HEADER MEMBRANE PROTEIN 11-MAY-22 7XRR
TITLE CRYSTAL STRUCTURE OF THE HUMAN OX2R BOUND TO THE INSOMNIA DRUG
TITLE 2 LEMBOREXANT.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OREXIN RECEPTOR TYPE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OX-2-R,OX2-R,OX2R,HYPOCRETIN RECEPTOR TYPE 2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HCRTR2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS GPCR, INSOMNIA DRUG, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.ASADA,D.IM,S.IWATA
REVDAT 3 14-DEC-22 7XRR 1 JRNL
REVDAT 2 07-DEC-22 7XRR 1 JRNL
REVDAT 1 23-NOV-22 7XRR 0
JRNL AUTH H.ASADA,D.IM,Y.HOTTA,S.YASUDA,T.MURATA,R.SUNO,S.IWATA
JRNL TITL MOLECULAR BASIS FOR ANTI-INSOMNIA DRUG DESIGN FROM STRUCTURE
JRNL TITL 2 OF LEMBOREXANT-BOUND OREXIN 2 RECEPTOR.
JRNL REF STRUCTURE V. 30 1582 2022
JRNL REFN ISSN 0969-2126
JRNL PMID 36417909
JRNL DOI 10.1016/J.STR.2022.11.001
REMARK 2
REMARK 2 RESOLUTION. 2.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 11819
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.276
REMARK 3 R VALUE (WORKING SET) : 0.275
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1182
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 40.5300 - 5.7800 1.00 1428 158 0.2304 0.2176
REMARK 3 2 5.7800 - 4.5900 1.00 1342 150 0.2542 0.3065
REMARK 3 3 4.5900 - 4.0100 1.00 1338 149 0.2728 0.2678
REMARK 3 4 4.0100 - 3.6400 1.00 1310 144 0.2778 0.2844
REMARK 3 5 3.6400 - 3.3800 1.00 1319 148 0.2934 0.3383
REMARK 3 6 3.3800 - 3.1800 1.00 1301 145 0.3139 0.2860
REMARK 3 7 3.1800 - 3.0200 1.00 1306 144 0.3462 0.3733
REMARK 3 8 3.0200 - 2.8900 1.00 1293 144 0.4076 0.4294
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.470
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.150
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 72.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.05
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 : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 107 THROUGH 218 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0926 9.0468 27.3731
REMARK 3 T TENSOR
REMARK 3 T11: 0.5191 T22: 0.6308
REMARK 3 T33: 0.6144 T12: 0.0287
REMARK 3 T13: -0.0157 T23: -0.0956
REMARK 3 L TENSOR
REMARK 3 L11: 0.9605 L22: 3.9510
REMARK 3 L33: 3.0234 L12: 0.4659
REMARK 3 L13: 0.9764 L23: 2.4331
REMARK 3 S TENSOR
REMARK 3 S11: -0.0408 S12: 0.1620 S13: 0.0099
REMARK 3 S21: -0.6295 S22: -0.4461 S23: 0.4762
REMARK 3 S31: -0.3328 S32: -0.3163 S33: 0.6095
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 219 THROUGH 328 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8290 14.6521 38.7322
REMARK 3 T TENSOR
REMARK 3 T11: 0.2415 T22: 0.4032
REMARK 3 T33: 0.3713 T12: 0.0322
REMARK 3 T13: 0.0372 T23: -0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 2.1849 L22: 3.2733
REMARK 3 L33: 6.6563 L12: 1.1998
REMARK 3 L13: 1.8490 L23: 2.2999
REMARK 3 S TENSOR
REMARK 3 S11: -0.1319 S12: -0.1547 S13: 0.2122
REMARK 3 S21: -0.1515 S22: -0.2265 S23: 0.0345
REMARK 3 S31: -0.1737 S32: -0.3339 S33: 0.3609
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 329 THROUGH 384 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2114 -0.4124 30.5058
REMARK 3 T TENSOR
REMARK 3 T11: 0.2515 T22: 0.5313
REMARK 3 T33: 0.5597 T12: 0.0684
REMARK 3 T13: -0.0095 T23: -0.1215
REMARK 3 L TENSOR
REMARK 3 L11: 2.9378 L22: 6.3907
REMARK 3 L33: 3.6120 L12: 0.9398
REMARK 3 L13: -0.1948 L23: 3.1602
REMARK 3 S TENSOR
REMARK 3 S11: 0.0820 S12: 0.3812 S13: -0.2808
REMARK 3 S21: -0.0067 S22: -0.1813 S23: 0.4120
REMARK 3 S31: 0.5955 S32: -0.3397 S33: 0.1154
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 53 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5705 -10.7998 5.7107
REMARK 3 T TENSOR
REMARK 3 T11: 0.9143 T22: 0.8868
REMARK 3 T33: 0.6473 T12: -0.0812
REMARK 3 T13: 0.1142 T23: -0.2037
REMARK 3 L TENSOR
REMARK 3 L11: 5.9990 L22: 2.4980
REMARK 3 L33: 8.8691 L12: 2.1882
REMARK 3 L13: 5.6085 L23: 3.1851
REMARK 3 S TENSOR
REMARK 3 S11: -0.5519 S12: -0.4370 S13: 1.5774
REMARK 3 S21: -0.3441 S22: 0.2295 S23: -0.1569
REMARK 3 S31: -0.2533 S32: -0.4971 S33: -0.0600
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 54 THROUGH 106 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3271 -2.8145 38.1481
REMARK 3 T TENSOR
REMARK 3 T11: 0.4277 T22: 0.5649
REMARK 3 T33: 0.5716 T12: -0.1746
REMARK 3 T13: 0.0048 T23: -0.1048
REMARK 3 L TENSOR
REMARK 3 L11: 1.5731 L22: 5.5023
REMARK 3 L33: 5.9148 L12: -1.7002
REMARK 3 L13: -1.5710 L23: 3.7406
REMARK 3 S TENSOR
REMARK 3 S11: -0.2386 S12: -0.1979 S13: -0.4565
REMARK 3 S21: 0.9082 S22: -0.1367 S23: 0.3436
REMARK 3 S31: 1.0186 S32: 0.0714 S33: 0.1321
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7XRR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAY-22.
REMARK 100 THE DEPOSITION ID IS D_1300029467.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL32XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11873
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.890
REMARK 200 RESOLUTION RANGE LOW (A) : 40.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 59.79
REMARK 200 R MERGE (I) : 0.71300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 57.87
REMARK 200 R MERGE FOR SHELL (I) : 4.98600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.810
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: 5WQC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 21-28% PEG300, 80-120 MM POTASSIUM
REMARK 280 CITRATE TRIBASIC MONOHYDRATE, 0.1 M MES, PH 6.0, LIPIDIC CUBIC
REMARK 280 PHASE, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 24.79500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.16000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.11500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.16000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.79500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.11500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 29
REMARK 465 PRO A 30
REMARK 465 LEU A 31
REMARK 465 GLU A 32
REMARK 465 ASP A 33
REMARK 465 TYR A 34
REMARK 465 ASP A 35
REMARK 465 ASP A 36
REMARK 465 PHE A 197
REMARK 465 PRO A 198
REMARK 465 GLY A 199
REMARK 465 LEU A 200
REMARK 465 ALA A 201
REMARK 465 GLN A 202
REMARK 465 LYS A 203
REMARK 465 THR A 204
REMARK 465 GLY A 385
REMARK 465 VAL A 386
REMARK 465 HIS A 387
REMARK 465 HIS A 388
REMARK 465 ARG A 389
REMARK 465 GLN A 390
REMARK 465 GLU A 391
REMARK 465 ASP A 392
REMARK 465 ARG A 393
REMARK 465 LEU A 394
REMARK 465 LEU A 395
REMARK 465 GLU A 396
REMARK 465 VAL A 397
REMARK 465 LEU A 398
REMARK 465 PHE A 399
REMARK 465 GLN A 400
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PHE A 121 -4.98 74.13
REMARK 500 TYR A 232 -50.85 -120.50
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7XRR A 33 394 UNP O43614 OX2R_HUMAN 33 394
SEQADV 7XRR GLY A 29 UNP O43614 EXPRESSION TAG
SEQADV 7XRR PRO A 30 UNP O43614 EXPRESSION TAG
SEQADV 7XRR LEU A 31 UNP O43614 EXPRESSION TAG
SEQADV 7XRR GLU A 32 UNP O43614 EXPRESSION TAG
SEQADV 7XRR ALA A 100 UNP O43614 ASP 100 ENGINEERED MUTATION
SEQADV 7XRR TRP A 143 UNP O43614 LEU 143 ENGINEERED MUTATION
SEQADV 7XRR ALA A 147 UNP O43614 CYS 147 ENGINEERED MUTATION
SEQADV 7XRR GLN A 202 UNP O43614 ASN 202 ENGINEERED MUTATION
SEQADV 7XRR A UNP O43614 THR 258 DELETION
SEQADV 7XRR A UNP O43614 SER 259 DELETION
SEQADV 7XRR A UNP O43614 SER 260 DELETION
SEQADV 7XRR A UNP O43614 VAL 261 DELETION
SEQADV 7XRR A UNP O43614 VAL 262 DELETION
SEQADV 7XRR A UNP O43614 GLN 263 DELETION
SEQADV 7XRR A UNP O43614 ARG 264 DELETION
SEQADV 7XRR A UNP O43614 LYS 265 DELETION
SEQADV 7XRR A UNP O43614 TRP 266 DELETION
SEQADV 7XRR A UNP O43614 LYS 267 DELETION
SEQADV 7XRR A UNP O43614 PRO 268 DELETION
SEQADV 7XRR A UNP O43614 LEU 269 DELETION
SEQADV 7XRR A UNP O43614 GLN 270 DELETION
SEQADV 7XRR A UNP O43614 PRO 271 DELETION
SEQADV 7XRR A UNP O43614 VAL 272 DELETION
SEQADV 7XRR A UNP O43614 SER 273 DELETION
SEQADV 7XRR A UNP O43614 GLN 274 DELETION
SEQADV 7XRR A UNP O43614 PRO 275 DELETION
SEQADV 7XRR A UNP O43614 ARG 276 DELETION
SEQADV 7XRR A UNP O43614 GLY 277 DELETION
SEQADV 7XRR A UNP O43614 PRO 278 DELETION
SEQADV 7XRR A UNP O43614 GLY 279 DELETION
SEQADV 7XRR A UNP O43614 GLN 280 DELETION
SEQADV 7XRR A UNP O43614 PRO 281 DELETION
SEQADV 7XRR A UNP O43614 THR 282 DELETION
SEQADV 7XRR A UNP O43614 LYS 283 DELETION
SEQADV 7XRR A UNP O43614 SER 284 DELETION
SEQADV 7XRR A UNP O43614 ARG 285 DELETION
SEQADV 7XRR A UNP O43614 MET 286 DELETION
SEQADV 7XRR A UNP O43614 SER 287 DELETION
SEQADV 7XRR A UNP O43614 ALA 288 DELETION
SEQADV 7XRR LEU A 395 UNP O43614 EXPRESSION TAG
SEQADV 7XRR GLU A 396 UNP O43614 EXPRESSION TAG
SEQADV 7XRR VAL A 397 UNP O43614 EXPRESSION TAG
SEQADV 7XRR LEU A 398 UNP O43614 EXPRESSION TAG
SEQADV 7XRR PHE A 399 UNP O43614 EXPRESSION TAG
SEQADV 7XRR GLN A 400 UNP O43614 EXPRESSION TAG
SEQRES 1 A 341 GLY PRO LEU GLU ASP TYR ASP ASP GLU GLU PHE LEU ARG
SEQRES 2 A 341 TYR LEU TRP ARG GLU TYR LEU HIS PRO LYS GLU TYR GLU
SEQRES 3 A 341 TRP VAL LEU ILE ALA GLY TYR ILE ILE VAL PHE VAL VAL
SEQRES 4 A 341 ALA LEU ILE GLY ASN VAL LEU VAL CYS VAL ALA VAL TRP
SEQRES 5 A 341 LYS ASN HIS HIS MET ARG THR VAL THR ASN TYR PHE ILE
SEQRES 6 A 341 VAL ASN LEU SER LEU ALA ALA VAL LEU VAL THR ILE THR
SEQRES 7 A 341 CYS LEU PRO ALA THR LEU VAL VAL ASP ILE THR GLU THR
SEQRES 8 A 341 TRP PHE PHE GLY GLN SER LEU CYS LYS VAL ILE PRO TYR
SEQRES 9 A 341 LEU GLN THR VAL SER VAL SER VAL SER VAL TRP THR LEU
SEQRES 10 A 341 SER ALA ILE ALA LEU ASP ARG TRP TYR ALA ILE CYS HIS
SEQRES 11 A 341 PRO LEU MET PHE LYS SER THR ALA LYS ARG ALA ARG ASN
SEQRES 12 A 341 SER ILE VAL ILE ILE TRP ILE VAL SER CYS ILE ILE MET
SEQRES 13 A 341 ILE PRO GLN ALA ILE VAL MET GLU CYS SER THR VAL PHE
SEQRES 14 A 341 PRO GLY LEU ALA GLN LYS THR THR LEU PHE THR VAL CYS
SEQRES 15 A 341 ASP GLU ARG TRP GLY GLY GLU ILE TYR PRO LYS MET TYR
SEQRES 16 A 341 HIS ILE CYS PHE PHE LEU VAL THR TYR MET ALA PRO LEU
SEQRES 17 A 341 CYS LEU MET VAL LEU ALA TYR LEU GLN ILE PHE ARG LYS
SEQRES 18 A 341 LEU TRP CYS ARG GLN ILE PRO GLY VAL ALA ALA GLU ILE
SEQRES 19 A 341 LYS GLN ILE ARG ALA ARG ARG LYS THR ALA ARG MET LEU
SEQRES 20 A 341 MET ILE VAL LEU LEU VAL PHE ALA ILE CYS TYR LEU PRO
SEQRES 21 A 341 ILE SER ILE LEU ASN VAL LEU LYS ARG VAL PHE GLY MET
SEQRES 22 A 341 PHE ALA HIS THR GLU ASP ARG GLU THR VAL TYR ALA TRP
SEQRES 23 A 341 PHE THR PHE SER HIS TRP LEU VAL TYR ALA ASN SER ALA
SEQRES 24 A 341 ALA ASN PRO ILE ILE TYR ASN PHE LEU SER GLY LYS PHE
SEQRES 25 A 341 ARG GLU GLU PHE LYS ALA ALA PHE SER CYS CYS CYS LEU
SEQRES 26 A 341 GLY VAL HIS HIS ARG GLN GLU ASP ARG LEU LEU GLU VAL
SEQRES 27 A 341 LEU PHE GLN
HET NRK A1001 30
HETNAM NRK (1~{R},2~{S})-2-[(2,4-DIMETHYLPYRIMIDIN-5-YL)
HETNAM 2 NRK OXYMETHYL]-~{N}-(5-FLUORANYLPYRIDIN-2-YL)-2-(3-
HETNAM 3 NRK FLUOROPHENYL)CYCLOPROPANE-1-CARBOXAMIDE
FORMUL 2 NRK C22 H20 F2 N4 O2
HELIX 1 AA1 GLU A 37 HIS A 49 1 13
HELIX 2 AA2 TYR A 53 ASN A 82 1 30
HELIX 3 AA3 THR A 87 CYS A 107 1 21
HELIX 4 AA4 CYS A 107 GLU A 118 1 12
HELIX 5 AA5 GLY A 123 CYS A 157 1 35
HELIX 6 AA6 THR A 165 MET A 184 1 20
HELIX 7 AA7 MET A 184 VAL A 190 1 7
HELIX 8 AA8 ILE A 218 TYR A 232 1 15
HELIX 9 AA9 TYR A 232 CYS A 252 1 21
HELIX 10 AB1 VAL A 289 VAL A 329 1 41
HELIX 11 AB2 ASP A 338 SER A 368 1 31
HELIX 12 AB3 SER A 368 LEU A 384 1 17
SHEET 1 AA1 2 MET A 191 SER A 194 0
SHEET 2 AA1 2 VAL A 209 GLU A 212 -1 O ASP A 211 N GLU A 192
SSBOND 1 CYS A 127 CYS A 210 1555 1555 2.02
CRYST1 49.590 90.230 112.320 90.00 90.00 90.00 P 21 21 21 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 0.020165 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008903 0.00000
ATOM 1 N GLU A 37 -9.927 -13.050 4.312 1.00106.97 N
ANISOU 1 N GLU A 37 13037 18316 9290 -1194 847 -2659 N
ATOM 2 CA GLU A 37 -9.219 -12.475 3.174 1.00111.91 C
ANISOU 2 CA GLU A 37 14025 18062 10434 -996 704 -2291 C
ATOM 3 C GLU A 37 -8.147 -11.492 3.629 1.00111.19 C
ANISOU 3 C GLU A 37 13943 17424 10882 -670 565 -2450 C
ATOM 4 O GLU A 37 -7.021 -11.518 3.134 1.00105.86 O
ANISOU 4 O GLU A 37 13662 16146 10415 -760 629 -2072 O
ATOM 5 CB GLU A 37 -10.200 -11.781 2.228 1.00119.93 C
ANISOU 5 CB GLU A 37 14879 19013 11677 -737 410 -2344 C
ATOM 6 CG GLU A 37 -11.200 -12.719 1.576 1.00124.49 C
ANISOU 6 CG GLU A 37 15485 20056 11760 -1073 534 -2129 C
ATOM 7 CD GLU A 37 -12.151 -11.996 0.644 1.00124.51 C
ANISOU 7 CD GLU A 37 15319 19982 12006 -776 199 -2204 C
ATOM 8 OE1 GLU A 37 -12.164 -10.747 0.658 1.00130.91 O
ANISOU 8 OE1 GLU A 37 15950 20438 13353 -276 -188 -2507 O
ATOM 9 OE2 GLU A 37 -12.883 -12.677 -0.105 1.00119.27 O
ANISOU 9 OE2 GLU A 37 14734 19579 11006 -1035 270 -1965 O
ATOM 10 N GLU A 38 -8.510 -10.622 4.575 1.00133.46 N
ANISOU 10 N GLU A 38 16292 20510 13908 -298 364 -3055 N
ATOM 11 CA GLU A 38 -7.545 -9.666 5.110 1.00129.02 C
ANISOU 11 CA GLU A 38 15719 19448 13852 7 194 -3257 C
ATOM 12 C GLU A 38 -6.399 -10.379 5.817 1.00121.26 C
ANISOU 12 C GLU A 38 14963 18440 12672 -271 504 -3096 C
ATOM 13 O GLU A 38 -5.243 -9.949 5.733 1.00118.67 O
ANISOU 13 O GLU A 38 14865 17513 12711 -211 467 -2942 O
ATOM 14 CB GLU A 38 -8.243 -8.691 6.058 1.00128.76 C
ANISOU 14 CB GLU A 38 15103 19795 14025 488 -102 -4031 C
ATOM 15 CG GLU A 38 -8.410 -7.285 5.503 1.00133.12 C
ANISOU 15 CG GLU A 38 15615 19710 15253 1002 -656 -4226 C
ATOM 16 CD GLU A 38 -7.082 -6.607 5.221 1.00131.77 C
ANISOU 16 CD GLU A 38 15864 18604 15599 1015 -807 -3905 C
ATOM 17 OE1 GLU A 38 -6.957 -5.959 4.160 1.00136.63 O
ANISOU 17 OE1 GLU A 38 16798 18520 16594 1063 -1136 -3566 O
ATOM 18 OE2 GLU A 38 -6.162 -6.724 6.058 1.00127.43 O
ANISOU 18 OE2 GLU A 38 15328 18047 15042 931 -610 -3979 O
ATOM 19 N PHE A 39 -6.703 -11.468 6.527 1.00103.33 N
ANISOU 19 N PHE A 39 12638 16821 9802 -603 771 -3130 N
ATOM 20 CA PHE A 39 -5.651 -12.258 7.157 1.00 94.47 C
ANISOU 20 CA PHE A 39 11801 15633 8460 -867 988 -2948 C
ATOM 21 C PHE A 39 -4.736 -12.885 6.111 1.00 89.08 C
ANISOU 21 C PHE A 39 11662 14359 7824 -1070 1101 -2368 C
ATOM 22 O PHE A 39 -3.516 -12.953 6.303 1.00 82.88 O
ANISOU 22 O PHE A 39 11089 13200 7201 -1062 1156 -2271 O
ATOM 23 CB PHE A 39 -6.268 -13.332 8.053 1.00 89.10 C
ANISOU 23 CB PHE A 39 11034 15744 7075 -1265 1159 -3037 C
ATOM 24 CG PHE A 39 -5.260 -14.235 8.702 1.00 79.91 C
ANISOU 24 CG PHE A 39 10229 14380 5754 -1514 1254 -2765 C
ATOM 25 CD1 PHE A 39 -4.413 -13.754 9.686 1.00 79.43 C
ANISOU 25 CD1 PHE A 39 10061 14262 5858 -1334 1231 -3067 C
ATOM 26 CD2 PHE A 39 -5.164 -15.568 8.335 1.00 76.47 C
ANISOU 26 CD2 PHE A 39 10220 13682 5154 -1837 1267 -2196 C
ATOM 27 CE1 PHE A 39 -3.485 -14.582 10.287 1.00 79.24 C
ANISOU 27 CE1 PHE A 39 10360 13979 5769 -1498 1238 -2793 C
ATOM 28 CE2 PHE A 39 -4.239 -16.401 8.934 1.00 69.64 C
ANISOU 28 CE2 PHE A 39 9673 12528 4261 -1946 1227 -1977 C
ATOM 29 CZ PHE A 39 -3.398 -15.908 9.911 1.00 74.06 C
ANISOU 29 CZ PHE A 39 10136 13082 4921 -1789 1219 -2265 C
ATOM 30 N LEU A 40 -5.310 -13.351 4.998 1.00 90.56 N
ANISOU 30 N LEU A 40 12040 14515 7854 -1243 1131 -2029 N
ATOM 31 CA LEU A 40 -4.497 -13.903 3.919 1.00 86.51 C
ANISOU 31 CA LEU A 40 11984 13520 7365 -1409 1229 -1548 C
ATOM 32 C LEU A 40 -3.572 -12.846 3.327 1.00 82.79 C
ANISOU 32 C LEU A 40 11559 12443 7456 -1195 1122 -1467 C
ATOM 33 O LEU A 40 -2.409 -13.131 3.017 1.00 76.57 O
ANISOU 33 O LEU A 40 11019 11344 6729 -1286 1232 -1266 O
ATOM 34 CB LEU A 40 -5.397 -14.498 2.836 1.00 89.83 C
ANISOU 34 CB LEU A 40 12557 14065 7510 -1620 1255 -1247 C
ATOM 35 CG LEU A 40 -6.278 -15.672 3.266 1.00 91.28 C
ANISOU 35 CG LEU A 40 12776 14831 7075 -1968 1349 -1232 C
ATOM 36 CD1 LEU A 40 -7.202 -16.095 2.134 1.00 95.35 C
ANISOU 36 CD1 LEU A 40 13389 15417 7424 -2128 1332 -953 C
ATOM 37 CD2 LEU A 40 -5.421 -16.841 3.729 1.00 82.06 C
ANISOU 37 CD2 LEU A 40 11905 13381 5894 -2080 1352 -1000 C
ATOM 38 N ARG A 41 -4.074 -11.620 3.155 1.00 91.28 N
ANISOU 38 N ARG A 41 12398 13357 8927 -928 864 -1638 N
ATOM 39 CA ARG A 41 -3.231 -10.545 2.641 1.00 87.75 C
ANISOU 39 CA ARG A 41 12045 12302 8995 -815 683 -1524 C
ATOM 40 C ARG A 41 -2.107 -10.207 3.610 1.00 83.14 C
ANISOU 40 C ARG A 41 11391 11571 8629 -720 712 -1751 C
ATOM 41 O ARG A 41 -1.009 -9.836 3.181 1.00 81.79 O
ANISOU 41 O ARG A 41 11386 10990 8701 -818 715 -1550 O
ATOM 42 CB ARG A 41 -4.078 -9.305 2.352 1.00 98.58 C
ANISOU 42 CB ARG A 41 13237 13462 10757 -522 269 -1692 C
ATOM 43 CG ARG A 41 -5.177 -9.539 1.331 1.00106.02 C
ANISOU 43 CG ARG A 41 14240 14521 11522 -586 188 -1475 C
ATOM 44 CD ARG A 41 -6.125 -8.355 1.246 1.00113.33 C
ANISOU 44 CD ARG A 41 14938 15294 12829 -192 -308 -1773 C
ATOM 45 NE ARG A 41 -5.496 -7.182 0.650 1.00114.65 N
ANISOU 45 NE ARG A 41 15346 14699 13519 -130 -695 -1573 N
ATOM 46 CZ ARG A 41 -6.106 -6.018 0.471 1.00121.24 C
ANISOU 46 CZ ARG A 41 16116 15165 14783 223 -1271 -1778 C
ATOM 47 NH1 ARG A 41 -5.490 -4.996 -0.100 1.00124.79 N
ANISOU 47 NH1 ARG A 41 16884 14861 15670 173 -1679 -1512 N
ATOM 48 NH2 ARG A 41 -7.365 -5.877 0.874 1.00122.83 N
ANISOU 48 NH2 ARG A 41 15928 15781 14960 620 -1486 -2280 N
ATOM 49 N TYR A 42 -2.363 -10.318 4.917 1.00 81.59 N
ANISOU 49 N TYR A 42 10923 11762 8314 -569 735 -2179 N
ATOM 50 CA TYR A 42 -1.302 -10.109 5.897 1.00 77.52 C
ANISOU 50 CA TYR A 42 10347 11154 7955 -488 771 -2402 C
ATOM 51 C TYR A 42 -0.218 -11.172 5.771 1.00 73.97 C
ANISOU 51 C TYR A 42 10193 10663 7250 -743 1039 -2129 C
ATOM 52 O TYR A 42 0.976 -10.866 5.875 1.00 71.88 O
ANISOU 52 O TYR A 42 9978 10108 7227 -730 1055 -2127 O
ATOM 53 CB TYR A 42 -1.884 -10.099 7.311 1.00 79.44 C
ANISOU 53 CB TYR A 42 10234 11921 8027 -318 747 -2917 C
ATOM 54 CG TYR A 42 -0.875 -10.446 8.382 1.00 75.26 C
ANISOU 54 CG TYR A 42 9717 11464 7413 -352 871 -3069 C
ATOM 55 CD1 TYR A 42 0.149 -9.568 8.711 1.00 75.97 C
ANISOU 55 CD1 TYR A 42 9759 11147 7960 -175 752 -3220 C
ATOM 56 CD2 TYR A 42 -0.947 -11.654 9.063 1.00 73.62 C
ANISOU 56 CD2 TYR A 42 9605 11712 6657 -593 1057 -3046 C
ATOM 57 CE1 TYR A 42 1.076 -9.885 9.686 1.00 77.75 C
ANISOU 57 CE1 TYR A 42 9982 11450 8109 -188 846 -3376 C
ATOM 58 CE2 TYR A 42 -0.027 -11.978 10.042 1.00 76.19 C
ANISOU 58 CE2 TYR A 42 9979 12070 6899 -613 1105 -3176 C
ATOM 59 CZ TYR A 42 0.982 -11.090 10.350 1.00 79.14 C
ANISOU 59 CZ TYR A 42 10256 12068 7745 -384 1014 -3359 C
ATOM 60 OH TYR A 42 1.902 -11.407 11.323 1.00 82.09 O
ANISOU 60 OH TYR A 42 10663 12489 8040 -385 1044 -3507 O
ATOM 61 N LEU A 43 -0.614 -12.428 5.554 1.00 76.64 N
ANISOU 61 N LEU A 43 10726 11295 7100 -965 1207 -1932 N
ATOM 62 CA LEU A 43 0.370 -13.490 5.375 1.00 72.86 C
ANISOU 62 CA LEU A 43 10555 10737 6392 -1132 1364 -1732 C
ATOM 63 C LEU A 43 1.218 -13.245 4.134 1.00 68.23 C
ANISOU 63 C LEU A 43 10117 9779 6027 -1198 1417 -1455 C
ATOM 64 O LEU A 43 2.428 -13.503 4.139 1.00 62.31 O
ANISOU 64 O LEU A 43 9444 8908 5323 -1206 1495 -1470 O
ATOM 65 CB LEU A 43 -0.332 -14.847 5.301 1.00 71.84 C
ANISOU 65 CB LEU A 43 10665 10919 5712 -1369 1433 -1566 C
ATOM 66 CG LEU A 43 -1.113 -15.249 6.555 1.00 75.27 C
ANISOU 66 CG LEU A 43 10977 11837 5784 -1462 1396 -1793 C
ATOM 67 CD1 LEU A 43 -1.783 -16.600 6.367 1.00 68.02 C
ANISOU 67 CD1 LEU A 43 10341 11129 4375 -1773 1388 -1519 C
ATOM 68 CD2 LEU A 43 -0.208 -15.261 7.780 1.00 67.05 C
ANISOU 68 CD2 LEU A 43 9902 10802 4774 -1371 1362 -2044 C
ATOM 69 N TRP A 44 0.600 -12.748 3.059 1.00 67.19 N
ANISOU 69 N TRP A 44 10006 9521 6001 -1267 1361 -1222 N
ATOM 70 CA TRP A 44 1.365 -12.357 1.878 1.00 64.80 C
ANISOU 70 CA TRP A 44 9818 8933 5871 -1418 1394 -943 C
ATOM 71 C TRP A 44 2.326 -11.218 2.194 1.00 65.74 C
ANISOU 71 C TRP A 44 9791 8765 6424 -1369 1289 -1060 C
ATOM 72 O TRP A 44 3.486 -11.237 1.765 1.00 64.49 O
ANISOU 72 O TRP A 44 9668 8538 6298 -1527 1404 -973 O
ATOM 73 CB TRP A 44 0.420 -11.952 0.747 1.00 63.67 C
ANISOU 73 CB TRP A 44 9750 8694 5747 -1523 1283 -653 C
ATOM 74 CG TRP A 44 0.198 -13.019 -0.280 1.00 62.34 C
ANISOU 74 CG TRP A 44 9814 8688 5184 -1733 1450 -369 C
ATOM 75 CD1 TRP A 44 -0.946 -13.732 -0.490 1.00 62.07 C
ANISOU 75 CD1 TRP A 44 9860 8883 4839 -1769 1457 -294 C
ATOM 76 CD2 TRP A 44 1.149 -13.494 -1.240 1.00 62.12 C
ANISOU 76 CD2 TRP A 44 9940 8654 5009 -1940 1621 -171 C
ATOM 77 NE1 TRP A 44 -0.768 -14.621 -1.523 1.00 60.73 N
ANISOU 77 NE1 TRP A 44 9930 8776 4368 -1969 1598 -42 N
ATOM 78 CE2 TRP A 44 0.511 -14.496 -1.999 1.00 61.12 C
ANISOU 78 CE2 TRP A 44 10011 8708 4506 -2054 1703 9 C
ATOM 79 CE3 TRP A 44 2.478 -13.171 -1.532 1.00 63.16 C
ANISOU 79 CE3 TRP A 44 10021 8715 5263 -2057 1712 -169 C
ATOM 80 CZ2 TRP A 44 1.156 -15.176 -3.030 1.00 61.58 C
ANISOU 80 CZ2 TRP A 44 10215 8861 4322 -2224 1858 151 C
ATOM 81 CZ3 TRP A 44 3.116 -13.846 -2.556 1.00 63.92 C
ANISOU 81 CZ3 TRP A 44 10213 8988 5085 -2252 1894 -41 C
ATOM 82 CH2 TRP A 44 2.455 -14.836 -3.294 1.00 63.17 C
ANISOU 82 CH2 TRP A 44 10315 9056 4631 -2307 1958 99 C
ATOM 83 N ARG A 45 1.859 -10.214 2.940 1.00 73.34 N
ANISOU 83 N ARG A 45 10563 9592 7709 -1156 1050 -1299 N
ATOM 84 CA ARG A 45 2.702 -9.063 3.248 1.00 75.10 C
ANISOU 84 CA ARG A 45 10686 9475 8372 -1126 877 -1409 C
ATOM 85 C ARG A 45 3.837 -9.443 4.191 1.00 74.84 C
ANISOU 85 C ARG A 45 10554 9569 8314 -1073 1039 -1663 C
ATOM 86 O ARG A 45 4.995 -9.072 3.965 1.00 75.08 O
ANISOU 86 O ARG A 45 10574 9446 8507 -1233 1074 -1607 O
ATOM 87 CB ARG A 45 1.857 -7.937 3.844 1.00 78.37 C
ANISOU 87 CB ARG A 45 10929 9697 9149 -833 508 -1686 C
ATOM 88 CG ARG A 45 1.318 -6.967 2.809 1.00 85.80 C
ANISOU 88 CG ARG A 45 12013 10221 10365 -901 162 -1420 C
ATOM 89 CD ARG A 45 0.463 -5.879 3.437 1.00 93.65 C
ANISOU 89 CD ARG A 45 12829 11005 11749 -501 -298 -1804 C
ATOM 90 NE ARG A 45 -0.867 -6.354 3.799 1.00 93.64 N
ANISOU 90 NE ARG A 45 12614 11456 11510 -228 -283 -2082 N
ATOM 91 CZ ARG A 45 -1.254 -6.634 5.036 1.00 89.25 C
ANISOU 91 CZ ARG A 45 11735 11360 10815 31 -194 -2576 C
ATOM 92 NH1 ARG A 45 -0.434 -6.492 6.065 1.00 85.20 N
ANISOU 92 NH1 ARG A 45 11098 10871 10405 108 -130 -2855 N
ATOM 93 NH2 ARG A 45 -2.495 -7.062 5.246 1.00 91.42 N
ANISOU 93 NH2 ARG A 45 11790 12141 10805 177 -172 -2801 N
ATOM 94 N GLU A 46 3.526 -10.183 5.257 1.00 75.77 N
ANISOU 94 N GLU A 46 10593 10000 8195 -889 1119 -1940 N
ATOM 95 CA GLU A 46 4.559 -10.555 6.215 1.00 76.40 C
ANISOU 95 CA GLU A 46 10607 10179 8244 -813 1207 -2187 C
ATOM 96 C GLU A 46 5.584 -11.506 5.613 1.00 78.21 C
ANISOU 96 C GLU A 46 10995 10476 8246 -964 1407 -2035 C
ATOM 97 O GLU A 46 6.711 -11.581 6.113 1.00 78.90 O
ANISOU 97 O GLU A 46 11000 10571 8406 -911 1443 -2225 O
ATOM 98 CB GLU A 46 3.930 -11.177 7.462 1.00 78.15 C
ANISOU 98 CB GLU A 46 10761 10746 8186 -661 1204 -2467 C
ATOM 99 CG GLU A 46 4.712 -10.892 8.730 1.00 81.30 C
ANISOU 99 CG GLU A 46 10993 11173 8724 -500 1149 -2826 C
ATOM 100 CD GLU A 46 4.923 -9.404 8.951 1.00 83.51 C
ANISOU 100 CD GLU A 46 11045 11158 9527 -360 953 -3026 C
ATOM 101 OE1 GLU A 46 3.924 -8.654 8.969 1.00 81.97 O
ANISOU 101 OE1 GLU A 46 10718 10930 9496 -228 769 -3142 O
ATOM 102 OE2 GLU A 46 6.091 -8.983 9.092 1.00 83.07 O
ANISOU 102 OE2 GLU A 46 10942 10898 9724 -377 940 -3093 O
ATOM 103 N TYR A 47 5.217 -12.237 4.560 1.00 71.50 N
ANISOU 103 N TYR A 47 10341 9704 7122 -1118 1514 -1751 N
ATOM 104 CA TYR A 47 6.183 -13.080 3.867 1.00 63.94 C
ANISOU 104 CA TYR A 47 9489 8843 5961 -1214 1668 -1685 C
ATOM 105 C TYR A 47 7.110 -12.255 2.982 1.00 66.54 C
ANISOU 105 C TYR A 47 9685 9087 6511 -1434 1732 -1569 C
ATOM 106 O TYR A 47 8.327 -12.469 2.976 1.00 65.52 O
ANISOU 106 O TYR A 47 9435 9090 6369 -1449 1827 -1737 O
ATOM 107 CB TYR A 47 5.457 -14.134 3.035 1.00 63.25 C
ANISOU 107 CB TYR A 47 9655 8882 5494 -1304 1733 -1459 C
ATOM 108 CG TYR A 47 6.391 -15.009 2.237 1.00 61.14 C
ANISOU 108 CG TYR A 47 9475 8743 5014 -1344 1849 -1469 C
ATOM 109 CD1 TYR A 47 7.018 -16.098 2.825 1.00 60.81 C
ANISOU 109 CD1 TYR A 47 9546 8781 4777 -1144 1788 -1725 C
ATOM 110 CD2 TYR A 47 6.649 -14.746 0.897 1.00 62.43 C
ANISOU 110 CD2 TYR A 47 9601 8970 5149 -1576 1975 -1259 C
ATOM 111 CE1 TYR A 47 7.871 -16.902 2.104 1.00 61.83 C
ANISOU 111 CE1 TYR A 47 9714 9048 4729 -1090 1833 -1847 C
ATOM 112 CE2 TYR A 47 7.503 -15.548 0.166 1.00 63.37 C
ANISOU 112 CE2 TYR A 47 9721 9320 5038 -1586 2086 -1367 C
ATOM 113 CZ TYR A 47 8.111 -16.625 0.776 1.00 63.11 C
ANISOU 113 CZ TYR A 47 9765 9362 4853 -1300 2006 -1700 C
ATOM 114 OH TYR A 47 8.964 -17.429 0.057 1.00 66.70 O
ANISOU 114 OH TYR A 47 10182 10063 5096 -1219 2055 -1917 O
ATOM 115 N LEU A 48 6.548 -11.318 2.215 1.00 68.03 N
ANISOU 115 N LEU A 48 9894 9083 6871 -1639 1649 -1285 N
ATOM 116 CA LEU A 48 7.361 -10.477 1.345 1.00 68.41 C
ANISOU 116 CA LEU A 48 9871 9053 7069 -1987 1663 -1091 C
ATOM 117 C LEU A 48 8.151 -9.438 2.127 1.00 70.40 C
ANISOU 117 C LEU A 48 9936 9112 7698 -1997 1529 -1280 C
ATOM 118 O LEU A 48 9.145 -8.915 1.611 1.00 73.10 O
ANISOU 118 O LEU A 48 10176 9498 8100 -2338 1575 -1191 O
ATOM 119 CB LEU A 48 6.475 -9.790 0.305 1.00 70.00 C
ANISOU 119 CB LEU A 48 10237 9033 7325 -2233 1516 -684 C
ATOM 120 CG LEU A 48 5.713 -10.724 -0.638 1.00 68.50 C
ANISOU 120 CG LEU A 48 10228 9039 6759 -2287 1644 -459 C
ATOM 121 CD1 LEU A 48 4.771 -9.939 -1.535 1.00 70.37 C
ANISOU 121 CD1 LEU A 48 10630 9016 7093 -2485 1427 -79 C
ATOM 122 CD2 LEU A 48 6.681 -11.551 -1.469 1.00 68.88 C
ANISOU 122 CD2 LEU A 48 10242 9466 6465 -2492 1921 -448 C
ATOM 123 N HIS A 49 7.736 -9.132 3.356 1.00 72.45 N
ANISOU 123 N HIS A 49 10133 9216 8179 -1671 1365 -1553 N
ATOM 124 CA HIS A 49 8.440 -8.202 4.236 1.00 71.76 C
ANISOU 124 CA HIS A 49 9871 8939 8456 -1623 1212 -1795 C
ATOM 125 C HIS A 49 8.649 -8.893 5.577 1.00 70.09 C
ANISOU 125 C HIS A 49 9541 8930 8160 -1259 1275 -2208 C
ATOM 126 O HIS A 49 7.962 -8.589 6.562 1.00 74.32 O
ANISOU 126 O HIS A 49 10024 9391 8825 -992 1115 -2434 O
ATOM 127 CB HIS A 49 7.665 -6.893 4.395 1.00 75.79 C
ANISOU 127 CB HIS A 49 10427 9000 9370 -1580 837 -1752 C
ATOM 128 CG HIS A 49 7.313 -6.237 3.096 1.00 84.85 C
ANISOU 128 CG HIS A 49 11780 9876 10582 -1936 671 -1301 C
ATOM 129 ND1 HIS A 49 8.205 -5.460 2.388 1.00 95.68 N
ANISOU 129 ND1 HIS A 49 13205 11075 12076 -2422 586 -1032 N
ATOM 130 CD2 HIS A 49 6.165 -6.240 2.378 1.00 85.54 C
ANISOU 130 CD2 HIS A 49 12047 9857 10600 -1922 547 -1056 C
ATOM 131 CE1 HIS A 49 7.622 -5.014 1.289 1.00101.20 C
ANISOU 131 CE1 HIS A 49 14147 11539 12764 -2710 395 -608 C
ATOM 132 NE2 HIS A 49 6.384 -5.474 1.259 1.00 95.55 N
ANISOU 132 NE2 HIS A 49 13507 10843 11954 -2376 364 -629 N
ATOM 133 N PRO A 50 9.589 -9.835 5.649 1.00 70.88 N
ANISOU 133 N PRO A 50 9593 9317 8021 -1235 1471 -2343 N
ATOM 134 CA PRO A 50 9.778 -10.598 6.892 1.00 74.55 C
ANISOU 134 CA PRO A 50 10029 9939 8359 -914 1462 -2687 C
ATOM 135 C PRO A 50 10.399 -9.735 7.982 1.00 79.67 C
ANISOU 135 C PRO A 50 10461 10472 9338 -802 1330 -2994 C
ATOM 136 O PRO A 50 11.411 -9.064 7.763 1.00 81.09 O
ANISOU 136 O PRO A 50 10475 10596 9739 -978 1335 -3031 O
ATOM 137 CB PRO A 50 10.717 -11.739 6.473 1.00 69.92 C
ANISOU 137 CB PRO A 50 9467 9619 7482 -899 1613 -2763 C
ATOM 138 CG PRO A 50 10.773 -11.693 4.964 1.00 68.53 C
ANISOU 138 CG PRO A 50 9317 9518 7205 -1207 1758 -2461 C
ATOM 139 CD PRO A 50 10.508 -10.275 4.589 1.00 70.79 C
ANISOU 139 CD PRO A 50 9543 9539 7816 -1487 1669 -2228 C
ATOM 140 N LYS A 51 9.783 -9.759 9.161 1.00 81.52 N
ANISOU 140 N LYS A 51 10681 10726 9567 -549 1211 -3225 N
ATOM 141 CA LYS A 51 10.303 -9.053 10.323 1.00 86.54 C
ANISOU 141 CA LYS A 51 11113 11297 10471 -396 1075 -3573 C
ATOM 142 C LYS A 51 11.108 -10.012 11.191 1.00 92.01 C
ANISOU 142 C LYS A 51 11800 12226 10935 -228 1112 -3826 C
ATOM 143 O LYS A 51 10.782 -11.198 11.300 1.00 92.04 O
ANISOU 143 O LYS A 51 12010 12409 10553 -160 1145 -3775 O
ATOM 144 CB LYS A 51 9.168 -8.420 11.130 1.00 85.68 C
ANISOU 144 CB LYS A 51 10934 11146 10476 -211 896 -3754 C
ATOM 145 CG LYS A 51 8.508 -7.238 10.430 1.00 82.14 C
ANISOU 145 CG LYS A 51 10476 10358 10377 -282 713 -3612 C
ATOM 146 CD LYS A 51 7.336 -6.691 11.227 1.00 77.10 C
ANISOU 146 CD LYS A 51 9702 9765 9828 -3 503 -3916 C
ATOM 147 CE LYS A 51 6.699 -5.504 10.521 1.00 80.46 C
ANISOU 147 CE LYS A 51 10153 9771 10647 4 202 -3823 C
ATOM 148 NZ LYS A 51 5.490 -5.008 11.234 1.00 79.31 N
ANISOU 148 NZ LYS A 51 9812 9744 10578 358 -36 -4223 N
ATOM 149 N GLU A 52 12.171 -9.493 11.802 1.00 97.26 N
ANISOU 149 N GLU A 52 12257 12858 11841 -175 1053 -4093 N
ATOM 150 CA GLU A 52 13.141 -10.375 12.438 1.00 96.63 C
ANISOU 150 CA GLU A 52 12163 12973 11577 -9 1046 -4335 C
ATOM 151 C GLU A 52 12.734 -10.758 13.857 1.00 93.88 C
ANISOU 151 C GLU A 52 11883 12738 11049 209 900 -4567 C
ATOM 152 O GLU A 52 12.984 -11.889 14.290 1.00 91.74 O
ANISOU 152 O GLU A 52 11800 12603 10452 326 826 -4626 O
ATOM 153 CB GLU A 52 14.523 -9.717 12.444 1.00100.58 C
ANISOU 153 CB GLU A 52 12375 13470 12371 -74 1052 -4541 C
ATOM 154 CG GLU A 52 15.148 -9.556 11.062 1.00106.61 C
ANISOU 154 CG GLU A 52 13040 14299 13170 -377 1219 -4341 C
ATOM 155 CD GLU A 52 14.613 -8.348 10.305 1.00111.27 C
ANISOU 155 CD GLU A 52 13636 14616 14026 -714 1203 -4033 C
ATOM 156 OE1 GLU A 52 13.819 -7.582 10.891 1.00108.89 O
ANISOU 156 OE1 GLU A 52 13383 14041 13948 -630 1027 -4051 O
ATOM 157 OE2 GLU A 52 14.989 -8.161 9.127 1.00117.58 O
ANISOU 157 OE2 GLU A 52 14392 15489 14795 -1063 1328 -3795 O
ATOM 158 N TYR A 53 12.107 -9.843 14.591 1.00 88.74 N
ANISOU 158 N TYR A 53 11092 12044 10581 255 811 -4717 N
ATOM 159 CA TYR A 53 11.911 -9.998 16.030 1.00 83.13 C
ANISOU 159 CA TYR A 53 10345 11535 9706 417 682 -5014 C
ATOM 160 C TYR A 53 10.458 -9.746 16.418 1.00 82.84 C
ANISOU 160 C TYR A 53 10283 11673 9518 415 656 -5042 C
ATOM 161 O TYR A 53 10.152 -8.970 17.325 1.00 82.11 O
ANISOU 161 O TYR A 53 9961 11678 9558 538 548 -5364 O
ATOM 162 CB TYR A 53 12.856 -9.075 16.787 1.00 83.33 C
ANISOU 162 CB TYR A 53 10096 11468 10097 528 575 -5364 C
ATOM 163 CG TYR A 53 14.284 -9.563 16.804 1.00 82.96 C
ANISOU 163 CG TYR A 53 10022 11434 10066 574 570 -5463 C
ATOM 164 CD1 TYR A 53 14.666 -10.607 17.634 1.00 80.43 C
ANISOU 164 CD1 TYR A 53 9856 11259 9444 696 434 -5385 C
ATOM 165 CD2 TYR A 53 15.250 -8.984 15.991 1.00 84.76 C
ANISOU 165 CD2 TYR A 53 10067 11525 10612 444 645 -5438 C
ATOM 166 CE1 TYR A 53 15.971 -11.063 17.659 1.00 82.13 C
ANISOU 166 CE1 TYR A 53 10020 11485 9703 801 362 -5471 C
ATOM 167 CE2 TYR A 53 16.560 -9.432 16.008 1.00 85.41 C
ANISOU 167 CE2 TYR A 53 10033 11737 10683 507 643 -5618 C
ATOM 168 CZ TYR A 53 16.914 -10.471 16.844 1.00 83.94 C
ANISOU 168 CZ TYR A 53 9979 11686 10228 736 484 -5648 C
ATOM 169 OH TYR A 53 18.217 -10.917 16.861 1.00 80.52 O
ANISOU 169 OH TYR A 53 9406 11372 9818 855 413 -5794 O
ATOM 170 N GLU A 54 9.531 -10.389 15.707 1.00 90.52 N
ANISOU 170 N GLU A 54 10280 11872 12240 496 597 -2163 N
ATOM 171 CA GLU A 54 8.137 -10.355 16.135 1.00 87.43 C
ANISOU 171 CA GLU A 54 10032 11377 11811 391 376 -2089 C
ATOM 172 C GLU A 54 7.928 -11.147 17.419 1.00 80.96 C
ANISOU 172 C GLU A 54 9116 10537 11109 420 193 -2020 C
ATOM 173 O GLU A 54 7.087 -10.774 18.247 1.00 80.58 O
ANISOU 173 O GLU A 54 9051 10485 11081 276 69 -1953 O
ATOM 174 CB GLU A 54 7.227 -10.899 15.034 1.00 88.77 C
ANISOU 174 CB GLU A 54 10514 11364 11850 450 317 -2160 C
ATOM 175 CG GLU A 54 7.218 -10.074 13.766 1.00 90.60 C
ANISOU 175 CG GLU A 54 10964 11574 11886 467 465 -2215 C
ATOM 176 CD GLU A 54 6.341 -10.683 12.694 1.00 93.67 C
ANISOU 176 CD GLU A 54 11657 11806 12127 581 349 -2327 C
ATOM 177 OE1 GLU A 54 5.956 -11.863 12.837 1.00 95.98 O
ANISOU 177 OE1 GLU A 54 11960 12002 12507 625 215 -2383 O
ATOM 178 OE2 GLU A 54 6.032 -9.979 11.711 1.00 96.35 O
ANISOU 178 OE2 GLU A 54 12258 12107 12246 639 395 -2374 O
ATOM 179 N TRP A 55 8.677 -12.240 17.598 1.00 76.50 N
ANISOU 179 N TRP A 55 8530 9939 10598 628 190 -2038 N
ATOM 180 CA TRP A 55 8.456 -13.113 18.746 1.00 73.28 C
ANISOU 180 CA TRP A 55 8171 9435 10238 707 42 -1960 C
ATOM 181 C TRP A 55 8.780 -12.408 20.057 1.00 70.52 C
ANISOU 181 C TRP A 55 7592 9264 9938 665 -39 -1888 C
ATOM 182 O TRP A 55 8.073 -12.592 21.054 1.00 67.35 O
ANISOU 182 O TRP A 55 7288 8771 9530 600 -148 -1793 O
ATOM 183 CB TRP A 55 9.277 -14.396 18.602 1.00 76.79 C
ANISOU 183 CB TRP A 55 8701 9789 10684 1010 54 -2000 C
ATOM 184 CG TRP A 55 10.761 -14.200 18.715 1.00 78.91 C
ANISOU 184 CG TRP A 55 8670 10305 11009 1222 105 -2081 C
ATOM 185 CD1 TRP A 55 11.638 -13.958 17.697 1.00 81.23 C
ANISOU 185 CD1 TRP A 55 8816 10725 11324 1282 287 -2216 C
ATOM 186 CD2 TRP A 55 11.543 -14.238 19.916 1.00 78.51 C
ANISOU 186 CD2 TRP A 55 8412 10419 11001 1412 -24 -2078 C
ATOM 187 NE1 TRP A 55 12.915 -13.839 18.190 1.00 78.14 N
ANISOU 187 NE1 TRP A 55 8074 10587 11027 1466 293 -2331 N
ATOM 188 CE2 TRP A 55 12.884 -14.006 19.550 1.00 79.20 C
ANISOU 188 CE2 TRP A 55 8160 10763 11169 1573 70 -2257 C
ATOM 189 CE3 TRP A 55 11.237 -14.441 21.266 1.00 74.06 C
ANISOU 189 CE3 TRP A 55 7928 9810 10400 1474 -205 -1964 C
ATOM 190 CZ2 TRP A 55 13.917 -13.974 20.483 1.00 81.05 C
ANISOU 190 CZ2 TRP A 55 8080 11250 11467 1813 -61 -2364 C
ATOM 191 CZ3 TRP A 55 12.264 -14.408 22.190 1.00 74.73 C
ANISOU 191 CZ3 TRP A 55 7776 10116 10501 1742 -342 -2029 C
ATOM 192 CH2 TRP A 55 13.588 -14.177 21.795 1.00 79.22 C
ANISOU 192 CH2 TRP A 55 7954 10977 11169 1918 -295 -2245 C
ATOM 193 N VAL A 56 9.843 -11.601 20.082 1.00 77.31 N
ANISOU 193 N VAL A 56 8151 10374 10848 688 35 -1958 N
ATOM 194 CA VAL A 56 10.175 -10.884 21.308 1.00 74.36 C
ANISOU 194 CA VAL A 56 7539 10192 10523 646 -60 -1934 C
ATOM 195 C VAL A 56 9.099 -9.854 21.627 1.00 69.61 C
ANISOU 195 C VAL A 56 6986 9569 9893 351 -79 -1846 C
ATOM 196 O VAL A 56 8.760 -9.637 22.795 1.00 67.06 O
ANISOU 196 O VAL A 56 6637 9274 9569 305 -206 -1767 O
ATOM 197 CB VAL A 56 11.576 -10.245 21.213 1.00 74.72 C
ANISOU 197 CB VAL A 56 7199 10525 10667 697 47 -2106 C
ATOM 198 CG1 VAL A 56 11.624 -9.178 20.136 1.00 74.47 C
ANISOU 198 CG1 VAL A 56 7131 10528 10638 448 310 -2174 C
ATOM 199 CG2 VAL A 56 11.986 -9.664 22.561 1.00 72.03 C
ANISOU 199 CG2 VAL A 56 6593 10396 10377 702 -103 -2131 C
ATOM 200 N LEU A 57 8.526 -9.223 20.598 1.00 67.64 N
ANISOU 200 N LEU A 57 6845 9262 9594 184 39 -1865 N
ATOM 201 CA LEU A 57 7.429 -8.288 20.826 1.00 65.68 C
ANISOU 201 CA LEU A 57 6668 8987 9299 -36 -5 -1804 C
ATOM 202 C LEU A 57 6.210 -9.003 21.394 1.00 62.34 C
ANISOU 202 C LEU A 57 6414 8400 8871 -71 -153 -1740 C
ATOM 203 O LEU A 57 5.571 -8.509 22.331 1.00 59.56 O
ANISOU 203 O LEU A 57 6028 8072 8529 -201 -230 -1679 O
ATOM 204 CB LEU A 57 7.071 -7.568 19.525 1.00 69.46 C
ANISOU 204 CB LEU A 57 7303 9416 9672 -113 125 -1855 C
ATOM 205 CG LEU A 57 6.072 -6.415 19.643 1.00 67.84 C
ANISOU 205 CG LEU A 57 7181 9208 9389 -277 81 -1821 C
ATOM 206 CD1 LEU A 57 6.666 -5.276 20.457 1.00 63.11 C
ANISOU 206 CD1 LEU A 57 6384 8760 8835 -412 153 -1793 C
ATOM 207 CD2 LEU A 57 5.638 -5.925 18.270 1.00 70.01 C
ANISOU 207 CD2 LEU A 57 7721 9386 9492 -245 163 -1879 C
ATOM 208 N ILE A 58 5.878 -10.173 20.844 1.00 65.37 N
ANISOU 208 N ILE A 58 6985 8605 9247 21 -163 -1777 N
ATOM 209 CA ILE A 58 4.735 -10.934 21.345 1.00 62.87 C
ANISOU 209 CA ILE A 58 6833 8101 8954 -66 -234 -1766 C
ATOM 210 C ILE A 58 4.965 -11.343 22.794 1.00 62.07 C
ANISOU 210 C ILE A 58 6744 7969 8872 -21 -275 -1649 C
ATOM 211 O ILE A 58 4.077 -11.211 23.646 1.00 58.82 O
ANISOU 211 O ILE A 58 6381 7495 8474 -180 -297 -1607 O
ATOM 212 CB ILE A 58 4.469 -12.157 20.449 1.00 61.45 C
ANISOU 212 CB ILE A 58 6862 7715 8771 12 -204 -1861 C
ATOM 213 CG1 ILE A 58 4.064 -11.712 19.044 1.00 61.50 C
ANISOU 213 CG1 ILE A 58 6907 7748 8713 -8 -200 -1994 C
ATOM 214 CG2 ILE A 58 3.395 -13.044 21.059 1.00 59.93 C
ANISOU 214 CG2 ILE A 58 6840 7297 8633 -122 -209 -1884 C
ATOM 215 CD1 ILE A 58 3.775 -12.860 18.106 1.00 59.60 C
ANISOU 215 CD1 ILE A 58 6865 7320 8462 66 -190 -2124 C
ATOM 216 N ALA A 59 6.166 -11.844 23.095 1.00 61.67 N
ANISOU 216 N ALA A 59 6661 7964 8806 225 -287 -1615 N
ATOM 217 CA ALA A 59 6.475 -12.270 24.456 1.00 60.86 C
ANISOU 217 CA ALA A 59 6636 7827 8661 363 -363 -1513 C
ATOM 218 C ALA A 59 6.423 -11.098 25.427 1.00 58.80 C
ANISOU 218 C ALA A 59 6182 7760 8397 240 -432 -1464 C
ATOM 219 O ALA A 59 5.868 -11.218 26.526 1.00 60.05 O
ANISOU 219 O ALA A 59 6490 7822 8506 193 -463 -1370 O
ATOM 220 CB ALA A 59 7.848 -12.940 24.496 1.00 61.14 C
ANISOU 220 CB ALA A 59 6635 7932 8666 728 -415 -1541 C
ATOM 221 N GLY A 60 6.992 -9.955 25.038 1.00 60.73 N
ANISOU 221 N GLY A 60 6133 8255 8689 172 -422 -1533 N
ATOM 222 CA GLY A 60 6.950 -8.789 25.900 1.00 60.39 C
ANISOU 222 CA GLY A 60 5915 8383 8647 36 -473 -1508 C
ATOM 223 C GLY A 60 5.537 -8.299 26.144 1.00 58.55 C
ANISOU 223 C GLY A 60 5797 8047 8402 -221 -457 -1450 C
ATOM 224 O GLY A 60 5.181 -7.945 27.269 1.00 56.35 O
ANISOU 224 O GLY A 60 5531 7788 8093 -286 -512 -1381 O
ATOM 225 N TYR A 61 4.709 -8.280 25.096 1.00 56.45 N
ANISOU 225 N TYR A 61 5610 7684 8153 -344 -392 -1505 N
ATOM 226 CA TYR A 61 3.326 -7.851 25.268 1.00 56.21 C
ANISOU 226 CA TYR A 61 5637 7590 8129 -554 -399 -1517 C
ATOM 227 C TYR A 61 2.552 -8.815 26.159 1.00 56.93 C
ANISOU 227 C TYR A 61 5910 7486 8235 -607 -381 -1475 C
ATOM 228 O TYR A 61 1.740 -8.382 26.982 1.00 54.97 O
ANISOU 228 O TYR A 61 5660 7234 7993 -763 -375 -1455 O
ATOM 229 CB TYR A 61 2.645 -7.695 23.910 1.00 56.55 C
ANISOU 229 CB TYR A 61 5723 7595 8168 -603 -382 -1640 C
ATOM 230 CG TYR A 61 2.633 -6.267 23.410 1.00 56.77 C
ANISOU 230 CG TYR A 61 5672 7763 8134 -654 -379 -1666 C
ATOM 231 CD1 TYR A 61 1.592 -5.405 23.738 1.00 57.50 C
ANISOU 231 CD1 TYR A 61 5745 7893 8209 -777 -437 -1694 C
ATOM 232 CD2 TYR A 61 3.665 -5.776 22.621 1.00 58.34 C
ANISOU 232 CD2 TYR A 61 5847 8036 8285 -578 -287 -1674 C
ATOM 233 CE1 TYR A 61 1.578 -4.096 23.289 1.00 57.94 C
ANISOU 233 CE1 TYR A 61 5812 8032 8171 -787 -424 -1707 C
ATOM 234 CE2 TYR A 61 3.658 -4.469 22.167 1.00 60.27 C
ANISOU 234 CE2 TYR A 61 6116 8343 8442 -636 -225 -1689 C
ATOM 235 CZ TYR A 61 2.613 -3.634 22.503 1.00 59.35 C
ANISOU 235 CZ TYR A 61 6033 8237 8279 -723 -305 -1694 C
ATOM 236 OH TYR A 61 2.605 -2.335 22.052 1.00 60.11 O
ANISOU 236 OH TYR A 61 6233 8353 8254 -744 -235 -1700 O
ATOM 237 N ILE A 62 2.791 -10.121 26.020 1.00 56.73 N
ANISOU 237 N ILE A 62 6078 7273 8206 -485 -335 -1468 N
ATOM 238 CA ILE A 62 2.102 -11.094 26.869 1.00 55.84 C
ANISOU 238 CA ILE A 62 6228 6903 8084 -554 -243 -1427 C
ATOM 239 C ILE A 62 2.517 -10.920 28.326 1.00 52.88 C
ANISOU 239 C ILE A 62 5935 6548 7607 -463 -274 -1275 C
ATOM 240 O ILE A 62 1.676 -10.911 29.238 1.00 52.36 O
ANISOU 240 O ILE A 62 6004 6368 7525 -627 -186 -1237 O
ATOM 241 CB ILE A 62 2.373 -12.526 26.372 1.00 55.02 C
ANISOU 241 CB ILE A 62 6382 6553 7971 -418 -168 -1447 C
ATOM 242 CG1 ILE A 62 1.674 -12.762 25.031 1.00 53.99 C
ANISOU 242 CG1 ILE A 62 6206 6372 7936 -551 -135 -1635 C
ATOM 243 CG2 ILE A 62 1.922 -13.549 27.408 1.00 51.21 C
ANISOU 243 CG2 ILE A 62 6275 5751 7431 -452 -21 -1369 C
ATOM 244 CD1 ILE A 62 1.955 -14.120 24.428 1.00 55.39 C
ANISOU 244 CD1 ILE A 62 6633 6307 8108 -428 -58 -1679 C
ATOM 245 N ILE A 63 3.824 -10.777 28.566 1.00 52.75 N
ANISOU 245 N ILE A 63 5834 6691 7519 -190 -399 -1218 N
ATOM 246 CA ILE A 63 4.317 -10.584 29.926 1.00 54.31 C
ANISOU 246 CA ILE A 63 6098 6947 7591 -38 -490 -1114 C
ATOM 247 C ILE A 63 3.739 -9.308 30.522 1.00 59.02 C
ANISOU 247 C ILE A 63 6515 7701 8207 -268 -508 -1108 C
ATOM 248 O ILE A 63 3.285 -9.294 31.673 1.00 56.13 O
ANISOU 248 O ILE A 63 6332 7247 7746 -305 -481 -1022 O
ATOM 249 CB ILE A 63 5.858 -10.566 29.938 1.00 53.55 C
ANISOU 249 CB ILE A 63 5829 7068 7450 305 -659 -1149 C
ATOM 250 CG1 ILE A 63 6.416 -11.937 29.550 1.00 53.23 C
ANISOU 250 CG1 ILE A 63 6029 6844 7353 601 -651 -1146 C
ATOM 251 CG2 ILE A 63 6.380 -10.144 31.300 1.00 50.80 C
ANISOU 251 CG2 ILE A 63 5474 6856 6971 476 -815 -1103 C
ATOM 252 CD1 ILE A 63 7.926 -11.973 29.448 1.00 52.79 C
ANISOU 252 CD1 ILE A 63 5740 7036 7283 966 -821 -1244 C
ATOM 253 N VAL A 64 3.739 -8.221 29.746 1.00 55.24 N
ANISOU 253 N VAL A 64 5728 7431 7828 -412 -532 -1196 N
ATOM 254 CA VAL A 64 3.207 -6.952 30.231 1.00 53.60 C
ANISOU 254 CA VAL A 64 5374 7362 7631 -608 -548 -1198 C
ATOM 255 C VAL A 64 1.723 -7.077 30.541 1.00 54.10 C
ANISOU 255 C VAL A 64 5578 7257 7719 -836 -434 -1200 C
ATOM 256 O VAL A 64 1.252 -6.593 31.573 1.00 55.41 O
ANISOU 256 O VAL A 64 5781 7434 7838 -928 -420 -1151 O
ATOM 257 CB VAL A 64 3.483 -5.832 29.210 1.00 53.21 C
ANISOU 257 CB VAL A 64 5067 7500 7650 -695 -554 -1292 C
ATOM 258 CG1 VAL A 64 2.558 -4.657 29.451 1.00 49.18 C
ANISOU 258 CG1 VAL A 64 4495 7048 7144 -904 -541 -1306 C
ATOM 259 CG2 VAL A 64 4.935 -5.386 29.295 1.00 53.17 C
ANISOU 259 CG2 VAL A 64 4854 7703 7645 -556 -619 -1333 C
ATOM 260 N PHE A 65 0.964 -7.731 29.659 1.00 53.97 N
ANISOU 260 N PHE A 65 5624 7095 7788 -934 -345 -1291 N
ATOM 261 CA PHE A 65 -0.463 -7.924 29.896 1.00 55.43 C
ANISOU 261 CA PHE A 65 5874 7144 8043 -1175 -217 -1376 C
ATOM 262 C PHE A 65 -0.702 -8.652 31.212 1.00 56.90 C
ANISOU 262 C PHE A 65 6352 7116 8151 -1206 -75 -1269 C
ATOM 263 O PHE A 65 -1.458 -8.178 32.072 1.00 57.29 O
ANISOU 263 O PHE A 65 6409 7163 8195 -1369 7 -1269 O
ATOM 264 CB PHE A 65 -1.074 -8.698 28.724 1.00 53.33 C
ANISOU 264 CB PHE A 65 5619 6757 7886 -1248 -160 -1545 C
ATOM 265 CG PHE A 65 -2.517 -9.080 28.922 1.00 51.36 C
ANISOU 265 CG PHE A 65 5388 6371 7754 -1518 -6 -1716 C
ATOM 266 CD1 PHE A 65 -3.532 -8.220 28.541 1.00 52.37 C
ANISOU 266 CD1 PHE A 65 5263 6662 7973 -1654 -66 -1910 C
ATOM 267 CD2 PHE A 65 -2.856 -10.309 29.465 1.00 51.02 C
ANISOU 267 CD2 PHE A 65 5624 6029 7732 -1627 216 -1715 C
ATOM 268 CE1 PHE A 65 -4.859 -8.569 28.715 1.00 54.16 C
ANISOU 268 CE1 PHE A 65 5424 6807 8346 -1908 77 -2142 C
ATOM 269 CE2 PHE A 65 -4.180 -10.664 29.641 1.00 50.50 C
ANISOU 269 CE2 PHE A 65 5540 5837 7813 -1934 418 -1929 C
ATOM 270 CZ PHE A 65 -5.183 -9.793 29.265 1.00 50.25 C
ANISOU 270 CZ PHE A 65 5163 6021 7909 -2081 340 -2164 C
ATOM 271 N VAL A 66 -0.042 -9.799 31.396 1.00 53.75 N
ANISOU 271 N VAL A 66 6240 6517 7664 -1024 -30 -1176 N
ATOM 272 CA VAL A 66 -0.277 -10.608 32.591 1.00 53.99 C
ANISOU 272 CA VAL A 66 6683 6266 7564 -1018 146 -1061 C
ATOM 273 C VAL A 66 0.141 -9.846 33.844 1.00 55.67 C
ANISOU 273 C VAL A 66 6931 6608 7613 -898 46 -926 C
ATOM 274 O VAL A 66 -0.605 -9.781 34.832 1.00 56.94 O
ANISOU 274 O VAL A 66 7286 6638 7710 -1049 212 -886 O
ATOM 275 CB VAL A 66 0.456 -11.957 32.479 1.00 60.00 C
ANISOU 275 CB VAL A 66 7808 6773 8215 -763 185 -981 C
ATOM 276 CG1 VAL A 66 0.304 -12.752 33.766 1.00 62.23 C
ANISOU 276 CG1 VAL A 66 8636 6720 8290 -695 377 -833 C
ATOM 277 CG2 VAL A 66 -0.073 -12.749 31.294 1.00 54.09 C
ANISOU 277 CG2 VAL A 66 7056 5865 7630 -920 311 -1137 C
ATOM 278 N VAL A 67 1.338 -9.251 33.819 1.00 59.19 N
ANISOU 278 N VAL A 67 7180 7316 7995 -639 -211 -887 N
ATOM 279 CA VAL A 67 1.855 -8.567 35.000 1.00 56.49 C
ANISOU 279 CA VAL A 67 6855 7117 7491 -493 -348 -803 C
ATOM 280 C VAL A 67 0.993 -7.360 35.344 1.00 57.82 C
ANISOU 280 C VAL A 67 6818 7421 7730 -776 -306 -845 C
ATOM 281 O VAL A 67 0.659 -7.137 36.511 1.00 59.76 O
ANISOU 281 O VAL A 67 7254 7611 7842 -797 -253 -772 O
ATOM 282 CB VAL A 67 3.329 -8.172 34.790 1.00 52.64 C
ANISOU 282 CB VAL A 67 6108 6915 6976 -196 -622 -840 C
ATOM 283 CG1 VAL A 67 3.790 -7.227 35.888 1.00 51.50 C
ANISOU 283 CG1 VAL A 67 5870 6984 6713 -105 -789 -831 C
ATOM 284 CG2 VAL A 67 4.206 -9.413 34.758 1.00 49.90 C
ANISOU 284 CG2 VAL A 67 6016 6436 6509 172 -688 -801 C
ATOM 285 N ALA A 68 0.619 -6.562 34.340 1.00 57.62 N
ANISOU 285 N ALA A 68 6444 7562 7886 -964 -328 -967 N
ATOM 286 CA ALA A 68 -0.211 -5.390 34.587 1.00 58.64 C
ANISOU 286 CA ALA A 68 6393 7816 8070 -1183 -305 -1023 C
ATOM 287 C ALA A 68 -1.557 -5.787 35.168 1.00 59.01 C
ANISOU 287 C ALA A 68 6620 7660 8142 -1409 -68 -1050 C
ATOM 288 O ALA A 68 -2.009 -5.210 36.164 1.00 62.26 O
ANISOU 288 O ALA A 68 7082 8091 8484 -1493 -12 -1020 O
ATOM 289 CB ALA A 68 -0.401 -4.601 33.291 1.00 58.24 C
ANISOU 289 CB ALA A 68 6038 7928 8164 -1277 -367 -1152 C
ATOM 290 N LEU A 69 -2.213 -6.782 34.563 1.00 57.33 N
ANISOU 290 N LEU A 69 6499 7247 8037 -1530 100 -1138 N
ATOM 291 CA LEU A 69 -3.517 -7.203 35.059 1.00 58.08 C
ANISOU 291 CA LEU A 69 6720 7147 8203 -1804 385 -1232 C
ATOM 292 C LEU A 69 -3.419 -7.676 36.503 1.00 57.38 C
ANISOU 292 C LEU A 69 7061 6835 7907 -1762 559 -1061 C
ATOM 293 O LEU A 69 -4.149 -7.191 37.380 1.00 58.69 O
ANISOU 293 O LEU A 69 7262 6991 8046 -1922 706 -1076 O
ATOM 294 CB LEU A 69 -4.086 -8.300 34.160 1.00 52.49 C
ANISOU 294 CB LEU A 69 6047 6244 7651 -1946 544 -1391 C
ATOM 295 CG LEU A 69 -5.595 -8.529 34.233 1.00 53.03 C
ANISOU 295 CG LEU A 69 6035 6206 7907 -2308 824 -1639 C
ATOM 296 CD1 LEU A 69 -6.343 -7.245 33.911 1.00 52.57 C
ANISOU 296 CD1 LEU A 69 5542 6459 7974 -2394 682 -1826 C
ATOM 297 CD2 LEU A 69 -6.004 -9.641 33.282 1.00 54.39 C
ANISOU 297 CD2 LEU A 69 6225 6198 8241 -2441 953 -1835 C
ATOM 298 N ILE A 70 -2.484 -8.592 36.779 1.00 55.89 N
ANISOU 298 N ILE A 70 7231 6467 7538 -1502 534 -899 N
ATOM 299 CA ILE A 70 -2.360 -9.145 38.125 1.00 58.83 C
ANISOU 299 CA ILE A 70 8131 6580 7644 -1386 693 -727 C
ATOM 300 C ILE A 70 -2.026 -8.046 39.126 1.00 59.69 C
ANISOU 300 C ILE A 70 8182 6906 7591 -1266 520 -642 C
ATOM 301 O ILE A 70 -2.653 -7.940 40.185 1.00 59.44 O
ANISOU 301 O ILE A 70 8413 6734 7436 -1377 730 -594 O
ATOM 302 CB ILE A 70 -1.310 -10.271 38.150 1.00 59.81 C
ANISOU 302 CB ILE A 70 8658 6500 7568 -1023 622 -584 C
ATOM 303 CG1 ILE A 70 -1.790 -11.469 37.329 1.00 55.61 C
ANISOU 303 CG1 ILE A 70 8294 5665 7171 -1185 874 -668 C
ATOM 304 CG2 ILE A 70 -1.011 -10.694 39.580 1.00 57.32 C
ANISOU 304 CG2 ILE A 70 8943 5944 6892 -779 703 -392 C
ATOM 305 CD1 ILE A 70 -0.829 -12.636 37.340 1.00 58.24 C
ANISOU 305 CD1 ILE A 70 9081 5752 7294 -809 831 -531 C
ATOM 306 N GLY A 71 -1.049 -7.198 38.796 1.00 64.60 N
ANISOU 306 N GLY A 71 8461 7863 8219 -1063 164 -647 N
ATOM 307 CA GLY A 71 -0.603 -6.190 39.742 1.00 65.61 C
ANISOU 307 CA GLY A 71 8537 8198 8194 -937 -22 -598 C
ATOM 308 C GLY A 71 -1.651 -5.138 40.041 1.00 64.07 C
ANISOU 308 C GLY A 71 8143 8102 8100 -1240 96 -676 C
ATOM 309 O GLY A 71 -1.841 -4.756 41.197 1.00 70.29 O
ANISOU 309 O GLY A 71 9132 8863 8711 -1223 143 -612 O
ATOM 310 N ASN A 72 -2.346 -4.648 39.012 1.00 59.13 N
ANISOU 310 N ASN A 72 7142 7592 7733 -1480 130 -827 N
ATOM 311 CA ASN A 72 -3.352 -3.620 39.250 1.00 59.27 C
ANISOU 311 CA ASN A 72 6957 7722 7842 -1711 213 -930 C
ATOM 312 C ASN A 72 -4.568 -4.191 39.971 1.00 60.98 C
ANISOU 312 C ASN A 72 7417 7692 8062 -1945 581 -968 C
ATOM 313 O ASN A 72 -5.143 -3.531 40.850 1.00 61.83 O
ANISOU 313 O ASN A 72 7555 7829 8110 -2044 684 -979 O
ATOM 314 CB ASN A 72 -3.741 -2.962 37.929 1.00 60.57 C
ANISOU 314 CB ASN A 72 6705 8073 8237 -1822 115 -1100 C
ATOM 315 CG ASN A 72 -2.596 -2.170 37.318 1.00 61.04 C
ANISOU 315 CG ASN A 72 6556 8357 8281 -1648 -166 -1074 C
ATOM 316 OD1 ASN A 72 -1.951 -1.370 37.995 1.00 59.27 O
ANISOU 316 OD1 ASN A 72 6316 8263 7940 -1559 -297 -1016 O
ATOM 317 ND2 ASN A 72 -2.330 -2.403 36.038 1.00 61.66 N
ANISOU 317 ND2 ASN A 72 6482 8470 8475 -1616 -235 -1139 N
ATOM 318 N VAL A 73 -4.965 -5.425 39.637 1.00 62.34 N
ANISOU 318 N VAL A 73 7781 7602 8305 -2053 819 -1005 N
ATOM 319 CA VAL A 73 -6.043 -6.065 40.386 1.00 60.95 C
ANISOU 319 CA VAL A 73 7888 7140 8130 -2316 1251 -1060 C
ATOM 320 C VAL A 73 -5.637 -6.248 41.843 1.00 62.50 C
ANISOU 320 C VAL A 73 8617 7144 7985 -2157 1359 -835 C
ATOM 321 O VAL A 73 -6.442 -6.034 42.756 1.00 63.88 O
ANISOU 321 O VAL A 73 8951 7216 8105 -2341 1645 -861 O
ATOM 322 CB VAL A 73 -6.439 -7.398 39.725 1.00 57.95 C
ANISOU 322 CB VAL A 73 7651 6479 7889 -2479 1510 -1161 C
ATOM 323 CG1 VAL A 73 -7.325 -8.213 40.651 1.00 57.27 C
ANISOU 323 CG1 VAL A 73 7995 6011 7753 -2751 2033 -1188 C
ATOM 324 CG2 VAL A 73 -7.157 -7.136 38.411 1.00 58.39 C
ANISOU 324 CG2 VAL A 73 7169 6736 8279 -2672 1435 -1456 C
ATOM 325 N LEU A 74 -4.380 -6.630 42.086 1.00 62.70 N
ANISOU 325 N LEU A 74 8929 7132 7762 -1783 1123 -635 N
ATOM 326 CA LEU A 74 -3.903 -6.781 43.457 1.00 62.72 C
ANISOU 326 CA LEU A 74 9470 6977 7385 -1534 1144 -437 C
ATOM 327 C LEU A 74 -3.884 -5.447 44.192 1.00 64.75 C
ANISOU 327 C LEU A 74 9535 7507 7561 -1504 969 -442 C
ATOM 328 O LEU A 74 -4.189 -5.393 45.385 1.00 69.57 O
ANISOU 328 O LEU A 74 10543 7964 7929 -1489 1153 -357 O
ATOM 329 CB LEU A 74 -2.514 -7.417 43.471 1.00 61.99 C
ANISOU 329 CB LEU A 74 9645 6855 7054 -1069 845 -287 C
ATOM 330 CG LEU A 74 -2.472 -8.927 43.236 1.00 61.55 C
ANISOU 330 CG LEU A 74 10074 6395 6919 -1001 1080 -212 C
ATOM 331 CD1 LEU A 74 -1.065 -9.464 43.439 1.00 66.37 C
ANISOU 331 CD1 LEU A 74 10978 7003 7237 -446 741 -74 C
ATOM 332 CD2 LEU A 74 -3.459 -9.632 44.150 1.00 66.92 C
ANISOU 332 CD2 LEU A 74 11369 6617 7441 -1221 1617 -150 C
ATOM 333 N VAL A 75 -3.513 -4.365 43.505 1.00 63.96 N
ANISOU 333 N VAL A 75 8881 7783 7640 -1493 639 -541 N
ATOM 334 CA VAL A 75 -3.528 -3.045 44.134 1.00 67.89 C
ANISOU 334 CA VAL A 75 9193 8522 8081 -1495 492 -569 C
ATOM 335 C VAL A 75 -4.944 -2.683 44.565 1.00 71.27 C
ANISOU 335 C VAL A 75 9608 8869 8601 -1826 842 -665 C
ATOM 336 O VAL A 75 -5.183 -2.271 45.711 1.00 70.85 O
ANISOU 336 O VAL A 75 9799 8774 8347 -1813 941 -611 O
ATOM 337 CB VAL A 75 -2.945 -1.986 43.180 1.00 63.37 C
ANISOU 337 CB VAL A 75 8074 8303 7701 -1472 153 -675 C
ATOM 338 CG1 VAL A 75 -3.243 -0.584 43.695 1.00 61.33 C
ANISOU 338 CG1 VAL A 75 7625 8245 7434 -1558 82 -738 C
ATOM 339 CG2 VAL A 75 -1.449 -2.181 43.015 1.00 61.30 C
ANISOU 339 CG2 VAL A 75 7796 8164 7330 -1143 -179 -622 C
ATOM 340 N CYS A 76 -5.907 -2.842 43.651 1.00 67.30 N
ANISOU 340 N CYS A 76 8807 8358 8406 -2112 1029 -841 N
ATOM 341 CA CYS A 76 -7.294 -2.531 43.984 1.00 70.26 C
ANISOU 341 CA CYS A 76 9080 8697 8917 -2426 1364 -1009 C
ATOM 342 C CYS A 76 -7.791 -3.401 45.131 1.00 74.66 C
ANISOU 342 C CYS A 76 10193 8892 9284 -2538 1812 -929 C
ATOM 343 O CYS A 76 -8.439 -2.907 46.062 1.00 80.66 O
ANISOU 343 O CYS A 76 11059 9626 9960 -2654 2030 -958 O
ATOM 344 CB CYS A 76 -8.187 -2.710 42.756 1.00 71.04 C
ANISOU 344 CB CYS A 76 8751 8864 9377 -2668 1451 -1272 C
ATOM 345 SG CYS A 76 -7.826 -1.587 41.392 1.00 68.81 S
ANISOU 345 SG CYS A 76 7908 8962 9274 -2535 992 -1382 S
ATOM 346 N VAL A 77 -7.481 -4.698 45.086 1.00 77.64 N
ANISOU 346 N VAL A 77 10979 8955 9565 -2495 1981 -823 N
ATOM 347 CA VAL A 77 -7.920 -5.623 46.126 1.00 80.59 C
ANISOU 347 CA VAL A 77 12004 8899 9718 -2599 2470 -731 C
ATOM 348 C VAL A 77 -7.317 -5.244 47.471 1.00 85.40 C
ANISOU 348 C VAL A 77 13094 9459 9895 -2299 2379 -504 C
ATOM 349 O VAL A 77 -8.007 -5.229 48.497 1.00 90.63 O
ANISOU 349 O VAL A 77 14114 9920 10402 -2445 2767 -491 O
ATOM 350 CB VAL A 77 -7.560 -7.066 45.724 1.00 76.70 C
ANISOU 350 CB VAL A 77 11912 8058 9174 -2549 2625 -645 C
ATOM 351 CG1 VAL A 77 -7.476 -7.963 46.944 1.00 81.57 C
ANISOU 351 CG1 VAL A 77 13414 8197 9382 -2446 3001 -433 C
ATOM 352 CG2 VAL A 77 -8.573 -7.606 44.726 1.00 72.18 C
ANISOU 352 CG2 VAL A 77 10995 7417 9011 -2973 2925 -931 C
ATOM 353 N ALA A 78 -6.022 -4.927 47.485 1.00 84.50 N
ANISOU 353 N ALA A 78 12985 9540 9582 -1876 1872 -357 N
ATOM 354 CA ALA A 78 -5.341 -4.597 48.729 1.00 87.03 C
ANISOU 354 CA ALA A 78 13743 9849 9475 -1531 1704 -186 C
ATOM 355 C ALA A 78 -5.898 -3.323 49.345 1.00 89.34 C
ANISOU 355 C ALA A 78 13800 10359 9787 -1673 1710 -273 C
ATOM 356 O ALA A 78 -6.081 -3.245 50.566 1.00 95.32 O
ANISOU 356 O ALA A 78 15043 10953 10221 -1596 1891 -179 O
ATOM 357 CB ALA A 78 -3.841 -4.464 48.474 1.00 83.34 C
ANISOU 357 CB ALA A 78 13170 9623 8874 -1075 1125 -112 C
ATOM 358 N VAL A 79 -6.169 -2.308 48.522 1.00 88.11 N
ANISOU 358 N VAL A 79 12952 10551 9975 -1851 1518 -450 N
ATOM 359 CA VAL A 79 -6.707 -1.067 49.072 1.00 90.62 C
ANISOU 359 CA VAL A 79 13060 11064 10308 -1962 1519 -542 C
ATOM 360 C VAL A 79 -8.144 -1.264 49.541 1.00102.21 C
ANISOU 360 C VAL A 79 14648 12325 11863 -2322 2083 -653 C
ATOM 361 O VAL A 79 -8.545 -0.739 50.586 1.00105.90 O
ANISOU 361 O VAL A 79 15334 12759 12145 -2345 2250 -641 O
ATOM 362 CB VAL A 79 -6.592 0.075 48.048 1.00 83.88 C
ANISOU 362 CB VAL A 79 11519 10593 9757 -2014 1176 -697 C
ATOM 363 CG1 VAL A 79 -7.180 1.356 48.619 1.00 80.71 C
ANISOU 363 CG1 VAL A 79 10949 10362 9357 -2108 1190 -795 C
ATOM 364 CG2 VAL A 79 -5.140 0.289 47.657 1.00 80.18 C
ANISOU 364 CG2 VAL A 79 10935 10319 9212 -1706 691 -622 C
ATOM 365 N TRP A 80 -8.944 -2.023 48.786 1.00110.50 N
ANISOU 365 N TRP A 80 15541 13239 13205 -2620 2402 -799 N
ATOM 366 CA TRP A 80 -10.354 -2.166 49.126 1.00114.21 C
ANISOU 366 CA TRP A 80 15993 13562 13839 -3015 2957 -999 C
ATOM 367 C TRP A 80 -10.584 -3.114 50.297 1.00120.37 C
ANISOU 367 C TRP A 80 17554 13880 14300 -3078 3481 -855 C
ATOM 368 O TRP A 80 -11.602 -2.996 50.989 1.00123.79 O
ANISOU 368 O TRP A 80 18086 14193 14757 -3359 3959 -984 O
ATOM 369 CB TRP A 80 -11.140 -2.644 47.902 1.00111.50 C
ANISOU 369 CB TRP A 80 15169 13258 13938 -3323 3107 -1277 C
ATOM 370 CG TRP A 80 -11.250 -1.606 46.820 1.00109.00 C
ANISOU 370 CG TRP A 80 14129 13369 13917 -3286 2690 -1471 C
ATOM 371 CD1 TRP A 80 -11.008 -0.266 46.939 1.00106.29 C
ANISOU 371 CD1 TRP A 80 13535 13327 13522 -3110 2343 -1458 C
ATOM 372 CD2 TRP A 80 -11.623 -1.825 45.453 1.00105.72 C
ANISOU 372 CD2 TRP A 80 13219 13093 13856 -3404 2585 -1707 C
ATOM 373 NE1 TRP A 80 -11.211 0.361 45.733 1.00105.36 N
ANISOU 373 NE1 TRP A 80 12849 13499 13685 -3100 2053 -1652 N
ATOM 374 CE2 TRP A 80 -11.588 -0.574 44.805 1.00104.84 C
ANISOU 374 CE2 TRP A 80 12620 13355 13861 -3259 2174 -1809 C
ATOM 375 CE3 TRP A 80 -11.983 -2.958 44.715 1.00103.10 C
ANISOU 375 CE3 TRP A 80 12846 12591 13737 -3608 2801 -1854 C
ATOM 376 CZ2 TRP A 80 -11.901 -0.424 43.453 1.00101.09 C
ANISOU 376 CZ2 TRP A 80 11686 13083 13640 -3197 1927 -2010 C
ATOM 377 CZ3 TRP A 80 -12.293 -2.806 43.374 1.00101.48 C
ANISOU 377 CZ3 TRP A 80 12138 12637 13783 -3495 2491 -2060 C
ATOM 378 CH2 TRP A 80 -12.250 -1.549 42.758 1.00 98.94 C
ANISOU 378 CH2 TRP A 80 11411 12672 13508 -3250 2051 -2110 C
ATOM 379 N LYS A 81 -9.673 -4.061 50.533 1.00111.50 N
ANISOU 379 N LYS A 81 17022 12479 12864 -2808 3425 -601 N
ATOM 380 CA LYS A 81 -9.910 -5.060 51.569 1.00117.17 C
ANISOU 380 CA LYS A 81 18599 12682 13238 -2846 3967 -452 C
ATOM 381 C LYS A 81 -9.536 -4.550 52.956 1.00120.09 C
ANISOU 381 C LYS A 81 19515 12994 13120 -2548 3917 -254 C
ATOM 382 O LYS A 81 -10.199 -4.891 53.942 1.00129.19 O
ANISOU 382 O LYS A 81 21246 13794 14048 -2706 4479 -219 O
ATOM 383 CB LYS A 81 -9.145 -6.344 51.247 1.00117.82 C
ANISOU 383 CB LYS A 81 19173 12446 13150 -2632 3944 -270 C
ATOM 384 CG LYS A 81 -9.868 -7.258 50.269 1.00114.98 C
ANISOU 384 CG LYS A 81 18605 11899 13181 -3046 4321 -471 C
ATOM 385 CD LYS A 81 -9.120 -8.567 50.074 1.00118.99 C
ANISOU 385 CD LYS A 81 19720 12026 13465 -2815 4349 -272 C
ATOM 386 CE LYS A 81 -9.869 -9.504 49.137 1.00120.43 C
ANISOU 386 CE LYS A 81 19730 11992 14036 -3261 4760 -498 C
ATOM 387 NZ LYS A 81 -9.044 -10.685 48.752 1.00121.99 N
ANISOU 387 NZ LYS A 81 20426 11873 14052 -2996 4691 -316 N
ATOM 388 N ASN A 82 -8.492 -3.734 53.055 1.00125.06 N
ANISOU 388 N ASN A 82 19980 13957 13580 -2134 3279 -152 N
ATOM 389 CA ASN A 82 -8.008 -3.250 54.338 1.00127.76 C
ANISOU 389 CA ASN A 82 20825 14280 13439 -1794 3138 6 C
ATOM 390 C ASN A 82 -8.215 -1.747 54.468 1.00126.59 C
ANISOU 390 C ASN A 82 20111 14550 13435 -1857 2880 -139 C
ATOM 391 O ASN A 82 -8.240 -1.012 53.477 1.00124.29 O
ANISOU 391 O ASN A 82 19060 14623 13542 -1983 2586 -303 O
ATOM 392 CB ASN A 82 -6.529 -3.590 54.530 1.00128.81 C
ANISOU 392 CB ASN A 82 21313 14438 13192 -1206 2597 202 C
ATOM 393 CG ASN A 82 -6.315 -5.035 54.928 1.00136.52 C
ANISOU 393 CG ASN A 82 23175 14895 13801 -1006 2898 403 C
ATOM 394 OD1 ASN A 82 -7.255 -5.729 55.315 1.00144.08 O
ANISOU 394 OD1 ASN A 82 24623 15417 14704 -1311 3573 428 O
ATOM 395 ND2 ASN A 82 -5.077 -5.493 54.847 1.00136.73 N
ANISOU 395 ND2 ASN A 82 23428 14954 13569 -486 2423 527 N
ATOM 396 N HIS A 83 -8.366 -1.300 55.715 1.00137.92 N
ANISOU 396 N HIS A 83 21990 15901 14511 -1748 3008 -73 N
ATOM 397 CA HIS A 83 -8.630 0.101 56.009 1.00132.45 C
ANISOU 397 CA HIS A 83 20881 15544 13902 -1805 2830 -205 C
ATOM 398 C HIS A 83 -7.375 0.892 56.349 1.00132.45 C
ANISOU 398 C HIS A 83 20844 15835 13647 -1364 2164 -144 C
ATOM 399 O HIS A 83 -7.386 2.121 56.221 1.00132.07 O
ANISOU 399 O HIS A 83 20296 16120 13765 -1418 1902 -281 O
ATOM 400 CB HIS A 83 -9.624 0.218 57.171 1.00134.67 C
ANISOU 400 CB HIS A 83 21618 15580 13970 -1988 3398 -216 C
ATOM 401 CG HIS A 83 -10.633 1.310 56.998 1.00137.11 C
ANISOU 401 CG HIS A 83 21312 16151 14634 -2319 3538 -465 C
ATOM 402 ND1 HIS A 83 -11.829 1.120 56.338 1.00133.90 N
ANISOU 402 ND1 HIS A 83 20468 15731 14676 -2771 3979 -700 N
ATOM 403 CD2 HIS A 83 -10.625 2.604 57.396 1.00135.35 C
ANISOU 403 CD2 HIS A 83 20840 16213 14376 -2237 3283 -543 C
ATOM 404 CE1 HIS A 83 -12.514 2.249 56.340 1.00134.51 C
ANISOU 404 CE1 HIS A 83 20056 16086 14968 -2912 3970 -909 C
ATOM 405 NE2 HIS A 83 -11.806 3.165 56.975 1.00134.04 N
ANISOU 405 NE2 HIS A 83 20125 16190 14616 -2601 3566 -801 N
ATOM 406 N HIS A 84 -6.300 0.226 56.775 1.00112.13 N
ANISOU 406 N HIS A 84 18784 13144 10676 -923 1886 24 N
ATOM 407 CA HIS A 84 -5.065 0.938 57.081 1.00105.33 C
ANISOU 407 CA HIS A 84 17816 12599 9604 -506 1233 2 C
ATOM 408 C HIS A 84 -4.363 1.436 55.826 1.00100.75 C
ANISOU 408 C HIS A 84 16439 12404 9439 -539 771 -135 C
ATOM 409 O HIS A 84 -3.498 2.312 55.921 1.00 97.37 O
ANISOU 409 O HIS A 84 15720 12298 8976 -343 286 -241 O
ATOM 410 CB HIS A 84 -4.122 0.045 57.892 1.00107.75 C
ANISOU 410 CB HIS A 84 18889 12697 9356 39 1036 170 C
ATOM 411 CG HIS A 84 -3.678 -1.187 57.166 1.00111.47 C
ANISOU 411 CG HIS A 84 19495 12989 9870 169 1027 267 C
ATOM 412 ND1 HIS A 84 -4.259 -2.420 57.369 1.00117.90 N
ANISOU 412 ND1 HIS A 84 20985 13301 10509 105 1563 435 N
ATOM 413 CD2 HIS A 84 -2.706 -1.376 56.243 1.00109.41 C
ANISOU 413 CD2 HIS A 84 18801 12965 9804 352 577 208 C
ATOM 414 CE1 HIS A 84 -3.665 -3.316 56.600 1.00114.69 C
ANISOU 414 CE1 HIS A 84 20567 12830 10181 262 1417 484 C
ATOM 415 NE2 HIS A 84 -2.720 -2.708 55.906 1.00109.05 N
ANISOU 415 NE2 HIS A 84 19171 12572 9692 422 815 348 N
ATOM 416 N MET A 85 -4.714 0.900 54.658 1.00 98.64 N
ANISOU 416 N MET A 85 15829 12095 9553 -795 933 -157 N
ATOM 417 CA MET A 85 -4.193 1.376 53.385 1.00 87.28 C
ANISOU 417 CA MET A 85 13670 10980 8511 -869 583 -285 C
ATOM 418 C MET A 85 -5.165 2.302 52.669 1.00 80.16 C
ANISOU 418 C MET A 85 12193 10241 8024 -1276 742 -443 C
ATOM 419 O MET A 85 -4.978 2.579 51.482 1.00 74.31 O
ANISOU 419 O MET A 85 10923 9691 7619 -1383 566 -539 O
ATOM 420 CB MET A 85 -3.848 0.199 52.473 1.00 80.23 C
ANISOU 420 CB MET A 85 12782 9958 7745 -822 594 -221 C
ATOM 421 CG MET A 85 -2.630 -0.591 52.891 1.00 83.73 C
ANISOU 421 CG MET A 85 13649 10337 7828 -329 283 -111 C
ATOM 422 SD MET A 85 -1.707 -1.147 51.449 1.00 84.03 S
ANISOU 422 SD MET A 85 13233 10532 8163 -235 -22 -162 S
ATOM 423 CE MET A 85 -3.043 -1.518 50.320 1.00 79.06 C
ANISOU 423 CE MET A 85 12322 9735 7981 -771 466 -194 C
ATOM 424 N ARG A 86 -6.202 2.777 53.356 1.00 86.14 N
ANISOU 424 N ARG A 86 13066 10920 8744 -1474 1075 -485 N
ATOM 425 CA ARG A 86 -7.250 3.571 52.722 1.00 81.91 C
ANISOU 425 CA ARG A 86 12019 10524 8580 -1809 1246 -663 C
ATOM 426 C ARG A 86 -6.944 5.052 52.934 1.00 74.89 C
ANISOU 426 C ARG A 86 10860 9915 7680 -1745 931 -758 C
ATOM 427 O ARG A 86 -7.530 5.729 53.778 1.00 72.32 O
ANISOU 427 O ARG A 86 10662 9585 7233 -1797 1086 -802 O
ATOM 428 CB ARG A 86 -8.619 3.178 53.268 1.00 93.06 C
ANISOU 428 CB ARG A 86 13655 11697 10009 -2082 1834 -710 C
ATOM 429 CG ARG A 86 -9.630 2.845 52.184 1.00 92.95 C
ANISOU 429 CG ARG A 86 13197 11688 10433 -2412 2100 -893 C
ATOM 430 CD ARG A 86 -10.853 2.134 52.739 1.00106.35 C
ANISOU 430 CD ARG A 86 15152 13103 12154 -2709 2745 -973 C
ATOM 431 NE ARG A 86 -10.595 0.723 53.005 1.00116.77 N
ANISOU 431 NE ARG A 86 17036 14050 13282 -2693 3017 -807 N
ATOM 432 CZ ARG A 86 -11.537 -0.170 53.277 1.00122.84 C
ANISOU 432 CZ ARG A 86 18071 14499 14104 -2999 3634 -880 C
ATOM 433 NH1 ARG A 86 -12.815 0.167 53.330 1.00125.04 N
ANISOU 433 NH1 ARG A 86 18035 14823 14650 -3354 4043 -1150 N
ATOM 434 NH2 ARG A 86 -11.188 -1.435 53.498 1.00122.54 N
ANISOU 434 NH2 ARG A 86 18631 14079 13848 -2948 3865 -704 N
ATOM 435 N THR A 87 -5.999 5.553 52.144 1.00 70.27 N
ANISOU 435 N THR A 87 9915 9558 7226 -1645 515 -802 N
ATOM 436 CA THR A 87 -5.637 6.961 52.126 1.00 60.81 C
ANISOU 436 CA THR A 87 8436 8601 6069 -1633 238 -919 C
ATOM 437 C THR A 87 -6.016 7.575 50.785 1.00 58.40 C
ANISOU 437 C THR A 87 7623 8429 6135 -1814 207 -1042 C
ATOM 438 O THR A 87 -6.232 6.873 49.793 1.00 61.06 O
ANISOU 438 O THR A 87 7785 8727 6687 -1892 280 -1041 O
ATOM 439 CB THR A 87 -4.137 7.158 52.380 1.00 58.33 C
ANISOU 439 CB THR A 87 8148 8437 5580 -1377 -197 -920 C
ATOM 440 OG1 THR A 87 -3.391 6.686 51.251 1.00 57.36 O
ANISOU 440 OG1 THR A 87 7744 8391 5659 -1348 -380 -927 O
ATOM 441 CG2 THR A 87 -3.701 6.398 53.622 1.00 62.72 C
ANISOU 441 CG2 THR A 87 9254 8856 5718 -1098 -226 -805 C
ATOM 442 N VAL A 88 -6.088 8.909 50.768 1.00 56.43 N
ANISOU 442 N VAL A 88 7186 8321 5932 -1855 93 -1155 N
ATOM 443 CA VAL A 88 -6.470 9.627 49.554 1.00 56.85 C
ANISOU 443 CA VAL A 88 6861 8472 6267 -1966 58 -1270 C
ATOM 444 C VAL A 88 -5.495 9.322 48.423 1.00 55.03 C
ANISOU 444 C VAL A 88 6425 8306 6178 -1930 -160 -1252 C
ATOM 445 O VAL A 88 -5.901 9.088 47.274 1.00 57.25 O
ANISOU 445 O VAL A 88 6489 8586 6677 -1994 -112 -1290 O
ATOM 446 CB VAL A 88 -6.566 11.138 49.845 1.00 56.38 C
ANISOU 446 CB VAL A 88 6752 8504 6166 -1977 -26 -1376 C
ATOM 447 CG1 VAL A 88 -5.361 11.607 50.652 1.00 59.65 C
ANISOU 447 CG1 VAL A 88 7314 8984 6365 -1879 -272 -1371 C
ATOM 448 CG2 VAL A 88 -6.692 11.928 48.556 1.00 55.94 C
ANISOU 448 CG2 VAL A 88 6412 8514 6329 -2021 -107 -1474 C
ATOM 449 N THR A 89 -4.195 9.305 48.732 1.00 52.23 N
ANISOU 449 N THR A 89 6125 8022 5696 -1812 -406 -1226 N
ATOM 450 CA THR A 89 -3.205 8.878 47.750 1.00 54.16 C
ANISOU 450 CA THR A 89 6177 8331 6070 -1771 -579 -1227 C
ATOM 451 C THR A 89 -3.512 7.473 47.248 1.00 55.52 C
ANISOU 451 C THR A 89 6396 8384 6316 -1749 -451 -1126 C
ATOM 452 O THR A 89 -3.415 7.198 46.047 1.00 55.82 O
ANISOU 452 O THR A 89 6222 8435 6552 -1793 -465 -1144 O
ATOM 453 CB THR A 89 -1.803 8.936 48.359 1.00 53.10 C
ANISOU 453 CB THR A 89 6074 8319 5782 -1619 -858 -1272 C
ATOM 454 OG1 THR A 89 -1.518 10.276 48.781 1.00 52.95 O
ANISOU 454 OG1 THR A 89 5993 8402 5722 -1686 -957 -1409 O
ATOM 455 CG2 THR A 89 -0.755 8.493 47.346 1.00 52.85 C
ANISOU 455 CG2 THR A 89 5800 8375 5905 -1580 -1012 -1311 C
ATOM 456 N ASN A 90 -3.914 6.577 48.151 1.00 54.47 N
ANISOU 456 N ASN A 90 6583 8103 6009 -1688 -294 -1025 N
ATOM 457 CA ASN A 90 -4.255 5.223 47.732 1.00 56.57 C
ANISOU 457 CA ASN A 90 6952 8205 6339 -1700 -117 -942 C
ATOM 458 C ASN A 90 -5.548 5.184 46.926 1.00 58.47 C
ANISOU 458 C ASN A 90 6985 8396 6837 -1923 136 -1030 C
ATOM 459 O ASN A 90 -5.686 4.341 46.036 1.00 60.19 O
ANISOU 459 O ASN A 90 7105 8548 7214 -1970 200 -1034 O
ATOM 460 CB ASN A 90 -4.349 4.303 48.947 1.00 59.02 C
ANISOU 460 CB ASN A 90 7756 8312 6359 -1583 42 -813 C
ATOM 461 CG ASN A 90 -2.992 4.000 49.554 1.00 59.79 C
ANISOU 461 CG ASN A 90 8068 8459 6189 -1264 -270 -749 C
ATOM 462 OD1 ASN A 90 -1.965 4.084 48.879 1.00 57.26 O
ANISOU 462 OD1 ASN A 90 7484 8306 5966 -1159 -557 -806 O
ATOM 463 ND2 ASN A 90 -2.980 3.643 50.832 1.00 61.41 N
ANISOU 463 ND2 ASN A 90 8760 8526 6046 -1088 -211 -657 N
ATOM 464 N TYR A 91 -6.501 6.076 47.209 1.00 53.66 N
ANISOU 464 N TYR A 91 6288 7831 6270 -2039 263 -1134 N
ATOM 465 CA TYR A 91 -7.695 6.155 46.369 1.00 56.13 C
ANISOU 465 CA TYR A 91 6326 8162 6839 -2194 431 -1290 C
ATOM 466 C TYR A 91 -7.337 6.564 44.945 1.00 57.06 C
ANISOU 466 C TYR A 91 6139 8404 7138 -2154 205 -1356 C
ATOM 467 O TYR A 91 -7.841 5.985 43.970 1.00 57.10 O
ANISOU 467 O TYR A 91 5967 8394 7333 -2208 263 -1443 O
ATOM 468 CB TYR A 91 -8.702 7.140 46.965 1.00 54.76 C
ANISOU 468 CB TYR A 91 6102 8044 6659 -2262 567 -1418 C
ATOM 469 CG TYR A 91 -9.466 6.614 48.159 1.00 57.37 C
ANISOU 469 CG TYR A 91 6697 8226 6875 -2367 918 -1411 C
ATOM 470 CD1 TYR A 91 -10.439 5.636 48.010 1.00 65.60 C
ANISOU 470 CD1 TYR A 91 7704 9146 8076 -2552 1262 -1515 C
ATOM 471 CD2 TYR A 91 -9.230 7.113 49.433 1.00 60.87 C
ANISOU 471 CD2 TYR A 91 7440 8640 7049 -2298 937 -1328 C
ATOM 472 CE1 TYR A 91 -11.145 5.158 49.097 1.00 69.93 C
ANISOU 472 CE1 TYR A 91 8532 9520 8519 -2690 1666 -1523 C
ATOM 473 CE2 TYR A 91 -9.930 6.642 50.527 1.00 66.58 C
ANISOU 473 CE2 TYR A 91 8470 9196 7631 -2390 1304 -1314 C
ATOM 474 CZ TYR A 91 -10.886 5.665 50.353 1.00 72.29 C
ANISOU 474 CZ TYR A 91 9175 9774 8519 -2598 1694 -1406 C
ATOM 475 OH TYR A 91 -11.588 5.195 51.438 1.00 78.58 O
ANISOU 475 OH TYR A 91 10314 10367 9176 -2731 2138 -1406 O
ATOM 476 N PHE A 92 -6.462 7.560 44.804 1.00 55.04 N
ANISOU 476 N PHE A 92 5842 8255 6817 -2067 -31 -1335 N
ATOM 477 CA PHE A 92 -6.016 7.951 43.471 1.00 54.78 C
ANISOU 477 CA PHE A 92 5608 8292 6913 -2032 -192 -1380 C
ATOM 478 C PHE A 92 -5.232 6.827 42.802 1.00 56.87 C
ANISOU 478 C PHE A 92 5852 8519 7235 -1995 -252 -1303 C
ATOM 479 O PHE A 92 -5.339 6.621 41.587 1.00 58.97 O
ANISOU 479 O PHE A 92 6001 8765 7640 -1948 -274 -1325 O
ATOM 480 CB PHE A 92 -5.179 9.225 43.551 1.00 54.73 C
ANISOU 480 CB PHE A 92 5609 8364 6822 -2002 -354 -1391 C
ATOM 481 CG PHE A 92 -5.988 10.473 43.772 1.00 56.28 C
ANISOU 481 CG PHE A 92 5823 8572 6988 -2001 -308 -1481 C
ATOM 482 CD1 PHE A 92 -6.890 10.908 42.815 1.00 57.32 C
ANISOU 482 CD1 PHE A 92 5885 8671 7222 -1902 -272 -1548 C
ATOM 483 CD2 PHE A 92 -5.832 11.221 44.927 1.00 54.22 C
ANISOU 483 CD2 PHE A 92 5695 8334 6572 -2023 -318 -1488 C
ATOM 484 CE1 PHE A 92 -7.632 12.057 43.012 1.00 57.92 C
ANISOU 484 CE1 PHE A 92 5973 8784 7251 -1883 -258 -1673 C
ATOM 485 CE2 PHE A 92 -6.569 12.373 45.127 1.00 53.82 C
ANISOU 485 CE2 PHE A 92 5677 8287 6485 -2013 -274 -1581 C
ATOM 486 CZ PHE A 92 -7.471 12.790 44.169 1.00 57.69 C
ANISOU 486 CZ PHE A 92 6062 8777 7081 -1951 -246 -1685 C
ATOM 487 N ILE A 93 -4.437 6.088 43.580 1.00 57.24 N
ANISOU 487 N ILE A 93 6076 8524 7149 -1927 -287 -1189 N
ATOM 488 CA ILE A 93 -3.712 4.944 43.033 1.00 55.17 C
ANISOU 488 CA ILE A 93 5826 8214 6923 -1850 -340 -1120 C
ATOM 489 C ILE A 93 -4.686 3.880 42.541 1.00 59.19 C
ANISOU 489 C ILE A 93 6346 8583 7559 -1938 -132 -1138 C
ATOM 490 O ILE A 93 -4.459 3.235 41.512 1.00 60.08 O
ANISOU 490 O ILE A 93 6359 8675 7794 -1922 -163 -1150 O
ATOM 491 CB ILE A 93 -2.732 4.388 44.083 1.00 53.46 C
ANISOU 491 CB ILE A 93 5844 7978 6491 -1683 -446 -1018 C
ATOM 492 CG1 ILE A 93 -1.560 5.354 44.274 1.00 53.22 C
ANISOU 492 CG1 ILE A 93 5685 8135 6402 -1607 -697 -1085 C
ATOM 493 CG2 ILE A 93 -2.228 3.010 43.685 1.00 57.60 C
ANISOU 493 CG2 ILE A 93 6466 8400 7019 -1566 -452 -940 C
ATOM 494 CD1 ILE A 93 -0.589 4.937 45.353 1.00 53.45 C
ANISOU 494 CD1 ILE A 93 5902 8204 6202 -1384 -875 -1054 C
ATOM 495 N VAL A 94 -5.790 3.686 43.266 1.00 52.55 N
ANISOU 495 N VAL A 94 5619 7644 6702 -2052 107 -1172 N
ATOM 496 CA VAL A 94 -6.821 2.748 42.831 1.00 56.00 C
ANISOU 496 CA VAL A 94 6018 7956 7302 -2201 353 -1265 C
ATOM 497 C VAL A 94 -7.435 3.202 41.515 1.00 58.25 C
ANISOU 497 C VAL A 94 5950 8370 7814 -2242 275 -1454 C
ATOM 498 O VAL A 94 -7.669 2.391 40.611 1.00 57.55 O
ANISOU 498 O VAL A 94 5760 8233 7874 -2283 311 -1532 O
ATOM 499 CB VAL A 94 -7.892 2.585 43.925 1.00 58.80 C
ANISOU 499 CB VAL A 94 6538 8193 7611 -2355 679 -1315 C
ATOM 500 CG1 VAL A 94 -9.154 1.954 43.354 1.00 63.22 C
ANISOU 500 CG1 VAL A 94 6907 8692 8421 -2572 945 -1534 C
ATOM 501 CG2 VAL A 94 -7.354 1.740 45.049 1.00 65.98 C
ANISOU 501 CG2 VAL A 94 7913 8892 8266 -2286 805 -1119 C
ATOM 502 N ASN A 95 -7.720 4.500 41.391 1.00 58.41 N
ANISOU 502 N ASN A 95 5841 8523 7829 -2171 160 -1520 N
ATOM 503 CA ASN A 95 -8.256 5.010 40.129 1.00 56.88 C
ANISOU 503 CA ASN A 95 5532 8349 7730 -1962 50 -1572 C
ATOM 504 C ASN A 95 -7.270 4.789 38.984 1.00 55.79 C
ANISOU 504 C ASN A 95 5410 8188 7600 -1830 -119 -1467 C
ATOM 505 O ASN A 95 -7.662 4.398 37.873 1.00 56.48 O
ANISOU 505 O ASN A 95 5436 8248 7775 -1744 -146 -1524 O
ATOM 506 CB ASN A 95 -8.603 6.493 40.266 1.00 58.40 C
ANISOU 506 CB ASN A 95 5704 8631 7857 -1861 -30 -1619 C
ATOM 507 CG ASN A 95 -9.077 7.104 38.962 1.00 57.17 C
ANISOU 507 CG ASN A 95 5471 8507 7746 -1668 -154 -1705 C
ATOM 508 OD1 ASN A 95 -10.180 6.819 38.495 1.00 58.56 O
ANISOU 508 OD1 ASN A 95 5516 8713 8023 -1622 -110 -1879 O
ATOM 509 ND2 ASN A 95 -8.248 7.956 38.371 1.00 57.59 N
ANISOU 509 ND2 ASN A 95 5604 8562 7714 -1571 -298 -1626 N
ATOM 510 N LEU A 96 -5.982 5.029 39.244 1.00 54.72 N
ANISOU 510 N LEU A 96 5343 8079 7370 -1819 -227 -1346 N
ATOM 511 CA LEU A 96 -4.955 4.790 38.236 1.00 56.31 C
ANISOU 511 CA LEU A 96 5543 8262 7589 -1718 -342 -1269 C
ATOM 512 C LEU A 96 -4.903 3.320 37.839 1.00 57.91 C
ANISOU 512 C LEU A 96 5720 8407 7877 -1772 -291 -1285 C
ATOM 513 O LEU A 96 -4.770 2.992 36.655 1.00 58.87 O
ANISOU 513 O LEU A 96 5814 8493 8061 -1683 -337 -1287 O
ATOM 514 CB LEU A 96 -3.595 5.260 38.757 1.00 52.95 C
ANISOU 514 CB LEU A 96 5149 7901 7069 -1710 -445 -1195 C
ATOM 515 CG LEU A 96 -2.373 5.110 37.849 1.00 56.68 C
ANISOU 515 CG LEU A 96 5591 8375 7571 -1627 -527 -1149 C
ATOM 516 CD1 LEU A 96 -1.459 6.308 38.008 1.00 53.09 C
ANISOU 516 CD1 LEU A 96 5151 7960 7062 -1609 -575 -1141 C
ATOM 517 CD2 LEU A 96 -1.615 3.827 38.160 1.00 61.76 C
ANISOU 517 CD2 LEU A 96 6180 9072 8214 -1654 -577 -1152 C
ATOM 518 N SER A 97 -5.002 2.420 38.818 1.00 56.91 N
ANISOU 518 N SER A 97 5629 8258 7736 -1954 -175 -1317 N
ATOM 519 CA SER A 97 -4.969 0.993 38.519 1.00 56.60 C
ANISOU 519 CA SER A 97 5672 8077 7755 -1979 -76 -1301 C
ATOM 520 C SER A 97 -6.204 0.559 37.739 1.00 57.75 C
ANISOU 520 C SER A 97 5706 8165 8073 -2058 47 -1463 C
ATOM 521 O SER A 97 -6.119 -0.322 36.878 1.00 56.71 O
ANISOU 521 O SER A 97 5558 7961 8028 -2046 52 -1498 O
ATOM 522 CB SER A 97 -4.836 0.191 39.813 1.00 54.67 C
ANISOU 522 CB SER A 97 5742 7667 7362 -1979 73 -1169 C
ATOM 523 OG SER A 97 -3.616 0.493 40.466 1.00 56.38 O
ANISOU 523 OG SER A 97 6077 7951 7395 -1797 -109 -1033 O
ATOM 524 N LEU A 98 -7.361 1.156 38.034 1.00 57.71 N
ANISOU 524 N LEU A 98 5655 8180 8094 -2063 134 -1549 N
ATOM 525 CA LEU A 98 -8.565 0.862 37.261 1.00 57.12 C
ANISOU 525 CA LEU A 98 5472 8085 8146 -2028 198 -1712 C
ATOM 526 C LEU A 98 -8.401 1.295 35.809 1.00 58.92 C
ANISOU 526 C LEU A 98 5633 8380 8373 -1804 -21 -1717 C
ATOM 527 O LEU A 98 -8.751 0.548 34.883 1.00 61.40 O
ANISOU 527 O LEU A 98 5894 8663 8774 -1781 -21 -1822 O
ATOM 528 CB LEU A 98 -9.777 1.548 37.892 1.00 57.13 C
ANISOU 528 CB LEU A 98 5392 8147 8167 -2057 310 -1851 C
ATOM 529 CG LEU A 98 -10.228 1.040 39.262 1.00 59.31 C
ANISOU 529 CG LEU A 98 5756 8326 8453 -2319 620 -1897 C
ATOM 530 CD1 LEU A 98 -11.367 1.890 39.800 1.00 59.15 C
ANISOU 530 CD1 LEU A 98 5620 8402 8452 -2315 709 -2055 C
ATOM 531 CD2 LEU A 98 -10.637 -0.423 39.181 1.00 63.41 C
ANISOU 531 CD2 LEU A 98 6337 8665 9091 -2511 880 -1995 C
ATOM 532 N ALA A 99 -7.861 2.496 35.590 1.00 59.65 N
ANISOU 532 N ALA A 99 5752 8551 8360 -1661 -181 -1626 N
ATOM 533 CA ALA A 99 -7.588 2.933 34.223 1.00 62.51 C
ANISOU 533 CA ALA A 99 6108 8948 8693 -1492 -338 -1640 C
ATOM 534 C ALA A 99 -6.586 2.005 33.544 1.00 63.75 C
ANISOU 534 C ALA A 99 6305 9047 8872 -1499 -368 -1562 C
ATOM 535 O ALA A 99 -6.726 1.682 32.357 1.00 63.61 O
ANISOU 535 O ALA A 99 6258 9029 8882 -1416 -430 -1649 O
ATOM 536 CB ALA A 99 -7.078 4.373 34.221 1.00 63.97 C
ANISOU 536 CB ALA A 99 6355 9190 8760 -1406 -437 -1574 C
ATOM 537 N ALA A 100 -5.571 1.561 34.290 1.00 58.56 N
ANISOU 537 N ALA A 100 5697 8358 8194 -1588 -337 -1434 N
ATOM 538 CA ALA A 100 -4.571 0.654 33.740 1.00 58.08 C
ANISOU 538 CA ALA A 100 5642 8265 8160 -1588 -367 -1394 C
ATOM 539 C ALA A 100 -5.191 -0.674 33.325 1.00 60.49 C
ANISOU 539 C ALA A 100 5925 8476 8582 -1668 -276 -1513 C
ATOM 540 O ALA A 100 -4.856 -1.217 32.267 1.00 61.81 O
ANISOU 540 O ALA A 100 6077 8622 8785 -1609 -327 -1552 O
ATOM 541 CB ALA A 100 -3.457 0.431 34.762 1.00 56.11 C
ANISOU 541 CB ALA A 100 5410 8050 7861 -1658 -376 -1308 C
ATOM 542 N VAL A 101 -6.087 -1.217 34.151 1.00 59.39 N
ANISOU 542 N VAL A 101 5793 8264 8507 -1827 -110 -1593 N
ATOM 543 CA VAL A 101 -6.780 -2.455 33.802 1.00 55.91 C
ANISOU 543 CA VAL A 101 5349 7698 8196 -1947 36 -1741 C
ATOM 544 C VAL A 101 -7.637 -2.250 32.561 1.00 61.37 C
ANISOU 544 C VAL A 101 5929 8458 8930 -1806 -58 -1890 C
ATOM 545 O VAL A 101 -7.699 -3.117 31.678 1.00 62.24 O
ANISOU 545 O VAL A 101 6021 8513 9114 -1808 -59 -1995 O
ATOM 546 CB VAL A 101 -7.620 -2.956 34.993 1.00 55.52 C
ANISOU 546 CB VAL A 101 5363 7530 8202 -2183 312 -1816 C
ATOM 547 CG1 VAL A 101 -8.585 -4.046 34.549 1.00 55.35 C
ANISOU 547 CG1 VAL A 101 5323 7381 8325 -2307 500 -2013 C
ATOM 548 CG2 VAL A 101 -6.718 -3.473 36.093 1.00 57.79 C
ANISOU 548 CG2 VAL A 101 5871 7680 8408 -2323 437 -1676 C
ATOM 549 N LEU A 102 -8.317 -1.103 32.477 1.00 60.29 N
ANISOU 549 N LEU A 102 5721 8444 8744 -1682 -142 -1937 N
ATOM 550 CA LEU A 102 -9.122 -0.808 31.296 1.00 61.09 C
ANISOU 550 CA LEU A 102 5714 8634 8864 -1525 -260 -2130 C
ATOM 551 C LEU A 102 -8.263 -0.810 30.036 1.00 62.35 C
ANISOU 551 C LEU A 102 5925 8803 8962 -1385 -421 -2090 C
ATOM 552 O LEU A 102 -8.635 -1.405 29.016 1.00 61.45 O
ANISOU 552 O LEU A 102 5756 8692 8901 -1327 -471 -2258 O
ATOM 553 CB LEU A 102 -9.826 0.538 31.469 1.00 60.78 C
ANISOU 553 CB LEU A 102 5610 8720 8762 -1398 -338 -2198 C
ATOM 554 CG LEU A 102 -10.641 1.042 30.276 1.00 59.42 C
ANISOU 554 CG LEU A 102 5329 8667 8582 -1181 -501 -2440 C
ATOM 555 CD1 LEU A 102 -11.763 0.072 29.941 1.00 60.22 C
ANISOU 555 CD1 LEU A 102 5258 8784 8837 -1226 -424 -2723 C
ATOM 556 CD2 LEU A 102 -11.192 2.431 30.556 1.00 60.90 C
ANISOU 556 CD2 LEU A 102 5478 8969 8693 -1042 -585 -2509 C
ATOM 557 N VAL A 103 -7.097 -0.161 30.096 1.00 60.64 N
ANISOU 557 N VAL A 103 5806 8596 8639 -1340 -488 -1898 N
ATOM 558 CA VAL A 103 -6.198 -0.137 28.943 1.00 60.58 C
ANISOU 558 CA VAL A 103 5845 8598 8576 -1237 -595 -1883 C
ATOM 559 C VAL A 103 -5.695 -1.539 28.624 1.00 60.69 C
ANISOU 559 C VAL A 103 5859 8520 8679 -1316 -542 -1895 C
ATOM 560 O VAL A 103 -5.639 -1.947 27.458 1.00 61.72 O
ANISOU 560 O VAL A 103 5984 8649 8818 -1235 -616 -2014 O
ATOM 561 CB VAL A 103 -5.028 0.831 29.190 1.00 60.72 C
ANISOU 561 CB VAL A 103 5936 8647 8488 -1223 -618 -1716 C
ATOM 562 CG1 VAL A 103 -4.149 0.914 27.964 1.00 63.58 C
ANISOU 562 CG1 VAL A 103 6332 9027 8800 -1148 -684 -1758 C
ATOM 563 CG2 VAL A 103 -5.542 2.190 29.532 1.00 65.65 C
ANISOU 563 CG2 VAL A 103 6578 9336 9030 -1169 -658 -1733 C
ATOM 564 N THR A 104 -5.316 -2.296 29.656 1.00 59.73 N
ANISOU 564 N THR A 104 5758 8318 8618 -1471 -422 -1802 N
ATOM 565 CA THR A 104 -4.729 -3.615 29.446 1.00 57.52 C
ANISOU 565 CA THR A 104 5497 7931 8427 -1555 -366 -1834 C
ATOM 566 C THR A 104 -5.726 -4.567 28.802 1.00 58.96 C
ANISOU 566 C THR A 104 5653 8030 8720 -1609 -308 -2041 C
ATOM 567 O THR A 104 -5.354 -5.394 27.961 1.00 59.12 O
ANISOU 567 O THR A 104 5688 7983 8791 -1598 -330 -2126 O
ATOM 568 CB THR A 104 -4.230 -4.177 30.778 1.00 58.39 C
ANISOU 568 CB THR A 104 5658 7956 8572 -1721 -244 -1753 C
ATOM 569 OG1 THR A 104 -3.400 -3.205 31.427 1.00 59.77 O
ANISOU 569 OG1 THR A 104 5829 8248 8631 -1647 -322 -1592 O
ATOM 570 CG2 THR A 104 -3.423 -5.443 30.558 1.00 55.78 C
ANISOU 570 CG2 THR A 104 5496 7461 8237 -1659 -190 -1671 C
ATOM 571 N ILE A 105 -7.000 -4.465 29.180 1.00 58.38 N
ANISOU 571 N ILE A 105 5522 7968 8694 -1669 -228 -2156 N
ATOM 572 CA ILE A 105 -7.999 -5.373 28.628 1.00 60.01 C
ANISOU 572 CA ILE A 105 5660 8118 9023 -1737 -151 -2398 C
ATOM 573 C ILE A 105 -8.470 -4.903 27.256 1.00 59.84 C
ANISOU 573 C ILE A 105 5540 8235 8962 -1518 -354 -2567 C
ATOM 574 O ILE A 105 -8.591 -5.706 26.324 1.00 62.05 O
ANISOU 574 O ILE A 105 5798 8476 9301 -1502 -385 -2730 O
ATOM 575 CB ILE A 105 -9.174 -5.529 29.611 1.00 60.65 C
ANISOU 575 CB ILE A 105 5682 8169 9194 -1908 58 -2510 C
ATOM 576 CG1 ILE A 105 -8.719 -6.270 30.870 1.00 62.78 C
ANISOU 576 CG1 ILE A 105 6122 8235 9498 -2156 308 -2388 C
ATOM 577 CG2 ILE A 105 -10.335 -6.259 28.953 1.00 53.04 C
ANISOU 577 CG2 ILE A 105 4580 7206 8366 -1960 130 -2822 C
ATOM 578 CD1 ILE A 105 -9.837 -6.557 31.850 1.00 62.99 C
ANISOU 578 CD1 ILE A 105 6141 8186 9607 -2367 592 -2514 C
ATOM 579 N THR A 106 -8.728 -3.603 27.096 1.00 58.90 N
ANISOU 579 N THR A 106 5383 8262 8734 -1339 -495 -2554 N
ATOM 580 CA THR A 106 -9.390 -3.111 25.895 1.00 59.92 C
ANISOU 580 CA THR A 106 5432 8517 8817 -1112 -686 -2775 C
ATOM 581 C THR A 106 -8.440 -2.583 24.828 1.00 61.94 C
ANISOU 581 C THR A 106 5810 8801 8922 -920 -870 -2716 C
ATOM 582 O THR A 106 -8.836 -2.510 23.659 1.00 63.43 O
ANISOU 582 O THR A 106 5986 9056 9058 -720 -1039 -2922 O
ATOM 583 CB THR A 106 -10.388 -2.002 26.255 1.00 62.23 C
ANISOU 583 CB THR A 106 5623 8943 9080 -1000 -737 -2878 C
ATOM 584 OG1 THR A 106 -9.696 -0.919 26.890 1.00 63.28 O
ANISOU 584 OG1 THR A 106 5868 9086 9089 -979 -755 -2642 O
ATOM 585 CG2 THR A 106 -11.459 -2.534 27.195 1.00 62.68 C
ANISOU 585 CG2 THR A 106 5530 8991 9296 -1187 -537 -3017 C
ATOM 586 N CYS A 107 -7.213 -2.214 25.182 1.00 61.19 N
ANISOU 586 N CYS A 107 6916 8150 8184 -116 350 -1358 N
ATOM 587 CA CYS A 107 -6.331 -1.545 24.237 1.00 61.02 C
ANISOU 587 CA CYS A 107 7005 8146 8035 22 325 -1255 C
ATOM 588 C CYS A 107 -5.034 -2.287 23.953 1.00 61.77 C
ANISOU 588 C CYS A 107 7192 8206 8073 45 414 -1160 C
ATOM 589 O CYS A 107 -4.468 -2.106 22.872 1.00 60.88 O
ANISOU 589 O CYS A 107 7175 8111 7844 140 412 -1138 O
ATOM 590 CB CYS A 107 -5.992 -0.131 24.737 1.00 60.97 C
ANISOU 590 CB CYS A 107 6991 8171 8005 37 335 -1146 C
ATOM 591 SG CYS A 107 -7.442 0.911 25.025 1.00 61.43 S
ANISOU 591 SG CYS A 107 6932 8270 8139 54 201 -1286 S
ATOM 592 N LEU A 108 -4.540 -3.103 24.890 1.00 60.88 N
ANISOU 592 N LEU A 108 7065 8036 8030 -36 487 -1117 N
ATOM 593 CA LEU A 108 -3.274 -3.798 24.657 1.00 60.68 C
ANISOU 593 CA LEU A 108 7103 7974 7978 17 540 -1063 C
ATOM 594 C LEU A 108 -3.357 -4.796 23.506 1.00 60.16 C
ANISOU 594 C LEU A 108 7100 7889 7867 87 504 -1167 C
ATOM 595 O LEU A 108 -2.478 -4.760 22.626 1.00 62.17 O
ANISOU 595 O LEU A 108 7403 8177 8042 180 545 -1157 O
ATOM 596 CB LEU A 108 -2.795 -4.453 25.959 1.00 60.36 C
ANISOU 596 CB LEU A 108 7070 7843 8021 -64 570 -1009 C
ATOM 597 CG LEU A 108 -1.377 -5.030 25.999 1.00 57.94 C
ANISOU 597 CG LEU A 108 6799 7488 7727 13 590 -970 C
ATOM 598 CD1 LEU A 108 -0.804 -4.902 27.399 1.00 57.06 C
ANISOU 598 CD1 LEU A 108 6694 7308 7677 -42 590 -879 C
ATOM 599 CD2 LEU A 108 -1.356 -6.487 25.555 1.00 55.32 C
ANISOU 599 CD2 LEU A 108 6544 7068 7407 48 541 -1064 C
ATOM 600 N PRO A 109 -4.336 -5.712 23.448 1.00 58.47 N
ANISOU 600 N PRO A 109 6892 7626 7700 35 443 -1280 N
ATOM 601 CA PRO A 109 -4.363 -6.648 22.309 1.00 61.83 C
ANISOU 601 CA PRO A 109 7388 8028 8077 113 397 -1381 C
ATOM 602 C PRO A 109 -4.506 -5.957 20.965 1.00 61.69 C
ANISOU 602 C PRO A 109 7420 8087 7934 224 356 -1418 C
ATOM 603 O PRO A 109 -3.870 -6.374 19.989 1.00 62.19 O
ANISOU 603 O PRO A 109 7569 8156 7906 314 377 -1446 O
ATOM 604 CB PRO A 109 -5.570 -7.545 22.622 1.00 64.34 C
ANISOU 604 CB PRO A 109 7687 8280 8479 1 337 -1502 C
ATOM 605 CG PRO A 109 -5.760 -7.431 24.090 1.00 60.50 C
ANISOU 605 CG PRO A 109 7159 7753 8076 -152 394 -1442 C
ATOM 606 CD PRO A 109 -5.409 -6.015 24.414 1.00 58.94 C
ANISOU 606 CD PRO A 109 6897 7643 7854 -116 430 -1336 C
ATOM 607 N ALA A 110 -5.319 -4.901 20.891 1.00 63.89 N
ANISOU 607 N ALA A 110 7668 8415 8194 225 289 -1428 N
ATOM 608 CA ALA A 110 -5.469 -4.174 19.635 1.00 63.67 C
ANISOU 608 CA ALA A 110 7753 8424 8016 334 214 -1452 C
ATOM 609 C ALA A 110 -4.154 -3.531 19.215 1.00 62.46 C
ANISOU 609 C ALA A 110 7702 8305 7727 373 337 -1327 C
ATOM 610 O ALA A 110 -3.772 -3.592 18.040 1.00 62.83 O
ANISOU 610 O ALA A 110 7895 8360 7618 441 351 -1352 O
ATOM 611 CB ALA A 110 -6.568 -3.120 19.765 1.00 62.76 C
ANISOU 611 CB ALA A 110 7592 8331 7924 346 81 -1499 C
ATOM 612 N THR A 111 -3.445 -2.917 20.166 1.00 63.08 N
ANISOU 612 N THR A 111 7708 8402 7858 315 437 -1206 N
ATOM 613 CA THR A 111 -2.159 -2.304 19.852 1.00 62.97 C
ANISOU 613 CA THR A 111 7756 8428 7743 321 575 -1110 C
ATOM 614 C THR A 111 -1.153 -3.348 19.387 1.00 63.77 C
ANISOU 614 C THR A 111 7859 8536 7835 353 683 -1163 C
ATOM 615 O THR A 111 -0.401 -3.113 18.435 1.00 63.77 O
ANISOU 615 O THR A 111 7956 8578 7694 376 787 -1171 O
ATOM 616 CB THR A 111 -1.625 -1.548 21.069 1.00 61.98 C
ANISOU 616 CB THR A 111 7525 8315 7709 251 643 -992 C
ATOM 617 OG1 THR A 111 -2.563 -0.534 21.452 1.00 65.43 O
ANISOU 617 OG1 THR A 111 7960 8749 8152 234 540 -964 O
ATOM 618 CG2 THR A 111 -0.285 -0.897 20.751 1.00 58.46 C
ANISOU 618 CG2 THR A 111 7115 7916 7180 234 797 -919 C
ATOM 619 N LEU A 112 -1.127 -4.511 20.044 1.00 62.11 N
ANISOU 619 N LEU A 112 7558 8274 7767 351 660 -1212 N
ATOM 620 CA LEU A 112 -0.214 -5.572 19.627 1.00 60.58 C
ANISOU 620 CA LEU A 112 7362 8070 7586 412 723 -1292 C
ATOM 621 C LEU A 112 -0.537 -6.059 18.219 1.00 64.19 C
ANISOU 621 C LEU A 112 7946 8538 7907 480 700 -1402 C
ATOM 622 O LEU A 112 0.369 -6.257 17.399 1.00 64.63 O
ANISOU 622 O LEU A 112 8041 8640 7876 528 813 -1461 O
ATOM 623 CB LEU A 112 -0.268 -6.731 20.623 1.00 59.63 C
ANISOU 623 CB LEU A 112 7180 7850 7627 400 653 -1321 C
ATOM 624 CG LEU A 112 0.508 -7.994 20.241 1.00 59.03 C
ANISOU 624 CG LEU A 112 7115 7727 7586 490 657 -1434 C
ATOM 625 CD1 LEU A 112 1.992 -7.695 20.082 1.00 60.95 C
ANISOU 625 CD1 LEU A 112 7276 8044 7838 549 787 -1452 C
ATOM 626 CD2 LEU A 112 0.285 -9.095 21.266 1.00 56.41 C
ANISOU 626 CD2 LEU A 112 6796 7250 7386 465 546 -1447 C
ATOM 627 N VAL A 113 -1.824 -6.250 17.918 1.00 64.53 N
ANISOU 627 N VAL A 113 8045 8542 7930 482 557 -1453 N
ATOM 628 CA VAL A 113 -2.216 -6.726 16.593 1.00 67.18 C
ANISOU 628 CA VAL A 113 8518 8873 8133 555 500 -1566 C
ATOM 629 C VAL A 113 -1.855 -5.698 15.528 1.00 68.59 C
ANISOU 629 C VAL A 113 8863 9112 8088 579 568 -1531 C
ATOM 630 O VAL A 113 -1.380 -6.051 14.442 1.00 68.20 O
ANISOU 630 O VAL A 113 8940 9082 7891 627 636 -1605 O
ATOM 631 CB VAL A 113 -3.718 -7.071 16.569 1.00 69.04 C
ANISOU 631 CB VAL A 113 8753 9054 8423 549 311 -1651 C
ATOM 632 CG1 VAL A 113 -4.184 -7.335 15.145 1.00 70.87 C
ANISOU 632 CG1 VAL A 113 9150 9278 8499 638 217 -1765 C
ATOM 633 CG2 VAL A 113 -3.996 -8.282 17.445 1.00 61.75 C
ANISOU 633 CG2 VAL A 113 7727 8053 7682 491 278 -1702 C
ATOM 634 N VAL A 114 -2.072 -4.413 15.817 1.00 67.77 N
ANISOU 634 N VAL A 114 8786 9024 7938 536 554 -1424 N
ATOM 635 CA VAL A 114 -1.729 -3.374 14.849 1.00 67.08 C
ANISOU 635 CA VAL A 114 8916 8961 7610 532 613 -1374 C
ATOM 636 C VAL A 114 -0.220 -3.296 14.652 1.00 68.70 C
ANISOU 636 C VAL A 114 9115 9236 7753 477 872 -1350 C
ATOM 637 O VAL A 114 0.263 -3.128 13.526 1.00 72.77 O
ANISOU 637 O VAL A 114 9824 9775 8049 467 983 -1384 O
ATOM 638 CB VAL A 114 -2.316 -2.020 15.285 1.00 63.60 C
ANISOU 638 CB VAL A 114 8518 8498 7148 503 512 -1270 C
ATOM 639 CG1 VAL A 114 -1.831 -0.911 14.366 1.00 63.07 C
ANISOU 639 CG1 VAL A 114 8727 8425 6812 473 582 -1195 C
ATOM 640 CG2 VAL A 114 -3.828 -2.080 15.277 1.00 65.55 C
ANISOU 640 CG2 VAL A 114 8761 8691 7455 574 251 -1355 C
ATOM 641 N ASP A 115 0.552 -3.421 15.733 1.00 61.44 N
ANISOU 641 N ASP A 115 7974 8349 7022 436 973 -1311 N
ATOM 642 CA ASP A 115 2.003 -3.324 15.610 1.00 63.55 C
ANISOU 642 CA ASP A 115 8178 8694 7274 388 1210 -1330 C
ATOM 643 C ASP A 115 2.596 -4.538 14.906 1.00 67.17 C
ANISOU 643 C ASP A 115 8611 9181 7730 457 1293 -1495 C
ATOM 644 O ASP A 115 3.652 -4.426 14.273 1.00 68.01 O
ANISOU 644 O ASP A 115 8727 9367 7745 418 1508 -1567 O
ATOM 645 CB ASP A 115 2.638 -3.141 16.989 1.00 65.02 C
ANISOU 645 CB ASP A 115 8131 8894 7680 351 1247 -1266 C
ATOM 646 CG ASP A 115 2.374 -1.764 17.575 1.00 66.88 C
ANISOU 646 CG ASP A 115 8397 9123 7892 268 1226 -1113 C
ATOM 647 OD1 ASP A 115 1.819 -0.907 16.856 1.00 62.40 O
ANISOU 647 OD1 ASP A 115 8042 8536 7130 241 1190 -1060 O
ATOM 648 OD2 ASP A 115 2.722 -1.540 18.755 1.00 67.63 O
ANISOU 648 OD2 ASP A 115 8325 9216 8155 238 1225 -1052 O
ATOM 649 N ILE A 116 1.944 -5.697 14.999 1.00 72.42 N
ANISOU 649 N ILE A 116 9242 9780 8493 547 1137 -1574 N
ATOM 650 CA ILE A 116 2.464 -6.890 14.337 1.00 69.77 C
ANISOU 650 CA ILE A 116 8894 9455 8160 631 1188 -1742 C
ATOM 651 C ILE A 116 2.031 -6.935 12.876 1.00 74.54 C
ANISOU 651 C ILE A 116 9744 10066 8512 654 1194 -1813 C
ATOM 652 O ILE A 116 2.848 -7.168 11.977 1.00 77.09 O
ANISOU 652 O ILE A 116 10124 10455 8712 660 1369 -1928 O
ATOM 653 CB ILE A 116 2.021 -8.155 15.095 1.00 70.36 C
ANISOU 653 CB ILE A 116 8861 9430 8442 706 1013 -1796 C
ATOM 654 CG1 ILE A 116 2.811 -8.302 16.396 1.00 71.04 C
ANISOU 654 CG1 ILE A 116 8747 9498 8747 703 1027 -1764 C
ATOM 655 CG2 ILE A 116 2.190 -9.392 14.223 1.00 73.08 C
ANISOU 655 CG2 ILE A 116 9258 9754 8757 808 1002 -1973 C
ATOM 656 CD1 ILE A 116 4.283 -8.592 16.185 1.00 74.61 C
ANISOU 656 CD1 ILE A 116 9070 10023 9253 758 1188 -1897 C
ATOM 657 N THR A 117 0.745 -6.704 12.614 1.00 74.15 N
ANISOU 657 N THR A 117 9845 9948 8382 668 998 -1766 N
ATOM 658 CA THR A 117 0.175 -6.894 11.288 1.00 76.36 C
ANISOU 658 CA THR A 117 10374 10201 8436 719 930 -1847 C
ATOM 659 C THR A 117 0.081 -5.617 10.467 1.00 79.34 C
ANISOU 659 C THR A 117 11030 10586 8530 659 970 -1765 C
ATOM 660 O THR A 117 -0.064 -5.702 9.242 1.00 81.90 O
ANISOU 660 O THR A 117 11616 10891 8609 686 965 -1835 O
ATOM 661 CB THR A 117 -1.227 -7.503 11.402 1.00 77.70 C
ANISOU 661 CB THR A 117 10547 10279 8698 787 653 -1891 C
ATOM 662 OG1 THR A 117 -2.094 -6.579 12.072 1.00 77.68 O
ANISOU 662 OG1 THR A 117 10516 10247 8752 748 515 -1783 O
ATOM 663 CG2 THR A 117 -1.179 -8.801 12.191 1.00 76.42 C
ANISOU 663 CG2 THR A 117 10176 10075 8783 818 611 -1965 C
ATOM 664 N GLU A 118 0.145 -4.447 11.104 1.00 74.55 N
ANISOU 664 N GLU A 118 10406 9986 7935 577 993 -1619 N
ATOM 665 CA GLU A 118 -0.044 -3.154 10.448 1.00 74.18 C
ANISOU 665 CA GLU A 118 10662 9904 7620 517 984 -1521 C
ATOM 666 C GLU A 118 -1.424 -3.028 9.806 1.00 77.18 C
ANISOU 666 C GLU A 118 11271 10177 7878 619 677 -1548 C
ATOM 667 O GLU A 118 -1.606 -2.240 8.874 1.00 87.51 O
ANISOU 667 O GLU A 118 12933 11422 8895 608 629 -1512 O
ATOM 668 CB GLU A 118 1.054 -2.882 9.411 1.00 81.99 C
ANISOU 668 CB GLU A 118 11867 10948 8338 416 1266 -1551 C
ATOM 669 CG GLU A 118 2.455 -2.789 9.997 1.00 85.64 C
ANISOU 669 CG GLU A 118 12089 11526 8923 303 1573 -1555 C
ATOM 670 CD GLU A 118 3.519 -2.563 8.938 1.00 97.88 C
ANISOU 670 CD GLU A 118 13827 13149 10215 173 1891 -1629 C
ATOM 671 OE1 GLU A 118 3.193 -2.649 7.735 1.00100.17 O
ANISOU 671 OE1 GLU A 118 14451 13394 10216 180 1877 -1678 O
ATOM 672 OE2 GLU A 118 4.682 -2.298 9.310 1.00103.88 O
ANISOU 672 OE2 GLU A 118 14401 14011 11057 55 2159 -1654 O
ATOM 673 N THR A 119 -2.400 -3.801 10.280 1.00 81.26 N
ANISOU 673 N THR A 119 11605 10661 8609 714 461 -1624 N
ATOM 674 CA THR A 119 -3.780 -3.719 9.821 1.00 84.02 C
ANISOU 674 CA THR A 119 12089 10920 8915 820 144 -1692 C
ATOM 675 C THR A 119 -4.693 -3.693 11.039 1.00 82.95 C
ANISOU 675 C THR A 119 11665 10777 9076 831 -19 -1695 C
ATOM 676 O THR A 119 -4.297 -4.076 12.142 1.00 81.23 O
ANISOU 676 O THR A 119 11173 10609 9081 765 106 -1658 O
ATOM 677 CB THR A 119 -4.171 -4.895 8.912 1.00 88.08 C
ANISOU 677 CB THR A 119 12683 11405 9376 911 49 -1856 C
ATOM 678 OG1 THR A 119 -4.485 -6.034 9.720 1.00 92.68 O
ANISOU 678 OG1 THR A 119 12955 12004 10255 923 16 -1939 O
ATOM 679 CG2 THR A 119 -3.035 -5.257 7.970 1.00 86.82 C
ANISOU 679 CG2 THR A 119 12705 11289 8993 877 297 -1884 C
ATOM 680 N TRP A 120 -5.929 -3.236 10.838 1.00 80.85 N
ANISOU 680 N TRP A 120 11468 10443 8808 916 -306 -1759 N
ATOM 681 CA TRP A 120 -6.804 -3.030 11.988 1.00 83.57 C
ANISOU 681 CA TRP A 120 11536 10796 9422 908 -433 -1785 C
ATOM 682 C TRP A 120 -7.461 -4.332 12.453 1.00 85.30 C
ANISOU 682 C TRP A 120 11498 11026 9885 899 -483 -1931 C
ATOM 683 O TRP A 120 -7.266 -4.756 13.599 1.00 84.60 O
ANISOU 683 O TRP A 120 11163 10976 10005 802 -357 -1897 O
ATOM 684 CB TRP A 120 -7.853 -1.959 11.670 1.00 81.88 C
ANISOU 684 CB TRP A 120 11458 10509 9143 1010 -728 -1832 C
ATOM 685 CG TRP A 120 -8.759 -1.682 12.828 1.00 82.18 C
ANISOU 685 CG TRP A 120 11191 10572 9461 1000 -840 -1895 C
ATOM 686 CD1 TRP A 120 -10.122 -1.703 12.823 1.00 83.80 C
ANISOU 686 CD1 TRP A 120 11278 10752 9811 1091 -1119 -2094 C
ATOM 687 CD2 TRP A 120 -8.367 -1.373 14.173 1.00 80.83 C
ANISOU 687 CD2 TRP A 120 10784 10464 9464 884 -666 -1786 C
ATOM 688 NE1 TRP A 120 -10.604 -1.416 14.077 1.00 85.23 N
ANISOU 688 NE1 TRP A 120 11156 10986 10242 1025 -1101 -2123 N
ATOM 689 CE2 TRP A 120 -9.547 -1.211 14.924 1.00 83.57 C
ANISOU 689 CE2 TRP A 120 10889 10823 10039 899 -829 -1924 C
ATOM 690 CE3 TRP A 120 -7.134 -1.212 14.813 1.00 76.23 C
ANISOU 690 CE3 TRP A 120 10165 9929 8870 771 -393 -1606 C
ATOM 691 CZ2 TRP A 120 -9.528 -0.901 16.282 1.00 82.26 C
ANISOU 691 CZ2 TRP A 120 10482 10711 10060 795 -713 -1871 C
ATOM 692 CZ3 TRP A 120 -7.119 -0.903 16.160 1.00 72.37 C
ANISOU 692 CZ3 TRP A 120 9441 9482 8574 686 -313 -1547 C
ATOM 693 CH2 TRP A 120 -8.308 -0.747 16.879 1.00 77.42 C
ANISOU 693 CH2 TRP A 120 9877 10129 9410 694 -465 -1671 C
ATOM 694 N PHE A 121 -8.250 -4.965 11.577 1.00 83.59 N
ANISOU 694 N PHE A 121 11365 10763 9633 989 -675 -2096 N
ATOM 695 CA PHE A 121 -8.987 -6.220 11.732 1.00 84.07 C
ANISOU 695 CA PHE A 121 11243 10812 9887 977 -755 -2266 C
ATOM 696 C PHE A 121 -10.231 -6.097 12.623 1.00 83.65 C
ANISOU 696 C PHE A 121 10920 10768 10095 938 -902 -2389 C
ATOM 697 O PHE A 121 -10.982 -7.067 12.726 1.00 85.25 O
ANISOU 697 O PHE A 121 10974 10956 10461 902 -975 -2555 O
ATOM 698 CB PHE A 121 -8.125 -7.377 12.283 1.00 83.88 C
ANISOU 698 CB PHE A 121 11099 10808 9962 881 -524 -2223 C
ATOM 699 CG PHE A 121 -7.138 -7.938 11.299 1.00 84.04 C
ANISOU 699 CG PHE A 121 11321 10825 9786 933 -407 -2211 C
ATOM 700 CD1 PHE A 121 -7.473 -8.116 9.965 1.00 94.14 C
ANISOU 700 CD1 PHE A 121 12833 12063 10873 1041 -548 -2319 C
ATOM 701 CD2 PHE A 121 -5.868 -8.292 11.714 1.00 83.05 C
ANISOU 701 CD2 PHE A 121 11146 10737 9672 880 -162 -2115 C
ATOM 702 CE1 PHE A 121 -6.550 -8.644 9.064 1.00100.15 C
ANISOU 702 CE1 PHE A 121 13779 12831 11444 1077 -412 -2328 C
ATOM 703 CE2 PHE A 121 -4.944 -8.818 10.827 1.00 86.20 C
ANISOU 703 CE2 PHE A 121 11692 11150 9912 927 -36 -2146 C
ATOM 704 CZ PHE A 121 -5.283 -8.994 9.497 1.00 92.37 C
ANISOU 704 CZ PHE A 121 12709 11899 10488 1017 -145 -2251 C
ATOM 705 N PHE A 122 -10.497 -4.950 13.253 1.00 82.18 N
ANISOU 705 N PHE A 122 10661 10605 9958 934 -942 -2336 N
ATOM 706 CA PHE A 122 -11.490 -4.916 14.322 1.00 83.33 C
ANISOU 706 CA PHE A 122 10501 10786 10375 855 -995 -2457 C
ATOM 707 C PHE A 122 -12.767 -4.156 13.992 1.00 85.68 C
ANISOU 707 C PHE A 122 10749 11070 10736 979 -1302 -2655 C
ATOM 708 O PHE A 122 -13.782 -4.380 14.659 1.00 87.63 O
ANISOU 708 O PHE A 122 10710 11355 11231 916 -1363 -2846 O
ATOM 709 CB PHE A 122 -10.876 -4.328 15.602 1.00 83.25 C
ANISOU 709 CB PHE A 122 10367 10826 10441 737 -788 -2283 C
ATOM 710 CG PHE A 122 -9.777 -5.171 16.187 1.00 80.99 C
ANISOU 710 CG PHE A 122 10062 10545 10165 616 -526 -2138 C
ATOM 711 CD1 PHE A 122 -10.019 -6.480 16.570 1.00 81.05 C
ANISOU 711 CD1 PHE A 122 9955 10530 10311 514 -468 -2227 C
ATOM 712 CD2 PHE A 122 -8.505 -4.653 16.358 1.00 79.37 C
ANISOU 712 CD2 PHE A 122 9961 10357 9839 606 -353 -1931 C
ATOM 713 CE1 PHE A 122 -9.008 -7.261 17.108 1.00 81.64 C
ANISOU 713 CE1 PHE A 122 10043 10581 10395 431 -276 -2107 C
ATOM 714 CE2 PHE A 122 -7.489 -5.427 16.895 1.00 73.75 C
ANISOU 714 CE2 PHE A 122 9216 9644 9160 526 -153 -1833 C
ATOM 715 CZ PHE A 122 -7.741 -6.732 17.272 1.00 78.17 C
ANISOU 715 CZ PHE A 122 9685 10164 9851 452 -131 -1920 C
ATOM 716 N GLY A 123 -12.754 -3.273 13.006 1.00 88.24 N
ANISOU 716 N GLY A 123 11347 11333 10846 1146 -1500 -2634 N
ATOM 717 CA GLY A 123 -13.972 -2.618 12.582 1.00 90.16 C
ANISOU 717 CA GLY A 123 11575 11535 11147 1307 -1857 -2853 C
ATOM 718 C GLY A 123 -14.030 -1.159 13.018 1.00 95.37 C
ANISOU 718 C GLY A 123 12269 12181 11787 1372 -1947 -2783 C
ATOM 719 O GLY A 123 -13.314 -0.710 13.919 1.00 97.39 O
ANISOU 719 O GLY A 123 12463 12484 12056 1257 -1714 -2593 O
ATOM 720 N GLN A 124 -14.927 -0.419 12.359 1.00 90.27 N
ANISOU 720 N GLN A 124 11731 11456 11112 1574 -2324 -2956 N
ATOM 721 CA GLN A 124 -15.030 1.021 12.577 1.00 94.52 C
ANISOU 721 CA GLN A 124 12375 11941 11599 1678 -2483 -2908 C
ATOM 722 C GLN A 124 -15.491 1.350 13.993 1.00 97.48 C
ANISOU 722 C GLN A 124 12337 12423 12278 1587 -2386 -2990 C
ATOM 723 O GLN A 124 -14.981 2.290 14.612 1.00 94.58 O
ANISOU 723 O GLN A 124 12016 12055 11867 1556 -2291 -2822 O
ATOM 724 CB GLN A 124 -15.979 1.633 11.547 1.00 94.43 C
ANISOU 724 CB GLN A 124 12577 11796 11508 1943 -2967 -3118 C
ATOM 725 CG GLN A 124 -16.173 3.132 11.685 1.00 97.40 C
ANISOU 725 CG GLN A 124 13107 12077 11823 2086 -3202 -3095 C
ATOM 726 CD GLN A 124 -14.911 3.915 11.378 1.00 96.94 C
ANISOU 726 CD GLN A 124 13498 11927 11409 2028 -3042 -2743 C
ATOM 727 OE1 GLN A 124 -14.596 4.174 10.216 1.00 95.50 O
ANISOU 727 OE1 GLN A 124 13794 11598 10895 2116 -3188 -2656 O
ATOM 728 NE2 GLN A 124 -14.182 4.299 12.421 1.00 94.72 N
ANISOU 728 NE2 GLN A 124 13076 11727 11186 1864 -2733 -2549 N
ATOM 729 N SER A 125 -16.463 0.601 14.519 1.00107.96 N
ANISOU 729 N SER A 125 13268 13842 13910 1527 -2398 -3260 N
ATOM 730 CA SER A 125 -16.966 0.888 15.860 1.00105.28 C
ANISOU 730 CA SER A 125 12541 13611 13849 1417 -2282 -3371 C
ATOM 731 C SER A 125 -15.891 0.644 16.914 1.00104.40 C
ANISOU 731 C SER A 125 12386 13566 13715 1182 -1863 -3089 C
ATOM 732 O SER A 125 -15.625 1.507 17.763 1.00107.82 O
ANISOU 732 O SER A 125 12766 14025 14174 1146 -1775 -2986 O
ATOM 733 CB SER A 125 -18.207 0.041 16.147 1.00107.77 C
ANISOU 733 CB SER A 125 12456 14013 14479 1355 -2339 -3738 C
ATOM 734 OG SER A 125 -19.222 0.279 15.187 1.00111.26 O
ANISOU 734 OG SER A 125 12909 14394 14971 1593 -2762 -4035 O
ATOM 735 N LEU A 126 -15.256 -0.530 16.869 1.00 97.14 N
ANISOU 735 N LEU A 126 11499 12661 12748 1034 -1627 -2972 N
ATOM 736 CA LEU A 126 -14.186 -0.822 17.815 1.00 96.21 C
ANISOU 736 CA LEU A 126 11368 12584 12606 840 -1274 -2718 C
ATOM 737 C LEU A 126 -13.025 0.149 17.657 1.00 93.66 C
ANISOU 737 C LEU A 126 11321 12215 12050 892 -1211 -2432 C
ATOM 738 O LEU A 126 -12.335 0.452 18.636 1.00 91.34 O
ANISOU 738 O LEU A 126 10970 11957 11777 775 -997 -2262 O
ATOM 739 CB LEU A 126 -13.705 -2.265 17.648 1.00 97.53 C
ANISOU 739 CB LEU A 126 11559 12744 12752 716 -1093 -2668 C
ATOM 740 CG LEU A 126 -14.491 -3.354 18.388 1.00100.76 C
ANISOU 740 CG LEU A 126 11683 13200 13401 533 -993 -2860 C
ATOM 741 CD1 LEU A 126 -15.882 -3.554 17.796 1.00106.07 C
ANISOU 741 CD1 LEU A 126 12193 13884 14226 613 -1251 -3204 C
ATOM 742 CD2 LEU A 126 -13.717 -4.664 18.398 1.00102.56 C
ANISOU 742 CD2 LEU A 126 12003 13389 13574 406 -794 -2738 C
ATOM 743 N CYS A 127 -12.801 0.664 16.445 1.00 90.00 N
ANISOU 743 N CYS A 127 11174 11664 11356 1054 -1395 -2382 N
ATOM 744 CA CYS A 127 -11.747 1.656 16.272 1.00 91.83 C
ANISOU 744 CA CYS A 127 11686 11846 11359 1070 -1323 -2129 C
ATOM 745 C CYS A 127 -12.128 3.000 16.880 1.00 89.50 C
ANISOU 745 C CYS A 127 11351 11534 11121 1132 -1454 -2137 C
ATOM 746 O CYS A 127 -11.289 3.673 17.484 1.00 87.03 O
ANISOU 746 O CYS A 127 11090 11227 10751 1053 -1287 -1934 O
ATOM 747 CB CYS A 127 -11.406 1.835 14.801 1.00 90.57 C
ANISOU 747 CB CYS A 127 11929 11583 10900 1190 -1459 -2074 C
ATOM 748 SG CYS A 127 -10.257 3.198 14.598 1.00 91.92 S
ANISOU 748 SG CYS A 127 12460 11679 10788 1172 -1372 -1795 S
ATOM 749 N LYS A 128 -13.374 3.431 16.705 1.00 89.59 N
ANISOU 749 N LYS A 128 11271 11519 11252 1285 -1770 -2387 N
ATOM 750 CA LYS A 128 -13.785 4.667 17.355 1.00 83.50 C
ANISOU 750 CA LYS A 128 10429 10732 10565 1358 -1905 -2430 C
ATOM 751 C LYS A 128 -13.823 4.518 18.869 1.00 80.32 C
ANISOU 751 C LYS A 128 9658 10457 10402 1185 -1655 -2442 C
ATOM 752 O LYS A 128 -13.796 5.528 19.580 1.00 78.94 O
ANISOU 752 O LYS A 128 9445 10281 10268 1199 -1668 -2403 O
ATOM 753 CB LYS A 128 -15.143 5.126 16.826 1.00 87.50 C
ANISOU 753 CB LYS A 128 10891 11181 11175 1588 -2331 -2747 C
ATOM 754 CG LYS A 128 -15.069 5.813 15.471 1.00 87.47 C
ANISOU 754 CG LYS A 128 11359 10995 10880 1794 -2652 -2698 C
ATOM 755 CD LYS A 128 -16.399 6.439 15.091 1.00 89.17 C
ANISOU 755 CD LYS A 128 11532 11131 11217 2058 -3130 -3025 C
ATOM 756 CE LYS A 128 -16.296 7.198 13.778 1.00 90.82 C
ANISOU 756 CE LYS A 128 12295 11117 11097 2265 -3482 -2957 C
ATOM 757 NZ LYS A 128 -15.310 8.311 13.856 1.00 85.64 N
ANISOU 757 NZ LYS A 128 12008 10351 10180 2218 -3395 -2646 N
ATOM 758 N VAL A 129 -13.874 3.288 19.372 1.00 83.11 N
ANISOU 758 N VAL A 129 9779 10903 10897 1018 -1433 -2492 N
ATOM 759 CA VAL A 129 -13.897 3.061 20.817 1.00 77.86 C
ANISOU 759 CA VAL A 129 8823 10338 10422 827 -1184 -2495 C
ATOM 760 C VAL A 129 -12.490 2.991 21.409 1.00 74.97 C
ANISOU 760 C VAL A 129 8578 9972 9935 683 -890 -2174 C
ATOM 761 O VAL A 129 -12.198 3.653 22.409 1.00 72.06 O
ANISOU 761 O VAL A 129 8139 9630 9611 616 -783 -2085 O
ATOM 762 CB VAL A 129 -14.706 1.787 21.138 1.00 79.01 C
ANISOU 762 CB VAL A 129 8691 10558 10771 692 -1097 -2720 C
ATOM 763 CG1 VAL A 129 -14.488 1.372 22.583 1.00 73.45 C
ANISOU 763 CG1 VAL A 129 7796 9926 10187 449 -789 -2663 C
ATOM 764 CG2 VAL A 129 -16.184 2.021 20.878 1.00 81.67 C
ANISOU 764 CG2 VAL A 129 8802 10926 11303 812 -1367 -3096 C
ATOM 765 N ILE A 130 -11.591 2.203 20.820 1.00 72.61 N
ANISOU 765 N ILE A 130 8451 9644 9494 642 -767 -2019 N
ATOM 766 CA ILE A 130 -10.364 1.800 21.513 1.00 68.80 C
ANISOU 766 CA ILE A 130 7994 9176 8969 493 -486 -1789 C
ATOM 767 C ILE A 130 -9.361 2.947 21.649 1.00 66.68 C
ANISOU 767 C ILE A 130 7891 8880 8563 513 -434 -1569 C
ATOM 768 O ILE A 130 -8.898 3.198 22.772 1.00 64.35 O
ANISOU 768 O ILE A 130 7498 8614 8338 409 -284 -1467 O
ATOM 769 CB ILE A 130 -9.731 0.568 20.839 1.00 67.96 C
ANISOU 769 CB ILE A 130 7992 9051 8780 461 -385 -1737 C
ATOM 770 CG1 ILE A 130 -10.610 -0.666 21.045 1.00 70.92 C
ANISOU 770 CG1 ILE A 130 8186 9446 9316 379 -382 -1931 C
ATOM 771 CG2 ILE A 130 -8.326 0.324 21.373 1.00 66.11 C
ANISOU 771 CG2 ILE A 130 7812 8817 8488 362 -149 -1515 C
ATOM 772 CD1 ILE A 130 -10.086 -1.905 20.355 1.00 74.13 C
ANISOU 772 CD1 ILE A 130 8698 9817 9649 366 -317 -1905 C
ATOM 773 N PRO A 131 -8.962 3.654 20.577 1.00 68.38 N
ANISOU 773 N PRO A 131 8378 9030 8575 624 -543 -1486 N
ATOM 774 CA PRO A 131 -8.118 4.844 20.790 1.00 67.52 C
ANISOU 774 CA PRO A 131 8419 8886 8348 612 -492 -1297 C
ATOM 775 C PRO A 131 -8.753 5.889 21.689 1.00 66.31 C
ANISOU 775 C PRO A 131 8145 8734 8314 641 -599 -1350 C
ATOM 776 O PRO A 131 -8.043 6.559 22.450 1.00 66.64 O
ANISOU 776 O PRO A 131 8188 8780 8353 568 -481 -1201 O
ATOM 777 CB PRO A 131 -7.907 5.376 19.367 1.00 67.13 C
ANISOU 777 CB PRO A 131 8720 8742 8043 716 -628 -1251 C
ATOM 778 CG PRO A 131 -7.955 4.177 18.529 1.00 65.87 C
ANISOU 778 CG PRO A 131 8592 8596 7839 729 -608 -1327 C
ATOM 779 CD PRO A 131 -8.971 3.266 19.155 1.00 67.89 C
ANISOU 779 CD PRO A 131 8538 8915 8342 719 -651 -1522 C
ATOM 780 N TYR A 132 -10.075 6.056 21.613 1.00 63.68 N
ANISOU 780 N TYR A 132 7696 8401 8098 752 -830 -1582 N
ATOM 781 CA TYR A 132 -10.754 6.988 22.507 1.00 63.46 C
ANISOU 781 CA TYR A 132 7511 8388 8212 789 -931 -1683 C
ATOM 782 C TYR A 132 -10.522 6.608 23.963 1.00 63.08 C
ANISOU 782 C TYR A 132 7211 8435 8323 611 -677 -1648 C
ATOM 783 O TYR A 132 -10.118 7.444 24.779 1.00 65.58 O
ANISOU 783 O TYR A 132 7520 8749 8648 574 -617 -1544 O
ATOM 784 CB TYR A 132 -12.249 7.022 22.188 1.00 66.44 C
ANISOU 784 CB TYR A 132 7738 8772 8734 937 -1209 -2003 C
ATOM 785 CG TYR A 132 -13.075 7.793 23.191 1.00 63.88 C
ANISOU 785 CG TYR A 132 7170 8495 8607 969 -1289 -2181 C
ATOM 786 CD1 TYR A 132 -13.114 9.181 23.166 1.00 64.39 C
ANISOU 786 CD1 TYR A 132 7379 8473 8611 1111 -1492 -2159 C
ATOM 787 CD2 TYR A 132 -13.820 7.134 24.161 1.00 61.99 C
ANISOU 787 CD2 TYR A 132 6570 8380 8604 845 -1153 -2385 C
ATOM 788 CE1 TYR A 132 -13.869 9.891 24.080 1.00 65.55 C
ANISOU 788 CE1 TYR A 132 7293 8666 8946 1155 -1569 -2347 C
ATOM 789 CE2 TYR A 132 -14.577 7.835 25.080 1.00 63.79 C
ANISOU 789 CE2 TYR A 132 6563 8666 9010 862 -1198 -2577 C
ATOM 790 CZ TYR A 132 -14.598 9.214 25.034 1.00 64.97 C
ANISOU 790 CZ TYR A 132 6835 8739 9113 1031 -1412 -2565 C
ATOM 791 OH TYR A 132 -15.350 9.918 25.945 1.00 63.93 O
ANISOU 791 OH TYR A 132 6458 8667 9166 1063 -1462 -2780 O
ATOM 792 N LEU A 133 -10.758 5.338 24.300 1.00 61.86 N
ANISOU 792 N LEU A 133 6881 8346 8279 492 -532 -1729 N
ATOM 793 CA LEU A 133 -10.545 4.881 25.670 1.00 64.47 C
ANISOU 793 CA LEU A 133 7037 8735 8723 307 -300 -1691 C
ATOM 794 C LEU A 133 -9.079 4.991 26.067 1.00 65.13 C
ANISOU 794 C LEU A 133 7261 8789 8695 230 -123 -1409 C
ATOM 795 O LEU A 133 -8.764 5.352 27.206 1.00 68.83 O
ANISOU 795 O LEU A 133 7664 9275 9214 139 -11 -1336 O
ATOM 796 CB LEU A 133 -11.040 3.443 25.827 1.00 61.82 C
ANISOU 796 CB LEU A 133 6562 8438 8490 181 -193 -1821 C
ATOM 797 CG LEU A 133 -12.550 3.219 25.712 1.00 59.58 C
ANISOU 797 CG LEU A 133 6056 8208 8374 199 -318 -2148 C
ATOM 798 CD1 LEU A 133 -12.884 1.750 25.904 1.00 56.93 C
ANISOU 798 CD1 LEU A 133 5620 7892 8118 28 -175 -2245 C
ATOM 799 CD2 LEU A 133 -13.301 4.078 26.719 1.00 58.43 C
ANISOU 799 CD2 LEU A 133 5705 8126 8371 175 -324 -2304 C
ATOM 800 N GLN A 134 -8.168 4.684 25.142 1.00 62.16 N
ANISOU 800 N GLN A 134 7073 8372 8172 263 -95 -1270 N
ATOM 801 CA GLN A 134 -6.744 4.737 25.457 1.00 63.18 C
ANISOU 801 CA GLN A 134 7296 8486 8224 193 73 -1048 C
ATOM 802 C GLN A 134 -6.310 6.158 25.800 1.00 64.55 C
ANISOU 802 C GLN A 134 7545 8635 8347 215 45 -934 C
ATOM 803 O GLN A 134 -5.642 6.388 26.817 1.00 66.00 O
ANISOU 803 O GLN A 134 7674 8828 8574 129 164 -827 O
ATOM 804 CB GLN A 134 -5.935 4.182 24.284 1.00 62.49 C
ANISOU 804 CB GLN A 134 7373 8375 7995 227 114 -975 C
ATOM 805 CG GLN A 134 -4.518 3.767 24.641 1.00 60.49 C
ANISOU 805 CG GLN A 134 7135 8127 7722 145 307 -823 C
ATOM 806 CD GLN A 134 -3.489 4.807 24.251 1.00 59.18 C
ANISOU 806 CD GLN A 134 7115 7946 7427 148 358 -680 C
ATOM 807 OE1 GLN A 134 -3.631 5.485 23.234 1.00 59.50 O
ANISOU 807 OE1 GLN A 134 7337 7952 7319 209 272 -675 O
ATOM 808 NE2 GLN A 134 -2.446 4.938 25.060 1.00 59.07 N
ANISOU 808 NE2 GLN A 134 7040 7944 7460 71 491 -571 N
ATOM 809 N THR A 135 -6.695 7.130 24.969 1.00 57.87 N
ANISOU 809 N THR A 135 6846 7739 7401 334 -135 -960 N
ATOM 810 CA THR A 135 -6.347 8.521 25.246 1.00 60.99 C
ANISOU 810 CA THR A 135 7349 8085 7739 354 -186 -857 C
ATOM 811 C THR A 135 -7.034 9.028 26.511 1.00 63.71 C
ANISOU 811 C THR A 135 7498 8464 8245 343 -219 -946 C
ATOM 812 O THR A 135 -6.419 9.747 27.312 1.00 64.39 O
ANISOU 812 O THR A 135 7588 8539 8338 286 -150 -828 O
ATOM 813 CB THR A 135 -6.705 9.401 24.049 1.00 60.72 C
ANISOU 813 CB THR A 135 7574 7955 7543 490 -408 -876 C
ATOM 814 OG1 THR A 135 -8.093 9.239 23.730 1.00 61.64 O
ANISOU 814 OG1 THR A 135 7604 8071 7744 622 -633 -1108 O
ATOM 815 CG2 THR A 135 -5.863 9.024 22.839 1.00 59.57 C
ANISOU 815 CG2 THR A 135 7667 7773 7195 466 -329 -768 C
ATOM 816 N VAL A 136 -8.307 8.665 26.708 1.00 62.93 N
ANISOU 816 N VAL A 136 7216 8411 8282 386 -316 -1173 N
ATOM 817 CA VAL A 136 -9.021 9.076 27.913 1.00 65.39 C
ANISOU 817 CA VAL A 136 7320 8773 8751 355 -314 -1299 C
ATOM 818 C VAL A 136 -8.302 8.566 29.151 1.00 67.53 C
ANISOU 818 C VAL A 136 7505 9085 9069 177 -69 -1179 C
ATOM 819 O VAL A 136 -8.111 9.303 30.124 1.00 68.84 O
ANISOU 819 O VAL A 136 7636 9252 9267 139 -31 -1134 O
ATOM 820 CB VAL A 136 -10.481 8.584 27.867 1.00 64.55 C
ANISOU 820 CB VAL A 136 6996 8730 8800 396 -414 -1604 C
ATOM 821 CG1 VAL A 136 -11.093 8.593 29.260 1.00 65.66 C
ANISOU 821 CG1 VAL A 136 6890 8955 9105 281 -295 -1745 C
ATOM 822 CG2 VAL A 136 -11.305 9.444 26.928 1.00 64.78 C
ANISOU 822 CG2 VAL A 136 7094 8704 8817 614 -729 -1763 C
ATOM 823 N SER A 137 -7.876 7.303 29.128 1.00 68.32 N
ANISOU 823 N SER A 137 7594 9200 9162 76 77 -1130 N
ATOM 824 CA ASER A 137 -7.206 6.727 30.288 0.47 68.47 C
ANISOU 824 CA ASER A 137 7576 9226 9213 -77 267 -1025 C
ATOM 825 CA BSER A 137 -7.206 6.725 30.287 0.53 68.63 C
ANISOU 825 CA BSER A 137 7596 9246 9234 -77 267 -1025 C
ATOM 826 C SER A 137 -5.811 7.304 30.483 1.00 67.62 C
ANISOU 826 C SER A 137 7594 9075 9024 -83 322 -799 C
ATOM 827 O SER A 137 -5.352 7.427 31.621 1.00 66.51 O
ANISOU 827 O SER A 137 7427 8927 8916 -169 409 -726 O
ATOM 828 CB ASER A 137 -7.141 5.208 30.154 0.47 73.76 C
ANISOU 828 CB ASER A 137 8235 9894 9896 -164 367 -1046 C
ATOM 829 CB BSER A 137 -7.137 5.208 30.147 0.53 74.66 C
ANISOU 829 CB BSER A 137 8350 10008 10010 -163 367 -1045 C
ATOM 830 OG ASER A 137 -8.439 4.644 30.103 0.47 70.47 O
ANISOU 830 OG ASER A 137 7683 9520 9572 -199 341 -1270 O
ATOM 831 OG BSER A 137 -8.433 4.648 30.026 0.53 75.49 O
ANISOU 831 OG BSER A 137 8324 10155 10204 -191 334 -1270 O
ATOM 832 N VAL A 138 -5.116 7.652 29.398 1.00 64.64 N
ANISOU 832 N VAL A 138 7358 8665 8537 -7 279 -700 N
ATOM 833 CA VAL A 138 -3.812 8.298 29.544 1.00 64.65 C
ANISOU 833 CA VAL A 138 7454 8635 8476 -34 345 -519 C
ATOM 834 C VAL A 138 -3.971 9.643 30.243 1.00 67.04 C
ANISOU 834 C VAL A 138 7762 8917 8796 -21 277 -495 C
ATOM 835 O VAL A 138 -3.231 9.975 31.183 1.00 66.67 O
ANISOU 835 O VAL A 138 7693 8860 8779 -89 351 -397 O
ATOM 836 CB VAL A 138 -3.129 8.448 28.173 1.00 62.42 C
ANISOU 836 CB VAL A 138 7337 8326 8053 11 343 -447 C
ATOM 837 CG1 VAL A 138 -1.970 9.429 28.259 1.00 58.99 C
ANISOU 837 CG1 VAL A 138 6997 7860 7556 -36 405 -296 C
ATOM 838 CG2 VAL A 138 -2.643 7.097 27.678 1.00 60.71 C
ANISOU 838 CG2 VAL A 138 7101 8133 7831 -12 444 -456 C
ATOM 839 N SER A 139 -4.956 10.431 29.802 1.00 64.55 N
ANISOU 839 N SER A 139 7476 8583 8466 81 111 -601 N
ATOM 840 CA SER A 139 -5.245 11.698 30.466 1.00 61.67 C
ANISOU 840 CA SER A 139 7113 8191 8130 116 18 -612 C
ATOM 841 C SER A 139 -5.650 11.475 31.919 1.00 61.43 C
ANISOU 841 C SER A 139 6896 8215 8228 36 101 -688 C
ATOM 842 O SER A 139 -5.213 12.210 32.816 1.00 60.40 O
ANISOU 842 O SER A 139 6771 8066 8113 -2 127 -614 O
ATOM 843 CB SER A 139 -6.344 12.443 29.707 1.00 61.33 C
ANISOU 843 CB SER A 139 7129 8106 8067 272 -218 -759 C
ATOM 844 OG SER A 139 -6.700 13.649 30.362 1.00 66.01 O
ANISOU 844 OG SER A 139 7715 8664 8701 327 -333 -801 O
ATOM 845 N VAL A 140 -6.476 10.455 32.170 1.00 66.27 N
ANISOU 845 N VAL A 140 7365 8892 8924 -9 155 -840 N
ATOM 846 CA VAL A 140 -6.923 10.156 33.527 1.00 67.98 C
ANISOU 846 CA VAL A 140 7443 9156 9232 -124 266 -926 C
ATOM 847 C VAL A 140 -5.736 9.826 34.418 1.00 65.20 C
ANISOU 847 C VAL A 140 7159 8769 8846 -240 405 -738 C
ATOM 848 O VAL A 140 -5.638 10.313 35.547 1.00 64.89 O
ANISOU 848 O VAL A 140 7103 8725 8827 -298 446 -721 O
ATOM 849 CB VAL A 140 -7.952 9.009 33.510 1.00 65.76 C
ANISOU 849 CB VAL A 140 7026 8935 9027 -192 326 -1120 C
ATOM 850 CG1 VAL A 140 -8.046 8.358 34.878 1.00 64.41 C
ANISOU 850 CG1 VAL A 140 6799 8783 8889 -381 508 -1144 C
ATOM 851 CG2 VAL A 140 -9.313 9.523 33.078 1.00 66.17 C
ANISOU 851 CG2 VAL A 140 6937 9037 9169 -83 178 -1380 C
ATOM 852 N SER A 141 -4.813 9.002 33.923 1.00 66.43 N
ANISOU 852 N SER A 141 7391 8895 8952 -261 462 -614 N
ATOM 853 CA SER A 141 -3.654 8.612 34.717 1.00 67.64 C
ANISOU 853 CA SER A 141 7601 9006 9095 -341 552 -468 C
ATOM 854 C SER A 141 -2.756 9.808 35.008 1.00 65.44 C
ANISOU 854 C SER A 141 7373 8695 8795 -313 517 -341 C
ATOM 855 O SER A 141 -2.316 10.005 36.150 1.00 66.79 O
ANISOU 855 O SER A 141 7552 8839 8986 -374 548 -287 O
ATOM 856 CB SER A 141 -2.871 7.515 33.994 1.00 69.35 C
ANISOU 856 CB SER A 141 7865 9201 9284 -336 593 -405 C
ATOM 857 OG SER A 141 -3.690 6.387 33.742 1.00 72.02 O
ANISOU 857 OG SER A 141 8171 9553 9640 -372 619 -521 O
ATOM 858 N VAL A 142 -2.477 10.628 33.991 1.00 59.11 N
ANISOU 858 N VAL A 142 6633 7885 7943 -233 449 -295 N
ATOM 859 CA VAL A 142 -1.554 11.736 34.215 1.00 58.62 C
ANISOU 859 CA VAL A 142 6634 7781 7858 -238 432 -173 C
ATOM 860 C VAL A 142 -2.169 12.764 35.161 1.00 56.20 C
ANISOU 860 C VAL A 142 6305 7463 7585 -229 363 -218 C
ATOM 861 O VAL A 142 -1.493 13.282 36.061 1.00 53.13 O
ANISOU 861 O VAL A 142 5928 7045 7216 -274 380 -140 O
ATOM 862 CB VAL A 142 -1.104 12.361 32.879 1.00 57.56 C
ANISOU 862 CB VAL A 142 6622 7619 7628 -194 397 -110 C
ATOM 863 CG1 VAL A 142 -2.231 13.126 32.196 1.00 56.10 C
ANISOU 863 CG1 VAL A 142 6512 7411 7393 -94 246 -198 C
ATOM 864 CG2 VAL A 142 0.107 13.253 33.105 1.00 52.91 C
ANISOU 864 CG2 VAL A 142 6092 6989 7023 -252 433 19 C
ATOM 865 N TRP A 143 -3.468 13.041 35.020 1.00 51.79 N
ANISOU 865 N TRP A 143 5701 6931 7047 -164 279 -370 N
ATOM 866 CA TRP A 143 -4.091 14.001 35.918 1.00 50.30 C
ANISOU 866 CA TRP A 143 5469 6740 6903 -143 216 -452 C
ATOM 867 C TRP A 143 -4.373 13.418 37.297 1.00 49.11 C
ANISOU 867 C TRP A 143 5223 6630 6806 -251 332 -515 C
ATOM 868 O TRP A 143 -4.440 14.174 38.267 1.00 51.84 O
ANISOU 868 O TRP A 143 5561 6965 7170 -268 322 -532 O
ATOM 869 CB TRP A 143 -5.365 14.562 35.286 1.00 49.58 C
ANISOU 869 CB TRP A 143 5342 6662 6836 -14 60 -635 C
ATOM 870 CG TRP A 143 -5.052 15.497 34.156 1.00 52.37 C
ANISOU 870 CG TRP A 143 5874 6926 7098 91 -93 -553 C
ATOM 871 CD1 TRP A 143 -5.334 15.313 32.834 1.00 53.04 C
ANISOU 871 CD1 TRP A 143 6053 6985 7116 174 -189 -579 C
ATOM 872 CD2 TRP A 143 -4.358 16.749 34.248 1.00 55.13 C
ANISOU 872 CD2 TRP A 143 6375 7182 7390 103 -166 -426 C
ATOM 873 NE1 TRP A 143 -4.875 16.381 32.099 1.00 54.51 N
ANISOU 873 NE1 TRP A 143 6469 7058 7185 228 -312 -470 N
ATOM 874 CE2 TRP A 143 -4.272 17.275 32.943 1.00 56.78 C
ANISOU 874 CE2 TRP A 143 6791 7302 7482 179 -295 -375 C
ATOM 875 CE3 TRP A 143 -3.810 17.480 35.308 1.00 51.82 C
ANISOU 875 CE3 TRP A 143 5958 6735 6997 49 -138 -353 C
ATOM 876 CZ2 TRP A 143 -3.660 18.498 32.670 1.00 55.03 C
ANISOU 876 CZ2 TRP A 143 6789 6958 7163 180 -383 -251 C
ATOM 877 CZ3 TRP A 143 -3.202 18.694 35.034 1.00 50.36 C
ANISOU 877 CZ3 TRP A 143 5957 6440 6740 64 -233 -238 C
ATOM 878 CH2 TRP A 143 -3.132 19.190 33.726 1.00 53.22 C
ANISOU 878 CH2 TRP A 143 6535 6708 6980 119 -347 -185 C
ATOM 879 N THR A 144 -4.492 12.095 37.420 1.00 52.69 N
ANISOU 879 N THR A 144 5641 7112 7266 -338 443 -543 N
ATOM 880 CA THR A 144 -4.567 11.482 38.741 1.00 52.75 C
ANISOU 880 CA THR A 144 5644 7121 7278 -474 563 -565 C
ATOM 881 C THR A 144 -3.235 11.598 39.470 1.00 51.07 C
ANISOU 881 C THR A 144 5540 6833 7029 -512 573 -382 C
ATOM 882 O THR A 144 -3.198 11.889 40.673 1.00 51.27 O
ANISOU 882 O THR A 144 5602 6836 7043 -579 603 -381 O
ATOM 883 CB THR A 144 -4.991 10.019 38.608 1.00 54.02 C
ANISOU 883 CB THR A 144 5790 7299 7437 -566 662 -631 C
ATOM 884 OG1 THR A 144 -6.271 9.948 37.967 1.00 55.32 O
ANISOU 884 OG1 THR A 144 5822 7539 7657 -533 643 -833 O
ATOM 885 CG2 THR A 144 -5.079 9.362 39.970 1.00 52.68 C
ANISOU 885 CG2 THR A 144 5686 7099 7232 -734 787 -645 C
ATOM 886 N LEU A 145 -2.128 11.384 38.755 1.00 47.19 N
ANISOU 886 N LEU A 145 5097 6307 6528 -470 547 -247 N
ATOM 887 CA LEU A 145 -0.817 11.633 39.345 1.00 48.01 C
ANISOU 887 CA LEU A 145 5262 6347 6631 -485 530 -109 C
ATOM 888 C LEU A 145 -0.666 13.100 39.735 1.00 48.80 C
ANISOU 888 C LEU A 145 5370 6432 6738 -456 463 -79 C
ATOM 889 O LEU A 145 -0.108 13.420 40.795 1.00 48.79 O
ANISOU 889 O LEU A 145 5412 6385 6743 -494 448 -28 O
ATOM 890 CB LEU A 145 0.284 11.215 38.370 1.00 48.70 C
ANISOU 890 CB LEU A 145 5351 6424 6728 -446 530 -23 C
ATOM 891 CG LEU A 145 0.368 9.726 38.032 1.00 47.27 C
ANISOU 891 CG LEU A 145 5176 6237 6547 -459 576 -46 C
ATOM 892 CD1 LEU A 145 1.376 9.496 36.919 1.00 47.32 C
ANISOU 892 CD1 LEU A 145 5157 6256 6568 -407 587 1 C
ATOM 893 CD2 LEU A 145 0.733 8.913 39.265 1.00 40.09 C
ANISOU 893 CD2 LEU A 145 4343 5251 5638 -522 574 -26 C
ATOM 894 N SER A 146 -1.165 14.006 38.890 1.00 46.19 N
ANISOU 894 N SER A 146 5027 6123 6402 -381 399 -114 N
ATOM 895 CA SER A 146 -1.131 15.427 39.222 1.00 45.48 C
ANISOU 895 CA SER A 146 4972 5997 6314 -346 313 -97 C
ATOM 896 C SER A 146 -1.954 15.726 40.471 1.00 47.90 C
ANISOU 896 C SER A 146 5242 6319 6638 -369 317 -207 C
ATOM 897 O SER A 146 -1.557 16.551 41.300 1.00 47.83 O
ANISOU 897 O SER A 146 5272 6267 6632 -381 279 -167 O
ATOM 898 CB SER A 146 -1.629 16.253 38.037 1.00 46.07 C
ANISOU 898 CB SER A 146 5089 6059 6357 -250 211 -127 C
ATOM 899 OG SER A 146 -0.813 16.045 36.898 1.00 50.13 O
ANISOU 899 OG SER A 146 5670 6554 6822 -257 235 -24 O
ATOM 900 N ALA A 147 -3.111 15.076 40.614 1.00 49.52 N
ANISOU 900 N ALA A 147 5368 6590 6857 -389 375 -365 N
ATOM 901 CA ALA A 147 -3.935 15.264 41.804 1.00 46.90 C
ANISOU 901 CA ALA A 147 4992 6291 6536 -445 426 -504 C
ATOM 902 C ALA A 147 -3.224 14.759 43.052 1.00 47.81 C
ANISOU 902 C ALA A 147 5208 6358 6601 -568 509 -413 C
ATOM 903 O ALA A 147 -3.302 15.385 44.116 1.00 51.06 O
ANISOU 903 O ALA A 147 5654 6753 6994 -600 513 -444 O
ATOM 904 CB ALA A 147 -5.279 14.559 41.630 1.00 47.49 C
ANISOU 904 CB ALA A 147 4943 6456 6645 -477 504 -718 C
ATOM 905 N ILE A 148 -2.538 13.617 42.944 1.00 48.43 N
ANISOU 905 N ILE A 148 5352 6399 6651 -625 557 -312 N
ATOM 906 CA ILE A 148 -1.741 13.121 44.065 1.00 45.91 C
ANISOU 906 CA ILE A 148 5170 5997 6276 -711 577 -218 C
ATOM 907 C ILE A 148 -0.694 14.151 44.459 1.00 47.11 C
ANISOU 907 C ILE A 148 5363 6090 6448 -657 469 -106 C
ATOM 908 O ILE A 148 -0.517 14.468 45.642 1.00 50.76 O
ANISOU 908 O ILE A 148 5918 6502 6868 -705 456 -97 O
ATOM 909 CB ILE A 148 -1.079 11.778 43.711 1.00 46.11 C
ANISOU 909 CB ILE A 148 5260 5972 6287 -736 591 -138 C
ATOM 910 CG1 ILE A 148 -2.128 10.724 43.388 1.00 47.63 C
ANISOU 910 CG1 ILE A 148 5431 6209 6456 -813 700 -252 C
ATOM 911 CG2 ILE A 148 -0.197 11.309 44.854 1.00 46.46 C
ANISOU 911 CG2 ILE A 148 5477 5899 6275 -791 551 -50 C
ATOM 912 CD1 ILE A 148 -1.542 9.377 43.036 1.00 48.25 C
ANISOU 912 CD1 ILE A 148 5592 6222 6517 -830 699 -185 C
ATOM 913 N ALA A 149 0.018 14.684 43.463 1.00 48.18 N
ANISOU 913 N ALA A 149 5443 6225 6639 -571 397 -25 N
ATOM 914 CA ALA A 149 1.054 15.672 43.741 1.00 45.70 C
ANISOU 914 CA ALA A 149 5153 5854 6356 -544 307 70 C
ATOM 915 C ALA A 149 0.468 16.915 44.399 1.00 49.85 C
ANISOU 915 C ALA A 149 5693 6376 6871 -529 262 12 C
ATOM 916 O ALA A 149 1.041 17.449 45.354 1.00 49.45 O
ANISOU 916 O ALA A 149 5705 6266 6818 -548 208 53 O
ATOM 917 CB ALA A 149 1.784 16.041 42.451 1.00 45.58 C
ANISOU 917 CB ALA A 149 5089 5846 6384 -498 281 143 C
ATOM 918 N LEU A 150 -0.677 17.386 43.900 1.00 48.02 N
ANISOU 918 N LEU A 150 5402 6202 6643 -479 263 -103 N
ATOM 919 CA LEU A 150 -1.302 18.582 44.457 1.00 49.30 C
ANISOU 919 CA LEU A 150 5562 6359 6810 -436 201 -194 C
ATOM 920 C LEU A 150 -1.751 18.355 45.894 1.00 51.53 C
ANISOU 920 C LEU A 150 5878 6654 7049 -518 277 -283 C
ATOM 921 O LEU A 150 -1.573 19.227 46.753 1.00 50.87 O
ANISOU 921 O LEU A 150 5847 6528 6954 -513 224 -287 O
ATOM 922 CB LEU A 150 -2.487 19.006 43.590 1.00 47.09 C
ANISOU 922 CB LEU A 150 5199 6134 6559 -339 155 -340 C
ATOM 923 CG LEU A 150 -3.106 20.363 43.924 1.00 52.09 C
ANISOU 923 CG LEU A 150 5828 6747 7218 -248 40 -454 C
ATOM 924 CD1 LEU A 150 -2.205 21.488 43.441 1.00 51.48 C
ANISOU 924 CD1 LEU A 150 5867 6560 7135 -196 -101 -306 C
ATOM 925 CD2 LEU A 150 -4.501 20.485 43.329 1.00 56.39 C
ANISOU 925 CD2 LEU A 150 6255 7359 7811 -145 -7 -675 C
ATOM 926 N ASP A 151 -2.346 17.193 46.175 1.00 54.23 N
ANISOU 926 N ASP A 151 6212 7043 7350 -609 410 -359 N
ATOM 927 CA ASP A 151 -2.775 16.904 47.538 1.00 54.35 C
ANISOU 927 CA ASP A 151 6308 7057 7285 -729 515 -443 C
ATOM 928 C ASP A 151 -1.585 16.805 48.482 1.00 57.49 C
ANISOU 928 C ASP A 151 6885 7340 7618 -775 459 -288 C
ATOM 929 O ASP A 151 -1.638 17.306 49.612 1.00 59.09 O
ANISOU 929 O ASP A 151 7184 7510 7758 -818 462 -325 O
ATOM 930 CB ASP A 151 -3.596 15.618 47.575 1.00 54.46 C
ANISOU 930 CB ASP A 151 6315 7125 7252 -854 681 -546 C
ATOM 931 CG ASP A 151 -4.039 15.261 48.976 1.00 62.40 C
ANISOU 931 CG ASP A 151 7456 8117 8138 -1024 824 -632 C
ATOM 932 OD1 ASP A 151 -4.717 16.096 49.609 1.00 69.83 O
ANISOU 932 OD1 ASP A 151 8346 9110 9077 -1033 866 -784 O
ATOM 933 OD2 ASP A 151 -3.704 14.154 49.448 1.00 62.75 O
ANISOU 933 OD2 ASP A 151 7680 8085 8076 -1150 890 -555 O
ATOM 934 N ARG A 152 -0.500 16.165 48.038 1.00 53.98 N
ANISOU 934 N ARG A 152 6484 6832 7192 -755 396 -137 N
ATOM 935 CA ARG A 152 0.690 16.081 48.879 1.00 52.97 C
ANISOU 935 CA ARG A 152 6503 6590 7035 -768 297 -18 C
ATOM 936 C ARG A 152 1.303 17.458 49.108 1.00 52.73 C
ANISOU 936 C ARG A 152 6448 6527 7061 -698 174 23 C
ATOM 937 O ARG A 152 1.790 17.752 50.205 1.00 49.72 O
ANISOU 937 O ARG A 152 6193 6064 6632 -721 104 48 O
ATOM 938 CB ARG A 152 1.706 15.123 48.257 1.00 45.18 C
ANISOU 938 CB ARG A 152 5518 5554 6093 -738 241 87 C
ATOM 939 CG ARG A 152 1.217 13.685 48.141 1.00 46.54 C
ANISOU 939 CG ARG A 152 5762 5722 6198 -810 337 58 C
ATOM 940 CD ARG A 152 1.521 12.854 49.385 1.00 45.29 C
ANISOU 940 CD ARG A 152 5863 5430 5913 -895 305 88 C
ATOM 941 NE ARG A 152 0.920 13.395 50.599 1.00 45.92 N
ANISOU 941 NE ARG A 152 6080 5492 5875 -988 359 28 N
ATOM 942 CZ ARG A 152 -0.349 13.231 50.945 1.00 51.26 C
ANISOU 942 CZ ARG A 152 6786 6232 6458 -1118 542 -97 C
ATOM 943 NH1 ARG A 152 -1.194 12.562 50.178 1.00 56.64 N
ANISOU 943 NH1 ARG A 152 7361 6998 7160 -1168 675 -176 N
ATOM 944 NH2 ARG A 152 -0.782 13.752 52.090 1.00 51.49 N
ANISOU 944 NH2 ARG A 152 6943 6244 6375 -1206 600 -164 N
ATOM 945 N TRP A 153 1.286 18.315 48.084 1.00 51.73 N
ANISOU 945 N TRP A 153 6188 6445 7023 -620 136 30 N
ATOM 946 CA TRP A 153 1.783 19.677 48.246 1.00 52.77 C
ANISOU 946 CA TRP A 153 6319 6531 7201 -572 23 64 C
ATOM 947 C TRP A 153 0.935 20.457 49.243 1.00 52.39 C
ANISOU 947 C TRP A 153 6320 6486 7099 -575 25 -50 C
ATOM 948 O TRP A 153 1.468 21.199 50.077 1.00 51.53 O
ANISOU 948 O TRP A 153 6289 6307 6983 -574 -64 -23 O
ATOM 949 CB TRP A 153 1.809 20.388 46.893 1.00 51.44 C
ANISOU 949 CB TRP A 153 6060 6384 7099 -509 -12 92 C
ATOM 950 CG TRP A 153 2.379 21.769 46.954 1.00 50.02 C
ANISOU 950 CG TRP A 153 5912 6134 6959 -484 -127 140 C
ATOM 951 CD1 TRP A 153 3.685 22.122 46.785 1.00 51.44 C
ANISOU 951 CD1 TRP A 153 6095 6252 7200 -517 -185 247 C
ATOM 952 CD2 TRP A 153 1.663 22.985 47.200 1.00 52.20 C
ANISOU 952 CD2 TRP A 153 6220 6387 7225 -428 -201 62 C
ATOM 953 NE1 TRP A 153 3.829 23.482 46.913 1.00 54.73 N
ANISOU 953 NE1 TRP A 153 6563 6600 7633 -506 -282 259 N
ATOM 954 CE2 TRP A 153 2.602 24.035 47.167 1.00 54.85 C
ANISOU 954 CE2 TRP A 153 6610 6630 7602 -438 -307 152 C
ATOM 955 CE3 TRP A 153 0.320 23.287 47.446 1.00 51.20 C
ANISOU 955 CE3 TRP A 153 6070 6310 7072 -368 -191 -100 C
ATOM 956 CZ2 TRP A 153 2.241 25.366 47.370 1.00 54.04 C
ANISOU 956 CZ2 TRP A 153 6573 6461 7497 -385 -419 108 C
ATOM 957 CZ3 TRP A 153 -0.036 24.609 47.647 1.00 52.88 C
ANISOU 957 CZ3 TRP A 153 6322 6471 7300 -294 -310 -165 C
ATOM 958 CH2 TRP A 153 0.921 25.631 47.608 1.00 53.91 C
ANISOU 958 CH2 TRP A 153 6541 6488 7454 -299 -430 -50 C
ATOM 959 N TYR A 154 -0.389 20.307 49.166 1.00 48.94 N
ANISOU 959 N TYR A 154 5823 6137 6633 -579 126 -203 N
ATOM 960 CA TYR A 154 -1.267 20.977 50.121 1.00 50.90 C
ANISOU 960 CA TYR A 154 6089 6412 6840 -587 157 -360 C
ATOM 961 C TYR A 154 -1.035 20.463 51.535 1.00 52.16 C
ANISOU 961 C TYR A 154 6419 6522 6877 -704 220 -354 C
ATOM 962 O TYR A 154 -1.096 21.232 52.501 1.00 54.56 O
ANISOU 962 O TYR A 154 6800 6795 7136 -707 189 -410 O
ATOM 963 CB TYR A 154 -2.729 20.787 49.715 1.00 52.92 C
ANISOU 963 CB TYR A 154 6204 6788 7116 -576 267 -570 C
ATOM 964 CG TYR A 154 -3.251 21.848 48.773 1.00 55.74 C
ANISOU 964 CG TYR A 154 6440 7166 7572 -422 141 -654 C
ATOM 965 CD1 TYR A 154 -2.991 23.194 48.998 1.00 54.70 C
ANISOU 965 CD1 TYR A 154 6353 6962 7469 -330 -10 -647 C
ATOM 966 CD2 TYR A 154 -4.001 21.504 47.655 1.00 56.02 C
ANISOU 966 CD2 TYR A 154 6348 7271 7666 -362 149 -742 C
ATOM 967 CE1 TYR A 154 -3.467 24.169 48.139 1.00 55.20 C
ANISOU 967 CE1 TYR A 154 6363 7006 7603 -182 -160 -720 C
ATOM 968 CE2 TYR A 154 -4.480 22.471 46.790 1.00 58.08 C
ANISOU 968 CE2 TYR A 154 6550 7519 7999 -204 -9 -822 C
ATOM 969 CZ TYR A 154 -4.210 23.801 47.037 1.00 54.62 C
ANISOU 969 CZ TYR A 154 6185 6992 7575 -114 -167 -807 C
ATOM 970 OH TYR A 154 -4.685 24.767 46.179 1.00 54.27 O
ANISOU 970 OH TYR A 154 6136 6899 7585 49 -357 -883 O
ATOM 971 N ALA A 155 -0.771 19.163 51.677 1.00 60.35 N
ANISOU 971 N ALA A 155 7550 7535 7844 -798 295 -290 N
ATOM 972 CA ALA A 155 -0.578 18.583 53.001 1.00 58.32 C
ANISOU 972 CA ALA A 155 7526 7198 7434 -917 338 -278 C
ATOM 973 C ALA A 155 0.788 18.910 53.595 1.00 59.48 C
ANISOU 973 C ALA A 155 7811 7209 7579 -872 147 -132 C
ATOM 974 O ALA A 155 0.919 18.980 54.821 1.00 59.87 O
ANISOU 974 O ALA A 155 8067 7178 7502 -933 127 -143 O
ATOM 975 CB ALA A 155 -0.771 17.068 52.940 1.00 58.22 C
ANISOU 975 CB ALA A 155 7613 7173 7336 -1032 454 -260 C
ATOM 976 N ILE A 156 1.806 19.112 52.763 1.00 54.37 N
ANISOU 976 N ILE A 156 7057 6534 7068 -775 10 -14 N
ATOM 977 CA ILE A 156 3.186 19.232 53.219 1.00 53.69 C
ANISOU 977 CA ILE A 156 7055 6327 7017 -736 -174 96 C
ATOM 978 C ILE A 156 3.713 20.654 53.055 1.00 53.65 C
ANISOU 978 C ILE A 156 6949 6310 7124 -664 -292 116 C
ATOM 979 O ILE A 156 4.240 21.242 54.000 1.00 57.24 O
ANISOU 979 O ILE A 156 7512 6679 7557 -658 -411 125 O
ATOM 980 CB ILE A 156 4.096 18.218 52.489 1.00 52.59 C
ANISOU 980 CB ILE A 156 6868 6159 6957 -705 -229 184 C
ATOM 981 CG1 ILE A 156 3.599 16.792 52.728 1.00 51.98 C
ANISOU 981 CG1 ILE A 156 6940 6058 6753 -781 -137 169 C
ATOM 982 CG2 ILE A 156 5.540 18.368 52.941 1.00 48.12 C
ANISOU 982 CG2 ILE A 156 6340 5478 6467 -650 -437 249 C
ATOM 983 CD1 ILE A 156 4.361 15.745 51.952 1.00 51.91 C
ANISOU 983 CD1 ILE A 156 6878 6022 6823 -735 -192 230 C
ATOM 984 N CYS A 157 3.580 21.223 51.857 1.00 51.89 N
ANISOU 984 N CYS A 157 6549 6156 7011 -617 -270 125 N
ATOM 985 CA CYS A 157 4.202 22.509 51.562 1.00 52.19 C
ANISOU 985 CA CYS A 157 6524 6156 7148 -574 -383 164 C
ATOM 986 C CYS A 157 3.323 23.697 51.931 1.00 50.22 C
ANISOU 986 C CYS A 157 6301 5914 6867 -541 -396 72 C
ATOM 987 O CYS A 157 3.841 24.726 52.377 1.00 50.27 O
ANISOU 987 O CYS A 157 6349 5845 6907 -525 -516 89 O
ATOM 988 CB CYS A 157 4.576 22.582 50.081 1.00 48.23 C
ANISOU 988 CB CYS A 157 5882 5693 6749 -558 -361 225 C
ATOM 989 SG CYS A 157 5.886 21.440 49.610 1.00 49.42 S
ANISOU 989 SG CYS A 157 5960 5834 6985 -580 -371 302 S
ATOM 990 N HIS A 158 2.012 23.586 51.746 1.00 53.13 N
ANISOU 990 N HIS A 158 6632 6371 7186 -527 -285 -47 N
ATOM 991 CA HIS A 158 1.133 24.696 52.076 1.00 53.11 C
ANISOU 991 CA HIS A 158 6626 6379 7173 -470 -313 -178 C
ATOM 992 C HIS A 158 1.184 24.959 53.580 1.00 56.50 C
ANISOU 992 C HIS A 158 7194 6760 7512 -508 -331 -232 C
ATOM 993 O HIS A 158 1.210 24.011 54.375 1.00 59.33 O
ANISOU 993 O HIS A 158 7661 7116 7765 -594 -249 -233 O
ATOM 994 CB HIS A 158 -0.302 24.404 51.635 1.00 53.91 C
ANISOU 994 CB HIS A 158 6622 6598 7263 -442 -191 -346 C
ATOM 995 CG HIS A 158 -1.166 25.624 51.547 1.00 57.68 C
ANISOU 995 CG HIS A 158 7047 7087 7783 -332 -268 -502 C
ATOM 996 ND1 HIS A 158 -1.845 26.138 52.631 1.00 58.19 N
ANISOU 996 ND1 HIS A 158 7135 7172 7803 -326 -242 -674 N
ATOM 997 CD2 HIS A 158 -1.458 26.437 50.503 1.00 55.64 C
ANISOU 997 CD2 HIS A 158 6735 6805 7601 -215 -388 -523 C
ATOM 998 CE1 HIS A 158 -2.518 27.212 52.259 1.00 53.23 C
ANISOU 998 CE1 HIS A 158 6441 6540 7245 -192 -353 -810 C
ATOM 999 NE2 HIS A 158 -2.301 27.415 50.973 1.00 53.81 N
ANISOU 999 NE2 HIS A 158 6484 6574 7386 -120 -458 -714 N
ATOM 1000 N PRO A 159 1.202 26.225 54.005 1.00 52.62 N
ANISOU 1000 N PRO A 159 6738 6213 7043 -451 -445 -277 N
ATOM 1001 CA PRO A 159 1.386 26.518 55.436 1.00 54.76 C
ANISOU 1001 CA PRO A 159 7162 6423 7220 -486 -480 -319 C
ATOM 1002 C PRO A 159 0.286 25.967 56.325 1.00 52.57 C
ANISOU 1002 C PRO A 159 6945 6227 6802 -554 -300 -489 C
ATOM 1003 O PRO A 159 0.489 25.867 57.541 1.00 54.92 O
ANISOU 1003 O PRO A 159 7426 6469 6972 -620 -295 -505 O
ATOM 1004 CB PRO A 159 1.422 28.053 55.479 1.00 55.97 C
ANISOU 1004 CB PRO A 159 7315 6511 7441 -395 -633 -360 C
ATOM 1005 CG PRO A 159 1.812 28.465 54.099 1.00 58.55 C
ANISOU 1005 CG PRO A 159 7543 6811 7891 -347 -713 -257 C
ATOM 1006 CD PRO A 159 1.192 27.450 53.188 1.00 54.11 C
ANISOU 1006 CD PRO A 159 6869 6359 7330 -356 -573 -273 C
ATOM 1007 N LEU A 160 -0.870 25.613 55.768 1.00 51.23 N
ANISOU 1007 N LEU A 160 6637 6183 6646 -553 -150 -630 N
ATOM 1008 CA LEU A 160 -1.975 25.090 56.557 1.00 53.54 C
ANISOU 1008 CA LEU A 160 6955 6570 6817 -654 63 -828 C
ATOM 1009 C LEU A 160 -2.019 23.570 56.612 1.00 57.59 C
ANISOU 1009 C LEU A 160 7547 7108 7226 -803 229 -773 C
ATOM 1010 O LEU A 160 -2.770 23.021 57.426 1.00 59.59 O
ANISOU 1010 O LEU A 160 7892 7412 7338 -944 428 -912 O
ATOM 1011 CB LEU A 160 -3.303 25.619 56.012 1.00 54.24 C
ANISOU 1011 CB LEU A 160 6820 6788 7002 -570 129 -1074 C
ATOM 1012 CG LEU A 160 -3.445 27.125 56.204 1.00 56.60 C
ANISOU 1012 CG LEU A 160 7086 7047 7372 -423 -34 -1179 C
ATOM 1013 CD1 LEU A 160 -4.638 27.624 55.451 1.00 59.55 C
ANISOU 1013 CD1 LEU A 160 7233 7521 7873 -292 -42 -1417 C
ATOM 1014 CD2 LEU A 160 -3.571 27.458 57.678 1.00 56.66 C
ANISOU 1014 CD2 LEU A 160 7242 7040 7247 -495 33 -1295 C
ATOM 1015 N MET A 161 -1.235 22.885 55.780 1.00 53.50 N
ANISOU 1015 N MET A 161 7011 6548 6767 -788 160 -588 N
ATOM 1016 CA MET A 161 -1.132 21.427 55.791 1.00 55.72 C
ANISOU 1016 CA MET A 161 7394 6819 6956 -910 271 -518 C
ATOM 1017 C MET A 161 -2.515 20.780 55.692 1.00 53.82 C
ANISOU 1017 C MET A 161 7069 6713 6669 -1018 519 -712 C
ATOM 1018 O MET A 161 -2.974 20.073 56.592 1.00 57.57 O
ANISOU 1018 O MET A 161 7715 7184 6973 -1190 692 -787 O
ATOM 1019 CB MET A 161 -0.377 20.951 57.036 1.00 57.49 C
ANISOU 1019 CB MET A 161 7927 6905 7010 -1002 225 -424 C
ATOM 1020 CG MET A 161 0.811 21.832 57.403 1.00 55.63 C
ANISOU 1020 CG MET A 161 7757 6551 6830 -900 -19 -309 C
ATOM 1021 SD MET A 161 1.926 21.091 58.608 1.00 69.51 S
ANISOU 1021 SD MET A 161 9870 8116 8424 -959 -162 -182 S
ATOM 1022 CE MET A 161 2.789 19.902 57.583 1.00 63.17 C
ANISOU 1022 CE MET A 161 8996 7277 7729 -920 -243 -33 C
ATOM 1023 N PHE A 162 -3.177 21.044 54.567 1.00 60.51 N
ANISOU 1023 N PHE A 162 7658 7669 7666 -924 530 -804 N
ATOM 1024 CA PHE A 162 -4.546 20.586 54.372 1.00 61.43 C
ANISOU 1024 CA PHE A 162 7624 7928 7789 -1002 741 -1037 C
ATOM 1025 C PHE A 162 -4.625 19.065 54.350 1.00 62.71 C
ANISOU 1025 C PHE A 162 7890 8086 7852 -1175 901 -986 C
ATOM 1026 O PHE A 162 -3.789 18.387 53.746 1.00 62.90 O
ANISOU 1026 O PHE A 162 7971 8037 7894 -1147 808 -786 O
ATOM 1027 CB PHE A 162 -5.112 21.150 53.069 1.00 61.64 C
ANISOU 1027 CB PHE A 162 7375 8041 8004 -833 653 -1132 C
ATOM 1028 CG PHE A 162 -5.334 22.634 53.091 1.00 62.23 C
ANISOU 1028 CG PHE A 162 7360 8115 8169 -668 502 -1240 C
ATOM 1029 CD1 PHE A 162 -6.152 23.211 54.049 1.00 67.02 C
ANISOU 1029 CD1 PHE A 162 7934 8785 8745 -695 595 -1485 C
ATOM 1030 CD2 PHE A 162 -4.746 23.450 52.139 1.00 62.02 C
ANISOU 1030 CD2 PHE A 162 7296 8017 8250 -496 273 -1111 C
ATOM 1031 CE1 PHE A 162 -6.365 24.575 54.066 1.00 66.11 C
ANISOU 1031 CE1 PHE A 162 7744 8656 8720 -524 433 -1601 C
ATOM 1032 CE2 PHE A 162 -4.956 24.815 52.151 1.00 61.48 C
ANISOU 1032 CE2 PHE A 162 7189 7918 8254 -346 113 -1207 C
ATOM 1033 CZ PHE A 162 -5.768 25.377 53.114 1.00 62.26 C
ANISOU 1033 CZ PHE A 162 7246 8074 8336 -346 177 -1454 C
ATOM 1034 N LYS A 163 -5.646 18.530 55.016 1.00 62.17 N
ANISOU 1034 N LYS A 163 7850 8095 7678 -1363 1151 -1185 N
ATOM 1035 CA LYS A 163 -5.948 17.103 55.016 1.00 64.10 C
ANISOU 1035 CA LYS A 163 8203 8335 7818 -1562 1335 -1179 C
ATOM 1036 C LYS A 163 -7.204 16.892 54.179 1.00 65.29 C
ANISOU 1036 C LYS A 163 8043 8659 8106 -1578 1481 -1421 C
ATOM 1037 O LYS A 163 -8.307 17.253 54.602 1.00 71.56 O
ANISOU 1037 O LYS A 163 8692 9582 8917 -1656 1658 -1710 O
ATOM 1038 CB LYS A 163 -6.129 16.586 56.443 1.00 67.17 C
ANISOU 1038 CB LYS A 163 8910 8658 7953 -1816 1530 -1223 C
ATOM 1039 CG LYS A 163 -4.819 16.394 57.199 1.00 70.59 C
ANISOU 1039 CG LYS A 163 9710 8882 8229 -1811 1353 -963 C
ATOM 1040 CD LYS A 163 -5.015 16.399 58.712 1.00 77.64 C
ANISOU 1040 CD LYS A 163 10932 9704 8862 -2011 1495 -1033 C
ATOM 1041 CE LYS A 163 -5.005 17.817 59.271 1.00 80.09 C
ANISOU 1041 CE LYS A 163 11166 10054 9212 -1893 1418 -1125 C
ATOM 1042 NZ LYS A 163 -5.004 17.837 60.762 1.00 74.05 N
ANISOU 1042 NZ LYS A 163 10771 9194 8172 -2072 1522 -1163 N
ATOM 1043 N SER A 164 -7.035 16.314 52.992 1.00 80.60 N
ANISOU 1043 N SER A 164 9870 10603 10152 -1498 1402 -1327 N
ATOM 1044 CA SER A 164 -8.153 16.145 52.076 1.00 85.08 C
ANISOU 1044 CA SER A 164 10138 11321 10869 -1476 1485 -1552 C
ATOM 1045 C SER A 164 -9.122 15.084 52.584 1.00 90.57 C
ANISOU 1045 C SER A 164 10858 12085 11470 -1761 1792 -1745 C
ATOM 1046 O SER A 164 -8.730 14.093 53.205 1.00 87.26 O
ANISOU 1046 O SER A 164 10734 11557 10863 -1963 1903 -1611 O
ATOM 1047 CB SER A 164 -7.652 15.765 50.684 1.00 82.55 C
ANISOU 1047 CB SER A 164 9734 10973 10658 -1326 1318 -1388 C
ATOM 1048 OG SER A 164 -6.854 14.595 50.734 1.00 83.52 O
ANISOU 1048 OG SER A 164 10087 10980 10666 -1433 1335 -1169 O
ATOM 1049 N THR A 165 -10.402 15.306 52.312 1.00108.28 N
ANISOU 1049 N THR A 165 12795 14500 13846 -1778 1921 -2078 N
ATOM 1050 CA THR A 165 -11.450 14.367 52.675 1.00109.32 C
ANISOU 1050 CA THR A 165 12884 14727 13928 -2067 2239 -2319 C
ATOM 1051 C THR A 165 -11.700 13.385 51.535 1.00105.74 C
ANISOU 1051 C THR A 165 12310 14295 13571 -2072 2230 -2307 C
ATOM 1052 O THR A 165 -11.345 13.631 50.379 1.00106.96 O
ANISOU 1052 O THR A 165 12333 14439 13866 -1823 1986 -2198 O
ATOM 1053 CB THR A 165 -12.743 15.107 53.020 1.00107.07 C
ANISOU 1053 CB THR A 165 12282 14634 13765 -2094 2398 -2748 C
ATOM 1054 OG1 THR A 165 -13.247 15.763 51.850 1.00107.19 O
ANISOU 1054 OG1 THR A 165 11932 14752 14046 -1813 2189 -2909 O
ATOM 1055 CG2 THR A 165 -12.484 16.146 54.101 1.00106.85 C
ANISOU 1055 CG2 THR A 165 12368 14584 13647 -2063 2389 -2769 C
ATOM 1056 N ALA A 166 -12.318 12.252 51.879 1.00100.70 N
ANISOU 1056 N ALA A 166 11744 13678 12838 -2379 2509 -2423 N
ATOM 1057 CA ALA A 166 -12.663 11.263 50.862 1.00 97.23 C
ANISOU 1057 CA ALA A 166 11190 13263 12490 -2413 2522 -2446 C
ATOM 1058 C ALA A 166 -13.653 11.825 49.851 1.00 97.37 C
ANISOU 1058 C ALA A 166 10750 13462 12785 -2225 2440 -2750 C
ATOM 1059 O ALA A 166 -13.608 11.461 48.669 1.00 97.00 O
ANISOU 1059 O ALA A 166 10588 13413 12855 -2082 2284 -2694 O
ATOM 1060 CB ALA A 166 -13.230 10.005 51.520 1.00 92.69 C
ANISOU 1060 CB ALA A 166 10794 12670 11755 -2814 2858 -2545 C
ATOM 1061 N LYS A 167 -14.549 12.711 50.294 1.00 87.94 N
ANISOU 1061 N LYS A 167 9298 12418 11698 -2210 2525 -3088 N
ATOM 1062 CA LYS A 167 -15.467 13.365 49.368 1.00 87.33 C
ANISOU 1062 CA LYS A 167 8792 12492 11899 -1980 2382 -3403 C
ATOM 1063 C LYS A 167 -14.702 14.135 48.301 1.00 86.77 C
ANISOU 1063 C LYS A 167 8721 12333 11915 -1599 1982 -3169 C
ATOM 1064 O LYS A 167 -15.012 14.042 47.108 1.00 86.81 O
ANISOU 1064 O LYS A 167 8544 12367 12072 -1426 1807 -3232 O
ATOM 1065 CB LYS A 167 -16.405 14.303 50.129 1.00 90.56 C
ANISOU 1065 CB LYS A 167 8947 13056 12406 -1990 2503 -3802 C
ATOM 1066 CG LYS A 167 -17.352 13.620 51.100 1.00 95.34 C
ANISOU 1066 CG LYS A 167 9490 13786 12949 -2391 2941 -4121 C
ATOM 1067 CD LYS A 167 -18.244 14.647 51.783 1.00102.65 C
ANISOU 1067 CD LYS A 167 10125 14881 13996 -2364 3045 -4550 C
ATOM 1068 CE LYS A 167 -19.271 13.992 52.692 1.00104.24 C
ANISOU 1068 CE LYS A 167 10296 15178 14134 -2763 3439 -4870 C
ATOM 1069 NZ LYS A 167 -20.152 15.002 53.346 1.00 96.73 N
ANISOU 1069 NZ LYS A 167 9110 14343 13301 -2710 3455 -5259 N
ATOM 1070 N ARG A 168 -13.688 14.900 48.717 1.00 88.73 N
ANISOU 1070 N ARG A 168 9191 12465 12058 -1479 1837 -2904 N
ATOM 1071 CA ARG A 168 -12.910 15.681 47.762 1.00 85.44 C
ANISOU 1071 CA ARG A 168 8807 11953 11702 -1162 1490 -2681 C
ATOM 1072 C ARG A 168 -12.153 14.780 46.796 1.00 83.80 C
ANISOU 1072 C ARG A 168 8740 11651 11450 -1142 1402 -2393 C
ATOM 1073 O ARG A 168 -12.077 15.070 45.597 1.00 81.46 O
ANISOU 1073 O ARG A 168 8359 11338 11253 -921 1174 -2353 O
ATOM 1074 CB ARG A 168 -11.945 16.605 48.503 1.00 86.30 C
ANISOU 1074 CB ARG A 168 9131 11955 11704 -1089 1389 -2466 C
ATOM 1075 CG ARG A 168 -11.218 17.583 47.598 1.00 85.00 C
ANISOU 1075 CG ARG A 168 8998 11695 11602 -793 1056 -2276 C
ATOM 1076 CD ARG A 168 -10.352 18.533 48.401 1.00 83.28 C
ANISOU 1076 CD ARG A 168 8966 11378 11298 -744 970 -2107 C
ATOM 1077 NE ARG A 168 -10.537 19.919 47.986 1.00 82.83 N
ANISOU 1077 NE ARG A 168 8811 11304 11355 -488 720 -2201 N
ATOM 1078 CZ ARG A 168 -9.760 20.554 47.119 1.00 81.54 C
ANISOU 1078 CZ ARG A 168 8752 11025 11207 -304 467 -1983 C
ATOM 1079 NH1 ARG A 168 -8.719 19.960 46.560 1.00 78.15 N
ANISOU 1079 NH1 ARG A 168 8485 10508 10701 -340 441 -1675 N
ATOM 1080 NH2 ARG A 168 -10.033 21.818 46.808 1.00 81.06 N
ANISOU 1080 NH2 ARG A 168 8640 10926 11232 -87 236 -2091 N
ATOM 1081 N ALA A 169 -11.582 13.682 47.299 1.00 87.13 N
ANISOU 1081 N ALA A 169 9398 11997 11711 -1366 1569 -2199 N
ATOM 1082 CA ALA A 169 -10.858 12.759 46.431 1.00 80.49 C
ANISOU 1082 CA ALA A 169 8683 11066 10833 -1345 1491 -1953 C
ATOM 1083 C ALA A 169 -11.784 12.128 45.398 1.00 80.98 C
ANISOU 1083 C ALA A 169 8520 11221 11026 -1334 1503 -2153 C
ATOM 1084 O ALA A 169 -11.436 12.034 44.213 1.00 77.07 O
ANISOU 1084 O ALA A 169 8005 10692 10585 -1162 1320 -2038 O
ATOM 1085 CB ALA A 169 -10.174 11.679 47.269 1.00 73.34 C
ANISOU 1085 CB ALA A 169 8087 10045 9734 -1581 1647 -1753 C
ATOM 1086 N ARG A 170 -12.970 11.693 45.826 1.00 82.40 N
ANISOU 1086 N ARG A 170 8529 11520 11257 -1529 1726 -2469 N
ATOM 1087 CA ARG A 170 -13.908 11.085 44.889 1.00 82.86 C
ANISOU 1087 CA ARG A 170 8348 11673 11462 -1529 1735 -2698 C
ATOM 1088 C ARG A 170 -14.419 12.102 43.875 1.00 82.03 C
ANISOU 1088 C ARG A 170 7978 11637 11552 -1212 1461 -2875 C
ATOM 1089 O ARG A 170 -14.568 11.781 42.689 1.00 81.86 O
ANISOU 1089 O ARG A 170 7877 11613 11612 -1079 1307 -2883 O
ATOM 1090 CB ARG A 170 -15.058 10.435 45.657 1.00 85.96 C
ANISOU 1090 CB ARG A 170 8601 12184 11875 -1843 2061 -3030 C
ATOM 1091 CG ARG A 170 -14.632 9.168 46.385 1.00 92.59 C
ANISOU 1091 CG ARG A 170 9761 12917 12502 -2173 2305 -2848 C
ATOM 1092 CD ARG A 170 -15.494 8.877 47.599 1.00 95.25 C
ANISOU 1092 CD ARG A 170 10086 13334 12770 -2528 2668 -3114 C
ATOM 1093 NE ARG A 170 -14.961 7.757 48.368 1.00 95.74 N
ANISOU 1093 NE ARG A 170 10558 13241 12577 -2836 2862 -2894 N
ATOM 1094 CZ ARG A 170 -15.408 7.383 49.558 1.00 93.94 C
ANISOU 1094 CZ ARG A 170 10488 13015 12190 -3194 3189 -3021 C
ATOM 1095 NH1 ARG A 170 -16.400 8.023 50.157 1.00 94.40 N
ANISOU 1095 NH1 ARG A 170 10291 13248 12329 -3306 3395 -3386 N
ATOM 1096 NH2 ARG A 170 -14.844 6.342 50.166 1.00 90.82 N
ANISOU 1096 NH2 ARG A 170 10534 12432 11541 -3447 3308 -2788 N
ATOM 1097 N ASN A 171 -14.678 13.337 44.315 1.00 78.62 N
ANISOU 1097 N ASN A 171 7439 11248 11185 -1078 1377 -3018 N
ATOM 1098 CA ASN A 171 -15.092 14.380 43.382 1.00 77.83 C
ANISOU 1098 CA ASN A 171 7155 11169 11248 -752 1065 -3168 C
ATOM 1099 C ASN A 171 -13.997 14.675 42.366 1.00 77.22 C
ANISOU 1099 C ASN A 171 7303 10942 11095 -539 796 -2810 C
ATOM 1100 O ASN A 171 -14.278 14.870 41.177 1.00 75.37 O
ANISOU 1100 O ASN A 171 6997 10693 10947 -331 562 -2869 O
ATOM 1101 CB ASN A 171 -15.471 15.650 44.146 1.00 79.46 C
ANISOU 1101 CB ASN A 171 7249 11421 11520 -650 1017 -3371 C
ATOM 1102 CG ASN A 171 -16.680 15.455 45.037 1.00 84.49 C
ANISOU 1102 CG ASN A 171 7608 12234 12260 -847 1289 -3802 C
ATOM 1103 OD1 ASN A 171 -17.553 14.636 44.747 1.00 86.89 O
ANISOU 1103 OD1 ASN A 171 7697 12646 12670 -974 1422 -4058 O
ATOM 1104 ND2 ASN A 171 -16.737 16.207 46.130 1.00 86.10 N
ANISOU 1104 ND2 ASN A 171 7811 12469 12432 -889 1387 -3901 N
ATOM 1105 N SER A 172 -12.740 14.718 42.817 1.00 74.81 N
ANISOU 1105 N SER A 172 7278 10522 10625 -593 825 -2454 N
ATOM 1106 CA SER A 172 -11.628 14.944 41.901 1.00 72.63 C
ANISOU 1106 CA SER A 172 7205 10117 10274 -438 622 -2129 C
ATOM 1107 C SER A 172 -11.506 13.809 40.893 1.00 70.62 C
ANISOU 1107 C SER A 172 6978 9850 10005 -466 630 -2043 C
ATOM 1108 O SER A 172 -11.273 14.049 39.703 1.00 67.54 O
ANISOU 1108 O SER A 172 6631 9408 9622 -288 427 -1962 O
ATOM 1109 CB SER A 172 -10.329 15.114 42.689 1.00 71.11 C
ANISOU 1109 CB SER A 172 7260 9822 9938 -516 675 -1816 C
ATOM 1110 OG SER A 172 -9.256 15.476 41.836 1.00 70.85 O
ANISOU 1110 OG SER A 172 7388 9679 9851 -379 498 -1544 O
ATOM 1111 N ILE A 173 -11.672 12.564 41.345 1.00 70.64 N
ANISOU 1111 N ILE A 173 6983 9887 9971 -698 861 -2065 N
ATOM 1112 CA ILE A 173 -11.618 11.432 40.422 1.00 68.93 C
ANISOU 1112 CA ILE A 173 6788 9655 9745 -729 869 -2007 C
ATOM 1113 C ILE A 173 -12.733 11.533 39.386 1.00 71.12 C
ANISOU 1113 C ILE A 173 6835 10014 10175 -586 729 -2286 C
ATOM 1114 O ILE A 173 -12.507 11.334 38.182 1.00 70.16 O
ANISOU 1114 O ILE A 173 6761 9847 10048 -448 568 -2201 O
ATOM 1115 CB ILE A 173 -11.684 10.104 41.202 1.00 66.61 C
ANISOU 1115 CB ILE A 173 6567 9362 9379 -1020 1137 -2001 C
ATOM 1116 CG1 ILE A 173 -10.409 9.905 42.025 1.00 64.63 C
ANISOU 1116 CG1 ILE A 173 6600 8989 8966 -1110 1197 -1693 C
ATOM 1117 CG2 ILE A 173 -11.905 8.933 40.257 1.00 63.84 C
ANISOU 1117 CG2 ILE A 173 6196 9009 9051 -1055 1144 -2019 C
ATOM 1118 CD1 ILE A 173 -10.393 8.624 42.832 1.00 60.44 C
ANISOU 1118 CD1 ILE A 173 6228 8410 8327 -1387 1419 -1662 C
ATOM 1119 N VAL A 174 -13.949 11.857 39.834 1.00 70.49 N
ANISOU 1119 N VAL A 174 6497 10052 10233 -613 779 -2644 N
ATOM 1120 CA VAL A 174 -15.082 11.948 38.915 1.00 69.85 C
ANISOU 1120 CA VAL A 174 6163 10051 10328 -464 618 -2966 C
ATOM 1121 C VAL A 174 -14.863 13.060 37.897 1.00 70.29 C
ANISOU 1121 C VAL A 174 6286 10024 10398 -135 260 -2906 C
ATOM 1122 O VAL A 174 -15.111 12.879 36.697 1.00 71.02 O
ANISOU 1122 O VAL A 174 6370 10089 10526 17 64 -2948 O
ATOM 1123 CB VAL A 174 -16.394 12.145 39.697 1.00 72.21 C
ANISOU 1123 CB VAL A 174 6136 10504 10795 -559 752 -3406 C
ATOM 1124 CG1 VAL A 174 -17.537 12.476 38.748 1.00 70.09 C
ANISOU 1124 CG1 VAL A 174 5579 10310 10742 -339 510 -3777 C
ATOM 1125 CG2 VAL A 174 -16.721 10.898 40.502 1.00 71.93 C
ANISOU 1125 CG2 VAL A 174 6066 10538 10726 -925 1120 -3485 C
ATOM 1126 N ILE A 175 -14.402 14.228 38.351 1.00 69.06 N
ANISOU 1126 N ILE A 175 6228 9810 10200 -26 161 -2808 N
ATOM 1127 CA ILE A 175 -14.203 15.338 37.424 1.00 69.57 C
ANISOU 1127 CA ILE A 175 6412 9767 10255 264 -181 -2748 C
ATOM 1128 C ILE A 175 -13.064 15.031 36.458 1.00 67.63 C
ANISOU 1128 C ILE A 175 6458 9397 9843 294 -250 -2382 C
ATOM 1129 O ILE A 175 -13.120 15.407 35.283 1.00 67.24 O
ANISOU 1129 O ILE A 175 6511 9267 9772 490 -507 -2370 O
ATOM 1130 CB ILE A 175 -13.987 16.664 38.182 1.00 71.70 C
ANISOU 1130 CB ILE A 175 6732 9992 10519 354 -266 -2737 C
ATOM 1131 CG1 ILE A 175 -14.075 17.850 37.216 1.00 73.66 C
ANISOU 1131 CG1 ILE A 175 7097 10115 10775 660 -652 -2757 C
ATOM 1132 CG2 ILE A 175 -12.653 16.691 38.903 1.00 70.54 C
ANISOU 1132 CG2 ILE A 175 6824 9773 10206 207 -105 -2370 C
ATOM 1133 CD1 ILE A 175 -13.845 19.196 37.875 1.00 75.66 C
ANISOU 1133 CD1 ILE A 175 7432 10297 11020 763 -770 -2741 C
ATOM 1134 N ILE A 176 -12.024 14.329 36.922 1.00 70.72 N
ANISOU 1134 N ILE A 176 6995 9765 10112 101 -29 -2099 N
ATOM 1135 CA ILE A 176 -10.943 13.928 36.025 1.00 69.36 C
ANISOU 1135 CA ILE A 176 7051 9498 9803 114 -59 -1797 C
ATOM 1136 C ILE A 176 -11.478 13.015 34.931 1.00 71.40 C
ANISOU 1136 C ILE A 176 7256 9783 10090 149 -110 -1900 C
ATOM 1137 O ILE A 176 -11.189 13.203 33.742 1.00 71.00 O
ANISOU 1137 O ILE A 176 7355 9654 9966 289 -286 -1806 O
ATOM 1138 CB ILE A 176 -9.807 13.253 36.817 1.00 66.54 C
ANISOU 1138 CB ILE A 176 6816 9119 9347 -84 170 -1537 C
ATOM 1139 CG1 ILE A 176 -8.984 14.298 37.573 1.00 65.79 C
ANISOU 1139 CG1 ILE A 176 6840 8961 9197 -74 152 -1374 C
ATOM 1140 CG2 ILE A 176 -8.914 12.440 35.890 1.00 63.36 C
ANISOU 1140 CG2 ILE A 176 6564 8662 8850 -97 186 -1321 C
ATOM 1141 CD1 ILE A 176 -7.884 13.705 38.425 1.00 60.41 C
ANISOU 1141 CD1 ILE A 176 6272 8248 8435 -242 332 -1151 C
ATOM 1142 N TRP A 177 -12.282 12.020 35.316 1.00 65.12 N
ANISOU 1142 N TRP A 177 6261 9090 9391 8 48 -2104 N
ATOM 1143 CA TRP A 177 -12.850 11.108 34.326 1.00 65.46 C
ANISOU 1143 CA TRP A 177 6235 9160 9478 30 0 -2227 C
ATOM 1144 C TRP A 177 -13.732 11.854 33.330 1.00 67.44 C
ANISOU 1144 C TRP A 177 6411 9400 9815 284 -311 -2455 C
ATOM 1145 O TRP A 177 -13.632 11.643 32.115 1.00 68.61 O
ANISOU 1145 O TRP A 177 6680 9485 9902 406 -475 -2403 O
ATOM 1146 CB TRP A 177 -13.642 10.000 35.021 1.00 61.79 C
ANISOU 1146 CB TRP A 177 5564 8802 9111 -196 236 -2438 C
ATOM 1147 CG TRP A 177 -12.821 8.796 35.351 1.00 62.79 C
ANISOU 1147 CG TRP A 177 5843 8888 9125 -406 458 -2208 C
ATOM 1148 CD1 TRP A 177 -12.317 8.456 36.572 1.00 61.78 C
ANISOU 1148 CD1 TRP A 177 5799 8746 8928 -613 681 -2085 C
ATOM 1149 CD2 TRP A 177 -12.404 7.769 34.444 1.00 64.42 C
ANISOU 1149 CD2 TRP A 177 6162 9047 9270 -413 450 -2085 C
ATOM 1150 NE1 TRP A 177 -11.614 7.278 36.482 1.00 62.76 N
ANISOU 1150 NE1 TRP A 177 6086 8804 8958 -736 789 -1897 N
ATOM 1151 CE2 TRP A 177 -11.651 6.837 35.185 1.00 61.68 C
ANISOU 1151 CE2 TRP A 177 5953 8652 8830 -617 660 -1898 C
ATOM 1152 CE3 TRP A 177 -12.594 7.547 33.076 1.00 64.31 C
ANISOU 1152 CE3 TRP A 177 6162 9013 9260 -259 271 -2123 C
ATOM 1153 CZ2 TRP A 177 -11.089 5.701 34.606 1.00 59.50 C
ANISOU 1153 CZ2 TRP A 177 5806 8314 8486 -660 693 -1763 C
ATOM 1154 CZ3 TRP A 177 -12.035 6.418 32.503 1.00 62.70 C
ANISOU 1154 CZ3 TRP A 177 6083 8761 8979 -319 331 -1983 C
ATOM 1155 CH2 TRP A 177 -11.291 5.510 33.267 1.00 59.41 C
ANISOU 1155 CH2 TRP A 177 5780 8303 8489 -512 539 -1811 C
ATOM 1156 N ILE A 178 -14.594 12.743 33.829 1.00 68.19 N
ANISOU 1156 N ILE A 178 6320 9544 10044 379 -414 -2722 N
ATOM 1157 CA ILE A 178 -15.518 13.452 32.948 1.00 67.63 C
ANISOU 1157 CA ILE A 178 6169 9450 10079 648 -757 -2988 C
ATOM 1158 C ILE A 178 -14.760 14.362 31.987 1.00 68.18 C
ANISOU 1158 C ILE A 178 6583 9343 9978 856 -1031 -2741 C
ATOM 1159 O ILE A 178 -15.046 14.388 30.783 1.00 68.92 O
ANISOU 1159 O ILE A 178 6784 9361 10040 1031 -1286 -2793 O
ATOM 1160 CB ILE A 178 -16.556 14.229 33.778 1.00 68.11 C
ANISOU 1160 CB ILE A 178 5940 9602 10337 713 -808 -3355 C
ATOM 1161 CG1 ILE A 178 -17.476 13.256 34.520 1.00 65.27 C
ANISOU 1161 CG1 ILE A 178 5230 9423 10147 487 -532 -3663 C
ATOM 1162 CG2 ILE A 178 -17.371 15.155 32.890 1.00 66.71 C
ANISOU 1162 CG2 ILE A 178 5727 9359 10261 1046 -1236 -3616 C
ATOM 1163 CD1 ILE A 178 -18.520 13.933 35.377 1.00 68.88 C
ANISOU 1163 CD1 ILE A 178 5360 10000 10809 517 -526 -4071 C
ATOM 1164 N VAL A 179 -13.778 15.113 32.494 1.00 69.16 N
ANISOU 1164 N VAL A 179 6907 9391 9980 823 -978 -2474 N
ATOM 1165 CA VAL A 179 -13.016 16.017 31.637 1.00 68.94 C
ANISOU 1165 CA VAL A 179 7230 9188 9775 970 -1199 -2237 C
ATOM 1166 C VAL A 179 -12.224 15.231 30.600 1.00 70.08 C
ANISOU 1166 C VAL A 179 7597 9279 9753 913 -1143 -1994 C
ATOM 1167 O VAL A 179 -12.151 15.624 29.429 1.00 69.90 O
ANISOU 1167 O VAL A 179 7822 9131 9607 1062 -1378 -1940 O
ATOM 1168 CB VAL A 179 -12.104 16.924 32.485 1.00 64.80 C
ANISOU 1168 CB VAL A 179 6843 8604 9172 908 -1120 -2016 C
ATOM 1169 CG1 VAL A 179 -11.143 17.702 31.596 1.00 63.57 C
ANISOU 1169 CG1 VAL A 179 7077 8268 8810 981 -1273 -1735 C
ATOM 1170 CG2 VAL A 179 -12.942 17.885 33.314 1.00 66.18 C
ANISOU 1170 CG2 VAL A 179 6841 8807 9498 1019 -1242 -2279 C
ATOM 1171 N SER A 180 -11.623 14.106 31.004 1.00 71.89 N
ANISOU 1171 N SER A 180 7763 9589 9962 698 -840 -1855 N
ATOM 1172 CA SER A 180 -10.886 13.286 30.049 1.00 68.34 C
ANISOU 1172 CA SER A 180 7492 9102 9374 649 -776 -1661 C
ATOM 1173 C SER A 180 -11.806 12.745 28.965 1.00 72.74 C
ANISOU 1173 C SER A 180 8009 9664 9966 772 -954 -1866 C
ATOM 1174 O SER A 180 -11.430 12.703 27.787 1.00 76.95 O
ANISOU 1174 O SER A 180 8786 10106 10347 849 -1069 -1753 O
ATOM 1175 CB SER A 180 -10.181 12.140 30.773 1.00 68.29 C
ANISOU 1175 CB SER A 180 7406 9172 9369 422 -456 -1522 C
ATOM 1176 OG SER A 180 -9.251 12.631 31.721 1.00 68.01 O
ANISOU 1176 OG SER A 180 7430 9118 9294 324 -323 -1330 O
ATOM 1177 N CYS A 181 -13.014 12.319 29.341 1.00 69.79 N
ANISOU 1177 N CYS A 181 7331 9396 9790 779 -971 -2184 N
ATOM 1178 CA CYS A 181 -13.958 11.828 28.343 1.00 67.91 C
ANISOU 1178 CA CYS A 181 7021 9165 9617 904 -1167 -2420 C
ATOM 1179 C CYS A 181 -14.401 12.943 27.402 1.00 69.26 C
ANISOU 1179 C CYS A 181 7373 9204 9738 1186 -1569 -2517 C
ATOM 1180 O CYS A 181 -14.608 12.707 26.207 1.00 68.88 O
ANISOU 1180 O CYS A 181 7480 9081 9608 1312 -1772 -2550 O
ATOM 1181 CB CYS A 181 -15.167 11.191 29.030 1.00 66.49 C
ANISOU 1181 CB CYS A 181 6442 9137 9684 824 -1079 -2777 C
ATOM 1182 SG CYS A 181 -14.785 9.685 29.944 1.00 66.44 S
ANISOU 1182 SG CYS A 181 6306 9241 9699 482 -644 -2681 S
ATOM 1183 N ILE A 182 -14.562 14.159 27.924 1.00 68.31 N
ANISOU 1183 N ILE A 182 7263 9037 9656 1294 -1710 -2570 N
ATOM 1184 CA ILE A 182 -15.040 15.264 27.097 1.00 69.58 C
ANISOU 1184 CA ILE A 182 7626 9040 9771 1578 -2135 -2681 C
ATOM 1185 C ILE A 182 -13.960 15.719 26.119 1.00 70.34 C
ANISOU 1185 C ILE A 182 8218 8949 9560 1602 -2217 -2333 C
ATOM 1186 O ILE A 182 -14.222 15.906 24.926 1.00 71.62 O
ANISOU 1186 O ILE A 182 8638 8974 9600 1775 -2511 -2367 O
ATOM 1187 CB ILE A 182 -15.528 16.422 27.986 1.00 68.12 C
ANISOU 1187 CB ILE A 182 7310 8851 9723 1689 -2266 -2855 C
ATOM 1188 CG1 ILE A 182 -16.828 16.034 28.695 1.00 66.50 C
ANISOU 1188 CG1 ILE A 182 6611 8828 9828 1701 -2241 -3296 C
ATOM 1189 CG2 ILE A 182 -15.729 17.678 27.159 1.00 63.55 C
ANISOU 1189 CG2 ILE A 182 7056 8051 9038 1975 -2717 -2885 C
ATOM 1190 CD1 ILE A 182 -17.355 17.096 29.633 1.00 67.96 C
ANISOU 1190 CD1 ILE A 182 6618 9036 10169 1804 -2338 -3516 C
ATOM 1191 N ILE A 183 -12.727 15.897 26.603 1.00 69.84 N
ANISOU 1191 N ILE A 183 8302 8871 9363 1418 -1956 -2007 N
ATOM 1192 CA ILE A 183 -11.687 16.490 25.766 1.00 69.93 C
ANISOU 1192 CA ILE A 183 8771 8708 9091 1409 -2005 -1704 C
ATOM 1193 C ILE A 183 -11.193 15.536 24.686 1.00 70.89 C
ANISOU 1193 C ILE A 183 9067 8822 9048 1339 -1908 -1573 C
ATOM 1194 O ILE A 183 -10.562 15.979 23.720 1.00 72.23 O
ANISOU 1194 O ILE A 183 9643 8838 8964 1351 -1990 -1387 O
ATOM 1195 CB ILE A 183 -10.501 16.977 26.621 1.00 68.54 C
ANISOU 1195 CB ILE A 183 8662 8530 8849 1226 -1751 -1431 C
ATOM 1196 CG1 ILE A 183 -9.812 15.799 27.312 1.00 68.15 C
ANISOU 1196 CG1 ILE A 183 8384 8648 8863 991 -1357 -1316 C
ATOM 1197 CG2 ILE A 183 -10.959 18.015 27.634 1.00 65.40 C
ANISOU 1197 CG2 ILE A 183 8139 8121 8588 1307 -1866 -1555 C
ATOM 1198 CD1 ILE A 183 -8.626 16.202 28.161 1.00 66.55 C
ANISOU 1198 CD1 ILE A 183 8226 8445 8615 824 -1130 -1073 C
ATOM 1199 N MET A 184 -11.460 14.238 24.816 1.00 73.00 N
ANISOU 1199 N MET A 184 9057 9241 9438 1251 -1728 -1670 N
ATOM 1200 CA MET A 184 -11.030 13.255 23.831 1.00 71.23 C
ANISOU 1200 CA MET A 184 8971 9018 9077 1193 -1636 -1573 C
ATOM 1201 C MET A 184 -12.120 12.922 22.821 1.00 73.09 C
ANISOU 1201 C MET A 184 9226 9214 9333 1383 -1934 -1819 C
ATOM 1202 O MET A 184 -11.957 11.982 22.036 1.00 76.35 O
ANISOU 1202 O MET A 184 9707 9641 9661 1346 -1871 -1791 O
ATOM 1203 CB MET A 184 -10.554 11.978 24.527 1.00 69.12 C
ANISOU 1203 CB MET A 184 8441 8910 8912 982 -1275 -1512 C
ATOM 1204 CG MET A 184 -9.357 12.176 25.444 1.00 65.92 C
ANISOU 1204 CG MET A 184 8037 8534 8476 802 -997 -1268 C
ATOM 1205 SD MET A 184 -7.895 12.789 24.588 1.00 67.02 S
ANISOU 1205 SD MET A 184 8593 8548 8326 740 -926 -956 S
ATOM 1206 CE MET A 184 -6.752 12.952 25.957 1.00 61.86 C
ANISOU 1206 CE MET A 184 7802 7960 7743 548 -634 -769 C
ATOM 1207 N ILE A 185 -13.232 13.661 22.834 1.00 72.87 N
ANISOU 1207 N ILE A 185 9127 9133 9426 1596 -2272 -2080 N
ATOM 1208 CA ILE A 185 -14.283 13.441 21.837 1.00 73.61 C
ANISOU 1208 CA ILE A 185 9250 9169 9548 1809 -2616 -2343 C
ATOM 1209 C ILE A 185 -13.775 13.632 20.411 1.00 77.95 C
ANISOU 1209 C ILE A 185 10318 9530 9771 1884 -2786 -2165 C
ATOM 1210 O ILE A 185 -14.055 12.772 19.561 1.00 79.30 O
ANISOU 1210 O ILE A 185 10522 9708 9900 1919 -2843 -2245 O
ATOM 1211 CB ILE A 185 -15.506 14.320 22.156 1.00 71.67 C
ANISOU 1211 CB ILE A 185 8830 8891 9509 2050 -2979 -2682 C
ATOM 1212 CG1 ILE A 185 -16.178 13.852 23.448 1.00 71.80 C
ANISOU 1212 CG1 ILE A 185 8293 9130 9859 1946 -2772 -2929 C
ATOM 1213 CG2 ILE A 185 -16.498 14.299 21.003 1.00 70.53 C
ANISOU 1213 CG2 ILE A 185 8794 8638 9366 2316 -3420 -2948 C
ATOM 1214 CD1 ILE A 185 -17.382 14.679 23.843 1.00 67.32 C
ANISOU 1214 CD1 ILE A 185 7483 8564 9530 2172 -3088 -3314 C
ATOM 1215 N PRO A 186 -13.044 14.705 20.075 1.00 77.53 N
ANISOU 1215 N PRO A 186 10696 9297 9464 1895 -2864 -1933 N
ATOM 1216 CA PRO A 186 -12.533 14.816 18.697 1.00 78.31 C
ANISOU 1216 CA PRO A 186 11325 9215 9214 1919 -2977 -1763 C
ATOM 1217 C PRO A 186 -11.610 13.677 18.305 1.00 78.15 C
ANISOU 1217 C PRO A 186 11324 9297 9072 1702 -2604 -1578 C
ATOM 1218 O PRO A 186 -11.546 13.323 17.119 1.00 81.69 O
ANISOU 1218 O PRO A 186 12082 9655 9303 1742 -2699 -1553 O
ATOM 1219 CB PRO A 186 -11.800 16.166 18.698 1.00 80.77 C
ANISOU 1219 CB PRO A 186 12051 9338 9300 1888 -3029 -1532 C
ATOM 1220 CG PRO A 186 -11.509 16.444 20.128 1.00 77.14 C
ANISOU 1220 CG PRO A 186 11239 9014 9058 1769 -2791 -1493 C
ATOM 1221 CD PRO A 186 -12.673 15.887 20.876 1.00 77.32 C
ANISOU 1221 CD PRO A 186 10732 9208 9437 1877 -2861 -1823 C
ATOM 1222 N GLN A 187 -10.894 13.090 19.267 1.00 77.97 N
ANISOU 1222 N GLN A 187 10994 9453 9180 1484 -2200 -1460 N
ATOM 1223 CA GLN A 187 -10.052 11.937 18.965 1.00 78.60 C
ANISOU 1223 CA GLN A 187 11046 9634 9185 1304 -1869 -1326 C
ATOM 1224 C GLN A 187 -10.888 10.782 18.431 1.00 78.81 C
ANISOU 1224 C GLN A 187 10907 9727 9312 1389 -1965 -1542 C
ATOM 1225 O GLN A 187 -10.530 10.152 17.429 1.00 80.37 O
ANISOU 1225 O GLN A 187 11318 9894 9325 1367 -1921 -1486 O
ATOM 1226 CB GLN A 187 -9.280 11.511 20.214 1.00 77.72 C
ANISOU 1226 CB GLN A 187 10612 9683 9235 1097 -1490 -1208 C
ATOM 1227 CG GLN A 187 -8.304 10.368 19.984 1.00 75.11 C
ANISOU 1227 CG GLN A 187 10251 9444 8842 928 -1164 -1077 C
ATOM 1228 CD GLN A 187 -7.136 10.767 19.102 1.00 76.86 C
ANISOU 1228 CD GLN A 187 10866 9575 8763 834 -1041 -858 C
ATOM 1229 OE1 GLN A 187 -6.708 11.922 19.102 1.00 77.66 O
ANISOU 1229 OE1 GLN A 187 11209 9569 8728 807 -1078 -731 O
ATOM 1230 NE2 GLN A 187 -6.617 9.811 18.339 1.00 75.91 N
ANISOU 1230 NE2 GLN A 187 10816 9494 8532 769 -883 -828 N
ATOM 1231 N ALA A 188 -12.019 10.499 19.082 1.00 78.29 N
ANISOU 1231 N ALA A 188 10457 9753 9537 1476 -2089 -1811 N
ATOM 1232 CA ALA A 188 -12.914 9.459 18.586 1.00 79.33 C
ANISOU 1232 CA ALA A 188 10414 9941 9788 1551 -2203 -2052 C
ATOM 1233 C ALA A 188 -13.613 9.886 17.302 1.00 80.73 C
ANISOU 1233 C ALA A 188 10909 9950 9815 1793 -2632 -2190 C
ATOM 1234 O ALA A 188 -13.964 9.035 16.477 1.00 81.34 O
ANISOU 1234 O ALA A 188 11017 10026 9861 1843 -2716 -2300 O
ATOM 1235 CB ALA A 188 -13.945 9.094 19.654 1.00 74.47 C
ANISOU 1235 CB ALA A 188 9295 9473 9529 1543 -2195 -2330 C
ATOM 1236 N ILE A 189 -13.832 11.191 17.123 1.00 79.78 N
ANISOU 1236 N ILE A 189 11048 9670 9596 1953 -2930 -2193 N
ATOM 1237 CA ILE A 189 -14.483 11.680 15.911 1.00 77.80 C
ANISOU 1237 CA ILE A 189 11168 9216 9175 2204 -3391 -2319 C
ATOM 1238 C ILE A 189 -13.606 11.432 14.688 1.00 80.55 C
ANISOU 1238 C ILE A 189 12023 9445 9137 2132 -3316 -2082 C
ATOM 1239 O ILE A 189 -14.093 10.996 13.637 1.00 82.47 O
ANISOU 1239 O ILE A 189 12457 9607 9272 2264 -3554 -2206 O
ATOM 1240 CB ILE A 189 -14.835 13.171 16.062 1.00 76.76 C
ANISOU 1240 CB ILE A 189 11245 8910 9009 2388 -3735 -2359 C
ATOM 1241 CG1 ILE A 189 -15.974 13.354 17.067 1.00 77.53 C
ANISOU 1241 CG1 ILE A 189 10824 9125 9508 2518 -3889 -2701 C
ATOM 1242 CG2 ILE A 189 -15.208 13.776 14.717 1.00 77.51 C
ANISOU 1242 CG2 ILE A 189 11892 8733 8826 2624 -4207 -2403 C
ATOM 1243 CD1 ILE A 189 -17.255 12.654 16.673 1.00 82.82 C
ANISOU 1243 CD1 ILE A 189 11208 9852 10408 2700 -4168 -3098 C
ATOM 1244 N VAL A 190 -12.300 11.697 14.802 1.00 85.39 N
ANISOU 1244 N VAL A 190 12855 10050 9538 1914 -2976 -1759 N
ATOM 1245 CA VAL A 190 -11.422 11.668 13.632 1.00 85.06 C
ANISOU 1245 CA VAL A 190 13334 9884 9101 1826 -2887 -1546 C
ATOM 1246 C VAL A 190 -10.932 10.276 13.267 1.00 87.77 C
ANISOU 1246 C VAL A 190 13547 10373 9430 1687 -2580 -1518 C
ATOM 1247 O VAL A 190 -10.232 10.130 12.256 1.00 90.35 O
ANISOU 1247 O VAL A 190 14275 10619 9434 1609 -2480 -1378 O
ATOM 1248 CB VAL A 190 -10.198 12.581 13.838 1.00 87.53 C
ANISOU 1248 CB VAL A 190 13940 10126 9192 1631 -2640 -1243 C
ATOM 1249 CG1 VAL A 190 -10.645 14.013 14.077 1.00 90.12 C
ANISOU 1249 CG1 VAL A 190 14486 10268 9489 1774 -2975 -1257 C
ATOM 1250 CG2 VAL A 190 -9.346 12.076 14.992 1.00 87.07 C
ANISOU 1250 CG2 VAL A 190 13453 10290 9340 1402 -2179 -1124 C
ATOM 1251 N MET A 191 -11.271 9.249 14.043 1.00 83.64 N
ANISOU 1251 N MET A 191 12500 10050 9229 1645 -2423 -1653 N
ATOM 1252 CA MET A 191 -10.823 7.894 13.736 1.00 84.76 C
ANISOU 1252 CA MET A 191 12522 10312 9370 1525 -2156 -1637 C
ATOM 1253 C MET A 191 -11.662 7.320 12.599 1.00 87.40 C
ANISOU 1253 C MET A 191 13008 10572 9630 1696 -2454 -1833 C
ATOM 1254 O MET A 191 -12.890 7.238 12.706 1.00 88.69 O
ANISOU 1254 O MET A 191 12953 10734 10010 1869 -2764 -2101 O
ATOM 1255 CB MET A 191 -10.912 7.002 14.972 1.00 83.53 C
ANISOU 1255 CB MET A 191 11816 10358 9562 1410 -1907 -1706 C
ATOM 1256 CG MET A 191 -9.993 7.414 16.109 1.00 81.09 C
ANISOU 1256 CG MET A 191 11362 10126 9323 1236 -1601 -1511 C
ATOM 1257 SD MET A 191 -8.276 7.634 15.602 1.00 76.11 S
ANISOU 1257 SD MET A 191 11077 9464 8378 1052 -1272 -1203 S
ATOM 1258 CE MET A 191 -7.856 5.972 15.088 1.00 80.82 C
ANISOU 1258 CE MET A 191 11565 10166 8977 977 -1048 -1241 C
ATOM 1259 N GLU A 192 -10.998 6.924 11.513 1.00 86.84 N
ANISOU 1259 N GLU A 192 13297 10441 9256 1645 -2358 -1723 N
ATOM 1260 CA GLU A 192 -11.665 6.352 10.351 1.00 87.99 C
ANISOU 1260 CA GLU A 192 13644 10504 9284 1797 -2627 -1889 C
ATOM 1261 C GLU A 192 -10.855 5.176 9.826 1.00 88.72 C
ANISOU 1261 C GLU A 192 13765 10685 9260 1654 -2306 -1814 C
ATOM 1262 O GLU A 192 -9.621 5.184 9.865 1.00 89.22 O
ANISOU 1262 O GLU A 192 13937 10793 9168 1464 -1942 -1600 O
ATOM 1263 CB GLU A 192 -11.856 7.394 9.235 1.00 87.54 C
ANISOU 1263 CB GLU A 192 14201 10194 8866 1946 -2982 -1857 C
ATOM 1264 CG GLU A 192 -12.621 8.645 9.654 1.00 90.05 C
ANISOU 1264 CG GLU A 192 14560 10385 9271 2121 -3352 -1939 C
ATOM 1265 CD GLU A 192 -14.070 8.364 10.007 1.00 90.16 C
ANISOU 1265 CD GLU A 192 14161 10446 9651 2345 -3711 -2291 C
ATOM 1266 OE1 GLU A 192 -14.600 7.317 9.579 1.00 93.18 O
ANISOU 1266 OE1 GLU A 192 14379 10891 10133 2399 -3778 -2476 O
ATOM 1267 OE2 GLU A 192 -14.681 9.194 10.715 1.00 85.05 O
ANISOU 1267 OE2 GLU A 192 13341 9774 9199 2461 -3921 -2402 O
ATOM 1268 N CYS A 193 -11.565 4.164 9.322 1.00 93.66 N
ANISOU 1268 N CYS A 193 14279 11334 9973 1751 -2454 -2018 N
ATOM 1269 CA CYS A 193 -10.946 2.957 8.770 1.00 92.64 C
ANISOU 1269 CA CYS A 193 14167 11277 9753 1652 -2203 -1993 C
ATOM 1270 C CYS A 193 -10.706 3.164 7.280 1.00 99.02 C
ANISOU 1270 C CYS A 193 15562 11926 10136 1715 -2333 -1952 C
ATOM 1271 O CYS A 193 -11.585 2.927 6.450 1.00101.75 O
ANISOU 1271 O CYS A 193 16070 12171 10421 1894 -2682 -2133 O
ATOM 1272 CB CYS A 193 -11.825 1.735 9.014 1.00 92.06 C
ANISOU 1272 CB CYS A 193 13690 11299 9988 1703 -2286 -2234 C
ATOM 1273 SG CYS A 193 -11.861 1.114 10.707 1.00 96.57 S
ANISOU 1273 SG CYS A 193 13631 12063 10997 1545 -2010 -2258 S
ATOM 1274 N SER A 194 -9.502 3.610 6.931 1.00 98.67 N
ANISOU 1274 N SER A 194 15847 11855 9787 1555 -2045 -1726 N
ATOM 1275 CA SER A 194 -9.123 3.735 5.534 1.00104.55 C
ANISOU 1275 CA SER A 194 17176 12460 10088 1554 -2078 -1674 C
ATOM 1276 C SER A 194 -8.745 2.372 4.965 1.00106.76 C
ANISOU 1276 C SER A 194 17385 12841 10337 1505 -1870 -1747 C
ATOM 1277 O SER A 194 -8.256 1.487 5.677 1.00102.20 O
ANISOU 1277 O SER A 194 16380 12443 10010 1398 -1567 -1750 O
ATOM 1278 CB SER A 194 -7.952 4.706 5.378 1.00106.60 C
ANISOU 1278 CB SER A 194 17808 12664 10033 1357 -1799 -1427 C
ATOM 1279 OG SER A 194 -8.242 5.953 5.982 1.00106.61 O
ANISOU 1279 OG SER A 194 17864 12567 10076 1393 -1980 -1352 O
ATOM 1280 N THR A 195 -8.976 2.211 3.664 1.00114.70 N
ANISOU 1280 N THR A 195 18845 13713 11021 1593 -2055 -1814 N
ATOM 1281 CA THR A 195 -8.703 0.968 2.951 1.00118.65 C
ANISOU 1281 CA THR A 195 19353 14281 11449 1575 -1910 -1906 C
ATOM 1282 C THR A 195 -7.582 1.147 1.931 1.00125.88 C
ANISOU 1282 C THR A 195 20777 15150 11900 1415 -1618 -1776 C
ATOM 1283 O THR A 195 -7.636 0.613 0.821 1.00128.61 O
ANISOU 1283 O THR A 195 21448 15431 11986 1462 -1680 -1860 O
ATOM 1284 CB THR A 195 -9.965 0.448 2.267 1.00121.60 C
ANISOU 1284 CB THR A 195 19793 14553 11855 1810 -2365 -2140 C
ATOM 1285 OG1 THR A 195 -10.451 1.431 1.343 1.00124.66 O
ANISOU 1285 OG1 THR A 195 20764 14705 11897 1944 -2741 -2137 O
ATOM 1286 CG2 THR A 195 -11.044 0.150 3.297 1.00118.78 C
ANISOU 1286 CG2 THR A 195 18873 14275 11985 1925 -2588 -2312 C
ATOM 1287 N VAL A 196 -6.552 1.903 2.299 1.00135.68 N
ANISOU 1287 N VAL A 196 22092 16428 13033 1211 -1286 -1583 N
ATOM 1288 CA VAL A 196 -5.415 2.130 1.416 1.00138.56 C
ANISOU 1288 CA VAL A 196 22904 16771 12973 1006 -941 -1476 C
ATOM 1289 C VAL A 196 -4.177 1.426 1.959 1.00136.57 C
ANISOU 1289 C VAL A 196 22248 16753 12889 810 -417 -1454 C
ATOM 1290 O VAL A 196 -3.545 0.632 1.262 1.00134.61 O
ANISOU 1290 O VAL A 196 22076 16579 12493 738 -167 -1527 O
ATOM 1291 CB VAL A 196 -5.144 3.632 1.228 1.00142.86 C
ANISOU 1291 CB VAL A 196 23939 17143 13197 895 -968 -1293 C
ATOM 1292 CG1 VAL A 196 -3.961 3.845 0.295 1.00144.08 C
ANISOU 1292 CG1 VAL A 196 24569 17280 12896 634 -564 -1200 C
ATOM 1293 CG2 VAL A 196 -6.385 4.331 0.695 1.00141.68 C
ANISOU 1293 CG2 VAL A 196 24208 16735 12888 1128 -1547 -1336 C
ATOM 1294 N THR A 205 0.354 -6.272 -2.030 1.00118.09 N
ANISOU 1294 N THR A 205 19456 15185 10226 630 1360 -2504 N
ATOM 1295 CA THR A 205 -0.991 -6.195 -1.471 1.00119.70 C
ANISOU 1295 CA THR A 205 19571 15266 10645 811 883 -2432 C
ATOM 1296 C THR A 205 -1.107 -5.039 -0.484 1.00121.87 C
ANISOU 1296 C THR A 205 19731 15519 11057 739 832 -2232 C
ATOM 1297 O THR A 205 -0.146 -4.701 0.208 1.00120.04 O
ANISOU 1297 O THR A 205 19252 15406 10950 591 1147 -2169 O
ATOM 1298 CB THR A 205 -1.387 -7.507 -0.765 1.00114.06 C
ANISOU 1298 CB THR A 205 18366 14607 10367 974 735 -2559 C
ATOM 1299 OG1 THR A 205 -0.437 -7.805 0.265 1.00105.81 O
ANISOU 1299 OG1 THR A 205 16854 13713 9638 900 1018 -2556 O
ATOM 1300 CG2 THR A 205 -1.426 -8.657 -1.759 1.00107.28 C
ANISOU 1300 CG2 THR A 205 17641 13740 9379 1072 719 -2763 C
ATOM 1301 N LEU A 206 -2.289 -4.433 -0.428 1.00140.80 N
ANISOU 1301 N LEU A 206 22298 17762 13436 855 421 -2156 N
ATOM 1302 CA LEU A 206 -2.561 -3.323 0.467 1.00142.02 C
ANISOU 1302 CA LEU A 206 22369 17876 13717 820 314 -1987 C
ATOM 1303 C LEU A 206 -3.226 -3.840 1.742 1.00137.89 C
ANISOU 1303 C LEU A 206 21293 17407 13692 939 124 -2012 C
ATOM 1304 O LEU A 206 -3.310 -5.049 1.983 1.00139.36 O
ANISOU 1304 O LEU A 206 21166 17665 14121 1014 125 -2142 O
ATOM 1305 CB LEU A 206 -3.414 -2.272 -0.245 1.00143.35 C
ANISOU 1305 CB LEU A 206 23078 17831 13557 880 -28 -1912 C
ATOM 1306 CG LEU A 206 -2.732 -1.546 -1.407 1.00147.77 C
ANISOU 1306 CG LEU A 206 24270 18302 13574 712 174 -1844 C
ATOM 1307 CD1 LEU A 206 -3.635 -0.461 -1.970 1.00150.12 C
ANISOU 1307 CD1 LEU A 206 25123 18347 13568 796 -235 -1757 C
ATOM 1308 CD2 LEU A 206 -1.397 -0.964 -0.966 1.00148.85 C
ANISOU 1308 CD2 LEU A 206 24312 18564 13682 441 661 -1731 C
ATOM 1309 N PHE A 207 -3.709 -2.918 2.571 1.00120.45 N
ANISOU 1309 N PHE A 207 18986 15153 11624 945 -39 -1893 N
ATOM 1310 CA PHE A 207 -4.251 -3.273 3.873 1.00113.53 C
ANISOU 1310 CA PHE A 207 17603 14337 11196 1009 -159 -1907 C
ATOM 1311 C PHE A 207 -5.281 -2.235 4.295 1.00114.11 C
ANISOU 1311 C PHE A 207 17727 14303 11327 1089 -494 -1846 C
ATOM 1312 O PHE A 207 -5.383 -1.152 3.713 1.00116.15 O
ANISOU 1312 O PHE A 207 18400 14439 11291 1083 -605 -1762 O
ATOM 1313 CB PHE A 207 -3.138 -3.391 4.919 1.00106.64 C
ANISOU 1313 CB PHE A 207 16357 13613 10549 869 198 -1830 C
ATOM 1314 CG PHE A 207 -2.038 -2.378 4.754 1.00106.65 C
ANISOU 1314 CG PHE A 207 16563 13642 10318 690 498 -1696 C
ATOM 1315 CD1 PHE A 207 -2.263 -1.038 5.016 1.00108.73 C
ANISOU 1315 CD1 PHE A 207 17005 13821 10486 641 401 -1547 C
ATOM 1316 CD2 PHE A 207 -0.775 -2.769 4.343 1.00106.12 C
ANISOU 1316 CD2 PHE A 207 16499 13682 10138 563 881 -1742 C
ATOM 1317 CE1 PHE A 207 -1.252 -0.107 4.869 1.00108.61 C
ANISOU 1317 CE1 PHE A 207 17192 13820 10255 447 687 -1426 C
ATOM 1318 CE2 PHE A 207 0.241 -1.843 4.193 1.00106.46 C
ANISOU 1318 CE2 PHE A 207 16710 13761 9982 364 1185 -1645 C
ATOM 1319 CZ PHE A 207 0.001 -0.510 4.456 1.00106.07 C
ANISOU 1319 CZ PHE A 207 16860 13616 9826 294 1092 -1477 C
ATOM 1320 N THR A 208 -6.053 -2.585 5.321 1.00106.72 N
ANISOU 1320 N THR A 208 16377 13404 10769 1159 -656 -1904 N
ATOM 1321 CA THR A 208 -7.042 -1.694 5.915 1.00104.39 C
ANISOU 1321 CA THR A 208 16016 13039 10608 1238 -952 -1892 C
ATOM 1322 C THR A 208 -6.525 -1.234 7.272 1.00 95.87 C
ANISOU 1322 C THR A 208 14607 12055 9764 1119 -745 -1760 C
ATOM 1323 O THR A 208 -6.255 -2.061 8.150 1.00 94.76 O
ANISOU 1323 O THR A 208 14081 12024 9900 1062 -578 -1781 O
ATOM 1324 CB THR A 208 -8.395 -2.393 6.061 1.00106.04 C
ANISOU 1324 CB THR A 208 15992 13226 11071 1388 -1284 -2097 C
ATOM 1325 OG1 THR A 208 -8.247 -3.562 6.877 1.00110.66 O
ANISOU 1325 OG1 THR A 208 16152 13928 11965 1322 -1108 -2154 O
ATOM 1326 CG2 THR A 208 -8.931 -2.801 4.698 1.00105.38 C
ANISOU 1326 CG2 THR A 208 16251 13036 10754 1522 -1528 -2238 C
ATOM 1327 N VAL A 209 -6.387 0.080 7.441 1.00 96.89 N
ANISOU 1327 N VAL A 209 14918 12125 9772 1083 -773 -1625 N
ATOM 1328 CA VAL A 209 -5.822 0.662 8.654 1.00 93.31 C
ANISOU 1328 CA VAL A 209 14208 11747 9499 966 -579 -1490 C
ATOM 1329 C VAL A 209 -6.766 1.735 9.170 1.00 92.16 C
ANISOU 1329 C VAL A 209 14059 11517 9440 1056 -876 -1484 C
ATOM 1330 O VAL A 209 -7.271 2.554 8.396 1.00 92.54 O
ANISOU 1330 O VAL A 209 14486 11418 9256 1151 -1138 -1488 O
ATOM 1331 CB VAL A 209 -4.419 1.257 8.407 1.00 91.50 C
ANISOU 1331 CB VAL A 209 14190 11543 9034 789 -236 -1327 C
ATOM 1332 CG1 VAL A 209 -3.909 1.965 9.655 1.00 90.83 C
ANISOU 1332 CG1 VAL A 209 13855 11519 9137 682 -86 -1196 C
ATOM 1333 CG2 VAL A 209 -3.454 0.174 7.988 1.00 94.86 C
ANISOU 1333 CG2 VAL A 209 14549 12074 9420 710 69 -1378 C
ATOM 1334 N CYS A 210 -7.007 1.734 10.477 1.00 85.93 N
ANISOU 1334 N CYS A 210 12863 10810 8975 1031 -849 -1485 N
ATOM 1335 CA CYS A 210 -7.779 2.797 11.101 1.00 88.45 C
ANISOU 1335 CA CYS A 210 13134 11071 9399 1103 -1083 -1489 C
ATOM 1336 C CYS A 210 -6.822 3.869 11.607 1.00 83.86 C
ANISOU 1336 C CYS A 210 12647 10488 8729 972 -883 -1281 C
ATOM 1337 O CYS A 210 -5.950 3.590 12.438 1.00 82.06 O
ANISOU 1337 O CYS A 210 12171 10373 8637 833 -583 -1189 O
ATOM 1338 CB CYS A 210 -8.643 2.265 12.240 1.00 87.38 C
ANISOU 1338 CB CYS A 210 12524 11025 9650 1131 -1155 -1627 C
ATOM 1339 SG CYS A 210 -10.019 3.365 12.600 1.00 93.43 S
ANISOU 1339 SG CYS A 210 13242 11712 10546 1296 -1556 -1766 S
ATOM 1340 N ASP A 211 -6.988 5.090 11.107 1.00 83.15 N
ANISOU 1340 N ASP A 211 12931 10252 8411 1021 -1070 -1215 N
ATOM 1341 CA ASP A 211 -6.088 6.191 11.424 1.00 83.56 C
ANISOU 1341 CA ASP A 211 13146 10269 8333 882 -897 -1018 C
ATOM 1342 C ASP A 211 -6.931 7.440 11.668 1.00 83.38 C
ANISOU 1342 C ASP A 211 13264 10106 8311 1009 -1239 -1026 C
ATOM 1343 O ASP A 211 -8.153 7.368 11.828 1.00 82.06 O
ANISOU 1343 O ASP A 211 12948 9912 8320 1196 -1567 -1205 O
ATOM 1344 CB ASP A 211 -5.054 6.378 10.304 1.00 83.04 C
ANISOU 1344 CB ASP A 211 13527 10144 7881 743 -683 -900 C
ATOM 1345 CG ASP A 211 -3.831 7.152 10.759 1.00 85.67 C
ANISOU 1345 CG ASP A 211 13901 10506 8143 526 -364 -716 C
ATOM 1346 OD1 ASP A 211 -3.168 6.709 11.721 1.00 93.12 O
ANISOU 1346 OD1 ASP A 211 14439 11607 9335 428 -104 -692 O
ATOM 1347 OD2 ASP A 211 -3.530 8.203 10.153 1.00 83.55 O
ANISOU 1347 OD2 ASP A 211 14089 10090 7565 447 -384 -603 O
ATOM 1348 N GLU A 212 -6.271 8.593 11.721 1.00 84.44 N
ANISOU 1348 N GLU A 212 13670 10149 8263 903 -1164 -853 N
ATOM 1349 CA GLU A 212 -6.934 9.871 11.939 1.00 86.00 C
ANISOU 1349 CA GLU A 212 14053 10188 8436 1020 -1487 -846 C
ATOM 1350 C GLU A 212 -7.167 10.548 10.594 1.00 87.63 C
ANISOU 1350 C GLU A 212 14905 10151 8238 1097 -1756 -822 C
ATOM 1351 O GLU A 212 -6.216 10.789 9.843 1.00 88.21 O
ANISOU 1351 O GLU A 212 15382 10158 7976 918 -1534 -667 O
ATOM 1352 CB GLU A 212 -6.101 10.764 12.858 1.00 83.96 C
ANISOU 1352 CB GLU A 212 13731 9950 8220 856 -1270 -671 C
ATOM 1353 CG GLU A 212 -5.955 10.231 14.276 1.00 83.92 C
ANISOU 1353 CG GLU A 212 13138 10149 8599 801 -1066 -696 C
ATOM 1354 CD GLU A 212 -5.039 11.086 15.130 1.00 79.56 C
ANISOU 1354 CD GLU A 212 12543 9613 8073 635 -850 -524 C
ATOM 1355 OE1 GLU A 212 -4.433 10.545 16.079 1.00 72.09 O
ANISOU 1355 OE1 GLU A 212 11214 8830 7348 524 -580 -495 O
ATOM 1356 OE2 GLU A 212 -4.921 12.299 14.850 1.00 79.74 O
ANISOU 1356 OE2 GLU A 212 12938 9470 7891 616 -968 -422 O
ATOM 1357 N ARG A 213 -8.428 10.846 10.293 1.00 88.37 N
ANISOU 1357 N ARG A 213 15104 10110 8364 1358 -2234 -991 N
ATOM 1358 CA ARG A 213 -8.817 11.545 9.074 1.00 91.07 C
ANISOU 1358 CA ARG A 213 16093 10178 8331 1482 -2592 -991 C
ATOM 1359 C ARG A 213 -9.339 12.924 9.449 1.00 91.06 C
ANISOU 1359 C ARG A 213 16285 9986 8330 1616 -2942 -984 C
ATOM 1360 O ARG A 213 -10.359 13.040 10.136 1.00 88.69 O
ANISOU 1360 O ARG A 213 15627 9718 8355 1828 -3235 -1182 O
ATOM 1361 CB ARG A 213 -9.878 10.761 8.300 1.00 97.16 C
ANISOU 1361 CB ARG A 213 16872 10915 9130 1717 -2935 -1229 C
ATOM 1362 CG ARG A 213 -9.326 9.633 7.438 1.00102.81 C
ANISOU 1362 CG ARG A 213 17684 11711 9667 1603 -2676 -1212 C
ATOM 1363 CD ARG A 213 -8.735 10.168 6.143 1.00106.75 C
ANISOU 1363 CD ARG A 213 18941 11992 9629 1511 -2676 -1061 C
ATOM 1364 NE ARG A 213 -8.259 9.100 5.273 1.00114.07 N
ANISOU 1364 NE ARG A 213 19970 12996 10376 1416 -2439 -1076 N
ATOM 1365 CZ ARG A 213 -9.014 8.461 4.389 1.00112.75 C
ANISOU 1365 CZ ARG A 213 19957 12758 10126 1600 -2729 -1246 C
ATOM 1366 NH1 ARG A 213 -10.298 8.744 4.243 1.00112.29 N
ANISOU 1366 NH1 ARG A 213 19943 12557 10166 1895 -3278 -1435 N
ATOM 1367 NH2 ARG A 213 -8.466 7.514 3.633 1.00112.89 N
ANISOU 1367 NH2 ARG A 213 20073 12852 9969 1492 -2471 -1250 N
ATOM 1368 N TRP A 214 -8.639 13.962 9.002 1.00 91.90 N
ANISOU 1368 N TRP A 214 16955 9891 8073 1481 -2904 -773 N
ATOM 1369 CA TRP A 214 -9.008 15.340 9.278 1.00 95.86 C
ANISOU 1369 CA TRP A 214 17734 10170 8520 1591 -3236 -739 C
ATOM 1370 C TRP A 214 -9.279 16.080 7.975 1.00100.48 C
ANISOU 1370 C TRP A 214 19138 10400 8639 1691 -3622 -701 C
ATOM 1371 O TRP A 214 -8.751 15.723 6.916 1.00102.43 O
ANISOU 1371 O TRP A 214 19818 10580 8523 1553 -3471 -607 O
ATOM 1372 CB TRP A 214 -7.909 16.065 10.053 1.00 99.16 C
ANISOU 1372 CB TRP A 214 18127 10627 8922 1318 -2863 -507 C
ATOM 1373 CG TRP A 214 -7.585 15.466 11.394 1.00 96.60 C
ANISOU 1373 CG TRP A 214 17065 10613 9025 1221 -2516 -527 C
ATOM 1374 CD1 TRP A 214 -6.922 14.296 11.634 1.00 93.02 C
ANISOU 1374 CD1 TRP A 214 16216 10417 8709 1055 -2090 -512 C
ATOM 1375 CD2 TRP A 214 -7.878 16.031 12.678 1.00 93.56 C
ANISOU 1375 CD2 TRP A 214 16297 10291 8961 1282 -2577 -565 C
ATOM 1376 NE1 TRP A 214 -6.800 14.090 12.987 1.00 90.37 N
ANISOU 1376 NE1 TRP A 214 15303 10285 8749 1012 -1901 -531 N
ATOM 1377 CE2 TRP A 214 -7.377 15.141 13.650 1.00 91.50 C
ANISOU 1377 CE2 TRP A 214 15440 10321 9005 1140 -2178 -562 C
ATOM 1378 CE3 TRP A 214 -8.522 17.198 13.101 1.00 94.45 C
ANISOU 1378 CE3 TRP A 214 16527 10232 9127 1453 -2945 -614 C
ATOM 1379 CZ2 TRP A 214 -7.500 15.381 15.018 1.00 90.35 C
ANISOU 1379 CZ2 TRP A 214 14839 10300 9191 1146 -2122 -595 C
ATOM 1380 CZ3 TRP A 214 -8.643 17.435 14.460 1.00 96.35 C
ANISOU 1380 CZ3 TRP A 214 16278 10615 9717 1463 -2873 -660 C
ATOM 1381 CH2 TRP A 214 -8.136 16.531 15.401 1.00 91.31 C
ANISOU 1381 CH2 TRP A 214 15072 10267 9355 1303 -2457 -645 C
ATOM 1382 N GLY A 215 -10.113 17.116 8.061 1.00110.94 N
ANISOU 1382 N GLY A 215 20696 11487 9969 1939 -4134 -788 N
ATOM 1383 CA GLY A 215 -10.426 17.897 6.874 1.00115.63 C
ANISOU 1383 CA GLY A 215 22128 11696 10111 2062 -4573 -755 C
ATOM 1384 C GLY A 215 -9.239 18.696 6.365 1.00118.14 C
ANISOU 1384 C GLY A 215 23124 11820 9943 1727 -4288 -435 C
ATOM 1385 O GLY A 215 -8.942 18.696 5.167 1.00124.57 O
ANISOU 1385 O GLY A 215 24601 12439 10290 1630 -4301 -339 O
ATOM 1386 N GLY A 216 -8.542 19.383 7.270 1.00111.16 N
ANISOU 1386 N GLY A 216 22092 10987 9156 1527 -4013 -276 N
ATOM 1387 CA GLY A 216 -7.440 20.245 6.915 1.00109.91 C
ANISOU 1387 CA GLY A 216 22534 10646 8579 1186 -3739 7 C
ATOM 1388 C GLY A 216 -6.096 19.730 7.408 1.00111.85 C
ANISOU 1388 C GLY A 216 22402 11193 8904 786 -3014 163 C
ATOM 1389 O GLY A 216 -5.984 18.696 8.062 1.00112.48 O
ANISOU 1389 O GLY A 216 21769 11613 9356 781 -2733 68 O
ATOM 1390 N GLU A 217 -5.058 20.493 7.068 1.00105.82 N
ANISOU 1390 N GLU A 217 22155 10280 7771 440 -2724 394 N
ATOM 1391 CA GLU A 217 -3.690 20.177 7.453 1.00105.54 C
ANISOU 1391 CA GLU A 217 21830 10494 7776 39 -2050 527 C
ATOM 1392 C GLU A 217 -3.196 21.028 8.617 1.00103.92 C
ANISOU 1392 C GLU A 217 21373 10324 7790 -90 -1911 630 C
ATOM 1393 O GLU A 217 -2.015 20.949 8.972 1.00105.38 O
ANISOU 1393 O GLU A 217 21354 10682 8005 -430 -1384 736 O
ATOM 1394 CB GLU A 217 -2.753 20.340 6.252 1.00109.06 C
ANISOU 1394 CB GLU A 217 22972 10795 7671 -320 -1727 681 C
ATOM 1395 CG GLU A 217 -3.090 19.432 5.074 1.00114.09 C
ANISOU 1395 CG GLU A 217 23866 11419 8064 -233 -1793 584 C
ATOM 1396 CD GLU A 217 -2.173 19.646 3.882 1.00121.12 C
ANISOU 1396 CD GLU A 217 25350 12160 8510 -607 -1432 702 C
ATOM 1397 OE1 GLU A 217 -1.259 20.492 3.973 1.00120.81 O
ANISOU 1397 OE1 GLU A 217 25490 12037 8376 -949 -1116 843 O
ATOM 1398 OE2 GLU A 217 -2.369 18.967 2.851 1.00120.14 O
ANISOU 1398 OE2 GLU A 217 25417 12006 8226 -564 -1447 622 O
ATOM 1399 N ILE A 218 -4.069 21.835 9.217 1.00105.22 N
ANISOU 1399 N ILE A 218 21533 10328 8117 181 -2379 578 N
ATOM 1400 CA ILE A 218 -3.710 22.687 10.340 1.00106.25 C
ANISOU 1400 CA ILE A 218 21444 10471 8457 94 -2304 660 C
ATOM 1401 C ILE A 218 -4.423 22.263 11.619 1.00101.82 C
ANISOU 1401 C ILE A 218 20080 10155 8452 368 -2437 481 C
ATOM 1402 O ILE A 218 -3.810 22.219 12.688 1.00 97.10 O
ANISOU 1402 O ILE A 218 18987 9771 8137 226 -2119 523 O
ATOM 1403 CB ILE A 218 -3.991 24.171 10.011 1.00106.65 C
ANISOU 1403 CB ILE A 218 22244 10092 8186 130 -2709 767 C
ATOM 1404 CG1 ILE A 218 -3.926 25.041 11.271 1.00110.30 C
ANISOU 1404 CG1 ILE A 218 22416 10558 8934 147 -2757 797 C
ATOM 1405 CG2 ILE A 218 -5.332 24.319 9.306 1.00106.18 C
ANISOU 1405 CG2 ILE A 218 22565 9770 8010 539 -3374 613 C
ATOM 1406 CD1 ILE A 218 -2.560 25.084 11.922 1.00108.82 C
ANISOU 1406 CD1 ILE A 218 21949 10571 8826 -262 -2155 952 C
ATOM 1407 N TYR A 219 -5.711 21.932 11.526 1.00105.28 N
ANISOU 1407 N TYR A 219 18420 11287 10294 1495 -5008 253 N
ATOM 1408 CA TYR A 219 -6.457 21.433 12.681 1.00102.81 C
ANISOU 1408 CA TYR A 219 17418 11326 10318 1854 -5006 -49 C
ATOM 1409 C TYR A 219 -5.795 20.250 13.380 1.00 98.94 C
ANISOU 1409 C TYR A 219 16549 11199 9845 1627 -4568 -45 C
ATOM 1410 O TYR A 219 -5.735 20.258 14.621 1.00 95.40 O
ANISOU 1410 O TYR A 219 15721 10880 9646 1779 -4464 -168 O
ATOM 1411 CB TYR A 219 -7.886 21.078 12.245 1.00106.39 C
ANISOU 1411 CB TYR A 219 17545 12003 10875 2180 -5294 -329 C
ATOM 1412 CG TYR A 219 -8.896 22.173 12.501 1.00111.01 C
ANISOU 1412 CG TYR A 219 18100 12406 11673 2657 -5716 -554 C
ATOM 1413 CD1 TYR A 219 -9.038 23.235 11.617 1.00113.35 C
ANISOU 1413 CD1 TYR A 219 18996 12252 11818 2725 -6076 -455 C
ATOM 1414 CD2 TYR A 219 -9.710 22.142 13.625 1.00112.44 C
ANISOU 1414 CD2 TYR A 219 17664 12872 12187 3023 -5745 -896 C
ATOM 1415 CE1 TYR A 219 -9.962 24.238 11.849 1.00118.16 C
ANISOU 1415 CE1 TYR A 219 19615 12677 12604 3185 -6482 -701 C
ATOM 1416 CE2 TYR A 219 -10.636 23.139 13.866 1.00115.97 C
ANISOU 1416 CE2 TYR A 219 18081 13175 12807 3467 -6106 -1152 C
ATOM 1417 CZ TYR A 219 -10.759 24.184 12.975 1.00119.44 C
ANISOU 1417 CZ TYR A 219 19144 13144 13093 3566 -6490 -1060 C
ATOM 1418 OH TYR A 219 -11.681 25.178 13.213 1.00122.72 O
ANISOU 1418 OH TYR A 219 19565 13401 13663 4032 -6877 -1352 O
ATOM 1419 N PRO A 220 -5.298 19.214 12.681 1.00 98.34 N
ANISOU 1419 N PRO A 220 16534 11293 9538 1266 -4267 57 N
ATOM 1420 CA PRO A 220 -4.599 18.139 13.408 1.00 94.78 C
ANISOU 1420 CA PRO A 220 15599 11132 9282 1006 -3634 20 C
ATOM 1421 C PRO A 220 -3.408 18.638 14.200 1.00 90.80 C
ANISOU 1421 C PRO A 220 15161 10480 8858 823 -3325 186 C
ATOM 1422 O PRO A 220 -3.173 18.172 15.320 1.00 86.03 O
ANISOU 1422 O PRO A 220 14076 10071 8541 839 -3003 80 O
ATOM 1423 CB PRO A 220 -4.159 17.178 12.293 1.00 94.72 C
ANISOU 1423 CB PRO A 220 15761 11228 9001 639 -3357 114 C
ATOM 1424 CG PRO A 220 -4.970 17.524 11.122 1.00 96.99 C
ANISOU 1424 CG PRO A 220 16443 11393 9014 758 -3852 123 C
ATOM 1425 CD PRO A 220 -5.313 18.966 11.228 1.00 99.83 C
ANISOU 1425 CD PRO A 220 17116 11410 9406 1039 -4318 180 C
ATOM 1426 N LYS A 221 -2.653 19.590 13.652 1.00 93.79 N
ANISOU 1426 N LYS A 221 16147 10518 8970 624 -3431 446 N
ATOM 1427 CA LYS A 221 -1.450 20.058 14.331 1.00 91.34 C
ANISOU 1427 CA LYS A 221 15906 10094 8706 384 -3124 603 C
ATOM 1428 C LYS A 221 -1.794 20.830 15.599 1.00 86.25 C
ANISOU 1428 C LYS A 221 15054 9352 8367 725 -3323 489 C
ATOM 1429 O LYS A 221 -1.166 20.625 16.643 1.00 83.62 O
ANISOU 1429 O LYS A 221 14371 9141 8258 650 -2974 462 O
ATOM 1430 CB LYS A 221 -0.613 20.903 13.374 1.00 94.98 C
ANISOU 1430 CB LYS A 221 17098 10231 8758 19 -3197 902 C
ATOM 1431 CG LYS A 221 -0.338 20.191 12.058 1.00 97.60 C
ANISOU 1431 CG LYS A 221 17662 10677 8744 -315 -3018 989 C
ATOM 1432 CD LYS A 221 0.727 20.880 11.228 1.00 99.40 C
ANISOU 1432 CD LYS A 221 18457 10691 8620 -803 -2885 1246 C
ATOM 1433 CE LYS A 221 1.067 20.040 10.006 1.00100.26 C
ANISOU 1433 CE LYS A 221 18657 10996 8442 -1138 -2599 1267 C
ATOM 1434 NZ LYS A 221 2.237 20.571 9.258 1.00108.95 N
ANISOU 1434 NZ LYS A 221 20105 12003 9287 -1666 -2325 1435 N
ATOM 1435 N MET A 222 -2.798 21.709 15.535 1.00 87.29 N
ANISOU 1435 N MET A 222 15389 9270 8507 1126 -3901 399 N
ATOM 1436 CA MET A 222 -3.240 22.410 16.737 1.00 85.98 C
ANISOU 1436 CA MET A 222 14988 9045 8635 1507 -4109 226 C
ATOM 1437 C MET A 222 -3.797 21.436 17.768 1.00 82.87 C
ANISOU 1437 C MET A 222 13795 9103 8590 1686 -3838 -68 C
ATOM 1438 O MET A 222 -3.495 21.543 18.967 1.00 80.13 O
ANISOU 1438 O MET A 222 13137 8829 8479 1732 -3636 -142 O
ATOM 1439 CB MET A 222 -4.290 23.460 16.376 1.00 88.80 C
ANISOU 1439 CB MET A 222 15584 9128 9026 1901 -4657 88 C
ATOM 1440 CG MET A 222 -3.802 24.526 15.412 1.00 92.87 C
ANISOU 1440 CG MET A 222 16836 9162 9290 1662 -4826 321 C
ATOM 1441 SD MET A 222 -5.125 25.650 14.928 1.00107.19 S
ANISOU 1441 SD MET A 222 18881 10663 11184 2125 -5415 87 S
ATOM 1442 CE MET A 222 -5.656 26.252 16.528 1.00 99.56 C
ANISOU 1442 CE MET A 222 17478 9751 10599 2594 -5525 -237 C
ATOM 1443 N TYR A 223 -4.607 20.471 17.319 1.00 84.21 N
ANISOU 1443 N TYR A 223 13649 9578 8769 1751 -3831 -234 N
ATOM 1444 CA TYR A 223 -5.180 19.508 18.251 1.00 80.72 C
ANISOU 1444 CA TYR A 223 12494 9566 8608 1848 -3577 -506 C
ATOM 1445 C TYR A 223 -4.096 18.688 18.933 1.00 76.06 C
ANISOU 1445 C TYR A 223 11668 9115 8117 1491 -2979 -400 C
ATOM 1446 O TYR A 223 -4.176 18.421 20.134 1.00 74.08 O
ANISOU 1446 O TYR A 223 10977 9060 8111 1562 -2783 -547 O
ATOM 1447 CB TYR A 223 -6.168 18.585 17.539 1.00 83.20 C
ANISOU 1447 CB TYR A 223 12573 10168 8870 1892 -3667 -682 C
ATOM 1448 CG TYR A 223 -6.648 17.458 18.426 1.00 83.34 C
ANISOU 1448 CG TYR A 223 11919 10626 9121 1856 -3344 -926 C
ATOM 1449 CD1 TYR A 223 -7.569 17.691 19.439 1.00 84.89 C
ANISOU 1449 CD1 TYR A 223 11643 11059 9551 2170 -3488 -1233 C
ATOM 1450 CD2 TYR A 223 -6.167 16.164 18.263 1.00 82.28 C
ANISOU 1450 CD2 TYR A 223 11647 10664 8951 1494 -2899 -860 C
ATOM 1451 CE1 TYR A 223 -8.004 16.668 20.260 1.00 84.72 C
ANISOU 1451 CE1 TYR A 223 11049 11447 9695 2063 -3180 -1444 C
ATOM 1452 CE2 TYR A 223 -6.598 15.133 19.080 1.00 80.85 C
ANISOU 1452 CE2 TYR A 223 10937 10834 8948 1419 -2629 -1060 C
ATOM 1453 CZ TYR A 223 -7.517 15.391 20.076 1.00 81.42 C
ANISOU 1453 CZ TYR A 223 10566 11147 9224 1673 -2762 -1339 C
ATOM 1454 OH TYR A 223 -7.951 14.372 20.893 1.00 75.85 O
ANISOU 1454 OH TYR A 223 9372 10799 8649 1527 -2482 -1528 O
ATOM 1455 N HIS A 224 -3.069 18.281 18.187 1.00 78.00 N
ANISOU 1455 N HIS A 224 12202 9274 8161 1115 -2693 -163 N
ATOM 1456 CA HIS A 224 -2.011 17.472 18.778 1.00 74.42 C
ANISOU 1456 CA HIS A 224 11518 8958 7800 826 -2162 -92 C
ATOM 1457 C HIS A 224 -1.060 18.299 19.634 1.00 71.31 C
ANISOU 1457 C HIS A 224 11210 8392 7492 765 -2055 30 C
ATOM 1458 O HIS A 224 -0.490 17.771 20.593 1.00 68.48 O
ANISOU 1458 O HIS A 224 10521 8184 7314 677 -1714 1 O
ATOM 1459 CB HIS A 224 -1.253 16.718 17.686 1.00 75.36 C
ANISOU 1459 CB HIS A 224 11858 9098 7678 482 -1891 55 C
ATOM 1460 CG HIS A 224 -1.985 15.516 17.173 1.00 71.79 C
ANISOU 1460 CG HIS A 224 11190 8883 7205 479 -1838 -94 C
ATOM 1461 ND1 HIS A 224 -1.997 14.312 17.844 1.00 69.76 N
ANISOU 1461 ND1 HIS A 224 10506 8874 7127 421 -1518 -226 N
ATOM 1462 CD2 HIS A 224 -2.741 15.335 16.065 1.00 76.31 C
ANISOU 1462 CD2 HIS A 224 11944 9465 7583 511 -2087 -134 C
ATOM 1463 CE1 HIS A 224 -2.722 13.440 17.167 1.00 73.06 C
ANISOU 1463 CE1 HIS A 224 10857 9439 7463 396 -1559 -341 C
ATOM 1464 NE2 HIS A 224 -3.185 14.036 16.083 1.00 75.58 N
ANISOU 1464 NE2 HIS A 224 11518 9636 7563 455 -1898 -295 N
ATOM 1465 N ILE A 225 -0.887 19.588 19.330 1.00 76.57 N
ANISOU 1465 N ILE A 225 12340 8729 8024 804 -2364 165 N
ATOM 1466 CA ILE A 225 -0.166 20.468 20.247 1.00 71.41 C
ANISOU 1466 CA ILE A 225 11761 7903 7470 777 -2328 242 C
ATOM 1467 C ILE A 225 -0.897 20.540 21.582 1.00 67.52 C
ANISOU 1467 C ILE A 225 10817 7552 7288 1120 -2405 -2 C
ATOM 1468 O ILE A 225 -0.291 20.407 22.656 1.00 64.38 O
ANISOU 1468 O ILE A 225 10157 7245 7061 1046 -2132 -16 O
ATOM 1469 CB ILE A 225 0.014 21.866 19.627 1.00 73.92 C
ANISOU 1469 CB ILE A 225 12739 7791 7557 753 -2713 424 C
ATOM 1470 CG1 ILE A 225 1.061 21.831 18.512 1.00 77.18 C
ANISOU 1470 CG1 ILE A 225 13587 8103 7634 277 -2512 689 C
ATOM 1471 CG2 ILE A 225 0.404 22.881 20.692 1.00 69.43 C
ANISOU 1471 CG2 ILE A 225 12235 7019 7127 830 -2797 434 C
ATOM 1472 CD1 ILE A 225 1.230 23.151 17.792 1.00 75.49 C
ANISOU 1472 CD1 ILE A 225 14115 7446 7122 165 -2895 899 C
ATOM 1473 N CYS A 226 -2.219 20.733 21.531 1.00 67.07 N
ANISOU 1473 N CYS A 226 10643 7547 7293 1496 -2779 -222 N
ATOM 1474 CA CYS A 226 -3.011 20.739 22.758 1.00 65.96 C
ANISOU 1474 CA CYS A 226 10019 7623 7421 1809 -2828 -508 C
ATOM 1475 C CYS A 226 -2.942 19.390 23.465 1.00 63.38 C
ANISOU 1475 C CYS A 226 9155 7685 7242 1638 -2375 -606 C
ATOM 1476 O CYS A 226 -2.880 19.328 24.698 1.00 62.26 O
ANISOU 1476 O CYS A 226 8689 7682 7284 1683 -2210 -718 O
ATOM 1477 CB CYS A 226 -4.461 21.108 22.448 1.00 65.47 C
ANISOU 1477 CB CYS A 226 9876 7622 7379 2239 -3306 -771 C
ATOM 1478 SG CYS A 226 -4.693 22.804 21.882 1.00 78.52 S
ANISOU 1478 SG CYS A 226 12180 8762 8893 2564 -3950 -712 S
ATOM 1479 N PHE A 227 -2.959 18.301 22.696 1.00 66.73 N
ANISOU 1479 N PHE A 227 9524 8265 7567 1434 -2188 -565 N
ATOM 1480 CA PHE A 227 -2.875 16.962 23.270 1.00 63.03 C
ANISOU 1480 CA PHE A 227 8644 8100 7204 1252 -1793 -638 C
ATOM 1481 C PHE A 227 -1.559 16.767 24.012 1.00 59.49 C
ANISOU 1481 C PHE A 227 8185 7597 6822 1024 -1426 -478 C
ATOM 1482 O PHE A 227 -1.535 16.242 25.130 1.00 60.14 O
ANISOU 1482 O PHE A 227 7930 7857 7061 1004 -1215 -572 O
ATOM 1483 CB PHE A 227 -3.035 15.924 22.157 1.00 63.83 C
ANISOU 1483 CB PHE A 227 8800 8300 7154 1074 -1701 -608 C
ATOM 1484 CG PHE A 227 -3.065 14.501 22.640 1.00 59.55 C
ANISOU 1484 CG PHE A 227 7912 8021 6694 891 -1356 -693 C
ATOM 1485 CD1 PHE A 227 -1.893 13.774 22.775 1.00 57.39 C
ANISOU 1485 CD1 PHE A 227 7686 7707 6412 643 -988 -542 C
ATOM 1486 CD2 PHE A 227 -4.269 13.881 22.932 1.00 61.99 C
ANISOU 1486 CD2 PHE A 227 7865 8618 7071 960 -1420 -939 C
ATOM 1487 CE1 PHE A 227 -1.919 12.464 23.211 1.00 57.00 C
ANISOU 1487 CE1 PHE A 227 7399 7835 6422 495 -723 -614 C
ATOM 1488 CE2 PHE A 227 -4.301 12.570 23.366 1.00 61.30 C
ANISOU 1488 CE2 PHE A 227 7541 8727 7024 742 -1122 -999 C
ATOM 1489 CZ PHE A 227 -3.125 11.860 23.506 1.00 59.34 C
ANISOU 1489 CZ PHE A 227 7410 8371 6767 523 -791 -826 C
ATOM 1490 N PHE A 228 -0.451 17.189 23.402 1.00 58.25 N
ANISOU 1490 N PHE A 228 8395 7211 6525 833 -1354 -243 N
ATOM 1491 CA PHE A 228 0.848 17.060 24.051 1.00 57.10 C
ANISOU 1491 CA PHE A 228 8212 7046 6437 625 -1029 -114 C
ATOM 1492 C PHE A 228 0.931 17.929 25.299 1.00 59.23 C
ANISOU 1492 C PHE A 228 8385 7250 6869 762 -1109 -162 C
ATOM 1493 O PHE A 228 1.492 17.507 26.318 1.00 59.00 O
ANISOU 1493 O PHE A 228 8110 7334 6975 690 -861 -175 O
ATOM 1494 CB PHE A 228 1.963 17.417 23.071 1.00 55.04 C
ANISOU 1494 CB PHE A 228 8339 6610 5963 360 -941 110 C
ATOM 1495 CG PHE A 228 3.334 17.407 23.684 1.00 56.55 C
ANISOU 1495 CG PHE A 228 8466 6815 6205 148 -637 213 C
ATOM 1496 CD1 PHE A 228 3.966 16.210 23.981 1.00 57.88 C
ANISOU 1496 CD1 PHE A 228 8357 7187 6448 40 -292 181 C
ATOM 1497 CD2 PHE A 228 3.991 18.594 23.961 1.00 56.66 C
ANISOU 1497 CD2 PHE A 228 8711 6632 6186 63 -725 330 C
ATOM 1498 CE1 PHE A 228 5.228 16.198 24.544 1.00 55.74 C
ANISOU 1498 CE1 PHE A 228 7992 6956 6230 -116 -47 246 C
ATOM 1499 CE2 PHE A 228 5.252 18.588 24.525 1.00 58.90 C
ANISOU 1499 CE2 PHE A 228 8896 6970 6515 -145 -455 402 C
ATOM 1500 CZ PHE A 228 5.871 17.388 24.817 1.00 58.66 C
ANISOU 1500 CZ PHE A 228 8541 7178 6571 -218 -120 352 C
ATOM 1501 N LEU A 229 0.382 19.145 25.241 1.00 60.93 N
ANISOU 1501 N LEU A 229 8820 7268 7065 976 -1477 -197 N
ATOM 1502 CA LEU A 229 0.443 20.027 26.402 1.00 59.88 C
ANISOU 1502 CA LEU A 229 8628 7050 7074 1126 -1575 -266 C
ATOM 1503 C LEU A 229 -0.411 19.501 27.551 1.00 59.91 C
ANISOU 1503 C LEU A 229 8143 7350 7272 1319 -1514 -527 C
ATOM 1504 O LEU A 229 -0.023 19.612 28.721 1.00 58.47 O
ANISOU 1504 O LEU A 229 7784 7219 7212 1307 -1375 -565 O
ATOM 1505 CB LEU A 229 0.012 21.440 26.012 1.00 57.38 C
ANISOU 1505 CB LEU A 229 8715 6410 6676 1345 -2029 -266 C
ATOM 1506 CG LEU A 229 1.008 22.189 25.128 1.00 56.75 C
ANISOU 1506 CG LEU A 229 9196 5993 6374 1074 -2086 17 C
ATOM 1507 CD1 LEU A 229 0.515 23.596 24.838 1.00 59.33 C
ANISOU 1507 CD1 LEU A 229 9993 5938 6612 1309 -2592 16 C
ATOM 1508 CD2 LEU A 229 2.378 22.217 25.787 1.00 52.52 C
ANISOU 1508 CD2 LEU A 229 8629 5455 5872 760 -1753 162 C
ATOM 1509 N VAL A 230 -1.571 18.922 27.241 1.00 55.97 N
ANISOU 1509 N VAL A 230 7419 7069 6780 1463 -1610 -715 N
ATOM 1510 CA VAL A 230 -2.486 18.468 28.284 1.00 55.42 C
ANISOU 1510 CA VAL A 230 6881 7325 6852 1598 -1554 -991 C
ATOM 1511 C VAL A 230 -2.044 17.128 28.860 1.00 55.02 C
ANISOU 1511 C VAL A 230 6573 7493 6839 1314 -1143 -948 C
ATOM 1512 O VAL A 230 -2.101 16.915 30.076 1.00 54.77 O
ANISOU 1512 O VAL A 230 6274 7627 6907 1298 -994 -1056 O
ATOM 1513 CB VAL A 230 -3.920 18.403 27.729 1.00 54.87 C
ANISOU 1513 CB VAL A 230 6642 7444 6762 1836 -1829 -1240 C
ATOM 1514 CG1 VAL A 230 -4.844 17.684 28.701 1.00 53.57 C
ANISOU 1514 CG1 VAL A 230 5947 7709 6700 1855 -1687 -1532 C
ATOM 1515 CG2 VAL A 230 -4.436 19.804 27.439 1.00 57.43 C
ANISOU 1515 CG2 VAL A 230 7198 7545 7079 2211 -2297 -1339 C
ATOM 1516 N THR A 231 -1.604 16.200 28.009 1.00 58.77 N
ANISOU 1516 N THR A 231 7154 7957 7218 1093 -971 -799 N
ATOM 1517 CA THR A 231 -1.333 14.851 28.488 1.00 54.38 C
ANISOU 1517 CA THR A 231 6397 7577 6688 868 -646 -788 C
ATOM 1518 C THR A 231 0.066 14.704 29.073 1.00 54.45 C
ANISOU 1518 C THR A 231 6484 7466 6737 712 -402 -605 C
ATOM 1519 O THR A 231 0.251 13.928 30.016 1.00 58.08 O
ANISOU 1519 O THR A 231 6761 8049 7259 610 -203 -632 O
ATOM 1520 CB THR A 231 -1.530 13.835 27.359 1.00 56.66 C
ANISOU 1520 CB THR A 231 6758 7909 6859 730 -584 -755 C
ATOM 1521 OG1 THR A 231 -0.648 14.139 26.270 1.00 59.84 O
ANISOU 1521 OG1 THR A 231 7505 8085 7145 661 -590 -554 O
ATOM 1522 CG2 THR A 231 -2.971 13.858 26.869 1.00 56.47 C
ANISOU 1522 CG2 THR A 231 6593 8062 6800 867 -826 -968 C
ATOM 1523 N TYR A 232 1.059 15.416 28.542 1.00 54.49 N
ANISOU 1523 N TYR A 232 6764 7249 6691 671 -423 -426 N
ATOM 1524 CA TYR A 232 2.434 15.200 28.977 1.00 56.29 C
ANISOU 1524 CA TYR A 232 7020 7420 6950 510 -188 -280 C
ATOM 1525 C TYR A 232 3.097 16.437 29.565 1.00 57.17 C
ANISOU 1525 C TYR A 232 7236 7380 7105 535 -270 -213 C
ATOM 1526 O TYR A 232 3.642 16.365 30.669 1.00 54.17 O
ANISOU 1526 O TYR A 232 6712 7047 6825 505 -150 -215 O
ATOM 1527 CB TYR A 232 3.276 14.666 27.807 1.00 53.82 C
ANISOU 1527 CB TYR A 232 6887 7053 6511 340 -42 -145 C
ATOM 1528 CG TYR A 232 4.620 14.132 28.240 1.00 51.12 C
ANISOU 1528 CG TYR A 232 6476 6736 6211 206 217 -63 C
ATOM 1529 CD1 TYR A 232 4.750 12.832 28.710 1.00 48.82 C
ANISOU 1529 CD1 TYR A 232 6016 6554 5978 186 393 -114 C
ATOM 1530 CD2 TYR A 232 5.755 14.929 28.190 1.00 51.24 C
ANISOU 1530 CD2 TYR A 232 6604 6665 6198 98 264 52 C
ATOM 1531 CE1 TYR A 232 5.975 12.337 29.113 1.00 47.61 C
ANISOU 1531 CE1 TYR A 232 5797 6421 5872 126 579 -67 C
ATOM 1532 CE2 TYR A 232 6.986 14.443 28.591 1.00 50.53 C
ANISOU 1532 CE2 TYR A 232 6393 6650 6156 1 482 86 C
ATOM 1533 CZ TYR A 232 7.090 13.146 29.051 1.00 51.11 C
ANISOU 1533 CZ TYR A 232 6286 6829 6305 49 625 19 C
ATOM 1534 OH TYR A 232 8.312 12.654 29.453 1.00 53.12 O
ANISOU 1534 OH TYR A 232 6418 7152 6612 13 793 27 O
ATOM 1535 N MET A 233 3.055 17.577 28.874 1.00 57.22 N
ANISOU 1535 N MET A 233 7530 7186 7025 578 -494 -150 N
ATOM 1536 CA MET A 233 3.958 18.677 29.209 1.00 57.56 C
ANISOU 1536 CA MET A 233 7765 7042 7064 501 -541 -39 C
ATOM 1537 C MET A 233 3.542 19.404 30.486 1.00 55.74 C
ANISOU 1537 C MET A 233 7419 6793 6968 688 -680 -170 C
ATOM 1538 O MET A 233 4.285 19.420 31.476 1.00 53.39 O
ANISOU 1538 O MET A 233 7000 6533 6754 607 -539 -150 O
ATOM 1539 CB MET A 233 4.042 19.658 28.036 1.00 59.80 C
ANISOU 1539 CB MET A 233 8482 7072 7168 440 -758 86 C
ATOM 1540 CG MET A 233 4.914 20.874 28.307 1.00 61.49 C
ANISOU 1540 CG MET A 233 8969 7056 7340 305 -838 208 C
ATOM 1541 SD MET A 233 6.578 20.425 28.837 1.00 75.88 S
ANISOU 1541 SD MET A 233 10609 9025 9195 -20 -454 315 S
ATOM 1542 CE MET A 233 7.156 19.507 27.412 1.00 69.82 C
ANISOU 1542 CE MET A 233 9896 8385 8246 -262 -215 413 C
ATOM 1543 N ALA A 234 2.363 20.027 30.474 1.00 54.35 N
ANISOU 1543 N ALA A 234 7272 6571 6807 956 -970 -328 N
ATOM 1544 CA ALA A 234 1.932 20.821 31.624 1.00 54.96 C
ANISOU 1544 CA ALA A 234 7254 6633 6996 1167 -1121 -496 C
ATOM 1545 C ALA A 234 1.762 19.996 32.895 1.00 55.72 C
ANISOU 1545 C ALA A 234 6941 7022 7209 1160 -892 -633 C
ATOM 1546 O ALA A 234 2.236 20.442 33.958 1.00 56.15 O
ANISOU 1546 O ALA A 234 6953 7053 7329 1150 -854 -653 O
ATOM 1547 CB ALA A 234 0.645 21.578 31.274 1.00 51.23 C
ANISOU 1547 CB ALA A 234 6859 6091 6516 1511 -1499 -691 C
ATOM 1548 N PRO A 235 1.084 18.838 32.888 1.00 58.12 N
ANISOU 1548 N PRO A 235 6970 7594 7519 1141 -751 -732 N
ATOM 1549 CA PRO A 235 1.013 18.054 34.131 1.00 55.62 C
ANISOU 1549 CA PRO A 235 6345 7521 7266 1064 -533 -828 C
ATOM 1550 C PRO A 235 2.375 17.637 34.650 1.00 52.78 C
ANISOU 1550 C PRO A 235 6025 7103 6924 846 -307 -637 C
ATOM 1551 O PRO A 235 2.600 17.665 35.866 1.00 51.16 O
ANISOU 1551 O PRO A 235 5695 6973 6768 826 -232 -687 O
ATOM 1552 CB PRO A 235 0.153 16.845 33.733 1.00 56.31 C
ANISOU 1552 CB PRO A 235 6237 7847 7311 1003 -434 -918 C
ATOM 1553 CG PRO A 235 0.286 16.754 32.257 1.00 54.60 C
ANISOU 1553 CG PRO A 235 6243 7485 7016 977 -508 -788 C
ATOM 1554 CD PRO A 235 0.359 18.169 31.792 1.00 57.87 C
ANISOU 1554 CD PRO A 235 6924 7649 7416 1150 -788 -759 C
ATOM 1555 N LEU A 236 3.302 17.266 33.762 1.00 54.38 N
ANISOU 1555 N LEU A 236 6389 7195 7079 692 -206 -440 N
ATOM 1556 CA LEU A 236 4.637 16.889 34.216 1.00 53.04 C
ANISOU 1556 CA LEU A 236 6211 7006 6935 524 -16 -299 C
ATOM 1557 C LEU A 236 5.363 18.073 34.839 1.00 52.06 C
ANISOU 1557 C LEU A 236 6188 6745 6847 514 -101 -257 C
ATOM 1558 O LEU A 236 6.033 17.921 35.864 1.00 50.74 O
ANISOU 1558 O LEU A 236 5911 6631 6735 453 -4 -243 O
ATOM 1559 CB LEU A 236 5.453 16.306 33.064 1.00 53.18 C
ANISOU 1559 CB LEU A 236 6341 6981 6883 381 111 -153 C
ATOM 1560 CG LEU A 236 6.869 15.835 33.401 1.00 54.57 C
ANISOU 1560 CG LEU A 236 6459 7186 7089 244 299 -53 C
ATOM 1561 CD1 LEU A 236 6.838 14.730 34.445 1.00 52.35 C
ANISOU 1561 CD1 LEU A 236 5990 7029 6871 266 408 -106 C
ATOM 1562 CD2 LEU A 236 7.600 15.374 32.148 1.00 55.71 C
ANISOU 1562 CD2 LEU A 236 6692 7329 7146 126 422 34 C
ATOM 1563 N CYS A 237 5.245 19.260 34.237 1.00 51.20 N
ANISOU 1563 N CYS A 237 6323 6437 6693 565 -306 -233 N
ATOM 1564 CA CYS A 237 5.889 20.438 34.815 1.00 52.54 C
ANISOU 1564 CA CYS A 237 6643 6438 6881 530 -412 -199 C
ATOM 1565 C CYS A 237 5.311 20.767 36.186 1.00 52.84 C
ANISOU 1565 C CYS A 237 6522 6549 7007 698 -484 -381 C
ATOM 1566 O CYS A 237 6.056 21.055 37.135 1.00 54.12 O
ANISOU 1566 O CYS A 237 6650 6703 7209 616 -434 -362 O
ATOM 1567 CB CYS A 237 5.745 21.633 33.872 1.00 51.44 C
ANISOU 1567 CB CYS A 237 6881 6018 6646 549 -664 -139 C
ATOM 1568 SG CYS A 237 6.634 21.454 32.310 1.00 54.87 S
ANISOU 1568 SG CYS A 237 7563 6371 6915 256 -558 89 S
ATOM 1569 N LEU A 238 3.982 20.725 36.311 1.00 51.17 N
ANISOU 1569 N LEU A 238 6189 6440 6812 927 -596 -581 N
ATOM 1570 CA LEU A 238 3.357 21.016 37.598 1.00 49.51 C
ANISOU 1570 CA LEU A 238 5795 6358 6658 1080 -638 -801 C
ATOM 1571 C LEU A 238 3.766 19.995 38.652 1.00 48.14 C
ANISOU 1571 C LEU A 238 5383 6407 6501 920 -382 -786 C
ATOM 1572 O LEU A 238 4.071 20.358 39.796 1.00 51.15 O
ANISOU 1572 O LEU A 238 5719 6812 6904 911 -370 -844 O
ATOM 1573 CB LEU A 238 1.837 21.058 37.445 1.00 49.98 C
ANISOU 1573 CB LEU A 238 5701 6569 6720 1340 -782 -1061 C
ATOM 1574 CG LEU A 238 1.284 22.207 36.597 1.00 55.33 C
ANISOU 1574 CG LEU A 238 6634 7005 7383 1592 -1126 -1130 C
ATOM 1575 CD1 LEU A 238 -0.226 22.098 36.457 1.00 56.91 C
ANISOU 1575 CD1 LEU A 238 6595 7432 7596 1873 -1267 -1428 C
ATOM 1576 CD2 LEU A 238 1.673 23.553 37.193 1.00 52.93 C
ANISOU 1576 CD2 LEU A 238 6570 6438 7103 1701 -1329 -1168 C
ATOM 1577 N MET A 239 3.789 18.711 38.284 1.00 47.90 N
ANISOU 1577 N MET A 239 5241 6515 6443 791 -199 -707 N
ATOM 1578 CA MET A 239 4.187 17.675 39.230 1.00 47.77 C
ANISOU 1578 CA MET A 239 5078 6654 6419 642 0 -673 C
ATOM 1579 C MET A 239 5.652 17.816 39.624 1.00 47.86 C
ANISOU 1579 C MET A 239 5173 6550 6462 520 53 -505 C
ATOM 1580 O MET A 239 6.006 17.594 40.786 1.00 46.91 O
ANISOU 1580 O MET A 239 4977 6506 6342 465 110 -519 O
ATOM 1581 CB MET A 239 3.912 16.290 38.643 1.00 46.55 C
ANISOU 1581 CB MET A 239 4861 6608 6219 541 141 -624 C
ATOM 1582 CG MET A 239 2.437 15.920 38.618 1.00 45.98 C
ANISOU 1582 CG MET A 239 4628 6745 6099 590 129 -824 C
ATOM 1583 SD MET A 239 2.115 14.249 38.023 1.00 46.33 S
ANISOU 1583 SD MET A 239 4645 6892 6067 411 288 -768 S
ATOM 1584 CE MET A 239 2.472 14.417 36.274 1.00 47.44 C
ANISOU 1584 CE MET A 239 4962 6843 6220 474 213 -639 C
ATOM 1585 N VAL A 240 6.519 18.178 38.675 1.00 48.98 N
ANISOU 1585 N VAL A 240 5463 6534 6611 457 34 -357 N
ATOM 1586 CA VAL A 240 7.929 18.378 38.996 1.00 48.52 C
ANISOU 1586 CA VAL A 240 5433 6422 6580 322 85 -233 C
ATOM 1587 C VAL A 240 8.092 19.529 39.979 1.00 49.42 C
ANISOU 1587 C VAL A 240 5600 6460 6718 342 -41 -296 C
ATOM 1588 O VAL A 240 8.837 19.420 40.959 1.00 49.74 O
ANISOU 1588 O VAL A 240 5563 6557 6781 270 1 -279 O
ATOM 1589 CB VAL A 240 8.749 18.602 37.711 1.00 47.97 C
ANISOU 1589 CB VAL A 240 5496 6253 6478 199 113 -95 C
ATOM 1590 CG1 VAL A 240 10.102 19.215 38.041 1.00 44.24 C
ANISOU 1590 CG1 VAL A 240 5043 5746 6020 34 127 -15 C
ATOM 1591 CG2 VAL A 240 8.937 17.288 36.973 1.00 45.11 C
ANISOU 1591 CG2 VAL A 240 5048 5995 6096 169 273 -45 C
ATOM 1592 N LEU A 241 7.389 20.642 39.747 1.00 46.92 N
ANISOU 1592 N LEU A 241 5435 6001 6390 459 -224 -385 N
ATOM 1593 CA LEU A 241 7.462 21.763 40.684 1.00 48.03 C
ANISOU 1593 CA LEU A 241 5662 6040 6548 506 -366 -477 C
ATOM 1594 C LEU A 241 6.966 21.356 42.070 1.00 48.39 C
ANISOU 1594 C LEU A 241 5502 6285 6600 581 -308 -635 C
ATOM 1595 O LEU A 241 7.618 21.636 43.090 1.00 47.37 O
ANISOU 1595 O LEU A 241 5361 6162 6474 506 -306 -639 O
ATOM 1596 CB LEU A 241 6.650 22.945 40.153 1.00 52.44 C
ANISOU 1596 CB LEU A 241 6450 6385 7090 686 -616 -579 C
ATOM 1597 CG LEU A 241 7.170 23.657 38.903 1.00 56.66 C
ANISOU 1597 CG LEU A 241 7309 6653 7567 569 -731 -412 C
ATOM 1598 CD1 LEU A 241 6.196 24.740 38.471 1.00 53.61 C
ANISOU 1598 CD1 LEU A 241 7189 6026 7154 812 -1040 -534 C
ATOM 1599 CD2 LEU A 241 8.550 24.243 39.157 1.00 57.76 C
ANISOU 1599 CD2 LEU A 241 7585 6676 7686 293 -706 -270 C
ATOM 1600 N ALA A 242 5.814 20.680 42.122 1.00 47.72 N
ANISOU 1600 N ALA A 242 5256 6383 6492 692 -254 -772 N
ATOM 1601 CA ALA A 242 5.241 20.291 43.405 1.00 47.40 C
ANISOU 1601 CA ALA A 242 5035 6567 6408 708 -177 -938 C
ATOM 1602 C ALA A 242 6.158 19.335 44.157 1.00 49.53 C
ANISOU 1602 C ALA A 242 5251 6920 6648 512 -25 -794 C
ATOM 1603 O ALA A 242 6.393 19.506 45.359 1.00 50.99 O
ANISOU 1603 O ALA A 242 5411 7168 6793 470 -22 -852 O
ATOM 1604 CB ALA A 242 3.863 19.663 43.194 1.00 43.24 C
ANISOU 1604 CB ALA A 242 4329 6263 5836 792 -124 -1110 C
ATOM 1605 N TYR A 243 6.708 18.335 43.463 1.00 47.22 N
ANISOU 1605 N TYR A 243 4958 6618 6365 412 77 -619 N
ATOM 1606 CA TYR A 243 7.551 17.358 44.140 1.00 46.83 C
ANISOU 1606 CA TYR A 243 4880 6624 6288 285 170 -501 C
ATOM 1607 C TYR A 243 8.916 17.932 44.485 1.00 47.17 C
ANISOU 1607 C TYR A 243 4967 6569 6384 229 109 -403 C
ATOM 1608 O TYR A 243 9.533 17.490 45.454 1.00 50.76 O
ANISOU 1608 O TYR A 243 5397 7080 6811 168 117 -366 O
ATOM 1609 CB TYR A 243 7.692 16.093 43.294 1.00 45.84 C
ANISOU 1609 CB TYR A 243 4752 6507 6159 240 271 -385 C
ATOM 1610 CG TYR A 243 6.497 15.176 43.413 1.00 45.29 C
ANISOU 1610 CG TYR A 243 4637 6574 5995 204 351 -471 C
ATOM 1611 CD1 TYR A 243 6.133 14.639 44.641 1.00 45.87 C
ANISOU 1611 CD1 TYR A 243 4698 6776 5956 99 398 -527 C
ATOM 1612 CD2 TYR A 243 5.730 14.852 42.303 1.00 44.21 C
ANISOU 1612 CD2 TYR A 243 4485 6453 5858 233 379 -500 C
ATOM 1613 CE1 TYR A 243 5.038 13.805 44.761 1.00 44.35 C
ANISOU 1613 CE1 TYR A 243 4471 6736 5643 -11 489 -611 C
ATOM 1614 CE2 TYR A 243 4.634 14.016 42.413 1.00 46.17 C
ANISOU 1614 CE2 TYR A 243 4677 6857 6010 152 455 -593 C
ATOM 1615 CZ TYR A 243 4.292 13.497 43.645 1.00 43.79 C
ANISOU 1615 CZ TYR A 243 4356 6693 5588 11 519 -650 C
ATOM 1616 OH TYR A 243 3.201 12.666 43.761 1.00 43.34 O
ANISOU 1616 OH TYR A 243 4249 6815 5403 -144 612 -747 O
ATOM 1617 N LEU A 244 9.398 18.923 43.732 1.00 46.82 N
ANISOU 1617 N LEU A 244 5006 6385 6399 225 35 -362 N
ATOM 1618 CA LEU A 244 10.615 19.616 44.138 1.00 52.72 C
ANISOU 1618 CA LEU A 244 5782 7070 7179 121 -26 -302 C
ATOM 1619 C LEU A 244 10.398 20.382 45.438 1.00 53.71 C
ANISOU 1619 C LEU A 244 5940 7195 7273 143 -124 -425 C
ATOM 1620 O LEU A 244 11.233 20.323 46.353 1.00 54.58 O
ANISOU 1620 O LEU A 244 6008 7354 7375 61 -144 -398 O
ATOM 1621 CB LEU A 244 11.077 20.554 43.023 1.00 54.69 C
ANISOU 1621 CB LEU A 244 6166 7163 7451 41 -80 -233 C
ATOM 1622 CG LEU A 244 12.425 21.252 43.205 1.00 60.76 C
ANISOU 1622 CG LEU A 244 6956 7895 8236 -150 -118 -164 C
ATOM 1623 CD1 LEU A 244 13.537 20.229 43.370 1.00 64.58 C
ANISOU 1623 CD1 LEU A 244 7224 8561 8751 -217 -10 -97 C
ATOM 1624 CD2 LEU A 244 12.707 22.168 42.027 1.00 65.93 C
ANISOU 1624 CD2 LEU A 244 7806 8387 8859 -292 -161 -91 C
ATOM 1625 N GLN A 245 9.269 21.090 45.546 1.00 51.27 N
ANISOU 1625 N GLN A 245 5694 6844 6941 273 -199 -585 N
ATOM 1626 CA GLN A 245 8.961 21.770 46.802 1.00 52.51 C
ANISOU 1626 CA GLN A 245 5870 7028 7052 319 -277 -750 C
ATOM 1627 C GLN A 245 8.790 20.770 47.942 1.00 52.83 C
ANISOU 1627 C GLN A 245 5783 7287 7003 268 -168 -784 C
ATOM 1628 O GLN A 245 9.249 21.011 49.065 1.00 52.87 O
ANISOU 1628 O GLN A 245 5805 7327 6956 205 -208 -818 O
ATOM 1629 CB GLN A 245 7.710 22.637 46.647 1.00 52.38 C
ANISOU 1629 CB GLN A 245 5911 6959 7030 526 -386 -969 C
ATOM 1630 CG GLN A 245 7.877 23.805 45.683 1.00 53.70 C
ANISOU 1630 CG GLN A 245 6315 6838 7252 580 -566 -936 C
ATOM 1631 CD GLN A 245 6.768 24.834 45.809 1.00 55.85 C
ANISOU 1631 CD GLN A 245 6685 7015 7519 846 -752 -1195 C
ATOM 1632 OE1 GLN A 245 6.186 25.010 46.881 1.00 54.36 O
ANISOU 1632 OE1 GLN A 245 6394 6969 7291 958 -755 -1422 O
ATOM 1633 NE2 GLN A 245 6.469 25.521 44.711 1.00 57.51 N
ANISOU 1633 NE2 GLN A 245 7105 6989 7755 958 -923 -1177 N
ATOM 1634 N ILE A 246 8.138 19.637 47.669 1.00 52.78 N
ANISOU 1634 N ILE A 246 5685 7417 6953 265 -42 -769 N
ATOM 1635 CA ILE A 246 7.947 18.615 48.696 1.00 53.31 C
ANISOU 1635 CA ILE A 246 5706 7659 6891 161 53 -775 C
ATOM 1636 C ILE A 246 9.288 18.035 49.135 1.00 54.90 C
ANISOU 1636 C ILE A 246 5953 7812 7096 60 24 -590 C
ATOM 1637 O ILE A 246 9.516 17.795 50.327 1.00 56.95 O
ANISOU 1637 O ILE A 246 6250 8144 7245 -20 2 -600 O
ATOM 1638 CB ILE A 246 6.990 17.522 48.186 1.00 52.17 C
ANISOU 1638 CB ILE A 246 5499 7637 6687 134 180 -786 C
ATOM 1639 CG1 ILE A 246 5.573 18.082 48.056 1.00 51.64 C
ANISOU 1639 CG1 ILE A 246 5323 7708 6591 239 196 -1037 C
ATOM 1640 CG2 ILE A 246 7.002 16.314 49.110 1.00 50.46 C
ANISOU 1640 CG2 ILE A 246 5327 7534 6311 -39 263 -724 C
ATOM 1641 CD1 ILE A 246 4.600 17.132 47.404 1.00 51.02 C
ANISOU 1641 CD1 ILE A 246 5154 7768 6463 194 308 -1069 C
ATOM 1642 N PHE A 247 10.190 17.794 48.181 1.00 54.89 N
ANISOU 1642 N PHE A 247 5940 7709 7207 69 13 -438 N
ATOM 1643 CA PHE A 247 11.515 17.281 48.510 1.00 57.16 C
ANISOU 1643 CA PHE A 247 6213 7984 7520 23 -39 -308 C
ATOM 1644 C PHE A 247 12.287 18.266 49.374 1.00 59.50 C
ANISOU 1644 C PHE A 247 6515 8267 7823 -28 -158 -344 C
ATOM 1645 O PHE A 247 12.965 17.867 50.328 1.00 57.22 O
ANISOU 1645 O PHE A 247 6232 8028 7480 -65 -231 -307 O
ATOM 1646 CB PHE A 247 12.289 16.975 47.226 1.00 53.63 C
ANISOU 1646 CB PHE A 247 5700 7486 7190 49 -6 -202 C
ATOM 1647 CG PHE A 247 13.690 16.483 47.462 1.00 50.27 C
ANISOU 1647 CG PHE A 247 5193 7098 6811 47 -69 -123 C
ATOM 1648 CD1 PHE A 247 13.940 15.134 47.640 1.00 46.02 C
ANISOU 1648 CD1 PHE A 247 4669 6575 6240 118 -80 -64 C
ATOM 1649 CD2 PHE A 247 14.757 17.367 47.495 1.00 49.34 C
ANISOU 1649 CD2 PHE A 247 4987 6999 6762 -25 -137 -126 C
ATOM 1650 CE1 PHE A 247 15.223 14.675 47.856 1.00 48.46 C
ANISOU 1650 CE1 PHE A 247 4883 6929 6601 181 -179 -30 C
ATOM 1651 CE2 PHE A 247 16.044 16.913 47.712 1.00 46.13 C
ANISOU 1651 CE2 PHE A 247 4441 6685 6403 -10 -205 -97 C
ATOM 1652 CZ PHE A 247 16.277 15.566 47.891 1.00 45.80 C
ANISOU 1652 CZ PHE A 247 4389 6669 6346 125 -237 -60 C
ATOM 1653 N ARG A 248 12.211 19.558 49.048 1.00 64.52 N
ANISOU 1653 N ARG A 248 7185 8815 8514 -33 -205 -414 N
ATOM 1654 CA ARG A 248 12.853 20.553 49.901 1.00 65.97 C
ANISOU 1654 CA ARG A 248 7412 8966 8689 -107 -328 -466 C
ATOM 1655 C ARG A 248 12.238 20.556 51.295 1.00 66.68 C
ANISOU 1655 C ARG A 248 7553 9142 8641 -98 -352 -590 C
ATOM 1656 O ARG A 248 12.953 20.659 52.298 1.00 68.72 O
ANISOU 1656 O ARG A 248 7827 9439 8846 -172 -442 -587 O
ATOM 1657 CB ARG A 248 12.755 21.943 49.273 1.00 66.34 C
ANISOU 1657 CB ARG A 248 7569 8844 8793 -123 -398 -522 C
ATOM 1658 CG ARG A 248 13.542 22.114 47.988 1.00 67.52 C
ANISOU 1658 CG ARG A 248 7707 8918 9029 -221 -377 -394 C
ATOM 1659 CD ARG A 248 13.825 23.584 47.735 1.00 75.69 C
ANISOU 1659 CD ARG A 248 8928 9759 10073 -336 -500 -422 C
ATOM 1660 NE ARG A 248 14.192 23.848 46.350 1.00 76.68 N
ANISOU 1660 NE ARG A 248 9118 9791 10227 -452 -465 -313 N
ATOM 1661 CZ ARG A 248 13.334 24.224 45.412 1.00 77.91 C
ANISOU 1661 CZ ARG A 248 9443 9786 10372 -366 -488 -318 C
ATOM 1662 NH1 ARG A 248 12.047 24.384 45.678 1.00 72.65 N
ANISOU 1662 NH1 ARG A 248 8852 9060 9692 -134 -548 -453 N
ATOM 1663 NH2 ARG A 248 13.777 24.448 44.178 1.00 86.21 N
ANISOU 1663 NH2 ARG A 248 10584 10759 11411 -521 -455 -201 N
ATOM 1664 N LYS A 249 10.911 20.435 51.377 1.00 62.34 N
ANISOU 1664 N LYS A 249 7015 8656 8015 -22 -269 -719 N
ATOM 1665 CA LYS A 249 10.239 20.500 52.670 1.00 62.91 C
ANISOU 1665 CA LYS A 249 7118 8862 7922 -44 -255 -878 C
ATOM 1666 C LYS A 249 10.537 19.279 53.534 1.00 63.84 C
ANISOU 1666 C LYS A 249 7264 9097 7895 -164 -223 -772 C
ATOM 1667 O LYS A 249 10.588 19.392 54.763 1.00 71.84 O
ANISOU 1667 O LYS A 249 8348 10192 8756 -245 -263 -840 O
ATOM 1668 CB LYS A 249 8.731 20.650 52.466 1.00 59.88 C
ANISOU 1668 CB LYS A 249 6679 8583 7489 58 -159 -1084 C
ATOM 1669 CG LYS A 249 7.972 21.125 53.696 1.00 65.81 C
ANISOU 1669 CG LYS A 249 7428 9499 8076 58 -140 -1337 C
ATOM 1670 CD LYS A 249 8.367 22.544 54.073 1.00 74.84 C
ANISOU 1670 CD LYS A 249 8668 10495 9271 140 -301 -1464 C
ATOM 1671 CE LYS A 249 7.423 23.128 55.114 1.00 77.16 C
ANISOU 1671 CE LYS A 249 8938 10962 9415 207 -276 -1789 C
ATOM 1672 NZ LYS A 249 7.405 22.331 56.371 1.00 86.19 N
ANISOU 1672 NZ LYS A 249 10082 12342 10325 6 -167 -1794 N
ATOM 1673 N LEU A 250 10.737 18.114 52.920 1.00 62.57 N
ANISOU 1673 N LEU A 250 7090 8923 7759 -175 -173 -609 N
ATOM 1674 CA LEU A 250 10.914 16.871 53.662 1.00 56.04 C
ANISOU 1674 CA LEU A 250 6369 8148 6774 -274 -179 -500 C
ATOM 1675 C LEU A 250 12.369 16.482 53.874 1.00 56.44 C
ANISOU 1675 C LEU A 250 6444 8117 6883 -250 -342 -343 C
ATOM 1676 O LEU A 250 12.691 15.884 54.906 1.00 59.88 O
ANISOU 1676 O LEU A 250 7018 8574 7162 -319 -438 -287 O
ATOM 1677 CB LEU A 250 10.196 15.718 52.950 1.00 56.54 C
ANISOU 1677 CB LEU A 250 6455 8224 6804 -296 -56 -437 C
ATOM 1678 CG LEU A 250 8.668 15.692 53.031 1.00 55.60 C
ANISOU 1678 CG LEU A 250 6305 8270 6552 -378 108 -604 C
ATOM 1679 CD1 LEU A 250 8.104 14.547 52.203 1.00 53.83 C
ANISOU 1679 CD1 LEU A 250 6104 8040 6309 -427 209 -526 C
ATOM 1680 CD2 LEU A 250 8.215 15.583 54.476 1.00 54.31 C
ANISOU 1680 CD2 LEU A 250 6245 8268 6122 -561 139 -698 C
ATOM 1681 N TRP A 251 13.257 16.793 52.931 1.00 53.44 N
ANISOU 1681 N TRP A 251 5933 7666 6707 -162 -385 -285 N
ATOM 1682 CA TRP A 251 14.645 16.365 53.022 1.00 54.06 C
ANISOU 1682 CA TRP A 251 5954 7730 6856 -113 -533 -183 C
ATOM 1683 C TRP A 251 15.638 17.510 53.161 1.00 57.86 C
ANISOU 1683 C TRP A 251 6313 8233 7439 -152 -637 -229 C
ATOM 1684 O TRP A 251 16.830 17.249 53.353 1.00 57.68 O
ANISOU 1684 O TRP A 251 6190 8258 7470 -121 -775 -186 O
ATOM 1685 CB TRP A 251 15.020 15.519 51.796 1.00 52.06 C
ANISOU 1685 CB TRP A 251 5612 7438 6732 -2 -485 -98 C
ATOM 1686 CG TRP A 251 14.517 14.104 51.856 1.00 50.82 C
ANISOU 1686 CG TRP A 251 5619 7227 6464 35 -471 -21 C
ATOM 1687 CD1 TRP A 251 15.087 13.060 52.526 1.00 48.45 C
ANISOU 1687 CD1 TRP A 251 5458 6875 6075 95 -636 61 C
ATOM 1688 CD2 TRP A 251 13.348 13.577 51.214 1.00 48.48 C
ANISOU 1688 CD2 TRP A 251 5400 6901 6119 2 -311 -21 C
ATOM 1689 NE1 TRP A 251 14.345 11.918 52.344 1.00 47.13 N
ANISOU 1689 NE1 TRP A 251 5495 6617 5796 77 -584 125 N
ATOM 1690 CE2 TRP A 251 13.273 12.209 51.542 1.00 46.54 C
ANISOU 1690 CE2 TRP A 251 5363 6575 5745 3 -372 72 C
ATOM 1691 CE3 TRP A 251 12.357 14.130 50.397 1.00 48.89 C
ANISOU 1691 CE3 TRP A 251 5382 6980 6215 -28 -148 -96 C
ATOM 1692 CZ2 TRP A 251 12.249 11.385 51.080 1.00 46.08 C
ANISOU 1692 CZ2 TRP A 251 5435 6476 5597 -71 -250 92 C
ATOM 1693 CZ3 TRP A 251 11.341 13.309 49.938 1.00 48.51 C
ANISOU 1693 CZ3 TRP A 251 5416 6926 6091 -69 -33 -90 C
ATOM 1694 CH2 TRP A 251 11.295 11.953 50.282 1.00 48.25 C
ANISOU 1694 CH2 TRP A 251 5581 6826 5927 -113 -71 3 C
ATOM 1695 N CYS A 252 15.191 18.762 53.068 1.00 63.17 N
ANISOU 1695 N CYS A 252 6996 8871 8133 -218 -595 -331 N
ATOM 1696 CA CYS A 252 16.066 19.919 53.214 1.00 66.56 C
ANISOU 1696 CA CYS A 252 7370 9288 8632 -312 -699 -376 C
ATOM 1697 C CYS A 252 15.612 20.822 54.358 1.00 74.05 C
ANISOU 1697 C CYS A 252 8459 10219 9458 -375 -767 -506 C
ATOM 1698 O CYS A 252 15.889 22.022 54.358 1.00 77.08 O
ANISOU 1698 O CYS A 252 8876 10527 9884 -457 -832 -580 O
ATOM 1699 CB CYS A 252 16.143 20.708 51.907 1.00 63.52 C
ANISOU 1699 CB CYS A 252 6937 8817 8380 -355 -627 -372 C
ATOM 1700 SG CYS A 252 16.988 19.848 50.562 1.00 61.96 S
ANISOU 1700 SG CYS A 252 6538 8691 8313 -325 -544 -257 S
ATOM 1701 N ARG A 253 14.917 20.255 55.341 1.00 87.43 N
ANISOU 1701 N ARG A 253 10260 11979 10978 -360 -753 -544 N
ATOM 1702 CA ARG A 253 14.391 21.014 56.465 1.00 89.06 C
ANISOU 1702 CA ARG A 253 10591 12213 11036 -414 -788 -703 C
ATOM 1703 C ARG A 253 14.703 20.285 57.765 1.00 92.26 C
ANISOU 1703 C ARG A 253 11092 12719 11243 -483 -882 -663 C
ATOM 1704 O ARG A 253 14.868 19.064 57.786 1.00 92.97 O
ANISOU 1704 O ARG A 253 11208 12836 11280 -465 -893 -526 O
ATOM 1705 CB ARG A 253 12.875 21.233 56.325 1.00 95.72 C
ANISOU 1705 CB ARG A 253 11478 13082 11811 -349 -631 -860 C
ATOM 1706 CG ARG A 253 12.291 22.248 57.295 1.00105.09 C
ANISOU 1706 CG ARG A 253 12757 14302 12872 -358 -658 -1095 C
ATOM 1707 CD ARG A 253 10.797 22.423 57.083 1.00110.64 C
ANISOU 1707 CD ARG A 253 13428 15087 13523 -250 -509 -1299 C
ATOM 1708 NE ARG A 253 10.078 21.157 57.164 1.00110.19 N
ANISOU 1708 NE ARG A 253 13330 15206 13333 -310 -349 -1253 N
ATOM 1709 CZ ARG A 253 9.631 20.621 58.291 1.00109.80 C
ANISOU 1709 CZ ARG A 253 13346 15348 13026 -448 -277 -1322 C
ATOM 1710 NH1 ARG A 253 9.832 21.204 59.462 1.00112.00 N
ANISOU 1710 NH1 ARG A 253 13718 15685 13153 -516 -348 -1447 N
ATOM 1711 NH2 ARG A 253 8.964 19.472 58.243 1.00103.28 N
ANISOU 1711 NH2 ARG A 253 12518 14657 12068 -554 -132 -1264 N
ATOM 1712 N GLN A 254 14.777 21.052 58.851 1.00 80.91 N
ANISOU 1712 N GLN A 254 9750 11313 9680 -562 -972 -787 N
ATOM 1713 CA GLN A 254 15.133 20.505 60.153 1.00 72.18 C
ANISOU 1713 CA GLN A 254 8777 10295 8354 -651 -1095 -753 C
ATOM 1714 C GLN A 254 14.079 19.529 60.663 1.00 68.74 C
ANISOU 1714 C GLN A 254 8488 9955 7675 -710 -961 -748 C
ATOM 1715 O GLN A 254 12.895 19.618 60.325 1.00 71.81 O
ANISOU 1715 O GLN A 254 8851 10401 8031 -702 -759 -866 O
ATOM 1716 CB GLN A 254 15.314 21.629 61.170 1.00 71.43 C
ANISOU 1716 CB GLN A 254 8768 10218 8155 -738 -1200 -919 C
ATOM 1717 CG GLN A 254 16.602 22.401 61.014 1.00 70.97 C
ANISOU 1717 CG GLN A 254 8613 10091 8262 -774 -1388 -895 C
ATOM 1718 CD GLN A 254 16.638 23.645 61.870 1.00 77.11 C
ANISOU 1718 CD GLN A 254 9506 10843 8948 -867 -1481 -1084 C
ATOM 1719 OE1 GLN A 254 15.597 24.191 62.229 1.00 85.22 O
ANISOU 1719 OE1 GLN A 254 10646 11871 9863 -843 -1374 -1273 O
ATOM 1720 NE2 GLN A 254 17.840 24.101 62.204 1.00 73.09 N
ANISOU 1720 NE2 GLN A 254 8956 10329 8484 -969 -1686 -1061 N
ATOM 1721 N ILE A 255 14.526 18.594 61.490 1.00 70.52 N
ANISOU 1721 N ILE A 255 8878 10203 7713 -784 -1092 -618 N
ATOM 1722 CA ILE A 255 13.625 17.622 62.112 1.00 69.03 C
ANISOU 1722 CA ILE A 255 8907 10095 7226 -926 -987 -587 C
ATOM 1723 C ILE A 255 12.894 18.301 63.268 1.00 70.77 C
ANISOU 1723 C ILE A 255 9236 10478 7175 -1089 -902 -798 C
ATOM 1724 O ILE A 255 13.543 18.947 64.105 1.00 72.86 O
ANISOU 1724 O ILE A 255 9560 10750 7372 -1120 -1064 -854 O
ATOM 1725 CB ILE A 255 14.403 16.402 62.594 1.00 65.34 C
ANISOU 1725 CB ILE A 255 8658 9540 6627 -947 -1208 -362 C
ATOM 1726 CG1 ILE A 255 15.156 15.758 61.428 1.00 66.63 C
ANISOU 1726 CG1 ILE A 255 8679 9566 7071 -738 -1293 -209 C
ATOM 1727 CG2 ILE A 255 13.472 15.391 63.244 1.00 66.27 C
ANISOU 1727 CG2 ILE A 255 9082 9707 6390 -1167 -1107 -306 C
ATOM 1728 CD1 ILE A 255 14.261 15.335 60.285 1.00 64.12 C
ANISOU 1728 CD1 ILE A 255 8278 9225 6858 -708 -1055 -201 C
ATOM 1729 N PRO A 256 11.571 18.186 63.348 1.00 67.69 N
ANISOU 1729 N PRO A 256 8852 10249 6617 -1198 -651 -946 N
ATOM 1730 CA PRO A 256 10.832 18.837 64.435 1.00 69.15 C
ANISOU 1730 CA PRO A 256 9099 10647 6530 -1342 -541 -1203 C
ATOM 1731 C PRO A 256 11.081 18.151 65.770 1.00 70.49 C
ANISOU 1731 C PRO A 256 9588 10884 6310 -1596 -637 -1106 C
ATOM 1732 O PRO A 256 11.717 17.100 65.862 1.00 72.11 O
ANISOU 1732 O PRO A 256 10000 10953 6444 -1651 -802 -835 O
ATOM 1733 CB PRO A 256 9.371 18.698 64.000 1.00 73.55 C
ANISOU 1733 CB PRO A 256 9516 11405 7026 -1388 -240 -1390 C
ATOM 1734 CG PRO A 256 9.361 17.475 63.144 1.00 70.61 C
ANISOU 1734 CG PRO A 256 9175 10928 6725 -1412 -213 -1140 C
ATOM 1735 CD PRO A 256 10.679 17.465 62.425 1.00 67.68 C
ANISOU 1735 CD PRO A 256 8772 10280 6665 -1200 -450 -916 C
ATOM 1736 N GLY A 257 10.563 18.777 66.823 1.00 74.26 N
ANISOU 1736 N GLY A 257 10131 11567 6517 -1740 -549 -1346 N
ATOM 1737 CA GLY A 257 10.722 18.254 68.165 1.00 82.91 C
ANISOU 1737 CA GLY A 257 11564 12751 7188 -2020 -628 -1281 C
ATOM 1738 C GLY A 257 9.620 17.307 68.597 1.00 84.50 C
ANISOU 1738 C GLY A 257 11938 13171 6996 -2355 -384 -1294 C
ATOM 1739 O GLY A 257 9.851 16.415 69.419 1.00 86.69 O
ANISOU 1739 O GLY A 257 12592 13423 6923 -2620 -489 -1102 O
ATOM 1740 N VAL A 289 8.418 17.486 68.049 1.00 91.94 N
ANISOU 1740 N VAL A 289 12623 14332 7976 -2366 -73 -1525 N
ATOM 1741 CA VAL A 289 7.294 16.634 68.419 1.00 93.09 C
ANISOU 1741 CA VAL A 289 12879 14754 7739 -2741 199 -1580 C
ATOM 1742 C VAL A 289 7.464 15.266 67.774 1.00 94.54 C
ANISOU 1742 C VAL A 289 13263 14721 7939 -2841 134 -1229 C
ATOM 1743 O VAL A 289 7.732 15.157 66.570 1.00 92.78 O
ANISOU 1743 O VAL A 289 12855 14293 8104 -2567 75 -1116 O
ATOM 1744 CB VAL A 289 5.965 17.288 68.011 1.00 90.57 C
ANISOU 1744 CB VAL A 289 12157 14781 7473 -2690 531 -1984 C
ATOM 1745 CG1 VAL A 289 4.790 16.451 68.497 1.00 91.71 C
ANISOU 1745 CG1 VAL A 289 12322 15182 7341 -3071 820 -2018 C
ATOM 1746 CG2 VAL A 289 5.880 18.704 68.561 1.00 91.44 C
ANISOU 1746 CG2 VAL A 289 12091 15037 7616 -2500 541 -2352 C
ATOM 1747 N ALA A 290 7.309 14.211 68.579 1.00 86.19 N
ANISOU 1747 N ALA A 290 12625 13691 6434 -3249 134 -1058 N
ATOM 1748 CA ALA A 290 7.506 12.853 68.079 1.00 85.99 C
ANISOU 1748 CA ALA A 290 12893 13402 6377 -3357 23 -718 C
ATOM 1749 C ALA A 290 6.495 12.505 66.993 1.00 85.42 C
ANISOU 1749 C ALA A 290 12556 13450 6449 -3390 297 -805 C
ATOM 1750 O ALA A 290 6.832 11.824 66.015 1.00 84.66 O
ANISOU 1750 O ALA A 290 12490 13078 6599 -3229 184 -587 O
ATOM 1751 CB ALA A 290 7.419 11.855 69.234 1.00 87.29 C
ANISOU 1751 CB ALA A 290 13544 13474 6148 -3752 -29 -514 C
ATOM 1752 N ALA A 291 5.247 12.951 67.154 1.00 81.27 N
ANISOU 1752 N ALA A 291 11718 13302 5860 -3542 642 -1125 N
ATOM 1753 CA ALA A 291 4.230 12.683 66.143 1.00 76.80 C
ANISOU 1753 CA ALA A 291 10842 12879 5457 -3557 881 -1240 C
ATOM 1754 C ALA A 291 4.619 13.288 64.802 1.00 76.32 C
ANISOU 1754 C ALA A 291 10468 12690 5842 -3090 799 -1277 C
ATOM 1755 O ALA A 291 4.457 12.652 63.754 1.00 77.61 O
ANISOU 1755 O ALA A 291 10580 12719 6191 -3032 813 -1148 O
ATOM 1756 CB ALA A 291 2.875 13.221 66.602 1.00 80.43 C
ANISOU 1756 CB ALA A 291 10914 13737 5906 -3688 1189 -1603 C
ATOM 1757 N GLU A 292 5.144 14.516 64.817 1.00 78.96 N
ANISOU 1757 N GLU A 292 10584 12981 6437 -2730 688 -1422 N
ATOM 1758 CA GLU A 292 5.613 15.130 63.581 1.00 78.33 C
ANISOU 1758 CA GLU A 292 10230 12675 6858 -2279 569 -1400 C
ATOM 1759 C GLU A 292 6.796 14.371 62.996 1.00 75.02 C
ANISOU 1759 C GLU A 292 10025 11845 6635 -2145 306 -1015 C
ATOM 1760 O GLU A 292 6.938 14.299 61.772 1.00 71.98 O
ANISOU 1760 O GLU A 292 9472 11303 6576 -1912 282 -939 O
ATOM 1761 CB GLU A 292 5.984 16.592 63.827 1.00 78.73 C
ANISOU 1761 CB GLU A 292 10093 12730 7091 -1990 481 -1620 C
ATOM 1762 CG GLU A 292 4.844 17.436 64.366 1.00 78.22 C
ANISOU 1762 CG GLU A 292 9791 13062 6866 -2030 711 -2060 C
ATOM 1763 CD GLU A 292 5.212 18.900 64.487 1.00 77.29 C
ANISOU 1763 CD GLU A 292 9536 12874 6956 -1703 585 -2281 C
ATOM 1764 OE1 GLU A 292 6.159 19.336 63.799 1.00 75.46 O
ANISOU 1764 OE1 GLU A 292 9307 12306 7059 -1437 364 -2110 O
ATOM 1765 OE2 GLU A 292 4.556 19.614 65.273 1.00 78.65 O
ANISOU 1765 OE2 GLU A 292 9608 13333 6940 -1730 708 -2639 O
ATOM 1766 N ILE A 293 7.644 13.789 63.846 1.00 78.21 N
ANISOU 1766 N ILE A 293 10799 12084 6832 -2274 96 -788 N
ATOM 1767 CA ILE A 293 8.767 12.994 63.357 1.00 77.50 C
ANISOU 1767 CA ILE A 293 10903 11632 6911 -2111 -181 -465 C
ATOM 1768 C ILE A 293 8.268 11.750 62.626 1.00 77.70 C
ANISOU 1768 C ILE A 293 11069 11560 6894 -2241 -103 -310 C
ATOM 1769 O ILE A 293 8.735 11.424 61.525 1.00 75.05 O
ANISOU 1769 O ILE A 293 10641 11011 6865 -1989 -192 -186 O
ATOM 1770 CB ILE A 293 9.705 12.628 64.521 1.00 79.40 C
ANISOU 1770 CB ILE A 293 11530 11733 6906 -2205 -463 -287 C
ATOM 1771 CG1 ILE A 293 10.369 13.886 65.085 1.00 79.44 C
ANISOU 1771 CG1 ILE A 293 11372 11796 7014 -2038 -579 -430 C
ATOM 1772 CG2 ILE A 293 10.747 11.617 64.074 1.00 79.65 C
ANISOU 1772 CG2 ILE A 293 11784 11413 7065 -2027 -767 14 C
ATOM 1773 CD1 ILE A 293 11.272 13.622 66.267 1.00 83.96 C
ANISOU 1773 CD1 ILE A 293 12298 12265 7337 -2125 -874 -285 C
ATOM 1774 N LYS A 294 7.312 11.036 63.227 1.00 71.99 N
ANISOU 1774 N LYS A 294 10583 11003 5768 -2667 70 -327 N
ATOM 1775 CA LYS A 294 6.748 9.861 62.566 1.00 71.00 C
ANISOU 1775 CA LYS A 294 10620 10789 5566 -2855 153 -196 C
ATOM 1776 C LYS A 294 6.050 10.249 61.270 1.00 68.52 C
ANISOU 1776 C LYS A 294 9859 10603 5575 -2674 361 -366 C
ATOM 1777 O LYS A 294 6.163 9.547 60.253 1.00 67.58 O
ANISOU 1777 O LYS A 294 9770 10275 5634 -2567 315 -224 O
ATOM 1778 CB LYS A 294 5.772 9.141 63.497 1.00 75.21 C
ANISOU 1778 CB LYS A 294 11476 11534 5566 -3433 337 -215 C
ATOM 1779 CG LYS A 294 6.341 8.766 64.854 1.00 82.93 C
ANISOU 1779 CG LYS A 294 12960 12401 6149 -3673 134 -48 C
ATOM 1780 CD LYS A 294 5.354 7.914 65.641 1.00 85.83 C
ANISOU 1780 CD LYS A 294 13570 12835 6206 -4192 309 -37 C
ATOM 1781 CE LYS A 294 5.799 7.733 67.085 1.00 87.52 C
ANISOU 1781 CE LYS A 294 14175 12931 6148 -4384 139 78 C
ATOM 1782 NZ LYS A 294 5.771 9.016 67.842 1.00 84.02 N
ANISOU 1782 NZ LYS A 294 13436 12810 5677 -4310 248 -179 N
ATOM 1783 N GLN A 295 5.320 11.367 61.291 1.00 65.22 N
ANISOU 1783 N GLN A 295 9040 10517 5223 -2618 570 -686 N
ATOM 1784 CA GLN A 295 4.660 11.850 60.086 1.00 64.91 C
ANISOU 1784 CA GLN A 295 8585 10590 5486 -2403 718 -864 C
ATOM 1785 C GLN A 295 5.675 12.160 58.996 1.00 62.67 C
ANISOU 1785 C GLN A 295 8190 9982 5639 -1968 517 -718 C
ATOM 1786 O GLN A 295 5.452 11.844 57.823 1.00 61.53 O
ANISOU 1786 O GLN A 295 7922 9758 5697 -1851 556 -680 O
ATOM 1787 CB GLN A 295 3.825 13.087 60.415 1.00 64.52 C
ANISOU 1787 CB GLN A 295 8166 10915 5434 -2344 900 -1254 C
ATOM 1788 CG GLN A 295 2.985 13.603 59.263 1.00 65.63 C
ANISOU 1788 CG GLN A 295 7896 11202 5838 -2123 1028 -1478 C
ATOM 1789 CD GLN A 295 2.320 14.925 59.587 1.00 68.03 C
ANISOU 1789 CD GLN A 295 7860 11808 6178 -1951 1124 -1881 C
ATOM 1790 OE1 GLN A 295 2.980 15.881 59.996 1.00 70.11 O
ANISOU 1790 OE1 GLN A 295 8131 11961 6548 -1730 985 -1929 O
ATOM 1791 NE2 GLN A 295 1.005 14.984 59.415 1.00 67.86 N
ANISOU 1791 NE2 GLN A 295 7539 12180 6066 -2045 1348 -2196 N
ATOM 1792 N ILE A 296 6.803 12.770 59.367 1.00 64.94 N
ANISOU 1792 N ILE A 296 8516 10104 6053 -1755 307 -645 N
ATOM 1793 CA ILE A 296 7.836 13.093 58.390 1.00 64.51 C
ANISOU 1793 CA ILE A 296 8339 9794 6378 -1399 135 -524 C
ATOM 1794 C ILE A 296 8.437 11.825 57.801 1.00 58.91 C
ANISOU 1794 C ILE A 296 7846 8822 5714 -1371 7 -258 C
ATOM 1795 O ILE A 296 8.681 11.749 56.595 1.00 55.96 O
ANISOU 1795 O ILE A 296 7323 8328 5610 -1162 0 -210 O
ATOM 1796 CB ILE A 296 8.910 13.997 59.023 1.00 65.02 C
ANISOU 1796 CB ILE A 296 8392 9786 6528 -1245 -57 -526 C
ATOM 1797 CG1 ILE A 296 8.409 15.439 59.083 1.00 70.17 C
ANISOU 1797 CG1 ILE A 296 8782 10607 7273 -1143 41 -807 C
ATOM 1798 CG2 ILE A 296 10.220 13.914 58.247 1.00 59.59 C
ANISOU 1798 CG2 ILE A 296 7660 8845 6136 -983 -265 -345 C
ATOM 1799 CD1 ILE A 296 9.503 16.451 59.294 1.00 79.36 C
ANISOU 1799 CD1 ILE A 296 9898 11648 8608 -966 -152 -808 C
ATOM 1800 N ARG A 297 8.689 10.812 58.633 1.00 58.50 N
ANISOU 1800 N ARG A 297 8179 8664 5385 -1573 -111 -90 N
ATOM 1801 CA ARG A 297 9.248 9.564 58.112 1.00 57.50 C
ANISOU 1801 CA ARG A 297 8312 8248 5289 -1509 -275 142 C
ATOM 1802 C ARG A 297 8.287 8.893 57.131 1.00 53.86 C
ANISOU 1802 C ARG A 297 7823 7803 4839 -1622 -84 128 C
ATOM 1803 O ARG A 297 8.686 8.464 56.034 1.00 52.24 O
ANISOU 1803 O ARG A 297 7568 7415 4867 -1403 -143 209 O
ATOM 1804 CB ARG A 297 9.589 8.625 59.270 1.00 59.20 C
ANISOU 1804 CB ARG A 297 9027 8313 5156 -1721 -476 320 C
ATOM 1805 CG ARG A 297 10.637 9.186 60.218 1.00 65.13 C
ANISOU 1805 CG ARG A 297 9823 9030 5892 -1589 -716 346 C
ATOM 1806 CD ARG A 297 10.816 8.310 61.445 1.00 73.87 C
ANISOU 1806 CD ARG A 297 11471 10002 6593 -1836 -921 514 C
ATOM 1807 NE ARG A 297 11.393 7.011 61.119 1.00 82.15 N
ANISOU 1807 NE ARG A 297 12888 10695 7631 -1722 -1187 737 N
ATOM 1808 CZ ARG A 297 11.673 6.074 62.014 1.00 89.39 C
ANISOU 1808 CZ ARG A 297 14367 11384 8212 -1876 -1452 925 C
ATOM 1809 NH1 ARG A 297 11.440 6.258 63.303 1.00 88.76 N
ANISOU 1809 NH1 ARG A 297 14552 11415 7757 -2190 -1469 934 N
ATOM 1810 NH2 ARG A 297 12.201 4.924 61.606 1.00 92.76 N
ANISOU 1810 NH2 ARG A 297 15131 11449 8665 -1703 -1724 1101 N
ATOM 1811 N ALA A 298 7.007 8.810 57.506 1.00 56.91 N
ANISOU 1811 N ALA A 298 8219 8440 4964 -1976 154 -1 N
ATOM 1812 CA ALA A 298 6.018 8.200 56.622 1.00 57.09 C
ANISOU 1812 CA ALA A 298 8188 8526 4977 -2126 338 -41 C
ATOM 1813 C ALA A 298 5.877 8.988 55.324 1.00 58.81 C
ANISOU 1813 C ALA A 298 7968 8806 5569 -1808 423 -175 C
ATOM 1814 O ALA A 298 5.806 8.403 54.233 1.00 55.56 O
ANISOU 1814 O ALA A 298 7549 8262 5297 -1726 429 -109 O
ATOM 1815 CB ALA A 298 4.672 8.095 57.337 1.00 57.64 C
ANISOU 1815 CB ALA A 298 8268 8946 4687 -2589 594 -209 C
ATOM 1816 N ARG A 299 5.842 10.320 55.422 1.00 55.00 N
ANISOU 1816 N ARG A 299 7160 8502 5236 -1629 471 -364 N
ATOM 1817 CA ARG A 299 5.730 11.155 54.235 1.00 54.49 C
ANISOU 1817 CA ARG A 299 6749 8459 5495 -1336 512 -478 C
ATOM 1818 C ARG A 299 6.974 11.068 53.367 1.00 50.23 C
ANISOU 1818 C ARG A 299 6227 7624 5234 -1041 337 -296 C
ATOM 1819 O ARG A 299 6.873 11.167 52.145 1.00 48.74 O
ANISOU 1819 O ARG A 299 5880 7387 5251 -883 374 -308 O
ATOM 1820 CB ARG A 299 5.458 12.604 54.636 1.00 56.99 C
ANISOU 1820 CB ARG A 299 6802 8975 5878 -1213 554 -719 C
ATOM 1821 CG ARG A 299 4.045 12.846 55.138 1.00 57.18 C
ANISOU 1821 CG ARG A 299 6664 9371 5691 -1421 765 -1000 C
ATOM 1822 CD ARG A 299 3.842 14.295 55.540 1.00 59.34 C
ANISOU 1822 CD ARG A 299 6703 9802 6040 -1231 766 -1267 C
ATOM 1823 NE ARG A 299 2.450 14.579 55.866 1.00 59.40 N
ANISOU 1823 NE ARG A 299 6473 10212 5884 -1353 966 -1605 N
ATOM 1824 CZ ARG A 299 2.001 15.765 56.253 1.00 60.05 C
ANISOU 1824 CZ ARG A 299 6336 10487 5993 -1182 984 -1917 C
ATOM 1825 NH1 ARG A 299 2.813 16.801 56.385 1.00 63.52 N
ANISOU 1825 NH1 ARG A 299 6808 10722 6604 -919 812 -1913 N
ATOM 1826 NH2 ARG A 299 0.706 15.915 56.516 1.00 61.20 N
ANISOU 1826 NH2 ARG A 299 6219 11049 5984 -1279 1171 -2264 N
ATOM 1827 N ARG A 300 8.149 10.881 53.970 1.00 52.62 N
ANISOU 1827 N ARG A 300 6705 7756 5533 -967 143 -147 N
ATOM 1828 CA ARG A 300 9.363 10.694 53.186 1.00 52.17 C
ANISOU 1828 CA ARG A 300 6624 7479 5719 -699 -14 -12 C
ATOM 1829 C ARG A 300 9.291 9.410 52.373 1.00 52.27 C
ANISOU 1829 C ARG A 300 6803 7326 5730 -698 -20 106 C
ATOM 1830 O ARG A 300 9.612 9.398 51.178 1.00 50.31 O
ANISOU 1830 O ARG A 300 6410 7004 5701 -506 -7 117 O
ATOM 1831 CB ARG A 300 10.585 10.681 54.104 1.00 51.49 C
ANISOU 1831 CB ARG A 300 6669 7291 5606 -620 -244 86 C
ATOM 1832 CG ARG A 300 11.057 12.056 54.534 1.00 51.91 C
ANISOU 1832 CG ARG A 300 6511 7449 5762 -538 -280 -20 C
ATOM 1833 CD ARG A 300 12.186 11.951 55.542 1.00 50.87 C
ANISOU 1833 CD ARG A 300 6517 7247 5565 -497 -521 67 C
ATOM 1834 NE ARG A 300 12.740 13.257 55.876 1.00 53.81 N
ANISOU 1834 NE ARG A 300 6692 7705 6049 -435 -570 -34 N
ATOM 1835 CZ ARG A 300 13.730 13.452 56.735 1.00 55.04 C
ANISOU 1835 CZ ARG A 300 6896 7845 6172 -402 -780 -1 C
ATOM 1836 NH1 ARG A 300 14.296 12.444 57.378 1.00 55.88 N
ANISOU 1836 NH1 ARG A 300 7245 7848 6139 -389 -987 131 N
ATOM 1837 NH2 ARG A 300 14.164 14.690 56.954 1.00 59.66 N
ANISOU 1837 NH2 ARG A 300 7307 8504 6858 -381 -811 -105 N
ATOM 1838 N LYS A 301 8.858 8.315 53.004 1.00 50.74 N
ANISOU 1838 N LYS A 301 6949 7064 5266 -936 -43 194 N
ATOM 1839 CA LYS A 301 8.717 7.064 52.262 1.00 43.89 C
ANISOU 1839 CA LYS A 301 6301 6003 4372 -960 -64 297 C
ATOM 1840 C LYS A 301 7.703 7.209 51.129 1.00 45.89 C
ANISOU 1840 C LYS A 301 6330 6388 4717 -1009 154 183 C
ATOM 1841 O LYS A 301 7.971 6.825 49.978 1.00 48.76 O
ANISOU 1841 O LYS A 301 6651 6622 5252 -834 141 215 O
ATOM 1842 CB LYS A 301 8.314 5.932 53.207 1.00 43.06 C
ANISOU 1842 CB LYS A 301 6667 5785 3909 -1286 -130 414 C
ATOM 1843 CG LYS A 301 9.395 5.536 54.196 1.00 44.87 C
ANISOU 1843 CG LYS A 301 7213 5802 4035 -1195 -422 559 C
ATOM 1844 CD LYS A 301 8.949 4.366 55.058 1.00 48.81 C
ANISOU 1844 CD LYS A 301 8273 6136 4138 -1554 -510 701 C
ATOM 1845 CE LYS A 301 10.023 3.980 56.062 1.00 54.83 C
ANISOU 1845 CE LYS A 301 9392 6661 4778 -1436 -856 850 C
ATOM 1846 NZ LYS A 301 9.603 2.836 56.919 1.00 66.72 N
ANISOU 1846 NZ LYS A 301 11541 7956 5854 -1816 -977 1015 N
ATOM 1847 N THR A 302 6.536 7.785 51.434 1.00 46.38 N
ANISOU 1847 N THR A 302 6228 6731 4663 -1229 346 24 N
ATOM 1848 CA THR A 302 5.497 7.938 50.419 1.00 47.28 C
ANISOU 1848 CA THR A 302 6112 7003 4851 -1266 521 -111 C
ATOM 1849 C THR A 302 5.952 8.856 49.290 1.00 44.84 C
ANISOU 1849 C THR A 302 5507 6667 4863 -922 503 -160 C
ATOM 1850 O THR A 302 5.688 8.582 48.114 1.00 43.54 O
ANISOU 1850 O THR A 302 5277 6459 4807 -851 547 -165 O
ATOM 1851 CB THR A 302 4.211 8.463 51.057 1.00 46.71 C
ANISOU 1851 CB THR A 302 5863 7289 4596 -1521 707 -327 C
ATOM 1852 OG1 THR A 302 3.764 7.542 52.061 1.00 46.72 O
ANISOU 1852 OG1 THR A 302 6168 7336 4248 -1923 752 -275 O
ATOM 1853 CG2 THR A 302 3.119 8.624 50.009 1.00 47.07 C
ANISOU 1853 CG2 THR A 302 5638 7524 4722 -1526 850 -496 C
ATOM 1854 N ALA A 303 6.643 9.948 49.626 1.00 43.39 N
ANISOU 1854 N ALA A 303 5177 6501 4809 -739 434 -192 N
ATOM 1855 CA ALA A 303 7.100 10.893 48.617 1.00 43.45 C
ANISOU 1855 CA ALA A 303 4960 6473 5078 -480 412 -225 C
ATOM 1856 C ALA A 303 8.180 10.284 47.737 1.00 43.39 C
ANISOU 1856 C ALA A 303 5018 6254 5215 -314 327 -79 C
ATOM 1857 O ALA A 303 8.219 10.546 46.532 1.00 47.10 O
ANISOU 1857 O ALA A 303 5364 6698 5833 -192 366 -94 O
ATOM 1858 CB ALA A 303 7.611 12.169 49.286 1.00 44.77 C
ANISOU 1858 CB ALA A 303 5010 6689 5313 -384 346 -292 C
ATOM 1859 N ARG A 304 9.072 9.477 48.317 1.00 42.96 N
ANISOU 1859 N ARG A 304 5159 6056 5107 -293 198 46 N
ATOM 1860 CA ARG A 304 10.057 8.782 47.496 1.00 43.45 C
ANISOU 1860 CA ARG A 304 5262 5949 5297 -101 113 133 C
ATOM 1861 C ARG A 304 9.374 7.829 46.524 1.00 43.67 C
ANISOU 1861 C ARG A 304 5399 5902 5292 -149 195 142 C
ATOM 1862 O ARG A 304 9.730 7.776 45.337 1.00 46.02 O
ANISOU 1862 O ARG A 304 5594 6158 5734 3 226 132 O
ATOM 1863 CB ARG A 304 11.049 8.036 48.386 1.00 44.02 C
ANISOU 1863 CB ARG A 304 5543 5878 5303 -28 -91 232 C
ATOM 1864 CG ARG A 304 12.091 7.239 47.623 1.00 44.72 C
ANISOU 1864 CG ARG A 304 5658 5813 5521 225 -206 270 C
ATOM 1865 CD ARG A 304 13.284 6.916 48.508 1.00 52.10 C
ANISOU 1865 CD ARG A 304 6683 6660 6451 388 -455 318 C
ATOM 1866 NE ARG A 304 14.215 5.998 47.864 1.00 55.98 N
ANISOU 1866 NE ARG A 304 7211 7012 7047 671 -594 310 N
ATOM 1867 CZ ARG A 304 14.271 4.697 48.113 1.00 59.33 C
ANISOU 1867 CZ ARG A 304 8005 7187 7352 742 -775 376 C
ATOM 1868 NH1 ARG A 304 13.468 4.128 48.997 1.00 61.32 N
ANISOU 1868 NH1 ARG A 304 8648 7300 7351 494 -828 482 N
ATOM 1869 NH2 ARG A 304 15.157 3.949 47.461 1.00 58.27 N
ANISOU 1869 NH2 ARG A 304 7865 6939 7336 1062 -912 320 N
ATOM 1870 N MET A 305 8.370 7.088 47.003 1.00 41.99 N
ANISOU 1870 N MET A 305 5397 5690 4866 -398 241 151 N
ATOM 1871 CA MET A 305 7.630 6.206 46.104 1.00 43.30 C
ANISOU 1871 CA MET A 305 5673 5797 4983 -494 318 148 C
ATOM 1872 C MET A 305 6.951 6.997 44.991 1.00 45.26 C
ANISOU 1872 C MET A 305 5631 6207 5359 -451 459 31 C
ATOM 1873 O MET A 305 7.001 6.604 43.818 1.00 45.70 O
ANISOU 1873 O MET A 305 5684 6183 5497 -358 482 34 O
ATOM 1874 CB MET A 305 6.598 5.396 46.885 1.00 43.20 C
ANISOU 1874 CB MET A 305 5921 5807 4687 -855 362 162 C
ATOM 1875 CG MET A 305 5.862 4.379 46.031 1.00 46.14 C
ANISOU 1875 CG MET A 305 6453 6098 4981 -1007 422 163 C
ATOM 1876 SD MET A 305 4.531 3.549 46.916 1.00 56.55 S
ANISOU 1876 SD MET A 305 8041 7516 5929 -1544 517 154 S
ATOM 1877 CE MET A 305 3.425 4.927 47.212 1.00 54.95 C
ANISOU 1877 CE MET A 305 7360 7788 5730 -1656 724 -77 C
ATOM 1878 N LEU A 306 6.318 8.120 45.341 1.00 48.84 N
ANISOU 1878 N LEU A 306 5861 6877 5819 -498 530 -85 N
ATOM 1879 CA LEU A 306 5.611 8.925 44.350 1.00 43.02 C
ANISOU 1879 CA LEU A 306 4887 6271 5187 -428 608 -205 C
ATOM 1880 C LEU A 306 6.569 9.514 43.323 1.00 45.94 C
ANISOU 1880 C LEU A 306 5164 6533 5759 -185 563 -157 C
ATOM 1881 O LEU A 306 6.260 9.554 42.127 1.00 46.95 O
ANISOU 1881 O LEU A 306 5237 6655 5947 -129 600 -183 O
ATOM 1882 CB LEU A 306 4.823 10.037 45.043 1.00 42.50 C
ANISOU 1882 CB LEU A 306 4626 6434 5088 -469 647 -368 C
ATOM 1883 CG LEU A 306 3.609 9.609 45.869 1.00 43.94 C
ANISOU 1883 CG LEU A 306 4806 6839 5049 -749 749 -490 C
ATOM 1884 CD1 LEU A 306 2.984 10.809 46.561 1.00 41.89 C
ANISOU 1884 CD1 LEU A 306 4316 6824 4777 -716 778 -698 C
ATOM 1885 CD2 LEU A 306 2.590 8.898 44.992 1.00 45.95 C
ANISOU 1885 CD2 LEU A 306 5033 7180 5245 -884 831 -556 C
ATOM 1886 N MET A 307 7.731 9.991 43.772 1.00 43.97 N
ANISOU 1886 N MET A 307 4893 6220 5594 -69 485 -96 N
ATOM 1887 CA MET A 307 8.706 10.552 42.846 1.00 44.46 C
ANISOU 1887 CA MET A 307 4854 6224 5814 93 466 -62 C
ATOM 1888 C MET A 307 9.240 9.488 41.897 1.00 44.83 C
ANISOU 1888 C MET A 307 4982 6164 5889 170 482 -8 C
ATOM 1889 O MET A 307 9.419 9.750 40.702 1.00 46.37 O
ANISOU 1889 O MET A 307 5106 6357 6154 233 533 -19 O
ATOM 1890 CB MET A 307 9.846 11.213 43.620 1.00 46.13 C
ANISOU 1890 CB MET A 307 5003 6433 6091 155 381 -31 C
ATOM 1891 CG MET A 307 9.427 12.459 44.386 1.00 45.54 C
ANISOU 1891 CG MET A 307 4853 6444 6006 108 358 -107 C
ATOM 1892 SD MET A 307 10.729 13.091 45.460 1.00 45.03 S
ANISOU 1892 SD MET A 307 4748 6376 5985 133 241 -73 S
ATOM 1893 CE MET A 307 9.834 14.348 46.370 1.00 47.84 C
ANISOU 1893 CE MET A 307 5079 6816 6282 70 227 -203 C
ATOM 1894 N ILE A 308 9.493 8.279 42.404 1.00 49.10 N
ANISOU 1894 N ILE A 308 5704 6596 6355 166 424 44 N
ATOM 1895 CA ILE A 308 9.963 7.213 41.523 1.00 49.42 C
ANISOU 1895 CA ILE A 308 5850 6511 6418 276 416 61 C
ATOM 1896 C ILE A 308 8.880 6.831 40.516 1.00 49.34 C
ANISOU 1896 C ILE A 308 5894 6501 6351 176 515 24 C
ATOM 1897 O ILE A 308 9.166 6.601 39.331 1.00 48.78 O
ANISOU 1897 O ILE A 308 5800 6400 6334 272 561 0 O
ATOM 1898 CB ILE A 308 10.442 6.008 42.354 1.00 48.55 C
ANISOU 1898 CB ILE A 308 5993 6229 6227 320 274 120 C
ATOM 1899 CG1 ILE A 308 11.720 6.383 43.113 1.00 51.76 C
ANISOU 1899 CG1 ILE A 308 6297 6652 6716 483 145 135 C
ATOM 1900 CG2 ILE A 308 10.674 4.796 41.466 1.00 52.56 C
ANISOU 1900 CG2 ILE A 308 6671 6567 6731 438 247 108 C
ATOM 1901 CD1 ILE A 308 12.419 5.220 43.785 1.00 60.07 C
ANISOU 1901 CD1 ILE A 308 7601 7510 7713 621 -60 179 C
ATOM 1902 N VAL A 309 7.620 6.780 40.960 1.00 50.68 N
ANISOU 1902 N VAL A 309 6117 6741 6400 -31 554 -3 N
ATOM 1903 CA VAL A 309 6.517 6.500 40.042 1.00 46.54 C
ANISOU 1903 CA VAL A 309 5597 6265 5820 -142 634 -64 C
ATOM 1904 C VAL A 309 6.436 7.571 38.960 1.00 49.78 C
ANISOU 1904 C VAL A 309 5804 6769 6340 -34 675 -116 C
ATOM 1905 O VAL A 309 6.254 7.264 37.775 1.00 51.32 O
ANISOU 1905 O VAL A 309 6026 6936 6539 -8 710 -135 O
ATOM 1906 CB VAL A 309 5.190 6.378 40.815 1.00 41.12 C
ANISOU 1906 CB VAL A 309 4925 5720 4978 -405 677 -128 C
ATOM 1907 CG1 VAL A 309 4.010 6.409 39.858 1.00 39.67 C
ANISOU 1907 CG1 VAL A 309 4641 5667 4764 -497 744 -235 C
ATOM 1908 CG2 VAL A 309 5.166 5.100 41.636 1.00 45.60 C
ANISOU 1908 CG2 VAL A 309 5802 6149 5376 -591 637 -53 C
ATOM 1909 N LEU A 310 6.564 8.843 39.351 1.00 47.13 N
ANISOU 1909 N LEU A 310 5308 6527 6074 19 654 -139 N
ATOM 1910 CA LEU A 310 6.508 9.934 38.383 1.00 44.42 C
ANISOU 1910 CA LEU A 310 4851 6220 5805 104 652 -169 C
ATOM 1911 C LEU A 310 7.657 9.854 37.387 1.00 46.91 C
ANISOU 1911 C LEU A 310 5188 6451 6184 200 679 -104 C
ATOM 1912 O LEU A 310 7.466 10.091 36.188 1.00 47.53 O
ANISOU 1912 O LEU A 310 5277 6528 6255 213 704 -114 O
ATOM 1913 CB LEU A 310 6.524 11.281 39.105 1.00 44.15 C
ANISOU 1913 CB LEU A 310 4708 6246 5820 140 593 -205 C
ATOM 1914 CG LEU A 310 6.655 12.514 38.206 1.00 46.02 C
ANISOU 1914 CG LEU A 310 4916 6450 6118 219 544 -208 C
ATOM 1915 CD1 LEU A 310 5.494 12.588 37.227 1.00 46.28 C
ANISOU 1915 CD1 LEU A 310 4955 6521 6108 236 517 -284 C
ATOM 1916 CD2 LEU A 310 6.749 13.789 39.031 1.00 44.53 C
ANISOU 1916 CD2 LEU A 310 4680 6268 5970 255 458 -247 C
ATOM 1917 N LEU A 311 8.862 9.538 37.866 1.00 45.63 N
ANISOU 1917 N LEU A 311 5021 6246 6070 265 671 -57 N
ATOM 1918 CA LEU A 311 10.003 9.415 36.965 1.00 43.84 C
ANISOU 1918 CA LEU A 311 4752 6010 5894 352 719 -46 C
ATOM 1919 C LEU A 311 9.790 8.291 35.959 1.00 45.91 C
ANISOU 1919 C LEU A 311 5126 6213 6104 382 773 -76 C
ATOM 1920 O LEU A 311 10.056 8.460 34.761 1.00 44.13 O
ANISOU 1920 O LEU A 311 4880 6020 5867 393 847 -98 O
ATOM 1921 CB LEU A 311 11.284 9.184 37.768 1.00 43.33 C
ANISOU 1921 CB LEU A 311 4616 5952 5895 448 672 -36 C
ATOM 1922 CG LEU A 311 12.562 8.960 36.956 1.00 44.07 C
ANISOU 1922 CG LEU A 311 4594 6109 6042 554 731 -83 C
ATOM 1923 CD1 LEU A 311 12.865 10.168 36.083 1.00 42.64 C
ANISOU 1923 CD1 LEU A 311 4303 6037 5862 442 820 -80 C
ATOM 1924 CD2 LEU A 311 13.737 8.647 37.872 1.00 39.70 C
ANISOU 1924 CD2 LEU A 311 3938 5588 5558 688 640 -109 C
ATOM 1925 N VAL A 312 9.298 7.139 36.425 1.00 44.39 N
ANISOU 1925 N VAL A 312 5089 5925 5853 368 735 -79 N
ATOM 1926 CA VAL A 312 9.045 6.024 35.515 1.00 46.48 C
ANISOU 1926 CA VAL A 312 5506 6099 6057 383 766 -117 C
ATOM 1927 C VAL A 312 7.959 6.391 34.510 1.00 46.83 C
ANISOU 1927 C VAL A 312 5548 6205 6041 271 819 -145 C
ATOM 1928 O VAL A 312 8.064 6.074 33.318 1.00 47.14 O
ANISOU 1928 O VAL A 312 5633 6229 6048 302 874 -182 O
ATOM 1929 CB VAL A 312 8.684 4.755 36.308 1.00 44.68 C
ANISOU 1929 CB VAL A 312 5515 5713 5748 337 686 -98 C
ATOM 1930 CG1 VAL A 312 8.267 3.637 35.364 1.00 40.59 C
ANISOU 1930 CG1 VAL A 312 5199 5074 5151 316 704 -144 C
ATOM 1931 CG2 VAL A 312 9.865 4.316 37.158 1.00 42.74 C
ANISOU 1931 CG2 VAL A 312 5312 5372 5555 507 582 -77 C
ATOM 1932 N PHE A 313 6.904 7.068 34.970 1.00 45.43 N
ANISOU 1932 N PHE A 313 5309 6113 5839 156 790 -151 N
ATOM 1933 CA PHE A 313 5.835 7.486 34.068 1.00 46.33 C
ANISOU 1933 CA PHE A 313 5396 6303 5903 91 790 -202 C
ATOM 1934 C PHE A 313 6.365 8.427 32.994 1.00 49.27 C
ANISOU 1934 C PHE A 313 5727 6691 6302 165 803 -180 C
ATOM 1935 O PHE A 313 6.046 8.279 31.808 1.00 51.38 O
ANISOU 1935 O PHE A 313 6064 6955 6504 149 819 -202 O
ATOM 1936 CB PHE A 313 4.715 8.154 34.869 1.00 44.23 C
ANISOU 1936 CB PHE A 313 5016 6166 5623 11 737 -260 C
ATOM 1937 CG PHE A 313 3.515 8.538 34.046 1.00 46.27 C
ANISOU 1937 CG PHE A 313 5216 6529 5835 -16 690 -352 C
ATOM 1938 CD1 PHE A 313 3.467 9.757 33.386 1.00 44.89 C
ANISOU 1938 CD1 PHE A 313 4992 6366 5696 94 612 -359 C
ATOM 1939 CD2 PHE A 313 2.426 7.688 33.948 1.00 49.31 C
ANISOU 1939 CD2 PHE A 313 5613 6996 6125 -164 701 -438 C
ATOM 1940 CE1 PHE A 313 2.363 10.112 32.633 1.00 46.02 C
ANISOU 1940 CE1 PHE A 313 5098 6594 5795 112 516 -454 C
ATOM 1941 CE2 PHE A 313 1.317 8.040 33.200 1.00 48.72 C
ANISOU 1941 CE2 PHE A 313 5445 7053 6012 -171 632 -550 C
ATOM 1942 CZ PHE A 313 1.287 9.252 32.541 1.00 47.32 C
ANISOU 1942 CZ PHE A 313 5217 6880 5884 -5 526 -560 C
ATOM 1943 N ALA A 314 7.181 9.405 33.396 1.00 48.27 N
ANISOU 1943 N ALA A 314 5515 6579 6247 210 794 -134 N
ATOM 1944 CA ALA A 314 7.735 10.350 32.435 1.00 47.56 C
ANISOU 1944 CA ALA A 314 5432 6496 6144 207 809 -98 C
ATOM 1945 C ALA A 314 8.633 9.647 31.428 1.00 48.76 C
ANISOU 1945 C ALA A 314 5622 6652 6252 218 928 -106 C
ATOM 1946 O ALA A 314 8.555 9.915 30.223 1.00 52.74 O
ANISOU 1946 O ALA A 314 6208 7166 6664 166 960 -102 O
ATOM 1947 CB ALA A 314 8.504 11.453 33.163 1.00 47.57 C
ANISOU 1947 CB ALA A 314 5352 6507 6215 203 779 -51 C
ATOM 1948 N ILE A 315 9.482 8.730 31.899 1.00 49.82 N
ANISOU 1948 N ILE A 315 5710 6782 6437 300 981 -136 N
ATOM 1949 CA ILE A 315 10.378 8.018 30.993 1.00 48.42 C
ANISOU 1949 CA ILE A 315 5532 6638 6226 361 1092 -201 C
ATOM 1950 C ILE A 315 9.581 7.176 30.003 1.00 52.44 C
ANISOU 1950 C ILE A 315 6204 7086 6633 345 1112 -248 C
ATOM 1951 O ILE A 315 9.883 7.149 28.803 1.00 51.46 O
ANISOU 1951 O ILE A 315 6117 7016 6420 320 1204 -291 O
ATOM 1952 CB ILE A 315 11.383 7.166 31.792 1.00 45.60 C
ANISOU 1952 CB ILE A 315 5098 6271 5957 522 1085 -256 C
ATOM 1953 CG1 ILE A 315 12.386 8.070 32.513 1.00 44.59 C
ANISOU 1953 CG1 ILE A 315 4772 6256 5915 521 1081 -234 C
ATOM 1954 CG2 ILE A 315 12.109 6.191 30.880 1.00 43.71 C
ANISOU 1954 CG2 ILE A 315 4868 6056 5684 649 1173 -383 C
ATOM 1955 CD1 ILE A 315 13.457 7.315 33.272 1.00 43.58 C
ANISOU 1955 CD1 ILE A 315 4537 6145 5875 713 1035 -308 C
ATOM 1956 N CYS A 316 8.539 6.490 30.482 1.00 52.40 N
ANISOU 1956 N CYS A 316 6306 6988 6617 323 1031 -249 N
ATOM 1957 CA CYS A 316 7.776 5.608 29.605 1.00 54.46 C
ANISOU 1957 CA CYS A 316 6728 7189 6776 280 1037 -305 C
ATOM 1958 C CYS A 316 6.909 6.380 28.618 1.00 54.52 C
ANISOU 1958 C CYS A 316 6758 7262 6694 176 1014 -293 C
ATOM 1959 O CYS A 316 6.682 5.905 27.499 1.00 55.90 O
ANISOU 1959 O CYS A 316 7049 7426 6763 148 1046 -342 O
ATOM 1960 CB CYS A 316 6.910 4.662 30.436 1.00 55.38 C
ANISOU 1960 CB CYS A 316 6960 7203 6878 216 960 -312 C
ATOM 1961 SG CYS A 316 7.846 3.474 31.420 1.00 60.13 S
ANISOU 1961 SG CYS A 316 7678 7639 7530 349 921 -321 S
ATOM 1962 N TYR A 317 6.406 7.554 29.004 1.00 51.49 N
ANISOU 1962 N TYR A 317 6290 6932 6341 138 932 -240 N
ATOM 1963 CA TYR A 317 5.523 8.315 28.131 1.00 48.64 C
ANISOU 1963 CA TYR A 317 5981 6604 5897 88 843 -238 C
ATOM 1964 C TYR A 317 6.243 9.363 27.292 1.00 49.73 C
ANISOU 1964 C TYR A 317 6176 6745 5972 64 862 -170 C
ATOM 1965 O TYR A 317 5.607 9.977 26.428 1.00 52.09 O
ANISOU 1965 O TYR A 317 6590 7032 6169 28 759 -154 O
ATOM 1966 CB TYR A 317 4.421 8.991 28.955 1.00 46.61 C
ANISOU 1966 CB TYR A 317 5623 6395 5692 94 700 -262 C
ATOM 1967 CG TYR A 317 3.275 8.070 29.307 1.00 49.67 C
ANISOU 1967 CG TYR A 317 5977 6840 6054 24 671 -356 C
ATOM 1968 CD1 TYR A 317 3.429 7.069 30.258 1.00 51.03 C
ANISOU 1968 CD1 TYR A 317 6151 6985 6253 -34 742 -363 C
ATOM 1969 CD2 TYR A 317 2.036 8.205 28.692 1.00 48.67 C
ANISOU 1969 CD2 TYR A 317 5833 6802 5859 -6 557 -442 C
ATOM 1970 CE1 TYR A 317 2.383 6.224 30.583 1.00 50.65 C
ANISOU 1970 CE1 TYR A 317 6109 6993 6143 -178 727 -442 C
ATOM 1971 CE2 TYR A 317 0.984 7.367 29.012 1.00 49.68 C
ANISOU 1971 CE2 TYR A 317 5899 7031 5946 -127 546 -548 C
ATOM 1972 CZ TYR A 317 1.163 6.379 29.959 1.00 52.48 C
ANISOU 1972 CZ TYR A 317 6277 7355 6307 -242 645 -542 C
ATOM 1973 OH TYR A 317 0.118 5.542 30.282 1.00 51.60 O
ANISOU 1973 OH TYR A 317 6140 7348 6118 -440 646 -641 O
ATOM 1974 N LEU A 318 7.537 9.589 27.521 1.00 50.03 N
ANISOU 1974 N LEU A 318 6149 6809 6051 62 976 -136 N
ATOM 1975 CA LEU A 318 8.277 10.523 26.674 1.00 50.15 C
ANISOU 1975 CA LEU A 318 6239 6855 5962 -46 1026 -76 C
ATOM 1976 C LEU A 318 8.340 10.091 25.213 1.00 52.48 C
ANISOU 1976 C LEU A 318 6680 7182 6076 -123 1113 -109 C
ATOM 1977 O LEU A 318 8.021 10.915 24.337 1.00 52.03 O
ANISOU 1977 O LEU A 318 6806 7091 5871 -234 1038 -41 O
ATOM 1978 CB LEU A 318 9.682 10.733 27.249 1.00 47.85 C
ANISOU 1978 CB LEU A 318 5788 6647 5744 -66 1153 -72 C
ATOM 1979 CG LEU A 318 10.572 11.731 26.505 1.00 47.65 C
ANISOU 1979 CG LEU A 318 5819 6693 5592 -261 1237 -15 C
ATOM 1980 CD1 LEU A 318 10.012 13.142 26.623 1.00 45.62 C
ANISOU 1980 CD1 LEU A 318 5730 6305 5300 -352 1053 106 C
ATOM 1981 CD2 LEU A 318 12.005 11.670 27.016 1.00 44.43 C
ANISOU 1981 CD2 LEU A 318 5179 6446 5257 -284 1390 -69 C
ATOM 1982 N PRO A 319 8.732 8.854 24.871 1.00 51.42 N
ANISOU 1982 N PRO A 319 6516 7095 5927 -65 1249 -215 N
ATOM 1983 CA PRO A 319 8.916 8.537 23.444 1.00 53.41 C
ANISOU 1983 CA PRO A 319 6909 7403 5981 -151 1354 -267 C
ATOM 1984 C PRO A 319 7.637 8.607 22.629 1.00 55.15 C
ANISOU 1984 C PRO A 319 7336 7545 6072 -201 1203 -240 C
ATOM 1985 O PRO A 319 7.655 9.144 21.516 1.00 57.41 O
ANISOU 1985 O PRO A 319 7802 7852 6160 -335 1206 -199 O
ATOM 1986 CB PRO A 319 9.495 7.115 23.476 1.00 51.91 C
ANISOU 1986 CB PRO A 319 6640 7246 5838 -11 1486 -422 C
ATOM 1987 CG PRO A 319 9.018 6.549 24.754 1.00 52.38 C
ANISOU 1987 CG PRO A 319 6633 7191 6079 120 1373 -417 C
ATOM 1988 CD PRO A 319 9.042 7.689 25.721 1.00 49.80 C
ANISOU 1988 CD PRO A 319 6193 6872 5858 86 1292 -302 C
ATOM 1989 N ILE A 320 6.524 8.085 23.149 1.00 54.68 N
ANISOU 1989 N ILE A 320 7260 7414 6100 -119 1065 -270 N
ATOM 1990 CA ILE A 320 5.287 8.087 22.374 1.00 55.69 C
ANISOU 1990 CA ILE A 320 7534 7513 6111 -157 907 -282 C
ATOM 1991 C ILE A 320 4.789 9.512 22.161 1.00 58.86 C
ANISOU 1991 C ILE A 320 8026 7879 6458 -184 712 -181 C
ATOM 1992 O ILE A 320 4.354 9.872 21.060 1.00 60.14 O
ANISOU 1992 O ILE A 320 8394 8018 6438 -246 605 -155 O
ATOM 1993 CB ILE A 320 4.226 7.195 23.047 1.00 56.00 C
ANISOU 1993 CB ILE A 320 7493 7536 6247 -111 820 -364 C
ATOM 1994 CG1 ILE A 320 2.912 7.243 22.262 1.00 55.87 C
ANISOU 1994 CG1 ILE A 320 7569 7543 6115 -155 639 -408 C
ATOM 1995 CG2 ILE A 320 4.019 7.588 24.507 1.00 55.63 C
ANISOU 1995 CG2 ILE A 320 7259 7496 6381 -52 762 -339 C
ATOM 1996 CD1 ILE A 320 1.888 6.236 22.727 1.00 58.43 C
ANISOU 1996 CD1 ILE A 320 7818 7900 6484 -193 588 -516 C
ATOM 1997 N SER A 321 4.864 10.352 23.196 1.00 51.33 N
ANISOU 1997 N SER A 321 6959 6899 5646 -128 640 -126 N
ATOM 1998 CA SER A 321 4.429 11.738 23.056 1.00 52.47 C
ANISOU 1998 CA SER A 321 7233 6959 5743 -116 418 -44 C
ATOM 1999 C SER A 321 5.313 12.501 22.076 1.00 55.84 C
ANISOU 1999 C SER A 321 7911 7335 5972 -287 469 74 C
ATOM 2000 O SER A 321 4.812 13.255 21.231 1.00 59.35 O
ANISOU 2000 O SER A 321 8622 7679 6250 -325 270 139 O
ATOM 2001 CB SER A 321 4.421 12.421 24.423 1.00 53.41 C
ANISOU 2001 CB SER A 321 7188 7055 6050 -20 349 -34 C
ATOM 2002 OG SER A 321 3.575 11.733 25.329 1.00 47.75 O
ANISOU 2002 OG SER A 321 6253 6419 5473 84 321 -149 O
ATOM 2003 N ILE A 322 6.633 12.310 22.165 1.00 61.28 N
ANISOU 2003 N ILE A 322 8524 8104 6657 -405 724 91 N
ATOM 2004 CA ILE A 322 7.545 13.007 21.261 1.00 60.58 C
ANISOU 2004 CA ILE A 322 8644 8026 6347 -644 822 184 C
ATOM 2005 C ILE A 322 7.317 12.562 19.821 1.00 65.93 C
ANISOU 2005 C ILE A 322 9545 8735 6770 -751 855 164 C
ATOM 2006 O ILE A 322 7.288 13.388 18.901 1.00 67.40 O
ANISOU 2006 O ILE A 322 10056 8843 6712 -930 757 274 O
ATOM 2007 CB ILE A 322 9.005 12.792 21.702 1.00 55.95 C
ANISOU 2007 CB ILE A 322 7837 7602 5819 -742 1106 147 C
ATOM 2008 CG1 ILE A 322 9.263 13.491 23.037 1.00 54.56 C
ANISOU 2008 CG1 ILE A 322 7509 7375 5847 -685 1036 194 C
ATOM 2009 CG2 ILE A 322 9.966 13.305 20.642 1.00 53.52 C
ANISOU 2009 CG2 ILE A 322 7702 7394 5240 -1053 1273 196 C
ATOM 2010 CD1 ILE A 322 8.972 14.973 23.015 1.00 51.80 C
ANISOU 2010 CD1 ILE A 322 7425 6841 5414 -793 813 338 C
ATOM 2011 N LEU A 323 7.152 11.254 19.601 1.00 61.47 N
ANISOU 2011 N LEU A 323 8857 8264 6235 -658 976 27 N
ATOM 2012 CA LEU A 323 6.913 10.754 18.250 1.00 66.23 C
ANISOU 2012 CA LEU A 323 9671 8901 6591 -753 1008 -16 C
ATOM 2013 C LEU A 323 5.578 11.244 17.704 1.00 69.11 C
ANISOU 2013 C LEU A 323 10278 9127 6852 -714 680 46 C
ATOM 2014 O LEU A 323 5.470 11.561 16.514 1.00 74.98 O
ANISOU 2014 O LEU A 323 11329 9844 7317 -864 618 101 O
ATOM 2015 CB LEU A 323 6.976 9.227 18.235 1.00 67.32 C
ANISOU 2015 CB LEU A 323 9649 9129 6802 -638 1174 -193 C
ATOM 2016 CG LEU A 323 8.365 8.615 18.430 1.00 68.27 C
ANISOU 2016 CG LEU A 323 9568 9406 6967 -638 1482 -307 C
ATOM 2017 CD1 LEU A 323 8.299 7.096 18.376 1.00 75.89 C
ANISOU 2017 CD1 LEU A 323 10459 10384 7992 -479 1572 -491 C
ATOM 2018 CD2 LEU A 323 9.337 9.153 17.391 1.00 70.39 C
ANISOU 2018 CD2 LEU A 323 9954 9828 6962 -889 1676 -298 C
ATOM 2019 N ASN A 324 4.548 11.306 18.553 1.00 65.84 N
ANISOU 2019 N ASN A 324 9725 8648 6644 -514 459 19 N
ATOM 2020 CA ASN A 324 3.263 11.835 18.110 1.00 65.48 C
ANISOU 2020 CA ASN A 324 9846 8508 6524 -427 111 33 C
ATOM 2021 C ASN A 324 3.382 13.300 17.712 1.00 69.32 C
ANISOU 2021 C ASN A 324 10654 8829 6854 -497 -100 195 C
ATOM 2022 O ASN A 324 2.802 13.727 16.707 1.00 74.45 O
ANISOU 2022 O ASN A 324 11619 9385 7283 -524 -337 246 O
ATOM 2023 CB ASN A 324 2.216 11.654 19.209 1.00 59.48 C
ANISOU 2023 CB ASN A 324 8802 7779 6019 -209 -49 -73 C
ATOM 2024 CG ASN A 324 0.843 12.135 18.789 1.00 62.85 C
ANISOU 2024 CG ASN A 324 9316 8174 6392 -73 -421 -122 C
ATOM 2025 OD1 ASN A 324 0.096 11.418 18.122 1.00 65.21 O
ANISOU 2025 OD1 ASN A 324 9624 8550 6605 -77 -491 -218 O
ATOM 2026 ND2 ASN A 324 0.500 13.356 19.181 1.00 63.38 N
ANISOU 2026 ND2 ASN A 324 9446 8128 6509 67 -683 -79 N
ATOM 2027 N VAL A 325 4.136 14.086 18.486 1.00 71.95 N
ANISOU 2027 N VAL A 325 10952 9103 7282 -538 -41 281 N
ATOM 2028 CA VAL A 325 4.354 15.486 18.129 1.00 72.09 C
ANISOU 2028 CA VAL A 325 11344 8919 7129 -655 -241 448 C
ATOM 2029 C VAL A 325 5.102 15.593 16.806 1.00 78.26 C
ANISOU 2029 C VAL A 325 12477 9708 7552 -987 -104 555 C
ATOM 2030 O VAL A 325 4.745 16.397 15.936 1.00 85.51 O
ANISOU 2030 O VAL A 325 13837 10441 8211 -1079 -366 677 O
ATOM 2031 CB VAL A 325 5.103 16.218 19.258 1.00 67.88 C
ANISOU 2031 CB VAL A 325 10694 8335 6763 -679 -173 504 C
ATOM 2032 CG1 VAL A 325 5.561 17.591 18.788 1.00 74.11 C
ANISOU 2032 CG1 VAL A 325 11936 8900 7323 -899 -329 691 C
ATOM 2033 CG2 VAL A 325 4.215 16.347 20.474 1.00 66.19 C
ANISOU 2033 CG2 VAL A 325 10218 8091 6841 -359 -368 400 C
ATOM 2034 N LEU A 326 6.150 14.785 16.632 1.00 79.39 N
ANISOU 2034 N LEU A 326 12440 10069 7655 -1167 296 495 N
ATOM 2035 CA LEU A 326 6.951 14.864 15.415 1.00 85.23 C
ANISOU 2035 CA LEU A 326 13461 10889 8035 -1517 487 556 C
ATOM 2036 C LEU A 326 6.165 14.428 14.186 1.00 91.55 C
ANISOU 2036 C LEU A 326 14528 11668 8590 -1523 354 536 C
ATOM 2037 O LEU A 326 6.374 14.971 13.095 1.00 98.99 O
ANISOU 2037 O LEU A 326 15893 12554 9165 -1802 315 653 O
ATOM 2038 CB LEU A 326 8.217 14.018 15.560 1.00 80.94 C
ANISOU 2038 CB LEU A 326 12583 10639 7532 -1641 942 425 C
ATOM 2039 CG LEU A 326 9.222 14.468 16.622 1.00 76.80 C
ANISOU 2039 CG LEU A 326 11804 10187 7190 -1703 1102 439 C
ATOM 2040 CD1 LEU A 326 10.442 13.560 16.632 1.00 72.29 C
ANISOU 2040 CD1 LEU A 326 10883 9940 6642 -1778 1517 262 C
ATOM 2041 CD2 LEU A 326 9.628 15.914 16.399 1.00 78.66 C
ANISOU 2041 CD2 LEU A 326 12402 10279 7208 -2024 997 639 C
ATOM 2042 N LYS A 327 5.263 13.456 14.335 1.00 76.29 N
ANISOU 2042 N LYS A 327 12378 9782 6828 -1256 278 390 N
ATOM 2043 CA LYS A 327 4.516 12.965 13.182 1.00 79.48 C
ANISOU 2043 CA LYS A 327 13007 10187 7004 -1267 150 348 C
ATOM 2044 C LYS A 327 3.322 13.855 12.858 1.00 79.74 C
ANISOU 2044 C LYS A 327 13350 9995 6952 -1138 -343 445 C
ATOM 2045 O LYS A 327 3.019 14.082 11.681 1.00 87.55 O
ANISOU 2045 O LYS A 327 14738 10912 7613 -1267 -509 514 O
ATOM 2046 CB LYS A 327 4.055 11.527 13.426 1.00 75.17 C
ANISOU 2046 CB LYS A 327 12130 9782 6649 -1081 265 142 C
ATOM 2047 CG LYS A 327 3.385 10.882 12.219 1.00 79.57 C
ANISOU 2047 CG LYS A 327 12901 10369 6965 -1124 174 70 C
ATOM 2048 CD LYS A 327 3.001 9.434 12.487 1.00 72.41 C
ANISOU 2048 CD LYS A 327 11707 9573 6232 -988 296 -135 C
ATOM 2049 CE LYS A 327 1.950 9.330 13.579 1.00 75.29 C
ANISOU 2049 CE LYS A 327 11791 9903 6913 -748 75 -190 C
ATOM 2050 NZ LYS A 327 1.552 7.917 13.830 1.00 78.98 N
ANISOU 2050 NZ LYS A 327 12047 10454 7509 -689 182 -371 N
ATOM 2051 N ARG A 328 2.635 14.369 13.878 1.00 83.53 N
ANISOU 2051 N ARG A 328 13659 10370 7710 -867 -598 433 N
ATOM 2052 CA ARG A 328 1.414 15.134 13.658 1.00 86.28 C
ANISOU 2052 CA ARG A 328 14224 10536 8024 -649 -1101 456 C
ATOM 2053 C ARG A 328 1.674 16.634 13.552 1.00 95.26 C
ANISOU 2053 C ARG A 328 15805 11385 9005 -719 -1365 656 C
ATOM 2054 O ARG A 328 1.166 17.290 12.638 1.00 96.96 O
ANISOU 2054 O ARG A 328 16485 11402 8952 -726 -1724 755 O
ATOM 2055 CB ARG A 328 0.415 14.851 14.784 1.00 81.08 C
ANISOU 2055 CB ARG A 328 13118 9958 7731 -299 -1251 277 C
ATOM 2056 CG ARG A 328 -0.068 13.410 14.840 1.00 76.88 C
ANISOU 2056 CG ARG A 328 12231 9666 7315 -257 -1075 86 C
ATOM 2057 CD ARG A 328 -0.883 13.051 13.609 1.00 75.52 C
ANISOU 2057 CD ARG A 328 12273 9516 6907 -270 -1293 36 C
ATOM 2058 NE ARG A 328 -1.374 11.679 13.657 1.00 75.74 N
ANISOU 2058 NE ARG A 328 11997 9751 7030 -266 -1143 -151 N
ATOM 2059 CZ ARG A 328 -2.130 11.122 12.721 1.00 79.70 C
ANISOU 2059 CZ ARG A 328 12598 10319 7365 -287 -1295 -240 C
ATOM 2060 NH1 ARG A 328 -2.507 11.794 11.645 1.00 78.69 N
ANISOU 2060 NH1 ARG A 328 12859 10076 6962 -291 -1615 -159 N
ATOM 2061 NH2 ARG A 328 -2.518 9.858 12.867 1.00 80.83 N
ANISOU 2061 NH2 ARG A 328 12481 10630 7602 -322 -1143 -409 N
ATOM 2062 N VAL A 329 2.457 17.189 14.475 1.00 96.80 N
ANISOU 2062 N VAL A 329 14861 12331 9588 2569 -3254 1643 N
ATOM 2063 CA VAL A 329 2.687 18.632 14.488 1.00 96.70 C
ANISOU 2063 CA VAL A 329 15250 11956 9536 2652 -3215 1956 C
ATOM 2064 C VAL A 329 3.751 19.018 13.469 1.00100.51 C
ANISOU 2064 C VAL A 329 16562 12272 9353 2385 -2861 2201 C
ATOM 2065 O VAL A 329 3.495 19.794 12.541 1.00105.01 O
ANISOU 2065 O VAL A 329 17835 12577 9486 2500 -3180 2494 O
ATOM 2066 CB VAL A 329 3.067 19.103 15.904 1.00 92.60 C
ANISOU 2066 CB VAL A 329 14196 11381 9605 2610 -2808 1883 C
ATOM 2067 CG1 VAL A 329 3.312 20.602 15.915 1.00 92.12 C
ANISOU 2067 CG1 VAL A 329 14553 10922 9526 2682 -2749 2188 C
ATOM 2068 CG2 VAL A 329 1.980 18.720 16.897 1.00 88.02 C
ANISOU 2068 CG2 VAL A 329 12842 10957 9645 2836 -3114 1625 C
ATOM 2069 N PHE A 330 4.960 18.480 13.624 1.00 91.11 N
ANISOU 2069 N PHE A 330 15318 11220 8079 2021 -2195 2071 N
ATOM 2070 CA PHE A 330 6.058 18.821 12.729 1.00 93.85 C
ANISOU 2070 CA PHE A 330 16390 11422 7847 1704 -1739 2235 C
ATOM 2071 C PHE A 330 6.037 18.027 11.430 1.00100.37 C
ANISOU 2071 C PHE A 330 17715 12389 8030 1588 -1873 2205 C
ATOM 2072 O PHE A 330 6.804 18.349 10.516 1.00100.93 O
ANISOU 2072 O PHE A 330 18504 12319 7527 1324 -1544 2355 O
ATOM 2073 CB PHE A 330 7.396 18.618 13.443 1.00 89.30 C
ANISOU 2073 CB PHE A 330 15496 10930 7506 1367 -965 2051 C
ATOM 2074 CG PHE A 330 7.603 19.542 14.609 1.00 89.73 C
ANISOU 2074 CG PHE A 330 15199 10810 8085 1420 -767 2097 C
ATOM 2075 CD1 PHE A 330 6.970 20.774 14.654 1.00 87.37 C
ANISOU 2075 CD1 PHE A 330 15164 10182 7850 1653 -1090 2378 C
ATOM 2076 CD2 PHE A 330 8.427 19.179 15.662 1.00 88.30 C
ANISOU 2076 CD2 PHE A 330 14435 10781 8335 1252 -287 1848 C
ATOM 2077 CE1 PHE A 330 7.156 21.627 15.724 1.00 85.02 C
ANISOU 2077 CE1 PHE A 330 14546 9719 8039 1692 -894 2394 C
ATOM 2078 CE2 PHE A 330 8.617 20.028 16.736 1.00 86.81 C
ANISOU 2078 CE2 PHE A 330 13939 10443 8603 1290 -117 1869 C
ATOM 2079 CZ PHE A 330 7.981 21.254 16.767 1.00 88.74 C
ANISOU 2079 CZ PHE A 330 14441 10368 8909 1498 -400 2134 C
ATOM 2080 N GLY A 331 5.185 17.011 11.324 1.00106.47 N
ANISOU 2080 N GLY A 331 18143 13429 8880 1751 -2317 1996 N
ATOM 2081 CA GLY A 331 5.065 16.256 10.088 1.00110.75 C
ANISOU 2081 CA GLY A 331 19154 14112 8815 1660 -2504 1942 C
ATOM 2082 C GLY A 331 6.311 15.497 9.694 1.00109.37 C
ANISOU 2082 C GLY A 331 19124 14089 8343 1242 -1822 1753 C
ATOM 2083 O GLY A 331 6.587 15.348 8.499 1.00113.59 O
ANISOU 2083 O GLY A 331 20344 14611 8204 1063 -1770 1809 O
ATOM 2084 N MET A 332 7.073 15.007 10.667 1.00106.90 N
ANISOU 2084 N MET A 332 18189 13914 8515 1088 -1305 1511 N
ATOM 2085 CA MET A 332 8.262 14.226 10.371 1.00107.37 C
ANISOU 2085 CA MET A 332 18276 14120 8399 727 -674 1267 C
ATOM 2086 C MET A 332 7.873 12.795 10.006 1.00107.92 C
ANISOU 2086 C MET A 332 18116 14484 8403 732 -876 967 C
ATOM 2087 O MET A 332 6.699 12.413 10.033 1.00107.72 O
ANISOU 2087 O MET A 332 17880 14558 8491 993 -1481 938 O
ATOM 2088 CB MET A 332 9.224 14.248 11.556 1.00104.89 C
ANISOU 2088 CB MET A 332 17382 13824 8648 599 -118 1107 C
ATOM 2089 CG MET A 332 9.876 15.597 11.801 1.00106.34 C
ANISOU 2089 CG MET A 332 17832 13720 8851 493 230 1338 C
ATOM 2090 SD MET A 332 11.116 15.522 13.107 1.00116.59 S
ANISOU 2090 SD MET A 332 18446 15076 10776 316 876 1077 S
ATOM 2091 CE MET A 332 12.199 14.244 12.470 1.00101.34 C
ANISOU 2091 CE MET A 332 16491 13378 8637 -6 1382 693 C
ATOM 2092 N PHE A 333 8.881 11.998 9.648 1.00108.01 N
ANISOU 2092 N PHE A 333 18155 14627 8256 431 -349 709 N
ATOM 2093 CA PHE A 333 8.725 10.584 9.310 1.00107.07 C
ANISOU 2093 CA PHE A 333 17823 14764 8095 386 -422 381 C
ATOM 2094 C PHE A 333 7.814 10.373 8.105 1.00114.73 C
ANISOU 2094 C PHE A 333 19328 15783 8480 461 -953 446 C
ATOM 2095 O PHE A 333 7.227 9.297 7.948 1.00116.85 O
ANISOU 2095 O PHE A 333 19344 16253 8800 527 -1241 204 O
ATOM 2096 CB PHE A 333 8.208 9.781 10.510 1.00 92.88 C
ANISOU 2096 CB PHE A 333 15186 13116 6989 583 -621 178 C
ATOM 2097 CG PHE A 333 8.892 10.116 11.805 1.00 90.27 C
ANISOU 2097 CG PHE A 333 14349 12722 7230 578 -252 161 C
ATOM 2098 CD1 PHE A 333 10.271 10.241 11.867 1.00 90.54 C
ANISOU 2098 CD1 PHE A 333 14418 12711 7270 321 392 57 C
ATOM 2099 CD2 PHE A 333 8.154 10.321 12.959 1.00 84.95 C
ANISOU 2099 CD2 PHE A 333 13157 12033 7085 819 -547 219 C
ATOM 2100 CE1 PHE A 333 10.900 10.555 13.057 1.00 83.85 C
ANISOU 2100 CE1 PHE A 333 13102 11814 6944 328 681 18 C
ATOM 2101 CE2 PHE A 333 8.777 10.635 14.152 1.00 80.41 C
ANISOU 2101 CE2 PHE A 333 12159 11404 6989 809 -230 198 C
ATOM 2102 CZ PHE A 333 10.152 10.752 14.200 1.00 81.03 C
ANISOU 2102 CZ PHE A 333 12280 11444 7063 574 357 102 C
ATOM 2103 N ALA A 334 7.681 11.383 7.245 1.00117.74 N
ANISOU 2103 N ALA A 334 20476 15968 8294 450 -1104 766 N
ATOM 2104 CA ALA A 334 6.798 11.313 6.084 1.00122.22 C
ANISOU 2104 CA ALA A 334 21631 16554 8253 552 -1689 863 C
ATOM 2105 C ALA A 334 7.567 11.036 4.796 1.00138.49 C
ANISOU 2105 C ALA A 334 24447 18634 9538 193 -1302 794 C
ATOM 2106 O ALA A 334 7.273 10.069 4.087 1.00139.11 O
ANISOU 2106 O ALA A 334 24526 18913 9416 137 -1464 552 O
ATOM 2107 CB ALA A 334 5.994 12.613 5.958 1.00118.87 C
ANISOU 2107 CB ALA A 334 21620 15864 7681 834 -2241 1282 C
ATOM 2108 N HIS A 335 8.554 11.871 4.483 1.00155.71 N
ANISOU 2108 N HIS A 335 27044 20606 11511 -80 -724 958 N
ATOM 2109 CA HIS A 335 9.340 11.734 3.265 1.00158.14 C
ANISOU 2109 CA HIS A 335 27822 20902 11363 -448 -259 867 C
ATOM 2110 C HIS A 335 10.528 10.795 3.436 1.00160.04 C
ANISOU 2110 C HIS A 335 27735 21319 11753 -773 492 444 C
ATOM 2111 O HIS A 335 11.346 10.674 2.520 1.00163.69 O
ANISOU 2111 O HIS A 335 28493 21763 11938 -1098 977 315 O
ATOM 2112 CB HIS A 335 9.823 13.110 2.794 1.00161.28 C
ANISOU 2112 CB HIS A 335 28802 20957 11522 -600 2 1212 C
ATOM 2113 CG HIS A 335 10.138 13.175 1.332 1.00167.49 C
ANISOU 2113 CG HIS A 335 30229 21672 11740 -866 171 1228 C
ATOM 2114 ND1 HIS A 335 10.697 14.287 0.740 1.00172.51 N
ANISOU 2114 ND1 HIS A 335 31461 21988 12097 -1080 488 1479 N
ATOM 2115 CD2 HIS A 335 9.969 12.267 0.341 1.00172.01 C
ANISOU 2115 CD2 HIS A 335 30960 22437 11959 -960 70 1016 C
ATOM 2116 CE1 HIS A 335 10.861 14.061 -0.551 1.00175.92 C
ANISOU 2116 CE1 HIS A 335 32412 22417 12011 -1297 577 1428 C
ATOM 2117 NE2 HIS A 335 10.427 12.843 -0.819 1.00176.48 N
ANISOU 2117 NE2 HIS A 335 32226 22805 12025 -1224 327 1150 N
ATOM 2118 N THR A 336 10.645 10.133 4.584 1.00149.67 N
ANISOU 2118 N THR A 336 25804 20156 10907 -680 592 207 N
ATOM 2119 CA THR A 336 11.734 9.199 4.835 1.00150.54 C
ANISOU 2119 CA THR A 336 25470 20419 11310 -930 1249 -232 C
ATOM 2120 C THR A 336 11.272 7.790 4.483 1.00150.53 C
ANISOU 2120 C THR A 336 25238 20668 11288 -880 994 -572 C
ATOM 2121 O THR A 336 10.255 7.317 5.002 1.00147.94 O
ANISOU 2121 O THR A 336 24466 20440 11304 -573 404 -576 O
ATOM 2122 CB THR A 336 12.184 9.266 6.293 1.00143.96 C
ANISOU 2122 CB THR A 336 23799 19573 11328 -811 1464 -310 C
ATOM 2123 OG1 THR A 336 11.104 8.864 7.147 1.00133.91 O
ANISOU 2123 OG1 THR A 336 21948 18390 10540 -439 841 -276 O
ATOM 2124 CG2 THR A 336 12.605 10.682 6.651 1.00142.43 C
ANISOU 2124 CG2 THR A 336 23821 19124 11172 -865 1703 5 C
ATOM 2125 N GLU A 337 12.015 7.126 3.600 1.00150.81 N
ANISOU 2125 N GLU A 337 25401 20786 11115 -1162 1430 -865 N
ATOM 2126 CA GLU A 337 11.714 5.750 3.228 1.00148.98 C
ANISOU 2126 CA GLU A 337 24963 20771 10870 -1153 1279 -1232 C
ATOM 2127 C GLU A 337 12.256 4.739 4.228 1.00148.11 C
ANISOU 2127 C GLU A 337 24138 20772 11367 -1148 1590 -1633 C
ATOM 2128 O GLU A 337 12.078 3.533 4.024 1.00147.21 O
ANISOU 2128 O GLU A 337 23796 20806 11330 -1145 1508 -1969 O
ATOM 2129 CB GLU A 337 12.265 5.446 1.832 1.00152.46 C
ANISOU 2129 CB GLU A 337 25792 21230 10905 -1423 1591 -1379 C
ATOM 2130 CG GLU A 337 11.580 6.221 0.719 1.00159.16 C
ANISOU 2130 CG GLU A 337 27353 21988 11133 -1412 1191 -1026 C
ATOM 2131 CD GLU A 337 12.110 5.859 -0.655 1.00171.95 C
ANISOU 2131 CD GLU A 337 29386 23629 12317 -1695 1509 -1194 C
ATOM 2132 OE1 GLU A 337 13.137 5.153 -0.730 1.00173.94 O
ANISOU 2132 OE1 GLU A 337 29369 23932 12788 -1916 2104 -1565 O
ATOM 2133 OE2 GLU A 337 11.497 6.278 -1.659 1.00176.67 O
ANISOU 2133 OE2 GLU A 337 30570 24181 12376 -1687 1147 -964 O
ATOM 2134 N ASP A 338 12.913 5.196 5.294 1.00142.81 N
ANISOU 2134 N ASP A 338 22990 20004 11268 -1104 1894 -1587 N
ATOM 2135 CA ASP A 338 13.428 4.308 6.337 1.00135.12 C
ANISOU 2135 CA ASP A 338 21204 19090 11045 -1014 2088 -1903 C
ATOM 2136 C ASP A 338 12.322 4.037 7.359 1.00127.46 C
ANISOU 2136 C ASP A 338 19718 18149 10562 -654 1461 -1760 C
ATOM 2137 O ASP A 338 12.365 4.464 8.514 1.00126.55 O
ANISOU 2137 O ASP A 338 19159 17960 10965 -491 1423 -1622 O
ATOM 2138 CB ASP A 338 14.663 4.918 6.988 1.00136.10 C
ANISOU 2138 CB ASP A 338 21070 19105 11536 -1139 2679 -1954 C
ATOM 2139 CG ASP A 338 15.348 3.968 7.955 1.00128.04 C
ANISOU 2139 CG ASP A 338 19280 18132 11238 -1052 2889 -2318 C
ATOM 2140 OD1 ASP A 338 14.949 2.787 8.022 1.00123.49 O
ANISOU 2140 OD1 ASP A 338 18435 17651 10835 -935 2652 -2541 O
ATOM 2141 OD2 ASP A 338 16.290 4.406 8.649 1.00126.89 O
ANISOU 2141 OD2 ASP A 338 18813 17911 11488 -1097 3272 -2387 O
ATOM 2142 N ARG A 339 11.304 3.305 6.897 1.00131.13 N
ANISOU 2142 N ARG A 339 20258 18725 10841 -554 979 -1823 N
ATOM 2143 CA ARG A 339 10.179 2.965 7.760 1.00128.86 C
ANISOU 2143 CA ARG A 339 19497 18473 10993 -261 413 -1745 C
ATOM 2144 C ARG A 339 10.556 1.964 8.845 1.00124.33 C
ANISOU 2144 C ARG A 339 18230 17908 11100 -190 578 -2010 C
ATOM 2145 O ARG A 339 9.849 1.874 9.854 1.00119.87 O
ANISOU 2145 O ARG A 339 17233 17326 10986 20 253 -1913 O
ATOM 2146 CB ARG A 339 9.024 2.407 6.925 1.00130.46 C
ANISOU 2146 CB ARG A 339 19943 18794 10832 -204 -127 -1805 C
ATOM 2147 CG ARG A 339 8.434 3.387 5.923 1.00138.11 C
ANISOU 2147 CG ARG A 339 21611 19736 11129 -197 -469 -1507 C
ATOM 2148 CD ARG A 339 7.300 2.749 5.134 1.00140.34 C
ANISOU 2148 CD ARG A 339 22073 20157 11093 -123 -1055 -1625 C
ATOM 2149 NE ARG A 339 6.719 3.668 4.162 1.00149.00 N
ANISOU 2149 NE ARG A 339 23877 21213 11524 -79 -1465 -1338 N
ATOM 2150 CZ ARG A 339 5.753 3.349 3.312 1.00152.72 C
ANISOU 2150 CZ ARG A 339 24640 21793 11594 -7 -2039 -1401 C
ATOM 2151 NH1 ARG A 339 5.232 2.133 3.282 1.00155.58 N
ANISOU 2151 NH1 ARG A 339 24637 22319 12156 2 -2243 -1760 N
ATOM 2152 NH2 ARG A 339 5.297 4.273 2.471 1.00151.30 N
ANISOU 2152 NH2 ARG A 339 24995 21540 10952 53 -2383 -1087 N
ATOM 2153 N GLU A 340 11.644 1.212 8.661 1.00113.31 N
ANISOU 2153 N GLU A 340 16738 16523 9789 -359 1073 -2351 N
ATOM 2154 CA GLU A 340 11.997 0.167 9.617 1.00106.84 C
ANISOU 2154 CA GLU A 340 15324 15680 9590 -266 1172 -2611 C
ATOM 2155 C GLU A 340 12.333 0.754 10.984 1.00100.16 C
ANISOU 2155 C GLU A 340 14053 14732 9273 -116 1228 -2433 C
ATOM 2156 O GLU A 340 11.769 0.344 12.005 1.00 98.27 O
ANISOU 2156 O GLU A 340 13412 14461 9466 67 950 -2389 O
ATOM 2157 CB GLU A 340 13.170 -0.654 9.079 1.00107.44 C
ANISOU 2157 CB GLU A 340 15396 15765 9663 -456 1691 -3034 C
ATOM 2158 CG GLU A 340 12.915 -1.292 7.721 1.00107.36 C
ANISOU 2158 CG GLU A 340 15818 15860 9114 -633 1688 -3262 C
ATOM 2159 CD GLU A 340 11.877 -2.396 7.778 1.00104.97 C
ANISOU 2159 CD GLU A 340 15340 15607 8937 -514 1238 -3391 C
ATOM 2160 OE1 GLU A 340 11.726 -3.018 8.851 1.00103.06 O
ANISOU 2160 OE1 GLU A 340 14596 15289 9271 -345 1112 -3438 O
ATOM 2161 OE2 GLU A 340 11.210 -2.640 6.749 1.00103.45 O
ANISOU 2161 OE2 GLU A 340 15535 15519 8253 -604 1011 -3453 O
ATOM 2162 N THR A 341 13.250 1.725 11.021 1.00104.32 N
ANISOU 2162 N THR A 341 14684 15199 9756 -217 1605 -2342 N
ATOM 2163 CA THR A 341 13.628 2.336 12.292 1.00101.40 C
ANISOU 2163 CA THR A 341 13925 14738 9865 -91 1665 -2199 C
ATOM 2164 C THR A 341 12.472 3.129 12.889 1.00 97.98 C
ANISOU 2164 C THR A 341 13477 14278 9473 93 1203 -1817 C
ATOM 2165 O THR A 341 12.253 3.103 14.108 1.00 92.33 O
ANISOU 2165 O THR A 341 12346 13518 9217 259 1052 -1746 O
ATOM 2166 CB THR A 341 14.853 3.231 12.099 1.00 98.07 C
ANISOU 2166 CB THR A 341 13629 14258 9375 -277 2191 -2226 C
ATOM 2167 OG1 THR A 341 15.922 2.464 11.531 1.00 99.00 O
ANISOU 2167 OG1 THR A 341 13707 14406 9501 -453 2646 -2645 O
ATOM 2168 CG2 THR A 341 15.309 3.811 13.430 1.00 95.05 C
ANISOU 2168 CG2 THR A 341 12815 13791 9508 -152 2248 -2131 C
ATOM 2169 N VAL A 342 11.719 3.837 12.043 1.00 98.87 N
ANISOU 2169 N VAL A 342 14053 14405 9106 71 964 -1584 N
ATOM 2170 CA VAL A 342 10.577 4.610 12.522 1.00 96.37 C
ANISOU 2170 CA VAL A 342 13713 14053 8852 269 497 -1260 C
ATOM 2171 C VAL A 342 9.541 3.690 13.156 1.00 94.89 C
ANISOU 2171 C VAL A 342 13128 13929 8996 437 90 -1349 C
ATOM 2172 O VAL A 342 9.017 3.970 14.241 1.00 89.54 O
ANISOU 2172 O VAL A 342 12105 13208 8707 593 -100 -1223 O
ATOM 2173 CB VAL A 342 9.970 5.436 11.372 1.00 93.85 C
ANISOU 2173 CB VAL A 342 14007 13717 7933 241 258 -1024 C
ATOM 2174 CG1 VAL A 342 8.704 6.141 11.833 1.00 91.70 C
ANISOU 2174 CG1 VAL A 342 13655 13402 7785 489 -288 -745 C
ATOM 2175 CG2 VAL A 342 10.985 6.439 10.850 1.00 93.79 C
ANISOU 2175 CG2 VAL A 342 14434 13599 7603 40 710 -903 C
ATOM 2176 N TYR A 343 9.239 2.571 12.493 1.00100.89 N
ANISOU 2176 N TYR A 343 13941 14783 9607 380 -15 -1592 N
ATOM 2177 CA TYR A 343 8.253 1.643 13.036 1.00 99.84 C
ANISOU 2177 CA TYR A 343 13455 14694 9787 493 -359 -1709 C
ATOM 2178 C TYR A 343 8.767 0.954 14.293 1.00 98.04 C
ANISOU 2178 C TYR A 343 12753 14391 10106 532 -154 -1836 C
ATOM 2179 O TYR A 343 7.991 0.690 15.217 1.00 95.31 O
ANISOU 2179 O TYR A 343 12085 14019 10108 639 -385 -1802 O
ATOM 2180 CB TYR A 343 7.853 0.615 11.980 1.00105.24 C
ANISOU 2180 CB TYR A 343 14331 15481 10172 399 -502 -1963 C
ATOM 2181 CG TYR A 343 6.933 1.183 10.926 1.00113.93 C
ANISOU 2181 CG TYR A 343 15846 16661 10781 424 -911 -1831 C
ATOM 2182 CD1 TYR A 343 6.225 2.354 11.159 1.00115.00 C
ANISOU 2182 CD1 TYR A 343 16037 16755 10903 584 -1233 -1518 C
ATOM 2183 CD2 TYR A 343 6.773 0.553 9.699 1.00123.66 C
ANISOU 2183 CD2 TYR A 343 17426 17997 11563 304 -1002 -2031 C
ATOM 2184 CE1 TYR A 343 5.382 2.883 10.202 1.00122.27 C
ANISOU 2184 CE1 TYR A 343 17352 17721 11385 651 -1677 -1394 C
ATOM 2185 CE2 TYR A 343 5.931 1.075 8.734 1.00126.72 C
ANISOU 2185 CE2 TYR A 343 18229 18450 11468 348 -1440 -1908 C
ATOM 2186 CZ TYR A 343 5.239 2.241 8.991 1.00128.24 C
ANISOU 2186 CZ TYR A 343 18473 18586 11667 536 -1797 -1582 C
ATOM 2187 OH TYR A 343 4.399 2.768 8.036 1.00133.80 O
ANISOU 2187 OH TYR A 343 19605 19329 11903 623 -2300 -1457 O
ATOM 2188 N ALA A 344 10.068 0.655 14.349 1.00101.57 N
ANISOU 2188 N ALA A 344 13161 14793 10637 446 275 -1998 N
ATOM 2189 CA ALA A 344 10.636 0.087 15.568 1.00 93.23 C
ANISOU 2189 CA ALA A 344 11696 13641 10086 520 418 -2098 C
ATOM 2190 C ALA A 344 10.471 1.045 16.741 1.00 93.03 C
ANISOU 2190 C ALA A 344 11462 13554 10331 638 344 -1833 C
ATOM 2191 O ALA A 344 10.034 0.648 17.829 1.00 89.58 O
ANISOU 2191 O ALA A 344 10734 13059 10243 734 198 -1811 O
ATOM 2192 CB ALA A 344 12.111 -0.255 15.350 1.00 90.83 C
ANISOU 2192 CB ALA A 344 11368 13299 9843 433 862 -2346 C
ATOM 2193 N TRP A 345 10.795 2.324 16.528 1.00 80.66 N
ANISOU 2193 N TRP A 345 10076 11984 8587 613 460 -1635 N
ATOM 2194 CA TRP A 345 10.629 3.313 17.589 1.00 77.19 C
ANISOU 2194 CA TRP A 345 9456 11481 8391 717 398 -1399 C
ATOM 2195 C TRP A 345 9.164 3.464 17.984 1.00 71.46 C
ANISOU 2195 C TRP A 345 8636 10771 7744 835 -21 -1244 C
ATOM 2196 O TRP A 345 8.841 3.546 19.175 1.00 68.23 O
ANISOU 2196 O TRP A 345 7932 10313 7679 922 -97 -1181 O
ATOM 2197 CB TRP A 345 11.210 4.658 17.155 1.00 77.07 C
ANISOU 2197 CB TRP A 345 9704 11429 8149 646 610 -1226 C
ATOM 2198 CG TRP A 345 12.642 4.845 17.552 1.00 81.34 C
ANISOU 2198 CG TRP A 345 10105 11921 8882 567 1038 -1357 C
ATOM 2199 CD1 TRP A 345 13.734 4.804 16.734 1.00 82.59 C
ANISOU 2199 CD1 TRP A 345 10434 12088 8859 393 1433 -1544 C
ATOM 2200 CD2 TRP A 345 13.139 5.097 18.872 1.00 83.36 C
ANISOU 2200 CD2 TRP A 345 9999 12113 9561 652 1112 -1352 C
ATOM 2201 NE1 TRP A 345 14.879 5.019 17.463 1.00 84.50 N
ANISOU 2201 NE1 TRP A 345 10394 12280 9434 374 1737 -1677 N
ATOM 2202 CE2 TRP A 345 14.541 5.200 18.779 1.00 85.31 C
ANISOU 2202 CE2 TRP A 345 10180 12338 9894 542 1520 -1552 C
ATOM 2203 CE3 TRP A 345 12.534 5.245 20.124 1.00 80.68 C
ANISOU 2203 CE3 TRP A 345 9390 11736 9528 797 880 -1221 C
ATOM 2204 CZ2 TRP A 345 15.347 5.445 19.889 1.00 85.76 C
ANISOU 2204 CZ2 TRP A 345 9900 12344 10341 598 1645 -1625 C
ATOM 2205 CZ3 TRP A 345 13.336 5.489 21.225 1.00 79.65 C
ANISOU 2205 CZ3 TRP A 345 8983 11550 9731 838 1023 -1269 C
ATOM 2206 CH2 TRP A 345 14.727 5.586 21.100 1.00 85.00 C
ANISOU 2206 CH2 TRP A 345 9590 12213 10494 752 1374 -1468 C
ATOM 2207 N PHE A 346 8.263 3.500 16.999 1.00 77.54 N
ANISOU 2207 N PHE A 346 9648 11612 8202 835 -299 -1209 N
ATOM 2208 CA PHE A 346 6.846 3.672 17.303 1.00 73.71 C
ANISOU 2208 CA PHE A 346 9023 11150 7835 955 -715 -1119 C
ATOM 2209 C PHE A 346 6.295 2.491 18.092 1.00 74.40 C
ANISOU 2209 C PHE A 346 8758 11243 8268 956 -801 -1306 C
ATOM 2210 O PHE A 346 5.550 2.679 19.061 1.00 74.61 O
ANISOU 2210 O PHE A 346 8510 11239 8601 1026 -937 -1250 O
ATOM 2211 CB PHE A 346 6.050 3.882 16.015 1.00 73.34 C
ANISOU 2211 CB PHE A 346 9309 11178 7377 971 -1045 -1085 C
ATOM 2212 CG PHE A 346 5.834 5.327 15.666 1.00 71.93 C
ANISOU 2212 CG PHE A 346 9406 10937 6986 1063 -1188 -800 C
ATOM 2213 CD1 PHE A 346 4.753 6.022 16.182 1.00 71.34 C
ANISOU 2213 CD1 PHE A 346 9145 10829 7133 1240 -1540 -668 C
ATOM 2214 CD2 PHE A 346 6.711 5.993 14.826 1.00 75.24 C
ANISOU 2214 CD2 PHE A 346 10281 11308 6999 964 -953 -680 C
ATOM 2215 CE1 PHE A 346 4.550 7.353 15.866 1.00 73.22 C
ANISOU 2215 CE1 PHE A 346 9652 10966 7201 1353 -1699 -404 C
ATOM 2216 CE2 PHE A 346 6.514 7.324 14.506 1.00 76.01 C
ANISOU 2216 CE2 PHE A 346 10695 11297 6887 1043 -1083 -395 C
ATOM 2217 CZ PHE A 346 5.431 8.004 15.027 1.00 74.03 C
ANISOU 2217 CZ PHE A 346 10261 10994 6872 1256 -1480 -248 C
ATOM 2218 N THR A 347 6.653 1.263 17.705 1.00 71.14 N
ANISOU 2218 N THR A 347 8368 10850 7814 861 -696 -1542 N
ATOM 2219 CA THR A 347 6.136 0.107 18.428 1.00 70.00 C
ANISOU 2219 CA THR A 347 7951 10664 7981 840 -759 -1711 C
ATOM 2220 C THR A 347 6.758 -0.006 19.816 1.00 66.11 C
ANISOU 2220 C THR A 347 7230 10045 7843 870 -547 -1668 C
ATOM 2221 O THR A 347 6.076 -0.413 20.763 1.00 66.39 O
ANISOU 2221 O THR A 347 7052 10021 8154 869 -630 -1681 O
ATOM 2222 CB THR A 347 6.344 -1.179 17.618 1.00 70.60 C
ANISOU 2222 CB THR A 347 8137 10760 7928 737 -713 -1984 C
ATOM 2223 OG1 THR A 347 5.655 -2.261 18.256 1.00 74.05 O
ANISOU 2223 OG1 THR A 347 8352 11130 8655 698 -805 -2136 O
ATOM 2224 CG2 THR A 347 7.818 -1.535 17.493 1.00 74.17 C
ANISOU 2224 CG2 THR A 347 8674 11151 8358 699 -349 -2091 C
ATOM 2225 N PHE A 348 8.030 0.378 19.971 1.00 67.11 N
ANISOU 2225 N PHE A 348 7406 10128 7964 885 -275 -1629 N
ATOM 2226 CA PHE A 348 8.623 0.403 21.303 1.00 63.77 C
ANISOU 2226 CA PHE A 348 6780 9594 7855 939 -138 -1581 C
ATOM 2227 C PHE A 348 7.931 1.430 22.191 1.00 62.28 C
ANISOU 2227 C PHE A 348 6460 9401 7801 997 -248 -1368 C
ATOM 2228 O PHE A 348 7.661 1.164 23.370 1.00 60.99 O
ANISOU 2228 O PHE A 348 6124 9158 7892 1011 -263 -1349 O
ATOM 2229 CB PHE A 348 10.121 0.691 21.203 1.00 63.68 C
ANISOU 2229 CB PHE A 348 6805 9556 7834 947 151 -1631 C
ATOM 2230 CG PHE A 348 10.821 0.727 22.529 1.00 61.04 C
ANISOU 2230 CG PHE A 348 6269 9115 7810 1024 242 -1609 C
ATOM 2231 CD1 PHE A 348 11.022 -0.436 23.253 1.00 60.33 C
ANISOU 2231 CD1 PHE A 348 6079 8902 7942 1065 210 -1734 C
ATOM 2232 CD2 PHE A 348 11.287 1.923 23.049 1.00 61.94 C
ANISOU 2232 CD2 PHE A 348 6323 9232 7978 1056 341 -1465 C
ATOM 2233 CE1 PHE A 348 11.668 -0.407 24.474 1.00 61.96 C
ANISOU 2233 CE1 PHE A 348 6149 9000 8391 1154 237 -1706 C
ATOM 2234 CE2 PHE A 348 11.936 1.959 24.268 1.00 62.51 C
ANISOU 2234 CE2 PHE A 348 6218 9218 8313 1129 388 -1466 C
ATOM 2235 CZ PHE A 348 12.126 0.792 24.982 1.00 60.63 C
ANISOU 2235 CZ PHE A 348 5902 8868 8266 1186 318 -1582 C
ATOM 2236 N SER A 349 7.626 2.608 21.640 1.00 61.75 N
ANISOU 2236 N SER A 349 6505 9399 7558 1027 -323 -1212 N
ATOM 2237 CA SER A 349 6.919 3.625 22.412 1.00 60.37 C
ANISOU 2237 CA SER A 349 6196 9207 7536 1096 -436 -1039 C
ATOM 2238 C SER A 349 5.519 3.155 22.787 1.00 58.58 C
ANISOU 2238 C SER A 349 5785 8998 7476 1094 -675 -1103 C
ATOM 2239 O SER A 349 5.049 3.409 23.902 1.00 56.83 O
ANISOU 2239 O SER A 349 5358 8729 7507 1105 -672 -1063 O
ATOM 2240 CB SER A 349 6.854 4.931 21.622 1.00 60.53 C
ANISOU 2240 CB SER A 349 6422 9251 7326 1145 -498 -862 C
ATOM 2241 OG SER A 349 6.075 4.778 20.448 1.00 61.64 O
ANISOU 2241 OG SER A 349 6745 9466 7208 1153 -754 -888 O
ATOM 2242 N HIS A 350 4.834 2.476 21.862 1.00 57.67 N
ANISOU 2242 N HIS A 350 5734 8954 7224 1058 -866 -1233 N
ATOM 2243 CA HIS A 350 3.525 1.916 22.176 1.00 58.27 C
ANISOU 2243 CA HIS A 350 5594 9049 7497 1021 -1066 -1362 C
ATOM 2244 C HIS A 350 3.623 0.893 23.299 1.00 58.53 C
ANISOU 2244 C HIS A 350 5480 8975 7782 918 -888 -1465 C
ATOM 2245 O HIS A 350 2.795 0.884 24.217 1.00 57.96 O
ANISOU 2245 O HIS A 350 5200 8866 7958 872 -902 -1493 O
ATOM 2246 CB HIS A 350 2.910 1.280 20.930 1.00 59.46 C
ANISOU 2246 CB HIS A 350 5847 9298 7445 988 -1302 -1525 C
ATOM 2247 CG HIS A 350 2.589 2.261 19.847 1.00 60.23 C
ANISOU 2247 CG HIS A 350 6138 9482 7264 1098 -1561 -1415 C
ATOM 2248 ND1 HIS A 350 2.274 1.874 18.562 1.00 62.33 N
ANISOU 2248 ND1 HIS A 350 6609 9845 7229 1083 -1787 -1526 N
ATOM 2249 CD2 HIS A 350 2.533 3.614 19.857 1.00 60.95 C
ANISOU 2249 CD2 HIS A 350 6292 9553 7312 1228 -1648 -1197 C
ATOM 2250 CE1 HIS A 350 2.038 2.946 17.827 1.00 64.70 C
ANISOU 2250 CE1 HIS A 350 7123 10176 7285 1206 -2021 -1362 C
ATOM 2251 NE2 HIS A 350 2.188 4.015 18.589 1.00 62.94 N
ANISOU 2251 NE2 HIS A 350 6817 9870 7226 1299 -1938 -1157 N
ATOM 2252 N TRP A 351 4.636 0.026 23.246 1.00 59.01 N
ANISOU 2252 N TRP A 351 5670 8967 7786 878 -712 -1532 N
ATOM 2253 CA TRP A 351 4.814 -0.974 24.292 1.00 58.09 C
ANISOU 2253 CA TRP A 351 5497 8699 7876 804 -576 -1602 C
ATOM 2254 C TRP A 351 5.146 -0.336 25.636 1.00 58.19 C
ANISOU 2254 C TRP A 351 5429 8631 8049 841 -453 -1447 C
ATOM 2255 O TRP A 351 4.757 -0.869 26.681 1.00 60.09 O
ANISOU 2255 O TRP A 351 5618 8756 8457 757 -396 -1468 O
ATOM 2256 CB TRP A 351 5.908 -1.963 23.887 1.00 58.48 C
ANISOU 2256 CB TRP A 351 5700 8668 7851 805 -455 -1717 C
ATOM 2257 CG TRP A 351 6.232 -2.974 24.943 1.00 57.27 C
ANISOU 2257 CG TRP A 351 5558 8311 7892 771 -356 -1760 C
ATOM 2258 CD1 TRP A 351 5.583 -4.151 25.180 1.00 55.36 C
ANISOU 2258 CD1 TRP A 351 5338 7941 7756 649 -376 -1891 C
ATOM 2259 CD2 TRP A 351 7.291 -2.899 25.905 1.00 54.55 C
ANISOU 2259 CD2 TRP A 351 5239 7840 7647 862 -243 -1672 C
ATOM 2260 NE1 TRP A 351 6.170 -4.812 26.232 1.00 52.49 N
ANISOU 2260 NE1 TRP A 351 5064 7355 7523 663 -283 -1856 N
ATOM 2261 CE2 TRP A 351 7.221 -4.065 26.694 1.00 51.07 C
ANISOU 2261 CE2 TRP A 351 4881 7183 7342 809 -229 -1727 C
ATOM 2262 CE3 TRP A 351 8.290 -1.960 26.177 1.00 54.68 C
ANISOU 2262 CE3 TRP A 351 5226 7896 7655 978 -164 -1566 C
ATOM 2263 CZ2 TRP A 351 8.112 -4.315 27.735 1.00 50.70 C
ANISOU 2263 CZ2 TRP A 351 4910 6958 7395 901 -191 -1662 C
ATOM 2264 CZ3 TRP A 351 9.173 -2.211 27.211 1.00 54.42 C
ANISOU 2264 CZ3 TRP A 351 5207 7713 7756 1059 -117 -1539 C
ATOM 2265 CH2 TRP A 351 9.078 -3.379 27.977 1.00 51.58 C
ANISOU 2265 CH2 TRP A 351 4953 7139 7505 1036 -157 -1579 C
ATOM 2266 N LEU A 352 5.855 0.797 25.629 1.00 59.62 N
ANISOU 2266 N LEU A 352 5629 8860 8163 944 -396 -1303 N
ATOM 2267 CA LEU A 352 6.299 1.400 26.884 1.00 59.43 C
ANISOU 2267 CA LEU A 352 5539 8765 8278 978 -281 -1184 C
ATOM 2268 C LEU A 352 5.137 1.871 27.751 1.00 59.11 C
ANISOU 2268 C LEU A 352 5339 8722 8397 925 -320 -1145 C
ATOM 2269 O LEU A 352 5.251 1.873 28.981 1.00 60.99 O
ANISOU 2269 O LEU A 352 5552 8870 8752 888 -216 -1105 O
ATOM 2270 CB LEU A 352 7.250 2.563 26.605 1.00 60.10 C
ANISOU 2270 CB LEU A 352 5661 8900 8275 1072 -197 -1071 C
ATOM 2271 CG LEU A 352 8.733 2.195 26.580 1.00 60.88 C
ANISOU 2271 CG LEU A 352 5827 8948 8357 1113 -49 -1134 C
ATOM 2272 CD1 LEU A 352 9.586 3.441 26.447 1.00 58.18 C
ANISOU 2272 CD1 LEU A 352 5485 8647 7975 1160 79 -1048 C
ATOM 2273 CD2 LEU A 352 9.109 1.419 27.832 1.00 58.18 C
ANISOU 2273 CD2 LEU A 352 5454 8468 8185 1125 -29 -1170 C
ATOM 2274 N VAL A 353 4.021 2.283 27.146 1.00 53.88 N
ANISOU 2274 N VAL A 353 4569 8155 7747 922 -476 -1178 N
ATOM 2275 CA VAL A 353 2.880 2.742 27.938 1.00 55.33 C
ANISOU 2275 CA VAL A 353 4541 8339 8141 872 -496 -1203 C
ATOM 2276 C VAL A 353 2.319 1.597 28.776 1.00 57.39 C
ANISOU 2276 C VAL A 353 4763 8503 8540 688 -390 -1339 C
ATOM 2277 O VAL A 353 2.144 1.713 29.999 1.00 59.30 O
ANISOU 2277 O VAL A 353 4963 8665 8904 602 -235 -1321 O
ATOM 2278 CB VAL A 353 1.806 3.348 27.018 1.00 54.11 C
ANISOU 2278 CB VAL A 353 4252 8297 8009 942 -745 -1255 C
ATOM 2279 CG1 VAL A 353 0.521 3.593 27.790 1.00 56.28 C
ANISOU 2279 CG1 VAL A 353 4271 8553 8558 863 -749 -1361 C
ATOM 2280 CG2 VAL A 353 2.314 4.638 26.388 1.00 50.47 C
ANISOU 2280 CG2 VAL A 353 3897 7873 7405 1112 -827 -1074 C
ATOM 2281 N TYR A 354 2.050 0.463 28.130 1.00 56.43 N
ANISOU 2281 N TYR A 354 4693 8370 8379 605 -450 -1482 N
ATOM 2282 CA TYR A 354 1.583 -0.706 28.861 1.00 58.17 C
ANISOU 2282 CA TYR A 354 4938 8451 8711 403 -321 -1607 C
ATOM 2283 C TYR A 354 2.657 -1.231 29.805 1.00 58.46 C
ANISOU 2283 C TYR A 354 5215 8309 8687 395 -158 -1493 C
ATOM 2284 O TYR A 354 2.337 -1.784 30.864 1.00 57.96 O
ANISOU 2284 O TYR A 354 5230 8095 8698 235 -11 -1510 O
ATOM 2285 CB TYR A 354 1.140 -1.786 27.875 1.00 60.51 C
ANISOU 2285 CB TYR A 354 5250 8760 8981 320 -428 -1799 C
ATOM 2286 CG TYR A 354 0.208 -1.278 26.793 1.00 58.85 C
ANISOU 2286 CG TYR A 354 4835 8737 8787 374 -675 -1919 C
ATOM 2287 CD1 TYR A 354 -1.166 -1.259 26.986 1.00 62.08 C
ANISOU 2287 CD1 TYR A 354 4961 9193 9434 253 -729 -2113 C
ATOM 2288 CD2 TYR A 354 0.703 -0.820 25.579 1.00 59.77 C
ANISOU 2288 CD2 TYR A 354 5055 8978 8679 541 -862 -1855 C
ATOM 2289 CE1 TYR A 354 -2.019 -0.797 26.000 1.00 63.72 C
ANISOU 2289 CE1 TYR A 354 4968 9564 9676 341 -1029 -2243 C
ATOM 2290 CE2 TYR A 354 -0.144 -0.353 24.587 1.00 59.18 C
ANISOU 2290 CE2 TYR A 354 4858 9054 8573 612 -1148 -1945 C
ATOM 2291 CZ TYR A 354 -1.505 -0.344 24.805 1.00 61.97 C
ANISOU 2291 CZ TYR A 354 4906 9452 9188 533 -1264 -2139 C
ATOM 2292 OH TYR A 354 -2.359 0.116 23.828 1.00 57.85 O
ANISOU 2292 OH TYR A 354 4245 9074 8660 641 -1618 -2251 O
ATOM 2293 N ALA A 355 3.933 -1.050 29.452 1.00 62.92 N
ANISOU 2293 N ALA A 355 5909 8879 9119 563 -186 -1390 N
ATOM 2294 CA ALA A 355 5.010 -1.449 30.351 1.00 62.82 C
ANISOU 2294 CA ALA A 355 6085 8703 9081 607 -101 -1303 C
ATOM 2295 C ALA A 355 4.981 -0.637 31.640 1.00 61.84 C
ANISOU 2295 C ALA A 355 5941 8552 9004 588 -8 -1185 C
ATOM 2296 O ALA A 355 5.193 -1.181 32.727 1.00 61.84 O
ANISOU 2296 O ALA A 355 6122 8380 8996 521 64 -1143 O
ATOM 2297 CB ALA A 355 6.360 -1.305 29.650 1.00 62.06 C
ANISOU 2297 CB ALA A 355 6045 8644 8891 790 -140 -1282 C
ATOM 2298 N ASN A 356 4.731 0.670 31.538 1.00 57.18 N
ANISOU 2298 N ASN A 356 5169 8112 8446 648 -16 -1129 N
ATOM 2299 CA ASN A 356 4.571 1.493 32.735 1.00 56.53 C
ANISOU 2299 CA ASN A 356 5043 8014 8424 611 89 -1056 C
ATOM 2300 C ASN A 356 3.350 1.059 33.535 1.00 56.06 C
ANISOU 2300 C ASN A 356 4958 7883 8461 386 214 -1148 C
ATOM 2301 O ASN A 356 3.382 1.022 34.776 1.00 56.88 O
ANISOU 2301 O ASN A 356 5192 7878 8543 281 351 -1108 O
ATOM 2302 CB ASN A 356 4.456 2.966 32.347 1.00 52.61 C
ANISOU 2302 CB ASN A 356 4351 7663 7973 723 54 -1001 C
ATOM 2303 CG ASN A 356 4.072 3.850 33.518 1.00 51.53 C
ANISOU 2303 CG ASN A 356 4129 7516 7936 667 175 -974 C
ATOM 2304 OD1 ASN A 356 4.928 4.275 34.296 1.00 49.83 O
ANISOU 2304 OD1 ASN A 356 4009 7256 7668 709 235 -889 O
ATOM 2305 ND2 ASN A 356 2.780 4.136 33.646 1.00 50.11 N
ANISOU 2305 ND2 ASN A 356 3825 7348 7866 554 205 -1040 N
ATOM 2306 N SER A 357 2.255 0.746 32.835 1.00 55.19 N
ANISOU 2306 N SER A 357 4681 7834 8454 293 175 -1294 N
ATOM 2307 CA SER A 357 1.065 0.236 33.510 1.00 55.16 C
ANISOU 2307 CA SER A 357 4616 7759 8582 37 337 -1445 C
ATOM 2308 C SER A 357 1.383 -1.022 34.312 1.00 55.31 C
ANISOU 2308 C SER A 357 4976 7546 8494 -131 476 -1420 C
ATOM 2309 O SER A 357 0.864 -1.212 35.419 1.00 57.22 O
ANISOU 2309 O SER A 357 5320 7671 8752 -351 694 -1450 O
ATOM 2310 CB SER A 357 -0.035 -0.043 32.487 1.00 57.48 C
ANISOU 2310 CB SER A 357 4659 8158 9024 -20 226 -1650 C
ATOM 2311 OG SER A 357 -1.098 -0.776 33.067 1.00 58.14 O
ANISOU 2311 OG SER A 357 4685 8151 9256 -310 417 -1845 O
ATOM 2312 N ALA A 358 2.233 -1.893 33.767 1.00 56.12 N
ANISOU 2312 N ALA A 358 5284 7558 8482 -32 360 -1372 N
ATOM 2313 CA ALA A 358 2.632 -3.102 34.482 1.00 56.03 C
ANISOU 2313 CA ALA A 358 5643 7277 8370 -140 436 -1327 C
ATOM 2314 C ALA A 358 3.643 -2.818 35.587 1.00 56.02 C
ANISOU 2314 C ALA A 358 5896 7162 8227 -40 436 -1142 C
ATOM 2315 O ALA A 358 3.660 -3.521 36.603 1.00 57.37 O
ANISOU 2315 O ALA A 358 6406 7098 8294 -181 533 -1082 O
ATOM 2316 CB ALA A 358 3.206 -4.128 33.503 1.00 52.85 C
ANISOU 2316 CB ALA A 358 5349 6797 7936 -41 295 -1374 C
ATOM 2317 N ALA A 359 4.491 -1.805 35.406 1.00 57.75 N
ANISOU 2317 N ALA A 359 5983 7532 8428 192 321 -1057 N
ATOM 2318 CA ALA A 359 5.576 -1.537 36.340 1.00 58.11 C
ANISOU 2318 CA ALA A 359 6227 7491 8360 319 265 -922 C
ATOM 2319 C ALA A 359 5.123 -0.782 37.581 1.00 56.41 C
ANISOU 2319 C ALA A 359 6054 7282 8099 180 420 -876 C
ATOM 2320 O ALA A 359 5.790 -0.875 38.617 1.00 57.44 O
ANISOU 2320 O ALA A 359 6464 7278 8084 206 386 -776 O
ATOM 2321 CB ALA A 359 6.686 -0.750 35.640 1.00 56.58 C
ANISOU 2321 CB ALA A 359 5851 7454 8194 586 120 -897 C
ATOM 2322 N ASN A 360 4.025 -0.029 37.499 1.00 56.47 N
ANISOU 2322 N ASN A 360 5791 7435 8230 46 570 -966 N
ATOM 2323 CA ASN A 360 3.559 0.699 38.680 1.00 56.91 C
ANISOU 2323 CA ASN A 360 5866 7495 8262 -104 760 -966 C
ATOM 2324 C ASN A 360 3.293 -0.207 39.881 1.00 53.89 C
ANISOU 2324 C ASN A 360 5900 6873 7701 -355 928 -940 C
ATOM 2325 O ASN A 360 3.762 0.121 40.987 1.00 52.04 O
ANISOU 2325 O ASN A 360 5908 6572 7294 -372 960 -850 O
ATOM 2326 CB ASN A 360 2.324 1.534 38.323 1.00 55.24 C
ANISOU 2326 CB ASN A 360 5258 7453 8276 -199 889 -1121 C
ATOM 2327 CG ASN A 360 2.675 2.795 37.562 1.00 51.93 C
ANISOU 2327 CG ASN A 360 4536 7227 7968 48 741 -1091 C
ATOM 2328 OD1 ASN A 360 3.708 3.417 37.812 1.00 48.16 O
ANISOU 2328 OD1 ASN A 360 4124 6769 7406 208 664 -976 O
ATOM 2329 ND2 ASN A 360 1.815 3.179 36.628 1.00 55.04 N
ANISOU 2329 ND2 ASN A 360 4612 7748 8552 77 688 -1202 N
ATOM 2330 N PRO A 361 2.566 -1.327 39.760 1.00 56.19 N
ANISOU 2330 N PRO A 361 6331 7017 8004 -573 1046 -1015 N
ATOM 2331 CA PRO A 361 2.391 -2.200 40.936 1.00 55.81 C
ANISOU 2331 CA PRO A 361 6779 6690 7736 -833 1227 -958 C
ATOM 2332 C PRO A 361 3.693 -2.762 41.484 1.00 53.92 C
ANISOU 2332 C PRO A 361 7005 6239 7242 -647 988 -749 C
ATOM 2333 O PRO A 361 3.811 -2.954 42.701 1.00 52.43 O
ANISOU 2333 O PRO A 361 7255 5865 6799 -783 1070 -647 O
ATOM 2334 CB PRO A 361 1.472 -3.313 40.413 1.00 60.70 C
ANISOU 2334 CB PRO A 361 7413 7187 8465 -1072 1370 -1095 C
ATOM 2335 CG PRO A 361 0.769 -2.709 39.251 1.00 61.59 C
ANISOU 2335 CG PRO A 361 6950 7575 8877 -1009 1336 -1284 C
ATOM 2336 CD PRO A 361 1.776 -1.809 38.612 1.00 58.46 C
ANISOU 2336 CD PRO A 361 6350 7371 8492 -630 1045 -1174 C
ATOM 2337 N ILE A 362 4.674 -3.041 40.623 1.00 55.43 N
ANISOU 2337 N ILE A 362 7121 6446 7494 -337 687 -702 N
ATOM 2338 CA ILE A 362 5.969 -3.523 41.100 1.00 54.72 C
ANISOU 2338 CA ILE A 362 7393 6164 7234 -107 410 -552 C
ATOM 2339 C ILE A 362 6.660 -2.449 41.931 1.00 58.02 C
ANISOU 2339 C ILE A 362 7808 6693 7544 21 320 -482 C
ATOM 2340 O ILE A 362 7.275 -2.738 42.967 1.00 60.18 O
ANISOU 2340 O ILE A 362 8508 6775 7585 61 184 -363 O
ATOM 2341 CB ILE A 362 6.839 -3.975 39.913 1.00 52.53 C
ANISOU 2341 CB ILE A 362 6941 5907 7110 188 152 -590 C
ATOM 2342 CG1 ILE A 362 6.099 -5.028 39.085 1.00 48.04 C
ANISOU 2342 CG1 ILE A 362 6377 5235 6643 40 248 -687 C
ATOM 2343 CG2 ILE A 362 8.179 -4.510 40.402 1.00 53.31 C
ANISOU 2343 CG2 ILE A 362 7358 5794 7105 455 -162 -488 C
ATOM 2344 CD1 ILE A 362 6.876 -5.524 37.885 1.00 48.61 C
ANISOU 2344 CD1 ILE A 362 6293 5324 6853 293 40 -761 C
ATOM 2345 N ILE A 363 6.570 -1.193 41.487 1.00 57.67 N
ANISOU 2345 N ILE A 363 7307 6944 7661 90 374 -560 N
ATOM 2346 CA ILE A 363 7.112 -0.081 42.262 1.00 56.18 C
ANISOU 2346 CA ILE A 363 7078 6868 7400 171 334 -530 C
ATOM 2347 C ILE A 363 6.403 0.021 43.605 1.00 54.12 C
ANISOU 2347 C ILE A 363 7137 6508 6919 -118 565 -506 C
ATOM 2348 O ILE A 363 7.037 0.249 44.643 1.00 53.39 O
ANISOU 2348 O ILE A 363 7335 6346 6606 -79 458 -431 O
ATOM 2349 CB ILE A 363 7.005 1.230 41.463 1.00 54.61 C
ANISOU 2349 CB ILE A 363 6355 6962 7434 267 389 -618 C
ATOM 2350 CG1 ILE A 363 7.775 1.120 40.146 1.00 52.89 C
ANISOU 2350 CG1 ILE A 363 5894 6829 7374 518 197 -642 C
ATOM 2351 CG2 ILE A 363 7.525 2.397 42.280 1.00 50.57 C
ANISOU 2351 CG2 ILE A 363 5797 6548 6870 324 378 -611 C
ATOM 2352 CD1 ILE A 363 7.655 2.344 39.271 1.00 48.17 C
ANISOU 2352 CD1 ILE A 363 4872 6472 6957 597 252 -699 C
ATOM 2353 N TYR A 364 5.076 -0.147 43.608 1.00 53.55 N
ANISOU 2353 N TYR A 364 7015 6430 6901 -426 890 -598 N
ATOM 2354 CA TYR A 364 4.340 -0.136 44.870 1.00 54.76 C
ANISOU 2354 CA TYR A 364 7494 6474 6840 -761 1189 -614 C
ATOM 2355 C TYR A 364 4.840 -1.229 45.805 1.00 56.57 C
ANISOU 2355 C TYR A 364 8419 6375 6702 -827 1085 -444 C
ATOM 2356 O TYR A 364 5.045 -0.990 47.001 1.00 57.88 O
ANISOU 2356 O TYR A 364 8968 6457 6568 -926 1120 -376 O
ATOM 2357 CB TYR A 364 2.842 -0.311 44.618 1.00 54.25 C
ANISOU 2357 CB TYR A 364 7225 6434 6952 -1095 1569 -795 C
ATOM 2358 CG TYR A 364 2.214 0.739 43.732 1.00 54.32 C
ANISOU 2358 CG TYR A 364 6579 6733 7329 -1020 1632 -971 C
ATOM 2359 CD1 TYR A 364 2.740 2.022 43.650 1.00 49.29 C
ANISOU 2359 CD1 TYR A 364 5653 6293 6781 -792 1510 -964 C
ATOM 2360 CD2 TYR A 364 1.087 0.444 42.978 1.00 57.77 C
ANISOU 2360 CD2 TYR A 364 6701 7223 8026 -1175 1793 -1153 C
ATOM 2361 CE1 TYR A 364 2.160 2.979 42.836 1.00 49.95 C
ANISOU 2361 CE1 TYR A 364 5202 6592 7186 -707 1537 -1100 C
ATOM 2362 CE2 TYR A 364 0.503 1.390 42.164 1.00 55.98 C
ANISOU 2362 CE2 TYR A 364 5910 7234 8126 -1071 1781 -1308 C
ATOM 2363 CZ TYR A 364 1.040 2.655 42.096 1.00 52.93 C
ANISOU 2363 CZ TYR A 364 5295 7012 7802 -830 1650 -1264 C
ATOM 2364 OH TYR A 364 0.451 3.594 41.282 1.00 56.12 O
ANISOU 2364 OH TYR A 364 5200 7607 8518 -710 1611 -1393 O
ATOM 2365 N ASN A 365 5.043 -2.437 45.275 1.00 60.46 N
ANISOU 2365 N ASN A 365 9112 6661 7198 -766 942 -374 N
ATOM 2366 CA ASN A 365 5.491 -3.550 46.107 1.00 62.40 C
ANISOU 2366 CA ASN A 365 10068 6536 7107 -806 809 -195 C
ATOM 2367 C ASN A 365 6.884 -3.300 46.670 1.00 61.99 C
ANISOU 2367 C ASN A 365 10234 6444 6875 -463 376 -62 C
ATOM 2368 O ASN A 365 7.155 -3.611 47.836 1.00 64.52 O
ANISOU 2368 O ASN A 365 11157 6536 6822 -534 295 77 O
ATOM 2369 CB ASN A 365 5.465 -4.852 45.306 1.00 61.94 C
ANISOU 2369 CB ASN A 365 10125 6254 7155 -772 723 -174 C
ATOM 2370 CG ASN A 365 5.961 -6.041 46.111 1.00 66.89 C
ANISOU 2370 CG ASN A 365 11523 6441 7453 -775 544 29 C
ATOM 2371 OD1 ASN A 365 5.193 -6.684 46.827 1.00 68.65 O
ANISOU 2371 OD1 ASN A 365 12244 6401 7440 -1145 835 82 O
ATOM 2372 ND2 ASN A 365 7.251 -6.338 45.996 1.00 68.29 N
ANISOU 2372 ND2 ASN A 365 11810 6515 7623 -362 66 129 N
ATOM 2373 N PHE A 366 7.783 -2.745 45.859 1.00 61.48 N
ANISOU 2373 N PHE A 366 9702 6593 7066 -100 94 -118 N
ATOM 2374 CA PHE A 366 9.167 -2.567 46.278 1.00 63.86 C
ANISOU 2374 CA PHE A 366 10121 6864 7281 245 -341 -55 C
ATOM 2375 C PHE A 366 9.416 -1.275 47.048 1.00 63.97 C
ANISOU 2375 C PHE A 366 10017 7090 7199 244 -327 -97 C
ATOM 2376 O PHE A 366 10.513 -1.103 47.591 1.00 68.00 O
ANISOU 2376 O PHE A 366 10664 7570 7604 493 -690 -68 O
ATOM 2377 CB PHE A 366 10.096 -2.622 45.061 1.00 67.30 C
ANISOU 2377 CB PHE A 366 10109 7411 8052 608 -613 -141 C
ATOM 2378 CG PHE A 366 10.378 -4.015 44.580 1.00 67.18 C
ANISOU 2378 CG PHE A 366 10336 7110 8079 729 -798 -96 C
ATOM 2379 CD1 PHE A 366 10.418 -5.074 45.473 1.00 67.37 C
ANISOU 2379 CD1 PHE A 366 11039 6746 7813 678 -936 64 C
ATOM 2380 CD2 PHE A 366 10.600 -4.269 43.237 1.00 72.12 C
ANISOU 2380 CD2 PHE A 366 10552 7832 9018 885 -829 -215 C
ATOM 2381 CE1 PHE A 366 10.676 -6.359 45.036 1.00 69.33 C
ANISOU 2381 CE1 PHE A 366 11527 6691 8124 801 -1111 102 C
ATOM 2382 CE2 PHE A 366 10.859 -5.553 42.794 1.00 75.71 C
ANISOU 2382 CE2 PHE A 366 11221 8012 9532 995 -985 -204 C
ATOM 2383 CZ PHE A 366 10.897 -6.599 43.695 1.00 71.19 C
ANISOU 2383 CZ PHE A 366 11302 7038 8711 962 -1131 -47 C
ATOM 2384 N LEU A 367 8.439 -0.367 47.121 1.00 62.60 N
ANISOU 2384 N LEU A 367 9581 7122 7084 -17 63 -193 N
ATOM 2385 CA LEU A 367 8.625 0.886 47.840 1.00 57.32 C
ANISOU 2385 CA LEU A 367 8791 6640 6347 -33 108 -259 C
ATOM 2386 C LEU A 367 7.590 1.149 48.924 1.00 56.52 C
ANISOU 2386 C LEU A 367 8995 6500 5982 -430 494 -281 C
ATOM 2387 O LEU A 367 7.750 2.115 49.679 1.00 56.67 O
ANISOU 2387 O LEU A 367 9000 6640 5891 -466 536 -343 O
ATOM 2388 CB LEU A 367 8.626 2.070 46.862 1.00 54.27 C
ANISOU 2388 CB LEU A 367 7704 6569 6345 89 192 -402 C
ATOM 2389 CG LEU A 367 9.838 2.158 45.937 1.00 57.19 C
ANISOU 2389 CG LEU A 367 7753 7026 6951 460 -146 -425 C
ATOM 2390 CD1 LEU A 367 9.700 3.363 45.031 1.00 54.14 C
ANISOU 2390 CD1 LEU A 367 6781 6911 6880 512 3 -540 C
ATOM 2391 CD2 LEU A 367 11.127 2.228 46.743 1.00 56.14 C
ANISOU 2391 CD2 LEU A 367 7835 6832 6664 682 -521 -409 C
ATOM 2392 N SER A 368 6.542 0.337 49.028 1.00 62.64 N
ANISOU 2392 N SER A 368 10031 7106 6663 -748 806 -264 N
ATOM 2393 CA SER A 368 5.530 0.489 50.065 1.00 64.65 C
ANISOU 2393 CA SER A 368 10596 7301 6667 -1177 1241 -322 C
ATOM 2394 C SER A 368 5.482 -0.790 50.885 1.00 73.26 C
ANISOU 2394 C SER A 368 12502 8014 7319 -1377 1241 -144 C
ATOM 2395 O SER A 368 5.216 -1.868 50.342 1.00 74.93 O
ANISOU 2395 O SER A 368 12846 8030 7593 -1421 1252 -81 O
ATOM 2396 CB SER A 368 4.158 0.797 49.464 1.00 64.34 C
ANISOU 2396 CB SER A 368 10079 7408 6959 -1446 1707 -529 C
ATOM 2397 OG SER A 368 3.172 0.911 50.476 1.00 71.11 O
ANISOU 2397 OG SER A 368 11206 8202 7610 -1887 2178 -640 O
ATOM 2398 N GLY A 369 5.746 -0.670 52.186 1.00 77.28 N
ANISOU 2398 N GLY A 369 13593 8403 7367 -1501 1223 -63 N
ATOM 2399 CA GLY A 369 5.671 -1.835 53.051 1.00 83.23 C
ANISOU 2399 CA GLY A 369 15231 8759 7633 -1718 1232 133 C
ATOM 2400 C GLY A 369 4.265 -2.391 53.158 1.00 94.26 C
ANISOU 2400 C GLY A 369 16798 10017 8998 -2242 1848 47 C
ATOM 2401 O GLY A 369 4.065 -3.607 53.131 1.00101.10 O
ANISOU 2401 O GLY A 369 18144 10551 9719 -2377 1880 183 O
ATOM 2402 N LYS A 370 3.271 -1.507 53.277 1.00 89.95 N
ANISOU 2402 N LYS A 370 15845 9710 8623 -2547 2353 -208 N
ATOM 2403 CA LYS A 370 1.884 -1.954 53.374 1.00 90.58 C
ANISOU 2403 CA LYS A 370 15980 9688 8746 -3069 2981 -372 C
ATOM 2404 C LYS A 370 1.440 -2.663 52.099 1.00 90.41 C
ANISOU 2404 C LYS A 370 15533 9652 9166 -3017 2991 -431 C
ATOM 2405 O LYS A 370 0.805 -3.724 52.153 1.00 94.53 O
ANISOU 2405 O LYS A 370 16424 9897 9595 -3343 3265 -417 O
ATOM 2406 CB LYS A 370 0.974 -0.763 53.678 1.00 95.81 C
ANISOU 2406 CB LYS A 370 16165 10638 9602 -3336 3470 -692 C
ATOM 2407 CG LYS A 370 0.650 -0.574 55.152 1.00 94.28 C
ANISOU 2407 CG LYS A 370 16612 10324 8888 -3759 3857 -728 C
ATOM 2408 CD LYS A 370 1.880 -0.217 55.972 1.00102.87 C
ANISOU 2408 CD LYS A 370 18185 11384 9516 -3490 3391 -511 C
ATOM 2409 CE LYS A 370 1.516 -0.011 57.436 1.00109.21 C
ANISOU 2409 CE LYS A 370 19667 12076 9750 -3938 3790 -562 C
ATOM 2410 NZ LYS A 370 2.699 0.341 58.269 1.00104.67 N
ANISOU 2410 NZ LYS A 370 19584 11482 8704 -3678 3296 -374 N
ATOM 2411 N PHE A 371 1.769 -2.091 50.936 1.00 77.48 N
ANISOU 2411 N PHE A 371 13148 8299 7993 -2627 2703 -506 N
ATOM 2412 CA PHE A 371 1.420 -2.733 49.673 1.00 74.84 C
ANISOU 2412 CA PHE A 371 12419 7970 8046 -2550 2661 -569 C
ATOM 2413 C PHE A 371 2.114 -4.081 49.531 1.00 78.44 C
ANISOU 2413 C PHE A 371 13426 8078 8298 -2417 2345 -322 C
ATOM 2414 O PHE A 371 1.518 -5.045 49.041 1.00 78.36 O
ANISOU 2414 O PHE A 371 13476 7892 8405 -2606 2512 -365 O
ATOM 2415 CB PHE A 371 1.777 -1.825 48.495 1.00 69.98 C
ANISOU 2415 CB PHE A 371 11006 7706 7876 -2143 2377 -661 C
ATOM 2416 CG PHE A 371 0.666 -0.901 48.077 1.00 70.32 C
ANISOU 2416 CG PHE A 371 10375 8030 8311 -2297 2716 -961 C
ATOM 2417 CD1 PHE A 371 -0.346 -1.347 47.242 1.00 66.38 C
ANISOU 2417 CD1 PHE A 371 9514 7561 8147 -2463 2921 -1156 C
ATOM 2418 CD2 PHE A 371 0.641 0.415 48.508 1.00 67.54 C
ANISOU 2418 CD2 PHE A 371 9742 7903 8018 -2256 2800 -1069 C
ATOM 2419 CE1 PHE A 371 -1.367 -0.500 46.852 1.00 64.90 C
ANISOU 2419 CE1 PHE A 371 8686 7619 8352 -2561 3168 -1454 C
ATOM 2420 CE2 PHE A 371 -0.377 1.267 48.121 1.00 63.10 C
ANISOU 2420 CE2 PHE A 371 8557 7565 7853 -2357 3073 -1355 C
ATOM 2421 CZ PHE A 371 -1.382 0.809 47.292 1.00 63.32 C
ANISOU 2421 CZ PHE A 371 8219 7620 8221 -2495 3237 -1548 C
ATOM 2422 N ARG A 372 3.377 -4.163 49.950 1.00 78.25 N
ANISOU 2422 N ARG A 372 13789 7942 8000 -2080 1872 -87 N
ATOM 2423 CA ARG A 372 4.110 -5.424 49.882 1.00 79.51 C
ANISOU 2423 CA ARG A 372 14489 7735 7985 -1901 1517 140 C
ATOM 2424 C ARG A 372 3.464 -6.485 50.766 1.00 87.64 C
ANISOU 2424 C ARG A 372 16343 8337 8619 -2348 1839 252 C
ATOM 2425 O ARG A 372 3.256 -7.630 50.339 1.00 92.31 O
ANISOU 2425 O ARG A 372 17173 8639 9261 -2428 1862 306 O
ATOM 2426 CB ARG A 372 5.564 -5.179 50.285 1.00 77.74 C
ANISOU 2426 CB ARG A 372 14481 7489 7568 -1449 934 318 C
ATOM 2427 CG ARG A 372 6.466 -6.395 50.289 1.00 80.85 C
ANISOU 2427 CG ARG A 372 15417 7494 7809 -1178 474 537 C
ATOM 2428 CD ARG A 372 7.915 -5.939 50.293 1.00 73.72 C
ANISOU 2428 CD ARG A 372 14372 6697 6941 -648 -133 590 C
ATOM 2429 NE ARG A 372 8.076 -4.697 51.041 1.00 74.94 N
ANISOU 2429 NE ARG A 372 14410 7121 6945 -670 -106 531 N
ATOM 2430 CZ ARG A 372 9.139 -3.907 50.969 1.00 75.69 C
ANISOU 2430 CZ ARG A 372 14158 7438 7163 -287 -502 477 C
ATOM 2431 NH1 ARG A 372 10.163 -4.197 50.183 1.00 76.29 N
ANISOU 2431 NH1 ARG A 372 13944 7517 7527 150 -945 461 N
ATOM 2432 NH2 ARG A 372 9.172 -2.796 51.698 1.00 72.62 N
ANISOU 2432 NH2 ARG A 372 13695 7271 6627 -363 -425 406 N
ATOM 2433 N GLU A 373 3.121 -6.111 52.003 1.00104.29 N
ANISOU 2433 N GLU A 373 18919 10387 10320 -2673 2123 276 N
ATOM 2434 CA GLU A 373 2.476 -7.050 52.915 1.00107.69 C
ANISOU 2434 CA GLU A 373 20206 10398 10315 -3162 2501 381 C
ATOM 2435 C GLU A 373 1.132 -7.512 52.370 1.00109.39 C
ANISOU 2435 C GLU A 373 20137 10591 10836 -3619 3095 141 C
ATOM 2436 O GLU A 373 0.789 -8.696 52.463 1.00115.49 O
ANISOU 2436 O GLU A 373 21460 10962 11461 -3886 3267 233 O
ATOM 2437 CB GLU A 373 2.302 -6.410 54.292 1.00109.81 C
ANISOU 2437 CB GLU A 373 20964 10668 10090 -3460 2758 396 C
ATOM 2438 CG GLU A 373 3.605 -6.081 55.003 1.00116.44 C
ANISOU 2438 CG GLU A 373 22222 11472 10545 -3059 2157 629 C
ATOM 2439 CD GLU A 373 3.425 -5.037 56.091 1.00124.40 C
ANISOU 2439 CD GLU A 373 23380 12666 11220 -3286 2400 536 C
ATOM 2440 OE1 GLU A 373 2.264 -4.710 56.415 1.00124.94 O
ANISOU 2440 OE1 GLU A 373 23356 12820 11296 -3798 3078 311 O
ATOM 2441 OE2 GLU A 373 4.443 -4.539 56.616 1.00121.65 O
ANISOU 2441 OE2 GLU A 373 23214 12382 10626 -2956 1917 652 O
ATOM 2442 N GLU A 374 0.356 -6.594 51.790 1.00 95.27 N
ANISOU 2442 N GLU A 374 17489 9213 9495 -3709 3395 -184 N
ATOM 2443 CA GLU A 374 -0.952 -6.980 51.273 1.00 88.83 C
ANISOU 2443 CA GLU A 374 16328 8406 9020 -4131 3927 -472 C
ATOM 2444 C GLU A 374 -0.842 -7.819 50.007 1.00 93.46 C
ANISOU 2444 C GLU A 374 16620 8926 9964 -3913 3671 -473 C
ATOM 2445 O GLU A 374 -1.672 -8.705 49.784 1.00 94.29 O
ANISOU 2445 O GLU A 374 16829 8820 10176 -4283 4024 -598 O
ATOM 2446 CB GLU A 374 -1.805 -5.739 51.031 1.00 88.11 C
ANISOU 2446 CB GLU A 374 15395 8756 9328 -4243 4256 -837 C
ATOM 2447 CG GLU A 374 -2.152 -5.019 52.311 1.00 97.19 C
ANISOU 2447 CG GLU A 374 16831 9942 10154 -4566 4645 -920 C
ATOM 2448 CD GLU A 374 -2.541 -5.982 53.413 1.00104.68 C
ANISOU 2448 CD GLU A 374 18584 10539 10651 -4885 4861 -896 C
ATOM 2449 OE1 GLU A 374 -3.487 -6.772 53.207 1.00107.19 O
ANISOU 2449 OE1 GLU A 374 18837 10753 11137 -5137 5155 -1113 O
ATOM 2450 OE2 GLU A 374 -1.898 -5.956 54.483 1.00110.00 O
ANISOU 2450 OE2 GLU A 374 19962 11040 10792 -4879 4725 -673 O
ATOM 2451 N PHE A 375 0.166 -7.565 49.169 1.00 88.84 N
ANISOU 2451 N PHE A 375 15672 8513 9569 -3343 3091 -365 N
ATOM 2452 CA PHE A 375 0.402 -8.437 48.025 1.00 83.33 C
ANISOU 2452 CA PHE A 375 14797 7718 9146 -3127 2831 -355 C
ATOM 2453 C PHE A 375 0.774 -9.841 48.480 1.00 91.01 C
ANISOU 2453 C PHE A 375 16649 8147 9784 -3214 2744 -105 C
ATOM 2454 O PHE A 375 0.303 -10.833 47.910 1.00 94.88 O
ANISOU 2454 O PHE A 375 17191 8421 10439 -3388 2883 -180 O
ATOM 2455 CB PHE A 375 1.496 -7.855 47.131 1.00 77.14 C
ANISOU 2455 CB PHE A 375 13514 7211 8584 -2524 2266 -296 C
ATOM 2456 CG PHE A 375 1.106 -6.577 46.444 1.00 76.49 C
ANISOU 2456 CG PHE A 375 12573 7618 8872 -2418 2324 -530 C
ATOM 2457 CD1 PHE A 375 -0.226 -6.217 46.319 1.00 74.08 C
ANISOU 2457 CD1 PHE A 375 11857 7480 8809 -2788 2788 -821 C
ATOM 2458 CD2 PHE A 375 2.074 -5.736 45.921 1.00 70.65 C
ANISOU 2458 CD2 PHE A 375 11441 7148 8256 -1947 1910 -476 C
ATOM 2459 CE1 PHE A 375 -0.584 -5.042 45.688 1.00 68.27 C
ANISOU 2459 CE1 PHE A 375 10364 7154 8422 -2650 2786 -1025 C
ATOM 2460 CE2 PHE A 375 1.722 -4.561 45.288 1.00 63.53 C
ANISOU 2460 CE2 PHE A 375 9824 6645 7670 -1848 1954 -662 C
ATOM 2461 CZ PHE A 375 0.393 -4.214 45.172 1.00 65.04 C
ANISOU 2461 CZ PHE A 375 9642 6980 8090 -2180 2367 -923 C
ATOM 2462 N LYS A 376 1.615 -9.944 49.512 1.00 87.03 N
ANISOU 2462 N LYS A 376 16863 7395 8808 -3090 2492 187 N
ATOM 2463 CA LYS A 376 1.945 -11.258 50.058 1.00 92.54 C
ANISOU 2463 CA LYS A 376 18500 7518 9143 -3170 2387 453 C
ATOM 2464 C LYS A 376 0.711 -11.941 50.638 1.00 91.55 C
ANISOU 2464 C LYS A 376 18862 7086 8837 -3858 3060 376 C
ATOM 2465 O LYS A 376 0.527 -13.152 50.468 1.00 94.43 O
ANISOU 2465 O LYS A 376 19594 7101 9185 -3967 3102 420 O
ATOM 2466 CB LYS A 376 3.040 -11.129 51.117 1.00 92.89 C
ANISOU 2466 CB LYS A 376 19227 7374 8691 -2896 1948 765 C
ATOM 2467 CG LYS A 376 4.450 -11.128 50.545 1.00 97.49 C
ANISOU 2467 CG LYS A 376 19598 8006 9436 -2210 1206 884 C
ATOM 2468 CD LYS A 376 5.271 -9.973 51.090 1.00 99.73 C
ANISOU 2468 CD LYS A 376 19727 8590 9576 -1900 875 926 C
ATOM 2469 CE LYS A 376 5.283 -9.969 52.610 1.00105.48 C
ANISOU 2469 CE LYS A 376 21354 9058 9665 -2141 935 1131 C
ATOM 2470 NZ LYS A 376 5.991 -8.777 53.155 1.00104.22 N
ANISOU 2470 NZ LYS A 376 21001 9221 9375 -1886 653 1121 N
ATOM 2471 N ALA A 377 -0.142 -11.182 51.329 1.00 96.82 N
ANISOU 2471 N ALA A 377 19402 7985 9402 -4247 3555 187 N
ATOM 2472 CA ALA A 377 -1.360 -11.756 51.894 1.00 96.55 C
ANISOU 2472 CA ALA A 377 19508 7907 9268 -4718 4104 -57 C
ATOM 2473 C ALA A 377 -2.301 -12.251 50.802 1.00 95.87 C
ANISOU 2473 C ALA A 377 18808 7918 9700 -4896 4385 -363 C
ATOM 2474 O ALA A 377 -2.883 -13.336 50.918 1.00104.72 O
ANISOU 2474 O ALA A 377 20234 8803 10753 -5140 4617 -433 O
ATOM 2475 CB ALA A 377 -2.061 -10.729 52.782 1.00 97.67 C
ANISOU 2475 CB ALA A 377 19476 8343 9292 -4991 4507 -295 C
ATOM 2476 N ALA A 378 -2.468 -11.466 49.735 1.00 95.67 N
ANISOU 2476 N ALA A 378 17916 8241 10191 -4777 4352 -564 N
ATOM 2477 CA ALA A 378 -3.320 -11.886 48.627 1.00 97.03 C
ANISOU 2477 CA ALA A 378 17460 8540 10867 -4895 4529 -880 C
ATOM 2478 C ALA A 378 -2.750 -13.115 47.932 1.00100.68 C
ANISOU 2478 C ALA A 378 18245 8635 11374 -4736 4228 -703 C
ATOM 2479 O ALA A 378 -3.498 -14.017 47.536 1.00104.19 O
ANISOU 2479 O ALA A 378 18609 8992 11985 -4949 4451 -892 O
ATOM 2480 CB ALA A 378 -3.497 -10.738 47.635 1.00 90.95 C
ANISOU 2480 CB ALA A 378 15726 8221 10610 -4738 4455 -1120 C
ATOM 2481 N PHE A 379 -1.425 -13.166 47.769 1.00 94.82 N
ANISOU 2481 N PHE A 379 17831 7693 10504 -4311 3688 -374 N
ATOM 2482 CA PHE A 379 -0.798 -14.349 47.189 1.00 96.84 C
ANISOU 2482 CA PHE A 379 18414 7583 10797 -4079 3347 -223 C
ATOM 2483 C PHE A 379 -1.029 -15.577 48.059 1.00102.38 C
ANISOU 2483 C PHE A 379 19927 7863 11110 -4318 3519 -73 C
ATOM 2484 O PHE A 379 -1.320 -16.664 47.547 1.00108.95 O
ANISOU 2484 O PHE A 379 20824 8482 12089 -4401 3575 -143 O
ATOM 2485 CB PHE A 379 0.698 -14.109 46.990 1.00 95.19 C
ANISOU 2485 CB PHE A 379 18228 7426 10513 -3394 2635 35 C
ATOM 2486 CG PHE A 379 1.080 -13.800 45.571 1.00 97.79 C
ANISOU 2486 CG PHE A 379 17721 8128 11307 -2969 2297 -140 C
ATOM 2487 CD1 PHE A 379 1.016 -12.504 45.086 1.00 93.46 C
ANISOU 2487 CD1 PHE A 379 16381 8139 10991 -2789 2246 -307 C
ATOM 2488 CD2 PHE A 379 1.508 -14.808 44.722 1.00 96.63 C
ANISOU 2488 CD2 PHE A 379 17621 7748 11348 -2758 2041 -140 C
ATOM 2489 CE1 PHE A 379 1.369 -12.220 43.779 1.00 89.73 C
ANISOU 2489 CE1 PHE A 379 15223 7984 10885 -2427 1954 -451 C
ATOM 2490 CE2 PHE A 379 1.863 -14.530 43.415 1.00 97.72 C
ANISOU 2490 CE2 PHE A 379 17037 8227 11865 -2399 1765 -314 C
ATOM 2491 CZ PHE A 379 1.793 -13.235 42.943 1.00 90.32 C
ANISOU 2491 CZ PHE A 379 15361 7845 11112 -2243 1725 -459 C
ATOM 2492 N SER A 380 -0.904 -15.424 49.380 1.00102.59 N
ANISOU 2492 N SER A 380 20557 7795 10627 -4412 3584 111 N
ATOM 2493 CA SER A 380 -1.106 -16.557 50.278 1.00109.61 C
ANISOU 2493 CA SER A 380 22243 8305 11098 -4620 3724 238 C
ATOM 2494 C SER A 380 -2.538 -17.073 50.207 1.00113.29 C
ANISOU 2494 C SER A 380 22495 8832 11720 -5134 4358 -107 C
ATOM 2495 O SER A 380 -2.767 -18.288 50.195 1.00121.64 O
ANISOU 2495 O SER A 380 23945 9560 12712 -5272 4452 -81 O
ATOM 2496 CB SER A 380 -0.749 -16.160 51.710 1.00112.77 C
ANISOU 2496 CB SER A 380 23299 8632 10916 -4641 3675 437 C
ATOM 2497 OG SER A 380 0.605 -15.753 51.800 1.00110.02 O
ANISOU 2497 OG SER A 380 23153 8224 10425 -4131 3036 740 O
ATOM 2498 N CYS A 381 -3.515 -16.166 50.163 1.00111.36 N
ANISOU 2498 N CYS A 381 21609 9001 11701 -5401 4783 -456 N
ATOM 2499 CA CYS A 381 -4.913 -16.581 50.081 1.00115.12 C
ANISOU 2499 CA CYS A 381 21796 9569 12376 -5847 5360 -848 C
ATOM 2500 C CYS A 381 -5.207 -17.279 48.758 1.00119.85 C
ANISOU 2500 C CYS A 381 21906 10169 13462 -5814 5312 -1015 C
ATOM 2501 O CYS A 381 -5.849 -18.336 48.730 1.00120.91 O
ANISOU 2501 O CYS A 381 22243 10090 13608 -6085 5591 -1135 O
ATOM 2502 CB CYS A 381 -5.828 -15.370 50.265 1.00113.69 C
ANISOU 2502 CB CYS A 381 20952 9848 12397 -6036 5728 -1220 C
ATOM 2503 SG CYS A 381 -7.561 -15.669 49.846 1.00117.27 S
ANISOU 2503 SG CYS A 381 20767 10509 13280 -6460 6333 -1803 S
ATOM 2504 N CYS A 382 -4.743 -16.700 47.648 1.00117.48 N
ANISOU 2504 N CYS A 382 20975 10100 13563 -5494 4962 -1043 N
ATOM 2505 CA CYS A 382 -5.044 -17.250 46.332 1.00116.54 C
ANISOU 2505 CA CYS A 382 20334 10027 13918 -5458 4893 -1259 C
ATOM 2506 C CYS A 382 -4.329 -18.569 46.070 1.00117.59 C
ANISOU 2506 C CYS A 382 21048 9682 13948 -5312 4616 -1010 C
ATOM 2507 O CYS A 382 -4.809 -19.367 45.257 1.00120.80 O
ANISOU 2507 O CYS A 382 21215 10033 14651 -5418 4700 -1214 O
ATOM 2508 CB CYS A 382 -4.678 -16.234 45.248 1.00106.22 C
ANISOU 2508 CB CYS A 382 18256 9083 13021 -5148 4571 -1371 C
ATOM 2509 SG CYS A 382 -5.243 -16.662 43.588 1.00106.22 S
ANISOU 2509 SG CYS A 382 17478 9268 13612 -5127 4499 -1747 S
ATOM 2510 N CYS A 383 -3.202 -18.821 46.737 1.00116.03 N
ANISOU 2510 N CYS A 383 21589 9143 13353 -5045 4261 -596 N
ATOM 2511 CA CYS A 383 -2.417 -20.021 46.482 1.00120.97 C
ANISOU 2511 CA CYS A 383 22735 9310 13916 -4810 3913 -362 C
ATOM 2512 C CYS A 383 -2.661 -21.137 47.489 1.00121.92 C
ANISOU 2512 C CYS A 383 23691 9016 13619 -5063 4129 -202 C
ATOM 2513 O CYS A 383 -2.411 -22.303 47.164 1.00124.89 O
ANISOU 2513 O CYS A 383 24386 9027 14041 -4993 3991 -119 O
ATOM 2514 CB CYS A 383 -0.922 -19.681 46.460 1.00118.88 C
ANISOU 2514 CB CYS A 383 22715 8914 13540 -4249 3271 -35 C
ATOM 2515 SG CYS A 383 -0.458 -18.498 45.172 1.00114.32 S
ANISOU 2515 SG CYS A 383 21255 8736 13446 -3909 2974 -220 S
ATOM 2516 N LEU A 384 -3.137 -20.821 48.688 1.00119.72 N
ANISOU 2516 N LEU A 384 23785 8768 12935 -5356 4466 -179 N
ATOM 2517 CA LEU A 384 -3.408 -21.850 49.686 1.00126.85 C
ANISOU 2517 CA LEU A 384 25532 9266 13398 -5632 4703 -55 C
ATOM 2518 C LEU A 384 -4.885 -22.228 49.696 1.00131.03 C
ANISOU 2518 C LEU A 384 25833 9887 14065 -6193 5396 -445 C
ATOM 2519 O LEU A 384 -5.251 -23.346 49.330 1.00134.85 O
ANISOU 2519 O LEU A 384 26460 10110 14669 -6357 5544 -516 O
ATOM 2520 CB LEU A 384 -2.975 -21.382 51.077 1.00129.39 C
ANISOU 2520 CB LEU A 384 26528 9506 13129 -5615 4631 188 C
ATOM 2521 CG LEU A 384 -1.482 -21.095 51.254 1.00126.69 C
ANISOU 2521 CG LEU A 384 26509 9038 12589 -5047 3911 573 C
ATOM 2522 CD1 LEU A 384 -1.184 -20.681 52.685 1.00130.19 C
ANISOU 2522 CD1 LEU A 384 27631 9407 12427 -5086 3866 760 C
ATOM 2523 CD2 LEU A 384 -0.651 -22.304 50.856 1.00128.92 C
ANISOU 2523 CD2 LEU A 384 27200 8875 12908 -4711 3451 810 C
TER 2524 LEU A 384
HETATM 2525 C01 NRK A1001 -3.558 7.652 20.258 1.00 59.23 C
HETATM 2526 C02 NRK A1001 -3.064 8.795 19.424 1.00 60.19 C
HETATM 2527 C03 NRK A1001 -2.036 7.902 20.053 1.00 58.73 C
HETATM 2528 C04 NRK A1001 -1.293 6.930 19.185 1.00 59.75 C
HETATM 2529 C05 NRK A1001 -4.126 6.485 19.555 1.00 61.48 C
HETATM 2530 C06 NRK A1001 -1.282 8.400 21.250 1.00 57.60 C
HETATM 2531 C07 NRK A1001 -1.446 7.812 22.496 1.00 57.10 C
HETATM 2532 C08 NRK A1001 -0.750 8.287 23.574 1.00 54.57 C
HETATM 2533 C09 NRK A1001 0.118 9.337 23.480 1.00 51.74 C
HETATM 2534 C10 NRK A1001 0.290 9.935 22.252 1.00 53.12 C
HETATM 2535 C11 NRK A1001 -0.406 9.474 21.144 1.00 55.90 C
HETATM 2536 O12 NRK A1001 -1.011 5.776 19.984 1.00 58.98 O
HETATM 2537 C13 NRK A1001 -1.106 4.562 19.380 1.00 60.14 C
HETATM 2538 C14 NRK A1001 -1.057 3.384 20.132 1.00 61.44 C
HETATM 2539 N15 NRK A1001 -1.167 2.202 19.519 1.00 63.46 N
HETATM 2540 C16 NRK A1001 -1.327 2.182 18.197 1.00 60.71 C
HETATM 2541 N17 NRK A1001 -1.390 3.268 17.420 1.00 59.14 N
HETATM 2542 C18 NRK A1001 -1.284 4.461 18.017 1.00 60.18 C
HETATM 2543 O19 NRK A1001 -4.378 6.505 18.357 1.00 61.40 O
HETATM 2544 N20 NRK A1001 -4.293 5.395 20.346 1.00 61.73 N
HETATM 2545 C21 NRK A1001 -4.542 4.064 19.963 1.00 61.80 C
HETATM 2546 C22 NRK A1001 -4.544 3.624 18.640 1.00 63.80 C
HETATM 2547 C23 NRK A1001 -4.796 2.290 18.394 1.00 62.37 C
HETATM 2548 C24 NRK A1001 -5.023 1.468 19.461 1.00 61.56 C
HETATM 2549 C25 NRK A1001 -5.003 1.948 20.735 1.00 60.77 C
HETATM 2550 N26 NRK A1001 -4.760 3.242 20.996 1.00 60.91 N
HETATM 2551 C27 NRK A1001 -1.447 0.849 17.534 1.00 62.14 C
HETATM 2552 C28 NRK A1001 -0.878 3.398 21.618 1.00 59.70 C
HETATM 2553 F29 NRK A1001 -5.272 0.147 19.239 1.00 65.23 F
HETATM 2554 F30 NRK A1001 -0.925 7.690 24.782 1.00 55.99 F
CONECT 748 1339
CONECT 1339 748
CONECT 2525 2526 2527 2529
CONECT 2526 2525 2527
CONECT 2527 2525 2526 2528 2530
CONECT 2528 2527 2536
CONECT 2529 2525 2543 2544
CONECT 2530 2527 2531 2535
CONECT 2531 2530 2532
CONECT 2532 2531 2533 2554
CONECT 2533 2532 2534
CONECT 2534 2533 2535
CONECT 2535 2530 2534
CONECT 2536 2528 2537
CONECT 2537 2536 2538 2542
CONECT 2538 2537 2539 2552
CONECT 2539 2538 2540
CONECT 2540 2539 2541 2551
CONECT 2541 2540 2542
CONECT 2542 2537 2541
CONECT 2543 2529
CONECT 2544 2529 2545
CONECT 2545 2544 2546 2550
CONECT 2546 2545 2547
CONECT 2547 2546 2548
CONECT 2548 2547 2549 2553
CONECT 2549 2548 2550
CONECT 2550 2545 2549
CONECT 2551 2540
CONECT 2552 2538
CONECT 2553 2548
CONECT 2554 2532
MASTER 328 0 1 12 2 0 0 6 2550 1 32 27
END