HEADER MEMBRANE PROTEIN 12-DEC-19 6TP4
TITLE CRYSTAL STRUCTURE OF THE OREXIN-1 RECEPTOR IN COMPLEX WITH ACT-462206
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: ACT-462206 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_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 6TP4 1 COMPND REMARK HETNAM SITE
REVDAT 3 11-MAR-20 6TP4 1 JRNL
REVDAT 2 29-JAN-20 6TP4 1 JRNL
REVDAT 1 01-JAN-20 6TP4 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. 3.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 54.9
REMARK 3 NUMBER OF REFLECTIONS : 13576
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 683
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 34.6200 - 5.1440 1.00 4745 238 0.2365 0.2556
REMARK 3 2 5.1440 - 4.0850 0.92 4292 240 0.2013 0.2475
REMARK 3 3 4.0850 - 3.5692 0.57 2657 141 0.2339 0.2819
REMARK 3 4 3.5692 - 3.2431 0.22 1032 55 0.2976 0.4495
REMARK 3 5 3.2431 - 3.0110 0.04 167 9 0.2972 0.5163
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.73
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 28:375)
REMARK 3 ORIGIN FOR THE GROUP (A): 64.2779 -4.6561 33.6373
REMARK 3 T TENSOR
REMARK 3 T11: 0.2167 T22: 0.3595
REMARK 3 T33: 0.5428 T12: 0.2580
REMARK 3 T13: -0.0546 T23: 0.0924
REMARK 3 L TENSOR
REMARK 3 L11: 0.3790 L22: 4.7504
REMARK 3 L33: 4.0157 L12: 0.0187
REMARK 3 L13: -0.4105 L23: 1.5263
REMARK 3 S TENSOR
REMARK 3 S11: 0.1608 S12: -0.1808 S13: 0.2684
REMARK 3 S21: 0.2653 S22: 0.1195 S23: -0.7752
REMARK 3 S31: -0.2375 S32: 0.4468 S33: 0.0340
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 46:377)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.3009 -26.1012 9.2131
REMARK 3 T TENSOR
REMARK 3 T11: 0.7587 T22: 0.3267
REMARK 3 T33: 0.2148 T12: 0.1676
REMARK 3 T13: 0.3161 T23: 0.1111
REMARK 3 L TENSOR
REMARK 3 L11: 2.4968 L22: 4.7443
REMARK 3 L33: 2.4350 L12: 0.1021
REMARK 3 L13: 0.0836 L23: 0.7130
REMARK 3 S TENSOR
REMARK 3 S11: -0.0883 S12: 0.3677 S13: -0.0572
REMARK 3 S21: -1.2035 S22: 0.0784 S23: -0.2716
REMARK 3 S31: 0.4111 S32: -0.0923 S33: 0.1017
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND RESID 46 THROUGH 375)
REMARK 3 SELECTION : (CHAIN B AND (RESID 46 THROUGH 187 OR
REMARK 3 RESID 198 THROUGH 243 OR RESID 284
REMARK 3 THROUGH 375))
REMARK 3 ATOM PAIRS NUMBER : 2509
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6TP4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-DEC-19.
REMARK 100 THE DEPOSITION ID IS D_1292105826.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-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) : 0.96861
REMARK 200 MONOCHROMATOR : SI (111)
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 : 13576
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.010
REMARK 200 RESOLUTION RANGE LOW (A) : 34.625
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 54.9
REMARK 200 DATA REDUNDANCY : 7.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.01
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 0.0
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 (%): 70.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRISODIUM CITRATE 50MM SODIUM
REMARK 280 CHLORIDE 50MM LITHIUM SULPHATE 15-34% PEG400, PH 4.2, 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 73.33300
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 ALA A 26
REMARK 465 SER A 27
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 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 TYR B 45
REMARK 465 PRO B 378
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: 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 -58.96 -139.46
REMARK 500 LEU A 152 9.25 57.51
REMARK 500 TYR A 224 -72.58 -131.44
REMARK 500 TYR B 224 -68.12 -134.07
REMARK 500 TRP B 376 44.99 -100.82
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 B 402
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 NRZ A 401
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: 6TP3 RELATED DB: NDB
DBREF 6TP4 A 28 380 UNP O43613 OX1R_HUMAN 28 380
DBREF 6TP4 B 28 380 UNP O43613 OX1R_HUMAN 28 380
SEQADV 6TP4 ALA A 25 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 ALA A 26 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 SER A 27 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 ALA A 46 UNP O43613 GLU 46 ENGINEERED MUTATION
SEQADV 6TP4 LEU A 85 UNP O43613 ILE 85 ENGINEERED MUTATION
SEQADV 6TP4 ALA A 95 UNP O43613 VAL 95 ENGINEERED MUTATION
SEQADV 6TP4 LEU A 162 UNP O43613 ARG 162 ENGINEERED MUTATION
SEQADV 6TP4 ALA A 194 UNP O43613 ASN 194 ENGINEERED MUTATION
SEQADV 6TP4 ALA A 198 UNP O43613 LEU 198 ENGINEERED MUTATION
SEQADV 6TP4 ALA A 211 UNP O43613 TYR 211 ENGINEERED MUTATION
SEQADV 6TP4 A UNP O43613 ALA 253 DELETION
SEQADV 6TP4 A UNP O43613 LEU 254 DELETION
SEQADV 6TP4 A UNP O43613 VAL 255 DELETION
SEQADV 6TP4 A UNP O43613 ARG 256 DELETION
SEQADV 6TP4 A UNP O43613 ASN 257 DELETION
SEQADV 6TP4 A UNP O43613 TRP 258 DELETION
SEQADV 6TP4 A UNP O43613 LYS 259 DELETION
SEQADV 6TP4 A UNP O43613 ARG 260 DELETION
SEQADV 6TP4 A UNP O43613 PRO 261 DELETION
SEQADV 6TP4 A UNP O43613 SER 262 DELETION
SEQADV 6TP4 A UNP O43613 ASP 263 DELETION
SEQADV 6TP4 A UNP O43613 GLN 264 DELETION
SEQADV 6TP4 A UNP O43613 LEU 265 DELETION
SEQADV 6TP4 A UNP O43613 GLY 266 DELETION
SEQADV 6TP4 A UNP O43613 ASP 267 DELETION
SEQADV 6TP4 A UNP O43613 LEU 268 DELETION
SEQADV 6TP4 A UNP O43613 GLU 269 DELETION
SEQADV 6TP4 A UNP O43613 GLN 270 DELETION
SEQADV 6TP4 A UNP O43613 GLY 271 DELETION
SEQADV 6TP4 A UNP O43613 LEU 272 DELETION
SEQADV 6TP4 A UNP O43613 SER 273 DELETION
SEQADV 6TP4 A UNP O43613 GLY 274 DELETION
SEQADV 6TP4 A UNP O43613 GLU 275 DELETION
SEQADV 6TP4 A UNP O43613 PRO 276 DELETION
SEQADV 6TP4 A UNP O43613 GLN 277 DELETION
SEQADV 6TP4 A UNP O43613 PRO 278 DELETION
SEQADV 6TP4 A UNP O43613 ARG 279 DELETION
SEQADV 6TP4 A UNP O43613 ALA 280 DELETION
SEQADV 6TP4 A UNP O43613 ARG 281 DELETION
SEQADV 6TP4 A UNP O43613 ALA 282 DELETION
SEQADV 6TP4 A UNP O43613 PHE 283 DELETION
SEQADV 6TP4 A UNP O43613 LEU 284 DELETION
SEQADV 6TP4 VAL A 304 UNP O43613 LEU 304 ENGINEERED MUTATION
SEQADV 6TP4 ALA A 339 UNP O43613 CYS 339 ENGINEERED MUTATION
SEQADV 6TP4 TRP A 375 UNP O43613 CYS 375 ENGINEERED MUTATION
SEQADV 6TP4 TRP A 376 UNP O43613 CYS 376 ENGINEERED MUTATION
SEQADV 6TP4 ALA A 381 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 ALA A 382 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 ALA A 383 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS A 384 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS A 385 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS A 386 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS A 387 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS A 388 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS A 389 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS A 390 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS A 391 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS A 392 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 ALA B 25 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 ALA B 26 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 SER B 27 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 ALA B 46 UNP O43613 GLU 46 ENGINEERED MUTATION
SEQADV 6TP4 LEU B 85 UNP O43613 ILE 85 ENGINEERED MUTATION
SEQADV 6TP4 ALA B 95 UNP O43613 VAL 95 ENGINEERED MUTATION
SEQADV 6TP4 LEU B 162 UNP O43613 ARG 162 ENGINEERED MUTATION
SEQADV 6TP4 ALA B 194 UNP O43613 ASN 194 ENGINEERED MUTATION
SEQADV 6TP4 ALA B 198 UNP O43613 LEU 198 ENGINEERED MUTATION
SEQADV 6TP4 ALA B 211 UNP O43613 TYR 211 ENGINEERED MUTATION
SEQADV 6TP4 B UNP O43613 ALA 253 DELETION
SEQADV 6TP4 B UNP O43613 LEU 254 DELETION
SEQADV 6TP4 B UNP O43613 VAL 255 DELETION
SEQADV 6TP4 B UNP O43613 ARG 256 DELETION
SEQADV 6TP4 B UNP O43613 ASN 257 DELETION
SEQADV 6TP4 B UNP O43613 TRP 258 DELETION
SEQADV 6TP4 B UNP O43613 LYS 259 DELETION
SEQADV 6TP4 B UNP O43613 ARG 260 DELETION
SEQADV 6TP4 B UNP O43613 PRO 261 DELETION
SEQADV 6TP4 B UNP O43613 SER 262 DELETION
SEQADV 6TP4 B UNP O43613 ASP 263 DELETION
SEQADV 6TP4 B UNP O43613 GLN 264 DELETION
SEQADV 6TP4 B UNP O43613 LEU 265 DELETION
SEQADV 6TP4 B UNP O43613 GLY 266 DELETION
SEQADV 6TP4 B UNP O43613 ASP 267 DELETION
SEQADV 6TP4 B UNP O43613 LEU 268 DELETION
SEQADV 6TP4 B UNP O43613 GLU 269 DELETION
SEQADV 6TP4 B UNP O43613 GLN 270 DELETION
SEQADV 6TP4 B UNP O43613 GLY 271 DELETION
SEQADV 6TP4 B UNP O43613 LEU 272 DELETION
SEQADV 6TP4 B UNP O43613 SER 273 DELETION
SEQADV 6TP4 B UNP O43613 GLY 274 DELETION
SEQADV 6TP4 B UNP O43613 GLU 275 DELETION
SEQADV 6TP4 B UNP O43613 PRO 276 DELETION
SEQADV 6TP4 B UNP O43613 GLN 277 DELETION
SEQADV 6TP4 B UNP O43613 PRO 278 DELETION
SEQADV 6TP4 B UNP O43613 ARG 279 DELETION
SEQADV 6TP4 B UNP O43613 ALA 280 DELETION
SEQADV 6TP4 B UNP O43613 ARG 281 DELETION
SEQADV 6TP4 B UNP O43613 ALA 282 DELETION
SEQADV 6TP4 B UNP O43613 PHE 283 DELETION
SEQADV 6TP4 B UNP O43613 LEU 284 DELETION
SEQADV 6TP4 VAL B 304 UNP O43613 LEU 304 ENGINEERED MUTATION
SEQADV 6TP4 ALA B 339 UNP O43613 CYS 339 ENGINEERED MUTATION
SEQADV 6TP4 TRP B 375 UNP O43613 CYS 375 ENGINEERED MUTATION
SEQADV 6TP4 TRP B 376 UNP O43613 CYS 376 ENGINEERED MUTATION
SEQADV 6TP4 ALA B 381 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 ALA B 382 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 ALA B 383 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS B 384 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS B 385 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS B 386 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS B 387 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS B 388 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS B 389 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS B 390 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS B 391 UNP O43613 EXPRESSION TAG
SEQADV 6TP4 HIS B 392 UNP O43613 EXPRESSION TAG
SEQRES 1 A 336 ALA ALA SER GLU ASP GLU PHE LEU ARG TYR LEU TRP ARG
SEQRES 2 A 336 ASP TYR LEU TYR PRO LYS GLN TYR ALA TRP VAL LEU ILE
SEQRES 3 A 336 ALA ALA TYR VAL ALA VAL PHE VAL VAL ALA LEU VAL GLY
SEQRES 4 A 336 ASN THR LEU VAL CYS LEU ALA VAL TRP ARG ASN HIS HIS
SEQRES 5 A 336 MET ARG THR VAL THR ASN TYR PHE LEU VAL ASN LEU SER
SEQRES 6 A 336 LEU ALA ASP VAL LEU ALA THR ALA ILE CYS LEU PRO ALA
SEQRES 7 A 336 SER LEU LEU VAL ASP ILE THR GLU SER TRP LEU PHE GLY
SEQRES 8 A 336 HIS ALA LEU CYS LYS VAL ILE PRO TYR LEU GLN ALA VAL
SEQRES 9 A 336 SER VAL SER VAL ALA VAL LEU THR LEU SER PHE ILE ALA
SEQRES 10 A 336 LEU ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU LEU PHE
SEQRES 11 A 336 LYS SER THR ALA ARG ARG ALA LEU GLY SER ILE LEU GLY
SEQRES 12 A 336 ILE TRP ALA VAL SER LEU ALA ILE MET VAL PRO GLN ALA
SEQRES 13 A 336 ALA VAL MET GLU CYS SER SER VAL LEU PRO GLU LEU ALA
SEQRES 14 A 336 ALA ARG THR ARG ALA PHE SER VAL CYS ASP GLU ARG TRP
SEQRES 15 A 336 ALA ASP ASP LEU ALA PRO LYS ILE TYR HIS SER CYS PHE
SEQRES 16 A 336 PHE ILE VAL THR TYR LEU ALA PRO LEU GLY LEU MET ALA
SEQRES 17 A 336 MET ALA TYR PHE GLN ILE PHE ARG LYS LEU TRP GLY ARG
SEQRES 18 A 336 GLN ILE PRO GLY THR THR SER ALA GLU VAL LYS GLN MET
SEQRES 19 A 336 ARG ALA ARG ARG LYS THR ALA LYS MET LEU MET VAL VAL
SEQRES 20 A 336 VAL LEU VAL PHE ALA LEU CYS TYR LEU PRO ILE SER VAL
SEQRES 21 A 336 LEU ASN VAL LEU LYS ARG VAL PHE GLY MET PHE ARG GLN
SEQRES 22 A 336 ALA SER ASP ARG GLU ALA VAL TYR ALA ALA PHE THR PHE
SEQRES 23 A 336 SER HIS TRP LEU VAL TYR ALA ASN SER ALA ALA ASN PRO
SEQRES 24 A 336 ILE ILE TYR ASN PHE LEU SER GLY LYS PHE ARG GLU GLN
SEQRES 25 A 336 PHE LYS ALA ALA PHE SER TRP TRP LEU PRO GLY LEU ALA
SEQRES 26 A 336 ALA ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 336 ALA ALA SER GLU ASP GLU PHE LEU ARG TYR LEU TRP ARG
SEQRES 2 B 336 ASP TYR LEU TYR PRO LYS GLN TYR ALA TRP VAL LEU ILE
SEQRES 3 B 336 ALA ALA TYR VAL ALA VAL PHE VAL VAL ALA LEU VAL GLY
SEQRES 4 B 336 ASN THR LEU VAL CYS LEU ALA VAL TRP ARG ASN HIS HIS
SEQRES 5 B 336 MET ARG THR VAL THR ASN TYR PHE LEU VAL ASN LEU SER
SEQRES 6 B 336 LEU ALA ASP VAL LEU ALA THR ALA ILE CYS LEU PRO ALA
SEQRES 7 B 336 SER LEU LEU VAL ASP ILE THR GLU SER TRP LEU PHE GLY
SEQRES 8 B 336 HIS ALA LEU CYS LYS VAL ILE PRO TYR LEU GLN ALA VAL
SEQRES 9 B 336 SER VAL SER VAL ALA VAL LEU THR LEU SER PHE ILE ALA
SEQRES 10 B 336 LEU ASP ARG TRP TYR ALA ILE CYS HIS PRO LEU LEU PHE
SEQRES 11 B 336 LYS SER THR ALA ARG ARG ALA LEU GLY SER ILE LEU GLY
SEQRES 12 B 336 ILE TRP ALA VAL SER LEU ALA ILE MET VAL PRO GLN ALA
SEQRES 13 B 336 ALA VAL MET GLU CYS SER SER VAL LEU PRO GLU LEU ALA
SEQRES 14 B 336 ALA ARG THR ARG ALA PHE SER VAL CYS ASP GLU ARG TRP
SEQRES 15 B 336 ALA ASP ASP LEU ALA PRO LYS ILE TYR HIS SER CYS PHE
SEQRES 16 B 336 PHE ILE VAL THR TYR LEU ALA PRO LEU GLY LEU MET ALA
SEQRES 17 B 336 MET ALA TYR PHE GLN ILE PHE ARG LYS LEU TRP GLY ARG
SEQRES 18 B 336 GLN ILE PRO GLY THR THR SER ALA GLU VAL LYS GLN MET
SEQRES 19 B 336 ARG ALA ARG ARG LYS THR ALA LYS MET LEU MET VAL VAL
SEQRES 20 B 336 VAL LEU VAL PHE ALA LEU CYS TYR LEU PRO ILE SER VAL
SEQRES 21 B 336 LEU ASN VAL LEU LYS ARG VAL PHE GLY MET PHE ARG GLN
SEQRES 22 B 336 ALA SER ASP ARG GLU ALA VAL TYR ALA ALA PHE THR PHE
SEQRES 23 B 336 SER HIS TRP LEU VAL TYR ALA ASN SER ALA ALA ASN PRO
SEQRES 24 B 336 ILE ILE TYR ASN PHE LEU SER GLY LYS PHE ARG GLU GLN
SEQRES 25 B 336 PHE LYS ALA ALA PHE SER TRP TRP LEU PRO GLY LEU ALA
SEQRES 26 B 336 ALA ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS
HET NRZ A 401 51
HET SOG A 402 20
HET SOG A 403 20
HET SOG A 404 20
HET SO4 A 405 5
HET PGW A 406 51
HET SOG B 401 20
HET SOG B 402 12
HET SO4 B 403 5
HET SO4 B 404 5
HET PGW B 405 51
HETNAM NRZ (2~{S})-~{N}-(3,5-DIMETHYLPHENYL)-1-(4-METHOXYPHENYL)
HETNAM 2 NRZ SULFONYL-PYRROLIDINE-2-CARBOXAMIDE
HETNAM SOG OCTYL 1-THIO-BETA-D-GLUCOPYRANOSIDE
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
HETSYN SOG 1-S-OCTYL-BETA-D-THIOGLUCOSIDE
HETSYN PGW 1-PALMITOYL-2-OLEOYL-SN-GLYCERO-3-[PHOSPHO-(1-
HETSYN 2 PGW GLYCEROL)]; PHOSPHATIDYLGLYCEROL
FORMUL 3 NRZ C20 H24 N2 O4 S
FORMUL 4 SOG 5(C14 H28 O5 S)
FORMUL 7 SO4 3(O4 S 2-)
FORMUL 8 PGW 2(C40 H77 O10 P)
FORMUL 14 HOH *4(H2 O)
HELIX 1 AA1 ASP A 29 TYR A 39 1 11
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 HIS A 150 1 37
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 ALA A 253 VAL A 323 1 39
HELIX 11 AB2 ASP A 332 SER A 362 1 31
HELIX 12 AB3 SER A 362 SER A 374 1 13
HELIX 13 AB4 TRP B 47 ASN B 74 1 28
HELIX 14 AB5 HIS B 75 ARG B 78 5 4
HELIX 15 AB6 THR B 79 GLU B 110 1 32
HELIX 16 AB7 PHE B 114 CYS B 149 1 36
HELIX 17 AB8 THR B 157 MET B 176 1 20
HELIX 18 AB9 MET B 176 VAL B 182 1 7
HELIX 19 AC1 GLU B 191 ARG B 195 5 5
HELIX 20 AC2 ASP B 209 TYR B 224 1 16
HELIX 21 AC3 TYR B 224 TRP B 243 1 20
HELIX 22 AC4 THR B 251 VAL B 323 1 41
HELIX 23 AC5 GLN B 329 SER B 331 5 3
HELIX 24 AC6 ASP B 332 SER B 362 1 31
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 2.03
CRYST1 61.719 146.666 73.748 90.00 108.29 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 0.016202 0.000000 0.005356 0.00000
SCALE2 0.000000 0.006818 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014281 0.00000
ATOM 1 N GLU A 28 38.186 16.930 68.545 1.00137.63 N
ANISOU 1 N GLU A 28 24539 13099 14655 2426 6781 -1849 N
ATOM 2 CA GLU A 28 39.215 17.962 68.561 1.00131.39 C
ANISOU 2 CA GLU A 28 24155 12099 13669 2473 6484 -1745 C
ATOM 3 C GLU A 28 40.405 17.555 67.697 1.00124.76 C
ANISOU 3 C GLU A 28 23238 11347 12819 2434 6017 -1615 C
ATOM 4 O GLU A 28 41.091 18.403 67.130 1.00113.59 O
ANISOU 4 O GLU A 28 21859 9893 11409 2548 5742 -1557 O
ATOM 5 CB GLU A 28 39.669 18.243 69.993 1.00126.32 C
ANISOU 5 CB GLU A 28 24305 11080 12610 2257 6574 -1700 C
ATOM 6 CG GLU A 28 38.631 18.956 70.840 1.00131.46 C
ANISOU 6 CG GLU A 28 25113 11590 13246 2323 7018 -1819 C
ATOM 7 CD GLU A 28 38.957 18.899 72.322 1.00142.27 C
ANISOU 7 CD GLU A 28 27261 12594 14201 2062 7153 -1771 C
ATOM 8 OE1 GLU A 28 39.746 18.014 72.716 1.00148.56 O
ANISOU 8 OE1 GLU A 28 28392 13295 14761 1820 6954 -1668 O
ATOM 9 OE2 GLU A 28 38.429 19.735 73.092 1.00141.09 O
ANISOU 9 OE2 GLU A 28 27406 12246 13957 2108 7445 -1835 O
ATOM 10 N ASP A 29 40.646 16.249 67.598 1.00130.28 N
ANISOU 10 N ASP A 29 23843 12155 13501 2267 5940 -1575 N
ATOM 11 CA ASP A 29 41.714 15.714 66.765 1.00130.38 C
ANISOU 11 CA ASP A 29 23744 12273 13523 2234 5520 -1467 C
ATOM 12 C ASP A 29 41.256 15.345 65.359 1.00120.86 C
ANISOU 12 C ASP A 29 21794 11416 12712 2423 5457 -1491 C
ATOM 13 O ASP A 29 41.995 14.662 64.641 1.00110.39 O
ANISOU 13 O ASP A 29 20316 10205 11421 2386 5164 -1410 O
ATOM 14 CB ASP A 29 42.358 14.500 67.435 1.00141.33 C
ANISOU 14 CB ASP A 29 25500 13561 14638 1957 5414 -1397 C
ATOM 15 CG ASP A 29 43.514 14.887 68.338 1.00149.78 C
ANISOU 15 CG ASP A 29 27277 14320 15310 1795 5154 -1318 C
ATOM 16 OD1 ASP A 29 44.125 15.956 68.095 1.00149.31 O
ANISOU 16 OD1 ASP A 29 27329 14178 15222 1883 4943 -1298 O
ATOM 17 OD2 ASP A 29 43.805 14.130 69.290 1.00152.61 O
ANISOU 17 OD2 ASP A 29 28087 14514 15384 1575 5148 -1278 O
ATOM 18 N GLU A 30 40.043 15.734 64.965 1.00126.89 N
ANISOU 18 N GLU A 30 22090 12355 13768 2626 5711 -1609 N
ATOM 19 CA GLU A 30 39.667 15.601 63.563 1.00119.51 C
ANISOU 19 CA GLU A 30 20469 11738 13200 2838 5576 -1627 C
ATOM 20 C GLU A 30 40.551 16.477 62.685 1.00114.05 C
ANISOU 20 C GLU A 30 19780 11011 12543 2988 5214 -1528 C
ATOM 21 O GLU A 30 40.981 16.057 61.603 1.00111.31 O
ANISOU 21 O GLU A 30 19099 10839 12355 3042 4949 -1458 O
ATOM 22 CB GLU A 30 38.196 15.966 63.377 1.00117.53 C
ANISOU 22 CB GLU A 30 19743 11673 13238 3044 5873 -1798 C
ATOM 23 CG GLU A 30 37.307 15.576 64.542 1.00121.06 C
ANISOU 23 CG GLU A 30 20344 12055 13598 2897 6306 -1920 C
ATOM 24 CD GLU A 30 35.942 16.224 64.456 1.00126.81 C
ANISOU 24 CD GLU A 30 20664 12931 14587 3134 6583 -2113 C
ATOM 25 OE1 GLU A 30 35.334 16.185 63.364 1.00121.65 O
ANISOU 25 OE1 GLU A 30 19374 12583 14265 3349 6480 -2191 O
ATOM 26 OE2 GLU A 30 35.488 16.794 65.473 1.00133.38 O
ANISOU 26 OE2 GLU A 30 21820 13572 15288 3117 6884 -2193 O
ATOM 27 N PHE A 31 40.863 17.691 63.149 1.00112.24 N
ANISOU 27 N PHE A 31 19954 10539 12152 3039 5205 -1517 N
ATOM 28 CA PHE A 31 41.776 18.540 62.394 1.00109.20 C
ANISOU 28 CA PHE A 31 19643 10084 11765 3132 4876 -1423 C
ATOM 29 C PHE A 31 43.154 17.905 62.303 1.00107.38 C
ANISOU 29 C PHE A 31 19653 9790 11355 2924 4549 -1309 C
ATOM 30 O PHE A 31 43.811 17.957 61.254 1.00110.68 O
ANISOU 30 O PHE A 31 19861 10298 11897 2987 4261 -1237 O
ATOM 31 CB PHE A 31 41.878 19.921 63.043 1.00115.62 C
ANISOU 31 CB PHE A 31 20914 10622 12396 3180 4947 -1438 C
ATOM 32 CG PHE A 31 42.929 20.797 62.427 1.00117.64 C
ANISOU 32 CG PHE A 31 21349 10757 12590 3207 4626 -1345 C
ATOM 33 CD1 PHE A 31 42.641 21.548 61.304 1.00133.44 C
ANISOU 33 CD1 PHE A 31 23013 12860 14828 3457 4532 -1335 C
ATOM 34 CD2 PHE A 31 44.209 20.859 62.959 1.00110.74 C
ANISOU 34 CD2 PHE A 31 20986 9669 11421 2968 4404 -1277 C
ATOM 35 CE1 PHE A 31 43.601 22.347 60.725 1.00142.92 C
ANISOU 35 CE1 PHE A 31 24401 13936 15967 3453 4264 -1250 C
ATOM 36 CE2 PHE A 31 45.176 21.655 62.379 1.00120.60 C
ANISOU 36 CE2 PHE A 31 22377 10814 12630 2961 4122 -1216 C
ATOM 37 CZ PHE A 31 44.871 22.401 61.263 1.00136.81 C
ANISOU 37 CZ PHE A 31 24111 12956 14916 3195 4074 -1197 C
ATOM 38 N LEU A 32 43.602 17.282 63.391 1.00107.57 N
ANISOU 38 N LEU A 32 20124 9659 11088 2677 4579 -1300 N
ATOM 39 CA LEU A 32 44.932 16.695 63.404 1.00107.20 C
ANISOU 39 CA LEU A 32 20335 9543 10852 2487 4230 -1217 C
ATOM 40 C LEU A 32 45.033 15.530 62.429 1.00105.32 C
ANISOU 40 C LEU A 32 19633 9566 10819 2506 4092 -1178 C
ATOM 41 O LEU A 32 46.073 15.338 61.789 1.00108.35 O
ANISOU 41 O LEU A 32 19992 9971 11206 2475 3753 -1113 O
ATOM 42 CB LEU A 32 45.278 16.251 64.823 1.00113.89 C
ANISOU 42 CB LEU A 32 21773 10168 11332 2235 4273 -1219 C
ATOM 43 CG LEU A 32 46.652 15.620 65.060 1.00119.53 C
ANISOU 43 CG LEU A 32 22821 10791 11803 2030 3873 -1156 C
ATOM 44 CD1 LEU A 32 47.768 16.561 64.626 1.00110.32 C
ANISOU 44 CD1 LEU A 32 21785 9527 10606 2032 3520 -1134 C
ATOM 45 CD2 LEU A 32 46.805 15.234 66.526 1.00131.58 C
ANISOU 45 CD2 LEU A 32 24945 12090 12961 1807 3926 -1154 C
ATOM 46 N ARG A 33 43.964 14.740 62.300 1.00101.81 N
ANISOU 46 N ARG A 33 18811 9321 10552 2548 4353 -1226 N
ATOM 47 CA ARG A 33 43.977 13.630 61.353 1.00100.48 C
ANISOU 47 CA ARG A 33 18189 9407 10582 2566 4239 -1189 C
ATOM 48 C ARG A 33 43.842 14.120 59.916 1.00 93.75 C
ANISOU 48 C ARG A 33 16808 8753 10059 2804 4088 -1160 C
ATOM 49 O ARG A 33 44.484 13.577 59.006 1.00 79.44 O
ANISOU 49 O ARG A 33 14773 7063 8348 2815 3831 -1082 O
ATOM 50 CB ARG A 33 42.857 12.643 61.687 1.00114.20 C
ANISOU 50 CB ARG A 33 19696 11293 12402 2500 4567 -1263 C
ATOM 51 CG ARG A 33 43.116 11.793 62.920 1.00123.97 C
ANISOU 51 CG ARG A 33 21441 12352 13310 2229 4663 -1256 C
ATOM 52 CD ARG A 33 41.842 11.094 63.384 1.00125.06 C
ANISOU 52 CD ARG A 33 21396 12588 13532 2150 5072 -1354 C
ATOM 53 NE ARG A 33 42.111 10.046 64.365 1.00125.25 N
ANISOU 53 NE ARG A 33 21870 12459 13260 1878 5135 -1323 N
ATOM 54 CZ ARG A 33 42.317 8.771 64.052 1.00133.50 C
ANISOU 54 CZ ARG A 33 22809 13615 14298 1760 5050 -1277 C
ATOM 55 NH1 ARG A 33 42.282 8.385 62.784 1.00135.27 N
ANISOU 55 NH1 ARG A 33 22479 14114 14804 1887 4912 -1259 N
ATOM 56 NH2 ARG A 33 42.558 7.880 65.005 1.00139.70 N
ANISOU 56 NH2 ARG A 33 24068 14224 14788 1518 5094 -1242 N
ATOM 57 N TYR A 34 43.008 15.140 59.695 1.00104.54 N
ANISOU 57 N TYR A 34 17986 10146 11588 3000 4233 -1221 N
ATOM 58 CA TYR A 34 42.846 15.667 58.345 1.00 99.28 C
ANISOU 58 CA TYR A 34 16869 9646 11208 3228 4061 -1189 C
ATOM 59 C TYR A 34 44.118 16.337 57.844 1.00104.79 C
ANISOU 59 C TYR A 34 17801 10196 11817 3218 3740 -1082 C
ATOM 60 O TYR A 34 44.391 16.309 56.640 1.00103.63 O
ANISOU 60 O TYR A 34 17325 10187 11863 3318 3521 -1010 O
ATOM 61 CB TYR A 34 41.660 16.631 58.294 1.00 93.79 C
ANISOU 61 CB TYR A 34 15969 8990 10676 3450 4264 -1296 C
ATOM 62 CG TYR A 34 40.352 15.962 58.649 1.00107.67 C
ANISOU 62 CG TYR A 34 17400 10934 12577 3464 4571 -1437 C
ATOM 63 CD1 TYR A 34 40.120 14.634 58.307 1.00111.27 C
ANISOU 63 CD1 TYR A 34 17514 11616 13149 3365 4577 -1442 C
ATOM 64 CD2 TYR A 34 39.359 16.645 59.344 1.00129.04 C
ANISOU 64 CD2 TYR A 34 20146 13587 15298 3563 4865 -1575 C
ATOM 65 CE1 TYR A 34 38.930 14.007 58.637 1.00129.06 C
ANISOU 65 CE1 TYR A 34 19467 14042 15528 3343 4868 -1587 C
ATOM 66 CE2 TYR A 34 38.166 16.027 59.681 1.00143.48 C
ANISOU 66 CE2 TYR A 34 21657 15593 17264 3557 5159 -1729 C
ATOM 67 CZ TYR A 34 37.956 14.709 59.326 1.00145.29 C
ANISOU 67 CZ TYR A 34 21546 16051 17606 3436 5160 -1737 C
ATOM 68 OH TYR A 34 36.767 14.099 59.662 1.00153.69 O
ANISOU 68 OH TYR A 34 22297 17296 18802 3404 5462 -1902 O
ATOM 69 N LEU A 35 44.916 16.928 58.741 1.00107.91 N
ANISOU 69 N LEU A 35 18764 10313 11924 3078 3700 -1076 N
ATOM 70 CA LEU A 35 46.186 17.497 58.297 1.00103.22 C
ANISOU 70 CA LEU A 35 18386 9582 11252 3020 3389 -1002 C
ATOM 71 C LEU A 35 47.105 16.413 57.750 1.00 95.37 C
ANISOU 71 C LEU A 35 17260 8688 10287 2909 3125 -937 C
ATOM 72 O LEU A 35 47.858 16.649 56.796 1.00 91.30 O
ANISOU 72 O LEU A 35 16617 8192 9880 2934 2878 -872 O
ATOM 73 CB LEU A 35 46.871 18.239 59.443 1.00100.54 C
ANISOU 73 CB LEU A 35 18678 8934 10589 2850 3371 -1032 C
ATOM 74 CG LEU A 35 48.269 18.775 59.114 1.00 92.00 C
ANISOU 74 CG LEU A 35 17841 7700 9416 2726 3038 -991 C
ATOM 75 CD1 LEU A 35 48.208 20.000 58.200 1.00 80.02 C
ANISOU 75 CD1 LEU A 35 16209 6151 8043 2885 3009 -959 C
ATOM 76 CD2 LEU A 35 49.040 19.081 60.384 1.00104.31 C
ANISOU 76 CD2 LEU A 35 20008 8993 10632 2488 2957 -1037 C
ATOM 77 N TRP A 36 47.049 15.217 58.334 1.00 93.56 N
ANISOU 77 N TRP A 36 17073 8514 9960 2783 3181 -955 N
ATOM 78 CA TRP A 36 47.817 14.098 57.802 1.00 93.69 C
ANISOU 78 CA TRP A 36 16946 8638 10012 2707 2942 -898 C
ATOM 79 C TRP A 36 47.228 13.620 56.485 1.00 94.89 C
ANISOU 79 C TRP A 36 16475 9080 10498 2879 2943 -844 C
ATOM 80 O TRP A 36 47.951 13.397 55.507 1.00 96.20 O
ANISOU 80 O TRP A 36 16438 9322 10793 2905 2690 -766 O
ATOM 81 CB TRP A 36 47.849 12.958 58.819 1.00 91.34 C
ANISOU 81 CB TRP A 36 16914 8305 9486 2527 3006 -929 C
ATOM 82 CG TRP A 36 48.223 11.634 58.225 1.00 85.30 C
ANISOU 82 CG TRP A 36 15911 7703 8795 2499 2848 -879 C
ATOM 83 CD1 TRP A 36 47.376 10.620 57.875 1.00 85.60 C
ANISOU 83 CD1 TRP A 36 15581 7964 8979 2537 3030 -871 C
ATOM 84 CD2 TRP A 36 49.543 11.179 57.913 1.00 85.34 C
ANISOU 84 CD2 TRP A 36 16028 7656 8741 2422 2466 -838 C
ATOM 85 NE1 TRP A 36 48.088 9.561 57.365 1.00 89.45 N
ANISOU 85 NE1 TRP A 36 15975 8534 9478 2498 2799 -814 N
ATOM 86 CE2 TRP A 36 49.421 9.879 57.377 1.00 90.68 C
ANISOU 86 CE2 TRP A 36 16393 8537 9524 2429 2433 -785 C
ATOM 87 CE3 TRP A 36 50.817 11.744 58.035 1.00 83.51 C
ANISOU 87 CE3 TRP A 36 16090 7240 8401 2322 2124 -845 C
ATOM 88 CZ2 TRP A 36 50.523 9.138 56.963 1.00 90.04 C
ANISOU 88 CZ2 TRP A 36 16177 8560 9475 2302 2014 -677 C
ATOM 89 CZ3 TRP A 36 51.908 11.008 57.624 1.00 85.13 C
ANISOU 89 CZ3 TRP A 36 16114 7568 8662 2186 1709 -751 C
ATOM 90 CH2 TRP A 36 51.755 9.718 57.094 1.00 88.43 C
ANISOU 90 CH2 TRP A 36 16170 8227 9200 2192 1658 -665 C
ATOM 91 N ARG A 37 45.905 13.474 56.442 1.00 93.35 N
ANISOU 91 N ARG A 37 15962 9050 10456 2986 3213 -893 N
ATOM 92 CA ARG A 37 45.258 12.931 55.254 1.00 92.63 C
ANISOU 92 CA ARG A 37 15271 9252 10673 3121 3186 -861 C
ATOM 93 C ARG A 37 45.469 13.834 54.039 1.00104.08 C
ANISOU 93 C ARG A 37 16490 10745 12311 3282 2976 -792 C
ATOM 94 O ARG A 37 45.675 13.340 52.922 1.00 98.97 O
ANISOU 94 O ARG A 37 15489 10272 11843 3325 2786 -711 O
ATOM 95 CB ARG A 37 43.768 12.730 55.541 1.00 98.09 C
ANISOU 95 CB ARG A 37 15680 10096 11493 3184 3497 -973 C
ATOM 96 CG ARG A 37 42.872 12.517 54.331 1.00101.74 C
ANISOU 96 CG ARG A 37 15511 10854 12292 3347 3452 -987 C
ATOM 97 CD ARG A 37 41.420 12.318 54.774 1.00111.22 C
ANISOU 97 CD ARG A 37 16453 12194 13611 3384 3761 -1149 C
ATOM 98 NE ARG A 37 41.216 11.043 55.467 1.00122.38 N
ANISOU 98 NE ARG A 37 17910 13660 14929 3179 3957 -1187 N
ATOM 99 CZ ARG A 37 40.148 10.749 56.207 1.00125.98 C
ANISOU 99 CZ ARG A 37 18292 14174 15399 3119 4284 -1331 C
ATOM 100 NH1 ARG A 37 39.174 11.640 56.370 1.00128.09 N
ANISOU 100 NH1 ARG A 37 18412 14468 15786 3276 4446 -1465 N
ATOM 101 NH2 ARG A 37 40.055 9.562 56.793 1.00120.87 N
ANISOU 101 NH2 ARG A 37 17736 13548 14639 2898 4455 -1348 N
ATOM 102 N ASP A 38 45.476 15.160 54.245 1.00115.30 N
ANISOU 102 N ASP A 38 18151 11988 13668 3355 3003 -815 N
ATOM 103 CA ASP A 38 45.415 16.130 53.153 1.00105.00 C
ANISOU 103 CA ASP A 38 16664 10708 12522 3518 2863 -766 C
ATOM 104 C ASP A 38 46.737 16.817 52.836 1.00 87.47 C
ANISOU 104 C ASP A 38 14749 8292 10193 3435 2640 -686 C
ATOM 105 O ASP A 38 46.837 17.468 51.788 1.00 67.97 O
ANISOU 105 O ASP A 38 12139 5844 7843 3534 2506 -626 O
ATOM 106 CB ASP A 38 44.372 17.214 53.470 1.00 98.44 C
ANISOU 106 CB ASP A 38 15865 9819 11717 3688 3059 -858 C
ATOM 107 CG ASP A 38 42.995 16.642 53.760 1.00108.80 C
ANISOU 107 CG ASP A 38 16835 11329 13176 3771 3291 -978 C
ATOM 108 OD1 ASP A 38 42.560 15.720 53.039 1.00117.58 O
ANISOU 108 OD1 ASP A 38 17497 12693 14487 3792 3229 -978 O
ATOM 109 OD2 ASP A 38 42.340 17.117 54.712 1.00112.28 O
ANISOU 109 OD2 ASP A 38 17456 11670 13534 3802 3540 -1085 O
ATOM 110 N TYR A 39 47.743 16.705 53.702 1.00 92.37 N
ANISOU 110 N TYR A 39 15795 8714 10587 3240 2586 -700 N
ATOM 111 CA TYR A 39 48.994 17.422 53.482 1.00 91.39 C
ANISOU 111 CA TYR A 39 15962 8387 10373 3127 2379 -666 C
ATOM 112 C TYR A 39 50.209 16.571 53.829 1.00 85.35 C
ANISOU 112 C TYR A 39 15372 7555 9503 2915 2172 -665 C
ATOM 113 O TYR A 39 51.065 16.331 52.970 1.00 83.98 O
ANISOU 113 O TYR A 39 15052 7413 9445 2868 1951 -603 O
ATOM 114 CB TYR A 39 49.022 18.722 54.293 1.00 97.32 C
ANISOU 114 CB TYR A 39 17173 8876 10929 3095 2483 -728 C
ATOM 115 CG TYR A 39 50.399 19.359 54.367 1.00104.72 C
ANISOU 115 CG TYR A 39 18483 9574 11732 2894 2277 -731 C
ATOM 116 CD1 TYR A 39 50.945 20.014 53.269 1.00105.78 C
ANISOU 116 CD1 TYR A 39 18535 9674 11982 2906 2144 -671 C
ATOM 117 CD2 TYR A 39 51.152 19.304 55.535 1.00108.67 C
ANISOU 117 CD2 TYR A 39 19425 9879 11988 2666 2205 -807 C
ATOM 118 CE1 TYR A 39 52.205 20.597 53.331 1.00103.37 C
ANISOU 118 CE1 TYR A 39 18552 9144 11580 2683 1975 -697 C
ATOM 119 CE2 TYR A 39 52.415 19.883 55.606 1.00104.95 C
ANISOU 119 CE2 TYR A 39 19260 9197 11420 2448 1985 -839 C
ATOM 120 CZ TYR A 39 52.936 20.528 54.501 1.00104.70 C
ANISOU 120 CZ TYR A 39 19113 9133 11535 2449 1886 -790 C
ATOM 121 OH TYR A 39 54.188 21.106 54.568 1.00111.03 O
ANISOU 121 OH TYR A 39 20199 9722 12265 2193 1688 -843 O
ATOM 122 N LEU A 40 50.293 16.115 55.082 1.00 78.00 N
ANISOU 122 N LEU A 40 14766 6521 8350 2784 2228 -740 N
ATOM 123 CA LEU A 40 51.490 15.416 55.542 1.00 76.59 C
ANISOU 123 CA LEU A 40 14831 6239 8030 2578 1970 -763 C
ATOM 124 C LEU A 40 51.733 14.154 54.727 1.00 79.69 C
ANISOU 124 C LEU A 40 14845 6837 8599 2616 1826 -692 C
ATOM 125 O LEU A 40 52.827 13.945 54.178 1.00 91.23 O
ANISOU 125 O LEU A 40 16151 8363 10148 2466 1505 -624 O
ATOM 126 CB LEU A 40 51.345 15.086 57.031 1.00 75.83 C
ANISOU 126 CB LEU A 40 15158 6019 7636 2442 2058 -846 C
ATOM 127 CG LEU A 40 51.669 16.213 58.019 1.00 83.99 C
ANISOU 127 CG LEU A 40 16698 6788 8427 2310 2061 -917 C
ATOM 128 CD1 LEU A 40 50.936 16.023 59.341 1.00 87.18 C
ANISOU 128 CD1 LEU A 40 17415 7123 8586 2261 2299 -967 C
ATOM 129 CD2 LEU A 40 53.175 16.274 58.247 1.00 87.87 C
ANISOU 129 CD2 LEU A 40 17474 7111 8800 2078 1668 -961 C
ATOM 130 N TYR A 41 50.725 13.293 54.652 1.00 75.28 N
ANISOU 130 N TYR A 41 14003 6488 8114 2723 2020 -671 N
ATOM 131 CA TYR A 41 50.857 12.083 53.850 1.00 71.95 C
ANISOU 131 CA TYR A 41 13160 6315 7861 2726 1880 -578 C
ATOM 132 C TYR A 41 51.087 12.389 52.380 1.00 82.66 C
ANISOU 132 C TYR A 41 14134 7788 9486 2844 1755 -483 C
ATOM 133 O TYR A 41 51.959 11.747 51.768 1.00 90.78 O
ANISOU 133 O TYR A 41 14937 8944 10610 2723 1481 -393 O
ATOM 134 CB TYR A 41 49.630 11.190 54.042 1.00 73.20 C
ANISOU 134 CB TYR A 41 13135 6632 8046 2826 2170 -608 C
ATOM 135 CG TYR A 41 49.709 9.996 53.151 1.00 83.65 C
ANISOU 135 CG TYR A 41 14012 8225 9548 2811 2023 -502 C
ATOM 136 CD1 TYR A 41 50.687 9.025 53.339 1.00 77.41 C
ANISOU 136 CD1 TYR A 41 13255 7487 8672 2605 1731 -435 C
ATOM 137 CD2 TYR A 41 48.845 9.860 52.082 1.00101.85 C
ANISOU 137 CD2 TYR A 41 15847 10743 12108 2993 2131 -466 C
ATOM 138 CE1 TYR A 41 50.778 7.933 52.503 1.00 77.66 C
ANISOU 138 CE1 TYR A 41 12902 7748 8858 2599 1603 -339 C
ATOM 139 CE2 TYR A 41 48.927 8.773 51.241 1.00103.42 C
ANISOU 139 CE2 TYR A 41 15683 11157 12455 2994 2008 -380 C
ATOM 140 CZ TYR A 41 49.891 7.813 51.454 1.00 94.43 C
ANISOU 140 CZ TYR A 41 14603 10056 11221 2782 1752 -310 C
ATOM 141 OH TYR A 41 49.960 6.733 50.609 1.00107.01 O
ANISOU 141 OH TYR A 41 15839 11865 12955 2770 1629 -218 O
ATOM 142 N PRO A 42 50.313 13.269 51.731 1.00 81.10 N
ANISOU 142 N PRO A 42 13749 7643 9422 2998 1891 -468 N
ATOM 143 CA PRO A 42 50.552 13.484 50.297 1.00 71.80 C
ANISOU 143 CA PRO A 42 12229 6590 8462 3063 1739 -365 C
ATOM 144 C PRO A 42 51.962 13.965 50.001 1.00 77.26 C
ANISOU 144 C PRO A 42 13127 7095 9136 2938 1519 -341 C
ATOM 145 O PRO A 42 52.600 13.474 49.055 1.00 82.53 O
ANISOU 145 O PRO A 42 13547 7861 9949 2912 1346 -255 O
ATOM 146 CB PRO A 42 49.500 14.536 49.913 1.00 68.17 C
ANISOU 146 CB PRO A 42 11663 6164 8074 3216 1886 -380 C
ATOM 147 CG PRO A 42 48.476 14.497 50.997 1.00 72.56 C
ANISOU 147 CG PRO A 42 12320 6714 8534 3261 2138 -480 C
ATOM 148 CD PRO A 42 49.176 14.057 52.244 1.00 80.64 C
ANISOU 148 CD PRO A 42 13757 7562 9323 3095 2150 -538 C
ATOM 149 N LYS A 43 52.497 14.844 50.852 1.00 80.01 N
ANISOU 149 N LYS A 43 13928 7169 9305 2828 1521 -426 N
ATOM 150 CA LYS A 43 53.844 15.356 50.643 1.00 76.54 C
ANISOU 150 CA LYS A 43 13640 6583 8861 2617 1294 -425 C
ATOM 151 C LYS A 43 54.876 14.263 50.867 1.00 78.47 C
ANISOU 151 C LYS A 43 13719 6980 9115 2368 998 -399 C
ATOM 152 O LYS A 43 55.807 14.107 50.069 1.00 88.69 O
ANISOU 152 O LYS A 43 14790 8352 10557 2246 801 -346 O
ATOM 153 CB LYS A 43 54.105 16.542 51.573 1.00 80.31 C
ANISOU 153 CB LYS A 43 14631 6751 9132 2515 1352 -537 C
ATOM 154 CG LYS A 43 53.835 17.917 50.963 1.00 84.49 C
ANISOU 154 CG LYS A 43 15256 7159 9689 2598 1480 -522 C
ATOM 155 CD LYS A 43 54.663 19.001 51.650 1.00 91.24 C
ANISOU 155 CD LYS A 43 16597 7701 10369 2381 1431 -621 C
ATOM 156 CE LYS A 43 54.672 20.288 50.834 1.00103.41 C
ANISOU 156 CE LYS A 43 18214 9131 11947 2407 1511 -584 C
ATOM 157 NZ LYS A 43 55.548 21.344 51.428 1.00112.20 N
ANISOU 157 NZ LYS A 43 19790 9941 12899 2152 1464 -684 N
ATOM 158 N GLN A 44 54.712 13.483 51.940 1.00 78.09 N
ANISOU 158 N GLN A 44 13794 6970 8906 2304 975 -440 N
ATOM 159 CA GLN A 44 55.654 12.409 52.225 1.00 77.00 C
ANISOU 159 CA GLN A 44 13545 6961 8752 2111 670 -421 C
ATOM 160 C GLN A 44 55.647 11.350 51.128 1.00 76.50 C
ANISOU 160 C GLN A 44 12996 7164 8906 2184 598 -304 C
ATOM 161 O GLN A 44 56.697 10.782 50.802 1.00 72.75 O
ANISOU 161 O GLN A 44 12328 6792 8521 2045 324 -273 O
ATOM 162 CB GLN A 44 55.317 11.798 53.588 1.00 87.68 C
ANISOU 162 CB GLN A 44 15207 8261 9846 2064 695 -483 C
ATOM 163 CG GLN A 44 56.163 10.605 53.993 1.00101.42 C
ANISOU 163 CG GLN A 44 16899 10111 11524 1914 374 -465 C
ATOM 164 CD GLN A 44 55.813 10.105 55.381 1.00 92.64 C
ANISOU 164 CD GLN A 44 16206 8889 10103 1867 414 -528 C
ATOM 165 OE1 GLN A 44 55.430 10.891 56.256 1.00 93.04 O
ANISOU 165 OE1 GLN A 44 16675 8725 9952 1855 579 -619 O
ATOM 166 NE2 GLN A 44 55.934 8.790 55.591 1.00 70.14 N
ANISOU 166 NE2 GLN A 44 13291 6164 7194 1843 277 -482 N
ATOM 167 N TYR A 45 54.486 11.100 50.519 1.00 84.11 N
ANISOU 167 N TYR A 45 13746 8244 9969 2405 837 -251 N
ATOM 168 CA TYR A 45 54.390 10.085 49.473 1.00 88.61 C
ANISOU 168 CA TYR A 45 13883 9057 10727 2475 778 -144 C
ATOM 169 C TYR A 45 54.992 10.575 48.158 1.00 82.07 C
ANISOU 169 C TYR A 45 12833 8251 10101 2487 689 -76 C
ATOM 170 O TYR A 45 55.717 9.826 47.487 1.00 70.33 O
ANISOU 170 O TYR A 45 11078 6907 8737 2409 505 -9 O
ATOM 171 CB TYR A 45 52.923 9.676 49.306 1.00 96.53 C
ANISOU 171 CB TYR A 45 14732 10177 11768 2689 1051 -136 C
ATOM 172 CG TYR A 45 52.562 8.889 48.057 1.00 95.60 C
ANISOU 172 CG TYR A 45 14177 10290 11858 2805 1036 -37 C
ATOM 173 CD1 TYR A 45 52.748 7.512 47.989 1.00 88.93 C
ANISOU 173 CD1 TYR A 45 13141 9621 11027 2722 921 18 C
ATOM 174 CD2 TYR A 45 51.985 9.522 46.966 1.00106.05 C
ANISOU 174 CD2 TYR A 45 15295 11660 13338 2969 1120 -1 C
ATOM 175 CE1 TYR A 45 52.395 6.796 46.852 1.00 89.24 C
ANISOU 175 CE1 TYR A 45 12809 9857 11241 2819 911 102 C
ATOM 176 CE2 TYR A 45 51.631 8.818 45.831 1.00104.70 C
ANISOU 176 CE2 TYR A 45 14710 11743 13329 2963 1049 79 C
ATOM 177 CZ TYR A 45 51.835 7.455 45.775 1.00 91.89 C
ANISOU 177 CZ TYR A 45 12922 10266 11727 2912 965 128 C
ATOM 178 OH TYR A 45 51.477 6.765 44.633 1.00 87.79 O
ANISOU 178 OH TYR A 45 12028 9977 11352 2867 890 192 O
ATOM 179 N ALA A 46 54.739 11.835 47.788 1.00 83.17 N
ANISOU 179 N ALA A 46 13117 8226 10259 2581 826 -97 N
ATOM 180 CA ALA A 46 55.431 12.384 46.625 1.00 70.51 C
ANISOU 180 CA ALA A 46 11404 6586 8802 2548 756 -43 C
ATOM 181 C ALA A 46 56.935 12.385 46.856 1.00 74.42 C
ANISOU 181 C ALA A 46 11928 7041 9306 2248 517 -81 C
ATOM 182 O ALA A 46 57.720 12.147 45.928 1.00 90.43 O
ANISOU 182 O ALA A 46 13719 9149 11491 2159 408 -30 O
ATOM 183 CB ALA A 46 54.936 13.798 46.331 1.00 57.29 C
ANISOU 183 CB ALA A 46 9982 4687 7096 2692 944 -69 C
ATOM 184 N TRP A 47 57.351 12.620 48.101 1.00 67.53 N
ANISOU 184 N TRP A 47 11338 6051 8270 2089 429 -183 N
ATOM 185 CA TRP A 47 58.768 12.644 48.431 1.00 68.59 C
ANISOU 185 CA TRP A 47 11486 6156 8420 1807 165 -253 C
ATOM 186 C TRP A 47 59.406 11.270 48.295 1.00 73.56 C
ANISOU 186 C TRP A 47 11785 7019 9146 1747 -74 -213 C
ATOM 187 O TRP A 47 60.473 11.134 47.687 1.00 73.82 O
ANISOU 187 O TRP A 47 11583 7122 9345 1603 -236 -219 O
ATOM 188 CB TRP A 47 58.967 13.198 49.833 1.00 91.87 C
ANISOU 188 CB TRP A 47 14847 8916 11145 1675 102 -379 C
ATOM 189 CG TRP A 47 60.384 13.472 50.109 1.00110.51 C
ANISOU 189 CG TRP A 47 17224 11225 13539 1385 -171 -479 C
ATOM 190 CD1 TRP A 47 61.058 14.644 49.943 1.00118.42 C
ANISOU 190 CD1 TRP A 47 18376 12046 14573 1198 -162 -561 C
ATOM 191 CD2 TRP A 47 61.309 12.551 50.691 1.00114.39 C
ANISOU 191 CD2 TRP A 47 17591 11842 14029 1244 -509 -530 C
ATOM 192 NE1 TRP A 47 62.366 14.493 50.343 1.00119.75 N
ANISOU 192 NE1 TRP A 47 18459 12246 14794 929 -474 -672 N
ATOM 193 CE2 TRP A 47 62.541 13.217 50.814 1.00114.36 C
ANISOU 193 CE2 TRP A 47 17605 11755 14092 975 -709 -655 C
ATOM 194 CE3 TRP A 47 61.216 11.217 51.110 1.00119.93 C
ANISOU 194 CE3 TRP A 47 18180 12712 14677 1325 -667 -488 C
ATOM 195 CZ2 TRP A 47 63.675 12.596 51.337 1.00112.12 C
ANISOU 195 CZ2 TRP A 47 17185 11571 13845 810 -1089 -750 C
ATOM 196 CZ3 TRP A 47 62.339 10.602 51.625 1.00121.00 C
ANISOU 196 CZ3 TRP A 47 18235 12920 14819 1179 -1041 -565 C
ATOM 197 CH2 TRP A 47 63.553 11.291 51.734 1.00115.58 C
ANISOU 197 CH2 TRP A 47 17524 12169 14222 937 -1262 -699 C
ATOM 198 N VAL A 48 58.757 10.235 48.833 1.00 79.64 N
ANISOU 198 N VAL A 48 12539 7904 9817 1857 -78 -178 N
ATOM 199 CA VAL A 48 59.308 8.888 48.704 1.00 79.87 C
ANISOU 199 CA VAL A 48 12301 8133 9914 1828 -300 -133 C
ATOM 200 C VAL A 48 59.362 8.494 47.237 1.00 76.98 C
ANISOU 200 C VAL A 48 11541 7924 9782 1906 -252 -27 C
ATOM 201 O VAL A 48 60.335 7.882 46.774 1.00 45.61 O
ANISOU 201 O VAL A 48 7311 4069 5948 1819 -449 -16 O
ATOM 202 CB VAL A 48 58.480 7.886 49.531 1.00 68.36 C
ANISOU 202 CB VAL A 48 10969 6731 8275 1925 -259 -113 C
ATOM 203 CG1 VAL A 48 58.887 6.447 49.212 1.00 46.54 C
ANISOU 203 CG1 VAL A 48 7940 4163 5580 1937 -448 -45 C
ATOM 204 CG2 VAL A 48 58.630 8.179 51.014 1.00 74.31 C
ANISOU 204 CG2 VAL A 48 12157 7311 8769 1822 -345 -222 C
ATOM 205 N LEU A 49 58.338 8.879 46.473 1.00 83.98 N
ANISOU 205 N LEU A 49 12384 8807 10717 2080 3 41 N
ATOM 206 CA LEU A 49 58.303 8.529 45.061 1.00 56.36 C
ANISOU 206 CA LEU A 49 8568 5437 7409 2167 48 144 C
ATOM 207 C LEU A 49 59.479 9.160 44.327 1.00 48.64 C
ANISOU 207 C LEU A 49 7508 4398 6577 2006 -25 124 C
ATOM 208 O LEU A 49 60.257 8.462 43.660 1.00 49.68 O
ANISOU 208 O LEU A 49 7364 4659 6853 1939 -145 157 O
ATOM 209 CB LEU A 49 56.977 8.981 44.455 1.00 52.93 C
ANISOU 209 CB LEU A 49 8149 4982 6981 2401 300 198 C
ATOM 210 CG LEU A 49 56.840 8.825 42.943 1.00 65.51 C
ANISOU 210 CG LEU A 49 9492 6662 8736 2513 347 301 C
ATOM 211 CD1 LEU A 49 57.032 7.378 42.540 1.00 88.23 C
ANISOU 211 CD1 LEU A 49 12072 9760 11693 2506 227 370 C
ATOM 212 CD2 LEU A 49 55.473 9.335 42.483 1.00 64.55 C
ANISOU 212 CD2 LEU A 49 9359 6567 8599 2674 525 315 C
ATOM 213 N ILE A 50 59.644 10.482 44.462 1.00 48.79 N
ANISOU 213 N ILE A 50 7777 4206 6554 1927 65 58 N
ATOM 214 CA ILE A 50 60.712 11.161 43.734 1.00 50.46 C
ANISOU 214 CA ILE A 50 7938 4334 6899 1738 52 25 C
ATOM 215 C ILE A 50 62.078 10.680 44.205 1.00 58.45 C
ANISOU 215 C ILE A 50 8783 5429 7996 1494 -210 -71 C
ATOM 216 O ILE A 50 63.009 10.535 43.403 1.00 58.89 O
ANISOU 216 O ILE A 50 8591 5549 8237 1365 -252 -80 O
ATOM 217 CB ILE A 50 60.599 12.685 43.900 1.00 55.02 C
ANISOU 217 CB ILE A 50 8881 4640 7386 1682 207 -38 C
ATOM 218 CG1 ILE A 50 59.272 13.207 43.371 1.00 60.67 C
ANISOU 218 CG1 ILE A 50 9752 5268 8034 1969 443 45 C
ATOM 219 CG2 ILE A 50 61.729 13.366 43.136 1.00 61.35 C
ANISOU 219 CG2 ILE A 50 9647 5340 8321 1442 227 -84 C
ATOM 220 CD1 ILE A 50 59.191 13.155 41.883 1.00 73.11 C
ANISOU 220 CD1 ILE A 50 11168 6875 9734 2068 536 151 C
ATOM 221 N ALA A 51 62.224 10.404 45.505 1.00 61.99 N
ANISOU 221 N ALA A 51 9365 5877 8310 1439 -394 -153 N
ATOM 222 CA ALA A 51 63.531 9.988 45.997 1.00 63.55 C
ANISOU 222 CA ALA A 51 9408 6150 8587 1236 -695 -264 C
ATOM 223 C ALA A 51 63.905 8.601 45.501 1.00 65.38 C
ANISOU 223 C ALA A 51 9269 6619 8955 1311 -843 -201 C
ATOM 224 O ALA A 51 65.044 8.380 45.072 1.00 69.79 O
ANISOU 224 O ALA A 51 9541 7266 9711 1174 -984 -264 O
ATOM 225 CB ALA A 51 63.549 10.026 47.527 1.00 64.72 C
ANISOU 225 CB ALA A 51 9856 6216 8518 1183 -883 -365 C
ATOM 226 N ALA A 52 62.952 7.667 45.489 1.00 58.70 N
ANISOU 226 N ALA A 52 8410 5873 8019 1525 -789 -85 N
ATOM 227 CA ALA A 52 63.258 6.342 44.967 1.00 50.84 C
ANISOU 227 CA ALA A 52 7103 5080 7135 1603 -911 -18 C
ATOM 228 C ALA A 52 63.556 6.398 43.476 1.00 59.83 C
ANISOU 228 C ALA A 52 7956 6281 8495 1600 -768 46 C
ATOM 229 O ALA A 52 64.530 5.792 43.003 1.00 50.84 O
ANISOU 229 O ALA A 52 6524 5263 7531 1538 -900 21 O
ATOM 230 CB ALA A 52 62.099 5.384 45.244 1.00 43.47 C
ANISOU 230 CB ALA A 52 6252 4217 6046 1800 -845 84 C
ATOM 231 N TYR A 53 62.762 7.173 42.728 1.00 72.49 N
ANISOU 231 N TYR A 53 9664 7789 10090 1671 -498 117 N
ATOM 232 CA TYR A 53 62.987 7.261 41.292 1.00 65.34 C
ANISOU 232 CA TYR A 53 8567 6907 9352 1674 -350 185 C
ATOM 233 C TYR A 53 64.337 7.913 40.983 1.00 70.48 C
ANISOU 233 C TYR A 53 9111 7498 10171 1419 -374 71 C
ATOM 234 O TYR A 53 65.080 7.422 40.122 1.00 84.78 O
ANISOU 234 O TYR A 53 10642 9408 12163 1363 -374 78 O
ATOM 235 CB TYR A 53 61.812 8.024 40.660 1.00 63.42 C
ANISOU 235 CB TYR A 53 8524 6545 9029 1830 -94 274 C
ATOM 236 CG TYR A 53 60.758 7.113 40.022 1.00 68.98 C
ANISOU 236 CG TYR A 53 9111 7383 9714 2068 -30 405 C
ATOM 237 CD1 TYR A 53 59.952 6.300 40.819 1.00 67.68 C
ANISOU 237 CD1 TYR A 53 8960 7321 9436 2187 -90 423 C
ATOM 238 CD2 TYR A 53 60.552 7.076 38.649 1.00 75.14 C
ANISOU 238 CD2 TYR A 53 9797 8176 10577 2156 94 500 C
ATOM 239 CE1 TYR A 53 58.982 5.464 40.264 1.00 57.04 C
ANISOU 239 CE1 TYR A 53 7489 6103 8080 2360 -28 519 C
ATOM 240 CE2 TYR A 53 59.580 6.242 38.085 1.00 64.42 C
ANISOU 240 CE2 TYR A 53 8317 6971 9188 2283 105 577 C
ATOM 241 CZ TYR A 53 58.805 5.441 38.898 1.00 55.39 C
ANISOU 241 CZ TYR A 53 7131 5966 7950 2283 31 554 C
ATOM 242 OH TYR A 53 57.856 4.614 38.347 1.00 52.43 O
ANISOU 242 OH TYR A 53 6617 5764 7540 2213 23 555 O
ATOM 243 N VAL A 54 64.724 8.949 41.744 1.00 52.82 N
ANISOU 243 N VAL A 54 7079 5108 7884 1243 -402 -52 N
ATOM 244 CA VAL A 54 65.989 9.647 41.485 1.00 61.40 C
ANISOU 244 CA VAL A 54 8061 6129 9139 956 -404 -188 C
ATOM 245 C VAL A 54 67.190 8.797 41.890 1.00 70.60 C
ANISOU 245 C VAL A 54 8879 7478 10469 840 -694 -306 C
ATOM 246 O VAL A 54 68.206 8.740 41.176 1.00 64.32 O
ANISOU 246 O VAL A 54 7788 6745 9904 683 -670 -379 O
ATOM 247 CB VAL A 54 66.023 11.010 42.188 1.00 67.87 C
ANISOU 247 CB VAL A 54 9225 6719 9846 788 -352 -295 C
ATOM 248 CG1 VAL A 54 67.459 11.495 42.262 1.00 53.78 C
ANISOU 248 CG1 VAL A 54 7277 4914 8244 447 -440 -483 C
ATOM 249 CG2 VAL A 54 65.170 12.011 41.430 1.00 77.61 C
ANISOU 249 CG2 VAL A 54 10761 7745 10984 872 -35 -201 C
ATOM 250 N ALA A 55 67.126 8.181 43.074 1.00 78.64 N
ANISOU 250 N ALA A 55 9945 8566 11368 914 -972 -344 N
ATOM 251 CA ALA A 55 68.233 7.345 43.514 1.00 67.81 C
ANISOU 251 CA ALA A 55 8271 7361 10134 856 -1299 -460 C
ATOM 252 C ALA A 55 68.464 6.217 42.528 1.00 68.10 C
ANISOU 252 C ALA A 55 7956 7581 10338 985 -1279 -376 C
ATOM 253 O ALA A 55 69.612 5.929 42.166 1.00 71.84 O
ANISOU 253 O ALA A 55 8074 8167 11054 876 -1382 -487 O
ATOM 254 CB ALA A 55 67.959 6.794 44.911 1.00 51.43 C
ANISOU 254 CB ALA A 55 6403 5297 7840 962 -1593 -485 C
ATOM 255 N VAL A 56 67.383 5.573 42.071 1.00 68.31 N
ANISOU 255 N VAL A 56 8067 7641 10248 1214 -1139 -194 N
ATOM 256 CA VAL A 56 67.526 4.517 41.075 1.00 61.14 C
ANISOU 256 CA VAL A 56 6872 6885 9473 1336 -1098 -105 C
ATOM 257 C VAL A 56 68.094 5.085 39.773 1.00 62.29 C
ANISOU 257 C VAL A 56 6835 7001 9833 1195 -847 -119 C
ATOM 258 O VAL A 56 68.911 4.438 39.108 1.00 61.60 O
ANISOU 258 O VAL A 56 6421 7035 9947 1178 -865 -151 O
ATOM 259 CB VAL A 56 66.181 3.803 40.860 1.00 52.65 C
ANISOU 259 CB VAL A 56 5949 5836 8219 1577 -991 79 C
ATOM 260 CG1 VAL A 56 66.144 3.141 39.490 1.00 55.44 C
ANISOU 260 CG1 VAL A 56 6085 6280 8698 1666 -835 187 C
ATOM 261 CG2 VAL A 56 65.948 2.780 41.970 1.00 47.88 C
ANISOU 261 CG2 VAL A 56 5434 5304 7453 1702 -1249 83 C
ATOM 262 N PHE A 57 67.711 6.317 39.410 1.00 61.64 N
ANISOU 262 N PHE A 57 6986 6736 9700 1090 -598 -107 N
ATOM 263 CA PHE A 57 68.226 6.915 38.178 1.00 59.18 C
ANISOU 263 CA PHE A 57 6587 6350 9549 939 -328 -119 C
ATOM 264 C PHE A 57 69.741 7.052 38.240 1.00 71.85 C
ANISOU 264 C PHE A 57 7872 8016 11412 673 -412 -322 C
ATOM 265 O PHE A 57 70.466 6.582 37.347 1.00 78.77 O
ANISOU 265 O PHE A 57 8447 8985 12497 623 -318 -348 O
ATOM 266 CB PHE A 57 67.587 8.296 37.981 1.00 51.42 C
ANISOU 266 CB PHE A 57 5989 5121 8429 872 -85 -88 C
ATOM 267 CG PHE A 57 68.095 9.057 36.782 1.00 57.76 C
ANISOU 267 CG PHE A 57 6815 5786 9346 691 215 -105 C
ATOM 268 CD1 PHE A 57 69.162 9.933 36.906 1.00 62.78 C
ANISOU 268 CD1 PHE A 57 7412 6325 10118 359 278 -285 C
ATOM 269 CD2 PHE A 57 67.510 8.899 35.536 1.00 70.55 C
ANISOU 269 CD2 PHE A 57 8520 7360 10925 835 438 49 C
ATOM 270 CE1 PHE A 57 69.635 10.640 35.818 1.00 71.87 C
ANISOU 270 CE1 PHE A 57 8628 7324 11357 159 595 -309 C
ATOM 271 CE2 PHE A 57 67.977 9.614 34.439 1.00 69.68 C
ANISOU 271 CE2 PHE A 57 8506 7086 10882 662 731 35 C
ATOM 272 CZ PHE A 57 69.044 10.482 34.584 1.00 69.57 C
ANISOU 272 CZ PHE A 57 8469 6965 10998 315 829 -143 C
ATOM 273 N VAL A 58 70.235 7.630 39.334 1.00 70.87 N
ANISOU 273 N VAL A 58 7791 7853 11284 507 -605 -482 N
ATOM 274 CA VAL A 58 71.669 7.869 39.470 1.00 69.21 C
ANISOU 274 CA VAL A 58 7252 7706 11337 229 -706 -712 C
ATOM 275 C VAL A 58 72.432 6.552 39.576 1.00 63.05 C
ANISOU 275 C VAL A 58 6035 7178 10743 347 -979 -775 C
ATOM 276 O VAL A 58 73.443 6.339 38.888 1.00 63.32 O
ANISOU 276 O VAL A 58 5684 7314 11060 222 -907 -889 O
ATOM 277 CB VAL A 58 71.943 8.770 40.686 1.00 67.23 C
ANISOU 277 CB VAL A 58 7181 7351 11012 35 -893 -873 C
ATOM 278 CG1 VAL A 58 73.432 8.838 40.955 1.00 69.70 C
ANISOU 278 CG1 VAL A 58 7087 7779 11618 -231 -1082 -1138 C
ATOM 279 CG2 VAL A 58 71.368 10.163 40.461 1.00 69.18 C
ANISOU 279 CG2 VAL A 58 7851 7325 11108 -108 -587 -837 C
ATOM 280 N VAL A 59 71.951 5.639 40.426 1.00 54.01 N
ANISOU 280 N VAL A 59 4963 6124 9434 596 -1277 -705 N
ATOM 281 CA VAL A 59 72.685 4.402 40.652 1.00 54.67 C
ANISOU 281 CA VAL A 59 4692 6418 9661 735 -1580 -771 C
ATOM 282 C VAL A 59 72.721 3.547 39.395 1.00 90.65 C
ANISOU 282 C VAL A 59 9013 11077 14353 866 -1379 -664 C
ATOM 283 O VAL A 59 73.773 3.004 39.037 1.00 94.10 O
ANISOU 283 O VAL A 59 9036 11660 15058 845 -1454 -789 O
ATOM 284 CB VAL A 59 72.038 3.627 41.817 1.00 53.51 C
ANISOU 284 CB VAL A 59 4789 6294 9248 974 -1904 -697 C
ATOM 285 CG1 VAL A 59 72.674 2.255 41.974 1.00 54.04 C
ANISOU 285 CG1 VAL A 59 4566 6548 9416 1172 -2210 -734 C
ATOM 286 CG2 VAL A 59 72.093 4.424 43.099 1.00 55.57 C
ANISOU 286 CG2 VAL A 59 5301 6446 9365 843 -2121 -819 C
ATOM 287 N ALA A 60 71.619 3.505 38.640 1.00 86.78 N
ANISOU 287 N ALA A 60 8772 10504 13697 988 -1101 -451 N
ATOM 288 CA ALA A 60 71.600 2.694 37.428 1.00 87.20 C
ANISOU 288 CA ALA A 60 8652 10633 13846 1111 -914 -344 C
ATOM 289 C ALA A 60 72.456 3.293 36.324 1.00 85.89 C
ANISOU 289 C ALA A 60 8267 10435 13933 881 -611 -439 C
ATOM 290 O ALA A 60 73.219 2.573 35.664 1.00 92.74 O
ANISOU 290 O ALA A 60 8797 11426 15015 906 -573 -492 O
ATOM 291 CB ALA A 60 70.162 2.514 36.945 1.00 88.06 C
ANISOU 291 CB ALA A 60 9092 10664 13705 1297 -733 -108 C
ATOM 292 N LEU A 61 72.426 4.617 36.173 1.00 79.90 N
ANISOU 292 N LEU A 61 7700 9500 13157 643 -391 -485 N
ATOM 293 CA LEU A 61 73.235 5.228 35.130 1.00 82.33 C
ANISOU 293 CA LEU A 61 7855 9744 13682 388 -60 -583 C
ATOM 294 C LEU A 61 74.720 5.034 35.410 1.00 92.24 C
ANISOU 294 C LEU A 61 8610 11160 15278 205 -202 -846 C
ATOM 295 O LEU A 61 75.465 4.504 34.566 1.00 95.28 O
ANISOU 295 O LEU A 61 8660 11644 15898 179 -53 -909 O
ATOM 296 CB LEU A 61 72.870 6.706 35.013 1.00 84.76 C
ANISOU 296 CB LEU A 61 8540 9799 13866 169 190 -582 C
ATOM 297 CG LEU A 61 73.577 7.534 33.950 1.00100.48 C
ANISOU 297 CG LEU A 61 10510 11651 16017 -136 591 -673 C
ATOM 298 CD1 LEU A 61 73.310 6.960 32.580 1.00 96.45 C
ANISOU 298 CD1 LEU A 61 10024 11124 15497 -5 867 -521 C
ATOM 299 CD2 LEU A 61 73.117 8.974 34.041 1.00109.47 C
ANISOU 299 CD2 LEU A 61 12106 12512 16977 -316 781 -662 C
ATOM 300 N VAL A 62 75.144 5.348 36.635 1.00 94.86 N
ANISOU 300 N VAL A 62 8869 11535 15637 111 -523 -1008 N
ATOM 301 CA VAL A 62 76.559 5.245 36.972 1.00 92.03 C
ANISOU 301 CA VAL A 62 8007 11339 15619 -64 -706 -1291 C
ATOM 302 C VAL A 62 77.019 3.791 36.899 1.00 86.88 C
ANISOU 302 C VAL A 62 6972 10921 15118 211 -937 -1304 C
ATOM 303 O VAL A 62 78.066 3.482 36.313 1.00 76.38 O
ANISOU 303 O VAL A 62 5181 9721 14117 126 -848 -1468 O
ATOM 304 CB VAL A 62 76.820 5.867 38.353 1.00 83.94 C
ANISOU 304 CB VAL A 62 7044 10300 14551 -197 -1055 -1455 C
ATOM 305 CG1 VAL A 62 78.256 5.624 38.782 1.00 69.71 C
ANISOU 305 CG1 VAL A 62 4680 8700 13107 -329 -1335 -1762 C
ATOM 306 CG2 VAL A 62 76.473 7.349 38.327 1.00 66.03 C
ANISOU 306 CG2 VAL A 62 5154 7781 12155 -492 -784 -1462 C
ATOM 307 N GLY A 63 76.252 2.876 37.497 1.00 88.23 N
ANISOU 307 N GLY A 63 7334 11139 15050 543 -1219 -1141 N
ATOM 308 CA GLY A 63 76.698 1.498 37.569 1.00 60.38 C
ANISOU 308 CA GLY A 63 3503 7807 11633 818 -1481 -1159 C
ATOM 309 C GLY A 63 76.756 0.813 36.217 1.00 69.03 C
ANISOU 309 C GLY A 63 4522 8941 12765 896 -1139 -1043 C
ATOM 310 O GLY A 63 77.696 0.066 35.936 1.00 79.80 O
ANISOU 310 O GLY A 63 5708 10451 14162 923 -1149 -1107 O
ATOM 311 N ASN A 64 75.769 1.054 35.348 1.00 71.10 N
ANISOU 311 N ASN A 64 5045 9059 12910 922 -808 -845 N
ATOM 312 CA ASN A 64 75.841 0.414 34.039 1.00 78.00 C
ANISOU 312 CA ASN A 64 5896 9956 13784 983 -496 -741 C
ATOM 313 C ASN A 64 76.962 1.006 33.186 1.00 70.54 C
ANISOU 313 C ASN A 64 4597 9011 13194 703 -177 -939 C
ATOM 314 O ASN A 64 77.654 0.270 32.456 1.00 74.09 O
ANISOU 314 O ASN A 64 4939 9562 13649 730 -57 -954 O
ATOM 315 CB ASN A 64 74.493 0.552 33.328 1.00 90.66 C
ANISOU 315 CB ASN A 64 7877 11396 15174 1089 -249 -489 C
ATOM 316 CG ASN A 64 73.414 -0.324 33.942 1.00 97.59 C
ANISOU 316 CG ASN A 64 9120 12316 15644 1346 -491 -291 C
ATOM 317 OD1 ASN A 64 73.504 -1.555 33.932 1.00105.14 O
ANISOU 317 OD1 ASN A 64 10178 13421 16351 1478 -594 -222 O
ATOM 318 ND2 ASN A 64 72.383 0.315 34.486 1.00 90.41 N
ANISOU 318 ND2 ASN A 64 8473 11276 14603 1384 -534 -199 N
ATOM 319 N THR A 65 77.210 2.317 33.307 1.00 63.37 N
ANISOU 319 N THR A 65 3690 7984 12405 382 -21 -1071 N
ATOM 320 CA THR A 65 78.358 2.871 32.598 1.00 68.76 C
ANISOU 320 CA THR A 65 4032 8671 13421 62 297 -1294 C
ATOM 321 C THR A 65 79.654 2.249 33.095 1.00 80.52 C
ANISOU 321 C THR A 65 5080 10400 15115 72 20 -1520 C
ATOM 322 O THR A 65 80.561 1.965 32.304 1.00 84.52 O
ANISOU 322 O THR A 65 5393 10977 15744 -10 243 -1609 O
ATOM 323 CB THR A 65 78.391 4.387 32.757 1.00 79.55 C
ANISOU 323 CB THR A 65 5620 9847 14757 -313 491 -1382 C
ATOM 324 OG1 THR A 65 78.162 4.718 34.130 1.00 91.90 O
ANISOU 324 OG1 THR A 65 7287 11429 16202 -296 83 -1428 O
ATOM 325 CG2 THR A 65 77.302 5.020 31.909 1.00 76.03 C
ANISOU 325 CG2 THR A 65 5749 9135 14004 -328 858 -1138 C
ATOM 326 N LEU A 66 79.751 2.018 34.409 1.00 90.22 N
ANISOU 326 N LEU A 66 6277 11735 16268 189 -468 -1582 N
ATOM 327 CA LEU A 66 80.925 1.348 34.960 1.00 89.04 C
ANISOU 327 CA LEU A 66 5866 11792 16171 256 -764 -1738 C
ATOM 328 C LEU A 66 81.034 -0.093 34.490 1.00 83.54 C
ANISOU 328 C LEU A 66 5244 11211 15288 563 -787 -1579 C
ATOM 329 O LEU A 66 82.145 -0.591 34.319 1.00101.12 O
ANISOU 329 O LEU A 66 7190 13579 17650 571 -809 -1707 O
ATOM 330 CB LEU A 66 80.934 1.409 36.484 1.00 82.59 C
ANISOU 330 CB LEU A 66 5083 11027 15269 326 -1277 -1819 C
ATOM 331 CG LEU A 66 81.077 2.818 37.038 1.00 75.17 C
ANISOU 331 CG LEU A 66 4032 9999 14531 -23 -1306 -2031 C
ATOM 332 CD1 LEU A 66 81.430 2.745 38.506 1.00 77.35 C
ANISOU 332 CD1 LEU A 66 4302 10359 14729 45 -1846 -2156 C
ATOM 333 CD2 LEU A 66 82.141 3.561 36.245 1.00 79.22 C
ANISOU 333 CD2 LEU A 66 4208 10525 15365 -397 -936 -2255 C
ATOM 334 N VAL A 67 79.910 -0.772 34.259 1.00 66.77 N
ANISOU 334 N VAL A 67 3489 9025 12856 801 -769 -1309 N
ATOM 335 CA VAL A 67 79.978 -2.133 33.731 1.00 75.72 C
ANISOU 335 CA VAL A 67 4724 10254 13792 1045 -751 -1159 C
ATOM 336 C VAL A 67 80.653 -2.103 32.372 1.00 74.14 C
ANISOU 336 C VAL A 67 4319 10058 13793 919 -350 -1223 C
ATOM 337 O VAL A 67 81.590 -2.868 32.089 1.00 73.53 O
ANISOU 337 O VAL A 67 4034 10114 13790 995 -359 -1292 O
ATOM 338 CB VAL A 67 78.573 -2.756 33.645 1.00 89.38 C
ANISOU 338 CB VAL A 67 6914 11909 15139 1259 -753 -869 C
ATOM 339 CG1 VAL A 67 78.578 -3.946 32.687 1.00 91.85 C
ANISOU 339 CG1 VAL A 67 7331 12285 15282 1424 -594 -727 C
ATOM 340 CG2 VAL A 67 78.086 -3.166 35.022 1.00 96.56 C
ANISOU 340 CG2 VAL A 67 8045 12840 15806 1416 -1146 -804 C
ATOM 341 N CYS A 68 80.215 -1.172 31.527 1.00 72.71 N
ANISOU 341 N CYS A 68 4199 9711 13715 717 27 -1210 N
ATOM 342 CA CYS A 68 80.807 -1.060 30.200 1.00 77.21 C
ANISOU 342 CA CYS A 68 4640 10241 14454 565 462 -1270 C
ATOM 343 C CYS A 68 82.283 -0.688 30.295 1.00 84.27 C
ANISOU 343 C CYS A 68 5091 11246 15683 344 501 -1563 C
ATOM 344 O CYS A 68 83.126 -1.294 29.625 1.00 86.89 O
ANISOU 344 O CYS A 68 5237 11669 16109 372 638 -1629 O
ATOM 345 CB CYS A 68 80.011 -0.080 29.346 1.00 85.32 C
ANISOU 345 CB CYS A 68 5889 11027 15503 381 882 -1186 C
ATOM 346 SG CYS A 68 78.334 -0.725 29.042 1.00100.24 S
ANISOU 346 SG CYS A 68 8284 12811 16991 690 839 -834 S
ATOM 347 N LEU A 69 82.617 0.338 31.083 1.00 92.52 N
ANISOU 347 N LEU A 69 5960 12280 16915 107 399 -1753 N
ATOM 348 CA LEU A 69 84.013 0.774 31.157 1.00100.93 C
ANISOU 348 CA LEU A 69 6605 13450 18294 -139 449 -2049 C
ATOM 349 C LEU A 69 84.919 -0.294 31.768 1.00104.27 C
ANISOU 349 C LEU A 69 6767 14107 18743 102 70 -2127 C
ATOM 350 O LEU A 69 86.081 -0.420 31.366 1.00103.51 O
ANISOU 350 O LEU A 69 6327 14118 18883 11 194 -2312 O
ATOM 351 CB LEU A 69 84.105 2.053 31.980 1.00102.63 C
ANISOU 351 CB LEU A 69 6731 13607 18656 -444 367 -2230 C
ATOM 352 CG LEU A 69 83.367 3.211 31.328 1.00101.67 C
ANISOU 352 CG LEU A 69 6859 13229 18541 -738 809 -2181 C
ATOM 353 CD1 LEU A 69 83.817 4.525 31.935 1.00111.91 C
ANISOU 353 CD1 LEU A 69 8029 14468 20026 -1142 829 -2420 C
ATOM 354 CD2 LEU A 69 83.633 3.166 29.831 1.00 89.59 C
ANISOU 354 CD2 LEU A 69 5383 11601 17057 -850 1350 -2150 C
ATOM 355 N ALA A 70 84.411 -1.078 32.724 1.00107.92 N
ANISOU 355 N ALA A 70 7406 14635 18963 408 -367 -1988 N
ATOM 356 CA ALA A 70 85.189 -2.170 33.299 1.00106.14 C
ANISOU 356 CA ALA A 70 7009 14594 18725 662 -709 -2030 C
ATOM 357 C ALA A 70 85.479 -3.218 32.238 1.00101.70 C
ANISOU 357 C ALA A 70 6426 14084 18131 832 -485 -1934 C
ATOM 358 O ALA A 70 86.611 -3.701 32.111 1.00102.88 O
ANISOU 358 O ALA A 70 6238 14373 18477 878 -512 -2085 O
ATOM 359 CB ALA A 70 84.451 -2.781 34.491 1.00101.61 C
ANISOU 359 CB ALA A 70 6739 14024 17844 930 -1157 -1874 C
ATOM 360 N VAL A 71 84.449 -3.610 31.483 1.00 98.40 N
ANISOU 360 N VAL A 71 6370 13556 17459 940 -277 -1686 N
ATOM 361 CA VAL A 71 84.672 -4.597 30.435 1.00 99.58 C
ANISOU 361 CA VAL A 71 6535 13744 17557 1092 -60 -1595 C
ATOM 362 C VAL A 71 85.622 -4.034 29.390 1.00112.09 C
ANISOU 362 C VAL A 71 7802 15320 19467 837 352 -1795 C
ATOM 363 O VAL A 71 86.385 -4.782 28.767 1.00127.40 O
ANISOU 363 O VAL A 71 9555 17349 21500 935 467 -1843 O
ATOM 364 CB VAL A 71 83.342 -5.043 29.801 1.00 95.78 C
ANISOU 364 CB VAL A 71 6521 13141 16732 1229 81 -1307 C
ATOM 365 CG1 VAL A 71 83.571 -5.537 28.376 1.00 85.17 C
ANISOU 365 CG1 VAL A 71 5180 11772 15407 1245 456 -1270 C
ATOM 366 CG2 VAL A 71 82.703 -6.133 30.639 1.00110.60 C
ANISOU 366 CG2 VAL A 71 8679 15072 18271 1535 -280 -1111 C
ATOM 367 N TRP A 72 85.591 -2.714 29.173 1.00108.25 N
ANISOU 367 N TRP A 72 7267 14711 19152 497 608 -1916 N
ATOM 368 CA TRP A 72 86.517 -2.110 28.221 1.00126.58 C
ANISOU 368 CA TRP A 72 9325 17000 21769 204 1043 -2120 C
ATOM 369 C TRP A 72 87.954 -2.129 28.736 1.00139.78 C
ANISOU 369 C TRP A 72 10488 18866 23756 139 885 -2406 C
ATOM 370 O TRP A 72 88.891 -2.291 27.946 1.00139.92 O
ANISOU 370 O TRP A 72 10243 18934 23989 54 1163 -2551 O
ATOM 371 CB TRP A 72 86.133 -0.645 27.970 1.00130.05 C
ANISOU 371 CB TRP A 72 9885 17236 22290 -173 1364 -2182 C
ATOM 372 CG TRP A 72 87.099 0.075 27.059 1.00137.97 C
ANISOU 372 CG TRP A 72 10676 18178 23570 -527 1844 -2405 C
ATOM 373 CD1 TRP A 72 87.355 -0.228 25.753 1.00140.46 C
ANISOU 373 CD1 TRP A 72 11054 18411 23903 -564 2272 -2384 C
ATOM 374 CD2 TRP A 72 88.031 1.112 27.416 1.00147.23 C
ANISOU 374 CD2 TRP A 72 11533 19377 25032 -886 1928 -2697 C
ATOM 375 NE1 TRP A 72 88.326 0.603 25.251 1.00148.93 N
ANISOU 375 NE1 TRP A 72 11908 19435 25245 -932 2651 -2636 N
ATOM 376 CE2 TRP A 72 88.768 1.427 26.253 1.00152.95 C
ANISOU 376 CE2 TRP A 72 12171 20017 25926 -1140 2448 -2834 C
ATOM 377 CE3 TRP A 72 88.295 1.821 28.593 1.00148.71 C
ANISOU 377 CE3 TRP A 72 11531 19638 25334 -1031 1622 -2860 C
ATOM 378 CZ2 TRP A 72 89.752 2.421 26.233 1.00154.95 C
ANISOU 378 CZ2 TRP A 72 12156 20264 26456 -1540 2683 -3127 C
ATOM 379 CZ3 TRP A 72 89.273 2.810 28.570 1.00149.76 C
ANISOU 379 CZ3 TRP A 72 11385 19771 25745 -1429 1838 -3150 C
ATOM 380 CH2 TRP A 72 89.988 3.099 27.398 1.00151.39 C
ANISOU 380 CH2 TRP A 72 11510 19898 26113 -1682 2370 -3280 C
ATOM 381 N ARG A 73 88.145 -1.984 30.052 1.00147.40 N
ANISOU 381 N ARG A 73 11314 19937 24753 184 437 -2496 N
ATOM 382 CA ARG A 73 89.486 -1.819 30.610 1.00153.50 C
ANISOU 382 CA ARG A 73 11595 20884 25843 87 268 -2794 C
ATOM 383 C ARG A 73 90.201 -3.141 30.868 1.00154.58 C
ANISOU 383 C ARG A 73 11520 21212 26003 436 -19 -2803 C
ATOM 384 O ARG A 73 91.406 -3.255 30.617 1.00164.55 O
ANISOU 384 O ARG A 73 12350 22605 27566 380 59 -3031 O
ATOM 385 CB ARG A 73 89.399 -1.028 31.914 1.00156.60 C
ANISOU 385 CB ARG A 73 11952 21293 26257 -31 -97 -2901 C
ATOM 386 CG ARG A 73 89.382 0.478 31.760 1.00161.06 C
ANISOU 386 CG ARG A 73 12494 21727 26975 -482 195 -3053 C
ATOM 387 CD ARG A 73 89.464 1.109 33.132 1.00168.54 C
ANISOU 387 CD ARG A 73 13362 22724 27953 -569 -229 -3184 C
ATOM 388 NE ARG A 73 88.232 0.801 33.860 1.00169.21 N
ANISOU 388 NE ARG A 73 13858 22731 27704 -324 -544 -2939 N
ATOM 389 CZ ARG A 73 87.976 1.145 35.119 1.00166.33 C
ANISOU 389 CZ ARG A 73 13567 22374 27256 -310 -963 -2976 C
ATOM 390 NH1 ARG A 73 88.868 1.834 35.817 1.00169.01 N
ANISOU 390 NH1 ARG A 73 13597 22801 27816 -533 -1145 -3248 N
ATOM 391 NH2 ARG A 73 86.815 0.807 35.676 1.00158.05 N
ANISOU 391 NH2 ARG A 73 12919 21240 25894 -81 -1195 -2744 N
ATOM 392 N ASN A 74 89.484 -4.140 31.373 1.00147.59 N
ANISOU 392 N ASN A 74 10937 20335 24805 789 -336 -2566 N
ATOM 393 CA ASN A 74 90.055 -5.442 31.703 1.00149.11 C
ANISOU 393 CA ASN A 74 11007 20674 24975 1139 -622 -2547 C
ATOM 394 C ASN A 74 89.815 -6.396 30.536 1.00146.89 C
ANISOU 394 C ASN A 74 10886 20362 24562 1315 -324 -2365 C
ATOM 395 O ASN A 74 88.675 -6.793 30.273 1.00144.78 O
ANISOU 395 O ASN A 74 11065 19982 23961 1438 -273 -2093 O
ATOM 396 CB ASN A 74 89.467 -5.974 33.010 1.00146.39 C
ANISOU 396 CB ASN A 74 10936 20333 24354 1394 -1130 -2409 C
ATOM 397 CG ASN A 74 90.084 -7.291 33.439 1.00148.58 C
ANISOU 397 CG ASN A 74 11114 20732 24608 1747 -1436 -2401 C
ATOM 398 OD1 ASN A 74 90.663 -8.020 32.635 1.00151.77 O
ANISOU 398 OD1 ASN A 74 11344 21203 25120 1868 -1250 -2413 O
ATOM 399 ND2 ASN A 74 89.979 -7.590 34.728 1.00148.59 N
ANISOU 399 ND2 ASN A 74 11238 20747 24472 1915 -1906 -2390 N
ATOM 400 N HIS A 75 90.891 -6.758 29.835 1.00149.74 N
ANISOU 400 N HIS A 75 10879 20826 25188 1323 -125 -2526 N
ATOM 401 CA HIS A 75 90.772 -7.652 28.688 1.00151.53 C
ANISOU 401 CA HIS A 75 11234 21026 25313 1484 171 -2383 C
ATOM 402 C HIS A 75 90.365 -9.063 29.084 1.00154.99 C
ANISOU 402 C HIS A 75 11927 21500 25461 1897 -130 -2156 C
ATOM 403 O HIS A 75 89.786 -9.773 28.256 1.00156.05 O
ANISOU 403 O HIS A 75 12350 21568 25376 2036 74 -1954 O
ATOM 404 CB HIS A 75 92.069 -7.689 27.878 1.00159.91 C
ANISOU 404 CB HIS A 75 11825 22188 26747 1391 467 -2631 C
ATOM 405 CG HIS A 75 92.319 -6.441 27.093 1.00163.33 C
ANISOU 405 CG HIS A 75 12129 22525 27404 962 929 -2803 C
ATOM 406 ND1 HIS A 75 93.308 -5.536 27.414 1.00170.02 N
ANISOU 406 ND1 HIS A 75 12536 23451 28613 680 960 -3117 N
ATOM 407 CD2 HIS A 75 91.691 -5.942 26.003 1.00160.56 C
ANISOU 407 CD2 HIS A 75 12070 21984 26953 756 1388 -2707 C
ATOM 408 CE1 HIS A 75 93.285 -4.538 26.548 1.00169.69 C
ANISOU 408 CE1 HIS A 75 12534 23264 28677 306 1445 -3200 C
ATOM 409 NE2 HIS A 75 92.311 -4.759 25.683 1.00164.68 N
ANISOU 409 NE2 HIS A 75 12352 22456 27765 351 1709 -2952 N
ATOM 410 N HIS A 76 90.636 -9.491 30.320 1.00159.72 N
ANISOU 410 N HIS A 76 12458 22185 26042 2089 -601 -2188 N
ATOM 411 CA HIS A 76 90.239 -10.844 30.688 1.00162.82 C
ANISOU 411 CA HIS A 76 13138 22573 26153 2458 -848 -1969 C
ATOM 412 C HIS A 76 88.735 -10.937 30.857 1.00166.69 C
ANISOU 412 C HIS A 76 14204 22911 26220 2487 -872 -1669 C
ATOM 413 O HIS A 76 88.193 -12.048 30.890 1.00165.73 O
ANISOU 413 O HIS A 76 14402 22746 25824 2742 -955 -1448 O
ATOM 414 CB HIS A 76 90.925 -11.296 31.980 1.00160.86 C
ANISOU 414 CB HIS A 76 12707 22424 25988 2656 -1345 -2090 C
ATOM 415 CG HIS A 76 92.414 -11.375 31.879 1.00162.45 C
ANISOU 415 CG HIS A 76 12326 22795 26603 2685 -1372 -2387 C
ATOM 416 ND1 HIS A 76 93.065 -12.485 31.386 1.00164.89 N
ANISOU 416 ND1 HIS A 76 12475 23176 26997 2954 -1324 -2391 N
ATOM 417 CD2 HIS A 76 93.381 -10.486 32.209 1.00166.31 C
ANISOU 417 CD2 HIS A 76 12339 23398 27453 2479 -1438 -2700 C
ATOM 418 CE1 HIS A 76 94.369 -12.275 31.414 1.00171.83 C
ANISOU 418 CE1 HIS A 76 12791 24215 28281 2923 -1360 -2698 C
ATOM 419 NE2 HIS A 76 94.587 -11.070 31.910 1.00172.79 N
ANISOU 419 NE2 HIS A 76 12709 24368 28576 2627 -1429 -2892 N
ATOM 420 N MET A 77 88.051 -9.803 30.986 1.00168.01 N
ANISOU 420 N MET A 77 14506 22991 26339 2229 -799 -1665 N
ATOM 421 CA MET A 77 86.609 -9.839 31.139 1.00155.83 C
ANISOU 421 CA MET A 77 13480 21313 24414 2255 -814 -1400 C
ATOM 422 C MET A 77 85.882 -9.878 29.798 1.00150.84 C
ANISOU 422 C MET A 77 13087 20590 23636 2203 -401 -1245 C
ATOM 423 O MET A 77 84.648 -9.940 29.789 1.00156.96 O
ANISOU 423 O MET A 77 14284 21260 24093 2230 -387 -1029 O
ATOM 424 CB MET A 77 86.131 -8.636 31.967 1.00147.22 C
ANISOU 424 CB MET A 77 12450 20160 23327 2038 -955 -1462 C
ATOM 425 CG MET A 77 86.304 -8.813 33.476 1.00138.59 C
ANISOU 425 CG MET A 77 11366 19105 22187 2154 -1436 -1516 C
ATOM 426 SD MET A 77 86.469 -7.264 34.386 1.00137.48 S
ANISOU 426 SD MET A 77 11043 18953 22239 1865 -1606 -1742 S
ATOM 427 CE MET A 77 84.872 -6.520 34.103 1.00138.36 C
ANISOU 427 CE MET A 77 11603 18884 22085 1720 -1391 -1527 C
ATOM 428 N ARG A 78 86.597 -9.830 28.666 1.00138.95 N
ANISOU 428 N ARG A 78 11333 19113 22349 2125 -64 -1363 N
ATOM 429 CA ARG A 78 85.911 -9.720 27.378 1.00119.71 C
ANISOU 429 CA ARG A 78 9142 16560 19780 2043 329 -1250 C
ATOM 430 C ARG A 78 85.532 -11.135 26.930 1.00114.97 C
ANISOU 430 C ARG A 78 8808 15974 18901 2348 324 -1048 C
ATOM 431 O ARG A 78 85.986 -11.654 25.908 1.00113.37 O
ANISOU 431 O ARG A 78 8524 15787 18763 2410 577 -1080 O
ATOM 432 CB ARG A 78 86.816 -9.036 26.354 1.00111.73 C
ANISOU 432 CB ARG A 78 7800 15540 19114 1799 729 -1469 C
ATOM 433 CG ARG A 78 87.010 -7.530 26.530 1.00115.87 C
ANISOU 433 CG ARG A 78 8147 15997 19883 1435 857 -1649 C
ATOM 434 CD ARG A 78 87.720 -6.919 25.316 1.00124.47 C
ANISOU 434 CD ARG A 78 9030 17018 21247 1165 1357 -1824 C
ATOM 435 NE ARG A 78 88.120 -5.530 25.549 1.00129.11 N
ANISOU 435 NE ARG A 78 9404 17551 22099 799 1490 -2033 N
ATOM 436 CZ ARG A 78 88.683 -4.738 24.638 1.00129.64 C
ANISOU 436 CZ ARG A 78 9337 17520 22400 482 1952 -2200 C
ATOM 437 NH1 ARG A 78 88.918 -5.183 23.410 1.00123.11 N
ANISOU 437 NH1 ARG A 78 8564 16628 21582 489 2328 -2185 N
ATOM 438 NH2 ARG A 78 89.026 -3.497 24.962 1.00137.21 N
ANISOU 438 NH2 ARG A 78 10130 18431 23571 144 2052 -2390 N
ATOM 439 N THR A 79 84.661 -11.749 27.722 1.00114.16 N
ANISOU 439 N THR A 79 9046 15850 18481 2524 48 -843 N
ATOM 440 CA THR A 79 84.072 -13.045 27.431 1.00109.89 C
ANISOU 440 CA THR A 79 8836 15290 17627 2783 36 -624 C
ATOM 441 C THR A 79 82.727 -12.878 26.739 1.00110.92 C
ANISOU 441 C THR A 79 9394 15312 17440 2724 207 -470 C
ATOM 442 O THR A 79 82.160 -11.783 26.671 1.00105.23 O
ANISOU 442 O THR A 79 8743 14510 16729 2506 288 -502 O
ATOM 443 CB THR A 79 83.935 -13.881 28.707 1.00 95.37 C
ANISOU 443 CB THR A 79 7129 13454 15652 2978 -333 -497 C
ATOM 444 OG1 THR A 79 82.928 -13.318 29.556 1.00 89.86 O
ANISOU 444 OG1 THR A 79 6701 12680 14762 2871 -494 -399 O
ATOM 445 CG2 THR A 79 85.263 -13.926 29.453 1.00 92.44 C
ANISOU 445 CG2 THR A 79 6329 13186 15608 3033 -565 -705 C
ATOM 446 N VAL A 80 82.216 -13.990 26.216 1.00104.99 N
ANISOU 446 N VAL A 80 8932 14547 16413 2926 253 -321 N
ATOM 447 CA VAL A 80 80.927 -13.955 25.539 1.00 86.20 C
ANISOU 447 CA VAL A 80 6962 12077 13714 2891 358 -237 C
ATOM 448 C VAL A 80 79.864 -13.464 26.514 1.00 72.79 C
ANISOU 448 C VAL A 80 5513 10333 11813 2818 167 -120 C
ATOM 449 O VAL A 80 79.082 -12.547 26.219 1.00 74.27 O
ANISOU 449 O VAL A 80 5839 10426 11955 2641 243 -155 O
ATOM 450 CB VAL A 80 80.586 -15.349 24.982 1.00 93.11 C
ANISOU 450 CB VAL A 80 8129 12941 14308 3111 362 -153 C
ATOM 451 CG1 VAL A 80 79.100 -15.451 24.692 1.00 94.26 C
ANISOU 451 CG1 VAL A 80 8758 12944 14113 3025 293 -144 C
ATOM 452 CG2 VAL A 80 81.435 -15.668 23.753 1.00 97.82 C
ANISOU 452 CG2 VAL A 80 8511 13565 15092 3173 611 -301 C
ATOM 453 N THR A 81 79.845 -14.060 27.708 1.00 72.79 N
ANISOU 453 N THR A 81 5563 10351 11743 2933 -67 31 N
ATOM 454 CA THR A 81 78.886 -13.674 28.736 1.00 71.63 C
ANISOU 454 CA THR A 81 5647 10124 11446 2842 -239 137 C
ATOM 455 C THR A 81 78.999 -12.190 29.073 1.00 78.62 C
ANISOU 455 C THR A 81 6343 11015 12513 2634 -259 -9 C
ATOM 456 O THR A 81 77.983 -11.504 29.200 1.00 84.58 O
ANISOU 456 O THR A 81 7317 11705 13114 2530 -250 30 O
ATOM 457 CB THR A 81 79.083 -14.538 29.979 1.00 76.45 C
ANISOU 457 CB THR A 81 6255 10665 12126 2949 -509 235 C
ATOM 458 OG1 THR A 81 78.789 -15.903 29.651 1.00 90.43 O
ANISOU 458 OG1 THR A 81 8247 12308 13804 3061 -480 360 O
ATOM 459 CG2 THR A 81 78.153 -14.080 31.097 1.00 60.87 C
ANISOU 459 CG2 THR A 81 4496 8607 10023 2840 -684 306 C
ATOM 460 N ASN A 82 80.219 -11.691 29.310 1.00 82.71 N
ANISOU 460 N ASN A 82 6453 11586 13386 2562 -306 -197 N
ATOM 461 CA ASN A 82 80.353 -10.278 29.668 1.00 77.42 C
ANISOU 461 CA ASN A 82 5598 10884 12933 2332 -318 -351 C
ATOM 462 C ASN A 82 79.970 -9.362 28.519 1.00 72.65 C
ANISOU 462 C ASN A 82 5022 10185 12398 2146 3 -400 C
ATOM 463 O ASN A 82 79.529 -8.234 28.760 1.00 72.83 O
ANISOU 463 O ASN A 82 5064 10117 12491 1967 30 -436 O
ATOM 464 CB ASN A 82 81.753 -9.951 30.167 1.00 86.46 C
ANISOU 464 CB ASN A 82 6286 12116 14447 2276 -441 -577 C
ATOM 465 CG ASN A 82 82.043 -10.575 31.506 1.00 99.06 C
ANISOU 465 CG ASN A 82 7880 13757 16001 2424 -821 -566 C
ATOM 466 OD1 ASN A 82 81.127 -11.013 32.208 1.00 99.59 O
ANISOU 466 OD1 ASN A 82 8294 13759 15788 2507 -976 -392 O
ATOM 467 ND2 ASN A 82 83.314 -10.591 31.889 1.00112.07 N
ANISOU 467 ND2 ASN A 82 9140 15503 17940 2442 -971 -771 N
ATOM 468 N TYR A 83 80.152 -9.801 27.270 1.00 71.44 N
ANISOU 468 N TYR A 83 4875 10018 12250 2176 259 -408 N
ATOM 469 CA TYR A 83 79.662 -8.993 26.157 1.00 74.14 C
ANISOU 469 CA TYR A 83 5321 10201 12648 1991 577 -423 C
ATOM 470 C TYR A 83 78.144 -8.908 26.214 1.00 64.46 C
ANISOU 470 C TYR A 83 4523 8869 11102 2016 510 -265 C
ATOM 471 O TYR A 83 77.554 -7.831 26.030 1.00 69.89 O
ANISOU 471 O TYR A 83 5294 9404 11855 1846 641 -246 O
ATOM 472 CB TYR A 83 80.111 -9.566 24.811 1.00 83.26 C
ANISOU 472 CB TYR A 83 6446 11328 13861 2019 860 -458 C
ATOM 473 CG TYR A 83 81.453 -9.071 24.320 1.00 96.13 C
ANISOU 473 CG TYR A 83 7665 12975 15885 1858 1112 -653 C
ATOM 474 CD1 TYR A 83 82.260 -8.281 25.124 1.00107.82 C
ANISOU 474 CD1 TYR A 83 8799 14522 17648 1713 1028 -812 C
ATOM 475 CD2 TYR A 83 81.900 -9.374 23.034 1.00 95.50 C
ANISOU 475 CD2 TYR A 83 7555 12832 15898 1828 1448 -700 C
ATOM 476 CE1 TYR A 83 83.485 -7.822 24.672 1.00116.21 C
ANISOU 476 CE1 TYR A 83 9477 15608 19071 1536 1268 -1026 C
ATOM 477 CE2 TYR A 83 83.124 -8.916 22.573 1.00103.71 C
ANISOU 477 CE2 TYR A 83 8229 13885 17290 1658 1717 -896 C
ATOM 478 CZ TYR A 83 83.910 -8.142 23.396 1.00113.36 C
ANISOU 478 CZ TYR A 83 9094 15191 18786 1507 1626 -1065 C
ATOM 479 OH TYR A 83 85.127 -7.685 22.945 1.00116.96 O
ANISOU 479 OH TYR A 83 9179 15667 19593 1313 1897 -1290 O
ATOM 480 N PHE A 84 77.489 -10.035 26.487 1.00 52.96 N
ANISOU 480 N PHE A 84 3341 7480 9301 2224 317 -158 N
ATOM 481 CA PHE A 84 76.045 -9.977 26.661 1.00 60.50 C
ANISOU 481 CA PHE A 84 4681 8346 9961 2228 221 -63 C
ATOM 482 C PHE A 84 75.668 -9.103 27.859 1.00 73.54 C
ANISOU 482 C PHE A 84 6332 9996 11613 2155 70 -27 C
ATOM 483 O PHE A 84 74.649 -8.406 27.825 1.00 82.35 O
ANISOU 483 O PHE A 84 7653 10987 12649 2066 95 17 O
ATOM 484 CB PHE A 84 75.487 -11.393 26.814 1.00 64.91 C
ANISOU 484 CB PHE A 84 5525 8967 10171 2426 41 -27 C
ATOM 485 CG PHE A 84 75.372 -12.156 25.512 1.00 67.24 C
ANISOU 485 CG PHE A 84 5928 9162 10459 2451 158 -90 C
ATOM 486 CD1 PHE A 84 74.825 -11.557 24.389 1.00 74.36 C
ANISOU 486 CD1 PHE A 84 6930 9855 11468 2279 388 -39 C
ATOM 487 CD2 PHE A 84 75.810 -13.470 25.411 1.00 64.33 C
ANISOU 487 CD2 PHE A 84 5604 8835 10002 2591 79 -119 C
ATOM 488 CE1 PHE A 84 74.708 -12.254 23.197 1.00 73.12 C
ANISOU 488 CE1 PHE A 84 6892 9576 11315 2280 537 -10 C
ATOM 489 CE2 PHE A 84 75.699 -14.168 24.212 1.00 68.59 C
ANISOU 489 CE2 PHE A 84 6222 9241 10596 2601 187 -173 C
ATOM 490 CZ PHE A 84 75.149 -13.557 23.109 1.00 72.96 C
ANISOU 490 CZ PHE A 84 6864 9620 11238 2442 427 -99 C
ATOM 491 N LEU A 85 76.442 -9.169 28.951 1.00 73.88 N
ANISOU 491 N LEU A 85 6160 10147 11764 2192 -105 -40 N
ATOM 492 CA LEU A 85 76.138 -8.333 30.112 1.00 69.57 C
ANISOU 492 CA LEU A 85 5609 9566 11257 2106 -269 -35 C
ATOM 493 C LEU A 85 76.326 -6.843 29.830 1.00 80.33 C
ANISOU 493 C LEU A 85 6780 10813 12930 1882 -119 -157 C
ATOM 494 O LEU A 85 75.571 -6.019 30.357 1.00 85.69 O
ANISOU 494 O LEU A 85 7583 11400 13576 1810 -169 -125 O
ATOM 495 CB LEU A 85 77.007 -8.728 31.308 1.00 58.65 C
ANISOU 495 CB LEU A 85 4033 8269 9984 2166 -527 -70 C
ATOM 496 CG LEU A 85 76.772 -10.079 31.974 1.00 54.94 C
ANISOU 496 CG LEU A 85 3766 7834 9274 2347 -687 97 C
ATOM 497 CD1 LEU A 85 77.702 -10.237 33.166 1.00 56.26 C
ANISOU 497 CD1 LEU A 85 3728 8029 9619 2376 -981 -5 C
ATOM 498 CD2 LEU A 85 75.322 -10.211 32.397 1.00 54.65 C
ANISOU 498 CD2 LEU A 85 4120 7728 8917 2355 -691 279 C
ATOM 499 N VAL A 86 77.307 -6.472 28.998 1.00 75.63 N
ANISOU 499 N VAL A 86 5890 10202 12645 1761 100 -290 N
ATOM 500 CA VAL A 86 77.412 -5.076 28.581 1.00 66.18 C
ANISOU 500 CA VAL A 86 4552 8855 11737 1518 343 -384 C
ATOM 501 C VAL A 86 76.215 -4.696 27.734 1.00 56.97 C
ANISOU 501 C VAL A 86 3719 7505 10423 1497 561 -230 C
ATOM 502 O VAL A 86 75.734 -3.563 27.799 1.00 61.06 O
ANISOU 502 O VAL A 86 4283 7869 11046 1367 678 -214 O
ATOM 503 CB VAL A 86 78.742 -4.767 27.864 1.00 69.88 C
ANISOU 503 CB VAL A 86 4649 9339 12563 1353 596 -575 C
ATOM 504 CG1 VAL A 86 79.914 -4.992 28.802 1.00 76.40 C
ANISOU 504 CG1 VAL A 86 5121 10341 13568 1365 341 -748 C
ATOM 505 CG2 VAL A 86 78.889 -5.550 26.568 1.00 58.80 C
ANISOU 505 CG2 VAL A 86 3322 7922 11096 1423 843 -524 C
ATOM 506 N ASN A 87 75.729 -5.620 26.901 1.00 49.55 N
ANISOU 506 N ASN A 87 3015 6561 9250 1623 622 -120 N
ATOM 507 CA ASN A 87 74.522 -5.296 26.146 1.00 59.30 C
ANISOU 507 CA ASN A 87 4588 7614 10330 1611 778 34 C
ATOM 508 C ASN A 87 73.320 -5.127 27.068 1.00 58.67 C
ANISOU 508 C ASN A 87 4763 7530 10000 1679 535 129 C
ATOM 509 O ASN A 87 72.479 -4.243 26.854 1.00 58.27 O
ANISOU 509 O ASN A 87 4885 7318 9939 1623 652 228 O
ATOM 510 CB ASN A 87 74.232 -6.372 25.104 1.00 69.14 C
ANISOU 510 CB ASN A 87 6034 8848 11389 1711 847 104 C
ATOM 511 CG ASN A 87 73.337 -5.865 23.993 1.00 66.98 C
ANISOU 511 CG ASN A 87 6039 8349 11061 1655 1107 259 C
ATOM 512 OD1 ASN A 87 73.491 -4.730 23.527 1.00 57.40 O
ANISOU 512 OD1 ASN A 87 4790 6969 10050 1525 1410 276 O
ATOM 513 ND2 ASN A 87 72.372 -6.686 23.586 1.00 67.13 N
ANISOU 513 ND2 ASN A 87 6357 8350 10799 1745 1000 367 N
ATOM 514 N LEU A 88 73.221 -5.974 28.093 1.00 63.70 N
ANISOU 514 N LEU A 88 5450 8335 10418 1809 227 106 N
ATOM 515 CA LEU A 88 72.150 -5.835 29.073 1.00 64.16 C
ANISOU 515 CA LEU A 88 5744 8394 10239 1855 28 166 C
ATOM 516 C LEU A 88 72.248 -4.494 29.786 1.00 76.07 C
ANISOU 516 C LEU A 88 7110 9819 11974 1746 35 150 C
ATOM 517 O LEU A 88 71.240 -3.807 29.999 1.00 84.14 O
ANISOU 517 O LEU A 88 8330 10731 12907 1731 42 227 O
ATOM 518 CB LEU A 88 72.207 -6.989 30.076 1.00 47.35 C
ANISOU 518 CB LEU A 88 3687 6445 7859 2010 -222 158 C
ATOM 519 CG LEU A 88 71.200 -6.930 31.222 1.00 38.73 C
ANISOU 519 CG LEU A 88 2828 5363 6524 2055 -383 219 C
ATOM 520 CD1 LEU A 88 69.788 -6.921 30.669 1.00 35.78 C
ANISOU 520 CD1 LEU A 88 2777 4846 5971 2003 -365 202 C
ATOM 521 CD2 LEU A 88 71.396 -8.085 32.176 1.00 39.13 C
ANISOU 521 CD2 LEU A 88 2963 5522 6382 2130 -507 315 C
ATOM 522 N SER A 89 73.470 -4.088 30.115 1.00 73.42 N
ANISOU 522 N SER A 89 6419 9522 11957 1657 31 19 N
ATOM 523 CA SER A 89 73.683 -2.789 30.729 1.00 74.17 C
ANISOU 523 CA SER A 89 6335 9515 12332 1514 33 -67 C
ATOM 524 C SER A 89 73.355 -1.667 29.754 1.00 76.58 C
ANISOU 524 C SER A 89 6669 9602 12827 1384 390 -28 C
ATOM 525 O SER A 89 72.894 -0.602 30.168 1.00 88.88 O
ANISOU 525 O SER A 89 8260 11019 14493 1324 430 -17 O
ATOM 526 CB SER A 89 75.130 -2.684 31.216 1.00 78.82 C
ANISOU 526 CB SER A 89 6514 10209 13226 1410 -65 -281 C
ATOM 527 OG SER A 89 75.367 -3.558 32.310 1.00 75.23 O
ANISOU 527 OG SER A 89 6074 9908 12603 1547 -408 -288 O
ATOM 528 N LEU A 90 73.562 -1.902 28.457 1.00 71.57 N
ANISOU 528 N LEU A 90 6057 8911 12223 1355 677 6 N
ATOM 529 CA LEU A 90 73.206 -0.917 27.441 1.00 66.72 C
ANISOU 529 CA LEU A 90 5561 8057 11731 1256 1079 79 C
ATOM 530 C LEU A 90 71.694 -0.729 27.353 1.00 67.12 C
ANISOU 530 C LEU A 90 6029 7994 11482 1401 1041 296 C
ATOM 531 O LEU A 90 71.197 0.406 27.288 1.00 72.32 O
ANISOU 531 O LEU A 90 6859 8461 12158 1349 1211 347 O
ATOM 532 CB LEU A 90 73.777 -1.382 26.102 1.00 57.02 C
ANISOU 532 CB LEU A 90 4317 6798 10549 1208 1376 72 C
ATOM 533 CG LEU A 90 74.180 -0.367 25.050 1.00 49.94 C
ANISOU 533 CG LEU A 90 3421 5676 9879 1001 1900 29 C
ATOM 534 CD1 LEU A 90 75.474 0.252 25.485 1.00 53.71 C
ANISOU 534 CD1 LEU A 90 3493 6211 10705 730 1995 -238 C
ATOM 535 CD2 LEU A 90 74.348 -1.080 23.732 1.00 50.17 C
ANISOU 535 CD2 LEU A 90 3590 5660 9812 1033 2129 91 C
ATOM 536 N ALA A 91 70.944 -1.830 27.386 1.00 62.98 N
ANISOU 536 N ALA A 91 5734 7597 10598 1544 799 387 N
ATOM 537 CA ALA A 91 69.487 -1.733 27.393 1.00 60.58 C
ANISOU 537 CA ALA A 91 5799 7240 9979 1633 710 530 C
ATOM 538 C ALA A 91 69.002 -1.030 28.653 1.00 76.24 C
ANISOU 538 C ALA A 91 7810 9217 11942 1650 540 518 C
ATOM 539 O ALA A 91 68.104 -0.169 28.605 1.00 86.10 O
ANISOU 539 O ALA A 91 9281 10325 13108 1680 614 611 O
ATOM 540 CB ALA A 91 68.862 -3.122 27.270 1.00 49.49 C
ANISOU 540 CB ALA A 91 4577 5981 8245 1704 495 536 C
ATOM 541 N ASP A 92 69.624 -1.357 29.791 1.00 77.06 N
ANISOU 541 N ASP A 92 7706 9459 12113 1644 313 402 N
ATOM 542 CA ASP A 92 69.219 -0.741 31.046 1.00 77.64 C
ANISOU 542 CA ASP A 92 7810 9511 12178 1663 144 389 C
ATOM 543 C ASP A 92 69.529 0.749 31.045 1.00 86.03 C
ANISOU 543 C ASP A 92 8754 10355 13579 1566 343 360 C
ATOM 544 O ASP A 92 68.741 1.551 31.558 1.00 93.19 O
ANISOU 544 O ASP A 92 9920 11162 14324 1559 318 401 O
ATOM 545 CB ASP A 92 69.960 -1.403 32.211 1.00 77.40 C
ANISOU 545 CB ASP A 92 7595 9651 12162 1677 -138 271 C
ATOM 546 CG ASP A 92 69.456 -2.794 32.522 1.00 84.56 C
ANISOU 546 CG ASP A 92 8716 10733 12679 1799 -304 302 C
ATOM 547 OD1 ASP A 92 68.459 -3.232 31.910 1.00 87.29 O
ANISOU 547 OD1 ASP A 92 9325 11067 12774 1836 -253 351 O
ATOM 548 OD2 ASP A 92 70.066 -3.451 33.395 1.00 89.43 O
ANISOU 548 OD2 ASP A 92 9234 11476 13268 1841 -488 260 O
ATOM 549 N VAL A 93 70.639 1.143 30.416 1.00 85.05 N
ANISOU 549 N VAL A 93 8444 10199 13672 1363 551 234 N
ATOM 550 CA VAL A 93 70.973 2.557 30.317 1.00 76.19 C
ANISOU 550 CA VAL A 93 7449 8908 12592 1099 759 142 C
ATOM 551 C VAL A 93 69.987 3.279 29.419 1.00 69.39 C
ANISOU 551 C VAL A 93 7026 7831 11508 1129 1008 302 C
ATOM 552 O VAL A 93 69.606 4.422 29.692 1.00 67.66 O
ANISOU 552 O VAL A 93 7079 7448 11180 1034 1070 298 O
ATOM 553 CB VAL A 93 72.416 2.733 29.819 1.00 70.51 C
ANISOU 553 CB VAL A 93 6405 8211 12175 848 959 -51 C
ATOM 554 CG1 VAL A 93 72.563 4.069 29.105 1.00 50.12 C
ANISOU 554 CG1 VAL A 93 4082 5386 9577 578 1328 -84 C
ATOM 555 CG2 VAL A 93 73.393 2.611 30.980 1.00 83.02 C
ANISOU 555 CG2 VAL A 93 7601 9962 13981 755 675 -265 C
ATOM 556 N LEU A 94 69.536 2.621 28.350 1.00 69.45 N
ANISOU 556 N LEU A 94 7133 7824 11432 1282 1131 441 N
ATOM 557 CA LEU A 94 68.520 3.233 27.498 1.00 77.08 C
ANISOU 557 CA LEU A 94 8532 8590 12166 1361 1303 595 C
ATOM 558 C LEU A 94 67.256 3.522 28.298 1.00 73.01 C
ANISOU 558 C LEU A 94 8229 8066 11445 1538 1093 686 C
ATOM 559 O LEU A 94 66.761 4.666 28.333 1.00 69.21 O
ANISOU 559 O LEU A 94 8057 7401 10839 1504 1179 703 O
ATOM 560 CB LEU A 94 68.212 2.314 26.310 1.00 85.64 C
ANISOU 560 CB LEU A 94 9671 9684 13182 1517 1403 723 C
ATOM 561 CG LEU A 94 67.072 2.655 25.337 1.00 77.36 C
ANISOU 561 CG LEU A 94 9055 8459 11877 1668 1505 894 C
ATOM 562 CD1 LEU A 94 67.273 1.896 24.029 1.00 77.36 C
ANISOU 562 CD1 LEU A 94 9099 8432 11862 1714 1678 963 C
ATOM 563 CD2 LEU A 94 65.692 2.333 25.906 1.00 67.67 C
ANISOU 563 CD2 LEU A 94 7952 7383 10377 1821 1178 960 C
ATOM 564 N ALA A 95 66.745 2.497 28.988 1.00 68.93 N
ANISOU 564 N ALA A 95 7558 7738 10892 1724 830 731 N
ATOM 565 CA ALA A 95 65.504 2.686 29.729 1.00 59.30 C
ANISOU 565 CA ALA A 95 6554 6556 9421 1827 641 772 C
ATOM 566 C ALA A 95 65.668 3.692 30.862 1.00 55.20 C
ANISOU 566 C ALA A 95 6061 5939 8973 1760 604 696 C
ATOM 567 O ALA A 95 64.812 4.564 31.039 1.00 37.14 O
ANISOU 567 O ALA A 95 4051 3522 6539 1820 639 737 O
ATOM 568 CB ALA A 95 65.017 1.349 30.278 1.00 58.88 C
ANISOU 568 CB ALA A 95 6460 6777 9134 1824 346 708 C
ATOM 569 N THR A 96 66.830 3.698 31.524 1.00 57.35 N
ANISOU 569 N THR A 96 6092 6277 9420 1574 529 544 N
ATOM 570 CA THR A 96 67.037 4.623 32.635 1.00 60.94 C
ANISOU 570 CA THR A 96 6617 6669 9870 1435 443 428 C
ATOM 571 C THR A 96 67.139 6.059 32.147 1.00 67.41 C
ANISOU 571 C THR A 96 7708 7245 10660 1261 695 397 C
ATOM 572 O THR A 96 66.501 6.964 32.703 1.00 68.81 O
ANISOU 572 O THR A 96 8160 7290 10694 1276 691 403 O
ATOM 573 CB THR A 96 68.291 4.234 33.411 1.00 47.95 C
ANISOU 573 CB THR A 96 4629 5161 8427 1284 261 256 C
ATOM 574 OG1 THR A 96 68.119 2.917 33.945 1.00 59.50 O
ANISOU 574 OG1 THR A 96 5922 6815 9871 1475 8 295 O
ATOM 575 CG2 THR A 96 68.545 5.215 34.556 1.00 43.75 C
ANISOU 575 CG2 THR A 96 4190 4552 7879 1118 154 124 C
ATOM 576 N ALA A 97 67.898 6.282 31.079 1.00 65.07 N
ANISOU 576 N ALA A 97 7378 6866 10479 1102 941 367 N
ATOM 577 CA ALA A 97 68.147 7.641 30.638 1.00 60.97 C
ANISOU 577 CA ALA A 97 7147 6090 9929 892 1204 319 C
ATOM 578 C ALA A 97 66.886 8.272 30.073 1.00 71.80 C
ANISOU 578 C ALA A 97 8975 7262 11043 1090 1309 479 C
ATOM 579 O ALA A 97 66.617 9.450 30.335 1.00 77.26 O
ANISOU 579 O ALA A 97 9988 7745 11621 1025 1390 457 O
ATOM 580 CB ALA A 97 69.265 7.664 29.598 1.00 57.76 C
ANISOU 580 CB ALA A 97 6612 5632 9702 657 1483 240 C
ATOM 581 N ILE A 98 66.060 7.510 29.355 1.00 76.39 N
ANISOU 581 N ILE A 98 9599 7903 11524 1351 1281 634 N
ATOM 582 CA ILE A 98 64.961 8.095 28.600 1.00 69.52 C
ANISOU 582 CA ILE A 98 9142 6841 10432 1550 1376 770 C
ATOM 583 C ILE A 98 63.604 7.810 29.235 1.00 74.60 C
ANISOU 583 C ILE A 98 9822 7585 10939 1851 1150 855 C
ATOM 584 O ILE A 98 62.798 8.724 29.426 1.00 81.84 O
ANISOU 584 O ILE A 98 11042 8347 11707 1969 1161 882 O
ATOM 585 CB ILE A 98 64.994 7.591 27.140 1.00 55.34 C
ANISOU 585 CB ILE A 98 7422 4997 8606 1610 1534 870 C
ATOM 586 CG1 ILE A 98 66.230 8.131 26.432 1.00 45.78 C
ANISOU 586 CG1 ILE A 98 6272 3621 7500 1295 1842 778 C
ATOM 587 CG2 ILE A 98 63.725 7.972 26.416 1.00 60.71 C
ANISOU 587 CG2 ILE A 98 8495 5524 9049 1885 1533 1015 C
ATOM 588 CD1 ILE A 98 66.140 9.580 26.095 1.00 67.76 C
ANISOU 588 CD1 ILE A 98 9538 6072 10137 1188 2058 772 C
ATOM 589 N CYS A 99 63.342 6.555 29.598 1.00 64.60 N
ANISOU 589 N CYS A 99 8254 6570 9721 1975 958 886 N
ATOM 590 CA CYS A 99 62.006 6.181 30.041 1.00 68.94 C
ANISOU 590 CA CYS A 99 8818 7348 10029 2045 698 861 C
ATOM 591 C CYS A 99 61.749 6.508 31.505 1.00 63.31 C
ANISOU 591 C CYS A 99 8087 6644 9325 2077 593 804 C
ATOM 592 O CYS A 99 60.646 6.950 31.857 1.00 55.88 O
ANISOU 592 O CYS A 99 7283 5723 8225 2130 516 778 O
ATOM 593 CB CYS A 99 61.797 4.693 29.777 1.00 72.56 C
ANISOU 593 CB CYS A 99 9051 8085 10434 1999 521 835 C
ATOM 594 SG CYS A 99 62.246 4.256 28.088 1.00 65.28 S
ANISOU 594 SG CYS A 99 8166 7126 9513 1972 670 907 S
ATOM 595 N LEU A 100 62.767 6.362 32.349 1.00 56.42 N
ANISOU 595 N LEU A 100 7034 5745 8659 2023 592 768 N
ATOM 596 CA LEU A 100 62.583 6.602 33.777 1.00 53.65 C
ANISOU 596 CA LEU A 100 6698 5423 8263 2001 454 689 C
ATOM 597 C LEU A 100 62.089 8.002 34.112 1.00 62.47 C
ANISOU 597 C LEU A 100 8150 6323 9262 2006 553 660 C
ATOM 598 O LEU A 100 61.108 8.120 34.867 1.00 67.53 O
ANISOU 598 O LEU A 100 8895 6976 9789 2164 491 670 O
ATOM 599 CB LEU A 100 63.913 6.320 34.480 1.00 48.22 C
ANISOU 599 CB LEU A 100 5778 4819 7725 1769 339 557 C
ATOM 600 CG LEU A 100 63.919 6.526 35.986 1.00 61.53 C
ANISOU 600 CG LEU A 100 7505 6521 9354 1718 165 460 C
ATOM 601 CD1 LEU A 100 62.772 5.724 36.607 1.00 59.19 C
ANISOU 601 CD1 LEU A 100 7229 6342 8920 1943 50 535 C
ATOM 602 CD2 LEU A 100 65.271 6.114 36.566 1.00 83.13 C
ANISOU 602 CD2 LEU A 100 9976 9360 12249 1520 -4 323 C
ATOM 603 N PRO A 101 62.697 9.082 33.629 1.00 60.93 N
ANISOU 603 N PRO A 101 8152 5916 9081 1840 721 617 N
ATOM 604 CA PRO A 101 62.163 10.406 34.001 1.00 64.15 C
ANISOU 604 CA PRO A 101 8929 6095 9351 1870 810 592 C
ATOM 605 C PRO A 101 60.708 10.592 33.574 1.00 58.39 C
ANISOU 605 C PRO A 101 8400 5313 8472 2207 836 704 C
ATOM 606 O PRO A 101 59.870 11.125 34.331 1.00 52.59 O
ANISOU 606 O PRO A 101 7794 4578 7611 2283 781 662 O
ATOM 607 CB PRO A 101 63.117 11.372 33.280 1.00 59.11 C
ANISOU 607 CB PRO A 101 8479 5228 8753 1617 1019 539 C
ATOM 608 CG PRO A 101 64.370 10.552 33.006 1.00 44.77 C
ANISOU 608 CG PRO A 101 6294 3570 7145 1389 1002 476 C
ATOM 609 CD PRO A 101 63.874 9.175 32.747 1.00 52.44 C
ANISOU 609 CD PRO A 101 7001 4783 8142 1610 866 578 C
ATOM 610 N ALA A 102 60.376 10.078 32.385 1.00 58.06 N
ANISOU 610 N ALA A 102 8263 5415 8381 2218 807 760 N
ATOM 611 CA ALA A 102 59.008 10.154 31.884 1.00 63.24 C
ANISOU 611 CA ALA A 102 8944 6217 8865 2303 697 763 C
ATOM 612 C ALA A 102 58.063 9.302 32.715 1.00 60.53 C
ANISOU 612 C ALA A 102 8348 6140 8509 2328 516 714 C
ATOM 613 O ALA A 102 56.925 9.708 32.991 1.00 65.60 O
ANISOU 613 O ALA A 102 9035 6822 9069 2405 478 681 O
ATOM 614 CB ALA A 102 58.962 9.721 30.419 1.00 69.93 C
ANISOU 614 CB ALA A 102 9773 7121 9676 2287 703 820 C
ATOM 615 N SER A 103 58.513 8.121 33.134 1.00 52.97 N
ANISOU 615 N SER A 103 7138 5348 7640 2258 424 702 N
ATOM 616 CA SER A 103 57.661 7.288 33.970 1.00 47.38 C
ANISOU 616 CA SER A 103 6255 4842 6907 2247 294 651 C
ATOM 617 C SER A 103 57.389 7.954 35.309 1.00 62.91 C
ANISOU 617 C SER A 103 8339 6721 8842 2318 327 612 C
ATOM 618 O SER A 103 56.286 7.842 35.860 1.00 73.85 O
ANISOU 618 O SER A 103 9693 8198 10169 2359 305 574 O
ATOM 619 CB SER A 103 58.318 5.932 34.185 1.00 37.42 C
ANISOU 619 CB SER A 103 4768 3733 5716 2154 192 642 C
ATOM 620 OG SER A 103 57.492 5.119 34.992 1.00 44.51 O
ANISOU 620 OG SER A 103 5561 4776 6575 2130 104 598 O
ATOM 621 N LEU A 104 58.383 8.661 35.846 1.00 68.74 N
ANISOU 621 N LEU A 104 9238 7256 9625 2333 404 613 N
ATOM 622 CA LEU A 104 58.168 9.378 37.097 1.00 64.21 C
ANISOU 622 CA LEU A 104 8858 6549 8989 2398 442 561 C
ATOM 623 C LEU A 104 57.134 10.484 36.920 1.00 63.72 C
ANISOU 623 C LEU A 104 9000 6399 8810 2479 528 541 C
ATOM 624 O LEU A 104 56.243 10.661 37.766 1.00 56.55 O
ANISOU 624 O LEU A 104 8133 5528 7826 2552 537 493 O
ATOM 625 CB LEU A 104 59.490 9.942 37.616 1.00 49.28 C
ANISOU 625 CB LEU A 104 7124 4433 7169 2304 482 523 C
ATOM 626 CG LEU A 104 59.361 10.973 38.733 1.00 44.51 C
ANISOU 626 CG LEU A 104 6804 3660 6449 2251 511 425 C
ATOM 627 CD1 LEU A 104 58.738 10.315 39.967 1.00 45.81 C
ANISOU 627 CD1 LEU A 104 6922 3952 6531 2327 415 391 C
ATOM 628 CD2 LEU A 104 60.730 11.529 39.080 1.00 54.24 C
ANISOU 628 CD2 LEU A 104 8087 4786 7736 1926 473 316 C
ATOM 629 N LEU A 105 57.215 11.226 35.813 1.00 71.24 N
ANISOU 629 N LEU A 105 10095 7234 9740 2483 601 576 N
ATOM 630 CA LEU A 105 56.221 12.284 35.617 1.00 66.37 C
ANISOU 630 CA LEU A 105 9674 6540 9005 2589 654 558 C
ATOM 631 C LEU A 105 54.820 11.717 35.432 1.00 57.21 C
ANISOU 631 C LEU A 105 8285 5620 7830 2666 562 544 C
ATOM 632 O LEU A 105 53.840 12.332 35.866 1.00 49.91 O
ANISOU 632 O LEU A 105 7435 4683 6845 2781 590 500 O
ATOM 633 CB LEU A 105 56.573 13.159 34.416 1.00 72.64 C
ANISOU 633 CB LEU A 105 10708 7145 9748 2585 742 604 C
ATOM 634 CG LEU A 105 57.477 14.360 34.671 1.00 87.14 C
ANISOU 634 CG LEU A 105 12933 8634 11542 2517 902 582 C
ATOM 635 CD1 LEU A 105 58.931 13.933 34.894 1.00 82.17 C
ANISOU 635 CD1 LEU A 105 12283 7875 11063 2351 965 577 C
ATOM 636 CD2 LEU A 105 57.351 15.343 33.512 1.00100.42 C
ANISOU 636 CD2 LEU A 105 14905 10147 13104 2542 994 621 C
ATOM 637 N VAL A 106 54.693 10.563 34.772 1.00 63.06 N
ANISOU 637 N VAL A 106 8763 6560 8636 2597 462 569 N
ATOM 638 CA VAL A 106 53.367 9.966 34.630 1.00 60.60 C
ANISOU 638 CA VAL A 106 8251 6437 8338 2638 386 536 C
ATOM 639 C VAL A 106 52.836 9.503 35.979 1.00 65.24 C
ANISOU 639 C VAL A 106 8737 7117 8934 2652 401 478 C
ATOM 640 O VAL A 106 51.659 9.713 36.301 1.00 72.20 O
ANISOU 640 O VAL A 106 9579 8046 9809 2753 423 426 O
ATOM 641 CB VAL A 106 53.380 8.819 33.611 1.00 66.25 C
ANISOU 641 CB VAL A 106 8763 7302 9108 2536 285 563 C
ATOM 642 CG1 VAL A 106 52.018 8.132 33.609 1.00 66.07 C
ANISOU 642 CG1 VAL A 106 8543 7439 9123 2558 218 513 C
ATOM 643 CG2 VAL A 106 53.710 9.352 32.228 1.00 73.83 C
ANISOU 643 CG2 VAL A 106 9866 8156 10029 2557 293 620 C
ATOM 644 N ASP A 107 53.692 8.866 36.790 1.00 72.47 N
ANISOU 644 N ASP A 107 9619 8049 9867 2569 395 482 N
ATOM 645 CA ASP A 107 53.276 8.371 38.099 1.00 76.31 C
ANISOU 645 CA ASP A 107 10066 8600 10329 2591 424 437 C
ATOM 646 C ASP A 107 52.948 9.483 39.086 1.00 89.48 C
ANISOU 646 C ASP A 107 11969 10114 11916 2714 542 387 C
ATOM 647 O ASP A 107 52.223 9.228 40.055 1.00 97.09 O
ANISOU 647 O ASP A 107 12923 11127 12841 2772 606 336 O
ATOM 648 CB ASP A 107 54.350 7.453 38.686 1.00 74.29 C
ANISOU 648 CB ASP A 107 9760 8372 10095 2497 364 460 C
ATOM 649 CG ASP A 107 54.452 6.138 37.946 1.00 74.72 C
ANISOU 649 CG ASP A 107 9581 8600 10209 2376 259 488 C
ATOM 650 OD1 ASP A 107 53.559 5.874 37.121 1.00 76.32 O
ANISOU 650 OD1 ASP A 107 9674 8896 10427 2364 242 478 O
ATOM 651 OD2 ASP A 107 55.417 5.374 38.179 1.00 76.65 O
ANISOU 651 OD2 ASP A 107 9767 8872 10485 2301 184 511 O
ATOM 652 N ILE A 108 53.496 10.688 38.909 1.00 89.15 N
ANISOU 652 N ILE A 108 12174 9863 11834 2749 593 394 N
ATOM 653 CA ILE A 108 53.096 11.788 39.787 1.00 76.19 C
ANISOU 653 CA ILE A 108 10794 8056 10097 2856 709 334 C
ATOM 654 C ILE A 108 51.759 12.394 39.362 1.00 74.37 C
ANISOU 654 C ILE A 108 10532 7870 9854 2994 745 305 C
ATOM 655 O ILE A 108 50.861 12.584 40.190 1.00 79.75 O
ANISOU 655 O ILE A 108 11230 8568 10504 3095 827 238 O
ATOM 656 CB ILE A 108 54.186 12.870 39.831 1.00 65.59 C
ANISOU 656 CB ILE A 108 9782 6432 8707 2818 759 336 C
ATOM 657 CG1 ILE A 108 55.415 12.374 40.579 1.00 73.61 C
ANISOU 657 CG1 ILE A 108 10863 7358 9748 2710 716 326 C
ATOM 658 CG2 ILE A 108 53.647 14.124 40.481 1.00 65.92 C
ANISOU 658 CG2 ILE A 108 10125 6291 8630 2918 878 272 C
ATOM 659 CD1 ILE A 108 56.572 13.329 40.463 1.00 78.02 C
ANISOU 659 CD1 ILE A 108 11728 7612 10303 2621 762 310 C
ATOM 660 N THR A 109 51.602 12.698 38.073 1.00 71.62 N
ANISOU 660 N THR A 109 10149 7530 9533 3013 685 348 N
ATOM 661 CA THR A 109 50.456 13.453 37.573 1.00 66.73 C
ANISOU 661 CA THR A 109 9550 6903 8901 3173 690 320 C
ATOM 662 C THR A 109 49.418 12.625 36.819 1.00 71.63 C
ANISOU 662 C THR A 109 9856 7732 9628 3198 588 309 C
ATOM 663 O THR A 109 48.390 13.182 36.411 1.00 69.69 O
ANISOU 663 O THR A 109 9593 7484 9402 3351 570 274 O
ATOM 664 CB THR A 109 50.943 14.605 36.680 1.00 75.30 C
ANISOU 664 CB THR A 109 10922 7787 9903 3213 704 368 C
ATOM 665 OG1 THR A 109 51.312 14.101 35.390 1.00 93.72 O
ANISOU 665 OG1 THR A 109 13156 10179 12275 3138 612 436 O
ATOM 666 CG2 THR A 109 52.137 15.302 37.312 1.00 71.18 C
ANISOU 666 CG2 THR A 109 10717 7029 9298 3130 805 372 C
ATOM 667 N GLU A 110 49.631 11.320 36.638 1.00 76.49 N
ANISOU 667 N GLU A 110 10236 8510 10317 3058 516 328 N
ATOM 668 CA GLU A 110 48.670 10.479 35.914 1.00 80.76 C
ANISOU 668 CA GLU A 110 10506 9219 10962 3054 421 307 C
ATOM 669 C GLU A 110 48.236 11.123 34.594 1.00 91.91 C
ANISOU 669 C GLU A 110 11970 10575 12377 3152 342 335 C
ATOM 670 O GLU A 110 47.074 11.040 34.183 1.00 90.59 O
ANISOU 670 O GLU A 110 11650 10477 12294 3254 288 291 O
ATOM 671 CB GLU A 110 47.452 10.161 36.780 1.00 83.44 C
ANISOU 671 CB GLU A 110 10672 9661 11370 3138 482 209 C
ATOM 672 CG GLU A 110 47.788 9.511 38.111 1.00 85.57 C
ANISOU 672 CG GLU A 110 10936 9976 11602 3066 581 184 C
ATOM 673 CD GLU A 110 48.661 8.283 37.944 1.00101.03 C
ANISOU 673 CD GLU A 110 12804 12023 13560 2882 509 244 C
ATOM 674 OE1 GLU A 110 48.689 7.732 36.815 1.00114.56 O
ANISOU 674 OE1 GLU A 110 14397 13802 15330 2802 394 279 O
ATOM 675 OE2 GLU A 110 49.293 7.858 38.947 1.00105.59 O
ANISOU 675 OE2 GLU A 110 13449 12592 14077 2829 568 253 O
ATOM 676 N SER A 111 49.183 11.794 33.936 1.00 94.22 N
ANISOU 676 N SER A 111 12500 10723 12578 3135 346 407 N
ATOM 677 CA SER A 111 48.921 12.565 32.728 1.00 80.18 C
ANISOU 677 CA SER A 111 10872 8847 10746 3249 296 445 C
ATOM 678 C SER A 111 50.179 12.544 31.878 1.00 74.65 C
ANISOU 678 C SER A 111 10333 8055 9975 3133 302 530 C
ATOM 679 O SER A 111 51.274 12.230 32.356 1.00 79.22 O
ANISOU 679 O SER A 111 10935 8611 10555 2995 360 551 O
ATOM 680 CB SER A 111 48.510 14.017 33.016 1.00 80.33 C
ANISOU 680 CB SER A 111 11151 8698 10672 3445 363 419 C
ATOM 681 OG SER A 111 49.621 14.813 33.393 1.00 78.51 O
ANISOU 681 OG SER A 111 11232 8275 10323 3397 475 452 O
ATOM 682 N TRP A 112 50.009 12.888 30.608 1.00 68.54 N
ANISOU 682 N TRP A 112 9680 7220 9143 3205 248 574 N
ATOM 683 CA TRP A 112 51.088 12.862 29.626 1.00 66.51 C
ANISOU 683 CA TRP A 112 9593 6866 8812 3113 275 652 C
ATOM 684 C TRP A 112 51.395 14.280 29.173 1.00 71.28 C
ANISOU 684 C TRP A 112 10612 7219 9251 3225 363 685 C
ATOM 685 O TRP A 112 50.524 14.961 28.618 1.00 93.94 O
ANISOU 685 O TRP A 112 13612 10037 12043 3405 308 678 O
ATOM 686 CB TRP A 112 50.715 11.991 28.427 1.00 67.23 C
ANISOU 686 CB TRP A 112 9540 7069 8935 3089 158 680 C
ATOM 687 CG TRP A 112 51.841 11.852 27.459 1.00 68.59 C
ANISOU 687 CG TRP A 112 9879 7148 9034 2994 211 754 C
ATOM 688 CD1 TRP A 112 51.973 12.514 26.266 1.00 72.12 C
ANISOU 688 CD1 TRP A 112 10625 7442 9338 3079 232 807 C
ATOM 689 CD2 TRP A 112 53.007 11.038 27.599 1.00 70.54 C
ANISOU 689 CD2 TRP A 112 10033 7431 9338 2813 267 780 C
ATOM 690 NE1 TRP A 112 53.146 12.154 25.650 1.00 74.33 N
ANISOU 690 NE1 TRP A 112 11003 7652 9586 2949 323 865 N
ATOM 691 CE2 TRP A 112 53.800 11.250 26.446 1.00 70.32 C
ANISOU 691 CE2 TRP A 112 10240 7263 9214 2792 342 849 C
ATOM 692 CE3 TRP A 112 53.462 10.154 28.581 1.00 63.54 C
ANISOU 692 CE3 TRP A 112 8906 6672 8565 2679 264 749 C
ATOM 693 CZ2 TRP A 112 55.016 10.606 26.248 1.00 61.12 C
ANISOU 693 CZ2 TRP A 112 9045 6086 8092 2648 429 887 C
ATOM 694 CZ3 TRP A 112 54.678 9.513 28.383 1.00 58.89 C
ANISOU 694 CZ3 TRP A 112 8286 6079 8011 2547 318 786 C
ATOM 695 CH2 TRP A 112 55.438 9.745 27.223 1.00 55.37 C
ANISOU 695 CH2 TRP A 112 8046 5497 7497 2536 407 854 C
ATOM 696 N LEU A 113 52.626 14.715 29.411 1.00 66.48 N
ANISOU 696 N LEU A 113 10229 6441 8590 3119 503 715 N
ATOM 697 CA LEU A 113 53.046 16.088 29.173 1.00 78.04 C
ANISOU 697 CA LEU A 113 12140 7623 9888 3174 630 735 C
ATOM 698 C LEU A 113 54.073 16.211 28.048 1.00 75.84 C
ANISOU 698 C LEU A 113 12119 7177 9521 3072 733 804 C
ATOM 699 O LEU A 113 54.590 17.310 27.814 1.00 89.13 O
ANISOU 699 O LEU A 113 14218 8591 11057 3061 878 818 O
ATOM 700 CB LEU A 113 53.584 16.697 30.472 1.00 89.70 C
ANISOU 700 CB LEU A 113 13744 8968 11369 3116 753 693 C
ATOM 701 CG LEU A 113 52.592 16.637 31.642 1.00 90.28 C
ANISOU 701 CG LEU A 113 13614 9181 11506 3221 691 621 C
ATOM 702 CD1 LEU A 113 53.244 17.055 32.954 1.00 81.48 C
ANISOU 702 CD1 LEU A 113 12628 7938 10392 3140 808 578 C
ATOM 703 CD2 LEU A 113 51.369 17.503 31.335 1.00 90.88 C
ANISOU 703 CD2 LEU A 113 13819 9223 11490 3454 639 597 C
ATOM 704 N PHE A 114 54.372 15.121 27.332 1.00 69.78 N
ANISOU 704 N PHE A 114 11143 6544 8828 2985 682 841 N
ATOM 705 CA PHE A 114 55.457 15.087 26.352 1.00 66.40 C
ANISOU 705 CA PHE A 114 10930 5958 8340 2866 819 903 C
ATOM 706 C PHE A 114 55.007 15.068 24.892 1.00 65.25 C
ANISOU 706 C PHE A 114 10938 5798 8057 2958 760 946 C
ATOM 707 O PHE A 114 55.863 14.944 24.002 1.00 60.51 O
ANISOU 707 O PHE A 114 10523 5073 7395 2857 890 995 O
ATOM 708 CB PHE A 114 56.373 13.888 26.630 1.00 68.67 C
ANISOU 708 CB PHE A 114 10919 6367 8805 2694 846 915 C
ATOM 709 CG PHE A 114 56.903 13.847 28.040 1.00 71.77 C
ANISOU 709 CG PHE A 114 11181 6759 9327 2609 892 870 C
ATOM 710 CD1 PHE A 114 56.530 12.836 28.907 1.00 85.26 C
ANISOU 710 CD1 PHE A 114 12498 8726 11171 2601 749 832 C
ATOM 711 CD2 PHE A 114 57.765 14.826 28.497 1.00 69.61 C
ANISOU 711 CD2 PHE A 114 11213 6204 9030 2517 1083 855 C
ATOM 712 CE1 PHE A 114 57.015 12.803 30.198 1.00 86.26 C
ANISOU 712 CE1 PHE A 114 12544 8839 11391 2541 782 790 C
ATOM 713 CE2 PHE A 114 58.247 14.798 29.783 1.00 68.53 C
ANISOU 713 CE2 PHE A 114 10985 6041 9012 2441 1113 803 C
ATOM 714 CZ PHE A 114 57.874 13.786 30.632 1.00 79.24 C
ANISOU 714 CZ PHE A 114 11955 7666 10488 2473 955 776 C
ATOM 715 N GLY A 115 53.707 15.158 24.614 1.00 67.60 N
ANISOU 715 N GLY A 115 11170 6205 8310 3145 582 923 N
ATOM 716 CA GLY A 115 53.221 15.240 23.250 1.00 74.11 C
ANISOU 716 CA GLY A 115 12183 6988 8986 3260 507 954 C
ATOM 717 C GLY A 115 52.987 13.900 22.567 1.00 72.83 C
ANISOU 717 C GLY A 115 11721 7032 8918 3214 380 970 C
ATOM 718 O GLY A 115 53.307 12.822 23.078 1.00 77.48 O
ANISOU 718 O GLY A 115 11960 7796 9683 3071 362 962 O
ATOM 719 N HIS A 116 52.425 13.991 21.359 1.00 72.72 N
ANISOU 719 N HIS A 116 11889 6978 8762 3341 289 990 N
ATOM 720 CA HIS A 116 51.950 12.805 20.651 1.00 79.40 C
ANISOU 720 CA HIS A 116 12483 8006 9680 3328 141 996 C
ATOM 721 C HIS A 116 53.119 11.905 20.256 1.00 71.43 C
ANISOU 721 C HIS A 116 11432 7005 8705 3129 263 1043 C
ATOM 722 O HIS A 116 53.109 10.680 20.490 1.00 51.72 O
ANISOU 722 O HIS A 116 8570 4709 6371 3018 192 1033 O
ATOM 723 CB HIS A 116 51.180 13.265 19.407 1.00 90.39 C
ANISOU 723 CB HIS A 116 14166 9304 10872 3530 25 1004 C
ATOM 724 CG HIS A 116 49.947 14.063 19.718 1.00 98.56 C
ANISOU 724 CG HIS A 116 15247 10344 11857 3786 -111 951 C
ATOM 725 ND1 HIS A 116 50.007 15.327 20.269 1.00102.15 N
ANISOU 725 ND1 HIS A 116 15935 10633 12242 3853 -33 937 N
ATOM 726 CD2 HIS A 116 48.631 13.798 19.536 1.00100.25 C
ANISOU 726 CD2 HIS A 116 15309 10697 12086 3997 -318 903 C
ATOM 727 CE1 HIS A 116 48.783 15.800 20.426 1.00102.12 C
ANISOU 727 CE1 HIS A 116 15919 10671 12210 4108 -184 884 C
ATOM 728 NE2 HIS A 116 47.929 14.892 19.988 1.00103.90 N
ANISOU 728 NE2 HIS A 116 15897 11082 12496 4200 -362 860 N
ATOM 729 N ALA A 117 54.143 12.509 19.651 1.00 77.60 N
ANISOU 729 N ALA A 117 12607 7550 9327 3078 467 1089 N
ATOM 730 CA ALA A 117 55.277 11.741 19.158 1.00 75.02 C
ANISOU 730 CA ALA A 117 12282 7197 9024 2909 621 1134 C
ATOM 731 C ALA A 117 55.960 10.999 20.296 1.00 83.50 C
ANISOU 731 C ALA A 117 12986 8409 10332 2751 672 1121 C
ATOM 732 O ALA A 117 56.276 9.810 20.179 1.00 89.56 O
ANISOU 732 O ALA A 117 13493 9325 11208 2658 646 1131 O
ATOM 733 CB ALA A 117 56.261 12.661 18.444 1.00 70.11 C
ANISOU 733 CB ALA A 117 12174 6259 8204 2853 890 1173 C
ATOM 734 N LEU A 118 56.211 11.694 21.408 1.00 83.50 N
ANISOU 734 N LEU A 118 12982 8348 10395 2728 743 1095 N
ATOM 735 CA LEU A 118 56.831 11.032 22.549 1.00 67.12 C
ANISOU 735 CA LEU A 118 10581 6395 8528 2601 771 1073 C
ATOM 736 C LEU A 118 55.898 10.020 23.202 1.00 64.70 C
ANISOU 736 C LEU A 118 9839 6388 8357 2615 535 1021 C
ATOM 737 O LEU A 118 56.373 9.022 23.756 1.00 65.67 O
ANISOU 737 O LEU A 118 9677 6655 8618 2503 519 1006 O
ATOM 738 CB LEU A 118 57.257 12.084 23.568 1.00 67.21 C
ANISOU 738 CB LEU A 118 10740 6241 8555 2577 898 1049 C
ATOM 739 CG LEU A 118 58.420 12.931 23.067 1.00 72.93 C
ANISOU 739 CG LEU A 118 11876 6640 9193 2465 1193 1083 C
ATOM 740 CD1 LEU A 118 58.912 13.870 24.162 1.00 77.71 C
ANISOU 740 CD1 LEU A 118 12613 7067 9845 2391 1325 1043 C
ATOM 741 CD2 LEU A 118 59.527 12.012 22.582 1.00 63.21 C
ANISOU 741 CD2 LEU A 118 10542 5400 8075 2312 1351 1121 C
ATOM 742 N CYS A 119 54.578 10.216 23.095 1.00 67.44 N
ANISOU 742 N CYS A 119 10142 6815 8668 2744 366 987 N
ATOM 743 CA CYS A 119 53.661 9.191 23.577 1.00 66.76 C
ANISOU 743 CA CYS A 119 9674 6974 8718 2719 187 933 C
ATOM 744 C CYS A 119 53.822 7.899 22.795 1.00 77.08 C
ANISOU 744 C CYS A 119 10841 8397 10047 2634 138 954 C
ATOM 745 O CYS A 119 53.656 6.808 23.355 1.00 83.61 O
ANISOU 745 O CYS A 119 11395 9408 10965 2560 80 922 O
ATOM 746 CB CYS A 119 52.220 9.700 23.508 1.00 77.84 C
ANISOU 746 CB CYS A 119 11094 8409 10071 2910 67 902 C
ATOM 747 SG CYS A 119 50.913 8.475 23.809 1.00 89.56 S
ANISOU 747 SG CYS A 119 12224 10162 11644 2956 -87 850 S
ATOM 748 N LYS A 120 54.227 7.995 21.527 1.00 84.42 N
ANISOU 748 N LYS A 120 12010 9208 10859 2654 193 1012 N
ATOM 749 CA LYS A 120 54.570 6.744 20.840 1.00 72.71 C
ANISOU 749 CA LYS A 120 10414 7819 9393 2565 178 1034 C
ATOM 750 C LYS A 120 56.004 6.290 21.144 1.00 70.08 C
ANISOU 750 C LYS A 120 10036 7464 9125 2428 341 1058 C
ATOM 751 O LYS A 120 56.248 5.091 21.311 1.00 84.18 O
ANISOU 751 O LYS A 120 11584 9400 11001 2326 297 1039 O
ATOM 752 CB LYS A 120 54.336 6.845 19.326 1.00 59.62 C
ANISOU 752 CB LYS A 120 9028 6058 7565 2660 170 1083 C
ATOM 753 CG LYS A 120 52.851 6.763 18.916 1.00 52.03 C
ANISOU 753 CG LYS A 120 8054 5187 6527 2842 -15 1059 C
ATOM 754 CD LYS A 120 52.686 6.599 17.405 1.00 59.01 C
ANISOU 754 CD LYS A 120 9194 5987 7239 2926 -52 1097 C
ATOM 755 CE LYS A 120 51.227 6.369 16.990 1.00 70.12 C
ANISOU 755 CE LYS A 120 10550 7496 8598 3107 -268 1061 C
ATOM 756 NZ LYS A 120 51.076 5.291 15.958 1.00 75.60 N
ANISOU 756 NZ LYS A 120 11248 8243 9234 3098 -342 1077 N
ATOM 757 N VAL A 121 56.959 7.215 21.243 1.00 64.88 N
ANISOU 757 N VAL A 121 9613 6609 8428 2427 547 1097 N
ATOM 758 CA VAL A 121 58.371 6.827 21.274 1.00 52.91 C
ANISOU 758 CA VAL A 121 8087 5029 6990 2318 757 1136 C
ATOM 759 C VAL A 121 58.758 6.254 22.632 1.00 56.46 C
ANISOU 759 C VAL A 121 8202 5629 7620 2240 713 1089 C
ATOM 760 O VAL A 121 59.416 5.210 22.712 1.00 71.17 O
ANISOU 760 O VAL A 121 9859 7600 9581 2163 735 1091 O
ATOM 761 CB VAL A 121 59.277 8.006 20.895 1.00 49.82 C
ANISOU 761 CB VAL A 121 8080 4324 6524 2302 1042 1183 C
ATOM 762 CG1 VAL A 121 60.720 7.641 21.171 1.00 44.00 C
ANISOU 762 CG1 VAL A 121 7256 3500 5960 2169 1298 1208 C
ATOM 763 CG2 VAL A 121 59.107 8.319 19.431 1.00 48.02 C
ANISOU 763 CG2 VAL A 121 8211 3948 6088 2350 1110 1224 C
ATOM 764 N ILE A 122 58.387 6.935 23.720 1.00 56.51 N
ANISOU 764 N ILE A 122 8173 5637 7663 2267 657 1043 N
ATOM 765 CA ILE A 122 58.836 6.503 25.043 1.00 65.42 C
ANISOU 765 CA ILE A 122 9042 6875 8938 2200 627 997 C
ATOM 766 C ILE A 122 58.321 5.106 25.363 1.00 69.92 C
ANISOU 766 C ILE A 122 9308 7707 9551 2135 430 937 C
ATOM 767 O ILE A 122 59.126 4.252 25.776 1.00 73.40 O
ANISOU 767 O ILE A 122 9568 8236 10084 2057 441 924 O
ATOM 768 CB ILE A 122 58.409 7.529 26.111 1.00 73.09 C
ANISOU 768 CB ILE A 122 10081 7781 9909 2253 606 956 C
ATOM 769 CG1 ILE A 122 59.171 8.850 25.990 1.00 63.23 C
ANISOU 769 CG1 ILE A 122 9165 6226 8633 2265 838 996 C
ATOM 770 CG2 ILE A 122 58.611 6.963 27.502 1.00 80.40 C
ANISOU 770 CG2 ILE A 122 10745 8847 10955 2197 525 896 C
ATOM 771 CD1 ILE A 122 60.673 8.683 26.009 1.00 62.57 C
ANISOU 771 CD1 ILE A 122 9068 5997 8706 2155 1068 1027 C
ATOM 772 N PRO A 123 57.030 4.803 25.216 1.00 59.09 N
ANISOU 772 N PRO A 123 7877 6444 8132 2153 263 893 N
ATOM 773 CA PRO A 123 56.598 3.411 25.408 1.00 52.94 C
ANISOU 773 CA PRO A 123 6877 5858 7381 2073 142 846 C
ATOM 774 C PRO A 123 57.285 2.428 24.470 1.00 61.23 C
ANISOU 774 C PRO A 123 7911 6936 8416 2017 179 882 C
ATOM 775 O PRO A 123 57.573 1.282 24.863 1.00 72.72 O
ANISOU 775 O PRO A 123 9209 8522 9901 1943 152 859 O
ATOM 776 CB PRO A 123 55.090 3.484 25.112 1.00 37.84 C
ANISOU 776 CB PRO A 123 4979 4002 5395 2181 64 848 C
ATOM 777 CG PRO A 123 54.718 4.907 25.387 1.00 44.36 C
ANISOU 777 CG PRO A 123 5945 4701 6210 2278 82 843 C
ATOM 778 CD PRO A 123 55.898 5.712 24.949 1.00 47.64 C
ANISOU 778 CD PRO A 123 6560 4931 6612 2265 208 890 C
ATOM 779 N TYR A 124 57.577 2.852 23.235 1.00 55.02 N
ANISOU 779 N TYR A 124 7319 6021 7567 2066 268 949 N
ATOM 780 CA TYR A 124 58.287 1.977 22.310 1.00 47.92 C
ANISOU 780 CA TYR A 124 6430 5129 6650 2029 346 994 C
ATOM 781 C TYR A 124 59.673 1.631 22.840 1.00 54.45 C
ANISOU 781 C TYR A 124 7139 5962 7589 1975 487 1010 C
ATOM 782 O TYR A 124 60.091 0.466 22.808 1.00 70.37 O
ANISOU 782 O TYR A 124 9006 8088 9641 1911 462 992 O
ATOM 783 CB TYR A 124 58.375 2.615 20.927 1.00 42.58 C
ANISOU 783 CB TYR A 124 6046 4279 5855 2114 470 1077 C
ATOM 784 CG TYR A 124 59.283 1.848 19.987 1.00 48.97 C
ANISOU 784 CG TYR A 124 6905 5054 6648 2087 623 1137 C
ATOM 785 CD1 TYR A 124 58.908 0.598 19.496 1.00 67.69 C
ANISOU 785 CD1 TYR A 124 9171 7555 8994 2048 507 1116 C
ATOM 786 CD2 TYR A 124 60.514 2.363 19.595 1.00 52.38 C
ANISOU 786 CD2 TYR A 124 7498 5294 7109 2090 920 1211 C
ATOM 787 CE1 TYR A 124 59.733 -0.110 18.634 1.00 63.51 C
ANISOU 787 CE1 TYR A 124 8697 6988 8445 2037 662 1173 C
ATOM 788 CE2 TYR A 124 61.339 1.668 18.736 1.00 36.73 C
ANISOU 788 CE2 TYR A 124 5557 3261 5138 2066 1106 1265 C
ATOM 789 CZ TYR A 124 60.945 0.435 18.260 1.00 56.03 C
ANISOU 789 CZ TYR A 124 7896 5860 7533 2053 966 1249 C
ATOM 790 OH TYR A 124 61.761 -0.265 17.407 1.00 59.39 O
ANISOU 790 OH TYR A 124 8373 6228 7963 2042 1164 1303 O
ATOM 791 N LEU A 125 60.407 2.639 23.330 1.00 47.90 N
ANISOU 791 N LEU A 125 6372 4995 6834 2004 642 1042 N
ATOM 792 CA LEU A 125 61.729 2.370 23.881 1.00 50.05 C
ANISOU 792 CA LEU A 125 6475 5257 7286 1958 781 1052 C
ATOM 793 C LEU A 125 61.653 1.540 25.147 1.00 62.99 C
ANISOU 793 C LEU A 125 7851 7103 8980 1897 576 955 C
ATOM 794 O LEU A 125 62.552 0.735 25.399 1.00 80.68 O
ANISOU 794 O LEU A 125 9902 9420 11332 1851 590 935 O
ATOM 795 CB LEU A 125 62.467 3.674 24.149 1.00 51.75 C
ANISOU 795 CB LEU A 125 6821 5226 7616 1980 1016 1090 C
ATOM 796 CG LEU A 125 62.690 4.490 22.887 1.00 46.34 C
ANISOU 796 CG LEU A 125 6489 4268 6851 1998 1274 1167 C
ATOM 797 CD1 LEU A 125 63.411 5.781 23.202 1.00 40.15 C
ANISOU 797 CD1 LEU A 125 5901 3174 6180 1952 1542 1169 C
ATOM 798 CD2 LEU A 125 63.515 3.646 21.953 1.00 38.18 C
ANISOU 798 CD2 LEU A 125 5401 3211 5896 1958 1457 1211 C
ATOM 799 N GLN A 126 60.583 1.685 25.934 1.00 64.07 N
ANISOU 799 N GLN A 126 7986 7316 9040 1894 392 885 N
ATOM 800 CA GLN A 126 60.437 0.817 27.099 1.00 72.75 C
ANISOU 800 CA GLN A 126 8910 8570 10161 1826 224 788 C
ATOM 801 C GLN A 126 60.266 -0.642 26.675 1.00 60.25 C
ANISOU 801 C GLN A 126 7255 7107 8529 1753 135 752 C
ATOM 802 O GLN A 126 60.926 -1.550 27.216 1.00 48.33 O
ANISOU 802 O GLN A 126 5621 5680 7062 1711 93 714 O
ATOM 803 CB GLN A 126 59.248 1.272 27.943 1.00 89.96 C
ANISOU 803 CB GLN A 126 11120 10769 12292 1837 112 734 C
ATOM 804 CG GLN A 126 59.067 0.458 29.191 1.00101.87 C
ANISOU 804 CG GLN A 126 12502 12390 13813 1781 -3 661 C
ATOM 805 CD GLN A 126 60.286 0.540 30.094 1.00118.91 C
ANISOU 805 CD GLN A 126 14573 14541 16065 1787 -2 639 C
ATOM 806 OE1 GLN A 126 60.497 1.546 30.783 1.00130.56 O
ANISOU 806 OE1 GLN A 126 16080 15936 17592 1848 43 655 O
ATOM 807 NE2 GLN A 126 61.105 -0.517 30.086 1.00117.80 N
ANISOU 807 NE2 GLN A 126 14324 14478 15957 1744 -45 607 N
ATOM 808 N ALA A 127 59.421 -0.883 25.664 1.00 56.27 N
ANISOU 808 N ALA A 127 6840 6610 7929 1779 155 811 N
ATOM 809 CA ALA A 127 59.235 -2.254 25.192 1.00 46.36 C
ANISOU 809 CA ALA A 127 5540 5457 6619 1748 139 833 C
ATOM 810 C ALA A 127 60.501 -2.810 24.550 1.00 38.34 C
ANISOU 810 C ALA A 127 4491 4417 5658 1722 217 849 C
ATOM 811 O ALA A 127 60.841 -3.982 24.753 1.00 28.96 O
ANISOU 811 O ALA A 127 3216 3315 4475 1684 189 836 O
ATOM 812 CB ALA A 127 58.070 -2.317 24.201 1.00 46.31 C
ANISOU 812 CB ALA A 127 5635 5451 6507 1799 125 876 C
ATOM 813 N VAL A 128 61.215 -1.985 23.780 1.00 47.93 N
ANISOU 813 N VAL A 128 5786 5504 6920 1759 348 890 N
ATOM 814 CA VAL A 128 62.476 -2.423 23.187 1.00 44.79 C
ANISOU 814 CA VAL A 128 5329 5076 6614 1770 518 947 C
ATOM 815 C VAL A 128 63.495 -2.752 24.270 1.00 44.53 C
ANISOU 815 C VAL A 128 5076 5113 6729 1740 488 879 C
ATOM 816 O VAL A 128 64.278 -3.703 24.133 1.00 62.24 O
ANISOU 816 O VAL A 128 7201 7413 9032 1723 498 854 O
ATOM 817 CB VAL A 128 63.008 -1.385 22.184 1.00 52.60 C
ANISOU 817 CB VAL A 128 6474 5865 7647 1844 796 1065 C
ATOM 818 CG1 VAL A 128 64.436 -1.742 21.790 1.00 56.83 C
ANISOU 818 CG1 VAL A 128 6884 6338 8373 1839 1037 1104 C
ATOM 819 CG2 VAL A 128 62.113 -1.368 20.953 1.00 55.19 C
ANISOU 819 CG2 VAL A 128 7043 6137 7790 1885 789 1114 C
ATOM 820 N SER A 129 63.536 -1.953 25.343 1.00 30.19 N
ANISOU 820 N SER A 129 3205 3289 4977 1748 444 842 N
ATOM 821 CA SER A 129 64.487 -2.230 26.412 1.00 53.83 C
ANISOU 821 CA SER A 129 5989 6357 8106 1734 379 762 C
ATOM 822 C SER A 129 64.178 -3.564 27.082 1.00 62.31 C
ANISOU 822 C SER A 129 7034 7569 9070 1692 149 650 C
ATOM 823 O SER A 129 65.086 -4.376 27.329 1.00 63.50 O
ANISOU 823 O SER A 129 7051 7790 9285 1698 102 586 O
ATOM 824 CB SER A 129 64.461 -1.102 27.441 1.00 71.72 C
ANISOU 824 CB SER A 129 8232 8571 10447 1759 370 751 C
ATOM 825 OG SER A 129 65.248 -1.422 28.577 1.00 80.70 O
ANISOU 825 OG SER A 129 9172 9800 11689 1755 253 661 O
ATOM 826 N VAL A 130 62.891 -3.831 27.330 1.00 53.01 N
ANISOU 826 N VAL A 130 5973 6413 7755 1661 51 652 N
ATOM 827 CA VAL A 130 62.520 -5.107 27.936 1.00 37.53 C
ANISOU 827 CA VAL A 130 3990 4536 5732 1637 -47 644 C
ATOM 828 C VAL A 130 62.903 -6.261 27.018 1.00 41.19 C
ANISOU 828 C VAL A 130 4446 5026 6178 1632 -2 680 C
ATOM 829 O VAL A 130 63.446 -7.281 27.467 1.00 48.69 O
ANISOU 829 O VAL A 130 5332 6019 7149 1639 -74 640 O
ATOM 830 CB VAL A 130 61.015 -5.134 28.270 1.00 33.85 C
ANISOU 830 CB VAL A 130 3613 4094 5154 1619 -73 681 C
ATOM 831 CG1 VAL A 130 60.614 -6.510 28.749 1.00 26.31 C
ANISOU 831 CG1 VAL A 130 2654 3207 4136 1592 -133 683 C
ATOM 832 CG2 VAL A 130 60.690 -4.103 29.330 1.00 56.11 C
ANISOU 832 CG2 VAL A 130 6435 6883 8000 1634 -121 638 C
ATOM 833 N SER A 131 62.641 -6.112 25.714 1.00 41.64 N
ANISOU 833 N SER A 131 4586 5042 6194 1637 112 753 N
ATOM 834 CA SER A 131 62.924 -7.200 24.781 1.00 34.27 C
ANISOU 834 CA SER A 131 3669 4122 5231 1640 164 794 C
ATOM 835 C SER A 131 64.424 -7.469 24.653 1.00 32.08 C
ANISOU 835 C SER A 131 3263 3836 5090 1667 205 740 C
ATOM 836 O SER A 131 64.855 -8.633 24.708 1.00 28.57 O
ANISOU 836 O SER A 131 2771 3433 4650 1682 164 721 O
ATOM 837 CB SER A 131 62.302 -6.862 23.420 1.00 32.13 C
ANISOU 837 CB SER A 131 3535 3793 4878 1657 267 875 C
ATOM 838 OG SER A 131 62.631 -7.805 22.411 1.00 40.00 O
ANISOU 838 OG SER A 131 4570 4784 5846 1671 335 917 O
ATOM 839 N VAL A 132 65.243 -6.417 24.540 1.00 36.47 N
ANISOU 839 N VAL A 132 3746 4342 5770 1683 286 697 N
ATOM 840 CA VAL A 132 66.688 -6.622 24.482 1.00 40.46 C
ANISOU 840 CA VAL A 132 4053 4868 6451 1725 380 661 C
ATOM 841 C VAL A 132 67.175 -7.277 25.763 1.00 55.25 C
ANISOU 841 C VAL A 132 5800 6854 8340 1746 159 508 C
ATOM 842 O VAL A 132 68.002 -8.198 25.729 1.00 75.41 O
ANISOU 842 O VAL A 132 8244 9464 10945 1793 125 440 O
ATOM 843 CB VAL A 132 67.428 -5.299 24.214 1.00 49.39 C
ANISOU 843 CB VAL A 132 5071 5903 7791 1736 625 723 C
ATOM 844 CG1 VAL A 132 68.948 -5.512 24.307 1.00 48.52 C
ANISOU 844 CG1 VAL A 132 4670 5840 7927 1742 719 632 C
ATOM 845 CG2 VAL A 132 67.043 -4.743 22.857 1.00 60.20 C
ANISOU 845 CG2 VAL A 132 6628 7112 9134 1750 879 873 C
ATOM 846 N ALA A 133 66.630 -6.855 26.910 1.00 42.71 N
ANISOU 846 N ALA A 133 4239 5286 6703 1736 20 474 N
ATOM 847 CA ALA A 133 67.097 -7.398 28.181 1.00 44.06 C
ANISOU 847 CA ALA A 133 4315 5539 6885 1790 -167 369 C
ATOM 848 C ALA A 133 66.799 -8.896 28.293 1.00 46.86 C
ANISOU 848 C ALA A 133 4736 5890 7177 1800 -262 390 C
ATOM 849 O ALA A 133 67.684 -9.701 28.637 1.00 51.25 O
ANISOU 849 O ALA A 133 5191 6494 7787 1883 -364 300 O
ATOM 850 CB ALA A 133 66.454 -6.618 29.326 1.00 30.51 C
ANISOU 850 CB ALA A 133 2655 3816 5121 1780 -268 350 C
ATOM 851 N VAL A 134 65.560 -9.299 27.994 1.00 40.60 N
ANISOU 851 N VAL A 134 4107 5056 6263 1732 -226 505 N
ATOM 852 CA VAL A 134 65.210 -10.704 28.198 1.00 30.88 C
ANISOU 852 CA VAL A 134 2944 3825 4963 1733 -294 537 C
ATOM 853 C VAL A 134 65.891 -11.583 27.154 1.00 32.80 C
ANISOU 853 C VAL A 134 3162 4068 5234 1775 -222 552 C
ATOM 854 O VAL A 134 66.295 -12.712 27.457 1.00 41.25 O
ANISOU 854 O VAL A 134 4219 5131 6322 1823 -310 527 O
ATOM 855 CB VAL A 134 63.687 -10.926 28.207 1.00 40.70 C
ANISOU 855 CB VAL A 134 4338 5074 6051 1664 -256 633 C
ATOM 856 CG1 VAL A 134 63.105 -10.736 26.826 1.00 63.20 C
ANISOU 856 CG1 VAL A 134 7260 7924 8828 1637 -110 715 C
ATOM 857 CG2 VAL A 134 63.367 -12.317 28.734 1.00 30.93 C
ANISOU 857 CG2 VAL A 134 3165 3842 4746 1668 -329 653 C
ATOM 858 N LEU A 135 66.037 -11.100 25.911 1.00 48.23 N
ANISOU 858 N LEU A 135 5121 6007 7199 1764 -59 600 N
ATOM 859 CA LEU A 135 66.771 -11.910 24.937 1.00 47.02 C
ANISOU 859 CA LEU A 135 4939 5842 7085 1814 25 607 C
ATOM 860 C LEU A 135 68.242 -12.036 25.311 1.00 48.82 C
ANISOU 860 C LEU A 135 4957 6109 7482 1908 -32 463 C
ATOM 861 O LEU A 135 68.851 -13.087 25.080 1.00 64.66 O
ANISOU 861 O LEU A 135 6922 8119 9529 1982 -54 428 O
ATOM 862 CB LEU A 135 66.625 -11.360 23.516 1.00 34.56 C
ANISOU 862 CB LEU A 135 3432 4213 5486 1790 223 693 C
ATOM 863 CG LEU A 135 65.256 -11.528 22.846 1.00 32.10 C
ANISOU 863 CG LEU A 135 3319 3883 4994 1741 267 813 C
ATOM 864 CD1 LEU A 135 65.267 -10.916 21.447 1.00 38.62 C
ANISOU 864 CD1 LEU A 135 4233 4633 5809 1747 442 882 C
ATOM 865 CD2 LEU A 135 64.816 -12.979 22.799 1.00 28.56 C
ANISOU 865 CD2 LEU A 135 2952 3463 4437 1750 216 845 C
ATOM 866 N THR A 136 68.839 -10.991 25.889 1.00 33.28 N
ANISOU 866 N THR A 136 2844 4194 5608 1924 -55 364 N
ATOM 867 CA THR A 136 70.235 -11.120 26.287 1.00 35.55 C
ANISOU 867 CA THR A 136 2896 4595 6015 2040 -112 206 C
ATOM 868 C THR A 136 70.380 -12.153 27.398 1.00 49.87 C
ANISOU 868 C THR A 136 4731 6432 7787 2110 -350 135 C
ATOM 869 O THR A 136 71.303 -12.974 27.365 1.00 72.00 O
ANISOU 869 O THR A 136 7439 9292 10627 2207 -393 55 O
ATOM 870 CB THR A 136 70.804 -9.772 26.728 1.00 75.97 C
ANISOU 870 CB THR A 136 7851 9817 11197 2032 -63 147 C
ATOM 871 OG1 THR A 136 70.885 -8.891 25.602 1.00 88.39 O
ANISOU 871 OG1 THR A 136 9384 11291 12910 1939 223 256 O
ATOM 872 CG2 THR A 136 72.188 -9.954 27.337 1.00 80.41 C
ANISOU 872 CG2 THR A 136 8140 10585 11826 2159 -108 56 C
ATOM 873 N LEU A 137 69.492 -12.127 28.401 1.00 39.35 N
ANISOU 873 N LEU A 137 3540 5035 6378 2039 -486 173 N
ATOM 874 CA LEU A 137 69.543 -13.179 29.422 1.00 43.58 C
ANISOU 874 CA LEU A 137 4122 5480 6956 2026 -686 155 C
ATOM 875 C LEU A 137 69.298 -14.572 28.827 1.00 54.84 C
ANISOU 875 C LEU A 137 5619 6811 8407 2031 -653 275 C
ATOM 876 O LEU A 137 69.932 -15.557 29.244 1.00 37.07 O
ANISOU 876 O LEU A 137 3301 4485 6301 2054 -735 316 O
ATOM 877 CB LEU A 137 68.531 -12.892 30.532 1.00 34.40 C
ANISOU 877 CB LEU A 137 3071 4224 5773 1908 -769 253 C
ATOM 878 CG LEU A 137 68.795 -11.636 31.363 1.00 34.79 C
ANISOU 878 CG LEU A 137 3087 4367 5765 1932 -840 119 C
ATOM 879 CD1 LEU A 137 67.643 -11.331 32.300 1.00 36.16 C
ANISOU 879 CD1 LEU A 137 3350 4398 5990 1776 -867 282 C
ATOM 880 CD2 LEU A 137 70.080 -11.784 32.147 1.00 49.10 C
ANISOU 880 CD2 LEU A 137 4696 6664 7297 2143 -407 754 C
ATOM 881 N SER A 138 68.388 -14.682 27.849 1.00 42.92 N
ANISOU 881 N SER A 138 4235 5303 6768 2018 -512 381 N
ATOM 882 CA SER A 138 68.153 -15.975 27.207 1.00 47.44 C
ANISOU 882 CA SER A 138 4921 5844 7259 2037 -455 475 C
ATOM 883 C SER A 138 69.414 -16.481 26.523 1.00 59.83 C
ANISOU 883 C SER A 138 6344 7408 8979 2156 -431 388 C
ATOM 884 O SER A 138 69.763 -17.658 26.634 1.00 67.56 O
ANISOU 884 O SER A 138 7335 8335 10002 2226 -491 413 O
ATOM 885 CB SER A 138 66.995 -15.888 26.216 1.00 56.12 C
ANISOU 885 CB SER A 138 6195 6968 8159 1949 -281 598 C
ATOM 886 OG SER A 138 65.756 -15.819 26.903 1.00 73.18 O
ANISOU 886 OG SER A 138 8482 9141 10181 1866 -315 658 O
ATOM 887 N PHE A 139 70.087 -15.612 25.770 1.00 60.85 N
ANISOU 887 N PHE A 139 6340 7605 9177 2185 -308 302 N
ATOM 888 CA PHE A 139 71.287 -16.037 25.056 1.00 57.61 C
ANISOU 888 CA PHE A 139 5769 7227 8894 2309 -241 196 C
ATOM 889 C PHE A 139 72.441 -16.311 26.009 1.00 61.12 C
ANISOU 889 C PHE A 139 6039 7729 9454 2388 -417 25 C
ATOM 890 O PHE A 139 73.266 -17.192 25.741 1.00 71.87 O
ANISOU 890 O PHE A 139 7309 9074 10925 2487 -435 -44 O
ATOM 891 CB PHE A 139 71.672 -14.995 24.006 1.00 61.36 C
ANISOU 891 CB PHE A 139 6157 7767 9390 2276 6 191 C
ATOM 892 CG PHE A 139 70.790 -15.008 22.787 1.00 70.49 C
ANISOU 892 CG PHE A 139 7530 8828 10423 2175 208 375 C
ATOM 893 CD1 PHE A 139 69.495 -15.508 22.848 1.00 76.64 C
ANISOU 893 CD1 PHE A 139 8549 9555 11015 2101 161 522 C
ATOM 894 CD2 PHE A 139 71.239 -14.467 21.591 1.00 82.30 C
ANISOU 894 CD2 PHE A 139 8991 10303 11976 2157 457 391 C
ATOM 895 CE1 PHE A 139 68.688 -15.515 21.727 1.00 87.76 C
ANISOU 895 CE1 PHE A 139 10147 10916 12284 2039 319 664 C
ATOM 896 CE2 PHE A 139 70.435 -14.462 20.469 1.00 94.04 C
ANISOU 896 CE2 PHE A 139 10704 11691 13334 2092 620 551 C
ATOM 897 CZ PHE A 139 69.156 -14.984 20.537 1.00 96.32 C
ANISOU 897 CZ PHE A 139 11219 11953 13423 2043 532 682 C
ATOM 898 N ILE A 140 72.479 -15.630 27.156 1.00 58.85 N
ANISOU 898 N ILE A 140 5723 7503 9134 2358 -563 -45 N
ATOM 899 CA ILE A 140 73.480 -15.967 28.162 1.00 56.61 C
ANISOU 899 CA ILE A 140 5334 7308 8867 2477 -770 -213 C
ATOM 900 C ILE A 140 73.236 -17.382 28.668 1.00 61.25 C
ANISOU 900 C ILE A 140 5812 7487 9973 2261 -580 484 C
ATOM 901 O ILE A 140 74.157 -18.207 28.739 1.00 72.50 O
ANISOU 901 O ILE A 140 7125 9024 11398 2455 -475 669 O
ATOM 902 CB ILE A 140 73.446 -14.944 29.314 1.00 57.28 C
ANISOU 902 CB ILE A 140 5369 7855 8539 2579 -270 620 C
ATOM 903 CG1 ILE A 140 74.015 -13.591 28.866 1.00 74.53 C
ANISOU 903 CG1 ILE A 140 7364 10156 10800 2581 -342 247 C
ATOM 904 CG2 ILE A 140 74.231 -15.470 30.513 1.00 54.96 C
ANISOU 904 CG2 ILE A 140 4809 7365 8706 2541 -448 753 C
ATOM 905 CD1 ILE A 140 73.890 -12.481 29.912 1.00 44.11 C
ANISOU 905 CD1 ILE A 140 3410 6314 7036 2480 -372 355 C
ATOM 906 N ALA A 141 71.978 -17.685 29.016 1.00 60.36 N
ANISOU 906 N ALA A 141 5980 7360 9594 2239 -700 474 N
ATOM 907 CA ALA A 141 71.637 -19.027 29.485 1.00 64.29 C
ANISOU 907 CA ALA A 141 6649 7862 9915 2362 -759 616 C
ATOM 908 C ALA A 141 71.872 -20.081 28.407 1.00 68.44 C
ANISOU 908 C ALA A 141 7226 8339 10439 2465 -716 557 C
ATOM 909 O ALA A 141 72.271 -21.202 28.718 1.00 72.83 O
ANISOU 909 O ALA A 141 7819 8885 10967 2622 -766 634 O
ATOM 910 CB ALA A 141 70.183 -19.072 29.959 1.00 73.79 C
ANISOU 910 CB ALA A 141 8119 9060 10857 2286 -810 660 C
ATOM 911 N LEU A 142 71.635 -19.737 27.139 1.00 72.15 N
ANISOU 911 N LEU A 142 7730 8812 10872 2433 -617 425 N
ATOM 912 CA LEU A 142 71.828 -20.693 26.052 1.00 63.19 C
ANISOU 912 CA LEU A 142 6656 7651 9703 2548 -526 417 C
ATOM 913 C LEU A 142 73.312 -20.984 25.872 1.00 69.93 C
ANISOU 913 C LEU A 142 7253 8488 10829 2658 -517 310 C
ATOM 914 O LEU A 142 73.710 -22.143 25.689 1.00 75.99 O
ANISOU 914 O LEU A 142 8044 9205 11623 2797 -510 365 O
ATOM 915 CB LEU A 142 71.177 -20.164 24.769 1.00 52.53 C
ANISOU 915 CB LEU A 142 5432 6358 8171 2479 -335 416 C
ATOM 916 CG LEU A 142 71.019 -21.070 23.551 1.00 39.76 C
ANISOU 916 CG LEU A 142 3975 4719 6412 2522 -171 492 C
ATOM 917 CD1 LEU A 142 69.940 -22.083 23.835 1.00 38.39 C
ANISOU 917 CD1 LEU A 142 4079 4524 5983 2483 -202 634 C
ATOM 918 CD2 LEU A 142 70.612 -20.234 22.356 1.00 38.35 C
ANISOU 918 CD2 LEU A 142 3854 4575 6143 2434 42 536 C
ATOM 919 N ASP A 143 74.146 -19.941 25.928 1.00 78.46 N
ANISOU 919 N ASP A 143 8084 9619 12109 2610 -517 137 N
ATOM 920 CA ASP A 143 75.588 -20.141 25.823 1.00 84.43 C
ANISOU 920 CA ASP A 143 8529 10344 13208 2677 -467 65 C
ATOM 921 C ASP A 143 76.096 -20.984 26.981 1.00 72.52 C
ANISOU 921 C ASP A 143 6952 8894 11709 2844 -395 517 C
ATOM 922 O ASP A 143 76.890 -21.911 26.783 1.00 69.89 O
ANISOU 922 O ASP A 143 6540 8573 11443 3045 -369 533 O
ATOM 923 CB ASP A 143 76.312 -18.789 25.793 1.00 89.80 C
ANISOU 923 CB ASP A 143 9150 11522 13446 2882 -605 -455 C
ATOM 924 CG ASP A 143 77.825 -18.918 26.009 1.00 83.53 C
ANISOU 924 CG ASP A 143 8101 11242 12394 3260 112 544 C
ATOM 925 OD1 ASP A 143 78.249 -18.879 27.186 1.00 76.91 O
ANISOU 925 OD1 ASP A 143 7021 10267 11934 3206 -55 619 O
ATOM 926 OD2 ASP A 143 78.589 -19.061 25.025 1.00 80.02 O
ANISOU 926 OD2 ASP A 143 7568 10992 11846 3442 97 176 O
ATOM 927 N ARG A 144 75.625 -20.696 28.195 1.00 70.12 N
ANISOU 927 N ARG A 144 6744 8695 11203 2859 -524 639 N
ATOM 928 CA ARG A 144 76.039 -21.480 29.352 1.00 73.75 C
ANISOU 928 CA ARG A 144 7229 9242 11550 3104 -743 679 C
ATOM 929 C ARG A 144 75.530 -22.916 29.259 1.00 77.63 C
ANISOU 929 C ARG A 144 7985 9592 11917 3204 -857 671 C
ATOM 930 O ARG A 144 76.226 -23.857 29.656 1.00 84.90 O
ANISOU 930 O ARG A 144 8930 10536 12793 3420 -983 639 O
ATOM 931 CB ARG A 144 75.546 -20.791 30.618 1.00 74.09 C
ANISOU 931 CB ARG A 144 7345 9367 11438 3061 -906 709 C
ATOM 932 CG ARG A 144 76.268 -19.477 30.885 1.00 79.54 C
ANISOU 932 CG ARG A 144 7767 10256 12199 3055 -855 687 C
ATOM 933 CD ARG A 144 77.781 -19.663 31.080 1.00 84.86 C
ANISOU 933 CD ARG A 144 8122 11082 13038 3300 -950 593 C
ATOM 934 NE ARG A 144 78.562 -19.646 29.844 1.00 87.25 N
ANISOU 934 NE ARG A 144 8220 11458 13474 3349 -691 572 N
ATOM 935 CZ ARG A 144 79.756 -20.223 29.718 1.00101.13 C
ANISOU 935 CZ ARG A 144 9723 13292 15409 3575 -734 492 C
ATOM 936 NH1 ARG A 144 80.293 -20.857 30.751 1.00102.80 N
ANISOU 936 NH1 ARG A 144 9915 13499 15644 3726 -1056 390 N
ATOM 937 NH2 ARG A 144 80.417 -20.170 28.568 1.00113.58 N
ANISOU 937 NH2 ARG A 144 11134 14954 17066 3621 -470 458 N
ATOM 938 N TRP A 145 74.326 -23.109 28.722 1.00 71.24 N
ANISOU 938 N TRP A 145 7438 8683 10946 3046 -820 658 N
ATOM 939 CA TRP A 145 73.758 -24.448 28.641 1.00 60.76 C
ANISOU 939 CA TRP A 145 6450 7303 9332 3118 -873 663 C
ATOM 940 C TRP A 145 74.498 -25.314 27.639 1.00 54.24 C
ANISOU 940 C TRP A 145 5565 6419 8626 3266 -790 616 C
ATOM 941 O TRP A 145 74.728 -26.502 27.892 1.00 53.84 O
ANISOU 941 O TRP A 145 5688 6344 8425 3441 -871 625 O
ATOM 942 CB TRP A 145 72.272 -24.370 28.293 1.00 61.08 C
ANISOU 942 CB TRP A 145 6773 7324 9110 2929 -811 688 C
ATOM 943 CG TRP A 145 71.609 -25.692 28.331 1.00 56.22 C
ANISOU 943 CG TRP A 145 6510 6674 8175 2987 -826 728 C
ATOM 944 CD1 TRP A 145 71.213 -26.400 29.424 1.00 61.32 C
ANISOU 944 CD1 TRP A 145 7408 7313 8577 3044 -950 754 C
ATOM 945 CD2 TRP A 145 71.225 -26.461 27.188 1.00 57.17 C
ANISOU 945 CD2 TRP A 145 6799 6754 8167 2990 -695 739 C
ATOM 946 NE1 TRP A 145 70.634 -27.590 29.031 1.00 62.53 N
ANISOU 946 NE1 TRP A 145 7866 7410 8481 3080 -900 777 N
ATOM 947 CE2 TRP A 145 70.622 -27.644 27.662 1.00 60.87 C
ANISOU 947 CE2 TRP A 145 7605 7188 8336 3045 -742 780 C
ATOM 948 CE3 TRP A 145 71.340 -26.264 25.804 1.00 44.74 C
ANISOU 948 CE3 TRP A 145 5150 5169 6680 2959 -535 711 C
ATOM 949 CZ2 TRP A 145 70.134 -28.624 26.805 1.00 60.75 C
ANISOU 949 CZ2 TRP A 145 7829 7126 8127 3060 -632 810 C
ATOM 950 CZ3 TRP A 145 70.859 -27.234 24.955 1.00 44.23 C
ANISOU 950 CZ3 TRP A 145 5334 5070 6402 2983 -427 754 C
ATOM 951 CH2 TRP A 145 70.266 -28.404 25.456 1.00 61.80 C
ANISOU 951 CH2 TRP A 145 7871 7260 8352 3028 -476 806 C
ATOM 952 N TYR A 146 74.871 -24.750 26.491 1.00 57.66 N
ANISOU 952 N TYR A 146 5781 6815 9311 3209 -633 533 N
ATOM 953 CA TYR A 146 75.672 -25.533 25.560 1.00 57.81 C
ANISOU 953 CA TYR A 146 5720 6777 9470 3365 -539 460 C
ATOM 954 C TYR A 146 77.098 -25.726 26.072 1.00 73.25 C
ANISOU 954 C TYR A 146 7363 8771 11698 3571 -558 470 C
ATOM 955 O TYR A 146 77.670 -26.812 25.915 1.00 93.27 O
ANISOU 955 O TYR A 146 9930 11268 14240 3787 -578 457 O
ATOM 956 CB TYR A 146 75.661 -24.867 24.187 1.00 59.36 C
ANISOU 956 CB TYR A 146 5834 6965 9754 3260 -369 296 C
ATOM 957 CG TYR A 146 74.433 -25.218 23.367 1.00 63.58 C
ANISOU 957 CG TYR A 146 6748 7507 9902 3178 -274 372 C
ATOM 958 CD1 TYR A 146 74.281 -26.480 22.798 1.00 60.86 C
ANISOU 958 CD1 TYR A 146 6647 7115 9364 3281 -207 442 C
ATOM 959 CD2 TYR A 146 73.420 -24.283 23.167 1.00 70.85 C
ANISOU 959 CD2 TYR A 146 7788 8488 10643 2989 -222 410 C
ATOM 960 CE1 TYR A 146 73.151 -26.799 22.050 1.00 56.59 C
ANISOU 960 CE1 TYR A 146 6438 6578 8485 3180 -85 556 C
ATOM 961 CE2 TYR A 146 72.294 -24.592 22.421 1.00 64.67 C
ANISOU 961 CE2 TYR A 146 7318 7714 9539 2897 -95 538 C
ATOM 962 CZ TYR A 146 72.167 -25.847 21.865 1.00 57.35 C
ANISOU 962 CZ TYR A 146 6608 6734 8449 2985 -29 608 C
ATOM 963 OH TYR A 146 71.045 -26.136 21.128 1.00 59.94 O
ANISOU 963 OH TYR A 146 7223 7062 8489 2883 94 727 O
ATOM 964 N ALA A 147 77.695 -24.688 26.686 1.00 68.28 N
ANISOU 964 N ALA A 147 6468 8268 11206 3527 -535 508 N
ATOM 965 CA ALA A 147 79.072 -24.787 27.176 1.00 72.33 C
ANISOU 965 CA ALA A 147 6685 8927 11871 3784 -552 528 C
ATOM 966 C ALA A 147 79.206 -25.795 28.309 1.00 80.71 C
ANISOU 966 C ALA A 147 7916 10003 12747 4019 -869 512 C
ATOM 967 O ALA A 147 80.258 -26.434 28.463 1.00 81.19 O
ANISOU 967 O ALA A 147 7832 10111 12904 4275 -952 447 O
ATOM 968 CB ALA A 147 79.563 -23.415 27.635 1.00 73.09 C
ANISOU 968 CB ALA A 147 6523 9251 11996 3734 -495 556 C
ATOM 969 N ILE A 148 78.148 -25.957 29.098 1.00 84.10 N
ANISOU 969 N ILE A 148 8696 10396 12862 3914 -1045 536 N
ATOM 970 CA ILE A 148 78.196 -26.711 30.338 1.00 82.45 C
ANISOU 970 CA ILE A 148 8724 10202 12402 4078 -1345 491 C
ATOM 971 C ILE A 148 77.473 -28.039 30.215 1.00 84.95 C
ANISOU 971 C ILE A 148 9469 10385 12423 4131 -1387 506 C
ATOM 972 O ILE A 148 77.909 -29.036 30.789 1.00 87.44 O
ANISOU 972 O ILE A 148 9949 10670 12604 4361 -1576 454 O
ATOM 973 CB ILE A 148 77.634 -25.883 31.515 1.00 63.85 C
ANISOU 973 CB ILE A 148 6463 7912 9886 3948 -1501 495 C
ATOM 974 CG1 ILE A 148 78.603 -24.758 31.874 1.00 71.60 C
ANISOU 974 CG1 ILE A 148 7047 9054 11102 3971 -1539 440 C
ATOM 975 CG2 ILE A 148 77.284 -26.770 32.708 1.00 64.87 C
ANISOU 975 CG2 ILE A 148 6978 7983 9687 4065 -1774 451 C
ATOM 976 CD1 ILE A 148 78.606 -23.586 30.930 1.00 80.22 C
ANISOU 976 CD1 ILE A 148 7855 10211 12413 3793 -1245 505 C
ATOM 977 N CYS A 149 76.381 -28.080 29.452 1.00 86.21 N
ANISOU 977 N CYS A 149 9826 10472 12458 3932 -1217 567 N
ATOM 978 CA CYS A 149 75.541 -29.266 29.419 1.00 81.29 C
ANISOU 978 CA CYS A 149 9645 9757 11484 3955 -1240 591 C
ATOM 979 C CYS A 149 75.721 -30.114 28.170 1.00 60.48 C
ANISOU 979 C CYS A 149 7059 7042 8878 4034 -1085 588 C
ATOM 980 O CYS A 149 75.589 -31.340 28.265 1.00 61.69 O
ANISOU 980 O CYS A 149 7532 7123 8785 4177 -1143 589 O
ATOM 981 CB CYS A 149 74.069 -28.874 29.591 1.00 95.11 C
ANISOU 981 CB CYS A 149 11644 11505 12989 3699 -1182 653 C
ATOM 982 SG CYS A 149 73.745 -28.139 31.232 1.00 94.34 S
ANISOU 982 SG CYS A 149 11601 11467 12777 3638 -1377 644 S
ATOM 983 N HIS A 150 75.973 -29.535 26.990 1.00 59.67 N
ANISOU 983 N HIS A 150 6697 6935 9041 3948 -885 570 N
ATOM 984 CA HIS A 150 76.203 -30.353 25.798 1.00 77.91 C
ANISOU 984 CA HIS A 150 9072 9164 11367 4041 -738 545 C
ATOM 985 C HIS A 150 77.383 -29.877 24.954 1.00 93.21 C
ANISOU 985 C HIS A 150 10575 11090 13749 4116 -594 449 C
ATOM 986 O HIS A 150 77.219 -29.264 23.890 1.00 88.98 O
ANISOU 986 O HIS A 150 9936 10536 13336 3975 -413 390 O
ATOM 987 CB HIS A 150 74.921 -30.443 24.959 1.00 74.63 C
ANISOU 987 CB HIS A 150 8958 8723 10674 3842 -592 602 C
ATOM 988 CG HIS A 150 73.740 -30.961 25.724 1.00 83.59 C
ANISOU 988 CG HIS A 150 10491 9858 11412 3759 -679 681 C
ATOM 989 ND1 HIS A 150 73.122 -30.239 26.722 1.00 90.78 N
ANISOU 989 ND1 HIS A 150 11411 10827 12254 3619 -779 705 N
ATOM 990 CD2 HIS A 150 73.081 -32.143 25.649 1.00 91.40 C
ANISOU 990 CD2 HIS A 150 11882 10781 12063 3799 -664 726 C
ATOM 991 CE1 HIS A 150 72.135 -30.954 27.231 1.00 93.10 C
ANISOU 991 CE1 HIS A 150 12080 11089 12204 3576 -815 749 C
ATOM 992 NE2 HIS A 150 72.085 -32.112 26.595 1.00 90.85 N
ANISOU 992 NE2 HIS A 150 12040 10728 11753 3677 -746 761 N
ATOM 993 N PRO A 151 78.595 -30.104 25.447 1.00107.96 N
ANISOU 993 N PRO A 151 12186 12983 15852 4347 -672 410 N
ATOM 994 CA PRO A 151 79.766 -29.366 24.967 1.00109.41 C
ANISOU 994 CA PRO A 151 11864 13194 16513 4395 -510 339 C
ATOM 995 C PRO A 151 80.221 -29.835 23.583 1.00115.19 C
ANISOU 995 C PRO A 151 12508 13814 17444 4460 -288 220 C
ATOM 996 O PRO A 151 79.834 -30.899 23.096 1.00117.90 O
ANISOU 996 O PRO A 151 13184 14082 17529 4541 -289 219 O
ATOM 997 CB PRO A 151 80.839 -29.655 26.026 1.00109.61 C
ANISOU 997 CB PRO A 151 11709 13329 16609 4671 -694 343 C
ATOM 998 CG PRO A 151 80.370 -30.877 26.731 1.00113.80 C
ANISOU 998 CG PRO A 151 12685 13809 16746 4812 -944 354 C
ATOM 999 CD PRO A 151 78.879 -30.807 26.710 1.00114.58 C
ANISOU 999 CD PRO A 151 13174 13860 16500 4554 -936 427 C
ATOM 1000 N LEU A 152 81.063 -29.020 22.952 1.00116.68 N
ANISOU 1000 N LEU A 152 12311 14034 17987 4381 -73 107 N
ATOM 1001 CA LEU A 152 81.502 -29.083 21.551 1.00113.99 C
ANISOU 1001 CA LEU A 152 11867 13631 17813 4348 143 -129 C
ATOM 1002 C LEU A 152 80.435 -29.035 20.458 1.00113.73 C
ANISOU 1002 C LEU A 152 12167 13591 17456 4235 192 -240 C
ATOM 1003 O LEU A 152 80.770 -29.267 19.288 1.00104.55 O
ANISOU 1003 O LEU A 152 11004 12437 16284 4313 370 -411 O
ATOM 1004 CB LEU A 152 82.403 -30.313 21.331 1.00110.65 C
ANISOU 1004 CB LEU A 152 11382 13135 17525 4667 197 -142 C
ATOM 1005 CG LEU A 152 83.783 -30.234 21.999 1.00114.77 C
ANISOU 1005 CG LEU A 152 11502 13768 18336 4890 274 -30 C
ATOM 1006 CD1 LEU A 152 83.673 -30.066 23.514 1.00109.72 C
ANISOU 1006 CD1 LEU A 152 10884 13283 17523 5020 -20 141 C
ATOM 1007 CD2 LEU A 152 84.647 -31.447 21.656 1.00121.75 C
ANISOU 1007 CD2 LEU A 152 12326 14577 19356 5228 320 -97 C
ATOM 1008 N LEU A 153 79.165 -28.756 20.754 1.00124.50 N
ANISOU 1008 N LEU A 153 13830 14964 18511 4093 101 -83 N
ATOM 1009 CA LEU A 153 78.178 -28.895 19.684 1.00124.23 C
ANISOU 1009 CA LEU A 153 14186 14947 18070 3988 256 -5 C
ATOM 1010 C LEU A 153 78.169 -27.630 18.832 1.00116.60 C
ANISOU 1010 C LEU A 153 13093 14093 17117 3849 434 -135 C
ATOM 1011 O LEU A 153 78.136 -27.712 17.597 1.00111.27 O
ANISOU 1011 O LEU A 153 12555 13420 16303 3848 689 -124 O
ATOM 1012 CB LEU A 153 76.781 -29.187 20.230 1.00117.73 C
ANISOU 1012 CB LEU A 153 13775 14122 16836 3850 149 238 C
ATOM 1013 CG LEU A 153 76.425 -30.655 20.481 1.00116.69 C
ANISOU 1013 CG LEU A 153 13997 13916 16424 3977 82 373 C
ATOM 1014 CD1 LEU A 153 77.356 -31.276 21.509 1.00126.95 C
ANISOU 1014 CD1 LEU A 153 15137 15186 17914 4199 -98 338 C
ATOM 1015 CD2 LEU A 153 74.982 -30.787 20.921 1.00109.54 C
ANISOU 1015 CD2 LEU A 153 13464 13038 15118 3806 14 539 C
ATOM 1016 N PHE A 154 78.230 -26.468 19.477 1.00108.75 N
ANISOU 1016 N PHE A 154 11867 13195 16259 3743 328 -233 N
ATOM 1017 CA PHE A 154 78.154 -25.149 18.857 1.00109.66 C
ANISOU 1017 CA PHE A 154 11908 13469 16290 3620 493 -318 C
ATOM 1018 C PHE A 154 79.312 -24.331 19.408 1.00116.78 C
ANISOU 1018 C PHE A 154 12421 14584 17368 3658 408 -586 C
ATOM 1019 O PHE A 154 79.615 -24.389 20.606 1.00114.31 O
ANISOU 1019 O PHE A 154 11967 14230 17236 3625 149 -630 O
ATOM 1020 CB PHE A 154 76.828 -24.410 19.108 1.00102.13 C
ANISOU 1020 CB PHE A 154 11206 12513 15084 3389 466 -103 C
ATOM 1021 CG PHE A 154 75.607 -25.076 18.524 1.00 89.70 C
ANISOU 1021 CG PHE A 154 10066 10835 13180 3294 560 168 C
ATOM 1022 CD1 PHE A 154 75.228 -24.788 17.225 1.00 77.03 C
ANISOU 1022 CD1 PHE A 154 8642 9206 11419 3209 836 267 C
ATOM 1023 CD2 PHE A 154 74.810 -25.928 19.272 1.00 91.67 C
ANISOU 1023 CD2 PHE A 154 10549 11026 13254 3281 384 319 C
ATOM 1024 CE1 PHE A 154 74.098 -25.350 16.667 1.00 70.80 C
ANISOU 1024 CE1 PHE A 154 8233 8339 10330 3128 901 482 C
ATOM 1025 CE2 PHE A 154 73.668 -26.497 18.712 1.00 86.02 C
ANISOU 1025 CE2 PHE A 154 10211 10268 12203 3197 470 514 C
ATOM 1026 CZ PHE A 154 73.317 -26.205 17.407 1.00 74.85 C
ANISOU 1026 CZ PHE A 154 8944 8831 10663 3123 713 586 C
ATOM 1027 N LYS A 155 79.984 -23.619 18.509 1.00121.47 N
ANISOU 1027 N LYS A 155 12850 15394 17908 3716 680 -702 N
ATOM 1028 CA LYS A 155 81.083 -22.733 18.855 1.00123.72 C
ANISOU 1028 CA LYS A 155 12808 16046 18154 3817 721 -834 C
ATOM 1029 C LYS A 155 80.556 -21.373 19.291 1.00117.33 C
ANISOU 1029 C LYS A 155 11988 15336 17256 3634 742 -725 C
ATOM 1030 O LYS A 155 79.721 -20.771 18.604 1.00118.77 O
ANISOU 1030 O LYS A 155 12313 15368 17446 3455 934 -616 O
ATOM 1031 CB LYS A 155 82.010 -22.539 17.662 1.00133.20 C
ANISOU 1031 CB LYS A 155 13787 17362 19463 3914 1143 -879 C
ATOM 1032 CG LYS A 155 81.281 -21.998 16.430 1.00137.40 C
ANISOU 1032 CG LYS A 155 14532 17656 20018 3661 1529 -707 C
ATOM 1033 CD LYS A 155 82.180 -21.962 15.207 1.00148.04 C
ANISOU 1033 CD LYS A 155 15751 18985 21515 3661 1988 -733 C
ATOM 1034 CE LYS A 155 82.909 -20.611 15.172 1.00152.59 C
ANISOU 1034 CE LYS A 155 16003 19697 22278 3499 2253 -759 C
ATOM 1035 NZ LYS A 155 83.811 -20.442 14.003 1.00151.13 N
ANISOU 1035 NZ LYS A 155 15679 19448 22295 3424 2740 -815 N
ATOM 1036 N SER A 156 81.054 -20.881 20.421 1.00116.48 N
ANISOU 1036 N SER A 156 11723 15494 17040 3724 601 -673 N
ATOM 1037 CA SER A 156 80.622 -19.596 20.958 1.00115.81 C
ANISOU 1037 CA SER A 156 11598 15476 16928 3546 617 -564 C
ATOM 1038 C SER A 156 81.863 -18.719 20.949 1.00131.92 C
ANISOU 1038 C SER A 156 13177 17737 19211 3573 878 -526 C
ATOM 1039 O SER A 156 82.715 -18.825 21.839 1.00135.40 O
ANISOU 1039 O SER A 156 13373 18330 19744 3708 812 -408 O
ATOM 1040 CB SER A 156 80.065 -19.734 22.375 1.00104.89 C
ANISOU 1040 CB SER A 156 10398 14134 15321 3580 308 -431 C
ATOM 1041 OG SER A 156 78.913 -20.556 22.420 1.00104.60 O
ANISOU 1041 OG SER A 156 10670 13716 15357 3422 14 -600 O
ATOM 1042 N THR A 157 81.931 -17.814 19.978 1.00142.55 N
ANISOU 1042 N THR A 157 14387 18988 20786 3363 1206 -594 N
ATOM 1043 CA THR A 157 83.056 -16.902 19.863 1.00138.61 C
ANISOU 1043 CA THR A 157 13466 18563 20636 3219 1462 -653 C
ATOM 1044 C THR A 157 82.560 -15.485 20.106 1.00126.68 C
ANISOU 1044 C THR A 157 11962 16959 19213 2910 1522 -619 C
ATOM 1045 O THR A 157 81.372 -15.189 19.941 1.00131.09 O
ANISOU 1045 O THR A 157 12862 17357 19589 2795 1489 -525 O
ATOM 1046 CB THR A 157 83.717 -16.995 18.480 1.00141.93 C
ANISOU 1046 CB THR A 157 13786 18877 21263 3141 1875 -757 C
ATOM 1047 OG1 THR A 157 82.775 -16.622 17.463 1.00136.91 O
ANISOU 1047 OG1 THR A 157 13501 17967 20551 2922 2110 -677 O
ATOM 1048 CG2 THR A 157 84.224 -18.402 18.215 1.00146.33 C
ANISOU 1048 CG2 THR A 157 14334 19517 21746 3465 1821 -810 C
ATOM 1049 N ALA A 158 83.484 -14.606 20.504 1.00112.79 N
ANISOU 1049 N ALA A 158 9812 15280 17762 2768 1607 -709 N
ATOM 1050 CA ALA A 158 83.095 -13.225 20.767 1.00105.98 C
ANISOU 1050 CA ALA A 158 8945 14321 17003 2477 1669 -706 C
ATOM 1051 C ALA A 158 82.599 -12.498 19.521 1.00113.17 C
ANISOU 1051 C ALA A 158 10071 14973 17954 2225 2067 -682 C
ATOM 1052 O ALA A 158 81.649 -11.713 19.606 1.00124.93 O
ANISOU 1052 O ALA A 158 11798 16321 19349 2077 2068 -580 O
ATOM 1053 CB ALA A 158 84.261 -12.473 21.383 1.00102.16 C
ANISOU 1053 CB ALA A 158 7988 13951 16879 2347 1680 -866 C
ATOM 1054 N ARG A 159 83.184 -12.763 18.348 1.00106.94 N
ANISOU 1054 N ARG A 159 9245 14097 17290 2184 2425 -748 N
ATOM 1055 CA ARG A 159 82.631 -12.146 17.146 1.00111.90 C
ANISOU 1055 CA ARG A 159 10179 14436 17904 1963 2824 -669 C
ATOM 1056 C ARG A 159 81.216 -12.671 16.852 1.00129.41 C
ANISOU 1056 C ARG A 159 12881 16505 19786 2063 2692 -457 C
ATOM 1057 O ARG A 159 80.324 -11.885 16.517 1.00137.03 O
ANISOU 1057 O ARG A 159 14134 17265 20667 1909 2820 -320 O
ATOM 1058 CB ARG A 159 83.546 -12.369 15.943 1.00111.67 C
ANISOU 1058 CB ARG A 159 10060 14320 18049 1895 3260 -776 C
ATOM 1059 CG ARG A 159 82.967 -11.898 14.605 1.00118.04 C
ANISOU 1059 CG ARG A 159 11283 14789 18778 1700 3698 -659 C
ATOM 1060 CD ARG A 159 83.888 -12.310 13.403 1.00128.07 C
ANISOU 1060 CD ARG A 159 12513 15968 20180 1659 4130 -766 C
ATOM 1061 NE ARG A 159 83.969 -11.216 12.426 1.00135.20 N
ANISOU 1061 NE ARG A 159 13627 16580 21162 1338 4638 -773 N
ATOM 1062 CZ ARG A 159 84.574 -11.308 11.244 1.00141.86 C
ANISOU 1062 CZ ARG A 159 14574 17251 22076 1227 5095 -839 C
ATOM 1063 NH1 ARG A 159 85.150 -12.452 10.915 1.00144.17 N
ANISOU 1063 NH1 ARG A 159 14731 17651 22395 1425 5098 -903 N
ATOM 1064 NH2 ARG A 159 84.652 -10.266 10.415 1.00143.68 N
ANISOU 1064 NH2 ARG A 159 15053 17196 22342 923 5554 -856 N
ATOM 1065 N ARG A 160 80.970 -13.996 16.954 1.00132.90 N
ANISOU 1065 N ARG A 160 13434 17031 20033 2317 2443 -428 N
ATOM 1066 CA ARG A 160 79.586 -14.489 16.827 1.00131.03 C
ANISOU 1066 CA ARG A 160 13632 16655 19499 2373 2271 -246 C
ATOM 1067 C ARG A 160 78.674 -13.961 17.937 1.00125.50 C
ANISOU 1067 C ARG A 160 13019 16004 18663 2343 1940 -175 C
ATOM 1068 O ARG A 160 77.469 -13.773 17.718 1.00129.80 O
ANISOU 1068 O ARG A 160 13901 16388 19028 2279 1912 -5 O
ATOM 1069 CB ARG A 160 79.542 -16.021 16.801 1.00136.57 C
ANISOU 1069 CB ARG A 160 14430 17413 20049 2615 2061 -270 C
ATOM 1070 CG ARG A 160 78.176 -16.640 16.413 1.00143.45 C
ANISOU 1070 CG ARG A 160 15755 18093 20658 2619 1962 -77 C
ATOM 1071 CD ARG A 160 77.411 -15.808 15.390 1.00148.74 C
ANISOU 1071 CD ARG A 160 16728 18518 21271 2431 2289 128 C
ATOM 1072 NE ARG A 160 78.019 -15.840 14.061 1.00151.64 N
ANISOU 1072 NE ARG A 160 17156 18729 21730 2386 2737 136 N
ATOM 1073 CZ ARG A 160 77.661 -15.040 13.059 1.00146.25 C
ANISOU 1073 CZ ARG A 160 16740 17810 21019 2232 3104 271 C
ATOM 1074 NH1 ARG A 160 78.268 -15.131 11.882 1.00142.62 N
ANISOU 1074 NH1 ARG A 160 16375 17191 20623 2183 3519 254 N
ATOM 1075 NH2 ARG A 160 76.702 -14.140 13.238 1.00144.04 N
ANISOU 1075 NH2 ARG A 160 16658 17441 20631 2134 3061 414 N
ATOM 1076 N ALA A 161 79.209 -13.753 19.144 1.00114.39 N
ANISOU 1076 N ALA A 161 11326 14819 17317 2404 1688 -288 N
ATOM 1077 CA ALA A 161 78.390 -13.176 20.208 1.00 95.31 C
ANISOU 1077 CA ALA A 161 9004 12435 14773 2363 1413 -227 C
ATOM 1078 C ALA A 161 77.971 -11.756 19.854 1.00 95.03 C
ANISOU 1078 C ALA A 161 9033 12224 14851 2118 1664 -145 C
ATOM 1079 O ALA A 161 76.831 -11.348 20.112 1.00102.79 O
ANISOU 1079 O ALA A 161 10271 13111 15672 2070 1552 -17 O
ATOM 1080 CB ALA A 161 79.147 -13.201 21.538 1.00 81.87 C
ANISOU 1080 CB ALA A 161 7005 10991 13113 2480 1145 -322 C
ATOM 1081 N LEU A 162 78.885 -10.989 19.257 1.00 85.69 N
ANISOU 1081 N LEU A 162 7629 10983 13946 1957 2020 -228 N
ATOM 1082 CA LEU A 162 78.556 -9.646 18.794 1.00 84.07 C
ANISOU 1082 CA LEU A 162 7530 10566 13847 1721 2325 -169 C
ATOM 1083 C LEU A 162 77.534 -9.690 17.656 1.00 84.59 C
ANISOU 1083 C LEU A 162 8043 10376 13723 1707 2541 31 C
ATOM 1084 O LEU A 162 76.647 -8.820 17.567 1.00 91.57 O
ANISOU 1084 O LEU A 162 9169 11098 14526 1623 2615 165 O
ATOM 1085 CB LEU A 162 79.848 -8.938 18.386 1.00 84.58 C
ANISOU 1085 CB LEU A 162 7280 10614 14243 1522 2681 -351 C
ATOM 1086 CG LEU A 162 79.872 -7.423 18.212 1.00 90.57 C
ANISOU 1086 CG LEU A 162 8055 11189 15169 1237 2991 -382 C
ATOM 1087 CD1 LEU A 162 81.307 -6.954 18.092 1.00102.30 C
ANISOU 1087 CD1 LEU A 162 9152 12730 16986 1038 3244 -626 C
ATOM 1088 CD2 LEU A 162 79.103 -7.041 16.963 1.00 95.23 C
ANISOU 1088 CD2 LEU A 162 9104 11465 15615 1153 3362 -217 C
ATOM 1089 N GLY A 163 77.605 -10.724 16.814 1.00 73.31 N
ANISOU 1089 N GLY A 163 6746 8907 12202 1812 2627 65 N
ATOM 1090 CA GLY A 163 76.583 -10.888 15.790 1.00 73.51 C
ANISOU 1090 CA GLY A 163 7221 8700 12009 1826 2784 278 C
ATOM 1091 C GLY A 163 75.220 -11.154 16.404 1.00 75.83 C
ANISOU 1091 C GLY A 163 7749 9026 12036 1920 2414 434 C
ATOM 1092 O GLY A 163 74.203 -10.597 15.969 1.00 83.84 O
ANISOU 1092 O GLY A 163 9082 9876 12898 1887 2496 612 O
ATOM 1093 N SER A 164 75.185 -11.997 17.441 1.00 73.62 N
ANISOU 1093 N SER A 164 7334 8956 11684 2039 2006 352 N
ATOM 1094 CA SER A 164 73.933 -12.276 18.139 1.00 65.68 C
ANISOU 1094 CA SER A 164 6539 7984 10432 2078 1658 450 C
ATOM 1095 C SER A 164 73.403 -11.013 18.807 1.00 69.77 C
ANISOU 1095 C SER A 164 7057 8489 10962 1981 1604 489 C
ATOM 1096 O SER A 164 72.189 -10.820 18.892 1.00 77.16 O
ANISOU 1096 O SER A 164 8245 9371 11700 1964 1484 623 O
ATOM 1097 CB SER A 164 74.115 -13.396 19.171 1.00 64.00 C
ANISOU 1097 CB SER A 164 6214 7953 10149 2201 1276 309 C
ATOM 1098 OG SER A 164 74.621 -14.592 18.589 1.00 71.69 O
ANISOU 1098 OG SER A 164 7189 8926 11124 2312 1319 265 O
ATOM 1099 N ILE A 165 74.295 -10.141 19.278 1.00 74.36 N
ANISOU 1099 N ILE A 165 7349 9125 11778 1909 1699 366 N
ATOM 1100 CA ILE A 165 73.855 -8.907 19.927 1.00 69.31 C
ANISOU 1100 CA ILE A 165 6705 8454 11177 1817 1672 398 C
ATOM 1101 C ILE A 165 73.175 -7.993 18.909 1.00 72.11 C
ANISOU 1101 C ILE A 165 7344 8556 11498 1742 1997 569 C
ATOM 1102 O ILE A 165 72.111 -7.397 19.174 1.00 76.88 O
ANISOU 1102 O ILE A 165 8152 9102 11957 1746 1898 689 O
ATOM 1103 CB ILE A 165 75.067 -8.217 20.582 1.00 54.41 C
ANISOU 1103 CB ILE A 165 4425 6668 9578 1729 1730 216 C
ATOM 1104 CG1 ILE A 165 75.523 -8.984 21.823 1.00 48.40 C
ANISOU 1104 CG1 ILE A 165 3451 6167 8771 1855 1344 84 C
ATOM 1105 CG2 ILE A 165 74.749 -6.774 20.923 1.00 47.99 C
ANISOU 1105 CG2 ILE A 165 3620 5743 8873 1592 1843 248 C
ATOM 1106 CD1 ILE A 165 76.771 -8.422 22.470 1.00 51.81 C
ANISOU 1106 CD1 ILE A 165 3475 6729 9483 1783 1366 -84 C
ATOM 1107 N LEU A 166 73.764 -7.888 17.715 1.00 69.55 N
ANISOU 1107 N LEU A 166 7075 8072 11278 1685 2400 574 N
ATOM 1108 CA LEU A 166 73.117 -7.114 16.661 1.00 65.27 C
ANISOU 1108 CA LEU A 166 6905 7257 10637 1647 2734 735 C
ATOM 1109 C LEU A 166 71.772 -7.728 16.287 1.00 53.38 C
ANISOU 1109 C LEU A 166 5760 5726 8798 1786 2535 933 C
ATOM 1110 O LEU A 166 70.782 -7.010 16.083 1.00 53.17 O
ANISOU 1110 O LEU A 166 6018 5578 8605 1811 2549 1069 O
ATOM 1111 CB LEU A 166 74.025 -7.042 15.433 1.00 75.00 C
ANISOU 1111 CB LEU A 166 8201 8309 11988 1544 3213 677 C
ATOM 1112 CG LEU A 166 75.006 -5.882 15.355 1.00 79.08 C
ANISOU 1112 CG LEU A 166 8561 8719 12766 1309 3585 515 C
ATOM 1113 CD1 LEU A 166 75.843 -5.816 16.619 1.00 77.53 C
ANISOU 1113 CD1 LEU A 166 7850 8784 12822 1250 3336 312 C
ATOM 1114 CD2 LEU A 166 75.884 -6.079 14.138 1.00 94.68 C
ANISOU 1114 CD2 LEU A 166 10625 10543 14807 1192 4011 437 C
ATOM 1115 N GLY A 167 71.686 -9.059 16.295 1.00 52.35 N
ANISOU 1115 N GLY A 167 5609 5729 8553 1870 2310 928 N
ATOM 1116 CA GLY A 167 70.410 -9.683 16.001 1.00 58.98 C
ANISOU 1116 CA GLY A 167 6748 6577 9083 1945 2108 1074 C
ATOM 1117 C GLY A 167 69.381 -9.455 17.087 1.00 72.91 C
ANISOU 1117 C GLY A 167 8509 8480 10712 1928 1734 1075 C
ATOM 1118 O GLY A 167 68.188 -9.327 16.795 1.00 89.02 O
ANISOU 1118 O GLY A 167 10799 10501 12524 1938 1636 1175 O
ATOM 1119 N ILE A 168 69.828 -9.342 18.340 1.00 67.78 N
ANISOU 1119 N ILE A 168 7586 7974 10194 1896 1529 935 N
ATOM 1120 CA ILE A 168 68.905 -9.061 19.435 1.00 58.39 C
ANISOU 1120 CA ILE A 168 6417 6886 8881 1863 1218 911 C
ATOM 1121 C ILE A 168 68.300 -7.680 19.251 1.00 62.57 C
ANISOU 1121 C ILE A 168 7085 7297 9391 1841 1345 1009 C
ATOM 1122 O ILE A 168 67.086 -7.488 19.397 1.00 66.76 O
ANISOU 1122 O ILE A 168 7793 7852 9723 1831 1175 1054 O
ATOM 1123 CB ILE A 168 69.610 -9.176 20.799 1.00 56.63 C
ANISOU 1123 CB ILE A 168 5921 6812 8784 1856 1005 735 C
ATOM 1124 CG1 ILE A 168 69.920 -10.631 21.128 1.00 59.30 C
ANISOU 1124 CG1 ILE A 168 6206 7257 9069 1910 805 628 C
ATOM 1125 CG2 ILE A 168 68.764 -8.532 21.896 1.00 60.63 C
ANISOU 1125 CG2 ILE A 168 6472 7368 9198 1814 786 715 C
ATOM 1126 CD1 ILE A 168 70.919 -10.795 22.257 1.00 71.47 C
ANISOU 1126 CD1 ILE A 168 7480 8938 10738 1960 641 439 C
ATOM 1127 N TRP A 169 69.135 -6.691 18.927 1.00 58.77 N
ANISOU 1127 N TRP A 169 6525 6674 9129 1822 1662 1014 N
ATOM 1128 CA TRP A 169 68.564 -5.366 18.690 1.00 52.36 C
ANISOU 1128 CA TRP A 169 5915 5696 8285 1821 1817 1107 C
ATOM 1129 C TRP A 169 67.648 -5.356 17.470 1.00 54.61 C
ANISOU 1129 C TRP A 169 6593 5847 8309 1883 1910 1249 C
ATOM 1130 O TRP A 169 66.621 -4.665 17.470 1.00 48.73 O
ANISOU 1130 O TRP A 169 6061 5073 7382 1905 1796 1299 O
ATOM 1131 CB TRP A 169 69.667 -4.318 18.588 1.00 45.32 C
ANISOU 1131 CB TRP A 169 4888 4635 7696 1746 2199 1042 C
ATOM 1132 CG TRP A 169 70.160 -3.998 19.949 1.00 46.19 C
ANISOU 1132 CG TRP A 169 4656 4896 7997 1682 2015 904 C
ATOM 1133 CD1 TRP A 169 71.186 -4.595 20.624 1.00 49.32 C
ANISOU 1133 CD1 TRP A 169 4690 5476 8575 1633 1894 738 C
ATOM 1134 CD2 TRP A 169 69.615 -3.013 20.831 1.00 46.13 C
ANISOU 1134 CD2 TRP A 169 4670 4872 7986 1679 1899 913 C
ATOM 1135 NE1 TRP A 169 71.316 -4.037 21.877 1.00 55.01 N
ANISOU 1135 NE1 TRP A 169 5210 6294 9399 1594 1707 647 N
ATOM 1136 CE2 TRP A 169 70.365 -3.060 22.026 1.00 57.95 C
ANISOU 1136 CE2 TRP A 169 5805 6537 9675 1615 1725 756 C
ATOM 1137 CE3 TRP A 169 68.561 -2.100 20.729 1.00 43.30 C
ANISOU 1137 CE3 TRP A 169 4624 4371 7456 1734 1903 1028 C
ATOM 1138 CZ2 TRP A 169 70.102 -2.219 23.105 1.00 66.24 C
ANISOU 1138 CZ2 TRP A 169 6792 7598 10777 1599 1595 726 C
ATOM 1139 CZ3 TRP A 169 68.301 -1.267 21.798 1.00 52.52 C
ANISOU 1139 CZ3 TRP A 169 5730 5551 8674 1723 1775 992 C
ATOM 1140 CH2 TRP A 169 69.071 -1.327 22.970 1.00 62.74 C
ANISOU 1140 CH2 TRP A 169 6654 6996 10187 1654 1642 850 C
ATOM 1141 N ALA A 170 67.987 -6.123 16.430 1.00 63.45 N
ANISOU 1141 N ALA A 170 7821 6899 9389 1912 2088 1290 N
ATOM 1142 CA ALA A 170 67.139 -6.147 15.240 1.00 49.92 C
ANISOU 1142 CA ALA A 170 6506 5070 7392 1970 2149 1398 C
ATOM 1143 C ALA A 170 65.754 -6.717 15.559 1.00 45.53 C
ANISOU 1143 C ALA A 170 5989 4722 6589 1976 1721 1380 C
ATOM 1144 O ALA A 170 64.717 -6.111 15.236 1.00 35.03 O
ANISOU 1144 O ALA A 170 4877 3366 5067 1992 1604 1393 O
ATOM 1145 CB ALA A 170 67.820 -6.971 14.150 1.00 45.77 C
ANISOU 1145 CB ALA A 170 6085 4435 6871 1995 2423 1429 C
ATOM 1146 N VAL A 171 65.719 -7.862 16.248 1.00 48.51 N
ANISOU 1146 N VAL A 171 6150 5292 6988 1941 1481 1308 N
ATOM 1147 CA VAL A 171 64.443 -8.463 16.631 1.00 51.66 C
ANISOU 1147 CA VAL A 171 6570 5845 7213 1898 1140 1249 C
ATOM 1148 C VAL A 171 63.669 -7.553 17.572 1.00 56.66 C
ANISOU 1148 C VAL A 171 7155 6531 7840 1852 949 1191 C
ATOM 1149 O VAL A 171 62.463 -7.325 17.390 1.00 58.18 O
ANISOU 1149 O VAL A 171 7466 6740 7898 1841 792 1171 O
ATOM 1150 CB VAL A 171 64.664 -9.841 17.270 1.00 55.69 C
ANISOU 1150 CB VAL A 171 6914 6490 7757 1856 975 1169 C
ATOM 1151 CG1 VAL A 171 63.354 -10.353 17.839 1.00 55.81 C
ANISOU 1151 CG1 VAL A 171 6945 6615 7646 1790 703 1107 C
ATOM 1152 CG2 VAL A 171 65.205 -10.820 16.252 1.00 65.13 C
ANISOU 1152 CG2 VAL A 171 8194 7631 8921 1914 1139 1225 C
ATOM 1153 N SER A 172 64.338 -7.038 18.610 1.00 56.32 N
ANISOU 1153 N SER A 172 6926 6513 7960 1828 952 1148 N
ATOM 1154 CA SER A 172 63.619 -6.256 19.604 1.00 43.82 C
ANISOU 1154 CA SER A 172 5307 4978 6363 1788 775 1087 C
ATOM 1155 C SER A 172 62.999 -5.030 18.957 1.00 43.02 C
ANISOU 1155 C SER A 172 5417 4752 6178 1841 858 1154 C
ATOM 1156 O SER A 172 61.825 -4.719 19.190 1.00 55.93 O
ANISOU 1156 O SER A 172 7112 6427 7713 1826 668 1108 O
ATOM 1157 CB SER A 172 64.573 -5.832 20.731 1.00 46.44 C
ANISOU 1157 CB SER A 172 5426 5334 6883 1771 789 1030 C
ATOM 1158 OG SER A 172 65.192 -6.937 21.371 1.00 30.06 O
ANISOU 1158 OG SER A 172 3181 3370 4872 1741 673 937 O
ATOM 1159 N LEU A 173 63.748 -4.367 18.073 1.00 49.35 N
ANISOU 1159 N LEU A 173 6360 5371 7020 1904 1159 1251 N
ATOM 1160 CA LEU A 173 63.216 -3.195 17.393 1.00 55.11 C
ANISOU 1160 CA LEU A 173 7375 5936 7627 1957 1242 1301 C
ATOM 1161 C LEU A 173 62.071 -3.558 16.448 1.00 53.39 C
ANISOU 1161 C LEU A 173 7359 5739 7188 1986 1077 1295 C
ATOM 1162 O LEU A 173 61.117 -2.785 16.306 1.00 53.89 O
ANISOU 1162 O LEU A 173 7565 5766 7144 2016 943 1277 O
ATOM 1163 CB LEU A 173 64.348 -2.477 16.649 1.00 47.39 C
ANISOU 1163 CB LEU A 173 6573 4693 6740 1979 1662 1381 C
ATOM 1164 CG LEU A 173 65.319 -1.779 17.609 1.00 41.99 C
ANISOU 1164 CG LEU A 173 5684 3935 6336 1937 1833 1358 C
ATOM 1165 CD1 LEU A 173 66.636 -1.527 16.915 1.00 52.27 C
ANISOU 1165 CD1 LEU A 173 7043 4971 7845 1898 2312 1376 C
ATOM 1166 CD2 LEU A 173 64.749 -0.504 18.231 1.00 37.50 C
ANISOU 1166 CD2 LEU A 173 5226 3300 5721 1943 1748 1344 C
ATOM 1167 N ALA A 174 62.114 -4.740 15.825 1.00 60.72 N
ANISOU 1167 N ALA A 174 8284 6722 8065 1981 1069 1301 N
ATOM 1168 CA ALA A 174 61.045 -5.054 14.882 1.00 59.58 C
ANISOU 1168 CA ALA A 174 8325 6574 7740 2008 915 1291 C
ATOM 1169 C ALA A 174 59.749 -5.425 15.597 1.00 62.03 C
ANISOU 1169 C ALA A 174 8468 7042 8057 1952 586 1201 C
ATOM 1170 O ALA A 174 58.683 -4.879 15.278 1.00 61.76 O
ANISOU 1170 O ALA A 174 8548 6986 7933 2011 467 1201 O
ATOM 1171 CB ALA A 174 61.484 -6.187 13.947 1.00 56.20 C
ANISOU 1171 CB ALA A 174 7978 6125 7249 2023 1030 1325 C
ATOM 1172 N ILE A 175 59.832 -6.291 16.614 1.00 61.82 N
ANISOU 1172 N ILE A 175 8208 7169 8113 1896 524 1161 N
ATOM 1173 CA ILE A 175 58.627 -6.888 17.188 1.00 47.13 C
ANISOU 1173 CA ILE A 175 6247 5443 6217 1887 346 1123 C
ATOM 1174 C ILE A 175 57.866 -5.963 18.123 1.00 55.86 C
ANISOU 1174 C ILE A 175 7281 6584 7357 1894 247 1085 C
ATOM 1175 O ILE A 175 56.714 -6.264 18.468 1.00 51.43 O
ANISOU 1175 O ILE A 175 6660 6106 6775 1902 115 1053 O
ATOM 1176 CB ILE A 175 59.005 -8.180 17.936 1.00 33.99 C
ANISOU 1176 CB ILE A 175 4418 3897 4600 1820 336 1097 C
ATOM 1177 CG1 ILE A 175 59.880 -7.840 19.143 1.00 35.08 C
ANISOU 1177 CG1 ILE A 175 4400 4067 4863 1771 369 1066 C
ATOM 1178 CG2 ILE A 175 59.706 -9.167 17.020 1.00 37.67 C
ANISOU 1178 CG2 ILE A 175 4954 4328 5031 1829 433 1133 C
ATOM 1179 CD1 ILE A 175 60.324 -9.039 19.940 1.00 36.85 C
ANISOU 1179 CD1 ILE A 175 4492 4383 5125 1720 341 1038 C
ATOM 1180 N MET A 176 58.463 -4.845 18.539 1.00 60.54 N
ANISOU 1180 N MET A 176 7881 7105 8015 1895 314 1085 N
ATOM 1181 CA MET A 176 57.753 -3.860 19.344 1.00 44.69 C
ANISOU 1181 CA MET A 176 5841 5107 6032 1919 234 1052 C
ATOM 1182 C MET A 176 57.161 -2.742 18.509 1.00 49.65 C
ANISOU 1182 C MET A 176 6671 5610 6584 2015 217 1081 C
ATOM 1183 O MET A 176 56.580 -1.811 19.071 1.00 64.48 O
ANISOU 1183 O MET A 176 8548 7474 8478 2057 160 1059 O
ATOM 1184 CB MET A 176 58.684 -3.254 20.396 1.00 37.53 C
ANISOU 1184 CB MET A 176 4835 4185 5240 1870 295 1025 C
ATOM 1185 CG MET A 176 59.125 -4.284 21.384 1.00 49.72 C
ANISOU 1185 CG MET A 176 6191 5853 6847 1792 269 986 C
ATOM 1186 SD MET A 176 57.765 -5.296 21.978 1.00 55.69 S
ANISOU 1186 SD MET A 176 6866 6753 7540 1772 133 952 S
ATOM 1187 CE MET A 176 58.638 -6.344 23.135 1.00 49.97 C
ANISOU 1187 CE MET A 176 5995 6112 6878 1689 130 917 C
ATOM 1188 N VAL A 177 57.299 -2.806 17.185 1.00 49.59 N
ANISOU 1188 N VAL A 177 6862 5498 6481 2059 267 1131 N
ATOM 1189 CA VAL A 177 56.621 -1.829 16.334 1.00 54.55 C
ANISOU 1189 CA VAL A 177 7724 6002 6999 2166 226 1158 C
ATOM 1190 C VAL A 177 55.120 -1.828 16.570 1.00 63.98 C
ANISOU 1190 C VAL A 177 8842 7292 8176 2242 28 1121 C
ATOM 1191 O VAL A 177 54.539 -0.734 16.681 1.00 65.79 O
ANISOU 1191 O VAL A 177 9152 7463 8383 2331 -22 1116 O
ATOM 1192 CB VAL A 177 56.979 -2.078 14.851 1.00 64.38 C
ANISOU 1192 CB VAL A 177 9227 7120 8115 2196 308 1211 C
ATOM 1193 CG1 VAL A 177 56.202 -1.113 13.954 1.00 38.20 C
ANISOU 1193 CG1 VAL A 177 6193 3673 4646 2321 242 1231 C
ATOM 1194 CG2 VAL A 177 58.467 -1.953 14.646 1.00 68.06 C
ANISOU 1194 CG2 VAL A 177 9781 7471 8608 2141 563 1252 C
ATOM 1195 N PRO A 178 54.429 -2.975 16.660 1.00 60.29 N
ANISOU 1195 N PRO A 178 8225 6957 7724 2219 -81 1094 N
ATOM 1196 CA PRO A 178 52.984 -2.912 16.924 1.00 55.99 C
ANISOU 1196 CA PRO A 178 7583 6492 7200 2292 -254 1056 C
ATOM 1197 C PRO A 178 52.690 -2.162 18.199 1.00 50.28 C
ANISOU 1197 C PRO A 178 6720 5813 6569 2291 -261 1012 C
ATOM 1198 O PRO A 178 51.703 -1.408 18.283 1.00 42.75 O
ANISOU 1198 O PRO A 178 5770 4854 5620 2401 -357 993 O
ATOM 1199 CB PRO A 178 52.587 -4.391 17.031 1.00 50.03 C
ANISOU 1199 CB PRO A 178 6671 5860 6476 2221 -320 1033 C
ATOM 1200 CG PRO A 178 53.864 -5.089 17.393 1.00 52.43 C
ANISOU 1200 CG PRO A 178 6934 6183 6802 2103 -176 1042 C
ATOM 1201 CD PRO A 178 54.930 -4.360 16.660 1.00 56.52 C
ANISOU 1201 CD PRO A 178 7649 6561 7266 2125 -42 1093 C
ATOM 1202 N GLN A 179 53.576 -2.315 19.187 1.00 52.03 N
ANISOU 1202 N GLN A 179 6834 6073 6860 2183 -160 995 N
ATOM 1203 CA GLN A 179 53.438 -1.552 20.417 1.00 49.56 C
ANISOU 1203 CA GLN A 179 6426 5783 6622 2178 -154 955 C
ATOM 1204 C GLN A 179 53.475 -0.056 20.163 1.00 61.36 C
ANISOU 1204 C GLN A 179 8091 7139 8085 2277 -127 978 C
ATOM 1205 O GLN A 179 52.708 0.697 20.776 1.00 69.93 O
ANISOU 1205 O GLN A 179 9139 8231 9199 2348 -180 946 O
ATOM 1206 CB GLN A 179 54.519 -1.946 21.412 1.00 42.14 C
ANISOU 1206 CB GLN A 179 5378 4888 5746 2055 -61 938 C
ATOM 1207 CG GLN A 179 54.326 -1.159 22.659 1.00 42.32 C
ANISOU 1207 CG GLN A 179 5327 4922 5832 2057 -66 896 C
ATOM 1208 CD GLN A 179 53.138 -1.700 23.410 1.00 59.12 C
ANISOU 1208 CD GLN A 179 7308 7168 7988 2060 -153 844 C
ATOM 1209 OE1 GLN A 179 52.987 -2.902 23.640 1.00 69.15 O
ANISOU 1209 OE1 GLN A 179 8481 8532 9260 1991 -172 828 O
ATOM 1210 NE2 GLN A 179 52.209 -0.802 23.715 1.00 69.83 N
ANISOU 1210 NE2 GLN A 179 8659 8507 9367 2155 -200 820 N
ATOM 1211 N ALA A 180 54.363 0.393 19.275 1.00 60.13 N
ANISOU 1211 N ALA A 180 8140 6843 7865 2285 -30 1032 N
ATOM 1212 CA ALA A 180 54.387 1.807 18.930 1.00 53.75 C
ANISOU 1212 CA ALA A 180 7556 5871 6996 2379 9 1058 C
ATOM 1213 C ALA A 180 53.114 2.187 18.189 1.00 60.31 C
ANISOU 1213 C ALA A 180 8504 6683 7728 2541 -127 1058 C
ATOM 1214 O ALA A 180 52.594 3.296 18.358 1.00 52.22 O
ANISOU 1214 O ALA A 180 7582 5587 6672 2654 -158 1048 O
ATOM 1215 CB ALA A 180 55.624 2.146 18.102 1.00 40.00 C
ANISOU 1215 CB ALA A 180 6040 3958 5201 2338 173 1115 C
ATOM 1216 N ALA A 181 52.621 1.276 17.345 1.00 39.44 N
ANISOU 1216 N ALA A 181 5858 4095 5032 2565 -214 1066 N
ATOM 1217 CA ALA A 181 51.456 1.528 16.506 1.00 46.98 C
ANISOU 1217 CA ALA A 181 6928 5031 5892 2731 -368 1062 C
ATOM 1218 C ALA A 181 50.175 1.728 17.317 1.00 59.44 C
ANISOU 1218 C ALA A 181 8296 6725 7563 2818 -505 1002 C
ATOM 1219 O ALA A 181 49.301 2.507 16.908 1.00 75.72 O
ANISOU 1219 O ALA A 181 10472 8740 9558 2996 -616 987 O
ATOM 1220 CB ALA A 181 51.270 0.370 15.529 1.00 42.59 C
ANISOU 1220 CB ALA A 181 6388 4515 5279 2716 -437 1078 C
ATOM 1221 N VAL A 182 50.024 1.028 18.446 1.00 57.76 N
ANISOU 1221 N VAL A 182 7795 6658 7495 2707 -499 960 N
ATOM 1222 CA VAL A 182 48.771 1.157 19.194 1.00 55.79 C
ANISOU 1222 CA VAL A 182 7344 6512 7343 2787 -604 900 C
ATOM 1223 C VAL A 182 48.725 2.383 20.107 1.00 66.47 C
ANISOU 1223 C VAL A 182 8711 7816 8730 2848 -552 875 C
ATOM 1224 O VAL A 182 47.638 2.757 20.566 1.00 75.82 O
ANISOU 1224 O VAL A 182 9776 9055 9978 2963 -632 826 O
ATOM 1225 CB VAL A 182 48.492 -0.104 20.032 1.00 50.99 C
ANISOU 1225 CB VAL A 182 6456 6061 6859 2651 -610 858 C
ATOM 1226 CG1 VAL A 182 48.292 -1.316 19.137 1.00 39.61 C
ANISOU 1226 CG1 VAL A 182 4995 4668 5389 2614 -684 877 C
ATOM 1227 CG2 VAL A 182 49.604 -0.338 21.036 1.00 47.94 C
ANISOU 1227 CG2 VAL A 182 6021 5685 6507 2488 -470 853 C
ATOM 1228 N MET A 183 49.861 3.014 20.400 1.00 64.34 N
ANISOU 1228 N MET A 183 8576 7441 8429 2779 -417 904 N
ATOM 1229 CA MET A 183 49.863 4.162 21.299 1.00 67.47 C
ANISOU 1229 CA MET A 183 9003 7778 8854 2829 -365 881 C
ATOM 1230 C MET A 183 49.174 5.380 20.688 1.00 73.40 C
ANISOU 1230 C MET A 183 9969 8413 9506 3044 -430 885 C
ATOM 1231 O MET A 183 49.391 5.720 19.520 1.00 59.96 O
ANISOU 1231 O MET A 183 8529 6591 7663 3119 -444 929 O
ATOM 1232 CB MET A 183 51.292 4.540 21.695 1.00 68.95 C
ANISOU 1232 CB MET A 183 9290 7867 9042 2700 -212 911 C
ATOM 1233 CG MET A 183 52.087 3.457 22.391 1.00 69.95 C
ANISOU 1233 CG MET A 183 9227 8097 9254 2513 -156 898 C
ATOM 1234 SD MET A 183 51.068 2.726 23.690 1.00 79.14 S
ANISOU 1234 SD MET A 183 10098 9445 10527 2485 -225 820 S
ATOM 1235 CE MET A 183 50.960 4.064 24.879 1.00 72.54 C
ANISOU 1235 CE MET A 183 9289 8539 9733 2546 -176 784 C
ATOM 1236 N GLU A 184 48.364 6.060 21.503 1.00 82.70 N
ANISOU 1236 N GLU A 184 11062 9615 10744 3153 -464 834 N
ATOM 1237 CA GLU A 184 47.668 7.265 21.082 1.00 74.65 C
ANISOU 1237 CA GLU A 184 10244 8489 9631 3382 -533 823 C
ATOM 1238 C GLU A 184 47.635 8.206 22.277 1.00 71.95 C
ANISOU 1238 C GLU A 184 9885 8105 9347 3412 -455 788 C
ATOM 1239 O GLU A 184 47.373 7.796 23.417 1.00 73.69 O
ANISOU 1239 O GLU A 184 9846 8444 9709 3335 -426 740 O
ATOM 1240 CB GLU A 184 46.255 6.981 20.542 1.00 81.23 C
ANISOU 1240 CB GLU A 184 10963 9420 10481 3564 -721 779 C
ATOM 1241 CG GLU A 184 46.248 6.319 19.150 1.00 96.80 C
ANISOU 1241 CG GLU A 184 13054 11383 12344 3585 -821 814 C
ATOM 1242 CD GLU A 184 46.623 7.281 18.020 1.00108.19 C
ANISOU 1242 CD GLU A 184 14927 12618 13562 3719 -834 854 C
ATOM 1243 OE1 GLU A 184 46.287 8.483 18.114 1.00112.58 O
ANISOU 1243 OE1 GLU A 184 15668 13065 14043 3893 -855 834 O
ATOM 1244 OE2 GLU A 184 47.270 6.835 17.042 1.00108.74 O
ANISOU 1244 OE2 GLU A 184 15177 12621 13519 3651 -811 904 O
ATOM 1245 N CYS A 185 47.898 9.470 21.984 1.00 80.60 N
ANISOU 1245 N CYS A 185 11292 9016 10315 3525 -416 810 N
ATOM 1246 CA CYS A 185 47.891 10.589 22.918 1.00 80.06 C
ANISOU 1246 CA CYS A 185 11305 8857 10258 3586 -341 783 C
ATOM 1247 C CYS A 185 46.640 11.418 22.648 1.00 89.68 C
ANISOU 1247 C CYS A 185 12610 10045 11420 3871 -467 738 C
ATOM 1248 O CYS A 185 46.522 12.048 21.589 1.00 93.24 O
ANISOU 1248 O CYS A 185 13366 10363 11697 4027 -533 761 O
ATOM 1249 CB CYS A 185 49.165 11.419 22.810 1.00 71.56 C
ANISOU 1249 CB CYS A 185 10542 7571 9078 3494 -191 836 C
ATOM 1250 SG CYS A 185 49.174 12.871 23.866 1.00 79.16 S
ANISOU 1250 SG CYS A 185 11666 8383 10026 3571 -99 803 S
ATOM 1251 N SER A 186 45.698 11.396 23.587 1.00 95.98 N
ANISOU 1251 N SER A 186 13147 10960 12361 3950 -502 666 N
ATOM 1252 CA SER A 186 44.409 12.047 23.407 1.00102.64 C
ANISOU 1252 CA SER A 186 13992 11807 13199 4237 -634 607 C
ATOM 1253 C SER A 186 44.127 12.882 24.648 1.00111.48 C
ANISOU 1253 C SER A 186 15072 12890 14395 4304 -544 553 C
ATOM 1254 O SER A 186 44.566 12.551 25.752 1.00120.85 O
ANISOU 1254 O SER A 186 16096 14129 15694 4125 -419 539 O
ATOM 1255 CB SER A 186 43.290 11.022 23.176 1.00100.58 C
ANISOU 1255 CB SER A 186 13390 11749 13075 4294 -780 555 C
ATOM 1256 OG SER A 186 43.235 10.081 24.236 1.00 96.62 O
ANISOU 1256 OG SER A 186 12540 11406 12767 4108 -696 523 O
ATOM 1257 N SER A 187 43.381 13.967 24.453 1.00103.04 N
ANISOU 1257 N SER A 187 14173 11724 13252 4578 -616 517 N
ATOM 1258 CA SER A 187 43.031 14.882 25.530 1.00 96.27 C
ANISOU 1258 CA SER A 187 13322 10808 12449 4685 -534 461 C
ATOM 1259 C SER A 187 41.706 14.547 26.210 1.00107.40 C
ANISOU 1259 C SER A 187 14344 12388 14076 4819 -587 360 C
ATOM 1260 O SER A 187 40.895 13.755 25.722 1.00118.48 O
ANISOU 1260 O SER A 187 15492 13945 15578 4878 -716 328 O
ATOM 1261 CB SER A 187 42.972 16.310 24.977 1.00 86.78 C
ANISOU 1261 CB SER A 187 12552 9384 11037 4924 -570 473 C
ATOM 1262 OG SER A 187 43.019 17.287 26.001 1.00 71.68 O
ANISOU 1262 OG SER A 187 10747 7359 9129 4975 -447 440 O
ATOM 1263 N VAL A 188 41.524 15.159 27.383 1.00100.70 N
ANISOU 1263 N VAL A 188 13455 11500 13306 4855 -466 304 N
ATOM 1264 CA VAL A 188 40.401 14.908 28.281 1.00 89.82 C
ANISOU 1264 CA VAL A 188 11711 10259 12157 4950 -443 196 C
ATOM 1265 C VAL A 188 40.056 16.162 29.090 1.00 90.74 C
ANISOU 1265 C VAL A 188 11963 10243 12270 5138 -355 134 C
ATOM 1266 O VAL A 188 38.997 16.771 28.907 1.00 90.08 O
ANISOU 1266 O VAL A 188 11840 10154 12232 5433 -441 67 O
ATOM 1267 CB VAL A 188 40.699 13.748 29.249 1.00 30.00 C
ATOM 1268 CG1 VAL A 188 39.568 13.589 30.254 1.00 30.00 C
ATOM 1269 CG2 VAL A 188 40.923 12.456 28.479 1.00 30.00 C
ATOM 1270 N PHE A 199 45.698 19.017 29.438 1.00132.58 N
ANISOU 1270 N PHE A 199 18901 14695 16780 4509 139 447 N
ATOM 1271 CA PHE A 199 45.697 17.761 30.184 1.00123.70 C
ANISOU 1271 CA PHE A 199 17350 13786 15864 4320 152 415 C
ATOM 1272 C PHE A 199 45.553 16.546 29.264 1.00110.40 C
ANISOU 1272 C PHE A 199 15408 12274 14263 4235 28 448 C
ATOM 1273 O PHE A 199 44.449 16.046 29.029 1.00115.16 O
ANISOU 1273 O PHE A 199 15764 13027 14963 4374 -80 403 O
ATOM 1274 CB PHE A 199 44.580 17.764 31.232 1.00127.72 C
ANISOU 1274 CB PHE A 199 17600 14396 16531 4450 169 309 C
ATOM 1275 CG PHE A 199 44.258 16.399 31.777 1.00119.98 C
ANISOU 1275 CG PHE A 199 16179 13644 15762 4296 160 263 C
ATOM 1276 CD1 PHE A 199 45.183 15.703 32.540 1.00119.75 C
ANISOU 1276 CD1 PHE A 199 16090 13665 15744 4057 250 277 C
ATOM 1277 CD2 PHE A 199 43.028 15.811 31.523 1.00115.52 C
ANISOU 1277 CD2 PHE A 199 15310 13246 15337 4437 68 206 C
ATOM 1278 CE1 PHE A 199 44.886 14.445 33.037 1.00122.16 C
ANISOU 1278 CE1 PHE A 199 16040 14164 16211 3921 245 233 C
ATOM 1279 CE2 PHE A 199 42.725 14.558 32.019 1.00113.88 C
ANISOU 1279 CE2 PHE A 199 14742 13232 15295 4297 83 161 C
ATOM 1280 CZ PHE A 199 43.655 13.873 32.778 1.00118.72 C
ANISOU 1280 CZ PHE A 199 15315 13879 15916 4035 173 176 C
ATOM 1281 N SER A 200 46.677 16.094 28.724 1.00 92.44 N
ANISOU 1281 N SER A 200 13220 9969 11933 4028 53 522 N
ATOM 1282 CA SER A 200 46.700 15.007 27.757 1.00 89.96 C
ANISOU 1282 CA SER A 200 12756 9787 11636 3960 -43 564 C
ATOM 1283 C SER A 200 46.963 13.683 28.471 1.00 92.18 C
ANISOU 1283 C SER A 200 12689 10259 12077 3742 -20 546 C
ATOM 1284 O SER A 200 47.517 13.641 29.575 1.00 94.88 O
ANISOU 1284 O SER A 200 12976 10594 12479 3604 79 521 O
ATOM 1285 CB SER A 200 47.740 15.259 26.662 1.00 92.01 C
ANISOU 1285 CB SER A 200 13328 9894 11740 3877 -16 649 C
ATOM 1286 OG SER A 200 48.968 15.697 27.208 1.00105.29 O
ANISOU 1286 OG SER A 200 15203 11434 13368 3723 141 676 O
ATOM 1287 N VAL A 201 46.546 12.591 27.832 1.00 88.36 N
ANISOU 1287 N VAL A 201 11993 9935 11646 3719 -118 554 N
ATOM 1288 CA VAL A 201 46.739 11.257 28.385 1.00 82.05 C
ANISOU 1288 CA VAL A 201 10898 9309 10970 3521 -105 538 C
ATOM 1289 C VAL A 201 47.217 10.334 27.274 1.00 91.18 C
ANISOU 1289 C VAL A 201 12042 10518 12085 3415 -167 601 C
ATOM 1290 O VAL A 201 46.656 10.315 26.169 1.00 96.56 O
ANISOU 1290 O VAL A 201 12778 11202 12707 3544 -271 620 O
ATOM 1291 CB VAL A 201 45.456 10.698 29.028 1.00 73.33 C
ANISOU 1291 CB VAL A 201 9480 8366 10014 3598 -142 452 C
ATOM 1292 CG1 VAL A 201 44.401 10.419 27.958 1.00 66.81 C
ANISOU 1292 CG1 VAL A 201 8562 7618 9205 3761 -285 446 C
ATOM 1293 CG2 VAL A 201 45.781 9.446 29.841 1.00 77.40 C
ANISOU 1293 CG2 VAL A 201 9762 9020 10625 3380 -93 429 C
ATOM 1294 N CYS A 202 48.291 9.607 27.571 1.00 84.47 N
ANISOU 1294 N CYS A 202 11142 9697 11257 3194 -104 628 N
ATOM 1295 CA CYS A 202 48.891 8.621 26.687 1.00 81.01 C
ANISOU 1295 CA CYS A 202 10677 9310 10794 3069 -135 681 C
ATOM 1296 C CYS A 202 48.434 7.211 27.037 1.00 82.84 C
ANISOU 1296 C CYS A 202 10616 9737 11124 2971 -180 646 C
ATOM 1297 O CYS A 202 48.736 6.720 28.131 1.00 83.54 O
ANISOU 1297 O CYS A 202 10573 9890 11279 2848 -126 611 O
ATOM 1298 CB CYS A 202 50.409 8.733 26.783 1.00 79.10 C
ANISOU 1298 CB CYS A 202 10563 8963 10527 2903 -35 725 C
ATOM 1299 SG CYS A 202 51.316 7.692 25.649 1.00 91.03 S
ANISOU 1299 SG CYS A 202 12082 10500 12006 2767 -39 788 S
ATOM 1300 N ASP A 203 47.703 6.561 26.127 1.00 87.80 N
ANISOU 1300 N ASP A 203 11164 10444 11750 3029 -281 652 N
ATOM 1301 CA ASP A 203 47.313 5.182 26.397 1.00101.74 C
ANISOU 1301 CA ASP A 203 12682 12373 13602 2922 -313 621 C
ATOM 1302 C ASP A 203 47.154 4.451 25.065 1.00109.13 C
ANISOU 1302 C ASP A 203 13631 13342 14491 2930 -408 661 C
ATOM 1303 O ASP A 203 47.163 5.056 23.990 1.00116.67 O
ANISOU 1303 O ASP A 203 14778 14203 15348 3045 -458 703 O
ATOM 1304 CB ASP A 203 46.034 5.118 27.250 1.00110.68 C
ANISOU 1304 CB ASP A 203 13593 13601 14861 3007 -329 537 C
ATOM 1305 CG ASP A 203 45.906 3.811 28.026 1.00112.35 C
ANISOU 1305 CG ASP A 203 13585 13946 15159 2852 -299 494 C
ATOM 1306 OD1 ASP A 203 46.646 3.642 29.024 1.00107.68 O
ANISOU 1306 OD1 ASP A 203 13005 13351 14558 2727 -211 483 O
ATOM 1307 OD2 ASP A 203 45.081 2.953 27.647 1.00113.69 O
ANISOU 1307 OD2 ASP A 203 13585 14216 15398 2860 -365 470 O
ATOM 1308 N GLU A 204 47.050 3.127 25.148 1.00105.67 N
ANISOU 1308 N GLU A 204 13020 13024 14106 2806 -427 648 N
ATOM 1309 CA GLU A 204 46.826 2.292 23.971 1.00 96.93 C
ANISOU 1309 CA GLU A 204 11908 11955 12965 2805 -518 679 C
ATOM 1310 C GLU A 204 45.423 2.476 23.389 1.00 81.77 C
ANISOU 1310 C GLU A 204 9901 10080 11089 2992 -651 650 C
ATOM 1311 O GLU A 204 44.430 2.527 24.122 1.00 79.26 O
ANISOU 1311 O GLU A 204 9381 9840 10893 3057 -665 584 O
ATOM 1312 CB GLU A 204 47.046 0.823 24.338 1.00 91.57 C
ANISOU 1312 CB GLU A 204 11076 11386 12332 2629 -497 665 C
ATOM 1313 CG GLU A 204 48.479 0.476 24.728 1.00 73.76 C
ANISOU 1313 CG GLU A 204 8904 9101 10020 2464 -392 694 C
ATOM 1314 CD GLU A 204 48.593 -0.938 25.256 1.00 64.84 C
ANISOU 1314 CD GLU A 204 7640 8077 8918 2321 -375 670 C
ATOM 1315 OE1 GLU A 204 47.578 -1.667 25.194 1.00 76.22 O
ANISOU 1315 OE1 GLU A 204 8936 9601 10422 2337 -440 635 O
ATOM 1316 OE2 GLU A 204 49.678 -1.310 25.761 1.00 56.84 O
ANISOU 1316 OE2 GLU A 204 6665 7062 7870 2201 -299 684 O
ATOM 1317 N ARG A 205 45.338 2.551 22.061 1.00 65.49 N
ANISOU 1317 N ARG A 205 7988 7969 8926 3087 -750 693 N
ATOM 1318 CA ARG A 205 44.063 2.681 21.357 1.00 67.02 C
ANISOU 1318 CA ARG A 205 8117 8209 9137 3283 -913 662 C
ATOM 1319 C ARG A 205 43.798 1.346 20.662 1.00 68.19 C
ANISOU 1319 C ARG A 205 8157 8452 9302 3205 -998 674 C
ATOM 1320 O ARG A 205 44.500 0.991 19.706 1.00 71.28 O
ANISOU 1320 O ARG A 205 8734 8779 9571 3155 -1010 732 O
ATOM 1321 CB ARG A 205 44.082 3.844 20.373 1.00 83.71 C
ANISOU 1321 CB ARG A 205 10530 10183 11093 3483 -989 688 C
ATOM 1322 CG ARG A 205 42.782 4.031 19.608 1.00103.77 C
ANISOU 1322 CG ARG A 205 13029 12769 13630 3719 -1194 641 C
ATOM 1323 CD ARG A 205 42.746 5.414 18.961 1.00119.52 C
ANISOU 1323 CD ARG A 205 15347 14603 15461 3948 -1262 645 C
ATOM 1324 NE ARG A 205 41.619 5.619 18.057 1.00125.29 N
ANISOU 1324 NE ARG A 205 16101 15355 16146 4200 -1495 592 N
ATOM 1325 CZ ARG A 205 41.510 6.662 17.243 1.00119.53 C
ANISOU 1325 CZ ARG A 205 15704 14476 15236 4424 -1602 588 C
ATOM 1326 NH1 ARG A 205 42.468 7.582 17.217 1.00113.15 N
ANISOU 1326 NH1 ARG A 205 15231 13482 14277 4409 -1471 642 N
ATOM 1327 NH2 ARG A 205 40.442 6.791 16.466 1.00120.39 N
ANISOU 1327 NH2 ARG A 205 15820 14614 15309 4667 -1846 522 N
ATOM 1328 N TRP A 206 42.766 0.630 21.118 1.00 67.90 N
ANISOU 1328 N TRP A 206 7823 8558 9416 3200 -1049 617 N
ATOM 1329 CA TRP A 206 42.411 -0.694 20.603 1.00 73.47 C
ANISOU 1329 CA TRP A 206 8395 9363 10156 3117 -1125 623 C
ATOM 1330 C TRP A 206 41.067 -0.708 19.895 1.00 87.71 C
ANISOU 1330 C TRP A 206 10064 11261 12002 3303 -1318 577 C
ATOM 1331 O TRP A 206 40.038 -0.337 20.471 1.00 91.86 O
ANISOU 1331 O TRP A 206 10366 11876 12661 3419 -1348 503 O
ATOM 1332 CB TRP A 206 42.421 -1.759 21.703 1.00 77.47 C
ANISOU 1332 CB TRP A 206 8673 9966 10798 2923 -1016 592 C
ATOM 1333 CG TRP A 206 43.787 -2.068 22.262 1.00 88.04 C
ANISOU 1333 CG TRP A 206 10145 11235 12070 2735 -871 623 C
ATOM 1334 CD1 TRP A 206 44.309 -1.681 23.468 1.00 89.34 C
ANISOU 1334 CD1 TRP A 206 10306 11377 12261 2664 -740 593 C
ATOM 1335 CD2 TRP A 206 44.774 -2.918 21.651 1.00 86.53 C
ANISOU 1335 CD2 TRP A 206 10095 11007 11775 2604 -851 678 C
ATOM 1336 NE1 TRP A 206 45.577 -2.197 23.620 1.00 80.60 N
ANISOU 1336 NE1 TRP A 206 9329 10232 11065 2507 -654 627 N
ATOM 1337 CE2 TRP A 206 45.882 -2.963 22.523 1.00 79.09 C
ANISOU 1337 CE2 TRP A 206 9219 10030 10800 2470 -711 677 C
ATOM 1338 CE3 TRP A 206 44.830 -3.632 20.443 1.00 83.44 C
ANISOU 1338 CE3 TRP A 206 9786 10609 11309 2600 -939 726 C
ATOM 1339 CZ2 TRP A 206 47.035 -3.686 22.225 1.00 76.49 C
ANISOU 1339 CZ2 TRP A 206 9015 9671 10378 2343 -651 719 C
ATOM 1340 CZ3 TRP A 206 45.973 -4.353 20.149 1.00 79.64 C
ANISOU 1340 CZ3 TRP A 206 9441 10080 10737 2466 -867 769 C
ATOM 1341 CH2 TRP A 206 47.061 -4.373 21.035 1.00 83.04 C
ANISOU 1341 CH2 TRP A 206 9915 10488 11147 2344 -722 763 C
ATOM 1342 N ALA A 207 41.111 -1.159 18.636 1.00101.90 N
ANISOU 1342 N ALA A 207 11996 13038 13682 3335 -1450 613 N
ATOM 1343 CA ALA A 207 39.953 -1.252 17.754 1.00111.73 C
ANISOU 1343 CA ALA A 207 13158 14366 14928 3514 -1680 562 C
ATOM 1344 C ALA A 207 38.932 -2.291 18.215 1.00113.77 C
ANISOU 1344 C ALA A 207 13033 14826 15371 3450 -1722 502 C
ATOM 1345 O ALA A 207 37.745 -2.142 17.906 1.00107.65 O
ANISOU 1345 O ALA A 207 12075 14162 14663 3620 -1898 418 O
ATOM 1346 CB ALA A 207 40.401 -1.542 16.321 1.00112.30 C
ANISOU 1346 CB ALA A 207 13517 14346 14807 3540 -1798 615 C
ATOM 1347 N ASP A 208 39.348 -3.333 18.947 1.00117.08 N
ANISOU 1347 N ASP A 208 13322 15293 15869 3217 -1572 529 N
ATOM 1348 CA ASP A 208 38.433 -4.404 19.313 1.00119.07 C
ANISOU 1348 CA ASP A 208 13238 15729 16275 3137 -1597 476 C
ATOM 1349 C ASP A 208 38.701 -4.816 20.748 1.00109.85 C
ANISOU 1349 C ASP A 208 11915 14585 15238 2958 -1373 465 C
ATOM 1350 O ASP A 208 39.745 -4.504 21.328 1.00112.81 O
ANISOU 1350 O ASP A 208 12467 14833 15564 2869 -1228 502 O
ATOM 1351 CB ASP A 208 38.667 -5.688 18.489 1.00126.05 C
ANISOU 1351 CB ASP A 208 14168 16640 17084 3011 -1675 527 C
ATOM 1352 CG ASP A 208 38.546 -5.493 16.994 1.00138.83 C
ANISOU 1352 CG ASP A 208 15994 18212 18545 3158 -1895 542 C
ATOM 1353 OD1 ASP A 208 37.938 -4.510 16.525 1.00147.91 O
ANISOU 1353 OD1 ASP A 208 17182 19351 19665 3381 -2044 486 O
ATOM 1354 OD2 ASP A 208 39.086 -6.364 16.277 1.00137.99 O
ANISOU 1354 OD2 ASP A 208 16032 18065 18331 3054 -1923 606 O
ATOM 1355 N ASP A 209 37.727 -5.534 21.309 1.00103.65 N
ANISOU 1355 N ASP A 209 10797 13972 14615 2908 -1353 396 N
ATOM 1356 CA ASP A 209 37.827 -5.927 22.702 1.00104.12 C
ANISOU 1356 CA ASP A 209 10708 14054 14799 2757 -1136 367 C
ATOM 1357 C ASP A 209 38.854 -7.036 22.873 1.00104.93 C
ANISOU 1357 C ASP A 209 10950 14080 14840 2538 -1052 424 C
ATOM 1358 O ASP A 209 39.474 -7.164 23.938 1.00112.59 O
ANISOU 1358 O ASP A 209 11961 14981 15837 2421 -887 404 O
ATOM 1359 CB ASP A 209 36.444 -6.351 23.201 1.00121.90 C
ANISOU 1359 CB ASP A 209 12558 16524 17234 2769 -1115 266 C
ATOM 1360 CG ASP A 209 35.641 -5.184 23.761 1.00132.41 C
ANISOU 1360 CG ASP A 209 13732 17902 18675 2954 -1080 180 C
ATOM 1361 OD1 ASP A 209 36.267 -4.136 24.066 1.00142.08 O
ANISOU 1361 OD1 ASP A 209 15165 18972 19846 3029 -1024 210 O
ATOM 1362 OD2 ASP A 209 34.393 -5.310 23.863 1.00125.85 O
ANISOU 1362 OD2 ASP A 209 12567 17268 17984 3023 -1115 72 O
ATOM 1363 N LEU A 210 39.029 -7.845 21.823 1.00 95.39 N
ANISOU 1363 N LEU A 210 9825 12880 13539 2495 -1178 479 N
ATOM 1364 CA LEU A 210 39.777 -9.099 21.811 1.00 77.62 C
ANISOU 1364 CA LEU A 210 7668 10585 11238 2310 -1137 520 C
ATOM 1365 C LEU A 210 41.263 -8.884 21.573 1.00 81.33 C
ANISOU 1365 C LEU A 210 8487 10871 11543 2267 -1093 578 C
ATOM 1366 O LEU A 210 42.096 -9.615 22.130 1.00 85.34 O
ANISOU 1366 O LEU A 210 9088 11325 12013 2130 -997 569 O
ATOM 1367 CB LEU A 210 39.215 -10.048 20.750 1.00 67.06 C
ANISOU 1367 CB LEU A 210 6257 9355 9870 2296 -1301 548 C
ATOM 1368 CG LEU A 210 39.913 -11.405 20.615 1.00 57.19 C
ANISOU 1368 CG LEU A 210 5113 8088 8527 2156 -1289 569 C
ATOM 1369 CD1 LEU A 210 39.847 -12.191 21.915 1.00 42.99 C
ANISOU 1369 CD1 LEU A 210 3146 6386 6801 2051 -1134 468 C
ATOM 1370 CD2 LEU A 210 39.327 -12.197 19.463 1.00 55.05 C
ANISOU 1370 CD2 LEU A 210 4794 7957 8165 2197 -1495 558 C
ATOM 1371 N ALA A 211 41.585 -7.949 20.675 1.00 80.16 N
ANISOU 1371 N ALA A 211 8534 10646 11278 2393 -1168 627 N
ATOM 1372 CA ALA A 211 42.971 -7.681 20.304 1.00 68.01 C
ANISOU 1372 CA ALA A 211 7303 8959 9578 2355 -1109 684 C
ATOM 1373 C ALA A 211 43.862 -7.377 21.496 1.00 56.09 C
ANISOU 1373 C ALA A 211 5854 7396 8063 2268 -944 650 C
ATOM 1374 O ALA A 211 44.952 -7.964 21.581 1.00 50.79 O
ANISOU 1374 O ALA A 211 5330 6675 7294 2158 -868 672 O
ATOM 1375 CB ALA A 211 42.997 -6.521 19.296 1.00 66.26 C
ANISOU 1375 CB ALA A 211 7258 8667 9251 2524 -1194 722 C
ATOM 1376 N PRO A 212 43.506 -6.476 22.413 1.00 59.53 N
ANISOU 1376 N PRO A 212 6193 7845 8579 2323 -886 599 N
ATOM 1377 CA PRO A 212 44.387 -6.279 23.570 1.00 60.11 C
ANISOU 1377 CA PRO A 212 6338 7883 8620 2235 -742 570 C
ATOM 1378 C PRO A 212 44.588 -7.542 24.388 1.00 45.04 C
ANISOU 1378 C PRO A 212 4364 6028 6721 2093 -671 529 C
ATOM 1379 O PRO A 212 45.701 -7.788 24.869 1.00 38.01 O
ANISOU 1379 O PRO A 212 3618 5106 5717 2008 -581 549 O
ATOM 1380 CB PRO A 212 43.676 -5.178 24.373 1.00 68.85 C
ANISOU 1380 CB PRO A 212 7322 9006 9833 2337 -708 516 C
ATOM 1381 CG PRO A 212 42.256 -5.199 23.900 1.00 69.78 C
ANISOU 1381 CG PRO A 212 7220 9214 10081 2449 -811 495 C
ATOM 1382 CD PRO A 212 42.309 -5.619 22.464 1.00 71.28 C
ANISOU 1382 CD PRO A 212 7510 9393 10178 2479 -946 564 C
ATOM 1383 N LYS A 213 43.567 -8.397 24.494 1.00 46.34 N
ANISOU 1383 N LYS A 213 4316 6280 7011 2070 -708 482 N
ATOM 1384 CA LYS A 213 43.741 -9.623 25.263 1.00 47.12 C
ANISOU 1384 CA LYS A 213 4375 6426 7104 1945 -633 438 C
ATOM 1385 C LYS A 213 44.695 -10.583 24.578 1.00 48.94 C
ANISOU 1385 C LYS A 213 4800 6616 7180 1874 -657 507 C
ATOM 1386 O LYS A 213 45.600 -11.124 25.221 1.00 69.98 O
ANISOU 1386 O LYS A 213 7585 9269 9734 1798 -562 525 O
ATOM 1387 CB LYS A 213 42.400 -10.314 25.498 1.00 45.51 C
ANISOU 1387 CB LYS A 213 3869 6329 7093 1924 -642 365 C
ATOM 1388 CG LYS A 213 41.318 -9.492 26.180 1.00 40.62 C
ANISOU 1388 CG LYS A 213 3002 5771 6659 1994 -576 301 C
ATOM 1389 CD LYS A 213 40.101 -10.380 26.327 1.00 47.01 C
ANISOU 1389 CD LYS A 213 3486 6798 7578 1989 -537 244 C
ATOM 1390 CE LYS A 213 38.960 -9.722 27.044 1.00 59.06 C
ANISOU 1390 CE LYS A 213 4729 8441 9271 2059 -423 179 C
ATOM 1391 NZ LYS A 213 38.559 -10.635 28.173 1.00 67.80 N
ANISOU 1391 NZ LYS A 213 5631 9730 10401 1964 -210 62 N
ATOM 1392 N ILE A 214 44.562 -10.743 23.261 1.00 38.10 N
ANISOU 1392 N ILE A 214 3474 5217 5786 1910 -776 565 N
ATOM 1393 CA ILE A 214 45.489 -11.621 22.553 1.00 47.97 C
ANISOU 1393 CA ILE A 214 4917 6417 6893 1851 -781 631 C
ATOM 1394 C ILE A 214 46.890 -11.039 22.578 1.00 55.20 C
ANISOU 1394 C ILE A 214 6048 7254 7671 1840 -675 682 C
ATOM 1395 O ILE A 214 47.873 -11.755 22.832 1.00 57.19 O
ANISOU 1395 O ILE A 214 6412 7491 7825 1766 -588 713 O
ATOM 1396 CB ILE A 214 45.022 -11.866 21.108 1.00 48.86 C
ANISOU 1396 CB ILE A 214 5046 6513 7004 1897 -930 689 C
ATOM 1397 CG1 ILE A 214 43.661 -12.561 21.097 1.00 56.07 C
ANISOU 1397 CG1 ILE A 214 5701 7535 8068 1885 -1036 655 C
ATOM 1398 CG2 ILE A 214 46.072 -12.665 20.353 1.00 32.50 C
ANISOU 1398 CG2 ILE A 214 3199 4370 4780 1844 -909 758 C
ATOM 1399 CD1 ILE A 214 42.988 -12.589 19.726 1.00 60.41 C
ANISOU 1399 CD1 ILE A 214 6229 8117 8608 1953 -1205 728 C
ATOM 1400 N TYR A 215 47.007 -9.730 22.338 1.00 31.99 N
ANISOU 1400 N TYR A 215 3152 4269 4734 1918 -676 694 N
ATOM 1401 CA TYR A 215 48.326 -9.125 22.259 1.00 39.21 C
ANISOU 1401 CA TYR A 215 4240 5113 5545 1905 -578 738 C
ATOM 1402 C TYR A 215 49.050 -9.195 23.594 1.00 53.24 C
ANISOU 1402 C TYR A 215 6011 6915 7304 1828 -457 721 C
ATOM 1403 O TYR A 215 50.248 -9.487 23.639 1.00 54.74 O
ANISOU 1403 O TYR A 215 6304 7078 7419 1770 -374 760 O
ATOM 1404 CB TYR A 215 48.222 -7.677 21.809 1.00 32.30 C
ANISOU 1404 CB TYR A 215 3416 4178 4678 2011 -604 752 C
ATOM 1405 CG TYR A 215 49.559 -6.983 21.850 1.00 51.15 C
ANISOU 1405 CG TYR A 215 5951 6494 6988 1991 -493 788 C
ATOM 1406 CD1 TYR A 215 50.494 -7.196 20.852 1.00 59.06 C
ANISOU 1406 CD1 TYR A 215 7104 7433 7904 1978 -454 845 C
ATOM 1407 CD2 TYR A 215 49.906 -6.141 22.899 1.00 40.36 C
ANISOU 1407 CD2 TYR A 215 4565 5124 5647 1983 -420 766 C
ATOM 1408 CE1 TYR A 215 51.728 -6.575 20.880 1.00 62.81 C
ANISOU 1408 CE1 TYR A 215 7680 7845 8339 1959 -343 874 C
ATOM 1409 CE2 TYR A 215 51.146 -5.510 22.932 1.00 30.37 C
ANISOU 1409 CE2 TYR A 215 3410 3793 4337 1960 -327 799 C
ATOM 1410 CZ TYR A 215 52.047 -5.733 21.919 1.00 45.91 C
ANISOU 1410 CZ TYR A 215 5501 5704 6240 1947 -287 852 C
ATOM 1411 OH TYR A 215 53.276 -5.120 21.928 1.00 57.46 O
ANISOU 1411 OH TYR A 215 7043 7099 7688 1927 -189 880 O
ATOM 1412 N HIS A 216 48.354 -8.902 24.696 1.00 58.51 N
ANISOU 1412 N HIS A 216 6552 7631 8048 1836 -445 663 N
ATOM 1413 CA HIS A 216 49.019 -8.892 25.987 1.00 40.05 C
ANISOU 1413 CA HIS A 216 4228 5303 5684 1776 -345 657 C
ATOM 1414 C HIS A 216 49.202 -10.282 26.557 1.00 36.47 C
ANISOU 1414 C HIS A 216 3771 4891 5194 1694 -311 663 C
ATOM 1415 O HIS A 216 50.175 -10.506 27.281 1.00 54.31 O
ANISOU 1415 O HIS A 216 6103 7133 7399 1643 -244 690 O
ATOM 1416 CB HIS A 216 48.243 -8.018 26.958 1.00 37.94 C
ANISOU 1416 CB HIS A 216 3852 5059 5505 1826 -332 595 C
ATOM 1417 CG HIS A 216 48.502 -6.565 26.751 1.00 45.09 C
ANISOU 1417 CG HIS A 216 4816 5900 6416 1899 -332 606 C
ATOM 1418 ND1 HIS A 216 49.637 -5.941 27.225 1.00 48.19 N
ANISOU 1418 ND1 HIS A 216 5313 6242 6757 1869 -264 636 N
ATOM 1419 CD2 HIS A 216 47.816 -5.628 26.056 1.00 47.94 C
ANISOU 1419 CD2 HIS A 216 5154 6231 6829 2008 -398 598 C
ATOM 1420 CE1 HIS A 216 49.615 -4.668 26.867 1.00 54.24 C
ANISOU 1420 CE1 HIS A 216 6122 6946 7540 1951 -277 642 C
ATOM 1421 NE2 HIS A 216 48.524 -4.455 26.151 1.00 58.21 N
ANISOU 1421 NE2 HIS A 216 6564 7458 8095 2043 -357 624 N
ATOM 1422 N SER A 217 48.375 -11.245 26.149 1.00 33.18 N
ANISOU 1422 N SER A 217 3283 4517 4809 1688 -367 644 N
ATOM 1423 CA SER A 217 48.692 -12.631 26.432 1.00 27.00 C
ANISOU 1423 CA SER A 217 2542 3748 3968 1620 -339 671 C
ATOM 1424 C SER A 217 50.000 -13.010 25.766 1.00 57.12 C
ANISOU 1424 C SER A 217 6519 7504 7679 1590 -311 743 C
ATOM 1425 O SER A 217 50.897 -13.578 26.403 1.00 84.61 O
ANISOU 1425 O SER A 217 10074 10968 11105 1547 -252 772 O
ATOM 1426 CB SER A 217 47.557 -13.519 25.932 1.00 42.00 C
ANISOU 1426 CB SER A 217 4327 5698 5934 1623 -419 635 C
ATOM 1427 OG SER A 217 46.371 -13.262 26.657 1.00 61.10 O
ANISOU 1427 OG SER A 217 6534 8207 8473 1657 -406 552 O
ATOM 1428 N CYS A 218 50.131 -12.688 24.476 1.00 44.40 N
ANISOU 1428 N CYS A 218 4959 5857 6054 1624 -354 766 N
ATOM 1429 CA CYS A 218 51.366 -13.010 23.765 1.00 53.39 C
ANISOU 1429 CA CYS A 218 6227 6942 7115 1606 -304 820 C
ATOM 1430 C CYS A 218 52.560 -12.264 24.356 1.00 49.97 C
ANISOU 1430 C CYS A 218 5828 6484 6675 1592 -220 830 C
ATOM 1431 O CYS A 218 53.654 -12.833 24.504 1.00 40.12 O
ANISOU 1431 O CYS A 218 4632 5217 5394 1561 -167 855 O
ATOM 1432 CB CYS A 218 51.206 -12.675 22.284 1.00 57.89 C
ANISOU 1432 CB CYS A 218 6856 7468 7671 1659 -361 843 C
ATOM 1433 SG CYS A 218 50.001 -13.717 21.404 1.00 62.40 S
ANISOU 1433 SG CYS A 218 7400 8053 8255 1671 -498 843 S
ATOM 1434 N PHE A 219 52.361 -10.991 24.716 1.00 44.75 N
ANISOU 1434 N PHE A 219 5128 5817 6059 1624 -221 807 N
ATOM 1435 CA PHE A 219 53.450 -10.174 25.236 1.00 37.46 C
ANISOU 1435 CA PHE A 219 4228 4860 5147 1614 -161 813 C
ATOM 1436 C PHE A 219 53.961 -10.762 26.539 1.00 37.86 C
ANISOU 1436 C PHE A 219 4258 4930 5197 1565 -140 801 C
ATOM 1437 O PHE A 219 55.172 -10.904 26.744 1.00 57.59 O
ANISOU 1437 O PHE A 219 6783 7401 7697 1545 -114 813 O
ATOM 1438 CB PHE A 219 52.952 -8.754 25.491 1.00 34.15 C
ANISOU 1438 CB PHE A 219 3778 4423 4774 1666 -176 787 C
ATOM 1439 CG PHE A 219 54.039 -7.783 25.861 1.00 41.66 C
ANISOU 1439 CG PHE A 219 4758 5323 5747 1663 -128 793 C
ATOM 1440 CD1 PHE A 219 54.454 -7.648 27.181 1.00 44.22 C
ANISOU 1440 CD1 PHE A 219 5047 5654 6100 1630 -116 768 C
ATOM 1441 CD2 PHE A 219 54.521 -6.893 24.913 1.00 48.81 C
ANISOU 1441 CD2 PHE A 219 5730 6160 6654 1706 -104 821 C
ATOM 1442 CE1 PHE A 219 55.428 -6.725 27.515 1.00 48.62 C
ANISOU 1442 CE1 PHE A 219 5616 6157 6699 1632 -94 764 C
ATOM 1443 CE2 PHE A 219 55.469 -5.953 25.242 1.00 41.25 C
ANISOU 1443 CE2 PHE A 219 4790 5145 5737 1706 -61 823 C
ATOM 1444 CZ PHE A 219 55.928 -5.867 26.543 1.00 43.40 C
ANISOU 1444 CZ PHE A 219 5006 5431 6052 1667 -63 790 C
ATOM 1445 N PHE A 220 53.033 -11.150 27.416 1.00 27.67 N
ANISOU 1445 N PHE A 220 2918 3681 3914 1557 -161 774 N
ATOM 1446 CA PHE A 220 53.407 -11.719 28.697 1.00 24.55 C
ANISOU 1446 CA PHE A 220 2532 3288 3506 1528 -151 767 C
ATOM 1447 C PHE A 220 54.130 -13.038 28.503 1.00 24.15 C
ANISOU 1447 C PHE A 220 2548 3223 3405 1503 -154 798 C
ATOM 1448 O PHE A 220 55.162 -13.294 29.135 1.00 40.68 O
ANISOU 1448 O PHE A 220 4677 5286 5495 1498 -163 800 O
ATOM 1449 CB PHE A 220 52.171 -11.948 29.561 1.00 24.70 C
ANISOU 1449 CB PHE A 220 2491 3349 3545 1536 -155 737 C
ATOM 1450 CG PHE A 220 52.474 -12.639 30.849 1.00 32.95 C
ANISOU 1450 CG PHE A 220 3581 4378 4560 1521 -147 741 C
ATOM 1451 CD1 PHE A 220 53.229 -12.010 31.822 1.00 44.73 C
ANISOU 1451 CD1 PHE A 220 5103 5833 6061 1528 -153 730 C
ATOM 1452 CD2 PHE A 220 52.095 -13.948 31.044 1.00 24.11 C
ANISOU 1452 CD2 PHE A 220 2497 3263 3399 1508 -151 760 C
ATOM 1453 CE1 PHE A 220 53.525 -12.655 32.997 1.00 38.89 C
ANISOU 1453 CE1 PHE A 220 4432 5057 5285 1532 -172 738 C
ATOM 1454 CE2 PHE A 220 52.403 -14.603 32.212 1.00 42.25 C
ANISOU 1454 CE2 PHE A 220 4882 5533 5640 1526 -143 790 C
ATOM 1455 CZ PHE A 220 53.120 -13.958 33.187 1.00 40.54 C
ANISOU 1455 CZ PHE A 220 4703 5266 5435 1532 -168 771 C
ATOM 1456 N ILE A 221 53.590 -13.905 27.644 1.00 24.13 N
ANISOU 1456 N ILE A 221 2563 3235 3370 1499 -163 818 N
ATOM 1457 CA ILE A 221 54.191 -15.225 27.511 1.00 23.89 C
ANISOU 1457 CA ILE A 221 2612 3180 3285 1487 -164 847 C
ATOM 1458 C ILE A 221 55.587 -15.119 26.904 1.00 31.32 C
ANISOU 1458 C ILE A 221 3586 4084 4229 1500 -140 861 C
ATOM 1459 O ILE A 221 56.495 -15.879 27.271 1.00 32.55 O
ANISOU 1459 O ILE A 221 3787 4211 4370 1509 -149 867 O
ATOM 1460 CB ILE A 221 53.278 -16.132 26.662 1.00 26.91 C
ANISOU 1460 CB ILE A 221 3011 3574 3638 1483 -188 864 C
ATOM 1461 CG1 ILE A 221 52.060 -16.612 27.461 1.00 23.94 C
ANISOU 1461 CG1 ILE A 221 2592 3228 3275 1473 -214 851 C
ATOM 1462 CG2 ILE A 221 54.064 -17.341 26.164 1.00 31.52 C
ANISOU 1462 CG2 ILE A 221 3703 4114 4160 1482 -180 900 C
ATOM 1463 CD1 ILE A 221 52.390 -17.390 28.705 1.00 40.72 C
ANISOU 1463 CD1 ILE A 221 4798 5319 5354 1464 -205 868 C
ATOM 1464 N VAL A 222 55.787 -14.176 25.978 1.00 39.30 N
ANISOU 1464 N VAL A 222 4576 5088 5268 1513 -113 866 N
ATOM 1465 CA VAL A 222 57.025 -14.122 25.196 1.00 37.28 C
ANISOU 1465 CA VAL A 222 4344 4794 5025 1533 -72 886 C
ATOM 1466 C VAL A 222 58.128 -13.337 25.904 1.00 31.88 C
ANISOU 1466 C VAL A 222 3607 4088 4416 1539 -72 864 C
ATOM 1467 O VAL A 222 59.292 -13.736 25.877 1.00 30.14 O
ANISOU 1467 O VAL A 222 3378 3841 4232 1559 -70 862 O
ATOM 1468 CB VAL A 222 56.765 -13.550 23.788 1.00 39.22 C
ANISOU 1468 CB VAL A 222 4621 5022 5260 1557 -40 912 C
ATOM 1469 CG1 VAL A 222 58.067 -12.990 23.207 1.00 51.36 C
ANISOU 1469 CG1 VAL A 222 6163 6512 6840 1582 27 931 C
ATOM 1470 CG2 VAL A 222 56.215 -14.624 22.874 1.00 33.52 C
ANISOU 1470 CG2 VAL A 222 3965 4297 4473 1564 -53 935 C
ATOM 1471 N THR A 223 57.804 -12.223 26.549 1.00 41.92 N
ANISOU 1471 N THR A 223 4837 5365 5727 1532 -87 839 N
ATOM 1472 CA THR A 223 58.816 -11.401 27.201 1.00 45.29 C
ANISOU 1472 CA THR A 223 5212 5760 6238 1540 -105 809 C
ATOM 1473 C THR A 223 59.042 -11.760 28.662 1.00 51.77 C
ANISOU 1473 C THR A 223 6014 6579 7077 1537 -183 771 C
ATOM 1474 O THR A 223 59.957 -11.209 29.292 1.00 64.30 O
ANISOU 1474 O THR A 223 7550 8134 8747 1553 -233 733 O
ATOM 1475 CB THR A 223 58.437 -9.925 27.089 1.00 51.14 C
ANISOU 1475 CB THR A 223 5936 6484 7009 1547 -82 803 C
ATOM 1476 OG1 THR A 223 57.304 -9.656 27.931 1.00 56.03 O
ANISOU 1476 OG1 THR A 223 6551 7134 7606 1541 -111 783 O
ATOM 1477 CG2 THR A 223 58.080 -9.582 25.661 1.00 55.72 C
ANISOU 1477 CG2 THR A 223 6565 7047 7558 1569 -25 844 C
ATOM 1478 N TYR A 224 58.216 -12.634 29.226 1.00 40.01 N
ANISOU 1478 N TYR A 224 4570 5114 5519 1525 -203 780 N
ATOM 1479 CA TYR A 224 58.386 -12.957 30.631 1.00 27.68 C
ANISOU 1479 CA TYR A 224 3024 3532 3961 1534 -278 757 C
ATOM 1480 C TYR A 224 58.381 -14.456 30.850 1.00 29.16 C
ANISOU 1480 C TYR A 224 3291 3709 4080 1545 -306 782 C
ATOM 1481 O TYR A 224 59.431 -15.050 31.100 1.00 53.57 O
ANISOU 1481 O TYR A 224 6394 6759 7199 1580 -372 777 O
ATOM 1482 CB TYR A 224 57.293 -12.335 31.500 1.00 32.17 C
ANISOU 1482 CB TYR A 224 3592 4118 4512 1524 -268 746 C
ATOM 1483 CG TYR A 224 57.557 -12.539 32.980 1.00 33.95 C
ANISOU 1483 CG TYR A 224 3858 4303 4738 1542 -345 734 C
ATOM 1484 CD1 TYR A 224 58.337 -11.643 33.695 1.00 45.39 C
ANISOU 1484 CD1 TYR A 224 5270 5709 6267 1557 -411 703 C
ATOM 1485 CD2 TYR A 224 57.071 -13.655 33.647 1.00 29.49 C
ANISOU 1485 CD2 TYR A 224 3384 3727 4092 1548 -360 761 C
ATOM 1486 CE1 TYR A 224 58.589 -11.822 35.044 1.00 48.08 C
ANISOU 1486 CE1 TYR A 224 5663 6000 6606 1577 -498 709 C
ATOM 1487 CE2 TYR A 224 57.328 -13.852 34.993 1.00 37.58 C
ANISOU 1487 CE2 TYR A 224 4486 4697 5094 1572 -435 770 C
ATOM 1488 CZ TYR A 224 58.092 -12.936 35.686 1.00 46.13 C
ANISOU 1488 CZ TYR A 224 5530 5742 6254 1587 -507 748 C
ATOM 1489 OH TYR A 224 58.349 -13.132 37.027 1.00 49.85 O
ANISOU 1489 OH TYR A 224 6098 6155 6686 1616 -590 776 O
ATOM 1490 N LEU A 225 57.212 -15.084 30.731 1.00 24.50 N
ANISOU 1490 N LEU A 225 2749 3146 3412 1526 -267 806 N
ATOM 1491 CA LEU A 225 57.055 -16.427 31.286 1.00 29.38 C
ANISOU 1491 CA LEU A 225 3475 3735 3954 1538 -299 832 C
ATOM 1492 C LEU A 225 57.900 -17.463 30.549 1.00 28.79 C
ANISOU 1492 C LEU A 225 3451 3631 3856 1565 -310 851 C
ATOM 1493 O LEU A 225 58.671 -18.198 31.174 1.00 44.70 O
ANISOU 1493 O LEU A 225 5536 5595 5854 1607 -378 858 O
ATOM 1494 CB LEU A 225 55.575 -16.823 31.278 1.00 37.09 C
ANISOU 1494 CB LEU A 225 4475 4740 4878 1511 -255 851 C
ATOM 1495 CG LEU A 225 55.218 -18.181 31.876 1.00 25.36 C
ANISOU 1495 CG LEU A 225 3135 3201 3298 1514 -277 893 C
ATOM 1496 CD1 LEU A 225 55.422 -18.148 33.374 1.00 31.07 C
ANISOU 1496 CD1 LEU A 225 3955 3880 3972 1551 -313 908 C
ATOM 1497 CD2 LEU A 225 53.785 -18.512 31.547 1.00 24.45 C
ANISOU 1497 CD2 LEU A 225 3008 3153 3129 1534 -198 940 C
ATOM 1498 N ALA A 226 57.777 -17.541 29.224 1.00 36.25 N
ANISOU 1498 N ALA A 226 4373 4602 4799 1554 -250 863 N
ATOM 1499 CA ALA A 226 58.536 -18.555 28.492 1.00 35.93 C
ANISOU 1499 CA ALA A 226 4390 4529 4732 1591 -247 883 C
ATOM 1500 C ALA A 226 60.049 -18.397 28.590 1.00 31.54 C
ANISOU 1500 C ALA A 226 3782 3942 4260 1647 -290 861 C
ATOM 1501 O ALA A 226 60.727 -19.390 28.916 1.00 35.75 O
ANISOU 1501 O ALA A 226 4378 4429 4774 1706 -343 868 O
ATOM 1502 CB ALA A 226 58.090 -18.568 27.024 1.00 35.52 C
ANISOU 1502 CB ALA A 226 4335 4501 4660 1573 -175 905 C
ATOM 1503 N PRO A 227 60.646 -17.238 28.292 1.00 36.64 N
ANISOU 1503 N PRO A 227 4314 4600 5006 1645 -276 834 N
ATOM 1504 CA PRO A 227 62.111 -17.141 28.426 1.00 40.61 C
ANISOU 1504 CA PRO A 227 4736 5067 5628 1708 -335 801 C
ATOM 1505 C PRO A 227 62.612 -17.407 29.835 1.00 54.98 C
ANISOU 1505 C PRO A 227 6552 6846 7491 1746 -469 781 C
ATOM 1506 O PRO A 227 63.647 -18.067 30.001 1.00 75.05 O
ANISOU 1506 O PRO A 227 9068 9349 10100 1823 -542 774 O
ATOM 1507 CB PRO A 227 62.411 -15.706 27.960 1.00 36.50 C
ANISOU 1507 CB PRO A 227 4106 4562 5202 1685 -289 773 C
ATOM 1508 CG PRO A 227 61.103 -14.968 28.097 1.00 50.68 C
ANISOU 1508 CG PRO A 227 5934 6395 6927 1618 -245 791 C
ATOM 1509 CD PRO A 227 60.043 -15.988 27.796 1.00 50.19 C
ANISOU 1509 CD PRO A 227 5974 6354 6743 1598 -212 832 C
ATOM 1510 N LEU A 228 61.876 -16.981 30.861 1.00 46.10 N
ANISOU 1510 N LEU A 228 5460 5727 6328 1706 -502 782 N
ATOM 1511 CA LEU A 228 62.370 -17.219 32.207 1.00 38.96 C
ANISOU 1511 CA LEU A 228 4577 4780 5448 1747 -626 788 C
ATOM 1512 C LEU A 228 62.180 -18.670 32.628 1.00 55.39 C
ANISOU 1512 C LEU A 228 6827 6832 7389 1793 -651 834 C
ATOM 1513 O LEU A 228 63.024 -19.210 33.347 1.00 74.15 O
ANISOU 1513 O LEU A 228 9233 9172 9769 1875 -751 846 O
ATOM 1514 CB LEU A 228 61.723 -16.251 33.201 1.00 34.24 C
ANISOU 1514 CB LEU A 228 3978 4187 4845 1702 -644 781 C
ATOM 1515 CG LEU A 228 62.116 -14.779 32.945 1.00 37.87 C
ANISOU 1515 CG LEU A 228 4289 4654 5445 1677 -641 728 C
ATOM 1516 CD1 LEU A 228 61.293 -13.772 33.757 1.00 27.51 C
ANISOU 1516 CD1 LEU A 228 2992 3349 4111 1637 -631 720 C
ATOM 1517 CD2 LEU A 228 63.608 -14.559 33.160 1.00 46.89 C
ANISOU 1517 CD2 LEU A 228 5290 5752 6772 1728 -749 705 C
ATOM 1518 N GLY A 229 61.120 -19.337 32.169 1.00 51.39 N
ANISOU 1518 N GLY A 229 6438 6338 6752 1754 -565 859 N
ATOM 1519 CA GLY A 229 60.988 -20.758 32.454 1.00 42.89 C
ANISOU 1519 CA GLY A 229 5548 5213 5534 1800 -582 895 C
ATOM 1520 C GLY A 229 62.044 -21.593 31.754 1.00 53.84 C
ANISOU 1520 C GLY A 229 6938 6576 6944 1889 -601 894 C
ATOM 1521 O GLY A 229 62.619 -22.518 32.348 1.00 69.74 O
ANISOU 1521 O GLY A 229 9076 8537 8885 1983 -677 902 O
ATOM 1522 N LEU A 230 62.349 -21.257 30.495 1.00 51.36 N
ANISOU 1522 N LEU A 230 6503 6293 6719 1876 -533 879 N
ATOM 1523 CA LEU A 230 63.412 -21.980 29.806 1.00 48.32 C
ANISOU 1523 CA LEU A 230 6104 5881 6376 1973 -541 876 C
ATOM 1524 C LEU A 230 64.750 -21.730 30.480 1.00 56.81 C
ANISOU 1524 C LEU A 230 7051 6934 7600 2068 -661 849 C
ATOM 1525 O LEU A 230 65.558 -22.654 30.641 1.00 60.20 O
ANISOU 1525 O LEU A 230 7526 7325 8020 2190 -723 852 O
ATOM 1526 CB LEU A 230 63.483 -21.571 28.335 1.00 36.93 C
ANISOU 1526 CB LEU A 230 4573 4470 4990 1945 -429 869 C
ATOM 1527 CG LEU A 230 62.344 -22.006 27.425 1.00 29.08 C
ANISOU 1527 CG LEU A 230 3694 3494 3862 1880 -319 906 C
ATOM 1528 CD1 LEU A 230 62.399 -21.219 26.127 1.00 31.65 C
ANISOU 1528 CD1 LEU A 230 3928 3856 4243 1849 -218 907 C
ATOM 1529 CD2 LEU A 230 62.457 -23.492 27.156 1.00 29.91 C
ANISOU 1529 CD2 LEU A 230 3967 3544 3854 1949 -312 932 C
ATOM 1530 N MET A 231 64.991 -20.486 30.897 1.00 51.83 N
ANISOU 1530 N MET A 231 6259 6324 7110 2023 -700 821 N
ATOM 1531 CA MET A 231 66.237 -20.176 31.578 1.00 45.55 C
ANISOU 1531 CA MET A 231 5308 5515 6485 2107 -816 805 C
ATOM 1532 C MET A 231 66.318 -20.916 32.901 1.00 58.77 C
ANISOU 1532 C MET A 231 7137 7174 8018 2194 -931 833 C
ATOM 1533 O MET A 231 67.394 -21.366 33.301 1.00 64.70 O
ANISOU 1533 O MET A 231 7845 7919 8817 2332 -1033 823 O
ATOM 1534 CB MET A 231 66.344 -18.671 31.790 1.00 35.03 C
ANISOU 1534 CB MET A 231 3797 4198 5315 2029 -826 773 C
ATOM 1535 CG MET A 231 66.854 -17.937 30.571 1.00 44.87 C
ANISOU 1535 CG MET A 231 4879 5441 6730 2010 -757 699 C
ATOM 1536 SD MET A 231 67.065 -16.172 30.866 1.00 48.56 S
ANISOU 1536 SD MET A 231 5181 5916 7355 1932 -775 618 S
ATOM 1537 CE MET A 231 65.630 -15.511 30.000 1.00 47.37 C
ANISOU 1537 CE MET A 231 5173 5821 7003 1848 -627 615 C
ATOM 1538 N ALA A 232 65.195 -21.034 33.610 1.00 61.63 N
ANISOU 1538 N ALA A 232 7693 7529 8193 2131 -919 851 N
ATOM 1539 CA ALA A 232 65.225 -21.746 34.876 1.00 36.18 C
ANISOU 1539 CA ALA A 232 4685 4268 4795 2220 -1030 853 C
ATOM 1540 C ALA A 232 65.539 -23.222 34.684 1.00 60.19 C
ANISOU 1540 C ALA A 232 7917 7252 7700 2340 -1058 848 C
ATOM 1541 O ALA A 232 66.339 -23.787 35.433 1.00 75.11 O
ANISOU 1541 O ALA A 232 9906 9105 9529 2487 -1200 817 O
ATOM 1542 CB ALA A 232 63.886 -21.581 35.586 1.00 34.78 C
ANISOU 1542 CB ALA A 232 4683 4073 4458 2120 -982 872 C
ATOM 1543 N MET A 233 64.975 -23.857 33.654 1.00 46.56 N
ANISOU 1543 N MET A 233 6256 5515 5922 2295 -937 869 N
ATOM 1544 CA MET A 233 65.317 -25.264 33.432 1.00 44.43 C
ANISOU 1544 CA MET A 233 6184 5178 5519 2417 -957 865 C
ATOM 1545 C MET A 233 66.755 -25.421 32.955 1.00 45.84 C
ANISOU 1545 C MET A 233 6188 5368 5861 2565 -1026 838 C
ATOM 1546 O MET A 233 67.445 -26.375 33.344 1.00 42.43 O
ANISOU 1546 O MET A 233 5896 4881 5343 2733 -1131 812 O
ATOM 1547 CB MET A 233 64.344 -25.910 32.455 1.00 56.87 C
ANISOU 1547 CB MET A 233 7881 6736 6989 2332 -810 896 C
ATOM 1548 CG MET A 233 62.948 -26.103 33.026 1.00 61.90 C
ANISOU 1548 CG MET A 233 8727 7340 7454 2217 -753 922 C
ATOM 1549 SD MET A 233 61.778 -26.511 31.718 1.00 61.79 S
ANISOU 1549 SD MET A 233 8750 7336 7393 2092 -588 959 S
ATOM 1550 CE MET A 233 61.600 -24.890 30.957 1.00 64.36 C
ANISOU 1550 CE MET A 233 8738 7781 7935 1987 -533 952 C
ATOM 1551 N ALA A 234 67.227 -24.482 32.129 1.00 52.31 N
ANISOU 1551 N ALA A 234 6708 6245 6922 2514 -969 837 N
ATOM 1552 CA ALA A 234 68.616 -24.502 31.689 1.00 43.85 C
ANISOU 1552 CA ALA A 234 5420 5180 6060 2647 -1015 810 C
ATOM 1553 C ALA A 234 69.561 -24.354 32.875 1.00 49.20 C
ANISOU 1553 C ALA A 234 6031 5874 6789 2782 -1196 778 C
ATOM 1554 O ALA A 234 70.549 -25.081 32.985 1.00 49.41 O
ANISOU 1554 O ALA A 234 6047 5883 6843 2969 -1296 744 O
ATOM 1555 CB ALA A 234 68.849 -23.400 30.661 1.00 41.82 C
ANISOU 1555 CB ALA A 234 4883 4957 6052 2546 -908 799 C
ATOM 1556 N TYR A 235 69.305 -23.372 33.742 1.00 54.96 N
ANISOU 1556 N TYR A 235 6709 6642 7532 2702 -1247 777 N
ATOM 1557 CA TYR A 235 70.187 -23.135 34.877 1.00 57.30 C
ANISOU 1557 CA TYR A 235 6952 6965 7853 2829 -1436 731 C
ATOM 1558 C TYR A 235 70.056 -24.246 35.899 1.00 57.40 C
ANISOU 1558 C TYR A 235 7318 6901 7592 2960 -1593 690 C
ATOM 1559 O TYR A 235 71.018 -24.561 36.600 1.00 64.11 O
ANISOU 1559 O TYR A 235 8177 7743 8438 3141 -1790 623 O
ATOM 1560 CB TYR A 235 69.888 -21.778 35.518 1.00 52.16 C
ANISOU 1560 CB TYR A 235 6188 6368 7261 2706 -1443 738 C
ATOM 1561 CG TYR A 235 70.515 -20.624 34.771 1.00 64.43 C
ANISOU 1561 CG TYR A 235 7379 7994 9108 2644 -1346 754 C
ATOM 1562 CD1 TYR A 235 69.735 -19.694 34.100 1.00 75.88 C
ANISOU 1562 CD1 TYR A 235 8748 9440 10643 2459 -1184 796 C
ATOM 1563 CD2 TYR A 235 71.896 -20.501 34.684 1.00 66.88 C
ANISOU 1563 CD2 TYR A 235 7433 8367 9609 2782 -1412 716 C
ATOM 1564 CE1 TYR A 235 70.313 -18.647 33.400 1.00 75.65 C
ANISOU 1564 CE1 TYR A 235 8425 9446 10873 2406 -1084 808 C
ATOM 1565 CE2 TYR A 235 72.483 -19.457 33.988 1.00 54.85 C
ANISOU 1565 CE2 TYR A 235 5587 6915 8337 2730 -1284 738 C
ATOM 1566 CZ TYR A 235 71.687 -18.536 33.346 1.00 66.13 C
ANISOU 1566 CZ TYR A 235 6972 8318 9834 2541 -1108 795 C
ATOM 1567 OH TYR A 235 72.245 -17.488 32.648 1.00 78.90 O
ANISOU 1567 OH TYR A 235 8346 10004 11629 2474 -948 796 O
ATOM 1568 N PHE A 236 68.905 -24.904 35.939 1.00 50.44 N
ANISOU 1568 N PHE A 236 6738 5949 6479 2884 -1510 721 N
ATOM 1569 CA PHE A 236 68.775 -26.079 36.778 1.00 54.17 C
ANISOU 1569 CA PHE A 236 7594 6311 6677 3009 -1628 683 C
ATOM 1570 C PHE A 236 69.678 -27.197 36.275 1.00 68.36 C
ANISOU 1570 C PHE A 236 9433 8069 8474 3206 -1692 653 C
ATOM 1571 O PHE A 236 70.386 -27.837 37.063 1.00 67.44 O
ANISOU 1571 O PHE A 236 9481 7888 8253 3402 -1892 584 O
ATOM 1572 CB PHE A 236 67.311 -26.507 36.753 1.00 62.82 C
ANISOU 1572 CB PHE A 236 8969 7344 7558 2861 -1478 729 C
ATOM 1573 CG PHE A 236 67.042 -27.788 37.450 1.00 80.68 C
ANISOU 1573 CG PHE A 236 11671 9460 9524 2960 -1545 698 C
ATOM 1574 CD1 PHE A 236 66.955 -28.960 36.718 1.00 93.45 C
ANISOU 1574 CD1 PHE A 236 13460 11012 11034 3014 -1473 707 C
ATOM 1575 CD2 PHE A 236 66.935 -27.844 38.826 1.00 82.41 C
ANISOU 1575 CD2 PHE A 236 12166 9587 9559 3006 -1684 652 C
ATOM 1576 CE1 PHE A 236 66.727 -30.154 37.336 1.00101.58 C
ANISOU 1576 CE1 PHE A 236 14931 11883 11780 3103 -1525 673 C
ATOM 1577 CE2 PHE A 236 66.699 -29.043 39.454 1.00 94.03 C
ANISOU 1577 CE2 PHE A 236 14095 10889 10741 3094 -1737 616 C
ATOM 1578 CZ PHE A 236 66.597 -30.200 38.708 1.00106.69 C
ANISOU 1578 CZ PHE A 236 15868 12426 12243 3141 -1655 626 C
ATOM 1579 N GLN A 237 69.697 -27.417 34.958 1.00 83.63 N
ANISOU 1579 N GLN A 237 11223 10030 10523 3171 -1534 694 N
ATOM 1580 CA GLN A 237 70.592 -28.425 34.397 1.00 82.97 C
ANISOU 1580 CA GLN A 237 11154 9909 10462 3367 -1575 668 C
ATOM 1581 C GLN A 237 72.053 -28.018 34.550 1.00 82.21 C
ANISOU 1581 C GLN A 237 10741 9877 10617 3537 -1724 613 C
ATOM 1582 O GLN A 237 72.920 -28.863 34.807 1.00 91.95 O
ANISOU 1582 O GLN A 237 12050 11068 11819 3770 -1876 554 O
ATOM 1583 CB GLN A 237 70.276 -28.690 32.926 1.00 82.98 C
ANISOU 1583 CB GLN A 237 11082 9916 10530 3287 -1366 720 C
ATOM 1584 CG GLN A 237 69.020 -29.484 32.660 1.00 82.90 C
ANISOU 1584 CG GLN A 237 11411 9834 10252 3182 -1240 758 C
ATOM 1585 CD GLN A 237 69.054 -30.121 31.280 1.00 97.79 C
ANISOU 1585 CD GLN A 237 13295 11703 12159 3196 -1094 784 C
ATOM 1586 OE1 GLN A 237 69.009 -29.429 30.261 1.00100.63 O
ANISOU 1586 OE1 GLN A 237 13412 12125 12697 3089 -967 810 O
ATOM 1587 NE2 GLN A 237 69.198 -31.441 31.242 1.00110.98 N
ANISOU 1587 NE2 GLN A 237 15258 13273 13635 3342 -1119 769 N
ATOM 1588 N ILE A 238 72.348 -26.729 34.362 1.00 76.14 N
ANISOU 1588 N ILE A 238 9614 9209 10106 3430 -1677 625 N
ATOM 1589 CA ILE A 238 73.716 -26.254 34.525 1.00 89.86 C
ANISOU 1589 CA ILE A 238 11020 11024 12098 3575 -1800 566 C
ATOM 1590 C ILE A 238 74.177 -26.469 35.955 1.00102.91 C
ANISOU 1590 C ILE A 238 12829 12660 13612 3736 -2087 476 C
ATOM 1591 O ILE A 238 75.315 -26.890 36.212 1.00118.27 O
ANISOU 1591 O ILE A 238 14675 14620 15643 3965 -2269 394 O
ATOM 1592 CB ILE A 238 73.782 -24.757 34.154 1.00 89.60 C
ANISOU 1592 CB ILE A 238 10631 11092 12321 3401 -1675 599 C
ATOM 1593 CG1 ILE A 238 73.737 -24.527 32.639 1.00 81.71 C
ANISOU 1593 CG1 ILE A 238 9429 10089 11527 3299 -1424 655 C
ATOM 1594 CG2 ILE A 238 74.996 -24.089 34.785 1.00 90.28 C
ANISOU 1594 CG2 ILE A 238 10430 11278 12594 3521 -1839 521 C
ATOM 1595 CD1 ILE A 238 73.401 -23.098 32.254 1.00 50.60 C
ANISOU 1595 CD1 ILE A 238 5268 6199 7758 3090 -1276 697 C
ATOM 1596 N PHE A 239 73.277 -26.233 36.908 1.00 94.61 N
ANISOU 1596 N PHE A 239 12045 11564 12340 3630 -2140 481 N
ATOM 1597 CA PHE A 239 73.592 -26.453 38.307 1.00 92.19 C
ANISOU 1597 CA PHE A 239 11962 11201 11865 3772 -2417 389 C
ATOM 1598 C PHE A 239 73.819 -27.932 38.604 1.00 95.16 C
ANISOU 1598 C PHE A 239 12695 11448 12014 3994 -2556 339 C
ATOM 1599 O PHE A 239 74.751 -28.285 39.336 1.00100.84 O
ANISOU 1599 O PHE A 239 13459 12140 12715 4222 -2825 236 O
ATOM 1600 CB PHE A 239 72.462 -25.863 39.150 1.00 89.36 C
ANISOU 1600 CB PHE A 239 11828 10802 11322 3591 -2388 417 C
ATOM 1601 CG PHE A 239 72.378 -26.407 40.536 1.00 93.85 C
ANISOU 1601 CG PHE A 239 12806 11241 11613 3710 -2619 341 C
ATOM 1602 CD1 PHE A 239 71.514 -27.445 40.837 1.00101.13 C
ANISOU 1602 CD1 PHE A 239 14189 12010 12224 3712 -2574 357 C
ATOM 1603 CD2 PHE A 239 73.181 -25.892 41.538 1.00 95.84 C
ANISOU 1603 CD2 PHE A 239 13003 11508 11906 3822 -2883 244 C
ATOM 1604 CE1 PHE A 239 71.444 -27.951 42.116 1.00109.17 C
ANISOU 1604 CE1 PHE A 239 15634 12875 12970 3822 -2774 284 C
ATOM 1605 CE2 PHE A 239 73.114 -26.391 42.819 1.00106.36 C
ANISOU 1605 CE2 PHE A 239 14754 12691 12967 3939 -3109 167 C
ATOM 1606 CZ PHE A 239 72.246 -27.422 43.110 1.00113.23 C
ANISOU 1606 CZ PHE A 239 16110 13392 13521 3940 -3047 190 C
ATOM 1607 N ARG A 240 72.990 -28.817 38.027 1.00 99.26 N
ANISOU 1607 N ARG A 240 13479 11882 12354 3940 -2387 401 N
ATOM 1608 CA ARG A 240 73.167 -30.250 38.264 1.00108.85 C
ANISOU 1608 CA ARG A 240 15075 12956 13326 4148 -2498 356 C
ATOM 1609 C ARG A 240 74.430 -30.822 37.632 1.00113.37 C
ANISOU 1609 C ARG A 240 15437 13562 14077 4393 -2585 311 C
ATOM 1610 O ARG A 240 75.055 -31.723 38.205 1.00125.33 O
ANISOU 1610 O ARG A 240 17183 14984 15453 4649 -2805 227 O
ATOM 1611 CB ARG A 240 71.967 -31.028 37.723 1.00118.01 C
ANISOU 1611 CB ARG A 240 16556 14023 14259 4014 -2275 430 C
ATOM 1612 CG ARG A 240 70.678 -30.890 38.497 1.00125.09 C
ANISOU 1612 CG ARG A 240 17780 14836 14912 3829 -2206 454 C
ATOM 1613 CD ARG A 240 70.295 -32.259 39.034 1.00137.38 C
ANISOU 1613 CD ARG A 240 19898 16190 16110 3935 -2254 417 C
ATOM 1614 NE ARG A 240 68.863 -32.405 39.278 1.00145.94 N
ANISOU 1614 NE ARG A 240 21293 17182 16978 3719 -2073 463 N
ATOM 1615 CZ ARG A 240 68.297 -33.524 39.724 1.00149.50 C
ANISOU 1615 CZ ARG A 240 22263 17433 17107 3745 -2053 437 C
ATOM 1616 NH1 ARG A 240 69.048 -34.592 39.962 1.00152.73 N
ANISOU 1616 NH1 ARG A 240 22961 17714 17356 3993 -2214 366 N
ATOM 1617 NH2 ARG A 240 66.985 -33.578 39.925 1.00146.84 N
ANISOU 1617 NH2 ARG A 240 22162 17016 16614 3526 -1867 477 N
ATOM 1618 N LYS A 241 74.832 -30.315 36.470 1.00109.46 N
ANISOU 1618 N LYS A 241 14517 13184 13888 4332 -2415 358 N
ATOM 1619 CA LYS A 241 76.051 -30.817 35.844 1.00110.47 C
ANISOU 1619 CA LYS A 241 14410 13342 14220 4567 -2469 313 C
ATOM 1620 C LYS A 241 77.312 -30.231 36.479 1.00110.96 C
ANISOU 1620 C LYS A 241 14146 13501 14511 4737 -2711 207 C
ATOM 1621 O LYS A 241 78.345 -30.908 36.519 1.00112.21 O
ANISOU 1621 O LYS A 241 14243 13652 14742 5016 -2878 123 O
ATOM 1622 CB LYS A 241 75.971 -30.637 34.326 1.00111.83 C
ANISOU 1622 CB LYS A 241 14314 13564 14613 4446 -2176 397 C
ATOM 1623 CG LYS A 241 75.050 -31.722 33.702 1.00115.08 C
ANISOU 1623 CG LYS A 241 15109 13857 14758 4401 -2020 458 C
ATOM 1624 CD LYS A 241 75.015 -31.734 32.170 1.00114.63 C
ANISOU 1624 CD LYS A 241 14855 13817 14880 4318 -1760 520 C
ATOM 1625 CE LYS A 241 74.082 -32.837 31.619 1.00103.32 C
ANISOU 1625 CE LYS A 241 13837 12274 13147 4276 -1628 568 C
ATOM 1626 NZ LYS A 241 72.625 -32.554 31.820 1.00 90.78 N
ANISOU 1626 NZ LYS A 241 12481 10672 11338 4011 -1520 625 N
ATOM 1627 N LEU A 242 77.251 -28.990 36.981 1.00110.45 N
ANISOU 1627 N LEU A 242 13875 13531 14561 4583 -2740 198 N
ATOM 1628 CA LEU A 242 78.410 -28.363 37.611 1.00107.63 C
ANISOU 1628 CA LEU A 242 13204 13278 14413 4722 -2977 82 C
ATOM 1629 C LEU A 242 78.544 -28.735 39.081 1.00123.70 C
ANISOU 1629 C LEU A 242 15575 15223 16203 4886 -3328 -28 C
ATOM 1630 O LEU A 242 79.592 -28.467 39.680 1.00139.09 O
ANISOU 1630 O LEU A 242 17318 17238 18293 5060 -3593 -154 O
ATOM 1631 CB LEU A 242 78.354 -26.836 37.497 1.00 92.07 C
ANISOU 1631 CB LEU A 242 10874 11443 12665 4491 -2859 109 C
ATOM 1632 CG LEU A 242 78.550 -26.119 36.163 1.00 92.71 C
ANISOU 1632 CG LEU A 242 10538 11632 13057 4350 -2553 184 C
ATOM 1633 CD1 LEU A 242 78.628 -24.628 36.401 1.00 86.11 C
ANISOU 1633 CD1 LEU A 242 9419 10920 12381 4173 -2521 174 C
ATOM 1634 CD2 LEU A 242 79.824 -26.602 35.479 1.00110.27 C
ANISOU 1634 CD2 LEU A 242 12443 13913 15540 4577 -2559 119 C
ATOM 1635 N TRP A 243 77.521 -29.353 39.667 1.00117.37 N
ANISOU 1635 N TRP A 243 15291 14265 15038 4838 -3335 7 N
ATOM 1636 CA TRP A 243 77.500 -29.710 41.084 1.00107.29 C
ANISOU 1636 CA TRP A 243 14422 12859 13485 4973 -3638 -89 C
ATOM 1637 C TRP A 243 76.970 -31.136 41.223 1.00 97.04 C
ANISOU 1637 C TRP A 243 13675 11365 11832 5093 -3644 -78 C
ATOM 1638 O TRP A 243 76.813 -31.652 42.328 1.00 91.59 O
ANISOU 1638 O TRP A 243 13439 10513 10849 5208 -3857 -149 O
ATOM 1639 CB TRP A 243 76.611 -28.744 41.891 1.00107.18 C
ANISOU 1639 CB TRP A 243 14536 12830 13359 4736 -3610 -60 C
ATOM 1640 CG TRP A 243 77.227 -27.421 42.290 1.00116.94 C
ANISOU 1640 CG TRP A 243 15383 14205 14842 4679 -3730 -118 C
ATOM 1641 CD1 TRP A 243 78.020 -27.190 43.375 1.00123.07 C
ANISOU 1641 CD1 TRP A 243 16173 14970 15618 4844 -4080 -257 C
ATOM 1642 CD2 TRP A 243 77.064 -26.149 41.637 1.00122.51 C
ANISOU 1642 CD2 TRP A 243 15669 15070 15809 4438 -3509 -48 C
ATOM 1643 NE1 TRP A 243 78.375 -25.864 43.434 1.00123.49 N
ANISOU 1643 NE1 TRP A 243 15825 15174 15921 4712 -4087 -280 N
ATOM 1644 CE2 TRP A 243 77.805 -25.202 42.378 1.00118.27 C
ANISOU 1644 CE2 TRP A 243 14902 14617 15418 4466 -3732 -152 C
ATOM 1645 CE3 TRP A 243 76.376 -25.721 40.493 1.00123.12 C
ANISOU 1645 CE3 TRP A 243 15562 15216 16002 4211 -3155 84 C
ATOM 1646 CZ2 TRP A 243 77.881 -23.856 42.012 1.00106.63 C
ANISOU 1646 CZ2 TRP A 243 13032 13292 14190 4270 -3596 -126 C
ATOM 1647 CZ3 TRP A 243 76.451 -24.381 40.133 1.00113.49 C
ANISOU 1647 CZ3 TRP A 243 13963 14134 15025 4030 -3027 113 C
ATOM 1648 CH2 TRP A 243 77.201 -23.466 40.890 1.00103.47 C
ANISOU 1648 CH2 TRP A 243 12481 12947 13886 4059 -3238 10 C
ATOM 1649 N SER A 252 91.554 -33.869 37.958 1.00138.06 N
ANISOU 1649 N SER A 252 14454 17706 20296 8266 -5230 -1444 N
ATOM 1650 CA SER A 252 91.827 -32.954 39.062 1.00139.64 C
ANISOU 1650 CA SER A 252 14523 18008 20526 8199 -5566 -1585 C
ATOM 1651 C SER A 252 92.163 -31.542 38.566 1.00146.79 C
ANISOU 1651 C SER A 252 14798 19152 21822 7895 -5326 -1610 C
ATOM 1652 O SER A 252 91.809 -30.567 39.229 1.00155.82 O
ANISOU 1652 O SER A 252 15958 20340 22908 7650 -5416 -1621 O
ATOM 1653 CB SER A 252 92.943 -33.495 39.973 1.00147.85 C
ANISOU 1653 CB SER A 252 15485 19070 21623 8641 -6101 -1834 C
ATOM 1654 OG SER A 252 94.132 -33.778 39.264 1.00153.34 O
ANISOU 1654 OG SER A 252 15615 19918 22728 8905 -6066 -1964 O
ATOM 1655 N ALA A 253 92.862 -31.412 37.429 1.00139.61 N
ANISOU 1655 N ALA A 253 13352 18392 21301 7913 -5017 -1628 N
ATOM 1656 CA ALA A 253 93.139 -30.067 36.925 1.00138.14 C
ANISOU 1656 CA ALA A 253 12619 18421 21448 7606 -4756 -1655 C
ATOM 1657 C ALA A 253 91.887 -29.372 36.386 1.00154.35 C
ANISOU 1657 C ALA A 253 14904 20409 23333 7177 -4351 -1418 C
ATOM 1658 O ALA A 253 91.885 -28.144 36.249 1.00128.03 O
ANISOU 1658 O ALA A 253 11264 17218 20164 6886 -4198 -1431 O
ATOM 1659 CB ALA A 253 94.213 -30.129 35.838 1.00142.25 C
ANISOU 1659 CB ALA A 253 12530 19110 22410 7739 -4498 -1748 C
ATOM 1660 N GLU A 286 90.830 -30.135 36.091 1.00139.46 N
ANISOU 1660 N GLU A 286 13557 18311 21121 7136 -4188 -1216 N
ATOM 1661 CA GLU A 286 89.529 -29.633 35.632 1.00120.75 C
ANISOU 1661 CA GLU A 286 11471 15854 18555 6760 -3845 -993 C
ATOM 1662 C GLU A 286 88.853 -28.739 36.658 1.00115.06 C
ANISOU 1662 C GLU A 286 10953 15131 17634 6520 -4023 -988 C
ATOM 1663 O GLU A 286 88.131 -27.807 36.285 1.00118.58 O
ANISOU 1663 O GLU A 286 11377 15605 18071 6182 -3747 -868 O
ATOM 1664 CB GLU A 286 88.574 -30.757 35.242 1.00124.19 C
ANISOU 1664 CB GLU A 286 12456 16061 18672 6791 -3705 -821 C
ATOM 1665 CG GLU A 286 88.224 -30.700 33.764 1.00124.49 C
ANISOU 1665 CG GLU A 286 12371 16080 18849 6621 -3198 -662 C
ATOM 1666 CD GLU A 286 87.431 -31.897 33.284 1.00129.94 C
ANISOU 1666 CD GLU A 286 13553 16549 19269 6676 -3073 -527 C
ATOM 1667 OE1 GLU A 286 88.054 -32.932 32.955 1.00141.54 O
ANISOU 1667 OE1 GLU A 286 15020 17960 20798 6981 -3111 -580 O
ATOM 1668 OE2 GLU A 286 86.183 -31.793 33.226 1.00119.78 O
ANISOU 1668 OE2 GLU A 286 12648 15150 17712 6411 -2937 -380 O
ATOM 1669 N VAL A 287 89.223 -28.911 37.923 1.00118.82 N
ANISOU 1669 N VAL A 287 11562 15589 17994 6706 -4485 -1140 N
ATOM 1670 CA VAL A 287 88.705 -28.151 39.057 1.00127.79 C
ANISOU 1670 CA VAL A 287 12915 16702 18937 6535 -4710 -1164 C
ATOM 1671 C VAL A 287 89.085 -26.686 38.965 1.00133.11 C
ANISOU 1671 C VAL A 287 13092 17578 19904 6286 -4618 -1232 C
ATOM 1672 O VAL A 287 88.301 -25.822 39.384 1.00125.46 O
ANISOU 1672 O VAL A 287 12285 16588 18795 6009 -4572 -1160 O
ATOM 1673 CB VAL A 287 89.169 -28.778 40.382 1.00129.36 C
ANISOU 1673 CB VAL A 287 13374 16818 18960 6847 -5242 -1332 C
ATOM 1674 CG1 VAL A 287 89.130 -27.744 41.494 1.00126.03 C
ANISOU 1674 CG1 VAL A 287 12945 16438 18500 6704 -5501 -1426 C
ATOM 1675 CG2 VAL A 287 88.284 -29.969 40.732 1.00120.65 C
ANISOU 1675 CG2 VAL A 287 12970 15462 17409 6964 -5303 -1225 C
ATOM 1676 N LYS A 288 90.254 -26.355 38.423 1.00138.99 N
ANISOU 1676 N LYS A 288 13238 18520 21052 6366 -4576 -1376 N
ATOM 1677 CA LYS A 288 90.517 -24.931 38.284 1.00139.71 C
ANISOU 1677 CA LYS A 288 12900 18792 21390 6085 -4448 -1439 C
ATOM 1678 C LYS A 288 89.419 -24.311 37.421 1.00139.25 C
ANISOU 1678 C LYS A 288 12981 18692 21235 5736 -3981 -1212 C
ATOM 1679 O LYS A 288 88.783 -23.332 37.836 1.00138.53 O
ANISOU 1679 O LYS A 288 12991 18603 21042 5470 -3959 -1166 O
ATOM 1680 CB LYS A 288 91.873 -24.695 37.627 1.00143.32 C
ANISOU 1680 CB LYS A 288 12684 19471 22302 6187 -4378 -1625 C
ATOM 1681 CG LYS A 288 93.104 -24.968 38.465 1.00150.76 C
ANISOU 1681 CG LYS A 288 13331 20515 23434 6490 -4848 -1899 C
ATOM 1682 CD LYS A 288 94.002 -23.742 38.457 1.00151.03 C
ANISOU 1682 CD LYS A 288 12745 20793 23848 6318 -4854 -2104 C
ATOM 1683 CE LYS A 288 95.214 -23.916 39.347 1.00147.89 C
ANISOU 1683 CE LYS A 288 12024 20510 23658 6599 -5353 -2397 C
ATOM 1684 NZ LYS A 288 96.349 -24.519 38.583 1.00150.10 N
ANISOU 1684 NZ LYS A 288 11808 20929 24294 6858 -5276 -2545 N
ATOM 1685 N GLN A 289 89.073 -24.943 36.290 1.00135.99 N
ANISOU 1685 N GLN A 289 12648 18212 20808 5750 -3629 -1058 N
ATOM 1686 CA GLN A 289 87.980 -24.393 35.487 1.00121.38 C
ANISOU 1686 CA GLN A 289 10965 16307 18846 5438 -3216 -845 C
ATOM 1687 C GLN A 289 86.684 -24.392 36.278 1.00112.14 C
ANISOU 1687 C GLN A 289 10343 14972 17293 5296 -3321 -716 C
ATOM 1688 O GLN A 289 85.988 -23.365 36.363 1.00108.44 O
ANISOU 1688 O GLN A 289 9922 14521 16760 5014 -3196 -645 O
ATOM 1689 CB GLN A 289 87.746 -25.239 34.240 1.00122.25 C
ANISOU 1689 CB GLN A 289 11156 16329 18963 5505 -2869 -699 C
ATOM 1690 CG GLN A 289 86.646 -24.679 33.349 1.00119.89 C
ANISOU 1690 CG GLN A 289 11021 15971 18561 5201 -2456 -490 C
ATOM 1691 CD GLN A 289 86.263 -25.628 32.227 1.00121.53 C
ANISOU 1691 CD GLN A 289 11405 16041 18728 5266 -2156 -341 C
ATOM 1692 OE1 GLN A 289 85.096 -25.683 31.818 1.00116.88 O
ANISOU 1692 OE1 GLN A 289 11155 15315 17939 5083 -1958 -164 O
ATOM 1693 NE2 GLN A 289 87.229 -26.397 31.742 1.00122.46 N
ANISOU 1693 NE2 GLN A 289 11297 16188 19045 5530 -2132 -421 N
ATOM 1694 N MET A 290 86.496 -25.443 37.068 1.00113.05 N
ANISOU 1694 N MET A 290 10848 14944 17161 5509 -3613 -732 N
ATOM 1695 CA MET A 290 85.295 -25.576 37.867 1.00111.84 C
ANISOU 1695 CA MET A 290 11241 14628 16626 5396 -3709 -632 C
ATOM 1696 C MET A 290 85.205 -24.488 38.912 1.00125.96 C
ANISOU 1696 C MET A 290 13008 16469 18381 5249 -3915 -710 C
ATOM 1697 O MET A 290 84.100 -24.044 39.243 1.00123.63 O
ANISOU 1697 O MET A 290 13022 16091 17860 5029 -3829 -597 O
ATOM 1698 CB MET A 290 85.261 -26.949 38.541 1.00110.09 C
ANISOU 1698 CB MET A 290 11449 14244 16138 5682 -3994 -669 C
ATOM 1699 CG MET A 290 85.092 -28.140 37.595 1.00121.69 C
ANISOU 1699 CG MET A 290 13075 15611 17552 5811 -3794 -572 C
ATOM 1700 SD MET A 290 83.444 -28.881 37.652 1.00120.96 S
ANISOU 1700 SD MET A 290 13672 15291 16998 5661 -3653 -389 S
ATOM 1701 CE MET A 290 83.779 -30.497 36.946 1.00121.95 C
ANISOU 1701 CE MET A 290 13969 15300 17066 5959 -3621 -379 C
ATOM 1702 N ARG A 291 86.330 -24.035 39.456 1.00141.62 N
ANISOU 1702 N ARG A 291 14631 18587 20590 5363 -4188 -908 N
ATOM 1703 CA ARG A 291 86.179 -22.983 40.442 1.00147.16 C
ANISOU 1703 CA ARG A 291 15346 19321 21248 5206 -4376 -976 C
ATOM 1704 C ARG A 291 85.682 -21.691 39.799 1.00144.94 C
ANISOU 1704 C ARG A 291 14860 19132 21079 4859 -4030 -881 C
ATOM 1705 O ARG A 291 84.775 -21.041 40.332 1.00139.49 O
ANISOU 1705 O ARG A 291 14427 18376 20196 4659 -4012 -804 O
ATOM 1706 CB ARG A 291 87.520 -22.743 41.155 1.00157.33 C
ANISOU 1706 CB ARG A 291 16269 20739 22772 5391 -4763 -1228 C
ATOM 1707 CG ARG A 291 87.907 -23.791 42.207 1.00161.60 C
ANISOU 1707 CG ARG A 291 17108 21161 23130 5732 -5218 -1347 C
ATOM 1708 CD ARG A 291 89.395 -23.746 42.569 1.00167.97 C
ANISOU 1708 CD ARG A 291 17452 22122 24245 5969 -5566 -1606 C
ATOM 1709 NE ARG A 291 90.103 -24.941 42.102 1.00177.22 N
ANISOU 1709 NE ARG A 291 18535 23292 25509 6302 -5628 -1664 N
ATOM 1710 CZ ARG A 291 91.355 -25.259 42.428 1.00189.63 C
ANISOU 1710 CZ ARG A 291 19777 24966 27308 6597 -5966 -1891 C
ATOM 1711 NH1 ARG A 291 92.064 -24.469 43.223 1.00195.56 N
ANISOU 1711 NH1 ARG A 291 20244 25834 28225 6589 -6283 -2090 N
ATOM 1712 NH2 ARG A 291 91.906 -26.371 41.950 1.00193.25 N
ANISOU 1712 NH2 ARG A 291 20182 25409 27834 6906 -5991 -1926 N
ATOM 1713 N ALA A 292 86.263 -21.282 38.661 1.00152.10 N
ANISOU 1713 N ALA A 292 15318 20185 22290 4790 -3747 -892 N
ATOM 1714 CA ALA A 292 85.746 -20.074 38.014 1.00147.42 C
ANISOU 1714 CA ALA A 292 14588 19659 21765 4472 -3411 -802 C
ATOM 1715 C ALA A 292 84.314 -20.175 37.474 1.00137.02 C
ANISOU 1715 C ALA A 292 13666 18203 20191 4303 -3104 -561 C
ATOM 1716 O ALA A 292 83.454 -19.362 37.851 1.00136.05 O
ANISOU 1716 O ALA A 292 13724 18044 19924 4091 -3057 -489 O
ATOM 1717 CB ALA A 292 86.693 -19.663 36.888 1.00152.15 C
ANISOU 1717 CB ALA A 292 14658 20432 22720 4443 -3157 -880 C
ATOM 1718 N ARG A 293 83.977 -21.281 36.793 1.00119.72 N
ANISOU 1718 N ARG A 293 11672 15910 17908 4416 -2956 -445 N
ATOM 1719 CA ARG A 293 82.626 -21.407 36.236 1.00109.31 C
ANISOU 1719 CA ARG A 293 10700 14462 16369 4247 -2675 -234 C
ATOM 1720 C ARG A 293 81.521 -21.517 37.267 1.00102.04 C
ANISOU 1720 C ARG A 293 10246 13403 15119 4172 -2832 -174 C
ATOM 1721 O ARG A 293 80.407 -21.048 37.012 1.00100.90 O
ANISOU 1721 O ARG A 293 10289 13206 14844 3957 -2620 -39 O
ATOM 1722 CB ARG A 293 82.529 -22.527 35.194 1.00103.98 C
ANISOU 1722 CB ARG A 293 10111 13704 15692 4360 -2467 -134 C
ATOM 1723 CG ARG A 293 83.108 -22.069 33.850 1.00103.86 C
ANISOU 1723 CG ARG A 293 9704 13803 15955 4314 -2126 -116 C
ATOM 1724 CD ARG A 293 83.197 -23.125 32.746 1.00105.23 C
ANISOU 1724 CD ARG A 293 9909 13895 16178 4445 -1905 -33 C
ATOM 1725 NE ARG A 293 83.460 -22.440 31.474 1.00105.11 N
ANISOU 1725 NE ARG A 293 9604 13976 16357 4342 -1521 11 N
ATOM 1726 CZ ARG A 293 83.607 -23.031 30.293 1.00101.22 C
ANISOU 1726 CZ ARG A 293 9072 13435 15953 4419 -1237 84 C
ATOM 1727 NH1 ARG A 293 83.523 -24.350 30.190 1.00 80.77 N
ANISOU 1727 NH1 ARG A 293 6692 10688 13307 4590 -1300 119 N
ATOM 1728 NH2 ARG A 293 83.821 -22.290 29.209 1.00 79.26 N
ANISOU 1728 NH2 ARG A 293 6071 10761 13284 4328 -886 110 N
ATOM 1729 N ARG A 294 81.776 -22.115 38.417 1.00 96.11 N
ANISOU 1729 N ARG A 294 9702 12589 14225 4350 -3190 -278 N
ATOM 1730 CA ARG A 294 80.713 -22.149 39.409 1.00 99.13 C
ANISOU 1730 CA ARG A 294 10541 12839 14286 4268 -3305 -228 C
ATOM 1731 C ARG A 294 80.395 -20.744 39.918 1.00107.27 C
ANISOU 1731 C ARG A 294 11484 13932 15341 4050 -3300 -238 C
ATOM 1732 O ARG A 294 79.222 -20.339 39.922 1.00109.61 O
ANISOU 1732 O ARG A 294 12011 14164 15473 3853 -3126 -116 O
ATOM 1733 CB ARG A 294 81.095 -23.082 40.565 1.00114.73 C
ANISOU 1733 CB ARG A 294 12800 14714 16077 4524 -3694 -346 C
ATOM 1734 CG ARG A 294 80.909 -24.576 40.251 1.00118.78 C
ANISOU 1734 CG ARG A 294 13615 15099 16419 4708 -3684 -302 C
ATOM 1735 CD ARG A 294 81.692 -25.487 41.212 1.00113.41 C
ANISOU 1735 CD ARG A 294 13113 14345 15631 5030 -4089 -455 C
ATOM 1736 NE ARG A 294 81.576 -26.902 40.860 1.00105.86 N
ANISOU 1736 NE ARG A 294 12445 13265 14510 5219 -4072 -420 N
ATOM 1737 CZ ARG A 294 81.943 -27.905 41.652 1.00112.09 C
ANISOU 1737 CZ ARG A 294 13551 13934 15103 5498 -4386 -520 C
ATOM 1738 NH1 ARG A 294 82.449 -27.659 42.852 1.00119.70 N
ANISOU 1738 NH1 ARG A 294 14586 14879 16016 5627 -4754 -663 N
ATOM 1739 NH2 ARG A 294 81.806 -29.158 41.242 1.00112.01 N
ANISOU 1739 NH2 ARG A 294 13810 13810 14937 5657 -4340 -483 N
ATOM 1740 N LYS A 295 81.422 -19.911 40.129 1.00109.93 N
ANISOU 1740 N LYS A 295 11433 14412 15924 4060 -3436 -378 N
ATOM 1741 CA LYS A 295 81.151 -18.570 40.646 1.00 99.06 C
ANISOU 1741 CA LYS A 295 9988 13086 14563 3856 -3448 -398 C
ATOM 1742 C LYS A 295 80.321 -17.751 39.669 1.00 91.46 C
ANISOU 1742 C LYS A 295 8965 12153 13631 3606 -3053 -249 C
ATOM 1743 O LYS A 295 79.258 -17.228 40.032 1.00 84.45 O
ANISOU 1743 O LYS A 295 8328 11196 12564 3448 -2979 -158 O
ATOM 1744 CB LYS A 295 82.480 -17.870 40.946 1.00102.35 C
ANISOU 1744 CB LYS A 295 9964 13662 15263 3901 -3659 -595 C
ATOM 1745 CG LYS A 295 83.047 -18.168 42.331 1.00105.41 C
ANISOU 1745 CG LYS A 295 10475 14006 15569 4083 -4121 -754 C
ATOM 1746 CD LYS A 295 84.584 -18.192 42.309 1.00106.63 C
ANISOU 1746 CD LYS A 295 10162 14315 16040 4248 -4342 -964 C
ATOM 1747 CE LYS A 295 85.182 -18.234 43.714 1.00105.05 C
ANISOU 1747 CE LYS A 295 10046 14084 15782 4407 -4829 -1142 C
ATOM 1748 NZ LYS A 295 86.655 -17.986 43.735 1.00104.95 N
ANISOU 1748 NZ LYS A 295 9511 14244 16121 4529 -5066 -1391 N
ATOM 1749 N THR A 296 80.704 -17.756 38.394 1.00 94.90 N
ANISOU 1749 N THR A 296 9121 12672 14265 3590 -2787 -212 N
ATOM 1750 CA THR A 296 79.950 -16.986 37.415 1.00 80.08 C
ANISOU 1750 CA THR A 296 7212 10813 12401 3378 -2422 -78 C
ATOM 1751 C THR A 296 78.534 -17.529 37.287 1.00 79.39 C
ANISOU 1751 C THR A 296 7542 10573 12051 3310 -2279 98 C
ATOM 1752 O THR A 296 77.568 -16.757 37.213 1.00 84.35 O
ANISOU 1752 O THR A 296 8289 11176 12584 3128 -2123 190 O
ATOM 1753 CB THR A 296 80.670 -17.005 36.071 1.00 70.55 C
ANISOU 1753 CB THR A 296 5669 9707 11428 3402 -2166 -81 C
ATOM 1754 OG1 THR A 296 80.899 -18.364 35.673 1.00 76.81 O
ANISOU 1754 OG1 THR A 296 6542 10435 12209 3595 -2170 -48 O
ATOM 1755 CG2 THR A 296 82.005 -16.283 36.177 1.00 73.73 C
ANISOU 1755 CG2 THR A 296 5617 10280 12116 3413 -2272 -279 C
ATOM 1756 N ALA A 297 78.374 -18.850 37.380 1.00 79.32 N
ANISOU 1756 N ALA A 297 7771 10457 11910 3455 -2361 126 N
ATOM 1757 CA ALA A 297 77.030 -19.390 37.234 1.00 72.38 C
ANISOU 1757 CA ALA A 297 7265 9440 10795 3365 -2225 265 C
ATOM 1758 C ALA A 297 76.180 -18.952 38.411 1.00 79.80 C
ANISOU 1758 C ALA A 297 8485 10318 11518 3272 -2357 263 C
ATOM 1759 O ALA A 297 75.049 -18.474 38.232 1.00 80.25 O
ANISOU 1759 O ALA A 297 8681 10334 11475 3094 -2174 366 O
ATOM 1760 CB ALA A 297 77.073 -20.911 37.130 1.00 64.42 C
ANISOU 1760 CB ALA A 297 6472 8331 9675 3539 -2296 270 C
ATOM 1761 N LYS A 298 76.785 -18.944 39.599 1.00 87.02 N
ANISOU 1761 N LYS A 298 9441 11234 12389 3387 -2673 135 N
ATOM 1762 CA LYS A 298 76.088 -18.451 40.773 1.00 85.25 C
ANISOU 1762 CA LYS A 298 9479 10943 11968 3309 -2804 123 C
ATOM 1763 C LYS A 298 75.657 -17.014 40.521 1.00 79.82 C
ANISOU 1763 C LYS A 298 8622 10330 11377 3098 -2626 171 C
ATOM 1764 O LYS A 298 74.509 -16.635 40.785 1.00 68.21 O
ANISOU 1764 O LYS A 298 7373 8795 9748 2962 -2517 253 O
ATOM 1765 CB LYS A 298 77.032 -18.602 41.974 1.00 90.46 C
ANISOU 1765 CB LYS A 298 10164 11596 12610 3484 -3191 -39 C
ATOM 1766 CG LYS A 298 76.680 -18.003 43.328 1.00 97.74 C
ANISOU 1766 CG LYS A 298 11319 12453 13365 3441 -3399 -91 C
ATOM 1767 CD LYS A 298 77.996 -17.885 44.127 1.00110.12 C
ANISOU 1767 CD LYS A 298 12721 14071 15048 3605 -3771 -273 C
ATOM 1768 CE LYS A 298 77.799 -17.918 45.644 1.00110.20 C
ANISOU 1768 CE LYS A 298 13113 13946 14812 3674 -4084 -353 C
ATOM 1769 NZ LYS A 298 79.007 -17.440 46.393 1.00106.52 N
ANISOU 1769 NZ LYS A 298 12446 13533 14493 3800 -4470 -565 N
ATOM 1770 N MET A 299 76.567 -16.199 39.989 1.00 86.11 N
ANISOU 1770 N MET A 299 9024 11264 12430 3073 -2585 112 N
ATOM 1771 CA MET A 299 76.217 -14.816 39.700 1.00 87.08 C
ANISOU 1771 CA MET A 299 9001 11454 12633 2885 -2413 145 C
ATOM 1772 C MET A 299 75.093 -14.714 38.677 1.00 85.97 C
ANISOU 1772 C MET A 299 8958 11274 12434 2755 -2071 310 C
ATOM 1773 O MET A 299 74.092 -14.019 38.906 1.00 89.88 O
ANISOU 1773 O MET A 299 9602 11730 12820 2624 -1977 378 O
ATOM 1774 CB MET A 299 77.433 -14.072 39.156 1.00 88.95 C
ANISOU 1774 CB MET A 299 8795 11846 13154 2877 -2395 37 C
ATOM 1775 CG MET A 299 77.195 -12.594 38.922 1.00 93.39 C
ANISOU 1775 CG MET A 299 9213 12462 13807 2703 -2273 2 C
ATOM 1776 SD MET A 299 78.613 -11.829 38.120 1.00111.46 S
ANISOU 1776 SD MET A 299 10974 14912 16464 2675 -2231 -190 S
ATOM 1777 CE MET A 299 78.485 -12.533 36.484 1.00106.71 C
ANISOU 1777 CE MET A 299 10337 14342 15868 2703 -1839 -18 C
ATOM 1778 N LEU A 300 75.167 -15.522 37.612 1.00 84.86 N
ANISOU 1778 N LEU A 300 8774 11124 12346 2804 -1906 377 N
ATOM 1779 CA LEU A 300 74.160 -15.409 36.562 1.00 76.65 C
ANISOU 1779 CA LEU A 300 7809 10041 11272 2680 -1601 524 C
ATOM 1780 C LEU A 300 72.780 -15.818 37.040 1.00 76.61 C
ANISOU 1780 C LEU A 300 8155 9907 11046 2601 -1596 601 C
ATOM 1781 O LEU A 300 71.791 -15.127 36.755 1.00 77.38 O
ANISOU 1781 O LEU A 300 8313 9979 11107 2457 -1430 681 O
ATOM 1782 CB LEU A 300 74.577 -16.246 35.351 1.00 62.98 C
ANISOU 1782 CB LEU A 300 5974 8307 9650 2754 -1447 570 C
ATOM 1783 CG LEU A 300 75.843 -15.768 34.632 1.00 53.19 C
ANISOU 1783 CG LEU A 300 4365 7213 8632 2819 -1367 497 C
ATOM 1784 CD1 LEU A 300 76.250 -16.698 33.511 1.00 53.99 C
ANISOU 1784 CD1 LEU A 300 4392 7295 8827 2918 -1213 544 C
ATOM 1785 CD2 LEU A 300 75.647 -14.363 34.101 1.00 51.49 C
ANISOU 1785 CD2 LEU A 300 4022 7094 8448 2687 -1168 505 C
ATOM 1786 N MET A 301 72.699 -16.858 37.860 1.00 69.66 N
ANISOU 1786 N MET A 301 7513 8949 10005 2701 -1788 559 N
ATOM 1787 CA MET A 301 71.389 -17.244 38.351 1.00 58.34 C
ANISOU 1787 CA MET A 301 6415 7410 8343 2625 -1766 609 C
ATOM 1788 C MET A 301 70.789 -16.127 39.190 1.00 62.25 C
ANISOU 1788 C MET A 301 6971 7910 8771 2521 -1789 606 C
ATOM 1789 O MET A 301 69.612 -15.780 39.017 1.00 80.53 O
ANISOU 1789 O MET A 301 9394 10185 11018 2389 -1632 679 O
ATOM 1790 CB MET A 301 71.503 -18.550 39.133 1.00 68.25 C
ANISOU 1790 CB MET A 301 7949 8580 9403 2772 -1964 553 C
ATOM 1791 CG MET A 301 71.887 -19.718 38.229 1.00 83.24 C
ANISOU 1791 CG MET A 301 9832 10456 11340 2872 -1913 568 C
ATOM 1792 SD MET A 301 72.392 -21.222 39.084 1.00 99.90 S
ANISOU 1792 SD MET A 301 12237 12472 13247 3105 -2175 481 S
ATOM 1793 CE MET A 301 73.069 -22.195 37.734 1.00 98.44 C
ANISOU 1793 CE MET A 301 11897 12299 13208 3216 -2070 502 C
ATOM 1794 N VAL A 302 71.628 -15.422 39.956 1.00 59.38 N
ANISOU 1794 N VAL A 302 6491 7604 8467 2572 -1971 516 N
ATOM 1795 CA VAL A 302 71.101 -14.313 40.740 1.00 69.52 C
ANISOU 1795 CA VAL A 302 7837 8884 9693 2477 -1995 509 C
ATOM 1796 C VAL A 302 70.603 -13.204 39.826 1.00 68.21 C
ANISOU 1796 C VAL A 302 7496 8773 9649 2338 -1740 588 C
ATOM 1797 O VAL A 302 69.490 -12.688 40.008 1.00 41.81 O
ANISOU 1797 O VAL A 302 4289 5380 6218 2237 -1632 648 O
ATOM 1798 CB VAL A 302 72.176 -13.796 41.711 1.00 73.64 C
ANISOU 1798 CB VAL A 302 8262 9452 10267 2554 -2273 377 C
ATOM 1799 CG1 VAL A 302 71.753 -12.450 42.293 1.00 81.11 C
ANISOU 1799 CG1 VAL A 302 9232 10385 11199 2474 -2322 318 C
ATOM 1800 CG2 VAL A 302 72.438 -14.816 42.800 1.00 52.21 C
ANISOU 1800 CG2 VAL A 302 5818 6644 7376 2700 -2549 299 C
ATOM 1801 N VAL A 303 71.329 -12.944 38.737 1.00 68.30 N
ANISOU 1801 N VAL A 303 7232 8872 9849 2343 -1616 595 N
ATOM 1802 CA VAL A 303 70.874 -11.918 37.808 1.00 60.39 C
ANISOU 1802 CA VAL A 303 6110 7912 8924 2236 -1366 667 C
ATOM 1803 C VAL A 303 69.515 -12.305 37.255 1.00 64.64 C
ANISOU 1803 C VAL A 303 6828 8344 9388 2142 -1190 785 C
ATOM 1804 O VAL A 303 68.627 -11.458 37.101 1.00 74.00 O
ANISOU 1804 O VAL A 303 8067 9499 10550 2028 -1060 820 O
ATOM 1805 CB VAL A 303 71.910 -11.691 36.692 1.00 62.31 C
ANISOU 1805 CB VAL A 303 6067 8270 9336 2279 -1248 640 C
ATOM 1806 CG1 VAL A 303 71.328 -10.805 35.606 1.00 41.13 C
ANISOU 1806 CG1 VAL A 303 3378 5620 6630 2185 -969 687 C
ATOM 1807 CG2 VAL A 303 73.172 -11.071 37.268 1.00 74.16 C
ANISOU 1807 CG2 VAL A 303 7336 9871 10970 2319 -1439 481 C
ATOM 1808 N VAL A 304 69.329 -13.585 36.937 1.00 64.43 N
ANISOU 1808 N VAL A 304 6909 8246 9326 2168 -1202 805 N
ATOM 1809 CA VAL A 304 68.053 -13.982 36.359 1.00 52.11 C
ANISOU 1809 CA VAL A 304 5501 6574 7723 2050 -1087 852 C
ATOM 1810 C VAL A 304 66.959 -13.876 37.409 1.00 48.21 C
ANISOU 1810 C VAL A 304 5237 6036 7047 2006 -1144 845 C
ATOM 1811 O VAL A 304 65.892 -13.294 37.165 1.00 53.27 O
ANISOU 1811 O VAL A 304 5921 6628 7693 1892 -1049 857 O
ATOM 1812 CB VAL A 304 68.124 -15.408 35.783 1.00 47.43 C
ANISOU 1812 CB VAL A 304 4991 5929 7100 2103 -1102 845 C
ATOM 1813 CG1 VAL A 304 66.729 -15.876 35.393 1.00 35.26 C
ANISOU 1813 CG1 VAL A 304 3653 4306 5436 1999 -1036 839 C
ATOM 1814 CG2 VAL A 304 69.064 -15.463 34.599 1.00 51.49 C
ANISOU 1814 CG2 VAL A 304 5298 6462 7803 2118 -1007 835 C
ATOM 1815 N LEU A 305 67.274 -14.283 38.641 1.00 50.64 N
ANISOU 1815 N LEU A 305 5691 6349 7201 2102 -1318 798 N
ATOM 1816 CA LEU A 305 66.270 -14.254 39.695 1.00 47.48 C
ANISOU 1816 CA LEU A 305 5541 5891 6609 2071 -1358 793 C
ATOM 1817 C LEU A 305 65.789 -12.843 39.995 1.00 49.05 C
ANISOU 1817 C LEU A 305 5678 6101 6856 1991 -1299 807 C
ATOM 1818 O LEU A 305 64.579 -12.576 39.975 1.00 54.75 O
ANISOU 1818 O LEU A 305 6495 6777 7530 1905 -1192 834 O
ATOM 1819 CB LEU A 305 66.852 -14.896 40.950 1.00 39.36 C
ANISOU 1819 CB LEU A 305 4709 4831 5417 2197 -1585 725 C
ATOM 1820 CG LEU A 305 65.975 -14.819 42.190 1.00 63.21 C
ANISOU 1820 CG LEU A 305 8028 7771 8219 2183 -1641 714 C
ATOM 1821 CD1 LEU A 305 64.771 -15.713 42.017 1.00 61.06 C
ANISOU 1821 CD1 LEU A 305 7970 7434 7796 2133 -1510 762 C
ATOM 1822 CD2 LEU A 305 66.787 -15.229 43.391 1.00 68.46 C
ANISOU 1822 CD2 LEU A 305 8900 8378 8735 2333 -1923 607 C
ATOM 1823 N VAL A 306 66.711 -11.900 40.176 1.00 46.48 N
ANISOU 1823 N VAL A 306 5182 5842 6638 2022 -1360 779 N
ATOM 1824 CA VAL A 306 66.237 -10.557 40.473 1.00 41.24 C
ANISOU 1824 CA VAL A 306 4503 5175 5991 1980 -1320 767 C
ATOM 1825 C VAL A 306 65.435 -10.034 39.304 1.00 50.51 C
ANISOU 1825 C VAL A 306 5561 6327 7305 1854 -1081 855 C
ATOM 1826 O VAL A 306 64.346 -9.477 39.499 1.00 65.57 O
ANISOU 1826 O VAL A 306 7566 8169 9178 1799 -1025 851 O
ATOM 1827 CB VAL A 306 67.407 -9.612 40.822 1.00 41.42 C
ANISOU 1827 CB VAL A 306 4376 5265 6099 2054 -1479 654 C
ATOM 1828 CG1 VAL A 306 68.175 -10.148 42.025 1.00 43.40 C
ANISOU 1828 CG1 VAL A 306 4755 5488 6248 2163 -1792 531 C
ATOM 1829 CG2 VAL A 306 68.330 -9.419 39.620 1.00 51.06 C
ANISOU 1829 CG2 VAL A 306 5304 6590 7507 2050 -1360 675 C
ATOM 1830 N PHE A 307 65.809 -10.428 38.086 1.00 54.56 N
ANISOU 1830 N PHE A 307 5954 6851 7925 1818 -987 854 N
ATOM 1831 CA PHE A 307 65.019 -10.008 36.938 1.00 50.10 C
ANISOU 1831 CA PHE A 307 5377 6194 7466 1673 -862 806 C
ATOM 1832 C PHE A 307 63.621 -10.592 36.998 1.00 51.16 C
ANISOU 1832 C PHE A 307 5703 6267 7469 1651 -877 764 C
ATOM 1833 O PHE A 307 62.628 -9.847 36.962 1.00 65.15 O
ANISOU 1833 O PHE A 307 7535 8012 9209 1615 -833 712 O
ATOM 1834 CB PHE A 307 65.744 -10.434 35.661 1.00 49.51 C
ANISOU 1834 CB PHE A 307 5186 6098 7528 1649 -826 758 C
ATOM 1835 CG PHE A 307 65.051 -10.042 34.388 1.00 54.40 C
ANISOU 1835 CG PHE A 307 5893 6648 8127 1620 -838 520 C
ATOM 1836 CD1 PHE A 307 64.029 -10.828 33.873 1.00 64.41 C
ANISOU 1836 CD1 PHE A 307 7294 7948 9231 1645 -776 552 C
ATOM 1837 CD2 PHE A 307 65.441 -8.918 33.683 1.00 64.36 C
ANISOU 1837 CD2 PHE A 307 7123 7959 9370 1673 -823 335 C
ATOM 1838 CE1 PHE A 307 63.401 -10.490 32.689 1.00 72.07 C
ANISOU 1838 CE1 PHE A 307 8297 8963 10124 1660 -660 531 C
ATOM 1839 CE2 PHE A 307 64.811 -8.574 32.502 1.00 72.48 C
ANISOU 1839 CE2 PHE A 307 8195 9044 10299 1701 -669 364 C
ATOM 1840 CZ PHE A 307 63.791 -9.361 32.004 1.00 74.11 C
ANISOU 1840 CZ PHE A 307 8490 9243 10425 1678 -599 470 C
ATOM 1841 N ALA A 308 63.515 -11.888 37.282 1.00 49.08 N
ANISOU 1841 N ALA A 308 5544 6012 7091 1712 -924 810 N
ATOM 1842 CA ALA A 308 62.180 -12.457 37.320 1.00 43.15 C
ANISOU 1842 CA ALA A 308 4973 5250 6170 1687 -869 793 C
ATOM 1843 C ALA A 308 61.376 -11.799 38.425 1.00 51.29 C
ANISOU 1843 C ALA A 308 6107 6266 7113 1681 -862 803 C
ATOM 1844 O ALA A 308 60.176 -11.547 38.263 1.00 65.59 O
ANISOU 1844 O ALA A 308 7976 8082 8864 1648 -769 776 O
ATOM 1845 CB ALA A 308 62.242 -13.968 37.516 1.00 36.28 C
ANISOU 1845 CB ALA A 308 4245 4384 5156 1739 -901 826 C
ATOM 1846 N LEU A 309 62.023 -11.508 39.561 1.00 45.62 N
ANISOU 1846 N LEU A 309 5421 5546 6365 1733 -957 836 N
ATOM 1847 CA LEU A 309 61.297 -10.845 40.635 1.00 40.97 C
ANISOU 1847 CA LEU A 309 5002 4943 5622 1800 -963 810 C
ATOM 1848 C LEU A 309 60.973 -9.396 40.302 1.00 37.02 C
ANISOU 1848 C LEU A 309 4375 4438 5253 1765 -887 786 C
ATOM 1849 O LEU A 309 59.802 -8.994 40.344 1.00 41.56 O
ANISOU 1849 O LEU A 309 5024 5008 5757 1774 -783 760 O
ATOM 1850 CB LEU A 309 62.112 -10.899 41.922 1.00 46.36 C
ANISOU 1850 CB LEU A 309 5847 5611 6157 1922 -1146 776 C
ATOM 1851 CG LEU A 309 62.378 -12.297 42.472 1.00 63.59 C
ANISOU 1851 CG LEU A 309 8247 7758 8158 1986 -1255 765 C
ATOM 1852 CD1 LEU A 309 63.302 -12.229 43.686 1.00 69.85 C
ANISOU 1852 CD1 LEU A 309 9209 8504 8825 2099 -1502 684 C
ATOM 1853 CD2 LEU A 309 61.075 -12.972 42.834 1.00 71.90 C
ANISOU 1853 CD2 LEU A 309 9581 8749 8988 2000 -1161 777 C
ATOM 1854 N CYS A 310 61.937 -8.673 39.731 1.00 40.40 N
ANISOU 1854 N CYS A 310 4596 4872 5881 1729 -902 795 N
ATOM 1855 CA CYS A 310 61.695 -7.254 39.502 1.00 52.10 C
ANISOU 1855 CA CYS A 310 6005 6327 7462 1720 -844 760 C
ATOM 1856 C CYS A 310 60.611 -7.028 38.475 1.00 60.97 C
ANISOU 1856 C CYS A 310 7129 7422 8616 1644 -743 680 C
ATOM 1857 O CYS A 310 59.797 -6.102 38.614 1.00 77.66 O
ANISOU 1857 O CYS A 310 9291 9537 10680 1680 -663 650 O
ATOM 1858 CB CYS A 310 62.984 -6.562 39.054 1.00 68.26 C
ANISOU 1858 CB CYS A 310 7869 8413 9655 1712 -842 772 C
ATOM 1859 SG CYS A 310 64.222 -6.306 40.347 1.00 82.93 S
ANISOU 1859 SG CYS A 310 9748 10359 11404 1894 -1045 741 S
ATOM 1860 N TYR A 311 60.563 -7.875 37.462 1.00 42.15 N
ANISOU 1860 N TYR A 311 4727 5066 6220 1608 -721 649 N
ATOM 1861 CA TYR A 311 59.583 -7.701 36.415 1.00 33.30 C
ANISOU 1861 CA TYR A 311 3627 4006 5019 1600 -592 609 C
ATOM 1862 C TYR A 311 58.263 -8.392 36.720 1.00 44.91 C
ANISOU 1862 C TYR A 311 5189 5523 6350 1602 -510 640 C
ATOM 1863 O TYR A 311 57.258 -8.082 36.070 1.00 53.61 O
ANISOU 1863 O TYR A 311 6278 6678 7412 1599 -400 632 O
ATOM 1864 CB TYR A 311 60.153 -8.240 35.107 1.00 29.22 C
ANISOU 1864 CB TYR A 311 3061 3526 4517 1591 -570 594 C
ATOM 1865 CG TYR A 311 61.128 -7.286 34.451 1.00 35.98 C
ANISOU 1865 CG TYR A 311 3827 4359 5486 1608 -588 532 C
ATOM 1866 CD1 TYR A 311 62.435 -7.205 34.913 1.00 62.20 C
ANISOU 1866 CD1 TYR A 311 7072 7642 8918 1605 -698 480 C
ATOM 1867 CD2 TYR A 311 60.751 -6.447 33.409 1.00 33.69 C
ANISOU 1867 CD2 TYR A 311 3539 4094 5167 1608 -469 534 C
ATOM 1868 CE1 TYR A 311 63.354 -6.346 34.342 1.00 74.98 C
ANISOU 1868 CE1 TYR A 311 8620 9281 10587 1641 -696 378 C
ATOM 1869 CE2 TYR A 311 61.673 -5.582 32.820 1.00 47.53 C
ANISOU 1869 CE2 TYR A 311 5232 5828 6999 1637 -460 485 C
ATOM 1870 CZ TYR A 311 62.978 -5.538 33.299 1.00 70.79 C
ANISOU 1870 CZ TYR A 311 8098 8772 10029 1670 -566 394 C
ATOM 1871 OH TYR A 311 63.931 -4.694 32.760 1.00 84.49 O
ANISOU 1871 OH TYR A 311 9759 10537 11806 1723 -521 335 O
ATOM 1872 N LEU A 312 58.211 -9.256 37.738 1.00 44.75 N
ANISOU 1872 N LEU A 312 5263 5478 6262 1615 -562 682 N
ATOM 1873 CA LEU A 312 56.957 -9.970 37.973 1.00 42.43 C
ANISOU 1873 CA LEU A 312 5063 5235 5824 1651 -461 710 C
ATOM 1874 C LEU A 312 55.746 -9.097 38.252 1.00 48.41 C
ANISOU 1874 C LEU A 312 5815 6040 6539 1717 -325 702 C
ATOM 1875 O LEU A 312 54.728 -9.254 37.552 1.00 55.53 O
ANISOU 1875 O LEU A 312 6655 7007 7438 1704 -225 693 O
ATOM 1876 CB LEU A 312 57.127 -10.946 39.137 1.00 40.57 C
ANISOU 1876 CB LEU A 312 5016 4977 5420 1740 -507 771 C
ATOM 1877 CG LEU A 312 55.854 -11.763 39.357 1.00 27.81 C
ANISOU 1877 CG LEU A 312 3533 3406 3627 1819 -369 813 C
ATOM 1878 CD1 LEU A 312 55.531 -12.658 38.179 1.00 26.86 C
ANISOU 1878 CD1 LEU A 312 3335 3332 3541 1745 -332 818 C
ATOM 1879 CD2 LEU A 312 55.925 -12.535 40.637 1.00 34.44 C
ANISOU 1879 CD2 LEU A 312 4681 4171 4234 1931 -404 859 C
ATOM 1880 N PRO A 313 55.779 -8.147 39.185 1.00 49.01 N
ANISOU 1880 N PRO A 313 5941 6086 6594 1798 -313 701 N
ATOM 1881 CA PRO A 313 54.529 -7.425 39.484 1.00 50.93 C
ANISOU 1881 CA PRO A 313 6181 6370 6801 1887 -152 693 C
ATOM 1882 C PRO A 313 53.947 -6.653 38.312 1.00 50.26 C
ANISOU 1882 C PRO A 313 5936 6321 6840 1815 -106 638 C
ATOM 1883 O PRO A 313 52.803 -6.933 37.912 1.00 45.42 O
ANISOU 1883 O PRO A 313 5256 5781 6220 1831 -8 630 O
ATOM 1884 CB PRO A 313 54.938 -6.510 40.655 1.00 43.17 C
ANISOU 1884 CB PRO A 313 5323 5312 5769 1990 -171 692 C
ATOM 1885 CG PRO A 313 56.440 -6.417 40.571 1.00 39.98 C
ANISOU 1885 CG PRO A 313 4892 4850 5449 1916 -363 688 C
ATOM 1886 CD PRO A 313 56.868 -7.770 40.098 1.00 44.32 C
ANISOU 1886 CD PRO A 313 5424 5420 5994 1839 -439 711 C
ATOM 1887 N ILE A 314 54.760 -5.880 37.593 1.00 57.10 N
ANISOU 1887 N ILE A 314 6747 7132 7815 1737 -193 601 N
ATOM 1888 CA ILE A 314 54.173 -5.110 36.503 1.00 56.28 C
ANISOU 1888 CA ILE A 314 6567 7042 7776 1709 -157 559 C
ATOM 1889 C ILE A 314 53.674 -6.057 35.429 1.00 63.30 C
ANISOU 1889 C ILE A 314 7414 8010 8628 1680 -133 583 C
ATOM 1890 O ILE A 314 52.547 -5.913 34.936 1.00 72.58 O
ANISOU 1890 O ILE A 314 8531 9235 9813 1707 -78 567 O
ATOM 1891 CB ILE A 314 55.170 -4.065 35.964 1.00 41.85 C
ANISOU 1891 CB ILE A 314 4736 5155 6009 1705 -199 556 C
ATOM 1892 CG1 ILE A 314 54.490 -3.169 34.920 1.00 55.82 C
ANISOU 1892 CG1 ILE A 314 6483 6937 7790 1741 -137 555 C
ATOM 1893 CG2 ILE A 314 56.414 -4.749 35.423 1.00 41.79 C
ANISOU 1893 CG2 ILE A 314 4716 5143 6017 1655 -273 573 C
ATOM 1894 CD1 ILE A 314 53.193 -2.534 35.391 1.00 65.81 C
ANISOU 1894 CD1 ILE A 314 7733 8211 9061 1812 -69 521 C
ATOM 1895 N SER A 315 54.397 -7.154 35.211 1.00 55.16 N
ANISOU 1895 N SER A 315 6411 6986 7562 1635 -181 614 N
ATOM 1896 CA SER A 315 53.996 -8.055 34.146 1.00 45.29 C
ANISOU 1896 CA SER A 315 5137 5794 6275 1608 -160 639 C
ATOM 1897 C SER A 315 52.669 -8.685 34.503 1.00 57.04 C
ANISOU 1897 C SER A 315 6594 7333 7745 1625 -108 626 C
ATOM 1898 O SER A 315 51.773 -8.790 33.657 1.00 78.22 O
ANISOU 1898 O SER A 315 9207 10069 10445 1631 -83 617 O
ATOM 1899 CB SER A 315 55.059 -9.122 33.910 1.00 40.07 C
ANISOU 1899 CB SER A 315 4521 5120 5585 1572 -214 668 C
ATOM 1900 OG SER A 315 56.280 -8.523 33.528 1.00 46.76 O
ANISOU 1900 OG SER A 315 5355 5924 6486 1566 -255 661 O
ATOM 1901 N VAL A 316 52.517 -9.088 35.761 1.00 46.17 N
ANISOU 1901 N VAL A 316 5267 5954 6324 1669 -75 642 N
ATOM 1902 CA VAL A 316 51.232 -9.626 36.171 1.00 46.11 C
ANISOU 1902 CA VAL A 316 5212 6042 6265 1762 60 672 C
ATOM 1903 C VAL A 316 50.160 -8.549 36.119 1.00 56.14 C
ANISOU 1903 C VAL A 316 6354 7353 7623 1807 132 602 C
ATOM 1904 O VAL A 316 49.077 -8.762 35.556 1.00 66.79 O
ANISOU 1904 O VAL A 316 7568 8781 9028 1818 175 563 O
ATOM 1905 CB VAL A 316 51.325 -10.259 37.567 1.00 45.83 C
ANISOU 1905 CB VAL A 316 5317 6002 6094 1883 148 748 C
ATOM 1906 CG1 VAL A 316 49.930 -10.613 38.073 1.00 29.13 C
ANISOU 1906 CG1 VAL A 316 3132 3981 3953 2008 372 762 C
ATOM 1907 CG2 VAL A 316 52.209 -11.483 37.517 1.00 27.13 C
ANISOU 1907 CG2 VAL A 316 3090 3586 3633 1850 53 807 C
ATOM 1908 N LEU A 317 50.479 -7.340 36.591 1.00 56.50 N
ANISOU 1908 N LEU A 317 6430 7339 7699 1833 125 572 N
ATOM 1909 CA LEU A 317 49.456 -6.300 36.631 1.00 52.17 C
ANISOU 1909 CA LEU A 317 5778 6814 7231 1898 196 500 C
ATOM 1910 C LEU A 317 48.923 -5.927 35.256 1.00 63.63 C
ANISOU 1910 C LEU A 317 7125 8263 8787 1850 105 438 C
ATOM 1911 O LEU A 317 47.696 -5.888 35.061 1.00 74.34 O
ANISOU 1911 O LEU A 317 8335 9689 10220 1902 154 372 O
ATOM 1912 CB LEU A 317 50.032 -5.059 37.308 1.00 31.49 C
ANISOU 1912 CB LEU A 317 3244 4110 4611 1944 196 493 C
ATOM 1913 CG LEU A 317 50.232 -5.122 38.811 1.00 30.14 C
ANISOU 1913 CG LEU A 317 3195 3920 4338 2052 309 532 C
ATOM 1914 CD1 LEU A 317 50.791 -3.808 39.318 1.00 37.42 C
ANISOU 1914 CD1 LEU A 317 4205 4744 5268 2098 292 517 C
ATOM 1915 CD2 LEU A 317 48.880 -5.381 39.422 1.00 31.77 C
ANISOU 1915 CD2 LEU A 317 3323 4209 4540 2153 523 487 C
ATOM 1916 N ASN A 318 49.790 -5.882 34.244 1.00 57.01 N
ANISOU 1916 N ASN A 318 6355 7382 7925 1792 7 485 N
ATOM 1917 CA ASN A 318 49.270 -5.522 32.935 1.00 51.47 C
ANISOU 1917 CA ASN A 318 5598 6701 7257 1826 -35 485 C
ATOM 1918 C ASN A 318 48.400 -6.627 32.388 1.00 51.83 C
ANISOU 1918 C ASN A 318 5543 6822 7330 1809 -50 464 C
ATOM 1919 O ASN A 318 47.324 -6.344 31.841 1.00 60.18 O
ANISOU 1919 O ASN A 318 6475 7914 8477 1869 -72 410 O
ATOM 1920 CB ASN A 318 50.404 -5.185 31.969 1.00 64.36 C
ANISOU 1920 CB ASN A 318 7336 8281 8838 1800 -83 551 C
ATOM 1921 CG ASN A 318 50.876 -3.751 32.111 1.00 92.82 C
ANISOU 1921 CG ASN A 318 10997 11808 12462 1848 -76 550 C
ATOM 1922 OD1 ASN A 318 51.083 -3.253 33.222 1.00 88.23 O
ANISOU 1922 OD1 ASN A 318 10436 11193 11895 1858 -46 526 O
ATOM 1923 ND2 ASN A 318 51.017 -3.067 30.983 1.00120.99 N
ANISOU 1923 ND2 ASN A 318 14604 15335 16029 1888 -103 576 N
ATOM 1924 N VAL A 319 48.709 -7.874 32.741 1.00 40.42 N
ANISOU 1924 N VAL A 319 4128 5398 5831 1742 -34 488 N
ATOM 1925 CA VAL A 319 47.828 -8.945 32.315 1.00 35.86 C
ANISOU 1925 CA VAL A 319 3444 4890 5293 1724 -38 456 C
ATOM 1926 C VAL A 319 46.474 -8.797 32.981 1.00 56.39 C
ANISOU 1926 C VAL A 319 5848 7600 7979 1806 73 379 C
ATOM 1927 O VAL A 319 45.447 -8.662 32.297 1.00 74.94 O
ANISOU 1927 O VAL A 319 8029 9992 10451 1833 36 300 O
ATOM 1928 CB VAL A 319 48.453 -10.306 32.650 1.00 27.36 C
ANISOU 1928 CB VAL A 319 2458 3838 4100 1687 -2 543 C
ATOM 1929 CG1 VAL A 319 47.389 -11.375 32.610 1.00 53.67 C
ANISOU 1929 CG1 VAL A 319 5649 7307 7435 1730 80 554 C
ATOM 1930 CG2 VAL A 319 49.593 -10.622 31.710 1.00 50.19 C
ANISOU 1930 CG2 VAL A 319 5483 6657 6932 1619 -91 597 C
ATOM 1931 N LEU A 320 46.468 -8.599 34.300 1.00 55.98 N
ANISOU 1931 N LEU A 320 5805 7578 7885 1858 215 387 N
ATOM 1932 CA LEU A 320 45.181 -8.477 34.965 1.00 47.83 C
ANISOU 1932 CA LEU A 320 4565 6664 6943 1925 381 283 C
ATOM 1933 C LEU A 320 44.416 -7.296 34.398 1.00 60.15 C
ANISOU 1933 C LEU A 320 5996 8190 8669 1967 301 166 C
ATOM 1934 O LEU A 320 43.189 -7.360 34.254 1.00 72.14 O
ANISOU 1934 O LEU A 320 7271 9802 10337 1995 358 48 O
ATOM 1935 CB LEU A 320 45.377 -8.351 36.479 1.00 42.08 C
ANISOU 1935 CB LEU A 320 3920 5943 6127 1985 583 309 C
ATOM 1936 CG LEU A 320 46.200 -9.488 37.103 1.00 44.84 C
ANISOU 1936 CG LEU A 320 4447 6280 6309 1991 663 451 C
ATOM 1937 CD1 LEU A 320 46.384 -9.278 38.593 1.00 55.38 C
ANISOU 1937 CD1 LEU A 320 5928 7570 7545 2085 878 470 C
ATOM 1938 CD2 LEU A 320 45.553 -10.834 36.839 1.00 39.87 C
ANISOU 1938 CD2 LEU A 320 3695 5779 5674 1958 785 459 C
ATOM 1939 N LYS A 321 45.130 -6.230 34.026 1.00 33.20 N
ANISOU 1939 N LYS A 321 2727 4638 5250 1971 178 198 N
ATOM 1940 CA LYS A 321 44.448 -5.066 33.487 1.00 60.52 C
ANISOU 1940 CA LYS A 321 6095 8041 8858 2040 113 125 C
ATOM 1941 C LYS A 321 44.013 -5.313 32.045 1.00 67.16 C
ANISOU 1941 C LYS A 321 6862 8902 9754 2063 -16 156 C
ATOM 1942 O LYS A 321 42.855 -5.061 31.686 1.00 71.28 O
ANISOU 1942 O LYS A 321 7179 9458 10447 2135 -27 89 O
ATOM 1943 CB LYS A 321 45.350 -3.829 33.621 1.00 49.46 C
ANISOU 1943 CB LYS A 321 4881 6541 7371 2088 86 196 C
ATOM 1944 CG LYS A 321 44.847 -2.532 32.986 1.00 45.94 C
ANISOU 1944 CG LYS A 321 4406 6049 7000 2218 36 188 C
ATOM 1945 CD LYS A 321 45.913 -1.443 33.127 1.00 54.07 C
ANISOU 1945 CD LYS A 321 5642 6975 7926 2240 28 259 C
ATOM 1946 CE LYS A 321 45.395 -0.068 32.708 1.00 73.52 C
ANISOU 1946 CE LYS A 321 8108 9378 10450 2390 4 246 C
ATOM 1947 NZ LYS A 321 46.333 1.042 33.085 1.00 75.34 N
ANISOU 1947 NZ LYS A 321 8528 9500 10600 2410 30 289 N
ATOM 1948 N ARG A 322 44.934 -5.803 31.204 1.00 64.28 N
ANISOU 1948 N ARG A 322 6656 8510 9256 2008 -105 262 N
ATOM 1949 CA ARG A 322 44.657 -5.872 29.772 1.00 47.37 C
ANISOU 1949 CA ARG A 322 4497 6365 7137 2046 -228 303 C
ATOM 1950 C ARG A 322 43.965 -7.147 29.316 1.00 45.81 C
ANISOU 1950 C ARG A 322 4153 6243 7009 1994 -263 271 C
ATOM 1951 O ARG A 322 43.189 -7.103 28.353 1.00 64.30 O
ANISOU 1951 O ARG A 322 6380 8603 9449 2053 -357 274 O
ATOM 1952 CB ARG A 322 45.947 -5.647 28.974 1.00 42.33 C
ANISOU 1952 CB ARG A 322 4091 5653 6341 2021 -278 413 C
ATOM 1953 CG ARG A 322 46.573 -4.278 29.263 1.00 56.07 C
ANISOU 1953 CG ARG A 322 5951 7313 8040 2075 -247 439 C
ATOM 1954 CD ARG A 322 45.678 -3.175 28.678 1.00 61.50 C
ANISOU 1954 CD ARG A 322 6577 7974 8819 2222 -305 419 C
ATOM 1955 NE ARG A 322 46.313 -1.862 28.597 1.00 59.66 N
ANISOU 1955 NE ARG A 322 6495 7645 8528 2287 -292 458 N
ATOM 1956 CZ ARG A 322 45.687 -0.776 28.151 1.00 87.84 C
ANISOU 1956 CZ ARG A 322 10063 11170 12143 2435 -334 454 C
ATOM 1957 NH1 ARG A 322 44.422 -0.857 27.754 1.00100.26 N
ANISOU 1957 NH1 ARG A 322 11468 12798 13830 2537 -399 415 N
ATOM 1958 NH2 ARG A 322 46.309 0.394 28.117 1.00 97.73 N
ANISOU 1958 NH2 ARG A 322 11477 12324 13333 2492 -310 488 N
ATOM 1959 N VAL A 323 44.217 -8.272 29.974 1.00 39.93 N
ANISOU 1959 N VAL A 323 3413 5541 6218 1892 -191 252 N
ATOM 1960 CA VAL A 323 43.603 -9.531 29.565 1.00 49.35 C
ANISOU 1960 CA VAL A 323 4471 6827 7453 1851 -203 229 C
ATOM 1961 C VAL A 323 42.330 -9.808 30.360 1.00 62.02 C
ANISOU 1961 C VAL A 323 5773 8604 9189 1882 -55 122 C
ATOM 1962 O VAL A 323 41.359 -10.343 29.817 1.00 65.86 O
ANISOU 1962 O VAL A 323 6029 9198 9797 1883 -75 83 O
ATOM 1963 CB VAL A 323 44.618 -10.688 29.667 1.00 46.19 C
ANISOU 1963 CB VAL A 323 4249 6441 6860 1779 -172 327 C
ATOM 1964 CG1 VAL A 323 43.982 -11.982 29.194 1.00 44.29 C
ANISOU 1964 CG1 VAL A 323 3868 6342 6617 1770 -170 335 C
ATOM 1965 CG2 VAL A 323 45.848 -10.378 28.821 1.00 45.04 C
ANISOU 1965 CG2 VAL A 323 4350 6160 6603 1748 -270 418 C
ATOM 1966 N PHE A 324 42.303 -9.454 31.646 1.00 68.92 N
ANISOU 1966 N PHE A 324 6625 9516 10045 1897 115 72 N
ATOM 1967 CA PHE A 324 41.165 -9.738 32.508 1.00 73.80 C
ANISOU 1967 CA PHE A 324 6956 10301 10783 1891 333 -56 C
ATOM 1968 C PHE A 324 40.307 -8.523 32.816 1.00104.11 C
ANISOU 1968 C PHE A 324 10631 14097 14828 1970 385 -152 C
ATOM 1969 O PHE A 324 39.280 -8.672 33.484 1.00120.79 O
ANISOU 1969 O PHE A 324 12486 16330 17079 1951 606 -254 O
ATOM 1970 CB PHE A 324 41.643 -10.311 33.846 1.00 65.30 C
ANISOU 1970 CB PHE A 324 5975 9306 9530 1851 569 -30 C
ATOM 1971 CG PHE A 324 42.302 -11.643 33.746 1.00 61.06 C
ANISOU 1971 CG PHE A 324 5558 8824 8819 1793 598 108 C
ATOM 1972 CD1 PHE A 324 43.480 -11.809 33.039 1.00 62.50 C
ANISOU 1972 CD1 PHE A 324 6006 8866 8876 1804 397 262 C
ATOM 1973 CD2 PHE A 324 41.755 -12.734 34.397 1.00 50.05 C
ANISOU 1973 CD2 PHE A 324 4020 7611 7388 1700 878 79 C
ATOM 1974 CE1 PHE A 324 44.080 -13.046 32.964 1.00 55.24 C
ANISOU 1974 CE1 PHE A 324 5200 7974 7814 1779 429 400 C
ATOM 1975 CE2 PHE A 324 42.352 -13.965 34.327 1.00 44.53 C
ANISOU 1975 CE2 PHE A 324 3457 6934 6528 1650 936 231 C
ATOM 1976 CZ PHE A 324 43.516 -14.123 33.611 1.00 54.14 C
ANISOU 1976 CZ PHE A 324 4920 8008 7641 1736 692 405 C
ATOM 1977 N GLY A 325 40.689 -7.332 32.369 1.00107.03 N
ANISOU 1977 N GLY A 325 11146 14302 15220 2048 232 -101 N
ATOM 1978 CA GLY A 325 39.770 -6.220 32.489 1.00112.65 C
ANISOU 1978 CA GLY A 325 11707 14984 16112 2146 278 -143 C
ATOM 1979 C GLY A 325 39.656 -5.695 33.902 1.00107.12 C
ANISOU 1979 C GLY A 325 10990 14304 15407 2174 494 -254 C
ATOM 1980 O GLY A 325 38.664 -5.038 34.235 1.00107.07 O
ANISOU 1980 O GLY A 325 10808 14318 15554 2245 617 -305 O
ATOM 1981 N MET A 326 40.634 -6.002 34.754 1.00100.44 N
ANISOU 1981 N MET A 326 10343 13470 14349 2131 562 -250 N
ATOM 1982 CA MET A 326 40.653 -5.586 36.147 1.00 92.65 C
ANISOU 1982 CA MET A 326 9400 12515 13288 2162 780 -326 C
ATOM 1983 C MET A 326 41.068 -4.121 36.299 1.00 83.86 C
ANISOU 1983 C MET A 326 8443 11256 12165 2268 699 -299 C
ATOM 1984 O MET A 326 41.557 -3.475 35.368 1.00 89.79 O
ANISOU 1984 O MET A 326 9310 11882 12925 2293 488 -207 O
ATOM 1985 CB MET A 326 41.565 -6.509 36.947 1.00 97.83 C
ANISOU 1985 CB MET A 326 10260 13218 13691 2094 897 -222 C
ATOM 1986 CG MET A 326 41.060 -7.935 36.941 1.00110.42 C
ANISOU 1986 CG MET A 326 11701 14975 15278 1985 1046 -256 C
ATOM 1987 SD MET A 326 41.820 -9.016 38.154 1.00122.28 S
ANISOU 1987 SD MET A 326 13445 16498 16518 1921 1325 -120 S
ATOM 1988 CE MET A 326 40.938 -10.541 37.817 1.00125.18 C
ANISOU 1988 CE MET A 326 13573 17065 16926 1746 1510 -191 C
ATOM 1989 N PHE A 327 40.861 -3.606 37.512 1.00 82.32 N
ANISOU 1989 N PHE A 327 8263 11083 11934 2322 904 -386 N
ATOM 1990 CA PHE A 327 41.316 -2.297 37.970 1.00 86.07 C
ANISOU 1990 CA PHE A 327 8915 11435 12353 2425 888 -359 C
ATOM 1991 C PHE A 327 40.534 -1.166 37.318 1.00 94.48 C
ANISOU 1991 C PHE A 327 9841 12424 13635 2538 802 -424 C
ATOM 1992 O PHE A 327 41.051 -0.047 37.176 1.00 96.38 O
ANISOU 1992 O PHE A 327 10254 12539 13829 2617 705 -358 O
ATOM 1993 CB PHE A 327 42.814 -2.075 37.691 1.00 80.03 C
ANISOU 1993 CB PHE A 327 8454 10545 11408 2392 715 -167 C
ATOM 1994 CG PHE A 327 43.699 -3.224 38.074 1.00 69.72 C
ANISOU 1994 CG PHE A 327 7291 9271 9929 2299 749 -50 C
ATOM 1995 CD1 PHE A 327 43.619 -3.804 39.329 1.00 72.16 C
ANISOU 1995 CD1 PHE A 327 7650 9635 10134 2304 999 -60 C
ATOM 1996 CD2 PHE A 327 44.646 -3.694 37.180 1.00 73.93 C
ANISOU 1996 CD2 PHE A 327 7935 9754 10400 2212 554 74 C
ATOM 1997 CE1 PHE A 327 44.450 -4.847 39.674 1.00 77.60 C
ANISOU 1997 CE1 PHE A 327 8499 10317 10670 2253 1034 72 C
ATOM 1998 CE2 PHE A 327 45.481 -4.734 37.517 1.00 82.02 C
ANISOU 1998 CE2 PHE A 327 9089 10792 11285 2149 574 184 C
ATOM 1999 CZ PHE A 327 45.383 -5.313 38.768 1.00 82.54 C
ANISOU 1999 CZ PHE A 327 9205 10902 11255 2188 801 196 C
ATOM 2000 N ARG A 328 39.308 -1.434 36.878 1.00101.14 N
ANISOU 2000 N ARG A 328 10393 13329 14708 2545 850 -508 N
ATOM 2001 CA ARG A 328 38.460 -0.395 36.310 1.00106.68 C
ANISOU 2001 CA ARG A 328 10977 13959 15599 2680 806 -494 C
ATOM 2002 C ARG A 328 37.511 0.292 37.288 1.00122.76 C
ANISOU 2002 C ARG A 328 12876 16014 17752 2776 1047 -635 C
ATOM 2003 O ARG A 328 36.903 1.293 36.902 1.00132.61 O
ANISOU 2003 O ARG A 328 14055 17198 19133 2940 1016 -604 O
ATOM 2004 CB ARG A 328 37.705 -0.969 35.116 1.00101.41 C
ANISOU 2004 CB ARG A 328 10115 13349 15066 2676 708 -386 C
ATOM 2005 CG ARG A 328 38.715 -1.312 34.054 1.00106.21 C
ANISOU 2005 CG ARG A 328 10914 13890 15550 2604 455 -264 C
ATOM 2006 CD ARG A 328 38.227 -2.210 32.958 1.00121.54 C
ANISOU 2006 CD ARG A 328 12712 15925 17541 2576 351 -176 C
ATOM 2007 NE ARG A 328 39.344 -2.442 32.049 1.00136.18 N
ANISOU 2007 NE ARG A 328 14789 17721 19230 2542 141 -80 N
ATOM 2008 CZ ARG A 328 39.328 -3.282 31.023 1.00144.41 C
ANISOU 2008 CZ ARG A 328 15804 18817 20250 2497 14 -7 C
ATOM 2009 NH1 ARG A 328 40.412 -3.412 30.264 1.00150.29 N
ANISOU 2009 NH1 ARG A 328 16797 19498 20807 2455 -133 78 N
ATOM 2010 NH2 ARG A 328 38.236 -3.990 30.759 1.00141.74 N
ANISOU 2010 NH2 ARG A 328 15206 18612 20036 2487 53 -9 N
ATOM 2011 N GLN A 329 37.360 -0.182 38.527 1.00124.24 N
ANISOU 2011 N GLN A 329 13038 16298 17871 2694 1295 -796 N
ATOM 2012 CA GLN A 329 36.487 0.521 39.464 1.00127.60 C
ANISOU 2012 CA GLN A 329 13359 16729 18394 2769 1541 -957 C
ATOM 2013 C GLN A 329 37.220 1.738 40.027 1.00128.91 C
ANISOU 2013 C GLN A 329 13774 16803 18402 2916 1486 -997 C
ATOM 2014 O GLN A 329 38.412 1.672 40.346 1.00139.24 O
ANISOU 2014 O GLN A 329 15346 18078 19482 2906 1429 -910 O
ATOM 2015 CB GLN A 329 35.982 -0.419 40.568 1.00137.10 C
ANISOU 2015 CB GLN A 329 14455 18116 19521 2606 1828 -1177 C
ATOM 2016 CG GLN A 329 37.017 -1.166 41.392 1.00142.39 C
ANISOU 2016 CG GLN A 329 15365 18985 19751 2560 1853 -1201 C
ATOM 2017 CD GLN A 329 36.360 -2.150 42.356 1.00148.72 C
ANISOU 2017 CD GLN A 329 16099 20183 20225 2529 2144 -1263 C
ATOM 2018 OE1 GLN A 329 35.150 -2.092 42.590 1.00155.87 O
ANISOU 2018 OE1 GLN A 329 16830 21361 21031 2694 2337 -1179 O
ATOM 2019 NE2 GLN A 329 37.153 -3.059 42.911 1.00146.31 N
ANISOU 2019 NE2 GLN A 329 16000 19791 19801 2381 2338 -1150 N
ATOM 2020 N ALA A 330 36.505 2.867 40.103 1.00136.84 N
ANISOU 2020 N ALA A 330 14705 17725 19563 3073 1542 -1056 N
ATOM 2021 CA ALA A 330 37.055 4.136 40.569 1.00134.90 C
ANISOU 2021 CA ALA A 330 14695 17360 19203 3238 1519 -1068 C
ATOM 2022 C ALA A 330 37.026 4.349 42.084 1.00143.88 C
ANISOU 2022 C ALA A 330 15941 18560 20167 3266 1785 -1244 C
ATOM 2023 O ALA A 330 37.608 5.332 42.552 1.00136.63 O
ANISOU 2023 O ALA A 330 15304 17508 19103 3375 1791 -1180 O
ATOM 2024 CB ALA A 330 36.308 5.299 39.898 1.00123.85 C
ANISOU 2024 CB ALA A 330 13195 15843 18019 3437 1453 -1039 C
ATOM 2025 N SER A 331 36.368 3.487 42.868 1.00161.99 N
ANISOU 2025 N SER A 331 18089 21068 22391 3158 2005 -1418 N
ATOM 2026 CA SER A 331 36.415 3.636 44.326 1.00167.38 C
ANISOU 2026 CA SER A 331 18953 21819 22825 3203 2302 -1515 C
ATOM 2027 C SER A 331 37.817 3.464 44.918 1.00169.48 C
ANISOU 2027 C SER A 331 19682 21893 22818 3109 2340 -1253 C
ATOM 2028 O SER A 331 38.156 4.127 45.906 1.00174.34 O
ANISOU 2028 O SER A 331 20606 22356 23278 3150 2511 -1219 O
ATOM 2029 CB SER A 331 35.437 2.658 44.982 1.00169.89 C
ANISOU 2029 CB SER A 331 19078 22470 23000 3130 2552 -1650 C
ATOM 2030 OG SER A 331 35.687 1.328 44.569 1.00168.52 O
ANISOU 2030 OG SER A 331 18847 22421 22760 2959 2512 -1546 O
ATOM 2031 N ASP A 332 38.641 2.595 44.343 1.00169.80 N
ANISOU 2031 N ASP A 332 19789 21922 22806 2985 2183 -1075 N
ATOM 2032 CA ASP A 332 40.024 2.393 44.775 1.00165.37 C
ANISOU 2032 CA ASP A 332 19630 21188 22013 2918 2168 -841 C
ATOM 2033 C ASP A 332 41.046 2.874 43.746 1.00157.34 C
ANISOU 2033 C ASP A 332 18717 20059 21007 2958 1824 -654 C
ATOM 2034 O ASP A 332 42.095 2.257 43.564 1.00159.04 O
ANISOU 2034 O ASP A 332 19093 20232 21105 2874 1712 -483 O
ATOM 2035 CB ASP A 332 40.267 0.925 45.126 1.00167.98 C
ANISOU 2035 CB ASP A 332 20011 21587 22226 2740 2310 -784 C
ATOM 2036 CG ASP A 332 39.927 -0.013 43.988 1.00170.26 C
ANISOU 2036 CG ASP A 332 19978 22055 22658 2666 2135 -796 C
ATOM 2037 OD1 ASP A 332 39.309 0.452 43.007 1.00172.64 O
ANISOU 2037 OD1 ASP A 332 19999 22422 23174 2742 1938 -892 O
ATOM 2038 OD2 ASP A 332 40.275 -1.212 44.076 1.00170.87 O
ANISOU 2038 OD2 ASP A 332 20116 22169 22639 2529 2204 -713 O
ATOM 2039 N ARG A 333 40.768 3.997 43.083 1.00148.07 N
ANISOU 2039 N ARG A 333 17472 18827 19963 3084 1670 -685 N
ATOM 2040 CA ARG A 333 41.707 4.539 42.104 1.00138.99 C
ANISOU 2040 CA ARG A 333 16455 17563 18792 3095 1391 -515 C
ATOM 2041 C ARG A 333 43.074 4.884 42.708 1.00135.16 C
ANISOU 2041 C ARG A 333 16344 16925 18086 3072 1389 -360 C
ATOM 2042 O ARG A 333 44.119 4.617 42.088 1.00140.78 O
ANISOU 2042 O ARG A 333 17149 17603 18739 2987 1204 -214 O
ATOM 2043 CB ARG A 333 41.039 5.799 41.532 1.00138.70 C
ANISOU 2043 CB ARG A 333 16338 17458 18906 3254 1313 -585 C
ATOM 2044 CG ARG A 333 41.624 6.575 40.357 1.00132.22 C
ANISOU 2044 CG ARG A 333 15624 16523 18092 3290 1067 -451 C
ATOM 2045 CD ARG A 333 40.646 7.748 40.096 1.00134.93 C
ANISOU 2045 CD ARG A 333 15881 16803 18585 3490 1076 -550 C
ATOM 2046 NE ARG A 333 41.075 8.753 39.122 1.00142.33 N
ANISOU 2046 NE ARG A 333 16981 17607 19491 3571 899 -434 N
ATOM 2047 CZ ARG A 333 41.204 10.051 39.399 1.00141.22 C
ANISOU 2047 CZ ARG A 333 17063 17324 19272 3718 938 -429 C
ATOM 2048 NH1 ARG A 333 40.940 10.503 40.620 1.00141.31 N
ANISOU 2048 NH1 ARG A 333 17159 17297 19235 3797 1139 -531 N
ATOM 2049 NH2 ARG A 333 41.591 10.901 38.457 1.00136.19 N
ANISOU 2049 NH2 ARG A 333 16591 16570 18584 3787 792 -327 N
ATOM 2050 N GLU A 334 43.107 5.409 43.940 1.00129.02 N
ANISOU 2050 N GLU A 334 15788 16044 17188 3132 1605 -404 N
ATOM 2051 CA GLU A 334 44.410 5.740 44.518 1.00116.52 C
ANISOU 2051 CA GLU A 334 14574 14287 15413 3112 1591 -278 C
ATOM 2052 C GLU A 334 45.257 4.501 44.855 1.00103.49 C
ANISOU 2052 C GLU A 334 13027 12650 13644 2993 1587 -180 C
ATOM 2053 O GLU A 334 46.484 4.509 44.656 1.00112.62 O
ANISOU 2053 O GLU A 334 14347 13719 14723 2953 1422 -58 O
ATOM 2054 CB GLU A 334 44.195 6.585 45.779 1.00126.33 C
ANISOU 2054 CB GLU A 334 16083 15377 16540 3194 1830 -363 C
ATOM 2055 CG GLU A 334 43.693 8.034 45.558 1.00133.69 C
ANISOU 2055 CG GLU A 334 17027 16228 17540 3342 1817 -429 C
ATOM 2056 CD GLU A 334 44.654 8.943 44.799 1.00131.77 C
ANISOU 2056 CD GLU A 334 16944 15856 17266 3366 1599 -308 C
ATOM 2057 OE1 GLU A 334 45.868 8.649 44.763 1.00126.39 O
ANISOU 2057 OE1 GLU A 334 16432 15107 16484 3269 1494 -191 O
ATOM 2058 OE2 GLU A 334 44.182 9.966 44.245 1.00133.45 O
ANISOU 2058 OE2 GLU A 334 17120 16028 17558 3486 1545 -342 O
ATOM 2059 N ALA A 335 44.615 3.399 45.276 1.00 89.78 N
ANISOU 2059 N ALA A 335 11181 11026 11905 2932 1759 -242 N
ATOM 2060 CA ALA A 335 45.347 2.165 45.576 1.00 89.90 C
ANISOU 2060 CA ALA A 335 11323 11039 11796 2842 1767 -150 C
ATOM 2061 C ALA A 335 45.955 1.512 44.335 1.00 95.96 C
ANISOU 2061 C ALA A 335 11907 11908 12644 2773 1477 -28 C
ATOM 2062 O ALA A 335 47.110 1.057 44.359 1.00101.83 O
ANISOU 2062 O ALA A 335 12813 12587 13290 2741 1345 89 O
ATOM 2063 CB ALA A 335 44.422 1.186 46.297 1.00 89.00 C
ANISOU 2063 CB ALA A 335 11168 11004 11645 2766 2073 -258 C
ATOM 2064 N VAL A 336 45.221 1.521 43.222 1.00 90.28 N
ANISOU 2064 N VAL A 336 10875 11325 12101 2749 1357 -70 N
ATOM 2065 CA VAL A 336 45.746 0.982 41.970 1.00 67.69 C
ANISOU 2065 CA VAL A 336 7891 8526 9301 2655 1098 25 C
ATOM 2066 C VAL A 336 46.902 1.834 41.480 1.00 63.76 C
ANISOU 2066 C VAL A 336 7547 7907 8774 2644 904 121 C
ATOM 2067 O VAL A 336 47.910 1.305 40.983 1.00 63.35 O
ANISOU 2067 O VAL A 336 7532 7848 8689 2545 749 220 O
ATOM 2068 CB VAL A 336 44.640 0.832 40.910 1.00 64.17 C
ANISOU 2068 CB VAL A 336 7140 8204 9037 2636 1023 -69 C
ATOM 2069 CG1 VAL A 336 43.763 -0.371 41.246 1.00 61.94 C
ANISOU 2069 CG1 VAL A 336 6682 8069 8785 2586 1195 -154 C
ATOM 2070 CG2 VAL A 336 43.816 2.103 40.815 1.00 74.03 C
ANISOU 2070 CG2 VAL A 336 8316 9414 10399 2759 1048 -181 C
ATOM 2071 N TYR A 337 46.763 3.167 41.567 1.00 59.18 N
ANISOU 2071 N TYR A 337 7047 7229 8212 2738 924 81 N
ATOM 2072 CA TYR A 337 47.879 4.014 41.164 1.00 53.25 C
ANISOU 2072 CA TYR A 337 6455 6351 7424 2721 788 161 C
ATOM 2073 C TYR A 337 49.117 3.686 41.985 1.00 59.62 C
ANISOU 2073 C TYR A 337 7473 7073 8106 2686 783 233 C
ATOM 2074 O TYR A 337 50.228 3.606 41.444 1.00 76.61 O
ANISOU 2074 O TYR A 337 9651 9194 10263 2597 627 308 O
ATOM 2075 CB TYR A 337 47.541 5.484 41.397 1.00 66.35 C
ANISOU 2075 CB TYR A 337 8234 7892 9085 2851 859 107 C
ATOM 2076 CG TYR A 337 46.583 6.135 40.434 1.00 82.22 C
ANISOU 2076 CG TYR A 337 10089 9931 11221 2921 803 50 C
ATOM 2077 CD1 TYR A 337 46.471 5.710 39.118 1.00 94.22 C
ANISOU 2077 CD1 TYR A 337 11445 11520 12833 2848 641 80 C
ATOM 2078 CD2 TYR A 337 45.767 7.181 40.859 1.00 86.37 C
ANISOU 2078 CD2 TYR A 337 10654 10392 11769 3076 915 -40 C
ATOM 2079 CE1 TYR A 337 45.577 6.325 38.250 1.00 98.00 C
ANISOU 2079 CE1 TYR A 337 11815 11995 13426 2941 581 31 C
ATOM 2080 CE2 TYR A 337 44.877 7.791 40.004 1.00 85.77 C
ANISOU 2080 CE2 TYR A 337 10443 10327 11819 3174 850 -94 C
ATOM 2081 CZ TYR A 337 44.785 7.364 38.707 1.00 85.97 C
ANISOU 2081 CZ TYR A 337 10317 10412 11936 3112 679 -53 C
ATOM 2082 OH TYR A 337 43.894 7.988 37.873 1.00 83.73 O
ANISOU 2082 OH TYR A 337 9928 10112 11775 3234 612 -96 O
ATOM 2083 N ALA A 338 48.942 3.418 43.282 1.00 45.09 N
ANISOU 2083 N ALA A 338 5793 5184 6155 2754 954 197 N
ATOM 2084 CA ALA A 338 50.116 3.122 44.094 1.00 41.03 C
ANISOU 2084 CA ALA A 338 5533 4546 5509 2749 909 250 C
ATOM 2085 C ALA A 338 50.750 1.793 43.689 1.00 51.62 C
ANISOU 2085 C ALA A 338 6773 5986 6853 2652 758 333 C
ATOM 2086 O ALA A 338 51.984 1.687 43.595 1.00 60.02 O
ANISOU 2086 O ALA A 338 7907 6994 7903 2600 576 393 O
ATOM 2087 CB ALA A 338 49.733 3.114 45.571 1.00 41.10 C
ANISOU 2087 CB ALA A 338 5833 4427 5357 2841 1139 170 C
ATOM 2088 N ALA A 339 49.925 0.796 43.357 1.00 54.46 N
ANISOU 2088 N ALA A 339 6948 6494 7250 2618 822 327 N
ATOM 2089 CA ALA A 339 50.478 -0.507 42.984 1.00 48.22 C
ANISOU 2089 CA ALA A 339 6097 5782 6444 2531 694 404 C
ATOM 2090 C ALA A 339 51.216 -0.446 41.647 1.00 57.49 C
ANISOU 2090 C ALA A 339 7107 7002 7733 2387 470 450 C
ATOM 2091 O ALA A 339 52.348 -0.949 41.517 1.00 57.55 O
ANISOU 2091 O ALA A 339 7149 6990 7727 2312 314 505 O
ATOM 2092 CB ALA A 339 49.362 -1.548 42.937 1.00 35.89 C
ANISOU 2092 CB ALA A 339 4398 4347 4891 2529 849 375 C
ATOM 2093 N PHE A 340 50.603 0.190 40.643 1.00 55.64 N
ANISOU 2093 N PHE A 340 6721 6807 7611 2353 455 409 N
ATOM 2094 CA PHE A 340 51.284 0.316 39.359 1.00 48.78 C
ANISOU 2094 CA PHE A 340 5775 5935 6824 2231 292 435 C
ATOM 2095 C PHE A 340 52.531 1.176 39.474 1.00 60.16 C
ANISOU 2095 C PHE A 340 7334 7257 8268 2226 223 464 C
ATOM 2096 O PHE A 340 53.535 0.911 38.802 1.00 71.91 O
ANISOU 2096 O PHE A 340 8787 8734 9801 2125 105 495 O
ATOM 2097 CB PHE A 340 50.351 0.882 38.297 1.00 50.73 C
ANISOU 2097 CB PHE A 340 5907 6206 7160 2237 283 385 C
ATOM 2098 CG PHE A 340 49.443 -0.139 37.700 1.00 62.89 C
ANISOU 2098 CG PHE A 340 7294 7860 8743 2193 274 356 C
ATOM 2099 CD1 PHE A 340 48.228 -0.437 38.285 1.00 79.46 C
ANISOU 2099 CD1 PHE A 340 9296 10039 10858 2273 404 292 C
ATOM 2100 CD2 PHE A 340 49.828 -0.842 36.574 1.00 61.74 C
ANISOU 2100 CD2 PHE A 340 7101 7734 8622 2073 153 381 C
ATOM 2101 CE1 PHE A 340 47.389 -1.395 37.727 1.00 86.43 C
ANISOU 2101 CE1 PHE A 340 10015 11026 11798 2235 399 255 C
ATOM 2102 CE2 PHE A 340 49.001 -1.798 36.016 1.00 71.34 C
ANISOU 2102 CE2 PHE A 340 8196 9039 9873 2041 141 354 C
ATOM 2103 CZ PHE A 340 47.781 -2.077 36.593 1.00 83.92 C
ANISOU 2103 CZ PHE A 340 9673 10718 11496 2122 257 293 C
ATOM 2104 N THR A 341 52.499 2.202 40.322 1.00 55.96 N
ANISOU 2104 N THR A 341 6947 6622 7692 2343 307 444 N
ATOM 2105 CA THR A 341 53.674 3.043 40.458 1.00 51.28 C
ANISOU 2105 CA THR A 341 6479 5898 7108 2350 248 465 C
ATOM 2106 C THR A 341 54.833 2.282 41.082 1.00 52.93 C
ANISOU 2106 C THR A 341 6736 6088 7287 2316 131 501 C
ATOM 2107 O THR A 341 55.976 2.389 40.617 1.00 53.50 O
ANISOU 2107 O THR A 341 6764 6125 7437 2254 17 525 O
ATOM 2108 CB THR A 341 53.359 4.264 41.303 1.00 52.37 C
ANISOU 2108 CB THR A 341 6819 5896 7182 2485 368 423 C
ATOM 2109 OG1 THR A 341 52.477 5.135 40.588 1.00 68.05 O
ANISOU 2109 OG1 THR A 341 8761 7881 9212 2527 434 391 O
ATOM 2110 CG2 THR A 341 54.650 4.971 41.650 1.00 50.24 C
ANISOU 2110 CG2 THR A 341 6723 5459 6905 2496 301 436 C
ATOM 2111 N PHE A 342 54.562 1.487 42.123 1.00 48.57 N
ANISOU 2111 N PHE A 342 6284 5553 6619 2374 153 501 N
ATOM 2112 CA PHE A 342 55.648 0.698 42.685 1.00 40.01 C
ANISOU 2112 CA PHE A 342 5271 4447 5482 2357 -16 531 C
ATOM 2113 C PHE A 342 56.170 -0.325 41.685 1.00 46.05 C
ANISOU 2113 C PHE A 342 5815 5331 6350 2209 -131 569 C
ATOM 2114 O PHE A 342 57.373 -0.615 41.673 1.00 49.42 O
ANISOU 2114 O PHE A 342 6207 5743 6826 2166 -295 585 O
ATOM 2115 CB PHE A 342 55.192 0.005 43.965 1.00 43.38 C
ANISOU 2115 CB PHE A 342 5940 4828 5715 2465 25 521 C
ATOM 2116 CG PHE A 342 56.228 -0.901 44.544 1.00 48.75 C
ANISOU 2116 CG PHE A 342 6742 5480 6300 2446 -209 540 C
ATOM 2117 CD1 PHE A 342 57.227 -0.383 45.349 1.00 56.69 C
ANISOU 2117 CD1 PHE A 342 7926 6371 7242 2369 -394 476 C
ATOM 2118 CD2 PHE A 342 56.244 -2.245 44.245 1.00 51.06 C
ANISOU 2118 CD2 PHE A 342 6944 5880 6575 2384 -266 586 C
ATOM 2119 CE1 PHE A 342 58.202 -1.199 45.872 1.00 56.60 C
ANISOU 2119 CE1 PHE A 342 8000 6352 7153 2324 -658 467 C
ATOM 2120 CE2 PHE A 342 57.218 -3.064 44.760 1.00 52.41 C
ANISOU 2120 CE2 PHE A 342 7232 6023 6657 2365 -504 592 C
ATOM 2121 CZ PHE A 342 58.198 -2.544 45.574 1.00 55.63 C
ANISOU 2121 CZ PHE A 342 7812 6318 7005 2361 -719 533 C
ATOM 2122 N SER A 343 55.298 -0.875 40.829 1.00 56.07 N
ANISOU 2122 N SER A 343 6943 6705 7655 2137 -57 567 N
ATOM 2123 CA SER A 343 55.773 -1.882 39.875 1.00 57.60 C
ANISOU 2123 CA SER A 343 6999 6968 7918 1999 -156 582 C
ATOM 2124 C SER A 343 56.625 -1.242 38.775 1.00 55.99 C
ANISOU 2124 C SER A 343 6700 6726 7848 1919 -221 566 C
ATOM 2125 O SER A 343 57.694 -1.771 38.403 1.00 64.46 O
ANISOU 2125 O SER A 343 7706 7795 8990 1850 -333 570 O
ATOM 2126 CB SER A 343 54.590 -2.642 39.283 1.00 64.71 C
ANISOU 2126 CB SER A 343 7827 7966 8795 1963 -72 573 C
ATOM 2127 OG SER A 343 53.531 -1.747 38.983 1.00 81.08 O
ANISOU 2127 OG SER A 343 9867 10049 10893 2013 38 535 O
ATOM 2128 N HIS A 344 56.182 -0.083 38.266 1.00 36.88 N
ANISOU 2128 N HIS A 344 4290 4266 5456 1954 -142 546 N
ATOM 2129 CA HIS A 344 57.032 0.684 37.368 1.00 34.48 C
ANISOU 2129 CA HIS A 344 3961 3899 5239 1931 -170 543 C
ATOM 2130 C HIS A 344 58.377 0.937 38.026 1.00 44.39 C
ANISOU 2130 C HIS A 344 5227 5085 6556 1968 -250 558 C
ATOM 2131 O HIS A 344 59.431 0.754 37.409 1.00 63.36 O
ANISOU 2131 O HIS A 344 7540 7486 9047 1930 -318 549 O
ATOM 2132 CB HIS A 344 56.383 2.017 36.965 1.00 45.30 C
ANISOU 2132 CB HIS A 344 5407 5202 6603 2003 -67 537 C
ATOM 2133 CG HIS A 344 55.021 1.891 36.354 1.00 53.99 C
ANISOU 2133 CG HIS A 344 6474 6368 7671 2001 -22 516 C
ATOM 2134 ND1 HIS A 344 54.102 2.918 36.373 1.00 55.99 N
ANISOU 2134 ND1 HIS A 344 6787 6578 7907 2100 58 499 N
ATOM 2135 CD2 HIS A 344 54.445 0.886 35.651 1.00 58.49 C
ANISOU 2135 CD2 HIS A 344 6956 7031 8237 1926 -56 502 C
ATOM 2136 CE1 HIS A 344 53.009 2.545 35.731 1.00 58.93 C
ANISOU 2136 CE1 HIS A 344 7080 7026 8286 2092 54 474 C
ATOM 2137 NE2 HIS A 344 53.192 1.315 35.282 1.00 60.69 N
ANISOU 2137 NE2 HIS A 344 7220 7329 8512 1988 -8 480 N
ATOM 2138 N TRP A 345 58.364 1.401 39.275 1.00 44.40 N
ANISOU 2138 N TRP A 345 5347 5021 6501 2069 -242 567 N
ATOM 2139 CA TRP A 345 59.633 1.703 39.918 1.00 49.12 C
ANISOU 2139 CA TRP A 345 5969 5545 7150 2131 -355 571 C
ATOM 2140 C TRP A 345 60.516 0.471 40.034 1.00 45.46 C
ANISOU 2140 C TRP A 345 5369 5170 6733 2071 -519 586 C
ATOM 2141 O TRP A 345 61.741 0.583 39.930 1.00 44.24 O
ANISOU 2141 O TRP A 345 5102 5015 6691 2090 -623 578 O
ATOM 2142 CB TRP A 345 59.399 2.292 41.304 1.00 66.54 C
ANISOU 2142 CB TRP A 345 8428 7643 9212 2266 -369 538 C
ATOM 2143 CG TRP A 345 60.675 2.467 42.042 1.00 63.45 C
ANISOU 2143 CG TRP A 345 8085 7191 8833 2207 -582 457 C
ATOM 2144 CD1 TRP A 345 61.540 3.521 41.967 1.00 64.73 C
ANISOU 2144 CD1 TRP A 345 8251 7255 9088 2074 -603 380 C
ATOM 2145 CD2 TRP A 345 61.253 1.531 42.952 1.00 59.85 C
ANISOU 2145 CD2 TRP A 345 7660 6782 8298 2176 -818 416 C
ATOM 2146 NE1 TRP A 345 62.619 3.304 42.793 1.00 59.85 N
ANISOU 2146 NE1 TRP A 345 7621 6643 8476 1957 -853 278 N
ATOM 2147 CE2 TRP A 345 62.469 2.086 43.405 1.00 58.15 C
ANISOU 2147 CE2 TRP A 345 7432 6513 8149 2038 -1005 303 C
ATOM 2148 CE3 TRP A 345 60.856 0.277 43.434 1.00 59.57 C
ANISOU 2148 CE3 TRP A 345 7687 6817 8131 2251 -893 457 C
ATOM 2149 CZ2 TRP A 345 63.290 1.433 44.321 1.00 62.10 C
ANISOU 2149 CZ2 TRP A 345 7965 7036 8593 2006 -1302 227 C
ATOM 2150 CZ3 TRP A 345 61.670 -0.373 44.337 1.00 56.80 C
ANISOU 2150 CZ3 TRP A 345 7421 6463 7698 2220 -1165 397 C
ATOM 2151 CH2 TRP A 345 62.875 0.207 44.776 1.00 64.39 C
ANISOU 2151 CH2 TRP A 345 8354 7379 8733 2114 -1386 282 C
ATOM 2152 N LEU A 346 59.922 -0.706 40.258 1.00 57.78 N
ANISOU 2152 N LEU A 346 6940 6812 8203 2016 -533 604 N
ATOM 2153 CA LEU A 346 60.712 -1.935 40.347 1.00 65.80 C
ANISOU 2153 CA LEU A 346 7867 7894 9240 1960 -664 634 C
ATOM 2154 C LEU A 346 61.418 -2.288 39.050 1.00 67.28 C
ANISOU 2154 C LEU A 346 7849 8100 9614 1849 -672 627 C
ATOM 2155 O LEU A 346 62.559 -2.786 39.076 1.00 71.77 O
ANISOU 2155 O LEU A 346 8303 8738 10229 1836 -723 678 O
ATOM 2156 CB LEU A 346 59.844 -3.128 40.744 1.00 60.97 C
ANISOU 2156 CB LEU A 346 7360 7331 8477 1940 -647 648 C
ATOM 2157 CG LEU A 346 59.744 -3.445 42.220 1.00 41.51 C
ANISOU 2157 CG LEU A 346 5140 4837 5794 2059 -743 637 C
ATOM 2158 CD1 LEU A 346 59.105 -4.804 42.385 1.00 39.32 C
ANISOU 2158 CD1 LEU A 346 4952 4602 5386 2041 -716 665 C
ATOM 2159 CD2 LEU A 346 61.145 -3.429 42.776 1.00 33.97 C
ANISOU 2159 CD2 LEU A 346 4188 3868 4850 2094 -981 600 C
ATOM 2160 N VAL A 347 60.791 -2.002 37.909 1.00 61.41 N
ANISOU 2160 N VAL A 347 7113 7351 8867 1804 -590 549 N
ATOM 2161 CA VAL A 347 61.483 -2.290 36.653 1.00 51.73 C
ANISOU 2161 CA VAL A 347 5815 6169 7669 1752 -598 470 C
ATOM 2162 C VAL A 347 62.804 -1.528 36.590 1.00 55.38 C
ANISOU 2162 C VAL A 347 6202 6654 8188 1850 -631 419 C
ATOM 2163 O VAL A 347 63.866 -2.111 36.334 1.00 39.35 O
ANISOU 2163 O VAL A 347 4094 4760 6096 1902 -667 369 O
ATOM 2164 CB VAL A 347 60.587 -1.948 35.448 1.00 58.91 C
ANISOU 2164 CB VAL A 347 6774 7090 8521 1736 -473 466 C
ATOM 2165 CG1 VAL A 347 61.398 -1.963 34.160 1.00 60.77 C
ANISOU 2165 CG1 VAL A 347 6960 7356 8774 1737 -432 441 C
ATOM 2166 CG2 VAL A 347 59.408 -2.902 35.356 1.00 69.64 C
ANISOU 2166 CG2 VAL A 347 8175 8496 9788 1669 -441 490 C
ATOM 2167 N TYR A 348 62.765 -0.224 36.879 1.00 79.39 N
ANISOU 2167 N TYR A 348 9274 9619 11270 1947 -563 459 N
ATOM 2168 CA TYR A 348 63.974 0.601 36.870 1.00 74.61 C
ANISOU 2168 CA TYR A 348 8528 9005 10813 2025 -507 506 C
ATOM 2169 C TYR A 348 64.937 0.186 37.989 1.00 72.71 C
ANISOU 2169 C TYR A 348 8142 8800 10684 2010 -719 483 C
ATOM 2170 O TYR A 348 66.177 0.267 37.843 1.00 81.09 O
ANISOU 2170 O TYR A 348 8954 9857 11998 1942 -830 384 O
ATOM 2171 CB TYR A 348 63.543 2.062 36.989 1.00 67.04 C
ANISOU 2171 CB TYR A 348 7674 7831 9966 2045 -381 553 C
ATOM 2172 CG TYR A 348 62.619 2.483 35.847 1.00 70.86 C
ANISOU 2172 CG TYR A 348 8308 8280 10337 2022 -203 580 C
ATOM 2173 CD1 TYR A 348 63.055 2.484 34.525 1.00 75.23 C
ANISOU 2173 CD1 TYR A 348 8797 8831 10955 1975 -78 608 C
ATOM 2174 CD2 TYR A 348 61.290 2.838 36.096 1.00 72.52 C
ANISOU 2174 CD2 TYR A 348 8695 8455 10403 2033 -170 580 C
ATOM 2175 CE1 TYR A 348 62.198 2.847 33.486 1.00 74.09 C
ANISOU 2175 CE1 TYR A 348 8809 8644 10699 1963 36 641 C
ATOM 2176 CE2 TYR A 348 60.427 3.199 35.064 1.00 73.96 C
ANISOU 2176 CE2 TYR A 348 8968 8623 10509 2008 -65 598 C
ATOM 2177 CZ TYR A 348 60.884 3.203 33.761 1.00 69.51 C
ANISOU 2177 CZ TYR A 348 8382 8050 9980 1981 16 630 C
ATOM 2178 OH TYR A 348 60.030 3.568 32.736 1.00 62.63 O
ANISOU 2178 OH TYR A 348 7623 7151 9022 1979 85 655 O
ATOM 2179 N ALA A 349 64.382 -0.281 39.109 1.00 63.61 N
ANISOU 2179 N ALA A 349 7140 7657 9373 2041 -825 513 N
ATOM 2180 CA ALA A 349 65.229 -0.704 40.208 1.00 57.44 C
ANISOU 2180 CA ALA A 349 6328 6885 8612 2034 -1133 402 C
ATOM 2181 C ALA A 349 66.081 -1.872 39.761 1.00 60.03 C
ANISOU 2181 C ALA A 349 6479 7378 8953 1995 -1156 419 C
ATOM 2182 O ALA A 349 67.190 -2.060 40.266 1.00 77.24 O
ANISOU 2182 O ALA A 349 8522 9585 11240 1981 -1402 295 O
ATOM 2183 CB ALA A 349 64.383 -1.080 41.429 1.00 36.70 C
ANISOU 2183 CB ALA A 349 3981 4212 5751 2084 -1223 422 C
ATOM 2184 N ASN A 350 65.575 -2.664 38.809 1.00 61.04 N
ANISOU 2184 N ASN A 350 6615 7609 8969 1985 -911 566 N
ATOM 2185 CA ASN A 350 66.379 -3.760 38.259 1.00 64.02 C
ANISOU 2185 CA ASN A 350 6861 8119 9343 1975 -904 586 C
ATOM 2186 C ASN A 350 67.651 -3.261 37.575 1.00 73.84 C
ANISOU 2186 C ASN A 350 7850 9395 10812 1957 -948 440 C
ATOM 2187 O ASN A 350 68.732 -3.863 37.728 1.00 63.24 O
ANISOU 2187 O ASN A 350 6339 8123 9566 1950 -1086 371 O
ATOM 2188 CB ASN A 350 65.532 -4.550 37.259 1.00 45.45 C
ANISOU 2188 CB ASN A 350 4628 5817 6822 1892 -638 710 C
ATOM 2189 CG ASN A 350 66.263 -5.743 36.687 1.00 54.03 C
ANISOU 2189 CG ASN A 350 5642 7002 7885 1882 -619 732 C
ATOM 2190 OD1 ASN A 350 66.460 -6.763 37.358 1.00 70.70 O
ANISOU 2190 OD1 ASN A 350 7742 9061 10061 1846 -748 787 O
ATOM 2191 ND2 ASN A 350 66.662 -5.624 35.415 1.00 52.22 N
ANISOU 2191 ND2 ASN A 350 5435 6882 7523 1976 -593 504 N
ATOM 2192 N SER A 351 67.542 -2.171 36.804 1.00 88.68 N
ANISOU 2192 N SER A 351 9675 11187 12833 1927 -821 394 N
ATOM 2193 CA SER A 351 68.725 -1.607 36.163 1.00 98.20 C
ANISOU 2193 CA SER A 351 10572 12357 14383 1840 -806 276 C
ATOM 2194 C SER A 351 69.716 -1.102 37.200 1.00 99.02 C
ANISOU 2194 C SER A 351 10449 12424 14749 1780 -1080 104 C
ATOM 2195 O SER A 351 70.935 -1.253 37.037 1.00 99.98 O
ANISOU 2195 O SER A 351 10271 12623 15092 1712 -1152 -30 O
ATOM 2196 CB SER A 351 68.329 -0.465 35.219 1.00103.94 C
ANISOU 2196 CB SER A 351 11306 12916 15270 1791 -567 308 C
ATOM 2197 OG SER A 351 67.518 -0.908 34.142 1.00105.32 O
ANISOU 2197 OG SER A 351 11689 13125 15202 1830 -382 402 O
ATOM 2198 N ALA A 352 69.209 -0.527 38.295 1.00 97.08 N
ANISOU 2198 N ALA A 352 10355 12073 14460 1808 -1258 78 N
ATOM 2199 CA ALA A 352 70.132 -0.180 39.377 1.00 86.25 C
ANISOU 2199 CA ALA A 352 8839 10698 13235 1748 -1587 -115 C
ATOM 2200 C ALA A 352 70.724 -1.415 40.052 1.00 74.96 C
ANISOU 2200 C ALA A 352 7410 9413 11659 1815 -1822 -143 C
ATOM 2201 O ALA A 352 71.874 -1.381 40.504 1.00 77.28 O
ANISOU 2201 O ALA A 352 7467 9768 12128 1762 -2063 -321 O
ATOM 2202 CB ALA A 352 69.438 0.705 40.413 1.00 89.05 C
ANISOU 2202 CB ALA A 352 9544 10921 13370 1675 -1628 -121 C
ATOM 2203 N ALA A 353 69.967 -2.511 40.112 1.00 66.30 N
ANISOU 2203 N ALA A 353 6580 8367 10245 1904 -1726 29 N
ATOM 2204 CA ALA A 353 70.350 -3.671 40.910 1.00 62.66 C
ANISOU 2204 CA ALA A 353 6211 7973 9623 1967 -1926 26 C
ATOM 2205 C ALA A 353 71.449 -4.496 40.252 1.00 79.43 C
ANISOU 2205 C ALA A 353 8089 10231 11860 1973 -1902 -4 C
ATOM 2206 O ALA A 353 72.301 -5.064 40.946 1.00 87.75 O
ANISOU 2206 O ALA A 353 9087 11328 12928 2017 -2152 -101 O
ATOM 2207 CB ALA A 353 69.120 -4.542 41.178 1.00 49.91 C
ANISOU 2207 CB ALA A 353 4933 6330 7701 2022 -1799 208 C
ATOM 2208 N ASN A 354 71.429 -4.599 38.923 1.00 86.64 N
ANISOU 2208 N ASN A 354 8883 11201 12834 1948 -1610 76 N
ATOM 2209 CA ASN A 354 72.372 -5.497 38.251 1.00 85.68 C
ANISOU 2209 CA ASN A 354 8574 11197 12782 1980 -1562 68 C
ATOM 2210 C ASN A 354 73.839 -5.172 38.539 1.00 84.97 C
ANISOU 2210 C ASN A 354 8137 11165 12982 1941 -1776 -157 C
ATOM 2211 O ASN A 354 74.602 -6.100 38.870 1.00 88.23 O
ANISOU 2211 O ASN A 354 8489 11651 13384 2023 -1929 -190 O
ATOM 2212 CB ASN A 354 72.088 -5.521 36.745 1.00 76.92 C
ANISOU 2212 CB ASN A 354 7432 10124 11671 1965 -1227 162 C
ATOM 2213 CG ASN A 354 70.774 -6.207 36.414 1.00 60.81 C
ANISOU 2213 CG ASN A 354 5711 8079 9317 2021 -1039 375 C
ATOM 2214 OD1 ASN A 354 70.342 -7.129 37.118 1.00 44.76 O
ANISOU 2214 OD1 ASN A 354 3852 6027 7129 2055 -1111 484 O
ATOM 2215 ND2 ASN A 354 70.136 -5.770 35.333 1.00 68.58 N
ANISOU 2215 ND2 ASN A 354 6768 9059 10231 2015 -813 402 N
ATOM 2216 N PRO A 355 74.309 -3.926 38.404 1.00 78.64 N
ANISOU 2216 N PRO A 355 7080 10331 12466 1808 -1786 -325 N
ATOM 2217 CA PRO A 355 75.723 -3.647 38.719 1.00 78.68 C
ANISOU 2217 CA PRO A 355 6718 10415 12763 1735 -1984 -563 C
ATOM 2218 C PRO A 355 76.107 -4.002 40.145 1.00 89.94 C
ANISOU 2218 C PRO A 355 8229 11853 14092 1815 -2387 -655 C
ATOM 2219 O PRO A 355 77.242 -4.441 40.383 1.00102.41 O
ANISOU 2219 O PRO A 355 9584 13531 15796 1847 -2560 -788 O
ATOM 2220 CB PRO A 355 75.847 -2.138 38.462 1.00 82.93 C
ANISOU 2220 CB PRO A 355 7026 10876 13609 1530 -1898 -715 C
ATOM 2221 CG PRO A 355 74.735 -1.824 37.513 1.00 80.33 C
ANISOU 2221 CG PRO A 355 6883 10441 13199 1528 -1563 -535 C
ATOM 2222 CD PRO A 355 73.603 -2.718 37.945 1.00 81.08 C
ANISOU 2222 CD PRO A 355 7404 10521 12880 1706 -1605 -314 C
ATOM 2223 N ILE A 356 75.197 -3.828 41.107 1.00 88.64 N
ANISOU 2223 N ILE A 356 8398 11578 13702 1858 -2542 -594 N
ATOM 2224 CA ILE A 356 75.485 -4.244 42.475 1.00 90.52 C
ANISOU 2224 CA ILE A 356 8801 11797 13797 1948 -2921 -671 C
ATOM 2225 C ILE A 356 75.674 -5.751 42.532 1.00 98.88 C
ANISOU 2225 C ILE A 356 9987 12906 14677 2109 -2939 -568 C
ATOM 2226 O ILE A 356 76.548 -6.263 43.255 1.00 97.55 O
ANISOU 2226 O ILE A 356 9769 12773 14524 2195 -3227 -686 O
ATOM 2227 CB ILE A 356 74.340 -3.788 43.400 1.00 74.27 C
ANISOU 2227 CB ILE A 356 7132 9587 11499 1964 -3028 -608 C
ATOM 2228 CG1 ILE A 356 74.275 -2.259 43.449 1.00 57.06 C
ANISOU 2228 CG1 ILE A 356 4816 7338 9527 1813 -3074 -736 C
ATOM 2229 CG2 ILE A 356 74.466 -4.440 44.782 1.00 78.33 C
ANISOU 2229 CG2 ILE A 356 7935 10048 11780 2081 -3377 -651 C
ATOM 2230 CD1 ILE A 356 73.061 -1.723 44.160 1.00 55.11 C
ANISOU 2230 CD1 ILE A 356 4955 6930 9055 1846 -3130 -654 C
ATOM 2231 N ILE A 357 74.923 -6.479 41.701 1.00102.77 N
ANISOU 2231 N ILE A 357 10622 13402 15025 2148 -2633 -359 N
ATOM 2232 CA ILE A 357 75.054 -7.926 41.660 1.00100.37 C
ANISOU 2232 CA ILE A 357 10434 13125 14575 2280 -2628 -257 C
ATOM 2233 C ILE A 357 76.414 -8.312 41.104 1.00 92.43 C
ANISOU 2233 C ILE A 357 9067 12246 13807 2324 -2663 -365 C
ATOM 2234 O ILE A 357 77.086 -9.204 41.640 1.00 94.27 O
ANISOU 2234 O ILE A 357 9309 12498 14013 2456 -2881 -417 O
ATOM 2235 CB ILE A 357 73.916 -8.524 40.810 1.00104.31 C
ANISOU 2235 CB ILE A 357 11138 13599 14897 2271 -2282 -18 C
ATOM 2236 CG1 ILE A 357 72.551 -8.266 41.456 1.00108.02 C
ANISOU 2236 CG1 ILE A 357 11955 13949 15137 2238 -2252 77 C
ATOM 2237 CG2 ILE A 357 74.132 -10.018 40.572 1.00107.30 C
ANISOU 2237 CG2 ILE A 357 11588 13995 15186 2381 -2252 79 C
ATOM 2238 CD1 ILE A 357 72.535 -8.407 42.955 1.00115.71 C
ANISOU 2238 CD1 ILE A 357 13175 14831 15958 2303 -2583 -16 C
ATOM 2239 N TYR A 358 76.857 -7.640 40.031 1.00 93.26 N
ANISOU 2239 N TYR A 358 8852 12429 14155 2220 -2451 -417 N
ATOM 2240 CA TYR A 358 78.182 -7.964 39.508 1.00 99.06 C
ANISOU 2240 CA TYR A 358 9217 13286 15137 2253 -2467 -544 C
ATOM 2241 C TYR A 358 79.270 -7.604 40.517 1.00111.01 C
ANISOU 2241 C TYR A 358 10507 14843 16828 2259 -2840 -791 C
ATOM 2242 O TYR A 358 80.291 -8.298 40.614 1.00122.30 O
ANISOU 2242 O TYR A 358 11743 16357 18366 2373 -2990 -885 O
ATOM 2243 CB TYR A 358 78.434 -7.251 38.172 1.00 90.39 C
ANISOU 2243 CB TYR A 358 7834 12242 14269 2115 -2143 -578 C
ATOM 2244 CG TYR A 358 77.320 -7.337 37.138 1.00 88.64 C
ANISOU 2244 CG TYR A 358 7837 11968 13874 2096 -1791 -362 C
ATOM 2245 CD1 TYR A 358 76.449 -8.421 37.098 1.00 85.20 C
ANISOU 2245 CD1 TYR A 358 7740 11494 13137 2213 -1719 -138 C
ATOM 2246 CD2 TYR A 358 77.155 -6.334 36.186 1.00 99.00 C
ANISOU 2246 CD2 TYR A 358 9020 13256 15340 1947 -1528 -398 C
ATOM 2247 CE1 TYR A 358 75.436 -8.496 36.141 1.00 89.62 C
ANISOU 2247 CE1 TYR A 358 8494 12024 13534 2193 -1416 42 C
ATOM 2248 CE2 TYR A 358 76.149 -6.399 35.231 1.00 99.18 C
ANISOU 2248 CE2 TYR A 358 9265 13230 15189 1951 -1239 -222 C
ATOM 2249 CZ TYR A 358 75.293 -7.478 35.211 1.00 94.19 C
ANISOU 2249 CZ TYR A 358 8961 12594 14233 2082 -1196 -7 C
ATOM 2250 OH TYR A 358 74.300 -7.526 34.254 1.00 89.68 O
ANISOU 2250 OH TYR A 358 8605 11995 13473 2087 -936 133 O
ATOM 2251 N ASN A 359 79.081 -6.509 41.262 1.00105.37 N
ANISOU 2251 N ASN A 359 9809 14073 16154 2140 -3003 -907 N
ATOM 2252 CA ASN A 359 80.095 -6.093 42.227 1.00111.63 C
ANISOU 2252 CA ASN A 359 10396 14909 17110 2124 -3373 -1152 C
ATOM 2253 C ASN A 359 80.240 -7.107 43.358 1.00108.07 C
ANISOU 2253 C ASN A 359 10206 14419 16437 2336 -3717 -1145 C
ATOM 2254 O ASN A 359 81.355 -7.367 43.829 1.00104.82 O
ANISOU 2254 O ASN A 359 9578 14085 16166 2416 -3992 -1319 O
ATOM 2255 CB ASN A 359 79.789 -4.700 42.784 1.00120.46 C
ANISOU 2255 CB ASN A 359 11516 15955 18299 1939 -3478 -1270 C
ATOM 2256 CG ASN A 359 80.804 -4.260 43.845 1.00131.10 C
ANISOU 2256 CG ASN A 359 12681 17345 19787 1903 -3887 -1527 C
ATOM 2257 OD1 ASN A 359 81.833 -3.657 43.524 1.00131.28 O
ANISOU 2257 OD1 ASN A 359 12263 17477 20139 1753 -3886 -1734 O
ATOM 2258 ND2 ASN A 359 80.518 -4.564 45.108 1.00135.08 N
ANISOU 2258 ND2 ASN A 359 13535 17754 20035 2029 -4226 -1520 N
ATOM 2259 N PHE A 360 79.130 -7.735 43.767 1.00108.36 N
ANISOU 2259 N PHE A 360 10708 14331 16134 2430 -3692 -953 N
ATOM 2260 CA PHE A 360 79.158 -8.642 44.913 1.00113.15 C
ANISOU 2260 CA PHE A 360 11630 14855 16505 2613 -4006 -957 C
ATOM 2261 C PHE A 360 79.295 -10.115 44.552 1.00114.90 C
ANISOU 2261 C PHE A 360 11939 15091 16628 2790 -3936 -843 C
ATOM 2262 O PHE A 360 79.530 -10.930 45.453 1.00120.75 O
ANISOU 2262 O PHE A 360 12902 15763 17214 2960 -4216 -881 O
ATOM 2263 CB PHE A 360 77.840 -8.527 45.705 1.00114.54 C
ANISOU 2263 CB PHE A 360 12306 14861 16353 2601 -4022 -837 C
ATOM 2264 CG PHE A 360 77.680 -7.268 46.514 1.00111.28 C
ANISOU 2264 CG PHE A 360 11951 14380 15951 2486 -4221 -960 C
ATOM 2265 CD1 PHE A 360 78.757 -6.463 46.839 1.00118.12 C
ANISOU 2265 CD1 PHE A 360 12492 15319 17070 2415 -4475 -1191 C
ATOM 2266 CD2 PHE A 360 76.415 -6.889 46.941 1.00 97.92 C
ANISOU 2266 CD2 PHE A 360 10644 12546 14015 2440 -4146 -847 C
ATOM 2267 CE1 PHE A 360 78.568 -5.306 47.586 1.00116.04 C
ANISOU 2267 CE1 PHE A 360 12310 14978 16801 2290 -4665 -1301 C
ATOM 2268 CE2 PHE A 360 76.222 -5.742 47.680 1.00 94.79 C
ANISOU 2268 CE2 PHE A 360 10341 12068 13609 2342 -4333 -950 C
ATOM 2269 CZ PHE A 360 77.296 -4.949 48.005 1.00103.47 C
ANISOU 2269 CZ PHE A 360 11137 13230 14948 2261 -4599 -1175 C
ATOM 2270 N LEU A 361 79.180 -10.481 43.277 1.00109.35 N
ANISOU 2270 N LEU A 361 11087 14458 16005 2763 -3587 -713 N
ATOM 2271 CA LEU A 361 79.322 -11.874 42.867 1.00 95.35 C
ANISOU 2271 CA LEU A 361 9389 12687 14151 2922 -3516 -605 C
ATOM 2272 C LEU A 361 80.435 -12.122 41.858 1.00 87.91 C
ANISOU 2272 C LEU A 361 8014 11892 13495 2965 -3411 -671 C
ATOM 2273 O LEU A 361 80.638 -13.274 41.454 1.00 87.65 O
ANISOU 2273 O LEU A 361 8019 11860 13423 3110 -3356 -591 O
ATOM 2274 CB LEU A 361 77.985 -12.397 42.320 1.00 82.09 C
ANISOU 2274 CB LEU A 361 8035 10920 12236 2875 -3195 -356 C
ATOM 2275 CG LEU A 361 76.936 -12.702 43.399 1.00 73.89 C
ANISOU 2275 CG LEU A 361 7475 9722 10877 2894 -3312 -290 C
ATOM 2276 CD1 LEU A 361 75.713 -13.385 42.812 1.00 69.66 C
ANISOU 2276 CD1 LEU A 361 7202 9115 10149 2843 -3000 -69 C
ATOM 2277 CD2 LEU A 361 77.553 -13.553 44.499 1.00 80.50 C
ANISOU 2277 CD2 LEU A 361 8488 10492 11606 3089 -3685 -403 C
ATOM 2278 N SER A 362 81.143 -11.083 41.421 1.00 89.89 N
ANISOU 2278 N SER A 362 7859 12255 14038 2837 -3365 -824 N
ATOM 2279 CA SER A 362 82.243 -11.227 40.476 1.00111.45 C
ANISOU 2279 CA SER A 362 10154 15129 17066 2860 -3247 -919 C
ATOM 2280 C SER A 362 83.457 -10.464 40.987 1.00135.14 C
ANISOU 2280 C SER A 362 12746 18236 20366 2814 -3513 -1209 C
ATOM 2281 O SER A 362 83.398 -9.242 41.158 1.00128.15 O
ANISOU 2281 O SER A 362 11739 17356 19597 2615 -3515 -1319 O
ATOM 2282 CB SER A 362 81.819 -10.714 39.094 1.00108.91 C
ANISOU 2282 CB SER A 362 9721 14835 16823 2699 -2805 -813 C
ATOM 2283 OG SER A 362 82.933 -10.468 38.255 1.00120.89 O
ANISOU 2283 OG SER A 362 10778 16486 18671 2658 -2681 -966 O
ATOM 2284 N GLY A 363 84.547 -11.190 41.260 1.00154.45 N
ANISOU 2284 N GLY A 363 14980 20761 22944 2998 -3748 -1343 N
ATOM 2285 CA GLY A 363 85.732 -10.536 41.790 1.00156.68 C
ANISOU 2285 CA GLY A 363 14854 21157 23520 2961 -4027 -1633 C
ATOM 2286 C GLY A 363 86.384 -9.603 40.785 1.00151.55 C
ANISOU 2286 C GLY A 363 13712 20639 23233 2738 -3750 -1775 C
ATOM 2287 O GLY A 363 86.873 -8.528 41.150 1.00158.26 O
ANISOU 2287 O GLY A 363 14296 21542 24294 2553 -3863 -1985 O
ATOM 2288 N LYS A 364 86.375 -9.978 39.501 1.00139.01 N
ANISOU 2288 N LYS A 364 12016 19088 21713 2732 -3368 -1668 N
ATOM 2289 CA LYS A 364 86.977 -9.112 38.491 1.00127.21 C
ANISOU 2289 CA LYS A 364 10088 17693 20552 2506 -3062 -1811 C
ATOM 2290 C LYS A 364 86.191 -7.811 38.374 1.00122.32 C
ANISOU 2290 C LYS A 364 9568 16993 19915 2220 -2881 -1795 C
ATOM 2291 O LYS A 364 86.774 -6.718 38.354 1.00126.78 O
ANISOU 2291 O LYS A 364 9798 17612 20760 1983 -2850 -2014 O
ATOM 2292 CB LYS A 364 87.095 -9.832 37.141 1.00117.27 C
ANISOU 2292 CB LYS A 364 8749 16470 19338 2577 -2690 -1696 C
ATOM 2293 CG LYS A 364 87.805 -11.194 37.196 1.00115.68 C
ANISOU 2293 CG LYS A 364 8474 16330 19149 2882 -2850 -1694 C
ATOM 2294 CD LYS A 364 87.861 -11.862 35.817 1.00108.63 C
ANISOU 2294 CD LYS A 364 7526 15458 18289 2946 -2461 -1573 C
ATOM 2295 CE LYS A 364 88.508 -13.241 35.878 1.00106.41 C
ANISOU 2295 CE LYS A 364 7195 15217 18017 3264 -2617 -1562 C
ATOM 2296 NZ LYS A 364 88.497 -13.942 34.562 1.00 98.38 N
ANISOU 2296 NZ LYS A 364 6170 14204 17004 3343 -2243 -1430 N
ATOM 2297 N PHE A 365 84.860 -7.914 38.260 1.00117.40 N
ANISOU 2297 N PHE A 365 9395 16235 18975 2231 -2743 -1543 N
ATOM 2298 CA PHE A 365 84.039 -6.708 38.219 1.00121.56 C
ANISOU 2298 CA PHE A 365 10042 16670 19477 1996 -2601 -1524 C
ATOM 2299 C PHE A 365 84.208 -5.862 39.470 1.00132.43 C
ANISOU 2299 C PHE A 365 11385 18028 20903 1899 -2950 -1700 C
ATOM 2300 O PHE A 365 84.273 -4.633 39.378 1.00133.07 O
ANISOU 2300 O PHE A 365 11291 18094 21174 1641 -2858 -1838 O
ATOM 2301 CB PHE A 365 82.552 -7.045 38.047 1.00113.73 C
ANISOU 2301 CB PHE A 365 9547 15544 18122 2062 -2452 -1232 C
ATOM 2302 CG PHE A 365 82.106 -7.188 36.622 1.00109.60 C
ANISOU 2302 CG PHE A 365 9061 15005 17576 2023 -2021 -1081 C
ATOM 2303 CD1 PHE A 365 82.083 -6.077 35.793 1.00102.86 C
ANISOU 2303 CD1 PHE A 365 8033 14126 16925 1787 -1726 -1162 C
ATOM 2304 CD2 PHE A 365 81.656 -8.398 36.125 1.00110.68 C
ANISOU 2304 CD2 PHE A 365 9442 15131 17482 2209 -1907 -863 C
ATOM 2305 CE1 PHE A 365 81.655 -6.174 34.486 1.00 96.28 C
ANISOU 2305 CE1 PHE A 365 7272 13255 16054 1757 -1342 -1035 C
ATOM 2306 CE2 PHE A 365 81.225 -8.504 34.813 1.00109.51 C
ANISOU 2306 CE2 PHE A 365 9354 14965 17290 2178 -1533 -735 C
ATOM 2307 CZ PHE A 365 81.225 -7.389 33.994 1.00101.99 C
ANISOU 2307 CZ PHE A 365 8238 13986 16527 1962 -1261 -825 C
ATOM 2308 N ARG A 366 84.266 -6.482 40.652 1.00136.56 N
ANISOU 2308 N ARG A 366 12102 18534 21250 2091 -3348 -1704 N
ATOM 2309 CA ARG A 366 84.411 -5.655 41.844 1.00133.04 C
ANISOU 2309 CA ARG A 366 11661 18060 20828 1999 -3693 -1872 C
ATOM 2310 C ARG A 366 85.742 -4.919 41.843 1.00126.37 C
ANISOU 2310 C ARG A 366 10282 17356 20379 1829 -3782 -2180 C
ATOM 2311 O ARG A 366 85.805 -3.732 42.195 1.00125.87 O
ANISOU 2311 O ARG A 366 10104 17274 20445 1586 -3836 -2332 O
ATOM 2312 CB ARG A 366 84.255 -6.513 43.102 1.00137.78 C
ANISOU 2312 CB ARG A 366 12608 18595 21148 2248 -4100 -1826 C
ATOM 2313 CG ARG A 366 84.576 -5.790 44.403 1.00145.72 C
ANISOU 2313 CG ARG A 366 13630 19574 22165 2190 -4515 -2019 C
ATOM 2314 CD ARG A 366 85.107 -6.718 45.503 1.00159.95 C
ANISOU 2314 CD ARG A 366 15577 21367 23831 2454 -4955 -2081 C
ATOM 2315 NE ARG A 366 86.399 -7.341 45.218 1.00171.84 N
ANISOU 2315 NE ARG A 366 16669 23031 25592 2581 -5054 -2233 N
ATOM 2316 CZ ARG A 366 86.600 -8.656 45.170 1.00172.85 C
ANISOU 2316 CZ ARG A 366 16902 23160 25613 2855 -5118 -2149 C
ATOM 2317 NH1 ARG A 366 85.591 -9.490 45.385 1.00172.43 N
ANISOU 2317 NH1 ARG A 366 17360 22957 25199 3001 -5076 -1916 N
ATOM 2318 NH2 ARG A 366 87.810 -9.138 44.914 1.00173.00 N
ANISOU 2318 NH2 ARG A 366 16512 23326 25893 2975 -5221 -2309 N
ATOM 2319 N GLU A 367 86.818 -5.594 41.435 1.00124.49 N
ANISOU 2319 N GLU A 367 9701 17255 20343 1938 -3786 -2283 N
ATOM 2320 CA GLU A 367 88.106 -4.915 41.381 1.00129.59 C
ANISOU 2320 CA GLU A 367 9803 18050 21387 1761 -3838 -2589 C
ATOM 2321 C GLU A 367 88.096 -3.774 40.369 1.00132.51 C
ANISOU 2321 C GLU A 367 9931 18420 21998 1407 -3404 -2663 C
ATOM 2322 O GLU A 367 88.624 -2.691 40.642 1.00141.89 O
ANISOU 2322 O GLU A 367 10848 19646 23418 1133 -3446 -2892 O
ATOM 2323 CB GLU A 367 89.260 -5.897 41.136 1.00133.29 C
ANISOU 2323 CB GLU A 367 9936 18669 22041 1969 -3926 -2695 C
ATOM 2324 CG GLU A 367 89.532 -6.798 42.365 1.00136.53 C
ANISOU 2324 CG GLU A 367 10520 19077 22280 2282 -4441 -2715 C
ATOM 2325 CD GLU A 367 90.610 -7.855 42.150 1.00136.25 C
ANISOU 2325 CD GLU A 367 10180 19174 22416 2534 -4552 -2812 C
ATOM 2326 OE1 GLU A 367 90.519 -8.932 42.786 1.00127.04 O
ANISOU 2326 OE1 GLU A 367 9288 17954 21027 2843 -4837 -2724 O
ATOM 2327 OE2 GLU A 367 91.558 -7.595 41.378 1.00144.50 O
ANISOU 2327 OE2 GLU A 367 10715 20367 23822 2418 -4357 -2991 O
ATOM 2328 N GLN A 368 87.553 -4.011 39.168 1.00124.90 N
ANISOU 2328 N GLN A 368 9061 17407 20987 1395 -2972 -2485 N
ATOM 2329 CA GLN A 368 87.491 -2.919 38.198 1.00123.22 C
ANISOU 2329 CA GLN A 368 8678 17156 20983 1057 -2539 -2553 C
ATOM 2330 C GLN A 368 86.595 -1.767 38.658 1.00114.41 C
ANISOU 2330 C GLN A 368 7797 15898 19776 838 -2545 -2535 C
ATOM 2331 O GLN A 368 86.942 -0.589 38.468 1.00109.75 O
ANISOU 2331 O GLN A 368 6978 15294 19428 497 -2377 -2723 O
ATOM 2332 CB GLN A 368 86.974 -3.470 36.866 1.00123.79 C
ANISOU 2332 CB GLN A 368 8888 17179 20969 1123 -2107 -2343 C
ATOM 2333 CG GLN A 368 88.026 -3.985 35.890 1.00138.64 C
ANISOU 2333 CG GLN A 368 10398 19182 23098 1141 -1869 -2446 C
ATOM 2334 CD GLN A 368 89.009 -2.924 35.454 1.00154.74 C
ANISOU 2334 CD GLN A 368 11983 21280 25533 791 -1636 -2737 C
ATOM 2335 OE1 GLN A 368 88.624 -1.799 35.134 1.00165.61 O
ANISOU 2335 OE1 GLN A 368 13404 22547 26973 482 -1376 -2776 O
ATOM 2336 NE2 GLN A 368 90.287 -3.278 35.427 1.00157.23 N
ANISOU 2336 NE2 GLN A 368 11860 21759 26120 826 -1710 -2950 N
ATOM 2337 N PHE A 369 85.480 -2.069 39.333 1.00109.71 N
ANISOU 2337 N PHE A 369 7658 15190 18837 1015 -2743 -2329 N
ATOM 2338 CA PHE A 369 84.643 -0.983 39.834 1.00109.00 C
ANISOU 2338 CA PHE A 369 7780 14962 18671 828 -2778 -2326 C
ATOM 2339 C PHE A 369 85.338 -0.172 40.916 1.00116.33 C
ANISOU 2339 C PHE A 369 8526 15933 19742 654 -3122 -2586 C
ATOM 2340 O PHE A 369 85.187 1.052 40.967 1.00123.24 O
ANISOU 2340 O PHE A 369 9356 16732 20738 342 -3025 -2702 O
ATOM 2341 CB PHE A 369 83.299 -1.515 40.343 1.00106.46 C
ANISOU 2341 CB PHE A 369 7986 14513 17950 1061 -2909 -2058 C
ATOM 2342 CG PHE A 369 82.416 -2.101 39.268 1.00106.19 C
ANISOU 2342 CG PHE A 369 8175 14419 17755 1174 -2548 -1796 C
ATOM 2343 CD1 PHE A 369 82.479 -1.632 37.966 1.00104.41 C
ANISOU 2343 CD1 PHE A 369 7769 14176 17724 994 -2103 -1802 C
ATOM 2344 CD2 PHE A 369 81.487 -3.085 39.573 1.00105.32 C
ANISOU 2344 CD2 PHE A 369 8487 14251 17280 1437 -2638 -1547 C
ATOM 2345 CE1 PHE A 369 81.653 -2.156 36.981 1.00 96.28 C
ANISOU 2345 CE1 PHE A 369 6973 13085 16525 1102 -1795 -1563 C
ATOM 2346 CE2 PHE A 369 80.661 -3.613 38.591 1.00101.12 C
ANISOU 2346 CE2 PHE A 369 8167 13672 16583 1520 -2315 -1311 C
ATOM 2347 CZ PHE A 369 80.745 -3.147 37.295 1.00 96.45 C
ANISOU 2347 CZ PHE A 369 7393 13073 16182 1366 -1914 -1318 C
ATOM 2348 N LYS A 370 86.103 -0.829 41.793 1.00120.02 N
ANISOU 2348 N LYS A 370 8905 16507 20190 842 -3527 -2684 N
ATOM 2349 CA LYS A 370 86.895 -0.085 42.770 1.00128.12 C
ANISOU 2349 CA LYS A 370 9725 17589 21364 673 -3865 -2949 C
ATOM 2350 C LYS A 370 88.057 0.677 42.138 1.00134.49 C
ANISOU 2350 C LYS A 370 9991 18521 22588 348 -3643 -3218 C
ATOM 2351 O LYS A 370 88.427 1.748 42.636 1.00142.00 O
ANISOU 2351 O LYS A 370 10804 19471 23678 48 -3744 -3425 O
ATOM 2352 CB LYS A 370 87.305 -0.991 43.932 1.00136.09 C
ANISOU 2352 CB LYS A 370 10844 18651 22212 981 -4378 -2971 C
ATOM 2353 CG LYS A 370 86.103 -1.154 44.873 1.00137.20 C
ANISOU 2353 CG LYS A 370 11571 18616 21944 1141 -4614 -2780 C
ATOM 2354 CD LYS A 370 86.181 -2.250 45.918 1.00141.80 C
ANISOU 2354 CD LYS A 370 12431 19180 22266 1486 -5036 -2723 C
ATOM 2355 CE LYS A 370 84.829 -2.323 46.644 1.00141.92 C
ANISOU 2355 CE LYS A 370 13061 18993 21871 1590 -5137 -2515 C
ATOM 2356 NZ LYS A 370 84.649 -3.508 47.523 1.00144.63 N
ANISOU 2356 NZ LYS A 370 13789 19265 21901 1921 -5438 -2408 N
ATOM 2357 N ALA A 371 88.669 0.149 41.074 1.00134.72 N
ANISOU 2357 N ALA A 371 9725 18652 22811 384 -3338 -3230 N
ATOM 2358 CA ALA A 371 89.715 0.922 40.410 1.00145.75 C
ANISOU 2358 CA ALA A 371 10636 20145 24598 43 -3059 -3487 C
ATOM 2359 C ALA A 371 89.129 2.201 39.820 1.00150.64 C
ANISOU 2359 C ALA A 371 11350 20613 25275 -355 -2651 -3494 C
ATOM 2360 O ALA A 371 89.788 3.249 39.802 1.00147.47 O
ANISOU 2360 O ALA A 371 10685 20230 25117 -736 -2532 -3733 O
ATOM 2361 CB ALA A 371 90.390 0.074 39.332 1.00137.93 C
ANISOU 2361 CB ALA A 371 9364 19267 23778 172 -2780 -3484 C
ATOM 2362 N ALA A 372 87.875 2.127 39.372 1.00152.37 N
ANISOU 2362 N ALA A 372 11965 20669 25259 -276 -2438 -3236 N
ATOM 2363 CA ALA A 372 87.116 3.256 38.836 1.00155.90 C
ANISOU 2363 CA ALA A 372 12585 20932 25716 -601 -2062 -3202 C
ATOM 2364 C ALA A 372 86.519 4.081 39.974 1.00160.76 C
ANISOU 2364 C ALA A 372 13451 21437 26194 -725 -2372 -3238 C
ATOM 2365 O ALA A 372 86.480 5.316 39.923 1.00161.50 O
ANISOU 2365 O ALA A 372 13547 21417 26397 -1123 -2182 -3368 O
ATOM 2366 CB ALA A 372 86.024 2.761 37.890 1.00156.25 C
ANISOU 2366 CB ALA A 372 12938 20855 25577 -426 -1737 -2912 C
ATOM 2367 N PHE A 373 86.103 3.369 41.020 1.00163.24 N
ANISOU 2367 N PHE A 373 14008 21769 26248 -394 -2845 -3130 N
ATOM 2368 CA PHE A 373 85.454 3.905 42.214 1.00157.35 C
ANISOU 2368 CA PHE A 373 13581 20910 25296 -421 -3208 -3131 C
ATOM 2369 C PHE A 373 86.368 4.829 43.014 1.00155.66 C
ANISOU 2369 C PHE A 373 13156 20746 25243 -732 -3445 -3426 C
ATOM 2370 O PHE A 373 85.928 5.885 43.483 1.00156.26 O
ANISOU 2370 O PHE A 373 13431 20675 25265 -1007 -3482 -3494 O
ATOM 2371 CB PHE A 373 84.968 2.738 43.076 1.00157.11 C
ANISOU 2371 CB PHE A 373 13868 20890 24935 27 -3620 -2949 C
ATOM 2372 CG PHE A 373 83.933 3.110 44.087 1.00152.77 C
ANISOU 2372 CG PHE A 373 13778 20176 24093 66 -3899 -2863 C
ATOM 2373 CD1 PHE A 373 82.598 3.160 43.731 1.00139.11 C
ANISOU 2373 CD1 PHE A 373 12391 18287 22177 138 -3704 -2638 C
ATOM 2374 CD2 PHE A 373 84.284 3.362 45.401 1.00162.02 C
ANISOU 2374 CD2 PHE A 373 15056 21345 25158 53 -4366 -3004 C
ATOM 2375 CE1 PHE A 373 81.632 3.489 44.654 1.00137.87 C
ANISOU 2375 CE1 PHE A 373 12665 17971 21749 183 -3958 -2565 C
ATOM 2376 CE2 PHE A 373 83.319 3.689 46.334 1.00159.47 C
ANISOU 2376 CE2 PHE A 373 15209 20849 24533 91 -4614 -2923 C
ATOM 2377 CZ PHE A 373 81.988 3.751 45.958 1.00147.42 C
ANISOU 2377 CZ PHE A 373 14016 19165 22833 156 -4407 -2707 C
ATOM 2378 N SER A 374 87.638 4.474 43.172 1.00150.27 N
ANISOU 2378 N SER A 374 12080 20258 24758 -708 -3606 -3610 N
ATOM 2379 CA SER A 374 88.492 5.284 44.028 1.00146.19 C
ANISOU 2379 CA SER A 374 11375 19800 24371 -979 -3886 -3884 C
ATOM 2380 C SER A 374 88.979 6.565 43.362 1.00151.12 C
ANISOU 2380 C SER A 374 11755 20389 25274 -1510 -3475 -4084 C
ATOM 2381 O SER A 374 89.518 7.430 44.063 1.00156.15 O
ANISOU 2381 O SER A 374 12314 21033 25984 -1809 -3664 -4300 O
ATOM 2382 CB SER A 374 89.709 4.462 44.457 1.00143.32 C
ANISOU 2382 CB SER A 374 10650 19661 24145 -762 -4223 -4028 C
ATOM 2383 OG SER A 374 89.312 3.279 45.124 1.00138.96 O
ANISOU 2383 OG SER A 374 10377 19109 23311 -294 -4590 -3851 O
ATOM 2384 N TRP A 375 88.800 6.729 42.056 1.00153.16 N
ANISOU 2384 N TRP A 375 11941 20589 25665 -1651 -2911 -4018 N
ATOM 2385 CA TRP A 375 89.439 7.842 41.362 1.00166.77 C
ANISOU 2385 CA TRP A 375 13437 22275 27654 -2155 -2475 -4219 C
ATOM 2386 C TRP A 375 88.859 9.167 41.853 1.00176.66 C
ANISOU 2386 C TRP A 375 15024 23305 28792 -2543 -2443 -4274 C
ATOM 2387 O TRP A 375 87.693 9.241 42.247 1.00178.83 O
ANISOU 2387 O TRP A 375 15735 23409 28805 -2429 -2556 -4102 O
ATOM 2388 CB TRP A 375 89.246 7.746 39.851 1.00166.45 C
ANISOU 2388 CB TRP A 375 13364 22164 27713 -2215 -1850 -4110 C
ATOM 2389 CG TRP A 375 90.342 7.030 39.165 1.00180.30 C
ANISOU 2389 CG TRP A 375 14671 24120 29716 -2115 -1713 -4210 C
ATOM 2390 CD1 TRP A 375 91.167 6.089 39.704 1.00189.24 C
ANISOU 2390 CD1 TRP A 375 15493 25481 30930 -1815 -2119 -4293 C
ATOM 2391 CD2 TRP A 375 90.794 7.241 37.823 1.00187.13 C
ANISOU 2391 CD2 TRP A 375 15360 24959 30784 -2334 -1120 -4261 C
ATOM 2392 NE1 TRP A 375 92.083 5.671 38.770 1.00196.05 N
ANISOU 2392 NE1 TRP A 375 15971 26469 32050 -1822 -1821 -4394 N
ATOM 2393 CE2 TRP A 375 91.878 6.366 37.607 1.00194.90 C
ANISOU 2393 CE2 TRP A 375 15903 26172 31979 -2143 -1205 -4378 C
ATOM 2394 CE3 TRP A 375 90.378 8.072 36.779 1.00184.64 C
ANISOU 2394 CE3 TRP A 375 15257 24426 30472 -2667 -516 -4216 C
ATOM 2395 CZ2 TRP A 375 92.553 6.297 36.391 1.00196.47 C
ANISOU 2395 CZ2 TRP A 375 15852 26398 32400 -2278 -711 -4461 C
ATOM 2396 CZ3 TRP A 375 91.052 8.003 35.569 1.00187.04 C
ANISOU 2396 CZ3 TRP A 375 15350 24747 30970 -2799 -21 -4287 C
ATOM 2397 CH2 TRP A 375 92.127 7.121 35.387 1.00192.49 C
ANISOU 2397 CH2 TRP A 375 15583 25676 31878 -2608 -122 -4413 C
TER 2398 TRP A 375
ATOM 2399 N ALA B 46 41.256 -46.681 5.563 1.00109.56 N
ANISOU 2399 N ALA B 46 19261 10413 11954 -2221 103 -1083 N
ATOM 2400 CA ALA B 46 42.635 -46.894 5.990 1.00116.13 C
ANISOU 2400 CA ALA B 46 20307 11120 12696 -1951 480 -965 C
ATOM 2401 C ALA B 46 43.606 -46.739 4.819 1.00131.73 C
ANISOU 2401 C ALA B 46 22704 13045 14301 -1716 511 -1100 C
ATOM 2402 O ALA B 46 44.709 -46.213 4.975 1.00134.54 O
ANISOU 2402 O ALA B 46 23113 13472 14536 -1422 765 -983 O
ATOM 2403 CB ALA B 46 42.780 -48.262 6.623 1.00109.35 C
ANISOU 2403 CB ALA B 46 19594 9911 12044 -2091 662 -965 C
ATOM 2404 N TRP B 47 43.154 -47.160 3.637 1.00140.67 N
ANISOU 2404 N TRP B 47 24127 14066 15254 -1859 246 -1355 N
ATOM 2405 CA TRP B 47 43.979 -47.066 2.436 1.00145.64 C
ANISOU 2405 CA TRP B 47 25204 14640 15492 -1669 278 -1510 C
ATOM 2406 C TRP B 47 44.266 -45.618 2.073 1.00135.88 C
ANISOU 2406 C TRP B 47 23872 13732 14024 -1447 250 -1393 C
ATOM 2407 O TRP B 47 45.377 -45.283 1.642 1.00135.02 O
ANISOU 2407 O TRP B 47 24006 13627 13670 -1191 488 -1380 O
ATOM 2408 CB TRP B 47 43.293 -47.781 1.275 1.00156.70 C
ANISOU 2408 CB TRP B 47 26938 15871 16730 -1897 -47 -1816 C
ATOM 2409 CG TRP B 47 44.031 -47.669 -0.018 1.00171.73 C
ANISOU 2409 CG TRP B 47 29336 17730 18183 -1725 -24 -1993 C
ATOM 2410 CD1 TRP B 47 45.009 -48.494 -0.490 1.00178.09 C
ANISOU 2410 CD1 TRP B 47 30515 18295 18855 -1593 238 -2115 C
ATOM 2411 CD2 TRP B 47 43.827 -46.668 -1.026 1.00181.76 C
ANISOU 2411 CD2 TRP B 47 30726 19237 19098 -1655 -265 -2033 C
ATOM 2412 NE1 TRP B 47 45.436 -48.062 -1.725 1.00185.23 N
ANISOU 2412 NE1 TRP B 47 31624 19352 19404 -1432 208 -2163 N
ATOM 2413 CE2 TRP B 47 44.724 -46.944 -2.077 1.00185.65 C
ANISOU 2413 CE2 TRP B 47 31605 19658 19276 -1480 -101 -2134 C
ATOM 2414 CE3 TRP B 47 42.974 -45.562 -1.139 1.00180.74 C
ANISOU 2414 CE3 TRP B 47 30308 19416 18948 -1695 -595 -1931 C
ATOM 2415 CZ2 TRP B 47 44.793 -46.156 -3.227 1.00183.76 C
ANISOU 2415 CZ2 TRP B 47 31509 19625 18687 -1366 -244 -2127 C
ATOM 2416 CZ3 TRP B 47 43.045 -44.780 -2.281 1.00178.02 C
ANISOU 2416 CZ3 TRP B 47 30246 19216 18179 -1588 -780 -1988 C
ATOM 2417 CH2 TRP B 47 43.948 -45.082 -3.309 1.00178.96 C
ANISOU 2417 CH2 TRP B 47 30765 19250 17981 -1428 -591 -2070 C
ATOM 2418 N VAL B 48 43.285 -44.738 2.269 1.00126.38 N
ANISOU 2418 N VAL B 48 22302 12796 12921 -1541 -21 -1301 N
ATOM 2419 CA VAL B 48 43.491 -43.330 1.963 1.00112.08 C
ANISOU 2419 CA VAL B 48 20393 11274 10917 -1336 -67 -1175 C
ATOM 2420 C VAL B 48 44.572 -42.755 2.860 1.00108.31 C
ANISOU 2420 C VAL B 48 19751 10884 10517 -1073 328 -947 C
ATOM 2421 O VAL B 48 45.403 -41.952 2.416 1.00112.48 O
ANISOU 2421 O VAL B 48 20414 11516 10809 -841 466 -886 O
ATOM 2422 CB VAL B 48 42.168 -42.553 2.101 1.00100.93 C
ANISOU 2422 CB VAL B 48 18577 10107 9666 -1481 -445 -1126 C
ATOM 2423 CG1 VAL B 48 42.379 -41.084 1.770 1.00 86.15 C
ANISOU 2423 CG1 VAL B 48 16629 8503 7602 -1259 -505 -987 C
ATOM 2424 CG2 VAL B 48 41.110 -43.162 1.197 1.00111.33 C
ANISOU 2424 CG2 VAL B 48 20042 11330 10929 -1746 -874 -1370 C
ATOM 2425 N LEU B 49 44.618 -43.193 4.119 1.00103.28 N
ANISOU 2425 N LEU B 49 18848 10191 10202 -1111 522 -822 N
ATOM 2426 CA LEU B 49 45.634 -42.661 5.017 1.00101.40 C
ANISOU 2426 CA LEU B 49 18449 10036 10041 -865 857 -614 C
ATOM 2427 C LEU B 49 47.035 -43.090 4.595 1.00 92.45 C
ANISOU 2427 C LEU B 49 17681 8717 8731 -647 1160 -669 C
ATOM 2428 O LEU B 49 47.951 -42.255 4.524 1.00 87.36 O
ANISOU 2428 O LEU B 49 17029 8194 7968 -405 1348 -575 O
ATOM 2429 CB LEU B 49 45.342 -43.150 6.437 1.00105.79 C
ANISOU 2429 CB LEU B 49 18700 10550 10944 -968 977 -477 C
ATOM 2430 CG LEU B 49 46.148 -42.630 7.622 1.00 96.36 C
ANISOU 2430 CG LEU B 49 17273 9460 9878 -760 1260 -250 C
ATOM 2431 CD1 LEU B 49 45.919 -41.143 7.750 1.00 90.51 C
ANISOU 2431 CD1 LEU B 49 16230 9047 9112 -655 1178 -133 C
ATOM 2432 CD2 LEU B 49 45.766 -43.369 8.905 1.00 93.52 C
ANISOU 2432 CD2 LEU B 49 16724 9003 9805 -908 1356 -140 C
ATOM 2433 N ILE B 50 47.202 -44.363 4.222 1.00 82.28 N
ANISOU 2433 N ILE B 50 16714 7125 7422 -732 1205 -843 N
ATOM 2434 CA ILE B 50 48.514 -44.825 3.784 1.00 77.13 C
ANISOU 2434 CA ILE B 50 16399 6279 6628 -515 1504 -924 C
ATOM 2435 C ILE B 50 48.934 -44.139 2.494 1.00 86.92 C
ANISOU 2435 C ILE B 50 17921 7615 7490 -391 1502 -1032 C
ATOM 2436 O ILE B 50 50.090 -43.721 2.351 1.00 99.12 O
ANISOU 2436 O ILE B 50 19461 9215 8985 -147 1772 -947 O
ATOM 2437 CB ILE B 50 48.521 -46.353 3.617 1.00 83.94 C
ANISOU 2437 CB ILE B 50 17564 6770 7560 -636 1537 -1109 C
ATOM 2438 CG1 ILE B 50 48.164 -47.036 4.932 1.00 94.39 C
ANISOU 2438 CG1 ILE B 50 18642 7975 9246 -758 1571 -968 C
ATOM 2439 CG2 ILE B 50 49.878 -46.813 3.125 1.00 84.81 C
ANISOU 2439 CG2 ILE B 50 17920 6731 7572 -390 1838 -1172 C
ATOM 2440 CD1 ILE B 50 49.235 -46.922 5.981 1.00105.94 C
ANISOU 2440 CD1 ILE B 50 19948 9432 10873 -508 1876 -764 C
ATOM 2441 N ALA B 51 48.007 -44.001 1.536 1.00 86.97 N
ANISOU 2441 N ALA B 51 18086 7678 7280 -565 1171 -1172 N
ATOM 2442 CA ALA B 51 48.371 -43.394 0.257 1.00 91.21 C
ANISOU 2442 CA ALA B 51 18858 8323 7474 -459 1143 -1219 C
ATOM 2443 C ALA B 51 48.694 -41.908 0.398 1.00 92.81 C
ANISOU 2443 C ALA B 51 18815 8813 7637 -286 1199 -999 C
ATOM 2444 O ALA B 51 49.665 -41.417 -0.194 1.00 86.47 O
ANISOU 2444 O ALA B 51 17989 8073 6791 -103 1388 -903 O
ATOM 2445 CB ALA B 51 47.246 -43.607 -0.756 1.00 84.66 C
ANISOU 2445 CB ALA B 51 18265 7482 6420 -686 724 -1416 C
ATOM 2446 N ALA B 52 47.912 -41.178 1.194 1.00 88.98 N
ANISOU 2446 N ALA B 52 18017 8510 7281 -350 1027 -876 N
ATOM 2447 CA ALA B 52 48.208 -39.768 1.399 1.00 81.07 C
ANISOU 2447 CA ALA B 52 16791 7760 6253 -184 1085 -674 C
ATOM 2448 C ALA B 52 49.552 -39.581 2.082 1.00 79.15 C
ANISOU 2448 C ALA B 52 16350 7508 6217 45 1488 -523 C
ATOM 2449 O ALA B 52 50.366 -38.746 1.655 1.00 64.13 O
ANISOU 2449 O ALA B 52 14318 5701 4348 207 1604 -409 O
ATOM 2450 CB ALA B 52 47.100 -39.108 2.220 1.00 77.31 C
ANISOU 2450 CB ALA B 52 15847 7489 6037 -291 816 -534 C
ATOM 2451 N TYR B 53 49.829 -40.401 3.105 1.00 86.64 N
ANISOU 2451 N TYR B 53 17232 8316 7371 49 1674 -523 N
ATOM 2452 CA TYR B 53 51.096 -40.298 3.818 1.00 81.19 C
ANISOU 2452 CA TYR B 53 16300 7613 6937 263 1987 -374 C
ATOM 2453 C TYR B 53 52.279 -40.622 2.908 1.00 80.25 C
ANISOU 2453 C TYR B 53 16295 7380 6818 392 2166 -411 C
ATOM 2454 O TYR B 53 53.280 -39.897 2.898 1.00 78.68 O
ANISOU 2454 O TYR B 53 15875 7267 6751 558 2318 -291 O
ATOM 2455 CB TYR B 53 51.040 -41.241 5.015 1.00 87.83 C
ANISOU 2455 CB TYR B 53 17083 8300 7989 225 2092 -364 C
ATOM 2456 CG TYR B 53 50.673 -40.560 6.321 1.00101.43 C
ANISOU 2456 CG TYR B 53 18356 10220 9962 222 2045 -150 C
ATOM 2457 CD1 TYR B 53 49.393 -40.043 6.504 1.00107.69 C
ANISOU 2457 CD1 TYR B 53 18922 11191 10803 41 1760 -105 C
ATOM 2458 CD2 TYR B 53 51.561 -40.492 7.392 1.00104.53 C
ANISOU 2458 CD2 TYR B 53 18550 10613 10554 395 2272 -9 C
ATOM 2459 CE1 TYR B 53 49.018 -39.438 7.703 1.00102.67 C
ANISOU 2459 CE1 TYR B 53 17886 10733 10390 35 1742 69 C
ATOM 2460 CE2 TYR B 53 51.188 -39.892 8.605 1.00 93.79 C
ANISOU 2460 CE2 TYR B 53 16813 9432 9390 382 2226 170 C
ATOM 2461 CZ TYR B 53 49.914 -39.369 8.746 1.00 89.72 C
ANISOU 2461 CZ TYR B 53 16094 9094 8903 200 1979 203 C
ATOM 2462 OH TYR B 53 49.523 -38.766 9.916 1.00 81.01 O
ANISOU 2462 OH TYR B 53 14630 8168 7982 189 1961 358 O
ATOM 2463 N VAL B 54 52.190 -41.717 2.142 1.00 82.16 N
ANISOU 2463 N VAL B 54 16868 7426 6925 304 2150 -588 N
ATOM 2464 CA VAL B 54 53.302 -42.119 1.277 1.00 83.08 C
ANISOU 2464 CA VAL B 54 17101 7445 7022 418 2348 -632 C
ATOM 2465 C VAL B 54 53.518 -41.106 0.152 1.00 78.12 C
ANISOU 2465 C VAL B 54 16507 6963 6214 456 2311 -606 C
ATOM 2466 O VAL B 54 54.662 -40.801 -0.229 1.00 69.64 O
ANISOU 2466 O VAL B 54 15352 5899 5208 594 2531 -552 O
ATOM 2467 CB VAL B 54 53.073 -43.538 0.727 1.00 68.65 C
ANISOU 2467 CB VAL B 54 15608 5381 5094 308 2322 -840 C
ATOM 2468 CG1 VAL B 54 54.209 -43.927 -0.200 1.00 71.18 C
ANISOU 2468 CG1 VAL B 54 16045 5625 5374 429 2544 -897 C
ATOM 2469 CG2 VAL B 54 52.940 -44.534 1.867 1.00 67.97 C
ANISOU 2469 CG2 VAL B 54 15477 5118 5232 274 2373 -851 C
ATOM 2470 N ALA B 55 52.426 -40.562 -0.394 1.00 70.18 N
ANISOU 2470 N ALA B 55 15623 6064 4977 327 2023 -647 N
ATOM 2471 CA ALA B 55 52.553 -39.562 -1.442 1.00 67.85 C
ANISOU 2471 CA ALA B 55 15382 5897 4500 363 1967 -607 C
ATOM 2472 C ALA B 55 53.253 -38.325 -0.908 1.00 79.97 C
ANISOU 2472 C ALA B 55 16551 7587 6246 510 2102 -413 C
ATOM 2473 O ALA B 55 54.161 -37.782 -1.550 1.00 69.73 O
ANISOU 2473 O ALA B 55 15238 6310 4947 605 2268 -370 O
ATOM 2474 CB ALA B 55 51.173 -39.212 -1.993 1.00 69.37 C
ANISOU 2474 CB ALA B 55 15749 6183 4425 204 1579 -669 C
ATOM 2475 N VAL B 56 52.847 -37.868 0.278 1.00 88.38 N
ANISOU 2475 N VAL B 56 17320 8759 7502 519 2034 -306 N
ATOM 2476 CA VAL B 56 53.504 -36.711 0.875 1.00 79.79 C
ANISOU 2476 CA VAL B 56 15858 7813 6646 652 2139 -143 C
ATOM 2477 C VAL B 56 54.968 -37.021 1.159 1.00 76.82 C
ANISOU 2477 C VAL B 56 15347 7339 6504 792 2446 -109 C
ATOM 2478 O VAL B 56 55.842 -36.169 0.969 1.00 72.00 O
ANISOU 2478 O VAL B 56 14569 6791 5997 888 2569 -33 O
ATOM 2479 CB VAL B 56 52.759 -36.271 2.146 1.00 76.58 C
ANISOU 2479 CB VAL B 56 15161 7540 6395 631 2011 -50 C
ATOM 2480 CG1 VAL B 56 53.666 -35.407 3.015 1.00 74.40 C
ANISOU 2480 CG1 VAL B 56 14479 7361 6430 779 2158 87 C
ATOM 2481 CG2 VAL B 56 51.479 -35.538 1.778 1.00 75.13 C
ANISOU 2481 CG2 VAL B 56 15034 7510 6003 524 1704 -38 C
ATOM 2482 N PHE B 57 55.261 -38.249 1.604 1.00 74.51 N
ANISOU 2482 N PHE B 57 15133 6884 6293 799 2565 -167 N
ATOM 2483 CA PHE B 57 56.638 -38.633 1.913 1.00 68.29 C
ANISOU 2483 CA PHE B 57 14214 6009 5724 937 2831 -128 C
ATOM 2484 C PHE B 57 57.517 -38.492 0.683 1.00 75.35 C
ANISOU 2484 C PHE B 57 15249 6870 6510 977 2993 -180 C
ATOM 2485 O PHE B 57 58.571 -37.836 0.713 1.00 77.31 O
ANISOU 2485 O PHE B 57 15287 7169 6917 1078 3153 -102 O
ATOM 2486 CB PHE B 57 56.677 -40.079 2.414 1.00 69.52 C
ANISOU 2486 CB PHE B 57 14501 5982 5933 928 2908 -198 C
ATOM 2487 CG PHE B 57 58.072 -40.610 2.676 1.00 81.51 C
ANISOU 2487 CG PHE B 57 15898 7416 7656 1074 3159 -170 C
ATOM 2488 CD1 PHE B 57 58.721 -40.357 3.877 1.00 85.93 C
ANISOU 2488 CD1 PHE B 57 16129 8031 8489 1187 3224 -30 C
ATOM 2489 CD2 PHE B 57 58.732 -41.367 1.717 1.00 86.56 C
ANISOU 2489 CD2 PHE B 57 16748 7934 8206 1097 3319 -295 C
ATOM 2490 CE1 PHE B 57 59.999 -40.854 4.116 1.00 86.45 C
ANISOU 2490 CE1 PHE B 57 16068 8042 8736 1317 3423 -14 C
ATOM 2491 CE2 PHE B 57 60.009 -41.865 1.952 1.00 89.50 C
ANISOU 2491 CE2 PHE B 57 16983 8247 8777 1233 3543 -289 C
ATOM 2492 CZ PHE B 57 60.642 -41.609 3.150 1.00 87.25 C
ANISOU 2492 CZ PHE B 57 16359 8027 8765 1342 3584 -149 C
ATOM 2493 N VAL B 58 57.071 -39.078 -0.425 1.00 84.03 N
ANISOU 2493 N VAL B 58 16715 7885 7326 886 2947 -321 N
ATOM 2494 CA VAL B 58 57.873 -39.066 -1.640 1.00 92.67 C
ANISOU 2494 CA VAL B 58 17991 8936 8283 917 3126 -388 C
ATOM 2495 C VAL B 58 58.010 -37.645 -2.176 1.00 87.07 C
ANISOU 2495 C VAL B 58 17200 8372 7511 929 3106 -296 C
ATOM 2496 O VAL B 58 59.120 -37.174 -2.471 1.00 67.70 O
ANISOU 2496 O VAL B 58 14641 5928 5152 1010 3331 -254 O
ATOM 2497 CB VAL B 58 57.246 -40.003 -2.685 1.00 90.20 C
ANISOU 2497 CB VAL B 58 18109 8506 7656 807 3044 -572 C
ATOM 2498 CG1 VAL B 58 58.036 -39.963 -3.982 1.00 75.03 C
ANISOU 2498 CG1 VAL B 58 16402 6547 5557 836 3241 -648 C
ATOM 2499 CG2 VAL B 58 57.128 -41.412 -2.123 1.00 83.98 C
ANISOU 2499 CG2 VAL B 58 17400 7554 6956 789 3067 -674 C
ATOM 2500 N VAL B 59 56.886 -36.928 -2.282 1.00 76.05 N
ANISOU 2500 N VAL B 59 15843 7089 5963 847 2836 -264 N
ATOM 2501 CA VAL B 59 56.932 -35.591 -2.856 1.00 74.21 C
ANISOU 2501 CA VAL B 59 15570 6981 5645 857 2799 -178 C
ATOM 2502 C VAL B 59 57.802 -34.668 -2.016 1.00 90.91 C
ANISOU 2502 C VAL B 59 17282 9178 8083 963 2935 -42 C
ATOM 2503 O VAL B 59 58.624 -33.917 -2.552 1.00102.93 O
ANISOU 2503 O VAL B 59 18774 10719 9614 1005 3097 1 O
ATOM 2504 CB VAL B 59 55.499 -35.039 -2.974 1.00 71.29 C
ANISOU 2504 CB VAL B 59 15282 6727 5079 759 2450 -161 C
ATOM 2505 CG1 VAL B 59 55.511 -33.583 -3.407 1.00 75.94 C
ANISOU 2505 CG1 VAL B 59 15796 7446 5612 784 2397 -48 C
ATOM 2506 CG2 VAL B 59 54.666 -35.898 -3.905 1.00 78.58 C
ANISOU 2506 CG2 VAL B 59 16622 7569 5664 641 2277 -308 C
ATOM 2507 N ALA B 60 57.706 -34.766 -0.688 1.00 92.08 N
ANISOU 2507 N ALA B 60 17131 9361 8495 1002 2886 18 N
ATOM 2508 CA ALA B 60 58.470 -33.856 0.151 1.00 80.19 C
ANISOU 2508 CA ALA B 60 15245 7940 7285 1093 2970 136 C
ATOM 2509 C ALA B 60 59.953 -34.184 0.135 1.00 64.85 C
ANISOU 2509 C ALA B 60 13217 5908 5516 1180 3260 136 C
ATOM 2510 O ALA B 60 60.787 -33.285 -0.038 1.00 58.27 O
ANISOU 2510 O ALA B 60 12241 5117 4782 1222 3387 194 O
ATOM 2511 CB ALA B 60 57.933 -33.886 1.581 1.00 89.75 C
ANISOU 2511 CB ALA B 60 16179 9218 8703 1109 2829 195 C
ATOM 2512 N LEU B 61 60.302 -35.472 0.198 1.00 67.74 N
ANISOU 2512 N LEU B 61 13694 6144 5900 1200 3378 61 N
ATOM 2513 CA LEU B 61 61.714 -35.822 0.171 1.00 76.30 C
ANISOU 2513 CA LEU B 61 14679 7159 7150 1286 3652 53 C
ATOM 2514 C LEU B 61 62.354 -35.393 -1.146 1.00 87.33 C
ANISOU 2514 C LEU B 61 16254 8538 8389 1272 3841 4 C
ATOM 2515 O LEU B 61 63.381 -34.694 -1.158 1.00 99.07 O
ANISOU 2515 O LEU B 61 17552 10059 10030 1320 4013 55 O
ATOM 2516 CB LEU B 61 61.868 -37.320 0.418 1.00 74.36 C
ANISOU 2516 CB LEU B 61 14543 6780 6931 1313 3731 -33 C
ATOM 2517 CG LEU B 61 63.305 -37.818 0.493 1.00 83.82 C
ANISOU 2517 CG LEU B 61 15605 7919 8325 1417 4001 -60 C
ATOM 2518 CD1 LEU B 61 64.019 -37.109 1.625 1.00 79.40 C
ANISOU 2518 CD1 LEU B 61 14634 7460 8072 1494 4003 72 C
ATOM 2519 CD2 LEU B 61 63.344 -39.323 0.688 1.00 86.63 C
ANISOU 2519 CD2 LEU B 61 16090 8135 8691 1451 4057 -162 C
ATOM 2520 N VAL B 62 61.701 -35.706 -2.266 1.00 81.40 N
ANISOU 2520 N VAL B 62 15876 7739 7312 1193 3798 -93 N
ATOM 2521 CA VAL B 62 62.293 -35.396 -3.563 1.00 88.77 C
ANISOU 2521 CA VAL B 62 17031 8645 8053 1176 3997 -145 C
ATOM 2522 C VAL B 62 62.367 -33.888 -3.769 1.00 90.71 C
ANISOU 2522 C VAL B 62 17169 9001 8296 1163 3973 -32 C
ATOM 2523 O VAL B 62 63.413 -33.346 -4.155 1.00 89.48 O
ANISOU 2523 O VAL B 62 16948 8840 8210 1193 4215 -9 O
ATOM 2524 CB VAL B 62 61.502 -36.071 -4.691 1.00 74.00 C
ANISOU 2524 CB VAL B 62 15610 6705 5803 1090 3918 -275 C
ATOM 2525 CG1 VAL B 62 61.916 -35.485 -6.031 1.00 77.75 C
ANISOU 2525 CG1 VAL B 62 16336 7178 6026 1061 4079 -300 C
ATOM 2526 CG2 VAL B 62 61.734 -37.561 -4.650 1.00 94.63 C
ANISOU 2526 CG2 VAL B 62 18344 9180 8430 1112 4024 -411 C
ATOM 2527 N GLY B 63 61.262 -33.183 -3.523 1.00 85.35 N
ANISOU 2527 N GLY B 63 16470 8420 7538 1116 3689 33 N
ATOM 2528 CA GLY B 63 61.233 -31.768 -3.822 1.00 80.66 C
ANISOU 2528 CA GLY B 63 15821 7921 6905 1102 3653 131 C
ATOM 2529 C GLY B 63 62.176 -30.970 -2.946 1.00 90.34 C
ANISOU 2529 C GLY B 63 16656 9195 8476 1172 3775 227 C
ATOM 2530 O GLY B 63 62.840 -30.048 -3.422 1.00103.49 O
ANISOU 2530 O GLY B 63 18306 10872 10145 1172 3928 276 O
ATOM 2531 N ASN B 64 62.236 -31.283 -1.652 1.00 93.10 N
ANISOU 2531 N ASN B 64 16700 9568 9107 1224 3702 258 N
ATOM 2532 CA ASN B 64 63.152 -30.542 -0.794 1.00 92.40 C
ANISOU 2532 CA ASN B 64 16248 9524 9334 1285 3793 343 C
ATOM 2533 C ASN B 64 64.617 -30.854 -1.125 1.00 85.29 C
ANISOU 2533 C ASN B 64 15307 8542 8556 1324 4120 309 C
ATOM 2534 O ASN B 64 65.472 -29.946 -1.116 1.00 86.14 O
ANISOU 2534 O ASN B 64 15251 8673 8806 1336 4264 362 O
ATOM 2535 CB ASN B 64 62.817 -30.854 0.662 1.00 95.71 C
ANISOU 2535 CB ASN B 64 16387 9993 9987 1328 3620 385 C
ATOM 2536 CG ASN B 64 61.559 -30.130 1.133 1.00 96.73 C
ANISOU 2536 CG ASN B 64 16447 10239 10068 1295 3335 433 C
ATOM 2537 OD1 ASN B 64 61.558 -28.913 1.348 1.00 97.21 O
ANISOU 2537 OD1 ASN B 64 16346 10386 10203 1300 3282 503 O
ATOM 2538 ND2 ASN B 64 60.460 -30.882 1.247 1.00 95.35 N
ANISOU 2538 ND2 ASN B 64 16407 10065 9757 1255 3160 386 N
ATOM 2539 N THR B 65 64.931 -32.108 -1.493 1.00 84.68 N
ANISOU 2539 N THR B 65 15390 8367 8418 1340 4256 210 N
ATOM 2540 CA THR B 65 66.291 -32.365 -1.962 1.00 94.55 C
ANISOU 2540 CA THR B 65 16611 9552 9761 1376 4587 156 C
ATOM 2541 C THR B 65 66.590 -31.539 -3.212 1.00106.37 C
ANISOU 2541 C THR B 65 18322 11038 11058 1321 4765 150 C
ATOM 2542 O THR B 65 67.700 -31.009 -3.375 1.00109.25 O
ANISOU 2542 O THR B 65 18549 11394 11566 1335 5013 164 O
ATOM 2543 CB THR B 65 66.497 -33.863 -2.216 1.00 87.89 C
ANISOU 2543 CB THR B 65 15925 8605 8866 1409 4704 30 C
ATOM 2544 OG1 THR B 65 65.373 -34.389 -2.928 1.00 93.95 O
ANISOU 2544 OG1 THR B 65 17060 9330 9308 1344 4563 -38 O
ATOM 2545 CG2 THR B 65 66.650 -34.625 -0.898 1.00 73.23 C
ANISOU 2545 CG2 THR B 65 13799 6749 7275 1484 4615 49 C
ATOM 2546 N LEU B 66 65.597 -31.399 -4.100 1.00103.08 N
ANISOU 2546 N LEU B 66 18246 10620 10299 1252 4639 132 N
ATOM 2547 CA LEU B 66 65.785 -30.569 -5.289 1.00 97.91 C
ANISOU 2547 CA LEU B 66 17832 9959 9411 1196 4786 146 C
ATOM 2548 C LEU B 66 65.929 -29.095 -4.939 1.00 87.56 C
ANISOU 2548 C LEU B 66 16312 8725 8232 1187 4749 274 C
ATOM 2549 O LEU B 66 66.620 -28.364 -5.648 1.00 87.75 O
ANISOU 2549 O LEU B 66 16412 8726 8202 1159 4979 300 O
ATOM 2550 CB LEU B 66 64.649 -30.757 -6.295 1.00 96.58 C
ANISOU 2550 CB LEU B 66 18089 9784 8825 1125 4619 102 C
ATOM 2551 CG LEU B 66 64.607 -32.111 -6.990 1.00 98.62 C
ANISOU 2551 CG LEU B 66 18650 9943 8878 1115 4710 -47 C
ATOM 2552 CD1 LEU B 66 63.536 -32.100 -8.058 1.00100.03 C
ANISOU 2552 CD1 LEU B 66 19263 10123 8621 1032 4531 -83 C
ATOM 2553 CD2 LEU B 66 65.974 -32.397 -7.601 1.00 95.35 C
ANISOU 2553 CD2 LEU B 66 18267 9450 8510 1144 5123 -120 C
ATOM 2554 N VAL B 67 65.296 -28.635 -3.862 1.00 86.59 N
ANISOU 2554 N VAL B 67 15935 8687 8276 1208 4481 351 N
ATOM 2555 CA VAL B 67 65.470 -27.235 -3.484 1.00 87.13 C
ANISOU 2555 CA VAL B 67 15800 8822 8484 1204 4454 460 C
ATOM 2556 C VAL B 67 66.918 -26.991 -3.093 1.00 85.12 C
ANISOU 2556 C VAL B 67 15275 8533 8534 1238 4730 472 C
ATOM 2557 O VAL B 67 67.555 -26.024 -3.547 1.00 82.48 O
ANISOU 2557 O VAL B 67 14941 8183 8214 1207 4917 518 O
ATOM 2558 CB VAL B 67 64.510 -26.847 -2.339 1.00 80.11 C
ANISOU 2558 CB VAL B 67 14679 8036 7722 1226 4122 523 C
ATOM 2559 CG1 VAL B 67 64.881 -25.482 -1.775 1.00 61.58 C
ANISOU 2559 CG1 VAL B 67 12076 5743 5578 1237 4125 620 C
ATOM 2560 CG2 VAL B 67 63.059 -26.858 -2.798 1.00 75.51 C
ANISOU 2560 CG2 VAL B 67 14346 7505 6840 1180 3851 518 C
ATOM 2561 N CYS B 68 67.486 -27.910 -2.307 1.00 84.41 N
ANISOU 2561 N CYS B 68 14968 8425 8680 1296 4774 426 N
ATOM 2562 CA CYS B 68 68.901 -27.760 -1.981 1.00 84.98 C
ANISOU 2562 CA CYS B 68 14775 8472 9040 1324 5033 422 C
ATOM 2563 C CYS B 68 69.771 -27.851 -3.227 1.00 82.99 C
ANISOU 2563 C CYS B 68 14731 8138 8665 1292 5396 355 C
ATOM 2564 O CYS B 68 70.697 -27.048 -3.403 1.00 88.34 O
ANISOU 2564 O CYS B 68 15290 8801 9475 1269 5624 382 O
ATOM 2565 CB CYS B 68 69.339 -28.811 -0.962 1.00 97.36 C
ANISOU 2565 CB CYS B 68 16091 10045 10855 1398 5001 381 C
ATOM 2566 SG CYS B 68 68.488 -28.749 0.630 1.00101.52 S
ANISOU 2566 SG CYS B 68 16357 10671 11546 1436 4620 465 S
ATOM 2567 N LEU B 69 69.478 -28.799 -4.118 1.00 77.26 N
ANISOU 2567 N LEU B 69 14326 7353 7677 1283 5467 261 N
ATOM 2568 CA LEU B 69 70.320 -28.956 -5.300 1.00 90.21 C
ANISOU 2568 CA LEU B 69 16175 8915 9185 1255 5836 184 C
ATOM 2569 C LEU B 69 70.238 -27.743 -6.223 1.00 95.82 C
ANISOU 2569 C LEU B 69 17104 9622 9680 1174 5936 256 C
ATOM 2570 O LEU B 69 71.245 -27.333 -6.817 1.00 93.25 O
ANISOU 2570 O LEU B 69 16789 9252 9392 1146 6277 243 O
ATOM 2571 CB LEU B 69 69.896 -30.218 -6.037 1.00 96.89 C
ANISOU 2571 CB LEU B 69 17350 9700 9765 1261 5858 61 C
ATOM 2572 CG LEU B 69 70.227 -31.396 -5.134 1.00101.65 C
ANISOU 2572 CG LEU B 69 17717 10288 10618 1348 5828 -11 C
ATOM 2573 CD1 LEU B 69 69.863 -32.713 -5.801 1.00107.76 C
ANISOU 2573 CD1 LEU B 69 18804 10983 11156 1359 5864 -149 C
ATOM 2574 CD2 LEU B 69 71.685 -31.330 -4.708 1.00106.20 C
ANISOU 2574 CD2 LEU B 69 17943 10860 11549 1403 6103 -37 C
ATOM 2575 N ALA B 70 69.054 -27.135 -6.321 1.00100.22 N
ANISOU 2575 N ALA B 70 17825 10231 10024 1138 5646 334 N
ATOM 2576 CA ALA B 70 68.867 -25.958 -7.158 1.00101.57 C
ANISOU 2576 CA ALA B 70 18219 10404 9970 1066 5700 418 C
ATOM 2577 C ALA B 70 69.642 -24.779 -6.605 1.00107.16 C
ANISOU 2577 C ALA B 70 18624 11125 10967 1059 5819 509 C
ATOM 2578 O ALA B 70 70.373 -24.102 -7.335 1.00 85.92 O
ANISOU 2578 O ALA B 70 16035 8384 8225 1005 6114 536 O
ATOM 2579 CB ALA B 70 67.381 -25.617 -7.276 1.00 93.50 C
ANISOU 2579 CB ALA B 70 17397 9447 8681 1041 5325 477 C
ATOM 2580 N VAL B 71 69.498 -24.521 -5.304 1.00106.12 N
ANISOU 2580 N VAL B 71 18127 11056 11137 1107 5601 555 N
ATOM 2581 CA VAL B 71 70.214 -23.388 -4.734 1.00104.86 C
ANISOU 2581 CA VAL B 71 17683 10904 11255 1096 5698 633 C
ATOM 2582 C VAL B 71 71.715 -23.624 -4.807 1.00 99.77 C
ANISOU 2582 C VAL B 71 16862 10195 10853 1094 6078 572 C
ATOM 2583 O VAL B 71 72.489 -22.676 -4.992 1.00 90.19 O
ANISOU 2583 O VAL B 71 15567 8945 9757 1045 6308 617 O
ATOM 2584 CB VAL B 71 69.759 -23.138 -3.279 1.00 95.69 C
ANISOU 2584 CB VAL B 71 16175 9825 10357 1150 5382 681 C
ATOM 2585 CG1 VAL B 71 70.631 -22.081 -2.612 1.00 93.59 C
ANISOU 2585 CG1 VAL B 71 15597 9556 10409 1139 5496 740 C
ATOM 2586 CG2 VAL B 71 68.290 -22.739 -3.222 1.00 79.89 C
ANISOU 2586 CG2 VAL B 71 14319 7896 8138 1147 5034 738 C
ATOM 2587 N TRP B 72 72.154 -24.884 -4.691 1.00100.95 N
ANISOU 2587 N TRP B 72 16947 10325 11083 1145 6163 464 N
ATOM 2588 CA TRP B 72 73.580 -25.166 -4.802 1.00109.48 C
ANISOU 2588 CA TRP B 72 17843 11355 12401 1152 6531 388 C
ATOM 2589 C TRP B 72 74.090 -24.943 -6.224 1.00125.04 C
ANISOU 2589 C TRP B 72 20126 13245 14138 1081 6910 356 C
ATOM 2590 O TRP B 72 75.233 -24.510 -6.408 1.00136.02 O
ANISOU 2590 O TRP B 72 21366 14594 15723 1048 7244 339 O
ATOM 2591 CB TRP B 72 73.867 -26.599 -4.345 1.00112.53 C
ANISOU 2591 CB TRP B 72 18095 11744 12916 1238 6518 275 C
ATOM 2592 CG TRP B 72 75.247 -27.060 -4.653 1.00118.07 C
ANISOU 2592 CG TRP B 72 18651 12395 13815 1258 6906 165 C
ATOM 2593 CD1 TRP B 72 76.368 -26.726 -3.952 1.00118.60 C
ANISOU 2593 CD1 TRP B 72 18310 12478 14276 1278 7043 153 C
ATOM 2594 CD2 TRP B 72 75.678 -27.915 -5.717 1.00136.36 C
ANISOU 2594 CD2 TRP B 72 21207 14642 15964 1265 7212 39 C
ATOM 2595 NE1 TRP B 72 77.469 -27.317 -4.504 1.00136.49 N
ANISOU 2595 NE1 TRP B 72 20521 14690 16648 1301 7414 25 N
ATOM 2596 CE2 TRP B 72 77.078 -28.053 -5.592 1.00150.32 C
ANISOU 2596 CE2 TRP B 72 22670 16387 18056 1296 7536 -47 C
ATOM 2597 CE3 TRP B 72 75.026 -28.578 -6.761 1.00141.32 C
ANISOU 2597 CE3 TRP B 72 22272 15223 16198 1248 7245 -21 C
ATOM 2598 CZ2 TRP B 72 77.838 -28.826 -6.471 1.00161.10 C
ANISOU 2598 CZ2 TRP B 72 24149 17688 19375 1319 7906 -193 C
ATOM 2599 CZ3 TRP B 72 75.789 -29.349 -7.637 1.00147.25 C
ANISOU 2599 CZ3 TRP B 72 23159 15907 16883 1265 7610 -164 C
ATOM 2600 CH2 TRP B 72 77.178 -29.464 -7.482 1.00155.20 C
ANISOU 2600 CH2 TRP B 72 23848 16893 18227 1304 7944 -249 C
ATOM 2601 N ARG B 73 73.268 -25.240 -7.242 1.00127.12 N
ANISOU 2601 N ARG B 73 20829 13489 13983 1050 6869 343 N
ATOM 2602 CA ARG B 73 73.746 -25.196 -8.626 1.00118.64 C
ANISOU 2602 CA ARG B 73 20096 12340 12642 985 7238 300 C
ATOM 2603 C ARG B 73 73.774 -23.774 -9.177 1.00112.83 C
ANISOU 2603 C ARG B 73 19502 11586 11783 892 7348 425 C
ATOM 2604 O ARG B 73 74.762 -23.361 -9.790 1.00103.12 O
ANISOU 2604 O ARG B 73 18297 10294 10589 834 7745 416 O
ATOM 2605 CB ARG B 73 72.907 -26.090 -9.548 1.00112.19 C
ANISOU 2605 CB ARG B 73 19722 11505 11399 982 7160 229 C
ATOM 2606 CG ARG B 73 73.347 -27.547 -9.600 1.00107.78 C
ANISOU 2606 CG ARG B 73 19145 10910 10894 1049 7296 66 C
ATOM 2607 CD ARG B 73 72.769 -28.263 -10.818 1.00104.76 C
ANISOU 2607 CD ARG B 73 19268 10483 10052 1020 7341 -21 C
ATOM 2608 NE ARG B 73 73.269 -27.727 -12.084 1.00115.20 N
ANISOU 2608 NE ARG B 73 20910 11752 11108 939 7700 -20 N
ATOM 2609 CZ ARG B 73 74.239 -28.281 -12.811 1.00127.60 C
ANISOU 2609 CZ ARG B 73 22572 13258 12653 940 8125 -147 C
ATOM 2610 NH1 ARG B 73 74.822 -29.405 -12.413 1.00132.47 N
ANISOU 2610 NH1 ARG B 73 22977 13854 13502 1027 8236 -292 N
ATOM 2611 NH2 ARG B 73 74.617 -27.715 -13.950 1.00132.63 N
ANISOU 2611 NH2 ARG B 73 23523 13849 13021 855 8447 -130 N
ATOM 2612 N ASN B 74 72.705 -23.010 -8.955 1.00106.02 N
ANISOU 2612 N ASN B 74 18725 10776 10783 877 7011 541 N
ATOM 2613 CA ASN B 74 72.552 -21.660 -9.496 1.00117.04 C
ANISOU 2613 CA ASN B 74 20297 12155 12017 795 7065 673 C
ATOM 2614 C ASN B 74 73.001 -20.662 -8.430 1.00123.94 C
ANISOU 2614 C ASN B 74 20757 13045 13288 797 7031 751 C
ATOM 2615 O ASN B 74 72.371 -20.543 -7.371 1.00129.60 O
ANISOU 2615 O ASN B 74 21238 13833 14169 853 6684 784 O
ATOM 2616 CB ASN B 74 71.095 -21.430 -9.908 1.00114.67 C
ANISOU 2616 CB ASN B 74 20333 11905 11329 784 6704 746 C
ATOM 2617 CG ASN B 74 70.854 -20.067 -10.535 1.00113.70 C
ANISOU 2617 CG ASN B 74 20436 11766 10997 704 6735 895 C
ATOM 2618 OD1 ASN B 74 71.707 -19.181 -10.490 1.00112.37 O
ANISOU 2618 OD1 ASN B 74 20135 11550 11012 655 6995 956 O
ATOM 2619 ND2 ASN B 74 69.664 -19.889 -11.106 1.00113.06 N
ANISOU 2619 ND2 ASN B 74 20698 11723 10535 688 6455 958 N
ATOM 2620 N HIS B 75 74.106 -19.956 -8.711 1.00121.41 N
ANISOU 2620 N HIS B 75 20351 12655 13123 730 7406 775 N
ATOM 2621 CA HIS B 75 74.648 -18.958 -7.790 1.00127.93 C
ANISOU 2621 CA HIS B 75 20801 13477 14329 714 7419 839 C
ATOM 2622 C HIS B 75 73.789 -17.702 -7.671 1.00134.87 C
ANISOU 2622 C HIS B 75 21777 14378 15088 682 7182 988 C
ATOM 2623 O HIS B 75 73.864 -17.020 -6.641 1.00133.07 O
ANISOU 2623 O HIS B 75 21225 14172 15165 699 7047 1032 O
ATOM 2624 CB HIS B 75 76.068 -18.575 -8.213 1.00135.34 C
ANISOU 2624 CB HIS B 75 21634 14325 15464 636 7912 814 C
ATOM 2625 CG HIS B 75 77.063 -19.683 -8.054 1.00145.12 C
ANISOU 2625 CG HIS B 75 22644 15552 16944 681 8141 663 C
ATOM 2626 ND1 HIS B 75 77.492 -20.124 -6.821 1.00144.46 N
ANISOU 2626 ND1 HIS B 75 22104 15513 17270 757 8005 600 N
ATOM 2627 CD2 HIS B 75 77.720 -20.433 -8.971 1.00151.50 C
ANISOU 2627 CD2 HIS B 75 23616 16310 17637 664 8498 560 C
ATOM 2628 CE1 HIS B 75 78.363 -21.103 -6.984 1.00144.47 C
ANISOU 2628 CE1 HIS B 75 21988 15497 17408 791 8255 468 C
ATOM 2629 NE2 HIS B 75 78.521 -21.309 -8.279 1.00151.11 N
ANISOU 2629 NE2 HIS B 75 23194 16278 17945 738 8567 435 N
ATOM 2630 N HIS B 76 72.965 -17.380 -8.672 1.00139.21 N
ANISOU 2630 N HIS B 76 22764 14926 15203 639 7115 1065 N
ATOM 2631 CA HIS B 76 72.097 -16.216 -8.515 1.00130.64 C
ANISOU 2631 CA HIS B 76 21755 13870 14013 619 6860 1210 C
ATOM 2632 C HIS B 76 71.101 -16.449 -7.398 1.00117.31 C
ANISOU 2632 C HIS B 76 19845 12287 12440 715 6404 1198 C
ATOM 2633 O HIS B 76 70.616 -15.490 -6.787 1.00113.02 O
ANISOU 2633 O HIS B 76 19177 11774 11990 722 6202 1291 O
ATOM 2634 CB HIS B 76 71.383 -15.852 -9.820 1.00140.91 C
ANISOU 2634 CB HIS B 76 23577 15152 14809 556 6846 1306 C
ATOM 2635 CG HIS B 76 72.283 -15.245 -10.851 1.00152.89 C
ANISOU 2635 CG HIS B 76 25326 16562 16203 444 7290 1366 C
ATOM 2636 ND1 HIS B 76 72.924 -15.983 -11.823 1.00158.55 N
ANISOU 2636 ND1 HIS B 76 26279 17224 16739 405 7632 1282 N
ATOM 2637 CD2 HIS B 76 72.661 -13.958 -11.048 1.00156.15 C
ANISOU 2637 CD2 HIS B 76 25772 16907 16653 355 7467 1503 C
ATOM 2638 CE1 HIS B 76 73.655 -15.179 -12.575 1.00165.04 C
ANISOU 2638 CE1 HIS B 76 27269 17954 17486 295 8007 1365 C
ATOM 2639 NE2 HIS B 76 73.512 -13.944 -12.125 1.00164.38 N
ANISOU 2639 NE2 HIS B 76 27066 17856 17534 260 7913 1504 N
ATOM 2640 N MET B 77 70.758 -17.706 -7.136 1.00119.08 N
ANISOU 2640 N MET B 77 20033 12563 12649 786 6246 1088 N
ATOM 2641 CA MET B 77 69.797 -17.967 -6.084 1.00110.42 C
ANISOU 2641 CA MET B 77 18737 11565 11652 867 5834 1078 C
ATOM 2642 C MET B 77 70.443 -17.997 -4.703 1.00120.96 C
ANISOU 2642 C MET B 77 19593 12918 13449 920 5814 1040 C
ATOM 2643 O MET B 77 69.718 -18.153 -3.714 1.00137.04 O
ANISOU 2643 O MET B 77 21440 15036 15593 986 5493 1037 O
ATOM 2644 CB MET B 77 69.056 -19.281 -6.361 1.00 91.18 C
ANISOU 2644 CB MET B 77 16479 9170 8994 909 5655 988 C
ATOM 2645 CG MET B 77 68.179 -19.240 -7.602 1.00 96.04 C
ANISOU 2645 CG MET B 77 17570 9787 9136 861 5574 1028 C
ATOM 2646 SD MET B 77 67.931 -20.851 -8.366 1.00107.66 S
ANISOU 2646 SD MET B 77 19331 11241 10335 873 5590 889 S
ATOM 2647 CE MET B 77 67.055 -21.742 -7.088 1.00 96.18 C
ANISOU 2647 CE MET B 77 17591 9878 9074 960 5198 824 C
ATOM 2648 N ARG B 78 71.773 -17.852 -4.590 1.00106.78 N
ANISOU 2648 N ARG B 78 17595 11051 11925 890 6142 1012 N
ATOM 2649 CA ARG B 78 72.403 -17.930 -3.271 1.00 93.76 C
ANISOU 2649 CA ARG B 78 15494 9423 10706 937 6096 975 C
ATOM 2650 C ARG B 78 72.226 -16.568 -2.600 1.00 96.80 C
ANISOU 2650 C ARG B 78 15716 9813 11249 919 5988 1071 C
ATOM 2651 O ARG B 78 73.173 -15.819 -2.345 1.00 97.46 O
ANISOU 2651 O ARG B 78 15597 9834 11598 871 6204 1090 O
ATOM 2652 CB ARG B 78 73.872 -18.328 -3.350 1.00 90.27 C
ANISOU 2652 CB ARG B 78 14862 8916 10521 912 6461 896 C
ATOM 2653 CG ARG B 78 74.152 -19.681 -3.970 1.00 96.18 C
ANISOU 2653 CG ARG B 78 15746 9652 11145 938 6602 788 C
ATOM 2654 CD ARG B 78 75.610 -20.070 -3.731 1.00104.90 C
ANISOU 2654 CD ARG B 78 16548 10716 12594 935 6915 700 C
ATOM 2655 NE ARG B 78 75.989 -21.311 -4.402 1.00115.26 N
ANISOU 2655 NE ARG B 78 17989 12005 13798 962 7108 586 N
ATOM 2656 CZ ARG B 78 77.156 -21.924 -4.225 1.00122.03 C
ANISOU 2656 CZ ARG B 78 18589 12843 14934 986 7354 483 C
ATOM 2657 NH1 ARG B 78 78.055 -21.412 -3.392 1.00134.84 N
ANISOU 2657 NH1 ARG B 78 19804 14470 16958 978 7419 479 N
ATOM 2658 NH2 ARG B 78 77.421 -23.054 -4.870 1.00111.88 N
ANISOU 2658 NH2 ARG B 78 17444 11535 13531 1021 7529 373 N
ATOM 2659 N THR B 79 70.967 -16.261 -2.316 1.00 93.99 N
ANISOU 2659 N THR B 79 15447 9531 10732 958 5652 1127 N
ATOM 2660 CA THR B 79 70.544 -15.052 -1.629 1.00 89.97 C
ANISOU 2660 CA THR B 79 14807 9041 10337 960 5495 1213 C
ATOM 2661 C THR B 79 70.303 -15.346 -0.151 1.00102.45 C
ANISOU 2661 C THR B 79 16041 10701 12187 1043 5230 1174 C
ATOM 2662 O THR B 79 70.294 -16.501 0.287 1.00112.00 O
ANISOU 2662 O THR B 79 17150 11958 13446 1095 5128 1098 O
ATOM 2663 CB THR B 79 69.295 -14.471 -2.302 1.00 88.50 C
ANISOU 2663 CB THR B 79 14941 8893 9792 947 5301 1304 C
ATOM 2664 OG1 THR B 79 68.226 -15.430 -2.273 1.00 84.10 O
ANISOU 2664 OG1 THR B 79 14488 8431 9035 1006 5012 1256 O
ATOM 2665 CG2 THR B 79 69.604 -14.107 -3.747 1.00 75.69 C
ANISOU 2665 CG2 THR B 79 13683 7188 7890 854 5568 1364 C
ATOM 2666 N VAL B 80 70.131 -14.278 0.630 1.00101.06 N
ANISOU 2666 N VAL B 80 15689 10530 12180 1050 5130 1233 N
ATOM 2667 CA VAL B 80 69.786 -14.455 2.039 1.00 98.60 C
ANISOU 2667 CA VAL B 80 15083 10297 12082 1124 4867 1208 C
ATOM 2668 C VAL B 80 68.487 -15.248 2.165 1.00 93.53 C
ANISOU 2668 C VAL B 80 14556 9765 11215 1190 4554 1187 C
ATOM 2669 O VAL B 80 68.406 -16.256 2.890 1.00 97.73 O
ANISOU 2669 O VAL B 80 14943 10357 11831 1240 4412 1129 O
ATOM 2670 CB VAL B 80 69.669 -13.084 2.730 1.00103.75 C
ANISOU 2670 CB VAL B 80 15586 10929 12907 1120 4821 1277 C
ATOM 2671 CG1 VAL B 80 69.050 -13.233 4.110 1.00 94.96 C
ANISOU 2671 CG1 VAL B 80 14235 9910 11935 1200 4523 1259 C
ATOM 2672 CG2 VAL B 80 71.024 -12.392 2.794 1.00115.63 C
ANISOU 2672 CG2 VAL B 80 16913 12318 14703 1044 5123 1280 C
ATOM 2673 N THR B 81 67.466 -14.831 1.409 1.00 78.23 N
ANISOU 2673 N THR B 81 12889 7856 8979 1179 4448 1239 N
ATOM 2674 CA THR B 81 66.168 -15.496 1.451 1.00 81.08 C
ANISOU 2674 CA THR B 81 13357 8323 9127 1223 4153 1217 C
ATOM 2675 C THR B 81 66.290 -16.970 1.086 1.00 85.33 C
ANISOU 2675 C THR B 81 13986 8865 9569 1229 4174 1130 C
ATOM 2676 O THR B 81 65.735 -17.841 1.763 1.00 88.60 O
ANISOU 2676 O THR B 81 14301 9351 10012 1277 3972 1080 O
ATOM 2677 CB THR B 81 65.185 -14.793 0.516 1.00 81.94 C
ANISOU 2677 CB THR B 81 13763 8451 8917 1187 4055 1299 C
ATOM 2678 OG1 THR B 81 64.954 -13.458 0.985 1.00 81.91 O
ANISOU 2678 OG1 THR B 81 13660 8446 9015 1191 4003 1387 O
ATOM 2679 CG2 THR B 81 63.860 -15.545 0.486 1.00 55.67 C
ANISOU 2679 CG2 THR B 81 10542 5233 5379 1215 3756 1270 C
ATOM 2680 N ASN B 82 66.977 -17.266 -0.015 1.00 85.04 N
ANISOU 2680 N ASN B 82 14160 8747 9404 1176 4428 1115 N
ATOM 2681 CA ASN B 82 67.095 -18.652 -0.443 1.00 76.94 C
ANISOU 2681 CA ASN B 82 13251 7710 8273 1183 4472 1029 C
ATOM 2682 C ASN B 82 67.916 -19.481 0.528 1.00 82.72 C
ANISOU 2682 C ASN B 82 13686 8439 9306 1226 4515 968 C
ATOM 2683 O ASN B 82 67.656 -20.678 0.679 1.00 99.97 O
ANISOU 2683 O ASN B 82 15890 10647 11449 1257 4424 906 O
ATOM 2684 CB ASN B 82 67.665 -18.719 -1.853 1.00 87.60 C
ANISOU 2684 CB ASN B 82 14906 8971 9407 1117 4761 1025 C
ATOM 2685 CG ASN B 82 66.695 -18.178 -2.882 1.00111.80 C
ANISOU 2685 CG ASN B 82 18328 12053 12100 1072 4660 1091 C
ATOM 2686 OD1 ASN B 82 65.484 -18.139 -2.646 1.00116.45 O
ANISOU 2686 OD1 ASN B 82 18956 12727 12562 1095 4351 1113 O
ATOM 2687 ND2 ASN B 82 67.216 -17.747 -4.023 1.00126.52 N
ANISOU 2687 ND2 ASN B 82 20453 13836 13782 1003 4918 1131 N
ATOM 2688 N TYR B 83 68.907 -18.888 1.193 1.00 78.63 N
ANISOU 2688 N TYR B 83 12897 7890 9089 1222 4646 988 N
ATOM 2689 CA TYR B 83 69.629 -19.669 2.190 1.00 79.05 C
ANISOU 2689 CA TYR B 83 12659 7962 9413 1258 4638 941 C
ATOM 2690 C TYR B 83 68.682 -20.069 3.319 1.00 69.41 C
ANISOU 2690 C TYR B 83 11308 6844 8222 1317 4299 947 C
ATOM 2691 O TYR B 83 68.655 -21.234 3.749 1.00 65.32 O
ANISOU 2691 O TYR B 83 10736 6357 7727 1351 4217 903 O
ATOM 2692 CB TYR B 83 70.821 -18.872 2.732 1.00 83.31 C
ANISOU 2692 CB TYR B 83 12918 8463 10272 1229 4813 958 C
ATOM 2693 CG TYR B 83 72.085 -18.968 1.891 1.00 91.50 C
ANISOU 2693 CG TYR B 83 13977 9408 11381 1176 5188 915 C
ATOM 2694 CD1 TYR B 83 72.097 -19.665 0.687 1.00 94.71 C
ANISOU 2694 CD1 TYR B 83 14673 9768 11545 1160 5360 873 C
ATOM 2695 CD2 TYR B 83 73.265 -18.347 2.295 1.00 98.37 C
ANISOU 2695 CD2 TYR B 83 14574 10237 12564 1136 5381 909 C
ATOM 2696 CE1 TYR B 83 73.249 -19.742 -0.092 1.00 96.97 C
ANISOU 2696 CE1 TYR B 83 14980 9971 11893 1112 5731 827 C
ATOM 2697 CE2 TYR B 83 74.421 -18.424 1.525 1.00105.36 C
ANISOU 2697 CE2 TYR B 83 15456 11041 13537 1085 5746 860 C
ATOM 2698 CZ TYR B 83 74.407 -19.121 0.332 1.00 99.58 C
ANISOU 2698 CZ TYR B 83 15018 10266 12553 1075 5928 821 C
ATOM 2699 OH TYR B 83 75.553 -19.195 -0.432 1.00 94.68 O
ANISOU 2699 OH TYR B 83 14394 9565 12015 1024 6316 766 O
ATOM 2700 N PHE B 84 67.849 -19.131 3.777 1.00 76.44 N
ANISOU 2700 N PHE B 84 12163 7784 9096 1329 4110 1002 N
ATOM 2701 CA PHE B 84 66.857 -19.505 4.784 1.00 74.71 C
ANISOU 2701 CA PHE B 84 11840 7666 8881 1380 3808 1002 C
ATOM 2702 C PHE B 84 65.865 -20.541 4.251 1.00 83.39 C
ANISOU 2702 C PHE B 84 13161 8797 9728 1390 3681 957 C
ATOM 2703 O PHE B 84 65.438 -21.437 4.993 1.00104.03 O
ANISOU 2703 O PHE B 84 15691 11463 12371 1421 3519 932 O
ATOM 2704 CB PHE B 84 66.142 -18.267 5.332 1.00 66.27 C
ANISOU 2704 CB PHE B 84 10690 6646 7844 1396 3658 1059 C
ATOM 2705 CG PHE B 84 66.966 -17.484 6.337 1.00 61.87 C
ANISOU 2705 CG PHE B 84 9853 6076 7579 1393 3702 1093 C
ATOM 2706 CD1 PHE B 84 67.573 -18.132 7.403 1.00 56.71 C
ANISOU 2706 CD1 PHE B 84 8962 5467 7119 1399 3646 1076 C
ATOM 2707 CD2 PHE B 84 67.110 -16.108 6.234 1.00 67.70 C
ANISOU 2707 CD2 PHE B 84 10572 6765 8386 1375 3791 1145 C
ATOM 2708 CE1 PHE B 84 68.320 -17.425 8.333 1.00 58.34 C
ANISOU 2708 CE1 PHE B 84 8910 5683 7574 1376 3666 1096 C
ATOM 2709 CE2 PHE B 84 67.854 -15.400 7.172 1.00 75.21 C
ANISOU 2709 CE2 PHE B 84 11265 7696 9614 1359 3831 1168 C
ATOM 2710 CZ PHE B 84 68.455 -16.061 8.217 1.00 70.99 C
ANISOU 2710 CZ PHE B 84 10491 7221 9262 1353 3759 1138 C
ATOM 2711 N LEU B 85 65.460 -20.424 2.980 1.00 68.93 N
ANISOU 2711 N LEU B 85 11624 6933 7634 1352 3748 950 N
ATOM 2712 CA LEU B 85 64.515 -21.397 2.431 1.00 58.40 C
ANISOU 2712 CA LEU B 85 10514 5625 6051 1345 3624 901 C
ATOM 2713 C LEU B 85 65.121 -22.793 2.359 1.00 66.94 C
ANISOU 2713 C LEU B 85 11623 6650 7163 1356 3735 834 C
ATOM 2714 O LEU B 85 64.420 -23.791 2.578 1.00 64.50 O
ANISOU 2714 O LEU B 85 11366 6366 6774 1369 3590 791 O
ATOM 2715 CB LEU B 85 64.059 -20.968 1.037 1.00 61.34 C
ANISOU 2715 CB LEU B 85 11221 5973 6111 1290 3673 918 C
ATOM 2716 CG LEU B 85 63.195 -19.721 0.919 1.00 75.60 C
ANISOU 2716 CG LEU B 85 13075 7843 7808 1275 3523 996 C
ATOM 2717 CD1 LEU B 85 62.903 -19.399 -0.545 1.00 83.27 C
ANISOU 2717 CD1 LEU B 85 14418 8777 8445 1212 3582 1033 C
ATOM 2718 CD2 LEU B 85 61.905 -20.004 1.672 1.00 65.26 C
ANISOU 2718 CD2 LEU B 85 11672 6647 6476 1301 3217 984 C
ATOM 2719 N VAL B 86 66.424 -22.884 2.078 1.00 80.67 N
ANISOU 2719 N VAL B 86 13316 8309 9024 1348 4003 822 N
ATOM 2720 CA VAL B 86 67.101 -24.178 2.136 1.00 75.25 C
ANISOU 2720 CA VAL B 86 12609 7577 8405 1370 4121 759 C
ATOM 2721 C VAL B 86 67.090 -24.718 3.559 1.00 73.08 C
ANISOU 2721 C VAL B 86 12060 7363 8344 1420 3950 771 C
ATOM 2722 O VAL B 86 66.944 -25.927 3.775 1.00 64.49 O
ANISOU 2722 O VAL B 86 11007 6265 7232 1447 3910 729 O
ATOM 2723 CB VAL B 86 68.526 -24.089 1.553 1.00 66.98 C
ANISOU 2723 CB VAL B 86 11536 6450 7465 1350 4461 735 C
ATOM 2724 CG1 VAL B 86 69.522 -23.574 2.577 1.00 63.80 C
ANISOU 2724 CG1 VAL B 86 10771 6071 7400 1364 4512 764 C
ATOM 2725 CG2 VAL B 86 68.948 -25.446 1.028 1.00 72.23 C
ANISOU 2725 CG2 VAL B 86 12328 7054 8063 1366 4616 646 C
ATOM 2726 N ASN B 87 67.263 -23.840 4.557 1.00 78.69 N
ANISOU 2726 N ASN B 87 12510 8134 9254 1430 3857 830 N
ATOM 2727 CA ASN B 87 67.162 -24.332 5.931 1.00 65.74 C
ANISOU 2727 CA ASN B 87 10641 6567 7770 1470 3676 848 C
ATOM 2728 C ASN B 87 65.765 -24.838 6.255 1.00 44.09 C
ANISOU 2728 C ASN B 87 7998 3876 4879 1485 3431 846 C
ATOM 2729 O ASN B 87 65.603 -25.853 6.950 1.00 43.04 O
ANISOU 2729 O ASN B 87 7817 3761 4775 1514 3344 837 O
ATOM 2730 CB ASN B 87 67.516 -23.230 6.928 1.00 70.67 C
ANISOU 2730 CB ASN B 87 10995 7254 8601 1466 3608 904 C
ATOM 2731 CG ASN B 87 67.811 -23.778 8.325 1.00 87.63 C
ANISOU 2731 CG ASN B 87 12896 9487 10914 1495 3479 914 C
ATOM 2732 OD1 ASN B 87 68.560 -24.740 8.492 1.00 92.45 O
ANISOU 2732 OD1 ASN B 87 13438 10090 11599 1519 3564 872 O
ATOM 2733 ND2 ASN B 87 67.179 -23.185 9.331 1.00101.10 N
ANISOU 2733 ND2 ASN B 87 14476 11281 12657 1497 3272 960 N
ATOM 2734 N LEU B 88 64.741 -24.161 5.741 1.00 49.68 N
ANISOU 2734 N LEU B 88 8845 4611 5421 1465 3327 849 N
ATOM 2735 CA LEU B 88 63.376 -24.635 5.948 1.00 62.73 C
ANISOU 2735 CA LEU B 88 10581 6323 6932 1466 3110 826 C
ATOM 2736 C LEU B 88 63.134 -25.986 5.278 1.00 85.32 C
ANISOU 2736 C LEU B 88 13673 9118 9627 1453 3153 760 C
ATOM 2737 O LEU B 88 62.520 -26.890 5.866 1.00 90.63 O
ANISOU 2737 O LEU B 88 14342 9807 10288 1463 3032 740 O
ATOM 2738 CB LEU B 88 62.412 -23.578 5.424 1.00 50.87 C
ANISOU 2738 CB LEU B 88 9172 4881 5277 1438 3007 838 C
ATOM 2739 CG LEU B 88 60.926 -23.863 5.472 1.00 43.96 C
ANISOU 2739 CG LEU B 88 8377 4091 4235 1417 2789 812 C
ATOM 2740 CD1 LEU B 88 60.215 -22.528 5.558 1.00 54.13 C
ANISOU 2740 CD1 LEU B 88 9604 5469 5495 1413 2673 861 C
ATOM 2741 CD2 LEU B 88 60.518 -24.618 4.219 1.00 48.37 C
ANISOU 2741 CD2 LEU B 88 9258 4596 4523 1367 2821 760 C
ATOM 2742 N SER B 89 63.690 -26.166 4.080 1.00 84.81 N
ANISOU 2742 N SER B 89 13818 8967 9439 1427 3349 725 N
ATOM 2743 CA SER B 89 63.605 -27.450 3.396 1.00 72.79 C
ANISOU 2743 CA SER B 89 12534 7363 7759 1415 3424 653 C
ATOM 2744 C SER B 89 64.388 -28.529 4.129 1.00 78.12 C
ANISOU 2744 C SER B 89 13081 7990 8609 1465 3507 643 C
ATOM 2745 O SER B 89 64.013 -29.703 4.093 1.00 86.71 O
ANISOU 2745 O SER B 89 14308 9028 9611 1469 3487 595 O
ATOM 2746 CB SER B 89 64.089 -27.300 1.958 1.00 75.27 C
ANISOU 2746 CB SER B 89 13105 7601 7893 1377 3636 616 C
ATOM 2747 OG SER B 89 63.097 -26.655 1.177 1.00 81.23 O
ANISOU 2747 OG SER B 89 14069 8397 8398 1325 3517 621 O
ATOM 2748 N LEU B 90 65.482 -28.149 4.786 1.00 82.16 N
ANISOU 2748 N LEU B 90 13335 8520 9360 1497 3601 686 N
ATOM 2749 CA LEU B 90 66.265 -29.092 5.578 1.00 71.92 C
ANISOU 2749 CA LEU B 90 11882 7210 8233 1549 3660 682 C
ATOM 2750 C LEU B 90 65.480 -29.574 6.793 1.00 57.49 C
ANISOU 2750 C LEU B 90 9961 5440 6442 1575 3435 724 C
ATOM 2751 O LEU B 90 65.499 -30.768 7.124 1.00 51.54 O
ANISOU 2751 O LEU B 90 9253 4643 5685 1609 3447 703 O
ATOM 2752 CB LEU B 90 67.564 -28.414 6.000 1.00 67.36 C
ANISOU 2752 CB LEU B 90 11031 6668 7895 1564 3786 705 C
ATOM 2753 CG LEU B 90 68.818 -29.235 6.214 1.00 61.26 C
ANISOU 2753 CG LEU B 90 10114 5871 7293 1616 3961 650 C
ATOM 2754 CD1 LEU B 90 69.386 -29.608 4.865 1.00 53.95 C
ANISOU 2754 CD1 LEU B 90 9382 4842 6275 1606 4231 565 C
ATOM 2755 CD2 LEU B 90 69.799 -28.409 7.021 1.00 62.84 C
ANISOU 2755 CD2 LEU B 90 9978 6148 7749 1624 3976 673 C
ATOM 2756 N ALA B 91 64.786 -28.654 7.470 1.00 59.68 N
ANISOU 2756 N ALA B 91 10115 5810 6751 1562 3245 779 N
ATOM 2757 CA ALA B 91 63.932 -29.058 8.583 1.00 55.67 C
ANISOU 2757 CA ALA B 91 9537 5359 6256 1580 3047 812 C
ATOM 2758 C ALA B 91 62.821 -29.971 8.081 1.00 58.01 C
ANISOU 2758 C ALA B 91 10086 5597 6356 1556 2989 753 C
ATOM 2759 O ALA B 91 62.445 -30.954 8.747 1.00 40.31 O
ANISOU 2759 O ALA B 91 7875 3330 4112 1576 2936 758 O
ATOM 2760 CB ALA B 91 63.353 -27.828 9.280 1.00 38.11 C
ANISOU 2760 CB ALA B 91 7140 3249 4090 1569 2875 858 C
ATOM 2761 N ASP B 92 62.303 -29.673 6.884 1.00 50.64 N
ANISOU 2761 N ASP B 92 9358 4642 5241 1506 3006 695 N
ATOM 2762 CA ASP B 92 61.238 -30.500 6.331 1.00 62.00 C
ANISOU 2762 CA ASP B 92 11053 6038 6468 1459 2940 625 C
ATOM 2763 C ASP B 92 61.749 -31.887 5.966 1.00 59.92 C
ANISOU 2763 C ASP B 92 10976 5635 6157 1475 3094 577 C
ATOM 2764 O ASP B 92 61.043 -32.878 6.169 1.00 47.14 O
ANISOU 2764 O ASP B 92 9496 3961 4453 1456 3035 541 O
ATOM 2765 CB ASP B 92 60.647 -29.851 5.079 1.00 71.89 C
ANISOU 2765 CB ASP B 92 12505 7312 7498 1394 2916 581 C
ATOM 2766 CG ASP B 92 59.788 -28.649 5.380 1.00 87.40 C
ANISOU 2766 CG ASP B 92 14334 9419 9454 1370 2735 618 C
ATOM 2767 OD1 ASP B 92 59.511 -28.386 6.569 1.00 98.24 O
ANISOU 2767 OD1 ASP B 92 15467 10877 10984 1397 2622 658 O
ATOM 2768 OD2 ASP B 92 59.395 -27.957 4.415 1.00 95.96 O
ANISOU 2768 OD2 ASP B 92 15566 10532 10361 1326 2711 612 O
ATOM 2769 N VAL B 93 62.975 -31.981 5.439 1.00 65.12 N
ANISOU 2769 N VAL B 93 11636 6233 6873 1505 3305 567 N
ATOM 2770 CA VAL B 93 63.547 -33.291 5.143 1.00 59.42 C
ANISOU 2770 CA VAL B 93 11056 5392 6128 1534 3469 508 C
ATOM 2771 C VAL B 93 63.811 -34.070 6.421 1.00 58.65 C
ANISOU 2771 C VAL B 93 10796 5294 6195 1599 3438 557 C
ATOM 2772 O VAL B 93 63.680 -35.296 6.437 1.00 63.66 O
ANISOU 2772 O VAL B 93 11586 5830 6772 1615 3483 509 O
ATOM 2773 CB VAL B 93 64.822 -33.152 4.297 1.00 54.77 C
ANISOU 2773 CB VAL B 93 10468 4761 5580 1555 3721 465 C
ATOM 2774 CG1 VAL B 93 65.682 -34.400 4.446 1.00 53.85 C
ANISOU 2774 CG1 VAL B 93 10343 4561 5556 1623 3887 406 C
ATOM 2775 CG2 VAL B 93 64.453 -32.918 2.844 1.00 61.53 C
ANISOU 2775 CG2 VAL B 93 11625 5571 6181 1488 3789 394 C
ATOM 2776 N LEU B 94 64.175 -33.389 7.509 1.00 58.53 N
ANISOU 2776 N LEU B 94 10487 5385 6368 1635 3360 647 N
ATOM 2777 CA LEU B 94 64.364 -34.098 8.773 1.00 50.48 C
ANISOU 2777 CA LEU B 94 9332 4383 5465 1697 3314 700 C
ATOM 2778 C LEU B 94 63.056 -34.696 9.266 1.00 46.80 C
ANISOU 2778 C LEU B 94 9018 3883 4881 1669 3170 717 C
ATOM 2779 O LEU B 94 62.963 -35.910 9.552 1.00 51.21 O
ANISOU 2779 O LEU B 94 9704 4351 5402 1697 3214 701 O
ATOM 2780 CB LEU B 94 64.887 -33.146 9.846 1.00 55.43 C
ANISOU 2780 CB LEU B 94 9637 5150 6275 1725 3230 783 C
ATOM 2781 CG LEU B 94 64.857 -33.855 11.211 1.00 61.09 C
ANISOU 2781 CG LEU B 94 10253 5903 7054 1785 3149 839 C
ATOM 2782 CD1 LEU B 94 65.776 -35.074 11.234 1.00 74.02 C
ANISOU 2782 CD1 LEU B 94 11897 7465 8763 1872 3286 773 C
ATOM 2783 CD2 LEU B 94 65.081 -32.924 12.420 1.00 59.42 C
ANISOU 2783 CD2 LEU B 94 9762 5847 6969 1799 3019 915 C
ATOM 2784 N ALA B 95 62.001 -33.872 9.272 1.00 41.98 N
ANISOU 2784 N ALA B 95 8403 3336 4209 1612 3009 723 N
ATOM 2785 CA ALA B 95 60.713 -34.374 9.724 1.00 50.10 C
ANISOU 2785 CA ALA B 95 9546 4342 5147 1574 2880 706 C
ATOM 2786 C ALA B 95 60.178 -35.441 8.782 1.00 63.87 C
ANISOU 2786 C ALA B 95 11627 5945 6695 1514 2941 607 C
ATOM 2787 O ALA B 95 59.696 -36.483 9.238 1.00 68.42 O
ANISOU 2787 O ALA B 95 12347 6425 7224 1503 2943 598 O
ATOM 2788 CB ALA B 95 59.723 -33.216 9.849 1.00 42.11 C
ANISOU 2788 CB ALA B 95 8407 3475 4119 1521 2700 689 C
ATOM 2789 N THR B 96 60.418 -35.284 7.483 1.00 67.17 N
ANISOU 2789 N THR B 96 12197 6330 6994 1478 3020 532 N
ATOM 2790 CA THR B 96 59.868 -36.209 6.505 1.00 62.60 C
ANISOU 2790 CA THR B 96 11964 5627 6193 1407 3056 421 C
ATOM 2791 C THR B 96 60.574 -37.550 6.583 1.00 55.92 C
ANISOU 2791 C THR B 96 11238 4633 5374 1459 3221 393 C
ATOM 2792 O THR B 96 59.931 -38.605 6.536 1.00 60.39 O
ANISOU 2792 O THR B 96 12045 5080 5821 1409 3209 327 O
ATOM 2793 CB THR B 96 59.992 -35.603 5.106 1.00 79.75 C
ANISOU 2793 CB THR B 96 14275 7817 8210 1363 3099 355 C
ATOM 2794 OG1 THR B 96 59.186 -34.421 5.031 1.00 82.27 O
ANISOU 2794 OG1 THR B 96 14503 8280 8475 1311 2926 377 O
ATOM 2795 CG2 THR B 96 59.532 -36.593 4.048 1.00 89.59 C
ANISOU 2795 CG2 THR B 96 15903 8933 9204 1288 3135 228 C
ATOM 2796 N ALA B 97 61.899 -37.525 6.727 1.00 64.68 N
ANISOU 2796 N ALA B 97 12170 5758 6649 1555 3370 426 N
ATOM 2797 CA ALA B 97 62.673 -38.756 6.739 1.00 63.42 C
ANISOU 2797 CA ALA B 97 12075 5483 6539 1626 3525 366 C
ATOM 2798 C ALA B 97 62.396 -39.574 7.991 1.00 57.56 C
ANISOU 2798 C ALA B 97 11293 4706 5870 1668 3463 420 C
ATOM 2799 O ALA B 97 62.273 -40.800 7.915 1.00 53.21 O
ANISOU 2799 O ALA B 97 10937 4010 5270 1676 3512 338 O
ATOM 2800 CB ALA B 97 64.166 -38.445 6.624 1.00 53.38 C
ANISOU 2800 CB ALA B 97 10570 4257 5453 1720 3686 361 C
ATOM 2801 N ILE B 98 62.292 -38.939 9.154 1.00 48.98 N
ANISOU 2801 N ILE B 98 9972 3743 4895 1694 3354 549 N
ATOM 2802 CA ILE B 98 62.264 -39.675 10.407 1.00 48.23 C
ANISOU 2802 CA ILE B 98 9817 3636 4871 1756 3321 606 C
ATOM 2803 C ILE B 98 60.872 -39.681 11.035 1.00 56.77 C
ANISOU 2803 C ILE B 98 11022 4713 5834 1667 3198 663 C
ATOM 2804 O ILE B 98 60.332 -40.745 11.339 1.00 75.47 O
ANISOU 2804 O ILE B 98 13582 6963 8129 1641 3208 623 O
ATOM 2805 CB ILE B 98 63.327 -39.138 11.390 1.00 65.47 C
ANISOU 2805 CB ILE B 98 11649 5962 7264 1866 3304 687 C
ATOM 2806 CG1 ILE B 98 64.720 -39.361 10.797 1.00 71.53 C
ANISOU 2806 CG1 ILE B 98 12301 6695 8183 1957 3442 593 C
ATOM 2807 CG2 ILE B 98 63.236 -39.866 12.709 1.00 71.30 C
ANISOU 2807 CG2 ILE B 98 12342 6695 8055 1937 3239 735 C
ATOM 2808 CD1 ILE B 98 65.852 -38.867 11.658 1.00 73.77 C
ANISOU 2808 CD1 ILE B 98 12234 7096 8698 2060 3411 627 C
ATOM 2809 N CYS B 99 60.270 -38.505 11.228 1.00 58.43 N
ANISOU 2809 N CYS B 99 11112 5031 6059 1621 3073 726 N
ATOM 2810 CA CYS B 99 59.009 -38.417 11.963 1.00 65.19 C
ANISOU 2810 CA CYS B 99 11961 5920 6890 1551 2925 716 C
ATOM 2811 C CYS B 99 57.830 -39.023 11.198 1.00 72.84 C
ANISOU 2811 C CYS B 99 13276 6725 7674 1423 2916 608 C
ATOM 2812 O CYS B 99 56.997 -39.719 11.791 1.00 78.16 O
ANISOU 2812 O CYS B 99 14052 7348 8299 1351 2887 566 O
ATOM 2813 CB CYS B 99 58.729 -36.960 12.324 1.00 67.61 C
ANISOU 2813 CB CYS B 99 11970 6410 7308 1556 2770 728 C
ATOM 2814 SG CYS B 99 60.052 -36.217 13.315 1.00 76.97 S
ANISOU 2814 SG CYS B 99 12786 7778 8679 1662 2756 847 S
ATOM 2815 N LEU B 100 57.741 -38.788 9.886 1.00 81.22 N
ANISOU 2815 N LEU B 100 14467 7779 8613 1359 2912 511 N
ATOM 2816 CA LEU B 100 56.565 -39.227 9.130 1.00 77.29 C
ANISOU 2816 CA LEU B 100 14256 7215 7896 1199 2841 381 C
ATOM 2817 C LEU B 100 56.270 -40.719 9.191 1.00 68.66 C
ANISOU 2817 C LEU B 100 13487 5900 6700 1135 2924 319 C
ATOM 2818 O LEU B 100 55.126 -41.088 9.519 1.00 73.35 O
ANISOU 2818 O LEU B 100 14230 6443 7195 994 2851 270 O
ATOM 2819 CB LEU B 100 56.723 -38.793 7.668 1.00 72.51 C
ANISOU 2819 CB LEU B 100 13761 6643 7147 1162 2830 293 C
ATOM 2820 CG LEU B 100 55.643 -39.191 6.650 1.00 65.54 C
ANISOU 2820 CG LEU B 100 13210 5708 5986 995 2728 152 C
ATOM 2821 CD1 LEU B 100 54.246 -38.846 7.107 1.00 49.92 C
ANISOU 2821 CD1 LEU B 100 11200 3850 3919 853 2540 151 C
ATOM 2822 CD2 LEU B 100 55.915 -38.511 5.312 1.00 81.66 C
ANISOU 2822 CD2 LEU B 100 15321 7814 7891 991 2712 100 C
ATOM 2823 N PRO B 101 57.210 -41.618 8.913 1.00 65.27 N
ANISOU 2823 N PRO B 101 13145 5355 6300 1212 3059 289 N
ATOM 2824 CA PRO B 101 56.858 -43.050 8.987 1.00 68.74 C
ANISOU 2824 CA PRO B 101 13840 5580 6698 1144 3080 184 C
ATOM 2825 C PRO B 101 56.359 -43.485 10.357 1.00 61.27 C
ANISOU 2825 C PRO B 101 12829 4592 5858 1120 3038 262 C
ATOM 2826 O PRO B 101 55.400 -44.276 10.469 1.00 57.39 O
ANISOU 2826 O PRO B 101 12530 3924 5353 952 2948 195 O
ATOM 2827 CB PRO B 101 58.176 -43.749 8.606 1.00 72.62 C
ANISOU 2827 CB PRO B 101 14303 5996 7292 1286 3217 143 C
ATOM 2828 CG PRO B 101 59.046 -42.667 7.978 1.00 67.44 C
ANISOU 2828 CG PRO B 101 13459 5502 6662 1372 3281 187 C
ATOM 2829 CD PRO B 101 58.628 -41.378 8.601 1.00 59.91 C
ANISOU 2829 CD PRO B 101 12286 4733 5745 1359 3178 323 C
ATOM 2830 N ALA B 102 56.948 -42.919 11.414 1.00 67.18 N
ANISOU 2830 N ALA B 102 13278 5509 6737 1255 3067 409 N
ATOM 2831 CA ALA B 102 56.528 -43.258 12.770 1.00 72.80 C
ANISOU 2831 CA ALA B 102 13863 6226 7571 1230 2986 487 C
ATOM 2832 C ALA B 102 55.110 -42.783 13.048 1.00 59.95 C
ANISOU 2832 C ALA B 102 12219 4654 5907 1025 2846 513 C
ATOM 2833 O ALA B 102 54.297 -43.514 13.632 1.00 63.43 O
ANISOU 2833 O ALA B 102 12690 5000 6409 849 2747 560 O
ATOM 2834 CB ALA B 102 57.497 -42.639 13.779 1.00 78.37 C
ANISOU 2834 CB ALA B 102 14236 7136 8405 1417 3008 603 C
ATOM 2835 N SER B 103 54.789 -41.567 12.612 1.00 64.34 N
ANISOU 2835 N SER B 103 12676 5387 6382 1017 2813 503 N
ATOM 2836 CA SER B 103 53.450 -41.044 12.833 1.00 69.10 C
ANISOU 2836 CA SER B 103 13139 6152 6963 791 2631 557 C
ATOM 2837 C SER B 103 52.404 -41.824 12.055 1.00 75.87 C
ANISOU 2837 C SER B 103 14310 6823 7693 538 2559 492 C
ATOM 2838 O SER B 103 51.294 -42.042 12.552 1.00 87.26 O
ANISOU 2838 O SER B 103 15656 8302 9199 314 2431 537 O
ATOM 2839 CB SER B 103 53.397 -39.566 12.448 1.00 63.67 C
ANISOU 2839 CB SER B 103 12196 5737 6258 840 2543 541 C
ATOM 2840 OG SER B 103 52.069 -39.093 12.549 1.00 63.68 O
ANISOU 2840 OG SER B 103 12088 5901 6208 634 2387 586 O
ATOM 2841 N LEU B 104 52.745 -42.294 10.855 1.00 70.88 N
ANISOU 2841 N LEU B 104 13968 6029 6936 565 2598 316 N
ATOM 2842 CA LEU B 104 51.791 -43.121 10.126 1.00 62.54 C
ANISOU 2842 CA LEU B 104 13134 4821 5809 322 2450 168 C
ATOM 2843 C LEU B 104 51.518 -44.416 10.883 1.00 60.49 C
ANISOU 2843 C LEU B 104 12962 4300 5721 199 2456 205 C
ATOM 2844 O LEU B 104 50.355 -44.808 11.064 1.00 61.31 O
ANISOU 2844 O LEU B 104 13030 4384 5882 -72 2304 199 O
ATOM 2845 CB LEU B 104 52.274 -43.391 8.698 1.00 54.61 C
ANISOU 2845 CB LEU B 104 12467 3683 4601 384 2504 -44 C
ATOM 2846 CG LEU B 104 51.587 -44.542 7.962 1.00 78.58 C
ANISOU 2846 CG LEU B 104 15812 6470 7575 171 2383 -234 C
ATOM 2847 CD1 LEU B 104 50.113 -44.215 7.753 1.00 76.16 C
ANISOU 2847 CD1 LEU B 104 15389 6320 7229 -111 2087 -257 C
ATOM 2848 CD2 LEU B 104 52.262 -44.755 6.624 1.00 60.04 C
ANISOU 2848 CD2 LEU B 104 13820 3994 4998 279 2487 -446 C
ATOM 2849 N LEU B 105 52.576 -45.077 11.377 1.00 69.47 N
ANISOU 2849 N LEU B 105 14199 5229 6966 395 2630 254 N
ATOM 2850 CA LEU B 105 52.329 -46.327 12.096 1.00 76.87 C
ANISOU 2850 CA LEU B 105 15172 5982 8054 280 2601 296 C
ATOM 2851 C LEU B 105 51.526 -46.086 13.362 1.00 92.34 C
ANISOU 2851 C LEU B 105 16874 8084 10127 129 2531 489 C
ATOM 2852 O LEU B 105 50.678 -46.913 13.728 1.00102.92 O
ANISOU 2852 O LEU B 105 18275 9274 11556 -112 2470 514 O
ATOM 2853 CB LEU B 105 53.637 -47.021 12.472 1.00 67.29 C
ANISOU 2853 CB LEU B 105 13915 4719 6933 531 2711 312 C
ATOM 2854 CG LEU B 105 54.193 -47.983 11.440 1.00 81.04 C
ANISOU 2854 CG LEU B 105 15915 6242 8636 584 2767 132 C
ATOM 2855 CD1 LEU B 105 55.361 -48.725 12.040 1.00 85.50 C
ANISOU 2855 CD1 LEU B 105 16387 6744 9354 801 2841 195 C
ATOM 2856 CD2 LEU B 105 53.095 -48.942 11.018 1.00 93.33 C
ANISOU 2856 CD2 LEU B 105 17728 7544 10190 295 2652 18 C
ATOM 2857 N VAL B 106 51.755 -44.956 14.027 1.00 89.76 N
ANISOU 2857 N VAL B 106 16240 8063 9802 255 2542 609 N
ATOM 2858 CA VAL B 106 50.994 -44.654 15.233 1.00 78.53 C
ANISOU 2858 CA VAL B 106 14542 6825 8470 122 2483 762 C
ATOM 2859 C VAL B 106 49.529 -44.397 14.896 1.00 74.15 C
ANISOU 2859 C VAL B 106 14001 6285 7886 -198 2401 767 C
ATOM 2860 O VAL B 106 48.627 -44.949 15.538 1.00 84.96 O
ANISOU 2860 O VAL B 106 15329 7595 9357 -440 2381 834 O
ATOM 2861 CB VAL B 106 51.628 -43.479 15.994 1.00 73.85 C
ANISOU 2861 CB VAL B 106 13604 6556 7899 340 2488 837 C
ATOM 2862 CG1 VAL B 106 50.644 -42.934 17.011 1.00 75.18 C
ANISOU 2862 CG1 VAL B 106 13495 6944 8124 181 2424 951 C
ATOM 2863 CG2 VAL B 106 52.907 -43.951 16.674 1.00 67.20 C
ANISOU 2863 CG2 VAL B 106 12734 5664 7134 584 2543 868 C
ATOM 2864 N ASP B 107 49.261 -43.586 13.868 1.00 68.56 N
ANISOU 2864 N ASP B 107 13234 5751 7066 -199 2295 634 N
ATOM 2865 CA ASP B 107 47.868 -43.287 13.555 1.00 77.37 C
ANISOU 2865 CA ASP B 107 14188 7009 8199 -468 2114 567 C
ATOM 2866 C ASP B 107 47.115 -44.518 13.068 1.00 86.24 C
ANISOU 2866 C ASP B 107 15517 7870 9380 -739 2021 439 C
ATOM 2867 O ASP B 107 45.901 -44.610 13.277 1.00105.02 O
ANISOU 2867 O ASP B 107 17724 10307 11871 -1012 1909 429 O
ATOM 2868 CB ASP B 107 47.772 -42.174 12.506 1.00 88.16 C
ANISOU 2868 CB ASP B 107 15484 8595 9419 -392 1983 461 C
ATOM 2869 CG ASP B 107 48.140 -40.800 13.062 1.00 94.35 C
ANISOU 2869 CG ASP B 107 15989 9668 10192 -201 2036 587 C
ATOM 2870 OD1 ASP B 107 48.279 -40.652 14.294 1.00 92.27 O
ANISOU 2870 OD1 ASP B 107 15551 9475 10034 -159 2146 740 O
ATOM 2871 OD2 ASP B 107 48.270 -39.854 12.255 1.00 97.58 O
ANISOU 2871 OD2 ASP B 107 16372 10228 10477 -100 1961 530 O
ATOM 2872 N ILE B 108 47.794 -45.471 12.428 1.00 82.59 N
ANISOU 2872 N ILE B 108 15405 7111 8864 -677 2071 328 N
ATOM 2873 CA ILE B 108 47.085 -46.669 11.967 1.00 94.73 C
ANISOU 2873 CA ILE B 108 17157 8370 10467 -945 1975 189 C
ATOM 2874 C ILE B 108 46.864 -47.669 13.103 1.00 93.68 C
ANISOU 2874 C ILE B 108 17049 8015 10529 -1092 2086 336 C
ATOM 2875 O ILE B 108 45.757 -48.195 13.280 1.00 92.43 O
ANISOU 2875 O ILE B 108 16830 7786 10505 -1412 2003 316 O
ATOM 2876 CB ILE B 108 47.810 -47.332 10.777 1.00 92.86 C
ANISOU 2876 CB ILE B 108 17313 7880 10090 -838 1985 -19 C
ATOM 2877 CG1 ILE B 108 49.210 -47.801 11.180 1.00 91.91 C
ANISOU 2877 CG1 ILE B 108 17369 7559 9993 -546 2219 57 C
ATOM 2878 CG2 ILE B 108 47.829 -46.400 9.563 1.00 82.25 C
ANISOU 2878 CG2 ILE B 108 15991 6744 8515 -756 1862 -168 C
ATOM 2879 CD1 ILE B 108 49.817 -48.791 10.218 1.00 87.68 C
ANISOU 2879 CD1 ILE B 108 17235 6687 9392 -480 2270 -153 C
ATOM 2880 N THR B 109 47.906 -47.944 13.893 1.00 85.06 N
ANISOU 2880 N THR B 109 16049 6807 9464 -865 2268 492 N
ATOM 2881 CA THR B 109 47.855 -48.994 14.906 1.00 80.15 C
ANISOU 2881 CA THR B 109 15444 6017 8991 -945 2335 618 C
ATOM 2882 C THR B 109 47.434 -48.520 16.295 1.00 94.51 C
ANISOU 2882 C THR B 109 16943 8086 10882 -994 2385 836 C
ATOM 2883 O THR B 109 47.142 -49.365 17.150 1.00114.51 O
ANISOU 2883 O THR B 109 19461 10522 13526 -1114 2417 938 O
ATOM 2884 CB THR B 109 49.221 -49.692 14.998 1.00 76.45 C
ANISOU 2884 CB THR B 109 15094 5435 8517 -629 2402 609 C
ATOM 2885 OG1 THR B 109 50.175 -48.812 15.608 1.00 83.43 O
ANISOU 2885 OG1 THR B 109 15762 6584 9355 -323 2461 717 O
ATOM 2886 CG2 THR B 109 49.706 -50.068 13.610 1.00 76.28 C
ANISOU 2886 CG2 THR B 109 15359 5218 8404 -549 2388 376 C
ATOM 2887 N GLU B 110 47.384 -47.211 16.550 1.00 86.13 N
ANISOU 2887 N GLU B 110 15631 7343 9753 -903 2393 904 N
ATOM 2888 CA GLU B 110 47.095 -46.686 17.890 1.00 88.75 C
ANISOU 2888 CA GLU B 110 15648 7942 10132 -904 2441 1075 C
ATOM 2889 C GLU B 110 48.068 -47.212 18.940 1.00102.41 C
ANISOU 2889 C GLU B 110 17364 9665 11882 -678 2474 1181 C
ATOM 2890 O GLU B 110 47.738 -47.263 20.129 1.00116.15 O
ANISOU 2890 O GLU B 110 18952 11514 13664 -741 2505 1319 O
ATOM 2891 CB GLU B 110 45.673 -47.051 18.334 1.00 95.62 C
ANISOU 2891 CB GLU B 110 16429 8776 11126 -1295 2467 1128 C
ATOM 2892 CG GLU B 110 44.580 -46.834 17.324 1.00108.07 C
ANISOU 2892 CG GLU B 110 17974 10338 12749 -1579 2362 976 C
ATOM 2893 CD GLU B 110 44.429 -45.380 16.962 1.00128.91 C
ANISOU 2893 CD GLU B 110 20307 13358 15315 -1447 2260 913 C
ATOM 2894 OE1 GLU B 110 44.831 -44.525 17.782 1.00128.36 O
ANISOU 2894 OE1 GLU B 110 20070 13509 15193 -1266 2359 1051 O
ATOM 2895 OE2 GLU B 110 43.901 -45.094 15.866 1.00149.40 O
ANISOU 2895 OE2 GLU B 110 22844 16020 17899 -1526 2067 726 O
ATOM 2896 N SER B 111 49.293 -47.554 18.546 1.00 99.81 N
ANISOU 2896 N SER B 111 17188 9216 11518 -411 2470 1120 N
ATOM 2897 CA SER B 111 50.256 -48.020 19.532 1.00 96.38 C
ANISOU 2897 CA SER B 111 16740 8766 11114 -201 2476 1225 C
ATOM 2898 C SER B 111 51.649 -47.572 19.130 1.00 80.66 C
ANISOU 2898 C SER B 111 14739 6829 9080 141 2481 1154 C
ATOM 2899 O SER B 111 51.908 -47.228 17.973 1.00 82.32 O
ANISOU 2899 O SER B 111 15031 7014 9233 208 2505 1015 O
ATOM 2900 CB SER B 111 50.226 -49.548 19.694 1.00109.43 C
ANISOU 2900 CB SER B 111 18638 10089 12852 -301 2479 1258 C
ATOM 2901 OG SER B 111 50.828 -50.200 18.588 1.00118.51 O
ANISOU 2901 OG SER B 111 20027 10993 14006 -206 2482 1107 O
ATOM 2902 N TRP B 112 52.549 -47.602 20.105 1.00 74.07 N
ANISOU 2902 N TRP B 112 13814 6058 8271 345 2461 1254 N
ATOM 2903 CA TRP B 112 53.943 -47.248 19.900 1.00 71.47 C
ANISOU 2903 CA TRP B 112 13440 5774 7941 660 2473 1205 C
ATOM 2904 C TRP B 112 54.764 -48.523 19.900 1.00 72.08 C
ANISOU 2904 C TRP B 112 13719 5573 8096 777 2471 1215 C
ATOM 2905 O TRP B 112 54.784 -49.252 20.897 1.00 81.42 O
ANISOU 2905 O TRP B 112 14946 6660 9328 755 2415 1351 O
ATOM 2906 CB TRP B 112 54.437 -46.283 20.977 1.00 69.06 C
ANISOU 2906 CB TRP B 112 12873 5739 7628 806 2425 1298 C
ATOM 2907 CG TRP B 112 55.836 -45.805 20.732 1.00 78.15 C
ANISOU 2907 CG TRP B 112 13942 6950 8801 1102 2443 1245 C
ATOM 2908 CD1 TRP B 112 56.969 -46.309 21.278 1.00 84.13 C
ANISOU 2908 CD1 TRP B 112 14715 7623 9628 1303 2405 1305 C
ATOM 2909 CD2 TRP B 112 56.251 -44.742 19.853 1.00 79.00 C
ANISOU 2909 CD2 TRP B 112 13933 7207 8876 1216 2509 1131 C
ATOM 2910 NE1 TRP B 112 58.067 -45.622 20.816 1.00 90.28 N
ANISOU 2910 NE1 TRP B 112 15365 8502 10436 1524 2448 1234 N
ATOM 2911 CE2 TRP B 112 57.655 -44.656 19.938 1.00 71.65 C
ANISOU 2911 CE2 TRP B 112 12932 6286 8006 1472 2529 1130 C
ATOM 2912 CE3 TRP B 112 55.573 -43.861 19.002 1.00 75.18 C
ANISOU 2912 CE3 TRP B 112 13399 6842 8324 1119 2544 1041 C
ATOM 2913 CZ2 TRP B 112 58.399 -43.727 19.206 1.00 47.74 C
ANISOU 2913 CZ2 TRP B 112 9779 3390 4969 1617 2614 1047 C
ATOM 2914 CZ3 TRP B 112 56.311 -42.939 18.279 1.00 67.65 C
ANISOU 2914 CZ3 TRP B 112 12354 6003 7348 1283 2615 958 C
ATOM 2915 CH2 TRP B 112 57.710 -42.880 18.385 1.00 55.97 C
ANISOU 2915 CH2 TRP B 112 10802 4538 5924 1522 2669 964 C
ATOM 2916 N LEU B 113 55.415 -48.799 18.777 1.00 72.73 N
ANISOU 2916 N LEU B 113 13928 5520 8187 897 2533 1073 N
ATOM 2917 CA LEU B 113 56.123 -50.054 18.586 1.00 83.56 C
ANISOU 2917 CA LEU B 113 15486 6607 9658 999 2533 1049 C
ATOM 2918 C LEU B 113 57.634 -49.847 18.519 1.00 89.45 C
ANISOU 2918 C LEU B 113 16117 7398 10471 1316 2554 1023 C
ATOM 2919 O LEU B 113 58.374 -50.809 18.274 1.00 97.51 O
ANISOU 2919 O LEU B 113 17251 8194 11603 1439 2555 985 O
ATOM 2920 CB LEU B 113 55.603 -50.743 17.318 1.00 75.53 C
ANISOU 2920 CB LEU B 113 14720 5359 8620 853 2585 882 C
ATOM 2921 CG LEU B 113 54.091 -51.006 17.285 1.00 71.28 C
ANISOU 2921 CG LEU B 113 14288 4746 8049 507 2550 890 C
ATOM 2922 CD1 LEU B 113 53.631 -51.411 15.897 1.00 65.37 C
ANISOU 2922 CD1 LEU B 113 13774 3808 7254 369 2576 687 C
ATOM 2923 CD2 LEU B 113 53.697 -52.067 18.304 1.00 83.64 C
ANISOU 2923 CD2 LEU B 113 15928 6134 9718 379 2494 1042 C
ATOM 2924 N PHE B 114 58.110 -48.620 18.769 1.00 77.51 N
ANISOU 2924 N PHE B 114 14363 6166 8923 1442 2564 1044 N
ATOM 2925 CA PHE B 114 59.508 -48.251 18.574 1.00 74.97 C
ANISOU 2925 CA PHE B 114 13887 5916 8682 1707 2597 1007 C
ATOM 2926 C PHE B 114 60.334 -48.153 19.862 1.00 75.94 C
ANISOU 2926 C PHE B 114 13838 6110 8904 1872 2471 1148 C
ATOM 2927 O PHE B 114 61.523 -47.835 19.780 1.00 65.86 O
ANISOU 2927 O PHE B 114 12398 4892 7735 2080 2471 1120 O
ATOM 2928 CB PHE B 114 59.596 -46.920 17.818 1.00 76.70 C
ANISOU 2928 CB PHE B 114 13956 6379 8807 1731 2699 921 C
ATOM 2929 CG PHE B 114 58.856 -46.906 16.498 1.00 87.83 C
ANISOU 2929 CG PHE B 114 15556 7724 10093 1583 2800 782 C
ATOM 2930 CD1 PHE B 114 59.265 -47.716 15.451 1.00 70.25 C
ANISOU 2930 CD1 PHE B 114 13511 5293 7886 1617 2880 652 C
ATOM 2931 CD2 PHE B 114 57.754 -46.082 16.304 1.00 99.38 C
ANISOU 2931 CD2 PHE B 114 17015 9323 11424 1411 2796 772 C
ATOM 2932 CE1 PHE B 114 58.602 -47.707 14.244 1.00 66.27 C
ANISOU 2932 CE1 PHE B 114 13212 4725 7245 1477 2947 515 C
ATOM 2933 CE2 PHE B 114 57.083 -46.076 15.088 1.00 89.90 C
ANISOU 2933 CE2 PHE B 114 16016 8041 10102 1274 2850 644 C
ATOM 2934 CZ PHE B 114 57.512 -46.893 14.062 1.00 76.08 C
ANISOU 2934 CZ PHE B 114 14476 6088 8343 1305 2923 515 C
ATOM 2935 N GLY B 115 59.748 -48.386 21.041 1.00 84.31 N
ANISOU 2935 N GLY B 115 14927 7172 9935 1775 2357 1298 N
ATOM 2936 CA GLY B 115 60.482 -48.379 22.294 1.00 90.06 C
ANISOU 2936 CA GLY B 115 15551 7939 10727 1920 2211 1438 C
ATOM 2937 C GLY B 115 60.598 -47.023 22.985 1.00 98.97 C
ANISOU 2937 C GLY B 115 16440 9378 11787 1962 2169 1481 C
ATOM 2938 O GLY B 115 60.203 -45.971 22.470 1.00118.71 O
ANISOU 2938 O GLY B 115 18816 12080 14209 1902 2261 1401 O
ATOM 2939 N HIS B 116 61.186 -47.066 24.188 1.00104.02 N
ANISOU 2939 N HIS B 116 17025 10037 12461 2074 2013 1612 N
ATOM 2940 CA HIS B 116 61.180 -45.908 25.082 1.00114.88 C
ANISOU 2940 CA HIS B 116 18217 11677 13753 2089 1944 1668 C
ATOM 2941 C HIS B 116 62.023 -44.771 24.502 1.00107.13 C
ANISOU 2941 C HIS B 116 16990 10880 12835 2237 1995 1557 C
ATOM 2942 O HIS B 116 61.602 -43.597 24.466 1.00108.14 O
ANISOU 2942 O HIS B 116 16972 11240 12877 2175 2051 1518 O
ATOM 2943 CB HIS B 116 61.733 -46.335 26.447 1.00135.99 C
ANISOU 2943 CB HIS B 116 20936 14291 16442 2189 1744 1831 C
ATOM 2944 CG HIS B 116 60.791 -47.173 27.265 1.00153.67 C
ANISOU 2944 CG HIS B 116 23395 16417 18575 2006 1703 1977 C
ATOM 2945 ND1 HIS B 116 60.478 -48.473 26.927 1.00159.07 N
ANISOU 2945 ND1 HIS B 116 24301 16824 19312 1929 1729 2007 N
ATOM 2946 CD2 HIS B 116 60.131 -46.920 28.420 1.00157.05 C
ANISOU 2946 CD2 HIS B 116 23856 16962 18853 1880 1645 2103 C
ATOM 2947 CE1 HIS B 116 59.650 -48.977 27.824 1.00159.46 C
ANISOU 2947 CE1 HIS B 116 24504 16827 19256 1753 1696 2156 C
ATOM 2948 NE2 HIS B 116 59.425 -48.055 28.743 1.00158.72 N
ANISOU 2948 NE2 HIS B 116 24298 16976 19031 1719 1651 2216 N
ATOM 2949 N ALA B 117 63.233 -45.112 24.047 1.00 96.24 N
ANISOU 2949 N ALA B 117 15544 9391 11632 2426 1975 1504 N
ATOM 2950 CA ALA B 117 64.161 -44.087 23.594 1.00 75.13 C
ANISOU 2950 CA ALA B 117 12608 6882 9056 2551 2011 1413 C
ATOM 2951 C ALA B 117 63.591 -43.354 22.392 1.00 54.01 C
ANISOU 2951 C ALA B 117 9903 4331 6289 2434 2219 1299 C
ATOM 2952 O ALA B 117 63.646 -42.122 22.318 1.00 48.13 O
ANISOU 2952 O ALA B 117 8972 3807 5509 2425 2258 1273 O
ATOM 2953 CB ALA B 117 65.518 -44.705 23.266 1.00 80.79 C
ANISOU 2953 CB ALA B 117 13236 7436 10022 2750 1955 1355 C
ATOM 2954 N LEU B 118 63.036 -44.101 21.431 1.00 56.73 N
ANISOU 2954 N LEU B 118 10444 4519 6590 2340 2342 1233 N
ATOM 2955 CA LEU B 118 62.446 -43.454 20.265 1.00 67.33 C
ANISOU 2955 CA LEU B 118 11803 5955 7822 2227 2515 1133 C
ATOM 2956 C LEU B 118 61.180 -42.699 20.655 1.00 69.57 C
ANISOU 2956 C LEU B 118 12087 6399 7948 2065 2509 1165 C
ATOM 2957 O LEU B 118 60.858 -41.679 20.036 1.00 76.12 O
ANISOU 2957 O LEU B 118 12831 7386 8706 2017 2599 1106 O
ATOM 2958 CB LEU B 118 62.163 -44.484 19.168 1.00 82.01 C
ANISOU 2958 CB LEU B 118 13903 7588 9669 2166 2620 1041 C
ATOM 2959 CG LEU B 118 63.406 -45.166 18.577 1.00 84.25 C
ANISOU 2959 CG LEU B 118 14161 7717 10132 2327 2655 964 C
ATOM 2960 CD1 LEU B 118 63.055 -45.994 17.348 1.00 55.35 C
ANISOU 2960 CD1 LEU B 118 10746 3859 6425 2252 2783 844 C
ATOM 2961 CD2 LEU B 118 64.452 -44.106 18.230 1.00 76.67 C
ANISOU 2961 CD2 LEU B 118 12920 6943 9270 2430 2703 920 C
ATOM 2962 N CYS B 119 60.508 -43.126 21.734 1.00 73.56 N
ANISOU 2962 N CYS B 119 12661 6873 8416 1982 2393 1261 N
ATOM 2963 CA CYS B 119 59.358 -42.371 22.218 1.00 73.79 C
ANISOU 2963 CA CYS B 119 12624 7068 8345 1822 2366 1282 C
ATOM 2964 C CYS B 119 59.768 -40.987 22.667 1.00 77.06 C
ANISOU 2964 C CYS B 119 12786 7731 8763 1914 2340 1280 C
ATOM 2965 O CYS B 119 58.981 -40.035 22.569 1.00 79.86 O
ANISOU 2965 O CYS B 119 13027 8242 9074 1817 2352 1236 O
ATOM 2966 CB CYS B 119 58.708 -43.114 23.386 1.00 74.93 C
ANISOU 2966 CB CYS B 119 12871 7142 8456 1704 2253 1407 C
ATOM 2967 SG CYS B 119 57.360 -42.235 24.233 1.00 85.33 S
ANISOU 2967 SG CYS B 119 14054 8685 9684 1493 2204 1448 S
ATOM 2968 N LYS B 120 61.006 -40.849 23.120 1.00 73.05 N
ANISOU 2968 N LYS B 120 12173 7247 8335 2096 2282 1321 N
ATOM 2969 CA LYS B 120 61.476 -39.491 23.372 1.00 55.91 C
ANISOU 2969 CA LYS B 120 9766 5300 6179 2172 2271 1307 C
ATOM 2970 C LYS B 120 62.077 -38.830 22.130 1.00 55.43 C
ANISOU 2970 C LYS B 120 9597 5299 6166 2210 2409 1224 C
ATOM 2971 O LYS B 120 61.810 -37.651 21.871 1.00 62.08 O
ANISOU 2971 O LYS B 120 10307 6314 6965 2171 2464 1195 O
ATOM 2972 CB LYS B 120 62.443 -39.446 24.557 1.00 49.90 C
ANISOU 2972 CB LYS B 120 8912 4563 5486 2315 2101 1393 C
ATOM 2973 CG LYS B 120 61.725 -39.659 25.898 1.00 44.56 C
ANISOU 2973 CG LYS B 120 8329 3904 4698 2243 1974 1495 C
ATOM 2974 CD LYS B 120 62.694 -39.647 27.071 1.00 54.36 C
ANISOU 2974 CD LYS B 120 9525 5152 5977 2396 1779 1585 C
ATOM 2975 CE LYS B 120 61.958 -39.570 28.414 1.00 65.32 C
ANISOU 2975 CE LYS B 120 11005 6611 7205 2306 1674 1687 C
ATOM 2976 NZ LYS B 120 62.561 -38.575 29.368 1.00 74.19 N
ANISOU 2976 NZ LYS B 120 11995 7892 8300 2420 1538 1711 N
ATOM 2977 N VAL B 121 62.863 -39.568 21.345 1.00 52.62 N
ANISOU 2977 N VAL B 121 9295 4793 5906 2271 2459 1190 N
ATOM 2978 CA VAL B 121 63.630 -38.969 20.249 1.00 45.97 C
ANISOU 2978 CA VAL B 121 8327 3999 5141 2287 2562 1130 C
ATOM 2979 C VAL B 121 62.719 -38.477 19.131 1.00 57.11 C
ANISOU 2979 C VAL B 121 9849 5451 6398 2146 2708 1097 C
ATOM 2980 O VAL B 121 62.834 -37.329 18.680 1.00 60.67 O
ANISOU 2980 O VAL B 121 10171 6035 6846 2097 2734 1116 O
ATOM 2981 CB VAL B 121 64.651 -39.979 19.708 1.00 45.10 C
ANISOU 2981 CB VAL B 121 8241 3697 5197 2389 2579 1070 C
ATOM 2982 CG1 VAL B 121 65.339 -39.419 18.485 1.00 45.10 C
ANISOU 2982 CG1 VAL B 121 8130 3731 5275 2372 2704 990 C
ATOM 2983 CG2 VAL B 121 65.648 -40.331 20.784 1.00 58.90 C
ANISOU 2983 CG2 VAL B 121 9851 5400 7130 2549 2400 1101 C
ATOM 2984 N ILE B 122 61.811 -39.338 18.654 1.00 63.09 N
ANISOU 2984 N ILE B 122 10858 6066 7047 2069 2770 1051 N
ATOM 2985 CA ILE B 122 61.018 -38.989 17.478 1.00 67.82 C
ANISOU 2985 CA ILE B 122 11598 6663 7506 1950 2883 1002 C
ATOM 2986 C ILE B 122 60.117 -37.790 17.762 1.00 73.58 C
ANISOU 2986 C ILE B 122 12118 7567 8270 1850 2718 953 C
ATOM 2987 O ILE B 122 60.139 -36.826 16.976 1.00 95.97 O
ANISOU 2987 O ILE B 122 14843 10464 11155 1770 2641 964 O
ATOM 2988 CB ILE B 122 60.216 -40.218 17.003 1.00 80.97 C
ANISOU 2988 CB ILE B 122 13556 8110 9099 1871 2911 920 C
ATOM 2989 CG1 ILE B 122 61.109 -41.326 16.420 1.00 85.25 C
ANISOU 2989 CG1 ILE B 122 14212 8449 9730 1937 2956 887 C
ATOM 2990 CG2 ILE B 122 59.228 -39.831 15.938 1.00 80.54 C
ANISOU 2990 CG2 ILE B 122 13624 8043 8936 1732 2926 831 C
ATOM 2991 CD1 ILE B 122 62.023 -40.892 15.306 1.00 87.42 C
ANISOU 2991 CD1 ILE B 122 14422 8738 10054 1973 3051 850 C
ATOM 2992 N PRO B 123 59.347 -37.762 18.851 1.00 57.69 N
ANISOU 2992 N PRO B 123 10074 5582 6263 1859 2652 943 N
ATOM 2993 CA PRO B 123 58.603 -36.534 19.184 1.00 57.89 C
ANISOU 2993 CA PRO B 123 9894 5735 6367 1803 2507 925 C
ATOM 2994 C PRO B 123 59.495 -35.312 19.404 1.00 66.49 C
ANISOU 2994 C PRO B 123 10701 6997 7565 1844 2407 961 C
ATOM 2995 O PRO B 123 59.104 -34.181 19.056 1.00 78.34 O
ANISOU 2995 O PRO B 123 12070 8565 9130 1782 2304 955 O
ATOM 2996 CB PRO B 123 57.889 -36.926 20.481 1.00 52.87 C
ANISOU 2996 CB PRO B 123 9253 5137 5699 1731 2422 992 C
ATOM 2997 CG PRO B 123 57.760 -38.425 20.410 1.00 55.48 C
ANISOU 2997 CG PRO B 123 9832 5284 5963 1671 2468 1023 C
ATOM 2998 CD PRO B 123 59.011 -38.889 19.739 1.00 53.25 C
ANISOU 2998 CD PRO B 123 9653 4905 5673 1834 2615 1004 C
ATOM 2999 N TYR B 124 60.701 -35.519 19.945 1.00 54.45 N
ANISOU 2999 N TYR B 124 9132 5547 6009 1927 2472 1051 N
ATOM 3000 CA TYR B 124 61.653 -34.424 20.106 1.00 52.69 C
ANISOU 3000 CA TYR B 124 8713 5443 5864 1944 2415 1139 C
ATOM 3001 C TYR B 124 62.055 -33.839 18.758 1.00 70.41 C
ANISOU 3001 C TYR B 124 10941 7630 8182 1888 2441 1136 C
ATOM 3002 O TYR B 124 62.096 -32.610 18.584 1.00 84.63 O
ANISOU 3002 O TYR B 124 12589 9508 10058 1842 2357 1134 O
ATOM 3003 CB TYR B 124 62.895 -34.900 20.848 1.00 61.94 C
ANISOU 3003 CB TYR B 124 9892 6602 7042 2124 2507 1226 C
ATOM 3004 CG TYR B 124 63.974 -33.852 20.829 1.00 61.38 C
ANISOU 3004 CG TYR B 124 9565 6612 7146 2138 2421 1214 C
ATOM 3005 CD1 TYR B 124 63.880 -32.706 21.603 1.00 62.91 C
ANISOU 3005 CD1 TYR B 124 9603 6955 7345 2121 2319 1240 C
ATOM 3006 CD2 TYR B 124 65.057 -33.978 19.968 1.00 61.88 C
ANISOU 3006 CD2 TYR B 124 9537 6597 7377 2159 2462 1141 C
ATOM 3007 CE1 TYR B 124 64.867 -31.730 21.558 1.00 71.05 C
ANISOU 3007 CE1 TYR B 124 10393 8049 8554 2119 2245 1181 C
ATOM 3008 CE2 TYR B 124 66.042 -33.017 19.912 1.00 63.00 C
ANISOU 3008 CE2 TYR B 124 9430 6809 7697 2161 2412 1084 C
ATOM 3009 CZ TYR B 124 65.947 -31.892 20.706 1.00 72.21 C
ANISOU 3009 CZ TYR B 124 10445 8118 8875 2136 2298 1101 C
ATOM 3010 OH TYR B 124 66.931 -30.924 20.648 1.00 79.11 O
ANISOU 3010 OH TYR B 124 11074 9045 9938 2128 2252 1021 O
ATOM 3011 N LEU B 125 62.384 -34.713 17.797 1.00 65.14 N
ANISOU 3011 N LEU B 125 10457 6813 7482 1908 2588 1125 N
ATOM 3012 CA LEU B 125 62.753 -34.245 16.470 1.00 58.75 C
ANISOU 3012 CA LEU B 125 9680 5928 6714 1870 2658 1109 C
ATOM 3013 C LEU B 125 61.589 -33.540 15.794 1.00 69.69 C
ANISOU 3013 C LEU B 125 11078 7320 8082 1763 2531 1027 C
ATOM 3014 O LEU B 125 61.800 -32.574 15.050 1.00 76.77 O
ANISOU 3014 O LEU B 125 11922 8228 9021 1738 2532 1019 O
ATOM 3015 CB LEU B 125 63.240 -35.416 15.635 1.00 38.51 C
ANISOU 3015 CB LEU B 125 7321 3198 4114 1913 2835 1078 C
ATOM 3016 CG LEU B 125 64.515 -35.973 16.243 1.00 40.07 C
ANISOU 3016 CG LEU B 125 7351 3410 4462 2036 2854 1029 C
ATOM 3017 CD1 LEU B 125 64.981 -37.212 15.460 1.00 52.32 C
ANISOU 3017 CD1 LEU B 125 9053 4786 6042 2089 2974 935 C
ATOM 3018 CD2 LEU B 125 65.572 -34.890 16.293 1.00 39.80 C
ANISOU 3018 CD2 LEU B 125 7028 3486 4606 2051 2819 1002 C
ATOM 3019 N GLN B 126 60.354 -33.974 16.070 1.00 63.90 N
ANISOU 3019 N GLN B 126 10423 6563 7292 1723 2451 963 N
ATOM 3020 CA GLN B 126 59.207 -33.242 15.541 1.00 66.98 C
ANISOU 3020 CA GLN B 126 10823 6971 7655 1660 2372 889 C
ATOM 3021 C GLN B 126 59.168 -31.815 16.090 1.00 65.30 C
ANISOU 3021 C GLN B 126 10359 6925 7529 1655 2254 916 C
ATOM 3022 O GLN B 126 59.008 -30.840 15.333 1.00 66.67 O
ANISOU 3022 O GLN B 126 10505 7120 7706 1630 2231 902 O
ATOM 3023 CB GLN B 126 57.910 -33.984 15.872 1.00 66.69 C
ANISOU 3023 CB GLN B 126 10930 6876 7533 1621 2369 831 C
ATOM 3024 CG GLN B 126 56.658 -33.286 15.353 1.00 89.46 C
ANISOU 3024 CG GLN B 126 13768 9892 10333 1473 2260 777 C
ATOM 3025 CD GLN B 126 56.618 -33.166 13.842 1.00111.75 C
ANISOU 3025 CD GLN B 126 16755 12652 13052 1425 2289 726 C
ATOM 3026 OE1 GLN B 126 56.619 -32.054 13.298 1.00111.37 O
ANISOU 3026 OE1 GLN B 126 16604 12704 13009 1409 2230 723 O
ATOM 3027 NE2 GLN B 126 56.578 -34.305 13.153 1.00124.49 N
ANISOU 3027 NE2 GLN B 126 18656 14092 14554 1401 2386 682 N
ATOM 3028 N ALA B 127 59.340 -31.667 17.407 1.00 55.35 N
ANISOU 3028 N ALA B 127 8938 5770 6321 1685 2187 956 N
ATOM 3029 CA ALA B 127 59.278 -30.319 17.966 1.00 60.89 C
ANISOU 3029 CA ALA B 127 9431 6616 7087 1671 2080 978 C
ATOM 3030 C ALA B 127 60.423 -29.449 17.453 1.00 67.91 C
ANISOU 3030 C ALA B 127 10237 7527 8040 1670 2108 1022 C
ATOM 3031 O ALA B 127 60.224 -28.263 17.143 1.00 79.43 O
ANISOU 3031 O ALA B 127 11609 9039 9531 1637 2058 1013 O
ATOM 3032 CB ALA B 127 59.293 -30.381 19.494 1.00 66.73 C
ANISOU 3032 CB ALA B 127 10067 7447 7841 1711 2024 1012 C
ATOM 3033 N VAL B 128 61.619 -30.028 17.311 1.00 62.40 N
ANISOU 3033 N VAL B 128 9583 6772 7356 1714 2225 1075 N
ATOM 3034 CA VAL B 128 62.745 -29.256 16.784 1.00 55.21 C
ANISOU 3034 CA VAL B 128 8608 5847 6522 1725 2319 1121 C
ATOM 3035 C VAL B 128 62.478 -28.839 15.345 1.00 53.06 C
ANISOU 3035 C VAL B 128 8444 5482 6233 1685 2371 1075 C
ATOM 3036 O VAL B 128 62.826 -27.725 14.938 1.00 58.76 O
ANISOU 3036 O VAL B 128 9080 6234 7012 1657 2380 1072 O
ATOM 3037 CB VAL B 128 64.079 -30.014 16.914 1.00 46.16 C
ANISOU 3037 CB VAL B 128 7435 4674 5428 1791 2456 1134 C
ATOM 3038 CG1 VAL B 128 65.134 -29.334 16.043 1.00 33.92 C
ANISOU 3038 CG1 VAL B 128 5772 3114 4000 1764 2548 1070 C
ATOM 3039 CG2 VAL B 128 64.539 -30.027 18.356 1.00 34.37 C
ANISOU 3039 CG2 VAL B 128 5780 3302 3976 1853 2384 1146 C
ATOM 3040 N SER B 129 61.902 -29.738 14.536 1.00 42.16 N
ANISOU 3040 N SER B 129 7266 3993 4759 1680 2417 1024 N
ATOM 3041 CA SER B 129 61.620 -29.387 13.149 1.00 50.99 C
ANISOU 3041 CA SER B 129 8521 5036 5814 1647 2472 965 C
ATOM 3042 C SER B 129 60.621 -28.236 13.053 1.00 56.78 C
ANISOU 3042 C SER B 129 9178 5870 6524 1605 2340 925 C
ATOM 3043 O SER B 129 60.809 -27.296 12.262 1.00 58.13 O
ANISOU 3043 O SER B 129 9345 6053 6689 1582 2370 912 O
ATOM 3044 CB SER B 129 61.078 -30.619 12.427 1.00 67.25 C
ANISOU 3044 CB SER B 129 10834 6974 7743 1636 2534 904 C
ATOM 3045 OG SER B 129 60.670 -30.318 11.103 1.00 86.47 O
ANISOU 3045 OG SER B 129 13415 9381 10057 1581 2560 826 O
ATOM 3046 N VAL B 130 59.586 -28.258 13.898 1.00 57.56 N
ANISOU 3046 N VAL B 130 9206 6055 6609 1594 2212 909 N
ATOM 3047 CA VAL B 130 58.617 -27.159 13.904 1.00 55.12 C
ANISOU 3047 CA VAL B 130 8794 5874 6275 1547 2099 879 C
ATOM 3048 C VAL B 130 59.302 -25.849 14.289 1.00 57.26 C
ANISOU 3048 C VAL B 130 8898 6196 6662 1570 2082 937 C
ATOM 3049 O VAL B 130 59.075 -24.795 13.674 1.00 45.82 O
ANISOU 3049 O VAL B 130 7436 4777 5196 1554 2074 927 O
ATOM 3050 CB VAL B 130 57.424 -27.473 14.818 1.00 50.08 C
ANISOU 3050 CB VAL B 130 8086 5339 5602 1508 1995 856 C
ATOM 3051 CG1 VAL B 130 56.486 -26.267 14.878 1.00 43.03 C
ANISOU 3051 CG1 VAL B 130 7072 4587 4692 1463 1897 851 C
ATOM 3052 CG2 VAL B 130 56.688 -28.692 14.304 1.00 60.54 C
ANISOU 3052 CG2 VAL B 130 9598 6612 6792 1447 2022 803 C
ATOM 3053 N SER B 131 60.140 -25.893 15.330 1.00 56.19 N
ANISOU 3053 N SER B 131 8642 6085 6622 1595 2076 998 N
ATOM 3054 CA SER B 131 60.784 -24.669 15.798 1.00 38.85 C
ANISOU 3054 CA SER B 131 6287 3958 4515 1582 2057 1042 C
ATOM 3055 C SER B 131 61.725 -24.111 14.738 1.00 43.06 C
ANISOU 3055 C SER B 131 6862 4408 5090 1576 2191 1054 C
ATOM 3056 O SER B 131 61.766 -22.893 14.511 1.00 41.97 O
ANISOU 3056 O SER B 131 6666 4289 4991 1559 2192 1062 O
ATOM 3057 CB SER B 131 61.552 -24.949 17.089 1.00 27.59 C
ANISOU 3057 CB SER B 131 4745 2598 3140 1597 2040 1089 C
ATOM 3058 OG SER B 131 62.407 -23.870 17.421 1.00 27.58 O
ANISOU 3058 OG SER B 131 4597 2654 3226 1573 2056 1103 O
ATOM 3059 N VAL B 132 62.499 -24.984 14.088 1.00 48.82 N
ANISOU 3059 N VAL B 132 7692 5046 5813 1585 2322 1046 N
ATOM 3060 CA VAL B 132 63.402 -24.529 13.037 1.00 45.74 C
ANISOU 3060 CA VAL B 132 7338 4581 5459 1569 2479 1034 C
ATOM 3061 C VAL B 132 62.606 -23.886 11.914 1.00 54.05 C
ANISOU 3061 C VAL B 132 8532 5594 6410 1559 2484 1000 C
ATOM 3062 O VAL B 132 63.009 -22.856 11.359 1.00 65.78 O
ANISOU 3062 O VAL B 132 10010 7055 7931 1546 2565 1011 O
ATOM 3063 CB VAL B 132 64.271 -25.684 12.521 1.00 42.90 C
ANISOU 3063 CB VAL B 132 7064 4136 5098 1585 2634 1013 C
ATOM 3064 CG1 VAL B 132 65.055 -25.221 11.318 1.00 42.79 C
ANISOU 3064 CG1 VAL B 132 7112 4041 5105 1564 2819 985 C
ATOM 3065 CG2 VAL B 132 65.210 -26.139 13.615 1.00 55.37 C
ANISOU 3065 CG2 VAL B 132 8463 5782 6792 1608 2639 1026 C
ATOM 3066 N ALA B 133 61.457 -24.471 11.566 1.00 44.85 N
ANISOU 3066 N ALA B 133 7500 4435 5107 1559 2407 951 N
ATOM 3067 CA ALA B 133 60.665 -23.915 10.474 1.00 37.20 C
ANISOU 3067 CA ALA B 133 6671 3468 3994 1536 2403 909 C
ATOM 3068 C ALA B 133 60.135 -22.530 10.836 1.00 43.67 C
ANISOU 3068 C ALA B 133 7369 4373 4852 1543 2316 937 C
ATOM 3069 O ALA B 133 60.209 -21.589 10.028 1.00 37.18 O
ANISOU 3069 O ALA B 133 6616 3526 3984 1540 2381 948 O
ATOM 3070 CB ALA B 133 59.516 -24.853 10.123 1.00 35.38 C
ANISOU 3070 CB ALA B 133 6590 3260 3593 1503 2324 848 C
ATOM 3071 N VAL B 134 59.574 -22.383 12.041 1.00 46.66 N
ANISOU 3071 N VAL B 134 7582 4845 5300 1556 2184 953 N
ATOM 3072 CA VAL B 134 58.956 -21.103 12.371 1.00 45.86 C
ANISOU 3072 CA VAL B 134 7382 4819 5225 1572 2115 979 C
ATOM 3073 C VAL B 134 60.017 -20.028 12.569 1.00 40.77 C
ANISOU 3073 C VAL B 134 6648 4124 4720 1587 2197 1040 C
ATOM 3074 O VAL B 134 59.815 -18.865 12.188 1.00 34.52 O
ANISOU 3074 O VAL B 134 5866 3321 3927 1609 2228 1063 O
ATOM 3075 CB VAL B 134 58.065 -21.235 13.618 1.00 39.13 C
ANISOU 3075 CB VAL B 134 6387 4082 4400 1573 1974 979 C
ATOM 3076 CG1 VAL B 134 57.292 -19.939 13.849 1.00 27.30 C
ANISOU 3076 CG1 VAL B 134 4808 2654 2909 1602 1922 1008 C
ATOM 3077 CG2 VAL B 134 57.124 -22.414 13.481 1.00 48.51 C
ANISOU 3077 CG2 VAL B 134 7658 5309 5465 1534 1923 924 C
ATOM 3078 N LEU B 135 61.177 -20.389 13.130 1.00 35.26 N
ANISOU 3078 N LEU B 135 5865 3399 4134 1565 2248 1070 N
ATOM 3079 CA LEU B 135 62.238 -19.392 13.226 1.00 41.76 C
ANISOU 3079 CA LEU B 135 6595 4186 5084 1543 2348 1113 C
ATOM 3080 C LEU B 135 62.795 -19.043 11.855 1.00 51.39 C
ANISOU 3080 C LEU B 135 7956 5285 6285 1545 2532 1106 C
ATOM 3081 O LEU B 135 63.167 -17.888 11.609 1.00 59.63 O
ANISOU 3081 O LEU B 135 8978 6279 7400 1542 2624 1139 O
ATOM 3082 CB LEU B 135 63.365 -19.859 14.142 1.00 41.87 C
ANISOU 3082 CB LEU B 135 6454 4246 5207 1503 2365 1114 C
ATOM 3083 CG LEU B 135 63.067 -19.921 15.631 1.00 47.37 C
ANISOU 3083 CG LEU B 135 6997 5083 5918 1487 2209 1108 C
ATOM 3084 CD1 LEU B 135 64.311 -20.423 16.373 1.00 44.94 C
ANISOU 3084 CD1 LEU B 135 6541 4826 5709 1472 2242 1067 C
ATOM 3085 CD2 LEU B 135 62.649 -18.544 16.103 1.00 27.85 C
ANISOU 3085 CD2 LEU B 135 4433 2665 3484 1470 2153 1119 C
ATOM 3086 N THR B 136 62.867 -20.020 10.946 1.00 38.91 N
ANISOU 3086 N THR B 136 6536 3651 4598 1543 2604 1063 N
ATOM 3087 CA THR B 136 63.370 -19.710 9.619 1.00 38.10 C
ANISOU 3087 CA THR B 136 6595 3448 4434 1528 2790 1052 C
ATOM 3088 C THR B 136 62.438 -18.751 8.891 1.00 50.89 C
ANISOU 3088 C THR B 136 8342 5079 5914 1539 2764 1056 C
ATOM 3089 O THR B 136 62.890 -17.771 8.285 1.00 56.73 O
ANISOU 3089 O THR B 136 9135 5754 6666 1528 2902 1087 O
ATOM 3090 CB THR B 136 63.524 -20.994 8.816 1.00 43.67 C
ANISOU 3090 CB THR B 136 7469 4104 5018 1515 2865 1002 C
ATOM 3091 OG1 THR B 136 64.612 -21.757 9.342 1.00 49.47 O
ANISOU 3091 OG1 THR B 136 8087 4819 5891 1509 2943 1005 O
ATOM 3092 CG2 THR B 136 63.818 -20.664 7.369 1.00 46.25 C
ANISOU 3092 CG2 THR B 136 8011 4346 5217 1487 3045 988 C
ATOM 3093 N LEU B 137 61.126 -19.016 8.935 1.00 53.99 N
ANISOU 3093 N LEU B 137 8787 5561 6164 1550 2596 1029 N
ATOM 3094 CA LEU B 137 60.181 -18.070 8.341 1.00 56.48 C
ANISOU 3094 CA LEU B 137 9207 5920 6333 1550 2545 1050 C
ATOM 3095 C LEU B 137 60.212 -16.713 9.035 1.00 61.13 C
ANISOU 3095 C LEU B 137 9643 6518 7067 1596 2547 1106 C
ATOM 3096 O LEU B 137 60.113 -15.668 8.374 1.00 58.85 O
ANISOU 3096 O LEU B 137 9452 6199 6711 1592 2610 1153 O
ATOM 3097 CB LEU B 137 58.763 -18.641 8.355 1.00 49.46 C
ANISOU 3097 CB LEU B 137 8374 5141 5279 1534 2358 1022 C
ATOM 3098 CG LEU B 137 58.548 -19.888 7.496 1.00 49.84 C
ANISOU 3098 CG LEU B 137 8625 5167 5143 1479 2352 972 C
ATOM 3099 CD1 LEU B 137 57.189 -20.514 7.756 1.00 62.76 C
ANISOU 3099 CD1 LEU B 137 10276 6910 6662 1451 2166 951 C
ATOM 3100 CD2 LEU B 137 58.688 -19.531 6.034 1.00 46.48 C
ANISOU 3100 CD2 LEU B 137 8469 4677 4515 1436 2438 997 C
ATOM 3101 N SER B 138 60.343 -16.700 10.366 1.00 59.04 N
ANISOU 3101 N SER B 138 9159 6287 6985 1630 2476 1115 N
ATOM 3102 CA SER B 138 60.429 -15.424 11.064 1.00 56.17 C
ANISOU 3102 CA SER B 138 8663 5914 6767 1670 2491 1172 C
ATOM 3103 C SER B 138 61.658 -14.638 10.628 1.00 65.17 C
ANISOU 3103 C SER B 138 9814 6924 8024 1644 2692 1212 C
ATOM 3104 O SER B 138 61.589 -13.419 10.449 1.00 89.63 O
ANISOU 3104 O SER B 138 12922 9978 11155 1670 2770 1254 O
ATOM 3105 CB SER B 138 60.433 -15.647 12.573 1.00 54.59 C
ANISOU 3105 CB SER B 138 8245 5808 6688 1640 2348 1183 C
ATOM 3106 OG SER B 138 59.212 -16.232 12.991 1.00 53.38 O
ANISOU 3106 OG SER B 138 8073 5774 6435 1657 2189 1148 O
ATOM 3107 N PHE B 139 62.790 -15.320 10.430 1.00 55.59 N
ANISOU 3107 N PHE B 139 8595 5649 6876 1589 2799 1198 N
ATOM 3108 CA PHE B 139 64.003 -14.608 10.045 1.00 55.66 C
ANISOU 3108 CA PHE B 139 8586 5540 7021 1547 3017 1227 C
ATOM 3109 C PHE B 139 63.950 -14.151 8.594 1.00 58.86 C
ANISOU 3109 C PHE B 139 9226 5874 7266 1534 3172 1231 C
ATOM 3110 O PHE B 139 64.488 -13.087 8.260 1.00 46.67 O
ANISOU 3110 O PHE B 139 7694 4240 5801 1511 3339 1274 O
ATOM 3111 CB PHE B 139 65.226 -15.489 10.300 1.00 62.52 C
ANISOU 3111 CB PHE B 139 9350 6395 8010 1486 3095 1202 C
ATOM 3112 CG PHE B 139 65.765 -15.378 11.702 1.00 69.24 C
ANISOU 3112 CG PHE B 139 9938 7323 9047 1444 3009 1207 C
ATOM 3113 CD1 PHE B 139 64.974 -14.865 12.721 1.00 60.18 C
ANISOU 3113 CD1 PHE B 139 8692 6269 7904 1456 2832 1230 C
ATOM 3114 CD2 PHE B 139 67.054 -15.799 12.003 1.00 83.28 C
ANISOU 3114 CD2 PHE B 139 11555 9108 10978 1388 3105 1164 C
ATOM 3115 CE1 PHE B 139 65.458 -14.760 14.009 1.00 59.92 C
ANISOU 3115 CE1 PHE B 139 8423 6351 7995 1399 2741 1192 C
ATOM 3116 CE2 PHE B 139 67.545 -15.700 13.295 1.00 83.74 C
ANISOU 3116 CE2 PHE B 139 11357 9280 11182 1352 3002 1119 C
ATOM 3117 CZ PHE B 139 66.742 -15.181 14.300 1.00 74.50 C
ANISOU 3117 CZ PHE B 139 10108 8214 9984 1355 2814 1124 C
ATOM 3118 N ILE B 140 63.270 -14.913 7.732 1.00 66.98 N
ANISOU 3118 N ILE B 140 10453 6947 8050 1527 3113 1197 N
ATOM 3119 CA ILE B 140 63.021 -14.446 6.369 1.00 62.52 C
ANISOU 3119 CA ILE B 140 10151 6345 7261 1484 3201 1228 C
ATOM 3120 C ILE B 140 62.171 -13.182 6.398 1.00 71.04 C
ANISOU 3120 C ILE B 140 11257 7454 8279 1502 3118 1300 C
ATOM 3121 O ILE B 140 62.463 -12.195 5.706 1.00 80.65 O
ANISOU 3121 O ILE B 140 12597 8594 9454 1461 3247 1373 O
ATOM 3122 CB ILE B 140 62.369 -15.553 5.521 1.00 49.98 C
ANISOU 3122 CB ILE B 140 8777 4802 5411 1456 3115 1185 C
ATOM 3123 CG1 ILE B 140 63.330 -16.741 5.389 1.00 51.65 C
ANISOU 3123 CG1 ILE B 140 8983 4958 5684 1439 3241 1125 C
ATOM 3124 CG2 ILE B 140 62.005 -15.006 4.153 1.00 45.74 C
ANISOU 3124 CG2 ILE B 140 8539 4235 4605 1399 3156 1245 C
ATOM 3125 CD1 ILE B 140 62.829 -17.893 4.509 1.00 44.50 C
ANISOU 3125 CD1 ILE B 140 8307 4067 4533 1410 3199 1075 C
ATOM 3126 N ALA B 141 61.082 -13.206 7.172 1.00 71.06 N
ANISOU 3126 N ALA B 141 11158 7570 8271 1556 2905 1292 N
ATOM 3127 CA ALA B 141 60.220 -12.032 7.253 1.00 70.62 C
ANISOU 3127 CA ALA B 141 11119 7546 8169 1578 2813 1372 C
ATOM 3128 C ALA B 141 60.973 -10.837 7.827 1.00 77.92 C
ANISOU 3128 C ALA B 141 11897 8381 9327 1598 2967 1417 C
ATOM 3129 O ALA B 141 60.792 -9.702 7.371 1.00 81.34 O
ANISOU 3129 O ALA B 141 12432 8757 9717 1571 2994 1514 O
ATOM 3130 CB ALA B 141 58.985 -12.348 8.095 1.00 62.69 C
ANISOU 3130 CB ALA B 141 9996 6680 7145 1635 2587 1348 C
ATOM 3131 N LEU B 142 61.862 -11.084 8.796 1.00 75.85 N
ANISOU 3131 N LEU B 142 11415 8082 9324 1629 3053 1366 N
ATOM 3132 CA LEU B 142 62.659 -10.009 9.382 1.00 70.27 C
ANISOU 3132 CA LEU B 142 10557 7269 8873 1632 3205 1404 C
ATOM 3133 C LEU B 142 63.627 -9.426 8.359 1.00 80.48 C
ANISOU 3133 C LEU B 142 11979 8425 10174 1543 3442 1448 C
ATOM 3134 O LEU B 142 63.805 -8.202 8.280 1.00 82.57 O
ANISOU 3134 O LEU B 142 12244 8604 10525 1515 3552 1518 O
ATOM 3135 CB LEU B 142 63.427 -10.539 10.592 1.00 65.72 C
ANISOU 3135 CB LEU B 142 9751 6671 8550 1633 3180 1375 C
ATOM 3136 CG LEU B 142 64.059 -9.535 11.553 1.00 59.85 C
ANISOU 3136 CG LEU B 142 8798 5865 8077 1583 3234 1414 C
ATOM 3137 CD1 LEU B 142 62.962 -8.746 12.277 1.00 70.31 C
ANISOU 3137 CD1 LEU B 142 10034 7313 9366 1605 3075 1427 C
ATOM 3138 CD2 LEU B 142 65.015 -10.237 12.534 1.00 45.50 C
ANISOU 3138 CD2 LEU B 142 6787 4077 6423 1483 3185 1400 C
ATOM 3139 N ASP B 143 64.259 -10.290 7.563 1.00 87.79 N
ANISOU 3139 N ASP B 143 13021 9322 11014 1489 3535 1414 N
ATOM 3140 CA ASP B 143 65.203 -9.814 6.558 1.00 78.77 C
ANISOU 3140 CA ASP B 143 12010 8052 9868 1399 3790 1453 C
ATOM 3141 C ASP B 143 64.492 -8.958 5.524 1.00 64.93 C
ANISOU 3141 C ASP B 143 10527 6282 7862 1356 3774 1558 C
ATOM 3142 O ASP B 143 64.969 -7.877 5.158 1.00 51.62 O
ANISOU 3142 O ASP B 143 8894 4481 6239 1291 3938 1640 O
ATOM 3143 CB ASP B 143 65.907 -10.996 5.894 1.00 76.74 C
ANISOU 3143 CB ASP B 143 11836 7780 9543 1358 3894 1393 C
ATOM 3144 CG ASP B 143 66.616 -10.605 4.612 1.00 79.81 C
ANISOU 3144 CG ASP B 143 12436 8060 9830 1265 4156 1438 C
ATOM 3145 OD1 ASP B 143 67.798 -10.207 4.675 1.00 87.27 O
ANISOU 3145 OD1 ASP B 143 13259 8895 11004 1209 4396 1436 O
ATOM 3146 OD2 ASP B 143 65.999 -10.720 3.531 1.00 80.07 O
ANISOU 3146 OD2 ASP B 143 12758 8113 9550 1237 4120 1477 O
ATOM 3147 N ARG B 144 63.344 -9.437 5.037 1.00 72.87 N
ANISOU 3147 N ARG B 144 11712 7390 8585 1374 3556 1570 N
ATOM 3148 CA ARG B 144 62.579 -8.669 4.063 1.00 75.94 C
ANISOU 3148 CA ARG B 144 12377 7756 8722 1326 3466 1698 C
ATOM 3149 C ARG B 144 62.067 -7.373 4.666 1.00 68.54 C
ANISOU 3149 C ARG B 144 11353 6787 7901 1350 3371 1794 C
ATOM 3150 O ARG B 144 62.019 -6.339 3.987 1.00 73.45 O
ANISOU 3150 O ARG B 144 12156 7302 8450 1290 3395 1930 O
ATOM 3151 CB ARG B 144 61.422 -9.516 3.541 1.00 82.59 C
ANISOU 3151 CB ARG B 144 13393 8710 9276 1340 3216 1688 C
ATOM 3152 CG ARG B 144 61.877 -10.800 2.856 1.00 87.62 C
ANISOU 3152 CG ARG B 144 14149 9358 9784 1309 3308 1598 C
ATOM 3153 CD ARG B 144 62.573 -10.493 1.533 1.00 80.02 C
ANISOU 3153 CD ARG B 144 13467 8282 8656 1219 3525 1667 C
ATOM 3154 NE ARG B 144 63.979 -10.130 1.684 1.00 72.09 N
ANISOU 3154 NE ARG B 144 12340 7165 7887 1185 3841 1649 N
ATOM 3155 CZ ARG B 144 64.599 -9.250 0.902 1.00 79.63 C
ANISOU 3155 CZ ARG B 144 13456 7999 8800 1103 4055 1747 C
ATOM 3156 NH1 ARG B 144 63.929 -8.645 -0.070 1.00 88.43 N
ANISOU 3156 NH1 ARG B 144 14880 9088 9632 1055 3965 1880 N
ATOM 3157 NH2 ARG B 144 65.881 -8.962 1.092 1.00 80.22 N
ANISOU 3157 NH2 ARG B 144 13387 7972 9122 1063 4350 1722 N
ATOM 3158 N TRP B 145 61.712 -7.396 5.945 1.00 60.02 N
ANISOU 3158 N TRP B 145 10008 5784 7013 1435 3267 1734 N
ATOM 3159 CA TRP B 145 61.194 -6.195 6.577 1.00 60.46 C
ANISOU 3159 CA TRP B 145 9973 5802 7198 1463 3172 1818 C
ATOM 3160 C TRP B 145 62.259 -5.113 6.683 1.00 54.65 C
ANISOU 3160 C TRP B 145 9169 4898 6696 1401 3416 1867 C
ATOM 3161 O TRP B 145 61.991 -3.941 6.393 1.00 61.31 O
ANISOU 3161 O TRP B 145 10120 5626 7550 1362 3372 1995 O
ATOM 3162 CB TRP B 145 60.626 -6.543 7.942 1.00 65.62 C
ANISOU 3162 CB TRP B 145 10358 6581 7992 1564 3041 1732 C
ATOM 3163 CG TRP B 145 59.887 -5.437 8.545 1.00 50.63 C
ANISOU 3163 CG TRP B 145 8384 4652 6202 1599 2896 1808 C
ATOM 3164 CD1 TRP B 145 58.661 -4.977 8.189 1.00 58.83 C
ANISOU 3164 CD1 TRP B 145 9555 5687 7111 1623 2624 1901 C
ATOM 3165 CD2 TRP B 145 60.320 -4.640 9.645 1.00 43.39 C
ANISOU 3165 CD2 TRP B 145 7227 3676 5583 1616 2986 1792 C
ATOM 3166 NE1 TRP B 145 58.298 -3.927 9.002 1.00 74.78 N
ANISOU 3166 NE1 TRP B 145 11430 7637 9346 1667 2530 1931 N
ATOM 3167 CE2 TRP B 145 59.301 -3.704 9.909 1.00 63.14 C
ANISOU 3167 CE2 TRP B 145 9732 6133 8126 1652 2750 1861 C
ATOM 3168 CE3 TRP B 145 61.469 -4.632 10.439 1.00 43.62 C
ANISOU 3168 CE3 TRP B 145 7032 3667 5875 1603 3221 1718 C
ATOM 3169 CZ2 TRP B 145 59.396 -2.765 10.933 1.00 67.82 C
ANISOU 3169 CZ2 TRP B 145 10121 6646 9001 1667 2737 1837 C
ATOM 3170 CZ3 TRP B 145 61.565 -3.705 11.452 1.00 58.18 C
ANISOU 3170 CZ3 TRP B 145 8673 5447 7985 1597 3221 1717 C
ATOM 3171 CH2 TRP B 145 60.534 -2.779 11.690 1.00 69.02 C
ANISOU 3171 CH2 TRP B 145 10066 6776 9383 1625 2969 1763 C
ATOM 3172 N TYR B 146 63.454 -5.464 7.171 1.00 61.00 N
ANISOU 3172 N TYR B 146 9780 5668 7728 1391 3649 1771 N
ATOM 3173 CA TYR B 146 64.525 -4.465 7.201 1.00 76.32 C
ANISOU 3173 CA TYR B 146 11645 7435 9918 1309 3897 1812 C
ATOM 3174 C TYR B 146 64.993 -4.064 5.800 1.00 71.05 C
ANISOU 3174 C TYR B 146 11262 6649 9084 1192 4057 1911 C
ATOM 3175 O TYR B 146 65.316 -2.891 5.570 1.00 71.04 O
ANISOU 3175 O TYR B 146 11311 6495 9187 1109 4166 2015 O
ATOM 3176 CB TYR B 146 65.702 -4.972 8.039 1.00 73.99 C
ANISOU 3176 CB TYR B 146 11062 7112 9938 1317 4076 1689 C
ATOM 3177 CG TYR B 146 65.536 -4.747 9.535 1.00 57.57 C
ANISOU 3177 CG TYR B 146 8686 5062 8127 1393 3993 1635 C
ATOM 3178 CD1 TYR B 146 65.598 -3.465 10.080 1.00 66.20 C
ANISOU 3178 CD1 TYR B 146 9656 6046 9452 1352 4045 1684 C
ATOM 3179 CD2 TYR B 146 65.300 -5.806 10.398 1.00 51.43 C
ANISOU 3179 CD2 TYR B 146 7770 4399 7371 1488 3846 1548 C
ATOM 3180 CE1 TYR B 146 65.445 -3.251 11.448 1.00 61.61 C
ANISOU 3180 CE1 TYR B 146 8803 5495 9112 1404 3984 1628 C
ATOM 3181 CE2 TYR B 146 65.140 -5.598 11.762 1.00 48.09 C
ANISOU 3181 CE2 TYR B 146 7107 4008 7157 1518 3736 1520 C
ATOM 3182 CZ TYR B 146 65.217 -4.325 12.277 1.00 49.86 C
ANISOU 3182 CZ TYR B 146 7189 4157 7597 1476 3826 1546 C
ATOM 3183 OH TYR B 146 65.065 -4.131 13.626 1.00 41.92 O
ANISOU 3183 OH TYR B 146 5955 3260 6715 1362 3657 1541 O
ATOM 3184 N ALA B 147 65.037 -5.012 4.847 1.00 69.68 N
ANISOU 3184 N ALA B 147 11288 6532 8656 1175 4078 1887 N
ATOM 3185 CA ALA B 147 65.518 -4.677 3.507 1.00 61.30 C
ANISOU 3185 CA ALA B 147 10512 5362 7417 1061 4259 1983 C
ATOM 3186 C ALA B 147 64.568 -3.746 2.761 1.00 62.75 C
ANISOU 3186 C ALA B 147 10985 5492 7363 1027 4083 2163 C
ATOM 3187 O ALA B 147 65.016 -2.933 1.942 1.00 65.44 O
ANISOU 3187 O ALA B 147 11524 5690 7653 923 4242 2288 O
ATOM 3188 CB ALA B 147 65.743 -5.952 2.697 1.00 60.26 C
ANISOU 3188 CB ALA B 147 10530 5298 7068 1055 4316 1907 C
ATOM 3189 N ILE B 148 63.265 -3.870 3.010 1.00 67.82 N
ANISOU 3189 N ILE B 148 11663 6237 7870 1111 3748 2187 N
ATOM 3190 CA ILE B 148 62.245 -3.182 2.232 1.00 77.45 C
ANISOU 3190 CA ILE B 148 13168 7407 8852 1097 3510 2361 C
ATOM 3191 C ILE B 148 61.601 -2.051 3.022 1.00 95.12 C
ANISOU 3191 C ILE B 148 15287 9568 11285 1144 3318 2443 C
ATOM 3192 O ILE B 148 61.285 -1.003 2.454 1.00108.93 O
ANISOU 3192 O ILE B 148 17239 11169 12980 1103 3227 2617 O
ATOM 3193 CB ILE B 148 61.169 -4.147 1.680 1.00 67.59 C
ANISOU 3193 CB ILE B 148 12089 6299 7292 1146 3242 2347 C
ATOM 3194 CG1 ILE B 148 61.782 -5.140 0.699 1.00 62.90 C
ANISOU 3194 CG1 ILE B 148 11680 5738 6483 1088 3427 2286 C
ATOM 3195 CG2 ILE B 148 60.058 -3.356 0.995 1.00 74.70 C
ANISOU 3195 CG2 ILE B 148 13248 7134 8000 1151 2946 2538 C
ATOM 3196 CD1 ILE B 148 62.532 -6.265 1.323 1.00 64.03 C
ANISOU 3196 CD1 ILE B 148 11583 5965 6779 1119 3595 2089 C
ATOM 3197 N CYS B 149 61.400 -2.238 4.332 1.00 88.48 N
ANISOU 3197 N CYS B 149 14130 8811 10677 1232 3249 2325 N
ATOM 3198 CA CYS B 149 60.674 -1.236 5.102 1.00 80.30 C
ANISOU 3198 CA CYS B 149 12982 7702 9825 1292 3040 2384 C
ATOM 3199 C CYS B 149 61.553 -0.300 5.916 1.00 73.47 C
ANISOU 3199 C CYS B 149 11906 6693 9318 1251 3239 2365 C
ATOM 3200 O CYS B 149 61.157 0.856 6.106 1.00 86.60 O
ANISOU 3200 O CYS B 149 13588 8199 11116 1256 3105 2459 O
ATOM 3201 CB CYS B 149 59.657 -1.919 6.026 1.00 89.63 C
ANISOU 3201 CB CYS B 149 13973 9060 11024 1418 2793 2279 C
ATOM 3202 SG CYS B 149 58.361 -2.841 5.135 1.00 93.00 S
ANISOU 3202 SG CYS B 149 14630 9624 11082 1461 2483 2314 S
ATOM 3203 N HIS B 150 62.727 -0.708 6.411 1.00 65.93 N
ANISOU 3203 N HIS B 150 10740 5758 8553 1212 3534 2246 N
ATOM 3204 CA HIS B 150 63.588 0.248 7.115 1.00 74.55 C
ANISOU 3204 CA HIS B 150 11629 6687 10011 1151 3718 2233 C
ATOM 3205 C HIS B 150 65.040 0.125 6.674 1.00 78.49 C
ANISOU 3205 C HIS B 150 12100 7107 10618 1033 4087 2201 C
ATOM 3206 O HIS B 150 65.906 -0.430 7.367 1.00 59.77 O
ANISOU 3206 O HIS B 150 9460 4777 8472 1037 4265 2063 O
ATOM 3207 CB HIS B 150 63.426 0.158 8.636 1.00 74.39 C
ANISOU 3207 CB HIS B 150 11265 6737 10264 1236 3639 2103 C
ATOM 3208 CG HIS B 150 62.015 0.370 9.093 1.00 87.85 C
ANISOU 3208 CG HIS B 150 12979 8501 11899 1349 3283 2119 C
ATOM 3209 ND1 HIS B 150 61.012 -0.556 8.901 1.00 96.12 N
ANISOU 3209 ND1 HIS B 150 14108 9738 12677 1440 3072 2102 N
ATOM 3210 CD2 HIS B 150 61.428 1.441 9.678 1.00 92.47 C
ANISOU 3210 CD2 HIS B 150 13501 8961 12672 1385 3089 2137 C
ATOM 3211 CE1 HIS B 150 59.873 -0.075 9.369 1.00 92.11 C
ANISOU 3211 CE1 HIS B 150 13566 9226 12205 1529 2775 2112 C
ATOM 3212 NE2 HIS B 150 60.099 1.136 9.846 1.00 91.90 N
ANISOU 3212 NE2 HIS B 150 13455 9010 12453 1508 2774 2125 N
ATOM 3213 N PRO B 151 65.284 0.525 5.434 1.00 82.12 N
ANISOU 3213 N PRO B 151 12851 7457 10892 932 4191 2331 N
ATOM 3214 CA PRO B 151 66.495 0.156 4.716 1.00 78.47 C
ANISOU 3214 CA PRO B 151 12433 6954 10429 829 4524 2302 C
ATOM 3215 C PRO B 151 67.715 0.825 5.326 1.00 82.37 C
ANISOU 3215 C PRO B 151 12657 7294 11344 730 4799 2248 C
ATOM 3216 O PRO B 151 67.630 1.758 6.133 1.00 86.75 O
ANISOU 3216 O PRO B 151 13051 7739 12173 716 4738 2260 O
ATOM 3217 CB PRO B 151 66.240 0.668 3.289 1.00 81.95 C
ANISOU 3217 CB PRO B 151 13285 7297 10556 741 4527 2489 C
ATOM 3218 CG PRO B 151 65.108 1.579 3.404 1.00 86.26 C
ANISOU 3218 CG PRO B 151 13951 7772 11053 783 4215 2626 C
ATOM 3219 CD PRO B 151 64.277 1.080 4.520 1.00 79.70 C
ANISOU 3219 CD PRO B 151 12888 7094 10300 931 3958 2509 C
ATOM 3220 N LEU B 152 68.862 0.277 4.985 1.00 89.63 N
ANISOU 3220 N LEU B 152 13506 8203 12346 664 5088 2168 N
ATOM 3221 CA LEU B 152 70.150 0.593 5.575 1.00 93.53 C
ANISOU 3221 CA LEU B 152 13685 8579 13272 573 5353 2072 C
ATOM 3222 C LEU B 152 70.257 0.486 7.090 1.00 88.21 C
ANISOU 3222 C LEU B 152 12612 7939 12963 645 5256 1930 C
ATOM 3223 O LEU B 152 71.157 1.115 7.668 1.00 84.68 O
ANISOU 3223 O LEU B 152 11899 7353 12922 547 5414 1870 O
ATOM 3224 CB LEU B 152 70.454 2.034 5.166 1.00 96.24 C
ANISOU 3224 CB LEU B 152 14133 8696 13737 417 5485 2212 C
ATOM 3225 CG LEU B 152 70.796 2.244 3.691 1.00 96.46 C
ANISOU 3225 CG LEU B 152 14512 8641 13499 297 5693 2351 C
ATOM 3226 CD1 LEU B 152 70.706 3.729 3.301 1.00 92.13 C
ANISOU 3226 CD1 LEU B 152 14144 7865 12996 165 5719 2538 C
ATOM 3227 CD2 LEU B 152 72.127 1.613 3.265 1.00 98.87 C
ANISOU 3227 CD2 LEU B 152 14709 8935 13921 213 6048 2249 C
ATOM 3228 N LEU B 153 69.386 -0.248 7.788 1.00 87.00 N
ANISOU 3228 N LEU B 153 12397 7957 12702 798 5002 1871 N
ATOM 3229 CA LEU B 153 69.636 -0.229 9.223 1.00 83.73 C
ANISOU 3229 CA LEU B 153 11607 7542 12664 838 4951 1747 C
ATOM 3230 C LEU B 153 70.624 -1.316 9.611 1.00 82.16 C
ANISOU 3230 C LEU B 153 11181 7392 12645 851 5042 1602 C
ATOM 3231 O LEU B 153 71.565 -1.062 10.370 1.00 82.82 O
ANISOU 3231 O LEU B 153 10952 7377 13139 777 5133 1503 O
ATOM 3232 CB LEU B 153 68.331 -0.362 10.004 1.00 78.84 C
ANISOU 3232 CB LEU B 153 10980 7057 11920 976 4651 1751 C
ATOM 3233 CG LEU B 153 67.599 0.964 10.198 1.00 74.35 C
ANISOU 3233 CG LEU B 153 10478 6369 11403 943 4505 1849 C
ATOM 3234 CD1 LEU B 153 66.102 0.706 10.321 1.00 73.90 C
ANISOU 3234 CD1 LEU B 153 10568 6462 11047 1078 4178 1895 C
ATOM 3235 CD2 LEU B 153 68.129 1.652 11.437 1.00 70.59 C
ANISOU 3235 CD2 LEU B 153 9657 5769 11396 888 4531 1746 C
ATOM 3236 N PHE B 154 70.425 -2.508 9.054 1.00 75.93 N
ANISOU 3236 N PHE B 154 10553 6740 11557 922 4983 1588 N
ATOM 3237 CA PHE B 154 71.166 -3.721 9.363 1.00 84.37 C
ANISOU 3237 CA PHE B 154 11466 7875 12716 934 4973 1478 C
ATOM 3238 C PHE B 154 71.635 -4.349 8.064 1.00 89.39 C
ANISOU 3238 C PHE B 154 12321 8518 13125 888 5145 1494 C
ATOM 3239 O PHE B 154 70.840 -4.507 7.129 1.00 84.91 O
ANISOU 3239 O PHE B 154 12072 8010 12181 924 5100 1571 O
ATOM 3240 CB PHE B 154 70.317 -4.709 10.166 1.00 87.27 C
ANISOU 3240 CB PHE B 154 11805 8413 12942 1063 4667 1443 C
ATOM 3241 CG PHE B 154 69.984 -4.239 11.562 1.00 81.00 C
ANISOU 3241 CG PHE B 154 10775 7616 12383 1085 4501 1417 C
ATOM 3242 CD1 PHE B 154 69.014 -3.275 11.795 1.00 80.96 C
ANISOU 3242 CD1 PHE B 154 10825 7581 12357 1153 4458 1477 C
ATOM 3243 CD2 PHE B 154 70.649 -4.785 12.648 1.00 69.10 C
ANISOU 3243 CD2 PHE B 154 8979 6193 11083 1013 4364 1319 C
ATOM 3244 CE1 PHE B 154 68.720 -2.868 13.094 1.00 76.20 C
ANISOU 3244 CE1 PHE B 154 10012 6956 11984 1158 4320 1451 C
ATOM 3245 CE2 PHE B 154 70.356 -4.376 13.938 1.00 61.99 C
ANISOU 3245 CE2 PHE B 154 7858 5362 10333 987 4169 1265 C
ATOM 3246 CZ PHE B 154 69.392 -3.424 14.161 1.00 67.65 C
ANISOU 3246 CZ PHE B 154 8650 6001 11053 1034 4152 1343 C
ATOM 3247 N LYS B 155 72.924 -4.657 7.996 1.00 98.70 N
ANISOU 3247 N LYS B 155 13323 9636 14543 796 5339 1419 N
ATOM 3248 CA LYS B 155 73.503 -5.361 6.863 1.00107.21 C
ANISOU 3248 CA LYS B 155 14565 10716 15453 752 5533 1414 C
ATOM 3249 C LYS B 155 73.217 -6.858 6.955 1.00108.77 C
ANISOU 3249 C LYS B 155 14796 11071 15459 845 5347 1357 C
ATOM 3250 O LYS B 155 73.531 -7.501 7.965 1.00 99.49 O
ANISOU 3250 O LYS B 155 13360 9972 14470 869 5193 1276 O
ATOM 3251 CB LYS B 155 75.003 -5.098 6.787 1.00118.12 C
ANISOU 3251 CB LYS B 155 15709 11976 17194 617 5828 1348 C
ATOM 3252 CG LYS B 155 75.310 -3.621 6.619 1.00140.55 C
ANISOU 3252 CG LYS B 155 18527 14646 20228 499 6028 1410 C
ATOM 3253 CD LYS B 155 74.262 -2.973 5.718 1.00146.40 C
ANISOU 3253 CD LYS B 155 19668 15375 20583 510 6012 1566 C
ATOM 3254 CE LYS B 155 74.303 -1.451 5.785 1.00141.00 C
ANISOU 3254 CE LYS B 155 18967 14531 20076 401 6113 1653 C
ATOM 3255 NZ LYS B 155 73.144 -0.835 5.070 1.00133.97 N
ANISOU 3255 NZ LYS B 155 18457 13645 18801 418 5999 1823 N
ATOM 3256 N SER B 156 72.654 -7.421 5.881 1.00121.96 N
ANISOU 3256 N SER B 156 16792 12793 16753 879 5353 1398 N
ATOM 3257 CA SER B 156 72.317 -8.841 5.807 1.00120.87 C
ANISOU 3257 CA SER B 156 16724 12785 16414 955 5193 1346 C
ATOM 3258 C SER B 156 73.169 -9.465 4.712 1.00123.68 C
ANISOU 3258 C SER B 156 17198 13098 16696 891 5463 1315 C
ATOM 3259 O SER B 156 72.953 -9.204 3.525 1.00120.90 O
ANISOU 3259 O SER B 156 17150 12702 16084 851 5611 1375 O
ATOM 3260 CB SER B 156 70.830 -9.034 5.493 1.00119.21 C
ANISOU 3260 CB SER B 156 16786 12675 15833 1046 4949 1398 C
ATOM 3261 OG SER B 156 70.007 -8.503 6.514 1.00127.63 O
ANISOU 3261 OG SER B 156 17737 13789 16968 1115 4717 1420 O
ATOM 3262 N THR B 157 74.097 -10.331 5.120 1.00128.79 N
ANISOU 3262 N THR B 157 17611 13772 17551 880 5513 1223 N
ATOM 3263 CA THR B 157 75.035 -11.023 4.247 1.00131.67 C
ANISOU 3263 CA THR B 157 18018 14099 17910 830 5787 1170 C
ATOM 3264 C THR B 157 74.913 -12.531 4.436 1.00127.09 C
ANISOU 3264 C THR B 157 17422 13638 17229 906 5631 1101 C
ATOM 3265 O THR B 157 74.309 -13.013 5.400 1.00125.54 O
ANISOU 3265 O THR B 157 17117 13551 17030 979 5324 1089 O
ATOM 3266 CB THR B 157 76.481 -10.558 4.501 1.00135.53 C
ANISOU 3266 CB THR B 157 18191 14495 18809 730 6055 1111 C
ATOM 3267 OG1 THR B 157 76.866 -10.889 5.841 1.00133.04 O
ANISOU 3267 OG1 THR B 157 17500 14257 18790 758 5854 1034 O
ATOM 3268 CG2 THR B 157 76.595 -9.050 4.307 1.00141.05 C
ANISOU 3268 CG2 THR B 157 18911 15059 19621 639 6222 1184 C
ATOM 3269 N ALA B 158 75.482 -13.280 3.488 1.00108.46 N
ANISOU 3269 N ALA B 158 15182 11252 14776 884 5861 1057 N
ATOM 3270 CA ALA B 158 75.391 -14.732 3.561 1.00 95.75 C
ANISOU 3270 CA ALA B 158 13577 9735 13067 954 5747 990 C
ATOM 3271 C ALA B 158 76.095 -15.282 4.796 1.00 96.66 C
ANISOU 3271 C ALA B 158 13296 9930 13500 983 5626 912 C
ATOM 3272 O ALA B 158 75.646 -16.279 5.368 1.00 93.40 O
ANISOU 3272 O ALA B 158 12851 9628 13010 1058 5385 884 O
ATOM 3273 CB ALA B 158 75.969 -15.346 2.287 1.00106.05 C
ANISOU 3273 CB ALA B 158 15078 10980 14237 921 6063 948 C
ATOM 3274 N ARG B 159 77.199 -14.668 5.219 1.00113.67 N
ANISOU 3274 N ARG B 159 15144 12036 16010 920 5784 868 N
ATOM 3275 CA ARG B 159 77.875 -15.156 6.416 1.00120.68 C
ANISOU 3275 CA ARG B 159 15641 13022 17191 951 5636 778 C
ATOM 3276 C ARG B 159 77.004 -14.952 7.657 1.00122.10 C
ANISOU 3276 C ARG B 159 15734 13311 17347 998 5252 812 C
ATOM 3277 O ARG B 159 76.822 -15.876 8.465 1.00122.16 O
ANISOU 3277 O ARG B 159 15627 13455 17332 1071 5010 767 O
ATOM 3278 CB ARG B 159 79.230 -14.459 6.555 1.00128.76 C
ANISOU 3278 CB ARG B 159 16342 13963 18618 867 5882 710 C
ATOM 3279 CG ARG B 159 79.126 -12.970 6.800 1.00140.85 C
ANISOU 3279 CG ARG B 159 17829 15398 20289 784 5909 770 C
ATOM 3280 CD ARG B 159 80.485 -12.295 6.916 1.00146.99 C
ANISOU 3280 CD ARG B 159 18273 16078 21498 684 6162 690 C
ATOM 3281 NE ARG B 159 80.323 -10.860 7.158 1.00147.46 N
ANISOU 3281 NE ARG B 159 18304 16028 21695 600 6187 748 N
ATOM 3282 CZ ARG B 159 81.224 -10.081 7.757 1.00154.96 C
ANISOU 3282 CZ ARG B 159 18904 16909 23065 515 6260 676 C
ATOM 3283 NH1 ARG B 159 80.977 -8.787 7.928 1.00162.79 N
ANISOU 3283 NH1 ARG B 159 19904 17785 24164 440 6287 731 N
ATOM 3284 NH2 ARG B 159 82.359 -10.594 8.201 1.00156.62 N
ANISOU 3284 NH2 ARG B 159 18746 17162 23601 511 6296 540 N
ATOM 3285 N ARG B 160 76.455 -13.742 7.828 1.00123.19 N
ANISOU 3285 N ARG B 160 15930 13391 17486 959 5206 889 N
ATOM 3286 CA ARG B 160 75.508 -13.525 8.914 1.00119.82 C
ANISOU 3286 CA ARG B 160 15460 13066 17000 1004 4865 923 C
ATOM 3287 C ARG B 160 74.260 -14.393 8.771 1.00116.41 C
ANISOU 3287 C ARG B 160 15292 12725 16212 1087 4646 970 C
ATOM 3288 O ARG B 160 73.685 -14.810 9.782 1.00123.63 O
ANISOU 3288 O ARG B 160 16119 13774 17082 1135 4359 961 O
ATOM 3289 CB ARG B 160 75.108 -12.046 8.977 1.00126.06 C
ANISOU 3289 CB ARG B 160 16292 13752 17853 957 4896 996 C
ATOM 3290 CG ARG B 160 76.197 -11.093 9.470 1.00132.64 C
ANISOU 3290 CG ARG B 160 16809 14500 19090 867 5039 940 C
ATOM 3291 CD ARG B 160 76.197 -10.895 10.998 1.00137.86 C
ANISOU 3291 CD ARG B 160 17161 15274 19946 877 4756 874 C
ATOM 3292 NE ARG B 160 74.941 -10.380 11.554 1.00134.91 N
ANISOU 3292 NE ARG B 160 16910 14944 19406 917 4524 947 N
ATOM 3293 CZ ARG B 160 74.090 -11.091 12.294 1.00118.37 C
ANISOU 3293 CZ ARG B 160 14844 13026 17106 993 4220 944 C
ATOM 3294 NH1 ARG B 160 72.983 -10.525 12.758 1.00105.12 N
ANISOU 3294 NH1 ARG B 160 13261 11377 15301 1022 4047 1005 N
ATOM 3295 NH2 ARG B 160 74.342 -12.365 12.572 1.00109.43 N
ANISOU 3295 NH2 ARG B 160 13643 12035 15900 1043 4102 876 N
ATOM 3296 N ALA B 161 73.808 -14.670 7.539 1.00103.81 N
ANISOU 3296 N ALA B 161 14020 11066 14358 1100 4772 1010 N
ATOM 3297 CA ALA B 161 72.654 -15.556 7.400 1.00 86.84 C
ANISOU 3297 CA ALA B 161 12094 8997 11904 1172 4559 1032 C
ATOM 3298 C ALA B 161 72.965 -16.988 7.840 1.00 95.81 C
ANISOU 3298 C ALA B 161 13119 10233 13052 1214 4466 960 C
ATOM 3299 O ALA B 161 72.133 -17.637 8.486 1.00109.56 O
ANISOU 3299 O ALA B 161 14880 12078 14670 1266 4205 968 O
ATOM 3300 CB ALA B 161 72.142 -15.531 5.958 1.00 69.71 C
ANISOU 3300 CB ALA B 161 10287 6748 9450 1170 4703 1065 C
ATOM 3301 N LEU B 162 74.162 -17.497 7.522 1.00 87.68 N
ANISOU 3301 N LEU B 162 11963 9171 12181 1196 4687 886 N
ATOM 3302 CA LEU B 162 74.535 -18.825 8.008 1.00 87.85 C
ANISOU 3302 CA LEU B 162 11851 9284 12244 1255 4605 808 C
ATOM 3303 C LEU B 162 74.682 -18.837 9.525 1.00 81.32 C
ANISOU 3303 C LEU B 162 10716 8589 11594 1284 4352 770 C
ATOM 3304 O LEU B 162 74.328 -19.826 10.185 1.00 70.40 O
ANISOU 3304 O LEU B 162 9303 7310 10134 1350 4149 743 O
ATOM 3305 CB LEU B 162 75.800 -19.327 7.303 1.00 99.99 C
ANISOU 3305 CB LEU B 162 13306 10757 13930 1246 4914 721 C
ATOM 3306 CG LEU B 162 77.195 -18.721 7.443 1.00107.93 C
ANISOU 3306 CG LEU B 162 14001 11717 15291 1199 5133 653 C
ATOM 3307 CD1 LEU B 162 77.836 -19.137 8.759 1.00104.12 C
ANISOU 3307 CD1 LEU B 162 13139 11355 15066 1260 4943 561 C
ATOM 3308 CD2 LEU B 162 78.054 -19.165 6.249 1.00111.33 C
ANISOU 3308 CD2 LEU B 162 14506 12049 15745 1181 5500 594 C
ATOM 3309 N GLY B 163 75.176 -17.737 10.098 1.00 87.38 N
ANISOU 3309 N GLY B 163 11263 9348 12589 1236 4360 762 N
ATOM 3310 CA GLY B 163 75.234 -17.654 11.546 1.00 88.45 C
ANISOU 3310 CA GLY B 163 11129 9618 12858 1267 4098 710 C
ATOM 3311 C GLY B 163 73.847 -17.644 12.156 1.00 82.39 C
ANISOU 3311 C GLY B 163 10510 8941 11853 1290 3817 780 C
ATOM 3312 O GLY B 163 73.608 -18.275 13.191 1.00 83.09 O
ANISOU 3312 O GLY B 163 10492 9165 11912 1347 3580 735 O
ATOM 3313 N SER B 164 72.908 -16.944 11.514 1.00 61.40 N
ANISOU 3313 N SER B 164 8101 6205 9023 1258 3844 883 N
ATOM 3314 CA SER B 164 71.542 -16.939 12.011 1.00 58.77 C
ANISOU 3314 CA SER B 164 7901 5951 8477 1287 3593 944 C
ATOM 3315 C SER B 164 70.939 -18.333 11.916 1.00 78.40 C
ANISOU 3315 C SER B 164 10534 8498 10758 1343 3482 942 C
ATOM 3316 O SER B 164 70.150 -18.735 12.776 1.00101.45 O
ANISOU 3316 O SER B 164 13444 11530 13575 1372 3250 948 O
ATOM 3317 CB SER B 164 70.705 -15.936 11.221 1.00 68.19 C
ANISOU 3317 CB SER B 164 9326 7034 9548 1273 3658 1040 C
ATOM 3318 OG SER B 164 71.354 -14.677 11.114 1.00 82.42 O
ANISOU 3318 OG SER B 164 11025 8734 11555 1218 3826 1049 O
ATOM 3319 N ILE B 165 71.284 -19.078 10.864 1.00 77.79 N
ANISOU 3319 N ILE B 165 10600 8339 10618 1353 3662 928 N
ATOM 3320 CA ILE B 165 70.758 -20.433 10.711 1.00 73.40 C
ANISOU 3320 CA ILE B 165 10189 7812 9887 1403 3583 918 C
ATOM 3321 C ILE B 165 71.304 -21.347 11.806 1.00 81.27 C
ANISOU 3321 C ILE B 165 10962 8918 10997 1450 3467 848 C
ATOM 3322 O ILE B 165 70.573 -22.164 12.395 1.00 84.95 O
ANISOU 3322 O ILE B 165 11482 9456 11339 1490 3287 859 O
ATOM 3323 CB ILE B 165 71.101 -20.975 9.312 1.00 55.92 C
ANISOU 3323 CB ILE B 165 8179 5480 7587 1402 3826 898 C
ATOM 3324 CG1 ILE B 165 70.287 -20.251 8.238 1.00 59.65 C
ANISOU 3324 CG1 ILE B 165 8931 5865 7869 1380 3883 954 C
ATOM 3325 CG2 ILE B 165 70.861 -22.467 9.264 1.00 57.76 C
ANISOU 3325 CG2 ILE B 165 8507 5733 7705 1455 3777 863 C
ATOM 3326 CD1 ILE B 165 70.731 -20.561 6.817 1.00 49.51 C
ANISOU 3326 CD1 ILE B 165 7856 4470 6485 1362 4152 921 C
ATOM 3327 N LEU B 166 72.599 -21.210 12.106 1.00 80.57 N
ANISOU 3327 N LEU B 166 10616 8840 11158 1457 3570 765 N
ATOM 3328 CA LEU B 166 73.182 -21.976 13.201 1.00 75.75 C
ANISOU 3328 CA LEU B 166 9771 8332 10678 1535 3434 674 C
ATOM 3329 C LEU B 166 72.518 -21.609 14.522 1.00 82.13 C
ANISOU 3329 C LEU B 166 10490 9266 11451 1544 3156 682 C
ATOM 3330 O LEU B 166 72.247 -22.483 15.360 1.00 87.62 O
ANISOU 3330 O LEU B 166 11161 10039 12091 1614 2985 656 O
ATOM 3331 CB LEU B 166 74.693 -21.729 13.242 1.00 77.87 C
ANISOU 3331 CB LEU B 166 9753 8581 11255 1554 3582 568 C
ATOM 3332 CG LEU B 166 75.594 -22.546 14.171 1.00 93.50 C
ANISOU 3332 CG LEU B 166 11462 10635 13428 1674 3472 443 C
ATOM 3333 CD1 LEU B 166 76.934 -22.825 13.491 1.00101.46 C
ANISOU 3333 CD1 LEU B 166 12311 11566 14674 1706 3723 353 C
ATOM 3334 CD2 LEU B 166 75.813 -21.821 15.500 1.00 96.84 C
ANISOU 3334 CD2 LEU B 166 11634 11163 13999 1699 3246 385 C
ATOM 3335 N GLY B 167 72.217 -20.322 14.711 1.00 74.21 N
ANISOU 3335 N GLY B 167 9455 8269 10471 1479 3121 717 N
ATOM 3336 CA GLY B 167 71.534 -19.906 15.922 1.00 64.95 C
ANISOU 3336 CA GLY B 167 8214 7215 9251 1486 2876 712 C
ATOM 3337 C GLY B 167 70.133 -20.480 15.995 1.00 66.48 C
ANISOU 3337 C GLY B 167 8638 7443 9177 1490 2745 796 C
ATOM 3338 O GLY B 167 69.656 -20.840 17.074 1.00 76.08 O
ANISOU 3338 O GLY B 167 9812 8764 10332 1527 2555 776 O
ATOM 3339 N ILE B 168 69.465 -20.605 14.840 1.00 60.21 N
ANISOU 3339 N ILE B 168 8093 6552 8230 1463 2850 884 N
ATOM 3340 CA ILE B 168 68.112 -21.159 14.828 1.00 56.89 C
ANISOU 3340 CA ILE B 168 7880 6151 7586 1475 2725 952 C
ATOM 3341 C ILE B 168 68.149 -22.607 15.276 1.00 61.15 C
ANISOU 3341 C ILE B 168 8435 6726 8075 1532 2672 928 C
ATOM 3342 O ILE B 168 67.310 -23.053 16.067 1.00 62.79 O
ANISOU 3342 O ILE B 168 8681 7004 8173 1552 2517 953 O
ATOM 3343 CB ILE B 168 67.470 -21.045 13.429 1.00 55.29 C
ANISOU 3343 CB ILE B 168 7935 5822 7249 1464 2833 1012 C
ATOM 3344 CG1 ILE B 168 67.105 -19.603 13.090 1.00 57.72 C
ANISOU 3344 CG1 ILE B 168 8270 6090 7573 1434 2854 1054 C
ATOM 3345 CG2 ILE B 168 66.233 -21.951 13.324 1.00 53.80 C
ANISOU 3345 CG2 ILE B 168 7938 5637 6866 1495 2713 1041 C
ATOM 3346 CD1 ILE B 168 66.666 -19.387 11.649 1.00 46.64 C
ANISOU 3346 CD1 ILE B 168 7114 4558 6050 1446 2978 1082 C
ATOM 3347 N TRP B 169 69.130 -23.363 14.786 1.00 63.68 N
ANISOU 3347 N TRP B 169 8726 6986 8483 1567 2817 877 N
ATOM 3348 CA TRP B 169 69.227 -24.744 15.237 1.00 54.81 C
ANISOU 3348 CA TRP B 169 7614 5878 7333 1641 2777 851 C
ATOM 3349 C TRP B 169 69.580 -24.818 16.712 1.00 53.90 C
ANISOU 3349 C TRP B 169 7285 5875 7319 1702 2610 795 C
ATOM 3350 O TRP B 169 69.042 -25.664 17.431 1.00 52.80 O
ANISOU 3350 O TRP B 169 7210 5771 7083 1754 2502 821 O
ATOM 3351 CB TRP B 169 70.215 -25.534 14.389 1.00 53.69 C
ANISOU 3351 CB TRP B 169 7477 5643 7281 1683 2974 791 C
ATOM 3352 CG TRP B 169 69.581 -25.930 13.114 1.00 56.86 C
ANISOU 3352 CG TRP B 169 8162 5932 7508 1652 3096 838 C
ATOM 3353 CD1 TRP B 169 69.649 -25.268 11.926 1.00 56.47 C
ANISOU 3353 CD1 TRP B 169 8230 5796 7429 1598 3253 849 C
ATOM 3354 CD2 TRP B 169 68.686 -27.029 12.915 1.00 53.59 C
ANISOU 3354 CD2 TRP B 169 7973 5474 6914 1676 3058 872 C
ATOM 3355 NE1 TRP B 169 68.895 -25.919 10.980 1.00 57.71 N
ANISOU 3355 NE1 TRP B 169 8667 5865 7394 1597 3301 868 N
ATOM 3356 CE2 TRP B 169 68.292 -27.005 11.563 1.00 55.69 C
ANISOU 3356 CE2 TRP B 169 8475 5631 7053 1640 3182 879 C
ATOM 3357 CE3 TRP B 169 68.200 -28.045 13.742 1.00 51.14 C
ANISOU 3357 CE3 TRP B 169 7698 5194 6539 1730 2942 890 C
ATOM 3358 CZ2 TRP B 169 67.437 -27.959 11.017 1.00 46.20 C
ANISOU 3358 CZ2 TRP B 169 7527 4354 5672 1650 3177 883 C
ATOM 3359 CZ3 TRP B 169 67.352 -28.989 13.198 1.00 47.34 C
ANISOU 3359 CZ3 TRP B 169 7472 4627 5887 1735 2961 915 C
ATOM 3360 CH2 TRP B 169 66.982 -28.942 11.846 1.00 40.97 C
ANISOU 3360 CH2 TRP B 169 6883 3715 4968 1694 3069 902 C
ATOM 3361 N ALA B 170 70.455 -23.930 17.193 1.00 57.06 N
ANISOU 3361 N ALA B 170 7445 6321 7912 1704 2586 716 N
ATOM 3362 CA ALA B 170 70.822 -24.001 18.604 1.00 54.22 C
ANISOU 3362 CA ALA B 170 6892 6054 7655 1788 2401 638 C
ATOM 3363 C ALA B 170 69.618 -23.701 19.493 1.00 58.36 C
ANISOU 3363 C ALA B 170 7504 6666 8005 1762 2234 699 C
ATOM 3364 O ALA B 170 69.337 -24.432 20.454 1.00 60.04 O
ANISOU 3364 O ALA B 170 7735 6921 8157 1841 2113 704 O
ATOM 3365 CB ALA B 170 71.968 -23.029 18.888 1.00 51.68 C
ANISOU 3365 CB ALA B 170 6295 5753 7587 1800 2399 527 C
ATOM 3366 N VAL B 171 68.861 -22.658 19.150 1.00 55.19 N
ANISOU 3366 N VAL B 171 7173 6277 7519 1663 2242 752 N
ATOM 3367 CA VAL B 171 67.661 -22.318 19.906 1.00 31.57 C
ANISOU 3367 CA VAL B 171 4257 3365 4372 1639 2103 800 C
ATOM 3368 C VAL B 171 66.646 -23.449 19.825 1.00 45.71 C
ANISOU 3368 C VAL B 171 6264 5141 5963 1657 2094 896 C
ATOM 3369 O VAL B 171 66.043 -23.841 20.835 1.00 50.08 O
ANISOU 3369 O VAL B 171 6848 5762 6418 1699 1990 919 O
ATOM 3370 CB VAL B 171 67.068 -20.992 19.411 1.00 32.63 C
ANISOU 3370 CB VAL B 171 4422 3492 4483 1549 2120 832 C
ATOM 3371 CG1 VAL B 171 65.701 -20.802 20.018 1.00 42.36 C
ANISOU 3371 CG1 VAL B 171 5748 4796 5553 1533 1995 880 C
ATOM 3372 CG2 VAL B 171 67.985 -19.842 19.788 1.00 31.61 C
ANISOU 3372 CG2 VAL B 171 4073 3384 4555 1540 2114 734 C
ATOM 3373 N SER B 172 66.433 -23.987 18.618 1.00 49.42 N
ANISOU 3373 N SER B 172 6900 5508 6370 1634 2213 952 N
ATOM 3374 CA SER B 172 65.391 -24.988 18.455 1.00 47.21 C
ANISOU 3374 CA SER B 172 6831 5189 5919 1650 2201 1029 C
ATOM 3375 C SER B 172 65.740 -26.250 19.220 1.00 54.17 C
ANISOU 3375 C SER B 172 7717 6079 6786 1740 2193 1026 C
ATOM 3376 O SER B 172 64.876 -26.863 19.860 1.00 61.57 O
ANISOU 3376 O SER B 172 8766 7037 7592 1770 2136 1086 O
ATOM 3377 CB SER B 172 65.245 -25.332 16.966 1.00 30.99 C
ANISOU 3377 CB SER B 172 4952 3001 3822 1627 2327 1051 C
ATOM 3378 OG SER B 172 65.020 -24.196 16.152 1.00 30.77 O
ANISOU 3378 OG SER B 172 4943 2941 3809 1573 2352 1055 O
ATOM 3379 N LEU B 173 67.015 -26.627 19.188 1.00 58.15 N
ANISOU 3379 N LEU B 173 8094 6556 7445 1801 2252 950 N
ATOM 3380 CA LEU B 173 67.483 -27.789 19.921 1.00 60.12 C
ANISOU 3380 CA LEU B 173 8327 6791 7726 1921 2223 929 C
ATOM 3381 C LEU B 173 67.411 -27.582 21.421 1.00 51.91 C
ANISOU 3381 C LEU B 173 7189 5848 6684 1991 2060 920 C
ATOM 3382 O LEU B 173 67.114 -28.525 22.164 1.00 33.92 O
ANISOU 3382 O LEU B 173 5011 3561 4317 2083 2016 967 O
ATOM 3383 CB LEU B 173 68.910 -28.114 19.484 1.00 57.21 C
ANISOU 3383 CB LEU B 173 7805 6354 7579 1989 2299 824 C
ATOM 3384 CG LEU B 173 68.932 -28.631 18.040 1.00 50.44 C
ANISOU 3384 CG LEU B 173 7101 5383 6682 1948 2489 836 C
ATOM 3385 CD1 LEU B 173 70.325 -28.542 17.432 1.00 39.61 C
ANISOU 3385 CD1 LEU B 173 5553 3959 5537 1986 2605 725 C
ATOM 3386 CD2 LEU B 173 68.319 -30.018 17.898 1.00 46.47 C
ANISOU 3386 CD2 LEU B 173 6824 4797 6034 1996 2529 889 C
ATOM 3387 N ALA B 174 67.625 -26.350 21.887 1.00 47.92 N
ANISOU 3387 N ALA B 174 6518 5426 6264 1956 1976 864 N
ATOM 3388 CA ALA B 174 67.632 -26.157 23.329 1.00 47.60 C
ANISOU 3388 CA ALA B 174 6395 5466 6223 2043 1818 840 C
ATOM 3389 C ALA B 174 66.223 -26.096 23.902 1.00 48.36 C
ANISOU 3389 C ALA B 174 6663 5635 6076 2012 1792 942 C
ATOM 3390 O ALA B 174 65.919 -26.791 24.879 1.00 38.03 O
ANISOU 3390 O ALA B 174 5447 4350 4655 2118 1739 992 O
ATOM 3391 CB ALA B 174 68.406 -24.884 23.676 1.00 42.02 C
ANISOU 3391 CB ALA B 174 5446 4808 5711 2031 1734 719 C
ATOM 3392 N ILE B 175 65.332 -25.324 23.273 1.00 64.25 N
ANISOU 3392 N ILE B 175 8733 7668 8010 1884 1829 977 N
ATOM 3393 CA ILE B 175 64.026 -25.083 23.885 1.00 67.25 C
ANISOU 3393 CA ILE B 175 9220 8115 8217 1864 1781 1045 C
ATOM 3394 C ILE B 175 63.067 -26.262 23.785 1.00 62.52 C
ANISOU 3394 C ILE B 175 8845 7456 7453 1891 1839 1160 C
ATOM 3395 O ILE B 175 62.033 -26.264 24.471 1.00 59.00 O
ANISOU 3395 O ILE B 175 8481 7042 6896 1910 1797 1213 O
ATOM 3396 CB ILE B 175 63.367 -23.826 23.280 1.00 60.26 C
ANISOU 3396 CB ILE B 175 8295 7245 7356 1742 1758 1025 C
ATOM 3397 CG1 ILE B 175 63.040 -24.028 21.802 1.00 62.70 C
ANISOU 3397 CG1 ILE B 175 8715 7442 7665 1675 1837 1069 C
ATOM 3398 CG2 ILE B 175 64.280 -22.614 23.413 1.00 57.38 C
ANISOU 3398 CG2 ILE B 175 7725 6918 7156 1716 1722 911 C
ATOM 3399 CD1 ILE B 175 62.471 -22.776 21.158 1.00 61.58 C
ANISOU 3399 CD1 ILE B 175 8542 7300 7554 1592 1810 1050 C
ATOM 3400 N MET B 176 63.367 -27.274 22.971 1.00 52.34 N
ANISOU 3400 N MET B 176 7658 6061 6168 1903 1935 1187 N
ATOM 3401 CA MET B 176 62.490 -28.433 22.888 1.00 55.74 C
ANISOU 3401 CA MET B 176 8284 6414 6482 1917 1974 1241 C
ATOM 3402 C MET B 176 62.940 -29.608 23.752 1.00 75.72 C
ANISOU 3402 C MET B 176 10912 8940 8916 2058 2041 1287 C
ATOM 3403 O MET B 176 62.281 -30.651 23.733 1.00 74.62 O
ANISOU 3403 O MET B 176 10899 8737 8718 2046 2059 1254 O
ATOM 3404 CB MET B 176 62.356 -28.872 21.429 1.00 49.67 C
ANISOU 3404 CB MET B 176 7596 5521 5754 1845 2034 1206 C
ATOM 3405 CG MET B 176 61.681 -27.806 20.608 1.00 64.38 C
ANISOU 3405 CG MET B 176 9405 7385 7672 1744 1967 1153 C
ATOM 3406 SD MET B 176 60.181 -27.218 21.407 1.00 76.93 S
ANISOU 3406 SD MET B 176 10933 9060 9237 1710 1828 1104 S
ATOM 3407 CE MET B 176 59.583 -26.036 20.199 1.00 74.41 C
ANISOU 3407 CE MET B 176 10577 8732 8962 1632 1801 1062 C
ATOM 3408 N VAL B 177 64.038 -29.462 24.508 1.00 81.91 N
ANISOU 3408 N VAL B 177 11545 9771 9806 2159 1959 1223 N
ATOM 3409 CA VAL B 177 64.429 -30.506 25.467 1.00 57.58 C
ANISOU 3409 CA VAL B 177 8534 6643 6699 2314 1903 1234 C
ATOM 3410 C VAL B 177 63.330 -30.832 26.467 1.00 47.92 C
ANISOU 3410 C VAL B 177 7489 5467 5253 2357 1923 1298 C
ATOM 3411 O VAL B 177 63.111 -32.023 26.745 1.00 57.64 O
ANISOU 3411 O VAL B 177 8884 6590 6427 2405 1930 1322 O
ATOM 3412 CB VAL B 177 65.758 -30.133 26.137 1.00 58.32 C
ANISOU 3412 CB VAL B 177 8416 6744 6999 2423 1726 1156 C
ATOM 3413 CG1 VAL B 177 66.097 -31.129 27.223 1.00 66.67 C
ANISOU 3413 CG1 VAL B 177 9574 7725 8031 2589 1586 1203 C
ATOM 3414 CG2 VAL B 177 66.858 -30.089 25.089 1.00 60.10 C
ANISOU 3414 CG2 VAL B 177 8471 6893 7470 2394 1757 1062 C
ATOM 3415 N PRO B 178 62.635 -29.867 27.072 1.00 47.47 N
ANISOU 3415 N PRO B 178 7402 5542 5092 2337 1918 1308 N
ATOM 3416 CA PRO B 178 61.563 -30.235 28.013 1.00 51.29 C
ANISOU 3416 CA PRO B 178 7996 6024 5466 2381 1922 1281 C
ATOM 3417 C PRO B 178 60.471 -31.104 27.392 1.00 63.37 C
ANISOU 3417 C PRO B 178 9625 7406 7044 2273 1967 1242 C
ATOM 3418 O PRO B 178 59.940 -32.007 28.068 1.00 71.27 O
ANISOU 3418 O PRO B 178 10767 8360 7952 2180 1900 1293 O
ATOM 3419 CB PRO B 178 61.016 -28.873 28.465 1.00 47.99 C
ANISOU 3419 CB PRO B 178 7434 5710 5090 2324 1815 1244 C
ATOM 3420 CG PRO B 178 61.429 -27.916 27.378 1.00 47.89 C
ANISOU 3420 CG PRO B 178 7288 5718 5188 2178 1773 1268 C
ATOM 3421 CD PRO B 178 62.766 -28.406 26.934 1.00 55.36 C
ANISOU 3421 CD PRO B 178 8222 6632 6179 2258 1839 1284 C
ATOM 3422 N GLN B 179 60.169 -30.900 26.103 1.00 59.86 N
ANISOU 3422 N GLN B 179 9107 6910 6726 2139 1965 1186 N
ATOM 3423 CA GLN B 179 59.214 -31.766 25.417 1.00 46.01 C
ANISOU 3423 CA GLN B 179 7482 5022 4976 2060 2029 1157 C
ATOM 3424 C GLN B 179 59.691 -33.214 25.409 1.00 50.19 C
ANISOU 3424 C GLN B 179 8199 5444 5425 2096 2104 1193 C
ATOM 3425 O GLN B 179 58.903 -34.134 25.658 1.00 54.64 O
ANISOU 3425 O GLN B 179 8893 5940 5928 1957 2065 1225 O
ATOM 3426 CB GLN B 179 59.007 -31.264 23.987 1.00 38.01 C
ANISOU 3426 CB GLN B 179 6394 3980 4069 1939 1997 1105 C
ATOM 3427 CG GLN B 179 58.008 -32.062 23.159 1.00 40.51 C
ANISOU 3427 CG GLN B 179 6844 4190 4357 1833 2049 1063 C
ATOM 3428 CD GLN B 179 56.562 -31.780 23.557 1.00 60.19 C
ANISOU 3428 CD GLN B 179 9263 6812 6795 1615 1955 1051 C
ATOM 3429 OE1 GLN B 179 56.144 -30.625 23.631 1.00 70.23 O
ANISOU 3429 OE1 GLN B 179 10378 8205 8102 1566 1881 1030 O
ATOM 3430 NE2 GLN B 179 55.795 -32.835 23.817 1.00 70.93 N
ANISOU 3430 NE2 GLN B 179 10742 8139 8070 1485 1975 1074 N
ATOM 3431 N ALA B 180 60.977 -33.437 25.123 1.00 62.85 N
ANISOU 3431 N ALA B 180 9812 7049 7017 2223 2189 1222 N
ATOM 3432 CA ALA B 180 61.517 -34.792 25.160 1.00 54.64 C
ANISOU 3432 CA ALA B 180 8932 5857 5971 2249 2161 1285 C
ATOM 3433 C ALA B 180 61.506 -35.342 26.582 1.00 54.21 C
ANISOU 3433 C ALA B 180 8968 5771 5860 2275 1995 1376 C
ATOM 3434 O ALA B 180 61.285 -36.544 26.791 1.00 54.72 O
ANISOU 3434 O ALA B 180 9211 5685 5895 2235 1958 1430 O
ATOM 3435 CB ALA B 180 62.933 -34.813 24.582 1.00 36.74 C
ANISOU 3435 CB ALA B 180 6575 3560 3826 2331 2158 1298 C
ATOM 3436 N ALA B 181 61.733 -34.472 27.570 1.00 51.93 N
ANISOU 3436 N ALA B 181 8580 5617 5536 2334 1894 1403 N
ATOM 3437 CA ALA B 181 61.795 -34.911 28.960 1.00 61.81 C
ANISOU 3437 CA ALA B 181 9945 6850 6690 2362 1727 1501 C
ATOM 3438 C ALA B 181 60.443 -35.393 29.475 1.00 61.99 C
ANISOU 3438 C ALA B 181 10103 6860 6590 2167 1737 1535 C
ATOM 3439 O ALA B 181 60.399 -36.314 30.300 1.00 79.53 O
ANISOU 3439 O ALA B 181 12501 8992 8724 2139 1647 1638 O
ATOM 3440 CB ALA B 181 62.328 -33.785 29.844 1.00 76.87 C
ANISOU 3440 CB ALA B 181 11729 8908 8567 2469 1612 1506 C
ATOM 3441 N VAL B 182 59.331 -34.814 28.994 1.00 48.60 N
ANISOU 3441 N VAL B 182 8312 5245 4908 2009 1824 1456 N
ATOM 3442 CA VAL B 182 58.020 -35.248 29.493 1.00 38.32 C
ANISOU 3442 CA VAL B 182 7086 3954 3521 1781 1820 1489 C
ATOM 3443 C VAL B 182 57.538 -36.517 28.803 1.00 46.09 C
ANISOU 3443 C VAL B 182 8216 4769 4527 1665 1878 1509 C
ATOM 3444 O VAL B 182 56.592 -37.158 29.285 1.00 45.96 O
ANISOU 3444 O VAL B 182 8298 4729 4435 1480 1884 1571 O
ATOM 3445 CB VAL B 182 56.917 -34.181 29.353 1.00 36.56 C
ANISOU 3445 CB VAL B 182 6681 3888 3322 1629 1844 1406 C
ATOM 3446 CG1 VAL B 182 57.286 -32.915 30.109 1.00 45.95 C
ANISOU 3446 CG1 VAL B 182 7744 5233 4481 1728 1789 1384 C
ATOM 3447 CG2 VAL B 182 56.625 -33.891 27.894 1.00 40.41 C
ANISOU 3447 CG2 VAL B 182 7063 4346 3943 1595 1902 1309 C
ATOM 3448 N MET B 183 58.159 -36.901 27.691 1.00 52.41 N
ANISOU 3448 N MET B 183 9043 5449 5420 1763 1939 1462 N
ATOM 3449 CA MET B 183 57.704 -38.059 26.939 1.00 55.02 C
ANISOU 3449 CA MET B 183 9532 5608 5767 1658 2000 1465 C
ATOM 3450 C MET B 183 57.955 -39.323 27.749 1.00 67.16 C
ANISOU 3450 C MET B 183 11283 6989 7245 1660 1939 1595 C
ATOM 3451 O MET B 183 59.014 -39.493 28.361 1.00 67.86 O
ANISOU 3451 O MET B 183 11413 7039 7332 1833 1851 1660 O
ATOM 3452 CB MET B 183 58.437 -38.159 25.598 1.00 54.79 C
ANISOU 3452 CB MET B 183 9507 5484 5826 1780 2093 1380 C
ATOM 3453 CG MET B 183 58.203 -37.024 24.638 1.00 52.61 C
ANISOU 3453 CG MET B 183 9063 5320 5606 1774 2154 1264 C
ATOM 3454 SD MET B 183 56.445 -36.689 24.579 1.00 75.53 S
ANISOU 3454 SD MET B 183 11899 8316 8484 1498 2109 1239 S
ATOM 3455 CE MET B 183 55.876 -38.200 23.792 1.00 60.31 C
ANISOU 3455 CE MET B 183 10222 6169 6523 1362 2176 1249 C
ATOM 3456 N GLU B 184 56.978 -40.221 27.741 1.00 73.09 N
ANISOU 3456 N GLU B 184 12172 7639 7961 1464 1971 1641 N
ATOM 3457 CA GLU B 184 57.130 -41.487 28.427 1.00 83.42 C
ANISOU 3457 CA GLU B 184 13705 8767 9225 1447 1920 1775 C
ATOM 3458 C GLU B 184 56.324 -42.528 27.676 1.00 83.50 C
ANISOU 3458 C GLU B 184 13863 8600 9265 1275 2004 1771 C
ATOM 3459 O GLU B 184 55.247 -42.252 27.136 1.00 69.37 O
ANISOU 3459 O GLU B 184 12004 6876 7478 1090 2077 1709 O
ATOM 3460 CB GLU B 184 56.630 -41.407 29.881 1.00 89.04 C
ANISOU 3460 CB GLU B 184 14453 9577 9802 1344 1859 1895 C
ATOM 3461 CG GLU B 184 57.522 -40.636 30.852 1.00 92.40 C
ANISOU 3461 CG GLU B 184 14817 10128 10164 1520 1742 1929 C
ATOM 3462 CD GLU B 184 58.763 -41.416 31.263 1.00103.12 C
ANISOU 3462 CD GLU B 184 16325 11318 11537 1721 1608 2029 C
ATOM 3463 OE1 GLU B 184 58.685 -42.667 31.359 1.00111.25 O
ANISOU 3463 OE1 GLU B 184 17559 12142 12569 1674 1590 2130 O
ATOM 3464 OE2 GLU B 184 59.812 -40.771 31.498 1.00103.26 O
ANISOU 3464 OE2 GLU B 184 16248 11404 11583 1926 1506 2011 O
ATOM 3465 N CYS B 185 56.864 -43.734 27.680 1.00 87.17 N
ANISOU 3465 N CYS B 185 14532 8827 9760 1337 1974 1843 N
ATOM 3466 CA CYS B 185 56.305 -44.894 27.012 1.00 65.67 C
ANISOU 3466 CA CYS B 185 11998 5877 7078 1201 2040 1846 C
ATOM 3467 C CYS B 185 55.766 -45.833 28.086 1.00 75.11 C
ANISOU 3467 C CYS B 185 13368 6962 8207 1054 2005 2017 C
ATOM 3468 O CYS B 185 56.512 -46.246 28.983 1.00 80.47 O
ANISOU 3468 O CYS B 185 14145 7571 8860 1180 1897 2139 O
ATOM 3469 CB CYS B 185 57.351 -45.548 26.116 1.00 53.49 C
ANISOU 3469 CB CYS B 185 10554 4129 5641 1388 2046 1785 C
ATOM 3470 SG CYS B 185 56.692 -46.795 25.021 1.00 77.00 S
ANISOU 3470 SG CYS B 185 13761 6823 8672 1229 2141 1732 S
ATOM 3471 N SER B 186 54.485 -46.172 28.004 1.00 75.04 N
ANISOU 3471 N SER B 186 13401 6933 8176 788 2092 2037 N
ATOM 3472 CA SER B 186 53.854 -46.995 29.028 1.00 85.11 C
ANISOU 3472 CA SER B 186 14831 8122 9385 616 2098 2207 C
ATOM 3473 C SER B 186 52.883 -47.950 28.359 1.00108.37 C
ANISOU 3473 C SER B 186 17910 10868 12396 379 2198 2202 C
ATOM 3474 O SER B 186 52.246 -47.615 27.362 1.00114.41 O
ANISOU 3474 O SER B 186 18587 11671 13214 270 2270 2073 O
ATOM 3475 CB SER B 186 53.111 -46.153 30.073 1.00 87.86 C
ANISOU 3475 CB SER B 186 15038 8733 9613 489 2123 2264 C
ATOM 3476 OG SER B 186 52.181 -45.277 29.456 1.00102.29 O
ANISOU 3476 OG SER B 186 16653 10745 11468 350 2210 2141 O
ATOM 3477 N SER B 187 52.763 -49.143 28.935 1.00115.13 N
ANISOU 3477 N SER B 187 18993 11501 13252 294 2193 2351 N
ATOM 3478 CA SER B 187 51.854 -50.154 28.421 1.00104.95 C
ANISOU 3478 CA SER B 187 17852 9987 12039 51 2286 2362 C
ATOM 3479 C SER B 187 50.501 -50.137 29.116 1.00105.91 C
ANISOU 3479 C SER B 187 17925 10207 12107 -254 2400 2457 C
ATOM 3480 O SER B 187 50.365 -49.717 30.268 1.00113.45 O
ANISOU 3480 O SER B 187 18824 11339 12944 -269 2405 2569 O
ATOM 3481 CB SER B 187 52.485 -51.540 28.587 1.00116.93 C
ANISOU 3481 CB SER B 187 19648 11165 13616 123 2224 2471 C
ATOM 3482 OG SER B 187 51.857 -52.517 27.774 1.00130.28 O
ANISOU 3482 OG SER B 187 21492 12591 15418 -64 2295 2426 O
ATOM 3483 N VAL B 188 49.495 -50.623 28.385 1.00107.47 N
ANISOU 3483 N VAL B 188 18154 10280 12401 -506 2500 2404 N
ATOM 3484 CA VAL B 188 48.097 -50.457 28.773 1.00110.09 C
ANISOU 3484 CA VAL B 188 18372 10728 12729 -818 2638 2449 C
ATOM 3485 C VAL B 188 47.823 -51.074 30.136 1.00110.73 C
ANISOU 3485 C VAL B 188 18576 10770 12727 -926 2693 2664 C
ATOM 3486 O VAL B 188 46.950 -50.602 30.878 1.00111.48 O
ANISOU 3486 O VAL B 188 18534 11065 12759 -1096 2806 2722 O
ATOM 3487 CB VAL B 188 47.189 -51.064 27.684 1.00112.15 C
ANISOU 3487 CB VAL B 188 18680 10793 13139 -1075 2713 2353 C
ATOM 3488 CG1 VAL B 188 45.852 -51.509 28.271 1.00108.70 C
ANISOU 3488 CG1 VAL B 188 18217 10337 12748 -1428 2866 2456 C
ATOM 3489 CG2 VAL B 188 46.999 -50.076 26.521 1.00106.23 C
ANISOU 3489 CG2 VAL B 188 17744 10193 12426 -1053 2698 2154 C
ATOM 3490 N LEU B 189 48.612 -52.097 30.463 1.00112.64 N
ANISOU 3490 N LEU B 189 19080 10751 12967 -829 2621 2786 N
ATOM 3491 CA LEU B 189 48.553 -52.776 31.783 1.00112.05 C
ANISOU 3491 CA LEU B 189 19178 10607 12790 -891 2648 3014 C
ATOM 3492 C LEU B 189 49.971 -52.816 32.350 1.00119.56 C
ANISOU 3492 C LEU B 189 20278 11489 13660 -575 2470 3103 C
ATOM 3493 O LEU B 189 50.924 -52.720 31.568 1.00124.66 O
ANISOU 3493 O LEU B 189 20942 12037 14388 -344 2348 2997 O
ATOM 3494 CB LEU B 189 47.896 -54.150 31.678 1.00103.99 C
ANISOU 3494 CB LEU B 189 18369 9264 11880 -1150 2745 3117 C
ATOM 3495 CG LEU B 189 46.425 -54.094 31.274 1.00 97.26 C
ANISOU 3495 CG LEU B 189 17399 8503 11051 -1514 2954 3152 C
ATOM 3496 CD1 LEU B 189 45.886 -55.496 31.048 1.00102.20 C
ANISOU 3496 CD1 LEU B 189 17752 9292 11787 -1633 3010 2936 C
ATOM 3497 CD2 LEU B 189 45.596 -53.361 32.313 1.00 91.75 C
ANISOU 3497 CD2 LEU B 189 16934 7464 10463 -1765 3045 3284 C
ATOM 3498 N PRO B 190 50.157 -52.996 33.667 1.00120.88 N
ANISOU 3498 N PRO B 190 20556 11707 13667 -560 2455 3297 N
ATOM 3499 CA PRO B 190 51.480 -52.827 34.261 1.00130.07 C
ANISOU 3499 CA PRO B 190 21807 12882 14733 -254 2264 3372 C
ATOM 3500 C PRO B 190 52.650 -53.668 33.736 1.00134.46 C
ANISOU 3500 C PRO B 190 22487 13168 15435 -14 2108 3333 C
ATOM 3501 O PRO B 190 53.701 -53.099 33.520 1.00138.30 O
ANISOU 3501 O PRO B 190 22832 13746 15968 222 2004 3188 O
ATOM 3502 CB PRO B 190 51.229 -53.247 35.717 1.00135.62 C
ANISOU 3502 CB PRO B 190 22737 13521 15271 -350 2290 3633 C
ATOM 3503 CG PRO B 190 49.779 -52.902 35.953 1.00132.18 C
ANISOU 3503 CG PRO B 190 22202 13230 14791 -679 2523 3645 C
ATOM 3504 CD PRO B 190 49.099 -53.236 34.644 1.00122.94 C
ANISOU 3504 CD PRO B 190 20898 11980 13833 -834 2618 3469 C
ATOM 3505 N GLU B 191 52.464 -54.966 33.525 1.00129.47 N
ANISOU 3505 N GLU B 191 22112 12194 14886 -72 2100 3460 N
ATOM 3506 CA GLU B 191 53.637 -55.753 33.076 1.00118.53 C
ANISOU 3506 CA GLU B 191 20867 10525 13644 171 1945 3452 C
ATOM 3507 C GLU B 191 53.449 -56.271 31.654 1.00110.59 C
ANISOU 3507 C GLU B 191 19894 9284 12842 85 2015 3295 C
ATOM 3508 O GLU B 191 54.250 -57.115 31.240 1.00102.51 O
ANISOU 3508 O GLU B 191 19063 7930 11956 179 1941 3330 O
ATOM 3509 CB GLU B 191 53.918 -56.899 34.038 1.00119.78 C
ANISOU 3509 CB GLU B 191 21314 10439 13759 225 1843 3715 C
ATOM 3510 CG GLU B 191 55.153 -57.661 33.630 1.00137.16 C
ANISOU 3510 CG GLU B 191 23612 12401 16101 547 1636 3723 C
ATOM 3511 CD GLU B 191 56.392 -56.795 33.731 1.00155.06 C
ANISOU 3511 CD GLU B 191 25642 14893 18380 832 1513 3564 C
ATOM 3512 OE1 GLU B 191 56.307 -55.713 34.343 1.00159.24 O
ANISOU 3512 OE1 GLU B 191 25978 15763 18763 804 1551 3503 O
ATOM 3513 OE2 GLU B 191 57.434 -57.198 33.190 1.00162.65 O
ANISOU 3513 OE2 GLU B 191 26602 15683 19515 1084 1386 3493 O
ATOM 3514 N LEU B 192 52.465 -55.749 30.928 1.00110.36 N
ANISOU 3514 N LEU B 192 19686 9410 12837 -95 2150 3121 N
ATOM 3515 CA LEU B 192 52.193 -56.273 29.595 1.00107.10 C
ANISOU 3515 CA LEU B 192 19309 8789 12593 -176 2203 2949 C
ATOM 3516 C LEU B 192 53.338 -56.010 28.621 1.00 96.10 C
ANISOU 3516 C LEU B 192 17858 7368 11286 124 2107 2767 C
ATOM 3517 O LEU B 192 53.588 -56.833 27.731 1.00 84.55 O
ANISOU 3517 O LEU B 192 16530 5626 9970 156 2100 2672 O
ATOM 3518 CB LEU B 192 50.892 -55.675 29.059 1.00105.18 C
ANISOU 3518 CB LEU B 192 18896 8719 12348 -466 2357 2828 C
ATOM 3519 CG LEU B 192 50.261 -56.314 27.819 1.00 96.56 C
ANISOU 3519 CG LEU B 192 17878 7396 11415 -655 2424 2675 C
ATOM 3520 CD1 LEU B 192 50.252 -57.831 27.925 1.00 90.24 C
ANISOU 3520 CD1 LEU B 192 17366 6188 10734 -742 2413 2786 C
ATOM 3521 CD2 LEU B 192 48.851 -55.781 27.619 1.00 94.67 C
ANISOU 3521 CD2 LEU B 192 17467 7326 11175 -982 2562 2616 C
ATOM 3522 N ALA B 193 54.072 -54.907 28.801 1.00 93.28 N
ANISOU 3522 N ALA B 193 17308 7285 10849 345 2040 2717 N
ATOM 3523 CA ALA B 193 55.133 -54.547 27.865 1.00 88.36 C
ANISOU 3523 CA ALA B 193 16595 6667 10311 617 1982 2540 C
ATOM 3524 C ALA B 193 56.264 -55.565 27.860 1.00 95.34 C
ANISOU 3524 C ALA B 193 17648 7247 11331 852 1860 2591 C
ATOM 3525 O ALA B 193 57.075 -55.572 26.927 1.00 94.54 O
ANISOU 3525 O ALA B 193 17504 7071 11345 1049 1844 2432 O
ATOM 3526 CB ALA B 193 55.685 -53.164 28.192 1.00 74.06 C
ANISOU 3526 CB ALA B 193 14537 5201 8402 790 1935 2497 C
ATOM 3527 N ALA B 194 56.339 -56.416 28.882 1.00 96.36 N
ANISOU 3527 N ALA B 194 17962 7196 11454 837 1778 2812 N
ATOM 3528 CA ALA B 194 57.327 -57.485 28.892 1.00 92.43 C
ANISOU 3528 CA ALA B 194 17632 6371 11117 1050 1648 2876 C
ATOM 3529 C ALA B 194 57.095 -58.490 27.773 1.00 99.46 C
ANISOU 3529 C ALA B 194 18672 6940 12180 975 1722 2746 C
ATOM 3530 O ALA B 194 58.002 -59.270 27.463 1.00103.81 O
ANISOU 3530 O ALA B 194 19315 7222 12906 1186 1632 2723 O
ATOM 3531 CB ALA B 194 57.315 -58.205 30.242 1.00 93.49 C
ANISOU 3531 CB ALA B 194 17963 6366 11191 1019 1548 3163 C
ATOM 3532 N ARG B 195 55.902 -58.508 27.179 1.00104.97 N
ANISOU 3532 N ARG B 195 19392 7646 12848 679 1874 2655 N
ATOM 3533 CA ARG B 195 55.564 -59.467 26.131 1.00105.46 C
ANISOU 3533 CA ARG B 195 19616 7394 13060 568 1938 2520 C
ATOM 3534 C ARG B 195 55.347 -58.837 24.759 1.00 98.47 C
ANISOU 3534 C ARG B 195 18615 6626 12175 537 2038 2242 C
ATOM 3535 O ARG B 195 55.795 -59.401 23.759 1.00 92.49 O
ANISOU 3535 O ARG B 195 17949 5649 11545 636 2045 2074 O
ATOM 3536 CB ARG B 195 54.313 -60.262 26.538 1.00109.13 C
ANISOU 3536 CB ARG B 195 20253 7687 13525 214 2016 2651 C
ATOM 3537 CG ARG B 195 54.396 -60.876 27.939 1.00109.33 C
ANISOU 3537 CG ARG B 195 20424 7602 13514 207 1944 2952 C
ATOM 3538 CD ARG B 195 53.070 -61.469 28.368 1.00100.49 C
ANISOU 3538 CD ARG B 195 19431 6372 12378 -173 2064 3082 C
ATOM 3539 NE ARG B 195 52.781 -62.723 27.685 1.00107.33 N
ANISOU 3539 NE ARG B 195 20511 6828 13439 -301 2088 3028 N
ATOM 3540 CZ ARG B 195 51.665 -63.424 27.856 1.00119.85 C
ANISOU 3540 CZ ARG B 195 22221 8240 15075 -645 2193 3113 C
ATOM 3541 NH1 ARG B 195 50.727 -62.985 28.685 1.00126.22 N
ANISOU 3541 NH1 ARG B 195 22947 9262 15749 -890 2301 3256 N
ATOM 3542 NH2 ARG B 195 51.488 -64.566 27.201 1.00120.59 N
ANISOU 3542 NH2 ARG B 195 22511 7942 15367 -747 2198 3046 N
ATOM 3543 N THR B 196 54.693 -57.677 24.666 1.00 84.24 N
ANISOU 3543 N THR B 196 16620 5156 10232 412 2112 2183 N
ATOM 3544 CA THR B 196 54.364 -57.121 23.359 1.00 81.74 C
ANISOU 3544 CA THR B 196 16229 4927 9903 352 2199 1938 C
ATOM 3545 C THR B 196 54.289 -55.600 23.417 1.00 91.42 C
ANISOU 3545 C THR B 196 17189 6559 10987 392 2229 1896 C
ATOM 3546 O THR B 196 53.930 -55.012 24.441 1.00 96.60 O
ANISOU 3546 O THR B 196 17723 7435 11547 327 2217 2042 O
ATOM 3547 CB THR B 196 53.033 -57.676 22.830 1.00 83.45 C
ANISOU 3547 CB THR B 196 16568 4984 10154 -9 2278 1877 C
ATOM 3548 OG1 THR B 196 52.745 -57.091 21.553 1.00 93.38 O
ANISOU 3548 OG1 THR B 196 17774 6326 11380 -60 2333 1640 O
ATOM 3549 CG2 THR B 196 51.907 -57.343 23.782 1.00 83.36 C
ANISOU 3549 CG2 THR B 196 16467 5141 10066 -284 2324 2041 C
ATOM 3550 N ARG B 197 54.645 -54.972 22.302 1.00 74.86 N
ANISOU 3550 N ARG B 197 15013 4554 8876 502 2272 1692 N
ATOM 3551 CA ARG B 197 54.466 -53.539 22.127 1.00 83.34 C
ANISOU 3551 CA ARG B 197 15853 5981 9833 515 2310 1627 C
ATOM 3552 C ARG B 197 53.119 -53.173 21.525 1.00 84.90 C
ANISOU 3552 C ARG B 197 16032 6246 9979 210 2380 1541 C
ATOM 3553 O ARG B 197 52.810 -51.981 21.414 1.00 74.30 O
ANISOU 3553 O ARG B 197 14494 5188 8550 192 2404 1501 O
ATOM 3554 CB ARG B 197 55.577 -52.973 21.244 1.00 78.11 C
ANISOU 3554 CB ARG B 197 15109 5392 9177 792 2331 1468 C
ATOM 3555 CG ARG B 197 56.935 -53.073 21.882 1.00 89.71 C
ANISOU 3555 CG ARG B 197 16513 6854 10719 1097 2250 1549 C
ATOM 3556 CD ARG B 197 58.006 -52.441 21.012 1.00 92.54 C
ANISOU 3556 CD ARG B 197 16744 7310 11105 1346 2298 1392 C
ATOM 3557 NE ARG B 197 59.268 -52.334 21.736 1.00 92.03 N
ANISOU 3557 NE ARG B 197 16549 7286 11131 1620 2201 1476 N
ATOM 3558 CZ ARG B 197 60.438 -52.062 21.171 1.00 90.86 C
ANISOU 3558 CZ ARG B 197 16278 7166 11081 1862 2224 1369 C
ATOM 3559 NH1 ARG B 197 60.525 -51.873 19.860 1.00 89.74 N
ANISOU 3559 NH1 ARG B 197 16147 7022 10928 1870 2361 1178 N
ATOM 3560 NH2 ARG B 197 61.524 -51.985 21.925 1.00 94.29 N
ANISOU 3560 NH2 ARG B 197 16575 7625 11625 2088 2103 1453 N
ATOM 3561 N ALA B 198 52.305 -54.156 21.135 1.00 99.07 N
ANISOU 3561 N ALA B 198 18018 7780 11844 -36 2400 1511 N
ATOM 3562 CA ALA B 198 51.052 -53.818 20.475 1.00 93.70 C
ANISOU 3562 CA ALA B 198 17315 7145 11142 -336 2443 1411 C
ATOM 3563 C ALA B 198 50.155 -52.991 21.375 1.00 80.48 C
ANISOU 3563 C ALA B 198 15415 5749 9414 -509 2468 1541 C
ATOM 3564 O ALA B 198 49.312 -52.239 20.875 1.00 82.35 O
ANISOU 3564 O ALA B 198 15533 6135 9621 -681 2493 1460 O
ATOM 3565 CB ALA B 198 50.318 -55.086 20.038 1.00 76.10 C
ANISOU 3565 CB ALA B 198 15317 4570 9027 -598 2445 1362 C
ATOM 3566 N PHE B 199 50.345 -53.079 22.689 1.00 86.40 N
ANISOU 3566 N PHE B 199 16105 6578 10146 -457 2457 1737 N
ATOM 3567 CA PHE B 199 49.538 -52.320 23.629 1.00 99.23 C
ANISOU 3567 CA PHE B 199 17518 8475 11710 -606 2497 1855 C
ATOM 3568 C PHE B 199 50.342 -51.243 24.341 1.00105.80 C
ANISOU 3568 C PHE B 199 18156 9606 12437 -344 2452 1906 C
ATOM 3569 O PHE B 199 49.902 -50.730 25.374 1.00112.12 O
ANISOU 3569 O PHE B 199 18811 10616 13174 -415 2473 2023 O
ATOM 3570 CB PHE B 199 48.902 -53.267 24.645 1.00102.86 C
ANISOU 3570 CB PHE B 199 18079 8792 12210 -818 2538 2040 C
ATOM 3571 CG PHE B 199 48.128 -54.389 24.019 1.00104.15 C
ANISOU 3571 CG PHE B 199 18428 8637 12508 -1094 2577 1992 C
ATOM 3572 CD1 PHE B 199 46.802 -54.217 23.660 1.00 99.74 C
ANISOU 3572 CD1 PHE B 199 17768 8115 12014 -1434 2650 1933 C
ATOM 3573 CD2 PHE B 199 48.725 -55.617 23.792 1.00106.86 C
ANISOU 3573 CD2 PHE B 199 19034 8633 12936 -1018 2530 1998 C
ATOM 3574 CE1 PHE B 199 46.086 -55.248 23.087 1.00103.73 C
ANISOU 3574 CE1 PHE B 199 18431 8316 12665 -1709 2667 1872 C
ATOM 3575 CE2 PHE B 199 48.011 -56.655 23.218 1.00107.15 C
ANISOU 3575 CE2 PHE B 199 19241 8362 13110 -1280 2554 1938 C
ATOM 3576 CZ PHE B 199 46.690 -56.469 22.867 1.00107.34 C
ANISOU 3576 CZ PHE B 199 19161 8425 13197 -1633 2618 1871 C
ATOM 3577 N SER B 200 51.503 -50.876 23.810 1.00106.36 N
ANISOU 3577 N SER B 200 18216 9699 12495 -52 2400 1810 N
ATOM 3578 CA SER B 200 52.282 -49.805 24.410 1.00105.09 C
ANISOU 3578 CA SER B 200 17856 9812 12262 182 2350 1836 C
ATOM 3579 C SER B 200 51.877 -48.477 23.775 1.00 96.14 C
ANISOU 3579 C SER B 200 16499 8944 11086 161 2381 1711 C
ATOM 3580 O SER B 200 51.436 -48.436 22.623 1.00 93.92 O
ANISOU 3580 O SER B 200 16262 8598 10825 64 2421 1580 O
ATOM 3581 CB SER B 200 53.779 -50.058 24.210 1.00 99.16 C
ANISOU 3581 CB SER B 200 17174 8953 11548 503 2286 1806 C
ATOM 3582 OG SER B 200 54.212 -51.174 24.968 1.00 95.68 O
ANISOU 3582 OG SER B 200 16914 8289 11151 549 2224 1949 O
ATOM 3583 N VAL B 201 52.029 -47.385 24.527 1.00 88.64 N
ANISOU 3583 N VAL B 201 15324 8281 10074 250 2351 1749 N
ATOM 3584 CA VAL B 201 51.706 -46.062 24.010 1.00 85.63 C
ANISOU 3584 CA VAL B 201 14714 8154 9668 253 2364 1642 C
ATOM 3585 C VAL B 201 52.757 -45.049 24.455 1.00 88.25 C
ANISOU 3585 C VAL B 201 14871 8689 9971 518 2303 1629 C
ATOM 3586 O VAL B 201 53.246 -45.097 25.592 1.00 76.09 O
ANISOU 3586 O VAL B 201 13321 7193 8397 606 2248 1737 O
ATOM 3587 CB VAL B 201 50.297 -45.634 24.466 1.00 81.33 C
ANISOU 3587 CB VAL B 201 14022 7774 9107 -17 2411 1689 C
ATOM 3588 CG1 VAL B 201 50.265 -45.417 25.984 1.00 74.55 C
ANISOU 3588 CG1 VAL B 201 13071 7068 8187 -14 2396 1826 C
ATOM 3589 CG2 VAL B 201 49.866 -44.389 23.719 1.00 87.37 C
ANISOU 3589 CG2 VAL B 201 14575 8754 9868 -29 2413 1574 C
ATOM 3590 N CYS B 202 53.089 -44.125 23.544 1.00 91.55 N
ANISOU 3590 N CYS B 202 15168 9221 10398 631 2312 1499 N
ATOM 3591 CA CYS B 202 53.983 -42.995 23.783 1.00 83.84 C
ANISOU 3591 CA CYS B 202 13995 8442 9419 852 2271 1463 C
ATOM 3592 C CYS B 202 53.202 -41.709 24.043 1.00 67.33 C
ANISOU 3592 C CYS B 202 11649 6626 7309 760 2249 1438 C
ATOM 3593 O CYS B 202 52.458 -41.262 23.166 1.00 64.78 O
ANISOU 3593 O CYS B 202 11264 6357 6992 649 2274 1362 O
ATOM 3594 CB CYS B 202 54.909 -42.823 22.577 1.00 91.08 C
ANISOU 3594 CB CYS B 202 14951 9289 10368 1037 2318 1341 C
ATOM 3595 SG CYS B 202 56.184 -41.547 22.726 1.00 93.98 S
ANISOU 3595 SG CYS B 202 15093 9851 10763 1312 2303 1297 S
ATOM 3596 N ASP B 203 53.324 -41.140 25.245 1.00 64.63 N
ANISOU 3596 N ASP B 203 11175 6446 6935 799 2196 1505 N
ATOM 3597 CA ASP B 203 52.590 -39.918 25.568 1.00 61.16 C
ANISOU 3597 CA ASP B 203 10493 6260 6485 719 2177 1475 C
ATOM 3598 C ASP B 203 53.325 -39.110 26.629 1.00 64.34 C
ANISOU 3598 C ASP B 203 10778 6810 6858 872 2110 1500 C
ATOM 3599 O ASP B 203 54.239 -39.593 27.296 1.00 86.42 O
ANISOU 3599 O ASP B 203 13690 9523 9623 1006 2073 1570 O
ATOM 3600 CB ASP B 203 51.152 -40.161 26.018 1.00 71.29 C
ANISOU 3600 CB ASP B 203 11753 7598 7735 449 2229 1537 C
ATOM 3601 CG ASP B 203 50.303 -38.906 25.884 1.00 81.26 C
ANISOU 3601 CG ASP B 203 12762 9100 9014 370 2230 1472 C
ATOM 3602 OD1 ASP B 203 49.962 -38.555 24.733 1.00 87.05 O
ANISOU 3602 OD1 ASP B 203 13448 9838 9791 342 2234 1391 O
ATOM 3603 OD2 ASP B 203 50.038 -38.232 26.909 1.00 83.15 O
ANISOU 3603 OD2 ASP B 203 12864 9515 9213 352 2223 1499 O
ATOM 3604 N GLU B 204 52.904 -37.857 26.768 1.00 48.40 N
ANISOU 3604 N GLU B 204 8537 5004 4849 851 2087 1443 N
ATOM 3605 CA GLU B 204 53.457 -36.967 27.778 1.00 55.33 C
ANISOU 3605 CA GLU B 204 9305 6024 5692 969 2028 1452 C
ATOM 3606 C GLU B 204 53.020 -37.405 29.176 1.00 62.63 C
ANISOU 3606 C GLU B 204 10317 6985 6495 861 2033 1566 C
ATOM 3607 O GLU B 204 51.867 -37.793 29.402 1.00 59.32 O
ANISOU 3607 O GLU B 204 9910 6591 6038 647 2102 1609 O
ATOM 3608 CB GLU B 204 53.028 -35.522 27.537 1.00 55.14 C
ANISOU 3608 CB GLU B 204 9036 6196 5717 958 2005 1357 C
ATOM 3609 CG GLU B 204 53.298 -34.998 26.148 1.00 59.07 C
ANISOU 3609 CG GLU B 204 9454 6671 6318 1033 1998 1259 C
ATOM 3610 CD GLU B 204 52.732 -33.599 25.948 1.00 65.59 C
ANISOU 3610 CD GLU B 204 10054 7676 7191 1000 1960 1187 C
ATOM 3611 OE1 GLU B 204 52.108 -33.072 26.897 1.00 66.25 O
ANISOU 3611 OE1 GLU B 204 10042 7902 7231 922 1955 1201 O
ATOM 3612 OE2 GLU B 204 52.907 -33.024 24.849 1.00 73.17 O
ANISOU 3612 OE2 GLU B 204 10948 8629 8223 1053 1940 1119 O
ATOM 3613 N ARG B 205 53.941 -37.273 30.124 1.00 60.19 N
ANISOU 3613 N ARG B 205 10066 6688 6114 1010 1968 1620 N
ATOM 3614 CA ARG B 205 53.735 -37.604 31.527 1.00 54.51 C
ANISOU 3614 CA ARG B 205 9464 6004 5242 942 1956 1736 C
ATOM 3615 C ARG B 205 53.779 -36.317 32.320 1.00 52.50 C
ANISOU 3615 C ARG B 205 9067 5957 4922 989 1923 1688 C
ATOM 3616 O ARG B 205 54.834 -35.680 32.405 1.00 66.74 O
ANISOU 3616 O ARG B 205 10833 7783 6741 1194 1843 1655 O
ATOM 3617 CB ARG B 205 54.882 -38.476 32.033 1.00 77.28 C
ANISOU 3617 CB ARG B 205 12567 8725 8070 1102 1872 1846 C
ATOM 3618 CG ARG B 205 54.730 -39.008 33.446 1.00100.74 C
ANISOU 3618 CG ARG B 205 15721 11695 10860 1033 1844 1995 C
ATOM 3619 CD ARG B 205 55.673 -40.167 33.724 1.00108.44 C
ANISOU 3619 CD ARG B 205 16939 12453 11809 1158 1747 2124 C
ATOM 3620 NE ARG B 205 55.729 -40.429 35.160 1.00115.64 N
ANISOU 3620 NE ARG B 205 18027 13387 12523 1137 1681 2271 N
ATOM 3621 CZ ARG B 205 56.624 -41.219 35.742 1.00128.37 C
ANISOU 3621 CZ ARG B 205 19852 14847 14075 1270 1544 2406 C
ATOM 3622 NH1 ARG B 205 57.558 -41.820 35.011 1.00133.44 N
ANISOU 3622 NH1 ARG B 205 20534 15303 14863 1440 1464 2402 N
ATOM 3623 NH2 ARG B 205 56.602 -41.386 37.060 1.00131.83 N
ANISOU 3623 NH2 ARG B 205 20463 15320 14306 1240 1481 2543 N
ATOM 3624 N TRP B 206 52.664 -35.962 32.951 1.00 50.67 N
ANISOU 3624 N TRP B 206 8768 5871 4613 806 1995 1689 N
ATOM 3625 CA TRP B 206 52.597 -34.713 33.692 1.00 65.09 C
ANISOU 3625 CA TRP B 206 10466 7893 6373 837 1981 1625 C
ATOM 3626 C TRP B 206 52.402 -34.925 35.179 1.00 75.25 C
ANISOU 3626 C TRP B 206 11902 9247 7441 769 2004 1722 C
ATOM 3627 O TRP B 206 51.461 -35.600 35.615 1.00 70.84 O
ANISOU 3627 O TRP B 206 11418 8697 6803 575 2110 1798 O
ATOM 3628 CB TRP B 206 51.497 -33.794 33.153 1.00 65.70 C
ANISOU 3628 CB TRP B 206 10300 8119 6543 712 2053 1508 C
ATOM 3629 CG TRP B 206 51.765 -33.369 31.775 1.00 59.20 C
ANISOU 3629 CG TRP B 206 9342 7250 5900 796 2009 1415 C
ATOM 3630 CD1 TRP B 206 51.251 -33.886 30.627 1.00 64.39 C
ANISOU 3630 CD1 TRP B 206 9979 7826 6661 712 2044 1399 C
ATOM 3631 CD2 TRP B 206 52.660 -32.328 31.391 1.00 61.97 C
ANISOU 3631 CD2 TRP B 206 9580 7628 6337 985 1928 1335 C
ATOM 3632 NE1 TRP B 206 51.769 -33.220 29.541 1.00 71.84 N
ANISOU 3632 NE1 TRP B 206 10814 8750 7733 836 1986 1312 N
ATOM 3633 CE2 TRP B 206 52.639 -32.258 29.986 1.00 69.46 C
ANISOU 3633 CE2 TRP B 206 10445 8511 7435 1002 1921 1276 C
ATOM 3634 CE3 TRP B 206 53.474 -31.442 32.104 1.00 66.77 C
ANISOU 3634 CE3 TRP B 206 10160 8308 6900 1140 1867 1314 C
ATOM 3635 CZ2 TRP B 206 53.402 -31.335 29.275 1.00 70.15 C
ANISOU 3635 CZ2 TRP B 206 10419 8600 7635 1159 1863 1205 C
ATOM 3636 CZ3 TRP B 206 54.237 -30.529 31.397 1.00 66.80 C
ANISOU 3636 CZ3 TRP B 206 10039 8312 7031 1300 1813 1244 C
ATOM 3637 CH2 TRP B 206 54.196 -30.482 29.997 1.00 65.79 C
ANISOU 3637 CH2 TRP B 206 9824 8113 7059 1304 1815 1195 C
ATOM 3638 N ALA B 207 53.260 -34.259 35.943 1.00 84.58 N
ANISOU 3638 N ALA B 207 13124 10492 8522 927 1912 1716 N
ATOM 3639 CA ALA B 207 53.191 -34.322 37.389 1.00 94.09 C
ANISOU 3639 CA ALA B 207 14493 11773 9482 886 1915 1799 C
ATOM 3640 C ALA B 207 51.933 -33.642 37.905 1.00 96.39 C
ANISOU 3640 C ALA B 207 14658 12263 9703 698 2062 1730 C
ATOM 3641 O ALA B 207 51.426 -34.028 38.961 1.00104.95 O
ANISOU 3641 O ALA B 207 15884 13405 10589 576 2142 1815 O
ATOM 3642 CB ALA B 207 54.438 -33.702 38.017 1.00104.74 C
ANISOU 3642 CB ALA B 207 15918 13147 10731 1116 1761 1795 C
ATOM 3643 N ASP B 208 51.391 -32.663 37.170 1.00 93.37 N
ANISOU 3643 N ASP B 208 14015 11983 9479 672 2107 1581 N
ATOM 3644 CA ASP B 208 50.258 -31.907 37.668 1.00 86.56 C
ANISOU 3644 CA ASP B 208 13010 11316 8564 525 2243 1495 C
ATOM 3645 C ASP B 208 49.296 -31.590 36.541 1.00 61.74 C
ANISOU 3645 C ASP B 208 9619 8208 5630 424 2314 1398 C
ATOM 3646 O ASP B 208 49.594 -31.769 35.357 1.00 64.14 O
ANISOU 3646 O ASP B 208 9863 8398 6109 483 2243 1382 O
ATOM 3647 CB ASP B 208 50.704 -30.528 38.185 1.00 97.39 C
ANISOU 3647 CB ASP B 208 14301 12818 9884 651 2191 1374 C
ATOM 3648 CG ASP B 208 51.802 -30.589 39.222 1.00116.86 C
ANISOU 3648 CG ASP B 208 17000 15265 12139 796 2081 1446 C
ATOM 3649 OD1 ASP B 208 52.019 -31.642 39.853 1.00129.14 O
ANISOU 3649 OD1 ASP B 208 18793 16741 13534 766 2065 1596 O
ATOM 3650 OD2 ASP B 208 52.472 -29.547 39.391 1.00117.98 O
ANISOU 3650 OD2 ASP B 208 17089 15466 12273 949 1996 1354 O
ATOM 3651 N ASP B 209 48.115 -31.131 36.949 1.00 55.41 N
ANISOU 3651 N ASP B 209 8684 7574 4796 275 2464 1334 N
ATOM 3652 CA ASP B 209 47.059 -30.816 36.008 1.00 73.38 C
ANISOU 3652 CA ASP B 209 10723 9907 7250 176 2542 1249 C
ATOM 3653 C ASP B 209 47.345 -29.498 35.317 1.00 74.38 C
ANISOU 3653 C ASP B 209 10657 10078 7526 310 2446 1101 C
ATOM 3654 O ASP B 209 46.842 -29.258 34.214 1.00 77.85 O
ANISOU 3654 O ASP B 209 10934 10507 8137 290 2441 1046 O
ATOM 3655 CB ASP B 209 45.716 -30.801 36.733 1.00102.33 C
ANISOU 3655 CB ASP B 209 14298 13741 10841 -10 2754 1234 C
ATOM 3656 CG ASP B 209 45.285 -32.190 37.161 1.00118.68 C
ANISOU 3656 CG ASP B 209 16542 15739 12814 -166 2870 1401 C
ATOM 3657 OD1 ASP B 209 45.883 -33.175 36.653 1.00122.76 O
ANISOU 3657 OD1 ASP B 209 17220 16060 13361 -144 2779 1509 O
ATOM 3658 OD2 ASP B 209 44.380 -32.293 38.018 1.00123.59 O
ANISOU 3658 OD2 ASP B 209 17142 16486 13330 -304 3060 1424 O
ATOM 3659 N LEU B 210 48.142 -28.645 35.971 1.00 70.47 N
ANISOU 3659 N LEU B 210 10192 9626 6959 446 2372 1046 N
ATOM 3660 CA LEU B 210 48.402 -27.257 35.605 1.00 62.99 C
ANISOU 3660 CA LEU B 210 9076 8730 6129 569 2302 909 C
ATOM 3661 C LEU B 210 49.561 -27.150 34.626 1.00 68.05 C
ANISOU 3661 C LEU B 210 9728 9223 6905 741 2138 931 C
ATOM 3662 O LEU B 210 49.561 -26.276 33.747 1.00 63.48 O
ANISOU 3662 O LEU B 210 8988 8642 6491 805 2082 851 O
ATOM 3663 CB LEU B 210 48.715 -26.427 36.852 1.00 54.86 C
ANISOU 3663 CB LEU B 210 8092 7813 4940 627 2319 841 C
ATOM 3664 CG LEU B 210 49.117 -24.973 36.613 1.00 40.28 C
ANISOU 3664 CG LEU B 210 6099 6001 3206 764 2243 704 C
ATOM 3665 CD1 LEU B 210 48.038 -24.223 35.852 1.00 43.91 C
ANISOU 3665 CD1 LEU B 210 6307 6526 3851 698 2302 585 C
ATOM 3666 CD2 LEU B 210 49.430 -24.290 37.909 1.00 41.95 C
ANISOU 3666 CD2 LEU B 210 6393 6318 3228 813 2269 635 C
ATOM 3667 N ALA B 211 50.602 -27.948 34.863 1.00 73.76 N
ANISOU 3667 N ALA B 211 10647 9831 7549 833 2065 1039 N
ATOM 3668 CA ALA B 211 51.799 -27.880 34.034 1.00 58.71 C
ANISOU 3668 CA ALA B 211 8749 7797 5761 1017 1940 1058 C
ATOM 3669 C ALA B 211 51.494 -28.100 32.565 1.00 59.93 C
ANISOU 3669 C ALA B 211 8802 7867 6101 984 1927 1045 C
ATOM 3670 O ALA B 211 52.004 -27.332 31.735 1.00 57.14 O
ANISOU 3670 O ALA B 211 8342 7484 5885 1095 1856 995 O
ATOM 3671 CB ALA B 211 52.829 -28.896 34.538 1.00 48.87 C
ANISOU 3671 CB ALA B 211 7733 6440 4396 1116 1888 1180 C
ATOM 3672 N PRO B 212 50.731 -29.124 32.162 1.00 62.53 N
ANISOU 3672 N PRO B 212 9177 8150 6432 839 1992 1095 N
ATOM 3673 CA PRO B 212 50.368 -29.217 30.736 1.00 50.09 C
ANISOU 3673 CA PRO B 212 7514 6512 5005 810 1980 1069 C
ATOM 3674 C PRO B 212 49.598 -28.020 30.219 1.00 33.28 C
ANISOU 3674 C PRO B 212 5176 4495 2975 784 1985 968 C
ATOM 3675 O PRO B 212 49.826 -27.608 29.075 1.00 31.69 O
ANISOU 3675 O PRO B 212 4911 4241 2890 850 1921 940 O
ATOM 3676 CB PRO B 212 49.525 -30.495 30.670 1.00 56.26 C
ANISOU 3676 CB PRO B 212 8390 7249 5736 635 2073 1142 C
ATOM 3677 CG PRO B 212 49.026 -30.684 32.068 1.00 66.23 C
ANISOU 3677 CG PRO B 212 9706 8612 6845 532 2164 1180 C
ATOM 3678 CD PRO B 212 50.155 -30.228 32.946 1.00 70.39 C
ANISOU 3678 CD PRO B 212 10315 9143 7286 692 2085 1185 C
ATOM 3679 N LYS B 213 48.737 -27.409 31.043 1.00 37.96 N
ANISOU 3679 N LYS B 213 5668 5238 3517 701 2064 911 N
ATOM 3680 CA LYS B 213 47.999 -26.242 30.571 1.00 51.41 C
ANISOU 3680 CA LYS B 213 7168 7039 5327 700 2075 808 C
ATOM 3681 C LYS B 213 48.932 -25.067 30.313 1.00 70.89 C
ANISOU 3681 C LYS B 213 9581 9479 7873 866 1955 759 C
ATOM 3682 O LYS B 213 48.884 -24.449 29.238 1.00 82.33 O
ANISOU 3682 O LYS B 213 10941 10898 9443 916 1899 734 O
ATOM 3683 CB LYS B 213 46.944 -25.839 31.600 1.00 36.41 C
ANISOU 3683 CB LYS B 213 5166 5305 3363 592 2210 737 C
ATOM 3684 CG LYS B 213 45.935 -26.911 31.973 1.00 52.32 C
ANISOU 3684 CG LYS B 213 7208 7369 5302 406 2363 792 C
ATOM 3685 CD LYS B 213 44.806 -26.304 32.815 1.00 65.89 C
ANISOU 3685 CD LYS B 213 8765 9274 6996 313 2521 693 C
ATOM 3686 CE LYS B 213 43.689 -27.310 33.122 1.00 78.00 C
ANISOU 3686 CE LYS B 213 10281 10870 8484 117 2704 755 C
ATOM 3687 NZ LYS B 213 43.731 -28.530 32.273 1.00 86.86 N
ANISOU 3687 NZ LYS B 213 11515 11848 9640 46 2685 881 N
ATOM 3688 N ILE B 214 49.873 -24.832 31.237 1.00 69.25 N
ANISOU 3688 N ILE B 214 9452 9271 7587 957 1917 763 N
ATOM 3689 CA ILE B 214 50.830 -23.741 31.064 1.00 57.98 C
ANISOU 3689 CA ILE B 214 7977 7820 6234 1106 1817 726 C
ATOM 3690 C ILE B 214 51.757 -24.034 29.901 1.00 54.88 C
ANISOU 3690 C ILE B 214 7626 7285 5940 1200 1732 791 C
ATOM 3691 O ILE B 214 52.031 -23.160 29.068 1.00 53.17 O
ANISOU 3691 O ILE B 214 7326 7040 5837 1256 1671 766 O
ATOM 3692 CB ILE B 214 51.641 -23.509 32.348 1.00 31.47 C
ANISOU 3692 CB ILE B 214 4706 4505 2746 1192 1808 722 C
ATOM 3693 CG1 ILE B 214 50.748 -22.985 33.463 1.00 47.28 C
ANISOU 3693 CG1 ILE B 214 6663 6655 4645 1105 1906 628 C
ATOM 3694 CG2 ILE B 214 52.777 -22.558 32.064 1.00 30.19 C
ANISOU 3694 CG2 ILE B 214 4502 4304 2664 1349 1710 703 C
ATOM 3695 CD1 ILE B 214 51.481 -22.810 34.786 1.00 65.67 C
ANISOU 3695 CD1 ILE B 214 9120 9040 6793 1185 1904 620 C
ATOM 3696 N TYR B 215 52.266 -25.264 29.835 1.00 44.06 N
ANISOU 3696 N TYR B 215 6399 5821 4523 1215 1739 874 N
ATOM 3697 CA TYR B 215 53.248 -25.584 28.816 1.00 31.49 C
ANISOU 3697 CA TYR B 215 4854 4092 3019 1319 1688 918 C
ATOM 3698 C TYR B 215 52.651 -25.507 27.426 1.00 36.09 C
ANISOU 3698 C TYR B 215 5380 4634 3698 1256 1681 899 C
ATOM 3699 O TYR B 215 53.290 -24.991 26.508 1.00 57.36 O
ANISOU 3699 O TYR B 215 8051 7262 6481 1332 1634 900 O
ATOM 3700 CB TYR B 215 53.841 -26.964 29.046 1.00 29.23 C
ANISOU 3700 CB TYR B 215 4737 3704 2663 1358 1718 996 C
ATOM 3701 CG TYR B 215 54.745 -27.360 27.909 1.00 46.18 C
ANISOU 3701 CG TYR B 215 6930 5710 4908 1462 1703 1021 C
ATOM 3702 CD1 TYR B 215 56.034 -26.852 27.824 1.00 50.99 C
ANISOU 3702 CD1 TYR B 215 7526 6277 5572 1637 1675 1043 C
ATOM 3703 CD2 TYR B 215 54.320 -28.243 26.919 1.00 46.49 C
ANISOU 3703 CD2 TYR B 215 7032 5661 4973 1384 1737 1025 C
ATOM 3704 CE1 TYR B 215 56.878 -27.205 26.785 1.00 54.37 C
ANISOU 3704 CE1 TYR B 215 7997 6574 6088 1728 1695 1069 C
ATOM 3705 CE2 TYR B 215 55.164 -28.611 25.872 1.00 45.56 C
ANISOU 3705 CE2 TYR B 215 6973 5409 4928 1480 1749 1032 C
ATOM 3706 CZ TYR B 215 56.444 -28.087 25.811 1.00 50.73 C
ANISOU 3706 CZ TYR B 215 7609 6020 5647 1653 1737 1054 C
ATOM 3707 OH TYR B 215 57.300 -28.435 24.786 1.00 48.94 O
ANISOU 3707 OH TYR B 215 7443 5659 5492 1745 1780 1070 O
ATOM 3708 N HIS B 216 51.441 -26.039 27.234 1.00 37.97 N
ANISOU 3708 N HIS B 216 5610 4913 3903 1116 1740 893 N
ATOM 3709 CA HIS B 216 50.854 -26.026 25.902 1.00 49.07 C
ANISOU 3709 CA HIS B 216 6988 6290 5365 1073 1740 884 C
ATOM 3710 C HIS B 216 50.309 -24.662 25.522 1.00 47.44 C
ANISOU 3710 C HIS B 216 6633 6167 5224 1092 1715 835 C
ATOM 3711 O HIS B 216 50.347 -24.308 24.333 1.00 52.03 O
ANISOU 3711 O HIS B 216 7215 6700 5855 1131 1685 844 O
ATOM 3712 CB HIS B 216 49.766 -27.096 25.829 1.00 59.99 C
ANISOU 3712 CB HIS B 216 8418 7691 6686 921 1827 909 C
ATOM 3713 CG HIS B 216 50.318 -28.475 25.685 1.00 60.54 C
ANISOU 3713 CG HIS B 216 8664 7627 6710 910 1844 965 C
ATOM 3714 ND1 HIS B 216 50.775 -28.967 24.483 1.00 62.47 N
ANISOU 3714 ND1 HIS B 216 9006 7746 6982 948 1826 971 N
ATOM 3715 CD2 HIS B 216 50.571 -29.435 26.606 1.00 60.96 C
ANISOU 3715 CD2 HIS B 216 8834 7640 6687 881 1881 1018 C
ATOM 3716 CE1 HIS B 216 51.239 -30.192 24.659 1.00 67.16 C
ANISOU 3716 CE1 HIS B 216 9758 8224 7534 945 1859 1015 C
ATOM 3717 NE2 HIS B 216 51.135 -30.496 25.940 1.00 63.85 N
ANISOU 3717 NE2 HIS B 216 9356 7851 7054 908 1887 1053 N
ATOM 3718 N SER B 217 49.948 -23.836 26.513 1.00 56.30 N
ANISOU 3718 N SER B 217 7650 7401 6342 1086 1729 784 N
ATOM 3719 CA SER B 217 49.685 -22.434 26.229 1.00 59.25 C
ANISOU 3719 CA SER B 217 7893 7826 6793 1138 1696 732 C
ATOM 3720 C SER B 217 50.941 -21.734 25.715 1.00 49.73 C
ANISOU 3720 C SER B 217 6722 6527 5647 1248 1605 756 C
ATOM 3721 O SER B 217 50.914 -21.057 24.672 1.00 42.53 O
ANISOU 3721 O SER B 217 5787 5579 4794 1288 1577 771 O
ATOM 3722 CB SER B 217 49.184 -21.763 27.512 1.00 49.49 C
ANISOU 3722 CB SER B 217 6554 6714 5535 1111 1741 646 C
ATOM 3723 OG SER B 217 47.925 -22.294 27.889 1.00 35.19 O
ANISOU 3723 OG SER B 217 4683 5000 3687 995 1856 619 O
ATOM 3724 N CYS B 218 52.064 -21.927 26.416 1.00 40.21 N
ANISOU 3724 N CYS B 218 5579 5284 4416 1300 1577 772 N
ATOM 3725 CA CYS B 218 53.323 -21.318 25.999 1.00 32.94 C
ANISOU 3725 CA CYS B 218 4676 4285 3555 1386 1519 799 C
ATOM 3726 C CYS B 218 53.782 -21.840 24.643 1.00 32.21 C
ANISOU 3726 C CYS B 218 4667 4070 3502 1407 1517 860 C
ATOM 3727 O CYS B 218 54.271 -21.077 23.803 1.00 67.36 O
ANISOU 3727 O CYS B 218 9112 8470 8011 1433 1496 878 O
ATOM 3728 CB CYS B 218 54.387 -21.586 27.058 1.00 58.63 C
ANISOU 3728 CB CYS B 218 7977 7541 6758 1457 1512 814 C
ATOM 3729 SG CYS B 218 54.024 -20.841 28.667 1.00 79.78 S
ANISOU 3729 SG CYS B 218 10588 10365 9358 1454 1526 724 S
ATOM 3730 N PHE B 219 53.603 -23.133 24.397 1.00 28.19 N
ANISOU 3730 N PHE B 219 4249 3510 2953 1384 1555 883 N
ATOM 3731 CA PHE B 219 54.105 -23.727 23.162 1.00 39.52 C
ANISOU 3731 CA PHE B 219 5782 4821 4412 1409 1570 913 C
ATOM 3732 C PHE B 219 53.327 -23.175 21.977 1.00 58.06 C
ANISOU 3732 C PHE B 219 8117 7175 6767 1378 1570 903 C
ATOM 3733 O PHE B 219 53.917 -22.771 20.964 1.00 70.84 O
ANISOU 3733 O PHE B 219 9782 8714 8419 1421 1571 923 O
ATOM 3734 CB PHE B 219 53.989 -25.251 23.242 1.00 51.66 C
ANISOU 3734 CB PHE B 219 7431 6304 5892 1380 1621 921 C
ATOM 3735 CG PHE B 219 54.588 -25.984 22.079 1.00 56.01 C
ANISOU 3735 CG PHE B 219 8104 6720 6456 1413 1657 930 C
ATOM 3736 CD1 PHE B 219 53.897 -26.143 20.889 1.00 69.48 C
ANISOU 3736 CD1 PHE B 219 9864 8407 8128 1350 1672 907 C
ATOM 3737 CD2 PHE B 219 55.819 -26.604 22.222 1.00 48.88 C
ANISOU 3737 CD2 PHE B 219 7282 5712 5580 1516 1693 966 C
ATOM 3738 CE1 PHE B 219 54.465 -26.842 19.839 1.00 68.16 C
ANISOU 3738 CE1 PHE B 219 9836 8114 7947 1375 1719 899 C
ATOM 3739 CE2 PHE B 219 56.378 -27.312 21.192 1.00 49.91 C
ANISOU 3739 CE2 PHE B 219 7535 5710 5719 1551 1753 967 C
ATOM 3740 CZ PHE B 219 55.708 -27.430 19.997 1.00 58.23 C
ANISOU 3740 CZ PHE B 219 8649 6742 6732 1474 1766 923 C
ATOM 3741 N PHE B 220 51.997 -23.073 22.129 1.00 62.69 N
ANISOU 3741 N PHE B 220 8640 7864 7315 1313 1587 882 N
ATOM 3742 CA PHE B 220 51.170 -22.516 21.066 1.00 52.75 C
ANISOU 3742 CA PHE B 220 7370 6630 6043 1319 1600 893 C
ATOM 3743 C PHE B 220 51.498 -21.051 20.807 1.00 54.59 C
ANISOU 3743 C PHE B 220 7544 6861 6338 1400 1568 909 C
ATOM 3744 O PHE B 220 51.645 -20.644 19.647 1.00 52.54 O
ANISOU 3744 O PHE B 220 7358 6537 6067 1454 1577 946 O
ATOM 3745 CB PHE B 220 49.687 -22.653 21.415 1.00 52.02 C
ANISOU 3745 CB PHE B 220 7187 6667 5912 1249 1652 879 C
ATOM 3746 CG PHE B 220 48.777 -21.951 20.445 1.00 50.07 C
ANISOU 3746 CG PHE B 220 6903 6474 5649 1301 1677 909 C
ATOM 3747 CD1 PHE B 220 48.621 -22.410 19.150 1.00 57.36 C
ANISOU 3747 CD1 PHE B 220 7976 7343 6475 1303 1687 955 C
ATOM 3748 CD2 PHE B 220 48.109 -20.799 20.824 1.00 52.26 C
ANISOU 3748 CD2 PHE B 220 7008 6853 5996 1363 1687 889 C
ATOM 3749 CE1 PHE B 220 47.795 -21.741 18.258 1.00 55.75 C
ANISOU 3749 CE1 PHE B 220 7772 7202 6209 1382 1706 1013 C
ATOM 3750 CE2 PHE B 220 47.284 -20.131 19.936 1.00 50.36 C
ANISOU 3750 CE2 PHE B 220 6712 6671 5752 1467 1717 928 C
ATOM 3751 CZ PHE B 220 47.129 -20.602 18.655 1.00 49.33 C
ANISOU 3751 CZ PHE B 220 6753 6506 5485 1489 1734 1008 C
ATOM 3752 N ILE B 221 51.672 -20.248 21.865 1.00 58.99 N
ANISOU 3752 N ILE B 221 7993 7478 6943 1404 1539 879 N
ATOM 3753 CA ILE B 221 51.926 -18.825 21.634 1.00 32.59 C
ANISOU 3753 CA ILE B 221 4597 4129 3655 1457 1518 887 C
ATOM 3754 C ILE B 221 53.285 -18.621 20.968 1.00 30.19 C
ANISOU 3754 C ILE B 221 4389 3704 3380 1485 1516 938 C
ATOM 3755 O ILE B 221 53.431 -17.773 20.078 1.00 23.85 O
ANISOU 3755 O ILE B 221 3621 2846 2593 1530 1541 985 O
ATOM 3756 CB ILE B 221 51.829 -18.033 22.949 1.00 34.46 C
ANISOU 3756 CB ILE B 221 4703 4457 3931 1435 1492 802 C
ATOM 3757 CG1 ILE B 221 50.388 -18.013 23.479 1.00 35.73 C
ANISOU 3757 CG1 ILE B 221 4746 4740 4091 1411 1527 737 C
ATOM 3758 CG2 ILE B 221 52.327 -16.619 22.737 1.00 39.80 C
ANISOU 3758 CG2 ILE B 221 5338 5104 4679 1470 1472 789 C
ATOM 3759 CD1 ILE B 221 49.378 -17.424 22.526 1.00 37.99 C
ANISOU 3759 CD1 ILE B 221 4970 5049 4415 1475 1550 758 C
ATOM 3760 N VAL B 222 54.299 -19.386 21.379 1.00 51.78 N
ANISOU 3760 N VAL B 222 7166 6392 6118 1469 1509 937 N
ATOM 3761 CA VAL B 222 55.667 -19.101 20.944 1.00 56.09 C
ANISOU 3761 CA VAL B 222 7755 6847 6709 1483 1531 972 C
ATOM 3762 C VAL B 222 55.951 -19.697 19.569 1.00 65.57 C
ANISOU 3762 C VAL B 222 9088 7926 7899 1511 1587 1013 C
ATOM 3763 O VAL B 222 56.651 -19.083 18.754 1.00 76.14 O
ANISOU 3763 O VAL B 222 10472 9185 9273 1527 1639 1049 O
ATOM 3764 CB VAL B 222 56.701 -19.581 21.981 1.00 41.87 C
ANISOU 3764 CB VAL B 222 5928 5065 4917 1478 1519 955 C
ATOM 3765 CG1 VAL B 222 58.097 -19.637 21.354 1.00 49.77 C
ANISOU 3765 CG1 VAL B 222 6967 5975 5966 1485 1574 991 C
ATOM 3766 CG2 VAL B 222 56.725 -18.642 23.172 1.00 32.77 C
ANISOU 3766 CG2 VAL B 222 4654 4016 3781 1465 1478 884 C
ATOM 3767 N THR B 223 55.402 -20.875 19.265 1.00 59.05 N
ANISOU 3767 N THR B 223 8332 7084 7019 1508 1595 988 N
ATOM 3768 CA THR B 223 55.690 -21.525 17.992 1.00 53.85 C
ANISOU 3768 CA THR B 223 7811 6319 6330 1522 1654 981 C
ATOM 3769 C THR B 223 54.650 -21.264 16.918 1.00 52.11 C
ANISOU 3769 C THR B 223 7660 6115 6024 1525 1667 967 C
ATOM 3770 O THR B 223 54.847 -21.687 15.776 1.00 62.80 O
ANISOU 3770 O THR B 223 9155 7396 7311 1519 1715 947 O
ATOM 3771 CB THR B 223 55.831 -23.036 18.170 1.00 46.78 C
ANISOU 3771 CB THR B 223 6988 5388 5400 1502 1673 952 C
ATOM 3772 OG1 THR B 223 54.547 -23.585 18.480 1.00 54.06 O
ANISOU 3772 OG1 THR B 223 7897 6394 6249 1444 1648 920 O
ATOM 3773 CG2 THR B 223 56.812 -23.359 19.273 1.00 42.99 C
ANISOU 3773 CG2 THR B 223 6461 4900 4974 1529 1667 985 C
ATOM 3774 N TYR B 224 53.552 -20.596 17.239 1.00 45.65 N
ANISOU 3774 N TYR B 224 6762 5400 5185 1533 1634 983 N
ATOM 3775 CA TYR B 224 52.550 -20.395 16.204 1.00 48.83 C
ANISOU 3775 CA TYR B 224 7249 5832 5471 1548 1646 997 C
ATOM 3776 C TYR B 224 52.053 -18.960 16.179 1.00 48.40 C
ANISOU 3776 C TYR B 224 7131 5822 5438 1645 1650 1059 C
ATOM 3777 O TYR B 224 52.324 -18.215 15.229 1.00 52.77 O
ANISOU 3777 O TYR B 224 7783 6310 5958 1704 1684 1092 O
ATOM 3778 CB TYR B 224 51.350 -21.324 16.383 1.00 51.13 C
ANISOU 3778 CB TYR B 224 7546 6218 5665 1473 1627 986 C
ATOM 3779 CG TYR B 224 50.360 -21.214 15.234 1.00 50.14 C
ANISOU 3779 CG TYR B 224 7558 6124 5371 1474 1604 1037 C
ATOM 3780 CD1 TYR B 224 50.525 -21.979 14.090 1.00 67.99 C
ANISOU 3780 CD1 TYR B 224 10037 8302 7493 1406 1581 1020 C
ATOM 3781 CD2 TYR B 224 49.276 -20.339 15.285 1.00 32.96 C
ANISOU 3781 CD2 TYR B 224 5314 4055 3155 1553 1586 1121 C
ATOM 3782 CE1 TYR B 224 49.647 -21.897 13.035 1.00 68.56 C
ANISOU 3782 CE1 TYR B 224 10288 8387 7376 1391 1492 1085 C
ATOM 3783 CE2 TYR B 224 48.382 -20.249 14.223 1.00 46.46 C
ANISOU 3783 CE2 TYR B 224 7192 5775 4688 1565 1482 1220 C
ATOM 3784 CZ TYR B 224 48.579 -21.035 13.096 1.00 59.68 C
ANISOU 3784 CZ TYR B 224 9113 7352 6209 1473 1412 1196 C
ATOM 3785 OH TYR B 224 47.717 -20.975 12.016 1.00 62.92 O
ANISOU 3785 OH TYR B 224 9694 7745 6469 1459 1206 1253 O
ATOM 3786 N LEU B 225 51.334 -18.556 17.221 1.00 40.33 N
ANISOU 3786 N LEU B 225 5948 4911 4465 1656 1629 1069 N
ATOM 3787 CA LEU B 225 50.555 -17.333 17.116 1.00 35.90 C
ANISOU 3787 CA LEU B 225 5319 4414 3908 1769 1648 1128 C
ATOM 3788 C LEU B 225 51.470 -16.117 17.025 1.00 26.39 C
ANISOU 3788 C LEU B 225 4130 3117 2781 1813 1666 1175 C
ATOM 3789 O LEU B 225 51.353 -15.317 16.096 1.00 27.36 O
ANISOU 3789 O LEU B 225 4357 3182 2857 1935 1721 1258 O
ATOM 3790 CB LEU B 225 49.616 -17.231 18.317 1.00 26.60 C
ANISOU 3790 CB LEU B 225 3915 3385 2806 1737 1623 1058 C
ATOM 3791 CG LEU B 225 48.607 -16.091 18.310 1.00 38.11 C
ANISOU 3791 CG LEU B 225 5206 4913 4363 1865 1603 1039 C
ATOM 3792 CD1 LEU B 225 47.617 -16.324 17.187 1.00 41.60 C
ANISOU 3792 CD1 LEU B 225 5701 5351 4753 1905 1491 1089 C
ATOM 3793 CD2 LEU B 225 47.898 -15.988 19.656 1.00 40.41 C
ANISOU 3793 CD2 LEU B 225 5258 5321 4776 1785 1569 910 C
ATOM 3794 N ALA B 226 52.388 -15.961 17.974 1.00 39.29 N
ANISOU 3794 N ALA B 226 5679 4742 4507 1713 1633 1125 N
ATOM 3795 CA ALA B 226 53.258 -14.786 17.967 1.00 27.65 C
ANISOU 3795 CA ALA B 226 4194 3209 3102 1704 1665 1148 C
ATOM 3796 C ALA B 226 54.149 -14.686 16.735 1.00 38.98 C
ANISOU 3796 C ALA B 226 5798 4495 4519 1738 1751 1220 C
ATOM 3797 O ALA B 226 54.152 -13.626 16.082 1.00 48.85 O
ANISOU 3797 O ALA B 226 7088 5707 5765 1782 1820 1262 O
ATOM 3798 CB ALA B 226 54.112 -14.784 19.240 1.00 24.64 C
ANISOU 3798 CB ALA B 226 3690 2867 2806 1597 1610 1048 C
ATOM 3799 N PRO B 227 54.946 -15.702 16.381 1.00 41.86 N
ANISOU 3799 N PRO B 227 6226 4791 4888 1694 1754 1170 N
ATOM 3800 CA PRO B 227 55.813 -15.538 15.201 1.00 38.54 C
ANISOU 3800 CA PRO B 227 5923 4249 4471 1705 1849 1162 C
ATOM 3801 C PRO B 227 55.033 -15.288 13.927 1.00 40.89 C
ANISOU 3801 C PRO B 227 6382 4512 4644 1820 1917 1170 C
ATOM 3802 O PRO B 227 55.442 -14.457 13.105 1.00 52.61 O
ANISOU 3802 O PRO B 227 7965 5913 6111 1862 2025 1197 O
ATOM 3803 CB PRO B 227 56.606 -16.854 15.147 1.00 27.72 C
ANISOU 3803 CB PRO B 227 4598 2831 3105 1655 1854 1118 C
ATOM 3804 CG PRO B 227 55.847 -17.811 15.998 1.00 38.83 C
ANISOU 3804 CG PRO B 227 5952 4322 4480 1644 1763 1096 C
ATOM 3805 CD PRO B 227 55.085 -17.020 17.020 1.00 44.32 C
ANISOU 3805 CD PRO B 227 6520 5123 5195 1650 1703 1129 C
ATOM 3806 N LEU B 228 53.869 -15.936 13.780 1.00 36.62 N
ANISOU 3806 N LEU B 228 5880 4063 3973 1823 1842 1159 N
ATOM 3807 CA LEU B 228 53.069 -15.745 12.576 1.00 44.95 C
ANISOU 3807 CA LEU B 228 7115 5133 4831 1794 1774 1206 C
ATOM 3808 C LEU B 228 52.346 -14.397 12.555 1.00 50.83 C
ANISOU 3808 C LEU B 228 7838 5892 5584 1873 1712 1311 C
ATOM 3809 O LEU B 228 52.200 -13.808 11.484 1.00 58.97 O
ANISOU 3809 O LEU B 228 9040 6845 6519 1851 1628 1380 O
ATOM 3810 CB LEU B 228 52.075 -16.899 12.413 1.00 34.01 C
ANISOU 3810 CB LEU B 228 5792 3822 3308 1728 1654 1197 C
ATOM 3811 CG LEU B 228 52.652 -18.291 12.101 1.00 34.00 C
ANISOU 3811 CG LEU B 228 5877 3780 3263 1626 1680 1108 C
ATOM 3812 CD1 LEU B 228 51.591 -19.379 12.114 1.00 30.21 C
ANISOU 3812 CD1 LEU B 228 5446 3374 2660 1558 1582 1105 C
ATOM 3813 CD2 LEU B 228 53.379 -18.280 10.764 1.00 43.99 C
ANISOU 3813 CD2 LEU B 228 7359 4935 4419 1581 1723 1103 C
ATOM 3814 N GLY B 229 51.915 -13.877 13.708 1.00 40.15 N
ANISOU 3814 N GLY B 229 6284 4612 4359 1961 1726 1329 N
ATOM 3815 CA GLY B 229 51.345 -12.537 13.738 1.00 38.77 C
ANISOU 3815 CA GLY B 229 6046 4396 4288 2029 1611 1396 C
ATOM 3816 C GLY B 229 52.379 -11.469 13.437 1.00 53.63 C
ANISOU 3816 C GLY B 229 7971 6166 6239 2005 1720 1412 C
ATOM 3817 O GLY B 229 52.106 -10.507 12.702 1.00 50.20 O
ANISOU 3817 O GLY B 229 7632 5623 5819 2021 1602 1484 O
ATOM 3818 N LEU B 230 53.590 -11.631 13.983 1.00 62.11 N
ANISOU 3818 N LEU B 230 8981 7255 7362 1969 1939 1359 N
ATOM 3819 CA LEU B 230 54.662 -10.688 13.676 1.00 66.69 C
ANISOU 3819 CA LEU B 230 9595 7718 8027 1942 2072 1384 C
ATOM 3820 C LEU B 230 55.027 -10.754 12.198 1.00 75.65 C
ANISOU 3820 C LEU B 230 10972 8728 9045 1907 2081 1416 C
ATOM 3821 O LEU B 230 55.223 -9.721 11.543 1.00 79.06 O
ANISOU 3821 O LEU B 230 11508 9040 9492 1887 2079 1495 O
ATOM 3822 CB LEU B 230 55.866 -10.967 14.569 1.00 56.56 C
ANISOU 3822 CB LEU B 230 8182 6455 6853 1812 2138 1344 C
ATOM 3823 CG LEU B 230 55.555 -10.468 15.979 1.00 45.17 C
ANISOU 3823 CG LEU B 230 6551 5076 5535 1780 2031 1326 C
ATOM 3824 CD1 LEU B 230 56.471 -11.117 16.990 1.00 47.98 C
ANISOU 3824 CD1 LEU B 230 6798 5461 5970 1663 1966 1248 C
ATOM 3825 CD2 LEU B 230 55.661 -8.930 16.026 1.00 47.10 C
ANISOU 3825 CD2 LEU B 230 6717 5222 5957 1804 2022 1297 C
ATOM 3826 N MET B 231 55.090 -11.964 11.650 1.00 70.00 N
ANISOU 3826 N MET B 231 10362 8030 8204 1867 2062 1360 N
ATOM 3827 CA MET B 231 55.366 -12.115 10.233 1.00 54.37 C
ANISOU 3827 CA MET B 231 8632 5961 6063 1787 2054 1390 C
ATOM 3828 C MET B 231 54.253 -11.489 9.405 1.00 61.41 C
ANISOU 3828 C MET B 231 9693 6831 6808 1779 1841 1506 C
ATOM 3829 O MET B 231 54.514 -10.881 8.364 1.00 74.76 O
ANISOU 3829 O MET B 231 11584 8416 8405 1735 1842 1584 O
ATOM 3830 CB MET B 231 55.494 -13.593 9.890 1.00 57.92 C
ANISOU 3830 CB MET B 231 9155 6441 6413 1731 2040 1304 C
ATOM 3831 CG MET B 231 56.826 -14.197 10.218 1.00 59.66 C
ANISOU 3831 CG MET B 231 9295 6595 6776 1724 2200 1226 C
ATOM 3832 SD MET B 231 56.811 -15.885 9.622 1.00 59.35 S
ANISOU 3832 SD MET B 231 9385 6567 6598 1646 2151 1151 S
ATOM 3833 CE MET B 231 56.493 -16.729 11.165 1.00 75.02 C
ANISOU 3833 CE MET B 231 11134 8642 8730 1678 2060 1098 C
ATOM 3834 N ALA B 232 52.997 -11.683 9.820 1.00 66.24 N
ANISOU 3834 N ALA B 232 10235 7528 7405 1828 1638 1528 N
ATOM 3835 CA ALA B 232 51.880 -11.098 9.092 1.00 56.03 C
ANISOU 3835 CA ALA B 232 9076 6189 6025 1856 1371 1644 C
ATOM 3836 C ALA B 232 51.952 -9.579 9.068 1.00 57.45 C
ANISOU 3836 C ALA B 232 9242 6246 6341 1905 1335 1733 C
ATOM 3837 O ALA B 232 51.760 -8.964 8.012 1.00 51.51 O
ANISOU 3837 O ALA B 232 8704 5385 5483 1884 1209 1840 O
ATOM 3838 CB ALA B 232 50.564 -11.559 9.718 1.00 37.19 C
ANISOU 3838 CB ALA B 232 6550 3905 3676 1933 1167 1642 C
ATOM 3839 N MET B 233 52.239 -8.947 10.214 1.00 54.11 N
ANISOU 3839 N MET B 233 8580 5828 6150 1964 1436 1689 N
ATOM 3840 CA MET B 233 52.340 -7.487 10.178 1.00 53.82 C
ANISOU 3840 CA MET B 233 8537 5646 6266 1997 1396 1759 C
ATOM 3841 C MET B 233 53.531 -7.051 9.338 1.00 50.67 C
ANISOU 3841 C MET B 233 8331 5124 5796 1904 1590 1817 C
ATOM 3842 O MET B 233 53.462 -6.036 8.632 1.00 62.68 O
ANISOU 3842 O MET B 233 10003 6496 7318 1897 1505 1930 O
ATOM 3843 CB MET B 233 52.415 -6.858 11.574 1.00 59.90 C
ANISOU 3843 CB MET B 233 9013 6436 7310 2058 1448 1673 C
ATOM 3844 CG MET B 233 51.086 -6.838 12.349 1.00 73.30 C
ANISOU 3844 CG MET B 233 10495 8214 9139 2164 1224 1607 C
ATOM 3845 SD MET B 233 51.204 -6.394 14.111 1.00 76.03 S
ANISOU 3845 SD MET B 233 10487 8645 9758 2180 1295 1423 S
ATOM 3846 CE MET B 233 51.853 -7.901 14.835 1.00 87.59 C
ANISOU 3846 CE MET B 233 11886 10303 11089 2096 1500 1347 C
ATOM 3847 N ALA B 234 54.630 -7.810 9.393 1.00 47.49 N
ANISOU 3847 N ALA B 234 7920 4770 5353 1840 1849 1738 N
ATOM 3848 CA ALA B 234 55.798 -7.465 8.592 1.00 40.91 C
ANISOU 3848 CA ALA B 234 7242 3819 4483 1760 2057 1774 C
ATOM 3849 C ALA B 234 55.475 -7.523 7.106 1.00 43.56 C
ANISOU 3849 C ALA B 234 7896 4093 4562 1697 1943 1870 C
ATOM 3850 O ALA B 234 55.819 -6.610 6.352 1.00 49.85 O
ANISOU 3850 O ALA B 234 8864 4748 5328 1654 1979 1981 O
ATOM 3851 CB ALA B 234 56.963 -8.390 8.931 1.00 39.43 C
ANISOU 3851 CB ALA B 234 6957 3682 4343 1734 2313 1652 C
ATOM 3852 N TYR B 235 54.843 -8.612 6.658 1.00 50.50 N
ANISOU 3852 N TYR B 235 8872 5070 5248 1683 1812 1834 N
ATOM 3853 CA TYR B 235 54.508 -8.741 5.244 1.00 56.22 C
ANISOU 3853 CA TYR B 235 9912 5745 5706 1621 1691 1922 C
ATOM 3854 C TYR B 235 53.385 -7.797 4.846 1.00 60.53 C
ANISOU 3854 C TYR B 235 10562 6218 6219 1671 1384 2076 C
ATOM 3855 O TYR B 235 53.309 -7.399 3.682 1.00 66.57 O
ANISOU 3855 O TYR B 235 11602 6891 6800 1627 1305 2196 O
ATOM 3856 CB TYR B 235 54.127 -10.187 4.912 1.00 55.46 C
ANISOU 3856 CB TYR B 235 9885 5760 5428 1588 1625 1834 C
ATOM 3857 CG TYR B 235 55.304 -11.140 4.807 1.00 57.02 C
ANISOU 3857 CG TYR B 235 10079 5970 5615 1529 1896 1706 C
ATOM 3858 CD1 TYR B 235 56.292 -10.948 3.850 1.00 57.32 C
ANISOU 3858 CD1 TYR B 235 10311 5906 5562 1463 2092 1731 C
ATOM 3859 CD2 TYR B 235 55.436 -12.221 5.673 1.00 65.09 C
ANISOU 3859 CD2 TYR B 235 10903 7088 6738 1549 1950 1569 C
ATOM 3860 CE1 TYR B 235 57.373 -11.809 3.740 1.00 53.48 C
ANISOU 3860 CE1 TYR B 235 9810 5407 5104 1429 2327 1618 C
ATOM 3861 CE2 TYR B 235 56.514 -13.089 5.572 1.00 71.97 C
ANISOU 3861 CE2 TYR B 235 11766 7937 7640 1514 2157 1463 C
ATOM 3862 CZ TYR B 235 57.480 -12.875 4.605 1.00 69.15 C
ANISOU 3862 CZ TYR B 235 11591 7472 7212 1461 2342 1486 C
ATOM 3863 OH TYR B 235 58.547 -13.740 4.509 1.00 81.15 O
ANISOU 3863 OH TYR B 235 13094 8951 8791 1440 2539 1390 O
ATOM 3864 N PHE B 236 52.557 -7.369 5.798 1.00 56.78 N
ANISOU 3864 N PHE B 236 9869 5765 5941 1775 1212 2076 N
ATOM 3865 CA PHE B 236 51.606 -6.307 5.508 1.00 65.59 C
ANISOU 3865 CA PHE B 236 11038 6770 7113 1852 918 2213 C
ATOM 3866 C PHE B 236 52.320 -5.000 5.199 1.00 66.00 C
ANISOU 3866 C PHE B 236 11186 6640 7251 1824 1025 2319 C
ATOM 3867 O PHE B 236 52.004 -4.324 4.212 1.00 78.76 O
ANISOU 3867 O PHE B 236 13035 8132 8757 1814 863 2475 O
ATOM 3868 CB PHE B 236 50.669 -6.133 6.698 1.00 75.79 C
ANISOU 3868 CB PHE B 236 12027 8116 8656 1985 748 2152 C
ATOM 3869 CG PHE B 236 49.573 -5.150 6.461 1.00 85.52 C
ANISOU 3869 CG PHE B 236 13258 9232 10002 2096 408 2261 C
ATOM 3870 CD1 PHE B 236 48.521 -5.431 5.613 1.00 95.55 C
ANISOU 3870 CD1 PHE B 236 14666 10512 11125 2133 88 2347 C
ATOM 3871 CD2 PHE B 236 49.609 -3.924 7.103 1.00 96.36 C
ANISOU 3871 CD2 PHE B 236 14478 10478 11656 2170 396 2266 C
ATOM 3872 CE1 PHE B 236 47.521 -4.499 5.407 1.00112.30 C
ANISOU 3872 CE1 PHE B 236 16752 12522 13396 2255 -242 2447 C
ATOM 3873 CE2 PHE B 236 48.617 -2.995 6.908 1.00118.93 C
ANISOU 3873 CE2 PHE B 236 17311 13211 14668 2286 78 2351 C
ATOM 3874 CZ PHE B 236 47.570 -3.279 6.057 1.00125.02 C
ANISOU 3874 CZ PHE B 236 18198 13995 15309 2335 -243 2448 C
ATOM 3875 N GLN B 237 53.313 -4.641 6.018 1.00 66.38 N
ANISOU 3875 N GLN B 237 11064 6663 7492 1806 1298 2246 N
ATOM 3876 CA GLN B 237 54.086 -3.433 5.730 1.00 71.61 C
ANISOU 3876 CA GLN B 237 11820 7139 8249 1761 1429 2344 C
ATOM 3877 C GLN B 237 54.905 -3.579 4.446 1.00 82.36 C
ANISOU 3877 C GLN B 237 13484 8445 9364 1637 1604 2424 C
ATOM 3878 O GLN B 237 55.038 -2.622 3.671 1.00 76.25 O
ANISOU 3878 O GLN B 237 12920 7505 8547 1598 1580 2579 O
ATOM 3879 CB GLN B 237 54.977 -3.045 6.913 1.00 65.89 C
ANISOU 3879 CB GLN B 237 10834 6398 7802 1765 1676 2242 C
ATOM 3880 CG GLN B 237 54.218 -2.695 8.189 1.00 66.69 C
ANISOU 3880 CG GLN B 237 10645 6531 8161 1885 1516 2158 C
ATOM 3881 CD GLN B 237 55.037 -1.799 9.121 1.00 72.30 C
ANISOU 3881 CD GLN B 237 11167 7141 9161 1878 1694 2103 C
ATOM 3882 OE1 GLN B 237 56.059 -2.221 9.673 1.00 80.87 O
ANISOU 3882 OE1 GLN B 237 12124 8290 10312 1825 1963 2015 O
ATOM 3883 NE2 GLN B 237 54.600 -0.545 9.275 1.00 74.06 N
ANISOU 3883 NE2 GLN B 237 11374 7188 9576 1933 1530 2153 N
ATOM 3884 N ILE B 238 55.439 -4.777 4.191 1.00 92.00 N
ANISOU 3884 N ILE B 238 14737 9792 10428 1578 1778 2317 N
ATOM 3885 CA ILE B 238 56.206 -5.002 2.970 1.00 86.66 C
ANISOU 3885 CA ILE B 238 14337 9066 9524 1471 1956 2364 C
ATOM 3886 C ILE B 238 55.300 -4.857 1.755 1.00 95.14 C
ANISOU 3886 C ILE B 238 15726 10099 10325 1463 1687 2515 C
ATOM 3887 O ILE B 238 55.699 -4.304 0.719 1.00103.66 O
ANISOU 3887 O ILE B 238 17078 11060 11250 1393 1760 2646 O
ATOM 3888 CB ILE B 238 56.861 -6.396 3.015 1.00 70.08 C
ANISOU 3888 CB ILE B 238 12180 7096 7352 1436 2157 2193 C
ATOM 3889 CG1 ILE B 238 57.980 -6.427 4.055 1.00 71.26 C
ANISOU 3889 CG1 ILE B 238 12049 7250 7776 1444 2444 2071 C
ATOM 3890 CG2 ILE B 238 57.403 -6.755 1.647 1.00 64.07 C
ANISOU 3890 CG2 ILE B 238 11730 6288 6324 1343 2289 2231 C
ATOM 3891 CD1 ILE B 238 58.541 -7.824 4.318 1.00 66.13 C
ANISOU 3891 CD1 ILE B 238 11289 6711 7124 1443 2586 1900 C
ATOM 3892 N PHE B 239 54.055 -5.325 1.878 1.00 90.53 N
ANISOU 3892 N PHE B 239 15105 9607 9684 1538 1367 2508 N
ATOM 3893 CA PHE B 239 53.092 -5.197 0.799 1.00 84.95 C
ANISOU 3893 CA PHE B 239 14669 8866 8743 1553 1062 2652 C
ATOM 3894 C PHE B 239 52.772 -3.734 0.551 1.00 80.26 C
ANISOU 3894 C PHE B 239 14162 8091 8244 1596 902 2847 C
ATOM 3895 O PHE B 239 52.714 -3.288 -0.601 1.00 92.57 O
ANISOU 3895 O PHE B 239 16032 9552 9590 1561 830 3008 O
ATOM 3896 CB PHE B 239 51.807 -5.966 1.116 1.00 88.15 C
ANISOU 3896 CB PHE B 239 14965 9401 9129 1636 744 2597 C
ATOM 3897 CG PHE B 239 50.678 -5.617 0.195 1.00 98.76 C
ANISOU 3897 CG PHE B 239 16519 10695 10310 1692 365 2754 C
ATOM 3898 CD1 PHE B 239 50.609 -6.166 -1.074 1.00109.10 C
ANISOU 3898 CD1 PHE B 239 18161 12022 11269 1630 312 2798 C
ATOM 3899 CD2 PHE B 239 49.711 -4.702 0.577 1.00 98.36 C
ANISOU 3899 CD2 PHE B 239 16336 10567 10468 1820 60 2853 C
ATOM 3900 CE1 PHE B 239 49.576 -5.834 -1.936 1.00115.17 C
ANISOU 3900 CE1 PHE B 239 19134 12748 11877 1694 -55 2942 C
ATOM 3901 CE2 PHE B 239 48.677 -4.361 -0.281 1.00104.90 C
ANISOU 3901 CE2 PHE B 239 17338 11346 11171 1894 -308 2999 C
ATOM 3902 CZ PHE B 239 48.609 -4.929 -1.539 1.00113.25 C
ANISOU 3902 CZ PHE B 239 18737 12436 11857 1830 -373 3047 C
ATOM 3903 N ARG B 240 52.560 -2.978 1.632 1.00 73.43 N
ANISOU 3903 N ARG B 240 13030 7168 7703 1678 844 2831 N
ATOM 3904 CA ARG B 240 52.242 -1.565 1.495 1.00 82.03 C
ANISOU 3904 CA ARG B 240 14173 8055 8939 1732 680 3003 C
ATOM 3905 C ARG B 240 53.402 -0.786 0.875 1.00 94.13 C
ANISOU 3905 C ARG B 240 15917 9428 10420 1615 959 3113 C
ATOM 3906 O ARG B 240 53.172 0.178 0.133 1.00 99.33 O
ANISOU 3906 O ARG B 240 16791 9916 11034 1619 824 3312 O
ATOM 3907 CB ARG B 240 51.906 -0.998 2.881 1.00 84.18 C
ANISOU 3907 CB ARG B 240 14096 8295 9594 1842 609 2913 C
ATOM 3908 CG ARG B 240 50.445 -1.227 3.335 1.00 97.26 C
ANISOU 3908 CG ARG B 240 15565 10024 11365 1996 233 2878 C
ATOM 3909 CD ARG B 240 49.423 -1.027 2.203 1.00113.53 C
ANISOU 3909 CD ARG B 240 17846 12032 13257 2053 -124 3057 C
ATOM 3910 NE ARG B 240 48.962 0.361 2.144 1.00128.41 N
ANISOU 3910 NE ARG B 240 19725 13701 15365 2152 -333 3206 N
ATOM 3911 CZ ARG B 240 48.295 0.978 3.122 1.00132.12 C
ANISOU 3911 CZ ARG B 240 19890 14107 16202 2295 -498 3141 C
ATOM 3912 NH1 ARG B 240 48.001 0.341 4.254 1.00123.44 N
ANISOU 3912 NH1 ARG B 240 18475 13157 15269 2353 -472 2931 N
ATOM 3913 NH2 ARG B 240 47.941 2.250 2.979 1.00139.19 N
ANISOU 3913 NH2 ARG B 240 20795 14782 17307 2383 -674 3279 N
ATOM 3914 N LYS B 241 54.646 -1.202 1.139 1.00102.31 N
ANISOU 3914 N LYS B 241 16892 10513 11470 1515 1348 2993 N
ATOM 3915 CA LYS B 241 55.808 -0.560 0.523 1.00100.86 C
ANISOU 3915 CA LYS B 241 16892 10184 11244 1395 1650 3084 C
ATOM 3916 C LYS B 241 55.930 -0.884 -0.959 1.00104.49 C
ANISOU 3916 C LYS B 241 17735 10638 11328 1315 1684 3197 C
ATOM 3917 O LYS B 241 56.095 0.013 -1.796 1.00116.67 O
ANISOU 3917 O LYS B 241 19542 12013 12775 1266 1693 3391 O
ATOM 3918 CB LYS B 241 57.102 -0.968 1.226 1.00 97.56 C
ANISOU 3918 CB LYS B 241 16265 9820 10982 1328 2051 2913 C
ATOM 3919 CG LYS B 241 58.248 0.006 0.913 1.00 91.62 C
ANISOU 3919 CG LYS B 241 15610 8878 10323 1219 2348 3008 C
ATOM 3920 CD LYS B 241 58.128 1.395 1.571 1.00 97.86 C
ANISOU 3920 CD LYS B 241 16292 9471 11418 1248 2261 3096 C
ATOM 3921 CE LYS B 241 59.478 2.104 1.503 1.00110.08 C
ANISOU 3921 CE LYS B 241 17852 10860 13112 1118 2634 3129 C
ATOM 3922 NZ LYS B 241 60.608 1.162 1.638 1.00111.39 N
ANISOU 3922 NZ LYS B 241 17892 11153 13281 1052 2996 2962 N
ATOM 3923 N LEU B 242 55.810 -2.163 -1.304 1.00 98.82 N
ANISOU 3923 N LEU B 242 17066 10092 10388 1305 1694 3079 N
ATOM 3924 CA LEU B 242 56.104 -2.602 -2.664 1.00 96.89 C
ANISOU 3924 CA LEU B 242 17183 9848 9783 1223 1790 3139 C
ATOM 3925 C LEU B 242 54.991 -2.294 -3.655 1.00108.24 C
ANISOU 3925 C LEU B 242 18920 11240 10965 1272 1427 3325 C
ATOM 3926 O LEU B 242 55.275 -2.080 -4.838 1.00115.48 O
ANISOU 3926 O LEU B 242 20197 12078 11604 1206 1502 3455 O
ATOM 3927 CB LEU B 242 56.414 -4.099 -2.678 1.00 88.90 C
ANISOU 3927 CB LEU B 242 16122 9009 8647 1199 1933 2932 C
ATOM 3928 CG LEU B 242 57.757 -4.493 -2.061 1.00 91.57 C
ANISOU 3928 CG LEU B 242 16245 9369 9177 1144 2341 2765 C
ATOM 3929 CD1 LEU B 242 57.975 -6.000 -2.160 1.00 90.01 C
ANISOU 3929 CD1 LEU B 242 16022 9316 8862 1135 2438 2575 C
ATOM 3930 CD2 LEU B 242 58.896 -3.732 -2.729 1.00 99.12 C
ANISOU 3930 CD2 LEU B 242 17381 10170 10110 1040 2668 2865 C
ATOM 3931 N TRP B 243 53.738 -2.274 -3.214 1.00112.98 N
ANISOU 3931 N TRP B 243 19385 11887 11655 1393 1038 3341 N
ATOM 3932 CA TRP B 243 52.607 -2.042 -4.103 1.00120.22 C
ANISOU 3932 CA TRP B 243 20549 12770 12359 1466 654 3504 C
ATOM 3933 C TRP B 243 52.036 -0.647 -3.875 1.00129.00 C
ANISOU 3933 C TRP B 243 21614 13704 13696 1560 414 3694 C
ATOM 3934 O TRP B 243 51.765 -0.256 -2.735 1.00123.08 O
ANISOU 3934 O TRP B 243 20530 12936 13299 1637 340 3635 O
ATOM 3935 CB TRP B 243 51.538 -3.110 -3.853 1.00111.80 C
ANISOU 3935 CB TRP B 243 19357 11880 11241 1547 365 3378 C
ATOM 3936 CG TRP B 243 51.825 -4.384 -4.588 1.00110.68 C
ANISOU 3936 CG TRP B 243 19419 11862 10773 1465 488 3259 C
ATOM 3937 CD1 TRP B 243 51.434 -4.719 -5.849 1.00113.54 C
ANISOU 3937 CD1 TRP B 243 20154 12225 10759 1450 337 3329 C
ATOM 3938 CD2 TRP B 243 52.643 -5.468 -4.119 1.00108.47 C
ANISOU 3938 CD2 TRP B 243 18992 11700 10522 1390 803 3041 C
ATOM 3939 NE1 TRP B 243 51.925 -5.963 -6.182 1.00114.37 N
ANISOU 3939 NE1 TRP B 243 20355 12437 10664 1368 538 3159 N
ATOM 3940 CE2 TRP B 243 52.673 -6.442 -5.138 1.00107.42 C
ANISOU 3940 CE2 TRP B 243 19150 11626 10039 1334 825 2986 C
ATOM 3941 CE3 TRP B 243 53.339 -5.714 -2.929 1.00103.90 C
ANISOU 3941 CE3 TRP B 243 18069 11175 10235 1377 1055 2885 C
ATOM 3942 CZ2 TRP B 243 53.373 -7.644 -5.006 1.00 97.84 C
ANISOU 3942 CZ2 TRP B 243 17880 10508 8787 1268 1091 2784 C
ATOM 3943 CZ3 TRP B 243 54.029 -6.904 -2.798 1.00101.97 C
ANISOU 3943 CZ3 TRP B 243 17764 11034 9944 1317 1307 2694 C
ATOM 3944 CH2 TRP B 243 54.045 -7.854 -3.833 1.00 99.44 C
ANISOU 3944 CH2 TRP B 243 17727 10758 9300 1265 1324 2647 C
ATOM 3945 N GLY B 244 51.861 0.094 -4.956 1.00143.81 N
ANISOU 3945 N GLY B 244 23831 15438 15371 1562 298 3917 N
ATOM 3946 CA GLY B 244 51.249 1.419 -4.910 1.00154.30 C
ANISOU 3946 CA GLY B 244 25158 16572 16897 1667 38 4122 C
ATOM 3947 C GLY B 244 52.151 2.622 -4.685 1.00161.51 C
ANISOU 3947 C GLY B 244 26080 17268 18020 1597 280 4237 C
ATOM 3948 O GLY B 244 52.082 3.598 -5.432 1.00168.50 O
ANISOU 3948 O GLY B 244 27229 17962 18833 1605 197 4473 O
ATOM 3949 N ARG B 245 52.997 2.567 -3.658 1.00157.65 N
ANISOU 3949 N ARG B 245 25312 16797 17792 1530 575 4073 N
ATOM 3950 CA ARG B 245 53.800 3.723 -3.276 1.00157.32 C
ANISOU 3950 CA ARG B 245 25229 16540 18006 1467 780 4152 C
ATOM 3951 C ARG B 245 54.919 3.955 -4.285 1.00152.86 C
ANISOU 3951 C ARG B 245 25003 15882 17195 1300 1128 4271 C
ATOM 3952 O ARG B 245 55.804 3.108 -4.446 1.00157.40 O
ANISOU 3952 O ARG B 245 25600 16585 17620 1190 1461 4131 O
ATOM 3953 CB ARG B 245 54.367 3.516 -1.876 1.00159.21 C
ANISOU 3953 CB ARG B 245 25074 16841 18575 1454 986 3920 C
ATOM 3954 CG ARG B 245 53.292 3.448 -0.810 1.00161.09 C
ANISOU 3954 CG ARG B 245 24980 17140 19087 1620 668 3808 C
ATOM 3955 CD ARG B 245 53.876 3.171 0.558 1.00156.69 C
ANISOU 3955 CD ARG B 245 24066 16660 18807 1612 887 3570 C
ATOM 3956 NE ARG B 245 52.900 3.441 1.609 1.00156.38 N
ANISOU 3956 NE ARG B 245 23725 16615 19075 1773 603 3483 N
ATOM 3957 CZ ARG B 245 53.027 3.046 2.870 1.00158.77 C
ANISOU 3957 CZ ARG B 245 23699 17029 19595 1815 699 3261 C
ATOM 3958 NH1 ARG B 245 54.093 2.348 3.244 1.00161.33 N
ANISOU 3958 NH1 ARG B 245 23941 17480 19875 1712 1059 3119 N
ATOM 3959 NH2 ARG B 245 52.081 3.343 3.751 1.00158.68 N
ANISOU 3959 NH2 ARG B 245 23433 17005 19854 1969 439 3179 N
ATOM 3960 N GLN B 246 54.890 5.113 -4.945 1.00149.42 N
ANISOU 3960 N GLN B 246 24822 15211 16740 1288 1061 4527 N
ATOM 3961 CA GLN B 246 55.823 5.448 -6.018 1.00149.52 C
ANISOU 3961 CA GLN B 246 25204 15110 16497 1134 1365 4681 C
ATOM 3962 C GLN B 246 56.513 6.768 -5.708 1.00147.66 C
ANISOU 3962 C GLN B 246 24951 14605 16549 1056 1535 4811 C
ATOM 3963 O GLN B 246 55.859 7.815 -5.651 1.00139.18 O
ANISOU 3963 O GLN B 246 23907 13328 15648 1145 1255 4991 O
ATOM 3964 CB GLN B 246 55.102 5.541 -7.363 1.00151.29 C
ANISOU 3964 CB GLN B 246 25856 15297 16330 1182 1120 4906 C
ATOM 3965 CG GLN B 246 54.437 4.264 -7.818 1.00146.50 C
ANISOU 3965 CG GLN B 246 25325 14932 15407 1243 947 4784 C
ATOM 3966 CD GLN B 246 53.906 4.382 -9.229 1.00156.57 C
ANISOU 3966 CD GLN B 246 27078 16155 16256 1271 750 4998 C
ATOM 3967 OE1 GLN B 246 53.895 5.471 -9.812 1.00162.48 O
ANISOU 3967 OE1 GLN B 246 28086 16685 16966 1270 696 5258 O
ATOM 3968 NE2 GLN B 246 53.467 3.261 -9.791 1.00158.44 N
ANISOU 3968 NE2 GLN B 246 27452 16581 16167 1295 637 4889 N
ATOM 3969 N ILE B 247 57.828 6.715 -5.511 1.00148.86 N
ANISOU 3969 N ILE B 247 25044 14743 16773 895 1989 4714 N
ATOM 3970 CA ILE B 247 58.642 7.900 -5.237 1.00146.05 C
ANISOU 3970 CA ILE B 247 24672 14130 16691 787 2207 4815 C
ATOM 3971 C ILE B 247 58.883 8.668 -6.535 1.00150.04 C
ANISOU 3971 C ILE B 247 25635 14433 16940 690 2290 5115 C
ATOM 3972 O ILE B 247 59.197 8.053 -7.565 1.00145.82 O
ANISOU 3972 O ILE B 247 25392 13996 16018 620 2464 5151 O
ATOM 3973 CB ILE B 247 59.961 7.507 -4.549 1.00138.82 C
ANISOU 3973 CB ILE B 247 23497 13284 15963 657 2667 4590 C
ATOM 3974 CG1 ILE B 247 60.809 8.746 -4.250 1.00131.98 C
ANISOU 3974 CG1 ILE B 247 22601 12141 15403 532 2894 4684 C
ATOM 3975 CG2 ILE B 247 60.721 6.481 -5.389 1.00140.25 C
ANISOU 3975 CG2 ILE B 247 23848 13631 15808 555 3004 4515 C
ATOM 3976 CD1 ILE B 247 61.731 8.572 -3.061 1.00115.63 C
ANISOU 3976 CD1 ILE B 247 20127 10117 13689 478 3180 4432 C
ATOM 3977 N PRO B 248 58.764 9.996 -6.538 1.00157.15 N
ANISOU 3977 N PRO B 248 26628 15041 18042 684 2179 5333 N
ATOM 3978 CA PRO B 248 58.865 10.737 -7.803 1.00165.06 C
ANISOU 3978 CA PRO B 248 28096 15842 18778 610 2219 5650 C
ATOM 3979 C PRO B 248 60.217 10.539 -8.474 1.00167.08 C
ANISOU 3979 C PRO B 248 28548 16097 18839 388 2755 5652 C
ATOM 3980 O PRO B 248 61.264 10.549 -7.818 1.00163.92 O
ANISOU 3980 O PRO B 248 27901 15686 18694 262 3116 5493 O
ATOM 3981 CB PRO B 248 58.647 12.195 -7.380 1.00167.91 C
ANISOU 3981 CB PRO B 248 28420 15869 19508 635 2046 5833 C
ATOM 3982 CG PRO B 248 58.988 12.225 -5.923 1.00161.94 C
ANISOU 3982 CG PRO B 248 27195 15127 19207 636 2117 5571 C
ATOM 3983 CD PRO B 248 58.574 10.888 -5.382 1.00154.04 C
ANISOU 3983 CD PRO B 248 25928 14468 18130 743 2029 5294 C
ATOM 3984 N GLY B 249 60.187 10.399 -9.799 1.00170.10 N
ANISOU 3984 N GLY B 249 29380 16477 18774 347 2807 5835 N
ATOM 3985 CA GLY B 249 61.388 10.219 -10.596 1.00169.26 C
ANISOU 3985 CA GLY B 249 29513 16358 18440 147 3314 5857 C
ATOM 3986 C GLY B 249 62.313 9.102 -10.148 1.00169.36 C
ANISOU 3986 C GLY B 249 29245 16600 18504 72 3694 5533 C
ATOM 3987 O GLY B 249 63.459 9.370 -9.774 1.00171.03 O
ANISOU 3987 O GLY B 249 29289 16733 18961 -78 4102 5457 O
ATOM 3988 N THR B 250 61.842 7.855 -10.172 1.00163.01 N
ANISOU 3988 N THR B 250 28376 16065 17495 177 3563 5340 N
ATOM 3989 CA THR B 250 62.684 6.728 -9.784 1.00144.86 C
ANISOU 3989 CA THR B 250 25821 13972 15246 127 3903 5038 C
ATOM 3990 C THR B 250 63.780 6.473 -10.817 1.00151.78 C
ANISOU 3990 C THR B 250 26986 14824 15860 -38 4388 5063 C
ATOM 3991 O THR B 250 63.604 6.699 -12.018 1.00160.96 O
ANISOU 3991 O THR B 250 28615 15906 16635 -76 4389 5273 O
ATOM 3992 CB THR B 250 61.856 5.452 -9.613 1.00120.88 C
ANISOU 3992 CB THR B 250 22676 11205 12049 277 3626 4841 C
ATOM 3993 OG1 THR B 250 61.238 5.110 -10.861 1.00124.26 O
ANISOU 3993 OG1 THR B 250 23549 11669 11995 310 3465 4973 O
ATOM 3994 CG2 THR B 250 60.788 5.633 -8.546 1.00111.95 C
ANISOU 3994 CG2 THR B 250 21231 10110 11193 438 3179 4795 C
ATOM 3995 N THR B 251 64.924 5.991 -10.330 1.00146.93 N
ANISOU 3995 N THR B 251 26086 14274 15467 -127 4805 4842 N
ATOM 3996 CA THR B 251 65.973 5.508 -11.218 1.00141.48 C
ANISOU 3996 CA THR B 251 25601 13595 14561 -262 5281 4802 C
ATOM 3997 C THR B 251 65.484 4.277 -11.970 1.00139.85 C
ANISOU 3997 C THR B 251 25621 13584 13931 -178 5176 4704 C
ATOM 3998 O THR B 251 64.634 3.525 -11.484 1.00140.73 O
ANISOU 3998 O THR B 251 25566 13870 14034 -31 4831 4564 O
ATOM 3999 CB THR B 251 67.237 5.154 -10.427 1.00130.65 C
ANISOU 3999 CB THR B 251 23806 12259 13574 -342 5705 4558 C
ATOM 4000 OG1 THR B 251 67.528 6.194 -9.484 1.00135.67 O
ANISOU 4000 OG1 THR B 251 24156 12738 14653 -392 5717 4599 O
ATOM 4001 CG2 THR B 251 68.429 4.966 -11.364 1.00129.31 C
ANISOU 4001 CG2 THR B 251 23845 12032 13253 -505 6244 4561 C
ATOM 4002 N SER B 252 66.014 4.078 -13.178 1.00139.98 N
ANISOU 4002 N SER B 252 26036 13560 13589 -281 5480 4779 N
ATOM 4003 CA SER B 252 65.697 2.852 -13.906 1.00132.26 C
ANISOU 4003 CA SER B 252 25279 12753 12221 -218 5434 4655 C
ATOM 4004 C SER B 252 66.131 1.628 -13.101 1.00129.28 C
ANISOU 4004 C SER B 252 24477 12566 12078 -163 5555 4314 C
ATOM 4005 O SER B 252 65.386 0.639 -12.982 1.00123.39 O
ANISOU 4005 O SER B 252 23686 11992 11204 -40 5272 4170 O
ATOM 4006 CB SER B 252 66.372 2.877 -15.279 1.00151.65 C
ANISOU 4006 CB SER B 252 28220 15113 14285 -353 5818 4774 C
ATOM 4007 OG SER B 252 66.304 4.174 -15.856 1.00160.62 O
ANISOU 4007 OG SER B 252 29687 16031 15311 -440 5820 5098 O
ATOM 4008 N ALA B 253 67.317 1.703 -12.492 1.00130.49 N
ANISOU 4008 N ALA B 253 24300 12678 12602 -250 5955 4188 N
ATOM 4009 CA ALA B 253 67.837 0.600 -11.690 1.00127.56 C
ANISOU 4009 CA ALA B 253 23513 12460 12492 -194 6084 3879 C
ATOM 4010 C ALA B 253 66.991 0.369 -10.442 1.00123.53 C
ANISOU 4010 C ALA B 253 22621 12076 12239 -44 5664 3763 C
ATOM 4011 O ALA B 253 66.816 -0.781 -10.004 1.00124.99 O
ANISOU 4011 O ALA B 253 22602 12431 12458 53 5570 3543 O
ATOM 4012 CB ALA B 253 69.295 0.867 -11.316 1.00129.22 C
ANISOU 4012 CB ALA B 253 23450 12576 13073 -319 6585 3793 C
ATOM 4013 N GLU B 286 66.434 1.445 -9.876 1.00120.80 N
ANISOU 4013 N GLU B 286 22190 11638 12069 -25 5410 3915 N
ATOM 4014 CA GLU B 286 65.574 1.289 -8.712 1.00119.88 C
ANISOU 4014 CA GLU B 286 21736 11631 12181 116 5017 3817 C
ATOM 4015 C GLU B 286 64.315 0.523 -9.084 1.00116.07 C
ANISOU 4015 C GLU B 286 21433 11298 11373 241 4607 3806 C
ATOM 4016 O GLU B 286 63.819 -0.302 -8.301 1.00118.25 O
ANISOU 4016 O GLU B 286 21431 11736 11760 353 4397 3623 O
ATOM 4017 CB GLU B 286 65.170 2.677 -8.204 1.00135.23 C
ANISOU 4017 CB GLU B 286 23626 13411 14345 109 4821 4009 C
ATOM 4018 CG GLU B 286 65.710 3.127 -6.861 1.00135.03 C
ANISOU 4018 CG GLU B 286 23140 13341 14823 102 4915 3894 C
ATOM 4019 CD GLU B 286 65.343 4.584 -6.568 1.00127.92 C
ANISOU 4019 CD GLU B 286 22269 12228 14106 77 4742 4109 C
ATOM 4020 OE1 GLU B 286 64.293 4.826 -5.918 1.00127.46 O
ANISOU 4020 OE1 GLU B 286 22097 12190 14140 203 4331 4129 O
ATOM 4021 OE2 GLU B 286 66.085 5.482 -7.022 1.00118.92 O
ANISOU 4021 OE2 GLU B 286 21277 10888 13019 -71 5015 4260 O
ATOM 4022 N VAL B 287 63.820 0.745 -10.304 1.00111.92 N
ANISOU 4022 N VAL B 287 21377 10713 10434 219 4502 3999 N
ATOM 4023 CA VAL B 287 62.654 0.010 -10.772 1.00110.39 C
ANISOU 4023 CA VAL B 287 21380 10649 9914 328 4119 3990 C
ATOM 4024 C VAL B 287 62.994 -1.462 -10.962 1.00150.09 C
ANISOU 4024 C VAL B 287 26377 15838 14813 340 4278 3742 C
ATOM 4025 O VAL B 287 62.176 -2.338 -10.647 1.00144.50 O
ANISOU 4025 O VAL B 287 25562 15283 14059 445 3981 3611 O
ATOM 4026 CB VAL B 287 62.057 0.640 -12.039 1.00116.40 C
ANISOU 4026 CB VAL B 287 22669 11295 10261 309 3954 4263 C
ATOM 4027 CG1 VAL B 287 61.028 -0.305 -12.637 1.00116.50 C
ANISOU 4027 CG1 VAL B 287 22902 11448 9912 406 3617 4212 C
ATOM 4028 CG2 VAL B 287 61.408 1.964 -11.696 1.00117.72 C
ANISOU 4028 CG2 VAL B 287 22819 11314 10594 348 3661 4497 C
ATOM 4029 N LYS B 288 64.199 -1.771 -11.475 1.00145.30 N
ANISOU 4029 N LYS B 288 25859 15187 14162 233 4749 3672 N
ATOM 4030 CA LYS B 288 64.548 -3.189 -11.593 1.00131.70 C
ANISOU 4030 CA LYS B 288 24082 13595 12364 256 4896 3429 C
ATOM 4031 C LYS B 288 64.562 -3.857 -10.226 1.00128.69 C
ANISOU 4031 C LYS B 288 23182 13342 12374 345 4809 3203 C
ATOM 4032 O LYS B 288 63.971 -4.933 -10.041 1.00132.60 O
ANISOU 4032 O LYS B 288 23609 13977 12795 431 4599 3052 O
ATOM 4033 CB LYS B 288 65.924 -3.409 -12.248 1.00132.85 C
ANISOU 4033 CB LYS B 288 24345 13660 12472 135 5444 3376 C
ATOM 4034 CG LYS B 288 66.019 -3.229 -13.762 1.00145.71 C
ANISOU 4034 CG LYS B 288 26541 15195 13625 46 5605 3534 C
ATOM 4035 CD LYS B 288 67.381 -2.669 -14.225 1.00154.21 C
ANISOU 4035 CD LYS B 288 27700 16122 14770 -108 6159 3594 C
ATOM 4036 CE LYS B 288 67.582 -2.819 -15.746 1.00154.64 C
ANISOU 4036 CE LYS B 288 28323 16108 14323 -193 6385 3693 C
ATOM 4037 NZ LYS B 288 68.620 -1.880 -16.293 1.00149.74 N
ANISOU 4037 NZ LYS B 288 27870 15311 13715 -357 6849 3850 N
ATOM 4038 N GLN B 289 65.198 -3.214 -9.239 1.00129.48 N
ANISOU 4038 N GLN B 289 22921 13386 12888 325 4955 3183 N
ATOM 4039 CA GLN B 289 65.232 -3.824 -7.909 1.00130.54 C
ANISOU 4039 CA GLN B 289 22579 13637 13382 414 4872 2975 C
ATOM 4040 C GLN B 289 63.838 -3.998 -7.296 1.00130.88 C
ANISOU 4040 C GLN B 289 22521 13799 13409 537 4377 2971 C
ATOM 4041 O GLN B 289 63.529 -5.057 -6.722 1.00132.30 O
ANISOU 4041 O GLN B 289 22494 14120 13653 619 4249 2789 O
ATOM 4042 CB GLN B 289 66.106 -2.963 -6.987 1.00127.10 C
ANISOU 4042 CB GLN B 289 21810 13105 13379 368 5091 2974 C
ATOM 4043 CG GLN B 289 66.304 -3.505 -5.572 1.00123.39 C
ANISOU 4043 CG GLN B 289 20850 12734 13297 456 5047 2767 C
ATOM 4044 CD GLN B 289 66.900 -2.470 -4.623 1.00123.55 C
ANISOU 4044 CD GLN B 289 20569 12649 13725 420 5169 2792 C
ATOM 4045 OE1 GLN B 289 66.466 -1.320 -4.600 1.00135.30 O
ANISOU 4045 OE1 GLN B 289 22145 14033 15230 391 5040 2967 O
ATOM 4046 NE2 GLN B 289 67.888 -2.878 -3.833 1.00114.80 N
ANISOU 4046 NE2 GLN B 289 19107 11554 12959 423 5403 2620 N
ATOM 4047 N MET B 290 62.942 -3.028 -7.510 1.00130.07 N
ANISOU 4047 N MET B 290 22590 13632 13198 551 4089 3178 N
ATOM 4048 CA MET B 290 61.598 -3.137 -6.941 1.00121.43 C
ANISOU 4048 CA MET B 290 21385 12638 12114 669 3621 3182 C
ATOM 4049 C MET B 290 60.771 -4.231 -7.613 1.00115.48 C
ANISOU 4049 C MET B 290 20844 12009 11022 719 3394 3120 C
ATOM 4050 O MET B 290 60.076 -5.010 -6.938 1.00115.97 O
ANISOU 4050 O MET B 290 20691 12211 11161 804 3156 2985 O
ATOM 4051 CB MET B 290 60.897 -1.780 -7.012 1.00129.13 C
ANISOU 4051 CB MET B 290 22480 13483 13101 681 3370 3427 C
ATOM 4052 CG MET B 290 59.486 -1.770 -6.445 1.00132.67 C
ANISOU 4052 CG MET B 290 22805 14010 13593 811 2884 3448 C
ATOM 4053 SD MET B 290 58.236 -1.667 -7.736 1.00138.69 S
ANISOU 4053 SD MET B 290 24026 14753 13916 856 2492 3650 S
ATOM 4054 CE MET B 290 58.508 0.015 -8.304 1.00135.87 C
ANISOU 4054 CE MET B 290 23927 14139 13559 793 2547 3959 C
ATOM 4055 N ARG B 291 60.854 -4.321 -8.942 1.00121.15 N
ANISOU 4055 N ARG B 291 21997 12674 11361 659 3475 3214 N
ATOM 4056 CA ARG B 291 60.050 -5.303 -9.658 1.00119.49 C
ANISOU 4056 CA ARG B 291 22031 12563 10808 700 3247 3161 C
ATOM 4057 C ARG B 291 60.515 -6.715 -9.326 1.00111.53 C
ANISOU 4057 C ARG B 291 20838 11670 9868 710 3413 2898 C
ATOM 4058 O ARG B 291 59.690 -7.621 -9.156 1.00110.51 O
ANISOU 4058 O ARG B 291 20663 11660 9666 774 3146 2790 O
ATOM 4059 CB ARG B 291 60.109 -5.046 -11.170 1.00130.77 C
ANISOU 4059 CB ARG B 291 23998 13893 11796 633 3319 3320 C
ATOM 4060 CG ARG B 291 59.514 -3.697 -11.683 1.00138.44 C
ANISOU 4060 CG ARG B 291 25234 14732 12636 634 3097 3614 C
ATOM 4061 CD ARG B 291 58.002 -3.463 -11.442 1.00143.83 C
ANISOU 4061 CD ARG B 291 25889 15462 13297 757 2538 3705 C
ATOM 4062 NE ARG B 291 57.652 -2.040 -11.590 1.00145.68 N
ANISOU 4062 NE ARG B 291 26245 15539 13567 772 2374 3977 N
ATOM 4063 CZ ARG B 291 56.447 -1.511 -11.363 1.00136.94 C
ANISOU 4063 CZ ARG B 291 25101 14420 12512 886 1912 4103 C
ATOM 4064 NH1 ARG B 291 55.437 -2.271 -10.961 1.00141.48 N
ANISOU 4064 NH1 ARG B 291 25510 15140 13104 990 1565 3981 N
ATOM 4065 NH2 ARG B 291 56.254 -0.209 -11.530 1.00122.63 N
ANISOU 4065 NH2 ARG B 291 23408 12434 10753 900 1799 4355 N
ATOM 4066 N ALA B 292 61.834 -6.920 -9.219 1.00115.05 N
ANISOU 4066 N ALA B 292 21169 12071 10473 647 3847 2797 N
ATOM 4067 CA ALA B 292 62.349 -8.220 -8.784 1.00119.72 C
ANISOU 4067 CA ALA B 292 21542 12749 11195 671 4001 2556 C
ATOM 4068 C ALA B 292 61.884 -8.586 -7.374 1.00117.71 C
ANISOU 4068 C ALA B 292 20844 12610 11272 763 3782 2432 C
ATOM 4069 O ALA B 292 61.510 -9.739 -7.116 1.00116.58 O
ANISOU 4069 O ALA B 292 20612 12570 11114 812 3660 2280 O
ATOM 4070 CB ALA B 292 63.875 -8.232 -8.861 1.00127.31 C
ANISOU 4070 CB ALA B 292 22426 13622 12324 598 4496 2490 C
ATOM 4071 N ARG B 293 61.915 -7.625 -6.444 1.00111.88 N
ANISOU 4071 N ARG B 293 19834 11845 10829 783 3741 2496 N
ATOM 4072 CA ARG B 293 61.476 -7.874 -5.068 1.00 91.56 C
ANISOU 4072 CA ARG B 293 16855 9375 8560 871 3548 2388 C
ATOM 4073 C ARG B 293 59.986 -8.202 -4.952 1.00 95.19 C
ANISOU 4073 C ARG B 293 17348 9943 8879 942 3107 2406 C
ATOM 4074 O ARG B 293 59.584 -8.955 -4.052 1.00103.68 O
ANISOU 4074 O ARG B 293 18155 11131 10107 1006 2972 2270 O
ATOM 4075 CB ARG B 293 61.784 -6.643 -4.223 1.00 76.27 C
ANISOU 4075 CB ARG B 293 14685 7362 6931 871 3599 2471 C
ATOM 4076 CG ARG B 293 63.232 -6.474 -3.855 1.00 75.63 C
ANISOU 4076 CG ARG B 293 14411 7203 7122 820 4003 2399 C
ATOM 4077 CD ARG B 293 63.393 -5.119 -3.216 1.00 75.52 C
ANISOU 4077 CD ARG B 293 14248 7088 7359 804 4021 2512 C
ATOM 4078 NE ARG B 293 64.688 -4.926 -2.591 1.00 88.34 N
ANISOU 4078 NE ARG B 293 15605 8644 9318 766 4361 2427 N
ATOM 4079 CZ ARG B 293 65.059 -3.784 -2.028 1.00 98.21 C
ANISOU 4079 CZ ARG B 293 16708 9784 10825 733 4444 2503 C
ATOM 4080 NH1 ARG B 293 64.230 -2.747 -2.030 1.00 92.80 N
ANISOU 4080 NH1 ARG B 293 16130 9035 10096 738 4211 2670 N
ATOM 4081 NH2 ARG B 293 66.254 -3.676 -1.467 1.00109.71 N
ANISOU 4081 NH2 ARG B 293 17907 11177 12602 694 4748 2413 N
ATOM 4082 N ARG B 294 59.161 -7.713 -5.882 1.00 89.58 N
ANISOU 4082 N ARG B 294 16969 9194 7872 933 2881 2572 N
ATOM 4083 CA ARG B 294 57.731 -8.035 -5.838 1.00 85.28 C
ANISOU 4083 CA ARG B 294 16457 8742 7202 1003 2448 2592 C
ATOM 4084 C ARG B 294 57.425 -9.526 -6.030 1.00 94.69 C
ANISOU 4084 C ARG B 294 17688 10046 8244 1012 2386 2419 C
ATOM 4085 O ARG B 294 56.608 -10.090 -5.285 1.00 95.49 O
ANISOU 4085 O ARG B 294 17577 10256 8450 1072 2144 2336 O
ATOM 4086 CB ARG B 294 57.027 -7.248 -6.944 1.00104.03 C
ANISOU 4086 CB ARG B 294 19219 11034 9273 996 2226 2810 C
ATOM 4087 CG ARG B 294 56.867 -5.758 -6.719 1.00118.98 C
ANISOU 4087 CG ARG B 294 21085 12810 11312 1013 2135 3014 C
ATOM 4088 CD ARG B 294 56.029 -5.165 -7.848 1.00118.56 C
ANISOU 4088 CD ARG B 294 21432 12680 10936 1029 1851 3229 C
ATOM 4089 NE ARG B 294 55.811 -3.727 -7.720 1.00108.48 N
ANISOU 4089 NE ARG B 294 20160 11261 9795 1055 1734 3447 N
ATOM 4090 CZ ARG B 294 54.613 -3.154 -7.724 1.00107.67 C
ANISOU 4090 CZ ARG B 294 20085 11131 9694 1155 1309 3588 C
ATOM 4091 NH1 ARG B 294 53.526 -3.902 -7.846 1.00109.75 N
ANISOU 4091 NH1 ARG B 294 20365 11511 9825 1233 964 3530 N
ATOM 4092 NH2 ARG B 294 54.501 -1.838 -7.611 1.00108.63 N
ANISOU 4092 NH2 ARG B 294 20212 11096 9968 1182 1223 3787 N
ATOM 4093 N LYS B 295 58.088 -10.198 -6.980 1.00104.34 N
ANISOU 4093 N LYS B 295 19174 11232 9237 951 2617 2359 N
ATOM 4094 CA LYS B 295 57.831 -11.627 -7.188 1.00105.52 C
ANISOU 4094 CA LYS B 295 19382 11460 9249 956 2566 2193 C
ATOM 4095 C LYS B 295 58.186 -12.447 -5.953 1.00102.02 C
ANISOU 4095 C LYS B 295 18528 11096 9141 993 2657 2010 C
ATOM 4096 O LYS B 295 57.393 -13.284 -5.491 1.00 98.67 O
ANISOU 4096 O LYS B 295 17990 10768 8733 1030 2432 1918 O
ATOM 4097 CB LYS B 295 58.573 -12.130 -8.428 1.00117.76 C
ANISOU 4097 CB LYS B 295 21302 12935 10507 887 2833 2162 C
ATOM 4098 CG LYS B 295 57.887 -11.693 -9.719 1.00132.39 C
ANISOU 4098 CG LYS B 295 23626 14738 11938 862 2640 2317 C
ATOM 4099 CD LYS B 295 58.586 -12.176 -10.982 1.00138.94 C
ANISOU 4099 CD LYS B 295 24861 15490 12439 791 2912 2287 C
ATOM 4100 CE LYS B 295 57.676 -11.984 -12.193 1.00136.78 C
ANISOU 4100 CE LYS B 295 25066 15190 11712 782 2631 2412 C
ATOM 4101 NZ LYS B 295 58.142 -12.721 -13.399 1.00134.88 N
ANISOU 4101 NZ LYS B 295 25247 14894 11106 721 2839 2344 N
ATOM 4102 N THR B 296 59.389 -12.238 -5.420 1.00103.19 N
ANISOU 4102 N THR B 296 18459 11195 9554 982 2985 1960 N
ATOM 4103 CA THR B 296 59.810 -12.996 -4.250 1.00 85.70 C
ANISOU 4103 CA THR B 296 15867 9040 7657 1026 3067 1799 C
ATOM 4104 C THR B 296 58.877 -12.720 -3.078 1.00 64.33 C
ANISOU 4104 C THR B 296 12867 6430 5145 1093 2780 1808 C
ATOM 4105 O THR B 296 58.583 -13.625 -2.294 1.00 61.24 O
ANISOU 4105 O THR B 296 12265 6125 4880 1132 2690 1686 O
ATOM 4106 CB THR B 296 61.274 -12.703 -3.912 1.00 77.21 C
ANISOU 4106 CB THR B 296 14616 7881 6839 1009 3443 1761 C
ATOM 4107 OG1 THR B 296 61.482 -11.290 -3.797 1.00 95.01 O
ANISOU 4107 OG1 THR B 296 16842 10069 9188 990 3496 1903 O
ATOM 4108 CG2 THR B 296 62.189 -13.282 -4.986 1.00 71.65 C
ANISOU 4108 CG2 THR B 296 14169 7092 5963 950 3745 1717 C
ATOM 4109 N ALA B 297 58.442 -11.467 -2.902 1.00 70.66 N
ANISOU 4109 N ALA B 297 13649 7208 5991 1106 2651 1955 N
ATOM 4110 CA ALA B 297 57.597 -11.167 -1.749 1.00 62.41 C
ANISOU 4110 CA ALA B 297 12319 6245 5150 1176 2406 1960 C
ATOM 4111 C ALA B 297 56.244 -11.855 -1.885 1.00 66.47 C
ANISOU 4111 C ALA B 297 12910 6856 5492 1202 2061 1950 C
ATOM 4112 O ALA B 297 55.682 -12.346 -0.897 1.00 82.22 O
ANISOU 4112 O ALA B 297 14650 8947 7642 1250 1925 1870 O
ATOM 4113 CB ALA B 297 57.408 -9.659 -1.601 1.00 62.28 C
ANISOU 4113 CB ALA B 297 12290 6153 5222 1190 2336 2128 C
ATOM 4114 N LYS B 298 55.723 -11.935 -3.111 1.00 67.96 N
ANISOU 4114 N LYS B 298 13457 7015 5349 1169 1921 2028 N
ATOM 4115 CA LYS B 298 54.478 -12.663 -3.336 1.00 77.15 C
ANISOU 4115 CA LYS B 298 14717 8261 6336 1188 1589 2008 C
ATOM 4116 C LYS B 298 54.653 -14.136 -2.980 1.00 76.66 C
ANISOU 4116 C LYS B 298 14554 8268 6304 1172 1675 1817 C
ATOM 4117 O LYS B 298 53.832 -14.727 -2.254 1.00 71.74 O
ANISOU 4117 O LYS B 298 13754 7738 5765 1203 1476 1757 O
ATOM 4118 CB LYS B 298 54.116 -12.502 -4.820 1.00 95.16 C
ANISOU 4118 CB LYS B 298 17443 10478 8234 1153 1463 2115 C
ATOM 4119 CG LYS B 298 52.792 -13.028 -5.363 1.00105.09 C
ANISOU 4119 CG LYS B 298 18893 11789 9246 1172 1071 2128 C
ATOM 4120 CD LYS B 298 53.011 -13.348 -6.857 1.00111.73 C
ANISOU 4120 CD LYS B 298 20201 12561 9689 1113 1116 2143 C
ATOM 4121 CE LYS B 298 51.741 -13.310 -7.703 1.00116.77 C
ANISOU 4121 CE LYS B 298 21131 13206 10031 1138 683 2229 C
ATOM 4122 NZ LYS B 298 51.970 -13.866 -9.079 1.00126.61 N
ANISOU 4122 NZ LYS B 298 22839 14394 10873 1076 737 2199 N
ATOM 4123 N MET B 299 55.773 -14.716 -3.412 1.00 82.25 N
ANISOU 4123 N MET B 299 15356 8920 6977 1127 1987 1726 N
ATOM 4124 CA MET B 299 56.067 -16.105 -3.085 1.00 74.81 C
ANISOU 4124 CA MET B 299 14324 8010 6092 1119 2087 1553 C
ATOM 4125 C MET B 299 56.138 -16.324 -1.576 1.00 77.92 C
ANISOU 4125 C MET B 299 14295 8476 6835 1170 2099 1477 C
ATOM 4126 O MET B 299 55.571 -17.286 -1.043 1.00 79.54 O
ANISOU 4126 O MET B 299 14395 8752 7076 1178 1975 1388 O
ATOM 4127 CB MET B 299 57.388 -16.502 -3.742 1.00 68.72 C
ANISOU 4127 CB MET B 299 13693 7140 5279 1081 2444 1488 C
ATOM 4128 CG MET B 299 57.745 -17.962 -3.622 1.00 76.15 C
ANISOU 4128 CG MET B 299 14608 8078 6248 1076 2550 1326 C
ATOM 4129 SD MET B 299 59.382 -18.248 -4.310 1.00 93.18 S
ANISOU 4129 SD MET B 299 16888 10103 8412 1048 2989 1270 S
ATOM 4130 CE MET B 299 60.395 -17.340 -3.144 1.00 92.53 C
ANISOU 4130 CE MET B 299 16398 10007 8752 1090 3183 1298 C
ATOM 4131 N LEU B 300 56.873 -15.454 -0.874 1.00 80.84 N
ANISOU 4131 N LEU B 300 14437 8821 7458 1200 2260 1509 N
ATOM 4132 CA LEU B 300 57.056 -15.623 0.565 1.00 73.56 C
ANISOU 4132 CA LEU B 300 13134 7958 6857 1254 2287 1433 C
ATOM 4133 C LEU B 300 55.751 -15.456 1.335 1.00 78.41 C
ANISOU 4133 C LEU B 300 13600 8678 7514 1294 1992 1468 C
ATOM 4134 O LEU B 300 55.517 -16.162 2.327 1.00 87.67 O
ANISOU 4134 O LEU B 300 14546 9925 8838 1321 1952 1381 O
ATOM 4135 CB LEU B 300 58.109 -14.640 1.074 1.00 66.70 C
ANISOU 4135 CB LEU B 300 12089 7025 6228 1278 2508 1464 C
ATOM 4136 CG LEU B 300 59.514 -14.801 0.472 1.00 66.38 C
ANISOU 4136 CG LEU B 300 12140 6875 6208 1243 2831 1429 C
ATOM 4137 CD1 LEU B 300 60.435 -13.677 0.927 1.00 73.46 C
ANISOU 4137 CD1 LEU B 300 12877 7699 7334 1254 3025 1480 C
ATOM 4138 CD2 LEU B 300 60.131 -16.162 0.769 1.00 60.98 C
ANISOU 4138 CD2 LEU B 300 11362 6187 5622 1254 2944 1291 C
ATOM 4139 N MET B 301 54.886 -14.532 0.905 1.00 67.36 N
ANISOU 4139 N MET B 301 12328 7277 5989 1301 1781 1604 N
ATOM 4140 CA MET B 301 53.599 -14.422 1.581 1.00 55.84 C
ANISOU 4140 CA MET B 301 10734 5906 4578 1350 1490 1643 C
ATOM 4141 C MET B 301 52.768 -15.678 1.372 1.00 65.74 C
ANISOU 4141 C MET B 301 12077 7229 5673 1322 1315 1573 C
ATOM 4142 O MET B 301 52.090 -16.144 2.299 1.00 78.84 O
ANISOU 4142 O MET B 301 13533 8974 7448 1351 1200 1531 O
ATOM 4143 CB MET B 301 52.842 -13.188 1.104 1.00 55.22 C
ANISOU 4143 CB MET B 301 10779 5783 4421 1383 1264 1816 C
ATOM 4144 CG MET B 301 53.534 -11.889 1.426 1.00 80.16 C
ANISOU 4144 CG MET B 301 13841 8859 7757 1408 1413 1895 C
ATOM 4145 SD MET B 301 52.798 -10.492 0.558 1.00109.45 S
ANISOU 4145 SD MET B 301 17780 12465 11342 1435 1158 2118 S
ATOM 4146 CE MET B 301 54.145 -9.308 0.610 1.00116.39 C
ANISOU 4146 CE MET B 301 18640 13212 12371 1407 1482 2177 C
ATOM 4147 N VAL B 302 52.877 -16.293 0.191 1.00 63.04 N
ANISOU 4147 N VAL B 302 12046 6842 5066 1262 1322 1550 N
ATOM 4148 CA VAL B 302 52.167 -17.551 -0.009 1.00 64.13 C
ANISOU 4148 CA VAL B 302 12288 7027 5052 1226 1173 1466 C
ATOM 4149 C VAL B 302 52.746 -18.637 0.889 1.00 66.15 C
ANISOU 4149 C VAL B 302 12330 7310 5496 1216 1366 1321 C
ATOM 4150 O VAL B 302 52.008 -19.452 1.455 1.00 66.30 O
ANISOU 4150 O VAL B 302 12261 7395 5534 1208 1234 1269 O
ATOM 4151 CB VAL B 302 52.219 -17.967 -1.490 1.00 75.08 C
ANISOU 4151 CB VAL B 302 14084 8344 6101 1168 1150 1459 C
ATOM 4152 CG1 VAL B 302 51.567 -19.331 -1.675 1.00 77.58 C
ANISOU 4152 CG1 VAL B 302 14523 8689 6264 1123 1010 1349 C
ATOM 4153 CG2 VAL B 302 51.556 -16.915 -2.359 1.00 76.76 C
ANISOU 4153 CG2 VAL B 302 14521 8526 6117 1185 912 1616 C
ATOM 4154 N VAL B 303 54.072 -18.673 1.028 1.00 66.30 N
ANISOU 4154 N VAL B 303 12268 7266 5656 1220 1668 1264 N
ATOM 4155 CA VAL B 303 54.694 -19.699 1.862 1.00 64.90 C
ANISOU 4155 CA VAL B 303 11894 7093 5674 1227 1824 1141 C
ATOM 4156 C VAL B 303 54.257 -19.545 3.316 1.00 65.01 C
ANISOU 4156 C VAL B 303 11568 7203 5932 1274 1747 1140 C
ATOM 4157 O VAL B 303 53.940 -20.532 3.996 1.00 63.42 O
ANISOU 4157 O VAL B 303 11259 7046 5794 1265 1710 1070 O
ATOM 4158 CB VAL B 303 56.222 -19.662 1.705 1.00 57.35 C
ANISOU 4158 CB VAL B 303 10914 6036 4839 1240 2130 1100 C
ATOM 4159 CG1 VAL B 303 56.872 -20.645 2.667 1.00 62.85 C
ANISOU 4159 CG1 VAL B 303 11389 6723 5768 1268 2247 1000 C
ATOM 4160 CG2 VAL B 303 56.587 -19.991 0.274 1.00 62.18 C
ANISOU 4160 CG2 VAL B 303 11883 6556 5187 1190 2228 1091 C
ATOM 4161 N VAL B 304 54.201 -18.303 3.805 1.00 63.76 N
ANISOU 4161 N VAL B 304 11258 7068 5900 1325 1725 1222 N
ATOM 4162 CA VAL B 304 53.817 -18.092 5.196 1.00 54.37 C
ANISOU 4162 CA VAL B 304 9761 5964 4931 1380 1674 1217 C
ATOM 4163 C VAL B 304 52.356 -18.456 5.381 1.00 65.36 C
ANISOU 4163 C VAL B 304 11168 7446 6220 1372 1421 1251 C
ATOM 4164 O VAL B 304 51.967 -19.034 6.403 1.00 80.79 O
ANISOU 4164 O VAL B 304 12931 9474 8290 1384 1400 1209 O
ATOM 4165 CB VAL B 304 54.083 -16.640 5.631 1.00 53.58 C
ANISOU 4165 CB VAL B 304 9526 5850 4982 1444 1717 1295 C
ATOM 4166 CG1 VAL B 304 53.477 -16.397 7.008 1.00 37.74 C
ANISOU 4166 CG1 VAL B 304 7240 3937 3162 1511 1645 1296 C
ATOM 4167 CG2 VAL B 304 55.576 -16.335 5.625 1.00 64.84 C
ANISOU 4167 CG2 VAL B 304 10905 7185 6547 1453 1978 1259 C
ATOM 4168 N LEU B 305 51.527 -18.148 4.383 1.00 67.78 N
ANISOU 4168 N LEU B 305 11712 7740 6300 1355 1213 1336 N
ATOM 4169 CA LEU B 305 50.113 -18.482 4.472 1.00 67.20 C
ANISOU 4169 CA LEU B 305 11669 7736 6127 1360 928 1379 C
ATOM 4170 C LEU B 305 49.909 -19.993 4.497 1.00 56.61 C
ANISOU 4170 C LEU B 305 10398 6417 4694 1286 932 1275 C
ATOM 4171 O LEU B 305 49.145 -20.518 5.319 1.00 50.87 O
ANISOU 4171 O LEU B 305 9537 5764 4025 1290 842 1267 O
ATOM 4172 CB LEU B 305 49.366 -17.840 3.306 1.00 69.47 C
ANISOU 4172 CB LEU B 305 12216 7984 6193 1369 659 1490 C
ATOM 4173 CG LEU B 305 47.859 -18.040 3.231 1.00 62.01 C
ANISOU 4173 CG LEU B 305 11320 7092 5148 1401 278 1545 C
ATOM 4174 CD1 LEU B 305 47.173 -17.491 4.463 1.00 50.45 C
ANISOU 4174 CD1 LEU B 305 9543 5696 3931 1514 183 1602 C
ATOM 4175 CD2 LEU B 305 47.375 -17.323 1.996 1.00 72.18 C
ANISOU 4175 CD2 LEU B 305 12868 8320 6237 1417 13 1646 C
ATOM 4176 N VAL B 306 50.600 -20.712 3.611 1.00 55.34 N
ANISOU 4176 N VAL B 306 10457 6179 4390 1220 1050 1197 N
ATOM 4177 CA VAL B 306 50.448 -22.162 3.572 1.00 65.65 C
ANISOU 4177 CA VAL B 306 11864 7473 5606 1150 1060 1092 C
ATOM 4178 C VAL B 306 50.954 -22.783 4.860 1.00 69.97 C
ANISOU 4178 C VAL B 306 12129 8048 6409 1160 1242 1023 C
ATOM 4179 O VAL B 306 50.367 -23.740 5.375 1.00 71.43 O
ANISOU 4179 O VAL B 306 12290 8263 6585 1116 1189 983 O
ATOM 4180 CB VAL B 306 51.201 -22.742 2.360 1.00 64.17 C
ANISOU 4180 CB VAL B 306 11975 7174 5231 1101 1180 1019 C
ATOM 4181 CG1 VAL B 306 51.176 -24.267 2.402 1.00 57.45 C
ANISOU 4181 CG1 VAL B 306 11226 6279 4322 1038 1223 899 C
ATOM 4182 CG2 VAL B 306 50.622 -22.204 1.069 1.00 72.89 C
ANISOU 4182 CG2 VAL B 306 13392 8254 6049 1083 973 1087 C
ATOM 4183 N PHE B 307 52.012 -22.211 5.433 1.00 67.29 N
ANISOU 4183 N PHE B 307 11580 7691 6295 1217 1437 1015 N
ATOM 4184 CA PHE B 307 52.513 -22.714 6.703 1.00 53.86 C
ANISOU 4184 CA PHE B 307 9613 6013 4840 1240 1563 958 C
ATOM 4185 C PHE B 307 51.493 -22.504 7.818 1.00 37.36 C
ANISOU 4185 C PHE B 307 7314 4042 2838 1257 1447 1005 C
ATOM 4186 O PHE B 307 51.193 -23.429 8.594 1.00 36.95 O
ANISOU 4186 O PHE B 307 7174 4023 2842 1223 1456 967 O
ATOM 4187 CB PHE B 307 53.839 -22.018 7.015 1.00 52.05 C
ANISOU 4187 CB PHE B 307 9233 5730 4814 1307 1744 949 C
ATOM 4188 CG PHE B 307 54.464 -22.449 8.300 1.00 55.32 C
ANISOU 4188 CG PHE B 307 9394 6150 5473 1345 1831 904 C
ATOM 4189 CD1 PHE B 307 55.245 -23.586 8.354 1.00 55.51 C
ANISOU 4189 CD1 PHE B 307 9455 6089 5547 1337 1934 840 C
ATOM 4190 CD2 PHE B 307 54.285 -21.704 9.454 1.00 69.67 C
ANISOU 4190 CD2 PHE B 307 10961 8047 7464 1398 1801 935 C
ATOM 4191 CE1 PHE B 307 55.833 -23.980 9.536 1.00 64.01 C
ANISOU 4191 CE1 PHE B 307 10328 7160 6832 1378 1977 825 C
ATOM 4192 CE2 PHE B 307 54.868 -22.092 10.639 1.00 70.25 C
ANISOU 4192 CE2 PHE B 307 10835 8121 7737 1430 1848 905 C
ATOM 4193 CZ PHE B 307 55.641 -23.234 10.683 1.00 68.35 C
ANISOU 4193 CZ PHE B 307 10638 7796 7534 1418 1922 858 C
ATOM 4194 N ALA B 308 50.907 -21.305 7.876 1.00 36.51 N
ANISOU 4194 N ALA B 308 7148 3989 2735 1314 1340 1100 N
ATOM 4195 CA ALA B 308 49.918 -21.021 8.910 1.00 61.88 C
ANISOU 4195 CA ALA B 308 10167 7311 6034 1360 1247 1160 C
ATOM 4196 C ALA B 308 48.700 -21.929 8.786 1.00 76.07 C
ANISOU 4196 C ALA B 308 12084 9152 7667 1302 1083 1184 C
ATOM 4197 O ALA B 308 48.211 -22.464 9.792 1.00 69.85 O
ANISOU 4197 O ALA B 308 11142 8439 6960 1290 1118 1184 O
ATOM 4198 CB ALA B 308 49.505 -19.549 8.846 1.00 57.01 C
ANISOU 4198 CB ALA B 308 9501 6711 5451 1461 1143 1271 C
ATOM 4199 N LEU B 309 48.248 -22.182 7.551 1.00 79.10 N
ANISOU 4199 N LEU B 309 12763 9485 7807 1256 907 1198 N
ATOM 4200 CA LEU B 309 47.099 -23.065 7.356 1.00 71.28 C
ANISOU 4200 CA LEU B 309 11933 8517 6635 1196 702 1207 C
ATOM 4201 C LEU B 309 47.426 -24.508 7.698 1.00 67.21 C
ANISOU 4201 C LEU B 309 11455 7966 6115 1081 865 1098 C
ATOM 4202 O LEU B 309 46.638 -25.192 8.364 1.00 60.97 O
ANISOU 4202 O LEU B 309 10498 7229 5439 992 794 1047 O
ATOM 4203 CB LEU B 309 46.604 -22.977 5.914 1.00 63.07 C
ANISOU 4203 CB LEU B 309 11224 7418 5322 1168 424 1220 C
ATOM 4204 CG LEU B 309 45.966 -21.649 5.549 1.00 64.31 C
ANISOU 4204 CG LEU B 309 11358 7595 5482 1284 158 1341 C
ATOM 4205 CD1 LEU B 309 45.744 -21.551 4.052 1.00 84.09 C
ANISOU 4205 CD1 LEU B 309 14200 10031 7720 1243 -85 1340 C
ATOM 4206 CD2 LEU B 309 44.649 -21.579 6.292 1.00 46.39 C
ANISOU 4206 CD2 LEU B 309 8658 5443 3523 1254 -103 1273 C
ATOM 4207 N CYS B 310 48.597 -24.982 7.289 1.00 66.99 N
ANISOU 4207 N CYS B 310 11496 7845 6112 1050 1051 1000 N
ATOM 4208 CA CYS B 310 48.903 -26.379 7.516 1.00 68.93 C
ANISOU 4208 CA CYS B 310 11808 8021 6359 967 1173 903 C
ATOM 4209 C CYS B 310 49.036 -26.671 8.995 1.00 76.11 C
ANISOU 4209 C CYS B 310 12421 8987 7511 975 1310 907 C
ATOM 4210 O CYS B 310 48.626 -27.744 9.456 1.00 86.30 O
ANISOU 4210 O CYS B 310 13754 10255 8783 888 1338 882 O
ATOM 4211 CB CYS B 310 50.210 -26.747 6.817 1.00 64.97 C
ANISOU 4211 CB CYS B 310 11424 7394 5866 983 1342 815 C
ATOM 4212 SG CYS B 310 50.110 -26.929 5.038 1.00 69.09 S
ANISOU 4212 SG CYS B 310 12374 7819 6058 935 1234 772 S
ATOM 4213 N TYR B 311 49.549 -25.708 9.758 1.00 70.00 N
ANISOU 4213 N TYR B 311 11370 8277 6950 1067 1384 938 N
ATOM 4214 CA TYR B 311 49.784 -25.949 11.170 1.00 60.72 C
ANISOU 4214 CA TYR B 311 9928 7149 5992 1078 1491 926 C
ATOM 4215 C TYR B 311 48.632 -25.534 12.085 1.00 66.42 C
ANISOU 4215 C TYR B 311 10477 8010 6749 1079 1448 1008 C
ATOM 4216 O TYR B 311 48.597 -25.978 13.237 1.00 63.20 O
ANISOU 4216 O TYR B 311 9894 7645 6474 1049 1534 994 O
ATOM 4217 CB TYR B 311 51.080 -25.221 11.536 1.00 60.10 C
ANISOU 4217 CB TYR B 311 9681 7042 6113 1175 1585 897 C
ATOM 4218 CG TYR B 311 52.308 -26.003 11.085 1.00 64.23 C
ANISOU 4218 CG TYR B 311 10319 7424 6661 1184 1689 825 C
ATOM 4219 CD1 TYR B 311 52.677 -26.011 9.736 1.00 65.78 C
ANISOU 4219 CD1 TYR B 311 10752 7532 6711 1179 1708 803 C
ATOM 4220 CD2 TYR B 311 53.107 -26.704 11.985 1.00 64.37 C
ANISOU 4220 CD2 TYR B 311 10232 7391 6837 1212 1771 794 C
ATOM 4221 CE1 TYR B 311 53.788 -26.711 9.290 1.00 63.12 C
ANISOU 4221 CE1 TYR B 311 10530 7058 6395 1203 1835 748 C
ATOM 4222 CE2 TYR B 311 54.231 -27.406 11.546 1.00 61.77 C
ANISOU 4222 CE2 TYR B 311 10022 6917 6529 1250 1876 753 C
ATOM 4223 CZ TYR B 311 54.563 -27.408 10.199 1.00 67.61 C
ANISOU 4223 CZ TYR B 311 10982 7570 7135 1245 1922 728 C
ATOM 4224 OH TYR B 311 55.674 -28.100 9.759 1.00 84.05 O
ANISOU 4224 OH TYR B 311 13189 9504 9243 1289 2056 695 O
ATOM 4225 N LEU B 312 47.670 -24.741 11.595 1.00 74.59 N
ANISOU 4225 N LEU B 312 11567 9109 7665 1122 1305 1100 N
ATOM 4226 CA LEU B 312 46.548 -24.298 12.428 1.00 69.08 C
ANISOU 4226 CA LEU B 312 10515 8543 7189 1094 1177 1076 C
ATOM 4227 C LEU B 312 45.712 -25.415 13.047 1.00 70.45 C
ANISOU 4227 C LEU B 312 10556 8753 7459 925 1159 1004 C
ATOM 4228 O LEU B 312 45.447 -25.361 14.265 1.00 73.61 O
ANISOU 4228 O LEU B 312 10694 9246 8029 912 1266 996 O
ATOM 4229 CB LEU B 312 45.653 -23.381 11.587 1.00 64.60 C
ANISOU 4229 CB LEU B 312 9911 8004 6630 1128 886 1088 C
ATOM 4230 CG LEU B 312 44.379 -22.779 12.188 1.00 55.42 C
ANISOU 4230 CG LEU B 312 8368 6968 5721 1123 711 1047 C
ATOM 4231 CD1 LEU B 312 44.654 -21.807 13.322 1.00 44.05 C
ANISOU 4231 CD1 LEU B 312 6666 5606 4466 1246 870 1067 C
ATOM 4232 CD2 LEU B 312 43.575 -22.111 11.099 1.00 61.07 C
ANISOU 4232 CD2 LEU B 312 9124 7670 6410 1161 374 1061 C
ATOM 4233 N PRO B 313 45.256 -26.426 12.299 1.00 65.42 N
ANISOU 4233 N PRO B 313 10094 8040 6722 783 1036 947 N
ATOM 4234 CA PRO B 313 44.342 -27.414 12.902 1.00 63.29 C
ANISOU 4234 CA PRO B 313 9667 7795 6586 596 1013 880 C
ATOM 4235 C PRO B 313 44.920 -28.165 14.089 1.00 70.05 C
ANISOU 4235 C PRO B 313 10496 8631 7489 565 1288 906 C
ATOM 4236 O PRO B 313 44.240 -28.288 15.117 1.00 71.57 O
ANISOU 4236 O PRO B 313 10429 8913 7850 482 1346 896 O
ATOM 4237 CB PRO B 313 44.045 -28.359 11.729 1.00 59.99 C
ANISOU 4237 CB PRO B 313 9525 7257 6013 463 840 808 C
ATOM 4238 CG PRO B 313 45.213 -28.182 10.800 1.00 62.41 C
ANISOU 4238 CG PRO B 313 10193 7456 6063 591 912 846 C
ATOM 4239 CD PRO B 313 45.559 -26.735 10.892 1.00 62.42 C
ANISOU 4239 CD PRO B 313 10078 7541 6096 773 927 932 C
ATOM 4240 N ILE B 314 46.170 -28.628 14.012 1.00 71.82 N
ANISOU 4240 N ILE B 314 10975 8740 7574 641 1466 943 N
ATOM 4241 CA ILE B 314 46.710 -29.410 15.121 1.00 73.37 C
ANISOU 4241 CA ILE B 314 11168 8897 7810 623 1685 978 C
ATOM 4242 C ILE B 314 47.029 -28.502 16.294 1.00 78.95 C
ANISOU 4242 C ILE B 314 11628 9735 8636 741 1790 1023 C
ATOM 4243 O ILE B 314 46.922 -28.910 17.451 1.00 86.78 O
ANISOU 4243 O ILE B 314 12482 10761 9730 681 1865 1022 O
ATOM 4244 CB ILE B 314 47.928 -30.252 14.722 1.00 77.65 C
ANISOU 4244 CB ILE B 314 11953 9269 8283 666 1756 945 C
ATOM 4245 CG1 ILE B 314 48.249 -31.188 15.899 1.00 79.96 C
ANISOU 4245 CG1 ILE B 314 12169 9513 8699 619 1848 943 C
ATOM 4246 CG2 ILE B 314 49.098 -29.365 14.351 1.00 72.32 C
ANISOU 4246 CG2 ILE B 314 11207 8592 7679 829 1717 898 C
ATOM 4247 CD1 ILE B 314 49.388 -32.145 15.669 1.00 92.89 C
ANISOU 4247 CD1 ILE B 314 13975 10972 10348 673 1884 888 C
ATOM 4248 N SER B 315 47.483 -27.279 16.019 1.00 78.72 N
ANISOU 4248 N SER B 315 11509 9756 8645 883 1724 1015 N
ATOM 4249 CA SER B 315 47.784 -26.354 17.104 1.00 65.48 C
ANISOU 4249 CA SER B 315 9573 8175 7133 970 1741 998 C
ATOM 4250 C SER B 315 46.526 -26.056 17.903 1.00 68.62 C
ANISOU 4250 C SER B 315 9770 8736 7568 930 1827 1039 C
ATOM 4251 O SER B 315 46.522 -26.130 19.141 1.00 75.92 O
ANISOU 4251 O SER B 315 10533 9715 8600 894 1876 1004 O
ATOM 4252 CB SER B 315 48.355 -25.057 16.543 1.00 55.76 C
ANISOU 4252 CB SER B 315 8315 6941 5929 1112 1676 998 C
ATOM 4253 OG SER B 315 49.537 -25.287 15.809 1.00 71.84 O
ANISOU 4253 OG SER B 315 10496 8839 7960 1140 1648 953 O
ATOM 4254 N VAL B 316 45.433 -25.747 17.204 1.00 63.95 N
ANISOU 4254 N VAL B 316 9074 8186 7039 868 1646 997 N
ATOM 4255 CA VAL B 316 44.180 -25.494 17.904 1.00 59.89 C
ANISOU 4255 CA VAL B 316 8241 7805 6709 786 1615 942 C
ATOM 4256 C VAL B 316 43.727 -26.751 18.637 1.00 58.62 C
ANISOU 4256 C VAL B 316 8068 7636 6568 593 1740 934 C
ATOM 4257 O VAL B 316 43.283 -26.695 19.793 1.00 64.90 O
ANISOU 4257 O VAL B 316 8665 8535 7458 548 1885 923 O
ATOM 4258 CB VAL B 316 43.110 -25.009 16.912 1.00 45.04 C
ANISOU 4258 CB VAL B 316 6239 5950 4924 760 1344 888 C
ATOM 4259 CG1 VAL B 316 41.734 -25.057 17.566 1.00 43.56 C
ANISOU 4259 CG1 VAL B 316 5701 5885 4966 637 1324 810 C
ATOM 4260 CG2 VAL B 316 43.455 -23.629 16.395 1.00 39.91 C
ANISOU 4260 CG2 VAL B 316 5580 5308 4276 957 1237 916 C
ATOM 4261 N LEU B 317 43.819 -27.903 17.970 1.00 53.49 N
ANISOU 4261 N LEU B 317 7650 6851 5824 470 1698 938 N
ATOM 4262 CA LEU B 317 43.357 -29.144 18.575 1.00 66.14 C
ANISOU 4262 CA LEU B 317 9266 8406 7457 266 1808 940 C
ATOM 4263 C LEU B 317 44.153 -29.483 19.834 1.00 68.48 C
ANISOU 4263 C LEU B 317 9639 8697 7685 309 2054 1022 C
ATOM 4264 O LEU B 317 43.581 -29.903 20.848 1.00 59.74 O
ANISOU 4264 O LEU B 317 8418 7640 6639 182 2196 1038 O
ATOM 4265 CB LEU B 317 43.497 -30.267 17.546 1.00 62.92 C
ANISOU 4265 CB LEU B 317 9142 7817 6948 154 1710 921 C
ATOM 4266 CG LEU B 317 42.423 -30.359 16.464 1.00 59.37 C
ANISOU 4266 CG LEU B 317 8628 7360 6568 22 1448 824 C
ATOM 4267 CD1 LEU B 317 42.663 -31.583 15.593 1.00 79.52 C
ANISOU 4267 CD1 LEU B 317 11506 9715 8994 -97 1383 789 C
ATOM 4268 CD2 LEU B 317 41.034 -30.366 17.074 1.00 51.97 C
ANISOU 4268 CD2 LEU B 317 7333 6542 5873 -152 1428 768 C
ATOM 4269 N ASN B 318 45.476 -29.287 19.794 1.00 70.19 N
ANISOU 4269 N ASN B 318 10030 8848 7790 484 2077 1061 N
ATOM 4270 CA ASN B 318 46.320 -29.565 20.947 1.00 61.65 C
ANISOU 4270 CA ASN B 318 8920 7744 6759 514 2046 1030 C
ATOM 4271 C ASN B 318 46.098 -28.572 22.068 1.00 68.79 C
ANISOU 4271 C ASN B 318 9589 8807 7743 561 2059 996 C
ATOM 4272 O ASN B 318 46.199 -28.943 23.241 1.00 77.51 O
ANISOU 4272 O ASN B 318 10671 9930 8849 511 2090 993 O
ATOM 4273 CB ASN B 318 47.790 -29.580 20.534 1.00 57.71 C
ANISOU 4273 CB ASN B 318 8546 7121 6259 660 1933 994 C
ATOM 4274 CG ASN B 318 48.211 -30.914 19.945 1.00 85.59 C
ANISOU 4274 CG ASN B 318 12320 10472 9727 610 1948 1004 C
ATOM 4275 OD1 ASN B 318 47.554 -31.935 20.158 1.00 90.81 O
ANISOU 4275 OD1 ASN B 318 13074 11077 10353 457 2027 1046 O
ATOM 4276 ND2 ASN B 318 49.307 -30.913 19.195 1.00108.77 N
ANISOU 4276 ND2 ASN B 318 15364 13301 12663 732 1895 963 N
ATOM 4277 N VAL B 319 45.792 -27.314 21.748 1.00 63.29 N
ANISOU 4277 N VAL B 319 8738 8213 7094 663 2039 971 N
ATOM 4278 CA VAL B 319 45.449 -26.392 22.821 1.00 54.34 C
ANISOU 4278 CA VAL B 319 7387 7219 6042 695 2065 917 C
ATOM 4279 C VAL B 319 44.157 -26.829 23.486 1.00 65.88 C
ANISOU 4279 C VAL B 319 8700 8790 7543 534 2231 915 C
ATOM 4280 O VAL B 319 44.055 -26.883 24.717 1.00 75.40 O
ANISOU 4280 O VAL B 319 9847 10055 8746 474 2275 876 O
ATOM 4281 CB VAL B 319 45.335 -24.956 22.297 1.00 39.64 C
ANISOU 4281 CB VAL B 319 5384 5428 4250 851 2018 891 C
ATOM 4282 CG1 VAL B 319 44.409 -24.176 23.201 1.00 32.12 C
ANISOU 4282 CG1 VAL B 319 4166 4632 3407 846 2096 820 C
ATOM 4283 CG2 VAL B 319 46.703 -24.317 22.240 1.00 52.52 C
ANISOU 4283 CG2 VAL B 319 7107 6963 5888 979 1879 874 C
ATOM 4284 N LEU B 320 43.143 -27.131 22.676 1.00 63.19 N
ANISOU 4284 N LEU B 320 8287 8478 7245 452 2344 961 N
ATOM 4285 CA LEU B 320 41.864 -27.543 23.238 1.00 52.44 C
ANISOU 4285 CA LEU B 320 6708 7198 6019 251 2449 917 C
ATOM 4286 C LEU B 320 41.977 -28.836 24.020 1.00 52.53 C
ANISOU 4286 C LEU B 320 6899 7129 5932 75 2592 984 C
ATOM 4287 O LEU B 320 41.299 -29.014 25.037 1.00 61.47 O
ANISOU 4287 O LEU B 320 7895 8348 7114 -55 2714 953 O
ATOM 4288 CB LEU B 320 40.846 -27.710 22.122 1.00 48.67 C
ANISOU 4288 CB LEU B 320 6085 6697 5709 130 2241 843 C
ATOM 4289 CG LEU B 320 40.542 -26.432 21.354 1.00 48.31 C
ANISOU 4289 CG LEU B 320 5848 6722 5787 291 2022 770 C
ATOM 4290 CD1 LEU B 320 39.556 -26.692 20.229 1.00 57.58 C
ANISOU 4290 CD1 LEU B 320 6909 7864 7105 172 1767 702 C
ATOM 4291 CD2 LEU B 320 39.978 -25.423 22.329 1.00 39.64 C
ANISOU 4291 CD2 LEU B 320 4430 5791 4840 368 2150 699 C
ATOM 4292 N LYS B 321 42.837 -29.743 23.581 1.00 49.32 N
ANISOU 4292 N LYS B 321 6791 6547 5402 69 2503 1045 N
ATOM 4293 CA LYS B 321 42.961 -31.007 24.290 1.00 62.01 C
ANISOU 4293 CA LYS B 321 8562 8052 6949 -82 2549 1095 C
ATOM 4294 C LYS B 321 43.807 -30.836 25.560 1.00 71.37 C
ANISOU 4294 C LYS B 321 9786 9275 8056 19 2472 1078 C
ATOM 4295 O LYS B 321 43.419 -31.295 26.641 1.00 85.36 O
ANISOU 4295 O LYS B 321 11547 11090 9795 -98 2569 1103 O
ATOM 4296 CB LYS B 321 43.438 -32.066 23.285 1.00 57.32 C
ANISOU 4296 CB LYS B 321 8249 7240 6291 -125 2498 1150 C
ATOM 4297 CG LYS B 321 43.841 -33.427 23.807 1.00 58.80 C
ANISOU 4297 CG LYS B 321 8654 7265 6422 -221 2509 1210 C
ATOM 4298 CD LYS B 321 44.482 -34.229 22.658 1.00 58.67 C
ANISOU 4298 CD LYS B 321 8913 7028 6353 -200 2432 1222 C
ATOM 4299 CE LYS B 321 45.141 -35.528 23.132 1.00 76.00 C
ANISOU 4299 CE LYS B 321 11333 9035 8508 -223 2423 1273 C
ATOM 4300 NZ LYS B 321 45.547 -36.372 21.974 1.00 80.71 N
ANISOU 4300 NZ LYS B 321 12194 9401 9069 -235 2386 1262 N
ATOM 4301 N ARG B 322 44.953 -30.157 25.465 1.00 60.11 N
ANISOU 4301 N ARG B 322 8407 7829 6605 221 2314 1041 N
ATOM 4302 CA ARG B 322 45.904 -30.045 26.570 1.00 58.99 C
ANISOU 4302 CA ARG B 322 8325 7686 6403 312 2243 1034 C
ATOM 4303 C ARG B 322 45.572 -28.899 27.516 1.00 69.54 C
ANISOU 4303 C ARG B 322 9481 9191 7750 344 2268 958 C
ATOM 4304 O ARG B 322 45.775 -29.018 28.728 1.00 91.97 O
ANISOU 4304 O ARG B 322 12365 12073 10507 325 2296 966 O
ATOM 4305 CB ARG B 322 47.318 -29.869 26.036 1.00 63.56 C
ANISOU 4305 CB ARG B 322 9012 8145 6993 495 2093 1024 C
ATOM 4306 CG ARG B 322 47.796 -30.973 25.143 1.00 68.54 C
ANISOU 4306 CG ARG B 322 9833 8600 7611 490 2074 1070 C
ATOM 4307 CD ARG B 322 48.250 -32.025 26.134 1.00 67.65 C
ANISOU 4307 CD ARG B 322 9869 8405 7430 461 2101 1137 C
ATOM 4308 NE ARG B 322 48.850 -33.230 25.586 1.00 63.16 N
ANISOU 4308 NE ARG B 322 9510 7641 6847 474 2096 1181 N
ATOM 4309 CZ ARG B 322 49.121 -34.301 26.329 1.00 80.41 C
ANISOU 4309 CZ ARG B 322 11855 9724 8974 439 2132 1259 C
ATOM 4310 NH1 ARG B 322 48.840 -34.300 27.630 1.00 84.86 N
ANISOU 4310 NH1 ARG B 322 12399 10375 9468 380 2172 1306 N
ATOM 4311 NH2 ARG B 322 49.691 -35.365 25.783 1.00 86.39 N
ANISOU 4311 NH2 ARG B 322 12809 10284 9730 469 2133 1289 N
ATOM 4312 N VAL B 323 45.080 -27.781 26.992 1.00 59.64 N
ANISOU 4312 N VAL B 323 8043 8028 6588 403 2264 887 N
ATOM 4313 CA VAL B 323 44.810 -26.637 27.857 1.00 56.84 C
ANISOU 4313 CA VAL B 323 7526 7813 6259 449 2285 793 C
ATOM 4314 C VAL B 323 43.375 -26.665 28.375 1.00 68.65 C
ANISOU 4314 C VAL B 323 8836 9456 7793 301 2470 749 C
ATOM 4315 O VAL B 323 43.133 -26.383 29.551 1.00 69.77 O
ANISOU 4315 O VAL B 323 8927 9702 7878 263 2542 694 O
ATOM 4316 CB VAL B 323 45.120 -25.321 27.112 1.00 48.59 C
ANISOU 4316 CB VAL B 323 6375 6771 5314 613 2177 734 C
ATOM 4317 CG1 VAL B 323 44.981 -24.133 28.048 1.00 38.76 C
ANISOU 4317 CG1 VAL B 323 4992 5636 4099 666 2185 626 C
ATOM 4318 CG2 VAL B 323 46.509 -25.366 26.479 1.00 53.24 C
ANISOU 4318 CG2 VAL B 323 7129 7212 5889 737 2024 782 C
ATOM 4319 N PHE B 324 42.413 -27.034 27.523 1.00 78.73 N
ANISOU 4319 N PHE B 324 10000 10744 9172 209 2566 774 N
ATOM 4320 CA PHE B 324 40.994 -26.967 27.848 1.00 74.26 C
ANISOU 4320 CA PHE B 324 9173 10318 8725 74 2756 719 C
ATOM 4321 C PHE B 324 40.376 -28.328 28.131 1.00 82.73 C
ANISOU 4321 C PHE B 324 10305 11355 9774 -160 2908 806 C
ATOM 4322 O PHE B 324 39.166 -28.400 28.368 1.00 73.65 O
ANISOU 4322 O PHE B 324 8914 10306 8762 -306 3082 765 O
ATOM 4323 CB PHE B 324 40.199 -26.323 26.704 1.00 68.14 C
ANISOU 4323 CB PHE B 324 8135 9587 8170 129 2778 681 C
ATOM 4324 CG PHE B 324 40.517 -24.883 26.458 1.00 75.01 C
ANISOU 4324 CG PHE B 324 8891 10501 9106 354 2651 597 C
ATOM 4325 CD1 PHE B 324 41.772 -24.486 26.031 1.00 78.46 C
ANISOU 4325 CD1 PHE B 324 9542 10831 9439 513 2469 635 C
ATOM 4326 CD2 PHE B 324 39.537 -23.923 26.627 1.00 80.32 C
ANISOU 4326 CD2 PHE B 324 9226 11310 9984 401 2706 473 C
ATOM 4327 CE1 PHE B 324 42.044 -23.154 25.798 1.00 80.35 C
ANISOU 4327 CE1 PHE B 324 9686 11088 9755 696 2359 570 C
ATOM 4328 CE2 PHE B 324 39.801 -22.598 26.395 1.00 75.93 C
ANISOU 4328 CE2 PHE B 324 8580 10766 9506 607 2576 398 C
ATOM 4329 CZ PHE B 324 41.057 -22.211 25.981 1.00 76.34 C
ANISOU 4329 CZ PHE B 324 8873 10701 9433 745 2408 456 C
ATOM 4330 N GLY B 325 41.157 -29.405 28.114 1.00107.10 N
ANISOU 4330 N GLY B 325 13684 14287 12723 -201 2848 918 N
ATOM 4331 CA GLY B 325 40.647 -30.683 28.574 1.00129.81 C
ANISOU 4331 CA GLY B 325 16650 17103 15568 -420 2986 1008 C
ATOM 4332 C GLY B 325 39.572 -31.279 27.689 1.00131.69 C
ANISOU 4332 C GLY B 325 16756 17287 15994 -625 3121 1025 C
ATOM 4333 O GLY B 325 38.730 -32.043 28.174 1.00139.96 O
ANISOU 4333 O GLY B 325 17747 18329 17102 -851 3287 1057 O
ATOM 4334 N MET B 326 39.554 -30.923 26.410 1.00111.78 N
ANISOU 4334 N MET B 326 14173 14717 13582 -569 3065 1002 N
ATOM 4335 CA MET B 326 38.558 -31.414 25.469 1.00 98.40 C
ANISOU 4335 CA MET B 326 12325 12956 12108 -786 3130 980 C
ATOM 4336 C MET B 326 38.903 -32.783 24.884 1.00101.79 C
ANISOU 4336 C MET B 326 13069 13145 12463 -937 3058 1061 C
ATOM 4337 O MET B 326 39.999 -33.323 25.057 1.00 93.75 O
ANISOU 4337 O MET B 326 12397 11994 11231 -843 3043 1166 O
ATOM 4338 CB MET B 326 38.323 -30.404 24.356 1.00 90.18 C
ANISOU 4338 CB MET B 326 11064 11983 11216 -633 2836 857 C
ATOM 4339 CG MET B 326 37.885 -29.078 24.907 1.00 98.14 C
ANISOU 4339 CG MET B 326 11746 13199 12343 -488 2902 765 C
ATOM 4340 SD MET B 326 37.182 -27.985 23.674 1.00107.68 S
ANISOU 4340 SD MET B 326 12627 14478 13810 -363 2559 622 S
ATOM 4341 CE MET B 326 37.096 -26.465 24.621 1.00115.81 C
ANISOU 4341 CE MET B 326 13393 15702 14906 -138 2706 544 C
ATOM 4342 N PHE B 327 37.920 -33.322 24.155 1.00111.23 N
ANISOU 4342 N PHE B 327 14107 14284 13872 -1161 2948 978 N
ATOM 4343 CA PHE B 327 37.955 -34.554 23.364 1.00108.24 C
ANISOU 4343 CA PHE B 327 13960 13673 13494 -1337 2828 994 C
ATOM 4344 C PHE B 327 38.027 -35.831 24.190 1.00114.03 C
ANISOU 4344 C PHE B 327 14935 14240 14153 -1553 3079 1125 C
ATOM 4345 O PHE B 327 38.211 -36.916 23.621 1.00121.08 O
ANISOU 4345 O PHE B 327 16076 14900 15027 -1682 2999 1149 O
ATOM 4346 CB PHE B 327 39.141 -34.542 22.393 1.00 99.12 C
ANISOU 4346 CB PHE B 327 13124 12390 12148 -1119 2606 1012 C
ATOM 4347 CG PHE B 327 39.301 -33.244 21.655 1.00 97.64 C
ANISOU 4347 CG PHE B 327 12784 12342 11972 -880 2388 927 C
ATOM 4348 CD1 PHE B 327 38.205 -32.641 21.051 1.00 94.10 C
ANISOU 4348 CD1 PHE B 327 11993 12011 11748 -936 2204 796 C
ATOM 4349 CD2 PHE B 327 40.534 -32.608 21.587 1.00101.12 C
ANISOU 4349 CD2 PHE B 327 13413 12788 12219 -600 2364 982 C
ATOM 4350 CE1 PHE B 327 38.334 -31.434 20.380 1.00 96.40 C
ANISOU 4350 CE1 PHE B 327 12171 12408 12047 -711 1994 738 C
ATOM 4351 CE2 PHE B 327 40.673 -31.404 20.924 1.00 99.29 C
ANISOU 4351 CE2 PHE B 327 13059 12663 12003 -398 2183 920 C
ATOM 4352 CZ PHE B 327 39.569 -30.814 20.317 1.00 98.39 C
ANISOU 4352 CZ PHE B 327 12641 12652 12091 -449 1996 806 C
ATOM 4353 N ARG B 328 37.906 -35.742 25.516 1.00116.20 N
ANISOU 4353 N ARG B 328 15173 14610 14367 -1593 3382 1214 N
ATOM 4354 CA ARG B 328 37.931 -36.930 26.363 1.00128.60 C
ANISOU 4354 CA ARG B 328 16945 16055 15861 -1724 3445 1319 C
ATOM 4355 C ARG B 328 36.670 -37.789 26.285 1.00145.53 C
ANISOU 4355 C ARG B 328 18936 18107 18252 -2121 3601 1295 C
ATOM 4356 O ARG B 328 36.758 -38.987 26.570 1.00156.41 O
ANISOU 4356 O ARG B 328 20556 19287 19587 -2260 3629 1390 O
ATOM 4357 CB ARG B 328 38.266 -36.525 27.795 1.00135.83 C
ANISOU 4357 CB ARG B 328 17856 17144 16607 -1549 3472 1368 C
ATOM 4358 CG ARG B 328 39.691 -36.036 27.806 1.00144.75 C
ANISOU 4358 CG ARG B 328 19191 18281 17527 -1219 3266 1386 C
ATOM 4359 CD ARG B 328 40.094 -35.159 28.958 1.00150.04 C
ANISOU 4359 CD ARG B 328 19794 19153 18060 -1031 3238 1367 C
ATOM 4360 NE ARG B 328 41.461 -34.691 28.732 1.00150.63 N
ANISOU 4360 NE ARG B 328 20022 19200 18012 -757 3021 1353 N
ATOM 4361 CZ ARG B 328 42.000 -33.609 29.283 1.00152.75 C
ANISOU 4361 CZ ARG B 328 20212 19620 18207 -566 2934 1286 C
ATOM 4362 NH1 ARG B 328 43.255 -33.287 29.000 1.00149.22 N
ANISOU 4362 NH1 ARG B 328 19889 19111 17698 -353 2745 1270 N
ATOM 4363 NH2 ARG B 328 41.316 -32.892 30.164 1.00158.54 N
ANISOU 4363 NH2 ARG B 328 20749 20549 18938 -599 3046 1229 N
ATOM 4364 N GLN B 329 35.522 -37.242 25.888 1.00148.23 N
ANISOU 4364 N GLN B 329 18859 18578 18885 -2304 3673 1154 N
ATOM 4365 CA GLN B 329 34.323 -38.068 25.795 1.00143.21 C
ANISOU 4365 CA GLN B 329 18016 17860 18537 -2687 3759 1097 C
ATOM 4366 C GLN B 329 34.480 -39.126 24.710 1.00138.26 C
ANISOU 4366 C GLN B 329 17626 16957 17951 -2820 3507 1072 C
ATOM 4367 O GLN B 329 34.953 -38.842 23.606 1.00134.88 O
ANISOU 4367 O GLN B 329 17278 16498 17473 -2636 3172 986 O
ATOM 4368 CB GLN B 329 33.084 -37.217 25.509 1.00135.17 C
ANISOU 4368 CB GLN B 329 16422 17071 17866 -2750 3692 899 C
ATOM 4369 CG GLN B 329 31.803 -38.031 25.349 1.00128.56 C
ANISOU 4369 CG GLN B 329 15303 16158 17386 -3157 3755 812 C
ATOM 4370 CD GLN B 329 31.015 -38.143 26.637 1.00122.94 C
ANISOU 4370 CD GLN B 329 14389 15565 16759 -3306 4110 859 C
ATOM 4371 OE1 GLN B 329 30.793 -37.148 27.329 1.00123.52 O
ANISOU 4371 OE1 GLN B 329 14235 15888 16811 -3107 4196 822 O
ATOM 4372 NE2 GLN B 329 30.583 -39.356 26.966 1.00118.15 N
ANISOU 4372 NE2 GLN B 329 13898 14784 16209 -3580 4211 936 N
ATOM 4373 N ALA B 330 34.074 -40.358 25.029 1.00137.23 N
ANISOU 4373 N ALA B 330 17626 16611 17902 -3150 3683 1144 N
ATOM 4374 CA ALA B 330 34.278 -41.471 24.113 1.00137.16 C
ANISOU 4374 CA ALA B 330 17897 16299 17917 -3288 3477 1122 C
ATOM 4375 C ALA B 330 33.156 -41.599 23.094 1.00145.72 C
ANISOU 4375 C ALA B 330 18640 17382 19346 -3521 3225 904 C
ATOM 4376 O ALA B 330 33.259 -42.431 22.184 1.00145.25 O
ANISOU 4376 O ALA B 330 18792 17084 19313 -3631 3002 838 O
ATOM 4377 CB ALA B 330 34.421 -42.781 24.898 1.00127.75 C
ANISOU 4377 CB ALA B 330 17031 14855 16653 -3479 3699 1297 C
ATOM 4378 N SER B 331 32.088 -40.810 23.235 1.00147.57 N
ANISOU 4378 N SER B 331 18349 17869 19852 -3595 3248 780 N
ATOM 4379 CA SER B 331 30.996 -40.889 22.276 1.00142.21 C
ANISOU 4379 CA SER B 331 17306 17201 19528 -3804 2965 565 C
ATOM 4380 C SER B 331 31.448 -40.374 20.920 1.00136.57 C
ANISOU 4380 C SER B 331 16682 16499 18709 -3548 2492 439 C
ATOM 4381 O SER B 331 30.941 -40.818 19.883 1.00135.91 O
ANISOU 4381 O SER B 331 16547 16306 18787 -3706 2174 284 O
ATOM 4382 CB SER B 331 29.788 -40.096 22.771 1.00139.04 C
ANISOU 4382 CB SER B 331 16291 17073 19466 -3901 3097 457 C
ATOM 4383 OG SER B 331 29.953 -38.711 22.519 1.00137.31 O
ANISOU 4383 OG SER B 331 15863 17109 19200 -3549 2917 387 O
ATOM 4384 N ASP B 332 32.401 -39.441 20.916 1.00135.57 N
ANISOU 4384 N ASP B 332 16706 16500 18305 -3164 2444 503 N
ATOM 4385 CA ASP B 332 32.836 -38.765 19.705 1.00143.11 C
ANISOU 4385 CA ASP B 332 17736 17498 19140 -2902 2042 405 C
ATOM 4386 C ASP B 332 34.214 -39.259 19.291 1.00144.31 C
ANISOU 4386 C ASP B 332 18452 17444 18935 -2724 1996 498 C
ATOM 4387 O ASP B 332 34.830 -38.697 18.372 1.00145.03 O
ANISOU 4387 O ASP B 332 18692 17559 18852 -2475 1736 451 O
ATOM 4388 CB ASP B 332 32.866 -37.256 19.985 1.00148.45 C
ANISOU 4388 CB ASP B 332 18133 18465 19808 -2604 2036 399 C
ATOM 4389 CG ASP B 332 32.858 -36.405 18.732 1.00154.95 C
ANISOU 4389 CG ASP B 332 18886 19369 20618 -2394 1604 276 C
ATOM 4390 OD1 ASP B 332 33.328 -36.865 17.673 1.00157.59 O
ANISOU 4390 OD1 ASP B 332 19544 19541 20794 -2372 1343 238 O
ATOM 4391 OD2 ASP B 332 32.398 -35.245 18.822 1.00155.89 O
ANISOU 4391 OD2 ASP B 332 18647 19708 20875 -2239 1536 222 O
ATOM 4392 N ARG B 333 34.652 -40.374 19.884 1.00144.59 N
ANISOU 4392 N ARG B 333 18804 17254 18880 -2866 2238 623 N
ATOM 4393 CA ARG B 333 36.026 -40.830 19.725 1.00145.35 C
ANISOU 4393 CA ARG B 333 19406 17157 18664 -2666 2256 729 C
ATOM 4394 C ARG B 333 36.408 -40.904 18.257 1.00144.98 C
ANISOU 4394 C ARG B 333 19569 17004 18514 -2563 1903 591 C
ATOM 4395 O ARG B 333 37.387 -40.285 17.816 1.00143.42 O
ANISOU 4395 O ARG B 333 19556 16852 18085 -2253 1814 610 O
ATOM 4396 CB ARG B 333 36.188 -42.201 20.388 1.00148.27 C
ANISOU 4396 CB ARG B 333 20067 17244 19025 -2892 2499 855 C
ATOM 4397 CG ARG B 333 37.605 -42.757 20.373 1.00149.46 C
ANISOU 4397 CG ARG B 333 20722 17174 18894 -2678 2541 975 C
ATOM 4398 CD ARG B 333 37.655 -44.148 20.987 1.00155.52 C
ANISOU 4398 CD ARG B 333 21778 17629 19685 -2912 2750 1101 C
ATOM 4399 NE ARG B 333 38.999 -44.720 20.942 1.00156.39 N
ANISOU 4399 NE ARG B 333 22353 17504 19563 -2689 2766 1205 N
ATOM 4400 CZ ARG B 333 39.772 -44.918 22.005 1.00155.11 C
ANISOU 4400 CZ ARG B 333 22398 17290 19247 -2552 2979 1414 C
ATOM 4401 NH1 ARG B 333 39.340 -44.589 23.214 1.00153.25 N
ANISOU 4401 NH1 ARG B 333 21914 17282 19033 -2556 3124 1507 N
ATOM 4402 NH2 ARG B 333 40.979 -45.447 21.857 1.00155.77 N
ANISOU 4402 NH2 ARG B 333 22798 17210 19177 -2281 2887 1448 N
ATOM 4403 N GLU B 334 35.554 -41.555 17.466 1.00148.41 N
ANISOU 4403 N GLU B 334 19940 17318 19129 -2830 1690 434 N
ATOM 4404 CA GLU B 334 35.846 -41.764 16.057 1.00142.69 C
ANISOU 4404 CA GLU B 334 19466 16470 18280 -2770 1355 285 C
ATOM 4405 C GLU B 334 36.150 -40.446 15.366 1.00141.64 C
ANISOU 4405 C GLU B 334 19250 16563 18003 -2462 1133 240 C
ATOM 4406 O GLU B 334 37.267 -40.236 14.872 1.00144.83 O
ANISOU 4406 O GLU B 334 19983 16917 18127 -2202 1105 273 O
ATOM 4407 CB GLU B 334 34.642 -42.476 15.426 1.00152.83 C
ANISOU 4407 CB GLU B 334 20590 17648 19830 -3129 1128 102 C
ATOM 4408 CG GLU B 334 34.502 -42.475 13.914 1.00157.50 C
ANISOU 4408 CG GLU B 334 21314 18186 20342 -3116 698 -103 C
ATOM 4409 CD GLU B 334 33.145 -43.046 13.484 1.00159.81 C
ANISOU 4409 CD GLU B 334 21337 18421 20963 -3491 460 -291 C
ATOM 4410 OE1 GLU B 334 32.148 -42.833 14.213 1.00157.50 O
ANISOU 4410 OE1 GLU B 334 20576 18270 20995 -3677 562 -283 O
ATOM 4411 OE2 GLU B 334 33.073 -43.721 12.433 1.00159.38 O
ANISOU 4411 OE2 GLU B 334 21531 18176 20850 -3606 179 -458 O
ATOM 4412 N ALA B 335 35.248 -39.474 15.506 1.00138.65 N
ANISOU 4412 N ALA B 335 18418 16441 17821 -2462 1034 194 N
ATOM 4413 CA ALA B 335 35.455 -38.209 14.814 1.00127.33 C
ANISOU 4413 CA ALA B 335 16911 15197 16271 -2179 799 159 C
ATOM 4414 C ALA B 335 36.731 -37.538 15.289 1.00126.27 C
ANISOU 4414 C ALA B 335 16972 15123 15880 -1853 1011 314 C
ATOM 4415 O ALA B 335 37.558 -37.102 14.473 1.00121.43 O
ANISOU 4415 O ALA B 335 16617 14495 15027 -1625 877 309 O
ATOM 4416 CB ALA B 335 34.250 -37.291 15.017 1.00115.06 C
ANISOU 4416 CB ALA B 335 14811 13889 15016 -2221 677 90 C
ATOM 4417 N VAL B 336 36.977 -37.577 16.600 1.00128.34 N
ANISOU 4417 N VAL B 336 17162 15427 16174 -1847 1355 451 N
ATOM 4418 CA VAL B 336 38.172 -36.936 17.129 1.00119.46 C
ANISOU 4418 CA VAL B 336 16193 14363 14831 -1549 1536 586 C
ATOM 4419 C VAL B 336 39.419 -37.561 16.531 1.00124.38 C
ANISOU 4419 C VAL B 336 17291 14771 15196 -1421 1531 617 C
ATOM 4420 O VAL B 336 40.297 -36.851 16.021 1.00120.12 O
ANISOU 4420 O VAL B 336 16893 14276 14473 -1160 1469 631 O
ATOM 4421 CB VAL B 336 38.185 -37.022 18.666 1.00104.35 C
ANISOU 4421 CB VAL B 336 14167 12511 12971 -1592 1887 721 C
ATOM 4422 CG1 VAL B 336 39.545 -36.612 19.213 1.00 90.65 C
ANISOU 4422 CG1 VAL B 336 12658 10787 10997 -1305 2048 855 C
ATOM 4423 CG2 VAL B 336 37.080 -36.164 19.248 1.00109.32 C
ANISOU 4423 CG2 VAL B 336 14313 13385 13837 -1653 1928 675 C
ATOM 4424 N TYR B 337 39.477 -38.896 16.473 1.00134.18 N
ANISOU 4424 N TYR B 337 18783 15763 16438 -1611 1587 609 N
ATOM 4425 CA TYR B 337 40.708 -39.466 15.943 1.00134.70 C
ANISOU 4425 CA TYR B 337 19285 15618 16278 -1459 1608 626 C
ATOM 4426 C TYR B 337 40.904 -39.096 14.487 1.00127.79 C
ANISOU 4426 C TYR B 337 18557 14737 15259 -1351 1338 490 C
ATOM 4427 O TYR B 337 41.994 -38.614 14.127 1.00130.33 O
ANISOU 4427 O TYR B 337 19072 15065 15381 -1089 1372 524 O
ATOM 4428 CB TYR B 337 40.744 -40.986 16.121 1.00147.25 C
ANISOU 4428 CB TYR B 337 21137 16904 17905 -1669 1711 636 C
ATOM 4429 CG TYR B 337 41.249 -41.456 17.477 1.00160.56 C
ANISOU 4429 CG TYR B 337 22900 18515 19590 -1653 2014 827 C
ATOM 4430 CD1 TYR B 337 42.589 -41.803 17.652 1.00161.97 C
ANISOU 4430 CD1 TYR B 337 23402 18541 19599 -1427 2132 921 C
ATOM 4431 CD2 TYR B 337 40.402 -41.562 18.574 1.00165.77 C
ANISOU 4431 CD2 TYR B 337 23318 19252 20414 -1859 2181 912 C
ATOM 4432 CE1 TYR B 337 43.070 -42.239 18.877 1.00162.02 C
ANISOU 4432 CE1 TYR B 337 23503 18469 19587 -1395 2362 1103 C
ATOM 4433 CE2 TYR B 337 40.878 -41.998 19.808 1.00165.93 C
ANISOU 4433 CE2 TYR B 337 23465 19198 20385 -1843 2447 1100 C
ATOM 4434 CZ TYR B 337 42.212 -42.335 19.950 1.00163.75 C
ANISOU 4434 CZ TYR B 337 23526 18765 19926 -1605 2513 1199 C
ATOM 4435 OH TYR B 337 42.688 -42.768 21.167 1.00163.78 O
ANISOU 4435 OH TYR B 337 23659 18698 19872 -1566 2718 1386 O
ATOM 4436 N ALA B 338 39.807 -38.975 13.737 1.00113.60 N
ANISOU 4436 N ALA B 338 16594 12998 13572 -1519 1065 350 N
ATOM 4437 CA ALA B 338 39.969 -38.583 12.347 1.00106.01 C
ANISOU 4437 CA ALA B 338 15812 12037 12429 -1414 789 231 C
ATOM 4438 C ALA B 338 40.566 -37.199 12.299 1.00104.45 C
ANISOU 4438 C ALA B 338 15538 12041 12106 -1115 798 313 C
ATOM 4439 O ALA B 338 41.597 -36.975 11.647 1.00107.67 O
ANISOU 4439 O ALA B 338 16243 12394 12273 -914 818 322 O
ATOM 4440 CB ALA B 338 38.628 -38.633 11.619 1.00105.10 C
ANISOU 4440 CB ALA B 338 15504 11963 12466 -1639 448 71 C
ATOM 4441 N ALA B 339 40.028 -36.292 13.105 1.00 98.79 N
ANISOU 4441 N ALA B 339 14431 11542 11561 -1081 838 379 N
ATOM 4442 CA ALA B 339 40.498 -34.927 13.018 1.00 83.30 C
ANISOU 4442 CA ALA B 339 12386 9754 9509 -813 818 443 C
ATOM 4443 C ALA B 339 41.983 -34.885 13.350 1.00 87.63 C
ANISOU 4443 C ALA B 339 13191 10236 9869 -595 1075 553 C
ATOM 4444 O ALA B 339 42.805 -34.445 12.530 1.00 86.25 O
ANISOU 4444 O ALA B 339 13246 10035 9491 -414 1033 551 O
ATOM 4445 CB ALA B 339 39.696 -34.031 13.960 1.00 56.59 C
ANISOU 4445 CB ALA B 339 8544 6595 6365 -811 857 482 C
ATOM 4446 N PHE B 340 42.363 -35.467 14.498 1.00 87.93 N
ANISOU 4446 N PHE B 340 13223 10220 9966 -624 1340 644 N
ATOM 4447 CA PHE B 340 43.778 -35.454 14.852 1.00 84.27 C
ANISOU 4447 CA PHE B 340 12972 9690 9357 -408 1552 741 C
ATOM 4448 C PHE B 340 44.624 -36.118 13.783 1.00 83.14 C
ANISOU 4448 C PHE B 340 13222 9342 9025 -348 1527 678 C
ATOM 4449 O PHE B 340 45.638 -35.552 13.348 1.00 77.51 O
ANISOU 4449 O PHE B 340 12646 8636 8168 -131 1579 700 O
ATOM 4450 CB PHE B 340 43.986 -36.134 16.203 1.00 82.98 C
ANISOU 4450 CB PHE B 340 12787 9472 9270 -464 1793 849 C
ATOM 4451 CG PHE B 340 43.709 -35.241 17.372 1.00 81.92 C
ANISOU 4451 CG PHE B 340 12340 9554 9233 -411 1904 931 C
ATOM 4452 CD1 PHE B 340 42.418 -35.065 17.837 1.00 93.94 C
ANISOU 4452 CD1 PHE B 340 13550 11206 10938 -597 1880 900 C
ATOM 4453 CD2 PHE B 340 44.740 -34.576 18.010 1.00 76.74 C
ANISOU 4453 CD2 PHE B 340 11693 8968 8497 -179 2038 1022 C
ATOM 4454 CE1 PHE B 340 42.160 -34.236 18.919 1.00 95.93 C
ANISOU 4454 CE1 PHE B 340 13527 11655 11269 -542 2010 955 C
ATOM 4455 CE2 PHE B 340 44.491 -33.750 19.090 1.00 82.63 C
ANISOU 4455 CE2 PHE B 340 12178 9906 9312 -131 2136 1075 C
ATOM 4456 CZ PHE B 340 43.200 -33.579 19.546 1.00 87.52 C
ANISOU 4456 CZ PHE B 340 12509 10653 10090 -307 2134 1040 C
ATOM 4457 N THR B 341 44.152 -37.243 13.243 1.00 82.44 N
ANISOU 4457 N THR B 341 13309 9072 8941 -548 1438 580 N
ATOM 4458 CA THR B 341 44.946 -37.926 12.236 1.00 73.45 C
ANISOU 4458 CA THR B 341 12566 7725 7618 -490 1436 496 C
ATOM 4459 C THR B 341 45.098 -37.038 11.018 1.00 63.90 C
ANISOU 4459 C THR B 341 11453 6604 6223 -367 1272 427 C
ATOM 4460 O THR B 341 46.218 -36.759 10.566 1.00 64.69 O
ANISOU 4460 O THR B 341 11760 6663 6155 -165 1392 441 O
ATOM 4461 CB THR B 341 44.305 -39.255 11.857 1.00 69.95 C
ANISOU 4461 CB THR B 341 12293 7063 7222 -746 1345 379 C
ATOM 4462 OG1 THR B 341 44.443 -40.169 12.949 1.00 91.40 O
ANISOU 4462 OG1 THR B 341 15016 9640 10073 -829 1545 471 O
ATOM 4463 CG2 THR B 341 44.982 -39.827 10.629 1.00 60.71 C
ANISOU 4463 CG2 THR B 341 11535 5694 5837 -686 1307 247 C
ATOM 4464 N PHE B 342 43.989 -36.447 10.580 1.00 49.00 N
ANISOU 4464 N PHE B 342 9380 4858 4382 -472 1008 372 N
ATOM 4465 CA PHE B 342 44.078 -35.553 9.446 1.00 49.19 C
ANISOU 4465 CA PHE B 342 9518 4962 4211 -353 827 332 C
ATOM 4466 C PHE B 342 44.982 -34.379 9.772 1.00 63.67 C
ANISOU 4466 C PHE B 342 11272 6923 5996 -98 991 462 C
ATOM 4467 O PHE B 342 45.852 -34.013 8.966 1.00 49.45 O
ANISOU 4467 O PHE B 342 9727 5083 3979 54 1044 462 O
ATOM 4468 CB PHE B 342 42.674 -35.078 9.083 1.00 55.09 C
ANISOU 4468 CB PHE B 342 10025 5843 5065 -492 486 269 C
ATOM 4469 CG PHE B 342 42.640 -34.086 7.973 1.00 66.70 C
ANISOU 4469 CG PHE B 342 11607 7397 6337 -368 256 254 C
ATOM 4470 CD1 PHE B 342 42.748 -34.502 6.660 1.00 84.43 C
ANISOU 4470 CD1 PHE B 342 14246 9521 8314 -401 87 140 C
ATOM 4471 CD2 PHE B 342 42.525 -32.733 8.238 1.00 68.00 C
ANISOU 4471 CD2 PHE B 342 11520 7747 6568 -214 213 358 C
ATOM 4472 CE1 PHE B 342 42.715 -33.594 5.631 1.00 93.22 C
ANISOU 4472 CE1 PHE B 342 15510 10703 9206 -290 -128 146 C
ATOM 4473 CE2 PHE B 342 42.502 -31.815 7.211 1.00 75.69 C
ANISOU 4473 CE2 PHE B 342 12632 8774 7353 -98 -4 369 C
ATOM 4474 CZ PHE B 342 42.596 -32.247 5.905 1.00 91.23 C
ANISOU 4474 CZ PHE B 342 15006 10625 9030 -138 -175 273 C
ATOM 4475 N SER B 343 44.891 -33.867 11.004 1.00 75.87 N
ANISOU 4475 N SER B 343 12489 8601 7737 -55 1113 567 N
ATOM 4476 CA SER B 343 45.710 -32.711 11.340 1.00 76.15 C
ANISOU 4476 CA SER B 343 12434 8752 7749 172 1246 673 C
ATOM 4477 C SER B 343 47.186 -33.078 11.315 1.00 80.37 C
ANISOU 4477 C SER B 343 13222 9154 8161 324 1500 706 C
ATOM 4478 O SER B 343 48.010 -32.322 10.774 1.00 69.41 O
ANISOU 4478 O SER B 343 11940 7783 6649 491 1564 735 O
ATOM 4479 CB SER B 343 45.300 -32.152 12.700 1.00 71.66 C
ANISOU 4479 CB SER B 343 11484 8342 7400 180 1325 754 C
ATOM 4480 OG SER B 343 45.606 -30.769 12.783 1.00 79.48 O
ANISOU 4480 OG SER B 343 12331 9474 8396 361 1327 817 O
ATOM 4481 N HIS B 344 47.524 -34.290 11.780 1.00 86.76 N
ANISOU 4481 N HIS B 344 14150 9807 9009 261 1639 693 N
ATOM 4482 CA HIS B 344 48.918 -34.715 11.720 1.00 84.13 C
ANISOU 4482 CA HIS B 344 14032 9332 8603 419 1859 703 C
ATOM 4483 C HIS B 344 49.393 -34.711 10.278 1.00 92.63 C
ANISOU 4483 C HIS B 344 15390 10318 9487 473 1820 596 C
ATOM 4484 O HIS B 344 50.436 -34.128 9.950 1.00111.80 O
ANISOU 4484 O HIS B 344 17721 12760 11996 637 1866 566 O
ATOM 4485 CB HIS B 344 49.101 -36.087 12.365 1.00 83.45 C
ANISOU 4485 CB HIS B 344 14059 9057 8593 343 1977 706 C
ATOM 4486 CG HIS B 344 48.820 -36.105 13.835 1.00 84.13 C
ANISOU 4486 CG HIS B 344 13867 9227 8870 308 2026 808 C
ATOM 4487 ND1 HIS B 344 47.794 -36.835 14.394 1.00 85.49 N
ANISOU 4487 ND1 HIS B 344 13988 9361 9133 85 1990 825 N
ATOM 4488 CD2 HIS B 344 49.450 -35.493 14.865 1.00 84.96 C
ANISOU 4488 CD2 HIS B 344 13656 9470 9156 456 2041 841 C
ATOM 4489 CE1 HIS B 344 47.799 -36.666 15.704 1.00 88.34 C
ANISOU 4489 CE1 HIS B 344 14159 9810 9598 103 2098 943 C
ATOM 4490 NE2 HIS B 344 48.795 -35.857 16.017 1.00 83.34 N
ANISOU 4490 NE2 HIS B 344 13327 9301 9039 336 2077 921 N
ATOM 4491 N TRP B 345 48.576 -35.259 9.383 1.00 84.04 N
ANISOU 4491 N TRP B 345 14522 9155 8255 311 1651 495 N
ATOM 4492 CA TRP B 345 48.996 -35.344 7.997 1.00 87.10 C
ANISOU 4492 CA TRP B 345 15268 9446 8382 350 1635 392 C
ATOM 4493 C TRP B 345 49.265 -33.959 7.435 1.00 88.83 C
ANISOU 4493 C TRP B 345 15400 9815 8535 482 1582 443 C
ATOM 4494 O TRP B 345 50.242 -33.761 6.696 1.00 94.94 O
ANISOU 4494 O TRP B 345 16230 10528 9313 593 1663 393 O
ATOM 4495 CB TRP B 345 47.910 -36.062 7.197 1.00 93.81 C
ANISOU 4495 CB TRP B 345 16284 10217 9141 134 1366 249 C
ATOM 4496 CG TRP B 345 48.113 -36.088 5.723 1.00 90.28 C
ANISOU 4496 CG TRP B 345 16231 9694 8378 148 1289 130 C
ATOM 4497 CD1 TRP B 345 48.879 -36.951 4.996 1.00 89.65 C
ANISOU 4497 CD1 TRP B 345 16534 9410 8117 179 1448 5 C
ATOM 4498 CD2 TRP B 345 47.466 -35.231 4.783 1.00 97.26 C
ANISOU 4498 CD2 TRP B 345 17185 10697 9074 127 1019 117 C
ATOM 4499 NE1 TRP B 345 48.777 -36.655 3.656 1.00 99.84 N
ANISOU 4499 NE1 TRP B 345 18148 10699 9086 173 1316 -86 N
ATOM 4500 CE2 TRP B 345 47.910 -35.603 3.501 1.00108.10 C
ANISOU 4500 CE2 TRP B 345 19019 11940 10116 141 1035 -9 C
ATOM 4501 CE3 TRP B 345 46.559 -34.174 4.906 1.00100.66 C
ANISOU 4501 CE3 TRP B 345 17339 11323 9584 110 761 199 C
ATOM 4502 CZ2 TRP B 345 47.475 -34.954 2.346 1.00118.82 C
ANISOU 4502 CZ2 TRP B 345 20597 13362 11187 130 787 -37 C
ATOM 4503 CZ3 TRP B 345 46.132 -33.532 3.767 1.00107.64 C
ANISOU 4503 CZ3 TRP B 345 18417 12259 10222 114 500 174 C
ATOM 4504 CH2 TRP B 345 46.588 -33.922 2.501 1.00114.75 C
ANISOU 4504 CH2 TRP B 345 19807 13032 10761 120 507 65 C
ATOM 4505 N LEU B 346 48.480 -32.962 7.858 1.00 77.83 N
ANISOU 4505 N LEU B 346 13774 8608 7191 472 1440 542 N
ATOM 4506 CA LEU B 346 48.661 -31.644 7.268 1.00 69.85 C
ANISOU 4506 CA LEU B 346 12682 7710 6146 584 1355 587 C
ATOM 4507 C LEU B 346 50.054 -31.104 7.546 1.00 58.23 C
ANISOU 4507 C LEU B 346 10968 6238 4920 743 1544 595 C
ATOM 4508 O LEU B 346 50.677 -30.511 6.654 1.00 68.12 O
ANISOU 4508 O LEU B 346 12291 7469 6122 811 1557 578 O
ATOM 4509 CB LEU B 346 47.607 -30.673 7.794 1.00 74.33 C
ANISOU 4509 CB LEU B 346 12985 8456 6799 567 1165 681 C
ATOM 4510 CG LEU B 346 46.309 -30.662 6.993 1.00 60.88 C
ANISOU 4510 CG LEU B 346 11316 6787 5030 431 790 608 C
ATOM 4511 CD1 LEU B 346 45.446 -29.491 7.414 1.00 60.66 C
ANISOU 4511 CD1 LEU B 346 10932 6933 5183 467 592 682 C
ATOM 4512 CD2 LEU B 346 46.621 -30.627 5.517 1.00 47.59 C
ANISOU 4512 CD2 LEU B 346 10066 5015 3000 456 705 561 C
ATOM 4513 N VAL B 347 50.616 -31.404 8.723 1.00 54.40 N
ANISOU 4513 N VAL B 347 10240 5750 4680 791 1683 614 N
ATOM 4514 CA VAL B 347 51.966 -30.920 9.007 1.00 64.09 C
ANISOU 4514 CA VAL B 347 11271 6959 6121 931 1813 614 C
ATOM 4515 C VAL B 347 52.924 -31.449 7.952 1.00 78.70 C
ANISOU 4515 C VAL B 347 13371 8641 7891 972 1927 540 C
ATOM 4516 O VAL B 347 53.656 -30.692 7.298 1.00 72.05 O
ANISOU 4516 O VAL B 347 12521 7794 7062 1039 1972 544 O
ATOM 4517 CB VAL B 347 52.408 -31.332 10.425 1.00 54.16 C
ANISOU 4517 CB VAL B 347 9781 5702 5094 975 1897 639 C
ATOM 4518 CG1 VAL B 347 53.911 -31.106 10.602 1.00 46.23 C
ANISOU 4518 CG1 VAL B 347 8669 4627 4270 1116 2015 633 C
ATOM 4519 CG2 VAL B 347 51.599 -30.592 11.492 1.00 55.68 C
ANISOU 4519 CG2 VAL B 347 9697 6076 5383 948 1811 714 C
ATOM 4520 N TYR B 348 52.882 -32.760 7.729 1.00 88.03 N
ANISOU 4520 N TYR B 348 14805 9667 8974 919 1988 473 N
ATOM 4521 CA TYR B 348 53.776 -33.349 6.750 1.00 75.43 C
ANISOU 4521 CA TYR B 348 13462 7897 7301 960 2120 400 C
ATOM 4522 C TYR B 348 53.412 -32.876 5.356 1.00 73.00 C
ANISOU 4522 C TYR B 348 13390 7605 6740 907 2029 362 C
ATOM 4523 O TYR B 348 54.298 -32.692 4.510 1.00 82.03 O
ANISOU 4523 O TYR B 348 14635 8678 7854 963 2143 341 O
ATOM 4524 CB TYR B 348 53.701 -34.869 6.864 1.00 73.87 C
ANISOU 4524 CB TYR B 348 13513 7513 7042 909 2200 331 C
ATOM 4525 CG TYR B 348 54.074 -35.383 8.243 1.00 78.89 C
ANISOU 4525 CG TYR B 348 13957 8113 7905 970 2290 386 C
ATOM 4526 CD1 TYR B 348 55.359 -35.209 8.751 1.00 86.69 C
ANISOU 4526 CD1 TYR B 348 14760 9065 9115 1125 2418 437 C
ATOM 4527 CD2 TYR B 348 53.128 -35.996 9.060 1.00 77.02 C
ANISOU 4527 CD2 TYR B 348 13733 7883 7650 862 2237 403 C
ATOM 4528 CE1 TYR B 348 55.705 -35.671 10.021 1.00 85.35 C
ANISOU 4528 CE1 TYR B 348 14447 8859 9122 1195 2473 495 C
ATOM 4529 CE2 TYR B 348 53.463 -36.458 10.330 1.00 81.37 C
ANISOU 4529 CE2 TYR B 348 14128 8402 8388 918 2315 464 C
ATOM 4530 CZ TYR B 348 54.751 -36.293 10.805 1.00 83.86 C
ANISOU 4530 CZ TYR B 348 14284 8678 8900 1099 2422 500 C
ATOM 4531 OH TYR B 348 55.082 -36.753 12.061 1.00 84.86 O
ANISOU 4531 OH TYR B 348 14293 8774 9176 1169 2476 558 O
ATOM 4532 N ALA B 349 52.125 -32.597 5.122 1.00 66.47 N
ANISOU 4532 N ALA B 349 12649 6879 5727 801 1815 369 N
ATOM 4533 CA ALA B 349 51.739 -32.103 3.811 1.00 65.53 C
ANISOU 4533 CA ALA B 349 12776 6776 5345 761 1682 345 C
ATOM 4534 C ALA B 349 52.449 -30.795 3.523 1.00 65.43 C
ANISOU 4534 C ALA B 349 12595 6841 5425 862 1739 422 C
ATOM 4535 O ALA B 349 52.803 -30.509 2.369 1.00 66.76 O
ANISOU 4535 O ALA B 349 12976 6960 5430 868 1763 401 O
ATOM 4536 CB ALA B 349 50.220 -31.933 3.740 1.00 64.59 C
ANISOU 4536 CB ALA B 349 12753 6761 5027 644 1390 362 C
ATOM 4537 N ASN B 350 52.738 -30.030 4.576 1.00 68.12 N
ANISOU 4537 N ASN B 350 12572 7285 6025 934 1781 503 N
ATOM 4538 CA ASN B 350 53.384 -28.745 4.377 1.00 69.29 C
ANISOU 4538 CA ASN B 350 12573 7490 6265 1012 1830 568 C
ATOM 4539 C ASN B 350 54.753 -28.934 3.746 1.00 88.87 C
ANISOU 4539 C ASN B 350 15146 9836 8783 1068 2054 531 C
ATOM 4540 O ASN B 350 55.152 -28.159 2.868 1.00101.07 O
ANISOU 4540 O ASN B 350 16791 11372 10239 1082 2099 556 O
ATOM 4541 CB ASN B 350 53.488 -28.020 5.718 1.00 54.10 C
ANISOU 4541 CB ASN B 350 10260 5679 4616 1071 1833 637 C
ATOM 4542 CG ASN B 350 54.046 -26.620 5.589 1.00 67.31 C
ANISOU 4542 CG ASN B 350 11794 7400 6379 1137 1867 700 C
ATOM 4543 OD1 ASN B 350 53.356 -25.684 5.164 1.00 74.28 O
ANISOU 4543 OD1 ASN B 350 12718 8359 7147 1124 1735 761 O
ATOM 4544 ND2 ASN B 350 55.311 -26.465 5.968 1.00 78.06 N
ANISOU 4544 ND2 ASN B 350 13010 8702 7948 1209 2037 696 N
ATOM 4545 N SER B 351 55.468 -29.995 4.146 1.00 88.83 N
ANISOU 4545 N SER B 351 15140 9716 8896 1098 2204 481 N
ATOM 4546 CA SER B 351 56.784 -30.219 3.566 1.00 82.92 C
ANISOU 4546 CA SER B 351 14476 8838 8191 1154 2427 459 C
ATOM 4547 C SER B 351 56.679 -30.533 2.084 1.00 92.45 C
ANISOU 4547 C SER B 351 16064 9963 9101 1096 2457 395 C
ATOM 4548 O SER B 351 57.587 -30.195 1.315 1.00107.72 O
ANISOU 4548 O SER B 351 18081 11839 11007 1125 2624 398 O
ATOM 4549 CB SER B 351 57.505 -31.345 4.308 1.00 87.15 C
ANISOU 4549 CB SER B 351 14951 9260 8900 1205 2562 437 C
ATOM 4550 OG SER B 351 57.759 -30.993 5.658 1.00 97.30 O
ANISOU 4550 OG SER B 351 15903 10618 10448 1267 2536 505 O
ATOM 4551 N ALA B 352 55.576 -31.161 1.660 1.00 85.16 N
ANISOU 4551 N ALA B 352 15386 9032 7940 1006 2293 336 N
ATOM 4552 CA ALA B 352 55.369 -31.377 0.234 1.00 86.72 C
ANISOU 4552 CA ALA B 352 15970 9162 7819 945 2272 272 C
ATOM 4553 C ALA B 352 54.900 -30.098 -0.437 1.00 89.09 C
ANISOU 4553 C ALA B 352 16316 9571 7963 928 2130 344 C
ATOM 4554 O ALA B 352 55.116 -29.911 -1.642 1.00 83.59 O
ANISOU 4554 O ALA B 352 15897 8825 7038 907 2171 326 O
ATOM 4555 CB ALA B 352 54.368 -32.509 0.003 1.00 82.35 C
ANISOU 4555 CB ALA B 352 15689 8547 7053 842 2114 170 C
ATOM 4556 N ALA B 353 54.209 -29.241 0.320 1.00 84.08 N
ANISOU 4556 N ALA B 353 15435 9080 7432 935 1960 431 N
ATOM 4557 CA ALA B 353 53.604 -28.060 -0.276 1.00 69.61 C
ANISOU 4557 CA ALA B 353 13665 7342 5441 922 1787 514 C
ATOM 4558 C ALA B 353 54.655 -27.020 -0.635 1.00 61.88 C
ANISOU 4558 C ALA B 353 12620 6350 4544 985 1978 581 C
ATOM 4559 O ALA B 353 54.529 -26.323 -1.648 1.00 66.59 O
ANISOU 4559 O ALA B 353 13433 6945 4924 967 1928 627 O
ATOM 4560 CB ALA B 353 52.574 -27.468 0.686 1.00 62.45 C
ANISOU 4560 CB ALA B 353 12508 6582 4636 921 1564 592 C
ATOM 4561 N ASN B 354 55.678 -26.877 0.204 1.00 62.58 N
ANISOU 4561 N ASN B 354 12419 6424 4936 1054 2182 593 N
ATOM 4562 CA ASN B 354 56.637 -25.791 0.009 1.00 80.53 C
ANISOU 4562 CA ASN B 354 14599 8687 7311 1101 2348 660 C
ATOM 4563 C ASN B 354 57.371 -25.840 -1.321 1.00 86.43 C
ANISOU 4563 C ASN B 354 15657 9325 7856 1081 2533 638 C
ATOM 4564 O ASN B 354 57.401 -24.813 -2.021 1.00 81.98 O
ANISOU 4564 O ASN B 354 15208 8775 7165 1070 2536 712 O
ATOM 4565 CB ASN B 354 57.617 -25.743 1.186 1.00 90.78 C
ANISOU 4565 CB ASN B 354 15546 9978 8968 1173 2503 666 C
ATOM 4566 CG ASN B 354 56.957 -25.264 2.466 1.00 94.88 C
ANISOU 4566 CG ASN B 354 15753 10622 9675 1197 2336 711 C
ATOM 4567 OD1 ASN B 354 56.053 -24.420 2.441 1.00 86.84 O
ANISOU 4567 OD1 ASN B 354 14722 9701 8573 1179 2160 772 O
ATOM 4568 ND2 ASN B 354 57.417 -25.788 3.596 1.00102.72 N
ANISOU 4568 ND2 ASN B 354 16504 11608 10915 1242 2389 689 N
ATOM 4569 N PRO B 355 57.989 -26.957 -1.730 1.00 92.15 N
ANISOU 4569 N PRO B 355 16541 9935 8538 1076 2705 546 N
ATOM 4570 CA PRO B 355 58.668 -26.960 -3.041 1.00 79.76 C
ANISOU 4570 CA PRO B 355 15284 8270 6753 1052 2902 523 C
ATOM 4571 C PRO B 355 57.751 -26.634 -4.204 1.00 83.93 C
ANISOU 4571 C PRO B 355 16175 8818 6898 986 2723 540 C
ATOM 4572 O PRO B 355 58.133 -25.863 -5.096 1.00 95.65 O
ANISOU 4572 O PRO B 355 17838 10278 8225 973 2826 596 O
ATOM 4573 CB PRO B 355 59.226 -28.390 -3.142 1.00 75.67 C
ANISOU 4573 CB PRO B 355 14869 7634 6248 1058 3068 409 C
ATOM 4574 CG PRO B 355 59.350 -28.843 -1.716 1.00 84.88 C
ANISOU 4574 CG PRO B 355 15686 8823 7742 1111 3040 410 C
ATOM 4575 CD PRO B 355 58.144 -28.243 -1.027 1.00 89.64 C
ANISOU 4575 CD PRO B 355 16139 9561 8360 1093 2747 466 C
ATOM 4576 N ILE B 356 56.505 -27.109 -4.160 1.00 88.29 N
ANISOU 4576 N ILE B 356 16832 9418 7298 941 2433 509 N
ATOM 4577 CA ILE B 356 55.568 -26.809 -5.236 1.00 91.42 C
ANISOU 4577 CA ILE B 356 17577 9836 7325 881 2202 531 C
ATOM 4578 C ILE B 356 55.357 -25.309 -5.328 1.00102.58 C
ANISOU 4578 C ILE B 356 18917 11329 8728 902 2107 679 C
ATOM 4579 O ILE B 356 55.394 -24.725 -6.420 1.00111.85 O
ANISOU 4579 O ILE B 356 20383 12474 9642 879 2108 734 O
ATOM 4580 CB ILE B 356 54.234 -27.543 -5.003 1.00 81.98 C
ANISOU 4580 CB ILE B 356 16453 8683 6011 826 1872 473 C
ATOM 4581 CG1 ILE B 356 54.458 -29.053 -4.929 1.00 80.71 C
ANISOU 4581 CG1 ILE B 356 16396 8418 5852 797 1977 324 C
ATOM 4582 CG2 ILE B 356 53.246 -27.226 -6.121 1.00 70.53 C
ANISOU 4582 CG2 ILE B 356 15364 7253 4180 768 1577 496 C
ATOM 4583 CD1 ILE B 356 53.183 -29.849 -4.742 1.00 71.97 C
ANISOU 4583 CD1 ILE B 356 15396 7332 4618 719 1666 249 C
ATOM 4584 N ILE B 357 55.223 -24.649 -4.175 1.00102.91 N
ANISOU 4584 N ILE B 357 18580 11463 9060 948 2051 750 N
ATOM 4585 CA ILE B 357 55.063 -23.200 -4.175 1.00100.88 C
ANISOU 4585 CA ILE B 357 18240 11267 8825 973 1975 892 C
ATOM 4586 C ILE B 357 56.224 -22.544 -4.905 1.00102.38 C
ANISOU 4586 C ILE B 357 18550 11373 8978 978 2265 937 C
ATOM 4587 O ILE B 357 56.019 -21.726 -5.815 1.00101.84 O
ANISOU 4587 O ILE B 357 18728 11290 8675 958 2204 1032 O
ATOM 4588 CB ILE B 357 54.951 -22.680 -2.731 1.00 96.73 C
ANISOU 4588 CB ILE B 357 17273 10834 8647 1025 1933 937 C
ATOM 4589 CG1 ILE B 357 53.633 -23.126 -2.108 1.00103.71 C
ANISOU 4589 CG1 ILE B 357 18071 11811 9523 1010 1627 924 C
ATOM 4590 CG2 ILE B 357 55.090 -21.162 -2.685 1.00 89.05 C
ANISOU 4590 CG2 ILE B 357 16202 9889 7743 1057 1933 1075 C
ATOM 4591 CD1 ILE B 357 53.564 -22.882 -0.613 1.00107.61 C
ANISOU 4591 CD1 ILE B 357 18144 12391 10350 1058 1625 943 C
ATOM 4592 N TYR B 358 57.457 -22.970 -4.603 1.00105.78 N
ANISOU 4592 N TYR B 358 18845 11733 9614 1002 2582 871 N
ATOM 4593 CA TYR B 358 58.585 -22.339 -5.277 1.00 99.97 C
ANISOU 4593 CA TYR B 358 18213 10916 8854 999 2877 914 C
ATOM 4594 C TYR B 358 58.491 -22.562 -6.777 1.00 96.76 C
ANISOU 4594 C TYR B 358 18282 10440 8042 942 2911 904 C
ATOM 4595 O TYR B 358 58.600 -21.611 -7.568 1.00 98.66 O
ANISOU 4595 O TYR B 358 18727 10658 8100 918 2952 1008 O
ATOM 4596 CB TYR B 358 59.906 -22.901 -4.734 1.00 90.83 C
ANISOU 4596 CB TYR B 358 16839 9689 7985 1035 3191 837 C
ATOM 4597 CG TYR B 358 60.046 -22.888 -3.222 1.00 83.19 C
ANISOU 4597 CG TYR B 358 15428 8780 7402 1094 3146 831 C
ATOM 4598 CD1 TYR B 358 59.419 -21.917 -2.453 1.00 76.60 C
ANISOU 4598 CD1 TYR B 358 14372 8043 6689 1115 2953 914 C
ATOM 4599 CD2 TYR B 358 60.787 -23.863 -2.565 1.00 90.30 C
ANISOU 4599 CD2 TYR B 358 16148 9633 8529 1131 3288 747 C
ATOM 4600 CE1 TYR B 358 59.542 -21.904 -1.075 1.00 80.42 C
ANISOU 4600 CE1 TYR B 358 14477 8580 7498 1168 2914 903 C
ATOM 4601 CE2 TYR B 358 60.912 -23.861 -1.183 1.00 95.84 C
ANISOU 4601 CE2 TYR B 358 16474 10385 9556 1186 3229 752 C
ATOM 4602 CZ TYR B 358 60.287 -22.877 -0.442 1.00 93.30 C
ANISOU 4602 CZ TYR B 358 15949 10166 9337 1202 3045 824 C
ATOM 4603 OH TYR B 358 60.408 -22.864 0.933 1.00100.95 O
ANISOU 4603 OH TYR B 358 16567 11184 10605 1255 2988 825 O
ATOM 4604 N ASN B 359 58.101 -23.774 -7.173 1.00 85.71 N
ANISOU 4604 N ASN B 359 17090 9010 6466 915 2841 790 N
ATOM 4605 CA ASN B 359 58.059 -24.089 -8.590 1.00 94.92 C
ANISOU 4605 CA ASN B 359 18728 10104 7232 861 2881 759 C
ATOM 4606 C ASN B 359 57.100 -23.161 -9.314 1.00104.44 C
ANISOU 4606 C ASN B 359 20186 11356 8139 832 2600 881 C
ATOM 4607 O ASN B 359 57.358 -22.764 -10.457 1.00123.22 O
ANISOU 4607 O ASN B 359 22917 13677 10223 799 2696 929 O
ATOM 4608 CB ASN B 359 57.668 -25.551 -8.797 1.00103.96 C
ANISOU 4608 CB ASN B 359 20049 11208 8244 834 2808 606 C
ATOM 4609 CG ASN B 359 57.541 -25.918 -10.266 1.00121.75 C
ANISOU 4609 CG ASN B 359 22816 13389 10054 775 2818 557 C
ATOM 4610 OD1 ASN B 359 56.512 -25.658 -10.893 1.00126.05 O
ANISOU 4610 OD1 ASN B 359 23625 13970 10300 738 2508 596 O
ATOM 4611 ND2 ASN B 359 58.594 -26.513 -10.826 1.00131.19 N
ANISOU 4611 ND2 ASN B 359 24161 14481 11203 771 3169 471 N
ATOM 4612 N PHE B 360 56.011 -22.770 -8.651 1.00 95.62 N
ANISOU 4612 N PHE B 360 18893 10340 7097 849 2256 942 N
ATOM 4613 CA PHE B 360 55.015 -21.954 -9.326 1.00 94.67 C
ANISOU 4613 CA PHE B 360 19009 10258 6703 834 1937 1063 C
ATOM 4614 C PHE B 360 55.225 -20.455 -9.149 1.00105.88 C
ANISOU 4614 C PHE B 360 20298 11699 8233 867 1967 1239 C
ATOM 4615 O PHE B 360 54.621 -19.677 -9.896 1.00111.91 O
ANISOU 4615 O PHE B 360 21314 12460 8746 860 1757 1364 O
ATOM 4616 CB PHE B 360 53.621 -22.317 -8.796 1.00 88.22 C
ANISOU 4616 CB PHE B 360 18098 9532 5889 836 1514 1043 C
ATOM 4617 CG PHE B 360 53.133 -23.673 -9.227 1.00 88.19 C
ANISOU 4617 CG PHE B 360 18332 9497 5679 782 1389 887 C
ATOM 4618 CD1 PHE B 360 53.733 -24.353 -10.272 1.00 86.07 C
ANISOU 4618 CD1 PHE B 360 18426 9126 5152 740 1586 794 C
ATOM 4619 CD2 PHE B 360 52.068 -24.270 -8.570 1.00 93.15 C
ANISOU 4619 CD2 PHE B 360 18828 10193 6372 768 1078 829 C
ATOM 4620 CE1 PHE B 360 53.277 -25.604 -10.655 1.00 89.02 C
ANISOU 4620 CE1 PHE B 360 19028 9458 5336 686 1464 640 C
ATOM 4621 CE2 PHE B 360 51.609 -25.519 -8.950 1.00 94.22 C
ANISOU 4621 CE2 PHE B 360 19191 10286 6322 704 953 677 C
ATOM 4622 CZ PHE B 360 52.214 -26.184 -9.994 1.00 94.21 C
ANISOU 4622 CZ PHE B 360 19554 10177 6066 664 1142 580 C
ATOM 4623 N LEU B 361 56.066 -20.021 -8.203 1.00105.61 N
ANISOU 4623 N LEU B 361 19894 11672 8560 902 2207 1254 N
ATOM 4624 CA LEU B 361 56.135 -18.596 -7.895 1.00 95.91 C
ANISOU 4624 CA LEU B 361 18519 10461 7461 929 2194 1414 C
ATOM 4625 C LEU B 361 57.535 -18.016 -8.005 1.00 95.31 C
ANISOU 4625 C LEU B 361 18399 10303 7513 919 2600 1445 C
ATOM 4626 O LEU B 361 57.713 -16.808 -7.795 1.00 76.87 O
ANISOU 4626 O LEU B 361 15964 7959 5283 930 2627 1576 O
ATOM 4627 CB LEU B 361 55.565 -18.323 -6.497 1.00 85.06 C
ANISOU 4627 CB LEU B 361 16714 9188 6417 982 2011 1429 C
ATOM 4628 CG LEU B 361 54.049 -18.505 -6.401 1.00 77.10 C
ANISOU 4628 CG LEU B 361 15742 8264 5290 993 1574 1452 C
ATOM 4629 CD1 LEU B 361 53.554 -18.192 -4.990 1.00 75.57 C
ANISOU 4629 CD1 LEU B 361 15119 8165 5427 1047 1441 1470 C
ATOM 4630 CD2 LEU B 361 53.343 -17.642 -7.436 1.00 75.36 C
ANISOU 4630 CD2 LEU B 361 15850 8019 4765 990 1325 1602 C
ATOM 4631 N SER B 362 58.528 -18.839 -8.323 1.00 95.05 N
ANISOU 4631 N SER B 362 18434 10199 7481 898 2913 1329 N
ATOM 4632 CA SER B 362 59.889 -18.392 -8.582 1.00 93.81 C
ANISOU 4632 CA SER B 362 18274 9952 7417 879 3315 1349 C
ATOM 4633 C SER B 362 60.322 -19.038 -9.891 1.00 94.73 C
ANISOU 4633 C SER B 362 18814 9982 7199 827 3515 1294 C
ATOM 4634 O SER B 362 60.449 -20.266 -9.969 1.00 87.43 O
ANISOU 4634 O SER B 362 17934 9038 6246 829 3573 1149 O
ATOM 4635 CB SER B 362 60.821 -18.764 -7.425 1.00 90.32 C
ANISOU 4635 CB SER B 362 17405 9509 7404 922 3526 1255 C
ATOM 4636 OG SER B 362 62.184 -18.594 -7.771 1.00 99.54 O
ANISOU 4636 OG SER B 362 18588 10580 8654 898 3927 1246 O
ATOM 4637 N GLY B 363 60.508 -18.218 -10.928 1.00100.79 N
ANISOU 4637 N GLY B 363 19913 10689 7694 779 3615 1413 N
ATOM 4638 CA GLY B 363 60.969 -18.747 -12.200 1.00105.61 C
ANISOU 4638 CA GLY B 363 20950 11214 7962 726 3837 1365 C
ATOM 4639 C GLY B 363 62.388 -19.277 -12.142 1.00109.69 C
ANISOU 4639 C GLY B 363 21348 11654 8673 717 4294 1258 C
ATOM 4640 O GLY B 363 62.747 -20.196 -12.889 1.00119.37 O
ANISOU 4640 O GLY B 363 22830 12825 9702 693 4473 1149 O
ATOM 4641 N LYS B 364 63.198 -18.742 -11.230 1.00103.48 N
ANISOU 4641 N LYS B 364 20168 10863 8284 741 4478 1281 N
ATOM 4642 CA LYS B 364 64.538 -19.274 -11.016 1.00109.65 C
ANISOU 4642 CA LYS B 364 20769 11578 9314 744 4877 1177 C
ATOM 4643 C LYS B 364 64.475 -20.708 -10.497 1.00118.82 C
ANISOU 4643 C LYS B 364 21781 12759 10605 795 4818 1009 C
ATOM 4644 O LYS B 364 65.126 -21.616 -11.045 1.00126.98 O
ANISOU 4644 O LYS B 364 22960 13725 11561 784 5071 899 O
ATOM 4645 CB LYS B 364 65.266 -18.349 -10.036 1.00110.03 C
ANISOU 4645 CB LYS B 364 20408 11625 9773 762 5004 1240 C
ATOM 4646 CG LYS B 364 66.087 -17.263 -10.720 1.00118.78 C
ANISOU 4646 CG LYS B 364 21666 12648 10816 690 5322 1355 C
ATOM 4647 CD LYS B 364 66.657 -16.260 -9.730 1.00111.68 C
ANISOU 4647 CD LYS B 364 20377 11744 10313 699 5397 1423 C
ATOM 4648 CE LYS B 364 67.388 -15.156 -10.478 1.00118.17 C
ANISOU 4648 CE LYS B 364 21385 12470 11046 610 5709 1550 C
ATOM 4649 NZ LYS B 364 67.863 -14.070 -9.582 1.00121.65 N
ANISOU 4649 NZ LYS B 364 21484 12891 11846 605 5767 1626 N
ATOM 4650 N PHE B 365 63.687 -20.930 -9.433 1.00120.99 N
ANISOU 4650 N PHE B 365 21775 13122 11075 849 4496 992 N
ATOM 4651 CA PHE B 365 63.502 -22.284 -8.918 1.00111.93 C
ANISOU 4651 CA PHE B 365 20511 11987 10031 890 4411 851 C
ATOM 4652 C PHE B 365 62.932 -23.290 -9.901 1.00 98.86 C
ANISOU 4652 C PHE B 365 19281 10305 7977 854 4324 773 C
ATOM 4653 O PHE B 365 63.378 -24.441 -9.945 1.00 97.41 O
ANISOU 4653 O PHE B 365 19143 10068 7799 864 4454 642 O
ATOM 4654 CB PHE B 365 62.635 -22.282 -7.655 1.00111.94 C
ANISOU 4654 CB PHE B 365 20180 12090 10262 940 4071 862 C
ATOM 4655 CG PHE B 365 63.400 -22.082 -6.382 1.00105.08 C
ANISOU 4655 CG PHE B 365 18850 11235 9842 996 4171 861 C
ATOM 4656 CD1 PHE B 365 64.278 -23.057 -5.931 1.00106.27 C
ANISOU 4656 CD1 PHE B 365 18826 11334 10218 1031 4364 761 C
ATOM 4657 CD2 PHE B 365 63.221 -20.946 -5.614 1.00100.45 C
ANISOU 4657 CD2 PHE B 365 18012 10708 9446 1015 4056 960 C
ATOM 4658 CE1 PHE B 365 64.976 -22.890 -4.746 1.00103.42 C
ANISOU 4658 CE1 PHE B 365 18053 10985 10257 1083 4422 768 C
ATOM 4659 CE2 PHE B 365 63.917 -20.771 -4.428 1.00100.38 C
ANISOU 4659 CE2 PHE B 365 17598 10709 9833 1064 4129 953 C
ATOM 4660 CZ PHE B 365 64.793 -21.742 -3.993 1.00 99.96 C
ANISOU 4660 CZ PHE B 365 17379 10608 9993 1097 4301 860 C
ATOM 4661 N ARG B 366 61.936 -22.893 -10.689 1.00 93.58 N
ANISOU 4661 N ARG B 366 18935 9667 6957 813 4091 850 N
ATOM 4662 CA ARG B 366 61.397 -23.871 -11.622 1.00 98.80 C
ANISOU 4662 CA ARG B 366 20012 10299 7229 775 3982 765 C
ATOM 4663 C ARG B 366 62.358 -24.187 -12.773 1.00101.22 C
ANISOU 4663 C ARG B 366 20622 10498 7337 740 4373 695 C
ATOM 4664 O ARG B 366 62.376 -25.304 -13.296 1.00105.93 O
ANISOU 4664 O ARG B 366 21411 11048 7789 732 4422 555 O
ATOM 4665 CB ARG B 366 60.100 -23.362 -12.249 1.00107.83 C
ANISOU 4665 CB ARG B 366 21454 11493 8024 741 3627 871 C
ATOM 4666 CG ARG B 366 60.304 -22.207 -13.226 1.00119.26 C
ANISOU 4666 CG ARG B 366 23401 12872 9042 683 3768 925 C
ATOM 4667 CD ARG B 366 59.047 -21.835 -14.020 1.00124.79 C
ANISOU 4667 CD ARG B 366 24392 13616 9406 660 3390 1059 C
ATOM 4668 NE ARG B 366 57.956 -21.310 -13.203 1.00121.25 N
ANISOU 4668 NE ARG B 366 23652 13271 9148 701 2990 1119 N
ATOM 4669 CZ ARG B 366 56.690 -21.272 -13.607 1.00129.17 C
ANISOU 4669 CZ ARG B 366 24849 14325 9906 695 2557 1161 C
ATOM 4670 NH1 ARG B 366 55.747 -20.774 -12.817 1.00129.29 N
ANISOU 4670 NH1 ARG B 366 24566 14433 10123 734 2224 1214 N
ATOM 4671 NH2 ARG B 366 56.368 -21.747 -14.803 1.00141.85 N
ANISOU 4671 NH2 ARG B 366 26950 15885 11060 650 2451 1144 N
ATOM 4672 N GLU B 367 63.212 -23.219 -13.125 1.00100.70 N
ANISOU 4672 N GLU B 367 20598 10389 7274 715 4675 785 N
ATOM 4673 CA GLU B 367 64.205 -23.479 -14.160 1.00107.25 C
ANISOU 4673 CA GLU B 367 21699 11120 7929 677 5089 717 C
ATOM 4674 C GLU B 367 65.156 -24.524 -13.589 1.00102.21 C
ANISOU 4674 C GLU B 367 20788 10438 7609 723 5357 569 C
ATOM 4675 O GLU B 367 65.456 -25.531 -14.247 1.00105.37 O
ANISOU 4675 O GLU B 367 21426 10777 7835 713 5532 436 O
ATOM 4676 CB GLU B 367 64.964 -22.250 -14.678 1.00115.26 C
ANISOU 4676 CB GLU B 367 22802 12094 8898 630 5374 853 C
ATOM 4677 CG GLU B 367 64.158 -21.401 -15.672 1.00127.23 C
ANISOU 4677 CG GLU B 367 24756 13617 9968 575 5182 994 C
ATOM 4678 CD GLU B 367 64.759 -20.025 -15.928 1.00139.40 C
ANISOU 4678 CD GLU B 367 26322 15122 11523 530 5400 1165 C
ATOM 4679 OE1 GLU B 367 64.550 -19.113 -15.101 1.00138.39 O
ANISOU 4679 OE1 GLU B 367 25889 15040 11654 553 5245 1279 O
ATOM 4680 OE2 GLU B 367 65.437 -19.849 -16.964 1.00147.91 O
ANISOU 4680 OE2 GLU B 367 27735 16120 12343 466 5737 1186 O
ATOM 4681 N GLN B 368 65.648 -24.312 -12.361 1.00 97.78 N
ANISOU 4681 N GLN B 368 19735 9905 7513 776 5386 588 N
ATOM 4682 CA GLN B 368 66.571 -25.305 -11.808 1.00115.26 C
ANISOU 4682 CA GLN B 368 21687 12074 10030 826 5619 461 C
ATOM 4683 C GLN B 368 65.896 -26.663 -11.588 1.00113.78 C
ANISOU 4683 C GLN B 368 21553 11890 9790 859 5411 332 C
ATOM 4684 O GLN B 368 66.458 -27.712 -11.951 1.00 99.33 O
ANISOU 4684 O GLN B 368 19823 9990 7928 872 5634 198 O
ATOM 4685 CB GLN B 368 67.147 -24.782 -10.488 1.00110.91 C
ANISOU 4685 CB GLN B 368 20612 11559 9971 877 5634 517 C
ATOM 4686 CG GLN B 368 68.428 -23.957 -10.593 1.00104.18 C
ANISOU 4686 CG GLN B 368 19619 10657 9306 853 6016 568 C
ATOM 4687 CD GLN B 368 69.545 -24.682 -11.312 1.00101.35 C
ANISOU 4687 CD GLN B 368 19378 10212 8920 841 6446 455 C
ATOM 4688 OE1 GLN B 368 69.832 -25.839 -11.013 1.00103.51 O
ANISOU 4688 OE1 GLN B 368 19544 10465 9320 894 6496 330 O
ATOM 4689 NE2 GLN B 368 70.180 -24.011 -12.260 1.00103.96 N
ANISOU 4689 NE2 GLN B 368 19930 10487 9084 771 6769 497 N
ATOM 4690 N PHE B 369 64.662 -26.665 -11.063 1.00117.30 N
ANISOU 4690 N PHE B 369 21955 12410 10204 867 4993 364 N
ATOM 4691 CA PHE B 369 63.970 -27.933 -10.862 1.00120.57 C
ANISOU 4691 CA PHE B 369 22435 12816 10558 881 4794 244 C
ATOM 4692 C PHE B 369 63.683 -28.629 -12.174 1.00124.91 C
ANISOU 4692 C PHE B 369 23492 13304 10665 828 4837 142 C
ATOM 4693 O PHE B 369 63.801 -29.850 -12.271 1.00130.27 O
ANISOU 4693 O PHE B 369 24257 13922 11317 841 4907 -1 O
ATOM 4694 CB PHE B 369 62.648 -27.733 -10.118 1.00128.48 C
ANISOU 4694 CB PHE B 369 23313 13915 11590 884 4348 300 C
ATOM 4695 CG PHE B 369 62.785 -27.226 -8.713 1.00128.47 C
ANISOU 4695 CG PHE B 369 22819 13980 12013 941 4268 375 C
ATOM 4696 CD1 PHE B 369 64.011 -27.210 -8.071 1.00125.49 C
ANISOU 4696 CD1 PHE B 369 22122 13570 11987 991 4544 374 C
ATOM 4697 CD2 PHE B 369 61.663 -26.796 -8.021 1.00120.80 C
ANISOU 4697 CD2 PHE B 369 21705 13109 11084 943 3906 441 C
ATOM 4698 CE1 PHE B 369 64.114 -26.762 -6.768 1.00115.76 C
ANISOU 4698 CE1 PHE B 369 20461 12400 11123 1041 4445 438 C
ATOM 4699 CE2 PHE B 369 61.762 -26.342 -6.726 1.00112.38 C
ANISOU 4699 CE2 PHE B 369 20207 12108 10385 995 3834 501 C
ATOM 4700 CZ PHE B 369 62.987 -26.324 -6.097 1.00110.67 C
ANISOU 4700 CZ PHE B 369 19696 11853 10499 1044 4096 499 C
ATOM 4701 N LYS B 370 63.243 -27.877 -13.178 1.00132.14 N
ANISOU 4701 N LYS B 370 24761 14233 11212 769 4769 215 N
ATOM 4702 CA LYS B 370 62.981 -28.465 -14.481 1.00137.36 C
ANISOU 4702 CA LYS B 370 25942 14837 11412 714 4800 121 C
ATOM 4703 C LYS B 370 64.236 -29.060 -15.102 1.00131.52 C
ANISOU 4703 C LYS B 370 25322 14001 10650 719 5275 8 C
ATOM 4704 O LYS B 370 64.166 -30.119 -15.724 1.00136.02 O
ANISOU 4704 O LYS B 370 26177 14510 10993 706 5329 -145 O
ATOM 4705 CB LYS B 370 62.249 -27.477 -15.384 1.00150.50 C
ANISOU 4705 CB LYS B 370 27962 16539 12684 656 4605 242 C
ATOM 4706 CG LYS B 370 60.785 -27.438 -14.919 1.00156.07 C
ANISOU 4706 CG LYS B 370 28628 17329 13342 651 4082 278 C
ATOM 4707 CD LYS B 370 59.747 -27.359 -16.017 1.00164.01 C
ANISOU 4707 CD LYS B 370 30127 18345 13846 590 3781 288 C
ATOM 4708 CE LYS B 370 58.356 -27.282 -15.387 1.00162.09 C
ANISOU 4708 CE LYS B 370 29753 18194 13641 591 3269 325 C
ATOM 4709 NZ LYS B 370 57.278 -26.997 -16.374 1.00166.88 N
ANISOU 4709 NZ LYS B 370 30793 18823 13791 541 2907 365 N
ATOM 4710 N ALA B 371 65.378 -28.368 -15.032 1.00127.58 N
ANISOU 4710 N ALA B 371 24637 13482 10355 731 5631 74 N
ATOM 4711 CA ALA B 371 66.576 -28.981 -15.601 1.00124.25 C
ANISOU 4711 CA ALA B 371 24304 12974 9932 737 6096 -46 C
ATOM 4712 C ALA B 371 66.936 -30.270 -14.863 1.00125.26 C
ANISOU 4712 C ALA B 371 24172 13066 10354 809 6154 -197 C
ATOM 4713 O ALA B 371 67.302 -31.282 -15.488 1.00129.58 O
ANISOU 4713 O ALA B 371 24941 13542 10752 815 6364 -358 O
ATOM 4714 CB ALA B 371 67.739 -27.993 -15.557 1.00114.38 C
ANISOU 4714 CB ALA B 371 22853 11711 8896 730 6461 50 C
ATOM 4715 N ALA B 372 66.752 -30.286 -13.538 1.00122.24 N
ANISOU 4715 N ALA B 372 23349 12733 10365 865 5945 -149 N
ATOM 4716 CA ALA B 372 67.029 -31.512 -12.793 1.00118.77 C
ANISOU 4716 CA ALA B 372 22679 12256 10191 935 5970 -273 C
ATOM 4717 C ALA B 372 66.030 -32.602 -13.170 1.00113.37 C
ANISOU 4717 C ALA B 372 22314 11540 9221 914 5731 -398 C
ATOM 4718 O ALA B 372 66.376 -33.785 -13.250 1.00109.43 O
ANISOU 4718 O ALA B 372 21867 10967 8745 950 5872 -556 O
ATOM 4719 CB ALA B 372 67.000 -31.237 -11.292 1.00124.71 C
ANISOU 4719 CB ALA B 372 22923 13071 11390 994 5783 -180 C
ATOM 4720 N PHE B 373 64.779 -32.193 -13.382 1.00130.29 N
ANISOU 4720 N PHE B 373 24663 13739 11103 856 5359 -334 N
ATOM 4721 CA PHE B 373 63.678 -33.066 -13.769 1.00135.78 C
ANISOU 4721 CA PHE B 373 25675 14413 11501 814 5071 -443 C
ATOM 4722 C PHE B 373 63.909 -33.671 -15.147 1.00135.51 C
ANISOU 4722 C PHE B 373 26132 14298 11057 773 5275 -589 C
ATOM 4723 O PHE B 373 63.620 -34.849 -15.383 1.00137.31 O
ANISOU 4723 O PHE B 373 26554 14460 11157 767 5229 -757 O
ATOM 4724 CB PHE B 373 62.416 -32.199 -13.759 1.00147.91 C
ANISOU 4724 CB PHE B 373 27294 16043 12861 760 4651 -317 C
ATOM 4725 CG PHE B 373 61.132 -32.948 -13.698 1.00160.18 C
ANISOU 4725 CG PHE B 373 29013 17604 14244 717 4258 -398 C
ATOM 4726 CD1 PHE B 373 60.598 -33.317 -12.478 1.00156.53 C
ANISOU 4726 CD1 PHE B 373 28219 17175 14080 742 4032 -389 C
ATOM 4727 CD2 PHE B 373 60.427 -33.239 -14.854 1.00171.07 C
ANISOU 4727 CD2 PHE B 373 30885 18960 15154 644 4100 -480 C
ATOM 4728 CE1 PHE B 373 59.401 -33.984 -12.407 1.00159.62 C
ANISOU 4728 CE1 PHE B 373 28757 17569 14322 687 3677 -465 C
ATOM 4729 CE2 PHE B 373 59.224 -33.913 -14.789 1.00174.37 C
ANISOU 4729 CE2 PHE B 373 31444 19384 15425 591 3714 -563 C
ATOM 4730 CZ PHE B 373 58.712 -34.287 -13.559 1.00169.58 C
ANISOU 4730 CZ PHE B 373 30491 18804 15136 609 3509 -557 C
ATOM 4731 N SER B 374 64.426 -32.862 -16.068 1.00136.35 N
ANISOU 4731 N SER B 374 26457 14405 10943 740 5507 -530 N
ATOM 4732 CA SER B 374 64.769 -33.305 -17.410 1.00139.83 C
ANISOU 4732 CA SER B 374 27375 14775 10980 701 5755 -658 C
ATOM 4733 C SER B 374 65.914 -34.298 -17.375 1.00143.19 C
ANISOU 4733 C SER B 374 27691 15115 11600 764 6168 -824 C
ATOM 4734 O SER B 374 65.974 -35.209 -18.210 1.00154.55 O
ANISOU 4734 O SER B 374 29482 16482 12760 751 6295 -1005 O
ATOM 4735 CB SER B 374 65.132 -32.109 -18.291 1.00136.02 C
ANISOU 4735 CB SER B 374 27119 14313 10250 651 5939 -530 C
ATOM 4736 OG SER B 374 64.025 -31.242 -18.462 1.00128.66 O
ANISOU 4736 OG SER B 374 26344 13452 9087 600 5542 -387 O
ATOM 4737 N TRP B 375 66.824 -34.147 -16.408 1.00135.75 N
ANISOU 4737 N TRP B 375 26262 14179 11136 836 6369 -775 N
ATOM 4738 CA TRP B 375 67.977 -35.039 -16.363 1.00136.35 C
ANISOU 4738 CA TRP B 375 26201 14179 11425 909 6764 -929 C
ATOM 4739 C TRP B 375 67.578 -36.476 -16.025 1.00144.45 C
ANISOU 4739 C TRP B 375 27246 15142 12495 953 6624 -1104 C
ATOM 4740 O TRP B 375 68.067 -37.421 -16.658 1.00157.65 O
ANISOU 4740 O TRP B 375 29122 16730 14047 980 6879 -1299 O
ATOM 4741 CB TRP B 375 68.974 -34.518 -15.329 1.00129.90 C
ANISOU 4741 CB TRP B 375 24837 13393 11124 976 6947 -830 C
ATOM 4742 CG TRP B 375 70.185 -35.361 -15.200 1.00133.14 C
ANISOU 4742 CG TRP B 375 25051 13739 11799 1062 7332 -980 C
ATOM 4743 CD1 TRP B 375 71.218 -35.443 -16.082 1.00138.85 C
ANISOU 4743 CD1 TRP B 375 25915 14411 12432 1065 7794 -1083 C
ATOM 4744 CD2 TRP B 375 70.466 -36.304 -14.157 1.00142.27 C
ANISOU 4744 CD2 TRP B 375 25849 14869 13338 1164 7289 -1056 C
ATOM 4745 NE1 TRP B 375 72.148 -36.351 -15.638 1.00148.69 N
ANISOU 4745 NE1 TRP B 375 26880 15607 14010 1171 8039 -1226 N
ATOM 4746 CE2 TRP B 375 71.708 -36.898 -14.460 1.00150.35 C
ANISOU 4746 CE2 TRP B 375 26789 15830 14508 1236 7726 -1209 C
ATOM 4747 CE3 TRP B 375 69.797 -36.691 -12.986 1.00138.45 C
ANISOU 4747 CE3 TRP B 375 25110 14409 13087 1203 6930 -1009 C
ATOM 4748 CZ2 TRP B 375 72.296 -37.861 -13.641 1.00152.01 C
ANISOU 4748 CZ2 TRP B 375 26665 15999 15092 1356 7791 -1315 C
ATOM 4749 CZ3 TRP B 375 70.383 -37.645 -12.173 1.00137.61 C
ANISOU 4749 CZ3 TRP B 375 24696 14258 13331 1312 7006 -1102 C
ATOM 4750 CH2 TRP B 375 71.620 -38.221 -12.506 1.00145.01 C
ANISOU 4750 CH2 TRP B 375 25553 15133 14412 1392 7422 -1254 C
ATOM 4751 N TRP B 376 66.666 -36.670 -15.073 1.00138.78 N
ANISOU 4751 N TRP B 376 26343 14458 11931 958 6227 -1049 N
ATOM 4752 CA TRP B 376 66.241 -38.015 -14.678 1.00142.17 C
ANISOU 4752 CA TRP B 376 26786 14815 12415 990 6083 -1203 C
ATOM 4753 C TRP B 376 64.899 -38.396 -15.305 1.00147.46 C
ANISOU 4753 C TRP B 376 27888 15473 12666 897 5727 -1276 C
ATOM 4754 O TRP B 376 64.010 -38.937 -14.640 1.00148.95 O
ANISOU 4754 O TRP B 376 28012 15655 12926 881 5399 -1294 O
ATOM 4755 CB TRP B 376 66.203 -38.130 -13.153 1.00136.52 C
ANISOU 4755 CB TRP B 376 25577 14129 12164 1057 5916 -1112 C
ATOM 4756 CG TRP B 376 65.746 -39.478 -12.630 1.00152.16 C
ANISOU 4756 CG TRP B 376 27558 16027 14228 1087 5762 -1250 C
ATOM 4757 CD1 TRP B 376 64.614 -39.722 -11.907 1.00155.77 C
ANISOU 4757 CD1 TRP B 376 27972 16501 14715 1048 5372 -1209 C
ATOM 4758 CD2 TRP B 376 66.392 -40.757 -12.806 1.00159.13 C
ANISOU 4758 CD2 TRP B 376 28498 16789 15176 1160 6001 -1458 C
ATOM 4759 NE1 TRP B 376 64.517 -41.061 -11.613 1.00161.36 N
ANISOU 4759 NE1 TRP B 376 28715 17096 15497 1082 5354 -1369 N
ATOM 4760 CE2 TRP B 376 65.592 -41.718 -12.152 1.00161.92 C
ANISOU 4760 CE2 TRP B 376 28847 17079 15595 1158 5727 -1525 C
ATOM 4761 CE3 TRP B 376 67.566 -41.179 -13.445 1.00151.87 C
ANISOU 4761 CE3 TRP B 376 27626 15802 14274 1230 6426 -1603 C
ATOM 4762 CZ2 TRP B 376 65.925 -43.074 -12.120 1.00153.12 C
ANISOU 4762 CZ2 TRP B 376 27784 15829 14564 1226 5851 -1729 C
ATOM 4763 CZ3 TRP B 376 67.895 -42.530 -13.408 1.00146.31 C
ANISOU 4763 CZ3 TRP B 376 26957 14975 13660 1309 6548 -1813 C
ATOM 4764 CH2 TRP B 376 67.076 -43.458 -12.751 1.00143.98 C
ANISOU 4764 CH2 TRP B 376 26665 14610 13430 1309 6254 -1873 C
ATOM 4765 N LEU B 377 64.735 -38.122 -16.598 1.00157.18 N
ANISOU 4765 N LEU B 377 29573 16701 13448 827 5783 -1322 N
ATOM 4766 CA LEU B 377 63.534 -38.500 -17.340 1.00147.56 C
ANISOU 4766 CA LEU B 377 28804 15470 11792 735 5447 -1412 C
ATOM 4767 C LEU B 377 63.768 -38.339 -18.836 1.00131.49 C
ANISOU 4767 C LEU B 377 27274 13411 9275 684 5644 -1492 C
ATOM 4768 O LEU B 377 62.871 -38.582 -19.641 1.00134.65 O
ANISOU 4768 O LEU B 377 28104 13802 9253 605 5386 -1575 O
ATOM 4769 CB LEU B 377 62.324 -37.664 -16.906 1.00135.18 C
ANISOU 4769 CB LEU B 377 27172 14005 10184 673 4979 -1240 C
ATOM 4770 CG LEU B 377 61.563 -38.092 -15.644 1.00129.13 C
ANISOU 4770 CG LEU B 377 26085 13254 9724 681 4653 -1216 C
ATOM 4771 CD1 LEU B 377 60.375 -37.176 -15.385 1.00112.56 C
ANISOU 4771 CD1 LEU B 377 23958 11268 7542 618 4216 -1060 C
ATOM 4772 CD2 LEU B 377 61.117 -39.543 -15.739 1.00117.15 C
ANISOU 4772 CD2 LEU B 377 24767 11629 8116 657 4547 -1441 C
TER 4773 LEU B 377
HETATM 4774 C1 NRZ A 401 56.284 -7.994 30.877 0.00 15.50 C
HETATM 4775 C10 NRZ A 401 54.399 -0.617 26.255 1.00119.35 C
HETATM 4776 C11 NRZ A 401 54.966 -0.326 27.649 1.00127.89 C
HETATM 4777 C12 NRZ A 401 54.494 1.008 28.212 1.00121.06 C
HETATM 4778 C13 NRZ A 401 55.475 3.146 29.055 1.00 99.74 C
HETATM 4779 C14 NRZ A 401 56.658 3.759 29.456 1.00 87.63 C
HETATM 4780 C15 NRZ A 401 56.651 5.047 29.984 1.00 81.73 C
HETATM 4781 C16 NRZ A 401 55.436 5.716 30.097 1.00 84.09 C
HETATM 4782 C17 NRZ A 401 54.241 5.127 29.693 1.00 88.82 C
HETATM 4783 C18 NRZ A 401 54.274 3.837 29.174 1.00100.24 C
HETATM 4784 C19 NRZ A 401 52.921 5.849 29.817 1.00 82.35 C
HETATM 4785 C2 NRZ A 401 56.260 -5.604 31.182 0.05 51.34 C
HETATM 4786 C20 NRZ A 401 57.947 5.682 30.429 1.00 81.80 C
HETATM 4787 C3 NRZ A 401 56.877 -4.436 31.608 1.00 63.66 C
HETATM 4788 C4 NRZ A 401 56.350 -3.207 31.262 0.13 89.55 C
HETATM 4789 C5 NRZ A 401 55.203 -3.136 30.489 0.80122.81 C
HETATM 4790 C6 NRZ A 401 54.578 -4.299 30.074 0.45 90.63 C
HETATM 4791 C7 NRZ A 401 55.104 -5.528 30.419 0.00 72.10 C
HETATM 4792 C8 NRZ A 401 53.203 -2.011 27.745 1.00134.38 C
HETATM 4793 C9 NRZ A 401 52.999 -1.070 26.580 1.00122.38 C
HETATM 4794 N1 NRZ A 401 54.422 -1.482 28.425 1.00153.29 N
HETATM 4795 N2 NRZ A 401 55.519 1.838 28.523 1.00111.05 N
HETATM 4796 O1 NRZ A 401 56.782 -6.826 31.528 0.61 22.66 O
HETATM 4797 O2 NRZ A 401 55.507 -0.581 30.434 1.00209.84 O
HETATM 4798 O3 NRZ A 401 53.202 -1.489 30.578 1.00210.14 O
HETATM 4799 O4 NRZ A 401 53.312 1.262 28.363 1.00116.89 O
HETATM 4800 S1 NRZ A 401 54.533 -1.558 30.055 1.00196.19 S
HETATM 4801 H2 NRZ A 401 56.760 -8.775 31.204 0.00 19.58 H
HETATM 4802 H1 NRZ A 401 56.418 -7.912 29.919 0.04 19.58 H
HETATM 4803 H3 NRZ A 401 55.336 -8.090 31.065 1.00 19.58 H
HETATM 4804 H12 NRZ A 401 54.394 0.186 25.694 1.00144.20 H
HETATM 4805 H13 NRZ A 401 54.906 -1.319 25.800 1.00144.20 H
HETATM 4806 H14 NRZ A 401 55.957 -0.326 27.634 1.00154.46 H
HETATM 4807 H16 NRZ A 401 57.475 3.298 29.370 1.00106.15 H
HETATM 4808 H17 NRZ A 401 55.422 6.586 30.455 1.00101.89 H
HETATM 4809 H18 NRZ A 401 53.471 3.427 28.901 1.00121.28 H
HETATM 4810 H19 NRZ A 401 52.211 5.204 29.967 1.00 99.81 H
HETATM 4811 H20 NRZ A 401 52.742 6.341 28.999 1.00 99.81 H
HETATM 4812 H21 NRZ A 401 52.958 6.468 30.564 1.00 99.81 H
HETATM 4813 H23 NRZ A 401 58.665 5.407 29.836 1.00 99.15 H
HETATM 4814 H24 NRZ A 401 58.153 5.401 31.336 1.00 99.15 H
HETATM 4815 H22 NRZ A 401 57.861 6.649 30.404 1.00 99.15 H
HETATM 4816 H4 NRZ A 401 57.654 -4.480 32.131 0.00 77.38 H
HETATM 4817 H5 NRZ A 401 56.772 -2.421 31.554 0.00108.45 H
HETATM 4818 H6 NRZ A 401 53.796 -4.256 29.557 0.00109.75 H
HETATM 4819 H7 NRZ A 401 54.677 -6.313 30.137 0.00 87.51 H
HETATM 4820 H8 NRZ A 401 53.346 -2.927 27.435 1.00162.24 H
HETATM 4821 H9 NRZ A 401 52.432 -1.995 28.347 1.00162.24 H
HETATM 4822 H11 NRZ A 401 52.593 -1.533 25.819 1.00147.84 H
HETATM 4823 H10 NRZ A 401 52.432 -0.313 26.831 1.00147.84 H
HETATM 4824 H15 NRZ A 401 56.321 1.523 28.375 1.00134.24 H
HETATM 4825 C1 SOG A 402 45.130 12.252 49.261 1.00107.82 C
HETATM 4826 C2 SOG A 402 43.896 11.605 49.876 1.00 98.99 C
HETATM 4827 C3 SOG A 402 42.679 12.497 49.649 1.00 94.49 C
HETATM 4828 C4 SOG A 402 42.946 13.919 50.107 1.00101.26 C
HETATM 4829 C5 SOG A 402 44.245 14.433 49.484 1.00100.96 C
HETATM 4830 C6 SOG A 402 44.634 15.826 49.952 1.00105.94 C
HETATM 4831 C1' SOG A 402 47.481 11.410 47.995 1.00107.95 C
HETATM 4832 C2' SOG A 402 48.329 10.191 47.719 1.00112.67 C
HETATM 4833 C3' SOG A 402 47.506 8.917 47.717 1.00123.13 C
HETATM 4834 C4' SOG A 402 48.334 7.651 47.673 1.00110.00 C
HETATM 4835 C5' SOG A 402 47.587 6.412 48.111 1.00 95.62 C
HETATM 4836 C6' SOG A 402 48.486 5.252 48.468 1.00 94.97 C
HETATM 4837 C7' SOG A 402 47.831 4.128 49.235 1.00 81.53 C
HETATM 4838 C8' SOG A 402 48.805 3.093 49.751 1.00 58.33 C
HETATM 4839 S1 SOG A 402 46.575 11.207 49.567 1.00111.47 S
HETATM 4840 O2 SOG A 402 43.665 10.343 49.261 1.00 95.15 O
HETATM 4841 O3 SOG A 402 41.536 11.959 50.312 1.00 89.46 O
HETATM 4842 O4 SOG A 402 41.861 14.771 49.740 1.00111.95 O
HETATM 4843 O5 SOG A 402 45.326 13.546 49.816 1.00100.33 O
HETATM 4844 O6 SOG A 402 43.755 16.828 49.432 1.00112.13 O
HETATM 4845 C1 SOG A 403 81.823 -14.972 11.486 1.00153.79 C
HETATM 4846 C2 SOG A 403 82.442 -15.436 10.174 1.00141.33 C
HETATM 4847 C3 SOG A 403 82.991 -16.848 10.356 1.00140.61 C
HETATM 4848 C4 SOG A 403 83.907 -16.946 11.574 1.00139.03 C
HETATM 4849 C5 SOG A 403 83.260 -16.307 12.808 1.00139.62 C
HETATM 4850 C6 SOG A 403 84.200 -16.202 13.998 1.00120.57 C
HETATM 4851 C1' SOG A 403 80.405 -13.162 13.065 1.00129.63 C
HETATM 4852 C2' SOG A 403 79.551 -11.937 13.306 1.00104.52 C
HETATM 4853 C3' SOG A 403 80.284 -10.648 13.026 1.00105.95 C
HETATM 4854 C4' SOG A 403 79.462 -9.417 13.325 1.00109.28 C
HETATM 4855 C5' SOG A 403 79.551 -8.355 12.257 1.00105.24 C
HETATM 4856 C6' SOG A 403 78.219 -8.009 11.644 1.00106.69 C
HETATM 4857 C7' SOG A 403 78.247 -7.777 10.157 1.00110.63 C
HETATM 4858 C8' SOG A 403 76.879 -7.533 9.562 1.00114.31 C
HETATM 4859 S1 SOG A 403 81.071 -13.328 11.370 1.00156.00 S
HETATM 4860 O2 SOG A 403 81.464 -15.449 9.140 1.00125.85 O
HETATM 4861 O3 SOG A 403 83.671 -17.271 9.175 1.00136.00 O
HETATM 4862 O4 SOG A 403 84.214 -18.310 11.860 1.00128.57 O
HETATM 4863 O5 SOG A 403 82.816 -14.975 12.502 1.00151.87 O
HETATM 4864 O6 SOG A 403 84.453 -17.472 14.598 1.00104.98 O
HETATM 4865 C1 SOG A 404 43.351 -2.733 15.038 1.00145.05 C
HETATM 4866 C2 SOG A 404 43.682 -2.840 16.523 1.00141.43 C
HETATM 4867 C3 SOG A 404 43.925 -1.448 17.097 1.00139.50 C
HETATM 4868 C4 SOG A 404 44.984 -0.722 16.297 1.00133.61 C
HETATM 4869 C5 SOG A 404 44.599 -0.710 14.823 1.00135.63 C
HETATM 4870 C6 SOG A 404 45.674 -0.086 13.950 1.00129.83 C
HETATM 4871 C1' SOG A 404 41.488 -4.212 13.545 1.00152.74 C
HETATM 4872 C2' SOG A 404 40.883 -5.514 13.063 1.00144.21 C
HETATM 4873 C3' SOG A 404 39.523 -5.321 12.424 1.00130.17 C
HETATM 4874 C4' SOG A 404 38.860 -6.612 12.002 1.00120.27 C
HETATM 4875 C5' SOG A 404 38.434 -7.505 13.146 1.00115.38 C
HETATM 4876 C6' SOG A 404 37.682 -8.742 12.714 1.00107.68 C
HETATM 4877 C7' SOG A 404 37.174 -9.609 13.839 1.00101.01 C
HETATM 4878 C8' SOG A 404 36.398 -10.826 13.384 1.00 92.39 C
HETATM 4879 S1 SOG A 404 43.126 -4.392 14.342 1.00151.96 S
HETATM 4880 O2 SOG A 404 42.611 -3.462 17.226 1.00139.58 O
HETATM 4881 O3 SOG A 404 44.314 -1.536 18.465 1.00146.96 O
HETATM 4882 O4 SOG A 404 45.141 0.616 16.766 1.00128.16 O
HETATM 4883 O5 SOG A 404 44.403 -2.058 14.359 1.00140.55 O
HETATM 4884 O6 SOG A 404 46.017 1.233 14.383 1.00121.50 O
HETATM 4885 S SO4 A 405 85.017 -13.843 38.237 1.00176.21 S
HETATM 4886 O1 SO4 A 405 85.442 -14.903 37.324 1.00177.84 O
HETATM 4887 O2 SO4 A 405 84.651 -12.663 37.458 1.00174.28 O
HETATM 4888 O3 SO4 A 405 83.863 -14.300 39.012 1.00178.33 O
HETATM 4889 O4 SO4 A 405 86.113 -13.501 39.142 1.00170.13 O
HETATM 4890 CAD PGW A 406 67.226 -36.515 30.464 1.00106.74 C
HETATM 4891 OAE PGW A 406 66.640 -36.809 29.198 1.00 89.57 O
HETATM 4892 OAF PGW A 406 67.349 -34.156 29.951 1.00103.10 O
HETATM 4893 P PGW A 406 66.904 -32.971 34.197 1.00170.37 P
HETATM 4894 C01 PGW A 406 62.776 -30.445 34.249 1.00111.94 C
HETATM 4895 C1 PGW A 406 64.733 -30.244 31.166 1.00 90.56 C
HETATM 4896 O01 PGW A 406 64.271 -29.978 32.403 1.00111.84 O
HETATM 4897 C02 PGW A 406 63.597 -31.045 33.131 1.00125.70 C
HETATM 4898 C2 PGW A 406 64.599 -29.075 30.227 1.00 74.46 C
HETATM 4899 O02 PGW A 406 65.190 -31.310 30.858 1.00 85.95 O
HETATM 4900 C03 PGW A 406 64.500 -32.183 33.553 1.00154.27 C
HETATM 4901 C3 PGW A 406 65.869 -28.313 30.017 1.00 55.32 C
HETATM 4902 O03 PGW A 406 61.533 -30.017 33.650 1.00109.86 O
HETATM 4903 C04 PGW A 406 67.432 -34.760 32.289 1.00140.91 C
HETATM 4904 C4 PGW A 406 65.735 -27.278 28.912 1.00 52.26 C
HETATM 4905 O04 PGW A 406 60.960 -32.152 33.299 1.00108.11 O
HETATM 4906 C05 PGW A 406 66.896 -35.108 30.915 1.00117.62 C
HETATM 4907 C5 PGW A 406 66.931 -26.373 28.745 1.00 58.89 C
HETATM 4908 C06 PGW A 406 66.617 -20.421 25.856 1.00 69.28 C
HETATM 4909 C6 PGW A 406 66.765 -25.314 27.683 1.00 49.36 C
HETATM 4910 C07 PGW A 406 65.975 -19.089 25.624 1.00 81.19 C
HETATM 4911 C7 PGW A 406 67.781 -24.185 27.791 1.00 47.15 C
HETATM 4912 C08 PGW A 406 65.848 -18.727 24.151 1.00 89.14 C
HETATM 4913 C8 PGW A 406 67.473 -23.004 26.931 1.00 55.62 C
HETATM 4914 C09 PGW A 406 64.875 -17.607 23.864 1.00 89.30 C
HETATM 4915 C9 PGW A 406 67.804 -21.698 27.588 1.00 50.53 C
HETATM 4916 C10 PGW A 406 67.340 -20.554 27.161 1.00 53.57 C
HETATM 4917 C11 PGW A 406 63.457 -18.069 23.608 1.00 78.69 C
HETATM 4918 O11 PGW A 406 65.781 -31.821 34.143 1.00170.15 O
HETATM 4919 C12 PGW A 406 62.447 -16.954 23.479 1.00 69.18 C
HETATM 4920 O12 PGW A 406 66.930 -33.441 32.655 1.00160.88 O
HETATM 4921 C13 PGW A 406 61.054 -17.452 23.199 1.00 67.40 C
HETATM 4922 O13 PGW A 406 68.224 -32.378 34.611 1.00167.63 O
HETATM 4923 C14 PGW A 406 60.004 -16.417 23.515 1.00 74.84 C
HETATM 4924 O14 PGW A 406 66.343 -34.112 34.999 1.00170.01 O
HETATM 4925 C15 PGW A 406 57.914 -22.687 30.954 1.00 42.76 C
HETATM 4926 C16 PGW A 406 57.369 -22.503 29.566 1.00 41.07 C
HETATM 4927 C17 PGW A 406 58.411 -22.560 28.477 1.00 38.21 C
HETATM 4928 C18 PGW A 406 58.034 -23.488 27.344 1.00 24.73 C
HETATM 4929 C19 PGW A 406 60.818 -30.978 33.063 1.00106.57 C
HETATM 4930 C20 PGW A 406 59.837 -30.431 32.061 1.00 94.24 C
HETATM 4931 C21 PGW A 406 58.952 -29.349 32.602 1.00 76.65 C
HETATM 4932 C22 PGW A 406 57.693 -29.164 31.768 1.00 62.43 C
HETATM 4933 C23 PGW A 406 56.755 -28.078 32.251 1.00 49.38 C
HETATM 4934 C24 PGW A 406 57.073 -26.689 31.752 1.00 35.15 C
HETATM 4935 C25 PGW A 406 55.939 -25.708 31.952 1.00 49.69 C
HETATM 4936 C26 PGW A 406 56.091 -24.402 31.202 1.00 54.49 C
HETATM 4937 C27 PGW A 406 56.938 -23.348 31.885 1.00 52.50 C
HETATM 4938 C28 PGW A 406 58.607 -23.104 25.999 1.00 23.11 C
HETATM 4939 C29 PGW A 406 58.635 -23.520 23.512 1.00 38.08 C
HETATM 4940 C30 PGW A 406 58.132 -23.974 24.861 1.00 33.16 C
HETATM 4941 C1 SOG B 401 57.585 -33.432 35.355 1.00125.54 C
HETATM 4942 C2 SOG B 401 56.176 -32.871 35.431 1.00110.38 C
HETATM 4943 C3 SOG B 401 56.223 -31.350 35.527 1.00106.45 C
HETATM 4944 C4 SOG B 401 57.095 -30.920 36.689 1.00117.54 C
HETATM 4945 C5 SOG B 401 58.470 -31.600 36.620 1.00127.23 C
HETATM 4946 C6 SOG B 401 59.301 -31.325 37.865 1.00112.50 C
HETATM 4947 C1' SOG B 401 58.696 -35.760 34.196 1.00131.67 C
HETATM 4948 C2' SOG B 401 58.421 -37.138 33.623 1.00117.14 C
HETATM 4949 C3' SOG B 401 59.643 -37.767 32.993 1.00111.45 C
HETATM 4950 C4' SOG B 401 60.627 -38.281 34.017 1.00112.95 C
HETATM 4951 C5' SOG B 401 62.083 -38.048 33.676 1.00116.51 C
HETATM 4952 C6' SOG B 401 62.612 -38.838 32.502 1.00113.47 C
HETATM 4953 C7' SOG B 401 64.081 -38.587 32.258 1.00108.44 C
HETATM 4954 C8' SOG B 401 64.725 -39.517 31.257 1.00103.67 C
HETATM 4955 S1 SOG B 401 57.364 -35.228 35.329 1.00133.76 S
HETATM 4956 O2 SOG B 401 55.430 -33.254 34.281 1.00102.97 O
HETATM 4957 O3 SOG B 401 54.905 -30.825 35.675 1.00 96.86 O
HETATM 4958 O4 SOG B 401 57.257 -29.501 36.703 1.00111.49 O
HETATM 4959 O5 SOG B 401 58.321 -33.029 36.503 1.00134.71 O
HETATM 4960 O6 SOG B 401 60.598 -31.920 37.814 1.00 95.77 O
HETATM 4961 C1 SOG B 402 68.823 -11.013 10.742 1.00156.96 C
HETATM 4962 C2 SOG B 402 67.646 -10.332 10.058 1.00150.82 C
HETATM 4963 C3 SOG B 402 68.166 -9.176 9.209 1.00137.93 C
HETATM 4964 C4 SOG B 402 69.033 -8.239 10.029 1.00132.55 C
HETATM 4965 C5 SOG B 402 70.108 -9.022 10.783 1.00142.75 C
HETATM 4966 C6 SOG B 402 70.904 -8.154 11.743 1.00144.24 C
HETATM 4967 S1 SOG B 402 68.289 -12.419 11.748 1.00164.02 S
HETATM 4968 O2 SOG B 402 66.962 -11.256 9.219 1.00155.27 O
HETATM 4969 O3 SOG B 402 67.082 -8.464 8.615 1.00134.53 O
HETATM 4970 O4 SOG B 402 69.658 -7.277 9.183 1.00125.00 O
HETATM 4971 O5 SOG B 402 69.505 -10.073 11.558 1.00152.71 O
HETATM 4972 O6 SOG B 402 72.304 -8.215 11.466 1.00146.73 O
HETATM 4973 S SO4 B 403 67.451 -7.115 -1.878 1.00109.09 S
HETATM 4974 O1 SO4 B 403 68.355 -6.475 -2.835 1.00109.54 O
HETATM 4975 O2 SO4 B 403 66.175 -7.400 -2.540 1.00105.75 O
HETATM 4976 O3 SO4 B 403 67.234 -6.229 -0.729 1.00104.06 O
HETATM 4977 O4 SO4 B 403 68.053 -8.367 -1.416 1.00117.70 O
HETATM 4978 S SO4 B 404 62.823 -15.616 -8.635 1.00173.36 S
HETATM 4979 O1 SO4 B 404 63.637 -14.484 -9.063 1.00170.67 O
HETATM 4980 O2 SO4 B 404 62.398 -16.371 -9.810 1.00172.10 O
HETATM 4981 O3 SO4 B 404 61.649 -15.137 -7.906 1.00172.92 O
HETATM 4982 O4 SO4 B 404 63.625 -16.476 -7.769 1.00174.92 O
HETATM 4983 CAD PGW B 405 46.748 -0.560 11.092 1.00122.77 C
HETATM 4984 OAE PGW B 405 45.495 -0.269 10.479 1.00111.82 O
HETATM 4985 OAF PGW B 405 46.898 1.687 12.005 1.00104.82 O
HETATM 4986 P PGW B 405 50.461 0.560 9.134 1.00146.73 P
HETATM 4987 C01 PGW B 405 52.659 -2.153 12.683 1.00 95.95 C
HETATM 4988 C1 PGW B 405 49.167 -2.343 13.132 1.00 95.67 C
HETATM 4989 O01 PGW B 405 50.401 -1.825 13.263 1.00 96.03 O
HETATM 4990 C02 PGW B 405 51.290 -1.876 12.115 1.00 98.67 C
HETATM 4991 C2 PGW B 405 48.396 -2.382 14.432 1.00 71.94 C
HETATM 4992 O02 PGW B 405 48.771 -2.755 12.072 1.00103.15 O
HETATM 4993 C03 PGW B 405 51.219 -0.551 11.400 1.00117.62 C
HETATM 4994 C3 PGW B 405 48.809 -3.508 15.336 1.00 58.48 C
HETATM 4995 O03 PGW B 405 53.372 -3.073 11.828 1.00109.14 O
HETATM 4996 C04 PGW B 405 48.038 1.276 9.942 1.00135.85 C
HETATM 4997 C4 PGW B 405 47.814 -3.715 16.465 1.00 54.34 C
HETATM 4998 O04 PGW B 405 54.279 -3.952 13.663 1.00123.31 O
HETATM 4999 C05 PGW B 405 47.595 0.686 11.261 1.00123.15 C
HETATM 5000 C5 PGW B 405 48.059 -4.914 17.367 1.00 48.04 C
HETATM 5001 C06 PGW B 405 49.935 -11.009 17.467 1.00 57.23 C
HETATM 5002 C6 PGW B 405 47.867 -6.265 16.711 1.00 48.00 C
HETATM 5003 C07 PGW B 405 50.939 -11.796 18.253 1.00 65.75 C
HETATM 5004 C7 PGW B 405 47.521 -7.403 17.671 1.00 49.58 C
HETATM 5005 C08 PGW B 405 52.384 -11.372 18.035 1.00 61.86 C
HETATM 5006 C8 PGW B 405 48.374 -8.624 17.483 1.00 71.78 C
HETATM 5007 C09 PGW B 405 52.768 -10.124 18.793 1.00 54.88 C
HETATM 5008 C9 PGW B 405 47.882 -9.869 18.160 1.00 75.37 C
HETATM 5009 C10 PGW B 405 48.566 -10.986 18.079 1.00 60.14 C
HETATM 5010 C11 PGW B 405 52.817 -10.297 20.295 1.00 49.14 C
HETATM 5011 O11 PGW B 405 50.601 -0.719 10.096 1.00139.96 O
HETATM 5012 C12 PGW B 405 54.210 -10.303 20.886 1.00 39.55 C
HETATM 5013 O12 PGW B 405 49.472 1.543 9.936 1.00143.69 O
HETATM 5014 C13 PGW B 405 54.951 -8.989 20.782 1.00 31.02 C
HETATM 5015 O13 PGW B 405 51.818 1.201 9.037 1.00137.82 O
HETATM 5016 C14 PGW B 405 56.289 -8.988 21.478 1.00 20.49 C
HETATM 5017 O14 PGW B 405 49.758 0.127 7.879 1.00146.34 O
HETATM 5018 C15 PGW B 405 60.288 -11.768 14.216 1.00 59.81 C
HETATM 5019 C16 PGW B 405 60.645 -13.102 14.823 1.00 68.00 C
HETATM 5020 C17 PGW B 405 60.315 -13.224 16.289 1.00 75.40 C
HETATM 5021 C18 PGW B 405 59.895 -14.616 16.709 1.00 64.92 C
HETATM 5022 C19 PGW B 405 54.221 -3.877 12.464 1.00112.91 C
HETATM 5023 C20 PGW B 405 55.110 -4.655 11.533 1.00 94.35 C
HETATM 5024 C21 PGW B 405 56.400 -5.062 12.191 1.00 73.41 C
HETATM 5025 C22 PGW B 405 56.894 -6.435 11.759 1.00 51.86 C
HETATM 5026 C23 PGW B 405 58.086 -6.937 12.540 1.00 36.85 C
HETATM 5027 C24 PGW B 405 58.717 -8.175 11.958 1.00 51.91 C
HETATM 5028 C25 PGW B 405 58.753 -9.366 12.886 1.00 72.73 C
HETATM 5029 C26 PGW B 405 59.187 -10.648 12.212 1.00 67.28 C
HETATM 5030 C27 PGW B 405 59.256 -11.860 13.113 1.00 59.80 C
HETATM 5031 C28 PGW B 405 59.437 -14.723 18.144 1.00 48.06 C
HETATM 5032 C29 PGW B 405 58.176 -16.092 19.836 1.00 50.85 C
HETATM 5033 C30 PGW B 405 58.602 -15.947 18.398 1.00 42.93 C
HETATM 5034 O HOH A 501 47.886 3.142 34.202 1.00 78.93 O
HETATM 5035 O HOH A 502 50.314 1.816 29.816 1.00 74.44 O
HETATM 5036 O HOH A 503 47.181 6.776 31.608 1.00 54.61 O
HETATM 5037 O HOH A 504 51.952 12.405 44.718 1.00 33.47 O
CONECT 747 1299
CONECT 1299 747
CONECT 2967 3595
CONECT 3595 2967
CONECT 4774 4796 4801 4802 4803
CONECT 4775 4776 4793 4804 4805
CONECT 4776 4775 4777 4794 4806
CONECT 4777 4776 4795 4799
CONECT 4778 4779 4783 4795
CONECT 4779 4778 4780 4807
CONECT 4780 4779 4781 4786
CONECT 4781 4780 4782 4808
CONECT 4782 4781 4783 4784
CONECT 4783 4778 4782 4809
CONECT 4784 4782 4810 4811 4812
CONECT 4785 4787 4791 4796
CONECT 4786 4780 4813 4814 4815
CONECT 4787 4785 4788 4816
CONECT 4788 4787 4789 4817
CONECT 4789 4788 4790 4800
CONECT 4790 4789 4791 4818
CONECT 4791 4785 4790 4819
CONECT 4792 4793 4794 4820 4821
CONECT 4793 4775 4792 4822 4823
CONECT 4794 4776 4792 4800
CONECT 4795 4777 4778 4824
CONECT 4796 4774 4785
CONECT 4797 4800
CONECT 4798 4800
CONECT 4799 4777
CONECT 4800 4789 4794 4797 4798
CONECT 4801 4774
CONECT 4802 4774
CONECT 4803 4774
CONECT 4804 4775
CONECT 4805 4775
CONECT 4806 4776
CONECT 4807 4779
CONECT 4808 4781
CONECT 4809 4783
CONECT 4810 4784
CONECT 4811 4784
CONECT 4812 4784
CONECT 4813 4786
CONECT 4814 4786
CONECT 4815 4786
CONECT 4816 4787
CONECT 4817 4788
CONECT 4818 4790
CONECT 4819 4791
CONECT 4820 4792
CONECT 4821 4792
CONECT 4822 4793
CONECT 4823 4793
CONECT 4824 4795
CONECT 4825 4826 4839 4843
CONECT 4826 4825 4827 4840
CONECT 4827 4826 4828 4841
CONECT 4828 4827 4829 4842
CONECT 4829 4828 4830 4843
CONECT 4830 4829 4844
CONECT 4831 4832 4839
CONECT 4832 4831 4833
CONECT 4833 4832 4834
CONECT 4834 4833 4835
CONECT 4835 4834 4836
CONECT 4836 4835 4837
CONECT 4837 4836 4838
CONECT 4838 4837
CONECT 4839 4825 4831
CONECT 4840 4826
CONECT 4841 4827
CONECT 4842 4828
CONECT 4843 4825 4829
CONECT 4844 4830
CONECT 4845 4846 4859 4863
CONECT 4846 4845 4847 4860
CONECT 4847 4846 4848 4861
CONECT 4848 4847 4849 4862
CONECT 4849 4848 4850 4863
CONECT 4850 4849 4864
CONECT 4851 4852 4859
CONECT 4852 4851 4853
CONECT 4853 4852 4854
CONECT 4854 4853 4855
CONECT 4855 4854 4856
CONECT 4856 4855 4857
CONECT 4857 4856 4858
CONECT 4858 4857
CONECT 4859 4845 4851
CONECT 4860 4846
CONECT 4861 4847
CONECT 4862 4848
CONECT 4863 4845 4849
CONECT 4864 4850
CONECT 4865 4866 4879 4883
CONECT 4866 4865 4867 4880
CONECT 4867 4866 4868 4881
CONECT 4868 4867 4869 4882
CONECT 4869 4868 4870 4883
CONECT 4870 4869 4884
CONECT 4871 4872 4879
CONECT 4872 4871 4873
CONECT 4873 4872 4874
CONECT 4874 4873 4875
CONECT 4875 4874 4876
CONECT 4876 4875 4877
CONECT 4877 4876 4878
CONECT 4878 4877
CONECT 4879 4865 4871
CONECT 4880 4866
CONECT 4881 4867
CONECT 4882 4868
CONECT 4883 4865 4869
CONECT 4884 4870
CONECT 4885 4886 4887 4888 4889
CONECT 4886 4885
CONECT 4887 4885
CONECT 4888 4885
CONECT 4889 4885
CONECT 4890 4891 4906
CONECT 4891 4890
CONECT 4892 4906
CONECT 4893 4918 4920 4922 4924
CONECT 4894 4897 4902
CONECT 4895 4896 4898 4899
CONECT 4896 4895 4897
CONECT 4897 4894 4896 4900
CONECT 4898 4895 4901
CONECT 4899 4895
CONECT 4900 4897 4918
CONECT 4901 4898 4904
CONECT 4902 4894 4929
CONECT 4903 4906 4920
CONECT 4904 4901 4907
CONECT 4905 4929
CONECT 4906 4890 4892 4903
CONECT 4907 4904 4909
CONECT 4908 4910 4916
CONECT 4909 4907 4911
CONECT 4910 4908 4912
CONECT 4911 4909 4913
CONECT 4912 4910 4914
CONECT 4913 4911 4915
CONECT 4914 4912 4917
CONECT 4915 4913 4916
CONECT 4916 4908 4915
CONECT 4917 4914 4919
CONECT 4918 4893 4900
CONECT 4919 4917 4921
CONECT 4920 4893 4903
CONECT 4921 4919 4923
CONECT 4922 4893
CONECT 4923 4921
CONECT 4924 4893
CONECT 4925 4926 4937
CONECT 4926 4925 4927
CONECT 4927 4926 4928
CONECT 4928 4927 4938
CONECT 4929 4902 4905 4930
CONECT 4930 4929 4931
CONECT 4931 4930 4932
CONECT 4932 4931 4933
CONECT 4933 4932 4934
CONECT 4934 4933 4935
CONECT 4935 4934 4936
CONECT 4936 4935 4937
CONECT 4937 4925 4936
CONECT 4938 4928 4940
CONECT 4939 4940
CONECT 4940 4938 4939
CONECT 4941 4942 4955 4959
CONECT 4942 4941 4943 4956
CONECT 4943 4942 4944 4957
CONECT 4944 4943 4945 4958
CONECT 4945 4944 4946 4959
CONECT 4946 4945 4960
CONECT 4947 4948 4955
CONECT 4948 4947 4949
CONECT 4949 4948 4950
CONECT 4950 4949 4951
CONECT 4951 4950 4952
CONECT 4952 4951 4953
CONECT 4953 4952 4954
CONECT 4954 4953
CONECT 4955 4941 4947
CONECT 4956 4942
CONECT 4957 4943
CONECT 4958 4944
CONECT 4959 4941 4945
CONECT 4960 4946
CONECT 4961 4962 4967 4971
CONECT 4962 4961 4963 4968
CONECT 4963 4962 4964 4969
CONECT 4964 4963 4965 4970
CONECT 4965 4964 4966 4971
CONECT 4966 4965 4972
CONECT 4967 4961
CONECT 4968 4962
CONECT 4969 4963
CONECT 4970 4964
CONECT 4971 4961 4965
CONECT 4972 4966
CONECT 4973 4974 4975 4976 4977
CONECT 4974 4973
CONECT 4975 4973
CONECT 4976 4973
CONECT 4977 4973
CONECT 4978 4979 4980 4981 4982
CONECT 4979 4978
CONECT 4980 4978
CONECT 4981 4978
CONECT 4982 4978
CONECT 4983 4984 4999
CONECT 4984 4983
CONECT 4985 4999
CONECT 4986 5011 5013 5015 5017
CONECT 4987 4990 4995
CONECT 4988 4989 4991 4992
CONECT 4989 4988 4990
CONECT 4990 4987 4989 4993
CONECT 4991 4988 4994
CONECT 4992 4988
CONECT 4993 4990 5011
CONECT 4994 4991 4997
CONECT 4995 4987 5022
CONECT 4996 4999 5013
CONECT 4997 4994 5000
CONECT 4998 5022
CONECT 4999 4983 4985 4996
CONECT 5000 4997 5002
CONECT 5001 5003 5009
CONECT 5002 5000 5004
CONECT 5003 5001 5005
CONECT 5004 5002 5006
CONECT 5005 5003 5007
CONECT 5006 5004 5008
CONECT 5007 5005 5010
CONECT 5008 5006 5009
CONECT 5009 5001 5008
CONECT 5010 5007 5012
CONECT 5011 4986 4993
CONECT 5012 5010 5014
CONECT 5013 4986 4996
CONECT 5014 5012 5016
CONECT 5015 4986
CONECT 5016 5014
CONECT 5017 4986
CONECT 5018 5019 5030
CONECT 5019 5018 5020
CONECT 5020 5019 5021
CONECT 5021 5020 5031
CONECT 5022 4995 4998 5023
CONECT 5023 5022 5024
CONECT 5024 5023 5025
CONECT 5025 5024 5026
CONECT 5026 5025 5027
CONECT 5027 5026 5028
CONECT 5028 5027 5029
CONECT 5029 5028 5030
CONECT 5030 5018 5029
CONECT 5031 5021 5033
CONECT 5032 5033
CONECT 5033 5031 5032
MASTER 354 0 11 25 4 0 0 6 5011 2 264 52
END