU 4409 CA TYR B 337 12551 11404 15488 -1570 -310 68 C
ATOM 4410 C TYR B 337 16.588 -39.986 210.013 1.00 95.45 C
ANISOU 4410 C TYR B 337 11518 10438 14309 -1525 -683 -134 C
ATOM 4411 O TYR B 337 17.716 -39.774 209.564 1.00 91.57 O
ANISOU 4411 O TYR B 337 11277 10012 13503 -1356 -759 -155 O
ATOM 4412 CB TYR B 337 16.432 -41.826 211.708 1.00114.83 C
ANISOU 4412 CB TYR B 337 14092 12491 17045 -1730 -182 79 C
ATOM 4413 CG TYR B 337 16.975 -42.218 213.063 1.00129.84 C
ANISOU 4413 CG TYR B 337 16185 14296 18851 -1665 163 315 C
ATOM 4414 CD1 TYR B 337 18.309 -42.574 213.222 1.00133.06 C
ANISOU 4414 CD1 TYR B 337 16926 14655 18977 -1482 187 384 C
ATOM 4415 CD2 TYR B 337 16.159 -42.215 214.187 1.00138.09 C
ANISOU 4415 CD2 TYR B 337 17082 15303 20083 -1776 462 471 C
ATOM 4416 CE1 TYR B 337 18.810 -42.928 214.460 1.00137.91 C
ANISOU 4416 CE1 TYR B 337 17730 15185 19484 -1403 455 608 C
ATOM 4417 CE2 TYR B 337 16.652 -42.567 215.429 1.00141.30 C
ANISOU 4417 CE2 TYR B 337 17712 15625 20351 -1709 766 699 C
ATOM 4418 CZ TYR B 337 17.978 -42.923 215.560 1.00142.01 C
ANISOU 4418 CZ TYR B 337 18143 15669 20144 -1518 737 771 C
ATOM 4419 OH TYR B 337 18.474 -43.274 216.795 1.00145.07 O
ANISOU 4419 OH TYR B 337 18769 15977 20376 -1432 994 1006 O
ATOM 4420 N ALA B 338 15.495 -39.898 209.250 1.00 84.72 N
ANISOU 4420 N ALA B 338 9906 9096 13190 -1668 -920 -282 N
ATOM 4421 CA ALA B 338 15.637 -39.489 207.858 1.00 86.67 C
ANISOU 4421 CA ALA B 338 10215 9450 13265 -1608 -1292 -457 C
ATOM 4422 C ALA B 338 16.209 -38.080 207.766 1.00 80.93 C
ANISOU 4422 C ALA B 338 9532 8972 12243 -1372 -1335 -378 C
ATOM 4423 O ALA B 338 17.132 -37.822 206.980 1.00 80.30 O
ANISOU 4423 O ALA B 338 9705 8960 11845 -1240 -1464 -433 O
ATOM 4424 CB ALA B 338 14.288 -39.580 207.145 1.00 84.47 C
ANISOU 4424 CB ALA B 338 9630 9159 13306 -1793 -1575 -621 C
ATOM 4425 N ALA B 339 15.712 -37.167 208.604 1.00 75.88 N
ANISOU 4425 N ALA B 339 8663 8456 11711 -1319 -1190 -248 N
ATOM 4426 CA ALA B 339 16.195 -35.792 208.568 1.00 72.94 C
ANISOU 4426 CA ALA B 339 8324 8292 11099 -1107 -1218 -177 C
ATOM 4427 C ALA B 339 17.661 -35.713 208.982 1.00 74.01 C
ANISOU 4427 C ALA B 339 8769 8448 10901 -951 -1037 -87 C
ATOM 4428 O ALA B 339 18.469 -35.049 208.319 1.00 74.42 O
ANISOU 4428 O ALA B 339 8990 8607 10680 -809 -1151 -110 O
ATOM 4429 CB ALA B 339 15.325 -34.911 209.466 1.00 69.24 C
ANISOU 4429 CB ALA B 339 7544 7917 10848 -1088 -1068 -76 C
ATOM 4430 N PHE B 340 18.028 -36.393 210.072 1.00 71.28 N
ANISOU 4430 N PHE B 340 8504 7998 10582 -975 -758 19 N
ATOM 4431 CA PHE B 340 19.415 -36.339 210.529 1.00 67.24 C
ANISOU 4431 CA PHE B 340 8254 7511 9784 -816 -617 101 C
ATOM 4432 C PHE B 340 20.358 -36.988 209.523 1.00 68.90 C
ANISOU 4432 C PHE B 340 8716 7647 9816 -779 -755 -13 C
ATOM 4433 O PHE B 340 21.474 -36.495 209.297 1.00 70.03 O
ANISOU 4433 O PHE B 340 9022 7881 9705 -622 -755 -10 O
ATOM 4434 CB PHE B 340 19.543 -37.003 211.901 1.00 66.75 C
ANISOU 4434 CB PHE B 340 8244 7340 9778 -842 -324 250 C
ATOM 4435 CG PHE B 340 19.259 -36.077 213.052 1.00 65.01 C
ANISOU 4435 CG PHE B 340 7903 7246 9550 -780 -125 379 C
ATOM 4436 CD1 PHE B 340 17.974 -35.942 213.551 1.00 65.49 C
ANISOU 4436 CD1 PHE B 340 7705 7299 9881 -904 -9 408 C
ATOM 4437 CD2 PHE B 340 20.280 -35.338 213.631 1.00 63.60 C
ANISOU 4437 CD2 PHE B 340 7863 7194 9110 -601 -47 451 C
ATOM 4438 CE1 PHE B 340 17.712 -35.087 214.607 1.00 69.38 C
ANISOU 4438 CE1 PHE B 340 8104 7901 10354 -840 203 506 C
ATOM 4439 CE2 PHE B 340 20.025 -34.484 214.686 1.00 60.89 C
ANISOU 4439 CE2 PHE B 340 7436 6960 8740 -546 132 542 C
ATOM 4440 CZ PHE B 340 18.739 -34.357 215.176 1.00 67.02 C
ANISOU 4440 CZ PHE B 340 7981 7724 9761 -660 269 569 C
ATOM 4441 N THR B 341 19.914 -38.071 208.878 1.00 71.92 N
ANISOU 4441 N THR B 341 9124 7860 10341 -928 -865 -134 N
ATOM 4442 CA THR B 341 20.739 -38.737 207.878 1.00 71.00 C
ANISOU 4442 CA THR B 341 9258 7657 10063 -897 -980 -273 C
ATOM 4443 C THR B 341 20.982 -37.822 206.688 1.00 66.14 C
ANISOU 4443 C THR B 341 8702 7208 9220 -810 -1199 -377 C
ATOM 4444 O THR B 341 22.124 -37.659 206.228 1.00 66.76 O
ANISOU 4444 O THR B 341 8992 7328 9045 -676 -1176 -408 O
ATOM 4445 CB THR B 341 20.054 -40.032 207.432 1.00 78.40 C
ANISOU 4445 CB THR B 341 10199 8365 11224 -1097 -1066 -407 C
ATOM 4446 OG1 THR B 341 19.899 -40.907 208.556 1.00 82.01 O
ANISOU 4446 OG1 THR B 341 10641 8637 11883 -1177 -827 -283 O
ATOM 4447 CG2 THR B 341 20.861 -40.735 206.351 1.00 76.21 C
ANISOU 4447 CG2 THR B 341 10197 7985 10774 -1064 -1177 -584 C
ATOM 4448 N PHE B 342 19.914 -37.194 206.191 1.00 67.10 N
ANISOU 4448 N PHE B 342 8635 7423 9437 -878 -1404 -421 N
ATOM 4449 CA PHE B 342 20.069 -36.285 205.068 1.00 69.48 C
ANISOU 4449 CA PHE B 342 9021 7874 9506 -788 -1623 -488 C
ATOM 4450 C PHE B 342 20.953 -35.102 205.439 1.00 71.16 C
ANISOU 4450 C PHE B 342 9288 8242 9508 -603 -1482 -356 C
ATOM 4451 O PHE B 342 21.749 -34.632 204.618 1.00 73.22 O
ANISOU 4451 O PHE B 342 9748 8573 9498 -502 -1533 -394 O
ATOM 4452 CB PHE B 342 18.697 -35.812 204.595 1.00 70.91 C
ANISOU 4452 CB PHE B 342 8960 8118 9862 -874 -1892 -535 C
ATOM 4453 CG PHE B 342 18.760 -34.791 203.507 1.00 70.33 C
ANISOU 4453 CG PHE B 342 8987 8194 9543 -764 -2134 -564 C
ATOM 4454 CD1 PHE B 342 18.914 -35.179 202.188 1.00 73.38 C
ANISOU 4454 CD1 PHE B 342 9609 8558 9715 -789 -2373 -726 C
ATOM 4455 CD2 PHE B 342 18.660 -33.443 203.799 1.00 69.50 C
ANISOU 4455 CD2 PHE B 342 8767 8236 9406 -635 -2114 -427 C
ATOM 4456 CE1 PHE B 342 18.973 -34.240 201.183 1.00 73.06 C
ANISOU 4456 CE1 PHE B 342 9705 8647 9408 -684 -2587 -728 C
ATOM 4457 CE2 PHE B 342 18.717 -32.499 202.797 1.00 70.45 C
ANISOU 4457 CE2 PHE B 342 9006 8465 9296 -530 -2329 -427 C
ATOM 4458 CZ PHE B 342 18.873 -32.898 201.486 1.00 70.13 C
ANISOU 4458 CZ PHE B 342 9219 8409 9019 -553 -2565 -566 C
ATOM 4459 N SER B 343 20.861 -34.630 206.685 1.00 65.08 N
ANISOU 4459 N SER B 343 8356 7517 8855 -565 -1284 -209 N
ATOM 4460 CA SER B 343 21.655 -33.471 207.078 1.00 65.34 C
ANISOU 4460 CA SER B 343 8426 7687 8714 -407 -1165 -106 C
ATOM 4461 C SER B 343 23.140 -33.818 207.154 1.00 69.88 C
ANISOU 4461 C SER B 343 9228 8236 9087 -311 -1018 -109 C
ATOM 4462 O SER B 343 23.999 -33.036 206.709 1.00 65.30 O
ANISOU 4462 O SER B 343 8759 7748 8303 -202 -1006 -109 O
ATOM 4463 CB SER B 343 21.137 -32.927 208.410 1.00 62.74 C
ANISOU 4463 CB SER B 343 7884 7404 8551 -397 -995 23 C
ATOM 4464 OG SER B 343 19.765 -32.570 208.299 1.00 61.46 O
ANISOU 4464 OG SER B 343 7473 7265 8614 -472 -1118 14 O
ATOM 4465 N HIS B 344 23.462 -35.003 207.679 1.00 64.50 N
ANISOU 4465 N HIS B 344 8611 7416 8480 -349 -903 -112 N
ATOM 4466 CA HIS B 344 24.852 -35.447 207.677 1.00 65.71 C
ANISOU 4466 CA HIS B 344 8955 7527 8485 -242 -790 -131 C
ATOM 4467 C HIS B 344 25.375 -35.547 206.249 1.00 64.93 C
ANISOU 4467 C HIS B 344 9040 7424 8207 -221 -899 -280 C
ATOM 4468 O HIS B 344 26.473 -35.055 205.922 1.00 69.03 O
ANISOU 4468 O HIS B 344 9666 8015 8548 -106 -825 -294 O
ATOM 4469 CB HIS B 344 24.967 -36.804 208.382 1.00 67.89 C
ANISOU 4469 CB HIS B 344 9284 7617 8896 -282 -681 -106 C
ATOM 4470 CG HIS B 344 24.486 -36.804 209.802 1.00 71.54 C
ANISOU 4470 CG HIS B 344 9621 8070 9492 -305 -541 54 C
ATOM 4471 ND1 HIS B 344 23.858 -37.891 210.376 1.00 73.42 N
ANISOU 4471 ND1 HIS B 344 9848 8128 9919 -420 -468 100 N
ATOM 4472 CD2 HIS B 344 24.557 -35.858 210.769 1.00 71.32 C
ANISOU 4472 CD2 HIS B 344 9500 8179 9419 -233 -442 173 C
ATOM 4473 CE1 HIS B 344 23.557 -37.611 211.632 1.00 74.56 C
ANISOU 4473 CE1 HIS B 344 9910 8310 10111 -414 -315 254 C
ATOM 4474 NE2 HIS B 344 23.975 -36.385 211.897 1.00 73.79 N
ANISOU 4474 NE2 HIS B 344 9764 8408 9865 -297 -304 290 N
ATOM 4475 N TRP B 345 24.579 -36.153 205.366 1.00 64.96 N
ANISOU 4475 N TRP B 345 9083 7346 8254 -341 -1073 -403 N
ATOM 4476 CA TRP B 345 25.041 -36.296 203.995 1.00 69.03 C
ANISOU 4476 CA TRP B 345 9819 7854 8556 -323 -1172 -558 C
ATOM 4477 C TRP B 345 25.239 -34.935 203.343 1.00 70.33 C
ANISOU 4477 C TRP B 345 10023 8196 8504 -244 -1230 -524 C
ATOM 4478 O TRP B 345 26.174 -34.748 202.563 1.00 71.99 O
ANISOU 4478 O TRP B 345 10432 8434 8487 -168 -1169 -586 O
ATOM 4479 CB TRP B 345 24.063 -37.139 203.180 1.00 62.91 C
ANISOU 4479 CB TRP B 345 9084 6965 7853 -476 -1389 -715 C
ATOM 4480 CG TRP B 345 24.425 -37.134 201.728 1.00 69.85 C
ANISOU 4480 CG TRP B 345 10220 7863 8455 -456 -1513 -880 C
ATOM 4481 CD1 TRP B 345 25.305 -37.963 201.102 1.00 64.30 C
ANISOU 4481 CD1 TRP B 345 9764 7049 7617 -423 -1423 -1028 C
ATOM 4482 CD2 TRP B 345 23.943 -36.229 200.727 1.00 75.21 C
ANISOU 4482 CD2 TRP B 345 10963 8679 8935 -453 -1734 -906 C
ATOM 4483 NE1 TRP B 345 25.391 -37.644 199.769 1.00 74.95 N
ANISOU 4483 NE1 TRP B 345 11340 8464 8672 -413 -1555 -1156 N
ATOM 4484 CE2 TRP B 345 24.565 -36.581 199.513 1.00 75.44 C
ANISOU 4484 CE2 TRP B 345 11308 8679 8678 -430 -1760 -1071 C
ATOM 4485 CE3 TRP B 345 23.042 -35.159 200.738 1.00 71.97 C
ANISOU 4485 CE3 TRP B 345 10383 8403 8560 -455 -1911 -802 C
ATOM 4486 CZ2 TRP B 345 24.312 -35.903 198.321 1.00 74.79 C
ANISOU 4486 CZ2 TRP B 345 11407 8702 8307 -415 -1964 -1121 C
ATOM 4487 CZ3 TRP B 345 22.793 -34.489 199.557 1.00 72.50 C
ANISOU 4487 CZ3 TRP B 345 10609 8564 8373 -427 -2135 -844 C
ATOM 4488 CH2 TRP B 345 23.424 -34.863 198.365 1.00 73.83 C
ANISOU 4488 CH2 TRP B 345 11124 8708 8222 -411 -2164 -995 C
ATOM 4489 N LEU B 346 24.385 -33.964 203.677 1.00 63.01 N
ANISOU 4489 N LEU B 346 8910 7373 7656 -255 -1323 -418 N
ATOM 4490 CA LEU B 346 24.507 -32.632 203.093 1.00 65.70 C
ANISOU 4490 CA LEU B 346 9297 7851 7813 -175 -1382 -362 C
ATOM 4491 C LEU B 346 25.811 -31.970 203.520 1.00 61.92 C
ANISOU 4491 C LEU B 346 8870 7434 7224 -57 -1142 -288 C
ATOM 4492 O LEU B 346 26.512 -31.338 202.703 1.00 66.23 O
ANISOU 4492 O LEU B 346 9584 8031 7547 4 -1106 -300 O
ATOM 4493 CB LEU B 346 23.305 -31.792 203.522 1.00 66.86 C
ANISOU 4493 CB LEU B 346 9203 8069 8132 -195 -1512 -264 C
ATOM 4494 CG LEU B 346 22.738 -30.722 202.597 1.00 71.74 C
ANISOU 4494 CG LEU B 346 9854 8776 8629 -152 -1732 -236 C
ATOM 4495 CD1 LEU B 346 22.302 -31.337 201.285 1.00 74.15 C
ANISOU 4495 CD1 LEU B 346 10332 9047 8795 -218 -1998 -377 C
ATOM 4496 CD2 LEU B 346 21.569 -30.028 203.280 1.00 74.64 C
ANISOU 4496 CD2 LEU B 346 9921 9187 9254 -154 -1817 -144 C
ATOM 4497 N VAL B 347 26.171 -32.143 204.795 1.00 55.71 N
ANISOU 4497 N VAL B 347 7948 6633 6587 -30 -973 -216 N
ATOM 4498 CA VAL B 347 27.465 -31.653 205.256 1.00 54.60 C
ANISOU 4498 CA VAL B 347 7831 6542 6371 74 -775 -174 C
ATOM 4499 C VAL B 347 28.572 -32.222 204.386 1.00 66.90 C
ANISOU 4499 C VAL B 347 9589 8053 7777 115 -690 -287 C
ATOM 4500 O VAL B 347 29.462 -31.497 203.928 1.00 76.49 O
ANISOU 4500 O VAL B 347 10882 9329 8852 175 -584 -290 O
ATOM 4501 CB VAL B 347 27.699 -32.014 206.732 1.00 51.00 C
ANISOU 4501 CB VAL B 347 7239 6066 6072 101 -649 -99 C
ATOM 4502 CG1 VAL B 347 29.189 -31.863 207.059 1.00 44.40 C
ANISOU 4502 CG1 VAL B 347 6440 5259 5170 209 -488 -103 C
ATOM 4503 CG2 VAL B 347 26.852 -31.136 207.641 1.00 55.42 C
ANISOU 4503 CG2 VAL B 347 7616 6699 6740 88 -658 10 C
ATOM 4504 N TYR B 348 28.536 -33.531 204.143 1.00 70.57 N
ANISOU 4504 N TYR B 348 10139 8391 8281 77 -712 -388 N
ATOM 4505 CA TYR B 348 29.605 -34.087 203.313 1.00 58.88 C
ANISOU 4505 CA TYR B 348 8850 6856 6667 130 -601 -516 C
ATOM 4506 C TYR B 348 29.505 -33.626 201.863 1.00 58.81 C
ANISOU 4506 C TYR B 348 9048 6891 6406 106 -673 -597 C
ATOM 4507 O TYR B 348 30.528 -33.527 201.175 1.00 66.60 O
ANISOU 4507 O TYR B 348 10185 7887 7234 166 -515 -667 O
ATOM 4508 CB TYR B 348 29.625 -35.607 203.423 1.00 63.46 C
ANISOU 4508 CB TYR B 348 9487 7260 7363 109 -594 -613 C
ATOM 4509 CG TYR B 348 30.042 -36.008 204.808 1.00 61.72 C
ANISOU 4509 CG TYR B 348 9121 6994 7335 173 -488 -509 C
ATOM 4510 CD1 TYR B 348 31.325 -35.737 205.265 1.00 59.35 C
ANISOU 4510 CD1 TYR B 348 8777 6741 7033 306 -329 -480 C
ATOM 4511 CD2 TYR B 348 29.143 -36.600 205.681 1.00 54.62 C
ANISOU 4511 CD2 TYR B 348 8126 6010 6616 98 -551 -433 C
ATOM 4512 CE1 TYR B 348 31.713 -36.075 206.549 1.00 56.62 C
ANISOU 4512 CE1 TYR B 348 8317 6364 6832 380 -276 -379 C
ATOM 4513 CE2 TYR B 348 29.520 -36.941 206.964 1.00 56.18 C
ANISOU 4513 CE2 TYR B 348 8237 6167 6940 166 -455 -316 C
ATOM 4514 CZ TYR B 348 30.804 -36.676 207.393 1.00 53.16 C
ANISOU 4514 CZ TYR B 348 7834 5840 6523 315 -339 -289 C
ATOM 4515 OH TYR B 348 31.174 -37.017 208.673 1.00 55.81 O
ANISOU 4515 OH TYR B 348 8108 6143 6956 395 -287 -170 O
ATOM 4516 N ALA B 349 28.295 -33.319 201.393 1.00 60.00 N
ANISOU 4516 N ALA B 349 9209 7072 6516 25 -905 -586 N
ATOM 4517 CA ALA B 349 28.119 -32.882 200.011 1.00 60.07 C
ANISOU 4517 CA ALA B 349 9452 7125 6247 12 -1019 -648 C
ATOM 4518 C ALA B 349 28.803 -31.551 199.749 1.00 61.88 C
ANISOU 4518 C ALA B 349 9738 7461 6312 87 -885 -540 C
ATOM 4519 O ALA B 349 29.215 -31.274 198.612 1.00 63.26 O
ANISOU 4519 O ALA B 349 10172 7654 6209 103 -846 -588 O
ATOM 4520 CB ALA B 349 26.634 -32.773 199.680 1.00 56.49 C
ANISOU 4520 CB ALA B 349 8952 6689 5824 -74 -1343 -644 C
ATOM 4521 N ASN B 350 28.915 -30.704 200.775 1.00 60.21 N
ANISOU 4521 N ASN B 350 9308 7310 6259 124 -804 -398 N
ATOM 4522 CA ASN B 350 29.541 -29.401 200.531 1.00 63.04 C
ANISOU 4522 CA ASN B 350 9718 7742 6492 177 -673 -301 C
ATOM 4523 C ASN B 350 30.983 -29.530 200.028 1.00 58.62 C
ANISOU 4523 C ASN B 350 9303 7167 5803 218 -396 -376 C
ATOM 4524 O ASN B 350 31.436 -28.712 199.202 1.00 65.33 O
ANISOU 4524 O ASN B 350 10328 8047 6448 230 -291 -340 O
ATOM 4525 CB ASN B 350 29.502 -28.548 201.795 1.00 52.83 C
ANISOU 4525 CB ASN B 350 8166 6497 5409 205 -619 -173 C
ATOM 4526 CG ASN B 350 30.017 -27.143 201.555 1.00 60.89 C
ANISOU 4526 CG ASN B 350 9233 7564 6337 240 -503 -75 C
ATOM 4527 OD1 ASN B 350 31.142 -26.805 201.934 1.00 60.58 O
ANISOU 4527 OD1 ASN B 350 9141 7535 6340 266 -279 -77 O
ATOM 4528 ND2 ASN B 350 29.202 -26.320 200.900 1.00 59.24 N
ANISOU 4528 ND2 ASN B 350 9121 7371 6018 241 -663 10 N
ATOM 4529 N SER B 351 31.710 -30.552 200.497 1.00 57.00 N
ANISOU 4529 N SER B 351 9029 6905 5725 244 -265 -475 N
ATOM 4530 CA SER B 351 33.094 -30.754 200.077 1.00 56.47 C
ANISOU 4530 CA SER B 351 9045 6817 5595 297 11 -564 C
ATOM 4531 C SER B 351 33.194 -31.119 198.604 1.00 62.58 C
ANISOU 4531 C SER B 351 10146 7555 6076 279 51 -685 C
ATOM 4532 O SER B 351 34.202 -30.805 197.956 1.00 69.24 O
ANISOU 4532 O SER B 351 11112 8408 6789 307 308 -725 O
ATOM 4533 CB SER B 351 33.761 -31.837 200.928 1.00 53.14 C
ANISOU 4533 CB SER B 351 8466 6325 5398 356 102 -639 C
ATOM 4534 OG SER B 351 33.826 -31.459 202.298 1.00 60.57 O
ANISOU 4534 OG SER B 351 9144 7310 6560 384 83 -529 O
ATOM 4535 N ALA B 352 32.182 -31.803 198.068 1.00 58.74 N
ANISOU 4535 N ALA B 352 9805 7025 5489 225 -187 -759 N
ATOM 4536 CA ALA B 352 32.142 -32.065 196.635 1.00 64.22 C
ANISOU 4536 CA ALA B 352 10853 7697 5850 203 -198 -880 C
ATOM 4537 C ALA B 352 31.643 -30.857 195.856 1.00 67.96 C
ANISOU 4537 C ALA B 352 11509 8257 6056 184 -308 -755 C
ATOM 4538 O ALA B 352 32.017 -30.673 194.692 1.00 80.07 O
ANISOU 4538 O ALA B 352 13366 9797 7258 189 -203 -803 O
ATOM 4539 CB ALA B 352 31.261 -33.284 196.345 1.00 66.77 C
ANISOU 4539 CB ALA B 352 11266 7930 6174 142 -442 -1033 C
ATOM 4540 N ALA B 353 30.794 -30.035 196.476 1.00 65.13 N
ANISOU 4540 N ALA B 353 10964 7954 5827 173 -508 -591 N
ATOM 4541 CA ALA B 353 30.247 -28.884 195.768 1.00 62.65 C
ANISOU 4541 CA ALA B 353 10819 7698 5286 178 -645 -454 C
ATOM 4542 C ALA B 353 31.314 -27.829 195.496 1.00 68.39 C
ANISOU 4542 C ALA B 353 11649 8446 5891 212 -328 -349 C
ATOM 4543 O ALA B 353 31.347 -27.241 194.409 1.00 64.36 O
ANISOU 4543 O ALA B 353 11458 7945 5051 218 -310 -294 O
ATOM 4544 CB ALA B 353 29.089 -28.274 196.560 1.00 56.49 C
ANISOU 4544 CB ALA B 353 9780 6954 4729 174 -914 -315 C
ATOM 4545 N ASN B 354 32.189 -27.562 196.465 1.00 63.45 N
ANISOU 4545 N ASN B 354 10763 7820 5523 229 -80 -317 N
ATOM 4546 CA ASN B 354 33.080 -26.411 196.303 1.00 61.92 C
ANISOU 4546 CA ASN B 354 10615 7635 5277 236 198 -207 C
ATOM 4547 C ASN B 354 33.926 -26.469 195.030 1.00 69.15 C
ANISOU 4547 C ASN B 354 11875 8527 5871 229 466 -270 C
ATOM 4548 O ASN B 354 33.954 -25.469 194.287 1.00 70.92 O
ANISOU 4548 O ASN B 354 12337 8748 5862 219 538 -137 O
ATOM 4549 CB ASN B 354 33.946 -26.248 197.554 1.00 60.85 C
ANISOU 4549 CB ASN B 354 10128 7505 5485 247 396 -208 C
ATOM 4550 CG ASN B 354 33.132 -25.857 198.771 1.00 60.00 C
ANISOU 4550 CG ASN B 354 9738 7425 5633 254 180 -114 C
ATOM 4551 OD1 ASN B 354 32.152 -25.119 198.661 1.00 64.10 O
ANISOU 4551 OD1 ASN B 354 10299 7954 6104 254 -23 6 O
ATOM 4552 ND2 ASN B 354 33.523 -26.357 199.934 1.00 58.33 N
ANISOU 4552 ND2 ASN B 354 9251 7223 5691 272 222 -168 N
ATOM 4553 N PRO B 355 34.631 -27.561 194.718 1.00 68.48 N
ANISOU 4553 N PRO B 355 11851 8414 5754 238 643 -459 N
ATOM 4554 CA PRO B 355 35.389 -27.598 193.455 1.00 64.25 C
ANISOU 4554 CA PRO B 355 11670 7856 4886 231 932 -529 C
ATOM 4555 C PRO B 355 34.530 -27.404 192.215 1.00 69.66 C
ANISOU 4555 C PRO B 355 12794 8551 5122 218 723 -489 C
ATOM 4556 O PRO B 355 34.989 -26.798 191.243 1.00 78.60 O
ANISOU 4556 O PRO B 355 14246 9677 5941 207 945 -427 O
ATOM 4557 CB PRO B 355 36.037 -28.996 193.473 1.00 61.91 C
ANISOU 4557 CB PRO B 355 11326 7511 4683 263 1081 -768 C
ATOM 4558 CG PRO B 355 36.083 -29.373 194.921 1.00 64.98 C
ANISOU 4558 CG PRO B 355 11278 7898 5515 292 989 -770 C
ATOM 4559 CD PRO B 355 34.839 -28.774 195.529 1.00 70.47 C
ANISOU 4559 CD PRO B 355 11858 8636 6281 264 625 -610 C
ATOM 4560 N ILE B 356 33.293 -27.906 192.214 1.00 70.90 N
ANISOU 4560 N ILE B 356 12972 8722 5243 215 296 -521 N
ATOM 4561 CA ILE B 356 32.408 -27.692 191.071 1.00 70.57 C
ANISOU 4561 CA ILE B 356 13308 8702 4802 211 20 -482 C
ATOM 4562 C ILE B 356 32.098 -26.208 190.919 1.00 73.48 C
ANISOU 4562 C ILE B 356 13722 9092 5105 230 -35 -213 C
ATOM 4563 O ILE B 356 32.068 -25.662 189.802 1.00 88.54 O
ANISOU 4563 O ILE B 356 15880 10999 6762 235 -19 -122 O
ATOM 4564 CB ILE B 356 31.121 -28.521 191.249 1.00 69.94 C
ANISOU 4564 CB ILE B 356 13158 8629 4786 193 -450 -585 C
ATOM 4565 CG1 ILE B 356 31.453 -30.014 191.292 1.00 77.13 C
ANISOU 4565 CG1 ILE B 356 14048 9479 5781 167 -376 -853 C
ATOM 4566 CG2 ILE B 356 30.116 -28.209 190.154 1.00 66.61 C
ANISOU 4566 CG2 ILE B 356 12931 8246 4133 192 -788 -520 C
ATOM 4567 CD1 ILE B 356 30.268 -30.897 191.633 1.00 74.42 C
ANISOU 4567 CD1 ILE B 356 13555 9112 5609 120 -789 -961 C
ATOM 4568 N ILE B 357 31.897 -25.524 192.046 1.00 71.12 N
ANISOU 4568 N ILE B 357 13104 8798 5122 242 -83 -79 N
ATOM 4569 CA ILE B 357 31.665 -24.087 192.008 1.00 70.09 C
ANISOU 4569 CA ILE B 357 13023 8654 4953 268 -105 170 C
ATOM 4570 C ILE B 357 32.872 -23.386 191.409 1.00 73.41 C
ANISOU 4570 C ILE B 357 13660 9029 5205 244 347 246 C
ATOM 4571 O ILE B 357 32.739 -22.506 190.552 1.00 70.93 O
ANISOU 4571 O ILE B 357 13553 8683 4714 254 345 405 O
ATOM 4572 CB ILE B 357 31.352 -23.557 193.417 1.00 68.08 C
ANISOU 4572 CB ILE B 357 12311 8401 5155 278 -183 257 C
ATOM 4573 CG1 ILE B 357 30.027 -24.134 193.919 1.00 64.27 C
ANISOU 4573 CG1 ILE B 357 11620 7957 4843 295 -617 209 C
ATOM 4574 CG2 ILE B 357 31.342 -22.034 193.424 1.00 73.83 C
ANISOU 4574 CG2 ILE B 357 13088 9080 5885 304 -121 494 C
ATOM 4575 CD1 ILE B 357 29.632 -23.653 195.299 1.00 63.21 C
ANISOU 4575 CD1 ILE B 357 11065 7827 5127 309 -678 284 C
ATOM 4576 N TYR B 358 34.076 -23.795 191.822 1.00 70.04 N
ANISOU 4576 N TYR B 358 13072 8590 4951 206 737 121 N
ATOM 4577 CA TYR B 358 35.271 -23.177 191.256 1.00 70.83 C
ANISOU 4577 CA TYR B 358 13309 8641 4963 163 1200 172 C
ATOM 4578 C TYR B 358 35.363 -23.437 189.761 1.00 80.01 C
ANISOU 4578 C TYR B 358 14801 9796 5803 158 1246 136 C
ATOM 4579 O TYR B 358 35.792 -22.567 188.994 1.00 90.18 O
ANISOU 4579 O TYR B 358 16274 11036 6956 132 1455 272 O
ATOM 4580 CB TYR B 358 36.529 -23.710 191.940 1.00 72.79 C
ANISOU 4580 CB TYR B 358 13269 8886 5500 135 1578 9 C
ATOM 4581 CG TYR B 358 36.522 -23.619 193.443 1.00 74.80 C
ANISOU 4581 CG TYR B 358 13019 9160 6242 141 1468 6 C
ATOM 4582 CD1 TYR B 358 35.787 -22.641 194.102 1.00 65.77 C
ANISOU 4582 CD1 TYR B 358 11734 8009 5246 145 1241 180 C
ATOM 4583 CD2 TYR B 358 37.262 -24.509 194.202 1.00 74.37 C
ANISOU 4583 CD2 TYR B 358 12646 9123 6488 155 1594 -172 C
ATOM 4584 CE1 TYR B 358 35.788 -22.565 195.480 1.00 62.23 C
ANISOU 4584 CE1 TYR B 358 10861 7582 5201 150 1157 162 C
ATOM 4585 CE2 TYR B 358 37.266 -24.439 195.574 1.00 76.90 C
ANISOU 4585 CE2 TYR B 358 12550 9467 7203 167 1481 -170 C
ATOM 4586 CZ TYR B 358 36.528 -23.467 196.211 1.00 67.23 C
ANISOU 4586 CZ TYR B 358 11213 8245 6087 158 1271 -9 C
ATOM 4587 OH TYR B 358 36.535 -23.399 197.582 1.00 73.63 O
ANISOU 4587 OH TYR B 358 11644 9082 7251 169 1173 -20 O
ATOM 4588 N ASN B 359 34.965 -24.634 189.330 1.00 80.87 N
ANISOU 4588 N ASN B 359 15000 9943 5785 177 1060 -50 N
ATOM 4589 CA ASN B 359 35.045 -24.967 187.914 1.00 82.97 C
ANISOU 4589 CA ASN B 359 15594 10208 5725 174 1100 -109 C
ATOM 4590 C ASN B 359 34.113 -24.103 187.080 1.00 87.13 C
ANISOU 4590 C ASN B 359 16377 10739 5991 199 809 86 C
ATOM 4591 O ASN B 359 34.446 -23.755 185.942 1.00 81.20 O
ANISOU 4591 O ASN B 359 15921 9967 4965 192 965 143 O
ATOM 4592 CB ASN B 359 34.721 -26.446 187.698 1.00 79.67 C
ANISOU 4592 CB ASN B 359 15206 9815 5250 184 929 -363 C
ATOM 4593 CG ASN B 359 34.689 -26.823 186.231 1.00 80.84 C
ANISOU 4593 CG ASN B 359 15712 9969 5036 182 930 -438 C
ATOM 4594 OD1 ASN B 359 35.729 -27.061 185.618 1.00 88.03 O
ANISOU 4594 OD1 ASN B 359 16736 10852 5858 167 1321 -522 O
ATOM 4595 ND2 ASN B 359 33.493 -26.870 185.657 1.00 77.38 N
ANISOU 4595 ND2 ASN B 359 15441 9568 4391 198 491 -412 N
ATOM 4596 N PHE B 360 32.950 -23.744 187.620 1.00 91.96 N
ANISOU 4596 N PHE B 360 16874 11375 6693 238 389 191 N
ATOM 4597 CA PHE B 360 32.016 -22.964 186.811 1.00 92.35 C
ANISOU 4597 CA PHE B 360 17138 11428 6524 286 81 367 C
ATOM 4598 C PHE B 360 32.185 -21.456 186.956 1.00 91.98 C
ANISOU 4598 C PHE B 360 17105 11311 6533 303 210 636 C
ATOM 4599 O PHE B 360 31.930 -20.723 185.995 1.00 94.77 O
ANISOU 4599 O PHE B 360 17729 11636 6643 335 150 789 O
ATOM 4600 CB PHE B 360 30.574 -23.358 187.135 1.00 98.87 C
ANISOU 4600 CB PHE B 360 17827 12311 7430 329 -468 333 C
ATOM 4601 CG PHE B 360 30.169 -24.670 186.536 1.00111.06 C
ANISOU 4601 CG PHE B 360 19467 13903 8827 307 -671 97 C
ATOM 4602 CD1 PHE B 360 30.803 -25.148 185.401 1.00120.68 C
ANISOU 4602 CD1 PHE B 360 20993 15120 9741 284 -458 -12 C
ATOM 4603 CD2 PHE B 360 29.165 -25.430 187.108 1.00111.63 C
ANISOU 4603 CD2 PHE B 360 19321 14013 9081 302 -1060 -23 C
ATOM 4604 CE1 PHE B 360 30.440 -26.358 184.844 1.00125.80 C
ANISOU 4604 CE1 PHE B 360 21741 15801 10258 262 -639 -244 C
ATOM 4605 CE2 PHE B 360 28.796 -26.640 186.556 1.00116.85 C
ANISOU 4605 CE2 PHE B 360 20069 14698 9631 266 -1241 -252 C
ATOM 4606 CZ PHE B 360 29.435 -27.105 185.422 1.00124.68 C
ANISOU 4606 CZ PHE B 360 21379 15685 10307 248 -1034 -366 C
ATOM 4607 N LEU B 361 32.619 -20.968 188.116 1.00 91.18 N
ANISOU 4607 N LEU B 361 16734 11172 6739 281 387 696 N
ATOM 4608 CA LEU B 361 32.702 -19.535 188.372 1.00 86.20 C
ANISOU 4608 CA LEU B 361 16090 10452 6209 291 487 940 C
ATOM 4609 C LEU B 361 34.121 -18.980 188.325 1.00 80.42 C
ANISOU 4609 C LEU B 361 15382 9637 5538 205 1037 977 C
ATOM 4610 O LEU B 361 34.312 -17.789 188.604 1.00 79.89 O
ANISOU 4610 O LEU B 361 15288 9471 5596 191 1168 1163 O
ATOM 4611 CB LEU B 361 32.061 -19.207 189.727 1.00 81.71 C
ANISOU 4611 CB LEU B 361 15199 9883 5966 327 267 999 C
ATOM 4612 CG LEU B 361 30.534 -19.315 189.769 1.00 75.88 C
ANISOU 4612 CG LEU B 361 14399 9196 5237 419 -286 1033 C
ATOM 4613 CD1 LEU B 361 30.019 -19.186 191.192 1.00 74.73 C
ANISOU 4613 CD1 LEU B 361 13905 9054 5436 448 -450 1052 C
ATOM 4614 CD2 LEU B 361 29.898 -18.266 188.870 1.00 65.20 C
ANISOU 4614 CD2 LEU B 361 13267 7790 3716 493 -467 1245 C
ATOM 4615 N SER B 362 35.119 -19.797 187.989 1.00 81.51 N
ANISOU 4615 N SER B 362 15547 9799 5625 146 1367 796 N
ATOM 4616 CA SER B 362 36.500 -19.333 187.887 1.00 82.97 C
ANISOU 4616 CA SER B 362 15708 9908 5909 58 1900 806 C
ATOM 4617 C SER B 362 37.138 -19.955 186.656 1.00 95.11 C
ANISOU 4617 C SER B 362 17506 11457 7174 35 2136 693 C
ATOM 4618 O SER B 362 37.287 -21.179 186.587 1.00101.16 O
ANISOU 4618 O SER B 362 18234 12294 7910 47 2130 473 O
ATOM 4619 CB SER B 362 37.305 -19.692 189.140 1.00 79.02 C
ANISOU 4619 CB SER B 362 14817 9422 5784 8 2138 672 C
ATOM 4620 OG SER B 362 38.684 -19.413 188.952 1.00 75.77 O
ANISOU 4620 OG SER B 362 14338 8950 5503 -83 2647 636 O
ATOM 4621 N GLY B 363 37.530 -19.115 185.695 1.00 95.98 N
ANISOU 4621 N GLY B 363 17890 11487 7093 3 2357 842 N
ATOM 4622 CA GLY B 363 38.113 -19.631 184.470 1.00 92.10 C
ANISOU 4622 CA GLY B 363 17682 11000 6310 -16 2596 749 C
ATOM 4623 C GLY B 363 39.503 -20.209 184.658 1.00100.39 C
ANISOU 4623 C GLY B 363 18529 12040 7572 -88 3083 563 C
ATOM 4624 O GLY B 363 39.902 -21.121 183.929 1.00111.12 O
ANISOU 4624 O GLY B 363 20025 13436 8760 -82 3222 394 O
ATOM 4625 N LYS B 364 40.257 -19.702 185.637 1.00 96.56 N
ANISOU 4625 N LYS B 364 17700 11505 7481 -154 3340 580 N
ATOM 4626 CA LYS B 364 41.587 -20.250 185.891 1.00 98.93 C
ANISOU 4626 CA LYS B 364 17736 11802 8049 -214 3776 393 C
ATOM 4627 C LYS B 364 41.502 -21.646 186.504 1.00100.42 C
ANISOU 4627 C LYS B 364 17702 12092 8363 -150 3632 147 C
ATOM 4628 O LYS B 364 42.197 -22.577 186.061 1.00106.93 O
ANISOU 4628 O LYS B 364 18520 12937 9174 -140 3854 -45 O
ATOM 4629 CB LYS B 364 42.376 -19.285 186.781 1.00 91.19 C
ANISOU 4629 CB LYS B 364 16425 10742 7480 -308 4050 469 C
ATOM 4630 CG LYS B 364 42.655 -17.948 186.090 1.00 93.90 C
ANISOU 4630 CG LYS B 364 16995 10953 7729 -387 4274 690 C
ATOM 4631 CD LYS B 364 43.163 -16.864 187.026 1.00 87.94 C
ANISOU 4631 CD LYS B 364 15933 10099 7379 -485 4448 783 C
ATOM 4632 CE LYS B 364 43.314 -15.547 186.270 1.00 93.05 C
ANISOU 4632 CE LYS B 364 16855 10593 7906 -557 4638 1012 C
ATOM 4633 NZ LYS B 364 43.711 -14.411 187.143 1.00 96.70 N
ANISOU 4633 NZ LYS B 364 17048 10934 8760 -661 4779 1105 N
ATOM 4634 N PHE B 365 40.619 -21.825 187.489 1.00 89.31 N
ANISOU 4634 N PHE B 365 16128 10736 7068 -100 3257 151 N
ATOM 4635 CA PHE B 365 40.366 -23.164 188.002 1.00 87.15 C
ANISOU 4635 CA PHE B 365 15702 10541 6871 -33 3074 -68 C
ATOM 4636 C PHE B 365 39.824 -24.068 186.905 1.00 93.14 C
ANISOU 4636 C PHE B 365 16794 11333 7262 15 2894 -173 C
ATOM 4637 O PHE B 365 40.180 -25.250 186.829 1.00 94.10 O
ANISOU 4637 O PHE B 365 16859 11477 7419 47 2967 -397 O
ATOM 4638 CB PHE B 365 39.371 -23.108 189.161 1.00 86.29 C
ANISOU 4638 CB PHE B 365 15414 10472 6899 7 2682 -18 C
ATOM 4639 CG PHE B 365 39.999 -22.875 190.504 1.00 82.86 C
ANISOU 4639 CG PHE B 365 14567 10037 6881 -18 2847 -46 C
ATOM 4640 CD1 PHE B 365 40.762 -23.864 191.105 1.00 77.35 C
ANISOU 4640 CD1 PHE B 365 13581 9367 6441 11 3013 -265 C
ATOM 4641 CD2 PHE B 365 39.797 -21.682 191.183 1.00 76.55 C
ANISOU 4641 CD2 PHE B 365 13659 9201 6225 -58 2816 141 C
ATOM 4642 CE1 PHE B 365 41.333 -23.659 192.352 1.00 75.68 C
ANISOU 4642 CE1 PHE B 365 12971 9164 6620 0 3136 -301 C
ATOM 4643 CE2 PHE B 365 40.364 -21.470 192.429 1.00 69.56 C
ANISOU 4643 CE2 PHE B 365 12391 8320 5719 -87 2958 99 C
ATOM 4644 CZ PHE B 365 41.133 -22.460 193.014 1.00 69.17 C
ANISOU 4644 CZ PHE B 365 12013 8316 5950 -56 3078 -124 C
ATOM 4645 N ARG B 366 38.968 -23.526 186.038 1.00 94.18 N
ANISOU 4645 N ARG B 366 17273 11462 7049 25 2653 -21 N
ATOM 4646 CA ARG B 366 38.379 -24.340 184.982 1.00 91.67 C
ANISOU 4646 CA ARG B 366 17275 11183 6373 65 2443 -127 C
ATOM 4647 C ARG B 366 39.440 -24.812 183.997 1.00101.41 C
ANISOU 4647 C ARG B 366 18675 12391 7463 41 2863 -257 C
ATOM 4648 O ARG B 366 39.403 -25.959 183.535 1.00106.99 O
ANISOU 4648 O ARG B 366 19481 13127 8042 72 2820 -468 O
ATOM 4649 CB ARG B 366 37.282 -23.543 184.275 1.00 87.75 C
ANISOU 4649 CB ARG B 366 17088 10692 5562 90 2092 77 C
ATOM 4650 CG ARG B 366 36.543 -24.284 183.177 1.00 94.60 C
ANISOU 4650 CG ARG B 366 18286 11610 6048 129 1811 -24 C
ATOM 4651 CD ARG B 366 35.204 -23.615 182.910 1.00100.58 C
ANISOU 4651 CD ARG B 366 19198 12392 6624 178 1323 159 C
ATOM 4652 NE ARG B 366 35.320 -22.159 182.947 1.00116.95 N
ANISOU 4652 NE ARG B 366 21314 14399 8723 173 1432 436 N
ATOM 4653 CZ ARG B 366 34.299 -21.329 183.138 1.00129.37 C
ANISOU 4653 CZ ARG B 366 22888 15969 10298 226 1064 632 C
ATOM 4654 NH1 ARG B 366 34.504 -20.019 183.160 1.00134.66 N
ANISOU 4654 NH1 ARG B 366 23605 16553 11007 222 1207 875 N
ATOM 4655 NH2 ARG B 366 33.075 -21.807 183.314 1.00132.43 N
ANISOU 4655 NH2 ARG B 366 23212 16428 10679 282 557 580 N
ATOM 4656 N GLU B 367 40.425 -23.959 183.702 1.00101.35 N
ANISOU 4656 N GLU B 367 18683 12319 7506 -18 3288 -147 N
ATOM 4657 CA GLU B 367 41.509 -24.378 182.822 1.00106.04 C
ANISOU 4657 CA GLU B 367 19399 12884 8006 -44 3728 -272 C
ATOM 4658 C GLU B 367 42.379 -25.437 183.484 1.00 98.85 C
ANISOU 4658 C GLU B 367 18132 11985 7441 -25 3954 -521 C
ATOM 4659 O GLU B 367 42.762 -26.424 182.841 1.00106.52 O
ANISOU 4659 O GLU B 367 19211 12964 8296 7 4094 -720 O
ATOM 4660 CB GLU B 367 42.354 -23.171 182.410 1.00111.61 C
ANISOU 4660 CB GLU B 367 20175 13504 8728 -126 4137 -90 C
ATOM 4661 CG GLU B 367 41.739 -22.333 181.305 1.00120.42 C
ANISOU 4661 CG GLU B 367 21760 14588 9405 -128 4023 121 C
ATOM 4662 CD GLU B 367 42.578 -21.118 180.944 1.00135.97 C
ANISOU 4662 CD GLU B 367 23803 16447 11414 -217 4443 308 C
ATOM 4663 OE1 GLU B 367 43.073 -20.435 181.867 1.00137.64 O
ANISOU 4663 OE1 GLU B 367 23677 16602 12017 -278 4600 378 O
ATOM 4664 OE2 GLU B 367 42.743 -20.848 179.734 1.00144.49 O
ANISOU 4664 OE2 GLU B 367 25281 17489 12131 -231 4617 379 O
ATOM 4665 N GLN B 368 42.700 -25.260 184.768 1.00 98.95 N
ANISOU 4665 N GLN B 368 17718 11996 7882 -34 3983 -520 N
ATOM 4666 CA GLN B 368 43.530 -26.264 185.427 1.00101.61 C
ANISOU 4666 CA GLN B 368 17698 12341 8568 6 4171 -750 C
ATOM 4667 C GLN B 368 42.807 -27.607 185.518 1.00103.79 C
ANISOU 4667 C GLN B 368 18023 12656 8756 93 3851 -945 C
ATOM 4668 O GLN B 368 43.422 -28.667 185.347 1.00101.57 O
ANISOU 4668 O GLN B 368 17667 12360 8564 144 4024 -1165 O
ATOM 4669 CB GLN B 368 43.954 -25.771 186.809 1.00 96.05 C
ANISOU 4669 CB GLN B 368 16533 11635 8327 -14 4224 -706 C
ATOM 4670 CG GLN B 368 44.820 -24.520 186.770 1.00 96.69 C
ANISOU 4670 CG GLN B 368 16509 11657 8573 -118 4577 -555 C
ATOM 4671 CD GLN B 368 46.063 -24.694 185.914 1.00 99.20 C
ANISOU 4671 CD GLN B 368 16842 11928 8920 -153 5055 -653 C
ATOM 4672 OE1 GLN B 368 46.777 -25.689 186.028 1.00 95.98 O
ANISOU 4672 OE1 GLN B 368 16223 11535 8711 -95 5216 -866 O
ATOM 4673 NE2 GLN B 368 46.325 -23.722 185.047 1.00103.94 N
ANISOU 4673 NE2 GLN B 368 17698 12464 9332 -241 5287 -493 N
ATOM 4674 N PHE B 369 41.490 -27.581 185.740 1.00100.58 N
ANISOU 4674 N PHE B 369 17747 12285 8184 109 3380 -872 N
ATOM 4675 CA PHE B 369 40.722 -28.823 185.780 1.00 92.92 C
ANISOU 4675 CA PHE B 369 16837 11333 7135 168 3055 -1057 C
ATOM 4676 C PHE B 369 40.639 -29.471 184.403 1.00104.10 C
ANISOU 4676 C PHE B 369 18631 12746 8175 176 3080 -1182 C
ATOM 4677 O PHE B 369 40.702 -30.701 184.285 1.00108.09 O
ANISOU 4677 O PHE B 369 19135 13232 8703 221 3061 -1418 O
ATOM 4678 CB PHE B 369 39.318 -28.560 186.320 1.00 86.39 C
ANISOU 4678 CB PHE B 369 16034 10544 6246 169 2543 -942 C
ATOM 4679 CG PHE B 369 39.289 -28.023 187.722 1.00 84.74 C
ANISOU 4679 CG PHE B 369 15474 10341 6380 169 2489 -840 C
ATOM 4680 CD1 PHE B 369 40.399 -28.116 188.546 1.00 80.21 C
ANISOU 4680 CD1 PHE B 369 14552 9747 6179 181 2819 -910 C
ATOM 4681 CD2 PHE B 369 38.141 -27.430 188.217 1.00 70.76 C
ANISOU 4681 CD2 PHE B 369 13710 8602 4571 164 2095 -681 C
ATOM 4682 CE1 PHE B 369 40.363 -27.621 189.836 1.00 67.59 C
ANISOU 4682 CE1 PHE B 369 12643 8162 4877 182 2762 -828 C
ATOM 4683 CE2 PHE B 369 38.099 -26.934 189.505 1.00 73.05 C
ANISOU 4683 CE2 PHE B 369 13701 8900 5154 165 2054 -595 C
ATOM 4684 CZ PHE B 369 39.210 -27.031 190.315 1.00 69.44 C
ANISOU 4684 CZ PHE B 369 12924 8425 5035 172 2391 -671 C
ATOM 4685 N LYS B 370 40.479 -28.665 183.351 1.00106.04 N
ANISOU 4685 N LYS B 370 19219 13002 8070 137 3117 -1032 N
ATOM 4686 CA LYS B 370 40.448 -29.224 182.005 1.00107.98 C
ANISOU 4686 CA LYS B 370 19851 13251 7926 145 3163 -1151 C
ATOM 4687 C LYS B 370 41.778 -29.884 181.671 1.00107.10 C
ANISOU 4687 C LYS B 370 19667 13097 7930 160 3660 -1342 C
ATOM 4688 O LYS B 370 41.816 -30.969 181.073 1.00103.65 O
ANISOU 4688 O LYS B 370 19379 12651 7353 198 3673 -1569 O
ATOM 4689 CB LYS B 370 40.123 -28.117 181.000 1.00115.61 C
ANISOU 4689 CB LYS B 370 21193 14228 8506 109 3142 -926 C
ATOM 4690 CG LYS B 370 39.109 -28.476 179.926 1.00123.80 C
ANISOU 4690 CG LYS B 370 22646 15310 9083 129 2785 -968 C
ATOM 4691 CD LYS B 370 38.738 -27.245 179.101 1.00131.35 C
ANISOU 4691 CD LYS B 370 23939 16271 9698 112 2725 -704 C
ATOM 4692 CE LYS B 370 38.166 -26.137 179.981 1.00132.84 C
ANISOU 4692 CE LYS B 370 23930 16453 10091 108 2497 -449 C
ATOM 4693 NZ LYS B 370 37.808 -24.916 179.202 1.00138.07 N
ANISOU 4693 NZ LYS B 370 24915 17098 10449 107 2437 -182 N
ATOM 4694 N ALA B 371 42.882 -29.258 182.088 1.00109.35 N
ANISOU 4694 N ALA B 371 19694 13348 8506 132 4067 -1265 N
ATOM 4695 CA ALA B 371 44.194 -29.860 181.883 1.00112.18 C
ANISOU 4695 CA ALA B 371 19903 13666 9056 155 4539 -1446 C
ATOM 4696 C ALA B 371 44.344 -31.140 182.691 1.00108.62 C
ANISOU 4696 C ALA B 371 19143 13199 8930 242 4462 -1688 C
ATOM 4697 O ALA B 371 44.942 -32.110 182.215 1.00115.74 O
ANISOU 4697 O ALA B 371 20069 14066 9840 298 4676 -1909 O
ATOM 4698 CB ALA B 371 45.293 -28.863 182.251 1.00 94.19 C
ANISOU 4698 CB ALA B 371 17356 11353 7079 94 4948 -1311 C
ATOM 4699 N ALA B 372 43.787 -31.177 183.904 1.00105.10 N
ANISOU 4699 N ALA B 372 18420 12766 8746 263 4157 -1650 N
ATOM 4700 CA ALA B 372 43.859 -32.401 184.694 1.00105.03 C
ANISOU 4700 CA ALA B 372 18147 12722 9039 354 4060 -1864 C
ATOM 4701 C ALA B 372 43.115 -33.533 184.000 1.00113.40 C
ANISOU 4701 C ALA B 372 19507 13760 9821 387 3818 -2057 C
ATOM 4702 O ALA B 372 43.639 -34.645 183.857 1.00119.13 O
ANISOU 4702 O ALA B 372 20176 14423 10663 461 3966 -2291 O
ATOM 4703 CB ALA B 372 43.297 -32.160 186.096 1.00 97.28 C
ANISOU 4703 CB ALA B 372 16865 11755 8340 363 3764 -1768 C
ATOM 4704 N PHE B 373 41.895 -33.259 183.537 1.00113.30 N
ANISOU 4704 N PHE B 373 19807 13790 9452 334 3438 -1969 N
ATOM 4705 CA PHE B 373 41.113 -34.309 182.895 1.00119.84 C
ANISOU 4705 CA PHE B 373 20901 14599 10032 348 3165 -2164 C
ATOM 4706 C PHE B 373 41.757 -34.771 181.594 1.00135.12 C
ANISOU 4706 C PHE B 373 23129 16517 11693 363 3473 -2323 C
ATOM 4707 O PHE B 373 41.732 -35.964 181.274 1.00144.74 O
ANISOU 4707 O PHE B 373 24425 17679 12888 407 3446 -2579 O
ATOM 4708 CB PHE B 373 39.681 -33.835 182.652 1.00118.96 C
ANISOU 4708 CB PHE B 373 21027 14550 9623 288 2672 -2029 C
ATOM 4709 CG PHE B 373 38.845 -33.778 183.900 1.00121.15 C
ANISOU 4709 CG PHE B 373 21040 14828 10162 282 2305 -1952 C
ATOM 4710 CD1 PHE B 373 38.396 -34.943 184.504 1.00121.55 C
ANISOU 4710 CD1 PHE B 373 20957 14812 10415 306 2081 -2146 C
ATOM 4711 CD2 PHE B 373 38.508 -32.563 184.470 1.00118.10 C
ANISOU 4711 CD2 PHE B 373 20550 14496 9828 251 2194 -1688 C
ATOM 4712 CE1 PHE B 373 37.629 -34.893 185.656 1.00114.22 C
ANISOU 4712 CE1 PHE B 373 19799 13876 9723 294 1763 -2072 C
ATOM 4713 CE2 PHE B 373 37.743 -32.508 185.621 1.00112.62 C
ANISOU 4713 CE2 PHE B 373 19621 13805 9365 248 1872 -1623 C
ATOM 4714 CZ PHE B 373 37.304 -33.674 186.214 1.00109.23 C
ANISOU 4714 CZ PHE B 373 19064 13315 9123 267 1660 -1813 C
ATOM 4715 N SER B 374 42.372 -33.854 180.843 1.00140.94 N
ANISOU 4715 N SER B 374 24031 17287 12232 325 3790 -2183 N
ATOM 4716 CA SER B 374 42.988 -34.263 179.584 1.00144.01 C
ANISOU 4716 CA SER B 374 24722 17660 12334 337 4107 -2331 C
ATOM 4717 C SER B 374 44.274 -35.048 179.824 1.00146.10 C
ANISOU 4717 C SER B 374 24711 17854 12948 413 4542 -2535 C
ATOM 4718 O SER B 374 44.460 -36.136 179.266 1.00152.87 O
ANISOU 4718 O SER B 374 25697 18664 13723 470 4622 -2792 O
ATOM 4719 CB SER B 374 43.248 -33.043 178.701 1.00140.76 C
ANISOU 4719 CB SER B 374 24592 17288 11602 271 4328 -2110 C
ATOM 4720 OG SER B 374 42.028 -32.446 178.295 1.00137.96 O
ANISOU 4720 OG SER B 374 24542 16992 10884 229 3903 -1947 O
ATOM 4721 N TRP B 375 45.170 -34.522 180.666 1.00146.89 N
ANISOU 4721 N TRP B 375 24411 17940 13459 421 4810 -2433 N
ATOM 4722 CA TRP B 375 46.441 -35.194 180.912 1.00150.46 C
ANISOU 4722 CA TRP B 375 24555 18330 14285 506 5211 -2612 C
ATOM 4723 C TRP B 375 46.262 -36.525 181.628 1.00152.97 C
ANISOU 4723 C TRP B 375 24661 18576 14885 616 5011 -2839 C
ATOM 4724 O TRP B 375 47.080 -37.434 181.444 1.00158.36 O
ANISOU 4724 O TRP B 375 25241 19188 15742 713 5275 -3058 O
ATOM 4725 CB TRP B 375 47.377 -34.294 181.726 1.00152.97 C
ANISOU 4725 CB TRP B 375 24454 18655 15013 483 5482 -2452 C
ATOM 4726 CG TRP B 375 48.007 -33.127 180.992 1.00156.46 C
ANISOU 4726 CG TRP B 375 25032 19117 15298 383 5848 -2279 C
ATOM 4727 CD1 TRP B 375 48.175 -31.856 181.473 1.00152.09 C
ANISOU 4727 CD1 TRP B 375 24317 18584 14886 293 5907 -2036 C
ATOM 4728 CD2 TRP B 375 48.566 -33.129 179.670 1.00164.86 C
ANISOU 4728 CD2 TRP B 375 26426 20164 16051 358 6220 -2340 C
ATOM 4729 NE1 TRP B 375 48.798 -31.072 180.532 1.00158.97 N
ANISOU 4729 NE1 TRP B 375 25396 19439 15566 210 6289 -1937 N
ATOM 4730 CE2 TRP B 375 49.047 -31.827 179.417 1.00165.87 C
ANISOU 4730 CE2 TRP B 375 26579 20294 16151 249 6492 -2114 C
ATOM 4731 CE3 TRP B 375 48.702 -34.102 178.674 1.00169.07 C
ANISOU 4731 CE3 TRP B 375 27247 20670 16320 416 6356 -2569 C
ATOM 4732 CZ2 TRP B 375 49.653 -31.474 178.210 1.00169.73 C
ANISOU 4732 CZ2 TRP B 375 27377 20757 16355 195 6903 -2099 C
ATOM 4733 CZ3 TRP B 375 49.306 -33.748 177.476 1.00172.17 C
ANISOU 4733 CZ3 TRP B 375 27949 21054 16415 368 6764 -2561 C
ATOM 4734 CH2 TRP B 375 49.773 -32.445 177.256 1.00171.51 C
ANISOU 4734 CH2 TRP B 375 27889 20971 16307 258 7037 -2321 C
ATOM 4735 N TRP B 376 45.217 -36.668 182.445 1.00151.78 N
ANISOU 4735 N TRP B 376 24444 18429 14798 608 4558 -2792 N
ATOM 4736 CA TRP B 376 45.076 -37.896 183.220 1.00153.31 C
ANISOU 4736 CA TRP B 376 24425 18527 15301 709 4382 -2986 C
ATOM 4737 C TRP B 376 44.199 -38.923 182.504 1.00153.24 C
ANISOU 4737 C TRP B 376 24763 18465 14996 707 4118 -3193 C
ATOM 4738 O TRP B 376 44.717 -39.908 181.963 1.00153.96 O
ANISOU 4738 O TRP B 376 24926 18474 15099 784 4312 -3436 O
ATOM 4739 CB TRP B 376 44.521 -37.594 184.615 1.00153.09 C
ANISOU 4739 CB TRP B 376 24097 18505 15567 706 4073 -2842 C
ATOM 4740 CG TRP B 376 45.494 -36.899 185.548 1.00156.16 C
ANISOU 4740 CG TRP B 376 24053 18919 16362 738 4315 -2712 C
ATOM 4741 CD1 TRP B 376 45.548 -35.564 185.831 1.00153.51 C
ANISOU 4741 CD1 TRP B 376 23631 18672 16023 651 4359 -2470 C
ATOM 4742 CD2 TRP B 376 46.533 -37.513 186.326 1.00158.61 C
ANISOU 4742 CD2 TRP B 376 23947 19159 17158 870 4517 -2824 C
ATOM 4743 NE1 TRP B 376 46.555 -35.308 186.729 1.00149.96 N
ANISOU 4743 NE1 TRP B 376 22734 18219 16026 704 4577 -2440 N
ATOM 4744 CE2 TRP B 376 47.176 -36.487 187.049 1.00154.67 C
ANISOU 4744 CE2 TRP B 376 23113 18726 16927 845 4664 -2649 C
ATOM 4745 CE3 TRP B 376 46.982 -38.830 186.479 1.00162.52 C
ANISOU 4745 CE3 TRP B 376 24318 19533 17900 1014 4571 -3054 C
ATOM 4746 CZ2 TRP B 376 48.244 -36.735 187.910 1.00156.65 C
ANISOU 4746 CZ2 TRP B 376 22896 18944 17680 959 4838 -2701 C
ATOM 4747 CZ3 TRP B 376 48.044 -39.074 187.336 1.00162.01 C
ANISOU 4747 CZ3 TRP B 376 23799 19427 18331 1144 4748 -3088 C
ATOM 4748 CH2 TRP B 376 48.662 -38.031 188.039 1.00160.04 C
ANISOU 4748 CH2 TRP B 376 23209 19263 18336 1115 4868 -2913 C
ATOM 4749 N LEU B 377 42.882 -38.719 182.504 1.00152.89 N
ANISOU 4749 N LEU B 377 24918 18461 14711 620 3672 -3113 N
ATOM 4750 CA LEU B 377 41.939 -39.663 181.900 1.00156.06 C
ANISOU 4750 CA LEU B 377 25614 18815 14866 596 3359 -3313 C
ATOM 4751 C LEU B 377 41.096 -38.984 180.828 1.00162.21 C
ANISOU 4751 C LEU B 377 26808 19706 15117 493 3151 -3215 C
ATOM 4752 O LEU B 377 40.402 -37.999 181.131 1.00164.01 O
ANISOU 4752 O LEU B 377 27035 20021 15262 425 2903 -2973 O
ATOM 4753 CB LEU B 377 41.027 -40.275 182.971 1.00153.19 C
ANISOU 4753 CB LEU B 377 25064 18373 14769 590 2947 -3346 C
ATOM 4754 CG LEU B 377 41.547 -41.483 183.755 1.00154.70 C
ANISOU 4754 CG LEU B 377 24982 18394 15403 703 3037 -3542 C
ATOM 4755 CD1 LEU B 377 42.680 -41.091 184.692 1.00153.36 C
ANISOU 4755 CD1 LEU B 377 24408 18220 15640 802 3349 -3427 C
ATOM 4756 CD2 LEU B 377 40.411 -42.144 184.524 1.00153.05 C
ANISOU 4756 CD2 LEU B 377 24717 18088 15349 661 2592 -3587 C
ATOM 4757 N PRO B 378 41.086 -39.481 179.578 1.00167.13 N
ANISOU 4757 N PRO B 378 27797 20328 15375 487 3218 -3398 N
ATOM 4758 CA PRO B 378 40.287 -38.874 178.505 1.00170.67 C
ANISOU 4758 CA PRO B 378 28662 20884 15302 405 2998 -3311 C
ATOM 4759 C PRO B 378 38.783 -39.082 178.680 1.00172.42 C
ANISOU 4759 C PRO B 378 28956 21127 15428 335 2396 -3318 C
ATOM 4760 O PRO B 378 38.379 -40.044 179.336 1.00171.74 O
ANISOU 4760 O PRO B 378 28692 20944 15616 340 2188 -3487 O
ATOM 4761 CB PRO B 378 40.787 -39.594 177.251 1.00173.99 C
ANISOU 4761 CB PRO B 378 29414 21277 15416 436 3255 -3564 C
ATOM 4762 CG PRO B 378 41.200 -40.930 177.749 1.00172.36 C
ANISOU 4762 CG PRO B 378 28991 20927 15571 515 3348 -3848 C
ATOM 4763 CD PRO B 378 41.773 -40.705 179.123 1.00166.61 C
ANISOU 4763 CD PRO B 378 27779 20154 15372 568 3475 -3713 C
TER 4764 PRO B 378
HETATM 4765 C01 NV8 A 401 26.501 -4.480 224.501 1.00115.93 C
HETATM 4766 C02 NV8 A 401 28.943 3.483 225.016 1.00 96.29 C
HETATM 4767 C03 NV8 A 401 28.646 4.788 225.388 1.00 84.56 C
HETATM 4768 C04 NV8 A 401 29.674 5.547 225.931 1.00 81.88 C
HETATM 4769 C05 NV8 A 401 30.951 5.033 226.096 1.00 84.01 C
HETATM 4770 C06 NV8 A 401 31.267 3.735 225.725 1.00 89.04 C
HETATM 4771 C07 NV8 A 401 30.231 2.989 225.185 1.00 97.60 C
HETATM 4772 C08 NV8 A 401 29.091 -3.889 226.837 1.00121.49 C
HETATM 4773 C09 NV8 A 401 28.862 -5.251 226.994 1.00115.49 C
HETATM 4774 C10 NV8 A 401 29.914 -6.089 227.326 1.00113.33 C
HETATM 4775 C11 NV8 A 401 31.181 -5.556 227.490 1.00115.43 C
HETATM 4776 C12 NV8 A 401 26.980 -4.914 223.136 1.00112.56 C
HETATM 4777 C13 NV8 A 401 31.405 -4.196 227.342 1.00119.71 C
HETATM 4778 C14 NV8 A 401 30.359 -3.358 227.012 1.00118.65 C
HETATM 4779 C15 NV8 A 401 27.270 -3.613 222.423 1.00110.18 C
HETATM 4780 C16 NV8 A 401 27.663 -2.551 223.474 1.00107.05 C
HETATM 4781 C17 NV8 A 401 26.782 -1.322 223.260 1.00104.65 C
HETATM 4782 C18 NV8 A 401 27.241 -0.067 223.990 1.00103.04 C
HETATM 4783 C19 NV8 A 401 29.543 -0.831 224.013 1.00 97.00 C
HETATM 4784 C20 NV8 A 401 29.143 -2.149 223.325 1.00 95.83 C
HETATM 4785 C21 NV8 A 401 28.976 1.514 224.334 1.00 97.83 C
HETATM 4786 N01 NV8 A 401 27.305 -3.258 224.744 1.00117.73 N
HETATM 4787 N02 NV8 A 401 28.642 0.301 223.825 1.00 98.94 N
HETATM 4788 N03 NV8 A 401 28.163 2.526 224.474 1.00 95.70 N
HETATM 4789 O01 NV8 A 401 26.637 -3.310 227.258 1.00145.16 O
HETATM 4790 O02 NV8 A 401 28.174 -1.470 226.551 1.00143.49 O
HETATM 4791 O03 NV8 A 401 30.248 1.716 224.748 1.00100.69 O
HETATM 4792 S01 NV8 A 401 27.717 -2.832 226.416 1.00143.30 S
HETATM 4793 H01 NV8 A 401 26.646 -5.177 225.161 1.00139.24 H
HETATM 4794 H02 NV8 A 401 25.558 -4.261 224.439 1.00139.24 H
HETATM 4795 H09 NV8 A 401 27.786 5.124 225.277 1.00101.59 H
HETATM 4796 H10 NV8 A 401 29.506 6.424 226.191 1.00 98.39 H
HETATM 4797 H11 NV8 A 401 31.610 5.578 226.460 1.00100.94 H
HETATM 4798 H12 NV8 A 401 32.118 3.375 225.828 1.00106.97 H
HETATM 4799 H13 NV8 A 401 28.008 -5.600 226.877 1.00138.71 H
HETATM 4800 H14 NV8 A 401 29.769 -7.002 227.428 1.00136.12 H
HETATM 4801 H15 NV8 A 401 31.889 -6.116 227.715 1.00138.64 H
HETATM 4802 H03 NV8 A 401 27.783 -5.452 223.216 1.00135.21 H
HETATM 4803 H18 NV8 A 401 26.319 -5.453 222.674 1.00135.21 H
HETATM 4804 H16 NV8 A 401 32.259 -3.847 227.456 1.00143.78 H
HETATM 4805 H17 NV8 A 401 30.509 -2.446 226.908 1.00142.50 H
HETATM 4806 H19 NV8 A 401 26.459 -3.347 221.963 1.00132.34 H
HETATM 4807 H20 NV8 A 401 27.932 -3.728 221.724 1.00132.34 H
HETATM 4808 H22 NV8 A 401 25.871 -1.517 223.533 1.00125.70 H
HETATM 4809 H21 NV8 A 401 26.718 -1.093 222.320 1.00125.70 H
HETATM 4810 H23 NV8 A 401 27.025 -0.113 224.935 1.00123.77 H
HETATM 4811 H04 NV8 A 401 26.700 0.662 223.649 1.00123.77 H
HETATM 4812 H06 NV8 A 401 30.405 -0.584 223.641 1.00116.53 H
HETATM 4813 H05 NV8 A 401 29.704 -0.943 224.963 1.00116.53 H
HETATM 4814 H08 NV8 A 401 29.379 -2.045 222.390 1.00115.12 H
HETATM 4815 H07 NV8 A 401 29.719 -2.867 223.634 1.00115.12 H
HETATM 4816 S SO4 A 402 58.016 -20.877 227.093 1.00 97.77 S
HETATM 4817 O1 SO4 A 402 57.865 -21.909 226.070 1.00104.58 O
HETATM 4818 O2 SO4 A 402 57.577 -19.593 226.554 1.00 98.99 O
HETATM 4819 O3 SO4 A 402 59.416 -20.781 227.494 1.00108.19 O
HETATM 4820 O4 SO4 A 402 57.206 -21.228 228.257 1.00 95.64 O
HETATM 4821 S SO4 A 403 58.904 -13.104 236.850 1.00127.38 S
HETATM 4822 O1 SO4 A 403 58.481 -13.927 235.720 1.00126.80 O
HETATM 4823 O2 SO4 A 403 58.951 -11.703 236.438 1.00124.83 O
HETATM 4824 O3 SO4 A 403 60.230 -13.528 237.290 1.00133.30 O
HETATM 4825 O4 SO4 A 403 57.958 -13.263 237.951 1.00126.49 O
HETATM 4826 CAD PGW A 404 36.468 -34.469 234.063 1.00145.80 C
HETATM 4827 OAE PGW A 404 35.642 -33.781 235.008 1.00148.64 O
HETATM 4828 OAF PGW A 404 37.481 -32.327 233.637 1.00145.47 O
HETATM 4829 P PGW A 404 40.445 -33.452 231.144 1.00140.35 P
HETATM 4830 C01 PGW A 404 36.958 -31.342 229.765 1.00103.43 C
HETATM 4831 C1 PGW A 404 39.537 -29.583 227.803 1.00 80.51 C
HETATM 4832 O01 PGW A 404 38.759 -29.915 228.984 1.00 90.54 O
HETATM 4833 C02 PGW A 404 38.161 -31.201 228.835 1.00102.66 C
HETATM 4834 C2 PGW A 404 40.183 -28.233 227.639 1.00 70.90 C
HETATM 4835 O02 PGW A 404 39.661 -30.420 226.929 1.00 91.34 O
HETATM 4836 C03 PGW A 404 39.207 -32.271 229.136 1.00116.55 C
HETATM 4837 C3 PGW A 404 39.882 -27.758 226.224 1.00 69.47 C
HETATM 4838 O03 PGW A 404 35.797 -30.850 229.095 1.00102.13 O
HETATM 4839 C04 PGW A 404 38.501 -34.284 232.670 1.00144.92 C
HETATM 4840 C4 PGW A 404 41.156 -27.444 225.455 1.00 69.27 C
HETATM 4841 O04 PGW A 404 34.290 -31.940 230.480 1.00110.71 O
HETATM 4842 C05 PGW A 404 37.774 -33.707 233.876 1.00145.33 C
HETATM 4843 C5 PGW A 404 41.694 -26.072 225.829 1.00 64.14 C
HETATM 4844 C06 PGW A 404 41.246 -20.380 222.598 1.00 61.94 C
HETATM 4845 C6 PGW A 404 41.242 -25.010 224.834 1.00 59.11 C
HETATM 4846 C07 PGW A 404 40.032 -19.499 222.313 1.00 77.41 C
HETATM 4847 C7 PGW A 404 42.439 -24.185 224.374 1.00 60.36 C
HETATM 4848 C08 PGW A 404 39.926 -19.146 220.831 1.00 79.36 C
HETATM 4849 C8 PGW A 404 41.982 -22.964 223.588 1.00 75.27 C
HETATM 4850 C09 PGW A 404 39.082 -17.892 220.608 1.00 78.67 C
HETATM 4851 C9 PGW A 404 41.671 -21.840 224.544 1.00 72.06 C
HETATM 4852 C10 PGW A 404 41.339 -20.638 224.081 1.00 63.65 C
HETATM 4853 C11 PGW A 404 37.586 -18.181 220.698 1.00 77.33 C
HETATM 4854 O11 PGW A 404 39.266 -32.537 230.535 1.00131.02 O
HETATM 4855 C12 PGW A 404 36.863 -17.533 219.522 1.00 85.53 C
HETATM 4856 O12 PGW A 404 39.844 -33.808 232.595 1.00144.72 O
HETATM 4857 C13 PGW A 404 35.388 -17.908 219.492 1.00 85.17 C
HETATM 4858 O13 PGW A 404 40.510 -34.723 230.329 1.00140.08 O
HETATM 4859 C14 PGW A 404 34.612 -17.135 220.532 1.00 83.17 C
HETATM 4860 O14 PGW A 404 41.674 -32.585 231.299 1.00135.43 O
HETATM 4861 C15 PGW A 404 32.032 -23.244 227.584 1.00 65.80 C
HETATM 4862 C16 PGW A 404 32.522 -22.770 226.220 1.00 63.22 C
HETATM 4863 C17 PGW A 404 32.253 -23.792 225.121 1.00 64.95 C
HETATM 4864 C18 PGW A 404 32.612 -23.223 223.749 1.00 61.53 C
HETATM 4865 C19 PGW A 404 34.473 -31.367 229.418 1.00103.47 C
HETATM 4866 C20 PGW A 404 33.343 -31.215 228.426 1.00 96.94 C
HETATM 4867 C21 PGW A 404 33.144 -29.748 228.062 1.00 87.08 C
HETATM 4868 C22 PGW A 404 31.886 -29.190 228.717 1.00 76.43 C
HETATM 4869 C23 PGW A 404 31.699 -27.717 228.379 1.00 69.89 C
HETATM 4870 C24 PGW A 404 30.475 -27.149 229.083 1.00 70.63 C
HETATM 4871 C25 PGW A 404 30.487 -25.627 229.031 1.00 70.26 C
HETATM 4872 C26 PGW A 404 30.363 -25.119 227.600 1.00 77.71 C
HETATM 4873 C27 PGW A 404 30.554 -23.608 227.543 1.00 76.13 C
HETATM 4874 C28 PGW A 404 32.517 -24.273 222.645 1.00 54.71 C
HETATM 4875 C29 PGW A 404 33.001 -24.727 220.205 1.00 49.11 C
HETATM 4876 C30 PGW A 404 32.878 -23.671 221.288 1.00 58.47 C
HETATM 4877 C1 SOG A 405 16.458 11.637 244.253 1.00110.18 C
HETATM 4878 C2 SOG A 405 15.192 10.877 244.615 1.00111.75 C
HETATM 4879 C3 SOG A 405 14.012 11.599 243.994 1.00114.05 C
HETATM 4880 C4 SOG A 405 14.009 13.056 244.439 1.00119.13 C
HETATM 4881 C5 SOG A 405 15.356 13.728 244.181 1.00118.27 C
HETATM 4882 C6 SOG A 405 15.341 15.149 244.738 1.00120.94 C
HETATM 4883 C1' SOG A 405 18.559 10.446 243.245 1.00 87.65 C
HETATM 4884 C2' SOG A 405 20.063 10.242 243.320 1.00 85.55 C
HETATM 4885 C3' SOG A 405 20.605 10.086 241.905 1.00 80.79 C
HETATM 4886 C4' SOG A 405 22.080 10.460 241.839 1.00 77.48 C
HETATM 4887 C5' SOG A 405 22.299 11.568 240.817 1.00 73.42 C
HETATM 4888 C6' SOG A 405 23.764 11.986 240.764 1.00 74.95 C
HETATM 4889 C7' SOG A 405 24.398 11.574 239.442 1.00 80.19 C
HETATM 4890 C8' SOG A 405 25.784 12.163 239.298 1.00 83.28 C
HETATM 4891 S1 SOG A 405 17.874 10.762 244.836 1.00100.44 S
HETATM 4892 O2 SOG A 405 15.265 9.542 244.102 1.00118.51 O
HETATM 4893 O3 SOG A 405 12.797 10.961 244.399 1.00118.74 O
HETATM 4894 O4 SOG A 405 12.986 13.759 243.727 1.00123.93 O
HETATM 4895 O5 SOG A 405 16.411 12.968 244.778 1.00112.72 O
HETATM 4896 O6 SOG A 405 16.585 15.809 244.478 1.00123.94 O
HETATM 4897 C1 SOG A 406 48.618 -15.250 212.800 1.00126.73 C
HETATM 4898 C2 SOG A 406 49.972 -15.773 212.328 1.00127.81 C
HETATM 4899 C3 SOG A 406 50.798 -14.663 211.689 1.00132.15 C
HETATM 4900 C4 SOG A 406 49.973 -13.942 210.631 1.00133.25 C
HETATM 4901 C5 SOG A 406 48.659 -13.461 211.234 1.00128.64 C
HETATM 4902 C6 SOG A 406 47.793 -12.750 210.200 1.00125.92 C
HETATM 4903 C1' SOG A 406 46.073 -15.772 213.541 1.00114.80 C
HETATM 4904 C2' SOG A 406 45.076 -16.676 214.259 1.00102.95 C
HETATM 4905 C3' SOG A 406 44.009 -17.210 213.310 1.00 97.24 C
HETATM 4906 C4' SOG A 406 42.791 -17.732 214.071 1.00 93.37 C
HETATM 4907 C5' SOG A 406 42.007 -16.578 214.686 1.00 92.01 C
HETATM 4908 C6' SOG A 406 40.597 -16.978 215.114 1.00 81.92 C
HETATM 4909 C7' SOG A 406 39.836 -15.748 215.600 1.00 75.63 C
HETATM 4910 C8' SOG A 406 38.370 -16.051 215.828 1.00 69.70 C
HETATM 4911 S1 SOG A 406 47.615 -16.601 213.334 1.00128.50 S
HETATM 4912 O2 SOG A 406 50.689 -16.324 213.439 1.00125.36 O
HETATM 4913 O3 SOG A 406 51.973 -15.222 211.089 1.00132.04 O
HETATM 4914 O4 SOG A 406 50.710 -12.828 210.113 1.00137.00 O
HETATM 4915 O5 SOG A 406 47.945 -14.590 211.730 1.00128.27 O
HETATM 4916 O6 SOG A 406 48.347 -11.464 209.902 1.00126.52 O
HETATM 4917 C1 SOG A 407 11.554 -14.156 226.175 1.00128.58 C
HETATM 4918 C2 SOG A 407 11.971 -13.979 227.637 1.00132.09 C
HETATM 4919 C3 SOG A 407 10.870 -13.560 228.609 1.00130.23 C
HETATM 4920 C4 SOG A 407 9.790 -12.710 227.960 1.00134.64 C
HETATM 4921 C5 SOG A 407 9.388 -13.315 226.627 1.00137.34 C
HETATM 4922 C6 SOG A 407 8.212 -12.555 226.024 1.00141.20 C
HETATM 4923 C1' SOG A 407 13.355 -15.556 224.660 1.00115.12 C
HETATM 4924 C2' SOG A 407 14.846 -15.706 224.359 1.00108.03 C
HETATM 4925 C3' SOG A 407 15.190 -15.404 222.901 1.00103.30 C
HETATM 4926 C4' SOG A 407 16.634 -15.798 222.597 1.00 94.90 C
HETATM 4927 C5' SOG A 407 16.983 -15.700 221.112 1.00 84.91 C
HETATM 4928 C6' SOG A 407 18.329 -16.372 220.846 1.00 78.84 C
HETATM 4929 C7' SOG A 407 18.706 -16.368 219.370 1.00 74.88 C
HETATM 4930 C8' SOG A 407 20.081 -16.975 219.162 1.00 71.84 C
HETATM 4931 S1 SOG A 407 12.996 -13.908 225.178 1.00123.64 S
HETATM 4932 O2 SOG A 407 12.503 -15.230 228.092 1.00138.63 O
HETATM 4933 O3 SOG A 407 11.468 -12.807 229.672 1.00126.98 O
HETATM 4934 O4 SOG A 407 8.648 -12.645 228.824 1.00137.28 O
HETATM 4935 O5 SOG A 407 10.523 -13.252 225.767 1.00132.31 O
HETATM 4936 O6 SOG A 407 7.083 -12.649 226.903 1.00140.12 O
HETATM 4937 C1 SOG A 408 10.412 -14.916 220.993 1.00145.96 C
HETATM 4938 C2 SOG A 408 9.982 -13.449 221.055 1.00145.67 C
HETATM 4939 C3 SOG A 408 9.774 -12.828 219.675 1.00141.82 C
HETATM 4940 C4 SOG A 408 8.820 -13.662 218.825 1.00141.29 C
HETATM 4941 C5 SOG A 408 8.662 -15.067 219.391 1.00145.81 C
HETATM 4942 C6 SOG A 408 8.048 -15.993 218.344 1.00149.44 C
HETATM 4943 C1' SOG A 408 12.359 -16.762 221.379 1.00145.02 C
HETATM 4944 S1 SOG A 408 12.173 -15.032 221.095 1.00144.54 S
HETATM 4945 O2 SOG A 408 8.769 -13.348 221.809 1.00146.26 O
HETATM 4946 O3 SOG A 408 11.031 -12.681 219.003 1.00135.45 O
HETATM 4947 O4 SOG A 408 7.539 -13.025 218.774 1.00138.23 O
HETATM 4948 O5 SOG A 408 9.941 -15.551 219.800 1.00148.02 O
HETATM 4949 O6 SOG A 408 7.138 -16.909 218.966 1.00149.96 O
HETATM 4950 C1 SOG A 409 55.303 -28.438 210.838 1.00149.97 C
HETATM 4951 C2 SOG A 409 54.302 -28.209 209.714 1.00152.41 C
HETATM 4952 C3 SOG A 409 54.738 -27.010 208.886 1.00152.93 C
HETATM 4953 C4 SOG A 409 54.908 -25.798 209.791 1.00149.92 C
HETATM 4954 C5 SOG A 409 55.820 -26.118 210.971 1.00146.33 C
HETATM 4955 C6 SOG A 409 55.875 -24.938 211.935 1.00140.84 C
HETATM 4956 C1' SOG A 409 56.367 -30.340 212.442 1.00145.35 C
HETATM 4957 C2' SOG A 409 56.198 -31.657 213.190 1.00144.74 C
HETATM 4958 S1 SOG A 409 54.808 -29.837 211.793 1.00147.54 S
HETATM 4959 O2 SOG A 409 54.221 -29.374 208.884 1.00152.97 O
HETATM 4960 O3 SOG A 409 53.756 -26.731 207.882 1.00155.81 O
HETATM 4961 O4 SOG A 409 55.472 -24.718 209.039 1.00150.35 O
HETATM 4962 O5 SOG A 409 55.361 -27.278 211.669 1.00148.04 O
HETATM 4963 O6 SOG A 409 55.961 -23.717 211.191 1.00136.73 O
HETATM 4964 C1 SOG A 410 21.914 4.441 226.712 1.00126.07 C
HETATM 4965 C2 SOG A 410 20.848 4.212 227.785 1.00128.82 C
HETATM 4966 C3 SOG A 410 19.904 5.401 227.946 1.00125.18 C
HETATM 4967 C4 SOG A 410 20.692 6.700 228.027 1.00117.64 C
HETATM 4968 C5 SOG A 410 21.640 6.784 226.841 1.00113.86 C
HETATM 4969 C6 SOG A 410 22.375 8.119 226.816 1.00 98.50 C
HETATM 4970 C1' SOG A 410 24.595 3.989 227.119 1.00116.22 C
HETATM 4971 C2' SOG A 410 25.424 3.156 228.092 1.00109.53 C
HETATM 4972 C3' SOG A 410 26.921 3.441 228.025 1.00101.43 C
HETATM 4973 C4' SOG A 410 27.684 2.122 228.105 1.00 94.48 C
HETATM 4974 C5' SOG A 410 29.154 2.297 228.470 1.00 91.54 C
HETATM 4975 C6' SOG A 410 29.851 0.940 228.443 1.00 88.79 C
HETATM 4976 C7' SOG A 410 31.192 0.969 229.165 1.00 86.37 C
HETATM 4977 C8' SOG A 410 31.780 -0.423 229.259 1.00 86.36 C
HETATM 4978 S1 SOG A 410 23.084 3.124 226.836 1.00124.67 S
HETATM 4979 O2 SOG A 410 20.083 3.044 227.458 1.00128.80 O
HETATM 4980 O3 SOG A 410 19.132 5.240 229.141 1.00123.99 O
HETATM 4981 O4 SOG A 410 19.797 7.816 228.012 1.00117.48 O
HETATM 4982 O5 SOG A 410 22.562 5.697 226.921 1.00121.17 O
HETATM 4983 O6 SOG A 410 22.808 8.403 225.481 1.00 91.61 O
HETATM 4984 C1' SOG A 411 18.587 -4.348 211.307 1.00139.92 C
HETATM 4985 C2' SOG A 411 18.587 -2.889 211.741 1.00122.56 C
HETATM 4986 C3' SOG A 411 19.686 -2.111 211.030 1.00112.76 C
HETATM 4987 C4' SOG A 411 19.603 -0.630 211.375 1.00107.43 C
HETATM 4988 S1 SOG A 411 17.209 -5.156 212.047 1.00157.56 S
HETATM 4989 C5' SOG A 412 16.624 0.500 230.457 1.00 69.41 C
HETATM 4990 C6' SOG A 412 18.109 0.157 230.527 1.00 72.48 C
HETATM 4991 C7' SOG A 412 18.971 1.414 230.479 1.00 82.01 C
HETATM 4992 C8' SOG A 412 20.432 1.060 230.305 1.00 74.06 C
HETATM 4993 NA NA A 413 39.671 -4.880 229.961 1.00 82.33 NA1+
HETATM 4994 C01 NV8 B 401 27.108 -31.262 217.287 1.00133.64 C
HETATM 4995 C02 NV8 B 401 30.330 -38.320 214.318 1.00 97.30 C
HETATM 4996 C03 NV8 B 401 30.145 -39.679 214.103 1.00 88.23 C
HETATM 4997 C04 NV8 B 401 30.696 -40.222 212.947 1.00 80.89 C
HETATM 4998 C05 NV8 B 401 31.405 -39.448 212.039 1.00 80.06 C
HETATM 4999 C06 NV8 B 401 31.600 -38.091 212.235 1.00 82.03 C
HETATM 5000 C07 NV8 B 401 31.046 -37.567 213.389 1.00 94.51 C
HETATM 5001 C08 NV8 B 401 27.460 -31.158 213.797 1.00131.07 C
HETATM 5002 C09 NV8 B 401 26.688 -29.999 213.880 1.00131.26 C
HETATM 5003 C10 NV8 B 401 27.023 -28.892 213.116 1.00133.01 C
HETATM 5004 C11 NV8 B 401 28.130 -28.949 212.281 1.00133.89 C
HETATM 5005 C12 NV8 B 401 28.293 -30.471 217.813 1.00134.94 C
HETATM 5006 C13 NV8 B 401 28.903 -30.100 212.201 1.00132.39 C
HETATM 5007 C14 NV8 B 401 28.574 -31.205 212.965 1.00129.30 C
HETATM 5008 C15 NV8 B 401 29.417 -31.483 217.867 1.00133.50 C
HETATM 5009 C16 NV8 B 401 29.128 -32.585 216.820 1.00129.48 C
HETATM 5010 C17 NV8 B 401 29.037 -33.946 217.529 1.00125.55 C
HETATM 5011 C18 NV8 B 401 29.097 -35.164 216.613 1.00117.44 C
HETATM 5012 C19 NV8 B 401 30.437 -33.928 214.992 1.00114.98 C
HETATM 5013 C20 NV8 B 401 30.260 -32.612 215.774 1.00120.27 C
HETATM 5014 C21 NV8 B 401 30.389 -36.351 214.997 1.00101.04 C
HETATM 5015 N01 NV8 B 401 27.782 -32.157 216.326 1.00131.18 N
HETATM 5016 N02 NV8 B 401 30.237 -35.195 215.701 1.00111.01 N
HETATM 5017 N03 NV8 B 401 29.919 -37.526 215.333 1.00101.18 N
HETATM 5018 O01 NV8 B 401 25.562 -32.510 214.924 1.00128.10 O
HETATM 5019 O02 NV8 B 401 27.635 -33.729 214.210 1.00138.81 O
HETATM 5020 O03 NV8 B 401 31.075 -36.298 213.827 1.00 98.74 O
HETATM 5021 S01 NV8 B 401 27.006 -32.570 214.797 1.00134.65 S
HETATM 5022 H01 NV8 B 401 26.445 -30.681 216.883 1.00160.49 H
HETATM 5023 H02 NV8 B 401 26.724 -31.769 218.020 1.00160.49 H
HETATM 5024 H09 NV8 B 401 29.670 -40.191 214.716 1.00106.01 H
HETATM 5025 H10 NV8 B 401 30.590 -41.129 212.775 1.00 97.19 H
HETATM 5026 H11 NV8 B 401 31.754 -39.855 211.280 1.00 96.20 H
HETATM 5027 H12 NV8 B 401 32.071 -37.557 211.637 1.00 98.56 H
HETATM 5028 H13 NV8 B 401 25.947 -29.970 214.440 1.00157.64 H
HETATM 5029 H14 NV8 B 401 26.509 -28.119 213.164 1.00159.74 H
HETATM 5030 H15 NV8 B 401 28.356 -28.207 211.769 1.00160.79 H
HETATM 5031 H03 NV8 B 401 28.511 -29.746 217.206 1.00162.05 H
HETATM 5032 H18 NV8 B 401 28.108 -30.073 218.678 1.00162.05 H
HETATM 5033 H16 NV8 B 401 29.644 -30.127 211.640 1.00159.00 H
HETATM 5034 H17 NV8 B 401 29.090 -31.977 212.909 1.00155.28 H
HETATM 5035 H19 NV8 B 401 29.426 -31.861 218.761 1.00160.33 H
HETATM 5036 H20 NV8 B 401 30.284 -31.064 217.759 1.00160.33 H
HETATM 5037 H22 NV8 B 401 28.217 -33.995 218.044 1.00150.79 H
HETATM 5038 H21 NV8 B 401 29.747 -34.050 218.181 1.00150.79 H
HETATM 5039 H23 NV8 B 401 28.273 -35.275 216.114 1.00141.05 H
HETATM 5040 H04 NV8 B 401 29.150 -35.944 217.187 1.00141.05 H
HETATM 5041 H06 NV8 B 401 31.352 -33.921 214.672 1.00138.11 H
HETATM 5042 H05 NV8 B 401 29.897 -33.946 214.186 1.00138.11 H
HETATM 5043 H08 NV8 B 401 31.116 -32.439 216.196 1.00144.46 H
HETATM 5044 H07 NV8 B 401 30.155 -31.876 215.151 1.00144.46 H
HETATM 5045 S SO4 B 402 43.282 -7.613 195.124 1.00 96.16 S
HETATM 5046 O1 SO4 B 402 41.866 -7.700 194.775 1.00 88.48 O
HETATM 5047 O2 SO4 B 402 44.066 -7.424 193.908 1.00111.44 O
HETATM 5048 O3 SO4 B 402 43.494 -6.480 196.019 1.00 96.80 O
HETATM 5049 O4 SO4 B 402 43.697 -8.844 195.788 1.00101.81 O
HETATM 5050 S SO4 B 403 38.844 -15.992 186.840 1.00117.19 S
HETATM 5051 O1 SO4 B 403 39.477 -15.071 185.901 1.00124.20 O
HETATM 5052 O2 SO4 B 403 38.935 -17.357 186.327 1.00120.07 O
HETATM 5053 O3 SO4 B 403 39.526 -15.914 188.130 1.00112.63 O
HETATM 5054 O4 SO4 B 403 37.438 -15.627 186.999 1.00106.60 O
HETATM 5055 CAD PGW B 404 26.692 2.713 208.269 1.00121.98 C
HETATM 5056 OAE PGW B 404 27.307 3.447 209.336 1.00112.00 O
HETATM 5057 OAF PGW B 404 28.418 1.070 207.868 1.00134.45 O
HETATM 5058 P PGW B 404 25.652 -0.331 205.020 1.00153.97 P
HETATM 5059 C01 PGW B 404 24.183 -3.588 208.047 1.00109.36 C
HETATM 5060 C1 PGW B 404 27.605 -3.906 208.064 1.00 85.07 C
HETATM 5061 O01 PGW B 404 26.409 -4.234 207.305 1.00100.05 O
HETATM 5062 C02 PGW B 404 25.462 -3.164 207.342 1.00111.48 C
HETATM 5063 C2 PGW B 404 28.953 -4.463 207.671 1.00 72.79 C
HETATM 5064 O02 PGW B 404 27.495 -3.168 209.025 1.00 91.10 O
HETATM 5065 C03 PGW B 404 25.090 -2.714 205.936 1.00131.17 C
HETATM 5066 C3 PGW B 404 29.451 -5.480 208.692 1.00 66.50 C
HETATM 5067 O03 PGW B 404 24.418 -3.660 209.449 1.00107.17 O
HETATM 5068 C04 PGW B 404 26.125 0.387 207.531 1.00137.82 C
HETATM 5069 C4 PGW B 404 30.969 -5.632 208.607 1.00 62.65 C
HETATM 5070 O04 PGW B 404 22.498 -2.512 210.012 1.00111.90 O
HETATM 5071 C05 PGW B 404 27.083 1.240 208.360 1.00131.71 C
HETATM 5072 C5 PGW B 404 31.417 -7.051 208.268 1.00 62.46 C
HETATM 5073 C06 PGW B 404 34.896 -12.010 210.193 1.00 80.84 C
HETATM 5074 C6 PGW B 404 32.866 -7.266 208.708 1.00 65.98 C
HETATM 5075 C07 PGW B 404 34.395 -13.266 210.899 1.00 75.79 C
HETATM 5076 C7 PGW B 404 33.519 -8.454 208.005 1.00 67.44 C
HETATM 5077 C08 PGW B 404 35.048 -13.451 212.268 1.00 81.87 C
HETATM 5078 C8 PGW B 404 33.828 -9.586 208.980 1.00 80.33 C
HETATM 5079 C09 PGW B 404 34.711 -14.821 212.853 1.00 85.76 C
HETATM 5080 C9 PGW B 404 33.902 -10.888 208.216 1.00 79.35 C
HETATM 5081 C10 PGW B 404 34.392 -11.997 208.768 1.00 76.21 C
HETATM 5082 C11 PGW B 404 35.278 -14.994 214.258 1.00 82.57 C
HETATM 5083 O11 PGW B 404 26.081 -1.828 205.426 1.00146.46 O
HETATM 5084 C12 PGW B 404 34.247 -14.621 215.317 1.00 79.78 C
HETATM 5085 O12 PGW B 404 26.380 0.577 206.139 1.00147.02 O
HETATM 5086 C13 PGW B 404 33.138 -15.664 215.400 1.00 74.11 C
HETATM 5087 O13 PGW B 404 26.278 -0.026 203.679 1.00155.11 O
HETATM 5088 C14 PGW B 404 33.489 -16.755 216.387 1.00 71.92 C
HETATM 5089 O14 PGW B 404 24.153 -0.222 205.183 1.00155.78 O
HETATM 5090 C15 PGW B 404 24.866 -12.423 213.340 1.00 56.31 C
HETATM 5091 C16 PGW B 404 25.851 -11.337 213.759 1.00 46.13 C
HETATM 5092 C17 PGW B 404 26.964 -11.839 214.675 1.00 44.16 C
HETATM 5093 C18 PGW B 404 27.508 -10.671 215.490 1.00 50.52 C
HETATM 5094 C19 PGW B 404 23.331 -3.337 210.356 1.00105.19 C
HETATM 5095 C20 PGW B 404 23.234 -4.037 211.690 1.00 92.97 C
HETATM 5096 C21 PGW B 404 22.951 -5.510 211.424 1.00 81.95 C
HETATM 5097 C22 PGW B 404 22.922 -6.331 212.706 1.00 69.46 C
HETATM 5098 C23 PGW B 404 22.238 -7.667 212.444 1.00 65.51 C
HETATM 5099 C24 PGW B 404 22.537 -8.678 213.544 1.00 72.36 C
HETATM 5100 C25 PGW B 404 21.895 -10.026 213.233 1.00 72.30 C
HETATM 5101 C26 PGW B 404 22.740 -11.162 213.797 1.00 76.72 C
HETATM 5102 C27 PGW B 404 23.622 -11.791 212.724 1.00 66.55 C
HETATM 5103 C28 PGW B 404 28.687 -11.054 216.378 1.00 51.17 C
HETATM 5104 C29 PGW B 404 30.550 -10.064 217.767 1.00 45.74 C
HETATM 5105 C30 PGW B 404 29.202 -9.824 217.120 1.00 52.62 C
HETATM 5106 C1 SOG B 405 43.873 -8.867 206.411 1.00165.26 C
HETATM 5107 C2 SOG B 405 43.210 -10.199 206.752 1.00166.26 C
HETATM 5108 C3 SOG B 405 43.418 -10.602 208.204 1.00167.97 C
HETATM 5109 C4 SOG B 405 44.892 -10.497 208.555 1.00166.66 C
HETATM 5110 C5 SOG B 405 45.384 -9.090 208.255 1.00163.78 C
HETATM 5111 C6 SOG B 405 46.849 -8.947 208.647 1.00161.97 C
HETATM 5112 C1' SOG B 405 43.854 -6.960 204.423 1.00163.51 C
HETATM 5113 C2' SOG B 405 43.615 -6.656 202.947 1.00160.35 C
HETATM 5114 S1 SOG B 405 43.831 -8.706 204.652 1.00166.83 S
HETATM 5115 O2 SOG B 405 41.806 -10.106 206.485 1.00166.68 O
HETATM 5116 O3 SOG B 405 42.976 -11.951 208.394 1.00168.91 O
HETATM 5117 O4 SOG B 405 45.084 -10.802 209.940 1.00167.99 O
HETATM 5118 O5 SOG B 405 45.230 -8.821 206.860 1.00164.07 O
HETATM 5119 O6 SOG B 405 47.038 -9.494 209.957 1.00162.19 O
HETATM 5120 C1 SOG B 406 41.476 -50.116 215.459 1.00124.49 C
HETATM 5121 C2 SOG B 406 40.435 -50.479 216.510 1.00116.77 C
HETATM 5122 C3 SOG B 406 39.571 -51.611 215.978 1.00111.13 C
HETATM 5123 C4 SOG B 406 38.942 -51.188 214.658 1.00121.05 C
HETATM 5124 C5 SOG B 406 40.006 -50.702 213.677 1.00126.38 C
HETATM 5125 C6 SOG B 406 39.343 -50.164 212.413 1.00127.17 C
HETATM 5126 C1' SOG B 406 43.808 -48.878 214.868 1.00127.45 C
HETATM 5127 S1 SOG B 406 42.527 -48.838 216.078 1.00125.46 S
HETATM 5128 O2 SOG B 406 41.077 -50.885 217.724 1.00116.87 O
HETATM 5129 O3 SOG B 406 38.552 -51.933 216.930 1.00104.04 O
HETATM 5130 O4 SOG B 406 38.235 -52.296 214.087 1.00124.94 O
HETATM 5131 O5 SOG B 406 40.810 -49.679 214.272 1.00127.09 O
HETATM 5132 O6 SOG B 406 40.339 -49.682 211.503 1.00129.39 O
HETATM 5133 C1' SOG B 407 31.812 -33.840 231.276 1.00 99.70 C
HETATM 5134 C2' SOG B 407 31.312 -35.186 230.766 1.00 98.14 C
HETATM 5135 C3' SOG B 407 32.471 -36.120 230.439 1.00 95.77 C
HETATM 5136 C4' SOG B 407 31.960 -37.426 229.841 1.00 90.91 C
HETATM 5137 S1 SOG B 407 30.425 -32.817 231.649 1.00105.86 S
HETATM 5138 C1 SOG B 408 21.737 -8.313 196.368 1.00150.48 C
HETATM 5139 C2 SOG B 408 20.805 -7.104 196.428 1.00145.61 C
HETATM 5140 C3 SOG B 408 19.692 -7.264 195.398 1.00146.81 C
HETATM 5141 C4 SOG B 408 20.305 -7.426 194.010 1.00148.64 C
HETATM 5142 C5 SOG B 408 21.339 -8.553 193.999 1.00148.40 C
HETATM 5143 C6 SOG B 408 22.061 -8.612 192.654 1.00141.27 C
HETATM 5144 C1' SOG B 408 23.715 -9.802 197.626 1.00134.82 C
HETATM 5145 C2' SOG B 408 24.733 -9.957 198.760 1.00122.51 C
HETATM 5146 C3' SOG B 408 24.994 -11.430 199.082 1.00117.59 C
HETATM 5147 C4' SOG B 408 26.007 -11.633 200.209 1.00110.65 C
HETATM 5148 C5' SOG B 408 26.345 -13.108 200.432 1.00103.86 C
HETATM 5149 C6' SOG B 408 25.235 -13.859 201.164 1.00106.92 C
HETATM 5150 C7' SOG B 408 25.695 -15.232 201.652 1.00105.94 C
HETATM 5151 C8' SOG B 408 24.702 -15.824 202.629 1.00102.69 C
HETATM 5152 S1 SOG B 408 23.011 -8.180 197.594 1.00156.73 S
HETATM 5153 O2 SOG B 408 20.252 -6.947 197.739 1.00141.49 O
HETATM 5154 O3 SOG B 408 18.823 -6.128 195.425 1.00146.08 O
HETATM 5155 O4 SOG B 408 19.279 -7.700 193.047 1.00149.90 O
HETATM 5156 O5 SOG B 408 22.300 -8.387 195.055 1.00151.27 O
HETATM 5157 O6 SOG B 408 21.142 -8.968 191.616 1.00135.89 O
HETATM 5158 C1 SOG B 409 43.197 -35.483 225.581 1.00138.00 C
HETATM 5159 C2 SOG B 409 42.065 -34.564 226.031 1.00135.96 C
HETATM 5160 C3 SOG B 409 40.950 -35.367 226.700 1.00138.29 C
HETATM 5161 C4 SOG B 409 40.530 -36.530 225.807 1.00133.40 C
HETATM 5162 C5 SOG B 409 41.759 -37.330 225.387 1.00133.15 C
HETATM 5163 C6 SOG B 409 41.374 -38.522 224.520 1.00126.24 C
HETATM 5164 C1' SOG B 409 45.589 -35.813 224.318 1.00122.92 C
HETATM 5165 C2' SOG B 409 46.544 -35.246 223.275 1.00123.06 C
HETATM 5166 C3' SOG B 409 47.710 -36.182 222.994 1.00122.69 C
HETATM 5167 C4' SOG B 409 48.697 -35.541 222.026 1.00124.52 C
HETATM 5168 C5' SOG B 409 49.862 -36.485 221.762 1.00127.37 C
HETATM 5169 C6' SOG B 409 50.919 -35.871 220.850 1.00127.51 C
HETATM 5170 C7' SOG B 409 52.057 -36.860 220.616 1.00126.14 C
HETATM 5171 C8' SOG B 409 53.075 -36.317 219.637 1.00123.32 C
HETATM 5172 S1 SOG B 409 44.455 -34.544 224.775 1.00137.18 S
HETATM 5173 O2 SOG B 409 42.574 -33.583 226.939 1.00132.18 O
HETATM 5174 O3 SOG B 409 39.828 -34.520 226.963 1.00140.22 O
HETATM 5175 O4 SOG B 409 39.612 -37.386 226.496 1.00131.29 O
HETATM 5176 O5 SOG B 409 42.671 -36.473 224.698 1.00137.22 O
HETATM 5177 O6 SOG B 409 40.754 -39.504 225.353 1.00125.20 O
HETATM 5178 O HOH A 501 47.744 -5.435 230.068 1.00 73.18 O
HETATM 5179 O HOH A 502 56.685 -14.457 229.089 1.00 83.11 O
HETATM 5180 O HOH A 503 18.073 0.596 222.025 1.00 57.88 O
HETATM 5181 O HOH A 504 42.041 -8.782 234.078 1.00 53.79 O
HETATM 5182 O HOH A 505 44.998 -15.836 228.810 1.00 54.86 O
HETATM 5183 O HOH A 506 61.327 -12.454 230.257 1.00 79.80 O
HETATM 5184 O HOH A 507 15.801 -5.965 222.481 1.00 69.76 O
HETATM 5185 O HOH A 508 26.950 12.169 227.177 1.00 60.04 O
HETATM 5186 O HOH A 509 31.330 -8.769 226.360 1.00 64.16 O
HETATM 5187 O HOH A 510 30.530 -5.334 234.358 1.00 46.76 O
HETATM 5188 O HOH A 511 28.922 -5.654 215.684 1.00 58.88 O
HETATM 5189 O HOH A 512 37.288 -2.385 227.586 1.00 76.44 O
HETATM 5190 O HOH A 513 52.901 -32.622 221.648 1.00 77.14 O
HETATM 5191 O HOH A 514 17.570 2.119 226.477 1.00 95.38 O
HETATM 5192 O HOH A 515 26.253 22.106 244.163 1.00105.37 O
HETATM 5193 O HOH A 516 53.136 -26.318 219.869 1.00 71.36 O
HETATM 5194 O HOH A 517 10.923 -4.957 231.844 1.00 72.40 O
HETATM 5195 O HOH A 518 26.496 -8.897 226.753 1.00 60.47 O
HETATM 5196 O HOH A 519 25.215 -0.646 228.562 1.00 76.48 O
HETATM 5197 O HOH A 520 56.936 -25.658 220.794 1.00 81.40 O
HETATM 5198 O HOH A 521 27.641 16.279 215.356 1.00 89.33 O
HETATM 5199 O HOH A 522 10.387 -7.415 222.637 1.00 67.41 O
HETATM 5200 O HOH A 523 37.471 -0.004 209.952 1.00 88.29 O
HETATM 5201 O HOH A 524 28.817 18.546 220.267 1.00 94.39 O
HETATM 5202 O HOH A 525 22.034 2.886 231.815 1.00 78.39 O
HETATM 5203 O HOH A 526 31.275 18.221 220.912 1.00 98.40 O
HETATM 5204 O HOH A 527 50.543 -20.467 216.426 1.00103.54 O
HETATM 5205 O HOH B 501 56.144 -13.138 209.035 1.00116.09 O
HETATM 5206 O HOH B 502 30.214 -24.130 199.843 1.00 62.11 O
HETATM 5207 O HOH B 503 32.193 -0.771 205.979 1.00 68.00 O
HETATM 5208 O HOH B 504 23.182 -30.302 207.101 1.00 57.12 O
HETATM 5209 O HOH B 505 43.276 -2.916 204.402 1.00 75.68 O
HETATM 5210 O HOH B 506 45.315 -1.991 194.539 1.00104.03 O
HETATM 5211 O HOH B 507 27.484 -43.515 224.377 1.00 80.56 O
HETATM 5212 O HOH B 508 28.965 -50.415 227.353 1.00 72.96 O
HETATM 5213 O HOH B 509 59.368 -14.030 206.475 1.00123.79 O
HETATM 5214 O HOH B 510 27.828 -38.323 217.235 1.00 76.80 O
HETATM 5215 O HOH B 511 55.590 -9.969 202.744 1.00 85.35 O
HETATM 5216 O HOH B 512 41.571 -17.700 190.186 1.00 86.47 O
HETATM 5217 O HOH B 513 24.729 -26.915 216.320 1.00 77.18 O
HETATM 5218 O HOH B 514 47.577 -8.146 196.195 1.00100.85 O
HETATM 5219 O HOH B 515 45.965 -30.916 219.785 1.00 67.55 O
CONECT 558 4993
CONECT 758 1310
CONECT 1310 758
CONECT 1862 4993
CONECT 2970 3598
CONECT 3598 2970
CONECT 4765 4776 4786 4793 4794
CONECT 4766 4767 4771 4788
CONECT 4767 4766 4768 4795
CONECT 4768 4767 4769 4796
CONECT 4769 4768 4770 4797
CONECT 4770 4769 4771 4798
CONECT 4771 4766 4770 4791
CONECT 4772 4773 4778 4792
CONECT 4773 4772 4774 4799
CONECT 4774 4773 4775 4800
CONECT 4775 4774 4777 4801
CONECT 4776 4765 4779 4802 4803
CONECT 4777 4775 4778 4804
CONECT 4778 4772 4777 4805
CONECT 4779 4776 4780 4806 4807
CONECT 4780 4779 4781 4784 4786
CONECT 4781 4780 4782 4808 4809
CONECT 4782 4781 4787 4810 4811
CONECT 4783 4784 4787 4812 4813
CONECT 4784 4780 4783 4814 4815
CONECT 4785 4787 4788 4791
CONECT 4786 4765 4780 4792
CONECT 4787 4782 4783 4785
CONECT 4788 4766 4785
CONECT 4789 4792
CONECT 4790 4792
CONECT 4791 4771 4785
CONECT 4792 4772 4786 4789 4790
CONECT 4793 4765
CONECT 4794 4765
CONECT 4795 4767
CONECT 4796 4768
CONECT 4797 4769
CONECT 4798 4770
CONECT 4799 4773
CONECT 4800 4774
CONECT 4801 4775
CONECT 4802 4776
CONECT 4803 4776
CONECT 4804 4777
CONECT 4805 4778
CONECT 4806 4779
CONECT 4807 4779
CONECT 4808 4781
CONECT 4809 4781
CONECT 4810 4782
CONECT 4811 4782
CONECT 4812 4783
CONECT 4813 4783
CONECT 4814 4784
CONECT 4815 4784
CONECT 4816 4817 4818 4819 4820
CONECT 4817 4816
CONECT 4818 4816
CONECT 4819 4816
CONECT 4820 4816
CONECT 4821 4822 4823 4824 4825
CONECT 4822 4821
CONECT 4823 4821
CONECT 4824 4821
CONECT 4825 4821
CONECT 4826 4827 4842
CONECT 4827 4826
CONECT 4828 4842
CONECT 4829 4854 4856 4858 4860
CONECT 4830 4833 4838
CONECT 4831 4832 4834 4835
CONECT 4832 4831 4833
CONECT 4833 4830 4832 4836
CONECT 4834 4831 4837
CONECT 4835 4831
CONECT 4836 4833 4854
CONECT 4837 4834 4840
CONECT 4838 4830 4865
CONECT 4839 4842 4856
CONECT 4840 4837 4843
CONECT 4841 4865
CONECT 4842 4826 4828 4839
CONECT 4843 4840 4845
CONECT 4844 4846 4852
CONECT 4845 4843 4847
CONECT 4846 4844 4848
CONECT 4847 4845 4849
CONECT 4848 4846 4850
CONECT 4849 4847 4851
CONECT 4850 4848 4853
CONECT 4851 4849 4852
CONECT 4852 4844 4851
CONECT 4853 4850 4855
CONECT 4854 4829 4836
CONECT 4855 4853 4857
CONECT 4856 4829 4839
CONECT 4857 4855 4859
CONECT 4858 4829
CONECT 4859 4857
CONECT 4860 4829
CONECT 4861 4862 4873
CONECT 4862 4861 4863
CONECT 4863 4862 4864
CONECT 4864 4863 4874
CONECT 4865 4838 4841 4866
CONECT 4866 4865 4867
CONECT 4867 4866 4868
CONECT 4868 4867 4869
CONECT 4869 4868 4870
CONECT 4870 4869 4871
CONECT 4871 4870 4872
CONECT 4872 4871 4873
CONECT 4873 4861 4872
CONECT 4874 4864 4876
CONECT 4875 4876
CONECT 4876 4874 4875
CONECT 4877 4878 4891 4895
CONECT 4878 4877 4879 4892
CONECT 4879 4878 4880 4893
CONECT 4880 4879 4881 4894
CONECT 4881 4880 4882 4895
CONECT 4882 4881 4896
CONECT 4883 4884 4891
CONECT 4884 4883 4885
CONECT 4885 4884 4886
CONECT 4886 4885 4887
CONECT 4887 4886 4888
CONECT 4888 4887 4889
CONECT 4889 4888 4890
CONECT 4890 4889
CONECT 4891 4877 4883
CONECT 4892 4878
CONECT 4893 4879
CONECT 4894 4880
CONECT 4895 4877 4881
CONECT 4896 4882
CONECT 4897 4898 4911 4915
CONECT 4898 4897 4899 4912
CONECT 4899 4898 4900 4913
CONECT 4900 4899 4901 4914
CONECT 4901 4900 4902 4915
CONECT 4902 4901 4916
CONECT 4903 4904 4911
CONECT 4904 4903 4905
CONECT 4905 4904 4906
CONECT 4906 4905 4907
CONECT 4907 4906 4908
CONECT 4908 4907 4909
CONECT 4909 4908 4910
CONECT 4910 4909
CONECT 4911 4897 4903
CONECT 4912 4898
CONECT 4913 4899
CONECT 4914 4900
CONECT 4915 4897 4901
CONECT 4916 4902
CONECT 4917 4918 4931 4935
CONECT 4918 4917 4919 4932
CONECT 4919 4918 4920 4933
CONECT 4920 4919 4921 4934
CONECT 4921 4920 4922 4935
CONECT 4922 4921 4936
CONECT 4923 4924 4931
CONECT 4924 4923 4925
CONECT 4925 4924 4926
CONECT 4926 4925 4927
CONECT 4927 4926 4928
CONECT 4928 4927 4929
CONECT 4929 4928 4930
CONECT 4930 4929
CONECT 4931 4917 4923
CONECT 4932 4918
CONECT 4933 4919
CONECT 4934 4920
CONECT 4935 4917 4921
CONECT 4936 4922
CONECT 4937 4938 4944 4948
CONECT 4938 4937 4939 4945
CONECT 4939 4938 4940 4946
CONECT 4940 4939 4941 4947
CONECT 4941 4940 4942 4948
CONECT 4942 4941 4949
CONECT 4943 4944
CONECT 4944 4937 4943
CONECT 4945 4938
CONECT 4946 4939
CONECT 4947 4940
CONECT 4948 4937 4941
CONECT 4949 4942
CONECT 4950 4951 4958 4962
CONECT 4951 4950 4952 4959
CONECT 4952 4951 4953 4960
CONECT 4953 4952 4954 4961
CONECT 4954 4953 4955 4962
CONECT 4955 4954 4963
CONECT 4956 4957 4958
CONECT 4957 4956
CONECT 4958 4950 4956
CONECT 4959 4951
CONECT 4960 4952
CONECT 4961 4953
CONECT 4962 4950 4954
CONECT 4963 4955
CONECT 4964 4965 4978 4982
CONECT 4965 4964 4966 4979
CONECT 4966 4965 4967 4980
CONECT 4967 4966 4968 4981
CONECT 4968 4967 4969 4982
CONECT 4969 4968 4983
CONECT 4970 4971 4978
CONECT 4971 4970 4972
CONECT 4972 4971 4973
CONECT 4973 4972 4974
CONECT 4974 4973 4975
CONECT 4975 4974 4976
CONECT 4976 4975 4977
CONECT 4977 4976
CONECT 4978 4964 4970
CONECT 4979 4965
CONECT 4980 4966
CONECT 4981 4967
CONECT 4982 4964 4968
CONECT 4983 4969
CONECT 4984 4985 4988
CONECT 4985 4984 4986
CONECT 4986 4985 4987
CONECT 4987 4986
CONECT 4988 4984
CONECT 4989 4990
CONECT 4990 4989 4991
CONECT 4991 4990 4992
CONECT 4992 4991
CONECT 4993 558 1862
CONECT 4994 5005 5015 5022 5023
CONECT 4995 4996 5000 5017
CONECT 4996 4995 4997 5024
CONECT 4997 4996 4998 5025
CONECT 4998 4997 4999 5026
CONECT 4999 4998 5000 5027
CONECT 5000 4995 4999 5020
CONECT 5001 5002 5007 5021
CONECT 5002 5001 5003 5028
CONECT 5003 5002 5004 5029
CONECT 5004 5003 5006 5030
CONECT 5005 4994 5008 5031 5032
CONECT 5006 5004 5007 5033
CONECT 5007 5001 5006 5034
CONECT 5008 5005 5009 5035 5036
CONECT 5009 5008 5010 5013 5015
CONECT 5010 5009 5011 5037 5038
CONECT 5011 5010 5016 5039 5040
CONECT 5012 5013 5016 5041 5042
CONECT 5013 5009 5012 5043 5044
CONECT 5014 5016 5017 5020
CONECT 5015 4994 5009 5021
CONECT 5016 5011 5012 5014
CONECT 5017 4995 5014
CONECT 5018 5021
CONECT 5019 5021
CONECT 5020 5000 5014
CONECT 5021 5001 5015 5018 5019
CONECT 5022 4994
CONECT 5023 4994
CONECT 5024 4996
CONECT 5025 4997
CONECT 5026 4998
CONECT 5027 4999
CONECT 5028 5002
CONECT 5029 5003
CONECT 5030 5004
CONECT 5031 5005
CONECT 5032 5005
CONECT 5033 5006
CONECT 5034 5007
CONECT 5035 5008
CONECT 5036 5008
CONECT 5037 5010
CONECT 5038 5010
CONECT 5039 5011
CONECT 5040 5011
CONECT 5041 5012
CONECT 5042 5012
CONECT 5043 5013
CONECT 5044 5013
CONECT 5045 5046 5047 5048 5049
CONECT 5046 5045
CONECT 5047 5045
CONECT 5048 5045
CONECT 5049 5045
CONECT 5050 5051 5052 5053 5054
CONECT 5051 5050
CONECT 5052 5050
CONECT 5053 5050
CONECT 5054 5050
CONECT 5055 5056 5071
CONECT 5056 5055
CONECT 5057 5071
CONECT 5058 5083 5085 5087 5089
CONECT 5059 5062 5067
CONECT 5060 5061 5063 5064
CONECT 5061 5060 5062
CONECT 5062 5059 5061 5065
CONECT 5063 5060 5066
CONECT 5064 5060
CONECT 5065 5062 5083
CONECT 5066 5063 5069
CONECT 5067 5059 5094
CONECT 5068 5071 5085
CONECT 5069 5066 5072
CONECT 5070 5094
CONECT 5071 5055 5057 5068
CONECT 5072 5069 5074
CONECT 5073 5075 5081
CONECT 5074 5072 5076
CONECT 5075 5073 5077
CONECT 5076 5074 5078
CONECT 5077 5075 5079
CONECT 5078 5076 5080
CONECT 5079 5077 5082
CONECT 5080 5078 5081
CONECT 5081 5073 5080
CONECT 5082 5079 5084
CONECT 5083 5058 5065
CONECT 5084 5082 5086
CONECT 5085 5058 5068
CONECT 5086 5084 5088
CONECT 5087 5058
CONECT 5088 5086
CONECT 5089 5058
CONECT 5090 5091 5102
CONECT 5091 5090 5092
CONECT 5092 5091 5093
CONECT 5093 5092 5103
CONECT 5094 5067 5070 5095
CONECT 5095 5094 5096
CONECT 5096 5095 5097
CONECT 5097 5096 5098
CONECT 5098 5097 5099
CONECT 5099 5098 5100
CONECT 5100 5099 5101
CONECT 5101 5100 5102
CONECT 5102 5090 5101
CONECT 5103 5093 5105
CONECT 5104 5105
CONECT 5105 5103 5104
CONECT 5106 5107 5114 5118
CONECT 5107 5106 5108 5115
CONECT 5108 5107 5109 5116
CONECT 5109 5108 5110 5117
CONECT 5110 5109 5111 5118
CONECT 5111 5110 5119
CONECT 5112 5113 5114
CONECT 5113 5112
CONECT 5114 5106 5112
CONECT 5115 5107
CONECT 5116 5108
CONECT 5117 5109
CONECT 5118 5106 5110
CONECT 5119 5111
CONECT 5120 5121 5127 5131
CONECT 5121 5120 5122 5128
CONECT 5122 5121 5123 5129
CONECT 5123 5122 5124 5130
CONECT 5124 5123 5125 5131
CONECT 5125 5124 5132
CONECT 5126 5127
CONECT 5127 5120 5126
CONECT 5128 5121
CONECT 5129 5122
CONECT 5130 5123
CONECT 5131 5120 5124
CONECT 5132 5125
CONECT 5133 5134 5137
CONECT 5134 5133 5135
CONECT 5135 5134 5136
CONECT 5136 5135
CONECT 5137 5133
CONECT 5138 5139 5152 5156
CONECT 5139 5138 5140 5153
CONECT 5140 5139 5141 5154
CONECT 5141 5140 5142 5155
CONECT 5142 5141 5143 5156
CONECT 5143 5142 5157
CONECT 5144 5145 5152
CONECT 5145 5144 5146
CONECT 5146 5145 5147
CONECT 5147 5146 5148
CONECT 5148 5147 5149
CONECT 5149 5148 5150
CONECT 5150 5149 5151
CONECT 5151 5150
CONECT 5152 5138 5144
CONECT 5153 5139
CONECT 5154 5140
CONECT 5155 5141
CONECT 5156 5138 5142
CONECT 5157 5143
CONECT 5158 5159 5172 5176
CONECT 5159 5158 5160 5173
CONECT 5160 5159 5161 5174
CONECT 5161 5160 5162 5175
CONECT 5162 5161 5163 5176
CONECT 5163 5162 5177
CONECT 5164 5165 5172
CONECT 5165 5164 5166
CONECT 5166 5165 5167
CONECT 5167 5166 5168
CONECT 5168 5167 5169
CONECT 5169 5168 5170
CONECT 5170 5169 5171
CONECT 5171 5170
CONECT 5172 5158 5164
CONECT 5173 5159
CONECT 5174 5160
CONECT 5175 5161
CONECT 5176 5158 5162
CONECT 5177 5163
MASTER 441 0 22 25 4 0 0 6 5171 2 419 58
END