***  7UJC   ***
Job options:
ID = 240508194650189588
JOBID = 7UJC
USERID = unknown
PRIVAT = 0
NMODES = 5
DQMIN = -100
DQMAX = 100
DQSTEP = 20
DOGRAPHS = on
DOPROJMODS = 0
DORMSD = 0
NRBL = 0
CUTOFF = 0
CAONLY = 0
Input data for this run:
HEADER 7UJC
HEADER TRANSCRIPTION 30-MAR-22 7UJC
TITLE RALOXIFENE IN COMPLEX WITH ESTROGEN RECEPTOR ALPHA LIGAND BINDING
TITLE 2 DOMAIN Y537S MUTATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTROGEN RECEPTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ER,ER-ALPHA,ESTRADIOL RECEPTOR,NUCLEAR RECEPTOR SUBFAMILY 3
COMPND 5 GROUP A MEMBER 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ESR1, ESR, NR3A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA HELICAL BUNDLE, HORMONE RECEPTOR, BREAST CANCER, ACTIVATING
KEYWDS 2 MUTATION, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.HOSFIELD,G.L.GREENE,S.W.FANNING
REVDAT 2 18-OCT-23 7UJC 1 REMARK
REVDAT 1 15-JUN-22 7UJC 0
SPRSDE 15-JUN-22 7UJC 7KCA
JRNL AUTH D.J.HOSFIELD,S.WEBER,N.S.LI,M.SUAVAGE,C.F.JOINER,
JRNL AUTH 2 G.R.HANCOCK,E.A.SULLIVAN,E.NDUKWE,R.HAN,S.CUSH,M.LAINE,
JRNL AUTH 3 S.C.MADER,G.L.GREENE,S.W.FANNING
JRNL TITL STEREOSPECIFIC LASOFOXIFENE DERIVATIVES REVEAL THE INTERPLAY
JRNL TITL 2 BETWEEN ESTROGEN RECEPTOR ALPHA STABILITY AND ANTAGONISTIC
JRNL TITL 3 ACTIVITY IN ESR1 MUTANT BREAST CANCER CELLS.
JRNL REF ELIFE V. 11 2022
JRNL REFN ESSN 2050-084X
JRNL PMID 35575456
JRNL DOI 10.7554/ELIFE.72512
REMARK 2
REMARK 2 RESOLUTION. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.18.2_3874
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.3
REMARK 3 NUMBER OF REFLECTIONS : 39306
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.220
REMARK 3 FREE R VALUE TEST SET COUNT : 2051
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 29.1800 - 4.4000 0.90 2802 158 0.1840 0.2094
REMARK 3 2 4.4000 - 3.4900 0.96 2926 169 0.1606 0.2010
REMARK 3 3 3.4900 - 3.0500 0.99 3011 152 0.1864 0.2408
REMARK 3 4 3.0500 - 2.7700 0.99 2993 168 0.1959 0.2174
REMARK 3 5 2.7700 - 2.5700 0.99 2966 172 0.1910 0.2384
REMARK 3 6 2.5700 - 2.4200 0.99 3024 163 0.1867 0.2353
REMARK 3 7 2.4200 - 2.3000 0.99 3006 162 0.1978 0.2324
REMARK 3 8 2.3000 - 2.2000 0.95 2829 163 0.2061 0.2854
REMARK 3 9 2.2000 - 2.1200 0.90 2705 139 0.2111 0.2291
REMARK 3 10 2.1200 - 2.0400 0.83 2484 142 0.2233 0.2522
REMARK 3 11 2.0400 - 1.9800 0.75 2235 117 0.2227 0.2343
REMARK 3 12 1.9800 - 1.9200 0.65 1944 113 0.2218 0.2657
REMARK 3 13 1.9200 - 1.8700 0.56 1678 98 0.2364 0.2879
REMARK 3 14 1.8700 - 1.8300 0.50 1500 78 0.2387 0.2790
REMARK 3 15 1.8300 - 1.7800 0.38 1152 57 0.2544 0.3169
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.980
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 306 THROUGH 549)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3441 -21.5663 22.5252
REMARK 3 T TENSOR
REMARK 3 T11: 0.1262 T22: 0.0900
REMARK 3 T33: 0.1257 T12: 0.0485
REMARK 3 T13: -0.0042 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 2.5374 L22: 1.1669
REMARK 3 L33: 2.3689 L12: 0.0034
REMARK 3 L13: -0.3826 L23: -0.2415
REMARK 3 S TENSOR
REMARK 3 S11: -0.0340 S12: 0.2119 S13: -0.0026
REMARK 3 S21: 0.0555 S22: 0.0118 S23: -0.0264
REMARK 3 S31: 0.0060 S32: -0.0762 S33: -0.0131
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND RESID 306 THROUGH 546)
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1241 -33.6387 23.2919
REMARK 3 T TENSOR
REMARK 3 T11: 0.1509 T22: 0.2663
REMARK 3 T33: 0.1558 T12: 0.0616
REMARK 3 T13: 0.0240 T23: 0.0557
REMARK 3 L TENSOR
REMARK 3 L11: 2.1972 L22: 3.8610
REMARK 3 L33: 0.8818 L12: -1.3978
REMARK 3 L13: 0.0970 L23: 0.2865
REMARK 3 S TENSOR
REMARK 3 S11: 0.0110 S12: 0.0985 S13: 0.1596
REMARK 3 S21: 0.0555 S22: -0.1130 S23: -0.2531
REMARK 3 S31: 0.0689 S32: 0.2137 S33: 0.0484
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 7UJC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-22.
REMARK 100 THE DEPOSITION ID IS D_1000264272.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUN-19
REMARK 200 TEMPERATURE (KELVIN) : 100
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 : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39306
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.780
REMARK 200 RESOLUTION RANGE LOW (A) : 29.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 2.4700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.82
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 5UFX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8,000, MGCL2, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 51.27850
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.92050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 51.27850
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.92050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 GLU A 298
REMARK 465 ASN A 299
REMARK 465 LEU A 300
REMARK 465 TYR A 301
REMARK 465 PHE A 302
REMARK 465 GLN A 303
REMARK 465 SER A 304
REMARK 465 MET A 305
REMARK 465 ASP A 332
REMARK 465 PRO A 333
REMARK 465 THR A 334
REMARK 465 ARG A 335
REMARK 465 PRO A 336
REMARK 465 LEU A 462
REMARK 465 SER A 463
REMARK 465 SER A 464
REMARK 465 LYS A 529
REMARK 465 SER A 530
REMARK 465 LYS A 531
REMARK 465 ASN A 532
REMARK 465 VAL A 533
REMARK 465 VAL A 534
REMARK 465 PRO A 535
REMARK 465 HIS A 550
REMARK 465 ALA A 551
REMARK 465 PRO A 552
REMARK 465 THR A 553
REMARK 465 SER A 554
REMARK 465 HIS B 292
REMARK 465 HIS B 293
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 GLU B 298
REMARK 465 ASN B 299
REMARK 465 LEU B 300
REMARK 465 TYR B 301
REMARK 465 PHE B 302
REMARK 465 GLN B 303
REMARK 465 SER B 304
REMARK 465 MET B 305
REMARK 465 PRO B 333
REMARK 465 THR B 334
REMARK 465 ARG B 335
REMARK 465 PRO B 336
REMARK 465 PHE B 337
REMARK 465 SER B 338
REMARK 465 GLU B 339
REMARK 465 ALA B 340
REMARK 465 THR B 460
REMARK 465 PHE B 461
REMARK 465 LEU B 462
REMARK 465 SER B 463
REMARK 465 SER B 464
REMARK 465 THR B 465
REMARK 465 LEU B 466
REMARK 465 LYS B 467
REMARK 465 SER B 468
REMARK 465 LEU B 469
REMARK 465 LYS B 529
REMARK 465 SER B 530
REMARK 465 LYS B 531
REMARK 465 ASN B 532
REMARK 465 VAL B 533
REMARK 465 VAL B 534
REMARK 465 HIS B 547
REMARK 465 ARG B 548
REMARK 465 LEU B 549
REMARK 465 HIS B 550
REMARK 465 ALA B 551
REMARK 465 PRO B 552
REMARK 465 THR B 553
REMARK 465 SER B 554
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 306 CG CD1 CD2
REMARK 470 GLU A 339 CG CD OE1 OE2
REMARK 470 VAL A 418 CG2
REMARK 470 MET A 437 CG SD CE
REMARK 470 THR A 460 CG2
REMARK 470 ARG A 477 CZ NH1 NH2
REMARK 470 LYS A 481 CD CE NZ
REMARK 470 ASP A 538 CG OD1 OD2
REMARK 470 LEU A 541 CG CD1 CD2
REMARK 470 ARG A 548 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 323 CG CD OE1 OE2
REMARK 470 TYR B 331 CD1 CE1
REMARK 470 ASP B 332 CG OD1 OD2
REMARK 470 LYS B 362 CE NZ
REMARK 470 GLU B 397 CG CD OE1 OE2
REMARK 470 LYS B 416 NZ
REMARK 470 GLU B 419 CG CD OE1 OE2
REMARK 470 GLU B 423 CG CD OE1 OE2
REMARK 470 MET B 437 CG SD CE
REMARK 470 GLU B 470 CG CD OE1 OE2
REMARK 470 GLU B 471 CG CD OE1 OE2
REMARK 470 LYS B 472 CG CD CE NZ
REMARK 470 ARG B 477 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 526 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP B 545 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 B 408 67.07 -152.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 877 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A 878 DISTANCE = 6.20 ANGSTROMS
DBREF 7UJC A 306 554 UNP P03372 ESR1_HUMAN 306 554
DBREF 7UJC B 306 554 UNP P03372 ESR1_HUMAN 306 554
SEQADV 7UJC HIS A 292 UNP P03372 EXPRESSION TAG
SEQADV 7UJC HIS A 293 UNP P03372 EXPRESSION TAG
SEQADV 7UJC HIS A 294 UNP P03372 EXPRESSION TAG
SEQADV 7UJC HIS A 295 UNP P03372 EXPRESSION TAG
SEQADV 7UJC HIS A 296 UNP P03372 EXPRESSION TAG
SEQADV 7UJC HIS A 297 UNP P03372 EXPRESSION TAG
SEQADV 7UJC GLU A 298 UNP P03372 EXPRESSION TAG
SEQADV 7UJC ASN A 299 UNP P03372 EXPRESSION TAG
SEQADV 7UJC LEU A 300 UNP P03372 EXPRESSION TAG
SEQADV 7UJC TYR A 301 UNP P03372 EXPRESSION TAG
SEQADV 7UJC PHE A 302 UNP P03372 EXPRESSION TAG
SEQADV 7UJC GLN A 303 UNP P03372 EXPRESSION TAG
SEQADV 7UJC SER A 304 UNP P03372 EXPRESSION TAG
SEQADV 7UJC MET A 305 UNP P03372 EXPRESSION TAG
SEQADV 7UJC SER A 381 UNP P03372 CYS 381 CONFLICT
SEQADV 7UJC SER A 417 UNP P03372 CYS 417 CONFLICT
SEQADV 7UJC SER A 530 UNP P03372 CYS 530 CONFLICT
SEQADV 7UJC SER A 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQADV 7UJC HIS B 292 UNP P03372 EXPRESSION TAG
SEQADV 7UJC HIS B 293 UNP P03372 EXPRESSION TAG
SEQADV 7UJC HIS B 294 UNP P03372 EXPRESSION TAG
SEQADV 7UJC HIS B 295 UNP P03372 EXPRESSION TAG
SEQADV 7UJC HIS B 296 UNP P03372 EXPRESSION TAG
SEQADV 7UJC HIS B 297 UNP P03372 EXPRESSION TAG
SEQADV 7UJC GLU B 298 UNP P03372 EXPRESSION TAG
SEQADV 7UJC ASN B 299 UNP P03372 EXPRESSION TAG
SEQADV 7UJC LEU B 300 UNP P03372 EXPRESSION TAG
SEQADV 7UJC TYR B 301 UNP P03372 EXPRESSION TAG
SEQADV 7UJC PHE B 302 UNP P03372 EXPRESSION TAG
SEQADV 7UJC GLN B 303 UNP P03372 EXPRESSION TAG
SEQADV 7UJC SER B 304 UNP P03372 EXPRESSION TAG
SEQADV 7UJC MET B 305 UNP P03372 EXPRESSION TAG
SEQADV 7UJC SER B 381 UNP P03372 CYS 381 CONFLICT
SEQADV 7UJC SER B 417 UNP P03372 CYS 417 CONFLICT
SEQADV 7UJC SER B 530 UNP P03372 CYS 530 CONFLICT
SEQADV 7UJC SER B 537 UNP P03372 TYR 537 ENGINEERED MUTATION
SEQRES 1 A 263 HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN SER
SEQRES 2 A 263 MET LEU ALA LEU SER LEU THR ALA ASP GLN MET VAL SER
SEQRES 3 A 263 ALA LEU LEU ASP ALA GLU PRO PRO ILE LEU TYR SER GLU
SEQRES 4 A 263 TYR ASP PRO THR ARG PRO PHE SER GLU ALA SER MET MET
SEQRES 5 A 263 GLY LEU LEU THR ASN LEU ALA ASP ARG GLU LEU VAL HIS
SEQRES 6 A 263 MET ILE ASN TRP ALA LYS ARG VAL PRO GLY PHE VAL ASP
SEQRES 7 A 263 LEU THR LEU HIS ASP GLN VAL HIS LEU LEU GLU SER ALA
SEQRES 8 A 263 TRP LEU GLU ILE LEU MET ILE GLY LEU VAL TRP ARG SER
SEQRES 9 A 263 MET GLU HIS PRO GLY LYS LEU LEU PHE ALA PRO ASN LEU
SEQRES 10 A 263 LEU LEU ASP ARG ASN GLN GLY LYS SER VAL GLU GLY MET
SEQRES 11 A 263 VAL GLU ILE PHE ASP MET LEU LEU ALA THR SER SER ARG
SEQRES 12 A 263 PHE ARG MET MET ASN LEU GLN GLY GLU GLU PHE VAL CYS
SEQRES 13 A 263 LEU LYS SER ILE ILE LEU LEU ASN SER GLY VAL TYR THR
SEQRES 14 A 263 PHE LEU SER SER THR LEU LYS SER LEU GLU GLU LYS ASP
SEQRES 15 A 263 HIS ILE HIS ARG VAL LEU ASP LYS ILE THR ASP THR LEU
SEQRES 16 A 263 ILE HIS LEU MET ALA LYS ALA GLY LEU THR LEU GLN GLN
SEQRES 17 A 263 GLN HIS GLN ARG LEU ALA GLN LEU LEU LEU ILE LEU SER
SEQRES 18 A 263 HIS ILE ARG HIS MET SER ASN LYS GLY MET GLU HIS LEU
SEQRES 19 A 263 TYR SER MET LYS SER LYS ASN VAL VAL PRO LEU SER ASP
SEQRES 20 A 263 LEU LEU LEU GLU MET LEU ASP ALA HIS ARG LEU HIS ALA
SEQRES 21 A 263 PRO THR SER
SEQRES 1 B 263 HIS HIS HIS HIS HIS HIS GLU ASN LEU TYR PHE GLN SER
SEQRES 2 B 263 MET LEU ALA LEU SER LEU THR ALA ASP GLN MET VAL SER
SEQRES 3 B 263 ALA LEU LEU ASP ALA GLU PRO PRO ILE LEU TYR SER GLU
SEQRES 4 B 263 TYR ASP PRO THR ARG PRO PHE SER GLU ALA SER MET MET
SEQRES 5 B 263 GLY LEU LEU THR ASN LEU ALA ASP ARG GLU LEU VAL HIS
SEQRES 6 B 263 MET ILE ASN TRP ALA LYS ARG VAL PRO GLY PHE VAL ASP
SEQRES 7 B 263 LEU THR LEU HIS ASP GLN VAL HIS LEU LEU GLU SER ALA
SEQRES 8 B 263 TRP LEU GLU ILE LEU MET ILE GLY LEU VAL TRP ARG SER
SEQRES 9 B 263 MET GLU HIS PRO GLY LYS LEU LEU PHE ALA PRO ASN LEU
SEQRES 10 B 263 LEU LEU ASP ARG ASN GLN GLY LYS SER VAL GLU GLY MET
SEQRES 11 B 263 VAL GLU ILE PHE ASP MET LEU LEU ALA THR SER SER ARG
SEQRES 12 B 263 PHE ARG MET MET ASN LEU GLN GLY GLU GLU PHE VAL CYS
SEQRES 13 B 263 LEU LYS SER ILE ILE LEU LEU ASN SER GLY VAL TYR THR
SEQRES 14 B 263 PHE LEU SER SER THR LEU LYS SER LEU GLU GLU LYS ASP
SEQRES 15 B 263 HIS ILE HIS ARG VAL LEU ASP LYS ILE THR ASP THR LEU
SEQRES 16 B 263 ILE HIS LEU MET ALA LYS ALA GLY LEU THR LEU GLN GLN
SEQRES 17 B 263 GLN HIS GLN ARG LEU ALA GLN LEU LEU LEU ILE LEU SER
SEQRES 18 B 263 HIS ILE ARG HIS MET SER ASN LYS GLY MET GLU HIS LEU
SEQRES 19 B 263 TYR SER MET LYS SER LYS ASN VAL VAL PRO LEU SER ASP
SEQRES 20 B 263 LEU LEU LEU GLU MET LEU ASP ALA HIS ARG LEU HIS ALA
SEQRES 21 B 263 PRO THR SER
HET RAL A 601 34
HET RAL B 601 34
HETNAM RAL RALOXIFENE
FORMUL 3 RAL 2(C28 H27 N O4 S)
FORMUL 5 HOH *302(H2 O)
HELIX 1 1 LEU A 306 GLU A 323 1 18
HELIX 2 2 SER A 341 LYS A 362 1 22
HELIX 3 3 GLY A 366 MET A 396 1 31
HELIX 4 4 ARG A 412 SER A 417 1 6
HELIX 5 5 MET A 421 MET A 438 1 18
HELIX 6 6 GLN A 441 SER A 456 1 16
HELIX 7 7 LEU A 466 ALA A 493 1 28
HELIX 8 8 THR A 496 MET A 528 1 33
HELIX 9 9 SER A 537 ASP A 545 1 9
SHEET 1 1 1 LYS A 401 ALA A 405 0
SHEET 2 2 1 LEU A 408 ASP A 411 0
CRYST1 102.557 57.841 87.938 90.00 103.74 90.00 C 1 2 1 8
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 0.009751 0.000000 0.002384 0.00000
SCALE2 0.000000 0.017289 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011707 0.00000
ATOM 1 N LEU A 306 10.882 -5.547 5.683 1.00 51.28 N
ANISOU 1 N LEU A 306 6202 6979 6302 270 329 2236 N
ATOM 2 CA LEU A 306 9.925 -5.148 6.716 1.00 53.33 C
ANISOU 2 CA LEU A 306 6556 7029 6679 334 290 2173 C
ATOM 3 C LEU A 306 10.330 -5.624 8.130 1.00 46.78 C
ANISOU 3 C LEU A 306 5775 6045 5954 289 271 2025 C
ATOM 4 O LEU A 306 10.736 -4.816 8.974 1.00 47.59 O
ANISOU 4 O LEU A 306 5963 5913 6206 233 277 2019 O
ATOM 5 CB LEU A 306 8.526 -5.670 6.368 1.00 57.72 C
ANISOU 5 CB LEU A 306 7074 7726 7131 452 247 2131 C
ATOM 6 N ALA A 307 10.209 -6.932 8.386 1.00 44.60 N
ANISOU 6 N ALA A 307 5448 5902 5597 312 246 1902 N
ATOM 7 CA ALA A 307 10.519 -7.466 9.707 1.00 43.11 C
ANISOU 7 CA ALA A 307 5299 5584 5495 284 224 1770 C
ATOM 8 C ALA A 307 11.976 -7.230 10.085 1.00 44.05 C
ANISOU 8 C ALA A 307 5413 5622 5700 156 256 1794 C
ATOM 9 O ALA A 307 12.287 -7.022 11.268 1.00 35.45 O
ANISOU 9 O ALA A 307 4386 4341 4741 109 237 1721 O
ATOM 10 CB ALA A 307 10.215 -8.960 9.767 1.00 40.92 C
ANISOU 10 CB ALA A 307 4964 5480 5102 330 199 1653 C
ATOM 11 N LEU A 308 12.883 -7.255 9.105 1.00 39.40 N
ANISOU 11 N LEU A 308 4743 5189 5038 91 303 1886 N
ATOM 12 CA LEU A 308 14.288 -7.061 9.437 1.00 36.13 C
ANISOU 12 CA LEU A 308 4298 4726 4704 -43 336 1906 C
ATOM 13 C LEU A 308 14.612 -5.610 9.753 1.00 42.48 C
ANISOU 13 C LEU A 308 5183 5296 5661 -126 347 1979 C
ATOM 14 O LEU A 308 15.728 -5.326 10.204 1.00 45.66 O
ANISOU 14 O LEU A 308 5568 5625 6156 -257 363 1978 O
ATOM 15 CB LEU A 308 15.176 -7.564 8.293 1.00 39.34 C
ANISOU 15 CB LEU A 308 4580 5393 4976 -84 392 1963 C
ATOM 16 CG LEU A 308 15.164 -9.076 8.022 1.00 41.07 C
ANISOU 16 CG LEU A 308 4716 5850 5039 -25 398 1859 C
ATOM 17 CD1 LEU A 308 16.089 -9.465 6.861 1.00 41.95 C
ANISOU 17 CD1 LEU A 308 4709 6215 5017 -59 464 1889 C
ATOM 18 CD2 LEU A 308 15.560 -9.822 9.270 1.00 35.30 C
ANISOU 18 CD2 LEU A 308 3992 5025 4396 -41 357 1661 C
ATOM 19 N SER A 309 13.683 -4.688 9.506 1.00 38.89 N
ANISOU 19 N SER A 309 4813 4731 5233 -58 341 2039 N
ATOM 20 CA SER A 309 13.942 -3.276 9.720 1.00 42.86 C
ANISOU 20 CA SER A 309 5409 5004 5870 -128 360 2110 C
ATOM 21 C SER A 309 13.386 -2.783 11.044 1.00 43.63 C
ANISOU 21 C SER A 309 5634 4842 6100 -108 322 1994 C
ATOM 22 O SER A 309 13.624 -1.629 11.412 1.00 41.49 O
ANISOU 22 O SER A 309 5460 4355 5948 -175 337 2018 O
ATOM 23 CB SER A 309 13.362 -2.451 8.562 1.00 45.56 C
ANISOU 23 CB SER A 309 5768 5383 6161 -66 388 2268 C
ATOM 24 OG SER A 309 12.009 -2.142 8.830 1.00 49.16 O
ANISOU 24 OG SER A 309 6299 5748 6631 65 353 2240 O
ATOM 25 N LEU A 310 12.688 -3.642 11.776 1.00 38.36 N
ANISOU 25 N LEU A 310 4971 4195 5408 -23 277 1861 N
ATOM 26 CA LEU A 310 12.101 -3.248 13.043 1.00 37.94 C
ANISOU 26 CA LEU A 310 5034 3925 5456 8 242 1735 C
ATOM 27 C LEU A 310 13.191 -2.979 14.067 1.00 33.75 C
ANISOU 27 C LEU A 310 4540 3238 5047 -138 237 1654 C
ATOM 28 O LEU A 310 14.147 -3.754 14.196 1.00 36.81 O
ANISOU 28 O LEU A 310 4835 3727 5425 -226 231 1630 O
ATOM 29 CB LEU A 310 11.183 -4.359 13.567 1.00 36.59 C
ANISOU 29 CB LEU A 310 4842 3843 5217 122 199 1610 C
ATOM 30 CG LEU A 310 9.929 -4.696 12.748 1.00 37.87 C
ANISOU 30 CG LEU A 310 4965 4162 5264 260 191 1651 C
ATOM 31 CD1 LEU A 310 9.174 -5.809 13.393 1.00 39.53 C
ANISOU 31 CD1 LEU A 310 5154 4445 5422 337 152 1513 C
ATOM 32 CD2 LEU A 310 9.044 -3.466 12.558 1.00 37.73 C
ANISOU 32 CD2 LEU A 310 5025 4018 5292 331 199 1718 C
ATOM 33 N THR A 311 13.021 -1.896 14.827 1.00 36.27 N
ANISOU 33 N THR A 311 4989 3316 5476 -165 234 1603 N
ATOM 34 CA THR A 311 13.790 -1.697 16.048 1.00 39.12 C
ANISOU 34 CA THR A 311 5399 3522 5941 -290 212 1472 C
ATOM 35 C THR A 311 13.434 -2.747 17.112 1.00 34.45 C
ANISOU 35 C THR A 311 4795 2966 5327 -233 159 1309 C
ATOM 36 O THR A 311 12.473 -3.515 17.003 1.00 26.61 O
ANISOU 36 O THR A 311 3779 2084 4248 -92 144 1287 O
ATOM 37 CB THR A 311 13.557 -0.299 16.610 1.00 35.56 C
ANISOU 37 CB THR A 311 5108 2809 5594 -318 223 1437 C
ATOM 38 OG1 THR A 311 12.235 -0.206 17.154 1.00 36.45 O
ANISOU 38 OG1 THR A 311 5309 2854 5687 -161 200 1356 O
ATOM 39 CG2 THR A 311 13.745 0.755 15.538 1.00 31.61 C
ANISOU 39 CG2 THR A 311 4636 2257 5118 -354 275 1612 C
ATOM 40 N ALA A 312 14.234 -2.786 18.169 1.00 33.63 N
ANISOU 40 N ALA A 312 4703 2775 5299 -353 127 1190 N
ATOM 41 CA ALA A 312 13.914 -3.706 19.254 1.00 36.44 C
ANISOU 41 CA ALA A 312 5058 3151 5636 -302 72 1036 C
ATOM 42 C ALA A 312 12.580 -3.345 19.892 1.00 33.82 C
ANISOU 42 C ALA A 312 4850 2716 5284 -161 72 944 C
ATOM 43 O ALA A 312 11.773 -4.230 20.200 1.00 29.09 O
ANISOU 43 O ALA A 312 4232 2207 4613 -42 51 882 O
ATOM 44 CB ALA A 312 15.023 -3.695 20.300 1.00 35.87 C
ANISOU 44 CB ALA A 312 4973 3010 5644 -468 21 919 C
ATOM 45 N ASP A 313 12.325 -2.042 20.074 1.00 29.43 N
ANISOU 45 N ASP A 313 4419 1975 4788 -173 96 939 N
ATOM 46 CA ASP A 313 11.067 -1.596 20.662 1.00 33.87 C
ANISOU 46 CA ASP A 313 5092 2444 5334 -38 90 861 C
ATOM 47 C ASP A 313 9.889 -1.986 19.789 1.00 31.44 C
ANISOU 47 C ASP A 313 4728 2275 4941 126 96 954 C
ATOM 48 O ASP A 313 8.855 -2.433 20.289 1.00 28.63 O
ANISOU 48 O ASP A 313 4375 1968 4535 244 73 875 O
ATOM 49 CB ASP A 313 11.090 -0.082 20.857 1.00 39.49 C
ANISOU 49 CB ASP A 313 5943 2926 6136 -84 107 863 C
ATOM 50 CG ASP A 313 11.667 0.308 22.196 1.00 46.96 C
ANISOU 50 CG ASP A 313 6983 3720 7139 -197 85 688 C
ATOM 51 OD1 ASP A 313 11.307 -0.334 23.214 1.00 50.61 O
ANISOU 51 OD1 ASP A 313 7454 4220 7557 -148 54 542 O
ATOM 52 OD2 ASP A 313 12.522 1.216 22.230 1.00 51.29 O
ANISOU 52 OD2 ASP A 313 7592 4126 7770 -347 100 692 O
ATOM 53 N GLN A 314 10.044 -1.860 18.475 1.00 30.27 N
ANISOU 53 N GLN A 314 4515 2215 4770 124 125 1120 N
ATOM 54 CA GLN A 314 8.970 -2.229 17.556 1.00 29.16 C
ANISOU 54 CA GLN A 314 4308 2231 4541 262 127 1208 C
ATOM 55 C GLN A 314 8.768 -3.744 17.475 1.00 30.00 C
ANISOU 55 C GLN A 314 4304 2551 4545 305 106 1163 C
ATOM 56 O GLN A 314 7.640 -4.209 17.258 1.00 26.11 O
ANISOU 56 O GLN A 314 3772 2169 3980 420 93 1154 O
ATOM 57 CB GLN A 314 9.285 -1.643 16.181 1.00 33.21 C
ANISOU 57 CB GLN A 314 4786 2787 5047 237 165 1396 C
ATOM 58 CG GLN A 314 9.250 -0.127 16.179 1.00 30.23 C
ANISOU 58 CG GLN A 314 4527 2190 4769 220 188 1456 C
ATOM 59 CD GLN A 314 9.904 0.436 14.921 1.00 38.93 C
ANISOU 59 CD GLN A 314 5597 3322 5874 154 231 1644 C
ATOM 60 OE1 GLN A 314 10.498 -0.309 14.136 1.00 39.80 O
ANISOU 60 OE1 GLN A 314 5592 3621 5909 109 244 1715 O
ATOM 61 NE2 GLN A 314 9.788 1.743 14.718 1.00 44.51 N
ANISOU 61 NE2 GLN A 314 6404 3846 6661 151 255 1728 N
ATOM 62 N MET A 315 9.827 -4.538 17.632 1.00 24.78 N
ANISOU 62 N MET A 315 3583 1950 3881 210 99 1137 N
ATOM 63 CA MET A 315 9.634 -5.994 17.735 1.00 26.14 C
ANISOU 63 CA MET A 315 3671 2292 3969 256 75 1077 C
ATOM 64 C MET A 315 8.832 -6.373 18.980 1.00 27.15 C
ANISOU 64 C MET A 315 3852 2371 4091 323 45 919 C
ATOM 65 O MET A 315 7.843 -7.127 18.898 1.00 23.28 O
ANISOU 65 O MET A 315 3322 2001 3522 416 33 886 O
ATOM 66 CB MET A 315 11.005 -6.680 17.694 1.00 22.19 C
ANISOU 66 CB MET A 315 3093 1851 3486 143 69 1094 C
ATOM 67 CG MET A 315 11.013 -8.218 17.753 1.00 31.71 C
ANISOU 67 CG MET A 315 4215 3248 4588 178 41 1005 C
ATOM 68 SD MET A 315 10.294 -9.083 16.362 1.00 37.82 S
ANISOU 68 SD MET A 315 4897 4258 5216 272 60 1084 S
ATOM 69 CE MET A 315 11.674 -9.177 15.252 1.00 30.84 C
ANISOU 69 CE MET A 315 3915 3517 4288 170 92 1176 C
ATOM 70 N VAL A 316 9.219 -5.832 20.137 1.00 21.78 N
ANISOU 70 N VAL A 316 3261 1525 3489 267 33 818 N
ATOM 71 CA VAL A 316 8.477 -6.097 21.382 1.00 25.32 C
ANISOU 71 CA VAL A 316 3765 1935 3921 329 9 670 C
ATOM 72 C VAL A 316 6.995 -5.788 21.190 1.00 27.17 C
ANISOU 72 C VAL A 316 4005 2199 4120 455 11 680 C
ATOM 73 O VAL A 316 6.131 -6.624 21.481 1.00 22.69 O
ANISOU 73 O VAL A 316 3390 1740 3491 526 -3 624 O
ATOM 74 CB VAL A 316 9.055 -5.284 22.560 1.00 29.45 C
ANISOU 74 CB VAL A 316 4396 2269 4525 249 2 562 C
ATOM 75 CG1 VAL A 316 8.160 -5.447 23.805 1.00 28.33 C
ANISOU 75 CG1 VAL A 316 4309 2103 4352 327 -22 418 C
ATOM 76 CG2 VAL A 316 10.489 -5.721 22.889 1.00 25.19 C
ANISOU 76 CG2 VAL A 316 3809 1725 4037 105 -23 533 C
ATOM 77 N SER A 317 6.684 -4.586 20.663 1.00 23.00 N
ANISOU 77 N SER A 317 3522 1576 3641 478 30 763 N
ATOM 78 CA SER A 317 5.288 -4.160 20.517 1.00 23.48 C
ANISOU 78 CA SER A 317 3575 1652 3694 601 34 782 C
ATOM 79 C SER A 317 4.499 -5.087 19.620 1.00 25.79 C
ANISOU 79 C SER A 317 3751 2157 3890 668 35 844 C
ATOM 80 O SER A 317 3.349 -5.414 19.919 1.00 28.83 O
ANISOU 80 O SER A 317 4098 2612 4245 751 32 800 O
ATOM 81 CB SER A 317 5.184 -2.748 19.932 1.00 32.70 C
ANISOU 81 CB SER A 317 4804 2685 4935 619 57 888 C
ATOM 82 OG SER A 317 5.777 -1.805 20.776 1.00 35.50 O
ANISOU 82 OG SER A 317 5277 2827 5385 556 54 819 O
ATOM 83 N ALA A 318 5.063 -5.432 18.459 1.00 25.89 N
ANISOU 83 N ALA A 318 3703 2278 3856 630 46 953 N
ATOM 84 CA ALA A 318 4.385 -6.339 17.543 1.00 26.55 C
ANISOU 84 CA ALA A 318 3677 2574 3838 682 43 1003 C
ATOM 85 C ALA A 318 4.144 -7.704 18.185 1.00 25.64 C
ANISOU 85 C ALA A 318 3517 2559 3665 683 22 885 C
ATOM 86 O ALA A 318 3.084 -8.315 17.987 1.00 24.95 O
ANISOU 86 O ALA A 318 3365 2599 3516 744 17 872 O
ATOM 87 CB ALA A 318 5.208 -6.500 16.265 1.00 22.78 C
ANISOU 87 CB ALA A 318 3142 2201 3314 631 58 1128 C
ATOM 88 N LEU A 319 5.118 -8.216 18.931 1.00 26.83 N
ANISOU 88 N LEU A 319 3697 2659 3837 613 12 806 N
ATOM 89 CA LEU A 319 4.901 -9.511 19.568 1.00 27.31 C
ANISOU 89 CA LEU A 319 3723 2804 3848 618 -6 701 C
ATOM 90 C LEU A 319 3.842 -9.417 20.671 1.00 23.91 C
ANISOU 90 C LEU A 319 3321 2330 3433 670 -10 606 C
ATOM 91 O LEU A 319 2.948 -10.278 20.763 1.00 20.21 O
ANISOU 91 O LEU A 319 2796 1972 2909 708 -9 570 O
ATOM 92 CB LEU A 319 6.225 -10.056 20.100 1.00 23.26 C
ANISOU 92 CB LEU A 319 3228 2252 3358 541 -15 654 C
ATOM 93 CG LEU A 319 7.267 -10.487 19.041 1.00 24.42 C
ANISOU 93 CG LEU A 319 3309 2487 3484 493 -6 748 C
ATOM 94 CD1 LEU A 319 8.497 -11.011 19.730 1.00 25.32 C
ANISOU 94 CD1 LEU A 319 3420 2581 3619 407 -27 667 C
ATOM 95 CD2 LEU A 319 6.694 -11.573 18.108 1.00 22.54 C
ANISOU 95 CD2 LEU A 319 2982 2443 3140 541 -6 771 C
ATOM 96 N LEU A 320 3.892 -8.352 21.483 1.00 20.37 N
ANISOU 96 N LEU A 320 2953 1724 3061 671 -7 568 N
ATOM 97 CA LEU A 320 2.896 -8.183 22.553 1.00 28.96 C
ANISOU 97 CA LEU A 320 4058 2780 4167 728 2 482 C
ATOM 98 C LEU A 320 1.500 -8.057 21.966 1.00 26.74 C
ANISOU 98 C LEU A 320 3714 2588 3856 821 22 540 C
ATOM 99 O LEU A 320 0.541 -8.655 22.476 1.00 23.28 O
ANISOU 99 O LEU A 320 3234 2230 3382 864 37 491 O
ATOM 100 CB LEU A 320 3.221 -6.953 23.408 1.00 30.01 C
ANISOU 100 CB LEU A 320 4287 2723 4392 718 5 431 C
ATOM 101 CG LEU A 320 4.374 -7.085 24.409 1.00 27.33 C
ANISOU 101 CG LEU A 320 4005 2296 4085 630 -13 336 C
ATOM 102 CD1 LEU A 320 4.583 -5.737 25.152 1.00 29.40 C
ANISOU 102 CD1 LEU A 320 4363 2363 4444 617 -6 278 C
ATOM 103 CD2 LEU A 320 4.126 -8.260 25.401 1.00 21.59 C
ANISOU 103 CD2 LEU A 320 3242 1663 3297 633 -5 239 C
ATOM 104 N AASP A 321 1.364 -7.323 20.872 0.49 25.06 N
ANISOU 104 N AASP A 321 3491 2378 3653 851 28 655 N
ATOM 105 N BASP A 321 1.374 -7.306 20.877 0.51 25.06 N
ANISOU 105 N BASP A 321 3492 2375 3654 851 28 655 N
ATOM 106 CA AASP A 321 0.047 -7.154 20.261 0.49 30.42 C
ANISOU 106 CA AASP A 321 4103 3155 4302 946 44 724 C
ATOM 107 CA BASP A 321 0.077 -7.130 20.224 0.51 30.43 C
ANISOU 107 CA BASP A 321 4105 3154 4304 945 44 727 C
ATOM 108 C AASP A 321 -0.407 -8.380 19.484 0.49 29.35 C
ANISOU 108 C AASP A 321 3860 3226 4065 945 35 751 C
ATOM 109 C BASP A 321 -0.407 -8.415 19.574 0.51 29.35 C
ANISOU 109 C BASP A 321 3863 3223 4067 943 35 743 C
ATOM 110 O AASP A 321 -1.605 -8.538 19.250 0.49 29.87 O
ANISOU 110 O AASP A 321 3855 3400 4093 1014 44 777 O
ATOM 111 O BASP A 321 -1.614 -8.659 19.523 0.51 29.72 O
ANISOU 111 O BASP A 321 3842 3371 4078 1010 46 751 O
ATOM 112 CB AASP A 321 0.031 -5.944 19.334 0.49 28.52 C
ANISOU 112 CB AASP A 321 3882 2853 4101 986 54 850 C
ATOM 113 CB BASP A 321 0.157 -6.028 19.174 0.51 28.41 C
ANISOU 113 CB BASP A 321 3863 2854 4079 975 52 861 C
ATOM 114 CG AASP A 321 -1.378 -5.497 19.005 0.49 33.90 C
ANISOU 114 CG AASP A 321 4508 3596 4775 1103 72 912 C
ATOM 115 CG BASP A 321 0.458 -4.673 19.779 0.51 30.80 C
ANISOU 115 CG BASP A 321 4274 2937 4490 987 63 850 C
ATOM 116 OD1AASP A 321 -2.069 -5.024 19.931 0.49 32.50 O
ANISOU 116 OD1AASP A 321 4359 3338 4650 1168 92 850 O
ATOM 117 OD1BASP A 321 0.517 -4.559 21.019 0.51 35.60 O
ANISOU 117 OD1BASP A 321 4940 3441 5146 978 64 730 O
ATOM 118 OD2AASP A 321 -1.791 -5.613 17.838 0.49 38.21 O
ANISOU 118 OD2AASP A 321 4976 4280 5260 1134 69 1023 O
ATOM 119 OD2BASP A 321 0.637 -3.717 19.014 0.51 30.75 O
ANISOU 119 OD2BASP A 321 4299 2862 4523 1003 73 962 O
ATOM 120 N ALA A 322 0.515 -9.241 19.077 1.00 25.65 N
ANISOU 120 N ALA A 322 3377 2818 3553 870 18 746 N
ATOM 121 CA ALA A 322 0.150 -10.482 18.436 1.00 28.40 C
ANISOU 121 CA ALA A 322 3634 3351 3808 864 6 749 C
ATOM 122 C ALA A 322 -0.376 -11.509 19.413 1.00 21.93 C
ANISOU 122 C ALA A 322 2798 2566 2970 862 7 643 C
ATOM 123 O ALA A 322 -0.872 -12.552 18.956 1.00 21.60 O
ANISOU 123 O ALA A 322 2678 2674 2855 863 -3 639 O
ATOM 124 CB ALA A 322 1.347 -11.100 17.716 1.00 22.10 C
ANISOU 124 CB ALA A 322 2824 2603 2969 796 -7 773 C
ATOM 125 N GLU A 323 -0.267 -11.260 20.715 1.00 19.92 N
ANISOU 125 N GLU A 323 2612 2186 2772 856 19 559 N
ATOM 126 CA GLU A 323 -0.529 -12.323 21.686 1.00 17.72 C
ANISOU 126 CA GLU A 323 2328 1938 2468 840 25 467 C
ATOM 127 C GLU A 323 -1.955 -12.895 21.563 1.00 22.13 C
ANISOU 127 C GLU A 323 2797 2634 2976 897 40 478 C
ATOM 128 O GLU A 323 -2.931 -12.142 21.421 1.00 21.03 O
ANISOU 128 O GLU A 323 2626 2518 2847 967 57 523 O
ATOM 129 CB GLU A 323 -0.265 -11.769 23.081 1.00 21.93 C
ANISOU 129 CB GLU A 323 2943 2333 3057 834 39 387 C
ATOM 130 CG GLU A 323 -0.253 -12.785 24.129 1.00 42.29 C
ANISOU 130 CG GLU A 323 5533 4930 5604 807 47 303 C
ATOM 131 CD GLU A 323 1.021 -13.625 24.172 1.00 23.88 C
ANISOU 131 CD GLU A 323 3227 2586 3260 730 19 273 C
ATOM 132 OE1 GLU A 323 1.872 -13.690 23.187 1.00 22.89 O
ANISOU 132 OE1 GLU A 323 3089 2472 3136 696 -5 320 O
ATOM 133 OE2 GLU A 323 1.156 -14.188 25.255 1.00 26.48 O
ANISOU 133 OE2 GLU A 323 3588 2898 3573 711 25 206 O
ATOM 134 N PRO A 324 -2.130 -14.220 21.588 1.00 21.36 N
ANISOU 134 N PRO A 324 2653 2637 2827 872 33 443 N
ATOM 135 CA PRO A 324 -3.517 -14.783 21.519 1.00 18.77 C
ANISOU 135 CA PRO A 324 2222 2455 2455 918 44 453 C
ATOM 136 C PRO A 324 -4.220 -14.606 22.848 1.00 21.70 C
ANISOU 136 C PRO A 324 2616 2778 2851 957 88 404 C
ATOM 137 O PRO A 324 -3.563 -14.374 23.870 1.00 19.37 O
ANISOU 137 O PRO A 324 2417 2353 2589 936 103 344 O
ATOM 138 CB PRO A 324 -3.296 -16.262 21.246 1.00 16.88 C
ANISOU 138 CB PRO A 324 1935 2312 2167 867 22 416 C
ATOM 139 CG PRO A 324 -1.948 -16.521 21.913 1.00 21.54 C
ANISOU 139 CG PRO A 324 2638 2754 2790 805 23 354 C
ATOM 140 CD PRO A 324 -1.113 -15.275 21.704 1.00 20.29 C
ANISOU 140 CD PRO A 324 2546 2486 2677 808 16 393 C
ATOM 141 N PRO A 325 -5.545 -14.719 22.877 1.00 21.32 N
ANISOU 141 N PRO A 325 2471 2851 2778 1012 109 426 N
ATOM 142 CA PRO A 325 -6.270 -14.615 24.144 1.00 19.03 C
ANISOU 142 CA PRO A 325 2190 2541 2500 1057 163 382 C
ATOM 143 C PRO A 325 -6.092 -15.874 24.981 1.00 16.76 C
ANISOU 143 C PRO A 325 1908 2271 2188 1013 182 321 C
ATOM 144 O PRO A 325 -5.734 -16.941 24.471 1.00 19.54 O
ANISOU 144 O PRO A 325 2232 2676 2515 925 150 307 O
ATOM 145 CB PRO A 325 -7.738 -14.460 23.690 1.00 20.00 C
ANISOU 145 CB PRO A 325 2176 2825 2597 1121 175 439 C
ATOM 146 CG PRO A 325 -7.819 -15.176 22.352 1.00 22.61 C
ANISOU 146 CG PRO A 325 2402 3310 2877 1074 120 486 C
ATOM 147 CD PRO A 325 -6.438 -14.955 21.716 1.00 23.07 C
ANISOU 147 CD PRO A 325 2557 3260 2949 1028 82 493 C
ATOM 148 N ILE A 326 -6.339 -15.721 26.276 1.00 16.82 N
ANISOU 148 N ILE A 326 1964 2228 2197 1041 234 273 N
ATOM 149 CA ILE A 326 -6.383 -16.863 27.196 1.00 21.52 C
ANISOU 149 CA ILE A 326 2565 2853 2759 985 265 225 C
ATOM 150 C ILE A 326 -7.767 -17.494 27.091 1.00 16.43 C
ANISOU 150 C ILE A 326 1774 2384 2085 969 295 249 C
ATOM 151 O ILE A 326 -8.770 -16.831 27.339 1.00 19.09 O
ANISOU 151 O ILE A 326 2039 2793 2422 1077 343 275 O
ATOM 152 CB ILE A 326 -6.049 -16.421 28.633 1.00 22.72 C
ANISOU 152 CB ILE A 326 2827 2902 2903 1027 311 168 C
ATOM 153 CG1 ILE A 326 -4.580 -15.947 28.701 1.00 24.63 C
ANISOU 153 CG1 ILE A 326 3198 2989 3170 981 260 133 C
ATOM 154 CG2 ILE A 326 -6.330 -17.519 29.640 1.00 21.25 C
ANISOU 154 CG2 ILE A 326 2639 2772 2665 951 348 139 C
ATOM 155 CD1 ILE A 326 -4.208 -15.259 30.015 1.00 25.62 C
ANISOU 155 CD1 ILE A 326 3428 3026 3282 997 284 63 C
ATOM 156 N LEU A 327 -7.827 -18.751 26.644 1.00 14.86 N
ANISOU 156 N LEU A 327 1525 2256 1866 835 268 238 N
ATOM 157 CA LEU A 327 -9.127 -19.394 26.436 1.00 16.13 C
ANISOU 157 CA LEU A 327 1534 2593 2003 788 288 256 C
ATOM 158 C LEU A 327 -9.588 -20.090 27.710 1.00 16.05 C
ANISOU 158 C LEU A 327 1527 2596 1974 737 358 235 C
ATOM 159 O LEU A 327 -8.803 -20.381 28.609 1.00 15.77 O
ANISOU 159 O LEU A 327 1615 2441 1934 710 375 206 O
ATOM 160 CB LEU A 327 -9.057 -20.410 25.291 1.00 15.18 C
ANISOU 160 CB LEU A 327 1355 2541 1872 653 229 240 C
ATOM 161 CG LEU A 327 -8.613 -19.825 23.947 1.00 17.65 C
ANISOU 161 CG LEU A 327 1653 2876 2178 692 161 267 C
ATOM 162 CD1 LEU A 327 -8.788 -20.936 22.780 1.00 17.27 C
ANISOU 162 CD1 LEU A 327 1524 2945 2095 547 107 229 C
ATOM 163 CD2 LEU A 327 -9.398 -18.553 23.611 1.00 16.49 C
ANISOU 163 CD2 LEU A 327 1418 2819 2029 847 166 347 C
ATOM 164 N TYR A 328 -10.874 -20.363 27.780 1.00 16.81 N
ANISOU 164 N TYR A 328 1479 2855 2053 722 398 259 N
ATOM 165 CA TYR A 328 -11.434 -21.078 28.920 1.00 17.98 C
ANISOU 165 CA TYR A 328 1609 3044 2178 659 474 257 C
ATOM 166 C TYR A 328 -11.820 -22.508 28.553 1.00 19.82 C
ANISOU 166 C TYR A 328 1772 3340 2418 468 462 253 C
ATOM 167 O TYR A 328 -12.035 -22.848 27.387 1.00 20.79 O
ANISOU 167 O TYR A 328 1813 3535 2552 397 402 242 O
ATOM 168 CB TYR A 328 -12.669 -20.346 29.456 1.00 19.86 C
ANISOU 168 CB TYR A 328 1725 3426 2393 778 550 289 C
ATOM 169 CG TYR A 328 -12.340 -19.092 30.176 1.00 25.85 C
ANISOU 169 CG TYR A 328 2580 4093 3147 953 590 272 C
ATOM 170 CD1 TYR A 328 -11.897 -17.967 29.481 1.00 24.19 C
ANISOU 170 CD1 TYR A 328 2413 3805 2975 1077 545 277 C
ATOM 171 CD2 TYR A 328 -12.551 -18.998 31.567 1.00 25.21 C
ANISOU 171 CD2 TYR A 328 2544 4013 3021 995 681 250 C
ATOM 172 CE1 TYR A 328 -11.617 -16.791 30.170 1.00 30.65 C
ANISOU 172 CE1 TYR A 328 3343 4502 3801 1202 574 244 C
ATOM 173 CE2 TYR A 328 -12.271 -17.824 32.251 1.00 26.56 C
ANISOU 173 CE2 TYR A 328 2811 4098 3182 1152 721 208 C
ATOM 174 CZ TYR A 328 -11.806 -16.748 31.547 1.00 28.32 C
ANISOU 174 CZ TYR A 328 3100 4201 3460 1229 655 198 C
ATOM 175 OH TYR A 328 -11.536 -15.633 32.271 1.00 35.29 O
ANISOU 175 OH TYR A 328 4102 4961 4345 1310 671 141 O
ATOM 176 N SER A 329 -11.957 -23.341 29.577 1.00 22.21 N
ANISOU 176 N SER A 329 2107 3622 2711 382 525 261 N
ATOM 177 CA SER A 329 -12.623 -24.619 29.394 1.00 23.29 C
ANISOU 177 CA SER A 329 2156 3827 2864 199 539 267 C
ATOM 178 C SER A 329 -14.151 -24.442 29.475 1.00 27.93 C
ANISOU 178 C SER A 329 2541 4641 3431 200 593 304 C
ATOM 179 O SER A 329 -14.664 -23.419 29.930 1.00 27.21 O
ANISOU 179 O SER A 329 2393 4636 3308 355 639 330 O
ATOM 180 CB SER A 329 -12.115 -25.618 30.435 1.00 24.72 C
ANISOU 180 CB SER A 329 2459 3883 3051 104 588 286 C
ATOM 181 OG SER A 329 -12.732 -26.854 30.233 1.00 25.79 O
ANISOU 181 OG SER A 329 2525 4052 3221 -83 606 293 O
ATOM 182 N GLU A 330 -14.904 -25.462 29.050 1.00 36.97 N
ANISOU 182 N GLU A 330 3568 5884 4596 21 591 302 N
ATOM 183 CA GLU A 330 -16.363 -25.300 29.000 1.00 35.85 C
ANISOU 183 CA GLU A 330 3201 5987 4434 11 631 338 C
ATOM 184 C GLU A 330 -16.999 -25.121 30.389 1.00 38.60 C
ANISOU 184 C GLU A 330 3513 6405 4747 65 753 396 C
ATOM 185 O GLU A 330 -16.559 -25.685 31.403 1.00 34.09 O
ANISOU 185 O GLU A 330 3065 5718 4168 12 814 416 O
ATOM 186 CB GLU A 330 -17.019 -26.485 28.288 1.00 51.62 C
ANISOU 186 CB GLU A 330 5077 8076 6461 -224 601 313 C
ATOM 187 CG GLU A 330 -17.342 -27.695 29.171 1.00 48.53 C
ANISOU 187 CG GLU A 330 4699 7643 6098 -413 684 340 C
ATOM 188 CD GLU A 330 -18.106 -28.781 28.409 1.00 60.78 C
ANISOU 188 CD GLU A 330 6115 9290 7689 -659 655 303 C
ATOM 189 OE1 GLU A 330 -19.305 -28.977 28.702 1.00 60.83 O
ANISOU 189 OE1 GLU A 330 5932 9493 7688 -743 711 346 O
ATOM 190 OE2 GLU A 330 -17.513 -29.432 27.516 1.00 71.87 O
ANISOU 190 OE2 GLU A 330 7597 10580 9130 -772 578 222 O
ATOM 191 N TYR A 331 -18.056 -24.321 30.435 1.00 32.10 N
ANISOU 191 N TYR A 331 2514 5788 3896 183 794 429 N
ATOM 192 CA TYR A 331 -18.836 -24.259 31.645 1.00 37.66 C
ANISOU 192 CA TYR A 331 3171 6575 4563 213 906 469 C
ATOM 193 C TYR A 331 -20.068 -25.181 31.586 1.00 43.88 C
ANISOU 193 C TYR A 331 3795 7508 5368 25 925 495 C
ATOM 194 O TYR A 331 -21.195 -24.731 31.367 1.00 48.33 O
ANISOU 194 O TYR A 331 4219 8218 5926 77 914 503 O
ATOM 195 CB TYR A 331 -19.245 -22.825 31.935 1.00 37.94 C
ANISOU 195 CB TYR A 331 3209 6632 4573 453 917 461 C
ATOM 196 CG TYR A 331 -18.149 -22.010 32.614 1.00 38.26 C
ANISOU 196 CG TYR A 331 3443 6507 4589 615 942 430 C
ATOM 197 CD1 TYR A 331 -18.025 -21.972 34.006 1.00 39.45 C
ANISOU 197 CD1 TYR A 331 3687 6621 4683 652 1039 428 C
ATOM 198 CD2 TYR A 331 -17.261 -21.257 31.861 1.00 31.91 C
ANISOU 198 CD2 TYR A 331 2730 5584 3812 724 865 400 C
ATOM 199 CE1 TYR A 331 -17.020 -21.211 34.615 1.00 33.57 C
ANISOU 199 CE1 TYR A 331 3124 5725 3906 787 1048 382 C
ATOM 200 CE2 TYR A 331 -16.268 -20.486 32.471 1.00 30.76 C
ANISOU 200 CE2 TYR A 331 2765 5272 3650 856 880 361 C
ATOM 201 CZ TYR A 331 -16.162 -20.450 33.846 1.00 32.78 C
ANISOU 201 CZ TYR A 331 3112 5497 3847 886 967 344 C
ATOM 202 OH TYR A 331 -15.140 -19.690 34.426 1.00 31.37 O
ANISOU 202 OH TYR A 331 3118 5154 3645 997 966 287 O
ATOM 203 N PHE A 337 -16.965 -31.231 35.894 1.00 55.68 N
ANISOU 203 N PHE A 337 6049 8171 6936 -748 1216 794 N
ATOM 204 CA PHE A 337 -15.593 -31.726 35.836 1.00 52.33 C
ANISOU 204 CA PHE A 337 5846 7484 6555 -740 1152 785 C
ATOM 205 C PHE A 337 -15.454 -33.030 36.620 1.00 46.87 C
ANISOU 205 C PHE A 337 5250 6659 5899 -895 1225 906 C
ATOM 206 O PHE A 337 -16.085 -33.197 37.661 1.00 55.45 O
ANISOU 206 O PHE A 337 6289 7857 6922 -928 1335 1018 O
ATOM 207 CB PHE A 337 -14.593 -30.694 36.397 1.00 52.15 C
ANISOU 207 CB PHE A 337 5954 7421 6441 -510 1122 764 C
ATOM 208 CG PHE A 337 -13.162 -31.203 36.438 1.00 54.72 C
ANISOU 208 CG PHE A 337 6486 7504 6801 -494 1058 769 C
ATOM 209 CD1 PHE A 337 -12.355 -31.138 35.298 1.00 41.41 C
ANISOU 209 CD1 PHE A 337 4858 5688 5189 -474 949 671 C
ATOM 210 CD2 PHE A 337 -12.648 -31.798 37.597 1.00 49.86 C
ANISOU 210 CD2 PHE A 337 5996 6808 6141 -501 1112 884 C
ATOM 211 CE1 PHE A 337 -11.061 -31.631 35.317 1.00 40.72 C
ANISOU 211 CE1 PHE A 337 4940 5394 5138 -452 898 678 C
ATOM 212 CE2 PHE A 337 -11.360 -32.295 37.621 1.00 43.84 C
ANISOU 212 CE2 PHE A 337 5404 5839 5416 -476 1052 901 C
ATOM 213 CZ PHE A 337 -10.563 -32.205 36.478 1.00 39.72 C
ANISOU 213 CZ PHE A 337 4928 5188 4975 -448 947 793 C
ATOM 214 N SER A 338 -14.601 -33.928 36.116 1.00 48.50 N
ANISOU 214 N SER A 338 5595 6624 6207 -977 1168 889 N
ATOM 215 CA SER A 338 -14.284 -35.196 36.775 1.00 41.42 C
ANISOU 215 CA SER A 338 4822 5545 5368 -1103 1228 1012 C
ATOM 216 C SER A 338 -12.981 -35.722 36.178 1.00 47.54 C
ANISOU 216 C SER A 338 5776 6054 6234 -1078 1141 961 C
ATOM 217 O SER A 338 -12.493 -35.220 35.161 1.00 43.29 O
ANISOU 217 O SER A 338 5240 5490 5718 -1006 1044 825 O
ATOM 218 CB SER A 338 -15.383 -36.248 36.569 1.00 43.90 C
ANISOU 218 CB SER A 338 5030 5871 5779 -1363 1298 1053 C
ATOM 219 OG SER A 338 -15.374 -36.623 35.192 1.00 42.65 O
ANISOU 219 OG SER A 338 4848 5623 5735 -1473 1214 910 O
ATOM 220 N GLU A 339 -12.446 -36.779 36.796 1.00 43.43 N
ANISOU 220 N GLU A 339 5398 5337 5768 -1137 1185 1080 N
ATOM 221 CA GLU A 339 -11.206 -37.358 36.290 1.00 45.63 C
ANISOU 221 CA GLU A 339 5840 5358 6140 -1099 1116 1042 C
ATOM 222 C GLU A 339 -11.414 -37.941 34.895 1.00 43.66 C
ANISOU 222 C GLU A 339 5561 5002 6028 -1244 1069 895 C
ATOM 223 O GLU A 339 -10.539 -37.805 34.027 1.00 42.38 O
ANISOU 223 O GLU A 339 5464 4736 5902 -1166 983 778 O
ATOM 224 CB GLU A 339 -10.672 -38.416 37.267 1.00 50.77 C
ANISOU 224 CB GLU A 339 6642 5820 6830 -1124 1180 1221 C
ATOM 225 N ALA A 340 -12.597 -38.540 34.650 1.00 41.37 N
ANISOU 225 N ALA A 340 5159 4761 5800 -1462 1125 891 N
ATOM 226 CA ALA A 340 -12.894 -39.207 33.379 1.00 41.83 C
ANISOU 226 CA ALA A 340 5186 4726 5981 -1636 1085 742 C
ATOM 227 C ALA A 340 -13.009 -38.246 32.183 1.00 43.48 C
ANISOU 227 C ALA A 340 5278 5104 6137 -1571 982 564 C
ATOM 228 O ALA A 340 -12.704 -38.633 31.047 1.00 42.17 O
ANISOU 228 O ALA A 340 5143 4837 6044 -1633 919 418 O
ATOM 229 CB ALA A 340 -14.184 -40.001 33.521 1.00 38.74 C
ANISOU 229 CB ALA A 340 4683 4380 5655 -1894 1167 789 C
ATOM 230 N SER A 341 -13.474 -37.014 32.389 1.00 37.70 N
ANISOU 230 N SER A 341 4413 4630 5280 -1446 969 572 N
ATOM 231 CA SER A 341 -13.618 -36.071 31.277 1.00 34.78 C
ANISOU 231 CA SER A 341 3931 4423 4860 -1373 875 432 C
ATOM 232 C SER A 341 -12.392 -35.175 31.105 1.00 31.93 C
ANISOU 232 C SER A 341 3676 4014 4444 -1140 802 395 C
ATOM 233 O SER A 341 -12.318 -34.380 30.167 1.00 31.97 O
ANISOU 233 O SER A 341 3615 4123 4410 -1063 723 294 O
ATOM 234 CB SER A 341 -14.939 -35.303 31.473 1.00 37.30 C
ANISOU 234 CB SER A 341 4030 5043 5099 -1382 907 461 C
ATOM 235 OG SER A 341 -14.846 -34.343 32.509 1.00 41.64 O
ANISOU 235 OG SER A 341 4582 5696 5544 -1192 948 554 O
ATOM 236 N MET A 342 -11.390 -35.331 31.957 1.00 28.02 N
ANISOU 236 N MET A 342 3339 3362 3944 -1036 823 480 N
ATOM 237 CA MET A 342 -10.202 -34.477 31.896 1.00 26.39 C
ANISOU 237 CA MET A 342 3223 3119 3685 -829 755 451 C
ATOM 238 C MET A 342 -9.492 -34.409 30.541 1.00 29.94 C
ANISOU 238 C MET A 342 3701 3499 4176 -805 664 311 C
ATOM 239 O MET A 342 -9.243 -33.313 29.995 1.00 27.83 O
ANISOU 239 O MET A 342 3389 3341 3846 -681 601 252 O
ATOM 240 CB MET A 342 -9.245 -34.912 32.975 1.00 34.24 C
ANISOU 240 CB MET A 342 4376 3955 4680 -756 787 566 C
ATOM 241 CG MET A 342 -7.979 -34.069 33.052 1.00 38.43 C
ANISOU 241 CG MET A 342 4992 4458 5153 -558 718 546 C
ATOM 242 SD MET A 342 -7.058 -34.693 34.450 1.00 44.30 S
ANISOU 242 SD MET A 342 5889 5063 5881 -492 757 705 S
ATOM 243 CE MET A 342 -5.572 -33.717 34.348 1.00 45.27 C
ANISOU 243 CE MET A 342 6084 5172 5946 -290 660 654 C
ATOM 244 N MET A 343 -9.162 -35.553 29.932 1.00 26.91 N
ANISOU 244 N MET A 343 3393 2935 3897 -922 661 253 N
ATOM 245 CA MET A 343 -8.492 -35.458 28.626 1.00 27.40 C
ANISOU 245 CA MET A 343 3476 2956 3977 -892 583 110 C
ATOM 246 C MET A 343 -9.362 -34.854 27.538 1.00 25.88 C
ANISOU 246 C MET A 343 3123 2975 3735 -946 531 5 C
ATOM 247 O MET A 343 -8.834 -34.170 26.648 1.00 25.44 O
ANISOU 247 O MET A 343 3056 2975 3634 -851 461 -74 O
ATOM 248 CB MET A 343 -7.914 -36.771 28.060 1.00 32.54 C
ANISOU 248 CB MET A 343 4247 3370 4749 -990 591 36 C
ATOM 249 CG MET A 343 -6.746 -37.466 28.773 1.00 37.60 C
ANISOU 249 CG MET A 343 5061 3768 5458 -905 623 119 C
ATOM 250 SD MET A 343 -5.425 -36.171 28.692 1.00 42.71 S
ANISOU 250 SD MET A 343 5734 4486 6009 -653 545 116 S
ATOM 251 CE MET A 343 -5.055 -36.135 26.941 1.00 33.76 C
ANISOU 251 CE MET A 343 4575 3365 4887 -669 480 -80 C
ATOM 252 N GLY A 344 -10.669 -35.142 27.562 1.00 29.01 N
ANISOU 252 N GLY A 344 3390 3495 4136 -1102 564 10 N
ATOM 253 CA GLY A 344 -11.575 -34.523 26.607 1.00 31.69 C
ANISOU 253 CA GLY A 344 3552 4072 4415 -1142 509 -69 C
ATOM 254 C GLY A 344 -11.541 -33.010 26.704 1.00 27.65 C
ANISOU 254 C GLY A 344 2971 3735 3801 -938 475 -23 C
ATOM 255 O GLY A 344 -11.496 -32.325 25.688 1.00 25.92 O
ANISOU 255 O GLY A 344 2686 3633 3530 -879 403 -92 O
ATOM 256 N LEU A 345 -11.573 -32.468 27.940 1.00 25.64 N
ANISOU 256 N LEU A 345 2733 3496 3512 -829 532 95 N
ATOM 257 CA LEU A 345 -11.521 -31.007 28.136 1.00 25.59 C
ANISOU 257 CA LEU A 345 2680 3621 3420 -631 511 130 C
ATOM 258 C LEU A 345 -10.192 -30.419 27.663 1.00 24.26 C
ANISOU 258 C LEU A 345 2628 3349 3239 -489 445 90 C
ATOM 259 O LEU A 345 -10.162 -29.372 26.990 1.00 21.54 O
ANISOU 259 O LEU A 345 2226 3112 2847 -382 392 65 O
ATOM 260 CB LEU A 345 -11.734 -30.685 29.620 1.00 24.38 C
ANISOU 260 CB LEU A 345 2548 3486 3230 -557 592 242 C
ATOM 261 CG LEU A 345 -13.092 -31.073 30.171 1.00 24.53 C
ANISOU 261 CG LEU A 345 2429 3647 3246 -677 671 300 C
ATOM 262 CD1 LEU A 345 -13.067 -30.778 31.695 1.00 29.86 C
ANISOU 262 CD1 LEU A 345 3156 4324 3864 -586 758 408 C
ATOM 263 CD2 LEU A 345 -14.212 -30.302 29.494 1.00 28.69 C
ANISOU 263 CD2 LEU A 345 2748 4422 3730 -658 648 271 C
ATOM 264 N LEU A 346 -9.076 -31.107 27.963 1.00 20.30 N
ANISOU 264 N LEU A 346 2285 2640 2786 -488 449 92 N
ATOM 265 CA LEU A 346 -7.765 -30.614 27.568 1.00 20.46 C
ANISOU 265 CA LEU A 346 2405 2571 2798 -363 393 59 C
ATOM 266 C LEU A 346 -7.618 -30.658 26.064 1.00 18.51 C
ANISOU 266 C LEU A 346 2118 2360 2554 -401 329 -48 C
ATOM 267 O LEU A 346 -7.017 -29.750 25.466 1.00 16.11 O
ANISOU 267 O LEU A 346 1814 2096 2209 -289 277 -68 O
ATOM 268 CB LEU A 346 -6.651 -31.445 28.241 1.00 22.21 C
ANISOU 268 CB LEU A 346 2784 2581 3073 -352 414 94 C
ATOM 269 CG LEU A 346 -6.638 -31.212 29.755 1.00 21.93 C
ANISOU 269 CG LEU A 346 2794 2539 3000 -288 466 209 C
ATOM 270 CD1 LEU A 346 -5.670 -32.169 30.476 1.00 21.50 C
ANISOU 270 CD1 LEU A 346 2880 2295 2993 -285 488 271 C
ATOM 271 CD2 LEU A 346 -6.196 -29.779 30.053 1.00 25.01 C
ANISOU 271 CD2 LEU A 346 3183 3008 3312 -125 433 219 C
ATOM 272 N THR A 347 -8.202 -31.692 25.444 1.00 18.40 N
ANISOU 272 N THR A 347 2066 2342 2584 -567 334 -119 N
ATOM 273 CA THR A 347 -8.133 -31.813 24.008 1.00 19.22 C
ANISOU 273 CA THR A 347 2129 2504 2671 -618 274 -237 C
ATOM 274 C THR A 347 -8.925 -30.698 23.360 1.00 21.76 C
ANISOU 274 C THR A 347 2295 3069 2904 -567 225 -231 C
ATOM 275 O THR A 347 -8.447 -30.071 22.393 1.00 18.74 O
ANISOU 275 O THR A 347 1899 2752 2469 -493 167 -270 O
ATOM 276 CB THR A 347 -8.657 -33.190 23.576 1.00 25.61 C
ANISOU 276 CB THR A 347 2936 3252 3545 -825 293 -331 C
ATOM 277 OG1 THR A 347 -7.721 -34.178 24.045 1.00 28.29 O
ANISOU 277 OG1 THR A 347 3440 3333 3975 -836 336 -333 O
ATOM 278 CG2 THR A 347 -8.766 -33.307 22.058 1.00 28.66 C
ANISOU 278 CG2 THR A 347 3260 3743 3887 -896 227 -474 C
ATOM 279 N ASN A 348 -10.153 -30.477 23.860 1.00 21.07 N
ANISOU 279 N ASN A 348 2081 3125 2800 -606 254 -174 N
ATOM 280 CA ASN A 348 -11.009 -29.442 23.303 1.00 28.06 C
ANISOU 280 CA ASN A 348 2802 4250 3609 -544 213 -151 C
ATOM 281 C ASN A 348 -10.328 -28.085 23.416 1.00 21.80 C
ANISOU 281 C ASN A 348 2052 3455 2776 -331 193 -87 C
ATOM 282 O ASN A 348 -10.305 -27.319 22.446 1.00 20.21 O
ANISOU 282 O ASN A 348 1789 3369 2520 -260 134 -94 O
ATOM 283 CB ASN A 348 -12.348 -29.430 24.021 1.00 23.36 C
ANISOU 283 CB ASN A 348 2067 3796 3012 -597 263 -88 C
ATOM 284 CG ASN A 348 -13.313 -28.403 23.458 1.00 30.07 C
ANISOU 284 CG ASN A 348 2728 4907 3790 -518 224 -54 C
ATOM 285 OD1 ASN A 348 -13.323 -27.244 23.883 1.00 25.19 O
ANISOU 285 OD1 ASN A 348 2096 4333 3144 -336 238 24 O
ATOM 286 ND2 ASN A 348 -14.217 -28.857 22.642 1.00 34.18 N
ANISOU 286 ND2 ASN A 348 3097 5602 4287 -658 183 -108 N
ATOM 287 N LEU A 349 -9.720 -27.811 24.575 1.00 20.40 N
ANISOU 287 N LEU A 349 1986 3140 2624 -239 241 -26 N
ATOM 288 CA LEU A 349 -8.976 -26.573 24.785 1.00 21.11 C
ANISOU 288 CA LEU A 349 2137 3196 2689 -59 227 20 C
ATOM 289 C LEU A 349 -7.810 -26.450 23.795 1.00 19.75 C
ANISOU 289 C LEU A 349 2039 2952 2512 -28 167 -28 C
ATOM 290 O LEU A 349 -7.633 -25.405 23.147 1.00 14.84 O
ANISOU 290 O LEU A 349 1386 2399 1853 75 127 -6 O
ATOM 291 CB LEU A 349 -8.460 -26.525 26.230 1.00 17.76 C
ANISOU 291 CB LEU A 349 1827 2639 2284 -1 283 71 C
ATOM 292 CG LEU A 349 -7.551 -25.349 26.657 1.00 17.66 C
ANISOU 292 CG LEU A 349 1901 2555 2253 159 271 100 C
ATOM 293 CD1 LEU A 349 -8.328 -24.046 26.548 1.00 15.16 C
ANISOU 293 CD1 LEU A 349 1490 2369 1902 277 274 135 C
ATOM 294 CD2 LEU A 349 -7.032 -25.582 28.116 1.00 17.24 C
ANISOU 294 CD2 LEU A 349 1960 2388 2202 181 319 135 C
ATOM 295 N ALA A 350 -6.975 -27.496 23.684 1.00 17.29 N
ANISOU 295 N ALA A 350 1829 2498 2243 -106 168 -86 N
ATOM 296 CA ALA A 350 -5.840 -27.398 22.777 1.00 19.25 C
ANISOU 296 CA ALA A 350 2140 2693 2483 -69 124 -133 C
ATOM 297 C ALA A 350 -6.296 -27.151 21.327 1.00 16.79 C
ANISOU 297 C ALA A 350 1722 2551 2108 -98 70 -180 C
ATOM 298 O ALA A 350 -5.694 -26.337 20.599 1.00 17.31 O
ANISOU 298 O ALA A 350 1789 2657 2131 -12 33 -164 O
ATOM 299 CB ALA A 350 -4.984 -28.660 22.885 1.00 15.80 C
ANISOU 299 CB ALA A 350 1815 2081 2106 -140 144 -193 C
ATOM 300 N ASP A 351 -7.386 -27.804 20.908 1.00 18.40 N
ANISOU 300 N ASP A 351 1824 2871 2296 -224 64 -230 N
ATOM 301 CA ASP A 351 -7.876 -27.626 19.550 1.00 17.27 C
ANISOU 301 CA ASP A 351 1568 2921 2073 -261 3 -278 C
ATOM 302 C ASP A 351 -8.363 -26.202 19.288 1.00 20.97 C
ANISOU 302 C ASP A 351 1935 3556 2479 -126 -28 -174 C
ATOM 303 O ASP A 351 -8.053 -25.624 18.228 1.00 21.48 O
ANISOU 303 O ASP A 351 1969 3718 2474 -73 -78 -166 O
ATOM 304 CB ASP A 351 -8.984 -28.644 19.283 1.00 25.59 C
ANISOU 304 CB ASP A 351 2526 4071 3126 -443 0 -358 C
ATOM 305 CG ASP A 351 -8.422 -30.067 19.122 1.00 26.18 C
ANISOU 305 CG ASP A 351 2711 3975 3260 -583 22 -486 C
ATOM 306 OD1 ASP A 351 -7.174 -30.231 19.019 1.00 32.99 O
ANISOU 306 OD1 ASP A 351 3705 4683 4148 -522 32 -515 O
ATOM 307 OD2 ASP A 351 -9.220 -30.982 19.067 1.00 28.45 O
ANISOU 307 OD2 ASP A 351 2949 4288 3573 -748 31 -556 O
ATOM 308 N ARG A 352 -9.075 -25.594 20.256 1.00 16.93 N
ANISOU 308 N ARG A 352 1375 3068 1991 -56 7 -86 N
ATOM 309 CA ARG A 352 -9.469 -24.194 20.097 1.00 19.71 C
ANISOU 309 CA ARG A 352 1650 3536 2305 100 -10 17 C
ATOM 310 C ARG A 352 -8.255 -23.268 20.146 1.00 16.53 C
ANISOU 310 C ARG A 352 1370 2995 1916 233 -12 65 C
ATOM 311 O ARG A 352 -8.211 -22.268 19.418 1.00 17.33 O
ANISOU 311 O ARG A 352 1432 3176 1977 334 -46 131 O
ATOM 312 CB ARG A 352 -10.478 -23.803 21.180 1.00 17.42 C
ANISOU 312 CB ARG A 352 1287 3290 2041 153 43 83 C
ATOM 313 CG ARG A 352 -11.915 -24.217 20.767 1.00 19.41 C
ANISOU 313 CG ARG A 352 1344 3775 2255 60 26 75 C
ATOM 314 CD ARG A 352 -12.883 -23.767 21.862 1.00 24.57 C
ANISOU 314 CD ARG A 352 1916 4486 2933 131 92 147 C
ATOM 315 NE ARG A 352 -12.728 -24.529 23.096 1.00 21.13 N
ANISOU 315 NE ARG A 352 1572 3904 2552 54 167 124 N
ATOM 316 CZ ARG A 352 -12.401 -24.042 24.290 1.00 22.48 C
ANISOU 316 CZ ARG A 352 1839 3953 2750 159 232 166 C
ATOM 317 NH1 ARG A 352 -12.164 -22.746 24.441 1.00 18.63 N
ANISOU 317 NH1 ARG A 352 1379 3444 2255 344 236 219 N
ATOM 318 NH2 ARG A 352 -12.314 -24.859 25.358 1.00 19.44 N
ANISOU 318 NH2 ARG A 352 1526 3465 2398 73 296 156 N
ATOM 319 N GLU A 353 -7.229 -23.609 20.922 1.00 16.28 N
ANISOU 319 N GLU A 353 1482 2764 1940 228 21 38 N
ATOM 320 CA GLU A 353 -6.051 -22.738 21.005 1.00 16.05 C
ANISOU 320 CA GLU A 353 1558 2613 1928 334 17 77 C
ATOM 321 C GLU A 353 -5.225 -22.786 19.715 1.00 17.23 C
ANISOU 321 C GLU A 353 1720 2792 2035 316 -28 51 C
ATOM 322 O GLU A 353 -4.612 -21.783 19.316 1.00 14.74 O
ANISOU 322 O GLU A 353 1429 2462 1709 406 -44 113 O
ATOM 323 CB GLU A 353 -5.157 -23.182 22.152 1.00 14.38 C
ANISOU 323 CB GLU A 353 1478 2212 1773 323 54 53 C
ATOM 324 CG GLU A 353 -5.714 -22.882 23.584 1.00 16.14 C
ANISOU 324 CG GLU A 353 1716 2396 2020 370 106 91 C
ATOM 325 CD GLU A 353 -4.585 -23.149 24.542 1.00 21.53 C
ANISOU 325 CD GLU A 353 2532 2911 2737 375 123 78 C
ATOM 326 OE1 GLU A 353 -4.518 -24.341 24.932 1.00 15.24 O
ANISOU 326 OE1 GLU A 353 1767 2062 1960 285 143 47 O
ATOM 327 OE2 GLU A 353 -3.775 -22.221 24.874 1.00 20.33 O
ANISOU 327 OE2 GLU A 353 2450 2682 2593 460 114 102 O
ATOM 328 N LEU A 354 -5.282 -23.904 19.006 1.00 14.58 N
ANISOU 328 N LEU A 354 1361 2508 1672 198 -45 -41 N
ATOM 329 CA LEU A 354 -4.530 -24.005 17.761 1.00 14.16 C
ANISOU 329 CA LEU A 354 1315 2504 1561 182 -79 -80 C
ATOM 330 C LEU A 354 -4.982 -22.965 16.761 1.00 18.06 C
ANISOU 330 C LEU A 354 1712 3180 1972 252 -122 2 C
ATOM 331 O LEU A 354 -4.153 -22.374 16.073 1.00 20.51 O
ANISOU 331 O LEU A 354 2050 3496 2247 306 -135 43 O
ATOM 332 CB LEU A 354 -4.650 -25.421 17.174 1.00 18.77 C
ANISOU 332 CB LEU A 354 1893 3115 2125 39 -84 -218 C
ATOM 333 CG LEU A 354 -3.785 -25.658 15.926 1.00 16.21 C
ANISOU 333 CG LEU A 354 1588 2839 1732 22 -105 -286 C
ATOM 334 CD1 LEU A 354 -2.317 -25.617 16.346 1.00 17.38 C
ANISOU 334 CD1 LEU A 354 1858 2806 1941 85 -72 -277 C
ATOM 335 CD2 LEU A 354 -4.136 -26.967 15.312 1.00 21.77 C
ANISOU 335 CD2 LEU A 354 2277 3586 2409 -120 -110 -439 C
ATOM 336 N VAL A 355 -6.307 -22.726 16.657 1.00 17.87 N
ANISOU 336 N VAL A 355 1561 3317 1912 254 -142 41 N
ATOM 337 CA VAL A 355 -6.811 -21.719 15.733 1.00 18.02 C
ANISOU 337 CA VAL A 355 1476 3520 1850 340 -187 144 C
ATOM 338 C VAL A 355 -6.128 -20.384 15.990 1.00 15.94 C
ANISOU 338 C VAL A 355 1283 3143 1629 488 -168 269 C
ATOM 339 O VAL A 355 -5.728 -19.674 15.061 1.00 18.22 O
ANISOU 339 O VAL A 355 1561 3499 1862 545 -194 347 O
ATOM 340 CB VAL A 355 -8.341 -21.583 15.873 1.00 21.14 C
ANISOU 340 CB VAL A 355 1719 4090 2225 348 -203 185 C
ATOM 341 CG1 VAL A 355 -8.803 -20.622 14.877 1.00 28.13 C
ANISOU 341 CG1 VAL A 355 2495 5170 3024 446 -253 301 C
ATOM 342 CG2 VAL A 355 -9.034 -22.941 15.698 1.00 24.68 C
ANISOU 342 CG2 VAL A 355 2095 4638 2645 171 -219 53 C
ATOM 343 N HIS A 356 -6.119 -19.968 17.248 1.00 16.70 N
ANISOU 343 N HIS A 356 1444 3083 1820 549 -121 295 N
ATOM 344 CA HIS A 356 -5.516 -18.696 17.645 1.00 17.07 C
ANISOU 344 CA HIS A 356 1570 2994 1924 675 -99 392 C
ATOM 345 C HIS A 356 -4.012 -18.722 17.493 1.00 16.08 C
ANISOU 345 C HIS A 356 1560 2732 1817 646 -95 368 C
ATOM 346 O HIS A 356 -3.400 -17.671 17.259 1.00 16.30 O
ANISOU 346 O HIS A 356 1631 2697 1865 721 -93 456 O
ATOM 347 CB HIS A 356 -5.857 -18.350 19.109 1.00 14.48 C
ANISOU 347 CB HIS A 356 1289 2535 1678 733 -47 392 C
ATOM 348 CG HIS A 356 -7.300 -18.027 19.295 1.00 23.79 C
ANISOU 348 CG HIS A 356 2346 3848 2847 799 -37 440 C
ATOM 349 ND1 HIS A 356 -7.819 -16.783 19.001 1.00 23.10 N
ANISOU 349 ND1 HIS A 356 2224 3789 2765 926 -34 548 N
ATOM 350 CD2 HIS A 356 -8.344 -18.794 19.693 1.00 23.66 C
ANISOU 350 CD2 HIS A 356 2234 3939 2816 739 -25 395 C
ATOM 351 CE1 HIS A 356 -9.132 -16.805 19.183 1.00 25.36 C
ANISOU 351 CE1 HIS A 356 2399 4202 3034 946 -22 561 C
ATOM 352 NE2 HIS A 356 -9.474 -18.003 19.635 1.00 22.46 N
ANISOU 352 NE2 HIS A 356 1963 3915 2656 855 -19 482 N
ATOM 353 N MET A 357 -3.396 -19.897 17.641 1.00 15.06 N
ANISOU 353 N MET A 357 1479 2551 1691 542 -89 256 N
ATOM 354 CA MET A 357 -1.962 -20.001 17.390 1.00 15.98 C
ANISOU 354 CA MET A 357 1681 2573 1820 521 -85 233 C
ATOM 355 C MET A 357 -1.602 -19.661 15.941 1.00 17.60 C
ANISOU 355 C MET A 357 1840 2909 1939 526 -112 279 C
ATOM 356 O MET A 357 -0.614 -18.955 15.707 1.00 16.50 O
ANISOU 356 O MET A 357 1747 2708 1814 561 -104 340 O
ATOM 357 CB MET A 357 -1.430 -21.384 17.790 1.00 12.46 C
ANISOU 357 CB MET A 357 1288 2049 1397 428 -70 110 C
ATOM 358 CG MET A 357 0.102 -21.433 17.860 1.00 15.20 C
ANISOU 358 CG MET A 357 1719 2279 1777 431 -58 95 C
ATOM 359 SD MET A 357 0.606 -23.196 17.909 1.00 15.89 S
ANISOU 359 SD MET A 357 1847 2311 1881 340 -39 -46 S
ATOM 360 CE MET A 357 -0.060 -23.571 19.543 1.00 14.41 C
ANISOU 360 CE MET A 357 1702 2005 1768 332 -17 -47 C
ATOM 361 N ILE A 358 -2.412 -20.097 14.972 1.00 18.29 N
ANISOU 361 N ILE A 358 1829 3191 1930 487 -144 256 N
ATOM 362 CA ILE A 358 -2.136 -19.778 13.569 1.00 17.34 C
ANISOU 362 CA ILE A 358 1659 3230 1700 494 -171 305 C
ATOM 363 C ILE A 358 -2.207 -18.269 13.381 1.00 22.14 C
ANISOU 363 C ILE A 358 2254 3840 2316 611 -174 484 C
ATOM 364 O ILE A 358 -1.320 -17.654 12.770 1.00 20.64 O
ANISOU 364 O ILE A 358 2094 3642 2105 636 -166 562 O
ATOM 365 CB ILE A 358 -3.142 -20.491 12.646 1.00 21.52 C
ANISOU 365 CB ILE A 358 2074 3992 2109 427 -215 242 C
ATOM 366 CG1 ILE A 358 -3.133 -22.012 12.837 1.00 33.75 C
ANISOU 366 CG1 ILE A 358 3647 5508 3667 299 -206 55 C
ATOM 367 CG2 ILE A 358 -3.172 -19.906 11.191 1.00 28.74 C
ANISOU 367 CG2 ILE A 358 2911 5129 2879 459 -254 333 C
ATOM 368 CD1 ILE A 358 -1.939 -22.641 12.589 1.00 27.05 C
ANISOU 368 CD1 ILE A 358 2880 4576 2822 260 -177 -34 C
ATOM 369 N ASN A 359 -3.266 -17.644 13.925 1.00 21.27 N
ANISOU 369 N ASN A 359 2101 3734 2247 687 -179 556 N
ATOM 370 CA ASN A 359 -3.411 -16.183 13.816 1.00 20.31 C
ANISOU 370 CA ASN A 359 1996 3558 2165 792 -162 709 C
ATOM 371 C ASN A 359 -2.229 -15.443 14.404 1.00 22.72 C
ANISOU 371 C ASN A 359 2426 3634 2572 811 -122 740 C
ATOM 372 O ASN A 359 -1.757 -14.447 13.812 1.00 20.89 O
ANISOU 372 O ASN A 359 2227 3359 2351 829 -105 835 O
ATOM 373 CB ASN A 359 -4.675 -15.701 14.490 1.00 26.63 C
ANISOU 373 CB ASN A 359 2763 4338 3018 849 -145 731 C
ATOM 374 CG ASN A 359 -5.884 -16.047 13.717 1.00 40.94 C
ANISOU 374 CG ASN A 359 4441 6382 4731 835 -180 738 C
ATOM 375 OD1 ASN A 359 -5.784 -16.608 12.610 1.00 34.56 O
ANISOU 375 OD1 ASN A 359 3572 5752 3809 773 -220 718 O
ATOM 376 ND2 ASN A 359 -7.062 -15.735 14.284 1.00 37.95 N
ANISOU 376 ND2 ASN A 359 4012 6019 4388 886 -165 757 N
ATOM 377 N TRP A 360 -1.757 -15.898 15.569 1.00 19.93 N
ANISOU 377 N TRP A 360 2141 3136 2295 797 -106 658 N
ATOM 378 CA TRP A 360 -0.565 -15.324 16.198 1.00 22.65 C
ANISOU 378 CA TRP A 360 2599 3278 2730 792 -77 664 C
ATOM 379 C TRP A 360 0.669 -15.539 15.320 1.00 21.07 C
ANISOU 379 C TRP A 360 2409 3111 2484 731 -80 672 C
ATOM 380 O TRP A 360 1.463 -14.616 15.101 1.00 18.74 O
ANISOU 380 O TRP A 360 2156 2737 2226 745 -65 762 O
ATOM 381 CB TRP A 360 -0.348 -15.925 17.599 1.00 18.27 C
ANISOU 381 CB TRP A 360 2112 2585 2244 758 -59 548 C
ATOM 382 CG TRP A 360 1.070 -15.792 18.153 1.00 17.69 C
ANISOU 382 CG TRP A 360 2133 2357 2232 716 -47 517 C
ATOM 383 CD1 TRP A 360 1.612 -14.707 18.784 1.00 16.49 C
ANISOU 383 CD1 TRP A 360 2058 2048 2160 732 -33 548 C
ATOM 384 CD2 TRP A 360 2.112 -16.775 18.089 1.00 15.39 C
ANISOU 384 CD2 TRP A 360 1859 2064 1927 635 -51 435 C
ATOM 385 NE1 TRP A 360 2.933 -14.958 19.129 1.00 16.49 N
ANISOU 385 NE1 TRP A 360 2108 1968 2190 678 -35 510 N
ATOM 386 CE2 TRP A 360 3.269 -16.214 18.704 1.00 17.98 C
ANISOU 386 CE2 TRP A 360 2258 2253 2323 621 -44 442 C
ATOM 387 CE3 TRP A 360 2.184 -18.091 17.570 1.00 15.92 C
ANISOU 387 CE3 TRP A 360 1887 2228 1934 576 -57 349 C
ATOM 388 CZ2 TRP A 360 4.500 -16.924 18.835 1.00 17.09 C
ANISOU 388 CZ2 TRP A 360 2162 2115 2217 562 -46 381 C
ATOM 389 CZ3 TRP A 360 3.415 -18.790 17.695 1.00 16.49 C
ANISOU 389 CZ3 TRP A 360 1994 2250 2022 528 -49 285 C
ATOM 390 CH2 TRP A 360 4.555 -18.192 18.303 1.00 14.70 C
ANISOU 390 CH2 TRP A 360 1820 1905 1859 528 -45 311 C
ATOM 391 N ALA A 361 0.875 -16.757 14.831 1.00 17.36 N
ANISOU 391 N ALA A 361 1905 2749 1941 655 -91 568 N
ATOM 392 CA ALA A 361 2.106 -16.988 14.057 1.00 19.88 C
ANISOU 392 CA ALA A 361 2233 3102 2218 606 -79 560 C
ATOM 393 C ALA A 361 2.177 -16.072 12.828 1.00 21.39 C
ANISOU 393 C ALA A 361 2378 3414 2334 641 -83 708 C
ATOM 394 O ALA A 361 3.239 -15.512 12.531 1.00 19.62 O
ANISOU 394 O ALA A 361 2182 3144 2127 629 -59 777 O
ATOM 395 CB ALA A 361 2.229 -18.456 13.646 1.00 16.08 C
ANISOU 395 CB ALA A 361 1725 2716 1668 533 -82 413 C
ATOM 396 N LYS A 362 1.040 -15.853 12.148 1.00 18.29 N
ANISOU 396 N LYS A 362 1909 3181 1860 686 -112 775 N
ATOM 397 CA LYS A 362 0.983 -14.944 10.994 1.00 23.03 C
ANISOU 397 CA LYS A 362 2470 3889 2393 715 -109 920 C
ATOM 398 C LYS A 362 1.348 -13.513 11.343 1.00 25.61 C
ANISOU 398 C LYS A 362 2868 4018 2843 747 -70 1032 C
ATOM 399 O LYS A 362 1.641 -12.714 10.434 1.00 26.05 O
ANISOU 399 O LYS A 362 2912 4114 2872 750 -52 1147 O
ATOM 400 CB LYS A 362 -0.430 -14.998 10.397 1.00 22.27 C
ANISOU 400 CB LYS A 362 2283 3962 2217 735 -138 928 C
ATOM 401 CG LYS A 362 -0.728 -16.307 9.669 1.00 26.61 C
ANISOU 401 CG LYS A 362 2750 4745 2614 672 -179 812 C
ATOM 402 CD LYS A 362 -2.205 -16.278 9.258 1.00 35.11 C
ANISOU 402 CD LYS A 362 3732 5971 3636 685 -209 822 C
ATOM 403 CE LYS A 362 -2.631 -15.268 8.217 1.00 43.90 C
ANISOU 403 CE LYS A 362 4797 7182 4700 730 -200 964 C
ATOM 404 NZ LYS A 362 -2.066 -15.346 6.890 1.00 55.27 N
ANISOU 404 NZ LYS A 362 6201 8790 6010 695 -199 990 N
ATOM 405 N ARG A 363 1.320 -13.166 12.623 1.00 20.66 N
ANISOU 405 N ARG A 363 2316 3185 2348 764 -58 992 N
ATOM 406 CA ARG A 363 1.685 -11.828 13.076 1.00 25.32 C
ANISOU 406 CA ARG A 363 2987 3574 3058 779 -28 1061 C
ATOM 407 C ARG A 363 3.109 -11.780 13.649 1.00 24.68 C
ANISOU 407 C ARG A 363 2977 3349 3049 721 -11 1038 C
ATOM 408 O ARG A 363 3.541 -10.709 14.084 1.00 25.50 O
ANISOU 408 O ARG A 363 3153 3282 3254 712 8 1077 O
ATOM 409 CB ARG A 363 0.664 -11.353 14.125 1.00 23.70 C
ANISOU 409 CB ARG A 363 2817 3250 2938 832 -26 1018 C
ATOM 410 CG ARG A 363 -0.722 -11.137 13.459 1.00 31.15 C
ANISOU 410 CG ARG A 363 3678 4339 3820 898 -36 1076 C
ATOM 411 CD ARG A 363 -1.772 -10.631 14.439 1.00 37.48 C
ANISOU 411 CD ARG A 363 4499 5045 4697 964 -25 1046 C
ATOM 412 NE ARG A 363 -1.375 -9.324 14.926 1.00 45.04 N
ANISOU 412 NE ARG A 363 5553 5794 5765 988 1 1084 N
ATOM 413 CZ ARG A 363 -2.059 -8.634 15.828 1.00 49.17 C
ANISOU 413 CZ ARG A 363 6116 6199 6366 1049 17 1056 C
ATOM 414 NH1 ARG A 363 -3.182 -9.155 16.343 1.00 43.56 N
ANISOU 414 NH1 ARG A 363 5349 5568 5634 1092 17 1001 N
ATOM 415 NH2 ARG A 363 -1.597 -7.448 16.238 1.00 42.42 N
ANISOU 415 NH2 ARG A 363 5356 5150 5611 1062 36 1078 N
ATOM 416 N VAL A 364 3.833 -12.909 13.716 1.00 16.28 N
ANISOU 416 N VAL A 364 1896 2349 1942 683 -20 971 N
ATOM 417 CA VAL A 364 5.248 -12.897 14.127 1.00 14.96 C
ANISOU 417 CA VAL A 364 1773 2076 1835 622 -3 956 C
ATOM 418 C VAL A 364 6.072 -12.353 12.957 1.00 22.32 C
ANISOU 418 C VAL A 364 2671 3089 2719 590 22 1087 C
ATOM 419 O VAL A 364 6.010 -12.908 11.842 1.00 25.00 O
ANISOU 419 O VAL A 364 2939 3633 2928 585 23 1101 O
ATOM 420 CB VAL A 364 5.735 -14.308 14.541 1.00 13.84 C
ANISOU 420 CB VAL A 364 1619 1972 1667 567 -11 786 C
ATOM 421 CG1 VAL A 364 7.264 -14.286 14.754 1.00 16.82 C
ANISOU 421 CG1 VAL A 364 2012 2285 2093 497 7 768 C
ATOM 422 CG2 VAL A 364 4.968 -14.819 15.841 1.00 15.45 C
ANISOU 422 CG2 VAL A 364 1864 2082 1925 589 -29 673 C
ATOM 423 N PRO A 365 6.802 -11.247 13.132 1.00 23.80 N
ANISOU 423 N PRO A 365 2909 3132 3003 555 47 1174 N
ATOM 424 CA PRO A 365 7.449 -10.594 11.984 1.00 26.28 C
ANISOU 424 CA PRO A 365 3189 3521 3277 517 80 1313 C
ATOM 425 C PRO A 365 8.323 -11.587 11.240 1.00 28.64 C
ANISOU 425 C PRO A 365 3412 4009 3460 470 95 1287 C
ATOM 426 O PRO A 365 9.063 -12.364 11.851 1.00 24.68 O
ANISOU 426 O PRO A 365 2909 3480 2987 421 94 1147 O
ATOM 427 CB PRO A 365 8.264 -9.467 12.629 1.00 30.41 C
ANISOU 427 CB PRO A 365 3786 3823 3946 456 100 1358 C
ATOM 428 CG PRO A 365 7.491 -9.150 13.905 1.00 32.05 C
ANISOU 428 CG PRO A 365 4077 3850 4252 496 75 1253 C
ATOM 429 CD PRO A 365 6.978 -10.489 14.383 1.00 27.85 C
ANISOU 429 CD PRO A 365 3514 3408 3661 536 46 1128 C
ATOM 430 N GLY A 366 8.157 -11.625 9.912 1.00 24.81 N
ANISOU 430 N GLY A 366 2861 3732 2835 488 110 1385 N
ATOM 431 CA GLY A 366 8.903 -12.521 9.047 1.00 26.15 C
ANISOU 431 CA GLY A 366 2957 4104 2877 444 138 1324 C
ATOM 432 C GLY A 366 8.223 -13.835 8.702 1.00 22.79 C
ANISOU 432 C GLY A 366 2488 3846 2324 471 111 1166 C
ATOM 433 O GLY A 366 8.534 -14.429 7.658 1.00 24.47 O
ANISOU 433 O GLY A 366 2638 4268 2391 456 135 1139 O
ATOM 434 N PHE A 367 7.306 -14.300 9.549 1.00 20.85 N
ANISOU 434 N PHE A 367 2275 3517 2129 504 68 1057 N
ATOM 435 CA PHE A 367 6.674 -15.593 9.341 1.00 23.24 C
ANISOU 435 CA PHE A 367 2545 3947 2337 506 44 893 C
ATOM 436 C PHE A 367 5.909 -15.663 8.026 1.00 23.20 C
ANISOU 436 C PHE A 367 2468 4192 2154 527 28 946 C
ATOM 437 O PHE A 367 6.042 -16.651 7.294 1.00 22.79 O
ANISOU 437 O PHE A 367 2374 4308 1976 497 36 827 O
ATOM 438 CB PHE A 367 5.754 -15.921 10.517 1.00 19.31 C
ANISOU 438 CB PHE A 367 2091 3312 1933 529 6 801 C
ATOM 439 CG PHE A 367 5.263 -17.343 10.508 1.00 15.85 C
ANISOU 439 CG PHE A 367 1633 2954 1435 504 -11 619 C
ATOM 440 CD1 PHE A 367 6.119 -18.373 10.888 1.00 19.62 C
ANISOU 440 CD1 PHE A 367 2134 3374 1946 466 14 474 C
ATOM 441 CD2 PHE A 367 3.982 -17.640 10.046 1.00 17.06 C
ANISOU 441 CD2 PHE A 367 1736 3247 1498 517 -49 599 C
ATOM 442 CE1 PHE A 367 5.697 -19.662 10.889 1.00 20.15 C
ANISOU 442 CE1 PHE A 367 2198 3480 1978 440 7 312 C
ATOM 443 CE2 PHE A 367 3.511 -18.987 10.023 1.00 17.94 C
ANISOU 443 CE2 PHE A 367 1832 3421 1563 470 -63 419 C
ATOM 444 CZ PHE A 367 4.421 -20.001 10.443 1.00 15.22 C
ANISOU 444 CZ PHE A 367 1533 2979 1269 431 -29 275 C
ATOM 445 N VAL A 368 5.090 -14.638 7.687 1.00 22.59 N
ANISOU 445 N VAL A 368 2376 4145 2065 581 5 1112 N
ATOM 446 CA VAL A 368 4.334 -14.709 6.426 1.00 23.28 C
ANISOU 446 CA VAL A 368 2382 4452 2012 585 -10 1125 C
ATOM 447 C VAL A 368 5.178 -14.427 5.186 1.00 27.36 C
ANISOU 447 C VAL A 368 2856 5113 2428 556 33 1201 C
ATOM 448 O VAL A 368 4.660 -14.512 4.052 1.00 28.16 O
ANISOU 448 O VAL A 368 2886 5413 2401 556 20 1210 O
ATOM 449 CB VAL A 368 3.116 -13.763 6.361 1.00 30.90 C
ANISOU 449 CB VAL A 368 3330 5381 3029 641 -33 1226 C
ATOM 450 CG1 VAL A 368 1.991 -14.308 7.261 1.00 35.48 C
ANISOU 450 CG1 VAL A 368 3912 5917 3653 664 -77 1122 C
ATOM 451 CG2 VAL A 368 3.515 -12.296 6.638 1.00 27.47 C
ANISOU 451 CG2 VAL A 368 2955 4747 2734 668 3 1387 C
ATOM 452 N ASP A 369 6.477 -14.119 5.361 1.00 24.96 N
ANISOU 452 N ASP A 369 2584 4725 2174 525 85 1256 N
ATOM 453 CA ASP A 369 7.381 -14.041 4.228 1.00 28.61 C
ANISOU 453 CA ASP A 369 2995 5342 2533 490 133 1304 C
ATOM 454 C ASP A 369 7.735 -15.411 3.690 1.00 24.93 C
ANISOU 454 C ASP A 369 2488 5067 1916 461 148 1121 C
ATOM 455 O ASP A 369 8.215 -15.498 2.563 1.00 26.01 O
ANISOU 455 O ASP A 369 2570 5375 1939 441 180 1127 O
ATOM 456 CB ASP A 369 8.684 -13.323 4.599 1.00 31.14 C
ANISOU 456 CB ASP A 369 3347 5524 2961 451 190 1411 C
ATOM 457 CG ASP A 369 8.476 -11.884 5.007 1.00 31.66 C
ANISOU 457 CG ASP A 369 3464 5382 3182 463 187 1575 C
ATOM 458 OD1 ASP A 369 7.535 -11.223 4.498 1.00 31.77 O
ANISOU 458 OD1 ASP A 369 3466 5419 3185 509 163 1658 O
ATOM 459 OD2 ASP A 369 9.271 -11.459 5.878 1.00 36.05 O
ANISOU 459 OD2 ASP A 369 4072 5751 3875 425 210 1607 O
ATOM 460 N LEU A 370 7.571 -16.455 4.503 1.00 23.88 N
ANISOU 460 N LEU A 370 2391 4892 1791 459 132 952 N
ATOM 461 CA LEU A 370 7.930 -17.819 4.129 1.00 24.85 C
ANISOU 461 CA LEU A 370 2497 5141 1806 432 158 736 C
ATOM 462 C LEU A 370 6.866 -18.423 3.202 1.00 22.81 C
ANISOU 462 C LEU A 370 2189 5062 1415 419 109 630 C
ATOM 463 O LEU A 370 5.721 -17.958 3.145 1.00 23.93 O
ANISOU 463 O LEU A 370 2309 5219 1563 436 49 702 O
ATOM 464 CB LEU A 370 8.046 -18.658 5.407 1.00 24.66 C
ANISOU 464 CB LEU A 370 2534 4885 1951 422 150 561 C
ATOM 465 CG LEU A 370 9.084 -18.157 6.432 1.00 23.67 C
ANISOU 465 CG LEU A 370 2449 4535 2009 419 180 620 C
ATOM 466 CD1 LEU A 370 8.912 -19.022 7.672 1.00 19.16 C
ANISOU 466 CD1 LEU A 370 1936 3769 1574 419 156 460 C
ATOM 467 CD2 LEU A 370 10.453 -18.280 5.807 1.00 23.87 C
ANISOU 467 CD2 LEU A 370 2428 4657 1983 403 256 622 C
ATOM 468 N THR A 371 7.239 -19.478 2.472 1.00 23.90 N
ANISOU 468 N THR A 371 2307 5328 1448 388 137 449 N
ATOM 469 CA THR A 371 6.241 -20.238 1.721 1.00 24.66 C
ANISOU 469 CA THR A 371 2366 5570 1435 354 88 307 C
ATOM 470 C THR A 371 5.212 -20.879 2.660 1.00 23.56 C
ANISOU 470 C THR A 371 2261 5335 1354 335 33 188 C
ATOM 471 O THR A 371 5.460 -21.114 3.860 1.00 21.98 O
ANISOU 471 O THR A 371 2127 4964 1260 349 46 149 O
ATOM 472 CB THR A 371 6.912 -21.332 0.878 1.00 27.00 C
ANISOU 472 CB THR A 371 2654 5970 1634 321 135 109 C
ATOM 473 OG1 THR A 371 7.534 -22.253 1.791 1.00 29.16 O
ANISOU 473 OG1 THR A 371 2997 6084 1999 322 180 -56 O
ATOM 474 CG2 THR A 371 7.951 -20.745 -0.082 1.00 29.42 C
ANISOU 474 CG2 THR A 371 2917 6391 1870 337 192 222 C
ATOM 475 N LEU A 372 4.027 -21.186 2.146 1.00 24.54 N
ANISOU 475 N LEU A 372 2333 5580 1409 300 -29 133 N
ATOM 476 CA LEU A 372 3.038 -21.835 3.031 1.00 24.38 C
ANISOU 476 CA LEU A 372 2339 5469 1454 269 -76 20 C
ATOM 477 C LEU A 372 3.564 -23.196 3.482 1.00 23.13 C
ANISOU 477 C LEU A 372 2251 5214 1325 219 -39 -230 C
ATOM 478 O LEU A 372 3.337 -23.547 4.619 1.00 21.84 O
ANISOU 478 O LEU A 372 2142 4869 1286 211 -47 -292 O
ATOM 479 CB LEU A 372 1.710 -22.007 2.308 1.00 28.77 C
ANISOU 479 CB LEU A 372 2816 6166 1949 232 -145 11 C
ATOM 480 CG LEU A 372 1.065 -20.726 1.821 1.00 32.77 C
ANISOU 480 CG LEU A 372 3242 6790 2417 283 -173 224 C
ATOM 481 CD1 LEU A 372 -0.357 -20.990 1.356 1.00 39.47 C
ANISOU 481 CD1 LEU A 372 4016 7771 3211 225 -235 132 C
ATOM 482 CD2 LEU A 372 1.083 -19.659 2.877 1.00 43.55 C
ANISOU 482 CD2 LEU A 372 4640 7987 3919 370 -168 436 C
ATOM 483 N HIS A 373 4.198 -23.937 2.576 1.00 26.71 N
ANISOU 483 N HIS A 373 2705 5737 1705 190 6 -371 N
ATOM 484 CA AHIS A 373 4.766 -25.223 2.971 0.51 27.94 C
ANISOU 484 CA AHIS A 373 2939 5753 1926 163 58 -599 C
ATOM 485 CA BHIS A 373 4.716 -25.226 3.008 0.49 27.94 C
ANISOU 485 CA BHIS A 373 2938 5749 1928 161 56 -600 C
ATOM 486 C HIS A 373 5.683 -25.062 4.179 1.00 25.89 C
ANISOU 486 C HIS A 373 2743 5287 1809 227 111 -556 C
ATOM 487 O HIS A 373 5.615 -25.837 5.141 1.00 23.24 O
ANISOU 487 O HIS A 373 2473 4728 1629 211 117 -662 O
ATOM 488 CB AHIS A 373 5.542 -25.847 1.808 0.51 29.88 C
ANISOU 488 CB AHIS A 373 3178 6090 2084 153 113 -718 C
ATOM 489 CB BHIS A 373 5.353 -25.975 1.837 0.49 30.04 C
ANISOU 489 CB BHIS A 373 3200 6106 2106 140 104 -741 C
ATOM 490 CG AHIS A 373 6.356 -27.034 2.215 0.51 30.73 C
ANISOU 490 CG AHIS A 373 3370 6019 2287 160 185 -915 C
ATOM 491 CG BHIS A 373 4.504 -27.102 1.330 0.49 37.22 C
ANISOU 491 CG BHIS A 373 4117 7049 2977 47 74 -949 C
ATOM 492 ND1AHIS A 373 7.613 -26.921 2.775 0.51 29.43 N
ANISOU 492 ND1AHIS A 373 3236 5736 2210 238 259 -877 N
ATOM 493 ND1BHIS A 373 4.991 -28.376 1.111 0.49 39.23 N
ANISOU 493 ND1BHIS A 373 4439 7204 3261 20 129 -1170 N
ATOM 494 CD2AHIS A 373 6.097 -28.361 2.134 0.51 30.99 C
ANISOU 494 CD2AHIS A 373 3460 5959 2356 103 197 -1141 C
ATOM 495 CD2BHIS A 373 3.190 -27.141 1.003 0.49 33.21 C
ANISOU 495 CD2BHIS A 373 3552 6656 2410 -27 -3 -962 C
ATOM 496 CE1AHIS A 373 8.082 -28.126 3.042 0.51 30.27 C
ANISOU 496 CE1AHIS A 373 3413 5682 2407 244 312 -1064 C
ATOM 497 CE1BHIS A 373 4.014 -29.144 0.658 0.49 37.16 C
ANISOU 497 CE1BHIS A 373 4171 6990 2958 -78 87 -1314 C
ATOM 498 NE2AHIS A 373 7.185 -29.017 2.658 0.51 30.73 N
ANISOU 498 NE2AHIS A 373 3498 5740 2439 162 278 -1225 N
ATOM 499 NE2BHIS A 373 2.912 -28.419 0.584 0.49 40.71 N
ANISOU 499 NE2BHIS A 373 4538 7581 3350 -112 6 -1194 N
ATOM 500 N ASP A 374 6.541 -24.031 4.165 1.00 21.93 N
ANISOU 500 N ASP A 374 2220 4791 1323 288 143 -367 N
ATOM 501 CA ASP A 374 7.461 -23.846 5.295 1.00 23.49 C
ANISOU 501 CA ASP A 374 2466 4742 1717 332 179 -308 C
ATOM 502 C ASP A 374 6.744 -23.366 6.558 1.00 24.74 C
ANISOU 502 C ASP A 374 2659 4708 2035 333 121 -214 C
ATOM 503 O ASP A 374 7.079 -23.792 7.687 1.00 18.39 O
ANISOU 503 O ASP A 374 1914 3683 1392 344 132 -259 O
ATOM 504 CB ASP A 374 8.573 -22.874 4.908 1.00 25.25 C
ANISOU 504 CB ASP A 374 2648 5034 1914 372 228 -141 C
ATOM 505 CG ASP A 374 9.591 -23.517 3.976 1.00 34.76 C
ANISOU 505 CG ASP A 374 3824 6379 3005 387 312 -255 C
ATOM 506 OD1 ASP A 374 9.518 -24.744 3.777 1.00 30.04 O
ANISOU 506 OD1 ASP A 374 3257 5776 2382 377 335 -475 O
ATOM 507 OD2 ASP A 374 10.433 -22.815 3.393 1.00 35.79 O
ANISOU 507 OD2 ASP A 374 3901 6626 3070 406 361 -129 O
ATOM 508 N GLN A 375 5.723 -22.502 6.399 1.00 20.36 N
ANISOU 508 N GLN A 375 2066 4241 1430 330 61 -82 N
ATOM 509 CA GLN A 375 4.936 -22.100 7.557 1.00 19.64 C
ANISOU 509 CA GLN A 375 2003 3985 1476 340 14 -13 C
ATOM 510 C GLN A 375 4.283 -23.321 8.197 1.00 18.17 C
ANISOU 510 C GLN A 375 1854 3696 1354 290 0 -193 C
ATOM 511 O GLN A 375 4.270 -23.452 9.427 1.00 16.81 O
ANISOU 511 O GLN A 375 1736 3317 1333 298 0 -194 O
ATOM 512 CB GLN A 375 3.865 -21.081 7.136 1.00 20.78 C
ANISOU 512 CB GLN A 375 2085 4267 1543 361 -42 144 C
ATOM 513 CG GLN A 375 4.385 -19.719 6.632 1.00 21.70 C
ANISOU 513 CG GLN A 375 2177 4443 1624 414 -27 365 C
ATOM 514 CD GLN A 375 3.231 -18.756 6.220 1.00 26.55 C
ANISOU 514 CD GLN A 375 2732 5187 2169 458 -84 533 C
ATOM 515 OE1 GLN A 375 2.161 -18.777 6.802 1.00 25.07 O
ANISOU 515 OE1 GLN A 375 2533 4959 2033 469 -129 523 O
ATOM 516 NE2 GLN A 375 3.451 -17.948 5.167 1.00 28.23 N
ANISOU 516 NE2 GLN A 375 2898 5537 2289 480 -70 680 N
ATOM 517 N VAL A 376 3.738 -24.232 7.364 1.00 21.69 N
ANISOU 517 N VAL A 376 2273 4288 1680 228 -12 -348 N
ATOM 518 CA VAL A 376 3.154 -25.476 7.876 1.00 24.61 C
ANISOU 518 CA VAL A 376 2684 4551 2116 159 -17 -529 C
ATOM 519 C VAL A 376 4.205 -26.309 8.609 1.00 25.86 C
ANISOU 519 C VAL A 376 2931 4484 2410 180 46 -624 C
ATOM 520 O VAL A 376 3.967 -26.820 9.716 1.00 22.67 O
ANISOU 520 O VAL A 376 2583 3884 2146 166 47 -654 O
ATOM 521 CB VAL A 376 2.516 -26.279 6.730 1.00 28.97 C
ANISOU 521 CB VAL A 376 3195 5306 2508 74 -38 -696 C
ATOM 522 CG1 VAL A 376 2.121 -27.681 7.236 1.00 26.75 C
ANISOU 522 CG1 VAL A 376 2975 4871 2317 -12 -26 -901 C
ATOM 523 CG2 VAL A 376 1.329 -25.521 6.170 1.00 25.54 C
ANISOU 523 CG2 VAL A 376 2658 5099 1948 56 -115 -591 C
ATOM 524 N HIS A 377 5.369 -26.492 7.984 1.00 23.02 N
ANISOU 524 N HIS A 377 2579 4164 2005 219 103 -667 N
ATOM 525 CA HIS A 377 6.432 -27.274 8.610 1.00 22.30 C
ANISOU 525 CA HIS A 377 2555 3881 2039 260 165 -746 C
ATOM 526 C HIS A 377 6.800 -26.719 9.990 1.00 20.03 C
ANISOU 526 C HIS A 377 2299 3400 1912 308 154 -607 C
ATOM 527 O HIS A 377 6.972 -27.475 10.944 1.00 20.73 O
ANISOU 527 O HIS A 377 2451 3297 2129 317 169 -661 O
ATOM 528 CB HIS A 377 7.682 -27.276 7.739 1.00 24.93 C
ANISOU 528 CB HIS A 377 2862 4318 2293 314 231 -771 C
ATOM 529 CG HIS A 377 8.792 -28.132 8.284 1.00 28.46 C
ANISOU 529 CG HIS A 377 3361 4592 2862 376 297 -856 C
ATOM 530 ND1 HIS A 377 8.740 -29.512 8.250 0.53 33.22 N
ANISOU 530 ND1 HIS A 377 4028 5090 3505 365 336 -1056 N
ATOM 531 CD2 HIS A 377 9.951 -27.816 8.914 1.00 30.33 C
ANISOU 531 CD2 HIS A 377 3590 4737 3196 450 328 -762 C
ATOM 532 CE1 HIS A 377 9.835 -30.009 8.796 0.46 34.78 C
ANISOU 532 CE1 HIS A 377 4256 5143 3817 449 392 -1072 C
ATOM 533 NE2 HIS A 377 10.590 -29.004 9.203 0.92 32.09 N
ANISOU 533 NE2 HIS A 377 3864 4822 3507 500 384 -897 N
ATOM 534 N LEU A 378 7.000 -25.406 10.091 1.00 20.29 N
ANISOU 534 N LEU A 378 2292 3479 1936 340 132 -429 N
ATOM 535 CA LEU A 378 7.392 -24.811 11.370 1.00 17.32 C
ANISOU 535 CA LEU A 378 1948 2933 1699 376 120 -315 C
ATOM 536 C LEU A 378 6.328 -25.013 12.436 1.00 19.87 C
ANISOU 536 C LEU A 378 2313 3132 2106 349 81 -319 C
ATOM 537 O LEU A 378 6.646 -25.432 13.557 1.00 17.79 O
ANISOU 537 O LEU A 378 2104 2698 1957 367 87 -330 O
ATOM 538 CB LEU A 378 7.699 -23.329 11.165 1.00 17.92 C
ANISOU 538 CB LEU A 378 1982 3078 1750 398 107 -137 C
ATOM 539 CG LEU A 378 9.015 -22.936 10.468 1.00 21.23 C
ANISOU 539 CG LEU A 378 2357 3583 2126 422 155 -86 C
ATOM 540 CD1 LEU A 378 9.049 -21.402 10.417 1.00 19.67 C
ANISOU 540 CD1 LEU A 378 2133 3412 1928 423 135 107 C
ATOM 541 CD2 LEU A 378 10.293 -23.472 11.188 1.00 16.96 C
ANISOU 541 CD2 LEU A 378 1834 2919 1692 457 192 -130 C
ATOM 542 N LEU A 379 5.042 -24.732 12.115 1.00 16.09 N
ANISOU 542 N LEU A 379 1800 2751 1562 310 40 -303 N
ATOM 543 CA LEU A 379 3.991 -24.944 13.105 1.00 14.88 C
ANISOU 543 CA LEU A 379 1670 2501 1482 283 12 -306 C
ATOM 544 C LEU A 379 3.827 -26.427 13.457 1.00 19.54 C
ANISOU 544 C LEU A 379 2313 2984 2127 231 36 -459 C
ATOM 545 O LEU A 379 3.592 -26.765 14.629 1.00 16.99 O
ANISOU 545 O LEU A 379 2039 2509 1908 226 38 -449 O
ATOM 546 CB LEU A 379 2.662 -24.371 12.589 1.00 14.94 C
ANISOU 546 CB LEU A 379 1607 2666 1404 258 -34 -256 C
ATOM 547 CG LEU A 379 2.586 -22.880 12.916 1.00 16.95 C
ANISOU 547 CG LEU A 379 1843 2920 1678 326 -53 -78 C
ATOM 548 CD1 LEU A 379 1.425 -22.343 12.056 1.00 15.43 C
ANISOU 548 CD1 LEU A 379 1561 2926 1375 324 -96 -20 C
ATOM 549 CD2 LEU A 379 2.316 -22.624 14.439 1.00 14.11 C
ANISOU 549 CD2 LEU A 379 1535 2382 1446 351 -53 -36 C
ATOM 550 N GLU A 380 3.930 -27.319 12.468 1.00 17.56 N
ANISOU 550 N GLU A 380 2058 2806 1807 189 57 -599 N
ATOM 551 CA GLU A 380 3.819 -28.754 12.740 1.00 21.38 C
ANISOU 551 CA GLU A 380 2606 3158 2359 136 88 -752 C
ATOM 552 C GLU A 380 4.906 -29.223 13.705 1.00 21.70 C
ANISOU 552 C GLU A 380 2722 2992 2530 205 131 -738 C
ATOM 553 O GLU A 380 4.655 -30.047 14.598 1.00 21.14 O
ANISOU 553 O GLU A 380 2715 2754 2563 183 145 -769 O
ATOM 554 CB GLU A 380 3.861 -29.540 11.416 1.00 25.97 C
ANISOU 554 CB GLU A 380 3177 3855 2835 86 109 -924 C
ATOM 555 CG GLU A 380 3.595 -31.028 11.621 1.00 27.67 C
ANISOU 555 CG GLU A 380 3468 3916 3129 15 143 -1097 C
ATOM 556 CD GLU A 380 3.445 -31.816 10.354 1.00 46.35 C
ANISOU 556 CD GLU A 380 5832 6392 5389 -55 160 -1297 C
ATOM 557 OE1 GLU A 380 3.724 -31.276 9.264 1.00 46.37 O
ANISOU 557 OE1 GLU A 380 5772 6604 5241 -33 153 -1304 O
ATOM 558 OE2 GLU A 380 2.996 -32.974 10.462 1.00 45.10 O
ANISOU 558 OE2 GLU A 380 5734 6109 5294 -142 181 -1447 O
ATOM 559 N SER A 381 6.113 -28.664 13.589 1.00 17.98 N
ANISOU 559 N SER A 381 2238 2539 2056 289 149 -673 N
ATOM 560 CA SER A 381 7.187 -28.994 14.520 1.00 19.07 C
ANISOU 560 CA SER A 381 2422 2515 2306 364 177 -641 C
ATOM 561 C SER A 381 6.984 -28.359 15.907 1.00 18.84 C
ANISOU 561 C SER A 381 2414 2390 2356 379 140 -508 C
ATOM 562 O SER A 381 7.353 -28.950 16.924 1.00 18.42 O
ANISOU 562 O SER A 381 2415 2187 2399 411 152 -496 O
ATOM 563 CB SER A 381 8.517 -28.565 13.888 1.00 22.95 C
ANISOU 563 CB SER A 381 2868 3092 2759 435 207 -616 C
ATOM 564 OG SER A 381 9.595 -28.720 14.811 1.00 33.47 O
ANISOU 564 OG SER A 381 4220 4302 4194 511 222 -563 O
ATOM 565 N ALA A 382 6.449 -27.152 15.983 1.00 14.41 N
ANISOU 565 N ALA A 382 1811 1911 1751 366 99 -406 N
ATOM 566 CA ALA A 382 6.489 -26.347 17.202 1.00 14.97 C
ANISOU 566 CA ALA A 382 1900 1906 1882 394 71 -291 C
ATOM 567 C ALA A 382 5.199 -26.307 18.029 1.00 14.50 C
ANISOU 567 C ALA A 382 1861 1805 1844 355 50 -268 C
ATOM 568 O ALA A 382 5.251 -25.840 19.180 1.00 13.57 O
ANISOU 568 O ALA A 382 1771 1610 1774 381 36 -195 O
ATOM 569 CB ALA A 382 6.839 -24.892 16.846 1.00 17.95 C
ANISOU 569 CB ALA A 382 2230 2374 2216 416 49 -186 C
ATOM 570 N TRP A 383 4.043 -26.728 17.478 1.00 15.15 N
ANISOU 570 N TRP A 383 1918 1954 1884 291 47 -328 N
ATOM 571 CA TRP A 383 2.759 -26.400 18.097 1.00 12.47 C
ANISOU 571 CA TRP A 383 1562 1629 1548 259 28 -285 C
ATOM 572 C TRP A 383 2.686 -26.895 19.530 1.00 11.72 C
ANISOU 572 C TRP A 383 1530 1386 1537 260 44 -262 C
ATOM 573 O TRP A 383 2.168 -26.176 20.381 1.00 11.90 O
ANISOU 573 O TRP A 383 1550 1403 1568 281 34 -188 O
ATOM 574 CB TRP A 383 1.586 -26.953 17.259 1.00 15.35 C
ANISOU 574 CB TRP A 383 1874 2105 1854 173 20 -365 C
ATOM 575 CG TRP A 383 1.537 -28.450 17.312 1.00 17.62 C
ANISOU 575 CG TRP A 383 2212 2293 2191 102 52 -485 C
ATOM 576 CD1 TRP A 383 2.177 -29.318 16.489 1.00 18.84 C
ANISOU 576 CD1 TRP A 383 2394 2430 2335 84 77 -602 C
ATOM 577 CD2 TRP A 383 0.775 -29.257 18.251 1.00 14.94 C
ANISOU 577 CD2 TRP A 383 1906 1846 1924 37 71 -499 C
ATOM 578 NE1 TRP A 383 1.886 -30.658 16.870 1.00 19.08 N
ANISOU 578 NE1 TRP A 383 2487 2319 2444 14 111 -695 N
ATOM 579 CE2 TRP A 383 1.033 -30.622 17.953 1.00 20.65 C
ANISOU 579 CE2 TRP A 383 2688 2463 2693 -21 107 -621 C
ATOM 580 CE3 TRP A 383 -0.085 -28.944 19.332 1.00 17.71 C
ANISOU 580 CE3 TRP A 383 2246 2179 2305 26 70 -416 C
ATOM 581 CZ2 TRP A 383 0.452 -31.670 18.673 1.00 20.28 C
ANISOU 581 CZ2 TRP A 383 2691 2283 2731 -101 138 -649 C
ATOM 582 CZ3 TRP A 383 -0.629 -29.998 20.060 1.00 18.23 C
ANISOU 582 CZ3 TRP A 383 2352 2135 2440 -52 103 -441 C
ATOM 583 CH2 TRP A 383 -0.390 -31.341 19.696 1.00 20.96 C
ANISOU 583 CH2 TRP A 383 2757 2369 2838 -122 135 -552 C
ATOM 584 N LEU A 384 3.252 -28.086 19.839 1.00 12.29 N
ANISOU 584 N LEU A 384 1663 1337 1669 251 74 -319 N
ATOM 585 CA LEU A 384 3.084 -28.515 21.240 1.00 14.19 C
ANISOU 585 CA LEU A 384 1961 1454 1976 254 88 -270 C
ATOM 586 C LEU A 384 4.034 -27.770 22.181 1.00 12.47 C
ANISOU 586 C LEU A 384 1769 1194 1774 337 70 -181 C
ATOM 587 O LEU A 384 3.684 -27.496 23.339 1.00 13.23 O
ANISOU 587 O LEU A 384 1890 1257 1879 346 67 -119 O
ATOM 588 CB LEU A 384 3.281 -30.043 21.396 1.00 17.14 C
ANISOU 588 CB LEU A 384 2400 1690 2422 222 129 -333 C
ATOM 589 CG LEU A 384 2.966 -30.684 22.810 1.00 14.60 C
ANISOU 589 CG LEU A 384 2141 1240 2164 210 152 -267 C
ATOM 590 CD1 LEU A 384 1.532 -30.293 23.365 1.00 14.28 C
ANISOU 590 CD1 LEU A 384 2063 1268 2095 142 152 -225 C
ATOM 591 CD2 LEU A 384 3.086 -32.213 22.824 1.00 15.64 C
ANISOU 591 CD2 LEU A 384 2345 1215 2381 174 200 -322 C
ATOM 592 N GLU A 385 5.239 -27.441 21.718 1.00 14.06 N
ANISOU 592 N GLU A 385 1960 1411 1971 390 60 -180 N
ATOM 593 CA GLU A 385 6.128 -26.614 22.536 1.00 14.93 C
ANISOU 593 CA GLU A 385 2079 1505 2090 447 32 -104 C
ATOM 594 C GLU A 385 5.505 -25.261 22.804 1.00 14.32 C
ANISOU 594 C GLU A 385 1981 1485 1976 444 7 -52 C
ATOM 595 O GLU A 385 5.638 -24.718 23.906 1.00 13.05 O
ANISOU 595 O GLU A 385 1849 1289 1822 466 -10 -5 O
ATOM 596 CB GLU A 385 7.464 -26.396 21.829 1.00 14.09 C
ANISOU 596 CB GLU A 385 1938 1433 1982 488 28 -110 C
ATOM 597 CG GLU A 385 8.383 -27.622 21.732 1.00 16.69 C
ANISOU 597 CG GLU A 385 2285 1696 2360 530 56 -152 C
ATOM 598 CD GLU A 385 9.542 -27.364 20.785 1.00 24.33 C
ANISOU 598 CD GLU A 385 3195 2738 3311 567 65 -169 C
ATOM 599 OE1 GLU A 385 10.597 -26.961 21.246 1.00 26.98 O
ANISOU 599 OE1 GLU A 385 3505 3082 3665 610 45 -115 O
ATOM 600 OE2 GLU A 385 9.374 -27.599 19.583 1.00 27.14 O
ANISOU 600 OE2 GLU A 385 3526 3156 3629 549 94 -239 O
ATOM 601 N ILE A 386 4.834 -24.697 21.791 1.00 13.15 N
ANISOU 601 N ILE A 386 1783 1427 1784 422 6 -61 N
ATOM 602 CA ILE A 386 4.153 -23.417 21.956 1.00 14.63 C
ANISOU 602 CA ILE A 386 1952 1658 1950 437 -10 -5 C
ATOM 603 C ILE A 386 3.009 -23.507 22.985 1.00 12.85 C
ANISOU 603 C ILE A 386 1744 1409 1728 429 2 5 C
ATOM 604 O ILE A 386 2.867 -22.630 23.850 1.00 12.75 O
ANISOU 604 O ILE A 386 1755 1371 1719 464 -3 45 O
ATOM 605 CB ILE A 386 3.694 -22.891 20.582 1.00 16.64 C
ANISOU 605 CB ILE A 386 2142 2029 2152 429 -15 2 C
ATOM 606 CG1 ILE A 386 4.963 -22.537 19.747 1.00 11.86 C
ANISOU 606 CG1 ILE A 386 1521 1451 1535 443 -19 16 C
ATOM 607 CG2 ILE A 386 2.815 -21.633 20.726 1.00 16.49 C
ANISOU 607 CG2 ILE A 386 2101 2045 2119 462 -25 71 C
ATOM 608 CD1 ILE A 386 4.667 -22.282 18.162 1.00 17.89 C
ANISOU 608 CD1 ILE A 386 2217 2361 2220 430 -19 21 C
ATOM 609 N LEU A 387 2.144 -24.521 22.871 1.00 13.39 N
ANISOU 609 N LEU A 387 1798 1494 1796 379 23 -35 N
ATOM 610 CA LEU A 387 1.138 -24.767 23.917 1.00 14.69 C
ANISOU 610 CA LEU A 387 1974 1642 1967 361 46 -18 C
ATOM 611 C LEU A 387 1.768 -24.874 25.298 1.00 16.78 C
ANISOU 611 C LEU A 387 2311 1814 2252 392 51 14 C
ATOM 612 O LEU A 387 1.278 -24.260 26.260 1.00 13.70 O
ANISOU 612 O LEU A 387 1932 1429 1842 418 61 47 O
ATOM 613 CB LEU A 387 0.329 -26.049 23.620 1.00 13.60 C
ANISOU 613 CB LEU A 387 1815 1511 1840 276 72 -69 C
ATOM 614 CG LEU A 387 -0.715 -25.927 22.496 1.00 15.00 C
ANISOU 614 CG LEU A 387 1901 1822 1976 229 62 -102 C
ATOM 615 CD1 LEU A 387 -1.549 -27.232 22.505 1.00 16.49 C
ANISOU 615 CD1 LEU A 387 2078 2001 2188 120 88 -158 C
ATOM 616 CD2 LEU A 387 -1.630 -24.691 22.620 1.00 14.48 C
ANISOU 616 CD2 LEU A 387 1770 1858 1873 280 53 -40 C
ATOM 617 N MET A 388 2.868 -25.673 25.432 1.00 13.60 N
ANISOU 617 N MET A 388 1952 1335 1881 397 46 5 N
ATOM 618 CA MET A 388 3.476 -25.858 26.741 1.00 14.05 C
ANISOU 618 CA MET A 388 2067 1327 1944 428 42 48 C
ATOM 619 C MET A 388 4.106 -24.591 27.283 1.00 16.42 C
ANISOU 619 C MET A 388 2377 1645 2216 475 6 71 C
ATOM 620 O MET A 388 3.979 -24.323 28.491 1.00 14.60 O
ANISOU 620 O MET A 388 2184 1408 1956 492 6 98 O
ATOM 621 CB MET A 388 4.478 -27.048 26.786 1.00 11.73 C
ANISOU 621 CB MET A 388 1809 952 1695 441 45 49 C
ATOM 622 CG MET A 388 3.913 -28.340 26.202 1.00 14.65 C
ANISOU 622 CG MET A 388 2187 1270 2109 386 86 7 C
ATOM 623 SD MET A 388 5.050 -29.727 26.246 1.00 14.64 S
ANISOU 623 SD MET A 388 2240 1142 2181 425 103 7 S
ATOM 624 CE MET A 388 4.102 -31.121 26.912 1.00 21.18 C
ANISOU 624 CE MET A 388 3131 1854 3064 359 160 33 C
ATOM 625 N ILE A 389 4.806 -23.805 26.463 1.00 11.46 N
ANISOU 625 N ILE A 389 1721 1040 1594 489 -21 60 N
ATOM 626 CA ILE A 389 5.399 -22.600 27.047 1.00 15.36 C
ANISOU 626 CA ILE A 389 2232 1530 2074 513 -53 76 C
ATOM 627 C ILE A 389 4.307 -21.624 27.479 1.00 14.14 C
ANISOU 627 C ILE A 389 2088 1391 1895 526 -36 77 C
ATOM 628 O ILE A 389 4.409 -20.986 28.544 1.00 14.76 O
ANISOU 628 O ILE A 389 2209 1448 1949 543 -46 72 O
ATOM 629 CB ILE A 389 6.455 -21.942 26.125 1.00 17.35 C
ANISOU 629 CB ILE A 389 2450 1796 2346 511 -80 77 C
ATOM 630 CG1 ILE A 389 7.300 -20.950 26.972 1.00 16.81 C
ANISOU 630 CG1 ILE A 389 2408 1705 2276 512 -119 84 C
ATOM 631 CG2 ILE A 389 5.865 -21.172 24.918 1.00 11.89 C
ANISOU 631 CG2 ILE A 389 1719 1147 1653 506 -66 85 C
ATOM 632 CD1 ILE A 389 8.446 -20.309 26.185 1.00 13.64 C
ANISOU 632 CD1 ILE A 389 1966 1316 1901 492 -143 96 C
ATOM 633 N GLY A 390 3.222 -21.521 26.693 1.00 15.15 N
ANISOU 633 N GLY A 390 2172 1562 2022 523 -10 77 N
ATOM 634 CA GLY A 390 2.078 -20.762 27.140 1.00 13.37 C
ANISOU 634 CA GLY A 390 1943 1360 1777 555 17 83 C
ATOM 635 C GLY A 390 1.575 -21.224 28.495 1.00 12.22 C
ANISOU 635 C GLY A 390 1833 1210 1600 556 45 80 C
ATOM 636 O GLY A 390 1.252 -20.408 29.369 1.00 12.41 O
ANISOU 636 O GLY A 390 1889 1229 1597 596 59 70 O
ATOM 637 N LEU A 391 1.417 -22.546 28.652 1.00 11.09 N
ANISOU 637 N LEU A 391 1687 1070 1457 513 61 88 N
ATOM 638 CA LEU A 391 0.947 -23.110 29.909 1.00 11.31 C
ANISOU 638 CA LEU A 391 1746 1100 1449 506 95 108 C
ATOM 639 C LEU A 391 1.875 -22.754 31.068 1.00 14.72 C
ANISOU 639 C LEU A 391 2247 1505 1842 537 68 111 C
ATOM 640 O LEU A 391 1.424 -22.278 32.134 1.00 13.63 O
ANISOU 640 O LEU A 391 2137 1396 1646 563 91 107 O
ATOM 641 CB LEU A 391 0.831 -24.632 29.760 1.00 13.07 C
ANISOU 641 CB LEU A 391 1968 1299 1701 447 115 127 C
ATOM 642 CG LEU A 391 0.416 -25.340 31.056 1.00 17.41 C
ANISOU 642 CG LEU A 391 2554 1845 2216 431 155 175 C
ATOM 643 CD1 LEU A 391 -0.966 -24.841 31.559 1.00 16.71 C
ANISOU 643 CD1 LEU A 391 2425 1842 2083 433 209 180 C
ATOM 644 CD2 LEU A 391 0.442 -26.857 30.808 1.00 12.60 C
ANISOU 644 CD2 LEU A 391 1957 1169 1660 369 177 200 C
ATOM 645 N VAL A 392 3.169 -23.005 30.901 1.00 15.65 N
ANISOU 645 N VAL A 392 2384 1583 1981 535 19 115 N
ATOM 646 CA AVAL A 392 4.137 -22.733 31.960 0.46 15.78 C
ANISOU 646 CA AVAL A 392 2447 1596 1953 554 -22 119 C
ATOM 647 CA BVAL A 392 4.068 -22.747 32.017 0.54 16.00 C
ANISOU 647 CA BVAL A 392 2476 1626 1977 554 -18 120 C
ATOM 648 C VAL A 392 4.086 -21.262 32.355 1.00 15.96 C
ANISOU 648 C VAL A 392 2492 1628 1944 574 -34 67 C
ATOM 649 O VAL A 392 4.098 -20.904 33.554 1.00 15.56 O
ANISOU 649 O VAL A 392 2488 1604 1822 587 -37 48 O
ATOM 650 CB AVAL A 392 5.530 -23.192 31.489 0.46 17.49 C
ANISOU 650 CB AVAL A 392 2650 1785 2209 552 -72 133 C
ATOM 651 CB BVAL A 392 5.476 -23.321 31.769 0.54 17.59 C
ANISOU 651 CB BVAL A 392 2672 1802 2209 554 -69 141 C
ATOM 652 CG1AVAL A 392 6.653 -22.594 32.323 0.46 16.15 C
ANISOU 652 CG1AVAL A 392 2501 1638 1998 562 -133 125 C
ATOM 653 CG1BVAL A 392 5.394 -24.819 31.513 0.54 14.60 C
ANISOU 653 CG1BVAL A 392 2291 1387 1870 548 -42 185 C
ATOM 654 CG2AVAL A 392 5.592 -24.713 31.551 0.46 14.75 C
ANISOU 654 CG2AVAL A 392 2309 1408 1886 552 -51 184 C
ATOM 655 CG2BVAL A 392 6.229 -22.581 30.674 0.54 14.91 C
ANISOU 655 CG2BVAL A 392 2295 1451 1919 548 -102 109 C
ATOM 656 N TRP A 393 3.997 -20.386 31.346 1.00 16.81 N
ANISOU 656 N TRP A 393 2573 1711 2102 577 -36 43 N
ATOM 657 CA TRP A 393 3.842 -18.948 31.591 1.00 19.93 C
ANISOU 657 CA TRP A 393 3000 2081 2493 600 -36 -4 C
ATOM 658 C TRP A 393 2.583 -18.655 32.424 1.00 18.16 C
ANISOU 658 C TRP A 393 2796 1887 2219 643 24 -26 C
ATOM 659 O TRP A 393 2.647 -17.968 33.465 1.00 16.34 O
ANISOU 659 O TRP A 393 2622 1651 1935 662 26 -79 O
ATOM 660 CB TRP A 393 3.832 -18.214 30.242 1.00 15.10 C
ANISOU 660 CB TRP A 393 2352 1436 1952 604 -37 8 C
ATOM 661 CG TRP A 393 3.454 -16.781 30.334 1.00 18.56 C
ANISOU 661 CG TRP A 393 2816 1826 2409 631 -20 -23 C
ATOM 662 CD1 TRP A 393 2.307 -16.188 29.842 1.00 18.17 C
ANISOU 662 CD1 TRP A 393 2729 1793 2383 667 25 -6 C
ATOM 663 CD2 TRP A 393 4.214 -15.727 30.960 1.00 15.19 C
ANISOU 663 CD2 TRP A 393 2461 1323 1988 624 -48 -79 C
ATOM 664 NE1 TRP A 393 2.308 -14.863 30.159 1.00 21.84 N
ANISOU 664 NE1 TRP A 393 3235 2189 2875 685 34 -42 N
ATOM 665 CE2 TRP A 393 3.466 -14.549 30.833 1.00 21.84 C
ANISOU 665 CE2 TRP A 393 3307 2124 2866 651 -7 -94 C
ATOM 666 CE3 TRP A 393 5.443 -15.684 31.632 1.00 21.29 C
ANISOU 666 CE3 TRP A 393 3267 2085 2738 568 -106 -117 C
ATOM 667 CZ2 TRP A 393 3.914 -13.324 31.326 1.00 23.71 C
ANISOU 667 CZ2 TRP A 393 3616 2264 3130 642 -14 -157 C
ATOM 668 CZ3 TRP A 393 5.881 -14.481 32.137 1.00 23.38 C
ANISOU 668 CZ3 TRP A 393 3594 2273 3015 545 -123 -188 C
ATOM 669 CH2 TRP A 393 5.117 -13.307 31.972 1.00 23.70 C
ANISOU 669 CH2 TRP A 393 3680 2221 3103 593 -75 -216 C
ATOM 670 N ARG A 394 1.422 -19.193 32.005 1.00 16.43 N
ANISOU 670 N ARG A 394 2524 1713 2008 655 75 8 N
ATOM 671 CA ARG A 394 0.155 -18.959 32.718 1.00 19.99 C
ANISOU 671 CA ARG A 394 2968 2215 2412 700 142 -3 C
ATOM 672 C ARG A 394 0.209 -19.481 34.141 1.00 19.06 C
ANISOU 672 C ARG A 394 2897 2140 2204 692 159 -8 C
ATOM 673 O ARG A 394 -0.467 -18.940 35.024 1.00 16.68 O
ANISOU 673 O ARG A 394 2618 1878 1841 737 209 -44 O
ATOM 674 CB ARG A 394 -1.011 -19.667 32.000 1.00 16.48 C
ANISOU 674 CB ARG A 394 2436 1836 1991 689 184 42 C
ATOM 675 CG ARG A 394 -1.417 -19.130 30.699 1.00 24.08 C
ANISOU 675 CG ARG A 394 3334 2802 3011 711 177 55 C
ATOM 676 CD ARG A 394 -2.851 -19.598 30.413 1.00 24.97 C
ANISOU 676 CD ARG A 394 3352 3019 3118 711 228 84 C
ATOM 677 NE ARG A 394 -2.991 -21.032 30.112 1.00 18.42 N
ANISOU 677 NE ARG A 394 2483 2223 2292 617 227 108 N
ATOM 678 CZ ARG A 394 -2.537 -21.581 28.986 1.00 15.82 C
ANISOU 678 CZ ARG A 394 2130 1879 2000 564 185 109 C
ATOM 679 NH1 ARG A 394 -1.841 -20.849 28.090 1.00 14.94 N
ANISOU 679 NH1 ARG A 394 2026 1736 1916 593 141 104 N
ATOM 680 NH2 ARG A 394 -2.752 -22.879 28.718 1.00 12.85 N
ANISOU 680 NH2 ARG A 394 1728 1517 1637 478 193 113 N
ATOM 681 N SER A 395 0.999 -20.540 34.381 1.00 16.25 N
ANISOU 681 N SER A 395 2557 1784 1834 643 123 35 N
ATOM 682 CA SER A 395 1.062 -21.221 35.666 1.00 14.13 C
ANISOU 682 CA SER A 395 2326 1568 1473 635 137 66 C
ATOM 683 C SER A 395 2.084 -20.619 36.624 1.00 21.84 C
ANISOU 683 C SER A 395 3369 2554 2375 645 82 19 C
ATOM 684 O SER A 395 2.172 -21.055 37.782 1.00 18.12 O
ANISOU 684 O SER A 395 2932 2150 1801 646 87 44 O
ATOM 685 CB SER A 395 1.398 -22.704 35.439 1.00 17.27 C
ANISOU 685 CB SER A 395 2710 1948 1902 589 127 151 C
ATOM 686 OG SER A 395 0.403 -23.320 34.626 1.00 15.31 O
ANISOU 686 OG SER A 395 2404 1698 1716 558 177 178 O
ATOM 687 N MET A 396 2.840 -19.630 36.166 1.00 15.22 N
ANISOU 687 N MET A 396 2545 1657 1579 645 30 -46 N
ATOM 688 CA MET A 396 4.009 -19.164 36.923 1.00 24.91 C
ANISOU 688 CA MET A 396 3820 2896 2748 625 -41 -94 C
ATOM 689 C MET A 396 3.621 -18.691 38.312 1.00 23.49 C
ANISOU 689 C MET A 396 3699 2787 2438 648 -16 -157 C
ATOM 690 O MET A 396 4.380 -18.860 39.272 1.00 25.17 O
ANISOU 690 O MET A 396 3942 3069 2551 629 -68 -165 O
ATOM 691 CB MET A 396 4.687 -17.995 36.201 1.00 21.90 C
ANISOU 691 CB MET A 396 3445 2431 2445 606 -85 -162 C
ATOM 692 CG MET A 396 6.193 -17.858 36.353 1.00 33.22 C
ANISOU 692 CG MET A 396 4880 3869 3874 553 -178 -179 C
ATOM 693 SD MET A 396 6.736 -16.625 35.151 1.00 33.73 S
ANISOU 693 SD MET A 396 4933 3819 4063 516 -201 -222 S
ATOM 694 CE MET A 396 6.543 -15.075 35.990 1.00 32.22 C
ANISOU 694 CE MET A 396 4833 3569 3840 508 -193 -360 C
ATOM 695 N GLU A 397 2.447 -18.077 38.440 1.00 21.18 N
ANISOU 695 N GLU A 397 3417 2496 2136 695 64 -205 N
ATOM 696 CA GLU A 397 2.003 -17.552 39.731 1.00 26.01 C
ANISOU 696 CA GLU A 397 4086 3180 2616 728 105 -285 C
ATOM 697 C GLU A 397 1.123 -18.517 40.502 1.00 24.16 C
ANISOU 697 C GLU A 397 3832 3064 2283 746 177 -208 C
ATOM 698 O GLU A 397 0.448 -18.106 41.453 1.00 26.78 O
ANISOU 698 O GLU A 397 4196 3475 2505 788 241 -267 O
ATOM 699 CB GLU A 397 1.314 -16.200 39.529 1.00 33.57 C
ANISOU 699 CB GLU A 397 5072 4065 3619 785 160 -395 C
ATOM 700 CG GLU A 397 2.159 -15.309 38.621 1.00 34.73 C
ANISOU 700 CG GLU A 397 5236 4075 3886 755 97 -440 C
ATOM 701 CD GLU A 397 1.400 -14.154 38.060 1.00 50.31 C
ANISOU 701 CD GLU A 397 7224 5944 5948 823 156 -496 C
ATOM 702 OE1 GLU A 397 0.266 -14.386 37.578 1.00 58.16 O
ANISOU 702 OE1 GLU A 397 8158 6964 6978 886 227 -436 O
ATOM 703 OE2 GLU A 397 1.924 -13.017 38.137 1.00 57.37 O
ANISOU 703 OE2 GLU A 397 8189 6733 6878 812 133 -597 O
ATOM 704 N HIS A 398 1.178 -19.806 40.175 1.00 18.72 N
ANISOU 704 N HIS A 398 3098 2390 1626 713 170 -79 N
ATOM 705 CA HIS A 398 0.336 -20.818 40.793 1.00 20.48 C
ANISOU 705 CA HIS A 398 3299 2704 1779 711 244 18 C
ATOM 706 C HIS A 398 1.229 -21.974 41.160 1.00 19.08 C
ANISOU 706 C HIS A 398 3135 2546 1568 674 187 130 C
ATOM 707 O HIS A 398 1.255 -22.994 40.455 1.00 20.96 O
ANISOU 707 O HIS A 398 3338 2724 1903 643 187 226 O
ATOM 708 CB HIS A 398 -0.784 -21.226 39.834 1.00 21.73 C
ANISOU 708 CB HIS A 398 3380 2832 2044 705 313 68 C
ATOM 709 CG HIS A 398 -1.594 -20.052 39.369 1.00 28.35 C
ANISOU 709 CG HIS A 398 4193 3652 2927 762 359 -24 C
ATOM 710 ND1 HIS A 398 -2.711 -19.615 40.049 1.00 32.39 N
ANISOU 710 ND1 HIS A 398 4688 4253 3364 817 454 -59 N
ATOM 711 CD2 HIS A 398 -1.427 -19.199 38.326 1.00 27.45 C
ANISOU 711 CD2 HIS A 398 4067 3444 2920 784 326 -80 C
ATOM 712 CE1 HIS A 398 -3.207 -18.556 39.436 1.00 32.08 C
ANISOU 712 CE1 HIS A 398 4628 4166 3394 881 477 -132 C
ATOM 713 NE2 HIS A 398 -2.439 -18.273 38.399 1.00 30.52 N
ANISOU 713 NE2 HIS A 398 4436 3853 3305 860 399 -141 N
ATOM 714 N PRO A 399 1.991 -21.851 42.254 1.00 23.44 N
ANISOU 714 N PRO A 399 3738 3183 1984 680 137 118 N
ATOM 715 CA PRO A 399 2.978 -22.885 42.573 1.00 22.87 C
ANISOU 715 CA PRO A 399 3671 3133 1886 664 69 236 C
ATOM 716 C PRO A 399 2.312 -24.238 42.743 1.00 19.97 C
ANISOU 716 C PRO A 399 3289 2774 1525 653 140 394 C
ATOM 717 O PRO A 399 1.298 -24.363 43.444 1.00 21.41 O
ANISOU 717 O PRO A 399 3476 3041 1618 655 229 424 O
ATOM 718 CB PRO A 399 3.598 -22.394 43.898 1.00 28.73 C
ANISOU 718 CB PRO A 399 4462 4014 2440 676 17 188 C
ATOM 719 CG PRO A 399 3.407 -20.856 43.864 1.00 24.00 C
ANISOU 719 CG PRO A 399 3892 3398 1830 681 20 -5 C
ATOM 720 CD PRO A 399 2.058 -20.695 43.190 1.00 27.01 C
ANISOU 720 CD PRO A 399 4244 3713 2304 704 131 -18 C
ATOM 721 N GLY A 400 2.924 -25.263 42.131 1.00 25.22 N
ANISOU 721 N GLY A 400 3938 3348 2295 641 105 497 N
ATOM 722 CA GLY A 400 2.430 -26.620 42.241 1.00 23.27 C
ANISOU 722 CA GLY A 400 3691 3069 2080 620 167 651 C
ATOM 723 C GLY A 400 1.195 -26.874 41.399 1.00 25.22 C
ANISOU 723 C GLY A 400 3897 3246 2439 573 257 641 C
ATOM 724 O GLY A 400 0.617 -27.956 41.491 1.00 27.47 O
ANISOU 724 O GLY A 400 4180 3499 2757 532 322 756 O
ATOM 725 N LYS A 401 0.745 -25.906 40.604 1.00 17.61 N
ANISOU 725 N LYS A 401 2896 2263 1532 572 264 513 N
ATOM 726 CA LYS A 401 -0.455 -26.131 39.795 1.00 20.70 C
ANISOU 726 CA LYS A 401 3229 2620 2016 528 339 506 C
ATOM 727 C LYS A 401 -0.220 -25.734 38.353 1.00 18.22 C
ANISOU 727 C LYS A 401 2877 2213 1834 522 295 423 C
ATOM 728 O LYS A 401 0.629 -24.892 38.032 1.00 18.35 O
ANISOU 728 O LYS A 401 2907 2206 1860 558 225 347 O
ATOM 729 CB LYS A 401 -1.674 -25.379 40.346 1.00 21.47 C
ANISOU 729 CB LYS A 401 3295 2833 2029 544 422 459 C
ATOM 730 CG LYS A 401 -1.982 -25.789 41.823 1.00 27.94 C
ANISOU 730 CG LYS A 401 4149 3776 2693 547 481 546 C
ATOM 731 CD LYS A 401 -3.306 -25.259 42.277 1.00 42.66 C
ANISOU 731 CD LYS A 401 5963 5760 4485 561 586 512 C
ATOM 732 CE LYS A 401 -3.676 -25.810 43.627 1.00 45.51 C
ANISOU 732 CE LYS A 401 6347 6251 4693 551 658 617 C
ATOM 733 NZ LYS A 401 -2.655 -25.349 44.607 1.00 45.50 N
ANISOU 733 NZ LYS A 401 6429 6317 4543 607 592 587 N
ATOM 734 N LEU A 402 -1.026 -26.318 37.461 1.00 16.71 N
ANISOU 734 N LEU A 402 2631 1979 1740 466 339 437 N
ATOM 735 CA LEU A 402 -0.952 -25.936 36.058 1.00 14.15 C
ANISOU 735 CA LEU A 402 2262 1597 1518 460 304 362 C
ATOM 736 C LEU A 402 -2.281 -25.278 35.656 1.00 16.81 C
ANISOU 736 C LEU A 402 2521 2007 1859 457 358 316 C
ATOM 737 O LEU A 402 -3.361 -25.897 35.755 1.00 19.63 O
ANISOU 737 O LEU A 402 2826 2411 2221 402 427 359 O
ATOM 738 CB LEU A 402 -0.637 -27.112 35.148 1.00 14.79 C
ANISOU 738 CB LEU A 402 2339 1575 1707 402 291 393 C
ATOM 739 CG LEU A 402 0.770 -27.745 35.389 1.00 20.24 C
ANISOU 739 CG LEU A 402 3093 2185 2412 431 236 441 C
ATOM 740 CD1 LEU A 402 0.880 -28.907 34.458 1.00 19.69 C
ANISOU 740 CD1 LEU A 402 3022 2004 2457 381 245 454 C
ATOM 741 CD2 LEU A 402 1.869 -26.739 35.055 1.00 15.24 C
ANISOU 741 CD2 LEU A 402 2463 1557 1772 489 157 372 C
ATOM 742 N LEU A 403 -2.193 -24.032 35.218 1.00 13.50 N
ANISOU 742 N LEU A 403 2088 1599 1444 517 330 237 N
ATOM 743 CA LEU A 403 -3.355 -23.233 34.812 1.00 17.35 C
ANISOU 743 CA LEU A 403 2499 2155 1938 548 374 199 C
ATOM 744 C LEU A 403 -3.569 -23.457 33.309 1.00 15.60 C
ANISOU 744 C LEU A 403 2206 1910 1809 508 346 190 C
ATOM 745 O LEU A 403 -3.202 -22.645 32.447 1.00 14.03 O
ANISOU 745 O LEU A 403 1999 1684 1648 548 301 149 O
ATOM 746 CB LEU A 403 -3.152 -21.752 35.165 1.00 14.02 C
ANISOU 746 CB LEU A 403 2112 1737 1476 643 364 127 C
ATOM 747 CG LEU A 403 -4.365 -20.780 35.107 1.00 15.28 C
ANISOU 747 CG LEU A 403 2208 1969 1629 718 427 93 C
ATOM 748 CD1 LEU A 403 -4.096 -19.453 35.856 1.00 28.11 C
ANISOU 748 CD1 LEU A 403 3905 3573 3204 812 435 12 C
ATOM 749 CD2 LEU A 403 -4.770 -20.429 33.745 1.00 24.41 C
ANISOU 749 CD2 LEU A 403 3286 3119 2870 729 406 93 C
ATOM 750 N PHE A 404 -4.144 -24.623 32.997 1.00 14.66 N
ANISOU 750 N PHE A 404 2041 1803 1724 418 374 229 N
ATOM 751 CA PHE A 404 -4.520 -24.883 31.614 1.00 17.02 C
ANISOU 751 CA PHE A 404 2264 2112 2090 367 351 204 C
ATOM 752 C PHE A 404 -5.523 -23.828 31.131 1.00 15.65 C
ANISOU 752 C PHE A 404 1993 2048 1907 426 366 184 C
ATOM 753 O PHE A 404 -5.443 -23.358 29.977 1.00 16.58 O
ANISOU 753 O PHE A 404 2069 2176 2056 444 321 158 O
ATOM 754 CB PHE A 404 -5.094 -26.297 31.497 1.00 15.40 C
ANISOU 754 CB PHE A 404 2027 1901 1921 244 386 235 C
ATOM 755 CG PHE A 404 -4.056 -27.406 31.618 1.00 13.86 C
ANISOU 755 CG PHE A 404 1927 1570 1768 198 367 257 C
ATOM 756 CD1 PHE A 404 -3.352 -27.849 30.476 1.00 18.31 C
ANISOU 756 CD1 PHE A 404 2505 2056 2395 170 318 208 C
ATOM 757 CD2 PHE A 404 -3.861 -28.070 32.848 1.00 17.41 C
ANISOU 757 CD2 PHE A 404 2445 1980 2190 186 406 333 C
ATOM 758 CE1 PHE A 404 -2.391 -28.875 30.562 1.00 17.40 C
ANISOU 758 CE1 PHE A 404 2473 1809 2328 149 309 226 C
ATOM 759 CE2 PHE A 404 -2.946 -29.106 32.940 1.00 16.78 C
ANISOU 759 CE2 PHE A 404 2447 1770 2157 162 391 370 C
ATOM 760 CZ PHE A 404 -2.221 -29.530 31.778 1.00 14.02 C
ANISOU 760 CZ PHE A 404 2111 1328 1887 147 344 312 C
ATOM 761 N ALA A 405 -6.455 -23.438 31.989 1.00 15.92 N
ANISOU 761 N ALA A 405 1987 2171 1892 466 431 201 N
ATOM 762 CA ALA A 405 -7.379 -22.338 31.723 1.00 17.05 C
ANISOU 762 CA ALA A 405 2041 2412 2025 557 456 189 C
ATOM 763 C ALA A 405 -7.729 -21.727 33.062 1.00 15.37 C
ANISOU 763 C ALA A 405 1858 2239 1745 640 526 185 C
ATOM 764 O ALA A 405 -7.558 -22.373 34.095 1.00 17.46 O
ANISOU 764 O ALA A 405 2178 2499 1959 597 561 208 O
ATOM 765 CB ALA A 405 -8.673 -22.810 31.022 1.00 16.20 C
ANISOU 765 CB ALA A 405 1778 2440 1936 495 479 212 C
ATOM 766 N PRO A 406 -8.379 -20.546 33.069 1.00 18.17 N
ANISOU 766 N PRO A 406 2165 2649 2090 762 558 163 N
ATOM 767 CA PRO A 406 -8.708 -19.929 34.365 1.00 16.85 C
ANISOU 767 CA PRO A 406 2034 2519 1850 851 635 136 C
ATOM 768 C PRO A 406 -9.689 -20.746 35.154 1.00 22.47 C
ANISOU 768 C PRO A 406 2669 3364 2504 796 722 183 C
ATOM 769 O PRO A 406 -9.676 -20.693 36.392 1.00 23.75 O
ANISOU 769 O PRO A 406 2888 3555 2579 823 782 172 O
ATOM 770 CB PRO A 406 -9.271 -18.549 33.978 1.00 18.87 C
ANISOU 770 CB PRO A 406 2244 2791 2135 1001 655 105 C
ATOM 771 CG PRO A 406 -8.594 -18.248 32.698 1.00 17.18 C
ANISOU 771 CG PRO A 406 2044 2485 1998 993 565 112 C
ATOM 772 CD PRO A 406 -8.512 -19.574 31.962 1.00 16.61 C
ANISOU 772 CD PRO A 406 1919 2446 1948 845 519 155 C
ATOM 773 N ASN A 407 -10.548 -21.505 34.475 1.00 21.04 N
ANISOU 773 N ASN A 407 2356 3276 2363 709 732 233 N
ATOM 774 CA ASN A 407 -11.461 -22.425 35.122 1.00 23.75 C
ANISOU 774 CA ASN A 407 2616 3741 2668 619 814 291 C
ATOM 775 C ASN A 407 -10.989 -23.880 35.038 1.00 21.22 C
ANISOU 775 C ASN A 407 2340 3346 2376 447 786 340 C
ATOM 776 O ASN A 407 -11.815 -24.806 35.163 1.00 22.99 O
ANISOU 776 O ASN A 407 2474 3653 2606 329 839 396 O
ATOM 777 CB ASN A 407 -12.864 -22.273 34.527 1.00 21.42 C
ANISOU 777 CB ASN A 407 2123 3617 2397 629 854 314 C
ATOM 778 CG ASN A 407 -12.954 -22.704 33.035 1.00 21.59 C
ANISOU 778 CG ASN A 407 2062 3641 2500 539 767 317 C
ATOM 779 OD1 ASN A 407 -11.983 -22.613 32.264 1.00 22.60 O
ANISOU 779 OD1 ASN A 407 2277 3641 2669 535 679 286 O
ATOM 780 ND2 ASN A 407 -14.177 -23.145 32.629 1.00 26.02 N
ANISOU 780 ND2 ASN A 407 2440 4373 3074 465 797 352 N
ATOM 781 N LEU A 408 -9.683 -24.106 34.822 1.00 22.60 N
ANISOU 781 N LEU A 408 2647 3362 2577 429 708 321 N
ATOM 782 CA LEU A 408 -9.164 -25.469 34.739 1.00 21.25 C
ANISOU 782 CA LEU A 408 2532 3096 2447 291 686 366 C
ATOM 783 C LEU A 408 -7.735 -25.465 35.285 1.00 18.23 C
ANISOU 783 C LEU A 408 2306 2582 2039 333 637 362 C
ATOM 784 O LEU A 408 -6.769 -25.530 34.520 1.00 18.32 O
ANISOU 784 O LEU A 408 2372 2482 2106 330 558 330 O
ATOM 785 CB LEU A 408 -9.214 -26.004 33.309 1.00 18.26 C
ANISOU 785 CB LEU A 408 2095 2682 2162 201 626 339 C
ATOM 786 CG LEU A 408 -9.063 -27.521 33.225 1.00 22.45 C
ANISOU 786 CG LEU A 408 2659 3123 2748 44 632 377 C
ATOM 787 CD1 LEU A 408 -10.095 -28.241 34.043 1.00 25.38 C
ANISOU 787 CD1 LEU A 408 2967 3578 3099 -52 727 453 C
ATOM 788 CD2 LEU A 408 -9.123 -27.948 31.775 1.00 21.79 C
ANISOU 788 CD2 LEU A 408 2521 3015 2742 -41 573 319 C
ATOM 789 N LEU A 409 -7.655 -25.353 36.602 1.00 20.10 N
ANISOU 789 N LEU A 409 2600 2857 2180 373 686 395 N
ATOM 790 CA LEU A 409 -6.400 -25.318 37.332 1.00 19.91 C
ANISOU 790 CA LEU A 409 2708 2754 2103 414 642 400 C
ATOM 791 C LEU A 409 -6.204 -26.680 37.974 1.00 23.38 C
ANISOU 791 C LEU A 409 3194 3158 2533 323 669 510 C
ATOM 792 O LEU A 409 -6.952 -27.050 38.881 1.00 24.59 O
ANISOU 792 O LEU A 409 3323 3405 2615 293 755 581 O
ATOM 793 CB LEU A 409 -6.442 -24.199 38.374 1.00 25.04 C
ANISOU 793 CB LEU A 409 3393 3487 2635 524 674 350 C
ATOM 794 CG LEU A 409 -5.160 -23.965 39.195 1.00 24.83 C
ANISOU 794 CG LEU A 409 3491 3414 2530 566 617 334 C
ATOM 795 CD1 LEU A 409 -4.182 -23.186 38.358 1.00 25.03 C
ANISOU 795 CD1 LEU A 409 3553 3333 2623 607 521 251 C
ATOM 796 CD2 LEU A 409 -5.528 -23.216 40.495 1.00 33.73 C
ANISOU 796 CD2 LEU A 409 4645 4662 3508 641 681 296 C
ATOM 797 N LEU A 410 -5.195 -27.419 37.499 1.00 19.04 N
ANISOU 797 N LEU A 410 2710 2470 2054 287 603 532 N
ATOM 798 CA LEU A 410 -5.002 -28.815 37.860 1.00 24.68 C
ANISOU 798 CA LEU A 410 3471 3107 2799 203 627 644 C
ATOM 799 C LEU A 410 -3.764 -28.990 38.740 1.00 28.88 C
ANISOU 799 C LEU A 410 4112 3596 3266 265 582 703 C
ATOM 800 O LEU A 410 -2.768 -28.296 38.549 1.00 19.62 O
ANISOU 800 O LEU A 410 2977 2397 2081 340 502 636 O
ATOM 801 CB LEU A 410 -4.881 -29.658 36.584 1.00 23.34 C
ANISOU 801 CB LEU A 410 3287 2807 2775 118 597 622 C
ATOM 802 CG LEU A 410 -6.150 -29.568 35.737 1.00 25.18 C
ANISOU 802 CG LEU A 410 3397 3112 3057 42 633 570 C
ATOM 803 CD1 LEU A 410 -6.035 -30.544 34.572 1.00 24.87 C
ANISOU 803 CD1 LEU A 410 3354 2950 3144 -62 606 539 C
ATOM 804 CD2 LEU A 410 -7.320 -29.923 36.564 1.00 26.33 C
ANISOU 804 CD2 LEU A 410 3483 3365 3156 -25 732 649 C
ATOM 805 N ASP A 411 -3.821 -29.923 39.695 1.00 30.02 N
ANISOU 805 N ASP A 411 4301 3740 3365 229 633 837 N
ATOM 806 CA ASP A 411 -2.655 -30.234 40.507 1.00 29.51 C
ANISOU 806 CA ASP A 411 4329 3647 3237 289 584 918 C
ATOM 807 C ASP A 411 -2.096 -31.571 40.048 1.00 33.43 C
ANISOU 807 C ASP A 411 4874 3967 3863 244 571 1007 C
ATOM 808 O ASP A 411 -2.700 -32.277 39.240 1.00 32.47 O
ANISOU 808 O ASP A 411 4723 3748 3865 151 610 1002 O
ATOM 809 CB ASP A 411 -2.981 -30.216 42.022 1.00 30.83 C
ANISOU 809 CB ASP A 411 4521 3960 3232 310 643 1018 C
ATOM 810 CG ASP A 411 -3.993 -31.285 42.459 1.00 31.57 C
ANISOU 810 CG ASP A 411 4597 4060 3338 209 755 1162 C
ATOM 811 OD1 ASP A 411 -4.129 -32.333 41.783 1.00 36.85 O
ANISOU 811 OD1 ASP A 411 5268 4578 4154 122 773 1217 O
ATOM 812 OD2 ASP A 411 -4.711 -31.069 43.467 1.00 41.60 O
ANISOU 812 OD2 ASP A 411 5847 5489 4471 208 834 1214 O
ATOM 813 N ARG A 412 -0.924 -31.899 40.586 1.00 32.79 N
ANISOU 813 N ARG A 412 4864 3847 3748 316 514 1085 N
ATOM 814 CA ARG A 412 -0.235 -33.152 40.301 1.00 36.89 C
ANISOU 814 CA ARG A 412 5440 4191 4384 311 503 1183 C
ATOM 815 C ARG A 412 -1.140 -34.382 40.456 1.00 40.19 C
ANISOU 815 C ARG A 412 5877 4515 4878 202 605 1307 C
ATOM 816 O ARG A 412 -1.112 -35.291 39.617 1.00 42.62 O
ANISOU 816 O ARG A 412 6206 4642 5345 144 620 1303 O
ATOM 817 CB ARG A 412 0.964 -33.245 41.245 1.00 40.14 C
ANISOU 817 CB ARG A 412 5903 4644 4704 413 435 1277 C
ATOM 818 CG ARG A 412 1.705 -34.466 41.149 1.00 35.88 C
ANISOU 818 CG ARG A 412 5384 3967 4280 413 398 1339 C
ATOM 819 CD ARG A 412 3.086 -34.269 41.728 1.00 30.66 C
ANISOU 819 CD ARG A 412 4722 3376 3552 513 291 1355 C
ATOM 820 NE ARG A 412 3.936 -35.239 41.064 1.00 35.69 N
ANISOU 820 NE ARG A 412 5363 3858 4341 534 252 1355 N
ATOM 821 CZ ARG A 412 3.977 -36.531 41.361 1.00 37.57 C
ANISOU 821 CZ ARG A 412 5639 3985 4651 516 274 1461 C
ATOM 822 NH1 ARG A 412 3.257 -36.999 42.365 1.00 35.63 N
ANISOU 822 NH1 ARG A 412 5426 3776 4336 470 330 1589 N
ATOM 823 NH2 ARG A 412 4.760 -37.331 40.664 1.00 32.78 N
ANISOU 823 NH2 ARG A 412 5039 3238 4179 549 242 1438 N
ATOM 824 N ASN A 413 -1.924 -34.440 41.542 1.00 38.14 N
ANISOU 824 N ASN A 413 5613 4376 4504 166 680 1415 N
ATOM 825 CA ASN A 413 -2.755 -35.617 41.800 1.00 36.87 C
ANISOU 825 CA ASN A 413 5454 4142 4414 42 762 1523 C
ATOM 826 C ASN A 413 -3.772 -35.838 40.687 1.00 40.58 C
ANISOU 826 C ASN A 413 5870 4529 5019 -87 830 1451 C
ATOM 827 O ASN A 413 -4.010 -36.980 40.275 1.00 42.28 O
ANISOU 827 O ASN A 413 6110 4579 5377 -192 858 1482 O
ATOM 828 CB ASN A 413 -3.466 -35.488 43.137 1.00 39.87 C
ANISOU 828 CB ASN A 413 5814 4704 4630 21 824 1623 C
ATOM 829 CG ASN A 413 -2.564 -35.788 44.294 1.00 40.50 C
ANISOU 829 CG ASN A 413 5951 4831 4605 100 761 1721 C
ATOM 830 OD1 ASN A 413 -1.463 -36.302 44.114 1.00 45.27 O
ANISOU 830 OD1 ASN A 413 6602 5317 5280 158 678 1736 O
ATOM 831 ND2 ASN A 413 -3.040 -35.513 45.500 1.00 44.98 N
ANISOU 831 ND2 ASN A 413 6507 5582 5002 100 803 1786 N
ATOM 832 N GLN A 414 -4.391 -34.756 40.195 1.00 34.46 N
ANISOU 832 N GLN A 414 4998 3892 4203 -91 818 1298 N
ATOM 833 CA GLN A 414 -5.255 -34.853 39.019 1.00 39.91 C
ANISOU 833 CA GLN A 414 5606 4547 5011 -206 836 1183 C
ATOM 834 C GLN A 414 -4.497 -35.328 37.777 1.00 38.88 C
ANISOU 834 C GLN A 414 5516 4226 5030 -211 771 1090 C
ATOM 835 O GLN A 414 -5.093 -35.939 36.884 1.00 45.11 O
ANISOU 835 O GLN A 414 6272 4929 5937 -336 795 1030 O
ATOM 836 CB GLN A 414 -5.908 -33.507 38.766 1.00 35.41 C
ANISOU 836 CB GLN A 414 4927 4169 4358 -167 824 1054 C
ATOM 837 CG GLN A 414 -6.991 -33.224 39.751 1.00 34.78 C
ANISOU 837 CG GLN A 414 4781 4272 4164 -195 918 1124 C
ATOM 838 CD GLN A 414 -7.422 -31.783 39.712 1.00 40.98 C
ANISOU 838 CD GLN A 414 5481 5236 4852 -105 906 1005 C
ATOM 839 OE1 GLN A 414 -6.591 -30.887 39.841 1.00 31.82 O
ANISOU 839 OE1 GLN A 414 4368 4096 3627 21 838 937 O
ATOM 840 NE2 GLN A 414 -8.724 -31.542 39.556 1.00 40.44 N
ANISOU 840 NE2 GLN A 414 5286 5300 4781 -168 976 981 N
ATOM 841 N GLY A 415 -3.195 -35.080 37.698 1.00 37.00 N
ANISOU 841 N GLY A 415 5342 3932 4783 -83 690 1070 N
ATOM 842 CA GLY A 415 -2.430 -35.632 36.585 1.00 36.56 C
ANISOU 842 CA GLY A 415 5327 3700 4864 -78 643 992 C
ATOM 843 C GLY A 415 -2.205 -37.129 36.684 1.00 45.81 C
ANISOU 843 C GLY A 415 6592 4653 6162 -131 692 1100 C
ATOM 844 O GLY A 415 -2.106 -37.806 35.653 1.00 42.83 O
ANISOU 844 O GLY A 415 6234 4121 5920 -188 690 1011 O
ATOM 845 N LYS A 416 -2.092 -37.657 37.917 1.00 46.65 N
ANISOU 845 N LYS A 416 6739 4777 6209 -110 706 1254 N
ATOM 846 CA LYS A 416 -1.952 -39.101 38.133 1.00 50.56 C
ANISOU 846 CA LYS A 416 7295 5114 6804 -161 711 1327 C
ATOM 847 C LYS A 416 -2.993 -39.864 37.344 1.00 50.14 C
ANISOU 847 C LYS A 416 7228 4941 6881 -340 778 1272 C
ATOM 848 O LYS A 416 -2.699 -40.871 36.683 1.00 51.43 O
ANISOU 848 O LYS A 416 7440 4925 7177 -376 760 1219 O
ATOM 849 CB LYS A 416 -2.173 -39.466 39.602 1.00 47.02 C
ANISOU 849 CB LYS A 416 6870 4741 6253 -162 741 1507 C
ATOM 850 CG LYS A 416 -1.276 -38.930 40.647 1.00 49.44 C
ANISOU 850 CG LYS A 416 7191 5180 6414 -18 680 1584 C
ATOM 851 CD LYS A 416 0.114 -39.467 40.597 1.00 60.63 C
ANISOU 851 CD LYS A 416 8655 6500 7881 96 591 1591 C
ATOM 852 CE LYS A 416 0.814 -38.794 41.730 1.00 47.62 C
ANISOU 852 CE LYS A 416 7000 5029 6063 209 536 1664 C
ATOM 853 NZ LYS A 416 0.182 -39.318 42.986 1.00 54.64 N
ANISOU 853 NZ LYS A 416 7918 5979 6865 157 593 1829 N
ATOM 854 N SER A 417 -4.236 -39.399 37.459 1.00 46.50 N
ANISOU 854 N SER A 417 6693 4598 6378 -455 855 1281 N
ATOM 855 CA SER A 417 -5.392 -40.145 37.012 1.00 48.32 C
ANISOU 855 CA SER A 417 6886 4765 6709 -656 921 1256 C
ATOM 856 C SER A 417 -5.314 -40.474 35.534 1.00 50.46 C
ANISOU 856 C SER A 417 7156 4901 7117 -723 892 1075 C
ATOM 857 O SER A 417 -5.859 -41.494 35.102 1.00 47.90 O
ANISOU 857 O SER A 417 6842 4455 6904 -871 912 1039 O
ATOM 858 CB SER A 417 -6.657 -39.348 37.321 1.00 54.18 C
ANISOU 858 CB SER A 417 7509 5715 7363 -746 1003 1278 C
ATOM 859 OG SER A 417 -6.822 -38.303 36.374 1.00 52.10 O
ANISOU 859 OG SER A 417 7149 5579 7069 -717 949 1102 O
ATOM 860 N VAL A 418 -4.635 -39.656 34.738 1.00 48.34 N
ANISOU 860 N VAL A 418 6878 4653 6835 -620 840 953 N
ATOM 861 CA VAL A 418 -4.450 -39.999 33.334 1.00 46.01 C
ANISOU 861 CA VAL A 418 6588 4246 6650 -671 805 771 C
ATOM 862 C VAL A 418 -3.132 -40.765 33.205 1.00 43.97 C
ANISOU 862 C VAL A 418 6428 3834 6446 -541 739 763 C
ATOM 863 O VAL A 418 -2.061 -40.206 33.439 1.00 40.00 O
ANISOU 863 O VAL A 418 5942 3375 5880 -370 683 785 O
ATOM 864 CB VAL A 418 -4.483 -38.757 32.448 1.00 44.70 C
ANISOU 864 CB VAL A 418 6320 4257 6405 -624 741 618 C
ATOM 865 CG1 VAL A 418 -4.161 -39.144 31.017 1.00 47.31 C
ANISOU 865 CG1 VAL A 418 6665 4482 6828 -664 706 437 C
ATOM 866 N GLU A 419 -3.209 -42.064 32.886 1.00 42.58 N
ANISOU 866 N GLU A 419 6307 3487 6384 -623 746 737 N
ATOM 867 CA GLU A 419 -2.015 -42.875 32.625 1.00 45.23 C
ANISOU 867 CA GLU A 419 6728 3673 6785 -505 696 714 C
ATOM 868 C GLU A 419 -1.026 -42.174 31.687 1.00 40.47 C
ANISOU 868 C GLU A 419 6104 3118 6157 -374 635 576 C
ATOM 869 O GLU A 419 -1.416 -41.658 30.637 1.00 39.47 O
ANISOU 869 O GLU A 419 5925 3041 6030 -439 634 423 O
ATOM 870 CB GLU A 419 -2.397 -44.218 31.993 1.00 51.21 C
ANISOU 870 CB GLU A 419 7541 4239 7678 -633 719 640 C
ATOM 871 CG GLU A 419 -1.147 -45.075 31.761 1.00 48.63 C
ANISOU 871 CG GLU A 419 7303 3755 7420 -495 679 624 C
ATOM 872 CD GLU A 419 -1.406 -46.424 31.154 1.00 74.58 C
ANISOU 872 CD GLU A 419 10664 6830 10843 -599 703 547 C
ATOM 873 OE1 GLU A 419 -2.581 -46.772 30.906 1.00 78.82 O
ANISOU 873 OE1 GLU A 419 11182 7339 11427 -796 742 504 O
ATOM 874 OE2 GLU A 419 -0.406 -47.105 30.836 1.00 87.11 O
ANISOU 874 OE2 GLU A 419 12322 8287 12491 -484 679 513 O
ATOM 875 N GLY A 420 0.275 -42.213 32.045 1.00 39.48 N
ANISOU 875 N GLY A 420 6011 2983 6008 -198 581 631 N
ATOM 876 CA GLY A 420 1.334 -41.586 31.269 1.00 39.12 C
ANISOU 876 CA GLY A 420 5935 2998 5933 -70 521 523 C
ATOM 877 C GLY A 420 1.631 -40.104 31.555 1.00 36.32 C
ANISOU 877 C GLY A 420 5511 2833 5456 15 483 543 C
ATOM 878 O GLY A 420 2.648 -39.584 31.077 1.00 38.04 O
ANISOU 878 O GLY A 420 5700 3111 5645 128 426 481 O
ATOM 879 N MET A 421 0.811 -39.399 32.320 1.00 37.29 N
ANISOU 879 N MET A 421 5606 3056 5505 -33 514 627 N
ATOM 880 CA MET A 421 0.933 -37.939 32.319 1.00 36.57 C
ANISOU 880 CA MET A 421 5458 3127 5311 31 485 605 C
ATOM 881 C MET A 421 1.787 -37.306 33.431 1.00 35.86 C
ANISOU 881 C MET A 421 5361 3151 5112 165 430 715 C
ATOM 882 O MET A 421 2.354 -36.221 33.205 1.00 27.56 O
ANISOU 882 O MET A 421 4268 2209 3994 244 378 664 O
ATOM 883 CB MET A 421 -0.472 -37.323 32.305 1.00 39.08 C
ANISOU 883 CB MET A 421 5730 3523 5596 -93 546 595 C
ATOM 884 CG MET A 421 -0.434 -35.843 32.001 1.00 37.62 C
ANISOU 884 CG MET A 421 5452 3546 5295 -33 480 515 C
ATOM 885 SD MET A 421 -1.991 -34.950 32.016 1.00 43.98 S
ANISOU 885 SD MET A 421 6140 4556 6016 -135 499 478 S
ATOM 886 CE MET A 421 -3.129 -36.035 31.254 1.00 49.13 C
ANISOU 886 CE MET A 421 6768 5125 6774 -330 557 414 C
ATOM 887 N VAL A 422 1.909 -37.930 34.603 1.00 32.12 N
ANISOU 887 N VAL A 422 4926 2662 4615 184 437 859 N
ATOM 888 CA VAL A 422 2.420 -37.204 35.770 1.00 30.34 C
ANISOU 888 CA VAL A 422 4688 2580 4259 277 395 958 C
ATOM 889 C VAL A 422 3.873 -36.791 35.563 1.00 27.81 C
ANISOU 889 C VAL A 422 4336 2311 3919 400 302 911 C
ATOM 890 O VAL A 422 4.279 -35.694 35.955 1.00 25.81 O
ANISOU 890 O VAL A 422 4047 2197 3562 459 254 907 O
ATOM 891 CB VAL A 422 2.203 -38.033 37.061 1.00 38.24 C
ANISOU 891 CB VAL A 422 5735 3565 5230 262 424 1127 C
ATOM 892 CG1 VAL A 422 3.027 -39.340 37.068 1.00 33.47 C
ANISOU 892 CG1 VAL A 422 5179 2815 4723 303 400 1172 C
ATOM 893 CG2 VAL A 422 2.427 -37.180 38.315 1.00 36.19 C
ANISOU 893 CG2 VAL A 422 5461 3486 4806 331 395 1219 C
ATOM 894 N GLU A 423 4.666 -37.614 34.866 1.00 27.64 N
ANISOU 894 N GLU A 423 4323 2182 3998 434 277 863 N
ATOM 895 CA GLU A 423 6.069 -37.256 34.647 1.00 31.42 C
ANISOU 895 CA GLU A 423 4755 2720 4462 542 199 825 C
ATOM 896 C GLU A 423 6.158 -35.961 33.859 1.00 23.53 C
ANISOU 896 C GLU A 423 3693 1825 3420 544 170 707 C
ATOM 897 O GLU A 423 7.007 -35.112 34.139 1.00 24.36 O
ANISOU 897 O GLU A 423 3751 2047 3459 607 107 706 O
ATOM 898 CB GLU A 423 6.780 -38.386 33.885 1.00 32.93 C
ANISOU 898 CB GLU A 423 4967 2772 4772 578 197 781 C
ATOM 899 CG GLU A 423 6.572 -39.794 34.556 1.00 41.89 C
ANISOU 899 CG GLU A 423 6181 3762 5972 568 236 897 C
ATOM 900 CD GLU A 423 5.191 -40.409 34.201 1.00 46.35 C
ANISOU 900 CD GLU A 423 6801 4206 6605 431 317 873 C
ATOM 901 OE1 GLU A 423 4.567 -41.056 35.073 1.00 54.17 O
ANISOU 901 OE1 GLU A 423 7843 5139 7600 380 358 995 O
ATOM 902 OE2 GLU A 423 4.709 -40.193 33.064 1.00 65.90 O
ANISOU 902 OE2 GLU A 423 9261 6656 9122 366 340 733 O
ATOM 903 N ILE A 424 5.261 -35.791 32.885 1.00 24.54 N
ANISOU 903 N ILE A 424 3822 1914 3587 467 215 609 N
ATOM 904 CA ILE A 424 5.253 -34.608 32.034 1.00 27.52 C
ANISOU 904 CA ILE A 424 4147 2381 3930 468 192 502 C
ATOM 905 C ILE A 424 4.755 -33.417 32.836 1.00 21.28 C
ANISOU 905 C ILE A 424 3347 1710 3028 472 186 545 C
ATOM 906 O ILE A 424 5.298 -32.312 32.802 1.00 19.34 O
ANISOU 906 O ILE A 424 3060 1569 2720 516 133 508 O
ATOM 907 CB ILE A 424 4.321 -34.795 30.826 1.00 29.03 C
ANISOU 907 CB ILE A 424 4344 2501 4183 382 247 394 C
ATOM 908 CG1 ILE A 424 4.640 -36.010 29.950 1.00 36.23 C
ANISOU 908 CG1 ILE A 424 5281 3285 5198 365 264 325 C
ATOM 909 CG2 ILE A 424 4.518 -33.581 29.945 1.00 22.60 C
ANISOU 909 CG2 ILE A 424 3474 1788 3327 404 214 299 C
ATOM 910 CD1 ILE A 424 5.856 -36.020 29.345 1.00 37.88 C
ANISOU 910 CD1 ILE A 424 5458 3516 5421 447 217 271 C
ATOM 911 N PHE A 425 3.691 -33.651 33.571 1.00 25.94 N
ANISOU 911 N PHE A 425 3979 2283 3595 417 250 618 N
ATOM 912 CA PHE A 425 3.118 -32.668 34.518 1.00 24.42 C
ANISOU 912 CA PHE A 425 3781 2220 3279 428 249 663 C
ATOM 913 C PHE A 425 4.225 -32.170 35.456 1.00 23.60 C
ANISOU 913 C PHE A 425 3684 2206 3079 518 185 731 C
ATOM 914 O PHE A 425 4.404 -30.997 35.641 1.00 16.03 O
ANISOU 914 O PHE A 425 2699 1356 2036 550 140 679 O
ATOM 915 CB PHE A 425 2.047 -33.416 35.287 1.00 31.47 C
ANISOU 915 CB PHE A 425 4673 3117 4168 323 328 699 C
ATOM 916 CG PHE A 425 0.897 -32.588 35.753 1.00 34.30 C
ANISOU 916 CG PHE A 425 5012 3617 4403 316 347 741 C
ATOM 917 CD1 PHE A 425 1.098 -31.576 36.665 1.00 45.02 C
ANISOU 917 CD1 PHE A 425 6328 5116 5663 338 330 686 C
ATOM 918 CD2 PHE A 425 -0.370 -32.820 35.275 1.00 34.81 C
ANISOU 918 CD2 PHE A 425 5061 3644 4520 205 424 755 C
ATOM 919 CE1 PHE A 425 0.036 -30.817 37.111 1.00 30.19 C
ANISOU 919 CE1 PHE A 425 4426 3348 3694 306 388 717 C
ATOM 920 CE2 PHE A 425 -1.426 -32.058 35.714 1.00 45.73 C
ANISOU 920 CE2 PHE A 425 6396 5149 5831 148 480 773 C
ATOM 921 CZ PHE A 425 -1.214 -31.061 36.629 1.00 48.05 C
ANISOU 921 CZ PHE A 425 6665 5592 5999 211 464 754 C
ATOM 922 N ASP A 426 4.985 -33.113 36.020 1.00 22.78 N
ANISOU 922 N ASP A 426 3586 2067 3001 549 157 802 N
ATOM 923 CA ASP A 426 6.125 -32.721 36.864 1.00 23.13 C
ANISOU 923 CA ASP A 426 3611 2214 2964 625 79 846 C
ATOM 924 C ASP A 426 7.168 -31.878 36.129 1.00 21.09 C
ANISOU 924 C ASP A 426 3292 2005 2717 664 8 746 C
ATOM 925 O ASP A 426 7.687 -30.906 36.698 1.00 19.71 O
ANISOU 925 O ASP A 426 3100 1944 2443 700 -49 741 O
ATOM 926 CB ASP A 426 6.756 -33.969 37.458 1.00 25.82 C
ANISOU 926 CB ASP A 426 3969 2499 3344 656 67 954 C
ATOM 927 CG ASP A 426 5.945 -34.496 38.621 1.00 32.03 C
ANISOU 927 CG ASP A 426 4810 3298 4064 627 118 1085 C
ATOM 928 OD1 ASP A 426 5.136 -33.692 39.178 1.00 28.99 O
ANISOU 928 OD1 ASP A 426 4436 3014 3567 603 147 1093 O
ATOM 929 OD2 ASP A 426 6.086 -35.698 38.959 1.00 32.58 O
ANISOU 929 OD2 ASP A 426 4912 3277 4191 630 134 1178 O
ATOM 930 N MET A 427 7.480 -32.193 34.857 1.00 20.80 N
ANISOU 930 N MET A 427 3222 1891 2791 652 12 662 N
ATOM 931 CA MET A 427 8.444 -31.368 34.126 1.00 20.25 C
ANISOU 931 CA MET A 427 3086 1878 2729 678 -43 579 C
ATOM 932 C MET A 427 7.880 -29.987 33.829 1.00 17.22 C
ANISOU 932 C MET A 427 2696 1562 2286 651 -48 503 C
ATOM 933 O MET A 427 8.594 -28.974 33.933 1.00 20.76 O
ANISOU 933 O MET A 427 3112 2090 2684 674 -104 474 O
ATOM 934 CB MET A 427 8.827 -32.068 32.822 1.00 20.39 C
ANISOU 934 CB MET A 427 3076 1811 2862 675 -26 510 C
ATOM 935 CG MET A 427 9.627 -33.413 33.050 1.00 21.10 C
ANISOU 935 CG MET A 427 3176 1823 3019 728 -31 573 C
ATOM 936 SD MET A 427 9.955 -34.100 31.380 1.00 32.26 S
ANISOU 936 SD MET A 427 4568 3140 4547 731 0 456 S
ATOM 937 CE MET A 427 8.417 -34.533 30.758 1.00 29.90 C
ANISOU 937 CE MET A 427 4333 2744 4286 639 71 398 C
ATOM 938 N LEU A 428 6.590 -29.921 33.477 1.00 15.92 N
ANISOU 938 N LEU A 428 2563 1359 2128 603 11 475 N
ATOM 939 CA LEU A 428 5.915 -28.622 33.308 1.00 19.12 C
ANISOU 939 CA LEU A 428 2966 1823 2475 590 10 413 C
ATOM 940 C LEU A 428 5.972 -27.763 34.578 1.00 19.60 C
ANISOU 940 C LEU A 428 3042 1986 2418 608 -23 435 C
ATOM 941 O LEU A 428 6.223 -26.547 34.501 1.00 16.53 O
ANISOU 941 O LEU A 428 2633 1657 1992 607 -63 365 O
ATOM 942 CB LEU A 428 4.445 -28.826 32.907 1.00 13.53 C
ANISOU 942 CB LEU A 428 2254 1097 1789 517 79 385 C
ATOM 943 CG LEU A 428 4.391 -29.333 31.454 1.00 16.91 C
ANISOU 943 CG LEU A 428 2656 1456 2313 485 97 318 C
ATOM 944 CD1 LEU A 428 3.027 -29.928 31.166 1.00 19.31 C
ANISOU 944 CD1 LEU A 428 2955 1736 2647 399 160 306 C
ATOM 945 CD2 LEU A 428 4.700 -28.185 30.402 1.00 17.95 C
ANISOU 945 CD2 LEU A 428 2731 1648 2440 492 58 231 C
ATOM 946 N LEU A 429 5.628 -28.357 35.726 1.00 14.16 N
ANISOU 946 N LEU A 429 2396 1316 1667 614 2 526 N
ATOM 947 CA LEU A 429 5.669 -27.638 37.009 1.00 17.65 C
ANISOU 947 CA LEU A 429 2859 1875 1973 631 -26 540 C
ATOM 948 C LEU A 429 7.069 -27.114 37.310 1.00 22.98 C
ANISOU 948 C LEU A 429 3517 2610 2606 675 -121 528 C
ATOM 949 O LEU A 429 7.224 -25.981 37.807 1.00 18.44 O
ANISOU 949 O LEU A 429 2941 2120 1945 665 -161 457 O
ATOM 950 CB LEU A 429 5.213 -28.560 38.143 1.00 21.10 C
ANISOU 950 CB LEU A 429 3341 2332 2344 636 18 667 C
ATOM 951 CG LEU A 429 3.705 -28.808 38.154 1.00 23.32 C
ANISOU 951 CG LEU A 429 3627 2603 2631 574 115 674 C
ATOM 952 CD1 LEU A 429 3.370 -29.962 39.121 1.00 18.75 C
ANISOU 952 CD1 LEU A 429 3094 2016 2015 568 168 829 C
ATOM 953 CD2 LEU A 429 2.907 -27.531 38.484 1.00 20.56 C
ANISOU 953 CD2 LEU A 429 3261 2361 2192 563 135 580 C
ATOM 954 N ALA A 430 8.099 -27.924 37.039 1.00 20.47 N
ANISOU 954 N ALA A 430 3181 2249 2348 722 -156 591 N
ATOM 955 CA ALA A 430 9.461 -27.468 37.315 1.00 19.32 C
ANISOU 955 CA ALA A 430 2994 2185 2163 759 -251 587 C
ATOM 956 C ALA A 430 9.850 -26.326 36.402 1.00 18.06 C
ANISOU 956 C ALA A 430 2786 2030 2046 721 -284 465 C
ATOM 957 O ALA A 430 10.608 -25.435 36.816 1.00 21.94 O
ANISOU 957 O ALA A 430 3252 2610 2476 707 -356 421 O
ATOM 958 CB ALA A 430 10.475 -28.630 37.143 1.00 22.12 C
ANISOU 958 CB ALA A 430 3294 2508 2605 792 -265 662 C
ATOM 959 N THR A 431 9.381 -26.331 35.148 1.00 20.73 N
ANISOU 959 N THR A 431 3110 2280 2485 696 -234 412 N
ATOM 960 CA THR A 431 9.685 -25.215 34.259 1.00 18.40 C
ANISOU 960 CA THR A 431 2775 1991 2226 660 -257 317 C
ATOM 961 C THR A 431 9.009 -23.951 34.765 1.00 18.82 C
ANISOU 961 C THR A 431 2859 2082 2210 617 -257 246 C
ATOM 962 O THR A 431 9.579 -22.859 34.735 1.00 22.04 O
ANISOU 962 O THR A 431 3251 2518 2605 588 -305 183 O
ATOM 963 CB THR A 431 9.224 -25.521 32.814 1.00 19.50 C
ANISOU 963 CB THR A 431 2894 2051 2466 646 -201 285 C
ATOM 964 OG1 THR A 431 9.700 -26.811 32.447 1.00 21.95 O
ANISOU 964 OG1 THR A 431 3172 2323 2844 661 -178 326 O
ATOM 965 CG2 THR A 431 9.802 -24.535 31.781 1.00 18.51 C
ANISOU 965 CG2 THR A 431 2714 1938 2379 620 -226 221 C
ATOM 966 N SER A 432 7.776 -24.076 35.208 1.00 17.06 N
ANISOU 966 N SER A 432 2680 1852 1949 612 -198 251 N
ATOM 967 CA SER A 432 7.083 -22.909 35.725 1.00 17.98 C
ANISOU 967 CA SER A 432 2829 2002 2002 593 -185 177 C
ATOM 968 C SER A 432 7.780 -22.389 36.976 1.00 22.04 C
ANISOU 968 C SER A 432 3369 2602 2403 592 -247 155 C
ATOM 969 O SER A 432 7.931 -21.170 37.146 1.00 21.09 O
ANISOU 969 O SER A 432 3266 2491 2258 566 -273 61 O
ATOM 970 CB SER A 432 5.612 -23.303 35.985 1.00 20.45 C
ANISOU 970 CB SER A 432 3165 2314 2292 596 -99 199 C
ATOM 971 OG SER A 432 4.877 -22.231 36.486 1.00 31.73 O
ANISOU 971 OG SER A 432 4620 3777 3661 599 -72 128 O
ATOM 972 N SER A 433 8.215 -23.297 37.868 1.00 19.84 N
ANISOU 972 N SER A 433 3098 2387 2054 620 -273 241 N
ATOM 973 CA SER A 433 9.008 -22.865 39.017 1.00 24.48 C
ANISOU 973 CA SER A 433 3696 3088 2518 615 -350 223 C
ATOM 974 C SER A 433 10.290 -22.162 38.590 1.00 23.31 C
ANISOU 974 C SER A 433 3495 2952 2408 582 -438 166 C
ATOM 975 O SER A 433 10.745 -21.236 39.273 1.00 23.43 O
ANISOU 975 O SER A 433 3522 3038 2342 540 -497 83 O
ATOM 976 CB SER A 433 9.363 -24.051 39.923 1.00 30.33 C
ANISOU 976 CB SER A 433 4439 3904 3180 663 -371 357 C
ATOM 977 OG SER A 433 8.216 -24.818 40.216 1.00 42.89 O
ANISOU 977 OG SER A 433 6073 5470 4755 680 -281 430 O
ATOM 978 N ARG A 434 10.926 -22.646 37.507 1.00 19.49 N
ANISOU 978 N ARG A 434 2950 2411 2043 595 -446 208 N
ATOM 979 CA ARG A 434 12.163 -22.052 36.998 1.00 21.02 C
ANISOU 979 CA ARG A 434 3075 2629 2283 559 -518 170 C
ATOM 980 C ARG A 434 11.914 -20.651 36.455 1.00 20.79 C
ANISOU 980 C ARG A 434 3064 2539 2296 488 -507 55 C
ATOM 981 O ARG A 434 12.669 -19.724 36.759 1.00 22.29 O
ANISOU 981 O ARG A 434 3238 2770 2461 424 -573 -15 O
ATOM 982 CB ARG A 434 12.746 -22.957 35.894 1.00 20.17 C
ANISOU 982 CB ARG A 434 2899 2476 2290 602 -504 240 C
ATOM 983 CG ARG A 434 13.966 -22.396 35.223 1.00 30.36 C
ANISOU 983 CG ARG A 434 4101 3798 3635 566 -559 212 C
ATOM 984 CD ARG A 434 15.136 -22.376 36.171 1.00 35.24 C
ANISOU 984 CD ARG A 434 4660 4555 4176 563 -660 236 C
ATOM 985 NE ARG A 434 16.358 -22.092 35.432 1.00 39.42 N
ANISOU 985 NE ARG A 434 5078 5128 4773 536 -704 232 N
ATOM 986 CZ ARG A 434 17.360 -21.353 35.889 1.00 42.24 C
ANISOU 986 CZ ARG A 434 5366 5596 5088 465 -795 194 C
ATOM 987 NH1 ARG A 434 17.294 -20.820 37.099 1.00 39.63 N
ANISOU 987 NH1 ARG A 434 5077 5343 4638 417 -857 144 N
ATOM 988 NH2 ARG A 434 18.428 -21.152 35.126 1.00 42.81 N
ANISOU 988 NH2 ARG A 434 5323 5712 5232 437 -821 201 N
ATOM 989 N PHE A 435 10.855 -20.478 35.649 1.00 18.74 N
ANISOU 989 N PHE A 435 2835 2181 2103 495 -427 37 N
ATOM 990 CA PHE A 435 10.434 -19.130 35.250 1.00 17.01 C
ANISOU 990 CA PHE A 435 2648 1894 1920 449 -406 -54 C
ATOM 991 C PHE A 435 10.163 -18.247 36.434 1.00 23.00 C
ANISOU 991 C PHE A 435 3476 2679 2583 425 -422 -145 C
ATOM 992 O PHE A 435 10.514 -17.057 36.405 1.00 21.04 O
ANISOU 992 O PHE A 435 3249 2389 2356 365 -448 -233 O
ATOM 993 CB PHE A 435 9.211 -19.125 34.331 1.00 20.28 C
ANISOU 993 CB PHE A 435 3077 2227 2401 479 -320 -44 C
ATOM 994 CG PHE A 435 9.466 -19.572 32.907 1.00 26.21 C
ANISOU 994 CG PHE A 435 3766 2943 3250 483 -303 5 C
ATOM 995 CD1 PHE A 435 10.760 -19.647 32.422 1.00 19.72 C
ANISOU 995 CD1 PHE A 435 2880 2146 2466 458 -353 24 C
ATOM 996 CD2 PHE A 435 8.406 -19.703 32.007 1.00 25.98 C
ANISOU 996 CD2 PHE A 435 3735 2870 3267 505 -237 18 C
ATOM 997 CE1 PHE A 435 11.016 -19.946 31.062 1.00 27.25 C
ANISOU 997 CE1 PHE A 435 3776 3081 3497 462 -328 56 C
ATOM 998 CE2 PHE A 435 8.655 -20.044 30.666 1.00 25.59 C
ANISOU 998 CE2 PHE A 435 3629 2807 3286 502 -223 48 C
ATOM 999 CZ PHE A 435 9.966 -20.170 30.217 1.00 27.24 C
ANISOU 999 CZ PHE A 435 3784 3039 3526 484 -265 65 C
ATOM 1000 N ARG A 436 9.504 -18.792 37.476 1.00 22.26 N
ANISOU 1000 N ARG A 436 3425 2650 2382 466 -399 -128 N
ATOM 1001 CA ARG A 436 9.195 -17.972 38.647 1.00 21.38 C
ANISOU 1001 CA ARG A 436 3385 2582 2157 450 -404 -230 C
ATOM 1002 C ARG A 436 10.482 -17.535 39.329 1.00 24.60 C
ANISOU 1002 C ARG A 436 3777 3073 2498 383 -511 -286 C
ATOM 1003 O ARG A 436 10.641 -16.359 39.688 1.00 28.65 O
ANISOU 1003 O ARG A 436 4336 3560 2989 324 -534 -416 O
ATOM 1004 CB ARG A 436 8.301 -18.753 39.627 1.00 21.27 C
ANISOU 1004 CB ARG A 436 3406 2649 2025 506 -353 -182 C
ATOM 1005 CG ARG A 436 7.870 -17.978 40.856 1.00 26.23 C
ANISOU 1005 CG ARG A 436 4109 3344 2515 502 -342 -293 C
ATOM 1006 CD ARG A 436 7.115 -18.918 41.840 1.00 29.61 C
ANISOU 1006 CD ARG A 436 4556 3884 2810 554 -291 -213 C
ATOM 1007 NE ARG A 436 6.291 -19.828 41.107 1.00 32.53 N
ANISOU 1007 NE ARG A 436 4893 4196 3270 592 -214 -101 N
ATOM 1008 CZ ARG A 436 6.307 -21.153 41.197 1.00 29.37 C
ANISOU 1008 CZ ARG A 436 4467 3830 2863 612 -205 42 C
ATOM 1009 NH1 ARG A 436 7.060 -21.782 42.065 1.00 26.80 N
ANISOU 1009 NH1 ARG A 436 4141 3609 2434 619 -265 115 N
ATOM 1010 NH2 ARG A 436 5.520 -21.842 40.380 1.00 28.87 N
ANISOU 1010 NH2 ARG A 436 4377 3689 2903 625 -134 112 N
ATOM 1011 N MET A 437 11.431 -18.468 39.500 1.00 21.98 N
ANISOU 1011 N MET A 437 3376 2839 2137 392 -579 -191 N
ATOM 1012 CA MET A 437 12.702 -18.115 40.122 1.00 23.31 C
ANISOU 1012 CA MET A 437 3501 3119 2236 327 -693 -233 C
ATOM 1013 C MET A 437 13.393 -16.984 39.360 1.00 27.34 C
ANISOU 1013 C MET A 437 3985 3549 2853 230 -726 -323 C
ATOM 1014 O MET A 437 13.893 -16.034 39.974 1.00 28.49 O
ANISOU 1014 O MET A 437 4151 3729 2945 140 -788 -443 O
ATOM 1015 CB MET A 437 13.613 -19.352 40.197 1.00 28.21 C
ANISOU 1015 CB MET A 437 4030 3849 2840 376 -752 -92 C
ATOM 1016 N MET A 438 13.442 -17.078 38.018 1.00 24.93 N
ANISOU 1016 N MET A 438 3634 3140 2696 239 -684 -267 N
ATOM 1017 CA MET A 438 14.080 -16.086 37.149 1.00 26.24 C
ANISOU 1017 CA MET A 438 3769 3228 2975 149 -701 -317 C
ATOM 1018 C MET A 438 13.282 -14.816 37.007 1.00 24.80 C
ANISOU 1018 C MET A 438 3684 2900 2837 111 -646 -425 C
ATOM 1019 O MET A 438 13.745 -13.892 36.341 1.00 27.25 O
ANISOU 1019 O MET A 438 3986 3123 3245 30 -653 -461 O
ATOM 1020 CB MET A 438 14.315 -16.672 35.744 1.00 18.75 C
ANISOU 1020 CB MET A 438 2740 2235 2149 184 -663 -212 C
ATOM 1021 CG MET A 438 15.047 -18.005 35.771 1.00 29.50 C
ANISOU 1021 CG MET A 438 4009 3711 3489 248 -699 -104 C
ATOM 1022 SD MET A 438 15.563 -18.397 34.081 1.00 31.80 S
ANISOU 1022 SD MET A 438 4204 3958 3920 265 -657 -26 S
ATOM 1023 CE MET A 438 16.483 -16.912 33.581 1.00 28.85 C
ANISOU 1023 CE MET A 438 3784 3565 3614 121 -697 -93 C
ATOM 1024 N ASN A 439 12.091 -14.752 37.589 1.00 26.28 N
ANISOU 1024 N ASN A 439 3964 3058 2965 174 -584 -466 N
ATOM 1025 CA ASN A 439 11.197 -13.596 37.430 1.00 27.40 C
ANISOU 1025 CA ASN A 439 4199 3052 3158 175 -515 -559 C
ATOM 1026 C ASN A 439 11.065 -13.213 35.939 1.00 25.32 C
ANISOU 1026 C ASN A 439 3908 2658 3053 175 -467 -496 C
ATOM 1027 O ASN A 439 11.162 -12.040 35.551 1.00 25.34 O
ANISOU 1027 O ASN A 439 3953 2533 3141 120 -455 -554 O
ATOM 1028 CB ASN A 439 11.677 -12.411 38.286 1.00 25.08 C
ANISOU 1028 CB ASN A 439 3973 2733 2822 77 -564 -720 C
ATOM 1029 CG ASN A 439 10.584 -11.332 38.470 1.00 32.62 C
ANISOU 1029 CG ASN A 439 5050 3541 3804 113 -479 -832 C
ATOM 1030 OD1 ASN A 439 9.394 -11.588 38.264 1.00 33.31 O
ANISOU 1030 OD1 ASN A 439 5162 3596 3899 224 -390 -789 O
ATOM 1031 ND2 ASN A 439 11.001 -10.125 38.794 1.00 36.15 N
ANISOU 1031 ND2 ASN A 439 5566 3891 4277 19 -504 -974 N
ATOM 1032 N LEU A 440 10.767 -14.221 35.120 1.00 20.97 N
ANISOU 1032 N LEU A 440 3293 2137 2536 241 -433 -376 N
ATOM 1033 CA LEU A 440 10.542 -14.026 33.665 1.00 21.97 C
ANISOU 1033 CA LEU A 440 3387 2178 2782 255 -385 -306 C
ATOM 1034 C LEU A 440 9.466 -12.955 33.421 1.00 23.77 C
ANISOU 1034 C LEU A 440 3693 2275 3064 292 -315 -345 C
ATOM 1035 O LEU A 440 8.425 -13.052 33.987 1.00 21.66 O
ANISOU 1035 O LEU A 440 3475 2010 2746 367 -264 -376 O
ATOM 1036 CB LEU A 440 10.087 -15.343 33.028 1.00 23.69 C
ANISOU 1036 CB LEU A 440 3545 2455 2999 329 -351 -204 C
ATOM 1037 CG LEU A 440 10.020 -15.320 31.503 1.00 18.96 C
ANISOU 1037 CG LEU A 440 2898 1809 2497 338 -313 -133 C
ATOM 1038 CD1 LEU A 440 11.400 -15.379 30.929 1.00 17.15 C
ANISOU 1038 CD1 LEU A 440 2593 1622 2300 269 -368 -106 C
ATOM 1039 CD2 LEU A 440 9.130 -16.394 30.926 1.00 20.68 C
ANISOU 1039 CD2 LEU A 440 3083 2064 2709 408 -265 -70 C
ATOM 1040 N GLN A 441 9.745 -12.022 32.520 1.00 23.57 N
ANISOU 1040 N GLN A 441 3671 2141 3144 249 -305 -331 N
ATOM 1041 CA GLN A 441 8.840 -10.933 32.175 1.00 23.59 C
ANISOU 1041 CA GLN A 441 3745 2001 3217 293 -239 -348 C
ATOM 1042 C GLN A 441 8.068 -11.257 30.894 1.00 22.31 C
ANISOU 1042 C GLN A 441 3529 1841 3105 371 -185 -228 C
ATOM 1043 O GLN A 441 8.529 -12.030 30.044 1.00 19.45 O
ANISOU 1043 O GLN A 441 3082 1558 2749 354 -202 -145 O
ATOM 1044 CB GLN A 441 9.631 -9.632 31.988 1.00 25.86 C
ANISOU 1044 CB GLN A 441 4077 2150 3596 192 -259 -390 C
ATOM 1045 CG GLN A 441 10.397 -9.217 33.242 1.00 27.73 C
ANISOU 1045 CG GLN A 441 4366 2390 3780 94 -321 -530 C
ATOM 1046 CD GLN A 441 9.443 -8.916 34.388 1.00 31.28 C
ANISOU 1046 CD GLN A 441 4917 2812 4156 166 -284 -651 C
ATOM 1047 OE1 GLN A 441 8.676 -7.945 34.330 1.00 32.27 O
ANISOU 1047 OE1 GLN A 441 5131 2785 4346 219 -218 -697 O
ATOM 1048 NE2 GLN A 441 9.482 -9.747 35.438 1.00 26.04 N
ANISOU 1048 NE2 GLN A 441 4241 2301 3353 178 -319 -698 N
ATOM 1049 N GLY A 442 6.887 -10.649 30.760 1.00 20.43 N
ANISOU 1049 N GLY A 442 3330 1536 2897 457 -118 -225 N
ATOM 1050 CA GLY A 442 6.046 -10.944 29.603 1.00 20.78 C
ANISOU 1050 CA GLY A 442 3282 1646 2969 511 -68 -111 C
ATOM 1051 C GLY A 442 6.743 -10.603 28.292 1.00 22.73 C
ANISOU 1051 C GLY A 442 3492 1855 3288 469 -81 -17 C
ATOM 1052 O GLY A 442 6.619 -11.326 27.311 1.00 19.25 O
ANISOU 1052 O GLY A 442 2975 1504 2834 486 -79 66 O
ATOM 1053 N GLU A 443 7.550 -9.540 28.280 1.00 20.41 N
ANISOU 1053 N GLU A 443 3258 1429 3067 401 -96 -33 N
ATOM 1054 CA GLU A 443 8.246 -9.199 27.034 1.00 21.43 C
ANISOU 1054 CA GLU A 443 3358 1521 3263 353 -105 74 C
ATOM 1055 C GLU A 443 9.265 -10.269 26.686 1.00 21.34 C
ANISOU 1055 C GLU A 443 3252 1652 3205 286 -152 99 C
ATOM 1056 O GLU A 443 9.533 -10.522 25.506 1.00 23.49 O
ANISOU 1056 O GLU A 443 3452 1988 3485 278 -141 198 O
ATOM 1057 CB GLU A 443 8.952 -7.864 27.147 1.00 27.64 C
ANISOU 1057 CB GLU A 443 4214 2142 4146 263 -105 54 C
ATOM 1058 CG GLU A 443 8.004 -6.691 27.324 1.00 27.83 C
ANISOU 1058 CG GLU A 443 4273 2061 4240 322 -29 41 C
ATOM 1059 CD GLU A 443 7.624 -6.439 28.792 1.00 42.71 C
ANISOU 1059 CD GLU A 443 6224 3910 6094 336 -26 -118 C
ATOM 1060 OE1 GLU A 443 8.012 -7.223 29.701 1.00 31.28 O
ANISOU 1060 OE1 GLU A 443 4801 2534 4550 306 -77 -211 O
ATOM 1061 OE2 GLU A 443 6.896 -5.452 29.019 1.00 40.79 O
ANISOU 1061 OE2 GLU A 443 6005 3572 5922 386 14 -146 O
ATOM 1062 N GLU A 444 9.859 -10.877 27.687 1.00 17.49 N
ANISOU 1062 N GLU A 444 2759 1224 2663 243 -199 14 N
ATOM 1063 CA GLU A 444 10.805 -11.954 27.428 1.00 17.78 C
ANISOU 1063 CA GLU A 444 2699 1397 2659 204 -238 40 C
ATOM 1064 C GLU A 444 10.060 -13.204 26.997 1.00 19.49 C
ANISOU 1064 C GLU A 444 2869 1716 2819 293 -213 77 C
ATOM 1065 O GLU A 444 10.473 -13.905 26.056 1.00 17.04 O
ANISOU 1065 O GLU A 444 2481 1490 2503 292 -208 134 O
ATOM 1066 CB GLU A 444 11.621 -12.227 28.684 1.00 20.52 C
ANISOU 1066 CB GLU A 444 3051 1786 2960 146 -301 -49 C
ATOM 1067 CG GLU A 444 12.673 -11.171 29.065 1.00 24.47 C
ANISOU 1067 CG GLU A 444 3568 2221 3510 18 -345 -98 C
ATOM 1068 CD GLU A 444 13.266 -11.438 30.449 1.00 25.57 C
ANISOU 1068 CD GLU A 444 3715 2427 3574 -28 -417 -199 C
ATOM 1069 OE1 GLU A 444 12.516 -11.891 31.353 1.00 21.85 O
ANISOU 1069 OE1 GLU A 444 3295 1982 3024 44 -413 -252 O
ATOM 1070 OE2 GLU A 444 14.483 -11.220 30.650 1.00 25.28 O
ANISOU 1070 OE2 GLU A 444 3622 2436 3548 -139 -478 -219 O
ATOM 1071 N PHE A 445 8.923 -13.474 27.643 1.00 18.06 N
ANISOU 1071 N PHE A 445 2736 1529 2599 366 -189 39 N
ATOM 1072 CA PHE A 445 8.103 -14.618 27.223 1.00 18.41 C
ANISOU 1072 CA PHE A 445 2737 1659 2600 432 -162 71 C
ATOM 1073 C PHE A 445 7.772 -14.565 25.729 1.00 17.96 C
ANISOU 1073 C PHE A 445 2626 1632 2566 451 -132 151 C
ATOM 1074 O PHE A 445 7.927 -15.559 25.006 1.00 14.52 O
ANISOU 1074 O PHE A 445 2128 1285 2104 453 -130 175 O
ATOM 1075 CB PHE A 445 6.823 -14.637 28.059 1.00 17.85 C
ANISOU 1075 CB PHE A 445 2716 1573 2493 498 -130 30 C
ATOM 1076 CG PHE A 445 5.766 -15.538 27.521 1.00 14.32 C
ANISOU 1076 CG PHE A 445 2208 1215 2019 534 -92 65 C
ATOM 1077 CD1 PHE A 445 5.942 -16.921 27.515 1.00 13.17 C
ANISOU 1077 CD1 PHE A 445 2030 1136 1837 528 -102 68 C
ATOM 1078 CD2 PHE A 445 4.591 -14.984 27.014 1.00 14.11 C
ANISOU 1078 CD2 PHE A 445 2154 1201 2008 569 -51 93 C
ATOM 1079 CE1 PHE A 445 4.943 -17.746 27.005 1.00 14.57 C
ANISOU 1079 CE1 PHE A 445 2162 1377 1996 545 -69 86 C
ATOM 1080 CE2 PHE A 445 3.554 -15.815 26.514 1.00 16.68 C
ANISOU 1080 CE2 PHE A 445 2422 1613 2302 596 -28 116 C
ATOM 1081 CZ PHE A 445 3.734 -17.182 26.513 1.00 15.22 C
ANISOU 1081 CZ PHE A 445 2219 1480 2084 579 -37 107 C
ATOM 1082 N VAL A 446 7.292 -13.422 25.240 1.00 14.28 N
ANISOU 1082 N VAL A 446 2186 1095 2145 473 -106 195 N
ATOM 1083 CA VAL A 446 6.842 -13.445 23.842 1.00 18.06 C
ANISOU 1083 CA VAL A 446 2606 1635 2619 503 -81 284 C
ATOM 1084 C VAL A 446 8.011 -13.666 22.898 1.00 18.29 C
ANISOU 1084 C VAL A 446 2576 1725 2650 439 -94 331 C
ATOM 1085 O VAL A 446 7.845 -14.243 21.811 1.00 16.71 O
ANISOU 1085 O VAL A 446 2311 1629 2407 454 -80 374 O
ATOM 1086 CB VAL A 446 6.036 -12.172 23.493 1.00 18.86 C
ANISOU 1086 CB VAL A 446 2727 1673 2764 537 -59 333 C
ATOM 1087 CG1 VAL A 446 4.799 -12.108 24.377 1.00 18.73 C
ANISOU 1087 CG1 VAL A 446 2719 1662 2736 582 -42 270 C
ATOM 1088 CG2 VAL A 446 6.879 -10.870 23.627 1.00 14.64 C
ANISOU 1088 CG2 VAL A 446 2262 989 2312 491 -60 356 C
ATOM 1089 N CYS A 447 9.204 -13.203 23.268 1.00 16.75 N
ANISOU 1089 N CYS A 447 2392 1478 2495 364 -117 317 N
ATOM 1090 CA CYS A 447 10.360 -13.422 22.408 1.00 15.65 C
ANISOU 1090 CA CYS A 447 2178 1414 2356 304 -121 364 C
ATOM 1091 C CYS A 447 10.690 -14.912 22.352 1.00 16.79 C
ANISOU 1091 C CYS A 447 2262 1674 2443 323 -130 320 C
ATOM 1092 O CYS A 447 11.037 -15.465 21.292 1.00 15.32 O
ANISOU 1092 O CYS A 447 2008 1588 2226 325 -109 352 O
ATOM 1093 CB CYS A 447 11.569 -12.664 22.972 1.00 17.34 C
ANISOU 1093 CB CYS A 447 2402 1561 2627 207 -150 349 C
ATOM 1094 SG CYS A 447 11.582 -10.839 22.725 1.00 24.23 S
ANISOU 1094 SG CYS A 447 3342 2269 3597 149 -128 418 S
ATOM 1095 N LEU A 448 10.634 -15.572 23.505 1.00 13.31 N
ANISOU 1095 N LEU A 448 1851 1220 1988 338 -157 245 N
ATOM 1096 CA LEU A 448 10.980 -16.996 23.580 1.00 10.54 C
ANISOU 1096 CA LEU A 448 1458 947 1602 364 -162 211 C
ATOM 1097 C LEU A 448 9.994 -17.830 22.792 1.00 11.61 C
ANISOU 1097 C LEU A 448 1579 1134 1699 414 -126 210 C
ATOM 1098 O LEU A 448 10.381 -18.780 22.101 1.00 14.53 O
ANISOU 1098 O LEU A 448 1900 1574 2048 425 -110 199 O
ATOM 1099 CB LEU A 448 10.987 -17.463 25.046 1.00 12.91 C
ANISOU 1099 CB LEU A 448 1801 1215 1888 376 -197 155 C
ATOM 1100 CG LEU A 448 12.203 -17.034 25.862 1.00 16.29 C
ANISOU 1100 CG LEU A 448 2217 1640 2332 320 -249 139 C
ATOM 1101 CD1 LEU A 448 12.105 -17.652 27.306 1.00 16.17 C
ANISOU 1101 CD1 LEU A 448 2244 1627 2274 345 -284 93 C
ATOM 1102 CD2 LEU A 448 13.515 -17.463 25.239 1.00 19.47 C
ANISOU 1102 CD2 LEU A 448 2524 2126 2749 298 -258 167 C
ATOM 1103 N LYS A 449 8.704 -17.466 22.864 1.00 12.89 N
ANISOU 1103 N LYS A 449 1780 1267 1851 444 -111 215 N
ATOM 1104 CA LYS A 449 7.703 -18.227 22.124 1.00 14.96 C
ANISOU 1104 CA LYS A 449 2017 1597 2072 474 -85 208 C
ATOM 1105 C LYS A 449 7.915 -18.041 20.613 1.00 16.09 C
ANISOU 1105 C LYS A 449 2100 1827 2187 465 -68 256 C
ATOM 1106 O LYS A 449 7.745 -18.986 19.843 1.00 14.60 O
ANISOU 1106 O LYS A 449 1873 1722 1954 468 -52 225 O
ATOM 1107 CB LYS A 449 6.297 -17.777 22.548 1.00 13.37 C
ANISOU 1107 CB LYS A 449 1847 1369 1866 510 -75 213 C
ATOM 1108 CG LYS A 449 5.183 -18.710 22.121 1.00 18.31 C
ANISOU 1108 CG LYS A 449 2439 2069 2450 524 -57 190 C
ATOM 1109 CD LYS A 449 3.875 -18.425 22.886 1.00 17.81 C
ANISOU 1109 CD LYS A 449 2396 1988 2385 560 -44 187 C
ATOM 1110 CE LYS A 449 3.487 -16.945 22.777 1.00 19.04 C
ANISOU 1110 CE LYS A 449 2564 2105 2564 607 -38 247 C
ATOM 1111 NZ LYS A 449 2.014 -16.801 23.107 1.00 19.53 N
ANISOU 1111 NZ LYS A 449 2608 2200 2614 661 -14 251 N
ATOM 1112 N SER A 450 8.302 -16.815 20.175 1.00 12.71 N
ANISOU 1112 N SER A 450 1668 1380 1781 449 -66 332 N
ATOM 1113 CA SER A 450 8.609 -16.583 18.769 1.00 14.13 C
ANISOU 1113 CA SER A 450 1790 1658 1922 438 -45 397 C
ATOM 1114 C SER A 450 9.864 -17.341 18.321 1.00 12.96 C
ANISOU 1114 C SER A 450 1588 1581 1756 409 -34 368 C
ATOM 1115 O SER A 450 9.897 -17.874 17.191 1.00 14.40 O
ANISOU 1115 O SER A 450 1718 1883 1871 415 -8 366 O
ATOM 1116 CB SER A 450 8.780 -15.078 18.540 1.00 17.63 C
ANISOU 1116 CB SER A 450 2253 2039 2409 422 -40 502 C
ATOM 1117 OG SER A 450 7.476 -14.541 18.413 1.00 26.21 O
ANISOU 1117 OG SER A 450 3361 3110 3487 479 -36 546 O
ATOM 1118 N ILE A 451 10.909 -17.394 19.178 1.00 15.47 N
ANISOU 1118 N ILE A 451 1910 1843 2126 382 -52 342 N
ATOM 1119 CA ILE A 451 12.072 -18.238 18.883 1.00 14.23 C
ANISOU 1119 CA ILE A 451 1690 1759 1958 377 -40 310 C
ATOM 1120 C ILE A 451 11.656 -19.685 18.614 1.00 14.10 C
ANISOU 1120 C ILE A 451 1670 1788 1901 426 -21 227 C
ATOM 1121 O ILE A 451 12.054 -20.280 17.591 1.00 16.60 O
ANISOU 1121 O ILE A 451 1934 2203 2171 439 16 205 O
ATOM 1122 CB ILE A 451 13.130 -18.122 19.992 1.00 12.57 C
ANISOU 1122 CB ILE A 451 1475 1495 1806 350 -76 296 C
ATOM 1123 CG1 ILE A 451 13.851 -16.772 19.789 1.00 18.34 C
ANISOU 1123 CG1 ILE A 451 2182 2212 2575 274 -80 374 C
ATOM 1124 CG2 ILE A 451 14.222 -19.236 19.862 1.00 13.29 C
ANISOU 1124 CG2 ILE A 451 1494 1663 1892 379 -64 258 C
ATOM 1125 CD1 ILE A 451 14.608 -16.241 21.085 1.00 16.36 C
ANISOU 1125 CD1 ILE A 451 1946 1887 2383 216 -133 353 C
ATOM 1126 N ILE A 452 10.842 -20.267 19.505 1.00 15.82 N
ANISOU 1126 N ILE A 452 1945 1933 2133 449 -39 176 N
ATOM 1127 CA ILE A 452 10.405 -21.657 19.332 1.00 15.10 C
ANISOU 1127 CA ILE A 452 1863 1854 2021 478 -18 97 C
ATOM 1128 C ILE A 452 9.742 -21.859 17.953 1.00 15.84 C
ANISOU 1128 C ILE A 452 1926 2051 2042 471 12 76 C
ATOM 1129 O ILE A 452 10.007 -22.849 17.259 1.00 14.76 O
ANISOU 1129 O ILE A 452 1768 1965 1876 484 43 5 O
ATOM 1130 CB ILE A 452 9.447 -22.072 20.472 1.00 17.98 C
ANISOU 1130 CB ILE A 452 2293 2129 2409 486 -36 70 C
ATOM 1131 CG1 ILE A 452 10.189 -22.138 21.866 1.00 11.50 C
ANISOU 1131 CG1 ILE A 452 1501 1232 1635 499 -67 80 C
ATOM 1132 CG2 ILE A 452 8.760 -23.485 20.095 1.00 12.31 C
ANISOU 1132 CG2 ILE A 452 1588 1414 1675 491 -7 -10 C
ATOM 1133 CD1 ILE A 452 9.191 -22.341 23.038 1.00 14.68 C
ANISOU 1133 CD1 ILE A 452 1970 1565 2042 503 -78 71 C
ATOM 1134 N LEU A 453 8.807 -20.963 17.575 1.00 12.61 N
ANISOU 1134 N LEU A 453 1516 1676 1600 458 1 131 N
ATOM 1135 CA LEU A 453 8.153 -21.053 16.277 1.00 16.91 C
ANISOU 1135 CA LEU A 453 2020 2349 2057 450 16 125 C
ATOM 1136 C LEU A 453 9.165 -21.117 15.148 1.00 19.51 C
ANISOU 1136 C LEU A 453 2293 2789 2330 447 50 130 C
ATOM 1137 O LEU A 453 9.083 -21.960 14.246 1.00 16.16 O
ANISOU 1137 O LEU A 453 1843 2463 1834 446 75 50 O
ATOM 1138 CB LEU A 453 7.214 -19.833 16.089 1.00 16.66 C
ANISOU 1138 CB LEU A 453 1984 2341 2006 456 -4 225 C
ATOM 1139 CG LEU A 453 6.576 -19.702 14.686 1.00 14.18 C
ANISOU 1139 CG LEU A 453 1612 2194 1582 455 0 254 C
ATOM 1140 CD1 LEU A 453 5.643 -20.877 14.485 1.00 15.86 C
ANISOU 1140 CD1 LEU A 453 1813 2465 1747 436 -6 141 C
ATOM 1141 CD2 LEU A 453 5.797 -18.398 14.560 1.00 16.28 C
ANISOU 1141 CD2 LEU A 453 1871 2470 1846 485 -18 383 C
ATOM 1142 N LEU A 454 10.163 -20.260 15.195 1.00 13.91 N
ANISOU 1142 N LEU A 454 1563 2071 1652 440 55 213 N
ATOM 1143 CA LEU A 454 11.031 -20.161 14.046 1.00 17.07 C
ANISOU 1143 CA LEU A 454 1896 2602 1988 433 96 240 C
ATOM 1144 C LEU A 454 12.156 -21.184 14.085 1.00 19.15 C
ANISOU 1144 C LEU A 454 2130 2878 2268 456 130 154 C
ATOM 1145 O LEU A 454 12.651 -21.587 13.013 1.00 18.01 O
ANISOU 1145 O LEU A 454 1932 2864 2046 467 178 121 O
ATOM 1146 CB LEU A 454 11.620 -18.756 13.944 1.00 16.71 C
ANISOU 1146 CB LEU A 454 1829 2551 1969 400 96 381 C
ATOM 1147 CG LEU A 454 10.627 -17.627 13.626 1.00 20.16 C
ANISOU 1147 CG LEU A 454 2288 2986 2386 396 78 494 C
ATOM 1148 CD1 LEU A 454 11.384 -16.328 13.901 1.00 20.02 C
ANISOU 1148 CD1 LEU A 454 2275 2889 2444 354 81 615 C
ATOM 1149 CD2 LEU A 454 10.172 -17.697 12.203 1.00 20.73 C
ANISOU 1149 CD2 LEU A 454 2311 3240 2325 406 101 526 C
ATOM 1150 N ASN A 455 12.486 -21.673 15.280 1.00 14.69 N
ANISOU 1150 N ASN A 455 1598 2188 1793 475 108 113 N
ATOM 1151 CA ASN A 455 13.642 -22.549 15.480 1.00 17.15 C
ANISOU 1151 CA ASN A 455 1876 2500 2142 517 135 57 C
ATOM 1152 C ASN A 455 13.316 -24.030 15.439 1.00 21.65 C
ANISOU 1152 C ASN A 455 2482 3032 2710 566 160 -70 C
ATOM 1153 O ASN A 455 14.179 -24.801 14.978 1.00 21.19 O
ANISOU 1153 O ASN A 455 2384 3019 2648 617 209 -130 O
ATOM 1154 CB ASN A 455 14.353 -22.254 16.823 1.00 17.28 C
ANISOU 1154 CB ASN A 455 1897 2419 2252 517 91 100 C
ATOM 1155 CG ASN A 455 15.635 -23.116 17.008 1.00 19.77 C
ANISOU 1155 CG ASN A 455 2152 2757 2604 577 115 64 C
ATOM 1156 OD1 ASN A 455 16.618 -22.923 16.293 1.00 22.33 O
ANISOU 1156 OD1 ASN A 455 2385 3192 2906 581 154 88 O
ATOM 1157 ND2 ASN A 455 15.632 -24.014 17.996 1.00 17.58 N
ANISOU 1157 ND2 ASN A 455 1917 2380 2382 630 94 23 N
ATOM 1158 N SER A 456 12.143 -24.477 15.965 1.00 22.66 N
ANISOU 1158 N SER A 456 2686 3069 2855 554 134 -114 N
ATOM 1159 CA SER A 456 12.014 -25.921 16.202 1.00 22.92 C
ANISOU 1159 CA SER A 456 2765 3019 2925 591 159 -223 C
ATOM 1160 C SER A 456 12.012 -26.718 14.923 1.00 28.11 C
ANISOU 1160 C SER A 456 3407 3761 3514 601 216 -337 C
ATOM 1161 O SER A 456 12.535 -27.840 14.932 1.00 25.84 O
ANISOU 1161 O SER A 456 3138 3413 3269 658 258 -425 O
ATOM 1162 CB SER A 456 10.781 -26.307 17.028 1.00 23.37 C
ANISOU 1162 CB SER A 456 2898 2965 3016 561 129 -242 C
ATOM 1163 OG SER A 456 10.947 -25.696 18.288 1.00 31.62 O
ANISOU 1163 OG SER A 456 3961 3935 4117 566 85 -154 O
ATOM 1164 N GLY A 457 11.450 -26.177 13.825 1.00 20.68 N
ANISOU 1164 N GLY A 457 2434 2961 2464 555 219 -338 N
ATOM 1165 CA GLY A 457 11.418 -26.941 12.600 1.00 23.42 C
ANISOU 1165 CA GLY A 457 2768 3410 2723 557 270 -464 C
ATOM 1166 C GLY A 457 12.532 -26.648 11.612 1.00 31.01 C
ANISOU 1166 C GLY A 457 3649 4523 3609 593 325 -453 C
ATOM 1167 O GLY A 457 12.567 -27.270 10.553 1.00 26.80 O
ANISOU 1167 O GLY A 457 3104 4094 2984 601 375 -570 O
ATOM 1168 N VAL A 458 13.462 -25.746 11.939 1.00 29.65 N
ANISOU 1168 N VAL A 458 3421 4374 3471 608 320 -324 N
ATOM 1169 CA VAL A 458 14.368 -25.218 10.920 1.00 25.04 C
ANISOU 1169 CA VAL A 458 2746 3967 2801 617 372 -279 C
ATOM 1170 C VAL A 458 15.440 -26.216 10.503 1.00 32.48 C
ANISOU 1170 C VAL A 458 3650 4949 3743 699 453 -387 C
ATOM 1171 O VAL A 458 16.043 -26.045 9.431 1.00 37.89 O
ANISOU 1171 O VAL A 458 4261 5812 4325 710 516 -391 O
ATOM 1172 CB VAL A 458 14.998 -23.898 11.422 1.00 22.31 C
ANISOU 1172 CB VAL A 458 2350 3623 2505 585 343 -105 C
ATOM 1173 CG1 VAL A 458 16.107 -24.166 12.497 1.00 33.98 C
ANISOU 1173 CG1 VAL A 458 3801 5001 4107 631 338 -90 C
ATOM 1174 CG2 VAL A 458 15.442 -22.989 10.180 1.00 30.86 C
ANISOU 1174 CG2 VAL A 458 3348 4908 3469 551 387 -10 C
ATOM 1175 N TYR A 459 15.676 -27.279 11.286 1.00 28.87 N
ANISOU 1175 N TYR A 459 3239 4336 3394 765 461 -472 N
ATOM 1176 CA TYR A 459 16.634 -28.330 10.907 1.00 36.73 C
ANISOU 1176 CA TYR A 459 4206 5346 4405 868 545 -585 C
ATOM 1177 C TYR A 459 16.019 -29.589 10.309 1.00 36.03 C
ANISOU 1177 C TYR A 459 4198 5208 4283 890 592 -783 C
ATOM 1178 O TYR A 459 16.758 -30.541 10.022 1.00 41.02 O
ANISOU 1178 O TYR A 459 4835 5801 4951 964 661 -872 O
ATOM 1179 CB TYR A 459 17.511 -28.707 12.101 1.00 33.29 C
ANISOU 1179 CB TYR A 459 3756 4778 4115 951 533 -538 C
ATOM 1180 CG TYR A 459 18.314 -27.495 12.466 1.00 38.80 C
ANISOU 1180 CG TYR A 459 4353 5564 4826 919 499 -374 C
ATOM 1181 CD1 TYR A 459 19.035 -26.818 11.472 1.00 43.54 C
ANISOU 1181 CD1 TYR A 459 4844 6364 5335 902 551 -327 C
ATOM 1182 CD2 TYR A 459 18.281 -26.964 13.738 1.00 42.83 C
ANISOU 1182 CD2 TYR A 459 4880 5968 5425 888 416 -268 C
ATOM 1183 CE1 TYR A 459 19.739 -25.696 11.753 1.00 46.83 C
ANISOU 1183 CE1 TYR A 459 5171 6853 5771 849 524 -180 C
ATOM 1184 CE2 TYR A 459 18.997 -25.831 14.028 1.00 51.50 C
ANISOU 1184 CE2 TYR A 459 5891 7142 6534 837 383 -138 C
ATOM 1185 CZ TYR A 459 19.715 -25.188 13.030 1.00 47.07 C
ANISOU 1185 CZ TYR A 459 5223 6761 5901 811 437 -91 C
ATOM 1186 OH TYR A 459 20.434 -24.047 13.309 1.00 64.82 O
ANISOU 1186 OH TYR A 459 7385 9072 8172 739 408 40 O
ATOM 1187 N THR A 460 14.711 -29.613 10.079 1.00 38.22 N
ANISOU 1187 N THR A 460 4544 5472 4506 799 550 -834 N
ATOM 1188 CA THR A 460 14.051 -30.753 9.446 1.00 37.64 C
ANISOU 1188 CA THR A 460 4545 5363 4393 786 587 -1035 C
ATOM 1189 C THR A 460 13.398 -30.399 8.110 1.00 46.21 C
ANISOU 1189 C THR A 460 5606 6662 5292 703 587 -1089 C
ATOM 1190 O THR A 460 12.461 -31.081 7.676 1.00 47.22 O
ANISOU 1190 O THR A 460 5799 6762 5379 631 572 -1216 O
ATOM 1191 CB THR A 460 13.047 -31.384 10.419 1.00 41.76 C
ANISOU 1191 CB THR A 460 5173 5667 5028 740 536 -1067 C
ATOM 1192 OG1 THR A 460 12.244 -30.354 11.022 1.00 38.05 O
ANISOU 1192 OG1 THR A 460 4693 5208 4555 660 448 -919 O
ATOM 1193 N PHE A 461 13.902 -29.370 7.428 1.00 44.06 N
ANISOU 1193 N PHE A 461 5236 6602 4904 705 600 -982 N
ATOM 1194 CA PHE A 461 13.517 -29.104 6.045 1.00 45.86 C
ANISOU 1194 CA PHE A 461 5435 7043 4948 640 604 -1009 C
ATOM 1195 C PHE A 461 14.273 -30.087 5.118 1.00 42.18 C
ANISOU 1195 C PHE A 461 4984 6593 4451 676 682 -1142 C
ATOM 1196 O PHE A 461 13.689 -30.992 4.533 1.00 53.35 O
ANISOU 1196 O PHE A 461 6466 7981 5826 636 686 -1299 O
ATOM 1197 CB PHE A 461 13.846 -27.651 5.651 1.00 39.69 C
ANISOU 1197 CB PHE A 461 4552 6463 4064 627 598 -814 C
ATOM 1198 CG PHE A 461 12.957 -26.596 6.284 1.00 40.12 C
ANISOU 1198 CG PHE A 461 4613 6483 4149 565 506 -649 C
ATOM 1199 CD1 PHE A 461 11.588 -26.579 6.073 1.00 47.05 C
ANISOU 1199 CD1 PHE A 461 5525 7392 4959 496 441 -679 C
ATOM 1200 CD2 PHE A 461 13.515 -25.611 7.089 1.00 42.37 C
ANISOU 1200 CD2 PHE A 461 4867 6693 4539 572 482 -462 C
ATOM 1201 CE1 PHE A 461 10.786 -25.582 6.656 1.00 42.86 C
ANISOU 1201 CE1 PHE A 461 4997 6817 4470 454 360 -516 C
ATOM 1202 CE2 PHE A 461 12.729 -24.605 7.679 1.00 38.27 C
ANISOU 1202 CE2 PHE A 461 4366 6113 4063 521 402 -314 C
ATOM 1203 CZ PHE A 461 11.363 -24.585 7.457 1.00 32.49 C
ANISOU 1203 CZ PHE A 461 3667 5410 3266 473 345 -337 C
ATOM 1204 N THR A 465 16.621 -26.780 -1.940 1.00 44.21 N
ANISOU 1204 N THR A 465 4817 8187 3795 585 851 -772 N
ATOM 1205 CA THR A 465 16.504 -25.946 -3.130 1.00 47.07 C
ANISOU 1205 CA THR A 465 5114 8792 3980 542 840 -651 C
ATOM 1206 C THR A 465 17.061 -24.558 -2.913 1.00 45.03 C
ANISOU 1206 C THR A 465 4777 8587 3746 527 840 -386 C
ATOM 1207 O THR A 465 17.336 -24.157 -1.792 1.00 36.95 O
ANISOU 1207 O THR A 465 3753 7417 2870 536 831 -295 O
ATOM 1208 CB THR A 465 15.047 -25.813 -3.577 1.00 45.10 C
ANISOU 1208 CB THR A 465 4889 8622 3624 475 745 -664 C
ATOM 1209 OG1 THR A 465 14.295 -25.127 -2.563 1.00 44.05 O
ANISOU 1209 OG1 THR A 465 4773 8375 3588 449 667 -538 O
ATOM 1210 CG2 THR A 465 14.438 -27.176 -3.863 1.00 44.97 C
ANISOU 1210 CG2 THR A 465 4950 8557 3581 464 741 -930 C
ATOM 1211 N LEU A 466 17.215 -23.800 -3.993 1.00 41.50 N
ANISOU 1211 N LEU A 466 4265 8346 3156 500 850 -256 N
ATOM 1212 CA LEU A 466 17.725 -22.453 -3.801 1.00 38.92 C
ANISOU 1212 CA LEU A 466 3874 8045 2867 472 853 5 C
ATOM 1213 C LEU A 466 16.700 -21.607 -3.025 1.00 39.94 C
ANISOU 1213 C LEU A 466 4038 8069 3069 434 760 149 C
ATOM 1214 O LEU A 466 17.074 -20.818 -2.149 1.00 32.65 O
ANISOU 1214 O LEU A 466 3103 7030 2274 420 759 302 O
ATOM 1215 CB LEU A 466 18.081 -21.888 -5.165 1.00 43.58 C
ANISOU 1215 CB LEU A 466 4394 8872 3291 453 888 112 C
ATOM 1216 CG LEU A 466 18.821 -20.603 -5.356 1.00 47.84 C
ANISOU 1216 CG LEU A 466 4860 9475 3841 419 918 369 C
ATOM 1217 CD1 LEU A 466 20.195 -20.848 -4.745 1.00 44.15 C
ANISOU 1217 CD1 LEU A 466 4350 8930 3494 444 1001 345 C
ATOM 1218 CD2 LEU A 466 18.960 -20.479 -6.851 1.00 45.68 C
ANISOU 1218 CD2 LEU A 466 4534 9454 3370 413 953 396 C
ATOM 1219 N LYS A 467 15.398 -21.812 -3.279 1.00 36.10 N
ANISOU 1219 N LYS A 467 3592 7612 2511 416 683 90 N
ATOM 1220 CA LYS A 467 14.368 -21.189 -2.452 1.00 39.45 C
ANISOU 1220 CA LYS A 467 4052 7922 3014 395 600 195 C
ATOM 1221 C LYS A 467 14.470 -21.626 -0.993 1.00 35.74 C
ANISOU 1221 C LYS A 467 3637 7226 2715 416 600 119 C
ATOM 1222 O LYS A 467 14.261 -20.817 -0.077 1.00 31.26 O
ANISOU 1222 O LYS A 467 3084 6539 2255 406 569 265 O
ATOM 1223 CB LYS A 467 12.973 -21.516 -3.011 1.00 43.97 C
ANISOU 1223 CB LYS A 467 4643 8584 3479 374 520 116 C
ATOM 1224 CG LYS A 467 11.818 -20.978 -2.130 1.00 46.11 C
ANISOU 1224 CG LYS A 467 4948 8739 3834 362 435 207 C
ATOM 1225 CD LYS A 467 10.553 -20.644 -2.928 1.00 52.52 C
ANISOU 1225 CD LYS A 467 5726 9697 4530 342 357 259 C
ATOM 1226 CE LYS A 467 9.856 -21.913 -3.370 1.00 47.85 C
ANISOU 1226 CE LYS A 467 5152 9177 3854 314 329 8 C
ATOM 1227 NZ LYS A 467 8.421 -21.774 -3.808 1.00 47.53 N
ANISOU 1227 NZ LYS A 467 5077 9248 3736 284 239 24 N
ATOM 1228 N SER A 468 14.762 -22.902 -0.741 1.00 34.30 N
ANISOU 1228 N SER A 468 3492 6971 2569 448 636 -108 N
ATOM 1229 CA SER A 468 14.815 -23.354 0.651 1.00 36.81 C
ANISOU 1229 CA SER A 468 3860 7072 3053 476 633 -178 C
ATOM 1230 C SER A 468 15.998 -22.719 1.366 1.00 30.39 C
ANISOU 1230 C SER A 468 2998 6190 2360 494 683 -41 C
ATOM 1231 O SER A 468 15.915 -22.366 2.562 1.00 32.08 O
ANISOU 1231 O SER A 468 3228 6255 2704 497 659 25 O
ATOM 1232 CB SER A 468 14.921 -24.878 0.705 1.00 43.30 C
ANISOU 1232 CB SER A 468 4737 7809 3906 513 666 -440 C
ATOM 1233 OG SER A 468 13.669 -25.466 0.423 1.00 57.90 O
ANISOU 1233 OG SER A 468 6642 9666 5693 473 606 -569 O
ATOM 1234 N LEU A 469 17.093 -22.520 0.617 1.00 33.51 N
ANISOU 1234 N LEU A 469 3323 6704 2706 500 749 8 N
ATOM 1235 CA LEU A 469 18.269 -21.848 1.160 1.00 33.86 C
ANISOU 1235 CA LEU A 469 3299 6710 2856 496 793 148 C
ATOM 1236 C LEU A 469 17.936 -20.409 1.535 1.00 35.00 C
ANISOU 1236 C LEU A 469 3434 6825 3041 430 749 389 C
ATOM 1237 O LEU A 469 18.332 -19.935 2.615 1.00 32.54 O
ANISOU 1237 O LEU A 469 3108 6382 2872 414 746 475 O
ATOM 1238 CB LEU A 469 19.393 -21.894 0.142 1.00 31.82 C
ANISOU 1238 CB LEU A 469 2962 6609 2517 505 872 157 C
ATOM 1239 CG LEU A 469 20.276 -23.129 0.231 1.00 50.44 C
ANISOU 1239 CG LEU A 469 5309 8934 4922 585 940 -33 C
ATOM 1240 CD1 LEU A 469 21.280 -23.153 -0.921 1.00 40.10 C
ANISOU 1240 CD1 LEU A 469 3921 7809 3507 597 1024 -25 C
ATOM 1241 CD2 LEU A 469 20.945 -23.198 1.606 1.00 38.03 C
ANISOU 1241 CD2 LEU A 469 3715 7194 3542 614 941 -15 C
ATOM 1242 N GLU A 470 17.199 -19.714 0.648 1.00 30.25 N
ANISOU 1242 N GLU A 470 2839 6334 2321 394 714 500 N
ATOM 1243 CA GLU A 470 16.712 -18.359 0.903 1.00 28.50 C
ANISOU 1243 CA GLU A 470 2627 6058 2143 344 669 731 C
ATOM 1244 C GLU A 470 15.840 -18.320 2.130 1.00 31.29 C
ANISOU 1244 C GLU A 470 3049 6234 2604 351 611 723 C
ATOM 1245 O GLU A 470 15.965 -17.403 2.950 1.00 31.08 O
ANISOU 1245 O GLU A 470 3033 6076 2701 316 600 876 O
ATOM 1246 CB GLU A 470 15.935 -17.841 -0.314 1.00 31.66 C
ANISOU 1246 CB GLU A 470 3022 6609 2398 331 633 821 C
ATOM 1247 CG GLU A 470 16.850 -17.549 -1.524 1.00 34.48 C
ANISOU 1247 CG GLU A 470 3305 7146 2651 314 696 892 C
ATOM 1248 CD GLU A 470 16.132 -17.327 -2.862 1.00 42.20 C
ANISOU 1248 CD GLU A 470 4264 8314 3455 316 669 937 C
ATOM 1249 OE1 GLU A 470 14.888 -17.518 -2.950 1.00 39.48 O
ANISOU 1249 OE1 GLU A 470 3957 7982 3063 332 596 890 O
ATOM 1250 OE2 GLU A 470 16.828 -17.002 -3.866 1.00 41.73 O
ANISOU 1250 OE2 GLU A 470 4144 8411 3303 302 721 1015 O
ATOM 1251 N GLU A 471 14.924 -19.300 2.257 1.00 27.11 N
ANISOU 1251 N GLU A 471 2572 5696 2032 388 573 543 N
ATOM 1252 CA GLU A 471 14.012 -19.352 3.395 1.00 30.48 C
ANISOU 1252 CA GLU A 471 3065 5970 2545 399 520 523 C
ATOM 1253 C GLU A 471 14.792 -19.489 4.701 1.00 26.47 C
ANISOU 1253 C GLU A 471 2576 5232 2250 402 517 489 C
ATOM 1254 O GLU A 471 14.537 -18.766 5.672 1.00 24.58 O
ANISOU 1254 O GLU A 471 2382 4801 2155 377 459 584 O
ATOM 1255 CB GLU A 471 13.024 -20.528 3.246 1.00 23.76 C
ANISOU 1255 CB GLU A 471 2261 5141 1625 422 480 306 C
ATOM 1256 CG GLU A 471 12.086 -20.451 2.074 1.00 33.47 C
ANISOU 1256 CG GLU A 471 3481 6531 2706 402 429 309 C
ATOM 1257 CD GLU A 471 10.833 -19.777 2.433 1.00 36.12 C
ANISOU 1257 CD GLU A 471 3843 6826 3055 395 348 419 C
ATOM 1258 OE1 GLU A 471 9.847 -20.419 2.903 1.00 29.94 O
ANISOU 1258 OE1 GLU A 471 3100 5996 2278 394 297 296 O
ATOM 1259 OE2 GLU A 471 10.883 -18.543 2.285 1.00 40.65 O
ANISOU 1259 OE2 GLU A 471 4397 7396 3652 389 339 640 O
ATOM 1260 N LYS A 472 15.750 -20.428 4.748 1.00 28.01 N
ANISOU 1260 N LYS A 472 2733 5446 2462 439 578 349 N
ATOM 1261 CA LYS A 472 16.492 -20.668 5.986 1.00 28.93 C
ANISOU 1261 CA LYS A 472 2856 5368 2767 454 566 314 C
ATOM 1262 C LYS A 472 17.307 -19.443 6.398 1.00 27.93 C
ANISOU 1262 C LYS A 472 2679 5196 2736 392 567 507 C
ATOM 1263 O LYS A 472 17.406 -19.125 7.589 1.00 23.21 O
ANISOU 1263 O LYS A 472 2118 4406 2296 371 511 534 O
ATOM 1264 CB LYS A 472 17.417 -21.850 5.809 1.00 34.06 C
ANISOU 1264 CB LYS A 472 3459 6076 3407 525 641 152 C
ATOM 1265 CG LYS A 472 16.792 -23.229 5.896 1.00 38.10 C
ANISOU 1265 CG LYS A 472 4045 6523 3909 584 634 -70 C
ATOM 1266 CD LYS A 472 18.008 -24.162 5.729 1.00 55.05 C
ANISOU 1266 CD LYS A 472 6132 8713 6073 667 724 -187 C
ATOM 1267 CE LYS A 472 17.690 -25.513 5.111 1.00 44.63 C
ANISOU 1267 CE LYS A 472 4882 7375 4701 708 746 -405 C
ATOM 1268 NZ LYS A 472 18.968 -26.128 4.620 1.00 57.18 N
ANISOU 1268 NZ LYS A 472 6418 9006 6300 768 825 -466 N
ATOM 1269 N AASP A 473 17.884 -18.738 5.426 0.97 24.23 N
ANISOU 1269 N AASP A 473 2130 4906 2169 354 632 641 N
ATOM 1270 CA AASP A 473 18.625 -17.524 5.744 0.97 27.97 C
ANISOU 1270 CA AASP A 473 2559 5329 2739 271 638 831 C
ATOM 1271 C AASP A 473 17.720 -16.487 6.378 0.97 27.72 C
ANISOU 1271 C AASP A 473 2621 5110 2799 222 556 950 C
ATOM 1272 O AASP A 473 18.076 -15.862 7.384 0.97 26.55 O
ANISOU 1272 O AASP A 473 2492 4787 2808 169 517 1003 O
ATOM 1273 CB AASP A 473 19.250 -16.948 4.489 0.97 31.81 C
ANISOU 1273 CB AASP A 473 2958 6031 3099 231 719 964 C
ATOM 1274 CG AASP A 473 20.043 -15.703 4.778 0.97 41.34 C
ANISOU 1274 CG AASP A 473 4120 7171 4416 125 728 1158 C
ATOM 1275 OD1AASP A 473 21.219 -15.836 5.190 0.97 41.56 O
ANISOU 1275 OD1AASP A 473 4062 7202 4527 99 758 1137 O
ATOM 1276 OD2AASP A 473 19.481 -14.597 4.586 0.97 45.57 O
ANISOU 1276 OD2AASP A 473 4710 7642 4964 69 699 1325 O
ATOM 1277 N HIS A 474 16.539 -16.295 5.786 1.00 26.94 N
ANISOU 1277 N HIS A 474 2578 5058 2599 245 529 987 N
ATOM 1278 CA HIS A 474 15.583 -15.344 6.314 1.00 23.93 C
ANISOU 1278 CA HIS A 474 2283 4511 2299 226 459 1098 C
ATOM 1279 C HIS A 474 15.199 -15.706 7.740 1.00 21.50 C
ANISOU 1279 C HIS A 474 2052 3974 2144 244 387 976 C
ATOM 1280 O HIS A 474 15.191 -14.851 8.623 1.00 22.44 O
ANISOU 1280 O HIS A 474 2219 3906 2399 203 350 1050 O
ATOM 1281 CB HIS A 474 14.357 -15.305 5.411 1.00 29.12 C
ANISOU 1281 CB HIS A 474 2964 5297 2805 269 439 1136 C
ATOM 1282 CG HIS A 474 13.298 -14.339 5.860 1.00 29.75 C
ANISOU 1282 CG HIS A 474 3120 5224 2960 276 375 1259 C
ATOM 1283 ND1 HIS A 474 13.480 -12.970 5.806 1.00 32.91 N
ANISOU 1283 ND1 HIS A 474 3535 5541 3429 234 388 1477 N
ATOM 1284 CD2 HIS A 474 12.062 -14.537 6.388 1.00 32.85 C
ANISOU 1284 CD2 HIS A 474 3575 5526 3379 325 305 1194 C
ATOM 1285 CE1 HIS A 474 12.387 -12.369 6.242 1.00 26.57 C
ANISOU 1285 CE1 HIS A 474 2805 4602 2688 273 331 1538 C
ATOM 1286 NE2 HIS A 474 11.517 -13.294 6.618 1.00 30.03 N
ANISOU 1286 NE2 HIS A 474 3267 5045 3100 328 280 1370 N
ATOM 1287 N ILE A 475 14.872 -16.974 7.990 1.00 22.67 N
ANISOU 1287 N ILE A 475 2217 4128 2267 301 371 786 N
ATOM 1288 CA ILE A 475 14.514 -17.405 9.353 1.00 17.98 C
ANISOU 1288 CA ILE A 475 1695 3332 1805 320 310 680 C
ATOM 1289 C ILE A 475 15.619 -17.046 10.351 1.00 25.98 C
ANISOU 1289 C ILE A 475 2689 4222 2959 278 304 703 C
ATOM 1290 O ILE A 475 15.355 -16.536 11.461 1.00 22.49 O
ANISOU 1290 O ILE A 475 2311 3601 2634 255 248 719 O
ATOM 1291 CB ILE A 475 14.217 -18.909 9.366 1.00 21.28 C
ANISOU 1291 CB ILE A 475 2126 3781 2180 379 312 483 C
ATOM 1292 CG1 ILE A 475 12.914 -19.192 8.592 1.00 22.43 C
ANISOU 1292 CG1 ILE A 475 2298 4026 2200 397 293 447 C
ATOM 1293 CG2 ILE A 475 14.036 -19.389 10.868 1.00 22.24 C
ANISOU 1293 CG2 ILE A 475 2314 3693 2443 396 257 395 C
ATOM 1294 CD1 ILE A 475 12.650 -20.702 8.306 1.00 24.55 C
ANISOU 1294 CD1 ILE A 475 2576 4349 2404 433 309 240 C
ATOM 1295 N HIS A 476 16.873 -17.304 9.970 1.00 22.12 N
ANISOU 1295 N HIS A 476 2105 3845 2454 266 361 701 N
ATOM 1296 CA HIS A 476 17.986 -17.036 10.887 1.00 27.45 C
ANISOU 1296 CA HIS A 476 2738 4440 3254 220 349 718 C
ATOM 1297 C HIS A 476 18.182 -15.542 11.105 1.00 24.66 C
ANISOU 1297 C HIS A 476 2393 4000 2975 115 333 878 C
ATOM 1298 O HIS A 476 18.540 -15.116 12.214 1.00 21.52 O
ANISOU 1298 O HIS A 476 2017 3461 2700 64 283 875 O
ATOM 1299 CB HIS A 476 19.279 -17.686 10.364 1.00 26.14 C
ANISOU 1299 CB HIS A 476 2444 4439 3048 242 420 682 C
ATOM 1300 CG HIS A 476 19.282 -19.174 10.545 1.00 29.61 C
ANISOU 1300 CG HIS A 476 2888 4892 3472 349 430 508 C
ATOM 1301 ND1 HIS A 476 19.012 -19.769 11.764 1.00 34.11 N
ANISOU 1301 ND1 HIS A 476 3523 5300 4137 389 366 419 N
ATOM 1302 CD2 HIS A 476 19.475 -20.184 9.664 1.00 32.52 C
ANISOU 1302 CD2 HIS A 476 3215 5401 3739 427 500 406 C
ATOM 1303 CE1 HIS A 476 19.061 -21.084 11.625 1.00 33.26 C
ANISOU 1303 CE1 HIS A 476 3416 5219 4003 485 397 283 C
ATOM 1304 NE2 HIS A 476 19.321 -21.359 10.361 1.00 32.09 N
ANISOU 1304 NE2 HIS A 476 3209 5245 3740 510 479 261 N
ATOM 1305 N ARG A 477 17.962 -14.738 10.051 1.00 22.39 N
ANISOU 1305 N ARG A 477 2094 3796 2616 81 376 1019 N
ATOM 1306 CA ARG A 477 17.998 -13.297 10.224 1.00 25.14 C
ANISOU 1306 CA ARG A 477 2477 4025 3051 -14 366 1179 C
ATOM 1307 C ARG A 477 16.929 -12.847 11.201 1.00 23.96 C
ANISOU 1307 C ARG A 477 2456 3656 2991 4 292 1157 C
ATOM 1308 O ARG A 477 17.193 -11.981 12.049 1.00 22.51 O
ANISOU 1308 O ARG A 477 2316 3303 2936 -72 261 1193 O
ATOM 1309 CB ARG A 477 17.836 -12.601 8.860 1.00 28.23 C
ANISOU 1309 CB ARG A 477 2841 4549 3337 -34 429 1353 C
ATOM 1310 CG ARG A 477 19.047 -12.706 7.957 1.00 33.47 C
ANISOU 1310 CG ARG A 477 3371 5422 3925 -81 516 1414 C
ATOM 1311 CD ARG A 477 18.920 -11.721 6.756 1.00 41.29 C
ANISOU 1311 CD ARG A 477 4346 6514 4830 -125 576 1635 C
ATOM 1312 NE ARG A 477 20.119 -11.639 5.915 1.00 54.91 N
ANISOU 1312 NE ARG A 477 5949 8418 6496 -183 656 1698 N
ATOM 1313 N VAL A 478 15.712 -13.435 11.115 1.00 20.67 N
ANISOU 1313 N VAL A 478 2099 3246 2508 98 265 1087 N
ATOM 1314 CA VAL A 478 14.650 -13.050 12.037 1.00 25.18 C
ANISOU 1314 CA VAL A 478 2779 3631 3157 127 205 1063 C
ATOM 1315 C VAL A 478 14.981 -13.538 13.440 1.00 23.88 C
ANISOU 1315 C VAL A 478 2643 3343 3088 119 156 927 C
ATOM 1316 O VAL A 478 14.832 -12.788 14.408 1.00 21.96 O
ANISOU 1316 O VAL A 478 2470 2926 2949 84 119 933 O
ATOM 1317 CB VAL A 478 13.259 -13.538 11.560 1.00 23.64 C
ANISOU 1317 CB VAL A 478 2617 3501 2864 219 189 1033 C
ATOM 1318 CG1 VAL A 478 12.198 -13.172 12.611 1.00 23.40 C
ANISOU 1318 CG1 VAL A 478 2683 3287 2919 255 135 1004 C
ATOM 1319 CG2 VAL A 478 12.887 -12.887 10.218 1.00 25.23 C
ANISOU 1319 CG2 VAL A 478 2790 3834 2961 228 225 1195 C
ATOM 1320 N LEU A 479 15.524 -14.765 13.568 1.00 20.64 N
ANISOU 1320 N LEU A 479 2177 3021 2643 152 160 807 N
ATOM 1321 CA LEU A 479 15.974 -15.234 14.880 1.00 17.83 C
ANISOU 1321 CA LEU A 479 1835 2570 2368 149 114 704 C
ATOM 1322 C LEU A 479 17.020 -14.280 15.481 1.00 25.74 C
ANISOU 1322 C LEU A 479 2810 3502 3467 43 97 760 C
ATOM 1323 O LEU A 479 16.938 -13.936 16.675 1.00 19.78 O
ANISOU 1323 O LEU A 479 2117 2609 2791 15 41 716 O
ATOM 1324 CB LEU A 479 16.500 -16.689 14.750 1.00 21.69 C
ANISOU 1324 CB LEU A 479 2260 3170 2809 214 133 593 C
ATOM 1325 CG LEU A 479 15.358 -17.762 14.732 1.00 17.33 C
ANISOU 1325 CG LEU A 479 1770 2611 2203 300 125 489 C
ATOM 1326 CD1 LEU A 479 15.888 -19.079 14.224 1.00 23.17 C
ANISOU 1326 CD1 LEU A 479 2452 3461 2891 361 168 393 C
ATOM 1327 CD2 LEU A 479 14.724 -18.015 16.131 1.00 19.57 C
ANISOU 1327 CD2 LEU A 479 2140 2741 2556 320 65 422 C
ATOM 1328 N ASP A 480 17.969 -13.797 14.661 1.00 18.33 N
ANISOU 1328 N ASP A 480 1781 2665 2520 -26 146 856 N
ATOM 1329 CA ASP A 480 18.978 -12.853 15.128 1.00 18.38 C
ANISOU 1329 CA ASP A 480 1748 2614 2620 -153 133 915 C
ATOM 1330 C ASP A 480 18.344 -11.563 15.661 1.00 22.67 C
ANISOU 1330 C ASP A 480 2409 2951 3252 -217 103 968 C
ATOM 1331 O ASP A 480 18.768 -11.043 16.700 1.00 24.95 O
ANISOU 1331 O ASP A 480 2724 3122 3633 -299 54 927 O
ATOM 1332 CB ASP A 480 19.942 -12.532 13.997 1.00 25.07 C
ANISOU 1332 CB ASP A 480 2476 3616 3433 -219 207 1030 C
ATOM 1333 CG ASP A 480 20.953 -13.650 13.746 1.00 29.15 C
ANISOU 1333 CG ASP A 480 2855 4324 3897 -175 238 964 C
ATOM 1334 OD1 ASP A 480 21.072 -14.587 14.568 1.00 27.23 O
ANISOU 1334 OD1 ASP A 480 2607 4072 3668 -106 194 841 O
ATOM 1335 OD2 ASP A 480 21.608 -13.610 12.709 1.00 25.17 O
ANISOU 1335 OD2 ASP A 480 2247 3982 3334 -197 313 1041 O
ATOM 1336 N LYS A 481 17.335 -11.023 14.952 1.00 23.25 N
ANISOU 1336 N LYS A 481 2554 2983 3298 -176 132 1058 N
ATOM 1337 CA LYS A 481 16.627 -9.840 15.442 1.00 26.43 C
ANISOU 1337 CA LYS A 481 3078 3173 3792 -204 112 1107 C
ATOM 1338 C LYS A 481 15.974 -10.098 16.801 1.00 24.70 C
ANISOU 1338 C LYS A 481 2950 2822 3615 -156 48 964 C
ATOM 1339 O LYS A 481 15.928 -9.194 17.647 1.00 21.78 O
ANISOU 1339 O LYS A 481 2662 2271 3342 -216 21 946 O
ATOM 1340 CB LYS A 481 15.571 -9.357 14.427 1.00 22.52 C
ANISOU 1340 CB LYS A 481 2629 2681 3247 -133 151 1237 C
ATOM 1341 CG LYS A 481 16.119 -8.864 13.097 1.00 32.65 C
ANISOU 1341 CG LYS A 481 3839 4081 4484 -185 219 1411 C
ATOM 1342 N ILE A 482 15.415 -11.299 17.022 1.00 20.37 N
ANISOU 1342 N ILE A 482 2396 2353 2991 -52 28 861 N
ATOM 1343 CA ILE A 482 14.758 -11.546 18.312 1.00 17.83 C
ANISOU 1343 CA ILE A 482 2158 1919 2697 -8 -24 742 C
ATOM 1344 C ILE A 482 15.796 -11.646 19.423 1.00 21.96 C
ANISOU 1344 C ILE A 482 2657 2416 3269 -86 -73 657 C
ATOM 1345 O ILE A 482 15.571 -11.161 20.548 1.00 24.49 O
ANISOU 1345 O ILE A 482 3060 2605 3641 -111 -115 590 O
ATOM 1346 CB ILE A 482 13.858 -12.796 18.232 1.00 16.39 C
ANISOU 1346 CB ILE A 482 1976 1822 2429 108 -27 670 C
ATOM 1347 CG1 ILE A 482 12.759 -12.558 17.197 1.00 20.55 C
ANISOU 1347 CG1 ILE A 482 2520 2386 2903 172 7 753 C
ATOM 1348 CG2 ILE A 482 13.201 -13.049 19.629 1.00 18.07 C
ANISOU 1348 CG2 ILE A 482 2271 1928 2666 146 -73 561 C
ATOM 1349 CD1 ILE A 482 11.902 -13.768 16.908 1.00 21.69 C
ANISOU 1349 CD1 ILE A 482 2649 2635 2958 259 7 684 C
ATOM 1350 N THR A 483 16.973 -12.233 19.116 1.00 20.92 N
ANISOU 1350 N THR A 483 2407 2424 3116 -123 -68 659 N
ATOM 1351 CA THR A 483 18.093 -12.178 20.055 1.00 20.98 C
ANISOU 1351 CA THR A 483 2365 2437 3169 -210 -120 604 C
ATOM 1352 C THR A 483 18.441 -10.729 20.419 1.00 21.60 C
ANISOU 1352 C THR A 483 2489 2376 3343 -352 -135 636 C
ATOM 1353 O THR A 483 18.538 -10.389 21.613 1.00 21.89 O
ANISOU 1353 O THR A 483 2579 2320 3419 -404 -196 547 O
ATOM 1354 CB THR A 483 19.308 -12.922 19.487 1.00 21.64 C
ANISOU 1354 CB THR A 483 2293 2707 3221 -219 -99 624 C
ATOM 1355 OG1 THR A 483 18.984 -14.303 19.211 1.00 20.38 O
ANISOU 1355 OG1 THR A 483 2109 2647 2986 -85 -81 574 O
ATOM 1356 CG2 THR A 483 20.493 -12.887 20.486 1.00 22.60 C
ANISOU 1356 CG2 THR A 483 2337 2865 3385 -306 -164 575 C
ATOM 1357 N ASP A 484 18.614 -9.855 19.408 1.00 20.54 N
ANISOU 1357 N ASP A 484 2340 2219 3244 -419 -79 761 N
ATOM 1358 CA ASP A 484 18.907 -8.445 19.690 1.00 26.18 C
ANISOU 1358 CA ASP A 484 3113 2767 4069 -562 -83 799 C
ATOM 1359 C ASP A 484 17.852 -7.859 20.628 1.00 24.08 C
ANISOU 1359 C ASP A 484 3010 2292 3848 -525 -112 720 C
ATOM 1360 O ASP A 484 18.182 -7.099 21.548 1.00 26.42 O
ANISOU 1360 O ASP A 484 3363 2456 4219 -632 -152 647 O
ATOM 1361 CB ASP A 484 18.918 -7.592 18.401 1.00 25.44 C
ANISOU 1361 CB ASP A 484 3012 2650 4005 -609 -5 974 C
ATOM 1362 CG ASP A 484 19.988 -7.980 17.399 1.00 31.25 C
ANISOU 1362 CG ASP A 484 3586 3594 4694 -660 41 1066 C
ATOM 1363 OD1 ASP A 484 20.899 -8.795 17.669 1.00 30.67 O
ANISOU 1363 OD1 ASP A 484 3391 3678 4585 -674 16 999 O
ATOM 1364 OD2 ASP A 484 19.893 -7.464 16.273 1.00 30.83 O
ANISOU 1364 OD2 ASP A 484 3522 3560 4630 -674 111 1218 O
ATOM 1365 N THR A 485 16.572 -8.193 20.376 1.00 22.82 N
ANISOU 1365 N THR A 485 2919 2112 3638 -375 -89 729 N
ATOM 1366 CA THR A 485 15.443 -7.693 21.161 1.00 27.34 C
ANISOU 1366 CA THR A 485 3634 2510 4245 -310 -100 664 C
ATOM 1367 C THR A 485 15.497 -8.191 22.608 1.00 26.40 C
ANISOU 1367 C THR A 485 3544 2386 4101 -308 -167 498 C
ATOM 1368 O THR A 485 15.249 -7.422 23.547 1.00 23.06 O
ANISOU 1368 O THR A 485 3224 1804 3731 -344 -187 414 O
ATOM 1369 CB THR A 485 14.124 -8.136 20.484 1.00 26.02 C
ANISOU 1369 CB THR A 485 3490 2384 4012 -150 -63 718 C
ATOM 1370 OG1 THR A 485 14.097 -7.649 19.138 1.00 28.56 O
ANISOU 1370 OG1 THR A 485 3781 2735 4336 -151 -7 883 O
ATOM 1371 CG2 THR A 485 12.864 -7.640 21.216 1.00 25.82 C
ANISOU 1371 CG2 THR A 485 3592 2202 4018 -60 -62 664 C
ATOM 1372 N LEU A 486 15.764 -9.485 22.807 1.00 23.73 N
ANISOU 1372 N LEU A 486 3124 2216 3677 -256 -196 448 N
ATOM 1373 CA LEU A 486 15.911 -9.990 24.176 1.00 23.63 C
ANISOU 1373 CA LEU A 486 3129 2219 3629 -255 -261 316 C
ATOM 1374 C LEU A 486 16.993 -9.223 24.930 1.00 24.99 C
ANISOU 1374 C LEU A 486 3292 2348 3856 -413 -315 257 C
ATOM 1375 O LEU A 486 16.787 -8.816 26.079 1.00 25.36 O
ANISOU 1375 O LEU A 486 3424 2305 3905 -441 -356 146 O
ATOM 1376 CB LEU A 486 16.239 -11.486 24.168 1.00 25.84 C
ANISOU 1376 CB LEU A 486 3312 2680 3825 -182 -280 300 C
ATOM 1377 CG LEU A 486 15.021 -12.404 24.088 1.00 26.41 C
ANISOU 1377 CG LEU A 486 3425 2774 3834 -38 -254 288 C
ATOM 1378 CD1 LEU A 486 15.568 -13.777 23.772 1.00 24.16 C
ANISOU 1378 CD1 LEU A 486 3040 2645 3496 14 -256 292 C
ATOM 1379 CD2 LEU A 486 14.171 -12.411 25.386 1.00 21.81 C
ANISOU 1379 CD2 LEU A 486 2946 2113 3228 6 -282 192 C
ATOM 1380 N ILE A 487 18.159 -9.032 24.299 1.00 21.00 N
ANISOU 1380 N ILE A 487 2675 1918 3386 -523 -313 325 N
ATOM 1381 CA ILE A 487 19.282 -8.371 24.962 1.00 28.09 C
ANISOU 1381 CA ILE A 487 3534 2804 4334 -695 -371 270 C
ATOM 1382 C ILE A 487 18.917 -6.930 25.293 1.00 27.38 C
ANISOU 1382 C ILE A 487 3584 2477 4342 -793 -360 234 C
ATOM 1383 O ILE A 487 19.195 -6.439 26.388 1.00 28.79 O
ANISOU 1383 O ILE A 487 3814 2589 4536 -888 -420 108 O
ATOM 1384 CB ILE A 487 20.550 -8.440 24.085 1.00 24.66 C
ANISOU 1384 CB ILE A 487 2936 2512 3924 -794 -355 369 C
ATOM 1385 CG1 ILE A 487 21.193 -9.834 24.103 1.00 28.83 C
ANISOU 1385 CG1 ILE A 487 3317 3272 4365 -712 -383 364 C
ATOM 1386 CG2 ILE A 487 21.558 -7.367 24.506 1.00 29.17 C
ANISOU 1386 CG2 ILE A 487 3480 3024 4581 -1011 -396 339 C
ATOM 1387 CD1 ILE A 487 21.667 -10.272 25.476 1.00 26.10 C
ANISOU 1387 CD1 ILE A 487 2944 2998 3974 -729 -482 248 C
ATOM 1388 N HIS A 488 18.277 -6.241 24.351 1.00 28.15 N
ANISOU 1388 N HIS A 488 3748 2444 4503 -764 -282 343 N
ATOM 1389 CA HIS A 488 17.808 -4.876 24.590 1.00 30.67 C
ANISOU 1389 CA HIS A 488 4218 2505 4933 -824 -256 322 C
ATOM 1390 C HIS A 488 16.894 -4.813 25.809 1.00 29.49 C
ANISOU 1390 C HIS A 488 4201 2251 4754 -743 -283 165 C
ATOM 1391 O HIS A 488 17.034 -3.931 26.654 1.00 29.62 O
ANISOU 1391 O HIS A 488 4313 2110 4831 -844 -307 49 O
ATOM 1392 CB HIS A 488 17.094 -4.380 23.342 1.00 33.29 C
ANISOU 1392 CB HIS A 488 4590 2745 5313 -749 -167 491 C
ATOM 1393 CG HIS A 488 16.402 -3.068 23.512 1.00 35.57 C
ANISOU 1393 CG HIS A 488 5044 2750 5720 -755 -126 491 C
ATOM 1394 ND1 HIS A 488 15.059 -2.973 23.807 1.00 46.53 N
ANISOU 1394 ND1 HIS A 488 6546 4056 7077 -582 -92 449 N
ATOM 1395 CD2 HIS A 488 16.839 -1.799 23.337 1.00 43.71 C
ANISOU 1395 CD2 HIS A 488 6141 3631 6837 -877 -79 515 C
ATOM 1396 CE1 HIS A 488 14.711 -1.700 23.860 1.00 40.52 C
ANISOU 1396 CE1 HIS A 488 5918 3118 6360 -587 -31 438 C
ATOM 1397 NE2 HIS A 488 15.771 -0.967 23.572 1.00 45.28 N
ANISOU 1397 NE2 HIS A 488 6505 3662 7039 -765 -21 477 N
ATOM 1398 N LEU A 489 15.944 -5.748 25.913 1.00 29.39 N
ANISOU 1398 N LEU A 489 4195 2326 4646 -566 -274 155 N
ATOM 1399 CA LEU A 489 15.058 -5.779 27.076 1.00 32.20 C
ANISOU 1399 CA LEU A 489 4661 2615 4957 -482 -291 15 C
ATOM 1400 C LEU A 489 15.851 -5.890 28.363 1.00 34.08 C
ANISOU 1400 C LEU A 489 4890 2911 5147 -590 -377 -141 C
ATOM 1401 O LEU A 489 15.598 -5.165 29.333 1.00 35.76 O
ANISOU 1401 O LEU A 489 5219 2993 5375 -627 -391 -277 O
ATOM 1402 CB LEU A 489 14.078 -6.948 26.970 1.00 31.03 C
ANISOU 1402 CB LEU A 489 4488 2595 4707 -302 -273 39 C
ATOM 1403 CG LEU A 489 12.989 -6.789 25.917 1.00 28.78 C
ANISOU 1403 CG LEU A 489 4228 2258 4449 -176 -197 162 C
ATOM 1404 CD1 LEU A 489 12.298 -8.116 25.705 1.00 21.12 C
ANISOU 1404 CD1 LEU A 489 3197 1455 3374 -45 -192 183 C
ATOM 1405 CD2 LEU A 489 12.024 -5.698 26.334 1.00 34.10 C
ANISOU 1405 CD2 LEU A 489 5045 2719 5192 -121 -155 119 C
ATOM 1406 N MET A 490 16.836 -6.779 28.379 1.00 28.29 N
ANISOU 1406 N MET A 490 4016 2381 4351 -637 -434 -124 N
ATOM 1407 CA MET A 490 17.577 -7.008 29.603 1.00 31.54 C
ANISOU 1407 CA MET A 490 4398 2891 4694 -722 -527 -254 C
ATOM 1408 C MET A 490 18.442 -5.812 29.950 1.00 30.96 C
ANISOU 1408 C MET A 490 4349 2710 4704 -930 -565 -332 C
ATOM 1409 O MET A 490 18.566 -5.468 31.131 1.00 36.68 O
ANISOU 1409 O MET A 490 5135 3415 5388 -1000 -625 -490 O
ATOM 1410 CB MET A 490 18.430 -8.271 29.478 1.00 28.98 C
ANISOU 1410 CB MET A 490 3907 2814 4292 -700 -576 -196 C
ATOM 1411 CG MET A 490 17.585 -9.546 29.363 1.00 27.76 C
ANISOU 1411 CG MET A 490 3744 2752 4051 -508 -547 -150 C
ATOM 1412 SD MET A 490 18.611 -10.900 28.816 1.00 28.03 S
ANISOU 1412 SD MET A 490 3589 3020 4039 -470 -572 -56 S
ATOM 1413 CE MET A 490 17.360 -12.196 28.583 1.00 24.44 C
ANISOU 1413 CE MET A 490 3174 2595 3516 -262 -517 -16 C
ATOM 1414 N ALA A 491 19.058 -5.166 28.940 1.00 33.08 N
ANISOU 1414 N ALA A 491 4568 2916 5086 -1042 -529 -226 N
ATOM 1415 CA ALA A 491 19.797 -3.916 29.179 1.00 32.62 C
ANISOU 1415 CA ALA A 491 4547 2712 5134 -1261 -551 -293 C
ATOM 1416 C ALA A 491 18.874 -2.826 29.705 1.00 41.81 C
ANISOU 1416 C ALA A 491 5919 3598 6367 -1253 -511 -403 C
ATOM 1417 O ALA A 491 19.248 -2.053 30.595 1.00 39.25 O
ANISOU 1417 O ALA A 491 5653 3204 6057 -1381 -536 -562 O
ATOM 1418 CB ALA A 491 20.485 -3.414 27.901 1.00 28.57 C
ANISOU 1418 CB ALA A 491 3952 2167 4736 -1372 -498 -128 C
ATOM 1419 N LYS A 492 17.673 -2.724 29.129 1.00 37.86 N
ANISOU 1419 N LYS A 492 5515 2973 5898 -1081 -422 -322 N
ATOM 1420 CA LYS A 492 16.701 -1.745 29.598 1.00 38.71 C
ANISOU 1420 CA LYS A 492 5786 2885 6037 -1003 -331 -414 C
ATOM 1421 C LYS A 492 16.326 -1.991 31.063 1.00 40.74 C
ANISOU 1421 C LYS A 492 6106 3187 6188 -963 -380 -620 C
ATOM 1422 O LYS A 492 16.111 -1.045 31.822 1.00 41.20 O
ANISOU 1422 O LYS A 492 6253 3121 6279 -993 -334 -765 O
ATOM 1423 CB LYS A 492 15.476 -1.805 28.687 1.00 41.87 C
ANISOU 1423 CB LYS A 492 6231 3226 6453 -800 -231 -269 C
ATOM 1424 CG LYS A 492 14.333 -0.919 29.076 1.00 49.74 C
ANISOU 1424 CG LYS A 492 7366 4058 7475 -680 -121 -335 C
ATOM 1425 CD LYS A 492 13.164 -1.125 28.117 1.00 48.74 C
ANISOU 1425 CD LYS A 492 7257 3934 7328 -480 -42 -173 C
ATOM 1426 CE LYS A 492 12.597 0.218 27.671 1.00 48.60 C
ANISOU 1426 CE LYS A 492 7392 3745 7329 -435 21 -106 C
ATOM 1427 NZ LYS A 492 11.190 0.067 27.219 1.00 57.27 N
ANISOU 1427 NZ LYS A 492 8508 4880 8374 -211 -35 -13 N
ATOM 1428 N ALA A 493 16.241 -3.258 31.475 1.00 38.74 N
ANISOU 1428 N ALA A 493 5799 3111 5808 -892 -469 -634 N
ATOM 1429 CA ALA A 493 15.995 -3.684 32.856 1.00 41.14 C
ANISOU 1429 CA ALA A 493 6144 3514 5971 -855 -525 -805 C
ATOM 1430 C ALA A 493 17.180 -3.440 33.789 1.00 46.19 C
ANISOU 1430 C ALA A 493 6741 4246 6564 -1053 -627 -949 C
ATOM 1431 O ALA A 493 17.070 -3.710 34.999 1.00 45.05 O
ANISOU 1431 O ALA A 493 6627 4204 6286 -1039 -678 -1095 O
ATOM 1432 CB ALA A 493 15.636 -5.175 32.886 1.00 37.99 C
ANISOU 1432 CB ALA A 493 5647 3352 5436 -698 -539 -725 C
ATOM 1433 N GLY A 494 18.308 -2.972 33.267 1.00 36.74 N
ANISOU 1433 N GLY A 494 5456 3046 5458 -1233 -653 -904 N
ATOM 1434 CA GLY A 494 19.423 -2.557 34.100 1.00 37.00 C
ANISOU 1434 CA GLY A 494 5428 3169 5463 -1428 -733 -1044 C
ATOM 1435 C GLY A 494 20.508 -3.601 34.292 1.00 48.36 C
ANISOU 1435 C GLY A 494 6693 4885 6797 -1508 -873 -1007 C
ATOM 1436 O GLY A 494 21.488 -3.335 35.008 1.00 39.59 O
ANISOU 1436 O GLY A 494 5499 3897 5647 -1660 -949 -1115 O
ATOM 1437 N LEU A 495 20.366 -4.776 33.681 1.00 38.59 N
ANISOU 1437 N LEU A 495 5346 3808 5508 -1350 -855 -845 N
ATOM 1438 CA LEU A 495 21.364 -5.826 33.827 1.00 37.65 C
ANISOU 1438 CA LEU A 495 5031 3980 5293 -1360 -942 -787 C
ATOM 1439 C LEU A 495 22.700 -5.382 33.233 1.00 40.71 C
ANISOU 1439 C LEU A 495 5271 4422 5775 -1563 -978 -733 C
ATOM 1440 O LEU A 495 22.750 -4.687 32.212 1.00 35.90 O
ANISOU 1440 O LEU A 495 4676 3658 5307 -1631 -903 -646 O
ATOM 1441 CB LEU A 495 20.868 -7.115 33.163 1.00 36.52 C
ANISOU 1441 CB LEU A 495 4823 3949 5103 -1142 -890 -628 C
ATOM 1442 CG LEU A 495 19.978 -8.027 34.015 1.00 36.29 C
ANISOU 1442 CG LEU A 495 4857 3998 4933 -964 -898 -666 C
ATOM 1443 CD1 LEU A 495 18.748 -7.272 34.461 1.00 38.32 C
ANISOU 1443 CD1 LEU A 495 5312 4049 5199 -916 -837 -774 C
ATOM 1444 CD2 LEU A 495 19.554 -9.297 33.233 1.00 30.91 C
ANISOU 1444 CD2 LEU A 495 4108 3405 4232 -776 -842 -509 C
ATOM 1445 N THR A 496 23.790 -5.748 33.907 1.00 40.59 N
ANISOU 1445 N THR A 496 5106 4639 5676 -1666 -1096 -780 N
ATOM 1446 CA THR A 496 25.113 -5.551 33.341 1.00 35.98 C
ANISOU 1446 CA THR A 496 4334 4172 5165 -1840 -1133 -710 C
ATOM 1447 C THR A 496 25.259 -6.405 32.098 1.00 39.26 C
ANISOU 1447 C THR A 496 4620 4684 5614 -1705 -1058 -503 C
ATOM 1448 O THR A 496 24.464 -7.306 31.838 1.00 33.64 O
ANISOU 1448 O THR A 496 3946 3988 4848 -1485 -1005 -432 O
ATOM 1449 CB THR A 496 26.203 -5.948 34.334 1.00 44.60 C
ANISOU 1449 CB THR A 496 5263 5543 6140 -1926 -1272 -786 C
ATOM 1450 OG1 THR A 496 26.262 -7.379 34.435 1.00 37.00 O
ANISOU 1450 OG1 THR A 496 4185 4814 5059 -1733 -1306 -684 O
ATOM 1451 CG2 THR A 496 25.913 -5.356 35.706 1.00 46.27 C
ANISOU 1451 CG2 THR A 496 5601 5707 6270 -1958 -1321 -999 C
ATOM 1452 N LEU A 497 26.306 -6.140 31.323 1.00 40.34 N
ANISOU 1452 N LEU A 497 4596 4895 5835 -1846 -1052 -413 N
ATOM 1453 CA LEU A 497 26.473 -6.917 30.096 1.00 42.52 C
ANISOU 1453 CA LEU A 497 4749 5271 6134 -1719 -970 -229 C
ATOM 1454 C LEU A 497 26.669 -8.405 30.397 1.00 36.53 C
ANISOU 1454 C LEU A 497 3868 4761 5250 -1525 -1014 -187 C
ATOM 1455 O LEU A 497 26.039 -9.272 29.774 1.00 36.26 O
ANISOU 1455 O LEU A 497 3855 4730 5192 -1323 -940 -98 O
ATOM 1456 CB LEU A 497 27.628 -6.353 29.278 1.00 38.47 C
ANISOU 1456 CB LEU A 497 4072 4822 5723 -1913 -952 -141 C
ATOM 1457 CG LEU A 497 27.655 -6.845 27.836 1.00 43.21 C
ANISOU 1457 CG LEU A 497 4586 5473 6360 -1802 -836 43 C
ATOM 1458 CD1 LEU A 497 26.693 -6.044 26.962 1.00 46.43 C
ANISOU 1458 CD1 LEU A 497 5170 5611 6860 -1792 -721 108 C
ATOM 1459 CD2 LEU A 497 29.087 -6.734 27.310 1.00 49.25 C
ANISOU 1459 CD2 LEU A 497 5108 6436 7170 -1963 -845 126 C
ATOM 1460 N GLN A 498 27.539 -8.712 31.352 1.00 37.26 N
ANISOU 1460 N GLN A 498 3833 5061 5263 -1586 -1136 -250 N
ATOM 1461 CA GLN A 498 27.729 -10.096 31.760 1.00 38.04 C
ANISOU 1461 CA GLN A 498 3826 5380 5247 -1395 -1183 -203 C
ATOM 1462 C GLN A 498 26.404 -10.756 32.139 1.00 35.60 C
ANISOU 1462 C GLN A 498 3698 4964 4865 -1186 -1146 -222 C
ATOM 1463 O GLN A 498 26.115 -11.876 31.701 1.00 30.00 O
ANISOU 1463 O GLN A 498 2960 4311 4128 -988 -1096 -127 O
ATOM 1464 CB GLN A 498 28.707 -10.145 32.933 1.00 40.49 C
ANISOU 1464 CB GLN A 498 4003 5915 5467 -1500 -1336 -281 C
ATOM 1465 CG GLN A 498 29.120 -11.548 33.264 1.00 43.46 C
ANISOU 1465 CG GLN A 498 4236 6534 5742 -1304 -1385 -197 C
ATOM 1466 CD GLN A 498 30.133 -11.571 34.365 1.00 46.79 C
ANISOU 1466 CD GLN A 498 4537 7163 6077 -1357 -1505 -260 C
ATOM 1467 OE1 GLN A 498 30.801 -12.581 34.604 1.00 47.47 O
ANISOU 1467 OE1 GLN A 498 4485 7446 6106 -1205 -1536 -179 O
ATOM 1468 NE2 GLN A 498 30.230 -10.461 35.082 1.00 49.23 N
ANISOU 1468 NE2 GLN A 498 4927 7395 6384 -1541 -1556 -409 N
ATOM 1469 N GLN A 499 25.577 -10.071 32.946 1.00 32.90 N
ANISOU 1469 N GLN A 499 3543 4464 4493 -1232 -1164 -352 N
ATOM 1470 CA GLN A 499 24.254 -10.579 33.308 1.00 38.87 C
ANISOU 1470 CA GLN A 499 4469 5116 5183 -1052 -1118 -372 C
ATOM 1471 C GLN A 499 23.336 -10.725 32.098 1.00 30.93 C
ANISOU 1471 C GLN A 499 3542 3951 4259 -932 -984 -276 C
ATOM 1472 O GLN A 499 22.518 -11.651 32.047 1.00 30.08 O
ANISOU 1472 O GLN A 499 3486 3840 4102 -749 -941 -232 O
ATOM 1473 CB GLN A 499 23.619 -9.655 34.352 1.00 33.82 C
ANISOU 1473 CB GLN A 499 4003 4343 4503 -1139 -1152 -540 C
ATOM 1474 CG GLN A 499 24.198 -9.808 35.725 1.00 38.39 C
ANISOU 1474 CG GLN A 499 4533 5110 4943 -1199 -1286 -643 C
ATOM 1475 CD GLN A 499 23.771 -8.682 36.659 1.00 46.80 C
ANISOU 1475 CD GLN A 499 5761 6043 5977 -1331 -1317 -840 C
ATOM 1476 OE1 GLN A 499 23.448 -7.569 36.222 1.00 42.60 O
ANISOU 1476 OE1 GLN A 499 5341 5279 5566 -1437 -1255 -901 O
ATOM 1477 NE2 GLN A 499 23.749 -8.974 37.950 1.00 47.93 N
ANISOU 1477 NE2 GLN A 499 5925 6330 5955 -1315 -1408 -938 N
ATOM 1478 N GLN A 500 23.459 -9.842 31.105 1.00 32.77 N
ANISOU 1478 N GLN A 500 3780 4059 4613 -1037 -920 -236 N
ATOM 1479 CA GLN A 500 22.642 -9.979 29.901 1.00 28.12 C
ANISOU 1479 CA GLN A 500 3248 3351 4083 -924 -801 -134 C
ATOM 1480 C GLN A 500 22.960 -11.276 29.150 1.00 29.90 C
ANISOU 1480 C GLN A 500 3340 3743 4279 -781 -768 -18 C
ATOM 1481 O GLN A 500 22.062 -12.052 28.819 1.00 26.92 O
ANISOU 1481 O GLN A 500 3023 3336 3870 -616 -711 19 O
ATOM 1482 CB GLN A 500 22.871 -8.771 28.990 1.00 26.21 C
ANISOU 1482 CB GLN A 500 3021 2969 3969 -1074 -743 -90 C
ATOM 1483 CG GLN A 500 22.286 -7.468 29.476 1.00 31.60 C
ANISOU 1483 CG GLN A 500 3879 3416 4714 -1179 -738 -193 C
ATOM 1484 CD GLN A 500 22.739 -6.316 28.605 1.00 35.69 C
ANISOU 1484 CD GLN A 500 4391 3801 5369 -1346 -687 -128 C
ATOM 1485 OE1 GLN A 500 22.842 -6.457 27.389 1.00 31.44 O
ANISOU 1485 OE1 GLN A 500 3786 3288 4874 -1313 -612 18 O
ATOM 1486 NE2 GLN A 500 23.013 -5.173 29.223 1.00 35.89 N
ANISOU 1486 NE2 GLN A 500 4492 3685 5460 -1531 -724 -239 N
ATOM 1487 N HIS A 501 24.243 -11.526 28.877 1.00 26.70 N
ANISOU 1487 N HIS A 501 2746 3514 3884 -843 -801 34 N
ATOM 1488 CA HIS A 501 24.651 -12.751 28.199 1.00 28.40 C
ANISOU 1488 CA HIS A 501 2828 3887 4075 -700 -765 129 C
ATOM 1489 C HIS A 501 24.220 -13.973 28.990 1.00 24.43 C
ANISOU 1489 C HIS A 501 2356 3446 3481 -524 -801 110 C
ATOM 1490 O HIS A 501 23.715 -14.941 28.410 1.00 26.50 O
ANISOU 1490 O HIS A 501 2633 3706 3731 -365 -734 163 O
ATOM 1491 CB HIS A 501 26.164 -12.762 28.029 1.00 27.90 C
ANISOU 1491 CB HIS A 501 2543 4024 4032 -796 -807 173 C
ATOM 1492 CG HIS A 501 26.674 -11.709 27.105 1.00 44.89 C
ANISOU 1492 CG HIS A 501 4642 6137 6278 -967 -755 222 C
ATOM 1493 ND1 HIS A 501 25.885 -11.127 26.130 1.00 39.03 N
ANISOU 1493 ND1 HIS A 501 4015 5222 5592 -972 -654 271 N
ATOM 1494 CD2 HIS A 501 27.864 -11.060 27.069 1.00 41.38 C
ANISOU 1494 CD2 HIS A 501 4043 5797 5881 -1154 -793 236 C
ATOM 1495 CE1 HIS A 501 26.591 -10.214 25.485 1.00 41.76 C
ANISOU 1495 CE1 HIS A 501 4284 5566 6016 -1144 -623 327 C
ATOM 1496 NE2 HIS A 501 27.790 -10.143 26.046 1.00 38.03 N
ANISOU 1496 NE2 HIS A 501 3648 5255 5545 -1267 -705 302 N
ATOM 1497 N GLN A 502 24.412 -13.931 30.321 1.00 28.47 N
ANISOU 1497 N GLN A 502 2879 4015 3924 -561 -904 35 N
ATOM 1498 CA GLN A 502 24.139 -15.093 31.156 1.00 27.08 C
ANISOU 1498 CA GLN A 502 2718 3918 3654 -404 -944 41 C
ATOM 1499 C GLN A 502 22.663 -15.417 31.154 1.00 26.08 C
ANISOU 1499 C GLN A 502 2772 3630 3507 -287 -875 26 C
ATOM 1500 O GLN A 502 22.288 -16.598 31.074 1.00 22.23 O
ANISOU 1500 O GLN A 502 2291 3165 2991 -127 -842 80 O
ATOM 1501 CB GLN A 502 24.598 -14.868 32.581 1.00 23.34 C
ANISOU 1501 CB GLN A 502 2225 3553 3090 -478 -1071 -34 C
ATOM 1502 CG GLN A 502 26.160 -14.902 32.747 1.00 28.47 C
ANISOU 1502 CG GLN A 502 2650 4433 3735 -561 -1162 -3 C
ATOM 1503 CD GLN A 502 26.614 -14.598 34.157 1.00 30.23 C
ANISOU 1503 CD GLN A 502 2848 4786 3852 -655 -1301 -87 C
ATOM 1504 OE1 GLN A 502 25.800 -14.416 35.064 1.00 29.81 O
ANISOU 1504 OE1 GLN A 502 2948 4660 3717 -649 -1327 -170 O
ATOM 1505 NE2 GLN A 502 27.931 -14.537 34.352 1.00 35.41 N
ANISOU 1505 NE2 GLN A 502 3300 5658 4498 -744 -1392 -68 N
ATOM 1506 N ARG A 503 21.817 -14.372 31.252 1.00 20.93 N
ANISOU 1506 N ARG A 503 2264 2810 2876 -367 -850 -47 N
ATOM 1507 CA ARG A 503 20.367 -14.581 31.255 1.00 20.32 C
ANISOU 1507 CA ARG A 503 2344 2593 2781 -262 -782 -61 C
ATOM 1508 C ARG A 503 19.879 -15.052 29.886 1.00 21.23 C
ANISOU 1508 C ARG A 503 2454 2656 2956 -173 -681 22 C
ATOM 1509 O ARG A 503 19.022 -15.941 29.797 1.00 19.05 O
ANISOU 1509 O ARG A 503 2233 2354 2651 -45 -636 44 O
ATOM 1510 CB ARG A 503 19.634 -13.288 31.669 1.00 24.72 C
ANISOU 1510 CB ARG A 503 3046 2990 3356 -356 -775 -160 C
ATOM 1511 CG ARG A 503 18.109 -13.511 31.905 1.00 24.01 C
ANISOU 1511 CG ARG A 503 3104 2787 3232 -239 -713 -182 C
ATOM 1512 CD ARG A 503 17.384 -12.242 32.442 1.00 22.13 C
ANISOU 1512 CD ARG A 503 3009 2393 3006 -306 -701 -291 C
ATOM 1513 NE ARG A 503 15.930 -12.436 32.554 1.00 20.85 N
ANISOU 1513 NE ARG A 503 2961 2141 2818 -186 -631 -300 N
ATOM 1514 CZ ARG A 503 15.327 -12.874 33.665 1.00 22.46 C
ANISOU 1514 CZ ARG A 503 3228 2388 2918 -122 -645 -355 C
ATOM 1515 NH1 ARG A 503 16.055 -13.198 34.747 1.00 24.27 N
ANISOU 1515 NH1 ARG A 503 3421 2753 3049 -159 -733 -399 N
ATOM 1516 NH2 ARG A 503 14.006 -13.006 33.679 1.00 25.90 N
ANISOU 1516 NH2 ARG A 503 3750 2751 3339 -22 -573 -355 N
ATOM 1517 N LEU A 504 20.406 -14.474 28.800 1.00 19.60 N
ANISOU 1517 N LEU A 504 2181 2441 2826 -248 -642 67 N
ATOM 1518 CA LEU A 504 20.057 -14.980 27.470 1.00 24.84 C
ANISOU 1518 CA LEU A 504 2823 3095 3521 -164 -551 143 C
ATOM 1519 C LEU A 504 20.309 -16.485 27.388 1.00 17.98 C
ANISOU 1519 C LEU A 504 1880 2339 2612 -24 -544 179 C
ATOM 1520 O LEU A 504 19.437 -17.263 26.979 1.00 16.81 O
ANISOU 1520 O LEU A 504 1790 2147 2449 86 -487 190 O
ATOM 1521 CB LEU A 504 20.856 -14.228 26.393 1.00 18.84 C
ANISOU 1521 CB LEU A 504 1971 2360 2829 -269 -516 202 C
ATOM 1522 CG LEU A 504 20.666 -14.666 24.947 1.00 20.71 C
ANISOU 1522 CG LEU A 504 2168 2624 3077 -198 -423 280 C
ATOM 1523 CD1 LEU A 504 19.214 -14.426 24.536 1.00 16.51 C
ANISOU 1523 CD1 LEU A 504 1777 1955 2542 -142 -368 281 C
ATOM 1524 CD2 LEU A 504 21.650 -13.945 24.028 1.00 22.04 C
ANISOU 1524 CD2 LEU A 504 2223 2853 3296 -313 -392 350 C
ATOM 1525 N ALA A 505 21.490 -16.903 27.801 1.00 17.15 N
ANISOU 1525 N ALA A 505 1646 2375 2495 -29 -601 194 N
ATOM 1526 CA ALA A 505 21.866 -18.314 27.780 1.00 18.99 C
ANISOU 1526 CA ALA A 505 1805 2706 2705 116 -594 235 C
ATOM 1527 C ALA A 505 20.935 -19.165 28.639 1.00 20.63 C
ANISOU 1527 C ALA A 505 2126 2853 2861 224 -604 218 C
ATOM 1528 O ALA A 505 20.498 -20.250 28.198 1.00 17.02 O
ANISOU 1528 O ALA A 505 1691 2368 2409 347 -546 243 O
ATOM 1529 CB ALA A 505 23.304 -18.463 28.265 1.00 18.53 C
ANISOU 1529 CB ALA A 505 1579 2821 2640 92 -669 261 C
ATOM 1530 N GLN A 506 20.626 -18.696 29.868 1.00 16.53 N
ANISOU 1530 N GLN A 506 1680 2314 2288 174 -673 172 N
ATOM 1531 CA GLN A 506 19.752 -19.461 30.762 1.00 19.40 C
ANISOU 1531 CA GLN A 506 2145 2636 2589 267 -679 168 C
ATOM 1532 C GLN A 506 18.359 -19.636 30.134 1.00 21.01 C
ANISOU 1532 C GLN A 506 2469 2701 2815 313 -588 157 C
ATOM 1533 O GLN A 506 17.765 -20.740 30.170 1.00 17.51 O
ANISOU 1533 O GLN A 506 2066 2227 2360 418 -550 186 O
ATOM 1534 CB GLN A 506 19.656 -18.765 32.154 1.00 17.59 C
ANISOU 1534 CB GLN A 506 1974 2429 2280 191 -762 106 C
ATOM 1535 CG GLN A 506 20.914 -18.761 33.039 1.00 23.55 C
ANISOU 1535 CG GLN A 506 2613 3355 2980 151 -873 113 C
ATOM 1536 CD GLN A 506 20.934 -17.552 34.043 1.00 33.97 C
ANISOU 1536 CD GLN A 506 3986 4685 4238 8 -950 8 C
ATOM 1537 OE1 GLN A 506 19.949 -16.810 34.161 1.00 30.11 O
ANISOU 1537 OE1 GLN A 506 3631 4061 3747 -36 -912 -67 O
ATOM 1538 NE2 GLN A 506 22.046 -17.375 34.756 1.00 29.60 N
ANISOU 1538 NE2 GLN A 506 3321 4294 3630 -61 -1058 -4 N
ATOM 1539 N LEU A 507 17.838 -18.571 29.502 1.00 18.08 N
ANISOU 1539 N LEU A 507 2146 2245 2480 234 -551 123 N
ATOM 1540 CA LEU A 507 16.533 -18.657 28.868 1.00 17.04 C
ANISOU 1540 CA LEU A 507 2104 2008 2362 277 -474 118 C
ATOM 1541 C LEU A 507 16.571 -19.620 27.680 1.00 16.02 C
ANISOU 1541 C LEU A 507 1923 1899 2264 351 -411 160 C
ATOM 1542 O LEU A 507 15.625 -20.394 27.471 1.00 16.07 O
ANISOU 1542 O LEU A 507 1986 1857 2262 419 -364 159 O
ATOM 1543 CB LEU A 507 16.053 -17.269 28.411 1.00 13.45 C
ANISOU 1543 CB LEU A 507 1702 1464 1943 192 -451 92 C
ATOM 1544 CG LEU A 507 15.713 -16.336 29.615 1.00 16.74 C
ANISOU 1544 CG LEU A 507 2207 1824 2328 133 -495 21 C
ATOM 1545 CD1 LEU A 507 15.116 -14.986 29.171 1.00 18.50 C
ANISOU 1545 CD1 LEU A 507 2502 1922 2606 72 -459 -3 C
ATOM 1546 CD2 LEU A 507 14.753 -17.060 30.600 1.00 23.58 C
ANISOU 1546 CD2 LEU A 507 3153 2685 3123 214 -492 -2 C
ATOM 1547 N LEU A 508 17.613 -19.548 26.856 1.00 18.76 N
ANISOU 1547 N LEU A 508 2162 2320 2646 331 -403 189 N
ATOM 1548 CA LEU A 508 17.609 -20.400 25.669 1.00 16.51 C
ANISOU 1548 CA LEU A 508 1836 2059 2379 402 -333 208 C
ATOM 1549 C LEU A 508 17.836 -21.861 26.037 1.00 16.18 C
ANISOU 1549 C LEU A 508 1778 2036 2332 517 -330 216 C
ATOM 1550 O LEU A 508 17.291 -22.743 25.360 1.00 20.43 O
ANISOU 1550 O LEU A 508 2345 2536 2879 585 -268 202 O
ATOM 1551 CB LEU A 508 18.638 -19.939 24.640 1.00 16.87 C
ANISOU 1551 CB LEU A 508 1765 2192 2452 356 -309 239 C
ATOM 1552 CG LEU A 508 18.431 -18.544 24.055 1.00 17.82 C
ANISOU 1552 CG LEU A 508 1903 2276 2590 245 -295 256 C
ATOM 1553 CD1 LEU A 508 19.561 -18.254 23.073 1.00 19.90 C
ANISOU 1553 CD1 LEU A 508 2037 2649 2876 200 -264 304 C
ATOM 1554 CD2 LEU A 508 17.058 -18.449 23.416 1.00 18.37 C
ANISOU 1554 CD2 LEU A 508 2071 2265 2646 271 -243 249 C
ATOM 1555 N LEU A 509 18.595 -22.136 27.104 1.00 16.99 N
ANISOU 1555 N LEU A 509 1839 2194 2421 540 -396 239 N
ATOM 1556 CA LEU A 509 18.750 -23.528 27.546 1.00 20.39 C
ANISOU 1556 CA LEU A 509 2269 2624 2855 664 -391 269 C
ATOM 1557 C LEU A 509 17.431 -24.120 28.047 1.00 19.14 C
ANISOU 1557 C LEU A 509 2244 2351 2677 697 -367 259 C
ATOM 1558 O LEU A 509 17.200 -25.322 27.903 1.00 20.12 O
ANISOU 1558 O LEU A 509 2397 2422 2827 788 -322 273 O
ATOM 1559 CB LEU A 509 19.827 -23.660 28.614 1.00 18.31 C
ANISOU 1559 CB LEU A 509 1924 2466 2568 689 -476 316 C
ATOM 1560 CG LEU A 509 21.237 -23.425 28.071 1.00 19.17 C
ANISOU 1560 CG LEU A 509 1868 2709 2706 681 -491 339 C
ATOM 1561 CD1 LEU A 509 22.275 -23.372 29.208 1.00 25.52 C
ANISOU 1561 CD1 LEU A 509 2574 3648 3474 683 -595 383 C
ATOM 1562 CD2 LEU A 509 21.662 -24.461 26.972 1.00 22.18 C
ANISOU 1562 CD2 LEU A 509 2185 3100 3141 801 -406 351 C
ATOM 1563 N ILE A 510 16.540 -23.290 28.591 1.00 20.51 N
ANISOU 1563 N ILE A 510 2501 2482 2812 623 -385 231 N
ATOM 1564 CA ILE A 510 15.211 -23.754 28.973 1.00 19.20 C
ANISOU 1564 CA ILE A 510 2444 2224 2625 643 -351 222 C
ATOM 1565 C ILE A 510 14.450 -24.245 27.748 1.00 20.69 C
ANISOU 1565 C ILE A 510 2656 2351 2854 658 -271 193 C
ATOM 1566 O ILE A 510 13.720 -25.245 27.828 1.00 15.26 O
ANISOU 1566 O ILE A 510 2025 1596 2176 699 -231 196 O
ATOM 1567 CB ILE A 510 14.475 -22.619 29.730 1.00 18.82 C
ANISOU 1567 CB ILE A 510 2465 2160 2527 567 -379 188 C
ATOM 1568 CG1 ILE A 510 15.173 -22.363 31.061 1.00 22.86 C
ANISOU 1568 CG1 ILE A 510 2963 2744 2978 555 -461 201 C
ATOM 1569 CG2 ILE A 510 12.992 -22.992 29.967 1.00 17.67 C
ANISOU 1569 CG2 ILE A 510 2414 1939 2362 582 -328 178 C
ATOM 1570 CD1 ILE A 510 14.510 -21.227 31.900 1.00 25.49 C
ANISOU 1570 CD1 ILE A 510 3373 3061 3253 484 -485 143 C
ATOM 1571 N LEU A 511 14.661 -23.609 26.582 1.00 16.33 N
ANISOU 1571 N LEU A 511 2056 1829 2321 619 -247 169 N
ATOM 1572 CA LEU A 511 14.055 -24.078 25.336 1.00 17.67 C
ANISOU 1572 CA LEU A 511 2233 1974 2506 631 -178 136 C
ATOM 1573 C LEU A 511 14.426 -25.529 25.021 1.00 17.20 C
ANISOU 1573 C LEU A 511 2162 1893 2482 716 -139 126 C
ATOM 1574 O LEU A 511 13.613 -26.233 24.424 1.00 18.31 O
ANISOU 1574 O LEU A 511 2347 1980 2632 724 -87 83 O
ATOM 1575 CB LEU A 511 14.470 -23.160 24.173 1.00 14.88 C
ANISOU 1575 CB LEU A 511 1815 1687 2153 583 -162 133 C
ATOM 1576 CG LEU A 511 13.901 -21.727 24.298 1.00 18.12 C
ANISOU 1576 CG LEU A 511 2257 2079 2547 505 -184 144 C
ATOM 1577 CD1 LEU A 511 14.077 -20.950 22.957 1.00 16.00 C
ANISOU 1577 CD1 LEU A 511 1939 1863 2277 464 -152 162 C
ATOM 1578 CD2 LEU A 511 12.439 -21.723 24.748 1.00 19.76 C
ANISOU 1578 CD2 LEU A 511 2555 2218 2734 505 -175 125 C
ATOM 1579 N SER A 512 15.638 -26.002 25.378 1.00 15.01 N
ANISOU 1579 N SER A 512 1821 1654 2228 782 -159 161 N
ATOM 1580 CA SER A 512 15.961 -27.439 25.218 1.00 15.14 C
ANISOU 1580 CA SER A 512 1837 1623 2293 853 -114 152 C
ATOM 1581 C SER A 512 15.092 -28.323 26.080 0.85 16.18 C
ANISOU 1581 C SER A 512 2057 1653 2439 832 -106 165 C
ATOM 1582 O SER A 512 14.720 -29.442 25.668 1.00 14.11 O
ANISOU 1582 O SER A 512 1831 1309 2220 846 -55 128 O
ATOM 1583 CB SER A 512 17.435 -27.803 25.500 1.00 22.87 C
ANISOU 1583 CB SER A 512 2720 2670 3300 925 -138 197 C
ATOM 1584 OG SER A 512 18.424 -27.267 24.592 1.00 29.19 O
ANISOU 1584 OG SER A 512 3405 3585 4100 952 -126 189 O
ATOM 1585 N HIS A 513 14.806 -27.870 27.298 1.00 14.80 N
ANISOU 1585 N HIS A 513 1914 1486 2224 805 -157 217 N
ATOM 1586 CA HIS A 513 13.896 -28.620 28.171 1.00 17.17 C
ANISOU 1586 CA HIS A 513 2290 1709 2523 784 -145 242 C
ATOM 1587 C HIS A 513 12.463 -28.628 27.633 1.00 16.81 C
ANISOU 1587 C HIS A 513 2305 1607 2475 721 -97 187 C
ATOM 1588 O HIS A 513 11.766 -29.647 27.750 1.00 16.61 O
ANISOU 1588 O HIS A 513 2329 1500 2481 712 -63 183 O
ATOM 1589 CB HIS A 513 13.912 -28.040 29.588 1.00 17.74 C
ANISOU 1589 CB HIS A 513 2382 1830 2529 779 -207 305 C
ATOM 1590 CG HIS A 513 13.073 -28.829 30.560 1.00 29.55 C
ANISOU 1590 CG HIS A 513 3949 3266 4012 771 -191 349 C
ATOM 1591 ND1 HIS A 513 11.979 -28.288 31.212 1.00 39.72 N
ANISOU 1591 ND1 HIS A 513 5300 4555 5238 727 -189 350 N
ATOM 1592 CD2 HIS A 513 13.171 -30.111 30.995 1.00 29.95 C
ANISOU 1592 CD2 HIS A 513 4022 3254 4103 808 -177 400 C
ATOM 1593 CE1 HIS A 513 11.447 -29.201 32.013 1.00 32.68 C
ANISOU 1593 CE1 HIS A 513 4459 3616 4343 734 -169 407 C
ATOM 1594 NE2 HIS A 513 12.150 -30.317 31.898 1.00 36.57 N
ANISOU 1594 NE2 HIS A 513 4932 4063 4900 780 -164 441 N
ATOM 1595 N ILE A 514 11.995 -27.505 27.076 1.00 13.64 N
ANISOU 1595 N ILE A 514 1900 1246 2036 680 -100 150 N
ATOM 1596 CA ILE A 514 10.663 -27.462 26.465 1.00 13.70 C
ANISOU 1596 CA ILE A 514 1948 1222 2036 632 -62 101 C
ATOM 1597 C ILE A 514 10.598 -28.400 25.248 1.00 17.61 C
ANISOU 1597 C ILE A 514 2442 1676 2573 649 -10 37 C
ATOM 1598 O ILE A 514 9.590 -29.106 25.051 1.00 13.05 O
ANISOU 1598 O ILE A 514 1913 1034 2012 621 27 2 O
ATOM 1599 CB ILE A 514 10.293 -26.006 26.138 1.00 12.76 C
ANISOU 1599 CB ILE A 514 1819 1157 1871 602 -84 88 C
ATOM 1600 CG1 ILE A 514 10.061 -25.259 27.479 1.00 16.82 C
ANISOU 1600 CG1 ILE A 514 2364 1682 2344 585 -123 126 C
ATOM 1601 CG2 ILE A 514 9.015 -25.925 25.264 1.00 14.88 C
ANISOU 1601 CG2 ILE A 514 2109 1417 2128 575 -49 43 C
ATOM 1602 CD1 ILE A 514 9.869 -23.783 27.294 1.00 16.90 C
ANISOU 1602 CD1 ILE A 514 2374 1720 2329 563 -149 112 C
ATOM 1603 N ARG A 515 11.676 -28.473 24.441 1.00 15.68 N
ANISOU 1603 N ARG A 515 2145 1467 2346 698 -1 14 N
ATOM 1604 CA ARG A 515 11.708 -29.469 23.366 1.00 14.42 C
ANISOU 1604 CA ARG A 515 1991 1266 2221 725 57 -64 C
ATOM 1605 C ARG A 515 11.549 -30.865 23.947 1.00 15.08 C
ANISOU 1605 C ARG A 515 2123 1237 2371 731 76 -63 C
ATOM 1606 O ARG A 515 10.768 -31.691 23.443 1.00 15.40 O
ANISOU 1606 O ARG A 515 2216 1199 2437 705 117 -134 O
ATOM 1607 CB ARG A 515 13.022 -29.409 22.568 1.00 14.45 C
ANISOU 1607 CB ARG A 515 1921 1339 2231 794 73 -83 C
ATOM 1608 CG ARG A 515 13.111 -30.444 21.333 1.00 20.18 C
ANISOU 1608 CG ARG A 515 2653 2035 2980 830 147 -193 C
ATOM 1609 CD ARG A 515 12.153 -30.119 20.212 1.00 23.34 C
ANISOU 1609 CD ARG A 515 3067 2486 3316 768 171 -281 C
ATOM 1610 NE ARG A 515 12.558 -28.796 19.717 1.00 31.54 N
ANISOU 1610 NE ARG A 515 4025 3673 4287 741 143 -238 N
ATOM 1611 CZ ARG A 515 13.497 -28.587 18.795 1.00 34.08 C
ANISOU 1611 CZ ARG A 515 4271 4098 4580 775 173 -258 C
ATOM 1612 NH1 ARG A 515 14.005 -29.607 18.113 1.00 34.04 N
ANISOU 1612 NH1 ARG A 515 4262 4080 4593 841 236 -346 N
ATOM 1613 NH2 ARG A 515 13.853 -27.348 18.465 1.00 30.88 N
ANISOU 1613 NH2 ARG A 515 3797 3811 4125 737 149 -196 N
ATOM 1614 N HIS A 516 12.311 -31.160 24.997 1.00 14.61 N
ANISOU 1614 N HIS A 516 2048 1167 2336 768 40 16 N
ATOM 1615 CA HIS A 516 12.260 -32.464 25.646 1.00 17.75 C
ANISOU 1615 CA HIS A 516 2495 1459 2790 791 45 41 C
ATOM 1616 C HIS A 516 10.826 -32.821 26.075 1.00 18.14 C
ANISOU 1616 C HIS A 516 2625 1433 2835 719 61 43 C
ATOM 1617 O HIS A 516 10.334 -33.931 25.799 1.00 16.19 O
ANISOU 1617 O HIS A 516 2439 1076 2637 707 98 2 O
ATOM 1618 CB HIS A 516 13.242 -32.432 26.835 1.00 17.31 C
ANISOU 1618 CB HIS A 516 2407 1439 2730 845 -7 146 C
ATOM 1619 CG HIS A 516 13.317 -33.712 27.617 1.00 19.51 C
ANISOU 1619 CG HIS A 516 2737 1619 3057 886 -7 201 C
ATOM 1620 ND1 HIS A 516 14.069 -34.796 27.225 1.00 29.01 N
ANISOU 1620 ND1 HIS A 516 3940 2753 4330 965 15 181 N
ATOM 1621 CD2 HIS A 516 12.648 -34.108 28.727 1.00 24.33 C
ANISOU 1621 CD2 HIS A 516 3410 2179 3654 862 -17 277 C
ATOM 1622 CE1 HIS A 516 13.908 -35.785 28.089 1.00 28.07 C
ANISOU 1622 CE1 HIS A 516 3882 2540 4243 989 12 252 C
ATOM 1623 NE2 HIS A 516 13.055 -35.390 29.016 1.00 25.51 N
ANISOU 1623 NE2 HIS A 516 3596 2231 3867 925 -6 316 N
ATOM 1624 N MET A 517 10.147 -31.882 26.759 1.00 13.71 N
ANISOU 1624 N MET A 517 2068 927 2213 672 38 90 N
ATOM 1625 CA MET A 517 8.772 -32.103 27.221 1.00 15.23 C
ANISOU 1625 CA MET A 517 2326 1067 2396 609 63 103 C
ATOM 1626 C MET A 517 7.815 -32.293 26.049 1.00 18.23 C
ANISOU 1626 C MET A 517 2731 1405 2789 556 113 3 C
ATOM 1627 O MET A 517 6.911 -33.137 26.099 1.00 16.23 O
ANISOU 1627 O MET A 517 2537 1057 2574 502 156 -12 O
ATOM 1628 CB MET A 517 8.279 -30.916 28.052 1.00 15.73 C
ANISOU 1628 CB MET A 517 2382 1212 2381 585 35 154 C
ATOM 1629 CG MET A 517 8.993 -30.744 29.316 1.00 17.03 C
ANISOU 1629 CG MET A 517 2540 1417 2514 623 -8 242 C
ATOM 1630 SD MET A 517 8.184 -29.512 30.380 1.00 19.33 S
ANISOU 1630 SD MET A 517 2857 1784 2705 599 -27 280 S
ATOM 1631 CE MET A 517 8.532 -27.969 29.561 1.00 15.48 C
ANISOU 1631 CE MET A 517 2314 1382 2186 589 -60 213 C
ATOM 1632 N SER A 518 7.967 -31.490 24.991 1.00 14.41 N
ANISOU 1632 N SER A 518 2206 997 2274 561 113 -64 N
ATOM 1633 CA SER A 518 7.142 -31.702 23.806 1.00 17.04 C
ANISOU 1633 CA SER A 518 2553 1316 2606 507 159 -172 C
ATOM 1634 C SER A 518 7.319 -33.113 23.243 1.00 20.40 C
ANISOU 1634 C SER A 518 3023 1625 3103 505 206 -253 C
ATOM 1635 O SER A 518 6.319 -33.771 22.911 1.00 16.60 O
ANISOU 1635 O SER A 518 2582 1073 2651 418 247 -323 O
ATOM 1636 CB SER A 518 7.460 -30.642 22.746 1.00 19.08 C
ANISOU 1636 CB SER A 518 2735 1719 2796 509 134 -215 C
ATOM 1637 OG SER A 518 6.807 -30.912 21.511 1.00 21.65 O
ANISOU 1637 OG SER A 518 3042 2088 3094 443 157 -324 O
ATOM 1638 N ASN A 519 8.571 -33.631 23.169 1.00 17.36 N
ANISOU 1638 N ASN A 519 2620 1229 2748 587 192 -248 N
ATOM 1639 CA ASN A 519 8.724 -34.980 22.616 1.00 16.34 C
ANISOU 1639 CA ASN A 519 2541 992 2675 594 229 -330 C
ATOM 1640 C ASN A 519 8.105 -36.047 23.516 1.00 18.11 C
ANISOU 1640 C ASN A 519 2842 1078 2963 550 240 -277 C
ATOM 1641 O ASN A 519 7.500 -36.999 23.028 1.00 18.85 O
ANISOU 1641 O ASN A 519 2994 1067 3100 488 282 -359 O
ATOM 1642 CB ASN A 519 10.192 -35.365 22.306 1.00 18.96 C
ANISOU 1642 CB ASN A 519 2837 1335 3033 707 224 -341 C
ATOM 1643 CG ASN A 519 10.771 -34.495 21.222 1.00 25.38 C
ANISOU 1643 CG ASN A 519 3575 2277 3790 740 237 -408 C
ATOM 1644 OD1 ASN A 519 10.274 -34.541 20.137 1.00 29.47 O
ANISOU 1644 OD1 ASN A 519 4112 2816 4268 701 281 -523 O
ATOM 1645 ND2 ASN A 519 11.982 -33.912 21.455 1.00 26.12 N
ANISOU 1645 ND2 ASN A 519 3582 2454 3889 813 215 -341 N
ATOM 1646 N LYS A 520 8.286 -35.937 24.822 1.00 17.31 N
ANISOU 1646 N LYS A 520 2737 974 2864 577 205 -142 N
ATOM 1647 CA LYS A 520 7.612 -36.846 25.753 1.00 19.03 C
ANISOU 1647 CA LYS A 520 3027 1074 3132 531 225 -69 C
ATOM 1648 C LYS A 520 6.106 -36.692 25.619 1.00 18.77 C
ANISOU 1648 C LYS A 520 3021 1019 3092 403 266 -104 C
ATOM 1649 O LYS A 520 5.368 -37.678 25.618 1.00 23.52 O
ANISOU 1649 O LYS A 520 3682 1500 3756 322 309 -127 O
ATOM 1650 CB LYS A 520 8.037 -36.617 27.193 1.00 25.45 C
ANISOU 1650 CB LYS A 520 3827 1920 3921 581 184 82 C
ATOM 1651 CG LYS A 520 9.533 -36.870 27.503 1.00 27.73 C
ANISOU 1651 CG LYS A 520 4080 2228 4228 699 144 131 C
ATOM 1652 CD LYS A 520 9.735 -38.387 27.281 1.00 36.34 C
ANISOU 1652 CD LYS A 520 5239 3156 5412 730 180 111 C
ATOM 1653 CE LYS A 520 11.116 -38.939 27.642 1.00 45.43 C
ANISOU 1653 CE LYS A 520 6368 4290 6602 857 154 169 C
ATOM 1654 NZ LYS A 520 11.218 -40.483 27.328 1.00 52.17 N
ANISOU 1654 NZ LYS A 520 7304 4956 7560 894 200 138 N
ATOM 1655 N GLY A 521 5.645 -35.471 25.463 1.00 19.06 N
ANISOU 1655 N GLY A 521 3011 1169 3063 377 256 -114 N
ATOM 1656 CA GLY A 521 4.211 -35.267 25.333 1.00 19.34 C
ANISOU 1656 CA GLY A 521 3056 1193 3099 256 301 -151 C
ATOM 1657 C GLY A 521 3.650 -35.941 24.097 1.00 23.54 C
ANISOU 1657 C GLY A 521 3599 1673 3672 157 340 -310 C
ATOM 1658 O GLY A 521 2.601 -36.585 24.159 1.00 26.14 O
ANISOU 1658 O GLY A 521 3951 1942 4040 30 373 -337 O
ATOM 1659 N AMET A 522 4.348 -35.819 22.961 0.62 21.65 N
ANISOU 1659 N AMET A 522 3332 1486 3407 202 329 -419 N
ATOM 1660 N BMET A 522 4.346 -35.789 22.960 0.38 21.71 N
ANISOU 1660 N BMET A 522 3339 1497 3414 203 329 -418 N
ATOM 1661 CA AMET A 522 3.854 -36.396 21.723 0.62 25.96 C
ANISOU 1661 CA AMET A 522 3881 2021 3961 106 357 -592 C
ATOM 1662 CA BMET A 522 3.919 -36.388 21.705 0.38 25.95 C
ANISOU 1662 CA BMET A 522 3879 2021 3958 112 356 -592 C
ATOM 1663 C AMET A 522 3.782 -37.917 21.816 0.62 27.04 C
ANISOU 1663 C AMET A 522 4098 1995 4180 64 383 -615 C
ATOM 1664 C BMET A 522 3.787 -37.900 21.834 0.38 27.06 C
ANISOU 1664 C BMET A 522 4100 1999 4182 66 382 -613 C
ATOM 1665 O AMET A 522 2.834 -38.528 21.309 0.62 30.80 O
ANISOU 1665 O AMET A 522 4590 2433 4680 -77 407 -721 O
ATOM 1666 O BMET A 522 2.804 -38.487 21.367 0.38 30.78 O
ANISOU 1666 O BMET A 522 4586 2432 4677 -78 406 -714 O
ATOM 1667 CB AMET A 522 4.746 -35.945 20.568 0.62 24.37 C
ANISOU 1667 CB AMET A 522 3634 1929 3697 182 345 -686 C
ATOM 1668 CB BMET A 522 4.925 -36.022 20.610 0.38 24.32 C
ANISOU 1668 CB BMET A 522 3633 1910 3696 200 345 -678 C
ATOM 1669 CG AMET A 522 4.429 -34.548 20.142 0.62 25.32 C
ANISOU 1669 CG AMET A 522 3649 2281 3691 169 285 -660 C
ATOM 1670 CG BMET A 522 4.278 -35.775 19.282 0.38 26.91 C
ANISOU 1670 CG BMET A 522 3905 2380 3939 103 335 -826 C
ATOM 1671 SD AMET A 522 5.305 -34.078 18.645 0.62 34.11 S
ANISOU 1671 SD AMET A 522 4704 3541 4715 227 281 -765 S
ATOM 1672 SD BMET A 522 3.339 -34.239 19.333 0.38 24.83 S
ANISOU 1672 SD BMET A 522 3527 2358 3551 53 263 -738 S
ATOM 1673 CE AMET A 522 4.690 -32.415 18.403 0.62 30.99 C
ANISOU 1673 CE AMET A 522 4200 3382 4191 202 212 -682 C
ATOM 1674 CE BMET A 522 4.574 -33.088 18.733 0.38 28.74 C
ANISOU 1674 CE BMET A 522 3960 2998 3963 183 234 -701 C
ATOM 1675 N GLU A 523 4.780 -38.544 22.459 1.00 25.96 N
ANISOU 1675 N GLU A 523 4006 1770 4089 181 373 -521 N
ATOM 1676 CA GLU A 523 4.713 -39.982 22.732 1.00 30.89 C
ANISOU 1676 CA GLU A 523 4713 2217 4806 156 400 -518 C
ATOM 1677 C GLU A 523 3.458 -40.303 23.526 1.00 34.17 C
ANISOU 1677 C GLU A 523 5156 2562 5265 19 425 -453 C
ATOM 1678 O GLU A 523 2.734 -41.256 23.235 1.00 30.07 O
ANISOU 1678 O GLU A 523 4683 1934 4808 -100 457 -525 O
ATOM 1679 CB GLU A 523 5.931 -40.418 23.566 1.00 27.52 C
ANISOU 1679 CB GLU A 523 4310 1729 4416 308 378 -394 C
ATOM 1680 CG GLU A 523 7.235 -40.509 22.884 1.00 33.71 C
ANISOU 1680 CG GLU A 523 5076 2540 5191 442 365 -451 C
ATOM 1681 CD GLU A 523 8.229 -41.305 23.748 1.00 47.28 C
ANISOU 1681 CD GLU A 523 6826 4160 6978 564 352 -340 C
ATOM 1682 OE1 GLU A 523 8.968 -40.701 24.574 1.00 40.38 O
ANISOU 1682 OE1 GLU A 523 5896 3372 6073 651 308 -218 O
ATOM 1683 OE2 GLU A 523 8.251 -42.548 23.602 1.00 40.39 O
ANISOU 1683 OE2 GLU A 523 6033 3123 6192 566 385 -378 O
ATOM 1684 N HIS A 524 3.212 -39.520 24.572 1.00 26.93 N
ANISOU 1684 N HIS A 524 4208 1710 4314 33 413 -315 N
ATOM 1685 CA HIS A 524 2.052 -39.751 25.408 1.00 34.32 C
ANISOU 1685 CA HIS A 524 5162 2598 5281 -90 448 -235 C
ATOM 1686 C HIS A 524 0.775 -39.589 24.593 1.00 34.58 C
ANISOU 1686 C HIS A 524 5154 2675 5310 -270 474 -369 C
ATOM 1687 O HIS A 524 -0.079 -40.480 24.583 1.00 36.25 O
ANISOU 1687 O HIS A 524 5393 2798 5583 -412 507 -399 O
ATOM 1688 CB HIS A 524 2.118 -38.787 26.599 1.00 35.39 C
ANISOU 1688 CB HIS A 524 5267 2825 5354 -22 431 -75 C
ATOM 1689 CG HIS A 524 0.974 -38.889 27.550 1.00 38.37 C
ANISOU 1689 CG HIS A 524 5654 3180 5743 -133 476 27 C
ATOM 1690 ND1 HIS A 524 0.319 -37.767 28.015 1.00 34.33 N
ANISOU 1690 ND1 HIS A 524 5089 2795 5159 -156 483 80 N
ATOM 1691 CD2 HIS A 524 0.344 -39.955 28.101 1.00 40.62 C
ANISOU 1691 CD2 HIS A 524 5990 3349 6097 -229 519 88 C
ATOM 1692 CE1 HIS A 524 -0.647 -38.138 28.840 1.00 44.50 C
ANISOU 1692 CE1 HIS A 524 6383 4066 6460 -258 530 174 C
ATOM 1693 NE2 HIS A 524 -0.658 -39.459 28.905 1.00 42.20 N
ANISOU 1693 NE2 HIS A 524 6159 3613 6262 -312 558 184 N
ATOM 1694 N LEU A 525 0.685 -38.501 23.816 1.00 24.19 N
ANISOU 1694 N LEU A 525 3767 1506 3921 -271 454 -461 N
ATOM 1695 CA LEU A 525 -0.526 -38.228 23.046 1.00 30.58 C
ANISOU 1695 CA LEU A 525 4490 2453 4677 -432 438 -573 C
ATOM 1696 C LEU A 525 -0.768 -39.317 22.010 1.00 40.18 C
ANISOU 1696 C LEU A 525 5746 3571 5949 -551 462 -754 C
ATOM 1697 O LEU A 525 -1.922 -39.717 21.775 1.00 39.25 O
ANISOU 1697 O LEU A 525 5594 3475 5845 -735 471 -821 O
ATOM 1698 CB LEU A 525 -0.404 -36.869 22.361 1.00 28.87 C
ANISOU 1698 CB LEU A 525 4163 2485 4322 -364 369 -599 C
ATOM 1699 CG LEU A 525 -0.528 -35.649 23.263 1.00 28.22 C
ANISOU 1699 CG LEU A 525 4018 2539 4164 -284 335 -446 C
ATOM 1700 CD1 LEU A 525 -0.437 -34.332 22.436 1.00 26.63 C
ANISOU 1700 CD1 LEU A 525 3718 2556 3846 -226 273 -477 C
ATOM 1701 CD2 LEU A 525 -1.808 -35.686 24.115 1.00 24.95 C
ANISOU 1701 CD2 LEU A 525 3565 2163 3753 -392 357 -366 C
ATOM 1702 N TYR A 526 0.307 -39.824 21.393 1.00 34.37 N
ANISOU 1702 N TYR A 526 5062 2778 5219 -438 453 -813 N
ATOM 1703 CA TYR A 526 0.148 -40.928 20.452 1.00 40.17 C
ANISOU 1703 CA TYR A 526 5838 3442 5983 -521 461 -965 C
ATOM 1704 C TYR A 526 -0.320 -42.211 21.142 1.00 44.52 C
ANISOU 1704 C TYR A 526 6469 3796 6649 -604 495 -909 C
ATOM 1705 O TYR A 526 -1.038 -43.000 20.522 1.00 47.76 O
ANISOU 1705 O TYR A 526 6893 4167 7088 -751 502 -1032 O
ATOM 1706 CB TYR A 526 1.445 -41.184 19.695 1.00 33.15 C
ANISOU 1706 CB TYR A 526 4988 2531 5075 -370 456 -1035 C
ATOM 1707 CG TYR A 526 1.345 -42.276 18.647 1.00 45.92 C
ANISOU 1707 CG TYR A 526 6657 4079 6713 -441 469 -1208 C
ATOM 1708 CD1 TYR A 526 0.894 -41.978 17.364 1.00 52.12 C
ANISOU 1708 CD1 TYR A 526 7381 5026 7397 -532 449 -1383 C
ATOM 1709 CD2 TYR A 526 1.725 -43.593 18.924 1.00 48.18 C
ANISOU 1709 CD2 TYR A 526 7051 4146 7110 -411 499 -1198 C
ATOM 1710 CE1 TYR A 526 0.814 -42.960 16.386 1.00 50.65 C
ANISOU 1710 CE1 TYR A 526 7244 4787 7215 -596 459 -1550 C
ATOM 1711 CE2 TYR A 526 1.644 -44.589 17.948 1.00 53.96 C
ANISOU 1711 CE2 TYR A 526 7840 4798 7863 -473 514 -1371 C
ATOM 1712 CZ TYR A 526 1.191 -44.268 16.681 1.00 56.79 C
ANISOU 1712 CZ TYR A 526 8140 5322 8115 -567 495 -1550 C
ATOM 1713 OH TYR A 526 1.111 -45.261 15.715 1.00 60.01 O
ANISOU 1713 OH TYR A 526 8609 5659 8535 -630 509 -1728 O
ATOM 1714 N SER A 527 0.047 -42.443 22.414 1.00 46.11 N
ANISOU 1714 N SER A 527 6722 3887 6912 -520 512 -725 N
ATOM 1715 CA SER A 527 -0.443 -43.648 23.095 1.00 44.98 C
ANISOU 1715 CA SER A 527 6653 3562 6877 -607 546 -657 C
ATOM 1716 C SER A 527 -1.960 -43.646 23.293 1.00 58.88 C
ANISOU 1716 C SER A 527 8359 5368 8646 -825 565 -661 C
ATOM 1717 O SER A 527 -2.527 -44.694 23.634 1.00 56.49 O
ANISOU 1717 O SER A 527 8108 4924 8432 -936 593 -635 O
ATOM 1718 CB SER A 527 0.202 -43.824 24.470 1.00 44.63 C
ANISOU 1718 CB SER A 527 6659 3427 6871 -477 554 -444 C
ATOM 1719 OG SER A 527 -0.204 -42.793 25.361 1.00 41.82 O
ANISOU 1719 OG SER A 527 6241 3195 6454 -477 553 -313 O
ATOM 1720 N MET A 528 -2.620 -42.498 23.125 1.00 51.30 N
ANISOU 1720 N MET A 528 7289 4604 7598 -888 550 -684 N
ATOM 1721 CA MET A 528 -4.076 -42.418 23.224 1.00 48.93 C
ANISOU 1721 CA MET A 528 6905 4395 7293 -1099 561 -697 C
ATOM 1722 C MET A 528 -4.707 -41.823 21.959 1.00 48.91 C
ANISOU 1722 C MET A 528 6788 4599 7197 -1209 516 -883 C
ATOM 1723 O MET A 528 -5.628 -41.005 22.038 1.00 53.72 O
ANISOU 1723 O MET A 528 7273 5394 7744 -1309 503 -872 O
ATOM 1724 CB MET A 528 -4.462 -41.623 24.489 1.00 41.58 C
ANISOU 1724 CB MET A 528 5928 3530 6340 -1085 591 -509 C
ATOM 1725 CG MET A 528 -3.939 -40.212 24.608 1.00 42.50 C
ANISOU 1725 CG MET A 528 5994 3789 6365 -946 567 -468 C
ATOM 1726 SD MET A 528 -3.917 -39.795 26.354 1.00 74.65 S
ANISOU 1726 SD MET A 528 10079 7870 10416 -847 597 -208 S
ATOM 1727 CE MET A 528 -2.709 -38.495 26.338 1.00 47.40 C
ANISOU 1727 CE MET A 528 6606 4552 6852 -604 527 -176 C
ATOM 1728 N LEU A 536 -2.485 -33.611 10.560 1.00 46.79 N
ANISOU 1728 N LEU A 536 5710 6648 5420 -698 -25 -1567 N
ATOM 1729 CA LEU A 536 -2.260 -32.287 11.167 1.00 33.84 C
ANISOU 1729 CA LEU A 536 4025 5052 3783 -552 -43 -1333 C
ATOM 1730 C LEU A 536 -1.704 -31.334 10.071 1.00 37.90 C
ANISOU 1730 C LEU A 536 4479 5790 4133 -457 -71 -1287 C
ATOM 1731 O LEU A 536 -2.079 -30.150 10.002 1.00 37.71 O
ANISOU 1731 O LEU A 536 4363 5928 4039 -392 -119 -1125 O
ATOM 1732 CB LEU A 536 -1.308 -32.363 12.385 1.00 36.34 C
ANISOU 1732 CB LEU A 536 4452 5095 4259 -443 19 -1237 C
ATOM 1733 CG LEU A 536 -1.017 -31.008 13.033 1.00 35.35 C
ANISOU 1733 CG LEU A 536 4293 5000 4139 -307 2 -1022 C
ATOM 1734 CD1 LEU A 536 -2.310 -30.305 13.413 1.00 39.15 C
ANISOU 1734 CD1 LEU A 536 4671 5609 4596 -340 -48 -915 C
ATOM 1735 CD2 LEU A 536 -0.006 -31.023 14.234 1.00 31.70 C
ANISOU 1735 CD2 LEU A 536 3931 4302 3813 -203 51 -931 C
ATOM 1736 N SER A 537 -0.861 -31.881 9.208 1.00 40.10 N
ANISOU 1736 N SER A 537 4811 6072 4352 -447 -34 -1429 N
ATOM 1737 CA SER A 537 -0.319 -31.128 8.051 1.00 41.83 C
ANISOU 1737 CA SER A 537 4971 6524 4397 -379 -50 -1402 C
ATOM 1738 C SER A 537 -1.456 -30.491 7.257 1.00 38.64 C
ANISOU 1738 C SER A 537 4430 6428 3825 -438 -138 -1360 C
ATOM 1739 O SER A 537 -1.383 -29.317 6.999 1.00 35.07 O
ANISOU 1739 O SER A 537 3904 6136 3286 -345 -171 -1181 O
ATOM 1740 CB SER A 537 0.433 -32.048 7.156 1.00 39.05 C
ANISOU 1740 CB SER A 537 4686 6153 4000 -391 6 -1591 C
ATOM 1741 OG SER A 537 1.799 -32.025 7.465 1.00 62.57 O
ANISOU 1741 OG SER A 537 7758 8934 7081 -281 84 -1594 O
ATOM 1742 N ASP A 538 -2.479 -31.271 6.906 1.00 40.21 N
ANISOU 1742 N ASP A 538 4590 6679 4007 -580 -169 -1481 N
ATOM 1743 CA ASP A 538 -3.562 -30.729 6.082 1.00 37.59 C
ANISOU 1743 CA ASP A 538 4117 6626 3541 -620 -243 -1411 C
ATOM 1744 C ASP A 538 -4.378 -29.706 6.858 1.00 35.91 C
ANISOU 1744 C ASP A 538 3808 6495 3342 -578 -300 -1226 C
ATOM 1745 O ASP A 538 -4.784 -28.674 6.304 1.00 35.13 O
ANISOU 1745 O ASP A 538 3603 6606 3137 -506 -346 -1068 O
ATOM 1746 CB ASP A 538 -4.454 -31.852 5.551 1.00 49.90 C
ANISOU 1746 CB ASP A 538 5656 8208 5095 -783 -255 -1577 C
ATOM 1747 N LEU A 539 -4.612 -29.964 8.151 1.00 33.44 N
ANISOU 1747 N LEU A 539 3536 5987 3182 -604 -284 -1216 N
ATOM 1748 CA LEU A 539 -5.354 -29.015 8.970 1.00 36.10 C
ANISOU 1748 CA LEU A 539 3793 6348 3576 -535 -311 -1013 C
ATOM 1749 C LEU A 539 -4.636 -27.670 9.065 1.00 33.51 C
ANISOU 1749 C LEU A 539 3474 6020 3238 -350 -302 -806 C
ATOM 1750 O LEU A 539 -5.278 -26.612 9.003 1.00 33.10 O
ANISOU 1750 O LEU A 539 3320 6120 3136 -275 -347 -642 O
ATOM 1751 CB LEU A 539 -5.586 -29.615 10.363 1.00 32.11 C
ANISOU 1751 CB LEU A 539 3356 5581 3263 -579 -262 -1017 C
ATOM 1752 CG LEU A 539 -6.372 -28.789 11.360 1.00 40.64 C
ANISOU 1752 CG LEU A 539 4366 6663 4412 -515 -272 -838 C
ATOM 1753 CD1 LEU A 539 -7.806 -28.532 10.858 1.00 41.54 C
ANISOU 1753 CD1 LEU A 539 4297 7063 4423 -585 -348 -818 C
ATOM 1754 CD2 LEU A 539 -6.361 -29.431 12.767 1.00 42.35 C
ANISOU 1754 CD2 LEU A 539 4674 6611 4806 -549 -208 -840 C
ATOM 1755 N LEU A 540 -3.299 -27.683 9.248 1.00 35.10 N
ANISOU 1755 N LEU A 540 3796 6043 3499 -274 -240 -806 N
ATOM 1756 CA LEU A 540 -2.536 -26.426 9.332 1.00 27.63 C
ANISOU 1756 CA LEU A 540 2862 5083 2554 -123 -227 -618 C
ATOM 1757 C LEU A 540 -2.574 -25.662 8.006 1.00 31.69 C
ANISOU 1757 C LEU A 540 3287 5874 2880 -84 -271 -547 C
ATOM 1758 O LEU A 540 -2.773 -24.434 7.981 1.00 28.59 O
ANISOU 1758 O LEU A 540 2840 5558 2463 16 -295 -352 O
ATOM 1759 CB LEU A 540 -1.056 -26.726 9.721 1.00 27.69 C
ANISOU 1759 CB LEU A 540 2997 4871 2654 -70 -155 -651 C
ATOM 1760 CG LEU A 540 -0.832 -27.315 11.103 1.00 21.26 C
ANISOU 1760 CG LEU A 540 2276 3782 2020 -75 -111 -674 C
ATOM 1761 CD1 LEU A 540 0.645 -27.737 11.298 1.00 24.40 C
ANISOU 1761 CD1 LEU A 540 2778 4007 2487 -22 -48 -719 C
ATOM 1762 CD2 LEU A 540 -1.220 -26.263 12.132 1.00 23.34 C
ANISOU 1762 CD2 LEU A 540 2522 3985 2361 2 -124 -496 C
ATOM 1763 N LEU A 541 -2.376 -26.373 6.898 1.00 30.01 N
ANISOU 1763 N LEU A 541 3064 5810 2530 -159 -277 -702 N
ATOM 1764 CA LEU A 541 -2.513 -25.747 5.580 1.00 36.07 C
ANISOU 1764 CA LEU A 541 3742 6839 3122 -131 -309 -627 C
ATOM 1765 C LEU A 541 -3.869 -25.061 5.449 1.00 49.62 C
ANISOU 1765 C LEU A 541 5335 8706 4814 -121 -368 -490 C
ATOM 1766 O LEU A 541 -3.955 -23.881 5.072 1.00 40.88 O
ANISOU 1766 O LEU A 541 4175 7686 3669 -17 -376 -289 O
ATOM 1767 CB LEU A 541 -2.315 -26.787 4.472 1.00 38.34 C
ANISOU 1767 CB LEU A 541 4041 7198 3327 -226 -286 -822 C
ATOM 1768 N GLU A 542 -4.945 -25.767 5.808 1.00 39.05 N
ANISOU 1768 N GLU A 542 3949 7378 3511 -225 -399 -589 N
ATOM 1769 CA GLU A 542 -6.271 -25.174 5.664 1.00 39.43 C
ANISOU 1769 CA GLU A 542 3870 7581 3532 -211 -445 -467 C
ATOM 1770 C GLU A 542 -6.371 -23.863 6.431 1.00 39.57 C
ANISOU 1770 C GLU A 542 3873 7537 3625 -59 -444 -237 C
ATOM 1771 O GLU A 542 -6.848 -22.852 5.903 1.00 40.62 O
ANISOU 1771 O GLU A 542 3937 7784 3711 31 -453 -68 O
ATOM 1772 CB GLU A 542 -7.336 -26.180 6.108 1.00 38.89 C
ANISOU 1772 CB GLU A 542 3757 7510 3510 -356 -467 -609 C
ATOM 1773 CG GLU A 542 -8.744 -25.715 5.966 1.00 48.53 C
ANISOU 1773 CG GLU A 542 4840 8902 4698 -351 -508 -505 C
ATOM 1774 CD GLU A 542 -9.204 -25.746 4.542 1.00 56.21 C
ANISOU 1774 CD GLU A 542 5729 10112 5515 -389 -534 -524 C
ATOM 1775 OE1 GLU A 542 -8.870 -26.711 3.827 1.00 53.08 O
ANISOU 1775 OE1 GLU A 542 5369 9741 5058 -501 -529 -708 O
ATOM 1776 OE2 GLU A 542 -9.930 -24.817 4.146 1.00 65.22 O
ANISOU 1776 OE2 GLU A 542 6770 11412 6597 -303 -558 -360 O
ATOM 1777 N MET A 543 -5.900 -23.842 7.673 1.00 33.40 N
ANISOU 1777 N MET A 543 3164 6560 2968 -24 -428 -228 N
ATOM 1778 CA MET A 543 -6.065 -22.624 8.448 1.00 26.83 C
ANISOU 1778 CA MET A 543 2324 5645 2226 120 -420 -22 C
ATOM 1779 C MET A 543 -5.092 -21.546 7.989 1.00 33.45 C
ANISOU 1779 C MET A 543 3219 6443 3046 240 -389 131 C
ATOM 1780 O MET A 543 -5.390 -20.341 8.079 1.00 33.11 O
ANISOU 1780 O MET A 543 3162 6371 3048 355 -374 315 O
ATOM 1781 CB MET A 543 -5.810 -22.915 9.946 1.00 29.28 C
ANISOU 1781 CB MET A 543 2728 5681 2718 121 -371 -56 C
ATOM 1782 CG MET A 543 -6.932 -23.600 10.666 1.00 40.94 C
ANISOU 1782 CG MET A 543 4143 7159 4254 33 -380 -131 C
ATOM 1783 SD MET A 543 -6.386 -23.967 12.352 1.00 58.83 S
ANISOU 1783 SD MET A 543 6554 9074 6723 39 -296 -158 S
ATOM 1784 CE MET A 543 -5.704 -25.613 12.117 1.00 28.32 C
ANISOU 1784 CE MET A 543 2787 5102 2871 -121 -270 -386 C
ATOM 1785 N LEU A 544 -3.891 -21.968 7.587 1.00 30.95 N
ANISOU 1785 N LEU A 544 2978 6099 2682 212 -368 50 N
ATOM 1786 CA LEU A 544 -2.848 -21.033 7.171 1.00 30.50 C
ANISOU 1786 CA LEU A 544 2973 6002 2615 303 -330 189 C
ATOM 1787 C LEU A 544 -3.114 -20.503 5.766 1.00 36.04 C
ANISOU 1787 C LEU A 544 3601 6894 3197 315 -329 273 C
ATOM 1788 O LEU A 544 -2.840 -19.331 5.486 1.00 37.13 O
ANISOU 1788 O LEU A 544 3744 7009 3354 406 -305 456 O
ATOM 1789 CB LEU A 544 -1.476 -21.724 7.200 1.00 28.86 C
ANISOU 1789 CB LEU A 544 2868 5673 2424 263 -276 66 C
ATOM 1790 CG LEU A 544 -0.815 -21.908 8.544 1.00 31.27 C
ANISOU 1790 CG LEU A 544 3283 5672 2925 276 -222 35 C
ATOM 1791 CD1 LEU A 544 0.324 -22.963 8.447 1.00 26.96 C
ANISOU 1791 CD1 LEU A 544 2817 5031 2394 221 -169 -133 C
ATOM 1792 CD2 LEU A 544 -0.305 -20.540 9.007 1.00 24.27 C
ANISOU 1792 CD2 LEU A 544 2431 4668 2123 384 -201 235 C
ATOM 1793 N ASP A 545 -3.669 -21.355 4.889 1.00 32.02 N
ANISOU 1793 N ASP A 545 3026 6567 2572 218 -356 136 N
ATOM 1794 CA ASP A 545 -3.862 -21.038 3.472 1.00 33.53 C
ANISOU 1794 CA ASP A 545 3142 6971 2628 218 -361 189 C
ATOM 1795 C ASP A 545 -5.176 -20.290 3.327 1.00 36.69 C
ANISOU 1795 C ASP A 545 3442 7476 3021 268 -393 325 C
ATOM 1796 O ASP A 545 -6.179 -20.798 2.843 1.00 32.78 O
ANISOU 1796 O ASP A 545 2856 7150 2447 200 -432 252 O
ATOM 1797 CB ASP A 545 -3.809 -22.305 2.625 1.00 32.40 C
ANISOU 1797 CB ASP A 545 2982 6960 2370 93 -370 -33 C
ATOM 1798 CG ASP A 545 -3.894 -22.024 1.111 1.00 31.99 C
ANISOU 1798 CG ASP A 545 2850 7143 2160 93 -377 12 C
ATOM 1799 OD1 ASP A 545 -3.585 -20.867 0.694 1.00 30.11 O
ANISOU 1799 OD1 ASP A 545 2595 6939 1906 192 -359 215 O
ATOM 1800 OD2 ASP A 545 -4.203 -23.013 0.369 1.00 31.30 O
ANISOU 1800 OD2 ASP A 545 2727 7191 1973 -13 -395 -168 O
ATOM 1801 N ALA A 546 -5.162 -19.057 3.789 1.00 34.90 N
ANISOU 1801 N ALA A 546 3237 7137 2886 387 -371 523 N
ATOM 1802 CA ALA A 546 -6.404 -18.323 3.667 1.00 36.21 C
ANISOU 1802 CA ALA A 546 3315 7393 3051 449 -391 650 C
ATOM 1803 C ALA A 546 -6.528 -17.719 2.274 1.00 45.59 C
ANISOU 1803 C ALA A 546 4429 8784 4110 481 -396 763 C
ATOM 1804 O ALA A 546 -5.542 -17.587 1.541 1.00 39.88 O
ANISOU 1804 O ALA A 546 3737 8090 3326 478 -372 784 O
ATOM 1805 CB ALA A 546 -6.491 -17.237 4.738 1.00 32.27 C
ANISOU 1805 CB ALA A 546 2872 6676 2712 567 -361 800 C
ATOM 1806 N HIS A 547 -7.776 -17.398 1.883 1.00 36.54 N
ANISOU 1806 N HIS A 547 3174 7800 2910 508 -428 833 N
ATOM 1807 CA HIS A 547 -7.951 -16.577 0.692 1.00 39.75 C
ANISOU 1807 CA HIS A 547 3509 8381 3211 570 -431 987 C
ATOM 1808 C HIS A 547 -7.824 -15.099 1.082 1.00 45.16 C
ANISOU 1808 C HIS A 547 4243 8897 4017 715 -391 1211 C
ATOM 1809 O HIS A 547 -7.656 -14.753 2.260 1.00 37.87 O
ANISOU 1809 O HIS A 547 3405 7731 3251 761 -362 1229 O
ATOM 1810 CB HIS A 547 -9.272 -16.913 0.004 1.00 36.46 C
ANISOU 1810 CB HIS A 547 2949 8234 2669 533 -487 962 C
ATOM 1811 CG HIS A 547 -10.464 -16.767 0.906 1.00 49.97 C
ANISOU 1811 CG HIS A 547 4614 9908 4466 570 -504 987 C
ATOM 1812 ND1 HIS A 547 -10.703 -15.631 1.654 1.00 48.98 N
ANISOU 1812 ND1 HIS A 547 4523 9614 4474 707 -471 1154 N
ATOM 1813 CD2 HIS A 547 -11.495 -17.607 1.164 1.00 47.61 C
ANISOU 1813 CD2 HIS A 547 4233 9719 4138 485 -546 864 C
ATOM 1814 CE1 HIS A 547 -11.812 -15.791 2.354 1.00 47.98 C
ANISOU 1814 CE1 HIS A 547 4336 9502 4393 714 -491 1131 C
ATOM 1815 NE2 HIS A 547 -12.321 -16.975 2.062 1.00 44.76 N
ANISOU 1815 NE2 HIS A 547 3850 9269 3886 578 -537 964 N
ATOM 1816 N ARG A 548 -7.836 -14.224 0.075 1.00 41.54 N
ANISOU 1816 N ARG A 548 3739 8558 3486 782 -385 1376 N
ATOM 1817 CA ARG A 548 -7.697 -12.792 0.299 1.00 42.80 C
ANISOU 1817 CA ARG A 548 3949 8555 3759 912 -345 1589 C
ATOM 1818 C ARG A 548 -9.031 -12.087 0.267 1.00 49.78 C
ANISOU 1818 C ARG A 548 4745 9521 4648 1010 -364 1715 C
ATOM 1819 O ARG A 548 -9.074 -10.874 0.029 1.00 57.22 O
ANISOU 1819 O ARG A 548 5699 10406 5638 1123 -339 1908 O
ATOM 1820 CB ARG A 548 -6.754 -12.175 -0.735 1.00 48.64 C
ANISOU 1820 CB ARG A 548 4705 9343 4434 930 -318 1713 C
ATOM 1821 N LEU A 549 -10.126 -12.825 0.477 1.00 45.28 N
ANISOU 1821 N LEU A 549 4083 9090 4030 970 -409 1611 N
ATOM 1822 CA LEU A 549 -11.455 -12.326 0.116 1.00 50.40 C
ANISOU 1822 CA LEU A 549 4608 9915 4628 1049 -439 1724 C
ATOM 1823 C LEU A 549 -12.080 -11.531 1.249 1.00 60.18 C
ANISOU 1823 C LEU A 549 5880 10952 6032 1166 -410 1806 C
ATOM 1824 O LEU A 549 -12.103 -10.304 1.176 1.00 55.90 O
ANISOU 1824 O LEU A 549 5366 10315 5559 1296 -379 1987 O
ATOM 1825 CB LEU A 549 -12.389 -13.472 -0.319 1.00 47.13 C
ANISOU 1825 CB LEU A 549 4060 9779 4067 940 -503 1580 C
ATOM 1826 CG LEU A 549 -12.059 -14.108 -1.678 1.00 43.28 C
ANISOU 1826 CG LEU A 549 3507 9551 3385 842 -537 1515 C
ATOM 1827 CD1 LEU A 549 -12.998 -15.272 -1.956 1.00 44.37 C
ANISOU 1827 CD1 LEU A 549 3527 9928 3402 716 -600 1344 C
ATOM 1828 CD2 LEU A 549 -12.050 -13.065 -2.824 1.00 45.75 C
ANISOU 1828 CD2 LEU A 549 3764 10012 3608 943 -535 1730 C
TER 1829 LEU A 549
HETATM 1830 C1 RAL A 601 -3.501 -28.347 26.415 1.00 14.32 C
HETATM 1831 C2 RAL A 601 -3.569 -26.991 26.273 1.00 17.07 C
HETATM 1832 C3 RAL A 601 -2.475 -26.192 26.587 1.00 15.01 C
HETATM 1833 O3 RAL A 601 -2.602 -24.851 26.454 1.00 15.20 O
HETATM 1834 C4 RAL A 601 -1.298 -26.762 27.025 1.00 14.37 C
HETATM 1835 C5 RAL A 601 -1.219 -28.140 27.137 1.00 11.59 C
HETATM 1836 S6 RAL A 601 0.143 -29.081 27.660 1.00 16.96 S
HETATM 1837 C7 RAL A 601 -0.732 -30.565 27.496 1.00 16.07 C
HETATM 1838 C8 RAL A 601 -0.102 -31.848 27.852 1.00 27.02 C
HETATM 1839 C9 RAL A 601 0.545 -32.016 29.063 1.00 28.33 C
HETATM 1840 C10 RAL A 601 1.084 -33.234 29.433 1.00 30.53 C
HETATM 1841 C11 RAL A 601 0.979 -34.324 28.587 1.00 36.09 C
HETATM 1842 O11 RAL A 601 1.504 -35.520 28.952 1.00 48.24 O
HETATM 1843 C12 RAL A 601 0.342 -34.179 27.372 1.00 29.05 C
HETATM 1844 C13 RAL A 601 -0.216 -32.958 27.028 1.00 30.43 C
HETATM 1845 C14 RAL A 601 -2.321 -28.948 26.842 1.00 13.28 C
HETATM 1846 C15 RAL A 601 -1.991 -30.354 27.038 1.00 14.49 C
HETATM 1847 C16 RAL A 601 -2.891 -31.455 26.680 1.00 16.58 C
HETATM 1848 O16 RAL A 601 -3.389 -32.098 27.552 1.00 22.27 O
HETATM 1849 C17 RAL A 601 -3.171 -31.819 25.260 1.00 16.68 C
HETATM 1850 C18 RAL A 601 -4.214 -32.634 24.866 1.00 18.41 C
HETATM 1851 C19 RAL A 601 -4.449 -32.908 23.534 1.00 20.81 C
HETATM 1852 C20 RAL A 601 -3.626 -32.386 22.560 1.00 22.00 C
HETATM 1853 C21 RAL A 601 -2.580 -31.577 22.941 1.00 21.27 C
HETATM 1854 C22 RAL A 601 -2.382 -31.284 24.265 1.00 18.81 C
HETATM 1855 O23 RAL A 601 -3.793 -32.677 21.240 1.00 25.07 O
HETATM 1856 C24 RAL A 601 -5.129 -32.804 20.784 1.00 27.57 C
HETATM 1857 C25 RAL A 601 -5.099 -33.191 19.342 1.00 36.36 C
HETATM 1858 N26 RAL A 601 -5.085 -32.025 18.478 1.00 36.98 N
HETATM 1859 C27 RAL A 601 -4.692 -32.408 17.135 1.00 49.29 C
HETATM 1860 C28 RAL A 601 -4.642 -31.221 16.215 1.00 43.02 C
HETATM 1861 C29 RAL A 601 -3.681 -30.201 16.773 1.00 46.33 C
HETATM 1862 C30 RAL A 601 -4.117 -29.813 18.162 1.00 36.98 C
HETATM 1863 C31 RAL A 601 -4.176 -31.033 19.019 1.00 34.48 C
HETATM 1864 O HOH A 701 0.769 -30.159 41.976 1.00 38.22 O
HETATM 1865 O HOH A 702 4.681 -30.014 7.640 1.00 41.97 O
HETATM 1866 O HOH A 703 -11.412 -25.419 2.481 1.00 36.81 O
HETATM 1867 O HOH A 704 13.248 -9.608 38.931 1.00 45.47 O
HETATM 1868 O HOH A 705 22.264 -13.829 5.911 1.00 58.87 O
HETATM 1869 O HOH A 706 -0.020 -8.607 24.830 1.00 35.74 O
HETATM 1870 O HOH A 707 -11.530 -30.638 19.741 1.00 33.72 O
HETATM 1871 O HOH A 708 -6.555 -18.925 12.660 1.00 31.01 O
HETATM 1872 O HOH A 709 -2.776 -12.930 17.419 1.00 26.20 O
HETATM 1873 O HOH A 710 -14.885 -17.247 34.093 1.00 27.58 O
HETATM 1874 O HOH A 711 -3.160 -13.097 12.230 1.00 29.33 O
HETATM 1875 O HOH A 712 10.472 -38.934 23.613 1.00 37.70 O
HETATM 1876 O HOH A 713 -4.824 -39.098 41.402 1.00 47.18 O
HETATM 1877 O HOH A 714 9.643 -29.796 18.347 1.00 28.56 O
HETATM 1878 O HOH A 715 -13.751 -26.375 34.696 1.00 30.67 O
HETATM 1879 O HOH A 716 -15.478 -29.250 26.004 1.00 41.29 O
HETATM 1880 O HOH A 717 12.932 -26.005 21.581 1.00 25.46 O
HETATM 1881 O HOH A 718 -3.059 -20.210 23.462 1.00 23.32 O
HETATM 1882 O HOH A 719 21.523 -11.616 11.097 1.00 29.25 O
HETATM 1883 O HOH A 720 -11.941 -37.483 28.878 1.00 33.15 O
HETATM 1884 O HOH A 721 20.912 -15.213 17.069 1.00 22.37 O
HETATM 1885 O HOH A 722 5.945 -31.910 40.879 1.00 28.23 O
HETATM 1886 O HOH A 723 -14.597 -27.210 32.149 1.00 29.77 O
HETATM 1887 O HOH A 724 -0.076 -11.367 9.024 1.00 35.51 O
HETATM 1888 O HOH A 725 9.324 -24.752 14.338 1.00 15.93 O
HETATM 1889 O HOH A 726 1.634 -7.562 15.930 1.00 32.49 O
HETATM 1890 O HOH A 727 -4.934 -11.496 19.843 1.00 38.10 O
HETATM 1891 O HOH A 728 -15.136 -20.063 37.041 1.00 37.96 O
HETATM 1892 O HOH A 729 19.092 -23.916 9.735 1.00 39.80 O
HETATM 1893 O HOH A 730 3.485 -12.863 20.948 1.00 21.23 O
HETATM 1894 O HOH A 731 18.537 -22.079 32.327 1.00 27.03 O
HETATM 1895 O HOH A 732 -12.318 -33.219 23.324 1.00 28.83 O
HETATM 1896 O HOH A 733 20.117 -5.299 21.232 1.00 38.85 O
HETATM 1897 O HOH A 734 -8.781 -33.540 18.475 1.00 36.76 O
HETATM 1898 O HOH A 735 7.446 -9.823 37.840 1.00 39.26 O
HETATM 1899 O HOH A 736 -8.103 -26.712 15.791 1.00 31.20 O
HETATM 1900 O HOH A 737 21.642 -2.295 31.781 1.00 39.38 O
HETATM 1901 O HOH A 738 18.371 -24.735 23.731 1.00 23.83 O
HETATM 1902 O HOH A 739 19.249 -23.662 15.677 1.00 33.36 O
HETATM 1903 O HOH A 740 21.977 -12.622 34.481 1.00 28.44 O
HETATM 1904 O HOH A 741 1.120 -17.843 20.804 1.00 19.60 O
HETATM 1905 O HOH A 742 2.401 -15.703 3.221 1.00 40.59 O
HETATM 1906 O HOH A 743 11.370 -24.088 0.211 1.00 44.04 O
HETATM 1907 O HOH A 744 7.185 -3.555 27.124 1.00 44.29 O
HETATM 1908 O HOH A 745 5.191 -24.517 40.165 1.00 21.58 O
HETATM 1909 O HOH A 746 5.941 -39.891 27.064 1.00 34.10 O
HETATM 1910 O HOH A 747 4.271 -12.557 9.799 1.00 22.67 O
HETATM 1911 O HOH A 748 20.465 -20.908 3.983 1.00 36.37 O
HETATM 1912 O HOH A 749 4.889 -28.453 5.092 1.00 34.10 O
HETATM 1913 O HOH A 750 -0.266 -17.693 6.245 1.00 36.56 O
HETATM 1914 O HOH A 751 17.234 -16.206 18.365 1.00 22.78 O
HETATM 1915 O HOH A 752 18.423 -5.184 16.007 1.00 42.79 O
HETATM 1916 O HOH A 753 -6.110 -20.975 28.833 1.00 20.01 O
HETATM 1917 O HOH A 754 8.561 -24.404 0.453 1.00 31.01 O
HETATM 1918 O HOH A 755 -1.155 -22.479 25.625 1.00 15.71 O
HETATM 1919 O HOH A 756 9.034 -14.341 40.605 1.00 42.20 O
HETATM 1920 O HOH A 757 5.678 -2.911 15.852 1.00 35.09 O
HETATM 1921 O HOH A 758 10.020 -31.440 14.793 1.00 37.39 O
HETATM 1922 O HOH A 759 -6.628 -14.641 17.745 1.00 33.12 O
HETATM 1923 O HOH A 760 -6.454 -27.629 41.529 1.00 42.40 O
HETATM 1924 O HOH A 761 1.125 -16.637 36.237 1.00 29.40 O
HETATM 1925 O HOH A 762 13.893 -29.214 12.917 1.00 29.90 O
HETATM 1926 O HOH A 763 3.092 -23.674 38.284 1.00 16.36 O
HETATM 1927 O HOH A 764 12.783 -25.740 38.487 1.00 33.11 O
HETATM 1928 O HOH A 765 -5.157 -20.377 26.394 1.00 18.49 O
HETATM 1929 O HOH A 766 -1.428 -15.057 25.701 1.00 37.17 O
HETATM 1930 O HOH A 767 23.170 -14.547 35.901 1.00 32.80 O
HETATM 1931 O HOH A 768 8.105 -30.557 39.417 1.00 26.47 O
HETATM 1932 O HOH A 769 1.078 -35.208 44.330 1.00 48.50 O
HETATM 1933 O HOH A 770 0.556 -21.093 23.851 1.00 13.59 O
HETATM 1934 O HOH A 771 5.628 -9.366 32.875 1.00 35.12 O
HETATM 1935 O HOH A 772 19.796 -8.099 13.567 1.00 34.32 O
HETATM 1936 O HOH A 773 8.347 -32.305 19.659 1.00 27.72 O
HETATM 1937 O HOH A 774 -4.791 -16.957 37.698 1.00 38.19 O
HETATM 1938 O HOH A 775 0.903 -18.626 24.898 1.00 21.93 O
HETATM 1939 O AHOH A 776 -12.201 -27.502 27.339 0.59 18.67 O
HETATM 1940 O BHOH A 776 -14.326 -27.247 26.868 0.41 22.35 O
HETATM 1941 O HOH A 777 6.023 -29.071 19.376 1.00 15.68 O
HETATM 1942 O HOH A 778 6.578 -31.219 8.708 1.00 37.67 O
HETATM 1943 O HOH A 779 -11.948 -19.283 19.847 1.00 18.22 O
HETATM 1944 O HOH A 780 -9.217 -14.358 28.587 1.00 32.67 O
HETATM 1945 O HOH A 781 9.293 -35.756 35.644 1.00 33.38 O
HETATM 1946 O HOH A 782 5.626 -32.563 15.409 1.00 37.51 O
HETATM 1947 O HOH A 783 -11.779 -24.194 6.180 1.00 40.67 O
HETATM 1948 O HOH A 784 8.074 -1.767 22.919 1.00 38.08 O
HETATM 1949 O HOH A 785 16.870 -14.797 2.341 1.00 34.22 O
HETATM 1950 O HOH A 786 14.174 0.262 20.146 1.00 38.72 O
HETATM 1951 O HOH A 787 19.080 -9.902 11.686 1.00 34.20 O
HETATM 1952 O HOH A 788 14.545 -22.641 -5.853 1.00 37.88 O
HETATM 1953 O HOH A 789 13.412 -10.328 35.854 1.00 36.48 O
HETATM 1954 O HOH A 790 -3.389 -18.248 25.419 1.00 21.55 O
HETATM 1955 O HOH A 791 4.196 -16.868 0.999 1.00 40.94 O
HETATM 1956 O HOH A 792 7.825 -37.634 37.776 1.00 41.65 O
HETATM 1957 O HOH A 793 15.327 -8.631 31.533 1.00 35.22 O
HETATM 1958 O HOH A 794 -5.548 -18.953 22.442 1.00 25.09 O
HETATM 1959 O HOH A 795 -3.095 -19.864 20.819 1.00 20.83 O
HETATM 1960 O HOH A 796 -4.124 -15.009 18.061 1.00 23.87 O
HETATM 1961 O HOH A 797 -5.802 -44.366 35.010 1.00 47.55 O
HETATM 1962 O HOH A 798 10.515 -20.675 42.090 1.00 30.06 O
HETATM 1963 O HOH A 799 23.340 -4.624 25.219 1.00 35.65 O
HETATM 1964 O HOH A 800 2.962 -32.905 15.390 1.00 32.90 O
HETATM 1965 O HOH A 801 -9.773 -38.131 31.109 1.00 37.42 O
HETATM 1966 O HOH A 802 -10.820 -21.356 18.538 1.00 19.52 O
HETATM 1967 O HOH A 803 0.297 -40.286 35.165 1.00 38.67 O
HETATM 1968 O HOH A 804 2.818 -15.175 34.262 1.00 28.90 O
HETATM 1969 O HOH A 805 6.119 -11.839 35.293 1.00 29.12 O
HETATM 1970 O HOH A 806 10.641 3.823 12.860 1.00 51.49 O
HETATM 1971 O HOH A 807 21.997 -15.519 10.522 1.00 30.86 O
HETATM 1972 O HOH A 808 29.141 -6.640 32.664 1.00 38.69 O
HETATM 1973 O HOH A 809 11.650 2.432 18.296 1.00 45.00 O
HETATM 1974 O HOH A 810 -10.160 -25.160 38.121 1.00 26.98 O
HETATM 1975 O HOH A 811 13.236 -24.214 19.696 1.00 27.73 O
HETATM 1976 O HOH A 812 26.286 -12.661 37.389 1.00 44.67 O
HETATM 1977 O HOH A 813 -15.966 -21.717 27.894 1.00 19.13 O
HETATM 1978 O HOH A 814 -2.409 -15.199 36.616 1.00 44.44 O
HETATM 1979 O HOH A 815 4.371 -41.001 29.135 1.00 47.47 O
HETATM 1980 O HOH A 816 16.497 -17.870 -6.686 1.00 32.46 O
HETATM 1981 O HOH A 817 -0.841 -22.304 43.735 1.00 40.20 O
HETATM 1982 O HOH A 818 2.399 -34.291 13.072 1.00 38.25 O
HETATM 1983 O HOH A 819 1.715 -37.821 18.634 1.00 40.45 O
HETATM 1984 O HOH A 820 -22.111 -27.342 32.504 1.00 51.28 O
HETATM 1985 O HOH A 821 -15.846 -24.819 34.494 1.00 33.84 O
HETATM 1986 O HOH A 822 16.881 -24.543 -6.893 1.00 34.36 O
HETATM 1987 O HOH A 823 18.955 -13.887 35.188 1.00 28.82 O
HETATM 1988 O HOH A 824 -6.936 -36.218 21.969 1.00 42.20 O
HETATM 1989 O HOH A 825 -14.718 -34.163 28.329 1.00 34.91 O
HETATM 1990 O AHOH A 826 -9.635 -17.532 4.293 0.62 29.81 O
HETATM 1991 O BHOH A 826 -10.279 -15.653 5.195 0.38 27.24 O
HETATM 1992 O HOH A 827 -18.450 -22.573 27.942 1.00 33.92 O
HETATM 1993 O HOH A 828 6.305 -26.992 41.247 1.00 32.06 O
HETATM 1994 O HOH A 829 -6.562 -12.844 27.408 1.00 29.47 O
HETATM 1995 O AHOH A 830 20.425 -19.478 36.848 0.43 28.48 O
HETATM 1996 O BHOH A 830 22.867 -18.412 37.820 0.57 33.93 O
HETATM 1997 O HOH A 831 20.103 -17.475 13.615 1.00 32.39 O
HETATM 1998 O HOH A 832 -2.084 -16.280 34.488 1.00 39.26 O
HETATM 1999 O HOH A 833 10.692 -44.371 24.437 1.00 45.65 O
HETATM 2000 O HOH A 834 16.266 -12.153 4.546 1.00 42.47 O
HETATM 2001 O HOH A 835 15.974 -27.258 15.887 1.00 36.25 O
HETATM 2002 O HOH A 836 21.115 -15.496 8.419 1.00 37.81 O
HETATM 2003 O HOH A 837 -6.726 -24.627 1.705 1.00 44.98 O
HETATM 2004 O HOH A 838 1.118 -12.116 27.835 1.00 38.05 O
HETATM 2005 O HOH A 839 16.542 -33.645 8.794 1.00 42.20 O
HETATM 2006 O HOH A 840 5.576 -26.819 -1.813 1.00 40.37 O
HETATM 2007 O HOH A 841 0.472 -15.074 33.047 1.00 32.79 O
HETATM 2008 O HOH A 842 19.726 -19.077 15.112 1.00 32.31 O
HETATM 2009 O HOH A 843 6.548 -39.510 30.150 1.00 43.21 O
HETATM 2010 O HOH A 844 -5.050 -22.772 44.380 1.00 39.33 O
HETATM 2011 O HOH A 845 -14.982 -32.569 26.407 1.00 41.73 O
HETATM 2012 O HOH A 846 -0.724 -15.774 28.513 1.00 32.75 O
HETATM 2013 O HOH A 847 8.607 -28.492 40.527 1.00 38.37 O
HETATM 2014 O HOH A 848 21.296 -23.445 5.110 1.00 36.33 O
HETATM 2015 O HOH A 849 6.308 -39.385 19.302 1.00 37.19 O
HETATM 2016 O HOH A 850 30.683 -7.022 30.766 1.00 51.11 O
HETATM 2017 O HOH A 851 16.935 -0.584 19.292 1.00 52.35 O
HETATM 2018 O HOH A 852 23.337 -20.884 31.055 1.00 26.93 O
HETATM 2019 O HOH A 853 20.712 -20.682 6.781 1.00 31.58 O
HETATM 2020 O HOH A 854 -1.079 -17.669 26.271 1.00 29.74 O
HETATM 2021 O HOH A 855 -9.965 -37.376 24.596 1.00 37.96 O
HETATM 2022 O HOH A 856 10.744 -18.641 43.287 1.00 30.72 O
HETATM 2023 O HOH A 857 15.530 -9.202 34.629 1.00 37.14 O
HETATM 2024 O HOH A 858 -20.350 -31.912 31.223 1.00 50.14 O
HETATM 2025 O HOH A 859 21.175 -3.564 23.474 1.00 44.26 O
HETATM 2026 O HOH A 860 -3.844 -11.757 7.574 1.00 42.66 O
HETATM 2027 O HOH A 861 -0.888 -38.055 17.923 1.00 41.80 O
HETATM 2028 O HOH A 862 -11.303 -35.679 22.807 1.00 38.83 O
HETATM 2029 O AHOH A 863 -4.237 -14.908 39.985 0.54 36.60 O
HETATM 2030 O BHOH A 863 -2.973 -14.451 40.853 0.46 39.41 O
HETATM 2031 O HOH A 864 3.089 -9.797 32.249 1.00 36.73 O
HETATM 2032 O HOH A 865 -2.392 -11.423 10.059 1.00 28.63 O
HETATM 2033 O HOH A 866 18.497 -3.748 18.880 1.00 46.15 O
HETATM 2034 O HOH A 867 -0.957 -10.266 26.380 1.00 49.41 O
HETATM 2035 O HOH A 868 5.057 -3.882 13.586 1.00 45.82 O
HETATM 2036 O HOH A 869 -0.371 -20.333 21.154 1.00 16.33 O
HETATM 2037 O HOH A 870 19.184 -8.330 9.268 1.00 46.79 O
HETATM 2038 O HOH A 871 -7.800 -35.701 19.498 1.00 50.74 O
HETATM 2039 O HOH A 872 -6.635 -17.106 35.837 1.00 31.44 O
HETATM 2040 O HOH A 873 -3.626 -13.446 34.750 1.00 40.07 O
HETATM 2041 O HOH A 874 -1.347 -11.170 29.796 1.00 47.69 O
HETATM 2042 O HOH A 875 -23.807 -29.292 33.338 1.00 45.44 O
HETATM 2043 O HOH A 876 -18.857 -34.919 26.803 1.00 47.87 O
HETATM 2044 O HOH A 877 -2.210 -11.889 32.373 1.00 45.70 O
HETATM 2045 O HOH A 878 -1.451 -38.711 15.553 1.00 60.51 O
CONECT 1830 1831 1845
CONECT 1840 1839 1841
CONECT 1841 1840 1842 1843
CONECT 1843 1841 1844
CONECT 1844 1843 1838
CONECT 1845 1835 1830 1846
CONECT 1846 1837 1845 1847
CONECT 1847 1848 1849 1846
CONECT 1849 1854 1850 1847
CONECT 1850 1849 1851
CONECT 1851 1852 1850
CONECT 1831 1832 1830
CONECT 1852 1851 1853 1855
CONECT 1853 1854 1852
CONECT 1854 1849 1853
CONECT 1856 1857 1855
CONECT 1857 1858 1856
CONECT 1859 1858 1860
CONECT 1860 1861 1859
CONECT 1861 1860 1862
CONECT 1832 1831 1834 1833
CONECT 1862 1861 1863
CONECT 1863 1858 1862
CONECT 1834 1832 1835
CONECT 1835 1834 1845 1836
CONECT 1837 1836 1838 1846
CONECT 1838 1837 1839 1844
CONECT 1839 1840 1838
CONECT 1858 1857 1859 1863
CONECT 1842 1841
CONECT 1848 1847
CONECT 1855 1852 1856
CONECT 1833 1832
CONECT 1836 1837 1835
END
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elNémo
is maintained by Yves-Henri Sanejouand.
It was developed
by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.
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