HEADER MEMBRANE PROTEIN 04-JUN-23 8T1V
TITLE CRYSTAL STRUCTURE OF ORPHAN G PROTEIN-COUPLED RECEPTOR 6 WITH BOUND
TITLE 2 INVERSE AGONIST 3H
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: G-PROTEIN COUPLED RECEPTOR 6, SOLUBLE CYTOCHROME B562
COMPND 3 CHIMERA;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: SPHINGOSINE 1-PHOSPHATE RECEPTOR GPR6,CYTOCHROME B-562;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 562;
SOURCE 5 GENE: GPR6, CYBC;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS ORPHAN GPCR, GPR6, BRIL, INVERSE AGONIST, IAG3H, LCP, APS, MEMBRANE
KEYWDS 2 PROTEIN, PARKINSON'S DISEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BAREKATAIN,L.JOHANSSON,J.H.LAM,A.V.SADYBEKOV,G.W.HAN,P.POPOV,
AUTHOR 2 J.RUSSO,J.BLIESATH,N.BRICE,M.BERESFORD,L.CARLSON,K.S.SAIKATENDU,
AUTHOR 3 H.SUN,S.MURPHY,H.MONENSCHEIN,H.H.SCHIFFER,C.LUTOMSKI,C.V.ROBINSON,
AUTHOR 4 Z.LIU,T.HUA,V.KATRITCH,V.CHEREZOV
REVDAT 2 18-DEC-24 8T1V 1 JRNL REMARK
REVDAT 1 04-DEC-24 8T1V 0
JRNL AUTH M.BAREKATAIN,L.C.JOHANSSON,J.H.LAM,H.CHANG,A.V.SADYBEKOV,
JRNL AUTH 2 G.W.HAN,J.RUSSO,J.BLIESATH,N.L.BRICE,M.B.L.CARLTON,
JRNL AUTH 3 K.S.SAIKATENDU,H.SUN,S.T.MURPHY,H.MONENSCHEIN,H.H.SCHIFFER,
JRNL AUTH 4 P.POPOV,C.A.LUTOMSKI,C.V.ROBINSON,Z.J.LIU,T.HUA,V.KATRITCH,
JRNL AUTH 5 V.CHEREZOV
JRNL TITL STRUCTURAL INSIGHTS INTO THE HIGH BASAL ACTIVITY AND INVERSE
JRNL TITL 2 AGONISM OF THE ORPHAN RECEPTOR GPR6 IMPLICATED IN
JRNL TITL 3 PARKINSON'S DISEASE.
JRNL REF SCI.SIGNAL. V. 17 O8741 2024
JRNL REFN ESSN 1937-9145
JRNL PMID 39626010
JRNL DOI 10.1126/SCISIGNAL.ADO8741
REMARK 2
REMARK 2 RESOLUTION. 2.60 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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 49.850
REMARK 3 COMPLETENESS FOR RANGE (%) : 71.5
REMARK 3 NUMBER OF REFLECTIONS : 13293
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 676
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 41.1300 - 4.4500 0.94 3696 202 0.2230 0.2714
REMARK 3 2 4.4500 - 3.5300 0.94 3488 206 0.2151 0.2324
REMARK 3 3 3.5300 - 3.0900 0.85 3135 137 0.2526 0.2729
REMARK 3 4 3.0900 - 2.8100 0.41 1478 70 0.2865 0.2585
REMARK 3 5 2.8000 - 2.6000 0.23 833 48 0.3250 0.3181
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) : 0.000
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.002 2727
REMARK 3 ANGLE : 0.442 3738
REMARK 3 CHIRALITY : 0.031 464
REMARK 3 PLANARITY : 0.004 458
REMARK 3 DIHEDRAL : 11.174 919
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 68:256 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.348 -3.902 -1.875
REMARK 3 T TENSOR
REMARK 3 T11: 0.1457 T22: 0.4177
REMARK 3 T33: 0.2820 T12: 0.1897
REMARK 3 T13: 0.0754 T23: -0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 1.1868 L22: 1.8708
REMARK 3 L33: 2.6263 L12: 0.2449
REMARK 3 L13: 0.2605 L23: 1.0409
REMARK 3 S TENSOR
REMARK 3 S11: -0.1376 S12: 0.1027 S13: -0.1934
REMARK 3 S21: 0.2031 S22: 0.2533 S23: -0.3462
REMARK 3 S31: 0.7442 S32: 0.7953 S33: 0.0958
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 1001:1106 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.710 10.547 -48.707
REMARK 3 T TENSOR
REMARK 3 T11: 0.6362 T22: 0.8175
REMARK 3 T33: 0.5382 T12: -0.3486
REMARK 3 T13: -0.1041 T23: 0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 1.3100 L22: 0.3772
REMARK 3 L33: 1.3554 L12: -0.6314
REMARK 3 L13: -1.2571 L23: 0.5004
REMARK 3 S TENSOR
REMARK 3 S11: -0.6236 S12: -0.2029 S13: 0.1320
REMARK 3 S21: -0.3910 S22: 0.2487 S23: -0.0192
REMARK 3 S31: -0.2196 S32: 1.0293 S33: -0.0957
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 270:900 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.684 -9.701 -6.594
REMARK 3 T TENSOR
REMARK 3 T11: 0.3477 T22: 0.2445
REMARK 3 T33: 0.2705 T12: 0.1776
REMARK 3 T13: 0.1325 T23: -0.1217
REMARK 3 L TENSOR
REMARK 3 L11: 1.9045 L22: 2.4947
REMARK 3 L33: 1.1264 L12: 0.2678
REMARK 3 L13: 0.2921 L23: -0.1640
REMARK 3 S TENSOR
REMARK 3 S11: -0.0719 S12: 0.5318 S13: -0.5464
REMARK 3 S21: -0.0857 S22: 0.0573 S23: -0.4057
REMARK 3 S31: 1.2460 S32: 0.4647 S33: -0.1210
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 8T1V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-23.
REMARK 100 THE DEPOSITION ID IS D_1000275051.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-19
REMARK 200 TEMPERATURE (KELVIN) : 123
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14570
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 78.2
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.14700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.69300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NACH3COO, PEG 400, NACL, PPG P40,
REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 166.44667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 83.22333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 83.22333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 166.44667
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 MET A 21
REMARK 465 LYS A 22
REMARK 465 THR A 23
REMARK 465 ILE A 24
REMARK 465 ILE A 25
REMARK 465 ALA A 26
REMARK 465 LEU A 27
REMARK 465 SER A 28
REMARK 465 TYR A 29
REMARK 465 ILE A 30
REMARK 465 PHE A 31
REMARK 465 CYS A 32
REMARK 465 LEU A 33
REMARK 465 VAL A 34
REMARK 465 PHE A 35
REMARK 465 ALA A 36
REMARK 465 ASP A 37
REMARK 465 TYR A 38
REMARK 465 LYS A 39
REMARK 465 ASP A 40
REMARK 465 ASP A 41
REMARK 465 ASP A 42
REMARK 465 ASP A 43
REMARK 465 ALA A 44
REMARK 465 GLY A 45
REMARK 465 ARG A 46
REMARK 465 ALA A 47
REMARK 465 GLY A 48
REMARK 465 GLY A 49
REMARK 465 ALA A 50
REMARK 465 ASN A 51
REMARK 465 GLY A 52
REMARK 465 SER A 53
REMARK 465 LEU A 54
REMARK 465 GLU A 55
REMARK 465 LEU A 56
REMARK 465 SER A 57
REMARK 465 SER A 58
REMARK 465 GLN A 59
REMARK 465 LEU A 60
REMARK 465 SER A 61
REMARK 465 ALA A 62
REMARK 465 GLY A 63
REMARK 465 PRO A 64
REMARK 465 PRO A 65
REMARK 465 GLY A 66
REMARK 465 LEU A 67
REMARK 465 PRO A 1046
REMARK 465 LYS A 1047
REMARK 465 LEU A 1048
REMARK 465 GLU A 1049
REMARK 465 ASP A 1050
REMARK 465 LYS A 1051
REMARK 465 SER A 1052
REMARK 465 PRO A 1053
REMARK 465 ASP A 1054
REMARK 465 SER A 1055
REMARK 465 PRO A 1056
REMARK 465 GLU A 1057
REMARK 465 MET A 1058
REMARK 465 LYS A 1059
REMARK 465 ASP A 1060
REMARK 465 PHE A 1061
REMARK 465 ARG A 1062
REMARK 465 HIS A 1063
REMARK 465 GLY A 1064
REMARK 465 PHE A 1065
REMARK 465 CYS A 347
REMARK 465 PHE A 348
REMARK 465 GLN A 349
REMARK 465 SER A 350
REMARK 465 LYS A 351
REMARK 465 VAL A 352
REMARK 465 PRO A 353
REMARK 465 PHE A 354
REMARK 465 ARG A 355
REMARK 465 SER A 356
REMARK 465 ARG A 357
REMARK 465 SER A 358
REMARK 465 PRO A 359
REMARK 465 SER A 360
REMARK 465 GLU A 361
REMARK 465 VAL A 362
REMARK 465 GLU A 363
REMARK 465 PHE A 364
REMARK 465 LEU A 365
REMARK 465 GLU A 366
REMARK 465 VAL A 367
REMARK 465 LEU A 368
REMARK 465 PHE A 369
REMARK 465 GLN A 370
REMARK 465 GLY A 371
REMARK 465 PRO A 372
REMARK 465 HIS A 373
REMARK 465 HIS A 374
REMARK 465 HIS A 375
REMARK 465 HIS A 376
REMARK 465 HIS A 377
REMARK 465 HIS A 378
REMARK 465 HIS A 379
REMARK 465 HIS A 380
REMARK 465 HIS A 381
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 69 CG CD1 CD2
REMARK 470 LEU A 134 CG CD1 CD2
REMARK 470 VAL A 135 CG1 CG2
REMARK 470 TYR A 177 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 212 CG CD OE1 OE2
REMARK 470 ARG A 220 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1025 CG CD OE1 NE2
REMARK 470 GLN A1041 CG CD OE1 NE2
REMARK 470 ASP A1066 CG OD1 OD2
REMARK 470 GLN A1103 CG CD OE1 NE2
REMARK 470 TYR A1105 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 338 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 340 CG CD1 CD2
REMARK 470 LEU A 344 CG CD1 CD2
REMARK 470 ASP A 345 CG OD1 OD2
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 LEU A 134 65.62 60.81
REMARK 500 ASN A 172 87.13 -159.79
REMARK 500 LYS A1019 58.52 -94.52
REMARK 500 GLU A1081 56.91 -94.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1202 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 118 OD1
REMARK 620 2 ASN A 321 OD1 127.5
REMARK 620 N 1
DBREF 8T1V A 48 256 UNP P46095 GPR6_HUMAN 48 256
DBREF 8T1V A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128
DBREF 8T1V A 270 362 UNP P46095 GPR6_HUMAN 270 362
SEQADV 8T1V MET A 21 UNP P46095 INITIATING METHIONINE
SEQADV 8T1V LYS A 22 UNP P46095 EXPRESSION TAG
SEQADV 8T1V THR A 23 UNP P46095 EXPRESSION TAG
SEQADV 8T1V ILE A 24 UNP P46095 EXPRESSION TAG
SEQADV 8T1V ILE A 25 UNP P46095 EXPRESSION TAG
SEQADV 8T1V ALA A 26 UNP P46095 EXPRESSION TAG
SEQADV 8T1V LEU A 27 UNP P46095 EXPRESSION TAG
SEQADV 8T1V SER A 28 UNP P46095 EXPRESSION TAG
SEQADV 8T1V TYR A 29 UNP P46095 EXPRESSION TAG
SEQADV 8T1V ILE A 30 UNP P46095 EXPRESSION TAG
SEQADV 8T1V PHE A 31 UNP P46095 EXPRESSION TAG
SEQADV 8T1V CYS A 32 UNP P46095 EXPRESSION TAG
SEQADV 8T1V LEU A 33 UNP P46095 EXPRESSION TAG
SEQADV 8T1V VAL A 34 UNP P46095 EXPRESSION TAG
SEQADV 8T1V PHE A 35 UNP P46095 EXPRESSION TAG
SEQADV 8T1V ALA A 36 UNP P46095 EXPRESSION TAG
SEQADV 8T1V ASP A 37 UNP P46095 EXPRESSION TAG
SEQADV 8T1V TYR A 38 UNP P46095 EXPRESSION TAG
SEQADV 8T1V LYS A 39 UNP P46095 EXPRESSION TAG
SEQADV 8T1V ASP A 40 UNP P46095 EXPRESSION TAG
SEQADV 8T1V ASP A 41 UNP P46095 EXPRESSION TAG
SEQADV 8T1V ASP A 42 UNP P46095 EXPRESSION TAG
SEQADV 8T1V ASP A 43 UNP P46095 EXPRESSION TAG
SEQADV 8T1V ALA A 44 UNP P46095 EXPRESSION TAG
SEQADV 8T1V GLY A 45 UNP P46095 EXPRESSION TAG
SEQADV 8T1V ARG A 46 UNP P46095 EXPRESSION TAG
SEQADV 8T1V ALA A 47 UNP P46095 EXPRESSION TAG
SEQADV 8T1V LEU A 123 UNP P46095 CYS 123 ENGINEERED MUTATION
SEQADV 8T1V PRO A 173 UNP P46095 ALA 173 ENGINEERED MUTATION
SEQADV 8T1V TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 8T1V ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION
SEQADV 8T1V LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION
SEQADV 8T1V ALA A 900 UNP P0ABE7 LINKER
SEQADV 8T1V ARG A 279 UNP P46095 GLY 279 ENGINEERED MUTATION
SEQADV 8T1V CYS A 291 UNP P46095 SER 291 ENGINEERED MUTATION
SEQADV 8T1V LEU A 320 UNP P46095 TYR 320 ENGINEERED MUTATION
SEQADV 8T1V ASP A 345 UNP P46095 CYS 345 ENGINEERED MUTATION
SEQADV 8T1V GLU A 363 UNP P46095 EXPRESSION TAG
SEQADV 8T1V PHE A 364 UNP P46095 EXPRESSION TAG
SEQADV 8T1V LEU A 365 UNP P46095 EXPRESSION TAG
SEQADV 8T1V GLU A 366 UNP P46095 EXPRESSION TAG
SEQADV 8T1V VAL A 367 UNP P46095 EXPRESSION TAG
SEQADV 8T1V LEU A 368 UNP P46095 EXPRESSION TAG
SEQADV 8T1V PHE A 369 UNP P46095 EXPRESSION TAG
SEQADV 8T1V GLN A 370 UNP P46095 EXPRESSION TAG
SEQADV 8T1V GLY A 371 UNP P46095 EXPRESSION TAG
SEQADV 8T1V PRO A 372 UNP P46095 EXPRESSION TAG
SEQADV 8T1V HIS A 373 UNP P46095 EXPRESSION TAG
SEQADV 8T1V HIS A 374 UNP P46095 EXPRESSION TAG
SEQADV 8T1V HIS A 375 UNP P46095 EXPRESSION TAG
SEQADV 8T1V HIS A 376 UNP P46095 EXPRESSION TAG
SEQADV 8T1V HIS A 377 UNP P46095 EXPRESSION TAG
SEQADV 8T1V HIS A 378 UNP P46095 EXPRESSION TAG
SEQADV 8T1V HIS A 379 UNP P46095 EXPRESSION TAG
SEQADV 8T1V HIS A 380 UNP P46095 EXPRESSION TAG
SEQADV 8T1V HIS A 381 UNP P46095 EXPRESSION TAG
SEQRES 1 A 455 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU
SEQRES 2 A 455 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA GLY ARG
SEQRES 3 A 455 ALA GLY GLY ALA ASN GLY SER LEU GLU LEU SER SER GLN
SEQRES 4 A 455 LEU SER ALA GLY PRO PRO GLY LEU LEU LEU PRO ALA VAL
SEQRES 5 A 455 ASN PRO TRP ASP VAL LEU LEU CYS VAL SER GLY THR VAL
SEQRES 6 A 455 ILE ALA GLY GLU ASN ALA LEU VAL VAL ALA LEU ILE ALA
SEQRES 7 A 455 SER THR PRO ALA LEU ARG THR PRO MET PHE VAL LEU VAL
SEQRES 8 A 455 GLY SER LEU ALA THR ALA ASP LEU LEU ALA GLY LEU GLY
SEQRES 9 A 455 LEU ILE LEU HIS PHE VAL PHE GLN TYR LEU VAL PRO SER
SEQRES 10 A 455 GLU THR VAL SER LEU LEU THR VAL GLY PHE LEU VAL ALA
SEQRES 11 A 455 SER PHE ALA ALA SER VAL SER SER LEU LEU ALA ILE THR
SEQRES 12 A 455 VAL ASP ARG TYR LEU SER LEU TYR ASN PRO LEU THR TYR
SEQRES 13 A 455 TYR SER ARG ARG THR LEU LEU GLY VAL HIS LEU LEU LEU
SEQRES 14 A 455 ALA ALA THR TRP THR VAL SER LEU GLY LEU GLY LEU LEU
SEQRES 15 A 455 PRO VAL LEU GLY TRP ASN CYS LEU ALA GLU ARG ALA ALA
SEQRES 16 A 455 CYS SER VAL VAL ARG PRO LEU ALA ARG SER HIS VAL ALA
SEQRES 17 A 455 LEU LEU SER ALA ALA PHE PHE MET VAL PHE GLY ILE MET
SEQRES 18 A 455 LEU HIS LEU TYR VAL ARG ILE CYS GLN VAL VAL TRP ARG
SEQRES 19 A 455 HIS ALA ALA ASP LEU GLU ASP ASN TRP GLU THR LEU ASN
SEQRES 20 A 455 ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA
SEQRES 21 A 455 GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA
SEQRES 22 A 455 LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP
SEQRES 23 A 455 LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS
SEQRES 24 A 455 GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU
SEQRES 25 A 455 LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA
SEQRES 26 A 455 ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA TYR ILE
SEQRES 27 A 455 GLN LYS TYR LEU ALA HIS LEU ALA ALA THR ARG LYS GLY
SEQRES 28 A 455 VAL ARG THR LEU ALA VAL VAL LEU GLY THR PHE GLY ALA
SEQRES 29 A 455 CYS TRP LEU PRO PHE ALA ILE TYR CYS VAL VAL GLY SER
SEQRES 30 A 455 HIS GLU ASP PRO ALA VAL TYR THR TYR ALA THR LEU LEU
SEQRES 31 A 455 PRO ALA THR LEU ASN SER MET ILE ASN PRO ILE ILE TYR
SEQRES 32 A 455 ALA PHE ARG ASN GLN GLU ILE GLN ARG ALA LEU TRP LEU
SEQRES 33 A 455 LEU LEU ASP GLY CYS PHE GLN SER LYS VAL PRO PHE ARG
SEQRES 34 A 455 SER ARG SER PRO SER GLU VAL GLU PHE LEU GLU VAL LEU
SEQRES 35 A 455 PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS HIS HIS HIS
HET XY8 A1201 30
HET NA A1202 1
HETNAM XY8 3-{4-[(2,4-DIFLUOROPHENYL)METHYL]PIPERAZIN-1-YL}-7-
HETNAM 2 XY8 METHYL-N-(PROPAN-2-YL)PYRIDO[3,4-B]PYRAZIN-2-AMINE
HETNAM NA SODIUM ION
FORMUL 2 XY8 C22 H26 F2 N6
FORMUL 3 NA NA 1+
FORMUL 4 HOH *5(H2 O)
HELIX 1 AA1 ALA A 71 THR A 100 1 30
HELIX 2 AA2 PRO A 101 ARG A 104 5 4
HELIX 3 AA3 THR A 105 TYR A 133 1 29
HELIX 4 AA4 SER A 137 ASN A 172 1 36
HELIX 5 AA5 ARG A 179 LEU A 202 1 24
HELIX 6 AA6 PRO A 203 GLY A 206 5 4
HELIX 7 AA7 ALA A 223 LYS A 1019 1 53
HELIX 8 AA8 ASN A 1022 THR A 1044 1 23
HELIX 9 AA9 ILE A 1067 GLU A 1081 1 15
HELIX 10 AB1 LYS A 1083 GLY A 302 1 58
HELIX 11 AB2 ALA A 308 ASN A 333 1 26
HELIX 12 AB3 ASN A 333 LEU A 343 1 11
SSBOND 1 CYS A 209 CYS A 216 1555 1555 2.03
LINK OD1 ASP A 118 NA NA A1202 1555 1555 2.89
LINK OD1 ASN A 321 NA NA A1202 1555 1555 2.42
CISPEP 1 ARG A 220 PRO A 221 0 -1.04
CRYST1 63.136 63.136 249.670 90.00 90.00 120.00 P 32 2 1 6
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 0.015839 0.009145 0.000000 0.00000
SCALE2 0.000000 0.018289 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004005 0.00000
ATOM 1 N LEU A 68 -2.585 -21.957 10.059 1.00 92.64 N
ANISOU 1 N LEU A 68 16241 8783 10175 -666 2230 380 N
ATOM 2 CA LEU A 68 -1.329 -21.784 10.778 1.00 93.37 C
ANISOU 2 CA LEU A 68 16457 8845 10173 -381 2102 483 C
ATOM 3 C LEU A 68 -1.416 -20.639 11.784 1.00 97.27 C
ANISOU 3 C LEU A 68 16788 9488 10684 -406 2107 503 C
ATOM 4 O LEU A 68 -0.399 -20.063 12.169 1.00 96.04 O
ANISOU 4 O LEU A 68 16596 9390 10506 -172 1993 571 O
ATOM 5 CB LEU A 68 -0.182 -21.529 9.795 1.00 96.73 C
ANISOU 5 CB LEU A 68 16757 9322 10675 -103 1973 506 C
ATOM 6 CG LEU A 68 0.314 -22.731 8.989 1.00101.84 C
ANISOU 6 CG LEU A 68 17619 9803 11273 23 1919 508 C
ATOM 7 CD1 LEU A 68 1.356 -22.293 7.969 1.00 98.27 C
ANISOU 7 CD1 LEU A 68 16970 9446 10923 279 1803 509 C
ATOM 8 CD2 LEU A 68 0.884 -23.800 9.911 1.00 99.47 C
ANISOU 8 CD2 LEU A 68 17719 9301 10774 161 1849 580 C
ATOM 9 N LEU A 69 -2.635 -20.306 12.207 1.00 99.75 N
ANISOU 9 N LEU A 69 16993 9873 11035 -685 2234 436 N
ATOM 10 CA LEU A 69 -2.798 -19.233 13.186 1.00 89.23 C
ANISOU 10 CA LEU A 69 15505 8682 9718 -723 2244 446 C
ATOM 11 C LEU A 69 -2.088 -19.540 14.496 1.00101.72 C
ANISOU 11 C LEU A 69 17385 10153 11111 -587 2184 546 C
ATOM 12 O LEU A 69 -1.309 -18.692 14.965 1.00100.81 O
ANISOU 12 O LEU A 69 17169 10139 10996 -411 2091 601 O
ATOM 13 CB LEU A 69 -4.290 -18.969 13.411 1.00 87.28 C
ANISOU 13 CB LEU A 69 15104 8524 9536 -1042 2389 341 C
ATOM 14 N PRO A 70 -2.290 -20.695 15.128 1.00101.32 N
ANISOU 14 N PRO A 70 17703 9903 10891 -653 2224 573 N
ATOM 15 CA PRO A 70 -1.549 -21.028 16.355 1.00101.59 C
ANISOU 15 CA PRO A 70 18042 9824 10735 -503 2145 671 C
ATOM 16 C PRO A 70 -0.212 -21.721 16.131 1.00105.00 C
ANISOU 16 C PRO A 70 18694 10127 11075 -179 1977 749 C
ATOM 17 O PRO A 70 0.390 -22.176 17.109 1.00 99.73 O
ANISOU 17 O PRO A 70 18313 9343 10237 -46 1897 823 O
ATOM 18 CB PRO A 70 -2.523 -21.973 17.071 1.00 98.25 C
ANISOU 18 CB PRO A 70 17913 9242 10176 -759 2279 653 C
ATOM 19 CG PRO A 70 -3.203 -22.693 15.959 1.00 93.81 C
ANISOU 19 CG PRO A 70 17337 8621 9685 -908 2360 577 C
ATOM 20 CD PRO A 70 -3.331 -21.697 14.829 1.00 96.03 C
ANISOU 20 CD PRO A 70 17183 9113 10192 -901 2352 508 C
ATOM 21 N ALA A 71 0.259 -21.813 14.891 1.00108.16 N
ANISOU 21 N ALA A 71 18964 10552 11582 -45 1918 727 N
ATOM 22 CA ALA A 71 1.477 -22.540 14.539 1.00105.87 C
ANISOU 22 CA ALA A 71 18853 10151 11221 264 1759 777 C
ATOM 23 C ALA A 71 2.570 -21.526 14.204 1.00105.27 C
ANISOU 23 C ALA A 71 18499 10260 11240 537 1619 796 C
ATOM 24 O ALA A 71 2.725 -21.115 13.053 1.00108.03 O
ANISOU 24 O ALA A 71 18594 10714 11738 582 1610 755 O
ATOM 25 CB ALA A 71 1.209 -23.489 13.373 1.00 95.97 C
ANISOU 25 CB ALA A 71 17672 8784 10007 213 1798 730 C
ATOM 26 N VAL A 72 3.347 -21.141 15.218 1.00104.10 N
ANISOU 26 N VAL A 72 18406 10150 10998 719 1504 857 N
ATOM 27 CA VAL A 72 4.380 -20.126 15.028 1.00 97.92 C
ANISOU 27 CA VAL A 72 17352 9560 10293 969 1369 870 C
ATOM 28 C VAL A 72 5.632 -20.735 14.407 1.00 98.02 C
ANISOU 28 C VAL A 72 17413 9541 10289 1297 1196 874 C
ATOM 29 O VAL A 72 6.152 -20.230 13.406 1.00104.87 O
ANISOU 29 O VAL A 72 18010 10546 11289 1424 1145 839 O
ATOM 30 CB VAL A 72 4.699 -19.435 16.365 1.00 91.15 C
ANISOU 30 CB VAL A 72 16511 8779 9344 1027 1308 922 C
ATOM 31 CG1 VAL A 72 5.809 -18.411 16.184 1.00 84.93 C
ANISOU 31 CG1 VAL A 72 15441 8200 8629 1290 1158 929 C
ATOM 32 CG2 VAL A 72 3.452 -18.783 16.940 1.00 89.78 C
ANISOU 32 CG2 VAL A 72 16252 8660 9201 702 1481 903 C
ATOM 33 N ASN A 73 6.151 -21.811 14.997 1.00104.99 N
ANISOU 33 N ASN A 73 18631 10250 11009 1442 1100 909 N
ATOM 34 CA ASN A 73 7.313 -22.464 14.402 1.00 98.34 C
ANISOU 34 CA ASN A 73 17828 9381 10157 1753 933 894 C
ATOM 35 C ASN A 73 7.018 -22.974 12.998 1.00102.01 C
ANISOU 35 C ASN A 73 18227 9801 10730 1694 999 840 C
ATOM 36 O ASN A 73 7.857 -22.758 12.105 1.00101.55 O
ANISOU 36 O ASN A 73 17949 9863 10772 1902 899 799 O
ATOM 37 CB ASN A 73 7.807 -23.596 15.314 1.00 86.40 C
ANISOU 37 CB ASN A 73 16717 7666 8445 1900 824 939 C
ATOM 38 CG ASN A 73 9.127 -24.185 14.852 1.00 70.44 C
ANISOU 38 CG ASN A 73 14706 5644 6412 2255 625 914 C
ATOM 39 OD1 ASN A 73 9.572 -23.944 13.731 1.00 85.42 O
ANISOU 39 OD1 ASN A 73 16341 7666 8448 2361 591 856 O
ATOM 40 ND2 ASN A 73 9.758 -24.969 15.718 1.00 64.00 N
ANISOU 40 ND2 ASN A 73 14194 4692 5432 2438 491 949 N
ATOM 41 N PRO A 74 5.887 -23.629 12.723 1.00 88.02 N
ANISOU 41 N PRO A 74 16617 7877 8949 1418 1159 826 N
ATOM 42 CA PRO A 74 5.580 -23.978 11.328 1.00 86.14 C
ANISOU 42 CA PRO A 74 16277 7622 8829 1351 1220 766 C
ATOM 43 C PRO A 74 5.511 -22.772 10.408 1.00 86.35 C
ANISOU 43 C PRO A 74 15884 7876 9049 1315 1257 720 C
ATOM 44 O PRO A 74 5.781 -22.906 9.208 1.00 88.06 O
ANISOU 44 O PRO A 74 15965 8125 9368 1387 1238 671 O
ATOM 45 CB PRO A 74 4.229 -24.695 11.439 1.00 93.98 C
ANISOU 45 CB PRO A 74 17488 8446 9772 1012 1398 754 C
ATOM 46 CG PRO A 74 4.246 -25.281 12.807 1.00 93.13 C
ANISOU 46 CG PRO A 74 17727 8188 9473 1016 1373 818 C
ATOM 47 CD PRO A 74 4.919 -24.238 13.654 1.00 92.37 C
ANISOU 47 CD PRO A 74 17476 8253 9367 1173 1276 857 C
ATOM 48 N TRP A 75 5.148 -21.595 10.923 1.00 87.48 N
ANISOU 48 N TRP A 75 15823 8172 9245 1205 1311 734 N
ATOM 49 CA TRP A 75 5.325 -20.383 10.130 1.00 84.20 C
ANISOU 49 CA TRP A 75 15017 7973 9000 1232 1310 702 C
ATOM 50 C TRP A 75 6.798 -20.165 9.819 1.00 86.00 C
ANISOU 50 C TRP A 75 15105 8322 9249 1588 1123 699 C
ATOM 51 O TRP A 75 7.158 -19.800 8.693 1.00 86.44 O
ANISOU 51 O TRP A 75 14915 8493 9435 1665 1100 650 O
ATOM 52 CB TRP A 75 4.752 -19.167 10.862 1.00 80.52 C
ANISOU 52 CB TRP A 75 14375 7644 8574 1072 1385 721 C
ATOM 53 CG TRP A 75 3.305 -18.884 10.576 1.00 82.03 C
ANISOU 53 CG TRP A 75 14469 7843 8857 716 1572 673 C
ATOM 54 CD1 TRP A 75 2.294 -18.793 11.487 1.00 83.62 C
ANISOU 54 CD1 TRP A 75 14741 8018 9012 467 1685 669 C
ATOM 55 CD2 TRP A 75 2.710 -18.644 9.294 1.00 84.22 C
ANISOU 55 CD2 TRP A 75 14532 8177 9291 574 1656 604 C
ATOM 56 NE1 TRP A 75 1.107 -18.516 10.855 1.00 90.06 N
ANISOU 56 NE1 TRP A 75 15378 8888 9954 186 1825 592 N
ATOM 57 CE2 TRP A 75 1.335 -18.419 9.507 1.00 86.34 C
ANISOU 57 CE2 TRP A 75 14736 8463 9605 244 1807 554 C
ATOM 58 CE3 TRP A 75 3.205 -18.599 7.987 1.00 86.94 C
ANISOU 58 CE3 TRP A 75 14723 8568 9742 694 1611 570 C
ATOM 59 CZ2 TRP A 75 0.450 -18.155 8.464 1.00 84.16 C
ANISOU 59 CZ2 TRP A 75 14244 8256 9477 40 1900 469 C
ATOM 60 CZ3 TRP A 75 2.325 -18.337 6.953 1.00 84.90 C
ANISOU 60 CZ3 TRP A 75 14281 8355 9622 481 1718 499 C
ATOM 61 CH2 TRP A 75 0.963 -18.118 7.198 1.00 83.02 C
ANISOU 61 CH2 TRP A 75 13978 8141 9426 159 1854 448 C
ATOM 62 N ASP A 76 7.668 -20.397 10.805 1.00 83.45 N
ANISOU 62 N ASP A 76 14922 7985 8799 1803 983 739 N
ATOM 63 CA ASP A 76 9.099 -20.204 10.594 1.00 86.82 C
ANISOU 63 CA ASP A 76 15184 8557 9247 2135 793 713 C
ATOM 64 C ASP A 76 9.661 -21.238 9.628 1.00 94.10 C
ANISOU 64 C ASP A 76 16173 9400 10183 2289 727 660 C
ATOM 65 O ASP A 76 10.352 -20.888 8.665 1.00 95.19 O
ANISOU 65 O ASP A 76 16035 9695 10438 2426 665 596 O
ATOM 66 CB ASP A 76 9.837 -20.264 11.930 1.00 85.45 C
ANISOU 66 CB ASP A 76 15156 8384 8929 2314 655 756 C
ATOM 67 CG ASP A 76 9.551 -19.065 12.806 1.00 87.52 C
ANISOU 67 CG ASP A 76 15281 8779 9194 2217 686 795 C
ATOM 68 OD1 ASP A 76 8.398 -18.921 13.260 1.00 95.37 O
ANISOU 68 OD1 ASP A 76 16382 9688 10165 1944 841 829 O
ATOM 69 OD2 ASP A 76 10.481 -18.263 13.036 1.00 92.02 O
ANISOU 69 OD2 ASP A 76 15621 9550 9794 2406 556 780 O
ATOM 70 N VAL A 77 9.363 -22.520 9.853 1.00 84.08 N
ANISOU 70 N VAL A 77 15264 7887 8795 2258 744 679 N
ATOM 71 CA VAL A 77 9.936 -23.551 8.991 1.00 75.32 C
ANISOU 71 CA VAL A 77 14238 6688 7692 2420 672 627 C
ATOM 72 C VAL A 77 9.581 -23.275 7.540 1.00 73.63 C
ANISOU 72 C VAL A 77 13783 6552 7643 2316 761 561 C
ATOM 73 O VAL A 77 10.374 -23.551 6.632 1.00 78.98 O
ANISOU 73 O VAL A 77 14333 7289 8386 2501 678 492 O
ATOM 74 CB VAL A 77 9.473 -24.957 9.425 1.00 77.84 C
ANISOU 74 CB VAL A 77 15003 6712 7860 2355 700 662 C
ATOM 75 CG1 VAL A 77 9.693 -25.159 10.919 1.00 79.92 C
ANISOU 75 CG1 VAL A 77 15522 6892 7953 2422 627 732 C
ATOM 76 CG2 VAL A 77 8.021 -25.183 9.050 1.00 71.03 C
ANISOU 76 CG2 VAL A 77 14240 5726 7024 1998 906 666 C
ATOM 77 N LEU A 78 8.399 -22.707 7.296 1.00 72.18 N
ANISOU 77 N LEU A 78 13520 6375 7530 2018 930 569 N
ATOM 78 CA LEU A 78 8.047 -22.308 5.940 1.00 71.63 C
ANISOU 78 CA LEU A 78 13203 6395 7620 1915 1009 503 C
ATOM 79 C LEU A 78 9.037 -21.281 5.408 1.00 74.13 C
ANISOU 79 C LEU A 78 13139 6975 8053 2111 912 457 C
ATOM 80 O LEU A 78 9.507 -21.392 4.269 1.00 81.26 O
ANISOU 80 O LEU A 78 13880 7949 9046 2204 881 380 O
ATOM 81 CB LEU A 78 6.622 -21.755 5.916 1.00 68.84 C
ANISOU 81 CB LEU A 78 12806 6028 7322 1564 1195 514 C
ATOM 82 CG LEU A 78 5.858 -21.901 4.598 1.00 74.27 C
ANISOU 82 CG LEU A 78 13402 6692 8125 1376 1305 443 C
ATOM 83 CD1 LEU A 78 4.394 -21.537 4.793 1.00 74.78 C
ANISOU 83 CD1 LEU A 78 13457 6733 8222 1015 1479 444 C
ATOM 84 CD2 LEU A 78 6.483 -21.051 3.504 1.00 72.74 C
ANISOU 84 CD2 LEU A 78 12856 6701 8079 1501 1258 381 C
ATOM 85 N LEU A 79 9.380 -20.280 6.221 1.00 76.81 N
ANISOU 85 N LEU A 79 13325 7470 8389 2167 863 495 N
ATOM 86 CA LEU A 79 10.352 -19.284 5.788 1.00 69.76 C
ANISOU 86 CA LEU A 79 12057 6846 7601 2336 767 446 C
ATOM 87 C LEU A 79 11.783 -19.794 5.913 1.00 73.05 C
ANISOU 87 C LEU A 79 12456 7332 7968 2647 583 403 C
ATOM 88 O LEU A 79 12.649 -19.380 5.134 1.00 67.28 O
ANISOU 88 O LEU A 79 11426 6803 7335 2776 514 323 O
ATOM 89 CB LEU A 79 10.173 -17.987 6.585 1.00 68.85 C
ANISOU 89 CB LEU A 79 11771 6881 7508 2269 782 494 C
ATOM 90 CG LEU A 79 10.838 -17.862 7.960 1.00 72.96 C
ANISOU 90 CG LEU A 79 12377 7436 7907 2420 661 543 C
ATOM 91 CD1 LEU A 79 12.267 -17.346 7.855 1.00 74.61 C
ANISOU 91 CD1 LEU A 79 12297 7893 8160 2672 492 482 C
ATOM 92 CD2 LEU A 79 10.015 -16.966 8.869 1.00 83.38 C
ANISOU 92 CD2 LEU A 79 13701 8770 9211 2237 751 613 C
ATOM 93 N CYS A 80 12.047 -20.692 6.866 1.00 86.30 N
ANISOU 93 N CYS A 80 14443 8849 9496 2757 506 446 N
ATOM 94 CA CYS A 80 13.414 -21.150 7.091 1.00 73.96 C
ANISOU 94 CA CYS A 80 12864 7353 7885 3059 322 400 C
ATOM 95 C CYS A 80 14.013 -21.725 5.817 1.00 81.52 C
ANISOU 95 C CYS A 80 13709 8341 8926 3180 290 300 C
ATOM 96 O CYS A 80 15.096 -21.315 5.385 1.00 82.91 O
ANISOU 96 O CYS A 80 13589 8737 9175 3350 192 217 O
ATOM 97 CB CYS A 80 13.444 -22.195 8.206 1.00 74.47 C
ANISOU 97 CB CYS A 80 13337 7190 7770 3141 258 461 C
ATOM 98 SG CYS A 80 12.909 -21.587 9.816 1.00 75.10 S
ANISOU 98 SG CYS A 80 13563 7241 7730 3025 279 564 S
ATOM 99 N VAL A 81 13.313 -22.671 5.194 1.00 66.10 N
ANISOU 99 N VAL A 81 11981 6173 6961 3079 379 297 N
ATOM 100 CA VAL A 81 13.824 -23.258 3.961 1.00 66.30 C
ANISOU 100 CA VAL A 81 11918 6213 7061 3187 357 196 C
ATOM 101 C VAL A 81 13.547 -22.348 2.769 1.00 67.53 C
ANISOU 101 C VAL A 81 11730 6551 7375 3049 454 134 C
ATOM 102 O VAL A 81 14.272 -22.395 1.769 1.00 68.41 O
ANISOU 102 O VAL A 81 11632 6789 7570 3162 418 30 O
ATOM 103 CB VAL A 81 13.233 -24.663 3.749 1.00 59.70 C
ANISOU 103 CB VAL A 81 11464 5073 6147 3139 404 209 C
ATOM 104 CG1 VAL A 81 13.825 -25.636 4.754 1.00 56.94 C
ANISOU 104 CG1 VAL A 81 11426 4564 5644 3341 273 245 C
ATOM 105 CG2 VAL A 81 11.716 -24.641 3.864 1.00 72.09 C
ANISOU 105 CG2 VAL A 81 13213 6480 7698 2810 578 280 C
ATOM 106 N SER A 82 12.515 -21.504 2.849 1.00 70.95 N
ANISOU 106 N SER A 82 12101 7006 7852 2804 578 187 N
ATOM 107 CA SER A 82 12.260 -20.560 1.766 1.00 72.96 C
ANISOU 107 CA SER A 82 12031 7440 8251 2678 660 129 C
ATOM 108 C SER A 82 13.428 -19.604 1.580 1.00 68.37 C
ANISOU 108 C SER A 82 11066 7167 7745 2826 561 67 C
ATOM 109 O SER A 82 13.680 -19.139 0.463 1.00 66.38 O
ANISOU 109 O SER A 82 10544 7079 7599 2799 590 -18 O
ATOM 110 CB SER A 82 10.977 -19.775 2.037 1.00 73.71 C
ANISOU 110 CB SER A 82 12127 7504 8375 2404 799 197 C
ATOM 111 OG SER A 82 9.858 -20.639 2.132 1.00 80.18 O
ANISOU 111 OG SER A 82 13272 8059 9135 2218 907 237 O
ATOM 112 N GLY A 83 14.146 -19.291 2.660 1.00 72.36 N
ANISOU 112 N GLY A 83 11544 7760 8191 2963 449 102 N
ATOM 113 CA GLY A 83 15.342 -18.479 2.523 1.00 72.82 C
ANISOU 113 CA GLY A 83 11246 8109 8315 3090 349 32 C
ATOM 114 C GLY A 83 16.405 -19.160 1.685 1.00 75.37 C
ANISOU 114 C GLY A 83 11478 8494 8666 3274 278 -83 C
ATOM 115 O GLY A 83 17.103 -18.513 0.901 1.00 75.69 O
ANISOU 115 O GLY A 83 11186 8769 8802 3282 270 -171 O
ATOM 116 N THR A 84 16.544 -20.479 1.841 1.00 68.48 N
ANISOU 116 N THR A 84 10904 7409 7706 3416 230 -85 N
ATOM 117 CA THR A 84 17.482 -21.219 1.004 1.00 74.05 C
ANISOU 117 CA THR A 84 11546 8149 8440 3598 172 -202 C
ATOM 118 C THR A 84 17.104 -21.101 -0.466 1.00 68.30 C
ANISOU 118 C THR A 84 10665 7468 7819 3465 291 -278 C
ATOM 119 O THR A 84 17.969 -20.891 -1.324 1.00 69.46 O
ANISOU 119 O THR A 84 10545 7807 8041 3539 275 -391 O
ATOM 120 CB THR A 84 17.522 -22.688 1.430 1.00 74.98 C
ANISOU 120 CB THR A 84 12053 7993 8442 3754 108 -182 C
ATOM 121 OG1 THR A 84 17.910 -22.781 2.807 1.00 79.65 O
ANISOU 121 OG1 THR A 84 12793 8547 8922 3882 -10 -116 O
ATOM 122 CG2 THR A 84 18.510 -23.472 0.574 1.00 73.23 C
ANISOU 122 CG2 THR A 84 11765 7804 8255 3962 46 -312 C
ATOM 123 N VAL A 85 15.812 -21.221 -0.775 1.00 86.65 N
ANISOU 123 N VAL A 85 13155 9623 10144 3256 416 -226 N
ATOM 124 CA VAL A 85 15.363 -21.058 -2.154 1.00 83.01 C
ANISOU 124 CA VAL A 85 12559 9207 9775 3115 528 -301 C
ATOM 125 C VAL A 85 15.704 -19.662 -2.654 1.00 90.18 C
ANISOU 125 C VAL A 85 13061 10420 10783 3026 553 -342 C
ATOM 126 O VAL A 85 16.348 -19.493 -3.696 1.00 89.99 O
ANISOU 126 O VAL A 85 12807 10560 10824 3054 565 -451 O
ATOM 127 CB VAL A 85 13.853 -21.334 -2.261 1.00 78.99 C
ANISOU 127 CB VAL A 85 12296 8469 9246 2883 656 -235 C
ATOM 128 CG1 VAL A 85 13.346 -20.985 -3.653 1.00 61.75 C
ANISOU 128 CG1 VAL A 85 9948 6361 7153 2722 766 -316 C
ATOM 129 CG2 VAL A 85 13.556 -22.780 -1.924 1.00 80.91 C
ANISOU 129 CG2 VAL A 85 12943 8410 9391 2941 641 -207 C
ATOM 130 N ILE A 86 15.309 -18.640 -1.894 1.00 79.23 N
ANISOU 130 N ILE A 86 11588 9113 9404 2912 563 -257 N
ATOM 131 CA ILE A 86 15.541 -17.265 -2.323 1.00 79.88 C
ANISOU 131 CA ILE A 86 11304 9468 9577 2797 587 -285 C
ATOM 132 C ILE A 86 17.031 -17.000 -2.465 1.00 83.68 C
ANISOU 132 C ILE A 86 11526 10180 10087 2950 490 -371 C
ATOM 133 O ILE A 86 17.476 -16.362 -3.427 1.00 84.54 O
ANISOU 133 O ILE A 86 11363 10488 10272 2878 527 -450 O
ATOM 134 CB ILE A 86 14.883 -16.286 -1.337 1.00 70.60 C
ANISOU 134 CB ILE A 86 10109 8317 8398 2668 602 -178 C
ATOM 135 CG1 ILE A 86 13.365 -16.465 -1.373 1.00 79.79 C
ANISOU 135 CG1 ILE A 86 11493 9271 9552 2481 728 -111 C
ATOM 136 CG2 ILE A 86 15.280 -14.855 -1.672 1.00 68.99 C
ANISOU 136 CG2 ILE A 86 9531 8397 8284 2560 602 -206 C
ATOM 137 CD1 ILE A 86 12.634 -15.720 -0.286 1.00 75.58 C
ANISOU 137 CD1 ILE A 86 11004 8711 9002 2371 757 -6 C
ATOM 138 N ALA A 87 17.826 -17.474 -1.506 1.00 84.62 N
ANISOU 138 N ALA A 87 11736 10276 10140 3150 370 -360 N
ATOM 139 CA ALA A 87 19.270 -17.326 -1.617 1.00 76.49 C
ANISOU 139 CA ALA A 87 10474 9455 9135 3304 279 -455 C
ATOM 140 C ALA A 87 19.802 -18.069 -2.834 1.00 73.11 C
ANISOU 140 C ALA A 87 10000 9038 8739 3390 308 -577 C
ATOM 141 O ALA A 87 20.652 -17.551 -3.567 1.00 64.46 O
ANISOU 141 O ALA A 87 8621 8163 7708 3381 320 -671 O
ATOM 142 CB ALA A 87 19.945 -17.830 -0.343 1.00 72.02 C
ANISOU 142 CB ALA A 87 10051 8836 8477 3519 136 -427 C
ATOM 143 N GLY A 88 19.300 -19.281 -3.075 1.00 71.87 N
ANISOU 143 N GLY A 88 10133 8640 8536 3460 329 -579 N
ATOM 144 CA GLY A 88 19.814 -20.072 -4.180 1.00 81.65 C
ANISOU 144 CA GLY A 88 11351 9874 9799 3560 353 -703 C
ATOM 145 C GLY A 88 19.464 -19.482 -5.533 1.00 75.33 C
ANISOU 145 C GLY A 88 10352 9194 9077 3367 484 -767 C
ATOM 146 O GLY A 88 20.343 -19.245 -6.367 1.00 79.98 O
ANISOU 146 O GLY A 88 10701 9975 9715 3397 504 -877 O
ATOM 147 N GLU A 89 18.176 -19.224 -5.767 1.00 70.17 N
ANISOU 147 N GLU A 89 9800 8433 8430 3160 580 -702 N
ATOM 148 CA GLU A 89 17.757 -18.763 -7.087 1.00 66.86 C
ANISOU 148 CA GLU A 89 9231 8107 8066 2981 699 -767 C
ATOM 149 C GLU A 89 18.396 -17.423 -7.426 1.00 63.10 C
ANISOU 149 C GLU A 89 8395 7928 7652 2876 714 -792 C
ATOM 150 O GLU A 89 18.894 -17.229 -8.542 1.00 63.11 O
ANISOU 150 O GLU A 89 8219 8075 7687 2838 775 -891 O
ATOM 151 CB GLU A 89 16.231 -18.667 -7.155 1.00 64.74 C
ANISOU 151 CB GLU A 89 9136 7675 7787 2778 785 -691 C
ATOM 152 CG GLU A 89 15.487 -19.904 -6.646 1.00 75.38 C
ANISOU 152 CG GLU A 89 10873 8703 9066 2829 779 -640 C
ATOM 153 CD GLU A 89 16.207 -21.210 -6.948 1.00 79.72 C
ANISOU 153 CD GLU A 89 11570 9140 9582 3041 729 -726 C
ATOM 154 OE1 GLU A 89 16.783 -21.343 -8.050 1.00 73.23 O
ANISOU 154 OE1 GLU A 89 10597 8431 8795 3080 761 -851 O
ATOM 155 OE2 GLU A 89 16.201 -22.107 -6.078 1.00 76.86 O
ANISOU 155 OE2 GLU A 89 11481 8571 9150 3167 660 -671 O
ATOM 156 N ASN A 90 18.410 -16.491 -6.473 1.00 71.50 N
ANISOU 156 N ASN A 90 9363 9079 8726 2819 665 -704 N
ATOM 157 CA ASN A 90 19.051 -15.205 -6.721 1.00 66.01 C
ANISOU 157 CA ASN A 90 8349 8645 8087 2703 672 -720 C
ATOM 158 C ASN A 90 20.542 -15.378 -6.971 1.00 59.38 C
ANISOU 158 C ASN A 90 7339 7965 7257 2859 624 -824 C
ATOM 159 O ASN A 90 21.114 -14.717 -7.845 1.00 54.33 O
ANISOU 159 O ASN A 90 6472 7513 6657 2763 681 -888 O
ATOM 160 CB ASN A 90 18.799 -14.260 -5.547 1.00 66.06 C
ANISOU 160 CB ASN A 90 8312 8690 8098 2626 618 -612 C
ATOM 161 CG ASN A 90 17.375 -13.740 -5.516 1.00 64.46 C
ANISOU 161 CG ASN A 90 8188 8397 7906 2425 690 -524 C
ATOM 162 OD1 ASN A 90 17.069 -12.703 -6.105 1.00 60.44 O
ANISOU 162 OD1 ASN A 90 7505 8010 7447 2227 746 -518 O
ATOM 163 ND2 ASN A 90 16.494 -14.462 -4.834 1.00 68.07 N
ANISOU 163 ND2 ASN A 90 8922 8630 8311 2469 690 -455 N
ATOM 164 N ALA A 91 21.191 -16.268 -6.215 1.00 60.47 N
ANISOU 164 N ALA A 91 7595 8029 7351 3099 521 -843 N
ATOM 165 CA ALA A 91 22.604 -16.543 -6.454 1.00 64.94 C
ANISOU 165 CA ALA A 91 8006 8745 7925 3272 471 -957 C
ATOM 166 C ALA A 91 22.842 -17.024 -7.877 1.00 58.81 C
ANISOU 166 C ALA A 91 7174 8001 7168 3274 569 -1077 C
ATOM 167 O ALA A 91 23.921 -16.798 -8.438 1.00 48.08 O
ANISOU 167 O ALA A 91 5598 6835 5834 3316 582 -1177 O
ATOM 168 CB ALA A 91 23.117 -17.579 -5.455 1.00 70.04 C
ANISOU 168 CB ALA A 91 8835 9269 8509 3547 336 -961 C
ATOM 169 N LEU A 92 21.856 -17.697 -8.471 1.00 55.26 N
ANISOU 169 N LEU A 92 6926 7366 6703 3227 641 -1074 N
ATOM 170 CA LEU A 92 21.975 -18.101 -9.867 1.00 59.84 C
ANISOU 170 CA LEU A 92 7465 7977 7296 3206 746 -1190 C
ATOM 171 C LEU A 92 21.844 -16.903 -10.798 1.00 54.74 C
ANISOU 171 C LEU A 92 6593 7522 6684 2956 857 -1196 C
ATOM 172 O LEU A 92 22.627 -16.755 -11.744 1.00 60.61 O
ANISOU 172 O LEU A 92 7165 8426 7437 2949 922 -1296 O
ATOM 173 CB LEU A 92 20.918 -19.155 -10.197 1.00 62.03 C
ANISOU 173 CB LEU A 92 8039 7991 7538 3213 786 -1189 C
ATOM 174 CG LEU A 92 20.709 -19.473 -11.680 1.00 59.14 C
ANISOU 174 CG LEU A 92 7661 7635 7174 3134 910 -1300 C
ATOM 175 CD1 LEU A 92 22.009 -19.918 -12.330 1.00 52.34 C
ANISOU 175 CD1 LEU A 92 6661 6907 6321 3302 917 -1444 C
ATOM 176 CD2 LEU A 92 19.634 -20.536 -11.845 1.00 53.66 C
ANISOU 176 CD2 LEU A 92 7285 6660 6442 3136 932 -1296 C
ATOM 177 N VAL A 93 20.864 -16.036 -10.545 1.00 51.51 N
ANISOU 177 N VAL A 93 6191 7094 6287 2749 882 -1087 N
ATOM 178 CA VAL A 93 20.635 -14.900 -11.432 1.00 56.59 C
ANISOU 178 CA VAL A 93 6658 7892 6953 2506 979 -1079 C
ATOM 179 C VAL A 93 21.850 -13.980 -11.442 1.00 59.30 C
ANISOU 179 C VAL A 93 6736 8473 7322 2483 963 -1101 C
ATOM 180 O VAL A 93 22.313 -13.547 -12.504 1.00 65.82 O
ANISOU 180 O VAL A 93 7417 9445 8146 2388 1049 -1161 O
ATOM 181 CB VAL A 93 19.361 -14.145 -11.017 1.00 55.36 C
ANISOU 181 CB VAL A 93 6563 7664 6807 2311 987 -957 C
ATOM 182 CG1 VAL A 93 19.187 -12.893 -11.862 1.00 53.79 C
ANISOU 182 CG1 VAL A 93 6189 7621 6628 2067 1065 -936 C
ATOM 183 CG2 VAL A 93 18.150 -15.053 -11.144 1.00 52.26 C
ANISOU 183 CG2 VAL A 93 6430 7044 6381 2313 1018 -949 C
ATOM 184 N VAL A 94 22.393 -13.678 -10.261 1.00 58.60 N
ANISOU 184 N VAL A 94 6592 8425 7247 2566 855 -1055 N
ATOM 185 CA VAL A 94 23.532 -12.768 -10.199 1.00 53.13 C
ANISOU 185 CA VAL A 94 5654 7954 6577 2531 835 -1080 C
ATOM 186 C VAL A 94 24.683 -13.315 -11.026 1.00 61.26 C
ANISOU 186 C VAL A 94 6571 9109 7597 2662 871 -1223 C
ATOM 187 O VAL A 94 25.436 -12.551 -11.643 1.00 65.35 O
ANISOU 187 O VAL A 94 6887 9821 8123 2563 924 -1267 O
ATOM 188 CB VAL A 94 23.958 -12.527 -8.736 1.00 56.96 C
ANISOU 188 CB VAL A 94 6121 8452 7067 2630 702 -1028 C
ATOM 189 CG1 VAL A 94 25.031 -11.447 -8.662 1.00 49.76 C
ANISOU 189 CG1 VAL A 94 4960 7768 6181 2555 685 -1053 C
ATOM 190 CG2 VAL A 94 22.760 -12.147 -7.886 1.00 67.01 C
ANISOU 190 CG2 VAL A 94 7534 9586 8342 2524 672 -895 C
ATOM 191 N ALA A 95 24.838 -14.639 -11.060 1.00 61.79 N
ANISOU 191 N ALA A 95 6774 9063 7642 2885 846 -1300 N
ATOM 192 CA ALA A 95 25.914 -15.236 -11.841 1.00 64.65 C
ANISOU 192 CA ALA A 95 7032 9537 7995 3029 881 -1449 C
ATOM 193 C ALA A 95 25.711 -15.008 -13.335 1.00 67.61 C
ANISOU 193 C ALA A 95 7352 9982 8356 2867 1036 -1503 C
ATOM 194 O ALA A 95 26.657 -14.650 -14.046 1.00 73.54 O
ANISOU 194 O ALA A 95 7908 10931 9102 2845 1096 -1591 O
ATOM 195 CB ALA A 95 26.014 -16.730 -11.535 1.00 66.31 C
ANISOU 195 CB ALA A 95 7435 9576 8183 3305 811 -1513 C
ATOM 196 N LEU A 96 24.485 -15.204 -13.829 1.00 64.26 N
ANISOU 196 N LEU A 96 7099 9402 7913 2748 1104 -1456 N
ATOM 197 CA LEU A 96 24.247 -15.085 -15.265 1.00 66.20 C
ANISOU 197 CA LEU A 96 7324 9702 8126 2606 1247 -1512 C
ATOM 198 C LEU A 96 24.533 -13.673 -15.758 1.00 63.92 C
ANISOU 198 C LEU A 96 6837 9616 7834 2380 1307 -1467 C
ATOM 199 O LEU A 96 25.134 -13.491 -16.822 1.00 70.49 O
ANISOU 199 O LEU A 96 7555 10596 8630 2329 1404 -1547 O
ATOM 200 CB LEU A 96 22.810 -15.484 -15.602 1.00 70.68 C
ANISOU 200 CB LEU A 96 8117 10070 8670 2509 1293 -1469 C
ATOM 201 CG LEU A 96 22.464 -16.974 -15.528 1.00 64.55 C
ANISOU 201 CG LEU A 96 7571 9076 7878 2701 1268 -1537 C
ATOM 202 CD1 LEU A 96 21.037 -17.204 -15.986 1.00 55.87 C
ANISOU 202 CD1 LEU A 96 6672 7808 6750 2558 1326 -1505 C
ATOM 203 CD2 LEU A 96 23.421 -17.803 -16.362 1.00 52.25 C
ANISOU 203 CD2 LEU A 96 5973 7579 6300 2861 1319 -1696 C
ATOM 204 N ILE A 97 24.106 -12.661 -15.003 1.00 59.45 N
ANISOU 204 N ILE A 97 6238 9053 7298 2239 1252 -1339 N
ATOM 205 CA ILE A 97 24.397 -11.285 -15.389 1.00 62.35 C
ANISOU 205 CA ILE A 97 6437 9589 7662 2026 1293 -1289 C
ATOM 206 C ILE A 97 25.902 -11.056 -15.413 1.00 65.98 C
ANISOU 206 C ILE A 97 6683 10259 8127 2104 1284 -1381 C
ATOM 207 O ILE A 97 26.436 -10.416 -16.328 1.00 62.31 O
ANISOU 207 O ILE A 97 6088 9958 7630 1980 1369 -1418 O
ATOM 208 CB ILE A 97 23.685 -10.300 -14.442 1.00 68.37 C
ANISOU 208 CB ILE A 97 7218 10295 8465 1886 1219 -1143 C
ATOM 209 CG1 ILE A 97 22.218 -10.121 -14.851 1.00 64.18 C
ANISOU 209 CG1 ILE A 97 6839 9627 7919 1726 1265 -1060 C
ATOM 210 CG2 ILE A 97 24.396 -8.953 -14.429 1.00 64.13 C
ANISOU 210 CG2 ILE A 97 6493 9933 7940 1736 1215 -1108 C
ATOM 211 CD1 ILE A 97 21.364 -11.360 -14.673 1.00 66.47 C
ANISOU 211 CD1 ILE A 97 7336 9721 8201 1849 1259 -1085 C
ATOM 212 N ALA A 98 26.610 -11.578 -14.409 1.00 63.40 N
ANISOU 212 N ALA A 98 6321 9936 7832 2312 1179 -1423 N
ATOM 213 CA ALA A 98 28.056 -11.395 -14.343 1.00 64.84 C
ANISOU 213 CA ALA A 98 6288 10328 8021 2400 1158 -1526 C
ATOM 214 C ALA A 98 28.772 -12.199 -15.423 1.00 67.61 C
ANISOU 214 C ALA A 98 6581 10769 8337 2516 1248 -1683 C
ATOM 215 O ALA A 98 29.775 -11.740 -15.982 1.00 68.64 O
ANISOU 215 O ALA A 98 6513 11113 8453 2475 1303 -1769 O
ATOM 216 CB ALA A 98 28.568 -11.790 -12.958 1.00 59.40 C
ANISOU 216 CB ALA A 98 5592 9614 7363 2607 1008 -1533 C
ATOM 217 N SER A 99 28.276 -13.397 -15.731 1.00 62.03 N
ANISOU 217 N SER A 99 6050 9904 7616 2657 1266 -1729 N
ATOM 218 CA SER A 99 28.949 -14.311 -16.643 1.00 62.54 C
ANISOU 218 CA SER A 99 6082 10028 7651 2804 1339 -1890 C
ATOM 219 C SER A 99 28.406 -14.245 -18.066 1.00 67.05 C
ANISOU 219 C SER A 99 6709 10604 8163 2641 1496 -1911 C
ATOM 220 O SER A 99 28.780 -15.081 -18.894 1.00 72.98 O
ANISOU 220 O SER A 99 7474 11375 8882 2754 1570 -2044 O
ATOM 221 CB SER A 99 28.843 -15.744 -16.120 1.00 70.90 C
ANISOU 221 CB SER A 99 7315 10899 8723 3082 1256 -1946 C
ATOM 222 OG SER A 99 27.492 -16.161 -16.048 1.00 73.86 O
ANISOU 222 OG SER A 99 7943 11032 9090 3030 1259 -1856 O
ATOM 223 N THR A 100 27.539 -13.286 -18.370 1.00 81.02 N
ANISOU 223 N THR A 100 8518 12355 9911 2386 1543 -1787 N
ATOM 224 CA THR A 100 26.969 -13.144 -19.709 1.00 79.47 C
ANISOU 224 CA THR A 100 8389 12167 9640 2221 1679 -1794 C
ATOM 225 C THR A 100 27.190 -11.719 -20.198 1.00 91.79 C
ANISOU 225 C THR A 100 9803 13906 11167 1972 1733 -1729 C
ATOM 226 O THR A 100 26.592 -10.778 -19.638 1.00 87.03 O
ANISOU 226 O THR A 100 9215 13262 10590 1820 1677 -1589 O
ATOM 227 CB THR A 100 25.482 -13.486 -19.710 1.00 82.09 C
ANISOU 227 CB THR A 100 8962 12268 9959 2156 1678 -1709 C
ATOM 228 OG1 THR A 100 25.293 -14.810 -19.195 1.00 57.50 O
ANISOU 228 OG1 THR A 100 6000 8973 6875 2382 1621 -1769 O
ATOM 229 CG2 THR A 100 24.921 -13.414 -21.119 1.00 82.59 C
ANISOU 229 CG2 THR A 100 9104 12347 9929 2002 1810 -1729 C
ATOM 230 N PRO A 101 28.029 -11.504 -21.217 1.00 92.83 N
ANISOU 230 N PRO A 101 9800 14232 11239 1923 1837 -1827 N
ATOM 231 CA PRO A 101 28.234 -10.130 -21.701 1.00 89.23 C
ANISOU 231 CA PRO A 101 9225 13936 10741 1674 1886 -1762 C
ATOM 232 C PRO A 101 26.966 -9.494 -22.233 1.00 88.80 C
ANISOU 232 C PRO A 101 9326 13782 10633 1456 1915 -1628 C
ATOM 233 O PRO A 101 26.780 -8.280 -22.077 1.00100.46 O
ANISOU 233 O PRO A 101 10759 15300 12112 1266 1888 -1516 O
ATOM 234 CB PRO A 101 29.290 -10.302 -22.801 1.00102.46 C
ANISOU 234 CB PRO A 101 10761 15822 12348 1685 2009 -1916 C
ATOM 235 CG PRO A 101 29.116 -11.699 -23.274 1.00102.67 C
ANISOU 235 CG PRO A 101 10912 15748 12351 1875 2055 -2028 C
ATOM 236 CD PRO A 101 28.715 -12.494 -22.066 1.00107.42 C
ANISOU 236 CD PRO A 101 11621 16151 13043 2073 1926 -2000 C
ATOM 237 N ALA A 102 26.082 -10.280 -22.852 1.00 79.94 N
ANISOU 237 N ALA A 102 8388 12525 9460 1482 1962 -1642 N
ATOM 238 CA ALA A 102 24.839 -9.730 -23.377 1.00 80.66 C
ANISOU 238 CA ALA A 102 8627 12529 9492 1288 1978 -1525 C
ATOM 239 C ALA A 102 23.963 -9.152 -22.276 1.00 67.50 C
ANISOU 239 C ALA A 102 7020 10725 7904 1227 1864 -1376 C
ATOM 240 O ALA A 102 23.097 -8.319 -22.561 1.00 73.66 O
ANISOU 240 O ALA A 102 7864 11475 8649 1040 1855 -1263 O
ATOM 241 CB ALA A 102 24.068 -10.806 -24.141 1.00 85.13 C
ANISOU 241 CB ALA A 102 9386 12970 9988 1348 2041 -1587 C
ATOM 242 N LEU A 103 24.168 -9.573 -21.031 1.00 61.89 N
ANISOU 242 N LEU A 103 6290 9934 7292 1384 1771 -1376 N
ATOM 243 CA LEU A 103 23.414 -9.063 -19.897 1.00 61.29 C
ANISOU 243 CA LEU A 103 6263 9735 7291 1338 1665 -1246 C
ATOM 244 C LEU A 103 24.149 -7.950 -19.159 1.00 63.12 C
ANISOU 244 C LEU A 103 6328 10080 7575 1270 1600 -1190 C
ATOM 245 O LEU A 103 23.693 -7.520 -18.096 1.00 60.69 O
ANISOU 245 O LEU A 103 6045 9682 7332 1250 1506 -1095 O
ATOM 246 CB LEU A 103 23.086 -10.207 -18.935 1.00 66.96 C
ANISOU 246 CB LEU A 103 7091 10282 8069 1542 1597 -1273 C
ATOM 247 CG LEU A 103 22.308 -11.372 -19.556 1.00 67.65 C
ANISOU 247 CG LEU A 103 7369 10226 8111 1612 1654 -1337 C
ATOM 248 CD1 LEU A 103 22.102 -12.484 -18.542 1.00 64.85 C
ANISOU 248 CD1 LEU A 103 7128 9698 7814 1817 1576 -1368 C
ATOM 249 CD2 LEU A 103 20.969 -10.901 -20.111 1.00 66.95 C
ANISOU 249 CD2 LEU A 103 7406 10059 7972 1418 1685 -1248 C
ATOM 250 N ARG A 104 25.269 -7.468 -19.700 1.00 70.36 N
ANISOU 250 N ARG A 104 7081 11194 8459 1226 1652 -1256 N
ATOM 251 CA ARG A 104 26.020 -6.392 -19.068 1.00 77.14 C
ANISOU 251 CA ARG A 104 7783 12168 9359 1147 1599 -1220 C
ATOM 252 C ARG A 104 25.390 -5.025 -19.299 1.00 77.37 C
ANISOU 252 C ARG A 104 7840 12188 9369 899 1593 -1089 C
ATOM 253 O ARG A 104 25.875 -4.035 -18.742 1.00 86.39 O
ANISOU 253 O ARG A 104 8880 13398 10546 814 1545 -1048 O
ATOM 254 CB ARG A 104 27.465 -6.378 -19.579 1.00 79.09 C
ANISOU 254 CB ARG A 104 7837 12638 9576 1182 1664 -1353 C
ATOM 255 CG ARG A 104 28.448 -5.680 -18.640 1.00 80.77 C
ANISOU 255 CG ARG A 104 7876 12966 9845 1187 1591 -1363 C
ATOM 256 CD ARG A 104 29.690 -5.185 -19.372 1.00 84.13 C
ANISOU 256 CD ARG A 104 8105 13636 10225 1110 1677 -1469 C
ATOM 257 NE ARG A 104 29.377 -4.114 -20.311 1.00 91.24 N
ANISOU 257 NE ARG A 104 9026 14586 11053 851 1754 -1400 N
ATOM 258 CZ ARG A 104 29.183 -2.847 -19.969 1.00 85.47 C
ANISOU 258 CZ ARG A 104 8285 13856 10333 668 1711 -1297 C
ATOM 259 NH1 ARG A 104 29.259 -2.450 -18.709 1.00 84.57 N
ANISOU 259 NH1 ARG A 104 8132 13711 10291 704 1595 -1256 N
ATOM 260 NH2 ARG A 104 28.899 -1.956 -20.914 1.00 80.83 N
ANISOU 260 NH2 ARG A 104 7735 13308 9670 444 1780 -1241 N
ATOM 261 N THR A 105 24.327 -4.948 -20.096 1.00 59.19 N
ANISOU 261 N THR A 105 5676 9804 7009 788 1633 -1029 N
ATOM 262 CA THR A 105 23.693 -3.670 -20.364 1.00 53.57 C
ANISOU 262 CA THR A 105 5001 9079 6273 566 1615 -908 C
ATOM 263 C THR A 105 23.175 -3.065 -19.060 1.00 50.23 C
ANISOU 263 C THR A 105 4602 8536 5947 551 1498 -801 C
ATOM 264 O THR A 105 22.863 -3.792 -18.111 1.00 50.94 O
ANISOU 264 O THR A 105 4740 8512 6102 696 1439 -801 O
ATOM 265 CB THR A 105 22.543 -3.840 -21.358 1.00 52.80 C
ANISOU 265 CB THR A 105 5059 8907 6095 478 1658 -868 C
ATOM 266 OG1 THR A 105 21.913 -2.576 -21.598 1.00 61.43 O
ANISOU 266 OG1 THR A 105 6190 9986 7164 273 1623 -751 O
ATOM 267 CG2 THR A 105 21.508 -4.815 -20.826 1.00 58.86 C
ANISOU 267 CG2 THR A 105 5968 9494 6904 600 1618 -854 C
ATOM 268 N PRO A 106 23.073 -1.736 -18.981 1.00 46.21 N
ANISOU 268 N PRO A 106 4070 8045 5444 379 1463 -713 N
ATOM 269 CA PRO A 106 22.634 -1.117 -17.720 1.00 48.52 C
ANISOU 269 CA PRO A 106 4384 8225 5827 368 1354 -622 C
ATOM 270 C PRO A 106 21.341 -1.694 -17.172 1.00 43.66 C
ANISOU 270 C PRO A 106 3912 7424 5255 429 1303 -563 C
ATOM 271 O PRO A 106 21.203 -1.834 -15.951 1.00 39.44 O
ANISOU 271 O PRO A 106 3385 6802 4796 512 1227 -539 O
ATOM 272 CB PRO A 106 22.476 0.357 -18.107 1.00 51.53 C
ANISOU 272 CB PRO A 106 4757 8645 6177 155 1342 -544 C
ATOM 273 CG PRO A 106 23.471 0.556 -19.190 1.00 58.63 C
ANISOU 273 CG PRO A 106 5561 9724 6991 80 1441 -617 C
ATOM 274 CD PRO A 106 23.472 -0.723 -19.976 1.00 47.43 C
ANISOU 274 CD PRO A 106 4174 8326 5519 191 1522 -703 C
ATOM 275 N MET A 107 20.389 -2.040 -18.039 1.00 42.56 N
ANISOU 275 N MET A 107 3883 7228 5058 384 1343 -546 N
ATOM 276 CA MET A 107 19.129 -2.592 -17.557 1.00 46.22 C
ANISOU 276 CA MET A 107 4476 7527 5558 428 1304 -501 C
ATOM 277 C MET A 107 19.368 -3.840 -16.720 1.00 38.43 C
ANISOU 277 C MET A 107 3503 6480 4617 629 1295 -570 C
ATOM 278 O MET A 107 18.871 -3.954 -15.594 1.00 40.75 O
ANISOU 278 O MET A 107 3839 6663 4981 679 1226 -528 O
ATOM 279 CB MET A 107 18.211 -2.911 -18.736 1.00 56.37 C
ANISOU 279 CB MET A 107 5867 8793 6758 361 1359 -500 C
ATOM 280 CG MET A 107 16.897 -3.562 -18.332 1.00 50.08 C
ANISOU 280 CG MET A 107 5197 7842 5989 400 1332 -471 C
ATOM 281 SD MET A 107 16.084 -4.382 -19.711 1.00 56.69 S
ANISOU 281 SD MET A 107 6155 8677 6707 377 1412 -521 S
ATOM 282 CE MET A 107 14.892 -5.383 -18.822 1.00 66.34 C
ANISOU 282 CE MET A 107 7502 9717 7985 474 1389 -522 C
ATOM 283 N PHE A 108 20.124 -4.795 -17.259 1.00 46.87 N
ANISOU 283 N PHE A 108 4544 7622 5644 749 1362 -680 N
ATOM 284 CA PHE A 108 20.313 -6.065 -16.569 1.00 48.38 C
ANISOU 284 CA PHE A 108 4772 7743 5868 956 1347 -753 C
ATOM 285 C PHE A 108 21.310 -5.958 -15.422 1.00 49.62 C
ANISOU 285 C PHE A 108 4818 7949 6087 1062 1272 -769 C
ATOM 286 O PHE A 108 21.230 -6.737 -14.465 1.00 49.52 O
ANISOU 286 O PHE A 108 4858 7847 6112 1215 1216 -785 O
ATOM 287 CB PHE A 108 20.751 -7.137 -17.564 1.00 46.97 C
ANISOU 287 CB PHE A 108 4613 7610 5622 1061 1438 -875 C
ATOM 288 CG PHE A 108 19.625 -7.668 -18.401 1.00 49.59 C
ANISOU 288 CG PHE A 108 5102 7847 5894 1015 1497 -878 C
ATOM 289 CD1 PHE A 108 18.796 -8.663 -17.913 1.00 61.66 C
ANISOU 289 CD1 PHE A 108 6775 9210 7444 1116 1481 -896 C
ATOM 290 CD2 PHE A 108 19.384 -7.164 -19.666 1.00 53.84 C
ANISOU 290 CD2 PHE A 108 5650 8464 6343 866 1563 -867 C
ATOM 291 CE1 PHE A 108 17.754 -9.151 -18.675 1.00 65.56 C
ANISOU 291 CE1 PHE A 108 7414 9620 7876 1066 1536 -911 C
ATOM 292 CE2 PHE A 108 18.343 -7.649 -20.433 1.00 63.03 C
ANISOU 292 CE2 PHE A 108 6960 9552 7436 825 1607 -875 C
ATOM 293 CZ PHE A 108 17.528 -8.643 -19.937 1.00 62.86 C
ANISOU 293 CZ PHE A 108 7076 9367 7442 924 1596 -900 C
ATOM 294 N VAL A 109 22.251 -5.015 -15.493 1.00 48.56 N
ANISOU 294 N VAL A 109 4540 7959 5953 986 1268 -769 N
ATOM 295 CA VAL A 109 23.143 -4.793 -14.360 1.00 45.00 C
ANISOU 295 CA VAL A 109 3982 7561 5554 1069 1189 -783 C
ATOM 296 C VAL A 109 22.343 -4.337 -13.149 1.00 35.06 C
ANISOU 296 C VAL A 109 2795 6171 4353 1036 1095 -680 C
ATOM 297 O VAL A 109 22.561 -4.809 -12.026 1.00 32.68 O
ANISOU 297 O VAL A 109 2501 5832 4086 1175 1021 -690 O
ATOM 298 CB VAL A 109 24.241 -3.780 -14.732 1.00 50.93 C
ANISOU 298 CB VAL A 109 4568 8495 6288 964 1212 -809 C
ATOM 299 CG1 VAL A 109 25.058 -3.409 -13.505 1.00 36.56 C
ANISOU 299 CG1 VAL A 109 2636 6747 4508 1031 1118 -824 C
ATOM 300 CG2 VAL A 109 25.136 -4.350 -15.819 1.00 53.84 C
ANISOU 300 CG2 VAL A 109 4850 9011 6598 1019 1308 -932 C
ATOM 301 N LEU A 110 21.401 -3.414 -13.357 1.00 39.26 N
ANISOU 301 N LEU A 110 3389 6636 4894 857 1094 -582 N
ATOM 302 CA LEU A 110 20.547 -2.959 -12.264 1.00 39.20 C
ANISOU 302 CA LEU A 110 3451 6500 4942 818 1014 -492 C
ATOM 303 C LEU A 110 19.649 -4.081 -11.760 1.00 36.29 C
ANISOU 303 C LEU A 110 3212 5992 4583 933 1001 -494 C
ATOM 304 O LEU A 110 19.409 -4.199 -10.553 1.00 41.80 O
ANISOU 304 O LEU A 110 3947 6619 5317 997 930 -464 O
ATOM 305 CB LEU A 110 19.711 -1.767 -12.722 1.00 36.83 C
ANISOU 305 CB LEU A 110 3187 6165 4641 617 1013 -403 C
ATOM 306 CG LEU A 110 20.517 -0.520 -13.087 1.00 33.11 C
ANISOU 306 CG LEU A 110 2597 5844 4138 495 1009 -400 C
ATOM 307 CD1 LEU A 110 19.649 0.467 -13.844 1.00 36.73 C
ANISOU 307 CD1 LEU A 110 3117 6264 4576 315 1016 -322 C
ATOM 308 CD2 LEU A 110 21.100 0.120 -11.836 1.00 30.43 C
ANISOU 308 CD2 LEU A 110 2180 5549 3831 515 925 -393 C
ATOM 309 N VAL A 111 19.130 -4.906 -12.669 1.00 35.18 N
ANISOU 309 N VAL A 111 3152 5815 4402 957 1072 -532 N
ATOM 310 CA VAL A 111 18.351 -6.065 -12.248 1.00 35.86 C
ANISOU 310 CA VAL A 111 3370 5768 4486 1075 1069 -551 C
ATOM 311 C VAL A 111 19.211 -6.998 -11.408 1.00 35.18 C
ANISOU 311 C VAL A 111 3276 5686 4403 1294 1021 -614 C
ATOM 312 O VAL A 111 18.753 -7.550 -10.400 1.00 38.44 O
ANISOU 312 O VAL A 111 3787 5991 4828 1394 965 -591 O
ATOM 313 CB VAL A 111 17.762 -6.785 -13.474 1.00 40.35 C
ANISOU 313 CB VAL A 111 4028 6304 5000 1061 1161 -600 C
ATOM 314 CG1 VAL A 111 17.092 -8.077 -13.054 1.00 45.41 C
ANISOU 314 CG1 VAL A 111 4818 6803 5632 1198 1161 -640 C
ATOM 315 CG2 VAL A 111 16.772 -5.881 -14.191 1.00 48.23 C
ANISOU 315 CG2 VAL A 111 5051 7290 5984 857 1187 -525 C
ATOM 316 N GLY A 112 20.472 -7.186 -11.803 1.00 36.38 N
ANISOU 316 N GLY A 112 3318 5968 4537 1380 1037 -694 N
ATOM 317 CA GLY A 112 21.363 -8.014 -11.011 1.00 40.02 C
ANISOU 317 CA GLY A 112 3761 6445 4999 1602 974 -757 C
ATOM 318 C GLY A 112 21.511 -7.504 -9.592 1.00 36.60 C
ANISOU 318 C GLY A 112 3305 6004 4598 1625 868 -695 C
ATOM 319 O GLY A 112 21.549 -8.287 -8.640 1.00 38.38 O
ANISOU 319 O GLY A 112 3613 6155 4813 1799 797 -700 O
ATOM 320 N SER A 113 21.584 -6.181 -9.430 1.00 34.03 N
ANISOU 320 N SER A 113 2884 5746 4301 1453 853 -634 N
ATOM 321 CA SER A 113 21.664 -5.603 -8.093 1.00 30.82 C
ANISOU 321 CA SER A 113 2461 5329 3920 1456 759 -578 C
ATOM 322 C SER A 113 20.444 -5.975 -7.265 1.00 40.62 C
ANISOU 322 C SER A 113 3864 6404 5164 1477 725 -508 C
ATOM 323 O SER A 113 20.562 -6.293 -6.076 1.00 41.33 O
ANISOU 323 O SER A 113 4001 6460 5243 1601 646 -491 O
ATOM 324 CB SER A 113 21.798 -4.086 -8.187 1.00 32.75 C
ANISOU 324 CB SER A 113 2606 5643 4196 1251 760 -527 C
ATOM 325 OG SER A 113 21.647 -3.486 -6.915 1.00 32.73 O
ANISOU 325 OG SER A 113 2612 5608 4216 1235 677 -470 O
ATOM 326 N LEU A 114 19.258 -5.937 -7.877 1.00 41.58 N
ANISOU 326 N LEU A 114 4075 6431 5293 1358 785 -468 N
ATOM 327 CA LEU A 114 18.058 -6.383 -7.181 1.00 39.42 C
ANISOU 327 CA LEU A 114 3954 6008 5015 1378 769 -415 C
ATOM 328 C LEU A 114 18.186 -7.838 -6.752 1.00 40.62 C
ANISOU 328 C LEU A 114 4236 6077 5119 1611 749 -455 C
ATOM 329 O LEU A 114 17.810 -8.199 -5.631 1.00 42.21 O
ANISOU 329 O LEU A 114 4551 6187 5299 1704 695 -408 O
ATOM 330 CB LEU A 114 16.837 -6.191 -8.077 1.00 35.43 C
ANISOU 330 CB LEU A 114 3508 5436 4518 1220 842 -389 C
ATOM 331 CG LEU A 114 15.549 -6.859 -7.596 1.00 29.90 C
ANISOU 331 CG LEU A 114 2970 4588 3801 1247 852 -355 C
ATOM 332 CD1 LEU A 114 15.196 -6.410 -6.191 1.00 32.72 C
ANISOU 332 CD1 LEU A 114 3356 4902 4174 1247 785 -282 C
ATOM 333 CD2 LEU A 114 14.422 -6.549 -8.553 1.00 30.58 C
ANISOU 333 CD2 LEU A 114 3083 4641 3895 1077 918 -344 C
ATOM 334 N ALA A 115 18.720 -8.690 -7.630 1.00 36.40 N
ANISOU 334 N ALA A 115 3707 5563 4560 1714 792 -540 N
ATOM 335 CA ALA A 115 18.934 -10.083 -7.259 1.00 48.84 C
ANISOU 335 CA ALA A 115 5428 7038 6091 1949 760 -584 C
ATOM 336 C ALA A 115 19.875 -10.190 -6.067 1.00 45.44 C
ANISOU 336 C ALA A 115 4972 6650 5645 2114 651 -582 C
ATOM 337 O ALA A 115 19.629 -10.969 -5.139 1.00 47.00 O
ANISOU 337 O ALA A 115 5341 6718 5798 2267 591 -550 O
ATOM 338 CB ALA A 115 19.486 -10.863 -8.449 1.00 59.33 C
ANISOU 338 CB ALA A 115 6743 8399 7403 2027 822 -692 C
ATOM 339 N THR A 116 20.954 -9.403 -6.066 1.00 45.25 N
ANISOU 339 N THR A 116 4747 6801 5644 2083 622 -614 N
ATOM 340 CA THR A 116 21.838 -9.382 -4.906 1.00 50.37 C
ANISOU 340 CA THR A 116 5355 7510 6275 2224 512 -619 C
ATOM 341 C THR A 116 21.092 -8.891 -3.672 1.00 50.69 C
ANISOU 341 C THR A 116 5481 7471 6306 2174 458 -516 C
ATOM 342 O THR A 116 21.300 -9.401 -2.566 1.00 59.97 O
ANISOU 342 O THR A 116 6757 8596 7431 2341 369 -498 O
ATOM 343 CB THR A 116 23.060 -8.502 -5.187 1.00 47.49 C
ANISOU 343 CB THR A 116 4753 7351 5938 2165 504 -677 C
ATOM 344 OG1 THR A 116 23.711 -8.945 -6.386 1.00 45.47 O
ANISOU 344 OG1 THR A 116 4416 7176 5683 2204 571 -776 O
ATOM 345 CG2 THR A 116 24.054 -8.568 -4.033 1.00 43.42 C
ANISOU 345 CG2 THR A 116 4187 6913 5398 2329 385 -705 C
ATOM 346 N ALA A 117 20.215 -7.900 -3.842 1.00 47.37 N
ANISOU 346 N ALA A 117 5033 7039 5928 1950 508 -449 N
ATOM 347 CA ALA A 117 19.385 -7.453 -2.729 1.00 44.83 C
ANISOU 347 CA ALA A 117 4795 6639 5598 1898 472 -358 C
ATOM 348 C ALA A 117 18.424 -8.552 -2.295 1.00 40.65 C
ANISOU 348 C ALA A 117 4508 5923 5014 2014 482 -314 C
ATOM 349 O ALA A 117 18.290 -8.844 -1.101 1.00 41.07 O
ANISOU 349 O ALA A 117 4687 5904 5013 2125 421 -264 O
ATOM 350 CB ALA A 117 18.618 -6.191 -3.120 1.00 56.21 C
ANISOU 350 CB ALA A 117 6159 8096 7102 1638 523 -308 C
ATOM 351 N ASP A 118 17.736 -9.169 -3.256 1.00 40.26 N
ANISOU 351 N ASP A 118 4546 5782 4967 1986 565 -331 N
ATOM 352 CA ASP A 118 16.900 -10.318 -2.930 1.00 48.19 C
ANISOU 352 CA ASP A 118 5814 6583 5914 2098 586 -296 C
ATOM 353 C ASP A 118 17.739 -11.495 -2.456 1.00 50.54 C
ANISOU 353 C ASP A 118 6241 6817 6144 2356 510 -334 C
ATOM 354 O ASP A 118 17.249 -12.342 -1.700 1.00 54.70 O
ANISOU 354 O ASP A 118 7021 7161 6602 2470 491 -281 O
ATOM 355 CB ASP A 118 16.058 -10.716 -4.141 1.00 51.57 C
ANISOU 355 CB ASP A 118 6304 6933 6358 2005 691 -324 C
ATOM 356 CG ASP A 118 14.913 -9.755 -4.395 1.00 52.02 C
ANISOU 356 CG ASP A 118 6309 6997 6460 1774 756 -270 C
ATOM 357 OD1 ASP A 118 14.753 -8.799 -3.609 1.00 44.86 O
ANISOU 357 OD1 ASP A 118 5325 6143 5577 1687 721 -210 O
ATOM 358 OD2 ASP A 118 14.174 -9.956 -5.382 1.00 43.71 O
ANISOU 358 OD2 ASP A 118 5294 5899 5417 1679 837 -294 O
ATOM 359 N LEU A 119 18.999 -11.567 -2.886 1.00 50.04 N
ANISOU 359 N LEU A 119 6023 6895 6096 2446 469 -423 N
ATOM 360 CA LEU A 119 19.892 -12.601 -2.380 1.00 49.26 C
ANISOU 360 CA LEU A 119 6022 6756 5937 2703 378 -468 C
ATOM 361 C LEU A 119 20.132 -12.422 -0.887 1.00 47.02 C
ANISOU 361 C LEU A 119 5801 6465 5598 2797 271 -407 C
ATOM 362 O LEU A 119 20.023 -13.376 -0.109 1.00 57.45 O
ANISOU 362 O LEU A 119 7365 7627 6836 2968 211 -374 O
ATOM 363 CB LEU A 119 21.211 -12.566 -3.151 1.00 50.73 C
ANISOU 363 CB LEU A 119 5993 7125 6158 2767 365 -586 C
ATOM 364 CG LEU A 119 22.328 -13.491 -2.673 1.00 54.46 C
ANISOU 364 CG LEU A 119 6509 7604 6580 3039 258 -655 C
ATOM 365 CD1 LEU A 119 21.885 -14.945 -2.716 1.00 54.39 C
ANISOU 365 CD1 LEU A 119 6790 7365 6513 3207 250 -655 C
ATOM 366 CD2 LEU A 119 23.568 -13.272 -3.523 1.00 58.53 C
ANISOU 366 CD2 LEU A 119 6772 8326 7139 3066 269 -777 C
ATOM 367 N LEU A 120 20.446 -11.194 -0.465 1.00 48.02 N
ANISOU 367 N LEU A 120 5731 6753 5762 2678 246 -391 N
ATOM 368 CA LEU A 120 20.683 -10.945 0.952 1.00 47.81 C
ANISOU 368 CA LEU A 120 5752 6735 5679 2758 146 -343 C
ATOM 369 C LEU A 120 19.453 -11.264 1.788 1.00 55.25 C
ANISOU 369 C LEU A 120 6959 7476 6557 2751 165 -233 C
ATOM 370 O LEU A 120 19.578 -11.614 2.967 1.00 66.06 O
ANISOU 370 O LEU A 120 8486 8777 7839 2888 81 -191 O
ATOM 371 CB LEU A 120 21.106 -9.492 1.172 1.00 35.54 C
ANISOU 371 CB LEU A 120 3949 5371 4183 2596 132 -348 C
ATOM 372 CG LEU A 120 22.615 -9.242 1.200 1.00 46.51 C
ANISOU 372 CG LEU A 120 5138 6950 5584 2683 55 -444 C
ATOM 373 CD1 LEU A 120 23.248 -9.502 -0.158 1.00 50.21 C
ANISOU 373 CD1 LEU A 120 5472 7502 6103 2680 114 -539 C
ATOM 374 CD2 LEU A 120 22.910 -7.828 1.669 1.00 56.75 C
ANISOU 374 CD2 LEU A 120 6250 8389 6922 2521 36 -433 C
ATOM 375 N ALA A 121 18.260 -11.145 1.203 1.00 58.44 N
ANISOU 375 N ALA A 121 7425 7783 6996 2591 279 -186 N
ATOM 376 CA ALA A 121 17.050 -11.501 1.934 1.00 53.14 C
ANISOU 376 CA ALA A 121 7019 6907 6264 2574 322 -84 C
ATOM 377 C ALA A 121 17.049 -12.979 2.298 1.00 54.24 C
ANISOU 377 C ALA A 121 7477 6831 6300 2770 288 -70 C
ATOM 378 O ALA A 121 16.724 -13.346 3.433 1.00 46.78 O
ANISOU 378 O ALA A 121 6768 5747 5259 2842 254 6 O
ATOM 379 CB ALA A 121 15.816 -11.148 1.104 1.00 60.30 C
ANISOU 379 CB ALA A 121 7919 7757 7235 2367 456 -57 C
ATOM 380 N GLY A 122 17.418 -13.843 1.351 1.00 53.14 N
ANISOU 380 N GLY A 122 7365 6652 6173 2852 298 -143 N
ATOM 381 CA GLY A 122 17.477 -15.265 1.647 1.00 60.86 C
ANISOU 381 CA GLY A 122 8653 7415 7056 3035 256 -136 C
ATOM 382 C GLY A 122 18.564 -15.606 2.649 1.00 53.67 C
ANISOU 382 C GLY A 122 7783 6542 6066 3255 106 -151 C
ATOM 383 O GLY A 122 18.351 -16.406 3.563 1.00 50.21 O
ANISOU 383 O GLY A 122 7649 5912 5515 3365 56 -89 O
ATOM 384 N LEU A 123 19.746 -15.008 2.488 1.00 49.05 N
ANISOU 384 N LEU A 123 6903 6200 5533 3311 34 -236 N
ATOM 385 CA LEU A 123 20.832 -15.258 3.428 1.00 50.59 C
ANISOU 385 CA LEU A 123 7109 6455 5659 3521 -116 -267 C
ATOM 386 C LEU A 123 20.491 -14.733 4.815 1.00 56.43 C
ANISOU 386 C LEU A 123 7947 7170 6324 3499 -164 -175 C
ATOM 387 O LEU A 123 20.728 -15.416 5.818 1.00 62.99 O
ANISOU 387 O LEU A 123 9008 7886 7040 3669 -264 -145 O
ATOM 388 CB LEU A 123 22.119 -14.608 2.925 1.00 58.21 C
ANISOU 388 CB LEU A 123 7720 7694 6704 3547 -161 -384 C
ATOM 389 CG LEU A 123 22.556 -14.981 1.509 1.00 66.49 C
ANISOU 389 CG LEU A 123 8632 8803 7827 3556 -101 -487 C
ATOM 390 CD1 LEU A 123 23.831 -14.234 1.140 1.00 52.55 C
ANISOU 390 CD1 LEU A 123 6526 7313 6129 3556 -135 -595 C
ATOM 391 CD2 LEU A 123 22.749 -16.487 1.377 1.00 62.97 C
ANISOU 391 CD2 LEU A 123 8434 8176 7317 3782 -148 -522 C
ATOM 392 N GLY A 124 19.930 -13.526 4.891 1.00 67.08 N
ANISOU 392 N GLY A 124 9135 8620 7732 3292 -96 -132 N
ATOM 393 CA GLY A 124 19.695 -12.919 6.189 1.00 59.41 C
ANISOU 393 CA GLY A 124 8222 7655 6697 3271 -142 -61 C
ATOM 394 C GLY A 124 18.779 -13.754 7.060 1.00 55.80 C
ANISOU 394 C GLY A 124 8161 6927 6112 3318 -127 45 C
ATOM 395 O GLY A 124 19.096 -14.046 8.215 1.00 63.35 O
ANISOU 395 O GLY A 124 9284 7829 6955 3450 -228 74 O
ATOM 396 N LEU A 125 17.639 -14.175 6.508 1.00 60.97 N
ANISOU 396 N LEU A 125 8988 7400 6778 3199 2 99 N
ATOM 397 CA LEU A 125 16.701 -14.958 7.303 1.00 66.88 C
ANISOU 397 CA LEU A 125 10135 7874 7404 3193 42 202 C
ATOM 398 C LEU A 125 17.228 -16.363 7.560 1.00 70.25 C
ANISOU 398 C LEU A 125 10841 8131 7721 3400 -49 188 C
ATOM 399 O LEU A 125 16.885 -16.975 8.578 1.00 71.91 O
ANISOU 399 O LEU A 125 11378 8149 7795 3441 -74 263 O
ATOM 400 CB LEU A 125 15.336 -15.009 6.614 1.00 56.61 C
ANISOU 400 CB LEU A 125 8934 6424 6152 2983 216 252 C
ATOM 401 CG LEU A 125 15.191 -15.879 5.364 1.00 64.00 C
ANISOU 401 CG LEU A 125 9921 7260 7135 2979 275 200 C
ATOM 402 CD1 LEU A 125 15.037 -17.352 5.723 1.00 71.07 C
ANISOU 402 CD1 LEU A 125 11217 7881 7906 3079 254 232 C
ATOM 403 CD2 LEU A 125 14.009 -15.405 4.537 1.00 70.98 C
ANISOU 403 CD2 LEU A 125 10746 8110 8114 2742 439 217 C
ATOM 404 N ILE A 126 18.048 -16.895 6.652 1.00 61.65 N
ANISOU 404 N ILE A 126 9638 7103 6684 3524 -96 92 N
ATOM 405 CA ILE A 126 18.654 -18.202 6.883 1.00 65.52 C
ANISOU 405 CA ILE A 126 10374 7445 7077 3746 -200 67 C
ATOM 406 C ILE A 126 19.561 -18.148 8.104 1.00 72.90 C
ANISOU 406 C ILE A 126 11336 8446 7915 3930 -362 62 C
ATOM 407 O ILE A 126 19.461 -18.977 9.015 1.00 75.40 O
ANISOU 407 O ILE A 126 11992 8565 8092 4035 -425 119 O
ATOM 408 CB ILE A 126 19.420 -18.667 5.631 1.00 71.58 C
ANISOU 408 CB ILE A 126 10971 8295 7932 3849 -215 -51 C
ATOM 409 CG1 ILE A 126 18.455 -19.292 4.619 1.00 73.31 C
ANISOU 409 CG1 ILE A 126 11336 8332 8187 3722 -78 -38 C
ATOM 410 CG2 ILE A 126 20.535 -19.642 6.009 1.00 74.38 C
ANISOU 410 CG2 ILE A 126 11441 8614 8208 4135 -374 -113 C
ATOM 411 CD1 ILE A 126 17.883 -20.635 5.044 1.00 75.31 C
ANISOU 411 CD1 ILE A 126 12040 8261 8315 3773 -77 26 C
ATOM 412 N LEU A 127 20.458 -17.164 8.143 1.00 65.93 N
ANISOU 412 N LEU A 127 10103 7842 7104 3959 -430 -9 N
ATOM 413 CA LEU A 127 21.289 -16.975 9.321 1.00 64.98 C
ANISOU 413 CA LEU A 127 9983 7805 6901 4113 -582 -22 C
ATOM 414 C LEU A 127 20.471 -16.535 10.527 1.00 70.43 C
ANISOU 414 C LEU A 127 10861 8402 7496 4010 -560 92 C
ATOM 415 O LEU A 127 20.899 -16.750 11.665 1.00 71.71 O
ANISOU 415 O LEU A 127 11176 8529 7541 4148 -681 109 O
ATOM 416 CB LEU A 127 22.385 -15.954 9.021 1.00 64.11 C
ANISOU 416 CB LEU A 127 9443 8016 6898 4124 -639 -132 C
ATOM 417 CG LEU A 127 23.319 -16.347 7.875 1.00 54.28 C
ANISOU 417 CG LEU A 127 7995 6885 5741 4228 -659 -258 C
ATOM 418 CD1 LEU A 127 23.681 -15.133 7.039 1.00 59.69 C
ANISOU 418 CD1 LEU A 127 8266 7838 6573 4058 -591 -328 C
ATOM 419 CD2 LEU A 127 24.571 -17.011 8.418 1.00 55.72 C
ANISOU 419 CD2 LEU A 127 8209 7107 5856 4512 -836 -341 C
ATOM 420 N HIS A 128 19.302 -15.930 10.305 1.00 77.54 N
ANISOU 420 N HIS A 128 11758 9260 8443 3774 -408 165 N
ATOM 421 CA HIS A 128 18.450 -15.541 11.423 1.00 73.04 C
ANISOU 421 CA HIS A 128 11379 8592 7783 3666 -368 271 C
ATOM 422 C HIS A 128 17.926 -16.765 12.160 1.00 73.27 C
ANISOU 422 C HIS A 128 11876 8315 7648 3719 -371 352 C
ATOM 423 O HIS A 128 18.028 -16.852 13.388 1.00 80.48 O
ANISOU 423 O HIS A 128 12981 9165 8432 3785 -448 398 O
ATOM 424 CB HIS A 128 17.289 -14.682 10.927 1.00 68.16 C
ANISOU 424 CB HIS A 128 10652 7989 7259 3407 -196 322 C
ATOM 425 CG HIS A 128 16.324 -14.296 12.004 1.00 66.19 C
ANISOU 425 CG HIS A 128 10599 7629 6921 3280 -131 426 C
ATOM 426 ND1 HIS A 128 16.638 -13.391 12.995 1.00 72.01 N
ANISOU 426 ND1 HIS A 128 11230 8504 7625 3294 -204 434 N
ATOM 427 CD2 HIS A 128 15.054 -14.696 12.249 1.00 67.09 C
ANISOU 427 CD2 HIS A 128 11010 7508 6974 3120 7 520 C
ATOM 428 CE1 HIS A 128 15.601 -13.247 13.801 1.00 73.56 C
ANISOU 428 CE1 HIS A 128 11652 8557 7739 3160 -114 531 C
ATOM 429 NE2 HIS A 128 14.627 -14.028 13.371 1.00 73.42 N
ANISOU 429 NE2 HIS A 128 11878 8314 7706 3042 20 584 N
ATOM 430 N PHE A 129 17.354 -17.722 11.427 1.00 67.45 N
ANISOU 430 N PHE A 129 11337 7381 6911 3676 -284 369 N
ATOM 431 CA PHE A 129 16.904 -18.956 12.059 1.00 65.94 C
ANISOU 431 CA PHE A 129 11600 6890 6563 3708 -285 438 C
ATOM 432 C PHE A 129 18.078 -19.727 12.644 1.00 70.22 C
ANISOU 432 C PHE A 129 12262 7415 7004 3994 -480 394 C
ATOM 433 O PHE A 129 18.012 -20.209 13.781 1.00 66.79 O
ANISOU 433 O PHE A 129 12135 6826 6414 4051 -542 455 O
ATOM 434 CB PHE A 129 16.151 -19.820 11.049 1.00 74.60 C
ANISOU 434 CB PHE A 129 12855 7796 7692 3601 -159 446 C
ATOM 435 CG PHE A 129 16.070 -21.273 11.435 1.00 81.45 C
ANISOU 435 CG PHE A 129 14152 8379 8415 3689 -197 480 C
ATOM 436 CD1 PHE A 129 15.062 -21.729 12.267 1.00 74.11 C
ANISOU 436 CD1 PHE A 129 13592 7210 7356 3528 -109 579 C
ATOM 437 CD2 PHE A 129 17.006 -22.183 10.966 1.00 74.01 C
ANISOU 437 CD2 PHE A 129 13243 7412 7466 3925 -318 407 C
ATOM 438 CE1 PHE A 129 14.987 -23.063 12.622 1.00 74.80 C
ANISOU 438 CE1 PHE A 129 14084 7032 7305 3593 -143 610 C
ATOM 439 CE2 PHE A 129 16.936 -23.517 11.321 1.00 76.08 C
ANISOU 439 CE2 PHE A 129 13911 7403 7593 4012 -360 439 C
ATOM 440 CZ PHE A 129 15.925 -23.957 12.149 1.00 65.21 C
ANISOU 440 CZ PHE A 129 12910 5783 6082 3842 -274 543 C
ATOM 441 N VAL A 130 19.168 -19.844 11.883 1.00 70.04 N
ANISOU 441 N VAL A 130 11995 7549 7066 4174 -577 283 N
ATOM 442 CA VAL A 130 20.329 -20.586 12.358 1.00 68.53 C
ANISOU 442 CA VAL A 130 11894 7351 6792 4462 -767 225 C
ATOM 443 C VAL A 130 20.852 -19.984 13.651 1.00 70.66 C
ANISOU 443 C VAL A 130 12141 7727 6980 4546 -891 237 C
ATOM 444 O VAL A 130 21.430 -20.690 14.487 1.00 73.09 O
ANISOU 444 O VAL A 130 12676 7936 7158 4748 -1038 237 O
ATOM 445 CB VAL A 130 21.419 -20.616 11.269 1.00 67.55 C
ANISOU 445 CB VAL A 130 11445 7424 6795 4612 -831 87 C
ATOM 446 CG1 VAL A 130 22.709 -21.189 11.827 1.00 69.90 C
ANISOU 446 CG1 VAL A 130 11776 7763 7021 4918 -1038 10 C
ATOM 447 CG2 VAL A 130 20.948 -21.427 10.072 1.00 70.97 C
ANISOU 447 CG2 VAL A 130 11966 7714 7284 4564 -728 73 C
ATOM 448 N PHE A 131 20.659 -18.681 13.842 1.00 77.06 N
ANISOU 448 N PHE A 131 12685 8732 7861 4396 -840 244 N
ATOM 449 CA PHE A 131 21.117 -18.002 15.045 1.00 81.85 C
ANISOU 449 CA PHE A 131 13248 9453 8400 4455 -950 250 C
ATOM 450 C PHE A 131 19.995 -17.691 16.022 1.00 80.40 C
ANISOU 450 C PHE A 131 13308 9125 8115 4273 -859 375 C
ATOM 451 O PHE A 131 20.226 -17.696 17.234 1.00 74.90 O
ANISOU 451 O PHE A 131 12776 8391 7292 4355 -960 407 O
ATOM 452 CB PHE A 131 21.846 -16.707 14.669 1.00 79.82 C
ANISOU 452 CB PHE A 131 12507 9534 8287 4424 -976 155 C
ATOM 453 CG PHE A 131 23.201 -16.938 14.056 1.00 81.99 C
ANISOU 453 CG PHE A 131 12538 9982 8634 4625 -1098 17 C
ATOM 454 CD1 PHE A 131 23.333 -17.670 12.886 1.00 74.68 C
ANISOU 454 CD1 PHE A 131 11587 9011 7776 4671 -1057 -34 C
ATOM 455 CD2 PHE A 131 24.340 -16.426 14.649 1.00 81.57 C
ANISOU 455 CD2 PHE A 131 12279 10136 8578 4763 -1249 -68 C
ATOM 456 CE1 PHE A 131 24.574 -17.887 12.322 1.00 73.42 C
ANISOU 456 CE1 PHE A 131 11202 9013 7680 4853 -1159 -167 C
ATOM 457 CE2 PHE A 131 25.586 -16.641 14.088 1.00 74.36 C
ANISOU 457 CE2 PHE A 131 11136 9386 7731 4939 -1351 -204 C
ATOM 458 CZ PHE A 131 25.702 -17.371 12.924 1.00 71.19 C
ANISOU 458 CZ PHE A 131 10712 8940 7396 4985 -1303 -253 C
ATOM 459 N GLN A 132 18.780 -17.440 15.536 1.00 77.01 N
ANISOU 459 N GLN A 132 12913 8610 7737 4028 -670 441 N
ATOM 460 CA GLN A 132 17.648 -17.337 16.447 1.00 74.27 C
ANISOU 460 CA GLN A 132 12843 8093 7284 3845 -566 557 C
ATOM 461 C GLN A 132 17.450 -18.626 17.228 1.00 74.59 C
ANISOU 461 C GLN A 132 13357 7842 7140 3915 -604 621 C
ATOM 462 O GLN A 132 16.821 -18.606 18.291 1.00 79.71 O
ANISOU 462 O GLN A 132 14257 8363 7664 3809 -566 705 O
ATOM 463 CB GLN A 132 16.377 -16.986 15.673 1.00 77.02 C
ANISOU 463 CB GLN A 132 13153 8386 7726 3572 -350 603 C
ATOM 464 CG GLN A 132 15.138 -16.871 16.540 1.00 77.63 C
ANISOU 464 CG GLN A 132 13496 8293 7706 3348 -216 710 C
ATOM 465 CD GLN A 132 13.955 -16.298 15.786 1.00 76.36 C
ANISOU 465 CD GLN A 132 13223 8129 7660 3079 -11 738 C
ATOM 466 OE1 GLN A 132 13.917 -16.323 14.555 1.00 75.60 O
ANISOU 466 OE1 GLN A 132 12951 8079 7693 3056 43 692 O
ATOM 467 NE2 GLN A 132 12.983 -15.772 16.522 1.00 65.98 N
ANISOU 467 NE2 GLN A 132 12006 6762 6301 2870 106 807 N
ATOM 468 N TYR A 133 17.974 -19.742 16.722 1.00 77.25 N
ANISOU 468 N TYR A 133 13824 8071 7456 4083 -677 581 N
ATOM 469 CA TYR A 133 17.936 -21.033 17.401 1.00 87.51 C
ANISOU 469 CA TYR A 133 15577 9094 8581 4181 -738 632 C
ATOM 470 C TYR A 133 19.370 -21.522 17.574 1.00 77.61 C
ANISOU 470 C TYR A 133 14284 7913 7290 4517 -967 548 C
ATOM 471 O TYR A 133 20.008 -21.941 16.603 1.00 76.85 O
ANISOU 471 O TYR A 133 14042 7874 7281 4655 -1015 463 O
ATOM 472 CB TYR A 133 17.106 -22.044 16.606 1.00 84.59 C
ANISOU 472 CB TYR A 133 15446 8484 8209 4058 -602 663 C
ATOM 473 CG TYR A 133 15.667 -21.628 16.360 1.00 83.94 C
ANISOU 473 CG TYR A 133 15393 8329 8172 3717 -370 730 C
ATOM 474 CD1 TYR A 133 15.356 -20.623 15.449 1.00 78.95 C
ANISOU 474 CD1 TYR A 133 14393 7890 7714 3580 -264 696 C
ATOM 475 CD2 TYR A 133 14.618 -22.253 17.024 1.00 77.80 C
ANISOU 475 CD2 TYR A 133 15009 7290 7262 3523 -254 821 C
ATOM 476 CE1 TYR A 133 14.043 -20.246 15.218 1.00 73.05 C
ANISOU 476 CE1 TYR A 133 13666 7077 7012 3277 -58 749 C
ATOM 477 CE2 TYR A 133 13.302 -21.882 16.798 1.00 70.55 C
ANISOU 477 CE2 TYR A 133 14096 6319 6392 3200 -37 865 C
ATOM 478 CZ TYR A 133 13.021 -20.880 15.894 1.00 74.60 C
ANISOU 478 CZ TYR A 133 14238 7026 7083 3086 56 828 C
ATOM 479 OH TYR A 133 11.715 -20.509 15.667 1.00 64.13 O
ANISOU 479 OH TYR A 133 12908 5650 5810 2770 266 862 O
ATOM 480 N LEU A 134 19.869 -21.483 18.810 1.00 82.62 N
ANISOU 480 N LEU A 134 15052 8544 7795 4646 -1108 567 N
ATOM 481 CA LEU A 134 21.203 -21.980 19.150 1.00 82.96 C
ANISOU 481 CA LEU A 134 15097 8640 7784 4973 -1339 489 C
ATOM 482 C LEU A 134 22.292 -21.218 18.384 1.00 95.39 C
ANISOU 482 C LEU A 134 16167 10546 9529 5098 -1420 350 C
ATOM 483 O LEU A 134 23.006 -21.764 17.539 1.00 87.44 O
ANISOU 483 O LEU A 134 15050 9583 8591 5261 -1482 259 O
ATOM 484 CB LEU A 134 21.298 -23.486 18.879 1.00 88.13 C
ANISOU 484 CB LEU A 134 16103 9033 8351 5117 -1389 495 C
ATOM 485 N VAL A 135 22.398 -19.931 18.707 1.00 94.59 N
ANISOU 485 N VAL A 135 15766 10680 9494 5004 -1411 333 N
ATOM 486 CA VAL A 135 23.423 -19.060 18.127 1.00 91.59 C
ANISOU 486 CA VAL A 135 14902 10630 9267 5081 -1479 202 C
ATOM 487 C VAL A 135 24.536 -18.812 19.139 1.00 94.97 C
ANISOU 487 C VAL A 135 15264 11194 9627 5292 -1687 140 C
ATOM 488 O VAL A 135 24.354 -19.072 20.337 1.00 88.19 O
ANISOU 488 O VAL A 135 14709 10192 8607 5338 -1760 215 O
ATOM 489 CB VAL A 135 22.832 -17.719 17.671 1.00 81.12 C
ANISOU 489 CB VAL A 135 13251 9491 8080 4819 -1325 211 C
ATOM 490 N PRO A 136 25.700 -18.316 18.705 1.00 95.25 N
ANISOU 490 N PRO A 136 14911 11505 9776 5414 -1785 1 N
ATOM 491 CA PRO A 136 26.719 -17.902 19.685 1.00 98.18 C
ANISOU 491 CA PRO A 136 15176 12033 10094 5583 -1974 -66 C
ATOM 492 C PRO A 136 26.233 -16.821 20.635 1.00 99.95 C
ANISOU 492 C PRO A 136 15369 12326 10282 5415 -1942 0 C
ATOM 493 O PRO A 136 26.578 -16.844 21.824 1.00103.05 O
ANISOU 493 O PRO A 136 15915 12693 10546 5534 -2083 16 O
ATOM 494 CB PRO A 136 27.876 -17.409 18.801 1.00 86.23 C
ANISOU 494 CB PRO A 136 13199 10822 8744 5660 -2023 -230 C
ATOM 495 CG PRO A 136 27.257 -17.116 17.471 1.00 85.55 C
ANISOU 495 CG PRO A 136 12925 10774 8806 5447 -1826 -226 C
ATOM 496 CD PRO A 136 26.151 -18.110 17.320 1.00 85.95 C
ANISOU 496 CD PRO A 136 13376 10506 8774 5394 -1725 -105 C
ATOM 497 N SER A 137 25.438 -15.872 20.146 1.00 97.89 N
ANISOU 497 N SER A 137 14918 12149 10128 5148 -1767 36 N
ATOM 498 CA SER A 137 24.927 -14.789 20.979 1.00102.11 C
ANISOU 498 CA SER A 137 15406 12754 10638 4980 -1728 93 C
ATOM 499 C SER A 137 23.827 -14.057 20.220 1.00 92.53 C
ANISOU 499 C SER A 137 14062 11557 9537 4694 -1511 147 C
ATOM 500 O SER A 137 23.699 -14.186 18.999 1.00 87.23 O
ANISOU 500 O SER A 137 13244 10911 8988 4631 -1412 116 O
ATOM 501 CB SER A 137 26.043 -13.818 21.381 1.00 99.38 C
ANISOU 501 CB SER A 137 14714 12699 10346 5052 -1862 -22 C
ATOM 502 OG SER A 137 26.628 -13.212 20.242 1.00 96.46 O
ANISOU 502 OG SER A 137 13924 12566 10161 4994 -1817 -137 O
ATOM 503 N GLU A 138 23.027 -13.294 20.971 1.00 91.10 N
ANISOU 503 N GLU A 138 13944 11360 9310 4525 -1443 229 N
ATOM 504 CA GLU A 138 21.950 -12.506 20.378 1.00 88.09 C
ANISOU 504 CA GLU A 138 13442 11001 9028 4261 -1249 280 C
ATOM 505 C GLU A 138 22.464 -11.275 19.643 1.00 85.56 C
ANISOU 505 C GLU A 138 12642 10979 8888 4169 -1232 179 C
ATOM 506 O GLU A 138 21.809 -10.806 18.707 1.00 87.71 O
ANISOU 506 O GLU A 138 12761 11286 9281 3988 -1083 192 O
ATOM 507 CB GLU A 138 20.958 -12.081 21.460 1.00 95.01 C
ANISOU 507 CB GLU A 138 14540 11769 9790 4116 -1186 392 C
ATOM 508 CG GLU A 138 19.625 -11.559 20.927 1.00 90.72 C
ANISOU 508 CG GLU A 138 13981 11172 9316 3854 -973 466 C
ATOM 509 CD GLU A 138 19.675 -10.107 20.476 1.00 81.55 C
ANISOU 509 CD GLU A 138 12405 10272 8308 3721 -931 408 C
ATOM 510 OE1 GLU A 138 20.676 -9.416 20.762 1.00 85.49 O
ANISOU 510 OE1 GLU A 138 12648 10989 8844 3799 -1060 317 O
ATOM 511 OE2 GLU A 138 18.705 -9.656 19.832 1.00 73.47 O
ANISOU 511 OE2 GLU A 138 11316 9231 7367 3530 -769 451 O
ATOM 512 N THR A 139 23.611 -10.729 20.053 1.00 83.98 N
ANISOU 512 N THR A 139 12211 10989 8708 4275 -1378 78 N
ATOM 513 CA THR A 139 24.171 -9.588 19.337 1.00 76.04 C
ANISOU 513 CA THR A 139 10762 10257 7871 4164 -1355 -25 C
ATOM 514 C THR A 139 24.365 -9.909 17.862 1.00 85.48 C
ANISOU 514 C THR A 139 11784 11492 9202 4135 -1274 -79 C
ATOM 515 O THR A 139 24.178 -9.042 17.003 1.00 83.46 O
ANISOU 515 O THR A 139 11254 11369 9088 3946 -1166 -107 O
ATOM 516 CB THR A 139 25.496 -9.167 19.968 1.00 80.78 C
ANISOU 516 CB THR A 139 11170 11059 8466 4300 -1531 -137 C
ATOM 517 OG1 THR A 139 25.256 -8.628 21.274 1.00 82.19 O
ANISOU 517 OG1 THR A 139 11461 11230 8535 4284 -1593 -91 O
ATOM 518 CG2 THR A 139 26.195 -8.123 19.106 1.00 70.80 C
ANISOU 518 CG2 THR A 139 9463 10060 7378 4175 -1498 -253 C
ATOM 519 N VAL A 140 24.744 -11.149 17.548 1.00 84.10 N
ANISOU 519 N VAL A 140 11774 11197 8981 4320 -1328 -96 N
ATOM 520 CA VAL A 140 24.870 -11.545 16.149 1.00 78.29 C
ANISOU 520 CA VAL A 140 10905 10482 8361 4298 -1248 -144 C
ATOM 521 C VAL A 140 23.518 -11.458 15.456 1.00 75.25 C
ANISOU 521 C VAL A 140 10600 9967 8024 4085 -1058 -47 C
ATOM 522 O VAL A 140 23.417 -10.990 14.315 1.00 73.14 O
ANISOU 522 O VAL A 140 10091 9803 7897 3942 -954 -83 O
ATOM 523 CB VAL A 140 25.467 -12.960 16.039 1.00 92.35 C
ANISOU 523 CB VAL A 140 12887 12134 10067 4552 -1349 -177 C
ATOM 524 CG1 VAL A 140 25.620 -13.348 14.576 1.00 94.95 C
ANISOU 524 CG1 VAL A 140 13068 12492 10515 4530 -1266 -235 C
ATOM 525 CG2 VAL A 140 26.805 -13.037 16.760 1.00 91.37 C
ANISOU 525 CG2 VAL A 140 12680 12143 9894 4778 -1547 -279 C
ATOM 526 N SER A 141 22.457 -11.906 16.133 1.00 90.14 N
ANISOU 526 N SER A 141 12835 11622 9793 4054 -1008 75 N
ATOM 527 CA SER A 141 21.114 -11.779 15.576 1.00 88.40 C
ANISOU 527 CA SER A 141 12697 11277 9613 3846 -825 166 C
ATOM 528 C SER A 141 20.761 -10.325 15.290 1.00 86.46 C
ANISOU 528 C SER A 141 12142 11219 9490 3631 -739 156 C
ATOM 529 O SER A 141 19.913 -10.051 14.433 1.00 81.66 O
ANISOU 529 O SER A 141 11471 10583 8972 3461 -594 190 O
ATOM 530 CB SER A 141 20.086 -12.386 16.531 1.00 88.75 C
ANISOU 530 CB SER A 141 13168 11054 9500 3824 -782 294 C
ATOM 531 OG SER A 141 18.774 -12.266 16.009 1.00 84.25 O
ANISOU 531 OG SER A 141 12677 10362 8970 3615 -596 374 O
ATOM 532 N LEU A 142 21.386 -9.384 16.003 1.00 79.06 N
ANISOU 532 N LEU A 142 11018 10465 8556 3634 -829 108 N
ATOM 533 CA LEU A 142 21.188 -7.972 15.711 1.00 70.76 C
ANISOU 533 CA LEU A 142 9661 9599 7626 3431 -762 84 C
ATOM 534 C LEU A 142 21.907 -7.544 14.438 1.00 76.97 C
ANISOU 534 C LEU A 142 10104 10566 8575 3356 -735 -17 C
ATOM 535 O LEU A 142 21.548 -6.516 13.856 1.00 81.00 O
ANISOU 535 O LEU A 142 10394 11180 9202 3149 -644 -24 O
ATOM 536 CB LEU A 142 21.656 -7.132 16.901 1.00 66.93 C
ANISOU 536 CB LEU A 142 9105 9240 7087 3451 -869 58 C
ATOM 537 CG LEU A 142 21.499 -5.615 16.791 1.00 76.57 C
ANISOU 537 CG LEU A 142 10032 10643 8419 3243 -818 29 C
ATOM 538 CD1 LEU A 142 21.191 -5.014 18.159 1.00 73.33 C
ANISOU 538 CD1 LEU A 142 9723 10236 7902 3238 -872 68 C
ATOM 539 CD2 LEU A 142 22.750 -4.984 16.190 1.00 73.45 C
ANISOU 539 CD2 LEU A 142 9289 10473 8145 3214 -873 -100 C
ATOM 540 N LEU A 143 22.929 -8.288 14.008 1.00 80.90 N
ANISOU 540 N LEU A 143 10559 11101 9079 3515 -814 -97 N
ATOM 541 CA LEU A 143 23.511 -8.053 12.690 1.00 71.29 C
ANISOU 541 CA LEU A 143 9064 10020 8002 3437 -765 -183 C
ATOM 542 C LEU A 143 22.639 -8.635 11.585 1.00 73.64 C
ANISOU 542 C LEU A 143 9451 10179 8348 3360 -632 -133 C
ATOM 543 O LEU A 143 22.496 -8.028 10.518 1.00 69.31 O
ANISOU 543 O LEU A 143 8692 9717 7926 3182 -534 -158 O
ATOM 544 CB LEU A 143 24.917 -8.648 12.607 1.00 74.06 C
ANISOU 544 CB LEU A 143 9329 10469 8341 3645 -892 -295 C
ATOM 545 CG LEU A 143 26.025 -7.892 13.341 1.00 85.49 C
ANISOU 545 CG LEU A 143 10577 12115 9788 3690 -1013 -383 C
ATOM 546 CD1 LEU A 143 26.213 -8.449 14.737 1.00100.01 C
ANISOU 546 CD1 LEU A 143 12655 13870 11473 3901 -1158 -359 C
ATOM 547 CD2 LEU A 143 27.325 -7.950 12.556 1.00 83.78 C
ANISOU 547 CD2 LEU A 143 10108 12074 9651 3757 -1055 -517 C
ATOM 548 N THR A 144 22.054 -9.812 11.820 1.00 82.62 N
ANISOU 548 N THR A 144 10916 11092 9384 3482 -627 -64 N
ATOM 549 CA THR A 144 21.237 -10.446 10.791 1.00 88.17 C
ANISOU 549 CA THR A 144 11724 11651 10127 3415 -503 -24 C
ATOM 550 C THR A 144 20.032 -9.586 10.444 1.00 90.61 C
ANISOU 550 C THR A 144 11973 11944 10509 3169 -358 44 C
ATOM 551 O THR A 144 19.673 -9.451 9.269 1.00 95.92 O
ANISOU 551 O THR A 144 12525 12633 11287 3040 -256 30 O
ATOM 552 CB THR A 144 20.780 -11.831 11.252 1.00 97.05 C
ANISOU 552 CB THR A 144 13250 12508 11115 3566 -521 44 C
ATOM 553 OG1 THR A 144 19.942 -11.702 12.407 1.00 90.47 O
ANISOU 553 OG1 THR A 144 12657 11543 10173 3527 -507 148 O
ATOM 554 CG2 THR A 144 21.977 -12.711 11.587 1.00100.94 C
ANISOU 554 CG2 THR A 144 13809 13008 11536 3826 -678 -28 C
ATOM 555 N VAL A 145 19.393 -8.989 11.454 1.00 70.71 N
ANISOU 555 N VAL A 145 9538 9396 7932 3107 -349 115 N
ATOM 556 CA VAL A 145 18.273 -8.099 11.177 1.00 57.51 C
ANISOU 556 CA VAL A 145 7792 7725 6335 2887 -218 171 C
ATOM 557 C VAL A 145 18.727 -6.965 10.272 1.00 65.09 C
ANISOU 557 C VAL A 145 8379 8903 7451 2721 -195 94 C
ATOM 558 O VAL A 145 17.954 -6.474 9.440 1.00 71.00 O
ANISOU 558 O VAL A 145 9031 9647 8296 2540 -81 113 O
ATOM 559 CB VAL A 145 17.668 -7.575 12.493 1.00 54.77 C
ANISOU 559 CB VAL A 145 7577 7337 5897 2866 -225 245 C
ATOM 560 CG1 VAL A 145 18.506 -6.437 13.055 1.00 57.18 C
ANISOU 560 CG1 VAL A 145 7628 7867 6233 2844 -324 179 C
ATOM 561 CG2 VAL A 145 16.231 -7.140 12.277 1.00 48.83 C
ANISOU 561 CG2 VAL A 145 6878 6489 5185 2687 -67 328 C
ATOM 562 N GLY A 146 19.985 -6.540 10.406 1.00 64.40 N
ANISOU 562 N GLY A 146 8092 8993 7386 2770 -300 5 N
ATOM 563 CA GLY A 146 20.526 -5.560 9.481 1.00 56.48 C
ANISOU 563 CA GLY A 146 6776 8163 6520 2600 -271 -68 C
ATOM 564 C GLY A 146 20.568 -6.076 8.056 1.00 58.50 C
ANISOU 564 C GLY A 146 6978 8398 6852 2563 -198 -100 C
ATOM 565 O GLY A 146 20.327 -5.326 7.107 1.00 57.71 O
ANISOU 565 O GLY A 146 6713 8354 6862 2363 -116 -112 O
ATOM 566 N PHE A 147 20.875 -7.364 7.884 1.00 63.08 N
ANISOU 566 N PHE A 147 7712 8887 7370 2757 -231 -116 N
ATOM 567 CA PHE A 147 20.834 -7.954 6.551 1.00 59.43 C
ANISOU 567 CA PHE A 147 7223 8388 6968 2738 -158 -148 C
ATOM 568 C PHE A 147 19.436 -7.848 5.959 1.00 56.65 C
ANISOU 568 C PHE A 147 6951 7914 6660 2571 -25 -74 C
ATOM 569 O PHE A 147 19.267 -7.455 4.799 1.00 65.94 O
ANISOU 569 O PHE A 147 7982 9139 7934 2417 56 -101 O
ATOM 570 CB PHE A 147 21.289 -9.417 6.603 1.00 61.12 C
ANISOU 570 CB PHE A 147 7633 8492 7098 2988 -221 -173 C
ATOM 571 CG PHE A 147 22.743 -9.626 6.265 1.00 64.42 C
ANISOU 571 CG PHE A 147 7879 9061 7535 3119 -306 -290 C
ATOM 572 CD1 PHE A 147 23.677 -8.617 6.450 1.00 72.66 C
ANISOU 572 CD1 PHE A 147 8667 10314 8627 3060 -355 -356 C
ATOM 573 CD2 PHE A 147 23.174 -10.840 5.756 1.00 65.80 C
ANISOU 573 CD2 PHE A 147 8155 9165 7682 3302 -332 -339 C
ATOM 574 CE1 PHE A 147 25.007 -8.817 6.135 1.00 77.49 C
ANISOU 574 CE1 PHE A 147 9118 11069 9256 3182 -423 -470 C
ATOM 575 CE2 PHE A 147 24.504 -11.045 5.439 1.00 68.59 C
ANISOU 575 CE2 PHE A 147 8342 9665 8055 3434 -406 -456 C
ATOM 576 CZ PHE A 147 25.420 -10.033 5.629 1.00 76.24 C
ANISOU 576 CZ PHE A 147 9047 10850 9070 3374 -449 -523 C
ATOM 577 N LEU A 148 18.414 -8.182 6.750 1.00 65.43 N
ANISOU 577 N LEU A 148 8303 8863 7695 2595 4 19 N
ATOM 578 CA LEU A 148 17.043 -8.043 6.271 1.00 63.78 C
ANISOU 578 CA LEU A 148 8166 8540 7528 2436 138 85 C
ATOM 579 C LEU A 148 16.701 -6.581 6.012 1.00 46.24 C
ANISOU 579 C LEU A 148 5703 6453 5413 2204 184 82 C
ATOM 580 O LEU A 148 16.021 -6.257 5.032 1.00 41.40 O
ANISOU 580 O LEU A 148 5014 5829 4886 2039 277 83 O
ATOM 581 CB LEU A 148 16.065 -8.652 7.276 1.00 59.79 C
ANISOU 581 CB LEU A 148 7985 7823 6911 2501 173 185 C
ATOM 582 CG LEU A 148 16.069 -10.177 7.437 1.00 50.57 C
ANISOU 582 CG LEU A 148 7139 6443 5633 2676 155 208 C
ATOM 583 CD1 LEU A 148 16.015 -10.872 6.090 1.00 50.99 C
ANISOU 583 CD1 LEU A 148 7182 6443 5747 2661 216 161 C
ATOM 584 CD2 LEU A 148 17.274 -10.645 8.227 1.00 67.96 C
ANISOU 584 CD2 LEU A 148 9388 8690 7743 2890 -1 169 C
ATOM 585 N VAL A 149 17.152 -5.684 6.890 1.00 53.91 N
ANISOU 585 N VAL A 149 6567 7541 6377 2183 112 76 N
ATOM 586 CA VAL A 149 16.992 -4.256 6.635 1.00 58.24 C
ANISOU 586 CA VAL A 149 6896 8205 7029 1957 138 62 C
ATOM 587 C VAL A 149 17.778 -3.854 5.397 1.00 59.76 C
ANISOU 587 C VAL A 149 6884 8503 7319 1850 142 -14 C
ATOM 588 O VAL A 149 17.282 -3.114 4.538 1.00 55.54 O
ANISOU 588 O VAL A 149 6252 7975 6878 1648 208 -14 O
ATOM 589 CB VAL A 149 17.429 -3.440 7.865 1.00 56.45 C
ANISOU 589 CB VAL A 149 6613 8070 6765 1971 54 59 C
ATOM 590 CG1 VAL A 149 17.512 -1.962 7.516 1.00 53.16 C
ANISOU 590 CG1 VAL A 149 5980 7758 6461 1738 67 28 C
ATOM 591 CG2 VAL A 149 16.474 -3.664 9.019 1.00 55.38 C
ANISOU 591 CG2 VAL A 149 6684 7826 6534 2043 75 143 C
ATOM 592 N ALA A 150 19.019 -4.332 5.287 1.00 53.90 N
ANISOU 592 N ALA A 150 6088 7840 6551 1989 73 -81 N
ATOM 593 CA ALA A 150 19.849 -3.983 4.141 1.00 50.65 C
ANISOU 593 CA ALA A 150 5493 7533 6219 1904 90 -154 C
ATOM 594 C ALA A 150 19.246 -4.506 2.845 1.00 46.66 C
ANISOU 594 C ALA A 150 5022 6952 5755 1845 184 -152 C
ATOM 595 O ALA A 150 19.250 -3.809 1.824 1.00 48.78 O
ANISOU 595 O ALA A 150 5167 7264 6102 1671 240 -173 O
ATOM 596 CB ALA A 150 21.262 -4.531 4.334 1.00 54.82 C
ANISOU 596 CB ALA A 150 5962 8163 6704 2093 2 -233 C
ATOM 597 N SER A 151 18.721 -5.733 2.865 1.00 44.81 N
ANISOU 597 N SER A 151 4976 6589 5460 1989 204 -128 N
ATOM 598 CA SER A 151 18.118 -6.288 1.659 1.00 40.65 C
ANISOU 598 CA SER A 151 4494 5985 4966 1940 295 -134 C
ATOM 599 C SER A 151 16.931 -5.450 1.210 1.00 43.17 C
ANISOU 599 C SER A 151 4784 6266 5352 1709 377 -87 C
ATOM 600 O SER A 151 16.789 -5.146 0.020 1.00 42.30 O
ANISOU 600 O SER A 151 4587 6180 5304 1575 435 -116 O
ATOM 601 CB SER A 151 17.681 -7.731 1.905 1.00 49.89 C
ANISOU 601 CB SER A 151 5915 6988 6052 2130 304 -109 C
ATOM 602 OG SER A 151 16.634 -7.787 2.858 1.00 48.07 O
ANISOU 602 OG SER A 151 5865 6628 5771 2127 326 -19 O
ATOM 603 N PHE A 152 16.071 -5.059 2.151 1.00 46.50 N
ANISOU 603 N PHE A 152 5282 6629 5756 1665 382 -18 N
ATOM 604 CA PHE A 152 14.886 -4.291 1.792 1.00 35.17 C
ANISOU 604 CA PHE A 152 3822 5153 4386 1457 453 19 C
ATOM 605 C PHE A 152 15.266 -2.948 1.180 1.00 36.51 C
ANISOU 605 C PHE A 152 3802 5424 4647 1258 434 -17 C
ATOM 606 O PHE A 152 14.698 -2.532 0.164 1.00 38.63 O
ANISOU 606 O PHE A 152 4032 5670 4975 1102 483 -26 O
ATOM 607 CB PHE A 152 14.004 -4.085 3.020 1.00 35.74 C
ANISOU 607 CB PHE A 152 3999 5158 4422 1461 466 91 C
ATOM 608 CG PHE A 152 12.841 -3.181 2.769 1.00 32.44 C
ANISOU 608 CG PHE A 152 3531 4715 4079 1245 525 116 C
ATOM 609 CD1 PHE A 152 11.734 -3.639 2.082 1.00 31.22 C
ANISOU 609 CD1 PHE A 152 3455 4461 3945 1177 622 135 C
ATOM 610 CD2 PHE A 152 12.861 -1.870 3.205 1.00 29.20 C
ANISOU 610 CD2 PHE A 152 3004 4369 3721 1108 479 110 C
ATOM 611 CE1 PHE A 152 10.664 -2.810 1.842 1.00 30.26 C
ANISOU 611 CE1 PHE A 152 3281 4321 3893 978 658 143 C
ATOM 612 CE2 PHE A 152 11.793 -1.035 2.968 1.00 27.13 C
ANISOU 612 CE2 PHE A 152 2711 4067 3528 917 513 116 C
ATOM 613 CZ PHE A 152 10.693 -1.507 2.285 1.00 28.06 C
ANISOU 613 CZ PHE A 152 2893 4103 3664 853 594 130 C
ATOM 614 N ALA A 153 16.225 -2.251 1.792 1.00 34.89 N
ANISOU 614 N ALA A 153 3500 5313 4444 1266 362 -36 N
ATOM 615 CA ALA A 153 16.686 -0.985 1.231 1.00 28.37 C
ANISOU 615 CA ALA A 153 2535 4549 3695 1092 353 -63 C
ATOM 616 C ALA A 153 17.375 -1.200 -0.109 1.00 33.11 C
ANISOU 616 C ALA A 153 3063 5200 4318 1077 388 -111 C
ATOM 617 O ALA A 153 17.187 -0.417 -1.046 1.00 35.44 O
ANISOU 617 O ALA A 153 3307 5501 4658 924 423 -110 O
ATOM 618 CB ALA A 153 17.624 -0.288 2.214 1.00 34.73 C
ANISOU 618 CB ALA A 153 3263 5444 4489 1121 278 -77 C
ATOM 619 N ALA A 154 18.185 -2.256 -0.214 1.00 43.13 N
ANISOU 619 N ALA A 154 4333 6518 5537 1254 376 -154 N
ATOM 620 CA ALA A 154 18.874 -2.547 -1.467 1.00 43.60 C
ANISOU 620 CA ALA A 154 4319 6639 5609 1257 418 -210 C
ATOM 621 C ALA A 154 17.914 -3.015 -2.550 1.00 32.02 C
ANISOU 621 C ALA A 154 2924 5087 4155 1195 499 -202 C
ATOM 622 O ALA A 154 18.217 -2.878 -3.740 1.00 38.85 O
ANISOU 622 O ALA A 154 3725 5996 5039 1127 549 -235 O
ATOM 623 CB ALA A 154 19.953 -3.603 -1.239 1.00 52.68 C
ANISOU 623 CB ALA A 154 5457 7856 6702 1482 377 -272 C
ATOM 624 N SER A 155 16.767 -3.581 -2.166 1.00 42.26 N
ANISOU 624 N SER A 155 4354 6270 5431 1220 518 -160 N
ATOM 625 CA SER A 155 15.780 -4.010 -3.151 1.00 41.22 C
ANISOU 625 CA SER A 155 4291 6062 5309 1155 595 -159 C
ATOM 626 C SER A 155 14.950 -2.833 -3.648 1.00 21.64 C
ANISOU 626 C SER A 155 1771 3560 2890 928 615 -130 C
ATOM 627 O SER A 155 14.814 -2.626 -4.858 1.00 19.95 O
ANISOU 627 O SER A 155 1526 3357 2696 830 660 -149 O
ATOM 628 CB SER A 155 14.873 -5.083 -2.549 1.00 39.62 C
ANISOU 628 CB SER A 155 4263 5737 5054 1273 618 -124 C
ATOM 629 OG SER A 155 14.101 -4.551 -1.488 1.00 42.58 O
ANISOU 629 OG SER A 155 4681 6065 5432 1219 601 -60 O
ATOM 630 N VAL A 156 14.394 -2.044 -2.728 1.00 30.97 N
ANISOU 630 N VAL A 156 2963 4708 4097 851 577 -86 N
ATOM 631 CA VAL A 156 13.588 -0.900 -3.139 1.00 29.84 C
ANISOU 631 CA VAL A 156 2801 4522 4013 656 578 -70 C
ATOM 632 C VAL A 156 14.448 0.114 -3.879 1.00 30.14 C
ANISOU 632 C VAL A 156 2738 4656 4058 584 563 -71 C
ATOM 633 O VAL A 156 14.052 0.633 -4.929 1.00 32.46 O
ANISOU 633 O VAL A 156 3023 4948 4363 476 588 -62 O
ATOM 634 CB VAL A 156 12.886 -0.272 -1.919 1.00 30.94 C
ANISOU 634 CB VAL A 156 2973 4614 4168 611 538 -36 C
ATOM 635 CG1 VAL A 156 13.884 0.426 -1.006 1.00 35.63 C
ANISOU 635 CG1 VAL A 156 3502 5282 4754 651 477 -26 C
ATOM 636 CG2 VAL A 156 11.807 0.699 -2.368 1.00 26.01 C
ANISOU 636 CG2 VAL A 156 2354 3949 3578 452 536 -21 C
ATOM 637 N SER A 157 15.647 0.391 -3.365 1.00 32.07 N
ANISOU 637 N SER A 157 2905 4998 4283 649 524 -83 N
ATOM 638 CA SER A 157 16.497 1.400 -3.986 1.00 31.34 C
ANISOU 638 CA SER A 157 2711 5015 4181 575 516 -89 C
ATOM 639 C SER A 157 16.812 1.031 -5.431 1.00 34.93 C
ANISOU 639 C SER A 157 3137 5516 4620 558 578 -118 C
ATOM 640 O SER A 157 16.623 1.840 -6.346 1.00 38.79 O
ANISOU 640 O SER A 157 3607 6023 5107 437 597 -99 O
ATOM 641 CB SER A 157 17.783 1.563 -3.175 1.00 41.93 C
ANISOU 641 CB SER A 157 3963 6470 5499 660 469 -120 C
ATOM 642 OG SER A 157 18.622 2.556 -3.739 1.00 49.61 O
ANISOU 642 OG SER A 157 4831 7557 6461 576 469 -137 O
ATOM 643 N SER A 158 17.277 -0.199 -5.658 1.00 34.35 N
ANISOU 643 N SER A 158 3067 5456 4527 686 611 -165 N
ATOM 644 CA SER A 158 17.599 -0.618 -7.019 1.00 29.74 C
ANISOU 644 CA SER A 158 2457 4919 3922 679 680 -203 C
ATOM 645 C SER A 158 16.347 -0.672 -7.885 1.00 32.57 C
ANISOU 645 C SER A 158 2903 5177 4294 578 728 -174 C
ATOM 646 O SER A 158 16.404 -0.382 -9.086 1.00 29.27 O
ANISOU 646 O SER A 158 2463 4804 3854 500 774 -176 O
ATOM 647 CB SER A 158 18.300 -1.976 -7.003 1.00 33.43 C
ANISOU 647 CB SER A 158 2925 5405 4371 855 702 -269 C
ATOM 648 OG SER A 158 17.436 -2.998 -6.539 1.00 53.57 O
ANISOU 648 OG SER A 158 5596 7841 6917 943 705 -264 O
ATOM 649 N LEU A 159 15.208 -1.044 -7.297 1.00 23.20 N
ANISOU 649 N LEU A 159 1812 3864 3136 575 718 -152 N
ATOM 650 CA LEU A 159 13.966 -1.078 -8.061 1.00 21.86 C
ANISOU 650 CA LEU A 159 1715 3609 2981 475 757 -137 C
ATOM 651 C LEU A 159 13.635 0.302 -8.611 1.00 26.59 C
ANISOU 651 C LEU A 159 2285 4232 3585 331 729 -86 C
ATOM 652 O LEU A 159 13.153 0.430 -9.742 1.00 31.38 O
ANISOU 652 O LEU A 159 2913 4832 4179 255 765 -75 O
ATOM 653 CB LEU A 159 12.828 -1.604 -7.186 1.00 31.61 C
ANISOU 653 CB LEU A 159 3034 4753 4224 496 744 -130 C
ATOM 654 CG LEU A 159 11.609 -2.186 -7.908 1.00 30.27 C
ANISOU 654 CG LEU A 159 2934 4532 4036 449 797 -140 C
ATOM 655 CD1 LEU A 159 12.008 -3.340 -8.800 1.00 33.74 C
ANISOU 655 CD1 LEU A 159 3397 5005 4419 546 870 -189 C
ATOM 656 CD2 LEU A 159 10.555 -2.648 -6.914 1.00 28.55 C
ANISOU 656 CD2 LEU A 159 2791 4250 3808 472 787 -124 C
ATOM 657 N LEU A 160 13.883 1.348 -7.822 1.00 29.22 N
ANISOU 657 N LEU A 160 2579 4593 3931 297 664 -54 N
ATOM 658 CA LEU A 160 13.783 2.704 -8.350 1.00 23.73 C
ANISOU 658 CA LEU A 160 1858 3926 3233 175 635 -15 C
ATOM 659 C LEU A 160 14.795 2.922 -9.466 1.00 26.91 C
ANISOU 659 C LEU A 160 2191 4446 3586 147 676 -30 C
ATOM 660 O LEU A 160 14.478 3.534 -10.493 1.00 29.05 O
ANISOU 660 O LEU A 160 2474 4729 3835 49 688 -4 O
ATOM 661 CB LEU A 160 14.000 3.716 -7.223 1.00 23.71 C
ANISOU 661 CB LEU A 160 1828 3930 3250 157 569 6 C
ATOM 662 CG LEU A 160 14.090 5.198 -7.594 1.00 21.02 C
ANISOU 662 CG LEU A 160 1461 3621 2907 44 537 38 C
ATOM 663 CD1 LEU A 160 12.733 5.760 -7.963 1.00 24.64 C
ANISOU 663 CD1 LEU A 160 1989 3981 3390 -37 514 72 C
ATOM 664 CD2 LEU A 160 14.692 5.983 -6.447 1.00 25.84 C
ANISOU 664 CD2 LEU A 160 2027 4263 3530 50 489 38 C
ATOM 665 N ALA A 161 16.016 2.411 -9.288 1.00 31.03 N
ANISOU 665 N ALA A 161 2640 5066 4084 235 697 -78 N
ATOM 666 CA ALA A 161 17.074 2.644 -10.266 1.00 25.53 C
ANISOU 666 CA ALA A 161 1860 4504 3337 205 742 -109 C
ATOM 667 C ALA A 161 16.706 2.075 -11.628 1.00 28.71 C
ANISOU 667 C ALA A 161 2303 4902 3703 179 814 -118 C
ATOM 668 O ALA A 161 17.023 2.670 -12.664 1.00 32.12 O
ANISOU 668 O ALA A 161 2706 5412 4088 84 847 -114 O
ATOM 669 CB ALA A 161 18.385 2.036 -9.769 1.00 26.84 C
ANISOU 669 CB ALA A 161 1933 4777 3490 327 748 -177 C
ATOM 670 N ILE A 162 16.043 0.918 -11.651 1.00 26.06 N
ANISOU 670 N ILE A 162 2043 4477 3383 256 845 -135 N
ATOM 671 CA ILE A 162 15.634 0.340 -12.926 1.00 23.82 C
ANISOU 671 CA ILE A 162 1808 4182 3059 232 919 -148 C
ATOM 672 C ILE A 162 14.627 1.245 -13.621 1.00 21.30 C
ANISOU 672 C ILE A 162 1540 3821 2730 91 897 -82 C
ATOM 673 O ILE A 162 14.557 1.276 -14.856 1.00 21.21 O
ANISOU 673 O ILE A 162 1543 3862 2654 30 944 -82 O
ATOM 674 CB ILE A 162 15.073 -1.080 -12.710 1.00 31.98 C
ANISOU 674 CB ILE A 162 2916 5137 4098 344 956 -188 C
ATOM 675 CG1 ILE A 162 16.107 -1.956 -11.995 1.00 30.06 C
ANISOU 675 CG1 ILE A 162 2628 4936 3858 504 959 -255 C
ATOM 676 CG2 ILE A 162 14.682 -1.709 -14.045 1.00 39.08 C
ANISOU 676 CG2 ILE A 162 3859 6067 4920 328 1032 -215 C
ATOM 677 CD1 ILE A 162 15.599 -3.327 -11.615 1.00 27.80 C
ANISOU 677 CD1 ILE A 162 2426 4574 3564 633 981 -300 C
ATOM 678 N THR A 163 13.836 1.996 -12.851 1.00 26.23 N
ANISOU 678 N THR A 163 2193 4367 3408 42 822 -32 N
ATOM 679 CA THR A 163 12.817 2.856 -13.449 1.00 29.19 C
ANISOU 679 CA THR A 163 2615 4696 3781 -74 786 23 C
ATOM 680 C THR A 163 13.445 4.016 -14.213 1.00 32.30 C
ANISOU 680 C THR A 163 2966 5186 4119 -179 780 49 C
ATOM 681 O THR A 163 13.079 4.282 -15.365 1.00 37.53 O
ANISOU 681 O THR A 163 3663 5866 4729 -262 799 73 O
ATOM 682 CB THR A 163 11.871 3.382 -12.369 1.00 25.05 C
ANISOU 682 CB THR A 163 2123 4068 3328 -87 709 53 C
ATOM 683 OG1 THR A 163 11.197 2.286 -11.741 1.00 25.78 O
ANISOU 683 OG1 THR A 163 2263 4071 3462 -14 728 26 O
ATOM 684 CG2 THR A 163 10.841 4.319 -12.974 1.00 28.81 C
ANISOU 684 CG2 THR A 163 2638 4501 3807 -192 661 102 C
ATOM 685 N VAL A 164 14.392 4.724 -13.591 1.00 28.08 N
ANISOU 685 N VAL A 164 2361 4716 3591 -186 756 43 N
ATOM 686 CA VAL A 164 15.029 5.846 -14.274 1.00 31.25 C
ANISOU 686 CA VAL A 164 2724 5208 3941 -300 763 64 C
ATOM 687 C VAL A 164 15.782 5.364 -15.499 1.00 27.59 C
ANISOU 687 C VAL A 164 2231 4858 3394 -322 852 27 C
ATOM 688 O VAL A 164 15.815 6.050 -16.527 1.00 34.08 O
ANISOU 688 O VAL A 164 3071 5727 4151 -440 874 56 O
ATOM 689 CB VAL A 164 15.950 6.620 -13.312 1.00 36.21 C
ANISOU 689 CB VAL A 164 3275 5889 4593 -304 730 54 C
ATOM 690 CG1 VAL A 164 15.153 7.154 -12.137 1.00 36.37 C
ANISOU 690 CG1 VAL A 164 3337 5797 4686 -288 649 87 C
ATOM 691 CG2 VAL A 164 17.085 5.742 -12.825 1.00 33.75 C
ANISOU 691 CG2 VAL A 164 2878 5668 4280 -193 767 -17 C
ATOM 692 N ASP A 165 16.389 4.179 -15.422 1.00 30.93 N
ANISOU 692 N ASP A 165 2614 5325 3811 -207 907 -39 N
ATOM 693 CA ASP A 165 17.052 3.629 -16.598 1.00 34.98 C
ANISOU 693 CA ASP A 165 3102 5944 4244 -214 1000 -88 C
ATOM 694 C ASP A 165 16.059 3.436 -17.732 1.00 34.83 C
ANISOU 694 C ASP A 165 3179 5893 4162 -280 1023 -58 C
ATOM 695 O ASP A 165 16.356 3.752 -18.890 1.00 40.58 O
ANISOU 695 O ASP A 165 3905 6723 4788 -380 1073 -63 O
ATOM 696 CB ASP A 165 17.727 2.304 -16.249 1.00 35.63 C
ANISOU 696 CB ASP A 165 3139 6058 4339 -55 1047 -171 C
ATOM 697 CG ASP A 165 18.657 1.821 -17.339 1.00 41.39 C
ANISOU 697 CG ASP A 165 3816 6922 4989 -50 1147 -242 C
ATOM 698 OD1 ASP A 165 19.668 2.512 -17.599 1.00 37.46 O
ANISOU 698 OD1 ASP A 165 3221 6558 4452 -120 1171 -268 O
ATOM 699 OD2 ASP A 165 18.380 0.753 -17.933 1.00 52.07 O
ANISOU 699 OD2 ASP A 165 5212 8277 6295 18 1201 -289 O
ATOM 700 N ARG A 166 14.869 2.925 -17.418 1.00 34.28 N
ANISOU 700 N ARG A 166 3185 5711 4131 -238 986 -36 N
ATOM 701 CA ARG A 166 13.843 2.774 -18.441 1.00 34.56 C
ANISOU 701 CA ARG A 166 3295 5746 4089 -313 990 -14 C
ATOM 702 C ARG A 166 13.394 4.132 -18.963 1.00 39.45 C
ANISOU 702 C ARG A 166 3944 6372 4671 -469 934 62 C
ATOM 703 O ARG A 166 13.306 4.346 -20.178 1.00 43.62 O
ANISOU 703 O ARG A 166 4508 6983 5083 -577 961 72 O
ATOM 704 CB ARG A 166 12.654 2.002 -17.878 1.00 32.82 C
ANISOU 704 CB ARG A 166 3134 5410 3928 -245 960 -9 C
ATOM 705 CG ARG A 166 11.638 1.604 -18.932 1.00 43.40 C
ANISOU 705 CG ARG A 166 4541 6768 5180 -311 972 -8 C
ATOM 706 CD ARG A 166 12.135 0.444 -19.769 1.00 42.21 C
ANISOU 706 CD ARG A 166 4404 6700 4933 -255 1073 -93 C
ATOM 707 NE ARG A 166 12.318 -0.757 -18.966 1.00 50.02 N
ANISOU 707 NE ARG A 166 5396 7630 5981 -95 1114 -152 N
ATOM 708 CZ ARG A 166 12.582 -1.957 -19.462 1.00 55.49 C
ANISOU 708 CZ ARG A 166 6121 8353 6609 -8 1198 -238 C
ATOM 709 NH1 ARG A 166 12.713 -2.152 -20.764 1.00 52.75 N
ANISOU 709 NH1 ARG A 166 5804 8101 6137 -64 1254 -283 N
ATOM 710 NH2 ARG A 166 12.709 -2.988 -18.632 1.00 62.77 N
ANISOU 710 NH2 ARG A 166 7062 9202 7586 141 1226 -287 N
ATOM 711 N TYR A 167 13.107 5.068 -18.057 1.00 35.58 N
ANISOU 711 N TYR A 167 3451 5796 4272 -485 854 112 N
ATOM 712 CA TYR A 167 12.667 6.390 -18.483 1.00 29.11 C
ANISOU 712 CA TYR A 167 2668 4973 3421 -623 794 185 C
ATOM 713 C TYR A 167 13.753 7.083 -19.292 1.00 36.06 C
ANISOU 713 C TYR A 167 3522 5974 4206 -731 847 188 C
ATOM 714 O TYR A 167 13.504 7.571 -20.399 1.00 42.54 O
ANISOU 714 O TYR A 167 4399 6850 4914 -865 850 228 O
ATOM 715 CB TYR A 167 12.279 7.231 -17.268 1.00 23.65 C
ANISOU 715 CB TYR A 167 1975 4164 2848 -600 710 219 C
ATOM 716 CG TYR A 167 12.085 8.692 -17.590 1.00 30.06 C
ANISOU 716 CG TYR A 167 2816 4975 3630 -732 653 289 C
ATOM 717 CD1 TYR A 167 10.943 9.134 -18.243 1.00 36.40 C
ANISOU 717 CD1 TYR A 167 3687 5756 4389 -821 587 353 C
ATOM 718 CD2 TYR A 167 13.045 9.632 -17.241 1.00 32.49 C
ANISOU 718 CD2 TYR A 167 3085 5308 3952 -776 661 295 C
ATOM 719 CE1 TYR A 167 10.764 10.471 -18.541 1.00 41.26 C
ANISOU 719 CE1 TYR A 167 4344 6363 4971 -947 526 431 C
ATOM 720 CE2 TYR A 167 12.875 10.971 -17.534 1.00 35.32 C
ANISOU 720 CE2 TYR A 167 3483 5658 4279 -905 612 364 C
ATOM 721 CZ TYR A 167 11.734 11.385 -18.184 1.00 40.19 C
ANISOU 721 CZ TYR A 167 4180 6241 4848 -989 542 436 C
ATOM 722 OH TYR A 167 11.562 12.719 -18.476 1.00 41.17 O
ANISOU 722 OH TYR A 167 4362 6346 4937 -1123 482 517 O
ATOM 723 N LEU A 168 14.975 7.117 -18.759 1.00 32.58 N
ANISOU 723 N LEU A 168 2997 5580 3801 -685 890 143 N
ATOM 724 CA LEU A 168 16.063 7.793 -19.456 1.00 36.39 C
ANISOU 724 CA LEU A 168 3439 6186 4201 -798 949 136 C
ATOM 725 C LEU A 168 16.360 7.123 -20.790 1.00 39.93 C
ANISOU 725 C LEU A 168 3901 6753 4517 -843 1040 95 C
ATOM 726 O LEU A 168 16.590 7.803 -21.797 1.00 47.29 O
ANISOU 726 O LEU A 168 4870 7762 5337 -996 1072 123 O
ATOM 727 CB LEU A 168 17.312 7.814 -18.577 1.00 35.83 C
ANISOU 727 CB LEU A 168 3252 6173 4188 -735 974 80 C
ATOM 728 CG LEU A 168 17.190 8.643 -17.299 1.00 25.66 C
ANISOU 728 CG LEU A 168 1943 4817 2990 -727 888 109 C
ATOM 729 CD1 LEU A 168 18.415 8.450 -16.432 1.00 38.85 C
ANISOU 729 CD1 LEU A 168 3489 6583 4691 -660 906 39 C
ATOM 730 CD2 LEU A 168 16.994 10.110 -17.631 1.00 28.16 C
ANISOU 730 CD2 LEU A 168 2310 5110 3281 -885 854 183 C
ATOM 731 N SER A 169 16.359 5.790 -20.817 1.00 35.48 N
ANISOU 731 N SER A 169 3321 6204 3958 -717 1085 28 N
ATOM 732 CA SER A 169 16.608 5.083 -22.068 1.00 45.78 C
ANISOU 732 CA SER A 169 4644 7616 5136 -746 1177 -25 C
ATOM 733 C SER A 169 15.540 5.415 -23.100 1.00 54.37 C
ANISOU 733 C SER A 169 5853 8689 6115 -878 1147 36 C
ATOM 734 O SER A 169 15.847 5.668 -24.269 1.00 56.80 O
ANISOU 734 O SER A 169 6201 9093 6286 -1002 1204 34 O
ATOM 735 CB SER A 169 16.663 3.576 -21.815 1.00 47.32 C
ANISOU 735 CB SER A 169 4816 7803 5362 -573 1222 -109 C
ATOM 736 OG SER A 169 15.427 3.101 -21.311 1.00 44.45 O
ANISOU 736 OG SER A 169 4521 7312 5057 -510 1157 -78 O
ATOM 737 N LEU A 170 14.274 5.421 -22.682 1.00 54.44 N
ANISOU 737 N LEU A 170 5924 8583 6176 -859 1057 90 N
ATOM 738 CA LEU A 170 13.189 5.733 -23.603 1.00 53.87 C
ANISOU 738 CA LEU A 170 5966 8502 6002 -984 1009 150 C
ATOM 739 C LEU A 170 13.067 7.228 -23.866 1.00 43.55 C
ANISOU 739 C LEU A 170 4712 7183 4654 -1147 943 250 C
ATOM 740 O LEU A 170 12.666 7.626 -24.965 1.00 41.99 O
ANISOU 740 O LEU A 170 4619 7019 4316 -1291 929 300 O
ATOM 741 CB LEU A 170 11.870 5.186 -23.056 1.00 55.24 C
ANISOU 741 CB LEU A 170 6170 8571 6249 -913 935 164 C
ATOM 742 CG LEU A 170 11.816 3.666 -22.891 1.00 45.58 C
ANISOU 742 CG LEU A 170 4928 7342 5046 -771 999 72 C
ATOM 743 CD1 LEU A 170 10.530 3.250 -22.198 1.00 38.93 C
ANISOU 743 CD1 LEU A 170 4108 6391 4292 -718 929 88 C
ATOM 744 CD2 LEU A 170 11.952 2.969 -24.238 1.00 41.30 C
ANISOU 744 CD2 LEU A 170 4445 6901 4344 -819 1081 14 C
ATOM 745 N TYR A 171 13.406 8.065 -22.884 1.00 42.38 N
ANISOU 745 N TYR A 171 4510 6980 4615 -1130 900 280 N
ATOM 746 CA TYR A 171 13.203 9.502 -23.033 1.00 45.19 C
ANISOU 746 CA TYR A 171 4930 7301 4940 -1277 830 377 C
ATOM 747 C TYR A 171 13.962 10.045 -24.237 1.00 48.72 C
ANISOU 747 C TYR A 171 5432 7851 5230 -1444 897 393 C
ATOM 748 O TYR A 171 13.401 10.772 -25.065 1.00 51.52 O
ANISOU 748 O TYR A 171 5915 8186 5472 -1595 844 480 O
ATOM 749 CB TYR A 171 13.634 10.226 -21.758 1.00 43.32 C
ANISOU 749 CB TYR A 171 4619 6999 4842 -1222 794 382 C
ATOM 750 CG TYR A 171 13.382 11.713 -21.798 1.00 42.04 C
ANISOU 750 CG TYR A 171 4528 6784 4662 -1363 718 479 C
ATOM 751 CD1 TYR A 171 12.165 12.237 -21.390 1.00 46.84 C
ANISOU 751 CD1 TYR A 171 5194 7277 5326 -1364 595 553 C
ATOM 752 CD2 TYR A 171 14.356 12.592 -22.251 1.00 44.74 C
ANISOU 752 CD2 TYR A 171 4881 7188 4930 -1499 767 497 C
ATOM 753 CE1 TYR A 171 11.924 13.594 -21.426 1.00 51.97 C
ANISOU 753 CE1 TYR A 171 5921 7864 5960 -1488 516 646 C
ATOM 754 CE2 TYR A 171 14.124 13.953 -22.291 1.00 43.86 C
ANISOU 754 CE2 TYR A 171 4855 7011 4797 -1634 696 590 C
ATOM 755 CZ TYR A 171 12.905 14.448 -21.877 1.00 40.10 C
ANISOU 755 CZ TYR A 171 4447 6410 4380 -1623 566 667 C
ATOM 756 OH TYR A 171 12.658 15.800 -21.911 1.00 39.04 O
ANISOU 756 OH TYR A 171 4411 6194 4226 -1751 483 764 O
ATOM 757 N ASN A 172 15.240 9.708 -24.348 1.00 57.57 N
ANISOU 757 N ASN A 172 6463 9078 6335 -1424 1011 312 N
ATOM 758 CA ASN A 172 16.045 10.171 -25.468 1.00 73.96 C
ANISOU 758 CA ASN A 172 8578 11262 8261 -1586 1095 313 C
ATOM 759 C ASN A 172 17.259 9.260 -25.609 1.00 72.01 C
ANISOU 759 C ASN A 172 8207 11149 8006 -1509 1227 191 C
ATOM 760 O ASN A 172 18.321 9.545 -25.039 1.00 70.99 O
ANISOU 760 O ASN A 172 7963 11073 7937 -1494 1271 148 O
ATOM 761 CB ASN A 172 16.461 11.628 -25.261 1.00 83.69 C
ANISOU 761 CB ASN A 172 9835 12470 9494 -1726 1065 383 C
ATOM 762 CG ASN A 172 16.619 12.382 -26.565 1.00 80.13 C
ANISOU 762 CG ASN A 172 9519 12064 8861 -1945 1097 442 C
ATOM 763 OD1 ASN A 172 16.795 11.784 -27.626 1.00 77.60 O
ANISOU 763 OD1 ASN A 172 9240 11832 8411 -1990 1175 405 O
ATOM 764 ND2 ASN A 172 16.553 13.706 -26.493 1.00 73.04 N
ANISOU 764 ND2 ASN A 172 8705 11097 7948 -2084 1036 535 N
ATOM 765 N PRO A 173 17.142 8.152 -26.345 1.00 67.17 N
ANISOU 765 N PRO A 173 7611 10593 7318 -1457 1289 128 N
ATOM 766 CA PRO A 173 18.258 7.195 -26.396 1.00 70.25 C
ANISOU 766 CA PRO A 173 7876 11102 7714 -1356 1407 5 C
ATOM 767 C PRO A 173 19.558 7.798 -26.897 1.00 70.72 C
ANISOU 767 C PRO A 173 7870 11299 7700 -1482 1508 -31 C
ATOM 768 O PRO A 173 20.634 7.353 -26.479 1.00 72.25 O
ANISOU 768 O PRO A 173 7917 11584 7949 -1395 1577 -125 O
ATOM 769 CB PRO A 173 17.741 6.102 -27.341 1.00 81.49 C
ANISOU 769 CB PRO A 173 9374 12554 9035 -1320 1453 -43 C
ATOM 770 CG PRO A 173 16.263 6.206 -27.280 1.00 64.53 C
ANISOU 770 CG PRO A 173 7348 10280 6892 -1333 1337 42 C
ATOM 771 CD PRO A 173 15.957 7.659 -27.066 1.00 63.30 C
ANISOU 771 CD PRO A 173 7248 10058 6743 -1473 1247 159 C
ATOM 772 N LEU A 174 19.499 8.793 -27.786 1.00 70.43 N
ANISOU 772 N LEU A 174 7943 11284 7534 -1692 1516 39 N
ATOM 773 CA LEU A 174 20.731 9.415 -28.260 1.00 68.88 C
ANISOU 773 CA LEU A 174 7688 11220 7262 -1837 1621 4 C
ATOM 774 C LEU A 174 21.475 10.084 -27.113 1.00 66.28 C
ANISOU 774 C LEU A 174 7230 10889 7062 -1818 1598 -3 C
ATOM 775 O LEU A 174 22.703 9.984 -27.017 1.00 66.27 O
ANISOU 775 O LEU A 174 7086 11023 7069 -1820 1691 -95 O
ATOM 776 CB LEU A 174 20.421 10.421 -29.369 1.00 72.59 C
ANISOU 776 CB LEU A 174 8335 11683 7565 -2076 1621 99 C
ATOM 777 CG LEU A 174 19.556 11.622 -28.985 1.00 77.77 C
ANISOU 777 CG LEU A 174 9118 12184 8247 -2169 1486 239 C
ATOM 778 CD1 LEU A 174 20.421 12.840 -28.683 1.00 74.63 C
ANISOU 778 CD1 LEU A 174 8687 11811 7858 -2314 1509 265 C
ATOM 779 CD2 LEU A 174 18.555 11.929 -30.089 1.00 83.03 C
ANISOU 779 CD2 LEU A 174 10006 12785 8755 -2301 1431 337 C
ATOM 780 N THR A 175 20.747 10.769 -26.229 1.00 64.72 N
ANISOU 780 N THR A 175 7079 10547 6964 -1798 1475 86 N
ATOM 781 CA THR A 175 21.368 11.290 -25.019 1.00 62.62 C
ANISOU 781 CA THR A 175 6695 10268 6831 -1753 1444 71 C
ATOM 782 C THR A 175 21.685 10.175 -24.036 1.00 64.63 C
ANISOU 782 C THR A 175 6809 10531 7218 -1520 1440 -18 C
ATOM 783 O THR A 175 22.534 10.357 -23.158 1.00 64.95 O
ANISOU 783 O THR A 175 6722 10611 7345 -1473 1444 -65 O
ATOM 784 CB THR A 175 20.461 12.324 -24.351 1.00 62.78 C
ANISOU 784 CB THR A 175 6812 10124 6918 -1791 1315 186 C
ATOM 785 OG1 THR A 175 19.375 11.659 -23.694 1.00 62.75 O
ANISOU 785 OG1 THR A 175 6834 9998 7012 -1621 1222 206 O
ATOM 786 CG2 THR A 175 19.912 13.302 -25.382 1.00 66.01 C
ANISOU 786 CG2 THR A 175 7401 10493 7186 -2004 1294 291 C
ATOM 787 N TYR A 176 21.028 9.023 -24.176 1.00 64.69 N
ANISOU 787 N TYR A 176 6846 10501 7232 -1381 1432 -44 N
ATOM 788 CA TYR A 176 21.325 7.841 -23.369 1.00 63.51 C
ANISOU 788 CA TYR A 176 6590 10354 7187 -1164 1435 -128 C
ATOM 789 C TYR A 176 22.621 7.206 -23.878 1.00 61.56 C
ANISOU 789 C TYR A 176 6216 10288 6885 -1144 1561 -251 C
ATOM 790 O TYR A 176 22.662 6.065 -24.340 1.00 57.21 O
ANISOU 790 O TYR A 176 5654 9783 6301 -1041 1618 -323 O
ATOM 791 CB TYR A 176 20.152 6.870 -23.428 1.00 56.27 C
ANISOU 791 CB TYR A 176 5764 9333 6283 -1046 1392 -113 C
ATOM 792 CG TYR A 176 20.209 5.701 -22.466 1.00 46.05 C
ANISOU 792 CG TYR A 176 4402 7994 5102 -826 1375 -177 C
ATOM 793 CD1 TYR A 176 19.777 5.831 -21.152 1.00 47.89 C
ANISOU 793 CD1 TYR A 176 4630 8098 5467 -732 1278 -137 C
ATOM 794 CD2 TYR A 176 20.663 4.458 -22.884 1.00 48.40 C
ANISOU 794 CD2 TYR A 176 4655 8369 5364 -715 1457 -276 C
ATOM 795 CE1 TYR A 176 19.815 4.760 -20.278 1.00 46.71 C
ANISOU 795 CE1 TYR A 176 4441 7900 5406 -544 1262 -187 C
ATOM 796 CE2 TYR A 176 20.704 3.384 -22.017 1.00 56.09 C
ANISOU 796 CE2 TYR A 176 5588 9292 6432 -517 1438 -329 C
ATOM 797 CZ TYR A 176 20.277 3.540 -20.717 1.00 44.17 C
ANISOU 797 CZ TYR A 176 4083 7654 5046 -439 1340 -280 C
ATOM 798 OH TYR A 176 20.317 2.476 -19.848 1.00 35.72 O
ANISOU 798 OH TYR A 176 2988 6527 4056 -254 1322 -327 O
ATOM 799 N TYR A 177 23.690 7.994 -23.804 1.00 75.81 N
ANISOU 799 N TYR A 177 7923 12203 8680 -1251 1606 -279 N
ATOM 800 CA TYR A 177 24.978 7.596 -24.341 1.00 86.70 C
ANISOU 800 CA TYR A 177 9167 13777 10000 -1267 1730 -400 C
ATOM 801 C TYR A 177 25.699 6.658 -23.379 1.00 82.52 C
ANISOU 801 C TYR A 177 8476 13306 9571 -1062 1722 -509 C
ATOM 802 O TYR A 177 25.364 6.551 -22.196 1.00 81.87 O
ANISOU 802 O TYR A 177 8382 13126 9600 -941 1619 -485 O
ATOM 803 CB TYR A 177 25.844 8.824 -24.620 1.00 67.98 C
ANISOU 803 CB TYR A 177 6744 11516 7568 -1482 1785 -399 C
ATOM 804 N SER A 178 26.712 5.974 -23.911 1.00 94.41 N
ANISOU 804 N SER A 178 9859 14983 11029 -1024 1830 -637 N
ATOM 805 CA SER A 178 27.489 5.028 -23.122 1.00106.75 C
ANISOU 805 CA SER A 178 11265 16624 12671 -824 1825 -755 C
ATOM 806 C SER A 178 28.346 5.707 -22.062 1.00103.83 C
ANISOU 806 C SER A 178 10747 16336 12369 -842 1776 -792 C
ATOM 807 O SER A 178 28.880 5.015 -21.188 1.00103.81 O
ANISOU 807 O SER A 178 10627 16374 12443 -664 1737 -874 O
ATOM 808 CB SER A 178 28.378 4.192 -24.045 1.00110.81 C
ANISOU 808 CB SER A 178 11680 17312 13111 -784 1957 -893 C
ATOM 809 OG SER A 178 27.598 3.472 -24.984 1.00111.87 O
ANISOU 809 OG SER A 178 11953 17376 13176 -753 2002 -873 O
ATOM 810 N ARG A 179 28.488 7.031 -22.108 1.00 88.61 N
ANISOU 810 N ARG A 179 8829 14430 10411 -1049 1775 -736 N
ATOM 811 CA ARG A 179 29.312 7.742 -21.134 1.00 90.80 C
ANISOU 811 CA ARG A 179 8969 14788 10744 -1084 1735 -775 C
ATOM 812 C ARG A 179 28.489 8.165 -19.920 1.00 83.47 C
ANISOU 812 C ARG A 179 8123 13678 9914 -1024 1593 -673 C
ATOM 813 O ARG A 179 28.797 7.777 -18.789 1.00 89.26 O
ANISOU 813 O ARG A 179 8768 14415 10731 -872 1522 -718 O
ATOM 814 CB ARG A 179 29.993 8.954 -21.789 1.00 91.01 C
ANISOU 814 CB ARG A 179 8959 14938 10682 -1348 1819 -781 C
ATOM 815 CG ARG A 179 29.116 9.788 -22.722 1.00 87.31 C
ANISOU 815 CG ARG A 179 8689 14357 10127 -1543 1837 -648 C
ATOM 816 CD ARG A 179 29.926 10.887 -23.393 1.00 83.78 C
ANISOU 816 CD ARG A 179 8206 14043 9582 -1807 1935 -666 C
ATOM 817 NE ARG A 179 29.227 11.476 -24.530 1.00 87.72 N
ANISOU 817 NE ARG A 179 8898 14462 9967 -1987 1974 -557 N
ATOM 818 CZ ARG A 179 28.424 12.530 -24.462 1.00 87.17 C
ANISOU 818 CZ ARG A 179 8994 14234 9892 -2109 1901 -417 C
ATOM 819 NH1 ARG A 179 28.177 13.141 -23.314 1.00 87.03 N
ANISOU 819 NH1 ARG A 179 8973 14116 9979 -2077 1792 -368 N
ATOM 820 NH2 ARG A 179 27.854 12.983 -25.574 1.00 86.26 N
ANISOU 820 NH2 ARG A 179 9056 14058 9659 -2264 1937 -326 N
ATOM 821 N ARG A 180 27.432 8.948 -20.139 1.00 72.40 N
ANISOU 821 N ARG A 180 6892 12119 8498 -1137 1549 -538 N
ATOM 822 CA ARG A 180 26.607 9.381 -19.017 1.00 65.51 C
ANISOU 822 CA ARG A 180 6097 11075 7717 -1084 1422 -447 C
ATOM 823 C ARG A 180 25.928 8.195 -18.346 1.00 61.73 C
ANISOU 823 C ARG A 180 5655 10484 7314 -854 1354 -446 C
ATOM 824 O ARG A 180 25.902 8.101 -17.113 1.00 59.61 O
ANISOU 824 O ARG A 180 5354 10164 7130 -742 1268 -449 O
ATOM 825 CB ARG A 180 25.566 10.397 -19.493 1.00 75.17 C
ANISOU 825 CB ARG A 180 7497 12155 8909 -1239 1390 -312 C
ATOM 826 CG ARG A 180 26.135 11.781 -19.773 1.00 83.11 C
ANISOU 826 CG ARG A 180 8492 13224 9861 -1468 1426 -289 C
ATOM 827 CD ARG A 180 26.529 12.500 -18.485 1.00 80.35 C
ANISOU 827 CD ARG A 180 8066 12868 9595 -1465 1355 -297 C
ATOM 828 NE ARG A 180 25.384 13.120 -17.826 1.00 61.74 N
ANISOU 828 NE ARG A 180 5844 10311 7305 -1451 1244 -182 N
ATOM 829 CZ ARG A 180 25.332 14.381 -17.415 1.00 68.91 C
ANISOU 829 CZ ARG A 180 6789 11162 8232 -1580 1204 -125 C
ATOM 830 NH1 ARG A 180 26.370 15.196 -17.534 1.00 57.26 N
ANISOU 830 NH1 ARG A 180 5231 9811 6716 -1743 1264 -168 N
ATOM 831 NH2 ARG A 180 24.212 14.836 -16.861 1.00 62.31 N
ANISOU 831 NH2 ARG A 180 6074 10140 7459 -1546 1105 -30 N
ATOM 832 N THR A 181 25.384 7.274 -19.139 1.00 75.93 N
ANISOU 832 N THR A 181 7528 12243 9077 -788 1394 -445 N
ATOM 833 CA THR A 181 24.657 6.143 -18.573 1.00 75.56 C
ANISOU 833 CA THR A 181 7538 12075 9097 -589 1338 -440 C
ATOM 834 C THR A 181 25.580 5.264 -17.736 1.00 73.84 C
ANISOU 834 C THR A 181 7179 11945 8931 -411 1329 -548 C
ATOM 835 O THR A 181 25.397 5.126 -16.522 1.00 72.83 O
ANISOU 835 O THR A 181 7049 11742 8882 -302 1239 -533 O
ATOM 836 CB THR A 181 24.003 5.332 -19.692 1.00 71.13 C
ANISOU 836 CB THR A 181 7078 11471 8476 -568 1399 -432 C
ATOM 837 OG1 THR A 181 25.008 4.864 -20.600 1.00 88.70 O
ANISOU 837 OG1 THR A 181 9208 13870 10626 -579 1515 -536 O
ATOM 838 CG2 THR A 181 22.995 6.183 -20.445 1.00 64.36 C
ANISOU 838 CG2 THR A 181 6370 10518 7567 -729 1387 -320 C
ATOM 839 N LEU A 182 26.595 4.672 -18.372 1.00 64.68 N
ANISOU 839 N LEU A 182 5902 10952 7723 -378 1421 -662 N
ATOM 840 CA LEU A 182 27.482 3.764 -17.650 1.00 64.48 C
ANISOU 840 CA LEU A 182 5741 11015 7743 -189 1407 -775 C
ATOM 841 C LEU A 182 28.123 4.447 -16.453 1.00 59.71 C
ANISOU 841 C LEU A 182 5030 10465 7192 -190 1331 -792 C
ATOM 842 O LEU A 182 28.394 3.796 -15.437 1.00 52.06 O
ANISOU 842 O LEU A 182 4011 9488 6282 -15 1263 -835 O
ATOM 843 CB LEU A 182 28.564 3.221 -18.583 1.00 61.93 C
ANISOU 843 CB LEU A 182 5287 10888 7356 -175 1524 -908 C
ATOM 844 CG LEU A 182 28.153 2.090 -19.529 1.00 80.31 C
ANISOU 844 CG LEU A 182 7695 13177 9643 -85 1597 -935 C
ATOM 845 CD1 LEU A 182 27.897 0.800 -18.758 1.00 83.61 C
ANISOU 845 CD1 LEU A 182 8144 13492 10132 164 1537 -964 C
ATOM 846 CD2 LEU A 182 26.929 2.475 -20.344 1.00 72.39 C
ANISOU 846 CD2 LEU A 182 6879 12037 8590 -218 1613 -815 C
ATOM 847 N LEU A 183 28.387 5.749 -16.554 1.00 54.41 N
ANISOU 847 N LEU A 183 4330 9847 6495 -386 1341 -761 N
ATOM 848 CA LEU A 183 28.840 6.489 -15.386 1.00 53.86 C
ANISOU 848 CA LEU A 183 4184 9805 6477 -399 1265 -766 C
ATOM 849 C LEU A 183 27.779 6.465 -14.296 1.00 58.33 C
ANISOU 849 C LEU A 183 4878 10168 7115 -310 1149 -666 C
ATOM 850 O LEU A 183 28.048 6.061 -13.159 1.00 60.81 O
ANISOU 850 O LEU A 183 5142 10480 7483 -167 1075 -700 O
ATOM 851 CB LEU A 183 29.180 7.925 -15.781 1.00 74.05 C
ANISOU 851 CB LEU A 183 6716 12429 8990 -643 1305 -740 C
ATOM 852 CG LEU A 183 29.417 8.901 -14.627 1.00 77.88 C
ANISOU 852 CG LEU A 183 7160 12904 9526 -692 1227 -721 C
ATOM 853 CD1 LEU A 183 30.516 8.389 -13.711 1.00 66.49 C
ANISOU 853 CD1 LEU A 183 5538 11606 8121 -551 1194 -847 C
ATOM 854 CD2 LEU A 183 29.752 10.289 -15.159 1.00 71.05 C
ANISOU 854 CD2 LEU A 183 6286 12099 8612 -946 1281 -697 C
ATOM 855 N GLY A 184 26.550 6.858 -14.639 1.00 61.93 N
ANISOU 855 N GLY A 184 5501 10458 7569 -390 1132 -548 N
ATOM 856 CA GLY A 184 25.490 6.905 -13.647 1.00 53.68 C
ANISOU 856 CA GLY A 184 4575 9228 6593 -322 1031 -460 C
ATOM 857 C GLY A 184 25.135 5.543 -13.088 1.00 46.86 C
ANISOU 857 C GLY A 184 3747 8290 5770 -113 995 -479 C
ATOM 858 O GLY A 184 24.737 5.430 -11.927 1.00 48.90 O
ANISOU 858 O GLY A 184 4044 8453 6084 -24 912 -449 O
ATOM 859 N VAL A 185 25.274 4.494 -13.900 1.00 54.09 N
ANISOU 859 N VAL A 185 4655 9243 6652 -34 1062 -532 N
ATOM 860 CA VAL A 185 24.914 3.152 -13.451 1.00 51.16 C
ANISOU 860 CA VAL A 185 4334 8787 6316 163 1037 -551 C
ATOM 861 C VAL A 185 25.766 2.742 -12.256 1.00 53.19 C
ANISOU 861 C VAL A 185 4487 9111 6610 314 975 -620 C
ATOM 862 O VAL A 185 25.257 2.224 -11.256 1.00 47.00 O
ANISOU 862 O VAL A 185 3775 8212 5872 434 903 -589 O
ATOM 863 CB VAL A 185 25.051 2.151 -14.611 1.00 65.96 C
ANISOU 863 CB VAL A 185 6211 10706 8144 217 1132 -611 C
ATOM 864 CG1 VAL A 185 24.851 0.728 -14.116 1.00 66.34 C
ANISOU 864 CG1 VAL A 185 6305 10673 8230 430 1111 -647 C
ATOM 865 CG2 VAL A 185 24.057 2.484 -15.707 1.00 64.81 C
ANISOU 865 CG2 VAL A 185 6190 10477 7956 81 1179 -535 C
ATOM 866 N HIS A 186 27.079 2.965 -12.342 1.00 57.19 N
ANISOU 866 N HIS A 186 4824 9811 7093 307 1002 -720 N
ATOM 867 CA HIS A 186 27.953 2.610 -11.230 1.00 55.43 C
ANISOU 867 CA HIS A 186 4491 9670 6899 455 934 -797 C
ATOM 868 C HIS A 186 27.631 3.427 -9.988 1.00 50.52 C
ANISOU 868 C HIS A 186 3904 8975 6316 419 839 -730 C
ATOM 869 O HIS A 186 27.746 2.921 -8.866 1.00 54.96 O
ANISOU 869 O HIS A 186 4466 9509 6907 569 759 -744 O
ATOM 870 CB HIS A 186 29.417 2.794 -11.631 1.00 58.45 C
ANISOU 870 CB HIS A 186 4668 10293 7249 435 985 -929 C
ATOM 871 CG HIS A 186 29.987 1.628 -12.376 1.00 57.26 C
ANISOU 871 CG HIS A 186 4452 10232 7074 570 1050 -1035 C
ATOM 872 ND1 HIS A 186 30.693 0.621 -11.753 1.00 60.71 N
ANISOU 872 ND1 HIS A 186 4807 10730 7532 794 1001 -1134 N
ATOM 873 CD2 HIS A 186 29.948 1.302 -13.690 1.00 64.98 C
ANISOU 873 CD2 HIS A 186 5438 11245 8005 520 1159 -1062 C
ATOM 874 CE1 HIS A 186 31.070 -0.271 -12.651 1.00 66.60 C
ANISOU 874 CE1 HIS A 186 5511 11542 8252 881 1078 -1221 C
ATOM 875 NE2 HIS A 186 30.631 0.118 -13.835 1.00 70.01 N
ANISOU 875 NE2 HIS A 186 5997 11963 8641 714 1179 -1181 N
ATOM 876 N LEU A 187 27.234 4.690 -10.162 1.00 52.80 N
ANISOU 876 N LEU A 187 4229 9231 6601 227 845 -658 N
ATOM 877 CA LEU A 187 26.824 5.497 -9.017 1.00 54.47 C
ANISOU 877 CA LEU A 187 4489 9357 6852 191 761 -594 C
ATOM 878 C LEU A 187 25.489 5.031 -8.447 1.00 58.24 C
ANISOU 878 C LEU A 187 5138 9626 7366 264 708 -500 C
ATOM 879 O LEU A 187 25.284 5.095 -7.229 1.00 56.08 O
ANISOU 879 O LEU A 187 4893 9290 7123 328 631 -477 O
ATOM 880 CB LEU A 187 26.740 6.971 -9.409 1.00 52.71 C
ANISOU 880 CB LEU A 187 4268 9144 6618 -28 785 -546 C
ATOM 881 CG LEU A 187 28.073 7.722 -9.471 1.00 63.24 C
ANISOU 881 CG LEU A 187 5426 10675 7926 -123 816 -635 C
ATOM 882 CD1 LEU A 187 28.860 7.370 -10.727 1.00 68.60 C
ANISOU 882 CD1 LEU A 187 6003 11511 8549 -163 920 -718 C
ATOM 883 CD2 LEU A 187 27.843 9.223 -9.389 1.00 72.81 C
ANISOU 883 CD2 LEU A 187 6671 11849 9145 -318 808 -571 C
ATOM 884 N LEU A 188 24.572 4.568 -9.298 1.00 48.60 N
ANISOU 884 N LEU A 188 4028 8299 6138 248 752 -451 N
ATOM 885 CA LEU A 188 23.302 4.053 -8.796 1.00 46.27 C
ANISOU 885 CA LEU A 188 3884 7817 5879 311 711 -376 C
ATOM 886 C LEU A 188 23.529 2.867 -7.869 1.00 45.02 C
ANISOU 886 C LEU A 188 3727 7642 5737 510 668 -417 C
ATOM 887 O LEU A 188 23.002 2.828 -6.751 1.00 52.60 O
ANISOU 887 O LEU A 188 4756 8505 6726 561 602 -375 O
ATOM 888 CB LEU A 188 22.394 3.661 -9.963 1.00 42.48 C
ANISOU 888 CB LEU A 188 3505 7252 5384 264 772 -337 C
ATOM 889 CG LEU A 188 21.805 4.814 -10.782 1.00 41.21 C
ANISOU 889 CG LEU A 188 3392 7060 5207 77 792 -271 C
ATOM 890 CD1 LEU A 188 21.014 4.281 -11.966 1.00 33.33 C
ANISOU 890 CD1 LEU A 188 2483 6000 4183 51 850 -247 C
ATOM 891 CD2 LEU A 188 20.931 5.713 -9.920 1.00 41.09 C
ANISOU 891 CD2 LEU A 188 3455 6922 5237 18 718 -194 C
ATOM 892 N LEU A 189 24.318 1.887 -8.313 1.00 34.64 N
ANISOU 892 N LEU A 189 2343 6421 4400 629 705 -501 N
ATOM 893 CA LEU A 189 24.642 0.768 -7.436 1.00 38.35 C
ANISOU 893 CA LEU A 189 2814 6877 4879 835 656 -545 C
ATOM 894 C LEU A 189 25.445 1.238 -6.233 1.00 48.50 C
ANISOU 894 C LEU A 189 4008 8250 6168 881 574 -577 C
ATOM 895 O LEU A 189 25.160 0.846 -5.096 1.00 46.97 O
ANISOU 895 O LEU A 189 3880 7979 5988 989 502 -552 O
ATOM 896 CB LEU A 189 25.415 -0.300 -8.207 1.00 52.24 C
ANISOU 896 CB LEU A 189 4508 8728 6615 961 709 -643 C
ATOM 897 CG LEU A 189 24.720 -0.860 -9.447 1.00 51.11 C
ANISOU 897 CG LEU A 189 4451 8510 6459 926 798 -628 C
ATOM 898 CD1 LEU A 189 25.466 -2.082 -9.958 1.00 36.97 C
ANISOU 898 CD1 LEU A 189 2610 6786 4649 1094 840 -733 C
ATOM 899 CD2 LEU A 189 23.266 -1.192 -9.148 1.00 43.97 C
ANISOU 899 CD2 LEU A 189 3726 7395 5584 917 784 -534 C
ATOM 900 N ALA A 190 26.444 2.093 -6.464 1.00 51.61 N
ANISOU 900 N ALA A 190 4253 8811 6546 795 587 -635 N
ATOM 901 CA ALA A 190 27.253 2.601 -5.362 1.00 50.41 C
ANISOU 901 CA ALA A 190 4001 8756 6396 828 512 -678 C
ATOM 902 C ALA A 190 26.398 3.392 -4.383 1.00 47.44 C
ANISOU 902 C ALA A 190 3726 8254 6046 753 454 -584 C
ATOM 903 O ALA A 190 26.452 3.167 -3.169 1.00 48.43 O
ANISOU 903 O ALA A 190 3870 8355 6176 860 375 -584 O
ATOM 904 CB ALA A 190 28.388 3.467 -5.905 1.00 47.62 C
ANISOU 904 CB ALA A 190 3470 8600 6024 713 553 -760 C
ATOM 905 N ALA A 191 25.592 4.322 -4.896 1.00 46.41 N
ANISOU 905 N ALA A 191 3665 8041 5929 575 490 -507 N
ATOM 906 CA ALA A 191 24.698 5.077 -4.030 1.00 65.85 C
ANISOU 906 CA ALA A 191 6226 10375 8419 508 441 -424 C
ATOM 907 C ALA A 191 23.616 4.198 -3.422 1.00 58.60 C
ANISOU 907 C ALA A 191 5455 9293 7518 612 411 -365 C
ATOM 908 O ALA A 191 22.987 4.601 -2.438 1.00 42.11 O
ANISOU 908 O ALA A 191 3437 7115 5449 599 361 -315 O
ATOM 909 CB ALA A 191 24.054 6.227 -4.805 1.00 55.70 C
ANISOU 909 CB ALA A 191 4987 9033 7145 312 481 -360 C
ATOM 910 N THR A 192 23.391 3.008 -3.980 1.00 49.14 N
ANISOU 910 N THR A 192 4303 8055 6311 711 446 -376 N
ATOM 911 CA THR A 192 22.370 2.113 -3.450 1.00 46.37 C
ANISOU 911 CA THR A 192 4095 7550 5975 801 428 -326 C
ATOM 912 C THR A 192 22.915 1.290 -2.290 1.00 46.09 C
ANISOU 912 C THR A 192 4053 7536 5922 988 361 -363 C
ATOM 913 O THR A 192 22.379 1.329 -1.177 1.00 57.46 O
ANISOU 913 O THR A 192 5570 8894 7367 1018 309 -319 O
ATOM 914 CB THR A 192 21.849 1.195 -4.561 1.00 40.27 C
ANISOU 914 CB THR A 192 3386 6714 5201 822 498 -324 C
ATOM 915 OG1 THR A 192 21.023 1.946 -5.460 1.00 34.76 O
ANISOU 915 OG1 THR A 192 2732 5958 4516 654 544 -272 O
ATOM 916 CG2 THR A 192 21.046 0.042 -3.981 1.00 42.54 C
ANISOU 916 CG2 THR A 192 3804 6862 5499 944 485 -299 C
ATOM 917 N TRP A 193 23.991 0.543 -2.532 1.00 42.17 N
ANISOU 917 N TRP A 193 3469 7154 5402 1121 358 -447 N
ATOM 918 CA TRP A 193 24.488 -0.374 -1.516 1.00 44.84 C
ANISOU 918 CA TRP A 193 3820 7500 5717 1326 284 -483 C
ATOM 919 C TRP A 193 25.195 0.357 -0.384 1.00 49.82 C
ANISOU 919 C TRP A 193 4368 8228 6335 1339 202 -509 C
ATOM 920 O TRP A 193 25.162 -0.104 0.762 1.00 51.40 O
ANISOU 920 O TRP A 193 4630 8385 6514 1469 127 -498 O
ATOM 921 CB TRP A 193 25.415 -1.395 -2.164 1.00 44.91 C
ANISOU 921 CB TRP A 193 3759 7599 5706 1479 299 -577 C
ATOM 922 CG TRP A 193 24.691 -2.272 -3.112 1.00 44.67 C
ANISOU 922 CG TRP A 193 3832 7456 5686 1494 373 -557 C
ATOM 923 CD1 TRP A 193 24.607 -2.127 -4.464 1.00 48.77 C
ANISOU 923 CD1 TRP A 193 4315 8005 6212 1388 465 -572 C
ATOM 924 CD2 TRP A 193 23.918 -3.428 -2.781 1.00 51.92 C
ANISOU 924 CD2 TRP A 193 4916 8209 6604 1618 365 -521 C
ATOM 925 NE1 TRP A 193 23.836 -3.131 -4.998 1.00 50.12 N
ANISOU 925 NE1 TRP A 193 4612 8042 6390 1441 514 -554 N
ATOM 926 CE2 TRP A 193 23.400 -3.943 -3.984 1.00 45.27 C
ANISOU 926 CE2 TRP A 193 4123 7307 5772 1581 454 -525 C
ATOM 927 CE3 TRP A 193 23.618 -4.081 -1.582 1.00 54.20 C
ANISOU 927 CE3 TRP A 193 5321 8415 6856 1769 286 -494 C
ATOM 928 CZ2 TRP A 193 22.601 -5.081 -4.023 1.00 49.55 C
ANISOU 928 CZ2 TRP A 193 4821 7719 6287 1691 468 -511 C
ATOM 929 CZ3 TRP A 193 22.826 -5.209 -1.623 1.00 49.18 C
ANISOU 929 CZ3 TRP A 193 4852 7645 6188 1881 300 -470 C
ATOM 930 CH2 TRP A 193 22.325 -5.699 -2.834 1.00 49.66 C
ANISOU 930 CH2 TRP A 193 4954 7652 6264 1840 391 -482 C
ATOM 931 N THR A 194 25.839 1.489 -0.675 1.00 47.87 N
ANISOU 931 N THR A 194 3986 8109 6094 1207 215 -544 N
ATOM 932 CA THR A 194 26.447 2.265 0.399 1.00 48.76 C
ANISOU 932 CA THR A 194 4021 8307 6199 1201 142 -571 C
ATOM 933 C THR A 194 25.394 2.762 1.380 1.00 48.02 C
ANISOU 933 C THR A 194 4054 8074 6118 1143 109 -480 C
ATOM 934 O THR A 194 25.681 2.929 2.571 1.00 53.89 O
ANISOU 934 O THR A 194 4788 8844 6845 1208 31 -492 O
ATOM 935 CB THR A 194 27.238 3.443 -0.174 1.00 50.17 C
ANISOU 935 CB THR A 194 4043 8633 6386 1044 176 -623 C
ATOM 936 OG1 THR A 194 26.391 4.234 -1.016 1.00 63.48 O
ANISOU 936 OG1 THR A 194 5789 10233 8096 851 248 -550 O
ATOM 937 CG2 THR A 194 28.432 2.945 -0.976 1.00 55.63 C
ANISOU 937 CG2 THR A 194 4582 9497 7059 1114 204 -736 C
ATOM 938 N VAL A 195 24.173 2.990 0.906 1.00 46.39 N
ANISOU 938 N VAL A 195 3962 7724 5939 1026 164 -396 N
ATOM 939 CA VAL A 195 23.076 3.392 1.782 1.00 57.13 C
ANISOU 939 CA VAL A 195 5441 8951 7316 975 141 -318 C
ATOM 940 C VAL A 195 22.387 2.177 2.385 1.00 59.66 C
ANISOU 940 C VAL A 195 5896 9153 7619 1117 123 -282 C
ATOM 941 O VAL A 195 22.170 2.110 3.598 1.00 62.75 O
ANISOU 941 O VAL A 195 6344 9506 7991 1182 67 -261 O
ATOM 942 CB VAL A 195 22.075 4.274 1.004 1.00 50.88 C
ANISOU 942 CB VAL A 195 4701 8066 6564 786 202 -255 C
ATOM 943 CG1 VAL A 195 20.878 4.615 1.873 1.00 34.84 C
ANISOU 943 CG1 VAL A 195 2786 5898 4554 743 183 -188 C
ATOM 944 CG2 VAL A 195 22.752 5.540 0.509 1.00 42.16 C
ANISOU 944 CG2 VAL A 195 3483 7065 5470 646 215 -284 C
ATOM 945 N SER A 196 22.049 1.195 1.548 1.00 50.37 N
ANISOU 945 N SER A 196 4778 7917 6445 1168 174 -276 N
ATOM 946 CA SER A 196 21.332 0.022 2.033 1.00 49.66 C
ANISOU 946 CA SER A 196 4833 7697 6340 1292 167 -241 C
ATOM 947 C SER A 196 22.099 -0.656 3.160 1.00 59.73 C
ANISOU 947 C SER A 196 6116 9021 7556 1495 78 -274 C
ATOM 948 O SER A 196 21.536 -0.958 4.219 1.00 67.87 O
ANISOU 948 O SER A 196 7259 9995 8535 1578 36 -234 O
ATOM 949 CB SER A 196 21.093 -0.951 0.879 1.00 55.69 C
ANISOU 949 CB SER A 196 5639 8409 7113 1328 234 -252 C
ATOM 950 OG SER A 196 20.402 -0.315 -0.181 1.00 40.96 O
ANISOU 950 OG SER A 196 3767 6512 5285 1152 306 -225 O
ATOM 951 N LEU A 197 23.394 -0.898 2.953 1.00 58.63 N
ANISOU 951 N LEU A 197 5861 9014 7403 1593 43 -355 N
ATOM 952 CA LEU A 197 24.215 -1.462 4.017 1.00 53.05 C
ANISOU 952 CA LEU A 197 5151 8382 6625 1803 -63 -403 C
ATOM 953 C LEU A 197 24.284 -0.517 5.208 1.00 53.12 C
ANISOU 953 C LEU A 197 5133 8427 6622 1754 -126 -389 C
ATOM 954 O LEU A 197 24.158 -0.948 6.360 1.00 53.60 O
ANISOU 954 O LEU A 197 5291 8466 6609 1898 -203 -374 O
ATOM 955 CB LEU A 197 25.615 -1.769 3.488 1.00 60.91 C
ANISOU 955 CB LEU A 197 5995 9527 7620 1902 -86 -510 C
ATOM 956 CG LEU A 197 25.698 -2.928 2.491 1.00 64.01 C
ANISOU 956 CG LEU A 197 6421 9895 8004 2015 -43 -545 C
ATOM 957 CD1 LEU A 197 26.976 -2.848 1.667 1.00 67.60 C
ANISOU 957 CD1 LEU A 197 6685 10520 8481 2032 -29 -654 C
ATOM 958 CD2 LEU A 197 25.614 -4.263 3.218 1.00 59.07 C
ANISOU 958 CD2 LEU A 197 5955 9194 7296 2273 -121 -547 C
ATOM 959 N GLY A 198 24.460 0.780 4.951 1.00 55.95 N
ANISOU 959 N GLY A 198 5376 8851 7033 1566 -98 -396 N
ATOM 960 CA GLY A 198 24.527 1.732 6.046 1.00 49.09 C
ANISOU 960 CA GLY A 198 4480 8016 6156 1514 -155 -390 C
ATOM 961 C GLY A 198 23.301 1.666 6.934 1.00 54.64 C
ANISOU 961 C GLY A 198 5342 8576 6841 1508 -160 -306 C
ATOM 962 O GLY A 198 23.413 1.642 8.161 1.00 53.12 O
ANISOU 962 O GLY A 198 5185 8413 6583 1611 -240 -311 O
ATOM 963 N LEU A 199 22.114 1.612 6.326 1.00 54.09 N
ANISOU 963 N LEU A 199 5367 8376 6809 1405 -79 -239 N
ATOM 964 CA LEU A 199 20.897 1.442 7.111 1.00 52.47 C
ANISOU 964 CA LEU A 199 5306 8066 6566 1419 -73 -171 C
ATOM 965 C LEU A 199 20.918 0.121 7.867 1.00 52.40 C
ANISOU 965 C LEU A 199 5425 8041 6442 1664 -127 -164 C
ATOM 966 O LEU A 199 20.509 0.055 9.033 1.00 54.53 O
ANISOU 966 O LEU A 199 5793 8288 6637 1745 -170 -131 O
ATOM 967 CB LEU A 199 19.668 1.520 6.204 1.00 51.11 C
ANISOU 967 CB LEU A 199 5197 7767 6457 1274 25 -116 C
ATOM 968 CG LEU A 199 19.119 2.913 5.876 1.00 47.46 C
ANISOU 968 CG LEU A 199 4690 7260 6082 1049 63 -96 C
ATOM 969 CD1 LEU A 199 18.679 3.630 7.141 1.00 46.03 C
ANISOU 969 CD1 LEU A 199 4536 7068 5888 1023 25 -76 C
ATOM 970 CD2 LEU A 199 20.139 3.747 5.117 1.00 45.63 C
ANISOU 970 CD2 LEU A 199 4316 7155 5867 972 60 -146 C
ATOM 971 N GLY A 200 21.394 -0.945 7.220 1.00 49.10 N
ANISOU 971 N GLY A 200 5028 7624 6003 1794 -126 -193 N
ATOM 972 CA GLY A 200 21.493 -2.231 7.883 1.00 52.97 C
ANISOU 972 CA GLY A 200 5675 8070 6384 2043 -187 -187 C
ATOM 973 C GLY A 200 22.505 -2.261 9.006 1.00 58.63 C
ANISOU 973 C GLY A 200 6369 8884 7025 2203 -313 -237 C
ATOM 974 O GLY A 200 22.408 -3.116 9.893 1.00 58.31 O
ANISOU 974 O GLY A 200 6504 8778 6874 2400 -379 -213 O
ATOM 975 N LEU A 201 23.475 -1.347 8.990 1.00 55.87 N
ANISOU 975 N LEU A 201 5825 8678 6726 2124 -348 -307 N
ATOM 976 CA LEU A 201 24.480 -1.285 10.041 1.00 56.82 C
ANISOU 976 CA LEU A 201 5900 8908 6782 2266 -472 -368 C
ATOM 977 C LEU A 201 24.084 -0.357 11.181 1.00 53.90 C
ANISOU 977 C LEU A 201 5545 8549 6385 2195 -508 -339 C
ATOM 978 O LEU A 201 24.592 -0.520 12.296 1.00 57.44 O
ANISOU 978 O LEU A 201 6031 9047 6746 2347 -620 -368 O
ATOM 979 CB LEU A 201 25.824 -0.837 9.456 1.00 54.56 C
ANISOU 979 CB LEU A 201 5387 8785 6558 2235 -493 -472 C
ATOM 980 CG LEU A 201 26.451 -1.765 8.410 1.00 54.19 C
ANISOU 980 CG LEU A 201 5297 8765 6527 2338 -473 -528 C
ATOM 981 CD1 LEU A 201 27.761 -1.182 7.897 1.00 59.62 C
ANISOU 981 CD1 LEU A 201 5748 9633 7271 2292 -484 -634 C
ATOM 982 CD2 LEU A 201 26.671 -3.160 8.972 1.00 57.15 C
ANISOU 982 CD2 LEU A 201 5828 9089 6798 2625 -566 -542 C
ATOM 983 N LEU A 202 23.174 0.584 10.941 1.00 58.06 N
ANISOU 983 N LEU A 202 6053 9026 6981 1978 -422 -286 N
ATOM 984 CA LEU A 202 22.707 1.461 12.010 1.00 57.95 C
ANISOU 984 CA LEU A 202 6059 9018 6942 1913 -450 -262 C
ATOM 985 C LEU A 202 22.261 0.704 13.253 1.00 59.05 C
ANISOU 985 C LEU A 202 6396 9102 6941 2110 -518 -220 C
ATOM 986 O LEU A 202 22.594 1.152 14.364 1.00 61.94 O
ANISOU 986 O LEU A 202 6755 9533 7245 2161 -605 -246 O
ATOM 987 CB LEU A 202 21.562 2.345 11.495 1.00 60.67 C
ANISOU 987 CB LEU A 202 6398 9278 7376 1680 -341 -203 C
ATOM 988 CG LEU A 202 21.956 3.476 10.544 1.00 66.63 C
ANISOU 988 CG LEU A 202 6992 10067 8258 1462 -291 -234 C
ATOM 989 CD1 LEU A 202 20.718 4.199 10.047 1.00 57.76 C
ANISOU 989 CD1 LEU A 202 5907 8823 7214 1265 -198 -172 C
ATOM 990 CD2 LEU A 202 22.907 4.452 11.221 1.00 71.34 C
ANISOU 990 CD2 LEU A 202 7462 10784 8860 1429 -364 -297 C
ATOM 991 N PRO A 203 21.530 -0.410 13.163 1.00 62.39 N
ANISOU 991 N PRO A 203 7013 9394 7298 2227 -484 -154 N
ATOM 992 CA PRO A 203 21.158 -1.116 14.397 1.00 71.11 C
ANISOU 992 CA PRO A 203 8350 10419 8249 2419 -550 -102 C
ATOM 993 C PRO A 203 22.353 -1.546 15.226 1.00 80.52 C
ANISOU 993 C PRO A 203 9560 11683 9350 2622 -701 -167 C
ATOM 994 O PRO A 203 22.234 -1.664 16.451 1.00 79.39 O
ANISOU 994 O PRO A 203 9568 11511 9084 2737 -780 -140 O
ATOM 995 CB PRO A 203 20.358 -2.324 13.883 1.00 69.89 C
ANISOU 995 CB PRO A 203 8407 10093 8055 2500 -476 -27 C
ATOM 996 CG PRO A 203 20.690 -2.434 12.432 1.00 79.45 C
ANISOU 996 CG PRO A 203 9467 11332 9387 2409 -412 -70 C
ATOM 997 CD PRO A 203 20.905 -1.031 11.984 1.00 70.56 C
ANISOU 997 CD PRO A 203 8095 10328 8388 2179 -378 -114 C
ATOM 998 N VAL A 204 23.505 -1.783 14.602 1.00 74.98 N
ANISOU 998 N VAL A 204 8712 11077 8700 2674 -744 -252 N
ATOM 999 CA VAL A 204 24.667 -2.317 15.308 1.00 74.42 C
ANISOU 999 CA VAL A 204 8653 11076 8548 2891 -893 -323 C
ATOM 1000 C VAL A 204 25.458 -1.160 15.896 1.00 81.21 C
ANISOU 1000 C VAL A 204 9311 12106 9439 2817 -964 -401 C
ATOM 1001 O VAL A 204 26.536 -1.360 16.465 1.00 83.88 O
ANISOU 1001 O VAL A 204 9601 12542 9730 2971 -1092 -479 O
ATOM 1002 CB VAL A 204 25.553 -3.172 14.380 1.00 81.93 C
ANISOU 1002 CB VAL A 204 9536 12058 9534 3006 -909 -390 C
ATOM 1003 CG1 VAL A 204 26.766 -3.732 15.132 1.00 73.91 C
ANISOU 1003 CG1 VAL A 204 8526 11120 8437 3249 -1074 -473 C
ATOM 1004 CG2 VAL A 204 24.746 -4.304 13.759 1.00 94.77 C
ANISOU 1004 CG2 VAL A 204 11369 13505 11135 3068 -836 -316 C
ATOM 1005 N LEU A 205 24.938 0.060 15.765 1.00 66.72 N
ANISOU 1005 N LEU A 205 7361 10305 7684 2584 -885 -385 N
ATOM 1006 CA LEU A 205 25.568 1.219 16.375 1.00 68.64 C
ANISOU 1006 CA LEU A 205 7440 10687 7955 2497 -945 -452 C
ATOM 1007 C LEU A 205 24.695 1.865 17.437 1.00 82.52 C
ANISOU 1007 C LEU A 205 9297 12406 9650 2443 -955 -400 C
ATOM 1008 O LEU A 205 25.082 2.905 17.981 1.00103.51 O
ANISOU 1008 O LEU A 205 11832 15167 12331 2354 -999 -453 O
ATOM 1009 CB LEU A 205 25.941 2.271 15.318 1.00 67.41 C
ANISOU 1009 CB LEU A 205 7050 10614 7951 2260 -858 -496 C
ATOM 1010 CG LEU A 205 27.169 1.967 14.456 1.00 68.13 C
ANISOU 1010 CG LEU A 205 6979 10810 8097 2304 -872 -583 C
ATOM 1011 CD1 LEU A 205 26.845 0.952 13.382 1.00 68.58 C
ANISOU 1011 CD1 LEU A 205 7109 10777 8173 2351 -796 -547 C
ATOM 1012 CD2 LEU A 205 27.733 3.242 13.836 1.00 59.18 C
ANISOU 1012 CD2 LEU A 205 5627 9779 7080 2082 -820 -636 C
ATOM 1013 N GLY A 206 23.539 1.286 17.755 1.00 75.83 N
ANISOU 1013 N GLY A 206 8673 11416 8722 2496 -913 -303 N
ATOM 1014 CA GLY A 206 22.700 1.839 18.799 1.00 70.53 C
ANISOU 1014 CA GLY A 206 8107 10716 7974 2463 -922 -256 C
ATOM 1015 C GLY A 206 21.245 1.952 18.404 1.00 67.99 C
ANISOU 1015 C GLY A 206 7875 10281 7677 2343 -784 -164 C
ATOM 1016 O GLY A 206 20.377 2.096 19.267 1.00 74.55 O
ANISOU 1016 O GLY A 206 8853 11062 8412 2360 -780 -106 O
ATOM 1017 N TRP A 207 20.962 1.889 17.103 1.00 74.00 N
ANISOU 1017 N TRP A 207 8555 11003 8561 2222 -672 -149 N
ATOM 1018 CA TRP A 207 19.594 2.016 16.600 1.00 68.50 C
ANISOU 1018 CA TRP A 207 7916 10203 7908 2099 -538 -70 C
ATOM 1019 C TRP A 207 18.837 0.696 16.755 1.00 62.64 C
ANISOU 1019 C TRP A 207 7445 9305 7050 2263 -504 25 C
ATOM 1020 O TRP A 207 18.399 0.077 15.788 1.00 74.55 O
ANISOU 1020 O TRP A 207 8993 10723 8610 2240 -414 62 O
ATOM 1021 CB TRP A 207 19.609 2.464 15.145 1.00 66.48 C
ANISOU 1021 CB TRP A 207 7489 9948 7821 1900 -441 -91 C
ATOM 1022 CG TRP A 207 19.882 3.917 14.958 1.00 65.09 C
ANISOU 1022 CG TRP A 207 7123 9848 7760 1687 -433 -144 C
ATOM 1023 CD1 TRP A 207 18.970 4.887 14.673 1.00 73.05 C
ANISOU 1023 CD1 TRP A 207 8089 10810 8858 1488 -351 -121 C
ATOM 1024 CD2 TRP A 207 21.154 4.571 15.038 1.00 68.13 C
ANISOU 1024 CD2 TRP A 207 7352 10352 8182 1656 -508 -229 C
ATOM 1025 NE1 TRP A 207 19.591 6.108 14.570 1.00 71.90 N
ANISOU 1025 NE1 TRP A 207 7797 10723 8799 1338 -374 -178 N
ATOM 1026 CE2 TRP A 207 20.933 5.941 14.790 1.00 68.88 C
ANISOU 1026 CE2 TRP A 207 7338 10449 8384 1434 -464 -243 C
ATOM 1027 CE3 TRP A 207 22.457 4.133 15.294 1.00 70.80 C
ANISOU 1027 CE3 TRP A 207 7635 10790 8475 1800 -609 -296 C
ATOM 1028 CZ2 TRP A 207 21.965 6.876 14.792 1.00 72.72 C
ANISOU 1028 CZ2 TRP A 207 7675 11029 8926 1349 -510 -313 C
ATOM 1029 CZ3 TRP A 207 23.481 5.063 15.296 1.00 81.13 C
ANISOU 1029 CZ3 TRP A 207 8769 12214 9844 1712 -653 -375 C
ATOM 1030 CH2 TRP A 207 23.229 6.419 15.046 1.00 82.53 C
ANISOU 1030 CH2 TRP A 207 8851 12386 10120 1486 -600 -379 C
ATOM 1031 N ASN A 208 18.673 0.276 18.007 1.00 50.91 N
ANISOU 1031 N ASN A 208 6179 7769 5398 2419 -576 69 N
ATOM 1032 CA ASN A 208 17.922 -0.928 18.344 1.00 50.44 C
ANISOU 1032 CA ASN A 208 6453 7513 5200 2555 -541 178 C
ATOM 1033 C ASN A 208 16.909 -0.578 19.425 1.00 47.39 C
ANISOU 1033 C ASN A 208 6258 7067 4683 2535 -514 262 C
ATOM 1034 O ASN A 208 16.823 0.567 19.876 1.00 54.85 O
ANISOU 1034 O ASN A 208 7050 8140 5650 2441 -535 222 O
ATOM 1035 CB ASN A 208 18.843 -2.067 18.804 1.00 55.82 C
ANISOU 1035 CB ASN A 208 7309 8134 5767 2769 -661 164 C
ATOM 1036 CG ASN A 208 19.567 -1.743 20.086 1.00 53.86 C
ANISOU 1036 CG ASN A 208 7086 7969 5411 2863 -810 123 C
ATOM 1037 OD1 ASN A 208 19.302 -2.330 21.133 1.00 51.90 O
ANISOU 1037 OD1 ASN A 208 7134 7596 4990 2970 -858 190 O
ATOM 1038 ND2 ASN A 208 20.493 -0.800 20.009 1.00 60.48 N
ANISOU 1038 ND2 ASN A 208 7629 9003 6346 2803 -878 12 N
ATOM 1039 N CYS A 209 16.136 -1.581 19.844 1.00 46.34 N
ANISOU 1039 N CYS A 209 6485 6722 4398 2601 -458 378 N
ATOM 1040 CA CYS A 209 15.030 -1.381 20.772 1.00 43.58 C
ANISOU 1040 CA CYS A 209 6384 6280 3893 2515 -381 474 C
ATOM 1041 C CYS A 209 15.247 -2.062 22.114 1.00 46.54 C
ANISOU 1041 C CYS A 209 7093 6543 4047 2613 -462 515 C
ATOM 1042 O CYS A 209 14.294 -2.183 22.893 1.00 50.69 O
ANISOU 1042 O CYS A 209 7901 6945 4416 2503 -360 596 O
ATOM 1043 CB CYS A 209 13.731 -1.898 20.155 1.00 40.22 C
ANISOU 1043 CB CYS A 209 6107 5653 3521 2314 -151 536 C
ATOM 1044 SG CYS A 209 13.608 -3.710 20.109 1.00 39.94 S
ANISOU 1044 SG CYS A 209 6505 5342 3330 2470 -134 654 S
ATOM 1045 N LEU A 210 16.465 -2.508 22.409 1.00 49.03 N
ANISOU 1045 N LEU A 210 7381 6897 4350 2783 -624 449 N
ATOM 1046 CA LEU A 210 16.739 -3.267 23.620 1.00 51.43 C
ANISOU 1046 CA LEU A 210 8002 7080 4462 2892 -713 487 C
ATOM 1047 C LEU A 210 16.979 -2.382 24.839 1.00 44.13 C
ANISOU 1047 C LEU A 210 7053 6279 3435 2875 -810 451 C
ATOM 1048 O LEU A 210 17.586 -2.841 25.813 1.00 43.43 O
ANISOU 1048 O LEU A 210 7134 6152 3216 2997 -936 449 O
ATOM 1049 CB LEU A 210 17.942 -4.185 23.393 1.00 66.19 C
ANISOU 1049 CB LEU A 210 9861 8937 6350 3100 -849 430 C
ATOM 1050 CG LEU A 210 17.801 -5.189 22.245 1.00 54.90 C
ANISOU 1050 CG LEU A 210 8484 7377 4998 3133 -768 452 C
ATOM 1051 CD1 LEU A 210 19.070 -6.011 22.094 1.00 53.67 C
ANISOU 1051 CD1 LEU A 210 8304 7241 4846 3343 -915 378 C
ATOM 1052 CD2 LEU A 210 16.595 -6.096 22.452 1.00 52.44 C
ANISOU 1052 CD2 LEU A 210 8570 6787 4568 3051 -626 582 C
ATOM 1053 N ALA A 211 16.519 -1.137 24.809 1.00 53.86 N
ANISOU 1053 N ALA A 211 8085 7658 4720 2728 -759 419 N
ATOM 1054 CA ALA A 211 16.643 -0.218 25.929 1.00 48.47 C
ANISOU 1054 CA ALA A 211 7379 7097 3940 2686 -836 374 C
ATOM 1055 C ALA A 211 15.315 -0.105 26.670 1.00 53.55 C
ANISOU 1055 C ALA A 211 8304 7627 4416 2512 -678 455 C
ATOM 1056 O ALA A 211 14.245 -0.392 26.128 1.00 57.16 O
ANISOU 1056 O ALA A 211 8873 7964 4880 2380 -488 525 O
ATOM 1057 CB ALA A 211 17.094 1.162 25.445 1.00 53.94 C
ANISOU 1057 CB ALA A 211 7649 8038 4807 2617 -885 253 C
ATOM 1058 N GLU A 212 15.398 0.314 27.935 1.00 55.24 N
ANISOU 1058 N GLU A 212 8627 7881 4479 2491 -743 432 N
ATOM 1059 CA GLU A 212 14.193 0.492 28.736 1.00 55.54 C
ANISOU 1059 CA GLU A 212 8912 7831 4359 2293 -572 477 C
ATOM 1060 C GLU A 212 13.358 1.680 28.273 1.00 65.32 C
ANISOU 1060 C GLU A 212 9932 9192 5696 2093 -422 410 C
ATOM 1061 O GLU A 212 12.171 1.753 28.607 1.00 69.44 O
ANISOU 1061 O GLU A 212 10597 9615 6173 1878 -208 424 O
ATOM 1062 CB GLU A 212 14.561 0.665 30.210 1.00 47.94 C
ANISOU 1062 CB GLU A 212 8107 6892 3215 2320 -684 457 C
ATOM 1063 N ARG A 213 13.944 2.605 27.514 1.00 71.20 N
ANISOU 1063 N ARG A 213 10271 10110 6672 2095 -500 305 N
ATOM 1064 CA ARG A 213 13.252 3.792 27.022 1.00 64.25 C
ANISOU 1064 CA ARG A 213 9107 9296 6008 1858 -359 210 C
ATOM 1065 C ARG A 213 13.045 3.724 25.511 1.00 58.22 C
ANISOU 1065 C ARG A 213 8116 8504 5500 1798 -268 213 C
ATOM 1066 O ARG A 213 13.153 4.728 24.807 1.00 57.91 O
ANISOU 1066 O ARG A 213 7752 8577 5673 1706 -267 128 O
ATOM 1067 CB ARG A 213 14.021 5.057 27.400 1.00 67.85 C
ANISOU 1067 CB ARG A 213 9300 9963 6518 1868 -513 83 C
ATOM 1068 CG ARG A 213 13.210 6.345 27.286 1.00 73.81 C
ANISOU 1068 CG ARG A 213 9854 10759 7433 1626 -377 -18 C
ATOM 1069 CD ARG A 213 12.143 6.442 28.372 1.00 78.04 C
ANISOU 1069 CD ARG A 213 10637 11213 7803 1489 -229 -23 C
ATOM 1070 NE ARG A 213 12.604 7.181 29.543 1.00 83.54 N
ANISOU 1070 NE ARG A 213 11356 12030 8356 1514 -354 -107 N
ATOM 1071 CZ ARG A 213 12.382 8.471 29.759 1.00 71.59 C
ANISOU 1071 CZ ARG A 213 9652 10605 6943 1381 -335 -236 C
ATOM 1072 NH1 ARG A 213 11.710 9.215 28.894 1.00 63.69 N
ANISOU 1072 NH1 ARG A 213 8423 9587 6189 1221 -207 -293 N
ATOM 1073 NH2 ARG A 213 12.844 9.031 30.874 1.00 68.27 N
ANISOU 1073 NH2 ARG A 213 9285 10289 6367 1415 -457 -312 N
ATOM 1074 N ALA A 214 12.744 2.532 24.999 1.00 54.31 N
ANISOU 1074 N ALA A 214 7809 7849 4976 1846 -193 314 N
ATOM 1075 CA ALA A 214 12.527 2.335 23.572 1.00 46.44 C
ANISOU 1075 CA ALA A 214 6635 6816 4196 1796 -106 322 C
ATOM 1076 C ALA A 214 11.609 1.140 23.380 1.00 45.56 C
ANISOU 1076 C ALA A 214 6818 6480 4011 1741 57 425 C
ATOM 1077 O ALA A 214 11.887 0.055 23.899 1.00 59.82 O
ANISOU 1077 O ALA A 214 8935 8172 5624 1888 2 513 O
ATOM 1078 CB ALA A 214 13.851 2.114 22.832 1.00 45.08 C
ANISOU 1078 CB ALA A 214 6273 6754 4102 2010 -288 304 C
ATOM 1079 N ALA A 215 10.526 1.338 22.636 1.00 43.33 N
ANISOU 1079 N ALA A 215 6445 6135 3884 1531 249 411 N
ATOM 1080 CA ALA A 215 9.542 0.291 22.408 1.00 47.10 C
ANISOU 1080 CA ALA A 215 7173 6409 4312 1432 425 489 C
ATOM 1081 C ALA A 215 9.907 -0.508 21.164 1.00 43.69 C
ANISOU 1081 C ALA A 215 6695 5915 3988 1531 402 528 C
ATOM 1082 O ALA A 215 10.148 0.066 20.097 1.00 31.13 O
ANISOU 1082 O ALA A 215 4797 4426 2604 1513 381 471 O
ATOM 1083 CB ALA A 215 8.144 0.889 22.259 1.00 52.97 C
ANISOU 1083 CB ALA A 215 7830 7129 5167 1156 639 435 C
ATOM 1084 N CYS A 216 9.942 -1.829 21.305 1.00 45.75 N
ANISOU 1084 N CYS A 216 7281 6001 4102 1631 408 624 N
ATOM 1085 CA CYS A 216 10.313 -2.699 20.204 1.00 45.30 C
ANISOU 1085 CA CYS A 216 7222 5866 4124 1745 384 656 C
ATOM 1086 C CYS A 216 9.185 -2.793 19.184 1.00 42.22 C
ANISOU 1086 C CYS A 216 6757 5393 3894 1522 581 643 C
ATOM 1087 O CYS A 216 8.012 -2.547 19.480 1.00 36.21 O
ANISOU 1087 O CYS A 216 6043 4578 3135 1291 752 632 O
ATOM 1088 CB CYS A 216 10.671 -4.092 20.715 1.00 40.91 C
ANISOU 1088 CB CYS A 216 7068 5122 3354 1927 321 760 C
ATOM 1089 SG CYS A 216 12.266 -4.158 21.562 1.00 47.55 S
ANISOU 1089 SG CYS A 216 7955 6075 4038 2275 27 765 S
ATOM 1090 N SER A 217 9.567 -3.145 17.963 1.00 44.71 N
ANISOU 1090 N SER A 217 6939 5708 4341 1597 553 632 N
ATOM 1091 CA SER A 217 8.638 -3.314 16.863 1.00 46.34 C
ANISOU 1091 CA SER A 217 7069 5842 4698 1417 709 617 C
ATOM 1092 C SER A 217 8.288 -4.789 16.713 1.00 31.27 C
ANISOU 1092 C SER A 217 5502 3696 2685 1438 783 695 C
ATOM 1093 O SER A 217 8.699 -5.641 17.502 1.00 32.65 O
ANISOU 1093 O SER A 217 5989 3749 2667 1583 720 769 O
ATOM 1094 CB SER A 217 9.237 -2.759 15.570 1.00 43.96 C
ANISOU 1094 CB SER A 217 6422 5686 4595 1465 642 553 C
ATOM 1095 OG SER A 217 10.372 -3.512 15.178 1.00 38.83 O
ANISOU 1095 OG SER A 217 5810 5034 3908 1714 512 569 O
ATOM 1096 N VAL A 218 7.513 -5.090 15.671 1.00 34.49 N
ANISOU 1096 N VAL A 218 5858 4029 3217 1289 911 677 N
ATOM 1097 CA VAL A 218 7.130 -6.468 15.406 1.00 31.70 C
ANISOU 1097 CA VAL A 218 5817 3443 2784 1282 990 739 C
ATOM 1098 C VAL A 218 8.326 -7.314 14.990 1.00 37.18 C
ANISOU 1098 C VAL A 218 6604 4089 3434 1573 837 766 C
ATOM 1099 O VAL A 218 8.272 -8.546 15.085 1.00 47.81 O
ANISOU 1099 O VAL A 218 8288 5216 4661 1638 856 832 O
ATOM 1100 CB VAL A 218 6.026 -6.507 14.332 1.00 32.53 C
ANISOU 1100 CB VAL A 218 5809 3505 3047 1048 1152 693 C
ATOM 1101 CG1 VAL A 218 6.538 -5.940 13.014 1.00 33.45 C
ANISOU 1101 CG1 VAL A 218 5581 3773 3355 1109 1079 626 C
ATOM 1102 CG2 VAL A 218 5.511 -7.921 14.148 1.00 40.68 C
ANISOU 1102 CG2 VAL A 218 7184 4283 3990 998 1251 749 C
ATOM 1103 N VAL A 219 9.402 -6.691 14.529 1.00 39.84 N
ANISOU 1103 N VAL A 219 6651 4621 3863 1747 689 711 N
ATOM 1104 CA VAL A 219 10.613 -7.400 14.122 1.00 35.38 C
ANISOU 1104 CA VAL A 219 6118 4052 3272 2042 538 709 C
ATOM 1105 C VAL A 219 11.735 -6.899 15.023 1.00 36.91 C
ANISOU 1105 C VAL A 219 6240 4402 3383 2255 350 699 C
ATOM 1106 O VAL A 219 12.422 -5.923 14.714 1.00 47.29 O
ANISOU 1106 O VAL A 219 7208 5951 4809 2297 266 623 O
ATOM 1107 CB VAL A 219 10.942 -7.193 12.642 1.00 35.34 C
ANISOU 1107 CB VAL A 219 5815 4159 3451 2055 540 632 C
ATOM 1108 CG1 VAL A 219 10.044 -8.065 11.779 1.00 40.43 C
ANISOU 1108 CG1 VAL A 219 6614 4612 4135 1920 685 645 C
ATOM 1109 CG2 VAL A 219 10.782 -5.727 12.253 1.00 32.56 C
ANISOU 1109 CG2 VAL A 219 5076 4035 3259 1891 562 564 C
ATOM 1110 N ARG A 220 11.947 -7.587 16.141 1.00 36.44 N
ANISOU 1110 N ARG A 220 6509 4213 3123 2379 280 767 N
ATOM 1111 CA ARG A 220 12.998 -7.193 17.058 1.00 36.61 C
ANISOU 1111 CA ARG A 220 6449 4388 3074 2533 97 720 C
ATOM 1112 C ARG A 220 14.353 -7.548 16.459 1.00 38.22 C
ANISOU 1112 C ARG A 220 6460 4714 3348 2724 -53 614 C
ATOM 1113 O ARG A 220 14.448 -8.430 15.604 1.00 44.46 O
ANISOU 1113 O ARG A 220 7304 5410 4178 2762 -26 596 O
ATOM 1114 CB ARG A 220 12.824 -7.881 18.409 1.00 36.46 C
ANISOU 1114 CB ARG A 220 6803 4202 2847 2541 76 779 C
ATOM 1115 N PRO A 221 15.427 -6.874 16.893 1.00 37.58 N
ANISOU 1115 N PRO A 221 6153 4846 3278 2822 -206 534 N
ATOM 1116 CA PRO A 221 15.477 -5.789 17.886 1.00 39.55 C
ANISOU 1116 CA PRO A 221 6311 5232 3483 2787 -262 531 C
ATOM 1117 C PRO A 221 15.190 -4.413 17.292 1.00 37.91 C
ANISOU 1117 C PRO A 221 5751 5216 3435 2641 -204 493 C
ATOM 1118 O PRO A 221 15.597 -3.406 17.862 1.00 41.38 O
ANISOU 1118 O PRO A 221 6009 5830 3883 2622 -283 443 O
ATOM 1119 CB PRO A 221 16.922 -5.864 18.419 1.00 43.82 C
ANISOU 1119 CB PRO A 221 6755 5905 3988 2962 -457 438 C
ATOM 1120 CG PRO A 221 17.546 -7.104 17.806 1.00 43.67 C
ANISOU 1120 CG PRO A 221 6828 5795 3968 3103 -499 408 C
ATOM 1121 CD PRO A 221 16.776 -7.347 16.553 1.00 41.01 C
ANISOU 1121 CD PRO A 221 6462 5380 3741 2988 -346 434 C
ATOM 1122 N LEU A 222 14.513 -4.328 16.150 1.00 36.47 N
ANISOU 1122 N LEU A 222 5464 5005 3387 2527 -70 506 N
ATOM 1123 CA LEU A 222 14.241 -3.032 15.545 1.00 39.41 C
ANISOU 1123 CA LEU A 222 5497 5550 3929 2374 -14 458 C
ATOM 1124 C LEU A 222 13.179 -2.279 16.340 1.00 42.82 C
ANISOU 1124 C LEU A 222 5985 5950 4336 2137 92 479 C
ATOM 1125 O LEU A 222 12.156 -2.846 16.736 1.00 35.69 O
ANISOU 1125 O LEU A 222 5355 4858 3348 2020 218 545 O
ATOM 1126 CB LEU A 222 13.785 -3.206 14.097 1.00 48.11 C
ANISOU 1126 CB LEU A 222 6478 6615 5187 2260 112 440 C
ATOM 1127 CG LEU A 222 14.780 -3.903 13.168 1.00 52.72 C
ANISOU 1127 CG LEU A 222 6982 7233 5815 2321 48 369 C
ATOM 1128 CD1 LEU A 222 14.082 -4.409 11.919 1.00 49.37 C
ANISOU 1128 CD1 LEU A 222 6573 6702 5482 2234 180 384 C
ATOM 1129 CD2 LEU A 222 15.911 -2.958 12.800 1.00 61.03 C
ANISOU 1129 CD2 LEU A 222 7702 8518 6970 2247 -47 257 C
ATOM 1130 N ALA A 223 13.427 -0.991 16.566 1.00 44.38 N
ANISOU 1130 N ALA A 223 5920 6334 4608 2057 45 412 N
ATOM 1131 CA ALA A 223 12.506 -0.160 17.323 1.00 37.01 C
ANISOU 1131 CA ALA A 223 5007 5394 3663 1851 133 406 C
ATOM 1132 C ALA A 223 11.378 0.343 16.432 1.00 36.08 C
ANISOU 1132 C ALA A 223 4757 5238 3714 1603 302 387 C
ATOM 1133 O ALA A 223 11.533 0.484 15.216 1.00 35.16 O
ANISOU 1133 O ALA A 223 4443 5170 3745 1578 317 360 O
ATOM 1134 CB ALA A 223 13.246 1.022 17.949 1.00 35.40 C
ANISOU 1134 CB ALA A 223 4589 5391 3469 1874 2 333 C
ATOM 1135 N ARG A 224 10.227 0.616 17.053 1.00 42.92 N
ANISOU 1135 N ARG A 224 5735 6024 4550 1420 430 395 N
ATOM 1136 CA ARG A 224 9.092 1.129 16.294 1.00 42.79 C
ANISOU 1136 CA ARG A 224 5586 5979 4693 1196 577 363 C
ATOM 1137 C ARG A 224 9.436 2.453 15.627 1.00 37.18 C
ANISOU 1137 C ARG A 224 4532 5434 4161 1138 518 288 C
ATOM 1138 O ARG A 224 8.989 2.729 14.508 1.00 35.92 O
ANISOU 1138 O ARG A 224 4221 5274 4155 1032 578 270 O
ATOM 1139 CB ARG A 224 7.873 1.299 17.200 1.00 42.28 C
ANISOU 1139 CB ARG A 224 5666 5834 4564 1023 715 358 C
ATOM 1140 CG ARG A 224 7.302 -0.005 17.720 1.00 44.06 C
ANISOU 1140 CG ARG A 224 6245 5873 4623 1012 819 435 C
ATOM 1141 CD ARG A 224 5.865 0.153 18.204 1.00 46.25 C
ANISOU 1141 CD ARG A 224 6602 6080 4890 778 1009 409 C
ATOM 1142 NE ARG A 224 4.936 0.392 17.103 1.00 43.46 N
ANISOU 1142 NE ARG A 224 6068 5714 4731 614 1120 361 N
ATOM 1143 CZ ARG A 224 4.516 1.586 16.706 1.00 46.84 C
ANISOU 1143 CZ ARG A 224 6217 6250 5330 511 1128 276 C
ATOM 1144 NH1 ARG A 224 4.908 2.698 17.307 1.00 61.38 N
ANISOU 1144 NH1 ARG A 224 7921 8215 7184 537 1046 223 N
ATOM 1145 NH2 ARG A 224 3.680 1.668 15.675 1.00 36.40 N
ANISOU 1145 NH2 ARG A 224 4760 4903 4167 383 1212 241 N
ATOM 1146 N SER A 225 10.234 3.283 16.299 1.00 31.21 N
ANISOU 1146 N SER A 225 3664 4816 3379 1201 395 244 N
ATOM 1147 CA SER A 225 10.596 4.576 15.732 1.00 38.66 C
ANISOU 1147 CA SER A 225 4306 5903 4481 1130 338 175 C
ATOM 1148 C SER A 225 11.342 4.409 14.417 1.00 34.68 C
ANISOU 1148 C SER A 225 3631 5464 4080 1188 294 175 C
ATOM 1149 O SER A 225 11.062 5.115 13.441 1.00 39.93 O
ANISOU 1149 O SER A 225 4193 6079 4899 979 301 142 O
ATOM 1150 CB SER A 225 11.446 5.360 16.731 1.00 43.38 C
ANISOU 1150 CB SER A 225 4834 6635 5015 1196 204 123 C
ATOM 1151 OG SER A 225 12.017 6.505 16.126 1.00 69.19 O
ANISOU 1151 OG SER A 225 7822 10042 8427 1138 135 59 O
ATOM 1152 N HIS A 226 12.289 3.473 14.367 1.00 36.91 N
ANISOU 1152 N HIS A 226 3982 5767 4276 1382 215 200 N
ATOM 1153 CA HIS A 226 13.136 3.339 13.189 1.00 36.67 C
ANISOU 1153 CA HIS A 226 3870 5733 4330 1313 155 169 C
ATOM 1154 C HIS A 226 12.429 2.589 12.068 1.00 36.04 C
ANISOU 1154 C HIS A 226 3847 5537 4309 1261 261 206 C
ATOM 1155 O HIS A 226 12.528 2.980 10.900 1.00 36.34 O
ANISOU 1155 O HIS A 226 3791 5548 4469 1097 259 171 O
ATOM 1156 CB HIS A 226 14.439 2.642 13.573 1.00 37.54 C
ANISOU 1156 CB HIS A 226 4024 5905 4333 1512 34 153 C
ATOM 1157 CG HIS A 226 15.159 3.308 14.703 1.00 47.27 C
ANISOU 1157 CG HIS A 226 5210 7253 5498 1567 -81 107 C
ATOM 1158 ND1 HIS A 226 15.866 2.606 15.656 1.00 49.68 N
ANISOU 1158 ND1 HIS A 226 5639 7590 5650 1790 -187 112 N
ATOM 1159 CD2 HIS A 226 15.274 4.615 15.038 1.00 54.14 C
ANISOU 1159 CD2 HIS A 226 5945 8197 6430 1423 -112 52 C
ATOM 1160 CE1 HIS A 226 16.387 3.452 16.527 1.00 55.49 C
ANISOU 1160 CE1 HIS A 226 6295 8434 6355 1779 -279 57 C
ATOM 1161 NE2 HIS A 226 16.043 4.678 16.174 1.00 58.23 N
ANISOU 1161 NE2 HIS A 226 6481 8811 6832 1559 -230 19 N
ATOM 1162 N VAL A 227 11.704 1.517 12.396 1.00 31.74 N
ANISOU 1162 N VAL A 227 3488 4897 3673 1402 363 276 N
ATOM 1163 CA VAL A 227 10.951 0.812 11.364 1.00 34.42 C
ANISOU 1163 CA VAL A 227 3892 5118 4070 1334 480 304 C
ATOM 1164 C VAL A 227 9.897 1.729 10.767 1.00 31.82 C
ANISOU 1164 C VAL A 227 3449 4759 3882 1063 549 274 C
ATOM 1165 O VAL A 227 9.565 1.620 9.580 1.00 26.11 O
ANISOU 1165 O VAL A 227 2691 3979 3251 940 567 257 O
ATOM 1166 CB VAL A 227 10.317 -0.476 11.929 1.00 38.27 C
ANISOU 1166 CB VAL A 227 4711 5406 4426 1376 555 368 C
ATOM 1167 CG1 VAL A 227 11.387 -1.404 12.463 1.00 42.97 C
ANISOU 1167 CG1 VAL A 227 5464 5984 4878 1632 441 395 C
ATOM 1168 CG2 VAL A 227 9.299 -0.145 13.001 1.00 39.05 C
ANISOU 1168 CG2 VAL A 227 4936 5432 4469 1233 634 381 C
ATOM 1169 N ALA A 228 9.344 2.637 11.574 1.00 40.87 N
ANISOU 1169 N ALA A 228 4554 5934 5043 973 571 254 N
ATOM 1170 CA ALA A 228 8.362 3.583 11.056 1.00 35.48 C
ANISOU 1170 CA ALA A 228 3787 5194 4501 727 591 201 C
ATOM 1171 C ALA A 228 8.984 4.530 10.037 1.00 29.10 C
ANISOU 1171 C ALA A 228 2858 4387 3812 604 466 134 C
ATOM 1172 O ALA A 228 8.384 4.803 8.990 1.00 20.90 O
ANISOU 1172 O ALA A 228 1808 3266 2869 466 469 91 O
ATOM 1173 CB ALA A 228 7.743 4.371 12.205 1.00 42.85 C
ANISOU 1173 CB ALA A 228 4711 6151 5418 673 631 176 C
ATOM 1174 N LEU A 229 10.182 5.044 10.320 1.00 40.71 N
ANISOU 1174 N LEU A 229 4263 5938 5266 656 366 117 N
ATOM 1175 CA LEU A 229 10.841 5.909 9.349 1.00 43.04 C
ANISOU 1175 CA LEU A 229 4488 6202 5665 543 295 68 C
ATOM 1176 C LEU A 229 11.142 5.147 8.066 1.00 33.21 C
ANISOU 1176 C LEU A 229 3256 4928 4434 547 306 71 C
ATOM 1177 O LEU A 229 10.949 5.672 6.964 1.00 39.48 O
ANISOU 1177 O LEU A 229 4034 5659 5309 433 304 41 O
ATOM 1178 CB LEU A 229 12.119 6.504 9.943 1.00 39.55 C
ANISOU 1178 CB LEU A 229 3977 5857 5193 593 208 52 C
ATOM 1179 CG LEU A 229 11.960 7.389 11.185 1.00 47.07 C
ANISOU 1179 CG LEU A 229 4902 6856 6126 586 182 36 C
ATOM 1180 CD1 LEU A 229 13.206 8.238 11.394 1.00 50.99 C
ANISOU 1180 CD1 LEU A 229 5319 7422 6632 576 95 2 C
ATOM 1181 CD2 LEU A 229 10.720 8.272 11.103 1.00 41.22 C
ANISOU 1181 CD2 LEU A 229 4173 6000 5489 444 230 15 C
ATOM 1182 N LEU A 230 11.602 3.900 8.187 1.00 25.25 N
ANISOU 1182 N LEU A 230 2289 3975 3330 706 319 111 N
ATOM 1183 CA LEU A 230 11.784 3.073 7.000 1.00 24.33 C
ANISOU 1183 CA LEU A 230 2191 3831 3224 722 342 111 C
ATOM 1184 C LEU A 230 10.462 2.869 6.276 1.00 25.07 C
ANISOU 1184 C LEU A 230 2333 3827 3365 615 417 112 C
ATOM 1185 O LEU A 230 10.404 2.926 5.043 1.00 21.44 O
ANISOU 1185 O LEU A 230 1855 3330 2960 530 416 78 O
ATOM 1186 CB LEU A 230 12.391 1.724 7.382 1.00 34.24 C
ANISOU 1186 CB LEU A 230 3516 5130 4362 943 345 149 C
ATOM 1187 CG LEU A 230 13.838 1.735 7.874 1.00 27.56 C
ANISOU 1187 CG LEU A 230 2620 4391 3462 1065 248 120 C
ATOM 1188 CD1 LEU A 230 14.243 0.354 8.333 1.00 26.07 C
ANISOU 1188 CD1 LEU A 230 2553 4204 3150 1308 236 148 C
ATOM 1189 CD2 LEU A 230 14.772 2.218 6.788 1.00 20.09 C
ANISOU 1189 CD2 LEU A 230 1561 3478 2595 970 215 65 C
ATOM 1190 N SER A 231 9.389 2.623 7.028 1.00 29.89 N
ANISOU 1190 N SER A 231 3008 4400 3949 617 489 147 N
ATOM 1191 CA SER A 231 8.079 2.452 6.410 1.00 22.19 C
ANISOU 1191 CA SER A 231 2072 3342 3019 498 556 134 C
ATOM 1192 C SER A 231 7.621 3.740 5.740 1.00 21.99 C
ANISOU 1192 C SER A 231 1985 3289 3080 325 489 42 C
ATOM 1193 O SER A 231 7.182 3.732 4.585 1.00 20.58 O
ANISOU 1193 O SER A 231 1809 3089 2922 252 482 13 O
ATOM 1194 CB SER A 231 7.063 1.999 7.457 1.00 20.19 C
ANISOU 1194 CB SER A 231 1907 3044 2720 516 671 182 C
ATOM 1195 OG SER A 231 5.802 1.753 6.863 1.00 17.38 O
ANISOU 1195 OG SER A 231 1586 2613 2404 386 731 161 O
ATOM 1196 N ALA A 232 7.728 4.866 6.448 1.00 31.76 N
ANISOU 1196 N ALA A 232 3183 4530 4353 284 445 5 N
ATOM 1197 CA ALA A 232 7.334 6.138 5.855 1.00 24.42 C
ANISOU 1197 CA ALA A 232 2211 3591 3475 189 401 -22 C
ATOM 1198 C ALA A 232 8.197 6.461 4.644 1.00 26.27 C
ANISOU 1198 C ALA A 232 2410 3843 3727 182 360 -4 C
ATOM 1199 O ALA A 232 7.696 6.943 3.623 1.00 32.15 O
ANISOU 1199 O ALA A 232 3155 4574 4489 116 348 -17 O
ATOM 1200 CB ALA A 232 7.425 7.254 6.893 1.00 33.67 C
ANISOU 1200 CB ALA A 232 3347 4763 4683 175 373 -42 C
ATOM 1201 N ALA A 233 9.500 6.195 4.739 1.00 28.74 N
ANISOU 1201 N ALA A 233 2693 4207 4021 254 340 22 N
ATOM 1202 CA ALA A 233 10.378 6.420 3.597 1.00 28.41 C
ANISOU 1202 CA ALA A 233 2609 4204 3981 243 318 32 C
ATOM 1203 C ALA A 233 9.990 5.524 2.429 1.00 27.08 C
ANISOU 1203 C ALA A 233 2473 4015 3802 237 356 32 C
ATOM 1204 O ALA A 233 10.020 5.953 1.270 1.00 33.73 O
ANISOU 1204 O ALA A 233 3298 4859 4659 181 350 32 O
ATOM 1205 CB ALA A 233 11.833 6.180 3.997 1.00 33.72 C
ANISOU 1205 CB ALA A 233 3230 4964 4617 329 290 40 C
ATOM 1206 N PHE A 234 9.619 4.275 2.717 1.00 18.90 N
ANISOU 1206 N PHE A 234 1488 2958 2737 297 399 32 N
ATOM 1207 CA PHE A 234 9.241 3.352 1.651 1.00 15.69 C
ANISOU 1207 CA PHE A 234 1113 2531 2319 293 439 27 C
ATOM 1208 C PHE A 234 8.006 3.840 0.904 1.00 16.67 C
ANISOU 1208 C PHE A 234 1254 2620 2461 185 440 13 C
ATOM 1209 O PHE A 234 7.939 3.743 -0.326 1.00 19.79 O
ANISOU 1209 O PHE A 234 1643 3018 2859 151 446 8 O
ATOM 1210 CB PHE A 234 9.002 1.961 2.234 1.00 23.52 C
ANISOU 1210 CB PHE A 234 2170 3497 3268 384 494 35 C
ATOM 1211 CG PHE A 234 8.295 1.021 1.298 1.00 24.53 C
ANISOU 1211 CG PHE A 234 2344 3597 3378 375 553 45 C
ATOM 1212 CD1 PHE A 234 8.834 0.715 0.061 1.00 23.92 C
ANISOU 1212 CD1 PHE A 234 2243 3540 3307 377 552 20 C
ATOM 1213 CD2 PHE A 234 7.098 0.429 1.666 1.00 23.43 C
ANISOU 1213 CD2 PHE A 234 2275 3403 3223 359 625 83 C
ATOM 1214 CE1 PHE A 234 8.185 -0.155 -0.797 1.00 22.37 C
ANISOU 1214 CE1 PHE A 234 2089 3320 3091 372 610 27 C
ATOM 1215 CE2 PHE A 234 6.448 -0.441 0.814 1.00 26.98 C
ANISOU 1215 CE2 PHE A 234 2775 3808 3668 344 691 97 C
ATOM 1216 CZ PHE A 234 6.993 -0.733 -0.420 1.00 22.48 C
ANISOU 1216 CZ PHE A 234 2177 3270 3094 356 678 69 C
ATOM 1217 N PHE A 235 7.016 4.367 1.625 1.00 16.24 N
ANISOU 1217 N PHE A 235 1216 2545 2411 137 433 4 N
ATOM 1218 CA PHE A 235 5.816 4.858 0.957 1.00 18.39 C
ANISOU 1218 CA PHE A 235 1497 2806 2683 55 418 -3 C
ATOM 1219 C PHE A 235 6.160 5.967 -0.025 1.00 19.09 C
ANISOU 1219 C PHE A 235 1551 2902 2799 12 372 -5 C
ATOM 1220 O PHE A 235 5.720 5.952 -1.180 1.00 21.32 O
ANISOU 1220 O PHE A 235 1841 3181 3078 -26 367 0 O
ATOM 1221 CB PHE A 235 4.800 5.352 1.988 1.00 25.65 C
ANISOU 1221 CB PHE A 235 2426 3722 3596 27 414 -4 C
ATOM 1222 CG PHE A 235 3.908 4.273 2.523 1.00 16.49 C
ANISOU 1222 CG PHE A 235 1314 2539 2412 29 476 16 C
ATOM 1223 CD1 PHE A 235 2.762 3.909 1.841 1.00 18.17 C
ANISOU 1223 CD1 PHE A 235 1547 2718 2637 -20 493 36 C
ATOM 1224 CD2 PHE A 235 4.212 3.625 3.707 1.00 19.36 C
ANISOU 1224 CD2 PHE A 235 1707 2898 2753 78 528 14 C
ATOM 1225 CE1 PHE A 235 1.937 2.917 2.329 1.00 17.70 C
ANISOU 1225 CE1 PHE A 235 1538 2611 2576 -35 566 49 C
ATOM 1226 CE2 PHE A 235 3.391 2.633 4.198 1.00 18.16 C
ANISOU 1226 CE2 PHE A 235 1618 2708 2574 67 607 36 C
ATOM 1227 CZ PHE A 235 2.251 2.279 3.507 1.00 17.71 C
ANISOU 1227 CZ PHE A 235 1583 2608 2539 2 629 51 C
ATOM 1228 N MET A 236 6.964 6.935 0.412 1.00 23.70 N
ANISOU 1228 N MET A 236 2100 3493 3411 17 341 -6 N
ATOM 1229 CA MET A 236 7.318 8.040 -0.470 1.00 27.77 C
ANISOU 1229 CA MET A 236 2587 4014 3949 -28 307 4 C
ATOM 1230 C MET A 236 8.113 7.552 -1.674 1.00 24.65 C
ANISOU 1230 C MET A 236 2176 3641 3548 -23 328 26 C
ATOM 1231 O MET A 236 7.860 7.975 -2.808 1.00 25.42 O
ANISOU 1231 O MET A 236 2273 3736 3650 -72 319 37 O
ATOM 1232 CB MET A 236 8.105 9.092 0.306 1.00 37.25 C
ANISOU 1232 CB MET A 236 3749 5228 5178 -27 278 3 C
ATOM 1233 CG MET A 236 7.286 9.782 1.384 1.00 36.88 C
ANISOU 1233 CG MET A 236 3722 5162 5129 -39 254 -23 C
ATOM 1234 SD MET A 236 8.199 11.097 2.201 1.00 52.15 S
ANISOU 1234 SD MET A 236 5609 7102 7105 -46 218 -32 S
ATOM 1235 CE MET A 236 6.852 12.113 2.798 1.00 49.47 C
ANISOU 1235 CE MET A 236 5298 6774 6726 -80 187 -64 C
ATOM 1236 N VAL A 237 9.071 6.651 -1.452 1.00 35.53 N
ANISOU 1236 N VAL A 237 3537 5053 4909 41 355 33 N
ATOM 1237 CA VAL A 237 9.859 6.128 -2.563 1.00 26.11 C
ANISOU 1237 CA VAL A 237 2320 3903 3697 54 381 45 C
ATOM 1238 C VAL A 237 8.964 5.392 -3.551 1.00 24.26 C
ANISOU 1238 C VAL A 237 2124 3634 3458 30 412 33 C
ATOM 1239 O VAL A 237 9.079 5.574 -4.769 1.00 27.36 O
ANISOU 1239 O VAL A 237 2506 4042 3848 -9 422 45 O
ATOM 1240 CB VAL A 237 10.990 5.227 -2.038 1.00 29.27 C
ANISOU 1240 CB VAL A 237 2691 4359 4071 150 400 41 C
ATOM 1241 CG1 VAL A 237 11.658 4.498 -3.188 1.00 43.16 C
ANISOU 1241 CG1 VAL A 237 4426 6166 5807 175 439 35 C
ATOM 1242 CG2 VAL A 237 12.008 6.057 -1.262 1.00 32.66 C
ANISOU 1242 CG2 VAL A 237 3063 4849 4499 164 363 47 C
ATOM 1243 N PHE A 238 8.055 4.555 -3.044 1.00 24.06 N
ANISOU 1243 N PHE A 238 2144 3575 3423 46 432 11 N
ATOM 1244 CA PHE A 238 7.139 3.843 -3.929 1.00 22.26 C
ANISOU 1244 CA PHE A 238 1948 3330 3179 12 459 -7 C
ATOM 1245 C PHE A 238 6.162 4.797 -4.599 1.00 25.58 C
ANISOU 1245 C PHE A 238 2378 3731 3610 -67 416 0 C
ATOM 1246 O PHE A 238 5.700 4.525 -5.712 1.00 23.53 O
ANISOU 1246 O PHE A 238 2131 3465 3344 -104 426 -5 O
ATOM 1247 CB PHE A 238 6.384 2.770 -3.145 1.00 23.28 C
ANISOU 1247 CB PHE A 238 2121 3451 3272 41 489 -16 C
ATOM 1248 CG PHE A 238 5.772 1.705 -4.006 1.00 23.41 C
ANISOU 1248 CG PHE A 238 2170 3473 3251 27 528 -23 C
ATOM 1249 CD1 PHE A 238 4.561 1.916 -4.639 1.00 21.12 C
ANISOU 1249 CD1 PHE A 238 1891 3182 2950 -45 504 -3 C
ATOM 1250 CD2 PHE A 238 6.403 0.480 -4.169 1.00 30.51 C
ANISOU 1250 CD2 PHE A 238 3085 4382 4127 100 587 -43 C
ATOM 1251 CE1 PHE A 238 3.993 0.930 -5.429 1.00 25.64 C
ANISOU 1251 CE1 PHE A 238 2486 3763 3492 -58 539 11 C
ATOM 1252 CE2 PHE A 238 5.840 -0.507 -4.956 1.00 23.62 C
ANISOU 1252 CE2 PHE A 238 2243 3507 3224 102 642 -27 C
ATOM 1253 CZ PHE A 238 4.634 -0.283 -5.587 1.00 20.02 C
ANISOU 1253 CZ PHE A 238 1791 3056 2761 11 618 -3 C
ATOM 1254 N GLY A 239 5.825 5.907 -3.938 1.00 18.05 N
ANISOU 1254 N GLY A 239 1418 2769 2673 -88 371 8 N
ATOM 1255 CA GLY A 239 4.963 6.894 -4.560 1.00 17.01 C
ANISOU 1255 CA GLY A 239 1285 2623 2554 -145 327 17 C
ATOM 1256 C GLY A 239 5.608 7.576 -5.747 1.00 27.39 C
ANISOU 1256 C GLY A 239 2571 3943 3892 -178 320 40 C
ATOM 1257 O GLY A 239 4.923 7.932 -6.709 1.00 35.81 O
ANISOU 1257 O GLY A 239 3641 4998 4968 -222 299 50 O
ATOM 1258 N ILE A 240 6.925 7.774 -5.698 1.00 27.08 N
ANISOU 1258 N ILE A 240 2504 3933 3850 -159 333 62 N
ATOM 1259 CA ILE A 240 7.623 8.418 -6.806 1.00 25.47 C
ANISOU 1259 CA ILE A 240 2276 3765 3637 -201 330 101 C
ATOM 1260 C ILE A 240 7.839 7.440 -7.951 1.00 21.98 C
ANISOU 1260 C ILE A 240 1835 3346 3170 -201 378 106 C
ATOM 1261 O ILE A 240 7.722 7.806 -9.126 1.00 22.24 O
ANISOU 1261 O ILE A 240 1868 3395 3186 -255 374 135 O
ATOM 1262 CB ILE A 240 8.954 9.012 -6.313 1.00 28.02 C
ANISOU 1262 CB ILE A 240 2554 4141 3952 -194 328 115 C
ATOM 1263 CG1 ILE A 240 8.691 10.091 -5.260 1.00 30.05 C
ANISOU 1263 CG1 ILE A 240 2810 4369 4239 -204 283 108 C
ATOM 1264 CG2 ILE A 240 9.740 9.572 -7.488 1.00 32.39 C
ANISOU 1264 CG2 ILE A 240 3078 4756 4475 -253 339 151 C
ATOM 1265 CD1 ILE A 240 9.939 10.595 -4.560 1.00 21.98 C
ANISOU 1265 CD1 ILE A 240 1738 3396 3219 -196 281 109 C
ATOM 1266 N MET A 241 8.163 6.186 -7.632 1.00 30.68 N
ANISOU 1266 N MET A 241 2940 4454 4264 -140 427 79 N
ATOM 1267 CA MET A 241 8.365 5.187 -8.676 1.00 33.87 C
ANISOU 1267 CA MET A 241 3347 4878 4645 -131 485 75 C
ATOM 1268 C MET A 241 7.127 5.054 -9.552 1.00 30.37 C
ANISOU 1268 C MET A 241 2936 4387 4217 -183 483 74 C
ATOM 1269 O MET A 241 7.232 4.831 -10.764 1.00 27.60 O
ANISOU 1269 O MET A 241 2585 4062 3840 -210 512 94 O
ATOM 1270 CB MET A 241 8.731 3.847 -8.040 1.00 22.55 C
ANISOU 1270 CB MET A 241 1920 3443 3206 -49 536 36 C
ATOM 1271 CG MET A 241 10.078 3.876 -7.335 1.00 24.35 C
ANISOU 1271 CG MET A 241 2102 3735 3415 16 535 38 C
ATOM 1272 SD MET A 241 10.318 2.602 -6.081 1.00 25.71 S
ANISOU 1272 SD MET A 241 2292 3893 3584 128 558 1 S
ATOM 1273 CE MET A 241 10.119 1.110 -7.047 1.00 27.87 C
ANISOU 1273 CE MET A 241 2601 4151 3838 163 640 -41 C
ATOM 1274 N LEU A 242 5.943 5.195 -8.956 1.00 26.14 N
ANISOU 1274 N LEU A 242 2429 3796 3707 -198 444 48 N
ATOM 1275 CA LEU A 242 4.717 5.175 -9.746 1.00 24.97 C
ANISOU 1275 CA LEU A 242 2302 3610 3574 -246 423 42 C
ATOM 1276 C LEU A 242 4.660 6.364 -10.696 1.00 32.07 C
ANISOU 1276 C LEU A 242 3173 4531 4481 -306 378 90 C
ATOM 1277 O LEU A 242 4.254 6.224 -11.856 1.00 35.65 O
ANISOU 1277 O LEU A 242 3630 4987 4929 -346 377 110 O
ATOM 1278 CB LEU A 242 3.502 5.162 -8.819 1.00 24.59 C
ANISOU 1278 CB LEU A 242 2279 3551 3515 -254 382 -5 C
ATOM 1279 CG LEU A 242 3.364 3.919 -7.935 1.00 22.38 C
ANISOU 1279 CG LEU A 242 2024 3322 3157 -223 408 -24 C
ATOM 1280 CD1 LEU A 242 2.194 4.067 -6.978 1.00 17.62 C
ANISOU 1280 CD1 LEU A 242 1419 2735 2541 -224 368 25 C
ATOM 1281 CD2 LEU A 242 3.207 2.659 -8.772 1.00 28.01 C
ANISOU 1281 CD2 LEU A 242 2754 4086 3800 -233 441 -25 C
ATOM 1282 N HIS A 243 5.070 7.544 -10.225 1.00 27.38 N
ANISOU 1282 N HIS A 243 2568 3953 3881 -314 331 116 N
ATOM 1283 CA HIS A 243 5.034 8.727 -11.078 1.00 23.35 C
ANISOU 1283 CA HIS A 243 2054 3461 3358 -378 278 169 C
ATOM 1284 C HIS A 243 5.951 8.565 -12.282 1.00 25.09 C
ANISOU 1284 C HIS A 243 2271 3746 3516 -418 318 210 C
ATOM 1285 O HIS A 243 5.577 8.918 -13.406 1.00 32.57 O
ANISOU 1285 O HIS A 243 3232 4705 4437 -484 293 247 O
ATOM 1286 CB HIS A 243 5.420 9.966 -10.272 1.00 23.80 C
ANISOU 1286 CB HIS A 243 2101 3517 3426 -383 236 188 C
ATOM 1287 CG HIS A 243 5.604 11.193 -11.107 1.00 27.82 C
ANISOU 1287 CG HIS A 243 2611 4041 3917 -460 190 250 C
ATOM 1288 ND1 HIS A 243 4.732 11.546 -12.115 1.00 21.70 N
ANISOU 1288 ND1 HIS A 243 1854 3247 3144 -513 138 283 N
ATOM 1289 CD2 HIS A 243 6.561 12.151 -11.084 1.00 35.48 C
ANISOU 1289 CD2 HIS A 243 3570 5042 4867 -504 186 288 C
ATOM 1290 CE1 HIS A 243 5.144 12.668 -12.677 1.00 28.93 C
ANISOU 1290 CE1 HIS A 243 2782 4173 4036 -590 102 346 C
ATOM 1291 NE2 HIS A 243 6.252 13.057 -12.070 1.00 38.16 N
ANISOU 1291 NE2 HIS A 243 3935 5374 5193 -590 137 348 N
ATOM 1292 N LEU A 244 7.156 8.030 -12.069 1.00 32.98 N
ANISOU 1292 N LEU A 244 3251 4798 4483 -383 380 201 N
ATOM 1293 CA LEU A 244 8.075 7.830 -13.184 1.00 34.83 C
ANISOU 1293 CA LEU A 244 3475 5115 4645 -419 432 223 C
ATOM 1294 C LEU A 244 7.511 6.839 -14.189 1.00 33.39 C
ANISOU 1294 C LEU A 244 3318 4932 4437 -426 470 215 C
ATOM 1295 O LEU A 244 7.661 7.022 -15.403 1.00 39.20 O
ANISOU 1295 O LEU A 244 4057 5758 5080 -505 477 256 O
ATOM 1296 CB LEU A 244 9.431 7.349 -12.675 1.00 31.86 C
ANISOU 1296 CB LEU A 244 3055 4804 4247 -364 488 195 C
ATOM 1297 CG LEU A 244 10.373 8.427 -12.147 1.00 35.68 C
ANISOU 1297 CG LEU A 244 3498 5332 4725 -391 467 210 C
ATOM 1298 CD1 LEU A 244 11.635 7.790 -11.600 1.00 34.02 C
ANISOU 1298 CD1 LEU A 244 3231 5195 4502 -324 514 171 C
ATOM 1299 CD2 LEU A 244 10.708 9.421 -13.244 1.00 36.66 C
ANISOU 1299 CD2 LEU A 244 3624 5511 4793 -504 466 256 C
ATOM 1300 N TYR A 245 6.862 5.779 -13.705 1.00 27.97 N
ANISOU 1300 N TYR A 245 2644 4186 3799 -364 492 175 N
ATOM 1301 CA TYR A 245 6.276 4.812 -14.624 1.00 33.07 C
ANISOU 1301 CA TYR A 245 3298 4869 4396 -383 525 178 C
ATOM 1302 C TYR A 245 5.266 5.481 -15.548 1.00 31.36 C
ANISOU 1302 C TYR A 245 3085 4683 4146 -486 449 223 C
ATOM 1303 O TYR A 245 5.195 5.160 -16.740 1.00 36.11 O
ANISOU 1303 O TYR A 245 3694 5383 4645 -559 463 242 O
ATOM 1304 CB TYR A 245 5.618 3.671 -13.850 1.00 26.11 C
ANISOU 1304 CB TYR A 245 2430 3906 3583 -316 561 137 C
ATOM 1305 CG TYR A 245 5.018 2.629 -14.762 1.00 22.29 C
ANISOU 1305 CG TYR A 245 1953 3476 3039 -343 600 135 C
ATOM 1306 CD1 TYR A 245 5.806 1.632 -15.319 1.00 28.11 C
ANISOU 1306 CD1 TYR A 245 2700 4297 3684 -306 691 109 C
ATOM 1307 CD2 TYR A 245 3.669 2.653 -15.083 1.00 32.63 C
ANISOU 1307 CD2 TYR A 245 3258 4763 4377 -409 545 139 C
ATOM 1308 CE1 TYR A 245 5.267 0.682 -16.162 1.00 32.46 C
ANISOU 1308 CE1 TYR A 245 3272 4904 4159 -342 736 73 C
ATOM 1309 CE2 TYR A 245 3.119 1.706 -15.927 1.00 37.90 C
ANISOU 1309 CE2 TYR A 245 3934 5492 4974 -463 578 108 C
ATOM 1310 CZ TYR A 245 3.924 0.724 -16.463 1.00 34.92 C
ANISOU 1310 CZ TYR A 245 3583 5194 4492 -434 681 67 C
ATOM 1311 OH TYR A 245 3.382 -0.221 -17.305 1.00 47.91 O
ANISOU 1311 OH TYR A 245 5259 6888 6058 -502 730 -4 O
ATOM 1312 N VAL A 246 4.475 6.413 -15.019 1.00 17.58 N
ANISOU 1312 N VAL A 246 1338 2864 2478 -499 364 231 N
ATOM 1313 CA VAL A 246 3.567 7.172 -15.874 1.00 38.34 C
ANISOU 1313 CA VAL A 246 3964 5525 5080 -596 267 288 C
ATOM 1314 C VAL A 246 4.364 8.014 -16.860 1.00 37.69 C
ANISOU 1314 C VAL A 246 3900 5543 4878 -697 252 370 C
ATOM 1315 O VAL A 246 4.062 8.053 -18.059 1.00 34.36 O
ANISOU 1315 O VAL A 246 3498 5203 4354 -810 215 425 O
ATOM 1316 CB VAL A 246 2.627 8.041 -15.021 1.00 36.85 C
ANISOU 1316 CB VAL A 246 3765 5238 5000 -569 181 268 C
ATOM 1317 CG1 VAL A 246 1.784 8.942 -15.911 1.00 40.35 C
ANISOU 1317 CG1 VAL A 246 4201 5706 5424 -664 51 346 C
ATOM 1318 CG2 VAL A 246 1.748 7.159 -14.165 1.00 29.80 C
ANISOU 1318 CG2 VAL A 246 2861 4260 4201 -501 209 171 C
ATOM 1319 N ARG A 247 5.404 8.692 -16.370 1.00 27.71 N
ANISOU 1319 N ARG A 247 2636 4276 3617 -677 279 375 N
ATOM 1320 CA ARG A 247 6.260 9.459 -17.264 1.00 33.70 C
ANISOU 1320 CA ARG A 247 3416 5127 4261 -786 285 442 C
ATOM 1321 C ARG A 247 6.860 8.559 -18.334 1.00 30.22 C
ANISOU 1321 C ARG A 247 2989 4801 3694 -825 371 426 C
ATOM 1322 O ARG A 247 6.994 8.965 -19.494 1.00 31.40 O
ANISOU 1322 O ARG A 247 3184 5034 3712 -956 361 485 O
ATOM 1323 CB ARG A 247 7.355 10.164 -16.466 1.00 37.85 C
ANISOU 1323 CB ARG A 247 3925 5634 4825 -753 316 425 C
ATOM 1324 CG ARG A 247 6.844 11.322 -15.619 1.00 39.88 C
ANISOU 1324 CG ARG A 247 4184 5799 5169 -749 231 448 C
ATOM 1325 CD ARG A 247 7.949 11.941 -14.774 1.00 34.51 C
ANISOU 1325 CD ARG A 247 3483 5107 4523 -724 268 417 C
ATOM 1326 NE ARG A 247 9.024 12.497 -15.587 1.00 49.27 N
ANISOU 1326 NE ARG A 247 5357 7069 6296 -832 305 463 N
ATOM 1327 CZ ARG A 247 10.159 12.981 -15.099 1.00 56.07 C
ANISOU 1327 CZ ARG A 247 6185 7949 7170 -836 349 439 C
ATOM 1328 NH1 ARG A 247 10.410 12.980 -13.800 1.00 45.10 N
ANISOU 1328 NH1 ARG A 247 4750 6529 5857 -752 343 390 N
ATOM 1329 NH2 ARG A 247 11.066 13.476 -15.936 1.00 50.26 N
ANISOU 1329 NH2 ARG A 247 5454 7303 6340 -953 389 475 N
ATOM 1330 N ILE A 248 7.207 7.324 -17.967 1.00 31.12 N
ANISOU 1330 N ILE A 248 3076 4913 3835 -719 457 346 N
ATOM 1331 CA ILE A 248 7.658 6.357 -18.964 1.00 29.52 C
ANISOU 1331 CA ILE A 248 2886 4816 3516 -739 543 313 C
ATOM 1332 C ILE A 248 6.563 6.121 -19.995 1.00 28.76 C
ANISOU 1332 C ILE A 248 2833 4762 3332 -844 500 341 C
ATOM 1333 O ILE A 248 6.809 6.143 -21.206 1.00 40.90 O
ANISOU 1333 O ILE A 248 4421 6402 4718 -952 526 360 O
ATOM 1334 CB ILE A 248 8.079 5.042 -18.286 1.00 23.98 C
ANISOU 1334 CB ILE A 248 2156 4086 2870 -598 626 231 C
ATOM 1335 CG1 ILE A 248 9.360 5.248 -17.481 1.00 29.48 C
ANISOU 1335 CG1 ILE A 248 2810 4773 3617 -522 664 208 C
ATOM 1336 CG2 ILE A 248 8.258 3.958 -19.331 1.00 28.95 C
ANISOU 1336 CG2 ILE A 248 2807 4812 3381 -610 710 184 C
ATOM 1337 CD1 ILE A 248 9.722 4.081 -16.599 1.00 28.07 C
ANISOU 1337 CD1 ILE A 248 2613 4549 3504 -386 719 147 C
ATOM 1338 N CYS A 249 5.333 5.901 -19.528 1.00 33.13 N
ANISOU 1338 N CYS A 249 3373 5239 3978 -823 431 339 N
ATOM 1339 CA CYS A 249 4.223 5.717 -20.454 1.00 30.79 C
ANISOU 1339 CA CYS A 249 3103 4983 3613 -941 367 362 C
ATOM 1340 C CYS A 249 4.056 6.938 -21.345 1.00 35.67 C
ANISOU 1340 C CYS A 249 3776 5643 4132 -1100 266 477 C
ATOM 1341 O CYS A 249 3.928 6.812 -22.569 1.00 36.26 O
ANISOU 1341 O CYS A 249 3929 5803 4046 -1231 260 509 O
ATOM 1342 CB CYS A 249 2.935 5.444 -19.681 1.00 23.91 C
ANISOU 1342 CB CYS A 249 2186 4006 2893 -892 292 330 C
ATOM 1343 SG CYS A 249 2.907 3.850 -18.843 1.00 28.69 S
ANISOU 1343 SG CYS A 249 2772 4554 3574 -760 410 216 S
ATOM 1344 N GLN A 250 4.078 8.133 -20.752 1.00 33.46 N
ANISOU 1344 N GLN A 250 3488 5292 3934 -1094 184 541 N
ATOM 1345 CA GLN A 250 3.982 9.347 -21.550 1.00 31.10 C
ANISOU 1345 CA GLN A 250 3270 5005 3541 -1252 78 669 C
ATOM 1346 C GLN A 250 5.065 9.375 -22.617 1.00 33.23 C
ANISOU 1346 C GLN A 250 3630 5381 3613 -1347 175 687 C
ATOM 1347 O GLN A 250 4.805 9.741 -23.769 1.00 37.69 O
ANISOU 1347 O GLN A 250 4322 5981 4017 -1502 116 774 O
ATOM 1348 CB GLN A 250 4.085 10.573 -20.645 1.00 31.44 C
ANISOU 1348 CB GLN A 250 3294 4951 3699 -1214 7 715 C
ATOM 1349 CG GLN A 250 2.948 10.692 -19.650 1.00 30.24 C
ANISOU 1349 CG GLN A 250 3071 4683 3736 -1112 -96 685 C
ATOM 1350 CD GLN A 250 3.161 11.812 -18.654 1.00 32.89 C
ANISOU 1350 CD GLN A 250 3395 4928 4174 -1055 -133 702 C
ATOM 1351 OE1 GLN A 250 4.176 12.509 -18.689 1.00 39.44 O
ANISOU 1351 OE1 GLN A 250 4261 5782 4942 -1104 -90 741 O
ATOM 1352 NE2 GLN A 250 2.202 11.991 -17.755 1.00 34.84 N
ANISOU 1352 NE2 GLN A 250 3593 5072 4574 -954 -206 656 N
ATOM 1353 N VAL A 251 6.283 8.972 -22.257 1.00 33.46 N
ANISOU 1353 N VAL A 251 3610 5452 3652 -1252 313 599 N
ATOM 1354 CA VAL A 251 7.366 8.927 -23.232 1.00 42.46 C
ANISOU 1354 CA VAL A 251 4806 6692 4635 -1323 412 583 C
ATOM 1355 C VAL A 251 7.024 7.960 -24.356 1.00 38.23 C
ANISOU 1355 C VAL A 251 4339 6238 3950 -1377 454 550 C
ATOM 1356 O VAL A 251 7.153 8.287 -25.542 1.00 34.15 O
ANISOU 1356 O VAL A 251 3945 5775 3257 -1511 449 596 O
ATOM 1357 CB VAL A 251 8.687 8.542 -22.543 1.00 38.00 C
ANISOU 1357 CB VAL A 251 4145 6151 4142 -1198 535 488 C
ATOM 1358 CG1 VAL A 251 9.711 8.095 -23.571 1.00 50.80 C
ANISOU 1358 CG1 VAL A 251 5790 7889 5621 -1244 652 437 C
ATOM 1359 CG2 VAL A 251 9.216 9.712 -21.729 1.00 51.38 C
ANISOU 1359 CG2 VAL A 251 5809 7789 5924 -1198 500 525 C
ATOM 1360 N VAL A 252 6.574 6.756 -24.003 1.00 45.23 N
ANISOU 1360 N VAL A 252 5168 7123 4895 -1275 495 464 N
ATOM 1361 CA VAL A 252 6.259 5.772 -25.031 1.00 48.25 C
ANISOU 1361 CA VAL A 252 5623 7581 5129 -1322 544 412 C
ATOM 1362 C VAL A 252 5.079 6.244 -25.866 1.00 37.81 C
ANISOU 1362 C VAL A 252 4428 6237 3700 -1463 398 503 C
ATOM 1363 O VAL A 252 5.074 6.101 -27.094 1.00 38.15 O
ANISOU 1363 O VAL A 252 4611 6332 3552 -1548 394 503 O
ATOM 1364 CB VAL A 252 5.990 4.393 -24.404 1.00 40.52 C
ANISOU 1364 CB VAL A 252 4570 6581 4244 -1185 616 295 C
ATOM 1365 CG1 VAL A 252 5.879 3.341 -25.490 1.00 40.96 C
ANISOU 1365 CG1 VAL A 252 4713 6717 4131 -1222 690 214 C
ATOM 1366 CG2 VAL A 252 7.090 4.025 -23.424 1.00 30.08 C
ANISOU 1366 CG2 VAL A 252 3154 5228 3048 -1016 705 230 C
ATOM 1367 N TRP A 253 4.062 6.816 -25.219 1.00 33.67 N
ANISOU 1367 N TRP A 253 3880 5577 3335 -1422 229 548 N
ATOM 1368 CA TRP A 253 2.945 7.384 -25.965 1.00 35.20 C
ANISOU 1368 CA TRP A 253 4206 5681 3486 -1469 18 604 C
ATOM 1369 C TRP A 253 3.432 8.460 -26.924 1.00 44.69 C
ANISOU 1369 C TRP A 253 5566 6913 4500 -1616 -24 730 C
ATOM 1370 O TRP A 253 3.064 8.472 -28.103 1.00 52.91 O
ANISOU 1370 O TRP A 253 6773 7962 5370 -1687 -108 752 O
ATOM 1371 CB TRP A 253 1.912 7.971 -25.006 1.00 36.95 C
ANISOU 1371 CB TRP A 253 4349 5768 3924 -1392 -145 624 C
ATOM 1372 CG TRP A 253 1.289 6.980 -24.082 1.00 32.33 C
ANISOU 1372 CG TRP A 253 3628 5142 3513 -1273 -112 506 C
ATOM 1373 CD1 TRP A 253 1.154 5.640 -24.283 1.00 31.52 C
ANISOU 1373 CD1 TRP A 253 3521 5070 3386 -1235 -22 390 C
ATOM 1374 CD2 TRP A 253 0.715 7.255 -22.799 1.00 33.42 C
ANISOU 1374 CD2 TRP A 253 3635 5195 3869 -1189 -160 492 C
ATOM 1375 NE1 TRP A 253 0.527 5.062 -23.205 1.00 38.32 N
ANISOU 1375 NE1 TRP A 253 4265 5862 4432 -1144 -10 313 N
ATOM 1376 CE2 TRP A 253 0.248 6.033 -22.280 1.00 32.23 C
ANISOU 1376 CE2 TRP A 253 3410 5029 3808 -1116 -89 372 C
ATOM 1377 CE3 TRP A 253 0.550 8.418 -22.040 1.00 36.82 C
ANISOU 1377 CE3 TRP A 253 4014 5556 4420 -1174 -253 565 C
ATOM 1378 CZ2 TRP A 253 -0.373 5.940 -21.037 1.00 32.79 C
ANISOU 1378 CZ2 TRP A 253 3355 5028 4074 -1040 -99 327 C
ATOM 1379 CZ3 TRP A 253 -0.064 8.324 -20.808 1.00 37.38 C
ANISOU 1379 CZ3 TRP A 253 3950 5562 4690 -1084 -265 510 C
ATOM 1380 CH2 TRP A 253 -0.515 7.095 -20.317 1.00 39.64 C
ANISOU 1380 CH2 TRP A 253 4163 5846 5052 -1023 -184 394 C
ATOM 1381 N ARG A 254 4.269 9.373 -26.430 1.00 46.29 N
ANISOU 1381 N ARG A 254 5733 7132 4723 -1675 33 814 N
ATOM 1382 CA ARG A 254 4.759 10.450 -27.279 1.00 46.35 C
ANISOU 1382 CA ARG A 254 5908 7153 4551 -1841 4 943 C
ATOM 1383 C ARG A 254 5.595 9.900 -28.425 1.00 50.37 C
ANISOU 1383 C ARG A 254 6499 7782 4859 -1902 145 878 C
ATOM 1384 O ARG A 254 5.459 10.344 -29.570 1.00 57.87 O
ANISOU 1384 O ARG A 254 7642 8717 5627 -2009 71 943 O
ATOM 1385 CB ARG A 254 5.570 11.443 -26.448 1.00 46.29 C
ANISOU 1385 CB ARG A 254 5822 7104 4661 -1837 39 974 C
ATOM 1386 CG ARG A 254 5.437 12.893 -26.891 1.00 46.54 C
ANISOU 1386 CG ARG A 254 6031 7028 4626 -1955 -106 1117 C
ATOM 1387 CD ARG A 254 4.000 13.405 -26.787 1.00 77.01 C
ANISOU 1387 CD ARG A 254 9979 10734 8547 -1929 -359 1217 C
ATOM 1388 NE ARG A 254 3.362 13.048 -25.523 1.00 70.45 N
ANISOU 1388 NE ARG A 254 8947 9846 7977 -1757 -397 1128 N
ATOM 1389 CZ ARG A 254 2.343 12.206 -25.390 1.00 58.21 C
ANISOU 1389 CZ ARG A 254 7325 8269 6523 -1627 -471 1028 C
ATOM 1390 NH1 ARG A 254 1.778 11.622 -26.436 1.00 60.83 N
ANISOU 1390 NH1 ARG A 254 7764 8622 6727 -1635 -537 998 N
ATOM 1391 NH2 ARG A 254 1.872 11.947 -24.173 1.00 51.19 N
ANISOU 1391 NH2 ARG A 254 6258 7334 5860 -1497 -476 953 N
ATOM 1392 N HIS A 255 6.463 8.926 -28.138 1.00 49.57 N
ANISOU 1392 N HIS A 255 6255 7771 4808 -1804 329 736 N
ATOM 1393 CA HIS A 255 7.228 8.296 -29.207 1.00 52.22 C
ANISOU 1393 CA HIS A 255 6648 8207 4986 -1832 458 653 C
ATOM 1394 C HIS A 255 6.313 7.607 -30.206 1.00 54.06 C
ANISOU 1394 C HIS A 255 7025 8464 5052 -1879 396 641 C
ATOM 1395 O HIS A 255 6.622 7.561 -31.402 1.00 63.14 O
ANISOU 1395 O HIS A 255 8308 9660 6022 -1957 427 630 O
ATOM 1396 CB HIS A 255 8.227 7.296 -28.627 1.00 54.50 C
ANISOU 1396 CB HIS A 255 6763 8566 5378 -1687 633 506 C
ATOM 1397 CG HIS A 255 9.356 7.936 -27.883 1.00 46.83 C
ANISOU 1397 CG HIS A 255 5678 7593 4522 -1647 695 501 C
ATOM 1398 ND1 HIS A 255 9.452 9.300 -27.710 1.00 47.22 N
ANISOU 1398 ND1 HIS A 255 5771 7584 4587 -1742 617 607 N
ATOM 1399 CD2 HIS A 255 10.438 7.401 -27.271 1.00 48.59 C
ANISOU 1399 CD2 HIS A 255 5759 7861 4843 -1524 815 401 C
ATOM 1400 CE1 HIS A 255 10.544 9.578 -27.020 1.00 56.12 C
ANISOU 1400 CE1 HIS A 255 6780 8730 5811 -1688 696 564 C
ATOM 1401 NE2 HIS A 255 11.161 8.443 -26.742 1.00 59.33 N
ANISOU 1401 NE2 HIS A 255 7073 9201 6269 -1554 810 443 N
ATOM 1402 N ALA A 256 5.191 7.061 -29.740 1.00 56.15 N
ANISOU 1402 N ALA A 256 7268 8699 5368 -1832 308 636 N
ATOM 1403 CA ALA A 256 4.218 6.448 -30.633 1.00 53.93 C
ANISOU 1403 CA ALA A 256 7114 8381 4995 -1820 189 583 C
ATOM 1404 C ALA A 256 3.293 7.463 -31.292 1.00 60.88 C
ANISOU 1404 C ALA A 256 8171 9157 5802 -1889 -60 706 C
ATOM 1405 O ALA A 256 2.604 7.111 -32.256 1.00 59.13 O
ANISOU 1405 O ALA A 256 8088 8929 5449 -1909 -171 676 O
ATOM 1406 CB ALA A 256 3.379 5.422 -29.869 1.00 49.45 C
ANISOU 1406 CB ALA A 256 6421 7737 4630 -1665 153 460 C
ATOM 1407 N AALA A1001 3.257 8.701 -30.800 0.49 63.88 N
ANISOU 1407 N AALA A1001 6580 10011 7681 337 -992 -76 N
ATOM 1408 N BALA A1001 3.257 8.701 -30.800 0.51 67.82 N
ANISOU 1408 N BALA A1001 7078 10510 8180 337 -992 -76 N
ATOM 1409 CA AALA A1001 2.390 9.728 -31.365 0.49 58.51 C
ANISOU 1409 CA AALA A1001 6092 8990 7150 -4 -1271 -167 C
ATOM 1410 CA BALA A1001 2.390 9.728 -31.365 0.51 60.85 C
ANISOU 1410 CA BALA A1001 6387 9286 7446 -4 -1271 -167 C
ATOM 1411 C AALA A1001 3.061 10.466 -32.517 0.49 74.68 C
ANISOU 1411 C AALA A1001 8184 11070 9120 -409 -1408 -205 C
ATOM 1412 C BALA A1001 3.061 10.467 -32.517 0.51 81.39 C
ANISOU 1412 C BALA A1001 9035 11920 9970 -409 -1408 -205 C
ATOM 1413 O AALA A1001 2.476 10.603 -33.596 0.49 73.26 O
ANISOU 1413 O AALA A1001 8210 10583 9041 -647 -1472 -212 O
ATOM 1414 O BALA A1001 2.475 10.604 -33.595 0.51 73.17 O
ANISOU 1414 O BALA A1001 8199 10571 9030 -648 -1472 -212 O
ATOM 1415 CB AALA A1001 1.972 10.719 -30.275 0.49 60.36 C
ANISOU 1415 CB AALA A1001 6267 9238 7429 15 -1505 -257 C
ATOM 1416 CB BALA A1001 1.973 10.718 -30.275 0.51 60.28 C
ANISOU 1416 CB BALA A1001 6257 9228 7419 15 -1505 -257 C
ATOM 1417 N ASP A1002 4.288 10.949 -32.305 1.00 64.32 N
ANISOU 1417 N ASP A1002 6678 10136 7624 -488 -1449 -235 N
ATOM 1418 CA ASP A1002 4.989 11.659 -33.367 1.00 68.28 C
ANISOU 1418 CA ASP A1002 7215 10679 8050 -871 -1561 -271 C
ATOM 1419 C ASP A1002 5.248 10.755 -34.564 1.00 68.70 C
ANISOU 1419 C ASP A1002 7363 10664 8075 -918 -1364 -180 C
ATOM 1420 O ASP A1002 5.346 11.239 -35.698 1.00 70.97 O
ANISOU 1420 O ASP A1002 7779 10818 8368 -1246 -1458 -196 O
ATOM 1421 CB ASP A1002 6.304 12.234 -32.834 1.00 66.85 C
ANISOU 1421 CB ASP A1002 6778 10948 7673 -919 -1608 -330 C
ATOM 1422 CG ASP A1002 7.228 11.166 -32.286 1.00 75.25 C
ANISOU 1422 CG ASP A1002 7619 12406 8567 -578 -1347 -252 C
ATOM 1423 OD1 ASP A1002 6.726 10.098 -31.879 1.00 85.49 O
ANISOU 1423 OD1 ASP A1002 8936 13633 9914 -238 -1148 -161 O
ATOM 1424 OD2 ASP A1002 8.455 11.395 -32.256 1.00 75.08 O
ANISOU 1424 OD2 ASP A1002 7401 12765 8361 -646 -1332 -282 O
ATOM 1425 N LEU A1003 5.355 9.443 -34.337 1.00 69.15 N
ANISOU 1425 N LEU A1003 7364 10808 8104 -591 -1080 -83 N
ATOM 1426 CA LEU A1003 5.586 8.519 -35.442 1.00 65.28 C
ANISOU 1426 CA LEU A1003 6961 10249 7592 -621 -871 -1 C
ATOM 1427 C LEU A1003 4.419 8.524 -36.421 1.00 70.83 C
ANISOU 1427 C LEU A1003 7932 10500 8479 -807 -936 -19 C
ATOM 1428 O LEU A1003 4.622 8.524 -37.641 1.00 75.63 O
ANISOU 1428 O LEU A1003 8648 11021 9066 -1050 -934 -8 O
ATOM 1429 CB LEU A1003 5.825 7.109 -34.905 1.00 59.23 C
ANISOU 1429 CB LEU A1003 6093 9634 6779 -207 -535 105 C
ATOM 1430 CG LEU A1003 7.271 6.607 -34.960 1.00 77.24 C
ANISOU 1430 CG LEU A1003 8175 12339 8835 -112 -350 172 C
ATOM 1431 CD1 LEU A1003 8.226 7.587 -34.285 1.00 75.80 C
ANISOU 1431 CD1 LEU A1003 7773 12539 8491 -189 -528 100 C
ATOM 1432 CD2 LEU A1003 7.377 5.222 -34.330 1.00 53.77 C
ANISOU 1432 CD2 LEU A1003 5119 9484 5827 337 -8 289 C
ATOM 1433 N GLU A1004 3.187 8.526 -35.909 1.00 69.16 N
ANISOU 1433 N GLU A1004 7825 10009 8442 -692 -996 -50 N
ATOM 1434 CA GLU A1004 2.030 8.561 -36.796 1.00 64.20 C
ANISOU 1434 CA GLU A1004 7438 8971 7984 -861 -1070 -83 C
ATOM 1435 C GLU A1004 2.013 9.840 -37.624 1.00 66.02 C
ANISOU 1435 C GLU A1004 7782 9096 8209 -1263 -1357 -147 C
ATOM 1436 O GLU A1004 1.722 9.807 -38.825 1.00 68.47 O
ANISOU 1436 O GLU A1004 8251 9212 8551 -1472 -1375 -148 O
ATOM 1437 CB GLU A1004 0.741 8.424 -35.985 1.00 63.60 C
ANISOU 1437 CB GLU A1004 7434 8641 8091 -662 -1096 -115 C
ATOM 1438 CG GLU A1004 -0.519 8.770 -36.767 1.00 72.01 C
ANISOU 1438 CG GLU A1004 8730 9303 9326 -863 -1249 -178 C
ATOM 1439 CD GLU A1004 -1.789 8.327 -36.065 1.00 73.96 C
ANISOU 1439 CD GLU A1004 9043 9297 9760 -634 -1203 -205 C
ATOM 1440 OE1 GLU A1004 -1.712 7.446 -35.184 1.00 70.87 O
ANISOU 1440 OE1 GLU A1004 8546 9005 9377 -302 -977 -155 O
ATOM 1441 OE2 GLU A1004 -2.868 8.863 -36.396 1.00 88.90 O
ANISOU 1441 OE2 GLU A1004 11096 10894 11789 -780 -1386 -274 O
ATOM 1442 N ASP A1005 2.333 10.978 -37.003 1.00 62.41 N
ANISOU 1442 N ASP A1005 7242 8766 7706 -1373 -1574 -204 N
ATOM 1443 CA ASP A1005 2.351 12.234 -37.744 1.00 63.38 C
ANISOU 1443 CA ASP A1005 7476 8781 7824 -1750 -1825 -259 C
ATOM 1444 C ASP A1005 3.362 12.181 -38.882 1.00 64.40 C
ANISOU 1444 C ASP A1005 7604 9049 7816 -1969 -1757 -221 C
ATOM 1445 O ASP A1005 3.080 12.640 -39.995 1.00 65.92 O
ANISOU 1445 O ASP A1005 7970 9040 8036 -2236 -1861 -228 O
ATOM 1446 CB ASP A1005 2.659 13.396 -36.800 1.00 72.52 C
ANISOU 1446 CB ASP A1005 8520 10085 8950 -1817 -2027 -335 C
ATOM 1447 CG ASP A1005 1.524 13.681 -35.836 1.00 62.77 C
ANISOU 1447 CG ASP A1005 7330 8653 7866 -1666 -2147 -381 C
ATOM 1448 OD1 ASP A1005 0.350 13.584 -36.253 1.00 70.35 O
ANISOU 1448 OD1 ASP A1005 8484 9270 8975 -1684 -2198 -383 O
ATOM 1449 OD2 ASP A1005 1.803 14.000 -34.661 1.00 53.18 O
ANISOU 1449 OD2 ASP A1005 5952 7638 6617 -1528 -2191 -422 O
ATOM 1450 N ASN A1006 4.544 11.617 -38.625 1.00 59.10 N
ANISOU 1450 N ASN A1006 6736 8730 6990 -1848 -1579 -178 N
ATOM 1451 CA ASN A1006 5.523 11.444 -39.693 1.00 56.87 C
ANISOU 1451 CA ASN A1006 6444 8588 6576 -2031 -1488 -135 C
ATOM 1452 C ASN A1006 4.974 10.549 -40.794 1.00 54.00 C
ANISOU 1452 C ASN A1006 6253 7989 6276 -2037 -1348 -80 C
ATOM 1453 O ASN A1006 5.143 10.839 -41.984 1.00 55.39 O
ANISOU 1453 O ASN A1006 6548 8077 6419 -2302 -1397 -73 O
ATOM 1454 CB ASN A1006 6.818 10.862 -39.131 1.00 57.09 C
ANISOU 1454 CB ASN A1006 6219 9046 6427 -1848 -1301 -95 C
ATOM 1455 CG ASN A1006 7.485 11.782 -38.130 1.00 63.37 C
ANISOU 1455 CG ASN A1006 6819 10123 7137 -1872 -1440 -172 C
ATOM 1456 OD1 ASN A1006 7.691 11.416 -36.974 1.00 70.85 O
ANISOU 1456 OD1 ASN A1006 7587 11295 8039 -1582 -1362 -172 O
ATOM 1457 ND2 ASN A1006 7.827 12.987 -38.571 1.00 68.46 N
ANISOU 1457 ND2 ASN A1006 7497 10759 7756 -2216 -1639 -243 N
ATOM 1458 N TRP A1007 4.310 9.455 -40.417 1.00 55.57 N
ANISOU 1458 N TRP A1007 6467 8082 6565 -1747 -1165 -47 N
ATOM 1459 CA TRP A1007 3.700 8.580 -41.412 1.00 47.82 C
ANISOU 1459 CA TRP A1007 5644 6866 5661 -1750 -1022 -21 C
ATOM 1460 C TRP A1007 2.654 9.326 -42.231 1.00 50.41 C
ANISOU 1460 C TRP A1007 6194 6853 6106 -2005 -1245 -82 C
ATOM 1461 O TRP A1007 2.614 9.201 -43.460 1.00 49.92 O
ANISOU 1461 O TRP A1007 6256 6683 6027 -2190 -1231 -74 O
ATOM 1462 CB TRP A1007 3.085 7.363 -40.718 1.00 52.81 C
ANISOU 1462 CB TRP A1007 6251 7422 6394 -1392 -785 7 C
ATOM 1463 CG TRP A1007 2.137 6.556 -41.568 1.00 65.17 C
ANISOU 1463 CG TRP A1007 7990 8683 8090 -1392 -662 -7 C
ATOM 1464 CD1 TRP A1007 0.799 6.777 -41.743 1.00 65.05 C
ANISOU 1464 CD1 TRP A1007 8137 8333 8245 -1447 -788 -80 C
ATOM 1465 CD2 TRP A1007 2.452 5.389 -42.340 1.00 62.27 C
ANISOU 1465 CD2 TRP A1007 7639 8329 7691 -1333 -384 41 C
ATOM 1466 NE1 TRP A1007 0.266 5.827 -42.580 1.00 62.91 N
ANISOU 1466 NE1 TRP A1007 7974 7878 8051 -1433 -608 -93 N
ATOM 1467 CE2 TRP A1007 1.259 4.964 -42.960 1.00 60.52 C
ANISOU 1467 CE2 TRP A1007 7589 7775 7631 -1367 -355 -20 C
ATOM 1468 CE3 TRP A1007 3.626 4.666 -42.570 1.00 61.15 C
ANISOU 1468 CE3 TRP A1007 7381 8452 7400 -1256 -153 124 C
ATOM 1469 CZ2 TRP A1007 1.208 3.847 -43.794 1.00 63.65 C
ANISOU 1469 CZ2 TRP A1007 8041 8093 8048 -1335 -100 -11 C
ATOM 1470 CZ3 TRP A1007 3.572 3.558 -43.401 1.00 62.90 C
ANISOU 1470 CZ3 TRP A1007 7670 8585 7643 -1218 101 148 C
ATOM 1471 CH2 TRP A1007 2.372 3.161 -44.003 1.00 59.89 C
ANISOU 1471 CH2 TRP A1007 7459 7867 7430 -1263 127 76 C
ATOM 1472 N GLU A1008 1.806 10.118 -41.571 1.00 50.93 N
ANISOU 1472 N GLU A1008 6312 6758 6283 -2010 -1453 -142 N
ATOM 1473 CA GLU A1008 0.782 10.862 -42.297 1.00 51.71 C
ANISOU 1473 CA GLU A1008 6620 6543 6485 -2229 -1669 -196 C
ATOM 1474 C GLU A1008 1.415 11.860 -43.256 1.00 52.54 C
ANISOU 1474 C GLU A1008 6790 6689 6483 -2568 -1826 -191 C
ATOM 1475 O GLU A1008 1.081 11.895 -44.445 1.00 62.37 O
ANISOU 1475 O GLU A1008 8192 7773 7732 -2744 -1859 -188 O
ATOM 1476 CB GLU A1008 -0.149 11.576 -41.318 1.00 60.05 C
ANISOU 1476 CB GLU A1008 7704 7445 7668 -2162 -1860 -255 C
ATOM 1477 CG GLU A1008 -1.018 10.645 -40.493 1.00 54.54 C
ANISOU 1477 CG GLU A1008 6985 6633 7104 -1845 -1720 -265 C
ATOM 1478 CD GLU A1008 -1.930 11.396 -39.544 1.00 49.73 C
ANISOU 1478 CD GLU A1008 6406 5873 6617 -1788 -1919 -323 C
ATOM 1479 OE1 GLU A1008 -2.036 12.632 -39.676 1.00 51.62 O
ANISOU 1479 OE1 GLU A1008 6714 6048 6852 -2012 -2171 -360 O
ATOM 1480 OE2 GLU A1008 -2.539 10.751 -38.666 1.00 54.55 O
ANISOU 1480 OE2 GLU A1008 6975 6423 7330 -1516 -1813 -330 O
ATOM 1481 N THR A1009 2.344 12.677 -42.755 1.00 50.14 N
ANISOU 1481 N THR A1009 6362 6608 6079 -2663 -1916 -195 N
ATOM 1482 CA THR A1009 3.019 13.634 -43.624 1.00 52.59 C
ANISOU 1482 CA THR A1009 6726 6951 6306 -2881 -1966 -185 C
ATOM 1483 C THR A1009 3.810 12.918 -44.709 1.00 53.60 C
ANISOU 1483 C THR A1009 6853 7207 6304 -3054 -1857 -129 C
ATOM 1484 O THR A1009 3.802 13.334 -45.874 1.00 57.58 O
ANISOU 1484 O THR A1009 7497 7584 6795 -3138 -1834 -103 O
ATOM 1485 CB THR A1009 3.939 14.538 -42.804 1.00 52.92 C
ANISOU 1485 CB THR A1009 6611 7218 6279 -2899 -2017 -218 C
ATOM 1486 OG1 THR A1009 4.901 13.740 -42.102 1.00 47.95 O
ANISOU 1486 OG1 THR A1009 5746 6954 5518 -2852 -1936 -202 O
ATOM 1487 CG2 THR A1009 3.132 15.361 -41.808 1.00 48.33 C
ANISOU 1487 CG2 THR A1009 6043 6492 5828 -2740 -2110 -283 C
ATOM 1488 N LEU A1010 4.493 11.831 -44.348 1.00 55.97 N
ANISOU 1488 N LEU A1010 6992 7739 6534 -2845 -1624 -87 N
ATOM 1489 CA LEU A1010 5.268 11.091 -45.337 1.00 57.47 C
ANISOU 1489 CA LEU A1010 7173 8051 6612 -2899 -1439 -25 C
ATOM 1490 C LEU A1010 4.371 10.575 -46.455 1.00 51.51 C
ANISOU 1490 C LEU A1010 6618 7018 5935 -2952 -1405 -22 C
ATOM 1491 O LEU A1010 4.721 10.672 -47.637 1.00 50.61 O
ANISOU 1491 O LEU A1010 6593 6891 5747 -3158 -1402 4 O
ATOM 1492 CB LEU A1010 6.005 9.934 -44.659 1.00 55.15 C
ANISOU 1492 CB LEU A1010 6681 8029 6246 -2609 -1174 25 C
ATOM 1493 CG LEU A1010 7.139 9.283 -45.448 1.00 50.67 C
ANISOU 1493 CG LEU A1010 6046 7682 5527 -2655 -979 92 C
ATOM 1494 CD1 LEU A1010 8.458 9.967 -45.124 1.00 64.32 C
ANISOU 1494 CD1 LEU A1010 7594 9746 7096 -2766 -1026 91 C
ATOM 1495 CD2 LEU A1010 7.212 7.795 -45.151 1.00 54.77 C
ANISOU 1495 CD2 LEU A1010 6484 8281 6046 -2335 -676 149 C
ATOM 1496 N ASN A1011 3.203 10.033 -46.101 1.00 53.76 N
ANISOU 1496 N ASN A1011 6972 7086 6370 -2769 -1376 -56 N
ATOM 1497 CA ASN A1011 2.278 9.540 -47.118 1.00 50.11 C
ANISOU 1497 CA ASN A1011 6684 6369 5986 -2816 -1346 -80 C
ATOM 1498 C ASN A1011 1.618 10.688 -47.870 1.00 52.03 C
ANISOU 1498 C ASN A1011 7112 6401 6258 -3079 -1615 -117 C
ATOM 1499 O ASN A1011 1.432 10.611 -49.090 1.00 51.96 O
ANISOU 1499 O ASN A1011 7214 6303 6223 -3129 -1569 -107 O
ATOM 1500 CB ASN A1011 1.217 8.646 -46.477 1.00 46.47 C
ANISOU 1500 CB ASN A1011 6231 5740 5683 -2549 -1229 -121 C
ATOM 1501 CG ASN A1011 1.772 7.309 -46.032 1.00 54.74 C
ANISOU 1501 CG ASN A1011 7140 6952 6706 -2285 -907 -72 C
ATOM 1502 OD1 ASN A1011 2.979 7.156 -45.836 1.00 54.38 O
ANISOU 1502 OD1 ASN A1011 6953 7188 6522 -2252 -799 -6 O
ATOM 1503 ND2 ASN A1011 0.891 6.328 -45.874 1.00 57.43 N
ANISOU 1503 ND2 ASN A1011 7521 7119 7182 -2090 -741 -107 N
ATOM 1504 N ASP A1012 1.252 11.759 -47.162 1.00 55.45 N
ANISOU 1504 N ASP A1012 7537 6778 6753 -2967 -1740 -136 N
ATOM 1505 CA ASP A1012 0.694 12.925 -47.836 1.00 46.71 C
ANISOU 1505 CA ASP A1012 6549 5525 5675 -2928 -1810 -133 C
ATOM 1506 C ASP A1012 1.697 13.510 -48.819 1.00 54.69 C
ANISOU 1506 C ASP A1012 7586 6646 6549 -3102 -1800 -73 C
ATOM 1507 O ASP A1012 1.331 13.904 -49.931 1.00 58.56 O
ANISOU 1507 O ASP A1012 8200 7030 7021 -3130 -1807 -49 O
ATOM 1508 CB ASP A1012 0.272 13.978 -46.810 1.00 44.91 C
ANISOU 1508 CB ASP A1012 6290 5250 5524 -2810 -1910 -162 C
ATOM 1509 CG ASP A1012 -0.832 13.492 -45.891 1.00 49.54 C
ANISOU 1509 CG ASP A1012 6867 5709 6248 -2628 -1922 -218 C
ATOM 1510 OD1 ASP A1012 -1.347 12.375 -46.113 1.00 49.69 O
ANISOU 1510 OD1 ASP A1012 6916 5644 6319 -2590 -1851 -240 O
ATOM 1511 OD2 ASP A1012 -1.183 14.227 -44.943 1.00 43.26 O
ANISOU 1511 OD2 ASP A1012 6035 4890 5511 -2527 -1991 -244 O
ATOM 1512 N ASN A1013 2.972 13.569 -48.426 1.00 56.20 N
ANISOU 1512 N ASN A1013 7651 7070 6632 -3222 -1783 -49 N
ATOM 1513 CA ASN A1013 4.002 14.072 -49.329 1.00 48.78 C
ANISOU 1513 CA ASN A1013 6728 6245 5562 -3397 -1758 5 C
ATOM 1514 C ASN A1013 4.126 13.195 -50.567 1.00 53.92 C
ANISOU 1514 C ASN A1013 7454 6895 6140 -3494 -1661 42 C
ATOM 1515 O ASN A1013 4.269 13.702 -51.685 1.00 65.77 O
ANISOU 1515 O ASN A1013 9062 8347 7580 -3581 -1666 83 O
ATOM 1516 CB ASN A1013 5.341 14.159 -48.600 1.00 50.08 C
ANISOU 1516 CB ASN A1013 6707 6702 5621 -3496 -1738 7 C
ATOM 1517 CG ASN A1013 5.373 15.274 -47.575 1.00 57.26 C
ANISOU 1517 CG ASN A1013 7552 7617 6586 -3430 -1832 -39 C
ATOM 1518 OD1 ASN A1013 5.671 15.050 -46.401 1.00 59.69 O
ANISOU 1518 OD1 ASN A1013 7696 8092 6892 -3371 -1848 -79 O
ATOM 1519 ND2 ASN A1013 5.062 16.487 -48.016 1.00 65.78 N
ANISOU 1519 ND2 ASN A1013 8752 8533 7710 -3442 -1890 -35 N
ATOM 1520 N LEU A1014 4.074 11.874 -50.391 1.00 56.34 N
ANISOU 1520 N LEU A1014 7703 7257 6448 -3490 -1562 26 N
ATOM 1521 CA LEU A1014 4.160 10.981 -51.540 1.00 56.21 C
ANISOU 1521 CA LEU A1014 7753 7233 6372 -3584 -1443 46 C
ATOM 1522 C LEU A1014 2.997 11.203 -52.498 1.00 58.16 C
ANISOU 1522 C LEU A1014 8176 7230 6694 -3500 -1486 24 C
ATOM 1523 O LEU A1014 3.188 11.246 -53.719 1.00 63.48 O
ANISOU 1523 O LEU A1014 8937 7897 7285 -3594 -1459 56 O
ATOM 1524 CB LEU A1014 4.199 9.527 -51.069 1.00 54.71 C
ANISOU 1524 CB LEU A1014 7457 7123 6207 -3453 -1239 35 C
ATOM 1525 CG LEU A1014 5.574 9.010 -50.647 1.00 48.82 C
ANISOU 1525 CG LEU A1014 6514 6699 5337 -3365 -1045 99 C
ATOM 1526 CD1 LEU A1014 5.432 7.760 -49.800 1.00 51.85 C
ANISOU 1526 CD1 LEU A1014 6781 7137 5782 -3040 -807 104 C
ATOM 1527 CD2 LEU A1014 6.433 8.729 -51.869 1.00 52.15 C
ANISOU 1527 CD2 LEU A1014 6958 7234 5621 -3527 -939 152 C
ATOM 1528 N LYS A1015 1.784 11.353 -51.964 1.00 57.71 N
ANISOU 1528 N LYS A1015 8157 6989 6781 -3323 -1552 -33 N
ATOM 1529 CA LYS A1015 0.617 11.521 -52.823 1.00 59.64 C
ANISOU 1529 CA LYS A1015 8528 7044 7087 -3234 -1586 -64 C
ATOM 1530 C LYS A1015 0.649 12.856 -53.556 1.00 68.95 C
ANISOU 1530 C LYS A1015 9797 8196 8204 -3280 -1689 -9 C
ATOM 1531 O LYS A1015 0.381 12.914 -54.761 1.00 71.09 O
ANISOU 1531 O LYS A1015 10168 8421 8421 -3327 -1690 8 O
ATOM 1532 CB LYS A1015 -0.660 11.393 -51.997 1.00 49.98 C
ANISOU 1532 CB LYS A1015 7298 5663 6028 -3036 -1619 -140 C
ATOM 1533 CG LYS A1015 -1.037 9.954 -51.696 1.00 62.84 C
ANISOU 1533 CG LYS A1015 8897 7242 7738 -2991 -1492 -208 C
ATOM 1534 CD LYS A1015 -1.968 9.848 -50.500 1.00 63.64 C
ANISOU 1534 CD LYS A1015 8961 7226 7995 -2813 -1520 -270 C
ATOM 1535 CE LYS A1015 -2.385 8.408 -50.254 1.00 58.23 C
ANISOU 1535 CE LYS A1015 8270 6450 7405 -2776 -1368 -339 C
ATOM 1536 NZ LYS A1015 -3.261 7.884 -51.338 1.00 56.28 N
ANISOU 1536 NZ LYS A1015 8096 6083 7204 -2740 -1295 -414 N
ATOM 1537 N VAL A1016 0.974 13.942 -52.850 1.00 68.31 N
ANISOU 1537 N VAL A1016 9684 8143 8129 -3275 -1770 18 N
ATOM 1538 CA VAL A1016 1.023 15.245 -53.501 1.00 70.38 C
ANISOU 1538 CA VAL A1016 10041 8364 8337 -3337 -1851 73 C
ATOM 1539 C VAL A1016 2.142 15.306 -54.531 1.00 73.58 C
ANISOU 1539 C VAL A1016 10482 8884 8590 -3536 -1810 141 C
ATOM 1540 O VAL A1016 2.074 16.115 -55.465 1.00 77.63 O
ANISOU 1540 O VAL A1016 11111 9343 9041 -3607 -1860 193 O
ATOM 1541 CB VAL A1016 1.182 16.377 -52.468 1.00 61.99 C
ANISOU 1541 CB VAL A1016 8930 7303 7321 -3304 -1924 72 C
ATOM 1542 CG1 VAL A1016 0.002 16.388 -51.499 1.00 61.68 C
ANISOU 1542 CG1 VAL A1016 8866 7146 7424 -3106 -1964 10 C
ATOM 1543 CG2 VAL A1016 2.496 16.243 -51.726 1.00 57.66 C
ANISOU 1543 CG2 VAL A1016 8244 6946 6717 -3401 -1885 73 C
ATOM 1544 N ILE A1017 3.175 14.473 -54.388 1.00 67.05 N
ANISOU 1544 N ILE A1017 9558 8227 7692 -3635 -1716 147 N
ATOM 1545 CA ILE A1017 4.224 14.422 -55.402 1.00 72.82 C
ANISOU 1545 CA ILE A1017 10315 9081 8272 -3824 -1658 209 C
ATOM 1546 C ILE A1017 3.631 14.031 -56.748 1.00 71.53 C
ANISOU 1546 C ILE A1017 10283 8826 8070 -3842 -1641 220 C
ATOM 1547 O ILE A1017 3.997 14.586 -57.792 1.00 78.50 O
ANISOU 1547 O ILE A1017 11262 9718 8848 -3965 -1660 280 O
ATOM 1548 CB ILE A1017 5.342 13.456 -54.969 1.00 68.65 C
ANISOU 1548 CB ILE A1017 9638 8775 7671 -3917 -1541 209 C
ATOM 1549 CG1 ILE A1017 6.263 14.144 -53.958 1.00 65.83 C
ANISOU 1549 CG1 ILE A1017 9150 8572 7293 -3961 -1569 211 C
ATOM 1550 CG2 ILE A1017 6.132 12.974 -56.178 1.00 71.65 C
ANISOU 1550 CG2 ILE A1017 10053 9264 7908 -4084 -1446 259 C
ATOM 1551 CD1 ILE A1017 7.201 13.205 -53.232 1.00 69.30 C
ANISOU 1551 CD1 ILE A1017 9398 9266 7667 -4016 -1467 201 C
ATOM 1552 N GLU A1018 2.706 13.071 -56.745 1.00 66.10 N
ANISOU 1552 N GLU A1018 9599 8052 7463 -3727 -1604 155 N
ATOM 1553 CA GLU A1018 2.056 12.662 -57.984 1.00 70.87 C
ANISOU 1553 CA GLU A1018 10312 8578 8037 -3735 -1589 141 C
ATOM 1554 C GLU A1018 1.118 13.741 -58.510 1.00 74.74 C
ANISOU 1554 C GLU A1018 10923 8928 8546 -3677 -1719 159 C
ATOM 1555 O GLU A1018 0.956 13.881 -59.727 1.00 74.73 O
ANISOU 1555 O GLU A1018 11031 8907 8458 -3752 -1739 188 O
ATOM 1556 CB GLU A1018 1.288 11.361 -57.759 1.00 65.07 C
ANISOU 1556 CB GLU A1018 9537 7785 7402 -3628 -1500 44 C
ATOM 1557 CG GLU A1018 2.136 10.236 -57.184 1.00 66.45 C
ANISOU 1557 CG GLU A1018 9597 8089 7560 -3691 -1351 32 C
ATOM 1558 CD GLU A1018 1.302 9.082 -56.664 1.00 83.09 C
ANISOU 1558 CD GLU A1018 11668 10102 9800 -3573 -1256 -67 C
ATOM 1559 OE1 GLU A1018 0.059 9.151 -56.761 1.00 88.54 O
ANISOU 1559 OE1 GLU A1018 12410 10634 10598 -3434 -1313 -136 O
ATOM 1560 OE2 GLU A1018 1.892 8.106 -56.154 1.00 88.42 O
ANISOU 1560 OE2 GLU A1018 12258 10867 10471 -3628 -1108 -75 O
ATOM 1561 N LYS A1019 0.500 14.510 -57.616 1.00 80.58 N
ANISOU 1561 N LYS A1019 11647 9580 9388 -3554 -1804 145 N
ATOM 1562 CA LYS A1019 -0.499 15.508 -58.000 1.00 77.94 C
ANISOU 1562 CA LYS A1019 11423 9115 9077 -3491 -1918 162 C
ATOM 1563 C LYS A1019 0.148 16.886 -58.165 1.00 89.76 C
ANISOU 1563 C LYS A1019 12989 10620 10494 -3608 -1990 255 C
ATOM 1564 O LYS A1019 -0.214 17.861 -57.504 1.00 98.61 O
ANISOU 1564 O LYS A1019 14120 11671 11676 -3545 -2064 264 O
ATOM 1565 CB LYS A1019 -1.620 15.548 -56.966 1.00 78.28 C
ANISOU 1565 CB LYS A1019 11413 9056 9275 -3292 -1954 91 C
ATOM 1566 CG LYS A1019 -2.237 14.191 -56.648 1.00 72.67 C
ANISOU 1566 CG LYS A1019 10625 8325 8661 -3179 -1868 -12 C
ATOM 1567 CD LYS A1019 -3.034 13.647 -57.819 1.00 56.28 C
ANISOU 1567 CD LYS A1019 8619 6201 6565 -3172 -1856 -57 C
ATOM 1568 CE LYS A1019 -3.676 12.313 -57.480 1.00 49.41 C
ANISOU 1568 CE LYS A1019 7669 5297 5809 -3066 -1755 -178 C
ATOM 1569 NZ LYS A1019 -4.530 11.813 -58.589 1.00 47.75 N
ANISOU 1569 NZ LYS A1019 7509 5043 5591 -3054 -1742 -249 N
ATOM 1570 N ALA A1020 1.127 16.957 -59.065 1.00 90.51 N
ANISOU 1570 N ALA A1020 13135 10803 10451 -3788 -1959 320 N
ATOM 1571 CA ALA A1020 1.783 18.225 -59.357 1.00 98.91 C
ANISOU 1571 CA ALA A1020 14277 11870 11434 -3924 -2012 403 C
ATOM 1572 C ALA A1020 2.668 18.062 -60.583 1.00100.47 C
ANISOU 1572 C ALA A1020 14545 12156 11471 -4116 -1966 468 C
ATOM 1573 O ALA A1020 3.375 17.059 -60.711 1.00103.13 O
ANISOU 1573 O ALA A1020 14802 12619 11762 -4172 -1864 450 O
ATOM 1574 CB ALA A1020 2.616 18.707 -58.163 1.00101.28 C
ANISOU 1574 CB ALA A1020 14459 12242 11780 -3941 -1993 392 C
ATOM 1575 N ASP A1021 2.624 19.050 -61.475 1.00 93.66 N
ANISOU 1575 N ASP A1021 13836 11230 10520 -4221 -2037 545 N
ATOM 1576 CA ASP A1021 3.456 19.063 -62.671 1.00 89.89 C
ANISOU 1576 CA ASP A1021 13444 10827 9882 -4415 -2001 615 C
ATOM 1577 C ASP A1021 4.634 20.024 -62.562 1.00 91.37 C
ANISOU 1577 C ASP A1021 13634 11075 10009 -4577 -1983 671 C
ATOM 1578 O ASP A1021 5.391 20.166 -63.527 1.00 93.19 O
ANISOU 1578 O ASP A1021 13939 11366 10105 -4750 -1950 733 O
ATOM 1579 CB ASP A1021 2.611 19.424 -63.898 1.00 77.19 C
ANISOU 1579 CB ASP A1021 12023 9112 8193 -4444 -2091 664 C
ATOM 1580 CG ASP A1021 3.271 19.015 -65.203 1.00 68.02 C
ANISOU 1580 CG ASP A1021 10938 8037 6868 -4616 -2040 714 C
ATOM 1581 OD1 ASP A1021 4.330 18.355 -65.154 1.00 60.36 O
ANISOU 1581 OD1 ASP A1021 9867 7212 5855 -4699 -1927 706 O
ATOM 1582 OD2 ASP A1021 2.731 19.351 -66.278 1.00 71.77 O
ANISOU 1582 OD2 ASP A1021 11576 8444 7251 -4672 -2115 763 O
ATOM 1583 N ASN A1022 4.808 20.684 -61.419 1.00 79.26 N
ANISOU 1583 N ASN A1022 12017 9527 8571 -4530 -1999 642 N
ATOM 1584 CA ASN A1022 5.935 21.580 -61.205 1.00 75.03 C
ANISOU 1584 CA ASN A1022 11457 9054 7996 -4682 -1969 667 C
ATOM 1585 C ASN A1022 7.084 20.835 -60.542 1.00 69.39 C
ANISOU 1585 C ASN A1022 10553 8537 7275 -4725 -1859 620 C
ATOM 1586 O ASN A1022 6.875 20.020 -59.639 1.00 75.61 O
ANISOU 1586 O ASN A1022 11206 9375 8146 -4594 -1834 556 O
ATOM 1587 CB ASN A1022 5.526 22.771 -60.337 1.00 75.92 C
ANISOU 1587 CB ASN A1022 11581 9052 8214 -4625 -2041 647 C
ATOM 1588 CG ASN A1022 4.955 23.919 -61.149 1.00 99.98 C
ANISOU 1588 CG ASN A1022 14836 11938 11215 -4688 -2130 722 C
ATOM 1589 OD1 ASN A1022 5.696 24.745 -61.686 1.00 93.96 O
ANISOU 1589 OD1 ASN A1022 14154 11175 10373 -4864 -2112 772 O
ATOM 1590 ND2 ASN A1022 3.632 23.981 -61.238 1.00104.83 N
ANISOU 1590 ND2 ASN A1022 15539 12416 11875 -4548 -2223 728 N
ATOM 1591 N ALA A1023 8.304 21.124 -60.996 1.00 65.69 N
ANISOU 1591 N ALA A1023 10073 8185 6701 -4914 -1793 654 N
ATOM 1592 CA ALA A1023 9.489 20.500 -60.423 1.00 62.39 C
ANISOU 1592 CA ALA A1023 9470 7982 6254 -4976 -1688 615 C
ATOM 1593 C ALA A1023 9.769 20.960 -58.999 1.00 62.23 C
ANISOU 1593 C ALA A1023 9299 8008 6337 -4922 -1697 542 C
ATOM 1594 O ALA A1023 10.599 20.345 -58.322 1.00 62.09 O
ANISOU 1594 O ALA A1023 9105 8184 6303 -4940 -1624 498 O
ATOM 1595 CB ALA A1023 10.707 20.788 -61.301 1.00 73.49 C
ANISOU 1595 CB ALA A1023 10900 9503 7518 -5195 -1614 665 C
ATOM 1596 N ALA A1024 9.112 22.022 -58.534 1.00 62.33 N
ANISOU 1596 N ALA A1024 9373 7864 6447 -4863 -1783 525 N
ATOM 1597 CA ALA A1024 9.310 22.504 -57.174 1.00 64.54 C
ANISOU 1597 CA ALA A1024 9512 8180 6830 -4808 -1795 444 C
ATOM 1598 C ALA A1024 8.418 21.780 -56.177 1.00 60.29 C
ANISOU 1598 C ALA A1024 8890 7614 6406 -4592 -1831 389 C
ATOM 1599 O ALA A1024 8.857 21.477 -55.062 1.00 60.19 O
ANISOU 1599 O ALA A1024 8703 7732 6437 -4547 -1806 320 O
ATOM 1600 CB ALA A1024 9.050 24.010 -57.104 1.00 77.88 C
ANISOU 1600 CB ALA A1024 11303 9714 8575 -4853 -1857 445 C
ATOM 1601 N GLN A1025 7.172 21.492 -56.560 1.00 61.35 N
ANISOU 1601 N GLN A1025 9140 7588 6584 -4460 -1889 414 N
ATOM 1602 CA GLN A1025 6.280 20.757 -55.669 1.00 60.10 C
ANISOU 1602 CA GLN A1025 8906 7392 6537 -4256 -1913 357 C
ATOM 1603 C GLN A1025 6.903 19.434 -55.248 1.00 62.59 C
ANISOU 1603 C GLN A1025 9066 7893 6822 -4246 -1826 326 C
ATOM 1604 O GLN A1025 6.709 18.980 -54.114 1.00 58.75 O
ANISOU 1604 O GLN A1025 8454 7451 6417 -4126 -1827 264 O
ATOM 1605 CB GLN A1025 4.934 20.522 -56.354 1.00 56.47 C
ANISOU 1605 CB GLN A1025 8588 6759 6107 -4140 -1969 384 C
ATOM 1606 N VAL A1026 7.656 18.801 -56.150 1.00 64.83 N
ANISOU 1606 N VAL A1026 9357 8294 6980 -4377 -1748 370 N
ATOM 1607 CA VAL A1026 8.374 17.580 -55.797 1.00 67.82 C
ANISOU 1607 CA VAL A1026 9584 8878 7309 -4396 -1651 349 C
ATOM 1608 C VAL A1026 9.439 17.873 -54.748 1.00 68.41 C
ANISOU 1608 C VAL A1026 9474 9152 7367 -4453 -1623 305 C
ATOM 1609 O VAL A1026 9.603 17.118 -53.782 1.00 79.84 O
ANISOU 1609 O VAL A1026 10764 10738 8835 -4381 -1592 260 O
ATOM 1610 CB VAL A1026 8.981 16.938 -57.058 1.00 73.11 C
ANISOU 1610 CB VAL A1026 10304 9637 7838 -4537 -1565 408 C
ATOM 1611 CG1 VAL A1026 9.904 15.786 -56.684 1.00 73.97 C
ANISOU 1611 CG1 VAL A1026 10237 9994 7874 -4586 -1446 393 C
ATOM 1612 CG2 VAL A1026 7.878 16.461 -57.992 1.00 84.24 C
ANISOU 1612 CG2 VAL A1026 11866 10877 9265 -4463 -1588 427 C
ATOM 1613 N LYS A1027 10.182 18.968 -54.920 1.00 62.94 N
ANISOU 1613 N LYS A1027 8793 8490 6632 -4588 -1632 312 N
ATOM 1614 CA LYS A1027 11.232 19.292 -53.959 1.00 66.56 C
ANISOU 1614 CA LYS A1027 9062 9157 7071 -4650 -1602 252 C
ATOM 1615 C LYS A1027 10.648 19.555 -52.575 1.00 68.33 C
ANISOU 1615 C LYS A1027 9197 9341 7426 -4491 -1673 173 C
ATOM 1616 O LYS A1027 11.183 19.078 -51.567 1.00 74.62 O
ANISOU 1616 O LYS A1027 9797 10347 8207 -4457 -1645 117 O
ATOM 1617 CB LYS A1027 12.038 20.500 -54.441 1.00 68.86 C
ANISOU 1617 CB LYS A1027 9398 9454 7312 -4829 -1594 259 C
ATOM 1618 CG LYS A1027 13.335 20.709 -53.663 1.00 79.10 C
ANISOU 1618 CG LYS A1027 10482 11016 8556 -4929 -1536 187 C
ATOM 1619 CD LYS A1027 13.683 22.182 -53.471 1.00 84.46 C
ANISOU 1619 CD LYS A1027 11183 11626 9282 -5029 -1566 137 C
ATOM 1620 CE LYS A1027 14.471 22.746 -54.644 1.00 86.31 C
ANISOU 1620 CE LYS A1027 11514 11864 9417 -5240 -1507 188 C
ATOM 1621 NZ LYS A1027 15.064 24.076 -54.319 1.00 76.17 N
ANISOU 1621 NZ LYS A1027 10201 10568 8172 -5363 -1505 117 N
ATOM 1622 N ASP A1028 9.545 20.304 -52.505 1.00 66.08 N
ANISOU 1622 N ASP A1028 9044 8806 7258 -4388 -1763 169 N
ATOM 1623 CA ASP A1028 8.945 20.618 -51.211 1.00 62.74 C
ANISOU 1623 CA ASP A1028 8544 8332 6962 -4235 -1829 93 C
ATOM 1624 C ASP A1028 8.520 19.351 -50.482 1.00 68.26 C
ANISOU 1624 C ASP A1028 9141 9103 7692 -4084 -1816 69 C
ATOM 1625 O ASP A1028 8.809 19.178 -49.292 1.00 71.22 O
ANISOU 1625 O ASP A1028 9347 9624 8091 -4019 -1823 2 O
ATOM 1626 CB ASP A1028 7.744 21.544 -51.399 1.00 63.04 C
ANISOU 1626 CB ASP A1028 8750 8095 7108 -4149 -1914 105 C
ATOM 1627 CG ASP A1028 8.144 22.935 -51.831 1.00 71.83 C
ANISOU 1627 CG ASP A1028 9946 9140 8207 -4294 -1930 115 C
ATOM 1628 OD1 ASP A1028 8.619 23.089 -52.976 1.00 73.70 O
ANISOU 1628 OD1 ASP A1028 10281 9377 8344 -4444 -1894 183 O
ATOM 1629 OD2 ASP A1028 7.985 23.875 -51.025 1.00 79.26 O
ANISOU 1629 OD2 ASP A1028 10853 10025 9235 -4264 -1973 53 O
ATOM 1630 N ALA A1029 7.827 18.452 -51.182 1.00 64.54 N
ANISOU 1630 N ALA A1029 8766 8537 7218 -4027 -1797 117 N
ATOM 1631 CA ALA A1029 7.352 17.230 -50.545 1.00 62.78 C
ANISOU 1631 CA ALA A1029 8462 8357 7034 -3895 -1775 92 C
ATOM 1632 C ALA A1029 8.518 16.378 -50.061 1.00 69.63 C
ANISOU 1632 C ALA A1029 9127 9542 7788 -3971 -1690 82 C
ATOM 1633 O ALA A1029 8.504 15.866 -48.936 1.00 73.34 O
ANISOU 1633 O ALA A1029 9446 10140 8282 -3874 -1694 37 O
ATOM 1634 CB ALA A1029 6.478 16.443 -51.519 1.00 57.24 C
ANISOU 1634 CB ALA A1029 7902 7500 6345 -3849 -1752 133 C
ATOM 1635 N LEU A1030 9.545 16.221 -50.897 1.00 67.50 N
ANISOU 1635 N LEU A1030 8838 9428 7381 -4142 -1609 128 N
ATOM 1636 CA LEU A1030 10.710 15.444 -50.490 1.00 70.82 C
ANISOU 1636 CA LEU A1030 9039 10198 7670 -4218 -1513 121 C
ATOM 1637 C LEU A1030 11.410 16.088 -49.301 1.00 76.70 C
ANISOU 1637 C LEU A1030 9593 11147 8404 -4204 -1545 49 C
ATOM 1638 O LEU A1030 11.834 15.392 -48.370 1.00 76.42 O
ANISOU 1638 O LEU A1030 9338 11388 8310 -4142 -1508 16 O
ATOM 1639 CB LEU A1030 11.676 15.295 -51.665 1.00 75.14 C
ANISOU 1639 CB LEU A1030 9608 10866 8075 -4406 -1417 180 C
ATOM 1640 CG LEU A1030 11.261 14.296 -52.744 1.00 68.21 C
ANISOU 1640 CG LEU A1030 8848 9899 7169 -4428 -1345 241 C
ATOM 1641 CD1 LEU A1030 12.027 14.556 -54.033 1.00 64.87 C
ANISOU 1641 CD1 LEU A1030 8509 9510 6629 -4606 -1287 300 C
ATOM 1642 CD2 LEU A1030 11.483 12.868 -52.263 1.00 70.64 C
ANISOU 1642 CD2 LEU A1030 8977 10434 7428 -4398 -1232 239 C
ATOM 1643 N THR A1031 11.545 17.416 -49.314 1.00 84.39 N
ANISOU 1643 N THR A1031 10631 12008 9425 -4257 -1606 18 N
ATOM 1644 CA THR A1031 12.166 18.104 -48.187 1.00 90.86 C
ANISOU 1644 CA THR A1031 11275 12999 10248 -4245 -1635 -72 C
ATOM 1645 C THR A1031 11.332 17.938 -46.922 1.00 84.16 C
ANISOU 1645 C THR A1031 10358 12110 9508 -4043 -1711 -129 C
ATOM 1646 O THR A1031 11.864 17.636 -45.848 1.00 90.96 O
ANISOU 1646 O THR A1031 10994 13249 10316 -3977 -1701 -189 O
ATOM 1647 CB THR A1031 12.364 19.584 -48.518 1.00 86.44 C
ANISOU 1647 CB THR A1031 10818 12286 9737 -4356 -1676 -98 C
ATOM 1648 OG1 THR A1031 11.153 20.124 -49.061 1.00 92.78 O
ANISOU 1648 OG1 THR A1031 11854 12736 10660 -4296 -1748 -58 O
ATOM 1649 CG2 THR A1031 13.496 19.764 -49.523 1.00 81.60 C
ANISOU 1649 CG2 THR A1031 10210 11802 8992 -4569 -1590 -61 C
ATOM 1650 N LYS A1032 10.014 18.131 -47.029 1.00 66.09 N
ANISOU 1650 N LYS A1032 8252 9498 7363 -3928 -1785 -114 N
ATOM 1651 CA LYS A1032 9.135 17.832 -45.906 1.00 65.86 C
ANISOU 1651 CA LYS A1032 8171 9415 7436 -3732 -1848 -161 C
ATOM 1652 C LYS A1032 9.089 16.340 -45.611 1.00 72.10 C
ANISOU 1652 C LYS A1032 8849 10382 8163 -3658 -1793 -133 C
ATOM 1653 O LYS A1032 8.742 15.949 -44.492 1.00 73.17 O
ANISOU 1653 O LYS A1032 8864 10603 8333 -3510 -1828 -174 O
ATOM 1654 CB LYS A1032 7.721 18.349 -46.182 1.00 61.10 C
ANISOU 1654 CB LYS A1032 7782 8443 6991 -3627 -1922 -150 C
ATOM 1655 CG LYS A1032 7.621 19.859 -46.349 1.00 79.65 C
ANISOU 1655 CG LYS A1032 10227 10632 9405 -3680 -1973 -176 C
ATOM 1656 CD LYS A1032 6.182 20.293 -46.610 1.00 74.94 C
ANISOU 1656 CD LYS A1032 9814 9727 8935 -3559 -2031 -158 C
ATOM 1657 CE LYS A1032 6.074 21.791 -46.877 1.00 75.50 C
ANISOU 1657 CE LYS A1032 9983 9655 9049 -3628 -2070 -168 C
ATOM 1658 NZ LYS A1032 5.837 22.584 -45.638 1.00 77.82 N
ANISOU 1658 NZ LYS A1032 10192 9935 9440 -3542 -2122 -262 N
ATOM 1659 N MET A1033 9.428 15.504 -46.594 1.00 71.67 N
ANISOU 1659 N MET A1033 8826 10394 8014 -3761 -1701 -64 N
ATOM 1660 CA MET A1033 9.477 14.063 -46.384 1.00 67.86 C
ANISOU 1660 CA MET A1033 8215 10113 7458 -3720 -1620 -37 C
ATOM 1661 C MET A1033 10.771 13.647 -45.693 1.00 73.70 C
ANISOU 1661 C MET A1033 8667 11293 8042 -3652 -1499 -45 C
ATOM 1662 O MET A1033 10.753 12.793 -44.800 1.00 72.91 O
ANISOU 1662 O MET A1033 8427 11338 7937 -3342 -1373 -31 O
ATOM 1663 CB MET A1033 9.333 13.348 -47.727 1.00 69.68 C
ANISOU 1663 CB MET A1033 8589 10229 7657 -3826 -1533 33 C
ATOM 1664 CG MET A1033 9.179 11.845 -47.641 1.00 67.36 C
ANISOU 1664 CG MET A1033 8243 9984 7366 -3538 -1304 84 C
ATOM 1665 SD MET A1033 9.272 11.064 -49.265 1.00 52.28 S
ANISOU 1665 SD MET A1033 6480 7982 5403 -3644 -1158 155 S
ATOM 1666 CE MET A1033 7.995 11.953 -50.149 1.00 51.63 C
ANISOU 1666 CE MET A1033 6683 7496 5437 -3867 -1394 122 C
ATOM 1667 N ARG A1034 11.901 14.240 -46.091 1.00 70.84 N
ANISOU 1667 N ARG A1034 8222 11136 7557 -3881 -1503 -62 N
ATOM 1668 CA ARG A1034 13.170 13.930 -45.438 1.00 66.21 C
ANISOU 1668 CA ARG A1034 7355 10983 6820 -3782 -1378 -79 C
ATOM 1669 C ARG A1034 13.146 14.347 -43.974 1.00 69.53 C
ANISOU 1669 C ARG A1034 7595 11565 7259 -3635 -1463 -170 C
ATOM 1670 O ARG A1034 13.643 13.620 -43.105 1.00 76.37 O
ANISOU 1670 O ARG A1034 8245 12732 8041 -3358 -1331 -164 O
ATOM 1671 CB ARG A1034 14.323 14.623 -46.165 1.00 68.16 C
ANISOU 1671 CB ARG A1034 7563 11382 6951 -4069 -1374 -97 C
ATOM 1672 CG ARG A1034 15.708 14.177 -45.701 1.00 80.65 C
ANISOU 1672 CG ARG A1034 8845 13449 8351 -3997 -1233 -113 C
ATOM 1673 CD ARG A1034 16.758 15.252 -45.943 1.00 74.08 C
ANISOU 1673 CD ARG A1034 7963 12731 7453 -4225 -1255 -182 C
ATOM 1674 NE ARG A1034 18.061 14.881 -45.400 1.00 78.21 N
ANISOU 1674 NE ARG A1034 8155 13773 7787 -4189 -1154 -226 N
ATOM 1675 CZ ARG A1034 19.111 14.504 -46.120 1.00 80.43 C
ANISOU 1675 CZ ARG A1034 8339 14300 7921 -4306 -1029 -189 C
ATOM 1676 NH1 ARG A1034 19.067 14.450 -47.442 1.00 78.84 N
ANISOU 1676 NH1 ARG A1034 8342 13884 7729 -4498 -995 -108 N
ATOM 1677 NH2 ARG A1034 20.241 14.179 -45.496 1.00 73.03 N
ANISOU 1677 NH2 ARG A1034 7108 13819 6822 -4185 -919 -229 N
ATOM 1678 N ALA A1035 12.578 15.519 -43.682 1.00 79.43 N
ANISOU 1678 N ALA A1035 8977 12555 8648 -3692 -1614 -237 N
ATOM 1679 CA ALA A1035 12.482 15.964 -42.296 1.00 76.88 C
ANISOU 1679 CA ALA A1035 8509 12336 8365 -3530 -1686 -328 C
ATOM 1680 C ALA A1035 11.654 14.992 -41.467 1.00 84.98 C
ANISOU 1680 C ALA A1035 9456 13417 9414 -3294 -1697 -307 C
ATOM 1681 O ALA A1035 12.018 14.665 -40.332 1.00 82.21 O
ANISOU 1681 O ALA A1035 8883 13350 9001 -3046 -1639 -339 O
ATOM 1682 CB ALA A1035 11.880 17.367 -42.239 1.00 73.42 C
ANISOU 1682 CB ALA A1035 8268 11523 8107 -3567 -1799 -385 C
ATOM 1683 N ALA A1036 10.535 14.517 -42.019 1.00 75.18 N
ANISOU 1683 N ALA A1036 8443 11823 8301 -3234 -1691 -238 N
ATOM 1684 CA ALA A1036 9.726 13.529 -41.314 1.00 66.35 C
ANISOU 1684 CA ALA A1036 7320 10630 7262 -2876 -1593 -195 C
ATOM 1685 C ALA A1036 10.507 12.241 -41.091 1.00 70.96 C
ANISOU 1685 C ALA A1036 7727 11517 7719 -2596 -1326 -119 C
ATOM 1686 O ALA A1036 10.418 11.628 -40.021 1.00 72.49 O
ANISOU 1686 O ALA A1036 7782 11855 7905 -2270 -1230 -107 O
ATOM 1687 CB ALA A1036 8.443 13.249 -42.095 1.00 68.41 C
ANISOU 1687 CB ALA A1036 7852 10465 7676 -2899 -1623 -152 C
ATOM 1688 N ALA A1037 11.274 11.810 -42.096 1.00 74.76 N
ANISOU 1688 N ALA A1037 8215 12096 8094 -2707 -1196 -59 N
ATOM 1689 CA ALA A1037 12.103 10.621 -41.934 1.00 71.37 C
ANISOU 1689 CA ALA A1037 7617 11969 7532 -2450 -933 20 C
ATOM 1690 C ALA A1037 13.160 10.829 -40.856 1.00 85.21 C
ANISOU 1690 C ALA A1037 9074 14170 9133 -2326 -915 -29 C
ATOM 1691 O ALA A1037 13.444 9.918 -40.070 1.00 86.42 O
ANISOU 1691 O ALA A1037 9066 14557 9214 -1978 -734 22 O
ATOM 1692 CB ALA A1037 12.761 10.259 -43.264 1.00 72.61 C
ANISOU 1692 CB ALA A1037 7842 12146 7602 -2631 -818 84 C
ATOM 1693 N LEU A1038 13.759 12.021 -40.808 1.00 89.34 N
ANISOU 1693 N LEU A1038 9517 14826 9602 -2604 -1090 -132 N
ATOM 1694 CA LEU A1038 14.788 12.291 -39.809 1.00 87.45 C
ANISOU 1694 CA LEU A1038 8977 15038 9212 -2514 -1085 -208 C
ATOM 1695 C LEU A1038 14.203 12.326 -38.402 1.00 88.15 C
ANISOU 1695 C LEU A1038 8965 15174 9354 -2238 -1144 -256 C
ATOM 1696 O LEU A1038 14.819 11.823 -37.455 1.00 87.23 O
ANISOU 1696 O LEU A1038 8604 15432 9108 -1949 -1030 -256 O
ATOM 1697 CB LEU A1038 15.493 13.609 -40.131 1.00 86.25 C
ANISOU 1697 CB LEU A1038 8777 14980 9014 -2909 -1254 -329 C
ATOM 1698 CG LEU A1038 16.393 13.588 -41.370 1.00 96.87 C
ANISOU 1698 CG LEU A1038 10151 16396 10259 -3163 -1173 -290 C
ATOM 1699 CD1 LEU A1038 16.842 14.995 -41.735 1.00100.22 C
ANISOU 1699 CD1 LEU A1038 10595 16793 10690 -3564 -1338 -408 C
ATOM 1700 CD2 LEU A1038 17.596 12.687 -41.139 1.00106.88 C
ANISOU 1700 CD2 LEU A1038 11163 18122 11323 -2951 -958 -247 C
ATOM 1701 N ASP A1039 13.013 12.913 -38.242 1.00 82.02 N
ANISOU 1701 N ASP A1039 8372 14033 8761 -2308 -1317 -295 N
ATOM 1702 CA ASP A1039 12.417 13.019 -36.914 1.00 82.05 C
ANISOU 1702 CA ASP A1039 8288 14063 8823 -2062 -1386 -346 C
ATOM 1703 C ASP A1039 12.179 11.649 -36.294 1.00 78.84 C
ANISOU 1703 C ASP A1039 7817 13741 8396 -1609 -1159 -235 C
ATOM 1704 O ASP A1039 12.229 11.506 -35.067 1.00 78.31 O
ANISOU 1704 O ASP A1039 7572 13899 8284 -1328 -1140 -261 O
ATOM 1705 CB ASP A1039 11.104 13.800 -36.989 1.00 87.93 C
ANISOU 1705 CB ASP A1039 9271 14361 9777 -2216 -1597 -390 C
ATOM 1706 CG ASP A1039 11.311 15.261 -37.342 1.00 78.90 C
ANISOU 1706 CG ASP A1039 8175 13147 8657 -2624 -1819 -506 C
ATOM 1707 OD1 ASP A1039 12.474 15.668 -37.539 1.00 73.96 O
ANISOU 1707 OD1 ASP A1039 7424 12764 7911 -2762 -1777 -553 O
ATOM 1708 OD2 ASP A1039 10.309 16.001 -37.420 1.00 93.50 O
ANISOU 1708 OD2 ASP A1039 10252 14581 10692 -2701 -1952 -532 O
ATOM 1709 N ALA A1040 11.915 10.633 -37.117 1.00 77.83 N
ANISOU 1709 N ALA A1040 7834 13436 8303 -1529 -976 -114 N
ATOM 1710 CA ALA A1040 11.714 9.287 -36.594 1.00 86.93 C
ANISOU 1710 CA ALA A1040 8940 14647 9444 -1105 -722 -4 C
ATOM 1711 C ALA A1040 13.007 8.669 -36.078 1.00 85.46 C
ANISOU 1711 C ALA A1040 8475 14965 9031 -866 -530 38 C
ATOM 1712 O ALA A1040 12.953 7.697 -35.318 1.00 84.63 O
ANISOU 1712 O ALA A1040 8279 14987 8889 -465 -328 121 O
ATOM 1713 CB ALA A1040 11.106 8.390 -37.672 1.00 86.72 C
ANISOU 1713 CB ALA A1040 9142 14290 9520 -1111 -566 95 C
ATOM 1714 N GLN A1041 14.163 9.207 -36.471 1.00 85.71 N
ANISOU 1714 N GLN A1041 8370 15289 8908 -1095 -578 -15 N
ATOM 1715 CA GLN A1041 15.433 8.641 -36.033 1.00 89.41 C
ANISOU 1715 CA GLN A1041 8562 16264 9146 -876 -401 19 C
ATOM 1716 C GLN A1041 15.853 9.184 -34.672 1.00 99.39 C
ANISOU 1716 C GLN A1041 9559 17903 10303 -722 -500 -86 C
ATOM 1717 O GLN A1041 16.320 8.424 -33.816 1.00104.39 O
ANISOU 1717 O GLN A1041 9990 18877 10796 -336 -327 -30 O
ATOM 1718 CB GLN A1041 16.516 8.922 -37.074 1.00 94.81 C
ANISOU 1718 CB GLN A1041 9205 17113 9705 -1185 -394 3 C
ATOM 1719 N LYS A1042 15.702 10.494 -34.453 1.00 95.93 N
ANISOU 1719 N LYS A1042 9112 17414 9923 -1011 -768 -241 N
ATOM 1720 CA LYS A1042 16.093 11.074 -33.172 1.00 98.12 C
ANISOU 1720 CA LYS A1042 9128 18051 10102 -891 -873 -366 C
ATOM 1721 C LYS A1042 15.227 10.553 -32.032 1.00100.00 C
ANISOU 1721 C LYS A1042 9358 18230 10406 -486 -828 -318 C
ATOM 1722 O LYS A1042 15.662 10.553 -30.875 1.00101.93 O
ANISOU 1722 O LYS A1042 9350 18861 10519 -228 -818 -370 O
ATOM 1723 CB LYS A1042 16.012 12.602 -33.237 1.00 99.00 C
ANISOU 1723 CB LYS A1042 9263 18060 10291 -1308 -1158 -546 C
ATOM 1724 CG LYS A1042 14.632 13.177 -32.920 1.00 94.85 C
ANISOU 1724 CG LYS A1042 8947 17101 9991 -1358 -1339 -581 C
ATOM 1725 CD LYS A1042 14.558 14.677 -33.184 1.00 89.75 C
ANISOU 1725 CD LYS A1042 8407 16242 9451 -1777 -1566 -730 C
ATOM 1726 CE LYS A1042 15.635 15.445 -32.427 1.00 92.99 C
ANISOU 1726 CE LYS A1042 8648 16915 9771 -1781 -1546 -865 C
ATOM 1727 NZ LYS A1042 15.693 15.085 -30.981 1.00 92.40 N
ANISOU 1727 NZ LYS A1042 8364 17135 9610 -1397 -1495 -894 N
ATOM 1728 N ALA A1043 14.004 10.114 -32.334 1.00 99.60 N
ANISOU 1728 N ALA A1043 9575 17712 10556 -423 -797 -227 N
ATOM 1729 CA ALA A1043 13.093 9.663 -31.287 1.00 95.81 C
ANISOU 1729 CA ALA A1043 9111 17129 10164 -60 -754 -185 C
ATOM 1730 C ALA A1043 13.659 8.457 -30.545 1.00 84.34 C
ANISOU 1730 C ALA A1043 7464 16038 8544 426 -474 -68 C
ATOM 1731 O ALA A1043 13.945 8.526 -29.345 1.00 76.48 O
ANISOU 1731 O ALA A1043 6245 15380 7435 694 -481 -109 O
ATOM 1732 CB ALA A1043 11.728 9.334 -31.894 1.00 86.79 C
ANISOU 1732 CB ALA A1043 8291 15419 9264 -102 -746 -112 C
ATOM 1733 N THR A1044 13.826 7.338 -31.247 1.00 84.42 N
ANISOU 1733 N THR A1044 7557 15988 8532 556 -215 81 N
ATOM 1734 CA THR A1044 14.266 6.080 -30.644 1.00 92.08 C
ANISOU 1734 CA THR A1044 8386 17238 9360 1038 94 221 C
ATOM 1735 C THR A1044 15.383 5.470 -31.484 1.00100.37 C
ANISOU 1735 C THR A1044 9365 18527 10244 1004 284 299 C
ATOM 1736 O THR A1044 15.179 4.469 -32.182 1.00 93.00 O
ANISOU 1736 O THR A1044 8585 17387 9364 1097 516 432 O
ATOM 1737 CB THR A1044 13.098 5.101 -30.506 1.00 91.50 C
ANISOU 1737 CB THR A1044 8520 16777 9468 1320 283 347 C
ATOM 1738 OG1 THR A1044 12.784 4.537 -31.785 1.00 88.17 O
ANISOU 1738 OG1 THR A1044 8331 16009 9161 1148 405 421 O
ATOM 1739 CG2 THR A1044 11.868 5.810 -29.957 1.00 85.82 C
ANISOU 1739 CG2 THR A1044 7926 15729 8953 1257 63 261 C
ATOM 1740 N PRO A1045 16.594 6.050 -31.434 1.00111.50 N
ANISOU 1740 N PRO A1045 10536 20381 11450 868 197 209 N
ATOM 1741 CA PRO A1045 17.732 5.469 -32.155 1.00111.87 C
ANISOU 1741 CA PRO A1045 10487 20701 11317 858 381 282 C
ATOM 1742 C PRO A1045 18.273 4.211 -31.483 1.00107.49 C
ANISOU 1742 C PRO A1045 9766 20489 10585 1383 701 432 C
ATOM 1743 O PRO A1045 17.880 3.923 -30.353 1.00108.73 O
ANISOU 1743 O PRO A1045 9953 20603 10756 1714 702 462 O
ATOM 1744 CB PRO A1045 18.773 6.591 -32.129 1.00114.22 C
ANISOU 1744 CB PRO A1045 10560 21375 11463 558 170 111 C
ATOM 1745 CG PRO A1045 18.456 7.365 -30.903 1.00112.14 C
ANISOU 1745 CG PRO A1045 10158 21243 11206 640 -23 -20 C
ATOM 1746 CD PRO A1045 16.958 7.300 -30.745 1.00115.02 C
ANISOU 1746 CD PRO A1045 10788 21087 11827 693 -74 22 C
ATOM 1747 N ASP A1066 18.190 4.642 -42.815 1.00 60.66 N
ANISOU 1747 N ASP A1066 5395 12457 5196 -1370 613 554 N
ATOM 1748 CA ASP A1066 19.395 4.886 -43.596 1.00 74.70 C
ANISOU 1748 CA ASP A1066 7082 14488 6812 -1599 627 552 C
ATOM 1749 C ASP A1066 19.090 4.788 -45.082 1.00 64.10 C
ANISOU 1749 C ASP A1066 5985 12821 5548 -1879 636 586 C
ATOM 1750 O ASP A1066 19.242 5.759 -45.823 1.00 71.07 O
ANISOU 1750 O ASP A1066 6943 13619 6441 -2253 447 520 O
ATOM 1751 CB ASP A1066 20.495 3.892 -43.215 1.00 63.44 C
ANISOU 1751 CB ASP A1066 5431 13493 5182 -1283 898 645 C
ATOM 1752 N ILE A1067 18.649 3.607 -45.514 1.00 60.64 N
ANISOU 1752 N ILE A1067 5672 12202 5167 -1692 867 687 N
ATOM 1753 CA ILE A1067 18.330 3.415 -46.923 1.00 60.07 C
ANISOU 1753 CA ILE A1067 5824 11836 5163 -1932 892 713 C
ATOM 1754 C ILE A1067 17.176 4.320 -47.328 1.00 65.87 C
ANISOU 1754 C ILE A1067 6780 12167 6081 -2200 631 629 C
ATOM 1755 O ILE A1067 17.150 4.854 -48.443 1.00 68.24 O
ANISOU 1755 O ILE A1067 7225 12307 6396 -2525 518 608 O
ATOM 1756 CB ILE A1067 18.019 1.934 -47.205 1.00 69.10 C
ANISOU 1756 CB ILE A1067 7050 12861 6346 -1660 1207 818 C
ATOM 1757 CG1 ILE A1067 18.122 1.651 -48.705 1.00 71.13 C
ANISOU 1757 CG1 ILE A1067 7470 12954 6601 -1901 1272 848 C
ATOM 1758 CG2 ILE A1067 16.633 1.564 -46.688 1.00 58.08 C
ANISOU 1758 CG2 ILE A1067 5791 11127 5152 -1475 1223 803 C
ATOM 1759 CD1 ILE A1067 17.836 0.211 -49.078 1.00 66.22 C
ANISOU 1759 CD1 ILE A1067 6934 12203 6023 -1670 1593 934 C
ATOM 1760 N LEU A1068 16.209 4.515 -46.430 1.00 65.26 N
ANISOU 1760 N LEU A1068 6733 11926 6137 -2058 535 585 N
ATOM 1761 CA LEU A1068 15.090 5.403 -46.723 1.00 61.10 C
ANISOU 1761 CA LEU A1068 6407 11031 5779 -2289 282 506 C
ATOM 1762 C LEU A1068 15.586 6.813 -47.013 1.00 60.28 C
ANISOU 1762 C LEU A1068 6285 10997 5620 -2647 25 429 C
ATOM 1763 O LEU A1068 15.400 7.340 -48.115 1.00 67.35 O
ANISOU 1763 O LEU A1068 7351 11690 6548 -2950 -85 415 O
ATOM 1764 CB LEU A1068 14.104 5.399 -45.553 1.00 69.24 C
ANISOU 1764 CB LEU A1068 7435 11931 6943 -2054 227 470 C
ATOM 1765 CG LEU A1068 12.811 6.203 -45.723 1.00 67.24 C
ANISOU 1765 CG LEU A1068 7387 11285 6875 -2234 -17 393 C
ATOM 1766 CD1 LEU A1068 11.761 5.713 -44.744 1.00 83.05 C
ANISOU 1766 CD1 LEU A1068 9412 13123 9021 -1936 30 386 C
ATOM 1767 CD2 LEU A1068 13.042 7.695 -45.529 1.00 56.53 C
ANISOU 1767 CD2 LEU A1068 5998 9981 5498 -2508 -306 305 C
ATOM 1768 N VAL A1069 16.230 7.441 -46.027 1.00 59.82 N
ANISOU 1768 N VAL A1069 6018 11232 5479 -2614 -62 373 N
ATOM 1769 CA VAL A1069 16.756 8.785 -46.235 1.00 68.13 C
ANISOU 1769 CA VAL A1069 7039 12361 6487 -2957 -280 285 C
ATOM 1770 C VAL A1069 17.758 8.783 -47.381 1.00 74.62 C
ANISOU 1770 C VAL A1069 7861 13310 7180 -3189 -207 322 C
ATOM 1771 O VAL A1069 17.774 9.697 -48.215 1.00 75.95 O
ANISOU 1771 O VAL A1069 8157 13330 7371 -3531 -356 286 O
ATOM 1772 CB VAL A1069 17.380 9.324 -44.935 1.00 60.33 C
ANISOU 1772 CB VAL A1069 5790 11719 5415 -2858 -350 203 C
ATOM 1773 CG1 VAL A1069 18.001 10.691 -45.170 1.00 67.10 C
ANISOU 1773 CG1 VAL A1069 6604 12663 6228 -3230 -545 97 C
ATOM 1774 CG2 VAL A1069 16.333 9.401 -43.841 1.00 59.17 C
ANISOU 1774 CG2 VAL A1069 5659 11422 5400 -2646 -439 165 C
ATOM 1775 N GLY A1070 18.604 7.754 -47.446 1.00 74.15 N
ANISOU 1775 N GLY A1070 7666 13524 6985 -2997 34 401 N
ATOM 1776 CA GLY A1070 19.540 7.655 -48.553 1.00 74.71 C
ANISOU 1776 CA GLY A1070 7739 13713 6934 -3198 121 444 C
ATOM 1777 C GLY A1070 18.839 7.614 -49.896 1.00 69.94 C
ANISOU 1777 C GLY A1070 7417 12729 6427 -3407 95 483 C
ATOM 1778 O GLY A1070 19.270 8.263 -50.853 1.00 68.31 O
ANISOU 1778 O GLY A1070 7286 12491 6177 -3720 17 474 O
ATOM 1779 N GLN A1071 17.746 6.853 -49.987 1.00 64.76 N
ANISOU 1779 N GLN A1071 6919 11787 5901 -3233 165 522 N
ATOM 1780 CA GLN A1071 16.971 6.827 -51.222 1.00 64.81 C
ANISOU 1780 CA GLN A1071 7186 11439 6001 -3419 126 539 C
ATOM 1781 C GLN A1071 16.218 8.133 -51.435 1.00 66.49 C
ANISOU 1781 C GLN A1071 7557 11384 6321 -3690 -161 464 C
ATOM 1782 O GLN A1071 16.012 8.546 -52.581 1.00 73.20 O
ANISOU 1782 O GLN A1071 8587 12041 7184 -3944 -240 471 O
ATOM 1783 CB GLN A1071 16.005 5.645 -51.213 1.00 57.76 C
ANISOU 1783 CB GLN A1071 6397 10327 5221 -3160 290 578 C
ATOM 1784 CG GLN A1071 16.693 4.304 -51.403 1.00 64.51 C
ANISOU 1784 CG GLN A1071 7162 11372 5978 -2942 604 667 C
ATOM 1785 CD GLN A1071 15.736 3.136 -51.295 1.00 67.88 C
ANISOU 1785 CD GLN A1071 7684 11576 6531 -2680 793 692 C
ATOM 1786 OE1 GLN A1071 14.553 3.312 -51.005 1.00 62.83 O
ANISOU 1786 OE1 GLN A1071 7163 10656 6053 -2648 685 638 O
ATOM 1787 NE2 GLN A1071 16.245 1.932 -51.530 1.00 67.54 N
ANISOU 1787 NE2 GLN A1071 7591 11653 6420 -2492 1088 772 N
ATOM 1788 N ILE A1072 15.791 8.790 -50.355 1.00 61.42 N
ANISOU 1788 N ILE A1072 6856 10727 5752 -3632 -313 395 N
ATOM 1789 CA ILE A1072 15.229 10.129 -50.495 1.00 60.57 C
ANISOU 1789 CA ILE A1072 6882 10400 5733 -3897 -579 325 C
ATOM 1790 C ILE A1072 16.285 11.086 -51.027 1.00 68.48 C
ANISOU 1790 C ILE A1072 7836 11561 6620 -4211 -652 303 C
ATOM 1791 O ILE A1072 16.003 11.932 -51.883 1.00 68.57 O
ANISOU 1791 O ILE A1072 8028 11356 6668 -4490 -791 294 O
ATOM 1792 CB ILE A1072 14.646 10.616 -49.156 1.00 57.58 C
ANISOU 1792 CB ILE A1072 6429 10001 5448 -3760 -712 251 C
ATOM 1793 CG1 ILE A1072 13.369 9.839 -48.834 1.00 56.57 C
ANISOU 1793 CG1 ILE A1072 6411 9617 5465 -3509 -669 267 C
ATOM 1794 CG2 ILE A1072 14.381 12.120 -49.214 1.00 63.62 C
ANISOU 1794 CG2 ILE A1072 7287 10613 6271 -4055 -970 174 C
ATOM 1795 CD1 ILE A1072 12.665 10.293 -47.575 1.00 64.02 C
ANISOU 1795 CD1 ILE A1072 7308 10502 6515 -3370 -803 201 C
ATOM 1796 N ASP A1073 17.516 10.974 -50.523 1.00 73.03 N
ANISOU 1796 N ASP A1073 8168 12526 7056 -4165 -553 292 N
ATOM 1797 CA ASP A1073 18.597 11.815 -51.026 1.00 69.61 C
ANISOU 1797 CA ASP A1073 7670 12266 6513 -4464 -595 261 C
ATOM 1798 C ASP A1073 18.793 11.602 -52.520 1.00 74.09 C
ANISOU 1798 C ASP A1073 8405 12711 7036 -4653 -526 339 C
ATOM 1799 O ASP A1073 18.904 12.565 -53.288 1.00 73.41 O
ANISOU 1799 O ASP A1073 8443 12496 6953 -4963 -640 323 O
ATOM 1800 CB ASP A1073 19.890 11.515 -50.269 1.00 64.10 C
ANISOU 1800 CB ASP A1073 6660 12038 5655 -4342 -470 236 C
ATOM 1801 CG ASP A1073 19.765 11.768 -48.782 1.00 71.25 C
ANISOU 1801 CG ASP A1073 7383 13105 6586 -4154 -542 149 C
ATOM 1802 OD1 ASP A1073 18.683 12.211 -48.343 1.00 78.07 O
ANISOU 1802 OD1 ASP A1073 8366 13699 7596 -4132 -692 110 O
ATOM 1803 OD2 ASP A1073 20.749 11.525 -48.052 1.00 76.86 O
ANISOU 1803 OD2 ASP A1073 7823 14221 7160 -4020 -450 119 O
ATOM 1804 N ASP A1074 18.823 10.341 -52.954 1.00 77.82 N
ANISOU 1804 N ASP A1074 8888 13212 7466 -4465 -329 426 N
ATOM 1805 CA ASP A1074 18.902 10.060 -54.383 1.00 77.35 C
ANISOU 1805 CA ASP A1074 8997 13022 7370 -4625 -262 497 C
ATOM 1806 C ASP A1074 17.683 10.613 -55.108 1.00 77.39 C
ANISOU 1806 C ASP A1074 9282 12615 7507 -4778 -427 490 C
ATOM 1807 O ASP A1074 17.804 11.182 -56.199 1.00 80.84 O
ANISOU 1807 O ASP A1074 9867 12936 7915 -5038 -486 513 O
ATOM 1808 CB ASP A1074 19.029 8.556 -54.618 1.00 77.24 C
ANISOU 1808 CB ASP A1074 8947 13092 7308 -4371 -11 578 C
ATOM 1809 CG ASP A1074 20.234 7.956 -53.919 1.00 86.42 C
ANISOU 1809 CG ASP A1074 9835 14675 8325 -4188 167 599 C
ATOM 1810 OD1 ASP A1074 20.914 8.686 -53.167 1.00 83.90 O
ANISOU 1810 OD1 ASP A1074 9337 14597 7946 -4244 85 536 O
ATOM 1811 OD2 ASP A1074 20.502 6.753 -54.124 1.00 91.96 O
ANISOU 1811 OD2 ASP A1074 10496 15474 8969 -3985 395 675 O
ATOM 1812 N ALA A1075 16.497 10.453 -54.516 1.00 73.29 N
ANISOU 1812 N ALA A1075 8839 11880 7128 -4608 -499 461 N
ATOM 1813 CA ALA A1075 15.301 11.063 -55.086 1.00 70.80 C
ANISOU 1813 CA ALA A1075 8772 11193 6934 -4740 -676 444 C
ATOM 1814 C ALA A1075 15.409 12.582 -55.084 1.00 75.10 C
ANISOU 1814 C ALA A1075 9383 11656 7494 -4965 -873 399 C
ATOM 1815 O ALA A1075 15.031 13.241 -56.060 1.00 73.87 O
ANISOU 1815 O ALA A1075 9457 11250 7360 -5019 -939 425 O
ATOM 1816 CB ALA A1075 14.064 10.612 -54.312 1.00 70.01 C
ANISOU 1816 CB ALA A1075 8713 10904 6982 -4495 -708 410 C
ATOM 1817 N LEU A1076 15.916 13.159 -53.991 1.00 74.84 N
ANISOU 1817 N LEU A1076 9177 11802 7455 -4938 -922 336 N
ATOM 1818 CA LEU A1076 16.095 14.606 -53.940 1.00 70.39 C
ANISOU 1818 CA LEU A1076 8700 11120 6926 -4994 -1030 296 C
ATOM 1819 C LEU A1076 17.126 15.066 -54.960 1.00 75.79 C
ANISOU 1819 C LEU A1076 9422 11881 7493 -5185 -966 331 C
ATOM 1820 O LEU A1076 16.948 16.107 -55.604 1.00 75.55 O
ANISOU 1820 O LEU A1076 9579 11628 7500 -5259 -1033 343 O
ATOM 1821 CB LEU A1076 16.514 15.039 -52.535 1.00 62.29 C
ANISOU 1821 CB LEU A1076 7455 10300 5911 -4926 -1069 206 C
ATOM 1822 CG LEU A1076 15.523 15.924 -51.776 1.00 63.38 C
ANISOU 1822 CG LEU A1076 7692 10176 6213 -4804 -1214 150 C
ATOM 1823 CD1 LEU A1076 16.084 16.293 -50.415 1.00 71.41 C
ANISOU 1823 CD1 LEU A1076 8472 11439 7221 -4743 -1236 53 C
ATOM 1824 CD2 LEU A1076 15.179 17.177 -52.571 1.00 65.70 C
ANISOU 1824 CD2 LEU A1076 8225 10160 6580 -4887 -1288 168 C
ATOM 1825 N LYS A1077 18.211 14.305 -55.120 1.00 80.26 N
ANISOU 1825 N LYS A1077 9804 12775 7916 -5260 -826 352 N
ATOM 1826 CA LYS A1077 19.255 14.699 -56.059 1.00 81.86 C
ANISOU 1826 CA LYS A1077 10032 13070 8003 -5438 -758 380 C
ATOM 1827 C LYS A1077 18.714 14.804 -57.478 1.00 81.80 C
ANISOU 1827 C LYS A1077 10303 12773 8005 -5504 -774 458 C
ATOM 1828 O LYS A1077 19.218 15.601 -58.276 1.00 72.78 O
ANISOU 1828 O LYS A1077 9265 11574 6814 -5642 -778 475 O
ATOM 1829 CB LYS A1077 20.412 13.699 -55.999 1.00 72.49 C
ANISOU 1829 CB LYS A1077 8589 12292 6662 -5470 -587 401 C
ATOM 1830 CG LYS A1077 21.595 14.056 -56.885 1.00 86.00 C
ANISOU 1830 CG LYS A1077 10298 14133 8245 -5643 -508 420 C
ATOM 1831 CD LYS A1077 22.698 13.009 -56.797 1.00 80.87 C
ANISOU 1831 CD LYS A1077 9385 13897 7446 -5630 -322 451 C
ATOM 1832 CE LYS A1077 23.879 13.366 -57.692 1.00 70.63 C
ANISOU 1832 CE LYS A1077 8093 12720 6023 -5793 -248 462 C
ATOM 1833 NZ LYS A1077 24.543 14.634 -57.275 1.00 72.25 N
ANISOU 1833 NZ LYS A1077 8247 12983 6222 -5906 -323 358 N
ATOM 1834 N LEU A1078 17.694 14.012 -57.812 1.00 78.23 N
ANISOU 1834 N LEU A1078 9966 12148 7611 -5405 -778 498 N
ATOM 1835 CA LEU A1078 17.128 14.050 -59.156 1.00 75.30 C
ANISOU 1835 CA LEU A1078 9842 11531 7237 -5446 -797 560 C
ATOM 1836 C LEU A1078 16.158 15.213 -59.325 1.00 75.42 C
ANISOU 1836 C LEU A1078 10069 11226 7361 -5411 -954 551 C
ATOM 1837 O LEU A1078 16.121 15.844 -60.387 1.00 73.61 O
ANISOU 1837 O LEU A1078 10015 10858 7096 -5502 -984 596 O
ATOM 1838 CB LEU A1078 16.426 12.727 -59.458 1.00 65.81 C
ANISOU 1838 CB LEU A1078 8667 10281 6056 -5352 -721 588 C
ATOM 1839 CG LEU A1078 17.316 11.487 -59.372 1.00 72.56 C
ANISOU 1839 CG LEU A1078 9314 11444 6812 -5365 -518 622 C
ATOM 1840 CD1 LEU A1078 16.482 10.255 -59.075 1.00 86.36 C
ANISOU 1840 CD1 LEU A1078 11046 13132 8637 -5175 -421 628 C
ATOM 1841 CD2 LEU A1078 18.104 11.301 -60.658 1.00 80.77 C
ANISOU 1841 CD2 LEU A1078 10415 12551 7722 -5482 -415 683 C
ATOM 1842 N ALA A1079 15.376 15.517 -58.286 1.00 79.89 N
ANISOU 1842 N ALA A1079 10615 11684 8056 -5275 -1049 499 N
ATOM 1843 CA ALA A1079 14.342 16.538 -58.410 1.00 84.57 C
ANISOU 1843 CA ALA A1079 11396 11975 8760 -5212 -1184 498 C
ATOM 1844 C ALA A1079 14.939 17.902 -58.733 1.00 85.51 C
ANISOU 1844 C ALA A1079 11578 12059 8853 -5351 -1215 503 C
ATOM 1845 O ALA A1079 14.394 18.647 -59.556 1.00 85.33 O
ANISOU 1845 O ALA A1079 11752 11823 8845 -5382 -1279 547 O
ATOM 1846 CB ALA A1079 13.520 16.607 -57.122 1.00 84.05 C
ANISOU 1846 CB ALA A1079 11267 11830 8836 -5038 -1265 434 C
ATOM 1847 N ASN A1080 16.056 18.251 -58.092 1.00 90.26 N
ANISOU 1847 N ASN A1080 12005 12876 9412 -5441 -1166 454 N
ATOM 1848 CA ASN A1080 16.636 19.575 -58.293 1.00 96.65 C
ANISOU 1848 CA ASN A1080 12861 13645 10215 -5580 -1181 438 C
ATOM 1849 C ASN A1080 17.055 19.787 -59.744 1.00 96.26 C
ANISOU 1849 C ASN A1080 12961 13554 10059 -5737 -1135 515 C
ATOM 1850 O ASN A1080 16.816 20.857 -60.316 1.00100.62 O
ANISOU 1850 O ASN A1080 13678 13918 10636 -5809 -1184 541 O
ATOM 1851 CB ASN A1080 17.830 19.771 -57.358 1.00100.95 C
ANISOU 1851 CB ASN A1080 13165 14468 10722 -5650 -1120 352 C
ATOM 1852 CG ASN A1080 17.418 19.902 -55.904 1.00 94.14 C
ANISOU 1852 CG ASN A1080 12171 13628 9972 -5506 -1185 265 C
ATOM 1853 OD1 ASN A1080 17.318 21.007 -55.372 1.00 88.07 O
ANISOU 1853 OD1 ASN A1080 11412 12758 9292 -5516 -1244 204 O
ATOM 1854 ND2 ASN A1080 17.173 18.770 -55.254 1.00 99.87 N
ANISOU 1854 ND2 ASN A1080 12767 14487 10693 -5373 -1168 256 N
ATOM 1855 N GLU A1081 17.676 18.781 -60.358 1.00 88.15 N
ANISOU 1855 N GLU A1081 11880 12703 8911 -5792 -1035 554 N
ATOM 1856 CA GLU A1081 18.238 18.927 -61.703 1.00 80.04 C
ANISOU 1856 CA GLU A1081 10969 11674 7769 -5946 -978 621 C
ATOM 1857 C GLU A1081 17.243 18.449 -62.763 1.00 78.48 C
ANISOU 1857 C GLU A1081 10972 11287 7560 -5890 -1017 696 C
ATOM 1858 O GLU A1081 17.525 17.578 -63.584 1.00 82.03 O
ANISOU 1858 O GLU A1081 11433 11823 7911 -5925 -941 740 O
ATOM 1859 CB GLU A1081 19.567 18.183 -61.807 1.00 78.90 C
ANISOU 1859 CB GLU A1081 10643 11844 7493 -6043 -840 615 C
ATOM 1860 CG GLU A1081 19.602 16.825 -61.119 1.00 84.35 C
ANISOU 1860 CG GLU A1081 11147 12737 8165 -5928 -776 598 C
ATOM 1861 CD GLU A1081 20.917 16.098 -61.323 1.00 77.97 C
ANISOU 1861 CD GLU A1081 10158 12252 7213 -6016 -627 605 C
ATOM 1862 OE1 GLU A1081 21.648 16.442 -62.275 1.00 88.42 O
ANISOU 1862 OE1 GLU A1081 11546 13603 8448 -6157 -577 637 O
ATOM 1863 OE2 GLU A1081 21.223 15.184 -60.528 1.00 73.16 O
ANISOU 1863 OE2 GLU A1081 9337 11881 6579 -5937 -555 581 O
ATOM 1864 N GLY A1082 16.061 19.061 -62.734 1.00 80.44 N
ANISOU 1864 N GLY A1082 11373 11281 7909 -5798 -1136 704 N
ATOM 1865 CA GLY A1082 15.049 18.851 -63.754 1.00 90.23 C
ANISOU 1865 CA GLY A1082 12812 12335 9136 -5752 -1192 765 C
ATOM 1866 C GLY A1082 14.848 17.408 -64.168 1.00 89.37 C
ANISOU 1866 C GLY A1082 12672 12306 8978 -5692 -1128 776 C
ATOM 1867 O GLY A1082 15.103 17.049 -65.321 1.00 84.16 O
ANISOU 1867 O GLY A1082 12094 11673 8209 -5779 -1077 827 O
ATOM 1868 N LYS A1083 14.399 16.569 -63.237 1.00 78.35 N
ANISOU 1868 N LYS A1083 11158 10948 7664 -5547 -1119 725 N
ATOM 1869 CA LYS A1083 14.091 15.166 -63.503 1.00 77.16 C
ANISOU 1869 CA LYS A1083 10973 10850 7494 -5479 -1044 721 C
ATOM 1870 C LYS A1083 12.758 14.794 -62.876 1.00 80.05 C
ANISOU 1870 C LYS A1083 11365 11054 7998 -5291 -1117 674 C
ATOM 1871 O LYS A1083 12.628 13.791 -62.172 1.00 84.27 O
ANISOU 1871 O LYS A1083 11774 11666 8581 -5200 -1052 632 O
ATOM 1872 CB LYS A1083 15.195 14.243 -62.996 1.00 80.16 C
ANISOU 1872 CB LYS A1083 11136 11511 7812 -5516 -898 706 C
ATOM 1873 CG LYS A1083 16.536 14.450 -63.675 1.00 86.95 C
ANISOU 1873 CG LYS A1083 11955 12552 8530 -5689 -807 746 C
ATOM 1874 CD LYS A1083 17.510 13.347 -63.315 1.00 88.36 C
ANISOU 1874 CD LYS A1083 11916 13020 8636 -5698 -645 741 C
ATOM 1875 CE LYS A1083 18.838 13.524 -64.027 1.00 84.45 C
ANISOU 1875 CE LYS A1083 11376 12709 8001 -5852 -552 776 C
ATOM 1876 NZ LYS A1083 19.748 12.367 -63.799 1.00 89.22 N
ANISOU 1876 NZ LYS A1083 11772 13601 8527 -5829 -375 785 N
ATOM 1877 N VAL A1084 11.738 15.615 -63.132 1.00 78.88 N
ANISOU 1877 N VAL A1084 11378 10680 7914 -5231 -1246 682 N
ATOM 1878 CA VAL A1084 10.431 15.398 -62.516 1.00 75.02 C
ANISOU 1878 CA VAL A1084 10911 10028 7565 -5042 -1323 632 C
ATOM 1879 C VAL A1084 9.922 13.995 -62.822 1.00 77.51 C
ANISOU 1879 C VAL A1084 11211 10353 7888 -4972 -1246 598 C
ATOM 1880 O VAL A1084 9.468 13.271 -61.928 1.00 78.09 O
ANISOU 1880 O VAL A1084 11188 10423 8061 -4844 -1220 538 O
ATOM 1881 CB VAL A1084 9.436 16.472 -62.990 1.00 72.73 C
ANISOU 1881 CB VAL A1084 10806 9516 7315 -5005 -1461 658 C
ATOM 1882 CG1 VAL A1084 8.062 16.224 -62.391 1.00 83.69 C
ANISOU 1882 CG1 VAL A1084 12207 10746 8844 -4801 -1535 600 C
ATOM 1883 CG2 VAL A1084 9.939 17.856 -62.625 1.00 84.85 C
ANISOU 1883 CG2 VAL A1084 12355 11030 8857 -5082 -1515 682 C
ATOM 1884 N LYS A1085 9.991 13.587 -64.091 1.00 80.51 N
ANISOU 1884 N LYS A1085 11685 10742 8163 -5060 -1200 629 N
ATOM 1885 CA LYS A1085 9.459 12.281 -64.469 1.00 74.31 C
ANISOU 1885 CA LYS A1085 10893 9950 7389 -5003 -1114 581 C
ATOM 1886 C LYS A1085 10.210 11.156 -63.767 1.00 78.47 C
ANISOU 1886 C LYS A1085 11235 10660 7918 -5005 -952 556 C
ATOM 1887 O LYS A1085 9.595 10.218 -63.246 1.00 78.76 O
ANISOU 1887 O LYS A1085 11216 10660 8050 -4894 -890 493 O
ATOM 1888 CB LYS A1085 9.523 12.109 -65.987 1.00 77.66 C
ANISOU 1888 CB LYS A1085 11445 10377 7686 -5118 -1088 618 C
ATOM 1889 CG LYS A1085 8.559 12.999 -66.759 1.00 81.68 C
ANISOU 1889 CG LYS A1085 12141 10708 8187 -5106 -1239 640 C
ATOM 1890 CD LYS A1085 7.108 12.612 -66.500 1.00 88.82 C
ANISOU 1890 CD LYS A1085 13074 11454 9218 -4930 -1301 557 C
ATOM 1891 CE LYS A1085 6.143 13.446 -67.333 1.00 85.93 C
ANISOU 1891 CE LYS A1085 12884 10938 8826 -4922 -1445 582 C
ATOM 1892 NZ LYS A1085 4.723 13.236 -66.924 1.00 85.51 N
ANISOU 1892 NZ LYS A1085 12839 10740 8911 -4734 -1516 496 N
ATOM 1893 N GLU A1086 11.543 11.230 -63.740 1.00 72.25 N
ANISOU 1893 N GLU A1086 10347 10078 7028 -5130 -867 607 N
ATOM 1894 CA GLU A1086 12.323 10.168 -63.116 1.00 73.15 C
ANISOU 1894 CA GLU A1086 10268 10401 7125 -5134 -691 603 C
ATOM 1895 C GLU A1086 12.425 10.338 -61.605 1.00 74.47 C
ANISOU 1895 C GLU A1086 10280 10639 7378 -5057 -718 573 C
ATOM 1896 O GLU A1086 12.515 9.341 -60.881 1.00 76.04 O
ANISOU 1896 O GLU A1086 10332 10948 7614 -4997 -584 559 O
ATOM 1897 CB GLU A1086 13.726 10.112 -63.720 1.00 71.61 C
ANISOU 1897 CB GLU A1086 10004 10428 6776 -5281 -575 668 C
ATOM 1898 CG GLU A1086 14.457 8.811 -63.426 1.00 74.44 C
ANISOU 1898 CG GLU A1086 10181 11008 7095 -5254 -339 689 C
ATOM 1899 CD GLU A1086 15.960 8.935 -63.570 1.00 77.31 C
ANISOU 1899 CD GLU A1086 10419 11637 7320 -5352 -239 747 C
ATOM 1900 OE1 GLU A1086 16.443 10.052 -63.847 1.00 87.95 O
ANISOU 1900 OE1 GLU A1086 11817 12986 8613 -5469 -357 758 O
ATOM 1901 OE2 GLU A1086 16.660 7.915 -63.402 1.00 76.01 O
ANISOU 1901 OE2 GLU A1086 10103 11678 7098 -5287 -25 782 O
ATOM 1902 N ALA A1087 12.418 11.580 -61.113 1.00 76.65 N
ANISOU 1902 N ALA A1087 10580 10859 7685 -5056 -868 569 N
ATOM 1903 CA ALA A1087 12.465 11.797 -59.671 1.00 71.11 C
ANISOU 1903 CA ALA A1087 9731 10225 7063 -4976 -907 528 C
ATOM 1904 C ALA A1087 11.246 11.190 -58.992 1.00 76.07 C
ANISOU 1904 C ALA A1087 10369 10700 7835 -4805 -933 471 C
ATOM 1905 O ALA A1087 11.349 10.621 -57.899 1.00 78.07 O
ANISOU 1905 O ALA A1087 10459 11072 8133 -4744 -877 442 O
ATOM 1906 CB ALA A1087 12.558 13.291 -59.366 1.00 73.31 C
ANISOU 1906 CB ALA A1087 10059 10431 7365 -4997 -1049 525 C
ATOM 1907 N GLN A1088 10.078 11.306 -59.626 1.00 81.55 N
ANISOU 1907 N GLN A1088 11242 11145 8597 -4727 -1014 451 N
ATOM 1908 CA GLN A1088 8.878 10.679 -59.085 1.00 76.21 C
ANISOU 1908 CA GLN A1088 10582 10314 8061 -4563 -1027 384 C
ATOM 1909 C GLN A1088 9.027 9.164 -59.042 1.00 77.32 C
ANISOU 1909 C GLN A1088 10625 10552 8198 -4571 -828 367 C
ATOM 1910 O GLN A1088 8.559 8.513 -58.101 1.00 73.63 O
ANISOU 1910 O GLN A1088 10076 10064 7835 -4403 -764 324 O
ATOM 1911 CB GLN A1088 7.667 11.081 -59.923 1.00 67.78 C
ANISOU 1911 CB GLN A1088 9706 9001 7046 -4488 -1136 365 C
ATOM 1912 CG GLN A1088 7.335 12.558 -59.832 1.00 69.82 C
ANISOU 1912 CG GLN A1088 10053 9141 7336 -4458 -1303 390 C
ATOM 1913 CD GLN A1088 6.547 13.060 -61.024 1.00 77.85 C
ANISOU 1913 CD GLN A1088 11252 9999 8329 -4460 -1385 411 C
ATOM 1914 OE1 GLN A1088 6.738 12.601 -62.149 1.00 89.82 O
ANISOU 1914 OE1 GLN A1088 12832 11550 9745 -4555 -1327 431 O
ATOM 1915 NE2 GLN A1088 5.653 14.011 -60.782 1.00 82.80 N
ANISOU 1915 NE2 GLN A1088 11956 10464 9040 -4358 -1517 406 N
ATOM 1916 N ALA A1089 9.681 8.585 -60.051 1.00 65.99 N
ANISOU 1916 N ALA A1089 9199 9222 6651 -4688 -690 409 N
ATOM 1917 CA ALA A1089 9.899 7.143 -60.055 1.00 68.49 C
ANISOU 1917 CA ALA A1089 9424 9634 6967 -4510 -426 407 C
ATOM 1918 C ALA A1089 10.689 6.708 -58.828 1.00 67.34 C
ANISOU 1918 C ALA A1089 9066 9704 6814 -4326 -284 436 C
ATOM 1919 O ALA A1089 10.366 5.694 -58.198 1.00 69.08 O
ANISOU 1919 O ALA A1089 9214 9921 7113 -4084 -115 413 O
ATOM 1920 CB ALA A1089 10.621 6.729 -61.337 1.00 73.40 C
ANISOU 1920 CB ALA A1089 10083 10354 7452 -4639 -300 457 C
ATOM 1921 N ALA A1090 11.728 7.467 -58.468 1.00 69.97 N
ANISOU 1921 N ALA A1090 9296 10237 7054 -4432 -342 483 N
ATOM 1922 CA ALA A1090 12.496 7.142 -57.272 1.00 65.30 C
ANISOU 1922 CA ALA A1090 8487 9886 6437 -4253 -228 502 C
ATOM 1923 C ALA A1090 11.647 7.286 -56.017 1.00 58.64 C
ANISOU 1923 C ALA A1090 7608 8940 5733 -4071 -315 446 C
ATOM 1924 O ALA A1090 11.826 6.531 -55.055 1.00 62.82 O
ANISOU 1924 O ALA A1090 7990 9597 6283 -3818 -161 454 O
ATOM 1925 CB ALA A1090 13.736 8.033 -57.184 1.00 70.60 C
ANISOU 1925 CB ALA A1090 9051 10795 6979 -4433 -293 536 C
ATOM 1926 N ALA A1091 10.723 8.249 -56.005 1.00 59.69 N
ANISOU 1926 N ALA A1091 7875 8845 5958 -4187 -554 395 N
ATOM 1927 CA ALA A1091 9.831 8.391 -54.861 1.00 60.62 C
ANISOU 1927 CA ALA A1091 7974 8844 6216 -4018 -644 339 C
ATOM 1928 C ALA A1091 8.952 7.160 -54.684 1.00 60.89 C
ANISOU 1928 C ALA A1091 8030 8744 6362 -3771 -479 309 C
ATOM 1929 O ALA A1091 8.627 6.789 -53.550 1.00 63.56 O
ANISOU 1929 O ALA A1091 8274 9091 6784 -3540 -425 289 O
ATOM 1930 CB ALA A1091 8.969 9.643 -55.020 1.00 64.62 C
ANISOU 1930 CB ALA A1091 8642 9115 6798 -4197 -925 295 C
ATOM 1931 N GLU A1092 8.559 6.515 -55.784 1.00 60.66 N
ANISOU 1931 N GLU A1092 8120 8592 6337 -3815 -389 300 N
ATOM 1932 CA GLU A1092 7.696 5.345 -55.697 1.00 57.53 C
ANISOU 1932 CA GLU A1092 7750 8052 6058 -3606 -215 251 C
ATOM 1933 C GLU A1092 8.455 4.082 -55.310 1.00 61.48 C
ANISOU 1933 C GLU A1092 8101 8741 6516 -3382 103 302 C
ATOM 1934 O GLU A1092 7.831 3.132 -54.825 1.00 64.23 O
ANISOU 1934 O GLU A1092 8434 8993 6979 -3155 275 269 O
ATOM 1935 CB GLU A1092 6.964 5.130 -57.026 1.00 64.67 C
ANISOU 1935 CB GLU A1092 8827 8764 6979 -3740 -235 199 C
ATOM 1936 CG GLU A1092 6.169 6.347 -57.503 1.00 74.36 C
ANISOU 1936 CG GLU A1092 10215 9805 8233 -3942 -538 159 C
ATOM 1937 CD GLU A1092 5.030 6.718 -56.573 1.00 66.38 C
ANISOU 1937 CD GLU A1092 9234 8609 7379 -3831 -684 89 C
ATOM 1938 OE1 GLU A1092 4.708 5.915 -55.675 1.00 62.94 O
ANISOU 1938 OE1 GLU A1092 8712 8157 7047 -3596 -537 60 O
ATOM 1939 OE2 GLU A1092 4.457 7.814 -56.743 1.00 66.84 O
ANISOU 1939 OE2 GLU A1092 9405 8534 7457 -3963 -935 70 O
ATOM 1940 N GLN A1093 9.777 4.039 -55.503 1.00 56.96 N
ANISOU 1940 N GLN A1093 7421 8436 5787 -3434 197 383 N
ATOM 1941 CA GLN A1093 10.546 2.915 -54.984 1.00 57.32 C
ANISOU 1941 CA GLN A1093 7309 8687 5781 -3192 494 444 C
ATOM 1942 C GLN A1093 10.761 3.028 -53.485 1.00 59.15 C
ANISOU 1942 C GLN A1093 7380 9064 6031 -2972 498 463 C
ATOM 1943 O GLN A1093 11.039 2.017 -52.833 1.00 60.85 O
ANISOU 1943 O GLN A1093 7482 9392 6245 -2696 750 506 O
ATOM 1944 CB GLN A1093 11.902 2.801 -55.692 1.00 68.80 C
ANISOU 1944 CB GLN A1093 8693 10398 7052 -3309 599 523 C
ATOM 1945 CG GLN A1093 12.938 3.860 -55.308 1.00 70.44 C
ANISOU 1945 CG GLN A1093 8780 10851 7133 -3442 444 560 C
ATOM 1946 CD GLN A1093 14.366 3.363 -55.455 1.00 69.73 C
ANISOU 1946 CD GLN A1093 8536 11087 6871 -3409 640 643 C
ATOM 1947 OE1 GLN A1093 14.612 2.296 -56.021 1.00 59.13 O
ANISOU 1947 OE1 GLN A1093 7201 9772 5494 -3321 880 684 O
ATOM 1948 NE2 GLN A1093 15.317 4.135 -54.937 1.00 64.34 N
ANISOU 1948 NE2 GLN A1093 7707 10659 6080 -3481 545 660 N
ATOM 1949 N LEU A1094 10.632 4.234 -52.925 1.00 64.74 N
ANISOU 1949 N LEU A1094 8076 9771 6753 -3079 233 432 N
ATOM 1950 CA LEU A1094 10.715 4.379 -51.478 1.00 62.80 C
ANISOU 1950 CA LEU A1094 7679 9651 6532 -2868 218 432 C
ATOM 1951 C LEU A1094 9.709 3.475 -50.788 1.00 67.78 C
ANISOU 1951 C LEU A1094 8331 10105 7316 -2580 361 408 C
ATOM 1952 O LEU A1094 9.968 2.985 -49.683 1.00 75.52 O
ANISOU 1952 O LEU A1094 9166 11237 8292 -2305 499 443 O
ATOM 1953 CB LEU A1094 10.475 5.835 -51.074 1.00 62.35 C
ANISOU 1953 CB LEU A1094 7643 9548 6500 -3049 -100 379 C
ATOM 1954 CG LEU A1094 11.386 6.889 -51.705 1.00 53.80 C
ANISOU 1954 CG LEU A1094 6552 8603 5287 -3357 -253 389 C
ATOM 1955 CD1 LEU A1094 11.058 8.270 -51.158 1.00 53.49 C
ANISOU 1955 CD1 LEU A1094 6533 8492 5297 -3504 -536 328 C
ATOM 1956 CD2 LEU A1094 12.852 6.555 -51.474 1.00 71.94 C
ANISOU 1956 CD2 LEU A1094 8641 11280 7413 -3300 -91 449 C
ATOM 1957 N LYS A1095 8.564 3.229 -51.430 1.00 68.10 N
ANISOU 1957 N LYS A1095 8548 9836 7491 -2634 341 346 N
ATOM 1958 CA LYS A1095 7.567 2.336 -50.851 1.00 69.12 C
ANISOU 1958 CA LYS A1095 8705 9776 7781 -2380 496 308 C
ATOM 1959 C LYS A1095 8.164 0.969 -50.550 1.00 70.06 C
ANISOU 1959 C LYS A1095 8715 10042 7863 -2105 865 380 C
ATOM 1960 O LYS A1095 7.829 0.347 -49.535 1.00 66.50 O
ANISOU 1960 O LYS A1095 8200 9572 7494 -1816 1020 392 O
ATOM 1961 CB LYS A1095 6.375 2.201 -51.796 1.00 65.92 C
ANISOU 1961 CB LYS A1095 8493 9051 7502 -2509 444 216 C
ATOM 1962 CG LYS A1095 5.626 3.499 -52.031 1.00 59.80 C
ANISOU 1962 CG LYS A1095 7839 8107 6775 -2736 93 150 C
ATOM 1963 CD LYS A1095 4.497 3.316 -53.037 1.00 64.03 C
ANISOU 1963 CD LYS A1095 8552 8367 7410 -2852 49 55 C
ATOM 1964 CE LYS A1095 3.635 4.564 -53.144 1.00 73.88 C
ANISOU 1964 CE LYS A1095 9920 9438 8713 -3027 -288 -4 C
ATOM 1965 NZ LYS A1095 2.590 4.442 -54.201 1.00 77.45 N
ANISOU 1965 NZ LYS A1095 10534 9662 9232 -3143 -345 -98 N
ATOM 1966 N THR A1096 9.055 0.485 -51.417 1.00 60.71 N
ANISOU 1966 N THR A1096 7512 9001 6552 -2181 1020 435 N
ATOM 1967 CA THR A1096 9.686 -0.806 -51.173 1.00 64.55 C
ANISOU 1967 CA THR A1096 7900 9634 6992 -1918 1384 514 C
ATOM 1968 C THR A1096 10.451 -0.786 -49.859 1.00 70.08 C
ANISOU 1968 C THR A1096 8401 10620 7605 -1668 1443 594 C
ATOM 1969 O THR A1096 10.313 -1.692 -49.029 1.00 63.96 O
ANISOU 1969 O THR A1096 7563 9858 6881 -1344 1689 635 O
ATOM 1970 CB THR A1096 10.621 -1.167 -52.329 1.00 56.13 C
ANISOU 1970 CB THR A1096 6839 8705 5784 -2066 1506 564 C
ATOM 1971 OG1 THR A1096 11.725 -0.256 -52.351 1.00 68.97 O
ANISOU 1971 OG1 THR A1096 8361 10607 7237 -2224 1337 614 O
ATOM 1972 CG2 THR A1096 9.888 -1.098 -53.659 1.00 63.19 C
ANISOU 1972 CG2 THR A1096 7922 9345 6744 -2321 1423 478 C
ATOM 1973 N THR A1097 11.261 0.252 -49.644 1.00 68.72 N
ANISOU 1973 N THR A1097 8126 10685 7299 -1811 1226 611 N
ATOM 1974 CA THR A1097 11.966 0.374 -48.375 1.00 69.96 C
ANISOU 1974 CA THR A1097 8079 11141 7363 -1585 1251 663 C
ATOM 1975 C THR A1097 11.015 0.815 -47.270 1.00 71.78 C
ANISOU 1975 C THR A1097 8312 11232 7730 -1456 1107 607 C
ATOM 1976 O THR A1097 11.093 0.319 -46.141 1.00 71.39 O
ANISOU 1976 O THR A1097 8140 11307 7678 -1134 1252 651 O
ATOM 1977 CB THR A1097 13.131 1.356 -48.505 1.00 59.35 C
ANISOU 1977 CB THR A1097 6612 10100 5839 -1797 1071 673 C
ATOM 1978 OG1 THR A1097 12.665 2.594 -49.060 1.00 60.48 O
ANISOU 1978 OG1 THR A1097 6879 10066 6033 -2140 750 591 O
ATOM 1979 CG2 THR A1097 14.218 0.780 -49.395 1.00 62.09 C
ANISOU 1979 CG2 THR A1097 6916 10643 6032 -1857 1260 746 C
ATOM 1980 N ARG A1098 10.100 1.738 -47.582 1.00 70.66 N
ANISOU 1980 N ARG A1098 8312 10831 7703 -1692 827 515 N
ATOM 1981 CA ARG A1098 9.197 2.258 -46.561 1.00 66.98 C
ANISOU 1981 CA ARG A1098 7854 10231 7365 -1593 666 458 C
ATOM 1982 C ARG A1098 8.336 1.149 -45.975 1.00 71.89 C
ANISOU 1982 C ARG A1098 8509 10672 8133 -1276 905 466 C
ATOM 1983 O ARG A1098 8.081 1.123 -44.765 1.00 73.33 O
ANISOU 1983 O ARG A1098 8604 10898 8358 -1032 919 473 O
ATOM 1984 CB ARG A1098 8.322 3.367 -47.144 1.00 72.42 C
ANISOU 1984 CB ARG A1098 8712 10652 8152 -1902 347 364 C
ATOM 1985 CG ARG A1098 7.336 3.962 -46.147 1.00 64.65 C
ANISOU 1985 CG ARG A1098 7749 9510 7306 -1819 165 301 C
ATOM 1986 CD ARG A1098 5.915 3.478 -46.397 1.00 65.40 C
ANISOU 1986 CD ARG A1098 8014 9236 7597 -1771 198 240 C
ATOM 1987 NE ARG A1098 5.360 4.027 -47.629 1.00 69.74 N
ANISOU 1987 NE ARG A1098 8746 9568 8186 -2079 19 178 N
ATOM 1988 CZ ARG A1098 4.114 3.838 -48.043 1.00 68.09 C
ANISOU 1988 CZ ARG A1098 8692 9050 8131 -2108 -14 101 C
ATOM 1989 NH1 ARG A1098 3.255 3.110 -47.347 1.00 65.34 N
ANISOU 1989 NH1 ARG A1098 8350 8547 7931 -1865 124 68 N
ATOM 1990 NH2 ARG A1098 3.718 4.394 -49.185 1.00 57.90 N
ANISOU 1990 NH2 ARG A1098 7551 7608 6840 -2383 -184 52 N
ATOM 1991 N ASN A1099 7.873 0.223 -46.818 1.00 72.55 N
ANISOU 1991 N ASN A1099 8717 10552 8297 -1276 1104 457 N
ATOM 1992 CA ASN A1099 7.124 -0.920 -46.306 1.00 77.55 C
ANISOU 1992 CA ASN A1099 9380 11010 9074 -977 1381 460 C
ATOM 1993 C ASN A1099 7.979 -1.748 -45.357 1.00 76.40 C
ANISOU 1993 C ASN A1099 9061 11140 8829 -619 1669 578 C
ATOM 1994 O ASN A1099 7.500 -2.203 -44.311 1.00 68.29 O
ANISOU 1994 O ASN A1099 7995 10062 7889 -321 1800 597 O
ATOM 1995 CB ASN A1099 6.619 -1.777 -47.465 1.00 77.17 C
ANISOU 1995 CB ASN A1099 9480 10725 9114 -1066 1565 416 C
ATOM 1996 CG ASN A1099 5.483 -1.119 -48.221 1.00 69.48 C
ANISOU 1996 CG ASN A1099 8681 9450 8269 -1339 1311 288 C
ATOM 1997 OD1 ASN A1099 4.871 -0.167 -47.738 1.00 55.28 O
ANISOU 1997 OD1 ASN A1099 6908 7563 6534 -1408 1036 235 O
ATOM 1998 ND2 ASN A1099 5.188 -1.630 -49.411 1.00 77.00 N
ANISOU 1998 ND2 ASN A1099 9750 10250 9256 -1487 1406 234 N
ATOM 1999 N ALA A1100 9.251 -1.957 -45.706 1.00 86.10 N
ANISOU 1999 N ALA A1100 10182 12667 9867 -630 1777 662 N
ATOM 2000 CA ALA A1100 10.167 -2.606 -44.777 1.00 86.84 C
ANISOU 2000 CA ALA A1100 10090 13077 9830 -288 2019 779 C
ATOM 2001 C ALA A1100 10.567 -1.668 -43.647 1.00 92.86 C
ANISOU 2001 C ALA A1100 10686 14097 10498 -219 1798 781 C
ATOM 2002 O ALA A1100 10.841 -2.125 -42.532 1.00 99.19 O
ANISOU 2002 O ALA A1100 11351 15088 11251 130 1959 852 O
ATOM 2003 CB ALA A1100 11.409 -3.097 -45.520 1.00 93.45 C
ANISOU 2003 CB ALA A1100 10856 14167 10484 -325 2196 863 C
ATOM 2004 N TYR A1101 10.604 -0.359 -43.913 1.00 83.09 N
ANISOU 2004 N TYR A1101 9460 12875 9235 -540 1440 701 N
ATOM 2005 CA TYR A1101 10.967 0.600 -42.874 1.00 80.75 C
ANISOU 2005 CA TYR A1101 9006 12817 8859 -509 1221 677 C
ATOM 2006 C TYR A1101 9.899 0.669 -41.790 1.00 77.43 C
ANISOU 2006 C TYR A1101 8609 12216 8593 -303 1171 640 C
ATOM 2007 O TYR A1101 10.218 0.684 -40.596 1.00 78.98 O
ANISOU 2007 O TYR A1101 8640 12648 8720 -39 1199 672 O
ATOM 2008 CB TYR A1101 11.190 1.981 -43.494 1.00 80.00 C
ANISOU 2008 CB TYR A1101 8943 12731 8723 -923 874 593 C
ATOM 2009 CG TYR A1101 12.390 2.727 -42.949 1.00 85.90 C
ANISOU 2009 CG TYR A1101 9471 13892 9277 -961 756 591 C
ATOM 2010 CD1 TYR A1101 13.674 2.434 -43.392 1.00 83.40 C
ANISOU 2010 CD1 TYR A1101 9027 13892 8769 -987 887 651 C
ATOM 2011 CD2 TYR A1101 12.238 3.732 -42.003 1.00 93.27 C
ANISOU 2011 CD2 TYR A1101 10317 14903 10221 -980 516 517 C
ATOM 2012 CE1 TYR A1101 14.772 3.115 -42.900 1.00 80.60 C
ANISOU 2012 CE1 TYR A1101 8457 13930 8238 -1031 783 630 C
ATOM 2013 CE2 TYR A1101 13.330 4.419 -41.507 1.00 84.18 C
ANISOU 2013 CE2 TYR A1101 8950 14138 8895 -1028 414 490 C
ATOM 2014 CZ TYR A1101 14.593 4.107 -41.961 1.00 79.59 C
ANISOU 2014 CZ TYR A1101 8239 13875 8125 -1056 548 543 C
ATOM 2015 OH TYR A1101 15.681 4.788 -41.467 1.00 85.62 O
ANISOU 2015 OH TYR A1101 8775 15039 8716 -1110 451 498 O
ATOM 2016 N ILE A1102 8.625 0.709 -42.184 1.00 75.62 N
ANISOU 2016 N ILE A1102 8579 11585 8568 -412 1096 570 N
ATOM 2017 CA ILE A1102 7.552 0.819 -41.201 1.00 74.64 C
ANISOU 2017 CA ILE A1102 8488 11270 8601 -237 1035 528 C
ATOM 2018 C ILE A1102 7.420 -0.473 -40.404 1.00 78.60 C
ANISOU 2018 C ILE A1102 8938 11786 9141 195 1396 614 C
ATOM 2019 O ILE A1102 7.207 -0.447 -39.186 1.00 80.71 O
ANISOU 2019 O ILE A1102 9114 12127 9425 459 1405 632 O
ATOM 2020 CB ILE A1102 6.229 1.198 -41.895 1.00 74.52 C
ANISOU 2020 CB ILE A1102 8695 10832 8787 -474 862 423 C
ATOM 2021 CG1 ILE A1102 5.138 1.490 -40.859 1.00 75.69 C
ANISOU 2021 CG1 ILE A1102 8871 10794 9093 -324 754 370 C
ATOM 2022 CG2 ILE A1102 5.770 0.087 -42.831 1.00 76.10 C
ANISOU 2022 CG2 ILE A1102 9033 10797 9083 -465 1120 425 C
ATOM 2023 CD1 ILE A1102 5.429 2.689 -39.977 1.00 75.39 C
ANISOU 2023 CD1 ILE A1102 8715 10944 8984 -368 469 340 C
ATOM 2024 N GLN A1103 7.553 -1.623 -41.070 1.00 86.86 N
ANISOU 2024 N GLN A1103 10043 12761 10199 280 1711 671 N
ATOM 2025 CA GLN A1103 7.399 -2.900 -40.384 1.00 79.90 C
ANISOU 2025 CA GLN A1103 9135 11858 9367 689 2094 759 C
ATOM 2026 C GLN A1103 8.461 -3.108 -39.314 1.00 75.04 C
ANISOU 2026 C GLN A1103 8296 11660 8556 1017 2222 875 C
ATOM 2027 O GLN A1103 8.297 -3.979 -38.453 1.00 75.98 O
ANISOU 2027 O GLN A1103 8375 11790 8706 1404 2502 956 O
ATOM 2028 CB GLN A1103 7.449 -4.047 -41.394 1.00 79.98 C
ANISOU 2028 CB GLN A1103 9249 11726 9415 686 2413 791 C
ATOM 2029 N LYS A1104 9.546 -2.333 -39.350 1.00 71.04 N
ANISOU 2029 N LYS A1104 7640 11506 7847 877 2033 881 N
ATOM 2030 CA LYS A1104 10.609 -2.496 -38.366 1.00 71.39 C
ANISOU 2030 CA LYS A1104 7448 11993 7683 1181 2140 976 C
ATOM 2031 C LYS A1104 10.279 -1.776 -37.062 1.00 70.26 C
ANISOU 2031 C LYS A1104 7199 11948 7548 1328 1945 935 C
ATOM 2032 O LYS A1104 10.463 -2.337 -35.976 1.00 71.69 O
ANISOU 2032 O LYS A1104 7255 12316 7666 1732 2138 1020 O
ATOM 2033 CB LYS A1104 11.928 -1.979 -38.944 1.00 76.59 C
ANISOU 2033 CB LYS A1104 7975 13005 8120 965 2029 981 C
ATOM 2034 CG LYS A1104 13.173 -2.457 -38.208 1.00 81.55 C
ANISOU 2034 CG LYS A1104 8360 14117 8508 1291 2226 1092 C
ATOM 2035 CD LYS A1104 14.432 -1.772 -38.730 1.00 76.87 C
ANISOU 2035 CD LYS A1104 7624 13880 7705 1039 2069 1068 C
ATOM 2036 CE LYS A1104 14.562 -0.350 -38.199 1.00 77.79 C
ANISOU 2036 CE LYS A1104 7624 14156 7775 832 1689 945 C
ATOM 2037 NZ LYS A1104 15.709 0.385 -38.807 1.00 67.28 N
ANISOU 2037 NZ LYS A1104 6174 13122 6269 533 1534 898 N
ATOM 2038 N TYR A1105 9.777 -0.542 -37.150 1.00 78.19 N
ANISOU 2038 N TYR A1105 8256 12826 8629 1015 1572 809 N
ATOM 2039 CA TYR A1105 9.540 0.247 -35.945 1.00 62.01 C
ANISOU 2039 CA TYR A1105 6096 10890 6576 1119 1363 757 C
ATOM 2040 C TYR A1105 8.482 -0.398 -35.060 1.00 71.94 C
ANISOU 2040 C TYR A1105 7420 11917 7997 1454 1522 789 C
ATOM 2041 O TYR A1105 8.579 -0.349 -33.829 1.00 76.90 O
ANISOU 2041 O TYR A1105 7903 12750 8563 1750 1535 817 O
ATOM 2042 CB TYR A1105 9.126 1.668 -36.326 1.00 56.82 C
ANISOU 2042 CB TYR A1105 5514 10085 5989 700 954 617 C
ATOM 2043 N LEU A1106 7.464 -1.008 -35.671 1.00 68.42 N
ANISOU 2043 N LEU A1106 7187 11050 7757 1412 1649 778 N
ATOM 2044 CA LEU A1106 6.375 -1.591 -34.894 1.00 61.41 C
ANISOU 2044 CA LEU A1106 6378 9903 7050 1697 1801 792 C
ATOM 2045 C LEU A1106 6.893 -2.633 -33.911 1.00 58.27 C
ANISOU 2045 C LEU A1106 5844 9746 6549 2193 2158 936 C
ATOM 2046 O LEU A1106 6.457 -2.678 -32.754 1.00 57.07 O
ANISOU 2046 O LEU A1106 5640 9606 6437 2482 2187 958 O
ATOM 2047 CB LEU A1106 5.343 -2.211 -35.835 1.00 71.15 C
ANISOU 2047 CB LEU A1106 7845 10682 8505 1564 1929 749 C
ATOM 2048 CG LEU A1106 4.715 -1.254 -36.851 1.00 71.97 C
ANISOU 2048 CG LEU A1106 8102 10530 8715 1103 1595 612 C
ATOM 2049 CD1 LEU A1106 3.858 -2.018 -37.848 1.00 84.54 C
ANISOU 2049 CD1 LEU A1106 9893 11739 10489 997 1765 567 C
ATOM 2050 CD2 LEU A1106 3.895 -0.190 -36.143 1.00 64.25 C
ANISOU 2050 CD2 LEU A1106 7142 9435 7836 1029 1271 519 C
ATOM 2051 N ALA A 900 7.829 -3.476 -34.350 1.00 61.86 N
ANISOU 2051 N ALA A 900 8445 10644 4414 116 2105 -1323 N
ATOM 2052 CA ALA A 900 8.356 -4.516 -33.473 1.00 58.85 C
ANISOU 2052 CA ALA A 900 8178 10024 4158 308 2213 -1441 C
ATOM 2053 C ALA A 900 9.083 -3.918 -32.274 1.00 66.27 C
ANISOU 2053 C ALA A 900 8831 10913 5438 359 2223 -1308 C
ATOM 2054 O ALA A 900 8.962 -4.423 -31.152 1.00 65.96 O
ANISOU 2054 O ALA A 900 8799 10684 5580 421 2176 -1335 O
ATOM 2055 CB ALA A 900 9.287 -5.439 -34.258 1.00 74.14 C
ANISOU 2055 CB ALA A 900 10359 11919 5894 491 2471 -1609 C
ATOM 2056 N HIS A 270 9.845 -2.842 -32.488 1.00 73.38 N
ANISOU 2056 N HIS A 270 9469 11996 6418 331 2266 -1172 N
ATOM 2057 CA HIS A 270 10.607 -2.252 -31.391 1.00 69.46 C
ANISOU 2057 CA HIS A 270 8687 11478 6227 387 2245 -1062 C
ATOM 2058 C HIS A 270 9.686 -1.761 -30.281 1.00 66.59 C
ANISOU 2058 C HIS A 270 8186 11045 6070 278 1999 -956 C
ATOM 2059 O HIS A 270 9.971 -1.958 -29.094 1.00 64.20 O
ANISOU 2059 O HIS A 270 7808 10600 5985 358 1969 -947 O
ATOM 2060 CB HIS A 270 11.476 -1.106 -31.907 1.00 68.95 C
ANISOU 2060 CB HIS A 270 8375 11634 6189 365 2292 -928 C
ATOM 2061 CG HIS A 270 12.440 -0.575 -30.890 1.00 80.55 C
ANISOU 2061 CG HIS A 270 9581 13082 7942 452 2274 -836 C
ATOM 2062 ND1 HIS A 270 12.839 0.744 -30.859 1.00 83.01 N
ANISOU 2062 ND1 HIS A 270 9621 13557 8362 391 2176 -659 N
ATOM 2063 CD2 HIS A 270 13.089 -1.188 -29.872 1.00 76.11 C
ANISOU 2063 CD2 HIS A 270 8999 12352 7567 596 2326 -896 C
ATOM 2064 CE1 HIS A 270 13.689 0.922 -29.863 1.00 76.98 C
ANISOU 2064 CE1 HIS A 270 8695 12724 7830 497 2160 -617 C
ATOM 2065 NE2 HIS A 270 13.858 -0.235 -29.248 1.00 78.42 N
ANISOU 2065 NE2 HIS A 270 9017 12712 8067 619 2251 -757 N
ATOM 2066 N LEU A 271 8.578 -1.112 -30.646 1.00 64.05 N
ANISOU 2066 N LEU A 271 7827 10823 5685 88 1823 -875 N
ATOM 2067 CA LEU A 271 7.617 -0.676 -29.638 1.00 63.43 C
ANISOU 2067 CA LEU A 271 7628 10675 5798 -29 1603 -789 C
ATOM 2068 C LEU A 271 6.995 -1.869 -28.925 1.00 54.85 C
ANISOU 2068 C LEU A 271 6758 9356 4726 23 1595 -917 C
ATOM 2069 O LEU A 271 6.711 -1.807 -27.723 1.00 51.77 O
ANISOU 2069 O LEU A 271 6281 8846 4545 20 1495 -873 O
ATOM 2070 CB LEU A 271 6.537 0.192 -30.280 1.00 65.22 C
ANISOU 2070 CB LEU A 271 7776 11054 5953 -254 1430 -691 C
ATOM 2071 CG LEU A 271 6.908 1.664 -30.472 1.00 62.18 C
ANISOU 2071 CG LEU A 271 7104 10864 5657 -333 1338 -509 C
ATOM 2072 CD1 LEU A 271 8.201 1.809 -31.265 1.00 62.52 C
ANISOU 2072 CD1 LEU A 271 7126 11035 5594 -218 1528 -506 C
ATOM 2073 CD2 LEU A 271 5.771 2.406 -31.152 1.00 57.03 C
ANISOU 2073 CD2 LEU A 271 6397 10345 4926 -560 1168 -422 C
ATOM 2074 N ALA A 272 6.767 -2.964 -29.651 1.00 55.34 N
ANISOU 2074 N ALA A 272 7118 9354 4556 74 1687 -1080 N
ATOM 2075 CA ALA A 272 6.316 -4.186 -28.997 1.00 65.20 C
ANISOU 2075 CA ALA A 272 8577 10395 5801 147 1678 -1225 C
ATOM 2076 C ALA A 272 7.330 -4.642 -27.958 1.00 60.89 C
ANISOU 2076 C ALA A 272 8020 9665 5451 343 1798 -1229 C
ATOM 2077 O ALA A 272 6.957 -5.081 -26.865 1.00 64.09 O
ANISOU 2077 O ALA A 272 8452 9903 5996 369 1728 -1240 O
ATOM 2078 CB ALA A 272 6.073 -5.282 -30.035 1.00 66.75 C
ANISOU 2078 CB ALA A 272 9090 10573 5697 190 1746 -1426 C
ATOM 2079 N ALA A 273 8.621 -4.534 -28.278 1.00 56.80 N
ANISOU 2079 N ALA A 273 7428 9211 4942 461 1974 -1235 N
ATOM 2080 CA ALA A 273 9.653 -4.832 -27.291 1.00 51.64 C
ANISOU 2080 CA ALA A 273 6688 8435 4499 611 2068 -1243 C
ATOM 2081 C ALA A 273 9.643 -3.809 -26.164 1.00 47.73 C
ANISOU 2081 C ALA A 273 5901 7970 4264 550 1906 -1073 C
ATOM 2082 O ALA A 273 9.858 -4.159 -24.998 1.00 55.29 O
ANISOU 2082 O ALA A 273 6836 8771 5400 624 1884 -1072 O
ATOM 2083 CB ALA A 273 11.024 -4.872 -27.961 1.00 54.78 C
ANISOU 2083 CB ALA A 273 7035 8920 4860 731 2283 -1293 C
ATOM 2084 N THR A 274 9.407 -2.538 -26.492 1.00 52.01 N
ANISOU 2084 N THR A 274 6232 8706 4825 416 1783 -930 N
ATOM 2085 CA THR A 274 9.349 -1.514 -25.456 1.00 57.57 C
ANISOU 2085 CA THR A 274 6689 9430 5756 357 1605 -776 C
ATOM 2086 C THR A 274 8.148 -1.719 -24.542 1.00 49.81 C
ANISOU 2086 C THR A 274 5763 8307 4854 268 1456 -766 C
ATOM 2087 O THR A 274 8.276 -1.635 -23.315 1.00 46.75 O
ANISOU 2087 O THR A 274 5303 7808 4653 308 1385 -718 O
ATOM 2088 CB THR A 274 9.304 -0.125 -26.091 1.00 53.47 C
ANISOU 2088 CB THR A 274 5962 9135 5219 230 1496 -634 C
ATOM 2089 OG1 THR A 274 10.526 0.123 -26.797 1.00 59.90 O
ANISOU 2089 OG1 THR A 274 6702 10076 5982 323 1640 -626 O
ATOM 2090 CG2 THR A 274 9.115 0.940 -25.026 1.00 48.55 C
ANISOU 2090 CG2 THR A 274 5140 8506 4799 168 1284 -487 C
ATOM 2091 N ARG A 275 6.974 -1.994 -25.115 1.00 48.52 N
ANISOU 2091 N ARG A 275 5736 8149 4550 142 1405 -814 N
ATOM 2092 CA ARG A 275 5.781 -2.159 -24.292 1.00 48.38 C
ANISOU 2092 CA ARG A 275 5757 8010 4614 40 1267 -806 C
ATOM 2093 C ARG A 275 5.937 -3.331 -23.334 1.00 47.07 C
ANISOU 2093 C ARG A 275 5768 7611 4505 185 1339 -897 C
ATOM 2094 O ARG A 275 5.617 -3.224 -22.145 1.00 51.92 O
ANISOU 2094 O ARG A 275 6322 8119 5287 170 1252 -842 O
ATOM 2095 CB ARG A 275 4.550 -2.355 -25.174 1.00 57.15 C
ANISOU 2095 CB ARG A 275 6989 9176 5550 -126 1200 -862 C
ATOM 2096 CG ARG A 275 4.070 -1.091 -25.856 1.00 56.10 C
ANISOU 2096 CG ARG A 275 6661 9247 5409 -315 1075 -741 C
ATOM 2097 CD ARG A 275 2.618 -1.221 -26.282 1.00 53.99 C
ANISOU 2097 CD ARG A 275 6437 9045 5034 -550 954 -795 C
ATOM 2098 NE ARG A 275 2.135 -0.011 -26.936 1.00 62.01 N
ANISOU 2098 NE ARG A 275 7261 10256 6044 -740 825 -669 N
ATOM 2099 CZ ARG A 275 2.235 0.233 -28.235 1.00 58.67 C
ANISOU 2099 CZ ARG A 275 6859 10009 5423 -799 853 -666 C
ATOM 2100 NH1 ARG A 275 2.798 -0.634 -29.061 1.00 60.76 N
ANISOU 2100 NH1 ARG A 275 7342 10279 5467 -681 1009 -793 N
ATOM 2101 NH2 ARG A 275 1.760 1.378 -28.718 1.00 62.38 N
ANISOU 2101 NH2 ARG A 275 7143 10648 5910 -975 715 -533 N
ATOM 2102 N LYS A 276 6.432 -4.462 -23.836 1.00 40.33 N
ANISOU 2102 N LYS A 276 5148 6669 3505 328 1495 -1039 N
ATOM 2103 CA LYS A 276 6.644 -5.609 -22.963 1.00 43.01 C
ANISOU 2103 CA LYS A 276 5671 6775 3895 476 1560 -1127 C
ATOM 2104 C LYS A 276 7.673 -5.287 -21.887 1.00 45.62 C
ANISOU 2104 C LYS A 276 5821 7059 4454 569 1594 -1050 C
ATOM 2105 O LYS A 276 7.483 -5.627 -20.714 1.00 49.33 O
ANISOU 2105 O LYS A 276 6320 7371 5053 601 1548 -1033 O
ATOM 2106 CB LYS A 276 7.077 -6.821 -23.786 1.00 52.35 C
ANISOU 2106 CB LYS A 276 7135 7874 4883 615 1717 -1304 C
ATOM 2107 CG LYS A 276 6.035 -7.292 -24.801 1.00 63.10 C
ANISOU 2107 CG LYS A 276 8680 9301 5993 527 1641 -1434 C
ATOM 2108 CD LYS A 276 4.692 -7.618 -24.150 1.00 63.61 C
ANISOU 2108 CD LYS A 276 8793 9286 6090 407 1455 -1472 C
ATOM 2109 CE LYS A 276 3.697 -6.471 -24.291 1.00 68.84 C
ANISOU 2109 CE LYS A 276 9240 10116 6801 138 1307 -1359 C
ATOM 2110 NZ LYS A 276 2.370 -6.795 -23.690 1.00 63.89 N
ANISOU 2110 NZ LYS A 276 8653 9393 6230 -33 1160 -1407 N
ATOM 2111 N GLY A 277 8.760 -4.611 -22.264 1.00 43.40 N
ANISOU 2111 N GLY A 277 5349 6923 4219 609 1654 -1004 N
ATOM 2112 CA GLY A 277 9.744 -4.210 -21.273 1.00 44.56 C
ANISOU 2112 CA GLY A 277 5303 7052 4578 690 1636 -931 C
ATOM 2113 C GLY A 277 9.155 -3.295 -20.219 1.00 42.38 C
ANISOU 2113 C GLY A 277 4874 6778 4452 589 1437 -788 C
ATOM 2114 O GLY A 277 9.450 -3.429 -19.029 1.00 46.06 O
ANISOU 2114 O GLY A 277 5309 7126 5068 647 1397 -760 O
ATOM 2115 N VAL A 278 8.319 -2.346 -20.642 1.00 42.31 N
ANISOU 2115 N VAL A 278 4771 6901 4403 429 1307 -702 N
ATOM 2116 CA VAL A 278 7.618 -1.501 -19.683 1.00 44.63 C
ANISOU 2116 CA VAL A 278 4950 7179 4828 318 1118 -588 C
ATOM 2117 C VAL A 278 6.556 -2.306 -18.949 1.00 37.01 C
ANISOU 2117 C VAL A 278 4142 6038 3881 281 1100 -636 C
ATOM 2118 O VAL A 278 6.361 -2.143 -17.739 1.00 31.89 O
ANISOU 2118 O VAL A 278 3462 5288 3367 276 1020 -580 O
ATOM 2119 CB VAL A 278 7.014 -0.278 -20.394 1.00 47.06 C
ANISOU 2119 CB VAL A 278 5122 7667 5091 153 980 -498 C
ATOM 2120 CG1 VAL A 278 6.181 0.534 -19.428 1.00 48.22 C
ANISOU 2120 CG1 VAL A 278 5202 7768 5352 38 788 -406 C
ATOM 2121 CG2 VAL A 278 8.114 0.581 -20.991 1.00 52.33 C
ANISOU 2121 CG2 VAL A 278 5643 8498 5741 201 989 -429 C
ATOM 2122 N ARG A 279 5.858 -3.191 -19.664 1.00 42.57 N
ANISOU 2122 N ARG A 279 5041 6704 4431 258 1169 -744 N
ATOM 2123 CA ARG A 279 4.842 -4.016 -19.021 1.00 37.83 C
ANISOU 2123 CA ARG A 279 4614 5939 3823 232 1138 -797 C
ATOM 2124 C ARG A 279 5.450 -4.879 -17.928 1.00 33.23 C
ANISOU 2124 C ARG A 279 4147 5160 3317 404 1212 -825 C
ATOM 2125 O ARG A 279 4.873 -5.023 -16.844 1.00 31.84 O
ANISOU 2125 O ARG A 279 3998 4872 3228 385 1142 -790 O
ATOM 2126 CB ARG A 279 4.146 -4.898 -20.055 1.00 40.65 C
ANISOU 2126 CB ARG A 279 5182 6297 3965 196 1170 -942 C
ATOM 2127 CG ARG A 279 2.898 -4.294 -20.661 1.00 45.05 C
ANISOU 2127 CG ARG A 279 5650 6994 4473 -61 1047 -940 C
ATOM 2128 CD ARG A 279 1.826 -4.097 -19.607 1.00 48.64 C
ANISOU 2128 CD ARG A 279 6040 7370 5070 -216 933 -904 C
ATOM 2129 NE ARG A 279 1.706 -2.701 -19.205 1.00 51.59 N
ANISOU 2129 NE ARG A 279 6173 7821 5608 -312 821 -732 N
ATOM 2130 CZ ARG A 279 1.108 -2.289 -18.097 1.00 48.00 C
ANISOU 2130 CZ ARG A 279 5649 7275 5314 -387 727 -660 C
ATOM 2131 NH1 ARG A 279 0.601 -3.145 -17.225 1.00 42.57 N
ANISOU 2131 NH1 ARG A 279 5077 6441 4658 -400 755 -734 N
ATOM 2132 NH2 ARG A 279 1.017 -0.984 -17.856 1.00 48.12 N
ANISOU 2132 NH2 ARG A 279 5497 7361 5426 -460 588 -547 N
ATOM 2133 N THR A 280 6.612 -5.472 -18.198 1.00 45.22 N
ANISOU 2133 N THR A 280 5735 6634 4814 558 1358 -896 N
ATOM 2134 CA THR A 280 7.289 -6.249 -17.167 1.00 62.21 C
ANISOU 2134 CA THR A 280 7965 8594 7077 685 1432 -935 C
ATOM 2135 C THR A 280 7.665 -5.363 -15.988 1.00 41.97 C
ANISOU 2135 C THR A 280 5175 6055 4716 663 1330 -809 C
ATOM 2136 O THR A 280 7.545 -5.774 -14.828 1.00 42.59 O
ANISOU 2136 O THR A 280 5310 5979 4892 686 1308 -801 O
ATOM 2137 CB THR A 280 8.527 -6.930 -17.747 1.00 46.10 C
ANISOU 2137 CB THR A 280 5952 6533 5029 799 1587 -1061 C
ATOM 2138 OG1 THR A 280 8.144 -7.776 -18.838 1.00 49.06 O
ANISOU 2138 OG1 THR A 280 6566 6870 5206 810 1652 -1178 O
ATOM 2139 CG2 THR A 280 9.218 -7.766 -16.687 1.00 46.48 C
ANISOU 2139 CG2 THR A 280 6001 6413 5244 874 1606 -1140 C
ATOM 2140 N LEU A 281 8.112 -4.139 -16.264 1.00 27.35 N
ANISOU 2140 N LEU A 281 3089 4392 2912 615 1248 -711 N
ATOM 2141 CA LEU A 281 8.380 -3.202 -15.181 1.00 31.30 C
ANISOU 2141 CA LEU A 281 3419 4913 3562 590 1111 -590 C
ATOM 2142 C LEU A 281 7.122 -2.955 -14.362 1.00 28.18 C
ANISOU 2142 C LEU A 281 3062 4441 3206 472 1004 -528 C
ATOM 2143 O LEU A 281 7.179 -2.857 -13.131 1.00 24.43 O
ANISOU 2143 O LEU A 281 2573 3872 2838 487 948 -479 O
ATOM 2144 CB LEU A 281 8.920 -1.892 -15.752 1.00 35.64 C
ANISOU 2144 CB LEU A 281 3772 5660 4108 547 1023 -498 C
ATOM 2145 CG LEU A 281 9.300 -0.802 -14.752 1.00 26.65 C
ANISOU 2145 CG LEU A 281 2510 4542 3074 527 872 -376 C
ATOM 2146 CD1 LEU A 281 10.459 -1.248 -13.883 1.00 29.41 C
ANISOU 2146 CD1 LEU A 281 2844 4817 3515 672 907 -391 C
ATOM 2147 CD2 LEU A 281 9.647 0.473 -15.498 1.00 31.48 C
ANISOU 2147 CD2 LEU A 281 2993 5333 3636 471 794 -291 C
ATOM 2148 N ALA A 282 5.972 -2.861 -15.029 1.00 30.63 N
ANISOU 2148 N ALA A 282 3413 4800 3427 348 970 -538 N
ATOM 2149 CA ALA A 282 4.721 -2.648 -14.314 1.00 22.60 C
ANISOU 2149 CA ALA A 282 2410 3723 2454 221 866 -495 C
ATOM 2150 C ALA A 282 4.429 -3.810 -13.377 1.00 24.44 C
ANISOU 2150 C ALA A 282 2830 3771 2684 314 928 -538 C
ATOM 2151 O ALA A 282 4.077 -3.612 -12.209 1.00 22.17 O
ANISOU 2151 O ALA A 282 2525 3409 2488 290 864 -476 O
ATOM 2152 CB ALA A 282 3.579 -2.464 -15.310 1.00 27.67 C
ANISOU 2152 CB ALA A 282 3051 4456 3005 51 817 -531 C
ATOM 2153 N VAL A 283 4.590 -5.038 -13.871 1.00 28.45 N
ANISOU 2153 N VAL A 283 3547 4200 3064 437 1035 -652 N
ATOM 2154 CA VAL A 283 4.271 -6.208 -13.059 1.00 27.04 C
ANISOU 2154 CA VAL A 283 3570 3864 2841 550 1011 -712 C
ATOM 2155 C VAL A 283 5.165 -6.260 -11.831 1.00 30.85 C
ANISOU 2155 C VAL A 283 4037 4222 3464 638 1021 -629 C
ATOM 2156 O VAL A 283 4.702 -6.534 -10.718 1.00 29.79 O
ANISOU 2156 O VAL A 283 3914 4083 3323 687 882 -624 O
ATOM 2157 CB VAL A 283 4.396 -7.489 -13.902 1.00 31.05 C
ANISOU 2157 CB VAL A 283 4278 4326 3193 661 1043 -886 C
ATOM 2158 CG1 VAL A 283 4.479 -8.705 -13.000 1.00 30.03 C
ANISOU 2158 CG1 VAL A 283 4210 4123 3079 795 921 -1033 C
ATOM 2159 CG2 VAL A 283 3.219 -7.605 -14.859 1.00 48.31 C
ANISOU 2159 CG2 VAL A 283 6508 6579 5269 478 1020 -1021 C
ATOM 2160 N VAL A 284 6.459 -5.999 -12.011 1.00 35.96 N
ANISOU 2160 N VAL A 284 4552 4863 4246 623 1130 -673 N
ATOM 2161 CA VAL A 284 7.393 -6.077 -10.894 1.00 29.32 C
ANISOU 2161 CA VAL A 284 3584 3981 3576 655 1101 -723 C
ATOM 2162 C VAL A 284 7.015 -5.078 -9.812 1.00 32.53 C
ANISOU 2162 C VAL A 284 3893 4407 4062 593 987 -579 C
ATOM 2163 O VAL A 284 7.007 -5.404 -8.619 1.00 31.69 O
ANISOU 2163 O VAL A 284 3785 4223 4033 589 921 -620 O
ATOM 2164 CB VAL A 284 8.830 -5.852 -11.392 1.00 27.06 C
ANISOU 2164 CB VAL A 284 3148 3817 3318 796 1145 -751 C
ATOM 2165 CG1 VAL A 284 9.782 -5.744 -10.220 1.00 42.31 C
ANISOU 2165 CG1 VAL A 284 4974 5736 5365 909 1055 -711 C
ATOM 2166 CG2 VAL A 284 9.240 -6.976 -12.318 1.00 35.43 C
ANISOU 2166 CG2 VAL A 284 4317 4836 4310 872 1266 -917 C
ATOM 2167 N LEU A 285 6.696 -3.845 -10.208 1.00 35.42 N
ANISOU 2167 N LEU A 285 4137 4913 4408 532 930 -458 N
ATOM 2168 CA LEU A 285 6.328 -2.835 -9.224 1.00 27.67 C
ANISOU 2168 CA LEU A 285 3064 3946 3503 452 807 -347 C
ATOM 2169 C LEU A 285 5.079 -3.247 -8.459 1.00 21.10 C
ANISOU 2169 C LEU A 285 2370 3013 2634 414 779 -295 C
ATOM 2170 O LEU A 285 5.015 -3.098 -7.234 1.00 26.60 O
ANISOU 2170 O LEU A 285 3080 3635 3391 408 727 -239 O
ATOM 2171 CB LEU A 285 6.112 -1.490 -9.915 1.00 33.49 C
ANISOU 2171 CB LEU A 285 3667 4845 4213 344 687 -276 C
ATOM 2172 CG LEU A 285 7.350 -0.882 -10.570 1.00 23.33 C
ANISOU 2172 CG LEU A 285 2264 3696 2905 403 663 -266 C
ATOM 2173 CD1 LEU A 285 6.961 0.263 -11.478 1.00 25.80 C
ANISOU 2173 CD1 LEU A 285 2503 4147 3152 295 574 -217 C
ATOM 2174 CD2 LEU A 285 8.316 -0.410 -9.505 1.00 28.12 C
ANISOU 2174 CD2 LEU A 285 2820 4289 3575 467 596 -215 C
ATOM 2175 N GLY A 286 4.078 -3.775 -9.164 1.00 29.45 N
ANISOU 2175 N GLY A 286 3504 4125 3561 394 785 -350 N
ATOM 2176 CA GLY A 286 2.852 -4.174 -8.496 1.00 28.76 C
ANISOU 2176 CA GLY A 286 3478 3993 3457 292 725 -402 C
ATOM 2177 C GLY A 286 3.080 -5.266 -7.472 1.00 27.30 C
ANISOU 2177 C GLY A 286 3419 3710 3245 418 706 -499 C
ATOM 2178 O GLY A 286 2.536 -5.220 -6.367 1.00 39.11 O
ANISOU 2178 O GLY A 286 4945 5097 4819 326 681 -470 O
ATOM 2179 N THR A 287 3.891 -6.263 -7.822 1.00 30.11 N
ANISOU 2179 N THR A 287 3834 4059 3548 566 694 -634 N
ATOM 2180 CA THR A 287 4.181 -7.336 -6.879 1.00 32.58 C
ANISOU 2180 CA THR A 287 4246 4186 3947 617 699 -767 C
ATOM 2181 C THR A 287 4.959 -6.817 -5.680 1.00 33.85 C
ANISOU 2181 C THR A 287 4302 4329 4233 637 665 -697 C
ATOM 2182 O THR A 287 4.685 -7.209 -4.539 1.00 39.31 O
ANISOU 2182 O THR A 287 5121 4853 4962 648 653 -647 O
ATOM 2183 CB THR A 287 4.965 -8.451 -7.568 1.00 39.74 C
ANISOU 2183 CB THR A 287 5206 5028 4865 713 751 -933 C
ATOM 2184 OG1 THR A 287 6.224 -7.945 -8.029 1.00 44.57 O
ANISOU 2184 OG1 THR A 287 5639 5729 5568 710 815 -935 O
ATOM 2185 CG2 THR A 287 4.179 -9.011 -8.747 1.00 54.32 C
ANISOU 2185 CG2 THR A 287 7196 6869 6574 693 784 -1022 C
ATOM 2186 N PHE A 288 5.932 -5.936 -5.917 1.00 35.07 N
ANISOU 2186 N PHE A 288 4279 4575 4472 608 684 -652 N
ATOM 2187 CA PHE A 288 6.769 -5.450 -4.826 1.00 35.32 C
ANISOU 2187 CA PHE A 288 4261 4557 4601 679 665 -553 C
ATOM 2188 C PHE A 288 5.924 -4.776 -3.753 1.00 38.55 C
ANISOU 2188 C PHE A 288 4673 4977 4996 594 584 -467 C
ATOM 2189 O PHE A 288 6.019 -5.112 -2.566 1.00 39.01 O
ANISOU 2189 O PHE A 288 4828 4922 5073 657 556 -416 O
ATOM 2190 CB PHE A 288 7.831 -4.492 -5.368 1.00 25.66 C
ANISOU 2190 CB PHE A 288 2893 3431 3427 704 685 -465 C
ATOM 2191 CG PHE A 288 8.893 -4.137 -4.365 1.00 27.51 C
ANISOU 2191 CG PHE A 288 3082 3673 3699 812 601 -371 C
ATOM 2192 CD1 PHE A 288 9.873 -5.056 -4.021 1.00 48.30 C
ANISOU 2192 CD1 PHE A 288 5763 6234 6353 987 603 -402 C
ATOM 2193 CD2 PHE A 288 8.911 -2.892 -3.763 1.00 24.80 C
ANISOU 2193 CD2 PHE A 288 2658 3398 3365 734 516 -261 C
ATOM 2194 CE1 PHE A 288 10.851 -4.736 -3.097 1.00 40.02 C
ANISOU 2194 CE1 PHE A 288 4670 5196 5341 1076 526 -323 C
ATOM 2195 CE2 PHE A 288 9.886 -2.568 -2.839 1.00 24.00 C
ANISOU 2195 CE2 PHE A 288 2525 3308 3285 816 445 -198 C
ATOM 2196 CZ PHE A 288 10.857 -3.490 -2.506 1.00 32.76 C
ANISOU 2196 CZ PHE A 288 3668 4359 4421 985 450 -227 C
ATOM 2197 N GLY A 289 5.072 -3.832 -4.158 1.00 23.80 N
ANISOU 2197 N GLY A 289 2733 3241 3068 457 535 -406 N
ATOM 2198 CA GLY A 289 4.197 -3.183 -3.197 1.00 28.60 C
ANISOU 2198 CA GLY A 289 3364 3835 3667 387 507 -291 C
ATOM 2199 C GLY A 289 3.190 -4.139 -2.590 1.00 35.05 C
ANISOU 2199 C GLY A 289 4377 4451 4489 343 572 -291 C
ATOM 2200 O GLY A 289 2.978 -4.136 -1.375 1.00 37.43 O
ANISOU 2200 O GLY A 289 4751 4645 4828 323 571 -237 O
ATOM 2201 N ALA A 290 2.564 -4.974 -3.423 1.00 37.92 N
ANISOU 2201 N ALA A 290 4847 4749 4811 309 629 -361 N
ATOM 2202 CA ALA A 290 1.553 -5.902 -2.933 1.00 43.68 C
ANISOU 2202 CA ALA A 290 5801 5232 5564 202 723 -374 C
ATOM 2203 C ALA A 290 2.122 -6.903 -1.939 1.00 26.96 C
ANISOU 2203 C ALA A 290 3857 2950 3436 338 716 -381 C
ATOM 2204 O ALA A 290 1.356 -7.500 -1.177 1.00 38.71 O
ANISOU 2204 O ALA A 290 5526 4262 4920 252 761 -341 O
ATOM 2205 CB ALA A 290 0.914 -6.644 -4.107 1.00 41.87 C
ANISOU 2205 CB ALA A 290 5672 4946 5291 122 781 -470 C
ATOM 2206 N CYS A 291 3.441 -7.102 -1.932 1.00 47.20 N
ANISOU 2206 N CYS A 291 6357 5573 6005 527 654 -425 N
ATOM 2207 CA CYS A 291 4.078 -8.048 -1.029 1.00 53.38 C
ANISOU 2207 CA CYS A 291 7290 6192 6800 654 634 -416 C
ATOM 2208 C CYS A 291 4.797 -7.391 0.137 1.00 54.72 C
ANISOU 2208 C CYS A 291 7382 6404 7006 717 572 -325 C
ATOM 2209 O CYS A 291 5.073 -8.072 1.128 1.00 60.62 O
ANISOU 2209 O CYS A 291 8282 7008 7742 793 551 -280 O
ATOM 2210 CB CYS A 291 5.089 -8.918 -1.792 1.00 46.43 C
ANISOU 2210 CB CYS A 291 6410 5294 5936 807 631 -525 C
ATOM 2211 SG CYS A 291 4.370 -10.010 -3.034 1.00 70.82 S
ANISOU 2211 SG CYS A 291 9650 8288 8970 763 691 -657 S
ATOM 2212 N TRP A 292 5.111 -6.097 0.048 1.00 34.27 N
ANISOU 2212 N TRP A 292 4565 4004 4452 675 526 -299 N
ATOM 2213 CA TRP A 292 5.816 -5.406 1.115 1.00 29.89 C
ANISOU 2213 CA TRP A 292 3945 3485 3926 722 466 -215 C
ATOM 2214 C TRP A 292 4.948 -4.412 1.867 1.00 23.78 C
ANISOU 2214 C TRP A 292 3143 2751 3142 589 464 -137 C
ATOM 2215 O TRP A 292 5.237 -4.130 3.033 1.00 23.83 O
ANISOU 2215 O TRP A 292 3178 2730 3147 619 424 -76 O
ATOM 2216 CB TRP A 292 7.041 -4.664 0.557 1.00 32.16 C
ANISOU 2216 CB TRP A 292 4038 3921 4260 782 430 -211 C
ATOM 2217 CG TRP A 292 8.290 -5.484 0.550 1.00 28.56 C
ANISOU 2217 CG TRP A 292 3612 3409 3831 956 416 -230 C
ATOM 2218 CD1 TRP A 292 8.936 -5.984 -0.541 1.00 37.41 C
ANISOU 2218 CD1 TRP A 292 4691 4551 4971 1034 460 -301 C
ATOM 2219 CD2 TRP A 292 9.048 -5.903 1.692 1.00 28.14 C
ANISOU 2219 CD2 TRP A 292 3635 3269 3788 1077 354 -178 C
ATOM 2220 NE1 TRP A 292 10.048 -6.689 -0.152 1.00 39.34 N
ANISOU 2220 NE1 TRP A 292 4974 4725 5249 1201 430 -296 N
ATOM 2221 CE2 TRP A 292 10.140 -6.654 1.214 1.00 35.62 C
ANISOU 2221 CE2 TRP A 292 4573 4187 4773 1228 357 -219 C
ATOM 2222 CE3 TRP A 292 8.909 -5.716 3.071 1.00 27.29 C
ANISOU 2222 CE3 TRP A 292 3605 3107 3659 1072 296 -104 C
ATOM 2223 CZ2 TRP A 292 11.086 -7.218 2.066 1.00 39.03 C
ANISOU 2223 CZ2 TRP A 292 5060 4534 5234 1373 292 -183 C
ATOM 2224 CZ3 TRP A 292 9.849 -6.276 3.913 1.00 34.09 C
ANISOU 2224 CZ3 TRP A 292 4532 3889 4531 1211 228 -69 C
ATOM 2225 CH2 TRP A 292 10.924 -7.018 3.408 1.00 37.18 C
ANISOU 2225 CH2 TRP A 292 4904 4251 4974 1359 221 -106 C
ATOM 2226 N LEU A 293 3.887 -3.901 1.250 1.00 26.00 N
ANISOU 2226 N LEU A 293 3376 3085 3417 439 508 -133 N
ATOM 2227 CA LEU A 293 3.089 -2.851 1.867 1.00 27.56 C
ANISOU 2227 CA LEU A 293 3523 3306 3642 295 511 -50 C
ATOM 2228 C LEU A 293 2.377 -3.346 3.122 1.00 21.94 C
ANISOU 2228 C LEU A 293 3002 2421 2914 254 597 3 C
ATOM 2229 O LEU A 293 2.388 -2.644 4.140 1.00 26.93 O
ANISOU 2229 O LEU A 293 3611 3068 3555 235 578 61 O
ATOM 2230 CB LEU A 293 2.089 -2.281 0.860 1.00 28.93 C
ANISOU 2230 CB LEU A 293 3624 3509 3858 133 521 -54 C
ATOM 2231 CG LEU A 293 2.706 -1.215 -0.053 1.00 26.41 C
ANISOU 2231 CG LEU A 293 3139 3363 3531 143 428 -54 C
ATOM 2232 CD1 LEU A 293 1.830 -0.945 -1.263 1.00 18.13 C
ANISOU 2232 CD1 LEU A 293 2066 2333 2490 37 421 -80 C
ATOM 2233 CD2 LEU A 293 2.949 0.081 0.719 1.00 21.93 C
ANISOU 2233 CD2 LEU A 293 2519 2829 2983 118 344 -1 C
ATOM 2234 N PRO A 294 1.761 -4.534 3.109 1.00 21.16 N
ANISOU 2234 N PRO A 294 3114 2161 2765 226 693 -15 N
ATOM 2235 CA PRO A 294 1.103 -5.016 4.338 1.00 16.23 C
ANISOU 2235 CA PRO A 294 2679 1423 2066 171 756 27 C
ATOM 2236 C PRO A 294 2.021 -4.997 5.544 1.00 18.79 C
ANISOU 2236 C PRO A 294 3066 1726 2346 316 671 66 C
ATOM 2237 O PRO A 294 1.598 -4.600 6.636 1.00 17.99 O
ANISOU 2237 O PRO A 294 3009 1623 2204 259 696 101 O
ATOM 2238 CB PRO A 294 0.676 -6.443 3.965 1.00 14.13 C
ANISOU 2238 CB PRO A 294 2603 1020 1747 159 780 -19 C
ATOM 2239 CG PRO A 294 0.497 -6.403 2.489 1.00 12.42 C
ANISOU 2239 CG PRO A 294 2288 849 1584 111 802 -80 C
ATOM 2240 CD PRO A 294 1.527 -5.437 1.969 1.00 25.59 C
ANISOU 2240 CD PRO A 294 3740 2671 3312 218 723 -90 C
ATOM 2241 N PHE A 295 3.281 -5.395 5.373 1.00 21.07 N
ANISOU 2241 N PHE A 295 3340 2020 2645 499 569 44 N
ATOM 2242 CA PHE A 295 4.229 -5.270 6.469 1.00 20.16 C
ANISOU 2242 CA PHE A 295 3247 1906 2508 625 473 83 C
ATOM 2243 C PHE A 295 4.550 -3.811 6.742 1.00 22.49 C
ANISOU 2243 C PHE A 295 3328 2363 2854 603 425 105 C
ATOM 2244 O PHE A 295 4.724 -3.419 7.901 1.00 25.40 O
ANISOU 2244 O PHE A 295 3740 2723 3186 623 385 148 O
ATOM 2245 CB PHE A 295 5.507 -6.039 6.152 1.00 23.79 C
ANISOU 2245 CB PHE A 295 3700 2344 2996 800 386 50 C
ATOM 2246 CG PHE A 295 6.548 -5.934 7.221 1.00 18.80 C
ANISOU 2246 CG PHE A 295 3070 1715 2359 916 278 95 C
ATOM 2247 CD1 PHE A 295 6.448 -6.689 8.376 1.00 19.10 C
ANISOU 2247 CD1 PHE A 295 3340 1609 2310 952 256 146 C
ATOM 2248 CD2 PHE A 295 7.622 -5.079 7.075 1.00 22.89 C
ANISOU 2248 CD2 PHE A 295 3356 2377 2963 961 194 87 C
ATOM 2249 CE1 PHE A 295 7.401 -6.592 9.365 1.00 21.72 C
ANISOU 2249 CE1 PHE A 295 3677 1943 2634 1054 146 190 C
ATOM 2250 CE2 PHE A 295 8.580 -4.978 8.061 1.00 30.72 C
ANISOU 2250 CE2 PHE A 295 4356 3367 3950 1058 96 133 C
ATOM 2251 CZ PHE A 295 8.469 -5.736 9.208 1.00 30.90 C
ANISOU 2251 CZ PHE A 295 4601 3248 3892 1105 63 183 C
ATOM 2252 N ALA A 296 4.615 -2.991 5.691 1.00 18.02 N
ANISOU 2252 N ALA A 296 2536 1945 2364 544 410 69 N
ATOM 2253 CA ALA A 296 4.927 -1.581 5.876 1.00 18.32 C
ANISOU 2253 CA ALA A 296 2380 2134 2445 491 346 88 C
ATOM 2254 C ALA A 296 3.899 -0.893 6.760 1.00 16.27 C
ANISOU 2254 C ALA A 296 2152 1850 2179 370 402 137 C
ATOM 2255 O ALA A 296 4.234 0.054 7.478 1.00 19.07 O
ANISOU 2255 O ALA A 296 2430 2272 2543 363 343 158 O
ATOM 2256 CB ALA A 296 5.011 -0.883 4.520 1.00 21.58 C
ANISOU 2256 CB ALA A 296 2627 2672 2899 418 334 67 C
ATOM 2257 N ILE A 297 2.652 -1.347 6.722 1.00 15.28 N
ANISOU 2257 N ILE A 297 2153 1606 2047 258 551 165 N
ATOM 2258 CA ILE A 297 1.608 -0.767 7.560 1.00 17.90 C
ANISOU 2258 CA ILE A 297 2487 1922 2395 131 548 144 C
ATOM 2259 C ILE A 297 1.564 -1.436 8.926 1.00 25.31 C
ANISOU 2259 C ILE A 297 3661 2769 3188 202 662 142 C
ATOM 2260 O ILE A 297 1.472 -0.761 9.954 1.00 24.69 O
ANISOU 2260 O ILE A 297 3586 2696 3098 197 643 136 O
ATOM 2261 CB ILE A 297 0.242 -0.863 6.850 1.00 13.42 C
ANISOU 2261 CB ILE A 297 1885 1348 1868 44 514 24 C
ATOM 2262 CG1 ILE A 297 0.258 -0.034 5.566 1.00 13.68 C
ANISOU 2262 CG1 ILE A 297 1790 1419 1987 17 439 14 C
ATOM 2263 CG2 ILE A 297 -0.856 -0.380 7.770 1.00 15.72 C
ANISOU 2263 CG2 ILE A 297 2204 1618 2150 -11 552 -28 C
ATOM 2264 CD1 ILE A 297 -0.959 -0.225 4.692 1.00 15.68 C
ANISOU 2264 CD1 ILE A 297 2048 1667 2244 -43 458 -67 C
ATOM 2265 N TYR A 298 1.637 -2.769 8.960 1.00 24.76 N
ANISOU 2265 N TYR A 298 3803 2577 3029 244 662 150 N
ATOM 2266 CA TYR A 298 1.463 -3.476 10.224 1.00 26.29 C
ANISOU 2266 CA TYR A 298 4222 2657 3112 253 643 163 C
ATOM 2267 C TYR A 298 2.558 -3.110 11.215 1.00 20.48 C
ANISOU 2267 C TYR A 298 3528 1919 2334 386 529 215 C
ATOM 2268 O TYR A 298 2.303 -2.999 12.420 1.00 25.37 O
ANISOU 2268 O TYR A 298 4269 2495 2876 357 525 228 O
ATOM 2269 CB TYR A 298 1.436 -4.985 9.990 1.00 25.58 C
ANISOU 2269 CB TYR A 298 4322 2433 2964 284 646 166 C
ATOM 2270 CG TYR A 298 1.169 -5.789 11.248 1.00 30.24 C
ANISOU 2270 CG TYR A 298 5146 2900 3444 277 642 191 C
ATOM 2271 CD1 TYR A 298 -0.090 -5.802 11.835 1.00 25.60 C
ANISOU 2271 CD1 TYR A 298 4597 2300 2828 131 723 161 C
ATOM 2272 CD2 TYR A 298 2.176 -6.538 11.845 1.00 35.66 C
ANISOU 2272 CD2 TYR A 298 5992 3488 4068 426 544 240 C
ATOM 2273 CE1 TYR A 298 -0.337 -6.535 12.985 1.00 31.55 C
ANISOU 2273 CE1 TYR A 298 5567 2938 3481 120 729 192 C
ATOM 2274 CE2 TYR A 298 1.938 -7.274 12.992 1.00 31.83 C
ANISOU 2274 CE2 TYR A 298 5731 2884 3479 415 541 274 C
ATOM 2275 CZ TYR A 298 0.681 -7.269 13.557 1.00 29.52 C
ANISOU 2275 CZ TYR A 298 5496 2574 3146 256 643 255 C
ATOM 2276 OH TYR A 298 0.447 -8.002 14.699 1.00 39.15 O
ANISOU 2276 OH TYR A 298 6941 3674 4262 242 645 295 O
ATOM 2277 N CYS A 299 3.784 -2.919 10.733 1.00 25.69 N
ANISOU 2277 N CYS A 299 4065 2643 3052 532 417 229 N
ATOM 2278 CA CYS A 299 4.867 -2.563 11.639 1.00 37.01 C
ANISOU 2278 CA CYS A 299 5487 4106 4467 653 278 258 C
ATOM 2279 C CYS A 299 4.706 -1.164 12.227 1.00 28.76 C
ANISOU 2279 C CYS A 299 4324 3157 3446 598 268 268 C
ATOM 2280 O CYS A 299 5.558 -0.752 13.026 1.00 26.65 O
ANISOU 2280 O CYS A 299 4035 2924 3165 677 143 287 O
ATOM 2281 CB CYS A 299 6.215 -2.675 10.920 1.00 24.86 C
ANISOU 2281 CB CYS A 299 3775 2645 3024 780 161 239 C
ATOM 2282 SG CYS A 299 6.538 -1.361 9.726 1.00 35.17 S
ANISOU 2282 SG CYS A 299 4727 4152 4484 707 139 189 S
ATOM 2283 N VAL A 300 3.653 -0.428 11.862 1.00 18.01 N
ANISOU 2283 N VAL A 300 2872 1838 2134 457 395 251 N
ATOM 2284 CA VAL A 300 3.453 0.929 12.360 1.00 34.17 C
ANISOU 2284 CA VAL A 300 4791 3965 4226 403 401 258 C
ATOM 2285 C VAL A 300 2.143 1.048 13.135 1.00 29.70 C
ANISOU 2285 C VAL A 300 4334 3334 3618 240 512 214 C
ATOM 2286 O VAL A 300 2.033 1.876 14.047 1.00 19.05 O
ANISOU 2286 O VAL A 300 2988 2002 2250 203 495 217 O
ATOM 2287 CB VAL A 300 3.493 1.944 11.203 1.00 26.98 C
ANISOU 2287 CB VAL A 300 3564 3216 3473 339 406 252 C
ATOM 2288 CG1 VAL A 300 3.206 3.344 11.719 1.00 27.19 C
ANISOU 2288 CG1 VAL A 300 3457 3304 3570 246 379 263 C
ATOM 2289 CG2 VAL A 300 4.839 1.893 10.488 1.00 27.12 C
ANISOU 2289 CG2 VAL A 300 3442 3334 3528 412 221 199 C
ATOM 2290 N VAL A 301 1.154 0.215 12.801 1.00 33.08 N
ANISOU 2290 N VAL A 301 4823 3706 4041 145 582 154 N
ATOM 2291 CA VAL A 301 -0.174 0.281 13.404 1.00 35.26 C
ANISOU 2291 CA VAL A 301 5128 3956 4312 16 629 87 C
ATOM 2292 C VAL A 301 -0.479 -0.943 14.234 1.00 36.05 C
ANISOU 2292 C VAL A 301 5495 3931 4273 7 675 104 C
ATOM 2293 O VAL A 301 -1.531 -0.995 14.882 1.00 50.02 O
ANISOU 2293 O VAL A 301 7351 5646 6007 -82 755 53 O
ATOM 2294 CB VAL A 301 -1.271 0.482 12.340 1.00 27.54 C
ANISOU 2294 CB VAL A 301 4020 2999 3446 -52 678 -10 C
ATOM 2295 CG1 VAL A 301 -0.993 1.725 11.515 1.00 24.35 C
ANISOU 2295 CG1 VAL A 301 3382 2687 3184 -31 590 -22 C
ATOM 2296 CG2 VAL A 301 -1.406 -0.763 11.457 1.00 34.02 C
ANISOU 2296 CG2 VAL A 301 4914 3775 4238 -44 724 -16 C
ATOM 2297 N GLY A 302 0.401 -1.934 14.231 1.00 21.68 N
ANISOU 2297 N GLY A 302 3841 2033 2364 112 638 165 N
ATOM 2298 CA GLY A 302 0.190 -3.109 15.041 1.00 43.94 C
ANISOU 2298 CA GLY A 302 6919 4720 5058 114 656 190 C
ATOM 2299 C GLY A 302 0.460 -2.844 16.510 1.00 61.81 C
ANISOU 2299 C GLY A 302 9346 6932 7205 135 619 225 C
ATOM 2300 O GLY A 302 1.031 -1.821 16.887 1.00 56.70 O
ANISOU 2300 O GLY A 302 8631 6351 6563 176 558 240 O
ATOM 2301 N SER A 303 0.025 -3.793 17.342 1.00 45.24 N
ANISOU 2301 N SER A 303 7474 4716 4998 104 654 244 N
ATOM 2302 CA SER A 303 0.227 -3.737 18.781 1.00 47.22 C
ANISOU 2302 CA SER A 303 7926 4901 5112 117 622 284 C
ATOM 2303 C SER A 303 0.880 -5.029 19.248 1.00 53.29 C
ANISOU 2303 C SER A 303 8942 5542 5765 217 547 357 C
ATOM 2304 O SER A 303 0.650 -6.097 18.677 1.00 60.95 O
ANISOU 2304 O SER A 303 9963 6443 6752 215 579 364 O
ATOM 2305 CB SER A 303 -1.100 -3.533 19.520 1.00 49.00 C
ANISOU 2305 CB SER A 303 8188 5108 5323 -37 747 241 C
ATOM 2306 OG SER A 303 -0.889 -3.282 20.899 1.00 67.37 O
ANISOU 2306 OG SER A 303 10700 7386 7513 -34 723 278 O
ATOM 2307 N HIS A 304 1.681 -4.932 20.311 1.00 54.46 N
ANISOU 2307 N HIS A 304 9239 5657 5798 303 436 413 N
ATOM 2308 CA HIS A 304 2.294 -6.135 20.863 1.00 63.75 C
ANISOU 2308 CA HIS A 304 10642 6709 6871 399 345 489 C
ATOM 2309 C HIS A 304 1.274 -7.017 21.565 1.00 64.91 C
ANISOU 2309 C HIS A 304 11001 6736 6928 282 458 511 C
ATOM 2310 O HIS A 304 1.597 -8.157 21.922 1.00 62.90 O
ANISOU 2310 O HIS A 304 10938 6360 6600 340 404 581 O
ATOM 2311 CB HIS A 304 3.454 -5.779 21.808 1.00 67.30 C
ANISOU 2311 CB HIS A 304 11171 7171 7230 525 169 544 C
ATOM 2312 CG HIS A 304 3.072 -4.898 22.958 1.00 71.98 C
ANISOU 2312 CG HIS A 304 11842 7790 7717 443 194 538 C
ATOM 2313 ND1 HIS A 304 2.571 -3.626 22.784 1.00 74.99 N
ANISOU 2313 ND1 HIS A 304 12054 8278 8163 356 269 473 N
ATOM 2314 CD2 HIS A 304 3.147 -5.090 24.296 1.00 77.41 C
ANISOU 2314 CD2 HIS A 304 12760 8411 8240 437 149 593 C
ATOM 2315 CE1 HIS A 304 2.337 -3.080 23.962 1.00 75.29 C
ANISOU 2315 CE1 HIS A 304 12215 8310 8081 299 277 479 C
ATOM 2316 NE2 HIS A 304 2.679 -3.947 24.898 1.00 82.05 N
ANISOU 2316 NE2 HIS A 304 13319 9067 8789 345 206 551 N
ATOM 2317 N GLU A 305 0.049 -6.529 21.740 1.00 59.21 N
ANISOU 2317 N GLU A 305 10229 6044 6225 123 609 455 N
ATOM 2318 CA GLU A 305 -1.061 -7.351 22.189 1.00 57.28 C
ANISOU 2318 CA GLU A 305 10126 5705 5934 2 734 466 C
ATOM 2319 C GLU A 305 -1.745 -8.063 21.029 1.00 52.37 C
ANISOU 2319 C GLU A 305 9398 5072 5429 -52 811 430 C
ATOM 2320 O GLU A 305 -2.767 -8.725 21.239 1.00 50.56 O
ANISOU 2320 O GLU A 305 9272 4763 5174 -159 926 428 O
ATOM 2321 CB GLU A 305 -2.088 -6.507 22.951 1.00 63.58 C
ANISOU 2321 CB GLU A 305 10899 6545 6714 -136 854 420 C
ATOM 2322 CG GLU A 305 -1.654 -6.109 24.346 1.00 69.37 C
ANISOU 2322 CG GLU A 305 11821 7251 7286 -116 804 470 C
ATOM 2323 CD GLU A 305 -0.493 -5.139 24.339 1.00 81.66 C
ANISOU 2323 CD GLU A 305 13294 8893 8839 -1 659 469 C
ATOM 2324 OE1 GLU A 305 -0.027 -4.779 23.237 1.00 78.93 O
ANISOU 2324 OE1 GLU A 305 12740 8626 8623 62 609 434 O
ATOM 2325 OE2 GLU A 305 -0.047 -4.736 25.435 1.00 82.05 O
ANISOU 2325 OE2 GLU A 305 13483 8938 8753 25 592 507 O
ATOM 2326 N ASP A 306 -1.183 -7.937 19.757 1.00 52.17 N
ANISOU 2326 N ASP A 306 9193 5115 5516 23 757 399 N
ATOM 2327 CA ASP A 306 -1.824 -8.588 18.623 1.00 58.21 C
ANISOU 2327 CA ASP A 306 9876 5868 6373 -30 826 361 C
ATOM 2328 C ASP A 306 -1.222 -9.975 18.403 1.00 57.48 C
ANISOU 2328 C ASP A 306 9943 5642 6253 59 757 430 C
ATOM 2329 O ASP A 306 -0.041 -10.194 18.689 1.00 57.94 O
ANISOU 2329 O ASP A 306 10096 5656 6262 205 632 485 O
ATOM 2330 CB ASP A 306 -1.663 -7.746 17.352 1.00 45.68 C
ANISOU 2330 CB ASP A 306 8016 4421 4918 -14 817 294 C
ATOM 2331 CG ASP A 306 -2.907 -6.930 17.020 1.00 50.40 C
ANISOU 2331 CG ASP A 306 8459 5102 5588 -151 940 200 C
ATOM 2332 OD1 ASP A 306 -3.991 -7.226 17.571 1.00 58.36 O
ANISOU 2332 OD1 ASP A 306 9566 6050 6560 -259 1046 180 O
ATOM 2333 OD2 ASP A 306 -2.805 -5.994 16.194 1.00 47.97 O
ANISOU 2333 OD2 ASP A 306 7925 4919 5384 -144 926 149 O
ATOM 2334 N PRO A 307 -2.007 -10.931 17.901 1.00 47.41 N
ANISOU 2334 N PRO A 307 8724 4284 5006 -16 836 422 N
ATOM 2335 CA PRO A 307 -1.472 -12.273 17.635 1.00 49.28 C
ANISOU 2335 CA PRO A 307 9104 4378 5244 67 768 484 C
ATOM 2336 C PRO A 307 -0.274 -12.259 16.695 1.00 58.13 C
ANISOU 2336 C PRO A 307 10128 5526 6431 223 658 473 C
ATOM 2337 O PRO A 307 -0.041 -11.302 15.954 1.00 56.44 O
ANISOU 2337 O PRO A 307 9705 5452 6286 240 653 416 O
ATOM 2338 CB PRO A 307 -2.659 -12.998 16.996 1.00 50.58 C
ANISOU 2338 CB PRO A 307 9286 4480 5453 -64 886 450 C
ATOM 2339 CG PRO A 307 -3.859 -12.322 17.550 1.00 48.08 C
ANISOU 2339 CG PRO A 307 8938 4222 5108 -213 1015 407 C
ATOM 2340 CD PRO A 307 -3.469 -10.878 17.701 1.00 46.02 C
ANISOU 2340 CD PRO A 307 8510 4119 4858 -181 988 361 C
ATOM 2341 N ALA A 308 0.483 -13.364 16.730 1.00 54.69 N
ANISOU 2341 N ALA A 308 9849 4947 5985 342 570 531 N
ATOM 2342 CA ALA A 308 1.682 -13.486 15.908 1.00 52.73 C
ANISOU 2342 CA ALA A 308 9518 4705 5812 513 461 519 C
ATOM 2343 C ALA A 308 1.342 -13.747 14.447 1.00 53.30 C
ANISOU 2343 C ALA A 308 9459 4794 5998 480 516 446 C
ATOM 2344 O ALA A 308 2.110 -13.365 13.559 1.00 51.85 O
ANISOU 2344 O ALA A 308 9122 4687 5891 582 466 404 O
ATOM 2345 CB ALA A 308 2.571 -14.606 16.450 1.00 55.31 C
ANISOU 2345 CB ALA A 308 10038 4865 6113 658 343 598 C
ATOM 2346 N VAL A 309 0.202 -14.390 14.175 1.00 58.57 N
ANISOU 2346 N VAL A 309 10178 5394 6682 337 615 430 N
ATOM 2347 CA VAL A 309 -0.149 -14.725 12.797 1.00 53.81 C
ANISOU 2347 CA VAL A 309 9472 4793 6182 300 654 361 C
ATOM 2348 C VAL A 309 -0.196 -13.471 11.939 1.00 46.88 C
ANISOU 2348 C VAL A 309 8343 4112 5357 270 682 293 C
ATOM 2349 O VAL A 309 0.149 -13.508 10.751 1.00 43.08 O
ANISOU 2349 O VAL A 309 7758 3658 4954 318 668 241 O
ATOM 2350 CB VAL A 309 -1.488 -15.491 12.757 1.00 61.88 C
ANISOU 2350 CB VAL A 309 10580 5723 7208 134 752 357 C
ATOM 2351 CG1 VAL A 309 -2.633 -14.618 13.257 1.00 46.72 C
ANISOU 2351 CG1 VAL A 309 8597 3915 5238 -28 864 339 C
ATOM 2352 CG2 VAL A 309 -1.769 -15.992 11.351 1.00 74.92 C
ANISOU 2352 CG2 VAL A 309 12163 7346 8958 107 771 287 C
ATOM 2353 N TYR A 310 -0.609 -12.342 12.518 1.00 42.37 N
ANISOU 2353 N TYR A 310 7673 3674 4751 193 722 291 N
ATOM 2354 CA TYR A 310 -0.600 -11.090 11.771 1.00 40.10 C
ANISOU 2354 CA TYR A 310 7144 3568 4525 170 739 237 C
ATOM 2355 C TYR A 310 0.810 -10.710 11.349 1.00 40.11 C
ANISOU 2355 C TYR A 310 7070 3612 4558 345 641 242 C
ATOM 2356 O TYR A 310 0.989 -10.013 10.345 1.00 43.13 O
ANISOU 2356 O TYR A 310 7264 4108 5014 350 647 199 O
ATOM 2357 CB TYR A 310 -1.210 -9.966 12.608 1.00 37.11 C
ANISOU 2357 CB TYR A 310 6689 3299 4112 77 790 229 C
ATOM 2358 CG TYR A 310 -2.693 -10.109 12.884 1.00 40.90 C
ANISOU 2358 CG TYR A 310 7214 3758 4567 -88 915 194 C
ATOM 2359 CD1 TYR A 310 -3.438 -11.135 12.316 1.00 36.20 C
ANISOU 2359 CD1 TYR A 310 6695 3068 3989 -161 969 182 C
ATOM 2360 CD2 TYR A 310 -3.351 -9.204 13.709 1.00 42.96 C
ANISOU 2360 CD2 TYR A 310 7434 4086 4801 -165 975 168 C
ATOM 2361 CE1 TYR A 310 -4.789 -11.259 12.567 1.00 34.68 C
ANISOU 2361 CE1 TYR A 310 6529 2859 3791 -305 1075 152 C
ATOM 2362 CE2 TYR A 310 -4.702 -9.321 13.965 1.00 37.50 C
ANISOU 2362 CE2 TYR A 310 6770 3372 4106 -301 1087 128 C
ATOM 2363 CZ TYR A 310 -5.416 -10.349 13.392 1.00 39.67 C
ANISOU 2363 CZ TYR A 310 7111 3562 4401 -370 1136 125 C
ATOM 2364 OH TYR A 310 -6.763 -10.468 13.646 1.00 53.04 O
ANISOU 2364 OH TYR A 310 8819 5232 6104 -502 1241 93 O
ATOM 2365 N THR A 311 1.819 -11.149 12.102 1.00 32.06 N
ANISOU 2365 N THR A 311 6180 2510 3493 492 543 295 N
ATOM 2366 CA THR A 311 3.198 -10.840 11.742 1.00 41.10 C
ANISOU 2366 CA THR A 311 7219 3706 4690 675 432 293 C
ATOM 2367 C THR A 311 3.626 -11.629 10.513 1.00 36.08 C
ANISOU 2367 C THR A 311 6550 3017 4143 758 419 244 C
ATOM 2368 O THR A 311 4.062 -11.058 9.507 1.00 39.10 O
ANISOU 2368 O THR A 311 6742 3510 4606 804 413 193 O
ATOM 2369 CB THR A 311 4.126 -11.140 12.919 1.00 42.81 C
ANISOU 2369 CB THR A 311 7566 3854 4845 808 315 361 C
ATOM 2370 OG1 THR A 311 3.736 -10.356 14.053 1.00 38.01 O
ANISOU 2370 OG1 THR A 311 6997 3296 4148 729 327 394 O
ATOM 2371 CG2 THR A 311 5.570 -10.829 12.554 1.00 38.44 C
ANISOU 2371 CG2 THR A 311 6859 3373 4374 996 192 354 C
ATOM 2372 N TYR A 312 3.507 -12.954 10.578 1.00 42.70 N
ANISOU 2372 N TYR A 312 7572 3680 4972 780 416 254 N
ATOM 2373 CA TYR A 312 3.935 -13.782 9.460 1.00 52.12 C
ANISOU 2373 CA TYR A 312 8749 4800 6253 868 403 193 C
ATOM 2374 C TYR A 312 3.063 -13.553 8.235 1.00 39.48 C
ANISOU 2374 C TYR A 312 7043 3262 4696 737 497 116 C
ATOM 2375 O TYR A 312 3.555 -13.629 7.103 1.00 37.71 O
ANISOU 2375 O TYR A 312 6714 3068 4548 813 489 42 O
ATOM 2376 CB TYR A 312 3.919 -15.252 9.872 1.00 59.20 C
ANISOU 2376 CB TYR A 312 9875 5477 7140 909 378 223 C
ATOM 2377 CG TYR A 312 4.765 -15.533 11.092 1.00 58.15 C
ANISOU 2377 CG TYR A 312 9858 5273 6964 1036 273 310 C
ATOM 2378 CD1 TYR A 312 6.151 -15.547 11.009 1.00 78.55 C
ANISOU 2378 CD1 TYR A 312 12356 7874 9617 1238 164 308 C
ATOM 2379 CD2 TYR A 312 4.181 -15.776 12.328 1.00 61.51 C
ANISOU 2379 CD2 TYR A 312 10465 5620 7285 950 282 393 C
ATOM 2380 CE1 TYR A 312 6.931 -15.799 12.119 1.00 80.83 C
ANISOU 2380 CE1 TYR A 312 12738 8099 9875 1350 53 394 C
ATOM 2381 CE2 TYR A 312 4.955 -16.029 13.445 1.00 76.16 C
ANISOU 2381 CE2 TYR A 312 12436 7409 9093 1063 174 478 C
ATOM 2382 CZ TYR A 312 6.329 -16.039 13.334 1.00 73.67 C
ANISOU 2382 CZ TYR A 312 12031 7109 8850 1263 53 480 C
ATOM 2383 OH TYR A 312 7.104 -16.290 14.442 1.00 65.98 O
ANISOU 2383 OH TYR A 312 11161 6072 7838 1371 -69 571 O
ATOM 2384 N ALA A 313 1.777 -13.259 8.435 1.00 37.66 N
ANISOU 2384 N ALA A 313 6825 3060 4423 541 585 128 N
ATOM 2385 CA ALA A 313 0.909 -12.967 7.302 1.00 37.51 C
ANISOU 2385 CA ALA A 313 6688 3114 4452 407 661 63 C
ATOM 2386 C ALA A 313 1.409 -11.759 6.522 1.00 32.24 C
ANISOU 2386 C ALA A 313 5793 2623 3832 444 653 27 C
ATOM 2387 O ALA A 313 1.126 -11.633 5.326 1.00 34.69 O
ANISOU 2387 O ALA A 313 6004 2983 4192 396 686 -38 O
ATOM 2388 CB ALA A 313 -0.523 -12.739 7.783 1.00 43.58 C
ANISOU 2388 CB ALA A 313 7463 3913 5184 202 745 83 C
ATOM 2389 N THR A 314 2.150 -10.866 7.178 1.00 32.66 N
ANISOU 2389 N THR A 314 5763 2772 3873 526 603 69 N
ATOM 2390 CA THR A 314 2.753 -9.723 6.505 1.00 32.08 C
ANISOU 2390 CA THR A 314 5462 2865 3861 576 582 43 C
ATOM 2391 C THR A 314 4.181 -9.999 6.053 1.00 32.59 C
ANISOU 2391 C THR A 314 5459 2941 3982 783 494 9 C
ATOM 2392 O THR A 314 4.636 -9.411 5.064 1.00 25.32 O
ANISOU 2392 O THR A 314 4346 2146 3127 821 490 -45 O
ATOM 2393 CB THR A 314 2.742 -8.500 7.427 1.00 23.70 C
ANISOU 2393 CB THR A 314 4312 1916 2775 540 573 98 C
ATOM 2394 OG1 THR A 314 3.539 -8.763 8.587 1.00 33.16 O
ANISOU 2394 OG1 THR A 314 5618 3057 3923 662 487 150 O
ATOM 2395 CG2 THR A 314 1.320 -8.164 7.854 1.00 22.48 C
ANISOU 2395 CG2 THR A 314 4180 1778 2581 337 672 108 C
ATOM 2396 N LEU A 315 4.905 -10.866 6.763 1.00 35.81 N
ANISOU 2396 N LEU A 315 6003 3230 4372 913 426 38 N
ATOM 2397 CA LEU A 315 6.234 -11.270 6.316 1.00 36.31 C
ANISOU 2397 CA LEU A 315 5992 3296 4510 1105 353 -1 C
ATOM 2398 C LEU A 315 6.168 -12.299 5.196 1.00 34.31 C
ANISOU 2398 C LEU A 315 5790 2947 4300 1135 395 -92 C
ATOM 2399 O LEU A 315 7.016 -12.295 4.298 1.00 41.49 O
ANISOU 2399 O LEU A 315 6558 3923 5284 1244 385 -164 O
ATOM 2400 CB LEU A 315 7.033 -11.829 7.489 1.00 31.22 C
ANISOU 2400 CB LEU A 315 5466 2551 3844 1232 258 68 C
ATOM 2401 CG LEU A 315 7.419 -10.794 8.538 1.00 31.91 C
ANISOU 2401 CG LEU A 315 5478 2747 3900 1238 190 140 C
ATOM 2402 CD1 LEU A 315 7.994 -11.486 9.755 1.00 37.90 C
ANISOU 2402 CD1 LEU A 315 6402 3381 4617 1337 95 213 C
ATOM 2403 CD2 LEU A 315 8.414 -9.801 7.958 1.00 40.76 C
ANISOU 2403 CD2 LEU A 315 6315 4054 5119 1307 144 109 C
ATOM 2404 N LEU A 316 5.181 -13.190 5.230 1.00 38.14 N
ANISOU 2404 N LEU A 316 6467 3279 4744 1033 446 -96 N
ATOM 2405 CA LEU A 316 5.103 -14.237 4.214 1.00 46.63 C
ANISOU 2405 CA LEU A 316 7610 4246 5863 1060 476 -193 C
ATOM 2406 C LEU A 316 5.093 -13.670 2.802 1.00 41.98 C
ANISOU 2406 C LEU A 316 6839 3798 5313 1036 522 -297 C
ATOM 2407 O LEU A 316 5.880 -14.144 1.967 1.00 51.72 O
ANISOU 2407 O LEU A 316 8022 5026 6604 1163 518 -390 O
ATOM 2408 CB LEU A 316 3.868 -15.112 4.474 1.00 47.31 C
ANISOU 2408 CB LEU A 316 7902 4168 5904 909 523 -175 C
ATOM 2409 CG LEU A 316 3.658 -16.284 3.510 1.00 57.29 C
ANISOU 2409 CG LEU A 316 9262 5291 7214 918 546 -278 C
ATOM 2410 CD1 LEU A 316 4.743 -17.340 3.686 1.00 52.42 C
ANISOU 2410 CD1 LEU A 316 8736 4525 6656 1119 487 -298 C
ATOM 2411 CD2 LEU A 316 2.272 -16.890 3.699 1.00 69.53 C
ANISOU 2411 CD2 LEU A 316 10963 6723 8731 725 594 -256 C
ATOM 2412 N PRO A 317 4.276 -12.669 2.467 1.00 40.97 N
ANISOU 2412 N PRO A 317 6605 3802 5160 882 569 -289 N
ATOM 2413 CA PRO A 317 4.365 -12.108 1.111 1.00 45.10 C
ANISOU 2413 CA PRO A 317 6952 4472 5714 870 601 -386 C
ATOM 2414 C PRO A 317 5.680 -11.397 0.867 1.00 32.66 C
ANISOU 2414 C PRO A 317 5161 3056 4190 1017 560 -402 C
ATOM 2415 O PRO A 317 6.273 -11.543 -0.209 1.00 52.20 O
ANISOU 2415 O PRO A 317 7536 5597 6701 1090 579 -503 O
ATOM 2416 CB PRO A 317 3.172 -11.142 1.047 1.00 40.63 C
ANISOU 2416 CB PRO A 317 6323 3997 5117 666 650 -343 C
ATOM 2417 CG PRO A 317 2.316 -11.479 2.227 1.00 36.21 C
ANISOU 2417 CG PRO A 317 5931 3315 4513 556 667 -250 C
ATOM 2418 CD PRO A 317 3.244 -11.992 3.266 1.00 38.45 C
ANISOU 2418 CD PRO A 317 6309 3513 4789 712 602 -199 C
ATOM 2419 N ALA A 318 6.158 -10.629 1.848 1.00 44.41 N
ANISOU 2419 N ALA A 318 6572 4616 5687 1049 507 -307 N
ATOM 2420 CA ALA A 318 7.428 -9.931 1.686 1.00 37.38 C
ANISOU 2420 CA ALA A 318 5462 3877 4864 1160 459 -310 C
ATOM 2421 C ALA A 318 8.573 -10.918 1.521 1.00 49.55 C
ANISOU 2421 C ALA A 318 7032 5332 6462 1340 436 -354 C
ATOM 2422 O ALA A 318 9.461 -10.719 0.684 1.00 48.77 O
ANISOU 2422 O ALA A 318 6766 5336 6427 1412 451 -413 O
ATOM 2423 CB ALA A 318 7.675 -9.017 2.884 1.00 27.35 C
ANISOU 2423 CB ALA A 318 4128 2673 3590 1148 393 -202 C
ATOM 2424 N THR A 319 8.569 -11.994 2.308 1.00 49.87 N
ANISOU 2424 N THR A 319 7285 5177 6486 1408 405 -322 N
ATOM 2425 CA THR A 319 9.615 -12.999 2.175 1.00 50.23 C
ANISOU 2425 CA THR A 319 7364 5117 6603 1585 382 -364 C
ATOM 2426 C THR A 319 9.588 -13.626 0.787 1.00 56.64 C
ANISOU 2426 C THR A 319 8168 5910 7443 1608 462 -505 C
ATOM 2427 O THR A 319 10.607 -13.660 0.088 1.00 68.49 O
ANISOU 2427 O THR A 319 9528 7476 9021 1721 482 -571 O
ATOM 2428 CB THR A 319 9.459 -14.072 3.254 1.00 65.40 C
ANISOU 2428 CB THR A 319 9532 6818 8501 1633 331 -300 C
ATOM 2429 OG1 THR A 319 8.121 -14.585 3.236 1.00 78.11 O
ANISOU 2429 OG1 THR A 319 11335 8309 10034 1489 382 -308 O
ATOM 2430 CG2 THR A 319 9.768 -13.502 4.633 1.00 59.46 C
ANISOU 2430 CG2 THR A 319 8778 6094 7719 1644 242 -171 C
ATOM 2431 N LEU A 320 8.421 -14.103 0.355 1.00 47.26 N
ANISOU 2431 N LEU A 320 7126 4636 6193 1489 514 -558 N
ATOM 2432 CA LEU A 320 8.329 -14.771 -0.936 1.00 51.63 C
ANISOU 2432 CA LEU A 320 7699 5160 6760 1503 583 -707 C
ATOM 2433 C LEU A 320 8.366 -13.798 -2.106 1.00 51.54 C
ANISOU 2433 C LEU A 320 7475 5374 6735 1443 639 -780 C
ATOM 2434 O LEU A 320 8.389 -14.244 -3.259 1.00 51.44 O
ANISOU 2434 O LEU A 320 7458 5370 6717 1457 702 -916 O
ATOM 2435 CB LEU A 320 7.058 -15.626 -1.005 1.00 47.37 C
ANISOU 2435 CB LEU A 320 7386 4448 6165 1377 605 -737 C
ATOM 2436 CG LEU A 320 5.705 -14.913 -0.996 1.00 48.55 C
ANISOU 2436 CG LEU A 320 7546 4663 6239 1160 626 -691 C
ATOM 2437 CD1 LEU A 320 5.274 -14.509 -2.399 1.00 52.40 C
ANISOU 2437 CD1 LEU A 320 7929 5282 6696 1076 681 -808 C
ATOM 2438 CD2 LEU A 320 4.653 -15.799 -0.349 1.00 47.17 C
ANISOU 2438 CD2 LEU A 320 7608 4281 6034 1047 623 -643 C
ATOM 2439 N ASN A 321 8.364 -12.489 -1.845 1.00 47.59 N
ANISOU 2439 N ASN A 321 6804 5053 6226 1370 618 -698 N
ATOM 2440 CA ASN A 321 8.537 -11.528 -2.928 1.00 45.91 C
ANISOU 2440 CA ASN A 321 6373 5058 6013 1312 665 -752 C
ATOM 2441 C ASN A 321 9.884 -11.716 -3.607 1.00 50.75 C
ANISOU 2441 C ASN A 321 6870 5726 6689 1464 706 -813 C
ATOM 2442 O ASN A 321 9.981 -11.659 -4.838 1.00 53.52 O
ANISOU 2442 O ASN A 321 7148 6170 7017 1448 786 -916 O
ATOM 2443 CB ASN A 321 8.408 -10.103 -2.398 1.00 50.74 C
ANISOU 2443 CB ASN A 321 6825 5829 6624 1216 623 -638 C
ATOM 2444 CG ASN A 321 8.876 -9.070 -3.401 1.00 42.46 C
ANISOU 2444 CG ASN A 321 5559 4993 5581 1184 664 -653 C
ATOM 2445 OD1 ASN A 321 10.002 -8.586 -3.326 1.00 31.84 O
ANISOU 2445 OD1 ASN A 321 4086 3729 4282 1275 648 -598 O
ATOM 2446 ND2 ASN A 321 8.017 -8.737 -4.354 1.00 47.79 N
ANISOU 2446 ND2 ASN A 321 6197 5758 6203 1049 710 -720 N
ATOM 2447 N SER A 322 10.939 -11.928 -2.818 1.00 45.50 N
ANISOU 2447 N SER A 322 6191 5005 6093 1614 655 -744 N
ATOM 2448 CA SER A 322 12.249 -12.219 -3.384 1.00 51.09 C
ANISOU 2448 CA SER A 322 6801 5740 6872 1780 695 -795 C
ATOM 2449 C SER A 322 12.283 -13.563 -4.100 1.00 58.95 C
ANISOU 2449 C SER A 322 7927 6584 7885 1864 764 -945 C
ATOM 2450 O SER A 322 13.141 -13.769 -4.964 1.00 58.16 O
ANISOU 2450 O SER A 322 7740 6531 7827 1969 841 -1030 O
ATOM 2451 CB SER A 322 13.307 -12.189 -2.281 1.00 58.40 C
ANISOU 2451 CB SER A 322 7685 6628 7876 1917 605 -687 C
ATOM 2452 OG SER A 322 13.433 -10.889 -1.730 1.00 53.73 O
ANISOU 2452 OG SER A 322 6954 6191 7268 1844 543 -568 O
ATOM 2453 N MET A 323 11.381 -14.485 -3.753 1.00 57.86 N
ANISOU 2453 N MET A 323 8000 6262 7722 1818 741 -977 N
ATOM 2454 CA MET A 323 11.289 -15.751 -4.471 1.00 55.50 C
ANISOU 2454 CA MET A 323 7845 5810 7431 1881 799 -1128 C
ATOM 2455 C MET A 323 10.584 -15.590 -5.810 1.00 58.46 C
ANISOU 2455 C MET A 323 8207 6291 7715 1763 885 -1264 C
ATOM 2456 O MET A 323 10.863 -16.348 -6.747 1.00 65.19 O
ANISOU 2456 O MET A 323 9098 7099 8574 1829 962 -1419 O
ATOM 2457 CB MET A 323 10.544 -16.788 -3.628 1.00 56.08 C
ANISOU 2457 CB MET A 323 8178 5637 7492 1870 738 -1095 C
ATOM 2458 CG MET A 323 10.723 -18.225 -4.112 1.00 63.48 C
ANISOU 2458 CG MET A 323 9271 6369 8480 1975 775 -1232 C
ATOM 2459 SD MET A 323 9.260 -19.261 -3.881 1.00 72.29 S
ANISOU 2459 SD MET A 323 10682 7250 9536 1840 745 -1253 S
ATOM 2460 CE MET A 323 8.169 -18.593 -5.137 1.00 67.82 C
ANISOU 2460 CE MET A 323 10065 6857 8846 1642 806 -1357 C
ATOM 2461 N ILE A 324 9.672 -14.626 -5.916 1.00 58.50 N
ANISOU 2461 N ILE A 324 8157 6435 7636 1589 872 -1215 N
ATOM 2462 CA ILE A 324 8.906 -14.444 -7.141 1.00 48.06 C
ANISOU 2462 CA ILE A 324 6826 5219 6215 1463 932 -1335 C
ATOM 2463 C ILE A 324 9.629 -13.548 -8.142 1.00 42.98 C
ANISOU 2463 C ILE A 324 5957 4807 5566 1455 1017 -1373 C
ATOM 2464 O ILE A 324 9.445 -13.706 -9.353 1.00 40.46 O
ANISOU 2464 O ILE A 324 5637 4563 5173 1412 1096 -1511 O
ATOM 2465 CB ILE A 324 7.511 -13.886 -6.808 1.00 45.59 C
ANISOU 2465 CB ILE A 324 6568 4930 5823 1277 874 -1260 C
ATOM 2466 CG1 ILE A 324 6.598 -15.019 -6.329 1.00 60.27 C
ANISOU 2466 CG1 ILE A 324 8693 6539 7667 1239 836 -1268 C
ATOM 2467 CG2 ILE A 324 6.910 -13.167 -8.016 1.00 51.87 C
ANISOU 2467 CG2 ILE A 324 7260 5929 6518 1146 911 -1337 C
ATOM 2468 CD1 ILE A 324 5.208 -14.574 -5.934 1.00 60.12 C
ANISOU 2468 CD1 ILE A 324 8747 6506 7589 1045 797 -1176 C
ATOM 2469 N ASN A 325 10.447 -12.608 -7.670 1.00 49.67 N
ANISOU 2469 N ASN A 325 6639 5763 6470 1499 1003 -1238 N
ATOM 2470 CA ASN A 325 11.120 -11.695 -8.592 1.00 50.75 C
ANISOU 2470 CA ASN A 325 6593 6100 6590 1491 1087 -1228 C
ATOM 2471 C ASN A 325 11.976 -12.435 -9.608 1.00 53.82 C
ANISOU 2471 C ASN A 325 6987 6477 6986 1619 1204 -1370 C
ATOM 2472 O ASN A 325 11.885 -12.117 -10.807 1.00 54.42 O
ANISOU 2472 O ASN A 325 7019 6679 6980 1546 1309 -1444 O
ATOM 2473 CB ASN A 325 11.947 -10.680 -7.798 1.00 47.10 C
ANISOU 2473 CB ASN A 325 5972 5728 6196 1543 1021 -1051 C
ATOM 2474 CG ASN A 325 11.085 -9.678 -7.068 1.00 45.58 C
ANISOU 2474 CG ASN A 325 5743 5594 5979 1388 934 -924 C
ATOM 2475 OD1 ASN A 325 9.911 -9.932 -6.797 1.00 41.17 O
ANISOU 2475 OD1 ASN A 325 5298 4967 5378 1276 904 -953 O
ATOM 2476 ND2 ASN A 325 11.663 -8.527 -6.747 1.00 46.78 N
ANISOU 2476 ND2 ASN A 325 5736 5876 6162 1380 886 -789 N
ATOM 2477 N PRO A 326 12.804 -13.411 -9.228 1.00 57.84 N
ANISOU 2477 N PRO A 326 7552 6837 7587 1805 1203 -1414 N
ATOM 2478 CA PRO A 326 13.562 -14.150 -10.250 1.00 54.64 C
ANISOU 2478 CA PRO A 326 7151 6415 7194 1926 1331 -1573 C
ATOM 2479 C PRO A 326 12.667 -14.824 -11.272 1.00 47.00 C
ANISOU 2479 C PRO A 326 6324 5418 6118 1825 1401 -1763 C
ATOM 2480 O PRO A 326 13.064 -14.976 -12.433 1.00 42.33 O
ANISOU 2480 O PRO A 326 5707 4902 5475 1848 1534 -1893 O
ATOM 2481 CB PRO A 326 14.356 -15.174 -9.425 1.00 60.72 C
ANISOU 2481 CB PRO A 326 7985 6984 8102 2127 1286 -1578 C
ATOM 2482 CG PRO A 326 14.420 -14.598 -8.050 1.00 57.68 C
ANISOU 2482 CG PRO A 326 7558 6585 7771 2127 1146 -1383 C
ATOM 2483 CD PRO A 326 13.134 -13.857 -7.864 1.00 54.40 C
ANISOU 2483 CD PRO A 326 7175 6244 7251 1914 1092 -1318 C
ATOM 2484 N ILE A 327 11.461 -15.228 -10.872 1.00 49.40 N
ANISOU 2484 N ILE A 327 6774 5618 6376 1711 1310 -1783 N
ATOM 2485 CA ILE A 327 10.570 -15.948 -11.774 1.00 42.38 C
ANISOU 2485 CA ILE A 327 6035 4692 5374 1632 1337 -1964 C
ATOM 2486 C ILE A 327 9.993 -15.022 -12.837 1.00 45.09 C
ANISOU 2486 C ILE A 327 6293 5272 5569 1451 1380 -1979 C
ATOM 2487 O ILE A 327 9.789 -15.439 -13.983 1.00 55.47 O
ANISOU 2487 O ILE A 327 7669 6636 6772 1415 1442 -2131 O
ATOM 2488 CB ILE A 327 9.457 -16.635 -10.962 1.00 45.84 C
ANISOU 2488 CB ILE A 327 6680 4933 5803 1581 1209 -1935 C
ATOM 2489 CG1 ILE A 327 10.066 -17.681 -10.021 1.00 56.02 C
ANISOU 2489 CG1 ILE A 327 8084 5971 7228 1750 1173 -1909 C
ATOM 2490 CG2 ILE A 327 8.432 -17.266 -11.891 1.00 45.33 C
ANISOU 2490 CG2 ILE A 327 6772 4837 5616 1484 1204 -2100 C
ATOM 2491 CD1 ILE A 327 9.107 -18.206 -8.969 1.00 66.92 C
ANISOU 2491 CD1 ILE A 327 9659 7147 8621 1688 1058 -1815 C
ATOM 2492 N ILE A 328 9.711 -13.765 -12.487 1.00 51.54 N
ANISOU 2492 N ILE A 328 6975 6231 6376 1327 1336 -1806 N
ATOM 2493 CA ILE A 328 9.011 -12.872 -13.410 1.00 52.50 C
ANISOU 2493 CA ILE A 328 7035 6549 6364 1131 1350 -1778 C
ATOM 2494 C ILE A 328 9.834 -12.648 -14.674 1.00 57.87 C
ANISOU 2494 C ILE A 328 7674 7330 6985 1142 1522 -1820 C
ATOM 2495 O ILE A 328 9.333 -12.792 -15.796 1.00 60.59 O
ANISOU 2495 O ILE A 328 8086 7744 7192 1031 1572 -1920 O
ATOM 2496 CB ILE A 328 8.674 -11.541 -12.714 1.00 56.66 C
ANISOU 2496 CB ILE A 328 7435 7166 6929 1011 1286 -1566 C
ATOM 2497 CG1 ILE A 328 7.462 -11.719 -11.796 1.00 41.67 C
ANISOU 2497 CG1 ILE A 328 5612 5210 5011 968 1118 -1546 C
ATOM 2498 CG2 ILE A 328 8.411 -10.452 -13.745 1.00 59.58 C
ANISOU 2498 CG2 ILE A 328 7765 7668 7204 844 1379 -1464 C
ATOM 2499 CD1 ILE A 328 7.295 -10.613 -10.777 1.00 41.15 C
ANISOU 2499 CD1 ILE A 328 5426 5190 5017 896 1048 -1357 C
ATOM 2500 N TYR A 329 11.111 -12.290 -14.514 1.00 58.69 N
ANISOU 2500 N TYR A 329 7669 7454 7175 1300 1603 -1744 N
ATOM 2501 CA TYR A 329 11.927 -11.935 -15.672 1.00 64.49 C
ANISOU 2501 CA TYR A 329 8351 8310 7842 1347 1758 -1758 C
ATOM 2502 C TYR A 329 12.104 -13.109 -16.626 1.00 66.85 C
ANISOU 2502 C TYR A 329 8775 8553 8071 1398 1864 -1990 C
ATOM 2503 O TYR A 329 12.178 -12.910 -17.844 1.00 67.40 O
ANISOU 2503 O TYR A 329 8883 8721 8003 1344 1988 -2032 O
ATOM 2504 CB TYR A 329 13.289 -11.417 -15.211 1.00 62.19 C
ANISOU 2504 CB TYR A 329 7870 8075 7686 1530 1781 -1659 C
ATOM 2505 CG TYR A 329 13.249 -10.002 -14.686 1.00 57.81 C
ANISOU 2505 CG TYR A 329 7158 7645 7164 1463 1690 -1436 C
ATOM 2506 CD1 TYR A 329 12.682 -9.715 -13.451 1.00 57.68 C
ANISOU 2506 CD1 TYR A 329 7134 7564 7217 1408 1539 -1327 C
ATOM 2507 CD2 TYR A 329 13.778 -8.952 -15.424 1.00 61.02 C
ANISOU 2507 CD2 TYR A 329 7420 8241 7525 1453 1730 -1332 C
ATOM 2508 CE1 TYR A 329 12.642 -8.423 -12.967 1.00 54.62 C
ANISOU 2508 CE1 TYR A 329 6607 7291 6857 1341 1437 -1133 C
ATOM 2509 CE2 TYR A 329 13.743 -7.656 -14.948 1.00 65.74 C
ANISOU 2509 CE2 TYR A 329 7865 8957 8158 1386 1605 -1136 C
ATOM 2510 CZ TYR A 329 13.174 -7.397 -13.718 1.00 58.11 C
ANISOU 2510 CZ TYR A 329 6901 7915 7262 1329 1460 -1041 C
ATOM 2511 OH TYR A 329 13.137 -6.109 -13.239 1.00 55.77 O
ANISOU 2511 OH TYR A 329 6464 7728 6998 1254 1331 -866 O
ATOM 2512 N ALA A 330 12.183 -14.332 -16.099 1.00 57.62 N
ANISOU 2512 N ALA A 330 7688 7216 6989 1515 1817 -2133 N
ATOM 2513 CA ALA A 330 12.359 -15.491 -16.967 1.00 65.87 C
ANISOU 2513 CA ALA A 330 8851 8194 7982 1581 1905 -2368 C
ATOM 2514 C ALA A 330 11.173 -15.663 -17.909 1.00 67.73 C
ANISOU 2514 C ALA A 330 9206 8503 8028 1390 1876 -2485 C
ATOM 2515 O ALA A 330 11.352 -15.925 -19.104 1.00 74.93 O
ANISOU 2515 O ALA A 330 10171 9484 8816 1369 1996 -2622 O
ATOM 2516 CB ALA A 330 12.557 -16.750 -16.124 1.00 67.87 C
ANISOU 2516 CB ALA A 330 9198 8210 8380 1749 1838 -2469 C
ATOM 2517 N PHE A 331 9.954 -15.509 -17.392 1.00 58.70 N
ANISOU 2517 N PHE A 331 8099 7359 6845 1271 1703 -2437 N
ATOM 2518 CA PHE A 331 8.751 -15.740 -18.183 1.00 61.64 C
ANISOU 2518 CA PHE A 331 8561 7827 7034 1156 1595 -2556 C
ATOM 2519 C PHE A 331 8.411 -14.579 -19.105 1.00 60.52 C
ANISOU 2519 C PHE A 331 8322 7919 6751 952 1638 -2469 C
ATOM 2520 O PHE A 331 7.583 -14.750 -20.007 1.00 58.43 O
ANISOU 2520 O PHE A 331 8080 7848 6270 979 1472 -2585 O
ATOM 2521 CB PHE A 331 7.562 -16.013 -17.258 1.00 63.85 C
ANISOU 2521 CB PHE A 331 8949 7991 7322 1156 1380 -2506 C
ATOM 2522 CG PHE A 331 7.585 -17.375 -16.622 1.00 57.11 C
ANISOU 2522 CG PHE A 331 8288 6829 6581 1278 1365 -2616 C
ATOM 2523 CD1 PHE A 331 8.612 -17.739 -15.766 1.00 52.17 C
ANISOU 2523 CD1 PHE A 331 7632 6049 6143 1420 1435 -2582 C
ATOM 2524 CD2 PHE A 331 6.574 -18.289 -16.872 1.00 66.55 C
ANISOU 2524 CD2 PHE A 331 9709 7868 7708 1249 1274 -2739 C
ATOM 2525 CE1 PHE A 331 8.635 -18.990 -15.180 1.00 51.31 C
ANISOU 2525 CE1 PHE A 331 7697 5652 6147 1535 1408 -2670 C
ATOM 2526 CE2 PHE A 331 6.592 -19.541 -16.286 1.00 72.51 C
ANISOU 2526 CE2 PHE A 331 10641 8316 8592 1332 1266 -2832 C
ATOM 2527 CZ PHE A 331 7.623 -19.892 -15.439 1.00 58.32 C
ANISOU 2527 CZ PHE A 331 8800 6382 6977 1480 1330 -2792 C
ATOM 2528 N ARG A 332 9.019 -13.413 -18.904 1.00 58.62 N
ANISOU 2528 N ARG A 332 8063 7632 6579 871 1811 -2202 N
ATOM 2529 CA ARG A 332 8.709 -12.222 -19.682 1.00 61.41 C
ANISOU 2529 CA ARG A 332 8641 7952 6742 808 1934 -1889 C
ATOM 2530 C ARG A 332 9.875 -11.756 -20.539 1.00 67.72 C
ANISOU 2530 C ARG A 332 9361 8888 7483 947 2075 -1863 C
ATOM 2531 O ARG A 332 9.727 -11.605 -21.756 1.00 70.60 O
ANISOU 2531 O ARG A 332 9884 9319 7621 970 2139 -1846 O
ATOM 2532 CB ARG A 332 8.272 -11.093 -18.739 1.00 59.35 C
ANISOU 2532 CB ARG A 332 8318 7702 6531 822 1810 -1602 C
ATOM 2533 CG ARG A 332 7.159 -11.487 -17.778 1.00 53.52 C
ANISOU 2533 CG ARG A 332 7683 6808 5843 718 1688 -1583 C
ATOM 2534 CD ARG A 332 5.923 -11.990 -18.511 1.00 63.08 C
ANISOU 2534 CD ARG A 332 8924 8419 6626 1195 1154 -1689 C
ATOM 2535 NE ARG A 332 5.463 -11.046 -19.522 1.00 66.01 N
ANISOU 2535 NE ARG A 332 9400 8800 6882 995 1307 -1573 N
ATOM 2536 CZ ARG A 332 4.776 -9.942 -19.260 1.00 56.25 C
ANISOU 2536 CZ ARG A 332 8017 7655 5699 800 1277 -1461 C
ATOM 2537 NH1 ARG A 332 4.464 -9.600 -18.021 1.00 45.36 N
ANISOU 2537 NH1 ARG A 332 6529 6230 4475 761 1198 -1366 N
ATOM 2538 NH2 ARG A 332 4.398 -9.158 -20.266 1.00 54.92 N
ANISOU 2538 NH2 ARG A 332 7796 7653 5416 652 1312 -1453 N
ATOM 2539 N ASN A 333 11.039 -11.529 -19.936 1.00 72.38 N
ANISOU 2539 N ASN A 333 9702 9547 8251 1082 2101 -1867 N
ATOM 2540 CA ASN A 333 12.190 -11.018 -20.670 1.00 75.60 C
ANISOU 2540 CA ASN A 333 9979 10114 8633 1208 2233 -1852 C
ATOM 2541 C ASN A 333 12.863 -12.165 -21.413 1.00 70.16 C
ANISOU 2541 C ASN A 333 9373 9374 7910 1299 2385 -2093 C
ATOM 2542 O ASN A 333 13.348 -13.117 -20.793 1.00 70.32 O
ANISOU 2542 O ASN A 333 9356 9280 8081 1410 2376 -2239 O
ATOM 2543 CB ASN A 333 13.169 -10.336 -19.717 1.00 73.59 C
ANISOU 2543 CB ASN A 333 9450 9927 8582 1331 2188 -1737 C
ATOM 2544 CG ASN A 333 14.269 -9.591 -20.447 1.00 71.27 C
ANISOU 2544 CG ASN A 333 8978 9824 8277 1425 2305 -1692 C
ATOM 2545 OD1 ASN A 333 14.921 -10.137 -21.337 1.00 69.79 O
ANISOU 2545 OD1 ASN A 333 8832 9659 8024 1504 2465 -1831 O
ATOM 2546 ND2 ASN A 333 14.473 -8.331 -20.080 1.00 69.98 N
ANISOU 2546 ND2 ASN A 333 8605 9803 8181 1401 2203 -1495 N
ATOM 2547 N GLN A 334 12.890 -12.071 -22.743 1.00 77.42 N
ANISOU 2547 N GLN A 334 10409 10382 8623 1275 2513 -2134 N
ATOM 2548 CA GLN A 334 13.454 -13.140 -23.558 1.00 70.71 C
ANISOU 2548 CA GLN A 334 9656 9490 7719 1343 2671 -2378 C
ATOM 2549 C GLN A 334 14.975 -13.139 -23.533 1.00 69.00 C
ANISOU 2549 C GLN A 334 9227 9346 7643 1550 2803 -2425 C
ATOM 2550 O GLN A 334 15.592 -14.208 -23.596 1.00 68.55 O
ANISOU 2550 O GLN A 334 9185 9198 7663 1671 2887 -2633 O
ATOM 2551 CB GLN A 334 12.957 -13.012 -25.000 1.00 68.90 C
ANISOU 2551 CB GLN A 334 9659 9326 7192 1259 2763 -2388 C
ATOM 2552 CG GLN A 334 13.300 -14.196 -25.887 1.00 74.32 C
ANISOU 2552 CG GLN A 334 10492 9951 7793 1283 2918 -2667 C
ATOM 2553 CD GLN A 334 12.602 -15.469 -25.450 1.00 84.29 C
ANISOU 2553 CD GLN A 334 11823 11066 9139 1187 2813 -2908 C
ATOM 2554 OE1 GLN A 334 11.640 -15.430 -24.681 1.00 59.06 O
ANISOU 2554 OE1 GLN A 334 8623 7818 5999 1074 2629 -2854 O
ATOM 2555 NE2 GLN A 334 13.086 -16.606 -25.937 1.00 77.74 N
ANISOU 2555 NE2 GLN A 334 10992 10225 8320 1265 2897 -3215 N
ATOM 2556 N GLU A 335 15.594 -11.962 -23.430 1.00 69.11 N
ANISOU 2556 N GLU A 335 9030 9523 7708 1599 2811 -2239 N
ATOM 2557 CA GLU A 335 17.048 -11.888 -23.511 1.00 77.81 C
ANISOU 2557 CA GLU A 335 9923 10702 8938 1784 2942 -2270 C
ATOM 2558 C GLU A 335 17.706 -12.705 -22.406 1.00 76.05 C
ANISOU 2558 C GLU A 335 9612 10320 8965 1950 2890 -2347 C
ATOM 2559 O GLU A 335 18.702 -13.398 -22.644 1.00 81.26 O
ANISOU 2559 O GLU A 335 10223 10943 9711 2117 3021 -2491 O
ATOM 2560 CB GLU A 335 17.500 -10.431 -23.441 1.00 73.80 C
ANISOU 2560 CB GLU A 335 9174 10394 8472 1776 2914 -2050 C
ATOM 2561 CG GLU A 335 18.984 -10.241 -23.677 1.00 80.39 C
ANISOU 2561 CG GLU A 335 9786 11330 9427 1942 3059 -2070 C
ATOM 2562 CD GLU A 335 19.365 -8.783 -23.829 1.00 87.29 C
ANISOU 2562 CD GLU A 335 10433 12425 10309 1894 3003 -1853 C
ATOM 2563 OE1 GLU A 335 18.565 -7.913 -23.420 1.00 86.74 O
ANISOU 2563 OE1 GLU A 335 10337 12405 10215 1760 2818 -1679 O
ATOM 2564 OE2 GLU A 335 20.459 -8.507 -24.364 1.00 93.04 O
ANISOU 2564 OE2 GLU A 335 11002 13274 11075 1987 3140 -1862 O
ATOM 2565 N ILE A 336 17.164 -12.633 -21.190 1.00 71.25 N
ANISOU 2565 N ILE A 336 8987 9613 8473 1917 2699 -2247 N
ATOM 2566 CA ILE A 336 17.710 -13.418 -20.086 1.00 70.20 C
ANISOU 2566 CA ILE A 336 8799 9313 8560 2082 2627 -2297 C
ATOM 2567 C ILE A 336 17.154 -14.837 -20.081 1.00 67.09 C
ANISOU 2567 C ILE A 336 8616 8724 8150 2090 2614 -2511 C
ATOM 2568 O ILE A 336 17.823 -15.764 -19.611 1.00 83.87 O
ANISOU 2568 O ILE A 336 10731 10702 10435 2271 2623 -2617 O
ATOM 2569 CB ILE A 336 17.441 -12.720 -18.742 1.00 68.91 C
ANISOU 2569 CB ILE A 336 8531 9129 8523 2055 2429 -2094 C
ATOM 2570 CG1 ILE A 336 17.895 -13.618 -17.590 1.00 70.42 C
ANISOU 2570 CG1 ILE A 336 8715 9123 8917 2222 2343 -2137 C
ATOM 2571 CG2 ILE A 336 15.956 -12.365 -18.597 1.00 73.26 C
ANISOU 2571 CG2 ILE A 336 9219 9673 8945 1832 2308 -2021 C
ATOM 2572 CD1 ILE A 336 18.041 -12.899 -16.274 1.00 74.24 C
ANISOU 2572 CD1 ILE A 336 9069 9607 9531 2236 2156 -1919 C
ATOM 2573 N GLN A 337 15.932 -15.035 -20.579 1.00 66.74 N
ANISOU 2573 N GLN A 337 8760 8670 7929 1897 2578 -2574 N
ATOM 2574 CA GLN A 337 15.370 -16.380 -20.623 1.00 77.60 C
ANISOU 2574 CA GLN A 337 10312 9879 9293 1895 2541 -2796 C
ATOM 2575 C GLN A 337 16.179 -17.293 -21.533 1.00 88.91 C
ANISOU 2575 C GLN A 337 11788 11283 10710 2032 2720 -3028 C
ATOM 2576 O GLN A 337 16.230 -18.507 -21.307 1.00 86.79 O
ANISOU 2576 O GLN A 337 11607 10838 10530 2143 2696 -3209 O
ATOM 2577 CB GLN A 337 13.917 -16.323 -21.091 1.00 75.34 C
ANISOU 2577 CB GLN A 337 10178 9628 8818 1645 2455 -2826 C
ATOM 2578 CG GLN A 337 13.180 -17.644 -20.967 1.00 71.68 C
ANISOU 2578 CG GLN A 337 9858 9018 8358 1647 2343 -3048 C
ATOM 2579 CD GLN A 337 11.754 -17.564 -21.470 1.00 78.39 C
ANISOU 2579 CD GLN A 337 10810 9957 9016 1436 2217 -3099 C
ATOM 2580 OE1 GLN A 337 11.452 -16.813 -22.397 1.00 74.03 O
ANISOU 2580 OE1 GLN A 337 10273 9562 8292 1266 2290 -3047 O
ATOM 2581 NE2 GLN A 337 10.868 -18.336 -20.854 1.00 79.57 N
ANISOU 2581 NE2 GLN A 337 11054 9983 9196 1460 2022 -3178 N
ATOM 2582 N ARG A 338 16.821 -16.730 -22.560 1.00 83.43 N
ANISOU 2582 N ARG A 338 11041 10750 9909 2038 2901 -3023 N
ATOM 2583 CA ARG A 338 17.605 -17.549 -23.479 1.00 73.32 C
ANISOU 2583 CA ARG A 338 9798 9456 8605 2163 3093 -3251 C
ATOM 2584 C ARG A 338 18.747 -18.245 -22.753 1.00 81.68 C
ANISOU 2584 C ARG A 338 10736 10373 9926 2428 3119 -3309 C
ATOM 2585 O ARG A 338 18.985 -19.442 -22.956 1.00 93.69 O
ANISOU 2585 O ARG A 338 12347 11750 11502 2544 3173 -3534 O
ATOM 2586 CB ARG A 338 18.142 -16.684 -24.619 1.00 70.68 C
ANISOU 2586 CB ARG A 338 9413 9330 8114 2130 3287 -3197 C
ATOM 2587 N ALA A 339 19.460 -17.517 -21.892 1.00 78.48 N
ANISOU 2587 N ALA A 339 10127 10001 9693 2529 3068 -3108 N
ATOM 2588 CA ALA A 339 20.561 -18.127 -21.156 1.00 87.16 C
ANISOU 2588 CA ALA A 339 11105 10959 11052 2777 3075 -3136 C
ATOM 2589 C ALA A 339 20.066 -19.199 -20.195 1.00 87.90 C
ANISOU 2589 C ALA A 339 11332 10795 11271 2834 2918 -3199 C
ATOM 2590 O ALA A 339 20.775 -20.181 -19.946 1.00 89.55 O
ANISOU 2590 O ALA A 339 11542 10830 11655 3033 2955 -3318 O
ATOM 2591 CB ALA A 339 21.345 -17.059 -20.395 1.00 81.76 C
ANISOU 2591 CB ALA A 339 10171 10376 10520 2846 3017 -2897 C
ATOM 2592 N LEU A 340 18.860 -19.033 -19.647 1.00 89.77 N
ANISOU 2592 N LEU A 340 11683 10996 11431 2668 2745 -3116 N
ATOM 2593 CA LEU A 340 18.335 -20.017 -18.706 1.00100.91 C
ANISOU 2593 CA LEU A 340 13228 12158 12955 2714 2592 -3159 C
ATOM 2594 C LEU A 340 18.160 -21.375 -19.376 1.00 98.02 C
ANISOU 2594 C LEU A 340 13041 11637 12564 2766 2658 -3435 C
ATOM 2595 O LEU A 340 18.587 -22.406 -18.841 1.00 94.19 O
ANISOU 2595 O LEU A 340 12605 10920 12262 2942 2636 -3516 O
ATOM 2596 CB LEU A 340 17.008 -19.525 -18.123 1.00 76.48 C
ANISOU 2596 CB LEU A 340 10215 9080 9763 2506 2411 -3029 C
ATOM 2597 N TRP A 341 17.530 -21.397 -20.549 1.00 90.93 N
ANISOU 2597 N TRP A 341 12247 10860 11443 2614 2732 -3581 N
ATOM 2598 CA TRP A 341 17.344 -22.624 -21.312 1.00100.97 C
ANISOU 2598 CA TRP A 341 13685 12014 12666 2651 2793 -3864 C
ATOM 2599 C TRP A 341 18.526 -22.924 -22.224 1.00111.95 C
ANISOU 2599 C TRP A 341 15008 13452 14078 2806 3026 -4025 C
ATOM 2600 O TRP A 341 18.504 -23.936 -22.933 1.00102.53 O
ANISOU 2600 O TRP A 341 13941 12170 12846 2854 3101 -4281 O
ATOM 2601 CB TRP A 341 16.051 -22.542 -22.139 1.00 97.77 C
ANISOU 2601 CB TRP A 341 13426 11725 11998 2417 2733 -3959 C
ATOM 2602 CG TRP A 341 14.792 -22.757 -21.334 1.00106.16 C
ANISOU 2602 CG TRP A 341 14613 12667 13055 2315 2502 -3895 C
ATOM 2603 CD1 TRP A 341 14.710 -23.164 -20.033 1.00104.36 C
ANISOU 2603 CD1 TRP A 341 14415 12214 13023 2404 2369 -3790 C
ATOM 2604 CD2 TRP A 341 13.441 -22.577 -21.782 1.00114.70 C
ANISOU 2604 CD2 TRP A 341 15807 13846 13928 2109 2376 -3926 C
ATOM 2605 NE1 TRP A 341 13.395 -23.249 -19.644 1.00108.41 N
ANISOU 2605 NE1 TRP A 341 15061 12666 13463 2262 2188 -3753 N
ATOM 2606 CE2 TRP A 341 12.596 -22.893 -20.698 1.00112.48 C
ANISOU 2606 CE2 TRP A 341 15621 13379 13739 2087 2180 -3837 C
ATOM 2607 CE3 TRP A 341 12.864 -22.178 -22.992 1.00111.65 C
ANISOU 2607 CE3 TRP A 341 15448 13686 13286 1946 2400 -4016 C
ATOM 2608 CZ2 TRP A 341 11.206 -22.823 -20.789 1.00114.28 C
ANISOU 2608 CZ2 TRP A 341 15964 13632 13825 1919 2012 -3833 C
ATOM 2609 CZ3 TRP A 341 11.483 -22.109 -23.080 1.00109.84 C
ANISOU 2609 CZ3 TRP A 341 15320 13502 12912 1794 2204 -4014 C
ATOM 2610 CH2 TRP A 341 10.671 -22.430 -21.985 1.00110.12 C
ANISOU 2610 CH2 TRP A 341 15446 13337 13057 1786 2016 -3923 C
ATOM 2611 N LEU A 342 19.559 -22.078 -22.213 1.00102.78 N
ANISOU 2611 N LEU A 342 13643 12426 12982 2890 3139 -3886 N
ATOM 2612 CA LEU A 342 20.749 -22.353 -23.010 1.00 99.36 C
ANISOU 2612 CA LEU A 342 13122 12035 12596 3053 3368 -4030 C
ATOM 2613 C LEU A 342 21.370 -23.684 -22.613 1.00114.67 C
ANISOU 2613 C LEU A 342 15096 13705 14767 3287 3382 -4195 C
ATOM 2614 O LEU A 342 21.815 -24.454 -23.472 1.00125.99 O
ANISOU 2614 O LEU A 342 16580 15102 16188 3378 3546 -4438 O
ATOM 2615 CB LEU A 342 21.763 -21.220 -22.842 1.00 96.34 C
ANISOU 2615 CB LEU A 342 12487 11821 12296 3122 3446 -3824 C
ATOM 2616 CG LEU A 342 23.032 -21.287 -23.696 1.00 88.39 C
ANISOU 2616 CG LEU A 342 11349 10901 11336 3277 3694 -3942 C
ATOM 2617 CD1 LEU A 342 22.794 -20.647 -25.055 1.00 88.12 C
ANISOU 2617 CD1 LEU A 342 11362 11104 11014 3111 3863 -3992 C
ATOM 2618 CD2 LEU A 342 24.195 -20.621 -22.977 1.00 86.90 C
ANISOU 2618 CD2 LEU A 342 10884 10756 11379 3435 3693 -3750 C
ATOM 2619 N LEU A 343 21.400 -23.975 -21.316 1.00108.05 N
ANISOU 2619 N LEU A 343 14240 12670 14143 3384 3215 -4065 N
ATOM 2620 CA LEU A 343 22.025 -25.194 -20.810 1.00114.56 C
ANISOU 2620 CA LEU A 343 15094 13213 15220 3612 3213 -4177 C
ATOM 2621 C LEU A 343 20.995 -26.310 -20.909 1.00122.69 C
ANISOU 2621 C LEU A 343 16385 14040 16191 3547 3124 -4360 C
ATOM 2622 O LEU A 343 20.041 -26.359 -20.130 1.00111.39 O
ANISOU 2622 O LEU A 343 15065 12508 14750 3440 2930 -4253 O
ATOM 2623 CB LEU A 343 22.508 -24.992 -19.379 1.00104.29 C
ANISOU 2623 CB LEU A 343 13671 11791 14164 3734 3064 -3939 C
ATOM 2624 CG LEU A 343 23.046 -23.589 -19.075 1.00106.24 C
ANISOU 2624 CG LEU A 343 13680 12271 14414 3707 3058 -3696 C
ATOM 2625 CD1 LEU A 343 23.548 -23.507 -17.646 1.00 94.55 C
ANISOU 2625 CD1 LEU A 343 12090 10658 13179 3835 2896 -3484 C
ATOM 2626 CD2 LEU A 343 24.146 -23.194 -20.054 1.00116.54 C
ANISOU 2626 CD2 LEU A 343 14804 13758 15718 3794 3286 -3771 C
ATOM 2627 N LEU A 344 21.180 -27.206 -21.880 1.00129.72 N
ANISOU 2627 N LEU A 344 17371 14870 17045 3609 3266 -4641 N
ATOM 2628 CA LEU A 344 20.193 -28.231 -22.189 1.00130.49 C
ANISOU 2628 CA LEU A 344 17715 14803 17062 3534 3190 -4846 C
ATOM 2629 C LEU A 344 20.712 -29.656 -22.073 1.00137.45 C
ANISOU 2629 C LEU A 344 18686 15372 18168 3748 3232 -5042 C
ATOM 2630 O LEU A 344 19.921 -30.552 -21.772 1.00138.16 O
ANISOU 2630 O LEU A 344 18982 15229 18285 3728 3104 -5124 O
ATOM 2631 CB LEU A 344 19.647 -28.024 -23.612 1.00124.14 C
ANISOU 2631 CB LEU A 344 16994 14226 15948 3367 3292 -5038 C
ATOM 2632 N ASP A 345 22.003 -29.895 -22.299 1.00144.78 N
ANISOU 2632 N ASP A 345 19471 16275 19265 3962 3407 -5115 N
ATOM 2633 CA ASP A 345 22.536 -31.250 -22.299 1.00142.50 C
ANISOU 2633 CA ASP A 345 19257 15689 19196 4169 3467 -5319 C
ATOM 2634 C ASP A 345 24.001 -31.220 -21.887 1.00146.29 C
ANISOU 2634 C ASP A 345 19511 16118 19953 4419 3577 -5240 C
ATOM 2635 O ASP A 345 24.643 -30.167 -21.882 1.00151.53 O
ANISOU 2635 O ASP A 345 19962 17011 20602 4425 3643 -5082 O
ATOM 2636 CB ASP A 345 22.384 -31.909 -23.674 1.00140.62 C
ANISOU 2636 CB ASP A 345 19146 15488 18795 4145 3622 -5664 C
ATOM 2637 N GLY A 346 24.520 -32.395 -21.539 1.00142.29 N
ANISOU 2637 N GLY A 346 19050 15300 19713 4624 3589 -5346 N
ATOM 2638 CA GLY A 346 25.907 -32.539 -21.129 1.00131.67 C
ANISOU 2638 CA GLY A 346 17495 13866 18668 4879 3680 -5286 C
ATOM 2639 C GLY A 346 26.890 -32.060 -22.178 1.00128.83 C
ANISOU 2639 C GLY A 346 16942 13747 18260 4951 3935 -5411 C
ATOM 2640 O GLY A 346 28.093 -31.986 -21.926 1.00134.16 O
ANISOU 2640 O GLY A 346 17399 14403 19173 5149 4023 -5348 O
TER 2641 GLY A 346
HETATM 2642 C01 XY8 A1201 12.979 -10.467 3.784 1.00 38.54 C
HETATM 2643 C02 XY8 A1201 12.141 -10.727 5.030 1.00 44.83 C
HETATM 2644 C03 XY8 A1201 10.663 -10.441 4.767 1.00 46.90 C
HETATM 2645 C05 XY8 A1201 12.503 -10.144 7.465 1.00 44.11 C
HETATM 2646 C07 XY8 A1201 12.167 -11.704 9.173 1.00 51.68 C
HETATM 2647 C08 XY8 A1201 12.248 -10.672 10.119 1.00 59.97 C
HETATM 2648 C09 XY8 A1201 12.108 -11.020 11.459 1.00 63.19 C
HETATM 2649 C11 XY8 A1201 11.826 -13.258 10.983 1.00 63.88 C
HETATM 2650 C12 XY8 A1201 11.597 -14.655 11.472 1.00 69.54 C
HETATM 2651 C13 XY8 A1201 11.954 -13.010 9.615 1.00 55.68 C
HETATM 2652 C15 XY8 A1201 12.585 -9.106 8.417 1.00 40.91 C
HETATM 2653 C17 XY8 A1201 13.440 -6.886 9.019 1.00 43.01 C
HETATM 2654 C18 XY8 A1201 13.855 -5.565 8.376 1.00 41.48 C
HETATM 2655 C20 XY8 A1201 12.938 -3.525 7.186 1.00 39.92 C
HETATM 2656 C21 XY8 A1201 11.669 -2.746 6.949 1.00 43.51 C
HETATM 2657 C22 XY8 A1201 11.154 -1.875 7.919 1.00 39.10 C
HETATM 2658 C24 XY8 A1201 9.977 -1.168 7.706 1.00 33.29 C
HETATM 2659 C25 XY8 A1201 9.298 -1.338 6.507 1.00 30.96 C
HETATM 2660 C27 XY8 A1201 9.778 -2.196 5.528 1.00 37.18 C
HETATM 2661 C28 XY8 A1201 10.959 -2.897 5.752 1.00 42.66 C
HETATM 2662 C29 XY8 A1201 12.092 -5.854 6.659 1.00 32.87 C
HETATM 2663 C30 XY8 A1201 11.653 -7.143 7.337 1.00 35.26 C
HETATM 2664 F23 XY8 A1201 11.805 -1.707 9.082 1.00 43.46 F
HETATM 2665 F26 XY8 A1201 8.160 -0.664 6.284 1.00 30.38 F
HETATM 2666 N04 XY8 A1201 12.638 -9.843 6.089 1.00 40.47 N
HETATM 2667 N06 XY8 A1201 12.295 -11.424 7.860 1.00 49.34 N
HETATM 2668 N10 XY8 A1201 11.901 -12.275 11.909 1.00 67.28 N
HETATM 2669 N14 XY8 A1201 12.453 -9.396 9.735 1.00 50.08 N
HETATM 2670 N16 XY8 A1201 12.797 -7.754 8.018 1.00 37.51 N
HETATM 2671 N19 XY8 A1201 12.657 -4.923 7.710 1.00 31.74 N
HETATM 2672 NA NA A1202 12.167 -7.520 -3.533 1.00 55.45 NA
HETATM 2673 O HOH A1301 4.696 -7.815 3.466 1.00 31.35 O
HETATM 2674 O HOH A1302 16.106 -0.136 15.210 1.00 38.11 O
HETATM 2675 O HOH A1303 1.221 0.338 18.281 1.00 44.49 O
HETATM 2676 O HOH A1304 14.297 -8.234 1.399 1.00 39.07 O
HETATM 2677 O HOH A1305 3.759 15.759 -68.321 1.00 38.25 O
CONECT 357 2672
CONECT 1044 1089
CONECT 1089 1044
CONECT 2445 2672
CONECT 2642 2643
CONECT 2643 2642 2644 2666
CONECT 2644 2643
CONECT 2645 2652 2666 2667
CONECT 2646 2647 2651 2667
CONECT 2647 2646 2648 2669
CONECT 2648 2647 2668
CONECT 2649 2650 2651 2668
CONECT 2650 2649
CONECT 2651 2646 2649
CONECT 2652 2645 2669 2670
CONECT 2653 2654 2670
CONECT 2654 2653 2671
CONECT 2655 2656 2671
CONECT 2656 2655 2657 2661
CONECT 2657 2656 2658 2664
CONECT 2658 2657 2659
CONECT 2659 2658 2660 2665
CONECT 2660 2659 2661
CONECT 2661 2656 2660
CONECT 2662 2663 2671
CONECT 2663 2662 2670
CONECT 2664 2657
CONECT 2665 2659
CONECT 2666 2643 2645
CONECT 2667 2645 2646
CONECT 2668 2648 2649
CONECT 2669 2647 2652
CONECT 2670 2652 2653 2663
CONECT 2671 2654 2655 2662
CONECT 2672 357 2445
MASTER 406 0 2 12 0 0 0 6 2671 1 35 35
END