HEADER MEMBRANE PROTEIN 16-DEC-19 6TQ9
TITLE CRYSTAL STRUCTURE OF THE OREXIN-1 RECEPTOR IN COMPLEX WITH SB-408124
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: SB-408124 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 6TQ9 1 COMPND REMARK HETNAM SITE
REVDAT 3 11-MAR-20 6TQ9 1 JRNL
REVDAT 2 29-JAN-20 6TQ9 1 JRNL
REVDAT 1 01-JAN-20 6TQ9 0
JRNL AUTH M.RAPPAS,A.A.E.ALI,K.A.BENNETT,J.D.BROWN,S.J.BUCKNELL,
JRNL AUTH 2 M.CONGREVE,R.M.COOKE,G.CSEKE,C.DE GRAAF,A.S.DORE,J.C.ERREY,
JRNL AUTH 3 A.JAZAYERI,F.H.MARSHALL,J.S.MASON,R.MOULD,J.C.PATEL,
JRNL AUTH 4 B.G.TEHAN,M.WEIR,J.A.CHRISTOPHER
JRNL TITL COMPARISON OF OREXIN 1 AND OREXIN 2 LIGAND BINDING MODES
JRNL TITL 2 USING X-RAY CRYSTALLOGRAPHY AND COMPUTATIONAL ANALYSIS.
JRNL REF J.MED.CHEM. V. 63 1528 2020
JRNL REFN ISSN 0022-2623
JRNL PMID 31860301
JRNL DOI 10.1021/ACS.JMEDCHEM.9B01787
REMARK 2
REMARK 2 RESOLUTION. 2.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3260
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 58.3
REMARK 3 NUMBER OF REFLECTIONS : 19851
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.710
REMARK 3 FREE R VALUE TEST SET COUNT : 934
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 44.7130 - 5.0770 0.99 4682 204 0.2586 0.2861
REMARK 3 2 5.0770 - 4.0306 1.00 4611 259 0.2069 0.2246
REMARK 3 3 4.0306 - 3.5214 0.86 4016 181 0.2212 0.2896
REMARK 3 4 3.5214 - 3.1995 0.58 2701 127 0.2736 0.3151
REMARK 3 5 3.1995 - 2.9702 0.38 1744 98 0.3108 0.3168
REMARK 3 6 2.9702 - 2.7951 0.19 878 53 0.3072 0.3170
REMARK 3 7 2.7951 - 2.6552 0.06 285 12 0.3370 0.4187
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) : 0.330
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 40.930
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 87.11
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 27:376)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8518 17.3499 -33.5299
REMARK 3 T TENSOR
REMARK 3 T11: 0.2124 T22: 0.3801
REMARK 3 T33: 0.5891 T12: -0.0430
REMARK 3 T13: -0.0256 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 0.5578 L22: 4.3248
REMARK 3 L33: 4.5267 L12: -0.0852
REMARK 3 L13: -0.8729 L23: -2.2012
REMARK 3 S TENSOR
REMARK 3 S11: 0.1237 S12: 0.2707 S13: 0.3262
REMARK 3 S21: -0.1815 S22: 0.4057 S23: 0.9969
REMARK 3 S31: -0.1680 S32: -0.7360 S33: -0.2097
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 45:378)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4294 -4.6156 -8.4910
REMARK 3 T TENSOR
REMARK 3 T11: 0.8240 T22: 0.3420
REMARK 3 T33: 0.1781 T12: -0.0921
REMARK 3 T13: 0.2194 T23: -0.0948
REMARK 3 L TENSOR
REMARK 3 L11: 2.6891 L22: 4.6626
REMARK 3 L33: 2.1118 L12: 1.1483
REMARK 3 L13: 0.0643 L23: -1.5435
REMARK 3 S TENSOR
REMARK 3 S11: 0.0428 S12: -0.5408 S13: -0.0248
REMARK 3 S21: 1.3356 S22: 0.1011 S23: 0.2851
REMARK 3 S31: 0.0205 S32: 0.2963 S33: -0.0223
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 45 THROUGH 376 OR
REMARK 3 RESID 501))
REMARK 3 SELECTION : (CHAIN B AND (RESID 45 THROUGH 189 OR
REMARK 3 RESID 198 THROUGH 244 OR RESID 250
REMARK 3 THROUGH 376 OR RESID 401))
REMARK 3 ATOM PAIRS NUMBER : 2699
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6TQ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-DEC-19.
REMARK 100 THE DEPOSITION ID IS D_1292105895.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-18
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00003
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : STARANISO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19851
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.655
REMARK 200 RESOLUTION RANGE LOW (A) : 44.713
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 58.3
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6TO7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRISODIUM CITRATE 50MM SODIUM
REMARK 280 CHLORIDE 50MM LITHIUM SULPHATE 15-34% PEG400, PH 5.0, 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 73.53350
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 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 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 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 GLY B 379
REMARK 465 LEU B 380
REMARK 465 ALA B 381
REMARK 465 ALA B 382
REMARK 465 ALA B 383
REMARK 465 HIS B 384
REMARK 465 HIS B 385
REMARK 465 HIS B 386
REMARK 465 HIS B 387
REMARK 465 HIS B 388
REMARK 465 HIS B 389
REMARK 465 HIS B 390
REMARK 465 HIS B 391
REMARK 465 HIS B 392
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 103 OH TYR A 348 2.07
REMARK 500 O ARG B 205 O2 SOG B 405 2.10
REMARK 500 O ARG A 205 O3 SOG A 406 2.15
REMARK 500 OD1 ASP A 143 OG SER A 156 2.15
REMARK 500 O GLY A 325 NE ARG A 328 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 39 -58.63 -142.65
REMARK 500 ARG A 78 56.29 -102.84
REMARK 500 LEU A 152 14.90 46.97
REMARK 500 TYR A 224 -64.03 -136.24
REMARK 500 ASP A 332 51.29 -108.84
REMARK 500 ARG B 78 56.53 -102.01
REMARK 500 LEU B 153 -61.76 -131.29
REMARK 500 TYR B 224 -64.77 -137.45
REMARK 500 ASP B 332 41.27 -103.60
REMARK 500 LEU B 377 -63.76 -98.74
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 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6TO7 RELATED DB: PDB
REMARK 900 RELATED ID: 6TOD RELATED DB: PDB
REMARK 900 RELATED ID: 6TOS RELATED DB: PDB
REMARK 900 RELATED ID: 6TOT RELATED DB: PDB
REMARK 900 RELATED ID: 6TP6 RELATED DB: PDB
REMARK 900 RELATED ID: 6TP3 RELATED DB: PDB
REMARK 900 RELATED ID: 6TP4 RELATED DB: PDB
REMARK 900 RELATED ID: 6TQ4 RELATED DB: PDB
REMARK 900 RELATED ID: 6TQ6 RELATED DB: PDB
REMARK 900 RELATED ID: 6TQ7 RELATED DB: PDB
DBREF 6TQ9 A 28 381 UNP O43613 OX1R_HUMAN 28 381
DBREF 6TQ9 B 28 381 UNP O43613 OX1R_HUMAN 28 381
SEQADV 6TQ9 ALA A 25 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 ALA A 26 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 SER A 27 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 ALA A 46 UNP O43613 GLU 46 ENGINEERED MUTATION
SEQADV 6TQ9 LEU A 85 UNP O43613 ILE 85 ENGINEERED MUTATION
SEQADV 6TQ9 ALA A 95 UNP O43613 VAL 95 ENGINEERED MUTATION
SEQADV 6TQ9 LEU A 162 UNP O43613 ARG 162 ENGINEERED MUTATION
SEQADV 6TQ9 ALA A 194 UNP O43613 ASN 194 ENGINEERED MUTATION
SEQADV 6TQ9 ALA A 198 UNP O43613 LEU 198 ENGINEERED MUTATION
SEQADV 6TQ9 ALA A 211 UNP O43613 TYR 211 ENGINEERED MUTATION
SEQADV 6TQ9 A UNP O43613 ALA 253 DELETION
SEQADV 6TQ9 A UNP O43613 LEU 254 DELETION
SEQADV 6TQ9 A UNP O43613 VAL 255 DELETION
SEQADV 6TQ9 A UNP O43613 ARG 256 DELETION
SEQADV 6TQ9 A UNP O43613 ASN 257 DELETION
SEQADV 6TQ9 A UNP O43613 TRP 258 DELETION
SEQADV 6TQ9 A UNP O43613 LYS 259 DELETION
SEQADV 6TQ9 A UNP O43613 ARG 260 DELETION
SEQADV 6TQ9 A UNP O43613 PRO 261 DELETION
SEQADV 6TQ9 A UNP O43613 SER 262 DELETION
SEQADV 6TQ9 A UNP O43613 ASP 263 DELETION
SEQADV 6TQ9 A UNP O43613 GLN 264 DELETION
SEQADV 6TQ9 A UNP O43613 LEU 265 DELETION
SEQADV 6TQ9 A UNP O43613 GLY 266 DELETION
SEQADV 6TQ9 A UNP O43613 ASP 267 DELETION
SEQADV 6TQ9 A UNP O43613 LEU 268 DELETION
SEQADV 6TQ9 A UNP O43613 GLU 269 DELETION
SEQADV 6TQ9 A UNP O43613 GLN 270 DELETION
SEQADV 6TQ9 A UNP O43613 GLY 271 DELETION
SEQADV 6TQ9 A UNP O43613 LEU 272 DELETION
SEQADV 6TQ9 A UNP O43613 SER 273 DELETION
SEQADV 6TQ9 A UNP O43613 GLY 274 DELETION
SEQADV 6TQ9 A UNP O43613 GLU 275 DELETION
SEQADV 6TQ9 A UNP O43613 PRO 276 DELETION
SEQADV 6TQ9 A UNP O43613 GLN 277 DELETION
SEQADV 6TQ9 A UNP O43613 PRO 278 DELETION
SEQADV 6TQ9 A UNP O43613 ARG 279 DELETION
SEQADV 6TQ9 A UNP O43613 ALA 280 DELETION
SEQADV 6TQ9 A UNP O43613 ARG 281 DELETION
SEQADV 6TQ9 A UNP O43613 ALA 282 DELETION
SEQADV 6TQ9 A UNP O43613 PHE 283 DELETION
SEQADV 6TQ9 A UNP O43613 LEU 284 DELETION
SEQADV 6TQ9 VAL A 304 UNP O43613 LEU 304 ENGINEERED MUTATION
SEQADV 6TQ9 ALA A 339 UNP O43613 CYS 339 ENGINEERED MUTATION
SEQADV 6TQ9 TRP A 375 UNP O43613 CYS 375 ENGINEERED MUTATION
SEQADV 6TQ9 TRP A 376 UNP O43613 CYS 376 ENGINEERED MUTATION
SEQADV 6TQ9 ALA A 381 UNP O43613 GLY 381 CONFLICT
SEQADV 6TQ9 ALA A 382 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 ALA A 383 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS A 384 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS A 385 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS A 386 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS A 387 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS A 388 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS A 389 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS A 390 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS A 391 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS A 392 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 ALA B 25 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 ALA B 26 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 SER B 27 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 ALA B 46 UNP O43613 GLU 46 ENGINEERED MUTATION
SEQADV 6TQ9 LEU B 85 UNP O43613 ILE 85 ENGINEERED MUTATION
SEQADV 6TQ9 ALA B 95 UNP O43613 VAL 95 ENGINEERED MUTATION
SEQADV 6TQ9 LEU B 162 UNP O43613 ARG 162 ENGINEERED MUTATION
SEQADV 6TQ9 ALA B 194 UNP O43613 ASN 194 ENGINEERED MUTATION
SEQADV 6TQ9 ALA B 198 UNP O43613 LEU 198 ENGINEERED MUTATION
SEQADV 6TQ9 ALA B 211 UNP O43613 TYR 211 ENGINEERED MUTATION
SEQADV 6TQ9 B UNP O43613 ALA 253 DELETION
SEQADV 6TQ9 B UNP O43613 LEU 254 DELETION
SEQADV 6TQ9 B UNP O43613 VAL 255 DELETION
SEQADV 6TQ9 B UNP O43613 ARG 256 DELETION
SEQADV 6TQ9 B UNP O43613 ASN 257 DELETION
SEQADV 6TQ9 B UNP O43613 TRP 258 DELETION
SEQADV 6TQ9 B UNP O43613 LYS 259 DELETION
SEQADV 6TQ9 B UNP O43613 ARG 260 DELETION
SEQADV 6TQ9 B UNP O43613 PRO 261 DELETION
SEQADV 6TQ9 B UNP O43613 SER 262 DELETION
SEQADV 6TQ9 B UNP O43613 ASP 263 DELETION
SEQADV 6TQ9 B UNP O43613 GLN 264 DELETION
SEQADV 6TQ9 B UNP O43613 LEU 265 DELETION
SEQADV 6TQ9 B UNP O43613 GLY 266 DELETION
SEQADV 6TQ9 B UNP O43613 ASP 267 DELETION
SEQADV 6TQ9 B UNP O43613 LEU 268 DELETION
SEQADV 6TQ9 B UNP O43613 GLU 269 DELETION
SEQADV 6TQ9 B UNP O43613 GLN 270 DELETION
SEQADV 6TQ9 B UNP O43613 GLY 271 DELETION
SEQADV 6TQ9 B UNP O43613 LEU 272 DELETION
SEQADV 6TQ9 B UNP O43613 SER 273 DELETION
SEQADV 6TQ9 B UNP O43613 GLY 274 DELETION
SEQADV 6TQ9 B UNP O43613 GLU 275 DELETION
SEQADV 6TQ9 B UNP O43613 PRO 276 DELETION
SEQADV 6TQ9 B UNP O43613 GLN 277 DELETION
SEQADV 6TQ9 B UNP O43613 PRO 278 DELETION
SEQADV 6TQ9 B UNP O43613 ARG 279 DELETION
SEQADV 6TQ9 B UNP O43613 ALA 280 DELETION
SEQADV 6TQ9 B UNP O43613 ARG 281 DELETION
SEQADV 6TQ9 B UNP O43613 ALA 282 DELETION
SEQADV 6TQ9 B UNP O43613 PHE 283 DELETION
SEQADV 6TQ9 B UNP O43613 LEU 284 DELETION
SEQADV 6TQ9 VAL B 304 UNP O43613 LEU 304 ENGINEERED MUTATION
SEQADV 6TQ9 ALA B 339 UNP O43613 CYS 339 ENGINEERED MUTATION
SEQADV 6TQ9 TRP B 375 UNP O43613 CYS 375 ENGINEERED MUTATION
SEQADV 6TQ9 TRP B 376 UNP O43613 CYS 376 ENGINEERED MUTATION
SEQADV 6TQ9 ALA B 381 UNP O43613 GLY 381 CONFLICT
SEQADV 6TQ9 ALA B 382 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 ALA B 383 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS B 384 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS B 385 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS B 386 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS B 387 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS B 388 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS B 389 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS B 390 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 HIS B 391 UNP O43613 EXPRESSION TAG
SEQADV 6TQ9 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 NVN A 401 44
HET NVN A 402 44
HET SOG A 403 20
HET SOG A 404 20
HET SOG A 405 20
HET SOG A 406 20
HET SOG A 407 20
HET SO4 A 408 5
HET SO4 A 409 5
HET PGW A 410 51
HET PGW A 411 51
HET NVN B 401 44
HET SOG B 402 20
HET SOG B 403 20
HET SOG B 404 9
HET SOG B 405 20
HET SOG B 406 20
HET SO4 B 407 5
HETNAM NVN 1-[6,8-BIS(FLUORANYL)-2-METHYL-QUINOLIN-4-YL]-3-[4-
HETNAM 2 NVN (DIMETHYLAMINO)PHENYL]UREA
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 NVN 3(C19 H18 F2 N4 O)
FORMUL 5 SOG 10(C14 H28 O5 S)
FORMUL 10 SO4 3(O4 S 2-)
FORMUL 12 PGW 2(C40 H77 O10 P)
FORMUL 21 HOH *16(H2 O)
HELIX 1 AA1 SER A 27 TYR A 39 1 13
HELIX 2 AA2 TYR A 39 ASN A 74 1 36
HELIX 3 AA3 HIS A 75 ARG A 78 5 4
HELIX 4 AA4 THR A 79 ILE A 98 1 20
HELIX 5 AA5 ILE A 98 GLU A 110 1 13
HELIX 6 AA6 PHE A 114 CYS A 149 1 36
HELIX 7 AA7 THR A 157 MET A 176 1 20
HELIX 8 AA8 MET A 176 VAL A 182 1 7
HELIX 9 AA9 ASP A 209 TYR A 224 1 16
HELIX 10 AB1 TYR A 224 TRP A 243 1 20
HELIX 11 AB2 THR A 251 VAL A 323 1 41
HELIX 12 AB3 ASP A 332 SER A 362 1 31
HELIX 13 AB4 SER A 362 TRP A 376 1 15
HELIX 14 AB5 ALA B 46 ASN B 74 1 29
HELIX 15 AB6 HIS B 75 ARG B 78 5 4
HELIX 16 AB7 THR B 79 ILE B 98 1 20
HELIX 17 AB8 ILE B 98 GLU B 110 1 13
HELIX 18 AB9 PHE B 114 HIS B 150 1 37
HELIX 19 AC1 THR B 157 MET B 176 1 20
HELIX 20 AC2 MET B 176 VAL B 182 1 7
HELIX 21 AC3 LEU B 189 ARG B 195 5 7
HELIX 22 AC4 LEU B 210 TYR B 224 1 15
HELIX 23 AC5 TYR B 224 TRP B 243 1 20
HELIX 24 AC6 THR B 251 VAL B 323 1 41
HELIX 25 AC7 GLN B 329 SER B 331 5 3
HELIX 26 AC8 ASP B 332 SER B 362 1 31
HELIX 27 AC9 SER B 362 LEU B 377 1 16
SHEET 1 AA1 2 MET A 183 SER A 186 0
SHEET 2 AA1 2 VAL A 201 GLU A 204 -1 O VAL A 201 N SER A 186
SHEET 1 AA2 2 MET B 183 SER B 187 0
SHEET 2 AA2 2 SER B 200 GLU B 204 -1 O ASP B 203 N GLU B 184
SSBOND 1 CYS A 119 CYS A 202 1555 1555 2.04
SSBOND 2 CYS B 119 CYS B 202 1555 1555 2.04
CRYST1 60.365 147.067 72.536 90.00 111.09 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 0.016566 0.000000 0.006389 0.00000
SCALE2 0.000000 0.006800 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014776 0.00000
ATOM 1 N SER A 27 28.529 38.275 -64.800 1.00141.93 N
ANISOU 1 N SER A 27 21474 15077 17374 -264 5772 2906 N
ATOM 2 CA SER A 27 28.070 39.653 -64.946 1.00145.50 C
ANISOU 2 CA SER A 27 22173 15313 17796 -412 5728 2865 C
ATOM 3 C SER A 27 26.555 39.765 -64.999 1.00142.98 C
ANISOU 3 C SER A 27 22257 14808 17261 -261 5455 2689 C
ATOM 4 O SER A 27 25.875 39.749 -63.975 1.00136.14 O
ANISOU 4 O SER A 27 21262 13995 16469 -392 5199 2578 O
ATOM 5 CB SER A 27 28.657 40.287 -66.211 1.00152.29 C
ANISOU 5 CB SER A 27 23299 16003 18562 -303 6033 2988 C
ATOM 6 OG SER A 27 30.000 40.693 -66.018 1.00159.21 O
ANISOU 6 OG SER A 27 23783 17029 19682 -557 6254 3171 O
ATOM 7 N GLU A 28 26.044 39.876 -66.227 1.00141.56 N
ANISOU 7 N GLU A 28 22564 14415 16808 20 5510 2675 N
ATOM 8 CA GLU A 28 24.643 40.221 -66.435 1.00132.37 C
ANISOU 8 CA GLU A 28 21790 13074 15431 155 5248 2549 C
ATOM 9 C GLU A 28 23.710 39.159 -65.871 1.00128.80 C
ANISOU 9 C GLU A 28 21305 12727 14905 256 4942 2438 C
ATOM 10 O GLU A 28 22.638 39.485 -65.350 1.00120.09 O
ANISOU 10 O GLU A 28 20276 11574 13777 231 4670 2349 O
ATOM 11 CB GLU A 28 24.396 40.433 -67.927 1.00126.47 C
ANISOU 11 CB GLU A 28 21548 12113 14391 434 5357 2571 C
ATOM 12 CG GLU A 28 22.958 40.655 -68.357 1.00122.03 C
ANISOU 12 CG GLU A 28 21397 11401 13569 619 5065 2473 C
ATOM 13 CD GLU A 28 22.873 41.013 -69.828 1.00128.56 C
ANISOU 13 CD GLU A 28 22703 12023 14121 852 5192 2505 C
ATOM 14 OE1 GLU A 28 23.944 41.156 -70.454 1.00132.79 O
ANISOU 14 OE1 GLU A 28 23254 12512 14688 861 5534 2600 O
ATOM 15 OE2 GLU A 28 21.751 41.151 -70.359 1.00132.00 O
ANISOU 15 OE2 GLU A 28 23488 12352 14315 1022 4948 2449 O
ATOM 16 N ASP A 29 24.105 37.887 -65.944 1.00131.59 N
ANISOU 16 N ASP A 29 21547 13224 15228 375 4987 2452 N
ATOM 17 CA ASP A 29 23.287 36.823 -65.382 1.00131.27 C
ANISOU 17 CA ASP A 29 21470 13287 15118 450 4703 2350 C
ATOM 18 C ASP A 29 23.674 36.489 -63.949 1.00132.50 C
ANISOU 18 C ASP A 29 21115 13667 15563 209 4654 2338 C
ATOM 19 O ASP A 29 22.847 35.945 -63.205 1.00128.65 O
ANISOU 19 O ASP A 29 20566 13244 15070 198 4388 2242 O
ATOM 20 CB ASP A 29 23.367 35.574 -66.272 1.00138.00 C
ANISOU 20 CB ASP A 29 22563 14140 15730 730 4746 2344 C
ATOM 21 CG ASP A 29 22.386 34.492 -65.856 1.00139.90 C
ANISOU 21 CG ASP A 29 22861 14453 15842 811 4416 2231 C
ATOM 22 OD1 ASP A 29 22.715 33.703 -64.945 1.00137.48 O
ANISOU 22 OD1 ASP A 29 22215 14333 15688 732 4404 2219 O
ATOM 23 OD2 ASP A 29 21.279 34.439 -66.433 1.00141.76 O
ANISOU 23 OD2 ASP A 29 23469 14569 15825 942 4149 2160 O
ATOM 24 N GLU A 30 24.909 36.800 -63.547 1.00134.73 N
ANISOU 24 N GLU A 30 21020 14077 16094 5 4886 2439 N
ATOM 25 CA GLU A 30 25.291 36.647 -62.149 1.00127.21 C
ANISOU 25 CA GLU A 30 19570 13344 15420 -270 4805 2424 C
ATOM 26 C GLU A 30 24.533 37.617 -61.252 1.00112.08 C
ANISOU 26 C GLU A 30 17640 11342 13603 -499 4589 2322 C
ATOM 27 O GLU A 30 24.223 37.281 -60.103 1.00100.17 O
ANISOU 27 O GLU A 30 15879 9953 12226 -641 4403 2238 O
ATOM 28 CB GLU A 30 26.795 36.844 -62.000 1.00132.91 C
ANISOU 28 CB GLU A 30 19888 14239 16373 -457 5058 2579 C
ATOM 29 CG GLU A 30 27.307 36.736 -60.578 1.00132.42 C
ANISOU 29 CG GLU A 30 19289 14431 16593 -773 4946 2577 C
ATOM 30 CD GLU A 30 28.794 36.990 -60.477 1.00142.73 C
ANISOU 30 CD GLU A 30 20181 15935 18116 -980 5149 2761 C
ATOM 31 OE1 GLU A 30 29.380 37.476 -61.467 1.00147.99 O
ANISOU 31 OE1 GLU A 30 20989 16504 18735 -915 5392 2887 O
ATOM 32 OE2 GLU A 30 29.375 36.700 -59.408 1.00145.48 O
ANISOU 32 OE2 GLU A 30 20057 16544 18676 -1212 5053 2787 O
ATOM 33 N PHE A 31 24.213 38.813 -61.756 1.00109.46 N
ANISOU 33 N PHE A 31 17597 10790 13202 -518 4617 2322 N
ATOM 34 CA PHE A 31 23.335 39.701 -61.006 1.00100.78 C
ANISOU 34 CA PHE A 31 16573 9567 12152 -655 4414 2217 C
ATOM 35 C PHE A 31 21.984 39.040 -60.780 1.00 93.70 C
ANISOU 35 C PHE A 31 15835 8644 11122 -458 4132 2113 C
ATOM 36 O PHE A 31 21.430 39.090 -59.678 1.00 84.12 O
ANISOU 36 O PHE A 31 14470 7460 10030 -585 3943 2021 O
ATOM 37 CB PHE A 31 23.171 41.032 -61.754 1.00107.00 C
ANISOU 37 CB PHE A 31 17702 10108 12844 -636 4511 2245 C
ATOM 38 CG PHE A 31 21.986 41.868 -61.301 1.00104.41 C
ANISOU 38 CG PHE A 31 17586 9607 12477 -627 4304 2144 C
ATOM 39 CD1 PHE A 31 22.177 43.002 -60.522 1.00 97.67 C
ANISOU 39 CD1 PHE A 31 16666 8670 11774 -899 4316 2105 C
ATOM 40 CD2 PHE A 31 20.690 41.544 -61.687 1.00103.71 C
ANISOU 40 CD2 PHE A 31 17774 9439 12193 -337 4093 2101 C
ATOM 41 CE1 PHE A 31 21.102 43.783 -60.118 1.00 95.03 C
ANISOU 41 CE1 PHE A 31 16548 8165 11396 -846 4162 2019 C
ATOM 42 CE2 PHE A 31 19.617 42.309 -61.283 1.00 99.51 C
ANISOU 42 CE2 PHE A 31 17398 8769 11644 -290 3919 2041 C
ATOM 43 CZ PHE A 31 19.820 43.433 -60.500 1.00 96.18 C
ANISOU 43 CZ PHE A 31 16922 8251 11371 -525 3976 1998 C
ATOM 44 N LEU A 32 21.443 38.404 -61.821 1.00104.81 N
ANISOU 44 N LEU A 32 17555 9996 12273 -154 4083 2130 N
ATOM 45 CA LEU A 32 20.101 37.839 -61.730 1.00109.00 C
ANISOU 45 CA LEU A 32 18256 10502 12658 25 3768 2057 C
ATOM 46 C LEU A 32 20.060 36.694 -60.729 1.00112.09 C
ANISOU 46 C LEU A 32 18343 11086 13158 -43 3643 2000 C
ATOM 47 O LEU A 32 19.061 36.505 -60.023 1.00114.67 O
ANISOU 47 O LEU A 32 18645 11413 13511 -36 3382 1930 O
ATOM 48 CB LEU A 32 19.647 37.382 -63.118 1.00110.26 C
ANISOU 48 CB LEU A 32 18819 10577 12500 322 3713 2087 C
ATOM 49 CG LEU A 32 20.019 38.368 -64.237 1.00117.52 C
ANISOU 49 CG LEU A 32 20022 11324 13306 392 3922 2155 C
ATOM 50 CD1 LEU A 32 20.136 37.661 -65.579 1.00124.02 C
ANISOU 50 CD1 LEU A 32 21171 12105 13848 636 3979 2183 C
ATOM 51 CD2 LEU A 32 19.007 39.500 -64.313 1.00117.32 C
ANISOU 51 CD2 LEU A 32 20211 11134 13230 437 3761 2144 C
ATOM 52 N ARG A 33 21.155 35.934 -60.640 1.00113.48 N
ANISOU 52 N ARG A 33 18272 11433 13414 -98 3835 2041 N
ATOM 53 CA ARG A 33 21.264 34.884 -59.632 1.00108.91 C
ANISOU 53 CA ARG A 33 17368 11056 12955 -175 3752 1993 C
ATOM 54 C ARG A 33 21.443 35.477 -58.240 1.00101.82 C
ANISOU 54 C ARG A 33 16107 10232 12349 -488 3707 1936 C
ATOM 55 O ARG A 33 20.772 35.067 -57.286 1.00 85.81 O
ANISOU 55 O ARG A 33 13912 8290 10401 -530 3457 1808 O
ATOM 56 CB ARG A 33 22.427 33.954 -59.978 1.00112.58 C
ANISOU 56 CB ARG A 33 17662 11691 13423 -106 3985 2071 C
ATOM 57 CG ARG A 33 22.255 33.239 -61.304 1.00118.05 C
ANISOU 57 CG ARG A 33 18754 12293 13806 207 4023 2095 C
ATOM 58 CD ARG A 33 23.267 32.115 -61.463 1.00125.34 C
ANISOU 58 CD ARG A 33 19509 13379 14734 320 4230 2154 C
ATOM 59 NE ARG A 33 23.503 31.757 -62.862 1.00135.04 N
ANISOU 59 NE ARG A 33 21121 14478 15708 588 4382 2196 N
ATOM 60 CZ ARG A 33 24.688 31.848 -63.459 1.00138.71 C
ANISOU 60 CZ ARG A 33 21508 14960 16235 651 4714 2319 C
ATOM 61 NH1 ARG A 33 25.733 32.276 -62.771 1.00137.41 N
ANISOU 61 NH1 ARG A 33 20865 14969 16376 444 4888 2424 N
ATOM 62 NH2 ARG A 33 24.835 31.504 -64.733 1.00139.44 N
ANISOU 62 NH2 ARG A 33 21997 14899 16087 910 4856 2342 N
ATOM 63 N TYR A 34 22.341 36.456 -58.108 1.00112.44 N
ANISOU 63 N TYR A 34 17295 11574 13854 -708 3876 1983 N
ATOM 64 CA TYR A 34 22.582 37.075 -56.810 1.00110.24 C
ANISOU 64 CA TYR A 34 16710 11354 13821 -1039 3801 1914 C
ATOM 65 C TYR A 34 21.377 37.858 -56.318 1.00 92.95 C
ANISOU 65 C TYR A 34 14740 8964 11613 -1052 3601 1800 C
ATOM 66 O TYR A 34 21.229 38.053 -55.106 1.00 85.50 O
ANISOU 66 O TYR A 34 13599 8058 10828 -1261 3472 1696 O
ATOM 67 CB TYR A 34 23.812 37.973 -56.887 1.00126.14 C
ANISOU 67 CB TYR A 34 18553 13401 15972 -1285 3988 2008 C
ATOM 68 CG TYR A 34 24.335 38.464 -55.556 1.00140.23 C
ANISOU 68 CG TYR A 34 19989 15299 17994 -1668 3885 1954 C
ATOM 69 CD1 TYR A 34 24.881 37.582 -54.635 1.00144.69 C
ANISOU 69 CD1 TYR A 34 20125 16139 18713 -1799 3806 1944 C
ATOM 70 CD2 TYR A 34 24.332 39.818 -55.246 1.00153.06 C
ANISOU 70 CD2 TYR A 34 21734 16756 19665 -1896 3856 1918 C
ATOM 71 CE1 TYR A 34 25.385 38.030 -53.431 1.00153.22 C
ANISOU 71 CE1 TYR A 34 20906 17331 19982 -2159 3667 1898 C
ATOM 72 CE2 TYR A 34 24.836 40.277 -54.043 1.00159.68 C
ANISOU 72 CE2 TYR A 34 22305 17684 20680 -2260 3729 1867 C
ATOM 73 CZ TYR A 34 25.363 39.376 -53.140 1.00160.94 C
ANISOU 73 CZ TYR A 34 22039 18127 20986 -2396 3619 1859 C
ATOM 74 OH TYR A 34 25.870 39.809 -51.935 1.00165.64 O
ANISOU 74 OH TYR A 34 22383 18819 21732 -2759 3448 1815 O
ATOM 75 N LEU A 35 20.519 38.318 -57.229 1.00 88.23 N
ANISOU 75 N LEU A 35 14545 8159 10821 -816 3567 1821 N
ATOM 76 CA LEU A 35 19.270 38.920 -56.794 1.00 88.20 C
ANISOU 76 CA LEU A 35 14725 7990 10797 -748 3368 1742 C
ATOM 77 C LEU A 35 18.357 37.885 -56.143 1.00 84.09 C
ANISOU 77 C LEU A 35 14048 7613 10290 -627 3077 1632 C
ATOM 78 O LEU A 35 17.539 38.228 -55.281 1.00 77.77 O
ANISOU 78 O LEU A 35 13191 6783 9575 -639 2893 1528 O
ATOM 79 CB LEU A 35 18.574 39.591 -57.980 1.00 92.61 C
ANISOU 79 CB LEU A 35 15696 8350 11143 -491 3364 1808 C
ATOM 80 CG LEU A 35 17.146 40.090 -57.747 1.00 92.02 C
ANISOU 80 CG LEU A 35 15810 8132 11022 -317 3144 1774 C
ATOM 81 CD1 LEU A 35 17.100 41.086 -56.598 1.00 95.03 C
ANISOU 81 CD1 LEU A 35 16102 8427 11579 -522 3160 1685 C
ATOM 82 CD2 LEU A 35 16.532 40.688 -59.017 1.00 92.79 C
ANISOU 82 CD2 LEU A 35 16279 8078 10898 -51 3127 1863 C
ATOM 83 N TRP A 36 18.475 36.614 -56.542 1.00 85.35 N
ANISOU 83 N TRP A 36 14117 7952 10360 -490 3012 1632 N
ATOM 84 CA TRP A 36 17.478 35.626 -56.136 1.00 75.26 C
ANISOU 84 CA TRP A 36 12720 6820 9055 -342 2682 1513 C
ATOM 85 C TRP A 36 17.635 35.210 -54.672 1.00 79.91 C
ANISOU 85 C TRP A 36 12894 7603 9867 -530 2567 1369 C
ATOM 86 O TRP A 36 16.642 35.136 -53.930 1.00 94.79 O
ANISOU 86 O TRP A 36 14690 9515 11810 -487 2326 1263 O
ATOM 87 CB TRP A 36 17.551 34.406 -57.059 1.00 69.79 C
ANISOU 87 CB TRP A 36 12147 6213 8157 -150 2654 1555 C
ATOM 88 CG TRP A 36 16.888 33.183 -56.508 1.00 71.40 C
ANISOU 88 CG TRP A 36 12164 6606 8360 -82 2360 1431 C
ATOM 89 CD1 TRP A 36 17.485 32.165 -55.819 1.00 73.97 C
ANISOU 89 CD1 TRP A 36 12185 7140 8778 -160 2367 1358 C
ATOM 90 CD2 TRP A 36 15.501 32.840 -56.604 1.00 72.21 C
ANISOU 90 CD2 TRP A 36 12365 6706 8367 71 2015 1384 C
ATOM 91 NE1 TRP A 36 16.556 31.211 -55.483 1.00 71.83 N
ANISOU 91 NE1 TRP A 36 11853 6976 8463 -70 2061 1252 N
ATOM 92 CE2 TRP A 36 15.330 31.602 -55.953 1.00 74.60 C
ANISOU 92 CE2 TRP A 36 12429 7208 8707 56 1836 1271 C
ATOM 93 CE3 TRP A 36 14.387 33.459 -57.178 1.00 78.82 C
ANISOU 93 CE3 TRP A 36 13450 7403 9096 218 1838 1448 C
ATOM 94 CZ2 TRP A 36 14.089 30.973 -55.861 1.00 84.32 C
ANISOU 94 CZ2 TRP A 36 13660 8497 9878 152 1487 1218 C
ATOM 95 CZ3 TRP A 36 13.156 32.835 -57.086 1.00 82.93 C
ANISOU 95 CZ3 TRP A 36 13934 8006 9569 325 1478 1413 C
ATOM 96 CH2 TRP A 36 13.017 31.604 -56.432 1.00 87.53 C
ANISOU 96 CH2 TRP A 36 14274 8785 10199 276 1306 1297 C
ATOM 97 N ARG A 37 18.866 34.923 -54.239 1.00 71.02 N
ANISOU 97 N ARG A 37 11502 6618 8864 -731 2739 1384 N
ATOM 98 CA ARG A 37 19.115 34.481 -52.873 1.00 72.69 C
ANISOU 98 CA ARG A 37 11331 7023 9266 -915 2624 1261 C
ATOM 99 C ARG A 37 19.140 35.611 -51.844 1.00 76.51 C
ANISOU 99 C ARG A 37 11761 7403 9908 -1174 2621 1198 C
ATOM 100 O ARG A 37 18.841 35.358 -50.674 1.00 74.01 O
ANISOU 100 O ARG A 37 11238 7182 9701 -1267 2449 1065 O
ATOM 101 CB ARG A 37 20.427 33.702 -52.824 1.00 76.03 C
ANISOU 101 CB ARG A 37 11474 7659 9757 -1012 2793 1334 C
ATOM 102 CG ARG A 37 21.699 34.519 -53.061 1.00 78.05 C
ANISOU 102 CG ARG A 37 11669 7878 10107 -1241 3093 1490 C
ATOM 103 CD ARG A 37 22.918 33.632 -52.887 1.00 79.78 C
ANISOU 103 CD ARG A 37 11527 8360 10424 -1304 3237 1589 C
ATOM 104 NE ARG A 37 24.166 34.322 -53.179 1.00101.63 N
ANISOU 104 NE ARG A 37 14179 11132 13302 -1522 3533 1782 N
ATOM 105 CZ ARG A 37 25.364 33.752 -53.125 1.00113.65 C
ANISOU 105 CZ ARG A 37 15340 12913 14931 -1563 3654 1910 C
ATOM 106 NH1 ARG A 37 25.485 32.473 -52.790 1.00115.67 N
ANISOU 106 NH1 ARG A 37 15380 13373 15196 -1423 3634 1908 N
ATOM 107 NH2 ARG A 37 26.441 34.467 -53.409 1.00114.62 N
ANISOU 107 NH2 ARG A 37 15310 13097 15143 -1732 3782 2049 N
ATOM 108 N ASP A 38 19.471 36.848 -52.230 1.00 79.59 N
ANISOU 108 N ASP A 38 12373 7576 10293 -1297 2811 1285 N
ATOM 109 CA ASP A 38 19.477 37.947 -51.272 1.00 82.21 C
ANISOU 109 CA ASP A 38 12742 7760 10734 -1555 2815 1220 C
ATOM 110 C ASP A 38 18.144 38.666 -51.159 1.00 70.98 C
ANISOU 110 C ASP A 38 11613 6112 9246 -1374 2710 1161 C
ATOM 111 O ASP A 38 17.955 39.406 -50.194 1.00 59.13 O
ANISOU 111 O ASP A 38 10168 4483 7816 -1537 2690 1078 O
ATOM 112 CB ASP A 38 20.547 38.987 -51.629 1.00 87.43 C
ANISOU 112 CB ASP A 38 13497 8295 11427 -1818 3064 1339 C
ATOM 113 CG ASP A 38 21.955 38.467 -51.461 1.00 93.22 C
ANISOU 113 CG ASP A 38 13839 9299 12283 -2039 3136 1410 C
ATOM 114 OD1 ASP A 38 22.110 37.253 -51.224 1.00 96.75 O
ANISOU 114 OD1 ASP A 38 14025 9965 12772 -1977 3093 1407 O
ATOM 115 OD2 ASP A 38 22.913 39.265 -51.576 1.00101.65 O
ANISOU 115 OD2 ASP A 38 14844 10373 13403 -2260 3225 1485 O
ATOM 116 N TYR A 39 17.214 38.465 -52.091 1.00 71.06 N
ANISOU 116 N TYR A 39 11819 6066 9114 -1041 2640 1215 N
ATOM 117 CA TYR A 39 15.944 39.178 -52.020 1.00 77.91 C
ANISOU 117 CA TYR A 39 12925 6740 9936 -839 2551 1208 C
ATOM 118 C TYR A 39 14.808 38.277 -52.469 1.00 80.26 C
ANISOU 118 C TYR A 39 13182 7163 10151 -516 2306 1217 C
ATOM 119 O TYR A 39 13.873 38.012 -51.707 1.00 81.75 O
ANISOU 119 O TYR A 39 13239 7413 10408 -418 2121 1143 O
ATOM 120 CB TYR A 39 15.983 40.446 -52.877 1.00 82.10 C
ANISOU 120 CB TYR A 39 13857 6975 10363 -801 2761 1338 C
ATOM 121 CG TYR A 39 14.644 41.120 -53.042 1.00 81.50 C
ANISOU 121 CG TYR A 39 14038 6711 10217 -510 2685 1384 C
ATOM 122 CD1 TYR A 39 13.953 41.602 -51.940 1.00 86.54 C
ANISOU 122 CD1 TYR A 39 14674 7259 10947 -503 2636 1304 C
ATOM 123 CD2 TYR A 39 14.071 41.276 -54.300 1.00 79.92 C
ANISOU 123 CD2 TYR A 39 14092 6422 9851 -228 2670 1528 C
ATOM 124 CE1 TYR A 39 12.727 42.223 -52.077 1.00 87.78 C
ANISOU 124 CE1 TYR A 39 15039 7257 11058 -198 2599 1385 C
ATOM 125 CE2 TYR A 39 12.834 41.901 -54.451 1.00 85.38 C
ANISOU 125 CE2 TYR A 39 14982 6968 10493 59 2590 1609 C
ATOM 126 CZ TYR A 39 12.168 42.371 -53.331 1.00 86.03 C
ANISOU 126 CZ TYR A 39 15017 6977 10692 84 2568 1546 C
ATOM 127 OH TYR A 39 10.944 42.994 -53.448 1.00 82.07 O
ANISOU 127 OH TYR A 39 14647 6377 10158 402 2505 1644 O
ATOM 128 N LEU A 40 14.888 37.780 -53.704 1.00 80.93 N
ANISOU 128 N LEU A 40 13389 7282 10079 -363 2304 1316 N
ATOM 129 CA LEU A 40 13.761 37.041 -54.265 1.00 74.18 C
ANISOU 129 CA LEU A 40 12567 6509 9109 -88 2042 1347 C
ATOM 130 C LEU A 40 13.475 35.774 -53.467 1.00 71.09 C
ANISOU 130 C LEU A 40 11839 6371 8801 -109 1819 1222 C
ATOM 131 O LEU A 40 12.340 35.546 -53.036 1.00 73.69 O
ANISOU 131 O LEU A 40 12068 6756 9175 19 1594 1198 O
ATOM 132 CB LEU A 40 14.032 36.719 -55.736 1.00 75.63 C
ANISOU 132 CB LEU A 40 13013 6656 9068 42 2089 1468 C
ATOM 133 CG LEU A 40 14.076 37.965 -56.624 1.00 81.03 C
ANISOU 133 CG LEU A 40 14077 7073 9640 117 2279 1609 C
ATOM 134 CD1 LEU A 40 14.676 37.623 -57.965 1.00 90.67 C
ANISOU 134 CD1 LEU A 40 15558 8249 10641 192 2404 1717 C
ATOM 135 CD2 LEU A 40 12.682 38.532 -56.797 1.00 70.15 C
ANISOU 135 CD2 LEU A 40 12847 5591 8215 359 2085 1684 C
ATOM 136 N TYR A 41 14.484 34.937 -53.247 1.00 70.34 N
ANISOU 136 N TYR A 41 11555 6434 8735 -259 1891 1160 N
ATOM 137 CA TYR A 41 14.269 33.776 -52.381 1.00 65.42 C
ANISOU 137 CA TYR A 41 10628 6035 8195 -289 1702 1037 C
ATOM 138 C TYR A 41 13.863 34.142 -50.968 1.00 71.74 C
ANISOU 138 C TYR A 41 11224 6849 9185 -391 1639 926 C
ATOM 139 O TYR A 41 12.872 33.578 -50.469 1.00 63.62 O
ANISOU 139 O TYR A 41 10063 5913 8196 -288 1421 872 O
ATOM 140 CB TYR A 41 15.531 32.895 -52.357 1.00 60.98 C
ANISOU 140 CB TYR A 41 9903 5632 7636 -413 1833 1015 C
ATOM 141 CG TYR A 41 15.409 31.744 -51.401 1.00 67.36 C
ANISOU 141 CG TYR A 41 10413 6654 8527 -449 1666 889 C
ATOM 142 CD1 TYR A 41 14.874 30.530 -51.810 1.00 73.72 C
ANISOU 142 CD1 TYR A 41 11245 7560 9203 -301 1485 870 C
ATOM 143 CD2 TYR A 41 15.824 31.871 -50.087 1.00 69.61 C
ANISOU 143 CD2 TYR A 41 10429 7023 8998 -645 1683 790 C
ATOM 144 CE1 TYR A 41 14.761 29.471 -50.940 1.00 77.91 C
ANISOU 144 CE1 TYR A 41 11531 8270 9801 -334 1348 758 C
ATOM 145 CE2 TYR A 41 15.718 30.815 -49.200 1.00 77.95 C
ANISOU 145 CE2 TYR A 41 11232 8267 10119 -668 1538 680 C
ATOM 146 CZ TYR A 41 15.188 29.618 -49.632 1.00 80.65 C
ANISOU 146 CZ TYR A 41 11595 8706 10343 -506 1383 665 C
ATOM 147 OH TYR A 41 15.085 28.572 -48.749 1.00 73.35 O
ANISOU 147 OH TYR A 41 10443 7950 9475 -530 1255 559 O
ATOM 148 N PRO A 42 14.552 35.051 -50.277 1.00 78.43 N
ANISOU 148 N PRO A 42 12059 7598 10142 -601 1815 895 N
ATOM 149 CA PRO A 42 14.176 35.348 -48.889 1.00 70.71 C
ANISOU 149 CA PRO A 42 10951 6610 9308 -700 1759 779 C
ATOM 150 C PRO A 42 12.758 35.862 -48.758 1.00 70.68 C
ANISOU 150 C PRO A 42 11067 6482 9308 -475 1660 808 C
ATOM 151 O PRO A 42 12.092 35.580 -47.752 1.00 80.25 O
ANISOU 151 O PRO A 42 12124 7753 10616 -445 1551 725 O
ATOM 152 CB PRO A 42 15.211 36.423 -48.469 1.00 69.83 C
ANISOU 152 CB PRO A 42 10929 6351 9254 -986 1975 774 C
ATOM 153 CG PRO A 42 16.397 36.156 -49.355 1.00 74.17 C
ANISOU 153 CG PRO A 42 11449 6977 9754 -1085 2118 866 C
ATOM 154 CD PRO A 42 15.786 35.749 -50.674 1.00 82.39 C
ANISOU 154 CD PRO A 42 12659 8006 10637 -791 2072 964 C
ATOM 155 N LYS A 43 12.276 36.601 -49.756 1.00 68.85 N
ANISOU 155 N LYS A 43 11101 6082 8976 -298 1708 943 N
ATOM 156 CA LYS A 43 10.907 37.103 -49.722 1.00 70.20 C
ANISOU 156 CA LYS A 43 11359 6156 9159 -42 1621 1021 C
ATOM 157 C LYS A 43 9.907 35.998 -50.044 1.00 64.10 C
ANISOU 157 C LYS A 43 10398 5588 8367 152 1336 1060 C
ATOM 158 O LYS A 43 8.935 35.787 -49.306 1.00 68.52 O
ANISOU 158 O LYS A 43 10786 6216 9034 261 1213 1051 O
ATOM 159 CB LYS A 43 10.750 38.272 -50.693 1.00 75.49 C
ANISOU 159 CB LYS A 43 12381 6581 9720 92 1762 1173 C
ATOM 160 CG LYS A 43 11.112 39.614 -50.097 1.00 65.93 C
ANISOU 160 CG LYS A 43 11404 5099 8549 -28 2016 1154 C
ATOM 161 CD LYS A 43 10.298 40.715 -50.737 1.00 74.86 C
ANISOU 161 CD LYS A 43 12852 5990 9602 238 2102 1320 C
ATOM 162 CE LYS A 43 10.339 41.972 -49.896 1.00 95.61 C
ANISOU 162 CE LYS A 43 15734 8326 12269 169 2338 1290 C
ATOM 163 NZ LYS A 43 9.682 43.117 -50.580 1.00109.36 N
ANISOU 163 NZ LYS A 43 17835 9801 13916 437 2473 1467 N
ATOM 164 N GLN A 44 10.157 35.253 -51.121 1.00 67.22 N
ANISOU 164 N GLN A 44 10839 6080 8620 180 1236 1107 N
ATOM 165 CA GLN A 44 9.295 34.142 -51.494 1.00 75.30 C
ANISOU 165 CA GLN A 44 11735 7284 9590 304 940 1139 C
ATOM 166 C GLN A 44 9.261 33.055 -50.433 1.00 84.12 C
ANISOU 166 C GLN A 44 12536 8601 10824 196 825 995 C
ATOM 167 O GLN A 44 8.255 32.346 -50.324 1.00 85.46 O
ANISOU 167 O GLN A 44 12551 8902 11019 288 582 1021 O
ATOM 168 CB GLN A 44 9.781 33.548 -52.817 1.00 88.98 C
ANISOU 168 CB GLN A 44 13669 9036 11104 318 896 1194 C
ATOM 169 CG GLN A 44 8.793 32.611 -53.474 1.00 98.96 C
ANISOU 169 CG GLN A 44 14931 10421 12248 439 564 1264 C
ATOM 170 CD GLN A 44 9.214 32.202 -54.864 1.00 98.73 C
ANISOU 170 CD GLN A 44 15219 10343 11950 472 538 1332 C
ATOM 171 OE1 GLN A 44 9.624 33.034 -55.672 1.00 96.61 O
ANISOU 171 OE1 GLN A 44 15231 9906 11572 529 709 1423 O
ATOM 172 NE2 GLN A 44 9.122 30.908 -55.151 1.00 99.66 N
ANISOU 172 NE2 GLN A 44 15337 10587 11943 438 342 1287 N
ATOM 173 N TYR A 45 10.333 32.915 -49.652 1.00 85.96 N
ANISOU 173 N TYR A 45 12666 8867 11129 -8 984 859 N
ATOM 174 CA TYR A 45 10.377 31.958 -48.555 1.00 77.45 C
ANISOU 174 CA TYR A 45 11308 7963 10158 -110 897 721 C
ATOM 175 C TYR A 45 9.547 32.447 -47.373 1.00 70.72 C
ANISOU 175 C TYR A 45 10334 7071 9467 -71 889 687 C
ATOM 176 O TYR A 45 8.771 31.678 -46.801 1.00 73.16 O
ANISOU 176 O TYR A 45 10439 7513 9847 -18 725 655 O
ATOM 177 CB TYR A 45 11.840 31.721 -48.158 1.00 79.92 C
ANISOU 177 CB TYR A 45 11549 8328 10487 -331 1065 623 C
ATOM 178 CG TYR A 45 12.067 30.885 -46.909 1.00 79.03 C
ANISOU 178 CG TYR A 45 11167 8378 10483 -452 1006 482 C
ATOM 179 CD1 TYR A 45 12.071 29.495 -46.969 1.00 80.10 C
ANISOU 179 CD1 TYR A 45 11171 8696 10568 -429 869 437 C
ATOM 180 CD2 TYR A 45 12.314 31.482 -45.673 1.00 83.83 C
ANISOU 180 CD2 TYR A 45 11697 8936 11218 -597 1093 393 C
ATOM 181 CE1 TYR A 45 12.284 28.734 -45.842 1.00 80.41 C
ANISOU 181 CE1 TYR A 45 10984 8874 10695 -524 824 317 C
ATOM 182 CE2 TYR A 45 12.531 30.713 -44.536 1.00 77.21 C
ANISOU 182 CE2 TYR A 45 10637 8241 10457 -703 1030 270 C
ATOM 183 CZ TYR A 45 12.513 29.341 -44.633 1.00 71.78 C
ANISOU 183 CZ TYR A 45 9797 7744 9731 -656 899 236 C
ATOM 184 OH TYR A 45 12.721 28.541 -43.532 1.00 83.66 O
ANISOU 184 OH TYR A 45 11098 9387 11301 -743 841 122 O
ATOM 185 N ALA A 46 9.715 33.717 -46.979 1.00 68.23 N
ANISOU 185 N ALA A 46 10169 6556 9201 -99 1086 696 N
ATOM 186 CA ALA A 46 8.969 34.243 -45.840 1.00 66.70 C
ANISOU 186 CA ALA A 46 9931 6279 9132 -38 1131 669 C
ATOM 187 C ALA A 46 7.474 34.303 -46.114 1.00 76.77 C
ANISOU 187 C ALA A 46 11153 7568 10448 249 1003 820 C
ATOM 188 O ALA A 46 6.670 34.115 -45.192 1.00 86.93 O
ANISOU 188 O ALA A 46 12276 8900 11855 334 972 810 O
ATOM 189 CB ALA A 46 9.479 35.640 -45.471 1.00 57.37 C
ANISOU 189 CB ALA A 46 9015 4832 7950 -131 1382 656 C
ATOM 190 N TRP A 47 7.086 34.568 -47.366 1.00 73.86 N
ANISOU 190 N TRP A 47 10914 7168 9983 403 931 980 N
ATOM 191 CA TRP A 47 5.667 34.610 -47.693 1.00 78.03 C
ANISOU 191 CA TRP A 47 11349 7743 10555 669 770 1165 C
ATOM 192 C TRP A 47 5.046 33.240 -47.483 1.00 83.52 C
ANISOU 192 C TRP A 47 11733 8697 11304 651 498 1147 C
ATOM 193 O TRP A 47 3.989 33.103 -46.857 1.00 96.18 O
ANISOU 193 O TRP A 47 13118 10377 13049 781 426 1223 O
ATOM 194 CB TRP A 47 5.456 35.059 -49.133 1.00 91.67 C
ANISOU 194 CB TRP A 47 13288 9405 12138 810 700 1342 C
ATOM 195 CG TRP A 47 4.002 35.112 -49.467 1.00112.44 C
ANISOU 195 CG TRP A 47 15784 12113 14824 1074 502 1566 C
ATOM 196 CD1 TRP A 47 3.172 36.180 -49.315 1.00119.63 C
ANISOU 196 CD1 TRP A 47 16742 12895 15818 1330 619 1742 C
ATOM 197 CD2 TRP A 47 3.175 34.019 -49.891 1.00129.13 C
ANISOU 197 CD2 TRP A 47 17664 14466 16934 1099 152 1655 C
ATOM 198 NE1 TRP A 47 1.893 35.843 -49.688 1.00127.14 N
ANISOU 198 NE1 TRP A 47 17462 14016 16830 1530 358 1962 N
ATOM 199 CE2 TRP A 47 1.867 34.518 -50.037 1.00132.98 C
ANISOU 199 CE2 TRP A 47 18025 14984 17517 1365 50 1908 C
ATOM 200 CE3 TRP A 47 3.422 32.674 -50.186 1.00139.57 C
ANISOU 200 CE3 TRP A 47 18894 15968 18168 919 -83 1557 C
ATOM 201 CZ2 TRP A 47 0.806 33.719 -50.470 1.00138.53 C
ANISOU 201 CZ2 TRP A 47 18476 15914 18246 1417 -313 2074 C
ATOM 202 CZ3 TRP A 47 2.370 31.883 -50.613 1.00143.08 C
ANISOU 202 CZ3 TRP A 47 19153 16600 18611 961 -433 1697 C
ATOM 203 CH2 TRP A 47 1.079 32.407 -50.752 1.00141.05 C
ANISOU 203 CH2 TRP A 47 18736 16393 18465 1189 -563 1956 C
ATOM 204 N VAL A 48 5.687 32.208 -48.034 1.00 80.83 N
ANISOU 204 N VAL A 48 11387 8481 10843 497 361 1062 N
ATOM 205 CA VAL A 48 5.165 30.853 -47.909 1.00 74.74 C
ANISOU 205 CA VAL A 48 10384 7927 10086 451 101 1036 C
ATOM 206 C VAL A 48 5.070 30.461 -46.442 1.00 70.72 C
ANISOU 206 C VAL A 48 9636 7488 9746 381 167 906 C
ATOM 207 O VAL A 48 4.152 29.732 -46.045 1.00 73.44 O
ANISOU 207 O VAL A 48 9743 7977 10183 417 -7 946 O
ATOM 208 CB VAL A 48 6.031 29.869 -48.711 1.00 69.60 C
ANISOU 208 CB VAL A 48 9857 7344 9245 307 12 953 C
ATOM 209 CG1 VAL A 48 5.508 28.452 -48.556 1.00 52.60 C
ANISOU 209 CG1 VAL A 48 7524 5380 7081 240 -248 916 C
ATOM 210 CG2 VAL A 48 6.090 30.279 -50.173 1.00 65.55 C
ANISOU 210 CG2 VAL A 48 9630 6736 8538 390 -38 1088 C
ATOM 211 N LEU A 49 6.002 30.935 -45.610 1.00 66.84 N
ANISOU 211 N LEU A 49 9210 6894 9291 265 407 761 N
ATOM 212 CA LEU A 49 5.957 30.599 -44.190 1.00 63.02 C
ANISOU 212 CA LEU A 49 8551 6456 8937 196 469 634 C
ATOM 213 C LEU A 49 4.721 31.189 -43.517 1.00 65.13 C
ANISOU 213 C LEU A 49 8723 6667 9355 396 521 747 C
ATOM 214 O LEU A 49 3.988 30.476 -42.824 1.00 71.59 O
ANISOU 214 O LEU A 49 9307 7613 10282 430 432 749 O
ATOM 215 CB LEU A 49 7.228 31.090 -43.510 1.00 62.87 C
ANISOU 215 CB LEU A 49 8657 6328 8901 8 684 477 C
ATOM 216 CG LEU A 49 7.315 30.864 -41.999 1.00 62.15 C
ANISOU 216 CG LEU A 49 8455 6250 8908 -85 755 336 C
ATOM 217 CD1 LEU A 49 7.022 29.411 -41.626 1.00 59.18 C
ANISOU 217 CD1 LEU A 49 7829 6095 8562 -115 574 273 C
ATOM 218 CD2 LEU A 49 8.692 31.276 -41.534 1.00 58.22 C
ANISOU 218 CD2 LEU A 49 8082 5675 8365 -322 900 205 C
ATOM 219 N ILE A 50 4.476 32.491 -43.707 1.00 61.60 N
ANISOU 219 N ILE A 50 8465 6022 8916 546 690 859 N
ATOM 220 CA ILE A 50 3.291 33.115 -43.124 1.00 61.17 C
ANISOU 220 CA ILE A 50 8342 5899 9001 794 788 1006 C
ATOM 221 C ILE A 50 2.016 32.604 -43.791 1.00 70.87 C
ANISOU 221 C ILE A 50 9310 7314 10301 978 541 1231 C
ATOM 222 O ILE A 50 0.958 32.534 -43.152 1.00 78.27 O
ANISOU 222 O ILE A 50 10025 8316 11400 1145 553 1353 O
ATOM 223 CB ILE A 50 3.390 34.652 -43.199 1.00 46.98 C
ANISOU 223 CB ILE A 50 6868 3814 7169 925 1055 1078 C
ATOM 224 CG1 ILE A 50 4.766 35.134 -42.723 1.00 46.13 C
ANISOU 224 CG1 ILE A 50 7032 3531 6966 663 1243 866 C
ATOM 225 CG2 ILE A 50 2.275 35.295 -42.378 1.00 51.95 C
ANISOU 225 CG2 ILE A 50 7465 4339 7936 1203 1234 1217 C
ATOM 226 CD1 ILE A 50 5.029 36.623 -42.950 1.00 48.44 C
ANISOU 226 CD1 ILE A 50 7708 3513 7185 724 1492 923 C
ATOM 227 N ALA A 51 2.081 32.248 -45.075 1.00 67.97 N
ANISOU 227 N ALA A 51 8974 7038 9815 946 313 1307 N
ATOM 228 CA ALA A 51 0.882 31.770 -45.756 1.00 69.59 C
ANISOU 228 CA ALA A 51 8949 7425 10067 1075 25 1535 C
ATOM 229 C ALA A 51 0.423 30.437 -45.177 1.00 71.21 C
ANISOU 229 C ALA A 51 8840 7854 10365 951 -172 1485 C
ATOM 230 O ALA A 51 -0.750 30.273 -44.822 1.00 72.78 O
ANISOU 230 O ALA A 51 8745 8175 10734 1082 -257 1664 O
ATOM 231 CB ALA A 51 1.130 31.668 -47.261 1.00 68.93 C
ANISOU 231 CB ALA A 51 9046 7357 9785 1039 -186 1609 C
ATOM 232 N ALA A 52 1.331 29.462 -45.084 1.00 74.27 N
ANISOU 232 N ALA A 52 9278 8297 10643 705 -236 1262 N
ATOM 233 CA ALA A 52 0.951 28.160 -44.544 1.00 68.15 C
ANISOU 233 CA ALA A 52 8254 7709 9931 577 -411 1203 C
ATOM 234 C ALA A 52 0.488 28.266 -43.093 1.00 67.44 C
ANISOU 234 C ALA A 52 7963 7617 10046 648 -219 1177 C
ATOM 235 O ALA A 52 -0.378 27.495 -42.658 1.00 77.18 O
ANISOU 235 O ALA A 52 8915 9005 11404 641 -351 1251 O
ATOM 236 CB ALA A 52 2.115 27.181 -44.675 1.00 63.45 C
ANISOU 236 CB ALA A 52 7799 7141 9166 341 -456 973 C
ATOM 237 N TYR A 53 1.064 29.195 -42.327 1.00 63.21 N
ANISOU 237 N TYR A 53 7592 6892 9531 700 94 1076 N
ATOM 238 CA TYR A 53 0.694 29.331 -40.924 1.00 61.14 C
ANISOU 238 CA TYR A 53 7225 6586 9421 771 303 1037 C
ATOM 239 C TYR A 53 -0.682 29.971 -40.752 1.00 72.05 C
ANISOU 239 C TYR A 53 8426 7965 10984 1066 380 1311 C
ATOM 240 O TYR A 53 -1.484 29.495 -39.940 1.00 83.53 O
ANISOU 240 O TYR A 53 9625 9517 12597 1130 403 1378 O
ATOM 241 CB TYR A 53 1.769 30.126 -40.184 1.00 56.50 C
ANISOU 241 CB TYR A 53 6932 5776 8762 700 586 843 C
ATOM 242 CG TYR A 53 2.773 29.243 -39.481 1.00 66.22 C
ANISOU 242 CG TYR A 53 8172 7064 9925 447 568 591 C
ATOM 243 CD1 TYR A 53 2.648 28.956 -38.131 1.00 77.42 C
ANISOU 243 CD1 TYR A 53 9529 8468 11419 427 688 490 C
ATOM 244 CD2 TYR A 53 3.839 28.690 -40.172 1.00 72.37 C
ANISOU 244 CD2 TYR A 53 9028 7909 10559 250 444 473 C
ATOM 245 CE1 TYR A 53 3.561 28.150 -37.484 1.00 76.61 C
ANISOU 245 CE1 TYR A 53 9433 8427 11248 211 658 278 C
ATOM 246 CE2 TYR A 53 4.757 27.884 -39.535 1.00 75.64 C
ANISOU 246 CE2 TYR A 53 9428 8392 10921 52 436 276 C
ATOM 247 CZ TYR A 53 4.612 27.617 -38.188 1.00 72.35 C
ANISOU 247 CZ TYR A 53 8939 7970 10580 30 528 180 C
ATOM 248 OH TYR A 53 5.510 26.817 -37.523 1.00 68.13 O
ANISOU 248 OH TYR A 53 8387 7510 9988 -152 508 0 O
ATOM 249 N VAL A 54 -0.977 31.037 -41.505 1.00 74.75 N
ANISOU 249 N VAL A 54 8889 8200 11311 1263 437 1493 N
ATOM 250 CA VAL A 54 -2.300 31.656 -41.418 1.00 72.36 C
ANISOU 250 CA VAL A 54 8391 7914 11188 1588 518 1801 C
ATOM 251 C VAL A 54 -3.380 30.688 -41.890 1.00 71.81 C
ANISOU 251 C VAL A 54 7899 8144 11243 1584 178 2017 C
ATOM 252 O VAL A 54 -4.462 30.611 -41.297 1.00 70.32 O
ANISOU 252 O VAL A 54 7395 8056 11266 1759 235 2222 O
ATOM 253 CB VAL A 54 -2.337 32.983 -42.207 1.00 66.76 C
ANISOU 253 CB VAL A 54 7927 7023 10414 1809 639 1961 C
ATOM 254 CG1 VAL A 54 -3.707 33.656 -42.085 1.00 64.97 C
ANISOU 254 CG1 VAL A 54 7488 6815 10382 2196 757 2315 C
ATOM 255 CG2 VAL A 54 -1.229 33.923 -41.743 1.00 72.04 C
ANISOU 255 CG2 VAL A 54 9041 7381 10949 1751 958 1742 C
ATOM 256 N ALA A 55 -3.102 29.913 -42.944 1.00 64.54 N
ANISOU 256 N ALA A 55 6975 7362 10185 1372 -173 1983 N
ATOM 257 CA ALA A 55 -4.082 28.933 -43.405 1.00 60.83 C
ANISOU 257 CA ALA A 55 6149 7163 9800 1298 -540 2174 C
ATOM 258 C ALA A 55 -4.368 27.899 -42.321 1.00 76.11 C
ANISOU 258 C ALA A 55 7829 9221 11869 1167 -534 2086 C
ATOM 259 O ALA A 55 -5.532 27.603 -42.021 1.00 93.35 O
ANISOU 259 O ALA A 55 9630 11576 14264 1252 -613 2326 O
ATOM 260 CB ALA A 55 -3.610 28.261 -44.694 1.00 57.82 C
ANISOU 260 CB ALA A 55 5929 6852 9187 1068 -899 2113 C
ATOM 261 N VAL A 56 -3.313 27.320 -41.742 1.00 76.11 N
ANISOU 261 N VAL A 56 8021 9146 11750 957 -443 1762 N
ATOM 262 CA VAL A 56 -3.495 26.340 -40.678 1.00 69.91 C
ANISOU 262 CA VAL A 56 7044 8453 11065 836 -417 1659 C
ATOM 263 C VAL A 56 -4.169 26.992 -39.477 1.00 77.45 C
ANISOU 263 C VAL A 56 7853 9339 12237 1084 -81 1768 C
ATOM 264 O VAL A 56 -5.081 26.419 -38.870 1.00 82.88 O
ANISOU 264 O VAL A 56 8215 10167 13111 1110 -95 1903 O
ATOM 265 CB VAL A 56 -2.142 25.706 -40.301 1.00 62.22 C
ANISOU 265 CB VAL A 56 6332 7401 9908 601 -365 1306 C
ATOM 266 CG1 VAL A 56 -2.249 24.986 -38.960 1.00 74.81 C
ANISOU 266 CG1 VAL A 56 7791 9029 11605 539 -238 1190 C
ATOM 267 CG2 VAL A 56 -1.671 24.767 -41.396 1.00 50.88 C
ANISOU 267 CG2 VAL A 56 5002 6057 8273 372 -688 1232 C
ATOM 268 N PHE A 57 -3.716 28.195 -39.103 1.00 77.11 N
ANISOU 268 N PHE A 57 8079 9060 12160 1263 246 1715 N
ATOM 269 CA PHE A 57 -4.324 28.898 -37.975 1.00 81.05 C
ANISOU 269 CA PHE A 57 8537 9438 12822 1528 610 1818 C
ATOM 270 C PHE A 57 -5.826 29.079 -38.170 1.00 87.34 C
ANISOU 270 C PHE A 57 8931 10392 13861 1794 582 2220 C
ATOM 271 O PHE A 57 -6.620 28.760 -37.280 1.00 89.47 O
ANISOU 271 O PHE A 57 8938 10735 14323 1900 722 2341 O
ATOM 272 CB PHE A 57 -3.635 30.246 -37.760 1.00 75.21 C
ANISOU 272 CB PHE A 57 8220 8389 11968 1666 931 1723 C
ATOM 273 CG PHE A 57 -4.147 31.007 -36.569 1.00 60.72 C
ANISOU 273 CG PHE A 57 6466 6365 10241 1938 1343 1798 C
ATOM 274 CD1 PHE A 57 -3.762 30.669 -35.275 1.00 56.04 C
ANISOU 274 CD1 PHE A 57 5999 5671 9622 1844 1536 1584 C
ATOM 275 CD2 PHE A 57 -5.026 32.062 -36.743 1.00 54.66 C
ANISOU 275 CD2 PHE A 57 5677 5506 9585 2310 1552 2098 C
ATOM 276 CE1 PHE A 57 -4.244 31.377 -34.174 1.00 51.64 C
ANISOU 276 CE1 PHE A 57 5585 4904 9130 2106 1939 1653 C
ATOM 277 CE2 PHE A 57 -5.503 32.761 -35.659 1.00 59.26 C
ANISOU 277 CE2 PHE A 57 6386 5885 10245 2592 1972 2179 C
ATOM 278 CZ PHE A 57 -5.108 32.416 -34.372 1.00 59.12 C
ANISOU 278 CZ PHE A 57 6533 5747 10182 2483 2169 1949 C
ATOM 279 N VAL A 58 -6.235 29.586 -39.335 1.00 84.89 N
ANISOU 279 N VAL A 58 8557 10147 13551 1911 404 2451 N
ATOM 280 CA VAL A 58 -7.653 29.840 -39.589 1.00 79.34 C
ANISOU 280 CA VAL A 58 7439 9618 13089 2182 359 2881 C
ATOM 281 C VAL A 58 -8.422 28.525 -39.716 1.00 73.51 C
ANISOU 281 C VAL A 58 6239 9202 12489 1970 1 3012 C
ATOM 282 O VAL A 58 -9.382 28.271 -38.978 1.00 74.04 O
ANISOU 282 O VAL A 58 6053 9388 12689 2008 123 3131 O
ATOM 283 CB VAL A 58 -7.819 30.732 -40.837 1.00 79.97 C
ANISOU 283 CB VAL A 58 7601 9680 13103 2352 233 3093 C
ATOM 284 CG1 VAL A 58 -9.291 30.842 -41.246 1.00 85.40 C
ANISOU 284 CG1 VAL A 58 7886 10623 13941 2502 96 3473 C
ATOM 285 CG2 VAL A 58 -7.214 32.093 -40.585 1.00 80.58 C
ANISOU 285 CG2 VAL A 58 8128 9418 13072 2586 638 3004 C
ATOM 286 N VAL A 59 -7.998 27.660 -40.642 1.00 62.46 N
ANISOU 286 N VAL A 59 4884 7925 10923 1637 -419 2890 N
ATOM 287 CA VAL A 59 -8.737 26.423 -40.884 1.00 59.07 C
ANISOU 287 CA VAL A 59 4076 7779 10590 1394 -800 3021 C
ATOM 288 C VAL A 59 -8.784 25.566 -39.620 1.00 72.34 C
ANISOU 288 C VAL A 59 5654 9479 12353 1262 -631 2858 C
ATOM 289 O VAL A 59 -9.851 25.082 -39.221 1.00 70.35 O
ANISOU 289 O VAL A 59 5148 9386 12196 1203 -640 2991 O
ATOM 290 CB VAL A 59 -8.130 25.661 -42.076 1.00 57.73 C
ANISOU 290 CB VAL A 59 4115 7664 10154 1056 -1238 2869 C
ATOM 291 CG1 VAL A 59 -8.641 24.227 -42.095 1.00 59.80 C
ANISOU 291 CG1 VAL A 59 4138 8143 10442 722 -1579 2884 C
ATOM 292 CG2 VAL A 59 -8.463 26.373 -43.362 1.00 60.43 C
ANISOU 292 CG2 VAL A 59 4483 8047 10433 1175 -1466 3112 C
ATOM 293 N ALA A 60 -7.635 25.374 -38.964 1.00 76.23 N
ANISOU 293 N ALA A 60 6478 9785 12700 1160 -440 2495 N
ATOM 294 CA ALA A 60 -7.621 24.610 -37.718 1.00 68.87 C
ANISOU 294 CA ALA A 60 5469 8852 11845 1068 -268 2350 C
ATOM 295 C ALA A 60 -8.547 25.235 -36.683 1.00 62.52 C
ANISOU 295 C ALA A 60 4478 8017 11260 1372 111 2554 C
ATOM 296 O ALA A 60 -9.216 24.522 -35.926 1.00 60.29 O
ANISOU 296 O ALA A 60 4037 7830 11040 1281 161 2576 O
ATOM 297 CB ALA A 60 -6.198 24.505 -37.171 1.00 67.09 C
ANISOU 297 CB ALA A 60 5684 8417 11389 937 -101 1932 C
ATOM 298 N LEU A 61 -8.589 26.569 -36.624 1.00 72.83 N
ANISOU 298 N LEU A 61 5935 9152 12584 1698 405 2656 N
ATOM 299 CA LEU A 61 -9.489 27.239 -35.693 1.00 82.30 C
ANISOU 299 CA LEU A 61 7108 10290 13871 1956 788 2812 C
ATOM 300 C LEU A 61 -10.942 27.062 -36.120 1.00 90.76 C
ANISOU 300 C LEU A 61 7803 11620 15061 1968 624 3149 C
ATOM 301 O LEU A 61 -11.788 26.650 -35.317 1.00 85.78 O
ANISOU 301 O LEU A 61 6990 11069 14535 1969 754 3254 O
ATOM 302 CB LEU A 61 -9.128 28.718 -35.593 1.00 86.40 C
ANISOU 302 CB LEU A 61 7968 10535 14326 2273 1137 2817 C
ATOM 303 CG LEU A 61 -7.847 29.010 -34.808 1.00 93.18 C
ANISOU 303 CG LEU A 61 9254 11081 15068 2273 1409 2487 C
ATOM 304 CD1 LEU A 61 -7.713 30.490 -34.494 1.00102.54 C
ANISOU 304 CD1 LEU A 61 10843 11967 16149 2554 1799 2498 C
ATOM 305 CD2 LEU A 61 -7.814 28.183 -33.536 1.00 88.75 C
ANISOU 305 CD2 LEU A 61 8682 10515 14526 2149 1550 2320 C
ATOM 306 N VAL A 62 -11.254 27.379 -37.381 1.00 99.55 N
ANISOU 306 N VAL A 62 8808 12858 16160 1978 341 3334 N
ATOM 307 CA VAL A 62 -12.613 27.171 -37.871 1.00 94.46 C
ANISOU 307 CA VAL A 62 7796 12469 15628 1956 145 3656 C
ATOM 308 C VAL A 62 -12.958 25.686 -37.863 1.00 95.22 C
ANISOU 308 C VAL A 62 7671 12766 15743 1584 -177 3614 C
ATOM 309 O VAL A 62 -14.100 25.299 -37.591 1.00 96.38 O
ANISOU 309 O VAL A 62 7522 13073 16023 1551 -191 3832 O
ATOM 310 CB VAL A 62 -12.781 27.784 -39.273 1.00 77.72 C
ANISOU 310 CB VAL A 62 5649 10428 13451 2019 -125 3835 C
ATOM 311 CG1 VAL A 62 -14.038 27.236 -39.931 1.00 75.94 C
ANISOU 311 CG1 VAL A 62 5040 10497 13316 1872 -457 4121 C
ATOM 312 CG2 VAL A 62 -12.832 29.288 -39.187 1.00 73.56 C
ANISOU 312 CG2 VAL A 62 5300 9721 12928 2424 242 3955 C
ATOM 313 N GLY A 63 -11.982 24.834 -38.167 1.00 94.75 N
ANISOU 313 N GLY A 63 7770 12686 15543 1297 -429 3341 N
ATOM 314 CA GLY A 63 -12.226 23.407 -38.257 1.00100.49 C
ANISOU 314 CA GLY A 63 8380 13569 16232 925 -741 3273 C
ATOM 315 C GLY A 63 -12.700 22.816 -36.948 1.00100.05 C
ANISOU 315 C GLY A 63 8215 13513 16287 909 -493 3249 C
ATOM 316 O GLY A 63 -13.809 22.285 -36.864 1.00106.93 O
ANISOU 316 O GLY A 63 8818 14546 17265 816 -585 3453 O
ATOM 317 N ASN A 64 -11.860 22.897 -35.913 1.00 92.00 N
ANISOU 317 N ASN A 64 7411 12304 15240 994 -180 3006 N
ATOM 318 CA ASN A 64 -12.207 22.280 -34.637 1.00 80.93 C
ANISOU 318 CA ASN A 64 5962 10880 13910 972 51 2956 C
ATOM 319 C ASN A 64 -13.434 22.932 -34.003 1.00 74.02 C
ANISOU 319 C ASN A 64 4879 10029 13217 1244 350 3265 C
ATOM 320 O ASN A 64 -14.189 22.262 -33.290 1.00 81.05 O
ANISOU 320 O ASN A 64 5601 10991 14203 1180 420 3354 O
ATOM 321 CB ASN A 64 -11.012 22.336 -33.682 1.00 81.06 C
ANISOU 321 CB ASN A 64 6288 10673 13839 1019 326 2634 C
ATOM 322 CG ASN A 64 -9.822 21.536 -34.187 1.00 81.32 C
ANISOU 322 CG ASN A 64 6496 10695 13706 734 49 2340 C
ATOM 323 OD1 ASN A 64 -9.835 20.304 -34.177 1.00 82.40 O
ANISOU 323 OD1 ASN A 64 6606 10926 13774 450 -166 2237 O
ATOM 324 ND2 ASN A 64 -8.787 22.236 -34.638 1.00 76.58 N
ANISOU 324 ND2 ASN A 64 6096 9966 13034 814 68 2211 N
ATOM 325 N THR A 65 -13.651 24.232 -34.233 1.00 76.25 N
ANISOU 325 N THR A 65 5187 10241 13544 1556 549 3439 N
ATOM 326 CA THR A 65 -14.840 24.890 -33.690 1.00 89.73 C
ANISOU 326 CA THR A 65 6709 11971 15414 1832 847 3762 C
ATOM 327 C THR A 65 -16.116 24.270 -34.252 1.00102.62 C
ANISOU 327 C THR A 65 7917 13886 17190 1685 563 4074 C
ATOM 328 O THR A 65 -17.051 23.954 -33.502 1.00103.38 O
ANISOU 328 O THR A 65 7802 14047 17432 1725 723 4263 O
ATOM 329 CB THR A 65 -14.785 26.393 -33.986 1.00 81.75 C
ANISOU 329 CB THR A 65 5847 10829 14387 2181 1088 3885 C
ATOM 330 OG1 THR A 65 -13.635 26.968 -33.351 1.00 79.31 O
ANISOU 330 OG1 THR A 65 5968 10229 13937 2301 1379 3595 O
ATOM 331 CG2 THR A 65 -16.045 27.090 -33.482 1.00 79.74 C
ANISOU 331 CG2 THR A 65 5407 10602 14289 2480 1407 4248 C
ATOM 332 N LEU A 66 -16.162 24.055 -35.571 1.00108.68 N
ANISOU 332 N LEU A 66 8569 14814 17908 1498 130 4134 N
ATOM 333 CA LEU A 66 -17.321 23.384 -36.145 1.00110.04 C
ANISOU 333 CA LEU A 66 8370 15247 18193 1302 -185 4411 C
ATOM 334 C LEU A 66 -17.421 21.947 -35.656 1.00113.61 C
ANISOU 334 C LEU A 66 8765 15762 18638 969 -333 4281 C
ATOM 335 O LEU A 66 -18.526 21.403 -35.551 1.00123.94 O
ANISOU 335 O LEU A 66 9759 17240 20094 867 -418 4531 O
ATOM 336 CB LEU A 66 -17.264 23.423 -37.672 1.00103.50 C
ANISOU 336 CB LEU A 66 7510 14549 17268 1144 -636 4470 C
ATOM 337 CG LEU A 66 -17.600 24.753 -38.336 1.00105.16 C
ANISOU 337 CG LEU A 66 7661 14774 17522 1459 -561 4716 C
ATOM 338 CD1 LEU A 66 -17.547 24.613 -39.846 1.00110.70 C
ANISOU 338 CD1 LEU A 66 8352 15606 18103 1257 -1054 4758 C
ATOM 339 CD2 LEU A 66 -18.974 25.240 -37.895 1.00107.15 C
ANISOU 339 CD2 LEU A 66 7556 15148 18007 1697 -330 5123 C
ATOM 340 N VAL A 67 -16.284 21.316 -35.358 1.00103.98 N
ANISOU 340 N VAL A 67 7846 14409 17252 799 -362 3905 N
ATOM 341 CA VAL A 67 -16.315 19.941 -34.870 1.00100.65 C
ANISOU 341 CA VAL A 67 7418 14026 16798 497 -480 3761 C
ATOM 342 C VAL A 67 -17.047 19.855 -33.538 1.00100.97 C
ANISOU 342 C VAL A 67 7310 14044 17012 651 -113 3889 C
ATOM 343 O VAL A 67 -17.721 18.857 -33.258 1.00106.84 O
ANISOU 343 O VAL A 67 7873 14899 17824 444 -220 3966 O
ATOM 344 CB VAL A 67 -14.881 19.381 -34.759 1.00100.41 C
ANISOU 344 CB VAL A 67 7757 13846 16548 331 -534 3337 C
ATOM 345 CG1 VAL A 67 -14.896 18.026 -34.088 1.00100.32 C
ANISOU 345 CG1 VAL A 67 7773 13848 16496 71 -579 3183 C
ATOM 346 CG2 VAL A 67 -14.232 19.300 -36.138 1.00101.94 C
ANISOU 346 CG2 VAL A 67 8101 14071 16561 143 -926 3236 C
ATOM 347 N CYS A 68 -16.923 20.885 -32.693 1.00 96.31 N
ANISOU 347 N CYS A 68 6823 13289 16480 1011 332 3915 N
ATOM 348 CA CYS A 68 -17.668 20.909 -31.438 1.00100.96 C
ANISOU 348 CA CYS A 68 7306 13833 17222 1193 711 4069 C
ATOM 349 C CYS A 68 -19.158 21.156 -31.665 1.00115.18 C
ANISOU 349 C CYS A 68 8686 15828 19249 1295 711 4530 C
ATOM 350 O CYS A 68 -20.001 20.539 -31.002 1.00118.37 O
ANISOU 350 O CYS A 68 8869 16309 19796 1250 797 4697 O
ATOM 351 CB CYS A 68 -17.084 21.973 -30.509 1.00 94.43 C
ANISOU 351 CB CYS A 68 6790 12740 16349 1540 1189 3961 C
ATOM 352 SG CYS A 68 -15.348 21.709 -30.050 1.00 84.10 S
ANISOU 352 SG CYS A 68 5957 11199 14799 1432 1235 3444 S
ATOM 353 N LEU A 69 -19.505 22.045 -32.600 1.00129.16 N
ANISOU 353 N LEU A 69 10328 17685 21060 1435 615 4754 N
ATOM 354 CA LEU A 69 -20.916 22.343 -32.851 1.00148.26 C
ANISOU 354 CA LEU A 69 12325 20304 23701 1549 617 5221 C
ATOM 355 C LEU A 69 -21.632 21.159 -33.480 1.00154.74 C
ANISOU 355 C LEU A 69 12826 21378 24589 1162 168 5352 C
ATOM 356 O LEU A 69 -22.836 20.980 -33.266 1.00161.51 O
ANISOU 356 O LEU A 69 13307 22399 25659 1183 204 5712 O
ATOM 357 CB LEU A 69 -21.054 23.596 -33.718 1.00160.31 C
ANISOU 357 CB LEU A 69 13816 21859 25235 1800 622 5418 C
ATOM 358 CG LEU A 69 -20.365 24.807 -33.094 1.00162.94 C
ANISOU 358 CG LEU A 69 14510 21917 25482 2178 1083 5293 C
ATOM 359 CD1 LEU A 69 -20.680 26.102 -33.843 1.00168.11 C
ANISOU 359 CD1 LEU A 69 15119 22594 26161 2474 1155 5540 C
ATOM 360 CD2 LEU A 69 -20.774 24.906 -31.633 1.00165.22 C
ANISOU 360 CD2 LEU A 69 14845 22065 25866 2398 1573 5372 C
ATOM 361 N ALA A 70 -20.921 20.354 -34.271 1.00139.68 N
ANISOU 361 N ALA A 70 11077 19499 22497 806 -250 5081 N
ATOM 362 CA ALA A 70 -21.527 19.125 -34.756 1.00130.09 C
ANISOU 362 CA ALA A 70 9650 18475 21302 407 -654 5161 C
ATOM 363 C ALA A 70 -21.851 18.192 -33.598 1.00125.46 C
ANISOU 363 C ALA A 70 8999 17868 20801 310 -476 5125 C
ATOM 364 O ALA A 70 -22.767 17.366 -33.704 1.00129.49 O
ANISOU 364 O ALA A 70 9221 18554 21427 72 -681 5333 O
ATOM 365 CB ALA A 70 -20.605 18.422 -35.757 1.00119.98 C
ANISOU 365 CB ALA A 70 8650 17175 19761 56 -1089 4847 C
ATOM 366 N VAL A 71 -21.112 18.302 -32.494 1.00115.71 N
ANISOU 366 N VAL A 71 8038 16418 19508 479 -105 4869 N
ATOM 367 CA VAL A 71 -21.397 17.494 -31.315 1.00108.74 C
ANISOU 367 CA VAL A 71 7119 15495 18702 427 107 4834 C
ATOM 368 C VAL A 71 -22.407 18.164 -30.383 1.00114.25 C
ANISOU 368 C VAL A 71 7570 16195 19647 774 538 5188 C
ATOM 369 O VAL A 71 -23.321 17.506 -29.881 1.00119.83 O
ANISOU 369 O VAL A 71 8001 17009 20521 690 577 5401 O
ATOM 370 CB VAL A 71 -20.074 17.173 -30.595 1.00 94.51 C
ANISOU 370 CB VAL A 71 5754 13462 16693 407 265 4376 C
ATOM 371 CG1 VAL A 71 -20.348 16.601 -29.216 1.00 86.46 C
ANISOU 371 CG1 VAL A 71 4732 12363 15755 452 582 4354 C
ATOM 372 CG2 VAL A 71 -19.247 16.222 -31.428 1.00 91.69 C
ANISOU 372 CG2 VAL A 71 5602 13127 16110 25 -159 4070 C
ATOM 373 N TRP A 72 -22.290 19.470 -30.124 1.00117.46 N
ANISOU 373 N TRP A 72 8081 16471 20077 1171 886 5275 N
ATOM 374 CA TRP A 72 -23.271 20.117 -29.249 1.00126.48 C
ANISOU 374 CA TRP A 72 9029 17594 21435 1519 1324 5635 C
ATOM 375 C TRP A 72 -24.659 20.138 -29.877 1.00134.10 C
ANISOU 375 C TRP A 72 9470 18842 22639 1498 1154 6128 C
ATOM 376 O TRP A 72 -25.662 20.007 -29.167 1.00141.66 O
ANISOU 376 O TRP A 72 10149 19865 23810 1613 1386 6445 O
ATOM 377 CB TRP A 72 -22.819 21.542 -28.889 1.00129.81 C
ANISOU 377 CB TRP A 72 9742 17790 21791 1943 1739 5616 C
ATOM 378 CG TRP A 72 -23.692 22.234 -27.854 1.00135.86 C
ANISOU 378 CG TRP A 72 10428 18468 22726 2331 2262 5949 C
ATOM 379 CD1 TRP A 72 -24.708 21.674 -27.131 1.00138.86 C
ANISOU 379 CD1 TRP A 72 10517 18934 23309 2343 2414 6226 C
ATOM 380 CD2 TRP A 72 -23.607 23.604 -27.425 1.00139.26 C
ANISOU 380 CD2 TRP A 72 11106 18688 23119 2761 2716 6044 C
ATOM 381 NE1 TRP A 72 -25.265 22.609 -26.292 1.00143.26 N
ANISOU 381 NE1 TRP A 72 11121 19349 23962 2767 2938 6499 N
ATOM 382 CE2 TRP A 72 -24.607 23.801 -26.450 1.00144.18 C
ANISOU 382 CE2 TRP A 72 11586 19276 23921 3025 3135 6389 C
ATOM 383 CE3 TRP A 72 -22.785 24.683 -27.772 1.00137.30 C
ANISOU 383 CE3 TRP A 72 11206 18268 22694 2945 2819 5877 C
ATOM 384 CZ2 TRP A 72 -24.808 25.033 -25.818 1.00148.50 C
ANISOU 384 CZ2 TRP A 72 12358 19611 24454 3466 3656 6570 C
ATOM 385 CZ3 TRP A 72 -22.987 25.907 -27.142 1.00138.74 C
ANISOU 385 CZ3 TRP A 72 11611 18243 22861 3368 3327 6044 C
ATOM 386 CH2 TRP A 72 -23.990 26.069 -26.178 1.00144.65 C
ANISOU 386 CH2 TRP A 72 12240 18951 23769 3623 3741 6386 C
ATOM 387 N ARG A 73 -24.742 20.274 -31.199 1.00132.32 N
ANISOU 387 N ARG A 73 9102 18789 22384 1345 746 6211 N
ATOM 388 CA ARG A 73 -26.041 20.328 -31.867 1.00136.93 C
ANISOU 388 CA ARG A 73 9182 19656 23188 1311 549 6692 C
ATOM 389 C ARG A 73 -26.617 18.936 -32.131 1.00142.66 C
ANISOU 389 C ARG A 73 9640 20585 23979 861 152 6755 C
ATOM 390 O ARG A 73 -27.724 18.616 -31.679 1.00150.87 O
ANISOU 390 O ARG A 73 10296 21772 25257 866 242 7110 O
ATOM 391 CB ARG A 73 -25.925 21.138 -33.159 1.00134.54 C
ANISOU 391 CB ARG A 73 8857 19443 22818 1357 292 6776 C
ATOM 392 CG ARG A 73 -26.198 22.615 -32.931 1.00137.81 C
ANISOU 392 CG ARG A 73 9265 19780 23317 1859 720 7024 C
ATOM 393 CD ARG A 73 -26.529 23.354 -34.215 1.00141.86 C
ANISOU 393 CD ARG A 73 9595 20461 23843 1916 458 7260 C
ATOM 394 NE ARG A 73 -27.803 22.923 -34.780 1.00157.00 N
ANISOU 394 NE ARG A 73 10980 22699 25976 1748 164 7699 N
ATOM 395 CZ ARG A 73 -28.975 23.495 -34.520 1.00170.36 C
ANISOU 395 CZ ARG A 73 12275 24533 27922 2026 408 8200 C
ATOM 396 NH1 ARG A 73 -29.048 24.534 -33.700 1.00176.02 N
ANISOU 396 NH1 ARG A 73 13105 25081 28692 2501 974 8322 N
ATOM 397 NH2 ARG A 73 -30.080 23.025 -35.083 1.00174.55 N
ANISOU 397 NH2 ARG A 73 12306 25370 28644 1825 90 8594 N
ATOM 398 N ASN A 74 -25.882 18.098 -32.866 1.00139.14 N
ANISOU 398 N ASN A 74 9406 20142 23318 469 -281 6425 N
ATOM 399 CA ASN A 74 -26.404 16.821 -33.344 1.00141.10 C
ANISOU 399 CA ASN A 74 9455 20575 23582 6 -716 6484 C
ATOM 400 C ASN A 74 -26.370 15.817 -32.202 1.00139.18 C
ANISOU 400 C ASN A 74 9272 20247 23362 -116 -532 6327 C
ATOM 401 O ASN A 74 -25.313 15.284 -31.849 1.00139.95 O
ANISOU 401 O ASN A 74 9767 20161 23246 -228 -509 5892 O
ATOM 402 CB ASN A 74 -25.602 16.326 -34.542 1.00137.61 C
ANISOU 402 CB ASN A 74 9290 20127 22868 -345 -1208 6189 C
ATOM 403 CG ASN A 74 -26.355 15.292 -35.346 1.00143.03 C
ANISOU 403 CG ASN A 74 9745 21026 23572 -798 -1703 6364 C
ATOM 404 OD1 ASN A 74 -27.220 14.593 -34.823 1.00146.18 O
ANISOU 404 OD1 ASN A 74 9854 21540 24146 -938 -1690 6575 O
ATOM 405 ND2 ASN A 74 -26.021 15.180 -36.625 1.00145.46 N
ANISOU 405 ND2 ASN A 74 10204 21375 23690 -1039 -2144 6278 N
ATOM 406 N HIS A 75 -27.545 15.560 -31.625 1.00135.72 N
ANISOU 406 N HIS A 75 8427 19951 23190 -88 -396 6701 N
ATOM 407 CA HIS A 75 -27.645 14.684 -30.464 1.00129.07 C
ANISOU 407 CA HIS A 75 7604 19035 22403 -163 -173 6605 C
ATOM 408 C HIS A 75 -27.287 13.233 -30.782 1.00123.72 C
ANISOU 408 C HIS A 75 7075 18377 21554 -672 -566 6322 C
ATOM 409 O HIS A 75 -26.838 12.503 -29.891 1.00116.38 O
ANISOU 409 O HIS A 75 6358 17310 20552 -744 -393 6055 O
ATOM 410 CB HIS A 75 -29.061 14.766 -29.908 1.00138.61 C
ANISOU 410 CB HIS A 75 8300 20413 23951 -25 37 7122 C
ATOM 411 CG HIS A 75 -29.395 16.105 -29.332 1.00137.92 C
ANISOU 411 CG HIS A 75 8132 20254 24019 514 531 7389 C
ATOM 412 ND1 HIS A 75 -29.331 16.388 -27.984 1.00135.14 N
ANISOU 412 ND1 HIS A 75 7920 19700 23725 843 1076 7364 N
ATOM 413 CD2 HIS A 75 -29.804 17.246 -29.935 1.00139.59 C
ANISOU 413 CD2 HIS A 75 8164 20553 24321 785 571 7696 C
ATOM 414 CE1 HIS A 75 -29.679 17.648 -27.784 1.00137.19 C
ANISOU 414 CE1 HIS A 75 8120 19912 24095 1292 1438 7641 C
ATOM 415 NE2 HIS A 75 -29.974 18.190 -28.952 1.00139.90 N
ANISOU 415 NE2 HIS A 75 8256 20435 24464 1270 1147 7848 N
ATOM 416 N HIS A 76 -27.495 12.785 -32.026 1.00128.44 N
ANISOU 416 N HIS A 76 7592 19134 22076 -1029 -1085 6383 N
ATOM 417 CA HIS A 76 -27.126 11.418 -32.399 1.00129.62 C
ANISOU 417 CA HIS A 76 7955 19270 22024 -1516 -1457 6112 C
ATOM 418 C HIS A 76 -25.618 11.170 -32.403 1.00126.47 C
ANISOU 418 C HIS A 76 8128 18628 21296 -1560 -1455 5566 C
ATOM 419 O HIS A 76 -25.187 10.025 -32.211 1.00129.62 O
ANISOU 419 O HIS A 76 8765 18949 21537 -1861 -1569 5293 O
ATOM 420 CB HIS A 76 -27.697 11.064 -33.772 1.00131.29 C
ANISOU 420 CB HIS A 76 8001 19680 22203 -1881 -2012 6319 C
ATOM 421 CG HIS A 76 -29.147 10.705 -33.757 1.00132.24 C
ANISOU 421 CG HIS A 76 7583 20055 22608 -2040 -2134 6802 C
ATOM 422 ND1 HIS A 76 -30.117 11.546 -33.260 1.00137.17 N
ANISOU 422 ND1 HIS A 76 7745 20816 23556 -1699 -1835 7244 N
ATOM 423 CD2 HIS A 76 -29.787 9.579 -34.153 1.00136.52 C
ANISOU 423 CD2 HIS A 76 7981 20733 23158 -2507 -2512 6925 C
ATOM 424 CE1 HIS A 76 -31.297 10.965 -33.378 1.00144.21 C
ANISOU 424 CE1 HIS A 76 8194 21940 24660 -1950 -2036 7632 C
ATOM 425 NE2 HIS A 76 -31.125 9.768 -33.908 1.00143.97 N
ANISOU 425 NE2 HIS A 76 8346 21912 24444 -2454 -2455 7443 N
ATOM 426 N MET A 77 -24.799 12.205 -32.614 1.00119.09 N
ANISOU 426 N MET A 77 7420 17573 20255 -1269 -1320 5411 N
ATOM 427 CA MET A 77 -23.356 12.037 -32.787 1.00109.69 C
ANISOU 427 CA MET A 77 6742 16179 18758 -1321 -1363 4932 C
ATOM 428 C MET A 77 -22.581 12.114 -31.477 1.00114.18 C
ANISOU 428 C MET A 77 7555 16540 19290 -1087 -914 4653 C
ATOM 429 O MET A 77 -21.416 12.528 -31.475 1.00121.34 O
ANISOU 429 O MET A 77 8816 17279 20010 -961 -822 4340 O
ATOM 430 CB MET A 77 -22.828 13.068 -33.789 1.00102.34 C
ANISOU 430 CB MET A 77 5936 15229 17719 -1172 -1491 4907 C
ATOM 431 CG MET A 77 -22.893 12.601 -35.238 1.00104.70 C
ANISOU 431 CG MET A 77 6289 15631 17863 -1527 -2028 4931 C
ATOM 432 SD MET A 77 -22.221 13.787 -36.425 1.00103.36 S
ANISOU 432 SD MET A 77 6293 15427 17552 -1354 -2172 4888 S
ATOM 433 CE MET A 77 -23.057 15.290 -35.940 1.00115.80 C
ANISOU 433 CE MET A 77 7466 17090 19442 -862 -1791 5287 C
ATOM 434 N ARG A 78 -23.199 11.745 -30.355 1.00113.75 N
ANISOU 434 N ARG A 78 7320 16491 19409 -1025 -631 4773 N
ATOM 435 CA ARG A 78 -22.513 11.818 -29.070 1.00 94.48 C
ANISOU 435 CA ARG A 78 5127 13846 16927 -803 -201 4527 C
ATOM 436 C ARG A 78 -22.020 10.473 -28.545 1.00 98.44 C
ANISOU 436 C ARG A 78 5855 14267 17280 -1097 -243 4224 C
ATOM 437 O ARG A 78 -22.365 10.090 -27.422 1.00104.77 O
ANISOU 437 O ARG A 78 6590 15026 18191 -1036 50 4260 O
ATOM 438 CB ARG A 78 -23.452 12.430 -28.034 1.00 98.44 C
ANISOU 438 CB ARG A 78 5340 14358 17704 -467 230 4858 C
ATOM 439 CG ARG A 78 -24.016 13.776 -28.413 1.00101.66 C
ANISOU 439 CG ARG A 78 5526 14830 18272 -135 346 5193 C
ATOM 440 CD ARG A 78 -25.213 14.086 -27.541 1.00117.83 C
ANISOU 440 CD ARG A 78 7220 16937 20613 114 700 5603 C
ATOM 441 NE ARG A 78 -25.910 15.285 -27.982 1.00117.43 N
ANISOU 441 NE ARG A 78 6910 16980 20729 411 792 5986 N
ATOM 442 CZ ARG A 78 -25.659 16.507 -27.530 1.00113.74 C
ANISOU 442 CZ ARG A 78 6604 16347 20266 840 1187 6020 C
ATOM 443 NH1 ARG A 78 -24.716 16.711 -26.619 1.00105.79 N
ANISOU 443 NH1 ARG A 78 6020 15070 19104 1010 1511 5691 N
ATOM 444 NH2 ARG A 78 -26.354 17.532 -28.000 1.00114.89 N
ANISOU 444 NH2 ARG A 78 6502 16593 20558 1092 1257 6391 N
ATOM 445 N THR A 79 -21.207 9.755 -29.319 1.00 92.94 N
ANISOU 445 N THR A 79 5451 13535 16328 -1401 -579 3931 N
ATOM 446 CA THR A 79 -20.617 8.514 -28.829 1.00 99.79 C
ANISOU 446 CA THR A 79 6591 14300 17024 -1657 -592 3623 C
ATOM 447 C THR A 79 -19.374 8.791 -27.982 1.00101.85 C
ANISOU 447 C THR A 79 7214 14348 17135 -1442 -277 3280 C
ATOM 448 O THR A 79 -18.870 9.913 -27.906 1.00102.38 O
ANISOU 448 O THR A 79 7365 14337 17199 -1133 -97 3246 O
ATOM 449 CB THR A 79 -20.273 7.561 -29.980 1.00104.82 C
ANISOU 449 CB THR A 79 7437 14959 17432 -2067 -1057 3466 C
ATOM 450 OG1 THR A 79 -19.220 8.111 -30.784 1.00 98.71 O
ANISOU 450 OG1 THR A 79 6958 14099 16447 -1998 -1190 3251 O
ATOM 451 CG2 THR A 79 -21.496 7.298 -30.852 1.00115.35 C
ANISOU 451 CG2 THR A 79 8433 16498 18897 -2306 -1401 3817 C
ATOM 452 N VAL A 80 -18.875 7.732 -27.340 1.00103.48 N
ANISOU 452 N VAL A 80 7650 14458 17210 -1622 -215 3030 N
ATOM 453 CA VAL A 80 -17.634 7.840 -26.574 1.00 92.08 C
ANISOU 453 CA VAL A 80 6567 12821 15600 -1471 37 2700 C
ATOM 454 C VAL A 80 -16.507 8.356 -27.462 1.00 79.16 C
ANISOU 454 C VAL A 80 5200 11121 13757 -1442 -142 2481 C
ATOM 455 O VAL A 80 -15.695 9.191 -27.045 1.00 80.25 O
ANISOU 455 O VAL A 80 5505 11137 13848 -1180 83 2346 O
ATOM 456 CB VAL A 80 -17.284 6.479 -25.937 1.00 95.64 C
ANISOU 456 CB VAL A 80 7228 13192 15918 -1726 67 2482 C
ATOM 457 CG1 VAL A 80 -15.952 6.550 -25.198 1.00 86.38 C
ANISOU 457 CG1 VAL A 80 6431 11830 14561 -1589 295 2157 C
ATOM 458 CG2 VAL A 80 -18.390 6.039 -25.017 1.00102.13 C
ANISOU 458 CG2 VAL A 80 7780 14069 16954 -1737 277 2708 C
ATOM 459 N THR A 81 -16.460 7.889 -28.712 1.00 69.04 N
ANISOU 459 N THR A 81 3975 9908 12348 -1712 -545 2456 N
ATOM 460 CA THR A 81 -15.392 8.302 -29.616 1.00 65.59 C
ANISOU 460 CA THR A 81 3809 9407 11706 -1699 -720 2256 C
ATOM 461 C THR A 81 -15.461 9.794 -29.931 1.00 81.87 C
ANISOU 461 C THR A 81 5726 11497 13886 -1389 -633 2413 C
ATOM 462 O THR A 81 -14.420 10.453 -30.051 1.00 83.06 O
ANISOU 462 O THR A 81 6097 11543 13920 -1239 -564 2226 O
ATOM 463 CB THR A 81 -15.459 7.488 -30.905 1.00 66.91 C
ANISOU 463 CB THR A 81 4091 9624 11707 -2040 -1157 2237 C
ATOM 464 OG1 THR A 81 -15.162 6.119 -30.613 1.00 66.06 O
ANISOU 464 OG1 THR A 81 4220 9435 11444 -2308 -1207 2041 O
ATOM 465 CG2 THR A 81 -14.462 8.025 -31.907 1.00 63.98 C
ANISOU 465 CG2 THR A 81 3978 9192 11141 -1997 -1325 2080 C
ATOM 466 N ASN A 82 -16.674 10.346 -30.068 1.00 82.26 N
ANISOU 466 N ASN A 82 5404 11682 14169 -1289 -628 2767 N
ATOM 467 CA ASN A 82 -16.792 11.760 -30.424 1.00 85.88 C
ANISOU 467 CA ASN A 82 5737 12159 14736 -991 -541 2939 C
ATOM 468 C ASN A 82 -16.435 12.678 -29.256 1.00 94.17 C
ANISOU 468 C ASN A 82 6852 13064 15866 -620 -78 2895 C
ATOM 469 O ASN A 82 -15.836 13.744 -29.455 1.00103.30 O
ANISOU 469 O ASN A 82 8125 14136 16988 -394 25 2845 O
ATOM 470 CB ASN A 82 -18.197 12.079 -30.942 1.00 87.11 C
ANISOU 470 CB ASN A 82 5479 12505 15114 -985 -669 3357 C
ATOM 471 CG ASN A 82 -18.415 11.612 -32.358 1.00 95.82 C
ANISOU 471 CG ASN A 82 6567 13728 16111 -1295 -1151 3419 C
ATOM 472 OD1 ASN A 82 -17.466 11.454 -33.129 1.00 92.14 O
ANISOU 472 OD1 ASN A 82 6411 13189 15410 -1419 -1362 3177 O
ATOM 473 ND2 ASN A 82 -19.675 11.407 -32.723 1.00109.83 N
ANISOU 473 ND2 ASN A 82 7989 15684 18056 -1418 -1326 3761 N
ATOM 474 N TYR A 83 -16.793 12.292 -28.029 1.00 88.92 N
ANISOU 474 N TYR A 83 6141 12349 15295 -554 213 2917 N
ATOM 475 CA TYR A 83 -16.368 13.083 -26.877 1.00 82.72 C
ANISOU 475 CA TYR A 83 5509 11382 14537 -219 654 2845 C
ATOM 476 C TYR A 83 -14.847 13.114 -26.789 1.00 74.28 C
ANISOU 476 C TYR A 83 4836 10152 13235 -230 671 2464 C
ATOM 477 O TYR A 83 -14.248 14.120 -26.385 1.00 67.97 O
ANISOU 477 O TYR A 83 4211 9203 12412 35 922 2388 O
ATOM 478 CB TYR A 83 -16.988 12.530 -25.601 1.00 84.23 C
ANISOU 478 CB TYR A 83 5624 11536 14843 -174 945 2924 C
ATOM 479 CG TYR A 83 -18.425 12.938 -25.430 1.00 92.06 C
ANISOU 479 CG TYR A 83 6235 12640 16104 -20 1078 3341 C
ATOM 480 CD1 TYR A 83 -18.964 13.993 -26.155 1.00 97.91 C
ANISOU 480 CD1 TYR A 83 6775 13462 16964 160 1038 3608 C
ATOM 481 CD2 TYR A 83 -19.237 12.300 -24.501 1.00 89.81 C
ANISOU 481 CD2 TYR A 83 5791 12374 15959 -34 1272 3487 C
ATOM 482 CE1 TYR A 83 -20.285 14.378 -26.007 1.00 99.64 C
ANISOU 482 CE1 TYR A 83 6628 13793 17437 316 1171 4023 C
ATOM 483 CE2 TYR A 83 -20.560 12.688 -24.337 1.00 89.90 C
ANISOU 483 CE2 TYR A 83 5432 12494 16233 122 1411 3901 C
ATOM 484 CZ TYR A 83 -21.074 13.726 -25.093 1.00 96.50 C
ANISOU 484 CZ TYR A 83 6061 13419 17184 299 1359 4172 C
ATOM 485 OH TYR A 83 -22.384 14.096 -24.915 1.00107.04 O
ANISOU 485 OH TYR A 83 7016 14869 18784 463 1510 4609 O
ATOM 486 N PHE A 84 -14.207 12.012 -27.171 1.00 72.55 N
ANISOU 486 N PHE A 84 4777 9953 12834 -541 410 2230 N
ATOM 487 CA PHE A 84 -12.751 11.987 -27.223 1.00 67.29 C
ANISOU 487 CA PHE A 84 4460 9158 11950 -572 389 1896 C
ATOM 488 C PHE A 84 -12.243 12.844 -28.382 1.00 70.90 C
ANISOU 488 C PHE A 84 4963 9631 12346 -524 198 1883 C
ATOM 489 O PHE A 84 -11.270 13.594 -28.225 1.00 79.98 O
ANISOU 489 O PHE A 84 6312 10651 13425 -364 338 1724 O
ATOM 490 CB PHE A 84 -12.239 10.558 -27.353 1.00 66.68 C
ANISOU 490 CB PHE A 84 4562 9088 11686 -902 179 1676 C
ATOM 491 CG PHE A 84 -12.313 9.761 -26.079 1.00 68.85 C
ANISOU 491 CG PHE A 84 4896 9292 11970 -929 417 1606 C
ATOM 492 CD1 PHE A 84 -11.683 10.209 -24.928 1.00 63.18 C
ANISOU 492 CD1 PHE A 84 4354 8410 11242 -702 765 1482 C
ATOM 493 CD2 PHE A 84 -12.988 8.540 -26.047 1.00 78.96 C
ANISOU 493 CD2 PHE A 84 6090 10653 13258 -1195 289 1659 C
ATOM 494 CE1 PHE A 84 -11.751 9.462 -23.751 1.00 66.96 C
ANISOU 494 CE1 PHE A 84 4914 8809 11719 -720 987 1425 C
ATOM 495 CE2 PHE A 84 -13.057 7.793 -24.888 1.00 78.31 C
ANISOU 495 CE2 PHE A 84 6071 10501 13183 -1225 514 1603 C
ATOM 496 CZ PHE A 84 -12.440 8.252 -23.735 1.00 72.40 C
ANISOU 496 CZ PHE A 84 5493 9591 12424 -979 865 1491 C
ATOM 497 N LEU A 85 -12.861 12.713 -29.566 1.00 68.70 N
ANISOU 497 N LEU A 85 4518 9501 12085 -677 -131 2047 N
ATOM 498 CA LEU A 85 -12.456 13.535 -30.705 1.00 70.98 C
ANISOU 498 CA LEU A 85 4847 9805 12318 -628 -315 2063 C
ATOM 499 C LEU A 85 -12.699 15.018 -30.448 1.00 86.46 C
ANISOU 499 C LEU A 85 6695 11717 14438 -269 -43 2235 C
ATOM 500 O LEU A 85 -11.924 15.858 -30.924 1.00 97.14 O
ANISOU 500 O LEU A 85 8187 12995 15726 -152 -41 2150 O
ATOM 501 CB LEU A 85 -13.190 13.110 -31.977 1.00 60.20 C
ANISOU 501 CB LEU A 85 3337 8598 10938 -857 -714 2237 C
ATOM 502 CG LEU A 85 -12.864 11.779 -32.657 1.00 66.29 C
ANISOU 502 CG LEU A 85 4310 9384 11491 -1222 -1046 2069 C
ATOM 503 CD1 LEU A 85 -13.644 11.651 -33.956 1.00 70.17 C
ANISOU 503 CD1 LEU A 85 4676 10010 11976 -1404 -1422 2283 C
ATOM 504 CD2 LEU A 85 -11.379 11.693 -32.909 1.00 64.61 C
ANISOU 504 CD2 LEU A 85 4471 9038 11041 -1253 -1074 1746 C
ATOM 505 N VAL A 86 -13.751 15.361 -29.691 1.00 84.21 N
ANISOU 505 N VAL A 86 6183 11457 14355 -83 207 2483 N
ATOM 506 CA VAL A 86 -13.939 16.748 -29.276 1.00 77.32 C
ANISOU 506 CA VAL A 86 5286 10488 13603 287 539 2631 C
ATOM 507 C VAL A 86 -12.800 17.164 -28.356 1.00 81.06 C
ANISOU 507 C VAL A 86 6099 10732 13967 441 845 2354 C
ATOM 508 O VAL A 86 -12.259 18.270 -28.473 1.00 72.46 O
ANISOU 508 O VAL A 86 5157 9522 12852 649 990 2319 O
ATOM 509 CB VAL A 86 -15.317 16.946 -28.609 1.00 68.23 C
ANISOU 509 CB VAL A 86 3851 9396 12677 457 768 2967 C
ATOM 510 CG1 VAL A 86 -15.346 18.260 -27.833 1.00 71.23 C
ANISOU 510 CG1 VAL A 86 4342 9599 13125 857 1212 3057 C
ATOM 511 CG2 VAL A 86 -16.434 16.899 -29.639 1.00 71.38 C
ANISOU 511 CG2 VAL A 86 3892 10022 13207 359 479 3292 C
ATOM 512 N ASN A 87 -12.412 16.284 -27.429 1.00 85.48 N
ANISOU 512 N ASN A 87 6802 11222 14454 333 946 2158 N
ATOM 513 CA ASN A 87 -11.254 16.577 -26.586 1.00 72.75 C
ANISOU 513 CA ASN A 87 5530 9395 12715 437 1195 1880 C
ATOM 514 C ASN A 87 -9.983 16.733 -27.413 1.00 70.85 C
ANISOU 514 C ASN A 87 5478 9123 12320 327 989 1643 C
ATOM 515 O ASN A 87 -9.107 17.531 -27.054 1.00 73.69 O
ANISOU 515 O ASN A 87 6075 9307 12616 479 1192 1490 O
ATOM 516 CB ASN A 87 -11.062 15.488 -25.535 1.00 63.69 C
ANISOU 516 CB ASN A 87 4497 8197 11507 314 1298 1719 C
ATOM 517 CG ASN A 87 -9.980 15.821 -24.525 1.00 51.49 C
ANISOU 517 CG ASN A 87 3310 6420 9836 436 1582 1460 C
ATOM 518 OD1 ASN A 87 -10.029 16.852 -23.856 1.00 49.71 O
ANISOU 518 OD1 ASN A 87 3231 6026 9630 703 1904 1504 O
ATOM 519 ND2 ASN A 87 -8.981 14.950 -24.427 1.00 56.48 N
ANISOU 519 ND2 ASN A 87 4117 7030 10314 231 1460 1189 N
ATOM 520 N LEU A 88 -9.864 15.992 -28.523 1.00 71.17 N
ANISOU 520 N LEU A 88 5445 9312 12285 60 595 1613 N
ATOM 521 CA LEU A 88 -8.713 16.160 -29.411 1.00 69.37 C
ANISOU 521 CA LEU A 88 5391 9055 11913 -36 394 1423 C
ATOM 522 C LEU A 88 -8.658 17.571 -29.991 1.00 78.52 C
ANISOU 522 C LEU A 88 6524 10168 13144 191 463 1542 C
ATOM 523 O LEU A 88 -7.571 18.134 -30.177 1.00 81.78 O
ANISOU 523 O LEU A 88 7129 10464 13481 237 505 1369 O
ATOM 524 CB LEU A 88 -8.764 15.140 -30.548 1.00 60.01 C
ANISOU 524 CB LEU A 88 4180 8016 10607 -346 -29 1406 C
ATOM 525 CG LEU A 88 -7.614 15.249 -31.544 1.00 54.77 C
ANISOU 525 CG LEU A 88 3719 7316 9776 -449 -245 1230 C
ATOM 526 CD1 LEU A 88 -6.311 15.096 -30.783 1.00 47.00 C
ANISOU 526 CD1 LEU A 88 2993 6180 8683 -447 -74 935 C
ATOM 527 CD2 LEU A 88 -7.758 14.192 -32.616 1.00 54.10 C
ANISOU 527 CD2 LEU A 88 3685 7338 9533 -743 -631 1219 C
ATOM 528 N SER A 89 -9.821 18.155 -30.292 1.00 82.52 N
ANISOU 528 N SER A 89 6792 10763 13800 336 481 1847 N
ATOM 529 CA SER A 89 -9.845 19.535 -30.762 1.00 82.88 C
ANISOU 529 CA SER A 89 6833 10748 13909 589 590 1983 C
ATOM 530 C SER A 89 -9.412 20.500 -29.669 1.00 94.85 C
ANISOU 530 C SER A 89 8581 12029 15431 869 1034 1898 C
ATOM 531 O SER A 89 -8.806 21.535 -29.960 1.00105.80 O
ANISOU 531 O SER A 89 10129 13284 16785 1029 1142 1855 O
ATOM 532 CB SER A 89 -11.242 19.899 -31.267 1.00 72.27 C
ANISOU 532 CB SER A 89 5182 9557 12720 688 524 2349 C
ATOM 533 OG SER A 89 -11.695 18.995 -32.257 1.00 68.50 O
ANISOU 533 OG SER A 89 4531 9281 12216 404 106 2427 O
ATOM 534 N LEU A 90 -9.716 20.180 -28.406 1.00 90.90 N
ANISOU 534 N LEU A 90 8140 11447 14949 929 1300 1872 N
ATOM 535 CA LEU A 90 -9.379 21.096 -27.320 1.00 81.45 C
ANISOU 535 CA LEU A 90 7241 9995 13711 1183 1725 1793 C
ATOM 536 C LEU A 90 -7.872 21.261 -27.174 1.00 79.16 C
ANISOU 536 C LEU A 90 7282 9534 13259 1119 1760 1454 C
ATOM 537 O LEU A 90 -7.384 22.373 -26.934 1.00 81.53 O
ANISOU 537 O LEU A 90 7862 9624 13493 1305 1998 1390 O
ATOM 538 CB LEU A 90 -10.004 20.608 -26.019 1.00 79.40 C
ANISOU 538 CB LEU A 90 7004 9682 13483 1234 1975 1833 C
ATOM 539 CG LEU A 90 -11.527 20.489 -26.059 1.00 72.77 C
ANISOU 539 CG LEU A 90 5823 8997 12830 1311 1988 2190 C
ATOM 540 CD1 LEU A 90 -12.004 19.566 -24.956 1.00 81.65 C
ANISOU 540 CD1 LEU A 90 6922 10115 13986 1256 2125 2191 C
ATOM 541 CD2 LEU A 90 -12.161 21.865 -25.922 1.00 60.10 C
ANISOU 541 CD2 LEU A 90 4263 7281 11293 1649 2291 2432 C
ATOM 542 N ALA A 91 -7.120 20.164 -27.297 1.00 79.31 N
ANISOU 542 N ALA A 91 7305 9630 13201 847 1534 1235 N
ATOM 543 CA ALA A 91 -5.664 20.273 -27.318 1.00 80.52 C
ANISOU 543 CA ALA A 91 7750 9654 13189 749 1511 921 C
ATOM 544 C ALA A 91 -5.185 21.023 -28.554 1.00 88.94 C
ANISOU 544 C ALA A 91 8882 10731 14180 736 1312 922 C
ATOM 545 O ALA A 91 -4.233 21.812 -28.477 1.00 95.34 O
ANISOU 545 O ALA A 91 10043 11366 14816 761 1397 740 O
ATOM 546 CB ALA A 91 -5.026 18.888 -27.251 1.00 73.03 C
ANISOU 546 CB ALA A 91 6849 8798 12100 448 1271 702 C
ATOM 547 N ASP A 92 -5.818 20.773 -29.708 1.00 86.59 N
ANISOU 547 N ASP A 92 8267 10634 14000 675 1033 1130 N
ATOM 548 CA ASP A 92 -5.392 21.435 -30.935 1.00 77.29 C
ANISOU 548 CA ASP A 92 7169 9463 12735 664 838 1141 C
ATOM 549 C ASP A 92 -5.592 22.938 -30.878 1.00 76.41 C
ANISOU 549 C ASP A 92 7169 9187 12676 970 1114 1268 C
ATOM 550 O ASP A 92 -4.769 23.690 -31.414 1.00 75.75 O
ANISOU 550 O ASP A 92 7359 8986 12438 967 1089 1149 O
ATOM 551 CB ASP A 92 -6.149 20.860 -32.126 1.00 68.17 C
ANISOU 551 CB ASP A 92 5670 8547 11683 539 474 1363 C
ATOM 552 CG ASP A 92 -5.813 19.430 -32.369 1.00 74.87 C
ANISOU 552 CG ASP A 92 6518 9513 12417 215 181 1214 C
ATOM 553 OD1 ASP A 92 -4.758 18.986 -31.861 1.00 87.42 O
ANISOU 553 OD1 ASP A 92 8400 11003 13815 102 232 918 O
ATOM 554 OD2 ASP A 92 -6.590 18.752 -33.080 1.00 73.81 O
ANISOU 554 OD2 ASP A 92 6151 9559 12336 66 -106 1386 O
ATOM 555 N VAL A 93 -6.658 23.393 -30.222 1.00 71.46 N
ANISOU 555 N VAL A 93 6358 8534 12260 1242 1404 1517 N
ATOM 556 CA VAL A 93 -6.926 24.825 -30.153 1.00 75.65 C
ANISOU 556 CA VAL A 93 7053 8884 12808 1557 1695 1655 C
ATOM 557 C VAL A 93 -5.963 25.511 -29.195 1.00 76.60 C
ANISOU 557 C VAL A 93 7676 8686 12742 1617 2006 1387 C
ATOM 558 O VAL A 93 -5.448 26.599 -29.479 1.00 75.38 O
ANISOU 558 O VAL A 93 7830 8341 12468 1708 2105 1334 O
ATOM 559 CB VAL A 93 -8.392 25.088 -29.756 1.00 74.58 C
ANISOU 559 CB VAL A 93 6736 8823 12779 1744 1853 1969 C
ATOM 560 CG1 VAL A 93 -8.611 26.574 -29.524 1.00 55.12 C
ANISOU 560 CG1 VAL A 93 4534 6138 10271 2059 2196 2084 C
ATOM 561 CG2 VAL A 93 -9.337 24.564 -30.822 1.00 68.66 C
ANISOU 561 CG2 VAL A 93 5556 8373 12157 1644 1501 2231 C
ATOM 562 N LEU A 94 -5.758 24.912 -28.021 1.00 78.85 N
ANISOU 562 N LEU A 94 8085 8900 12974 1547 2155 1222 N
ATOM 563 CA LEU A 94 -4.736 25.407 -27.108 1.00 76.88 C
ANISOU 563 CA LEU A 94 8355 8370 12486 1507 2354 934 C
ATOM 564 C LEU A 94 -3.415 25.558 -27.845 1.00 75.13 C
ANISOU 564 C LEU A 94 8366 8131 12048 1252 2087 689 C
ATOM 565 O LEU A 94 -2.707 26.558 -27.674 1.00 83.64 O
ANISOU 565 O LEU A 94 9839 8974 12967 1270 2222 566 O
ATOM 566 CB LEU A 94 -4.589 24.474 -25.905 1.00 78.16 C
ANISOU 566 CB LEU A 94 8588 8515 12594 1399 2439 774 C
ATOM 567 CG LEU A 94 -3.300 24.523 -25.084 1.00 68.89 C
ANISOU 567 CG LEU A 94 7892 7146 11138 1217 2464 429 C
ATOM 568 CD1 LEU A 94 -3.207 25.782 -24.229 1.00 74.69 C
ANISOU 568 CD1 LEU A 94 9100 7536 11745 1409 2831 398 C
ATOM 569 CD2 LEU A 94 -3.145 23.274 -24.214 1.00 57.82 C
ANISOU 569 CD2 LEU A 94 6455 5822 9692 1063 2418 289 C
ATOM 570 N ALA A 95 -3.071 24.569 -28.677 1.00 65.19 N
ANISOU 570 N ALA A 95 6884 7108 10776 1008 1719 628 N
ATOM 571 CA ALA A 95 -1.872 24.670 -29.497 1.00 61.79 C
ANISOU 571 CA ALA A 95 6629 6684 10163 795 1486 442 C
ATOM 572 C ALA A 95 -2.000 25.789 -30.526 1.00 67.03 C
ANISOU 572 C ALA A 95 7332 7289 10847 928 1485 589 C
ATOM 573 O ALA A 95 -1.086 26.605 -30.682 1.00 74.84 O
ANISOU 573 O ALA A 95 8639 8114 11683 873 1531 457 O
ATOM 574 CB ALA A 95 -1.589 23.337 -30.192 1.00 51.14 C
ANISOU 574 CB ALA A 95 5065 5580 8787 553 1136 377 C
ATOM 575 N THR A 96 -3.115 25.826 -31.265 1.00 60.36 N
ANISOU 575 N THR A 96 6159 6585 10189 1086 1414 877 N
ATOM 576 CA THR A 96 -3.257 26.801 -32.345 1.00 52.76 C
ANISOU 576 CA THR A 96 5220 5590 9237 1216 1375 1035 C
ATOM 577 C THR A 96 -3.358 28.228 -31.814 1.00 60.84 C
ANISOU 577 C THR A 96 6548 6325 10245 1481 1752 1091 C
ATOM 578 O THR A 96 -2.619 29.120 -32.252 1.00 73.47 O
ANISOU 578 O THR A 96 8456 7758 11702 1459 1785 1005 O
ATOM 579 CB THR A 96 -4.489 26.473 -33.189 1.00 47.35 C
ANISOU 579 CB THR A 96 4092 5142 8757 1323 1187 1359 C
ATOM 580 OG1 THR A 96 -4.264 25.272 -33.936 1.00 47.62 O
ANISOU 580 OG1 THR A 96 3953 5398 8741 1040 798 1291 O
ATOM 581 CG2 THR A 96 -4.773 27.608 -34.150 1.00 47.41 C
ANISOU 581 CG2 THR A 96 4136 5093 8784 1528 1200 1562 C
ATOM 582 N ALA A 97 -4.284 28.473 -30.892 1.00 61.49 N
ANISOU 582 N ALA A 97 6569 6328 10467 1741 2058 1250 N
ATOM 583 CA ALA A 97 -4.538 29.843 -30.464 1.00 66.64 C
ANISOU 583 CA ALA A 97 7535 6684 11100 2045 2447 1351 C
ATOM 584 C ALA A 97 -3.347 30.418 -29.713 1.00 68.87 C
ANISOU 584 C ALA A 97 8385 6661 11123 1895 2603 1035 C
ATOM 585 O ALA A 97 -2.905 31.536 -29.996 1.00 72.28 O
ANISOU 585 O ALA A 97 9171 6862 11430 1947 2723 1008 O
ATOM 586 CB ALA A 97 -5.794 29.889 -29.593 1.00 75.57 C
ANISOU 586 CB ALA A 97 8519 7845 12349 2288 2713 1580 C
ATOM 587 N ILE A 98 -2.825 29.674 -28.740 1.00 70.16 N
ANISOU 587 N ILE A 98 8648 6814 11194 1695 2595 807 N
ATOM 588 CA ILE A 98 -1.773 30.188 -27.877 1.00 65.82 C
ANISOU 588 CA ILE A 98 8626 5982 10399 1538 2728 532 C
ATOM 589 C ILE A 98 -0.409 29.918 -28.494 1.00 57.82 C
ANISOU 589 C ILE A 98 7688 5053 9226 1166 2403 295 C
ATOM 590 O ILE A 98 0.370 30.843 -28.730 1.00 64.30 O
ANISOU 590 O ILE A 98 8851 5682 9897 1071 2435 201 O
ATOM 591 CB ILE A 98 -1.888 29.585 -26.467 1.00 66.10 C
ANISOU 591 CB ILE A 98 8766 5952 10398 1527 2891 423 C
ATOM 592 CG1 ILE A 98 -3.048 30.252 -25.724 1.00 64.24 C
ANISOU 592 CG1 ILE A 98 8617 5642 10150 1805 3208 650 C
ATOM 593 CG2 ILE A 98 -0.611 29.780 -25.705 1.00 71.76 C
ANISOU 593 CG2 ILE A 98 9954 6469 10843 1249 2870 111 C
ATOM 594 CD1 ILE A 98 -3.618 29.445 -24.580 1.00 69.10 C
ANISOU 594 CD1 ILE A 98 9145 6332 10780 1820 3310 667 C
ATOM 595 N CYS A 99 -0.104 28.645 -28.742 1.00 54.99 N
ANISOU 595 N CYS A 99 7022 4974 8898 957 2109 210 N
ATOM 596 CA CYS A 99 1.239 28.262 -29.160 1.00 57.77 C
ANISOU 596 CA CYS A 99 7440 5412 9098 628 1845 -7 C
ATOM 597 C CYS A 99 1.512 28.659 -30.608 1.00 66.76 C
ANISOU 597 C CYS A 99 8501 6625 10241 597 1677 73 C
ATOM 598 O CYS A 99 2.575 29.205 -30.917 1.00 80.68 O
ANISOU 598 O CYS A 99 10497 8294 11863 421 1633 -50 O
ATOM 599 CB CYS A 99 1.425 26.754 -28.985 1.00 49.46 C
ANISOU 599 CB CYS A 99 6117 4612 8063 462 1622 -102 C
ATOM 600 SG CYS A 99 0.823 26.060 -27.428 1.00 53.67 S
ANISOU 600 SG CYS A 99 6655 5107 8631 539 1807 -140 S
ATOM 601 N LEU A 100 0.573 28.387 -31.516 1.00 63.65 N
ANISOU 601 N LEU A 100 7782 6402 10001 751 1572 289 N
ATOM 602 CA LEU A 100 0.852 28.589 -32.939 1.00 56.84 C
ANISOU 602 CA LEU A 100 6856 5628 9115 705 1374 358 C
ATOM 603 C LEU A 100 1.309 30.002 -33.267 1.00 62.92 C
ANISOU 603 C LEU A 100 7965 6151 9790 756 1534 365 C
ATOM 604 O LEU A 100 2.322 30.147 -33.976 1.00 64.38 O
ANISOU 604 O LEU A 100 8267 6339 9856 564 1408 264 O
ATOM 605 CB LEU A 100 -0.376 28.191 -33.777 1.00 57.11 C
ANISOU 605 CB LEU A 100 6517 5861 9321 874 1231 623 C
ATOM 606 CG LEU A 100 -0.099 28.421 -35.265 1.00 51.32 C
ANISOU 606 CG LEU A 100 5774 5196 8529 831 1019 696 C
ATOM 607 CD1 LEU A 100 -0.664 27.309 -36.166 1.00 58.48 C
ANISOU 607 CD1 LEU A 100 6348 6377 9496 764 690 812 C
ATOM 608 CD2 LEU A 100 -0.638 29.773 -35.694 1.00 51.15 C
ANISOU 608 CD2 LEU A 100 5874 5011 8550 1093 1195 896 C
ATOM 609 N PRO A 101 0.649 31.068 -32.803 1.00 64.46 N
ANISOU 609 N PRO A 101 8350 6117 10023 1007 1826 487 N
ATOM 610 CA PRO A 101 1.184 32.413 -33.080 1.00 53.74 C
ANISOU 610 CA PRO A 101 7390 4486 8542 1021 1987 470 C
ATOM 611 C PRO A 101 2.599 32.588 -32.567 1.00 50.49 C
ANISOU 611 C PRO A 101 7302 3941 7939 688 1974 198 C
ATOM 612 O PRO A 101 3.419 33.274 -33.196 1.00 54.00 O
ANISOU 612 O PRO A 101 7958 4283 8276 546 1950 150 O
ATOM 613 CB PRO A 101 0.204 33.335 -32.342 1.00 52.27 C
ANISOU 613 CB PRO A 101 7395 4053 8413 1360 2350 627 C
ATOM 614 CG PRO A 101 -1.046 32.527 -32.168 1.00 57.53 C
ANISOU 614 CG PRO A 101 7622 4941 9294 1581 2334 826 C
ATOM 615 CD PRO A 101 -0.588 31.112 -31.998 1.00 64.85 C
ANISOU 615 CD PRO A 101 8290 6126 10222 1298 2055 657 C
ATOM 616 N ALA A 102 2.893 31.997 -31.416 1.00 56.31 N
ANISOU 616 N ALA A 102 8081 4681 8633 556 1990 36 N
ATOM 617 CA ALA A 102 4.246 32.034 -30.888 1.00 62.96 C
ANISOU 617 CA ALA A 102 9170 5450 9303 213 1922 -201 C
ATOM 618 C ALA A 102 5.188 31.222 -31.762 1.00 66.07 C
ANISOU 618 C ALA A 102 9311 6109 9682 -29 1626 -271 C
ATOM 619 O ALA A 102 6.355 31.593 -31.939 1.00 67.87 O
ANISOU 619 O ALA A 102 9703 6290 9797 -285 1566 -378 O
ATOM 620 CB ALA A 102 4.268 31.523 -29.446 1.00 72.63 C
ANISOU 620 CB ALA A 102 10491 6629 10476 152 1989 -337 C
ATOM 621 N SER A 103 4.685 30.125 -32.332 1.00 75.92 N
ANISOU 621 N SER A 103 10176 7630 11041 48 1452 -196 N
ATOM 622 CA SER A 103 5.501 29.277 -33.192 1.00 66.19 C
ANISOU 622 CA SER A 103 8743 6629 9775 -137 1204 -249 C
ATOM 623 C SER A 103 5.926 29.980 -34.473 1.00 75.44 C
ANISOU 623 C SER A 103 9992 7766 10907 -158 1171 -171 C
ATOM 624 O SER A 103 7.041 29.755 -34.953 1.00 71.41 O
ANISOU 624 O SER A 103 9480 7336 10316 -365 1065 -249 O
ATOM 625 CB SER A 103 4.725 27.999 -33.531 1.00 73.49 C
ANISOU 625 CB SER A 103 9317 7802 10801 -44 1037 -174 C
ATOM 626 OG SER A 103 4.303 27.322 -32.362 1.00 84.74 O
ANISOU 626 OG SER A 103 10671 9257 12269 -22 1084 -234 O
ATOM 627 N LEU A 104 5.068 30.833 -35.028 1.00 86.42 N
ANISOU 627 N LEU A 104 11448 9035 12351 68 1277 -2 N
ATOM 628 CA LEU A 104 5.408 31.545 -36.253 1.00 70.37 C
ANISOU 628 CA LEU A 104 9522 6947 10268 70 1261 83 C
ATOM 629 C LEU A 104 6.548 32.533 -36.034 1.00 66.73 C
ANISOU 629 C LEU A 104 9395 6274 9687 -142 1386 -28 C
ATOM 630 O LEU A 104 7.506 32.565 -36.819 1.00 65.84 O
ANISOU 630 O LEU A 104 9299 6211 9506 -315 1308 -53 O
ATOM 631 CB LEU A 104 4.174 32.253 -36.802 1.00 62.16 C
ANISOU 631 CB LEU A 104 8480 5823 9313 386 1350 310 C
ATOM 632 CG LEU A 104 4.406 33.100 -38.039 1.00 55.16 C
ANISOU 632 CG LEU A 104 7750 4846 8363 429 1356 417 C
ATOM 633 CD1 LEU A 104 4.729 32.202 -39.221 1.00 53.62 C
ANISOU 633 CD1 LEU A 104 7356 4886 8134 338 1094 437 C
ATOM 634 CD2 LEU A 104 3.184 33.950 -38.316 1.00 48.97 C
ANISOU 634 CD2 LEU A 104 7002 3943 7660 772 1489 651 C
ATOM 635 N LEU A 105 6.467 33.351 -34.974 1.00 58.31 N
ANISOU 635 N LEU A 105 8616 4957 8582 -142 1589 -84 N
ATOM 636 CA LEU A 105 7.483 34.385 -34.785 1.00 61.26 C
ANISOU 636 CA LEU A 105 9353 5098 8827 -378 1694 -174 C
ATOM 637 C LEU A 105 8.867 33.789 -34.568 1.00 60.45 C
ANISOU 637 C LEU A 105 9160 5147 8661 -744 1529 -328 C
ATOM 638 O LEU A 105 9.865 34.383 -34.989 1.00 65.34 O
ANISOU 638 O LEU A 105 9918 5697 9210 -973 1530 -348 O
ATOM 639 CB LEU A 105 7.100 35.311 -33.625 1.00 74.98 C
ANISOU 639 CB LEU A 105 11483 6509 10498 -320 1936 -214 C
ATOM 640 CG LEU A 105 6.235 36.517 -34.007 1.00 93.83 C
ANISOU 640 CG LEU A 105 14146 8621 12885 -25 2182 -50 C
ATOM 641 CD1 LEU A 105 4.769 36.123 -34.047 1.00 98.60 C
ANISOU 641 CD1 LEU A 105 14493 9328 13644 382 2242 130 C
ATOM 642 CD2 LEU A 105 6.466 37.691 -33.059 1.00 99.03 C
ANISOU 642 CD2 LEU A 105 15331 8923 13372 -108 2407 -130 C
ATOM 643 N VAL A 106 8.959 32.639 -33.897 1.00 58.93 N
ANISOU 643 N VAL A 106 8731 5161 8499 -801 1398 -419 N
ATOM 644 CA VAL A 106 10.270 32.050 -33.645 1.00 52.48 C
ANISOU 644 CA VAL A 106 7804 4506 7629 -1114 1247 -534 C
ATOM 645 C VAL A 106 10.873 31.531 -34.942 1.00 56.49 C
ANISOU 645 C VAL A 106 8072 5229 8161 -1149 1129 -463 C
ATOM 646 O VAL A 106 12.068 31.710 -35.206 1.00 74.85 O
ANISOU 646 O VAL A 106 10397 7598 10443 -1395 1094 -480 O
ATOM 647 CB VAL A 106 10.173 30.943 -32.578 1.00 57.98 C
ANISOU 647 CB VAL A 106 8337 5355 8338 -1131 1152 -637 C
ATOM 648 CG1 VAL A 106 11.521 30.222 -32.435 1.00 59.77 C
ANISOU 648 CG1 VAL A 106 8390 5795 8523 -1409 984 -716 C
ATOM 649 CG2 VAL A 106 9.756 31.531 -31.238 1.00 74.64 C
ANISOU 649 CG2 VAL A 106 10757 7217 10385 -1129 1292 -717 C
ATOM 650 N ASP A 107 10.056 30.896 -35.781 1.00 52.35 N
ANISOU 650 N ASP A 107 7356 4836 7700 -910 1070 -367 N
ATOM 651 CA ASP A 107 10.570 30.368 -37.038 1.00 54.38 C
ANISOU 651 CA ASP A 107 7456 5264 7942 -922 972 -300 C
ATOM 652 C ASP A 107 11.012 31.490 -37.977 1.00 63.75 C
ANISOU 652 C ASP A 107 8840 6298 9084 -967 1075 -215 C
ATOM 653 O ASP A 107 11.890 31.281 -38.820 1.00 74.72 O
ANISOU 653 O ASP A 107 10166 7788 10437 -1067 1047 -179 O
ATOM 654 CB ASP A 107 9.525 29.476 -37.713 1.00 69.42 C
ANISOU 654 CB ASP A 107 9175 7311 9892 -687 859 -215 C
ATOM 655 CG ASP A 107 9.542 28.044 -37.181 1.00 69.32 C
ANISOU 655 CG ASP A 107 8936 7510 9891 -711 725 -296 C
ATOM 656 OD1 ASP A 107 10.645 27.485 -37.007 1.00 71.07 O
ANISOU 656 OD1 ASP A 107 9087 7851 10065 -878 685 -371 O
ATOM 657 OD2 ASP A 107 8.455 27.485 -36.929 1.00 59.05 O
ANISOU 657 OD2 ASP A 107 7523 6259 8653 -562 668 -268 O
ATOM 658 N ILE A 108 10.419 32.679 -37.866 1.00 73.22 N
ANISOU 658 N ILE A 108 10299 7243 10281 -877 1221 -168 N
ATOM 659 CA ILE A 108 10.835 33.790 -38.722 1.00 67.39 C
ANISOU 659 CA ILE A 108 9789 6330 9489 -925 1336 -87 C
ATOM 660 C ILE A 108 12.122 34.414 -38.206 1.00 63.02 C
ANISOU 660 C ILE A 108 9387 5678 8879 -1276 1396 -171 C
ATOM 661 O ILE A 108 13.148 34.437 -38.898 1.00 63.10 O
ANISOU 661 O ILE A 108 9343 5765 8869 -1453 1387 -136 O
ATOM 662 CB ILE A 108 9.725 34.848 -38.818 1.00 61.92 C
ANISOU 662 CB ILE A 108 9343 5384 8801 -676 1487 14 C
ATOM 663 CG1 ILE A 108 8.577 34.336 -39.679 1.00 65.26 C
ANISOU 663 CG1 ILE A 108 9579 5935 9282 -359 1392 159 C
ATOM 664 CG2 ILE A 108 10.286 36.148 -39.372 1.00 53.56 C
ANISOU 664 CG2 ILE A 108 8609 4077 7662 -779 1644 64 C
ATOM 665 CD1 ILE A 108 7.444 35.293 -39.780 1.00 64.65 C
ANISOU 665 CD1 ILE A 108 9676 5654 9232 -72 1534 302 C
ATOM 666 N THR A 109 12.089 34.911 -36.967 1.00 54.26 N
ANISOU 666 N THR A 109 8476 4399 7741 -1394 1455 -272 N
ATOM 667 CA THR A 109 13.238 35.594 -36.382 1.00 48.37 C
ANISOU 667 CA THR A 109 7920 3534 6925 -1774 1477 -346 C
ATOM 668 C THR A 109 14.212 34.639 -35.707 1.00 66.43 C
ANISOU 668 C THR A 109 9934 6078 9229 -2028 1303 -434 C
ATOM 669 O THR A 109 15.426 34.872 -35.721 1.00 80.34 O
ANISOU 669 O THR A 109 11641 7922 10962 -2320 1239 -422 O
ATOM 670 CB THR A 109 12.754 36.626 -35.368 1.00 56.36 C
ANISOU 670 CB THR A 109 9336 4235 7844 -1776 1603 -408 C
ATOM 671 OG1 THR A 109 12.532 35.986 -34.107 1.00 55.25 O
ANISOU 671 OG1 THR A 109 9131 4173 7688 -1780 1519 -521 O
ATOM 672 CG2 THR A 109 11.445 37.256 -35.826 1.00 70.53 C
ANISOU 672 CG2 THR A 109 11347 5792 9660 -1409 1798 -305 C
ATOM 673 N GLU A 110 13.690 33.568 -35.115 1.00 66.04 N
ANISOU 673 N GLU A 110 9676 6197 9218 -1879 1205 -494 N
ATOM 674 CA GLU A 110 14.481 32.670 -34.276 1.00 60.90 C
ANISOU 674 CA GLU A 110 8809 5763 8566 -2080 1048 -580 C
ATOM 675 C GLU A 110 15.102 33.395 -33.082 1.00 72.73 C
ANISOU 675 C GLU A 110 10514 7174 9947 -2316 983 -648 C
ATOM 676 O GLU A 110 16.265 33.186 -32.731 1.00 71.17 O
ANISOU 676 O GLU A 110 10147 7169 9725 -2534 825 -638 O
ATOM 677 CB GLU A 110 15.502 31.907 -35.114 1.00 56.23 C
ANISOU 677 CB GLU A 110 7881 5461 8022 -2164 960 -503 C
ATOM 678 CG GLU A 110 14.796 30.740 -35.800 1.00 77.50 C
ANISOU 678 CG GLU A 110 10339 8345 10763 -1849 918 -464 C
ATOM 679 CD GLU A 110 15.667 30.007 -36.760 1.00 95.00 C
ANISOU 679 CD GLU A 110 12305 10794 12995 -1861 885 -375 C
ATOM 680 OE1 GLU A 110 16.887 30.226 -36.690 1.00100.17 O
ANISOU 680 OE1 GLU A 110 12878 11526 13656 -2114 882 -338 O
ATOM 681 OE2 GLU A 110 15.131 29.214 -37.569 1.00106.34 O
ANISOU 681 OE2 GLU A 110 13638 12333 14432 -1623 865 -329 O
ATOM 682 N SER A 111 14.309 34.285 -32.488 1.00 76.81 N
ANISOU 682 N SER A 111 11387 7418 10381 -2215 1100 -687 N
ATOM 683 CA SER A 111 14.554 34.886 -31.188 1.00 79.67 C
ANISOU 683 CA SER A 111 11996 7684 10592 -2339 1047 -762 C
ATOM 684 C SER A 111 13.278 34.721 -30.380 1.00 78.01 C
ANISOU 684 C SER A 111 11960 7322 10357 -2082 1169 -822 C
ATOM 685 O SER A 111 12.183 34.608 -30.935 1.00 80.73 O
ANISOU 685 O SER A 111 12310 7561 10802 -1809 1331 -777 O
ATOM 686 CB SER A 111 14.946 36.371 -31.278 1.00 96.24 C
ANISOU 686 CB SER A 111 14432 9566 12569 -2481 1120 -731 C
ATOM 687 OG SER A 111 16.221 36.527 -31.873 1.00110.03 O
ANISOU 687 OG SER A 111 15999 11462 14347 -2746 1004 -666 O
ATOM 688 N TRP A 112 13.413 34.694 -29.061 1.00 77.72 N
ANISOU 688 N TRP A 112 12058 7275 10196 -2156 1098 -904 N
ATOM 689 CA TRP A 112 12.238 34.646 -28.198 1.00 77.55 C
ANISOU 689 CA TRP A 112 12240 7094 10131 -1910 1250 -945 C
ATOM 690 C TRP A 112 11.851 36.063 -27.797 1.00 77.76 C
ANISOU 690 C TRP A 112 12736 6816 9992 -1860 1436 -931 C
ATOM 691 O TRP A 112 12.655 36.786 -27.197 1.00 72.41 O
ANISOU 691 O TRP A 112 12288 6082 9143 -2106 1355 -969 O
ATOM 692 CB TRP A 112 12.488 33.790 -26.960 1.00 68.54 C
ANISOU 692 CB TRP A 112 11024 6093 8925 -1981 1104 -1033 C
ATOM 693 CG TRP A 112 11.261 33.686 -26.100 1.00 51.54 C
ANISOU 693 CG TRP A 112 9062 3783 6736 -1714 1289 -1058 C
ATOM 694 CD1 TRP A 112 10.942 34.452 -25.021 1.00 59.19 C
ANISOU 694 CD1 TRP A 112 10428 4545 7516 -1681 1407 -1084 C
ATOM 695 CD2 TRP A 112 10.161 32.792 -26.291 1.00 50.38 C
ANISOU 695 CD2 TRP A 112 8717 3672 6753 -1431 1405 -1037 C
ATOM 696 NE1 TRP A 112 9.723 34.076 -24.512 1.00 63.10 N
ANISOU 696 NE1 TRP A 112 10967 4960 8050 -1378 1602 -1067 N
ATOM 697 CE2 TRP A 112 9.223 33.058 -25.277 1.00 57.59 C
ANISOU 697 CE2 TRP A 112 9891 4410 7581 -1224 1598 -1036 C
ATOM 698 CE3 TRP A 112 9.885 31.782 -27.216 1.00 55.63 C
ANISOU 698 CE3 TRP A 112 9007 4502 7627 -1339 1368 -1010 C
ATOM 699 CZ2 TRP A 112 8.030 32.356 -25.167 1.00 64.88 C
ANISOU 699 CZ2 TRP A 112 10674 5332 8647 -923 1755 -992 C
ATOM 700 CZ3 TRP A 112 8.700 31.081 -27.102 1.00 52.82 C
ANISOU 700 CZ3 TRP A 112 8530 4128 7413 -1061 1505 -985 C
ATOM 701 CH2 TRP A 112 7.788 31.370 -26.084 1.00 65.25 C
ANISOU 701 CH2 TRP A 112 10331 5540 8921 -851 1696 -968 C
ATOM 702 N LEU A 113 10.620 36.454 -28.127 1.00 79.48 N
ANISOU 702 N LEU A 113 13093 6845 10259 -1533 1690 -859 N
ATOM 703 CA LEU A 113 10.178 37.820 -27.905 1.00 77.69 C
ANISOU 703 CA LEU A 113 13308 6335 9874 -1432 1909 -817 C
ATOM 704 C LEU A 113 9.026 37.948 -26.914 1.00 84.67 C
ANISOU 704 C LEU A 113 14420 7066 10684 -1142 2134 -800 C
ATOM 705 O LEU A 113 8.522 39.057 -26.731 1.00104.05 O
ANISOU 705 O LEU A 113 17246 9286 13000 -1002 2361 -743 O
ATOM 706 CB LEU A 113 9.798 38.455 -29.242 1.00 77.25 C
ANISOU 706 CB LEU A 113 13259 6177 9915 -1271 2049 -696 C
ATOM 707 CG LEU A 113 10.808 38.259 -30.380 1.00 79.81 C
ANISOU 707 CG LEU A 113 13335 6656 10333 -1508 1872 -680 C
ATOM 708 CD1 LEU A 113 10.183 38.697 -31.687 1.00 72.08 C
ANISOU 708 CD1 LEU A 113 12352 5573 9462 -1270 2029 -542 C
ATOM 709 CD2 LEU A 113 12.097 39.023 -30.105 1.00 83.63 C
ANISOU 709 CD2 LEU A 113 13994 7129 10651 -1888 1743 -736 C
ATOM 710 N PHE A 114 8.597 36.868 -26.260 1.00 86.44 N
ANISOU 710 N PHE A 114 14444 7414 10985 -1041 2099 -836 N
ATOM 711 CA PHE A 114 7.489 36.942 -25.312 1.00 86.98 C
ANISOU 711 CA PHE A 114 14698 7355 10995 -755 2336 -794 C
ATOM 712 C PHE A 114 7.934 36.895 -23.855 1.00 87.89 C
ANISOU 712 C PHE A 114 15065 7446 10883 -934 2268 -903 C
ATOM 713 O PHE A 114 7.095 36.695 -22.968 1.00 87.78 O
ANISOU 713 O PHE A 114 15160 7367 10824 -722 2443 -875 O
ATOM 714 CB PHE A 114 6.465 35.833 -25.582 1.00 80.76 C
ANISOU 714 CB PHE A 114 13530 6696 10461 -457 2402 -720 C
ATOM 715 CG PHE A 114 6.081 35.684 -27.026 1.00 74.12 C
ANISOU 715 CG PHE A 114 12399 5907 9856 -298 2416 -604 C
ATOM 716 CD1 PHE A 114 6.797 34.862 -27.885 1.00 81.78 C
ANISOU 716 CD1 PHE A 114 13042 7067 10963 -491 2180 -655 C
ATOM 717 CD2 PHE A 114 4.986 36.368 -27.528 1.00 69.81 C
ANISOU 717 CD2 PHE A 114 11905 5231 9389 58 2667 -420 C
ATOM 718 CE1 PHE A 114 6.424 34.739 -29.212 1.00 87.62 C
ANISOU 718 CE1 PHE A 114 13554 7832 11903 -341 2196 -535 C
ATOM 719 CE2 PHE A 114 4.615 36.247 -28.849 1.00 73.26 C
ANISOU 719 CE2 PHE A 114 12081 5719 10036 221 2657 -286 C
ATOM 720 CZ PHE A 114 5.331 35.435 -29.689 1.00 81.90 C
ANISOU 720 CZ PHE A 114 12892 6971 11257 17 2421 -347 C
ATOM 721 N GLY A 115 9.221 37.083 -23.587 1.00 89.02 N
ANISOU 721 N GLY A 115 15294 7643 10885 -1312 2024 -1001 N
ATOM 722 CA GLY A 115 9.688 37.233 -22.227 1.00 93.23 C
ANISOU 722 CA GLY A 115 16129 8121 11175 -1494 1952 -1081 C
ATOM 723 C GLY A 115 9.974 35.903 -21.549 1.00 86.48 C
ANISOU 723 C GLY A 115 14994 7489 10376 -1564 1749 -1153 C
ATOM 724 O GLY A 115 9.738 34.817 -22.087 1.00 91.36 O
ANISOU 724 O GLY A 115 15193 8303 11216 -1459 1683 -1148 O
ATOM 725 N HIS A 116 10.514 36.010 -20.332 1.00 80.00 N
ANISOU 725 N HIS A 116 14439 6628 9328 -1752 1647 -1216 N
ATOM 726 CA HIS A 116 10.980 34.835 -19.605 1.00 75.28 C
ANISOU 726 CA HIS A 116 13618 6240 8746 -1855 1424 -1282 C
ATOM 727 C HIS A 116 9.847 33.860 -19.311 1.00 73.01 C
ANISOU 727 C HIS A 116 13163 5995 8582 -1535 1586 -1264 C
ATOM 728 O HIS A 116 10.052 32.642 -19.338 1.00 71.56 O
ANISOU 728 O HIS A 116 12617 6040 8531 -1546 1422 -1301 O
ATOM 729 CB HIS A 116 11.624 35.258 -18.287 1.00 88.69 C
ANISOU 729 CB HIS A 116 15709 7839 10152 -2084 1320 -1331 C
ATOM 730 CG HIS A 116 12.825 36.140 -18.444 1.00108.85 C
ANISOU 730 CG HIS A 116 18414 10368 12576 -2444 1126 -1341 C
ATOM 731 ND1 HIS A 116 12.731 37.462 -18.819 1.00117.27 N
ANISOU 731 ND1 HIS A 116 19832 11204 13523 -2480 1283 -1308 N
ATOM 732 CD2 HIS A 116 14.144 35.900 -18.249 1.00113.87 C
ANISOU 732 CD2 HIS A 116 18899 11184 13183 -2784 797 -1366 C
ATOM 733 CE1 HIS A 116 13.939 37.998 -18.856 1.00119.74 C
ANISOU 733 CE1 HIS A 116 20208 11550 13738 -2846 1052 -1320 C
ATOM 734 NE2 HIS A 116 14.816 37.070 -18.517 1.00117.55 N
ANISOU 734 NE2 HIS A 116 19612 11528 13523 -3035 754 -1346 N
ATOM 735 N ALA A 117 8.643 34.373 -19.047 1.00 65.84 N
ANISOU 735 N ALA A 117 12504 4877 7636 -1241 1920 -1191 N
ATOM 736 CA ALA A 117 7.573 33.540 -18.502 1.00 60.24 C
ANISOU 736 CA ALA A 117 11686 4191 7010 -956 2095 -1152 C
ATOM 737 C ALA A 117 6.837 32.768 -19.589 1.00 73.04 C
ANISOU 737 C ALA A 117 12847 5956 8949 -730 2154 -1089 C
ATOM 738 O ALA A 117 6.590 31.562 -19.446 1.00 88.93 O
ANISOU 738 O ALA A 117 14559 8138 11093 -662 2091 -1109 O
ATOM 739 CB ALA A 117 6.586 34.402 -17.714 1.00 66.74 C
ANISOU 739 CB ALA A 117 12947 4746 7664 -724 2450 -1061 C
ATOM 740 N LEU A 118 6.481 33.440 -20.688 1.00 71.86 N
ANISOU 740 N LEU A 118 12650 5734 8918 -614 2273 -1005 N
ATOM 741 CA LEU A 118 5.862 32.723 -21.800 1.00 68.04 C
ANISOU 741 CA LEU A 118 11733 5385 8735 -425 2297 -933 C
ATOM 742 C LEU A 118 6.821 31.722 -22.429 1.00 68.39 C
ANISOU 742 C LEU A 118 11418 5676 8890 -667 1979 -1033 C
ATOM 743 O LEU A 118 6.378 30.798 -23.127 1.00 77.96 O
ANISOU 743 O LEU A 118 12263 7028 10329 -548 1963 -1003 O
ATOM 744 CB LEU A 118 5.318 33.701 -22.852 1.00 72.48 C
ANISOU 744 CB LEU A 118 12336 5813 9388 -243 2480 -802 C
ATOM 745 CG LEU A 118 4.197 34.626 -22.355 1.00 72.56 C
ANISOU 745 CG LEU A 118 12639 5610 9320 67 2839 -654 C
ATOM 746 CD1 LEU A 118 3.920 35.712 -23.383 1.00 66.81 C
ANISOU 746 CD1 LEU A 118 12000 4754 8632 201 2977 -533 C
ATOM 747 CD2 LEU A 118 2.944 33.816 -22.050 1.00 71.96 C
ANISOU 747 CD2 LEU A 118 12298 5615 9429 388 3019 -527 C
ATOM 748 N CYS A 119 8.126 31.892 -22.200 1.00 64.34 N
ANISOU 748 N CYS A 119 10994 5229 8224 -1000 1731 -1132 N
ATOM 749 CA CYS A 119 9.096 30.866 -22.561 1.00 67.53 C
ANISOU 749 CA CYS A 119 11052 5903 8703 -1217 1437 -1202 C
ATOM 750 C CYS A 119 8.769 29.536 -21.896 1.00 69.84 C
ANISOU 750 C CYS A 119 11148 6345 9044 -1131 1395 -1245 C
ATOM 751 O CYS A 119 9.037 28.470 -22.455 1.00 83.96 O
ANISOU 751 O CYS A 119 12580 8353 10966 -1170 1251 -1269 O
ATOM 752 CB CYS A 119 10.493 31.336 -22.153 1.00 63.66 C
ANISOU 752 CB CYS A 119 10695 5459 8034 -1556 1201 -1258 C
ATOM 753 SG CYS A 119 11.834 30.156 -22.342 1.00 63.25 S
ANISOU 753 SG CYS A 119 10229 5761 8041 -1805 847 -1299 S
ATOM 754 N LYS A 120 8.185 29.574 -20.701 1.00 71.85 N
ANISOU 754 N LYS A 120 11642 6481 9177 -1010 1532 -1249 N
ATOM 755 CA LYS A 120 7.787 28.339 -20.035 1.00 67.02 C
ANISOU 755 CA LYS A 120 10867 5991 8606 -910 1523 -1277 C
ATOM 756 C LYS A 120 6.334 27.957 -20.314 1.00 56.79 C
ANISOU 756 C LYS A 120 9418 4652 7509 -583 1790 -1181 C
ATOM 757 O LYS A 120 6.025 26.767 -20.411 1.00 56.84 O
ANISOU 757 O LYS A 120 9129 4816 7651 -518 1752 -1192 O
ATOM 758 CB LYS A 120 8.038 28.459 -18.531 1.00 67.04 C
ANISOU 758 CB LYS A 120 11192 5913 8368 -978 1507 -1321 C
ATOM 759 CG LYS A 120 9.513 28.434 -18.146 1.00 63.40 C
ANISOU 759 CG LYS A 120 10768 5565 7755 -1301 1190 -1401 C
ATOM 760 CD LYS A 120 9.705 28.803 -16.678 1.00 50.69 C
ANISOU 760 CD LYS A 120 9555 3818 5887 -1373 1196 -1429 C
ATOM 761 CE LYS A 120 10.460 27.714 -15.918 1.00 64.24 C
ANISOU 761 CE LYS A 120 11140 5724 7544 -1496 952 -1489 C
ATOM 762 NZ LYS A 120 11.901 27.644 -16.316 1.00 74.34 N
ANISOU 762 NZ LYS A 120 12229 7193 8823 -1784 629 -1514 N
ATOM 763 N VAL A 121 5.425 28.925 -20.438 1.00 52.38 N
ANISOU 763 N VAL A 121 9033 3894 6975 -367 2062 -1065 N
ATOM 764 CA VAL A 121 4.015 28.583 -20.606 1.00 42.52 C
ANISOU 764 CA VAL A 121 7590 2633 5934 -36 2316 -920 C
ATOM 765 C VAL A 121 3.767 27.990 -21.992 1.00 57.01 C
ANISOU 765 C VAL A 121 8999 4604 8060 28 2252 -874 C
ATOM 766 O VAL A 121 3.222 26.892 -22.129 1.00 72.72 O
ANISOU 766 O VAL A 121 10660 6735 10234 126 2248 -846 O
ATOM 767 CB VAL A 121 3.124 29.808 -20.350 1.00 55.80 C
ANISOU 767 CB VAL A 121 9551 4090 7560 201 2631 -768 C
ATOM 768 CG1 VAL A 121 1.693 29.515 -20.779 1.00 70.44 C
ANISOU 768 CG1 VAL A 121 11096 5986 9684 549 2864 -558 C
ATOM 769 CG2 VAL A 121 3.156 30.165 -18.884 1.00 48.20 C
ANISOU 769 CG2 VAL A 121 8993 2991 6328 172 2735 -797 C
ATOM 770 N ILE A 122 4.153 28.724 -23.039 1.00 66.30 N
ANISOU 770 N ILE A 122 10184 5730 9276 -31 2202 -855 N
ATOM 771 CA ILE A 122 3.838 28.307 -24.407 1.00 75.21 C
ANISOU 771 CA ILE A 122 10901 7026 10647 50 2113 -755 C
ATOM 772 C ILE A 122 4.343 26.898 -24.680 1.00 72.51 C
ANISOU 772 C ILE A 122 10185 7019 10346 -117 1818 -825 C
ATOM 773 O ILE A 122 3.551 26.065 -25.162 1.00 81.83 O
ANISOU 773 O ILE A 122 10993 8401 11696 21 1773 -707 O
ATOM 774 CB ILE A 122 4.409 29.338 -25.405 1.00 86.10 C
ANISOU 774 CB ILE A 122 12395 8328 11992 -42 2061 -731 C
ATOM 775 CG1 ILE A 122 3.747 30.687 -25.180 1.00 81.16 C
ANISOU 775 CG1 ILE A 122 12128 7391 11316 174 2368 -624 C
ATOM 776 CG2 ILE A 122 4.202 28.855 -26.841 1.00 96.01 C
ANISOU 776 CG2 ILE A 122 13203 9860 13416 8 1876 -603 C
ATOM 777 CD1 ILE A 122 2.251 30.637 -25.157 1.00 73.12 C
ANISOU 777 CD1 ILE A 122 10930 6369 10483 568 2611 -405 C
ATOM 778 N PRO A 123 5.620 26.554 -24.455 1.00 57.40 N
ANISOU 778 N PRO A 123 8336 5184 8288 -406 1607 -991 N
ATOM 779 CA PRO A 123 6.049 25.164 -24.647 1.00 46.41 C
ANISOU 779 CA PRO A 123 6618 4091 6925 -510 1374 -1039 C
ATOM 780 C PRO A 123 5.278 24.181 -23.790 1.00 56.37 C
ANISOU 780 C PRO A 123 7790 5399 8228 -383 1451 -1038 C
ATOM 781 O PRO A 123 5.018 23.056 -24.225 1.00 61.20 O
ANISOU 781 O PRO A 123 8081 6236 8935 -358 1328 -999 O
ATOM 782 CB PRO A 123 7.546 25.211 -24.292 1.00 32.06 C
ANISOU 782 CB PRO A 123 4950 2300 4932 -813 1194 -1189 C
ATOM 783 CG PRO A 123 7.948 26.638 -24.515 1.00 34.29 C
ANISOU 783 CG PRO A 123 5527 2362 5141 -911 1264 -1189 C
ATOM 784 CD PRO A 123 6.745 27.446 -24.115 1.00 48.99 C
ANISOU 784 CD PRO A 123 7631 3949 7033 -659 1563 -1114 C
ATOM 785 N TYR A 124 4.917 24.583 -22.578 1.00 56.49 N
ANISOU 785 N TYR A 124 8120 5184 8158 -309 1663 -1080 N
ATOM 786 CA TYR A 124 4.207 23.674 -21.685 1.00 53.19 C
ANISOU 786 CA TYR A 124 7648 4790 7771 -188 1769 -1076 C
ATOM 787 C TYR A 124 2.817 23.356 -22.217 1.00 63.80 C
ANISOU 787 C TYR A 124 8663 6222 9357 62 1897 -872 C
ATOM 788 O TYR A 124 2.395 22.192 -22.234 1.00 66.70 O
ANISOU 788 O TYR A 124 8749 6776 9819 78 1823 -836 O
ATOM 789 CB TYR A 124 4.139 24.262 -20.270 1.00 50.16 C
ANISOU 789 CB TYR A 124 7681 4199 7178 -156 1933 -1105 C
ATOM 790 CG TYR A 124 3.183 23.562 -19.325 1.00 60.33 C
ANISOU 790 CG TYR A 124 8937 5492 8493 19 2105 -1035 C
ATOM 791 CD1 TYR A 124 3.549 22.374 -18.696 1.00 54.12 C
ANISOU 791 CD1 TYR A 124 8084 4846 7635 -79 1968 -1125 C
ATOM 792 CD2 TYR A 124 1.919 24.097 -19.046 1.00 57.47 C
ANISOU 792 CD2 TYR A 124 8610 5004 8221 284 2408 -853 C
ATOM 793 CE1 TYR A 124 2.688 21.734 -17.816 1.00 43.72 C
ANISOU 793 CE1 TYR A 124 6754 3523 6334 63 2130 -1053 C
ATOM 794 CE2 TYR A 124 1.054 23.463 -18.168 1.00 53.91 C
ANISOU 794 CE2 TYR A 124 8118 4568 7799 422 2570 -765 C
ATOM 795 CZ TYR A 124 1.443 22.285 -17.558 1.00 45.41 C
ANISOU 795 CZ TYR A 124 6993 3612 6650 303 2433 -873 C
ATOM 796 OH TYR A 124 0.597 21.642 -16.684 1.00 48.99 O
ANISOU 796 OH TYR A 124 7420 4066 7127 424 2598 -780 O
ATOM 797 N LEU A 125 2.079 24.387 -22.625 1.00 66.01 N
ANISOU 797 N LEU A 125 8980 6363 9736 253 2088 -721 N
ATOM 798 CA LEU A 125 0.793 24.167 -23.269 1.00 61.34 C
ANISOU 798 CA LEU A 125 8019 5894 9395 476 2166 -483 C
ATOM 799 C LEU A 125 0.960 23.326 -24.528 1.00 62.91 C
ANISOU 799 C LEU A 125 7823 6391 9688 347 1842 -446 C
ATOM 800 O LEU A 125 0.208 22.371 -24.761 1.00 61.42 O
ANISOU 800 O LEU A 125 7305 6386 9645 383 1773 -337 O
ATOM 801 CB LEU A 125 0.142 25.511 -23.574 1.00 55.32 C
ANISOU 801 CB LEU A 125 7383 4936 8702 711 2409 -317 C
ATOM 802 CG LEU A 125 -0.103 26.401 -22.356 1.00 48.50 C
ANISOU 802 CG LEU A 125 6970 3763 7693 853 2744 -324 C
ATOM 803 CD1 LEU A 125 -0.902 27.617 -22.762 1.00 44.10 C
ANISOU 803 CD1 LEU A 125 6471 3095 7189 1100 2953 -97 C
ATOM 804 CD2 LEU A 125 -0.801 25.662 -21.208 1.00 54.57 C
ANISOU 804 CD2 LEU A 125 7704 4582 8450 929 2872 -271 C
ATOM 805 N GLN A 126 1.964 23.658 -25.341 1.00 58.26 N
ANISOU 805 N GLN A 126 7292 5842 9003 182 1646 -534 N
ATOM 806 CA GLN A 126 2.246 22.870 -26.535 1.00 54.00 C
ANISOU 806 CA GLN A 126 6463 5550 8504 62 1359 -513 C
ATOM 807 C GLN A 126 2.583 21.429 -26.170 1.00 51.22 C
ANISOU 807 C GLN A 126 5994 5363 8103 -73 1207 -621 C
ATOM 808 O GLN A 126 2.081 20.490 -26.803 1.00 54.38 O
ANISOU 808 O GLN A 126 6127 5942 8593 -85 1064 -539 O
ATOM 809 CB GLN A 126 3.372 23.543 -27.323 1.00 52.69 C
ANISOU 809 CB GLN A 126 6430 5364 8225 -81 1234 -590 C
ATOM 810 CG GLN A 126 4.345 22.624 -28.021 1.00 55.24 C
ANISOU 810 CG GLN A 126 6627 5891 8470 -273 973 -679 C
ATOM 811 CD GLN A 126 3.678 21.654 -28.976 1.00 71.22 C
ANISOU 811 CD GLN A 126 8356 8111 10593 -239 812 -566 C
ATOM 812 OE1 GLN A 126 2.467 21.700 -29.179 1.00 79.84 O
ANISOU 812 OE1 GLN A 126 9286 9216 11834 -95 860 -402 O
ATOM 813 NE2 GLN A 126 4.467 20.768 -29.570 1.00 76.99 N
ANISOU 813 NE2 GLN A 126 9025 8991 11234 -375 619 -637 N
ATOM 814 N ALA A 127 3.428 21.234 -25.151 1.00 43.31 N
ANISOU 814 N ALA A 127 5215 4297 6944 -182 1228 -796 N
ATOM 815 CA ALA A 127 3.731 19.881 -24.697 1.00 36.54 C
ANISOU 815 CA ALA A 127 4279 3576 6028 -275 1114 -888 C
ATOM 816 C ALA A 127 2.495 19.205 -24.123 1.00 44.26 C
ANISOU 816 C ALA A 127 5122 4562 7132 -147 1246 -791 C
ATOM 817 O ALA A 127 2.266 18.013 -24.363 1.00 41.73 O
ANISOU 817 O ALA A 127 4612 4398 6847 -199 1122 -775 O
ATOM 818 CB ALA A 127 4.853 19.913 -23.658 1.00 27.32 C
ANISOU 818 CB ALA A 127 3382 2335 4664 -403 1105 -1068 C
ATOM 819 N VAL A 128 1.680 19.955 -23.378 1.00 50.66 N
ANISOU 819 N VAL A 128 6043 5195 8010 24 1515 -712 N
ATOM 820 CA VAL A 128 0.467 19.388 -22.805 1.00 44.85 C
ANISOU 820 CA VAL A 128 5154 4467 7420 161 1685 -584 C
ATOM 821 C VAL A 128 -0.515 19.013 -23.907 1.00 42.41 C
ANISOU 821 C VAL A 128 4445 4341 7330 200 1575 -371 C
ATOM 822 O VAL A 128 -1.184 17.973 -23.836 1.00 45.69 O
ANISOU 822 O VAL A 128 4636 4880 7845 170 1534 -294 O
ATOM 823 CB VAL A 128 -0.154 20.364 -21.790 1.00 45.54 C
ANISOU 823 CB VAL A 128 5479 4303 7521 373 2045 -523 C
ATOM 824 CG1 VAL A 128 -1.660 20.187 -21.748 1.00 50.21 C
ANISOU 824 CG1 VAL A 128 5779 4936 8364 581 2245 -267 C
ATOM 825 CG2 VAL A 128 0.455 20.131 -20.415 1.00 39.45 C
ANISOU 825 CG2 VAL A 128 5067 3382 6540 317 2145 -711 C
ATOM 826 N SER A 129 -0.598 19.839 -24.960 1.00 36.45 N
ANISOU 826 N SER A 129 3608 3604 6639 243 1505 -268 N
ATOM 827 CA SER A 129 -1.522 19.551 -26.054 1.00 42.80 C
ANISOU 827 CA SER A 129 4047 4584 7632 265 1359 -50 C
ATOM 828 C SER A 129 -1.117 18.295 -26.830 1.00 42.42 C
ANISOU 828 C SER A 129 3869 4729 7519 39 1034 -121 C
ATOM 829 O SER A 129 -1.985 17.555 -27.314 1.00 48.05 O
ANISOU 829 O SER A 129 4306 5587 8363 -7 907 32 O
ATOM 830 CB SER A 129 -1.616 20.764 -26.980 1.00 57.23 C
ANISOU 830 CB SER A 129 5870 6368 9507 375 1357 69 C
ATOM 831 OG SER A 129 -0.610 20.750 -27.981 1.00 64.52 O
ANISOU 831 OG SER A 129 6869 7353 10294 211 1107 -47 O
ATOM 832 N VAL A 130 0.187 18.030 -26.951 1.00 47.75 N
ANISOU 832 N VAL A 130 4750 5403 7989 -105 904 -334 N
ATOM 833 CA VAL A 130 0.645 16.770 -27.528 1.00 47.81 C
ANISOU 833 CA VAL A 130 4709 5556 7901 -282 659 -410 C
ATOM 834 C VAL A 130 0.188 15.605 -26.660 1.00 51.06 C
ANISOU 834 C VAL A 130 5071 5998 8330 -325 702 -431 C
ATOM 835 O VAL A 130 -0.402 14.635 -27.148 1.00 52.61 O
ANISOU 835 O VAL A 130 5105 6308 8578 -423 553 -350 O
ATOM 836 CB VAL A 130 2.175 16.796 -27.698 1.00 33.42 C
ANISOU 836 CB VAL A 130 3105 3723 5869 -380 571 -603 C
ATOM 837 CG1 VAL A 130 2.705 15.428 -28.105 1.00 31.28 C
ANISOU 837 CG1 VAL A 130 2837 3572 5475 -514 385 -682 C
ATOM 838 CG2 VAL A 130 2.577 17.865 -28.703 1.00 47.09 C
ANISOU 838 CG2 VAL A 130 4870 5431 7591 -362 521 -562 C
ATOM 839 N SER A 131 0.428 15.699 -25.349 1.00 50.78 N
ANISOU 839 N SER A 131 5204 5848 8240 -264 906 -534 N
ATOM 840 CA SER A 131 0.034 14.613 -24.460 1.00 40.52 C
ANISOU 840 CA SER A 131 3894 4560 6943 -294 975 -557 C
ATOM 841 C SER A 131 -1.472 14.375 -24.514 1.00 45.43 C
ANISOU 841 C SER A 131 4225 5235 7802 -245 1045 -326 C
ATOM 842 O SER A 131 -1.922 13.236 -24.679 1.00 32.41 O
ANISOU 842 O SER A 131 2444 3683 6186 -371 931 -282 O
ATOM 843 CB SER A 131 0.491 14.910 -23.027 1.00 44.31 C
ANISOU 843 CB SER A 131 4641 4884 7312 -218 1194 -690 C
ATOM 844 OG SER A 131 -0.092 13.963 -22.134 1.00 54.27 O
ANISOU 844 OG SER A 131 5887 6135 8599 -212 1308 -677 O
ATOM 845 N VAL A 132 -2.268 15.434 -24.348 1.00 51.83 N
ANISOU 845 N VAL A 132 4936 5979 8780 -64 1246 -161 N
ATOM 846 CA VAL A 132 -3.720 15.274 -24.381 1.00 44.40 C
ANISOU 846 CA VAL A 132 3656 5116 8098 4 1330 109 C
ATOM 847 C VAL A 132 -4.165 14.692 -25.720 1.00 50.62 C
ANISOU 847 C VAL A 132 4163 6099 8970 -166 1001 245 C
ATOM 848 O VAL A 132 -5.100 13.880 -25.785 1.00 52.93 O
ANISOU 848 O VAL A 132 4226 6506 9379 -262 924 402 O
ATOM 849 CB VAL A 132 -4.411 16.616 -24.075 1.00 50.80 C
ANISOU 849 CB VAL A 132 4422 5818 9064 277 1621 288 C
ATOM 850 CG1 VAL A 132 -5.889 16.553 -24.421 1.00 44.08 C
ANISOU 850 CG1 VAL A 132 3196 5103 8450 348 1619 620 C
ATOM 851 CG2 VAL A 132 -4.201 16.977 -22.622 1.00 63.95 C
ANISOU 851 CG2 VAL A 132 6398 7265 10635 427 1967 178 C
ATOM 852 N ALA A 133 -3.495 15.088 -26.804 1.00 52.06 N
ANISOU 852 N ALA A 133 4419 6314 9048 -223 784 185 N
ATOM 853 CA ALA A 133 -3.800 14.541 -28.123 1.00 49.06 C
ANISOU 853 CA ALA A 133 3865 6089 8687 -397 450 289 C
ATOM 854 C ALA A 133 -3.494 13.052 -28.182 1.00 58.47 C
ANISOU 854 C ALA A 133 5145 7332 9739 -634 266 165 C
ATOM 855 O ALA A 133 -4.386 12.220 -28.386 1.00 65.16 O
ANISOU 855 O ALA A 133 5848 8282 10629 -766 134 300 O
ATOM 856 CB ALA A 133 -3.004 15.288 -29.191 1.00 36.80 C
ANISOU 856 CB ALA A 133 2449 4524 7010 -388 302 226 C
ATOM 857 N VAL A 134 -2.220 12.698 -28.027 1.00 57.95 N
ANISOU 857 N VAL A 134 5386 7199 9432 -678 248 -87 N
ATOM 858 CA VAL A 134 -1.831 11.305 -28.182 1.00 47.08 C
ANISOU 858 CA VAL A 134 4147 5850 7891 -867 89 -201 C
ATOM 859 C VAL A 134 -2.526 10.428 -27.146 1.00 48.25 C
ANISOU 859 C VAL A 134 4227 5987 8119 -916 215 -170 C
ATOM 860 O VAL A 134 -2.799 9.252 -27.404 1.00 57.49 O
ANISOU 860 O VAL A 134 5413 7194 9235 -1107 64 -161 O
ATOM 861 CB VAL A 134 -0.299 11.187 -28.103 1.00 42.11 C
ANISOU 861 CB VAL A 134 3829 5162 7010 -847 96 -441 C
ATOM 862 CG1 VAL A 134 0.163 11.345 -26.662 1.00 53.69 C
ANISOU 862 CG1 VAL A 134 5418 6538 8442 -734 342 -567 C
ATOM 863 CG2 VAL A 134 0.144 9.860 -28.671 1.00 28.29 C
ANISOU 863 CG2 VAL A 134 2245 3437 5068 -1008 -88 -524 C
ATOM 864 N LEU A 135 -2.858 10.982 -25.976 1.00 53.94 N
ANISOU 864 N LEU A 135 4901 6637 8956 -749 503 -143 N
ATOM 865 CA LEU A 135 -3.600 10.205 -24.984 1.00 41.41 C
ANISOU 865 CA LEU A 135 3240 5032 7460 -778 659 -86 C
ATOM 866 C LEU A 135 -5.042 9.977 -25.421 1.00 47.87 C
ANISOU 866 C LEU A 135 3755 5980 8453 -851 563 195 C
ATOM 867 O LEU A 135 -5.560 8.860 -25.311 1.00 54.79 O
ANISOU 867 O LEU A 135 4613 6905 9300 -1021 483 238 O
ATOM 868 CB LEU A 135 -3.569 10.904 -23.625 1.00 37.25 C
ANISOU 868 CB LEU A 135 2814 4375 6966 -556 1011 -125 C
ATOM 869 CG LEU A 135 -2.557 10.370 -22.608 1.00 30.68 C
ANISOU 869 CG LEU A 135 2325 3432 5899 -544 1109 -369 C
ATOM 870 CD1 LEU A 135 -2.565 11.221 -21.349 1.00 36.74 C
ANISOU 870 CD1 LEU A 135 3240 4047 6673 -335 1434 -398 C
ATOM 871 CD2 LEU A 135 -2.836 8.913 -22.263 1.00 31.41 C
ANISOU 871 CD2 LEU A 135 2441 3543 5949 -696 1076 -385 C
ATOM 872 N THR A 136 -5.702 11.020 -25.927 1.00 49.31 N
ANISOU 872 N THR A 136 3737 6226 8772 -723 560 387 N
ATOM 873 CA THR A 136 -7.083 10.873 -26.370 1.00 52.44 C
ANISOU 873 CA THR A 136 3863 6771 9291 -774 449 653 C
ATOM 874 C THR A 136 -7.198 9.840 -27.479 1.00 49.24 C
ANISOU 874 C THR A 136 3483 6478 8748 -1066 84 646 C
ATOM 875 O THR A 136 -8.133 9.028 -27.494 1.00 59.42 O
ANISOU 875 O THR A 136 4650 7853 10074 -1220 -2 764 O
ATOM 876 CB THR A 136 -7.609 12.217 -26.859 1.00 57.25 C
ANISOU 876 CB THR A 136 4289 7415 10048 -572 489 844 C
ATOM 877 OG1 THR A 136 -7.539 13.173 -25.796 1.00 56.80 O
ANISOU 877 OG1 THR A 136 4282 7215 10085 -294 862 847 O
ATOM 878 CG2 THR A 136 -9.039 12.080 -27.337 1.00 69.43 C
ANISOU 878 CG2 THR A 136 5534 9117 11728 -620 363 1128 C
ATOM 879 N LEU A 137 -6.255 9.858 -28.421 1.00 46.14 N
ANISOU 879 N LEU A 137 3278 6068 8187 -1144 -121 504 N
ATOM 880 CA LEU A 137 -6.286 8.888 -29.508 1.00 51.58 C
ANISOU 880 CA LEU A 137 4085 6815 8698 -1401 -439 474 C
ATOM 881 C LEU A 137 -6.144 7.461 -28.984 1.00 51.95 C
ANISOU 881 C LEU A 137 4312 6812 8616 -1592 -439 351 C
ATOM 882 O LEU A 137 -6.781 6.538 -29.505 1.00 64.36 O
ANISOU 882 O LEU A 137 5899 8424 10129 -1802 -622 399 O
ATOM 883 CB LEU A 137 -5.179 9.202 -30.512 1.00 53.21 C
ANISOU 883 CB LEU A 137 4513 6976 8729 -1407 -598 335 C
ATOM 884 CG LEU A 137 -5.419 10.484 -31.313 1.00 55.77 C
ANISOU 884 CG LEU A 137 4676 7352 9163 -1272 -663 480 C
ATOM 885 CD1 LEU A 137 -4.125 10.959 -31.946 1.00 47.42 C
ANISOU 885 CD1 LEU A 137 3837 6215 7965 -1232 -718 320 C
ATOM 886 CD2 LEU A 137 -6.504 10.272 -32.358 1.00 67.79 C
ANISOU 886 CD2 LEU A 137 6063 8990 10703 -1403 -927 680 C
ATOM 887 N SER A 138 -5.326 7.262 -27.942 1.00 39.98 N
ANISOU 887 N SER A 138 2945 5182 7063 -1517 -230 193 N
ATOM 888 CA SER A 138 -5.194 5.929 -27.358 1.00 47.27 C
ANISOU 888 CA SER A 138 4047 6036 7875 -1680 -207 92 C
ATOM 889 C SER A 138 -6.485 5.485 -26.684 1.00 53.76 C
ANISOU 889 C SER A 138 4648 6919 8858 -1750 -107 265 C
ATOM 890 O SER A 138 -6.879 4.316 -26.794 1.00 61.02 O
ANISOU 890 O SER A 138 5653 7834 9698 -1980 -209 256 O
ATOM 891 CB SER A 138 -4.039 5.896 -26.355 1.00 42.07 C
ANISOU 891 CB SER A 138 3594 5226 7165 -1542 10 -124 C
ATOM 892 OG SER A 138 -2.858 6.480 -26.888 1.00 33.97 O
ANISOU 892 OG SER A 138 2728 4162 6016 -1442 -41 -285 O
ATOM 893 N PHE A 139 -7.155 6.398 -25.976 1.00 57.61 N
ANISOU 893 N PHE A 139 4876 7442 9573 -1542 114 419 N
ATOM 894 CA PHE A 139 -8.416 6.025 -25.343 1.00 65.54 C
ANISOU 894 CA PHE A 139 5654 8509 10740 -1581 229 608 C
ATOM 895 C PHE A 139 -9.492 5.726 -26.383 1.00 75.43 C
ANISOU 895 C PHE A 139 6713 9909 12040 -1772 -42 781 C
ATOM 896 O PHE A 139 -10.340 4.848 -26.172 1.00 81.74 O
ANISOU 896 O PHE A 139 7421 10747 12890 -1952 -67 872 O
ATOM 897 CB PHE A 139 -8.876 7.110 -24.374 1.00 73.38 C
ANISOU 897 CB PHE A 139 6461 9475 11944 -1273 559 738 C
ATOM 898 CG PHE A 139 -8.510 6.834 -22.943 1.00 83.76 C
ANISOU 898 CG PHE A 139 7929 10634 13260 -1158 887 633 C
ATOM 899 CD1 PHE A 139 -9.476 6.412 -22.026 1.00106.62 C
ANISOU 899 CD1 PHE A 139 10700 13532 16280 -1142 1093 779 C
ATOM 900 CD2 PHE A 139 -7.197 6.976 -22.519 1.00 67.13 C
ANISOU 900 CD2 PHE A 139 6109 8372 11025 -1068 995 378 C
ATOM 901 CE1 PHE A 139 -9.145 6.148 -20.700 1.00106.59 C
ANISOU 901 CE1 PHE A 139 10884 13362 16254 -1023 1412 675 C
ATOM 902 CE2 PHE A 139 -6.850 6.716 -21.204 1.00 75.59 C
ANISOU 902 CE2 PHE A 139 7363 9287 12071 -963 1302 258 C
ATOM 903 CZ PHE A 139 -7.827 6.299 -20.285 1.00 94.63 C
ANISOU 903 CZ PHE A 139 9681 11685 14590 -933 1516 407 C
ATOM 904 N ILE A 140 -9.508 6.465 -27.494 1.00 77.65 N
ANISOU 904 N ILE A 140 6926 10259 12320 -1732 -241 841 N
ATOM 905 CA ILE A 140 -10.459 6.125 -28.545 1.00 72.48 C
ANISOU 905 CA ILE A 140 6127 9717 11694 -1922 -531 1004 C
ATOM 906 C ILE A 140 -10.130 4.761 -29.120 1.00 69.58 C
ANISOU 906 C ILE A 140 6052 9281 11104 -2219 -757 850 C
ATOM 907 O ILE A 140 -11.024 3.985 -29.478 1.00 78.34 O
ANISOU 907 O ILE A 140 7085 10439 12239 -2439 -927 969 O
ATOM 908 CB ILE A 140 -10.467 7.200 -29.641 1.00 64.69 C
ANISOU 908 CB ILE A 140 5050 8798 10732 -1812 -700 1105 C
ATOM 909 CG1 ILE A 140 -10.835 8.540 -29.033 1.00 68.35 C
ANISOU 909 CG1 ILE A 140 5257 9291 11420 -1496 -443 1267 C
ATOM 910 CG2 ILE A 140 -11.443 6.813 -30.746 1.00 65.70 C
ANISOU 910 CG2 ILE A 140 5051 9037 10875 -2023 -1027 1293 C
ATOM 911 CD1 ILE A 140 -10.486 9.702 -29.907 1.00 72.33 C
ANISOU 911 CD1 ILE A 140 5748 9808 11926 -1345 -532 1307 C
ATOM 912 N ALA A 141 -8.837 4.456 -29.242 1.00 58.84 N
ANISOU 912 N ALA A 141 5044 7793 9520 -2220 -761 599 N
ATOM 913 CA ALA A 141 -8.437 3.123 -29.665 1.00 54.24 C
ANISOU 913 CA ALA A 141 4801 7094 8715 -2446 -917 449 C
ATOM 914 C ALA A 141 -8.800 2.087 -28.611 1.00 68.48 C
ANISOU 914 C ALA A 141 6626 8832 10560 -2570 -761 428 C
ATOM 915 O ALA A 141 -9.247 0.986 -28.951 1.00 87.11 O
ANISOU 915 O ALA A 141 9110 11144 12845 -2800 -915 445 O
ATOM 916 CB ALA A 141 -6.938 3.096 -29.975 1.00 54.00 C
ANISOU 916 CB ALA A 141 5135 6933 8449 -2363 -920 210 C
ATOM 917 N LEU A 142 -8.605 2.422 -27.327 1.00 66.48 N
ANISOU 917 N LEU A 142 6284 8566 10410 -2424 -455 403 N
ATOM 918 CA LEU A 142 -8.845 1.460 -26.253 1.00 64.84 C
ANISOU 918 CA LEU A 142 6134 8278 10224 -2533 -273 379 C
ATOM 919 C LEU A 142 -10.335 1.212 -26.064 1.00 74.40 C
ANISOU 919 C LEU A 142 7026 9603 11639 -2655 -273 615 C
ATOM 920 O LEU A 142 -10.771 0.063 -25.929 1.00 72.92 O
ANISOU 920 O LEU A 142 6926 9351 11430 -2882 -312 615 O
ATOM 921 CB LEU A 142 -8.211 1.942 -24.948 1.00 55.00 C
ANISOU 921 CB LEU A 142 4913 6981 9004 -2325 40 331 C
ATOM 922 CG LEU A 142 -8.160 0.948 -23.791 1.00 51.76 C
ANISOU 922 CG LEU A 142 4661 6449 8558 -2410 234 293 C
ATOM 923 CD1 LEU A 142 -7.221 -0.176 -24.156 1.00 53.39 C
ANISOU 923 CD1 LEU A 142 5299 6485 8502 -2579 108 68 C
ATOM 924 CD2 LEU A 142 -7.719 1.604 -22.496 1.00 49.83 C
ANISOU 924 CD2 LEU A 142 4401 6103 8428 -2094 575 264 C
ATOM 925 N ASP A 143 -11.129 2.285 -26.025 1.00 87.05 N
ANISOU 925 N ASP A 143 8259 11361 13454 -2490 -219 832 N
ATOM 926 CA ASP A 143 -12.577 2.122 -25.922 1.00 86.24 C
ANISOU 926 CA ASP A 143 7815 11385 13568 -2586 -235 1093 C
ATOM 927 C ASP A 143 -13.129 1.308 -27.087 1.00 87.60 C
ANISOU 927 C ASP A 143 8019 11591 13676 -2892 -601 1150 C
ATOM 928 O ASP A 143 -13.992 0.442 -26.897 1.00 99.89 O
ANISOU 928 O ASP A 143 9480 13166 15306 -3115 -640 1260 O
ATOM 929 CB ASP A 143 -13.258 3.482 -25.860 1.00 86.59 C
ANISOU 929 CB ASP A 143 7490 11565 13845 -2314 -135 1331 C
ATOM 930 CG ASP A 143 -14.740 3.388 -26.058 1.00 91.78 C
ANISOU 930 CG ASP A 143 7772 12375 14724 -2416 -223 1635 C
ATOM 931 OD1 ASP A 143 -15.406 2.758 -25.210 1.00 98.29 O
ANISOU 931 OD1 ASP A 143 8483 13205 15658 -2498 -58 1724 O
ATOM 932 OD2 ASP A 143 -15.230 3.947 -27.058 1.00 93.54 O
ANISOU 932 OD2 ASP A 143 7813 12714 15013 -2416 -458 1800 O
ATOM 933 N ARG A 144 -12.639 1.568 -28.303 1.00 78.90 N
ANISOU 933 N ARG A 144 7070 10486 12423 -2911 -873 1090 N
ATOM 934 CA ARG A 144 -13.098 0.809 -29.461 1.00 84.21 C
ANISOU 934 CA ARG A 144 7843 11170 12984 -3195 -1237 1155 C
ATOM 935 C ARG A 144 -12.543 -0.613 -29.460 1.00 84.25 C
ANISOU 935 C ARG A 144 8275 10984 12751 -3416 -1296 958 C
ATOM 936 O ARG A 144 -13.250 -1.557 -29.832 1.00101.28 O
ANISOU 936 O ARG A 144 10475 13135 14870 -3698 -1491 1050 O
ATOM 937 CB ARG A 144 -12.725 1.541 -30.747 1.00 88.07 C
ANISOU 937 CB ARG A 144 8407 11698 13358 -3132 -1487 1166 C
ATOM 938 CG ARG A 144 -13.259 2.978 -30.852 1.00 90.97 C
ANISOU 938 CG ARG A 144 8383 12231 13952 -2899 -1442 1379 C
ATOM 939 CD ARG A 144 -14.772 3.059 -31.086 1.00 96.42 C
ANISOU 939 CD ARG A 144 8666 13100 14870 -3013 -1583 1719 C
ATOM 940 NE ARG A 144 -15.534 2.830 -29.861 1.00 95.58 N
ANISOU 940 NE ARG A 144 8288 13041 14988 -2989 -1320 1836 N
ATOM 941 CZ ARG A 144 -16.774 2.353 -29.826 1.00 95.80 C
ANISOU 941 CZ ARG A 144 8032 13186 15182 -3180 -1417 2086 C
ATOM 942 NH1 ARG A 144 -17.408 2.049 -30.954 1.00 99.69 N
ANISOU 942 NH1 ARG A 144 8475 13764 15637 -3427 -1795 2250 N
ATOM 943 NH2 ARG A 144 -17.381 2.175 -28.659 1.00 94.41 N
ANISOU 943 NH2 ARG A 144 7628 13039 15204 -3132 -1136 2186 N
ATOM 944 N TRP A 145 -11.292 -0.797 -29.029 1.00 69.21 N
ANISOU 944 N TRP A 145 6698 8916 10682 -3290 -1132 705 N
ATOM 945 CA TRP A 145 -10.732 -2.144 -29.021 1.00 63.68 C
ANISOU 945 CA TRP A 145 6434 8018 9744 -3453 -1175 542 C
ATOM 946 C TRP A 145 -11.532 -3.058 -28.100 1.00 67.79 C
ANISOU 946 C TRP A 145 6865 8502 10390 -3632 -1047 616 C
ATOM 947 O TRP A 145 -11.729 -4.241 -28.402 1.00 72.99 O
ANISOU 947 O TRP A 145 7782 9057 10894 -3876 -1196 606 O
ATOM 948 CB TRP A 145 -9.261 -2.093 -28.619 1.00 64.17 C
ANISOU 948 CB TRP A 145 6820 7926 9637 -3245 -1005 298 C
ATOM 949 CG TRP A 145 -8.592 -3.427 -28.672 1.00 61.99 C
ANISOU 949 CG TRP A 145 7036 7447 9070 -3352 -1047 152 C
ATOM 950 CD1 TRP A 145 -8.193 -4.092 -29.795 1.00 62.61 C
ANISOU 950 CD1 TRP A 145 7510 7445 8833 -3457 -1278 98 C
ATOM 951 CD2 TRP A 145 -8.211 -4.252 -27.563 1.00 55.46 C
ANISOU 951 CD2 TRP A 145 6408 6468 8197 -3343 -834 56 C
ATOM 952 NE1 TRP A 145 -7.604 -5.285 -29.457 1.00 53.54 N
ANISOU 952 NE1 TRP A 145 6794 6113 7435 -3502 -1207 -26 N
ATOM 953 CE2 TRP A 145 -7.600 -5.407 -28.093 1.00 55.59 C
ANISOU 953 CE2 TRP A 145 6942 6330 7851 -3433 -948 -55 C
ATOM 954 CE3 TRP A 145 -8.333 -4.131 -26.176 1.00 55.96 C
ANISOU 954 CE3 TRP A 145 6292 6504 8465 -3261 -544 69 C
ATOM 955 CZ2 TRP A 145 -7.109 -6.433 -27.282 1.00 55.86 C
ANISOU 955 CZ2 TRP A 145 7314 6198 7711 -3431 -786 -161 C
ATOM 956 CZ3 TRP A 145 -7.848 -5.149 -25.374 1.00 52.75 C
ANISOU 956 CZ3 TRP A 145 6223 5925 7894 -3277 -408 -26 C
ATOM 957 CH2 TRP A 145 -7.243 -6.284 -25.930 1.00 52.19 C
ANISOU 957 CH2 TRP A 145 6664 5718 7449 -3356 -530 -148 C
ATOM 958 N TYR A 146 -11.988 -2.531 -26.964 1.00 68.41 N
ANISOU 958 N TYR A 146 6611 8659 10724 -3513 -754 696 N
ATOM 959 CA TYR A 146 -12.866 -3.297 -26.093 1.00 79.49 C
ANISOU 959 CA TYR A 146 7881 10048 12273 -3680 -606 799 C
ATOM 960 C TYR A 146 -14.283 -3.357 -26.654 1.00 89.36 C
ANISOU 960 C TYR A 146 8788 11478 13685 -3892 -821 1069 C
ATOM 961 O TYR A 146 -14.929 -4.409 -26.594 1.00 95.17 O
ANISOU 961 O TYR A 146 9565 12169 14427 -4168 -899 1136 O
ATOM 962 CB TYR A 146 -12.864 -2.693 -24.685 1.00 84.75 C
ANISOU 962 CB TYR A 146 8350 10743 13106 -3468 -195 815 C
ATOM 963 CG TYR A 146 -11.672 -3.114 -23.858 1.00 72.99 C
ANISOU 963 CG TYR A 146 7230 9034 11468 -3370 32 583 C
ATOM 964 CD1 TYR A 146 -11.596 -4.394 -23.336 1.00 70.53 C
ANISOU 964 CD1 TYR A 146 7179 8516 11102 -3523 100 524 C
ATOM 965 CD2 TYR A 146 -10.623 -2.235 -23.599 1.00 60.57 C
ANISOU 965 CD2 TYR A 146 5750 7453 9813 -3117 157 456 C
ATOM 966 CE1 TYR A 146 -10.509 -4.801 -22.585 1.00 59.89 C
ANISOU 966 CE1 TYR A 146 6167 6945 9645 -3387 250 387 C
ATOM 967 CE2 TYR A 146 -9.531 -2.632 -22.843 1.00 55.35 C
ANISOU 967 CE2 TYR A 146 5410 6576 9044 -3025 335 276 C
ATOM 968 CZ TYR A 146 -9.478 -3.916 -22.338 1.00 57.44 C
ANISOU 968 CZ TYR A 146 5912 6621 9293 -3121 325 309 C
ATOM 969 OH TYR A 146 -8.402 -4.332 -21.584 1.00 60.17 O
ANISOU 969 OH TYR A 146 6681 6852 9326 -3015 426 176 O
ATOM 970 N ALA A 147 -14.771 -2.254 -27.229 1.00 91.56 N
ANISOU 970 N ALA A 147 8737 11956 14096 -3772 -935 1243 N
ATOM 971 CA ALA A 147 -16.145 -2.240 -27.725 1.00 93.82 C
ANISOU 971 CA ALA A 147 8655 12427 14564 -3954 -1145 1543 C
ATOM 972 C ALA A 147 -16.331 -3.178 -28.910 1.00 94.73 C
ANISOU 972 C ALA A 147 9019 12497 14477 -4294 -1554 1556 C
ATOM 973 O ALA A 147 -17.415 -3.751 -29.075 1.00108.20 O
ANISOU 973 O ALA A 147 10537 14289 16286 -4568 -1716 1763 O
ATOM 974 CB ALA A 147 -16.555 -0.820 -28.107 1.00 92.66 C
ANISOU 974 CB ALA A 147 8135 12478 14593 -3713 -1177 1743 C
ATOM 975 N ILE A 148 -15.302 -3.344 -29.737 1.00 76.48 N
ANISOU 975 N ILE A 148 7140 10053 11865 -4284 -1721 1356 N
ATOM 976 CA ILE A 148 -15.394 -4.166 -30.936 1.00 81.97 C
ANISOU 976 CA ILE A 148 8151 10690 12304 -4581 -2101 1371 C
ATOM 977 C ILE A 148 -14.687 -5.507 -30.766 1.00 90.96 C
ANISOU 977 C ILE A 148 9825 11581 13155 -4731 -2075 1156 C
ATOM 978 O ILE A 148 -15.230 -6.548 -31.144 1.00105.33 O
ANISOU 978 O ILE A 148 11820 13348 14853 -5059 -2282 1227 O
ATOM 979 CB ILE A 148 -14.861 -3.396 -32.164 1.00 82.72 C
ANISOU 979 CB ILE A 148 8378 10817 12236 -4472 -2326 1353 C
ATOM 980 CG1 ILE A 148 -15.836 -2.283 -32.564 1.00 96.75 C
ANISOU 980 CG1 ILE A 148 9649 12839 14274 -4412 -2447 1640 C
ATOM 981 CG2 ILE A 148 -14.626 -4.322 -33.345 1.00 78.56 C
ANISOU 981 CG2 ILE A 148 8338 10162 11351 -4741 -2656 1309 C
ATOM 982 CD1 ILE A 148 -15.237 -1.251 -33.508 1.00104.50 C
ANISOU 982 CD1 ILE A 148 10697 13850 15157 -4218 -2566 1615 C
ATOM 983 N CYS A 149 -13.485 -5.515 -30.188 1.00 88.36 N
ANISOU 983 N CYS A 149 9773 11096 12705 -4497 -1827 910 N
ATOM 984 CA CYS A 149 -12.748 -6.768 -30.068 1.00 86.45 C
ANISOU 984 CA CYS A 149 10073 10616 12158 -4595 -1799 725 C
ATOM 985 C CYS A 149 -13.080 -7.562 -28.813 1.00 86.47 C
ANISOU 985 C CYS A 149 10040 10528 12285 -4678 -1556 717 C
ATOM 986 O CYS A 149 -13.035 -8.798 -28.850 1.00 81.18 O
ANISOU 986 O CYS A 149 9752 9699 11392 -4890 -1619 666 O
ATOM 987 CB CYS A 149 -11.243 -6.502 -30.092 1.00 77.59 C
ANISOU 987 CB CYS A 149 9303 9365 10812 -4306 -1667 487 C
ATOM 988 SG CYS A 149 -10.687 -5.732 -31.625 1.00 77.05 S
ANISOU 988 SG CYS A 149 9384 9350 10541 -4216 -1924 475 S
ATOM 989 N HIS A 150 -13.412 -6.903 -27.703 1.00 87.74 N
ANISOU 989 N HIS A 150 9789 10775 12774 -4519 -1263 773 N
ATOM 990 CA HIS A 150 -13.689 -7.602 -26.446 1.00 84.83 C
ANISOU 990 CA HIS A 150 9398 10302 12532 -4576 -986 773 C
ATOM 991 C HIS A 150 -14.931 -7.037 -25.758 1.00 90.31 C
ANISOU 991 C HIS A 150 9511 11190 13615 -4599 -820 1000 C
ATOM 992 O HIS A 150 -14.852 -6.387 -24.707 1.00 87.35 O
ANISOU 992 O HIS A 150 8921 10843 13423 -4375 -474 997 O
ATOM 993 CB HIS A 150 -12.444 -7.556 -25.561 1.00 76.12 C
ANISOU 993 CB HIS A 150 8563 9028 11330 -4300 -699 565 C
ATOM 994 CG HIS A 150 -11.245 -8.175 -26.214 1.00 74.75 C
ANISOU 994 CG HIS A 150 8973 8690 10739 -4261 -841 364 C
ATOM 995 ND1 HIS A 150 -11.136 -9.532 -26.435 1.00 70.92 N
ANISOU 995 ND1 HIS A 150 8948 8041 9957 -4467 -941 306 N
ATOM 996 CD2 HIS A 150 -10.130 -7.618 -26.742 1.00 72.67 C
ANISOU 996 CD2 HIS A 150 8918 8413 10282 -4038 -884 220 C
ATOM 997 CE1 HIS A 150 -9.994 -9.785 -27.049 1.00 68.80 C
ANISOU 997 CE1 HIS A 150 9156 7667 9318 -4346 -1009 136 C
ATOM 998 NE2 HIS A 150 -9.365 -8.641 -27.247 1.00 73.83 N
ANISOU 998 NE2 HIS A 150 9636 8394 10022 -4089 -978 83 N
ATOM 999 N PRO A 151 -16.105 -7.292 -26.329 1.00 93.15 N
ANISOU 999 N PRO A 151 9629 11690 14074 -4874 -1060 1217 N
ATOM 1000 CA PRO A 151 -17.336 -6.611 -25.899 1.00 99.65 C
ANISOU 1000 CA PRO A 151 9861 12753 15249 -4867 -955 1487 C
ATOM 1001 C PRO A 151 -17.786 -6.978 -24.488 1.00103.58 C
ANISOU 1001 C PRO A 151 10206 13206 15943 -4868 -562 1531 C
ATOM 1002 O PRO A 151 -17.453 -8.040 -23.950 1.00 93.71 O
ANISOU 1002 O PRO A 151 9283 11735 14587 -4994 -442 1402 O
ATOM 1003 CB PRO A 151 -18.371 -7.077 -26.932 1.00104.33 C
ANISOU 1003 CB PRO A 151 10326 13468 15847 -5221 -1364 1707 C
ATOM 1004 CG PRO A 151 -17.573 -7.430 -28.124 1.00 99.30 C
ANISOU 1004 CG PRO A 151 10165 12713 14852 -5305 -1693 1552 C
ATOM 1005 CD PRO A 151 -16.305 -8.042 -27.579 1.00 91.43 C
ANISOU 1005 CD PRO A 151 9675 11448 13618 -5178 -1481 1252 C
ATOM 1006 N LEU A 152 -18.548 -6.046 -23.889 1.00114.71 N
ANISOU 1006 N LEU A 152 11130 14827 17628 -4696 -351 1738 N
ATOM 1007 CA LEU A 152 -19.121 -6.127 -22.545 1.00119.15 C
ANISOU 1007 CA LEU A 152 11481 15409 18381 -4645 52 1842 C
ATOM 1008 C LEU A 152 -18.109 -6.582 -21.505 1.00115.32 C
ANISOU 1008 C LEU A 152 11406 14677 17735 -4539 397 1585 C
ATOM 1009 O LEU A 152 -18.459 -6.957 -20.383 1.00118.86 O
ANISOU 1009 O LEU A 152 11824 15083 18255 -4560 728 1633 O
ATOM 1010 CB LEU A 152 -20.350 -7.029 -22.503 1.00122.28 C
ANISOU 1010 CB LEU A 152 11661 15862 18939 -5000 -31 2059 C
ATOM 1011 CG LEU A 152 -21.252 -6.473 -21.406 1.00121.31 C
ANISOU 1011 CG LEU A 152 11094 15906 19094 -4835 330 2304 C
ATOM 1012 CD1 LEU A 152 -21.272 -4.961 -21.522 1.00121.28 C
ANISOU 1012 CD1 LEU A 152 10782 16091 19207 -4440 373 2437 C
ATOM 1013 CD2 LEU A 152 -22.673 -7.020 -21.478 1.00122.67 C
ANISOU 1013 CD2 LEU A 152 10877 16226 19506 -5141 224 2613 C
ATOM 1014 N LEU A 153 -16.831 -6.539 -21.874 1.00110.82 N
ANISOU 1014 N LEU A 153 11228 13944 16936 -4416 321 1330 N
ATOM 1015 CA LEU A 153 -15.767 -6.602 -20.883 1.00107.85 C
ANISOU 1015 CA LEU A 153 11183 13373 16424 -4224 651 1122 C
ATOM 1016 C LEU A 153 -15.853 -5.363 -20.013 1.00107.78 C
ANISOU 1016 C LEU A 153 10918 13563 16470 -3923 933 1233 C
ATOM 1017 O LEU A 153 -16.085 -5.448 -18.807 1.00109.47 O
ANISOU 1017 O LEU A 153 11119 13783 16692 -3853 1243 1324 O
ATOM 1018 CB LEU A 153 -14.401 -6.710 -21.579 1.00104.58 C
ANISOU 1018 CB LEU A 153 11180 12769 15787 -4117 452 887 C
ATOM 1019 CG LEU A 153 -14.091 -8.036 -22.236 1.00 96.41 C
ANISOU 1019 CG LEU A 153 10551 11533 14549 -4339 160 814 C
ATOM 1020 CD1 LEU A 153 -12.597 -8.136 -22.548 1.00 89.00 C
ANISOU 1020 CD1 LEU A 153 10088 10437 13291 -4159 53 598 C
ATOM 1021 CD2 LEU A 153 -14.565 -9.196 -21.381 1.00 95.41 C
ANISOU 1021 CD2 LEU A 153 10532 11244 14476 -4520 329 877 C
ATOM 1022 N PHE A 154 -15.644 -4.201 -20.616 1.00 99.36 N
ANISOU 1022 N PHE A 154 9672 12639 15440 -3695 800 1269 N
ATOM 1023 CA PHE A 154 -15.891 -2.909 -20.001 1.00 98.29 C
ANISOU 1023 CA PHE A 154 9235 12653 15457 -3328 1012 1442 C
ATOM 1024 C PHE A 154 -17.059 -2.274 -20.720 1.00107.73 C
ANISOU 1024 C PHE A 154 9956 14064 16911 -3319 841 1707 C
ATOM 1025 O PHE A 154 -17.074 -2.241 -21.950 1.00114.72 O
ANISOU 1025 O PHE A 154 10816 15005 17767 -3454 490 1692 O
ATOM 1026 CB PHE A 154 -14.653 -2.022 -20.101 1.00 92.85 C
ANISOU 1026 CB PHE A 154 8746 11909 14625 -3041 1020 1276 C
ATOM 1027 CG PHE A 154 -13.495 -2.600 -19.379 1.00 92.76 C
ANISOU 1027 CG PHE A 154 9177 11694 14375 -3019 1155 1075 C
ATOM 1028 CD1 PHE A 154 -13.274 -2.302 -18.041 1.00 93.27 C
ANISOU 1028 CD1 PHE A 154 9298 11647 14494 -2711 1518 1106 C
ATOM 1029 CD2 PHE A 154 -12.621 -3.435 -20.022 1.00 88.73 C
ANISOU 1029 CD2 PHE A 154 9053 11049 13610 -3252 947 848 C
ATOM 1030 CE1 PHE A 154 -12.179 -2.846 -17.367 1.00 82.03 C
ANISOU 1030 CE1 PHE A 154 8295 9981 12892 -2625 1651 906 C
ATOM 1031 CE2 PHE A 154 -11.539 -3.977 -19.366 1.00 80.08 C
ANISOU 1031 CE2 PHE A 154 8356 9751 12321 -3181 1001 760 C
ATOM 1032 CZ PHE A 154 -11.311 -3.688 -18.039 1.00 73.47 C
ANISOU 1032 CZ PHE A 154 7557 8781 11578 -2842 1389 734 C
ATOM 1033 N LYS A 155 -18.035 -1.782 -19.969 1.00109.53 N
ANISOU 1033 N LYS A 155 9827 14401 17387 -3144 1083 1971 N
ATOM 1034 CA LYS A 155 -19.084 -1.012 -20.597 1.00113.42 C
ANISOU 1034 CA LYS A 155 9862 15098 18135 -3068 946 2262 C
ATOM 1035 C LYS A 155 -18.571 0.413 -20.647 1.00108.52 C
ANISOU 1035 C LYS A 155 9210 14487 17536 -2653 1038 2261 C
ATOM 1036 O LYS A 155 -18.223 0.987 -19.609 1.00105.07 O
ANISOU 1036 O LYS A 155 8861 13947 17112 -2326 1392 2238 O
ATOM 1037 CB LYS A 155 -20.389 -1.131 -19.818 1.00120.90 C
ANISOU 1037 CB LYS A 155 10435 16144 19358 -3053 1174 2572 C
ATOM 1038 CG LYS A 155 -20.854 -2.554 -19.656 1.00129.19 C
ANISOU 1038 CG LYS A 155 11543 17160 20385 -3474 1123 2562 C
ATOM 1039 CD LYS A 155 -22.162 -2.727 -18.922 1.00137.89 C
ANISOU 1039 CD LYS A 155 12255 18370 21768 -3489 1341 2883 C
ATOM 1040 CE LYS A 155 -22.389 -4.209 -18.647 1.00138.32 C
ANISOU 1040 CE LYS A 155 12474 18334 21747 -3919 1332 2807 C
ATOM 1041 NZ LYS A 155 -23.737 -4.479 -18.091 1.00142.13 N
ANISOU 1041 NZ LYS A 155 12543 18944 22518 -4005 1493 3139 N
ATOM 1042 N SER A 156 -18.545 0.989 -21.839 1.00108.48 N
ANISOU 1042 N SER A 156 9106 14580 17531 -2659 728 2294 N
ATOM 1043 CA SER A 156 -18.052 2.347 -22.000 1.00105.24 C
ANISOU 1043 CA SER A 156 8685 14168 17134 -2294 798 2290 C
ATOM 1044 C SER A 156 -19.239 3.188 -22.418 1.00106.58 C
ANISOU 1044 C SER A 156 8401 14515 17579 -2159 750 2651 C
ATOM 1045 O SER A 156 -19.700 3.119 -23.560 1.00111.89 O
ANISOU 1045 O SER A 156 8910 15323 18282 -2355 393 2769 O
ATOM 1046 CB SER A 156 -16.907 2.417 -23.006 1.00103.66 C
ANISOU 1046 CB SER A 156 8786 13912 16686 -2373 515 2028 C
ATOM 1047 OG SER A 156 -17.366 2.655 -24.329 1.00106.24 O
ANISOU 1047 OG SER A 156 8941 14376 17051 -2497 149 2157 O
ATOM 1048 N THR A 157 -19.723 3.974 -21.480 1.00104.39 N
ANISOU 1048 N THR A 157 7952 14219 17492 -1813 1119 2839 N
ATOM 1049 CA THR A 157 -20.786 4.931 -21.700 1.00117.05 C
ANISOU 1049 CA THR A 157 9151 15958 19366 -1596 1165 3206 C
ATOM 1050 C THR A 157 -20.149 6.302 -21.828 1.00125.67 C
ANISOU 1050 C THR A 157 10362 16966 20421 -1224 1280 3157 C
ATOM 1051 O THR A 157 -18.966 6.485 -21.542 1.00126.03 O
ANISOU 1051 O THR A 157 10776 16847 20261 -1125 1372 2857 O
ATOM 1052 CB THR A 157 -21.811 4.875 -20.559 1.00124.76 C
ANISOU 1052 CB THR A 157 9881 16939 20582 -1443 1534 3476 C
ATOM 1053 OG1 THR A 157 -21.131 4.704 -19.309 1.00125.29 O
ANISOU 1053 OG1 THR A 157 10278 16792 20533 -1280 1902 3267 O
ATOM 1054 CG2 THR A 157 -22.753 3.698 -20.769 1.00127.49 C
ANISOU 1054 CG2 THR A 157 9968 17436 21035 -1841 1340 3634 C
ATOM 1055 N ALA A 158 -20.934 7.267 -22.298 1.00131.95 N
ANISOU 1055 N ALA A 158 10847 17874 21414 -1032 1265 3466 N
ATOM 1056 CA ALA A 158 -20.404 8.621 -22.368 1.00118.74 C
ANISOU 1056 CA ALA A 158 9300 16102 19715 -672 1414 3441 C
ATOM 1057 C ALA A 158 -19.963 9.102 -20.992 1.00118.35 C
ANISOU 1057 C ALA A 158 9513 15817 19639 -335 1897 3340 C
ATOM 1058 O ALA A 158 -19.010 9.884 -20.882 1.00119.55 O
ANISOU 1058 O ALA A 158 9963 15810 19649 -129 2010 3143 O
ATOM 1059 CB ALA A 158 -21.438 9.570 -22.961 1.00111.90 C
ANISOU 1059 CB ALA A 158 8055 15381 19082 -495 1381 3836 C
ATOM 1060 N ARG A 159 -20.615 8.620 -19.930 1.00122.23 N
ANISOU 1060 N ARG A 159 9924 16268 20250 -288 2182 3467 N
ATOM 1061 CA ARG A 159 -20.219 8.999 -18.577 1.00127.59 C
ANISOU 1061 CA ARG A 159 10908 16692 20879 23 2643 3370 C
ATOM 1062 C ARG A 159 -18.812 8.524 -18.236 1.00119.46 C
ANISOU 1062 C ARG A 159 10334 15495 19560 -75 2627 2944 C
ATOM 1063 O ARG A 159 -18.042 9.261 -17.610 1.00113.34 O
ANISOU 1063 O ARG A 159 9899 14501 18666 189 2877 2785 O
ATOM 1064 CB ARG A 159 -21.233 8.443 -17.577 1.00143.25 C
ANISOU 1064 CB ARG A 159 12713 18672 23043 60 2927 3600 C
ATOM 1065 CG ARG A 159 -20.750 8.293 -16.135 1.00147.99 C
ANISOU 1065 CG ARG A 159 13697 19001 23533 249 3341 3433 C
ATOM 1066 CD ARG A 159 -20.765 9.581 -15.317 1.00150.21 C
ANISOU 1066 CD ARG A 159 14192 19041 23838 720 3772 3530 C
ATOM 1067 NE ARG A 159 -20.398 9.314 -13.927 1.00150.23 N
ANISOU 1067 NE ARG A 159 14583 18775 23725 866 4144 3383 N
ATOM 1068 CZ ARG A 159 -19.170 9.408 -13.430 1.00147.36 C
ANISOU 1068 CZ ARG A 159 14712 18185 23094 916 4219 3035 C
ATOM 1069 NH1 ARG A 159 -18.155 9.760 -14.207 1.00141.32 N
ANISOU 1069 NH1 ARG A 159 14097 17436 22161 833 3959 2793 N
ATOM 1070 NH2 ARG A 159 -18.962 9.129 -12.153 1.00149.24 N
ANISOU 1070 NH2 ARG A 159 15296 18176 23230 1042 4550 2938 N
ATOM 1071 N ARG A 160 -18.456 7.299 -18.632 1.00117.72 N
ANISOU 1071 N ARG A 160 10151 15363 19216 -459 2341 2763 N
ATOM 1072 CA ARG A 160 -17.077 6.856 -18.463 1.00112.81 C
ANISOU 1072 CA ARG A 160 9943 14600 18320 -557 2294 2385 C
ATOM 1073 C ARG A 160 -16.164 7.462 -19.523 1.00105.92 C
ANISOU 1073 C ARG A 160 9184 13750 17311 -574 2023 2217 C
ATOM 1074 O ARG A 160 -14.958 7.614 -19.293 1.00 94.88 O
ANISOU 1074 O ARG A 160 8130 12201 15720 -513 2071 1942 O
ATOM 1075 CB ARG A 160 -17.022 5.326 -18.477 1.00113.78 C
ANISOU 1075 CB ARG A 160 10107 14778 18345 -950 2120 2270 C
ATOM 1076 CG ARG A 160 -17.797 4.722 -17.314 1.00121.32 C
ANISOU 1076 CG ARG A 160 10999 15681 19416 -923 2429 2409 C
ATOM 1077 CD ARG A 160 -18.021 3.232 -17.428 1.00126.71 C
ANISOU 1077 CD ARG A 160 11663 16440 20041 -1345 2250 2365 C
ATOM 1078 NE ARG A 160 -18.683 2.723 -16.230 1.00134.55 N
ANISOU 1078 NE ARG A 160 12626 17361 21137 -1289 2587 2491 N
ATOM 1079 CZ ARG A 160 -19.968 2.913 -15.945 1.00146.52 C
ANISOU 1079 CZ ARG A 160 13777 18974 22918 -1205 2740 2820 C
ATOM 1080 NH1 ARG A 160 -20.730 3.613 -16.771 1.00149.99 N
ANISOU 1080 NH1 ARG A 160 13849 19591 23551 -1159 2578 3067 N
ATOM 1081 NH2 ARG A 160 -20.489 2.415 -14.831 1.00151.24 N
ANISOU 1081 NH2 ARG A 160 14384 19488 23594 -1152 3062 2919 N
ATOM 1082 N ALA A 161 -16.712 7.794 -20.692 1.00109.87 N
ANISOU 1082 N ALA A 161 9405 14432 17907 -661 1735 2385 N
ATOM 1083 CA ALA A 161 -15.916 8.466 -21.712 1.00107.50 C
ANISOU 1083 CA ALA A 161 9210 14145 17490 -648 1502 2255 C
ATOM 1084 C ALA A 161 -15.479 9.853 -21.255 1.00 97.87 C
ANISOU 1084 C ALA A 161 8142 12766 16278 -258 1793 2242 C
ATOM 1085 O ALA A 161 -14.352 10.279 -21.532 1.00 92.56 O
ANISOU 1085 O ALA A 161 7727 12001 15441 -219 1738 2009 O
ATOM 1086 CB ALA A 161 -16.712 8.558 -23.015 1.00112.30 C
ANISOU 1086 CB ALA A 161 9497 14966 18204 -803 1152 2473 C
ATOM 1087 N LEU A 162 -16.356 10.570 -20.547 1.00 97.59 N
ANISOU 1087 N LEU A 162 7974 12680 16427 29 2115 2496 N
ATOM 1088 CA LEU A 162 -15.999 11.890 -20.034 1.00 88.03 C
ANISOU 1088 CA LEU A 162 6976 11273 15199 396 2427 2489 C
ATOM 1089 C LEU A 162 -15.068 11.820 -18.832 1.00 79.84 C
ANISOU 1089 C LEU A 162 6371 9979 13986 506 2716 2222 C
ATOM 1090 O LEU A 162 -14.207 12.687 -18.671 1.00 69.73 O
ANISOU 1090 O LEU A 162 5391 8528 12573 673 2833 2059 O
ATOM 1091 CB LEU A 162 -17.258 12.683 -19.698 1.00 91.80 C
ANISOU 1091 CB LEU A 162 7213 11757 15910 674 2691 2869 C
ATOM 1092 CG LEU A 162 -18.031 12.985 -20.976 1.00 98.82 C
ANISOU 1092 CG LEU A 162 7707 12887 16953 599 2395 3131 C
ATOM 1093 CD1 LEU A 162 -19.505 13.177 -20.682 1.00108.16 C
ANISOU 1093 CD1 LEU A 162 8526 14164 18408 748 2576 3557 C
ATOM 1094 CD2 LEU A 162 -17.437 14.215 -21.657 1.00 99.72 C
ANISOU 1094 CD2 LEU A 162 7954 12941 16994 773 2360 3084 C
ATOM 1095 N GLY A 163 -15.234 10.822 -17.965 1.00 88.37 N
ANISOU 1095 N GLY A 163 7507 11017 15054 412 2839 2180 N
ATOM 1096 CA GLY A 163 -14.285 10.652 -16.878 1.00 90.03 C
ANISOU 1096 CA GLY A 163 8154 10984 15068 487 3072 1911 C
ATOM 1097 C GLY A 163 -12.871 10.473 -17.395 1.00 89.11 C
ANISOU 1097 C GLY A 163 8280 10846 14733 329 2841 1579 C
ATOM 1098 O GLY A 163 -11.916 11.035 -16.851 1.00 80.74 O
ANISOU 1098 O GLY A 163 7588 9583 13506 468 2998 1370 O
ATOM 1099 N SER A 164 -12.719 9.654 -18.440 1.00 88.49 N
ANISOU 1099 N SER A 164 8020 10965 14635 21 2461 1529 N
ATOM 1100 CA SER A 164 -11.408 9.458 -19.049 1.00 70.65 C
ANISOU 1100 CA SER A 164 5968 8695 12183 -131 2230 1244 C
ATOM 1101 C SER A 164 -10.844 10.773 -19.580 1.00 86.85 C
ANISOU 1101 C SER A 164 8098 10697 14206 46 2217 1200 C
ATOM 1102 O SER A 164 -9.634 11.027 -19.492 1.00 94.84 O
ANISOU 1102 O SER A 164 9396 11588 15052 64 2226 947 O
ATOM 1103 CB SER A 164 -11.518 8.425 -20.173 1.00 56.35 C
ANISOU 1103 CB SER A 164 3975 7089 10348 -488 1821 1246 C
ATOM 1104 OG SER A 164 -11.986 7.188 -19.679 1.00 62.07 O
ANISOU 1104 OG SER A 164 4667 7839 11078 -681 1838 1274 O
ATOM 1105 N ILE A 165 -11.705 11.609 -20.166 1.00 88.93 N
ANISOU 1105 N ILE A 165 8105 11055 14628 168 2191 1451 N
ATOM 1106 CA ILE A 165 -11.226 12.835 -20.793 1.00 79.13 C
ANISOU 1106 CA ILE A 165 6928 9775 13364 316 2163 1429 C
ATOM 1107 C ILE A 165 -10.632 13.776 -19.756 1.00 78.61 C
ANISOU 1107 C ILE A 165 7229 9443 13198 581 2522 1308 C
ATOM 1108 O ILE A 165 -9.690 14.521 -20.054 1.00 81.88 O
ANISOU 1108 O ILE A 165 7847 9767 13497 632 2501 1144 O
ATOM 1109 CB ILE A 165 -12.366 13.520 -21.572 1.00 66.32 C
ANISOU 1109 CB ILE A 165 4964 8297 11936 410 2089 1754 C
ATOM 1110 CG1 ILE A 165 -12.850 12.620 -22.712 1.00 60.77 C
ANISOU 1110 CG1 ILE A 165 3963 7847 11281 105 1678 1843 C
ATOM 1111 CG2 ILE A 165 -11.900 14.869 -22.113 1.00 54.11 C
ANISOU 1111 CG2 ILE A 165 3518 6677 10363 599 2119 1746 C
ATOM 1112 CD1 ILE A 165 -14.169 13.059 -23.285 1.00 64.51 C
ANISOU 1112 CD1 ILE A 165 4069 8476 11966 173 1618 2199 C
ATOM 1113 N LEU A 166 -11.166 13.769 -18.529 1.00 76.68 N
ANISOU 1113 N LEU A 166 7106 9054 12976 741 2853 1387 N
ATOM 1114 CA LEU A 166 -10.619 14.646 -17.502 1.00 70.35 C
ANISOU 1114 CA LEU A 166 6737 7971 12021 961 3176 1268 C
ATOM 1115 C LEU A 166 -9.254 14.179 -17.014 1.00 67.45 C
ANISOU 1115 C LEU A 166 6738 7482 11406 837 3142 911 C
ATOM 1116 O LEU A 166 -8.407 15.015 -16.682 1.00 74.49 O
ANISOU 1116 O LEU A 166 7988 8197 12118 924 3238 744 O
ATOM 1117 CB LEU A 166 -11.593 14.780 -16.333 1.00 89.46 C
ANISOU 1117 CB LEU A 166 9228 10252 14512 1165 3536 1468 C
ATOM 1118 CG LEU A 166 -12.653 15.877 -16.456 1.00 95.40 C
ANISOU 1118 CG LEU A 166 9831 10987 15431 1421 3729 1796 C
ATOM 1119 CD1 LEU A 166 -13.752 15.702 -15.415 1.00102.97 C
ANISOU 1119 CD1 LEU A 166 10761 11856 16505 1584 4054 2038 C
ATOM 1120 CD2 LEU A 166 -12.009 17.253 -16.322 1.00 87.86 C
ANISOU 1120 CD2 LEU A 166 9255 9816 14311 1602 3890 1709 C
ATOM 1121 N GLY A 167 -9.021 12.865 -16.958 1.00 68.16 N
ANISOU 1121 N GLY A 167 6766 7663 11468 623 3001 799 N
ATOM 1122 CA GLY A 167 -7.723 12.367 -16.523 1.00 68.43 C
ANISOU 1122 CA GLY A 167 7136 7596 11266 511 2964 475 C
ATOM 1123 C GLY A 167 -6.608 12.710 -17.492 1.00 75.19 C
ANISOU 1123 C GLY A 167 8024 8511 12034 407 2722 284 C
ATOM 1124 O GLY A 167 -5.461 12.933 -17.088 1.00 81.92 O
ANISOU 1124 O GLY A 167 9220 9238 12669 402 2740 31 O
ATOM 1125 N ILE A 168 -6.920 12.723 -18.789 1.00 77.49 N
ANISOU 1125 N ILE A 168 7971 8999 12472 306 2464 406 N
ATOM 1126 CA ILE A 168 -5.901 13.026 -19.790 1.00 69.30 C
ANISOU 1126 CA ILE A 168 6948 8017 11365 202 2229 245 C
ATOM 1127 C ILE A 168 -5.259 14.371 -19.486 1.00 64.57 C
ANISOU 1127 C ILE A 168 6635 7239 10660 388 2400 144 C
ATOM 1128 O ILE A 168 -4.030 14.522 -19.519 1.00 65.75 O
ANISOU 1128 O ILE A 168 7033 7327 10624 321 2316 -108 O
ATOM 1129 CB ILE A 168 -6.509 13.000 -21.203 1.00 57.90 C
ANISOU 1129 CB ILE A 168 5140 6789 10071 92 1926 437 C
ATOM 1130 CG1 ILE A 168 -7.032 11.598 -21.518 1.00 45.38 C
ANISOU 1130 CG1 ILE A 168 3367 5361 8516 -151 1708 501 C
ATOM 1131 CG2 ILE A 168 -5.489 13.474 -22.213 1.00 62.37 C
ANISOU 1131 CG2 ILE A 168 5753 7382 10563 20 1716 291 C
ATOM 1132 CD1 ILE A 168 -7.483 11.436 -22.942 1.00 43.04 C
ANISOU 1132 CD1 ILE A 168 2813 5266 8276 -314 1350 642 C
ATOM 1133 N TRP A 169 -6.087 15.374 -19.191 1.00 62.72 N
ANISOU 1133 N TRP A 169 6409 6916 10506 609 2610 347 N
ATOM 1134 CA TRP A 169 -5.535 16.679 -18.852 1.00 58.13 C
ANISOU 1134 CA TRP A 169 6171 6129 9785 765 2774 261 C
ATOM 1135 C TRP A 169 -4.759 16.633 -17.541 1.00 71.59 C
ANISOU 1135 C TRP A 169 8355 7628 11218 759 2916 38 C
ATOM 1136 O TRP A 169 -3.720 17.291 -17.413 1.00 85.03 O
ANISOU 1136 O TRP A 169 10384 9210 12712 726 2875 -158 O
ATOM 1137 CB TRP A 169 -6.650 17.724 -18.799 1.00 46.36 C
ANISOU 1137 CB TRP A 169 4613 4578 8422 1003 2984 549 C
ATOM 1138 CG TRP A 169 -7.114 18.103 -20.160 1.00 51.41 C
ANISOU 1138 CG TRP A 169 4885 5398 9253 1013 2799 733 C
ATOM 1139 CD1 TRP A 169 -8.132 17.540 -20.853 1.00 52.74 C
ANISOU 1139 CD1 TRP A 169 4619 5792 9627 961 2637 972 C
ATOM 1140 CD2 TRP A 169 -6.573 19.128 -21.000 1.00 54.81 C
ANISOU 1140 CD2 TRP A 169 5374 5795 9658 1062 2731 697 C
ATOM 1141 NE1 TRP A 169 -8.277 18.153 -22.070 1.00 63.89 N
ANISOU 1141 NE1 TRP A 169 5822 7319 11133 977 2458 1093 N
ATOM 1142 CE2 TRP A 169 -7.329 19.132 -22.186 1.00 54.63 C
ANISOU 1142 CE2 TRP A 169 4937 5986 9833 1053 2529 931 C
ATOM 1143 CE3 TRP A 169 -5.526 20.048 -20.861 1.00 53.03 C
ANISOU 1143 CE3 TRP A 169 5533 5371 9245 1094 2805 491 C
ATOM 1144 CZ2 TRP A 169 -7.078 20.016 -23.229 1.00 48.47 C
ANISOU 1144 CZ2 TRP A 169 4109 5226 9083 1105 2424 973 C
ATOM 1145 CZ3 TRP A 169 -5.272 20.937 -21.909 1.00 57.75 C
ANISOU 1145 CZ3 TRP A 169 6079 5978 9885 1141 2717 527 C
ATOM 1146 CH2 TRP A 169 -6.048 20.910 -23.075 1.00 59.39 C
ANISOU 1146 CH2 TRP A 169 5860 6399 10306 1161 2540 770 C
ATOM 1147 N ALA A 170 -5.243 15.877 -16.551 1.00 63.51 N
ANISOU 1147 N ALA A 170 7394 6566 10172 769 3050 78 N
ATOM 1148 CA ALA A 170 -4.507 15.785 -15.294 1.00 58.00 C
ANISOU 1148 CA ALA A 170 7160 5695 9181 741 3128 -112 C
ATOM 1149 C ALA A 170 -3.120 15.179 -15.499 1.00 63.34 C
ANISOU 1149 C ALA A 170 7968 6432 9666 537 2860 -402 C
ATOM 1150 O ALA A 170 -2.159 15.586 -14.836 1.00 62.81 O
ANISOU 1150 O ALA A 170 8284 6264 9318 485 2796 -564 O
ATOM 1151 CB ALA A 170 -5.321 14.985 -14.277 1.00 63.63 C
ANISOU 1151 CB ALA A 170 7887 6363 9925 787 3316 0 C
ATOM 1152 N VAL A 171 -2.992 14.213 -16.411 1.00 61.71 N
ANISOU 1152 N VAL A 171 7443 6411 9594 406 2678 -447 N
ATOM 1153 CA VAL A 171 -1.686 13.624 -16.694 1.00 49.24 C
ANISOU 1153 CA VAL A 171 5976 4895 7839 233 2431 -706 C
ATOM 1154 C VAL A 171 -0.872 14.523 -17.618 1.00 64.00 C
ANISOU 1154 C VAL A 171 7860 6798 9658 178 2226 -778 C
ATOM 1155 O VAL A 171 0.323 14.751 -17.392 1.00 70.29 O
ANISOU 1155 O VAL A 171 8926 7551 10230 90 2092 -968 O
ATOM 1156 CB VAL A 171 -1.848 12.203 -17.272 1.00 52.10 C
ANISOU 1156 CB VAL A 171 6074 5453 8269 68 2225 -685 C
ATOM 1157 CG1 VAL A 171 -0.498 11.621 -17.683 1.00 64.15 C
ANISOU 1157 CG1 VAL A 171 7729 7072 9574 -99 1910 -890 C
ATOM 1158 CG2 VAL A 171 -2.536 11.284 -16.271 1.00 53.82 C
ANISOU 1158 CG2 VAL A 171 6323 5614 8513 100 2441 -635 C
ATOM 1159 N SER A 172 -1.507 15.048 -18.667 1.00 62.59 N
ANISOU 1159 N SER A 172 7387 6709 9687 218 2188 -607 N
ATOM 1160 CA SER A 172 -0.789 15.913 -19.595 1.00 52.08 C
ANISOU 1160 CA SER A 172 6075 5402 8309 169 2006 -656 C
ATOM 1161 C SER A 172 -0.243 17.139 -18.874 1.00 56.77 C
ANISOU 1161 C SER A 172 7059 5764 8748 253 2173 -756 C
ATOM 1162 O SER A 172 0.881 17.585 -19.139 1.00 65.65 O
ANISOU 1162 O SER A 172 8356 6877 9710 130 1997 -902 O
ATOM 1163 CB SER A 172 -1.715 16.330 -20.742 1.00 51.41 C
ANISOU 1163 CB SER A 172 5633 5428 8472 233 1971 -426 C
ATOM 1164 OG SER A 172 -2.162 15.204 -21.487 1.00 39.86 O
ANISOU 1164 OG SER A 172 3850 4173 7122 99 1761 -339 O
ATOM 1165 N LEU A 173 -1.040 17.709 -17.973 1.00 61.04 N
ANISOU 1165 N LEU A 173 7756 6130 9305 437 2482 -645 N
ATOM 1166 CA LEU A 173 -0.619 18.898 -17.249 1.00 60.26 C
ANISOU 1166 CA LEU A 173 8078 5840 8978 467 2564 -681 C
ATOM 1167 C LEU A 173 0.513 18.578 -16.285 1.00 55.12 C
ANISOU 1167 C LEU A 173 7763 5167 8012 300 2403 -874 C
ATOM 1168 O LEU A 173 1.345 19.441 -16.001 1.00 58.80 O
ANISOU 1168 O LEU A 173 8526 5544 8272 219 2321 -961 O
ATOM 1169 CB LEU A 173 -1.816 19.494 -16.514 1.00 62.98 C
ANISOU 1169 CB LEU A 173 8506 6054 9371 683 2877 -461 C
ATOM 1170 CG LEU A 173 -2.877 19.982 -17.509 1.00 66.35 C
ANISOU 1170 CG LEU A 173 8579 6536 10093 857 2988 -219 C
ATOM 1171 CD1 LEU A 173 -4.170 20.477 -16.855 1.00 70.38 C
ANISOU 1171 CD1 LEU A 173 9106 6949 10685 1085 3299 48 C
ATOM 1172 CD2 LEU A 173 -2.289 21.021 -18.431 1.00 66.00 C
ANISOU 1172 CD2 LEU A 173 8594 6447 10035 847 2901 -268 C
ATOM 1173 N ALA A 174 0.548 17.353 -15.755 1.00 52.78 N
ANISOU 1173 N ALA A 174 7415 4962 7676 244 2345 -918 N
ATOM 1174 CA ALA A 174 1.631 16.961 -14.854 1.00 64.49 C
ANISOU 1174 CA ALA A 174 9165 6467 8872 108 2158 -1061 C
ATOM 1175 C ALA A 174 2.931 16.661 -15.587 1.00 76.24 C
ANISOU 1175 C ALA A 174 10577 8104 10287 -74 1842 -1209 C
ATOM 1176 O ALA A 174 3.934 17.356 -15.408 1.00 89.05 O
ANISOU 1176 O ALA A 174 12399 9701 11733 -179 1691 -1286 O
ATOM 1177 CB ALA A 174 1.202 15.763 -14.005 1.00 74.27 C
ANISOU 1177 CB ALA A 174 10394 7742 10084 136 2217 -1033 C
ATOM 1178 N ILE A 175 2.939 15.599 -16.383 1.00 63.49 N
ANISOU 1178 N ILE A 175 8677 6646 8802 -124 1740 -1239 N
ATOM 1179 CA ILE A 175 4.208 15.110 -16.893 1.00 48.39 C
ANISOU 1179 CA ILE A 175 6710 4894 6783 -281 1450 -1353 C
ATOM 1180 C ILE A 175 4.911 16.091 -17.821 1.00 60.43 C
ANISOU 1180 C ILE A 175 8206 6427 8328 -370 1333 -1395 C
ATOM 1181 O ILE A 175 6.119 15.954 -18.063 1.00 64.23 O
ANISOU 1181 O ILE A 175 8684 7033 8688 -501 1102 -1460 O
ATOM 1182 CB ILE A 175 4.002 13.751 -17.560 1.00 49.06 C
ANISOU 1182 CB ILE A 175 6535 5125 6980 -307 1382 -1369 C
ATOM 1183 CG1 ILE A 175 3.042 13.891 -18.744 1.00 46.43 C
ANISOU 1183 CG1 ILE A 175 5895 4841 6907 -268 1422 -1249 C
ATOM 1184 CG2 ILE A 175 3.506 12.723 -16.505 1.00 55.91 C
ANISOU 1184 CG2 ILE A 175 7484 5979 7779 -251 1476 -1332 C
ATOM 1185 CD1 ILE A 175 2.680 12.544 -19.334 1.00 36.78 C
ANISOU 1185 CD1 ILE A 175 4445 3777 5753 -320 1310 -1198 C
ATOM 1186 N MET A 176 4.194 17.060 -18.380 1.00 62.23 N
ANISOU 1186 N MET A 176 8395 6532 8718 -290 1493 -1335 N
ATOM 1187 CA MET A 176 4.874 18.128 -19.102 1.00 62.60 C
ANISOU 1187 CA MET A 176 8486 6548 8752 -378 1401 -1365 C
ATOM 1188 C MET A 176 5.467 19.168 -18.157 1.00 68.87 C
ANISOU 1188 C MET A 176 9641 7210 9316 -429 1396 -1380 C
ATOM 1189 O MET A 176 6.202 20.054 -18.616 1.00 56.30 O
ANISOU 1189 O MET A 176 8126 5593 7673 -545 1294 -1408 O
ATOM 1190 CB MET A 176 3.905 18.816 -20.068 1.00 61.86 C
ANISOU 1190 CB MET A 176 8203 6431 8872 -249 1514 -1208 C
ATOM 1191 CG MET A 176 3.435 17.944 -21.227 1.00 56.36 C
ANISOU 1191 CG MET A 176 7110 5961 8345 -242 1375 -1100 C
ATOM 1192 SD MET A 176 4.625 16.708 -21.748 1.00 54.44 S
ANISOU 1192 SD MET A 176 6750 5950 7983 -421 1071 -1206 S
ATOM 1193 CE MET A 176 3.572 15.633 -22.694 1.00 39.65 C
ANISOU 1193 CE MET A 176 4545 4234 6285 -383 1005 -1068 C
ATOM 1194 N VAL A 177 5.164 19.084 -16.851 1.00 74.09 N
ANISOU 1194 N VAL A 177 10531 7781 9837 -360 1495 -1359 N
ATOM 1195 CA VAL A 177 5.756 20.013 -15.875 1.00 66.09 C
ANISOU 1195 CA VAL A 177 9882 6635 8593 -428 1462 -1386 C
ATOM 1196 C VAL A 177 7.278 19.929 -15.840 1.00 73.35 C
ANISOU 1196 C VAL A 177 10829 7677 9362 -649 1148 -1480 C
ATOM 1197 O VAL A 177 7.937 20.980 -15.868 1.00 71.06 O
ANISOU 1197 O VAL A 177 10709 7310 8979 -775 1069 -1499 O
ATOM 1198 CB VAL A 177 5.134 19.794 -14.493 1.00 55.23 C
ANISOU 1198 CB VAL A 177 8730 5151 7104 -314 1624 -1345 C
ATOM 1199 CG1 VAL A 177 6.013 20.397 -13.401 1.00 50.44 C
ANISOU 1199 CG1 VAL A 177 8483 4451 6231 -438 1508 -1403 C
ATOM 1200 CG2 VAL A 177 3.739 20.395 -14.451 1.00 63.55 C
ANISOU 1200 CG2 VAL A 177 9824 6041 8281 -103 1964 -1210 C
ATOM 1201 N PRO A 178 7.898 18.746 -15.796 1.00 74.82 N
ANISOU 1201 N PRO A 178 10849 8055 9524 -703 968 -1519 N
ATOM 1202 CA PRO A 178 9.377 18.702 -15.821 1.00 63.43 C
ANISOU 1202 CA PRO A 178 9387 6748 7968 -897 681 -1570 C
ATOM 1203 C PRO A 178 9.925 19.399 -17.040 1.00 62.10 C
ANISOU 1203 C PRO A 178 9071 6636 7890 -1019 593 -1561 C
ATOM 1204 O PRO A 178 10.986 20.021 -16.975 1.00 60.28 O
ANISOU 1204 O PRO A 178 8907 6429 7568 -1195 418 -1571 O
ATOM 1205 CB PRO A 178 9.690 17.203 -15.811 1.00 56.57 C
ANISOU 1205 CB PRO A 178 8317 6075 7102 -867 574 -1583 C
ATOM 1206 CG PRO A 178 8.437 16.531 -15.328 1.00 59.81 C
ANISOU 1206 CG PRO A 178 8748 6414 7563 -684 788 -1552 C
ATOM 1207 CD PRO A 178 7.322 17.391 -15.848 1.00 74.49 C
ANISOU 1207 CD PRO A 178 10606 8127 9571 -595 1018 -1502 C
ATOM 1208 N GLN A 179 9.200 19.307 -18.164 1.00 61.97 N
ANISOU 1208 N GLN A 179 8841 6642 8062 -934 711 -1531 N
ATOM 1209 CA GLN A 179 9.518 20.099 -19.344 1.00 47.24 C
ANISOU 1209 CA GLN A 179 6866 4792 6293 -1021 673 -1510 C
ATOM 1210 C GLN A 179 9.592 21.588 -19.005 1.00 58.06 C
ANISOU 1210 C GLN A 179 8535 5950 7575 -1083 732 -1502 C
ATOM 1211 O GLN A 179 10.586 22.258 -19.309 1.00 74.50 O
ANISOU 1211 O GLN A 179 10640 8064 9602 -1261 579 -1498 O
ATOM 1212 CB GLN A 179 8.468 19.833 -20.425 1.00 40.94 C
ANISOU 1212 CB GLN A 179 5840 3994 5721 -888 820 -1480 C
ATOM 1213 CG GLN A 179 8.738 20.554 -21.701 1.00 40.15 C
ANISOU 1213 CG GLN A 179 5621 3907 5728 -959 783 -1453 C
ATOM 1214 CD GLN A 179 9.957 20.007 -22.424 1.00 51.63 C
ANISOU 1214 CD GLN A 179 6853 5611 7153 -1090 552 -1442 C
ATOM 1215 OE1 GLN A 179 10.270 18.812 -22.355 1.00 45.23 O
ANISOU 1215 OE1 GLN A 179 5890 4979 6317 -1068 456 -1449 O
ATOM 1216 NE2 GLN A 179 10.678 20.893 -23.088 1.00 59.25 N
ANISOU 1216 NE2 GLN A 179 7818 6580 8112 -1213 483 -1407 N
ATOM 1217 N ALA A 180 8.560 22.118 -18.341 1.00 59.26 N
ANISOU 1217 N ALA A 180 8923 5886 7706 -934 964 -1480 N
ATOM 1218 CA ALA A 180 8.540 23.546 -18.028 1.00 55.24 C
ANISOU 1218 CA ALA A 180 8737 5158 7094 -966 1055 -1461 C
ATOM 1219 C ALA A 180 9.712 23.954 -17.156 1.00 65.94 C
ANISOU 1219 C ALA A 180 10313 6510 8232 -1181 851 -1507 C
ATOM 1220 O ALA A 180 10.204 25.086 -17.270 1.00 65.68 O
ANISOU 1220 O ALA A 180 10464 6371 8121 -1316 817 -1501 O
ATOM 1221 CB ALA A 180 7.237 23.909 -17.337 1.00 44.14 C
ANISOU 1221 CB ALA A 180 7542 3545 5684 -737 1362 -1400 C
ATOM 1222 N ALA A 181 10.150 23.067 -16.268 1.00 68.54 N
ANISOU 1222 N ALA A 181 10636 6943 8464 -1216 720 -1545 N
ATOM 1223 CA ALA A 181 11.275 23.402 -15.411 1.00 71.39 C
ANISOU 1223 CA ALA A 181 11183 7309 8633 -1426 512 -1578 C
ATOM 1224 C ALA A 181 12.557 23.588 -16.212 1.00 71.00 C
ANISOU 1224 C ALA A 181 10919 7432 8625 -1653 261 -1567 C
ATOM 1225 O ALA A 181 13.368 24.468 -15.899 1.00 68.12 O
ANISOU 1225 O ALA A 181 10726 7014 8143 -1858 139 -1564 O
ATOM 1226 CB ALA A 181 11.442 22.318 -14.358 1.00 77.49 C
ANISOU 1226 CB ALA A 181 11968 8166 9310 -1393 431 -1610 C
ATOM 1227 N VAL A 182 12.767 22.764 -17.239 1.00 64.48 N
ANISOU 1227 N VAL A 182 9722 6819 7960 -1625 189 -1545 N
ATOM 1228 CA VAL A 182 14.027 22.842 -17.967 1.00 56.89 C
ANISOU 1228 CA VAL A 182 8525 6048 7044 -1819 -29 -1502 C
ATOM 1229 C VAL A 182 14.127 24.087 -18.825 1.00 66.19 C
ANISOU 1229 C VAL A 182 9749 7126 8273 -1915 18 -1464 C
ATOM 1230 O VAL A 182 15.237 24.514 -19.166 1.00 62.69 O
ANISOU 1230 O VAL A 182 9203 6785 7831 -2115 -149 -1417 O
ATOM 1231 CB VAL A 182 14.231 21.607 -18.853 1.00 56.02 C
ANISOU 1231 CB VAL A 182 8028 6192 7068 -1746 -87 -1468 C
ATOM 1232 CG1 VAL A 182 14.154 20.372 -18.003 1.00 48.08 C
ANISOU 1232 CG1 VAL A 182 7003 5271 5994 -1652 -125 -1506 C
ATOM 1233 CG2 VAL A 182 13.201 21.586 -19.974 1.00 60.20 C
ANISOU 1233 CG2 VAL A 182 8440 6682 7753 -1592 106 -1456 C
ATOM 1234 N MET A 183 12.997 24.690 -19.177 1.00 71.56 N
ANISOU 1234 N MET A 183 10579 7609 9002 -1771 253 -1470 N
ATOM 1235 CA MET A 183 13.012 25.899 -19.992 1.00 67.64 C
ANISOU 1235 CA MET A 183 10167 6991 8543 -1840 323 -1432 C
ATOM 1236 C MET A 183 13.677 27.066 -19.277 1.00 72.00 C
ANISOU 1236 C MET A 183 11038 7398 8919 -2042 256 -1438 C
ATOM 1237 O MET A 183 13.423 27.328 -18.099 1.00 81.72 O
ANISOU 1237 O MET A 183 12588 8479 9984 -2034 304 -1476 O
ATOM 1238 CB MET A 183 11.585 26.275 -20.392 1.00 58.57 C
ANISOU 1238 CB MET A 183 9130 5644 7478 -1608 612 -1423 C
ATOM 1239 CG MET A 183 10.817 25.155 -21.064 1.00 51.96 C
ANISOU 1239 CG MET A 183 7990 4932 6821 -1423 690 -1416 C
ATOM 1240 SD MET A 183 11.759 24.463 -22.445 1.00 53.95 S
ANISOU 1240 SD MET A 183 7813 5481 7205 -1539 495 -1379 S
ATOM 1241 CE MET A 183 11.514 25.748 -23.645 1.00 43.52 C
ANISOU 1241 CE MET A 183 6557 4003 5974 -1553 619 -1323 C
ATOM 1242 N GLU A 184 14.568 27.741 -19.992 1.00 69.00 N
ANISOU 1242 N GLU A 184 10577 7070 8568 -2237 145 -1391 N
ATOM 1243 CA GLU A 184 15.166 28.980 -19.524 1.00 78.07 C
ANISOU 1243 CA GLU A 184 12037 8068 9560 -2454 96 -1387 C
ATOM 1244 C GLU A 184 15.310 29.949 -20.685 1.00 76.91 C
ANISOU 1244 C GLU A 184 11877 7855 9491 -2525 160 -1333 C
ATOM 1245 O GLU A 184 15.701 29.556 -21.787 1.00 62.81 O
ANISOU 1245 O GLU A 184 9743 6251 7872 -2535 103 -1278 O
ATOM 1246 CB GLU A 184 16.510 28.727 -18.850 1.00 90.14 C
ANISOU 1246 CB GLU A 184 13478 9768 11003 -2709 -185 -1373 C
ATOM 1247 CG GLU A 184 16.366 28.027 -17.516 1.00 96.41 C
ANISOU 1247 CG GLU A 184 14410 10561 11661 -2663 -238 -1428 C
ATOM 1248 CD GLU A 184 15.692 28.909 -16.483 1.00102.48 C
ANISOU 1248 CD GLU A 184 15706 11023 12209 -2646 -86 -1474 C
ATOM 1249 OE1 GLU A 184 15.679 30.145 -16.677 1.00111.45 O
ANISOU 1249 OE1 GLU A 184 17115 11968 13261 -2747 -6 -1458 O
ATOM 1250 OE2 GLU A 184 15.192 28.367 -15.470 1.00 96.45 O
ANISOU 1250 OE2 GLU A 184 15103 10203 11342 -2528 -36 -1515 O
ATOM 1251 N CYS A 185 15.024 31.221 -20.419 1.00 87.48 N
ANISOU 1251 N CYS A 185 13622 8928 10690 -2572 289 -1341 N
ATOM 1252 CA CYS A 185 15.200 32.273 -21.411 1.00 81.86 C
ANISOU 1252 CA CYS A 185 12969 8118 10015 -2656 357 -1291 C
ATOM 1253 C CYS A 185 16.633 32.787 -21.301 1.00 85.44 C
ANISOU 1253 C CYS A 185 13404 8662 10398 -3006 125 -1257 C
ATOM 1254 O CYS A 185 17.087 33.149 -20.208 1.00 91.64 O
ANISOU 1254 O CYS A 185 14454 9377 10989 -3182 20 -1285 O
ATOM 1255 CB CYS A 185 14.185 33.400 -21.198 1.00 74.85 C
ANISOU 1255 CB CYS A 185 12546 6894 9000 -2516 632 -1301 C
ATOM 1256 SG CYS A 185 14.017 34.549 -22.600 1.00 84.38 S
ANISOU 1256 SG CYS A 185 13821 7956 10285 -2501 791 -1233 S
ATOM 1257 N SER A 186 17.369 32.682 -22.410 1.00 84.74 N
ANISOU 1257 N SER A 186 13008 8727 10464 -3109 52 -1183 N
ATOM 1258 CA SER A 186 18.808 33.049 -22.442 1.00 94.32 C
ANISOU 1258 CA SER A 186 14094 10077 11665 -3430 -165 -1119 C
ATOM 1259 C SER A 186 18.998 34.559 -22.571 1.00102.65 C
ANISOU 1259 C SER A 186 15427 10931 12644 -3608 -94 -1089 C
ATOM 1260 O SER A 186 18.476 35.151 -23.524 1.00104.06 O
ANISOU 1260 O SER A 186 15747 10937 12856 -3462 118 -1086 O
ATOM 1261 CB SER A 186 19.527 32.308 -23.529 1.00 96.20 C
ANISOU 1261 CB SER A 186 13786 10639 12125 -3430 -280 -1029 C
ATOM 1262 OG SER A 186 19.679 30.941 -23.180 1.00100.44 O
ANISOU 1262 OG SER A 186 14080 11371 12711 -3286 -359 -1050 O
ATOM 1263 N SER A 187 19.760 35.133 -21.641 1.00110.60 N
ANISOU 1263 N SER A 187 16529 11957 13536 -3935 -279 -1060 N
ATOM 1264 CA SER A 187 20.060 36.585 -21.630 1.00125.06 C
ANISOU 1264 CA SER A 187 18620 13617 15281 -4164 -247 -1024 C
ATOM 1265 C SER A 187 20.831 36.930 -22.904 1.00129.99 C
ANISOU 1265 C SER A 187 18842 14439 16110 -4304 -317 -907 C
ATOM 1266 O SER A 187 20.523 37.962 -23.528 1.00136.69 O
ANISOU 1266 O SER A 187 19838 15136 16960 -4367 -196 -875 O
ATOM 1267 CB SER A 187 20.885 36.905 -20.419 1.00138.57 C
ANISOU 1267 CB SER A 187 20681 15229 16740 -4484 -415 -1042 C
ATOM 1268 OG SER A 187 22.010 36.041 -20.350 1.00142.21 O
ANISOU 1268 OG SER A 187 20844 15960 17231 -4649 -690 -1001 O
ATOM 1269 N VAL A 188 21.782 36.070 -23.273 1.00129.95 N
ANISOU 1269 N VAL A 188 18343 14761 16271 -4335 -486 -834 N
ATOM 1270 CA VAL A 188 22.607 36.263 -24.499 1.00136.62 C
ANISOU 1270 CA VAL A 188 18763 15828 17317 -4453 -541 -695 C
ATOM 1271 C VAL A 188 21.719 35.978 -25.713 1.00152.24 C
ANISOU 1271 C VAL A 188 20940 17679 19225 -4778 -571 -640 C
ATOM 1272 O VAL A 188 22.287 35.847 -26.806 1.00159.60 O
ANISOU 1272 O VAL A 188 22248 18452 19943 -5001 -664 -688 O
ATOM 1273 CB VAL A 188 23.825 35.324 -24.474 1.00125.46 C
ANISOU 1273 CB VAL A 188 17114 14462 16092 -4180 -349 -658 C
ATOM 1274 CG1 VAL A 188 24.647 35.509 -23.209 1.00123.20 C
ANISOU 1274 CG1 VAL A 188 16541 14373 15897 -3917 -364 -680 C
ATOM 1275 CG2 VAL A 188 23.402 33.872 -24.623 1.00114.90 C
ANISOU 1275 CG2 VAL A 188 16176 12808 14675 -4034 -117 -728 C
ATOM 1276 N ALA A 198 21.904 41.159 -28.530 1.00115.15 N
ANISOU 1276 N ALA A 198 17518 11896 14339 -4643 301 -651 N
ATOM 1277 CA ALA A 198 20.901 41.973 -27.846 1.00117.43 C
ANISOU 1277 CA ALA A 198 18386 11852 14380 -4529 458 -759 C
ATOM 1278 C ALA A 198 19.511 41.354 -27.931 1.00124.55 C
ANISOU 1278 C ALA A 198 19310 12693 15321 -4101 644 -814 C
ATOM 1279 O ALA A 198 18.505 42.060 -27.878 1.00129.71 O
ANISOU 1279 O ALA A 198 20375 13068 15841 -3899 871 -854 O
ATOM 1280 CB ALA A 198 20.890 43.384 -28.404 1.00115.72 C
ANISOU 1280 CB ALA A 198 18565 11360 14045 -4632 620 -736 C
ATOM 1281 N PHE A 199 19.482 40.035 -28.139 1.00120.59 N
ANISOU 1281 N PHE A 199 18352 12456 15010 -3952 563 -797 N
ATOM 1282 CA PHE A 199 18.200 39.308 -28.311 1.00114.83 C
ANISOU 1282 CA PHE A 199 17582 11702 14348 -3573 715 -835 C
ATOM 1283 C PHE A 199 18.177 38.068 -27.420 1.00107.95 C
ANISOU 1283 C PHE A 199 16479 11032 13504 -3520 560 -890 C
ATOM 1284 O PHE A 199 19.224 37.432 -27.221 1.00112.55 O
ANISOU 1284 O PHE A 199 16773 11854 14136 -3728 334 -864 O
ATOM 1285 CB PHE A 199 18.032 38.900 -29.774 1.00115.60 C
ANISOU 1285 CB PHE A 199 17379 11894 14650 -3403 815 -749 C
ATOM 1286 CG PHE A 199 19.086 37.945 -30.264 1.00115.35 C
ANISOU 1286 CG PHE A 199 16853 12183 14791 -3563 643 -662 C
ATOM 1287 CD1 PHE A 199 19.125 36.641 -29.805 1.00107.30 C
ANISOU 1287 CD1 PHE A 199 15447 11411 13909 -3412 576 -654 C
ATOM 1288 CD2 PHE A 199 20.040 38.352 -31.179 1.00121.42 C
ANISOU 1288 CD2 PHE A 199 17548 13005 15583 -3855 566 -577 C
ATOM 1289 CE1 PHE A 199 20.095 35.762 -30.253 1.00106.91 C
ANISOU 1289 CE1 PHE A 199 14959 11657 14006 -3521 454 -555 C
ATOM 1290 CE2 PHE A 199 21.010 37.471 -31.626 1.00121.78 C
ANISOU 1290 CE2 PHE A 199 17123 13349 15800 -3969 445 -467 C
ATOM 1291 CZ PHE A 199 21.035 36.178 -31.164 1.00116.86 C
ANISOU 1291 CZ PHE A 199 16129 12972 15302 -3788 398 -453 C
ATOM 1292 N SER A 200 16.976 37.725 -26.958 1.00 96.54 N
ANISOU 1292 N SER A 200 15163 9486 12033 -3227 698 -952 N
ATOM 1293 CA SER A 200 16.728 36.586 -26.084 1.00 88.78 C
ANISOU 1293 CA SER A 200 14019 8650 11065 -3128 601 -1011 C
ATOM 1294 C SER A 200 16.416 35.319 -26.885 1.00 89.05 C
ANISOU 1294 C SER A 200 13607 8910 11317 -2932 593 -980 C
ATOM 1295 O SER A 200 15.953 35.372 -28.027 1.00 96.91 O
ANISOU 1295 O SER A 200 14515 9877 12430 -2788 727 -927 O
ATOM 1296 CB SER A 200 15.576 36.891 -25.120 1.00 84.92 C
ANISOU 1296 CB SER A 200 13935 7913 10416 -2919 782 -1083 C
ATOM 1297 OG SER A 200 16.018 37.658 -24.010 1.00 93.57 O
ANISOU 1297 OG SER A 200 15414 8868 11271 -3132 723 -1126 O
ATOM 1298 N VAL A 201 16.666 34.164 -26.253 1.00 77.07 N
ANISOU 1298 N VAL A 201 11836 7611 9835 -2927 437 -1012 N
ATOM 1299 CA VAL A 201 16.319 32.853 -26.798 1.00 73.28 C
ANISOU 1299 CA VAL A 201 10982 7343 9520 -2741 427 -999 C
ATOM 1300 C VAL A 201 15.714 31.993 -25.689 1.00 67.75 C
ANISOU 1300 C VAL A 201 10307 6667 8769 -2601 406 -1082 C
ATOM 1301 O VAL A 201 16.110 32.085 -24.523 1.00 78.66 O
ANISOU 1301 O VAL A 201 11844 8030 10013 -2722 300 -1128 O
ATOM 1302 CB VAL A 201 17.547 32.133 -27.418 1.00 69.77 C
ANISOU 1302 CB VAL A 201 10100 7213 9195 -2888 248 -913 C
ATOM 1303 CG1 VAL A 201 18.348 33.086 -28.313 1.00 73.42 C
ANISOU 1303 CG1 VAL A 201 10559 7647 9690 -3078 260 -819 C
ATOM 1304 CG2 VAL A 201 18.448 31.529 -26.327 1.00 73.51 C
ANISOU 1304 CG2 VAL A 201 10444 7870 9616 -3034 27 -926 C
ATOM 1305 N CYS A 202 14.738 31.153 -26.057 1.00 48.59 N
ANISOU 1305 N CYS A 202 7738 4275 6450 -2351 513 -1097 N
ATOM 1306 CA CYS A 202 14.069 30.223 -25.143 1.00 61.32 C
ANISOU 1306 CA CYS A 202 9338 5919 8041 -2195 522 -1166 C
ATOM 1307 C CYS A 202 14.494 28.802 -25.494 1.00 68.88 C
ANISOU 1307 C CYS A 202 9876 7187 9109 -2175 379 -1150 C
ATOM 1308 O CYS A 202 14.287 28.364 -26.629 1.00 68.06 O
ANISOU 1308 O CYS A 202 9539 7183 9140 -2089 426 -1106 O
ATOM 1309 CB CYS A 202 12.547 30.378 -25.235 1.00 67.83 C
ANISOU 1309 CB CYS A 202 10329 6529 8912 -1911 782 -1179 C
ATOM 1310 SG CYS A 202 11.545 29.314 -24.179 1.00 71.59 S
ANISOU 1310 SG CYS A 202 10798 7013 9389 -1690 857 -1242 S
ATOM 1311 N ASP A 203 15.101 28.096 -24.535 1.00 73.28 N
ANISOU 1311 N ASP A 203 10356 7889 9597 -2248 215 -1178 N
ATOM 1312 CA ASP A 203 15.559 26.728 -24.767 1.00 65.73 C
ANISOU 1312 CA ASP A 203 9034 7223 8719 -2208 92 -1151 C
ATOM 1313 C ASP A 203 15.698 26.012 -23.430 1.00 54.57 C
ANISOU 1313 C ASP A 203 7667 5863 7202 -2205 -14 -1209 C
ATOM 1314 O ASP A 203 15.776 26.642 -22.371 1.00 66.03 O
ANISOU 1314 O ASP A 203 9404 7167 8518 -2296 -40 -1255 O
ATOM 1315 CB ASP A 203 16.897 26.695 -25.527 1.00 73.28 C
ANISOU 1315 CB ASP A 203 9711 8394 9739 -2370 -45 -1043 C
ATOM 1316 CG ASP A 203 17.023 25.500 -26.457 1.00 89.36 C
ANISOU 1316 CG ASP A 203 11393 10675 11887 -2244 -47 -984 C
ATOM 1317 OD1 ASP A 203 16.409 25.550 -27.544 1.00 98.31 O
ANISOU 1317 OD1 ASP A 203 12478 11773 13101 -2138 85 -969 O
ATOM 1318 OD2 ASP A 203 17.743 24.528 -26.124 1.00 97.21 O
ANISOU 1318 OD2 ASP A 203 12171 11888 12878 -2245 -170 -947 O
ATOM 1319 N GLU A 204 15.761 24.681 -23.504 1.00 46.54 N
ANISOU 1319 N GLU A 204 6388 5059 6237 -2100 -71 -1202 N
ATOM 1320 CA GLU A 204 15.933 23.864 -22.310 1.00 52.04 C
ANISOU 1320 CA GLU A 204 7110 5824 6840 -2086 -171 -1248 C
ATOM 1321 C GLU A 204 17.305 24.080 -21.677 1.00 60.17 C
ANISOU 1321 C GLU A 204 8104 6961 7796 -2306 -386 -1204 C
ATOM 1322 O GLU A 204 18.319 24.129 -22.378 1.00 70.09 O
ANISOU 1322 O GLU A 204 9113 8389 9131 -2418 -481 -1104 O
ATOM 1323 CB GLU A 204 15.752 22.385 -22.666 1.00 54.65 C
ANISOU 1323 CB GLU A 204 7168 6361 7237 -1925 -170 -1239 C
ATOM 1324 CG GLU A 204 14.374 22.041 -23.247 1.00 65.83 C
ANISOU 1324 CG GLU A 204 8580 7692 8740 -1717 26 -1283 C
ATOM 1325 CD GLU A 204 14.315 20.642 -23.825 1.00 67.17 C
ANISOU 1325 CD GLU A 204 8471 8073 8975 -1581 18 -1265 C
ATOM 1326 OE1 GLU A 204 15.120 19.796 -23.382 1.00 67.04 O
ANISOU 1326 OE1 GLU A 204 8339 8230 8901 -1605 -104 -1246 O
ATOM 1327 OE2 GLU A 204 13.455 20.386 -24.699 1.00 70.19 O
ANISOU 1327 OE2 GLU A 204 8765 8439 9466 -1449 130 -1267 O
ATOM 1328 N ARG A 205 17.333 24.228 -20.353 1.00 59.59 N
ANISOU 1328 N ARG A 205 8278 6788 7574 -2369 -450 -1269 N
ATOM 1329 CA ARG A 205 18.580 24.330 -19.594 1.00 68.66 C
ANISOU 1329 CA ARG A 205 9403 8050 8637 -2585 -671 -1231 C
ATOM 1330 C ARG A 205 18.834 23.011 -18.871 1.00 80.89 C
ANISOU 1330 C ARG A 205 10816 9774 10144 -2509 -782 -1240 C
ATOM 1331 O ARG A 205 18.249 22.741 -17.821 1.00104.35 O
ANISOU 1331 O ARG A 205 14031 12627 12990 -2439 -753 -1327 O
ATOM 1332 CB ARG A 205 18.541 25.497 -18.616 1.00 77.90 C
ANISOU 1332 CB ARG A 205 10987 8982 9629 -2745 -682 -1284 C
ATOM 1333 CG ARG A 205 19.854 25.670 -17.883 1.00 88.21 C
ANISOU 1333 CG ARG A 205 12271 10409 10835 -3009 -933 -1231 C
ATOM 1334 CD ARG A 205 20.098 27.076 -17.394 1.00103.11 C
ANISOU 1334 CD ARG A 205 14524 12087 12568 -3246 -962 -1240 C
ATOM 1335 NE ARG A 205 21.355 27.130 -16.648 1.00117.00 N
ANISOU 1335 NE ARG A 205 16246 13983 14226 -3517 -1231 -1175 N
ATOM 1336 CZ ARG A 205 21.915 28.247 -16.196 1.00124.60 C
ANISOU 1336 CZ ARG A 205 17477 14825 15042 -3801 -1335 -1152 C
ATOM 1337 NH1 ARG A 205 23.061 28.203 -15.529 1.00121.43 N
ANISOU 1337 NH1 ARG A 205 17009 14572 14556 -4057 -1604 -1074 N
ATOM 1338 NH2 ARG A 205 21.329 29.414 -16.417 1.00131.51 N
ANISOU 1338 NH2 ARG A 205 18694 15428 15845 -3833 -1174 -1195 N
ATOM 1339 N TRP A 206 19.704 22.183 -19.444 1.00 79.65 N
ANISOU 1339 N TRP A 206 10280 9896 10086 -2508 -888 -1140 N
ATOM 1340 CA TRP A 206 20.067 20.891 -18.873 1.00 81.39 C
ANISOU 1340 CA TRP A 206 10346 10313 10267 -2433 -995 -1125 C
ATOM 1341 C TRP A 206 21.393 20.995 -18.135 1.00 82.72 C
ANISOU 1341 C TRP A 206 10428 10639 10364 -2642 -1237 -1043 C
ATOM 1342 O TRP A 206 22.377 21.493 -18.689 1.00 75.68 O
ANISOU 1342 O TRP A 206 9324 9876 9554 -2793 -1321 -922 O
ATOM 1343 CB TRP A 206 20.136 19.815 -19.961 1.00 82.20 C
ANISOU 1343 CB TRP A 206 10098 10633 10501 -2267 -930 -1047 C
ATOM 1344 CG TRP A 206 18.789 19.433 -20.469 1.00 76.55 C
ANISOU 1344 CG TRP A 206 9473 9793 9820 -2062 -719 -1134 C
ATOM 1345 CD1 TRP A 206 18.223 19.796 -21.651 1.00 72.57 C
ANISOU 1345 CD1 TRP A 206 8916 9231 9425 -1991 -567 -1120 C
ATOM 1346 CD2 TRP A 206 17.832 18.604 -19.805 1.00 79.15 C
ANISOU 1346 CD2 TRP A 206 9953 10045 10075 -1904 -635 -1242 C
ATOM 1347 NE1 TRP A 206 16.970 19.251 -21.766 1.00 74.30 N
ANISOU 1347 NE1 TRP A 206 9222 9354 9653 -1803 -405 -1207 N
ATOM 1348 CE2 TRP A 206 16.706 18.512 -20.644 1.00 79.38 C
ANISOU 1348 CE2 TRP A 206 9986 9983 10193 -1746 -432 -1281 C
ATOM 1349 CE3 TRP A 206 17.817 17.929 -18.578 1.00 78.50 C
ANISOU 1349 CE3 TRP A 206 10005 9963 9860 -1880 -707 -1303 C
ATOM 1350 CZ2 TRP A 206 15.579 17.776 -20.301 1.00 80.54 C
ANISOU 1350 CZ2 TRP A 206 10236 10041 10323 -1570 -295 -1368 C
ATOM 1351 CZ3 TRP A 206 16.696 17.198 -18.237 1.00 78.49 C
ANISOU 1351 CZ3 TRP A 206 10138 9859 9827 -1697 -554 -1398 C
ATOM 1352 CH2 TRP A 206 15.592 17.127 -19.096 1.00 81.07 C
ANISOU 1352 CH2 TRP A 206 10436 10100 10266 -1547 -347 -1423 C
ATOM 1353 N ALA A 207 21.406 20.527 -16.882 1.00 81.37 N
ANISOU 1353 N ALA A 207 10424 10458 10037 -2653 -1346 -1098 N
ATOM 1354 CA ALA A 207 22.610 20.595 -16.062 1.00 69.97 C
ANISOU 1354 CA ALA A 207 8923 9164 8499 -2859 -1600 -1012 C
ATOM 1355 C ALA A 207 23.704 19.656 -16.553 1.00 91.44 C
ANISOU 1355 C ALA A 207 11172 12243 11328 -2826 -1723 -839 C
ATOM 1356 O ALA A 207 24.881 19.879 -16.250 1.00104.91 O
ANISOU 1356 O ALA A 207 12716 14121 13023 -3013 -1925 -706 O
ATOM 1357 CB ALA A 207 22.278 20.273 -14.604 1.00 52.24 C
ANISOU 1357 CB ALA A 207 7002 6807 6040 -2857 -1675 -1109 C
ATOM 1358 N ASP A 208 23.352 18.613 -17.300 1.00 91.51 N
ANISOU 1358 N ASP A 208 10960 12376 11435 -2592 -1596 -819 N
ATOM 1359 CA ASP A 208 24.345 17.637 -17.727 1.00 84.74 C
ANISOU 1359 CA ASP A 208 9675 11862 10660 -2509 -1673 -634 C
ATOM 1360 C ASP A 208 23.914 17.009 -19.040 1.00 79.74 C
ANISOU 1360 C ASP A 208 8831 11304 10164 -2290 -1457 -601 C
ATOM 1361 O ASP A 208 22.747 17.075 -19.430 1.00 78.74 O
ANISOU 1361 O ASP A 208 8898 10979 10043 -2191 -1281 -739 O
ATOM 1362 CB ASP A 208 24.557 16.546 -16.672 1.00 86.11 C
ANISOU 1362 CB ASP A 208 9848 12177 10695 -2432 -1817 -623 C
ATOM 1363 CG ASP A 208 23.297 15.768 -16.384 1.00 95.28 C
ANISOU 1363 CG ASP A 208 11250 13193 11760 -2241 -1676 -796 C
ATOM 1364 OD1 ASP A 208 22.623 16.086 -15.382 1.00 98.69 O
ANISOU 1364 OD1 ASP A 208 12067 13386 12046 -2288 -1686 -950 O
ATOM 1365 OD2 ASP A 208 22.961 14.866 -17.182 1.00102.27 O
ANISOU 1365 OD2 ASP A 208 11952 14196 12709 -2041 -1531 -776 O
ATOM 1366 N ASP A 209 24.893 16.420 -19.727 1.00 82.62 N
ANISOU 1366 N ASP A 209 8798 11959 10632 -2206 -1460 -397 N
ATOM 1367 CA ASP A 209 24.660 15.841 -21.043 1.00 85.20 C
ANISOU 1367 CA ASP A 209 8922 12379 11072 -1994 -1243 -335 C
ATOM 1368 C ASP A 209 23.688 14.669 -21.005 1.00 78.25 C
ANISOU 1368 C ASP A 209 8124 11504 10105 -1770 -1125 -450 C
ATOM 1369 O ASP A 209 22.942 14.459 -21.968 1.00 76.76 O
ANISOU 1369 O ASP A 209 7946 11255 9963 -1637 -927 -513 O
ATOM 1370 CB ASP A 209 25.986 15.384 -21.636 1.00 97.96 C
ANISOU 1370 CB ASP A 209 10121 14306 12793 -1909 -1244 -70 C
ATOM 1371 CG ASP A 209 27.054 16.446 -21.567 1.00109.01 C
ANISOU 1371 CG ASP A 209 11408 15744 14266 -2153 -1375 48 C
ATOM 1372 OD1 ASP A 209 26.697 17.640 -21.502 1.00114.84 O
ANISOU 1372 OD1 ASP A 209 12379 16254 15001 -2364 -1400 -72 O
ATOM 1373 OD2 ASP A 209 28.255 16.100 -21.581 1.00114.57 O
ANISOU 1373 OD2 ASP A 209 11794 16710 15026 -2129 -1441 272 O
ATOM 1374 N LEU A 210 23.694 13.892 -19.920 1.00 72.38 N
ANISOU 1374 N LEU A 210 7442 10837 9221 -1728 -1245 -486 N
ATOM 1375 CA LEU A 210 23.025 12.598 -19.945 1.00 67.68 C
ANISOU 1375 CA LEU A 210 6875 10296 8544 -1462 -1113 -563 C
ATOM 1376 C LEU A 210 21.531 12.731 -19.683 1.00 67.74 C
ANISOU 1376 C LEU A 210 7278 9963 8498 -1430 -981 -815 C
ATOM 1377 O LEU A 210 20.731 12.002 -20.281 1.00 85.59 O
ANISOU 1377 O LEU A 210 9611 12129 10780 -1189 -776 -871 O
ATOM 1378 CB LEU A 210 23.672 11.660 -18.921 1.00 75.10 C
ANISOU 1378 CB LEU A 210 7752 11424 9358 -1362 -1263 -469 C
ATOM 1379 CG LEU A 210 23.069 10.280 -18.648 1.00 72.90 C
ANISOU 1379 CG LEU A 210 7639 11085 8974 -1025 -1111 -530 C
ATOM 1380 CD1 LEU A 210 23.104 9.440 -19.903 1.00 74.34 C
ANISOU 1380 CD1 LEU A 210 7673 11336 9235 -719 -863 -427 C
ATOM 1381 CD2 LEU A 210 23.813 9.590 -17.514 1.00 68.51 C
ANISOU 1381 CD2 LEU A 210 7036 10714 8280 -974 -1301 -425 C
ATOM 1382 N ALA A 211 21.139 13.639 -18.790 1.00 56.30 N
ANISOU 1382 N ALA A 211 6097 8320 6973 -1668 -1088 -951 N
ATOM 1383 CA ALA A 211 19.721 13.803 -18.479 1.00 58.72 C
ANISOU 1383 CA ALA A 211 6757 8313 7240 -1617 -933 -1157 C
ATOM 1384 C ALA A 211 18.891 14.128 -19.714 1.00 69.01 C
ANISOU 1384 C ALA A 211 8039 9491 8692 -1526 -722 -1191 C
ATOM 1385 O ALA A 211 17.858 13.468 -19.931 1.00 75.15 O
ANISOU 1385 O ALA A 211 8918 10150 9485 -1324 -551 -1265 O
ATOM 1386 CB ALA A 211 19.557 14.878 -17.405 1.00 64.80 C
ANISOU 1386 CB ALA A 211 7865 8830 7927 -1783 -1023 -1212 C
ATOM 1387 N PRO A 212 19.266 15.104 -20.550 1.00 68.01 N
ANISOU 1387 N PRO A 212 7810 9355 8677 -1631 -722 -1099 N
ATOM 1388 CA PRO A 212 18.465 15.371 -21.750 1.00 45.64 C
ANISOU 1388 CA PRO A 212 4965 6415 5962 -1539 -539 -1125 C
ATOM 1389 C PRO A 212 18.359 14.163 -22.659 1.00 37.78 C
ANISOU 1389 C PRO A 212 3795 5553 5005 -1301 -424 -1080 C
ATOM 1390 O PRO A 212 17.327 13.994 -23.320 1.00 48.78 O
ANISOU 1390 O PRO A 212 5275 6812 6449 -1176 -284 -1136 O
ATOM 1391 CB PRO A 212 19.213 16.543 -22.422 1.00 41.09 C
ANISOU 1391 CB PRO A 212 4295 5847 5472 -1691 -587 -999 C
ATOM 1392 CG PRO A 212 20.583 16.524 -21.824 1.00 47.99 C
ANISOU 1392 CG PRO A 212 5007 6915 6313 -1822 -783 -873 C
ATOM 1393 CD PRO A 212 20.391 16.038 -20.415 1.00 67.78 C
ANISOU 1393 CD PRO A 212 7698 9384 8671 -1832 -888 -967 C
ATOM 1394 N LYS A 213 19.401 13.326 -22.726 1.00 35.42 N
ANISOU 1394 N LYS A 213 3284 5497 4676 -1206 -475 -944 N
ATOM 1395 CA LYS A 213 19.316 12.101 -23.517 1.00 45.10 C
ANISOU 1395 CA LYS A 213 4447 6795 5895 -931 -337 -882 C
ATOM 1396 C LYS A 213 18.237 11.175 -22.978 1.00 51.64 C
ANISOU 1396 C LYS A 213 5503 7476 6640 -786 -264 -1010 C
ATOM 1397 O LYS A 213 17.429 10.634 -23.741 1.00 63.01 O
ANISOU 1397 O LYS A 213 7029 8818 8096 -654 -137 -1043 O
ATOM 1398 CB LYS A 213 20.666 11.384 -23.528 1.00 48.66 C
ANISOU 1398 CB LYS A 213 4647 7525 6316 -823 -379 -689 C
ATOM 1399 CG LYS A 213 21.787 12.157 -24.190 1.00 62.12 C
ANISOU 1399 CG LYS A 213 6067 9410 8127 -946 -419 -513 C
ATOM 1400 CD LYS A 213 23.133 11.511 -23.909 1.00 75.68 C
ANISOU 1400 CD LYS A 213 7494 11432 9829 -852 -484 -290 C
ATOM 1401 CE LYS A 213 24.253 12.224 -24.648 1.00 77.83 C
ANISOU 1401 CE LYS A 213 7434 11904 10234 -966 -493 -75 C
ATOM 1402 NZ LYS A 213 24.048 12.148 -26.119 1.00 74.49 N
ANISOU 1402 NZ LYS A 213 7018 11416 9869 -798 -251 -30 N
ATOM 1403 N ILE A 214 18.220 10.980 -21.660 1.00 45.46 N
ANISOU 1403 N ILE A 214 4836 6674 5762 -828 -353 -1075 N
ATOM 1404 CA ILE A 214 17.265 10.070 -21.043 1.00 51.77 C
ANISOU 1404 CA ILE A 214 5850 7338 6481 -697 -271 -1182 C
ATOM 1405 C ILE A 214 15.869 10.676 -21.059 1.00 55.03 C
ANISOU 1405 C ILE A 214 6439 7505 6963 -761 -176 -1313 C
ATOM 1406 O ILE A 214 14.881 9.991 -21.360 1.00 63.69 O
ANISOU 1406 O ILE A 214 7625 8498 8077 -648 -58 -1356 O
ATOM 1407 CB ILE A 214 17.710 9.714 -19.613 1.00 57.30 C
ANISOU 1407 CB ILE A 214 6642 8087 7043 -715 -387 -1200 C
ATOM 1408 CG1 ILE A 214 19.014 8.916 -19.646 1.00 64.78 C
ANISOU 1408 CG1 ILE A 214 7381 9302 7931 -590 -463 -1030 C
ATOM 1409 CG2 ILE A 214 16.644 8.916 -18.883 1.00 52.73 C
ANISOU 1409 CG2 ILE A 214 6317 7335 6384 -605 -280 -1317 C
ATOM 1410 CD1 ILE A 214 19.875 9.159 -18.443 1.00 74.18 C
ANISOU 1410 CD1 ILE A 214 8547 10616 9024 -715 -679 -986 C
ATOM 1411 N TYR A 215 15.760 11.965 -20.735 1.00 51.49 N
ANISOU 1411 N TYR A 215 6050 6957 6555 -945 -223 -1362 N
ATOM 1412 CA TYR A 215 14.451 12.607 -20.737 1.00 41.80 C
ANISOU 1412 CA TYR A 215 4980 5500 5403 -966 -103 -1452 C
ATOM 1413 C TYR A 215 13.786 12.482 -22.108 1.00 48.11 C
ANISOU 1413 C TYR A 215 5671 6282 6325 -879 -7 -1410 C
ATOM 1414 O TYR A 215 12.668 11.958 -22.224 1.00 57.73 O
ANISOU 1414 O TYR A 215 6950 7401 7583 -787 93 -1439 O
ATOM 1415 CB TYR A 215 14.588 14.072 -20.306 1.00 44.81 C
ANISOU 1415 CB TYR A 215 5477 5762 5785 -1148 -149 -1473 C
ATOM 1416 CG TYR A 215 13.287 14.850 -20.237 1.00 56.93 C
ANISOU 1416 CG TYR A 215 7188 7057 7387 -1103 4 -1494 C
ATOM 1417 CD1 TYR A 215 12.362 14.620 -19.219 1.00 73.33 C
ANISOU 1417 CD1 TYR A 215 9471 8977 9414 -1015 112 -1540 C
ATOM 1418 CD2 TYR A 215 12.976 15.790 -21.197 1.00 46.60 C
ANISOU 1418 CD2 TYR A 215 5826 5686 6192 -1132 56 -1456 C
ATOM 1419 CE1 TYR A 215 11.171 15.339 -19.164 1.00 72.52 C
ANISOU 1419 CE1 TYR A 215 9488 8679 9388 -958 278 -1543 C
ATOM 1420 CE2 TYR A 215 11.790 16.505 -21.157 1.00 34.75 C
ANISOU 1420 CE2 TYR A 215 4457 3984 4762 -1080 207 -1476 C
ATOM 1421 CZ TYR A 215 10.888 16.276 -20.140 1.00 58.97 C
ANISOU 1421 CZ TYR A 215 7700 6911 7793 -990 326 -1516 C
ATOM 1422 OH TYR A 215 9.716 17.005 -20.125 1.00 72.37 O
ANISOU 1422 OH TYR A 215 9500 8415 9582 -920 509 -1517 O
ATOM 1423 N HIS A 216 14.474 12.945 -23.164 1.00 49.75 N
ANISOU 1423 N HIS A 216 5721 6591 6590 -920 -46 -1327 N
ATOM 1424 CA HIS A 216 13.916 12.960 -24.515 1.00 47.39 C
ANISOU 1424 CA HIS A 216 5359 6266 6382 -855 22 -1281 C
ATOM 1425 C HIS A 216 13.821 11.570 -25.150 1.00 45.04 C
ANISOU 1425 C HIS A 216 5046 6036 6031 -698 58 -1243 C
ATOM 1426 O HIS A 216 12.981 11.368 -26.033 1.00 49.82 O
ANISOU 1426 O HIS A 216 5678 6571 6682 -655 100 -1233 O
ATOM 1427 CB HIS A 216 14.745 13.917 -25.377 1.00 49.39 C
ANISOU 1427 CB HIS A 216 5489 6587 6690 -949 -13 -1202 C
ATOM 1428 CG HIS A 216 14.486 15.364 -25.081 1.00 57.31 C
ANISOU 1428 CG HIS A 216 6575 7449 7751 -1104 -15 -1243 C
ATOM 1429 ND1 HIS A 216 13.298 15.983 -25.388 1.00 55.62 N
ANISOU 1429 ND1 HIS A 216 6455 7059 7619 -1078 73 -1272 N
ATOM 1430 CD2 HIS A 216 15.264 16.317 -24.514 1.00 58.30 C
ANISOU 1430 CD2 HIS A 216 6737 7570 7845 -1268 -91 -1225 C
ATOM 1431 CE1 HIS A 216 13.346 17.250 -25.014 1.00 58.46 C
ANISOU 1431 CE1 HIS A 216 6931 7297 7983 -1187 80 -1275 C
ATOM 1432 NE2 HIS A 216 14.531 17.481 -24.483 1.00 58.80 N
ANISOU 1432 NE2 HIS A 216 6965 7429 7946 -1313 -28 -1247 N
ATOM 1433 N SER A 217 14.651 10.615 -24.723 1.00 53.16 N
ANISOU 1433 N SER A 217 6056 7190 6951 -614 37 -1213 N
ATOM 1434 CA SER A 217 14.464 9.226 -25.141 1.00 52.24 C
ANISOU 1434 CA SER A 217 6015 7086 6749 -456 97 -1193 C
ATOM 1435 C SER A 217 13.203 8.635 -24.520 1.00 54.79 C
ANISOU 1435 C SER A 217 6494 7262 7064 -448 139 -1286 C
ATOM 1436 O SER A 217 12.413 7.972 -25.206 1.00 46.29 O
ANISOU 1436 O SER A 217 5497 6109 5981 -413 177 -1285 O
ATOM 1437 CB SER A 217 15.685 8.381 -24.749 1.00 40.12 C
ANISOU 1437 CB SER A 217 4430 5716 5097 -334 89 -1116 C
ATOM 1438 OG SER A 217 16.896 8.991 -25.168 1.00 49.30 O
ANISOU 1438 OG SER A 217 5393 7044 6296 -358 52 -999 O
ATOM 1439 N CYS A 218 12.974 8.911 -23.229 1.00 54.65 N
ANISOU 1439 N CYS A 218 6533 7191 7040 -499 130 -1357 N
ATOM 1440 CA CYS A 218 11.793 8.376 -22.551 1.00 43.09 C
ANISOU 1440 CA CYS A 218 5205 5588 5579 -486 203 -1425 C
ATOM 1441 C CYS A 218 10.504 8.948 -23.137 1.00 50.95 C
ANISOU 1441 C CYS A 218 6171 6463 6725 -546 250 -1424 C
ATOM 1442 O CYS A 218 9.516 8.216 -23.294 1.00 63.26 O
ANISOU 1442 O CYS A 218 7775 7952 8310 -533 295 -1420 O
ATOM 1443 CB CYS A 218 11.872 8.634 -21.037 1.00 36.15 C
ANISOU 1443 CB CYS A 218 4431 4661 4642 -514 207 -1493 C
ATOM 1444 SG CYS A 218 13.119 7.649 -20.141 1.00 50.01 S
ANISOU 1444 SG CYS A 218 6242 6555 6204 -420 139 -1477 S
ATOM 1445 N PHE A 219 10.479 10.255 -23.445 1.00 47.32 N
ANISOU 1445 N PHE A 219 5634 5978 6366 -618 235 -1410 N
ATOM 1446 CA PHE A 219 9.222 10.869 -23.871 1.00 47.17 C
ANISOU 1446 CA PHE A 219 5576 5850 6497 -644 289 -1383 C
ATOM 1447 C PHE A 219 8.920 10.664 -25.347 1.00 47.34 C
ANISOU 1447 C PHE A 219 5514 5908 6565 -645 233 -1308 C
ATOM 1448 O PHE A 219 7.757 10.789 -25.743 1.00 51.74 O
ANISOU 1448 O PHE A 219 6020 6402 7235 -661 247 -1260 O
ATOM 1449 CB PHE A 219 9.200 12.359 -23.537 1.00 37.45 C
ANISOU 1449 CB PHE A 219 4355 4537 5338 -697 324 -1394 C
ATOM 1450 CG PHE A 219 8.596 12.666 -22.194 1.00 54.47 C
ANISOU 1450 CG PHE A 219 6648 6555 7494 -684 439 -1448 C
ATOM 1451 CD1 PHE A 219 7.219 12.576 -21.989 1.00 57.33 C
ANISOU 1451 CD1 PHE A 219 6999 6812 7972 -624 570 -1409 C
ATOM 1452 CD2 PHE A 219 9.405 13.061 -21.142 1.00 62.65 C
ANISOU 1452 CD2 PHE A 219 7830 7570 8404 -727 416 -1501 C
ATOM 1453 CE1 PHE A 219 6.675 12.857 -20.740 1.00 65.50 C
ANISOU 1453 CE1 PHE A 219 8187 7703 8997 -582 723 -1444 C
ATOM 1454 CE2 PHE A 219 8.882 13.346 -19.908 1.00 64.53 C
ANISOU 1454 CE2 PHE A 219 8257 7668 8596 -694 524 -1519 C
ATOM 1455 CZ PHE A 219 7.517 13.247 -19.692 1.00 66.73 C
ANISOU 1455 CZ PHE A 219 8545 7819 8988 -612 702 -1506 C
ATOM 1456 N PHE A 220 9.926 10.392 -26.175 1.00 48.72 N
ANISOU 1456 N PHE A 220 5676 6183 6653 -625 172 -1280 N
ATOM 1457 CA PHE A 220 9.614 9.966 -27.532 1.00 41.11 C
ANISOU 1457 CA PHE A 220 4717 5224 5678 -618 125 -1217 C
ATOM 1458 C PHE A 220 8.960 8.594 -27.509 1.00 45.67 C
ANISOU 1458 C PHE A 220 5406 5763 6183 -608 120 -1228 C
ATOM 1459 O PHE A 220 8.032 8.316 -28.280 1.00 48.50 O
ANISOU 1459 O PHE A 220 5781 6072 6574 -665 62 -1183 O
ATOM 1460 CB PHE A 220 10.868 9.950 -28.399 1.00 41.72 C
ANISOU 1460 CB PHE A 220 4792 5397 5661 -571 109 -1172 C
ATOM 1461 CG PHE A 220 10.656 9.321 -29.748 1.00 45.86 C
ANISOU 1461 CG PHE A 220 5415 5900 6110 -546 77 -1117 C
ATOM 1462 CD1 PHE A 220 9.981 10.001 -30.754 1.00 51.34 C
ANISOU 1462 CD1 PHE A 220 6086 6542 6877 -602 19 -1066 C
ATOM 1463 CD2 PHE A 220 11.121 8.056 -30.019 1.00 43.55 C
ANISOU 1463 CD2 PHE A 220 5278 5620 5650 -459 105 -1109 C
ATOM 1464 CE1 PHE A 220 9.771 9.427 -32.017 1.00 31.85 C
ANISOU 1464 CE1 PHE A 220 3761 4036 4304 -599 -37 -1015 C
ATOM 1465 CE2 PHE A 220 10.915 7.488 -31.268 1.00 33.81 C
ANISOU 1465 CE2 PHE A 220 4215 4327 4306 -448 78 -1065 C
ATOM 1466 CZ PHE A 220 10.240 8.176 -32.265 1.00 22.43 C
ANISOU 1466 CZ PHE A 220 2760 2834 2926 -531 -6 -1022 C
ATOM 1467 N ILE A 221 9.447 7.719 -26.630 1.00 44.41 N
ANISOU 1467 N ILE A 221 5337 5624 5914 -549 166 -1277 N
ATOM 1468 CA ILE A 221 8.830 6.409 -26.461 1.00 32.85 C
ANISOU 1468 CA ILE A 221 4016 4096 4369 -551 180 -1294 C
ATOM 1469 C ILE A 221 7.426 6.554 -25.881 1.00 44.81 C
ANISOU 1469 C ILE A 221 5471 5526 6029 -640 203 -1294 C
ATOM 1470 O ILE A 221 6.467 5.940 -26.367 1.00 40.57 O
ANISOU 1470 O ILE A 221 4964 4936 5516 -727 158 -1253 O
ATOM 1471 CB ILE A 221 9.715 5.505 -25.579 1.00 30.02 C
ANISOU 1471 CB ILE A 221 3777 3775 3856 -440 242 -1335 C
ATOM 1472 CG1 ILE A 221 11.075 5.242 -26.250 1.00 27.27 C
ANISOU 1472 CG1 ILE A 221 3456 3528 3376 -319 245 -1286 C
ATOM 1473 CG2 ILE A 221 8.996 4.212 -25.264 1.00 42.74 C
ANISOU 1473 CG2 ILE A 221 5567 5289 5385 -455 279 -1359 C
ATOM 1474 CD1 ILE A 221 10.979 4.492 -27.575 1.00 33.86 C
ANISOU 1474 CD1 ILE A 221 4457 4307 4100 -297 241 -1241 C
ATOM 1475 N VAL A 222 7.285 7.368 -24.833 1.00 55.19 N
ANISOU 1475 N VAL A 222 6710 6822 7438 -626 277 -1324 N
ATOM 1476 CA VAL A 222 6.047 7.392 -24.059 1.00 51.89 C
ANISOU 1476 CA VAL A 222 6253 6318 7145 -662 363 -1309 C
ATOM 1477 C VAL A 222 4.909 8.071 -24.820 1.00 48.86 C
ANISOU 1477 C VAL A 222 5697 5917 6951 -727 331 -1204 C
ATOM 1478 O VAL A 222 3.748 7.653 -24.715 1.00 56.91 O
ANISOU 1478 O VAL A 222 6646 6901 8077 -786 355 -1134 O
ATOM 1479 CB VAL A 222 6.300 8.063 -22.698 1.00 50.53 C
ANISOU 1479 CB VAL A 222 6123 6100 6975 -605 477 -1370 C
ATOM 1480 CG1 VAL A 222 5.029 8.669 -22.153 1.00 52.35 C
ANISOU 1480 CG1 VAL A 222 6280 6233 7379 -606 607 -1318 C
ATOM 1481 CG2 VAL A 222 6.872 7.037 -21.718 1.00 50.48 C
ANISOU 1481 CG2 VAL A 222 6289 6092 6801 -553 515 -1443 C
ATOM 1482 N THR A 223 5.210 9.121 -25.593 1.00 47.83 N
ANISOU 1482 N THR A 223 5482 5819 6873 -719 276 -1171 N
ATOM 1483 CA THR A 223 4.162 9.946 -26.191 1.00 48.00 C
ANISOU 1483 CA THR A 223 5333 5824 7079 -743 260 -1054 C
ATOM 1484 C THR A 223 4.126 9.917 -27.719 1.00 45.76 C
ANISOU 1484 C THR A 223 5015 5593 6781 -805 90 -982 C
ATOM 1485 O THR A 223 3.360 10.682 -28.321 1.00 46.12 O
ANISOU 1485 O THR A 223 4914 5640 6967 -814 50 -870 O
ATOM 1486 CB THR A 223 4.280 11.385 -25.665 1.00 37.29 C
ANISOU 1486 CB THR A 223 3945 4415 5810 -667 375 -1058 C
ATOM 1487 OG1 THR A 223 5.337 12.084 -26.333 1.00 39.36 O
ANISOU 1487 OG1 THR A 223 4244 4711 6000 -668 307 -1090 O
ATOM 1488 CG2 THR A 223 4.566 11.377 -24.163 1.00 45.07 C
ANISOU 1488 CG2 THR A 223 5059 5328 6737 -617 522 -1153 C
ATOM 1489 N TYR A 224 4.922 9.065 -28.369 1.00 43.03 N
ANISOU 1489 N TYR A 224 4819 5277 6253 -829 2 -1030 N
ATOM 1490 CA TYR A 224 4.785 8.899 -29.812 1.00 35.67 C
ANISOU 1490 CA TYR A 224 3924 4360 5268 -894 -153 -961 C
ATOM 1491 C TYR A 224 4.845 7.424 -30.176 1.00 33.45 C
ANISOU 1491 C TYR A 224 3852 4050 4806 -964 -225 -988 C
ATOM 1492 O TYR A 224 3.860 6.851 -30.655 1.00 56.21 O
ANISOU 1492 O TYR A 224 6746 6907 7706 -1101 -349 -919 O
ATOM 1493 CB TYR A 224 5.864 9.667 -30.572 1.00 42.10 C
ANISOU 1493 CB TYR A 224 4777 5205 6013 -827 -157 -972 C
ATOM 1494 CG TYR A 224 5.706 9.570 -32.080 1.00 47.13 C
ANISOU 1494 CG TYR A 224 5496 5835 6575 -880 -302 -898 C
ATOM 1495 CD1 TYR A 224 5.006 10.537 -32.794 1.00 52.70 C
ANISOU 1495 CD1 TYR A 224 6077 6542 7406 -905 -384 -794 C
ATOM 1496 CD2 TYR A 224 6.249 8.505 -32.786 1.00 44.83 C
ANISOU 1496 CD2 TYR A 224 5446 5520 6067 -889 -349 -922 C
ATOM 1497 CE1 TYR A 224 4.861 10.448 -34.166 1.00 45.27 C
ANISOU 1497 CE1 TYR A 224 5244 5588 6371 -959 -535 -723 C
ATOM 1498 CE2 TYR A 224 6.109 8.407 -34.149 1.00 34.23 C
ANISOU 1498 CE2 TYR A 224 4246 4142 4618 -940 -477 -859 C
ATOM 1499 CZ TYR A 224 5.413 9.382 -34.840 1.00 34.55 C
ANISOU 1499 CZ TYR A 224 4156 4193 4780 -985 -585 -762 C
ATOM 1500 OH TYR A 224 5.279 9.276 -36.209 1.00 38.83 O
ANISOU 1500 OH TYR A 224 4874 4692 5188 -1041 -732 -696 O
ATOM 1501 N LEU A 225 5.989 6.793 -29.925 1.00 26.40 N
ANISOU 1501 N LEU A 225 3134 3161 3737 -874 -150 -1074 N
ATOM 1502 CA LEU A 225 6.200 5.455 -30.457 1.00 27.77 C
ANISOU 1502 CA LEU A 225 3579 3277 3696 -902 -191 -1093 C
ATOM 1503 C LEU A 225 5.362 4.417 -29.716 1.00 38.47 C
ANISOU 1503 C LEU A 225 5001 4568 5048 -1001 -186 -1110 C
ATOM 1504 O LEU A 225 4.640 3.627 -30.340 1.00 44.11 O
ANISOU 1504 O LEU A 225 5857 5210 5691 -1156 -305 -1072 O
ATOM 1505 CB LEU A 225 7.683 5.098 -30.382 1.00 26.45 C
ANISOU 1505 CB LEU A 225 3557 3142 3353 -732 -78 -1144 C
ATOM 1506 CG LEU A 225 7.971 3.875 -31.249 1.00 32.97 C
ANISOU 1506 CG LEU A 225 4720 3878 3929 -719 -93 -1139 C
ATOM 1507 CD1 LEU A 225 8.088 4.259 -32.721 1.00 36.89 C
ANISOU 1507 CD1 LEU A 225 5315 4349 4353 -740 -176 -1078 C
ATOM 1508 CD2 LEU A 225 9.195 3.108 -30.762 1.00 31.36 C
ANISOU 1508 CD2 LEU A 225 4666 3694 3557 -524 63 -1171 C
ATOM 1509 N ALA A 226 5.411 4.418 -28.383 1.00 48.52 N
ANISOU 1509 N ALA A 226 6193 5853 6389 -937 -56 -1161 N
ATOM 1510 CA ALA A 226 4.648 3.413 -27.644 1.00 45.98 C
ANISOU 1510 CA ALA A 226 5949 5460 6060 -1024 -21 -1172 C
ATOM 1511 C ALA A 226 3.152 3.548 -27.879 1.00 49.92 C
ANISOU 1511 C ALA A 226 6273 5948 6747 -1216 -120 -1064 C
ATOM 1512 O ALA A 226 2.503 2.539 -28.207 1.00 45.62 O
ANISOU 1512 O ALA A 226 5861 5336 6134 -1386 -210 -1032 O
ATOM 1513 CB ALA A 226 4.971 3.510 -26.147 1.00 27.32 C
ANISOU 1513 CB ALA A 226 3545 3107 3730 -906 145 -1239 C
ATOM 1514 N PRO A 227 2.547 4.733 -27.725 1.00 40.56 N
ANISOU 1514 N PRO A 227 4794 4822 5793 -1202 -107 -989 N
ATOM 1515 CA PRO A 227 1.117 4.879 -28.072 1.00 39.96 C
ANISOU 1515 CA PRO A 227 4499 4768 5917 -1365 -211 -835 C
ATOM 1516 C PRO A 227 0.780 4.566 -29.510 1.00 43.47 C
ANISOU 1516 C PRO A 227 5014 5217 6286 -1537 -461 -758 C
ATOM 1517 O PRO A 227 -0.215 3.878 -29.779 1.00 51.08 O
ANISOU 1517 O PRO A 227 5953 6165 7289 -1729 -596 -652 O
ATOM 1518 CB PRO A 227 0.830 6.352 -27.753 1.00 47.42 C
ANISOU 1518 CB PRO A 227 5165 5767 7083 -1240 -117 -768 C
ATOM 1519 CG PRO A 227 1.835 6.746 -26.753 1.00 49.38 C
ANISOU 1519 CG PRO A 227 5509 5989 7265 -1063 68 -902 C
ATOM 1520 CD PRO A 227 3.079 5.921 -27.025 1.00 48.81 C
ANISOU 1520 CD PRO A 227 5711 5905 6932 -1036 29 -1027 C
ATOM 1521 N LEU A 228 1.577 5.073 -30.452 1.00 40.21 N
ANISOU 1521 N LEU A 228 4699 4817 5760 -1462 -531 -789 N
ATOM 1522 CA LEU A 228 1.212 4.881 -31.847 1.00 35.53 C
ANISOU 1522 CA LEU A 228 4205 4213 5082 -1608 -769 -706 C
ATOM 1523 C LEU A 228 1.388 3.431 -32.265 1.00 44.33 C
ANISOU 1523 C LEU A 228 5681 5223 5940 -1668 -823 -749 C
ATOM 1524 O LEU A 228 0.556 2.894 -33.004 1.00 41.74 O
ANISOU 1524 O LEU A 228 5407 4881 5573 -1810 -982 -656 O
ATOM 1525 CB LEU A 228 2.005 5.817 -32.736 1.00 26.68 C
ANISOU 1525 CB LEU A 228 3117 3118 3900 -1492 -795 -717 C
ATOM 1526 CG LEU A 228 1.676 7.301 -32.574 1.00 35.50 C
ANISOU 1526 CG LEU A 228 3905 4319 5265 -1388 -746 -634 C
ATOM 1527 CD1 LEU A 228 2.445 8.065 -33.624 1.00 37.42 C
ANISOU 1527 CD1 LEU A 228 4240 4565 5414 -1302 -788 -637 C
ATOM 1528 CD2 LEU A 228 0.174 7.594 -32.656 1.00 45.50 C
ANISOU 1528 CD2 LEU A 228 4877 5647 6766 -1515 -873 -448 C
ATOM 1529 N GLY A 229 2.460 2.783 -31.810 1.00 56.36 N
ANISOU 1529 N GLY A 229 7464 6680 7270 -1554 -676 -879 N
ATOM 1530 CA GLY A 229 2.644 1.380 -32.142 1.00 47.20 C
ANISOU 1530 CA GLY A 229 6669 5407 5859 -1580 -684 -902 C
ATOM 1531 C GLY A 229 1.572 0.492 -31.537 1.00 46.10 C
ANISOU 1531 C GLY A 229 6501 5231 5784 -1739 -711 -850 C
ATOM 1532 O GLY A 229 1.097 -0.450 -32.177 1.00 55.40 O
ANISOU 1532 O GLY A 229 7892 6336 6820 -1871 -818 -797 O
ATOM 1533 N LEU A 230 1.181 0.777 -30.291 1.00 44.83 N
ANISOU 1533 N LEU A 230 6096 5111 5825 -1740 -601 -858 N
ATOM 1534 CA LEU A 230 0.099 0.034 -29.652 1.00 43.34 C
ANISOU 1534 CA LEU A 230 5839 4892 5736 -1903 -605 -791 C
ATOM 1535 C LEU A 230 -1.234 0.310 -30.335 1.00 51.96 C
ANISOU 1535 C LEU A 230 6674 6055 7011 -2089 -797 -626 C
ATOM 1536 O LEU A 230 -1.999 -0.619 -30.620 1.00 59.20 O
ANISOU 1536 O LEU A 230 7687 6933 7874 -2267 -899 -558 O
ATOM 1537 CB LEU A 230 0.022 0.388 -28.167 1.00 49.70 C
ANISOU 1537 CB LEU A 230 6451 5723 6708 -1845 -398 -830 C
ATOM 1538 CG LEU A 230 1.040 -0.280 -27.251 1.00 36.94 C
ANISOU 1538 CG LEU A 230 5106 4031 4899 -1688 -193 -983 C
ATOM 1539 CD1 LEU A 230 1.214 0.477 -25.933 1.00 40.80 C
ANISOU 1539 CD1 LEU A 230 5393 4565 5545 -1552 25 -1050 C
ATOM 1540 CD2 LEU A 230 0.592 -1.704 -26.994 1.00 29.75 C
ANISOU 1540 CD2 LEU A 230 4436 3008 3861 -1806 -187 -965 C
ATOM 1541 N MET A 231 -1.541 1.588 -30.582 1.00 56.98 N
ANISOU 1541 N MET A 231 6984 6808 7857 -2045 -835 -552 N
ATOM 1542 CA MET A 231 -2.787 1.923 -31.265 1.00 53.35 C
ANISOU 1542 CA MET A 231 6271 6451 7547 -2181 -998 -380 C
ATOM 1543 C MET A 231 -2.835 1.270 -32.638 1.00 53.89 C
ANISOU 1543 C MET A 231 6629 6473 7372 -2303 -1223 -350 C
ATOM 1544 O MET A 231 -3.905 0.860 -33.101 1.00 72.12 O
ANISOU 1544 O MET A 231 8874 8818 9711 -2491 -1388 -217 O
ATOM 1545 CB MET A 231 -2.950 3.441 -31.391 1.00 56.50 C
ANISOU 1545 CB MET A 231 6339 6982 8148 -2065 -978 -302 C
ATOM 1546 CG MET A 231 -3.208 4.145 -30.085 1.00 63.09 C
ANISOU 1546 CG MET A 231 6873 7875 9222 -1971 -749 -271 C
ATOM 1547 SD MET A 231 -3.375 5.937 -30.264 1.00 73.23 S
ANISOU 1547 SD MET A 231 7837 9286 10699 -1787 -706 -141 S
ATOM 1548 CE MET A 231 -1.808 6.507 -29.635 1.00 63.62 C
ANISOU 1548 CE MET A 231 6779 7968 9427 -1587 -530 -339 C
ATOM 1549 N ALA A 232 -1.682 1.170 -33.308 1.00 44.60 N
ANISOU 1549 N ALA A 232 5784 5216 5945 -2201 -1225 -458 N
ATOM 1550 CA ALA A 232 -1.641 0.535 -34.622 1.00 44.05 C
ANISOU 1550 CA ALA A 232 6056 5071 5610 -2307 -1404 -425 C
ATOM 1551 C ALA A 232 -1.981 -0.948 -34.520 1.00 58.18 C
ANISOU 1551 C ALA A 232 8136 6746 7225 -2468 -1430 -423 C
ATOM 1552 O ALA A 232 -2.805 -1.461 -35.285 1.00 73.24 O
ANISOU 1552 O ALA A 232 10138 8636 9052 -2679 -1632 -311 O
ATOM 1553 CB ALA A 232 -0.274 0.744 -35.273 1.00 38.22 C
ANISOU 1553 CB ALA A 232 5617 4259 4645 -2135 -1339 -529 C
ATOM 1554 N MET A 233 -1.352 -1.657 -33.580 1.00 59.38 N
ANISOU 1554 N MET A 233 8451 6813 7298 -2380 -1235 -537 N
ATOM 1555 CA MET A 233 -1.700 -3.059 -33.389 1.00 57.13 C
ANISOU 1555 CA MET A 233 8447 6412 6849 -2531 -1238 -529 C
ATOM 1556 C MET A 233 -3.164 -3.215 -32.997 1.00 58.58 C
ANISOU 1556 C MET A 233 8329 6669 7260 -2767 -1351 -402 C
ATOM 1557 O MET A 233 -3.788 -4.238 -33.322 1.00 50.46 O
ANISOU 1557 O MET A 233 7506 5568 6098 -2986 -1469 -338 O
ATOM 1558 CB MET A 233 -0.805 -3.687 -32.324 1.00 53.36 C
ANISOU 1558 CB MET A 233 8157 5846 6271 -2368 -989 -659 C
ATOM 1559 CG MET A 233 0.681 -3.702 -32.640 1.00 55.98 C
ANISOU 1559 CG MET A 233 8783 6112 6373 -2114 -846 -759 C
ATOM 1560 SD MET A 233 1.629 -4.577 -31.388 1.00 67.60 S
ANISOU 1560 SD MET A 233 10469 7500 7718 -1912 -565 -867 S
ATOM 1561 CE MET A 233 1.422 -3.491 -29.987 1.00 74.97 C
ANISOU 1561 CE MET A 233 10937 8566 8983 -1847 -469 -919 C
ATOM 1562 N ALA A 234 -3.720 -2.232 -32.280 1.00 62.99 N
ANISOU 1562 N ALA A 234 8411 7366 8158 -2726 -1299 -350 N
ATOM 1563 CA ALA A 234 -5.139 -2.284 -31.946 1.00 61.11 C
ANISOU 1563 CA ALA A 234 7834 7219 8164 -2922 -1377 -194 C
ATOM 1564 C ALA A 234 -5.996 -2.187 -33.202 1.00 67.43 C
ANISOU 1564 C ALA A 234 8592 8093 8937 -3110 -1665 -36 C
ATOM 1565 O ALA A 234 -6.942 -2.962 -33.388 1.00 79.32 O
ANISOU 1565 O ALA A 234 10113 9595 10430 -3358 -1811 77 O
ATOM 1566 CB ALA A 234 -5.496 -1.165 -30.972 1.00 53.79 C
ANISOU 1566 CB ALA A 234 6429 6421 7590 -2795 -1213 -148 C
ATOM 1567 N TYR A 235 -5.687 -1.228 -34.075 1.00 63.00 N
ANISOU 1567 N TYR A 235 7982 7595 8359 -3007 -1761 -13 N
ATOM 1568 CA TYR A 235 -6.545 -1.002 -35.230 1.00 75.75 C
ANISOU 1568 CA TYR A 235 9529 9288 9965 -3176 -2045 162 C
ATOM 1569 C TYR A 235 -6.400 -2.090 -36.287 1.00 77.97 C
ANISOU 1569 C TYR A 235 10314 9421 9890 -3368 -2236 160 C
ATOM 1570 O TYR A 235 -7.346 -2.336 -37.046 1.00 87.05 O
ANISOU 1570 O TYR A 235 11455 10607 11013 -3607 -2495 324 O
ATOM 1571 CB TYR A 235 -6.261 0.371 -35.828 1.00 79.02 C
ANISOU 1571 CB TYR A 235 9761 9800 10462 -3006 -2082 197 C
ATOM 1572 CG TYR A 235 -6.885 1.506 -35.049 1.00 80.78 C
ANISOU 1572 CG TYR A 235 9453 10194 11046 -2882 -1968 298 C
ATOM 1573 CD1 TYR A 235 -8.256 1.702 -35.058 1.00 79.39 C
ANISOU 1573 CD1 TYR A 235 8916 10162 11086 -3011 -2091 524 C
ATOM 1574 CD2 TYR A 235 -6.097 2.393 -34.320 1.00 80.25 C
ANISOU 1574 CD2 TYR A 235 9260 10143 11090 -2633 -1730 188 C
ATOM 1575 CE1 TYR A 235 -8.832 2.740 -34.361 1.00 78.65 C
ANISOU 1575 CE1 TYR A 235 8366 10216 11303 -2862 -1951 645 C
ATOM 1576 CE2 TYR A 235 -6.664 3.436 -33.619 1.00 81.85 C
ANISOU 1576 CE2 TYR A 235 9029 10481 11588 -2508 -1600 297 C
ATOM 1577 CZ TYR A 235 -8.030 3.604 -33.643 1.00 83.03 C
ANISOU 1577 CZ TYR A 235 8843 10765 11941 -2605 -1697 528 C
ATOM 1578 OH TYR A 235 -8.600 4.642 -32.947 1.00 90.93 O
ANISOU 1578 OH TYR A 235 9440 11889 13221 -2440 -1534 664 O
ATOM 1579 N PHE A 236 -5.236 -2.741 -36.364 1.00 73.92 N
ANISOU 1579 N PHE A 236 10256 8737 9092 -3265 -2107 -3 N
ATOM 1580 CA PHE A 236 -5.107 -3.899 -37.243 1.00 79.65 C
ANISOU 1580 CA PHE A 236 11517 9289 9458 -3438 -2233 4 C
ATOM 1581 C PHE A 236 -6.016 -5.030 -36.793 1.00 82.90 C
ANISOU 1581 C PHE A 236 11978 9661 9857 -3704 -2301 70 C
ATOM 1582 O PHE A 236 -6.600 -5.737 -37.623 1.00 97.22 O
ANISOU 1582 O PHE A 236 14052 11404 11482 -3969 -2528 177 O
ATOM 1583 CB PHE A 236 -3.660 -4.374 -37.290 1.00 82.38 C
ANISOU 1583 CB PHE A 236 12320 9462 9518 -3229 -2021 -160 C
ATOM 1584 CG PHE A 236 -3.509 -5.788 -37.774 1.00 93.81 C
ANISOU 1584 CG PHE A 236 14340 10699 10604 -3376 -2047 -158 C
ATOM 1585 CD1 PHE A 236 -3.619 -6.078 -39.125 1.00 99.42 C
ANISOU 1585 CD1 PHE A 236 15424 11296 11054 -3527 -2247 -69 C
ATOM 1586 CD2 PHE A 236 -3.240 -6.820 -36.887 1.00100.97 C
ANISOU 1586 CD2 PHE A 236 15446 11503 11415 -3361 -1863 -236 C
ATOM 1587 CE1 PHE A 236 -3.482 -7.371 -39.589 1.00107.98 C
ANISOU 1587 CE1 PHE A 236 17081 12158 11787 -3667 -2257 -53 C
ATOM 1588 CE2 PHE A 236 -3.095 -8.124 -37.342 1.00108.30 C
ANISOU 1588 CE2 PHE A 236 16936 12221 11993 -3488 -1868 -220 C
ATOM 1589 CZ PHE A 236 -3.213 -8.399 -38.698 1.00111.93 C
ANISOU 1589 CZ PHE A 236 17777 12558 12192 -3644 -2062 -127 C
ATOM 1590 N GLN A 237 -6.141 -5.226 -35.479 1.00 68.32 N
ANISOU 1590 N GLN A 237 9909 7847 8202 -3653 -2107 14 N
ATOM 1591 CA GLN A 237 -7.056 -6.245 -34.984 1.00 77.72 C
ANISOU 1591 CA GLN A 237 11109 9007 9414 -3914 -2158 85 C
ATOM 1592 C GLN A 237 -8.496 -5.905 -35.341 1.00 85.14 C
ANISOU 1592 C GLN A 237 11657 10110 10580 -4163 -2414 303 C
ATOM 1593 O GLN A 237 -9.318 -6.807 -35.541 1.00101.37 O
ANISOU 1593 O GLN A 237 13826 12130 12559 -4467 -2583 408 O
ATOM 1594 CB GLN A 237 -6.896 -6.408 -33.473 1.00 82.73 C
ANISOU 1594 CB GLN A 237 11566 9638 10231 -3792 -1880 -9 C
ATOM 1595 CG GLN A 237 -5.752 -7.315 -33.069 1.00 82.83 C
ANISOU 1595 CG GLN A 237 12064 9459 9950 -3655 -1669 -178 C
ATOM 1596 CD GLN A 237 -5.884 -7.833 -31.647 1.00 83.00 C
ANISOU 1596 CD GLN A 237 11996 9444 10096 -3643 -1453 -229 C
ATOM 1597 OE1 GLN A 237 -6.679 -7.323 -30.854 1.00 87.25 O
ANISOU 1597 OE1 GLN A 237 12071 10100 10979 -3683 -1409 -155 O
ATOM 1598 NE2 GLN A 237 -5.105 -8.858 -31.318 1.00 75.43 N
ANISOU 1598 NE2 GLN A 237 11498 8313 8849 -3575 -1295 -339 N
ATOM 1599 N ILE A 238 -8.820 -4.612 -35.405 1.00 81.00 N
ANISOU 1599 N ILE A 238 10673 9769 10333 -4039 -2441 388 N
ATOM 1600 CA ILE A 238 -10.162 -4.200 -35.793 1.00 90.95 C
ANISOU 1600 CA ILE A 238 11542 11206 11810 -4237 -2678 628 C
ATOM 1601 C ILE A 238 -10.402 -4.419 -37.283 1.00 98.86 C
ANISOU 1601 C ILE A 238 12836 12167 12559 -4449 -3016 739 C
ATOM 1602 O ILE A 238 -11.490 -4.849 -37.687 1.00107.50 O
ANISOU 1602 O ILE A 238 13852 13318 13674 -4753 -3271 929 O
ATOM 1603 CB ILE A 238 -10.400 -2.735 -35.386 1.00 89.38 C
ANISOU 1603 CB ILE A 238 10798 11204 11960 -4004 -2571 701 C
ATOM 1604 CG1 ILE A 238 -10.328 -2.588 -33.865 1.00 76.32 C
ANISOU 1604 CG1 ILE A 238 8871 9574 10554 -3841 -2239 624 C
ATOM 1605 CG2 ILE A 238 -11.740 -2.257 -35.896 1.00 98.43 C
ANISOU 1605 CG2 ILE A 238 11548 12540 13309 -4170 -2817 981 C
ATOM 1606 CD1 ILE A 238 -9.930 -1.199 -33.409 1.00 60.60 C
ANISOU 1606 CD1 ILE A 238 6563 7686 8774 -3528 -2042 597 C
ATOM 1607 N PHE A 239 -9.411 -4.114 -38.126 1.00 98.45 N
ANISOU 1607 N PHE A 239 13126 12015 12267 -4304 -3027 638 N
ATOM 1608 CA PHE A 239 -9.611 -4.278 -39.565 1.00101.97 C
ANISOU 1608 CA PHE A 239 13886 12395 12461 -4501 -3335 749 C
ATOM 1609 C PHE A 239 -9.841 -5.738 -39.931 1.00103.27 C
ANISOU 1609 C PHE A 239 14544 12380 12313 -4813 -3474 768 C
ATOM 1610 O PHE A 239 -10.703 -6.050 -40.764 1.00116.54 O
ANISOU 1610 O PHE A 239 16304 14068 13908 -5123 -3792 948 O
ATOM 1611 CB PHE A 239 -8.426 -3.714 -40.344 1.00 99.81 C
ANISOU 1611 CB PHE A 239 13918 12020 11984 -4271 -3271 631 C
ATOM 1612 CG PHE A 239 -8.446 -4.066 -41.804 1.00100.67 C
ANISOU 1612 CG PHE A 239 14490 11991 11770 -4466 -3539 716 C
ATOM 1613 CD1 PHE A 239 -9.130 -3.267 -42.713 1.00109.17 C
ANISOU 1613 CD1 PHE A 239 15372 13179 12930 -4565 -3814 898 C
ATOM 1614 CD2 PHE A 239 -7.793 -5.198 -42.267 1.00 94.77 C
ANISOU 1614 CD2 PHE A 239 14393 10987 10627 -4547 -3508 629 C
ATOM 1615 CE1 PHE A 239 -9.158 -3.589 -44.058 1.00114.24 C
ANISOU 1615 CE1 PHE A 239 16468 13672 13267 -4759 -4069 981 C
ATOM 1616 CE2 PHE A 239 -7.817 -5.527 -43.607 1.00 99.55 C
ANISOU 1616 CE2 PHE A 239 15470 11432 10923 -4730 -3739 716 C
ATOM 1617 CZ PHE A 239 -8.500 -4.721 -44.506 1.00109.70 C
ANISOU 1617 CZ PHE A 239 16564 12822 12294 -4846 -4028 887 C
ATOM 1618 N ARG A 240 -9.080 -6.650 -39.321 1.00 92.00 N
ANISOU 1618 N ARG A 240 13470 10783 10701 -4742 -3243 594 N
ATOM 1619 CA ARG A 240 -9.266 -8.065 -39.620 1.00 92.92 C
ANISOU 1619 CA ARG A 240 14100 10709 10496 -5028 -3345 612 C
ATOM 1620 C ARG A 240 -10.633 -8.552 -39.165 1.00108.06 C
ANISOU 1620 C ARG A 240 15717 12738 12603 -5359 -3517 773 C
ATOM 1621 O ARG A 240 -11.183 -9.490 -39.754 1.00126.74 O
ANISOU 1621 O ARG A 240 18421 14997 14737 -5703 -3748 875 O
ATOM 1622 CB ARG A 240 -8.167 -8.890 -38.955 1.00 84.87 C
ANISOU 1622 CB ARG A 240 13488 9498 9261 -4845 -3028 409 C
ATOM 1623 CG ARG A 240 -6.866 -8.947 -39.720 1.00 90.81 C
ANISOU 1623 CG ARG A 240 14764 10058 9680 -4629 -2905 300 C
ATOM 1624 CD ARG A 240 -5.905 -9.924 -39.058 1.00101.99 C
ANISOU 1624 CD ARG A 240 16593 11286 10871 -4472 -2600 149 C
ATOM 1625 NE ARG A 240 -6.368 -11.306 -39.114 1.00119.51 N
ANISOU 1625 NE ARG A 240 19246 13335 12826 -4765 -2676 200 N
ATOM 1626 CZ ARG A 240 -6.075 -12.155 -40.092 1.00132.94 C
ANISOU 1626 CZ ARG A 240 21607 14792 14113 -4892 -2743 241 C
ATOM 1627 NH1 ARG A 240 -5.319 -11.762 -41.107 1.00135.80 N
ANISOU 1627 NH1 ARG A 240 22258 15046 14293 -4741 -2735 240 N
ATOM 1628 NH2 ARG A 240 -6.540 -13.397 -40.059 1.00139.36 N
ANISOU 1628 NH2 ARG A 240 22813 15451 14687 -5175 -2808 289 N
ATOM 1629 N LYS A 241 -11.195 -7.931 -38.126 1.00 96.57 N
ANISOU 1629 N LYS A 241 13644 11486 11563 -5268 -3401 810 N
ATOM 1630 CA LYS A 241 -12.530 -8.306 -37.679 1.00 90.17 C
ANISOU 1630 CA LYS A 241 12484 10799 10977 -5566 -3542 991 C
ATOM 1631 C LYS A 241 -13.595 -7.737 -38.613 1.00 92.79 C
ANISOU 1631 C LYS A 241 12527 11301 11426 -5784 -3904 1255 C
ATOM 1632 O LYS A 241 -14.402 -8.482 -39.180 1.00 98.28 O
ANISOU 1632 O LYS A 241 13376 11973 11994 -6165 -4196 1413 O
ATOM 1633 CB LYS A 241 -12.749 -7.833 -36.241 1.00 80.45 C
ANISOU 1633 CB LYS A 241 10715 9706 10148 -5373 -3253 960 C
ATOM 1634 CG LYS A 241 -13.849 -8.581 -35.507 1.00 86.02 C
ANISOU 1634 CG LYS A 241 11191 10461 11032 -5655 -3278 1087 C
ATOM 1635 CD LYS A 241 -13.308 -9.913 -34.993 1.00 95.31 C
ANISOU 1635 CD LYS A 241 12875 11400 11938 -5738 -3128 919 C
ATOM 1636 CE LYS A 241 -14.238 -10.584 -33.998 1.00108.32 C
ANISOU 1636 CE LYS A 241 14271 13081 13806 -5956 -3057 1006 C
ATOM 1637 NZ LYS A 241 -13.522 -11.676 -33.281 1.00111.97 N
ANISOU 1637 NZ LYS A 241 15194 13311 14039 -5930 -2822 812 N
ATOM 1638 N LEU A 242 -13.612 -6.407 -38.782 1.00 95.15 N
ANISOU 1638 N LEU A 242 12419 11773 11961 -5552 -3894 1316 N
ATOM 1639 CA LEU A 242 -14.651 -5.773 -39.590 1.00105.43 C
ANISOU 1639 CA LEU A 242 13393 13258 13407 -5723 -4221 1591 C
ATOM 1640 C LEU A 242 -14.539 -6.148 -41.062 1.00113.11 C
ANISOU 1640 C LEU A 242 14882 14091 14006 -5954 -4550 1649 C
ATOM 1641 O LEU A 242 -15.545 -6.139 -41.781 1.00120.99 O
ANISOU 1641 O LEU A 242 15750 15187 15033 -6248 -4898 1899 O
ATOM 1642 CB LEU A 242 -14.582 -4.251 -39.449 1.00 99.22 C
ANISOU 1642 CB LEU A 242 12118 12659 12920 -5387 -4104 1635 C
ATOM 1643 CG LEU A 242 -14.721 -3.615 -38.064 1.00 84.22 C
ANISOU 1643 CG LEU A 242 9690 10903 11406 -5123 -3769 1611 C
ATOM 1644 CD1 LEU A 242 -14.717 -2.092 -38.166 1.00 85.90 C
ANISOU 1644 CD1 LEU A 242 9498 11284 11857 -4826 -3706 1694 C
ATOM 1645 CD2 LEU A 242 -15.983 -4.102 -37.374 1.00 86.80 C
ANISOU 1645 CD2 LEU A 242 9634 11361 11985 -5355 -3809 1811 C
ATOM 1646 N TRP A 243 -13.338 -6.454 -41.535 1.00107.16 N
ANISOU 1646 N TRP A 243 14710 13105 12901 -5824 -4445 1442 N
ATOM 1647 CA TRP A 243 -13.172 -6.775 -42.942 1.00106.20 C
ANISOU 1647 CA TRP A 243 15125 12815 12409 -6019 -4719 1497 C
ATOM 1648 C TRP A 243 -12.627 -8.182 -43.110 1.00105.83 C
ANISOU 1648 C TRP A 243 15794 12477 11939 -6184 -4680 1373 C
ATOM 1649 O TRP A 243 -11.651 -8.392 -43.832 1.00103.44 O
ANISOU 1649 O TRP A 243 16058 11950 11296 -6082 -4617 1257 O
ATOM 1650 CB TRP A 243 -12.262 -5.765 -43.641 1.00105.37 C
ANISOU 1650 CB TRP A 243 15123 12675 12237 -5719 -4652 1412 C
ATOM 1651 CG TRP A 243 -12.974 -4.515 -44.062 1.00115.38 C
ANISOU 1651 CG TRP A 243 15876 14176 13788 -5684 -4841 1609 C
ATOM 1652 CD1 TRP A 243 -13.733 -4.348 -45.181 1.00124.94 C
ANISOU 1652 CD1 TRP A 243 17120 15421 14932 -5946 -5223 1835 C
ATOM 1653 CD2 TRP A 243 -12.952 -3.243 -43.400 1.00112.00 C
ANISOU 1653 CD2 TRP A 243 14860 13963 13731 -5358 -4652 1608 C
ATOM 1654 NE1 TRP A 243 -14.209 -3.062 -45.245 1.00127.17 N
ANISOU 1654 NE1 TRP A 243 16849 15938 15531 -5793 -5281 1982 N
ATOM 1655 CE2 TRP A 243 -13.741 -2.361 -44.167 1.00117.19 C
ANISOU 1655 CE2 TRP A 243 15209 14782 14534 -5429 -4925 1847 C
ATOM 1656 CE3 TRP A 243 -12.352 -2.766 -42.230 1.00100.63 C
ANISOU 1656 CE3 TRP A 243 13146 12583 12505 -5022 -4280 1438 C
ATOM 1657 CZ2 TRP A 243 -13.944 -1.032 -43.802 1.00107.32 C
ANISOU 1657 CZ2 TRP A 243 13400 13749 13629 -5157 -4819 1924 C
ATOM 1658 CZ3 TRP A 243 -12.554 -1.445 -41.870 1.00 92.89 C
ANISOU 1658 CZ3 TRP A 243 11627 11807 11860 -4773 -4183 1510 C
ATOM 1659 CH2 TRP A 243 -13.344 -0.594 -42.653 1.00 94.10 C
ANISOU 1659 CH2 TRP A 243 11494 12116 12146 -4832 -4442 1753 C
ATOM 1660 N GLY A 249 -25.495 -15.819 -39.751 1.00175.60 N
ANISOU 1660 N GLY A 249 22188 22364 22169 -10759 -6885 3630 N
ATOM 1661 CA GLY A 249 -26.897 -15.498 -39.556 1.00182.18 C
ANISOU 1661 CA GLY A 249 22242 23532 23447 -11010 -7094 4018 C
ATOM 1662 C GLY A 249 -27.129 -14.317 -38.634 1.00179.62 C
ANISOU 1662 C GLY A 249 21082 23488 23678 -10547 -6749 4089 C
ATOM 1663 O GLY A 249 -28.060 -14.322 -37.831 1.00185.83 O
ANISOU 1663 O GLY A 249 21257 24478 24870 -10642 -6659 4301 O
ATOM 1664 N THR A 250 -26.264 -13.314 -38.741 1.00168.25 N
ANISOU 1664 N THR A 250 19643 22042 22244 -10045 -6537 3916 N
ATOM 1665 CA THR A 250 -26.360 -12.113 -37.925 1.00162.01 C
ANISOU 1665 CA THR A 250 18150 21483 21924 -9569 -6193 3963 C
ATOM 1666 C THR A 250 -27.495 -11.207 -38.400 1.00165.59 C
ANISOU 1666 C THR A 250 17919 22284 22713 -9638 -6473 4391 C
ATOM 1667 O THR A 250 -27.879 -11.208 -39.573 1.00170.23 O
ANISOU 1667 O THR A 250 18641 22915 23123 -9936 -6933 4589 O
ATOM 1668 CB THR A 250 -25.037 -11.352 -37.928 1.00155.12 C
ANISOU 1668 CB THR A 250 17541 20479 20919 -9041 -5898 3642 C
ATOM 1669 OG1 THR A 250 -25.107 -10.277 -36.984 1.00155.60 O
ANISOU 1669 OG1 THR A 250 16974 20732 21416 -8593 -5523 3669 O
ATOM 1670 CG2 THR A 250 -24.749 -10.800 -39.311 1.00152.63 C
ANISOU 1670 CG2 THR A 250 17488 20152 20351 -9044 -6232 3694 C
ATOM 1671 N THR A 251 -28.037 -10.439 -37.459 1.00165.51 N
ANISOU 1671 N THR A 251 17185 22514 23186 -9354 -6179 4547 N
ATOM 1672 CA THR A 251 -29.278 -9.706 -37.661 1.00173.73 C
ANISOU 1672 CA THR A 251 17492 23909 24610 -9422 -6382 5006 C
ATOM 1673 C THR A 251 -29.075 -8.543 -38.628 1.00178.42 C
ANISOU 1673 C THR A 251 18013 24607 25173 -9180 -6561 5099 C
ATOM 1674 O THR A 251 -27.963 -8.045 -38.825 1.00172.07 O
ANISOU 1674 O THR A 251 17568 23641 24170 -8829 -6389 4799 O
ATOM 1675 CB THR A 251 -29.798 -9.177 -36.322 1.00173.22 C
ANISOU 1675 CB THR A 251 16736 24038 25045 -9113 -5937 5131 C
ATOM 1676 OG1 THR A 251 -30.113 -10.278 -35.462 1.00178.74 O
ANISOU 1676 OG1 THR A 251 17467 24650 25796 -9385 -5791 5085 O
ATOM 1677 CG2 THR A 251 -31.041 -8.314 -36.507 1.00180.00 C
ANISOU 1677 CG2 THR A 251 16813 25269 26310 -9104 -6097 5632 C
ATOM 1678 N SER A 252 -30.181 -8.123 -39.248 1.00189.08 N
ANISOU 1678 N SER A 252 18885 26232 26725 -9386 -6918 5537 N
ATOM 1679 CA SER A 252 -30.141 -6.978 -40.151 1.00189.53 C
ANISOU 1679 CA SER A 252 18802 26412 26798 -9169 -7094 5680 C
ATOM 1680 C SER A 252 -29.637 -5.731 -39.437 1.00189.10 C
ANISOU 1680 C SER A 252 18424 26425 27001 -8525 -6617 5571 C
ATOM 1681 O SER A 252 -28.939 -4.903 -40.036 1.00184.97 O
ANISOU 1681 O SER A 252 18086 25847 26348 -8239 -6611 5447 O
ATOM 1682 CB SER A 252 -31.529 -6.730 -40.734 1.00192.95 C
ANISOU 1682 CB SER A 252 18671 27164 27478 -9478 -7511 6215 C
ATOM 1683 OG SER A 252 -31.583 -5.487 -41.406 1.00174.33 O
ANISOU 1683 OG SER A 252 16056 24959 25222 -9196 -7603 6387 O
ATOM 1684 N ALA A 253 -29.988 -5.572 -38.158 1.00192.23 N
ANISOU 1684 N ALA A 253 18352 26930 27758 -8298 -6207 5623 N
ATOM 1685 CA ALA A 253 -29.459 -4.446 -37.395 1.00185.86 C
ANISOU 1685 CA ALA A 253 17310 26148 27160 -7695 -5727 5500 C
ATOM 1686 C ALA A 253 -27.971 -4.611 -37.119 1.00176.11 C
ANISOU 1686 C ALA A 253 16696 24601 25616 -7451 -5443 4978 C
ATOM 1687 O ALA A 253 -27.242 -3.614 -37.044 1.00175.87 O
ANISOU 1687 O ALA A 253 16685 24540 25597 -7009 -5204 4827 O
ATOM 1688 CB ALA A 253 -30.235 -4.283 -36.087 1.00188.17 C
ANISOU 1688 CB ALA A 253 16989 26613 27893 -7527 -5348 5703 C
ATOM 1689 N GLU A 286 -27.502 -5.852 -36.967 1.00169.58 N
ANISOU 1689 N GLU A 286 16382 23541 24511 -7732 -5462 4714 N
ATOM 1690 CA GLU A 286 -26.095 -6.068 -36.651 1.00159.98 C
ANISOU 1690 CA GLU A 286 15738 22035 23012 -7496 -5179 4244 C
ATOM 1691 C GLU A 286 -25.200 -5.647 -37.808 1.00153.31 C
ANISOU 1691 C GLU A 286 15358 21063 21830 -7402 -5380 4080 C
ATOM 1692 O GLU A 286 -24.200 -4.947 -37.606 1.00144.34 O
ANISOU 1692 O GLU A 286 14366 19833 20642 -6993 -5102 3830 O
ATOM 1693 CB GLU A 286 -25.865 -7.525 -36.270 1.00164.80 C
ANISOU 1693 CB GLU A 286 16796 22423 23397 -7825 -5163 4039 C
ATOM 1694 CG GLU A 286 -26.648 -7.922 -35.030 1.00175.62 C
ANISOU 1694 CG GLU A 286 17727 23893 25109 -7888 -4900 4166 C
ATOM 1695 CD GLU A 286 -26.389 -6.974 -33.875 1.00177.32 C
ANISOU 1695 CD GLU A 286 17564 24175 25636 -7370 -4383 4099 C
ATOM 1696 OE1 GLU A 286 -25.210 -6.647 -33.622 1.00171.34 O
ANISOU 1696 OE1 GLU A 286 17139 23243 24720 -7034 -4121 3763 O
ATOM 1697 OE2 GLU A 286 -27.370 -6.548 -33.229 1.00183.49 O
ANISOU 1697 OE2 GLU A 286 17723 25183 26811 -7299 -4237 4399 O
ATOM 1698 N VAL A 287 -25.549 -6.055 -39.032 1.00152.85 N
ANISOU 1698 N VAL A 287 15545 20995 21535 -7788 -5861 4229 N
ATOM 1699 CA VAL A 287 -24.760 -5.626 -40.181 1.00143.04 C
ANISOU 1699 CA VAL A 287 14742 19630 19978 -7705 -6049 4103 C
ATOM 1700 C VAL A 287 -24.913 -4.124 -40.359 1.00138.02 C
ANISOU 1700 C VAL A 287 13631 19201 19610 -7330 -5981 4269 C
ATOM 1701 O VAL A 287 -24.004 -3.452 -40.857 1.00133.44 O
ANISOU 1701 O VAL A 287 13316 18518 18867 -7059 -5920 4084 O
ATOM 1702 CB VAL A 287 -25.173 -6.404 -41.448 1.00146.12 C
ANISOU 1702 CB VAL A 287 15519 19951 20048 -8225 -6583 4252 C
ATOM 1703 CG1 VAL A 287 -24.289 -6.019 -42.634 1.00139.93 C
ANISOU 1703 CG1 VAL A 287 15257 18999 18911 -8136 -6743 4103 C
ATOM 1704 CG2 VAL A 287 -25.111 -7.905 -41.194 1.00141.77 C
ANISOU 1704 CG2 VAL A 287 15431 19194 19241 -8605 -6632 4114 C
ATOM 1705 N LYS A 288 -26.049 -3.570 -39.928 1.00143.64 N
ANISOU 1705 N LYS A 288 13639 20200 20737 -7293 -5968 4628 N
ATOM 1706 CA LYS A 288 -26.181 -2.123 -39.850 1.00145.64 C
ANISOU 1706 CA LYS A 288 13424 20639 21274 -6868 -5802 4782 C
ATOM 1707 C LYS A 288 -25.221 -1.549 -38.821 1.00135.00 C
ANISOU 1707 C LYS A 288 12105 19188 20002 -6376 -5274 4473 C
ATOM 1708 O LYS A 288 -24.766 -0.407 -38.962 1.00123.76 O
ANISOU 1708 O LYS A 288 10597 17792 18636 -6001 -5130 4438 O
ATOM 1709 CB LYS A 288 -27.622 -1.751 -39.491 1.00152.00 C
ANISOU 1709 CB LYS A 288 13477 21765 22512 -6918 -5850 5253 C
ATOM 1710 CG LYS A 288 -27.985 -0.296 -39.683 1.00151.21 C
ANISOU 1710 CG LYS A 288 12895 21875 22682 -6550 -5782 5513 C
ATOM 1711 CD LYS A 288 -29.455 -0.086 -39.357 1.00152.99 C
ANISOU 1711 CD LYS A 288 12395 22416 23320 -6632 -5842 6015 C
ATOM 1712 CE LYS A 288 -29.910 1.331 -39.650 1.00151.07 C
ANISOU 1712 CE LYS A 288 11677 22386 23335 -6283 -5804 6327 C
ATOM 1713 NZ LYS A 288 -31.391 1.481 -39.555 1.00159.50 N
ANISOU 1713 NZ LYS A 288 12051 23774 24777 -6407 -5937 6872 N
ATOM 1714 N GLN A 289 -24.906 -2.328 -37.785 1.00133.36 N
ANISOU 1714 N GLN A 289 12027 18855 19787 -6386 -4991 4254 N
ATOM 1715 CA GLN A 289 -23.889 -1.914 -36.828 1.00122.99 C
ANISOU 1715 CA GLN A 289 10826 17411 18492 -5966 -4517 3933 C
ATOM 1716 C GLN A 289 -22.496 -2.044 -37.433 1.00121.54 C
ANISOU 1716 C GLN A 289 11297 16975 17910 -5891 -4537 3558 C
ATOM 1717 O GLN A 289 -21.638 -1.176 -37.228 1.00122.23 O
ANISOU 1717 O GLN A 289 11437 17010 17995 -5507 -4284 3375 O
ATOM 1718 CB GLN A 289 -24.024 -2.732 -35.544 1.00117.13 C
ANISOU 1718 CB GLN A 289 10022 16613 17869 -6019 -4216 3836 C
ATOM 1719 CG GLN A 289 -23.112 -2.297 -34.414 1.00110.40 C
ANISOU 1719 CG GLN A 289 9226 15646 17076 -5602 -3714 3551 C
ATOM 1720 CD GLN A 289 -23.230 -3.195 -33.198 1.00119.10 C
ANISOU 1720 CD GLN A 289 10320 16667 18265 -5690 -3432 3450 C
ATOM 1721 OE1 GLN A 289 -23.538 -4.379 -33.322 1.00130.19 O
ANISOU 1721 OE1 GLN A 289 11919 18001 19547 -6080 -3617 3448 O
ATOM 1722 NE2 GLN A 289 -22.985 -2.638 -32.016 1.00106.84 N
ANISOU 1722 NE2 GLN A 289 8571 15112 16911 -5335 -2979 3371 N
ATOM 1723 N MET A 290 -22.253 -3.125 -38.184 1.00118.61 N
ANISOU 1723 N MET A 290 11439 16437 17189 -6256 -4829 3452 N
ATOM 1724 CA MET A 290 -20.967 -3.289 -38.855 1.00115.23 C
ANISOU 1724 CA MET A 290 11653 15765 16365 -6189 -4854 3135 C
ATOM 1725 C MET A 290 -20.744 -2.183 -39.877 1.00119.43 C
ANISOU 1725 C MET A 290 12166 16357 16856 -6018 -5013 3213 C
ATOM 1726 O MET A 290 -19.622 -1.689 -40.039 1.00121.76 O
ANISOU 1726 O MET A 290 12747 16521 16995 -5739 -4850 2965 O
ATOM 1727 CB MET A 290 -20.900 -4.651 -39.546 1.00125.31 C
ANISOU 1727 CB MET A 290 13496 16851 17264 -6626 -5150 3071 C
ATOM 1728 CG MET A 290 -19.494 -5.112 -39.868 1.00128.44 C
ANISOU 1728 CG MET A 290 14597 16953 17250 -6530 -5048 2710 C
ATOM 1729 SD MET A 290 -19.463 -6.564 -40.930 1.00144.98 S
ANISOU 1729 SD MET A 290 17425 18810 18853 -7028 -5424 2691 S
ATOM 1730 CE MET A 290 -17.842 -7.215 -40.550 1.00141.76 C
ANISOU 1730 CE MET A 290 17691 18078 18094 -6795 -5076 2259 C
ATOM 1731 N ARG A 291 -21.806 -1.796 -40.592 1.00124.38 N
ANISOU 1731 N ARG A 291 12458 17181 17620 -6196 -5340 3568 N
ATOM 1732 CA ARG A 291 -21.672 -0.786 -41.633 1.00126.11 C
ANISOU 1732 CA ARG A 291 12669 17452 17793 -6068 -5521 3665 C
ATOM 1733 C ARG A 291 -21.276 0.549 -41.029 1.00129.70 C
ANISOU 1733 C ARG A 291 12788 17996 18497 -5566 -5163 3618 C
ATOM 1734 O ARG A 291 -20.534 1.321 -41.648 1.00131.84 O
ANISOU 1734 O ARG A 291 13246 18201 18644 -5355 -5156 3508 O
ATOM 1735 CB ARG A 291 -22.997 -0.650 -42.378 1.00129.65 C
ANISOU 1735 CB ARG A 291 12757 18119 18384 -6359 -5929 4091 C
ATOM 1736 CG ARG A 291 -23.435 -1.923 -43.072 1.00136.33 C
ANISOU 1736 CG ARG A 291 13958 18876 18966 -6897 -6331 4166 C
ATOM 1737 CD ARG A 291 -24.871 -1.826 -43.560 1.00149.71 C
ANISOU 1737 CD ARG A 291 15184 20828 20870 -7202 -6713 4625 C
ATOM 1738 NE ARG A 291 -25.342 -3.111 -44.070 1.00158.34 N
ANISOU 1738 NE ARG A 291 16603 21835 21723 -7752 -7087 4705 N
ATOM 1739 CZ ARG A 291 -25.527 -3.400 -45.354 1.00162.63 C
ANISOU 1739 CZ ARG A 291 17494 22312 21988 -8101 -7542 4822 C
ATOM 1740 NH1 ARG A 291 -25.272 -2.496 -46.289 1.00164.12 N
ANISOU 1740 NH1 ARG A 291 17743 22510 22105 -7954 -7681 4867 N
ATOM 1741 NH2 ARG A 291 -25.963 -4.603 -45.701 1.00165.77 N
ANISOU 1741 NH2 ARG A 291 18204 22616 22163 -8609 -7857 4895 N
ATOM 1742 N ALA A 292 -21.757 0.836 -39.818 1.00131.79 N
ANISOU 1742 N ALA A 292 12578 18395 19103 -5375 -4854 3706 N
ATOM 1743 CA ALA A 292 -21.381 2.075 -39.154 1.00127.95 C
ANISOU 1743 CA ALA A 292 11815 17966 18835 -4900 -4487 3663 C
ATOM 1744 C ALA A 292 -19.991 1.960 -38.546 1.00120.70 C
ANISOU 1744 C ALA A 292 11296 16826 17737 -4674 -4159 3242 C
ATOM 1745 O ALA A 292 -19.199 2.905 -38.618 1.00108.84 O
ANISOU 1745 O ALA A 292 9861 15280 16213 -4357 -3995 3110 O
ATOM 1746 CB ALA A 292 -22.414 2.441 -38.090 1.00130.52 C
ANISOU 1746 CB ALA A 292 11522 18495 19574 -4764 -4255 3934 C
ATOM 1747 N ARG A 293 -19.682 0.812 -37.937 1.00125.49 N
ANISOU 1747 N ARG A 293 12169 17294 18219 -4838 -4062 3040 N
ATOM 1748 CA ARG A 293 -18.364 0.636 -37.334 1.00115.92 C
ANISOU 1748 CA ARG A 293 11329 15877 16837 -4634 -3757 2658 C
ATOM 1749 C ARG A 293 -17.246 0.653 -38.375 1.00104.41 C
ANISOU 1749 C ARG A 293 10403 14246 15023 -4621 -3897 2441 C
ATOM 1750 O ARG A 293 -16.136 1.099 -38.065 1.00102.43 O
ANISOU 1750 O ARG A 293 10334 13888 14696 -4341 -3648 2193 O
ATOM 1751 CB ARG A 293 -18.339 -0.648 -36.505 1.00 90.30 C
ANISOU 1751 CB ARG A 293 8259 12519 13533 -4828 -3638 2517 C
ATOM 1752 CG ARG A 293 -19.031 -0.471 -35.157 1.00 91.01 C
ANISOU 1752 CG ARG A 293 7869 12732 13978 -4703 -3328 2634 C
ATOM 1753 CD ARG A 293 -19.340 -1.787 -34.459 1.00 92.80 C
ANISOU 1753 CD ARG A 293 8196 12880 14185 -4974 -3276 2582 C
ATOM 1754 NE ARG A 293 -19.477 -1.592 -33.018 1.00 91.20 N
ANISOU 1754 NE ARG A 293 7698 12708 14246 -4762 -2861 2562 N
ATOM 1755 CZ ARG A 293 -19.843 -2.537 -32.160 1.00 95.42 C
ANISOU 1755 CZ ARG A 293 8213 13195 14847 -4934 -2723 2547 C
ATOM 1756 NH1 ARG A 293 -20.133 -3.756 -32.592 1.00 99.46 N
ANISOU 1756 NH1 ARG A 293 8975 13628 15187 -5331 -2980 2551 N
ATOM 1757 NH2 ARG A 293 -19.929 -2.256 -30.867 1.00 99.64 N
ANISOU 1757 NH2 ARG A 293 8500 13748 15609 -4715 -2323 2535 N
ATOM 1758 N ARG A 294 -17.500 0.171 -39.600 1.00 96.80 N
ANISOU 1758 N ARG A 294 9706 13243 13829 -4922 -4285 2537 N
ATOM 1759 CA ARG A 294 -16.486 0.304 -40.646 1.00 89.18 C
ANISOU 1759 CA ARG A 294 9235 12113 12535 -4883 -4399 2366 C
ATOM 1760 C ARG A 294 -16.284 1.758 -41.054 1.00 90.79 C
ANISOU 1760 C ARG A 294 9214 12417 12866 -4587 -4365 2434 C
ATOM 1761 O ARG A 294 -15.144 2.200 -41.240 1.00 93.08 O
ANISOU 1761 O ARG A 294 9778 12584 13005 -4364 -4222 2212 O
ATOM 1762 CB ARG A 294 -16.841 -0.518 -41.884 1.00 93.33 C
ANISOU 1762 CB ARG A 294 10136 12554 12771 -5279 -4817 2471 C
ATOM 1763 CG ARG A 294 -16.732 -2.026 -41.757 1.00 94.73 C
ANISOU 1763 CG ARG A 294 10749 12552 12692 -5580 -4870 2352 C
ATOM 1764 CD ARG A 294 -17.509 -2.684 -42.899 1.00105.61 C
ANISOU 1764 CD ARG A 294 12346 13909 13872 -6017 -5326 2566 C
ATOM 1765 NE ARG A 294 -17.342 -4.136 -42.969 1.00117.78 N
ANISOU 1765 NE ARG A 294 14416 15240 15098 -6326 -5404 2457 N
ATOM 1766 CZ ARG A 294 -17.260 -4.808 -44.116 1.00127.03 C
ANISOU 1766 CZ ARG A 294 16139 16233 15895 -6622 -5707 2483 C
ATOM 1767 NH1 ARG A 294 -17.307 -4.151 -45.266 1.00125.89 N
ANISOU 1767 NH1 ARG A 294 16075 16098 15660 -6646 -5956 2601 N
ATOM 1768 NH2 ARG A 294 -17.100 -6.124 -44.122 1.00132.80 N
ANISOU 1768 NH2 ARG A 294 17375 16756 16326 -6886 -5748 2389 N
ATOM 1769 N LYS A 295 -17.375 2.524 -41.183 1.00 93.38 N
ANISOU 1769 N LYS A 295 9037 12969 13476 -4574 -4486 2755 N
ATOM 1770 CA LYS A 295 -17.228 3.927 -41.552 1.00 91.81 C
ANISOU 1770 CA LYS A 295 8623 12861 13401 -4283 -4443 2838 C
ATOM 1771 C LYS A 295 -16.494 4.701 -40.468 1.00 90.34 C
ANISOU 1771 C LYS A 295 8295 12658 13371 -3884 -4007 2660 C
ATOM 1772 O LYS A 295 -15.729 5.623 -40.773 1.00 90.53 O
ANISOU 1772 O LYS A 295 8406 12641 13351 -3639 -3916 2561 O
ATOM 1773 CB LYS A 295 -18.590 4.570 -41.828 1.00 99.63 C
ANISOU 1773 CB LYS A 295 9080 14099 14675 -4326 -4631 3246 C
ATOM 1774 CG LYS A 295 -19.176 4.292 -43.197 1.00105.72 C
ANISOU 1774 CG LYS A 295 9984 14899 15286 -4658 -5103 3449 C
ATOM 1775 CD LYS A 295 -20.294 5.279 -43.496 1.00113.88 C
ANISOU 1775 CD LYS A 295 10466 16187 16616 -4586 -5239 3842 C
ATOM 1776 CE LYS A 295 -20.948 5.038 -44.845 1.00125.97 C
ANISOU 1776 CE LYS A 295 12094 17765 18002 -4932 -5733 4072 C
ATOM 1777 NZ LYS A 295 -21.987 6.075 -45.117 1.00133.31 N
ANISOU 1777 NZ LYS A 295 12463 18955 19232 -4821 -5845 4464 N
ATOM 1778 N THR A 296 -16.693 4.330 -39.205 1.00 92.76 N
ANISOU 1778 N THR A 296 8409 12988 13849 -3828 -3738 2616 N
ATOM 1779 CA THR A 296 -15.905 4.929 -38.134 1.00 83.76 C
ANISOU 1779 CA THR A 296 7217 11797 12812 -3485 -3328 2419 C
ATOM 1780 C THR A 296 -14.495 4.350 -38.090 1.00 72.93 C
ANISOU 1780 C THR A 296 6366 10204 11140 -3470 -3221 2046 C
ATOM 1781 O THR A 296 -13.522 5.097 -37.958 1.00 68.74 O
ANISOU 1781 O THR A 296 5937 9608 10573 -3212 -3034 1879 O
ATOM 1782 CB THR A 296 -16.608 4.748 -36.789 1.00 96.30 C
ANISOU 1782 CB THR A 296 8442 13470 14677 -3426 -3063 2510 C
ATOM 1783 OG1 THR A 296 -17.995 5.072 -36.934 1.00115.61 O
ANISOU 1783 OG1 THR A 296 10422 16124 17381 -3489 -3197 2891 O
ATOM 1784 CG2 THR A 296 -15.989 5.660 -35.743 1.00 74.46 C
ANISOU 1784 CG2 THR A 296 5562 10676 12052 -3044 -2651 2387 C
ATOM 1785 N ALA A 297 -14.367 3.026 -38.209 1.00 73.76 N
ANISOU 1785 N ALA A 297 6809 10188 11026 -3743 -3337 1931 N
ATOM 1786 CA ALA A 297 -13.049 2.395 -38.218 1.00 69.74 C
ANISOU 1786 CA ALA A 297 6815 9464 10218 -3721 -3234 1608 C
ATOM 1787 C ALA A 297 -12.198 2.919 -39.370 1.00 73.58 C
ANISOU 1787 C ALA A 297 7618 9866 10475 -3645 -3363 1526 C
ATOM 1788 O ALA A 297 -11.009 3.209 -39.199 1.00 79.52 O
ANISOU 1788 O ALA A 297 8588 10509 11116 -3438 -3167 1300 O
ATOM 1789 CB ALA A 297 -13.193 0.877 -38.299 1.00 71.89 C
ANISOU 1789 CB ALA A 297 7420 9615 10278 -4038 -3364 1550 C
ATOM 1790 N LYS A 298 -12.787 3.025 -40.561 1.00 79.11 N
ANISOU 1790 N LYS A 298 8355 10609 11096 -3823 -3697 1717 N
ATOM 1791 CA LYS A 298 -12.067 3.585 -41.700 1.00 78.18 C
ANISOU 1791 CA LYS A 298 8526 10408 10771 -3755 -3824 1666 C
ATOM 1792 C LYS A 298 -11.606 5.008 -41.401 1.00 79.87 C
ANISOU 1792 C LYS A 298 8474 10701 11174 -3409 -3617 1645 C
ATOM 1793 O LYS A 298 -10.450 5.367 -41.658 1.00 77.23 O
ANISOU 1793 O LYS A 298 8412 10251 10681 -3248 -3509 1454 O
ATOM 1794 CB LYS A 298 -12.959 3.527 -42.940 1.00 85.06 C
ANISOU 1794 CB LYS A 298 9422 11330 11566 -4016 -4225 1914 C
ATOM 1795 CG LYS A 298 -12.314 3.953 -44.245 1.00 89.55 C
ANISOU 1795 CG LYS A 298 10355 11787 11882 -4002 -4396 1877 C
ATOM 1796 CD LYS A 298 -13.357 3.995 -45.360 1.00101.49 C
ANISOU 1796 CD LYS A 298 11816 13376 13368 -4263 -4801 2158 C
ATOM 1797 CE LYS A 298 -12.755 4.406 -46.697 1.00107.94 C
ANISOU 1797 CE LYS A 298 13028 14064 13922 -4260 -4978 2127 C
ATOM 1798 NZ LYS A 298 -13.807 4.523 -47.752 1.00117.15 N
ANISOU 1798 NZ LYS A 298 14120 15314 15079 -4512 -5383 2413 N
ATOM 1799 N MET A 299 -12.511 5.838 -40.870 1.00 83.02 N
ANISOU 1799 N MET A 299 8346 11290 11907 -3289 -3554 1860 N
ATOM 1800 CA MET A 299 -12.176 7.229 -40.575 1.00 78.77 C
ANISOU 1800 CA MET A 299 7559 10817 11554 -2960 -3353 1875 C
ATOM 1801 C MET A 299 -11.100 7.340 -39.498 1.00 91.12 C
ANISOU 1801 C MET A 299 9209 12286 13125 -2740 -2991 1608 C
ATOM 1802 O MET A 299 -10.149 8.117 -39.636 1.00 93.96 O
ANISOU 1802 O MET A 299 9681 12586 13433 -2543 -2879 1483 O
ATOM 1803 CB MET A 299 -13.425 7.992 -40.131 1.00 72.75 C
ANISOU 1803 CB MET A 299 6237 10260 11144 -2859 -3316 2183 C
ATOM 1804 CG MET A 299 -13.133 9.445 -39.741 1.00 71.57 C
ANISOU 1804 CG MET A 299 5847 10158 11190 -2497 -3070 2218 C
ATOM 1805 SD MET A 299 -14.483 10.222 -38.834 1.00 80.61 S
ANISOU 1805 SD MET A 299 6378 11499 12750 -2303 -2879 2552 S
ATOM 1806 CE MET A 299 -14.215 9.504 -37.207 1.00 73.01 C
ANISOU 1806 CE MET A 299 5416 10465 11859 -2258 -2519 2355 C
ATOM 1807 N LEU A 300 -11.229 6.567 -38.414 1.00 95.16 N
ANISOU 1807 N LEU A 300 9672 12782 13702 -2783 -2812 1525 N
ATOM 1808 CA LEU A 300 -10.319 6.747 -37.282 1.00 79.15 C
ANISOU 1808 CA LEU A 300 7678 10681 11715 -2573 -2466 1304 C
ATOM 1809 C LEU A 300 -8.888 6.363 -37.636 1.00 68.32 C
ANISOU 1809 C LEU A 300 6776 9137 10047 -2562 -2440 1023 C
ATOM 1810 O LEU A 300 -7.942 7.047 -37.226 1.00 60.52 O
ANISOU 1810 O LEU A 300 5819 8104 9071 -2350 -2234 881 O
ATOM 1811 CB LEU A 300 -10.805 5.964 -36.068 1.00 68.37 C
ANISOU 1811 CB LEU A 300 6177 9329 10473 -2634 -2289 1289 C
ATOM 1812 CG LEU A 300 -12.141 6.423 -35.490 1.00 68.72 C
ANISOU 1812 CG LEU A 300 5730 9541 10840 -2587 -2226 1570 C
ATOM 1813 CD1 LEU A 300 -12.604 5.431 -34.447 1.00 68.16 C
ANISOU 1813 CD1 LEU A 300 5593 9461 10843 -2708 -2090 1549 C
ATOM 1814 CD2 LEU A 300 -12.011 7.818 -34.893 1.00 63.09 C
ANISOU 1814 CD2 LEU A 300 4760 8876 10337 -2249 -1961 1628 C
ATOM 1815 N MET A 301 -8.701 5.275 -38.387 1.00 64.51 N
ANISOU 1815 N MET A 301 6672 8547 9291 -2784 -2635 956 N
ATOM 1816 CA MET A 301 -7.351 4.892 -38.790 1.00 64.61 C
ANISOU 1816 CA MET A 301 7150 8388 9010 -2746 -2590 720 C
ATOM 1817 C MET A 301 -6.702 5.998 -39.610 1.00 68.40 C
ANISOU 1817 C MET A 301 7685 8864 9440 -2596 -2633 718 C
ATOM 1818 O MET A 301 -5.489 6.221 -39.516 1.00 65.04 O
ANISOU 1818 O MET A 301 7465 8346 8901 -2449 -2477 532 O
ATOM 1819 CB MET A 301 -7.378 3.588 -39.582 1.00 66.53 C
ANISOU 1819 CB MET A 301 7823 8503 8954 -2999 -2792 696 C
ATOM 1820 CG MET A 301 -8.016 2.415 -38.862 1.00 76.15 C
ANISOU 1820 CG MET A 301 9032 9706 10195 -3182 -2775 705 C
ATOM 1821 SD MET A 301 -8.290 1.027 -39.986 1.00 91.63 S
ANISOU 1821 SD MET A 301 11492 11518 11804 -3518 -3070 749 S
ATOM 1822 CE MET A 301 -9.446 0.037 -39.040 1.00 95.05 C
ANISOU 1822 CE MET A 301 11705 12013 12398 -3747 -3080 847 C
ATOM 1823 N VAL A 302 -7.496 6.686 -40.435 1.00 76.13 N
ANISOU 1823 N VAL A 302 8483 9941 10501 -2637 -2852 935 N
ATOM 1824 CA VAL A 302 -6.981 7.826 -41.184 1.00 70.68 C
ANISOU 1824 CA VAL A 302 7812 9253 9791 -2490 -2897 958 C
ATOM 1825 C VAL A 302 -6.469 8.895 -40.226 1.00 62.43 C
ANISOU 1825 C VAL A 302 6501 8254 8965 -2220 -2612 897 C
ATOM 1826 O VAL A 302 -5.431 9.529 -40.470 1.00 55.83 O
ANISOU 1826 O VAL A 302 5813 7350 8051 -2085 -2535 781 O
ATOM 1827 CB VAL A 302 -8.073 8.382 -42.119 1.00 67.15 C
ANISOU 1827 CB VAL A 302 7168 8920 9428 -2575 -3179 1234 C
ATOM 1828 CG1 VAL A 302 -7.578 9.642 -42.817 1.00 67.46 C
ANISOU 1828 CG1 VAL A 302 7201 8961 9469 -2402 -3211 1271 C
ATOM 1829 CG2 VAL A 302 -8.503 7.323 -43.123 1.00 59.74 C
ANISOU 1829 CG2 VAL A 302 6548 7909 8242 -2872 -3479 1291 C
ATOM 1830 N VAL A 303 -7.205 9.132 -39.135 1.00 61.78 N
ANISOU 1830 N VAL A 303 6036 8278 9159 -2141 -2448 988 N
ATOM 1831 CA VAL A 303 -6.817 10.171 -38.190 1.00 59.98 C
ANISOU 1831 CA VAL A 303 5577 8073 9140 -1886 -2164 955 C
ATOM 1832 C VAL A 303 -5.505 9.806 -37.514 1.00 65.17 C
ANISOU 1832 C VAL A 303 6487 8606 9669 -1829 -1952 675 C
ATOM 1833 O VAL A 303 -4.679 10.679 -37.222 1.00 69.76 O
ANISOU 1833 O VAL A 303 7055 9149 10301 -1655 -1791 592 O
ATOM 1834 CB VAL A 303 -7.933 10.407 -37.157 1.00 48.90 C
ANISOU 1834 CB VAL A 303 3763 6785 8032 -1808 -2008 1127 C
ATOM 1835 CG1 VAL A 303 -7.451 11.383 -36.089 1.00 45.59 C
ANISOU 1835 CG1 VAL A 303 3190 6341 7790 -1541 -1675 1072 C
ATOM 1836 CG2 VAL A 303 -9.183 10.917 -37.847 1.00 52.13 C
ANISOU 1836 CG2 VAL A 303 3889 7331 8588 -1827 -2204 1435 C
ATOM 1837 N VAL A 304 -5.300 8.516 -37.238 1.00 63.57 N
ANISOU 1837 N VAL A 304 6516 8333 9304 -1974 -1947 538 N
ATOM 1838 CA VAL A 304 -4.072 8.091 -36.576 1.00 52.43 C
ANISOU 1838 CA VAL A 304 5343 6811 7767 -1913 -1748 292 C
ATOM 1839 C VAL A 304 -2.902 8.143 -37.550 1.00 61.20 C
ANISOU 1839 C VAL A 304 6810 7818 8626 -1896 -1823 169 C
ATOM 1840 O VAL A 304 -1.819 8.639 -37.219 1.00 65.23 O
ANISOU 1840 O VAL A 304 7387 8279 9119 -1761 -1665 36 O
ATOM 1841 CB VAL A 304 -4.239 6.687 -35.967 1.00 44.73 C
ANISOU 1841 CB VAL A 304 4509 5781 6703 -2052 -1708 205 C
ATOM 1842 CG1 VAL A 304 -3.143 6.441 -34.954 1.00 39.85 C
ANISOU 1842 CG1 VAL A 304 4022 5079 6039 -1944 -1461 -5 C
ATOM 1843 CG2 VAL A 304 -5.611 6.537 -35.347 1.00 47.57 C
ANISOU 1843 CG2 VAL A 304 4536 6249 7289 -2125 -1706 378 C
ATOM 1844 N LEU A 305 -3.104 7.630 -38.768 1.00 59.49 N
ANISOU 1844 N LEU A 305 6843 7558 8201 -2039 -2063 223 N
ATOM 1845 CA LEU A 305 -2.055 7.691 -39.785 1.00 61.12 C
ANISOU 1845 CA LEU A 305 7423 7653 8148 -2015 -2124 132 C
ATOM 1846 C LEU A 305 -1.665 9.129 -40.099 1.00 68.72 C
ANISOU 1846 C LEU A 305 8234 8654 9224 -1871 -2114 176 C
ATOM 1847 O LEU A 305 -0.480 9.428 -40.304 1.00 67.64 O
ANISOU 1847 O LEU A 305 8304 8433 8962 -1780 -2023 47 O
ATOM 1848 CB LEU A 305 -2.517 6.973 -41.051 1.00 66.73 C
ANISOU 1848 CB LEU A 305 8434 8298 8621 -2201 -2387 219 C
ATOM 1849 CG LEU A 305 -1.538 6.876 -42.215 1.00 74.71 C
ANISOU 1849 CG LEU A 305 9912 9161 9315 -2186 -2444 144 C
ATOM 1850 CD1 LEU A 305 -0.892 5.499 -42.240 1.00 66.65 C
ANISOU 1850 CD1 LEU A 305 9333 7980 8010 -2231 -2352 9 C
ATOM 1851 CD2 LEU A 305 -2.252 7.164 -43.516 1.00 84.86 C
ANISOU 1851 CD2 LEU A 305 11283 10447 10515 -2310 -2738 317 C
ATOM 1852 N VAL A 306 -2.648 10.029 -40.157 1.00 70.37 N
ANISOU 1852 N VAL A 306 8085 8984 9669 -1842 -2201 373 N
ATOM 1853 CA VAL A 306 -2.339 11.436 -40.364 1.00 63.80 C
ANISOU 1853 CA VAL A 306 7087 8178 8977 -1688 -2175 435 C
ATOM 1854 C VAL A 306 -1.533 11.970 -39.190 1.00 70.10 C
ANISOU 1854 C VAL A 306 7755 8950 9930 -1528 -1882 302 C
ATOM 1855 O VAL A 306 -0.644 12.812 -39.359 1.00 72.62 O
ANISOU 1855 O VAL A 306 8177 9213 10200 -1346 -1711 224 O
ATOM 1856 CB VAL A 306 -3.636 12.239 -40.576 1.00 53.47 C
ANISOU 1856 CB VAL A 306 5408 7004 7904 -1653 -2296 704 C
ATOM 1857 CG1 VAL A 306 -3.336 13.719 -40.493 1.00 49.72 C
ANISOU 1857 CG1 VAL A 306 4720 6543 7626 -1445 -2196 775 C
ATOM 1858 CG2 VAL A 306 -4.284 11.868 -41.896 1.00 48.60 C
ANISOU 1858 CG2 VAL A 306 4953 6399 7115 -1819 -2620 841 C
ATOM 1859 N PHE A 307 -1.842 11.492 -37.981 1.00 64.54 N
ANISOU 1859 N PHE A 307 6902 8276 9346 -1513 -1703 256 N
ATOM 1860 CA PHE A 307 -1.176 11.972 -36.774 1.00 55.47 C
ANISOU 1860 CA PHE A 307 5663 7093 8320 -1345 -1397 131 C
ATOM 1861 C PHE A 307 0.285 11.538 -36.745 1.00 51.79 C
ANISOU 1861 C PHE A 307 5541 6530 7607 -1299 -1265 -100 C
ATOM 1862 O PHE A 307 1.183 12.351 -36.483 1.00 55.90 O
ANISOU 1862 O PHE A 307 6096 7017 8126 -1133 -1066 -187 O
ATOM 1863 CB PHE A 307 -1.923 11.455 -35.557 1.00 57.06 C
ANISOU 1863 CB PHE A 307 5659 7340 8680 -1367 -1274 156 C
ATOM 1864 CG PHE A 307 -1.424 11.990 -34.254 1.00 59.04 C
ANISOU 1864 CG PHE A 307 5832 7545 9056 -1192 -962 51 C
ATOM 1865 CD1 PHE A 307 -0.604 11.232 -33.440 1.00 58.77 C
ANISOU 1865 CD1 PHE A 307 5988 7449 8892 -1196 -821 -147 C
ATOM 1866 CD2 PHE A 307 -1.802 13.265 -33.831 1.00 66.60 C
ANISOU 1866 CD2 PHE A 307 6574 8510 10221 -1000 -790 155 C
ATOM 1867 CE1 PHE A 307 -0.168 11.743 -32.225 1.00 63.16 C
ANISOU 1867 CE1 PHE A 307 6517 7963 9519 -1039 -547 -243 C
ATOM 1868 CE2 PHE A 307 -1.376 13.777 -32.624 1.00 60.17 C
ANISOU 1868 CE2 PHE A 307 5772 7624 9464 -842 -494 49 C
ATOM 1869 CZ PHE A 307 -0.558 13.023 -31.820 1.00 63.43 C
ANISOU 1869 CZ PHE A 307 6372 7985 9741 -875 -389 -152 C
ATOM 1870 N ALA A 308 0.538 10.252 -37.004 1.00 39.68 N
ANISOU 1870 N ALA A 308 4268 4949 5861 -1447 -1369 -184 N
ATOM 1871 CA ALA A 308 1.908 9.743 -37.025 1.00 39.03 C
ANISOU 1871 CA ALA A 308 4504 4785 5541 -1373 -1229 -365 C
ATOM 1872 C ALA A 308 2.757 10.446 -38.080 1.00 50.89 C
ANISOU 1872 C ALA A 308 6178 6250 6908 -1271 -1219 -370 C
ATOM 1873 O ALA A 308 3.903 10.829 -37.816 1.00 64.39 O
ANISOU 1873 O ALA A 308 7944 7946 8575 -1123 -1012 -466 O
ATOM 1874 CB ALA A 308 1.897 8.237 -37.267 1.00 40.48 C
ANISOU 1874 CB ALA A 308 4987 4896 5499 -1537 -1343 -422 C
ATOM 1875 N LEU A 309 2.220 10.599 -39.296 1.00 54.07 N
ANISOU 1875 N LEU A 309 6671 6638 7234 -1361 -1448 -253 N
ATOM 1876 CA LEU A 309 2.958 11.284 -40.356 1.00 52.47 C
ANISOU 1876 CA LEU A 309 6655 6386 6894 -1261 -1430 -243 C
ATOM 1877 C LEU A 309 3.260 12.726 -39.971 1.00 48.99 C
ANISOU 1877 C LEU A 309 5973 5987 6654 -1090 -1248 -221 C
ATOM 1878 O LEU A 309 4.385 13.208 -40.152 1.00 53.56 O
ANISOU 1878 O LEU A 309 6663 6530 7157 -971 -1074 -287 O
ATOM 1879 CB LEU A 309 2.175 11.230 -41.663 1.00 54.34 C
ANISOU 1879 CB LEU A 309 7034 6598 7014 -1399 -1738 -106 C
ATOM 1880 CG LEU A 309 2.050 9.857 -42.312 1.00 58.44 C
ANISOU 1880 CG LEU A 309 7937 7020 7246 -1594 -1933 -137 C
ATOM 1881 CD1 LEU A 309 1.355 9.973 -43.653 1.00 59.37 C
ANISOU 1881 CD1 LEU A 309 8227 7105 7224 -1738 -2260 4 C
ATOM 1882 CD2 LEU A 309 3.413 9.202 -42.447 1.00 56.34 C
ANISOU 1882 CD2 LEU A 309 8053 6635 6717 -1479 -1710 -291 C
ATOM 1883 N CYS A 310 2.254 13.438 -39.455 1.00 48.41 N
ANISOU 1883 N CYS A 310 5578 5981 6835 -1076 -1276 -110 N
ATOM 1884 CA CYS A 310 2.451 14.836 -39.079 1.00 54.35 C
ANISOU 1884 CA CYS A 310 6159 6733 7757 -914 -1093 -84 C
ATOM 1885 C CYS A 310 3.505 14.965 -37.980 1.00 63.77 C
ANISOU 1885 C CYS A 310 7358 7904 8967 -833 -827 -247 C
ATOM 1886 O CYS A 310 4.430 15.784 -38.078 1.00 69.38 O
ANISOU 1886 O CYS A 310 8133 8576 9653 -748 -682 -292 O
ATOM 1887 CB CYS A 310 1.123 15.447 -38.624 1.00 48.00 C
ANISOU 1887 CB CYS A 310 5030 5992 7215 -882 -1132 82 C
ATOM 1888 SG CYS A 310 -0.120 15.709 -39.915 1.00 62.13 S
ANISOU 1888 SG CYS A 310 6724 7845 9037 -945 -1457 339 S
ATOM 1889 N TYR A 311 3.388 14.148 -36.927 1.00 58.18 N
ANISOU 1889 N TYR A 311 6588 7221 8296 -875 -773 -326 N
ATOM 1890 CA TYR A 311 4.335 14.219 -35.821 1.00 45.86 C
ANISOU 1890 CA TYR A 311 5034 5649 6740 -811 -558 -468 C
ATOM 1891 C TYR A 311 5.616 13.426 -36.030 1.00 57.45 C
ANISOU 1891 C TYR A 311 6717 7115 7996 -812 -512 -581 C
ATOM 1892 O TYR A 311 6.542 13.583 -35.225 1.00 67.17 O
ANISOU 1892 O TYR A 311 7936 8360 9225 -762 -358 -673 O
ATOM 1893 CB TYR A 311 3.682 13.766 -34.531 1.00 35.87 C
ANISOU 1893 CB TYR A 311 3627 4402 5600 -827 -493 -494 C
ATOM 1894 CG TYR A 311 2.718 14.789 -33.995 1.00 44.95 C
ANISOU 1894 CG TYR A 311 4559 5541 6978 -752 -416 -387 C
ATOM 1895 CD1 TYR A 311 1.449 14.907 -34.536 1.00 47.15 C
ANISOU 1895 CD1 TYR A 311 4668 5862 7385 -774 -554 -205 C
ATOM 1896 CD2 TYR A 311 3.090 15.658 -32.972 1.00 51.75 C
ANISOU 1896 CD2 TYR A 311 5403 6345 7916 -655 -204 -450 C
ATOM 1897 CE1 TYR A 311 0.564 15.841 -34.074 1.00 50.66 C
ANISOU 1897 CE1 TYR A 311 4905 6301 8044 -659 -448 -72 C
ATOM 1898 CE2 TYR A 311 2.203 16.603 -32.494 1.00 45.53 C
ANISOU 1898 CE2 TYR A 311 4473 5512 7313 -552 -89 -342 C
ATOM 1899 CZ TYR A 311 0.932 16.691 -33.052 1.00 54.65 C
ANISOU 1899 CZ TYR A 311 5433 6719 8611 -532 -194 -143 C
ATOM 1900 OH TYR A 311 0.024 17.629 -32.592 1.00 69.63 O
ANISOU 1900 OH TYR A 311 7173 8579 10704 -383 -46 3 O
ATOM 1901 N LEU A 312 5.711 12.583 -37.058 1.00 53.60 N
ANISOU 1901 N LEU A 312 6438 6607 7321 -863 -635 -564 N
ATOM 1902 CA LEU A 312 6.988 11.913 -37.320 1.00 52.97 C
ANISOU 1902 CA LEU A 312 6574 6514 7037 -809 -537 -640 C
ATOM 1903 C LEU A 312 8.163 12.879 -37.471 1.00 59.76 C
ANISOU 1903 C LEU A 312 7406 7393 7906 -711 -379 -645 C
ATOM 1904 O LEU A 312 9.215 12.643 -36.850 1.00 60.37 O
ANISOU 1904 O LEU A 312 7469 7517 7951 -654 -239 -707 O
ATOM 1905 CB LEU A 312 6.872 11.027 -38.572 1.00 45.29 C
ANISOU 1905 CB LEU A 312 5906 5472 5832 -860 -671 -604 C
ATOM 1906 CG LEU A 312 8.176 10.253 -38.771 1.00 37.83 C
ANISOU 1906 CG LEU A 312 5200 4500 4672 -755 -514 -662 C
ATOM 1907 CD1 LEU A 312 8.554 9.390 -37.538 1.00 34.39 C
ANISOU 1907 CD1 LEU A 312 4720 4106 4242 -721 -404 -753 C
ATOM 1908 CD2 LEU A 312 8.166 9.423 -40.046 1.00 42.94 C
ANISOU 1908 CD2 LEU A 312 6241 5031 5042 -780 -601 -630 C
ATOM 1909 N PRO A 313 8.078 13.926 -38.290 1.00 52.71 N
ANISOU 1909 N PRO A 313 6506 6471 7051 -696 -400 -567 N
ATOM 1910 CA PRO A 313 9.228 14.821 -38.473 1.00 49.41 C
ANISOU 1910 CA PRO A 313 6073 6063 6638 -635 -244 -560 C
ATOM 1911 C PRO A 313 9.744 15.436 -37.175 1.00 47.44 C
ANISOU 1911 C PRO A 313 5634 5860 6532 -642 -120 -625 C
ATOM 1912 O PRO A 313 10.890 15.195 -36.777 1.00 42.87 O
ANISOU 1912 O PRO A 313 5037 5345 5908 -622 -13 -661 O
ATOM 1913 CB PRO A 313 8.668 15.899 -39.413 1.00 42.26 C
ANISOU 1913 CB PRO A 313 5185 5095 5777 -632 -310 -461 C
ATOM 1914 CG PRO A 313 7.621 15.194 -40.199 1.00 36.71 C
ANISOU 1914 CG PRO A 313 4604 4361 4983 -679 -519 -403 C
ATOM 1915 CD PRO A 313 6.979 14.244 -39.220 1.00 44.88 C
ANISOU 1915 CD PRO A 313 5546 5437 6071 -743 -581 -461 C
ATOM 1916 N ILE A 314 8.908 16.229 -36.499 1.00 46.84 N
ANISOU 1916 N ILE A 314 5426 5750 6620 -667 -134 -625 N
ATOM 1917 CA ILE A 314 9.387 16.955 -35.326 1.00 48.16 C
ANISOU 1917 CA ILE A 314 5493 5918 6887 -691 -20 -688 C
ATOM 1918 C ILE A 314 9.787 15.996 -34.216 1.00 55.04 C
ANISOU 1918 C ILE A 314 6333 6856 7722 -704 4 -782 C
ATOM 1919 O ILE A 314 10.685 16.299 -33.418 1.00 58.42 O
ANISOU 1919 O ILE A 314 6720 7320 8157 -739 76 -832 O
ATOM 1920 CB ILE A 314 8.327 17.974 -34.847 1.00 44.22 C
ANISOU 1920 CB ILE A 314 4925 5331 6545 -679 -2 -657 C
ATOM 1921 CG1 ILE A 314 8.911 18.846 -33.757 1.00 37.17 C
ANISOU 1921 CG1 ILE A 314 4027 4390 5705 -721 121 -726 C
ATOM 1922 CG2 ILE A 314 7.091 17.286 -34.330 1.00 34.27 C
ANISOU 1922 CG2 ILE A 314 3586 4079 5356 -660 -64 -646 C
ATOM 1923 CD1 ILE A 314 10.328 19.341 -34.072 1.00 34.96 C
ANISOU 1923 CD1 ILE A 314 3786 4138 5359 -792 172 -735 C
ATOM 1924 N SER A 315 9.146 14.829 -34.147 1.00 62.41 N
ANISOU 1924 N SER A 315 7299 7807 8609 -692 -68 -797 N
ATOM 1925 CA SER A 315 9.487 13.865 -33.105 1.00 55.50 C
ANISOU 1925 CA SER A 315 6421 6980 7685 -688 -36 -880 C
ATOM 1926 C SER A 315 10.873 13.273 -33.333 1.00 61.77 C
ANISOU 1926 C SER A 315 7271 7858 8341 -642 19 -886 C
ATOM 1927 O SER A 315 11.698 13.237 -32.410 1.00 64.50 O
ANISOU 1927 O SER A 315 7551 8271 8684 -641 74 -927 O
ATOM 1928 CB SER A 315 8.429 12.756 -33.028 1.00 47.61 C
ANISOU 1928 CB SER A 315 5465 5960 6665 -704 -117 -885 C
ATOM 1929 OG SER A 315 7.105 13.280 -33.025 1.00 63.32 O
ANISOU 1929 OG SER A 315 7356 7902 8802 -736 -171 -825 O
ATOM 1930 N VAL A 316 11.155 12.831 -34.566 1.00 58.99 N
ANISOU 1930 N VAL A 316 7046 7501 7867 -594 9 -826 N
ATOM 1931 CA VAL A 316 12.484 12.319 -34.908 1.00 48.55 C
ANISOU 1931 CA VAL A 316 5774 6254 6420 -504 110 -790 C
ATOM 1932 C VAL A 316 13.524 13.429 -34.827 1.00 52.86 C
ANISOU 1932 C VAL A 316 6165 6870 7048 -529 190 -744 C
ATOM 1933 O VAL A 316 14.630 13.229 -34.308 1.00 50.17 O
ANISOU 1933 O VAL A 316 5723 6645 6694 -499 260 -720 O
ATOM 1934 CB VAL A 316 12.470 11.660 -36.302 1.00 36.11 C
ANISOU 1934 CB VAL A 316 4436 4614 4671 -435 112 -729 C
ATOM 1935 CG1 VAL A 316 13.882 11.417 -36.836 1.00 47.10 C
ANISOU 1935 CG1 VAL A 316 5870 6072 5954 -304 275 -647 C
ATOM 1936 CG2 VAL A 316 11.691 10.358 -36.247 1.00 22.61 C
ANISOU 1936 CG2 VAL A 316 2913 2836 2840 -440 33 -776 C
ATOM 1937 N LEU A 317 13.184 14.624 -35.326 1.00 53.91 N
ANISOU 1937 N LEU A 317 6275 6938 7270 -595 172 -714 N
ATOM 1938 CA LEU A 317 14.135 15.736 -35.307 1.00 47.46 C
ANISOU 1938 CA LEU A 317 5343 6164 6528 -659 244 -666 C
ATOM 1939 C LEU A 317 14.571 16.050 -33.879 1.00 60.58 C
ANISOU 1939 C LEU A 317 6865 7887 8266 -755 233 -728 C
ATOM 1940 O LEU A 317 15.746 16.345 -33.631 1.00 80.42 O
ANISOU 1940 O LEU A 317 9257 10506 10793 -809 274 -677 O
ATOM 1941 CB LEU A 317 13.503 16.970 -35.956 1.00 38.29 C
ANISOU 1941 CB LEU A 317 4224 4884 5441 -711 228 -637 C
ATOM 1942 CG LEU A 317 13.531 17.013 -37.483 1.00 50.26 C
ANISOU 1942 CG LEU A 317 5877 6353 6867 -641 255 -544 C
ATOM 1943 CD1 LEU A 317 13.095 18.373 -38.035 1.00 64.42 C
ANISOU 1943 CD1 LEU A 317 7701 8037 8737 -687 254 -499 C
ATOM 1944 CD2 LEU A 317 14.902 16.608 -37.994 1.00 48.11 C
ANISOU 1944 CD2 LEU A 317 5597 6176 6508 -577 387 -462 C
ATOM 1945 N ASN A 318 13.631 15.983 -32.921 1.00 62.48 N
ANISOU 1945 N ASN A 318 7125 8062 8552 -784 174 -823 N
ATOM 1946 CA ASN A 318 13.959 16.287 -31.527 1.00 56.83 C
ANISOU 1946 CA ASN A 318 6349 7370 7874 -877 159 -891 C
ATOM 1947 C ASN A 318 14.917 15.259 -30.930 1.00 46.64 C
ANISOU 1947 C ASN A 318 4985 6234 6503 -837 151 -885 C
ATOM 1948 O ASN A 318 15.828 15.629 -30.179 1.00 44.78 O
ANISOU 1948 O ASN A 318 4654 6084 6278 -935 125 -875 O
ATOM 1949 CB ASN A 318 12.668 16.375 -30.701 1.00 60.04 C
ANISOU 1949 CB ASN A 318 6825 7653 8334 -877 141 -976 C
ATOM 1950 CG ASN A 318 12.910 16.826 -29.267 1.00 75.70 C
ANISOU 1950 CG ASN A 318 8828 9608 10326 -974 138 -1054 C
ATOM 1951 OD1 ASN A 318 13.221 17.987 -29.015 1.00 90.64 O
ANISOU 1951 OD1 ASN A 318 10758 11432 12251 -1090 151 -1059 O
ATOM 1952 ND2 ASN A 318 12.749 15.907 -28.319 1.00 75.14 N
ANISOU 1952 ND2 ASN A 318 8776 9569 10206 -935 122 -1115 N
ATOM 1953 N VAL A 319 14.748 13.976 -31.268 1.00 42.20 N
ANISOU 1953 N VAL A 319 4479 5706 5851 -698 167 -876 N
ATOM 1954 CA VAL A 319 15.649 12.945 -30.752 1.00 42.05 C
ANISOU 1954 CA VAL A 319 4409 5825 5744 -613 186 -849 C
ATOM 1955 C VAL A 319 17.037 13.092 -31.357 1.00 53.15 C
ANISOU 1955 C VAL A 319 5676 7378 7139 -579 252 -708 C
ATOM 1956 O VAL A 319 18.050 12.931 -30.663 1.00 58.18 O
ANISOU 1956 O VAL A 319 6159 8171 7775 -586 239 -649 O
ATOM 1957 CB VAL A 319 15.060 11.540 -30.994 1.00 37.33 C
ANISOU 1957 CB VAL A 319 3969 5183 5030 -473 209 -876 C
ATOM 1958 CG1 VAL A 319 16.130 10.478 -30.883 1.00 42.63 C
ANISOU 1958 CG1 VAL A 319 4624 5986 5588 -322 280 -801 C
ATOM 1959 CG2 VAL A 319 13.915 11.272 -30.016 1.00 27.30 C
ANISOU 1959 CG2 VAL A 319 2769 3817 3787 -521 152 -991 C
ATOM 1960 N LEU A 320 17.109 13.414 -32.648 1.00 52.65 N
ANISOU 1960 N LEU A 320 5655 7277 7073 -540 325 -632 N
ATOM 1961 CA LEU A 320 18.404 13.640 -33.281 1.00 52.77 C
ANISOU 1961 CA LEU A 320 5527 7427 7097 -503 427 -473 C
ATOM 1962 C LEU A 320 19.125 14.828 -32.651 1.00 55.19 C
ANISOU 1962 C LEU A 320 5624 7818 7529 -713 366 -438 C
ATOM 1963 O LEU A 320 20.352 14.810 -32.477 1.00 69.72 O
ANISOU 1963 O LEU A 320 7247 9845 9400 -726 394 -302 O
ATOM 1964 CB LEU A 320 18.201 13.864 -34.776 1.00 60.34 C
ANISOU 1964 CB LEU A 320 6626 8287 8013 -434 522 -412 C
ATOM 1965 CG LEU A 320 17.604 12.688 -35.551 1.00 53.69 C
ANISOU 1965 CG LEU A 320 6048 7345 7007 -257 569 -429 C
ATOM 1966 CD1 LEU A 320 17.268 13.068 -36.984 1.00 62.82 C
ANISOU 1966 CD1 LEU A 320 7390 8376 8104 -228 618 -382 C
ATOM 1967 CD2 LEU A 320 18.545 11.489 -35.525 1.00 40.20 C
ANISOU 1967 CD2 LEU A 320 4343 5749 5183 -52 703 -332 C
ATOM 1968 N LYS A 321 18.376 15.882 -32.326 1.00 49.19 N
ANISOU 1968 N LYS A 321 4934 6918 6840 -884 285 -543 N
ATOM 1969 CA LYS A 321 18.972 17.049 -31.693 1.00 45.49 C
ANISOU 1969 CA LYS A 321 4352 6476 6456 -1119 218 -529 C
ATOM 1970 C LYS A 321 19.401 16.739 -30.264 1.00 59.07 C
ANISOU 1970 C LYS A 321 5986 8301 8158 -1206 97 -568 C
ATOM 1971 O LYS A 321 20.554 16.979 -29.887 1.00 66.89 O
ANISOU 1971 O LYS A 321 6777 9459 9179 -1332 40 -461 O
ATOM 1972 CB LYS A 321 17.977 18.209 -31.726 1.00 34.56 C
ANISOU 1972 CB LYS A 321 3139 4872 5121 -1237 198 -630 C
ATOM 1973 CG LYS A 321 18.509 19.526 -31.205 1.00 46.18 C
ANISOU 1973 CG LYS A 321 4590 6306 6651 -1498 145 -626 C
ATOM 1974 CD LYS A 321 17.341 20.456 -30.911 1.00 41.29 C
ANISOU 1974 CD LYS A 321 4201 5437 6048 -1554 147 -746 C
ATOM 1975 CE LYS A 321 17.790 21.908 -30.826 1.00 62.29 C
ANISOU 1975 CE LYS A 321 6937 7991 8741 -1789 140 -723 C
ATOM 1976 NZ LYS A 321 18.151 22.463 -32.164 1.00 72.74 N
ANISOU 1976 NZ LYS A 321 8215 9310 10112 -1795 240 -611 N
ATOM 1977 N ARG A 322 18.479 16.217 -29.450 1.00 60.68 N
ANISOU 1977 N ARG A 322 6335 8410 8310 -1151 49 -707 N
ATOM 1978 CA ARG A 322 18.700 16.131 -28.013 1.00 60.66 C
ANISOU 1978 CA ARG A 322 6329 8448 8269 -1257 -72 -770 C
ATOM 1979 C ARG A 322 19.449 14.875 -27.583 1.00 65.42 C
ANISOU 1979 C ARG A 322 6800 9253 8803 -1118 -94 -696 C
ATOM 1980 O ARG A 322 20.300 14.946 -26.691 1.00 78.70 O
ANISOU 1980 O ARG A 322 8360 11073 10469 -1235 -215 -647 O
ATOM 1981 CB ARG A 322 17.359 16.220 -27.294 1.00 53.23 C
ANISOU 1981 CB ARG A 322 5620 7298 7308 -1251 -76 -937 C
ATOM 1982 CG ARG A 322 16.617 17.486 -27.645 1.00 49.98 C
ANISOU 1982 CG ARG A 322 5341 6684 6963 -1350 -34 -986 C
ATOM 1983 CD ARG A 322 17.136 18.658 -26.839 1.00 64.28 C
ANISOU 1983 CD ARG A 322 7253 8420 8749 -1543 -117 -968 C
ATOM 1984 NE ARG A 322 16.456 19.902 -27.182 1.00 78.83 N
ANISOU 1984 NE ARG A 322 9265 10051 10635 -1600 -50 -994 N
ATOM 1985 CZ ARG A 322 16.781 21.090 -26.686 1.00 88.19 C
ANISOU 1985 CZ ARG A 322 10598 11117 11795 -1770 -95 -987 C
ATOM 1986 NH1 ARG A 322 17.780 21.203 -25.820 1.00 77.42 N
ANISOU 1986 NH1 ARG A 322 9220 9826 10372 -1913 -236 -949 N
ATOM 1987 NH2 ARG A 322 16.108 22.166 -27.056 1.00101.51 N
ANISOU 1987 NH2 ARG A 322 12454 12601 13514 -1798 -2 -1015 N
ATOM 1988 N VAL A 323 19.162 13.728 -28.199 1.00 65.47 N
ANISOU 1988 N VAL A 323 6849 9273 8754 -876 13 -675 N
ATOM 1989 CA VAL A 323 19.835 12.485 -27.829 1.00 64.06 C
ANISOU 1989 CA VAL A 323 6588 9259 8492 -701 28 -595 C
ATOM 1990 C VAL A 323 21.117 12.254 -28.627 1.00 63.59 C
ANISOU 1990 C VAL A 323 6299 9407 8455 -593 119 -375 C
ATOM 1991 O VAL A 323 22.088 11.706 -28.091 1.00 69.30 O
ANISOU 1991 O VAL A 323 6838 10336 9157 -522 91 -245 O
ATOM 1992 CB VAL A 323 18.880 11.290 -27.980 1.00 60.75 C
ANISOU 1992 CB VAL A 323 6388 8720 7974 -502 109 -683 C
ATOM 1993 CG1 VAL A 323 19.474 10.062 -27.317 1.00 58.64 C
ANISOU 1993 CG1 VAL A 323 6095 8584 7602 -330 121 -625 C
ATOM 1994 CG2 VAL A 323 17.526 11.621 -27.392 1.00 64.56 C
ANISOU 1994 CG2 VAL A 323 7056 9000 8473 -604 57 -862 C
ATOM 1995 N PHE A 324 21.153 12.668 -29.891 1.00 61.09 N
ANISOU 1995 N PHE A 324 5984 9046 8181 -565 239 -308 N
ATOM 1996 CA PHE A 324 22.321 12.448 -30.731 1.00 70.02 C
ANISOU 1996 CA PHE A 324 6918 10354 9334 -431 381 -81 C
ATOM 1997 C PHE A 324 23.129 13.710 -30.997 1.00 83.92 C
ANISOU 1997 C PHE A 324 8442 12212 11233 -653 352 40 C
ATOM 1998 O PHE A 324 24.101 13.654 -31.757 1.00 92.30 O
ANISOU 1998 O PHE A 324 9311 13423 12339 -556 495 254 O
ATOM 1999 CB PHE A 324 21.904 11.823 -32.066 1.00 66.60 C
ANISOU 1999 CB PHE A 324 6704 9793 8807 -202 577 -64 C
ATOM 2000 CG PHE A 324 21.320 10.449 -31.927 1.00 64.52 C
ANISOU 2000 CG PHE A 324 6681 9446 8388 14 626 -141 C
ATOM 2001 CD1 PHE A 324 20.067 10.255 -31.380 1.00 60.94 C
ANISOU 2001 CD1 PHE A 324 6440 8822 7895 -62 512 -346 C
ATOM 2002 CD2 PHE A 324 22.050 9.345 -32.325 1.00 65.32 C
ANISOU 2002 CD2 PHE A 324 6802 9635 8383 299 805 11 C
ATOM 2003 CE1 PHE A 324 19.546 8.981 -31.243 1.00 46.70 C
ANISOU 2003 CE1 PHE A 324 4862 6934 5947 103 555 -408 C
ATOM 2004 CE2 PHE A 324 21.543 8.067 -32.199 1.00 52.16 C
ANISOU 2004 CE2 PHE A 324 5405 7862 6550 487 860 -58 C
ATOM 2005 CZ PHE A 324 20.288 7.881 -31.657 1.00 38.21 C
ANISOU 2005 CZ PHE A 324 3848 5925 4746 369 724 -273 C
ATOM 2006 N GLY A 325 22.753 14.845 -30.412 1.00 86.07 N
ANISOU 2006 N GLY A 325 8745 12389 11568 -945 194 -78 N
ATOM 2007 CA GLY A 325 23.537 16.057 -30.569 1.00 87.04 C
ANISOU 2007 CA GLY A 325 8677 12585 11808 -1202 150 32 C
ATOM 2008 C GLY A 325 23.712 16.469 -32.011 1.00 80.20 C
ANISOU 2008 C GLY A 325 7807 11676 10989 -1136 342 141 C
ATOM 2009 O GLY A 325 24.722 17.077 -32.356 1.00 94.45 O
ANISOU 2009 O GLY A 325 9384 13607 12894 -1253 377 322 O
ATOM 2010 N MET A 326 22.740 16.167 -32.865 1.00 68.43 N
ANISOU 2010 N MET A 326 6584 9993 9424 -959 456 42 N
ATOM 2011 CA MET A 326 22.808 16.486 -34.284 1.00 68.60 C
ANISOU 2011 CA MET A 326 6672 9943 9449 -872 637 135 C
ATOM 2012 C MET A 326 22.398 17.936 -34.529 1.00 71.22 C
ANISOU 2012 C MET A 326 7092 10114 9856 -1116 589 68 C
ATOM 2013 O MET A 326 21.980 18.656 -33.621 1.00 76.50 O
ANISOU 2013 O MET A 326 7808 10700 10559 -1333 432 -60 O
ATOM 2014 CB MET A 326 21.947 15.515 -35.095 1.00 71.10 C
ANISOU 2014 CB MET A 326 7276 10116 9623 -602 743 65 C
ATOM 2015 CG MET A 326 22.457 14.082 -35.103 1.00 77.58 C
ANISOU 2015 CG MET A 326 8078 11059 10341 -327 857 160 C
ATOM 2016 SD MET A 326 21.871 13.117 -36.509 1.00 86.64 S
ANISOU 2016 SD MET A 326 9603 12025 11290 -37 1044 158 S
ATOM 2017 CE MET A 326 22.835 13.887 -37.803 1.00 91.24 C
ANISOU 2017 CE MET A 326 10095 12648 11923 -4 1267 378 C
ATOM 2018 N PHE A 327 22.517 18.372 -35.781 1.00 76.06 N
ANISOU 2018 N PHE A 327 7767 10659 10474 -1064 745 161 N
ATOM 2019 CA PHE A 327 22.095 19.714 -36.175 1.00 71.85 C
ANISOU 2019 CA PHE A 327 7358 9948 9992 -1252 732 112 C
ATOM 2020 C PHE A 327 22.897 20.780 -35.431 1.00 81.36 C
ANISOU 2020 C PHE A 327 8372 11226 11314 -1581 638 165 C
ATOM 2021 O PHE A 327 22.376 21.839 -35.068 1.00 96.44 O
ANISOU 2021 O PHE A 327 10433 12964 13247 -1789 550 53 O
ATOM 2022 CB PHE A 327 20.597 19.901 -35.938 1.00 58.21 C
ANISOU 2022 CB PHE A 327 5908 7994 8215 -1240 627 -97 C
ATOM 2023 CG PHE A 327 19.769 18.728 -36.374 1.00 55.23 C
ANISOU 2023 CG PHE A 327 5696 7567 7722 -983 647 -159 C
ATOM 2024 CD1 PHE A 327 19.982 18.134 -37.611 1.00 66.91 C
ANISOU 2024 CD1 PHE A 327 7265 9047 9109 -783 796 -54 C
ATOM 2025 CD2 PHE A 327 18.803 18.192 -35.531 1.00 51.96 C
ANISOU 2025 CD2 PHE A 327 5371 7096 7277 -955 524 -312 C
ATOM 2026 CE1 PHE A 327 19.226 17.035 -38.025 1.00 67.03 C
ANISOU 2026 CE1 PHE A 327 7489 8992 8988 -586 793 -113 C
ATOM 2027 CE2 PHE A 327 18.045 17.096 -35.931 1.00 64.57 C
ANISOU 2027 CE2 PHE A 327 7124 8643 8766 -764 526 -359 C
ATOM 2028 CZ PHE A 327 18.259 16.516 -37.184 1.00 68.76 C
ANISOU 2028 CZ PHE A 327 7772 9163 9189 -594 646 -264 C
ATOM 2029 N ARG A 328 24.180 20.490 -35.192 1.00 79.59 N
ANISOU 2029 N ARG A 328 7824 11259 11159 -1632 654 352 N
ATOM 2030 CA ARG A 328 25.079 21.433 -34.540 1.00 82.72 C
ANISOU 2030 CA ARG A 328 8091 11676 11661 -1903 529 411 C
ATOM 2031 C ARG A 328 26.171 21.976 -35.451 1.00107.69 C
ANISOU 2031 C ARG A 328 11086 14913 14916 -1948 687 616 C
ATOM 2032 O ARG A 328 26.902 22.879 -35.031 1.00121.50 O
ANISOU 2032 O ARG A 328 12776 16643 16745 -2179 588 645 O
ATOM 2033 CB ARG A 328 25.702 20.789 -33.293 1.00 79.09 C
ANISOU 2033 CB ARG A 328 7485 11362 11203 -1893 352 413 C
ATOM 2034 CG ARG A 328 24.675 20.489 -32.215 1.00 93.74 C
ANISOU 2034 CG ARG A 328 9544 13105 12967 -1900 183 203 C
ATOM 2035 CD ARG A 328 25.259 19.789 -30.996 1.00106.10 C
ANISOU 2035 CD ARG A 328 10987 14818 14510 -1883 18 216 C
ATOM 2036 NE ARG A 328 25.945 18.545 -31.339 1.00112.28 N
ANISOU 2036 NE ARG A 328 11526 15848 15288 -1633 131 379 N
ATOM 2037 CZ ARG A 328 26.581 17.776 -30.459 1.00115.36 C
ANISOU 2037 CZ ARG A 328 11768 16409 15656 -1567 24 443 C
ATOM 2038 NH1 ARG A 328 27.182 16.663 -30.857 1.00115.82 N
ANISOU 2038 NH1 ARG A 328 11638 16668 15701 -1295 164 611 N
ATOM 2039 NH2 ARG A 328 26.602 18.116 -29.179 1.00112.09 N
ANISOU 2039 NH2 ARG A 328 11425 15952 15212 -1754 -211 348 N
ATOM 2040 N GLN A 329 26.288 21.476 -36.681 1.00113.00 N
ANISOU 2040 N GLN A 329 11713 15657 15565 -1731 938 762 N
ATOM 2041 CA GLN A 329 27.179 22.056 -37.676 1.00111.63 C
ANISOU 2041 CA GLN A 329 11443 15513 15457 -1755 1130 948 C
ATOM 2042 C GLN A 329 26.421 23.174 -38.380 1.00103.68 C
ANISOU 2042 C GLN A 329 10674 14272 14445 -1911 1194 895 C
ATOM 2043 O GLN A 329 25.296 22.973 -38.851 1.00 96.70 O
ANISOU 2043 O GLN A 329 10083 13206 13454 -1743 1226 764 O
ATOM 2044 CB GLN A 329 27.639 20.998 -38.680 1.00121.52 C
ANISOU 2044 CB GLN A 329 12620 16896 16658 -1395 1400 1141 C
ATOM 2045 CG GLN A 329 28.544 21.507 -39.803 1.00136.19 C
ANISOU 2045 CG GLN A 329 14412 18775 18560 -1371 1636 1345 C
ATOM 2046 CD GLN A 329 29.928 21.916 -39.318 1.00146.71 C
ANISOU 2046 CD GLN A 329 15442 20281 20021 -1545 1558 1470 C
ATOM 2047 OE1 GLN A 329 30.272 23.099 -39.289 1.00151.47 O
ANISOU 2047 OE1 GLN A 329 16019 20823 20710 -1845 1503 1469 O
ATOM 2048 NE2 GLN A 329 30.731 20.929 -38.934 1.00147.20 N
ANISOU 2048 NE2 GLN A 329 15282 20551 20095 -1354 1555 1594 N
ATOM 2049 N ALA A 330 27.044 24.343 -38.463 1.00112.76 N
ANISOU 2049 N ALA A 330 11807 15355 15681 -2160 1190 936 N
ATOM 2050 CA ALA A 330 26.399 25.564 -38.934 1.00111.16 C
ANISOU 2050 CA ALA A 330 11861 14899 15478 -2345 1224 879 C
ATOM 2051 C ALA A 330 26.337 25.693 -40.455 1.00115.96 C
ANISOU 2051 C ALA A 330 12567 15441 16052 -2195 1510 1034 C
ATOM 2052 O ALA A 330 25.733 26.658 -40.936 1.00112.48 O
ANISOU 2052 O ALA A 330 12417 14748 15571 -2272 1541 954 O
ATOM 2053 CB ALA A 330 27.102 26.787 -38.346 1.00101.41 C
ANISOU 2053 CB ALA A 330 10609 13576 14348 -2654 1102 870 C
ATOM 2054 N SER A 331 26.936 24.772 -41.218 1.00124.33 N
ANISOU 2054 N SER A 331 13484 16659 17097 -1912 1723 1214 N
ATOM 2055 CA SER A 331 27.019 24.929 -42.669 1.00127.27 C
ANISOU 2055 CA SER A 331 14026 16918 17411 -1722 2010 1343 C
ATOM 2056 C SER A 331 25.648 25.131 -43.311 1.00131.21 C
ANISOU 2056 C SER A 331 15000 17110 17742 -1567 1981 1139 C
ATOM 2057 O SER A 331 25.435 26.092 -44.055 1.00135.91 O
ANISOU 2057 O SER A 331 15809 17513 18317 -1636 2073 1155 O
ATOM 2058 CB SER A 331 27.706 23.702 -43.271 1.00122.23 C
ANISOU 2058 CB SER A 331 13262 16460 16720 -1372 2232 1521 C
ATOM 2059 OG SER A 331 26.873 22.563 -43.147 1.00110.90 O
ANISOU 2059 OG SER A 331 12015 14980 15139 -1094 2172 1376 O
ATOM 2060 N ASP A 332 24.698 24.240 -43.033 1.00132.78 N
ANISOU 2060 N ASP A 332 15363 17265 17823 -1363 1846 963 N
ATOM 2061 CA ASP A 332 23.357 24.350 -43.610 1.00130.25 C
ANISOU 2061 CA ASP A 332 15442 16691 17357 -1223 1782 798 C
ATOM 2062 C ASP A 332 22.370 24.756 -42.521 1.00116.36 C
ANISOU 2062 C ASP A 332 13746 14837 15629 -1375 1520 580 C
ATOM 2063 O ASP A 332 21.323 24.129 -42.354 1.00125.82 O
ANISOU 2063 O ASP A 332 15098 15970 16740 -1225 1391 436 O
ATOM 2064 CB ASP A 332 22.949 23.047 -44.314 1.00141.73 C
ANISOU 2064 CB ASP A 332 17084 18136 18632 -882 1845 790 C
ATOM 2065 CG ASP A 332 22.965 21.842 -43.401 1.00151.63 C
ANISOU 2065 CG ASP A 332 18181 19553 19878 -792 1738 725 C
ATOM 2066 OD1 ASP A 332 23.394 21.966 -42.243 1.00156.56 O
ANISOU 2066 OD1 ASP A 332 18521 20326 20637 -976 1621 707 O
ATOM 2067 OD2 ASP A 332 22.534 20.762 -43.835 1.00156.34 O
ANISOU 2067 OD2 ASP A 332 18973 20114 20315 -547 1760 691 O
ATOM 2068 N ARG A 333 22.694 25.827 -41.784 1.00 87.27 N
ANISOU 2068 N ARG A 333 9965 11130 12063 -1683 1451 566 N
ATOM 2069 CA ARG A 333 21.798 26.302 -40.730 1.00 68.39 C
ANISOU 2069 CA ARG A 333 7686 8614 9685 -1816 1247 371 C
ATOM 2070 C ARG A 333 20.431 26.663 -41.295 1.00 70.18 C
ANISOU 2070 C ARG A 333 8244 8598 9824 -1656 1226 267 C
ATOM 2071 O ARG A 333 19.406 26.468 -40.633 1.00 81.57 O
ANISOU 2071 O ARG A 333 9775 9971 11247 -1599 1084 119 O
ATOM 2072 CB ARG A 333 22.397 27.526 -40.049 1.00 68.83 C
ANISOU 2072 CB ARG A 333 7692 8623 9838 -2184 1208 387 C
ATOM 2073 CG ARG A 333 21.747 27.894 -38.736 1.00 75.65 C
ANISOU 2073 CG ARG A 333 8659 9383 10701 -2338 1017 203 C
ATOM 2074 CD ARG A 333 22.308 29.215 -38.208 1.00 97.77 C
ANISOU 2074 CD ARG A 333 11524 12072 13553 -2724 989 218 C
ATOM 2075 NE ARG A 333 23.676 29.175 -37.713 1.00115.17 N
ANISOU 2075 NE ARG A 333 13431 14488 15839 -2878 887 362 N
ATOM 2076 CZ ARG A 333 24.281 30.233 -37.184 1.00126.89 C
ANISOU 2076 CZ ARG A 333 14968 15881 17364 -3112 787 387 C
ATOM 2077 NH1 ARG A 333 23.620 31.378 -37.077 1.00124.08 N
ANISOU 2077 NH1 ARG A 333 14970 15239 16936 -3208 786 285 N
ATOM 2078 NH2 ARG A 333 25.532 30.149 -36.752 1.00135.63 N
ANISOU 2078 NH2 ARG A 333 15787 17169 18577 -3239 709 500 N
ATOM 2079 N GLU A 334 20.405 27.221 -42.509 1.00 65.14 N
ANISOU 2079 N GLU A 334 7781 7833 9137 -1584 1369 363 N
ATOM 2080 CA GLU A 334 19.142 27.468 -43.192 1.00 57.99 C
ANISOU 2080 CA GLU A 334 7167 6728 8138 -1402 1335 306 C
ATOM 2081 C GLU A 334 18.427 26.154 -43.478 1.00 60.92 C
ANISOU 2081 C GLU A 334 7575 7167 8407 -1149 1244 258 C
ATOM 2082 O GLU A 334 17.205 26.052 -43.305 1.00 54.69 O
ANISOU 2082 O GLU A 334 6900 6290 7589 -1055 1102 162 O
ATOM 2083 CB GLU A 334 19.373 28.260 -44.476 1.00 53.50 C
ANISOU 2083 CB GLU A 334 6790 6020 7515 -1370 1508 437 C
ATOM 2084 CG GLU A 334 19.910 29.666 -44.234 1.00 70.89 C
ANISOU 2084 CG GLU A 334 9026 8104 9806 -1639 1593 477 C
ATOM 2085 CD GLU A 334 19.138 30.409 -43.146 1.00 72.18 C
ANISOU 2085 CD GLU A 334 9289 8122 10015 -1764 1460 333 C
ATOM 2086 OE1 GLU A 334 17.942 30.107 -42.936 1.00 72.17 O
ANISOU 2086 OE1 GLU A 334 9387 8060 9976 -1584 1341 234 O
ATOM 2087 OE2 GLU A 334 19.726 31.303 -42.500 1.00 73.93 O
ANISOU 2087 OE2 GLU A 334 9504 8283 10304 -2050 1482 330 O
ATOM 2088 N ALA A 335 19.170 25.137 -43.932 1.00 68.26 N
ANISOU 2088 N ALA A 335 8416 8245 9276 -1038 1336 340 N
ATOM 2089 CA ALA A 335 18.557 23.832 -44.169 1.00 73.01 C
ANISOU 2089 CA ALA A 335 9101 8886 9752 -827 1253 289 C
ATOM 2090 C ALA A 335 18.040 23.234 -42.867 1.00 79.78 C
ANISOU 2090 C ALA A 335 9816 9827 10671 -869 1073 145 C
ATOM 2091 O ALA A 335 17.035 22.511 -42.868 1.00 80.90 O
ANISOU 2091 O ALA A 335 10064 9935 10738 -753 938 64 O
ATOM 2092 CB ALA A 335 19.551 22.891 -44.848 1.00 73.43 C
ANISOU 2092 CB ALA A 335 9132 9055 9713 -684 1434 416 C
ATOM 2093 N VAL A 336 18.709 23.532 -41.751 1.00 80.70 N
ANISOU 2093 N VAL A 336 9702 10047 10915 -1050 1060 122 N
ATOM 2094 CA VAL A 336 18.282 23.023 -40.453 1.00 66.67 C
ANISOU 2094 CA VAL A 336 7814 8335 9183 -1094 905 -11 C
ATOM 2095 C VAL A 336 17.120 23.857 -39.929 1.00 60.32 C
ANISOU 2095 C VAL A 336 7135 7359 8425 -1156 795 -124 C
ATOM 2096 O VAL A 336 16.123 23.317 -39.437 1.00 59.90 O
ANISOU 2096 O VAL A 336 7114 7285 8360 -1073 679 -221 O
ATOM 2097 CB VAL A 336 19.457 23.002 -39.458 1.00 66.58 C
ANISOU 2097 CB VAL A 336 7535 8500 9264 -1268 910 21 C
ATOM 2098 CG1 VAL A 336 19.006 22.418 -38.121 1.00 66.99 C
ANISOU 2098 CG1 VAL A 336 7515 8605 9332 -1296 752 -118 C
ATOM 2099 CG2 VAL A 336 20.623 22.216 -40.026 1.00 77.58 C
ANISOU 2099 CG2 VAL A 336 8769 10076 10632 -1164 1057 182 C
ATOM 2100 N TYR A 337 17.236 25.189 -40.019 1.00 60.02 N
ANISOU 2100 N TYR A 337 7178 7189 8440 -1294 853 -96 N
ATOM 2101 CA TYR A 337 16.090 26.042 -39.708 1.00 54.61 C
ANISOU 2101 CA TYR A 337 6660 6309 7782 -1290 802 -169 C
ATOM 2102 C TYR A 337 14.881 25.648 -40.549 1.00 54.67 C
ANISOU 2102 C TYR A 337 6793 6252 7727 -1062 744 -154 C
ATOM 2103 O TYR A 337 13.769 25.486 -40.033 1.00 61.98 O
ANISOU 2103 O TYR A 337 7734 7133 8680 -984 647 -218 O
ATOM 2104 CB TYR A 337 16.412 27.510 -39.988 1.00 58.38 C
ANISOU 2104 CB TYR A 337 7277 6618 8288 -1434 909 -115 C
ATOM 2105 CG TYR A 337 17.443 28.189 -39.121 1.00 64.18 C
ANISOU 2105 CG TYR A 337 7942 7363 9080 -1728 932 -127 C
ATOM 2106 CD1 TYR A 337 17.893 27.629 -37.937 1.00 68.13 C
ANISOU 2106 CD1 TYR A 337 8275 8003 9610 -1853 831 -198 C
ATOM 2107 CD2 TYR A 337 17.939 29.434 -39.489 1.00 75.22 C
ANISOU 2107 CD2 TYR A 337 9473 8617 10492 -1901 1039 -59 C
ATOM 2108 CE1 TYR A 337 18.832 28.285 -37.158 1.00 75.07 C
ANISOU 2108 CE1 TYR A 337 9106 8892 10526 -2161 808 -195 C
ATOM 2109 CE2 TYR A 337 18.868 30.096 -38.722 1.00 81.51 C
ANISOU 2109 CE2 TYR A 337 10230 9410 11331 -2222 1030 -60 C
ATOM 2110 CZ TYR A 337 19.313 29.520 -37.555 1.00 84.06 C
ANISOU 2110 CZ TYR A 337 10375 9887 11679 -2361 899 -126 C
ATOM 2111 OH TYR A 337 20.237 30.189 -36.785 1.00 98.12 O
ANISOU 2111 OH TYR A 337 12127 11671 13483 -2703 840 -114 O
ATOM 2112 N ALA A 338 15.094 25.477 -41.855 1.00 55.97 N
ANISOU 2112 N ALA A 338 7050 6415 7802 -962 800 -52 N
ATOM 2113 CA ALA A 338 14.039 25.035 -42.761 1.00 52.38 C
ANISOU 2113 CA ALA A 338 6737 5910 7257 -779 704 -21 C
ATOM 2114 C ALA A 338 13.462 23.693 -42.337 1.00 50.30 C
ANISOU 2114 C ALA A 338 6395 5755 6960 -706 561 -93 C
ATOM 2115 O ALA A 338 12.238 23.510 -42.306 1.00 46.49 O
ANISOU 2115 O ALA A 338 5940 5236 6487 -632 421 -107 O
ATOM 2116 CB ALA A 338 14.588 24.953 -44.184 1.00 53.70 C
ANISOU 2116 CB ALA A 338 7058 6053 7291 -701 800 95 C
ATOM 2117 N ALA A 339 14.338 22.723 -42.065 1.00 56.35 N
ANISOU 2117 N ALA A 339 7062 6660 7688 -720 601 -115 N
ATOM 2118 CA ALA A 339 13.899 21.395 -41.650 1.00 52.41 C
ANISOU 2118 CA ALA A 339 6526 6250 7140 -657 489 -185 C
ATOM 2119 C ALA A 339 12.978 21.482 -40.440 1.00 64.68 C
ANISOU 2119 C ALA A 339 7970 7795 8811 -703 379 -282 C
ATOM 2120 O ALA A 339 11.858 20.952 -40.448 1.00 72.70 O
ANISOU 2120 O ALA A 339 9013 8795 9816 -643 245 -301 O
ATOM 2121 CB ALA A 339 15.117 20.520 -41.345 1.00 28.71 C
ANISOU 2121 CB ALA A 339 3416 3393 4098 -655 589 -179 C
ATOM 2122 N PHE A 340 13.442 22.147 -39.378 1.00 64.63 N
ANISOU 2122 N PHE A 340 7850 7794 8912 -822 436 -334 N
ATOM 2123 CA PHE A 340 12.620 22.261 -38.175 1.00 54.97 C
ANISOU 2123 CA PHE A 340 6569 6537 7780 -849 373 -424 C
ATOM 2124 C PHE A 340 11.355 23.083 -38.432 1.00 63.33 C
ANISOU 2124 C PHE A 340 7711 7453 8899 -775 345 -384 C
ATOM 2125 O PHE A 340 10.302 22.810 -37.845 1.00 75.65 O
ANISOU 2125 O PHE A 340 9225 9001 10519 -717 280 -410 O
ATOM 2126 CB PHE A 340 13.434 22.858 -37.022 1.00 50.62 C
ANISOU 2126 CB PHE A 340 5951 5992 7289 -1009 432 -485 C
ATOM 2127 CG PHE A 340 14.408 21.895 -36.391 1.00 68.92 C
ANISOU 2127 CG PHE A 340 8129 8483 9576 -1061 416 -520 C
ATOM 2128 CD1 PHE A 340 14.002 21.035 -35.377 1.00 70.85 C
ANISOU 2128 CD1 PHE A 340 8318 8782 9820 -1035 345 -610 C
ATOM 2129 CD2 PHE A 340 15.731 21.861 -36.804 1.00 74.46 C
ANISOU 2129 CD2 PHE A 340 8743 9294 10253 -1123 485 -440 C
ATOM 2130 CE1 PHE A 340 14.898 20.154 -34.794 1.00 69.20 C
ANISOU 2130 CE1 PHE A 340 7990 8731 9573 -1059 330 -627 C
ATOM 2131 CE2 PHE A 340 16.639 20.982 -36.228 1.00 71.76 C
ANISOU 2131 CE2 PHE A 340 8243 9131 9892 -1140 476 -436 C
ATOM 2132 CZ PHE A 340 16.221 20.126 -35.219 1.00 72.25 C
ANISOU 2132 CZ PHE A 340 8271 9241 9939 -1104 391 -533 C
ATOM 2133 N THR A 341 11.445 24.123 -39.266 1.00 65.14 N
ANISOU 2133 N THR A 341 8054 7574 9121 -766 410 -301 N
ATOM 2134 CA THR A 341 10.293 24.997 -39.473 1.00 54.20 C
ANISOU 2134 CA THR A 341 6744 6052 7796 -668 402 -236 C
ATOM 2135 C THR A 341 9.122 24.245 -40.104 1.00 62.21 C
ANISOU 2135 C THR A 341 7724 7119 8795 -537 242 -167 C
ATOM 2136 O THR A 341 7.977 24.364 -39.647 1.00 59.01 O
ANISOU 2136 O THR A 341 7246 6688 8487 -457 197 -134 O
ATOM 2137 CB THR A 341 10.704 26.205 -40.316 1.00 46.57 C
ANISOU 2137 CB THR A 341 5936 4956 6804 -678 509 -153 C
ATOM 2138 OG1 THR A 341 11.704 26.967 -39.625 1.00 49.90 O
ANISOU 2138 OG1 THR A 341 6390 5318 7251 -849 637 -210 O
ATOM 2139 CG2 THR A 341 9.495 27.082 -40.622 1.00 46.46 C
ANISOU 2139 CG2 THR A 341 6007 4804 6842 -532 508 -57 C
ATOM 2140 N PHE A 342 9.392 23.432 -41.124 1.00 67.95 N
ANISOU 2140 N PHE A 342 8509 7915 9393 -522 157 -133 N
ATOM 2141 CA PHE A 342 8.322 22.617 -41.686 1.00 59.34 C
ANISOU 2141 CA PHE A 342 7414 6872 8261 -457 -38 -74 C
ATOM 2142 C PHE A 342 7.812 21.610 -40.659 1.00 58.50 C
ANISOU 2142 C PHE A 342 7154 6858 8216 -488 -114 -152 C
ATOM 2143 O PHE A 342 6.611 21.318 -40.600 1.00 60.81 O
ANISOU 2143 O PHE A 342 7356 7176 8573 -454 -252 -90 O
ATOM 2144 CB PHE A 342 8.799 21.927 -42.959 1.00 60.12 C
ANISOU 2144 CB PHE A 342 7694 6986 8162 -450 -100 -36 C
ATOM 2145 CG PHE A 342 7.834 20.931 -43.486 1.00 55.98 C
ANISOU 2145 CG PHE A 342 7214 6503 7552 -443 -331 7 C
ATOM 2146 CD1 PHE A 342 6.739 21.331 -44.238 1.00 52.15 C
ANISOU 2146 CD1 PHE A 342 6759 5985 7070 -396 -504 140 C
ATOM 2147 CD2 PHE A 342 8.014 19.585 -43.223 1.00 49.49 C
ANISOU 2147 CD2 PHE A 342 6411 5751 6640 -495 -389 -74 C
ATOM 2148 CE1 PHE A 342 5.841 20.402 -44.723 1.00 46.41 C
ANISOU 2148 CE1 PHE A 342 6068 5306 6261 -441 -760 195 C
ATOM 2149 CE2 PHE A 342 7.129 18.653 -43.700 1.00 51.42 C
ANISOU 2149 CE2 PHE A 342 6733 6013 6789 -534 -617 -37 C
ATOM 2150 CZ PHE A 342 6.038 19.058 -44.453 1.00 49.64 C
ANISOU 2150 CZ PHE A 342 6524 5766 6570 -527 -819 98 C
ATOM 2151 N SER A 343 8.715 21.067 -39.842 1.00 59.66 N
ANISOU 2151 N SER A 343 7258 7063 8348 -556 -28 -270 N
ATOM 2152 CA SER A 343 8.300 20.121 -38.816 1.00 57.64 C
ANISOU 2152 CA SER A 343 6884 6879 8137 -581 -79 -348 C
ATOM 2153 C SER A 343 7.330 20.773 -37.838 1.00 57.30 C
ANISOU 2153 C SER A 343 6720 6787 8263 -548 -45 -338 C
ATOM 2154 O SER A 343 6.339 20.156 -37.431 1.00 63.84 O
ANISOU 2154 O SER A 343 7443 7656 9158 -529 -130 -318 O
ATOM 2155 CB SER A 343 9.531 19.583 -38.092 1.00 56.87 C
ANISOU 2155 CB SER A 343 6767 6851 7990 -641 18 -456 C
ATOM 2156 OG SER A 343 10.444 19.044 -39.031 1.00 60.60 O
ANISOU 2156 OG SER A 343 7350 7363 8313 -629 38 -432 O
ATOM 2157 N HIS A 344 7.586 22.030 -37.464 1.00 62.28 N
ANISOU 2157 N HIS A 344 7386 7316 8963 -538 95 -338 N
ATOM 2158 CA HIS A 344 6.673 22.726 -36.564 1.00 57.40 C
ANISOU 2158 CA HIS A 344 6716 6612 8484 -468 177 -314 C
ATOM 2159 C HIS A 344 5.334 22.999 -37.229 1.00 63.30 C
ANISOU 2159 C HIS A 344 7388 7348 9316 -337 97 -145 C
ATOM 2160 O HIS A 344 4.280 22.844 -36.601 1.00 69.10 O
ANISOU 2160 O HIS A 344 7985 8098 10173 -261 101 -87 O
ATOM 2161 CB HIS A 344 7.296 24.039 -36.087 1.00 51.97 C
ANISOU 2161 CB HIS A 344 6163 5776 7807 -500 352 -351 C
ATOM 2162 CG HIS A 344 8.641 23.884 -35.456 1.00 56.00 C
ANISOU 2162 CG HIS A 344 6718 6315 8243 -662 396 -483 C
ATOM 2163 ND1 HIS A 344 9.496 24.949 -35.254 1.00 56.16 N
ANISOU 2163 ND1 HIS A 344 6872 6226 8239 -771 502 -514 N
ATOM 2164 CD2 HIS A 344 9.284 22.789 -34.993 1.00 57.64 C
ANISOU 2164 CD2 HIS A 344 6846 6657 8396 -739 336 -572 C
ATOM 2165 CE1 HIS A 344 10.605 24.513 -34.684 1.00 58.68 C
ANISOU 2165 CE1 HIS A 344 7157 6634 8505 -923 485 -604 C
ATOM 2166 NE2 HIS A 344 10.502 23.207 -34.517 1.00 55.75 N
ANISOU 2166 NE2 HIS A 344 6655 6413 8115 -885 393 -638 N
ATOM 2167 N TRP A 345 5.356 23.399 -38.498 1.00 66.16 N
ANISOU 2167 N TRP A 345 7829 7693 9617 -304 25 -45 N
ATOM 2168 CA TRP A 345 4.111 23.661 -39.201 1.00 60.91 C
ANISOU 2168 CA TRP A 345 7080 7040 9024 -183 -91 143 C
ATOM 2169 C TRP A 345 3.308 22.380 -39.388 1.00 61.91 C
ANISOU 2169 C TRP A 345 7054 7311 9156 -232 -315 191 C
ATOM 2170 O TRP A 345 2.072 22.425 -39.405 1.00 73.91 O
ANISOU 2170 O TRP A 345 8395 8881 10807 -154 -405 352 O
ATOM 2171 CB TRP A 345 4.397 24.341 -40.538 1.00 55.19 C
ANISOU 2171 CB TRP A 345 6515 6255 8198 -147 -131 235 C
ATOM 2172 CG TRP A 345 3.192 24.465 -41.413 1.00 54.36 C
ANISOU 2172 CG TRP A 345 6329 6192 8134 -40 -313 444 C
ATOM 2173 CD1 TRP A 345 2.293 25.493 -41.440 1.00 60.04 C
ANISOU 2173 CD1 TRP A 345 6978 6852 8981 136 -256 618 C
ATOM 2174 CD2 TRP A 345 2.755 23.528 -42.398 1.00 51.31 C
ANISOU 2174 CD2 TRP A 345 5935 5915 7647 -105 -593 519 C
ATOM 2175 NE1 TRP A 345 1.322 25.251 -42.379 1.00 60.62 N
ANISOU 2175 NE1 TRP A 345 6951 7023 9060 184 -504 814 N
ATOM 2176 CE2 TRP A 345 1.584 24.050 -42.981 1.00 50.28 C
ANISOU 2176 CE2 TRP A 345 5694 5811 7601 15 -730 749 C
ATOM 2177 CE3 TRP A 345 3.238 22.294 -42.844 1.00 54.28 C
ANISOU 2177 CE3 TRP A 345 6416 6355 7853 -251 -741 425 C
ATOM 2178 CZ2 TRP A 345 0.891 23.386 -43.982 1.00 46.38 C
ANISOU 2178 CZ2 TRP A 345 5181 5417 7025 -47 -1049 882 C
ATOM 2179 CZ3 TRP A 345 2.548 21.635 -43.842 1.00 48.83 C
ANISOU 2179 CZ3 TRP A 345 5764 5729 7060 -307 -1030 540 C
ATOM 2180 CH2 TRP A 345 1.387 22.182 -44.400 1.00 42.61 C
ANISOU 2180 CH2 TRP A 345 4855 4978 6358 -225 -1202 764 C
ATOM 2181 N LEU A 346 3.987 21.241 -39.560 1.00 53.80 N
ANISOU 2181 N LEU A 346 6102 6352 7989 -361 -404 74 N
ATOM 2182 CA LEU A 346 3.273 19.982 -39.725 1.00 55.01 C
ANISOU 2182 CA LEU A 346 6174 6611 8117 -442 -617 105 C
ATOM 2183 C LEU A 346 2.435 19.658 -38.502 1.00 59.12 C
ANISOU 2183 C LEU A 346 6469 7179 8815 -432 -573 114 C
ATOM 2184 O LEU A 346 1.360 19.061 -38.630 1.00 67.46 O
ANISOU 2184 O LEU A 346 7369 8321 9943 -472 -745 233 O
ATOM 2185 CB LEU A 346 4.259 18.844 -39.995 1.00 55.15 C
ANISOU 2185 CB LEU A 346 6371 6652 7932 -553 -657 -34 C
ATOM 2186 CG LEU A 346 4.381 18.375 -41.441 1.00 48.10 C
ANISOU 2186 CG LEU A 346 5696 5748 6833 -599 -836 21 C
ATOM 2187 CD1 LEU A 346 5.220 17.110 -41.472 1.00 45.55 C
ANISOU 2187 CD1 LEU A 346 5554 5434 6319 -675 -829 -108 C
ATOM 2188 CD2 LEU A 346 2.989 18.083 -42.035 1.00 45.20 C
ANISOU 2188 CD2 LEU A 346 5245 5432 6497 -651 -1117 184 C
ATOM 2189 N VAL A 347 2.915 20.033 -37.314 1.00 59.77 N
ANISOU 2189 N VAL A 347 6543 7205 8960 -395 -348 -1 N
ATOM 2190 CA VAL A 347 2.160 19.778 -36.094 1.00 61.44 C
ANISOU 2190 CA VAL A 347 6585 7436 9325 -363 -260 5 C
ATOM 2191 C VAL A 347 0.815 20.482 -36.161 1.00 67.45 C
ANISOU 2191 C VAL A 347 7146 8203 10279 -225 -253 228 C
ATOM 2192 O VAL A 347 -0.241 19.875 -35.960 1.00 57.63 O
ANISOU 2192 O VAL A 347 5684 7055 9157 -236 -344 349 O
ATOM 2193 CB VAL A 347 2.956 20.235 -34.862 1.00 59.73 C
ANISOU 2193 CB VAL A 347 6464 7124 9105 -343 -22 -151 C
ATOM 2194 CG1 VAL A 347 2.081 20.146 -33.625 1.00 60.94 C
ANISOU 2194 CG1 VAL A 347 6486 7261 9407 -272 108 -123 C
ATOM 2195 CG2 VAL A 347 4.238 19.435 -34.720 1.00 66.90 C
ANISOU 2195 CG2 VAL A 347 7503 8069 9848 -468 -44 -331 C
ATOM 2196 N TYR A 348 0.834 21.787 -36.423 1.00 81.91 N
ANISOU 2196 N TYR A 348 9041 9932 12148 -86 -131 303 N
ATOM 2197 CA TYR A 348 -0.425 22.510 -36.515 1.00 74.69 C
ANISOU 2197 CA TYR A 348 7935 9025 11420 95 -97 548 C
ATOM 2198 C TYR A 348 -1.231 22.086 -37.735 1.00 68.92 C
ANISOU 2198 C TYR A 348 7045 8438 10703 54 -404 746 C
ATOM 2199 O TYR A 348 -2.462 22.205 -37.729 1.00 73.24 O
ANISOU 2199 O TYR A 348 7320 9074 11435 156 -453 984 O
ATOM 2200 CB TYR A 348 -0.184 24.016 -36.524 1.00 71.24 C
ANISOU 2200 CB TYR A 348 7660 8415 10993 267 123 584 C
ATOM 2201 CG TYR A 348 0.624 24.490 -35.354 1.00 64.17 C
ANISOU 2201 CG TYR A 348 6972 7357 10053 263 391 392 C
ATOM 2202 CD1 TYR A 348 0.101 24.480 -34.069 1.00 61.53 C
ANISOU 2202 CD1 TYR A 348 6583 6970 9826 352 590 389 C
ATOM 2203 CD2 TYR A 348 1.918 24.939 -35.536 1.00 60.43 C
ANISOU 2203 CD2 TYR A 348 6758 6781 9420 154 437 226 C
ATOM 2204 CE1 TYR A 348 0.855 24.919 -32.992 1.00 61.62 C
ANISOU 2204 CE1 TYR A 348 6840 6815 9759 324 806 208 C
ATOM 2205 CE2 TYR A 348 2.673 25.375 -34.480 1.00 62.11 C
ANISOU 2205 CE2 TYR A 348 7166 6854 9580 104 632 62 C
ATOM 2206 CZ TYR A 348 2.141 25.364 -33.211 1.00 69.93 C
ANISOU 2206 CZ TYR A 348 8143 7778 10649 184 804 46 C
ATOM 2207 OH TYR A 348 2.908 25.802 -32.160 1.00 82.79 O
ANISOU 2207 OH TYR A 348 10018 9251 12189 110 970 -121 O
ATOM 2208 N ALA A 349 -0.571 21.583 -38.783 1.00 62.67 N
ANISOU 2208 N ALA A 349 6425 7673 9715 -93 -614 671 N
ATOM 2209 CA ALA A 349 -1.317 21.061 -39.923 1.00 58.22 C
ANISOU 2209 CA ALA A 349 5773 7229 9117 -176 -945 843 C
ATOM 2210 C ALA A 349 -2.207 19.892 -39.519 1.00 60.49 C
ANISOU 2210 C ALA A 349 5825 7659 9500 -315 -1114 909 C
ATOM 2211 O ALA A 349 -3.269 19.681 -40.117 1.00 68.59 O
ANISOU 2211 O ALA A 349 6645 8809 10607 -360 -1367 1138 O
ATOM 2212 CB ALA A 349 -0.353 20.642 -41.035 1.00 60.94 C
ANISOU 2212 CB ALA A 349 6428 7537 9190 -308 -1098 724 C
ATOM 2213 N ASN A 350 -1.778 19.107 -38.530 1.00 63.78 N
ANISOU 2213 N ASN A 350 6270 8062 9901 -402 -995 724 N
ATOM 2214 CA ASN A 350 -2.613 18.030 -38.009 1.00 61.46 C
ANISOU 2214 CA ASN A 350 5763 7881 9708 -534 -1108 784 C
ATOM 2215 C ASN A 350 -3.877 18.580 -37.372 1.00 67.42 C
ANISOU 2215 C ASN A 350 6147 8710 10761 -382 -1004 1029 C
ATOM 2216 O ASN A 350 -4.928 17.930 -37.409 1.00 72.43 O
ANISOU 2216 O ASN A 350 6508 9485 11526 -490 -1185 1213 O
ATOM 2217 CB ASN A 350 -1.823 17.209 -36.986 1.00 49.21 C
ANISOU 2217 CB ASN A 350 4348 6276 8074 -612 -950 535 C
ATOM 2218 CG ASN A 350 -2.668 16.142 -36.303 1.00 49.83 C
ANISOU 2218 CG ASN A 350 4225 6445 8263 -739 -1012 588 C
ATOM 2219 OD1 ASN A 350 -2.916 15.077 -36.869 1.00 65.54 O
ANISOU 2219 OD1 ASN A 350 6256 8494 10151 -954 -1272 603 O
ATOM 2220 ND2 ASN A 350 -3.102 16.417 -35.077 1.00 50.33 N
ANISOU 2220 ND2 ASN A 350 4109 6497 8516 -615 -761 618 N
ATOM 2221 N SER A 351 -3.793 19.766 -36.766 1.00 76.28 N
ANISOU 2221 N SER A 351 7264 9729 11989 -135 -697 1048 N
ATOM 2222 CA SER A 351 -4.984 20.362 -36.175 1.00 77.92 C
ANISOU 2222 CA SER A 351 7147 9986 12474 70 -539 1307 C
ATOM 2223 C SER A 351 -5.969 20.782 -37.252 1.00 67.99 C
ANISOU 2223 C SER A 351 5644 8862 11327 130 -774 1630 C
ATOM 2224 O SER A 351 -7.167 20.505 -37.145 1.00 65.26 O
ANISOU 2224 O SER A 351 4916 8679 11201 138 -864 1901 O
ATOM 2225 CB SER A 351 -4.601 21.546 -35.291 1.00 88.88 C
ANISOU 2225 CB SER A 351 8686 11184 13900 326 -136 1239 C
ATOM 2226 OG SER A 351 -3.755 21.098 -34.243 1.00 98.37 O
ANISOU 2226 OG SER A 351 10095 12283 14999 245 38 963 O
ATOM 2227 N ALA A 352 -5.480 21.424 -38.313 1.00 77.93 N
ANISOU 2227 N ALA A 352 7106 10065 12437 163 -887 1623 N
ATOM 2228 CA ALA A 352 -6.352 21.736 -39.435 1.00 86.11 C
ANISOU 2228 CA ALA A 352 7946 11234 13536 197 -1166 1925 C
ATOM 2229 C ALA A 352 -6.710 20.501 -40.254 1.00 88.41 C
ANISOU 2229 C ALA A 352 8169 11687 13734 -126 -1616 1974 C
ATOM 2230 O ALA A 352 -7.728 20.515 -40.954 1.00 86.73 O
ANISOU 2230 O ALA A 352 7732 11628 13595 -153 -1872 2252 O
ATOM 2231 CB ALA A 352 -5.696 22.798 -40.322 1.00 84.02 C
ANISOU 2231 CB ALA A 352 7969 10839 13118 332 -1139 1898 C
ATOM 2232 N ALA A 353 -5.905 19.436 -40.177 1.00 82.20 N
ANISOU 2232 N ALA A 353 7640 10849 12742 -372 -1692 1697 N
ATOM 2233 CA ALA A 353 -6.177 18.247 -40.973 1.00 67.63 C
ANISOU 2233 CA ALA A 353 5837 9105 10756 -692 -2104 1721 C
ATOM 2234 C ALA A 353 -7.360 17.458 -40.422 1.00 80.82 C
ANISOU 2234 C ALA A 353 7291 10895 12520 -799 -2109 1827 C
ATOM 2235 O ALA A 353 -8.201 16.975 -41.189 1.00 94.05 O
ANISOU 2235 O ALA A 353 8940 12669 14126 -961 -2383 1973 O
ATOM 2236 CB ALA A 353 -4.927 17.369 -41.044 1.00 56.46 C
ANISOU 2236 CB ALA A 353 4855 7557 9041 -867 -2094 1379 C
ATOM 2237 N ASN A 354 -7.443 17.320 -39.098 1.00 79.19 N
ANISOU 2237 N ASN A 354 6957 10670 12463 -713 -1805 1758 N
ATOM 2238 CA ASN A 354 -8.448 16.438 -38.505 1.00 76.28 C
ANISOU 2238 CA ASN A 354 6432 10395 12158 -830 -1798 1829 C
ATOM 2239 C ASN A 354 -9.873 16.832 -38.860 1.00 93.11 C
ANISOU 2239 C ASN A 354 8247 12676 14454 -772 -1894 2167 C
ATOM 2240 O ASN A 354 -10.642 15.955 -39.295 1.00107.43 O
ANISOU 2240 O ASN A 354 10019 14585 16214 -1005 -2140 2258 O
ATOM 2241 CB ASN A 354 -8.256 16.372 -36.987 1.00 65.91 C
ANISOU 2241 CB ASN A 354 5057 9016 10968 -708 -1428 1709 C
ATOM 2242 CG ASN A 354 -6.937 15.740 -36.597 1.00 57.85 C
ANISOU 2242 CG ASN A 354 4338 7869 9772 -814 -1363 1381 C
ATOM 2243 OD1 ASN A 354 -6.492 14.784 -37.233 1.00 47.54 O
ANISOU 2243 OD1 ASN A 354 3278 6548 8236 -1046 -1591 1244 O
ATOM 2244 ND2 ASN A 354 -6.309 16.262 -35.551 1.00 66.75 N
ANISOU 2244 ND2 ASN A 354 5477 8892 10994 -639 -1039 1259 N
ATOM 2245 N PRO A 355 -10.295 18.088 -38.703 1.00 94.33 N
ANISOU 2245 N PRO A 355 8185 12851 14807 -474 -1705 2370 N
ATOM 2246 CA PRO A 355 -11.681 18.422 -39.050 1.00 89.40 C
ANISOU 2246 CA PRO A 355 7247 12382 14337 -416 -1793 2712 C
ATOM 2247 C PRO A 355 -12.006 18.123 -40.497 1.00 85.70 C
ANISOU 2247 C PRO A 355 6832 12007 13723 -634 -2231 2822 C
ATOM 2248 O PRO A 355 -13.129 17.704 -40.800 1.00 84.23 O
ANISOU 2248 O PRO A 355 6436 11966 13603 -769 -2418 3041 O
ATOM 2249 CB PRO A 355 -11.776 19.930 -38.752 1.00 96.11 C
ANISOU 2249 CB PRO A 355 7971 13186 15361 -19 -1486 2868 C
ATOM 2250 CG PRO A 355 -10.612 20.228 -37.843 1.00101.60 C
ANISOU 2250 CG PRO A 355 8875 13692 16036 118 -1165 2602 C
ATOM 2251 CD PRO A 355 -9.539 19.255 -38.221 1.00 99.15 C
ANISOU 2251 CD PRO A 355 8845 13328 15498 -172 -1391 2308 C
ATOM 2252 N ILE A 356 -11.039 18.310 -41.401 1.00 87.70 N
ANISOU 2252 N ILE A 356 7377 12173 13772 -681 -2403 2681 N
ATOM 2253 CA ILE A 356 -11.248 17.927 -42.790 1.00 86.53 C
ANISOU 2253 CA ILE A 356 7374 12075 13427 -910 -2822 2750 C
ATOM 2254 C ILE A 356 -11.408 16.417 -42.900 1.00 95.25 C
ANISOU 2254 C ILE A 356 8640 13184 14368 -1275 -3036 2633 C
ATOM 2255 O ILE A 356 -12.143 15.914 -43.759 1.00103.10 O
ANISOU 2255 O ILE A 356 9636 14257 15279 -1495 -3356 2776 O
ATOM 2256 CB ILE A 356 -10.090 18.438 -43.666 1.00 76.78 C
ANISOU 2256 CB ILE A 356 6472 10715 11984 -866 -2925 2612 C
ATOM 2257 CG1 ILE A 356 -9.990 19.962 -43.538 1.00 61.44 C
ANISOU 2257 CG1 ILE A 356 4379 8752 10214 -485 -2695 2752 C
ATOM 2258 CG2 ILE A 356 -10.314 17.988 -45.110 1.00 78.76 C
ANISOU 2258 CG2 ILE A 356 6943 10991 11992 -1109 -3349 2673 C
ATOM 2259 CD1 ILE A 356 -8.772 20.600 -44.191 1.00 58.87 C
ANISOU 2259 CD1 ILE A 356 4361 8281 9726 -389 -2728 2629 C
ATOM 2260 N ILE A 357 -10.705 15.668 -42.051 1.00 95.50 N
ANISOU 2260 N ILE A 357 8833 13116 14336 -1343 -2862 2373 N
ATOM 2261 CA ILE A 357 -10.835 14.216 -42.082 1.00 94.41 C
ANISOU 2261 CA ILE A 357 8879 12959 14035 -1659 -3022 2259 C
ATOM 2262 C ILE A 357 -12.253 13.793 -41.735 1.00 94.03 C
ANISOU 2262 C ILE A 357 8488 13063 14177 -1757 -3079 2504 C
ATOM 2263 O ILE A 357 -12.788 12.841 -42.317 1.00101.10 O
ANISOU 2263 O ILE A 357 9472 13988 14952 -2048 -3358 2559 O
ATOM 2264 CB ILE A 357 -9.809 13.566 -41.139 1.00 90.74 C
ANISOU 2264 CB ILE A 357 8632 12363 13481 -1666 -2785 1946 C
ATOM 2265 CG1 ILE A 357 -8.391 13.910 -41.581 1.00 90.23 C
ANISOU 2265 CG1 ILE A 357 8908 12157 13220 -1603 -2762 1724 C
ATOM 2266 CG2 ILE A 357 -10.003 12.066 -41.104 1.00 84.95 C
ANISOU 2266 CG2 ILE A 357 8089 11600 12587 -1959 -2915 1847 C
ATOM 2267 CD1 ILE A 357 -7.348 13.479 -40.595 1.00 86.61 C
ANISOU 2267 CD1 ILE A 357 8612 11587 12710 -1568 -2501 1442 C
ATOM 2268 N TYR A 358 -12.870 14.471 -40.765 1.00 83.33 N
ANISOU 2268 N TYR A 358 6757 11792 13112 -1520 -2802 2661 N
ATOM 2269 CA TYR A 358 -14.222 14.117 -40.352 1.00 81.23 C
ANISOU 2269 CA TYR A 358 6137 11677 13051 -1590 -2821 2918 C
ATOM 2270 C TYR A 358 -15.231 14.380 -41.464 1.00 90.02 C
ANISOU 2270 C TYR A 358 7061 12939 14202 -1689 -3150 3232 C
ATOM 2271 O TYR A 358 -16.176 13.602 -41.653 1.00 98.39 O
ANISOU 2271 O TYR A 358 7981 14106 15296 -1936 -3364 3398 O
ATOM 2272 CB TYR A 358 -14.610 14.902 -39.096 1.00 78.64 C
ANISOU 2272 CB TYR A 358 5490 11380 13008 -1268 -2411 3030 C
ATOM 2273 CG TYR A 358 -13.633 14.811 -37.936 1.00 72.22 C
ANISOU 2273 CG TYR A 358 4853 10417 12172 -1142 -2068 2740 C
ATOM 2274 CD1 TYR A 358 -12.824 13.694 -37.757 1.00 63.79 C
ANISOU 2274 CD1 TYR A 358 4099 9246 10893 -1361 -2120 2441 C
ATOM 2275 CD2 TYR A 358 -13.528 15.846 -37.015 1.00 83.27 C
ANISOU 2275 CD2 TYR A 358 6123 11766 13748 -797 -1681 2776 C
ATOM 2276 CE1 TYR A 358 -11.938 13.618 -36.689 1.00 68.41 C
ANISOU 2276 CE1 TYR A 358 4829 9706 11458 -1249 -1817 2191 C
ATOM 2277 CE2 TYR A 358 -12.645 15.778 -35.947 1.00 82.78 C
ANISOU 2277 CE2 TYR A 358 6234 11561 13659 -697 -1379 2519 C
ATOM 2278 CZ TYR A 358 -11.852 14.661 -35.788 1.00 78.09 C
ANISOU 2278 CZ TYR A 358 5915 10891 12866 -929 -1460 2231 C
ATOM 2279 OH TYR A 358 -10.973 14.589 -34.728 1.00 83.42 O
ANISOU 2279 OH TYR A 358 6750 11434 13511 -836 -1173 1989 O
ATOM 2280 N ASN A 359 -15.046 15.473 -42.207 1.00 88.92 N
ANISOU 2280 N ASN A 359 6916 12811 14059 -1505 -3199 3325 N
ATOM 2281 CA ASN A 359 -16.019 15.843 -43.225 1.00 97.76 C
ANISOU 2281 CA ASN A 359 7833 14082 15228 -1562 -3495 3641 C
ATOM 2282 C ASN A 359 -16.067 14.837 -44.369 1.00100.77 C
ANISOU 2282 C ASN A 359 8494 14448 15345 -1960 -3940 3602 C
ATOM 2283 O ASN A 359 -17.128 14.645 -44.975 1.00108.14 O
ANISOU 2283 O ASN A 359 9225 15528 16334 -2132 -4221 3874 O
ATOM 2284 CB ASN A 359 -15.707 17.244 -43.738 1.00102.95 C
ANISOU 2284 CB ASN A 359 8470 14732 15915 -1252 -3425 3724 C
ATOM 2285 CG ASN A 359 -16.688 17.703 -44.788 1.00114.64 C
ANISOU 2285 CG ASN A 359 9740 16375 17443 -1277 -3721 4055 C
ATOM 2286 OD1 ASN A 359 -17.829 18.047 -44.480 1.00127.15 O
ANISOU 2286 OD1 ASN A 359 10904 18128 19280 -1171 -3660 4371 O
ATOM 2287 ND2 ASN A 359 -16.251 17.710 -46.042 1.00109.03 N
ANISOU 2287 ND2 ASN A 359 9331 15615 16483 -1413 -4041 3994 N
ATOM 2288 N PHE A 360 -14.945 14.189 -44.680 1.00 97.19 N
ANISOU 2288 N PHE A 360 8518 13812 14599 -2109 -4002 3281 N
ATOM 2289 CA PHE A 360 -14.900 13.245 -45.794 1.00103.11 C
ANISOU 2289 CA PHE A 360 9628 14496 15055 -2466 -4388 3229 C
ATOM 2290 C PHE A 360 -15.288 11.828 -45.392 1.00106.04 C
ANISOU 2290 C PHE A 360 10071 14850 15371 -2778 -4468 3178 C
ATOM 2291 O PHE A 360 -15.988 11.144 -46.145 1.00118.04 O
ANISOU 2291 O PHE A 360 11649 16408 16791 -3086 -4807 3320 O
ATOM 2292 CB PHE A 360 -13.500 13.232 -46.409 1.00103.41 C
ANISOU 2292 CB PHE A 360 10190 14323 14777 -2458 -4401 2930 C
ATOM 2293 CG PHE A 360 -13.188 14.451 -47.228 1.00106.95 C
ANISOU 2293 CG PHE A 360 10667 14774 15195 -2249 -4459 3005 C
ATOM 2294 CD1 PHE A 360 -12.268 15.382 -46.777 1.00104.25 C
ANISOU 2294 CD1 PHE A 360 10337 14364 14907 -1939 -4171 2876 C
ATOM 2295 CD2 PHE A 360 -13.821 14.674 -48.436 1.00109.92 C
ANISOU 2295 CD2 PHE A 360 11060 15216 15487 -2365 -4804 3214 C
ATOM 2296 CE1 PHE A 360 -11.977 16.507 -47.516 1.00102.82 C
ANISOU 2296 CE1 PHE A 360 10197 14176 14694 -1738 -4218 2955 C
ATOM 2297 CE2 PHE A 360 -13.534 15.802 -49.182 1.00108.73 C
ANISOU 2297 CE2 PHE A 360 10952 15064 15297 -2154 -4851 3283 C
ATOM 2298 CZ PHE A 360 -12.610 16.719 -48.719 1.00105.74 C
ANISOU 2298 CZ PHE A 360 10595 14612 14970 -1834 -4551 3155 C
ATOM 2299 N LEU A 361 -14.854 11.380 -44.215 1.00 93.80 N
ANISOU 2299 N LEU A 361 8525 13237 13877 -2709 -4165 2984 N
ATOM 2300 CA LEU A 361 -15.025 10.003 -43.768 1.00 90.01 C
ANISOU 2300 CA LEU A 361 8178 12708 13312 -2979 -4200 2887 C
ATOM 2301 C LEU A 361 -16.113 9.871 -42.712 1.00 82.58 C
ANISOU 2301 C LEU A 361 6761 11929 12687 -2958 -4058 3090 C
ATOM 2302 O LEU A 361 -16.218 8.826 -42.061 1.00 82.38 O
ANISOU 2302 O LEU A 361 6797 11867 12639 -3125 -4004 2998 O
ATOM 2303 CB LEU A 361 -13.698 9.459 -43.239 1.00 90.42 C
ANISOU 2303 CB LEU A 361 8627 12561 13166 -2932 -3973 2511 C
ATOM 2304 CG LEU A 361 -12.608 9.388 -44.309 1.00 79.80 C
ANISOU 2304 CG LEU A 361 7803 11039 11481 -2983 -4111 2315 C
ATOM 2305 CD1 LEU A 361 -11.226 9.272 -43.684 1.00 66.98 C
ANISOU 2305 CD1 LEU A 361 6460 9257 9734 -2825 -3817 1985 C
ATOM 2306 CD2 LEU A 361 -12.883 8.214 -45.235 1.00 85.07 C
ANISOU 2306 CD2 LEU A 361 8831 11617 11874 -3351 -4442 2330 C
ATOM 2307 N SER A 362 -16.907 10.918 -42.516 1.00 84.82 N
ANISOU 2307 N SER A 362 6585 12382 13259 -2738 -3974 3372 N
ATOM 2308 CA SER A 362 -18.038 10.892 -41.595 1.00 93.67 C
ANISOU 2308 CA SER A 362 7231 13666 14694 -2694 -3831 3622 C
ATOM 2309 C SER A 362 -19.182 11.630 -42.269 1.00102.40 C
ANISOU 2309 C SER A 362 7945 14977 15987 -2666 -4031 4026 C
ATOM 2310 O SER A 362 -19.130 12.854 -42.413 1.00100.33 O
ANISOU 2310 O SER A 362 7528 14757 15836 -2360 -3906 4133 O
ATOM 2311 CB SER A 362 -17.695 11.535 -40.254 1.00 84.45 C
ANISOU 2311 CB SER A 362 5899 12466 13722 -2335 -3353 3533 C
ATOM 2312 OG SER A 362 -18.826 11.556 -39.408 1.00 88.00 O
ANISOU 2312 OG SER A 362 5905 13062 14469 -2271 -3198 3801 O
ATOM 2313 N GLY A 363 -20.215 10.890 -42.676 1.00 99.11 N
ANISOU 2313 N GLY A 363 7367 14686 15604 -2986 -4340 4263 N
ATOM 2314 CA GLY A 363 -21.328 11.519 -43.360 1.00123.16 C
ANISOU 2314 CA GLY A 363 10026 17944 18824 -2989 -4565 4670 C
ATOM 2315 C GLY A 363 -22.222 12.347 -42.462 1.00119.23 C
ANISOU 2315 C GLY A 363 8970 17622 18710 -2674 -4260 4977 C
ATOM 2316 O GLY A 363 -22.949 13.211 -42.960 1.00111.57 O
ANISOU 2316 O GLY A 363 7677 16816 17898 -2540 -4346 5302 O
ATOM 2317 N LYS A 364 -22.197 12.094 -41.153 1.00111.85 N
ANISOU 2317 N LYS A 364 7929 16650 17919 -2546 -3896 4894 N
ATOM 2318 CA LYS A 364 -22.955 12.909 -40.208 1.00110.52 C
ANISOU 2318 CA LYS A 364 7294 16604 18094 -2204 -3537 5169 C
ATOM 2319 C LYS A 364 -22.250 14.228 -39.894 1.00111.16 C
ANISOU 2319 C LYS A 364 7438 16586 18212 -1747 -3178 5072 C
ATOM 2320 O LYS A 364 -22.909 15.266 -39.770 1.00117.45 O
ANISOU 2320 O LYS A 364 7895 17496 19236 -1445 -3003 5377 O
ATOM 2321 CB LYS A 364 -23.272 12.076 -38.967 1.00107.50 C
ANISOU 2321 CB LYS A 364 6795 16211 17838 -2268 -3304 5137 C
ATOM 2322 CG LYS A 364 -24.021 10.813 -39.384 1.00112.08 C
ANISOU 2322 CG LYS A 364 7310 16895 18382 -2739 -3689 5263 C
ATOM 2323 CD LYS A 364 -24.099 9.721 -38.335 1.00111.37 C
ANISOU 2323 CD LYS A 364 7242 16751 18322 -2895 -3532 5137 C
ATOM 2324 CE LYS A 364 -25.032 8.617 -38.847 1.00118.61 C
ANISOU 2324 CE LYS A 364 8030 17799 19237 -3365 -3938 5348 C
ATOM 2325 NZ LYS A 364 -25.094 7.407 -37.976 1.00121.80 N
ANISOU 2325 NZ LYS A 364 8504 18140 19632 -3585 -3845 5211 N
ATOM 2326 N PHE A 365 -20.920 14.216 -39.751 1.00106.58 N
ANISOU 2326 N PHE A 365 7290 15793 17411 -1687 -3053 4667 N
ATOM 2327 CA PHE A 365 -20.192 15.480 -39.648 1.00108.50 C
ANISOU 2327 CA PHE A 365 7630 15937 17659 -1301 -2779 4578 C
ATOM 2328 C PHE A 365 -20.323 16.300 -40.924 1.00117.00 C
ANISOU 2328 C PHE A 365 8678 17091 18686 -1251 -3037 4747 C
ATOM 2329 O PHE A 365 -20.500 17.522 -40.869 1.00116.27 O
ANISOU 2329 O PHE A 365 8416 17027 18734 -898 -2824 4919 O
ATOM 2330 CB PHE A 365 -18.712 15.239 -39.358 1.00102.56 C
ANISOU 2330 CB PHE A 365 7339 14957 16671 -1295 -2651 4126 C
ATOM 2331 CG PHE A 365 -18.376 15.133 -37.904 1.00103.54 C
ANISOU 2331 CG PHE A 365 7480 14974 16884 -1124 -2228 3965 C
ATOM 2332 CD1 PHE A 365 -18.330 16.267 -37.109 1.00103.30 C
ANISOU 2332 CD1 PHE A 365 7338 14891 17019 -720 -1814 4034 C
ATOM 2333 CD2 PHE A 365 -18.053 13.915 -37.339 1.00 93.02 C
ANISOU 2333 CD2 PHE A 365 6325 13572 15448 -1360 -2234 3735 C
ATOM 2334 CE1 PHE A 365 -17.997 16.179 -35.768 1.00 89.90 C
ANISOU 2334 CE1 PHE A 365 5704 13073 15380 -568 -1427 3880 C
ATOM 2335 CE2 PHE A 365 -17.717 13.822 -35.997 1.00 79.28 C
ANISOU 2335 CE2 PHE A 365 4618 11728 13775 -1203 -1849 3582 C
ATOM 2336 CZ PHE A 365 -17.689 14.956 -35.210 1.00 78.57 C
ANISOU 2336 CZ PHE A 365 4420 11586 13848 -812 -1452 3654 C
ATOM 2337 N ARG A 366 -20.232 15.643 -42.082 1.00120.74 N
ANISOU 2337 N ARG A 366 9352 17581 18942 -1596 -3487 4700 N
ATOM 2338 CA ARG A 366 -20.283 16.355 -43.354 1.00116.01 C
ANISOU 2338 CA ARG A 366 8783 17039 18257 -1571 -3761 4833 C
ATOM 2339 C ARG A 366 -21.578 17.143 -43.494 1.00124.12 C
ANISOU 2339 C ARG A 366 9307 18293 19561 -1398 -3766 5294 C
ATOM 2340 O ARG A 366 -21.572 18.284 -43.972 1.00125.24 O
ANISOU 2340 O ARG A 366 9381 18465 19741 -1121 -3719 5423 O
ATOM 2341 CB ARG A 366 -20.155 15.354 -44.499 1.00112.91 C
ANISOU 2341 CB ARG A 366 8694 16622 17585 -2011 -4248 4740 C
ATOM 2342 CG ARG A 366 -19.928 15.951 -45.873 1.00112.55 C
ANISOU 2342 CG ARG A 366 8825 16575 17364 -2019 -4549 4784 C
ATOM 2343 CD ARG A 366 -20.208 14.884 -46.906 1.00121.85 C
ANISOU 2343 CD ARG A 366 10225 17759 18315 -2483 -5035 4797 C
ATOM 2344 NE ARG A 366 -19.261 13.778 -46.798 1.00120.62 N
ANISOU 2344 NE ARG A 366 10554 17390 17886 -2723 -5054 4427 N
ATOM 2345 CZ ARG A 366 -19.614 12.537 -46.474 1.00122.49 C
ANISOU 2345 CZ ARG A 366 10837 17619 18085 -3043 -5158 4399 C
ATOM 2346 NH1 ARG A 366 -20.887 12.254 -46.223 1.00131.34 N
ANISOU 2346 NH1 ARG A 366 11531 18939 19435 -3177 -5265 4722 N
ATOM 2347 NH2 ARG A 366 -18.702 11.579 -46.394 1.00116.31 N
ANISOU 2347 NH2 ARG A 366 10525 16630 17039 -3221 -5146 4062 N
ATOM 2348 N GLU A 367 -22.702 16.549 -43.080 1.00135.87 N
ANISOU 2348 N GLU A 367 10433 19945 21247 -1550 -3816 5561 N
ATOM 2349 CA GLU A 367 -23.970 17.267 -43.087 1.00142.54 C
ANISOU 2349 CA GLU A 367 10756 21019 22383 -1366 -3779 6032 C
ATOM 2350 C GLU A 367 -23.989 18.371 -42.039 1.00141.16 C
ANISOU 2350 C GLU A 367 10400 20805 22428 -863 -3230 6116 C
ATOM 2351 O GLU A 367 -24.671 19.387 -42.216 1.00150.71 O
ANISOU 2351 O GLU A 367 11305 22141 23816 -574 -3127 6449 O
ATOM 2352 CB GLU A 367 -25.119 16.280 -42.886 1.00148.28 C
ANISOU 2352 CB GLU A 367 11148 21927 23264 -1682 -3974 6300 C
ATOM 2353 CG GLU A 367 -25.276 15.313 -44.059 1.00158.02 C
ANISOU 2353 CG GLU A 367 12550 23207 24282 -2182 -4549 6293 C
ATOM 2354 CD GLU A 367 -26.381 14.306 -43.859 1.00175.07 C
ANISOU 2354 CD GLU A 367 14397 25536 26584 -2526 -4757 6556 C
ATOM 2355 OE1 GLU A 367 -26.869 14.182 -42.718 1.00180.29 O
ANISOU 2355 OE1 GLU A 367 14765 26250 27486 -2399 -4437 6673 O
ATOM 2356 OE2 GLU A 367 -26.760 13.641 -44.847 1.00182.62 O
ANISOU 2356 OE2 GLU A 367 15417 26564 27405 -2929 -5241 6653 O
ATOM 2357 N GLN A 368 -23.247 18.190 -40.945 1.00128.00 N
ANISOU 2357 N GLN A 368 8944 18954 20738 -747 -2868 5823 N
ATOM 2358 CA GLN A 368 -23.175 19.230 -39.927 1.00118.88 C
ANISOU 2358 CA GLN A 368 7707 17714 19748 -279 -2332 5872 C
ATOM 2359 C GLN A 368 -22.360 20.411 -40.414 1.00117.02 C
ANISOU 2359 C GLN A 368 7710 17356 19397 14 -2224 5754 C
ATOM 2360 O GLN A 368 -22.628 21.554 -40.020 1.00118.28 O
ANISOU 2360 O GLN A 368 7738 17501 19704 422 -1871 5940 O
ATOM 2361 CB GLN A 368 -22.598 18.658 -38.636 1.00108.68 C
ANISOU 2361 CB GLN A 368 6600 16252 18442 -266 -2005 5586 C
ATOM 2362 CG GLN A 368 -23.555 17.682 -38.002 1.00110.69 C
ANISOU 2362 CG GLN A 368 6563 16631 18862 -468 -2023 5767 C
ATOM 2363 CD GLN A 368 -24.984 18.187 -38.073 1.00123.20 C
ANISOU 2363 CD GLN A 368 7627 18447 20735 -327 -1996 6293 C
ATOM 2364 OE1 GLN A 368 -25.230 19.381 -37.915 1.00130.06 O
ANISOU 2364 OE1 GLN A 368 8365 19319 21733 71 -1704 6497 O
ATOM 2365 NE2 GLN A 368 -25.926 17.293 -38.352 1.00128.52 N
ANISOU 2365 NE2 GLN A 368 8011 19317 21505 -656 -2306 6528 N
ATOM 2366 N PHE A 369 -21.356 20.155 -41.249 1.00114.40 N
ANISOU 2366 N PHE A 369 7751 16921 18794 -179 -2503 5452 N
ATOM 2367 CA PHE A 369 -20.559 21.244 -41.788 1.00109.84 C
ANISOU 2367 CA PHE A 369 7405 16229 18100 79 -2430 5346 C
ATOM 2368 C PHE A 369 -21.332 22.003 -42.860 1.00123.83 C
ANISOU 2368 C PHE A 369 8951 18172 19929 178 -2655 5689 C
ATOM 2369 O PHE A 369 -21.338 23.237 -42.862 1.00126.96 O
ANISOU 2369 O PHE A 369 9310 18535 20395 565 -2404 5815 O
ATOM 2370 CB PHE A 369 -19.233 20.700 -42.306 1.00 97.17 C
ANISOU 2370 CB PHE A 369 6268 14459 16192 -151 -2638 4934 C
ATOM 2371 CG PHE A 369 -18.435 19.983 -41.252 1.00 91.25 C
ANISOU 2371 CG PHE A 369 5737 13549 15384 -229 -2413 4601 C
ATOM 2372 CD1 PHE A 369 -18.603 20.294 -39.907 1.00 89.36 C
ANISOU 2372 CD1 PHE A 369 5372 13251 15329 27 -1956 4625 C
ATOM 2373 CD2 PHE A 369 -17.526 18.997 -41.599 1.00 85.70 C
ANISOU 2373 CD2 PHE A 369 5388 12745 14430 -546 -2646 4274 C
ATOM 2374 CE1 PHE A 369 -17.877 19.638 -38.931 1.00 85.61 C
ANISOU 2374 CE1 PHE A 369 5103 12631 14792 -42 -1759 4321 C
ATOM 2375 CE2 PHE A 369 -16.789 18.330 -40.629 1.00 81.22 C
ANISOU 2375 CE2 PHE A 369 5014 12040 13805 -606 -2440 3976 C
ATOM 2376 CZ PHE A 369 -16.964 18.650 -39.293 1.00 83.46 C
ANISOU 2376 CZ PHE A 369 5152 12279 14280 -359 -2007 3996 C
ATOM 2377 N LYS A 370 -22.019 21.287 -43.754 1.00131.59 N
ANISOU 2377 N LYS A 370 9790 19331 20878 -164 -3119 5854 N
ATOM 2378 CA LYS A 370 -22.821 21.975 -44.760 1.00128.16 C
ANISOU 2378 CA LYS A 370 9114 19078 20504 -81 -3356 6202 C
ATOM 2379 C LYS A 370 -23.934 22.777 -44.101 1.00127.21 C
ANISOU 2379 C LYS A 370 8525 19104 20705 270 -3027 6615 C
ATOM 2380 O LYS A 370 -24.253 23.890 -44.535 1.00127.22 O
ANISOU 2380 O LYS A 370 8402 19164 20771 587 -2951 6845 O
ATOM 2381 CB LYS A 370 -23.446 20.971 -45.729 1.00126.54 C
ANISOU 2381 CB LYS A 370 8828 19036 20215 -547 -3915 6326 C
ATOM 2382 CG LYS A 370 -22.503 20.100 -46.513 1.00119.57 C
ANISOU 2382 CG LYS A 370 8429 18010 18990 -921 -4272 5970 C
ATOM 2383 CD LYS A 370 -23.346 19.098 -47.290 1.00122.85 C
ANISOU 2383 CD LYS A 370 8734 18585 19358 -1378 -4774 6152 C
ATOM 2384 CE LYS A 370 -22.549 17.892 -47.751 1.00119.84 C
ANISOU 2384 CE LYS A 370 8844 18036 18652 -1803 -5061 5801 C
ATOM 2385 NZ LYS A 370 -23.439 16.747 -48.117 1.00122.34 N
ANISOU 2385 NZ LYS A 370 9044 18478 18960 -2262 -5455 5975 N
ATOM 2386 N ALA A 371 -24.535 22.229 -43.040 1.00128.51 N
ANISOU 2386 N ALA A 371 8442 19320 21066 236 -2811 6722 N
ATOM 2387 CA ALA A 371 -25.588 22.961 -42.347 1.00136.16 C
ANISOU 2387 CA ALA A 371 8985 20411 22336 584 -2455 7129 C
ATOM 2388 C ALA A 371 -25.025 24.177 -41.624 1.00133.83 C
ANISOU 2388 C ALA A 371 8876 19914 22061 1084 -1907 7041 C
ATOM 2389 O ALA A 371 -25.680 25.224 -41.552 1.00140.41 O
ANISOU 2389 O ALA A 371 9484 20814 23053 1460 -1654 7370 O
ATOM 2390 CB ALA A 371 -26.312 22.041 -41.367 1.00138.69 C
ANISOU 2390 CB ALA A 371 9035 20814 22846 423 -2346 7255 C
ATOM 2391 N ALA A 372 -23.813 24.052 -41.071 1.00125.69 N
ANISOU 2391 N ALA A 372 8269 18628 20861 1093 -1712 6608 N
ATOM 2392 CA ALA A 372 -23.188 25.188 -40.409 1.00122.85 C
ANISOU 2392 CA ALA A 372 8147 18046 20485 1530 -1212 6497 C
ATOM 2393 C ALA A 372 -22.701 26.222 -41.414 1.00117.48 C
ANISOU 2393 C ALA A 372 7657 17312 19667 1725 -1302 6478 C
ATOM 2394 O ALA A 372 -22.783 27.430 -41.158 1.00117.81 O
ANISOU 2394 O ALA A 372 7732 17265 19765 2149 -928 6612 O
ATOM 2395 CB ALA A 372 -22.032 24.710 -39.530 1.00121.37 C
ANISOU 2395 CB ALA A 372 8343 17612 20160 1454 -1008 6052 C
ATOM 2396 N PHE A 373 -22.201 25.774 -42.568 1.00113.21 N
ANISOU 2396 N PHE A 373 7277 16808 18929 1429 -1782 6319 N
ATOM 2397 CA PHE A 373 -21.714 26.732 -43.554 1.00113.79 C
ANISOU 2397 CA PHE A 373 7558 16820 18857 1615 -1880 6298 C
ATOM 2398 C PHE A 373 -22.832 27.578 -44.138 1.00123.02 C
ANISOU 2398 C PHE A 373 8385 18182 20174 1858 -1916 6746 C
ATOM 2399 O PHE A 373 -22.590 28.728 -44.522 1.00121.23 O
ANISOU 2399 O PHE A 373 8304 17866 19893 2196 -1765 6796 O
ATOM 2400 CB PHE A 373 -20.960 26.025 -44.684 1.00112.91 C
ANISOU 2400 CB PHE A 373 7722 16696 18481 1240 -2390 6046 C
ATOM 2401 CG PHE A 373 -19.640 25.440 -44.271 1.00114.64 C
ANISOU 2401 CG PHE A 373 8344 16696 18516 1076 -2331 5596 C
ATOM 2402 CD1 PHE A 373 -18.729 26.205 -43.564 1.00114.24 C
ANISOU 2402 CD1 PHE A 373 8559 16411 18436 1374 -1907 5391 C
ATOM 2403 CD2 PHE A 373 -19.294 24.145 -44.631 1.00116.90 C
ANISOU 2403 CD2 PHE A 373 8769 17001 18645 623 -2701 5385 C
ATOM 2404 CE1 PHE A 373 -17.505 25.691 -43.196 1.00109.82 C
ANISOU 2404 CE1 PHE A 373 8342 15664 17720 1227 -1862 5001 C
ATOM 2405 CE2 PHE A 373 -18.069 23.617 -44.265 1.00111.90 C
ANISOU 2405 CE2 PHE A 373 8501 16174 17843 490 -2638 4989 C
ATOM 2406 CZ PHE A 373 -17.170 24.392 -43.545 1.00108.74 C
ANISOU 2406 CZ PHE A 373 8310 15566 17439 792 -2227 4803 C
ATOM 2407 N SER A 374 -24.050 27.039 -44.227 1.00128.71 N
ANISOU 2407 N SER A 374 8660 19165 21080 1697 -2115 7086 N
ATOM 2408 CA SER A 374 -25.142 27.840 -44.769 1.00130.72 C
ANISOU 2408 CA SER A 374 8552 19625 21492 1937 -2150 7545 C
ATOM 2409 C SER A 374 -25.615 28.892 -43.775 1.00138.75 C
ANISOU 2409 C SER A 374 9430 20582 22707 2441 -1541 7782 C
ATOM 2410 O SER A 374 -25.876 30.040 -44.157 1.00145.17 O
ANISOU 2410 O SER A 374 10216 21399 23542 2812 -1390 7998 O
ATOM 2411 CB SER A 374 -26.305 26.939 -45.180 1.00135.73 C
ANISOU 2411 CB SER A 374 8734 20565 22270 1593 -2562 7864 C
ATOM 2412 OG SER A 374 -25.959 26.147 -46.303 1.00134.87 O
ANISOU 2412 OG SER A 374 8798 20504 21942 1158 -3144 7695 O
ATOM 2413 N TRP A 375 -25.730 28.529 -42.495 1.00141.35 N
ANISOU 2413 N TRP A 375 9707 20838 23164 2474 -1172 7748 N
ATOM 2414 CA TRP A 375 -26.207 29.516 -41.534 1.00150.67 C
ANISOU 2414 CA TRP A 375 10805 21938 24506 2953 -573 7985 C
ATOM 2415 C TRP A 375 -25.167 30.596 -41.269 1.00154.72 C
ANISOU 2415 C TRP A 375 11814 22131 24842 3299 -182 7715 C
ATOM 2416 O TRP A 375 -25.519 31.762 -41.063 1.00159.82 O
ANISOU 2416 O TRP A 375 12470 22712 25544 3738 208 7944 O
ATOM 2417 CB TRP A 375 -26.604 28.836 -40.225 1.00133.59 C
ANISOU 2417 CB TRP A 375 8495 19759 22503 2900 -279 8022 C
ATOM 2418 CG TRP A 375 -27.914 28.128 -40.310 1.00147.45 C
ANISOU 2418 CG TRP A 375 9695 21831 24500 2709 -505 8436 C
ATOM 2419 CD1 TRP A 375 -28.114 26.783 -40.317 1.00139.76 C
ANISOU 2419 CD1 TRP A 375 8562 20984 23555 2246 -863 8372 C
ATOM 2420 CD2 TRP A 375 -29.203 28.728 -40.468 1.00153.94 C
ANISOU 2420 CD2 TRP A 375 10045 22885 25562 2963 -409 8993 C
ATOM 2421 NE1 TRP A 375 -29.453 26.504 -40.432 1.00147.16 N
ANISOU 2421 NE1 TRP A 375 8954 22216 24744 2183 -996 8855 N
ATOM 2422 CE2 TRP A 375 -30.144 27.683 -40.531 1.00155.66 C
ANISOU 2422 CE2 TRP A 375 9809 23373 25962 2622 -726 9253 C
ATOM 2423 CE3 TRP A 375 -29.655 30.049 -40.548 1.00152.20 C
ANISOU 2423 CE3 TRP A 375 9747 22666 25415 3453 -74 9309 C
ATOM 2424 CZ2 TRP A 375 -31.509 27.915 -40.673 1.00160.87 C
ANISOU 2424 CZ2 TRP A 375 9910 24322 26893 2748 -729 9830 C
ATOM 2425 CZ3 TRP A 375 -31.011 30.279 -40.687 1.00160.55 C
ANISOU 2425 CZ3 TRP A 375 10258 24008 26735 3599 -62 9880 C
ATOM 2426 CH2 TRP A 375 -31.922 29.217 -40.747 1.00164.85 C
ANISOU 2426 CH2 TRP A 375 10324 24836 27475 3245 -393 10143 C
ATOM 2427 N TRP A 376 -23.888 30.236 -41.268 1.00157.06 N
ANISOU 2427 N TRP A 376 12536 22219 24920 3107 -271 7244 N
ATOM 2428 CA TRP A 376 -22.837 31.225 -41.034 1.00160.21 C
ANISOU 2428 CA TRP A 376 13423 22305 25145 3396 75 6980 C
ATOM 2429 C TRP A 376 -21.900 31.369 -42.231 1.00152.79 C
ANISOU 2429 C TRP A 376 12774 21303 23975 3271 -295 6740 C
ATOM 2430 O TRP A 376 -22.335 31.638 -43.351 1.00154.52 O
ANISOU 2430 O TRP A 376 12845 21685 24181 3276 -618 6945 O
ATOM 2431 CB TRP A 376 -22.054 30.891 -39.762 1.00165.18 C
ANISOU 2431 CB TRP A 376 14351 22687 25721 3366 424 6647 C
ATOM 2432 CG TRP A 376 -21.031 31.945 -39.380 1.00174.98 C
ANISOU 2432 CG TRP A 376 16104 23589 26791 3659 823 6397 C
ATOM 2433 CD1 TRP A 376 -21.293 33.199 -38.904 1.00182.30 C
ANISOU 2433 CD1 TRP A 376 17181 24356 27730 4100 1320 6564 C
ATOM 2434 CD2 TRP A 376 -19.603 31.796 -39.339 1.00177.96 C
ANISOU 2434 CD2 TRP A 376 16927 23731 26957 3518 788 5945 C
ATOM 2435 NE1 TRP A 376 -20.119 33.859 -38.628 1.00183.47 N
ANISOU 2435 NE1 TRP A 376 17863 24176 27672 4219 1571 6233 N
ATOM 2436 CE2 TRP A 376 -19.067 33.017 -38.878 1.00179.11 C
ANISOU 2436 CE2 TRP A 376 17478 23580 26996 3870 1251 5858 C
ATOM 2437 CE3 TRP A 376 -18.726 30.757 -39.668 1.00174.87 C
ANISOU 2437 CE3 TRP A 376 16643 23349 26451 3128 415 5618 C
ATOM 2438 CZ2 TRP A 376 -17.691 33.227 -38.739 1.00171.40 C
ANISOU 2438 CZ2 TRP A 376 16984 22324 25817 3829 1335 5463 C
ATOM 2439 CZ3 TRP A 376 -17.359 30.967 -39.529 1.00166.76 C
ANISOU 2439 CZ3 TRP A 376 16069 22058 25236 3115 513 5243 C
ATOM 2440 CH2 TRP A 376 -16.857 32.192 -39.068 1.00164.42 C
ANISOU 2440 CH2 TRP A 376 16144 21475 24852 3457 962 5172 C
TER 2441 TRP A 376
ATOM 2442 N TYR B 45 21.774 -25.215 -2.525 1.00119.85 N
ANISOU 2442 N TYR B 45 17675 12953 14908 1930 -2526 2993 N
ATOM 2443 CA TYR B 45 21.377 -24.068 -3.336 1.00118.38 C
ANISOU 2443 CA TYR B 45 17452 12978 14549 1795 -2249 2598 C
ATOM 2444 C TYR B 45 19.894 -24.127 -3.687 1.00116.04 C
ANISOU 2444 C TYR B 45 17486 12595 14008 1685 -1846 2346 C
ATOM 2445 O TYR B 45 19.157 -23.164 -3.483 1.00108.36 O
ANISOU 2445 O TYR B 45 16745 11801 12627 1446 -1749 2180 O
ATOM 2446 CB TYR B 45 22.223 -24.014 -4.617 1.00118.89 C
ANISOU 2446 CB TYR B 45 17033 13045 15093 2014 -2085 2416 C
ATOM 2447 CG TYR B 45 21.772 -22.983 -5.633 1.00123.11 C
ANISOU 2447 CG TYR B 45 17519 13758 15501 1897 -1760 2011 C
ATOM 2448 CD1 TYR B 45 22.415 -21.762 -5.738 1.00117.00 C
ANISOU 2448 CD1 TYR B 45 16545 13267 14644 1773 -1896 1933 C
ATOM 2449 CD2 TYR B 45 20.704 -23.237 -6.494 1.00129.15 C
ANISOU 2449 CD2 TYR B 45 18436 14398 16239 1896 -1341 1726 C
ATOM 2450 CE1 TYR B 45 22.007 -20.819 -6.664 1.00110.75 C
ANISOU 2450 CE1 TYR B 45 15708 12627 13745 1662 -1612 1589 C
ATOM 2451 CE2 TYR B 45 20.287 -22.297 -7.421 1.00121.02 C
ANISOU 2451 CE2 TYR B 45 17360 13527 15094 1777 -1075 1389 C
ATOM 2452 CZ TYR B 45 20.942 -21.092 -7.503 1.00111.25 C
ANISOU 2452 CZ TYR B 45 15925 12568 13779 1667 -1205 1324 C
ATOM 2453 OH TYR B 45 20.529 -20.158 -8.425 1.00106.31 O
ANISOU 2453 OH TYR B 45 15252 12090 13050 1545 -951 1012 O
ATOM 2454 N ALA B 46 19.458 -25.276 -4.207 1.00116.03 N
ANISOU 2454 N ALA B 46 17502 12303 14283 1858 -1616 2329 N
ATOM 2455 CA ALA B 46 18.065 -25.415 -4.618 1.00107.36 C
ANISOU 2455 CA ALA B 46 16675 11101 13015 1750 -1252 2112 C
ATOM 2456 C ALA B 46 17.106 -25.349 -3.435 1.00110.18 C
ANISOU 2456 C ALA B 46 17465 11480 12918 1527 -1310 2275 C
ATOM 2457 O ALA B 46 15.972 -24.881 -3.585 1.00103.56 O
ANISOU 2457 O ALA B 46 16839 10690 11819 1353 -1045 2085 O
ATOM 2458 CB ALA B 46 17.870 -26.723 -5.384 1.00102.52 C
ANISOU 2458 CB ALA B 46 16004 10143 12805 1969 -1036 2077 C
ATOM 2459 N TRP B 47 17.542 -25.816 -2.263 1.00118.90 N
ANISOU 2459 N TRP B 47 18699 12546 13931 1528 -1645 2640 N
ATOM 2460 CA TRP B 47 16.685 -25.832 -1.080 1.00118.69 C
ANISOU 2460 CA TRP B 47 19111 12533 13451 1318 -1690 2823 C
ATOM 2461 C TRP B 47 16.258 -24.423 -0.675 1.00110.26 C
ANISOU 2461 C TRP B 47 18240 11761 11893 1053 -1649 2653 C
ATOM 2462 O TRP B 47 15.073 -24.173 -0.422 1.00113.33 O
ANISOU 2462 O TRP B 47 18928 12157 11974 887 -1390 2563 O
ATOM 2463 CB TRP B 47 17.410 -26.572 0.045 1.00133.86 C
ANISOU 2463 CB TRP B 47 21111 14372 15376 1368 -2106 3265 C
ATOM 2464 CG TRP B 47 16.759 -26.582 1.398 1.00150.74 C
ANISOU 2464 CG TRP B 47 23716 16551 17009 1144 -2216 3508 C
ATOM 2465 CD1 TRP B 47 15.723 -27.366 1.813 1.00157.89 C
ANISOU 2465 CD1 TRP B 47 24930 17268 17794 1089 -2033 3637 C
ATOM 2466 CD2 TRP B 47 17.222 -25.884 2.559 1.00164.14 C
ANISOU 2466 CD2 TRP B 47 25624 18472 18271 949 -2569 3696 C
ATOM 2467 NE1 TRP B 47 15.456 -27.131 3.144 1.00168.85 N
ANISOU 2467 NE1 TRP B 47 26719 18770 18667 870 -2201 3873 N
ATOM 2468 CE2 TRP B 47 16.371 -26.231 3.627 1.00173.43 C
ANISOU 2468 CE2 TRP B 47 27255 19604 19036 777 -2535 3900 C
ATOM 2469 CE3 TRP B 47 18.256 -24.971 2.788 1.00166.27 C
ANISOU 2469 CE3 TRP B 47 25747 18979 18449 883 -2906 3701 C
ATOM 2470 CZ2 TRP B 47 16.525 -25.693 4.909 1.00181.14 C
ANISOU 2470 CZ2 TRP B 47 28398 20844 19584 534 -2722 3985 C
ATOM 2471 CZ3 TRP B 47 18.407 -24.439 4.055 1.00171.61 C
ANISOU 2471 CZ3 TRP B 47 26770 19826 18608 640 -3220 3895 C
ATOM 2472 CH2 TRP B 47 17.547 -24.801 5.100 1.00179.65 C
ANISOU 2472 CH2 TRP B 47 28096 20867 19295 468 -3063 3971 C
ATOM 2473 N VAL B 48 17.205 -23.485 -0.607 1.00102.63 N
ANISOU 2473 N VAL B 48 17100 11024 10870 1011 -1893 2612 N
ATOM 2474 CA VAL B 48 16.857 -22.124 -0.208 1.00101.19 C
ANISOU 2474 CA VAL B 48 17120 11095 10233 760 -1867 2440 C
ATOM 2475 C VAL B 48 15.872 -21.497 -1.196 1.00 99.11 C
ANISOU 2475 C VAL B 48 16827 10860 9968 707 -1424 2066 C
ATOM 2476 O VAL B 48 15.002 -20.704 -0.811 1.00102.56 O
ANISOU 2476 O VAL B 48 17541 11398 10030 509 -1248 1940 O
ATOM 2477 CB VAL B 48 18.131 -21.270 -0.057 1.00102.24 C
ANISOU 2477 CB VAL B 48 17035 11444 10367 723 -2236 2467 C
ATOM 2478 CG1 VAL B 48 17.778 -19.841 0.318 1.00 93.19 C
ANISOU 2478 CG1 VAL B 48 16116 10527 8764 460 -2204 2264 C
ATOM 2479 CG2 VAL B 48 19.066 -21.885 0.971 1.00111.61 C
ANISOU 2479 CG2 VAL B 48 18253 12601 11552 750 -2717 2877 C
ATOM 2480 N LEU B 49 15.996 -21.829 -2.486 1.00 92.73 N
ANISOU 2480 N LEU B 49 15691 9960 9581 879 -1234 1887 N
ATOM 2481 CA LEU B 49 15.128 -21.218 -3.491 1.00 86.90 C
ANISOU 2481 CA LEU B 49 14906 9258 8854 814 -860 1553 C
ATOM 2482 C LEU B 49 13.670 -21.573 -3.242 1.00 88.86 C
ANISOU 2482 C LEU B 49 15465 9375 8925 708 -571 1549 C
ATOM 2483 O LEU B 49 12.788 -20.707 -3.304 1.00 92.13 O
ANISOU 2483 O LEU B 49 16006 9885 9112 544 -346 1373 O
ATOM 2484 CB LEU B 49 15.559 -21.655 -4.891 1.00 89.42 C
ANISOU 2484 CB LEU B 49 14861 9483 9631 1010 -725 1387 C
ATOM 2485 CG LEU B 49 14.716 -21.117 -6.051 1.00 84.56 C
ANISOU 2485 CG LEU B 49 14184 8894 9052 939 -372 1062 C
ATOM 2486 CD1 LEU B 49 14.558 -19.610 -5.934 1.00 81.63 C
ANISOU 2486 CD1 LEU B 49 13845 8780 8391 741 -360 902 C
ATOM 2487 CD2 LEU B 49 15.339 -21.482 -7.387 1.00 78.58 C
ANISOU 2487 CD2 LEU B 49 13091 8071 8693 1120 -270 900 C
ATOM 2488 N ILE B 50 13.399 -22.852 -2.974 1.00 87.03 N
ANISOU 2488 N ILE B 50 15337 8905 8826 803 -567 1757 N
ATOM 2489 CA ILE B 50 12.037 -23.276 -2.686 1.00 80.81 C
ANISOU 2489 CA ILE B 50 14826 7980 7899 696 -305 1799 C
ATOM 2490 C ILE B 50 11.565 -22.673 -1.370 1.00 78.60 C
ANISOU 2490 C ILE B 50 14904 7831 7129 498 -332 1927 C
ATOM 2491 O ILE B 50 10.375 -22.373 -1.205 1.00 81.62 O
ANISOU 2491 O ILE B 50 15483 8208 7320 357 -40 1862 O
ATOM 2492 CB ILE B 50 11.954 -24.815 -2.655 1.00 86.84 C
ANISOU 2492 CB ILE B 50 15621 8441 8933 839 -328 2017 C
ATOM 2493 CG1 ILE B 50 12.708 -25.422 -3.847 1.00 75.88 C
ANISOU 2493 CG1 ILE B 50 13896 6914 8021 1064 -341 1896 C
ATOM 2494 CG2 ILE B 50 10.496 -25.265 -2.674 1.00 93.15 C
ANISOU 2494 CG2 ILE B 50 16629 9081 9684 725 -19 2022 C
ATOM 2495 CD1 ILE B 50 12.860 -26.952 -3.785 1.00 75.87 C
ANISOU 2495 CD1 ILE B 50 13911 6585 8331 1239 -408 2117 C
ATOM 2496 N ALA B 51 12.486 -22.461 -0.426 1.00 80.71 N
ANISOU 2496 N ALA B 51 15263 8217 7187 476 -676 2110 N
ATOM 2497 CA ALA B 51 12.110 -21.916 0.874 1.00 81.81 C
ANISOU 2497 CA ALA B 51 15800 8474 6808 274 -716 2227 C
ATOM 2498 C ALA B 51 11.625 -20.477 0.749 1.00 91.33 C
ANISOU 2498 C ALA B 51 17072 9873 7755 113 -510 1935 C
ATOM 2499 O ALA B 51 10.531 -20.138 1.217 1.00 98.52 O
ANISOU 2499 O ALA B 51 18133 10815 8487 -26 -216 1841 O
ATOM 2500 CB ALA B 51 13.285 -22.017 1.839 1.00 76.48 C
ANISOU 2500 CB ALA B 51 15205 7879 5973 268 -1185 2491 C
ATOM 2501 N ALA B 52 12.430 -19.612 0.122 1.00 83.53 N
ANISOU 2501 N ALA B 52 15821 9038 6877 133 -641 1739 N
ATOM 2502 CA ALA B 52 12.036 -18.211 -0.024 1.00 78.98 C
ANISOU 2502 CA ALA B 52 15296 8625 6088 -16 -468 1466 C
ATOM 2503 C ALA B 52 10.763 -18.072 -0.848 1.00 85.81 C
ANISOU 2503 C ALA B 52 16102 9410 7092 -29 -22 1268 C
ATOM 2504 O ALA B 52 9.966 -17.157 -0.608 1.00 95.45 O
ANISOU 2504 O ALA B 52 17401 10708 8160 -165 213 1094 O
ATOM 2505 CB ALA B 52 13.172 -17.404 -0.650 1.00 63.09 C
ANISOU 2505 CB ALA B 52 12970 6773 4229 13 -701 1318 C
ATOM 2506 N TYR B 53 10.556 -18.956 -1.825 1.00 86.12 N
ANISOU 2506 N TYR B 53 15902 9297 7524 109 89 1257 N
ATOM 2507 CA TYR B 53 9.357 -18.860 -2.646 1.00 77.51 C
ANISOU 2507 CA TYR B 53 14744 8127 6581 73 463 1094 C
ATOM 2508 C TYR B 53 8.119 -19.247 -1.843 1.00 71.49 C
ANISOU 2508 C TYR B 53 14291 7252 5621 -26 712 1240 C
ATOM 2509 O TYR B 53 7.079 -18.584 -1.940 1.00 71.20 O
ANISOU 2509 O TYR B 53 14167 7261 5626 -128 987 1064 O
ATOM 2510 CB TYR B 53 9.492 -19.742 -3.880 1.00 74.43 C
ANISOU 2510 CB TYR B 53 14062 7590 6629 221 491 1041 C
ATOM 2511 CG TYR B 53 9.913 -19.019 -5.129 1.00 67.36 C
ANISOU 2511 CG TYR B 53 12852 6802 5941 250 514 778 C
ATOM 2512 CD1 TYR B 53 8.986 -18.323 -5.887 1.00 69.14 C
ANISOU 2512 CD1 TYR B 53 13009 7055 6205 146 779 581 C
ATOM 2513 CD2 TYR B 53 11.230 -19.062 -5.574 1.00 68.78 C
ANISOU 2513 CD2 TYR B 53 12785 7048 6298 380 276 750 C
ATOM 2514 CE1 TYR B 53 9.357 -17.675 -7.046 1.00 75.78 C
ANISOU 2514 CE1 TYR B 53 13579 7995 7219 156 794 361 C
ATOM 2515 CE2 TYR B 53 11.616 -18.417 -6.738 1.00 77.14 C
ANISOU 2515 CE2 TYR B 53 13562 8211 7538 399 322 520 C
ATOM 2516 CZ TYR B 53 10.673 -17.725 -7.469 1.00 74.85 C
ANISOU 2516 CZ TYR B 53 13242 7952 7244 279 577 326 C
ATOM 2517 OH TYR B 53 11.041 -17.078 -8.627 1.00 59.85 O
ANISOU 2517 OH TYR B 53 11081 6159 5501 280 616 117 O
ATOM 2518 N VAL B 54 8.203 -20.324 -1.050 1.00 76.96 N
ANISOU 2518 N VAL B 54 15127 7832 6283 13 591 1498 N
ATOM 2519 CA VAL B 54 7.089 -20.689 -0.176 1.00 79.84 C
ANISOU 2519 CA VAL B 54 15570 8168 6597 -85 792 1565 C
ATOM 2520 C VAL B 54 6.864 -19.610 0.881 1.00 93.97 C
ANISOU 2520 C VAL B 54 17453 10151 8099 -224 837 1453 C
ATOM 2521 O VAL B 54 5.720 -19.289 1.225 1.00104.05 O
ANISOU 2521 O VAL B 54 18720 11435 9379 -307 1121 1370 O
ATOM 2522 CB VAL B 54 7.338 -22.072 0.460 1.00 75.62 C
ANISOU 2522 CB VAL B 54 15155 7485 6092 -20 623 1877 C
ATOM 2523 CG1 VAL B 54 6.162 -22.494 1.349 1.00 78.38 C
ANISOU 2523 CG1 VAL B 54 15583 7816 6381 -126 842 1966 C
ATOM 2524 CG2 VAL B 54 7.604 -23.108 -0.604 1.00 83.49 C
ANISOU 2524 CG2 VAL B 54 16052 8236 7436 139 577 1963 C
ATOM 2525 N ALA B 55 7.951 -19.026 1.401 1.00 88.74 N
ANISOU 2525 N ALA B 55 16875 9631 7212 -247 549 1454 N
ATOM 2526 CA ALA B 55 7.828 -17.949 2.380 1.00 80.85 C
ANISOU 2526 CA ALA B 55 15982 8785 5953 -384 576 1328 C
ATOM 2527 C ALA B 55 7.098 -16.750 1.777 1.00 71.69 C
ANISOU 2527 C ALA B 55 14660 7667 4912 -431 853 1035 C
ATOM 2528 O ALA B 55 6.145 -16.227 2.368 1.00 65.17 O
ANISOU 2528 O ALA B 55 13881 6844 4037 -508 1100 948 O
ATOM 2529 CB ALA B 55 9.209 -17.544 2.898 1.00 68.35 C
ANISOU 2529 CB ALA B 55 14484 7336 4151 -415 171 1381 C
ATOM 2530 N VAL B 56 7.531 -16.297 0.593 1.00 76.73 N
ANISOU 2530 N VAL B 56 15101 8329 5725 -379 812 895 N
ATOM 2531 CA VAL B 56 6.881 -15.154 -0.044 1.00 73.68 C
ANISOU 2531 CA VAL B 56 14523 7976 5495 -424 1040 645 C
ATOM 2532 C VAL B 56 5.440 -15.492 -0.402 1.00 70.42 C
ANISOU 2532 C VAL B 56 14012 7435 5309 -419 1383 634 C
ATOM 2533 O VAL B 56 4.522 -14.692 -0.181 1.00 67.74 O
ANISOU 2533 O VAL B 56 13618 7094 5026 -478 1607 519 O
ATOM 2534 CB VAL B 56 7.686 -14.701 -1.275 1.00 61.23 C
ANISOU 2534 CB VAL B 56 12745 6463 4056 -375 912 520 C
ATOM 2535 CG1 VAL B 56 6.834 -13.805 -2.160 1.00 53.73 C
ANISOU 2535 CG1 VAL B 56 11550 5508 3357 -409 1162 315 C
ATOM 2536 CG2 VAL B 56 8.953 -13.977 -0.846 1.00 58.52 C
ANISOU 2536 CG2 VAL B 56 12452 6273 3510 -416 592 489 C
ATOM 2537 N PHE B 57 5.222 -16.688 -0.956 1.00 65.87 N
ANISOU 2537 N PHE B 57 13412 6734 4881 -348 1416 770 N
ATOM 2538 CA PHE B 57 3.877 -17.096 -1.345 1.00 65.80 C
ANISOU 2538 CA PHE B 57 13290 6604 5108 -360 1702 779 C
ATOM 2539 C PHE B 57 2.916 -16.946 -0.173 1.00 73.35 C
ANISOU 2539 C PHE B 57 14354 7560 5956 -426 1892 824 C
ATOM 2540 O PHE B 57 1.816 -16.398 -0.316 1.00 66.83 O
ANISOU 2540 O PHE B 57 13401 6707 5284 -461 2141 735 O
ATOM 2541 CB PHE B 57 3.905 -18.537 -1.850 1.00 72.24 C
ANISOU 2541 CB PHE B 57 14118 7265 6066 -289 1662 958 C
ATOM 2542 CG PHE B 57 2.606 -19.001 -2.436 1.00 80.19 C
ANISOU 2542 CG PHE B 57 14968 8148 7350 -318 1905 965 C
ATOM 2543 CD1 PHE B 57 2.236 -18.612 -3.715 1.00 86.30 C
ANISOU 2543 CD1 PHE B 57 15524 8898 8368 -333 1997 816 C
ATOM 2544 CD2 PHE B 57 1.762 -19.838 -1.716 1.00 74.44 C
ANISOU 2544 CD2 PHE B 57 14300 7341 6642 -345 2018 1136 C
ATOM 2545 CE1 PHE B 57 1.046 -19.040 -4.270 1.00 86.40 C
ANISOU 2545 CE1 PHE B 57 15373 8811 8644 -378 2171 836 C
ATOM 2546 CE2 PHE B 57 0.570 -20.276 -2.255 1.00 70.40 C
ANISOU 2546 CE2 PHE B 57 13615 6732 6402 -383 2206 1158 C
ATOM 2547 CZ PHE B 57 0.203 -19.878 -3.541 1.00 76.14 C
ANISOU 2547 CZ PHE B 57 14116 7438 7378 -402 2270 1008 C
ATOM 2548 N VAL B 58 3.319 -17.437 1.000 1.00 85.17 N
ANISOU 2548 N VAL B 58 16089 9083 7187 -442 1773 980 N
ATOM 2549 CA VAL B 58 2.464 -17.352 2.180 1.00 78.65 C
ANISOU 2549 CA VAL B 58 15406 8263 6214 -508 1964 1033 C
ATOM 2550 C VAL B 58 2.329 -15.900 2.634 1.00 78.57 C
ANISOU 2550 C VAL B 58 15426 8337 6089 -568 2058 834 C
ATOM 2551 O VAL B 58 1.217 -15.367 2.761 1.00 73.46 O
ANISOU 2551 O VAL B 58 14717 7648 5546 -590 2345 759 O
ATOM 2552 CB VAL B 58 3.017 -18.240 3.309 1.00 72.79 C
ANISOU 2552 CB VAL B 58 14923 7538 5197 -526 1783 1263 C
ATOM 2553 CG1 VAL B 58 2.231 -17.995 4.601 1.00 79.41 C
ANISOU 2553 CG1 VAL B 58 15947 8407 5820 -609 1986 1297 C
ATOM 2554 CG2 VAL B 58 2.975 -19.687 2.901 1.00 71.57 C
ANISOU 2554 CG2 VAL B 58 14726 7255 5211 -463 1723 1482 C
ATOM 2555 N VAL B 59 3.465 -15.241 2.894 1.00 78.70 N
ANISOU 2555 N VAL B 59 15538 8461 5904 -595 1808 759 N
ATOM 2556 CA VAL B 59 3.432 -13.869 3.395 1.00 72.47 C
ANISOU 2556 CA VAL B 59 14807 7733 4996 -663 1869 579 C
ATOM 2557 C VAL B 59 2.754 -12.944 2.391 1.00 70.91 C
ANISOU 2557 C VAL B 59 14341 7494 5107 -643 2063 399 C
ATOM 2558 O VAL B 59 1.951 -12.081 2.762 1.00 73.89 O
ANISOU 2558 O VAL B 59 14731 7834 5508 -675 2293 301 O
ATOM 2559 CB VAL B 59 4.849 -13.379 3.732 1.00 71.91 C
ANISOU 2559 CB VAL B 59 14852 7785 4686 -709 1520 543 C
ATOM 2560 CG1 VAL B 59 4.836 -11.878 3.866 1.00 88.47 C
ANISOU 2560 CG1 VAL B 59 16936 9921 6756 -773 1579 331 C
ATOM 2561 CG2 VAL B 59 5.344 -14.038 4.989 1.00 70.19 C
ANISOU 2561 CG2 VAL B 59 14933 7608 4127 -762 1344 722 C
ATOM 2562 N ALA B 60 3.116 -13.059 1.112 1.00 68.98 N
ANISOU 2562 N ALA B 60 13862 7252 5095 -592 1964 359 N
ATOM 2563 CA ALA B 60 2.479 -12.222 0.099 1.00 65.26 C
ANISOU 2563 CA ALA B 60 13125 6747 4923 -585 2119 216 C
ATOM 2564 C ALA B 60 0.971 -12.440 0.072 1.00 65.59 C
ANISOU 2564 C ALA B 60 13088 6669 5163 -575 2440 258 C
ATOM 2565 O ALA B 60 0.203 -11.486 -0.107 1.00 55.08 O
ANISOU 2565 O ALA B 60 11642 5298 3987 -590 2625 160 O
ATOM 2566 CB ALA B 60 3.096 -12.503 -1.268 1.00 68.20 C
ANISOU 2566 CB ALA B 60 13285 7143 5487 -541 1966 189 C
ATOM 2567 N LEU B 61 0.527 -13.692 0.222 1.00 77.80 N
ANISOU 2567 N LEU B 61 14681 8153 6726 -550 2504 420 N
ATOM 2568 CA LEU B 61 -0.907 -13.956 0.261 1.00 77.94 C
ANISOU 2568 CA LEU B 61 14609 8073 6932 -547 2797 483 C
ATOM 2569 C LEU B 61 -1.526 -13.454 1.562 1.00 89.88 C
ANISOU 2569 C LEU B 61 16312 9576 8262 -578 3006 486 C
ATOM 2570 O LEU B 61 -2.520 -12.717 1.542 1.00 97.72 O
ANISOU 2570 O LEU B 61 17207 10510 9413 -576 3254 424 O
ATOM 2571 CB LEU B 61 -1.174 -15.444 0.071 1.00 67.10 C
ANISOU 2571 CB LEU B 61 13221 6638 5636 -526 2790 669 C
ATOM 2572 CG LEU B 61 -0.987 -15.986 -1.342 1.00 66.39 C
ANISOU 2572 CG LEU B 61 12922 6506 5798 -500 2682 664 C
ATOM 2573 CD1 LEU B 61 -1.588 -17.373 -1.422 1.00 60.80 C
ANISOU 2573 CD1 LEU B 61 12188 5702 5211 -498 2732 856 C
ATOM 2574 CD2 LEU B 61 -1.607 -15.070 -2.390 1.00 70.94 C
ANISOU 2574 CD2 LEU B 61 13230 7072 6651 -514 2784 520 C
ATOM 2575 N VAL B 62 -0.947 -13.836 2.707 1.00 84.21 N
ANISOU 2575 N VAL B 62 15880 8911 7206 -607 2911 566 N
ATOM 2576 CA VAL B 62 -1.501 -13.406 3.988 1.00 80.22 C
ANISOU 2576 CA VAL B 62 15600 8397 6483 -649 3119 567 C
ATOM 2577 C VAL B 62 -1.432 -11.892 4.128 1.00 82.89 C
ANISOU 2577 C VAL B 62 15967 8741 6788 -674 3179 366 C
ATOM 2578 O VAL B 62 -2.341 -11.264 4.683 1.00 80.95 O
ANISOU 2578 O VAL B 62 15783 8427 6547 -680 3469 321 O
ATOM 2579 CB VAL B 62 -0.771 -14.108 5.147 1.00 81.38 C
ANISOU 2579 CB VAL B 62 16063 8613 6245 -696 2955 700 C
ATOM 2580 CG1 VAL B 62 -1.047 -13.387 6.451 1.00 75.15 C
ANISOU 2580 CG1 VAL B 62 15554 7836 5162 -760 3119 645 C
ATOM 2581 CG2 VAL B 62 -1.195 -15.556 5.235 1.00 72.10 C
ANISOU 2581 CG2 VAL B 62 14879 7398 5117 -679 2989 933 C
ATOM 2582 N GLY B 63 -0.347 -11.283 3.657 1.00 84.90 N
ANISOU 2582 N GLY B 63 16181 9069 7008 -689 2915 253 N
ATOM 2583 CA GLY B 63 -0.181 -9.848 3.785 1.00 65.82 C
ANISOU 2583 CA GLY B 63 13794 6658 4559 -726 2939 77 C
ATOM 2584 C GLY B 63 -1.253 -9.099 3.027 1.00 76.66 C
ANISOU 2584 C GLY B 63 14924 7927 6278 -688 3196 0 C
ATOM 2585 O GLY B 63 -2.049 -8.360 3.616 1.00 77.12 O
ANISOU 2585 O GLY B 63 15074 7901 6329 -694 3465 -54 O
ATOM 2586 N ASN B 64 -1.281 -9.295 1.706 1.00 82.79 N
ANISOU 2586 N ASN B 64 15397 8700 7358 -649 3117 4 N
ATOM 2587 CA ASN B 64 -2.201 -8.539 0.861 1.00 75.02 C
ANISOU 2587 CA ASN B 64 14164 7628 6713 -625 3306 -56 C
ATOM 2588 C ASN B 64 -3.662 -8.848 1.166 1.00 68.79 C
ANISOU 2588 C ASN B 64 13341 6719 6078 -586 3651 32 C
ATOM 2589 O ASN B 64 -4.522 -7.979 0.980 1.00 66.86 O
ANISOU 2589 O ASN B 64 12989 6378 6038 -568 3875 -18 O
ATOM 2590 CB ASN B 64 -1.888 -8.807 -0.609 1.00 65.24 C
ANISOU 2590 CB ASN B 64 12634 6424 5729 -610 3128 -59 C
ATOM 2591 CG ASN B 64 -0.497 -8.348 -1.002 1.00 66.24 C
ANISOU 2591 CG ASN B 64 12747 6675 5747 -641 2819 -148 C
ATOM 2592 OD1 ASN B 64 -0.232 -7.150 -1.130 1.00 75.07 O
ANISOU 2592 OD1 ASN B 64 13824 7815 6885 -673 2790 -259 O
ATOM 2593 ND2 ASN B 64 0.409 -9.299 -1.166 1.00 58.90 N
ANISOU 2593 ND2 ASN B 64 11854 5824 4703 -628 2593 -88 N
ATOM 2594 N THR B 65 -3.976 -10.076 1.593 1.00 72.02 N
ANISOU 2594 N THR B 65 13820 7128 6416 -572 3701 178 N
ATOM 2595 CA THR B 65 -5.352 -10.369 1.988 1.00 81.37 C
ANISOU 2595 CA THR B 65 14966 8217 7735 -541 4035 279 C
ATOM 2596 C THR B 65 -5.772 -9.483 3.155 1.00100.17 C
ANISOU 2596 C THR B 65 17582 10538 9941 -549 4293 214 C
ATOM 2597 O THR B 65 -6.883 -8.935 3.170 1.00107.01 O
ANISOU 2597 O THR B 65 18349 11293 11017 -510 4599 212 O
ATOM 2598 CB THR B 65 -5.502 -11.857 2.346 1.00 74.44 C
ANISOU 2598 CB THR B 65 14144 7364 6774 -543 4021 466 C
ATOM 2599 OG1 THR B 65 -5.203 -12.670 1.204 1.00 63.94 O
ANISOU 2599 OG1 THR B 65 12600 6060 5634 -535 3813 521 O
ATOM 2600 CG2 THR B 65 -6.916 -12.172 2.853 1.00 81.75 C
ANISOU 2600 CG2 THR B 65 15024 8210 7828 -521 4372 593 C
ATOM 2601 N LEU B 66 -4.881 -9.311 4.131 1.00102.74 N
ANISOU 2601 N LEU B 66 18223 10931 9881 -602 4172 161 N
ATOM 2602 CA LEU B 66 -5.177 -8.436 5.258 1.00 89.79 C
ANISOU 2602 CA LEU B 66 16852 9234 8028 -627 4404 78 C
ATOM 2603 C LEU B 66 -5.303 -6.980 4.829 1.00 93.45 C
ANISOU 2603 C LEU B 66 17229 9619 8660 -619 4486 -84 C
ATOM 2604 O LEU B 66 -6.087 -6.229 5.417 1.00103.50 O
ANISOU 2604 O LEU B 66 18608 10774 9943 -603 4807 -134 O
ATOM 2605 CB LEU B 66 -4.088 -8.581 6.321 1.00 77.89 C
ANISOU 2605 CB LEU B 66 15704 7832 6057 -707 4197 57 C
ATOM 2606 CG LEU B 66 -4.099 -9.884 7.119 1.00 79.07 C
ANISOU 2606 CG LEU B 66 16033 8039 5972 -729 4187 234 C
ATOM 2607 CD1 LEU B 66 -2.994 -9.857 8.160 1.00 84.77 C
ANISOU 2607 CD1 LEU B 66 17117 8861 6230 -820 3959 210 C
ATOM 2608 CD2 LEU B 66 -5.455 -10.141 7.767 1.00 82.53 C
ANISOU 2608 CD2 LEU B 66 16517 8385 6455 -700 4605 327 C
ATOM 2609 N VAL B 67 -4.550 -6.562 3.808 1.00 87.99 N
ANISOU 2609 N VAL B 67 16347 8983 8103 -631 4215 -158 N
ATOM 2610 CA VAL B 67 -4.640 -5.177 3.354 1.00 81.10 C
ANISOU 2610 CA VAL B 67 15380 8040 7394 -634 4277 -290 C
ATOM 2611 C VAL B 67 -6.023 -4.884 2.790 1.00 94.28 C
ANISOU 2611 C VAL B 67 16808 9556 9457 -562 4598 -246 C
ATOM 2612 O VAL B 67 -6.552 -3.775 2.949 1.00112.01 O
ANISOU 2612 O VAL B 67 19079 11679 11803 -548 4829 -323 O
ATOM 2613 CB VAL B 67 -3.538 -4.878 2.321 1.00 67.61 C
ANISOU 2613 CB VAL B 67 13493 6443 5752 -667 3914 -354 C
ATOM 2614 CG1 VAL B 67 -3.747 -3.494 1.706 1.00 63.17 C
ANISOU 2614 CG1 VAL B 67 12790 5806 5406 -673 3989 -461 C
ATOM 2615 CG2 VAL B 67 -2.177 -4.979 2.970 1.00 65.13 C
ANISOU 2615 CG2 VAL B 67 13415 6268 5063 -734 3614 -400 C
ATOM 2616 N CYS B 68 -6.626 -5.865 2.110 1.00 90.25 N
ANISOU 2616 N CYS B 68 16059 9047 9187 -515 4615 -114 N
ATOM 2617 CA CYS B 68 -7.996 -5.693 1.643 1.00 84.72 C
ANISOU 2617 CA CYS B 68 15114 8208 8867 -444 4913 -44 C
ATOM 2618 C CYS B 68 -8.970 -5.732 2.812 1.00 93.93 C
ANISOU 2618 C CYS B 68 16457 9269 9962 -405 5301 11 C
ATOM 2619 O CYS B 68 -9.930 -4.953 2.859 1.00 99.25 O
ANISOU 2619 O CYS B 68 17055 9791 10865 -350 5616 5 O
ATOM 2620 CB CYS B 68 -8.344 -6.765 0.604 1.00 79.55 C
ANISOU 2620 CB CYS B 68 14152 7603 8470 -421 4795 84 C
ATOM 2621 SG CYS B 68 -7.331 -6.738 -0.906 1.00 86.32 S
ANISOU 2621 SG CYS B 68 14784 8572 9441 -463 4389 19 S
ATOM 2622 N LEU B 69 -8.722 -6.621 3.777 1.00 96.11 N
ANISOU 2622 N LEU B 69 16976 9619 9921 -433 5294 74 N
ATOM 2623 CA LEU B 69 -9.599 -6.735 4.938 1.00 99.59 C
ANISOU 2623 CA LEU B 69 17608 9979 10251 -408 5668 134 C
ATOM 2624 C LEU B 69 -9.486 -5.514 5.844 1.00100.53 C
ANISOU 2624 C LEU B 69 18030 10012 10155 -428 5858 -21 C
ATOM 2625 O LEU B 69 -10.470 -5.118 6.482 1.00107.35 O
ANISOU 2625 O LEU B 69 18969 10739 11079 -380 6261 -8 O
ATOM 2626 CB LEU B 69 -9.261 -8.019 5.692 1.00104.30 C
ANISOU 2626 CB LEU B 69 18396 10693 10540 -451 5574 253 C
ATOM 2627 CG LEU B 69 -9.263 -9.218 4.733 1.00103.42 C
ANISOU 2627 CG LEU B 69 17997 10659 10637 -443 5359 400 C
ATOM 2628 CD1 LEU B 69 -9.102 -10.576 5.418 1.00 94.36 C
ANISOU 2628 CD1 LEU B 69 17001 9603 9250 -482 5299 562 C
ATOM 2629 CD2 LEU B 69 -10.504 -9.203 3.848 1.00108.65 C
ANISOU 2629 CD2 LEU B 69 18277 11228 11779 -375 5555 491 C
ATOM 2630 N ALA B 70 -8.297 -4.909 5.914 1.00 95.58 N
ANISOU 2630 N ALA B 70 17576 9460 9280 -501 5580 -165 N
ATOM 2631 CA ALA B 70 -8.144 -3.655 6.644 1.00 92.75 C
ANISOU 2631 CA ALA B 70 17488 9018 8736 -533 5730 -327 C
ATOM 2632 C ALA B 70 -8.938 -2.526 5.999 1.00102.92 C
ANISOU 2632 C ALA B 70 18564 10130 10410 -469 5974 -378 C
ATOM 2633 O ALA B 70 -9.359 -1.591 6.690 1.00105.00 O
ANISOU 2633 O ALA B 70 19025 10255 10615 -460 6279 -470 O
ATOM 2634 CB ALA B 70 -6.664 -3.275 6.731 1.00 95.31 C
ANISOU 2634 CB ALA B 70 17988 9476 8751 -632 5334 -451 C
ATOM 2635 N VAL B 71 -9.156 -2.595 4.690 1.00112.98 N
ANISOU 2635 N VAL B 71 19450 11400 12076 -428 5854 -317 N
ATOM 2636 CA VAL B 71 -9.951 -1.578 4.009 1.00117.41 C
ANISOU 2636 CA VAL B 71 19782 11790 13037 -367 6075 -334 C
ATOM 2637 C VAL B 71 -11.436 -1.912 4.042 1.00126.18 C
ANISOU 2637 C VAL B 71 20709 12753 14480 -259 6468 -189 C
ATOM 2638 O VAL B 71 -12.269 -1.023 4.235 1.00122.97 O
ANISOU 2638 O VAL B 71 20287 12155 14282 -197 6823 -204 O
ATOM 2639 CB VAL B 71 -9.437 -1.392 2.570 1.00105.12 C
ANISOU 2639 CB VAL B 71 17908 10303 11729 -387 5747 -340 C
ATOM 2640 CG1 VAL B 71 -10.416 -0.558 1.763 1.00104.29 C
ANISOU 2640 CG1 VAL B 71 17514 10020 12093 -317 5974 -306 C
ATOM 2641 CG2 VAL B 71 -8.063 -0.733 2.590 1.00 97.00 C
ANISOU 2641 CG2 VAL B 71 17047 9392 10417 -486 5429 -489 C
ATOM 2642 N TRP B 72 -11.803 -3.179 3.834 1.00139.12 N
ANISOU 2642 N TRP B 72 22188 14475 16197 -233 6416 -34 N
ATOM 2643 CA TRP B 72 -13.214 -3.535 3.937 1.00148.63 C
ANISOU 2643 CA TRP B 72 23202 15558 17713 -136 6783 124 C
ATOM 2644 C TRP B 72 -13.731 -3.354 5.357 1.00149.12 C
ANISOU 2644 C TRP B 72 23585 15522 17550 -114 7188 110 C
ATOM 2645 O TRP B 72 -14.912 -3.041 5.548 1.00163.52 O
ANISOU 2645 O TRP B 72 25293 17177 19659 -22 7593 190 O
ATOM 2646 CB TRP B 72 -13.463 -4.967 3.472 1.00158.60 C
ANISOU 2646 CB TRP B 72 24236 16949 19076 -133 6628 300 C
ATOM 2647 CG TRP B 72 -14.931 -5.264 3.432 1.00172.80 C
ANISOU 2647 CG TRP B 72 25767 18636 21252 -41 6971 483 C
ATOM 2648 CD1 TRP B 72 -15.839 -4.769 2.541 1.00178.84 C
ANISOU 2648 CD1 TRP B 72 26155 19283 22514 38 7086 562 C
ATOM 2649 CD2 TRP B 72 -15.668 -6.096 4.335 1.00181.96 C
ANISOU 2649 CD2 TRP B 72 27002 19798 22339 -22 7240 629 C
ATOM 2650 NE1 TRP B 72 -17.093 -5.253 2.825 1.00183.16 N
ANISOU 2650 NE1 TRP B 72 26518 19757 23317 108 7399 754 N
ATOM 2651 CE2 TRP B 72 -17.016 -6.070 3.922 1.00185.70 C
ANISOU 2651 CE2 TRP B 72 27113 20152 23294 70 7508 796 C
ATOM 2652 CE3 TRP B 72 -15.319 -6.868 5.448 1.00185.95 C
ANISOU 2652 CE3 TRP B 72 27833 20398 22421 -80 7272 651 C
ATOM 2653 CZ2 TRP B 72 -18.014 -6.786 4.583 1.00191.27 C
ANISOU 2653 CZ2 TRP B 72 27767 20832 24075 102 7816 982 C
ATOM 2654 CZ3 TRP B 72 -16.312 -7.579 6.103 1.00190.29 C
ANISOU 2654 CZ3 TRP B 72 28349 20924 23028 -51 7584 831 C
ATOM 2655 CH2 TRP B 72 -17.643 -7.533 5.669 1.00193.23 C
ANISOU 2655 CH2 TRP B 72 28352 21178 23890 38 7857 994 C
ATOM 2656 N ARG B 73 -12.874 -3.549 6.361 1.00133.50 N
ANISOU 2656 N ARG B 73 22007 13648 15068 -198 7090 18 N
ATOM 2657 CA ARG B 73 -13.313 -3.363 7.739 1.00123.92 C
ANISOU 2657 CA ARG B 73 21140 12354 13588 -193 7472 -10 C
ATOM 2658 C ARG B 73 -13.401 -1.880 8.068 1.00128.15 C
ANISOU 2658 C ARG B 73 21849 12717 14127 -179 7714 -179 C
ATOM 2659 O ARG B 73 -14.473 -1.369 8.407 1.00134.61 O
ANISOU 2659 O ARG B 73 22644 13342 15160 -91 8169 -151 O
ATOM 2660 CB ARG B 73 -12.356 -4.055 8.717 1.00120.15 C
ANISOU 2660 CB ARG B 73 21048 12050 12554 -299 7268 -45 C
ATOM 2661 CG ARG B 73 -12.699 -5.475 9.111 1.00123.97 C
ANISOU 2661 CG ARG B 73 21518 12639 12945 -305 7294 146 C
ATOM 2662 CD ARG B 73 -11.953 -5.840 10.393 1.00120.76 C
ANISOU 2662 CD ARG B 73 21579 12346 11959 -407 7229 103 C
ATOM 2663 NE ARG B 73 -12.440 -5.081 11.544 1.00111.43 N
ANISOU 2663 NE ARG B 73 20736 11040 10561 -405 7647 7 N
ATOM 2664 CZ ARG B 73 -13.399 -5.510 12.355 1.00113.70 C
ANISOU 2664 CZ ARG B 73 21118 11277 10806 -372 8054 119 C
ATOM 2665 NH1 ARG B 73 -13.965 -6.690 12.138 1.00118.52 N
ANISOU 2665 NH1 ARG B 73 21493 11956 11582 -345 8075 342 N
ATOM 2666 NH2 ARG B 73 -13.794 -4.767 13.379 1.00119.40 N
ANISOU 2666 NH2 ARG B 73 22171 11878 11318 -370 8447 13 N
ATOM 2667 N ASN B 74 -12.279 -1.173 7.959 1.00135.29 N
ANISOU 2667 N ASN B 74 22916 13682 14808 -265 7418 -348 N
ATOM 2668 CA ASN B 74 -12.189 0.219 8.390 1.00142.44 C
ANISOU 2668 CA ASN B 74 24047 14444 15631 -279 7610 -525 C
ATOM 2669 C ASN B 74 -12.719 1.128 7.285 1.00153.76 C
ANISOU 2669 C ASN B 74 25124 15722 17575 -207 7696 -514 C
ATOM 2670 O ASN B 74 -12.019 1.418 6.311 1.00157.02 O
ANISOU 2670 O ASN B 74 25351 16213 18097 -250 7344 -549 O
ATOM 2671 CB ASN B 74 -10.749 0.563 8.755 1.00136.22 C
ANISOU 2671 CB ASN B 74 23567 13801 14388 -412 7235 -693 C
ATOM 2672 CG ASN B 74 -10.644 1.780 9.655 1.00129.78 C
ANISOU 2672 CG ASN B 74 23127 12857 13325 -451 7470 -884 C
ATOM 2673 OD1 ASN B 74 -11.505 2.662 9.650 1.00118.55 O
ANISOU 2673 OD1 ASN B 74 21660 11221 12161 -374 7861 -918 O
ATOM 2674 ND2 ASN B 74 -9.580 1.825 10.446 1.00135.95 N
ANISOU 2674 ND2 ASN B 74 24287 13762 13607 -572 7232 -1008 N
ATOM 2675 N HIS B 75 -13.968 1.586 7.432 1.00159.01 N
ANISOU 2675 N HIS B 75 25689 16163 18567 -96 8175 -453 N
ATOM 2676 CA HIS B 75 -14.499 2.545 6.468 1.00159.54 C
ANISOU 2676 CA HIS B 75 25436 16055 19127 -28 8284 -432 C
ATOM 2677 C HIS B 75 -13.751 3.866 6.538 1.00151.31 C
ANISOU 2677 C HIS B 75 24598 14965 17928 -98 8218 -634 C
ATOM 2678 O HIS B 75 -13.722 4.610 5.551 1.00159.45 O
ANISOU 2678 O HIS B 75 25370 15933 19282 -90 8125 -633 O
ATOM 2679 CB HIS B 75 -15.999 2.767 6.662 1.00175.79 C
ANISOU 2679 CB HIS B 75 27330 17866 21595 116 8826 -305 C
ATOM 2680 CG HIS B 75 -16.846 1.680 6.078 1.00185.07 C
ANISOU 2680 CG HIS B 75 28120 19069 23127 199 8835 -71 C
ATOM 2681 ND1 HIS B 75 -17.476 1.807 4.858 1.00186.98 N
ANISOU 2681 ND1 HIS B 75 27889 19227 23929 276 8791 73 N
ATOM 2682 CD2 HIS B 75 -17.136 0.435 6.524 1.00188.07 C
ANISOU 2682 CD2 HIS B 75 28511 19568 23380 208 8855 51 C
ATOM 2683 CE1 HIS B 75 -18.147 0.701 4.594 1.00185.51 C
ANISOU 2683 CE1 HIS B 75 27436 19105 23944 331 8786 267 C
ATOM 2684 NE2 HIS B 75 -17.952 -0.150 5.587 1.00186.18 N
ANISOU 2684 NE2 HIS B 75 27804 19314 23621 289 8830 260 N
ATOM 2685 N HIS B 76 -13.146 4.181 7.684 1.00144.03 N
ANISOU 2685 N HIS B 76 24138 14076 16512 -174 8260 -803 N
ATOM 2686 CA HIS B 76 -12.297 5.363 7.740 1.00138.22 C
ANISOU 2686 CA HIS B 76 23602 13330 15587 -257 8127 -1002 C
ATOM 2687 C HIS B 76 -11.113 5.212 6.807 1.00140.53 C
ANISOU 2687 C HIS B 76 23732 13840 15825 -351 7559 -1019 C
ATOM 2688 O HIS B 76 -10.545 6.211 6.343 1.00147.74 O
ANISOU 2688 O HIS B 76 24620 14743 16773 -399 7412 -1129 O
ATOM 2689 CB HIS B 76 -11.789 5.589 9.159 1.00142.69 C
ANISOU 2689 CB HIS B 76 24712 13912 15590 -337 8220 -1179 C
ATOM 2690 CG HIS B 76 -12.791 6.226 10.061 1.00152.00 C
ANISOU 2690 CG HIS B 76 26114 14842 16796 -259 8810 -1236 C
ATOM 2691 ND1 HIS B 76 -14.058 5.717 10.245 1.00154.54 N
ANISOU 2691 ND1 HIS B 76 26290 15031 17395 -134 9234 -1078 N
ATOM 2692 CD2 HIS B 76 -12.713 7.337 10.828 1.00156.74 C
ANISOU 2692 CD2 HIS B 76 27072 15296 17185 -286 9060 -1435 C
ATOM 2693 CE1 HIS B 76 -14.718 6.489 11.089 1.00160.88 C
ANISOU 2693 CE1 HIS B 76 27348 15615 18165 -82 9737 -1175 C
ATOM 2694 NE2 HIS B 76 -13.925 7.478 11.459 1.00162.38 N
ANISOU 2694 NE2 HIS B 76 27857 15788 18051 -173 9645 -1399 N
ATOM 2695 N MET B 77 -10.728 3.967 6.529 1.00135.25 N
ANISOU 2695 N MET B 77 22952 13367 15072 -375 7248 -911 N
ATOM 2696 CA MET B 77 -9.565 3.654 5.717 1.00112.82 C
ANISOU 2696 CA MET B 77 19973 10744 12151 -458 6718 -919 C
ATOM 2697 C MET B 77 -9.897 3.491 4.237 1.00109.77 C
ANISOU 2697 C MET B 77 19108 10359 12242 -410 6589 -791 C
ATOM 2698 O MET B 77 -9.105 2.893 3.499 1.00119.63 O
ANISOU 2698 O MET B 77 20202 11794 13459 -459 6183 -758 O
ATOM 2699 CB MET B 77 -8.885 2.379 6.231 1.00101.59 C
ANISOU 2699 CB MET B 77 18706 9527 10365 -512 6447 -876 C
ATOM 2700 CG MET B 77 -7.854 2.600 7.326 1.00 98.71 C
ANISOU 2700 CG MET B 77 18782 9259 9464 -621 6290 -1025 C
ATOM 2701 SD MET B 77 -7.040 1.069 7.813 1.00 98.66 S
ANISOU 2701 SD MET B 77 18911 9487 9086 -683 5948 -936 S
ATOM 2702 CE MET B 77 -6.811 0.293 6.221 1.00 96.32 C
ANISOU 2702 CE MET B 77 18115 9317 9165 -645 5608 -797 C
ATOM 2703 N ARG B 78 -11.025 4.025 3.780 1.00106.26 N
ANISOU 2703 N ARG B 78 18429 9704 12239 -316 6922 -716 N
ATOM 2704 CA ARG B 78 -11.366 3.988 2.358 1.00113.04 C
ANISOU 2704 CA ARG B 78 18844 10546 13560 -280 6800 -596 C
ATOM 2705 C ARG B 78 -11.081 5.350 1.731 1.00120.44 C
ANISOU 2705 C ARG B 78 19695 11405 14663 -316 6775 -684 C
ATOM 2706 O ARG B 78 -11.948 6.012 1.153 1.00130.84 O
ANISOU 2706 O ARG B 78 20767 12528 16420 -247 7017 -610 O
ATOM 2707 CB ARG B 78 -12.822 3.573 2.146 1.00112.40 C
ANISOU 2707 CB ARG B 78 18497 10292 13917 -148 7142 -417 C
ATOM 2708 CG ARG B 78 -13.250 2.218 2.705 1.00111.63 C
ANISOU 2708 CG ARG B 78 18438 10270 13707 -105 7201 -306 C
ATOM 2709 CD ARG B 78 -14.786 2.130 2.735 1.00111.90 C
ANISOU 2709 CD ARG B 78 18242 10096 14178 35 7634 -141 C
ATOM 2710 NE ARG B 78 -15.287 0.915 3.374 1.00116.19 N
ANISOU 2710 NE ARG B 78 18827 10706 14615 74 7749 -27 N
ATOM 2711 CZ ARG B 78 -15.537 -0.221 2.728 1.00131.29 C
ANISOU 2711 CZ ARG B 78 20460 12740 16685 94 7561 123 C
ATOM 2712 NH1 ARG B 78 -15.318 -0.318 1.423 1.00142.60 N
ANISOU 2712 NH1 ARG B 78 21567 14247 18369 82 7243 163 N
ATOM 2713 NH2 ARG B 78 -15.995 -1.273 3.393 1.00134.79 N
ANISOU 2713 NH2 ARG B 78 20957 13242 17016 118 7690 232 N
ATOM 2714 N THR B 79 -9.824 5.761 1.886 1.00107.53 N
ANISOU 2714 N THR B 79 18260 9926 12669 -425 6472 -835 N
ATOM 2715 CA THR B 79 -9.299 6.950 1.242 1.00 99.70 C
ANISOU 2715 CA THR B 79 17188 8924 11768 -480 6357 -927 C
ATOM 2716 C THR B 79 -8.956 6.624 -0.208 1.00109.34 C
ANISOU 2716 C THR B 79 18040 10270 13235 -511 6027 -836 C
ATOM 2717 O THR B 79 -8.953 5.463 -0.620 1.00108.45 O
ANISOU 2717 O THR B 79 17785 10269 13150 -500 5847 -733 O
ATOM 2718 CB THR B 79 -8.058 7.455 1.984 1.00 94.89 C
ANISOU 2718 CB THR B 79 16928 8446 10679 -581 6134 -1121 C
ATOM 2719 OG1 THR B 79 -6.992 6.506 1.833 1.00 97.35 O
ANISOU 2719 OG1 THR B 79 17252 9015 10722 -650 5694 -1111 O
ATOM 2720 CG2 THR B 79 -8.339 7.616 3.478 1.00105.02 C
ANISOU 2720 CG2 THR B 79 18629 9620 11655 -566 6436 -1221 C
ATOM 2721 N VAL B 80 -8.682 7.665 -0.998 1.00110.54 N
ANISOU 2721 N VAL B 80 18039 10397 13565 -552 5961 -880 N
ATOM 2722 CA VAL B 80 -8.252 7.421 -2.370 1.00 96.46 C
ANISOU 2722 CA VAL B 80 15938 8743 11969 -599 5645 -813 C
ATOM 2723 C VAL B 80 -6.985 6.581 -2.383 1.00 91.12 C
ANISOU 2723 C VAL B 80 15356 8348 10917 -677 5207 -861 C
ATOM 2724 O VAL B 80 -6.858 5.632 -3.168 1.00 95.31 O
ANISOU 2724 O VAL B 80 15687 8993 11533 -682 4992 -772 O
ATOM 2725 CB VAL B 80 -8.065 8.755 -3.115 1.00 99.84 C
ANISOU 2725 CB VAL B 80 16220 9113 12602 -642 5652 -865 C
ATOM 2726 CG1 VAL B 80 -7.567 8.507 -4.538 1.00 96.56 C
ANISOU 2726 CG1 VAL B 80 15498 8841 12349 -705 5331 -804 C
ATOM 2727 CG2 VAL B 80 -9.372 9.510 -3.118 1.00102.96 C
ANISOU 2727 CG2 VAL B 80 16483 9210 13425 -551 6099 -786 C
ATOM 2728 N THR B 81 -6.035 6.902 -1.503 1.00 88.91 N
ANISOU 2728 N THR B 81 15380 8171 10231 -733 5072 -1004 N
ATOM 2729 CA THR B 81 -4.772 6.175 -1.484 1.00 82.52 C
ANISOU 2729 CA THR B 81 14640 7616 9100 -798 4653 -1038 C
ATOM 2730 C THR B 81 -4.960 4.729 -1.048 1.00 79.57 C
ANISOU 2730 C THR B 81 14320 7304 8609 -758 4623 -943 C
ATOM 2731 O THR B 81 -4.302 3.824 -1.575 1.00 77.11 O
ANISOU 2731 O THR B 81 13892 7168 8238 -780 4318 -893 O
ATOM 2732 CB THR B 81 -3.785 6.870 -0.555 1.00 83.50 C
ANISOU 2732 CB THR B 81 15081 7802 8842 -862 4526 -1205 C
ATOM 2733 OG1 THR B 81 -3.458 8.152 -1.097 1.00 92.80 O
ANISOU 2733 OG1 THR B 81 16183 8949 10127 -903 4490 -1298 O
ATOM 2734 CG2 THR B 81 -2.543 6.027 -0.421 1.00 68.19 C
ANISOU 2734 CG2 THR B 81 13207 6101 6602 -915 4118 -1213 C
ATOM 2735 N ASN B 82 -5.835 4.495 -0.071 1.00 85.85 N
ANISOU 2735 N ASN B 82 15298 7955 9365 -698 4948 -920 N
ATOM 2736 CA ASN B 82 -6.058 3.137 0.405 1.00 81.99 C
ANISOU 2736 CA ASN B 82 14873 7521 8759 -660 4943 -828 C
ATOM 2737 C ASN B 82 -6.876 2.323 -0.593 1.00 77.49 C
ANISOU 2737 C ASN B 82 13969 6919 8556 -597 4980 -676 C
ATOM 2738 O ASN B 82 -6.683 1.108 -0.694 1.00 81.80 O
ANISOU 2738 O ASN B 82 14472 7581 9027 -588 4814 -602 O
ATOM 2739 CB ASN B 82 -6.711 3.166 1.787 1.00 87.16 C
ANISOU 2739 CB ASN B 82 15841 8043 9232 -623 5289 -856 C
ATOM 2740 CG ASN B 82 -5.726 3.531 2.887 1.00 94.09 C
ANISOU 2740 CG ASN B 82 17104 9002 9644 -702 5164 -1001 C
ATOM 2741 OD1 ASN B 82 -4.518 3.322 2.752 1.00 87.06 O
ANISOU 2741 OD1 ASN B 82 16244 8300 8537 -774 4778 -1043 O
ATOM 2742 ND2 ASN B 82 -6.239 4.078 3.982 1.00109.22 N
ANISOU 2742 ND2 ASN B 82 19318 10770 11411 -690 5495 -1078 N
ATOM 2743 N TYR B 83 -7.801 2.955 -1.324 1.00 84.25 N
ANISOU 2743 N TYR B 83 14586 7609 9818 -550 5195 -626 N
ATOM 2744 CA TYR B 83 -8.458 2.257 -2.429 1.00 84.50 C
ANISOU 2744 CA TYR B 83 14274 7625 10206 -498 5160 -496 C
ATOM 2745 C TYR B 83 -7.451 1.816 -3.483 1.00 81.04 C
ANISOU 2745 C TYR B 83 13682 7392 9718 -571 4743 -509 C
ATOM 2746 O TYR B 83 -7.611 0.755 -4.097 1.00 70.98 O
ANISOU 2746 O TYR B 83 12238 6194 8539 -545 4615 -428 O
ATOM 2747 CB TYR B 83 -9.541 3.142 -3.054 1.00 90.35 C
ANISOU 2747 CB TYR B 83 14773 8146 11411 -433 5434 -439 C
ATOM 2748 CG TYR B 83 -10.915 3.000 -2.447 1.00 96.11 C
ANISOU 2748 CG TYR B 83 15475 8673 12369 -311 5843 -337 C
ATOM 2749 CD1 TYR B 83 -11.263 1.847 -1.753 1.00 91.72 C
ANISOU 2749 CD1 TYR B 83 15010 8168 11672 -265 5911 -269 C
ATOM 2750 CD2 TYR B 83 -11.856 4.015 -2.539 1.00 98.26 C
ANISOU 2750 CD2 TYR B 83 15624 8703 13009 -241 6176 -297 C
ATOM 2751 CE1 TYR B 83 -12.523 1.697 -1.204 1.00 92.19 C
ANISOU 2751 CE1 TYR B 83 15023 8058 11945 -154 6295 -162 C
ATOM 2752 CE2 TYR B 83 -13.116 3.878 -1.979 1.00 99.56 C
ANISOU 2752 CE2 TYR B 83 15740 8680 13409 -119 6564 -187 C
ATOM 2753 CZ TYR B 83 -13.443 2.714 -1.311 1.00 93.61 C
ANISOU 2753 CZ TYR B 83 15070 7998 12498 -78 6622 -121 C
ATOM 2754 OH TYR B 83 -14.692 2.568 -0.753 1.00 95.21 O
ANISOU 2754 OH TYR B 83 15209 8029 12937 41 7018 0 O
ATOM 2755 N PHE B 84 -6.417 2.624 -3.721 1.00 91.71 N
ANISOU 2755 N PHE B 84 15083 8840 10924 -659 4537 -611 N
ATOM 2756 CA PHE B 84 -5.346 2.198 -4.614 1.00 83.45 C
ANISOU 2756 CA PHE B 84 13913 8002 9792 -727 4151 -626 C
ATOM 2757 C PHE B 84 -4.477 1.132 -3.970 1.00 81.33 C
ANISOU 2757 C PHE B 84 13820 7906 9176 -739 3927 -631 C
ATOM 2758 O PHE B 84 -4.076 0.172 -4.635 1.00 79.58 O
ANISOU 2758 O PHE B 84 13471 7808 8959 -745 3706 -582 O
ATOM 2759 CB PHE B 84 -4.501 3.391 -5.047 1.00 79.26 C
ANISOU 2759 CB PHE B 84 13360 7535 9221 -809 4006 -724 C
ATOM 2760 CG PHE B 84 -5.116 4.192 -6.148 1.00 66.29 C
ANISOU 2760 CG PHE B 84 11460 5771 7956 -818 4119 -696 C
ATOM 2761 CD1 PHE B 84 -5.414 3.582 -7.355 1.00 57.07 C
ANISOU 2761 CD1 PHE B 84 10025 4623 7036 -810 4016 -628 C
ATOM 2762 CD2 PHE B 84 -5.387 5.541 -5.991 1.00 61.50 C
ANISOU 2762 CD2 PHE B 84 10881 5026 7458 -830 4324 -748 C
ATOM 2763 CE1 PHE B 84 -5.975 4.292 -8.381 1.00 51.62 C
ANISOU 2763 CE1 PHE B 84 9095 3813 6704 -803 4098 -614 C
ATOM 2764 CE2 PHE B 84 -5.953 6.267 -7.018 1.00 58.30 C
ANISOU 2764 CE2 PHE B 84 10224 4494 7435 -837 4435 -707 C
ATOM 2765 CZ PHE B 84 -6.248 5.635 -8.218 1.00 56.46 C
ANISOU 2765 CZ PHE B 84 9721 4270 7459 -821 4313 -639 C
ATOM 2766 N LEU B 85 -4.166 1.280 -2.682 1.00 89.52 N
ANISOU 2766 N LEU B 85 15157 8945 9911 -742 3984 -691 N
ATOM 2767 CA LEU B 85 -3.334 0.275 -2.035 1.00 91.49 C
ANISOU 2767 CA LEU B 85 15576 9344 9842 -752 3771 -684 C
ATOM 2768 C LEU B 85 -4.009 -1.090 -2.061 1.00 98.71 C
ANISOU 2768 C LEU B 85 16432 10239 10836 -692 3846 -560 C
ATOM 2769 O LEU B 85 -3.326 -2.121 -2.051 1.00 96.92 O
ANISOU 2769 O LEU B 85 16232 10142 10452 -698 3626 -522 O
ATOM 2770 CB LEU B 85 -3.007 0.707 -0.602 1.00 84.70 C
ANISOU 2770 CB LEU B 85 15073 8466 8642 -774 3846 -771 C
ATOM 2771 CG LEU B 85 -2.091 1.933 -0.489 1.00 76.97 C
ANISOU 2771 CG LEU B 85 14188 7539 7519 -844 3699 -909 C
ATOM 2772 CD1 LEU B 85 -1.755 2.203 0.965 1.00 62.90 C
ANISOU 2772 CD1 LEU B 85 12794 5738 5367 -879 3750 -999 C
ATOM 2773 CD2 LEU B 85 -0.825 1.772 -1.328 1.00 67.51 C
ANISOU 2773 CD2 LEU B 85 12821 6542 6287 -889 3298 -922 C
ATOM 2774 N VAL B 86 -5.343 -1.114 -2.075 1.00 98.02 N
ANISOU 2774 N VAL B 86 16260 9984 11000 -629 4162 -493 N
ATOM 2775 CA VAL B 86 -6.065 -2.369 -2.248 1.00 84.97 C
ANISOU 2775 CA VAL B 86 14497 8318 9470 -571 4230 -369 C
ATOM 2776 C VAL B 86 -5.847 -2.924 -3.649 1.00 80.26 C
ANISOU 2776 C VAL B 86 13614 7811 9071 -584 3997 -330 C
ATOM 2777 O VAL B 86 -5.593 -4.121 -3.837 1.00 86.73 O
ANISOU 2777 O VAL B 86 14408 8721 9824 -580 3852 -267 O
ATOM 2778 CB VAL B 86 -7.558 -2.161 -1.938 1.00 75.27 C
ANISOU 2778 CB VAL B 86 13208 6898 8494 -489 4628 -300 C
ATOM 2779 CG1 VAL B 86 -8.395 -3.323 -2.474 1.00 75.99 C
ANISOU 2779 CG1 VAL B 86 13068 6995 8809 -431 4667 -159 C
ATOM 2780 CG2 VAL B 86 -7.730 -1.997 -0.446 1.00 68.21 C
ANISOU 2780 CG2 VAL B 86 12644 5938 7336 -478 4862 -329 C
ATOM 2781 N ASN B 87 -5.921 -2.053 -4.652 1.00 76.77 N
ANISOU 2781 N ASN B 87 12968 7340 8862 -606 3963 -369 N
ATOM 2782 CA ASN B 87 -5.696 -2.496 -6.019 1.00 79.71 C
ANISOU 2782 CA ASN B 87 13085 7805 9395 -630 3745 -350 C
ATOM 2783 C ASN B 87 -4.282 -3.030 -6.208 1.00 71.57 C
ANISOU 2783 C ASN B 87 12128 6955 8109 -693 3415 -389 C
ATOM 2784 O ASN B 87 -4.070 -3.978 -6.972 1.00 58.79 O
ANISOU 2784 O ASN B 87 10392 5418 6528 -699 3258 -351 O
ATOM 2785 CB ASN B 87 -5.964 -1.350 -6.985 1.00 83.84 C
ANISOU 2785 CB ASN B 87 13402 8270 10182 -649 3771 -393 C
ATOM 2786 CG ASN B 87 -5.958 -1.793 -8.403 1.00 76.33 C
ANISOU 2786 CG ASN B 87 12177 7424 9403 -664 3582 -374 C
ATOM 2787 OD1 ASN B 87 -6.690 -2.709 -8.767 1.00 71.90 O
ANISOU 2787 OD1 ASN B 87 11454 6896 8969 -617 3600 -278 O
ATOM 2788 ND2 ASN B 87 -5.151 -1.146 -9.227 1.00 77.70 N
ANISOU 2788 ND2 ASN B 87 12280 7675 9568 -741 3394 -451 N
ATOM 2789 N LEU B 88 -3.297 -2.434 -5.531 1.00 73.93 N
ANISOU 2789 N LEU B 88 12610 7327 8153 -732 3305 -463 N
ATOM 2790 CA LEU B 88 -1.941 -2.964 -5.615 1.00 66.24 C
ANISOU 2790 CA LEU B 88 11681 6533 6954 -762 2996 -486 C
ATOM 2791 C LEU B 88 -1.858 -4.364 -5.020 1.00 86.35 C
ANISOU 2791 C LEU B 88 14359 9105 9343 -720 2968 -411 C
ATOM 2792 O LEU B 88 -1.136 -5.222 -5.540 1.00 90.52 O
ANISOU 2792 O LEU B 88 14835 9736 9824 -722 2762 -386 O
ATOM 2793 CB LEU B 88 -0.955 -2.024 -4.924 1.00 53.60 C
ANISOU 2793 CB LEU B 88 10235 5013 5117 -799 2880 -582 C
ATOM 2794 CG LEU B 88 0.497 -2.522 -4.905 1.00 53.35 C
ANISOU 2794 CG LEU B 88 10240 5170 4862 -812 2559 -604 C
ATOM 2795 CD1 LEU B 88 1.003 -2.801 -6.315 1.00 55.59 C
ANISOU 2795 CD1 LEU B 88 10261 5557 5303 -828 2370 -594 C
ATOM 2796 CD2 LEU B 88 1.394 -1.535 -4.193 1.00 60.98 C
ANISOU 2796 CD2 LEU B 88 11356 6203 5609 -852 2444 -706 C
ATOM 2797 N SER B 89 -2.600 -4.623 -3.937 1.00 90.29 N
ANISOU 2797 N SER B 89 15037 9505 9762 -681 3190 -369 N
ATOM 2798 CA SER B 89 -2.583 -5.961 -3.358 1.00 78.07 C
ANISOU 2798 CA SER B 89 13620 7977 8066 -648 3180 -281 C
ATOM 2799 C SER B 89 -3.209 -6.990 -4.292 1.00 78.10 C
ANISOU 2799 C SER B 89 13423 7953 8297 -623 3197 -191 C
ATOM 2800 O SER B 89 -2.769 -8.146 -4.319 1.00 78.71 O
ANISOU 2800 O SER B 89 13550 8082 8275 -613 3073 -128 O
ATOM 2801 CB SER B 89 -3.289 -5.940 -2.010 1.00 75.85 C
ANISOU 2801 CB SER B 89 13570 7604 7646 -622 3436 -252 C
ATOM 2802 OG SER B 89 -2.717 -4.936 -1.194 1.00 74.30 O
ANISOU 2802 OG SER B 89 13575 7427 7228 -660 3419 -353 O
ATOM 2803 N LEU B 90 -4.224 -6.598 -5.065 1.00 76.43 N
ANISOU 2803 N LEU B 90 12989 7662 8389 -613 3342 -179 N
ATOM 2804 CA LEU B 90 -4.856 -7.561 -5.959 1.00 67.48 C
ANISOU 2804 CA LEU B 90 11650 6528 7462 -601 3337 -93 C
ATOM 2805 C LEU B 90 -3.893 -8.015 -7.051 1.00 64.76 C
ANISOU 2805 C LEU B 90 11218 6286 7103 -646 3063 -130 C
ATOM 2806 O LEU B 90 -3.862 -9.201 -7.400 1.00 67.86 O
ANISOU 2806 O LEU B 90 11589 6699 7497 -646 2992 -61 O
ATOM 2807 CB LEU B 90 -6.133 -6.974 -6.553 1.00 54.84 C
ANISOU 2807 CB LEU B 90 9795 4852 6189 -578 3520 -60 C
ATOM 2808 CG LEU B 90 -7.215 -6.534 -5.566 1.00 63.09 C
ANISOU 2808 CG LEU B 90 10894 5770 7307 -518 3840 -10 C
ATOM 2809 CD1 LEU B 90 -8.183 -5.581 -6.247 1.00 72.06 C
ANISOU 2809 CD1 LEU B 90 11767 6832 8779 -488 3980 1 C
ATOM 2810 CD2 LEU B 90 -7.956 -7.732 -4.982 1.00 65.97 C
ANISOU 2810 CD2 LEU B 90 11275 6122 7670 -486 3968 138 C
ATOM 2811 N ALA B 91 -3.091 -7.093 -7.593 1.00 55.57 N
ANISOU 2811 N ALA B 91 10007 5183 5925 -691 2916 -230 N
ATOM 2812 CA ALA B 91 -2.075 -7.487 -8.567 1.00 52.44 C
ANISOU 2812 CA ALA B 91 9540 4890 5494 -733 2672 -265 C
ATOM 2813 C ALA B 91 -1.029 -8.398 -7.939 1.00 63.26 C
ANISOU 2813 C ALA B 91 11104 6323 6608 -705 2531 -239 C
ATOM 2814 O ALA B 91 -0.565 -9.355 -8.575 1.00 76.56 O
ANISOU 2814 O ALA B 91 12771 8034 8284 -705 2417 -217 O
ATOM 2815 CB ALA B 91 -1.410 -6.252 -9.173 1.00 55.00 C
ANISOU 2815 CB ALA B 91 9759 5290 5847 -789 2551 -358 C
ATOM 2816 N ASP B 92 -0.621 -8.098 -6.701 1.00 55.82 N
ANISOU 2816 N ASP B 92 10360 5403 5447 -681 2537 -245 N
ATOM 2817 CA ASP B 92 0.358 -8.940 -6.026 1.00 62.15 C
ANISOU 2817 CA ASP B 92 11353 6269 5992 -647 2392 -210 C
ATOM 2818 C ASP B 92 -0.193 -10.340 -5.804 1.00 75.78 C
ANISOU 2818 C ASP B 92 13168 7910 7715 -611 2483 -92 C
ATOM 2819 O ASP B 92 0.561 -11.317 -5.860 1.00 77.21 O
ANISOU 2819 O ASP B 92 13441 8117 7779 -583 2349 -44 O
ATOM 2820 CB ASP B 92 0.769 -8.305 -4.699 1.00 62.91 C
ANISOU 2820 CB ASP B 92 11662 6403 5839 -648 2385 -240 C
ATOM 2821 CG ASP B 92 1.465 -6.978 -4.873 1.00 76.97 C
ANISOU 2821 CG ASP B 92 13370 8276 7599 -689 2265 -353 C
ATOM 2822 OD1 ASP B 92 1.957 -6.704 -5.990 1.00 67.16 O
ANISOU 2822 OD1 ASP B 92 11921 7110 6488 -706 2132 -397 O
ATOM 2823 OD2 ASP B 92 1.522 -6.208 -3.884 1.00 92.75 O
ANISOU 2823 OD2 ASP B 92 15531 10271 9439 -709 2310 -399 O
ATOM 2824 N VAL B 93 -1.500 -10.459 -5.563 1.00 77.85 N
ANISOU 2824 N VAL B 93 13395 8070 8115 -606 2714 -34 N
ATOM 2825 CA VAL B 93 -2.089 -11.776 -5.362 1.00 67.08 C
ANISOU 2825 CA VAL B 93 12076 6640 6769 -582 2798 98 C
ATOM 2826 C VAL B 93 -2.188 -12.510 -6.695 1.00 64.04 C
ANISOU 2826 C VAL B 93 11514 6241 6580 -604 2721 117 C
ATOM 2827 O VAL B 93 -1.870 -13.701 -6.795 1.00 65.00 O
ANISOU 2827 O VAL B 93 11715 6334 6649 -591 2648 198 O
ATOM 2828 CB VAL B 93 -3.458 -11.657 -4.665 1.00 58.70 C
ANISOU 2828 CB VAL B 93 10996 5502 5805 -569 3069 171 C
ATOM 2829 CG1 VAL B 93 -4.124 -13.019 -4.580 1.00 61.66 C
ANISOU 2829 CG1 VAL B 93 11354 5829 6244 -562 3136 333 C
ATOM 2830 CG2 VAL B 93 -3.309 -11.037 -3.279 1.00 62.65 C
ANISOU 2830 CG2 VAL B 93 11734 6004 6065 -557 3161 146 C
ATOM 2831 N LEU B 94 -2.650 -11.815 -7.736 1.00 64.02 N
ANISOU 2831 N LEU B 94 11278 6249 6799 -643 2732 49 N
ATOM 2832 CA LEU B 94 -2.640 -12.392 -9.076 1.00 63.97 C
ANISOU 2832 CA LEU B 94 11114 6250 6942 -689 2630 45 C
ATOM 2833 C LEU B 94 -1.258 -12.929 -9.439 1.00 59.56 C
ANISOU 2833 C LEU B 94 10691 5717 6220 -682 2447 -2 C
ATOM 2834 O LEU B 94 -1.127 -14.044 -9.956 1.00 65.21 O
ANISOU 2834 O LEU B 94 11438 6382 6957 -690 2398 50 O
ATOM 2835 CB LEU B 94 -3.088 -11.344 -10.089 1.00 71.43 C
ANISOU 2835 CB LEU B 94 11812 7239 8087 -741 2623 -32 C
ATOM 2836 CG LEU B 94 -2.675 -11.627 -11.532 1.00 68.53 C
ANISOU 2836 CG LEU B 94 11324 6922 7795 -810 2465 -84 C
ATOM 2837 CD1 LEU B 94 -3.517 -12.743 -12.145 1.00 75.21 C
ANISOU 2837 CD1 LEU B 94 12042 7734 8798 -856 2443 37 C
ATOM 2838 CD2 LEU B 94 -2.772 -10.335 -12.316 1.00 52.68 C
ANISOU 2838 CD2 LEU B 94 9127 4987 5903 -856 2429 -172 C
ATOM 2839 N ALA B 95 -0.213 -12.135 -9.188 1.00 56.42 N
ANISOU 2839 N ALA B 95 10356 5405 5677 -667 2337 -86 N
ATOM 2840 CA ALA B 95 1.153 -12.593 -9.428 1.00 54.37 C
ANISOU 2840 CA ALA B 95 10189 5206 5262 -632 2158 -112 C
ATOM 2841 C ALA B 95 1.515 -13.734 -8.490 1.00 62.89 C
ANISOU 2841 C ALA B 95 11515 6230 6149 -558 2144 1 C
ATOM 2842 O ALA B 95 2.055 -14.760 -8.921 1.00 67.37 O
ANISOU 2842 O ALA B 95 12173 6745 6680 -521 2082 44 O
ATOM 2843 CB ALA B 95 2.141 -11.440 -9.269 1.00 52.91 C
ANISOU 2843 CB ALA B 95 9947 5176 4979 -627 2011 -206 C
ATOM 2844 N THR B 96 1.248 -13.562 -7.195 1.00 70.10 N
ANISOU 2844 N THR B 96 12560 7145 6929 -537 2203 60 N
ATOM 2845 CA THR B 96 1.659 -14.563 -6.220 1.00 71.56 C
ANISOU 2845 CA THR B 96 12990 7296 6905 -480 2159 188 C
ATOM 2846 C THR B 96 0.895 -15.868 -6.408 1.00 72.80 C
ANISOU 2846 C THR B 96 13166 7312 7185 -477 2255 327 C
ATOM 2847 O THR B 96 1.498 -16.943 -6.500 1.00 73.37 O
ANISOU 2847 O THR B 96 13365 7313 7200 -429 2157 425 O
ATOM 2848 CB THR B 96 1.464 -14.028 -4.805 1.00 68.85 C
ANISOU 2848 CB THR B 96 12789 6993 6378 -486 2211 212 C
ATOM 2849 OG1 THR B 96 2.422 -12.992 -4.550 1.00 57.32 O
ANISOU 2849 OG1 THR B 96 11346 5661 4771 -496 2059 105 O
ATOM 2850 CG2 THR B 96 1.653 -15.153 -3.798 1.00 80.27 C
ANISOU 2850 CG2 THR B 96 14476 8395 7626 -450 2179 381 C
ATOM 2851 N ALA B 97 -0.436 -15.797 -6.459 1.00 74.75 N
ANISOU 2851 N ALA B 97 13270 7510 7622 -524 2433 354 N
ATOM 2852 CA ALA B 97 -1.238 -17.017 -6.459 1.00 74.34 C
ANISOU 2852 CA ALA B 97 13200 7348 7698 -537 2501 509 C
ATOM 2853 C ALA B 97 -1.025 -17.827 -7.735 1.00 66.79 C
ANISOU 2853 C ALA B 97 12161 6310 6907 -559 2398 505 C
ATOM 2854 O ALA B 97 -0.800 -19.042 -7.678 1.00 66.79 O
ANISOU 2854 O ALA B 97 12266 6195 6915 -533 2329 624 O
ATOM 2855 CB ALA B 97 -2.711 -16.665 -6.268 1.00 79.88 C
ANISOU 2855 CB ALA B 97 13722 8046 8583 -582 2697 550 C
ATOM 2856 N ILE B 98 -1.104 -17.176 -8.897 1.00 56.42 N
ANISOU 2856 N ILE B 98 10664 5038 5735 -612 2378 371 N
ATOM 2857 CA ILE B 98 -1.019 -17.865 -10.185 1.00 59.35 C
ANISOU 2857 CA ILE B 98 10951 5332 6266 -659 2286 344 C
ATOM 2858 C ILE B 98 0.425 -18.009 -10.643 1.00 64.39 C
ANISOU 2858 C ILE B 98 11753 5941 6771 -604 2170 267 C
ATOM 2859 O ILE B 98 0.916 -19.129 -10.829 1.00 77.93 O
ANISOU 2859 O ILE B 98 13591 7504 8514 -555 2089 327 O
ATOM 2860 CB ILE B 98 -1.848 -17.132 -11.260 1.00 61.10 C
ANISOU 2860 CB ILE B 98 10891 5627 6696 -761 2297 260 C
ATOM 2861 CG1 ILE B 98 -3.347 -17.401 -11.075 1.00 75.10 C
ANISOU 2861 CG1 ILE B 98 12473 7384 8678 -816 2370 397 C
ATOM 2862 CG2 ILE B 98 -1.414 -17.535 -12.668 1.00 50.66 C
ANISOU 2862 CG2 ILE B 98 9522 4266 5459 -821 2169 170 C
ATOM 2863 CD1 ILE B 98 -4.259 -16.338 -11.720 1.00 77.13 C
ANISOU 2863 CD1 ILE B 98 12447 7740 9119 -883 2391 365 C
ATOM 2864 N CYS B 99 1.107 -16.876 -10.825 1.00 61.06 N
ANISOU 2864 N CYS B 99 11314 5655 6233 -601 2153 140 N
ATOM 2865 CA CYS B 99 2.418 -16.893 -11.464 1.00 61.94 C
ANISOU 2865 CA CYS B 99 11447 5813 6273 -535 2012 29 C
ATOM 2866 C CYS B 99 3.502 -17.468 -10.555 1.00 71.98 C
ANISOU 2866 C CYS B 99 12865 7096 7389 -377 1866 91 C
ATOM 2867 O CYS B 99 4.314 -18.287 -11.007 1.00 78.25 O
ANISOU 2867 O CYS B 99 13626 7830 8277 -267 1723 56 O
ATOM 2868 CB CYS B 99 2.789 -15.493 -11.949 1.00 55.08 C
ANISOU 2868 CB CYS B 99 10426 5146 5357 -576 1994 -139 C
ATOM 2869 SG CYS B 99 1.446 -14.679 -12.828 1.00 53.69 S
ANISOU 2869 SG CYS B 99 10013 4964 5424 -746 2095 -176 S
ATOM 2870 N LEU B 100 3.525 -17.081 -9.279 1.00 76.20 N
ANISOU 2870 N LEU B 100 13568 7693 7690 -364 1901 192 N
ATOM 2871 CA LEU B 100 4.641 -17.470 -8.419 1.00 70.33 C
ANISOU 2871 CA LEU B 100 12954 6990 6779 -238 1707 263 C
ATOM 2872 C LEU B 100 4.888 -18.976 -8.424 1.00 60.41 C
ANISOU 2872 C LEU B 100 11753 5542 5659 -134 1610 395 C
ATOM 2873 O LEU B 100 6.046 -19.387 -8.586 1.00 67.62 O
ANISOU 2873 O LEU B 100 12601 6468 6622 2 1408 372 O
ATOM 2874 CB LEU B 100 4.412 -16.968 -6.995 1.00 66.42 C
ANISOU 2874 CB LEU B 100 12676 6560 5999 -277 1762 367 C
ATOM 2875 CG LEU B 100 5.561 -17.369 -6.052 1.00 60.75 C
ANISOU 2875 CG LEU B 100 12137 5884 5061 -180 1524 485 C
ATOM 2876 CD1 LEU B 100 5.927 -16.297 -5.022 1.00 66.74 C
ANISOU 2876 CD1 LEU B 100 12976 6817 5567 -231 1439 435 C
ATOM 2877 CD2 LEU B 100 5.264 -18.704 -5.395 1.00 56.88 C
ANISOU 2877 CD2 LEU B 100 11825 5210 4576 -137 1522 726 C
ATOM 2878 N PRO B 101 3.880 -19.840 -8.287 1.00 54.35 N
ANISOU 2878 N PRO B 101 11082 4579 4988 -188 1743 541 N
ATOM 2879 CA PRO B 101 4.134 -21.283 -8.436 1.00 58.95 C
ANISOU 2879 CA PRO B 101 11710 4946 5743 -92 1642 646 C
ATOM 2880 C PRO B 101 4.716 -21.630 -9.801 1.00 68.12 C
ANISOU 2880 C PRO B 101 12685 6054 7144 -22 1558 455 C
ATOM 2881 O PRO B 101 5.530 -22.550 -9.914 1.00 76.88 O
ANISOU 2881 O PRO B 101 13796 7043 8370 128 1424 478 O
ATOM 2882 CB PRO B 101 2.746 -21.906 -8.238 1.00 54.14 C
ANISOU 2882 CB PRO B 101 11191 4155 5223 -216 1828 805 C
ATOM 2883 CG PRO B 101 1.985 -20.884 -7.477 1.00 47.21 C
ANISOU 2883 CG PRO B 101 10256 3489 4193 -306 1962 785 C
ATOM 2884 CD PRO B 101 2.469 -19.555 -7.950 1.00 44.99 C
ANISOU 2884 CD PRO B 101 9910 3374 3810 -326 1971 605 C
ATOM 2885 N ALA B 102 4.283 -20.927 -10.864 1.00 70.22 N
ANISOU 2885 N ALA B 102 12796 6393 7490 -132 1646 272 N
ATOM 2886 CA ALA B 102 4.816 -21.227 -12.179 1.00 65.85 C
ANISOU 2886 CA ALA B 102 12106 5799 7116 -86 1590 80 C
ATOM 2887 C ALA B 102 6.286 -20.849 -12.282 1.00 69.88 C
ANISOU 2887 C ALA B 102 12497 6469 7585 75 1449 -30 C
ATOM 2888 O ALA B 102 7.079 -21.590 -12.871 1.00 66.00 O
ANISOU 2888 O ALA B 102 11952 5880 7246 213 1386 -104 O
ATOM 2889 CB ALA B 102 3.987 -20.507 -13.242 1.00 57.96 C
ANISOU 2889 CB ALA B 102 10988 4856 6179 -269 1695 -59 C
ATOM 2890 N SER B 103 6.676 -19.712 -11.712 1.00 75.61 N
ANISOU 2890 N SER B 103 13179 7426 8126 60 1406 -40 N
ATOM 2891 CA SER B 103 8.083 -19.338 -11.770 1.00 68.44 C
ANISOU 2891 CA SER B 103 12132 6672 7201 194 1249 -114 C
ATOM 2892 C SER B 103 8.961 -20.256 -10.934 1.00 70.32 C
ANISOU 2892 C SER B 103 12437 6818 7462 373 1083 54 C
ATOM 2893 O SER B 103 10.126 -20.481 -11.283 1.00 76.80 O
ANISOU 2893 O SER B 103 13104 7666 8412 529 967 10 O
ATOM 2894 CB SER B 103 8.257 -17.883 -11.353 1.00 71.14 C
ANISOU 2894 CB SER B 103 12427 7261 7341 106 1220 -163 C
ATOM 2895 OG SER B 103 7.471 -17.042 -12.173 1.00 68.44 O
ANISOU 2895 OG SER B 103 12001 6986 7019 -48 1364 -299 O
ATOM 2896 N LEU B 104 8.430 -20.782 -9.832 1.00 61.78 N
ANISOU 2896 N LEU B 104 11571 5630 6274 354 1073 267 N
ATOM 2897 CA LEU B 104 9.220 -21.673 -8.993 1.00 58.97 C
ANISOU 2897 CA LEU B 104 11290 5177 5939 510 888 468 C
ATOM 2898 C LEU B 104 9.618 -22.925 -9.764 1.00 68.37 C
ANISOU 2898 C LEU B 104 12403 6131 7443 672 881 446 C
ATOM 2899 O LEU B 104 10.794 -23.311 -9.777 1.00 78.87 O
ANISOU 2899 O LEU B 104 13607 7447 8915 858 729 480 O
ATOM 2900 CB LEU B 104 8.438 -22.056 -7.739 1.00 65.58 C
ANISOU 2900 CB LEU B 104 12402 5928 6587 433 910 709 C
ATOM 2901 CG LEU B 104 9.178 -23.084 -6.884 1.00 70.66 C
ANISOU 2901 CG LEU B 104 13140 6444 7263 580 699 957 C
ATOM 2902 CD1 LEU B 104 10.400 -22.452 -6.227 1.00 73.79 C
ANISOU 2902 CD1 LEU B 104 13479 7046 7514 641 439 1014 C
ATOM 2903 CD2 LEU B 104 8.246 -23.708 -5.862 1.00 74.36 C
ANISOU 2903 CD2 LEU B 104 13892 6775 7587 494 767 1202 C
ATOM 2904 N LEU B 105 8.643 -23.580 -10.410 1.00 70.63 N
ANISOU 2904 N LEU B 105 12763 6215 7857 601 1046 395 N
ATOM 2905 CA LEU B 105 8.933 -24.805 -11.150 1.00 64.75 C
ANISOU 2905 CA LEU B 105 11999 5204 7398 739 1060 349 C
ATOM 2906 C LEU B 105 9.854 -24.516 -12.329 1.00 64.26 C
ANISOU 2906 C LEU B 105 11716 5222 7479 844 1083 100 C
ATOM 2907 O LEU B 105 10.730 -25.322 -12.653 1.00 82.85 O
ANISOU 2907 O LEU B 105 13996 7427 10056 1048 1047 82 O
ATOM 2908 CB LEU B 105 7.629 -25.445 -11.650 1.00 60.65 C
ANISOU 2908 CB LEU B 105 11622 4460 6962 589 1215 328 C
ATOM 2909 CG LEU B 105 6.865 -26.440 -10.771 1.00 71.46 C
ANISOU 2909 CG LEU B 105 13207 5591 8353 552 1212 588 C
ATOM 2910 CD1 LEU B 105 5.953 -25.709 -9.776 1.00 83.26 C
ANISOU 2910 CD1 LEU B 105 14807 7238 9589 377 1275 748 C
ATOM 2911 CD2 LEU B 105 6.032 -27.409 -11.620 1.00 77.18 C
ANISOU 2911 CD2 LEU B 105 14019 6016 9289 469 1313 524 C
ATOM 2912 N VAL B 106 9.679 -23.367 -12.981 1.00 54.42 N
ANISOU 2912 N VAL B 106 10357 4202 6117 711 1160 -84 N
ATOM 2913 CA VAL B 106 10.457 -23.080 -14.183 1.00 61.51 C
ANISOU 2913 CA VAL B 106 11061 5181 7128 781 1216 -320 C
ATOM 2914 C VAL B 106 11.909 -22.797 -13.825 1.00 67.49 C
ANISOU 2914 C VAL B 106 11617 6086 7939 973 1074 -273 C
ATOM 2915 O VAL B 106 12.834 -23.312 -14.463 1.00 64.38 O
ANISOU 2915 O VAL B 106 11084 5616 7761 1159 1103 -358 O
ATOM 2916 CB VAL B 106 9.816 -21.910 -14.950 1.00 64.58 C
ANISOU 2916 CB VAL B 106 11390 5770 7379 565 1318 -493 C
ATOM 2917 CG1 VAL B 106 10.677 -21.501 -16.134 1.00 55.15 C
ANISOU 2917 CG1 VAL B 106 10000 4696 6258 620 1377 -716 C
ATOM 2918 CG2 VAL B 106 8.411 -22.284 -15.405 1.00 77.57 C
ANISOU 2918 CG2 VAL B 106 13196 7247 9029 375 1435 -517 C
ATOM 2919 N ASP B 107 12.132 -21.982 -12.791 1.00 83.00 N
ANISOU 2919 N ASP B 107 13567 8253 9716 927 921 -132 N
ATOM 2920 CA ASP B 107 13.500 -21.675 -12.386 1.00 79.66 C
ANISOU 2920 CA ASP B 107 12944 7975 9346 1075 735 -54 C
ATOM 2921 C ASP B 107 14.199 -22.897 -11.790 1.00 72.55 C
ANISOU 2921 C ASP B 107 12048 6866 8653 1299 600 152 C
ATOM 2922 O ASP B 107 15.426 -23.018 -11.879 1.00 71.61 O
ANISOU 2922 O ASP B 107 11697 6781 8730 1484 495 192 O
ATOM 2923 CB ASP B 107 13.501 -20.511 -11.389 1.00 86.29 C
ANISOU 2923 CB ASP B 107 13822 9061 9905 934 581 41 C
ATOM 2924 CG ASP B 107 13.422 -19.163 -12.067 1.00 88.02 C
ANISOU 2924 CG ASP B 107 13914 9517 10014 785 659 -159 C
ATOM 2925 OD1 ASP B 107 14.139 -18.965 -13.072 1.00 78.86 O
ANISOU 2925 OD1 ASP B 107 12522 8429 9013 854 712 -307 O
ATOM 2926 OD2 ASP B 107 12.633 -18.312 -11.595 1.00 89.67 O
ANISOU 2926 OD2 ASP B 107 14257 9827 9985 602 683 -163 O
ATOM 2927 N ILE B 108 13.439 -23.809 -11.183 1.00 73.20 N
ANISOU 2927 N ILE B 108 12369 6723 8719 1287 601 306 N
ATOM 2928 CA ILE B 108 14.023 -25.005 -10.581 1.00 76.23 C
ANISOU 2928 CA ILE B 108 12775 6879 9310 1492 462 532 C
ATOM 2929 C ILE B 108 14.341 -26.049 -11.643 1.00 87.98 C
ANISOU 2929 C ILE B 108 14179 8099 11149 1682 618 395 C
ATOM 2930 O ILE B 108 15.469 -26.549 -11.734 1.00 87.07 O
ANISOU 2930 O ILE B 108 13869 7904 11308 1922 547 453 O
ATOM 2931 CB ILE B 108 13.083 -25.566 -9.498 1.00 65.05 C
ANISOU 2931 CB ILE B 108 11662 5323 7733 1390 409 768 C
ATOM 2932 CG1 ILE B 108 13.088 -24.645 -8.276 1.00 78.67 C
ANISOU 2932 CG1 ILE B 108 13482 7295 9115 1253 230 933 C
ATOM 2933 CG2 ILE B 108 13.490 -26.982 -9.110 1.00 69.09 C
ANISOU 2933 CG2 ILE B 108 12219 5526 8508 1593 306 986 C
ATOM 2934 CD1 ILE B 108 12.147 -25.071 -7.182 1.00 91.08 C
ANISOU 2934 CD1 ILE B 108 15367 8764 10474 1134 217 1162 C
ATOM 2935 N THR B 109 13.353 -26.392 -12.467 1.00 91.64 N
ANISOU 2935 N THR B 109 14793 8408 11617 1575 835 211 N
ATOM 2936 CA THR B 109 13.545 -27.443 -13.460 1.00 84.01 C
ANISOU 2936 CA THR B 109 13826 7149 10946 1729 995 57 C
ATOM 2937 C THR B 109 14.208 -26.931 -14.734 1.00 88.02 C
ANISOU 2937 C THR B 109 14126 7780 11535 1786 1160 -235 C
ATOM 2938 O THR B 109 14.880 -27.701 -15.430 1.00 90.58 O
ANISOU 2938 O THR B 109 14378 7905 12135 1995 1281 -346 O
ATOM 2939 CB THR B 109 12.207 -28.096 -13.809 1.00 72.28 C
ANISOU 2939 CB THR B 109 12615 5421 9427 1561 1127 -7 C
ATOM 2940 OG1 THR B 109 11.535 -27.308 -14.799 1.00 68.63 O
ANISOU 2940 OG1 THR B 109 12161 5107 8809 1350 1280 -261 O
ATOM 2941 CG2 THR B 109 11.323 -28.203 -12.572 1.00 62.34 C
ANISOU 2941 CG2 THR B 109 11552 4140 7994 1420 1008 270 C
ATOM 2942 N GLU B 110 14.014 -25.657 -15.065 1.00 81.40 N
ANISOU 2942 N GLU B 110 13204 7255 10467 1603 1188 -362 N
ATOM 2943 CA GLU B 110 14.375 -25.115 -16.374 1.00 77.36 C
ANISOU 2943 CA GLU B 110 12550 6868 9975 1588 1371 -646 C
ATOM 2944 C GLU B 110 13.599 -25.799 -17.494 1.00 86.53 C
ANISOU 2944 C GLU B 110 13914 7794 11169 1507 1584 -874 C
ATOM 2945 O GLU B 110 14.094 -25.923 -18.617 1.00103.95 O
ANISOU 2945 O GLU B 110 16058 9967 13470 1580 1768 -1105 O
ATOM 2946 CB GLU B 110 15.873 -25.259 -16.652 1.00 87.09 C
ANISOU 2946 CB GLU B 110 13497 8129 11466 1863 1391 -662 C
ATOM 2947 CG GLU B 110 16.791 -24.272 -15.979 1.00 99.13 C
ANISOU 2947 CG GLU B 110 14753 9960 12953 1894 1196 -513 C
ATOM 2948 CD GLU B 110 18.240 -24.584 -16.307 1.00117.67 C
ANISOU 2948 CD GLU B 110 16788 12291 15632 2179 1233 -501 C
ATOM 2949 OE1 GLU B 110 18.483 -25.348 -17.269 1.00123.69 O
ANISOU 2949 OE1 GLU B 110 17546 12845 16605 2332 1481 -681 O
ATOM 2950 OE2 GLU B 110 19.140 -24.068 -15.619 1.00124.69 O
ANISOU 2950 OE2 GLU B 110 17434 13363 16579 2248 1023 -313 O
ATOM 2951 N SER B 111 12.372 -26.224 -17.207 1.00 81.67 N
ANISOU 2951 N SER B 111 13550 7016 10464 1336 1563 -808 N
ATOM 2952 CA SER B 111 11.450 -26.700 -18.222 1.00 86.84 C
ANISOU 2952 CA SER B 111 14415 7478 11104 1176 1710 -1004 C
ATOM 2953 C SER B 111 10.074 -26.104 -17.985 1.00 78.81 C
ANISOU 2953 C SER B 111 13516 6558 9870 870 1660 -935 C
ATOM 2954 O SER B 111 9.682 -25.831 -16.848 1.00 83.17 O
ANISOU 2954 O SER B 111 14083 7185 10333 823 1542 -705 O
ATOM 2955 CB SER B 111 11.358 -28.226 -18.210 1.00 96.52 C
ANISOU 2955 CB SER B 111 15765 8355 12553 1284 1712 -962 C
ATOM 2956 OG SER B 111 12.587 -28.804 -18.619 1.00103.43 O
ANISOU 2956 OG SER B 111 16513 9118 13666 1568 1800 -1058 O
ATOM 2957 N TRP B 112 9.332 -25.937 -19.069 1.00 71.58 N
ANISOU 2957 N TRP B 112 12551 5771 8875 630 1691 -1074 N
ATOM 2958 CA TRP B 112 7.927 -25.560 -19.009 1.00 67.54 C
ANISOU 2958 CA TRP B 112 12096 5333 8233 342 1642 -985 C
ATOM 2959 C TRP B 112 7.090 -26.829 -19.103 1.00 79.78 C
ANISOU 2959 C TRP B 112 13783 6631 9899 265 1608 -923 C
ATOM 2960 O TRP B 112 7.210 -27.582 -20.076 1.00 85.95 O
ANISOU 2960 O TRP B 112 14575 7318 10763 265 1631 -1072 O
ATOM 2961 CB TRP B 112 7.576 -24.587 -20.134 1.00 65.05 C
ANISOU 2961 CB TRP B 112 11636 5293 7786 130 1657 -1122 C
ATOM 2962 CG TRP B 112 6.160 -24.132 -20.098 1.00 66.52 C
ANISOU 2962 CG TRP B 112 11844 5545 7885 -140 1611 -1012 C
ATOM 2963 CD1 TRP B 112 5.115 -24.658 -20.789 1.00 71.96 C
ANISOU 2963 CD1 TRP B 112 12586 6156 8601 -334 1574 -1009 C
ATOM 2964 CD2 TRP B 112 5.624 -23.068 -19.304 1.00 68.19 C
ANISOU 2964 CD2 TRP B 112 12024 5896 7989 -236 1605 -883 C
ATOM 2965 NE1 TRP B 112 3.958 -23.983 -20.488 1.00 78.70 N
ANISOU 2965 NE1 TRP B 112 13409 7095 9396 -535 1546 -873 N
ATOM 2966 CE2 TRP B 112 4.244 -23.001 -19.576 1.00 76.32 C
ANISOU 2966 CE2 TRP B 112 13057 6925 9015 -476 1581 -798 C
ATOM 2967 CE3 TRP B 112 6.178 -22.160 -18.392 1.00 66.56 C
ANISOU 2967 CE3 TRP B 112 11792 5808 7689 -141 1617 -837 C
ATOM 2968 CZ2 TRP B 112 3.407 -22.062 -18.967 1.00 75.88 C
ANISOU 2968 CZ2 TRP B 112 12958 6978 8895 -606 1601 -667 C
ATOM 2969 CZ3 TRP B 112 5.345 -21.227 -17.789 1.00 61.81 C
ANISOU 2969 CZ3 TRP B 112 11184 5313 6988 -287 1630 -724 C
ATOM 2970 CH2 TRP B 112 3.976 -21.185 -18.079 1.00 67.95 C
ANISOU 2970 CH2 TRP B 112 11945 6078 7793 -509 1639 -638 C
ATOM 2971 N LEU B 113 6.257 -27.072 -18.090 1.00 84.64 N
ANISOU 2971 N LEU B 113 14506 7140 10514 195 1558 -701 N
ATOM 2972 CA LEU B 113 5.466 -28.291 -18.024 1.00 82.08 C
ANISOU 2972 CA LEU B 113 14291 6579 10317 123 1510 -608 C
ATOM 2973 C LEU B 113 3.968 -28.025 -18.097 1.00 81.53 C
ANISOU 2973 C LEU B 113 14210 6582 10186 -164 1478 -509 C
ATOM 2974 O LEU B 113 3.183 -28.961 -17.928 1.00 94.50 O
ANISOU 2974 O LEU B 113 15919 8047 11938 -247 1425 -400 O
ATOM 2975 CB LEU B 113 5.798 -29.071 -16.748 1.00 70.45 C
ANISOU 2975 CB LEU B 113 12927 4890 8952 306 1468 -388 C
ATOM 2976 CG LEU B 113 7.291 -29.239 -16.438 1.00 59.33 C
ANISOU 2976 CG LEU B 113 11506 3400 7637 623 1475 -413 C
ATOM 2977 CD1 LEU B 113 7.497 -29.764 -15.026 1.00 58.07 C
ANISOU 2977 CD1 LEU B 113 11457 3072 7535 770 1389 -116 C
ATOM 2978 CD2 LEU B 113 7.943 -30.160 -17.454 1.00 58.90 C
ANISOU 2978 CD2 LEU B 113 11416 3192 7771 749 1518 -619 C
ATOM 2979 N PHE B 114 3.541 -26.787 -18.343 1.00 72.65 N
ANISOU 2979 N PHE B 114 12979 5707 8919 -312 1502 -532 N
ATOM 2980 CA PHE B 114 2.120 -26.454 -18.366 1.00 74.65 C
ANISOU 2980 CA PHE B 114 13174 6033 9156 -559 1476 -415 C
ATOM 2981 C PHE B 114 1.544 -26.230 -19.765 1.00 78.53 C
ANISOU 2981 C PHE B 114 13590 6615 9634 -759 1425 -553 C
ATOM 2982 O PHE B 114 0.398 -25.779 -19.876 1.00 84.95 O
ANISOU 2982 O PHE B 114 14308 7515 10453 -955 1386 -454 O
ATOM 2983 CB PHE B 114 1.863 -25.219 -17.508 1.00 76.78 C
ANISOU 2983 CB PHE B 114 13373 6494 9305 -590 1538 -294 C
ATOM 2984 CG PHE B 114 2.585 -25.226 -16.189 1.00 81.39 C
ANISOU 2984 CG PHE B 114 14067 7023 9837 -399 1576 -170 C
ATOM 2985 CD1 PHE B 114 3.649 -24.367 -15.962 1.00 75.36 C
ANISOU 2985 CD1 PHE B 114 13305 6370 8957 -263 1604 -252 C
ATOM 2986 CD2 PHE B 114 2.195 -26.086 -15.176 1.00 90.71 C
ANISOU 2986 CD2 PHE B 114 15344 8046 11077 -362 1562 44 C
ATOM 2987 CE1 PHE B 114 4.302 -24.373 -14.740 1.00 74.45 C
ANISOU 2987 CE1 PHE B 114 13321 6187 8778 -96 1600 -113 C
ATOM 2988 CE2 PHE B 114 2.841 -26.095 -13.966 1.00 85.06 C
ANISOU 2988 CE2 PHE B 114 14749 7286 10282 -202 1569 192 C
ATOM 2989 CZ PHE B 114 3.896 -25.240 -13.743 1.00 76.86 C
ANISOU 2989 CZ PHE B 114 13745 6339 9118 -69 1578 122 C
ATOM 2990 N GLY B 115 2.279 -26.562 -20.829 1.00 66.93 N
ANISOU 2990 N GLY B 115 12152 5125 8153 -710 1420 -763 N
ATOM 2991 CA GLY B 115 1.716 -26.597 -22.165 1.00 71.58 C
ANISOU 2991 CA GLY B 115 12733 5753 8712 -906 1354 -877 C
ATOM 2992 C GLY B 115 1.726 -25.269 -22.909 1.00 83.58 C
ANISOU 2992 C GLY B 115 14118 7551 10087 -1019 1359 -946 C
ATOM 2993 O GLY B 115 2.094 -24.214 -22.387 1.00 86.50 O
ANISOU 2993 O GLY B 115 14381 8097 10389 -962 1416 -910 O
ATOM 2994 N HIS B 116 1.313 -25.339 -24.184 1.00 90.77 N
ANISOU 2994 N HIS B 116 15050 8491 10949 -1192 1288 -1043 N
ATOM 2995 CA HIS B 116 1.375 -24.159 -25.049 1.00 78.25 C
ANISOU 2995 CA HIS B 116 13350 7154 9226 -1306 1279 -1102 C
ATOM 2996 C HIS B 116 0.530 -23.010 -24.529 1.00 78.61 C
ANISOU 2996 C HIS B 116 13236 7360 9272 -1424 1249 -933 C
ATOM 2997 O HIS B 116 0.923 -21.847 -24.664 1.00 83.22 O
ANISOU 2997 O HIS B 116 13697 8153 9768 -1423 1288 -953 O
ATOM 2998 CB HIS B 116 0.894 -24.461 -26.472 1.00 79.65 C
ANISOU 2998 CB HIS B 116 13610 7319 9335 -1504 1184 -1195 C
ATOM 2999 CG HIS B 116 1.785 -25.360 -27.270 1.00 89.40 C
ANISOU 2999 CG HIS B 116 14996 8441 10532 -1405 1242 -1403 C
ATOM 3000 ND1 HIS B 116 1.898 -26.715 -27.043 1.00 91.00 N
ANISOU 3000 ND1 HIS B 116 15355 8375 10847 -1310 1251 -1455 N
ATOM 3001 CD2 HIS B 116 2.580 -25.089 -28.332 1.00 93.14 C
ANISOU 3001 CD2 HIS B 116 15483 9029 10878 -1390 1303 -1570 C
ATOM 3002 CE1 HIS B 116 2.741 -27.235 -27.918 1.00 94.60 C
ANISOU 3002 CE1 HIS B 116 15915 8780 11249 -1226 1327 -1661 C
ATOM 3003 NE2 HIS B 116 3.169 -26.270 -28.710 1.00 94.55 N
ANISOU 3003 NE2 HIS B 116 15824 9009 11092 -1274 1366 -1733 N
ATOM 3004 N ALA B 117 -0.613 -23.306 -23.912 1.00 75.53 N
ANISOU 3004 N ALA B 117 12819 6873 9005 -1514 1186 -759 N
ATOM 3005 CA ALA B 117 -1.588 -22.254 -23.656 1.00 75.00 C
ANISOU 3005 CA ALA B 117 12559 6957 8982 -1635 1147 -603 C
ATOM 3006 C ALA B 117 -1.246 -21.460 -22.403 1.00 79.90 C
ANISOU 3006 C ALA B 117 13104 7666 9588 -1497 1279 -526 C
ATOM 3007 O ALA B 117 -1.268 -20.226 -22.419 1.00 87.54 O
ANISOU 3007 O ALA B 117 13934 8822 10507 -1526 1305 -514 O
ATOM 3008 CB ALA B 117 -2.989 -22.857 -23.550 1.00 72.90 C
ANISOU 3008 CB ALA B 117 12225 6572 8902 -1775 1023 -430 C
ATOM 3009 N LEU B 118 -0.919 -22.145 -21.307 1.00 77.61 N
ANISOU 3009 N LEU B 118 12917 7236 9334 -1348 1356 -471 N
ATOM 3010 CA LEU B 118 -0.416 -21.438 -20.138 1.00 64.42 C
ANISOU 3010 CA LEU B 118 11236 5638 7601 -1211 1480 -417 C
ATOM 3011 C LEU B 118 0.926 -20.789 -20.422 1.00 66.28 C
ANISOU 3011 C LEU B 118 11487 5992 7704 -1100 1527 -582 C
ATOM 3012 O LEU B 118 1.308 -19.843 -19.723 1.00 77.02 O
ANISOU 3012 O LEU B 118 12806 7466 8992 -1036 1598 -561 O
ATOM 3013 CB LEU B 118 -0.290 -22.383 -18.946 1.00 65.08 C
ANISOU 3013 CB LEU B 118 11456 5540 7733 -1076 1529 -305 C
ATOM 3014 CG LEU B 118 -1.568 -23.052 -18.436 1.00 63.78 C
ANISOU 3014 CG LEU B 118 11242 5272 7719 -1164 1495 -108 C
ATOM 3015 CD1 LEU B 118 -1.202 -24.150 -17.451 1.00 72.20 C
ANISOU 3015 CD1 LEU B 118 12474 6143 8816 -1025 1525 -15 C
ATOM 3016 CD2 LEU B 118 -2.482 -22.026 -17.798 1.00 59.71 C
ANISOU 3016 CD2 LEU B 118 10539 4916 7232 -1220 1556 35 C
ATOM 3017 N CYS B 119 1.637 -21.275 -21.444 1.00 65.69 N
ANISOU 3017 N CYS B 119 11451 5902 7605 -1072 1486 -743 N
ATOM 3018 CA CYS B 119 2.838 -20.599 -21.915 1.00 71.14 C
ANISOU 3018 CA CYS B 119 12062 6760 8207 -976 1511 -887 C
ATOM 3019 C CYS B 119 2.548 -19.171 -22.336 1.00 72.46 C
ANISOU 3019 C CYS B 119 12063 7159 8309 -1114 1499 -871 C
ATOM 3020 O CYS B 119 3.423 -18.302 -22.224 1.00 80.09 O
ANISOU 3020 O CYS B 119 12920 8291 9221 -1030 1520 -921 O
ATOM 3021 CB CYS B 119 3.456 -21.376 -23.076 1.00 66.80 C
ANISOU 3021 CB CYS B 119 11558 6166 7658 -944 1489 -1050 C
ATOM 3022 SG CYS B 119 4.861 -20.555 -23.866 1.00 77.29 S
ANISOU 3022 SG CYS B 119 12726 7731 8909 -842 1522 -1211 S
ATOM 3023 N LYS B 120 1.341 -18.917 -22.846 1.00 56.22 N
ANISOU 3023 N LYS B 120 9962 5118 6280 -1318 1440 -795 N
ATOM 3024 CA LYS B 120 0.921 -17.569 -23.202 1.00 51.00 C
ANISOU 3024 CA LYS B 120 9137 4651 5590 -1445 1419 -756 C
ATOM 3025 C LYS B 120 0.171 -16.875 -22.071 1.00 62.48 C
ANISOU 3025 C LYS B 120 10511 6122 7106 -1441 1475 -615 C
ATOM 3026 O LYS B 120 0.303 -15.658 -21.905 1.00 69.30 O
ANISOU 3026 O LYS B 120 11260 7135 7938 -1449 1510 -611 O
ATOM 3027 CB LYS B 120 0.059 -17.606 -24.473 1.00 55.02 C
ANISOU 3027 CB LYS B 120 9608 5188 6109 -1645 1289 -745 C
ATOM 3028 CG LYS B 120 0.836 -17.931 -25.748 1.00 59.27 C
ANISOU 3028 CG LYS B 120 10219 5762 6539 -1673 1261 -895 C
ATOM 3029 CD LYS B 120 -0.137 -18.191 -26.899 1.00 57.55 C
ANISOU 3029 CD LYS B 120 10032 5525 6309 -1886 1113 -868 C
ATOM 3030 CE LYS B 120 0.067 -17.269 -28.111 1.00 63.49 C
ANISOU 3030 CE LYS B 120 10721 6465 6937 -2014 1062 -905 C
ATOM 3031 NZ LYS B 120 0.929 -17.896 -29.144 1.00 75.35 N
ANISOU 3031 NZ LYS B 120 12365 7947 8319 -2009 1096 -1064 N
ATOM 3032 N VAL B 121 -0.622 -17.623 -21.300 1.00 64.31 N
ANISOU 3032 N VAL B 121 10784 6208 7442 -1421 1485 -494 N
ATOM 3033 CA VAL B 121 -1.431 -17.016 -20.241 1.00 58.82 C
ANISOU 3033 CA VAL B 121 9975 5544 6829 -1397 1550 -347 C
ATOM 3034 C VAL B 121 -0.557 -16.587 -19.063 1.00 66.60 C
ANISOU 3034 C VAL B 121 11074 6536 7693 -1253 1696 -369 C
ATOM 3035 O VAL B 121 -0.498 -15.396 -18.718 1.00 77.08 O
ANISOU 3035 O VAL B 121 12315 7989 8983 -1244 1754 -377 O
ATOM 3036 CB VAL B 121 -2.551 -17.973 -19.783 1.00 53.94 C
ANISOU 3036 CB VAL B 121 9331 4787 6376 -1420 1516 -184 C
ATOM 3037 CG1 VAL B 121 -3.247 -17.448 -18.528 1.00 59.17 C
ANISOU 3037 CG1 VAL B 121 9887 5482 7112 -1353 1627 -36 C
ATOM 3038 CG2 VAL B 121 -3.574 -18.205 -20.903 1.00 51.21 C
ANISOU 3038 CG2 VAL B 121 8840 4437 6180 -1586 1338 -124 C
ATOM 3039 N ILE B 122 0.126 -17.548 -18.420 1.00 55.80 N
ANISOU 3039 N ILE B 122 9908 5021 6274 -1133 1734 -373 N
ATOM 3040 CA ILE B 122 0.869 -17.230 -17.200 1.00 44.69 C
ANISOU 3040 CA ILE B 122 8637 3594 4749 -997 1832 -355 C
ATOM 3041 C ILE B 122 1.860 -16.097 -17.426 1.00 55.87 C
ANISOU 3041 C ILE B 122 9997 5174 6056 -967 1820 -491 C
ATOM 3042 O ILE B 122 1.882 -15.152 -16.619 1.00 63.69 O
ANISOU 3042 O ILE B 122 10999 6233 6966 -950 1894 -468 O
ATOM 3043 CB ILE B 122 1.540 -18.494 -16.643 1.00 50.92 C
ANISOU 3043 CB ILE B 122 9633 4193 5522 -851 1814 -336 C
ATOM 3044 CG1 ILE B 122 0.491 -19.516 -16.219 1.00 53.27 C
ANISOU 3044 CG1 ILE B 122 9950 4360 5931 -885 1819 -169 C
ATOM 3045 CG2 ILE B 122 2.423 -18.155 -15.448 1.00 54.00 C
ANISOU 3045 CG2 ILE B 122 10142 4612 5763 -691 1842 -313 C
ATOM 3046 CD1 ILE B 122 1.061 -20.801 -15.667 1.00 44.28 C
ANISOU 3046 CD1 ILE B 122 9006 3016 4803 -747 1791 -117 C
ATOM 3047 N PRO B 123 2.719 -16.130 -18.444 1.00 58.02 N
ANISOU 3047 N PRO B 123 10166 5556 6324 -939 1716 -621 N
ATOM 3048 CA PRO B 123 3.621 -14.982 -18.674 1.00 59.15 C
ANISOU 3048 CA PRO B 123 10122 5936 6416 -901 1649 -692 C
ATOM 3049 C PRO B 123 2.847 -13.685 -18.879 1.00 64.28 C
ANISOU 3049 C PRO B 123 10640 6687 7097 -1060 1680 -645 C
ATOM 3050 O PRO B 123 3.297 -12.609 -18.463 1.00 69.71 O
ANISOU 3050 O PRO B 123 11210 7513 7764 -1023 1644 -645 O
ATOM 3051 CB PRO B 123 4.400 -15.404 -19.931 1.00 46.17 C
ANISOU 3051 CB PRO B 123 8383 4355 4805 -876 1565 -813 C
ATOM 3052 CG PRO B 123 4.343 -16.920 -19.914 1.00 47.73 C
ANISOU 3052 CG PRO B 123 8766 4333 5038 -806 1587 -828 C
ATOM 3053 CD PRO B 123 2.975 -17.238 -19.382 1.00 57.66 C
ANISOU 3053 CD PRO B 123 10146 5426 6334 -925 1649 -695 C
ATOM 3054 N TYR B 124 1.675 -13.776 -19.518 1.00 52.78 N
ANISOU 3054 N TYR B 124 9178 5171 5707 -1223 1720 -603 N
ATOM 3055 CA TYR B 124 0.862 -12.601 -19.780 1.00 53.65 C
ANISOU 3055 CA TYR B 124 9131 5390 5862 -1331 1736 -576 C
ATOM 3056 C TYR B 124 0.314 -12.013 -18.486 1.00 69.33 C
ANISOU 3056 C TYR B 124 11126 7341 7875 -1255 1838 -521 C
ATOM 3057 O TYR B 124 0.372 -10.796 -18.270 1.00 78.99 O
ANISOU 3057 O TYR B 124 12259 8641 9112 -1251 1846 -564 O
ATOM 3058 CB TYR B 124 -0.275 -12.980 -20.727 1.00 50.67 C
ANISOU 3058 CB TYR B 124 8627 5006 5621 -1430 1615 -520 C
ATOM 3059 CG TYR B 124 -1.360 -11.943 -20.826 1.00 63.00 C
ANISOU 3059 CG TYR B 124 9945 6652 7342 -1463 1553 -424 C
ATOM 3060 CD1 TYR B 124 -1.183 -10.814 -21.622 1.00 67.52 C
ANISOU 3060 CD1 TYR B 124 10375 7370 7912 -1521 1474 -463 C
ATOM 3061 CD2 TYR B 124 -2.576 -12.100 -20.154 1.00 55.11 C
ANISOU 3061 CD2 TYR B 124 8834 5582 6525 -1429 1567 -265 C
ATOM 3062 CE1 TYR B 124 -2.164 -9.865 -21.735 1.00 54.22 C
ANISOU 3062 CE1 TYR B 124 8454 5735 6412 -1526 1399 -341 C
ATOM 3063 CE2 TYR B 124 -3.572 -11.149 -20.266 1.00 51.42 C
ANISOU 3063 CE2 TYR B 124 8116 5174 6248 -1442 1511 -142 C
ATOM 3064 CZ TYR B 124 -3.356 -10.037 -21.057 1.00 46.03 C
ANISOU 3064 CZ TYR B 124 7304 4613 5571 -1484 1422 -177 C
ATOM 3065 OH TYR B 124 -4.334 -9.086 -21.179 1.00 45.05 O
ANISOU 3065 OH TYR B 124 6931 4522 5662 -1486 1357 -26 O
ATOM 3066 N LEU B 125 -0.247 -12.868 -17.621 1.00 62.39 N
ANISOU 3066 N LEU B 125 10334 6335 7038 -1186 1894 -420 N
ATOM 3067 CA LEU B 125 -0.741 -12.411 -16.321 1.00 56.33 C
ANISOU 3067 CA LEU B 125 9575 5541 6289 -1098 1997 -350 C
ATOM 3068 C LEU B 125 0.357 -11.735 -15.510 1.00 55.49 C
ANISOU 3068 C LEU B 125 9606 5437 6040 -1034 2015 -417 C
ATOM 3069 O LEU B 125 0.128 -10.685 -14.903 1.00 59.63 O
ANISOU 3069 O LEU B 125 10054 6005 6598 -1009 2038 -413 O
ATOM 3070 CB LEU B 125 -1.360 -13.581 -15.560 1.00 69.62 C
ANISOU 3070 CB LEU B 125 11344 7101 8008 -1046 2052 -217 C
ATOM 3071 CG LEU B 125 -2.544 -14.159 -16.333 1.00 69.65 C
ANISOU 3071 CG LEU B 125 11153 7087 8225 -1133 1964 -111 C
ATOM 3072 CD1 LEU B 125 -3.308 -15.190 -15.513 1.00 65.99 C
ANISOU 3072 CD1 LEU B 125 10730 6507 7838 -1100 2018 43 C
ATOM 3073 CD2 LEU B 125 -3.444 -13.028 -16.787 1.00 65.50 C
ANISOU 3073 CD2 LEU B 125 10350 6668 7868 -1183 1926 -69 C
ATOM 3074 N GLN B 126 1.558 -12.312 -15.492 1.00 61.06 N
ANISOU 3074 N GLN B 126 10421 6162 6618 -979 1939 -429 N
ATOM 3075 CA GLN B 126 2.666 -11.672 -14.781 1.00 63.22 C
ANISOU 3075 CA GLN B 126 10643 6595 6782 -862 1814 -453 C
ATOM 3076 C GLN B 126 2.948 -10.277 -15.339 1.00 64.54 C
ANISOU 3076 C GLN B 126 10580 6922 7020 -918 1722 -513 C
ATOM 3077 O GLN B 126 3.152 -9.319 -14.579 1.00 62.49 O
ANISOU 3077 O GLN B 126 10291 6732 6721 -887 1696 -514 O
ATOM 3078 CB GLN B 126 3.908 -12.561 -14.849 1.00 54.95 C
ANISOU 3078 CB GLN B 126 9663 5591 5624 -735 1704 -506 C
ATOM 3079 CG GLN B 126 5.239 -11.825 -14.997 1.00 56.35 C
ANISOU 3079 CG GLN B 126 9682 5973 5755 -665 1538 -596 C
ATOM 3080 CD GLN B 126 5.511 -10.762 -13.945 1.00 85.02 C
ANISOU 3080 CD GLN B 126 13310 9701 9293 -648 1490 -578 C
ATOM 3081 OE1 GLN B 126 4.750 -10.599 -12.996 1.00100.86 O
ANISOU 3081 OE1 GLN B 126 15437 11623 11261 -666 1582 -501 O
ATOM 3082 NE2 GLN B 126 6.605 -10.026 -14.121 1.00 91.85 N
ANISOU 3082 NE2 GLN B 126 14045 10734 10120 -619 1355 -657 N
ATOM 3083 N ALA B 127 2.944 -10.139 -16.669 1.00 59.38 N
ANISOU 3083 N ALA B 127 9787 6318 6455 -1014 1679 -562 N
ATOM 3084 CA ALA B 127 3.144 -8.831 -17.280 1.00 51.88 C
ANISOU 3084 CA ALA B 127 8643 5501 5570 -1084 1608 -603 C
ATOM 3085 C ALA B 127 2.013 -7.876 -16.930 1.00 61.07 C
ANISOU 3085 C ALA B 127 9800 6569 6836 -1167 1722 -573 C
ATOM 3086 O ALA B 127 2.250 -6.683 -16.688 1.00 66.43 O
ANISOU 3086 O ALA B 127 10391 7323 7527 -1166 1689 -592 O
ATOM 3087 CB ALA B 127 3.268 -8.990 -18.792 1.00 45.19 C
ANISOU 3087 CB ALA B 127 7688 4713 4770 -1186 1554 -649 C
ATOM 3088 N VAL B 128 0.775 -8.381 -16.913 1.00 64.94 N
ANISOU 3088 N VAL B 128 10367 6905 7403 -1194 1846 -569 N
ATOM 3089 CA VAL B 128 -0.363 -7.534 -16.579 1.00 59.63 C
ANISOU 3089 CA VAL B 128 9586 6236 6836 -1156 1938 -549 C
ATOM 3090 C VAL B 128 -0.291 -7.091 -15.121 1.00 57.94 C
ANISOU 3090 C VAL B 128 9491 5943 6581 -1078 2028 -516 C
ATOM 3091 O VAL B 128 -0.597 -5.939 -14.796 1.00 55.69 O
ANISOU 3091 O VAL B 128 9149 5653 6358 -1071 2084 -532 O
ATOM 3092 CB VAL B 128 -1.685 -8.264 -16.880 1.00 56.42 C
ANISOU 3092 CB VAL B 128 9051 5821 6566 -1148 1965 -418 C
ATOM 3093 CG1 VAL B 128 -2.747 -7.808 -15.905 1.00 55.62 C
ANISOU 3093 CG1 VAL B 128 8889 5652 6590 -1071 2107 -323 C
ATOM 3094 CG2 VAL B 128 -2.127 -8.005 -18.312 1.00 57.57 C
ANISOU 3094 CG2 VAL B 128 8964 6072 6839 -1241 1807 -370 C
ATOM 3095 N SER B 129 0.114 -7.992 -14.215 1.00 64.29 N
ANISOU 3095 N SER B 129 10468 6703 7258 -1010 2041 -462 N
ATOM 3096 CA SER B 129 0.213 -7.614 -12.806 1.00 55.83 C
ANISOU 3096 CA SER B 129 9518 5613 6081 -932 2100 -428 C
ATOM 3097 C SER B 129 1.320 -6.591 -12.573 1.00 54.52 C
ANISOU 3097 C SER B 129 9316 5591 5809 -928 1963 -479 C
ATOM 3098 O SER B 129 1.191 -5.739 -11.687 1.00 57.19 O
ANISOU 3098 O SER B 129 9715 5913 6102 -909 2023 -489 O
ATOM 3099 CB SER B 129 0.442 -8.855 -11.943 1.00 58.63 C
ANISOU 3099 CB SER B 129 10069 5923 6286 -854 2116 -364 C
ATOM 3100 OG SER B 129 1.824 -9.131 -11.834 1.00 63.07 O
ANISOU 3100 OG SER B 129 10680 6606 6676 -807 1943 -388 O
ATOM 3101 N VAL B 130 2.410 -6.662 -13.345 1.00 52.96 N
ANISOU 3101 N VAL B 130 9017 5539 5567 -935 1787 -523 N
ATOM 3102 CA VAL B 130 3.428 -5.614 -13.294 1.00 45.54 C
ANISOU 3102 CA VAL B 130 7993 4752 4558 -927 1649 -588 C
ATOM 3103 C VAL B 130 2.845 -4.289 -13.777 1.00 50.15 C
ANISOU 3103 C VAL B 130 8461 5311 5283 -1021 1714 -612 C
ATOM 3104 O VAL B 130 3.004 -3.239 -13.137 1.00 39.02 O
ANISOU 3104 O VAL B 130 7083 3914 3830 -1021 1723 -643 O
ATOM 3105 CB VAL B 130 4.668 -6.023 -14.111 1.00 37.38 C
ANISOU 3105 CB VAL B 130 6850 3872 3480 -897 1474 -640 C
ATOM 3106 CG1 VAL B 130 5.626 -4.840 -14.222 1.00 32.75 C
ANISOU 3106 CG1 VAL B 130 6153 3430 2859 -909 1348 -711 C
ATOM 3107 CG2 VAL B 130 5.332 -7.214 -13.475 1.00 36.15 C
ANISOU 3107 CG2 VAL B 130 6842 3717 3175 -790 1425 -629 C
ATOM 3108 N SER B 131 2.164 -4.319 -14.924 1.00 67.58 N
ANISOU 3108 N SER B 131 10558 7469 7651 -1114 1762 -608 N
ATOM 3109 CA SER B 131 1.540 -3.111 -15.454 1.00 54.63 C
ANISOU 3109 CA SER B 131 8822 5777 6157 -1208 1833 -642 C
ATOM 3110 C SER B 131 0.517 -2.548 -14.472 1.00 59.42 C
ANISOU 3110 C SER B 131 9524 6222 6832 -1162 2029 -632 C
ATOM 3111 O SER B 131 0.519 -1.347 -14.173 1.00 60.33 O
ANISOU 3111 O SER B 131 9637 6314 6973 -1184 2082 -663 O
ATOM 3112 CB SER B 131 0.896 -3.403 -16.807 1.00 48.35 C
ANISOU 3112 CB SER B 131 7911 4980 5481 -1272 1819 -681 C
ATOM 3113 OG SER B 131 0.097 -2.312 -17.222 1.00 45.35 O
ANISOU 3113 OG SER B 131 7406 4617 5207 -1262 1883 -719 O
ATOM 3114 N VAL B 132 -0.380 -3.402 -13.972 1.00 66.19 N
ANISOU 3114 N VAL B 132 10460 6968 7722 -1090 2155 -589 N
ATOM 3115 CA VAL B 132 -1.380 -2.931 -13.022 1.00 60.68 C
ANISOU 3115 CA VAL B 132 9828 6131 7098 -1021 2370 -568 C
ATOM 3116 C VAL B 132 -0.698 -2.336 -11.794 1.00 64.93 C
ANISOU 3116 C VAL B 132 10536 6678 7457 -1008 2375 -572 C
ATOM 3117 O VAL B 132 -1.175 -1.347 -11.212 1.00 70.28 O
ANISOU 3117 O VAL B 132 11264 7256 8183 -1000 2531 -591 O
ATOM 3118 CB VAL B 132 -2.343 -4.079 -12.656 1.00 62.25 C
ANISOU 3118 CB VAL B 132 10049 6264 7338 -940 2489 -489 C
ATOM 3119 CG1 VAL B 132 -3.187 -3.708 -11.436 1.00 58.96 C
ANISOU 3119 CG1 VAL B 132 9735 5710 6957 -865 2725 -450 C
ATOM 3120 CG2 VAL B 132 -3.207 -4.414 -13.837 1.00 71.53 C
ANISOU 3120 CG2 VAL B 132 10964 7516 8697 -945 2456 -427 C
ATOM 3121 N ALA B 133 0.437 -2.913 -11.392 1.00 64.37 N
ANISOU 3121 N ALA B 133 10547 6744 7168 -984 2199 -569 N
ATOM 3122 CA ALA B 133 1.189 -2.385 -10.261 1.00 58.05 C
ANISOU 3122 CA ALA B 133 9894 6004 6157 -950 2145 -607 C
ATOM 3123 C ALA B 133 1.732 -0.976 -10.517 1.00 59.24 C
ANISOU 3123 C ALA B 133 9975 6219 6315 -1006 2080 -683 C
ATOM 3124 O ALA B 133 1.330 -0.023 -9.835 1.00 56.69 O
ANISOU 3124 O ALA B 133 9750 5803 5985 -1014 2217 -716 O
ATOM 3125 CB ALA B 133 2.320 -3.349 -9.910 1.00 58.45 C
ANISOU 3125 CB ALA B 133 10020 6187 6002 -895 1950 -604 C
ATOM 3126 N VAL B 134 2.633 -0.829 -11.496 1.00 65.53 N
ANISOU 3126 N VAL B 134 10610 7164 7125 -1044 1888 -716 N
ATOM 3127 CA VAL B 134 3.325 0.446 -11.710 1.00 66.81 C
ANISOU 3127 CA VAL B 134 10714 7402 7270 -1097 1800 -790 C
ATOM 3128 C VAL B 134 2.362 1.555 -12.099 1.00 70.10 C
ANISOU 3128 C VAL B 134 11080 7682 7873 -1173 1993 -798 C
ATOM 3129 O VAL B 134 2.607 2.728 -11.791 1.00 78.70 O
ANISOU 3129 O VAL B 134 12211 8758 8933 -1204 2009 -861 O
ATOM 3130 CB VAL B 134 4.442 0.267 -12.764 1.00 53.95 C
ANISOU 3130 CB VAL B 134 8908 5954 5635 -1120 1580 -815 C
ATOM 3131 CG1 VAL B 134 3.866 0.181 -14.170 1.00 54.70 C
ANISOU 3131 CG1 VAL B 134 8825 6035 5922 -1203 1628 -783 C
ATOM 3132 CG2 VAL B 134 5.468 1.390 -12.659 1.00 50.38 C
ANISOU 3132 CG2 VAL B 134 8442 5597 5102 -1156 1445 -897 C
ATOM 3133 N LEU B 135 1.251 1.219 -12.760 1.00 62.69 N
ANISOU 3133 N LEU B 135 10062 6618 7139 -1201 2147 -746 N
ATOM 3134 CA LEU B 135 0.256 2.242 -13.056 1.00 53.66 C
ANISOU 3134 CA LEU B 135 8874 5299 6216 -1252 2363 -760 C
ATOM 3135 C LEU B 135 -0.459 2.675 -11.784 1.00 51.00 C
ANISOU 3135 C LEU B 135 8709 4796 5871 -1182 2591 -756 C
ATOM 3136 O LEU B 135 -0.647 3.873 -11.539 1.00 55.90 O
ANISOU 3136 O LEU B 135 9360 5331 6550 -1207 2726 -795 O
ATOM 3137 CB LEU B 135 -0.753 1.712 -14.070 1.00 47.06 C
ANISOU 3137 CB LEU B 135 7856 4437 5588 -1196 2389 -757 C
ATOM 3138 CG LEU B 135 -0.502 2.115 -15.521 1.00 47.28 C
ANISOU 3138 CG LEU B 135 7664 4635 5666 -1229 2244 -808 C
ATOM 3139 CD1 LEU B 135 -1.538 1.476 -16.441 1.00 51.93 C
ANISOU 3139 CD1 LEU B 135 8028 5286 6416 -1170 2218 -696 C
ATOM 3140 CD2 LEU B 135 -0.503 3.626 -15.644 1.00 41.35 C
ANISOU 3140 CD2 LEU B 135 6850 3873 4990 -1247 2320 -858 C
ATOM 3141 N THR B 136 -0.850 1.710 -10.944 1.00 53.86 N
ANISOU 3141 N THR B 136 9197 5113 6153 -1097 2653 -710 N
ATOM 3142 CA THR B 136 -1.531 2.075 -9.706 1.00 56.41 C
ANISOU 3142 CA THR B 136 9702 5284 6446 -1036 2889 -709 C
ATOM 3143 C THR B 136 -0.652 2.943 -8.811 1.00 64.65 C
ANISOU 3143 C THR B 136 10917 6400 7247 -1050 2818 -794 C
ATOM 3144 O THR B 136 -1.134 3.917 -8.223 1.00 77.56 O
ANISOU 3144 O THR B 136 12656 7899 8915 -1046 3023 -834 O
ATOM 3145 CB THR B 136 -2.003 0.833 -8.954 1.00 59.11 C
ANISOU 3145 CB THR B 136 10160 5589 6712 -954 2956 -646 C
ATOM 3146 OG1 THR B 136 -2.920 0.096 -9.770 1.00 54.17 O
ANISOU 3146 OG1 THR B 136 9367 4892 6323 -920 3023 -589 O
ATOM 3147 CG2 THR B 136 -2.702 1.262 -7.673 1.00 62.48 C
ANISOU 3147 CG2 THR B 136 10787 5861 7091 -900 3222 -650 C
ATOM 3148 N LEU B 137 0.639 2.611 -8.691 1.00 61.06 N
ANISOU 3148 N LEU B 137 10496 6141 6561 -1058 2533 -834 N
ATOM 3149 CA LEU B 137 1.542 3.446 -7.898 1.00 52.33 C
ANISOU 3149 CA LEU B 137 9550 5097 5238 -1075 2424 -935 C
ATOM 3150 C LEU B 137 1.653 4.851 -8.472 1.00 65.53 C
ANISOU 3150 C LEU B 137 11135 6741 7024 -1142 2445 -1005 C
ATOM 3151 O LEU B 137 1.817 5.824 -7.725 1.00 75.83 O
ANISOU 3151 O LEU B 137 12604 7984 8223 -1156 2495 -1095 O
ATOM 3152 CB LEU B 137 2.924 2.813 -7.814 1.00 38.82 C
ANISOU 3152 CB LEU B 137 7846 3587 3318 -1068 2107 -956 C
ATOM 3153 CG LEU B 137 3.052 1.572 -6.936 1.00 39.90 C
ANISOU 3153 CG LEU B 137 8139 3749 3272 -1006 2072 -909 C
ATOM 3154 CD1 LEU B 137 4.292 0.820 -7.331 1.00 38.82 C
ANISOU 3154 CD1 LEU B 137 7914 3797 3038 -993 1785 -903 C
ATOM 3155 CD2 LEU B 137 3.114 1.979 -5.470 1.00 46.01 C
ANISOU 3155 CD2 LEU B 137 9217 4459 3807 -1008 2138 -969 C
ATOM 3156 N SER B 138 1.604 4.974 -9.800 1.00 65.18 N
ANISOU 3156 N SER B 138 10849 6738 7178 -1194 2403 -973 N
ATOM 3157 CA SER B 138 1.633 6.299 -10.406 1.00 59.59 C
ANISOU 3157 CA SER B 138 10052 5993 6597 -1265 2445 -1031 C
ATOM 3158 C SER B 138 0.378 7.093 -10.066 1.00 65.44 C
ANISOU 3158 C SER B 138 10845 6495 7523 -1247 2797 -1027 C
ATOM 3159 O SER B 138 0.451 8.301 -9.808 1.00 73.60 O
ANISOU 3159 O SER B 138 11943 7456 8566 -1265 2868 -1112 O
ATOM 3160 CB SER B 138 1.784 6.176 -11.920 1.00 48.03 C
ANISOU 3160 CB SER B 138 8328 4625 5295 -1339 2349 -991 C
ATOM 3161 OG SER B 138 2.814 5.265 -12.260 1.00 49.97 O
ANISOU 3161 OG SER B 138 8512 5071 5404 -1333 2072 -978 O
ATOM 3162 N PHE B 139 -0.785 6.435 -10.064 1.00 60.82 N
ANISOU 3162 N PHE B 139 10226 5768 7115 -1202 3023 -930 N
ATOM 3163 CA PHE B 139 -2.025 7.132 -9.731 1.00 56.88 C
ANISOU 3163 CA PHE B 139 9745 5017 6850 -1163 3388 -905 C
ATOM 3164 C PHE B 139 -2.037 7.596 -8.277 1.00 62.61 C
ANISOU 3164 C PHE B 139 10755 5664 7371 -1109 3511 -983 C
ATOM 3165 O PHE B 139 -2.558 8.676 -7.971 1.00 71.77 O
ANISOU 3165 O PHE B 139 11961 6660 8648 -1094 3751 -1026 O
ATOM 3166 CB PHE B 139 -3.230 6.245 -10.033 1.00 67.80 C
ANISOU 3166 CB PHE B 139 11021 6237 8503 -1106 3566 -791 C
ATOM 3167 CG PHE B 139 -3.880 6.544 -11.344 1.00 84.51 C
ANISOU 3167 CG PHE B 139 12765 8400 10943 -1023 3515 -774 C
ATOM 3168 CD1 PHE B 139 -5.105 7.206 -11.392 1.00104.13 C
ANISOU 3168 CD1 PHE B 139 15096 10703 13765 -892 3766 -745 C
ATOM 3169 CD2 PHE B 139 -3.260 6.181 -12.526 1.00 81.14 C
ANISOU 3169 CD2 PHE B 139 12159 8184 10484 -1044 3224 -813 C
ATOM 3170 CE1 PHE B 139 -5.720 7.493 -12.609 1.00109.44 C
ANISOU 3170 CE1 PHE B 139 15416 11430 14735 -773 3766 -738 C
ATOM 3171 CE2 PHE B 139 -3.852 6.460 -13.755 1.00 87.95 C
ANISOU 3171 CE2 PHE B 139 12720 9104 11592 -958 3243 -819 C
ATOM 3172 CZ PHE B 139 -5.095 7.121 -13.801 1.00103.34 C
ANISOU 3172 CZ PHE B 139 14487 10872 13905 -835 3492 -748 C
ATOM 3173 N ILE B 140 -1.468 6.804 -7.369 1.00 60.41 N
ANISOU 3173 N ILE B 140 10674 5490 6790 -1081 3364 -1005 N
ATOM 3174 CA ILE B 140 -1.377 7.247 -5.983 1.00 64.25 C
ANISOU 3174 CA ILE B 140 11464 5908 7040 -1054 3463 -1097 C
ATOM 3175 C ILE B 140 -0.481 8.470 -5.869 1.00 75.84 C
ANISOU 3175 C ILE B 140 13018 7418 8380 -1112 3326 -1239 C
ATOM 3176 O ILE B 140 -0.735 9.368 -5.058 1.00 90.94 O
ANISOU 3176 O ILE B 140 15133 9190 10230 -1104 3508 -1333 O
ATOM 3177 CB ILE B 140 -0.877 6.100 -5.087 1.00 58.30 C
ANISOU 3177 CB ILE B 140 10895 5266 5990 -1027 3314 -1085 C
ATOM 3178 CG1 ILE B 140 -1.807 4.916 -5.195 1.00 62.35 C
ANISOU 3178 CG1 ILE B 140 11330 5719 6643 -966 3455 -954 C
ATOM 3179 CG2 ILE B 140 -0.790 6.516 -3.634 1.00 64.40 C
ANISOU 3179 CG2 ILE B 140 12012 5965 6491 -1020 3421 -1183 C
ATOM 3180 CD1 ILE B 140 -1.173 3.692 -4.663 1.00 48.46 C
ANISOU 3180 CD1 ILE B 140 9679 4101 4633 -947 3255 -927 C
ATOM 3181 N ALA B 141 0.583 8.523 -6.669 1.00 78.12 N
ANISOU 3181 N ALA B 141 13164 7889 8631 -1172 3007 -1262 N
ATOM 3182 CA ALA B 141 1.438 9.705 -6.674 1.00 76.95 C
ANISOU 3182 CA ALA B 141 13071 7765 8400 -1233 2856 -1393 C
ATOM 3183 C ALA B 141 0.700 10.932 -7.204 1.00 79.71 C
ANISOU 3183 C ALA B 141 13321 7940 9024 -1241 3093 -1425 C
ATOM 3184 O ALA B 141 0.871 12.037 -6.678 1.00 88.23 O
ANISOU 3184 O ALA B 141 14562 8915 10046 -1257 3139 -1551 O
ATOM 3185 CB ALA B 141 2.709 9.437 -7.483 1.00 71.10 C
ANISOU 3185 CB ALA B 141 12169 7249 7598 -1291 2478 -1393 C
ATOM 3186 N LEU B 142 -0.125 10.761 -8.242 1.00 84.09 N
ANISOU 3186 N LEU B 142 13613 8448 9892 -1231 3246 -1314 N
ATOM 3187 CA LEU B 142 -0.791 11.901 -8.871 1.00 84.20 C
ANISOU 3187 CA LEU B 142 13474 8302 10216 -1230 3458 -1326 C
ATOM 3188 C LEU B 142 -1.865 12.478 -7.960 1.00 90.38 C
ANISOU 3188 C LEU B 142 14404 8830 11105 -1152 3847 -1344 C
ATOM 3189 O LEU B 142 -1.963 13.700 -7.798 1.00 94.48 O
ANISOU 3189 O LEU B 142 14974 9209 11716 -1142 3961 -1442 O
ATOM 3190 CB LEU B 142 -1.378 11.478 -10.216 1.00 74.52 C
ANISOU 3190 CB LEU B 142 11911 7102 9300 -1243 3514 -1192 C
ATOM 3191 CG LEU B 142 -1.921 12.536 -11.172 1.00 69.86 C
ANISOU 3191 CG LEU B 142 11060 6408 9076 -1231 3648 -1183 C
ATOM 3192 CD1 LEU B 142 -0.786 13.405 -11.668 1.00 75.36 C
ANISOU 3192 CD1 LEU B 142 11738 7201 9694 -1305 3328 -1296 C
ATOM 3193 CD2 LEU B 142 -2.616 11.858 -12.341 1.00 57.08 C
ANISOU 3193 CD2 LEU B 142 9108 4855 7723 -1198 3705 -1052 C
ATOM 3194 N ASP B 143 -2.691 11.611 -7.365 1.00 92.39 N
ANISOU 3194 N ASP B 143 14729 9008 11369 -1091 4057 -1249 N
ATOM 3195 CA ASP B 143 -3.685 12.078 -6.401 1.00 89.02 C
ANISOU 3195 CA ASP B 143 14463 8339 11021 -1013 4442 -1263 C
ATOM 3196 C ASP B 143 -3.009 12.837 -5.268 1.00 88.28 C
ANISOU 3196 C ASP B 143 14720 8225 10599 -1027 4394 -1453 C
ATOM 3197 O ASP B 143 -3.525 13.855 -4.796 1.00 95.11 O
ANISOU 3197 O ASP B 143 15692 8886 11559 -988 4664 -1533 O
ATOM 3198 CB ASP B 143 -4.487 10.902 -5.851 1.00 84.48 C
ANISOU 3198 CB ASP B 143 13943 7708 10447 -951 4611 -1143 C
ATOM 3199 CG ASP B 143 -5.338 11.278 -4.658 1.00 94.91 C
ANISOU 3199 CG ASP B 143 15495 8806 11759 -873 4988 -1177 C
ATOM 3200 OD1 ASP B 143 -6.270 12.100 -4.824 1.00104.97 O
ANISOU 3200 OD1 ASP B 143 16650 9860 13374 -819 5320 -1142 O
ATOM 3201 OD2 ASP B 143 -5.066 10.756 -3.555 1.00 97.55 O
ANISOU 3201 OD2 ASP B 143 16124 9184 11756 -865 4961 -1236 O
ATOM 3202 N ARG B 144 -1.844 12.353 -4.819 1.00 81.79 N
ANISOU 3202 N ARG B 144 14074 7599 9403 -1084 4052 -1525 N
ATOM 3203 CA ARG B 144 -1.097 13.061 -3.788 1.00 81.04 C
ANISOU 3203 CA ARG B 144 14312 7488 8993 -1122 3960 -1704 C
ATOM 3204 C ARG B 144 -0.459 14.326 -4.340 1.00 87.98 C
ANISOU 3204 C ARG B 144 15134 8347 9948 -1179 3810 -1824 C
ATOM 3205 O ARG B 144 -0.409 15.351 -3.651 1.00106.04 O
ANISOU 3205 O ARG B 144 17653 10485 12152 -1187 3910 -1975 O
ATOM 3206 CB ARG B 144 -0.037 12.153 -3.185 1.00 68.32 C
ANISOU 3206 CB ARG B 144 12866 6082 7008 -1169 3630 -1721 C
ATOM 3207 CG ARG B 144 -0.613 10.877 -2.633 1.00 61.14 C
ANISOU 3207 CG ARG B 144 12019 5187 6023 -1113 3752 -1607 C
ATOM 3208 CD ARG B 144 -1.403 11.164 -1.374 1.00 72.57 C
ANISOU 3208 CD ARG B 144 13779 6436 7358 -1070 4104 -1670 C
ATOM 3209 NE ARG B 144 -2.704 11.761 -1.656 1.00 77.86 N
ANISOU 3209 NE ARG B 144 14330 6876 8377 -997 4519 -1628 N
ATOM 3210 CZ ARG B 144 -3.359 12.544 -0.808 1.00 80.62 C
ANISOU 3210 CZ ARG B 144 14908 7008 8715 -959 4864 -1720 C
ATOM 3211 NH1 ARG B 144 -2.842 12.827 0.384 1.00 80.38 N
ANISOU 3211 NH1 ARG B 144 15268 6963 8310 -1001 4838 -1874 N
ATOM 3212 NH2 ARG B 144 -4.537 13.040 -1.153 1.00 85.27 N
ANISOU 3212 NH2 ARG B 144 15334 7385 9679 -881 5242 -1656 N
ATOM 3213 N TRP B 145 0.045 14.272 -5.577 1.00 75.12 N
ANISOU 3213 N TRP B 145 13213 6857 8472 -1223 3568 -1765 N
ATOM 3214 CA TRP B 145 0.681 15.444 -6.175 1.00 70.52 C
ANISOU 3214 CA TRP B 145 12560 6253 7984 -1284 3399 -1868 C
ATOM 3215 C TRP B 145 -0.304 16.589 -6.383 1.00 75.13 C
ANISOU 3215 C TRP B 145 13074 6574 8897 -1226 3731 -1899 C
ATOM 3216 O TRP B 145 0.031 17.755 -6.148 1.00 90.71 O
ANISOU 3216 O TRP B 145 15177 8422 10868 -1253 3698 -2045 O
ATOM 3217 CB TRP B 145 1.334 15.070 -7.502 1.00 56.55 C
ANISOU 3217 CB TRP B 145 10480 4680 6325 -1344 3104 -1782 C
ATOM 3218 CG TRP B 145 2.043 16.230 -8.160 1.00 53.18 C
ANISOU 3218 CG TRP B 145 9969 4232 6006 -1419 2896 -1871 C
ATOM 3219 CD1 TRP B 145 3.254 16.757 -7.815 1.00 55.42 C
ANISOU 3219 CD1 TRP B 145 10403 4575 6077 -1507 2589 -1992 C
ATOM 3220 CD2 TRP B 145 1.568 17.009 -9.261 1.00 52.32 C
ANISOU 3220 CD2 TRP B 145 9594 4016 6269 -1417 2969 -1832 C
ATOM 3221 NE1 TRP B 145 3.570 17.807 -8.645 1.00 56.36 N
ANISOU 3221 NE1 TRP B 145 10373 4628 6412 -1567 2462 -2028 N
ATOM 3222 CE2 TRP B 145 2.548 17.982 -9.541 1.00 52.71 C
ANISOU 3222 CE2 TRP B 145 9657 4063 6309 -1510 2686 -1929 C
ATOM 3223 CE3 TRP B 145 0.411 16.974 -10.042 1.00 53.40 C
ANISOU 3223 CE3 TRP B 145 9465 4052 6774 -1348 3229 -1707 C
ATOM 3224 CZ2 TRP B 145 2.404 18.911 -10.568 1.00 58.79 C
ANISOU 3224 CZ2 TRP B 145 10193 4728 7416 -1537 2642 -1897 C
ATOM 3225 CZ3 TRP B 145 0.270 17.897 -11.061 1.00 58.44 C
ANISOU 3225 CZ3 TRP B 145 9856 4596 7752 -1363 3177 -1676 C
ATOM 3226 CH2 TRP B 145 1.259 18.854 -11.316 1.00 67.92 C
ANISOU 3226 CH2 TRP B 145 11088 5792 8929 -1458 2880 -1766 C
ATOM 3227 N TYR B 146 -1.516 16.284 -6.848 1.00 71.85 N
ANISOU 3227 N TYR B 146 12439 6060 8801 -1147 4044 -1756 N
ATOM 3228 CA TYR B 146 -2.527 17.327 -6.992 1.00 77.19 C
ANISOU 3228 CA TYR B 146 13013 6471 9844 -1069 4389 -1758 C
ATOM 3229 C TYR B 146 -3.126 17.712 -5.647 1.00 85.47 C
ANISOU 3229 C TYR B 146 14383 7312 10781 -1003 4724 -1853 C
ATOM 3230 O TYR B 146 -3.402 18.890 -5.396 1.00 88.38 O
ANISOU 3230 O TYR B 146 14830 7464 11288 -965 4901 -1962 O
ATOM 3231 CB TYR B 146 -3.622 16.874 -7.952 1.00 67.98 C
ANISOU 3231 CB TYR B 146 11463 5263 9103 -1008 4607 -1550 C
ATOM 3232 CG TYR B 146 -3.312 17.096 -9.417 1.00 67.18 C
ANISOU 3232 CG TYR B 146 11006 5261 9258 -1048 4371 -1483 C
ATOM 3233 CD1 TYR B 146 -3.347 18.368 -9.958 1.00 71.76 C
ANISOU 3233 CD1 TYR B 146 11446 5694 10127 -1033 4352 -1524 C
ATOM 3234 CD2 TYR B 146 -3.007 16.035 -10.259 1.00 71.81 C
ANISOU 3234 CD2 TYR B 146 11404 6073 9808 -1099 4156 -1376 C
ATOM 3235 CE1 TYR B 146 -3.075 18.589 -11.299 1.00 57.39 C
ANISOU 3235 CE1 TYR B 146 9300 3955 8550 -1070 4088 -1440 C
ATOM 3236 CE2 TYR B 146 -2.737 16.244 -11.594 1.00 77.07 C
ANISOU 3236 CE2 TYR B 146 11759 6831 10692 -1131 3918 -1317 C
ATOM 3237 CZ TYR B 146 -2.774 17.523 -12.112 1.00 66.56 C
ANISOU 3237 CZ TYR B 146 10287 5357 9646 -1120 3864 -1336 C
ATOM 3238 OH TYR B 146 -2.505 17.747 -13.444 1.00 71.56 O
ANISOU 3238 OH TYR B 146 10614 6080 10494 -1164 3553 -1232 O
ATOM 3239 N ALA B 147 -3.335 16.736 -4.763 1.00 84.66 N
ANISOU 3239 N ALA B 147 14478 7259 10432 -986 4814 -1817 N
ATOM 3240 CA ALA B 147 -3.970 17.046 -3.484 1.00 85.86 C
ANISOU 3240 CA ALA B 147 14942 7208 10472 -924 5161 -1902 C
ATOM 3241 C ALA B 147 -3.097 17.932 -2.602 1.00 92.11 C
ANISOU 3241 C ALA B 147 16110 7959 10930 -983 5027 -2142 C
ATOM 3242 O ALA B 147 -3.622 18.730 -1.816 1.00 97.26 O
ANISOU 3242 O ALA B 147 16987 8379 11587 -933 5339 -2259 O
ATOM 3243 CB ALA B 147 -4.325 15.754 -2.747 1.00 77.47 C
ANISOU 3243 CB ALA B 147 14012 6211 9211 -901 5249 -1807 C
ATOM 3244 N ILE B 148 -1.780 17.802 -2.705 1.00 89.87 N
ANISOU 3244 N ILE B 148 15898 7882 10364 -1091 4576 -2216 N
ATOM 3245 CA ILE B 148 -0.851 18.506 -1.825 1.00 91.92 C
ANISOU 3245 CA ILE B 148 16524 8119 10284 -1172 4395 -2429 C
ATOM 3246 C ILE B 148 -0.190 19.700 -2.511 1.00 99.00 C
ANISOU 3246 C ILE B 148 17330 8961 11323 -1230 4176 -2540 C
ATOM 3247 O ILE B 148 -0.105 20.786 -1.928 1.00102.55 O
ANISOU 3247 O ILE B 148 18028 9217 11719 -1246 4256 -2722 O
ATOM 3248 CB ILE B 148 0.214 17.523 -1.292 1.00 81.18 C
ANISOU 3248 CB ILE B 148 15327 7006 8511 -1261 4033 -2426 C
ATOM 3249 CG1 ILE B 148 -0.416 16.494 -0.334 1.00 78.76 C
ANISOU 3249 CG1 ILE B 148 15207 6701 8019 -1210 4260 -2356 C
ATOM 3250 CG2 ILE B 148 1.327 18.314 -0.608 1.00 88.31 C
ANISOU 3250 CG2 ILE B 148 16544 7900 9110 -1376 3767 -2629 C
ATOM 3251 CD1 ILE B 148 0.427 15.215 -0.079 1.00 87.43 C
ANISOU 3251 CD1 ILE B 148 16341 8056 8822 -1266 3924 -2277 C
ATOM 3252 N CYS B 149 0.287 19.512 -3.754 1.00 94.15 N
ANISOU 3252 N CYS B 149 16374 8506 10894 -1269 3897 -2435 N
ATOM 3253 CA CYS B 149 1.037 20.564 -4.433 1.00 92.16 C
ANISOU 3253 CA CYS B 149 16033 8218 10767 -1343 3634 -2523 C
ATOM 3254 C CYS B 149 0.150 21.546 -5.183 1.00 98.94 C
ANISOU 3254 C CYS B 149 16667 8840 12086 -1265 3883 -2500 C
ATOM 3255 O CYS B 149 0.501 22.729 -5.292 1.00117.30 O
ANISOU 3255 O CYS B 149 19049 11007 14514 -1302 3790 -2626 O
ATOM 3256 CB CYS B 149 2.068 19.951 -5.383 1.00 83.64 C
ANISOU 3256 CB CYS B 149 14712 7413 9655 -1434 3204 -2427 C
ATOM 3257 SG CYS B 149 3.298 18.923 -4.558 1.00 86.66 S
ANISOU 3257 SG CYS B 149 15315 8060 9552 -1526 2854 -2446 S
ATOM 3258 N HIS B 150 -0.993 21.087 -5.684 1.00 92.97 N
ANISOU 3258 N HIS B 150 15650 8042 11634 -1160 4190 -2332 N
ATOM 3259 CA HIS B 150 -1.960 21.925 -6.394 1.00 90.18 C
ANISOU 3259 CA HIS B 150 15030 7458 11777 -1069 4453 -2266 C
ATOM 3260 C HIS B 150 -3.330 21.608 -5.810 1.00 91.63 C
ANISOU 3260 C HIS B 150 15218 7484 12112 -938 4959 -2184 C
ATOM 3261 O HIS B 150 -4.170 20.954 -6.433 1.00100.58 O
ANISOU 3261 O HIS B 150 16041 8646 13530 -877 5130 -1982 O
ATOM 3262 CB HIS B 150 -1.883 21.695 -7.903 1.00 80.01 C
ANISOU 3262 CB HIS B 150 13305 6296 10798 -1095 4242 -2093 C
ATOM 3263 CG HIS B 150 -0.534 21.979 -8.487 1.00 82.38 C
ANISOU 3263 CG HIS B 150 13592 6746 10963 -1234 3754 -2152 C
ATOM 3264 ND1 HIS B 150 0.531 21.115 -8.361 1.00 80.48 N
ANISOU 3264 ND1 HIS B 150 13452 6780 10348 -1335 3429 -2168 N
ATOM 3265 CD2 HIS B 150 -0.072 23.044 -9.181 1.00 81.91 C
ANISOU 3265 CD2 HIS B 150 13420 6586 11115 -1292 3535 -2181 C
ATOM 3266 CE1 HIS B 150 1.587 21.628 -8.968 1.00 76.01 C
ANISOU 3266 CE1 HIS B 150 12821 6285 9775 -1451 3049 -2202 C
ATOM 3267 NE2 HIS B 150 1.248 22.800 -9.474 1.00 75.42 N
ANISOU 3267 NE2 HIS B 150 12626 5985 10046 -1436 3097 -2209 N
ATOM 3268 N PRO B 151 -3.574 22.074 -4.583 1.00 79.26 N
ANISOU 3268 N PRO B 151 14014 5740 10363 -901 5208 -2339 N
ATOM 3269 CA PRO B 151 -4.672 21.517 -3.775 1.00 93.39 C
ANISOU 3269 CA PRO B 151 15898 7424 12161 -804 5650 -2268 C
ATOM 3270 C PRO B 151 -6.041 21.633 -4.414 1.00104.52 C
ANISOU 3270 C PRO B 151 16927 8655 14129 -679 6038 -2070 C
ATOM 3271 O PRO B 151 -6.886 20.748 -4.218 1.00116.92 O
ANISOU 3271 O PRO B 151 18413 10228 15783 -625 6292 -1909 O
ATOM 3272 CB PRO B 151 -4.585 22.312 -2.474 1.00100.47 C
ANISOU 3272 CB PRO B 151 17255 8125 12794 -796 5828 -2504 C
ATOM 3273 CG PRO B 151 -3.158 22.800 -2.430 1.00101.95 C
ANISOU 3273 CG PRO B 151 17645 8423 12668 -931 5360 -2687 C
ATOM 3274 CD PRO B 151 -2.819 23.104 -3.849 1.00 88.28 C
ANISOU 3274 CD PRO B 151 15517 6762 11262 -959 5085 -2589 C
ATOM 3275 N LEU B 152 -6.315 22.702 -5.164 1.00 99.94 N
ANISOU 3275 N LEU B 152 16100 7903 13970 -630 6086 -2058 N
ATOM 3276 CA LEU B 152 -7.644 22.900 -5.750 1.00102.44 C
ANISOU 3276 CA LEU B 152 16014 8030 14876 -505 6455 -1847 C
ATOM 3277 C LEU B 152 -7.448 22.975 -7.257 1.00100.53 C
ANISOU 3277 C LEU B 152 15315 7900 14981 -533 6158 -1693 C
ATOM 3278 O LEU B 152 -7.468 24.054 -7.852 1.00113.65 O
ANISOU 3278 O LEU B 152 16800 9409 16974 -502 6104 -1701 O
ATOM 3279 CB LEU B 152 -8.325 24.148 -5.155 1.00114.54 C
ANISOU 3279 CB LEU B 152 17658 9209 16652 -394 6842 -1951 C
ATOM 3280 CG LEU B 152 -9.061 23.919 -3.830 1.00116.17 C
ANISOU 3280 CG LEU B 152 18181 9259 16698 -323 7295 -2005 C
ATOM 3281 CD1 LEU B 152 -8.096 23.525 -2.718 1.00108.85 C
ANISOU 3281 CD1 LEU B 152 17789 8477 15092 -423 7105 -2232 C
ATOM 3282 CD2 LEU B 152 -9.898 25.127 -3.424 1.00126.52 C
ANISOU 3282 CD2 LEU B 152 19518 10198 18355 -192 7734 -2071 C
ATOM 3283 N LEU B 153 -7.287 21.806 -7.871 1.00 93.90 N
ANISOU 3283 N LEU B 153 14289 7317 14072 -590 5962 -1546 N
ATOM 3284 CA LEU B 153 -7.358 21.674 -9.318 1.00 93.49 C
ANISOU 3284 CA LEU B 153 13764 7374 14383 -597 5740 -1359 C
ATOM 3285 C LEU B 153 -8.279 20.516 -9.677 1.00 97.52 C
ANISOU 3285 C LEU B 153 13978 7967 15107 -554 5921 -1116 C
ATOM 3286 O LEU B 153 -9.303 20.716 -10.341 1.00101.24 O
ANISOU 3286 O LEU B 153 14020 8326 16119 -457 6105 -906 O
ATOM 3287 CB LEU B 153 -5.963 21.463 -9.919 1.00 82.56 C
ANISOU 3287 CB LEU B 153 12448 6247 12675 -735 5206 -1450 C
ATOM 3288 CG LEU B 153 -4.989 22.647 -10.001 1.00 76.60 C
ANISOU 3288 CG LEU B 153 11850 5421 11834 -805 4917 -1625 C
ATOM 3289 CD1 LEU B 153 -3.819 22.307 -10.920 1.00 65.40 C
ANISOU 3289 CD1 LEU B 153 10346 4261 10242 -944 4401 -1611 C
ATOM 3290 CD2 LEU B 153 -5.684 23.910 -10.520 1.00 71.83 C
ANISOU 3290 CD2 LEU B 153 10989 4539 11766 -715 5051 -1552 C
ATOM 3291 N PHE B 154 -7.908 19.307 -9.247 1.00 90.84 N
ANISOU 3291 N PHE B 154 13342 7314 13857 -625 5840 -1129 N
ATOM 3292 CA PHE B 154 -8.677 18.095 -9.484 1.00 94.04 C
ANISOU 3292 CA PHE B 154 13537 7790 14406 -608 5981 -912 C
ATOM 3293 C PHE B 154 -9.176 17.515 -8.169 1.00 93.66 C
ANISOU 3293 C PHE B 154 13826 7616 14144 -592 6278 -916 C
ATOM 3294 O PHE B 154 -8.409 17.389 -7.208 1.00 87.74 O
ANISOU 3294 O PHE B 154 13512 6933 12893 -638 6164 -1108 O
ATOM 3295 CB PHE B 154 -7.829 17.067 -10.233 1.00 88.86 C
ANISOU 3295 CB PHE B 154 12819 7451 13491 -698 5582 -904 C
ATOM 3296 CG PHE B 154 -7.420 17.516 -11.600 1.00 83.32 C
ANISOU 3296 CG PHE B 154 11777 6872 13007 -686 5233 -884 C
ATOM 3297 CD1 PHE B 154 -8.121 17.097 -12.709 1.00 76.46 C
ANISOU 3297 CD1 PHE B 154 10454 6077 12519 -574 5139 -700 C
ATOM 3298 CD2 PHE B 154 -6.348 18.367 -11.774 1.00 85.89 C
ANISOU 3298 CD2 PHE B 154 12252 7224 13158 -768 4915 -1040 C
ATOM 3299 CE1 PHE B 154 -7.753 17.504 -13.973 1.00 75.00 C
ANISOU 3299 CE1 PHE B 154 10013 5984 12498 -590 4669 -625 C
ATOM 3300 CE2 PHE B 154 -5.972 18.782 -13.047 1.00 82.24 C
ANISOU 3300 CE2 PHE B 154 11504 6845 12899 -792 4530 -969 C
ATOM 3301 CZ PHE B 154 -6.679 18.347 -14.145 1.00 79.67 C
ANISOU 3301 CZ PHE B 154 10761 6593 12914 -717 4394 -744 C
ATOM 3302 N LYS B 155 -10.463 17.171 -8.140 1.00 96.96 N
ANISOU 3302 N LYS B 155 14025 7849 14965 -519 6628 -692 N
ATOM 3303 CA LYS B 155 -11.100 16.493 -7.011 1.00115.30 C
ANISOU 3303 CA LYS B 155 16622 10025 17163 -477 6894 -658 C
ATOM 3304 C LYS B 155 -11.001 14.977 -7.165 1.00121.14 C
ANISOU 3304 C LYS B 155 17378 10909 17740 -530 6691 -549 C
ATOM 3305 O LYS B 155 -11.323 14.438 -8.227 1.00123.93 O
ANISOU 3305 O LYS B 155 17324 11440 18325 -443 6388 -429 O
ATOM 3306 CB LYS B 155 -12.559 16.924 -6.896 1.00128.85 C
ANISOU 3306 CB LYS B 155 18099 11410 19447 -359 7354 -462 C
ATOM 3307 CG LYS B 155 -12.760 18.416 -6.750 1.00139.57 C
ANISOU 3307 CG LYS B 155 19421 12582 21025 -287 7580 -560 C
ATOM 3308 CD LYS B 155 -14.232 18.770 -6.619 1.00141.00 C
ANISOU 3308 CD LYS B 155 19345 12428 21801 -166 8047 -337 C
ATOM 3309 CE LYS B 155 -14.459 20.272 -6.671 1.00141.56 C
ANISOU 3309 CE LYS B 155 19304 12302 22180 -85 8249 -409 C
ATOM 3310 NZ LYS B 155 -15.865 20.650 -6.364 1.00149.91 N
ANISOU 3310 NZ LYS B 155 20159 13011 23790 41 8740 -207 N
ATOM 3311 N SER B 156 -10.562 14.292 -6.108 1.00121.81 N
ANISOU 3311 N SER B 156 17870 11076 17335 -539 6626 -678 N
ATOM 3312 CA SER B 156 -10.436 12.837 -6.105 1.00121.28 C
ANISOU 3312 CA SER B 156 17857 11139 17086 -561 6420 -607 C
ATOM 3313 C SER B 156 -11.408 12.234 -5.099 1.00120.34 C
ANISOU 3313 C SER B 156 17887 10840 16998 -450 6728 -541 C
ATOM 3314 O SER B 156 -11.212 12.372 -3.888 1.00121.75 O
ANISOU 3314 O SER B 156 18428 11016 16813 -433 6858 -687 O
ATOM 3315 CB SER B 156 -9.003 12.423 -5.780 1.00126.25 C
ANISOU 3315 CB SER B 156 18776 12070 17121 -660 6026 -792 C
ATOM 3316 OG SER B 156 -8.824 12.261 -4.379 1.00135.32 O
ANISOU 3316 OG SER B 156 20328 13216 17870 -633 6115 -922 O
ATOM 3317 N THR B 157 -12.446 11.559 -5.594 1.00116.45 N
ANISOU 3317 N THR B 157 17105 10220 16922 -349 6804 -339 N
ATOM 3318 CA THR B 157 -13.383 10.822 -4.753 1.00114.27 C
ANISOU 3318 CA THR B 157 16932 9779 16704 -235 7083 -254 C
ATOM 3319 C THR B 157 -13.139 9.319 -4.816 1.00118.89 C
ANISOU 3319 C THR B 157 17549 10558 17065 -224 6799 -236 C
ATOM 3320 O THR B 157 -12.438 8.807 -5.695 1.00116.69 O
ANISOU 3320 O THR B 157 17133 10517 16686 -276 6389 -262 O
ATOM 3321 CB THR B 157 -14.837 11.100 -5.154 1.00114.97 C
ANISOU 3321 CB THR B 157 16621 9649 17412 -61 7335 -53 C
ATOM 3322 OG1 THR B 157 -14.936 11.175 -6.582 1.00106.91 O
ANISOU 3322 OG1 THR B 157 15110 8820 16693 -2 6960 29 O
ATOM 3323 CG2 THR B 157 -15.327 12.406 -4.534 1.00124.40 C
ANISOU 3323 CG2 THR B 157 17918 10532 18817 -54 7821 -55 C
ATOM 3324 N ALA B 158 -13.718 8.619 -3.841 1.00122.59 N
ANISOU 3324 N ALA B 158 18176 10985 17417 -141 7009 -208 N
ATOM 3325 CA ALA B 158 -13.740 7.163 -3.890 1.00115.99 C
ANISOU 3325 CA ALA B 158 17307 10314 16451 -105 6804 -156 C
ATOM 3326 C ALA B 158 -14.537 6.657 -5.084 1.00122.84 C
ANISOU 3326 C ALA B 158 17715 11152 17807 16 6690 10 C
ATOM 3327 O ALA B 158 -14.240 5.581 -5.623 1.00120.00 O
ANISOU 3327 O ALA B 158 17242 11024 17329 15 6374 20 O
ATOM 3328 CB ALA B 158 -14.330 6.607 -2.597 1.00118.23 C
ANISOU 3328 CB ALA B 158 17821 10541 16561 -34 7106 -139 C
ATOM 3329 N ARG B 159 -15.560 7.406 -5.501 1.00130.56 N
ANISOU 3329 N ARG B 159 18386 11915 19307 133 6910 142 N
ATOM 3330 CA ARG B 159 -16.349 6.989 -6.651 1.00129.96 C
ANISOU 3330 CA ARG B 159 17794 11928 19655 272 6723 309 C
ATOM 3331 C ARG B 159 -15.508 6.998 -7.921 1.00112.85 C
ANISOU 3331 C ARG B 159 15417 10059 17402 211 6248 237 C
ATOM 3332 O ARG B 159 -15.639 6.105 -8.765 1.00101.82 O
ANISOU 3332 O ARG B 159 13764 8828 16094 258 6001 313 O
ATOM 3333 CB ARG B 159 -17.557 7.908 -6.820 1.00138.46 C
ANISOU 3333 CB ARG B 159 18550 12770 21290 404 7000 484 C
ATOM 3334 CG ARG B 159 -18.240 7.756 -8.154 1.00140.22 C
ANISOU 3334 CG ARG B 159 18213 13101 21965 524 6742 672 C
ATOM 3335 CD ARG B 159 -19.210 6.600 -8.078 1.00145.00 C
ANISOU 3335 CD ARG B 159 18636 13659 22798 644 6827 868 C
ATOM 3336 NE ARG B 159 -19.929 6.366 -9.323 1.00146.47 N
ANISOU 3336 NE ARG B 159 18264 14017 23372 703 6526 1102 N
ATOM 3337 CZ ARG B 159 -19.562 5.461 -10.223 1.00146.52 C
ANISOU 3337 CZ ARG B 159 18089 14426 23157 576 6043 1142 C
ATOM 3338 NH1 ARG B 159 -18.491 4.711 -10.007 1.00145.99 N
ANISOU 3338 NH1 ARG B 159 18334 14589 22548 439 5855 952 N
ATOM 3339 NH2 ARG B 159 -20.265 5.302 -11.333 1.00145.96 N
ANISOU 3339 NH2 ARG B 159 17554 14505 23397 555 5733 1389 N
ATOM 3340 N ARG B 160 -14.645 8.008 -8.078 1.00110.78 N
ANISOU 3340 N ARG B 160 15263 9853 16976 98 6145 101 N
ATOM 3341 CA ARG B 160 -13.721 8.033 -9.208 1.00111.25 C
ANISOU 3341 CA ARG B 160 15174 10188 16907 33 5727 14 C
ATOM 3342 C ARG B 160 -12.506 7.136 -9.007 1.00111.06 C
ANISOU 3342 C ARG B 160 15459 10374 16365 -107 5475 -131 C
ATOM 3343 O ARG B 160 -11.956 6.625 -9.989 1.00109.51 O
ANISOU 3343 O ARG B 160 15110 10410 16091 -133 5149 -160 O
ATOM 3344 CB ARG B 160 -13.240 9.458 -9.476 1.00109.09 C
ANISOU 3344 CB ARG B 160 14881 9891 16677 -30 5716 -66 C
ATOM 3345 CG ARG B 160 -14.327 10.437 -9.851 1.00114.13 C
ANISOU 3345 CG ARG B 160 15170 10337 17856 106 5909 83 C
ATOM 3346 CD ARG B 160 -13.785 11.857 -9.836 1.00114.28 C
ANISOU 3346 CD ARG B 160 15264 10285 17873 12 5969 -10 C
ATOM 3347 NE ARG B 160 -14.794 12.821 -10.251 1.00116.14 N
ANISOU 3347 NE ARG B 160 15144 10331 18654 148 6132 140 N
ATOM 3348 CZ ARG B 160 -15.806 13.203 -9.483 1.00125.35 C
ANISOU 3348 CZ ARG B 160 16326 11201 20102 188 6545 273 C
ATOM 3349 NH1 ARG B 160 -15.941 12.691 -8.267 1.00129.18 N
ANISOU 3349 NH1 ARG B 160 17164 11563 20354 148 6860 239 N
ATOM 3350 NH2 ARG B 160 -16.688 14.086 -9.931 1.00132.84 N
ANISOU 3350 NH2 ARG B 160 16928 11973 21572 297 6659 434 N
ATOM 3351 N ALA B 161 -12.077 6.920 -7.760 1.00107.94 N
ANISOU 3351 N ALA B 161 15495 9893 15624 -201 5633 -206 N
ATOM 3352 CA ALA B 161 -10.945 6.028 -7.527 1.00 97.30 C
ANISOU 3352 CA ALA B 161 14421 8730 13818 -325 5379 -308 C
ATOM 3353 C ALA B 161 -11.269 4.624 -8.002 1.00100.60 C
ANISOU 3353 C ALA B 161 14674 9276 14272 -249 5224 -236 C
ATOM 3354 O ALA B 161 -10.396 3.910 -8.514 1.00 98.19 O
ANISOU 3354 O ALA B 161 14373 9221 13712 -329 4890 -290 O
ATOM 3355 CB ALA B 161 -10.583 6.013 -6.044 1.00 99.03 C
ANISOU 3355 CB ALA B 161 15091 8866 13669 -402 5577 -368 C
ATOM 3356 N LEU B 162 -12.523 4.204 -7.822 1.00107.39 N
ANISOU 3356 N LEU B 162 15341 10050 15412 -115 5432 -82 N
ATOM 3357 CA LEU B 162 -12.945 2.926 -8.368 1.00 99.88 C
ANISOU 3357 CA LEU B 162 14129 9330 14491 -85 5232 49 C
ATOM 3358 C LEU B 162 -13.072 3.011 -9.885 1.00 96.67 C
ANISOU 3358 C LEU B 162 13289 9135 14308 -100 4917 145 C
ATOM 3359 O LEU B 162 -12.794 2.037 -10.594 1.00 95.70 O
ANISOU 3359 O LEU B 162 13033 9279 14048 -190 4583 208 O
ATOM 3360 CB LEU B 162 -14.251 2.493 -7.712 1.00100.57 C
ANISOU 3360 CB LEU B 162 14121 9275 14816 29 5535 218 C
ATOM 3361 CG LEU B 162 -14.132 2.248 -6.211 1.00113.18 C
ANISOU 3361 CG LEU B 162 16140 10742 16120 17 5805 154 C
ATOM 3362 CD1 LEU B 162 -15.477 2.462 -5.548 1.00124.13 C
ANISOU 3362 CD1 LEU B 162 17442 11889 17831 147 6226 298 C
ATOM 3363 CD2 LEU B 162 -13.600 0.851 -5.929 1.00115.32 C
ANISOU 3363 CD2 LEU B 162 16546 11240 16029 -51 5594 150 C
ATOM 3364 N GLY B 163 -13.505 4.165 -10.397 1.00100.42 N
ANISOU 3364 N GLY B 163 13543 9489 15122 -37 4999 183 N
ATOM 3365 CA GLY B 163 -13.521 4.364 -11.839 1.00 99.70 C
ANISOU 3365 CA GLY B 163 13069 9627 15187 -101 4632 300 C
ATOM 3366 C GLY B 163 -12.141 4.270 -12.465 1.00 96.10 C
ANISOU 3366 C GLY B 163 12733 9415 14367 -251 4283 159 C
ATOM 3367 O GLY B 163 -11.954 3.625 -13.503 1.00 93.52 O
ANISOU 3367 O GLY B 163 12220 9348 13965 -372 3887 265 O
ATOM 3368 N SER B 164 -11.161 4.951 -11.865 1.00 94.47 N
ANISOU 3368 N SER B 164 12858 9099 13937 -266 4421 -74 N
ATOM 3369 CA SER B 164 -9.799 4.887 -12.383 1.00 83.43 C
ANISOU 3369 CA SER B 164 11581 7916 12203 -404 4118 -209 C
ATOM 3370 C SER B 164 -9.280 3.458 -12.367 1.00 86.90 C
ANISOU 3370 C SER B 164 12134 8549 12337 -480 3896 -206 C
ATOM 3371 O SER B 164 -8.606 3.022 -13.310 1.00 87.63 O
ANISOU 3371 O SER B 164 12126 8882 12288 -588 3550 -187 O
ATOM 3372 CB SER B 164 -8.881 5.799 -11.573 1.00 73.07 C
ANISOU 3372 CB SER B 164 10652 6415 10697 -441 4304 -444 C
ATOM 3373 OG SER B 164 -9.316 7.140 -11.606 1.00 86.75 O
ANISOU 3373 OG SER B 164 12257 8015 12691 -392 4477 -427 O
ATOM 3374 N ILE B 165 -9.595 2.710 -11.308 1.00 81.90 N
ANISOU 3374 N ILE B 165 11711 7798 11608 -431 4091 -207 N
ATOM 3375 CA ILE B 165 -9.067 1.358 -11.185 1.00 76.20 C
ANISOU 3375 CA ILE B 165 11113 7234 10604 -493 3906 -205 C
ATOM 3376 C ILE B 165 -9.596 0.485 -12.317 1.00 76.37 C
ANISOU 3376 C ILE B 165 10788 7468 10761 -537 3633 -16 C
ATOM 3377 O ILE B 165 -8.925 -0.461 -12.753 1.00 71.34 O
ANISOU 3377 O ILE B 165 10188 6999 9918 -622 3383 -23 O
ATOM 3378 CB ILE B 165 -9.405 0.773 -9.797 1.00 74.04 C
ANISOU 3378 CB ILE B 165 11113 6804 10217 -439 4158 -201 C
ATOM 3379 CG1 ILE B 165 -8.722 1.596 -8.700 1.00 73.25 C
ANISOU 3379 CG1 ILE B 165 11397 6528 9907 -482 4313 -339 C
ATOM 3380 CG2 ILE B 165 -8.974 -0.684 -9.692 1.00 66.92 C
ANISOU 3380 CG2 ILE B 165 10295 6060 9070 -486 3973 -169 C
ATOM 3381 CD1 ILE B 165 -9.244 1.310 -7.299 1.00 79.81 C
ANISOU 3381 CD1 ILE B 165 12467 7218 10641 -435 4589 -296 C
ATOM 3382 N LEU B 166 -10.807 0.777 -12.806 1.00 86.97 N
ANISOU 3382 N LEU B 166 11808 8779 12458 -501 3660 170 N
ATOM 3383 CA LEU B 166 -11.359 0.005 -13.912 1.00 91.60 C
ANISOU 3383 CA LEU B 166 12103 9539 13163 -602 3341 376 C
ATOM 3384 C LEU B 166 -10.639 0.316 -15.217 1.00 90.55 C
ANISOU 3384 C LEU B 166 11860 9590 12953 -735 2965 376 C
ATOM 3385 O LEU B 166 -10.453 -0.573 -16.054 1.00 91.83 O
ANISOU 3385 O LEU B 166 11962 9913 13014 -862 2656 455 O
ATOM 3386 CB LEU B 166 -12.855 0.283 -14.035 1.00 93.24 C
ANISOU 3386 CB LEU B 166 12017 9641 13769 -547 3451 588 C
ATOM 3387 CG LEU B 166 -13.674 -0.616 -13.116 1.00 87.80 C
ANISOU 3387 CG LEU B 166 11366 8852 13141 -477 3687 673 C
ATOM 3388 CD1 LEU B 166 -15.100 -0.107 -12.971 1.00 94.64 C
ANISOU 3388 CD1 LEU B 166 11970 9548 14439 -373 3911 854 C
ATOM 3389 CD2 LEU B 166 -13.660 -2.050 -13.643 1.00 79.33 C
ANISOU 3389 CD2 LEU B 166 10256 7956 11932 -620 3389 777 C
ATOM 3390 N GLY B 167 -10.225 1.571 -15.409 1.00 89.19 N
ANISOU 3390 N GLY B 167 11680 9382 12827 -717 2993 292 N
ATOM 3391 CA GLY B 167 -9.468 1.909 -16.601 1.00 86.13 C
ANISOU 3391 CA GLY B 167 11213 9169 12345 -846 2644 295 C
ATOM 3392 C GLY B 167 -8.099 1.254 -16.608 1.00 86.69 C
ANISOU 3392 C GLY B 167 11511 9361 12064 -904 2524 131 C
ATOM 3393 O GLY B 167 -7.590 0.853 -17.661 1.00 88.11 O
ANISOU 3393 O GLY B 167 11627 9708 12144 -1019 2210 177 O
ATOM 3394 N ILE B 168 -7.475 1.154 -15.432 1.00 84.95 N
ANISOU 3394 N ILE B 168 11585 9041 11650 -830 2777 -60 N
ATOM 3395 CA ILE B 168 -6.131 0.593 -15.344 1.00 70.29 C
ANISOU 3395 CA ILE B 168 9966 7276 9466 -885 2676 -221 C
ATOM 3396 C ILE B 168 -6.096 -0.809 -15.932 1.00 71.15 C
ANISOU 3396 C ILE B 168 10025 7510 9498 -943 2466 -133 C
ATOM 3397 O ILE B 168 -5.212 -1.146 -16.730 1.00 76.88 O
ANISOU 3397 O ILE B 168 10762 8370 10080 -1024 2247 -178 O
ATOM 3398 CB ILE B 168 -5.650 0.591 -13.883 1.00 57.04 C
ANISOU 3398 CB ILE B 168 8648 5434 7590 -827 2939 -393 C
ATOM 3399 CG1 ILE B 168 -5.578 2.021 -13.354 1.00 55.63 C
ANISOU 3399 CG1 ILE B 168 8571 5095 7471 -802 3143 -502 C
ATOM 3400 CG2 ILE B 168 -4.318 -0.102 -13.765 1.00 40.85 C
ANISOU 3400 CG2 ILE B 168 6830 3461 5229 -900 2785 -513 C
ATOM 3401 CD1 ILE B 168 -4.921 2.097 -12.027 1.00 44.32 C
ANISOU 3401 CD1 ILE B 168 7535 3486 5817 -832 3277 -624 C
ATOM 3402 N TRP B 169 -7.061 -1.647 -15.545 1.00 62.80 N
ANISOU 3402 N TRP B 169 8921 6397 8545 -906 2548 -9 N
ATOM 3403 CA TRP B 169 -7.091 -3.031 -16.013 1.00 59.51 C
ANISOU 3403 CA TRP B 169 8483 6063 8068 -970 2375 74 C
ATOM 3404 C TRP B 169 -7.368 -3.123 -17.508 1.00 64.23 C
ANISOU 3404 C TRP B 169 8838 6784 8781 -1096 2052 222 C
ATOM 3405 O TRP B 169 -6.783 -3.965 -18.202 1.00 71.90 O
ANISOU 3405 O TRP B 169 9852 7837 9630 -1171 1869 204 O
ATOM 3406 CB TRP B 169 -8.132 -3.808 -15.209 1.00 58.61 C
ANISOU 3406 CB TRP B 169 8364 5849 8056 -916 2544 190 C
ATOM 3407 CG TRP B 169 -7.655 -4.063 -13.821 1.00 57.16 C
ANISOU 3407 CG TRP B 169 8486 5557 7674 -822 2795 55 C
ATOM 3408 CD1 TRP B 169 -7.885 -3.293 -12.718 1.00 56.40 C
ANISOU 3408 CD1 TRP B 169 8529 5312 7588 -726 3079 -12 C
ATOM 3409 CD2 TRP B 169 -6.830 -5.147 -13.388 1.00 48.35 C
ANISOU 3409 CD2 TRP B 169 7609 4453 6307 -830 2763 -19 C
ATOM 3410 NE1 TRP B 169 -7.270 -3.845 -11.619 1.00 56.79 N
ANISOU 3410 NE1 TRP B 169 8896 5293 7388 -694 3184 -104 N
ATOM 3411 CE2 TRP B 169 -6.615 -4.983 -12.005 1.00 55.38 C
ANISOU 3411 CE2 TRP B 169 8770 5218 7053 -750 2988 -102 C
ATOM 3412 CE3 TRP B 169 -6.258 -6.251 -14.033 1.00 39.93 C
ANISOU 3412 CE3 TRP B 169 6568 3472 5130 -900 2564 -13 C
ATOM 3413 CZ2 TRP B 169 -5.855 -5.878 -11.256 1.00 48.34 C
ANISOU 3413 CZ2 TRP B 169 8146 4308 5913 -744 2976 -147 C
ATOM 3414 CZ3 TRP B 169 -5.503 -7.140 -13.287 1.00 47.64 C
ANISOU 3414 CZ3 TRP B 169 7813 4410 5880 -874 2601 -81 C
ATOM 3415 CH2 TRP B 169 -5.306 -6.950 -11.914 1.00 45.29 C
ANISOU 3415 CH2 TRP B 169 7757 4008 5443 -798 2785 -133 C
ATOM 3416 N ALA B 170 -8.268 -2.283 -18.018 1.00 59.43 N
ANISOU 3416 N ALA B 170 8003 6174 8404 -1129 1981 370 N
ATOM 3417 CA ALA B 170 -8.516 -2.284 -19.453 1.00 56.96 C
ANISOU 3417 CA ALA B 170 7511 5973 8159 -1285 1641 526 C
ATOM 3418 C ALA B 170 -7.250 -1.907 -20.215 1.00 75.65 C
ANISOU 3418 C ALA B 170 9932 8448 10363 -1320 1482 413 C
ATOM 3419 O ALA B 170 -6.999 -2.407 -21.319 1.00 86.04 O
ANISOU 3419 O ALA B 170 11212 9834 11644 -1429 1261 464 O
ATOM 3420 CB ALA B 170 -9.667 -1.336 -19.796 1.00 57.93 C
ANISOU 3420 CB ALA B 170 7429 6036 8545 -1323 1647 679 C
ATOM 3421 N VAL B 171 -6.444 -1.014 -19.647 1.00 76.41 N
ANISOU 3421 N VAL B 171 10137 8523 10372 -1238 1643 237 N
ATOM 3422 CA VAL B 171 -5.191 -0.645 -20.294 1.00 56.16 C
ANISOU 3422 CA VAL B 171 7634 6061 7642 -1278 1521 113 C
ATOM 3423 C VAL B 171 -4.132 -1.721 -20.076 1.00 57.55 C
ANISOU 3423 C VAL B 171 8036 6273 7559 -1275 1563 -65 C
ATOM 3424 O VAL B 171 -3.460 -2.146 -21.022 1.00 54.47 O
ANISOU 3424 O VAL B 171 7657 5980 7058 -1346 1403 -100 O
ATOM 3425 CB VAL B 171 -4.753 0.747 -19.794 1.00 41.77 C
ANISOU 3425 CB VAL B 171 5847 4198 5826 -1229 1653 3 C
ATOM 3426 CG1 VAL B 171 -3.402 1.155 -20.377 1.00 54.09 C
ANISOU 3426 CG1 VAL B 171 7474 5873 7206 -1283 1536 -127 C
ATOM 3427 CG2 VAL B 171 -5.816 1.774 -20.151 1.00 33.60 C
ANISOU 3427 CG2 VAL B 171 4590 3117 5058 -1244 1601 186 C
ATOM 3428 N SER B 172 -4.002 -2.212 -18.846 1.00 58.37 N
ANISOU 3428 N SER B 172 8336 6285 7558 -1198 1783 -171 N
ATOM 3429 CA SER B 172 -3.009 -3.248 -18.587 1.00 38.96 C
ANISOU 3429 CA SER B 172 6106 3841 4856 -1208 1805 -312 C
ATOM 3430 C SER B 172 -3.302 -4.509 -19.402 1.00 53.16 C
ANISOU 3430 C SER B 172 7858 5672 6670 -1268 1663 -225 C
ATOM 3431 O SER B 172 -2.398 -5.089 -20.023 1.00 61.96 O
ANISOU 3431 O SER B 172 9072 6851 7621 -1327 1580 -323 O
ATOM 3432 CB SER B 172 -2.961 -3.538 -17.088 1.00 29.07 C
ANISOU 3432 CB SER B 172 5080 2457 3508 -1121 2033 -387 C
ATOM 3433 OG SER B 172 -2.578 -2.364 -16.393 1.00 45.59 O
ANISOU 3433 OG SER B 172 7266 4493 5564 -1095 2150 -490 O
ATOM 3434 N LEU B 173 -4.575 -4.916 -19.455 1.00 59.49 N
ANISOU 3434 N LEU B 173 8510 6420 7674 -1272 1635 -38 N
ATOM 3435 CA LEU B 173 -4.959 -6.144 -20.149 1.00 50.39 C
ANISOU 3435 CA LEU B 173 7329 5262 6554 -1349 1498 55 C
ATOM 3436 C LEU B 173 -4.750 -6.034 -21.654 1.00 48.32 C
ANISOU 3436 C LEU B 173 6963 5089 6306 -1459 1263 86 C
ATOM 3437 O LEU B 173 -4.521 -7.049 -22.326 1.00 46.61 O
ANISOU 3437 O LEU B 173 6829 4870 6008 -1531 1178 53 O
ATOM 3438 CB LEU B 173 -6.421 -6.460 -19.844 1.00 53.70 C
ANISOU 3438 CB LEU B 173 7590 5606 7208 -1357 1497 276 C
ATOM 3439 CG LEU B 173 -6.700 -6.774 -18.373 1.00 53.28 C
ANISOU 3439 CG LEU B 173 7661 5453 7129 -1248 1758 250 C
ATOM 3440 CD1 LEU B 173 -8.185 -6.944 -18.111 1.00 46.91 C
ANISOU 3440 CD1 LEU B 173 6679 4586 6560 -1269 1775 469 C
ATOM 3441 CD2 LEU B 173 -5.922 -7.985 -17.904 1.00 56.19 C
ANISOU 3441 CD2 LEU B 173 8279 5779 7291 -1223 1828 135 C
ATOM 3442 N ALA B 174 -4.884 -4.825 -22.200 1.00 47.09 N
ANISOU 3442 N ALA B 174 6640 4993 6258 -1475 1166 155 N
ATOM 3443 CA ALA B 174 -4.664 -4.609 -23.625 1.00 52.34 C
ANISOU 3443 CA ALA B 174 7218 5735 6935 -1568 961 189 C
ATOM 3444 C ALA B 174 -3.183 -4.648 -23.968 1.00 59.40 C
ANISOU 3444 C ALA B 174 8308 6731 7532 -1589 996 -51 C
ATOM 3445 O ALA B 174 -2.727 -5.512 -24.724 1.00 64.85 O
ANISOU 3445 O ALA B 174 9119 7455 8067 -1671 942 -132 O
ATOM 3446 CB ALA B 174 -5.281 -3.279 -24.053 1.00 60.41 C
ANISOU 3446 CB ALA B 174 8024 6761 8168 -1596 874 349 C
ATOM 3447 N ILE B 175 -2.415 -3.702 -23.430 1.00 54.85 N
ANISOU 3447 N ILE B 175 7770 6202 6869 -1535 1088 -161 N
ATOM 3448 CA ILE B 175 -1.045 -3.504 -23.889 1.00 53.14 C
ANISOU 3448 CA ILE B 175 7671 6103 6417 -1579 1083 -337 C
ATOM 3449 C ILE B 175 -0.133 -4.691 -23.621 1.00 59.32 C
ANISOU 3449 C ILE B 175 8689 6884 6968 -1600 1186 -504 C
ATOM 3450 O ILE B 175 0.907 -4.831 -24.274 1.00 53.88 O
ANISOU 3450 O ILE B 175 8081 6296 6095 -1668 1175 -618 O
ATOM 3451 CB ILE B 175 -0.483 -2.220 -23.264 1.00 47.81 C
ANISOU 3451 CB ILE B 175 6975 5455 5736 -1529 1151 -400 C
ATOM 3452 CG1 ILE B 175 -0.496 -2.327 -21.734 1.00 41.59 C
ANISOU 3452 CG1 ILE B 175 6321 4556 4925 -1444 1350 -475 C
ATOM 3453 CG2 ILE B 175 -1.301 -1.024 -23.759 1.00 54.20 C
ANISOU 3453 CG2 ILE B 175 7550 6257 6787 -1523 1033 -218 C
ATOM 3454 CD1 ILE B 175 -0.133 -1.039 -21.015 1.00 25.46 C
ANISOU 3454 CD1 ILE B 175 4285 2497 2890 -1411 1433 -537 C
ATOM 3455 N MET B 176 -0.484 -5.551 -22.677 1.00 69.23 N
ANISOU 3455 N MET B 176 10049 8019 8234 -1542 1299 -503 N
ATOM 3456 CA MET B 176 0.264 -6.783 -22.475 1.00 64.94 C
ANISOU 3456 CA MET B 176 9726 7435 7513 -1556 1386 -614 C
ATOM 3457 C MET B 176 -0.113 -7.876 -23.465 1.00 72.64 C
ANISOU 3457 C MET B 176 10729 8390 8478 -1640 1296 -574 C
ATOM 3458 O MET B 176 0.539 -8.925 -23.484 1.00 70.09 O
ANISOU 3458 O MET B 176 10586 8025 8020 -1655 1368 -650 O
ATOM 3459 CB MET B 176 0.076 -7.260 -21.044 1.00 49.23 C
ANISOU 3459 CB MET B 176 7865 5306 5532 -1455 1535 -611 C
ATOM 3460 CG MET B 176 0.760 -6.328 -20.064 1.00 50.09 C
ANISOU 3460 CG MET B 176 8040 5398 5595 -1404 1616 -699 C
ATOM 3461 SD MET B 176 2.186 -5.498 -20.786 1.00 52.11 S
ANISOU 3461 SD MET B 176 8154 5806 5838 -1463 1456 -717 S
ATOM 3462 CE MET B 176 2.452 -4.247 -19.548 1.00 58.01 C
ANISOU 3462 CE MET B 176 8905 6515 6622 -1426 1509 -707 C
ATOM 3463 N VAL B 177 -1.126 -7.633 -24.305 1.00 80.96 N
ANISOU 3463 N VAL B 177 11614 9459 9686 -1698 1136 -437 N
ATOM 3464 CA VAL B 177 -1.507 -8.617 -25.323 1.00 70.74 C
ANISOU 3464 CA VAL B 177 10372 8135 8370 -1809 1026 -406 C
ATOM 3465 C VAL B 177 -0.354 -8.947 -26.259 1.00 64.54 C
ANISOU 3465 C VAL B 177 9748 7440 7334 -1898 1044 -557 C
ATOM 3466 O VAL B 177 -0.129 -10.141 -26.531 1.00 59.89 O
ANISOU 3466 O VAL B 177 9330 6776 6650 -1939 1078 -613 O
ATOM 3467 CB VAL B 177 -2.749 -8.118 -26.090 1.00 57.31 C
ANISOU 3467 CB VAL B 177 8445 6433 6898 -1868 836 -210 C
ATOM 3468 CG1 VAL B 177 -2.884 -8.839 -27.420 1.00 49.02 C
ANISOU 3468 CG1 VAL B 177 7483 5390 5753 -2023 700 -218 C
ATOM 3469 CG2 VAL B 177 -3.990 -8.294 -25.235 1.00 52.95 C
ANISOU 3469 CG2 VAL B 177 7741 5753 6624 -1801 846 -27 C
ATOM 3470 N PRO B 178 0.408 -7.976 -26.783 1.00 58.13 N
ANISOU 3470 N PRO B 178 8886 6778 6425 -1928 1038 -610 N
ATOM 3471 CA PRO B 178 1.525 -8.348 -27.660 1.00 52.28 C
ANISOU 3471 CA PRO B 178 8262 6122 5479 -2015 1105 -708 C
ATOM 3472 C PRO B 178 2.503 -9.279 -26.975 1.00 45.52 C
ANISOU 3472 C PRO B 178 7503 5169 4623 -1933 1255 -770 C
ATOM 3473 O PRO B 178 3.089 -10.145 -27.633 1.00 43.94 O
ANISOU 3473 O PRO B 178 7376 4924 4393 -1934 1252 -836 O
ATOM 3474 CB PRO B 178 2.175 -7.000 -28.009 1.00 54.22 C
ANISOU 3474 CB PRO B 178 8383 6537 5680 -2034 1092 -720 C
ATOM 3475 CG PRO B 178 1.162 -5.966 -27.670 1.00 53.10 C
ANISOU 3475 CG PRO B 178 8066 6376 5734 -1971 951 -613 C
ATOM 3476 CD PRO B 178 0.415 -6.533 -26.496 1.00 60.71 C
ANISOU 3476 CD PRO B 178 9038 7184 6846 -1871 1005 -569 C
ATOM 3477 N GLN B 179 2.695 -9.119 -25.665 1.00 58.09 N
ANISOU 3477 N GLN B 179 9077 6703 6293 -1814 1330 -761 N
ATOM 3478 CA GLN B 179 3.508 -10.068 -24.913 1.00 57.86 C
ANISOU 3478 CA GLN B 179 9111 6564 6309 -1644 1354 -816 C
ATOM 3479 C GLN B 179 2.984 -11.497 -25.062 1.00 65.59 C
ANISOU 3479 C GLN B 179 10263 7395 7263 -1642 1369 -829 C
ATOM 3480 O GLN B 179 3.738 -12.412 -25.420 1.00 75.72 O
ANISOU 3480 O GLN B 179 11603 8640 8526 -1546 1358 -918 O
ATOM 3481 CB GLN B 179 3.582 -9.648 -23.441 1.00 55.51 C
ANISOU 3481 CB GLN B 179 8800 6225 6064 -1525 1397 -781 C
ATOM 3482 CG GLN B 179 4.446 -10.577 -22.649 1.00 60.05 C
ANISOU 3482 CG GLN B 179 9441 6752 6622 -1309 1388 -831 C
ATOM 3483 CD GLN B 179 5.906 -10.478 -23.055 1.00 75.96 C
ANISOU 3483 CD GLN B 179 11343 8911 8609 -1179 1320 -928 C
ATOM 3484 OE1 GLN B 179 6.388 -9.414 -23.453 1.00 80.74 O
ANISOU 3484 OE1 GLN B 179 11801 9657 9219 -1217 1273 -940 O
ATOM 3485 NE2 GLN B 179 6.607 -11.605 -23.005 1.00 78.13 N
ANISOU 3485 NE2 GLN B 179 11694 9136 8856 -1033 1335 -1003 N
ATOM 3486 N ALA B 180 1.685 -11.705 -24.806 1.00 60.90 N
ANISOU 3486 N ALA B 180 9730 6722 6689 -1715 1371 -755 N
ATOM 3487 CA ALA B 180 1.104 -13.044 -24.901 1.00 55.27 C
ANISOU 3487 CA ALA B 180 9154 5847 5998 -1722 1342 -749 C
ATOM 3488 C ALA B 180 1.209 -13.599 -26.312 1.00 66.01 C
ANISOU 3488 C ALA B 180 10576 7218 7287 -1830 1257 -807 C
ATOM 3489 O ALA B 180 1.347 -14.816 -26.497 1.00 73.78 O
ANISOU 3489 O ALA B 180 11704 8067 8263 -1798 1258 -864 O
ATOM 3490 CB ALA B 180 -0.355 -13.017 -24.458 1.00 36.15 C
ANISOU 3490 CB ALA B 180 6657 3357 3720 -1755 1278 -619 C
ATOM 3491 N ALA B 181 1.111 -12.729 -27.315 1.00 64.31 N
ANISOU 3491 N ALA B 181 10271 7151 7012 -1958 1183 -794 N
ATOM 3492 CA ALA B 181 1.167 -13.189 -28.696 1.00 59.80 C
ANISOU 3492 CA ALA B 181 9791 6592 6339 -2085 1112 -841 C
ATOM 3493 C ALA B 181 2.540 -13.754 -29.038 1.00 56.39 C
ANISOU 3493 C ALA B 181 9419 6148 5859 -1974 1205 -986 C
ATOM 3494 O ALA B 181 2.645 -14.774 -29.728 1.00 60.86 O
ANISOU 3494 O ALA B 181 10134 6618 6370 -1991 1198 -1069 O
ATOM 3495 CB ALA B 181 0.794 -12.045 -29.633 1.00 58.83 C
ANISOU 3495 CB ALA B 181 9562 6637 6155 -2234 1004 -774 C
ATOM 3496 N VAL B 182 3.607 -13.115 -28.561 1.00 59.27 N
ANISOU 3496 N VAL B 182 9646 6608 6264 -1832 1269 -1026 N
ATOM 3497 CA VAL B 182 4.929 -13.584 -28.937 1.00 54.60 C
ANISOU 3497 CA VAL B 182 9050 6041 5655 -1674 1320 -1168 C
ATOM 3498 C VAL B 182 5.301 -14.878 -28.245 1.00 50.51 C
ANISOU 3498 C VAL B 182 8643 5366 5182 -1478 1373 -1242 C
ATOM 3499 O VAL B 182 6.187 -15.592 -28.727 1.00 58.82 O
ANISOU 3499 O VAL B 182 9745 6395 6210 -1358 1429 -1374 O
ATOM 3500 CB VAL B 182 5.978 -12.512 -28.657 1.00 62.90 C
ANISOU 3500 CB VAL B 182 9899 7261 6739 -1568 1332 -1183 C
ATOM 3501 CG1 VAL B 182 5.605 -11.276 -29.417 1.00 68.13 C
ANISOU 3501 CG1 VAL B 182 10469 8055 7362 -1776 1284 -1109 C
ATOM 3502 CG2 VAL B 182 6.036 -12.259 -27.187 1.00 60.44 C
ANISOU 3502 CG2 VAL B 182 9520 6930 6513 -1429 1333 -1127 C
ATOM 3503 N MET B 183 4.645 -15.217 -27.139 1.00 48.03 N
ANISOU 3503 N MET B 183 8382 4934 4933 -1443 1372 -1163 N
ATOM 3504 CA MET B 183 4.973 -16.464 -26.463 1.00 60.07 C
ANISOU 3504 CA MET B 183 10031 6290 6504 -1268 1419 -1217 C
ATOM 3505 C MET B 183 4.697 -17.652 -27.381 1.00 75.09 C
ANISOU 3505 C MET B 183 12114 8045 8372 -1329 1416 -1301 C
ATOM 3506 O MET B 183 3.633 -17.741 -27.999 1.00 87.06 O
ANISOU 3506 O MET B 183 13713 9517 9848 -1537 1347 -1248 O
ATOM 3507 CB MET B 183 4.167 -16.598 -25.161 1.00 67.09 C
ANISOU 3507 CB MET B 183 10976 7063 7452 -1257 1425 -1095 C
ATOM 3508 CG MET B 183 4.258 -15.380 -24.219 1.00 56.94 C
ANISOU 3508 CG MET B 183 9550 5903 6180 -1225 1435 -1013 C
ATOM 3509 SD MET B 183 5.951 -14.864 -23.867 1.00 43.00 S
ANISOU 3509 SD MET B 183 7631 4300 4406 -1001 1433 -1101 S
ATOM 3510 CE MET B 183 6.455 -16.107 -22.680 1.00 40.68 C
ANISOU 3510 CE MET B 183 7495 3826 4135 -775 1482 -1120 C
ATOM 3511 N GLU B 184 5.676 -18.551 -27.487 1.00 77.54 N
ANISOU 3511 N GLU B 184 12484 8277 8699 -1144 1486 -1435 N
ATOM 3512 CA GLU B 184 5.510 -19.808 -28.203 1.00 85.14 C
ANISOU 3512 CA GLU B 184 13644 9060 9646 -1166 1501 -1536 C
ATOM 3513 C GLU B 184 6.223 -20.901 -27.414 1.00 89.73 C
ANISOU 3513 C GLU B 184 14297 9464 10331 -918 1576 -1604 C
ATOM 3514 O GLU B 184 7.365 -20.707 -26.985 1.00 81.27 O
ANISOU 3514 O GLU B 184 13114 8463 9300 -709 1647 -1657 O
ATOM 3515 CB GLU B 184 6.087 -19.707 -29.624 1.00 89.45 C
ANISOU 3515 CB GLU B 184 14207 9699 10082 -1220 1542 -1671 C
ATOM 3516 CG GLU B 184 5.339 -18.763 -30.577 1.00 94.29 C
ANISOU 3516 CG GLU B 184 14796 10451 10577 -1491 1457 -1599 C
ATOM 3517 CD GLU B 184 3.972 -19.264 -30.995 1.00101.64 C
ANISOU 3517 CD GLU B 184 15900 11255 11463 -1723 1344 -1532 C
ATOM 3518 OE1 GLU B 184 3.720 -20.486 -30.894 1.00114.34 O
ANISOU 3518 OE1 GLU B 184 17680 12656 13108 -1689 1342 -1588 O
ATOM 3519 OE2 GLU B 184 3.155 -18.426 -31.441 1.00 93.61 O
ANISOU 3519 OE2 GLU B 184 14840 10344 10384 -1940 1244 -1418 O
ATOM 3520 N CYS B 185 5.574 -22.056 -27.253 1.00 92.49 N
ANISOU 3520 N CYS B 185 14831 9576 10734 -941 1554 -1597 N
ATOM 3521 CA CYS B 185 6.170 -23.191 -26.553 1.00 83.06 C
ANISOU 3521 CA CYS B 185 13728 8170 9661 -715 1618 -1647 C
ATOM 3522 C CYS B 185 6.797 -24.177 -27.530 1.00 81.45 C
ANISOU 3522 C CYS B 185 13643 7841 9462 -636 1697 -1840 C
ATOM 3523 O CYS B 185 6.155 -24.603 -28.488 1.00 84.10 O
ANISOU 3523 O CYS B 185 14122 8109 9724 -813 1657 -1897 O
ATOM 3524 CB CYS B 185 5.134 -23.906 -25.685 1.00 82.03 C
ANISOU 3524 CB CYS B 185 13724 7827 9616 -770 1550 -1510 C
ATOM 3525 SG CYS B 185 5.824 -25.041 -24.458 1.00 86.72 S
ANISOU 3525 SG CYS B 185 14404 8165 10379 -484 1609 -1488 S
ATOM 3526 N SER B 186 8.045 -24.545 -27.286 1.00 76.58 N
ANISOU 3526 N SER B 186 12977 7185 8934 -372 1814 -1941 N
ATOM 3527 CA SER B 186 8.728 -25.474 -28.173 1.00 84.82 C
ANISOU 3527 CA SER B 186 14127 8098 10002 -266 1930 -2136 C
ATOM 3528 C SER B 186 9.691 -26.291 -27.340 1.00 90.06 C
ANISOU 3528 C SER B 186 14777 8577 10866 47 2026 -2166 C
ATOM 3529 O SER B 186 10.274 -25.767 -26.397 1.00 87.98 O
ANISOU 3529 O SER B 186 14364 8392 10673 200 2034 -2078 O
ATOM 3530 CB SER B 186 9.467 -24.760 -29.304 1.00 97.81 C
ANISOU 3530 CB SER B 186 15680 9965 11520 -285 2023 -2264 C
ATOM 3531 OG SER B 186 8.555 -24.006 -30.086 1.00105.02 O
ANISOU 3531 OG SER B 186 16617 11027 12261 -577 1921 -2212 O
ATOM 3532 N SER B 187 9.871 -27.557 -27.707 1.00 97.82 N
ANISOU 3532 N SER B 187 15921 9300 11946 142 2095 -2287 N
ATOM 3533 CA SER B 187 10.850 -28.448 -27.092 1.00 95.26 C
ANISOU 3533 CA SER B 187 15584 8759 11852 459 2201 -2324 C
ATOM 3534 C SER B 187 12.186 -28.335 -27.823 1.00 88.36 C
ANISOU 3534 C SER B 187 14592 7973 11007 656 2398 -2498 C
ATOM 3535 O SER B 187 12.249 -27.844 -28.954 1.00 82.46 O
ANISOU 3535 O SER B 187 13846 7402 10083 524 2458 -2617 O
ATOM 3536 CB SER B 187 10.356 -29.902 -27.099 1.00 98.72 C
ANISOU 3536 CB SER B 187 16248 8846 12415 471 2178 -2360 C
ATOM 3537 OG SER B 187 9.808 -30.246 -28.360 1.00105.48 O
ANISOU 3537 OG SER B 187 17279 9673 13125 268 2184 -2512 O
ATOM 3538 N VAL B 188 13.261 -28.771 -27.145 1.00 88.14 N
ANISOU 3538 N VAL B 188 14454 7819 11217 978 2501 -2489 N
ATOM 3539 CA VAL B 188 14.599 -28.660 -27.724 1.00 93.83 C
ANISOU 3539 CA VAL B 188 15019 8619 12015 1198 2712 -2628 C
ATOM 3540 C VAL B 188 14.589 -29.225 -29.140 1.00110.44 C
ANISOU 3540 C VAL B 188 17289 10666 14007 1118 2844 -2851 C
ATOM 3541 O VAL B 188 15.103 -28.614 -30.083 1.00107.54 O
ANISOU 3541 O VAL B 188 16851 10508 13503 1081 2972 -2963 O
ATOM 3542 CB VAL B 188 15.631 -29.371 -26.831 1.00 84.93 C
ANISOU 3542 CB VAL B 188 13773 7270 11225 1571 2797 -2568 C
ATOM 3543 CG1 VAL B 188 15.809 -28.611 -25.538 1.00 87.67 C
ANISOU 3543 CG1 VAL B 188 13954 7714 11644 1654 2683 -2351 C
ATOM 3544 CG2 VAL B 188 15.179 -30.799 -26.580 1.00 81.07 C
ANISOU 3544 CG2 VAL B 188 13498 6405 10899 1631 2755 -2569 C
ATOM 3545 N LEU B 189 14.022 -30.409 -29.304 1.00118.16 N
ANISOU 3545 N LEU B 189 18504 11351 15041 1089 2820 -2915 N
ATOM 3546 CA LEU B 189 13.777 -30.988 -30.617 1.00115.62 C
ANISOU 3546 CA LEU B 189 18410 10944 14575 963 2912 -3126 C
ATOM 3547 C LEU B 189 12.270 -31.137 -30.757 1.00128.08 C
ANISOU 3547 C LEU B 189 20207 12467 15991 633 2699 -3067 C
ATOM 3548 O LEU B 189 11.678 -31.981 -30.075 1.00136.66 O
ANISOU 3548 O LEU B 189 21407 13299 17218 639 2587 -2990 O
ATOM 3549 CB LEU B 189 14.505 -32.327 -30.771 1.00112.91 C
ANISOU 3549 CB LEU B 189 18163 10273 14464 1232 3091 -3276 C
ATOM 3550 CG LEU B 189 16.037 -32.270 -30.719 1.00113.75 C
ANISOU 3550 CG LEU B 189 18033 10411 14776 1582 3332 -3329 C
ATOM 3551 CD1 LEU B 189 16.542 -33.206 -29.601 1.00118.51 C
ANISOU 3551 CD1 LEU B 189 18557 10710 15761 1898 3328 -3223 C
ATOM 3552 CD2 LEU B 189 16.657 -32.632 -32.036 1.00115.59 C
ANISOU 3552 CD2 LEU B 189 18371 10620 14929 1632 3594 -3582 C
ATOM 3553 N PRO B 190 11.620 -30.365 -31.639 1.00135.98 N
ANISOU 3553 N PRO B 190 21266 13684 16717 342 2634 -3086 N
ATOM 3554 CA PRO B 190 10.178 -30.106 -31.474 1.00137.51 C
ANISOU 3554 CA PRO B 190 21555 13902 16790 34 2398 -2939 C
ATOM 3555 C PRO B 190 9.303 -31.334 -31.403 1.00132.69 C
ANISOU 3555 C PRO B 190 21193 12970 16253 -55 2300 -2955 C
ATOM 3556 O PRO B 190 8.330 -31.344 -30.634 1.00140.59 O
ANISOU 3556 O PRO B 190 22201 13920 17299 -182 2120 -2772 O
ATOM 3557 CB PRO B 190 9.842 -29.246 -32.699 1.00139.14 C
ANISOU 3557 CB PRO B 190 21805 14348 16714 -226 2386 -2994 C
ATOM 3558 CG PRO B 190 11.117 -28.544 -33.011 1.00136.57 C
ANISOU 3558 CG PRO B 190 21287 14232 16371 -48 2572 -3071 C
ATOM 3559 CD PRO B 190 12.198 -29.558 -32.724 1.00138.83 C
ANISOU 3559 CD PRO B 190 21570 14296 16884 290 2768 -3200 C
ATOM 3560 N GLU B 191 9.614 -32.374 -32.147 1.00125.00 N
ANISOU 3560 N GLU B 191 20425 11769 15302 10 2419 -3163 N
ATOM 3561 CA GLU B 191 8.762 -33.563 -32.114 1.00112.19 C
ANISOU 3561 CA GLU B 191 19049 9822 13756 -92 2310 -3184 C
ATOM 3562 C GLU B 191 8.978 -34.401 -30.860 1.00104.32 C
ANISOU 3562 C GLU B 191 18000 8565 13072 143 2288 -3079 C
ATOM 3563 O GLU B 191 8.217 -35.342 -30.632 1.00101.72 O
ANISOU 3563 O GLU B 191 17840 7965 12842 57 2171 -3048 O
ATOM 3564 CB GLU B 191 8.967 -34.434 -33.359 1.00104.06 C
ANISOU 3564 CB GLU B 191 18295 8607 12635 -119 2440 -3457 C
ATOM 3565 CG GLU B 191 10.407 -34.582 -33.819 1.00105.24 C
ANISOU 3565 CG GLU B 191 18393 8757 12838 172 2729 -3656 C
ATOM 3566 CD GLU B 191 10.929 -33.344 -34.515 1.00119.72 C
ANISOU 3566 CD GLU B 191 20086 10952 14450 121 2833 -3683 C
ATOM 3567 OE1 GLU B 191 11.255 -32.358 -33.817 1.00123.17 O
ANISOU 3567 OE1 GLU B 191 20238 11630 14930 195 2803 -3519 O
ATOM 3568 OE2 GLU B 191 10.999 -33.351 -35.763 1.00128.96 O
ANISOU 3568 OE2 GLU B 191 21443 12159 15399 -3 2941 -3864 O
ATOM 3569 N LEU B 192 10.001 -34.092 -30.052 1.00101.88 N
ANISOU 3569 N LEU B 192 17461 8321 12929 431 2387 -3011 N
ATOM 3570 CA LEU B 192 10.182 -34.776 -28.773 1.00 99.61 C
ANISOU 3570 CA LEU B 192 17115 7799 12933 643 2339 -2860 C
ATOM 3571 C LEU B 192 9.041 -34.470 -27.820 1.00100.31 C
ANISOU 3571 C LEU B 192 17186 7918 13008 453 2118 -2602 C
ATOM 3572 O LEU B 192 8.782 -35.240 -26.882 1.00106.55 O
ANISOU 3572 O LEU B 192 18016 8463 14006 531 2033 -2460 O
ATOM 3573 CB LEU B 192 11.520 -34.373 -28.141 1.00100.12 C
ANISOU 3573 CB LEU B 192 16927 7954 13162 975 2474 -2818 C
ATOM 3574 CG LEU B 192 11.737 -34.540 -26.625 1.00100.75 C
ANISOU 3574 CG LEU B 192 16877 7913 13489 1173 2386 -2574 C
ATOM 3575 CD1 LEU B 192 12.008 -35.981 -26.223 1.00 98.83 C
ANISOU 3575 CD1 LEU B 192 16738 7259 13553 1384 2398 -2573 C
ATOM 3576 CD2 LEU B 192 12.892 -33.650 -26.222 1.00100.98 C
ANISOU 3576 CD2 LEU B 192 16636 8160 13573 1400 2489 -2526 C
ATOM 3577 N ALA B 193 8.379 -33.332 -28.030 1.00 92.28 N
ANISOU 3577 N ALA B 193 16101 7199 11761 212 2033 -2525 N
ATOM 3578 CA ALA B 193 7.283 -32.911 -27.175 1.00 94.50 C
ANISOU 3578 CA ALA B 193 16349 7539 12018 28 1853 -2281 C
ATOM 3579 C ALA B 193 6.113 -33.883 -27.237 1.00 99.88 C
ANISOU 3579 C ALA B 193 17232 7966 12753 -169 1712 -2237 C
ATOM 3580 O ALA B 193 5.309 -33.954 -26.295 1.00104.79 O
ANISOU 3580 O ALA B 193 17834 8527 13454 -250 1585 -2016 O
ATOM 3581 CB ALA B 193 6.845 -31.504 -27.590 1.00 90.13 C
ANISOU 3581 CB ALA B 193 15681 7343 11223 -186 1807 -2236 C
ATOM 3582 N ALA B 194 6.021 -34.650 -28.327 1.00 99.39 N
ANISOU 3582 N ALA B 194 17367 7745 12650 -248 1739 -2443 N
ATOM 3583 CA ALA B 194 5.005 -35.687 -28.429 1.00100.75 C
ANISOU 3583 CA ALA B 194 17739 7639 12901 -425 1602 -2422 C
ATOM 3584 C ALA B 194 5.169 -36.723 -27.330 1.00105.51 C
ANISOU 3584 C ALA B 194 18355 7933 13801 -232 1581 -2305 C
ATOM 3585 O ALA B 194 4.184 -37.350 -26.929 1.00124.72 O
ANISOU 3585 O ALA B 194 20869 10181 16339 -384 1430 -2167 O
ATOM 3586 CB ALA B 194 5.072 -36.365 -29.803 1.00 82.69 C
ANISOU 3586 CB ALA B 194 15691 5216 10513 -511 1657 -2696 C
ATOM 3587 N ARG B 195 6.394 -36.908 -26.827 1.00 93.99 N
ANISOU 3587 N ARG B 195 16800 6412 12498 99 1719 -2335 N
ATOM 3588 CA ARG B 195 6.673 -37.870 -25.769 1.00 90.90 C
ANISOU 3588 CA ARG B 195 16411 5721 12407 309 1694 -2200 C
ATOM 3589 C ARG B 195 6.704 -37.248 -24.384 1.00 81.00 C
ANISOU 3589 C ARG B 195 14977 4589 11210 396 1635 -1910 C
ATOM 3590 O ARG B 195 6.374 -37.928 -23.408 1.00 85.78 O
ANISOU 3590 O ARG B 195 15606 4980 12005 435 1538 -1704 O
ATOM 3591 CB ARG B 195 8.012 -38.570 -26.022 1.00 88.27 C
ANISOU 3591 CB ARG B 195 16084 5198 12259 641 1869 -2384 C
ATOM 3592 CG ARG B 195 8.348 -38.762 -27.476 1.00 89.65 C
ANISOU 3592 CG ARG B 195 16396 5369 12298 607 2009 -2706 C
ATOM 3593 CD ARG B 195 9.594 -39.615 -27.622 1.00 94.08 C
ANISOU 3593 CD ARG B 195 16965 5686 13094 953 2193 -2869 C
ATOM 3594 NE ARG B 195 9.520 -40.806 -26.786 1.00 96.82 N
ANISOU 3594 NE ARG B 195 17374 5647 13766 1088 2105 -2746 N
ATOM 3595 CZ ARG B 195 10.412 -41.791 -26.800 1.00110.38 C
ANISOU 3595 CZ ARG B 195 19122 7059 15756 1380 2222 -2851 C
ATOM 3596 NH1 ARG B 195 10.261 -42.838 -25.999 1.00114.20 N
ANISOU 3596 NH1 ARG B 195 19657 7191 16541 1479 2109 -2702 N
ATOM 3597 NH2 ARG B 195 11.452 -41.734 -27.618 1.00103.80 N
ANISOU 3597 NH2 ARG B 195 18265 6269 14907 1575 2455 -3091 N
ATOM 3598 N THR B 196 7.102 -35.983 -24.273 1.00 82.50 N
ANISOU 3598 N THR B 196 14999 5111 11235 423 1691 -1884 N
ATOM 3599 CA THR B 196 7.253 -35.384 -22.958 1.00 73.61 C
ANISOU 3599 CA THR B 196 13733 4089 10148 525 1649 -1629 C
ATOM 3600 C THR B 196 7.389 -33.873 -23.083 1.00 92.08 C
ANISOU 3600 C THR B 196 15919 6815 12254 456 1688 -1634 C
ATOM 3601 O THR B 196 7.941 -33.371 -24.064 1.00 94.24 O
ANISOU 3601 O THR B 196 16141 7258 12410 465 1791 -1839 O
ATOM 3602 CB THR B 196 8.477 -35.966 -22.231 1.00 88.38 C
ANISOU 3602 CB THR B 196 15538 5769 12275 887 1713 -1577 C
ATOM 3603 OG1 THR B 196 8.505 -35.491 -20.879 1.00 92.83 O
ANISOU 3603 OG1 THR B 196 16015 6398 12860 961 1638 -1293 O
ATOM 3604 CG2 THR B 196 9.776 -35.580 -22.930 1.00 88.48 C
ANISOU 3604 CG2 THR B 196 15429 5902 12289 1103 1887 -1792 C
ATOM 3605 N ARG B 197 6.883 -33.161 -22.081 1.00 80.88 N
ANISOU 3605 N ARG B 197 14434 5529 10769 385 1610 -1403 N
ATOM 3606 CA ARG B 197 7.193 -31.756 -21.876 1.00 73.21 C
ANISOU 3606 CA ARG B 197 13310 4880 9627 382 1645 -1374 C
ATOM 3607 C ARG B 197 8.475 -31.567 -21.082 1.00 67.36 C
ANISOU 3607 C ARG B 197 12462 4136 8995 695 1707 -1319 C
ATOM 3608 O ARG B 197 8.832 -30.428 -20.777 1.00 64.81 O
ANISOU 3608 O ARG B 197 12019 4056 8550 718 1726 -1285 O
ATOM 3609 CB ARG B 197 6.036 -31.058 -21.162 1.00 72.18 C
ANISOU 3609 CB ARG B 197 13171 4880 9374 163 1549 -1160 C
ATOM 3610 CG ARG B 197 4.711 -31.169 -21.881 1.00 83.06 C
ANISOU 3610 CG ARG B 197 14613 6265 10680 -145 1468 -1172 C
ATOM 3611 CD ARG B 197 3.573 -30.803 -20.954 1.00 84.69 C
ANISOU 3611 CD ARG B 197 14798 6520 10862 -308 1389 -917 C
ATOM 3612 NE ARG B 197 2.289 -30.735 -21.645 1.00 88.88 N
ANISOU 3612 NE ARG B 197 15333 7089 11348 -602 1301 -905 N
ATOM 3613 CZ ARG B 197 1.145 -30.423 -21.045 1.00 91.29 C
ANISOU 3613 CZ ARG B 197 15578 7447 11662 -771 1237 -694 C
ATOM 3614 NH1 ARG B 197 1.134 -30.154 -19.747 1.00 92.02 N
ANISOU 3614 NH1 ARG B 197 15629 7565 11768 -683 1272 -491 N
ATOM 3615 NH2 ARG B 197 0.013 -30.377 -21.735 1.00 95.21 N
ANISOU 3615 NH2 ARG B 197 16045 7971 12159 -1024 1140 -676 N
ATOM 3616 N ALA B 198 9.183 -32.656 -20.763 1.00 84.64 N
ANISOU 3616 N ALA B 198 14686 6043 11428 940 1727 -1302 N
ATOM 3617 CA ALA B 198 10.351 -32.563 -19.893 1.00 87.44 C
ANISOU 3617 CA ALA B 198 14933 6358 11933 1251 1749 -1186 C
ATOM 3618 C ALA B 198 11.447 -31.712 -20.518 1.00 87.67 C
ANISOU 3618 C ALA B 198 14777 6612 11920 1387 1879 -1362 C
ATOM 3619 O ALA B 198 12.328 -31.210 -19.810 1.00 76.00 O
ANISOU 3619 O ALA B 198 13173 5194 10510 1601 1882 -1252 O
ATOM 3620 CB ALA B 198 10.896 -33.953 -19.594 1.00 86.24 C
ANISOU 3620 CB ALA B 198 14826 5846 12095 1489 1740 -1135 C
ATOM 3621 N PHE B 199 11.373 -31.474 -21.825 1.00 93.71 N
ANISOU 3621 N PHE B 199 15525 7519 12559 1252 1974 -1611 N
ATOM 3622 CA PHE B 199 12.408 -30.737 -22.539 1.00 89.21 C
ANISOU 3622 CA PHE B 199 14774 7170 11952 1363 2114 -1779 C
ATOM 3623 C PHE B 199 11.800 -29.592 -23.336 1.00 94.10 C
ANISOU 3623 C PHE B 199 15360 8119 12273 1072 2106 -1873 C
ATOM 3624 O PHE B 199 12.321 -29.203 -24.384 1.00104.07 O
ANISOU 3624 O PHE B 199 16538 9547 13456 1060 2219 -2056 O
ATOM 3625 CB PHE B 199 13.213 -31.661 -23.449 1.00 80.69 C
ANISOU 3625 CB PHE B 199 13691 5926 11043 1542 2270 -1987 C
ATOM 3626 CG PHE B 199 13.709 -32.901 -22.771 1.00 83.93 C
ANISOU 3626 CG PHE B 199 14132 5977 11780 1814 2263 -1891 C
ATOM 3627 CD1 PHE B 199 14.908 -32.897 -22.080 1.00 86.58 C
ANISOU 3627 CD1 PHE B 199 14272 6259 12367 2150 2305 -1775 C
ATOM 3628 CD2 PHE B 199 12.987 -34.080 -22.838 1.00 89.32 C
ANISOU 3628 CD2 PHE B 199 15022 6367 12546 1738 2200 -1897 C
ATOM 3629 CE1 PHE B 199 15.379 -34.050 -21.462 1.00 88.73 C
ANISOU 3629 CE1 PHE B 199 14548 6193 12973 2408 2273 -1651 C
ATOM 3630 CE2 PHE B 199 13.451 -35.233 -22.224 1.00 96.84 C
ANISOU 3630 CE2 PHE B 199 15994 6979 13821 1987 2178 -1795 C
ATOM 3631 CZ PHE B 199 14.648 -35.216 -21.536 1.00 96.63 C
ANISOU 3631 CZ PHE B 199 15765 6903 14046 2324 2210 -1665 C
ATOM 3632 N SER B 200 10.671 -29.079 -22.858 1.00 82.69 N
ANISOU 3632 N SER B 200 13982 6760 10676 835 1972 -1729 N
ATOM 3633 CA SER B 200 9.986 -27.959 -23.471 1.00 77.29 C
ANISOU 3633 CA SER B 200 13248 6370 9748 561 1934 -1760 C
ATOM 3634 C SER B 200 10.472 -26.668 -22.827 1.00 78.63 C
ANISOU 3634 C SER B 200 13247 6790 9839 609 1926 -1679 C
ATOM 3635 O SER B 200 10.919 -26.653 -21.679 1.00 73.30 O
ANISOU 3635 O SER B 200 12559 6036 9254 791 1905 -1543 O
ATOM 3636 CB SER B 200 8.468 -28.093 -23.305 1.00 71.80 C
ANISOU 3636 CB SER B 200 12691 5620 8971 287 1805 -1637 C
ATOM 3637 OG SER B 200 7.924 -28.988 -24.261 1.00 78.47 O
ANISOU 3637 OG SER B 200 13680 6312 9823 163 1797 -1752 O
ATOM 3638 N VAL B 201 10.376 -25.576 -23.575 1.00 77.09 N
ANISOU 3638 N VAL B 201 12933 6885 9472 442 1930 -1749 N
ATOM 3639 CA VAL B 201 10.659 -24.248 -23.045 1.00 72.21 C
ANISOU 3639 CA VAL B 201 12158 6521 8757 431 1901 -1677 C
ATOM 3640 C VAL B 201 9.604 -23.285 -23.564 1.00 77.16 C
ANISOU 3640 C VAL B 201 12750 7363 9204 123 1817 -1640 C
ATOM 3641 O VAL B 201 9.144 -23.407 -24.705 1.00 73.73 O
ANISOU 3641 O VAL B 201 12349 6959 8705 -40 1816 -1724 O
ATOM 3642 CB VAL B 201 12.073 -23.774 -23.431 1.00 69.55 C
ANISOU 3642 CB VAL B 201 11629 6334 8464 620 2015 -1798 C
ATOM 3643 CG1 VAL B 201 13.094 -24.884 -23.169 1.00 70.92 C
ANISOU 3643 CG1 VAL B 201 11816 6255 8877 942 2124 -1840 C
ATOM 3644 CG2 VAL B 201 12.103 -23.359 -24.887 1.00 79.00 C
ANISOU 3644 CG2 VAL B 201 12752 7720 9543 467 2067 -1945 C
ATOM 3645 N CYS B 202 9.231 -22.323 -22.725 1.00 80.68 N
ANISOU 3645 N CYS B 202 13139 7941 9574 51 1750 -1507 N
ATOM 3646 CA CYS B 202 8.256 -21.297 -23.072 1.00 81.24 C
ANISOU 3646 CA CYS B 202 13143 8202 9522 -210 1677 -1441 C
ATOM 3647 C CYS B 202 8.995 -19.980 -23.248 1.00 78.17 C
ANISOU 3647 C CYS B 202 12540 8098 9063 -203 1675 -1473 C
ATOM 3648 O CYS B 202 9.646 -19.509 -22.311 1.00 70.65 O
ANISOU 3648 O CYS B 202 11531 7205 8109 -71 1674 -1436 O
ATOM 3649 CB CYS B 202 7.170 -21.185 -21.998 1.00 78.85 C
ANISOU 3649 CB CYS B 202 12937 7819 9204 -307 1624 -1261 C
ATOM 3650 SG CYS B 202 5.961 -19.872 -22.289 1.00 58.72 S
ANISOU 3650 SG CYS B 202 10284 5468 6558 -594 1568 -1162 S
ATOM 3651 N ASP B 203 8.916 -19.397 -24.444 1.00 80.91 N
ANISOU 3651 N ASP B 203 12788 8608 9346 -348 1666 -1535 N
ATOM 3652 CA ASP B 203 9.652 -18.159 -24.673 1.00 65.84 C
ANISOU 3652 CA ASP B 203 10671 6957 7386 -346 1659 -1556 C
ATOM 3653 C ASP B 203 9.032 -17.387 -25.829 1.00 71.32 C
ANISOU 3653 C ASP B 203 11303 7793 8001 -579 1611 -1544 C
ATOM 3654 O ASP B 203 8.225 -17.910 -26.602 1.00 94.34 O
ANISOU 3654 O ASP B 203 14345 10611 10888 -724 1600 -1553 O
ATOM 3655 CB ASP B 203 11.138 -18.437 -24.938 1.00 60.42 C
ANISOU 3655 CB ASP B 203 9905 6302 6748 -124 1772 -1697 C
ATOM 3656 CG ASP B 203 12.048 -17.315 -24.463 1.00 74.10 C
ANISOU 3656 CG ASP B 203 11446 8246 8462 -51 1768 -1686 C
ATOM 3657 OD1 ASP B 203 12.338 -17.221 -23.247 1.00 82.64 O
ANISOU 3657 OD1 ASP B 203 12544 9291 9566 66 1748 -1629 O
ATOM 3658 OD2 ASP B 203 12.476 -16.524 -25.330 1.00 82.83 O
ANISOU 3658 OD2 ASP B 203 12409 9545 9517 -121 1786 -1731 O
ATOM 3659 N GLU B 204 9.420 -16.116 -25.916 1.00 58.22 N
ANISOU 3659 N GLU B 204 9463 6352 6307 -620 1576 -1515 N
ATOM 3660 CA GLU B 204 9.006 -15.259 -27.019 1.00 53.85 C
ANISOU 3660 CA GLU B 204 8841 5930 5688 -825 1536 -1493 C
ATOM 3661 C GLU B 204 9.586 -15.779 -28.326 1.00 60.23 C
ANISOU 3661 C GLU B 204 9702 6742 6441 -820 1622 -1631 C
ATOM 3662 O GLU B 204 10.758 -16.159 -28.391 1.00 63.44 O
ANISOU 3662 O GLU B 204 10070 7166 6868 -630 1727 -1746 O
ATOM 3663 CB GLU B 204 9.472 -13.824 -26.776 1.00 58.62 C
ANISOU 3663 CB GLU B 204 9244 6743 6287 -843 1490 -1440 C
ATOM 3664 CG GLU B 204 8.905 -13.199 -25.506 1.00 61.20 C
ANISOU 3664 CG GLU B 204 9534 7068 6649 -856 1418 -1316 C
ATOM 3665 CD GLU B 204 9.624 -11.938 -25.110 1.00 63.78 C
ANISOU 3665 CD GLU B 204 9685 7578 6972 -828 1376 -1295 C
ATOM 3666 OE1 GLU B 204 10.214 -11.269 -25.988 1.00 64.57 O
ANISOU 3666 OE1 GLU B 204 9672 7816 7046 -878 1384 -1335 O
ATOM 3667 OE2 GLU B 204 9.613 -11.613 -23.904 1.00 59.40 O
ANISOU 3667 OE2 GLU B 204 9124 7021 6425 -765 1340 -1239 O
ATOM 3668 N ARG B 205 8.756 -15.817 -29.363 1.00 71.51 N
ANISOU 3668 N ARG B 205 11232 8145 7794 -1032 1592 -1622 N
ATOM 3669 CA ARG B 205 9.167 -16.284 -30.681 1.00 81.90 C
ANISOU 3669 CA ARG B 205 12644 9456 9017 -1066 1675 -1753 C
ATOM 3670 C ARG B 205 9.323 -15.045 -31.553 1.00 92.13 C
ANISOU 3670 C ARG B 205 13826 10951 10229 -1222 1654 -1719 C
ATOM 3671 O ARG B 205 8.340 -14.518 -32.071 1.00147.60 O
ANISOU 3671 O ARG B 205 20890 17996 17196 -1463 1564 -1627 O
ATOM 3672 CB ARG B 205 8.122 -17.259 -31.209 1.00 82.24 C
ANISOU 3672 CB ARG B 205 12924 9314 9011 -1213 1643 -1767 C
ATOM 3673 CG ARG B 205 8.442 -18.027 -32.489 1.00 84.53 C
ANISOU 3673 CG ARG B 205 13389 9541 9189 -1246 1735 -1925 C
ATOM 3674 CD ARG B 205 7.629 -19.331 -32.458 1.00 98.94 C
ANISOU 3674 CD ARG B 205 15451 11120 11024 -1289 1706 -1958 C
ATOM 3675 NE ARG B 205 7.750 -20.193 -33.629 1.00121.89 N
ANISOU 3675 NE ARG B 205 18577 13921 13813 -1343 1780 -2117 N
ATOM 3676 CZ ARG B 205 7.198 -21.401 -33.699 1.00133.08 C
ANISOU 3676 CZ ARG B 205 20216 15109 15238 -1369 1763 -2176 C
ATOM 3677 NH1 ARG B 205 6.508 -21.860 -32.667 1.00127.44 N
ANISOU 3677 NH1 ARG B 205 19516 14257 14648 -1344 1677 -2077 N
ATOM 3678 NH2 ARG B 205 7.324 -22.148 -34.788 1.00140.43 N
ANISOU 3678 NH2 ARG B 205 21368 15940 16048 -1427 1834 -2335 N
ATOM 3679 N TRP B 206 10.558 -14.576 -31.719 1.00 68.18 N
ANISOU 3679 N TRP B 206 10653 8060 7191 -1093 1743 -1787 N
ATOM 3680 CA TRP B 206 10.824 -13.363 -32.485 1.00 71.04 C
ANISOU 3680 CA TRP B 206 10901 8610 7483 -1233 1732 -1751 C
ATOM 3681 C TRP B 206 11.271 -13.705 -33.899 1.00 86.37 C
ANISOU 3681 C TRP B 206 12959 10571 9286 -1292 1854 -1875 C
ATOM 3682 O TRP B 206 12.190 -14.507 -34.092 1.00102.31 O
ANISOU 3682 O TRP B 206 15021 12552 11301 -1104 2014 -2016 O
ATOM 3683 CB TRP B 206 11.875 -12.496 -31.789 1.00 78.15 C
ANISOU 3683 CB TRP B 206 11574 9669 8452 -1089 1755 -1733 C
ATOM 3684 CG TRP B 206 11.378 -11.854 -30.524 1.00 80.16 C
ANISOU 3684 CG TRP B 206 11726 9930 8802 -1087 1625 -1605 C
ATOM 3685 CD1 TRP B 206 11.710 -12.192 -29.244 1.00 72.83 C
ANISOU 3685 CD1 TRP B 206 10760 8955 7956 -897 1620 -1602 C
ATOM 3686 CD2 TRP B 206 10.427 -10.786 -30.422 1.00 77.45 C
ANISOU 3686 CD2 TRP B 206 11325 9629 8473 -1289 1497 -1468 C
ATOM 3687 NE1 TRP B 206 11.047 -11.384 -28.353 1.00 62.10 N
ANISOU 3687 NE1 TRP B 206 9337 7615 6643 -968 1500 -1477 N
ATOM 3688 CE2 TRP B 206 10.250 -10.515 -29.050 1.00 67.59 C
ANISOU 3688 CE2 TRP B 206 10011 8359 7313 -1199 1432 -1396 C
ATOM 3689 CE3 TRP B 206 9.717 -10.027 -31.357 1.00 77.32 C
ANISOU 3689 CE3 TRP B 206 11317 9660 8400 -1543 1443 -1402 C
ATOM 3690 CZ2 TRP B 206 9.391 -9.517 -28.590 1.00 68.81 C
ANISOU 3690 CZ2 TRP B 206 10104 8530 7512 -1337 1337 -1271 C
ATOM 3691 CZ3 TRP B 206 8.864 -9.035 -30.898 1.00 71.50 C
ANISOU 3691 CZ3 TRP B 206 10505 8942 7720 -1685 1342 -1269 C
ATOM 3692 CH2 TRP B 206 8.709 -8.790 -29.528 1.00 68.98 C
ANISOU 3692 CH2 TRP B 206 10118 8593 7500 -1573 1301 -1212 C
ATOM 3693 N ALA B 207 10.604 -13.104 -34.885 1.00 85.64 N
ANISOU 3693 N ALA B 207 12931 10529 9078 -1558 1790 -1820 N
ATOM 3694 CA ALA B 207 10.893 -13.413 -36.280 1.00 82.40 C
ANISOU 3694 CA ALA B 207 12679 10131 8497 -1657 1898 -1932 C
ATOM 3695 C ALA B 207 12.238 -12.877 -36.768 1.00 89.66 C
ANISOU 3695 C ALA B 207 13473 11219 9374 -1555 2055 -2008 C
ATOM 3696 O ALA B 207 12.771 -13.409 -37.748 1.00101.25 O
ANISOU 3696 O ALA B 207 15077 12679 10714 -1540 2215 -2143 O
ATOM 3697 CB ALA B 207 9.770 -12.882 -37.170 1.00 75.85 C
ANISOU 3697 CB ALA B 207 11965 9313 7541 -1996 1769 -1833 C
ATOM 3698 N ASP B 208 12.808 -11.857 -36.122 1.00 88.85 N
ANISOU 3698 N ASP B 208 13127 11265 9368 -1488 2029 -1929 N
ATOM 3699 CA ASP B 208 14.015 -11.223 -36.649 1.00 91.57 C
ANISOU 3699 CA ASP B 208 13340 11786 9667 -1435 2175 -1975 C
ATOM 3700 C ASP B 208 14.839 -10.632 -35.512 1.00 77.54 C
ANISOU 3700 C ASP B 208 11305 10113 8042 -1254 2178 -1925 C
ATOM 3701 O ASP B 208 14.374 -10.512 -34.378 1.00 66.15 O
ANISOU 3701 O ASP B 208 9798 8620 6716 -1211 2041 -1846 O
ATOM 3702 CB ASP B 208 13.662 -10.153 -37.687 1.00100.97 C
ANISOU 3702 CB ASP B 208 14541 13096 10726 -1725 2112 -1903 C
ATOM 3703 CG ASP B 208 12.828 -9.036 -37.108 1.00 94.79 C
ANISOU 3703 CG ASP B 208 13632 12354 10030 -1896 1895 -1734 C
ATOM 3704 OD1 ASP B 208 11.588 -9.045 -37.271 1.00 96.41 O
ANISOU 3704 OD1 ASP B 208 13952 12469 10212 -2096 1755 -1654 O
ATOM 3705 OD2 ASP B 208 13.425 -8.157 -36.458 1.00 90.29 O
ANISOU 3705 OD2 ASP B 208 12846 11904 9558 -1829 1875 -1680 O
ATOM 3706 N ASP B 209 16.098 -10.308 -35.824 1.00 84.34 N
ANISOU 3706 N ASP B 209 12029 11122 8896 -1147 2355 -1976 N
ATOM 3707 CA ASP B 209 17.018 -9.821 -34.802 1.00 95.54 C
ANISOU 3707 CA ASP B 209 13199 12647 10454 -981 2386 -1939 C
ATOM 3708 C ASP B 209 16.522 -8.516 -34.181 1.00 94.22 C
ANISOU 3708 C ASP B 209 12900 12568 10333 -1148 2173 -1797 C
ATOM 3709 O ASP B 209 16.759 -8.259 -32.995 1.00 90.93 O
ANISOU 3709 O ASP B 209 12349 12171 10029 -1047 2112 -1758 O
ATOM 3710 CB ASP B 209 18.402 -9.626 -35.421 1.00106.07 C
ANISOU 3710 CB ASP B 209 14386 14139 11776 -878 2635 -1996 C
ATOM 3711 CG ASP B 209 18.835 -10.806 -36.281 1.00116.53 C
ANISOU 3711 CG ASP B 209 15864 15378 13034 -744 2873 -2146 C
ATOM 3712 OD1 ASP B 209 18.362 -11.941 -36.061 1.00119.48 O
ANISOU 3712 OD1 ASP B 209 16411 15559 13425 -650 2865 -2226 O
ATOM 3713 OD2 ASP B 209 19.624 -10.574 -37.231 1.00123.68 O
ANISOU 3713 OD2 ASP B 209 16725 16406 13862 -747 3074 -2185 O
ATOM 3714 N LEU B 210 15.846 -7.675 -34.966 1.00 90.32 N
ANISOU 3714 N LEU B 210 12445 12122 9751 -1408 2066 -1728 N
ATOM 3715 CA LEU B 210 15.541 -6.321 -34.522 1.00 74.42 C
ANISOU 3715 CA LEU B 210 10284 10201 7790 -1568 1898 -1607 C
ATOM 3716 C LEU B 210 14.259 -6.196 -33.704 1.00 74.10 C
ANISOU 3716 C LEU B 210 10297 10032 7824 -1645 1699 -1518 C
ATOM 3717 O LEU B 210 14.215 -5.407 -32.757 1.00 74.09 O
ANISOU 3717 O LEU B 210 10169 10069 7913 -1650 1596 -1450 O
ATOM 3718 CB LEU B 210 15.433 -5.382 -35.717 1.00 74.37 C
ANISOU 3718 CB LEU B 210 10276 10308 7673 -1818 1878 -1564 C
ATOM 3719 CG LEU B 210 14.912 -4.022 -35.271 1.00 60.57 C
ANISOU 3719 CG LEU B 210 8402 8621 5991 -2001 1684 -1443 C
ATOM 3720 CD1 LEU B 210 15.863 -3.344 -34.287 1.00 68.25 C
ANISOU 3720 CD1 LEU B 210 9152 9716 7065 -1890 1690 -1428 C
ATOM 3721 CD2 LEU B 210 14.637 -3.160 -36.481 1.00 38.10 C
ANISOU 3721 CD2 LEU B 210 5582 5865 3030 -2271 1637 -1392 C
ATOM 3722 N ALA B 211 13.218 -6.962 -34.027 1.00 77.28 N
ANISOU 3722 N ALA B 211 10888 10284 8191 -1711 1657 -1516 N
ATOM 3723 CA ALA B 211 11.923 -6.772 -33.371 1.00 68.36 C
ANISOU 3723 CA ALA B 211 9795 9044 7135 -1812 1500 -1408 C
ATOM 3724 C ALA B 211 11.993 -6.839 -31.854 1.00 59.87 C
ANISOU 3724 C ALA B 211 8642 7924 6183 -1629 1455 -1382 C
ATOM 3725 O ALA B 211 11.461 -5.932 -31.194 1.00 46.18 O
ANISOU 3725 O ALA B 211 6828 6199 4520 -1711 1348 -1287 O
ATOM 3726 CB ALA B 211 10.928 -7.809 -33.897 1.00 74.46 C
ANISOU 3726 CB ALA B 211 10782 9663 7845 -1889 1495 -1419 C
ATOM 3727 N PRO B 212 12.612 -7.847 -31.243 1.00 68.37 N
ANISOU 3727 N PRO B 212 9749 8947 7282 -1393 1536 -1462 N
ATOM 3728 CA PRO B 212 12.685 -7.872 -29.777 1.00 56.42 C
ANISOU 3728 CA PRO B 212 8183 7397 5856 -1243 1483 -1432 C
ATOM 3729 C PRO B 212 13.381 -6.650 -29.196 1.00 50.02 C
ANISOU 3729 C PRO B 212 7194 6736 5075 -1257 1444 -1402 C
ATOM 3730 O PRO B 212 13.045 -6.211 -28.088 1.00 47.75 O
ANISOU 3730 O PRO B 212 6883 6422 4838 -1240 1352 -1342 O
ATOM 3731 CB PRO B 212 13.447 -9.166 -29.478 1.00 71.26 C
ANISOU 3731 CB PRO B 212 10124 9212 7738 -1004 1605 -1543 C
ATOM 3732 CG PRO B 212 14.132 -9.520 -30.775 1.00 78.52 C
ANISOU 3732 CG PRO B 212 11065 10186 8584 -1004 1755 -1642 C
ATOM 3733 CD PRO B 212 13.212 -9.047 -31.847 1.00 81.26 C
ANISOU 3733 CD PRO B 212 11487 10532 8856 -1258 1686 -1588 C
ATOM 3734 N LYS B 213 14.343 -6.074 -29.919 1.00 57.98 N
ANISOU 3734 N LYS B 213 8081 7904 6044 -1300 1521 -1444 N
ATOM 3735 CA LYS B 213 15.070 -4.915 -29.405 1.00 62.99 C
ANISOU 3735 CA LYS B 213 8535 8697 6700 -1343 1488 -1425 C
ATOM 3736 C LYS B 213 14.146 -3.735 -29.117 1.00 71.53 C
ANISOU 3736 C LYS B 213 9598 9765 7816 -1533 1331 -1321 C
ATOM 3737 O LYS B 213 14.260 -3.090 -28.068 1.00 78.42 O
ANISOU 3737 O LYS B 213 10410 10664 8721 -1524 1259 -1298 O
ATOM 3738 CB LYS B 213 16.157 -4.515 -30.403 1.00 66.83 C
ANISOU 3738 CB LYS B 213 8888 9363 7141 -1388 1615 -1470 C
ATOM 3739 CG LYS B 213 17.218 -5.584 -30.617 1.00 68.33 C
ANISOU 3739 CG LYS B 213 9052 9577 7332 -1173 1826 -1575 C
ATOM 3740 CD LYS B 213 18.110 -5.264 -31.804 1.00 83.58 C
ANISOU 3740 CD LYS B 213 10875 11661 9219 -1221 1985 -1598 C
ATOM 3741 CE LYS B 213 19.209 -6.301 -31.960 1.00101.14 C
ANISOU 3741 CE LYS B 213 13040 13901 11488 -978 2237 -1697 C
ATOM 3742 NZ LYS B 213 20.114 -6.357 -30.784 1.00102.99 N
ANISOU 3742 NZ LYS B 213 13053 14218 11861 -814 2295 -1717 N
ATOM 3743 N ILE B 214 13.233 -3.431 -30.045 1.00 68.57 N
ANISOU 3743 N ILE B 214 9282 9347 7427 -1717 1287 -1265 N
ATOM 3744 CA ILE B 214 12.365 -2.260 -29.898 1.00 49.32 C
ANISOU 3744 CA ILE B 214 6809 6896 5033 -1910 1171 -1172 C
ATOM 3745 C ILE B 214 11.312 -2.504 -28.814 1.00 48.00 C
ANISOU 3745 C ILE B 214 6728 6569 4943 -1851 1120 -1110 C
ATOM 3746 O ILE B 214 11.078 -1.654 -27.942 1.00 48.93 O
ANISOU 3746 O ILE B 214 6802 6677 5112 -1876 1066 -1066 O
ATOM 3747 CB ILE B 214 11.711 -1.891 -31.249 1.00 48.26 C
ANISOU 3747 CB ILE B 214 6716 6776 4845 -2149 1143 -1133 C
ATOM 3748 CG1 ILE B 214 12.764 -1.428 -32.272 1.00 45.72 C
ANISOU 3748 CG1 ILE B 214 6311 6629 4433 -2220 1190 -1181 C
ATOM 3749 CG2 ILE B 214 10.655 -0.806 -31.069 1.00 47.75 C
ANISOU 3749 CG2 ILE B 214 6639 6675 4828 -2299 1019 -1029 C
ATOM 3750 CD1 ILE B 214 12.390 -1.743 -33.703 1.00 57.67 C
ANISOU 3750 CD1 ILE B 214 7936 8142 5836 -2374 1216 -1182 C
ATOM 3751 N TYR B 215 10.688 -3.687 -28.829 1.00 55.55 N
ANISOU 3751 N TYR B 215 7816 7395 5896 -1772 1150 -1111 N
ATOM 3752 CA TYR B 215 9.658 -3.995 -27.842 1.00 49.20 C
ANISOU 3752 CA TYR B 215 7097 6445 5153 -1725 1124 -1049 C
ATOM 3753 C TYR B 215 10.189 -3.865 -26.420 1.00 43.02 C
ANISOU 3753 C TYR B 215 6289 5660 4396 -1551 1102 -1062 C
ATOM 3754 O TYR B 215 9.637 -3.111 -25.613 1.00 42.35 O
ANISOU 3754 O TYR B 215 6201 5532 4357 -1587 1067 -1005 O
ATOM 3755 CB TYR B 215 9.107 -5.396 -28.096 1.00 47.20 C
ANISOU 3755 CB TYR B 215 6990 6069 4875 -1670 1166 -1065 C
ATOM 3756 CG TYR B 215 8.068 -5.833 -27.100 1.00 43.83 C
ANISOU 3756 CG TYR B 215 6658 5495 4501 -1631 1160 -1003 C
ATOM 3757 CD1 TYR B 215 6.802 -5.271 -27.082 1.00 46.00 C
ANISOU 3757 CD1 TYR B 215 6958 5710 4808 -1807 1157 -907 C
ATOM 3758 CD2 TYR B 215 8.347 -6.840 -26.188 1.00 43.36 C
ANISOU 3758 CD2 TYR B 215 6674 5359 4443 -1430 1181 -1039 C
ATOM 3759 CE1 TYR B 215 5.850 -5.685 -26.163 1.00 54.24 C
ANISOU 3759 CE1 TYR B 215 8098 6621 5891 -1777 1192 -855 C
ATOM 3760 CE2 TYR B 215 7.407 -7.265 -25.271 1.00 40.12 C
ANISOU 3760 CE2 TYR B 215 6363 4813 4068 -1407 1193 -980 C
ATOM 3761 CZ TYR B 215 6.159 -6.683 -25.261 1.00 56.05 C
ANISOU 3761 CZ TYR B 215 8403 6769 6125 -1580 1206 -892 C
ATOM 3762 OH TYR B 215 5.250 -7.133 -24.332 1.00 79.74 O
ANISOU 3762 OH TYR B 215 11515 9631 9154 -1559 1257 -839 O
ATOM 3763 N HIS B 216 11.272 -4.576 -26.098 1.00 42.97 N
ANISOU 3763 N HIS B 216 6280 5699 4346 -1374 1135 -1144 N
ATOM 3764 CA HIS B 216 11.785 -4.558 -24.735 1.00 42.31 C
ANISOU 3764 CA HIS B 216 6209 5619 4249 -1235 1105 -1161 C
ATOM 3765 C HIS B 216 12.394 -3.216 -24.349 1.00 50.76 C
ANISOU 3765 C HIS B 216 7169 6812 5307 -1317 1049 -1166 C
ATOM 3766 O HIS B 216 12.474 -2.916 -23.154 1.00 50.48 O
ANISOU 3766 O HIS B 216 7179 6751 5248 -1263 992 -1160 O
ATOM 3767 CB HIS B 216 12.788 -5.692 -24.564 1.00 45.57 C
ANISOU 3767 CB HIS B 216 6652 6053 4610 -1052 1174 -1260 C
ATOM 3768 CG HIS B 216 12.140 -7.027 -24.431 1.00 54.63 C
ANISOU 3768 CG HIS B 216 7947 7040 5768 -950 1209 -1256 C
ATOM 3769 ND1 HIS B 216 11.427 -7.399 -23.316 1.00 58.84 N
ANISOU 3769 ND1 HIS B 216 8597 7450 6309 -893 1171 -1200 N
ATOM 3770 CD2 HIS B 216 12.043 -8.059 -25.299 1.00 62.94 C
ANISOU 3770 CD2 HIS B 216 9065 8030 6820 -920 1286 -1303 C
ATOM 3771 CE1 HIS B 216 10.946 -8.619 -23.487 1.00 67.28 C
ANISOU 3771 CE1 HIS B 216 9784 8390 7390 -837 1221 -1210 C
ATOM 3772 NE2 HIS B 216 11.305 -9.042 -24.684 1.00 67.26 N
ANISOU 3772 NE2 HIS B 216 9757 8415 7383 -852 1284 -1278 N
ATOM 3773 N SER B 217 12.833 -2.406 -25.315 1.00 58.66 N
ANISOU 3773 N SER B 217 8042 7941 6303 -1462 1060 -1180 N
ATOM 3774 CA SER B 217 13.226 -1.043 -24.971 1.00 54.03 C
ANISOU 3774 CA SER B 217 7360 7459 5710 -1585 999 -1175 C
ATOM 3775 C SER B 217 12.025 -0.188 -24.578 1.00 60.74 C
ANISOU 3775 C SER B 217 8263 8187 6627 -1684 956 -1084 C
ATOM 3776 O SER B 217 12.099 0.576 -23.605 1.00 62.40 O
ANISOU 3776 O SER B 217 8495 8383 6833 -1684 903 -1080 O
ATOM 3777 CB SER B 217 13.969 -0.380 -26.127 1.00 38.69 C
ANISOU 3777 CB SER B 217 5263 5698 3739 -1740 1032 -1205 C
ATOM 3778 OG SER B 217 15.036 -1.187 -26.603 1.00 44.98 O
ANISOU 3778 OG SER B 217 5996 6611 4486 -1637 1133 -1289 O
ATOM 3779 N CYS B 218 10.906 -0.310 -25.314 1.00 62.25 N
ANISOU 3779 N CYS B 218 8491 8292 6870 -1776 989 -1019 N
ATOM 3780 CA CYS B 218 9.737 0.537 -25.057 1.00 55.16 C
ANISOU 3780 CA CYS B 218 7627 7303 6027 -1890 1002 -937 C
ATOM 3781 C CYS B 218 9.108 0.238 -23.696 1.00 65.50 C
ANISOU 3781 C CYS B 218 9061 8460 7366 -1753 1013 -922 C
ATOM 3782 O CYS B 218 8.753 1.159 -22.947 1.00 82.25 O
ANISOU 3782 O CYS B 218 11213 10534 9505 -1776 1027 -902 O
ATOM 3783 CB CYS B 218 8.702 0.370 -26.175 1.00 42.77 C
ANISOU 3783 CB CYS B 218 6081 5708 4462 -1901 977 -866 C
ATOM 3784 SG CYS B 218 9.184 1.047 -27.796 1.00 59.08 S
ANISOU 3784 SG CYS B 218 8079 7964 6403 -1957 917 -859 S
ATOM 3785 N PHE B 219 8.956 -1.045 -23.358 1.00 60.93 N
ANISOU 3785 N PHE B 219 8570 7804 6777 -1610 1024 -931 N
ATOM 3786 CA PHE B 219 8.251 -1.399 -22.132 1.00 66.67 C
ANISOU 3786 CA PHE B 219 9425 8390 7515 -1507 1052 -902 C
ATOM 3787 C PHE B 219 9.129 -1.256 -20.898 1.00 66.36 C
ANISOU 3787 C PHE B 219 9434 8381 7399 -1373 992 -944 C
ATOM 3788 O PHE B 219 8.601 -1.219 -19.779 1.00 69.40 O
ANISOU 3788 O PHE B 219 9937 8663 7770 -1315 1015 -920 O
ATOM 3789 CB PHE B 219 7.661 -2.802 -22.242 1.00 72.46 C
ANISOU 3789 CB PHE B 219 10249 9029 8252 -1440 1094 -882 C
ATOM 3790 CG PHE B 219 6.239 -2.810 -22.714 1.00 85.88 C
ANISOU 3790 CG PHE B 219 11994 10617 10019 -1591 1172 -823 C
ATOM 3791 CD1 PHE B 219 5.212 -2.421 -21.862 1.00 91.33 C
ANISOU 3791 CD1 PHE B 219 12767 11173 10763 -1619 1255 -784 C
ATOM 3792 CD2 PHE B 219 5.932 -3.180 -24.007 1.00 82.16 C
ANISOU 3792 CD2 PHE B 219 11503 10174 9542 -1723 1180 -812 C
ATOM 3793 CE1 PHE B 219 3.903 -2.406 -22.294 1.00 81.63 C
ANISOU 3793 CE1 PHE B 219 11530 9902 9583 -1595 1245 -758 C
ATOM 3794 CE2 PHE B 219 4.630 -3.171 -24.446 1.00 74.55 C
ANISOU 3794 CE2 PHE B 219 10553 9197 8575 -1705 1162 -756 C
ATOM 3795 CZ PHE B 219 3.612 -2.782 -23.590 1.00 74.74 C
ANISOU 3795 CZ PHE B 219 10644 9137 8618 -1632 1201 -777 C
ATOM 3796 N PHE B 220 10.452 -1.207 -21.069 1.00 55.13 N
ANISOU 3796 N PHE B 220 7939 7099 5909 -1344 925 -1012 N
ATOM 3797 CA PHE B 220 11.305 -0.834 -19.945 1.00 39.97 C
ANISOU 3797 CA PHE B 220 6073 5220 3893 -1285 842 -1060 C
ATOM 3798 C PHE B 220 11.103 0.634 -19.582 1.00 42.61 C
ANISOU 3798 C PHE B 220 6404 5537 4249 -1399 812 -1050 C
ATOM 3799 O PHE B 220 11.045 0.992 -18.399 1.00 57.58 O
ANISOU 3799 O PHE B 220 8427 7364 6086 -1358 774 -1058 O
ATOM 3800 CB PHE B 220 12.775 -1.102 -20.260 1.00 27.50 C
ANISOU 3800 CB PHE B 220 4407 3809 2232 -1271 788 -1151 C
ATOM 3801 CG PHE B 220 13.724 -0.503 -19.243 1.00 34.19 C
ANISOU 3801 CG PHE B 220 5296 4727 2967 -1292 654 -1207 C
ATOM 3802 CD1 PHE B 220 13.908 -1.081 -17.986 1.00 48.82 C
ANISOU 3802 CD1 PHE B 220 7324 6525 4699 -1188 583 -1218 C
ATOM 3803 CD2 PHE B 220 14.392 0.666 -19.530 1.00 33.62 C
ANISOU 3803 CD2 PHE B 220 5103 4771 2901 -1444 572 -1239 C
ATOM 3804 CE1 PHE B 220 14.774 -0.509 -17.049 1.00 52.41 C
ANISOU 3804 CE1 PHE B 220 7843 7042 5028 -1247 405 -1258 C
ATOM 3805 CE2 PHE B 220 15.253 1.245 -18.601 1.00 43.11 C
ANISOU 3805 CE2 PHE B 220 6344 6028 4009 -1499 393 -1281 C
ATOM 3806 CZ PHE B 220 15.446 0.658 -17.359 1.00 49.53 C
ANISOU 3806 CZ PHE B 220 7343 6786 4690 -1405 296 -1289 C
ATOM 3807 N ILE B 221 11.006 1.501 -20.595 1.00 41.79 N
ANISOU 3807 N ILE B 221 6171 5491 4215 -1550 835 -1037 N
ATOM 3808 CA ILE B 221 10.695 2.912 -20.369 1.00 45.80 C
ANISOU 3808 CA ILE B 221 6681 5962 4759 -1659 830 -1025 C
ATOM 3809 C ILE B 221 9.270 3.046 -19.845 1.00 50.56 C
ANISOU 3809 C ILE B 221 7403 6385 5422 -1645 947 -977 C
ATOM 3810 O ILE B 221 9.011 3.719 -18.839 1.00 46.33 O
ANISOU 3810 O ILE B 221 6983 5751 4871 -1624 960 -995 O
ATOM 3811 CB ILE B 221 10.887 3.716 -21.674 1.00 42.02 C
ANISOU 3811 CB ILE B 221 6040 5604 4323 -1820 837 -1002 C
ATOM 3812 CG1 ILE B 221 12.328 3.621 -22.170 1.00 33.65 C
ANISOU 3812 CG1 ILE B 221 4848 4732 3204 -1858 752 -1059 C
ATOM 3813 CG2 ILE B 221 10.513 5.208 -21.504 1.00 57.01 C
ANISOU 3813 CG2 ILE B 221 7944 7449 6269 -1891 823 -979 C
ATOM 3814 CD1 ILE B 221 13.365 4.223 -21.206 1.00 54.98 C
ANISOU 3814 CD1 ILE B 221 7563 7471 5856 -1857 603 -1115 C
ATOM 3815 N VAL B 222 8.328 2.377 -20.510 1.00 61.43 N
ANISOU 3815 N VAL B 222 8766 7713 6863 -1668 1042 -923 N
ATOM 3816 CA VAL B 222 6.917 2.594 -20.228 1.00 58.00 C
ANISOU 3816 CA VAL B 222 8415 7124 6498 -1702 1188 -880 C
ATOM 3817 C VAL B 222 6.515 2.052 -18.860 1.00 57.18 C
ANISOU 3817 C VAL B 222 8476 6878 6372 -1569 1229 -882 C
ATOM 3818 O VAL B 222 5.642 2.627 -18.199 1.00 59.62 O
ANISOU 3818 O VAL B 222 8881 7048 6726 -1581 1359 -876 O
ATOM 3819 CB VAL B 222 6.061 1.982 -21.351 1.00 54.05 C
ANISOU 3819 CB VAL B 222 7852 6644 6040 -1699 1204 -833 C
ATOM 3820 CG1 VAL B 222 4.675 1.648 -20.823 1.00 49.06 C
ANISOU 3820 CG1 VAL B 222 7321 5861 5458 -1606 1302 -828 C
ATOM 3821 CG2 VAL B 222 5.948 2.989 -22.500 1.00 56.09 C
ANISOU 3821 CG2 VAL B 222 8020 7023 6269 -1736 1138 -856 C
ATOM 3822 N THR B 223 7.109 0.945 -18.417 1.00 59.88 N
ANISOU 3822 N THR B 223 8862 7257 6632 -1434 1149 -888 N
ATOM 3823 CA THR B 223 6.654 0.296 -17.196 1.00 58.02 C
ANISOU 3823 CA THR B 223 8790 6911 6342 -1317 1200 -868 C
ATOM 3824 C THR B 223 7.680 0.297 -16.069 1.00 57.09 C
ANISOU 3824 C THR B 223 8774 6851 6068 -1217 1087 -916 C
ATOM 3825 O THR B 223 7.412 -0.290 -15.016 1.00 68.65 O
ANISOU 3825 O THR B 223 10391 8243 7448 -1131 1120 -898 O
ATOM 3826 CB THR B 223 6.206 -1.142 -17.512 1.00 62.35 C
ANISOU 3826 CB THR B 223 9356 7423 6912 -1264 1234 -823 C
ATOM 3827 OG1 THR B 223 7.349 -1.999 -17.618 1.00 66.93 O
ANISOU 3827 OG1 THR B 223 9911 8119 7401 -1166 1117 -858 O
ATOM 3828 CG2 THR B 223 5.455 -1.153 -18.825 1.00 70.32 C
ANISOU 3828 CG2 THR B 223 10268 8409 8043 -1402 1294 -797 C
ATOM 3829 N TYR B 224 8.827 0.954 -16.237 1.00 47.33 N
ANISOU 3829 N TYR B 224 7473 5735 4777 -1250 956 -977 N
ATOM 3830 CA TYR B 224 9.761 1.065 -15.125 1.00 40.40 C
ANISOU 3830 CA TYR B 224 6717 4896 3736 -1199 832 -1030 C
ATOM 3831 C TYR B 224 10.349 2.461 -15.021 1.00 39.14 C
ANISOU 3831 C TYR B 224 6544 4768 3559 -1301 745 -1088 C
ATOM 3832 O TYR B 224 10.119 3.167 -14.031 1.00 51.98 O
ANISOU 3832 O TYR B 224 8323 6305 5120 -1312 754 -1113 O
ATOM 3833 CB TYR B 224 10.880 0.034 -15.254 1.00 48.25 C
ANISOU 3833 CB TYR B 224 7684 6012 4636 -1129 714 -1058 C
ATOM 3834 CG TYR B 224 11.840 0.066 -14.090 1.00 53.84 C
ANISOU 3834 CG TYR B 224 8544 6762 5152 -1110 557 -1104 C
ATOM 3835 CD1 TYR B 224 11.652 -0.755 -12.977 1.00 53.29 C
ANISOU 3835 CD1 TYR B 224 8674 6630 4945 -1024 558 -1075 C
ATOM 3836 CD2 TYR B 224 12.924 0.932 -14.090 1.00 49.34 C
ANISOU 3836 CD2 TYR B 224 7928 6290 4528 -1208 390 -1165 C
ATOM 3837 CE1 TYR B 224 12.529 -0.717 -11.901 1.00 49.71 C
ANISOU 3837 CE1 TYR B 224 8386 6216 4287 -1037 383 -1101 C
ATOM 3838 CE2 TYR B 224 13.794 0.977 -13.033 1.00 52.23 C
ANISOU 3838 CE2 TYR B 224 8441 6691 4712 -1226 200 -1192 C
ATOM 3839 CZ TYR B 224 13.598 0.154 -11.941 1.00 51.55 C
ANISOU 3839 CZ TYR B 224 8569 6547 4472 -1142 190 -1158 C
ATOM 3840 OH TYR B 224 14.478 0.203 -10.886 1.00 52.54 O
ANISOU 3840 OH TYR B 224 8859 6710 4395 -1186 -36 -1163 O
ATOM 3841 N LEU B 225 11.118 2.869 -16.031 1.00 27.81 N
ANISOU 3841 N LEU B 225 4935 3455 2176 -1388 665 -1111 N
ATOM 3842 CA LEU B 225 11.909 4.085 -15.885 1.00 36.20 C
ANISOU 3842 CA LEU B 225 5980 4560 3213 -1496 537 -1165 C
ATOM 3843 C LEU B 225 11.020 5.321 -15.936 1.00 46.32 C
ANISOU 3843 C LEU B 225 7286 5720 4592 -1575 643 -1160 C
ATOM 3844 O LEU B 225 11.094 6.189 -15.057 1.00 59.09 O
ANISOU 3844 O LEU B 225 9041 7255 6154 -1599 600 -1208 O
ATOM 3845 CB LEU B 225 12.981 4.141 -16.976 1.00 40.39 C
ANISOU 3845 CB LEU B 225 6299 5269 3780 -1586 437 -1182 C
ATOM 3846 CG LEU B 225 14.113 5.144 -16.741 1.00 46.45 C
ANISOU 3846 CG LEU B 225 7024 6111 4515 -1704 239 -1224 C
ATOM 3847 CD1 LEU B 225 15.114 4.570 -15.760 1.00 55.17 C
ANISOU 3847 CD1 LEU B 225 8226 7274 5461 -1670 49 -1261 C
ATOM 3848 CD2 LEU B 225 14.780 5.518 -18.050 1.00 43.35 C
ANISOU 3848 CD2 LEU B 225 6375 5876 4221 -1831 210 -1210 C
ATOM 3849 N ALA B 226 10.163 5.417 -16.959 1.00 46.45 N
ANISOU 3849 N ALA B 226 7187 5717 4746 -1625 781 -1109 N
ATOM 3850 CA ALA B 226 9.280 6.580 -17.049 1.00 41.49 C
ANISOU 3850 CA ALA B 226 6580 4966 4218 -1701 894 -1109 C
ATOM 3851 C ALA B 226 8.296 6.650 -15.889 1.00 49.91 C
ANISOU 3851 C ALA B 226 7853 5848 5262 -1629 1043 -1123 C
ATOM 3852 O ALA B 226 8.195 7.707 -15.246 1.00 53.33 O
ANISOU 3852 O ALA B 226 8399 6176 5688 -1655 1063 -1180 O
ATOM 3853 CB ALA B 226 8.548 6.574 -18.396 1.00 42.35 C
ANISOU 3853 CB ALA B 226 6527 5106 4456 -1774 996 -1044 C
ATOM 3854 N PRO B 227 7.548 5.597 -15.566 1.00 53.47 N
ANISOU 3854 N PRO B 227 8369 6243 5706 -1542 1157 -1075 N
ATOM 3855 CA PRO B 227 6.668 5.691 -14.391 1.00 51.39 C
ANISOU 3855 CA PRO B 227 8305 5810 5412 -1478 1314 -1082 C
ATOM 3856 C PRO B 227 7.414 6.005 -13.107 1.00 51.93 C
ANISOU 3856 C PRO B 227 8562 5872 5296 -1435 1201 -1153 C
ATOM 3857 O PRO B 227 6.928 6.812 -12.303 1.00 54.36 O
ANISOU 3857 O PRO B 227 9031 6044 5580 -1440 1313 -1200 O
ATOM 3858 CB PRO B 227 6.003 4.302 -14.338 1.00 49.09 C
ANISOU 3858 CB PRO B 227 8025 5493 5132 -1397 1397 -1004 C
ATOM 3859 CG PRO B 227 6.093 3.767 -15.733 1.00 57.59 C
ANISOU 3859 CG PRO B 227 8902 6673 6306 -1452 1352 -961 C
ATOM 3860 CD PRO B 227 7.331 4.357 -16.336 1.00 63.64 C
ANISOU 3860 CD PRO B 227 9550 7594 7035 -1513 1172 -1008 C
ATOM 3861 N LEU B 228 8.575 5.378 -12.885 1.00 52.31 N
ANISOU 3861 N LEU B 228 8608 6057 5209 -1400 993 -1167 N
ATOM 3862 CA LEU B 228 9.319 5.630 -11.655 1.00 41.52 C
ANISOU 3862 CA LEU B 228 7438 4690 3648 -1389 862 -1233 C
ATOM 3863 C LEU B 228 9.929 7.024 -11.654 1.00 48.82 C
ANISOU 3863 C LEU B 228 8375 5602 4573 -1498 752 -1314 C
ATOM 3864 O LEU B 228 9.956 7.698 -10.616 1.00 54.95 O
ANISOU 3864 O LEU B 228 9361 6285 5233 -1518 743 -1383 O
ATOM 3865 CB LEU B 228 10.415 4.581 -11.469 1.00 37.66 C
ANISOU 3865 CB LEU B 228 6937 4345 3026 -1342 664 -1223 C
ATOM 3866 CG LEU B 228 9.938 3.164 -11.170 1.00 46.06 C
ANISOU 3866 CG LEU B 228 8053 5402 4047 -1230 745 -1155 C
ATOM 3867 CD1 LEU B 228 11.120 2.250 -10.896 1.00 60.40 C
ANISOU 3867 CD1 LEU B 228 9891 7346 5713 -1194 541 -1158 C
ATOM 3868 CD2 LEU B 228 8.994 3.209 -9.984 1.00 35.20 C
ANISOU 3868 CD2 LEU B 228 6910 3879 2587 -1196 904 -1147 C
ATOM 3869 N GLY B 229 10.434 7.468 -12.806 1.00 50.80 N
ANISOU 3869 N GLY B 229 8412 5941 4948 -1580 666 -1308 N
ATOM 3870 CA GLY B 229 11.019 8.795 -12.875 1.00 47.62 C
ANISOU 3870 CA GLY B 229 8002 5518 4574 -1694 547 -1371 C
ATOM 3871 C GLY B 229 10.010 9.902 -12.631 1.00 45.77 C
ANISOU 3871 C GLY B 229 7877 5093 4423 -1719 730 -1414 C
ATOM 3872 O GLY B 229 10.316 10.901 -11.977 1.00 44.91 O
ANISOU 3872 O GLY B 229 7908 4894 4261 -1772 661 -1498 O
ATOM 3873 N LEU B 230 8.805 9.762 -13.187 1.00 59.33 N
ANISOU 3873 N LEU B 230 9526 6733 6283 -1689 965 -1363 N
ATOM 3874 CA LEU B 230 7.758 10.746 -12.930 1.00 60.91 C
ANISOU 3874 CA LEU B 230 9823 6730 6589 -1696 1179 -1404 C
ATOM 3875 C LEU B 230 7.307 10.685 -11.475 1.00 58.97 C
ANISOU 3875 C LEU B 230 9861 6355 6192 -1620 1305 -1458 C
ATOM 3876 O LEU B 230 7.133 11.723 -10.827 1.00 76.66 O
ANISOU 3876 O LEU B 230 12265 8447 8416 -1641 1369 -1549 O
ATOM 3877 CB LEU B 230 6.578 10.538 -13.878 1.00 62.21 C
ANISOU 3877 CB LEU B 230 9831 6844 6961 -1690 1398 -1325 C
ATOM 3878 CG LEU B 230 6.806 11.073 -15.294 1.00 47.29 C
ANISOU 3878 CG LEU B 230 7688 5033 5246 -1784 1300 -1283 C
ATOM 3879 CD1 LEU B 230 5.839 10.443 -16.298 1.00 52.35 C
ANISOU 3879 CD1 LEU B 230 8158 5694 6038 -1771 1437 -1187 C
ATOM 3880 CD2 LEU B 230 6.712 12.600 -15.334 1.00 36.00 C
ANISOU 3880 CD2 LEU B 230 6260 3455 3963 -1838 1294 -1335 C
ATOM 3881 N MET B 231 7.093 9.474 -10.946 1.00 59.66 N
ANISOU 3881 N MET B 231 10015 6485 6167 -1534 1347 -1402 N
ATOM 3882 CA MET B 231 6.695 9.351 -9.546 1.00 60.42 C
ANISOU 3882 CA MET B 231 10386 6473 6099 -1474 1461 -1441 C
ATOM 3883 C MET B 231 7.759 9.938 -8.622 1.00 64.29 C
ANISOU 3883 C MET B 231 11071 6980 6375 -1526 1251 -1547 C
ATOM 3884 O MET B 231 7.430 10.553 -7.600 1.00 70.67 O
ANISOU 3884 O MET B 231 12130 7649 7073 -1530 1360 -1629 O
ATOM 3885 CB MET B 231 6.437 7.888 -9.183 1.00 64.25 C
ANISOU 3885 CB MET B 231 10895 7015 6501 -1386 1492 -1352 C
ATOM 3886 CG MET B 231 5.235 7.236 -9.811 1.00 72.16 C
ANISOU 3886 CG MET B 231 11769 7957 7693 -1341 1718 -1249 C
ATOM 3887 SD MET B 231 5.137 5.523 -9.253 1.00 54.30 S
ANISOU 3887 SD MET B 231 9568 5754 5311 -1245 1698 -1160 S
ATOM 3888 CE MET B 231 5.707 4.628 -10.684 1.00 89.17 C
ANISOU 3888 CE MET B 231 13697 10344 9838 -1249 1523 -1091 C
ATOM 3889 N ALA B 232 9.041 9.782 -8.977 1.00 68.88 N
ANISOU 3889 N ALA B 232 11546 7725 6902 -1580 954 -1549 N
ATOM 3890 CA ALA B 232 10.123 10.300 -8.138 1.00 70.14 C
ANISOU 3890 CA ALA B 232 11876 7904 6870 -1656 719 -1637 C
ATOM 3891 C ALA B 232 10.083 11.818 -8.060 1.00 79.65 C
ANISOU 3891 C ALA B 232 13166 8967 8131 -1744 734 -1744 C
ATOM 3892 O ALA B 232 10.143 12.397 -6.968 1.00 89.58 O
ANISOU 3892 O ALA B 232 14698 10116 9222 -1780 733 -1842 O
ATOM 3893 CB ALA B 232 11.479 9.836 -8.667 1.00 60.05 C
ANISOU 3893 CB ALA B 232 10421 6823 5573 -1705 410 -1600 C
ATOM 3894 N MET B 233 9.974 12.480 -9.212 1.00 73.58 N
ANISOU 3894 N MET B 233 12177 8188 7592 -1788 748 -1729 N
ATOM 3895 CA MET B 233 9.890 13.935 -9.220 1.00 78.24 C
ANISOU 3895 CA MET B 233 12831 8621 8276 -1866 764 -1826 C
ATOM 3896 C MET B 233 8.663 14.430 -8.467 1.00 79.72 C
ANISOU 3896 C MET B 233 13243 8584 8462 -1803 1081 -1895 C
ATOM 3897 O MET B 233 8.688 15.527 -7.895 1.00 85.97 O
ANISOU 3897 O MET B 233 14222 9218 9225 -1852 1094 -2016 O
ATOM 3898 CB MET B 233 9.883 14.441 -10.658 1.00 76.28 C
ANISOU 3898 CB MET B 233 12288 8400 8296 -1921 737 -1768 C
ATOM 3899 CG MET B 233 11.148 14.105 -11.416 1.00 78.64 C
ANISOU 3899 CG MET B 233 12361 8911 8606 -1997 443 -1702 C
ATOM 3900 SD MET B 233 11.218 14.781 -13.078 1.00 89.60 S
ANISOU 3900 SD MET B 233 13413 10342 10289 -2084 398 -1618 S
ATOM 3901 CE MET B 233 9.923 13.845 -13.891 1.00 89.90 C
ANISOU 3901 CE MET B 233 13316 10403 10440 -1988 677 -1518 C
ATOM 3902 N ALA B 234 7.579 13.653 -8.469 1.00 75.76 N
ANISOU 3902 N ALA B 234 12723 8055 8006 -1698 1347 -1820 N
ATOM 3903 CA ALA B 234 6.383 14.055 -7.733 1.00 71.46 C
ANISOU 3903 CA ALA B 234 12375 7297 7480 -1632 1683 -1869 C
ATOM 3904 C ALA B 234 6.634 14.076 -6.224 1.00 74.02 C
ANISOU 3904 C ALA B 234 13055 7566 7505 -1636 1675 -1967 C
ATOM 3905 O ALA B 234 6.313 15.062 -5.548 1.00 77.12 O
ANISOU 3905 O ALA B 234 13669 7772 7861 -1652 1811 -2090 O
ATOM 3906 CB ALA B 234 5.215 13.134 -8.090 1.00 60.21 C
ANISOU 3906 CB ALA B 234 10826 5861 6191 -1536 1952 -1744 C
ATOM 3907 N TYR B 235 7.228 13.004 -5.678 1.00 67.92 N
ANISOU 3907 N TYR B 235 12350 6943 6513 -1627 1514 -1919 N
ATOM 3908 CA TYR B 235 7.391 12.914 -4.227 1.00 68.45 C
ANISOU 3908 CA TYR B 235 12771 6959 6279 -1643 1516 -1996 C
ATOM 3909 C TYR B 235 8.457 13.875 -3.705 1.00 81.24 C
ANISOU 3909 C TYR B 235 14573 8557 7737 -1772 1260 -2130 C
ATOM 3910 O TYR B 235 8.399 14.295 -2.542 1.00 94.58 O
ANISOU 3910 O TYR B 235 16603 10129 9204 -1812 1320 -2238 O
ATOM 3911 CB TYR B 235 7.701 11.470 -3.807 1.00 63.05 C
ANISOU 3911 CB TYR B 235 12106 6429 5423 -1602 1411 -1894 C
ATOM 3912 CG TYR B 235 6.477 10.576 -3.814 1.00 56.58 C
ANISOU 3912 CG TYR B 235 11242 5562 4692 -1487 1710 -1789 C
ATOM 3913 CD1 TYR B 235 5.476 10.737 -2.871 1.00 60.47 C
ANISOU 3913 CD1 TYR B 235 11986 5881 5108 -1448 2020 -1826 C
ATOM 3914 CD2 TYR B 235 6.312 9.577 -4.771 1.00 50.79 C
ANISOU 3914 CD2 TYR B 235 10224 4947 4127 -1426 1690 -1655 C
ATOM 3915 CE1 TYR B 235 4.346 9.945 -2.867 1.00 64.21 C
ANISOU 3915 CE1 TYR B 235 12413 6297 5686 -1355 2294 -1721 C
ATOM 3916 CE2 TYR B 235 5.169 8.767 -4.773 1.00 59.98 C
ANISOU 3916 CE2 TYR B 235 11352 6049 5388 -1337 1950 -1555 C
ATOM 3917 CZ TYR B 235 4.196 8.961 -3.816 1.00 68.73 C
ANISOU 3917 CZ TYR B 235 12697 6983 6434 -1304 2247 -1584 C
ATOM 3918 OH TYR B 235 3.048 8.203 -3.757 1.00 91.31 O
ANISOU 3918 OH TYR B 235 15529 9762 9404 -1226 2513 -1482 O
ATOM 3919 N PHE B 236 9.438 14.236 -4.530 1.00 83.39 N
ANISOU 3919 N PHE B 236 14635 8935 8115 -1852 974 -2123 N
ATOM 3920 CA PHE B 236 10.363 15.280 -4.107 1.00 85.29 C
ANISOU 3920 CA PHE B 236 15030 9125 8253 -1991 739 -2246 C
ATOM 3921 C PHE B 236 9.636 16.610 -3.957 1.00 82.75 C
ANISOU 3921 C PHE B 236 14856 8557 8030 -2001 958 -2381 C
ATOM 3922 O PHE B 236 9.871 17.348 -2.992 1.00 84.09 O
ANISOU 3922 O PHE B 236 15338 8598 8014 -2081 926 -2520 O
ATOM 3923 CB PHE B 236 11.520 15.400 -5.097 1.00 83.98 C
ANISOU 3923 CB PHE B 236 14572 9114 8221 -2079 406 -2192 C
ATOM 3924 CG PHE B 236 12.284 16.680 -4.974 1.00 96.02 C
ANISOU 3924 CG PHE B 236 16178 10551 9754 -2227 197 -2304 C
ATOM 3925 CD1 PHE B 236 13.217 16.849 -3.960 1.00100.12 C
ANISOU 3925 CD1 PHE B 236 16940 11083 10017 -2352 -54 -2368 C
ATOM 3926 CD2 PHE B 236 12.054 17.721 -5.856 1.00105.93 C
ANISOU 3926 CD2 PHE B 236 17273 11697 11277 -2255 242 -2336 C
ATOM 3927 CE1 PHE B 236 13.915 18.039 -3.840 1.00109.77 C
ANISOU 3927 CE1 PHE B 236 18240 12212 11256 -2505 -257 -2469 C
ATOM 3928 CE2 PHE B 236 12.743 18.911 -5.747 1.00113.73 C
ANISOU 3928 CE2 PHE B 236 18332 12586 12295 -2396 45 -2435 C
ATOM 3929 CZ PHE B 236 13.676 19.074 -4.740 1.00116.11 C
ANISOU 3929 CZ PHE B 236 18872 12901 12344 -2523 -203 -2505 C
ATOM 3930 N GLN B 237 8.737 16.923 -4.895 1.00 88.70 N
ANISOU 3930 N GLN B 237 15397 9227 9078 -1924 1186 -2342 N
ATOM 3931 CA GLN B 237 7.943 18.143 -4.780 1.00 89.73 C
ANISOU 3931 CA GLN B 237 15648 9100 9346 -1910 1430 -2460 C
ATOM 3932 C GLN B 237 6.980 18.074 -3.600 1.00 92.18 C
ANISOU 3932 C GLN B 237 16280 9251 9493 -1834 1769 -2531 C
ATOM 3933 O GLN B 237 6.717 19.093 -2.948 1.00 94.70 O
ANISOU 3933 O GLN B 237 16855 9356 9770 -1856 1902 -2686 O
ATOM 3934 CB GLN B 237 7.192 18.396 -6.085 1.00 81.34 C
ANISOU 3934 CB GLN B 237 14262 7989 8655 -1850 1588 -2374 C
ATOM 3935 CG GLN B 237 8.033 19.067 -7.148 1.00 75.66 C
ANISOU 3935 CG GLN B 237 13300 7319 8127 -1955 1302 -2357 C
ATOM 3936 CD GLN B 237 7.183 19.713 -8.221 1.00 84.08 C
ANISOU 3936 CD GLN B 237 14134 8248 9565 -1915 1482 -2308 C
ATOM 3937 OE1 GLN B 237 5.982 19.454 -8.314 1.00 83.20 O
ANISOU 3937 OE1 GLN B 237 13982 8046 9586 -1802 1814 -2257 O
ATOM 3938 NE2 GLN B 237 7.797 20.561 -9.035 1.00 93.74 N
ANISOU 3938 NE2 GLN B 237 15188 9448 10979 -2016 1259 -2304 N
ATOM 3939 N ILE B 238 6.450 16.885 -3.306 1.00 85.62 N
ANISOU 3939 N ILE B 238 15448 8510 8573 -1746 1917 -2422 N
ATOM 3940 CA ILE B 238 5.596 16.749 -2.134 1.00 85.48 C
ANISOU 3940 CA ILE B 238 15744 8351 8385 -1688 2232 -2475 C
ATOM 3941 C ILE B 238 6.422 16.892 -0.867 1.00 96.51 C
ANISOU 3941 C ILE B 238 17523 9747 9399 -1795 2048 -2598 C
ATOM 3942 O ILE B 238 5.970 17.479 0.124 1.00109.19 O
ANISOU 3942 O ILE B 238 19471 11166 10851 -1804 2264 -2732 O
ATOM 3943 CB ILE B 238 4.819 15.421 -2.171 1.00 72.85 C
ANISOU 3943 CB ILE B 238 14033 6835 6811 -1580 2420 -2312 C
ATOM 3944 CG1 ILE B 238 3.869 15.414 -3.363 1.00 72.23 C
ANISOU 3944 CG1 ILE B 238 13613 6715 7117 -1494 2636 -2200 C
ATOM 3945 CG2 ILE B 238 4.033 15.222 -0.886 1.00 74.28 C
ANISOU 3945 CG2 ILE B 238 14553 6878 6793 -1536 2727 -2358 C
ATOM 3946 CD1 ILE B 238 3.529 14.031 -3.841 1.00 59.77 C
ANISOU 3946 CD1 ILE B 238 11819 5286 5604 -1430 2651 -2019 C
ATOM 3947 N PHE B 239 7.642 16.355 -0.879 1.00 92.06 N
ANISOU 3947 N PHE B 239 16914 9387 8679 -1885 1654 -2553 N
ATOM 3948 CA PHE B 239 8.520 16.465 0.280 1.00 89.83 C
ANISOU 3948 CA PHE B 239 16982 9114 8037 -2015 1431 -2649 C
ATOM 3949 C PHE B 239 8.871 17.918 0.591 1.00 97.64 C
ANISOU 3949 C PHE B 239 18184 9925 8990 -2130 1367 -2839 C
ATOM 3950 O PHE B 239 8.852 18.330 1.757 1.00113.90 O
ANISOU 3950 O PHE B 239 20653 11853 10771 -2200 1429 -2974 O
ATOM 3951 CB PHE B 239 9.780 15.644 0.029 1.00 86.78 C
ANISOU 3951 CB PHE B 239 16434 8973 7563 -2088 1013 -2539 C
ATOM 3952 CG PHE B 239 10.889 15.923 0.988 1.00 98.69 C
ANISOU 3952 CG PHE B 239 18237 10501 8760 -2259 697 -2619 C
ATOM 3953 CD1 PHE B 239 10.959 15.243 2.188 1.00 98.21 C
ANISOU 3953 CD1 PHE B 239 18500 10457 8359 -2295 684 -2611 C
ATOM 3954 CD2 PHE B 239 11.870 16.857 0.681 1.00104.28 C
ANISOU 3954 CD2 PHE B 239 18897 11204 9519 -2400 397 -2689 C
ATOM 3955 CE1 PHE B 239 11.983 15.488 3.075 1.00 99.34 C
ANISOU 3955 CE1 PHE B 239 18927 10613 8204 -2475 370 -2670 C
ATOM 3956 CE2 PHE B 239 12.898 17.112 1.561 1.00106.39 C
ANISOU 3956 CE2 PHE B 239 19432 11483 9508 -2579 83 -2746 C
ATOM 3957 CZ PHE B 239 12.957 16.425 2.764 1.00105.95 C
ANISOU 3957 CZ PHE B 239 19710 11446 9099 -2620 63 -2735 C
ATOM 3958 N ARG B 240 9.192 18.715 -0.433 1.00 92.04 N
ANISOU 3958 N ARG B 240 17218 9197 8556 -2159 1240 -2855 N
ATOM 3959 CA ARG B 240 9.537 20.112 -0.181 1.00 96.69 C
ANISOU 3959 CA ARG B 240 17998 9598 9141 -2272 1162 -3035 C
ATOM 3960 C ARG B 240 8.332 20.915 0.301 1.00 98.19 C
ANISOU 3960 C ARG B 240 18426 9505 9378 -2189 1592 -3176 C
ATOM 3961 O ARG B 240 8.500 21.925 0.995 1.00108.03 O
ANISOU 3961 O ARG B 240 19988 10561 10498 -2279 1592 -3362 O
ATOM 3962 CB ARG B 240 10.166 20.736 -1.426 1.00 98.73 C
ANISOU 3962 CB ARG B 240 17909 9898 9707 -2328 918 -3001 C
ATOM 3963 CG ARG B 240 11.637 20.370 -1.571 1.00 99.52 C
ANISOU 3963 CG ARG B 240 17892 10217 9706 -2473 451 -2927 C
ATOM 3964 CD ARG B 240 12.347 21.157 -2.656 1.00105.68 C
ANISOU 3964 CD ARG B 240 18376 11010 10768 -2563 205 -2909 C
ATOM 3965 NE ARG B 240 12.496 22.575 -2.332 1.00118.03 N
ANISOU 3965 NE ARG B 240 20146 12339 12363 -2675 162 -3085 N
ATOM 3966 CZ ARG B 240 13.550 23.094 -1.706 1.00131.25 C
ANISOU 3966 CZ ARG B 240 22011 14000 13858 -2863 -153 -3165 C
ATOM 3967 NH1 ARG B 240 14.551 22.308 -1.333 1.00129.85 N
ANISOU 3967 NH1 ARG B 240 21835 14036 13468 -2959 -455 -3070 N
ATOM 3968 NH2 ARG B 240 13.611 24.398 -1.461 1.00144.07 N
ANISOU 3968 NH2 ARG B 240 23821 15386 15532 -2963 -175 -3332 N
ATOM 3969 N LYS B 241 7.120 20.492 -0.062 1.00 90.41 N
ANISOU 3969 N LYS B 241 17290 8477 8585 -2022 1965 -3090 N
ATOM 3970 CA LYS B 241 5.913 21.158 0.419 1.00 88.84 C
ANISOU 3970 CA LYS B 241 17292 8008 8456 -1926 2417 -3200 C
ATOM 3971 C LYS B 241 5.643 20.822 1.881 1.00101.16 C
ANISOU 3971 C LYS B 241 19297 9504 9634 -1940 2598 -3284 C
ATOM 3972 O LYS B 241 5.573 21.711 2.738 1.00124.60 O
ANISOU 3972 O LYS B 241 22637 12265 12440 -1995 2714 -3479 O
ATOM 3973 CB LYS B 241 4.721 20.758 -0.458 1.00 81.66 C
ANISOU 3973 CB LYS B 241 16051 7080 7898 -1759 2746 -3049 C
ATOM 3974 CG LYS B 241 3.472 21.627 -0.305 1.00 84.69 C
ANISOU 3974 CG LYS B 241 16515 7163 8498 -1648 3212 -3135 C
ATOM 3975 CD LYS B 241 3.514 22.930 -1.076 1.00 97.00 C
ANISOU 3975 CD LYS B 241 17935 8542 10377 -1659 3175 -3220 C
ATOM 3976 CE LYS B 241 2.121 23.541 -1.107 1.00111.56 C
ANISOU 3976 CE LYS B 241 19755 10109 12524 -1509 3677 -3239 C
ATOM 3977 NZ LYS B 241 2.000 24.620 -2.116 1.00114.32 N
ANISOU 3977 NZ LYS B 241 19858 10294 13286 -1490 3652 -3252 N
ATOM 3978 N LEU B 242 5.506 19.530 2.182 1.00 92.64 N
ANISOU 3978 N LEU B 242 18199 8595 8404 -1899 2618 -3141 N
ATOM 3979 CA LEU B 242 5.102 19.084 3.511 1.00 96.28 C
ANISOU 3979 CA LEU B 242 19061 8996 8528 -1901 2830 -3189 C
ATOM 3980 C LEU B 242 6.126 19.385 4.594 1.00111.83 C
ANISOU 3980 C LEU B 242 21450 10965 10077 -2083 2551 -3332 C
ATOM 3981 O LEU B 242 5.753 19.452 5.772 1.00127.71 O
ANISOU 3981 O LEU B 242 23884 12846 11793 -2111 2765 -3439 O
ATOM 3982 CB LEU B 242 4.808 17.587 3.490 1.00 93.31 C
ANISOU 3982 CB LEU B 242 18534 8803 8115 -1825 2862 -2987 C
ATOM 3983 CG LEU B 242 3.727 17.148 2.499 1.00 93.38 C
ANISOU 3983 CG LEU B 242 18154 8811 8516 -1662 3142 -2830 C
ATOM 3984 CD1 LEU B 242 3.431 15.657 2.606 1.00 86.17 C
ANISOU 3984 CD1 LEU B 242 17146 8054 7543 -1600 3171 -2647 C
ATOM 3985 CD2 LEU B 242 2.466 17.967 2.707 1.00103.20 C
ANISOU 3985 CD2 LEU B 242 19497 9776 9937 -1565 3634 -2914 C
ATOM 3986 N TRP B 243 7.399 19.552 4.240 1.00108.28 N
ANISOU 3986 N TRP B 243 20901 10651 9589 -2218 2083 -3328 N
ATOM 3987 CA TRP B 243 8.466 19.704 5.230 1.00112.76 C
ANISOU 3987 CA TRP B 243 21837 11244 9762 -2416 1758 -3423 C
ATOM 3988 C TRP B 243 9.155 21.064 5.198 1.00116.02 C
ANISOU 3988 C TRP B 243 22376 11518 10189 -2560 1550 -3602 C
ATOM 3989 O TRP B 243 9.094 21.796 6.183 1.00128.56 O
ANISOU 3989 O TRP B 243 24410 12913 11524 -2653 1643 -3791 O
ATOM 3990 CB TRP B 243 9.500 18.579 5.033 1.00 96.19 C
ANISOU 3990 CB TRP B 243 19545 9432 7569 -2480 1344 -3241 C
ATOM 3991 CG TRP B 243 9.115 17.306 5.717 1.00106.82 C
ANISOU 3991 CG TRP B 243 21013 10874 8699 -2423 1464 -3124 C
ATOM 3992 CD1 TRP B 243 9.360 16.973 7.019 1.00113.10 C
ANISOU 3992 CD1 TRP B 243 22248 11654 9072 -2534 1411 -3166 C
ATOM 3993 CD2 TRP B 243 8.382 16.209 5.156 1.00103.31 C
ANISOU 3993 CD2 TRP B 243 20267 10537 8447 -2251 1659 -2948 C
ATOM 3994 NE1 TRP B 243 8.852 15.727 7.295 1.00 99.68 N
ANISOU 3994 NE1 TRP B 243 20527 10050 7298 -2438 1555 -3022 N
ATOM 3995 CE2 TRP B 243 8.244 15.238 6.169 1.00105.67 C
ANISOU 3995 CE2 TRP B 243 20832 10881 8436 -2263 1709 -2890 C
ATOM 3996 CE3 TRP B 243 7.839 15.947 3.893 1.00 95.18 C
ANISOU 3996 CE3 TRP B 243 18782 9566 7817 -2102 1782 -2831 C
ATOM 3997 CZ2 TRP B 243 7.584 14.025 5.957 1.00104.45 C
ANISOU 3997 CZ2 TRP B 243 20490 10820 8375 -2125 1878 -2724 C
ATOM 3998 CZ3 TRP B 243 7.185 14.740 3.686 1.00 90.79 C
ANISOU 3998 CZ3 TRP B 243 18050 9104 7342 -1974 1945 -2668 C
ATOM 3999 CH2 TRP B 243 7.063 13.796 4.711 1.00 86.18 C
ANISOU 3999 CH2 TRP B 243 17727 8556 6462 -1983 1992 -2617 C
ATOM 4000 N GLY B 244 9.805 21.429 4.096 1.00113.51 N
ANISOU 4000 N GLY B 244 21690 11282 10158 -2589 1276 -3550 N
ATOM 4001 CA GLY B 244 10.620 22.635 4.059 1.00125.42 C
ANISOU 4001 CA GLY B 244 23297 12676 11682 -2753 1009 -3696 C
ATOM 4002 C GLY B 244 9.916 23.922 4.446 1.00140.61 C
ANISOU 4002 C GLY B 244 25510 14273 13643 -2741 1308 -3928 C
ATOM 4003 O GLY B 244 10.265 24.543 5.455 1.00146.32 O
ANISOU 4003 O GLY B 244 26676 14853 14066 -2889 1242 -4105 O
ATOM 4004 N ARG B 245 8.924 24.338 3.660 1.00145.20 N
ANISOU 4004 N ARG B 245 25855 14722 14592 -2570 1639 -3930 N
ATOM 4005 CA ARG B 245 8.240 25.596 3.921 1.00148.16 C
ANISOU 4005 CA ARG B 245 26459 14765 15069 -2536 1936 -4144 C
ATOM 4006 C ARG B 245 7.456 25.539 5.226 1.00137.23 C
ANISOU 4006 C ARG B 245 25555 13220 13366 -2500 2320 -4276 C
ATOM 4007 O ARG B 245 6.877 24.510 5.581 1.00134.29 O
ANISOU 4007 O ARG B 245 25198 12956 12869 -2405 2535 -4161 O
ATOM 4008 CB ARG B 245 7.318 25.941 2.758 1.00153.36 C
ANISOU 4008 CB ARG B 245 26725 15325 16221 -2354 2203 -4075 C
ATOM 4009 CG ARG B 245 6.527 24.766 2.221 1.00150.36 C
ANISOU 4009 CG ARG B 245 26029 15117 15984 -2182 2426 -3853 C
ATOM 4010 CD ARG B 245 6.320 24.886 0.721 1.00146.71 C
ANISOU 4010 CD ARG B 245 25058 14697 15988 -2097 2389 -3711 C
ATOM 4011 NE ARG B 245 7.593 24.916 0.007 1.00146.27 N
ANISOU 4011 NE ARG B 245 24776 14821 15979 -2239 1891 -3648 N
ATOM 4012 CZ ARG B 245 7.709 25.020 -1.313 1.00142.45 C
ANISOU 4012 CZ ARG B 245 23869 14404 15853 -2216 1761 -3522 C
ATOM 4013 NH1 ARG B 245 6.624 25.107 -2.067 1.00137.23 N
ANISOU 4013 NH1 ARG B 245 22967 13641 15531 -2061 2074 -3442 N
ATOM 4014 NH2 ARG B 245 8.908 25.038 -1.880 1.00141.58 N
ANISOU 4014 NH2 ARG B 245 23571 14457 15768 -2356 1324 -3463 N
ATOM 4015 N GLN B 246 7.448 26.670 5.948 1.00132.63 N
ANISOU 4015 N GLN B 246 25378 12363 12653 -2583 2410 -4526 N
ATOM 4016 CA GLN B 246 6.802 26.799 7.257 1.00141.07 C
ANISOU 4016 CA GLN B 246 26973 13243 13383 -2579 2772 -4695 C
ATOM 4017 C GLN B 246 5.924 28.051 7.233 1.00147.44 C
ANISOU 4017 C GLN B 246 27901 13687 14432 -2474 3171 -4898 C
ATOM 4018 O GLN B 246 6.239 29.068 7.860 1.00150.58 O
ANISOU 4018 O GLN B 246 28687 13856 14670 -2596 3135 -5140 O
ATOM 4019 CB GLN B 246 7.846 26.862 8.376 1.00147.71 C
ANISOU 4019 CB GLN B 246 28292 14111 13718 -2831 2435 -4815 C
ATOM 4020 CG GLN B 246 8.818 25.689 8.399 1.00148.79 C
ANISOU 4020 CG GLN B 246 28299 14588 13645 -2944 2001 -4606 C
ATOM 4021 CD GLN B 246 8.229 24.449 9.046 1.00153.40 C
ANISOU 4021 CD GLN B 246 28995 15297 13992 -2860 2235 -4481 C
ATOM 4022 OE1 GLN B 246 7.692 24.509 10.152 1.00164.69 O
ANISOU 4022 OE1 GLN B 246 30890 16577 15109 -2875 2529 -4611 O
ATOM 4023 NE2 GLN B 246 8.323 23.318 8.356 1.00144.98 N
ANISOU 4023 NE2 GLN B 246 27512 14498 13078 -2773 2111 -4232 N
ATOM 4024 N ILE B 247 4.808 27.956 6.518 1.00144.52 N
ANISOU 4024 N ILE B 247 27200 13254 14457 -2249 3557 -4793 N
ATOM 4025 CA ILE B 247 4.070 29.170 6.150 1.00140.70 C
ANISOU 4025 CA ILE B 247 26681 12439 14340 -2133 3867 -4934 C
ATOM 4026 C ILE B 247 3.619 29.888 7.416 1.00143.09 C
ANISOU 4026 C ILE B 247 27564 12438 14367 -2151 4220 -5206 C
ATOM 4027 O ILE B 247 2.989 29.264 8.295 1.00144.39 O
ANISOU 4027 O ILE B 247 27989 12607 14266 -2099 4558 -5204 O
ATOM 4028 CB ILE B 247 2.883 28.820 5.234 1.00137.65 C
ANISOU 4028 CB ILE B 247 25839 12046 14417 -1893 4239 -4738 C
ATOM 4029 CG1 ILE B 247 2.299 30.093 4.617 1.00137.52 C
ANISOU 4029 CG1 ILE B 247 25687 11705 14860 -1783 4455 -4838 C
ATOM 4030 CG2 ILE B 247 1.826 28.037 6.000 1.00139.44 C
ANISOU 4030 CG2 ILE B 247 26223 12264 14493 -1768 4724 -4683 C
ATOM 4031 CD1 ILE B 247 1.363 29.823 3.455 1.00129.58 C
ANISOU 4031 CD1 ILE B 247 24147 10718 14371 -1588 4683 -4606 C
ATOM 4032 N PRO B 248 3.913 31.177 7.564 1.00150.02 N
ANISOU 4032 N PRO B 248 28671 13038 15290 -2228 4163 -5447 N
ATOM 4033 CA PRO B 248 3.722 31.834 8.859 1.00161.94 C
ANISOU 4033 CA PRO B 248 30807 14276 16447 -2294 4421 -5734 C
ATOM 4034 C PRO B 248 2.268 31.851 9.297 1.00152.13 C
ANISOU 4034 C PRO B 248 29680 12816 15307 -2072 5117 -5774 C
ATOM 4035 O PRO B 248 1.356 31.962 8.482 1.00149.56 O
ANISOU 4035 O PRO B 248 28955 12404 15466 -1860 5422 -5654 O
ATOM 4036 CB PRO B 248 4.256 33.254 8.608 1.00151.86 C
ANISOU 4036 CB PRO B 248 29627 12727 15345 -2391 4213 -5954 C
ATOM 4037 CG PRO B 248 4.069 33.462 7.148 1.00150.16 C
ANISOU 4037 CG PRO B 248 28799 12533 15720 -2259 4128 -5777 C
ATOM 4038 CD PRO B 248 4.331 32.125 6.517 1.00145.07 C
ANISOU 4038 CD PRO B 248 27740 12301 15080 -2245 3900 -5467 C
ATOM 4039 N GLY B 249 2.065 31.726 10.606 1.00158.20 N
ANISOU 4039 N GLY B 249 30999 13494 15614 -2133 5367 -5931 N
ATOM 4040 CA GLY B 249 0.733 31.858 11.173 1.00166.68 C
ANISOU 4040 CA GLY B 249 32258 14321 16751 -1943 6057 -6005 C
ATOM 4041 C GLY B 249 -0.260 30.835 10.674 1.00158.07 C
ANISOU 4041 C GLY B 249 30735 13386 15940 -1736 6378 -5716 C
ATOM 4042 O GLY B 249 -1.449 31.149 10.561 1.00160.02 O
ANISOU 4042 O GLY B 249 30869 13407 16525 -1527 6925 -5709 O
ATOM 4043 N THR B 250 0.191 29.617 10.367 1.00152.19 N
ANISOU 4043 N THR B 250 29736 13008 15082 -1790 6054 -5470 N
ATOM 4044 CA THR B 250 -0.721 28.597 9.869 1.00147.70 C
ANISOU 4044 CA THR B 250 28756 12585 14778 -1612 6325 -5190 C
ATOM 4045 C THR B 250 -1.690 28.164 10.966 1.00154.85 C
ANISOU 4045 C THR B 250 30006 13374 15457 -1534 6874 -5223 C
ATOM 4046 O THR B 250 -1.333 28.104 12.146 1.00167.27 O
ANISOU 4046 O THR B 250 32126 14918 16511 -1674 6872 -5388 O
ATOM 4047 CB THR B 250 0.064 27.395 9.336 1.00140.72 C
ANISOU 4047 CB THR B 250 27561 12104 13801 -1698 5831 -4943 C
ATOM 4048 OG1 THR B 250 -0.837 26.468 8.717 1.00143.91 O
ANISOU 4048 OG1 THR B 250 27533 12629 14517 -1527 6074 -4674 O
ATOM 4049 CG2 THR B 250 0.822 26.685 10.457 1.00143.11 C
ANISOU 4049 CG2 THR B 250 28307 12572 13496 -1887 5592 -4987 C
ATOM 4050 N THR B 251 -2.923 27.857 10.566 1.00152.00 N
ANISOU 4050 N THR B 251 29321 12940 15493 -1321 7343 -5056 N
ATOM 4051 CA THR B 251 -4.018 27.669 11.508 1.00157.55 C
ANISOU 4051 CA THR B 251 30306 13456 16098 -1214 7960 -5096 C
ATOM 4052 C THR B 251 -3.898 26.336 12.239 1.00156.51 C
ANISOU 4052 C THR B 251 30354 13567 15545 -1294 7894 -4970 C
ATOM 4053 O THR B 251 -3.217 25.406 11.798 1.00150.61 O
ANISOU 4053 O THR B 251 29369 13139 14718 -1374 7440 -4783 O
ATOM 4054 CB THR B 251 -5.371 27.767 10.806 1.00156.22 C
ANISOU 4054 CB THR B 251 29691 13125 16541 -966 8468 -4929 C
ATOM 4055 OG1 THR B 251 -5.525 26.684 9.883 1.00148.79 O
ANISOU 4055 OG1 THR B 251 28214 12460 15860 -914 8288 -4603 O
ATOM 4056 CG2 THR B 251 -5.484 29.089 10.067 1.00157.05 C
ANISOU 4056 CG2 THR B 251 29604 12978 17088 -884 8518 -5040 C
ATOM 4057 N SER B 252 -4.579 26.258 13.383 1.00163.04 N
ANISOU 4057 N SER B 252 31616 14224 16108 -1267 8371 -5077 N
ATOM 4058 CA SER B 252 -4.568 25.036 14.179 1.00163.42 C
ANISOU 4058 CA SER B 252 31878 14461 15752 -1336 8366 -4969 C
ATOM 4059 C SER B 252 -5.045 23.831 13.373 1.00176.95 C
ANISOU 4059 C SER B 252 33038 16402 17793 -1222 8334 -4625 C
ATOM 4060 O SER B 252 -4.546 22.715 13.563 1.00174.56 O
ANISOU 4060 O SER B 252 32739 16368 17219 -1315 8023 -4484 O
ATOM 4061 CB SER B 252 -5.445 25.228 15.418 1.00172.08 C
ANISOU 4061 CB SER B 252 33479 15295 16607 -1288 8987 -5128 C
ATOM 4062 OG SER B 252 -5.678 23.999 16.074 1.00172.04 O
ANISOU 4062 OG SER B 252 33601 15451 16314 -1314 9065 -4984 O
ATOM 4063 N ALA B 253 -6.023 24.028 12.486 1.00171.08 N
ANISOU 4063 N ALA B 253 31821 15543 17639 -1025 8654 -4482 N
ATOM 4064 CA ALA B 253 -6.463 22.935 11.624 1.00154.48 C
ANISOU 4064 CA ALA B 253 29179 13643 15874 -931 8594 -4157 C
ATOM 4065 C ALA B 253 -5.436 22.597 10.548 1.00151.51 C
ANISOU 4065 C ALA B 253 28425 13560 15584 -1018 7952 -4031 C
ATOM 4066 O ALA B 253 -5.332 21.433 10.146 1.00151.81 O
ANISOU 4066 O ALA B 253 28190 13846 15645 -1023 7730 -3804 O
ATOM 4067 CB ALA B 253 -7.805 23.277 10.980 1.00149.97 C
ANISOU 4067 CB ALA B 253 28211 12849 15923 -714 9110 -4028 C
ATOM 4068 N GLU B 286 -4.671 23.586 10.077 1.00152.48 N
ANISOU 4068 N GLU B 286 28530 13647 15757 -1086 7654 -4177 N
ATOM 4069 CA GLU B 286 -3.732 23.342 8.986 1.00140.84 C
ANISOU 4069 CA GLU B 286 26675 12432 14407 -1157 7080 -4057 C
ATOM 4070 C GLU B 286 -2.643 22.361 9.399 1.00131.19 C
ANISOU 4070 C GLU B 286 25614 11510 12723 -1324 6595 -4011 C
ATOM 4071 O GLU B 286 -2.350 21.401 8.677 1.00124.16 O
ANISOU 4071 O GLU B 286 24360 10878 11938 -1324 6301 -3793 O
ATOM 4072 CB GLU B 286 -3.079 24.655 8.543 1.00150.44 C
ANISOU 4072 CB GLU B 286 27904 13524 15731 -1212 6860 -4247 C
ATOM 4073 CG GLU B 286 -3.970 25.731 7.927 1.00163.03 C
ANISOU 4073 CG GLU B 286 29273 14827 17845 -1052 7238 -4286 C
ATOM 4074 CD GLU B 286 -4.733 25.262 6.707 1.00168.22 C
ANISOU 4074 CD GLU B 286 29314 15554 19049 -906 7340 -4001 C
ATOM 4075 OE1 GLU B 286 -4.121 24.610 5.836 1.00165.81 O
ANISOU 4075 OE1 GLU B 286 28673 15522 18803 -961 6912 -3833 O
ATOM 4076 OE2 GLU B 286 -5.934 25.583 6.596 1.00176.19 O
ANISOU 4076 OE2 GLU B 286 30171 16332 20442 -741 7849 -3943 O
ATOM 4077 N VAL B 287 -2.038 22.580 10.570 1.00140.12 N
ANISOU 4077 N VAL B 287 27297 12601 13342 -1471 6512 -4212 N
ATOM 4078 CA VAL B 287 -0.934 21.728 10.999 1.00142.01 C
ANISOU 4078 CA VAL B 287 27699 13108 13150 -1644 6027 -4166 C
ATOM 4079 C VAL B 287 -1.396 20.312 11.310 1.00143.77 C
ANISOU 4079 C VAL B 287 27862 13489 13276 -1595 6135 -3957 C
ATOM 4080 O VAL B 287 -0.615 19.361 11.194 1.00128.62 O
ANISOU 4080 O VAL B 287 25841 11836 11193 -1680 5716 -3820 O
ATOM 4081 CB VAL B 287 -0.225 22.363 12.211 1.00149.18 C
ANISOU 4081 CB VAL B 287 29240 13909 13533 -1831 5922 -4429 C
ATOM 4082 CG1 VAL B 287 0.977 21.524 12.610 1.00143.75 C
ANISOU 4082 CG1 VAL B 287 28693 13494 12432 -2022 5384 -4360 C
ATOM 4083 CG2 VAL B 287 0.201 23.790 11.887 1.00142.41 C
ANISOU 4083 CG2 VAL B 287 28442 12868 12799 -1879 5817 -4645 C
ATOM 4084 N LYS B 288 -2.655 20.141 11.704 1.00149.45 N
ANISOU 4084 N LYS B 288 28634 14038 14112 -1457 6694 -3924 N
ATOM 4085 CA LYS B 288 -3.187 18.798 11.883 1.00152.21 C
ANISOU 4085 CA LYS B 288 28872 14521 14440 -1396 6810 -3710 C
ATOM 4086 C LYS B 288 -3.248 18.048 10.557 1.00143.56 C
ANISOU 4086 C LYS B 288 27156 13621 13767 -1309 6592 -3450 C
ATOM 4087 O LYS B 288 -3.150 16.817 10.533 1.00144.78 O
ANISOU 4087 O LYS B 288 27187 13975 13847 -1314 6431 -3270 O
ATOM 4088 CB LYS B 288 -4.567 18.879 12.545 1.00162.60 C
ANISOU 4088 CB LYS B 288 30358 15585 15839 -1262 7484 -3733 C
ATOM 4089 CG LYS B 288 -5.082 17.578 13.133 1.00164.89 C
ANISOU 4089 CG LYS B 288 30709 15968 15972 -1232 7644 -3571 C
ATOM 4090 CD LYS B 288 -6.403 17.816 13.853 1.00170.19 C
ANISOU 4090 CD LYS B 288 31586 16364 16715 -1107 8337 -3620 C
ATOM 4091 CE LYS B 288 -6.878 16.567 14.574 1.00172.03 C
ANISOU 4091 CE LYS B 288 31945 16679 16739 -1093 8504 -3482 C
ATOM 4092 NZ LYS B 288 -8.022 16.852 15.484 1.00182.11 N
ANISOU 4092 NZ LYS B 288 33524 17686 17984 -997 9177 -3567 N
ATOM 4093 N GLN B 289 -3.415 18.776 9.452 1.00137.06 N
ANISOU 4093 N GLN B 289 25955 12736 13383 -1233 6589 -3431 N
ATOM 4094 CA GLN B 289 -3.372 18.188 8.118 1.00123.42 C
ANISOU 4094 CA GLN B 289 23663 11193 12038 -1175 6350 -3206 C
ATOM 4095 C GLN B 289 -1.951 17.870 7.665 1.00111.93 C
ANISOU 4095 C GLN B 289 22111 10011 10406 -1310 5719 -3186 C
ATOM 4096 O GLN B 289 -1.708 16.814 7.073 1.00106.03 O
ANISOU 4096 O GLN B 289 21066 9486 9733 -1302 5471 -2993 O
ATOM 4097 CB GLN B 289 -4.033 19.140 7.121 1.00124.60 C
ANISOU 4097 CB GLN B 289 23468 11169 12705 -1060 6570 -3196 C
ATOM 4098 CG GLN B 289 -4.155 18.611 5.701 1.00119.77 C
ANISOU 4098 CG GLN B 289 22281 10712 12515 -1000 6388 -2963 C
ATOM 4099 CD GLN B 289 -4.728 19.649 4.749 1.00126.23 C
ANISOU 4099 CD GLN B 289 22785 11350 13826 -908 6579 -2960 C
ATOM 4100 OE1 GLN B 289 -4.540 20.852 4.940 1.00128.69 O
ANISOU 4100 OE1 GLN B 289 23276 11485 14134 -923 6640 -3158 O
ATOM 4101 NE2 GLN B 289 -5.455 19.190 3.737 1.00127.70 N
ANISOU 4101 NE2 GLN B 289 22509 11562 14449 -814 6678 -2735 N
ATOM 4102 N MET B 290 -1.004 18.772 7.926 1.00113.65 N
ANISOU 4102 N MET B 290 22573 10204 10405 -1435 5459 -3382 N
ATOM 4103 CA MET B 290 0.359 18.576 7.439 1.00111.20 C
ANISOU 4103 CA MET B 290 22139 10134 9980 -1563 4868 -3357 C
ATOM 4104 C MET B 290 1.016 17.341 8.058 1.00115.63 C
ANISOU 4104 C MET B 290 22842 10917 10173 -1652 4587 -3259 C
ATOM 4105 O MET B 290 1.732 16.604 7.368 1.00114.45 O
ANISOU 4105 O MET B 290 22395 11005 10085 -1678 4203 -3113 O
ATOM 4106 CB MET B 290 1.168 19.842 7.704 1.00118.20 C
ANISOU 4106 CB MET B 290 23292 10909 10711 -1688 4675 -3592 C
ATOM 4107 CG MET B 290 2.370 20.044 6.805 1.00129.28 C
ANISOU 4107 CG MET B 290 24430 12488 12201 -1784 4142 -3566 C
ATOM 4108 SD MET B 290 3.359 21.442 7.364 1.00146.45 S
ANISOU 4108 SD MET B 290 27000 14516 14129 -1966 3895 -3848 S
ATOM 4109 CE MET B 290 4.216 21.903 5.863 1.00135.31 C
ANISOU 4109 CE MET B 290 25098 13230 13083 -1995 3463 -3784 C
ATOM 4110 N ARG B 291 0.796 17.098 9.359 1.00124.13 N
ANISOU 4110 N ARG B 291 24379 11915 10868 -1701 4777 -3337 N
ATOM 4111 CA ARG B 291 1.419 15.944 10.014 1.00119.05 C
ANISOU 4111 CA ARG B 291 23899 11469 9866 -1794 4509 -3243 C
ATOM 4112 C ARG B 291 0.901 14.607 9.492 1.00112.28 C
ANISOU 4112 C ARG B 291 22686 10760 9216 -1675 4555 -2996 C
ATOM 4113 O ARG B 291 1.658 13.630 9.449 1.00117.59 O
ANISOU 4113 O ARG B 291 23277 11652 9749 -1732 4193 -2874 O
ATOM 4114 CB ARG B 291 1.213 15.992 11.532 1.00132.66 C
ANISOU 4114 CB ARG B 291 26217 13061 11125 -1878 4733 -3380 C
ATOM 4115 CG ARG B 291 1.989 17.053 12.293 1.00140.17 C
ANISOU 4115 CG ARG B 291 27628 13904 11727 -2054 4576 -3622 C
ATOM 4116 CD ARG B 291 1.460 17.139 13.720 1.00152.14 C
ANISOU 4116 CD ARG B 291 29728 15247 12832 -2106 4934 -3762 C
ATOM 4117 NE ARG B 291 2.153 18.114 14.558 1.00160.64 N
ANISOU 4117 NE ARG B 291 31312 16199 13523 -2293 4801 -4005 N
ATOM 4118 CZ ARG B 291 2.958 17.767 15.559 1.00167.71 C
ANISOU 4118 CZ ARG B 291 32636 17174 13911 -2492 4518 -4042 C
ATOM 4119 NH1 ARG B 291 3.150 16.482 15.830 1.00162.42 N
ANISOU 4119 NH1 ARG B 291 31930 16704 13077 -2514 4355 -3852 N
ATOM 4120 NH2 ARG B 291 3.566 18.690 16.294 1.00180.79 N
ANISOU 4120 NH2 ARG B 291 34765 18704 15224 -2677 4390 -4265 N
ATOM 4121 N ALA B 292 -0.370 14.533 9.097 1.00108.56 N
ANISOU 4121 N ALA B 292 22000 10163 9084 -1515 4989 -2917 N
ATOM 4122 CA ALA B 292 -0.925 13.260 8.648 1.00104.73 C
ANISOU 4122 CA ALA B 292 21205 9795 8793 -1413 5043 -2689 C
ATOM 4123 C ALA B 292 -0.466 12.902 7.241 1.00124.22 C
ANISOU 4123 C ALA B 292 23161 12448 11591 -1381 4710 -2543 C
ATOM 4124 O ALA B 292 -0.136 11.742 6.970 1.00119.46 O
ANISOU 4124 O ALA B 292 22383 12036 10972 -1377 4476 -2388 O
ATOM 4125 CB ALA B 292 -2.450 13.303 8.722 1.00106.65 C
ANISOU 4125 CB ALA B 292 21394 9826 9302 -1266 5618 -2642 C
ATOM 4126 N ARG B 293 -0.423 13.888 6.342 1.00118.50 N
ANISOU 4126 N ARG B 293 22206 11664 11156 -1361 4687 -2597 N
ATOM 4127 CA ARG B 293 0.002 13.628 4.969 1.00105.04 C
ANISOU 4127 CA ARG B 293 20031 10126 9753 -1340 4390 -2470 C
ATOM 4128 C ARG B 293 1.445 13.146 4.915 1.00111.73 C
ANISOU 4128 C ARG B 293 20878 11215 10360 -1455 3858 -2457 C
ATOM 4129 O ARG B 293 1.817 12.390 4.006 1.00114.32 O
ANISOU 4129 O ARG B 293 20861 11727 10850 -1431 3611 -2313 O
ATOM 4130 CB ARG B 293 -0.166 14.891 4.127 1.00 92.57 C
ANISOU 4130 CB ARG B 293 18262 8422 8487 -1315 4466 -2549 C
ATOM 4131 CG ARG B 293 -1.602 15.168 3.736 1.00 89.68 C
ANISOU 4131 CG ARG B 293 17712 7854 8509 -1178 4946 -2483 C
ATOM 4132 CD ARG B 293 -1.781 16.585 3.233 1.00 90.79 C
ANISOU 4132 CD ARG B 293 17780 7816 8899 -1161 5071 -2602 C
ATOM 4133 NE ARG B 293 -2.962 16.740 2.392 1.00 89.42 N
ANISOU 4133 NE ARG B 293 17260 7508 9207 -1036 5408 -2473 N
ATOM 4134 CZ ARG B 293 -3.386 17.910 1.928 1.00 90.70 C
ANISOU 4134 CZ ARG B 293 17315 7477 9669 -989 5602 -2542 C
ATOM 4135 NH1 ARG B 293 -2.732 19.023 2.242 1.00 93.38 N
ANISOU 4135 NH1 ARG B 293 17886 7729 9864 -1055 5492 -2754 N
ATOM 4136 NH2 ARG B 293 -4.473 17.972 1.172 1.00 91.89 N
ANISOU 4136 NH2 ARG B 293 17129 7507 10280 -881 5903 -2396 N
ATOM 4137 N ARG B 294 2.270 13.580 5.866 1.00109.80 N
ANISOU 4137 N ARG B 294 21018 10964 9738 -1584 3680 -2605 N
ATOM 4138 CA ARG B 294 3.642 13.095 5.929 1.00103.53 C
ANISOU 4138 CA ARG B 294 20239 10383 8714 -1702 3181 -2577 C
ATOM 4139 C ARG B 294 3.687 11.601 6.229 1.00108.27 C
ANISOU 4139 C ARG B 294 20817 11138 9183 -1677 3095 -2413 C
ATOM 4140 O ARG B 294 4.499 10.867 5.649 1.00117.72 O
ANISOU 4140 O ARG B 294 21772 12536 10420 -1692 2746 -2299 O
ATOM 4141 CB ARG B 294 4.401 13.864 7.005 1.00102.00 C
ANISOU 4141 CB ARG B 294 20506 10120 8130 -1863 3034 -2763 C
ATOM 4142 CG ARG B 294 4.620 15.332 6.711 1.00103.19 C
ANISOU 4142 CG ARG B 294 20693 10131 8384 -1913 3022 -2938 C
ATOM 4143 CD ARG B 294 4.865 16.074 8.022 1.00108.28 C
ANISOU 4143 CD ARG B 294 21894 10621 8627 -2049 3062 -3142 C
ATOM 4144 NE ARG B 294 5.172 17.486 7.821 1.00105.71 N
ANISOU 4144 NE ARG B 294 21643 10148 8373 -2115 3015 -3327 N
ATOM 4145 CZ ARG B 294 6.013 18.186 8.577 1.00110.12 C
ANISOU 4145 CZ ARG B 294 22578 10648 8615 -2294 2785 -3491 C
ATOM 4146 NH1 ARG B 294 6.649 17.606 9.587 1.00113.17 N
ANISOU 4146 NH1 ARG B 294 23301 11118 8579 -2433 2572 -3484 N
ATOM 4147 NH2 ARG B 294 6.236 19.465 8.310 1.00111.67 N
ANISOU 4147 NH2 ARG B 294 22815 10695 8921 -2345 2750 -3658 N
ATOM 4148 N LYS B 295 2.815 11.130 7.129 1.00101.04 N
ANISOU 4148 N LYS B 295 20153 10120 8117 -1636 3424 -2399 N
ATOM 4149 CA LYS B 295 2.784 9.713 7.475 1.00102.27 C
ANISOU 4149 CA LYS B 295 20313 10400 8145 -1612 3365 -2245 C
ATOM 4150 C LYS B 295 2.329 8.855 6.302 1.00 90.01 C
ANISOU 4150 C LYS B 295 18285 8942 6975 -1483 3380 -2063 C
ATOM 4151 O LYS B 295 2.789 7.716 6.154 1.00 83.60 O
ANISOU 4151 O LYS B 295 17353 8295 6117 -1477 3147 -1932 O
ATOM 4152 CB LYS B 295 1.881 9.497 8.691 1.00106.70 C
ANISOU 4152 CB LYS B 295 21258 10813 8469 -1600 3749 -2279 C
ATOM 4153 CG LYS B 295 2.555 9.876 9.999 1.00108.60 C
ANISOU 4153 CG LYS B 295 22025 11022 8217 -1761 3634 -2422 C
ATOM 4154 CD LYS B 295 1.821 9.362 11.221 1.00116.56 C
ANISOU 4154 CD LYS B 295 23420 11936 8931 -1763 3955 -2424 C
ATOM 4155 CE LYS B 295 2.512 9.827 12.493 1.00122.18 C
ANISOU 4155 CE LYS B 295 24685 12609 9131 -1947 3828 -2577 C
ATOM 4156 NZ LYS B 295 1.828 9.302 13.703 1.00120.53 N
ANISOU 4156 NZ LYS B 295 24878 12319 8600 -1961 4140 -2578 N
ATOM 4157 N THR B 296 1.430 9.375 5.466 1.00 83.97 N
ANISOU 4157 N THR B 296 17258 8064 6585 -1385 3647 -2050 N
ATOM 4158 CA THR B 296 1.082 8.682 4.230 1.00 89.10 C
ANISOU 4158 CA THR B 296 17454 8800 7601 -1289 3618 -1887 C
ATOM 4159 C THR B 296 2.177 8.854 3.184 1.00 74.69 C
ANISOU 4159 C THR B 296 15344 7146 5888 -1333 3213 -1877 C
ATOM 4160 O THR B 296 2.547 7.891 2.501 1.00 75.22 O
ANISOU 4160 O THR B 296 15155 7375 6052 -1304 2998 -1750 O
ATOM 4161 CB THR B 296 -0.256 9.187 3.687 1.00 93.46 C
ANISOU 4161 CB THR B 296 17826 9164 8521 -1187 4032 -1860 C
ATOM 4162 OG1 THR B 296 -1.213 9.270 4.754 1.00 97.38 O
ANISOU 4162 OG1 THR B 296 18623 9474 8902 -1152 4439 -1900 O
ATOM 4163 CG2 THR B 296 -0.787 8.249 2.611 1.00 92.25 C
ANISOU 4163 CG2 THR B 296 17272 9079 8700 -1102 4036 -1673 C
ATOM 4164 N ALA B 297 2.701 10.075 3.042 1.00 75.62 N
ANISOU 4164 N ALA B 297 15510 7221 6000 -1400 3115 -2014 N
ATOM 4165 CA ALA B 297 3.793 10.308 2.100 1.00 72.31 C
ANISOU 4165 CA ALA B 297 14838 6959 5675 -1452 2734 -2013 C
ATOM 4166 C ALA B 297 5.010 9.460 2.454 1.00 84.14 C
ANISOU 4166 C ALA B 297 16401 8653 6914 -1523 2342 -1968 C
ATOM 4167 O ALA B 297 5.640 8.864 1.574 1.00100.43 O
ANISOU 4167 O ALA B 297 18166 10885 9107 -1508 2087 -1873 O
ATOM 4168 CB ALA B 297 4.156 11.793 2.057 1.00 74.17 C
ANISOU 4168 CB ALA B 297 15170 7093 5918 -1526 2698 -2180 C
ATOM 4169 N LYS B 298 5.365 9.404 3.742 1.00 88.67 N
ANISOU 4169 N LYS B 298 17372 9200 7117 -1607 2292 -2035 N
ATOM 4170 CA LYS B 298 6.483 8.565 4.166 1.00 90.77 C
ANISOU 4170 CA LYS B 298 17720 9638 7131 -1683 1924 -1973 C
ATOM 4171 C LYS B 298 6.246 7.111 3.794 1.00 83.20 C
ANISOU 4171 C LYS B 298 16549 8794 6268 -1584 1919 -1797 C
ATOM 4172 O LYS B 298 7.125 6.444 3.233 1.00 74.01 O
ANISOU 4172 O LYS B 298 15175 7801 5145 -1587 1610 -1710 O
ATOM 4173 CB LYS B 298 6.696 8.691 5.672 1.00100.00 C
ANISOU 4173 CB LYS B 298 19387 10736 7872 -1798 1919 -2059 C
ATOM 4174 CG LYS B 298 7.884 7.890 6.179 1.00101.16 C
ANISOU 4174 CG LYS B 298 19645 11048 7745 -1898 1514 -1983 C
ATOM 4175 CD LYS B 298 7.963 7.849 7.696 1.00109.34 C
ANISOU 4175 CD LYS B 298 21194 12013 8336 -2018 1525 -2040 C
ATOM 4176 CE LYS B 298 9.149 7.017 8.162 1.00107.67 C
ANISOU 4176 CE LYS B 298 21076 11966 7869 -2127 1095 -1934 C
ATOM 4177 NZ LYS B 298 9.155 6.905 9.644 1.00103.80 N
ANISOU 4177 NZ LYS B 298 21102 11410 6929 -2254 1108 -1971 N
ATOM 4178 N MET B 299 5.063 6.598 4.130 1.00 86.28 N
ANISOU 4178 N MET B 299 17006 9081 6695 -1498 2265 -1744 N
ATOM 4179 CA MET B 299 4.754 5.204 3.851 1.00 82.34 C
ANISOU 4179 CA MET B 299 16340 8666 6280 -1410 2277 -1582 C
ATOM 4180 C MET B 299 4.806 4.926 2.358 1.00 83.80 C
ANISOU 4180 C MET B 299 16067 8945 6827 -1334 2184 -1498 C
ATOM 4181 O MET B 299 5.320 3.886 1.928 1.00 92.25 O
ANISOU 4181 O MET B 299 16972 10156 7925 -1304 1979 -1391 O
ATOM 4182 CB MET B 299 3.382 4.864 4.425 1.00 80.55 C
ANISOU 4182 CB MET B 299 16252 8286 6067 -1338 2695 -1548 C
ATOM 4183 CG MET B 299 2.920 3.456 4.131 1.00 77.57 C
ANISOU 4183 CG MET B 299 15708 7965 5800 -1248 2739 -1382 C
ATOM 4184 SD MET B 299 1.192 3.228 4.528 1.00 79.03 S
ANISOU 4184 SD MET B 299 15965 7951 6113 -1156 3257 -1335 S
ATOM 4185 CE MET B 299 0.397 4.039 3.155 1.00 91.99 C
ANISOU 4185 CE MET B 299 17218 9497 8236 -1084 3440 -1335 C
ATOM 4186 N LEU B 300 4.261 5.840 1.552 1.00 79.11 N
ANISOU 4186 N LEU B 300 15281 8267 6509 -1305 2343 -1545 N
ATOM 4187 CA LEU B 300 4.211 5.625 0.110 1.00 63.49 C
ANISOU 4187 CA LEU B 300 12891 6367 4865 -1248 2278 -1466 C
ATOM 4188 C LEU B 300 5.607 5.683 -0.495 1.00 61.45 C
ANISOU 4188 C LEU B 300 12477 6289 4583 -1303 1884 -1480 C
ATOM 4189 O LEU B 300 5.955 4.860 -1.351 1.00 72.68 O
ANISOU 4189 O LEU B 300 13639 7839 6135 -1260 1735 -1387 O
ATOM 4190 CB LEU B 300 3.309 6.674 -0.542 1.00 59.76 C
ANISOU 4190 CB LEU B 300 12283 5751 4672 -1224 2538 -1507 C
ATOM 4191 CG LEU B 300 1.854 6.673 -0.083 1.00 71.46 C
ANISOU 4191 CG LEU B 300 13868 7036 6248 -1159 2963 -1480 C
ATOM 4192 CD1 LEU B 300 1.113 7.898 -0.619 1.00 61.90 C
ANISOU 4192 CD1 LEU B 300 12557 5666 5295 -1148 3206 -1535 C
ATOM 4193 CD2 LEU B 300 1.166 5.387 -0.487 1.00 59.54 C
ANISOU 4193 CD2 LEU B 300 12182 5548 4892 -1081 3050 -1323 C
ATOM 4194 N MET B 301 6.419 6.655 -0.067 1.00 63.48 N
ANISOU 4194 N MET B 301 12895 6545 4677 -1402 1718 -1600 N
ATOM 4195 CA MET B 301 7.762 6.787 -0.625 1.00 59.24 C
ANISOU 4195 CA MET B 301 12207 6167 4135 -1466 1346 -1612 C
ATOM 4196 C MET B 301 8.620 5.560 -0.347 1.00 63.40 C
ANISOU 4196 C MET B 301 12746 6847 4495 -1468 1088 -1519 C
ATOM 4197 O MET B 301 9.422 5.160 -1.198 1.00 63.01 O
ANISOU 4197 O MET B 301 12444 6942 4555 -1459 860 -1467 O
ATOM 4198 CB MET B 301 8.439 8.051 -0.088 1.00 64.42 C
ANISOU 4198 CB MET B 301 13071 6771 4636 -1591 1211 -1756 C
ATOM 4199 CG MET B 301 7.667 9.318 -0.364 1.00 68.07 C
ANISOU 4199 CG MET B 301 13534 7066 5261 -1589 1457 -1857 C
ATOM 4200 SD MET B 301 8.304 10.753 0.511 1.00 85.10 S
ANISOU 4200 SD MET B 301 16027 9113 7194 -1739 1343 -2046 S
ATOM 4201 CE MET B 301 6.892 11.840 0.340 1.00 91.70 C
ANISOU 4201 CE MET B 301 16896 9707 8239 -1673 1788 -2135 C
ATOM 4202 N VAL B 302 8.504 4.977 0.851 1.00 71.20 N
ANISOU 4202 N VAL B 302 14042 7801 5209 -1486 1119 -1496 N
ATOM 4203 CA VAL B 302 9.207 3.726 1.125 1.00 73.06 C
ANISOU 4203 CA VAL B 302 14301 8165 5294 -1480 893 -1385 C
ATOM 4204 C VAL B 302 8.729 2.636 0.174 1.00 78.67 C
ANISOU 4204 C VAL B 302 14719 8928 6244 -1351 987 -1267 C
ATOM 4205 O VAL B 302 9.520 1.816 -0.315 1.00 82.31 O
ANISOU 4205 O VAL B 302 15026 9523 6726 -1328 761 -1190 O
ATOM 4206 CB VAL B 302 9.025 3.322 2.604 1.00 74.87 C
ANISOU 4206 CB VAL B 302 14939 8331 5177 -1531 940 -1374 C
ATOM 4207 CG1 VAL B 302 9.638 1.952 2.858 1.00 66.60 C
ANISOU 4207 CG1 VAL B 302 13913 7402 3990 -1517 723 -1233 C
ATOM 4208 CG2 VAL B 302 9.647 4.366 3.524 1.00 87.09 C
ANISOU 4208 CG2 VAL B 302 16797 9833 6459 -1684 796 -1494 C
ATOM 4209 N VAL B 303 7.420 2.608 -0.086 1.00 74.94 N
ANISOU 4209 N VAL B 303 14183 8339 5953 -1272 1323 -1250 N
ATOM 4210 CA VAL B 303 6.825 1.587 -0.940 1.00 66.63 C
ANISOU 4210 CA VAL B 303 12884 7307 5126 -1167 1428 -1138 C
ATOM 4211 C VAL B 303 7.326 1.742 -2.369 1.00 68.37 C
ANISOU 4211 C VAL B 303 12748 7633 5597 -1148 1287 -1136 C
ATOM 4212 O VAL B 303 7.537 0.753 -3.082 1.00 77.78 O
ANISOU 4212 O VAL B 303 13755 8910 6889 -1089 1208 -1054 O
ATOM 4213 CB VAL B 303 5.288 1.672 -0.873 1.00 59.08 C
ANISOU 4213 CB VAL B 303 11944 6183 4319 -1113 1809 -1118 C
ATOM 4214 CG1 VAL B 303 4.648 0.709 -1.882 1.00 63.81 C
ANISOU 4214 CG1 VAL B 303 12273 6790 5181 -1027 1897 -1005 C
ATOM 4215 CG2 VAL B 303 4.813 1.402 0.534 1.00 63.62 C
ANISOU 4215 CG2 VAL B 303 12877 6662 4633 -1128 1966 -1117 C
ATOM 4216 N VAL B 304 7.534 2.986 -2.814 1.00 62.43 N
ANISOU 4216 N VAL B 304 11909 6869 4940 -1203 1260 -1229 N
ATOM 4217 CA VAL B 304 8.003 3.202 -4.180 1.00 60.19 C
ANISOU 4217 CA VAL B 304 11300 6685 4883 -1198 1138 -1227 C
ATOM 4218 C VAL B 304 9.475 2.833 -4.309 1.00 64.61 C
ANISOU 4218 C VAL B 304 11808 7411 5328 -1233 799 -1226 C
ATOM 4219 O VAL B 304 9.871 2.129 -5.245 1.00 56.97 O
ANISOU 4219 O VAL B 304 10614 6551 4483 -1187 706 -1173 O
ATOM 4220 CB VAL B 304 7.733 4.649 -4.628 1.00 54.17 C
ANISOU 4220 CB VAL B 304 10473 5847 4262 -1253 1222 -1316 C
ATOM 4221 CG1 VAL B 304 7.844 4.739 -6.136 1.00 44.52 C
ANISOU 4221 CG1 VAL B 304 8912 4702 3302 -1244 1177 -1286 C
ATOM 4222 CG2 VAL B 304 6.367 5.115 -4.153 1.00 60.39 C
ANISOU 4222 CG2 VAL B 304 11398 6445 5103 -1231 1560 -1330 C
ATOM 4223 N LEU B 305 10.304 3.283 -3.361 1.00 77.67 N
ANISOU 4223 N LEU B 305 13686 9083 6743 -1323 608 -1281 N
ATOM 4224 CA LEU B 305 11.716 2.908 -3.391 1.00 79.39 C
ANISOU 4224 CA LEU B 305 13866 9450 6847 -1373 263 -1258 C
ATOM 4225 C LEU B 305 11.890 1.397 -3.282 1.00 84.36 C
ANISOU 4225 C LEU B 305 14506 10148 7400 -1296 202 -1142 C
ATOM 4226 O LEU B 305 12.753 0.815 -3.954 1.00 87.18 O
ANISOU 4226 O LEU B 305 14690 10630 7805 -1279 6 -1098 O
ATOM 4227 CB LEU B 305 12.481 3.615 -2.277 1.00 77.98 C
ANISOU 4227 CB LEU B 305 13959 9259 6411 -1507 53 -1317 C
ATOM 4228 CG LEU B 305 13.981 3.346 -2.216 1.00 82.64 C
ANISOU 4228 CG LEU B 305 14515 9995 6889 -1591 -349 -1273 C
ATOM 4229 CD1 LEU B 305 14.769 4.500 -2.831 1.00 84.53 C
ANISOU 4229 CD1 LEU B 305 14591 10278 7249 -1695 -527 -1348 C
ATOM 4230 CD2 LEU B 305 14.386 3.109 -0.782 1.00 85.18 C
ANISOU 4230 CD2 LEU B 305 15187 10297 6882 -1680 -519 -1239 C
ATOM 4231 N VAL B 306 11.073 0.746 -2.447 1.00 80.14 N
ANISOU 4231 N VAL B 306 14182 9522 6744 -1251 375 -1091 N
ATOM 4232 CA VAL B 306 11.119 -0.708 -2.337 1.00 75.81 C
ANISOU 4232 CA VAL B 306 13665 9011 6130 -1176 341 -971 C
ATOM 4233 C VAL B 306 10.729 -1.345 -3.667 1.00 69.78 C
ANISOU 4233 C VAL B 306 12600 8273 5640 -1071 459 -934 C
ATOM 4234 O VAL B 306 11.276 -2.378 -4.071 1.00 71.28 O
ANISOU 4234 O VAL B 306 12720 8538 5825 -1017 336 -862 O
ATOM 4235 CB VAL B 306 10.213 -1.182 -1.185 1.00 74.87 C
ANISOU 4235 CB VAL B 306 13836 8774 5838 -1162 534 -924 C
ATOM 4236 CG1 VAL B 306 10.030 -2.698 -1.249 1.00 83.04 C
ANISOU 4236 CG1 VAL B 306 14874 9817 6861 -1070 554 -790 C
ATOM 4237 CG2 VAL B 306 10.787 -0.743 0.141 1.00 65.45 C
ANISOU 4237 CG2 VAL B 306 12972 7574 4323 -1279 369 -950 C
ATOM 4238 N PHE B 307 9.783 -0.726 -4.372 1.00 65.23 N
ANISOU 4238 N PHE B 307 11860 7626 5299 -1050 690 -977 N
ATOM 4239 CA PHE B 307 9.344 -1.237 -5.664 1.00 59.24 C
ANISOU 4239 CA PHE B 307 10826 6882 4800 -978 794 -941 C
ATOM 4240 C PHE B 307 10.440 -1.109 -6.717 1.00 54.49 C
ANISOU 4240 C PHE B 307 9996 6425 4285 -992 591 -977 C
ATOM 4241 O PHE B 307 10.721 -2.062 -7.453 1.00 48.03 O
ANISOU 4241 O PHE B 307 9052 5665 3532 -931 555 -936 O
ATOM 4242 CB PHE B 307 8.076 -0.499 -6.086 1.00 58.69 C
ANISOU 4242 CB PHE B 307 10663 6696 4942 -982 1054 -959 C
ATOM 4243 CG PHE B 307 7.526 -0.937 -7.413 1.00 52.20 C
ANISOU 4243 CG PHE B 307 9576 5876 4380 -940 1148 -913 C
ATOM 4244 CD1 PHE B 307 6.792 -2.110 -7.534 1.00 61.29 C
ANISOU 4244 CD1 PHE B 307 10730 6967 5592 -879 1270 -825 C
ATOM 4245 CD2 PHE B 307 7.722 -0.161 -8.538 1.00 44.82 C
ANISOU 4245 CD2 PHE B 307 8412 4996 3622 -980 1111 -956 C
ATOM 4246 CE1 PHE B 307 6.270 -2.511 -8.761 1.00 51.80 C
ANISOU 4246 CE1 PHE B 307 9310 5756 4617 -865 1341 -787 C
ATOM 4247 CE2 PHE B 307 7.200 -0.559 -9.779 1.00 47.09 C
ANISOU 4247 CE2 PHE B 307 8482 5285 4127 -966 1186 -911 C
ATOM 4248 CZ PHE B 307 6.476 -1.736 -9.884 1.00 47.20 C
ANISOU 4248 CZ PHE B 307 8506 5235 4193 -912 1295 -830 C
ATOM 4249 N ALA B 308 11.068 0.066 -6.808 1.00 48.73 N
ANISOU 4249 N ALA B 308 9222 5741 3553 -1077 467 -1059 N
ATOM 4250 CA ALA B 308 12.154 0.255 -7.767 1.00 47.78 C
ANISOU 4250 CA ALA B 308 8890 5757 3507 -1111 273 -1093 C
ATOM 4251 C ALA B 308 13.309 -0.706 -7.510 1.00 58.67 C
ANISOU 4251 C ALA B 308 10329 7246 4718 -1101 25 -1048 C
ATOM 4252 O ALA B 308 13.855 -1.301 -8.448 1.00 51.84 O
ANISOU 4252 O ALA B 308 9291 6472 3932 -1067 -38 -1040 O
ATOM 4253 CB ALA B 308 12.644 1.698 -7.726 1.00 41.30 C
ANISOU 4253 CB ALA B 308 8054 4947 2693 -1226 164 -1177 C
ATOM 4254 N LEU B 309 13.710 -0.857 -6.248 1.00 67.21 N
ANISOU 4254 N LEU B 309 11666 8315 5555 -1141 -130 -1011 N
ATOM 4255 CA LEU B 309 14.794 -1.778 -5.923 1.00 58.45 C
ANISOU 4255 CA LEU B 309 10634 7299 4275 -1141 -415 -926 C
ATOM 4256 C LEU B 309 14.444 -3.203 -6.335 1.00 53.54 C
ANISOU 4256 C LEU B 309 10006 6657 3681 -1007 -304 -847 C
ATOM 4257 O LEU B 309 15.254 -3.894 -6.961 1.00 58.12 O
ANISOU 4257 O LEU B 309 10496 7322 4266 -971 -463 -811 O
ATOM 4258 CB LEU B 309 15.118 -1.714 -4.430 1.00 55.51 C
ANISOU 4258 CB LEU B 309 10563 6898 3630 -1216 -597 -870 C
ATOM 4259 CG LEU B 309 15.771 -0.443 -3.887 1.00 52.30 C
ANISOU 4259 CG LEU B 309 10214 6512 3145 -1369 -796 -935 C
ATOM 4260 CD1 LEU B 309 16.092 -0.608 -2.413 1.00 58.83 C
ANISOU 4260 CD1 LEU B 309 11364 7311 3679 -1448 -986 -863 C
ATOM 4261 CD2 LEU B 309 17.022 -0.100 -4.673 1.00 51.48 C
ANISOU 4261 CD2 LEU B 309 9865 6551 3146 -1443 -1092 -933 C
ATOM 4262 N CYS B 310 13.232 -3.659 -6.000 1.00 59.66 N
ANISOU 4262 N CYS B 310 10884 7306 4478 -938 -35 -816 N
ATOM 4263 CA CYS B 310 12.858 -5.039 -6.306 1.00 64.95 C
ANISOU 4263 CA CYS B 310 11579 7927 5171 -821 70 -732 C
ATOM 4264 C CYS B 310 12.887 -5.303 -7.809 1.00 65.56 C
ANISOU 4264 C CYS B 310 11388 8044 5478 -764 162 -787 C
ATOM 4265 O CYS B 310 13.488 -6.282 -8.265 1.00 67.18 O
ANISOU 4265 O CYS B 310 11601 8276 5648 -689 77 -753 O
ATOM 4266 CB CYS B 310 11.478 -5.355 -5.727 1.00 67.78 C
ANISOU 4266 CB CYS B 310 12066 8139 5549 -787 344 -687 C
ATOM 4267 SG CYS B 310 11.478 -5.506 -3.927 1.00 79.71 S
ANISOU 4267 SG CYS B 310 13955 9595 6734 -839 258 -604 S
ATOM 4268 N TYR B 311 12.274 -4.414 -8.597 1.00 58.42 N
ANISOU 4268 N TYR B 311 10264 7135 4797 -798 324 -866 N
ATOM 4269 CA TYR B 311 12.206 -4.559 -10.047 1.00 43.58 C
ANISOU 4269 CA TYR B 311 8125 5293 3138 -768 420 -913 C
ATOM 4270 C TYR B 311 13.442 -4.050 -10.779 1.00 40.58 C
ANISOU 4270 C TYR B 311 7591 5064 2765 -826 242 -992 C
ATOM 4271 O TYR B 311 13.585 -4.329 -11.979 1.00 40.61 O
ANISOU 4271 O TYR B 311 7406 5114 2911 -805 316 -1037 O
ATOM 4272 CB TYR B 311 10.964 -3.839 -10.587 1.00 42.29 C
ANISOU 4272 CB TYR B 311 7812 5055 3200 -797 630 -920 C
ATOM 4273 CG TYR B 311 9.676 -4.574 -10.323 1.00 46.42 C
ANISOU 4273 CG TYR B 311 8419 5435 3782 -750 827 -838 C
ATOM 4274 CD1 TYR B 311 9.074 -4.543 -9.070 1.00 42.66 C
ANISOU 4274 CD1 TYR B 311 8167 4863 3180 -756 894 -791 C
ATOM 4275 CD2 TYR B 311 9.064 -5.311 -11.328 1.00 49.21 C
ANISOU 4275 CD2 TYR B 311 8644 5745 4310 -718 944 -810 C
ATOM 4276 CE1 TYR B 311 7.890 -5.243 -8.824 1.00 39.55 C
ANISOU 4276 CE1 TYR B 311 7855 4331 2840 -726 1085 -712 C
ATOM 4277 CE2 TYR B 311 7.890 -5.999 -11.098 1.00 48.17 C
ANISOU 4277 CE2 TYR B 311 8598 5472 4233 -700 1107 -730 C
ATOM 4278 CZ TYR B 311 7.306 -5.961 -9.841 1.00 49.46 C
ANISOU 4278 CZ TYR B 311 8973 5541 4278 -702 1183 -679 C
ATOM 4279 OH TYR B 311 6.136 -6.643 -9.600 1.00 56.54 O
ANISOU 4279 OH TYR B 311 9960 6291 5232 -692 1361 -598 O
ATOM 4280 N LEU B 312 14.343 -3.336 -10.103 1.00 45.51 N
ANISOU 4280 N LEU B 312 8288 5763 3241 -918 4 -1005 N
ATOM 4281 CA LEU B 312 15.591 -2.922 -10.744 1.00 46.46 C
ANISOU 4281 CA LEU B 312 8256 6036 3362 -1009 -209 -1058 C
ATOM 4282 C LEU B 312 16.354 -4.099 -11.334 1.00 57.08 C
ANISOU 4282 C LEU B 312 9345 7442 4900 -843 -263 -956 C
ATOM 4283 O LEU B 312 16.741 -4.025 -12.512 1.00 63.90 O
ANISOU 4283 O LEU B 312 9901 8391 5986 -820 -196 -988 O
ATOM 4284 CB LEU B 312 16.460 -2.132 -9.756 1.00 48.99 C
ANISOU 4284 CB LEU B 312 8673 6412 3529 -1132 -523 -1033 C
ATOM 4285 CG LEU B 312 17.784 -1.626 -10.349 1.00 43.19 C
ANISOU 4285 CG LEU B 312 7611 5840 2957 -1201 -770 -1005 C
ATOM 4286 CD1 LEU B 312 17.545 -0.752 -11.576 1.00 49.34 C
ANISOU 4286 CD1 LEU B 312 8162 6663 3922 -1277 -599 -1113 C
ATOM 4287 CD2 LEU B 312 18.668 -0.902 -9.330 1.00 47.90 C
ANISOU 4287 CD2 LEU B 312 8327 6484 3390 -1358 -1138 -964 C
ATOM 4288 N PRO B 313 16.597 -5.189 -10.607 1.00 48.84 N
ANISOU 4288 N PRO B 313 8406 6349 3800 -719 -363 -829 N
ATOM 4289 CA PRO B 313 17.389 -6.285 -11.179 1.00 41.14 C
ANISOU 4289 CA PRO B 313 7162 5406 3065 -538 -403 -730 C
ATOM 4290 C PRO B 313 16.796 -6.863 -12.458 1.00 55.10 C
ANISOU 4290 C PRO B 313 8789 7125 5021 -445 -101 -813 C
ATOM 4291 O PRO B 313 17.426 -6.793 -13.518 1.00 68.81 O
ANISOU 4291 O PRO B 313 10226 8956 6964 -411 -58 -850 O
ATOM 4292 CB PRO B 313 17.411 -7.312 -10.040 1.00 43.29 C
ANISOU 4292 CB PRO B 313 7657 5582 3211 -439 -533 -575 C
ATOM 4293 CG PRO B 313 17.310 -6.477 -8.799 1.00 46.42 C
ANISOU 4293 CG PRO B 313 8361 5985 3290 -610 -714 -568 C
ATOM 4294 CD PRO B 313 16.359 -5.367 -9.156 1.00 50.97 C
ANISOU 4294 CD PRO B 313 9043 6543 3782 -753 -488 -755 C
ATOM 4295 N ILE B 314 15.592 -7.439 -12.374 1.00 51.86 N
ANISOU 4295 N ILE B 314 8602 6567 4534 -419 108 -838 N
ATOM 4296 CA ILE B 314 15.050 -8.160 -13.523 1.00 56.63 C
ANISOU 4296 CA ILE B 314 9109 7103 5305 -343 349 -900 C
ATOM 4297 C ILE B 314 14.770 -7.224 -14.692 1.00 57.59 C
ANISOU 4297 C ILE B 314 9073 7309 5500 -469 483 -1031 C
ATOM 4298 O ILE B 314 14.900 -7.629 -15.859 1.00 57.49 O
ANISOU 4298 O ILE B 314 8889 7315 5641 -423 609 -1086 O
ATOM 4299 CB ILE B 314 13.786 -8.940 -13.109 1.00 67.98 C
ANISOU 4299 CB ILE B 314 10817 8359 6655 -319 513 -871 C
ATOM 4300 CG1 ILE B 314 13.392 -9.895 -14.220 1.00 68.53 C
ANISOU 4300 CG1 ILE B 314 10803 8336 6901 -238 700 -917 C
ATOM 4301 CG2 ILE B 314 12.645 -7.974 -12.829 1.00 66.70 C
ANISOU 4301 CG2 ILE B 314 10831 8165 6349 -480 639 -934 C
ATOM 4302 CD1 ILE B 314 14.578 -10.651 -14.756 1.00 70.19 C
ANISOU 4302 CD1 ILE B 314 10794 8579 7297 -74 636 -900 C
ATOM 4303 N SER B 315 14.412 -5.962 -14.411 1.00 58.48 N
ANISOU 4303 N SER B 315 9253 7464 5502 -633 459 -1080 N
ATOM 4304 CA SER B 315 14.154 -5.025 -15.503 1.00 48.36 C
ANISOU 4304 CA SER B 315 7815 6254 4304 -762 562 -1174 C
ATOM 4305 C SER B 315 15.448 -4.694 -16.236 1.00 59.63 C
ANISOU 4305 C SER B 315 8938 7853 5866 -760 456 -1179 C
ATOM 4306 O SER B 315 15.515 -4.793 -17.469 1.00 55.86 O
ANISOU 4306 O SER B 315 8285 7430 5508 -765 586 -1228 O
ATOM 4307 CB SER B 315 13.467 -3.755 -14.983 1.00 39.55 C
ANISOU 4307 CB SER B 315 6734 5104 3188 -866 535 -1145 C
ATOM 4308 OG SER B 315 12.391 -4.087 -14.119 1.00 65.07 O
ANISOU 4308 OG SER B 315 10126 8189 6407 -809 608 -1063 O
ATOM 4309 N VAL B 316 16.506 -4.367 -15.483 1.00 62.42 N
ANISOU 4309 N VAL B 316 9227 8291 6198 -756 218 -1113 N
ATOM 4310 CA VAL B 316 17.821 -4.159 -16.090 1.00 49.74 C
ANISOU 4310 CA VAL B 316 7293 6846 4760 -738 114 -1080 C
ATOM 4311 C VAL B 316 18.347 -5.466 -16.691 1.00 53.41 C
ANISOU 4311 C VAL B 316 7598 7302 5392 -532 215 -1047 C
ATOM 4312 O VAL B 316 18.911 -5.478 -17.795 1.00 42.69 O
ANISOU 4312 O VAL B 316 5989 6042 4189 -507 328 -1080 O
ATOM 4313 CB VAL B 316 18.803 -3.541 -15.068 1.00 37.60 C
ANISOU 4313 CB VAL B 316 5722 5385 3177 -800 -203 -991 C
ATOM 4314 CG1 VAL B 316 20.248 -3.606 -15.580 1.00 39.51 C
ANISOU 4314 CG1 VAL B 316 5581 5783 3649 -742 -321 -905 C
ATOM 4315 CG2 VAL B 316 18.405 -2.107 -14.747 1.00 37.72 C
ANISOU 4315 CG2 VAL B 316 5865 5406 3060 -1019 -272 -1062 C
ATOM 4316 N LEU B 317 18.171 -6.588 -15.982 1.00 61.44 N
ANISOU 4316 N LEU B 317 8772 8190 6383 -382 194 -981 N
ATOM 4317 CA LEU B 317 18.618 -7.874 -16.518 1.00 71.14 C
ANISOU 4317 CA LEU B 317 9875 9364 7791 -171 306 -957 C
ATOM 4318 C LEU B 317 17.903 -8.198 -17.824 1.00 76.12 C
ANISOU 4318 C LEU B 317 10515 9948 8459 -179 600 -1096 C
ATOM 4319 O LEU B 317 18.522 -8.661 -18.792 1.00 73.59 O
ANISOU 4319 O LEU B 317 10000 9665 8296 -81 737 -1140 O
ATOM 4320 CB LEU B 317 18.370 -8.987 -15.501 1.00 69.19 C
ANISOU 4320 CB LEU B 317 9836 8953 7498 -31 231 -853 C
ATOM 4321 CG LEU B 317 19.394 -9.228 -14.398 1.00 61.35 C
ANISOU 4321 CG LEU B 317 8782 7987 6543 53 -67 -671 C
ATOM 4322 CD1 LEU B 317 19.041 -10.485 -13.621 1.00 63.43 C
ANISOU 4322 CD1 LEU B 317 9256 8067 6779 200 -92 -563 C
ATOM 4323 CD2 LEU B 317 20.813 -9.351 -14.957 1.00 51.18 C
ANISOU 4323 CD2 LEU B 317 7094 6812 5538 173 -129 -604 C
ATOM 4324 N ASN B 318 16.593 -7.957 -17.872 1.00 78.70 N
ANISOU 4324 N ASN B 318 11072 10189 8641 -304 702 -1162 N
ATOM 4325 CA ASN B 318 15.853 -8.253 -19.086 1.00 75.98 C
ANISOU 4325 CA ASN B 318 10757 9796 8317 -349 932 -1273 C
ATOM 4326 C ASN B 318 16.250 -7.310 -20.220 1.00 65.69 C
ANISOU 4326 C ASN B 318 9246 8664 7051 -478 995 -1343 C
ATOM 4327 O ASN B 318 16.292 -7.718 -21.386 1.00 61.83 O
ANISOU 4327 O ASN B 318 8697 8186 6608 -468 1170 -1427 O
ATOM 4328 CB ASN B 318 14.359 -8.194 -18.802 1.00 85.67 C
ANISOU 4328 CB ASN B 318 12241 10888 9421 -461 998 -1284 C
ATOM 4329 CG ASN B 318 13.548 -8.644 -19.978 1.00 90.57 C
ANISOU 4329 CG ASN B 318 12878 11438 10098 -507 1156 -1337 C
ATOM 4330 OD1 ASN B 318 13.001 -7.827 -20.712 1.00 82.42 O
ANISOU 4330 OD1 ASN B 318 11724 10459 9132 -635 1127 -1286 O
ATOM 4331 ND2 ASN B 318 13.482 -9.952 -20.186 1.00 97.58 N
ANISOU 4331 ND2 ASN B 318 13864 12187 11026 -383 1254 -1370 N
ATOM 4332 N VAL B 319 16.536 -6.044 -19.900 1.00 53.99 N
ANISOU 4332 N VAL B 319 7672 7307 5534 -612 858 -1312 N
ATOM 4333 CA VAL B 319 16.925 -5.092 -20.937 1.00 49.46 C
ANISOU 4333 CA VAL B 319 6896 6894 5001 -750 904 -1351 C
ATOM 4334 C VAL B 319 18.294 -5.437 -21.511 1.00 63.40 C
ANISOU 4334 C VAL B 319 8383 8786 6918 -631 942 -1338 C
ATOM 4335 O VAL B 319 18.508 -5.369 -22.729 1.00 69.32 O
ANISOU 4335 O VAL B 319 9014 9624 7702 -674 1114 -1400 O
ATOM 4336 CB VAL B 319 16.893 -3.658 -20.377 1.00 49.03 C
ANISOU 4336 CB VAL B 319 6828 6909 4893 -924 737 -1315 C
ATOM 4337 CG1 VAL B 319 17.719 -2.721 -21.263 1.00 31.87 C
ANISOU 4337 CG1 VAL B 319 4385 4922 2804 -1041 730 -1311 C
ATOM 4338 CG2 VAL B 319 15.468 -3.162 -20.255 1.00 69.40 C
ANISOU 4338 CG2 VAL B 319 9628 9373 7370 -1057 792 -1347 C
ATOM 4339 N LEU B 320 19.238 -5.822 -20.653 1.00 70.57 N
ANISOU 4339 N LEU B 320 9183 9704 7925 -483 791 -1243 N
ATOM 4340 CA LEU B 320 20.554 -6.216 -21.145 1.00 58.83 C
ANISOU 4340 CA LEU B 320 7391 8320 6642 -341 843 -1204 C
ATOM 4341 C LEU B 320 20.478 -7.470 -22.011 1.00 49.63 C
ANISOU 4341 C LEU B 320 6258 7056 5543 -171 1118 -1297 C
ATOM 4342 O LEU B 320 21.188 -7.583 -23.014 1.00 48.37 O
ANISOU 4342 O LEU B 320 5895 6988 5495 -121 1308 -1341 O
ATOM 4343 CB LEU B 320 21.515 -6.414 -19.975 1.00 61.34 C
ANISOU 4343 CB LEU B 320 7581 8648 7078 -221 584 -1048 C
ATOM 4344 CG LEU B 320 21.720 -5.114 -19.193 1.00 53.47 C
ANISOU 4344 CG LEU B 320 6563 7752 6003 -417 302 -974 C
ATOM 4345 CD1 LEU B 320 22.535 -5.353 -17.933 1.00 50.95 C
ANISOU 4345 CD1 LEU B 320 6187 7424 5747 -336 -5 -810 C
ATOM 4346 CD2 LEU B 320 22.365 -4.044 -20.068 1.00 48.22 C
ANISOU 4346 CD2 LEU B 320 5619 7274 5427 -565 334 -977 C
ATOM 4347 N LYS B 321 19.630 -8.431 -21.637 1.00 56.52 N
ANISOU 4347 N LYS B 321 7398 7730 6347 -86 1156 -1330 N
ATOM 4348 CA LYS B 321 19.514 -9.660 -22.420 1.00 59.47 C
ANISOU 4348 CA LYS B 321 7846 7969 6780 64 1403 -1433 C
ATOM 4349 C LYS B 321 18.861 -9.392 -23.774 1.00 65.98 C
ANISOU 4349 C LYS B 321 8763 8830 7477 -101 1622 -1585 C
ATOM 4350 O LYS B 321 19.391 -9.789 -24.818 1.00 66.90 O
ANISOU 4350 O LYS B 321 8791 8978 7650 -36 1849 -1680 O
ATOM 4351 CB LYS B 321 18.734 -10.715 -21.637 1.00 51.58 C
ANISOU 4351 CB LYS B 321 7116 6736 5745 168 1361 -1411 C
ATOM 4352 CG LYS B 321 18.673 -12.090 -22.309 1.00 50.96 C
ANISOU 4352 CG LYS B 321 7136 6472 5754 338 1589 -1513 C
ATOM 4353 CD LYS B 321 17.587 -12.959 -21.669 1.00 59.82 C
ANISOU 4353 CD LYS B 321 8566 7359 6803 358 1549 -1495 C
ATOM 4354 CE LYS B 321 17.797 -14.441 -21.980 1.00 78.40 C
ANISOU 4354 CE LYS B 321 10995 9488 9305 579 1710 -1553 C
ATOM 4355 NZ LYS B 321 18.971 -14.994 -21.242 1.00 89.88 N
ANISOU 4355 NZ LYS B 321 12246 10910 10994 837 1617 -1414 N
ATOM 4356 N ARG B 322 17.694 -8.739 -23.775 1.00 71.58 N
ANISOU 4356 N ARG B 322 9659 9526 8013 -316 1561 -1601 N
ATOM 4357 CA ARG B 322 16.884 -8.643 -24.985 1.00 61.11 C
ANISOU 4357 CA ARG B 322 8455 8188 6577 -477 1692 -1686 C
ATOM 4358 C ARG B 322 17.341 -7.517 -25.905 1.00 71.30 C
ANISOU 4358 C ARG B 322 9554 9683 7853 -635 1711 -1670 C
ATOM 4359 O ARG B 322 17.341 -7.679 -27.129 1.00 91.28 O
ANISOU 4359 O ARG B 322 12084 12216 10383 -669 1796 -1674 O
ATOM 4360 CB ARG B 322 15.416 -8.436 -24.620 1.00 51.72 C
ANISOU 4360 CB ARG B 322 7440 6861 5351 -593 1504 -1559 C
ATOM 4361 CG ARG B 322 14.784 -9.546 -23.806 1.00 53.44 C
ANISOU 4361 CG ARG B 322 7852 6875 5578 -472 1484 -1543 C
ATOM 4362 CD ARG B 322 14.280 -10.669 -24.707 1.00 61.08 C
ANISOU 4362 CD ARG B 322 8923 7701 6583 -436 1556 -1567 C
ATOM 4363 NE ARG B 322 13.650 -11.760 -23.963 1.00 76.35 N
ANISOU 4363 NE ARG B 322 11039 9432 8539 -344 1543 -1548 N
ATOM 4364 CZ ARG B 322 13.204 -12.887 -24.516 1.00 87.60 C
ANISOU 4364 CZ ARG B 322 12586 10701 9997 -312 1600 -1580 C
ATOM 4365 NH1 ARG B 322 13.317 -13.080 -25.824 1.00 87.69 N
ANISOU 4365 NH1 ARG B 322 12579 10740 10001 -362 1670 -1643 N
ATOM 4366 NH2 ARG B 322 12.650 -13.824 -23.761 1.00 97.01 N
ANISOU 4366 NH2 ARG B 322 13944 11701 11217 -243 1590 -1551 N
ATOM 4367 N VAL B 323 17.735 -6.375 -25.353 1.00 69.32 N
ANISOU 4367 N VAL B 323 9151 9591 7598 -738 1596 -1624 N
ATOM 4368 CA VAL B 323 18.130 -5.243 -26.187 1.00 69.54 C
ANISOU 4368 CA VAL B 323 9002 9816 7605 -918 1622 -1610 C
ATOM 4369 C VAL B 323 19.611 -5.277 -26.537 1.00 87.81 C
ANISOU 4369 C VAL B 323 11015 12284 10066 -801 1716 -1588 C
ATOM 4370 O VAL B 323 19.999 -4.901 -27.646 1.00 98.16 O
ANISOU 4370 O VAL B 323 12214 13734 11347 -898 1878 -1619 O
ATOM 4371 CB VAL B 323 17.756 -3.930 -25.474 1.00 64.62 C
ANISOU 4371 CB VAL B 323 8357 9234 6960 -1088 1396 -1516 C
ATOM 4372 CG1 VAL B 323 17.846 -2.770 -26.443 1.00 63.78 C
ANISOU 4372 CG1 VAL B 323 8125 9290 6820 -1312 1421 -1494 C
ATOM 4373 CG2 VAL B 323 16.376 -4.047 -24.863 1.00 63.97 C
ANISOU 4373 CG2 VAL B 323 8526 8947 6833 -1117 1289 -1476 C
ATOM 4374 N PHE B 324 20.454 -5.733 -25.621 1.00 87.99 N
ANISOU 4374 N PHE B 324 10894 12283 10255 -598 1620 -1515 N
ATOM 4375 CA PHE B 324 21.892 -5.712 -25.826 1.00 80.17 C
ANISOU 4375 CA PHE B 324 9560 11434 9467 -480 1681 -1451 C
ATOM 4376 C PHE B 324 22.498 -7.085 -26.088 1.00 84.79 C
ANISOU 4376 C PHE B 324 10095 11923 10198 -201 1903 -1506 C
ATOM 4377 O PHE B 324 23.725 -7.188 -26.205 1.00 90.33 O
ANISOU 4377 O PHE B 324 10478 12720 11122 -62 1977 -1435 O
ATOM 4378 CB PHE B 324 22.555 -5.060 -24.605 1.00 77.73 C
ANISOU 4378 CB PHE B 324 9066 11185 9283 -479 1364 -1288 C
ATOM 4379 CG PHE B 324 22.137 -3.627 -24.391 1.00 78.89 C
ANISOU 4379 CG PHE B 324 9239 11417 9319 -747 1169 -1246 C
ATOM 4380 CD1 PHE B 324 21.092 -3.318 -23.542 1.00 78.43 C
ANISOU 4380 CD1 PHE B 324 9453 11235 9111 -838 995 -1256 C
ATOM 4381 CD2 PHE B 324 22.777 -2.594 -25.054 1.00 66.00 C
ANISOU 4381 CD2 PHE B 324 7361 9972 7742 -905 1183 -1194 C
ATOM 4382 CE1 PHE B 324 20.705 -2.019 -23.343 1.00 60.90 C
ANISOU 4382 CE1 PHE B 324 7265 9059 6815 -1063 844 -1230 C
ATOM 4383 CE2 PHE B 324 22.391 -1.282 -24.858 1.00 53.86 C
ANISOU 4383 CE2 PHE B 324 5857 8480 6126 -1147 1002 -1155 C
ATOM 4384 CZ PHE B 324 21.352 -0.995 -24.000 1.00 50.59 C
ANISOU 4384 CZ PHE B 324 5722 7923 5577 -1219 836 -1181 C
ATOM 4385 N GLY B 325 21.687 -8.137 -26.181 1.00 88.64 N
ANISOU 4385 N GLY B 325 10874 12210 10597 -114 2014 -1620 N
ATOM 4386 CA GLY B 325 22.217 -9.450 -26.516 1.00 94.66 C
ANISOU 4386 CA GLY B 325 11620 12843 11504 150 2252 -1695 C
ATOM 4387 C GLY B 325 23.243 -9.989 -25.548 1.00103.31 C
ANISOU 4387 C GLY B 325 12469 13894 12889 409 2133 -1548 C
ATOM 4388 O GLY B 325 24.143 -10.726 -25.964 1.00114.58 O
ANISOU 4388 O GLY B 325 13712 15289 14533 635 2355 -1566 O
ATOM 4389 N MET B 326 23.138 -9.639 -24.265 1.00 98.38 N
ANISOU 4389 N MET B 326 11842 13261 12277 382 1790 -1397 N
ATOM 4390 CA MET B 326 24.102 -10.099 -23.272 1.00 87.95 C
ANISOU 4390 CA MET B 326 10296 11906 11217 595 1609 -1219 C
ATOM 4391 C MET B 326 23.789 -11.524 -22.822 1.00 84.32 C
ANISOU 4391 C MET B 326 10027 11182 10827 825 1650 -1232 C
ATOM 4392 O MET B 326 22.778 -12.124 -23.200 1.00 77.47 O
ANISOU 4392 O MET B 326 9482 10155 9799 803 1797 -1381 O
ATOM 4393 CB MET B 326 24.136 -9.170 -22.056 1.00 81.21 C
ANISOU 4393 CB MET B 326 9410 11141 10306 449 1208 -1053 C
ATOM 4394 CG MET B 326 24.709 -7.791 -22.312 1.00 83.93 C
ANISOU 4394 CG MET B 326 9506 11724 10660 247 1111 -995 C
ATOM 4395 SD MET B 326 25.238 -7.040 -20.754 1.00 92.30 S
ANISOU 4395 SD MET B 326 10467 12847 11755 158 619 -772 S
ATOM 4396 CE MET B 326 26.686 -8.022 -20.401 1.00105.27 C
ANISOU 4396 CE MET B 326 11727 14470 13801 459 563 -575 C
ATOM 4397 N PHE B 327 24.691 -12.066 -22.005 1.00 89.55 N
ANISOU 4397 N PHE B 327 10476 11793 11756 1038 1496 -1052 N
ATOM 4398 CA PHE B 327 24.504 -13.370 -21.370 1.00 88.42 C
ANISOU 4398 CA PHE B 327 10485 11394 11717 1260 1467 -1004 C
ATOM 4399 C PHE B 327 24.418 -14.505 -22.390 1.00101.36 C
ANISOU 4399 C PHE B 327 12215 12843 13454 1449 1858 -1188 C
ATOM 4400 O PHE B 327 23.625 -15.437 -22.233 1.00113.68 O
ANISOU 4400 O PHE B 327 14080 14167 14945 1512 1904 -1256 O
ATOM 4401 CB PHE B 327 23.257 -13.366 -20.485 1.00 70.40 C
ANISOU 4401 CB PHE B 327 8589 9005 9153 1115 1258 -995 C
ATOM 4402 CG PHE B 327 23.078 -12.103 -19.690 1.00 64.34 C
ANISOU 4402 CG PHE B 327 7836 8413 8197 876 951 -897 C
ATOM 4403 CD1 PHE B 327 24.147 -11.518 -19.029 1.00 60.35 C
ANISOU 4403 CD1 PHE B 327 7039 8056 7837 877 685 -707 C
ATOM 4404 CD2 PHE B 327 21.828 -11.508 -19.602 1.00 62.98 C
ANISOU 4404 CD2 PHE B 327 7972 8239 7720 648 929 -994 C
ATOM 4405 CE1 PHE B 327 23.977 -10.353 -18.293 1.00 50.26 C
ANISOU 4405 CE1 PHE B 327 5817 6911 6367 643 402 -641 C
ATOM 4406 CE2 PHE B 327 21.641 -10.345 -18.868 1.00 56.16 C
ANISOU 4406 CE2 PHE B 327 7148 7503 6689 440 681 -927 C
ATOM 4407 CZ PHE B 327 22.717 -9.764 -18.210 1.00 50.35 C
ANISOU 4407 CZ PHE B 327 6161 6904 6064 432 417 -764 C
ATOM 4408 N ARG B 328 25.237 -14.439 -23.442 1.00100.90 N
ANISOU 4408 N ARG B 328 11907 12877 13554 1533 2154 -1271 N
ATOM 4409 CA ARG B 328 25.254 -15.490 -24.453 1.00104.10 C
ANISOU 4409 CA ARG B 328 12416 13094 14042 1715 2561 -1471 C
ATOM 4410 C ARG B 328 26.503 -16.364 -24.431 1.00114.29 C
ANISOU 4410 C ARG B 328 13377 14273 15777 2073 2718 -1377 C
ATOM 4411 O ARG B 328 26.563 -17.338 -25.189 1.00120.06 O
ANISOU 4411 O ARG B 328 14209 14800 16606 2261 3074 -1551 O
ATOM 4412 CB ARG B 328 25.081 -14.896 -25.855 1.00104.87 C
ANISOU 4412 CB ARG B 328 12571 13342 13934 1539 2877 -1689 C
ATOM 4413 CG ARG B 328 23.731 -14.248 -26.098 1.00101.15 C
ANISOU 4413 CG ARG B 328 12456 12922 13056 1209 2781 -1804 C
ATOM 4414 CD ARG B 328 23.645 -13.680 -27.503 1.00108.66 C
ANISOU 4414 CD ARG B 328 13451 14024 13810 1030 3068 -1984 C
ATOM 4415 NE ARG B 328 24.720 -12.737 -27.792 1.00120.54 N
ANISOU 4415 NE ARG B 328 14559 15798 15443 1004 3112 -1883 N
ATOM 4416 CZ ARG B 328 24.906 -12.165 -28.977 1.00132.77 C
ANISOU 4416 CZ ARG B 328 16072 17517 16859 863 3370 -1993 C
ATOM 4417 NH1 ARG B 328 25.910 -11.318 -29.158 1.00138.95 N
ANISOU 4417 NH1 ARG B 328 16469 18538 17787 838 3398 -1870 N
ATOM 4418 NH2 ARG B 328 24.092 -12.449 -29.984 1.00136.51 N
ANISOU 4418 NH2 ARG B 328 16917 17916 17037 727 3417 -2103 N
ATOM 4419 N GLN B 329 27.497 -16.062 -23.599 1.00119.06 N
ANISOU 4419 N GLN B 329 13591 14984 16664 2172 2463 -1105 N
ATOM 4420 CA GLN B 329 28.640 -16.952 -23.427 1.00125.17 C
ANISOU 4420 CA GLN B 329 14022 15620 17916 2528 2561 -961 C
ATOM 4421 C GLN B 329 28.337 -17.992 -22.357 1.00126.20 C
ANISOU 4421 C GLN B 329 14317 15476 18158 2694 2321 -822 C
ATOM 4422 O GLN B 329 27.830 -17.655 -21.281 1.00124.15 O
ANISOU 4422 O GLN B 329 14203 15252 17717 2537 1914 -672 O
ATOM 4423 CB GLN B 329 29.904 -16.177 -23.062 1.00127.62 C
ANISOU 4423 CB GLN B 329 13796 16169 18525 2549 2374 -694 C
ATOM 4424 CG GLN B 329 31.085 -17.088 -22.766 1.00133.59 C
ANISOU 4424 CG GLN B 329 14149 16776 19833 2923 2424 -487 C
ATOM 4425 CD GLN B 329 31.548 -17.863 -23.987 1.00139.04 C
ANISOU 4425 CD GLN B 329 14746 17326 20757 3190 3012 -689 C
ATOM 4426 OE1 GLN B 329 31.345 -19.074 -24.078 1.00137.88 O
ANISOU 4426 OE1 GLN B 329 14782 16866 20742 3434 3209 -785 O
ATOM 4427 NE2 GLN B 329 32.174 -17.169 -24.932 1.00144.34 N
ANISOU 4427 NE2 GLN B 329 15148 18219 21477 3140 3307 -756 N
ATOM 4428 N ALA B 330 28.637 -19.256 -22.660 1.00129.36 N
ANISOU 4428 N ALA B 330 14713 15590 18849 3009 2591 -876 N
ATOM 4429 CA ALA B 330 28.275 -20.352 -21.771 1.00128.00 C
ANISOU 4429 CA ALA B 330 14735 15116 18784 3169 2407 -760 C
ATOM 4430 C ALA B 330 29.217 -20.497 -20.587 1.00134.34 C
ANISOU 4430 C ALA B 330 15173 15920 19950 3333 2029 -372 C
ATOM 4431 O ALA B 330 28.929 -21.296 -19.690 1.00135.24 O
ANISOU 4431 O ALA B 330 15444 15813 20128 3432 1800 -218 O
ATOM 4432 CB ALA B 330 28.253 -21.674 -22.537 1.00125.51 C
ANISOU 4432 CB ALA B 330 14565 14454 18669 3447 2831 -962 C
ATOM 4433 N SER B 331 30.338 -19.770 -20.577 1.00137.42 N
ANISOU 4433 N SER B 331 15080 16546 20587 3355 1949 -194 N
ATOM 4434 CA SER B 331 31.272 -19.861 -19.463 1.00139.06 C
ANISOU 4434 CA SER B 331 14919 16769 21150 3480 1542 203 C
ATOM 4435 C SER B 331 30.588 -19.482 -18.156 1.00135.98 C
ANISOU 4435 C SER B 331 14808 16434 20423 3234 1010 374 C
ATOM 4436 O SER B 331 30.748 -20.172 -17.141 1.00142.29 O
ANISOU 4436 O SER B 331 15608 17071 21386 3358 704 635 O
ATOM 4437 CB SER B 331 32.483 -18.964 -19.706 1.00141.61 C
ANISOU 4437 CB SER B 331 14689 17371 21745 3467 1513 361 C
ATOM 4438 OG SER B 331 32.108 -17.606 -19.654 1.00139.94 O
ANISOU 4438 OG SER B 331 14568 17465 21138 3094 1317 309 O
ATOM 4439 N ASP B 332 29.815 -18.391 -18.150 1.00128.11 N
ANISOU 4439 N ASP B 332 14062 15657 18957 2886 903 238 N
ATOM 4440 CA ASP B 332 29.186 -17.930 -16.912 1.00121.93 C
ANISOU 4440 CA ASP B 332 13553 14937 17837 2644 439 383 C
ATOM 4441 C ASP B 332 27.698 -18.270 -16.851 1.00108.10 C
ANISOU 4441 C ASP B 332 12361 13035 15678 2519 529 177 C
ATOM 4442 O ASP B 332 26.878 -17.457 -16.417 1.00 95.65 O
ANISOU 4442 O ASP B 332 11061 11585 13697 2233 355 126 O
ATOM 4443 CB ASP B 332 29.385 -16.430 -16.798 1.00126.48 C
ANISOU 4443 CB ASP B 332 14008 15841 18206 2343 226 405 C
ATOM 4444 CG ASP B 332 28.808 -15.691 -17.983 1.00132.31 C
ANISOU 4444 CG ASP B 332 14863 16712 18696 2172 578 84 C
ATOM 4445 OD1 ASP B 332 28.354 -16.373 -18.932 1.00135.87 O
ANISOU 4445 OD1 ASP B 332 15465 17012 19148 2293 988 -150 O
ATOM 4446 OD2 ASP B 332 28.791 -14.443 -17.975 1.00135.03 O
ANISOU 4446 OD2 ASP B 332 15167 17297 18840 1908 438 68 O
ATOM 4447 N ARG B 333 27.321 -19.472 -17.285 1.00110.20 N
ANISOU 4447 N ARG B 333 12796 13013 16063 2728 809 60 N
ATOM 4448 CA ARG B 333 25.927 -19.879 -17.189 1.00103.19 C
ANISOU 4448 CA ARG B 333 12411 11962 14836 2608 871 -97 C
ATOM 4449 C ARG B 333 25.482 -20.051 -15.740 1.00 98.49 C
ANISOU 4449 C ARG B 333 12039 11307 14076 2524 464 147 C
ATOM 4450 O ARG B 333 24.309 -19.829 -15.427 1.00 88.17 O
ANISOU 4450 O ARG B 333 11115 9992 12394 2312 424 60 O
ATOM 4451 CB ARG B 333 25.687 -21.140 -18.033 1.00108.52 C
ANISOU 4451 CB ARG B 333 13215 12322 15694 2838 1257 -284 C
ATOM 4452 CG ARG B 333 24.213 -21.408 -18.343 1.00109.44 C
ANISOU 4452 CG ARG B 333 13823 12302 15458 2664 1399 -514 C
ATOM 4453 CD ARG B 333 24.018 -22.646 -19.225 1.00114.08 C
ANISOU 4453 CD ARG B 333 14562 12563 16221 2867 1767 -716 C
ATOM 4454 NE ARG B 333 24.421 -22.406 -20.609 1.00124.30 N
ANISOU 4454 NE ARG B 333 15730 13931 17566 2902 2157 -980 N
ATOM 4455 CZ ARG B 333 24.308 -23.297 -21.591 1.00133.66 C
ANISOU 4455 CZ ARG B 333 17067 14868 18850 3043 2533 -1222 C
ATOM 4456 NH1 ARG B 333 23.787 -24.491 -21.348 1.00135.24 N
ANISOU 4456 NH1 ARG B 333 17538 14714 19134 3162 2555 -1233 N
ATOM 4457 NH2 ARG B 333 24.715 -22.997 -22.819 1.00136.72 N
ANISOU 4457 NH2 ARG B 333 17355 15352 19239 3055 2891 -1455 N
ATOM 4458 N GLU B 334 26.397 -20.445 -14.857 1.00111.17 N
ANISOU 4458 N GLU B 334 13410 12870 15960 2683 166 465 N
ATOM 4459 CA GLU B 334 26.067 -20.585 -13.444 1.00116.16 C
ANISOU 4459 CA GLU B 334 14264 13463 16408 2588 -242 723 C
ATOM 4460 C GLU B 334 25.652 -19.252 -12.825 1.00114.04 C
ANISOU 4460 C GLU B 334 14153 13471 15708 2245 -499 723 C
ATOM 4461 O GLU B 334 24.641 -19.174 -12.116 1.00109.87 O
ANISOU 4461 O GLU B 334 14021 12910 14813 2069 -604 720 O
ATOM 4462 CB GLU B 334 27.259 -21.182 -12.696 1.00127.94 C
ANISOU 4462 CB GLU B 334 15427 14879 18306 2810 -545 1091 C
ATOM 4463 CG GLU B 334 27.304 -20.883 -11.200 1.00135.19 C
ANISOU 4463 CG GLU B 334 16474 15884 19007 2642 -1070 1407 C
ATOM 4464 CD GLU B 334 28.623 -21.288 -10.572 1.00144.34 C
ANISOU 4464 CD GLU B 334 17232 17016 20596 2829 -1413 1795 C
ATOM 4465 OE1 GLU B 334 28.947 -22.498 -10.586 1.00143.47 O
ANISOU 4465 OE1 GLU B 334 17012 16632 20869 3124 -1348 1936 O
ATOM 4466 OE2 GLU B 334 29.342 -20.389 -10.083 1.00149.84 O
ANISOU 4466 OE2 GLU B 334 17711 17952 21268 2678 -1756 1965 O
ATOM 4467 N ALA B 335 26.435 -18.193 -13.058 1.00116.33 N
ANISOU 4467 N ALA B 335 14134 14019 16047 2147 -592 731 N
ATOM 4468 CA ALA B 335 26.120 -16.887 -12.483 1.00110.24 C
ANISOU 4468 CA ALA B 335 13509 13486 14892 1823 -837 721 C
ATOM 4469 C ALA B 335 24.851 -16.262 -13.066 1.00100.06 C
ANISOU 4469 C ALA B 335 12545 12242 13231 1614 -568 409 C
ATOM 4470 O ALA B 335 24.131 -15.557 -12.348 1.00 95.62 O
ANISOU 4470 O ALA B 335 12278 11758 12297 1376 -730 397 O
ATOM 4471 CB ALA B 335 27.315 -15.952 -12.655 1.00115.96 C
ANISOU 4471 CB ALA B 335 13798 14450 15810 1770 -1003 817 C
ATOM 4472 N VAL B 336 24.544 -16.520 -14.341 1.00 92.22 N
ANISOU 4472 N VAL B 336 11517 11191 12331 1694 -160 163 N
ATOM 4473 CA VAL B 336 23.452 -15.806 -15.007 1.00 76.03 C
ANISOU 4473 CA VAL B 336 9707 9211 9969 1477 63 -105 C
ATOM 4474 C VAL B 336 22.090 -16.380 -14.616 1.00 74.63 C
ANISOU 4474 C VAL B 336 9969 8845 9542 1416 128 -163 C
ATOM 4475 O VAL B 336 21.173 -15.634 -14.251 1.00 75.48 O
ANISOU 4475 O VAL B 336 10330 9024 9324 1186 81 -224 O
ATOM 4476 CB VAL B 336 23.662 -15.822 -16.536 1.00 66.38 C
ANISOU 4476 CB VAL B 336 8299 8014 8908 1550 448 -331 C
ATOM 4477 CG1 VAL B 336 22.554 -15.045 -17.251 1.00 61.69 C
ANISOU 4477 CG1 VAL B 336 7936 7501 8003 1305 636 -573 C
ATOM 4478 CG2 VAL B 336 25.022 -15.240 -16.893 1.00 71.13 C
ANISOU 4478 CG2 VAL B 336 8440 8810 9774 1607 406 -248 C
ATOM 4479 N TYR B 337 21.925 -17.709 -14.675 1.00 78.26 N
ANISOU 4479 N TYR B 337 10519 9048 10169 1620 245 -135 N
ATOM 4480 CA TYR B 337 20.685 -18.298 -14.167 1.00 88.06 C
ANISOU 4480 CA TYR B 337 12157 10103 11198 1554 268 -137 C
ATOM 4481 C TYR B 337 20.464 -17.921 -12.707 1.00 96.40 C
ANISOU 4481 C TYR B 337 13401 11220 12007 1420 -62 75 C
ATOM 4482 O TYR B 337 19.343 -17.585 -12.307 1.00102.49 O
ANISOU 4482 O TYR B 337 14481 11987 12472 1234 -37 25 O
ATOM 4483 CB TYR B 337 20.679 -19.821 -14.330 1.00 97.08 C
ANISOU 4483 CB TYR B 337 13357 10936 12592 1797 395 -99 C
ATOM 4484 CG TYR B 337 20.557 -20.309 -15.757 1.00111.43 C
ANISOU 4484 CG TYR B 337 15140 12636 14562 1891 767 -359 C
ATOM 4485 CD1 TYR B 337 20.184 -19.445 -16.774 1.00110.52 C
ANISOU 4485 CD1 TYR B 337 15017 12683 14291 1718 965 -600 C
ATOM 4486 CD2 TYR B 337 20.794 -21.643 -16.080 1.00125.68 C
ANISOU 4486 CD2 TYR B 337 16949 14150 16655 2141 917 -362 C
ATOM 4487 CE1 TYR B 337 20.064 -19.888 -18.079 1.00114.30 C
ANISOU 4487 CE1 TYR B 337 15510 13059 14858 1775 1294 -838 C
ATOM 4488 CE2 TYR B 337 20.675 -22.099 -17.388 1.00130.63 C
ANISOU 4488 CE2 TYR B 337 17599 14651 17383 2211 1268 -626 C
ATOM 4489 CZ TYR B 337 20.310 -21.212 -18.382 1.00128.42 C
ANISOU 4489 CZ TYR B 337 17331 14558 16905 2017 1450 -864 C
ATOM 4490 OH TYR B 337 20.185 -21.637 -19.686 1.00136.67 O
ANISOU 4490 OH TYR B 337 18440 15490 17997 2055 1786 -1127 O
ATOM 4491 N ALA B 338 21.520 -17.975 -11.894 1.00 93.85 N
ANISOU 4491 N ALA B 338 12898 10950 11812 1506 -370 320 N
ATOM 4492 CA ALA B 338 21.407 -17.515 -10.515 1.00 82.63 C
ANISOU 4492 CA ALA B 338 11678 9610 10107 1347 -708 513 C
ATOM 4493 C ALA B 338 20.946 -16.065 -10.467 1.00 82.94 C
ANISOU 4493 C ALA B 338 11825 9867 9820 1070 -721 364 C
ATOM 4494 O ALA B 338 20.053 -15.711 -9.689 1.00 85.43 O
ANISOU 4494 O ALA B 338 12482 10182 9794 897 -765 365 O
ATOM 4495 CB ALA B 338 22.743 -17.693 -9.796 1.00 76.70 C
ANISOU 4495 CB ALA B 338 10667 8905 9568 1457 -1074 804 C
ATOM 4496 N ALA B 339 21.571 -15.198 -11.270 1.00 83.20 N
ANISOU 4496 N ALA B 339 11567 10080 9966 1029 -674 244 N
ATOM 4497 CA ALA B 339 21.163 -13.796 -11.304 1.00 74.12 C
ANISOU 4497 CA ALA B 339 10502 9114 8548 771 -681 101 C
ATOM 4498 C ALA B 339 19.676 -13.666 -11.617 1.00 72.22 C
ANISOU 4498 C ALA B 339 10573 8794 8073 652 -401 -92 C
ATOM 4499 O ALA B 339 18.930 -12.997 -10.894 1.00 76.65 O
ANISOU 4499 O ALA B 339 11410 9386 8329 469 -455 -110 O
ATOM 4500 CB ALA B 339 22.009 -13.031 -12.321 1.00 65.22 C
ANISOU 4500 CB ALA B 339 8996 8163 7623 761 -617 2 C
ATOM 4501 N PHE B 340 19.227 -14.305 -12.697 1.00 70.61 N
ANISOU 4501 N PHE B 340 10331 8478 8018 751 -98 -235 N
ATOM 4502 CA PHE B 340 17.824 -14.197 -13.087 1.00 67.29 C
ANISOU 4502 CA PHE B 340 10164 7982 7422 625 145 -394 C
ATOM 4503 C PHE B 340 16.909 -14.836 -12.053 1.00 66.51 C
ANISOU 4503 C PHE B 340 10406 7720 7146 608 113 -279 C
ATOM 4504 O PHE B 340 15.825 -14.310 -11.773 1.00 68.99 O
ANISOU 4504 O PHE B 340 10950 8031 7232 442 202 -337 O
ATOM 4505 CB PHE B 340 17.616 -14.829 -14.457 1.00 67.42 C
ANISOU 4505 CB PHE B 340 10086 7903 7628 717 434 -557 C
ATOM 4506 CG PHE B 340 18.124 -13.991 -15.584 1.00 64.55 C
ANISOU 4506 CG PHE B 340 9467 7715 7343 660 542 -708 C
ATOM 4507 CD1 PHE B 340 17.329 -13.008 -16.143 1.00 59.12 C
ANISOU 4507 CD1 PHE B 340 8847 7124 6493 449 655 -851 C
ATOM 4508 CD2 PHE B 340 19.400 -14.171 -16.077 1.00 62.25 C
ANISOU 4508 CD2 PHE B 340 8857 7492 7304 816 537 -685 C
ATOM 4509 CE1 PHE B 340 17.799 -12.225 -17.181 1.00 51.74 C
ANISOU 4509 CE1 PHE B 340 7687 6353 5618 381 746 -967 C
ATOM 4510 CE2 PHE B 340 19.869 -13.389 -17.115 1.00 53.70 C
ANISOU 4510 CE2 PHE B 340 7542 6580 6281 752 658 -809 C
ATOM 4511 CZ PHE B 340 19.068 -12.415 -17.668 1.00 45.25 C
ANISOU 4511 CZ PHE B 340 6564 5608 5019 526 755 -949 C
ATOM 4512 N THR B 341 17.329 -15.964 -11.470 1.00 69.97 N
ANISOU 4512 N THR B 341 10870 8014 7702 779 -3 -99 N
ATOM 4513 CA THR B 341 16.476 -16.642 -10.500 1.00 65.49 C
ANISOU 4513 CA THR B 341 10628 7285 6969 760 -24 34 C
ATOM 4514 C THR B 341 16.213 -15.752 -9.297 1.00 70.75 C
ANISOU 4514 C THR B 341 11518 8071 7293 577 -196 116 C
ATOM 4515 O THR B 341 15.086 -15.701 -8.788 1.00 78.72 O
ANISOU 4515 O THR B 341 12819 9014 8078 462 -78 114 O
ATOM 4516 CB THR B 341 17.101 -17.967 -10.058 1.00 65.32 C
ANISOU 4516 CB THR B 341 10576 7088 7153 976 -157 244 C
ATOM 4517 OG1 THR B 341 17.225 -18.838 -11.187 1.00 66.96 O
ANISOU 4517 OG1 THR B 341 10631 7142 7668 1147 54 135 O
ATOM 4518 CG2 THR B 341 16.223 -18.648 -9.006 1.00 70.19 C
ANISOU 4518 CG2 THR B 341 11543 7546 7580 935 -186 411 C
ATOM 4519 N PHE B 342 17.247 -15.050 -8.823 1.00 73.64 N
ANISOU 4519 N PHE B 342 11757 8604 7619 541 -470 190 N
ATOM 4520 CA PHE B 342 17.062 -14.082 -7.746 1.00 71.74 C
ANISOU 4520 CA PHE B 342 11756 8477 7026 343 -635 226 C
ATOM 4521 C PHE B 342 16.184 -12.923 -8.198 1.00 76.19 C
ANISOU 4521 C PHE B 342 12397 9118 7433 164 -413 -3 C
ATOM 4522 O PHE B 342 15.332 -12.445 -7.441 1.00 86.10 O
ANISOU 4522 O PHE B 342 13961 10358 8394 23 -352 -21 O
ATOM 4523 CB PHE B 342 18.416 -13.571 -7.269 1.00 64.09 C
ANISOU 4523 CB PHE B 342 10609 7662 6079 322 -1005 349 C
ATOM 4524 CG PHE B 342 18.332 -12.420 -6.307 1.00 61.99 C
ANISOU 4524 CG PHE B 342 10591 7518 5446 89 -1185 337 C
ATOM 4525 CD1 PHE B 342 18.080 -12.657 -4.968 1.00 64.31 C
ANISOU 4525 CD1 PHE B 342 11251 7763 5421 10 -1353 497 C
ATOM 4526 CD2 PHE B 342 18.513 -11.106 -6.741 1.00 64.24 C
ANISOU 4526 CD2 PHE B 342 10765 7952 5692 -58 -1181 164 C
ATOM 4527 CE1 PHE B 342 18.008 -11.607 -4.063 1.00 68.26 C
ANISOU 4527 CE1 PHE B 342 12031 8358 5548 -213 -1504 462 C
ATOM 4528 CE2 PHE B 342 18.439 -10.048 -5.852 1.00 67.69 C
ANISOU 4528 CE2 PHE B 342 11460 8468 5792 -275 -1340 131 C
ATOM 4529 CZ PHE B 342 18.186 -10.297 -4.507 1.00 73.14 C
ANISOU 4529 CZ PHE B 342 12541 9103 6143 -353 -1496 268 C
ATOM 4530 N SER B 343 16.388 -12.448 -9.429 1.00 70.46 N
ANISOU 4530 N SER B 343 11394 8470 6907 170 -282 -170 N
ATOM 4531 CA SER B 343 15.557 -11.368 -9.953 1.00 68.71 C
ANISOU 4531 CA SER B 343 11216 8307 6583 7 -82 -364 C
ATOM 4532 C SER B 343 14.096 -11.793 -10.044 1.00 69.12 C
ANISOU 4532 C SER B 343 11490 8205 6567 -21 198 -409 C
ATOM 4533 O SER B 343 13.190 -11.004 -9.751 1.00 72.65 O
ANISOU 4533 O SER B 343 12114 8653 6835 -165 321 -480 O
ATOM 4534 CB SER B 343 16.072 -10.916 -11.317 1.00 72.81 C
ANISOU 4534 CB SER B 343 11397 8933 7333 19 1 -502 C
ATOM 4535 OG SER B 343 17.425 -10.510 -11.265 1.00 83.89 O
ANISOU 4535 OG SER B 343 12555 10483 8837 40 -242 -441 O
ATOM 4536 N HIS B 344 13.843 -13.035 -10.459 1.00 71.03 N
ANISOU 4536 N HIS B 344 11715 8296 6976 114 308 -364 N
ATOM 4537 CA HIS B 344 12.467 -13.508 -10.528 1.00 70.17 C
ANISOU 4537 CA HIS B 344 11800 8030 6831 72 546 -377 C
ATOM 4538 C HIS B 344 11.851 -13.577 -9.136 1.00 74.66 C
ANISOU 4538 C HIS B 344 12692 8537 7137 12 526 -241 C
ATOM 4539 O HIS B 344 10.673 -13.250 -8.952 1.00 82.29 O
ANISOU 4539 O HIS B 344 13824 9449 7993 -97 728 -272 O
ATOM 4540 CB HIS B 344 12.431 -14.872 -11.226 1.00 73.12 C
ANISOU 4540 CB HIS B 344 12107 8234 7441 220 633 -356 C
ATOM 4541 CG HIS B 344 13.063 -14.878 -12.586 1.00 65.04 C
ANISOU 4541 CG HIS B 344 10807 7261 6643 284 689 -501 C
ATOM 4542 ND1 HIS B 344 13.446 -16.041 -13.225 1.00 67.89 N
ANISOU 4542 ND1 HIS B 344 11083 7483 7228 449 739 -506 N
ATOM 4543 CD2 HIS B 344 13.368 -13.865 -13.431 1.00 66.29 C
ANISOU 4543 CD2 HIS B 344 10774 7586 6829 202 722 -648 C
ATOM 4544 CE1 HIS B 344 13.959 -15.742 -14.405 1.00 71.18 C
ANISOU 4544 CE1 HIS B 344 11279 7986 7779 465 821 -661 C
ATOM 4545 NE2 HIS B 344 13.924 -14.428 -14.553 1.00 68.41 N
ANISOU 4545 NE2 HIS B 344 10853 7829 7310 311 805 -737 N
ATOM 4546 N TRP B 345 12.635 -14.015 -8.146 1.00 70.31 N
ANISOU 4546 N TRP B 345 12233 7991 6491 79 286 -73 N
ATOM 4547 CA TRP B 345 12.131 -14.100 -6.780 1.00 71.68 C
ANISOU 4547 CA TRP B 345 12751 8117 6365 9 257 68 C
ATOM 4548 C TRP B 345 11.906 -12.714 -6.183 1.00 71.50 C
ANISOU 4548 C TRP B 345 12891 8220 6057 -166 264 -29 C
ATOM 4549 O TRP B 345 10.971 -12.514 -5.401 1.00 78.55 O
ANISOU 4549 O TRP B 345 14077 9057 6711 -259 424 -8 O
ATOM 4550 CB TRP B 345 13.097 -14.896 -5.907 1.00 73.15 C
ANISOU 4550 CB TRP B 345 12995 8284 6515 107 -45 294 C
ATOM 4551 CG TRP B 345 12.704 -14.896 -4.460 1.00 71.01 C
ANISOU 4551 CG TRP B 345 13110 7993 5876 6 -108 447 C
ATOM 4552 CD1 TRP B 345 11.897 -15.796 -3.837 1.00 71.95 C
ANISOU 4552 CD1 TRP B 345 13478 7959 5901 19 14 601 C
ATOM 4553 CD2 TRP B 345 13.080 -13.940 -3.466 1.00 69.39 C
ANISOU 4553 CD2 TRP B 345 13115 7922 5328 -140 -295 455 C
ATOM 4554 NE1 TRP B 345 11.752 -15.470 -2.514 1.00 83.73 N
ANISOU 4554 NE1 TRP B 345 15326 9492 6995 -105 -67 710 N
ATOM 4555 CE2 TRP B 345 12.469 -14.332 -2.259 1.00 80.47 C
ANISOU 4555 CE2 TRP B 345 14913 9250 6411 -208 -261 612 C
ATOM 4556 CE3 TRP B 345 13.876 -12.790 -3.477 1.00 53.72 C
ANISOU 4556 CE3 TRP B 345 11038 6105 3267 -236 -491 347 C
ATOM 4557 CZ2 TRP B 345 12.630 -13.617 -1.073 1.00 71.88 C
ANISOU 4557 CZ2 TRP B 345 14101 8251 4957 -364 -403 634 C
ATOM 4558 CZ3 TRP B 345 14.037 -12.078 -2.295 1.00 56.00 C
ANISOU 4558 CZ3 TRP B 345 11651 6468 3159 -400 -661 379 C
ATOM 4559 CH2 TRP B 345 13.416 -12.497 -1.111 1.00 64.86 C
ANISOU 4559 CH2 TRP B 345 13107 7514 4023 -458 -603 505 C
ATOM 4560 N LEU B 346 12.763 -11.746 -6.519 1.00 70.52 N
ANISOU 4560 N LEU B 346 12585 8251 5957 -214 105 -136 N
ATOM 4561 CA LEU B 346 12.635 -10.422 -5.923 1.00 75.49 C
ANISOU 4561 CA LEU B 346 13390 8973 6321 -384 86 -237 C
ATOM 4562 C LEU B 346 11.293 -9.797 -6.272 1.00 83.63 C
ANISOU 4562 C LEU B 346 14363 9940 7471 -455 425 -362 C
ATOM 4563 O LEU B 346 10.712 -9.065 -5.462 1.00 93.37 O
ANISOU 4563 O LEU B 346 15652 11159 8665 -541 497 -376 O
ATOM 4564 CB LEU B 346 13.781 -9.527 -6.397 1.00 71.25 C
ANISOU 4564 CB LEU B 346 12597 8597 5878 -427 -144 -321 C
ATOM 4565 CG LEU B 346 15.013 -9.349 -5.498 1.00 66.16 C
ANISOU 4565 CG LEU B 346 11999 8052 5085 -469 -546 -198 C
ATOM 4566 CD1 LEU B 346 15.866 -8.217 -6.030 1.00 48.36 C
ANISOU 4566 CD1 LEU B 346 9500 5947 2926 -560 -706 -309 C
ATOM 4567 CD2 LEU B 346 14.685 -9.170 -4.026 1.00 85.54 C
ANISOU 4567 CD2 LEU B 346 14908 10473 7119 -592 -628 -126 C
ATOM 4568 N VAL B 347 10.779 -10.075 -7.473 1.00 78.37 N
ANISOU 4568 N VAL B 347 13501 9228 7046 -409 615 -431 N
ATOM 4569 CA VAL B 347 9.500 -9.501 -7.864 1.00 59.87 C
ANISOU 4569 CA VAL B 347 10984 6827 4937 -471 858 -482 C
ATOM 4570 C VAL B 347 8.408 -9.958 -6.902 1.00 68.82 C
ANISOU 4570 C VAL B 347 12313 7821 6012 -479 1018 -374 C
ATOM 4571 O VAL B 347 7.671 -9.138 -6.338 1.00 75.10 O
ANISOU 4571 O VAL B 347 13114 8592 6829 -547 1125 -393 O
ATOM 4572 CB VAL B 347 9.189 -9.849 -9.332 1.00 47.11 C
ANISOU 4572 CB VAL B 347 9137 5186 3576 -442 976 -543 C
ATOM 4573 CG1 VAL B 347 7.780 -9.410 -9.683 1.00 46.60 C
ANISOU 4573 CG1 VAL B 347 8936 5041 3727 -513 1176 -536 C
ATOM 4574 CG2 VAL B 347 10.197 -9.193 -10.249 1.00 55.81 C
ANISOU 4574 CG2 VAL B 347 10025 6437 4743 -453 851 -663 C
ATOM 4575 N TYR B 348 8.296 -11.276 -6.694 1.00 68.75 N
ANISOU 4575 N TYR B 348 12486 7708 5926 -404 1047 -256 N
ATOM 4576 CA TYR B 348 7.311 -11.803 -5.757 1.00 72.71 C
ANISOU 4576 CA TYR B 348 13179 8083 6366 -415 1197 -138 C
ATOM 4577 C TYR B 348 7.624 -11.394 -4.319 1.00 77.79 C
ANISOU 4577 C TYR B 348 14036 8773 6746 -462 1088 -92 C
ATOM 4578 O TYR B 348 6.709 -11.279 -3.491 1.00 81.34 O
ANISOU 4578 O TYR B 348 14596 9151 7159 -504 1251 -59 O
ATOM 4579 CB TYR B 348 7.268 -13.330 -5.871 1.00 74.96 C
ANISOU 4579 CB TYR B 348 13621 8242 6618 -325 1223 5 C
ATOM 4580 CG TYR B 348 7.072 -13.832 -7.290 1.00 75.21 C
ANISOU 4580 CG TYR B 348 13492 8211 6872 -285 1323 -56 C
ATOM 4581 CD1 TYR B 348 5.861 -13.663 -7.949 1.00 69.35 C
ANISOU 4581 CD1 TYR B 348 12584 7389 6376 -354 1529 -99 C
ATOM 4582 CD2 TYR B 348 8.110 -14.469 -7.973 1.00 78.05 C
ANISOU 4582 CD2 TYR B 348 13731 8585 7340 -171 1148 -68 C
ATOM 4583 CE1 TYR B 348 5.683 -14.114 -9.245 1.00 66.11 C
ANISOU 4583 CE1 TYR B 348 12044 6922 6152 -349 1595 -160 C
ATOM 4584 CE2 TYR B 348 7.940 -14.925 -9.272 1.00 72.92 C
ANISOU 4584 CE2 TYR B 348 12867 7870 6969 -139 1218 -154 C
ATOM 4585 CZ TYR B 348 6.724 -14.745 -9.902 1.00 72.15 C
ANISOU 4585 CZ TYR B 348 12736 7701 6977 -243 1445 -205 C
ATOM 4586 OH TYR B 348 6.545 -15.195 -11.190 1.00 85.37 O
ANISOU 4586 OH TYR B 348 14239 9309 8889 -243 1487 -289 O
ATOM 4587 N ALA B 349 8.901 -11.161 -4.008 1.00 67.75 N
ANISOU 4587 N ALA B 349 12835 7622 5286 -465 810 -92 N
ATOM 4588 CA ALA B 349 9.249 -10.651 -2.690 1.00 53.72 C
ANISOU 4588 CA ALA B 349 11258 5897 3255 -543 674 -63 C
ATOM 4589 C ALA B 349 8.631 -9.279 -2.444 1.00 56.94 C
ANISOU 4589 C ALA B 349 11592 6315 3726 -635 822 -207 C
ATOM 4590 O ALA B 349 8.284 -8.952 -1.305 1.00 85.20 O
ANISOU 4590 O ALA B 349 15374 9865 7132 -696 873 -195 O
ATOM 4591 CB ALA B 349 10.774 -10.592 -2.540 1.00 53.58 C
ANISOU 4591 CB ALA B 349 11291 6008 3059 -548 295 -23 C
ATOM 4592 N ASN B 350 8.493 -8.460 -3.490 1.00 52.00 N
ANISOU 4592 N ASN B 350 10696 5724 3338 -644 892 -334 N
ATOM 4593 CA ASN B 350 7.861 -7.155 -3.327 1.00 55.44 C
ANISOU 4593 CA ASN B 350 11068 6142 3855 -714 1032 -442 C
ATOM 4594 C ASN B 350 6.397 -7.297 -2.941 1.00 57.05 C
ANISOU 4594 C ASN B 350 11338 6199 4140 -708 1335 -405 C
ATOM 4595 O ASN B 350 5.856 -6.429 -2.250 1.00 55.73 O
ANISOU 4595 O ASN B 350 11268 5983 3924 -758 1462 -458 O
ATOM 4596 CB ASN B 350 7.994 -6.331 -4.610 1.00 51.79 C
ANISOU 4596 CB ASN B 350 10294 5743 3643 -722 1028 -547 C
ATOM 4597 CG ASN B 350 7.267 -4.990 -4.532 1.00 66.89 C
ANISOU 4597 CG ASN B 350 12146 7608 5660 -783 1179 -633 C
ATOM 4598 OD1 ASN B 350 6.045 -4.920 -4.670 1.00 63.91 O
ANISOU 4598 OD1 ASN B 350 11728 7116 5439 -774 1420 -613 O
ATOM 4599 ND2 ASN B 350 8.026 -3.916 -4.313 1.00 83.16 N
ANISOU 4599 ND2 ASN B 350 14217 9746 7636 -848 1033 -721 N
ATOM 4600 N SER B 351 5.729 -8.365 -3.389 1.00 63.72 N
ANISOU 4600 N SER B 351 12140 6959 5111 -649 1464 -318 N
ATOM 4601 CA SER B 351 4.319 -8.544 -3.045 1.00 60.26 C
ANISOU 4601 CA SER B 351 11750 6380 4766 -647 1748 -272 C
ATOM 4602 C SER B 351 4.143 -8.759 -1.552 1.00 58.89 C
ANISOU 4602 C SER B 351 11886 6170 4320 -668 1801 -214 C
ATOM 4603 O SER B 351 3.241 -8.177 -0.938 1.00 71.65 O
ANISOU 4603 O SER B 351 13580 7707 5936 -695 2018 -243 O
ATOM 4604 CB SER B 351 3.731 -9.722 -3.823 1.00 75.02 C
ANISOU 4604 CB SER B 351 13526 8166 6814 -595 1843 -183 C
ATOM 4605 OG SER B 351 3.818 -9.481 -5.217 1.00 81.98 O
ANISOU 4605 OG SER B 351 14139 9077 7933 -596 1807 -245 O
ATOM 4606 N ALA B 352 5.003 -9.585 -0.949 1.00 60.12 N
ANISOU 4606 N ALA B 352 12232 6379 4232 -657 1606 -124 N
ATOM 4607 CA ALA B 352 5.012 -9.731 0.501 1.00 64.75 C
ANISOU 4607 CA ALA B 352 13131 6958 4514 -701 1603 -62 C
ATOM 4608 C ALA B 352 5.594 -8.509 1.203 1.00 70.35 C
ANISOU 4608 C ALA B 352 13962 7736 5032 -788 1494 -176 C
ATOM 4609 O ALA B 352 5.332 -8.306 2.393 1.00 72.66 O
ANISOU 4609 O ALA B 352 14517 8000 5090 -845 1568 -170 O
ATOM 4610 CB ALA B 352 5.800 -10.979 0.905 1.00 57.39 C
ANISOU 4610 CB ALA B 352 12363 6059 3382 -674 1384 103 C
ATOM 4611 N ALA B 353 6.380 -7.697 0.497 1.00 71.84 N
ANISOU 4611 N ALA B 353 13978 8011 5305 -806 1323 -281 N
ATOM 4612 CA ALA B 353 7.035 -6.562 1.135 1.00 74.28 C
ANISOU 4612 CA ALA B 353 14411 8381 5432 -900 1186 -384 C
ATOM 4613 C ALA B 353 6.039 -5.464 1.490 1.00 78.20 C
ANISOU 4613 C ALA B 353 14954 8777 5981 -936 1465 -494 C
ATOM 4614 O ALA B 353 6.152 -4.827 2.544 1.00 89.02 O
ANISOU 4614 O ALA B 353 16584 10131 7109 -1017 1463 -550 O
ATOM 4615 CB ALA B 353 8.124 -6.007 0.217 1.00 55.53 C
ANISOU 4615 CB ALA B 353 11815 6125 3159 -910 936 -456 C
ATOM 4616 N ASN B 354 5.077 -5.207 0.609 1.00 70.09 N
ANISOU 4616 N ASN B 354 13693 7673 5265 -884 1697 -524 N
ATOM 4617 CA ASN B 354 4.200 -4.054 0.806 1.00 67.51 C
ANISOU 4617 CA ASN B 354 13386 7243 5022 -910 1945 -621 C
ATOM 4618 C ASN B 354 3.425 -4.097 2.109 1.00 71.70 C
ANISOU 4618 C ASN B 354 14230 7667 5347 -932 2177 -608 C
ATOM 4619 O ASN B 354 3.464 -3.103 2.861 1.00 76.62 O
ANISOU 4619 O ASN B 354 15053 8252 5806 -997 2230 -710 O
ATOM 4620 CB ASN B 354 3.265 -3.918 -0.393 1.00 65.27 C
ANISOU 4620 CB ASN B 354 12795 6890 5116 -854 2132 -615 C
ATOM 4621 CG ASN B 354 4.011 -3.631 -1.667 1.00 69.91 C
ANISOU 4621 CG ASN B 354 13093 7585 5886 -852 1927 -652 C
ATOM 4622 OD1 ASN B 354 4.976 -2.874 -1.662 1.00 66.54 O
ANISOU 4622 OD1 ASN B 354 12667 7249 5365 -901 1730 -732 O
ATOM 4623 ND2 ASN B 354 3.572 -4.228 -2.768 1.00 76.68 N
ANISOU 4623 ND2 ASN B 354 13708 8430 6998 -803 1974 -594 N
ATOM 4624 N PRO B 355 2.736 -5.182 2.455 1.00 72.94 N
ANISOU 4624 N PRO B 355 14460 7770 5484 -886 2325 -492 N
ATOM 4625 CA PRO B 355 1.995 -5.190 3.724 1.00 75.11 C
ANISOU 4625 CA PRO B 355 15039 7953 5546 -911 2567 -480 C
ATOM 4626 C PRO B 355 2.878 -4.954 4.933 1.00 82.56 C
ANISOU 4626 C PRO B 355 16332 8960 6077 -1008 2388 -515 C
ATOM 4627 O PRO B 355 2.429 -4.341 5.909 1.00 85.95 O
ANISOU 4627 O PRO B 355 17027 9311 6319 -1058 2580 -584 O
ATOM 4628 CB PRO B 355 1.347 -6.590 3.756 1.00 75.03 C
ANISOU 4628 CB PRO B 355 15011 7911 5584 -849 2680 -320 C
ATOM 4629 CG PRO B 355 1.369 -7.056 2.344 1.00 71.73 C
ANISOU 4629 CG PRO B 355 14248 7514 5492 -786 2594 -280 C
ATOM 4630 CD PRO B 355 2.568 -6.438 1.702 1.00 76.71 C
ANISOU 4630 CD PRO B 355 14757 8260 6131 -815 2297 -367 C
ATOM 4631 N ILE B 356 4.120 -5.450 4.912 1.00 82.54 N
ANISOU 4631 N ILE B 356 16351 9090 5922 -1041 2025 -464 N
ATOM 4632 CA ILE B 356 5.017 -5.174 6.027 1.00 82.57 C
ANISOU 4632 CA ILE B 356 16682 9155 5537 -1155 1807 -487 C
ATOM 4633 C ILE B 356 5.311 -3.682 6.115 1.00 81.74 C
ANISOU 4633 C ILE B 356 16628 9029 5399 -1232 1788 -665 C
ATOM 4634 O ILE B 356 5.502 -3.131 7.209 1.00 83.31 O
ANISOU 4634 O ILE B 356 17162 9203 5287 -1336 1777 -731 O
ATOM 4635 CB ILE B 356 6.311 -5.992 5.895 1.00 78.28 C
ANISOU 4635 CB ILE B 356 16116 8751 4877 -1173 1397 -373 C
ATOM 4636 CG1 ILE B 356 5.979 -7.484 5.843 1.00 71.82 C
ANISOU 4636 CG1 ILE B 356 15276 7928 4085 -1095 1432 -186 C
ATOM 4637 CG2 ILE B 356 7.231 -5.671 7.053 1.00 88.16 C
ANISOU 4637 CG2 ILE B 356 17702 10061 5732 -1312 1137 -379 C
ATOM 4638 CD1 ILE B 356 7.170 -8.354 5.539 1.00 71.14 C
ANISOU 4638 CD1 ILE B 356 15132 7953 3946 -1082 1053 -52 C
ATOM 4639 N ILE B 357 5.393 -3.015 4.961 1.00 79.03 N
ANISOU 4639 N ILE B 357 15968 8697 5363 -1190 1769 -740 N
ATOM 4640 CA ILE B 357 5.608 -1.574 4.944 1.00 78.07 C
ANISOU 4640 CA ILE B 357 15872 8544 5246 -1256 1766 -900 C
ATOM 4641 C ILE B 357 4.440 -0.865 5.616 1.00 76.92 C
ANISOU 4641 C ILE B 357 15927 8232 5068 -1260 2153 -984 C
ATOM 4642 O ILE B 357 4.628 0.097 6.369 1.00 85.79 O
ANISOU 4642 O ILE B 357 17313 9303 5981 -1352 2169 -1105 O
ATOM 4643 CB ILE B 357 5.813 -1.084 3.496 1.00 71.47 C
ANISOU 4643 CB ILE B 357 14636 7753 4765 -1205 1696 -939 C
ATOM 4644 CG1 ILE B 357 7.020 -1.770 2.848 1.00 64.68 C
ANISOU 4644 CG1 ILE B 357 13595 7056 3925 -1198 1333 -866 C
ATOM 4645 CG2 ILE B 357 5.989 0.417 3.465 1.00 76.56 C
ANISOU 4645 CG2 ILE B 357 15308 8355 5427 -1273 1704 -1093 C
ATOM 4646 CD1 ILE B 357 7.148 -1.506 1.358 1.00 59.32 C
ANISOU 4646 CD1 ILE B 357 12519 6429 3591 -1138 1293 -888 C
ATOM 4647 N TYR B 358 3.214 -1.328 5.356 1.00 78.28 N
ANISOU 4647 N TYR B 358 15987 8308 5449 -1164 2475 -920 N
ATOM 4648 CA TYR B 358 2.054 -0.700 5.976 1.00 88.66 C
ANISOU 4648 CA TYR B 358 17477 9453 6758 -1154 2873 -987 C
ATOM 4649 C TYR B 358 2.060 -0.928 7.480 1.00100.83 C
ANISOU 4649 C TYR B 358 19465 10968 7878 -1230 2941 -994 C
ATOM 4650 O TYR B 358 1.696 -0.034 8.255 1.00111.32 O
ANISOU 4650 O TYR B 358 21065 12184 9047 -1281 3149 -1113 O
ATOM 4651 CB TYR B 358 0.757 -1.235 5.358 1.00 81.51 C
ANISOU 4651 CB TYR B 358 16334 8451 6183 -1039 3183 -893 C
ATOM 4652 CG TYR B 358 0.701 -1.157 3.854 1.00 80.79 C
ANISOU 4652 CG TYR B 358 15819 8388 6490 -978 3107 -866 C
ATOM 4653 CD1 TYR B 358 1.407 -0.181 3.160 1.00 78.12 C
ANISOU 4653 CD1 TYR B 358 15334 8103 6247 -1015 2920 -961 C
ATOM 4654 CD2 TYR B 358 -0.058 -2.060 3.126 1.00 83.68 C
ANISOU 4654 CD2 TYR B 358 15942 8729 7126 -895 3218 -744 C
ATOM 4655 CE1 TYR B 358 1.359 -0.112 1.771 1.00 70.63 C
ANISOU 4655 CE1 TYR B 358 14009 7188 5639 -971 2853 -932 C
ATOM 4656 CE2 TYR B 358 -0.113 -1.998 1.751 1.00 84.37 C
ANISOU 4656 CE2 TYR B 358 15669 8839 7548 -857 3142 -722 C
ATOM 4657 CZ TYR B 358 0.597 -1.023 1.080 1.00 79.22 C
ANISOU 4657 CZ TYR B 358 14881 8247 6970 -897 2963 -814 C
ATOM 4658 OH TYR B 358 0.544 -0.958 -0.289 1.00 85.40 O
ANISOU 4658 OH TYR B 358 15323 9061 8064 -871 2892 -789 O
ATOM 4659 N ASN B 359 2.481 -2.118 7.910 1.00 97.03 N
ANISOU 4659 N ASN B 359 19081 10584 7199 -1245 2768 -864 N
ATOM 4660 CA ASN B 359 2.453 -2.432 9.331 1.00 99.42 C
ANISOU 4660 CA ASN B 359 19814 10874 7087 -1327 2827 -845 C
ATOM 4661 C ASN B 359 3.422 -1.561 10.108 1.00 96.39 C
ANISOU 4661 C ASN B 359 19745 10519 6359 -1475 2600 -968 C
ATOM 4662 O ASN B 359 3.173 -1.247 11.277 1.00107.71 O
ANISOU 4662 O ASN B 359 21577 11883 7465 -1559 2752 -1030 O
ATOM 4663 CB ASN B 359 2.773 -3.911 9.547 1.00110.06 C
ANISOU 4663 CB ASN B 359 21180 12328 8309 -1317 2650 -655 C
ATOM 4664 CG ASN B 359 2.735 -4.305 11.009 1.00118.39 C
ANISOU 4664 CG ASN B 359 22680 13383 8920 -1412 2698 -608 C
ATOM 4665 OD1 ASN B 359 1.662 -4.412 11.600 1.00119.40 O
ANISOU 4665 OD1 ASN B 359 22958 13412 8998 -1386 3072 -600 O
ATOM 4666 ND2 ASN B 359 3.905 -4.546 11.596 1.00123.71 N
ANISOU 4666 ND2 ASN B 359 23564 14172 9270 -1528 2317 -563 N
ATOM 4667 N PHE B 360 4.533 -1.179 9.484 1.00 92.68 N
ANISOU 4667 N PHE B 360 19113 10149 5952 -1517 2238 -1002 N
ATOM 4668 CA PHE B 360 5.539 -0.343 10.128 1.00 92.75 C
ANISOU 4668 CA PHE B 360 19390 10188 5664 -1671 1974 -1110 C
ATOM 4669 C PHE B 360 5.295 1.145 9.911 1.00 96.85 C
ANISOU 4669 C PHE B 360 19914 10592 6292 -1692 2132 -1302 C
ATOM 4670 O PHE B 360 5.477 1.940 10.837 1.00110.41 O
ANISOU 4670 O PHE B 360 22000 12240 7711 -1815 2146 -1426 O
ATOM 4671 CB PHE B 360 6.932 -0.719 9.626 1.00 90.06 C
ANISOU 4671 CB PHE B 360 18877 10015 5327 -1715 1482 -1031 C
ATOM 4672 CG PHE B 360 7.453 -2.012 10.192 1.00 98.70 C
ANISOU 4672 CG PHE B 360 20099 11213 6188 -1746 1247 -848 C
ATOM 4673 CD1 PHE B 360 7.600 -3.128 9.380 1.00 97.35 C
ANISOU 4673 CD1 PHE B 360 19624 11129 6235 -1635 1138 -691 C
ATOM 4674 CD2 PHE B 360 7.792 -2.105 11.539 1.00106.06 C
ANISOU 4674 CD2 PHE B 360 21473 12150 6675 -1893 1132 -826 C
ATOM 4675 CE1 PHE B 360 8.079 -4.313 9.899 1.00 98.45 C
ANISOU 4675 CE1 PHE B 360 19885 11352 6169 -1659 918 -506 C
ATOM 4676 CE2 PHE B 360 8.272 -3.282 12.072 1.00106.22 C
ANISOU 4676 CE2 PHE B 360 21611 12266 6481 -1929 897 -633 C
ATOM 4677 CZ PHE B 360 8.416 -4.392 11.253 1.00103.60 C
ANISOU 4677 CZ PHE B 360 20962 12016 6387 -1806 790 -466 C
ATOM 4678 N LEU B 361 4.887 1.546 8.710 1.00 91.65 N
ANISOU 4678 N LEU B 361 18871 9907 6046 -1583 2247 -1327 N
ATOM 4679 CA LEU B 361 4.782 2.961 8.382 1.00 91.43 C
ANISOU 4679 CA LEU B 361 18812 9783 6145 -1604 2346 -1490 C
ATOM 4680 C LEU B 361 3.340 3.446 8.313 1.00 93.81 C
ANISOU 4680 C LEU B 361 19094 9900 6649 -1509 2838 -1541 C
ATOM 4681 O LEU B 361 3.095 4.580 7.886 1.00 95.93 O
ANISOU 4681 O LEU B 361 19286 10072 7092 -1500 2962 -1657 O
ATOM 4682 CB LEU B 361 5.498 3.244 7.059 1.00 87.21 C
ANISOU 4682 CB LEU B 361 17867 9355 5915 -1575 2082 -1483 C
ATOM 4683 CG LEU B 361 7.002 2.965 7.045 1.00 88.50 C
ANISOU 4683 CG LEU B 361 18020 9688 5917 -1672 1594 -1443 C
ATOM 4684 CD1 LEU B 361 7.514 2.869 5.614 1.00 88.23 C
ANISOU 4684 CD1 LEU B 361 17527 9770 6227 -1603 1402 -1395 C
ATOM 4685 CD2 LEU B 361 7.782 4.023 7.832 1.00 94.34 C
ANISOU 4685 CD2 LEU B 361 19079 10397 6368 -1840 1408 -1580 C
ATOM 4686 N SER B 362 2.383 2.624 8.733 1.00 87.87 N
ANISOU 4686 N SER B 362 18411 9090 5886 -1439 3121 -1451 N
ATOM 4687 CA SER B 362 0.980 3.023 8.760 1.00 89.00 C
ANISOU 4687 CA SER B 362 18546 9047 6222 -1349 3606 -1481 C
ATOM 4688 C SER B 362 0.354 2.438 10.014 1.00 93.78 C
ANISOU 4688 C SER B 362 19516 9587 6529 -1364 3864 -1452 C
ATOM 4689 O SER B 362 0.165 1.222 10.103 1.00 93.05 O
ANISOU 4689 O SER B 362 19370 9566 6417 -1324 3848 -1302 O
ATOM 4690 CB SER B 362 0.238 2.548 7.509 1.00109.18 C
ANISOU 4690 CB SER B 362 20642 11598 9244 -1213 3720 -1360 C
ATOM 4691 OG SER B 362 -1.134 2.896 7.551 1.00105.84 O
ANISOU 4691 OG SER B 362 20200 10987 9029 -1129 4182 -1366 O
ATOM 4692 N GLY B 363 0.027 3.297 10.978 1.00143.67 N
ANISOU 4692 N GLY B 363 26213 15766 12611 -1423 4114 -1596 N
ATOM 4693 CA GLY B 363 -0.585 2.807 12.194 1.00103.97 C
ANISOU 4693 CA GLY B 363 21554 10673 7276 -1444 4390 -1577 C
ATOM 4694 C GLY B 363 -2.013 2.355 11.994 1.00103.69 C
ANISOU 4694 C GLY B 363 21346 10522 7529 -1300 4839 -1482 C
ATOM 4695 O GLY B 363 -2.541 1.611 12.823 1.00121.41 O
ANISOU 4695 O GLY B 363 23801 12753 9574 -1296 5043 -1409 O
ATOM 4696 N LYS B 364 -2.654 2.798 10.913 1.00110.68 N
ANISOU 4696 N LYS B 364 21850 11323 8879 -1188 4993 -1470 N
ATOM 4697 CA LYS B 364 -4.002 2.331 10.610 1.00116.58 C
ANISOU 4697 CA LYS B 364 22383 11960 9953 -1054 5385 -1354 C
ATOM 4698 C LYS B 364 -3.966 0.916 10.049 1.00116.40 C
ANISOU 4698 C LYS B 364 22085 12080 10064 -1005 5192 -1158 C
ATOM 4699 O LYS B 364 -4.780 0.068 10.433 1.00110.48 O
ANISOU 4699 O LYS B 364 21356 11299 9323 -950 5435 -1042 O
ATOM 4700 CB LYS B 364 -4.655 3.297 9.620 1.00124.51 C
ANISOU 4700 CB LYS B 364 23076 12822 11412 -967 5581 -1392 C
ATOM 4701 CG LYS B 364 -4.576 4.744 10.074 1.00137.55 C
ANISOU 4701 CG LYS B 364 24985 14332 12948 -1016 5738 -1593 C
ATOM 4702 CD LYS B 364 -4.829 5.715 8.935 1.00137.86 C
ANISOU 4702 CD LYS B 364 24686 14281 13414 -958 5781 -1624 C
ATOM 4703 CE LYS B 364 -4.879 7.149 9.438 1.00144.00 C
ANISOU 4703 CE LYS B 364 25733 14887 14092 -994 5996 -1823 C
ATOM 4704 NZ LYS B 364 -4.995 8.114 8.312 1.00144.71 N
ANISOU 4704 NZ LYS B 364 25497 14906 14579 -951 5993 -1849 N
ATOM 4705 N PHE B 365 -3.030 0.648 9.130 1.00116.04 N
ANISOU 4705 N PHE B 365 21779 12185 10124 -1024 4769 -1120 N
ATOM 4706 CA PHE B 365 -2.792 -0.719 8.681 1.00108.26 C
ANISOU 4706 CA PHE B 365 20592 11341 9201 -993 4547 -952 C
ATOM 4707 C PHE B 365 -2.221 -1.562 9.812 1.00111.26 C
ANISOU 4707 C PHE B 365 21318 11826 9131 -1075 4406 -901 C
ATOM 4708 O PHE B 365 -2.625 -2.715 10.006 1.00106.68 O
ANISOU 4708 O PHE B 365 20718 11281 8534 -1037 4469 -752 O
ATOM 4709 CB PHE B 365 -1.857 -0.720 7.475 1.00 98.91 C
ANISOU 4709 CB PHE B 365 19082 10286 8211 -997 4147 -941 C
ATOM 4710 CG PHE B 365 -2.555 -0.469 6.172 1.00 91.18 C
ANISOU 4710 CG PHE B 365 17690 9239 7714 -906 4260 -905 C
ATOM 4711 CD1 PHE B 365 -3.312 -1.464 5.579 1.00 85.87 C
ANISOU 4711 CD1 PHE B 365 16768 8554 7304 -822 4359 -757 C
ATOM 4712 CD2 PHE B 365 -2.441 0.761 5.532 1.00 85.59 C
ANISOU 4712 CD2 PHE B 365 16851 8479 7189 -915 4252 -1014 C
ATOM 4713 CE1 PHE B 365 -3.953 -1.238 4.377 1.00 87.32 C
ANISOU 4713 CE1 PHE B 365 16587 8672 7919 -755 4442 -719 C
ATOM 4714 CE2 PHE B 365 -3.076 1.001 4.327 1.00 81.70 C
ANISOU 4714 CE2 PHE B 365 15991 7926 7128 -847 4342 -967 C
ATOM 4715 CZ PHE B 365 -3.836 -0.002 3.745 1.00 87.13 C
ANISOU 4715 CZ PHE B 365 16438 8598 8069 -770 4432 -820 C
ATOM 4716 N ARG B 366 -1.281 -0.997 10.573 1.00115.21 N
ANISOU 4716 N ARG B 366 22143 12373 9259 -1196 4205 -1014 N
ATOM 4717 CA ARG B 366 -0.721 -1.719 11.708 1.00107.98 C
ANISOU 4717 CA ARG B 366 21590 11551 7888 -1296 4056 -959 C
ATOM 4718 C ARG B 366 -1.818 -2.107 12.690 1.00102.27 C
ANISOU 4718 C ARG B 366 21119 10730 7007 -1275 4478 -914 C
ATOM 4719 O ARG B 366 -1.773 -3.189 13.288 1.00103.99 O
ANISOU 4719 O ARG B 366 21477 11032 7004 -1302 4429 -775 O
ATOM 4720 CB ARG B 366 0.359 -0.880 12.403 1.00110.19 C
ANISOU 4720 CB ARG B 366 22204 11866 7797 -1447 3798 -1101 C
ATOM 4721 CG ARG B 366 1.116 -1.651 13.482 1.00108.64 C
ANISOU 4721 CG ARG B 366 22364 11787 7128 -1572 3549 -1020 C
ATOM 4722 CD ARG B 366 1.973 -0.787 14.419 1.00110.50 C
ANISOU 4722 CD ARG B 366 23024 12022 6940 -1748 3360 -1164 C
ATOM 4723 NE ARG B 366 3.157 -0.200 13.786 1.00106.65 N
ANISOU 4723 NE ARG B 366 22384 11615 6523 -1808 2941 -1227 N
ATOM 4724 CZ ARG B 366 3.401 1.105 13.675 1.00108.98 C
ANISOU 4724 CZ ARG B 366 22737 11831 6837 -1862 2938 -1410 C
ATOM 4725 NH1 ARG B 366 2.542 1.995 14.157 1.00113.07 N
ANISOU 4725 NH1 ARG B 366 23479 12173 7309 -1857 3341 -1559 N
ATOM 4726 NH2 ARG B 366 4.521 1.521 13.093 1.00109.08 N
ANISOU 4726 NH2 ARG B 366 22593 11937 6917 -1920 2537 -1440 N
ATOM 4727 N GLU B 367 -2.814 -1.233 12.871 1.00104.57 N
ANISOU 4727 N GLU B 367 21472 10843 7417 -1227 4908 -1020 N
ATOM 4728 CA GLU B 367 -3.941 -1.556 13.742 1.00109.14 C
ANISOU 4728 CA GLU B 367 22259 11318 7889 -1191 5362 -976 C
ATOM 4729 C GLU B 367 -4.817 -2.665 13.170 1.00106.57 C
ANISOU 4729 C GLU B 367 21600 11004 7889 -1070 5514 -778 C
ATOM 4730 O GLU B 367 -5.379 -3.458 13.929 1.00109.86 O
ANISOU 4730 O GLU B 367 22179 11428 8135 -1069 5724 -667 O
ATOM 4731 CB GLU B 367 -4.772 -0.300 13.980 1.00112.26 C
ANISOU 4731 CB GLU B 367 22770 11503 8380 -1154 5796 -1137 C
ATOM 4732 CG GLU B 367 -5.797 -0.416 15.083 1.00133.27 C
ANISOU 4732 CG GLU B 367 25741 14048 10848 -1138 6287 -1133 C
ATOM 4733 CD GLU B 367 -6.252 0.943 15.563 1.00143.13 C
ANISOU 4733 CD GLU B 367 27240 15094 12049 -1141 6650 -1335 C
ATOM 4734 OE1 GLU B 367 -7.092 1.017 16.483 1.00128.24 O
ANISOU 4734 OE1 GLU B 367 25634 13089 10002 -1125 7098 -1360 O
ATOM 4735 OE2 GLU B 367 -5.758 1.947 15.016 1.00150.03 O
ANISOU 4735 OE2 GLU B 367 28034 15926 13045 -1160 6495 -1468 O
ATOM 4736 N GLN B 368 -4.947 -2.739 11.844 1.00117.23 N
ANISOU 4736 N GLN B 368 22493 12356 9694 -979 5410 -726 N
ATOM 4737 CA GLN B 368 -5.741 -3.798 11.229 1.00123.37 C
ANISOU 4737 CA GLN B 368 22948 13139 10788 -878 5519 -541 C
ATOM 4738 C GLN B 368 -5.008 -5.134 11.184 1.00124.01 C
ANISOU 4738 C GLN B 368 23000 13399 10719 -914 5168 -386 C
ATOM 4739 O GLN B 368 -5.645 -6.186 11.315 1.00112.50 O
ANISOU 4739 O GLN B 368 21477 11956 9313 -873 5304 -219 O
ATOM 4740 CB GLN B 368 -6.154 -3.406 9.806 1.00115.61 C
ANISOU 4740 CB GLN B 368 21507 12089 10332 -782 5524 -539 C
ATOM 4741 CG GLN B 368 -7.119 -2.230 9.717 1.00116.29 C
ANISOU 4741 CG GLN B 368 21547 11971 10666 -719 5922 -635 C
ATOM 4742 CD GLN B 368 -8.177 -2.249 10.801 1.00116.90 C
ANISOU 4742 CD GLN B 368 21867 11921 10626 -687 6406 -616 C
ATOM 4743 OE1 GLN B 368 -8.671 -3.307 11.191 1.00102.56 O
ANISOU 4743 OE1 GLN B 368 20062 10146 8758 -665 6525 -467 O
ATOM 4744 NE2 GLN B 368 -8.499 -1.071 11.322 1.00104.79 N
ANISOU 4744 NE2 GLN B 368 20547 10235 9036 -689 6696 -766 N
ATOM 4745 N PHE B 369 -3.684 -5.121 10.990 1.00129.79 N
ANISOU 4745 N PHE B 369 23768 14261 11285 -989 4722 -426 N
ATOM 4746 CA PHE B 369 -2.949 -6.377 10.861 1.00121.91 C
ANISOU 4746 CA PHE B 369 22722 13415 10184 -1010 4385 -269 C
ATOM 4747 C PHE B 369 -2.799 -7.076 12.207 1.00133.09 C
ANISOU 4747 C PHE B 369 24531 14893 11143 -1097 4396 -175 C
ATOM 4748 O PHE B 369 -3.037 -8.283 12.320 1.00136.14 O
ANISOU 4748 O PHE B 369 24879 15334 11515 -1077 4393 15 O
ATOM 4749 CB PHE B 369 -1.571 -6.116 10.245 1.00109.38 C
ANISOU 4749 CB PHE B 369 21042 11942 8576 -1057 3921 -330 C
ATOM 4750 CG PHE B 369 -1.619 -5.440 8.907 1.00 98.42 C
ANISOU 4750 CG PHE B 369 19274 10514 7604 -988 3882 -411 C
ATOM 4751 CD1 PHE B 369 -2.723 -5.584 8.080 1.00 89.80 C
ANISOU 4751 CD1 PHE B 369 17874 9327 6921 -884 4140 -361 C
ATOM 4752 CD2 PHE B 369 -0.577 -4.624 8.497 1.00100.59 C
ANISOU 4752 CD2 PHE B 369 19509 10851 7858 -1039 3587 -531 C
ATOM 4753 CE1 PHE B 369 -2.775 -4.946 6.852 1.00 86.89 C
ANISOU 4753 CE1 PHE B 369 17172 8925 6917 -836 4093 -424 C
ATOM 4754 CE2 PHE B 369 -0.620 -3.978 7.275 1.00 96.91 C
ANISOU 4754 CE2 PHE B 369 18703 10360 7758 -987 3555 -595 C
ATOM 4755 CZ PHE B 369 -1.723 -4.140 6.449 1.00 91.60 C
ANISOU 4755 CZ PHE B 369 17736 9592 7475 -888 3806 -540 C
ATOM 4756 N LYS B 370 -2.395 -6.335 13.241 1.00146.32 N
ANISOU 4756 N LYS B 370 26602 16563 12431 -1204 4398 -297 N
ATOM 4757 CA LYS B 370 -2.236 -6.927 14.565 1.00156.46 C
ANISOU 4757 CA LYS B 370 28298 17909 13240 -1308 4400 -209 C
ATOM 4758 C LYS B 370 -3.565 -7.408 15.139 1.00156.05 C
ANISOU 4758 C LYS B 370 28318 17780 13195 -1257 4872 -112 C
ATOM 4759 O LYS B 370 -3.598 -8.403 15.871 1.00159.95 O
ANISOU 4759 O LYS B 370 28992 18353 13431 -1306 4862 60 O
ATOM 4760 CB LYS B 370 -1.568 -5.924 15.505 1.00165.34 C
ANISOU 4760 CB LYS B 370 29845 19025 13951 -1447 4314 -382 C
ATOM 4761 CG LYS B 370 -0.167 -5.518 15.062 1.00159.02 C
ANISOU 4761 CG LYS B 370 28994 18321 13107 -1519 3815 -450 C
ATOM 4762 CD LYS B 370 0.766 -6.718 14.986 1.00154.40 C
ANISOU 4762 CD LYS B 370 28353 17898 12413 -1553 3389 -249 C
ATOM 4763 CE LYS B 370 2.143 -6.324 14.473 1.00145.58 C
ANISOU 4763 CE LYS B 370 27141 16874 11300 -1611 2907 -303 C
ATOM 4764 NZ LYS B 370 3.145 -7.421 14.591 1.00139.20 N
ANISOU 4764 NZ LYS B 370 26346 16213 10331 -1659 2480 -101 N
ATOM 4765 N ALA B 371 -4.663 -6.715 14.824 1.00146.92 N
ANISOU 4765 N ALA B 371 27016 16468 12338 -1162 5285 -202 N
ATOM 4766 CA ALA B 371 -5.970 -7.101 15.345 1.00137.28 C
ANISOU 4766 CA ALA B 371 25836 15165 11160 -1106 5763 -106 C
ATOM 4767 C ALA B 371 -6.419 -8.461 14.825 1.00135.27 C
ANISOU 4767 C ALA B 371 25277 14973 11145 -1039 5743 138 C
ATOM 4768 O ALA B 371 -7.099 -9.203 15.543 1.00149.16 O
ANISOU 4768 O ALA B 371 27157 16745 12771 -1049 5989 289 O
ATOM 4769 CB ALA B 371 -7.004 -6.037 14.996 1.00131.58 C
ANISOU 4769 CB ALA B 371 24975 14251 10769 -1006 6185 -239 C
ATOM 4770 N ALA B 372 -6.054 -8.811 13.588 1.00124.88 N
ANISOU 4770 N ALA B 372 23577 13697 10175 -980 5459 183 N
ATOM 4771 CA ALA B 372 -6.450 -10.109 13.046 1.00124.72 C
ANISOU 4771 CA ALA B 372 23278 13724 10387 -926 5424 409 C
ATOM 4772 C ALA B 372 -5.773 -11.252 13.785 1.00136.43 C
ANISOU 4772 C ALA B 372 24990 15346 11499 -1017 5180 591 C
ATOM 4773 O ALA B 372 -6.330 -12.350 13.886 1.00146.26 O
ANISOU 4773 O ALA B 372 26152 16616 12803 -1003 5277 807 O
ATOM 4774 CB ALA B 372 -6.126 -10.180 11.556 1.00116.24 C
ANISOU 4774 CB ALA B 372 21784 12655 9727 -855 5165 396 C
ATOM 4775 N PHE B 373 -4.567 -11.015 14.294 1.00139.21 N
ANISOU 4775 N PHE B 373 25621 15790 11483 -1116 4846 524 N
ATOM 4776 CA PHE B 373 -3.816 -12.067 14.965 1.00145.15 C
ANISOU 4776 CA PHE B 373 26587 16673 11890 -1206 4560 716 C
ATOM 4777 C PHE B 373 -4.482 -12.500 16.268 1.00158.63 C
ANISOU 4777 C PHE B 373 28623 18391 13256 -1275 4852 841 C
ATOM 4778 O PHE B 373 -4.292 -13.641 16.706 1.00161.95 O
ANISOU 4778 O PHE B 373 29130 18902 13503 -1324 4719 1079 O
ATOM 4779 CB PHE B 373 -2.390 -11.572 15.195 1.00146.25 C
ANISOU 4779 CB PHE B 373 26934 16897 11736 -1302 4131 612 C
ATOM 4780 CG PHE B 373 -1.671 -11.247 13.917 1.00144.06 C
ANISOU 4780 CG PHE B 373 26325 16628 11781 -1239 3834 518 C
ATOM 4781 CD1 PHE B 373 -1.662 -12.151 12.864 1.00138.82 C
ANISOU 4781 CD1 PHE B 373 25307 15980 11459 -1149 3704 653 C
ATOM 4782 CD2 PHE B 373 -1.058 -10.013 13.744 1.00142.19 C
ANISOU 4782 CD2 PHE B 373 26133 16376 11515 -1273 3710 294 C
ATOM 4783 CE1 PHE B 373 -1.020 -11.854 11.670 1.00127.14 C
ANISOU 4783 CE1 PHE B 373 23535 14510 10262 -1093 3456 564 C
ATOM 4784 CE2 PHE B 373 -0.413 -9.703 12.553 1.00131.44 C
ANISOU 4784 CE2 PHE B 373 24456 15033 10450 -1219 3454 219 C
ATOM 4785 CZ PHE B 373 -0.394 -10.627 11.512 1.00121.84 C
ANISOU 4785 CZ PHE B 373 22898 13841 9554 -1127 3333 351 C
ATOM 4786 N SER B 374 -5.239 -11.601 16.911 1.00170.99 N
ANISOU 4786 N SER B 374 30389 19864 14715 -1282 5253 693 N
ATOM 4787 CA SER B 374 -5.936 -11.953 18.148 1.00185.44 C
ANISOU 4787 CA SER B 374 32541 21702 16214 -1346 5584 800 C
ATOM 4788 C SER B 374 -7.119 -12.879 17.885 1.00191.10 C
ANISOU 4788 C SER B 374 32984 22390 17235 -1263 5894 1016 C
ATOM 4789 O SER B 374 -7.377 -13.802 18.668 1.00205.26 O
ANISOU 4789 O SER B 374 34941 24255 18792 -1327 5974 1237 O
ATOM 4790 CB SER B 374 -6.399 -10.691 18.870 1.00192.55 C
ANISOU 4790 CB SER B 374 33742 22492 16927 -1369 5948 567 C
ATOM 4791 OG SER B 374 -6.960 -11.017 20.131 1.00202.73 O
ANISOU 4791 OG SER B 374 35393 23799 17835 -1445 6258 662 O
ATOM 4792 N TRP B 375 -7.845 -12.656 16.788 1.00177.59 N
ANISOU 4792 N TRP B 375 30850 20576 16048 -1133 6056 974 N
ATOM 4793 CA TRP B 375 -8.946 -13.548 16.439 1.00170.30 C
ANISOU 4793 CA TRP B 375 29627 19624 15455 -1066 6307 1191 C
ATOM 4794 C TRP B 375 -8.427 -14.939 16.121 1.00168.60 C
ANISOU 4794 C TRP B 375 29281 19517 15261 -1100 5955 1445 C
ATOM 4795 O TRP B 375 -9.163 -15.928 16.236 1.00176.47 O
ANISOU 4795 O TRP B 375 30160 20526 16366 -1103 6112 1688 O
ATOM 4796 CB TRP B 375 -9.719 -12.999 15.246 1.00158.33 C
ANISOU 4796 CB TRP B 375 27676 17978 14504 -932 6480 1098 C
ATOM 4797 CG TRP B 375 -10.700 -11.927 15.566 1.00162.88 C
ANISOU 4797 CG TRP B 375 28300 18410 15177 -872 6961 952 C
ATOM 4798 CD1 TRP B 375 -10.559 -10.596 15.329 1.00158.56 C
ANISOU 4798 CD1 TRP B 375 27788 17758 14699 -833 7018 698 C
ATOM 4799 CD2 TRP B 375 -12.010 -12.103 16.119 1.00171.33 C
ANISOU 4799 CD2 TRP B 375 29357 19410 16332 -836 7465 1070 C
ATOM 4800 NE1 TRP B 375 -11.687 -9.923 15.731 1.00162.37 N
ANISOU 4800 NE1 TRP B 375 28301 18095 15296 -769 7534 645 N
ATOM 4801 CE2 TRP B 375 -12.595 -10.827 16.217 1.00170.26 C
ANISOU 4801 CE2 TRP B 375 29265 19115 16311 -765 7822 869 C
ATOM 4802 CE3 TRP B 375 -12.738 -13.215 16.553 1.00174.89 C
ANISOU 4802 CE3 TRP B 375 29759 19912 16779 -861 7653 1339 C
ATOM 4803 CZ2 TRP B 375 -13.873 -10.630 16.731 1.00173.42 C
ANISOU 4803 CZ2 TRP B 375 29661 19403 16829 -705 8373 922 C
ATOM 4804 CZ3 TRP B 375 -14.007 -13.020 17.063 1.00176.92 C
ANISOU 4804 CZ3 TRP B 375 30003 20073 17144 -812 8191 1395 C
ATOM 4805 CH2 TRP B 375 -14.562 -11.736 17.147 1.00175.82 C
ANISOU 4805 CH2 TRP B 375 29907 19772 17125 -728 8553 1184 C
ATOM 4806 N TRP B 376 -7.162 -15.019 15.726 1.00158.43 N
ANISOU 4806 N TRP B 376 28012 18301 13884 -1128 5484 1402 N
ATOM 4807 CA TRP B 376 -6.493 -16.246 15.334 1.00156.00 C
ANISOU 4807 CA TRP B 376 27587 18072 13615 -1148 5110 1622 C
ATOM 4808 C TRP B 376 -5.814 -16.948 16.505 1.00163.46 C
ANISOU 4808 C TRP B 376 28911 19132 14064 -1272 4916 1805 C
ATOM 4809 O TRP B 376 -5.787 -18.183 16.552 1.00164.69 O
ANISOU 4809 O TRP B 376 29009 19328 14238 -1296 4790 2084 O
ATOM 4810 CB TRP B 376 -5.433 -15.912 14.287 1.00152.47 C
ANISOU 4810 CB TRP B 376 26960 17634 13335 -1105 4710 1481 C
ATOM 4811 CG TRP B 376 -4.699 -17.086 13.750 1.00159.76 C
ANISOU 4811 CG TRP B 376 27747 18609 14345 -1103 4333 1682 C
ATOM 4812 CD1 TRP B 376 -5.122 -17.963 12.793 1.00161.37 C
ANISOU 4812 CD1 TRP B 376 27609 18761 14942 -1038 4318 1826 C
ATOM 4813 CD2 TRP B 376 -3.429 -17.564 14.202 1.00166.28 C
ANISOU 4813 CD2 TRP B 376 28795 19532 14852 -1174 3918 1786 C
ATOM 4814 NE1 TRP B 376 -4.164 -18.930 12.586 1.00161.99 N
ANISOU 4814 NE1 TRP B 376 27691 18884 14976 -1053 3931 1996 N
ATOM 4815 CE2 TRP B 376 -3.120 -18.711 13.447 1.00165.98 C
ANISOU 4815 CE2 TRP B 376 28529 19483 15055 -1130 3680 1986 C
ATOM 4816 CE3 TRP B 376 -2.515 -17.122 15.163 1.00171.27 C
ANISOU 4816 CE3 TRP B 376 29796 20251 15027 -1274 3712 1734 C
ATOM 4817 CZ2 TRP B 376 -1.933 -19.422 13.623 1.00169.69 C
ANISOU 4817 CZ2 TRP B 376 29115 20016 15344 -1165 3255 2147 C
ATOM 4818 CZ3 TRP B 376 -1.341 -17.826 15.337 1.00175.15 C
ANISOU 4818 CZ3 TRP B 376 30391 20824 15335 -1322 3268 1900 C
ATOM 4819 CH2 TRP B 376 -1.059 -18.964 14.571 1.00174.72 C
ANISOU 4819 CH2 TRP B 376 30090 20748 15547 -1258 3050 2110 C
ATOM 4820 N LEU B 377 -5.257 -16.191 17.453 1.00167.48 N
ANISOU 4820 N LEU B 377 29814 19687 14135 -1361 4875 1667 N
ATOM 4821 CA LEU B 377 -4.492 -16.786 18.542 1.00167.45 C
ANISOU 4821 CA LEU B 377 30185 19800 13640 -1493 4628 1840 C
ATOM 4822 C LEU B 377 -5.357 -16.905 19.793 1.00174.99 C
ANISOU 4822 C LEU B 377 31452 20769 14268 -1572 5022 1936 C
ATOM 4823 O LEU B 377 -5.623 -18.023 20.254 1.00179.91 O
ANISOU 4823 O LEU B 377 32113 21447 14797 -1619 5038 2233 O
ATOM 4824 CB LEU B 377 -3.230 -15.961 18.811 1.00164.43 C
ANISOU 4824 CB LEU B 377 30052 19469 12953 -1570 4271 1654 C
ATOM 4825 CG LEU B 377 -2.257 -16.406 19.908 1.00164.83 C
ANISOU 4825 CG LEU B 377 30503 19641 12483 -1722 3933 1811 C
ATOM 4826 CD1 LEU B 377 -1.897 -17.877 19.760 1.00162.55 C
ANISOU 4826 CD1 LEU B 377 30085 19413 12263 -1718 3649 2162 C
ATOM 4827 CD2 LEU B 377 -1.003 -15.541 19.886 1.00163.17 C
ANISOU 4827 CD2 LEU B 377 30435 19469 12095 -1786 3542 1618 C
ATOM 4828 N PRO B 378 -5.816 -15.787 20.378 1.00178.25 N
ANISOU 4828 N PRO B 378 32101 21126 14499 -1592 5355 1702 N
ATOM 4829 CA PRO B 378 -6.745 -15.940 21.496 1.00182.98 C
ANISOU 4829 CA PRO B 378 32974 21729 14820 -1652 5788 1798 C
ATOM 4830 C PRO B 378 -8.182 -15.611 21.104 1.00179.79 C
ANISOU 4830 C PRO B 378 32306 21199 14808 -1532 6329 1740 C
ATOM 4831 O PRO B 378 -8.837 -14.857 21.820 1.00182.51 O
ANISOU 4831 O PRO B 378 32890 21480 14977 -1543 6743 1604 O
ATOM 4832 CB PRO B 378 -6.210 -14.938 22.514 1.00187.14 C
ANISOU 4832 CB PRO B 378 34002 22268 14833 -1769 5784 1582 C
ATOM 4833 CG PRO B 378 -5.704 -13.816 21.657 1.00182.18 C
ANISOU 4833 CG PRO B 378 33218 21559 14445 -1702 5630 1283 C
ATOM 4834 CD PRO B 378 -5.228 -14.434 20.352 1.00177.74 C
ANISOU 4834 CD PRO B 378 32192 21017 14324 -1607 5272 1379 C
TER 4835 PRO B 378
HETATM 4836 C1 NVN A 401 11.505 26.174 -26.793 1.00 65.12 C
HETATM 4837 C10 NVN A 401 9.485 24.724 -27.210 1.00 72.55 C
HETATM 4838 C11 NVN A 401 8.024 22.170 -27.079 1.00 56.66 C
HETATM 4839 C12 NVN A 401 7.361 19.819 -26.649 1.00 58.38 C
HETATM 4840 C13 NVN A 401 6.352 18.858 -26.725 1.00 73.43 C
HETATM 4841 C14 NVN A 401 6.560 17.589 -26.226 1.00 83.48 C
HETATM 4842 C15 NVN A 401 7.782 17.231 -25.631 1.00 79.21 C
HETATM 4843 C16 NVN A 401 8.786 18.213 -25.564 1.00 76.11 C
HETATM 4844 C17 NVN A 401 8.581 19.482 -26.062 1.00 63.63 C
HETATM 4845 C18 NVN A 401 9.234 15.620 -24.489 1.00 69.94 C
HETATM 4846 C19 NVN A 401 6.967 14.952 -25.239 1.00 79.67 C
HETATM 4847 C2 NVN A 401 10.124 25.973 -27.342 1.00 72.80 C
HETATM 4848 C3 NVN A 401 8.294 26.869 -28.458 1.00 74.53 C
HETATM 4849 C4 NVN A 401 7.697 27.978 -29.094 1.00 72.35 C
HETATM 4850 C5 NVN A 401 6.447 27.866 -29.615 1.00 57.01 C
HETATM 4851 C6 NVN A 401 5.764 26.682 -29.524 1.00 51.30 C
HETATM 4852 C7 NVN A 401 6.282 25.583 -28.926 1.00 48.03 C
HETATM 4853 C8 NVN A 401 7.579 25.650 -28.370 1.00 63.50 C
HETATM 4854 C9 NVN A 401 8.221 24.544 -27.713 1.00 68.21 C
HETATM 4855 F1 NVN A 401 4.514 26.613 -30.058 1.00 62.60 F
HETATM 4856 F2 NVN A 401 8.356 29.149 -29.192 1.00 86.54 F
HETATM 4857 N1 NVN A 401 9.556 27.007 -27.941 1.00 80.54 N
HETATM 4858 N2 NVN A 401 7.514 23.316 -27.619 1.00 63.66 N
HETATM 4859 N3 NVN A 401 7.154 21.114 -27.157 1.00 56.82 N
HETATM 4860 N4 NVN A 401 7.988 15.972 -25.135 1.00 71.34 N
HETATM 4861 O1 NVN A 401 9.140 22.098 -26.579 1.00 49.13 O
HETATM 4862 H3 NVN A 401 11.979 26.826 -27.334 1.00 79.75 H
HETATM 4863 H1 NVN A 401 11.988 25.332 -26.808 1.00 79.75 H
HETATM 4864 H2 NVN A 401 11.449 26.496 -25.878 1.00 79.75 H
HETATM 4865 H6 NVN A 401 9.923 24.010 -26.776 1.00 88.67 H
HETATM 4866 H9 NVN A 401 5.523 19.078 -27.120 1.00 89.73 H
HETATM 4867 H10 NVN A 401 5.869 16.948 -26.283 1.00101.79 H
HETATM 4868 H11 NVN A 401 9.616 17.997 -25.169 1.00 92.94 H
HETATM 4869 H12 NVN A 401 9.269 20.126 -26.007 1.00 77.96 H
HETATM 4870 H13 NVN A 401 9.928 16.245 -24.755 1.00 85.54 H
HETATM 4871 H14 NVN A 401 9.495 14.722 -24.749 1.00 85.54 H
HETATM 4872 H15 NVN A 401 9.123 15.655 -23.525 1.00 85.54 H
HETATM 4873 H16 NVN A 401 6.103 15.331 -25.013 1.00 97.21 H
HETATM 4874 H17 NVN A 401 7.169 14.225 -24.628 1.00 97.21 H
HETATM 4875 H18 NVN A 401 6.940 14.610 -26.148 1.00 97.21 H
HETATM 4876 H4 NVN A 401 6.049 28.608 -30.040 1.00 70.02 H
HETATM 4877 H5 NVN A 401 5.790 24.780 -28.877 1.00 59.24 H
HETATM 4878 H7 NVN A 401 6.707 23.290 -27.922 1.00 78.00 H
HETATM 4879 H8 NVN A 401 6.389 21.260 -27.565 1.00 69.79 H
HETATM 4880 C1 NVN A 402 11.646 25.690 -30.631 1.00 83.55 C
HETATM 4881 C10 NVN A 402 10.372 23.518 -30.514 1.00 89.77 C
HETATM 4882 C11 NVN A 402 8.354 20.386 -30.528 1.00 86.57 C
HETATM 4883 C12 NVN A 402 8.273 17.959 -29.775 1.00 78.52 C
HETATM 4884 C13 NVN A 402 7.014 17.531 -30.199 1.00 69.09 C
HETATM 4885 C14 NVN A 402 6.623 16.221 -30.002 1.00 71.34 C
HETATM 4886 C15 NVN A 402 7.471 15.278 -29.375 1.00 80.05 C
HETATM 4887 C16 NVN A 402 8.736 15.732 -28.964 1.00 81.60 C
HETATM 4888 C17 NVN A 402 9.127 17.039 -29.160 1.00 77.85 C
HETATM 4889 C18 NVN A 402 7.922 13.037 -28.459 1.00 80.63 C
HETATM 4890 C19 NVN A 402 5.836 13.478 -29.723 1.00 76.78 C
HETATM 4891 C2 NVN A 402 10.424 24.865 -30.900 1.00 87.41 C
HETATM 4892 C3 NVN A 402 8.275 24.757 -31.785 1.00 94.06 C
HETATM 4893 C4 NVN A 402 7.221 25.421 -32.440 1.00 98.25 C
HETATM 4894 C5 NVN A 402 6.081 24.752 -32.735 1.00 90.15 C
HETATM 4895 C6 NVN A 402 5.945 23.433 -32.391 1.00 75.40 C
HETATM 4896 C7 NVN A 402 6.920 22.735 -31.754 1.00 74.67 C
HETATM 4897 C8 NVN A 402 8.130 23.392 -31.429 1.00 83.67 C
HETATM 4898 C9 NVN A 402 9.245 22.777 -30.756 1.00 87.64 C
HETATM 4899 F1 NVN A 402 4.778 22.807 -32.704 1.00 77.18 F
HETATM 4900 F2 NVN A 402 7.336 26.712 -32.788 1.00 96.13 F
HETATM 4901 N1 NVN A 402 9.420 25.465 -31.512 1.00 89.64 N
HETATM 4902 N2 NVN A 402 9.246 21.415 -30.360 1.00 87.59 N
HETATM 4903 N3 NVN A 402 8.823 19.256 -29.906 1.00 88.84 N
HETATM 4904 N4 NVN A 402 7.083 13.975 -29.179 1.00 78.64 N
HETATM 4905 O1 NVN A 402 7.227 20.489 -31.002 1.00 84.14 O
HETATM 4906 H3 NVN A 402 12.267 25.609 -31.375 1.00101.87 H
HETATM 4907 H1 NVN A 402 12.079 25.382 -29.819 1.00101.87 H
HETATM 4908 H2 NVN A 402 11.396 26.623 -30.527 1.00101.87 H
HETATM 4909 H6 NVN A 402 11.110 23.118 -30.084 1.00109.33 H
HETATM 4910 H9 NVN A 402 6.428 18.139 -30.621 1.00 84.51 H
HETATM 4911 H10 NVN A 402 5.768 15.945 -30.290 1.00 87.22 H
HETATM 4912 H11 NVN A 402 9.328 15.126 -28.548 1.00 99.52 H
HETATM 4913 H12 NVN A 402 9.982 17.317 -28.873 1.00 95.03 H
HETATM 4914 H13 NVN A 402 8.038 13.339 -27.544 1.00 98.37 H
HETATM 4915 H14 NVN A 402 8.790 12.978 -28.888 1.00 98.37 H
HETATM 4916 H15 NVN A 402 7.504 12.159 -28.457 1.00 98.37 H
HETATM 4917 H16 NVN A 402 5.406 14.174 -30.244 1.00 93.74 H
HETATM 4918 H17 NVN A 402 5.249 13.209 -29.000 1.00 93.74 H
HETATM 4919 H18 NVN A 402 6.014 12.713 -30.296 1.00 93.74 H
HETATM 4920 H4 NVN A 402 5.376 25.198 -33.179 1.00109.78 H
HETATM 4921 H5 NVN A 402 6.801 21.829 -31.528 1.00 91.21 H
HETATM 4922 H7 NVN A 402 9.953 21.181 -29.926 1.00106.71 H
HETATM 4923 H8 NVN A 402 9.606 19.355 -29.519 1.00108.22 H
HETATM 4924 C1 SOG A 403 19.572 34.331 -47.621 1.00 85.54 C
HETATM 4925 C2 SOG A 403 20.871 33.671 -48.053 1.00 82.38 C
HETATM 4926 C3 SOG A 403 22.042 34.465 -47.484 1.00 83.64 C
HETATM 4927 C4 SOG A 403 21.931 35.929 -47.876 1.00 87.98 C
HETATM 4928 C5 SOG A 403 20.534 36.498 -47.603 1.00 81.80 C
HETATM 4929 C6 SOG A 403 20.344 37.865 -48.236 1.00 82.77 C
HETATM 4930 C1' SOG A 403 18.196 31.968 -47.083 1.00 72.57 C
HETATM 4931 C2' SOG A 403 16.925 31.864 -46.280 1.00 55.63 C
HETATM 4932 C3' SOG A 403 16.612 33.129 -45.537 1.00 45.39 C
HETATM 4933 C4' SOG A 403 15.286 33.080 -44.815 1.00 48.52 C
HETATM 4934 C5' SOG A 403 14.969 34.353 -44.071 1.00 57.37 C
HETATM 4935 C6' SOG A 403 13.680 34.337 -43.305 1.00 61.69 C
HETATM 4936 C7' SOG A 403 12.415 34.370 -44.111 1.00 62.56 C
HETATM 4937 C8' SOG A 403 11.228 34.434 -43.186 1.00 60.63 C
HETATM 4938 S1 SOG A 403 18.130 33.410 -48.197 1.00 80.47 S
HETATM 4939 O2 SOG A 403 20.939 32.326 -47.594 1.00 85.86 O
HETATM 4940 O3 SOG A 403 23.275 33.918 -47.948 1.00 86.98 O
HETATM 4941 O4 SOG A 403 22.884 36.719 -47.170 1.00 98.55 O
HETATM 4942 O5 SOG A 403 19.520 35.643 -48.157 1.00 81.02 O
HETATM 4943 O6 SOG A 403 21.448 38.716 -47.936 1.00 78.97 O
HETATM 4944 C1 SOG A 404 -12.080 7.644 -14.486 1.00138.89 C
HETATM 4945 C2 SOG A 404 -13.430 7.243 -15.073 1.00135.96 C
HETATM 4946 C3 SOG A 404 -13.296 5.924 -15.827 1.00133.58 C
HETATM 4947 C4 SOG A 404 -12.180 5.999 -16.845 1.00129.17 C
HETATM 4948 C5 SOG A 404 -10.891 6.453 -16.168 1.00132.79 C
HETATM 4949 C6 SOG A 404 -9.751 6.638 -17.153 1.00128.16 C
HETATM 4950 C1' SOG A 404 -10.585 9.212 -12.749 1.00125.90 C
HETATM 4951 C2' SOG A 404 -10.247 10.324 -11.779 1.00114.99 C
HETATM 4952 C3' SOG A 404 -9.881 11.616 -12.473 1.00103.83 C
HETATM 4953 C4' SOG A 404 -9.361 12.699 -11.545 1.00 95.47 C
HETATM 4954 C5' SOG A 404 -8.062 12.374 -10.828 1.00 88.30 C
HETATM 4955 C6' SOG A 404 -7.198 13.589 -10.561 1.00 77.25 C
HETATM 4956 C7' SOG A 404 -6.421 13.580 -9.270 1.00 75.88 C
HETATM 4957 C8' SOG A 404 -7.311 13.754 -8.063 1.00 78.87 C
HETATM 4958 S1 SOG A 404 -12.183 9.237 -13.629 1.00138.34 S
HETATM 4959 O2 SOG A 404 -14.385 7.085 -14.030 1.00134.17 O
HETATM 4960 O3 SOG A 404 -14.528 5.581 -16.460 1.00138.28 O
HETATM 4961 O4 SOG A 404 -11.973 4.725 -17.451 1.00124.21 O
HETATM 4962 O5 SOG A 404 -11.100 7.716 -15.513 1.00137.54 O
HETATM 4963 O6 SOG A 404 -9.458 5.409 -17.816 1.00120.94 O
HETATM 4964 C1 SOG A 405 20.215 7.112 -22.611 1.00126.69 C
HETATM 4965 C2 SOG A 405 18.936 6.615 -23.250 1.00111.49 C
HETATM 4966 C3 SOG A 405 17.863 6.467 -22.178 1.00 96.65 C
HETATM 4967 C4 SOG A 405 18.354 5.606 -21.026 1.00125.22 C
HETATM 4968 C5 SOG A 405 19.745 6.030 -20.546 1.00137.86 C
HETATM 4969 C6 SOG A 405 20.345 5.015 -19.590 1.00132.45 C
HETATM 4970 C1' SOG A 405 22.864 7.925 -22.866 1.00107.73 C
HETATM 4971 C2' SOG A 405 24.103 8.116 -23.707 1.00 98.58 C
HETATM 4972 C3' SOG A 405 25.297 8.602 -22.914 1.00 96.35 C
HETATM 4973 C4' SOG A 405 26.529 8.760 -23.774 1.00 92.37 C
HETATM 4974 C5' SOG A 405 27.760 9.268 -23.060 1.00 91.90 C
HETATM 4975 C6' SOG A 405 27.622 10.649 -22.476 1.00 90.16 C
HETATM 4976 C7' SOG A 405 26.849 10.688 -21.195 1.00 90.22 C
HETATM 4977 C8' SOG A 405 27.573 10.007 -20.062 1.00 93.17 C
HETATM 4978 S1 SOG A 405 21.488 7.284 -23.876 1.00117.29 S
HETATM 4979 O2 SOG A 405 18.493 7.531 -24.245 1.00114.89 O
HETATM 4980 O3 SOG A 405 16.684 5.903 -22.749 1.00 59.87 O
HETATM 4981 O4 SOG A 405 17.450 5.683 -19.921 1.00135.74 O
HETATM 4982 O5 SOG A 405 20.655 6.164 -21.652 1.00142.51 O
HETATM 4983 O6 SOG A 405 19.416 4.702 -18.551 1.00125.86 O
HETATM 4984 C1 SOG A 406 16.660 21.429 -12.851 1.00134.35 C
HETATM 4985 C2 SOG A 406 17.419 22.075 -14.008 1.00122.40 C
HETATM 4986 C3 SOG A 406 17.821 21.019 -15.033 1.00101.55 C
HETATM 4987 C4 SOG A 406 18.533 19.859 -14.373 1.00104.17 C
HETATM 4988 C5 SOG A 406 17.651 19.297 -13.273 1.00119.34 C
HETATM 4989 C6 SOG A 406 18.305 18.157 -12.515 1.00118.10 C
HETATM 4990 C1' SOG A 406 15.182 23.709 -12.181 1.00118.80 C
HETATM 4991 C2' SOG A 406 14.995 24.785 -11.144 1.00107.83 C
HETATM 4992 C3' SOG A 406 15.209 24.242 -9.751 1.00107.18 C
HETATM 4993 C4' SOG A 406 15.259 25.296 -8.676 1.00110.53 C
HETATM 4994 C5' SOG A 406 15.637 24.746 -7.322 1.00116.63 C
HETATM 4995 C6' SOG A 406 15.567 25.739 -6.189 1.00122.13 C
HETATM 4996 C7' SOG A 406 15.895 25.136 -4.848 1.00119.38 C
HETATM 4997 C8' SOG A 406 15.718 26.094 -3.697 1.00113.74 C
HETATM 4998 S1 SOG A 406 16.456 22.604 -11.501 1.00135.70 S
HETATM 4999 O2 SOG A 406 16.613 23.061 -14.643 1.00127.07 O
HETATM 5000 O3 SOG A 406 18.642 21.597 -16.045 1.00 89.39 O
HETATM 5001 O4 SOG A 406 18.794 18.835 -15.328 1.00101.10 O
HETATM 5002 O5 SOG A 406 17.377 20.328 -12.313 1.00134.81 O
HETATM 5003 O6 SOG A 406 17.441 17.023 -12.482 1.00118.12 O
HETATM 5004 C1 SOG A 407 25.912 9.397 -29.615 1.00124.80 C
HETATM 5005 C2 SOG A 407 25.060 9.767 -28.407 1.00120.51 C
HETATM 5006 C3 SOG A 407 24.568 8.504 -27.705 1.00123.71 C
HETATM 5007 C4 SOG A 407 23.915 7.549 -28.687 1.00124.10 C
HETATM 5008 C5 SOG A 407 24.852 7.291 -29.856 1.00129.87 C
HETATM 5009 C6 SOG A 407 24.236 6.416 -30.931 1.00132.15 C
HETATM 5010 C1' SOG A 407 26.583 10.021 -32.202 1.00118.23 C
HETATM 5011 C2' SOG A 407 25.343 10.037 -33.064 1.00112.65 C
HETATM 5012 C3' SOG A 407 25.418 9.031 -34.188 1.00113.53 C
HETATM 5013 C4' SOG A 407 24.354 9.210 -35.245 1.00113.20 C
HETATM 5014 C5' SOG A 407 24.657 10.286 -36.260 1.00112.37 C
HETATM 5015 C6' SOG A 407 24.515 9.819 -37.689 1.00110.00 C
HETATM 5016 C7' SOG A 407 25.343 8.596 -38.003 1.00109.74 C
HETATM 5017 C8' SOG A 407 25.173 8.042 -39.401 1.00110.19 C
HETATM 5018 S1 SOG A 407 26.392 10.836 -30.587 1.00130.78 S
HETATM 5019 O2 SOG A 407 25.813 10.565 -27.500 1.00116.03 O
HETATM 5020 O3 SOG A 407 23.653 8.844 -26.666 1.00124.52 O
HETATM 5021 O4 SOG A 407 23.608 6.306 -28.059 1.00123.23 O
HETATM 5022 O5 SOG A 407 25.196 8.535 -30.483 1.00128.45 O
HETATM 5023 O6 SOG A 407 25.124 6.308 -32.040 1.00130.56 O
HETATM 5024 S SO4 A 408 -21.412 8.340 -40.412 1.00151.31 S
HETATM 5025 O1 SO4 A 408 -20.159 7.683 -40.770 1.00146.53 O
HETATM 5026 O2 SO4 A 408 -22.131 8.728 -41.621 1.00148.88 O
HETATM 5027 O3 SO4 A 408 -22.226 7.408 -39.636 1.00159.69 O
HETATM 5028 O4 SO4 A 408 -21.125 9.539 -39.631 1.00149.88 O
HETATM 5029 S SO4 A 409 -20.531 0.608 -30.106 1.00139.02 S
HETATM 5030 O1 SO4 A 409 -19.313 0.446 -30.891 1.00131.36 O
HETATM 5031 O2 SO4 A 409 -21.722 0.240 -30.866 1.00140.93 O
HETATM 5032 O3 SO4 A 409 -20.479 -0.263 -28.936 1.00139.92 O
HETATM 5033 O4 SO4 A 409 -20.609 2.009 -29.702 1.00143.30 O
HETATM 5034 CAD PGW A 410 -5.222 -14.252 -29.755 1.00143.29 C
HETATM 5035 OAE PGW A 410 -4.807 -15.240 -28.816 1.00141.73 O
HETATM 5036 OAF PGW A 410 -3.089 -13.131 -29.775 1.00140.11 O
HETATM 5037 P PGW A 410 -3.580 -11.843 -33.965 1.00157.94 P
HETATM 5038 C01 PGW A 410 -1.557 -9.041 -30.840 1.00115.92 C
HETATM 5039 C1 PGW A 410 0.753 -9.186 -33.716 1.00125.59 C
HETATM 5040 O01 PGW A 410 0.280 -9.193 -32.459 1.00121.43 O
HETATM 5041 C02 PGW A 410 -1.163 -9.184 -32.295 1.00124.74 C
HETATM 5042 C2 PGW A 410 1.371 -10.483 -34.172 1.00124.33 C
HETATM 5043 O02 PGW A 410 0.646 -8.210 -34.411 1.00124.45 O
HETATM 5044 C03 PGW A 410 -1.597 -10.492 -32.915 1.00139.50 C
HETATM 5045 C3 PGW A 410 2.349 -11.073 -33.202 1.00114.74 C
HETATM 5046 O03 PGW A 410 -1.306 -7.695 -30.371 1.00105.83 O
HETATM 5047 C04 PGW A 410 -4.476 -12.814 -31.693 1.00150.56 C
HETATM 5048 C4 PGW A 410 3.462 -10.117 -32.806 1.00105.52 C
HETATM 5049 O04 PGW A 410 -3.291 -7.045 -31.157 1.00 98.52 O
HETATM 5050 C05 PGW A 410 -4.063 -13.770 -30.599 1.00144.99 C
HETATM 5051 C5 PGW A 410 3.122 -9.217 -31.640 1.00 97.39 C
HETATM 5052 C06 PGW A 410 7.152 -4.006 -32.532 1.00 73.89 C
HETATM 5053 C6 PGW A 410 4.246 -8.303 -31.196 1.00 79.11 C
HETATM 5054 C07 PGW A 410 7.073 -2.568 -32.108 1.00 85.71 C
HETATM 5055 C7 PGW A 410 4.698 -7.297 -32.246 1.00 63.28 C
HETATM 5056 C08 PGW A 410 5.898 -2.250 -31.198 1.00 75.44 C
HETATM 5057 C8 PGW A 410 5.088 -5.958 -31.692 1.00 70.68 C
HETATM 5058 C09 PGW A 410 5.820 -0.812 -30.751 1.00 52.70 C
HETATM 5059 C9 PGW A 410 6.452 -5.890 -31.081 1.00 78.36 C
HETATM 5060 C10 PGW A 410 7.330 -4.974 -31.402 1.00 73.21 C
HETATM 5061 C11 PGW A 410 5.058 -0.636 -29.465 1.00 43.03 C
HETATM 5062 O11 PGW A 410 -3.012 -10.530 -33.236 1.00149.37 O
HETATM 5063 C12 PGW A 410 5.676 -1.377 -28.310 1.00 50.11 C
HETATM 5064 O12 PGW A 410 -3.527 -12.927 -32.784 1.00155.33 O
HETATM 5065 C13 PGW A 410 4.804 -1.435 -27.093 1.00 67.30 C
HETATM 5066 O13 PGW A 410 -5.025 -11.653 -34.335 1.00155.89 O
HETATM 5067 C14 PGW A 410 4.529 -0.082 -26.489 1.00 80.05 C
HETATM 5068 O14 PGW A 410 -2.579 -12.269 -35.004 1.00163.63 O
HETATM 5069 C15 PGW A 410 -3.402 2.622 -25.776 1.00 79.51 C
HETATM 5070 C16 PGW A 410 -2.101 2.332 -25.074 1.00 90.27 C
HETATM 5071 C17 PGW A 410 -1.716 3.396 -24.078 1.00 88.48 C
HETATM 5072 C18 PGW A 410 -0.439 3.122 -23.320 1.00 82.51 C
HETATM 5073 C19 PGW A 410 -2.294 -6.813 -30.525 1.00 93.28 C
HETATM 5074 C20 PGW A 410 -2.016 -5.512 -29.805 1.00 73.06 C
HETATM 5075 C21 PGW A 410 -3.043 -5.140 -28.762 1.00 58.61 C
HETATM 5076 C22 PGW A 410 -3.604 -3.734 -28.963 1.00 49.52 C
HETATM 5077 C23 PGW A 410 -3.902 -2.958 -27.686 1.00 41.30 C
HETATM 5078 C24 PGW A 410 -4.392 -1.538 -27.921 1.00 51.71 C
HETATM 5079 C25 PGW A 410 -4.188 -0.582 -26.763 1.00 57.47 C
HETATM 5080 C26 PGW A 410 -4.680 0.823 -27.026 1.00 55.00 C
HETATM 5081 C27 PGW A 410 -3.599 1.873 -27.070 1.00 60.88 C
HETATM 5082 C28 PGW A 410 0.065 4.311 -22.545 1.00 76.65 C
HETATM 5083 C29 PGW A 410 1.746 6.189 -22.557 1.00 77.12 C
HETATM 5084 C30 PGW A 410 1.423 4.776 -22.985 1.00 75.43 C
HETATM 5085 CAD PGW A 411 10.589 22.132 -5.560 1.00164.57 C
HETATM 5086 OAE PGW A 411 9.619 22.455 -4.568 1.00160.74 O
HETATM 5087 OAF PGW A 411 10.216 24.117 -6.891 1.00169.91 O
HETATM 5088 P PGW A 411 11.267 22.825 -9.432 1.00165.93 P
HETATM 5089 C01 PGW A 411 12.649 19.616 -11.605 1.00115.81 C
HETATM 5090 C1 PGW A 411 9.199 18.482 -11.524 1.00101.81 C
HETATM 5091 O01 PGW A 411 10.531 18.489 -11.338 1.00113.45 O
HETATM 5092 C02 PGW A 411 11.198 19.777 -11.217 1.00119.05 C
HETATM 5093 C2 PGW A 411 8.575 17.132 -11.252 1.00 84.57 C
HETATM 5094 O02 PGW A 411 8.621 19.467 -11.904 1.00102.80 O
HETATM 5095 C03 PGW A 411 11.021 20.204 -9.776 1.00135.90 C
HETATM 5096 C3 PGW A 411 7.091 17.044 -11.492 1.00 62.45 C
HETATM 5097 O03 PGW A 411 12.750 18.809 -12.799 1.00115.36 O
HETATM 5098 C04 PGW A 411 12.397 23.099 -7.048 1.00170.65 C
HETATM 5099 C4 PGW A 411 6.626 15.594 -11.558 1.00 57.31 C
HETATM 5100 O04 PGW A 411 14.360 20.122 -13.590 1.00102.09 O
HETATM 5101 C05 PGW A 411 11.199 23.378 -6.167 1.00169.09 C
HETATM 5102 C5 PGW A 411 5.134 15.389 -11.679 1.00 52.31 C
HETATM 5103 C06 PGW A 411 2.392 9.954 -14.108 1.00 74.58 C
HETATM 5104 C6 PGW A 411 4.737 13.997 -12.119 1.00 60.66 C
HETATM 5105 C07 PGW A 411 2.608 8.765 -14.979 1.00 77.80 C
HETATM 5106 C7 PGW A 411 3.485 13.452 -11.438 1.00 64.80 C
HETATM 5107 C08 PGW A 411 1.688 8.717 -16.183 1.00 74.78 C
HETATM 5108 C8 PGW A 411 2.793 12.349 -12.190 1.00 75.45 C
HETATM 5109 C09 PGW A 411 1.914 7.523 -17.081 1.00 72.56 C
HETATM 5110 C9 PGW A 411 3.565 11.066 -12.209 1.00 71.89 C
HETATM 5111 C10 PGW A 411 3.425 10.063 -13.033 1.00 67.81 C
HETATM 5112 C11 PGW A 411 3.283 7.468 -17.730 1.00 67.05 C
HETATM 5113 O11 PGW A 411 11.866 21.333 -9.399 1.00151.41 O
HETATM 5114 C12 PGW A 411 3.545 6.207 -18.521 1.00 56.43 C
HETATM 5115 O12 PGW A 411 12.216 23.613 -8.401 1.00170.90 O
HETATM 5116 C13 PGW A 411 2.600 5.900 -19.653 1.00 60.62 C
HETATM 5117 O13 PGW A 411 11.461 23.413 -10.803 1.00164.84 O
HETATM 5118 C14 PGW A 411 2.108 4.475 -19.642 1.00 61.48 C
HETATM 5119 O14 PGW A 411 9.884 22.767 -8.845 1.00168.40 O
HETATM 5120 C15 PGW A 411 14.253 11.834 -15.980 1.00 82.95 C
HETATM 5121 C16 PGW A 411 13.514 10.525 -15.820 1.00 69.65 C
HETATM 5122 C17 PGW A 411 12.767 10.074 -17.049 1.00 50.11 C
HETATM 5123 C18 PGW A 411 11.443 10.771 -17.267 1.00 37.86 C
HETATM 5124 C19 PGW A 411 13.815 19.051 -13.556 1.00106.25 C
HETATM 5125 C20 PGW A 411 14.284 17.828 -14.299 1.00 98.26 C
HETATM 5126 C21 PGW A 411 13.311 17.347 -15.326 1.00 93.84 C
HETATM 5127 C22 PGW A 411 13.943 16.435 -16.367 1.00 89.69 C
HETATM 5128 C23 PGW A 411 14.381 15.075 -15.869 1.00 89.57 C
HETATM 5129 C24 PGW A 411 15.730 15.048 -15.193 1.00 91.07 C
HETATM 5130 C25 PGW A 411 16.359 13.674 -15.147 1.00 90.99 C
HETATM 5131 C26 PGW A 411 16.436 12.984 -16.492 1.00 93.44 C
HETATM 5132 C27 PGW A 411 15.643 11.705 -16.559 1.00 92.94 C
HETATM 5133 C28 PGW A 411 10.812 10.463 -18.604 1.00 55.36 C
HETATM 5134 C29 PGW A 411 8.722 10.105 -19.979 1.00 88.95 C
HETATM 5135 C30 PGW A 411 9.307 10.496 -18.639 1.00 76.33 C
HETATM 5136 C1 NVN B 401 10.165 -16.556 -20.085 1.00 96.96 C
HETATM 5137 C10 NVN B 401 8.753 -14.898 -18.810 1.00113.21 C
HETATM 5138 C11 NVN B 401 7.607 -12.192 -18.247 1.00107.45 C
HETATM 5139 C12 NVN B 401 6.895 -9.819 -18.298 1.00 95.01 C
HETATM 5140 C13 NVN B 401 6.134 -8.823 -17.689 1.00103.25 C
HETATM 5141 C14 NVN B 401 6.108 -7.545 -18.208 1.00107.01 C
HETATM 5142 C15 NVN B 401 6.847 -7.199 -19.355 1.00 92.59 C
HETATM 5143 C16 NVN B 401 7.597 -8.227 -19.960 1.00 90.54 C
HETATM 5144 C17 NVN B 401 7.623 -9.504 -19.444 1.00 88.33 C
HETATM 5145 C18 NVN B 401 7.601 -5.584 -21.044 1.00 63.10 C
HETATM 5146 C19 NVN B 401 6.018 -4.872 -19.269 1.00 61.17 C
HETATM 5147 C2 NVN B 401 9.227 -16.215 -18.967 1.00102.02 C
HETATM 5148 C3 NVN B 401 8.016 -16.950 -17.127 1.00106.01 C
HETATM 5149 C4 NVN B 401 7.641 -18.008 -16.277 1.00103.56 C
HETATM 5150 C5 NVN B 401 6.791 -17.776 -15.242 1.00101.02 C
HETATM 5151 C6 NVN B 401 6.296 -16.518 -15.019 1.00101.72 C
HETATM 5152 C7 NVN B 401 6.616 -15.464 -15.805 1.00109.75 C
HETATM 5153 C8 NVN B 401 7.493 -15.658 -16.895 1.00112.90 C
HETATM 5154 C9 NVN B 401 7.900 -14.605 -17.781 1.00113.56 C
HETATM 5155 F1 NVN B 401 5.449 -16.323 -13.970 1.00100.80 F
HETATM 5156 F2 NVN B 401 8.116 -19.251 -16.482 1.00105.33 F
HETATM 5157 N1 NVN B 401 8.870 -17.206 -18.167 1.00 99.53 N
HETATM 5158 N2 NVN B 401 7.366 -13.325 -17.525 1.00109.44 N
HETATM 5159 N3 NVN B 401 6.917 -11.117 -17.755 1.00102.51 N
HETATM 5160 N4 NVN B 401 6.813 -5.924 -19.877 1.00 61.79 N
HETATM 5161 O1 NVN B 401 8.367 -12.123 -19.207 1.00107.70 O
HETATM 5162 H3 NVN B 401 10.736 -17.294 -19.819 1.00117.96 H
HETATM 5163 H1 NVN B 401 10.715 -15.784 -20.296 1.00117.96 H
HETATM 5164 H2 NVN B 401 9.656 -16.811 -20.872 1.00117.96 H
HETATM 5165 H6 NVN B 401 9.019 -14.222 -19.411 1.00137.46 H
HETATM 5166 H9 NVN B 401 5.633 -9.025 -16.915 1.00125.50 H
HETATM 5167 H10 NVN B 401 5.584 -6.886 -17.784 1.00130.02 H
HETATM 5168 H11 NVN B 401 8.095 -8.032 -20.739 1.00110.26 H
HETATM 5169 H12 NVN B 401 8.139 -10.171 -19.869 1.00107.61 H
HETATM 5170 H13 NVN B 401 8.017 -6.386 -21.402 1.00 77.33 H
HETATM 5171 H14 NVN B 401 8.292 -4.948 -20.796 1.00 77.33 H
HETATM 5172 H15 NVN B 401 7.028 -5.189 -21.721 1.00 77.33 H
HETATM 5173 H16 NVN B 401 5.355 -5.265 -18.678 1.00 75.01 H
HETATM 5174 H17 NVN B 401 5.568 -4.362 -19.962 1.00 75.01 H
HETATM 5175 H18 NVN B 401 6.594 -4.282 -18.758 1.00 75.01 H
HETATM 5176 H4 NVN B 401 6.539 -18.487 -14.676 1.00122.84 H
HETATM 5177 H5 NVN B 401 6.262 -14.607 -15.633 1.00133.31 H
HETATM 5178 H7 NVN B 401 6.837 -13.248 -16.850 1.00132.94 H
HETATM 5179 H8 NVN B 401 6.439 -11.249 -17.028 1.00124.62 H
HETATM 5180 C1 SOG B 402 -3.763 -27.099 -17.338 1.00106.63 C
HETATM 5181 C2 SOG B 402 -2.916 -28.353 -17.105 1.00 97.29 C
HETATM 5182 C3 SOG B 402 -2.141 -28.719 -18.367 1.00 87.32 C
HETATM 5183 C4 SOG B 402 -3.066 -28.798 -19.548 1.00 85.72 C
HETATM 5184 C5 SOG B 402 -3.779 -27.475 -19.696 1.00 99.00 C
HETATM 5185 C6 SOG B 402 -4.727 -27.475 -20.881 1.00 97.59 C
HETATM 5186 C1' SOG B 402 -5.551 -25.236 -16.226 1.00108.87 C
HETATM 5187 C2' SOG B 402 -6.484 -24.822 -15.110 1.00 99.97 C
HETATM 5188 C3' SOG B 402 -7.167 -23.503 -15.380 1.00 93.99 C
HETATM 5189 C4' SOG B 402 -6.725 -22.392 -14.455 1.00 95.51 C
HETATM 5190 C5' SOG B 402 -7.468 -22.329 -13.136 1.00 99.95 C
HETATM 5191 C6' SOG B 402 -7.052 -21.174 -12.248 1.00 97.95 C
HETATM 5192 C7' SOG B 402 -7.862 -21.005 -10.986 1.00 93.77 C
HETATM 5193 C8' SOG B 402 -7.383 -19.877 -10.099 1.00 89.81 C
HETATM 5194 S1 SOG B 402 -4.808 -26.865 -15.878 1.00112.73 S
HETATM 5195 O2 SOG B 402 -1.991 -28.127 -16.047 1.00 97.29 O
HETATM 5196 O3 SOG B 402 -1.462 -29.961 -18.205 1.00 84.18 O
HETATM 5197 O4 SOG B 402 -2.318 -29.059 -20.730 1.00 64.17 O
HETATM 5198 O5 SOG B 402 -4.557 -27.224 -18.512 1.00106.56 O
HETATM 5199 O6 SOG B 402 -4.939 -26.151 -21.354 1.00 92.90 O
HETATM 5200 C1 SOG B 403 -0.828 -27.638 -24.842 1.00148.57 C
HETATM 5201 C2 SOG B 403 -1.919 -28.709 -24.830 1.00149.90 C
HETATM 5202 C3 SOG B 403 -1.320 -30.030 -24.355 1.00156.10 C
HETATM 5203 C4 SOG B 403 -0.076 -30.395 -25.141 1.00149.52 C
HETATM 5204 C5 SOG B 403 0.894 -29.220 -25.164 1.00145.51 C
HETATM 5205 C6 SOG B 403 2.115 -29.485 -26.024 1.00144.85 C
HETATM 5206 C1' SOG B 403 -2.575 -26.506 -26.700 1.00129.39 C
HETATM 5207 C2' SOG B 403 -3.454 -25.361 -27.138 1.00113.52 C
HETATM 5208 C3' SOG B 403 -2.659 -24.116 -27.445 1.00111.07 C
HETATM 5209 C4' SOG B 403 -3.493 -22.972 -27.973 1.00112.75 C
HETATM 5210 C5' SOG B 403 -2.708 -21.702 -28.210 1.00111.95 C
HETATM 5211 C6' SOG B 403 -3.500 -20.586 -28.846 1.00113.75 C
HETATM 5212 C7' SOG B 403 -4.737 -20.173 -28.090 1.00112.74 C
HETATM 5213 C8' SOG B 403 -5.514 -19.058 -28.749 1.00110.18 C
HETATM 5214 S1 SOG B 403 -1.466 -26.022 -25.340 1.00145.81 S
HETATM 5215 O2 SOG B 403 -2.980 -28.354 -23.950 1.00143.71 O
HETATM 5216 O3 SOG B 403 -2.285 -31.080 -24.412 1.00163.07 O
HETATM 5217 O4 SOG B 403 0.563 -31.522 -24.540 1.00148.67 O
HETATM 5218 O5 SOG B 403 0.238 -28.051 -25.685 1.00147.21 O
HETATM 5219 O6 SOG B 403 2.852 -30.604 -25.539 1.00144.05 O
HETATM 5220 C1' SOG B 404 -7.416 -10.876 -23.720 1.00 75.04 C
HETATM 5221 C2' SOG B 404 -6.604 -11.088 -24.978 1.00 74.79 C
HETATM 5222 C3' SOG B 404 -6.165 -12.516 -25.165 1.00 75.16 C
HETATM 5223 C4' SOG B 404 -5.097 -12.933 -24.191 1.00 70.88 C
HETATM 5224 C5' SOG B 404 -4.813 -14.408 -24.208 1.00 77.40 C
HETATM 5225 C6' SOG B 404 -4.331 -14.922 -25.534 1.00 86.88 C
HETATM 5226 C7' SOG B 404 -4.052 -16.396 -25.514 1.00 94.91 C
HETATM 5227 C8' SOG B 404 -3.641 -16.910 -26.870 1.00100.22 C
HETATM 5228 S1 SOG B 404 -8.014 -9.149 -23.661 1.00 78.50 S
HETATM 5229 C1 SOG B 405 5.727 -12.508 -34.317 1.00133.90 C
HETATM 5230 C2 SOG B 405 7.221 -12.446 -34.606 1.00125.30 C
HETATM 5231 C3 SOG B 405 7.684 -10.996 -34.678 1.00121.42 C
HETATM 5232 C4 SOG B 405 6.838 -10.223 -35.666 1.00122.43 C
HETATM 5233 C5 SOG B 405 5.360 -10.394 -35.330 1.00127.08 C
HETATM 5234 C6 SOG B 405 4.459 -9.713 -36.343 1.00127.62 C
HETATM 5235 C1' SOG B 405 3.710 -14.246 -33.441 1.00140.06 C
HETATM 5236 C2' SOG B 405 3.221 -15.670 -33.335 1.00131.66 C
HETATM 5237 C3' SOG B 405 1.773 -15.765 -32.933 1.00128.90 C
HETATM 5238 C4' SOG B 405 1.178 -17.123 -33.220 1.00128.39 C
HETATM 5239 C5' SOG B 405 -0.328 -17.186 -33.115 1.00120.91 C
HETATM 5240 C6' SOG B 405 -0.867 -17.027 -31.716 1.00116.49 C
HETATM 5241 C7' SOG B 405 -2.371 -17.056 -31.632 1.00116.15 C
HETATM 5242 C8' SOG B 405 -2.905 -16.989 -30.220 1.00113.19 C
HETATM 5243 S1 SOG B 405 5.267 -14.249 -34.384 1.00144.18 S
HETATM 5244 O2 SOG B 405 7.953 -13.127 -33.594 1.00119.90 O
HETATM 5245 O3 SOG B 405 9.063 -10.938 -35.038 1.00121.04 O
HETATM 5246 O4 SOG B 405 7.163 -8.834 -35.640 1.00117.67 O
HETATM 5247 O5 SOG B 405 5.011 -11.788 -35.310 1.00131.09 O
HETATM 5248 O6 SOG B 405 4.744 -8.314 -36.399 1.00123.28 O
HETATM 5249 C1 SOG B 406 -7.736 27.979 15.404 1.00141.82 C
HETATM 5250 C2 SOG B 406 -7.365 29.458 15.318 1.00130.71 C
HETATM 5251 C3 SOG B 406 -6.180 29.796 16.216 1.00123.59 C
HETATM 5252 C4 SOG B 406 -6.404 29.274 17.611 1.00133.52 C
HETATM 5253 C5 SOG B 406 -6.636 27.780 17.519 1.00136.54 C
HETATM 5254 C6 SOG B 406 -6.829 27.133 18.879 1.00135.55 C
HETATM 5255 C1' SOG B 406 -9.467 26.285 13.913 1.00154.17 C
HETATM 5256 C2' SOG B 406 -10.614 26.335 12.922 1.00149.06 C
HETATM 5257 C3' SOG B 406 -10.946 24.997 12.302 1.00144.99 C
HETATM 5258 C4' SOG B 406 -11.791 24.112 13.189 1.00138.44 C
HETATM 5259 C5' SOG B 406 -12.185 22.799 12.551 1.00131.37 C
HETATM 5260 C6' SOG B 406 -12.956 21.870 13.458 1.00125.38 C
HETATM 5261 C7' SOG B 406 -13.186 20.494 12.885 1.00122.04 C
HETATM 5262 C8' SOG B 406 -13.866 19.535 13.834 1.00120.39 C
HETATM 5263 S1 SOG B 406 -9.368 27.961 14.629 1.00155.35 S
HETATM 5264 O2 SOG B 406 -7.053 29.803 13.973 1.00127.66 O
HETATM 5265 O3 SOG B 406 -5.972 31.206 16.241 1.00113.69 O
HETATM 5266 O4 SOG B 406 -5.261 29.534 18.424 1.00138.20 O
HETATM 5267 O5 SOG B 406 -7.831 27.541 16.754 1.00139.24 O
HETATM 5268 O6 SOG B 406 -6.578 25.731 18.812 1.00134.10 O
HETATM 5269 S SO4 B 407 -5.972 14.388 1.768 1.00101.57 S
HETATM 5270 O1 SO4 B 407 -7.007 13.384 1.997 1.00 98.53 O
HETATM 5271 O2 SO4 B 407 -5.706 14.518 0.336 1.00116.14 O
HETATM 5272 O3 SO4 B 407 -4.725 13.986 2.415 1.00 97.01 O
HETATM 5273 O4 SO4 B 407 -6.436 15.645 2.340 1.00 98.74 O
HETATM 5274 O HOH A 501 11.555 39.666 -19.456 1.00 64.61 O
HETATM 5275 O HOH A 502 21.558 16.312 -24.749 1.00 41.91 O
HETATM 5276 O HOH A 503 11.677 13.365 -28.155 1.00 38.58 O
HETATM 5277 O HOH A 504 13.883 32.119 -17.489 1.00 44.27 O
HETATM 5278 O HOH A 505 12.223 20.689 -28.947 1.00 75.82 O
HETATM 5279 O HOH A 506 23.061 38.277 -44.628 1.00 54.36 O
HETATM 5280 O HOH A 507 19.442 32.780 -18.258 1.00 93.93 O
HETATM 5281 O HOH A 508 -25.962 6.834 -40.982 1.00 59.66 O
HETATM 5282 O HOH B 501 -8.232 18.665 -4.478 1.00 51.62 O
HETATM 5283 O HOH B 502 -2.179 11.340 3.645 1.00 70.11 O
HETATM 5284 O HOH B 503 10.101 -13.267 -21.035 1.00 53.19 O
HETATM 5285 O HOH B 504 15.928 -13.676 -36.181 1.00 51.00 O
HETATM 5286 O HOH B 505 -7.464 12.354 -1.710 1.00 60.35 O
HETATM 5287 O HOH B 506 7.799 -28.231 -30.616 1.00 55.80 O
HETATM 5288 O HOH B 507 12.413 -4.871 -19.619 1.00 49.26 O
HETATM 5289 O HOH B 508 0.185 22.046 -12.849 1.00 35.02 O
CONECT 753 1310
CONECT 1310 753
CONECT 3022 3650
CONECT 3650 3022
CONECT 4836 4847 4862 4863 4864
CONECT 4837 4847 4854 4865
CONECT 4838 4858 4859 4861
CONECT 4839 4840 4844 4859
CONECT 4840 4839 4841 4866
CONECT 4841 4840 4842 4867
CONECT 4842 4841 4843 4860
CONECT 4843 4842 4844 4868
CONECT 4844 4839 4843 4869
CONECT 4845 4860 4870 4871 4872
CONECT 4846 4860 4873 4874 4875
CONECT 4847 4836 4837 4857
CONECT 4848 4849 4853 4857
CONECT 4849 4848 4850 4856
CONECT 4850 4849 4851 4876
CONECT 4851 4850 4852 4855
CONECT 4852 4851 4853 4877
CONECT 4853 4848 4852 4854
CONECT 4854 4837 4853 4858
CONECT 4855 4851
CONECT 4856 4849
CONECT 4857 4847 4848
CONECT 4858 4838 4854 4878
CONECT 4859 4838 4839 4879
CONECT 4860 4842 4845 4846
CONECT 4861 4838
CONECT 4862 4836
CONECT 4863 4836
CONECT 4864 4836
CONECT 4865 4837
CONECT 4866 4840
CONECT 4867 4841
CONECT 4868 4843
CONECT 4869 4844
CONECT 4870 4845
CONECT 4871 4845
CONECT 4872 4845
CONECT 4873 4846
CONECT 4874 4846
CONECT 4875 4846
CONECT 4876 4850
CONECT 4877 4852
CONECT 4878 4858
CONECT 4879 4859
CONECT 4880 4891 4906 4907 4908
CONECT 4881 4891 4898 4909
CONECT 4882 4902 4903 4905
CONECT 4883 4884 4888 4903
CONECT 4884 4883 4885 4910
CONECT 4885 4884 4886 4911
CONECT 4886 4885 4887 4904
CONECT 4887 4886 4888 4912
CONECT 4888 4883 4887 4913
CONECT 4889 4904 4914 4915 4916
CONECT 4890 4904 4917 4918 4919
CONECT 4891 4880 4881 4901
CONECT 4892 4893 4897 4901
CONECT 4893 4892 4894 4900
CONECT 4894 4893 4895 4920
CONECT 4895 4894 4896 4899
CONECT 4896 4895 4897 4921
CONECT 4897 4892 4896 4898
CONECT 4898 4881 4897 4902
CONECT 4899 4895
CONECT 4900 4893
CONECT 4901 4891 4892
CONECT 4902 4882 4898 4922
CONECT 4903 4882 4883 4923
CONECT 4904 4886 4889 4890
CONECT 4905 4882
CONECT 4906 4880
CONECT 4907 4880
CONECT 4908 4880
CONECT 4909 4881
CONECT 4910 4884
CONECT 4911 4885
CONECT 4912 4887
CONECT 4913 4888
CONECT 4914 4889
CONECT 4915 4889
CONECT 4916 4889
CONECT 4917 4890
CONECT 4918 4890
CONECT 4919 4890
CONECT 4920 4894
CONECT 4921 4896
CONECT 4922 4902
CONECT 4923 4903
CONECT 4924 4925 4938 4942
CONECT 4925 4924 4926 4939
CONECT 4926 4925 4927 4940
CONECT 4927 4926 4928 4941
CONECT 4928 4927 4929 4942
CONECT 4929 4928 4943
CONECT 4930 4931 4938
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 4936
CONECT 4938 4924 4930
CONECT 4939 4925
CONECT 4940 4926
CONECT 4941 4927
CONECT 4942 4924 4928
CONECT 4943 4929
CONECT 4944 4945 4958 4962
CONECT 4945 4944 4946 4959
CONECT 4946 4945 4947 4960
CONECT 4947 4946 4948 4961
CONECT 4948 4947 4949 4962
CONECT 4949 4948 4963
CONECT 4950 4951 4958
CONECT 4951 4950 4952
CONECT 4952 4951 4953
CONECT 4953 4952 4954
CONECT 4954 4953 4955
CONECT 4955 4954 4956
CONECT 4956 4955 4957
CONECT 4957 4956
CONECT 4958 4944 4950
CONECT 4959 4945
CONECT 4960 4946
CONECT 4961 4947
CONECT 4962 4944 4948
CONECT 4963 4949
CONECT 4964 4965 4978 4982
CONECT 4965 4964 4966 4979
CONECT 4966 4965 4967 4980
CONECT 4967 4966 4968 4981
CONECT 4968 4967 4969 4982
CONECT 4969 4968 4983
CONECT 4970 4971 4978
CONECT 4971 4970 4972
CONECT 4972 4971 4973
CONECT 4973 4972 4974
CONECT 4974 4973 4975
CONECT 4975 4974 4976
CONECT 4976 4975 4977
CONECT 4977 4976
CONECT 4978 4964 4970
CONECT 4979 4965
CONECT 4980 4966
CONECT 4981 4967
CONECT 4982 4964 4968
CONECT 4983 4969
CONECT 4984 4985 4998 5002
CONECT 4985 4984 4986 4999
CONECT 4986 4985 4987 5000
CONECT 4987 4986 4988 5001
CONECT 4988 4987 4989 5002
CONECT 4989 4988 5003
CONECT 4990 4991 4998
CONECT 4991 4990 4992
CONECT 4992 4991 4993
CONECT 4993 4992 4994
CONECT 4994 4993 4995
CONECT 4995 4994 4996
CONECT 4996 4995 4997
CONECT 4997 4996
CONECT 4998 4984 4990
CONECT 4999 4985
CONECT 5000 4986
CONECT 5001 4987
CONECT 5002 4984 4988
CONECT 5003 4989
CONECT 5004 5005 5018 5022
CONECT 5005 5004 5006 5019
CONECT 5006 5005 5007 5020
CONECT 5007 5006 5008 5021
CONECT 5008 5007 5009 5022
CONECT 5009 5008 5023
CONECT 5010 5011 5018
CONECT 5011 5010 5012
CONECT 5012 5011 5013
CONECT 5013 5012 5014
CONECT 5014 5013 5015
CONECT 5015 5014 5016
CONECT 5016 5015 5017
CONECT 5017 5016
CONECT 5018 5004 5010
CONECT 5019 5005
CONECT 5020 5006
CONECT 5021 5007
CONECT 5022 5004 5008
CONECT 5023 5009
CONECT 5024 5025 5026 5027 5028
CONECT 5025 5024
CONECT 5026 5024
CONECT 5027 5024
CONECT 5028 5024
CONECT 5029 5030 5031 5032 5033
CONECT 5030 5029
CONECT 5031 5029
CONECT 5032 5029
CONECT 5033 5029
CONECT 5034 5035 5050
CONECT 5035 5034
CONECT 5036 5050
CONECT 5037 5062 5064 5066 5068
CONECT 5038 5041 5046
CONECT 5039 5040 5042 5043
CONECT 5040 5039 5041
CONECT 5041 5038 5040 5044
CONECT 5042 5039 5045
CONECT 5043 5039
CONECT 5044 5041 5062
CONECT 5045 5042 5048
CONECT 5046 5038 5073
CONECT 5047 5050 5064
CONECT 5048 5045 5051
CONECT 5049 5073
CONECT 5050 5034 5036 5047
CONECT 5051 5048 5053
CONECT 5052 5054 5060
CONECT 5053 5051 5055
CONECT 5054 5052 5056
CONECT 5055 5053 5057
CONECT 5056 5054 5058
CONECT 5057 5055 5059
CONECT 5058 5056 5061
CONECT 5059 5057 5060
CONECT 5060 5052 5059
CONECT 5061 5058 5063
CONECT 5062 5037 5044
CONECT 5063 5061 5065
CONECT 5064 5037 5047
CONECT 5065 5063 5067
CONECT 5066 5037
CONECT 5067 5065
CONECT 5068 5037
CONECT 5069 5070 5081
CONECT 5070 5069 5071
CONECT 5071 5070 5072
CONECT 5072 5071 5082
CONECT 5073 5046 5049 5074
CONECT 5074 5073 5075
CONECT 5075 5074 5076
CONECT 5076 5075 5077
CONECT 5077 5076 5078
CONECT 5078 5077 5079
CONECT 5079 5078 5080
CONECT 5080 5079 5081
CONECT 5081 5069 5080
CONECT 5082 5072 5084
CONECT 5083 5084
CONECT 5084 5082 5083
CONECT 5085 5086 5101
CONECT 5086 5085
CONECT 5087 5101
CONECT 5088 5113 5115 5117 5119
CONECT 5089 5092 5097
CONECT 5090 5091 5093 5094
CONECT 5091 5090 5092
CONECT 5092 5089 5091 5095
CONECT 5093 5090 5096
CONECT 5094 5090
CONECT 5095 5092 5113
CONECT 5096 5093 5099
CONECT 5097 5089 5124
CONECT 5098 5101 5115
CONECT 5099 5096 5102
CONECT 5100 5124
CONECT 5101 5085 5087 5098
CONECT 5102 5099 5104
CONECT 5103 5105 5111
CONECT 5104 5102 5106
CONECT 5105 5103 5107
CONECT 5106 5104 5108
CONECT 5107 5105 5109
CONECT 5108 5106 5110
CONECT 5109 5107 5112
CONECT 5110 5108 5111
CONECT 5111 5103 5110
CONECT 5112 5109 5114
CONECT 5113 5088 5095
CONECT 5114 5112 5116
CONECT 5115 5088 5098
CONECT 5116 5114 5118
CONECT 5117 5088
CONECT 5118 5116
CONECT 5119 5088
CONECT 5120 5121 5132
CONECT 5121 5120 5122
CONECT 5122 5121 5123
CONECT 5123 5122 5133
CONECT 5124 5097 5100 5125
CONECT 5125 5124 5126
CONECT 5126 5125 5127
CONECT 5127 5126 5128
CONECT 5128 5127 5129
CONECT 5129 5128 5130
CONECT 5130 5129 5131
CONECT 5131 5130 5132
CONECT 5132 5120 5131
CONECT 5133 5123 5135
CONECT 5134 5135
CONECT 5135 5133 5134
CONECT 5136 5147 5162 5163 5164
CONECT 5137 5147 5154 5165
CONECT 5138 5158 5159 5161
CONECT 5139 5140 5144 5159
CONECT 5140 5139 5141 5166
CONECT 5141 5140 5142 5167
CONECT 5142 5141 5143 5160
CONECT 5143 5142 5144 5168
CONECT 5144 5139 5143 5169
CONECT 5145 5160 5170 5171 5172
CONECT 5146 5160 5173 5174 5175
CONECT 5147 5136 5137 5157
CONECT 5148 5149 5153 5157
CONECT 5149 5148 5150 5156
CONECT 5150 5149 5151 5176
CONECT 5151 5150 5152 5155
CONECT 5152 5151 5153 5177
CONECT 5153 5148 5152 5154
CONECT 5154 5137 5153 5158
CONECT 5155 5151
CONECT 5156 5149
CONECT 5157 5147 5148
CONECT 5158 5138 5154 5178
CONECT 5159 5138 5139 5179
CONECT 5160 5142 5145 5146
CONECT 5161 5138
CONECT 5162 5136
CONECT 5163 5136
CONECT 5164 5136
CONECT 5165 5137
CONECT 5166 5140
CONECT 5167 5141
CONECT 5168 5143
CONECT 5169 5144
CONECT 5170 5145
CONECT 5171 5145
CONECT 5172 5145
CONECT 5173 5146
CONECT 5174 5146
CONECT 5175 5146
CONECT 5176 5150
CONECT 5177 5152
CONECT 5178 5158
CONECT 5179 5159
CONECT 5180 5181 5194 5198
CONECT 5181 5180 5182 5195
CONECT 5182 5181 5183 5196
CONECT 5183 5182 5184 5197
CONECT 5184 5183 5185 5198
CONECT 5185 5184 5199
CONECT 5186 5187 5194
CONECT 5187 5186 5188
CONECT 5188 5187 5189
CONECT 5189 5188 5190
CONECT 5190 5189 5191
CONECT 5191 5190 5192
CONECT 5192 5191 5193
CONECT 5193 5192
CONECT 5194 5180 5186
CONECT 5195 5181
CONECT 5196 5182
CONECT 5197 5183
CONECT 5198 5180 5184
CONECT 5199 5185
CONECT 5200 5201 5214 5218
CONECT 5201 5200 5202 5215
CONECT 5202 5201 5203 5216
CONECT 5203 5202 5204 5217
CONECT 5204 5203 5205 5218
CONECT 5205 5204 5219
CONECT 5206 5207 5214
CONECT 5207 5206 5208
CONECT 5208 5207 5209
CONECT 5209 5208 5210
CONECT 5210 5209 5211
CONECT 5211 5210 5212
CONECT 5212 5211 5213
CONECT 5213 5212
CONECT 5214 5200 5206
CONECT 5215 5201
CONECT 5216 5202
CONECT 5217 5203
CONECT 5218 5200 5204
CONECT 5219 5205
CONECT 5220 5221 5228
CONECT 5221 5220 5222
CONECT 5222 5221 5223
CONECT 5223 5222 5224
CONECT 5224 5223 5225
CONECT 5225 5224 5226
CONECT 5226 5225 5227
CONECT 5227 5226
CONECT 5228 5220
CONECT 5229 5230 5243 5247
CONECT 5230 5229 5231 5244
CONECT 5231 5230 5232 5245
CONECT 5232 5231 5233 5246
CONECT 5233 5232 5234 5247
CONECT 5234 5233 5248
CONECT 5235 5236 5243
CONECT 5236 5235 5237
CONECT 5237 5236 5238
CONECT 5238 5237 5239
CONECT 5239 5238 5240
CONECT 5240 5239 5241
CONECT 5241 5240 5242
CONECT 5242 5241
CONECT 5243 5229 5235
CONECT 5244 5230
CONECT 5245 5231
CONECT 5246 5232
CONECT 5247 5229 5233
CONECT 5248 5234
CONECT 5249 5250 5263 5267
CONECT 5250 5249 5251 5264
CONECT 5251 5250 5252 5265
CONECT 5252 5251 5253 5266
CONECT 5253 5252 5254 5267
CONECT 5254 5253 5268
CONECT 5255 5256 5263
CONECT 5256 5255 5257
CONECT 5257 5256 5258
CONECT 5258 5257 5259
CONECT 5259 5258 5260
CONECT 5260 5259 5261
CONECT 5261 5260 5262
CONECT 5262 5261
CONECT 5263 5249 5255
CONECT 5264 5250
CONECT 5265 5251
CONECT 5266 5252
CONECT 5267 5249 5253
CONECT 5268 5254
CONECT 5269 5270 5271 5272 5273
CONECT 5270 5269
CONECT 5271 5269
CONECT 5272 5269
CONECT 5273 5269
MASTER 365 0 18 27 4 0 0 6 5233 2 442 52
END