HEADER MEMBRANE PROTEIN 08-FEB-17 5N2R
TITLE CRYSTAL STRUCTURE OF STABILIZED A2A ADENOSINE RECEPTOR A2AR-STAR2-BRIL
TITLE 2 IN COMPLEX WITH PSB36 AT 2.8A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE
COMPND 3 RECEPTOR A2A SOLUBLE CYTOCHROME B562 ADENOSINE RECEPTOR A2A,ADENOSINE
COMPND 4 RECEPTOR A2A;
COMPND 5 CHAIN: A;
COMPND 6 SYNONYM: CYTOCHROME B-562;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 562;
SOURCE 5 GENE: ADORA2A, ADORA2, CYBC, ADORA2A;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TNI PRO;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PFAST-BAC
KEYWDS G-PROTEIN-COUPLED RECEPTOR, INTEGRAL THERMOSTABILIZING MUTATIONS,
KEYWDS 2 MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.K.Y.CHENG,E.SEGALA,N.ROBERTSON,F.DEFLORIAN,A.S.DORE,J.C.ERREY,
AUTHOR 2 C.FIEZ-VANDAL,F.H.MARSHALL,R.M.COOKE
REVDAT 2 09-AUG-17 5N2R 1 JRNL
REVDAT 1 26-JUL-17 5N2R 0
JRNL AUTH R.K.Y.CHENG,E.SEGALA,N.ROBERTSON,F.DEFLORIAN,A.S.DORE,
JRNL AUTH 2 J.C.ERREY,C.FIEZ-VANDAL,F.H.MARSHALL,R.M.COOKE
JRNL TITL STRUCTURES OF HUMAN A1 AND A2A ADENOSINE RECEPTORS WITH
JRNL TITL 2 XANTHINES REVEAL DETERMINANTS OF SELECTIVITY.
JRNL REF STRUCTURE V. 25 1275 2017
JRNL REFN ISSN 1878-4186
JRNL PMID 28712806
JRNL DOI 10.1016/J.STR.2017.06.012
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 12814
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 658
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 38.3633 - 4.7855 1.00 2542 153 0.1869 0.2348
REMARK 3 2 4.7855 - 3.7995 1.00 2435 137 0.1525 0.1867
REMARK 3 3 3.7995 - 3.3195 1.00 2402 131 0.1958 0.2189
REMARK 3 4 3.3195 - 3.0161 1.00 2394 112 0.2319 0.3199
REMARK 3 5 3.0161 - 2.8000 1.00 2383 125 0.2423 0.2721
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.680
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 3542
REMARK 3 ANGLE : 0.501 4716
REMARK 3 CHIRALITY : 0.045 529
REMARK 3 PLANARITY : 0.004 561
REMARK 3 DIHEDRAL : 17.289 1170
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID -1 THROUGH 186 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8727 184.3023 20.9676
REMARK 3 T TENSOR
REMARK 3 T11: 0.1334 T22: 0.2010
REMARK 3 T33: 0.1389 T12: -0.0238
REMARK 3 T13: -0.0027 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 0.2086 L22: 0.1448
REMARK 3 L33: 1.0324 L12: 0.0351
REMARK 3 L13: -0.1185 L23: -0.2939
REMARK 3 S TENSOR
REMARK 3 S11: -0.0451 S12: 0.0118 S13: -0.0246
REMARK 3 S21: -0.0718 S22: 0.0211 S23: 0.0423
REMARK 3 S31: 0.0120 S32: 0.1588 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 187 THROUGH 1018 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8606 213.8854 19.8192
REMARK 3 T TENSOR
REMARK 3 T11: -0.0396 T22: -0.9905
REMARK 3 T33: 0.8868 T12: 0.4054
REMARK 3 T13: -0.2298 T23: 0.0861
REMARK 3 L TENSOR
REMARK 3 L11: -0.0984 L22: 0.0155
REMARK 3 L33: -0.1221 L12: -0.0104
REMARK 3 L13: 0.1450 L23: 0.0154
REMARK 3 S TENSOR
REMARK 3 S11: -0.2153 S12: -0.2522 S13: 0.5607
REMARK 3 S21: -0.1334 S22: 0.0030 S23: 0.2379
REMARK 3 S31: 0.1471 S32: 0.3389 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1019 THROUGH 1101 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6091 238.2556 22.1585
REMARK 3 T TENSOR
REMARK 3 T11: 0.7388 T22: 0.3068
REMARK 3 T33: 1.6020 T12: 0.2060
REMARK 3 T13: 0.3492 T23: 0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 0.0132 L22: 0.0327
REMARK 3 L33: -0.0076 L12: -0.0066
REMARK 3 L13: 0.0101 L23: 0.0436
REMARK 3 S TENSOR
REMARK 3 S11: -0.0058 S12: -0.5078 S13: -0.0638
REMARK 3 S21: -0.3029 S22: 0.3941 S23: 0.1232
REMARK 3 S31: -0.0698 S32: -0.1022 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1102 THROUGH 305 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8408 193.8876 11.4668
REMARK 3 T TENSOR
REMARK 3 T11: 0.3127 T22: 0.2846
REMARK 3 T33: 0.2304 T12: -0.0379
REMARK 3 T13: -0.0535 T23: 0.0612
REMARK 3 L TENSOR
REMARK 3 L11: 0.0275 L22: 0.0949
REMARK 3 L33: 0.3921 L12: -0.1061
REMARK 3 L13: 0.0484 L23: 0.2018
REMARK 3 S TENSOR
REMARK 3 S11: -0.1756 S12: 0.2487 S13: 0.0803
REMARK 3 S21: -0.3000 S22: 0.3540 S23: 0.3178
REMARK 3 S31: -0.0428 S32: -0.1487 S33: -0.0000
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 5N2R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003469.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96862
REMARK 200 MONOCHROMATOR : DOUBLE SI (111) CRYSTAL
REMARK 200 OPTICS : (DOUBLE) KB MIRROR PAIR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JANUARY, 2014
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12834
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 90.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.17300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 1.14300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: RECTANGULAR
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 5.5, 0.2M K/NA TARTRATE,
REMARK 280 27.5-40% PEG400, 0.5-1% (V/V) (+/-)-2-METHYL-2,4-PENTANEDIOL,
REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 70.32050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.32050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 19.62700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.36950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.62700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.36950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.32050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.62700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.36950
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.32050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.62700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 90.36950
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 70.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ASP A -8
REMARK 465 TYR A -7
REMARK 465 LYS A -6
REMARK 465 ASP A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 PRO A 1045
REMARK 465 PRO A 1046
REMARK 465 LYS A 1047
REMARK 465 LEU A 1048
REMARK 465 GLU A 1049
REMARK 465 ASP A 1050
REMARK 465 LYS A 1051
REMARK 465 SER A 1052
REMARK 465 PRO A 1053
REMARK 465 ASP A 1054
REMARK 465 SER A 1055
REMARK 465 PRO A 1056
REMARK 465 GLU A 1057
REMARK 465 MET A 1058
REMARK 465 LYS A 1059
REMARK 465 HIS A 306
REMARK 465 VAL A 307
REMARK 465 LEU A 308
REMARK 465 ARG A 309
REMARK 465 GLN A 310
REMARK 465 GLN A 311
REMARK 465 GLU A 312
REMARK 465 PRO A 313
REMARK 465 PHE A 314
REMARK 465 LYS A 315
REMARK 465 ALA A 316
REMARK 465 ALA A 317
REMARK 465 ALA A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 465 HIS A 327
REMARK 465 HIS A 328
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O GLY A -1 NH2 ARG A 300 4575 2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 58 -50.81 -124.72
REMARK 500 VAL A 186 -53.63 -121.81
REMARK 500 TYR A1101 -55.67 -131.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLA A 2406
REMARK 610 OLA A 2407
REMARK 610 OLA A 2408
REMARK 610 OLA A 2409
REMARK 610 OLA A 2410
REMARK 610 OLA A 2412
REMARK 610 OLA A 2413
REMARK 610 OLA A 2414
REMARK 610 OLA A 2415
REMARK 610 OLA A 2416
REMARK 610 OLA A 2417
REMARK 610 OLA A 2419
REMARK 610 OLA A 2420
REMARK 610 OLA A 2421
REMARK 610 OLA A 2422
REMARK 610 OLA A 2423
REMARK 610 OLA A 2424
REMARK 610 OLA A 2425
REMARK 610 OLC A 2426
REMARK 610 OLC A 2427
REMARK 610 OLC A 2428
REMARK 610 OLC A 2429
REMARK 610 OLC A 2430
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A2400 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 52 OD1
REMARK 620 2 SER A 91 OG 122.7
REMARK 620 3 HOH A2514 O 97.7 111.6
REMARK 620 4 HOH A2534 O 75.1 77.8 61.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 2400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8JN A 2401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2417
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2418
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2419
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2420
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2421
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2422
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2424
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2425
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2426
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2427
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2428
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2429
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2430
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TAR A 2431
DBREF 5N2R A 2 208 UNP P29274 AA2AR_HUMAN 2 208
DBREF 5N2R A 1001 1105 UNP P0ABE7 C562_ECOLX 23 127
DBREF 5N2R A 219 233 PDB 5N2R 5N2R 219 233
DBREF 5N2R A 234 318 UNP P29274 AA2AR_HUMAN 234 318
SEQADV 5N2R ASP A -8 UNP P29274 EXPRESSION TAG
SEQADV 5N2R TYR A -7 UNP P29274 EXPRESSION TAG
SEQADV 5N2R LYS A -6 UNP P29274 EXPRESSION TAG
SEQADV 5N2R ASP A -5 UNP P29274 EXPRESSION TAG
SEQADV 5N2R ASP A -4 UNP P29274 EXPRESSION TAG
SEQADV 5N2R ASP A -3 UNP P29274 EXPRESSION TAG
SEQADV 5N2R ASP A -2 UNP P29274 EXPRESSION TAG
SEQADV 5N2R GLY A -1 UNP P29274 EXPRESSION TAG
SEQADV 5N2R ALA A 0 UNP P29274 EXPRESSION TAG
SEQADV 5N2R PRO A 1 UNP P29274 EXPRESSION TAG
SEQADV 5N2R LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION
SEQADV 5N2R ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION
SEQADV 5N2R ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION
SEQADV 5N2R ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION
SEQADV 5N2R ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION
SEQADV 5N2R ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION
SEQADV 5N2R TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 5N2R ILE A 1102 UNP P0ABE7 HIS 124 CONFLICT
SEQADV 5N2R LEU A 1106 UNP P0ABE7 LINKER
SEQADV 5N2R ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION
SEQADV 5N2R ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION
SEQADV 5N2R ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION
SEQADV 5N2R ALA A 318 UNP P29274 GLY 318 ENGINEERED MUTATION
SEQADV 5N2R HIS A 319 UNP P29274 EXPRESSION TAG
SEQADV 5N2R HIS A 320 UNP P29274 EXPRESSION TAG
SEQADV 5N2R HIS A 321 UNP P29274 EXPRESSION TAG
SEQADV 5N2R HIS A 322 UNP P29274 EXPRESSION TAG
SEQADV 5N2R HIS A 323 UNP P29274 EXPRESSION TAG
SEQADV 5N2R HIS A 324 UNP P29274 EXPRESSION TAG
SEQADV 5N2R HIS A 325 UNP P29274 EXPRESSION TAG
SEQADV 5N2R HIS A 326 UNP P29274 EXPRESSION TAG
SEQADV 5N2R HIS A 327 UNP P29274 EXPRESSION TAG
SEQADV 5N2R HIS A 328 UNP P29274 EXPRESSION TAG
SEQRES 1 A 433 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE MET
SEQRES 2 A 433 GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE ALA
SEQRES 3 A 433 VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP ALA
SEQRES 4 A 433 VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN TYR
SEQRES 5 A 433 PHE VAL VAL SER LEU ALA ALA ALA ASP ILE LEU VAL GLY
SEQRES 6 A 433 VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR GLY
SEQRES 7 A 433 PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA CYS
SEQRES 8 A 433 PHE VAL LEU VAL LEU ALA GLN SER SER ILE PHE SER LEU
SEQRES 9 A 433 LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ALA ILE
SEQRES 10 A 433 PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG ALA
SEQRES 11 A 433 ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE ALA
SEQRES 12 A 433 ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS GLY
SEQRES 13 A 433 GLN PRO LYS GLU GLY LYS ALA HIS SER GLN GLY CYS GLY
SEQRES 14 A 433 GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL PRO
SEQRES 15 A 433 MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS VAL
SEQRES 16 A 433 LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU ARG
SEQRES 17 A 433 ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA ASP LEU GLU
SEQRES 18 A 433 ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE
SEQRES 19 A 433 GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU
SEQRES 20 A 433 THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA
SEQRES 21 A 433 THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO
SEQRES 22 A 433 GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL
SEQRES 23 A 433 GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY
SEQRES 24 A 433 LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS
SEQRES 25 A 433 THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU ARG
SEQRES 26 A 433 ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS
SEQRES 27 A 433 SER ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS TRP
SEQRES 28 A 433 LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS
SEQRES 29 A 433 PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU
SEQRES 30 A 433 ALA ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN PRO
SEQRES 31 A 433 PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR
SEQRES 32 A 433 PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN
SEQRES 33 A 433 GLU PRO PHE LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS
SEQRES 34 A 433 HIS HIS HIS HIS
HET NA A2400 1
HET 8JN A2401 28
HET CLR A2402 28
HET CLR A2403 28
HET CLR A2404 28
HET OLA A2405 20
HET OLA A2406 15
HET OLA A2407 14
HET OLA A2408 11
HET OLA A2409 7
HET OLA A2410 17
HET OLA A2411 20
HET OLA A2412 7
HET OLA A2413 8
HET OLA A2414 9
HET OLA A2415 14
HET OLA A2416 17
HET OLA A2417 14
HET OLA A2418 20
HET OLA A2419 17
HET OLA A2420 11
HET OLA A2421 9
HET OLA A2422 14
HET OLA A2423 10
HET OLA A2424 16
HET OLA A2425 10
HET OLC A2426 16
HET OLC A2427 20
HET OLC A2428 20
HET OLC A2429 21
HET OLC A2430 18
HET TAR A2431 10
HETNAM NA SODIUM ION
HETNAM 8JN 1-BUTYL-3-[(~{E})-3-OXIDANYLPROP-1-ENYL]-8-[(1~{R},
HETNAM 2 8JN 5~{S})-3-TRICYCLO[3.3.1.0^{3,7}]NONANYL]-7~{H}-PURINE-
HETNAM 3 8JN 2,6-DIONE
HETNAM CLR CHOLESTEROL
HETNAM OLA OLEIC ACID
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM TAR D(-)-TARTARIC ACID
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 NA NA 1+
FORMUL 3 8JN C21 H28 N4 O3
FORMUL 4 CLR 3(C27 H46 O)
FORMUL 7 OLA 21(C18 H34 O2)
FORMUL 28 OLC 5(C21 H40 O4)
FORMUL 33 TAR C4 H6 O6
FORMUL 34 HOH *37(H2 O)
HELIX 1 AA1 PRO A 1 ASN A 34 1 34
HELIX 2 AA2 SER A 35 GLN A 38 5 4
HELIX 3 AA3 ASN A 39 LEU A 58 1 20
HELIX 4 AA4 LEU A 58 SER A 67 1 10
HELIX 5 AA5 CYS A 74 ILE A 108 1 35
HELIX 6 AA6 ARG A 111 VAL A 116 1 6
HELIX 7 AA7 THR A 117 LEU A 137 1 21
HELIX 8 AA8 THR A 138 GLY A 142 5 5
HELIX 9 AA9 LYS A 150 GLN A 157 1 8
HELIX 10 AB1 LEU A 167 VAL A 172 1 6
HELIX 11 AB2 PRO A 173 PHE A 180 1 8
HELIX 12 AB3 VAL A 186 LEU A 208 1 23
HELIX 13 AB4 ASP A 1002 LYS A 1019 1 18
HELIX 14 AB5 ASN A 1022 THR A 1044 1 23
HELIX 15 AB6 PHE A 1061 GLU A 1081 1 21
HELIX 16 AB7 LYS A 1083 GLN A 1093 1 11
HELIX 17 AB8 GLN A 1093 TYR A 1101 1 9
HELIX 18 AB9 TYR A 1101 LEU A 1106 1 6
HELIX 19 AC1 ARG A 220 CYS A 259 1 40
HELIX 20 AC2 PRO A 266 ILE A 292 1 27
HELIX 21 AC3 ILE A 292 SER A 305 1 14
SHEET 1 AA1 2 CYS A 71 ALA A 73 0
SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72
SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.03
SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03
SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03
SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03
LINK OD1 ASP A 52 NA NA A2400 1555 1555 2.41
LINK OG SER A 91 NA NA A2400 1555 1555 2.44
LINK NA NA A2400 O HOH A2514 1555 1555 2.59
LINK NA NA A2400 O HOH A2534 1555 1555 2.52
SITE 1 AC1 5 ASP A 52 SER A 91 ASN A 280 HOH A2514
SITE 2 AC1 5 HOH A2534
SITE 1 AC2 15 PHE A 168 GLU A 169 MET A 174 MET A 177
SITE 2 AC2 15 TRP A 246 LEU A 249 ASN A 253 THR A 256
SITE 3 AC2 15 HIS A 264 MET A 270 ILE A 274 HIS A 278
SITE 4 AC2 15 HOH A2502 HOH A2504 HOH A2513
SITE 1 AC3 6 ALA A 72 ALA A 73 GLY A 76 ILE A 80
SITE 2 AC3 6 CLR A2404 OLC A2426
SITE 1 AC4 5 PRO A 248 CYS A 262 SER A 263 LEU A 269
SITE 2 AC4 5 OLA A2424
SITE 1 AC5 7 CYS A 254 PHE A 255 PHE A 258 CYS A 259
SITE 2 AC5 7 CLR A2402 OLA A2407 OLC A2428
SITE 1 AC6 2 THR A 65 OLC A2428
SITE 1 AC7 2 PRO A 266 LEU A 272
SITE 1 AC8 6 LEU A 194 PHE A 201 ALA A 236 CLR A2404
SITE 2 AC8 6 OLA A2416 OLA A2417
SITE 1 AC9 3 HIS A 75 GLY A 76 OLA A2419
SITE 1 AD1 2 LEU A 19 THR A 279
SITE 1 AD2 4 GLY A 5 SER A 6 LEU A 267 TYR A 271
SITE 1 AD3 4 LEU A 96 ILE A 127 OLA A2415 OLA A2418
SITE 1 AD4 3 LEU A 19 PHE A 286 HOH A2524
SITE 1 AD5 3 GLY A 123 OLA A2411 OLA A2418
SITE 1 AD6 5 TRP A 32 PHE A 201 LYS A 233 OLA A2407
SITE 2 AD6 5 OLC A2430
SITE 1 AD7 3 ALA A 236 GLY A 240 OLA A2407
SITE 1 AD8 12 HIS A 75 LEU A 131 ALA A 134 MET A 140
SITE 2 AD8 12 LEU A 141 TYR A 179 PHE A 183 OLA A2411
SITE 3 AD8 12 OLA A2415 OLA A2419 OLC A2427 HOH A2503
SITE 1 AD9 5 PHE A 133 MET A 140 OLA A2408 OLA A2418
SITE 2 AD9 5 OLA A2420
SITE 1 AE1 4 ALA A 122 OLA A2419 OLA A2422 OLC A2429
SITE 1 AE2 3 ALA A 97 ILE A 100 VAL A 116
SITE 1 AE3 3 ALA A 122 GLY A 123 OLA A2420
SITE 1 AE4 3 PHE A 255 SER A 263 CLR A2403
SITE 1 AE5 2 ILE A 287 TYR A 290
SITE 1 AE6 3 PHE A 258 CLR A2402 OLC A2427
SITE 1 AE7 4 TYR A 179 PHE A 257 OLA A2418 OLC A2426
SITE 1 AE8 9 LEU A 58 PHE A 62 THR A 65 PHE A 70
SITE 2 AE8 9 CYS A 71 GLN A 163 ASP A 261 CLR A2404
SITE 3 AE8 9 OLA A2405
SITE 1 AE9 6 GLY A 118 ILE A 125 TRP A 129 PHE A 133
SITE 2 AE9 6 OLA A2420 OLC A2430
SITE 1 AF1 8 CYS A 28 TRP A 32 TYR A 43 VAL A 46
SITE 2 AF1 8 ALA A 50 ARG A 205 OLA A2416 OLC A2429
SITE 1 AF2 6 GLY A 142 TRP A 143 ASN A 144 ASN A 145
SITE 2 AF2 6 PRO A 173 ASN A 175
CRYST1 39.254 180.739 140.641 90.00 90.00 90.00 C 2 2 21 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 0.025475 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005533 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007110 0.00000
ATOM 1 N GLY A -1 20.540 156.058 1.537 1.00134.68 N
ANISOU 1 N GLY A -1 19324 15925 15924 -496 270 -637 N
ATOM 2 CA GLY A -1 21.144 157.182 2.228 1.00132.27 C
ANISOU 2 CA GLY A -1 18841 15728 15687 -416 268 -605 C
ATOM 3 C GLY A -1 22.390 157.708 1.544 1.00135.39 C
ANISOU 3 C GLY A -1 19204 16180 16059 -311 304 -610 C
ATOM 4 O GLY A -1 23.447 157.076 1.592 1.00137.46 O
ANISOU 4 O GLY A -1 19539 16410 16281 -193 372 -616 O
ATOM 5 N ALA A 0 22.259 158.872 0.910 1.00133.55 N
ANISOU 5 N ALA A 0 18860 16033 15849 -353 260 -604 N
ATOM 6 CA ALA A 0 23.374 159.483 0.205 1.00125.93 C
ANISOU 6 CA ALA A 0 17852 15132 14863 -269 287 -607 C
ATOM 7 C ALA A 0 24.528 159.761 1.169 1.00125.17 C
ANISOU 7 C ALA A 0 17671 15092 14796 -134 334 -579 C
ATOM 8 O ALA A 0 24.309 159.937 2.372 1.00127.39 O
ANISOU 8 O ALA A 0 17876 15391 15134 -127 326 -553 O
ATOM 9 CB ALA A 0 22.928 160.780 -0.467 1.00123.66 C
ANISOU 9 CB ALA A 0 17447 14931 14606 -345 225 -599 C
ATOM 10 N PRO A 1 25.763 159.793 0.669 1.00123.65 N
ANISOU 10 N PRO A 1 17488 14932 14563 -27 384 -581 N
ATOM 11 CA PRO A 1 26.920 160.051 1.538 1.00120.83 C
ANISOU 11 CA PRO A 1 17045 14640 14224 100 430 -551 C
ATOM 12 C PRO A 1 26.736 161.329 2.335 1.00121.27 C
ANISOU 12 C PRO A 1 16923 14793 14360 71 384 -519 C
ATOM 13 O PRO A 1 26.386 162.378 1.773 1.00118.86 O
ANISOU 13 O PRO A 1 16536 14547 14079 2 335 -518 O
ATOM 14 CB PRO A 1 28.084 160.174 0.544 1.00118.42 C
ANISOU 14 CB PRO A 1 16757 14378 13860 185 471 -557 C
ATOM 15 CG PRO A 1 27.665 159.328 -0.611 1.00119.30 C
ANISOU 15 CG PRO A 1 17031 14396 13903 140 477 -597 C
ATOM 16 CD PRO A 1 26.172 159.506 -0.718 1.00121.40 C
ANISOU 16 CD PRO A 1 17300 14625 14204 -16 405 -610 C
ATOM 17 N PRO A 2 26.949 161.276 3.653 1.00117.96 N
ANISOU 17 N PRO A 2 16446 14390 13981 121 401 -493 N
ATOM 18 CA PRO A 2 26.656 162.452 4.489 1.00112.22 C
ANISOU 18 CA PRO A 2 15563 13744 13330 85 356 -465 C
ATOM 19 C PRO A 2 27.465 163.682 4.123 1.00100.48 C
ANISOU 19 C PRO A 2 13958 12368 11852 114 349 -450 C
ATOM 20 O PRO A 2 26.972 164.802 4.300 1.00101.56 O
ANISOU 20 O PRO A 2 13988 12561 12041 49 298 -437 O
ATOM 21 CB PRO A 2 26.988 161.962 5.906 1.00111.82 C
ANISOU 21 CB PRO A 2 15494 13687 13304 157 391 -442 C
ATOM 22 CG PRO A 2 26.886 160.473 5.830 1.00108.08 C
ANISOU 22 CG PRO A 2 15182 13102 12780 185 433 -461 C
ATOM 23 CD PRO A 2 27.361 160.113 4.456 1.00111.83 C
ANISOU 23 CD PRO A 2 15754 13552 13184 207 458 -488 C
ATOM 24 N ILE A 3 28.687 163.512 3.610 1.00100.71 N
ANISOU 24 N ILE A 3 14006 12430 11828 209 399 -448 N
ATOM 25 CA ILE A 3 29.536 164.659 3.304 1.00106.06 C
ANISOU 25 CA ILE A 3 14570 13218 12508 236 395 -430 C
ATOM 26 C ILE A 3 28.975 165.494 2.159 1.00102.61 C
ANISOU 26 C ILE A 3 14114 12800 12074 143 343 -445 C
ATOM 27 O ILE A 3 29.326 166.672 2.027 1.00102.72 O
ANISOU 27 O ILE A 3 14019 12901 12108 130 320 -429 O
ATOM 28 CB ILE A 3 30.971 164.195 2.987 1.00104.36 C
ANISOU 28 CB ILE A 3 14383 13040 12229 362 463 -421 C
ATOM 29 CG1 ILE A 3 31.949 165.371 3.062 1.00105.02 C
ANISOU 29 CG1 ILE A 3 14328 13253 12321 395 462 -391 C
ATOM 30 CG2 ILE A 3 31.028 163.544 1.620 1.00103.48 C
ANISOU 30 CG2 ILE A 3 14395 12874 12048 366 483 -453 C
ATOM 31 CD1 ILE A 3 33.349 165.038 2.593 1.00104.14 C
ANISOU 31 CD1 ILE A 3 14231 13197 12140 511 525 -378 C
ATOM 32 N MET A 4 28.103 164.919 1.328 1.00 91.56 N
ANISOU 32 N MET A 4 12819 11321 10650 74 324 -476 N
ATOM 33 CA MET A 4 27.517 165.675 0.227 1.00 83.49 C
ANISOU 33 CA MET A 4 11778 10318 9626 -16 274 -488 C
ATOM 34 C MET A 4 26.551 166.734 0.745 1.00 78.56 C
ANISOU 34 C MET A 4 11048 9728 9075 -105 210 -471 C
ATOM 35 O MET A 4 26.719 167.931 0.479 1.00 79.81 O
ANISOU 35 O MET A 4 11109 9962 9254 -126 182 -457 O
ATOM 36 CB MET A 4 26.819 164.723 -0.743 1.00 86.81 C
ANISOU 36 CB MET A 4 12341 10645 9996 -71 270 -524 C
ATOM 37 CG MET A 4 27.753 163.695 -1.354 1.00 89.99 C
ANISOU 37 CG MET A 4 12863 11007 10321 19 336 -543 C
ATOM 38 SD MET A 4 26.935 162.662 -2.580 1.00 90.61 S
ANISOU 38 SD MET A 4 13117 10976 10334 -56 329 -589 S
ATOM 39 CE MET A 4 26.392 163.905 -3.751 1.00 92.48 C
ANISOU 39 CE MET A 4 13278 11278 10581 -160 262 -592 C
ATOM 40 N GLY A 5 25.527 166.311 1.490 1.00 72.09 N
ANISOU 40 N GLY A 5 10248 8855 8290 -158 187 -471 N
ATOM 41 CA GLY A 5 24.666 167.274 2.154 1.00 75.53 C
ANISOU 41 CA GLY A 5 10579 9327 8794 -224 135 -450 C
ATOM 42 C GLY A 5 25.413 168.125 3.160 1.00 69.65 C
ANISOU 42 C GLY A 5 9718 8657 8090 -165 146 -421 C
ATOM 43 O GLY A 5 25.028 169.267 3.423 1.00 62.51 O
ANISOU 43 O GLY A 5 8715 7803 7231 -207 106 -403 O
ATOM 44 N SER A 6 26.488 167.583 3.739 1.00 61.45 N
ANISOU 44 N SER A 6 8691 7626 7032 -66 201 -414 N
ATOM 45 CA SER A 6 27.308 168.364 4.658 1.00 57.85 C
ANISOU 45 CA SER A 6 8126 7250 6606 -11 213 -386 C
ATOM 46 C SER A 6 28.028 169.491 3.931 1.00 58.42 C
ANISOU 46 C SER A 6 8126 7405 6665 -9 204 -377 C
ATOM 47 O SER A 6 28.166 170.596 4.469 1.00 66.02 O
ANISOU 47 O SER A 6 8986 8433 7666 -22 182 -356 O
ATOM 48 CB SER A 6 28.315 167.456 5.364 1.00 60.12 C
ANISOU 48 CB SER A 6 8444 7533 6867 96 276 -378 C
ATOM 49 OG SER A 6 27.680 166.321 5.925 1.00 80.00 O
ANISOU 49 OG SER A 6 11045 9964 9387 95 288 -387 O
ATOM 50 N SER A 7 28.489 169.231 2.704 1.00 59.75 N
ANISOU 50 N SER A 7 8353 7573 6779 6 220 -394 N
ATOM 51 CA SER A 7 29.237 170.243 1.964 1.00 56.01 C
ANISOU 51 CA SER A 7 7815 7180 6287 10 215 -384 C
ATOM 52 C SER A 7 28.371 171.452 1.634 1.00 55.85 C
ANISOU 52 C SER A 7 7732 7181 6308 -85 153 -380 C
ATOM 53 O SER A 7 28.843 172.592 1.693 1.00 61.02 O
ANISOU 53 O SER A 7 8299 7910 6977 -90 139 -361 O
ATOM 54 CB SER A 7 29.821 169.639 0.688 1.00 58.60 C
ANISOU 54 CB SER A 7 8226 7497 6544 45 246 -404 C
ATOM 55 OG SER A 7 30.817 168.678 0.991 1.00 72.93 O
ANISOU 55 OG SER A 7 10086 9309 8316 151 310 -401 O
ATOM 56 N VAL A 8 27.103 171.226 1.284 1.00 52.96 N
ANISOU 56 N VAL A 8 7413 6754 5957 -162 115 -396 N
ATOM 57 CA VAL A 8 26.200 172.344 1.016 1.00 56.54 C
ANISOU 57 CA VAL A 8 7806 7228 6448 -247 57 -387 C
ATOM 58 C VAL A 8 25.986 173.165 2.280 1.00 64.66 C
ANISOU 58 C VAL A 8 8741 8289 7537 -252 40 -361 C
ATOM 59 O VAL A 8 26.036 174.401 2.259 1.00 58.55 O
ANISOU 59 O VAL A 8 7891 7569 6787 -276 14 -344 O
ATOM 60 CB VAL A 8 24.868 171.833 0.439 1.00 53.65 C
ANISOU 60 CB VAL A 8 7506 6797 6080 -327 22 -405 C
ATOM 61 CG1 VAL A 8 23.815 172.926 0.492 1.00 46.88 C
ANISOU 61 CG1 VAL A 8 6578 5964 5270 -404 -35 -387 C
ATOM 62 CG2 VAL A 8 25.064 171.355 -0.988 1.00 56.86 C
ANISOU 62 CG2 VAL A 8 7995 7184 6424 -337 30 -430 C
ATOM 63 N TYR A 9 25.752 172.488 3.406 1.00 55.42 N
ANISOU 63 N TYR A 9 7582 7085 6392 -228 54 -358 N
ATOM 64 CA TYR A 9 25.562 173.199 4.665 1.00 38.90 C
ANISOU 64 CA TYR A 9 5406 5020 4354 -228 41 -335 C
ATOM 65 C TYR A 9 26.827 173.942 5.081 1.00 39.24 C
ANISOU 65 C TYR A 9 5378 5140 4393 -174 64 -317 C
ATOM 66 O TYR A 9 26.757 175.082 5.554 1.00 37.18 O
ANISOU 66 O TYR A 9 5041 4921 4166 -198 40 -299 O
ATOM 67 CB TYR A 9 25.124 172.221 5.754 1.00 39.40 C
ANISOU 67 CB TYR A 9 5499 5031 4438 -210 56 -335 C
ATOM 68 CG TYR A 9 25.229 172.782 7.153 1.00 54.21 C
ANISOU 68 CG TYR A 9 7296 6941 6361 -189 56 -312 C
ATOM 69 CD1 TYR A 9 24.435 173.849 7.555 1.00 46.08 C
ANISOU 69 CD1 TYR A 9 6200 5932 5378 -241 14 -297 C
ATOM 70 CD2 TYR A 9 26.119 172.243 8.073 1.00 38.91 C
ANISOU 70 CD2 TYR A 9 5352 5015 4416 -114 99 -304 C
ATOM 71 CE1 TYR A 9 24.529 174.368 8.833 1.00 42.71 C
ANISOU 71 CE1 TYR A 9 5707 5532 4990 -222 15 -278 C
ATOM 72 CE2 TYR A 9 26.219 172.755 9.354 1.00 41.36 C
ANISOU 72 CE2 TYR A 9 5590 5358 4766 -98 98 -284 C
ATOM 73 CZ TYR A 9 25.423 173.817 9.729 1.00 39.24 C
ANISOU 73 CZ TYR A 9 5262 5105 4544 -154 56 -272 C
ATOM 74 OH TYR A 9 25.519 174.327 11.003 1.00 34.82 O
ANISOU 74 OH TYR A 9 4638 4575 4019 -138 57 -254 O
ATOM 75 N ILE A 10 27.994 173.317 4.908 1.00 43.32 N
ANISOU 75 N ILE A 10 5920 5676 4864 -102 112 -320 N
ATOM 76 CA ILE A 10 29.241 173.951 5.329 1.00 40.89 C
ANISOU 76 CA ILE A 10 5540 5450 4544 -52 135 -299 C
ATOM 77 C ILE A 10 29.581 175.129 4.422 1.00 44.73 C
ANISOU 77 C ILE A 10 5983 5995 5018 -89 112 -293 C
ATOM 78 O ILE A 10 30.009 176.189 4.896 1.00 51.22 O
ANISOU 78 O ILE A 10 6728 6878 5856 -100 101 -272 O
ATOM 79 CB ILE A 10 30.379 172.915 5.371 1.00 45.96 C
ANISOU 79 CB ILE A 10 6220 6106 5136 41 194 -298 C
ATOM 80 CG1 ILE A 10 30.181 171.950 6.542 1.00 58.72 C
ANISOU 80 CG1 ILE A 10 7862 7678 6771 83 218 -295 C
ATOM 81 CG2 ILE A 10 31.731 173.601 5.482 1.00 41.63 C
ANISOU 81 CG2 ILE A 10 5597 5660 4562 85 216 -273 C
ATOM 82 CD1 ILE A 10 31.171 170.799 6.562 1.00 57.31 C
ANISOU 82 CD1 ILE A 10 7736 7499 6541 182 280 -294 C
ATOM 83 N THR A 11 29.392 174.971 3.110 1.00 51.04 N
ANISOU 83 N THR A 11 6833 6775 5784 -113 104 -310 N
ATOM 84 CA THR A 11 29.704 176.056 2.183 1.00 53.65 C
ANISOU 84 CA THR A 11 7127 7159 6100 -148 83 -303 C
ATOM 85 C THR A 11 28.807 177.266 2.424 1.00 57.20 C
ANISOU 85 C THR A 11 7524 7610 6600 -221 32 -292 C
ATOM 86 O THR A 11 29.270 178.411 2.378 1.00 45.63 O
ANISOU 86 O THR A 11 5999 6202 5137 -239 19 -275 O
ATOM 87 CB THR A 11 29.572 175.569 0.738 1.00 49.37 C
ANISOU 87 CB THR A 11 6656 6589 5512 -161 83 -326 C
ATOM 88 OG1 THR A 11 30.390 174.408 0.546 1.00 45.09 O
ANISOU 88 OG1 THR A 11 6173 6039 4919 -85 136 -336 O
ATOM 89 CG2 THR A 11 30.014 176.650 -0.232 1.00 46.06 C
ANISOU 89 CG2 THR A 11 6198 6231 5073 -191 66 -317 C
ATOM 90 N VAL A 12 27.520 177.031 2.688 1.00 50.29 N
ANISOU 90 N VAL A 12 6673 6674 5762 -263 3 -300 N
ATOM 91 CA VAL A 12 26.610 178.135 2.980 1.00 39.98 C
ANISOU 91 CA VAL A 12 5319 5370 4503 -322 -41 -286 C
ATOM 92 C VAL A 12 27.006 178.823 4.282 1.00 49.00 C
ANISOU 92 C VAL A 12 6393 6546 5677 -303 -36 -265 C
ATOM 93 O VAL A 12 26.976 180.056 4.384 1.00 40.04 O
ANISOU 93 O VAL A 12 5209 5443 4560 -333 -58 -250 O
ATOM 94 CB VAL A 12 25.156 177.627 3.016 1.00 48.56 C
ANISOU 94 CB VAL A 12 6441 6392 5616 -366 -69 -294 C
ATOM 95 CG1 VAL A 12 24.230 178.684 3.599 1.00 46.35 C
ANISOU 95 CG1 VAL A 12 6106 6117 5387 -408 -107 -273 C
ATOM 96 CG2 VAL A 12 24.702 177.234 1.617 1.00 35.25 C
ANISOU 96 CG2 VAL A 12 4815 4682 3896 -404 -84 -311 C
ATOM 97 N GLU A 13 27.402 178.041 5.291 1.00 38.31 N
ANISOU 97 N GLU A 13 5041 5186 4328 -253 -5 -265 N
ATOM 98 CA GLU A 13 27.791 178.619 6.575 1.00 32.71 C
ANISOU 98 CA GLU A 13 4270 4511 3646 -235 1 -246 C
ATOM 99 C GLU A 13 29.053 179.464 6.448 1.00 39.38 C
ANISOU 99 C GLU A 13 5066 5434 4461 -223 14 -232 C
ATOM 100 O GLU A 13 29.171 180.513 7.092 1.00 43.61 O
ANISOU 100 O GLU A 13 5551 6003 5018 -246 -1 -216 O
ATOM 101 CB GLU A 13 27.990 177.512 7.609 1.00 33.81 C
ANISOU 101 CB GLU A 13 4425 4631 3791 -181 34 -248 C
ATOM 102 CG GLU A 13 26.695 176.912 8.128 1.00 44.08 C
ANISOU 102 CG GLU A 13 5756 5862 5131 -203 17 -255 C
ATOM 103 CD GLU A 13 26.161 177.632 9.353 1.00 56.03 C
ANISOU 103 CD GLU A 13 7215 7381 6694 -220 -1 -239 C
ATOM 104 OE1 GLU A 13 26.019 176.983 10.412 1.00 40.85 O
ANISOU 104 OE1 GLU A 13 5292 5438 4791 -192 14 -235 O
ATOM 105 OE2 GLU A 13 25.893 178.849 9.263 1.00 67.89 O
ANISOU 105 OE2 GLU A 13 8677 8905 8213 -259 -30 -228 O
ATOM 106 N LEU A 14 30.008 179.024 5.628 1.00 39.57 N
ANISOU 106 N LEU A 14 5108 5491 4434 -189 41 -236 N
ATOM 107 CA LEU A 14 31.214 179.818 5.420 1.00 38.77 C
ANISOU 107 CA LEU A 14 4957 5473 4299 -184 52 -218 C
ATOM 108 C LEU A 14 30.910 181.098 4.652 1.00 47.69 C
ANISOU 108 C LEU A 14 6070 6616 5433 -250 14 -214 C
ATOM 109 O LEU A 14 31.525 182.140 4.907 1.00 43.71 O
ANISOU 109 O LEU A 14 5516 6168 4923 -272 7 -195 O
ATOM 110 CB LEU A 14 32.268 178.988 4.690 1.00 40.75 C
ANISOU 110 CB LEU A 14 5232 5760 4490 -125 92 -221 C
ATOM 111 CG LEU A 14 32.816 177.811 5.496 1.00 40.04 C
ANISOU 111 CG LEU A 14 5154 5672 4387 -46 137 -218 C
ATOM 112 CD1 LEU A 14 33.821 177.011 4.680 1.00 53.36 C
ANISOU 112 CD1 LEU A 14 6871 7393 6009 20 181 -219 C
ATOM 113 CD2 LEU A 14 33.439 178.306 6.792 1.00 28.48 C
ANISOU 113 CD2 LEU A 14 3618 4267 2935 -33 145 -193 C
ATOM 114 N ALA A 15 29.970 181.042 3.706 1.00 47.33 N
ANISOU 114 N ALA A 15 6068 6521 5395 -285 -11 -228 N
ATOM 115 CA ALA A 15 29.571 182.252 2.995 1.00 36.83 C
ANISOU 115 CA ALA A 15 4724 5198 4071 -346 -47 -221 C
ATOM 116 C ALA A 15 28.915 183.251 3.940 1.00 44.96 C
ANISOU 116 C ALA A 15 5719 6215 5148 -380 -74 -207 C
ATOM 117 O ALA A 15 29.085 184.467 3.790 1.00 51.94 O
ANISOU 117 O ALA A 15 6576 7126 6031 -417 -92 -193 O
ATOM 118 CB ALA A 15 28.631 181.896 1.845 1.00 34.04 C
ANISOU 118 CB ALA A 15 4423 4797 3715 -374 -69 -238 C
ATOM 119 N ILE A 16 28.169 182.754 4.928 1.00 40.54 N
ANISOU 119 N ILE A 16 5163 5612 4628 -368 -75 -211 N
ATOM 120 CA ILE A 16 27.536 183.637 5.901 1.00 39.09 C
ANISOU 120 CA ILE A 16 4950 5415 4487 -392 -97 -198 C
ATOM 121 C ILE A 16 28.578 184.241 6.832 1.00 41.18 C
ANISOU 121 C ILE A 16 5170 5733 4745 -381 -80 -184 C
ATOM 122 O ILE A 16 28.497 185.421 7.195 1.00 41.22 O
ANISOU 122 O ILE A 16 5153 5747 4762 -414 -98 -171 O
ATOM 123 CB ILE A 16 26.451 182.871 6.680 1.00 30.26 C
ANISOU 123 CB ILE A 16 3847 4241 3410 -381 -101 -204 C
ATOM 124 CG1 ILE A 16 25.296 182.505 5.750 1.00 21.49 C
ANISOU 124 CG1 ILE A 16 2774 3085 2305 -411 -126 -212 C
ATOM 125 CG2 ILE A 16 25.958 183.686 7.869 1.00 22.29 C
ANISOU 125 CG2 ILE A 16 2804 3224 2440 -392 -114 -189 C
ATOM 126 CD1 ILE A 16 24.252 181.655 6.410 1.00 45.06 C
ANISOU 126 CD1 ILE A 16 5776 6022 5322 -407 -131 -216 C
ATOM 127 N ALA A 17 29.574 183.448 7.231 1.00 44.84 N
ANISOU 127 N ALA A 17 5622 6232 5182 -334 -45 -185 N
ATOM 128 CA ALA A 17 30.616 183.960 8.113 1.00 49.35 C
ANISOU 128 CA ALA A 17 6146 6865 5739 -327 -30 -168 C
ATOM 129 C ALA A 17 31.391 185.091 7.447 1.00 55.37 C
ANISOU 129 C ALA A 17 6886 7683 6467 -367 -40 -155 C
ATOM 130 O ALA A 17 31.660 186.125 8.069 1.00 63.48 O
ANISOU 130 O ALA A 17 7886 8736 7497 -401 -50 -142 O
ATOM 131 CB ALA A 17 31.556 182.828 8.526 1.00 25.60 C
ANISOU 131 CB ALA A 17 3129 3894 2703 -263 11 -167 C
ATOM 132 N VAL A 18 31.751 184.912 6.173 1.00 46.38 N
ANISOU 132 N VAL A 18 5765 6563 5293 -367 -36 -159 N
ATOM 133 CA VAL A 18 32.485 185.949 5.452 1.00 35.31 C
ANISOU 133 CA VAL A 18 4345 5217 3855 -408 -45 -146 C
ATOM 134 C VAL A 18 31.664 187.229 5.376 1.00 43.58 C
ANISOU 134 C VAL A 18 5401 6226 4931 -469 -82 -141 C
ATOM 135 O VAL A 18 32.184 188.332 5.588 1.00 41.71 O
ANISOU 135 O VAL A 18 5143 6025 4680 -510 -91 -125 O
ATOM 136 CB VAL A 18 32.880 185.447 4.050 1.00 36.20 C
ANISOU 136 CB VAL A 18 4479 5349 3926 -393 -35 -152 C
ATOM 137 CG1 VAL A 18 33.503 186.573 3.238 1.00 42.37 C
ANISOU 137 CG1 VAL A 18 5243 6183 4673 -442 -48 -137 C
ATOM 138 CG2 VAL A 18 33.836 184.272 4.160 1.00 45.48 C
ANISOU 138 CG2 VAL A 18 5647 6569 5065 -324 8 -152 C
ATOM 139 N LEU A 19 30.366 187.105 5.084 1.00 41.85 N
ANISOU 139 N LEU A 19 5216 5936 4749 -476 -104 -152 N
ATOM 140 CA LEU A 19 29.515 188.285 4.970 1.00 35.14 C
ANISOU 140 CA LEU A 19 4378 5051 3924 -523 -136 -144 C
ATOM 141 C LEU A 19 29.277 188.938 6.327 1.00 40.04 C
ANISOU 141 C LEU A 19 4983 5656 4575 -532 -141 -135 C
ATOM 142 O LEU A 19 29.187 190.168 6.422 1.00 39.83 O
ANISOU 142 O LEU A 19 4960 5625 4549 -572 -157 -123 O
ATOM 143 CB LEU A 19 28.186 187.912 4.313 1.00 32.91 C
ANISOU 143 CB LEU A 19 4128 4708 3668 -525 -157 -153 C
ATOM 144 CG LEU A 19 28.253 187.486 2.845 1.00 43.13 C
ANISOU 144 CG LEU A 19 5446 6010 4931 -530 -160 -162 C
ATOM 145 CD1 LEU A 19 26.870 187.121 2.326 1.00 39.51 C
ANISOU 145 CD1 LEU A 19 5018 5497 4499 -540 -184 -169 C
ATOM 146 CD2 LEU A 19 28.874 188.584 1.998 1.00 44.04 C
ANISOU 146 CD2 LEU A 19 5555 6163 5013 -568 -170 -148 C
ATOM 147 N ALA A 20 29.169 188.136 7.388 1.00 46.33 N
ANISOU 147 N ALA A 20 5767 6442 5393 -495 -125 -142 N
ATOM 148 CA ALA A 20 28.943 188.705 8.713 1.00 38.26 C
ANISOU 148 CA ALA A 20 4731 5407 4397 -501 -127 -134 C
ATOM 149 C ALA A 20 30.174 189.448 9.212 1.00 37.75 C
ANISOU 149 C ALA A 20 4641 5404 4299 -525 -117 -122 C
ATOM 150 O ALA A 20 30.056 190.522 9.815 1.00 46.75 O
ANISOU 150 O ALA A 20 5785 6533 5445 -559 -129 -114 O
ATOM 151 CB ALA A 20 28.543 187.606 9.696 1.00 28.84 C
ANISOU 151 CB ALA A 20 3532 4192 3235 -455 -112 -143 C
ATOM 152 N ILE A 21 31.363 188.896 8.967 1.00 41.64 N
ANISOU 152 N ILE A 21 5107 5963 4750 -508 -95 -120 N
ATOM 153 CA ILE A 21 32.592 189.535 9.427 1.00 39.95 C
ANISOU 153 CA ILE A 21 4860 5822 4496 -536 -86 -104 C
ATOM 154 C ILE A 21 32.827 190.843 8.682 1.00 53.06 C
ANISOU 154 C ILE A 21 6535 7495 6132 -600 -106 -93 C
ATOM 155 O ILE A 21 33.078 191.886 9.295 1.00 58.63 O
ANISOU 155 O ILE A 21 7240 8209 6827 -647 -115 -83 O
ATOM 156 CB ILE A 21 33.785 188.575 9.270 1.00 36.42 C
ANISOU 156 CB ILE A 21 4377 5453 4006 -495 -54 -98 C
ATOM 157 CG1 ILE A 21 33.631 187.382 10.215 1.00 42.06 C
ANISOU 157 CG1 ILE A 21 5081 6156 4744 -432 -32 -105 C
ATOM 158 CG2 ILE A 21 35.100 189.303 9.523 1.00 26.21 C
ANISOU 158 CG2 ILE A 21 3043 4252 2662 -533 -49 -76 C
ATOM 159 CD1 ILE A 21 34.624 186.273 9.961 1.00 39.69 C
ANISOU 159 CD1 ILE A 21 4758 5918 4404 -375 3 -99 C
ATOM 160 N LEU A 22 32.742 190.808 7.350 1.00 51.03 N
ANISOU 160 N LEU A 22 6295 7236 5860 -606 -113 -95 N
ATOM 161 CA LEU A 22 33.024 191.997 6.550 1.00 48.77 C
ANISOU 161 CA LEU A 22 6022 6964 5545 -666 -132 -83 C
ATOM 162 C LEU A 22 32.050 193.125 6.868 1.00 46.37 C
ANISOU 162 C LEU A 22 5756 6590 5273 -702 -156 -81 C
ATOM 163 O LEU A 22 32.460 194.264 7.118 1.00 43.54 O
ANISOU 163 O LEU A 22 5407 6243 4892 -756 -165 -69 O
ATOM 164 CB LEU A 22 32.975 191.652 5.061 1.00 41.00 C
ANISOU 164 CB LEU A 22 5051 5984 4543 -659 -135 -87 C
ATOM 165 CG LEU A 22 34.096 190.767 4.514 1.00 43.33 C
ANISOU 165 CG LEU A 22 5315 6356 4792 -627 -108 -85 C
ATOM 166 CD1 LEU A 22 33.868 190.464 3.042 1.00 37.76 C
ANISOU 166 CD1 LEU A 22 4634 5642 4072 -620 -113 -92 C
ATOM 167 CD2 LEU A 22 35.450 191.428 4.724 1.00 42.21 C
ANISOU 167 CD2 LEU A 22 5134 6305 4598 -665 -100 -62 C
ATOM 168 N GLY A 23 30.750 192.824 6.865 1.00 43.37 N
ANISOU 168 N GLY A 23 5401 6138 4940 -674 -167 -91 N
ATOM 169 CA GLY A 23 29.761 193.872 7.051 1.00 32.11 C
ANISOU 169 CA GLY A 23 4012 4649 3540 -697 -188 -85 C
ATOM 170 C GLY A 23 29.867 194.554 8.401 1.00 37.11 C
ANISOU 170 C GLY A 23 4649 5271 4180 -713 -184 -81 C
ATOM 171 O GLY A 23 29.773 195.780 8.497 1.00 40.75 O
ANISOU 171 O GLY A 23 5144 5708 4632 -754 -196 -71 O
ATOM 172 N ASN A 24 30.074 193.771 9.462 1.00 45.43 N
ANISOU 172 N ASN A 24 5674 6341 5248 -681 -168 -89 N
ATOM 173 CA ASN A 24 30.088 194.337 10.806 1.00 48.64 C
ANISOU 173 CA ASN A 24 6084 6734 5661 -694 -164 -86 C
ATOM 174 C ASN A 24 31.440 194.938 11.169 1.00 45.23 C
ANISOU 174 C ASN A 24 5637 6369 5179 -744 -158 -77 C
ATOM 175 O ASN A 24 31.502 195.834 12.020 1.00 40.01 O
ANISOU 175 O ASN A 24 4999 5693 4511 -780 -161 -73 O
ATOM 176 CB ASN A 24 29.677 193.274 11.823 1.00 28.15 C
ANISOU 176 CB ASN A 24 3465 4129 3103 -640 -151 -96 C
ATOM 177 CG ASN A 24 28.242 192.831 11.642 1.00 40.71 C
ANISOU 177 CG ASN A 24 5074 5654 4742 -602 -160 -102 C
ATOM 178 OD1 ASN A 24 27.310 193.531 12.041 1.00 50.01 O
ANISOU 178 OD1 ASN A 24 6279 6779 5945 -603 -171 -97 O
ATOM 179 ND2 ASN A 24 28.052 191.669 11.027 1.00 46.94 N
ANISOU 179 ND2 ASN A 24 5849 6447 5540 -568 -156 -110 N
ATOM 180 N VAL A 25 32.527 194.467 10.553 1.00 37.86 N
ANISOU 180 N VAL A 25 4668 5512 4206 -750 -148 -72 N
ATOM 181 CA VAL A 25 33.797 195.176 10.681 1.00 54.74 C
ANISOU 181 CA VAL A 25 6789 7722 6287 -811 -146 -56 C
ATOM 182 C VAL A 25 33.674 196.569 10.080 1.00 52.41 C
ANISOU 182 C VAL A 25 6545 7396 5973 -877 -166 -48 C
ATOM 183 O VAL A 25 34.244 197.540 10.593 1.00 52.36 O
ANISOU 183 O VAL A 25 6555 7407 5934 -940 -171 -38 O
ATOM 184 CB VAL A 25 34.936 194.364 10.032 1.00 49.52 C
ANISOU 184 CB VAL A 25 6075 7156 5585 -795 -129 -48 C
ATOM 185 CG1 VAL A 25 36.099 195.266 9.646 1.00 43.23 C
ANISOU 185 CG1 VAL A 25 5267 6434 4725 -869 -135 -27 C
ATOM 186 CG2 VAL A 25 35.413 193.273 10.980 1.00 33.11 C
ANISOU 186 CG2 VAL A 25 3948 5125 3508 -744 -105 -48 C
ATOM 187 N LEU A 26 32.899 196.693 9.000 1.00 44.47 N
ANISOU 187 N LEU A 26 5569 6341 4985 -865 -179 -50 N
ATOM 188 CA LEU A 26 32.662 197.997 8.392 1.00 41.45 C
ANISOU 188 CA LEU A 26 5241 5920 4589 -919 -197 -41 C
ATOM 189 C LEU A 26 31.863 198.904 9.322 1.00 44.80 C
ANISOU 189 C LEU A 26 5718 6267 5035 -931 -203 -42 C
ATOM 190 O LEU A 26 32.083 200.121 9.351 1.00 49.99 O
ANISOU 190 O LEU A 26 6425 6906 5664 -990 -212 -32 O
ATOM 191 CB LEU A 26 31.939 197.819 7.057 1.00 46.36 C
ANISOU 191 CB LEU A 26 5878 6510 5226 -896 -208 -41 C
ATOM 192 CG LEU A 26 31.806 199.036 6.145 1.00 63.03 C
ANISOU 192 CG LEU A 26 8039 8594 7316 -946 -225 -27 C
ATOM 193 CD1 LEU A 26 33.177 199.536 5.721 1.00 66.74 C
ANISOU 193 CD1 LEU A 26 8496 9140 7724 -1012 -224 -13 C
ATOM 194 CD2 LEU A 26 30.961 198.682 4.933 1.00 68.81 C
ANISOU 194 CD2 LEU A 26 8779 9296 8070 -913 -235 -28 C
ATOM 195 N VAL A 27 30.933 198.330 10.089 1.00 48.16 N
ANISOU 195 N VAL A 27 6142 6647 5511 -874 -198 -53 N
ATOM 196 CA VAL A 27 30.168 199.119 11.050 1.00 43.28 C
ANISOU 196 CA VAL A 27 5572 5960 4913 -874 -200 -54 C
ATOM 197 C VAL A 27 31.082 199.661 12.143 1.00 44.51 C
ANISOU 197 C VAL A 27 5733 6145 5033 -925 -194 -53 C
ATOM 198 O VAL A 27 31.047 200.853 12.469 1.00 51.16 O
ANISOU 198 O VAL A 27 6636 6948 5855 -971 -199 -48 O
ATOM 199 CB VAL A 27 29.018 198.282 11.639 1.00 36.02 C
ANISOU 199 CB VAL A 27 4638 4998 4051 -801 -196 -63 C
ATOM 200 CG1 VAL A 27 28.377 199.009 12.811 1.00 23.17 C
ANISOU 200 CG1 VAL A 27 3053 3312 2440 -796 -193 -63 C
ATOM 201 CG2 VAL A 27 27.984 197.975 10.569 1.00 43.82 C
ANISOU 201 CG2 VAL A 27 5632 5950 5068 -764 -207 -60 C
ATOM 202 N CYS A 28 31.914 198.792 12.727 1.00 42.77 N
ANISOU 202 N CYS A 28 5452 5997 4802 -917 -181 -57 N
ATOM 203 CA CYS A 28 32.816 199.235 13.786 1.00 46.51 C
ANISOU 203 CA CYS A 28 5922 6511 5237 -969 -176 -54 C
ATOM 204 C CYS A 28 33.839 200.230 13.257 1.00 52.03 C
ANISOU 204 C CYS A 28 6642 7254 5874 -1058 -185 -40 C
ATOM 205 O CYS A 28 34.164 201.216 13.929 1.00 61.84 O
ANISOU 205 O CYS A 28 7928 8485 7083 -1122 -189 -37 O
ATOM 206 CB CYS A 28 33.520 198.035 14.420 1.00 41.13 C
ANISOU 206 CB CYS A 28 5164 5909 4554 -936 -159 -56 C
ATOM 207 SG CYS A 28 32.411 196.869 15.231 1.00 58.75 S
ANISOU 207 SG CYS A 28 7376 8093 6854 -841 -147 -71 S
ATOM 208 N TRP A 29 34.356 199.987 12.052 1.00 55.78 N
ANISOU 208 N TRP A 29 7089 7778 6327 -1067 -188 -31 N
ATOM 209 CA TRP A 29 35.312 200.910 11.452 1.00 63.10 C
ANISOU 209 CA TRP A 29 8032 8750 7192 -1154 -198 -14 C
ATOM 210 C TRP A 29 34.681 202.281 11.225 1.00 64.64 C
ANISOU 210 C TRP A 29 8321 8855 7384 -1199 -212 -12 C
ATOM 211 O TRP A 29 35.340 203.313 11.395 1.00 61.68 O
ANISOU 211 O TRP A 29 7987 8491 6958 -1285 -219 -2 O
ATOM 212 CB TRP A 29 35.837 200.319 10.142 1.00 73.65 C
ANISOU 212 CB TRP A 29 9322 10151 8512 -1142 -197 -5 C
ATOM 213 CG TRP A 29 37.145 200.880 9.681 1.00 94.27 C
ANISOU 213 CG TRP A 29 11914 12851 11052 -1224 -202 17 C
ATOM 214 CD1 TRP A 29 37.859 201.886 10.262 1.00104.52 C
ANISOU 214 CD1 TRP A 29 13239 14175 12300 -1316 -209 29 C
ATOM 215 CD2 TRP A 29 37.900 200.460 8.537 1.00105.95 C
ANISOU 215 CD2 TRP A 29 13346 14412 12499 -1226 -199 31 C
ATOM 216 NE1 TRP A 29 39.010 202.123 9.548 1.00110.80 N
ANISOU 216 NE1 TRP A 29 14000 15066 13032 -1379 -213 52 N
ATOM 217 CE2 TRP A 29 39.059 201.261 8.485 1.00108.70 C
ANISOU 217 CE2 TRP A 29 13688 14837 12778 -1321 -206 54 C
ATOM 218 CE3 TRP A 29 37.708 199.487 7.550 1.00110.35 C
ANISOU 218 CE3 TRP A 29 13869 14984 13076 -1158 -191 27 C
ATOM 219 CZ2 TRP A 29 40.021 201.118 7.486 1.00106.88 C
ANISOU 219 CZ2 TRP A 29 13410 14703 12498 -1345 -204 75 C
ATOM 220 CZ3 TRP A 29 38.665 199.347 6.559 1.00108.66 C
ANISOU 220 CZ3 TRP A 29 13615 14860 12813 -1179 -188 45 C
ATOM 221 CH2 TRP A 29 39.807 200.158 6.535 1.00107.73 C
ANISOU 221 CH2 TRP A 29 13484 14822 12627 -1270 -194 70 C
ATOM 222 N ALA A 30 33.397 202.311 10.857 1.00 56.09 N
ANISOU 222 N ALA A 30 7278 7684 6352 -1142 -215 -19 N
ATOM 223 CA ALA A 30 32.715 203.584 10.639 1.00 50.13 C
ANISOU 223 CA ALA A 30 6614 6839 5593 -1169 -225 -14 C
ATOM 224 C ALA A 30 32.553 204.352 11.945 1.00 50.40 C
ANISOU 224 C ALA A 30 6708 6822 5621 -1195 -220 -20 C
ATOM 225 O ALA A 30 32.807 205.561 12.003 1.00 45.93 O
ANISOU 225 O ALA A 30 6218 6222 5013 -1264 -225 -13 O
ATOM 226 CB ALA A 30 31.357 203.346 9.979 1.00 40.35 C
ANISOU 226 CB ALA A 30 5392 5530 4409 -1093 -228 -16 C
ATOM 227 N VAL A 31 32.129 203.664 13.008 1.00 61.37 N
ANISOU 227 N VAL A 31 8069 8203 7046 -1141 -209 -33 N
ATOM 228 CA VAL A 31 31.956 204.324 14.296 1.00 59.13 C
ANISOU 228 CA VAL A 31 7840 7872 6754 -1161 -203 -41 C
ATOM 229 C VAL A 31 33.297 204.795 14.846 1.00 58.71 C
ANISOU 229 C VAL A 31 7787 7884 6635 -1258 -205 -37 C
ATOM 230 O VAL A 31 33.374 205.833 15.513 1.00 55.23 O
ANISOU 230 O VAL A 31 7424 7398 6161 -1314 -206 -39 O
ATOM 231 CB VAL A 31 31.235 203.381 15.277 1.00 54.89 C
ANISOU 231 CB VAL A 31 7263 7322 6270 -1080 -191 -54 C
ATOM 232 CG1 VAL A 31 31.081 204.030 16.644 1.00 41.94 C
ANISOU 232 CG1 VAL A 31 5679 5637 4619 -1098 -183 -63 C
ATOM 233 CG2 VAL A 31 29.876 202.984 14.718 1.00 44.48 C
ANISOU 233 CG2 VAL A 31 5946 5943 5010 -995 -191 -54 C
ATOM 234 N TRP A 32 34.376 204.062 14.566 1.00 63.90 N
ANISOU 234 N TRP A 32 8361 8652 7267 -1280 -206 -30 N
ATOM 235 CA TRP A 32 35.683 204.458 15.079 1.00 68.41 C
ANISOU 235 CA TRP A 32 8919 9303 7771 -1375 -209 -21 C
ATOM 236 C TRP A 32 36.194 205.720 14.391 1.00 67.20 C
ANISOU 236 C TRP A 32 8835 9139 7560 -1474 -223 -7 C
ATOM 237 O TRP A 32 36.850 206.554 15.025 1.00 71.50 O
ANISOU 237 O TRP A 32 9423 9695 8049 -1566 -228 -3 O
ATOM 238 CB TRP A 32 36.680 203.312 14.909 1.00 69.29 C
ANISOU 238 CB TRP A 32 8917 9543 7868 -1362 -203 -11 C
ATOM 239 CG TRP A 32 38.092 203.672 15.271 1.00 88.75 C
ANISOU 239 CG TRP A 32 11353 12112 10257 -1461 -208 6 C
ATOM 240 CD1 TRP A 32 39.017 204.279 14.469 1.00 99.64 C
ANISOU 240 CD1 TRP A 32 12732 13552 11574 -1546 -219 27 C
ATOM 241 CD2 TRP A 32 38.744 203.437 16.526 1.00 98.66 C
ANISOU 241 CD2 TRP A 32 12571 13432 11485 -1488 -202 8 C
ATOM 242 NE1 TRP A 32 40.200 204.441 15.148 1.00103.10 N
ANISOU 242 NE1 TRP A 32 13134 14076 11965 -1600 -205 52 N
ATOM 243 CE2 TRP A 32 40.059 203.932 16.413 1.00110.51 C
ANISOU 243 CE2 TRP A 32 14049 15023 12919 -1572 -199 38 C
ATOM 244 CE3 TRP A 32 38.343 202.859 17.735 1.00 93.40 C
ANISOU 244 CE3 TRP A 32 11886 12750 10852 -1435 -191 -6 C
ATOM 245 CZ2 TRP A 32 40.976 203.865 17.463 1.00113.37 C
ANISOU 245 CZ2 TRP A 32 14369 15461 13245 -1606 -185 56 C
ATOM 246 CZ3 TRP A 32 39.255 202.794 18.776 1.00 92.82 C
ANISOU 246 CZ3 TRP A 32 11773 12763 10732 -1486 -189 3 C
ATOM 247 CH2 TRP A 32 40.555 203.293 18.633 1.00101.05 C
ANISOU 247 CH2 TRP A 32 12792 13892 11711 -1564 -182 36 C
ATOM 248 N LEU A 33 35.906 205.880 13.097 1.00 70.41 N
ANISOU 248 N LEU A 33 9254 9523 7975 -1462 -230 1 N
ATOM 249 CA LEU A 33 36.456 206.988 12.322 1.00 71.99 C
ANISOU 249 CA LEU A 33 9512 9723 8119 -1555 -242 17 C
ATOM 250 C LEU A 33 35.589 208.240 12.381 1.00 67.74 C
ANISOU 250 C LEU A 33 9102 9055 7582 -1571 -245 13 C
ATOM 251 O LEU A 33 36.114 209.353 12.493 1.00 76.81 O
ANISOU 251 O LEU A 33 10326 10185 8672 -1669 -252 21 O
ATOM 252 CB LEU A 33 36.650 206.564 10.863 1.00 79.62 C
ANISOU 252 CB LEU A 33 10429 10736 9088 -1536 -248 30 C
ATOM 253 CG LEU A 33 37.768 205.563 10.564 1.00 85.83 C
ANISOU 253 CG LEU A 33 11102 11660 9849 -1539 -244 42 C
ATOM 254 CD1 LEU A 33 37.815 205.250 9.076 1.00 87.02 C
ANISOU 254 CD1 LEU A 33 11222 11839 10003 -1516 -248 53 C
ATOM 255 CD2 LEU A 33 39.110 206.096 11.044 1.00 86.29 C
ANISOU 255 CD2 LEU A 33 11146 11802 9838 -1637 -242 64 C
ATOM 256 N ASN A 34 34.271 208.084 12.311 1.00 63.11 N
ANISOU 256 N ASN A 34 8543 8377 7057 -1476 -238 4 N
ATOM 257 CA ASN A 34 33.361 209.219 12.240 1.00 66.72 C
ANISOU 257 CA ASN A 34 9119 8713 7517 -1472 -236 5 C
ATOM 258 C ASN A 34 32.943 209.632 13.646 1.00 72.32 C
ANISOU 258 C ASN A 34 9891 9357 8229 -1466 -225 -9 C
ATOM 259 O ASN A 34 32.315 208.851 14.369 1.00 76.66 O
ANISOU 259 O ASN A 34 10399 9900 8828 -1387 -215 -22 O
ATOM 260 CB ASN A 34 32.138 208.871 11.394 1.00 70.45 C
ANISOU 260 CB ASN A 34 9585 9132 8050 -1372 -235 9 C
ATOM 261 CG ASN A 34 31.358 210.099 10.964 1.00 70.00 C
ANISOU 261 CG ASN A 34 9645 8968 7986 -1371 -234 21 C
ATOM 262 OD1 ASN A 34 31.579 211.201 11.469 1.00 70.85 O
ANISOU 262 OD1 ASN A 34 9851 9021 8049 -1433 -231 22 O
ATOM 263 ND2 ASN A 34 30.434 209.914 10.028 1.00 63.92 N
ANISOU 263 ND2 ASN A 34 8866 8165 7254 -1299 -236 31 N
ATOM 264 N SER A 35 33.283 210.866 14.028 1.00 81.35 N
ANISOU 264 N SER A 35 11142 10451 9317 -1551 -225 -8 N
ATOM 265 CA SER A 35 32.881 211.374 15.334 1.00 82.49 C
ANISOU 265 CA SER A 35 11363 10524 9456 -1549 -212 -23 C
ATOM 266 C SER A 35 31.389 211.670 15.401 1.00 79.99 C
ANISOU 266 C SER A 35 11113 10090 9187 -1445 -197 -25 C
ATOM 267 O SER A 35 30.821 211.683 16.499 1.00 81.71 O
ANISOU 267 O SER A 35 11363 10261 9423 -1403 -183 -38 O
ATOM 268 CB SER A 35 33.678 212.632 15.681 1.00 77.15 C
ANISOU 268 CB SER A 35 10794 9822 8698 -1676 -217 -21 C
ATOM 269 OG SER A 35 33.421 213.668 14.751 1.00 82.82 O
ANISOU 269 OG SER A 35 11610 10466 9392 -1701 -219 -7 O
ATOM 270 N ASN A 36 30.742 211.909 14.257 1.00 76.15 N
ANISOU 270 N ASN A 36 10648 9564 8723 -1402 -200 -9 N
ATOM 271 CA ASN A 36 29.298 212.109 14.245 1.00 77.36 C
ANISOU 271 CA ASN A 36 10849 9623 8922 -1296 -186 -4 C
ATOM 272 C ASN A 36 28.540 210.824 14.545 1.00 80.16 C
ANISOU 272 C ASN A 36 11099 10010 9346 -1192 -182 -11 C
ATOM 273 O ASN A 36 27.379 210.884 14.963 1.00 78.55 O
ANISOU 273 O ASN A 36 10925 9741 9179 -1105 -168 -9 O
ATOM 274 CB ASN A 36 28.855 212.671 12.895 1.00 82.00 C
ANISOU 274 CB ASN A 36 11478 10171 9509 -1280 -191 19 C
ATOM 275 CG ASN A 36 29.552 213.969 12.554 1.00 88.47 C
ANISOU 275 CG ASN A 36 12409 10950 10258 -1383 -195 29 C
ATOM 276 OD1 ASN A 36 29.950 214.723 13.441 1.00103.27 O
ANISOU 276 OD1 ASN A 36 14370 12783 12086 -1446 -187 18 O
ATOM 277 ND2 ASN A 36 29.705 214.237 11.262 1.00 88.07 N
ANISOU 277 ND2 ASN A 36 12359 10909 10194 -1405 -207 48 N
ATOM 278 N LEU A 37 29.167 209.669 14.335 1.00 75.25 N
ANISOU 278 N LEU A 37 10360 9491 8742 -1198 -192 -17 N
ATOM 279 CA LEU A 37 28.582 208.383 14.680 1.00 68.15 C
ANISOU 279 CA LEU A 37 9364 8625 7903 -1112 -189 -25 C
ATOM 280 C LEU A 37 28.956 207.925 16.083 1.00 67.89 C
ANISOU 280 C LEU A 37 9303 8622 7870 -1119 -180 -43 C
ATOM 281 O LEU A 37 28.534 206.841 16.498 1.00 67.24 O
ANISOU 281 O LEU A 37 9144 8569 7836 -1053 -175 -50 O
ATOM 282 CB LEU A 37 29.008 207.321 13.661 1.00 60.63 C
ANISOU 282 CB LEU A 37 8308 7761 6969 -1106 -201 -21 C
ATOM 283 CG LEU A 37 28.454 207.462 12.243 1.00 52.83 C
ANISOU 283 CG LEU A 37 7326 6754 5995 -1079 -211 -4 C
ATOM 284 CD1 LEU A 37 29.110 206.453 11.316 1.00 53.33 C
ANISOU 284 CD1 LEU A 37 7294 6908 6061 -1087 -222 -4 C
ATOM 285 CD2 LEU A 37 26.944 207.285 12.243 1.00 38.51 C
ANISOU 285 CD2 LEU A 37 5520 4879 4234 -979 -205 3 C
ATOM 286 N GLN A 38 29.732 208.716 16.822 1.00 59.21 N
ANISOU 286 N GLN A 38 8265 7516 6716 -1202 -178 -50 N
ATOM 287 CA GLN A 38 30.174 208.339 18.164 1.00 56.48 C
ANISOU 287 CA GLN A 38 7894 7205 6362 -1219 -170 -66 C
ATOM 288 C GLN A 38 29.187 208.900 19.178 1.00 60.36 C
ANISOU 288 C GLN A 38 8468 7600 6867 -1169 -153 -74 C
ATOM 289 O GLN A 38 29.356 209.999 19.705 1.00 82.27 O
ANISOU 289 O GLN A 38 11348 10316 9594 -1224 -147 -78 O
ATOM 290 CB GLN A 38 31.591 208.834 18.424 1.00 59.96 C
ANISOU 290 CB GLN A 38 8348 7703 6730 -1342 -179 -67 C
ATOM 291 CG GLN A 38 32.649 208.132 17.594 1.00 58.98 C
ANISOU 291 CG GLN A 38 8125 7694 6590 -1383 -193 -57 C
ATOM 292 CD GLN A 38 34.016 208.774 17.719 1.00 70.32 C
ANISOU 292 CD GLN A 38 9580 9192 7947 -1512 -204 -50 C
ATOM 293 OE1 GLN A 38 34.158 209.863 18.276 1.00 84.54 O
ANISOU 293 OE1 GLN A 38 11483 10939 9701 -1582 -203 -55 O
ATOM 294 NE2 GLN A 38 35.034 208.101 17.195 1.00 72.03 N
ANISOU 294 NE2 GLN A 38 9700 9526 8143 -1546 -213 -39 N
ATOM 295 N ASN A 39 28.137 208.131 19.453 1.00 50.64 N
ANISOU 295 N ASN A 39 7190 6353 5698 -1065 -144 -75 N
ATOM 296 CA ASN A 39 27.175 208.468 20.490 1.00 51.62 C
ANISOU 296 CA ASN A 39 7373 6402 5840 -1005 -125 -80 C
ATOM 297 C ASN A 39 26.828 207.198 21.250 1.00 58.60 C
ANISOU 297 C ASN A 39 8158 7332 6774 -939 -120 -89 C
ATOM 298 O ASN A 39 27.217 206.094 20.863 1.00 71.04 O
ANISOU 298 O ASN A 39 9631 8987 8374 -932 -130 -89 O
ATOM 299 CB ASN A 39 25.919 209.127 19.907 1.00 56.26 C
ANISOU 299 CB ASN A 39 8030 6900 6448 -933 -116 -63 C
ATOM 300 CG ASN A 39 25.371 208.377 18.712 1.00 61.89 C
ANISOU 300 CG ASN A 39 8664 7643 7207 -877 -127 -47 C
ATOM 301 OD1 ASN A 39 24.585 207.442 18.859 1.00 78.43 O
ANISOU 301 OD1 ASN A 39 10688 9757 9356 -798 -125 -45 O
ATOM 302 ND2 ASN A 39 25.783 208.786 17.518 1.00 59.01 N
ANISOU 302 ND2 ASN A 39 8316 7286 6820 -921 -141 -36 N
ATOM 303 N VAL A 40 26.090 207.365 22.349 1.00 63.51 N
ANISOU 303 N VAL A 40 8818 7903 7409 -889 -102 -95 N
ATOM 304 CA VAL A 40 25.758 206.222 23.197 1.00 52.01 C
ANISOU 304 CA VAL A 40 7276 6487 5997 -830 -96 -102 C
ATOM 305 C VAL A 40 24.991 205.173 22.404 1.00 52.57 C
ANISOU 305 C VAL A 40 7261 6584 6130 -754 -102 -89 C
ATOM 306 O VAL A 40 25.218 203.966 22.558 1.00 55.57 O
ANISOU 306 O VAL A 40 7546 7030 6539 -736 -106 -94 O
ATOM 307 CB VAL A 40 24.967 206.683 24.434 1.00 49.18 C
ANISOU 307 CB VAL A 40 6982 6063 5642 -783 -75 -107 C
ATOM 308 CG1 VAL A 40 24.466 205.482 25.210 1.00 39.92 C
ANISOU 308 CG1 VAL A 40 5719 4929 4521 -715 -69 -110 C
ATOM 309 CG2 VAL A 40 25.831 207.569 25.318 1.00 60.76 C
ANISOU 309 CG2 VAL A 40 8530 7512 7044 -868 -70 -124 C
ATOM 310 N THR A 41 24.083 205.616 21.531 1.00 44.26 N
ANISOU 310 N THR A 41 6243 5481 5093 -710 -103 -72 N
ATOM 311 CA THR A 41 23.249 204.677 20.788 1.00 42.38 C
ANISOU 311 CA THR A 41 5930 5265 4908 -642 -111 -59 C
ATOM 312 C THR A 41 24.093 203.759 19.913 1.00 45.93 C
ANISOU 312 C THR A 41 6297 5792 5361 -679 -128 -63 C
ATOM 313 O THR A 41 23.826 202.555 19.825 1.00 50.98 O
ANISOU 313 O THR A 41 6854 6474 6041 -639 -131 -64 O
ATOM 314 CB THR A 41 22.233 205.441 19.938 1.00 45.41 C
ANISOU 314 CB THR A 41 6368 5588 5297 -597 -110 -35 C
ATOM 315 OG1 THR A 41 21.733 206.561 20.681 1.00 58.29 O
ANISOU 315 OG1 THR A 41 8100 7142 6906 -576 -90 -31 O
ATOM 316 CG2 THR A 41 21.072 204.535 19.557 1.00 49.90 C
ANISOU 316 CG2 THR A 41 6865 6172 5921 -516 -114 -19 C
ATOM 317 N ASN A 42 25.125 204.307 19.270 1.00 46.36 N
ANISOU 317 N ASN A 42 6377 5866 5372 -756 -137 -65 N
ATOM 318 CA ASN A 42 25.972 203.520 18.384 1.00 49.60 C
ANISOU 318 CA ASN A 42 6715 6352 5778 -789 -151 -67 C
ATOM 319 C ASN A 42 26.987 202.665 19.133 1.00 47.12 C
ANISOU 319 C ASN A 42 6335 6114 5455 -817 -148 -81 C
ATOM 320 O ASN A 42 27.545 201.735 18.540 1.00 56.72 O
ANISOU 320 O ASN A 42 7478 7396 6676 -819 -154 -82 O
ATOM 321 CB ASN A 42 26.696 204.438 17.395 1.00 60.33 C
ANISOU 321 CB ASN A 42 8123 7711 7090 -861 -162 -60 C
ATOM 322 CG ASN A 42 25.756 205.049 16.367 1.00 55.76 C
ANISOU 322 CG ASN A 42 7591 7073 6523 -827 -166 -42 C
ATOM 323 OD1 ASN A 42 24.667 204.531 16.121 1.00 55.14 O
ANISOU 323 OD1 ASN A 42 7484 6978 6490 -753 -166 -33 O
ATOM 324 ND2 ASN A 42 26.179 206.151 15.757 1.00 63.17 N
ANISOU 324 ND2 ASN A 42 8601 7983 7417 -885 -171 -34 N
ATOM 325 N TYR A 43 27.246 202.952 20.411 1.00 40.94 N
ANISOU 325 N TYR A 43 5575 5324 4655 -835 -138 -91 N
ATOM 326 CA TYR A 43 28.127 202.079 21.182 1.00 41.42 C
ANISOU 326 CA TYR A 43 5566 5462 4709 -852 -134 -100 C
ATOM 327 C TYR A 43 27.484 200.715 21.394 1.00 41.89 C
ANISOU 327 C TYR A 43 5549 5541 4825 -771 -128 -101 C
ATOM 328 O TYR A 43 28.168 199.686 21.354 1.00 46.98 O
ANISOU 328 O TYR A 43 6120 6258 5473 -769 -128 -103 O
ATOM 329 CB TYR A 43 28.484 202.724 22.521 1.00 35.88 C
ANISOU 329 CB TYR A 43 4911 4748 3974 -891 -125 -109 C
ATOM 330 CG TYR A 43 29.172 204.064 22.388 1.00 58.01 C
ANISOU 330 CG TYR A 43 7799 7530 6713 -982 -131 -109 C
ATOM 331 CD1 TYR A 43 29.868 204.398 21.233 1.00 67.87 C
ANISOU 331 CD1 TYR A 43 9049 8808 7930 -1039 -144 -100 C
ATOM 332 CD2 TYR A 43 29.123 204.998 23.416 1.00 66.68 C
ANISOU 332 CD2 TYR A 43 8979 8576 7779 -1014 -122 -118 C
ATOM 333 CE1 TYR A 43 30.493 205.625 21.102 1.00 77.22 C
ANISOU 333 CE1 TYR A 43 10315 9972 9054 -1129 -150 -98 C
ATOM 334 CE2 TYR A 43 29.748 206.229 23.295 1.00 74.22 C
ANISOU 334 CE2 TYR A 43 10024 9507 8671 -1105 -128 -118 C
ATOM 335 CZ TYR A 43 30.433 206.536 22.135 1.00 81.54 C
ANISOU 335 CZ TYR A 43 10950 10465 9568 -1165 -142 -107 C
ATOM 336 OH TYR A 43 31.059 207.757 22.003 1.00 78.56 O
ANISOU 336 OH TYR A 43 10663 10062 9125 -1262 -148 -106 O
ATOM 337 N PHE A 44 26.167 200.686 21.615 1.00 25.72 N
ANISOU 337 N PHE A 44 3520 3432 2821 -703 -123 -98 N
ATOM 338 CA PHE A 44 25.456 199.413 21.637 1.00 29.88 C
ANISOU 338 CA PHE A 44 3979 3974 3401 -634 -121 -97 C
ATOM 339 C PHE A 44 25.423 198.786 20.250 1.00 40.66 C
ANISOU 339 C PHE A 44 5306 5363 4779 -625 -133 -91 C
ATOM 340 O PHE A 44 25.469 197.557 20.117 1.00 43.75 O
ANISOU 340 O PHE A 44 5633 5793 5195 -596 -132 -94 O
ATOM 341 CB PHE A 44 24.040 199.607 22.177 1.00 33.70 C
ANISOU 341 CB PHE A 44 4490 4394 3921 -569 -114 -89 C
ATOM 342 CG PHE A 44 23.995 200.053 23.610 1.00 48.04 C
ANISOU 342 CG PHE A 44 6339 6186 5726 -566 -99 -97 C
ATOM 343 CD1 PHE A 44 24.280 199.162 24.635 1.00 45.45 C
ANISOU 343 CD1 PHE A 44 5958 5899 5411 -552 -90 -105 C
ATOM 344 CD2 PHE A 44 23.683 201.365 23.933 1.00 35.46 C
ANISOU 344 CD2 PHE A 44 4835 4530 4107 -577 -92 -95 C
ATOM 345 CE1 PHE A 44 24.249 199.568 25.957 1.00 52.78 C
ANISOU 345 CE1 PHE A 44 6917 6809 6328 -552 -77 -112 C
ATOM 346 CE2 PHE A 44 23.649 201.780 25.252 1.00 38.20 C
ANISOU 346 CE2 PHE A 44 5220 4853 4440 -576 -77 -103 C
ATOM 347 CZ PHE A 44 23.932 200.881 26.267 1.00 51.83 C
ANISOU 347 CZ PHE A 44 6888 6625 6180 -565 -71 -112 C
ATOM 348 N VAL A 45 25.338 199.616 19.207 1.00 36.98 N
ANISOU 348 N VAL A 45 4884 4871 4296 -650 -143 -82 N
ATOM 349 CA VAL A 45 25.429 199.117 17.837 1.00 35.72 C
ANISOU 349 CA VAL A 45 4694 4738 4141 -651 -155 -77 C
ATOM 350 C VAL A 45 26.762 198.416 17.618 1.00 44.87 C
ANISOU 350 C VAL A 45 5800 5975 5273 -687 -155 -85 C
ATOM 351 O VAL A 45 26.821 197.333 17.023 1.00 51.99 O
ANISOU 351 O VAL A 45 6650 6912 6192 -662 -156 -87 O
ATOM 352 CB VAL A 45 25.224 200.270 16.836 1.00 31.37 C
ANISOU 352 CB VAL A 45 4204 4147 3568 -678 -166 -65 C
ATOM 353 CG1 VAL A 45 25.549 199.816 15.420 1.00 37.24 C
ANISOU 353 CG1 VAL A 45 4916 4928 4306 -691 -178 -62 C
ATOM 354 CG2 VAL A 45 23.804 200.802 16.923 1.00 36.68 C
ANISOU 354 CG2 VAL A 45 4919 4751 4269 -624 -164 -51 C
ATOM 355 N VAL A 46 27.852 199.019 18.098 1.00 37.58 N
ANISOU 355 N VAL A 46 4891 5083 4304 -747 -151 -88 N
ATOM 356 CA VAL A 46 29.160 198.382 17.991 1.00 35.26 C
ANISOU 356 CA VAL A 46 4541 4876 3979 -779 -148 -90 C
ATOM 357 C VAL A 46 29.207 197.115 18.837 1.00 33.61 C
ANISOU 357 C VAL A 46 4270 4703 3796 -730 -135 -96 C
ATOM 358 O VAL A 46 29.778 196.099 18.424 1.00 43.91 O
ANISOU 358 O VAL A 46 5519 6066 5099 -712 -130 -96 O
ATOM 359 CB VAL A 46 30.271 199.375 18.378 1.00 31.29 C
ANISOU 359 CB VAL A 46 4067 4405 3417 -862 -150 -87 C
ATOM 360 CG1 VAL A 46 31.619 198.672 18.460 1.00 34.07 C
ANISOU 360 CG1 VAL A 46 4350 4862 3734 -888 -144 -83 C
ATOM 361 CG2 VAL A 46 30.327 200.504 17.369 1.00 30.58 C
ANISOU 361 CG2 VAL A 46 4037 4284 3297 -912 -163 -79 C
ATOM 362 N SER A 47 28.604 197.150 20.029 1.00 36.14 N
ANISOU 362 N SER A 47 4602 4988 4139 -703 -127 -101 N
ATOM 363 CA SER A 47 28.476 195.931 20.823 1.00 45.34 C
ANISOU 363 CA SER A 47 5713 6178 5335 -651 -115 -105 C
ATOM 364 C SER A 47 27.670 194.877 20.075 1.00 37.34 C
ANISOU 364 C SER A 47 4673 5149 4365 -593 -116 -106 C
ATOM 365 O SER A 47 27.971 193.680 20.151 1.00 50.02 O
ANISOU 365 O SER A 47 6229 6793 5981 -561 -106 -108 O
ATOM 366 CB SER A 47 27.828 196.243 22.171 1.00 42.61 C
ANISOU 366 CB SER A 47 5391 5791 5007 -632 -107 -109 C
ATOM 367 OG SER A 47 27.706 195.070 22.959 1.00 33.48 O
ANISOU 367 OG SER A 47 4184 4659 3880 -583 -95 -112 O
ATOM 368 N LEU A 48 26.645 195.308 19.337 1.00 32.74 N
ANISOU 368 N LEU A 48 4126 4509 3805 -580 -128 -101 N
ATOM 369 CA LEU A 48 25.856 194.378 18.538 1.00 30.22 C
ANISOU 369 CA LEU A 48 3785 4177 3521 -537 -133 -100 C
ATOM 370 C LEU A 48 26.652 193.865 17.344 1.00 33.64 C
ANISOU 370 C LEU A 48 4196 4656 3931 -553 -136 -102 C
ATOM 371 O LEU A 48 26.558 192.685 16.988 1.00 49.34 O
ANISOU 371 O LEU A 48 6152 6659 5935 -520 -132 -107 O
ATOM 372 CB LEU A 48 24.565 195.058 18.084 1.00 34.20 C
ANISOU 372 CB LEU A 48 4328 4618 4048 -521 -146 -91 C
ATOM 373 CG LEU A 48 23.554 194.206 17.319 1.00 43.07 C
ANISOU 373 CG LEU A 48 5432 5726 5206 -483 -155 -86 C
ATOM 374 CD1 LEU A 48 23.235 192.945 18.093 1.00 39.66 C
ANISOU 374 CD1 LEU A 48 4960 5304 4805 -443 -145 -91 C
ATOM 375 CD2 LEU A 48 22.287 195.002 17.052 1.00 54.20 C
ANISOU 375 CD2 LEU A 48 6876 7085 6633 -466 -165 -69 C
ATOM 376 N ALA A 49 27.441 194.736 16.713 1.00 38.95 N
ANISOU 376 N ALA A 49 4887 5348 4562 -605 -142 -98 N
ATOM 377 CA ALA A 49 28.302 194.287 15.626 1.00 39.88 C
ANISOU 377 CA ALA A 49 4981 5518 4652 -620 -143 -98 C
ATOM 378 C ALA A 49 29.433 193.405 16.138 1.00 43.36 C
ANISOU 378 C ALA A 49 5371 6032 5072 -612 -125 -101 C
ATOM 379 O ALA A 49 29.868 192.488 15.434 1.00 52.17 O
ANISOU 379 O ALA A 49 6458 7185 6179 -591 -117 -102 O
ATOM 380 CB ALA A 49 28.865 195.488 14.868 1.00 31.65 C
ANISOU 380 CB ALA A 49 3972 4484 3569 -681 -154 -91 C
ATOM 381 N ALA A 50 29.921 193.667 17.353 1.00 47.96 N
ANISOU 381 N ALA A 50 5945 6637 5642 -626 -116 -99 N
ATOM 382 CA ALA A 50 30.960 192.819 17.927 1.00 41.59 C
ANISOU 382 CA ALA A 50 5085 5905 4813 -613 -98 -97 C
ATOM 383 C ALA A 50 30.466 191.389 18.103 1.00 52.57 C
ANISOU 383 C ALA A 50 6448 7285 6241 -542 -84 -103 C
ATOM 384 O ALA A 50 31.195 190.432 17.817 1.00 46.08 O
ANISOU 384 O ALA A 50 5590 6516 5402 -515 -68 -100 O
ATOM 385 CB ALA A 50 31.425 193.392 19.264 1.00 23.67 C
ANISOU 385 CB ALA A 50 2812 3657 2524 -643 -93 -94 C
ATOM 386 N ALA A 51 29.226 191.226 18.572 1.00 46.76 N
ANISOU 386 N ALA A 51 5731 6482 5553 -511 -88 -109 N
ATOM 387 CA ALA A 51 28.661 189.890 18.719 1.00 39.60 C
ANISOU 387 CA ALA A 51 4806 5558 4681 -452 -78 -114 C
ATOM 388 C ALA A 51 28.513 189.203 17.367 1.00 42.25 C
ANISOU 388 C ALA A 51 5148 5889 5018 -437 -81 -119 C
ATOM 389 O ALA A 51 28.780 188.002 17.240 1.00 55.36 O
ANISOU 389 O ALA A 51 6790 7568 6678 -398 -65 -122 O
ATOM 390 CB ALA A 51 27.311 189.967 19.433 1.00 28.07 C
ANISOU 390 CB ALA A 51 3365 4032 3268 -431 -85 -116 C
ATOM 391 N ASP A 52 28.097 189.951 16.342 1.00 38.90 N
ANISOU 391 N ASP A 52 4753 5438 4591 -467 -100 -118 N
ATOM 392 CA ASP A 52 27.907 189.353 15.025 1.00 41.01 C
ANISOU 392 CA ASP A 52 5028 5699 4856 -457 -105 -123 C
ATOM 393 C ASP A 52 29.236 189.012 14.362 1.00 39.21 C
ANISOU 393 C ASP A 52 4779 5537 4580 -461 -91 -121 C
ATOM 394 O ASP A 52 29.322 188.021 13.627 1.00 24.92 O
ANISOU 394 O ASP A 52 2970 3734 2766 -432 -82 -128 O
ATOM 395 CB ASP A 52 27.080 190.287 14.141 1.00 31.00 C
ANISOU 395 CB ASP A 52 3795 4388 3596 -486 -129 -119 C
ATOM 396 CG ASP A 52 25.639 190.401 14.607 1.00 60.96 C
ANISOU 396 CG ASP A 52 7605 8122 7436 -468 -141 -116 C
ATOM 397 OD1 ASP A 52 25.140 189.445 15.238 1.00 69.16 O
ANISOU 397 OD1 ASP A 52 8629 9147 8501 -433 -133 -120 O
ATOM 398 OD2 ASP A 52 25.004 191.444 14.342 1.00 67.62 O
ANISOU 398 OD2 ASP A 52 8475 8933 8284 -488 -157 -107 O
ATOM 399 N ILE A 53 30.280 189.809 14.608 1.00 39.16 N
ANISOU 399 N ILE A 53 4758 5585 4536 -498 -88 -112 N
ATOM 400 CA ILE A 53 31.611 189.440 14.131 1.00 33.94 C
ANISOU 400 CA ILE A 53 4066 5003 3826 -497 -71 -105 C
ATOM 401 C ILE A 53 32.039 188.114 14.745 1.00 38.43 C
ANISOU 401 C ILE A 53 4603 5603 4395 -438 -44 -105 C
ATOM 402 O ILE A 53 32.542 187.224 14.048 1.00 31.36 O
ANISOU 402 O ILE A 53 3700 4738 3479 -403 -26 -106 O
ATOM 403 CB ILE A 53 32.626 190.559 14.433 1.00 38.91 C
ANISOU 403 CB ILE A 53 4681 5691 4412 -556 -75 -91 C
ATOM 404 CG1 ILE A 53 32.357 191.785 13.563 1.00 38.97 C
ANISOU 404 CG1 ILE A 53 4727 5670 4410 -613 -99 -89 C
ATOM 405 CG2 ILE A 53 34.052 190.068 14.208 1.00 31.75 C
ANISOU 405 CG2 ILE A 53 3727 4884 3452 -548 -54 -77 C
ATOM 406 CD1 ILE A 53 33.247 192.969 13.889 1.00 48.73 C
ANISOU 406 CD1 ILE A 53 5962 6952 5602 -682 -106 -76 C
ATOM 407 N LEU A 54 31.829 187.955 16.057 1.00 41.54 N
ANISOU 407 N LEU A 54 4985 5989 4811 -422 -37 -105 N
ATOM 408 CA LEU A 54 32.176 186.714 16.743 1.00 49.18 C
ANISOU 408 CA LEU A 54 5925 6981 5780 -363 -10 -102 C
ATOM 409 C LEU A 54 31.338 185.531 16.274 1.00 52.41 C
ANISOU 409 C LEU A 54 6360 7332 6220 -313 -3 -116 C
ATOM 410 O LEU A 54 31.752 184.382 16.466 1.00 45.01 O
ANISOU 410 O LEU A 54 5412 6414 5274 -260 23 -114 O
ATOM 411 CB LEU A 54 32.029 186.889 18.256 1.00 39.99 C
ANISOU 411 CB LEU A 54 4744 5816 4635 -362 -7 -99 C
ATOM 412 CG LEU A 54 33.098 187.753 18.928 1.00 41.80 C
ANISOU 412 CG LEU A 54 4941 6119 4821 -405 -6 -84 C
ATOM 413 CD1 LEU A 54 32.765 188.015 20.393 1.00 31.34 C
ANISOU 413 CD1 LEU A 54 3611 4780 3518 -409 -7 -83 C
ATOM 414 CD2 LEU A 54 34.456 187.088 18.798 1.00 41.85 C
ANISOU 414 CD2 LEU A 54 4900 6224 4778 -379 19 -66 C
ATOM 415 N VAL A 55 30.171 185.779 15.676 1.00 40.65 N
ANISOU 415 N VAL A 55 4908 5772 4763 -331 -26 -127 N
ATOM 416 CA VAL A 55 29.404 184.691 15.076 1.00 43.26 C
ANISOU 416 CA VAL A 55 5268 6053 5115 -298 -24 -139 C
ATOM 417 C VAL A 55 30.181 184.079 13.917 1.00 43.97 C
ANISOU 417 C VAL A 55 5366 6176 5165 -280 -8 -142 C
ATOM 418 O VAL A 55 30.298 182.853 13.799 1.00 41.57 O
ANISOU 418 O VAL A 55 5075 5864 4855 -232 14 -148 O
ATOM 419 CB VAL A 55 28.019 185.188 14.626 1.00 37.82 C
ANISOU 419 CB VAL A 55 4611 5297 4463 -327 -54 -145 C
ATOM 420 CG1 VAL A 55 27.374 184.186 13.681 1.00 31.01 C
ANISOU 420 CG1 VAL A 55 3781 4395 3607 -312 -56 -157 C
ATOM 421 CG2 VAL A 55 27.127 185.436 15.832 1.00 27.96 C
ANISOU 421 CG2 VAL A 55 3357 4011 3255 -326 -62 -141 C
ATOM 422 N GLY A 56 30.736 184.925 13.050 1.00 34.19 N
ANISOU 422 N GLY A 56 4124 4973 3896 -317 -19 -137 N
ATOM 423 CA GLY A 56 31.488 184.413 11.918 1.00 42.60 C
ANISOU 423 CA GLY A 56 5195 6074 4919 -299 -3 -139 C
ATOM 424 C GLY A 56 32.823 183.815 12.319 1.00 46.26 C
ANISOU 424 C GLY A 56 5622 6615 5340 -255 32 -125 C
ATOM 425 O GLY A 56 33.256 182.807 11.754 1.00 56.13 O
ANISOU 425 O GLY A 56 6884 7877 6564 -206 57 -128 O
ATOM 426 N VAL A 57 33.491 184.418 13.301 1.00 46.48 N
ANISOU 426 N VAL A 57 5606 6698 5357 -270 35 -109 N
ATOM 427 CA VAL A 57 34.830 183.967 13.670 1.00 41.32 C
ANISOU 427 CA VAL A 57 4907 6137 4656 -233 67 -89 C
ATOM 428 C VAL A 57 34.773 182.684 14.495 1.00 36.25 C
ANISOU 428 C VAL A 57 4265 5480 4027 -161 96 -89 C
ATOM 429 O VAL A 57 35.629 181.804 14.348 1.00 50.34 O
ANISOU 429 O VAL A 57 6037 7317 5775 -101 130 -78 O
ATOM 430 CB VAL A 57 35.574 185.094 14.412 1.00 45.13 C
ANISOU 430 CB VAL A 57 5344 6689 5116 -285 57 -70 C
ATOM 431 CG1 VAL A 57 36.933 184.614 14.909 1.00 48.13 C
ANISOU 431 CG1 VAL A 57 5666 7176 5444 -248 89 -44 C
ATOM 432 CG2 VAL A 57 35.736 186.306 13.505 1.00 31.38 C
ANISOU 432 CG2 VAL A 57 3609 4962 3353 -356 31 -67 C
ATOM 433 N LEU A 58 33.767 182.542 15.362 1.00 38.21 N
ANISOU 433 N LEU A 58 4530 5662 4326 -161 85 -100 N
ATOM 434 CA LEU A 58 33.749 181.430 16.308 1.00 35.20 C
ANISOU 434 CA LEU A 58 4145 5271 3957 -99 112 -97 C
ATOM 435 C LEU A 58 32.477 180.592 16.225 1.00 39.06 C
ANISOU 435 C LEU A 58 4689 5660 4492 -80 108 -117 C
ATOM 436 O LEU A 58 32.551 179.364 16.116 1.00 46.67 O
ANISOU 436 O LEU A 58 5679 6605 5448 -22 135 -121 O
ATOM 437 CB LEU A 58 33.934 181.949 17.737 1.00 26.49 C
ANISOU 437 CB LEU A 58 3000 4202 2865 -114 109 -83 C
ATOM 438 CG LEU A 58 35.321 182.499 18.070 1.00 36.26 C
ANISOU 438 CG LEU A 58 4177 5552 4049 -126 120 -58 C
ATOM 439 CD1 LEU A 58 35.345 183.052 19.483 1.00 24.43 C
ANISOU 439 CD1 LEU A 58 2645 4074 2562 -152 113 -48 C
ATOM 440 CD2 LEU A 58 36.376 181.418 17.895 1.00 40.92 C
ANISOU 440 CD2 LEU A 58 4745 6210 4594 -52 162 -39 C
ATOM 441 N ALA A 59 31.308 181.238 16.274 1.00 43.21 N
ANISOU 441 N ALA A 59 5233 6123 5061 -128 74 -129 N
ATOM 442 CA ALA A 59 30.055 180.495 16.394 1.00 40.56 C
ANISOU 442 CA ALA A 59 4939 5704 4769 -118 67 -143 C
ATOM 443 C ALA A 59 29.811 179.604 15.181 1.00 45.77 C
ANISOU 443 C ALA A 59 5651 6325 5415 -101 73 -158 C
ATOM 444 O ALA A 59 29.466 178.426 15.324 1.00 35.51 O
ANISOU 444 O ALA A 59 4387 4984 4123 -64 91 -165 O
ATOM 445 CB ALA A 59 28.884 181.458 16.596 1.00 47.04 C
ANISOU 445 CB ALA A 59 5764 6479 5632 -171 30 -147 C
ATOM 446 N ILE A 60 29.974 180.149 13.979 1.00 52.28 N
ANISOU 446 N ILE A 60 6486 7161 6218 -132 60 -163 N
ATOM 447 CA ILE A 60 29.728 179.387 12.755 1.00 51.59 C
ANISOU 447 CA ILE A 60 6452 7038 6113 -122 64 -179 C
ATOM 448 C ILE A 60 30.745 178.255 12.621 1.00 48.16 C
ANISOU 448 C ILE A 60 6031 6631 5635 -53 108 -177 C
ATOM 449 O ILE A 60 30.348 177.128 12.291 1.00 43.21 O
ANISOU 449 O ILE A 60 5462 5951 5006 -25 122 -190 O
ATOM 450 CB ILE A 60 29.723 180.301 11.517 1.00 40.84 C
ANISOU 450 CB ILE A 60 5094 5688 4735 -170 39 -182 C
ATOM 451 CG1 ILE A 60 28.479 181.194 11.528 1.00 38.39 C
ANISOU 451 CG1 ILE A 60 4785 5333 4467 -228 -2 -184 C
ATOM 452 CG2 ILE A 60 29.796 179.476 10.240 1.00 31.95 C
ANISOU 452 CG2 ILE A 60 4020 4543 3578 -154 50 -197 C
ATOM 453 CD1 ILE A 60 28.368 182.111 10.328 1.00 26.95 C
ANISOU 453 CD1 ILE A 60 3344 3892 3005 -275 -27 -185 C
ATOM 454 N PRO A 61 32.047 178.479 12.856 1.00 45.85 N
ANISOU 454 N PRO A 61 5693 6422 5305 -24 132 -158 N
ATOM 455 CA PRO A 61 32.963 177.328 12.927 1.00 46.84 C
ANISOU 455 CA PRO A 61 5829 6577 5390 57 179 -150 C
ATOM 456 C PRO A 61 32.586 176.327 14.004 1.00 50.09 C
ANISOU 456 C PRO A 61 6259 6946 5826 102 199 -150 C
ATOM 457 O PRO A 61 32.824 175.125 13.829 1.00 49.03 O
ANISOU 457 O PRO A 61 6171 6789 5668 164 234 -153 O
ATOM 458 CB PRO A 61 34.323 177.979 13.211 1.00 44.36 C
ANISOU 458 CB PRO A 61 5445 6375 5036 68 194 -123 C
ATOM 459 CG PRO A 61 34.212 179.326 12.614 1.00 39.67 C
ANISOU 459 CG PRO A 61 4828 5800 4444 -9 157 -125 C
ATOM 460 CD PRO A 61 32.793 179.753 12.864 1.00 37.95 C
ANISOU 460 CD PRO A 61 4635 5498 4285 -62 119 -142 C
ATOM 461 N PHE A 62 32.003 176.783 15.116 1.00 39.18 N
ANISOU 461 N PHE A 62 4847 5552 4489 73 179 -145 N
ATOM 462 CA PHE A 62 31.517 175.846 16.124 1.00 31.21 C
ANISOU 462 CA PHE A 62 3857 4496 3505 110 195 -145 C
ATOM 463 C PHE A 62 30.329 175.048 15.601 1.00 42.78 C
ANISOU 463 C PHE A 62 5397 5862 4993 96 184 -167 C
ATOM 464 O PHE A 62 30.198 173.854 15.895 1.00 44.22 O
ANISOU 464 O PHE A 62 5627 6002 5174 142 211 -170 O
ATOM 465 CB PHE A 62 31.133 176.585 17.407 1.00 29.95 C
ANISOU 465 CB PHE A 62 3647 4347 3385 79 174 -135 C
ATOM 466 CG PHE A 62 32.307 177.097 18.198 1.00 41.85 C
ANISOU 466 CG PHE A 62 5085 5949 4866 97 190 -110 C
ATOM 467 CD1 PHE A 62 33.608 176.880 17.769 1.00 53.90 C
ANISOU 467 CD1 PHE A 62 6590 7553 6336 140 220 -95 C
ATOM 468 CD2 PHE A 62 32.105 177.788 19.384 1.00 48.25 C
ANISOU 468 CD2 PHE A 62 5853 6778 5704 70 175 -101 C
ATOM 469 CE1 PHE A 62 34.686 177.354 18.503 1.00 42.65 C
ANISOU 469 CE1 PHE A 62 5096 6228 4882 150 232 -68 C
ATOM 470 CE2 PHE A 62 33.177 178.261 20.124 1.00 35.99 C
ANISOU 470 CE2 PHE A 62 4237 5315 4121 77 187 -79 C
ATOM 471 CZ PHE A 62 34.469 178.044 19.682 1.00 45.58 C
ANISOU 471 CZ PHE A 62 5427 6613 5280 115 214 -61 C
ATOM 472 N ALA A 63 29.449 175.695 14.828 1.00 35.46 N
ANISOU 472 N ALA A 63 4486 4899 4087 30 146 -182 N
ATOM 473 CA ALA A 63 28.290 175.000 14.275 1.00 30.36 C
ANISOU 473 CA ALA A 63 3907 4170 3458 6 131 -201 C
ATOM 474 C ALA A 63 28.712 173.956 13.250 1.00 45.60 C
ANISOU 474 C ALA A 63 5906 6076 5343 42 159 -214 C
ATOM 475 O ALA A 63 28.122 172.871 13.182 1.00 32.18 O
ANISOU 475 O ALA A 63 4275 4309 3645 52 169 -227 O
ATOM 476 CB ALA A 63 27.321 176.006 13.653 1.00 40.32 C
ANISOU 476 CB ALA A 63 5161 5413 4746 -70 84 -207 C
ATOM 477 N ILE A 64 29.730 174.266 12.445 1.00 52.64 N
ANISOU 477 N ILE A 64 6787 7023 6192 62 174 -212 N
ATOM 478 CA ILE A 64 30.259 173.289 11.498 1.00 51.33 C
ANISOU 478 CA ILE A 64 6686 6841 5975 109 207 -223 C
ATOM 479 C ILE A 64 30.863 172.105 12.241 1.00 48.36 C
ANISOU 479 C ILE A 64 6336 6458 5579 194 257 -214 C
ATOM 480 O ILE A 64 30.696 170.947 11.840 1.00 50.35 O
ANISOU 480 O ILE A 64 6674 6648 5809 226 281 -229 O
ATOM 481 CB ILE A 64 31.286 173.956 10.563 1.00 43.36 C
ANISOU 481 CB ILE A 64 5648 5906 4923 116 214 -217 C
ATOM 482 CG1 ILE A 64 30.608 175.010 9.685 1.00 43.59 C
ANISOU 482 CG1 ILE A 64 5667 5928 4969 34 166 -228 C
ATOM 483 CG2 ILE A 64 32.005 172.915 9.712 1.00 33.14 C
ANISOU 483 CG2 ILE A 64 4417 4606 3570 182 257 -225 C
ATOM 484 CD1 ILE A 64 31.572 175.777 8.805 1.00 44.79 C
ANISOU 484 CD1 ILE A 64 5785 6153 5080 31 169 -220 C
ATOM 485 N THR A 65 31.564 172.377 13.345 1.00 52.83 N
ANISOU 485 N THR A 65 6834 7088 6150 230 273 -189 N
ATOM 486 CA THR A 65 32.245 171.312 14.074 1.00 47.87 C
ANISOU 486 CA THR A 65 6222 6467 5498 318 322 -175 C
ATOM 487 C THR A 65 31.252 170.384 14.763 1.00 49.94 C
ANISOU 487 C THR A 65 6542 6638 5793 317 323 -184 C
ATOM 488 O THR A 65 31.396 169.157 14.702 1.00 57.68 O
ANISOU 488 O THR A 65 7597 7572 6748 377 362 -188 O
ATOM 489 CB THR A 65 33.213 171.913 15.094 1.00 50.14 C
ANISOU 489 CB THR A 65 6415 6855 5781 348 334 -143 C
ATOM 490 OG1 THR A 65 34.158 172.755 14.423 1.00 65.79 O
ANISOU 490 OG1 THR A 65 8345 8926 7726 341 333 -132 O
ATOM 491 CG2 THR A 65 33.959 170.816 15.824 1.00 50.98 C
ANISOU 491 CG2 THR A 65 6533 6978 5859 446 388 -123 C
ATOM 492 N ILE A 66 30.235 170.947 15.421 1.00 59.24 N
ANISOU 492 N ILE A 66 7690 7791 7027 252 283 -187 N
ATOM 493 CA ILE A 66 29.279 170.125 16.162 1.00 48.92 C
ANISOU 493 CA ILE A 66 6427 6407 5752 246 281 -192 C
ATOM 494 C ILE A 66 28.304 169.390 15.256 1.00 49.22 C
ANISOU 494 C ILE A 66 6562 6353 5788 207 269 -217 C
ATOM 495 O ILE A 66 27.603 168.484 15.723 1.00 49.95 O
ANISOU 495 O ILE A 66 6708 6377 5894 205 274 -222 O
ATOM 496 CB ILE A 66 28.505 170.985 17.180 1.00 37.34 C
ANISOU 496 CB ILE A 66 4894 4950 4342 192 244 -183 C
ATOM 497 CG1 ILE A 66 27.973 170.112 18.319 1.00 44.21 C
ANISOU 497 CG1 ILE A 66 5786 5774 5238 214 257 -176 C
ATOM 498 CG2 ILE A 66 27.370 171.740 16.496 1.00 26.28 C
ANISOU 498 CG2 ILE A 66 3496 3517 2971 104 193 -198 C
ATOM 499 CD1 ILE A 66 27.330 170.891 19.438 1.00 54.38 C
ANISOU 499 CD1 ILE A 66 7006 7078 6576 175 227 -164 C
ATOM 500 N SER A 67 28.239 169.745 13.972 1.00 57.89 N
ANISOU 500 N SER A 67 7682 7448 6864 171 252 -234 N
ATOM 501 CA SER A 67 27.389 169.017 13.039 1.00 50.85 C
ANISOU 501 CA SER A 67 6886 6475 5961 130 241 -259 C
ATOM 502 C SER A 67 27.999 167.696 12.597 1.00 51.21 C
ANISOU 502 C SER A 67 7029 6476 5953 199 292 -269 C
ATOM 503 O SER A 67 27.297 166.882 11.987 1.00 54.92 O
ANISOU 503 O SER A 67 7594 6866 6408 169 289 -290 O
ATOM 504 CB SER A 67 27.091 169.874 11.807 1.00 59.14 C
ANISOU 504 CB SER A 67 7926 7539 7005 67 204 -272 C
ATOM 505 OG SER A 67 28.261 170.079 11.036 1.00 63.20 O
ANISOU 505 OG SER A 67 8434 8105 7472 113 230 -272 O
ATOM 506 N THR A 68 29.281 167.465 12.881 1.00 53.90 N
ANISOU 506 N THR A 68 7351 6870 6260 291 339 -252 N
ATOM 507 CA THR A 68 29.930 166.212 12.521 1.00 59.76 C
ANISOU 507 CA THR A 68 8186 7573 6946 373 395 -257 C
ATOM 508 C THR A 68 29.772 165.134 13.584 1.00 66.34 C
ANISOU 508 C THR A 68 9067 8353 7786 420 426 -248 C
ATOM 509 O THR A 68 29.992 163.954 13.287 1.00 73.33 O
ANISOU 509 O THR A 68 10057 9175 8628 475 468 -256 O
ATOM 510 CB THR A 68 31.423 166.441 12.261 1.00 57.66 C
ANISOU 510 CB THR A 68 7877 7398 6632 459 435 -238 C
ATOM 511 OG1 THR A 68 32.087 166.724 13.499 1.00 63.08 O
ANISOU 511 OG1 THR A 68 8476 8158 7334 508 451 -206 O
ATOM 512 CG2 THR A 68 31.626 167.612 11.314 1.00 52.18 C
ANISOU 512 CG2 THR A 68 7127 6767 5934 409 403 -243 C
ATOM 513 N GLY A 69 29.398 165.508 14.806 1.00 60.32 N
ANISOU 513 N GLY A 69 8234 7611 7074 401 407 -230 N
ATOM 514 CA GLY A 69 29.268 164.539 15.877 1.00 59.23 C
ANISOU 514 CA GLY A 69 8133 7428 6944 446 436 -218 C
ATOM 515 C GLY A 69 30.580 163.969 16.365 1.00 65.89 C
ANISOU 515 C GLY A 69 8971 8317 7746 567 498 -193 C
ATOM 516 O GLY A 69 30.622 162.816 16.804 1.00 82.04 O
ANISOU 516 O GLY A 69 11094 10304 9774 624 537 -188 O
ATOM 517 N PHE A 70 31.656 164.751 16.302 1.00 60.13 N
ANISOU 517 N PHE A 70 8154 7695 6999 607 508 -174 N
ATOM 518 CA PHE A 70 32.975 164.276 16.695 1.00 60.83 C
ANISOU 518 CA PHE A 70 8225 7847 7041 724 567 -143 C
ATOM 519 C PHE A 70 33.013 163.940 18.185 1.00 57.64 C
ANISOU 519 C PHE A 70 7785 7455 6662 763 582 -116 C
ATOM 520 O PHE A 70 32.214 164.432 18.986 1.00 60.27 O
ANISOU 520 O PHE A 70 8070 7779 7050 696 543 -117 O
ATOM 521 CB PHE A 70 34.035 165.330 16.371 1.00 62.09 C
ANISOU 521 CB PHE A 70 8282 8133 7178 739 565 -125 C
ATOM 522 CG PHE A 70 34.016 166.513 17.300 1.00 67.36 C
ANISOU 522 CG PHE A 70 8826 8879 7890 687 526 -107 C
ATOM 523 CD1 PHE A 70 32.957 167.407 17.287 1.00 70.65 C
ANISOU 523 CD1 PHE A 70 9214 9268 8360 579 467 -127 C
ATOM 524 CD2 PHE A 70 35.059 166.732 18.186 1.00 78.81 C
ANISOU 524 CD2 PHE A 70 10190 10433 9322 748 552 -70 C
ATOM 525 CE1 PHE A 70 32.934 168.489 18.145 1.00 66.93 C
ANISOU 525 CE1 PHE A 70 8642 8862 7926 535 435 -113 C
ATOM 526 CE2 PHE A 70 35.044 167.817 19.043 1.00 75.93 C
ANISOU 526 CE2 PHE A 70 9721 10137 8993 695 517 -56 C
ATOM 527 CZ PHE A 70 33.981 168.696 19.022 1.00 74.00 C
ANISOU 527 CZ PHE A 70 9460 9855 8803 590 460 -79 C
ATOM 528 N CYS A 71 33.966 163.087 18.553 1.00 61.65 N
ANISOU 528 N CYS A 71 8315 7986 7124 878 643 -90 N
ATOM 529 CA CYS A 71 34.129 162.683 19.943 1.00 57.18 C
ANISOU 529 CA CYS A 71 7716 7437 6573 928 664 -60 C
ATOM 530 C CYS A 71 34.819 163.785 20.735 1.00 53.93 C
ANISOU 530 C CYS A 71 7159 7158 6175 924 649 -30 C
ATOM 531 O CYS A 71 35.814 164.360 20.281 1.00 59.66 O
ANISOU 531 O CYS A 71 7823 7983 6864 952 658 -14 O
ATOM 532 CB CYS A 71 34.934 161.387 20.030 1.00 62.02 C
ANISOU 532 CB CYS A 71 8407 8032 7129 1058 737 -39 C
ATOM 533 SG CYS A 71 34.160 159.965 19.230 1.00 75.84 S
ANISOU 533 SG CYS A 71 10349 9613 8854 1066 763 -74 S
ATOM 534 N ALA A 72 34.298 164.072 21.925 1.00 45.32 N
ANISOU 534 N ALA A 72 6016 6071 5134 887 624 -21 N
ATOM 535 CA ALA A 72 34.869 165.115 22.763 1.00 50.41 C
ANISOU 535 CA ALA A 72 6530 6833 5790 874 607 5 C
ATOM 536 C ALA A 72 34.418 164.909 24.199 1.00 52.96 C
ANISOU 536 C ALA A 72 6827 7144 6153 873 603 20 C
ATOM 537 O ALA A 72 33.417 164.238 24.466 1.00 56.06 O
ANISOU 537 O ALA A 72 7290 7434 6577 851 597 4 O
ATOM 538 CB ALA A 72 34.467 166.511 22.274 1.00 51.81 C
ANISOU 538 CB ALA A 72 6648 7040 5998 767 549 -15 C
ATOM 539 N ALA A 73 35.180 165.491 25.123 1.00 49.77 N
ANISOU 539 N ALA A 73 6319 6850 5743 893 606 52 N
ATOM 540 CA ALA A 73 34.733 165.571 26.505 1.00 51.16 C
ANISOU 540 CA ALA A 73 6452 7028 5959 876 593 65 C
ATOM 541 C ALA A 73 33.454 166.395 26.575 1.00 58.18 C
ANISOU 541 C ALA A 73 7333 7861 6911 761 533 34 C
ATOM 542 O ALA A 73 33.289 167.373 25.840 1.00 65.01 O
ANISOU 542 O ALA A 73 8174 8742 7784 693 497 15 O
ATOM 543 CB ALA A 73 35.819 166.189 27.385 1.00 55.16 C
ANISOU 543 CB ALA A 73 6844 7672 6441 906 603 104 C
ATOM 544 N CYS A 74 32.544 165.997 27.465 1.00 49.20 N
ANISOU 544 N CYS A 74 6217 6661 5816 742 524 32 N
ATOM 545 CA CYS A 74 31.191 166.546 27.423 1.00 50.12 C
ANISOU 545 CA CYS A 74 6344 6711 5989 643 472 4 C
ATOM 546 C CYS A 74 31.171 168.037 27.744 1.00 54.82 C
ANISOU 546 C CYS A 74 6845 7377 6607 576 431 2 C
ATOM 547 O CYS A 74 30.462 168.807 27.085 1.00 54.52 O
ANISOU 547 O CYS A 74 6810 7312 6594 501 390 -22 O
ATOM 548 CB CYS A 74 30.282 165.779 28.380 1.00 55.58 C
ANISOU 548 CB CYS A 74 7071 7332 6715 642 474 7 C
ATOM 549 SG CYS A 74 28.538 166.227 28.238 1.00 64.74 S
ANISOU 549 SG CYS A 74 8254 8408 7936 529 416 -22 S
ATOM 550 N HIS A 75 31.936 168.465 28.750 1.00 53.25 N
ANISOU 550 N HIS A 75 6566 7268 6397 601 440 29 N
ATOM 551 CA HIS A 75 31.907 169.874 29.132 1.00 48.10 C
ANISOU 551 CA HIS A 75 5837 6677 5764 534 402 26 C
ATOM 552 C HIS A 75 32.558 170.753 28.072 1.00 44.64 C
ANISOU 552 C HIS A 75 5373 6292 5295 505 389 19 C
ATOM 553 O HIS A 75 32.113 171.882 27.838 1.00 54.08 O
ANISOU 553 O HIS A 75 6545 7489 6513 430 349 3 O
ATOM 554 CB HIS A 75 32.579 170.067 30.487 1.00 58.24 C
ANISOU 554 CB HIS A 75 7046 8044 7037 563 415 56 C
ATOM 555 CG HIS A 75 31.807 169.479 31.625 1.00 70.85 C
ANISOU 555 CG HIS A 75 8656 9593 8671 573 418 63 C
ATOM 556 ND1 HIS A 75 31.845 168.137 31.934 1.00 90.23 N
ANISOU 556 ND1 HIS A 75 11160 12007 11117 645 457 77 N
ATOM 557 CD2 HIS A 75 30.963 170.047 32.519 1.00 71.38 C
ANISOU 557 CD2 HIS A 75 8697 9643 8782 522 389 57 C
ATOM 558 CE1 HIS A 75 31.068 167.904 32.976 1.00 92.26 C
ANISOU 558 CE1 HIS A 75 11416 12228 11411 634 449 81 C
ATOM 559 NE2 HIS A 75 30.520 169.046 33.350 1.00 89.64 N
ANISOU 559 NE2 HIS A 75 11036 11911 11111 561 408 69 N
ATOM 560 N GLY A 76 33.613 170.259 27.422 1.00 41.24 N
ANISOU 560 N GLY A 76 4951 5907 4813 567 424 32 N
ATOM 561 CA GLY A 76 34.143 170.964 26.266 1.00 43.26 C
ANISOU 561 CA GLY A 76 5194 6203 5040 540 413 24 C
ATOM 562 C GLY A 76 33.154 171.000 25.116 1.00 49.43 C
ANISOU 562 C GLY A 76 6046 6891 5846 490 387 -11 C
ATOM 563 O GLY A 76 33.065 171.994 24.391 1.00 61.42 O
ANISOU 563 O GLY A 76 7546 8423 7366 428 355 -25 O
ATOM 564 N CYS A 77 32.397 169.916 24.934 1.00 47.47 N
ANISOU 564 N CYS A 77 5878 6545 5613 511 399 -24 N
ATOM 565 CA CYS A 77 31.338 169.907 23.932 1.00 40.86 C
ANISOU 565 CA CYS A 77 5107 5619 4801 454 370 -56 C
ATOM 566 C CYS A 77 30.247 170.910 24.282 1.00 46.48 C
ANISOU 566 C CYS A 77 5787 6307 5565 367 320 -69 C
ATOM 567 O CYS A 77 29.640 171.517 23.391 1.00 37.98 O
ANISOU 567 O CYS A 77 4726 5202 4502 306 287 -89 O
ATOM 568 CB CYS A 77 30.760 168.498 23.805 1.00 43.59 C
ANISOU 568 CB CYS A 77 5547 5869 5147 489 394 -65 C
ATOM 569 SG CYS A 77 29.357 168.353 22.679 1.00 57.14 S
ANISOU 569 SG CYS A 77 7345 7475 6888 410 358 -101 S
ATOM 570 N LEU A 78 29.990 171.104 25.579 1.00 39.08 N
ANISOU 570 N LEU A 78 4807 5385 4656 363 314 -56 N
ATOM 571 CA LEU A 78 28.969 172.057 26.001 1.00 38.71 C
ANISOU 571 CA LEU A 78 4733 5319 4657 291 271 -65 C
ATOM 572 C LEU A 78 29.319 173.473 25.569 1.00 48.10 C
ANISOU 572 C LEU A 78 5873 6564 5838 241 244 -70 C
ATOM 573 O LEU A 78 28.436 174.243 25.173 1.00 44.51 O
ANISOU 573 O LEU A 78 5423 6076 5411 180 208 -84 O
ATOM 574 CB LEU A 78 28.786 172.003 27.516 1.00 46.81 C
ANISOU 574 CB LEU A 78 5719 6360 5706 305 276 -48 C
ATOM 575 CG LEU A 78 27.705 171.069 28.051 1.00 44.54 C
ANISOU 575 CG LEU A 78 5476 5993 5452 308 277 -49 C
ATOM 576 CD1 LEU A 78 27.762 171.034 29.569 1.00 34.16 C
ANISOU 576 CD1 LEU A 78 4116 4710 4154 331 287 -29 C
ATOM 577 CD2 LEU A 78 26.336 171.521 27.568 1.00 43.64 C
ANISOU 577 CD2 LEU A 78 5385 5820 5378 235 235 -68 C
ATOM 578 N PHE A 79 30.601 173.839 25.646 1.00 42.71 N
ANISOU 578 N PHE A 79 5143 5969 5115 267 262 -54 N
ATOM 579 CA PHE A 79 31.000 175.197 25.292 1.00 31.54 C
ANISOU 579 CA PHE A 79 3686 4610 3689 214 236 -56 C
ATOM 580 C PHE A 79 30.764 175.469 23.812 1.00 38.28 C
ANISOU 580 C PHE A 79 4577 5433 4534 182 220 -75 C
ATOM 581 O PHE A 79 30.185 176.497 23.443 1.00 46.82 O
ANISOU 581 O PHE A 79 5655 6499 5636 119 185 -87 O
ATOM 582 CB PHE A 79 32.465 175.434 25.653 1.00 33.30 C
ANISOU 582 CB PHE A 79 3849 4942 3862 245 260 -31 C
ATOM 583 CG PHE A 79 32.948 176.821 25.328 1.00 39.19 C
ANISOU 583 CG PHE A 79 4554 5748 4589 183 234 -31 C
ATOM 584 CD1 PHE A 79 32.681 177.879 26.183 1.00 44.65 C
ANISOU 584 CD1 PHE A 79 5212 6455 5299 129 209 -31 C
ATOM 585 CD2 PHE A 79 33.663 177.067 24.169 1.00 33.78 C
ANISOU 585 CD2 PHE A 79 3868 5101 3864 178 237 -31 C
ATOM 586 CE1 PHE A 79 33.119 179.156 25.889 1.00 33.75 C
ANISOU 586 CE1 PHE A 79 3804 5121 3897 69 186 -32 C
ATOM 587 CE2 PHE A 79 34.103 178.340 23.870 1.00 35.23 C
ANISOU 587 CE2 PHE A 79 4019 5338 4029 116 214 -30 C
ATOM 588 CZ PHE A 79 33.831 179.387 24.732 1.00 34.87 C
ANISOU 588 CZ PHE A 79 3946 5302 4002 60 188 -30 C
ATOM 589 N ILE A 80 31.219 174.552 22.952 1.00 31.36 N
ANISOU 589 N ILE A 80 3741 4548 3627 227 246 -77 N
ATOM 590 CA ILE A 80 31.021 174.682 21.511 1.00 35.13 C
ANISOU 590 CA ILE A 80 4260 4996 4093 201 233 -96 C
ATOM 591 C ILE A 80 29.539 174.757 21.172 1.00 27.68 C
ANISOU 591 C ILE A 80 3360 3963 3196 147 199 -117 C
ATOM 592 O ILE A 80 29.141 175.445 20.224 1.00 47.73 O
ANISOU 592 O ILE A 80 5910 6487 5738 97 171 -130 O
ATOM 593 CB ILE A 80 31.719 173.511 20.786 1.00 40.37 C
ANISOU 593 CB ILE A 80 4969 5657 4713 270 274 -94 C
ATOM 594 CG1 ILE A 80 33.239 173.655 20.883 1.00 45.48 C
ANISOU 594 CG1 ILE A 80 5562 6412 5307 318 304 -68 C
ATOM 595 CG2 ILE A 80 31.280 173.415 19.332 1.00 58.33 C
ANISOU 595 CG2 ILE A 80 7303 7880 6979 243 261 -118 C
ATOM 596 CD1 ILE A 80 34.000 172.603 20.113 1.00 67.96 C
ANISOU 596 CD1 ILE A 80 8452 9266 8104 395 348 -63 C
ATOM 597 N ALA A 81 28.699 174.077 21.951 1.00 41.46 N
ANISOU 597 N ALA A 81 5126 5653 4973 155 200 -117 N
ATOM 598 CA ALA A 81 27.267 174.061 21.682 1.00 40.51 C
ANISOU 598 CA ALA A 81 5042 5457 4892 104 168 -132 C
ATOM 599 C ALA A 81 26.571 175.324 22.168 1.00 50.28 C
ANISOU 599 C ALA A 81 6233 6704 6165 49 132 -130 C
ATOM 600 O ALA A 81 25.573 175.743 21.569 1.00 62.58 O
ANISOU 600 O ALA A 81 7809 8224 7745 -1 100 -139 O
ATOM 601 CB ALA A 81 26.620 172.841 22.340 1.00 26.02 C
ANISOU 601 CB ALA A 81 3247 3563 3075 129 183 -130 C
ATOM 602 N CYS A 82 27.079 175.947 23.232 1.00 36.76 N
ANISOU 602 N CYS A 82 4466 5044 4456 58 136 -116 N
ATOM 603 CA CYS A 82 26.361 177.009 23.923 1.00 41.84 C
ANISOU 603 CA CYS A 82 5077 5686 5133 16 108 -113 C
ATOM 604 C CYS A 82 26.924 178.403 23.676 1.00 50.00 C
ANISOU 604 C CYS A 82 6077 6769 6150 -19 92 -113 C
ATOM 605 O CYS A 82 26.269 179.384 24.045 1.00 39.72 O
ANISOU 605 O CYS A 82 4762 5458 4873 -56 68 -112 O
ATOM 606 CB CYS A 82 26.349 176.742 25.434 1.00 23.19 C
ANISOU 606 CB CYS A 82 2686 3337 2788 44 122 -99 C
ATOM 607 SG CYS A 82 25.445 175.264 25.935 1.00 48.72 S
ANISOU 607 SG CYS A 82 5959 6505 6048 72 135 -97 S
ATOM 608 N PHE A 83 28.112 178.527 23.075 1.00 28.04 N
ANISOU 608 N PHE A 83 3285 4042 3326 -9 106 -111 N
ATOM 609 CA PHE A 83 28.702 179.853 22.913 1.00 29.29 C
ANISOU 609 CA PHE A 83 3414 4252 3465 -49 91 -108 C
ATOM 610 C PHE A 83 27.840 180.757 22.039 1.00 44.48 C
ANISOU 610 C PHE A 83 5360 6134 5406 -102 57 -119 C
ATOM 611 O PHE A 83 27.806 181.974 22.253 1.00 40.21 O
ANISOU 611 O PHE A 83 4804 5606 4866 -142 39 -117 O
ATOM 612 CB PHE A 83 30.109 179.748 22.330 1.00 26.89 C
ANISOU 612 CB PHE A 83 3091 4018 3107 -30 112 -100 C
ATOM 613 CG PHE A 83 30.815 181.069 22.239 1.00 36.00 C
ANISOU 613 CG PHE A 83 4213 5232 4235 -77 98 -94 C
ATOM 614 CD1 PHE A 83 31.315 181.680 23.379 1.00 38.38 C
ANISOU 614 CD1 PHE A 83 4472 5583 4526 -91 99 -81 C
ATOM 615 CD2 PHE A 83 30.966 181.710 21.021 1.00 45.10 C
ANISOU 615 CD2 PHE A 83 5378 6388 5368 -114 82 -101 C
ATOM 616 CE1 PHE A 83 31.961 182.904 23.307 1.00 40.23 C
ANISOU 616 CE1 PHE A 83 4685 5870 4732 -145 85 -76 C
ATOM 617 CE2 PHE A 83 31.612 182.935 20.940 1.00 43.82 C
ANISOU 617 CE2 PHE A 83 5192 6278 5179 -164 69 -94 C
ATOM 618 CZ PHE A 83 32.111 183.532 22.087 1.00 33.74 C
ANISOU 618 CZ PHE A 83 3879 5048 3891 -182 70 -82 C
ATOM 619 N VAL A 84 27.139 180.187 21.055 1.00 28.31 N
ANISOU 619 N VAL A 84 3353 4036 3369 -104 50 -130 N
ATOM 620 CA VAL A 84 26.260 180.987 20.210 1.00 34.37 C
ANISOU 620 CA VAL A 84 4139 4768 4152 -151 17 -137 C
ATOM 621 C VAL A 84 25.095 181.546 21.014 1.00 47.27 C
ANISOU 621 C VAL A 84 5766 6367 5827 -169 -3 -132 C
ATOM 622 O VAL A 84 24.528 182.583 20.650 1.00 42.18 O
ANISOU 622 O VAL A 84 5126 5709 5191 -205 -27 -131 O
ATOM 623 CB VAL A 84 25.771 180.155 19.001 1.00 29.43 C
ANISOU 623 CB VAL A 84 3558 4102 3523 -151 13 -149 C
ATOM 624 CG1 VAL A 84 24.823 179.052 19.448 1.00 32.64 C
ANISOU 624 CG1 VAL A 84 3987 4455 3957 -134 17 -150 C
ATOM 625 CG2 VAL A 84 25.119 181.053 17.954 1.00 31.60 C
ANISOU 625 CG2 VAL A 84 3846 4358 3802 -199 -18 -153 C
ATOM 626 N LEU A 85 24.732 180.889 22.119 1.00 34.28 N
ANISOU 626 N LEU A 85 4113 4709 4205 -142 9 -127 N
ATOM 627 CA LEU A 85 23.702 181.428 22.999 1.00 24.82 C
ANISOU 627 CA LEU A 85 2903 3486 3042 -153 -6 -119 C
ATOM 628 C LEU A 85 24.197 182.663 23.742 1.00 38.72 C
ANISOU 628 C LEU A 85 4639 5280 4794 -168 -8 -115 C
ATOM 629 O LEU A 85 23.404 183.564 24.042 1.00 40.19 O
ANISOU 629 O LEU A 85 4827 5446 4999 -186 -25 -110 O
ATOM 630 CB LEU A 85 23.246 180.353 23.985 1.00 34.04 C
ANISOU 630 CB LEU A 85 4068 4635 4233 -121 8 -114 C
ATOM 631 CG LEU A 85 22.881 179.001 23.365 1.00 36.32 C
ANISOU 631 CG LEU A 85 4390 4887 4523 -109 15 -119 C
ATOM 632 CD1 LEU A 85 22.438 178.022 24.442 1.00 23.47 C
ANISOU 632 CD1 LEU A 85 2761 3239 2917 -82 29 -111 C
ATOM 633 CD2 LEU A 85 21.802 179.162 22.303 1.00 28.34 C
ANISOU 633 CD2 LEU A 85 3405 3840 3524 -147 -14 -122 C
ATOM 634 N VAL A 86 25.497 182.722 24.044 1.00 31.42 N
ANISOU 634 N VAL A 86 3693 4409 3836 -160 10 -114 N
ATOM 635 CA VAL A 86 26.069 183.916 24.662 1.00 31.49 C
ANISOU 635 CA VAL A 86 3684 4452 3826 -186 7 -110 C
ATOM 636 C VAL A 86 25.986 185.096 23.705 1.00 35.53 C
ANISOU 636 C VAL A 86 4218 4956 4327 -230 -15 -114 C
ATOM 637 O VAL A 86 25.578 186.201 24.083 1.00 38.22 O
ANISOU 637 O VAL A 86 4568 5280 4673 -256 -28 -113 O
ATOM 638 CB VAL A 86 27.521 183.654 25.098 1.00 37.26 C
ANISOU 638 CB VAL A 86 4384 5256 4518 -173 29 -104 C
ATOM 639 CG1 VAL A 86 28.161 184.941 25.613 1.00 31.92 C
ANISOU 639 CG1 VAL A 86 3695 4619 3815 -215 22 -100 C
ATOM 640 CG2 VAL A 86 27.565 182.565 26.151 1.00 29.33 C
ANISOU 640 CG2 VAL A 86 3360 4259 3526 -125 52 -96 C
ATOM 641 N LEU A 87 26.379 184.878 22.448 1.00 37.79 N
ANISOU 641 N LEU A 87 4514 5251 4593 -238 -17 -119 N
ATOM 642 CA LEU A 87 26.320 185.947 21.458 1.00 32.28 C
ANISOU 642 CA LEU A 87 3837 4546 3882 -280 -38 -121 C
ATOM 643 C LEU A 87 24.885 186.392 21.215 1.00 41.19 C
ANISOU 643 C LEU A 87 4990 5614 5046 -289 -60 -120 C
ATOM 644 O LEU A 87 24.612 187.592 21.087 1.00 48.07 O
ANISOU 644 O LEU A 87 5878 6471 5914 -318 -74 -117 O
ATOM 645 CB LEU A 87 26.966 185.485 20.153 1.00 27.24 C
ANISOU 645 CB LEU A 87 3205 3930 3216 -281 -34 -126 C
ATOM 646 CG LEU A 87 28.390 184.949 20.283 1.00 33.54 C
ANISOU 646 CG LEU A 87 3973 4796 3973 -262 -9 -121 C
ATOM 647 CD1 LEU A 87 28.907 184.538 18.920 1.00 32.48 C
ANISOU 647 CD1 LEU A 87 3851 4679 3811 -259 -5 -125 C
ATOM 648 CD2 LEU A 87 29.308 185.983 20.927 1.00 24.84 C
ANISOU 648 CD2 LEU A 87 2849 3750 2841 -296 -9 -113 C
ATOM 649 N ALA A 88 23.951 185.440 21.151 1.00 32.29 N
ANISOU 649 N ALA A 88 3868 4453 3949 -264 -61 -120 N
ATOM 650 CA ALA A 88 22.552 185.800 20.955 1.00 29.63 C
ANISOU 650 CA ALA A 88 3545 4071 3643 -271 -82 -113 C
ATOM 651 C ALA A 88 22.013 186.577 22.148 1.00 33.81 C
ANISOU 651 C ALA A 88 4068 4587 4190 -265 -82 -104 C
ATOM 652 O ALA A 88 21.211 187.504 21.984 1.00 44.20 O
ANISOU 652 O ALA A 88 5400 5879 5515 -275 -97 -96 O
ATOM 653 CB ALA A 88 21.713 184.547 20.705 1.00 39.28 C
ANISOU 653 CB ALA A 88 4771 5267 4887 -254 -84 -113 C
ATOM 654 N GLN A 89 22.447 186.218 23.359 1.00 38.20 N
ANISOU 654 N GLN A 89 4605 5162 4748 -245 -64 -105 N
ATOM 655 CA GLN A 89 22.004 186.952 24.540 1.00 33.08 C
ANISOU 655 CA GLN A 89 3954 4502 4112 -239 -63 -98 C
ATOM 656 C GLN A 89 22.571 188.366 24.549 1.00 35.11 C
ANISOU 656 C GLN A 89 4232 4767 4342 -270 -67 -100 C
ATOM 657 O GLN A 89 21.865 189.321 24.894 1.00 46.75 O
ANISOU 657 O GLN A 89 5728 6212 5824 -272 -73 -94 O
ATOM 658 CB GLN A 89 22.405 186.205 25.811 1.00 34.65 C
ANISOU 658 CB GLN A 89 4127 4722 4316 -212 -42 -98 C
ATOM 659 CG GLN A 89 21.620 186.632 27.037 1.00 38.79 C
ANISOU 659 CG GLN A 89 4648 5228 4862 -196 -40 -90 C
ATOM 660 CD GLN A 89 20.127 186.426 26.866 1.00 40.53 C
ANISOU 660 CD GLN A 89 4872 5411 5118 -180 -53 -77 C
ATOM 661 OE1 GLN A 89 19.689 185.446 26.262 1.00 32.64 O
ANISOU 661 OE1 GLN A 89 3867 4403 4133 -175 -58 -75 O
ATOM 662 NE2 GLN A 89 19.337 187.357 27.390 1.00 35.72 N
ANISOU 662 NE2 GLN A 89 4273 4781 4518 -173 -57 -67 N
ATOM 663 N SER A 90 23.844 188.516 24.173 1.00 39.22 N
ANISOU 663 N SER A 90 4749 5327 4825 -295 -62 -107 N
ATOM 664 CA SER A 90 24.436 189.844 24.054 1.00 31.79 C
ANISOU 664 CA SER A 90 3832 4394 3852 -337 -68 -109 C
ATOM 665 C SER A 90 23.681 190.691 23.037 1.00 38.15 C
ANISOU 665 C SER A 90 4674 5160 4662 -353 -86 -105 C
ATOM 666 O SER A 90 23.500 191.899 23.233 1.00 35.69 O
ANISOU 666 O SER A 90 4397 4824 4339 -373 -91 -102 O
ATOM 667 CB SER A 90 25.910 189.723 23.671 1.00 29.81 C
ANISOU 667 CB SER A 90 3563 4203 3558 -364 -60 -113 C
ATOM 668 OG SER A 90 26.516 190.997 23.547 1.00 50.71 O
ANISOU 668 OG SER A 90 6236 6862 6169 -414 -68 -113 O
ATOM 669 N SER A 91 23.226 190.071 21.946 1.00 37.29 N
ANISOU 669 N SER A 91 4561 5041 4566 -344 -96 -104 N
ATOM 670 CA SER A 91 22.417 190.788 20.967 1.00 36.61 C
ANISOU 670 CA SER A 91 4504 4921 4486 -355 -114 -96 C
ATOM 671 C SER A 91 21.108 191.271 21.579 1.00 44.52 C
ANISOU 671 C SER A 91 5519 5882 5516 -329 -118 -83 C
ATOM 672 O SER A 91 20.650 192.383 21.287 1.00 42.47 O
ANISOU 672 O SER A 91 5292 5594 5249 -336 -126 -73 O
ATOM 673 CB SER A 91 22.143 189.892 19.759 1.00 27.04 C
ANISOU 673 CB SER A 91 3282 3711 3281 -351 -123 -97 C
ATOM 674 OG SER A 91 23.344 189.538 19.095 1.00 43.40 O
ANISOU 674 OG SER A 91 5347 5821 5322 -370 -118 -108 O
ATOM 675 N ILE A 92 20.489 190.446 22.427 1.00 40.04 N
ANISOU 675 N ILE A 92 4926 5311 4978 -295 -111 -79 N
ATOM 676 CA ILE A 92 19.226 190.825 23.059 1.00 36.47 C
ANISOU 676 CA ILE A 92 4478 4828 4550 -265 -112 -62 C
ATOM 677 C ILE A 92 19.425 192.035 23.963 1.00 40.51 C
ANISOU 677 C ILE A 92 5021 5324 5046 -267 -102 -62 C
ATOM 678 O ILE A 92 18.634 192.986 23.943 1.00 40.28 O
ANISOU 678 O ILE A 92 5023 5264 5019 -253 -105 -49 O
ATOM 679 CB ILE A 92 18.639 189.633 23.836 1.00 45.69 C
ANISOU 679 CB ILE A 92 5609 6001 5748 -234 -106 -58 C
ATOM 680 CG1 ILE A 92 18.054 188.600 22.874 1.00 47.21 C
ANISOU 680 CG1 ILE A 92 5785 6195 5956 -236 -119 -53 C
ATOM 681 CG2 ILE A 92 17.573 190.104 24.804 1.00 31.46 C
ANISOU 681 CG2 ILE A 92 3809 4180 3966 -202 -101 -41 C
ATOM 682 CD1 ILE A 92 16.738 189.029 22.267 1.00 54.87 C
ANISOU 682 CD1 ILE A 92 6760 7150 6940 -229 -137 -31 C
ATOM 683 N PHE A 93 20.488 192.016 24.771 1.00 39.65 N
ANISOU 683 N PHE A 93 4910 5239 4919 -282 -89 -77 N
ATOM 684 CA PHE A 93 20.759 193.140 25.662 1.00 38.40 C
ANISOU 684 CA PHE A 93 4788 5065 4738 -293 -80 -80 C
ATOM 685 C PHE A 93 21.052 194.412 24.876 1.00 38.45 C
ANISOU 685 C PHE A 93 4847 5050 4713 -329 -88 -80 C
ATOM 686 O PHE A 93 20.645 195.507 25.281 1.00 54.74 O
ANISOU 686 O PHE A 93 6959 7075 6765 -325 -83 -75 O
ATOM 687 CB PHE A 93 21.925 192.801 26.589 1.00 38.38 C
ANISOU 687 CB PHE A 93 4765 5102 4715 -312 -67 -93 C
ATOM 688 CG PHE A 93 21.588 191.789 27.645 1.00 53.00 C
ANISOU 688 CG PHE A 93 6577 6967 6595 -274 -55 -91 C
ATOM 689 CD1 PHE A 93 20.342 191.789 28.249 1.00 53.07 C
ANISOU 689 CD1 PHE A 93 6587 6944 6633 -232 -52 -79 C
ATOM 690 CD2 PHE A 93 22.522 190.844 28.042 1.00 47.52 C
ANISOU 690 CD2 PHE A 93 5844 6320 5894 -277 -46 -98 C
ATOM 691 CE1 PHE A 93 20.031 190.863 29.225 1.00 46.88 C
ANISOU 691 CE1 PHE A 93 5767 6172 5874 -200 -42 -76 C
ATOM 692 CE2 PHE A 93 22.216 189.914 29.017 1.00 38.36 C
ANISOU 692 CE2 PHE A 93 4650 5168 4757 -241 -34 -95 C
ATOM 693 CZ PHE A 93 20.969 189.924 29.610 1.00 44.70 C
ANISOU 693 CZ PHE A 93 5455 5937 5591 -205 -33 -84 C
ATOM 694 N SER A 94 21.757 194.289 23.748 1.00 36.12 N
ANISOU 694 N SER A 94 4547 4778 4401 -363 -98 -85 N
ATOM 695 CA SER A 94 22.061 195.463 22.937 1.00 34.29 C
ANISOU 695 CA SER A 94 4364 4526 4137 -401 -107 -83 C
ATOM 696 C SER A 94 20.822 195.995 22.230 1.00 44.18 C
ANISOU 696 C SER A 94 5644 5735 5408 -372 -116 -65 C
ATOM 697 O SER A 94 20.696 197.209 22.034 1.00 45.89 O
ANISOU 697 O SER A 94 5918 5915 5602 -384 -116 -59 O
ATOM 698 CB SER A 94 23.154 195.132 21.922 1.00 31.56 C
ANISOU 698 CB SER A 94 4000 4225 3767 -442 -114 -91 C
ATOM 699 OG SER A 94 24.390 194.884 22.570 1.00 48.34 O
ANISOU 699 OG SER A 94 6103 6398 5865 -471 -105 -102 O
ATOM 700 N LEU A 95 19.902 195.111 21.839 1.00 42.46 N
ANISOU 700 N LEU A 95 5388 5521 5225 -336 -123 -55 N
ATOM 701 CA LEU A 95 18.664 195.562 21.213 1.00 36.04 C
ANISOU 701 CA LEU A 95 4590 4677 4425 -307 -132 -32 C
ATOM 702 C LEU A 95 17.747 196.228 22.230 1.00 37.38 C
ANISOU 702 C LEU A 95 4785 4813 4604 -263 -120 -17 C
ATOM 703 O LEU A 95 17.146 197.271 21.945 1.00 41.03 O
ANISOU 703 O LEU A 95 5292 5241 5056 -246 -119 0 O
ATOM 704 CB LEU A 95 17.955 194.387 20.543 1.00 31.65 C
ANISOU 704 CB LEU A 95 3985 4143 3899 -290 -145 -23 C
ATOM 705 CG LEU A 95 18.602 193.847 19.269 1.00 31.22 C
ANISOU 705 CG LEU A 95 3918 4113 3833 -325 -158 -34 C
ATOM 706 CD1 LEU A 95 17.949 192.539 18.848 1.00 35.96 C
ANISOU 706 CD1 LEU A 95 4475 4730 4458 -312 -168 -30 C
ATOM 707 CD2 LEU A 95 18.501 194.882 18.166 1.00 24.50 C
ANISOU 707 CD2 LEU A 95 3104 3245 2960 -343 -170 -23 C
ATOM 708 N LEU A 96 17.627 195.638 23.420 1.00 35.20 N
ANISOU 708 N LEU A 96 4482 4546 4345 -240 -108 -22 N
ATOM 709 CA LEU A 96 16.811 196.248 24.463 1.00 45.63 C
ANISOU 709 CA LEU A 96 5827 5838 5672 -195 -93 -9 C
ATOM 710 C LEU A 96 17.398 197.583 24.904 1.00 55.53 C
ANISOU 710 C LEU A 96 7155 7055 6887 -215 -80 -18 C
ATOM 711 O LEU A 96 16.657 198.523 25.215 1.00 65.62 O
ANISOU 711 O LEU A 96 8482 8293 8158 -179 -69 -3 O
ATOM 712 CB LEU A 96 16.683 195.293 25.651 1.00 52.74 C
ANISOU 712 CB LEU A 96 6682 6759 6595 -173 -82 -14 C
ATOM 713 CG LEU A 96 15.783 195.720 26.813 1.00 44.94 C
ANISOU 713 CG LEU A 96 5709 5751 5617 -121 -65 1 C
ATOM 714 CD1 LEU A 96 14.355 195.946 26.342 1.00 39.39 C
ANISOU 714 CD1 LEU A 96 4999 5038 4930 -71 -70 36 C
ATOM 715 CD2 LEU A 96 15.826 194.678 27.919 1.00 39.34 C
ANISOU 715 CD2 LEU A 96 4951 5067 4929 -107 -57 -6 C
ATOM 716 N ALA A 97 18.728 197.691 24.923 1.00 47.00 N
ANISOU 716 N ALA A 97 6088 5991 5780 -273 -81 -42 N
ATOM 717 CA ALA A 97 19.361 198.940 25.335 1.00 49.64 C
ANISOU 717 CA ALA A 97 6497 6293 6071 -307 -71 -52 C
ATOM 718 C ALA A 97 19.122 200.048 24.318 1.00 46.45 C
ANISOU 718 C ALA A 97 6155 5848 5646 -316 -77 -40 C
ATOM 719 O ALA A 97 18.896 201.204 24.695 1.00 61.00 O
ANISOU 719 O ALA A 97 8075 7639 7463 -308 -65 -36 O
ATOM 720 CB ALA A 97 20.858 198.723 25.550 1.00 45.32 C
ANISOU 720 CB ALA A 97 5938 5786 5495 -374 -74 -75 C
ATOM 721 N ILE A 98 19.176 199.719 23.026 1.00 39.36 N
ANISOU 721 N ILE A 98 5230 4970 4754 -331 -95 -33 N
ATOM 722 CA ILE A 98 18.926 200.719 21.991 1.00 36.19 C
ANISOU 722 CA ILE A 98 4884 4534 4333 -337 -101 -19 C
ATOM 723 C ILE A 98 17.494 201.229 22.079 1.00 45.09 C
ANISOU 723 C ILE A 98 6036 5621 5476 -265 -92 10 C
ATOM 724 O ILE A 98 17.239 202.434 21.958 1.00 42.25 O
ANISOU 724 O ILE A 98 5753 5210 5089 -254 -83 22 O
ATOM 725 CB ILE A 98 19.239 200.135 20.600 1.00 27.43 C
ANISOU 725 CB ILE A 98 3732 3461 3229 -365 -122 -17 C
ATOM 726 CG1 ILE A 98 20.744 199.930 20.437 1.00 29.57 C
ANISOU 726 CG1 ILE A 98 3992 3770 3472 -436 -127 -41 C
ATOM 727 CG2 ILE A 98 18.698 201.035 19.500 1.00 41.34 C
ANISOU 727 CG2 ILE A 98 5539 5190 4978 -357 -129 4 C
ATOM 728 CD1 ILE A 98 21.126 199.236 19.152 1.00 29.00 C
ANISOU 728 CD1 ILE A 98 3877 3739 3403 -458 -143 -42 C
ATOM 729 N ALA A 99 16.537 200.323 22.300 1.00 43.33 N
ANISOU 729 N ALA A 99 5749 5423 5292 -213 -94 25 N
ATOM 730 CA ALA A 99 15.142 200.733 22.418 1.00 40.70 C
ANISOU 730 CA ALA A 99 5427 5067 4972 -140 -85 58 C
ATOM 731 C ALA A 99 14.933 201.633 23.629 1.00 47.22 C
ANISOU 731 C ALA A 99 6318 5846 5779 -106 -58 58 C
ATOM 732 O ALA A 99 14.200 202.626 23.555 1.00 49.57 O
ANISOU 732 O ALA A 99 6674 6101 6061 -59 -45 82 O
ATOM 733 CB ALA A 99 14.235 199.506 22.500 1.00 32.03 C
ANISOU 733 CB ALA A 99 4242 4013 3915 -103 -93 74 C
ATOM 734 N ILE A 100 15.574 201.305 24.753 1.00 45.54 N
ANISOU 734 N ILE A 100 6100 5640 5565 -127 -49 33 N
ATOM 735 CA ILE A 100 15.466 202.147 25.940 1.00 48.47 C
ANISOU 735 CA ILE A 100 6539 5964 5912 -102 -23 28 C
ATOM 736 C ILE A 100 16.160 203.484 25.710 1.00 49.15 C
ANISOU 736 C ILE A 100 6731 5996 5949 -144 -16 17 C
ATOM 737 O ILE A 100 15.653 204.539 26.111 1.00 42.96 O
ANISOU 737 O ILE A 100 6029 5153 5140 -104 5 28 O
ATOM 738 CB ILE A 100 16.035 201.415 27.168 1.00 36.64 C
ANISOU 738 CB ILE A 100 5005 4494 4422 -120 -17 4 C
ATOM 739 CG1 ILE A 100 15.200 200.172 27.476 1.00 31.74 C
ANISOU 739 CG1 ILE A 100 4292 3918 3849 -72 -20 19 C
ATOM 740 CG2 ILE A 100 16.078 202.343 28.373 1.00 29.36 C
ANISOU 740 CG2 ILE A 100 4163 3524 3468 -107 9 -5 C
ATOM 741 CD1 ILE A 100 15.766 199.322 28.586 1.00 43.79 C
ANISOU 741 CD1 ILE A 100 5776 5477 5386 -89 -16 -3 C
ATOM 742 N ASP A 101 17.326 203.462 25.059 1.00 58.51 N
ANISOU 742 N ASP A 101 7918 7199 7116 -224 -33 -3 N
ATOM 743 CA ASP A 101 18.028 204.705 24.755 1.00 58.48 C
ANISOU 743 CA ASP A 101 8013 7146 7061 -276 -29 -12 C
ATOM 744 C ASP A 101 17.180 205.616 23.877 1.00 59.58 C
ANISOU 744 C ASP A 101 8210 7236 7191 -232 -25 18 C
ATOM 745 O ASP A 101 17.184 206.841 24.051 1.00 64.92 O
ANISOU 745 O ASP A 101 8995 7846 7828 -232 -8 20 O
ATOM 746 CB ASP A 101 19.367 204.398 24.081 1.00 52.96 C
ANISOU 746 CB ASP A 101 7288 6491 6345 -367 -50 -32 C
ATOM 747 CG ASP A 101 20.097 205.651 23.640 1.00 53.23 C
ANISOU 747 CG ASP A 101 7420 6481 6325 -431 -50 -37 C
ATOM 748 OD1 ASP A 101 20.699 206.327 24.501 1.00 67.06 O
ANISOU 748 OD1 ASP A 101 9239 8203 8036 -473 -39 -55 O
ATOM 749 OD2 ASP A 101 20.065 205.959 22.430 1.00 46.61 O
ANISOU 749 OD2 ASP A 101 6592 5636 5481 -442 -62 -24 O
ATOM 750 N ARG A 102 16.430 205.036 22.938 1.00 56.16 N
ANISOU 750 N ARG A 102 7711 6834 6791 -193 -39 42 N
ATOM 751 CA ARG A 102 15.588 205.848 22.069 1.00 52.31 C
ANISOU 751 CA ARG A 102 7270 6312 6296 -146 -35 76 C
ATOM 752 C ARG A 102 14.351 206.358 22.795 1.00 52.80 C
ANISOU 752 C ARG A 102 7366 6335 6359 -50 -8 104 C
ATOM 753 O ARG A 102 13.868 207.456 22.496 1.00 56.90 O
ANISOU 753 O ARG A 102 7968 6799 6850 -10 8 127 O
ATOM 754 CB ARG A 102 15.197 205.051 20.823 1.00 41.38 C
ANISOU 754 CB ARG A 102 5801 4980 4942 -141 -60 94 C
ATOM 755 CG ARG A 102 16.337 204.832 19.827 1.00 40.55 C
ANISOU 755 CG ARG A 102 5681 4902 4824 -226 -83 74 C
ATOM 756 CD ARG A 102 16.885 206.155 19.295 1.00 58.26 C
ANISOU 756 CD ARG A 102 8026 7090 7019 -265 -79 75 C
ATOM 757 NE ARG A 102 17.902 206.728 20.176 1.00 75.50 N
ANISOU 757 NE ARG A 102 10277 9244 9167 -323 -67 46 N
ATOM 758 CZ ARG A 102 18.213 208.019 20.222 1.00 67.62 C
ANISOU 758 CZ ARG A 102 9392 8179 8122 -348 -54 45 C
ATOM 759 NH1 ARG A 102 17.583 208.884 19.441 1.00 74.08 N
ANISOU 759 NH1 ARG A 102 10271 8951 8926 -312 -48 74 N
ATOM 760 NH2 ARG A 102 19.150 208.447 21.058 1.00 66.75 N
ANISOU 760 NH2 ARG A 102 9338 8049 7976 -410 -46 18 N
ATOM 761 N TYR A 103 13.827 205.587 23.750 1.00 42.20 N
ANISOU 761 N TYR A 103 5964 5023 5046 -7 -1 104 N
ATOM 762 CA TYR A 103 12.681 206.062 24.517 1.00 49.06 C
ANISOU 762 CA TYR A 103 6864 5863 5913 87 28 132 C
ATOM 763 C TYR A 103 13.061 207.242 25.402 1.00 55.65 C
ANISOU 763 C TYR A 103 7823 6619 6701 87 57 116 C
ATOM 764 O TYR A 103 12.288 208.197 25.539 1.00 57.90 O
ANISOU 764 O TYR A 103 8185 6852 6963 159 83 142 O
ATOM 765 CB TYR A 103 12.094 204.930 25.360 1.00 49.99 C
ANISOU 765 CB TYR A 103 6888 6035 6072 125 28 136 C
ATOM 766 CG TYR A 103 10.960 205.389 26.246 1.00 57.62 C
ANISOU 766 CG TYR A 103 7881 6979 7033 223 59 165 C
ATOM 767 CD1 TYR A 103 9.735 205.755 25.700 1.00 66.59 C
ANISOU 767 CD1 TYR A 103 9010 8119 8170 306 67 215 C
ATOM 768 CD2 TYR A 103 11.114 205.468 27.623 1.00 56.52 C
ANISOU 768 CD2 TYR A 103 7772 6819 6885 236 81 146 C
ATOM 769 CE1 TYR A 103 8.695 206.183 26.502 1.00 70.76 C
ANISOU 769 CE1 TYR A 103 9560 8634 8690 403 98 246 C
ATOM 770 CE2 TYR A 103 10.079 205.895 28.434 1.00 63.36 C
ANISOU 770 CE2 TYR A 103 8664 7666 7744 330 112 173 C
ATOM 771 CZ TYR A 103 8.871 206.250 27.868 1.00 71.25 C
ANISOU 771 CZ TYR A 103 9655 8673 8744 416 121 224 C
ATOM 772 OH TYR A 103 7.837 206.675 28.670 1.00 73.78 O
ANISOU 772 OH TYR A 103 9999 8982 9054 518 155 256 O
ATOM 773 N ILE A 104 14.249 207.195 26.009 1.00 58.28 N
ANISOU 773 N ILE A 104 8181 6947 7017 6 53 74 N
ATOM 774 CA ILE A 104 14.694 208.293 26.862 1.00 61.25 C
ANISOU 774 CA ILE A 104 8681 7250 7343 -11 78 54 C
ATOM 775 C ILE A 104 14.896 209.555 26.037 1.00 62.92 C
ANISOU 775 C ILE A 104 9004 7393 7509 -30 84 62 C
ATOM 776 O ILE A 104 14.603 210.669 26.490 1.00 58.54 O
ANISOU 776 O ILE A 104 8569 6760 6914 5 114 68 O
ATOM 777 CB ILE A 104 15.978 207.898 27.613 1.00 49.87 C
ANISOU 777 CB ILE A 104 7228 5831 5888 -104 69 11 C
ATOM 778 CG1 ILE A 104 15.723 206.681 28.502 1.00 44.60 C
ANISOU 778 CG1 ILE A 104 6458 5226 5263 -77 67 6 C
ATOM 779 CG2 ILE A 104 16.503 209.066 28.435 1.00 60.03 C
ANISOU 779 CG2 ILE A 104 8650 7043 7115 -138 91 -11 C
ATOM 780 CD1 ILE A 104 16.975 206.123 29.137 1.00 41.63 C
ANISOU 780 CD1 ILE A 104 6050 4889 4878 -163 55 -31 C
ATOM 781 N ALA A 105 15.392 209.400 24.808 1.00 59.01 N
ANISOU 781 N ALA A 105 8478 6924 7018 -85 57 64 N
ATOM 782 CA ALA A 105 15.666 210.558 23.966 1.00 60.74 C
ANISOU 782 CA ALA A 105 8801 7082 7194 -112 60 72 C
ATOM 783 C ALA A 105 14.382 211.271 23.560 1.00 60.87 C
ANISOU 783 C ALA A 105 8866 7055 7208 -5 83 117 C
ATOM 784 O ALA A 105 14.362 212.502 23.443 1.00 71.23 O
ANISOU 784 O ALA A 105 10306 8285 8473 5 104 125 O
ATOM 785 CB ALA A 105 16.455 210.129 22.729 1.00 50.70 C
ANISOU 785 CB ALA A 105 7473 5860 5932 -191 26 66 C
ATOM 786 N ILE A 106 13.300 210.525 23.351 1.00 58.99 N
ANISOU 786 N ILE A 106 8529 6870 7015 77 79 149 N
ATOM 787 CA ILE A 106 12.082 211.128 22.826 1.00 66.23 C
ANISOU 787 CA ILE A 106 9474 7764 7927 179 97 199 C
ATOM 788 C ILE A 106 11.101 211.526 23.930 1.00 80.18 C
ANISOU 788 C ILE A 106 11283 9498 9685 284 136 219 C
ATOM 789 O ILE A 106 10.350 212.493 23.766 1.00 86.26 O
ANISOU 789 O ILE A 106 12135 10214 10426 366 165 255 O
ATOM 790 CB ILE A 106 11.426 210.178 21.807 1.00 67.60 C
ANISOU 790 CB ILE A 106 9517 8022 8146 202 69 230 C
ATOM 791 CG1 ILE A 106 10.344 210.908 21.014 1.00 74.87 C
ANISOU 791 CG1 ILE A 106 10469 8926 9054 292 83 285 C
ATOM 792 CG2 ILE A 106 10.846 208.949 22.494 1.00 76.34 C
ANISOU 792 CG2 ILE A 106 10506 9200 9298 236 63 233 C
ATOM 793 CD1 ILE A 106 9.928 210.178 19.771 1.00 81.92 C
ANISOU 793 CD1 ILE A 106 11255 9894 9976 289 51 312 C
ATOM 794 N ALA A 107 11.101 210.820 25.061 1.00 74.45 N
ANISOU 794 N ALA A 107 10507 8801 8980 288 140 199 N
ATOM 795 CA ALA A 107 10.170 211.116 26.144 1.00 66.48 C
ANISOU 795 CA ALA A 107 9529 7768 7962 389 177 219 C
ATOM 796 C ALA A 107 10.686 212.207 27.075 1.00 79.29 C
ANISOU 796 C ALA A 107 11303 9293 9529 377 210 191 C
ATOM 797 O ALA A 107 9.907 213.053 27.527 1.00 90.84 O
ANISOU 797 O ALA A 107 12854 10700 10962 472 250 216 O
ATOM 798 CB ALA A 107 9.874 209.849 26.948 1.00 63.72 C
ANISOU 798 CB ALA A 107 9057 7496 7659 401 168 213 C
ATOM 799 N ILE A 108 11.981 212.204 27.373 1.00 76.30 N
ANISOU 799 N ILE A 108 10959 8899 9134 263 195 141 N
ATOM 800 CA ILE A 108 12.567 213.197 28.271 1.00 75.63 C
ANISOU 800 CA ILE A 108 11020 8726 8991 231 222 110 C
ATOM 801 C ILE A 108 13.823 213.786 27.635 1.00 76.83 C
ANISOU 801 C ILE A 108 11247 8840 9105 110 203 81 C
ATOM 802 O ILE A 108 14.924 213.629 28.182 1.00 76.40 O
ANISOU 802 O ILE A 108 11204 8793 9034 8 190 40 O
ATOM 803 CB ILE A 108 12.875 212.583 29.646 1.00 74.13 C
ANISOU 803 CB ILE A 108 10795 8561 8809 211 226 78 C
ATOM 804 CG1 ILE A 108 13.557 211.221 29.485 1.00 79.29 C
ANISOU 804 CG1 ILE A 108 11303 9313 9512 134 185 58 C
ATOM 805 CG2 ILE A 108 11.601 212.439 30.464 1.00 82.67 C
ANISOU 805 CG2 ILE A 108 11855 9649 9906 340 258 108 C
ATOM 806 CD1 ILE A 108 14.075 210.639 30.782 1.00 76.60 C
ANISOU 806 CD1 ILE A 108 10932 8999 9174 98 186 24 C
ATOM 807 N PRO A 109 13.712 214.487 26.501 1.00 80.55 N
ANISOU 807 N PRO A 109 11772 9274 9557 115 202 105 N
ATOM 808 CA PRO A 109 14.925 214.974 25.824 1.00 84.88 C
ANISOU 808 CA PRO A 109 12381 9798 10071 -8 180 80 C
ATOM 809 C PRO A 109 15.673 216.041 26.601 1.00 94.73 C
ANISOU 809 C PRO A 109 13790 10955 11250 -73 201 48 C
ATOM 810 O PRO A 109 16.870 216.235 26.351 1.00 96.49 O
ANISOU 810 O PRO A 109 14042 11177 11443 -198 179 20 O
ATOM 811 CB PRO A 109 14.386 215.526 24.498 1.00 84.05 C
ANISOU 811 CB PRO A 109 12302 9671 9964 36 180 120 C
ATOM 812 CG PRO A 109 12.990 215.936 24.817 1.00 87.28 C
ANISOU 812 CG PRO A 109 12746 10045 10373 183 219 162 C
ATOM 813 CD PRO A 109 12.484 214.937 25.822 1.00 84.49 C
ANISOU 813 CD PRO A 109 12287 9755 10062 232 221 158 C
ATOM 814 N LEU A 110 15.016 216.735 27.534 1.00107.19 N
ANISOU 814 N LEU A 110 15472 12458 12797 5 243 53 N
ATOM 815 CA LEU A 110 15.686 217.800 28.272 1.00115.52 C
ANISOU 815 CA LEU A 110 16697 13418 13779 -58 264 21 C
ATOM 816 C LEU A 110 16.753 217.256 29.213 1.00111.90 C
ANISOU 816 C LEU A 110 16202 13002 13312 -169 245 -26 C
ATOM 817 O LEU A 110 17.732 217.952 29.503 1.00118.26 O
ANISOU 817 O LEU A 110 17116 13758 14057 -277 243 -56 O
ATOM 818 CB LEU A 110 14.664 218.627 29.053 1.00117.32 C
ANISOU 818 CB LEU A 110 17047 13555 13974 64 317 39 C
ATOM 819 CG LEU A 110 13.687 219.459 28.220 1.00112.34 C
ANISOU 819 CG LEU A 110 16493 12862 13331 174 345 87 C
ATOM 820 CD1 LEU A 110 12.774 220.279 29.119 1.00113.23 C
ANISOU 820 CD1 LEU A 110 16734 12885 13403 296 402 102 C
ATOM 821 CD2 LEU A 110 14.444 220.357 27.254 1.00103.53 C
ANISOU 821 CD2 LEU A 110 15485 11683 12168 85 335 83 C
ATOM 822 N ARG A 111 16.589 216.023 29.694 1.00111.45 N
ANISOU 822 N ARG A 111 15995 13039 13313 -146 230 -29 N
ATOM 823 CA ARG A 111 17.531 215.424 30.632 1.00112.51 C
ANISOU 823 CA ARG A 111 16082 13223 13442 -237 213 -69 C
ATOM 824 C ARG A 111 18.209 214.184 30.061 1.00103.20 C
ANISOU 824 C ARG A 111 14738 12161 12314 -302 170 -75 C
ATOM 825 O ARG A 111 18.741 213.371 30.822 1.00 92.15 O
ANISOU 825 O ARG A 111 13258 10825 10928 -344 157 -97 O
ATOM 826 CB ARG A 111 16.829 215.086 31.949 1.00116.24 C
ANISOU 826 CB ARG A 111 16541 13698 13928 -154 240 -72 C
ATOM 827 CG ARG A 111 15.465 214.442 31.777 1.00124.88 C
ANISOU 827 CG ARG A 111 17535 14829 15083 -14 251 -32 C
ATOM 828 CD ARG A 111 14.765 214.275 33.115 1.00137.85 C
ANISOU 828 CD ARG A 111 19183 16465 16729 69 282 -33 C
ATOM 829 NE ARG A 111 13.312 214.314 32.977 1.00147.24 N
ANISOU 829 NE ARG A 111 20353 17647 17943 217 309 13 N
ATOM 830 CZ ARG A 111 12.463 214.254 33.998 1.00152.09 C
ANISOU 830 CZ ARG A 111 20972 18255 18560 314 341 24 C
ATOM 831 NH1 ARG A 111 12.920 214.148 35.238 1.00153.63 N
ANISOU 831 NH1 ARG A 111 21193 18444 18734 278 350 -11 N
ATOM 832 NH2 ARG A 111 11.155 214.299 33.779 1.00151.73 N
ANISOU 832 NH2 ARG A 111 20902 18215 18534 448 365 72 N
ATOM 833 N TYR A 112 18.208 214.023 28.736 1.00101.26 N
ANISOU 833 N TYR A 112 14441 11941 12091 -309 149 -54 N
ATOM 834 CA TYR A 112 18.850 212.855 28.139 1.00 96.01 C
ANISOU 834 CA TYR A 112 13627 11382 11469 -365 111 -59 C
ATOM 835 C TYR A 112 20.369 212.953 28.219 1.00107.27 C
ANISOU 835 C TYR A 112 15069 12835 12853 -509 88 -91 C
ATOM 836 O TYR A 112 21.043 211.964 28.530 1.00109.19 O
ANISOU 836 O TYR A 112 15205 13164 13118 -557 68 -107 O
ATOM 837 CB TYR A 112 18.402 212.688 26.686 1.00 84.53 C
ANISOU 837 CB TYR A 112 12121 9949 10048 -332 95 -28 C
ATOM 838 CG TYR A 112 19.178 211.632 25.925 1.00 74.60 C
ANISOU 838 CG TYR A 112 10734 8788 8823 -399 58 -36 C
ATOM 839 CD1 TYR A 112 18.839 210.290 26.021 1.00 69.47 C
ANISOU 839 CD1 TYR A 112 9942 8219 8233 -358 45 -32 C
ATOM 840 CD2 TYR A 112 20.251 211.979 25.110 1.00 75.69 C
ANISOU 840 CD2 TYR A 112 10896 8935 8928 -502 37 -45 C
ATOM 841 CE1 TYR A 112 19.546 209.323 25.330 1.00 68.17 C
ANISOU 841 CE1 TYR A 112 9670 8137 8095 -414 15 -39 C
ATOM 842 CE2 TYR A 112 20.964 211.019 24.418 1.00 71.11 C
ANISOU 842 CE2 TYR A 112 10200 8444 8374 -556 6 -51 C
ATOM 843 CZ TYR A 112 20.608 209.693 24.531 1.00 67.56 C
ANISOU 843 CZ TYR A 112 9617 8069 7983 -509 -3 -48 C
ATOM 844 OH TYR A 112 21.315 208.734 23.842 1.00 60.67 O
ANISOU 844 OH TYR A 112 8640 7281 7132 -556 -30 -53 O
ATOM 845 N ASN A 113 20.927 214.134 27.938 1.00119.80 N
ANISOU 845 N ASN A 113 16790 14353 14376 -580 93 -98 N
ATOM 846 CA ASN A 113 22.380 214.272 27.886 1.00125.09 C
ANISOU 846 CA ASN A 113 17470 15058 15000 -726 69 -122 C
ATOM 847 C ASN A 113 23.010 214.091 29.261 1.00124.67 C
ANISOU 847 C ASN A 113 17423 15028 14919 -781 72 -152 C
ATOM 848 O ASN A 113 24.084 213.490 29.383 1.00117.87 O
ANISOU 848 O ASN A 113 16482 14252 14050 -872 47 -167 O
ATOM 849 CB ASN A 113 22.759 215.629 27.291 1.00122.07 C
ANISOU 849 CB ASN A 113 17240 14591 14552 -791 73 -120 C
ATOM 850 CG ASN A 113 22.586 215.673 25.785 1.00118.66 C
ANISOU 850 CG ASN A 113 16778 14166 14141 -778 59 -94 C
ATOM 851 OD1 ASN A 113 22.790 214.672 25.096 1.00116.39 O
ANISOU 851 OD1 ASN A 113 16353 13971 13901 -780 33 -86 O
ATOM 852 ND2 ASN A 113 22.208 216.835 25.265 1.00116.02 N
ANISOU 852 ND2 ASN A 113 16579 13734 13770 -761 76 -78 N
ATOM 853 N GLY A 114 22.362 214.603 30.310 1.00131.15 N
ANISOU 853 N GLY A 114 18334 15776 15720 -725 103 -160 N
ATOM 854 CA GLY A 114 22.874 214.403 31.654 1.00134.31 C
ANISOU 854 CA GLY A 114 18738 16200 16096 -771 107 -187 C
ATOM 855 C GLY A 114 22.647 213.014 32.208 1.00127.46 C
ANISOU 855 C GLY A 114 17712 15426 15292 -717 99 -187 C
ATOM 856 O GLY A 114 23.333 212.616 33.155 1.00132.02 O
ANISOU 856 O GLY A 114 18257 16054 15853 -774 93 -208 O
ATOM 857 N LEU A 115 21.707 212.266 31.635 1.00111.78 N
ANISOU 857 N LEU A 115 15629 13466 13376 -613 100 -162 N
ATOM 858 CA LEU A 115 21.362 210.937 32.124 1.00101.65 C
ANISOU 858 CA LEU A 115 14204 12264 12156 -555 94 -159 C
ATOM 859 C LEU A 115 22.117 209.839 31.383 1.00 94.69 C
ANISOU 859 C LEU A 115 13184 11487 11309 -605 61 -157 C
ATOM 860 O LEU A 115 22.685 208.939 32.011 1.00 98.66 O
ANISOU 860 O LEU A 115 13597 12065 11824 -633 51 -169 O
ATOM 861 CB LEU A 115 19.849 210.722 32.005 1.00 97.99 C
ANISOU 861 CB LEU A 115 13717 11773 11744 -414 115 -130 C
ATOM 862 CG LEU A 115 19.272 209.307 32.068 1.00 91.57 C
ANISOU 862 CG LEU A 115 12748 11040 11003 -346 105 -116 C
ATOM 863 CD1 LEU A 115 19.634 208.626 33.372 1.00 91.58 C
ANISOU 863 CD1 LEU A 115 12701 11088 11008 -361 108 -137 C
ATOM 864 CD2 LEU A 115 17.761 209.346 31.888 1.00 92.20 C
ANISOU 864 CD2 LEU A 115 12825 11089 11119 -217 126 -83 C
ATOM 865 N VAL A 116 22.137 209.902 30.056 1.00 80.12 N
ANISOU 865 N VAL A 116 11321 9646 9476 -612 46 -141 N
ATOM 866 CA VAL A 116 22.709 208.855 29.219 1.00 70.20 C
ANISOU 866 CA VAL A 116 9938 8482 8254 -643 18 -136 C
ATOM 867 C VAL A 116 24.064 209.351 28.725 1.00 71.10 C
ANISOU 867 C VAL A 116 10084 8618 8312 -768 -1 -148 C
ATOM 868 O VAL A 116 24.152 210.095 27.744 1.00 77.52 O
ANISOU 868 O VAL A 116 10958 9394 9103 -796 -7 -139 O
ATOM 869 CB VAL A 116 21.778 208.492 28.060 1.00 63.28 C
ANISOU 869 CB VAL A 116 9010 7604 7428 -565 13 -110 C
ATOM 870 CG1 VAL A 116 22.334 207.318 27.285 1.00 51.81 C
ANISOU 870 CG1 VAL A 116 7430 6244 6010 -591 -14 -108 C
ATOM 871 CG2 VAL A 116 20.386 208.173 28.587 1.00 61.24 C
ANISOU 871 CG2 VAL A 116 8732 7322 7214 -446 33 -93 C
ATOM 872 N THR A 117 25.128 208.929 29.401 1.00 68.56 N
ANISOU 872 N THR A 117 9718 8365 7966 -844 -12 -165 N
ATOM 873 CA THR A 117 26.490 209.313 29.064 1.00 70.94 C
ANISOU 873 CA THR A 117 10035 8708 8209 -970 -30 -173 C
ATOM 874 C THR A 117 27.250 208.128 28.479 1.00 66.67 C
ANISOU 874 C THR A 117 9353 8282 7695 -992 -52 -167 C
ATOM 875 O THR A 117 26.789 206.984 28.504 1.00 81.74 O
ANISOU 875 O THR A 117 11159 10234 9663 -917 -52 -161 O
ATOM 876 CB THR A 117 27.221 209.856 30.298 1.00 81.54 C
ANISOU 876 CB THR A 117 11443 10048 9489 -1051 -25 -194 C
ATOM 877 OG1 THR A 117 27.382 208.805 31.258 1.00 78.67 O
ANISOU 877 OG1 THR A 117 10981 9758 9152 -1028 -25 -201 O
ATOM 878 CG2 THR A 117 26.428 210.991 30.927 1.00 89.59 C
ANISOU 878 CG2 THR A 117 12612 10948 10481 -1020 1 -202 C
ATOM 879 N GLY A 118 28.437 208.423 27.954 1.00 67.75 N
ANISOU 879 N GLY A 118 9490 8468 7783 -1097 -70 -167 N
ATOM 880 CA GLY A 118 29.269 207.413 27.328 1.00 64.25 C
ANISOU 880 CA GLY A 118 8924 8135 7353 -1122 -88 -159 C
ATOM 881 C GLY A 118 29.928 206.454 28.297 1.00 73.61 C
ANISOU 881 C GLY A 118 10016 9413 8540 -1132 -89 -165 C
ATOM 882 O GLY A 118 29.984 205.250 28.032 1.00 87.34 O
ANISOU 882 O GLY A 118 11643 11221 10323 -1084 -92 -158 O
ATOM 883 N THR A 119 30.428 206.965 29.425 1.00 78.04 N
ANISOU 883 N THR A 119 10626 9975 9049 -1195 -85 -177 N
ATOM 884 CA THR A 119 31.101 206.103 30.393 1.00 78.39 C
ANISOU 884 CA THR A 119 10583 10114 9089 -1209 -86 -180 C
ATOM 885 C THR A 119 30.124 205.129 31.043 1.00 68.76 C
ANISOU 885 C THR A 119 9305 8883 7938 -1094 -70 -182 C
ATOM 886 O THR A 119 30.478 203.975 31.315 1.00 67.73 O
ANISOU 886 O THR A 119 9066 8837 7832 -1067 -72 -177 O
ATOM 887 CB THR A 119 31.803 206.956 31.451 1.00 79.82 C
ANISOU 887 CB THR A 119 10839 10296 9194 -1308 -86 -193 C
ATOM 888 OG1 THR A 119 32.701 207.869 30.808 1.00 81.58 O
ANISOU 888 OG1 THR A 119 11117 10529 9349 -1424 -102 -188 O
ATOM 889 CG2 THR A 119 32.594 206.085 32.415 1.00 86.30 C
ANISOU 889 CG2 THR A 119 11562 11226 10002 -1329 -89 -191 C
ATOM 890 N ARG A 120 28.894 205.577 31.309 1.00 70.63 N
ANISOU 890 N ARG A 120 9614 9018 8203 -1023 -55 -188 N
ATOM 891 CA ARG A 120 27.880 204.673 31.840 1.00 73.84 C
ANISOU 891 CA ARG A 120 9965 9415 8676 -914 -41 -186 C
ATOM 892 C ARG A 120 27.494 203.618 30.813 1.00 74.52 C
ANISOU 892 C ARG A 120 9956 9534 8824 -848 -48 -171 C
ATOM 893 O ARG A 120 27.239 202.462 31.167 1.00 72.86 O
ANISOU 893 O ARG A 120 9658 9367 8659 -789 -44 -168 O
ATOM 894 CB ARG A 120 26.645 205.460 32.278 1.00 80.85 C
ANISOU 894 CB ARG A 120 10952 10194 9575 -852 -21 -190 C
ATOM 895 CG ARG A 120 26.864 206.390 33.455 1.00 87.64 C
ANISOU 895 CG ARG A 120 11911 11011 10376 -900 -9 -208 C
ATOM 896 CD ARG A 120 25.577 207.123 33.799 1.00 92.43 C
ANISOU 896 CD ARG A 120 12617 11508 10995 -822 15 -208 C
ATOM 897 NE ARG A 120 25.769 208.131 34.837 1.00107.32 N
ANISOU 897 NE ARG A 120 14620 13340 12818 -870 29 -227 N
ATOM 898 CZ ARG A 120 24.818 208.960 35.255 1.00112.97 C
ANISOU 898 CZ ARG A 120 15445 13955 13525 -813 54 -230 C
ATOM 899 NH1 ARG A 120 23.605 208.904 34.723 1.00110.17 N
ANISOU 899 NH1 ARG A 120 15089 13552 13220 -705 67 -211 N
ATOM 900 NH2 ARG A 120 25.079 209.848 36.205 1.00115.56 N
ANISOU 900 NH2 ARG A 120 15885 14233 13789 -863 67 -249 N
ATOM 901 N ALA A 121 27.443 204.000 29.535 1.00 73.63 N
ANISOU 901 N ALA A 121 9865 9399 8711 -860 -58 -163 N
ATOM 902 CA ALA A 121 27.091 203.046 28.490 1.00 58.72 C
ANISOU 902 CA ALA A 121 7896 7540 6875 -805 -66 -150 C
ATOM 903 C ALA A 121 28.118 201.926 28.387 1.00 59.54 C
ANISOU 903 C ALA A 121 7893 7750 6979 -829 -74 -148 C
ATOM 904 O ALA A 121 27.763 200.773 28.119 1.00 73.52 O
ANISOU 904 O ALA A 121 9584 9551 8798 -766 -73 -142 O
ATOM 905 CB ALA A 121 26.951 203.764 27.150 1.00 52.17 C
ANISOU 905 CB ALA A 121 7115 6672 6037 -823 -75 -141 C
ATOM 906 N ALA A 122 29.400 202.247 28.582 1.00 53.60 N
ANISOU 906 N ALA A 122 7139 7058 6167 -919 -81 -150 N
ATOM 907 CA ALA A 122 30.432 201.218 28.519 1.00 53.39 C
ANISOU 907 CA ALA A 122 7010 7141 6133 -936 -86 -143 C
ATOM 908 C ALA A 122 30.279 200.214 29.655 1.00 58.29 C
ANISOU 908 C ALA A 122 7568 7797 6783 -882 -74 -146 C
ATOM 909 O ALA A 122 30.460 199.007 29.455 1.00 52.25 O
ANISOU 909 O ALA A 122 6715 7090 6047 -838 -71 -138 O
ATOM 910 CB ALA A 122 31.818 201.861 28.547 1.00 50.38 C
ANISOU 910 CB ALA A 122 6641 6826 5676 -1048 -97 -140 C
ATOM 911 N GLY A 123 29.942 200.694 30.854 1.00 58.97 N
ANISOU 911 N GLY A 123 7703 7845 6858 -885 -65 -156 N
ATOM 912 CA GLY A 123 29.710 199.784 31.962 1.00 55.33 C
ANISOU 912 CA GLY A 123 7185 7411 6425 -831 -52 -157 C
ATOM 913 C GLY A 123 28.514 198.882 31.731 1.00 52.19 C
ANISOU 913 C GLY A 123 6751 6976 6102 -728 -44 -153 C
ATOM 914 O GLY A 123 28.537 197.701 32.085 1.00 61.67 O
ANISOU 914 O GLY A 123 7875 8224 7334 -681 -38 -148 O
ATOM 915 N ILE A 124 27.453 199.425 31.128 1.00 36.83 N
ANISOU 915 N ILE A 124 4862 4947 4183 -693 -45 -153 N
ATOM 916 CA ILE A 124 26.279 198.614 30.818 1.00 44.75 C
ANISOU 916 CA ILE A 124 5830 5920 5252 -603 -40 -145 C
ATOM 917 C ILE A 124 26.636 197.528 29.815 1.00 49.20 C
ANISOU 917 C ILE A 124 6317 6538 5839 -589 -49 -137 C
ATOM 918 O ILE A 124 26.230 196.368 29.960 1.00 46.47 O
ANISOU 918 O ILE A 124 5910 6211 5536 -532 -43 -133 O
ATOM 919 CB ILE A 124 25.135 199.506 30.302 1.00 35.98 C
ANISOU 919 CB ILE A 124 4793 4720 4156 -572 -40 -142 C
ATOM 920 CG1 ILE A 124 24.712 200.501 31.382 1.00 43.67 C
ANISOU 920 CG1 ILE A 124 5849 5636 5107 -572 -26 -149 C
ATOM 921 CG2 ILE A 124 23.952 198.658 29.861 1.00 31.73 C
ANISOU 921 CG2 ILE A 124 4210 4164 3680 -490 -39 -129 C
ATOM 922 CD1 ILE A 124 23.677 201.497 30.916 1.00 55.08 C
ANISOU 922 CD1 ILE A 124 7377 6994 6556 -539 -21 -142 C
ATOM 923 N ILE A 125 27.405 197.886 28.784 1.00 47.68 N
ANISOU 923 N ILE A 125 6131 6370 5616 -642 -60 -136 N
ATOM 924 CA ILE A 125 27.848 196.900 27.803 1.00 49.82 C
ANISOU 924 CA ILE A 125 6335 6695 5900 -631 -66 -129 C
ATOM 925 C ILE A 125 28.697 195.828 28.472 1.00 53.25 C
ANISOU 925 C ILE A 125 6694 7211 6328 -624 -57 -126 C
ATOM 926 O ILE A 125 28.548 194.632 28.193 1.00 55.46 O
ANISOU 926 O ILE A 125 6918 7514 6641 -572 -52 -122 O
ATOM 927 CB ILE A 125 28.607 197.595 26.657 1.00 48.78 C
ANISOU 927 CB ILE A 125 6227 6580 5728 -694 -79 -126 C
ATOM 928 CG1 ILE A 125 27.658 198.508 25.876 1.00 50.15 C
ANISOU 928 CG1 ILE A 125 6470 6669 5913 -687 -87 -125 C
ATOM 929 CG2 ILE A 125 29.255 196.568 25.739 1.00 51.42 C
ANISOU 929 CG2 ILE A 125 6491 6981 6066 -684 -82 -119 C
ATOM 930 CD1 ILE A 125 28.338 199.332 24.814 1.00 44.33 C
ANISOU 930 CD1 ILE A 125 5769 5940 5135 -753 -99 -121 C
ATOM 931 N ALA A 126 29.591 196.236 29.376 1.00 44.39 N
ANISOU 931 N ALA A 126 5573 6134 5160 -675 -54 -128 N
ATOM 932 CA ALA A 126 30.407 195.266 30.099 1.00 42.63 C
ANISOU 932 CA ALA A 126 5277 5995 4926 -665 -44 -121 C
ATOM 933 C ALA A 126 29.542 194.352 30.960 1.00 40.27 C
ANISOU 933 C ALA A 126 4951 5672 4678 -589 -31 -122 C
ATOM 934 O ALA A 126 29.753 193.134 30.993 1.00 37.58 O
ANISOU 934 O ALA A 126 4546 5376 4357 -544 -22 -114 O
ATOM 935 CB ALA A 126 31.446 195.991 30.954 1.00 41.29 C
ANISOU 935 CB ALA A 126 5117 5879 4692 -743 -46 -120 C
ATOM 936 N ILE A 127 28.557 194.922 31.657 1.00 41.44 N
ANISOU 936 N ILE A 127 5149 5750 4846 -572 -28 -130 N
ATOM 937 CA ILE A 127 27.679 194.119 32.502 1.00 43.50 C
ANISOU 937 CA ILE A 127 5386 5990 5154 -503 -16 -129 C
ATOM 938 C ILE A 127 26.827 193.184 31.652 1.00 44.92 C
ANISOU 938 C ILE A 127 5538 6143 5388 -441 -17 -123 C
ATOM 939 O ILE A 127 26.636 192.011 31.995 1.00 49.86 O
ANISOU 939 O ILE A 127 6114 6788 6044 -393 -8 -117 O
ATOM 940 CB ILE A 127 26.810 195.033 33.386 1.00 40.87 C
ANISOU 940 CB ILE A 127 5116 5590 4824 -497 -12 -137 C
ATOM 941 CG1 ILE A 127 27.676 195.771 34.409 1.00 46.62 C
ANISOU 941 CG1 ILE A 127 5870 6349 5496 -559 -9 -144 C
ATOM 942 CG2 ILE A 127 25.727 194.230 34.088 1.00 30.79 C
ANISOU 942 CG2 ILE A 127 3814 4287 3599 -421 -1 -132 C
ATOM 943 CD1 ILE A 127 26.924 196.832 35.193 1.00 37.08 C
ANISOU 943 CD1 ILE A 127 4742 5068 4278 -560 -3 -154 C
ATOM 944 N CYS A 128 26.313 193.681 30.525 1.00 43.13 N
ANISOU 944 N CYS A 128 5346 5870 5170 -446 -29 -124 N
ATOM 945 CA CYS A 128 25.449 192.860 29.683 1.00 38.98 C
ANISOU 945 CA CYS A 128 4799 5319 4691 -396 -32 -118 C
ATOM 946 C CYS A 128 26.210 191.708 29.037 1.00 44.43 C
ANISOU 946 C CYS A 128 5435 6065 5380 -388 -30 -115 C
ATOM 947 O CYS A 128 25.622 190.653 28.772 1.00 40.62 O
ANISOU 947 O CYS A 128 4926 5573 4935 -342 -27 -111 O
ATOM 948 CB CYS A 128 24.783 193.727 28.616 1.00 46.06 C
ANISOU 948 CB CYS A 128 5746 6162 5592 -406 -46 -117 C
ATOM 949 SG CYS A 128 23.534 194.869 29.258 1.00 47.90 S
ANISOU 949 SG CYS A 128 6045 6318 5836 -384 -43 -114 S
ATOM 950 N TRP A 129 27.509 191.884 28.776 1.00 48.15 N
ANISOU 950 N TRP A 129 5892 6597 5807 -433 -30 -115 N
ATOM 951 CA TRP A 129 28.299 190.786 28.227 1.00 44.09 C
ANISOU 951 CA TRP A 129 5326 6141 5284 -417 -23 -109 C
ATOM 952 C TRP A 129 28.549 189.708 29.275 1.00 47.51 C
ANISOU 952 C TRP A 129 5712 6612 5727 -375 -5 -103 C
ATOM 953 O TRP A 129 28.475 188.512 28.971 1.00 44.29 O
ANISOU 953 O TRP A 129 5275 6213 5340 -329 4 -99 O
ATOM 954 CB TRP A 129 29.622 191.309 27.667 1.00 36.19 C
ANISOU 954 CB TRP A 129 4318 5204 4227 -474 -27 -105 C
ATOM 955 CG TRP A 129 29.534 191.753 26.239 1.00 33.30 C
ANISOU 955 CG TRP A 129 3979 4817 3858 -496 -41 -107 C
ATOM 956 CD1 TRP A 129 29.374 193.029 25.785 1.00 50.34 C
ANISOU 956 CD1 TRP A 129 6190 6938 5998 -546 -56 -111 C
ATOM 957 CD2 TRP A 129 29.599 190.919 25.076 1.00 36.27 C
ANISOU 957 CD2 TRP A 129 4335 5203 4243 -469 -40 -105 C
ATOM 958 NE1 TRP A 129 29.336 193.043 24.412 1.00 49.03 N
ANISOU 958 NE1 TRP A 129 6032 6764 5832 -551 -66 -110 N
ATOM 959 CE2 TRP A 129 29.471 191.760 23.952 1.00 39.02 C
ANISOU 959 CE2 TRP A 129 4720 5525 4580 -506 -57 -107 C
ATOM 960 CE3 TRP A 129 29.751 189.543 24.876 1.00 29.08 C
ANISOU 960 CE3 TRP A 129 3384 4317 3346 -417 -26 -102 C
ATOM 961 CZ2 TRP A 129 29.493 191.272 22.649 1.00 34.54 C
ANISOU 961 CZ2 TRP A 129 4147 4961 4016 -494 -60 -107 C
ATOM 962 CZ3 TRP A 129 29.772 189.060 23.580 1.00 37.82 C
ANISOU 962 CZ3 TRP A 129 4493 5423 4455 -404 -28 -103 C
ATOM 963 CH2 TRP A 129 29.643 189.922 22.484 1.00 39.50 C
ANISOU 963 CH2 TRP A 129 4739 5614 4657 -444 -46 -106 C
ATOM 964 N VAL A 130 28.845 190.112 30.514 1.00 47.63 N
ANISOU 964 N VAL A 130 5724 6649 5724 -392 0 -102 N
ATOM 965 CA VAL A 130 29.056 189.139 31.583 1.00 31.27 C
ANISOU 965 CA VAL A 130 3606 4614 3659 -352 18 -95 C
ATOM 966 C VAL A 130 27.786 188.334 31.829 1.00 38.73 C
ANISOU 966 C VAL A 130 4553 5499 4663 -292 23 -95 C
ATOM 967 O VAL A 130 27.831 187.109 31.989 1.00 50.23 O
ANISOU 967 O VAL A 130 5975 6973 6136 -245 36 -88 O
ATOM 968 CB VAL A 130 29.537 189.845 32.864 1.00 30.24 C
ANISOU 968 CB VAL A 130 3478 4516 3496 -388 20 -94 C
ATOM 969 CG1 VAL A 130 29.615 188.857 34.020 1.00 28.70 C
ANISOU 969 CG1 VAL A 130 3238 4355 3313 -343 38 -85 C
ATOM 970 CG2 VAL A 130 30.887 190.499 32.631 1.00 30.62 C
ANISOU 970 CG2 VAL A 130 3517 4638 3481 -455 15 -89 C
ATOM 971 N LEU A 131 26.634 189.007 31.857 1.00 43.74 N
ANISOU 971 N LEU A 131 5230 6065 5325 -291 12 -102 N
ATOM 972 CA LEU A 131 25.374 188.290 32.015 1.00 43.97 C
ANISOU 972 CA LEU A 131 5257 6045 5406 -240 14 -99 C
ATOM 973 C LEU A 131 25.114 187.366 30.833 1.00 41.58 C
ANISOU 973 C LEU A 131 4945 5730 5125 -218 11 -97 C
ATOM 974 O LEU A 131 24.547 186.279 30.998 1.00 51.32 O
ANISOU 974 O LEU A 131 6161 6950 6390 -178 18 -91 O
ATOM 975 CB LEU A 131 24.221 189.278 32.181 1.00 41.18 C
ANISOU 975 CB LEU A 131 4948 5629 5071 -241 5 -101 C
ATOM 976 CG LEU A 131 24.260 190.198 33.399 1.00 42.65 C
ANISOU 976 CG LEU A 131 5157 5812 5237 -256 11 -105 C
ATOM 977 CD1 LEU A 131 22.993 191.036 33.460 1.00 39.47 C
ANISOU 977 CD1 LEU A 131 4799 5343 4854 -240 6 -103 C
ATOM 978 CD2 LEU A 131 24.444 189.399 34.678 1.00 35.56 C
ANISOU 978 CD2 LEU A 131 4219 4947 4346 -229 26 -100 C
ATOM 979 N SER A 132 25.518 187.781 29.629 1.00 28.06 N
ANISOU 979 N SER A 132 3248 4021 3392 -247 0 -101 N
ATOM 980 CA SER A 132 25.310 186.945 28.452 1.00 30.35 C
ANISOU 980 CA SER A 132 3535 4299 3697 -231 -3 -101 C
ATOM 981 C SER A 132 26.081 185.636 28.565 1.00 28.76 C
ANISOU 981 C SER A 132 3299 4140 3487 -199 16 -97 C
ATOM 982 O SER A 132 25.569 184.571 28.198 1.00 31.52 O
ANISOU 982 O SER A 132 3650 4466 3862 -167 20 -96 O
ATOM 983 CB SER A 132 25.715 187.707 27.191 1.00 27.08 C
ANISOU 983 CB SER A 132 3143 3888 3257 -270 -17 -106 C
ATOM 984 OG SER A 132 25.009 188.931 27.096 1.00 31.04 O
ANISOU 984 OG SER A 132 3683 4346 3763 -294 -32 -107 O
ATOM 985 N PHE A 133 27.313 185.693 29.077 1.00 28.50 N
ANISOU 985 N PHE A 133 3239 4172 3416 -208 29 -93 N
ATOM 986 CA PHE A 133 28.063 184.469 29.339 1.00 24.85 C
ANISOU 986 CA PHE A 133 2743 3756 2943 -167 52 -84 C
ATOM 987 C PHE A 133 27.373 183.624 30.402 1.00 36.78 C
ANISOU 987 C PHE A 133 4244 5242 4488 -124 63 -78 C
ATOM 988 O PHE A 133 27.252 182.401 30.259 1.00 40.77 O
ANISOU 988 O PHE A 133 4746 5737 5007 -81 78 -74 O
ATOM 989 CB PHE A 133 29.492 184.808 29.766 1.00 21.35 C
ANISOU 989 CB PHE A 133 2266 3399 2448 -187 62 -74 C
ATOM 990 CG PHE A 133 30.426 185.057 28.616 1.00 35.29 C
ANISOU 990 CG PHE A 133 4027 5208 4173 -211 59 -72 C
ATOM 991 CD1 PHE A 133 31.135 184.014 28.046 1.00 26.91 C
ANISOU 991 CD1 PHE A 133 2944 4186 3093 -170 79 -63 C
ATOM 992 CD2 PHE A 133 30.598 186.333 28.106 1.00 33.63 C
ANISOU 992 CD2 PHE A 133 3837 4999 3941 -273 40 -78 C
ATOM 993 CE1 PHE A 133 31.997 184.238 26.988 1.00 26.09 C
ANISOU 993 CE1 PHE A 133 2835 4128 2951 -189 79 -59 C
ATOM 994 CE2 PHE A 133 31.459 186.562 27.047 1.00 39.44 C
ANISOU 994 CE2 PHE A 133 4568 5780 4640 -298 37 -74 C
ATOM 995 CZ PHE A 133 32.159 185.513 26.489 1.00 26.75 C
ANISOU 995 CZ PHE A 133 2932 4216 3014 -255 57 -65 C
ATOM 996 N ALA A 134 26.912 184.263 31.481 1.00 33.11 N
ANISOU 996 N ALA A 134 3780 4767 4035 -135 59 -78 N
ATOM 997 CA ALA A 134 26.240 183.529 32.548 1.00 39.88 C
ANISOU 997 CA ALA A 134 4625 5604 4923 -96 70 -72 C
ATOM 998 C ALA A 134 24.996 182.819 32.031 1.00 36.00 C
ANISOU 998 C ALA A 134 4154 5049 4475 -74 63 -73 C
ATOM 999 O ALA A 134 24.742 181.661 32.380 1.00 34.71 O
ANISOU 999 O ALA A 134 3982 4875 4330 -36 77 -65 O
ATOM 1000 CB ALA A 134 25.881 184.479 33.690 1.00 37.52 C
ANISOU 1000 CB ALA A 134 4330 5301 4627 -114 65 -73 C
ATOM 1001 N ILE A 135 24.217 183.493 31.187 1.00 32.76 N
ANISOU 1001 N ILE A 135 3772 4596 4079 -98 43 -80 N
ATOM 1002 CA ILE A 135 22.979 182.909 30.684 1.00 30.72 C
ANISOU 1002 CA ILE A 135 3529 4285 3857 -86 33 -77 C
ATOM 1003 C ILE A 135 23.268 181.851 29.629 1.00 34.59 C
ANISOU 1003 C ILE A 135 4029 4771 4342 -76 38 -81 C
ATOM 1004 O ILE A 135 22.700 180.752 29.658 1.00 35.37 O
ANISOU 1004 O ILE A 135 4135 4844 4462 -54 43 -76 O
ATOM 1005 CB ILE A 135 22.057 184.013 30.138 1.00 31.48 C
ANISOU 1005 CB ILE A 135 3650 4346 3965 -112 10 -79 C
ATOM 1006 CG1 ILE A 135 21.570 184.906 31.281 1.00 28.58 C
ANISOU 1006 CG1 ILE A 135 3282 3973 3606 -110 10 -74 C
ATOM 1007 CG2 ILE A 135 20.890 183.404 29.370 1.00 35.85 C
ANISOU 1007 CG2 ILE A 135 4214 4858 4547 -108 -3 -74 C
ATOM 1008 CD1 ILE A 135 20.735 186.077 30.827 1.00 24.40 C
ANISOU 1008 CD1 ILE A 135 2780 3409 3081 -127 -7 -73 C
ATOM 1009 N GLY A 136 24.158 182.162 28.685 1.00 33.12 N
ANISOU 1009 N GLY A 136 3850 4610 4125 -93 36 -88 N
ATOM 1010 CA GLY A 136 24.404 181.241 27.587 1.00 30.78 C
ANISOU 1010 CA GLY A 136 3570 4306 3820 -83 42 -93 C
ATOM 1011 C GLY A 136 25.139 179.986 28.019 1.00 37.95 C
ANISOU 1011 C GLY A 136 4468 5236 4714 -38 71 -87 C
ATOM 1012 O GLY A 136 24.880 178.897 27.501 1.00 48.84 O
ANISOU 1012 O GLY A 136 5872 6586 6100 -18 79 -89 O
ATOM 1013 N LEU A 137 26.065 180.118 28.970 1.00 35.12 N
ANISOU 1013 N LEU A 137 4077 4932 4336 -23 87 -79 N
ATOM 1014 CA LEU A 137 26.861 178.997 29.447 1.00 38.36 C
ANISOU 1014 CA LEU A 137 4473 5374 4729 27 118 -68 C
ATOM 1015 C LEU A 137 26.300 178.385 30.725 1.00 38.18 C
ANISOU 1015 C LEU A 137 4440 5335 4733 54 128 -58 C
ATOM 1016 O LEU A 137 27.018 177.662 31.425 1.00 46.55 O
ANISOU 1016 O LEU A 137 5480 6431 5777 96 154 -45 O
ATOM 1017 CB LEU A 137 28.310 179.434 29.658 1.00 31.69 C
ANISOU 1017 CB LEU A 137 3590 4613 3836 28 131 -59 C
ATOM 1018 CG LEU A 137 28.992 180.063 28.443 1.00 33.08 C
ANISOU 1018 CG LEU A 137 3772 4818 3981 -1 123 -65 C
ATOM 1019 CD1 LEU A 137 30.469 180.287 28.726 1.00 29.14 C
ANISOU 1019 CD1 LEU A 137 3229 4414 3430 3 139 -50 C
ATOM 1020 CD2 LEU A 137 28.792 179.200 27.202 1.00 19.40 C
ANISOU 1020 CD2 LEU A 137 2076 3046 2248 19 128 -73 C
ATOM 1021 N THR A 138 25.037 178.670 31.045 1.00 38.87 N
ANISOU 1021 N THR A 138 4538 5373 4859 35 109 -61 N
ATOM 1022 CA THR A 138 24.394 178.021 32.185 1.00 42.09 C
ANISOU 1022 CA THR A 138 4938 5762 5293 60 119 -50 C
ATOM 1023 C THR A 138 24.431 176.496 32.114 1.00 37.75 C
ANISOU 1023 C THR A 138 4410 5190 4746 101 141 -44 C
ATOM 1024 O THR A 138 24.626 175.867 33.170 1.00 52.43 O
ANISOU 1024 O THR A 138 6252 7062 6606 136 161 -31 O
ATOM 1025 CB THR A 138 22.952 178.533 32.325 1.00 42.21 C
ANISOU 1025 CB THR A 138 4961 5729 5346 34 94 -51 C
ATOM 1026 OG1 THR A 138 22.967 179.858 32.869 1.00 52.43 O
ANISOU 1026 OG1 THR A 138 6238 7045 6637 11 83 -53 O
ATOM 1027 CG2 THR A 138 22.129 177.629 33.236 1.00 41.18 C
ANISOU 1027 CG2 THR A 138 4829 5573 5245 57 102 -39 C
ATOM 1028 N PRO A 139 24.257 175.844 30.956 1.00 34.56 N
ANISOU 1028 N PRO A 139 4046 4748 4338 100 140 -52 N
ATOM 1029 CA PRO A 139 24.436 174.382 30.921 1.00 31.55 C
ANISOU 1029 CA PRO A 139 3697 4343 3950 142 166 -47 C
ATOM 1030 C PRO A 139 25.771 173.911 31.469 1.00 27.99 C
ANISOU 1030 C PRO A 139 3223 3946 3464 196 201 -34 C
ATOM 1031 O PRO A 139 25.845 172.813 32.037 1.00 30.37 O
ANISOU 1031 O PRO A 139 3540 4234 3765 240 227 -22 O
ATOM 1032 CB PRO A 139 24.293 174.058 29.430 1.00 25.48 C
ANISOU 1032 CB PRO A 139 2976 3536 3169 125 159 -62 C
ATOM 1033 CG PRO A 139 23.355 175.094 28.935 1.00 23.18 C
ANISOU 1033 CG PRO A 139 2680 3227 2901 69 122 -71 C
ATOM 1034 CD PRO A 139 23.703 176.345 29.683 1.00 22.20 C
ANISOU 1034 CD PRO A 139 2506 3152 2776 58 114 -66 C
ATOM 1035 N MET A 140 26.831 174.711 31.328 1.00 37.17 N
ANISOU 1035 N MET A 140 4351 5176 4595 194 203 -33 N
ATOM 1036 CA MET A 140 28.128 174.330 31.872 1.00 32.39 C
ANISOU 1036 CA MET A 140 3714 4640 3952 244 235 -14 C
ATOM 1037 C MET A 140 28.161 174.404 33.391 1.00 37.47 C
ANISOU 1037 C MET A 140 4315 5316 4604 258 243 2 C
ATOM 1038 O MET A 140 29.064 173.828 34.008 1.00 37.32 O
ANISOU 1038 O MET A 140 4273 5350 4559 309 272 22 O
ATOM 1039 CB MET A 140 29.228 175.211 31.282 1.00 38.23 C
ANISOU 1039 CB MET A 140 4422 5451 4651 228 232 -15 C
ATOM 1040 CG MET A 140 29.328 175.128 29.771 1.00 41.99 C
ANISOU 1040 CG MET A 140 4937 5905 5113 219 228 -29 C
ATOM 1041 SD MET A 140 30.829 175.896 29.145 1.00 50.14 S
ANISOU 1041 SD MET A 140 5928 7035 6087 212 234 -21 S
ATOM 1042 CE MET A 140 32.069 174.777 29.790 1.00 48.70 C
ANISOU 1042 CE MET A 140 5718 6923 5862 300 283 10 C
ATOM 1043 N LEU A 141 27.201 175.091 34.007 1.00 51.16 N
ANISOU 1043 N LEU A 141 6041 7024 6374 219 218 -4 N
ATOM 1044 CA LEU A 141 27.109 175.145 35.459 1.00 42.70 C
ANISOU 1044 CA LEU A 141 4935 5977 5312 231 224 9 C
ATOM 1045 C LEU A 141 26.378 173.947 36.052 1.00 44.27 C
ANISOU 1045 C LEU A 141 5156 6125 5538 266 239 20 C
ATOM 1046 O LEU A 141 26.176 173.910 37.271 1.00 51.45 O
ANISOU 1046 O LEU A 141 6040 7050 6460 277 244 32 O
ATOM 1047 CB LEU A 141 26.417 176.439 35.894 1.00 42.11 C
ANISOU 1047 CB LEU A 141 4845 5897 5258 178 195 -1 C
ATOM 1048 CG LEU A 141 27.066 177.743 35.427 1.00 40.24 C
ANISOU 1048 CG LEU A 141 4594 5703 4994 134 178 -11 C
ATOM 1049 CD1 LEU A 141 26.431 178.934 36.128 1.00 39.21 C
ANISOU 1049 CD1 LEU A 141 4456 5565 4879 94 157 -18 C
ATOM 1050 CD2 LEU A 141 28.568 177.712 35.660 1.00 44.10 C
ANISOU 1050 CD2 LEU A 141 5044 6280 5432 152 198 3 C
ATOM 1051 N GLY A 142 25.972 172.977 35.236 1.00 35.16 N
ANISOU 1051 N GLY A 142 4054 4914 4393 280 245 15 N
ATOM 1052 CA GLY A 142 25.345 171.779 35.758 1.00 40.08 C
ANISOU 1052 CA GLY A 142 4706 5486 5035 309 261 26 C
ATOM 1053 C GLY A 142 24.073 171.364 35.047 1.00 46.07 C
ANISOU 1053 C GLY A 142 5517 6163 5823 274 242 14 C
ATOM 1054 O GLY A 142 23.712 170.183 35.057 1.00 60.14 O
ANISOU 1054 O GLY A 142 7344 7897 7610 294 257 20 O
ATOM 1055 N TRP A 143 23.384 172.323 34.425 1.00 42.73 N
ANISOU 1055 N TRP A 143 5091 5728 5417 219 208 -1 N
ATOM 1056 CA TRP A 143 22.115 172.061 33.744 1.00 41.80 C
ANISOU 1056 CA TRP A 143 5011 5545 5324 178 185 -8 C
ATOM 1057 C TRP A 143 22.394 171.491 32.351 1.00 43.65 C
ANISOU 1057 C TRP A 143 5300 5748 5536 175 189 -22 C
ATOM 1058 O TRP A 143 22.207 172.140 31.319 1.00 43.18 O
ANISOU 1058 O TRP A 143 5249 5683 5474 139 167 -37 O
ATOM 1059 CB TRP A 143 21.280 173.333 33.673 1.00 37.20 C
ANISOU 1059 CB TRP A 143 4400 4969 4764 130 151 -14 C
ATOM 1060 CG TRP A 143 19.844 173.097 33.318 1.00 28.59 C
ANISOU 1060 CG TRP A 143 3333 3829 3702 90 127 -11 C
ATOM 1061 CD1 TRP A 143 19.278 171.916 32.938 1.00 26.05 C
ANISOU 1061 CD1 TRP A 143 3058 3457 3383 82 129 -9 C
ATOM 1062 CD2 TRP A 143 18.786 174.066 33.325 1.00 31.76 C
ANISOU 1062 CD2 TRP A 143 3710 4230 4127 53 97 -8 C
ATOM 1063 NE1 TRP A 143 17.935 172.089 32.701 1.00 39.71 N
ANISOU 1063 NE1 TRP A 143 4788 5164 5136 35 100 -3 N
ATOM 1064 CE2 TRP A 143 17.607 173.399 32.933 1.00 30.12 C
ANISOU 1064 CE2 TRP A 143 3528 3982 3936 22 81 -1 C
ATOM 1065 CE3 TRP A 143 18.720 175.431 33.624 1.00 36.13 C
ANISOU 1065 CE3 TRP A 143 4227 4814 4685 44 83 -9 C
ATOM 1066 CZ2 TRP A 143 16.378 174.050 32.830 1.00 22.31 C
ANISOU 1066 CZ2 TRP A 143 2519 2991 2967 -13 53 9 C
ATOM 1067 CZ3 TRP A 143 17.498 176.077 33.521 1.00 23.59 C
ANISOU 1067 CZ3 TRP A 143 2628 3216 3119 15 58 -1 C
ATOM 1068 CH2 TRP A 143 16.344 175.386 33.127 1.00 25.27 C
ANISOU 1068 CH2 TRP A 143 2857 3396 3347 -11 43 10 C
ATOM 1069 N ASN A 144 22.841 170.237 32.336 1.00 33.01 N
ANISOU 1069 N ASN A 144 3996 4376 4170 218 220 -17 N
ATOM 1070 CA ASN A 144 23.238 169.577 31.101 1.00 41.66 C
ANISOU 1070 CA ASN A 144 5151 5440 5236 227 232 -30 C
ATOM 1071 C ASN A 144 22.911 168.092 31.193 1.00 45.33 C
ANISOU 1071 C ASN A 144 5687 5841 5697 248 254 -25 C
ATOM 1072 O ASN A 144 22.417 167.603 32.213 1.00 64.85 O
ANISOU 1072 O ASN A 144 8154 8298 8189 255 260 -9 O
ATOM 1073 CB ASN A 144 24.725 169.789 30.820 1.00 39.21 C
ANISOU 1073 CB ASN A 144 4822 5188 4886 275 257 -30 C
ATOM 1074 CG ASN A 144 25.594 169.404 31.995 1.00 41.26 C
ANISOU 1074 CG ASN A 144 5050 5496 5133 338 291 -7 C
ATOM 1075 OD1 ASN A 144 25.694 168.230 32.346 1.00 42.51 O
ANISOU 1075 OD1 ASN A 144 5247 5623 5282 384 321 4 O
ATOM 1076 ND2 ASN A 144 26.227 170.393 32.615 1.00 52.49 N
ANISOU 1076 ND2 ASN A 144 6400 6993 6549 339 286 1 N
ATOM 1077 N ASN A 145 23.200 167.372 30.108 1.00 39.75 N
ANISOU 1077 N ASN A 145 5049 5094 4961 258 268 -38 N
ATOM 1078 CA ASN A 145 23.019 165.928 30.048 1.00 52.24 C
ANISOU 1078 CA ASN A 145 6715 6605 6527 280 294 -35 C
ATOM 1079 C ASN A 145 24.347 165.181 30.121 1.00 47.32 C
ANISOU 1079 C ASN A 145 6118 5998 5863 370 345 -26 C
ATOM 1080 O ASN A 145 24.420 164.014 29.724 1.00 40.66 O
ANISOU 1080 O ASN A 145 5363 5093 4993 397 373 -28 O
ATOM 1081 CB ASN A 145 22.261 165.537 28.778 1.00 45.11 C
ANISOU 1081 CB ASN A 145 5888 5636 5617 223 275 -56 C
ATOM 1082 CG ASN A 145 20.863 166.125 28.726 1.00 52.80 C
ANISOU 1082 CG ASN A 145 6837 6597 6628 138 226 -58 C
ATOM 1083 OD1 ASN A 145 20.206 166.285 29.755 1.00 46.56 O
ANISOU 1083 OD1 ASN A 145 6004 5817 5869 123 215 -41 O
ATOM 1084 ND2 ASN A 145 20.402 166.452 27.524 1.00 59.66 N
ANISOU 1084 ND2 ASN A 145 7729 7448 7491 84 199 -76 N
ATOM 1085 N CYS A 146 25.401 165.832 30.622 1.00 48.32 N
ANISOU 1085 N CYS A 146 6173 6209 5978 416 359 -13 N
ATOM 1086 CA CYS A 146 26.705 165.182 30.707 1.00 51.31 C
ANISOU 1086 CA CYS A 146 6564 6620 6312 506 409 2 C
ATOM 1087 C CYS A 146 26.688 163.998 31.662 1.00 54.84 C
ANISOU 1087 C CYS A 146 7048 7031 6756 561 444 24 C
ATOM 1088 O CYS A 146 27.479 163.061 31.501 1.00 63.70 O
ANISOU 1088 O CYS A 146 8222 8142 7838 637 489 35 O
ATOM 1089 CB CYS A 146 27.769 166.190 31.140 1.00 60.62 C
ANISOU 1089 CB CYS A 146 7647 7908 7478 532 411 16 C
ATOM 1090 SG CYS A 146 28.186 167.388 29.864 1.00 69.61 S
ANISOU 1090 SG CYS A 146 8755 9092 8600 489 385 -5 S
ATOM 1091 N GLY A 147 25.802 164.019 32.659 1.00 66.08 N
ANISOU 1091 N GLY A 147 8449 8438 8219 526 425 32 N
ATOM 1092 CA GLY A 147 25.737 162.928 33.613 1.00 69.13 C
ANISOU 1092 CA GLY A 147 8871 8792 8605 573 457 54 C
ATOM 1093 C GLY A 147 25.116 161.660 33.067 1.00 61.54 C
ANISOU 1093 C GLY A 147 8027 7722 7632 565 470 46 C
ATOM 1094 O GLY A 147 25.272 160.597 33.676 1.00 69.26 O
ANISOU 1094 O GLY A 147 9055 8663 8596 618 507 65 O
ATOM 1095 N GLN A 148 24.415 161.745 31.936 1.00 61.06 N
ANISOU 1095 N GLN A 148 8017 7608 7574 498 443 19 N
ATOM 1096 CA GLN A 148 23.732 160.600 31.332 1.00 68.04 C
ANISOU 1096 CA GLN A 148 9021 8388 8445 472 450 8 C
ATOM 1097 C GLN A 148 24.097 160.516 29.854 1.00 64.48 C
ANISOU 1097 C GLN A 148 8633 7910 7957 469 454 -18 C
ATOM 1098 O GLN A 148 23.267 160.785 28.977 1.00 54.04 O
ANISOU 1098 O GLN A 148 7336 6553 6644 388 417 -40 O
ATOM 1099 CB GLN A 148 22.216 160.708 31.511 1.00 76.84 C
ANISOU 1099 CB GLN A 148 10136 9462 9599 371 404 3 C
ATOM 1100 CG GLN A 148 21.764 161.222 32.871 1.00 91.25 C
ANISOU 1100 CG GLN A 148 11871 11334 11466 360 387 25 C
ATOM 1101 CD GLN A 148 21.688 162.738 32.927 1.00106.69 C
ANISOU 1101 CD GLN A 148 13719 13369 13450 328 351 20 C
ATOM 1102 OE1 GLN A 148 21.368 163.393 31.933 1.00107.28 O
ANISOU 1102 OE1 GLN A 148 13790 13445 13527 277 320 0 O
ATOM 1103 NE2 GLN A 148 21.989 163.304 34.090 1.00110.97 N
ANISOU 1103 NE2 GLN A 148 14177 13975 14010 358 354 38 N
ATOM 1104 N PRO A 149 25.332 160.127 29.542 1.00 68.13 N
ANISOU 1104 N PRO A 149 9121 8390 8374 560 500 -13 N
ATOM 1105 CA PRO A 149 25.764 160.113 28.142 1.00 73.79 C
ANISOU 1105 CA PRO A 149 9892 9091 9054 565 507 -36 C
ATOM 1106 C PRO A 149 25.152 158.955 27.372 1.00 72.12 C
ANISOU 1106 C PRO A 149 9822 8763 8816 538 517 -55 C
ATOM 1107 O PRO A 149 24.826 157.906 27.933 1.00 80.80 O
ANISOU 1107 O PRO A 149 10996 9795 9910 553 540 -44 O
ATOM 1108 CB PRO A 149 27.285 159.964 28.246 1.00 79.00 C
ANISOU 1108 CB PRO A 149 10532 9815 9671 681 559 -17 C
ATOM 1109 CG PRO A 149 27.483 159.197 29.510 1.00 74.62 C
ANISOU 1109 CG PRO A 149 9982 9255 9117 744 594 14 C
ATOM 1110 CD PRO A 149 26.394 159.656 30.451 1.00 67.40 C
ANISOU 1110 CD PRO A 149 9009 8339 8259 667 550 18 C
ATOM 1111 N LYS A 150 24.994 159.160 26.065 1.00 75.12 N
ANISOU 1111 N LYS A 150 10245 9119 9178 494 500 -83 N
ATOM 1112 CA LYS A 150 24.570 158.094 25.158 1.00 70.30 C
ANISOU 1112 CA LYS A 150 9778 8401 8530 470 512 -105 C
ATOM 1113 C LYS A 150 25.792 157.236 24.861 1.00 71.77 C
ANISOU 1113 C LYS A 150 10043 8570 8658 587 579 -99 C
ATOM 1114 O LYS A 150 26.536 157.478 23.909 1.00 71.50 O
ANISOU 1114 O LYS A 150 10017 8562 8589 623 593 -111 O
ATOM 1115 CB LYS A 150 23.960 158.663 23.883 1.00 64.78 C
ANISOU 1115 CB LYS A 150 9092 7691 7832 379 468 -135 C
ATOM 1116 CG LYS A 150 22.657 159.416 24.089 1.00 60.56 C
ANISOU 1116 CG LYS A 150 8491 7169 7349 266 404 -137 C
ATOM 1117 CD LYS A 150 21.926 159.618 22.768 1.00 71.40 C
ANISOU 1117 CD LYS A 150 9910 8509 8711 174 366 -165 C
ATOM 1118 CE LYS A 150 20.723 160.537 22.928 1.00 77.57 C
ANISOU 1118 CE LYS A 150 10608 9324 9542 73 303 -161 C
ATOM 1119 NZ LYS A 150 19.750 160.020 23.928 1.00 76.40 N
ANISOU 1119 NZ LYS A 150 10466 9143 9421 30 291 -143 N
ATOM 1120 N GLU A 151 26.001 156.215 25.695 1.00 86.04 N
ANISOU 1120 N GLU A 151 11908 10334 10451 652 622 -78 N
ATOM 1121 CA GLU A 151 27.219 155.417 25.596 1.00 87.30 C
ANISOU 1121 CA GLU A 151 12131 10487 10554 782 692 -64 C
ATOM 1122 C GLU A 151 27.240 154.587 24.318 1.00 83.62 C
ANISOU 1122 C GLU A 151 11815 9925 10031 786 716 -92 C
ATOM 1123 O GLU A 151 28.303 154.395 23.716 1.00 87.97 O
ANISOU 1123 O GLU A 151 12395 10497 10532 879 761 -90 O
ATOM 1124 CB GLU A 151 27.357 154.521 26.826 1.00 94.48 C
ANISOU 1124 CB GLU A 151 13068 11367 11461 849 731 -32 C
ATOM 1125 CG GLU A 151 28.761 154.481 27.414 1.00101.56 C
ANISOU 1125 CG GLU A 151 13908 12349 12329 988 786 4 C
ATOM 1126 CD GLU A 151 29.265 155.853 27.831 1.00 99.73 C
ANISOU 1126 CD GLU A 151 13505 12259 12130 985 757 18 C
ATOM 1127 OE1 GLU A 151 29.829 156.570 26.976 1.00 99.47 O
ANISOU 1127 OE1 GLU A 151 13428 12286 12079 989 749 7 O
ATOM 1128 OE2 GLU A 151 29.091 156.217 29.013 1.00 94.64 O
ANISOU 1128 OE2 GLU A 151 12771 11664 11524 976 742 40 O
ATOM 1129 N GLY A 152 26.079 154.090 23.888 1.00 81.23 N
ANISOU 1129 N GLY A 152 11610 9522 9733 684 687 -117 N
ATOM 1130 CA GLY A 152 26.033 153.317 22.657 1.00 86.84 C
ANISOU 1130 CA GLY A 152 12472 10137 10386 675 707 -148 C
ATOM 1131 C GLY A 152 26.405 154.135 21.436 1.00 86.96 C
ANISOU 1131 C GLY A 152 12450 10203 10386 660 688 -171 C
ATOM 1132 O GLY A 152 27.036 153.628 20.505 1.00 95.67 O
ANISOU 1132 O GLY A 152 13649 11270 11431 717 728 -186 O
ATOM 1133 N LYS A 153 26.018 155.412 21.421 1.00 89.98 N
ANISOU 1133 N LYS A 153 12699 10670 10820 586 630 -174 N
ATOM 1134 CA LYS A 153 26.393 156.280 20.311 1.00 75.04 C
ANISOU 1134 CA LYS A 153 10763 8834 8916 572 611 -193 C
ATOM 1135 C LYS A 153 27.888 156.575 20.316 1.00 74.42 C
ANISOU 1135 C LYS A 153 10625 8845 8808 698 658 -173 C
ATOM 1136 O LYS A 153 28.493 156.728 19.248 1.00 72.52 O
ANISOU 1136 O LYS A 153 10407 8620 8526 726 672 -187 O
ATOM 1137 CB LYS A 153 25.587 157.580 20.369 1.00 66.93 C
ANISOU 1137 CB LYS A 153 9609 7871 7948 465 540 -197 C
ATOM 1138 CG LYS A 153 25.810 158.504 19.185 1.00 63.62 C
ANISOU 1138 CG LYS A 153 9150 7502 7520 434 514 -217 C
ATOM 1139 CD LYS A 153 24.913 159.728 19.255 1.00 73.75 C
ANISOU 1139 CD LYS A 153 10323 8837 8860 330 445 -219 C
ATOM 1140 CE LYS A 153 23.443 159.348 19.182 1.00 72.42 C
ANISOU 1140 CE LYS A 153 10210 8594 8712 217 404 -231 C
ATOM 1141 NZ LYS A 153 22.569 160.553 19.130 1.00 74.70 N
ANISOU 1141 NZ LYS A 153 10396 8938 9051 124 340 -230 N
ATOM 1142 N ALA A 154 28.500 156.644 21.500 1.00 72.38 N
ANISOU 1142 N ALA A 154 10288 8648 8564 773 683 -138 N
ATOM 1143 CA ALA A 154 29.929 156.921 21.591 1.00 70.34 C
ANISOU 1143 CA ALA A 154 9964 8489 8274 890 726 -112 C
ATOM 1144 C ALA A 154 30.764 155.702 21.218 1.00 76.72 C
ANISOU 1144 C ALA A 154 10896 9245 9011 1009 800 -105 C
ATOM 1145 O ALA A 154 31.793 155.835 20.545 1.00 76.10 O
ANISOU 1145 O ALA A 154 10808 9222 8885 1087 833 -99 O
ATOM 1146 CB ALA A 154 30.284 157.397 23.000 1.00 67.54 C
ANISOU 1146 CB ALA A 154 9484 8224 7956 925 726 -75 C
ATOM 1147 N HIS A 155 30.345 154.509 21.649 1.00 83.01 N
ANISOU 1147 N HIS A 155 11811 9934 9793 1029 830 -103 N
ATOM 1148 CA HIS A 155 31.086 153.302 21.300 1.00 88.45 C
ANISOU 1148 CA HIS A 155 12635 10560 10411 1147 905 -97 C
ATOM 1149 C HIS A 155 31.001 152.999 19.810 1.00 82.55 C
ANISOU 1149 C HIS A 155 12006 9743 9615 1124 910 -135 C
ATOM 1150 O HIS A 155 31.926 152.401 19.248 1.00 81.67 O
ANISOU 1150 O HIS A 155 11972 9623 9438 1236 972 -130 O
ATOM 1151 CB HIS A 155 30.575 152.112 22.112 1.00 94.72 C
ANISOU 1151 CB HIS A 155 13541 11247 11203 1162 932 -87 C
ATOM 1152 CG HIS A 155 30.946 152.164 23.561 1.00101.66 C
ANISOU 1152 CG HIS A 155 14323 12192 12109 1224 948 -42 C
ATOM 1153 ND1 HIS A 155 32.254 152.176 23.994 1.00106.48 N
ANISOU 1153 ND1 HIS A 155 14870 12900 12689 1363 1000 -2 N
ATOM 1154 CD2 HIS A 155 30.180 152.195 24.678 1.00105.20 C
ANISOU 1154 CD2 HIS A 155 14729 12631 12612 1166 918 -30 C
ATOM 1155 CE1 HIS A 155 32.279 152.220 25.314 1.00109.36 C
ANISOU 1155 CE1 HIS A 155 15156 13309 13087 1385 1001 32 C
ATOM 1156 NE2 HIS A 155 31.034 152.232 25.754 1.00108.11 N
ANISOU 1156 NE2 HIS A 155 15011 13086 12981 1269 952 15 N
ATOM 1157 N SER A 156 29.909 153.400 19.155 1.00 79.34 N
ANISOU 1157 N SER A 156 11616 9292 9237 984 849 -172 N
ATOM 1158 CA SER A 156 29.775 153.153 17.724 1.00 80.35 C
ANISOU 1158 CA SER A 156 11854 9356 9319 952 849 -210 C
ATOM 1159 C SER A 156 30.681 154.066 16.908 1.00 77.16 C
ANISOU 1159 C SER A 156 11361 9059 8896 992 850 -210 C
ATOM 1160 O SER A 156 31.058 153.718 15.783 1.00 77.85 O
ANISOU 1160 O SER A 156 11541 9112 8926 1024 877 -231 O
ATOM 1161 CB SER A 156 28.319 153.328 17.294 1.00 82.55 C
ANISOU 1161 CB SER A 156 12167 9566 9631 787 781 -245 C
ATOM 1162 OG SER A 156 27.843 154.622 17.620 1.00 93.84 O
ANISOU 1162 OG SER A 156 13437 11089 11129 703 715 -240 O
ATOM 1163 N GLN A 157 31.039 155.229 17.450 1.00 81.06 N
ANISOU 1163 N GLN A 157 11683 9681 9435 989 821 -187 N
ATOM 1164 CA GLN A 157 31.901 156.181 16.766 1.00 80.55 C
ANISOU 1164 CA GLN A 157 11522 9727 9355 1017 818 -183 C
ATOM 1165 C GLN A 157 33.335 156.152 17.280 1.00 83.24 C
ANISOU 1165 C GLN A 157 11797 10171 9661 1162 876 -139 C
ATOM 1166 O GLN A 157 34.119 157.047 16.951 1.00 84.41 O
ANISOU 1166 O GLN A 157 11838 10434 9801 1184 871 -126 O
ATOM 1167 CB GLN A 157 31.328 157.593 16.890 1.00 81.05 C
ANISOU 1167 CB GLN A 157 11444 9867 9485 904 743 -188 C
ATOM 1168 CG GLN A 157 29.938 157.743 16.296 1.00 91.30 C
ANISOU 1168 CG GLN A 157 12791 11085 10814 762 683 -226 C
ATOM 1169 CD GLN A 157 29.452 159.175 16.320 1.00102.35 C
ANISOU 1169 CD GLN A 157 14054 12563 12271 666 615 -228 C
ATOM 1170 OE1 GLN A 157 28.295 159.457 16.009 1.00105.84 O
ANISOU 1170 OE1 GLN A 157 14507 12961 12745 551 562 -250 O
ATOM 1171 NE2 GLN A 157 30.339 160.091 16.689 1.00101.05 N
ANISOU 1171 NE2 GLN A 157 13761 12517 12116 711 617 -203 N
ATOM 1172 N GLY A 158 33.693 155.148 18.078 1.00 83.36 N
ANISOU 1172 N GLY A 158 11870 10151 9653 1259 931 -113 N
ATOM 1173 CA GLY A 158 35.061 155.008 18.533 1.00 82.73 C
ANISOU 1173 CA GLY A 158 11733 10169 9531 1405 992 -67 C
ATOM 1174 C GLY A 158 35.503 156.024 19.557 1.00 79.49 C
ANISOU 1174 C GLY A 158 11141 9899 9162 1404 967 -31 C
ATOM 1175 O GLY A 158 36.708 156.209 19.748 1.00 90.50 O
ANISOU 1175 O GLY A 158 12458 11408 10520 1506 1006 8 O
ATOM 1176 N CYS A 159 34.563 156.692 20.221 1.00 72.05 N
ANISOU 1176 N CYS A 159 10130 8955 8293 1290 905 -41 N
ATOM 1177 CA CYS A 159 34.916 157.667 21.243 1.00 74.00 C
ANISOU 1177 CA CYS A 159 10213 9325 8578 1280 880 -10 C
ATOM 1178 C CYS A 159 35.656 156.995 22.394 1.00 73.30 C
ANISOU 1178 C CYS A 159 10106 9276 8468 1398 934 37 C
ATOM 1179 O CYS A 159 35.404 155.836 22.734 1.00 81.51 O
ANISOU 1179 O CYS A 159 11258 10220 9494 1448 972 41 O
ATOM 1180 CB CYS A 159 33.662 158.365 21.774 1.00 72.77 C
ANISOU 1180 CB CYS A 159 10007 9141 8500 1144 808 -31 C
ATOM 1181 SG CYS A 159 32.754 159.363 20.568 1.00 78.35 S
ANISOU 1181 SG CYS A 159 10707 9825 9238 1002 738 -78 S
ATOM 1182 N GLY A 160 36.584 157.737 22.995 1.00 71.33 N
ANISOU 1182 N GLY A 160 9716 9172 8215 1439 937 75 N
ATOM 1183 CA GLY A 160 37.308 157.232 24.140 1.00 82.46 C
ANISOU 1183 CA GLY A 160 11082 10636 9614 1528 970 128 C
ATOM 1184 C GLY A 160 36.513 157.356 25.425 1.00 87.29 C
ANISOU 1184 C GLY A 160 11657 11229 10280 1483 949 129 C
ATOM 1185 O GLY A 160 35.448 157.972 25.477 1.00 83.77 O
ANISOU 1185 O GLY A 160 11193 10740 9894 1359 888 97 O
ATOM 1186 N GLU A 161 37.049 156.748 26.481 1.00100.76 N
ANISOU 1186 N GLU A 161 13339 12963 11982 1549 969 178 N
ATOM 1187 CA GLU A 161 36.407 156.829 27.785 1.00103.57 C
ANISOU 1187 CA GLU A 161 13655 13314 12385 1520 956 185 C
ATOM 1188 C GLU A 161 36.373 158.272 28.270 1.00 91.79 C
ANISOU 1188 C GLU A 161 12010 11934 10931 1444 908 183 C
ATOM 1189 O GLU A 161 37.329 159.031 28.086 1.00 78.83 O
ANISOU 1189 O GLU A 161 10269 10413 9270 1447 893 205 O
ATOM 1190 CB GLU A 161 37.135 155.946 28.798 1.00115.44 C
ANISOU 1190 CB GLU A 161 15151 14839 13871 1597 977 244 C
ATOM 1191 CG GLU A 161 36.758 154.475 28.724 1.00127.56 C
ANISOU 1191 CG GLU A 161 16846 16236 15386 1650 1020 243 C
ATOM 1192 CD GLU A 161 37.356 153.666 29.857 1.00141.52 C
ANISOU 1192 CD GLU A 161 18604 18027 17140 1721 1039 303 C
ATOM 1193 OE1 GLU A 161 38.372 154.109 30.433 1.00147.90 O
ANISOU 1193 OE1 GLU A 161 19293 18966 17938 1747 1025 350 O
ATOM 1194 OE2 GLU A 161 36.807 152.590 30.179 1.00141.98 O
ANISOU 1194 OE2 GLU A 161 18778 17973 17195 1745 1068 303 O
ATOM 1195 N GLY A 162 35.258 158.650 28.890 1.00 96.84 N
ANISOU 1195 N GLY A 162 12633 12525 11636 1342 857 163 N
ATOM 1196 CA GLY A 162 35.045 160.015 29.314 1.00 88.91 C
ANISOU 1196 CA GLY A 162 11504 11603 10676 1249 799 157 C
ATOM 1197 C GLY A 162 34.610 160.960 28.219 1.00 89.78 C
ANISOU 1197 C GLY A 162 11604 11704 10804 1151 751 118 C
ATOM 1198 O GLY A 162 34.402 162.149 28.496 1.00 97.94 O
ANISOU 1198 O GLY A 162 12543 12798 11872 1072 703 111 O
ATOM 1199 N GLN A 163 34.465 160.478 26.989 1.00 80.61 N
ANISOU 1199 N GLN A 163 10542 10469 9618 1155 762 92 N
ATOM 1200 CA GLN A 163 34.050 161.294 25.860 1.00 72.30 C
ANISOU 1200 CA GLN A 163 9488 9404 8578 1067 719 55 C
ATOM 1201 C GLN A 163 32.658 160.892 25.393 1.00 66.74 C
ANISOU 1201 C GLN A 163 8885 8564 7909 984 689 16 C
ATOM 1202 O GLN A 163 32.147 159.818 25.724 1.00 73.31 O
ANISOU 1202 O GLN A 163 9809 9302 8742 1005 710 15 O
ATOM 1203 CB GLN A 163 35.040 161.171 24.696 1.00 71.40 C
ANISOU 1203 CB GLN A 163 9400 9328 8402 1131 753 57 C
ATOM 1204 CG GLN A 163 36.386 161.821 24.948 1.00 71.00 C
ANISOU 1204 CG GLN A 163 9231 9431 8313 1190 771 96 C
ATOM 1205 CD GLN A 163 37.263 161.822 23.715 1.00 73.97 C
ANISOU 1205 CD GLN A 163 9626 9850 8631 1240 798 96 C
ATOM 1206 OE1 GLN A 163 37.097 160.993 22.820 1.00 75.22 O
ANISOU 1206 OE1 GLN A 163 9900 9920 8761 1273 825 76 O
ATOM 1207 NE2 GLN A 163 38.199 162.762 23.655 1.00 82.43 N
ANISOU 1207 NE2 GLN A 163 10584 11056 9678 1241 791 120 N
ATOM 1208 N VAL A 164 32.044 161.783 24.616 1.00 54.88 N
ANISOU 1208 N VAL A 164 7364 7055 6433 886 638 -15 N
ATOM 1209 CA VAL A 164 30.731 161.556 24.032 1.00 55.69 C
ANISOU 1209 CA VAL A 164 7549 7047 6565 797 603 -50 C
ATOM 1210 C VAL A 164 30.778 161.971 22.569 1.00 51.79 C
ANISOU 1210 C VAL A 164 7082 6548 6048 760 586 -78 C
ATOM 1211 O VAL A 164 31.693 162.666 22.123 1.00 49.18 O
ANISOU 1211 O VAL A 164 6689 6306 5693 786 591 -70 O
ATOM 1212 CB VAL A 164 29.613 162.334 24.762 1.00 56.66 C
ANISOU 1212 CB VAL A 164 7607 7167 6754 697 545 -57 C
ATOM 1213 CG1 VAL A 164 29.592 161.994 26.244 1.00 59.46 C
ANISOU 1213 CG1 VAL A 164 7927 7535 7130 732 560 -28 C
ATOM 1214 CG2 VAL A 164 29.785 163.830 24.550 1.00 61.27 C
ANISOU 1214 CG2 VAL A 164 8083 7839 7357 644 504 -60 C
ATOM 1215 N ALA A 165 29.776 161.523 21.819 1.00 54.43 N
ANISOU 1215 N ALA A 165 7513 6781 6389 695 566 -109 N
ATOM 1216 CA ALA A 165 29.529 162.068 20.490 1.00 50.26 C
ANISOU 1216 CA ALA A 165 7001 6244 5851 634 537 -138 C
ATOM 1217 C ALA A 165 28.944 163.464 20.653 1.00 50.97 C
ANISOU 1217 C ALA A 165 6985 6389 5994 542 476 -142 C
ATOM 1218 O ALA A 165 27.819 163.619 21.138 1.00 51.20 O
ANISOU 1218 O ALA A 165 7006 6380 6070 469 438 -147 O
ATOM 1219 CB ALA A 165 28.586 161.162 19.706 1.00 49.46 C
ANISOU 1219 CB ALA A 165 7034 6021 5738 584 531 -168 C
ATOM 1220 N CYS A 166 29.708 164.483 20.268 1.00 52.03 N
ANISOU 1220 N CYS A 166 7038 6613 6117 548 467 -137 N
ATOM 1221 CA CYS A 166 29.325 165.870 20.525 1.00 53.58 C
ANISOU 1221 CA CYS A 166 7133 6867 6358 474 416 -136 C
ATOM 1222 C CYS A 166 28.179 166.253 19.598 1.00 60.40 C
ANISOU 1222 C CYS A 166 8030 7676 7244 376 368 -164 C
ATOM 1223 O CYS A 166 28.389 166.581 18.429 1.00 54.93 O
ANISOU 1223 O CYS A 166 7354 6991 6527 358 360 -180 O
ATOM 1224 CB CYS A 166 30.517 166.800 20.341 1.00 58.29 C
ANISOU 1224 CB CYS A 166 7644 7573 6929 504 423 -121 C
ATOM 1225 SG CYS A 166 30.185 168.504 20.827 1.00 62.43 S
ANISOU 1225 SG CYS A 166 8053 8168 7502 421 368 -117 S
ATOM 1226 N LEU A 167 26.956 166.209 20.125 1.00 60.60 N
ANISOU 1226 N LEU A 167 8062 7650 7314 313 336 -168 N
ATOM 1227 CA LEU A 167 25.763 166.621 19.402 1.00 52.10 C
ANISOU 1227 CA LEU A 167 7002 6533 6261 217 287 -188 C
ATOM 1228 C LEU A 167 24.932 167.521 20.302 1.00 56.34 C
ANISOU 1228 C LEU A 167 7458 7095 6853 163 247 -176 C
ATOM 1229 O LEU A 167 24.862 167.299 21.515 1.00 67.76 O
ANISOU 1229 O LEU A 167 8877 8547 8322 187 258 -159 O
ATOM 1230 CB LEU A 167 24.942 165.411 18.944 1.00 42.39 C
ANISOU 1230 CB LEU A 167 5886 5202 5017 189 291 -204 C
ATOM 1231 CG LEU A 167 25.620 164.539 17.885 1.00 45.03 C
ANISOU 1231 CG LEU A 167 6318 5498 5292 234 328 -221 C
ATOM 1232 CD1 LEU A 167 24.826 163.266 17.645 1.00 59.96 C
ANISOU 1232 CD1 LEU A 167 8332 7283 7166 206 335 -235 C
ATOM 1233 CD2 LEU A 167 25.792 165.320 16.592 1.00 32.26 C
ANISOU 1233 CD2 LEU A 167 4689 3911 3657 200 306 -237 C
ATOM 1234 N PHE A 168 24.304 168.536 19.702 1.00 51.17 N
ANISOU 1234 N PHE A 168 6768 6456 6219 94 203 -184 N
ATOM 1235 CA PHE A 168 23.630 169.569 20.486 1.00 43.44 C
ANISOU 1235 CA PHE A 168 5708 5509 5286 53 168 -172 C
ATOM 1236 C PHE A 168 22.533 168.979 21.366 1.00 54.42 C
ANISOU 1236 C PHE A 168 7113 6854 6710 27 158 -163 C
ATOM 1237 O PHE A 168 22.457 169.275 22.564 1.00 49.33 O
ANISOU 1237 O PHE A 168 6414 6237 6094 42 158 -146 O
ATOM 1238 CB PHE A 168 23.059 170.640 19.555 1.00 33.58 C
ANISOU 1238 CB PHE A 168 4435 4275 4047 -13 125 -181 C
ATOM 1239 CG PHE A 168 22.481 171.829 20.275 1.00 38.98 C
ANISOU 1239 CG PHE A 168 5041 4995 4773 -46 94 -167 C
ATOM 1240 CD1 PHE A 168 21.170 171.813 20.737 1.00 38.40 C
ANISOU 1240 CD1 PHE A 168 4962 4894 4735 -91 66 -159 C
ATOM 1241 CD2 PHE A 168 23.247 172.967 20.486 1.00 36.30 C
ANISOU 1241 CD2 PHE A 168 4639 4720 4434 -32 93 -161 C
ATOM 1242 CE1 PHE A 168 20.635 172.906 21.402 1.00 36.43 C
ANISOU 1242 CE1 PHE A 168 4645 4677 4520 -112 42 -145 C
ATOM 1243 CE2 PHE A 168 22.719 174.067 21.148 1.00 26.74 C
ANISOU 1243 CE2 PHE A 168 3369 3535 3257 -59 67 -150 C
ATOM 1244 CZ PHE A 168 21.411 174.037 21.607 1.00 34.23 C
ANISOU 1244 CZ PHE A 168 4312 4452 4240 -95 43 -142 C
ATOM 1245 N GLU A 169 21.667 168.144 20.788 1.00 55.61 N
ANISOU 1245 N GLU A 169 7338 6939 6854 -16 147 -173 N
ATOM 1246 CA GLU A 169 20.543 167.602 21.545 1.00 51.17 C
ANISOU 1246 CA GLU A 169 6787 6337 6319 -53 133 -162 C
ATOM 1247 C GLU A 169 20.981 166.646 22.642 1.00 50.24 C
ANISOU 1247 C GLU A 169 6691 6199 6199 7 173 -150 C
ATOM 1248 O GLU A 169 20.222 166.426 23.593 1.00 63.47 O
ANISOU 1248 O GLU A 169 8350 7863 7904 -12 164 -134 O
ATOM 1249 CB GLU A 169 19.567 166.887 20.613 1.00 71.94 C
ANISOU 1249 CB GLU A 169 9497 8905 8934 -122 112 -175 C
ATOM 1250 CG GLU A 169 20.174 165.751 19.807 1.00103.77 C
ANISOU 1250 CG GLU A 169 13634 12879 12915 -95 146 -195 C
ATOM 1251 CD GLU A 169 20.744 166.211 18.480 1.00115.75 C
ANISOU 1251 CD GLU A 169 15166 14413 14401 -96 143 -214 C
ATOM 1252 OE1 GLU A 169 20.943 167.432 18.303 1.00111.24 O
ANISOU 1252 OE1 GLU A 169 14516 13904 13846 -102 122 -210 O
ATOM 1253 OE2 GLU A 169 20.987 165.348 17.610 1.00113.87 O
ANISOU 1253 OE2 GLU A 169 15022 14123 14119 -92 162 -233 O
ATOM 1254 N ASP A 170 22.179 166.075 22.533 1.00 45.57 N
ANISOU 1254 N ASP A 170 6135 5608 5572 81 217 -154 N
ATOM 1255 CA ASP A 170 22.655 165.102 23.504 1.00 58.32 C
ANISOU 1255 CA ASP A 170 7778 7204 7178 147 259 -140 C
ATOM 1256 C ASP A 170 23.299 165.735 24.730 1.00 47.31 C
ANISOU 1256 C ASP A 170 6290 5882 5805 197 271 -118 C
ATOM 1257 O ASP A 170 23.433 165.059 25.756 1.00 58.97 O
ANISOU 1257 O ASP A 170 7773 7348 7286 239 297 -101 O
ATOM 1258 CB ASP A 170 23.656 164.143 22.847 1.00 68.65 C
ANISOU 1258 CB ASP A 170 9171 8481 8433 214 307 -149 C
ATOM 1259 CG ASP A 170 23.056 163.378 21.677 1.00 73.48 C
ANISOU 1259 CG ASP A 170 9892 9012 9016 166 300 -173 C
ATOM 1260 OD1 ASP A 170 21.820 163.428 21.504 1.00 74.14 O
ANISOU 1260 OD1 ASP A 170 9987 9062 9122 78 259 -178 O
ATOM 1261 OD2 ASP A 170 23.819 162.720 20.936 1.00 75.36 O
ANISOU 1261 OD2 ASP A 170 10204 9222 9205 216 336 -185 O
ATOM 1262 N VAL A 171 23.689 167.007 24.663 1.00 38.26 N
ANISOU 1262 N VAL A 171 5061 4807 4669 190 252 -117 N
ATOM 1263 CA VAL A 171 24.408 167.623 25.774 1.00 36.75 C
ANISOU 1263 CA VAL A 171 4788 4688 4489 233 264 -97 C
ATOM 1264 C VAL A 171 23.603 168.762 26.392 1.00 43.07 C
ANISOU 1264 C VAL A 171 5515 5518 5334 178 224 -92 C
ATOM 1265 O VAL A 171 23.657 168.981 27.608 1.00 36.47 O
ANISOU 1265 O VAL A 171 4628 4713 4517 197 229 -75 O
ATOM 1266 CB VAL A 171 25.802 168.108 25.328 1.00 35.68 C
ANISOU 1266 CB VAL A 171 4620 4621 4316 281 286 -97 C
ATOM 1267 CG1 VAL A 171 26.676 166.922 24.952 1.00 35.01 C
ANISOU 1267 CG1 VAL A 171 4603 4515 4184 356 335 -95 C
ATOM 1268 CG2 VAL A 171 25.695 169.076 24.162 1.00 34.82 C
ANISOU 1268 CG2 VAL A 171 4499 4528 4204 229 254 -114 C
ATOM 1269 N VAL A 172 22.851 169.487 25.573 1.00 40.14 N
ANISOU 1269 N VAL A 172 5140 5137 4976 114 186 -105 N
ATOM 1270 CA VAL A 172 22.077 170.642 26.019 1.00 50.45 C
ANISOU 1270 CA VAL A 172 6381 6468 6318 67 149 -99 C
ATOM 1271 C VAL A 172 20.639 170.189 26.250 1.00 50.43 C
ANISOU 1271 C VAL A 172 6400 6416 6344 20 126 -93 C
ATOM 1272 O VAL A 172 19.990 169.725 25.299 1.00 40.22 O
ANISOU 1272 O VAL A 172 5160 5079 5043 -22 111 -103 O
ATOM 1273 CB VAL A 172 22.136 171.787 24.997 1.00 35.38 C
ANISOU 1273 CB VAL A 172 4452 4586 4404 31 123 -111 C
ATOM 1274 CG1 VAL A 172 21.384 172.999 25.516 1.00 23.13 C
ANISOU 1274 CG1 VAL A 172 2842 3060 2887 -6 91 -102 C
ATOM 1275 CG2 VAL A 172 23.584 172.139 24.683 1.00 36.90 C
ANISOU 1275 CG2 VAL A 172 4627 4832 4562 72 146 -114 C
ATOM 1276 N PRO A 173 20.107 170.300 27.468 1.00 46.19 N
ANISOU 1276 N PRO A 173 5823 5889 5837 21 123 -76 N
ATOM 1277 CA PRO A 173 18.736 169.837 27.718 1.00 33.82 C
ANISOU 1277 CA PRO A 173 4272 4284 4295 -25 102 -66 C
ATOM 1278 C PRO A 173 17.719 170.752 27.057 1.00 40.22 C
ANISOU 1278 C PRO A 173 5057 5102 5121 -86 60 -66 C
ATOM 1279 O PRO A 173 17.895 171.972 27.001 1.00 59.01 O
ANISOU 1279 O PRO A 173 7389 7525 7509 -87 46 -66 O
ATOM 1280 CB PRO A 173 18.613 169.881 29.247 1.00 30.29 C
ANISOU 1280 CB PRO A 173 3777 3859 3872 3 112 -45 C
ATOM 1281 CG PRO A 173 20.008 170.083 29.764 1.00 24.94 C
ANISOU 1281 CG PRO A 173 3074 3224 3178 66 144 -46 C
ATOM 1282 CD PRO A 173 20.748 170.808 28.689 1.00 41.97 C
ANISOU 1282 CD PRO A 173 5228 5405 5312 64 139 -63 C
ATOM 1283 N MET A 174 16.634 170.150 26.567 1.00 29.12 N
ANISOU 1283 N MET A 174 3688 3658 3716 -140 39 -62 N
ATOM 1284 CA MET A 174 15.653 170.919 25.810 1.00 25.28 C
ANISOU 1284 CA MET A 174 3180 3185 3239 -197 -1 -58 C
ATOM 1285 C MET A 174 14.831 171.837 26.708 1.00 38.74 C
ANISOU 1285 C MET A 174 4814 4929 4978 -203 -20 -35 C
ATOM 1286 O MET A 174 14.375 172.893 26.255 1.00 53.26 O
ANISOU 1286 O MET A 174 6618 6795 6824 -224 -45 -30 O
ATOM 1287 CB MET A 174 14.745 169.975 25.025 1.00 27.97 C
ANISOU 1287 CB MET A 174 3579 3482 3565 -259 -19 -59 C
ATOM 1288 CG MET A 174 14.307 170.522 23.677 1.00 40.91 C
ANISOU 1288 CG MET A 174 5225 5127 5191 -309 -50 -66 C
ATOM 1289 SD MET A 174 15.688 171.138 22.690 1.00 56.38 S
ANISOU 1289 SD MET A 174 7198 7100 7125 -273 -35 -94 S
ATOM 1290 CE MET A 174 16.775 169.711 22.679 1.00 65.00 C
ANISOU 1290 CE MET A 174 8371 8142 8184 -228 10 -113 C
ATOM 1291 N ASN A 175 14.636 171.463 27.977 1.00 43.71 N
ANISOU 1291 N ASN A 175 5423 5561 5626 -181 -6 -19 N
ATOM 1292 CA ASN A 175 13.883 172.329 28.881 1.00 43.53 C
ANISOU 1292 CA ASN A 175 5334 5575 5631 -179 -20 4 C
ATOM 1293 C ASN A 175 14.639 173.618 29.182 1.00 43.06 C
ANISOU 1293 C ASN A 175 5232 5553 5576 -141 -13 -3 C
ATOM 1294 O ASN A 175 14.014 174.654 29.437 1.00 40.81 O
ANISOU 1294 O ASN A 175 4904 5296 5307 -146 -30 10 O
ATOM 1295 CB ASN A 175 13.536 171.584 30.174 1.00 44.30 C
ANISOU 1295 CB ASN A 175 5421 5667 5745 -164 -5 22 C
ATOM 1296 CG ASN A 175 14.753 170.985 30.868 1.00 52.45 C
ANISOU 1296 CG ASN A 175 6472 6690 6768 -108 33 12 C
ATOM 1297 OD1 ASN A 175 15.854 171.535 30.820 1.00 76.84 O
ANISOU 1297 OD1 ASN A 175 9550 9799 9846 -70 48 -2 O
ATOM 1298 ND2 ASN A 175 14.551 169.850 31.526 1.00 42.55 N
ANISOU 1298 ND2 ASN A 175 5244 5408 5516 -104 49 23 N
ATOM 1299 N TYR A 176 15.973 173.578 29.161 1.00 45.55 N
ANISOU 1299 N TYR A 176 5561 5873 5874 -104 11 -22 N
ATOM 1300 CA TYR A 176 16.745 174.813 29.246 1.00 34.96 C
ANISOU 1300 CA TYR A 176 4187 4569 4528 -82 14 -30 C
ATOM 1301 C TYR A 176 16.500 175.686 28.024 1.00 30.43 C
ANISOU 1301 C TYR A 176 3618 3999 3947 -115 -11 -38 C
ATOM 1302 O TYR A 176 16.254 176.891 28.143 1.00 46.73 O
ANISOU 1302 O TYR A 176 5650 6086 6020 -119 -25 -32 O
ATOM 1303 CB TYR A 176 18.238 174.504 29.386 1.00 27.45 C
ANISOU 1303 CB TYR A 176 3247 3631 3553 -41 45 -44 C
ATOM 1304 CG TYR A 176 19.126 175.688 29.055 1.00 35.17 C
ANISOU 1304 CG TYR A 176 4203 4646 4515 -36 43 -55 C
ATOM 1305 CD1 TYR A 176 19.374 176.680 29.996 1.00 46.90 C
ANISOU 1305 CD1 TYR A 176 5646 6166 6006 -23 45 -49 C
ATOM 1306 CD2 TYR A 176 19.704 175.819 27.796 1.00 25.10 C
ANISOU 1306 CD2 TYR A 176 2952 3369 3214 -48 40 -70 C
ATOM 1307 CE1 TYR A 176 20.177 177.763 29.696 1.00 38.03 C
ANISOU 1307 CE1 TYR A 176 4511 5075 4865 -28 43 -59 C
ATOM 1308 CE2 TYR A 176 20.505 176.900 27.487 1.00 30.94 C
ANISOU 1308 CE2 TYR A 176 3673 4145 3938 -50 37 -78 C
ATOM 1309 CZ TYR A 176 20.737 177.870 28.442 1.00 39.05 C
ANISOU 1309 CZ TYR A 176 4663 5205 4971 -42 38 -72 C
ATOM 1310 OH TYR A 176 21.535 178.949 28.144 1.00 33.52 O
ANISOU 1310 OH TYR A 176 3949 4538 4249 -53 35 -79 O
ATOM 1311 N MET A 177 16.565 175.086 26.833 1.00 35.70 N
ANISOU 1311 N MET A 177 4328 4642 4596 -139 -17 -50 N
ATOM 1312 CA MET A 177 16.411 175.854 25.603 1.00 46.65 C
ANISOU 1312 CA MET A 177 5720 6033 5972 -170 -40 -57 C
ATOM 1313 C MET A 177 15.023 176.467 25.485 1.00 43.50 C
ANISOU 1313 C MET A 177 5295 5641 5592 -204 -71 -37 C
ATOM 1314 O MET A 177 14.872 177.547 24.903 1.00 49.96 O
ANISOU 1314 O MET A 177 6098 6475 6408 -215 -88 -35 O
ATOM 1315 CB MET A 177 16.700 174.965 24.392 1.00 40.22 C
ANISOU 1315 CB MET A 177 4962 5189 5131 -190 -39 -74 C
ATOM 1316 CG MET A 177 18.165 174.607 24.208 1.00 28.75 C
ANISOU 1316 CG MET A 177 3533 3741 3652 -150 -8 -93 C
ATOM 1317 SD MET A 177 19.184 176.065 23.924 1.00 49.91 S
ANISOU 1317 SD MET A 177 6178 6468 6319 -137 -9 -101 S
ATOM 1318 CE MET A 177 18.301 176.842 22.571 1.00 36.06 C
ANISOU 1318 CE MET A 177 4430 4707 4564 -191 -47 -101 C
ATOM 1319 N VAL A 178 14.003 175.805 26.027 1.00 33.35 N
ANISOU 1319 N VAL A 178 4003 4345 4322 -220 -78 -18 N
ATOM 1320 CA VAL A 178 12.624 176.252 25.865 1.00 33.44 C
ANISOU 1320 CA VAL A 178 3986 4372 4346 -252 -108 8 C
ATOM 1321 C VAL A 178 12.219 177.160 27.019 1.00 38.51 C
ANISOU 1321 C VAL A 178 4577 5044 5011 -220 -105 28 C
ATOM 1322 O VAL A 178 11.798 178.303 26.804 1.00 28.68 O
ANISOU 1322 O VAL A 178 3307 3819 3769 -217 -118 39 O
ATOM 1323 CB VAL A 178 11.666 175.054 25.749 1.00 29.79 C
ANISOU 1323 CB VAL A 178 3543 3893 3883 -295 -120 22 C
ATOM 1324 CG1 VAL A 178 10.224 175.531 25.726 1.00 28.27 C
ANISOU 1324 CG1 VAL A 178 3307 3732 3701 -325 -149 56 C
ATOM 1325 CG2 VAL A 178 11.984 174.250 24.502 1.00 20.05 C
ANISOU 1325 CG2 VAL A 178 2370 2627 2622 -331 -125 1 C
ATOM 1326 N TYR A 179 12.340 176.661 28.251 1.00 33.57 N
ANISOU 1326 N TYR A 179 3940 4417 4399 -193 -85 34 N
ATOM 1327 CA TYR A 179 11.873 177.416 29.410 1.00 35.57 C
ANISOU 1327 CA TYR A 179 4148 4695 4671 -163 -81 53 C
ATOM 1328 C TYR A 179 12.841 178.533 29.787 1.00 34.32 C
ANISOU 1328 C TYR A 179 3982 4549 4508 -127 -66 38 C
ATOM 1329 O TYR A 179 12.424 179.675 30.013 1.00 33.07 O
ANISOU 1329 O TYR A 179 3803 4407 4354 -114 -72 49 O
ATOM 1330 CB TYR A 179 11.659 176.473 30.597 1.00 29.30 C
ANISOU 1330 CB TYR A 179 3345 3898 3891 -150 -65 65 C
ATOM 1331 CG TYR A 179 10.452 175.572 30.462 1.00 39.45 C
ANISOU 1331 CG TYR A 179 4628 5180 5181 -191 -82 90 C
ATOM 1332 CD1 TYR A 179 9.282 176.028 29.867 1.00 51.08 C
ANISOU 1332 CD1 TYR A 179 6078 6677 6654 -222 -111 114 C
ATOM 1333 CD2 TYR A 179 10.479 174.268 30.940 1.00 42.70 C
ANISOU 1333 CD2 TYR A 179 5063 5568 5593 -200 -70 91 C
ATOM 1334 CE1 TYR A 179 8.175 175.208 29.747 1.00 51.42 C
ANISOU 1334 CE1 TYR A 179 6115 6726 6697 -268 -129 140 C
ATOM 1335 CE2 TYR A 179 9.379 173.441 30.823 1.00 38.50 C
ANISOU 1335 CE2 TYR A 179 4534 5034 5061 -247 -88 115 C
ATOM 1336 CZ TYR A 179 8.230 173.916 30.227 1.00 53.11 C
ANISOU 1336 CZ TYR A 179 6356 6914 6911 -285 -118 139 C
ATOM 1337 OH TYR A 179 7.133 173.093 30.110 1.00 68.02 O
ANISOU 1337 OH TYR A 179 8242 8809 8793 -340 -137 165 O
ATOM 1338 N PHE A 180 14.136 178.225 29.862 1.00 33.82 N
ANISOU 1338 N PHE A 180 3940 4479 4432 -111 -46 14 N
ATOM 1339 CA PHE A 180 15.105 179.208 30.334 1.00 41.50 C
ANISOU 1339 CA PHE A 180 4903 5470 5395 -86 -32 1 C
ATOM 1340 C PHE A 180 15.546 180.138 29.209 1.00 39.86 C
ANISOU 1340 C PHE A 180 4712 5265 5170 -103 -44 -12 C
ATOM 1341 O PHE A 180 15.428 181.363 29.319 1.00 44.33 O
ANISOU 1341 O PHE A 180 5269 5839 5734 -99 -50 -9 O
ATOM 1342 CB PHE A 180 16.313 178.497 30.954 1.00 47.11 C
ANISOU 1342 CB PHE A 180 5619 6186 6094 -61 -5 -12 C
ATOM 1343 CG PHE A 180 17.234 179.412 31.718 1.00 56.09 C
ANISOU 1343 CG PHE A 180 6740 7350 7220 -40 9 -20 C
ATOM 1344 CD1 PHE A 180 18.238 180.114 31.067 1.00 53.61 C
ANISOU 1344 CD1 PHE A 180 6437 7051 6881 -48 9 -36 C
ATOM 1345 CD2 PHE A 180 17.096 179.567 33.087 1.00 41.67 C
ANISOU 1345 CD2 PHE A 180 4890 5539 5405 -16 21 -10 C
ATOM 1346 CE1 PHE A 180 19.088 180.954 31.765 1.00 27.67 C
ANISOU 1346 CE1 PHE A 180 3138 3794 3579 -40 20 -42 C
ATOM 1347 CE2 PHE A 180 17.942 180.406 33.793 1.00 35.28 C
ANISOU 1347 CE2 PHE A 180 4070 4756 4580 -4 32 -17 C
ATOM 1348 CZ PHE A 180 18.940 181.100 33.130 1.00 34.23 C
ANISOU 1348 CZ PHE A 180 3949 4638 4420 -19 31 -34 C
ATOM 1349 N ASN A 181 16.056 179.573 28.115 1.00 32.82 N
ANISOU 1349 N ASN A 181 3847 4361 4261 -121 -47 -27 N
ATOM 1350 CA ASN A 181 16.653 180.398 27.069 1.00 47.05 C
ANISOU 1350 CA ASN A 181 5665 6170 6044 -137 -55 -41 C
ATOM 1351 C ASN A 181 15.586 181.121 26.253 1.00 49.76 C
ANISOU 1351 C ASN A 181 6007 6507 6392 -162 -82 -28 C
ATOM 1352 O ASN A 181 15.585 182.354 26.164 1.00 57.76 O
ANISOU 1352 O ASN A 181 7016 7528 7401 -160 -88 -25 O
ATOM 1353 CB ASN A 181 17.541 179.538 26.167 1.00 37.23 C
ANISOU 1353 CB ASN A 181 4450 4918 4777 -143 -47 -59 C
ATOM 1354 CG ASN A 181 18.367 180.369 25.197 1.00 41.98 C
ANISOU 1354 CG ASN A 181 5063 5534 5354 -156 -51 -73 C
ATOM 1355 OD1 ASN A 181 17.946 180.626 24.069 1.00 47.83 O
ANISOU 1355 OD1 ASN A 181 5819 6265 6089 -183 -71 -74 O
ATOM 1356 ND2 ASN A 181 19.550 180.793 25.635 1.00 27.76 N
ANISOU 1356 ND2 ASN A 181 3253 3760 3535 -140 -34 -82 N
ATOM 1357 N PHE A 182 14.664 180.369 25.651 1.00 32.42 N
ANISOU 1357 N PHE A 182 3817 4299 4202 -186 -98 -18 N
ATOM 1358 CA PHE A 182 13.700 180.973 24.735 1.00 39.25 C
ANISOU 1358 CA PHE A 182 4679 5168 5068 -211 -125 -2 C
ATOM 1359 C PHE A 182 12.672 181.816 25.482 1.00 41.08 C
ANISOU 1359 C PHE A 182 4878 5415 5317 -193 -131 26 C
ATOM 1360 O PHE A 182 12.558 183.025 25.251 1.00 41.63 O
ANISOU 1360 O PHE A 182 4944 5491 5381 -184 -137 32 O
ATOM 1361 CB PHE A 182 13.012 179.887 23.905 1.00 33.61 C
ANISOU 1361 CB PHE A 182 3980 4442 4349 -250 -142 2 C
ATOM 1362 CG PHE A 182 11.977 180.414 22.954 1.00 45.01 C
ANISOU 1362 CG PHE A 182 5414 5899 5788 -279 -171 22 C
ATOM 1363 CD1 PHE A 182 12.208 181.574 22.230 1.00 41.49 C
ANISOU 1363 CD1 PHE A 182 4971 5462 5333 -277 -180 20 C
ATOM 1364 CD2 PHE A 182 10.779 179.741 22.771 1.00 44.95 C
ANISOU 1364 CD2 PHE A 182 5395 5899 5785 -312 -191 46 C
ATOM 1365 CE1 PHE A 182 11.260 182.060 21.350 1.00 42.35 C
ANISOU 1365 CE1 PHE A 182 5069 5586 5435 -300 -206 42 C
ATOM 1366 CE2 PHE A 182 9.825 180.221 21.891 1.00 45.84 C
ANISOU 1366 CE2 PHE A 182 5492 6035 5889 -339 -219 69 C
ATOM 1367 CZ PHE A 182 10.067 181.382 21.179 1.00 42.17 C
ANISOU 1367 CZ PHE A 182 5029 5578 5415 -330 -225 67 C
ATOM 1368 N PHE A 183 11.908 181.192 26.382 1.00 30.18 N
ANISOU 1368 N PHE A 183 3473 4039 3953 -185 -129 45 N
ATOM 1369 CA PHE A 183 10.809 181.896 27.039 1.00 31.41 C
ANISOU 1369 CA PHE A 183 3595 4215 4123 -164 -134 76 C
ATOM 1370 C PHE A 183 11.318 183.045 27.903 1.00 40.44 C
ANISOU 1370 C PHE A 183 4738 5360 5267 -123 -116 71 C
ATOM 1371 O PHE A 183 10.887 184.193 27.746 1.00 35.82 O
ANISOU 1371 O PHE A 183 4151 4781 4677 -107 -121 85 O
ATOM 1372 CB PHE A 183 9.982 180.923 27.883 1.00 34.28 C
ANISOU 1372 CB PHE A 183 3934 4589 4503 -165 -133 98 C
ATOM 1373 CG PHE A 183 9.062 180.048 27.080 1.00 26.34 C
ANISOU 1373 CG PHE A 183 2925 3591 3494 -212 -156 115 C
ATOM 1374 CD1 PHE A 183 8.943 180.209 25.710 1.00 34.34 C
ANISOU 1374 CD1 PHE A 183 3954 4603 4490 -247 -178 112 C
ATOM 1375 CD2 PHE A 183 8.306 179.067 27.698 1.00 36.60 C
ANISOU 1375 CD2 PHE A 183 4206 4898 4803 -228 -159 135 C
ATOM 1376 CE1 PHE A 183 8.095 179.403 24.970 1.00 37.30 C
ANISOU 1376 CE1 PHE A 183 4329 4988 4857 -298 -201 128 C
ATOM 1377 CE2 PHE A 183 7.456 178.260 26.964 1.00 29.98 C
ANISOU 1377 CE2 PHE A 183 3368 4067 3955 -282 -182 152 C
ATOM 1378 CZ PHE A 183 7.351 178.429 25.598 1.00 26.27 C
ANISOU 1378 CZ PHE A 183 2916 3599 3467 -318 -204 148 C
ATOM 1379 N ALA A 184 12.239 182.754 28.823 1.00 25.52 N
ANISOU 1379 N ALA A 184 2853 3464 3378 -106 -94 52 N
ATOM 1380 CA ALA A 184 12.651 183.750 29.807 1.00 34.12 C
ANISOU 1380 CA ALA A 184 3943 4557 4466 -73 -76 48 C
ATOM 1381 C ALA A 184 13.635 184.760 29.223 1.00 35.23 C
ANISOU 1381 C ALA A 184 4114 4690 4584 -82 -75 27 C
ATOM 1382 O ALA A 184 13.458 185.973 29.385 1.00 38.00 O
ANISOU 1382 O ALA A 184 4476 5036 4927 -67 -74 32 O
ATOM 1383 CB ALA A 184 13.257 183.057 31.029 1.00 33.91 C
ANISOU 1383 CB ALA A 184 3905 4533 4445 -56 -55 39 C
ATOM 1384 N CYS A 185 14.676 184.285 28.541 1.00 32.79 N
ANISOU 1384 N CYS A 185 3821 4379 4261 -104 -74 4 N
ATOM 1385 CA CYS A 185 15.790 185.141 28.155 1.00 35.42 C
ANISOU 1385 CA CYS A 185 4177 4712 4568 -116 -70 -17 C
ATOM 1386 C CYS A 185 15.698 185.677 26.731 1.00 39.29 C
ANISOU 1386 C CYS A 185 4687 5195 5046 -141 -89 -18 C
ATOM 1387 O CYS A 185 16.501 186.542 26.364 1.00 34.55 O
ANISOU 1387 O CYS A 185 4109 4596 4424 -154 -88 -30 O
ATOM 1388 CB CYS A 185 17.116 184.389 28.328 1.00 29.80 C
ANISOU 1388 CB CYS A 185 3466 4015 3843 -120 -55 -37 C
ATOM 1389 SG CYS A 185 17.447 183.866 30.027 1.00 47.94 S
ANISOU 1389 SG CYS A 185 5739 6326 6148 -90 -31 -36 S
ATOM 1390 N VAL A 186 14.754 185.194 25.921 1.00 32.51 N
ANISOU 1390 N VAL A 186 3823 4333 4198 -153 -107 -3 N
ATOM 1391 CA VAL A 186 14.577 185.654 24.549 1.00 32.38 C
ANISOU 1391 CA VAL A 186 3822 4313 4168 -177 -126 -2 C
ATOM 1392 C VAL A 186 13.174 186.206 24.319 1.00 41.78 C
ANISOU 1392 C VAL A 186 5000 5506 5369 -168 -142 30 C
ATOM 1393 O VAL A 186 13.010 187.343 23.867 1.00 39.89 O
ANISOU 1393 O VAL A 186 4776 5262 5118 -164 -148 38 O
ATOM 1394 CB VAL A 186 14.898 184.533 23.532 1.00 39.93 C
ANISOU 1394 CB VAL A 186 4788 5268 5117 -206 -134 -15 C
ATOM 1395 CG1 VAL A 186 14.498 184.958 22.124 1.00 41.94 C
ANISOU 1395 CG1 VAL A 186 5054 5522 5359 -232 -157 -9 C
ATOM 1396 CG2 VAL A 186 16.379 184.184 23.581 1.00 45.32 C
ANISOU 1396 CG2 VAL A 186 5484 5955 5782 -206 -116 -42 C
ATOM 1397 N LEU A 187 12.146 185.418 24.644 1.00 46.24 N
ANISOU 1397 N LEU A 187 6344 5136 6090 883 301 347 N
ATOM 1398 CA LEU A 187 10.772 185.825 24.360 1.00 38.89 C
ANISOU 1398 CA LEU A 187 5356 4125 5296 859 218 328 C
ATOM 1399 C LEU A 187 10.358 187.029 25.202 1.00 44.94 C
ANISOU 1399 C LEU A 187 6047 4805 6225 845 111 287 C
ATOM 1400 O LEU A 187 9.786 187.995 24.682 1.00 56.19 O
ANISOU 1400 O LEU A 187 7434 6150 7767 837 7 260 O
ATOM 1401 CB LEU A 187 9.822 184.649 24.596 1.00 51.57 C
ANISOU 1401 CB LEU A 187 7016 5784 6793 867 276 333 C
ATOM 1402 CG LEU A 187 8.481 184.707 23.866 1.00 58.64 C
ANISOU 1402 CG LEU A 187 7878 6622 7781 847 218 325 C
ATOM 1403 CD1 LEU A 187 8.718 184.852 22.375 1.00 58.65 C
ANISOU 1403 CD1 LEU A 187 7875 6603 7804 841 202 341 C
ATOM 1404 CD2 LEU A 187 7.637 183.472 24.157 1.00 55.35 C
ANISOU 1404 CD2 LEU A 187 7524 6268 7240 859 285 331 C
ATOM 1405 N VAL A 188 10.632 186.987 26.507 1.00 53.35 N
ANISOU 1405 N VAL A 188 7115 5894 7263 855 134 275 N
ATOM 1406 CA VAL A 188 10.248 188.100 27.382 1.00 48.86 C
ANISOU 1406 CA VAL A 188 6489 5252 6822 853 34 226 C
ATOM 1407 C VAL A 188 10.971 189.390 27.020 1.00 51.46 C
ANISOU 1407 C VAL A 188 6803 5532 7217 863 -38 206 C
ATOM 1408 O VAL A 188 10.305 190.437 26.915 1.00 62.41 O
ANISOU 1408 O VAL A 188 8208 6872 8633 884 -88 184 O
ATOM 1409 CB VAL A 188 10.436 187.702 28.855 1.00 39.59 C
ANISOU 1409 CB VAL A 188 5325 4119 5599 862 81 220 C
ATOM 1410 CG1 VAL A 188 10.528 188.937 29.736 1.00 22.19 C
ANISOU 1410 CG1 VAL A 188 3080 1856 3496 872 -10 168 C
ATOM 1411 CG2 VAL A 188 9.294 186.805 29.311 1.00 20.63 C
ANISOU 1411 CG2 VAL A 188 2946 1742 3150 860 114 222 C
ATOM 1412 N PRO A 189 12.297 189.415 26.822 1.00 53.44 N
ANISOU 1412 N PRO A 189 7054 5813 7438 862 3 230 N
ATOM 1413 CA PRO A 189 12.934 190.679 26.418 1.00 34.86 C
ANISOU 1413 CA PRO A 189 4696 3417 5132 876 -58 214 C
ATOM 1414 C PRO A 189 12.410 191.232 25.103 1.00 32.92 C
ANISOU 1414 C PRO A 189 4469 3136 4905 879 -84 226 C
ATOM 1415 O PRO A 189 12.248 192.452 24.975 1.00 39.85 O
ANISOU 1415 O PRO A 189 5325 3981 5835 881 -75 237 O
ATOM 1416 CB PRO A 189 14.419 190.306 26.327 1.00 25.85 C
ANISOU 1416 CB PRO A 189 3552 2326 3944 871 9 248 C
ATOM 1417 CG PRO A 189 14.569 189.158 27.250 1.00 28.59 C
ANISOU 1417 CG PRO A 189 3933 2751 4179 877 110 270 C
ATOM 1418 CD PRO A 189 13.306 188.373 27.100 1.00 36.37 C
ANISOU 1418 CD PRO A 189 4937 3745 5138 870 125 273 C
ATOM 1419 N LEU A 190 12.138 190.371 24.119 1.00 37.18 N
ANISOU 1419 N LEU A 190 5013 3688 5427 860 -71 248 N
ATOM 1420 CA LEU A 190 11.601 190.854 22.850 1.00 31.48 C
ANISOU 1420 CA LEU A 190 4308 2932 4722 861 -93 261 C
ATOM 1421 C LEU A 190 10.222 191.475 23.035 1.00 42.30 C
ANISOU 1421 C LEU A 190 5663 4270 6140 858 -84 261 C
ATOM 1422 O LEU A 190 9.910 192.504 22.424 1.00 37.31 O
ANISOU 1422 O LEU A 190 4963 3603 5609 824 -78 283 O
ATOM 1423 CB LEU A 190 11.547 189.716 21.830 1.00 31.10 C
ANISOU 1423 CB LEU A 190 4262 2909 4645 840 -70 287 C
ATOM 1424 CG LEU A 190 12.891 189.250 21.263 1.00 36.99 C
ANISOU 1424 CG LEU A 190 5009 3704 5343 835 -5 324 C
ATOM 1425 CD1 LEU A 190 12.708 188.038 20.363 1.00 33.10 C
ANISOU 1425 CD1 LEU A 190 4549 3264 4761 832 74 359 C
ATOM 1426 CD2 LEU A 190 13.581 190.377 20.510 1.00 27.65 C
ANISOU 1426 CD2 LEU A 190 3822 2478 4205 841 -60 322 C
ATOM 1427 N LEU A 191 9.381 190.864 23.875 1.00 35.57 N
ANISOU 1427 N LEU A 191 4823 3426 5265 864 -87 240 N
ATOM 1428 CA LEU A 191 8.084 191.459 24.180 1.00 34.46 C
ANISOU 1428 CA LEU A 191 4633 3257 5205 841 -71 243 C
ATOM 1429 C LEU A 191 8.249 192.802 24.878 1.00 46.87 C
ANISOU 1429 C LEU A 191 6102 4801 6905 803 -74 239 C
ATOM 1430 O LEU A 191 7.452 193.724 24.665 1.00 44.75 O
ANISOU 1430 O LEU A 191 5726 4494 6783 741 -105 235 O
ATOM 1431 CB LEU A 191 7.254 190.509 25.042 1.00 43.94 C
ANISOU 1431 CB LEU A 191 5874 4475 6346 860 -75 218 C
ATOM 1432 CG LEU A 191 6.697 189.257 24.362 1.00 44.70 C
ANISOU 1432 CG LEU A 191 6009 4585 6389 858 -99 215 C
ATOM 1433 CD1 LEU A 191 6.013 188.355 25.378 1.00 28.76 C
ANISOU 1433 CD1 LEU A 191 3983 2589 4355 850 -101 193 C
ATOM 1434 CD2 LEU A 191 5.735 189.643 23.251 1.00 31.41 C
ANISOU 1434 CD2 LEU A 191 4316 2872 4747 844 -86 240 C
ATOM 1435 N LEU A 192 9.278 192.929 25.719 1.00 46.65 N
ANISOU 1435 N LEU A 192 6093 4793 6840 828 -65 227 N
ATOM 1436 CA LEU A 192 9.562 194.212 26.355 1.00 31.74 C
ANISOU 1436 CA LEU A 192 4103 2878 5080 786 -81 216 C
ATOM 1437 C LEU A 192 9.953 195.260 25.320 1.00 35.29 C
ANISOU 1437 C LEU A 192 4471 3297 5642 737 -114 230 C
ATOM 1438 O LEU A 192 9.496 196.407 25.384 1.00 40.13 O
ANISOU 1438 O LEU A 192 4962 3871 6414 670 -165 213 O
ATOM 1439 CB LEU A 192 10.663 194.051 27.403 1.00 39.06 C
ANISOU 1439 CB LEU A 192 5078 3836 5929 830 -62 204 C
ATOM 1440 CG LEU A 192 10.289 193.316 28.692 1.00 46.38 C
ANISOU 1440 CG LEU A 192 6054 4787 6783 864 -49 179 C
ATOM 1441 CD1 LEU A 192 11.450 193.337 29.671 1.00 45.19 C
ANISOU 1441 CD1 LEU A 192 5930 4661 6577 897 -45 162 C
ATOM 1442 CD2 LEU A 192 9.046 193.925 29.323 1.00 59.69 C
ANISOU 1442 CD2 LEU A 192 7648 6440 8592 815 -62 162 C
ATOM 1443 N MET A 193 10.805 194.887 24.358 1.00 38.29 N
ANISOU 1443 N MET A 193 4913 3693 5942 766 -97 256 N
ATOM 1444 CA MET A 193 11.162 195.817 23.289 1.00 38.20 C
ANISOU 1444 CA MET A 193 4829 3653 6031 721 -129 272 C
ATOM 1445 C MET A 193 9.926 196.273 22.527 1.00 36.77 C
ANISOU 1445 C MET A 193 4565 3437 5972 660 -174 271 C
ATOM 1446 O MET A 193 9.798 197.455 22.185 1.00 46.66 O
ANISOU 1446 O MET A 193 5702 4654 7375 595 -233 262 O
ATOM 1447 CB MET A 193 12.161 195.174 22.324 1.00 37.23 C
ANISOU 1447 CB MET A 193 4797 3557 5794 765 -103 299 C
ATOM 1448 CG MET A 193 13.427 194.645 22.965 1.00 56.89 C
ANISOU 1448 CG MET A 193 7367 6085 8162 821 -78 293 C
ATOM 1449 SD MET A 193 14.508 193.885 21.738 1.00 64.60 S
ANISOU 1449 SD MET A 193 8423 7088 9034 851 -78 311 S
ATOM 1450 CE MET A 193 15.476 192.788 22.771 1.00 64.48 C
ANISOU 1450 CE MET A 193 8453 7122 8925 878 -81 284 C
ATOM 1451 N LEU A 194 9.004 195.346 22.253 1.00 42.02 N
ANISOU 1451 N LEU A 194 5284 4110 6572 680 -156 276 N
ATOM 1452 CA LEU A 194 7.770 195.703 21.563 1.00 47.73 C
ANISOU 1452 CA LEU A 194 5931 4802 7404 626 -201 274 C
ATOM 1453 C LEU A 194 6.991 196.758 22.337 1.00 45.68 C
ANISOU 1453 C LEU A 194 5544 4509 7304 562 -259 238 C
ATOM 1454 O LEU A 194 6.454 197.702 21.746 1.00 47.42 O
ANISOU 1454 O LEU A 194 5655 4696 7668 496 -325 229 O
ATOM 1455 CB LEU A 194 6.915 194.455 21.344 1.00 48.97 C
ANISOU 1455 CB LEU A 194 6176 4977 7454 664 -167 282 C
ATOM 1456 CG LEU A 194 5.539 194.689 20.719 1.00 43.41 C
ANISOU 1456 CG LEU A 194 5401 4242 6849 614 -209 278 C
ATOM 1457 CD1 LEU A 194 5.677 195.326 19.346 1.00 36.60 C
ANISOU 1457 CD1 LEU A 194 4485 3357 6066 574 -250 296 C
ATOM 1458 CD2 LEU A 194 4.760 193.390 20.635 1.00 36.49 C
ANISOU 1458 CD2 LEU A 194 4622 3388 5856 657 -170 286 C
ATOM 1459 N GLY A 195 6.926 196.619 23.663 1.00 43.58 N
ANISOU 1459 N GLY A 195 5288 4254 7016 579 -241 215 N
ATOM 1460 CA GLY A 195 6.241 197.612 24.470 1.00 38.01 C
ANISOU 1460 CA GLY A 195 4462 3519 6459 519 -298 176 C
ATOM 1461 C GLY A 195 6.979 198.934 24.536 1.00 46.20 C
ANISOU 1461 C GLY A 195 5402 4534 7620 472 -349 161 C
ATOM 1462 O GLY A 195 6.352 199.996 24.598 1.00 47.65 O
ANISOU 1462 O GLY A 195 5459 4684 7961 403 -421 132 O
ATOM 1463 N VAL A 196 8.313 198.893 24.524 1.00 43.06 N
ANISOU 1463 N VAL A 196 5056 4154 7150 507 -315 178 N
ATOM 1464 CA VAL A 196 9.087 200.130 24.538 1.00 48.44 C
ANISOU 1464 CA VAL A 196 5650 4815 7942 464 -361 166 C
ATOM 1465 C VAL A 196 8.877 200.901 23.242 1.00 60.35 C
ANISOU 1465 C VAL A 196 7075 6294 9560 408 -421 176 C
ATOM 1466 O VAL A 196 8.669 202.121 23.257 1.00 64.92 O
ANISOU 1466 O VAL A 196 7530 6842 10296 341 -495 149 O
ATOM 1467 CB VAL A 196 10.577 199.831 24.786 1.00 52.36 C
ANISOU 1467 CB VAL A 196 6228 5340 8326 520 -308 185 C
ATOM 1468 CG1 VAL A 196 11.413 201.083 24.574 1.00 38.45 C
ANISOU 1468 CG1 VAL A 196 4379 3555 6674 475 -355 178 C
ATOM 1469 CG2 VAL A 196 10.783 199.290 26.191 1.00 52.96 C
ANISOU 1469 CG2 VAL A 196 6364 5442 8318 566 -263 168 C
ATOM 1470 N TYR A 197 8.919 200.206 22.102 1.00 52.94 N
ANISOU 1470 N TYR A 197 6205 5367 8544 434 -394 212 N
ATOM 1471 CA TYR A 197 8.701 200.882 20.828 1.00 46.00 C
ANISOU 1471 CA TYR A 197 5252 4462 7763 383 -452 223 C
ATOM 1472 C TYR A 197 7.264 201.357 20.682 1.00 50.93 C
ANISOU 1472 C TYR A 197 5778 5059 8516 324 -518 199 C
ATOM 1473 O TYR A 197 7.016 202.374 20.025 1.00 51.66 O
ANISOU 1473 O TYR A 197 5762 5123 8744 262 -592 191 O
ATOM 1474 CB TYR A 197 9.084 199.969 19.665 1.00 42.43 C
ANISOU 1474 CB TYR A 197 4901 4030 7192 428 -405 266 C
ATOM 1475 CG TYR A 197 10.577 199.853 19.471 1.00 50.75 C
ANISOU 1475 CG TYR A 197 6018 5104 8159 469 -363 290 C
ATOM 1476 CD1 TYR A 197 11.325 200.945 19.051 1.00 36.68 C
ANISOU 1476 CD1 TYR A 197 4160 3303 6475 428 -409 291 C
ATOM 1477 CD2 TYR A 197 11.239 198.655 19.707 1.00 45.89 C
ANISOU 1477 CD2 TYR A 197 5540 4529 7368 548 -283 309 C
ATOM 1478 CE1 TYR A 197 12.690 200.849 18.876 1.00 44.24 C
ANISOU 1478 CE1 TYR A 197 5174 4279 7355 465 -371 313 C
ATOM 1479 CE2 TYR A 197 12.604 198.549 19.533 1.00 47.98 C
ANISOU 1479 CE2 TYR A 197 5861 4814 7554 586 -249 328 C
ATOM 1480 CZ TYR A 197 13.324 199.649 19.118 1.00 45.00 C
ANISOU 1480 CZ TYR A 197 5406 4416 7276 544 -291 331 C
ATOM 1481 OH TYR A 197 14.686 199.548 18.944 1.00 52.12 O
ANISOU 1481 OH TYR A 197 6363 5339 8101 582 -257 351 O
ATOM 1482 N LEU A 198 6.306 200.643 21.278 1.00 44.06 N
ANISOU 1482 N LEU A 198 4940 4196 7603 342 -495 187 N
ATOM 1483 CA LEU A 198 4.936 201.144 21.297 1.00 48.81 C
ANISOU 1483 CA LEU A 198 5442 4773 8332 286 -560 160 C
ATOM 1484 C LEU A 198 4.850 202.460 22.058 1.00 51.55 C
ANISOU 1484 C LEU A 198 5656 5094 8836 225 -630 117 C
ATOM 1485 O LEU A 198 4.101 203.363 21.669 1.00 50.80 O
ANISOU 1485 O LEU A 198 5442 4972 8886 162 -710 97 O
ATOM 1486 CB LEU A 198 3.997 200.107 21.911 1.00 47.45 C
ANISOU 1486 CB LEU A 198 5335 4616 8079 321 -517 155 C
ATOM 1487 CG LEU A 198 3.607 198.942 21.004 1.00 61.63 C
ANISOU 1487 CG LEU A 198 7230 6428 9759 362 -472 189 C
ATOM 1488 CD1 LEU A 198 2.667 197.999 21.734 1.00 73.00 C
ANISOU 1488 CD1 LEU A 198 8727 7883 11129 392 -434 180 C
ATOM 1489 CD2 LEU A 198 2.976 199.453 19.717 1.00 57.35 C
ANISOU 1489 CD2 LEU A 198 6615 5861 9314 313 -534 197 C
ATOM 1490 N ARG A 199 5.619 202.589 23.140 1.00 53.14 N
ANISOU 1490 N ARG A 199 5875 5305 9010 245 -604 101 N
ATOM 1491 CA ARG A 199 5.632 203.838 23.894 1.00 52.62 C
ANISOU 1491 CA ARG A 199 5687 5216 9089 188 -669 58 C
ATOM 1492 C ARG A 199 6.348 204.943 23.126 1.00 60.74 C
ANISOU 1492 C ARG A 199 6636 6224 10217 143 -725 62 C
ATOM 1493 O ARG A 199 5.943 206.110 23.190 1.00 66.86 O
ANISOU 1493 O ARG A 199 7280 6973 11151 77 -808 29 O
ATOM 1494 CB ARG A 199 6.287 203.618 25.257 1.00 53.54 C
ANISOU 1494 CB ARG A 199 5852 5349 9141 225 -622 41 C
ATOM 1495 CG ARG A 199 5.456 202.779 26.215 1.00 63.78 C
ANISOU 1495 CG ARG A 199 7198 6661 10376 255 -584 26 C
ATOM 1496 CD ARG A 199 6.107 202.696 27.586 1.00 82.53 C
ANISOU 1496 CD ARG A 199 9606 9049 12701 285 -548 6 C
ATOM 1497 NE ARG A 199 5.182 202.187 28.594 1.00 96.33 N
ANISOU 1497 NE ARG A 199 11366 10804 14430 297 -533 -18 N
ATOM 1498 CZ ARG A 199 4.372 202.955 29.315 1.00105.48 C
ANISOU 1498 CZ ARG A 199 12418 11941 15720 244 -591 -65 C
ATOM 1499 NH1 ARG A 199 4.375 204.270 29.141 1.00109.28 N
ANISOU 1499 NH1 ARG A 199 12771 12392 16359 177 -669 -93 N
ATOM 1500 NH2 ARG A 199 3.560 202.410 30.211 1.00107.14 N
ANISOU 1500 NH2 ARG A 199 12647 12159 15902 259 -572 -84 N
ATOM 1501 N ILE A 200 7.414 204.598 22.401 1.00 51.15 N
ANISOU 1501 N ILE A 200 5497 5025 8913 179 -684 101 N
ATOM 1502 CA ILE A 200 8.150 205.596 21.625 1.00 48.01 C
ANISOU 1502 CA ILE A 200 5030 4609 8602 139 -735 108 C
ATOM 1503 C ILE A 200 7.243 206.221 20.572 1.00 54.91 C
ANISOU 1503 C ILE A 200 5805 5459 9598 79 -814 107 C
ATOM 1504 O ILE A 200 7.073 207.444 20.515 1.00 61.08 O
ANISOU 1504 O ILE A 200 6459 6215 10532 14 -897 80 O
ATOM 1505 CB ILE A 200 9.398 204.968 20.982 1.00 53.33 C
ANISOU 1505 CB ILE A 200 5814 5306 9144 194 -670 153 C
ATOM 1506 CG1 ILE A 200 10.437 204.617 22.047 1.00 58.68 C
ANISOU 1506 CG1 ILE A 200 6566 6006 9722 245 -607 151 C
ATOM 1507 CG2 ILE A 200 9.992 205.906 19.944 1.00 54.78 C
ANISOU 1507 CG2 ILE A 200 5928 5472 9415 151 -725 167 C
ATOM 1508 CD1 ILE A 200 11.703 204.022 21.476 1.00 51.84 C
ANISOU 1508 CD1 ILE A 200 5804 5165 8726 302 -545 193 C
ATOM 1509 N PHE A 201 6.646 205.383 19.723 1.00 53.71 N
ANISOU 1509 N PHE A 201 5712 5316 9380 102 -790 135 N
ATOM 1510 CA PHE A 201 5.791 205.891 18.656 1.00 52.20 C
ANISOU 1510 CA PHE A 201 5435 5104 9294 51 -863 136 C
ATOM 1511 C PHE A 201 4.552 206.579 19.208 1.00 63.34 C
ANISOU 1511 C PHE A 201 6728 6495 10843 -3 -934 93 C
ATOM 1512 O PHE A 201 4.068 207.551 18.616 1.00 77.89 O
ANISOU 1512 O PHE A 201 8529 8331 12733 -28 -982 85 O
ATOM 1513 CB PHE A 201 5.408 204.751 17.713 1.00 43.71 C
ANISOU 1513 CB PHE A 201 4457 4043 8106 92 -816 174 C
ATOM 1514 CG PHE A 201 6.580 204.151 16.985 1.00 48.16 C
ANISOU 1514 CG PHE A 201 5126 4625 8547 140 -755 217 C
ATOM 1515 CD1 PHE A 201 7.503 204.962 16.347 1.00 52.71 C
ANISOU 1515 CD1 PHE A 201 5657 5191 9178 114 -789 228 C
ATOM 1516 CD2 PHE A 201 6.754 202.777 16.933 1.00 50.22 C
ANISOU 1516 CD2 PHE A 201 5529 4915 8639 211 -666 244 C
ATOM 1517 CE1 PHE A 201 8.580 204.416 15.676 1.00 51.15 C
ANISOU 1517 CE1 PHE A 201 5553 5012 8869 159 -734 267 C
ATOM 1518 CE2 PHE A 201 7.831 202.227 16.265 1.00 41.32 C
ANISOU 1518 CE2 PHE A 201 4495 3807 7399 256 -613 281 C
ATOM 1519 CZ PHE A 201 8.743 203.047 15.635 1.00 42.39 C
ANISOU 1519 CZ PHE A 201 4583 3931 7592 230 -646 293 C
ATOM 1520 N ALA A 202 4.028 206.103 20.340 1.00 65.24 N
ANISOU 1520 N ALA A 202 6995 6744 11048 17 -902 69 N
ATOM 1521 CA ALA A 202 2.899 206.786 20.960 1.00 68.00 C
ANISOU 1521 CA ALA A 202 7278 7086 11475 -12 -945 29 C
ATOM 1522 C ALA A 202 3.318 208.137 21.522 1.00 66.50 C
ANISOU 1522 C ALA A 202 7070 6897 11299 -18 -961 2 C
ATOM 1523 O ALA A 202 2.545 209.101 21.474 1.00 65.65 O
ANISOU 1523 O ALA A 202 6947 6791 11205 -28 -987 -17 O
ATOM 1524 CB ALA A 202 2.285 205.918 22.057 1.00 62.19 C
ANISOU 1524 CB ALA A 202 6556 6354 10718 3 -914 9 C
ATOM 1525 N ALA A 203 4.538 208.226 22.059 1.00 60.46 N
ANISOU 1525 N ALA A 203 6308 6132 10531 -13 -944 0 N
ATOM 1526 CA ALA A 203 5.040 209.507 22.546 1.00 54.49 C
ANISOU 1526 CA ALA A 203 5538 5377 9789 -20 -958 -23 C
ATOM 1527 C ALA A 203 5.342 210.456 21.393 1.00 63.54 C
ANISOU 1527 C ALA A 203 6676 6522 10944 -33 -988 -5 C
ATOM 1528 O ALA A 203 5.127 211.667 21.508 1.00 66.78 O
ANISOU 1528 O ALA A 203 7070 6935 11369 -42 -1011 -25 O
ATOM 1529 CB ALA A 203 6.286 209.296 23.406 1.00 47.48 C
ANISOU 1529 CB ALA A 203 4655 4489 8895 -10 -932 -29 C
ATOM 1530 N ALA A 204 5.849 209.926 20.278 1.00 68.62 N
ANISOU 1530 N ALA A 204 7330 7161 11581 -34 -988 33 N
ATOM 1531 CA ALA A 204 6.115 210.769 19.117 1.00 56.71 C
ANISOU 1531 CA ALA A 204 5815 5651 10081 -46 -1018 52 C
ATOM 1532 C ALA A 204 4.824 211.323 18.531 1.00 66.24 C
ANISOU 1532 C ALA A 204 7010 6859 11298 -56 -1047 45 C
ATOM 1533 O ALA A 204 4.752 212.505 18.175 1.00 72.15 O
ANISOU 1533 O ALA A 204 7744 7610 12059 -67 -1074 38 O
ATOM 1534 CB ALA A 204 6.880 209.976 18.061 1.00 51.64 C
ANISOU 1534 CB ALA A 204 5188 5005 9429 -44 -1010 95 C
ATOM 1535 N ARG A 205 3.796 210.478 18.423 1.00 71.36 N
ANISOU 1535 N ARG A 205 7665 7507 11941 -52 -1043 48 N
ATOM 1536 CA ARG A 205 2.516 210.915 17.876 1.00 77.96 C
ANISOU 1536 CA ARG A 205 8490 8344 12786 -60 -1070 42 C
ATOM 1537 C ARG A 205 1.850 211.946 18.780 1.00 86.41 C
ANISOU 1537 C ARG A 205 9542 9421 13871 -64 -1080 4 C
ATOM 1538 O ARG A 205 1.226 212.896 18.292 1.00 92.34 O
ANISOU 1538 O ARG A 205 10277 10174 14634 -74 -1107 -2 O
ATOM 1539 CB ARG A 205 1.609 209.701 17.671 1.00 83.04 C
ANISOU 1539 CB ARG A 205 9145 8985 13420 -54 -1060 53 C
ATOM 1540 CG ARG A 205 0.157 210.022 17.372 1.00 95.11 C
ANISOU 1540 CG ARG A 205 10663 10515 14960 -60 -1082 42 C
ATOM 1541 CD ARG A 205 -0.682 208.762 17.481 1.00103.35 C
ANISOU 1541 CD ARG A 205 11719 11556 15992 -51 -1067 47 C
ATOM 1542 NE ARG A 205 -0.447 208.081 18.753 1.00111.84 N
ANISOU 1542 NE ARG A 205 12802 12635 17057 -39 -1033 29 N
ATOM 1543 CZ ARG A 205 -0.893 206.865 19.049 1.00113.31 C
ANISOU 1543 CZ ARG A 205 13002 12820 17230 -30 -1011 34 C
ATOM 1544 NH1 ARG A 205 -1.602 206.180 18.163 1.00112.30 N
ANISOU 1544 NH1 ARG A 205 12882 12689 17099 -31 -1019 55 N
ATOM 1545 NH2 ARG A 205 -0.627 206.330 20.234 1.00112.39 N
ANISOU 1545 NH2 ARG A 205 12892 12707 17105 -20 -981 17 N
ATOM 1546 N ARG A 206 1.981 211.782 20.098 1.00 89.04 N
ANISOU 1546 N ARG A 206 9875 9757 14201 -56 -1057 -23 N
ATOM 1547 CA ARG A 206 1.369 212.726 21.027 1.00 89.91 C
ANISOU 1547 CA ARG A 206 9966 9873 14323 -60 -1065 -60 C
ATOM 1548 C ARG A 206 2.047 214.088 20.976 1.00 87.12 C
ANISOU 1548 C ARG A 206 9599 9522 13980 -69 -1083 -68 C
ATOM 1549 O ARG A 206 1.387 215.115 21.172 1.00 97.80 O
ANISOU 1549 O ARG A 206 10933 10880 15345 -77 -1101 -88 O
ATOM 1550 CB ARG A 206 1.416 212.167 22.449 1.00103.24 C
ANISOU 1550 CB ARG A 206 11659 11562 16004 -49 -1037 -85 C
ATOM 1551 CG ARG A 206 0.764 213.064 23.490 1.00119.44 C
ANISOU 1551 CG ARG A 206 13693 13621 18069 -52 -1043 -124 C
ATOM 1552 CD ARG A 206 0.777 212.432 24.874 1.00139.30 C
ANISOU 1552 CD ARG A 206 16213 16138 20577 -41 -1016 -149 C
ATOM 1553 NE ARG A 206 0.136 213.297 25.861 1.00151.63 N
ANISOU 1553 NE ARG A 206 17757 17706 22151 -45 -1023 -186 N
ATOM 1554 CZ ARG A 206 -0.058 212.969 27.135 1.00155.44 C
ANISOU 1554 CZ ARG A 206 18239 18190 22631 -37 -1004 -214 C
ATOM 1555 NH1 ARG A 206 0.337 211.788 27.588 1.00154.91 N
ANISOU 1555 NH1 ARG A 206 18189 18121 22550 -25 -977 -210 N
ATOM 1556 NH2 ARG A 206 -0.652 213.825 27.956 1.00155.24 N
ANISOU 1556 NH2 ARG A 206 18196 18172 22618 -42 -1013 -245 N
ATOM 1557 N GLN A 207 3.353 214.123 20.716 1.00 78.98 N
ANISOU 1557 N GLN A 207 8576 8488 12944 -69 -1077 -51 N
ATOM 1558 CA GLN A 207 4.068 215.393 20.736 1.00 68.68 C
ANISOU 1558 CA GLN A 207 7258 7186 11649 -78 -1092 -59 C
ATOM 1559 C GLN A 207 3.852 216.184 19.451 1.00 73.91 C
ANISOU 1559 C GLN A 207 7913 7850 12321 -90 -1123 -41 C
ATOM 1560 O GLN A 207 3.781 217.418 19.485 1.00 78.55 O
ANISOU 1560 O GLN A 207 8483 8443 12918 -100 -1142 -56 O
ATOM 1561 CB GLN A 207 5.560 215.151 20.970 1.00 53.77 C
ANISOU 1561 CB GLN A 207 5382 5294 9755 -72 -1075 -49 C
ATOM 1562 CG GLN A 207 5.899 214.610 22.350 1.00 60.01 C
ANISOU 1562 CG GLN A 207 6178 6085 10540 -60 -1046 -72 C
ATOM 1563 CD GLN A 207 7.381 214.328 22.512 1.00 75.36 C
ANISOU 1563 CD GLN A 207 8133 8024 12478 -54 -1028 -59 C
ATOM 1564 OE1 GLN A 207 8.213 214.915 21.821 1.00 79.53 O
ANISOU 1564 OE1 GLN A 207 8658 8550 13008 -61 -1040 -42 O
ATOM 1565 NE2 GLN A 207 7.717 213.418 23.422 1.00 77.08 N
ANISOU 1565 NE2 GLN A 207 8361 8240 12686 -41 -999 -67 N
ATOM 1566 N LEU A 208 3.746 215.496 18.318 1.00 72.00 N
ANISOU 1566 N LEU A 208 7681 7603 12073 -91 -1129 -10 N
ATOM 1567 CA LEU A 208 3.614 216.149 17.017 1.00 76.75 C
ANISOU 1567 CA LEU A 208 8275 8204 12681 -102 -1158 10 C
ATOM 1568 C LEU A 208 2.340 216.978 16.911 1.00 86.62 C
ANISOU 1568 C LEU A 208 9507 9461 13944 -109 -1181 -7 C
ATOM 1569 O LEU A 208 2.307 217.994 16.217 1.00 92.22 O
ANISOU 1569 O LEU A 208 10203 10173 14662 -120 -1207 -4 O
ATOM 1570 CB LEU A 208 3.649 215.110 15.896 1.00 77.95 C
ANISOU 1570 CB LEU A 208 8444 8350 12825 -100 -1158 46 C
ATOM 1571 CG LEU A 208 5.041 214.705 15.407 1.00 88.41 C
ANISOU 1571 CG LEU A 208 9782 9669 14141 -98 -1148 75 C
ATOM 1572 CD1 LEU A 208 4.961 213.520 14.455 1.00 94.11 C
ANISOU 1572 CD1 LEU A 208 10521 10385 14853 -94 -1144 109 C
ATOM 1573 CD2 LEU A 208 5.719 215.887 14.734 1.00 87.24 C
ANISOU 1573 CD2 LEU A 208 9624 9523 14002 -109 -1171 82 C
ATOM 1574 N ALA A1001 0.324 215.426 18.667 1.00107.19 N
ANISOU 1574 N ALA A1001 12117 12068 16544 -92 -1148 -45 N
ATOM 1575 CA ALA A1001 -0.654 216.411 18.230 1.00107.46 C
ANISOU 1575 CA ALA A1001 12131 12107 16592 -101 -1176 -54 C
ATOM 1576 C ALA A1001 -0.440 217.745 18.940 1.00110.79 C
ANISOU 1576 C ALA A1001 12533 12537 17023 -108 -1184 -80 C
ATOM 1577 O ALA A1001 -1.049 218.748 18.576 1.00122.74 O
ANISOU 1577 O ALA A1001 14030 14058 18549 -116 -1207 -87 O
ATOM 1578 CB ALA A1001 -2.054 215.900 18.475 1.00111.17 C
ANISOU 1578 CB ALA A1001 12598 12578 17065 -98 -1175 -65 C
ATOM 1579 N ASP A1002 0.450 217.752 19.938 1.00109.01 N
ANISOU 1579 N ASP A1002 12313 12313 16793 -103 -1164 -95 N
ATOM 1580 CA ASP A1002 0.591 218.923 20.802 1.00109.76 C
ANISOU 1580 CA ASP A1002 12391 12416 16897 -108 -1169 -124 C
ATOM 1581 C ASP A1002 1.132 220.129 20.041 1.00110.76 C
ANISOU 1581 C ASP A1002 12860 12155 17071 22 -1107 -87 C
ATOM 1582 O ASP A1002 0.649 221.252 20.228 1.00119.34 O
ANISOU 1582 O ASP A1002 13500 13637 18207 24 -1246 -97 O
ATOM 1583 CB ASP A1002 1.490 218.596 21.996 1.00113.38 C
ANISOU 1583 CB ASP A1002 12859 12873 17349 -101 -1143 -140 C
ATOM 1584 CG ASP A1002 0.798 217.723 23.029 1.00119.00 C
ANISOU 1584 CG ASP A1002 13575 13584 18056 -90 -1121 -159 C
ATOM 1585 OD1 ASP A1002 -0.445 217.788 23.130 1.00121.62 O
ANISOU 1585 OD1 ASP A1002 13896 13919 18393 -92 -1129 -171 O
ATOM 1586 OD2 ASP A1002 1.495 216.970 23.741 1.00121.93 O
ANISOU 1586 OD2 ASP A1002 13960 13951 18418 -81 -1097 -163 O
ATOM 1587 N LEU A1003 2.145 219.925 19.196 1.00104.67 N
ANISOU 1587 N LEU A1003 11748 11770 16253 -121 -1194 -87 N
ATOM 1588 CA LEU A1003 2.660 221.027 18.387 1.00101.29 C
ANISOU 1588 CA LEU A1003 11661 10939 15887 11 -1136 -45 C
ATOM 1589 C LEU A1003 1.580 221.576 17.465 1.00108.25 C
ANISOU 1589 C LEU A1003 12526 11780 16826 9 -1176 -37 C
ATOM 1590 O LEU A1003 1.397 222.795 17.357 1.00111.32 O
ANISOU 1590 O LEU A1003 12890 12120 17289 12 -1214 -46 O
ATOM 1591 CB LEU A1003 3.874 220.567 17.579 1.00 97.85 C
ANISOU 1591 CB LEU A1003 10890 10901 15388 -132 -1214 -46 C
ATOM 1592 CG LEU A1003 5.206 220.466 18.321 1.00100.64 C
ANISOU 1592 CG LEU A1003 11253 11251 15735 -127 -1193 -50 C
ATOM 1593 CD1 LEU A1003 6.276 219.903 17.402 1.00102.67 C
ANISOU 1593 CD1 LEU A1003 11526 11500 15985 -126 -1190 -15 C
ATOM 1594 CD2 LEU A1003 5.624 221.826 18.861 1.00 97.40 C
ANISOU 1594 CD2 LEU A1003 11176 10464 15370 10 -1119 -38 C
ATOM 1595 N GLU A1004 0.845 220.685 16.796 1.00113.69 N
ANISOU 1595 N GLU A1004 12814 12928 17454 5 -1274 -19 N
ATOM 1596 CA GLU A1004 -0.218 221.128 15.902 1.00115.80 C
ANISOU 1596 CA GLU A1004 13060 13167 17770 3 -1315 -11 C
ATOM 1597 C GLU A1004 -1.375 221.753 16.673 1.00112.57 C
ANISOU 1597 C GLU A1004 12618 12730 17424 10 -1337 -40 C
ATOM 1598 O GLU A1004 -2.037 222.662 16.161 1.00119.44 O
ANISOU 1598 O GLU A1004 13456 13564 18360 11 -1381 -41 O
ATOM 1599 CB GLU A1004 -0.708 219.954 15.052 1.00125.15 C
ANISOU 1599 CB GLU A1004 14274 14377 18900 -3 -1297 11 C
ATOM 1600 CG GLU A1004 -1.741 220.325 13.996 1.00135.15 C
ANISOU 1600 CG GLU A1004 15522 15617 20211 -6 -1338 23 C
ATOM 1601 CD GLU A1004 -1.181 221.224 12.907 1.00143.40 C
ANISOU 1601 CD GLU A1004 16553 16640 21293 -11 -1375 42 C
ATOM 1602 OE1 GLU A1004 0.052 221.228 12.706 1.00144.02 O
ANISOU 1602 OE1 GLU A1004 16646 16733 21343 -15 -1363 56 O
ATOM 1603 OE2 GLU A1004 -1.979 221.927 12.251 1.00143.91 O
ANISOU 1603 OE2 GLU A1004 17026 16206 21447 -13 -1300 49 O
ATOM 1604 N ASP A1005 -1.623 221.297 17.903 1.00107.77 N
ANISOU 1604 N ASP A1005 12441 11682 16825 18 -1199 -70 N
ATOM 1605 CA ASP A1005 -2.739 221.836 18.674 1.00109.67 C
ANISOU 1605 CA ASP A1005 12659 11888 17123 26 -1216 -102 C
ATOM 1606 C ASP A1005 -2.438 223.239 19.186 1.00111.16 C
ANISOU 1606 C ASP A1005 12820 12032 17385 32 -1246 -124 C
ATOM 1607 O ASP A1005 -3.325 224.100 19.207 1.00110.49 O
ANISOU 1607 O ASP A1005 12256 12385 17341 33 -1396 -128 O
ATOM 1608 CB ASP A1005 -3.082 220.900 19.831 1.00115.74 C
ANISOU 1608 CB ASP A1005 13438 12691 17846 31 -1179 -123 C
ATOM 1609 CG ASP A1005 -3.875 219.689 19.380 1.00127.27 C
ANISOU 1609 CG ASP A1005 14497 14630 19231 25 -1265 -98 C
ATOM 1610 OD1 ASP A1005 -4.672 219.829 18.429 1.00131.37 O
ANISOU 1610 OD1 ASP A1005 15007 15132 19776 22 -1293 -85 O
ATOM 1611 OD2 ASP A1005 -3.700 218.601 19.969 1.00128.04 O
ANISOU 1611 OD2 ASP A1005 14625 14762 19262 25 -1222 -100 O
ATOM 1612 N ASN A1006 -1.197 223.488 19.612 1.00109.37 N
ANISOU 1612 N ASN A1006 12155 12287 17114 29 -1346 -116 N
ATOM 1613 CA ASN A1006 -0.814 224.842 19.997 1.00104.60 C
ANISOU 1613 CA ASN A1006 11516 11650 16576 34 -1377 -133 C
ATOM 1614 C ASN A1006 -0.763 225.770 18.791 1.00106.01 C
ANISOU 1614 C ASN A1006 11675 11798 16805 30 -1423 -114 C
ATOM 1615 O ASN A1006 -0.991 226.978 18.929 1.00 94.95 O
ANISOU 1615 O ASN A1006 10238 10361 15478 34 -1461 -129 O
ATOM 1616 CB ASN A1006 0.535 224.827 20.715 1.00105.64 C
ANISOU 1616 CB ASN A1006 11662 11800 16676 35 -1351 -139 C
ATOM 1617 CG ASN A1006 0.403 224.538 22.196 1.00110.81 C
ANISOU 1617 CG ASN A1006 12317 12467 17318 42 -1323 -171 C
ATOM 1618 OD1 ASN A1006 -0.592 224.902 22.824 1.00113.78 O
ANISOU 1618 OD1 ASN A1006 12669 12824 17740 48 -1337 -196 O
ATOM 1619 ND2 ASN A1006 1.409 223.884 22.765 1.00113.86 N
ANISOU 1619 ND2 ASN A1006 12732 12885 17644 42 -1283 -170 N
ATOM 1620 N TRP A1007 -0.468 225.228 17.607 1.00109.11 N
ANISOU 1620 N TRP A1007 12091 12206 17160 21 -1420 -81 N
ATOM 1621 CA TRP A1007 -0.469 226.043 16.397 1.00107.53 C
ANISOU 1621 CA TRP A1007 12334 11487 17037 18 -1341 -67 C
ATOM 1622 C TRP A1007 -1.886 226.440 16.003 1.00116.89 C
ANISOU 1622 C TRP A1007 13033 13135 18245 18 -1499 -67 C
ATOM 1623 O TRP A1007 -2.135 227.595 15.638 1.00126.52 O
ANISOU 1623 O TRP A1007 14220 14318 19535 19 -1544 -70 O
ATOM 1624 CB TRP A1007 0.217 225.289 15.258 1.00101.64 C
ANISOU 1624 CB TRP A1007 11613 10774 16231 7 -1328 -28 C
ATOM 1625 CG TRP A1007 0.155 226.001 13.945 1.00108.61 C
ANISOU 1625 CG TRP A1007 12029 12116 17123 1 -1492 -3 C
ATOM 1626 CD1 TRP A1007 -0.639 225.689 12.881 1.00116.57 C
ANISOU 1626 CD1 TRP A1007 13499 12627 18165 -5 -1383 17 C
ATOM 1627 CD2 TRP A1007 0.913 227.152 13.556 1.00115.95 C
ANISOU 1627 CD2 TRP A1007 12938 13021 18098 -1 -1525 3 C
ATOM 1628 NE1 TRP A1007 -0.420 226.572 11.851 1.00121.84 N
ANISOU 1628 NE1 TRP A1007 13691 13762 18841 -9 -1550 33 N
ATOM 1629 CE2 TRP A1007 0.529 227.480 12.241 1.00118.54 C
ANISOU 1629 CE2 TRP A1007 13258 13330 18452 -7 -1561 26 C
ATOM 1630 CE3 TRP A1007 1.881 227.936 14.192 1.00116.73 C
ANISOU 1630 CE3 TRP A1007 13024 13110 18217 2 -1528 -9 C
ATOM 1631 CZ2 TRP A1007 1.077 228.557 11.551 1.00117.27 C
ANISOU 1631 CZ2 TRP A1007 13077 13142 18336 -11 -1599 38 C
ATOM 1632 CZ3 TRP A1007 2.424 229.004 13.504 1.00110.83 C
ANISOU 1632 CZ3 TRP A1007 12732 11827 17552 -1 -1435 3 C
ATOM 1633 CH2 TRP A1007 2.021 229.305 12.198 1.00116.24 C
ANISOU 1633 CH2 TRP A1007 13414 12489 18263 -8 -1468 29 C
ATOM 1634 N GLU A1008 -2.826 225.495 16.068 1.00123.08 N
ANISOU 1634 N GLU A1008 13831 13935 18999 18 -1480 -68 N
ATOM 1635 CA GLU A1008 -4.219 225.825 15.787 1.00131.06 C
ANISOU 1635 CA GLU A1008 14818 14919 20061 20 -1511 -75 C
ATOM 1636 C GLU A1008 -4.785 226.759 16.849 1.00128.37 C
ANISOU 1636 C GLU A1008 14440 14549 19787 29 -1531 -110 C
ATOM 1637 O GLU A1008 -5.550 227.676 16.531 1.00137.41 O
ANISOU 1637 O GLU A1008 16042 15133 21036 34 -1442 -127 O
ATOM 1638 CB GLU A1008 -5.055 224.549 15.693 1.00144.97 C
ANISOU 1638 CB GLU A1008 17067 16209 21803 20 -1360 -75 C
ATOM 1639 CG GLU A1008 -4.639 223.613 14.570 1.00152.35 C
ANISOU 1639 CG GLU A1008 17574 17669 22642 9 -1467 -34 C
ATOM 1640 CD GLU A1008 -5.370 222.284 14.621 1.00158.81 C
ANISOU 1640 CD GLU A1008 18420 18516 23403 8 -1434 -31 C
ATOM 1641 OE1 GLU A1008 -6.420 222.208 15.294 1.00160.45 O
ANISOU 1641 OE1 GLU A1008 18615 18717 23633 14 -1434 -52 O
ATOM 1642 OE2 GLU A1008 -4.892 221.316 13.994 1.00160.57 O
ANISOU 1642 OE2 GLU A1008 18678 18771 23560 2 -1408 -7 O
ATOM 1643 N THR A1009 -4.421 226.540 18.115 1.00125.08 N
ANISOU 1643 N THR A1009 14028 14147 19351 35 -1500 -133 N
ATOM 1644 CA THR A1009 -4.852 227.442 19.179 1.00122.40 C
ANISOU 1644 CA THR A1009 13653 13780 19073 44 -1517 -169 C
ATOM 1645 C THR A1009 -4.344 228.858 18.935 1.00130.97 C
ANISOU 1645 C THR A1009 14707 14831 20224 45 -1559 -172 C
ATOM 1646 O THR A1009 -5.035 229.838 19.239 1.00138.87 O
ANISOU 1646 O THR A1009 15671 15797 21297 51 -1593 -193 O
ATOM 1647 CB THR A1009 -4.369 226.920 20.535 1.00118.53 C
ANISOU 1647 CB THR A1009 13176 13315 18543 49 -1475 -191 C
ATOM 1648 OG1 THR A1009 -4.886 225.601 20.753 1.00122.23 O
ANISOU 1648 OG1 THR A1009 13675 13817 18951 48 -1437 -188 O
ATOM 1649 CG2 THR A1009 -4.833 227.831 21.663 1.00116.67 C
ANISOU 1649 CG2 THR A1009 13393 12535 18402 64 -1367 -250 C
ATOM 1650 N LEU A1010 -3.140 228.983 18.373 1.00123.67 N
ANISOU 1650 N LEU A1010 13796 13915 19277 40 -1557 -151 N
ATOM 1651 CA LEU A1010 -2.600 230.301 18.058 1.00115.70 C
ANISOU 1651 CA LEU A1010 12760 12873 18328 40 -1597 -150 C
ATOM 1652 C LEU A1010 -3.397 230.978 16.949 1.00117.04 C
ANISOU 1652 C LEU A1010 12907 13011 18553 37 -1645 -137 C
ATOM 1653 O LEU A1010 -3.709 232.171 17.040 1.00127.63 O
ANISOU 1653 O LEU A1010 14212 14315 19967 41 -1685 -152 O
ATOM 1654 CB LEU A1010 -1.129 230.176 17.664 1.00115.46 C
ANISOU 1654 CB LEU A1010 12753 12863 18255 34 -1582 -129 C
ATOM 1655 CG LEU A1010 -0.450 231.412 17.073 1.00116.49 C
ANISOU 1655 CG LEU A1010 12861 12964 18436 32 -1622 -120 C
ATOM 1656 CD1 LEU A1010 -0.475 232.566 18.058 1.00120.88 C
ANISOU 1656 CD1 LEU A1010 13891 12943 19094 45 -1507 -166 C
ATOM 1657 CD2 LEU A1010 0.977 231.088 16.662 1.00116.26 C
ANISOU 1657 CD2 LEU A1010 12860 12959 18356 26 -1601 -96 C
ATOM 1658 N ASN A1011 -3.741 230.232 15.897 1.00115.48 N
ANISOU 1658 N ASN A1011 13233 12286 18358 33 -1505 -120 N
ATOM 1659 CA ASN A1011 -4.435 230.826 14.759 1.00117.28 C
ANISOU 1659 CA ASN A1011 12939 13025 18596 26 -1687 -94 C
ATOM 1660 C ASN A1011 -5.916 231.048 15.046 1.00118.83 C
ANISOU 1660 C ASN A1011 13110 13199 18841 31 -1707 -114 C
ATOM 1661 O ASN A1011 -6.494 232.039 14.587 1.00126.34 O
ANISOU 1661 O ASN A1011 14031 14114 19860 32 -1753 -117 O
ATOM 1662 CB ASN A1011 -4.261 229.948 13.520 1.00110.43 C
ANISOU 1662 CB ASN A1011 12104 12180 17675 16 -1677 -58 C
ATOM 1663 CG ASN A1011 -2.862 230.028 12.942 1.00111.70 C
ANISOU 1663 CG ASN A1011 12781 11815 17845 11 -1533 -38 C
ATOM 1664 OD1 ASN A1011 -2.225 231.080 12.977 1.00114.03 O
ANISOU 1664 OD1 ASN A1011 12556 12626 18144 11 -1697 -38 O
ATOM 1665 ND2 ASN A1011 -2.376 228.913 12.409 1.00114.96 N
ANISOU 1665 ND2 ASN A1011 12733 12803 18146 3 -1640 -11 N
ATOM 1666 N ASP A1012 -6.545 230.141 15.796 1.00116.73 N
ANISOU 1666 N ASP A1012 12857 12954 18541 35 -1674 -129 N
ATOM 1667 CA ASP A1012 -7.978 230.260 16.051 1.00121.21 C
ANISOU 1667 CA ASP A1012 13402 13502 19150 40 -1690 -147 C
ATOM 1668 C ASP A1012 -8.285 231.464 16.933 1.00124.37 C
ANISOU 1668 C ASP A1012 14289 13302 19664 53 -1574 -196 C
ATOM 1669 O ASP A1012 -9.220 232.225 16.658 1.00133.66 O
ANISOU 1669 O ASP A1012 14907 15010 20866 51 -1756 -188 O
ATOM 1670 CB ASP A1012 -8.508 228.976 16.689 1.00129.43 C
ANISOU 1670 CB ASP A1012 14468 14575 20134 42 -1646 -154 C
ATOM 1671 CG ASP A1012 -8.482 227.801 15.734 1.00138.68 C
ANISOU 1671 CG ASP A1012 15677 15777 21238 33 -1624 -122 C
ATOM 1672 OD1 ASP A1012 -8.629 228.023 14.514 1.00139.49 O
ANISOU 1672 OD1 ASP A1012 15777 15867 21354 27 -1653 -99 O
ATOM 1673 OD2 ASP A1012 -8.312 226.655 16.203 1.00143.52 O
ANISOU 1673 OD2 ASP A1012 16812 15900 21819 36 -1447 -133 O
ATOM 1674 N ASN A1013 -7.510 231.651 18.004 1.00123.98 N
ANISOU 1674 N ASN A1013 13711 13827 19569 54 -1697 -200 N
ATOM 1675 CA ASN A1013 -7.738 232.781 18.896 1.00127.07 C
ANISOU 1675 CA ASN A1013 14601 13614 20068 68 -1578 -255 C
ATOM 1676 C ASN A1013 -7.435 234.119 18.231 1.00131.48 C
ANISOU 1676 C ASN A1013 14594 14708 20653 62 -1771 -228 C
ATOM 1677 O ASN A1013 -7.932 235.151 18.694 1.00127.52 O
ANISOU 1677 O ASN A1013 14611 13579 20261 75 -1651 -275 O
ATOM 1678 CB ASN A1013 -6.903 232.624 20.167 1.00119.74 C
ANISOU 1678 CB ASN A1013 13143 13277 19074 68 -1687 -255 C
ATOM 1679 CG ASN A1013 -7.472 231.586 21.119 1.00111.60 C
ANISOU 1679 CG ASN A1013 12655 11712 18036 78 -1509 -297 C
ATOM 1680 OD1 ASN A1013 -8.688 231.422 21.223 1.00118.06 O
ANISOU 1680 OD1 ASN A1013 13464 12519 18876 81 -1515 -309 O
ATOM 1681 ND2 ASN A1013 -6.592 230.884 21.824 1.00111.91 N
ANISOU 1681 ND2 ASN A1013 12194 12345 17981 71 -1604 -275 N
ATOM 1682 N LEU A1014 -6.632 234.129 17.164 1.00132.68 N
ANISOU 1682 N LEU A1014 14762 14866 20785 54 -1779 -196 N
ATOM 1683 CA LEU A1014 -6.431 235.364 16.412 1.00134.26 C
ANISOU 1683 CA LEU A1014 15488 14438 21088 56 -1676 -204 C
ATOM 1684 C LEU A1014 -7.694 235.756 15.657 1.00140.58 C
ANISOU 1684 C LEU A1014 16273 15200 21940 56 -1712 -200 C
ATOM 1685 O LEU A1014 -8.029 236.943 15.572 1.00146.65 O
ANISOU 1685 O LEU A1014 16448 16533 22738 55 -1911 -195 O
ATOM 1686 CB LEU A1014 -5.255 235.213 15.448 1.00135.39 C
ANISOU 1686 CB LEU A1014 15103 15188 21152 43 -1826 -153 C
ATOM 1687 CG LEU A1014 -3.859 235.354 16.055 1.00138.20 C
ANISOU 1687 CG LEU A1014 16012 14974 21523 48 -1654 -172 C
ATOM 1688 CD1 LEU A1014 -2.793 234.956 15.047 1.00142.01 C
ANISOU 1688 CD1 LEU A1014 15981 16061 21916 34 -1795 -121 C
ATOM 1689 CD2 LEU A1014 -3.633 236.778 16.538 1.00140.10 C
ANISOU 1689 CD2 LEU A1014 15673 15764 21796 50 -1840 -179 C
ATOM 1690 N LYS A1015 -8.406 234.773 15.101 1.00141.43 N
ANISOU 1690 N LYS A1015 16397 15331 22011 51 -1699 -183 N
ATOM 1691 CA LYS A1015 -9.676 235.062 14.443 1.00141.21 C
ANISOU 1691 CA LYS A1015 15795 15874 21985 46 -1888 -165 C
ATOM 1692 C LYS A1015 -10.723 235.525 15.448 1.00141.60 C
ANISOU 1692 C LYS A1015 15812 15901 22087 56 -1898 -202 C
ATOM 1693 O LYS A1015 -11.552 236.387 15.135 1.00145.92 O
ANISOU 1693 O LYS A1015 16329 16414 22701 59 -1941 -209 O
ATOM 1694 CB LYS A1015 -10.170 233.828 13.689 1.00144.02 C
ANISOU 1694 CB LYS A1015 16734 15659 22327 43 -1712 -154 C
ATOM 1695 CG LYS A1015 -9.253 233.363 12.571 1.00146.83 C
ANISOU 1695 CG LYS A1015 16568 16631 22591 30 -1861 -104 C
ATOM 1696 CD LYS A1015 -9.730 232.037 11.995 1.00147.89 C
ANISOU 1696 CD LYS A1015 16734 16795 22662 24 -1834 -84 C
ATOM 1697 CE LYS A1015 -8.854 231.575 10.841 1.00146.68 C
ANISOU 1697 CE LYS A1015 16611 16661 22461 14 -1829 -48 C
ATOM 1698 NZ LYS A1015 -8.960 232.483 9.665 1.00151.43 N
ANISOU 1698 NZ LYS A1015 17193 17231 23111 9 -1879 -30 N
ATOM 1699 N VAL A1016 -10.699 234.964 16.659 1.00139.18 N
ANISOU 1699 N VAL A1016 16077 15010 21794 68 -1705 -245 N
ATOM 1700 CA VAL A1016 -11.665 235.348 17.685 1.00146.61 C
ANISOU 1700 CA VAL A1016 16146 15523 24036 97 -2332 -356 C
ATOM 1701 C VAL A1016 -11.478 236.809 18.077 1.00148.45 C
ANISOU 1701 C VAL A1016 16621 16735 23049 77 -1904 -283 C
ATOM 1702 O VAL A1016 -12.453 237.539 18.293 1.00155.58 O
ANISOU 1702 O VAL A1016 17491 17608 24016 83 -1935 -303 O
ATOM 1703 CB VAL A1016 -11.542 234.414 18.904 1.00131.05 C
ANISOU 1703 CB VAL A1016 14475 14601 20717 75 -1815 -280 C
ATOM 1704 CG1 VAL A1016 -12.455 234.876 20.030 1.00133.12 C
ANISOU 1704 CG1 VAL A1016 15275 14237 21069 93 -1669 -348 C
ATOM 1705 CG2 VAL A1016 -11.862 232.981 18.507 1.00129.63 C
ANISOU 1705 CG2 VAL A1016 14332 14456 20466 70 -1780 -259 C
ATOM 1706 N ILE A1017 -10.225 237.258 18.167 1.00149.74 N
ANISOU 1706 N ILE A1017 16788 16901 23206 76 -1903 -279 N
ATOM 1707 CA ILE A1017 -9.953 238.638 18.558 1.00147.34 C
ANISOU 1707 CA ILE A1017 17037 15931 23014 90 -1776 -326 C
ATOM 1708 C ILE A1017 -10.426 239.607 17.481 1.00154.03 C
ANISOU 1708 C ILE A1017 17868 16730 23925 87 -1826 -312 C
ATOM 1709 O ILE A1017 -10.948 240.687 17.784 1.00160.97 O
ANISOU 1709 O ILE A1017 18720 17563 24876 94 -1859 -336 O
ATOM 1710 CB ILE A1017 -8.453 238.814 18.864 1.00140.24 C
ANISOU 1710 CB ILE A1017 15562 15678 22045 81 -1922 -295 C
ATOM 1711 CG1 ILE A1017 -8.069 238.023 20.114 1.00133.48 C
ANISOU 1711 CG1 ILE A1017 15302 14235 21179 93 -1716 -344 C
ATOM 1712 CG2 ILE A1017 -8.101 240.282 19.040 1.00144.71 C
ANISOU 1712 CG2 ILE A1017 16688 15569 22726 93 -1799 -339 C
ATOM 1713 CD1 ILE A1017 -6.588 238.016 20.399 1.00133.01 C
ANISOU 1713 CD1 ILE A1017 15255 14199 21083 91 -1697 -338 C
ATOM 1714 N GLU A1018 -10.270 239.232 16.208 1.00152.76 N
ANISOU 1714 N GLU A1018 17724 16578 23738 77 -1833 -273 N
ATOM 1715 CA GLU A1018 -10.606 240.144 15.119 1.00160.52 C
ANISOU 1715 CA GLU A1018 18694 17518 24778 73 -1880 -256 C
ATOM 1716 C GLU A1018 -12.103 240.418 15.038 1.00169.33 C
ANISOU 1716 C GLU A1018 19181 19258 25897 71 -2079 -248 C
ATOM 1717 O GLU A1018 -12.506 241.528 14.672 1.00177.38 O
ANISOU 1717 O GLU A1018 20169 20240 26985 73 -2126 -253 O
ATOM 1718 CB GLU A1018 -10.099 239.585 13.791 1.00154.00 C
ANISOU 1718 CB GLU A1018 17295 17358 23859 55 -2050 -193 C
ATOM 1719 CG GLU A1018 -8.587 239.511 13.692 1.00155.81 C
ANISOU 1719 CG GLU A1018 18136 16968 24095 55 -1863 -193 C
ATOM 1720 CD GLU A1018 -8.118 238.891 12.393 1.00160.45 C
ANISOU 1720 CD GLU A1018 18164 18213 24588 40 -2029 -137 C
ATOM 1721 OE1 GLU A1018 -8.975 238.472 11.586 1.00162.66 O
ANISOU 1721 OE1 GLU A1018 18448 18491 24864 35 -2039 -122 O
ATOM 1722 OE2 GLU A1018 -6.890 238.824 12.177 1.00152.63 O
ANISOU 1722 OE2 GLU A1018 17770 16609 23612 38 -1848 -132 O
ATOM 1723 N LYS A1019 -12.939 239.433 15.369 1.00163.66 N
ANISOU 1723 N LYS A1019 19815 15974 26394 1186 2193 1133 N
ATOM 1724 CA LYS A1019 -14.386 239.589 15.281 1.00135.59 C
ANISOU 1724 CA LYS A1019 16241 12420 22858 1201 2139 1261 C
ATOM 1725 C LYS A1019 -15.049 239.703 16.650 1.00139.12 C
ANISOU 1725 C LYS A1019 16527 12930 23400 1288 2185 1361 C
ATOM 1726 O LYS A1019 -16.259 239.489 16.768 1.00137.59 O
ANISOU 1726 O LYS A1019 16289 12753 23235 1305 2130 1497 O
ATOM 1727 CB LYS A1019 -14.999 238.436 14.486 1.00129.40 C
ANISOU 1727 CB LYS A1019 15506 11614 22046 1150 2015 1367 C
ATOM 1728 CG LYS A1019 -14.664 237.055 15.015 1.00129.31 C
ANISOU 1728 CG LYS A1019 15414 11634 22083 1159 1984 1437 C
ATOM 1729 CD LYS A1019 -15.328 235.980 14.171 1.00134.73 C
ANISOU 1729 CD LYS A1019 16157 12303 22731 1105 1859 1536 C
ATOM 1730 CE LYS A1019 -14.984 236.147 12.698 1.00137.44 C
ANISOU 1730 CE LYS A1019 16676 12584 22959 1024 1807 1443 C
ATOM 1731 NZ LYS A1019 -15.708 235.170 11.839 1.00140.30 N
ANISOU 1731 NZ LYS A1019 17102 12933 23273 973 1684 1536 N
ATOM 1732 N ALA A1020 -14.285 240.038 17.685 1.00151.55 N
ANISOU 1732 N ALA A1020 18017 14550 25017 1343 2282 1295 N
ATOM 1733 CA ALA A1020 -14.873 240.314 18.985 1.00161.83 C
ANISOU 1733 CA ALA A1020 19174 15923 26393 1430 2331 1375 C
ATOM 1734 C ALA A1020 -15.530 241.693 18.984 1.00180.71 C
ANISOU 1734 C ALA A1020 21581 18311 28769 1454 2375 1350 C
ATOM 1735 O ALA A1020 -15.217 242.560 18.164 1.00177.58 O
ANISOU 1735 O ALA A1020 21299 17865 28310 1411 2396 1237 O
ATOM 1736 CB ALA A1020 -13.815 240.230 20.086 1.00156.32 C
ANISOU 1736 CB ALA A1020 18384 15282 25728 1482 2416 1303 C
ATOM 1737 N ASP A1021 -16.459 241.889 19.921 1.00195.34 N
ANISOU 1737 N ASP A1021 23318 20223 30678 1524 2387 1459 N
ATOM 1738 CA ASP A1021 -17.188 243.145 20.024 1.00208.95 C
ANISOU 1738 CA ASP A1021 25043 21953 32396 1554 2426 1452 C
ATOM 1739 C ASP A1021 -17.025 243.838 21.370 1.00206.03 C
ANISOU 1739 C ASP A1021 24554 21667 32060 1642 2522 1425 C
ATOM 1740 O ASP A1021 -17.591 244.921 21.560 1.00219.30 O
ANISOU 1740 O ASP A1021 26228 23362 33735 1673 2560 1414 O
ATOM 1741 CB ASP A1021 -18.683 242.924 19.745 1.00221.38 C
ANISOU 1741 CB ASP A1021 26605 23524 33987 1550 2341 1611 C
ATOM 1742 CG ASP A1021 -19.395 242.226 20.887 1.00230.92 C
ANISOU 1742 CG ASP A1021 27658 24817 35263 1617 2321 1765 C
ATOM 1743 OD1 ASP A1021 -18.793 241.323 21.505 1.00233.32 O
ANISOU 1743 OD1 ASP A1021 27892 25163 35598 1636 2323 1784 O
ATOM 1744 OD2 ASP A1021 -20.559 242.584 21.168 1.00233.59 O
ANISOU 1744 OD2 ASP A1021 27947 25186 35621 1649 2300 1868 O
ATOM 1745 N ASN A1022 -16.281 243.255 22.306 1.00188.28 N
ANISOU 1745 N ASN A1022 22216 19483 29840 1683 2557 1412 N
ATOM 1746 CA ASN A1022 -16.029 243.900 23.587 1.00168.08 C
ANISOU 1746 CA ASN A1022 19551 17019 27291 1766 2642 1371 C
ATOM 1747 C ASN A1022 -14.645 243.503 24.077 1.00158.79 C
ANISOU 1747 C ASN A1022 18354 15878 26102 1773 2691 1261 C
ATOM 1748 O ASN A1022 -14.027 242.563 23.572 1.00156.91 O
ANISOU 1748 O ASN A1022 18158 15595 25864 1724 2653 1251 O
ATOM 1749 CB ASN A1022 -17.099 243.540 24.624 1.00160.49 C
ANISOU 1749 CB ASN A1022 18450 16151 26380 1839 2614 1535 C
ATOM 1750 CG ASN A1022 -17.180 242.052 24.883 1.00153.53 C
ANISOU 1750 CG ASN A1022 17503 15295 25539 1837 2543 1657 C
ATOM 1751 OD1 ASN A1022 -16.377 241.495 25.630 1.00150.54 O
ANISOU 1751 OD1 ASN A1022 17057 14975 25166 1867 2569 1628 O
ATOM 1752 ND2 ASN A1022 -18.157 241.398 24.267 1.00152.67 N
ANISOU 1752 ND2 ASN A1022 17413 15146 25450 1801 2450 1792 N
ATOM 1753 N ALA A1023 -14.166 244.236 25.084 1.00153.74 N
ANISOU 1753 N ALA A1023 17648 15325 25441 1835 2773 1176 N
ATOM 1754 CA ALA A1023 -12.820 244.012 25.596 1.00153.75 C
ANISOU 1754 CA ALA A1023 17632 15372 25414 1842 2823 1054 C
ATOM 1755 C ALA A1023 -12.692 242.699 26.357 1.00155.52 C
ANISOU 1755 C ALA A1023 17752 15659 25679 1875 2786 1149 C
ATOM 1756 O ALA A1023 -11.578 242.180 26.484 1.00160.72 O
ANISOU 1756 O ALA A1023 18417 16327 26322 1860 2804 1066 O
ATOM 1757 CB ALA A1023 -12.402 245.177 26.492 1.00151.83 C
ANISOU 1757 CB ALA A1023 17348 15222 25118 1897 2910 938 C
ATOM 1758 N ALA A1024 -13.798 242.150 26.866 1.00148.62 N
ANISOU 1758 N ALA A1024 16783 14833 24851 1917 2731 1321 N
ATOM 1759 CA ALA A1024 -13.716 240.898 27.612 1.00149.43 C
ANISOU 1759 CA ALA A1024 16785 15005 24987 1948 2690 1418 C
ATOM 1760 C ALA A1024 -13.452 239.716 26.686 1.00145.04 C
ANISOU 1760 C ALA A1024 16293 14356 24461 1876 2622 1459 C
ATOM 1761 O ALA A1024 -12.725 238.785 27.053 1.00142.58 O
ANISOU 1761 O ALA A1024 15943 14074 24159 1878 2613 1454 O
ATOM 1762 CB ALA A1024 -14.997 240.678 28.417 1.00152.60 C
ANISOU 1762 CB ALA A1024 17069 15495 25418 2009 2647 1590 C
ATOM 1763 N GLN A1025 -14.033 239.733 25.483 1.00139.08 N
ANISOU 1763 N GLN A1025 15639 13495 23710 1810 2569 1497 N
ATOM 1764 CA GLN A1025 -13.794 238.652 24.532 1.00129.03 C
ANISOU 1764 CA GLN A1025 14438 12141 22445 1735 2496 1527 C
ATOM 1765 C GLN A1025 -12.363 238.681 24.011 1.00121.54 C
ANISOU 1765 C GLN A1025 13580 11142 21457 1686 2538 1358 C
ATOM 1766 O GLN A1025 -11.753 237.627 23.795 1.00118.22 O
ANISOU 1766 O GLN A1025 13171 10703 21046 1653 2502 1362 O
ATOM 1767 CB GLN A1025 -14.788 238.740 23.375 1.00130.01 C
ANISOU 1767 CB GLN A1025 14654 12183 22560 1676 2423 1598 C
ATOM 1768 CG GLN A1025 -16.231 238.503 23.782 1.00133.91 C
ANISOU 1768 CG GLN A1025 15064 12725 23091 1712 2364 1779 C
ATOM 1769 CD GLN A1025 -17.198 238.690 22.632 1.00139.00 C
ANISOU 1769 CD GLN A1025 15806 13295 23713 1653 2294 1833 C
ATOM 1770 OE1 GLN A1025 -16.828 239.186 21.568 1.00140.72 O
ANISOU 1770 OE1 GLN A1025 16155 13431 23882 1592 2296 1729 O
ATOM 1771 NE2 GLN A1025 -18.448 238.293 22.840 1.00140.37 N
ANISOU 1771 NE2 GLN A1025 15916 13505 23912 1669 2226 1996 N
ATOM 1772 N VAL A1026 -11.813 239.878 23.797 1.00116.83 N
ANISOU 1772 N VAL A1026 13050 10527 20812 1678 2613 1208 N
ATOM 1773 CA VAL A1026 -10.413 239.990 23.401 1.00113.89 C
ANISOU 1773 CA VAL A1026 12757 10123 20392 1634 2657 1039 C
ATOM 1774 C VAL A1026 -9.508 239.489 24.519 1.00115.89 C
ANISOU 1774 C VAL A1026 12914 10464 20657 1684 2700 999 C
ATOM 1775 O VAL A1026 -8.501 238.814 24.269 1.00122.36 O
ANISOU 1775 O VAL A1026 13767 11260 21463 1646 2696 932 O
ATOM 1776 CB VAL A1026 -10.084 241.443 23.008 1.00106.20 C
ANISOU 1776 CB VAL A1026 11868 9126 19355 1617 2725 893 C
ATOM 1777 CG1 VAL A1026 -8.613 241.582 22.648 1.00103.20 C
ANISOU 1777 CG1 VAL A1026 11567 8728 18916 1569 2770 719 C
ATOM 1778 CG2 VAL A1026 -10.965 241.891 21.851 1.00103.52 C
ANISOU 1778 CG2 VAL A1026 11632 8704 18997 1564 2676 933 C
ATOM 1779 N LYS A1027 -9.859 239.798 25.769 1.00117.37 N
ANISOU 1779 N LYS A1027 12979 10758 20857 1769 2736 1038 N
ATOM 1780 CA LYS A1027 -9.050 239.354 26.899 1.00122.97 C
ANISOU 1780 CA LYS A1027 13593 11570 21560 1820 2770 1000 C
ATOM 1781 C LYS A1027 -9.078 237.837 27.042 1.00127.84 C
ANISOU 1781 C LYS A1027 14154 12191 22228 1816 2701 1117 C
ATOM 1782 O LYS A1027 -8.055 237.220 27.363 1.00122.20 O
ANISOU 1782 O LYS A1027 13422 11504 21504 1814 2714 1053 O
ATOM 1783 CB LYS A1027 -9.536 240.023 28.185 1.00116.15 C
ANISOU 1783 CB LYS A1027 12614 10838 20679 1911 2809 1024 C
ATOM 1784 CG LYS A1027 -8.758 239.619 29.426 1.00116.47 C
ANISOU 1784 CG LYS A1027 12555 11008 20691 1967 2836 983 C
ATOM 1785 CD LYS A1027 -9.375 240.208 30.683 1.00119.61 C
ANISOU 1785 CD LYS A1027 12841 11551 21057 2053 2856 1022 C
ATOM 1786 CE LYS A1027 -8.614 239.771 31.924 1.00121.78 C
ANISOU 1786 CE LYS A1027 13020 11969 21283 2105 2871 981 C
ATOM 1787 NZ LYS A1027 -9.217 240.326 33.167 1.00123.21 N
ANISOU 1787 NZ LYS A1027 13094 12306 21413 2186 2881 1017 N
ATOM 1788 N ASP A1028 -10.239 237.218 26.807 1.00132.83 N
ANISOU 1788 N ASP A1028 14758 12800 22910 1813 2624 1288 N
ATOM 1789 CA ASP A1028 -10.347 235.767 26.932 1.00137.21 C
ANISOU 1789 CA ASP A1028 15260 13365 23510 1807 2550 1409 C
ATOM 1790 C ASP A1028 -9.432 235.054 25.945 1.00127.11 C
ANISOU 1790 C ASP A1028 14081 11991 22223 1726 2525 1340 C
ATOM 1791 O ASP A1028 -8.774 234.067 26.297 1.00127.37 O
ANISOU 1791 O ASP A1028 14073 12050 22272 1728 2509 1346 O
ATOM 1792 CB ASP A1028 -11.796 235.323 26.729 1.00147.25 C
ANISOU 1792 CB ASP A1028 16499 14628 24821 1806 2466 1599 C
ATOM 1793 CG ASP A1028 -12.588 235.296 28.023 1.00158.27 C
ANISOU 1793 CG ASP A1028 17750 16154 26232 1891 2464 1715 C
ATOM 1794 OD1 ASP A1028 -12.504 234.284 28.751 1.00161.81 O
ANISOU 1794 OD1 ASP A1028 18107 16676 26699 1920 2430 1795 O
ATOM 1795 OD2 ASP A1028 -13.301 236.280 28.310 1.00160.33 O
ANISOU 1795 OD2 ASP A1028 17990 16449 26480 1929 2492 1727 O
ATOM 1796 N ALA A1029 -9.378 235.537 24.702 1.00117.19 N
ANISOU 1796 N ALA A1029 12961 10632 20936 1654 2516 1273 N
ATOM 1797 CA ALA A1029 -8.536 234.894 23.699 1.00111.82 C
ANISOU 1797 CA ALA A1029 12385 9870 20231 1574 2484 1204 C
ATOM 1798 C ALA A1029 -7.059 235.185 23.929 1.00111.93 C
ANISOU 1798 C ALA A1029 12423 9900 20206 1569 2561 1026 C
ATOM 1799 O ALA A1029 -6.211 234.334 23.639 1.00115.10 O
ANISOU 1799 O ALA A1029 12854 10277 20603 1530 2540 988 O
ATOM 1800 CB ALA A1029 -8.955 235.338 22.299 1.00111.74 C
ANISOU 1800 CB ALA A1029 12515 9763 20177 1498 2442 1185 C
ATOM 1801 N LEU A1030 -6.729 236.369 24.447 1.00103.04 N
ANISOU 1801 N LEU A1030 11287 8819 19046 1606 2646 916 N
ATOM 1802 CA LEU A1030 -5.327 236.701 24.684 1.00 95.20 C
ANISOU 1802 CA LEU A1030 10319 7851 18002 1599 2717 742 C
ATOM 1803 C LEU A1030 -4.743 235.877 25.824 1.00 99.60 C
ANISOU 1803 C LEU A1030 10763 8500 18582 1652 2728 756 C
ATOM 1804 O LEU A1030 -3.585 235.447 25.756 1.00 99.64 O
ANISOU 1804 O LEU A1030 10795 8501 18562 1623 2743 657 O
ATOM 1805 CB LEU A1030 -5.183 238.194 24.974 1.00 96.95 C
ANISOU 1805 CB LEU A1030 10558 8110 18169 1624 2797 625 C
ATOM 1806 CG LEU A1030 -5.279 239.141 23.778 1.00 98.38 C
ANISOU 1806 CG LEU A1030 10875 8205 18301 1558 2802 550 C
ATOM 1807 CD1 LEU A1030 -5.418 240.575 24.257 1.00 90.72 C
ANISOU 1807 CD1 LEU A1030 9895 7286 17290 1598 2874 473 C
ATOM 1808 CD2 LEU A1030 -4.063 238.992 22.875 1.00 92.32 C
ANISOU 1808 CD2 LEU A1030 10222 7380 17474 1478 2805 416 C
ATOM 1809 N THR A1031 -5.524 235.651 26.884 1.00104.16 N
ANISOU 1809 N THR A1031 11212 9166 19197 1729 2717 876 N
ATOM 1810 CA THR A1031 -5.034 234.850 28.003 1.00103.83 C
ANISOU 1810 CA THR A1031 11059 9226 19164 1782 2719 897 C
ATOM 1811 C THR A1031 -4.772 233.411 27.577 1.00103.60 C
ANISOU 1811 C THR A1031 11037 9146 19181 1741 2651 967 C
ATOM 1812 O THR A1031 -3.801 232.789 28.024 1.00101.53 O
ANISOU 1812 O THR A1031 10745 8924 18909 1746 2664 909 O
ATOM 1813 CB THR A1031 -6.031 234.894 29.161 1.00101.60 C
ANISOU 1813 CB THR A1031 10643 9061 18898 1869 2708 1023 C
ATOM 1814 OG1 THR A1031 -7.326 234.494 28.695 1.00105.88 O
ANISOU 1814 OG1 THR A1031 11179 9554 19498 1858 2636 1194 O
ATOM 1815 CG2 THR A1031 -6.113 236.299 29.746 1.00 92.24 C
ANISOU 1815 CG2 THR A1031 9443 7949 17653 1915 2777 935 C
ATOM 1816 N LYS A1032 -5.627 232.866 26.709 1.00105.27 N
ANISOU 1816 N LYS A1032 11290 9274 19433 1696 2576 1089 N
ATOM 1817 CA LYS A1032 -5.418 231.517 26.197 1.00106.53 C
ANISOU 1817 CA LYS A1032 11468 9384 19626 1648 2503 1154 C
ATOM 1818 C LYS A1032 -4.265 231.449 25.206 1.00105.24 C
ANISOU 1818 C LYS A1032 11429 9136 19421 1569 2514 1011 C
ATOM 1819 O LYS A1032 -3.678 230.376 25.029 1.00116.34 O
ANISOU 1819 O LYS A1032 12839 10524 20840 1538 2476 1019 O
ATOM 1820 CB LYS A1032 -6.706 230.998 25.555 1.00110.41 C
ANISOU 1820 CB LYS A1032 11971 9826 20152 1620 2410 1323 C
ATOM 1821 CG LYS A1032 -7.866 230.862 26.535 1.00108.89 C
ANISOU 1821 CG LYS A1032 11650 9724 19999 1693 2385 1484 C
ATOM 1822 CD LYS A1032 -9.108 230.298 25.866 1.00109.38 C
ANISOU 1822 CD LYS A1032 11730 9744 20087 1657 2287 1647 C
ATOM 1823 CE LYS A1032 -10.225 230.104 26.878 1.00117.05 C
ANISOU 1823 CE LYS A1032 12569 10815 21090 1726 2258 1808 C
ATOM 1824 NZ LYS A1032 -11.450 229.525 26.261 1.00114.00 N
ANISOU 1824 NZ LYS A1032 12196 10397 20721 1688 2159 1967 N
ATOM 1825 N MET A1033 -3.924 232.566 24.563 1.00 98.01 N
ANISOU 1825 N MET A1033 10614 8176 18449 1534 2563 880 N
ATOM 1826 CA MET A1033 -2.744 232.590 23.707 1.00100.58 C
ANISOU 1826 CA MET A1033 11056 8442 18719 1461 2578 732 C
ATOM 1827 C MET A1033 -1.467 232.717 24.526 1.00102.56 C
ANISOU 1827 C MET A1033 11266 8761 18942 1489 2651 598 C
ATOM 1828 O MET A1033 -0.454 232.089 24.200 1.00102.96 O
ANISOU 1828 O MET A1033 11358 8789 18973 1445 2644 525 O
ATOM 1829 CB MET A1033 -2.830 233.741 22.704 1.00105.81 C
ANISOU 1829 CB MET A1033 11843 9042 19317 1410 2597 643 C
ATOM 1830 CG MET A1033 -3.877 233.556 21.629 1.00106.14 C
ANISOU 1830 CG MET A1033 11959 9010 19360 1362 2514 748 C
ATOM 1831 SD MET A1033 -4.059 235.000 20.564 1.00107.60 S
ANISOU 1831 SD MET A1033 12280 9138 19464 1313 2537 647 S
ATOM 1832 CE MET A1033 -2.432 235.076 19.826 1.00102.03 C
ANISOU 1832 CE MET A1033 11690 8406 18670 1241 2564 458 C
ATOM 1833 N ARG A1034 -1.496 233.533 25.583 1.00 99.76 N
ANISOU 1833 N ARG A1034 10834 8497 18574 1559 2717 560 N
ATOM 1834 CA ARG A1034 -0.309 233.705 26.415 1.00102.54 C
ANISOU 1834 CA ARG A1034 11149 8932 18881 1587 2780 428 C
ATOM 1835 C ARG A1034 0.063 232.405 27.116 1.00104.69 C
ANISOU 1835 C ARG A1034 11332 9254 19193 1615 2749 489 C
ATOM 1836 O ARG A1034 1.248 232.076 27.246 1.00102.29 O
ANISOU 1836 O ARG A1034 11041 8968 18855 1596 2771 382 O
ATOM 1837 CB ARG A1034 -0.537 234.819 27.436 1.00 98.95 C
ANISOU 1837 CB ARG A1034 10627 8582 18388 1659 2842 387 C
ATOM 1838 CG ARG A1034 0.738 235.288 28.108 1.00101.83 C
ANISOU 1838 CG ARG A1034 10986 9032 18674 1672 2906 222 C
ATOM 1839 CD ARG A1034 0.463 236.275 29.228 1.00114.99 C
ANISOU 1839 CD ARG A1034 12577 10823 20292 1748 2953 194 C
ATOM 1840 NE ARG A1034 1.689 236.935 29.668 1.00123.89 N
ANISOU 1840 NE ARG A1034 13726 12024 21322 1745 3009 19 N
ATOM 1841 CZ ARG A1034 2.563 236.404 30.517 1.00125.88 C
ANISOU 1841 CZ ARG A1034 13921 12370 21539 1772 3014 -31 C
ATOM 1842 NH1 ARG A1034 2.351 235.198 31.025 1.00123.25 N
ANISOU 1842 NH1 ARG A1034 13502 12069 21261 1805 2971 79 N
ATOM 1843 NH2 ARG A1034 3.653 237.080 30.858 1.00123.13 N
ANISOU 1843 NH2 ARG A1034 13602 12088 21093 1765 3059 -190 N
ATOM 1844 N ALA A1035 -0.929 231.632 27.506 1.00107.68 N
ANISOU 1844 N ALA A1035 11623 9654 19638 1654 2692 661 N
ATOM 1845 CA ALA A1035 -0.642 230.364 28.128 1.00109.62 C
ANISOU 1845 CA ALA A1035 11785 9947 19920 1678 2655 730 C
ATOM 1846 C ALA A1035 -0.102 229.433 27.054 1.00104.04 C
ANISOU 1846 C ALA A1035 11165 9135 19231 1595 2606 720 C
ATOM 1847 O ALA A1035 0.890 228.751 27.260 1.00103.36 O
ANISOU 1847 O ALA A1035 11070 9066 19138 1585 2610 661 O
ATOM 1848 CB ALA A1035 -1.892 229.787 28.759 1.00115.23 C
ANISOU 1848 CB ALA A1035 12384 10711 20686 1734 2598 924 C
ATOM 1849 N ALA A1036 -0.734 229.430 25.887 1.00102.64 N
ANISOU 1849 N ALA A1036 11079 8856 19065 1535 2556 773 N
ATOM 1850 CA ALA A1036 -0.287 228.555 24.809 1.00107.13 C
ANISOU 1850 CA ALA A1036 11738 9336 19630 1453 2498 767 C
ATOM 1851 C ALA A1036 1.097 228.940 24.306 1.00110.69 C
ANISOU 1851 C ALA A1036 12285 9759 20012 1400 2548 577 C
ATOM 1852 O ALA A1036 1.853 228.074 23.851 1.00105.41 O
ANISOU 1852 O ALA A1036 11657 9058 19337 1352 2516 546 O
ATOM 1853 CB ALA A1036 -1.294 228.577 23.659 1.00104.69 C
ANISOU 1853 CB ALA A1036 11513 8943 19320 1399 2428 854 C
ATOM 1854 N ALA A1037 1.420 230.221 24.304 1.00109.11 N
ANISOU 1854 N ALA A1037 12128 9573 19755 1402 2619 452 N
ATOM 1855 CA ALA A1037 2.727 230.636 23.845 1.00 96.22 C
ANISOU 1855 CA ALA A1037 10587 7927 18047 1350 2662 274 C
ATOM 1856 C ALA A1037 3.766 230.157 24.838 1.00 94.82 C
ANISOU 1856 C ALA A1037 10333 7827 17868 1385 2699 208 C
ATOM 1857 O ALA A1037 4.810 229.656 24.464 1.00 94.11 O
ANISOU 1857 O ALA A1037 10292 7717 17748 1338 2695 124 O
ATOM 1858 CB ALA A1037 2.773 232.140 23.707 1.00 99.57 C
ANISOU 1858 CB ALA A1037 11065 8361 18407 1348 2726 165 C
ATOM 1859 N LEU A1038 3.466 230.297 26.117 1.00106.73 N
ANISOU 1859 N LEU A1038 11719 9433 19399 1470 2730 247 N
ATOM 1860 CA LEU A1038 4.382 229.864 27.157 1.00105.26 C
ANISOU 1860 CA LEU A1038 11455 9341 19198 1511 2759 189 C
ATOM 1861 C LEU A1038 4.618 228.370 27.119 1.00108.75 C
ANISOU 1861 C LEU A1038 11863 9760 19695 1497 2700 267 C
ATOM 1862 O LEU A1038 5.728 227.910 27.335 1.00116.34 O
ANISOU 1862 O LEU A1038 12826 10748 20631 1483 2714 178 O
ATOM 1863 CB LEU A1038 3.889 230.283 28.532 1.00105.23 C
ANISOU 1863 CB LEU A1038 11329 9464 19191 1607 2788 230 C
ATOM 1864 CG LEU A1038 4.080 231.773 28.747 1.00 97.84 C
ANISOU 1864 CG LEU A1038 10424 8574 18175 1621 2857 107 C
ATOM 1865 CD1 LEU A1038 4.093 232.096 30.227 1.00 94.63 C
ANISOU 1865 CD1 LEU A1038 9904 8325 17727 1709 2887 97 C
ATOM 1866 CD2 LEU A1038 5.390 232.181 28.106 1.00 93.84 C
ANISOU 1866 CD2 LEU A1038 10026 8033 17596 1551 2893 -69 C
ATOM 1867 N ASP A1039 3.578 227.602 26.832 1.00107.35 N
ANISOU 1867 N ASP A1039 11660 9539 19589 1498 2629 434 N
ATOM 1868 CA ASP A1039 3.729 226.165 26.780 1.00107.03 C
ANISOU 1868 CA ASP A1039 11587 9480 19599 1482 2566 518 C
ATOM 1869 C ASP A1039 4.726 225.779 25.716 1.00107.96 C
ANISOU 1869 C ASP A1039 11821 9516 19684 1395 2551 418 C
ATOM 1870 O ASP A1039 5.607 224.985 25.973 1.00118.98 O
ANISOU 1870 O ASP A1039 13196 10931 21081 1388 2547 379 O
ATOM 1871 CB ASP A1039 2.391 225.499 26.503 1.00109.51 C
ANISOU 1871 CB ASP A1039 11870 9759 19981 1485 2484 714 C
ATOM 1872 CG ASP A1039 1.637 225.180 27.766 1.00112.64 C
ANISOU 1872 CG ASP A1039 12120 10260 20420 1574 2472 844 C
ATOM 1873 OD1 ASP A1039 2.075 224.280 28.504 1.00111.55 O
ANISOU 1873 OD1 ASP A1039 11901 10184 20299 1604 2458 871 O
ATOM 1874 OD2 ASP A1039 0.605 225.823 28.025 1.00113.56 O
ANISOU 1874 OD2 ASP A1039 12200 10403 20544 1613 2475 919 O
ATOM 1875 N ALA A1040 4.653 226.401 24.547 1.00105.03 N
ANISOU 1875 N ALA A1040 11574 9065 19268 1329 2545 365 N
ATOM 1876 CA ALA A1040 5.588 226.107 23.471 1.00106.51 C
ANISOU 1876 CA ALA A1040 11880 9189 19402 1243 2525 267 C
ATOM 1877 C ALA A1040 7.012 226.452 23.873 1.00115.80 C
ANISOU 1877 C ALA A1040 13065 10413 20519 1239 2594 96 C
ATOM 1878 O ALA A1040 7.947 225.755 23.519 1.00113.46 O
ANISOU 1878 O ALA A1040 12808 10099 20201 1194 2577 38 O
ATOM 1879 CB ALA A1040 5.203 226.845 22.209 1.00 98.08 C
ANISOU 1879 CB ALA A1040 10942 8049 18277 1180 2505 241 C
ATOM 1880 N GLN A1041 7.183 227.551 24.584 1.00121.73 N
ANISOU 1880 N GLN A1041 13787 11230 21235 1282 2669 13 N
ATOM 1881 CA GLN A1041 8.496 227.944 25.037 1.00128.96 C
ANISOU 1881 CA GLN A1041 14709 12207 22083 1280 2730 -148 C
ATOM 1882 C GLN A1041 9.095 226.922 26.004 1.00140.11 C
ANISOU 1882 C GLN A1041 16024 13684 23528 1320 2726 -135 C
ATOM 1883 O GLN A1041 10.304 226.723 26.018 1.00135.99 O
ANISOU 1883 O GLN A1041 15530 13182 22957 1290 2745 -250 O
ATOM 1884 CB GLN A1041 8.411 229.293 25.730 1.00124.65 C
ANISOU 1884 CB GLN A1041 14139 11734 21489 1327 2799 -221 C
ATOM 1885 CG GLN A1041 9.593 230.198 25.468 1.00123.75 C
ANISOU 1885 CG GLN A1041 14106 11642 21270 1283 2851 -403 C
ATOM 1886 CD GLN A1041 9.501 231.483 26.249 1.00124.73 C
ANISOU 1886 CD GLN A1041 14199 11851 21341 1333 2913 -468 C
ATOM 1887 OE1 GLN A1041 9.017 231.498 27.373 1.00127.22 O
ANISOU 1887 OE1 GLN A1041 14406 12249 21681 1412 2926 -411 O
ATOM 1888 NE2 GLN A1041 9.967 232.569 25.660 1.00122.61 N
ANISOU 1888 NE2 GLN A1041 14025 11571 20990 1286 2945 -584 N
ATOM 1889 N LYS A1042 8.266 226.274 26.818 1.00150.35 N
ANISOU 1889 N LYS A1042 17207 15021 24899 1387 2697 6 N
ATOM 1890 CA LYS A1042 8.813 225.314 27.771 1.00155.99 C
ANISOU 1890 CA LYS A1042 17825 15808 25635 1428 2690 22 C
ATOM 1891 C LYS A1042 9.025 223.952 27.122 1.00165.75 C
ANISOU 1891 C LYS A1042 19084 16971 26922 1379 2623 85 C
ATOM 1892 O LYS A1042 10.086 223.337 27.277 1.00168.08 O
ANISOU 1892 O LYS A1042 19379 17284 27199 1361 2626 12 O
ATOM 1893 CB LYS A1042 7.887 225.185 28.981 1.00152.99 C
ANISOU 1893 CB LYS A1042 17310 15525 25296 1523 2682 147 C
ATOM 1894 CG LYS A1042 7.753 226.439 29.823 1.00151.08 C
ANISOU 1894 CG LYS A1042 17030 15383 24990 1582 2743 83 C
ATOM 1895 CD LYS A1042 6.900 226.164 31.050 1.00151.47 C
ANISOU 1895 CD LYS A1042 16941 15547 25064 1674 2725 210 C
ATOM 1896 CE LYS A1042 6.767 227.394 31.930 1.00156.41 C
ANISOU 1896 CE LYS A1042 17529 16287 25611 1733 2779 146 C
ATOM 1897 NZ LYS A1042 5.975 227.103 33.159 1.00158.79 N
ANISOU 1897 NZ LYS A1042 17696 16719 25917 1821 2754 267 N
ATOM 1898 N ALA A1043 7.986 223.548 26.390 1.00172.51 N
ANISOU 1898 N ALA A1043 19964 17750 27832 1355 2559 220 N
ATOM 1899 CA ALA A1043 7.902 222.261 25.713 1.00179.14 C
ANISOU 1899 CA ALA A1043 20826 18522 28716 1308 2479 310 C
ATOM 1900 C ALA A1043 8.918 222.003 24.632 1.00186.03 C
ANISOU 1900 C ALA A1043 21820 19328 29535 1220 2465 200 C
ATOM 1901 O ALA A1043 9.104 220.838 24.292 1.00200.77 O
ANISOU 1901 O ALA A1043 23692 21164 31430 1188 2404 254 O
ATOM 1902 CB ALA A1043 6.499 222.002 25.186 1.00180.20 C
ANISOU 1902 CB ALA A1043 20964 18605 28900 1301 2408 477 C
ATOM 1903 N THR A1044 9.571 223.071 24.135 1.00178.40 N
ANISOU 1903 N THR A1044 20947 18352 28486 1182 2518 50 N
ATOM 1904 CA THR A1044 10.627 223.076 23.125 1.00173.82 C
ANISOU 1904 CA THR A1044 20488 17729 27828 1100 2514 -75 C
ATOM 1905 C THR A1044 10.446 221.954 22.105 1.00170.36 C
ANISOU 1905 C THR A1044 20111 17218 27399 1040 2421 6 C
ATOM 1906 O THR A1044 11.030 221.988 21.022 1.00171.07 O
ANISOU 1906 O THR A1044 20320 17266 27413 967 2398 -70 O
ATOM 1907 CB THR A1044 12.031 222.957 23.758 1.00172.93 C
ANISOU 1907 CB THR A1044 20351 17677 27678 1104 2564 -208 C
ATOM 1908 OG1 THR A1044 12.198 221.653 24.328 1.00175.10 O
ANISOU 1908 OG1 THR A1044 20542 17969 28018 1128 2529 -136 O
ATOM 1909 CG2 THR A1044 12.221 224.011 24.839 1.00170.91 C
ANISOU 1909 CG2 THR A1044 20033 17511 27395 1166 2646 -286 C
ATOM 1910 N ASP A1060 17.773 233.104 18.941 1.00126.73 N
ANISOU 1910 N ASP A1060 15301 11967 20882 736 2850 -1303 N
ATOM 1911 CA ASP A1060 16.756 233.385 17.933 1.00129.73 C
ANISOU 1911 CA ASP A1060 15752 12276 21264 716 2811 -1234 C
ATOM 1912 C ASP A1060 15.415 232.802 18.359 1.00136.72 C
ANISOU 1912 C ASP A1060 16563 13116 22268 765 2798 -1101 C
ATOM 1913 O ASP A1060 14.369 233.427 18.183 1.00127.83 O
ANISOU 1913 O ASP A1060 15446 11961 21164 783 2799 -1047 O
ATOM 1914 CB ASP A1060 17.172 232.818 16.575 1.00138.81 C
ANISOU 1914 CB ASP A1060 17012 13377 22352 648 2741 -1233 C
ATOM 1915 CG ASP A1060 18.607 233.154 16.218 1.00142.81 C
ANISOU 1915 CG ASP A1060 17579 13932 22749 603 2747 -1352 C
ATOM 1916 OD1 ASP A1060 19.030 234.303 16.465 1.00142.04 O
ANISOU 1916 OD1 ASP A1060 17490 13888 22591 605 2793 -1434 O
ATOM 1917 OD2 ASP A1060 19.312 232.266 15.693 1.00142.59 O
ANISOU 1917 OD2 ASP A1060 17589 13893 22694 566 2703 -1361 O
ATOM 1918 N PHE A1061 15.459 231.588 18.913 1.00145.43 N
ANISOU 1918 N PHE A1061 17593 14216 23447 788 2781 -1045 N
ATOM 1919 CA PHE A1061 14.252 230.970 19.454 1.00157.52 C
ANISOU 1919 CA PHE A1061 19039 15717 25096 842 2766 -912 C
ATOM 1920 C PHE A1061 13.724 231.760 20.642 1.00167.35 C
ANISOU 1920 C PHE A1061 20189 17018 26380 914 2830 -907 C
ATOM 1921 O PHE A1061 12.524 232.043 20.734 1.00167.44 O
ANISOU 1921 O PHE A1061 20172 17002 26446 949 2826 -815 O
ATOM 1922 CB PHE A1061 14.543 229.521 19.854 1.00159.49 C
ANISOU 1922 CB PHE A1061 19225 15962 25411 852 2735 -860 C
ATOM 1923 CG PHE A1061 13.584 228.962 20.874 1.00158.50 C
ANISOU 1923 CG PHE A1061 18976 15843 25404 926 2739 -741 C
ATOM 1924 CD1 PHE A1061 12.366 228.429 20.484 1.00155.40 C
ANISOU 1924 CD1 PHE A1061 18577 15387 25082 934 2683 -598 C
ATOM 1925 CD2 PHE A1061 13.908 228.957 22.224 1.00159.34 C
ANISOU 1925 CD2 PHE A1061 18973 16029 25541 988 2789 -766 C
ATOM 1926 CE1 PHE A1061 11.486 227.911 21.419 1.00156.41 C
ANISOU 1926 CE1 PHE A1061 18586 15527 25314 1002 2680 -479 C
ATOM 1927 CE2 PHE A1061 13.031 228.442 23.163 1.00159.97 C
ANISOU 1927 CE2 PHE A1061 18937 16126 25720 1060 2786 -650 C
ATOM 1928 CZ PHE A1061 11.819 227.918 22.760 1.00158.61 C
ANISOU 1928 CZ PHE A1061 18755 15888 25623 1068 2732 -504 C
ATOM 1929 N ARG A1062 14.612 232.121 21.570 1.00173.40 N
ANISOU 1929 N ARG A1062 20906 17868 27111 939 2883 -1002 N
ATOM 1930 CA ARG A1062 14.187 232.847 22.760 1.00174.79 C
ANISOU 1930 CA ARG A1062 20992 18113 27306 1012 2936 -1002 C
ATOM 1931 C ARG A1062 13.675 234.241 22.418 1.00158.94 C
ANISOU 1931 C ARG A1062 19036 16103 25250 1008 2963 -1031 C
ATOM 1932 O ARG A1062 12.741 234.730 23.065 1.00161.46 O
ANISOU 1932 O ARG A1062 19292 16443 25611 1067 2986 -975 O
ATOM 1933 CB ARG A1062 15.342 232.919 23.760 1.00181.90 C
ANISOU 1933 CB ARG A1062 21843 19114 28157 1034 2974 -1105 C
ATOM 1934 CG ARG A1062 15.095 233.840 24.939 1.00191.10 C
ANISOU 1934 CG ARG A1062 22934 20372 29302 1104 3023 -1130 C
ATOM 1935 CD ARG A1062 15.896 233.406 26.152 1.00195.94 C
ANISOU 1935 CD ARG A1062 23464 21086 29898 1149 3039 -1175 C
ATOM 1936 NE ARG A1062 15.432 232.123 26.670 1.00201.27 N
ANISOU 1936 NE ARG A1062 24051 21753 30672 1192 3011 -1067 N
ATOM 1937 CZ ARG A1062 14.408 231.984 27.506 1.00203.37 C
ANISOU 1937 CZ ARG A1062 24218 22051 31003 1270 3011 -964 C
ATOM 1938 NH1 ARG A1062 13.737 233.051 27.918 1.00202.33 N
ANISOU 1938 NH1 ARG A1062 24066 21962 30848 1312 3040 -960 N
ATOM 1939 NH2 ARG A1062 14.053 230.779 27.929 1.00204.61 N
ANISOU 1939 NH2 ARG A1062 24295 22203 31243 1305 2979 -861 N
ATOM 1940 N HIS A1063 14.249 234.885 21.399 1.00140.48 N
ANISOU 1940 N HIS A1063 16810 13744 22821 941 2956 -1113 N
ATOM 1941 CA HIS A1063 13.824 236.239 21.054 1.00131.84 C
ANISOU 1941 CA HIS A1063 15768 12650 21676 935 2980 -1145 C
ATOM 1942 C HIS A1063 12.439 236.244 20.419 1.00120.02 C
ANISOU 1942 C HIS A1063 14293 11073 20238 939 2948 -1031 C
ATOM 1943 O HIS A1063 11.633 237.142 20.689 1.00125.68 O
ANISOU 1943 O HIS A1063 14991 11798 20965 973 2975 -1009 O
ATOM 1944 CB HIS A1063 14.843 236.891 20.118 1.00132.82 C
ANISOU 1944 CB HIS A1063 16005 12779 21683 863 2975 -1257 C
ATOM 1945 CG HIS A1063 14.571 238.338 19.843 1.00131.00 C
ANISOU 1945 CG HIS A1063 15824 12561 21390 858 3002 -1302 C
ATOM 1946 ND1 HIS A1063 14.475 239.280 20.844 1.00127.95 N
ANISOU 1946 ND1 HIS A1063 15378 12246 20990 908 3055 -1341 N
ATOM 1947 CD2 HIS A1063 14.377 239.004 18.680 1.00127.40 C
ANISOU 1947 CD2 HIS A1063 15471 12060 20875 809 2979 -1314 C
ATOM 1948 CE1 HIS A1063 14.233 240.464 20.310 1.00129.53 C
ANISOU 1948 CE1 HIS A1063 15642 12440 21133 888 3067 -1375 C
ATOM 1949 NE2 HIS A1063 14.169 240.324 18.998 1.00125.14 N
ANISOU 1949 NE2 HIS A1063 15185 11814 20550 829 3021 -1359 N
ATOM 1950 N GLY A1064 12.143 235.253 19.575 1.00106.53 N
ANISOU 1950 N GLY A1064 12624 9289 18562 904 2885 -955 N
ATOM 1951 CA GLY A1064 10.851 235.223 18.908 1.00 97.38 C
ANISOU 1951 CA GLY A1064 11495 8058 17447 902 2842 -843 C
ATOM 1952 C GLY A1064 9.691 235.073 19.874 1.00 94.68 C
ANISOU 1952 C GLY A1064 11041 7723 17212 978 2857 -730 C
ATOM 1953 O GLY A1064 8.635 235.684 19.691 1.00 85.16 O
ANISOU 1953 O GLY A1064 9842 6490 16027 996 2854 -670 O
ATOM 1954 N PHE A1065 9.868 234.257 20.915 1.00 94.67 N
ANISOU 1954 N PHE A1065 10933 7763 17276 1027 2869 -697 N
ATOM 1955 CA PHE A1065 8.818 234.097 21.914 1.00 95.76 C
ANISOU 1955 CA PHE A1065 10954 7923 17507 1107 2880 -585 C
ATOM 1956 C PHE A1065 8.764 235.273 22.880 1.00110.93 C
ANISOU 1956 C PHE A1065 12821 9926 19401 1162 2949 -644 C
ATOM 1957 O PHE A1065 7.690 235.582 23.409 1.00109.90 O
ANISOU 1957 O PHE A1065 12625 9808 19322 1220 2957 -557 O
ATOM 1958 CB PHE A1065 9.010 232.789 22.683 1.00 95.42 C
ANISOU 1958 CB PHE A1065 10815 7904 17536 1142 2861 -522 C
ATOM 1959 CG PHE A1065 8.416 231.591 21.998 1.00 94.12 C
ANISOU 1959 CG PHE A1065 10664 7661 17435 1117 2782 -397 C
ATOM 1960 CD1 PHE A1065 7.074 231.283 22.157 1.00 87.54 C
ANISOU 1960 CD1 PHE A1065 9775 6802 16685 1157 2747 -243 C
ATOM 1961 CD2 PHE A1065 9.196 230.773 21.198 1.00 93.62 C
ANISOU 1961 CD2 PHE A1065 10671 7558 17341 1052 2738 -429 C
ATOM 1962 CE1 PHE A1065 6.522 230.183 21.530 1.00 93.52 C
ANISOU 1962 CE1 PHE A1065 10548 7496 17491 1130 2666 -123 C
ATOM 1963 CE2 PHE A1065 8.648 229.670 20.568 1.00 87.27 C
ANISOU 1963 CE2 PHE A1065 9883 6690 16584 1027 2659 -313 C
ATOM 1964 CZ PHE A1065 7.310 229.375 20.735 1.00 88.79 C
ANISOU 1964 CZ PHE A1065 10021 6858 16856 1065 2621 -160 C
ATOM 1965 N ASP A1066 9.899 235.935 23.127 1.00120.00 N
ANISOU 1965 N ASP A1066 13997 11138 20461 1146 2992 -786 N
ATOM 1966 CA ASP A1066 9.875 237.154 23.929 1.00118.47 C
ANISOU 1966 CA ASP A1066 13768 11025 20220 1191 3049 -849 C
ATOM 1967 C ASP A1066 9.058 238.240 23.243 1.00107.23 C
ANISOU 1967 C ASP A1066 12408 9557 18777 1176 3055 -838 C
ATOM 1968 O ASP A1066 8.331 238.992 23.902 1.00117.33 O
ANISOU 1968 O ASP A1066 13634 10878 20068 1232 3085 -812 O
ATOM 1969 CB ASP A1066 11.299 237.642 24.197 1.00131.56 C
ANISOU 1969 CB ASP A1066 15455 12757 21775 1167 3081 -1002 C
ATOM 1970 CG ASP A1066 12.039 236.767 25.190 1.00148.94 C
ANISOU 1970 CG ASP A1066 17574 15029 23987 1202 3084 -1018 C
ATOM 1971 OD1 ASP A1066 11.373 236.099 26.008 1.00156.55 O
ANISOU 1971 OD1 ASP A1066 18437 16019 25028 1267 3075 -919 O
ATOM 1972 OD2 ASP A1066 13.288 236.751 25.153 1.00151.05 O
ANISOU 1972 OD2 ASP A1066 17877 15333 24182 1165 3091 -1125 O
ATOM 1973 N ILE A1067 9.162 238.334 21.915 1.00 95.67 N
ANISOU 1973 N ILE A1067 11059 8015 17276 1101 3023 -856 N
ATOM 1974 CA ILE A1067 8.342 239.283 21.171 1.00 87.82 C
ANISOU 1974 CA ILE A1067 10131 6974 16262 1083 3019 -837 C
ATOM 1975 C ILE A1067 6.876 238.876 21.227 1.00 85.47 C
ANISOU 1975 C ILE A1067 9784 6627 16065 1124 2989 -683 C
ATOM 1976 O ILE A1067 5.989 239.718 21.411 1.00 84.93 O
ANISOU 1976 O ILE A1067 9699 6562 16008 1157 3009 -649 O
ATOM 1977 CB ILE A1067 8.839 239.395 19.718 1.00 83.17 C
ANISOU 1977 CB ILE A1067 9679 6324 15597 996 2980 -889 C
ATOM 1978 CG1 ILE A1067 10.300 239.845 19.680 1.00 86.40 C
ANISOU 1978 CG1 ILE A1067 10134 6790 15905 957 3007 -1036 C
ATOM 1979 CG2 ILE A1067 7.962 240.355 18.926 1.00 79.12 C
ANISOU 1979 CG2 ILE A1067 9237 5766 15060 979 2970 -866 C
ATOM 1980 CD1 ILE A1067 10.896 239.866 18.288 1.00 80.28 C
ANISOU 1980 CD1 ILE A1067 9486 5969 15047 876 2962 -1084 C
ATOM 1981 N LEU A1068 6.598 237.578 21.078 1.00 81.70 N
ANISOU 1981 N LEU A1068 9280 6106 15657 1122 2936 -584 N
ATOM 1982 CA LEU A1068 5.217 237.108 21.041 1.00 76.73 C
ANISOU 1982 CA LEU A1068 8609 5429 15117 1153 2894 -426 C
ATOM 1983 C LEU A1068 4.519 237.339 22.376 1.00 82.64 C
ANISOU 1983 C LEU A1068 9227 6245 15927 1245 2933 -362 C
ATOM 1984 O LEU A1068 3.399 237.862 22.419 1.00 82.38 O
ANISOU 1984 O LEU A1068 9174 6199 15927 1276 2931 -284 O
ATOM 1985 CB LEU A1068 5.181 235.627 20.666 1.00 77.14 C
ANISOU 1985 CB LEU A1068 8656 5432 15220 1130 2824 -336 C
ATOM 1986 CG LEU A1068 3.800 235.036 20.383 1.00 77.52 C
ANISOU 1986 CG LEU A1068 8683 5425 15347 1145 2759 -167 C
ATOM 1987 CD1 LEU A1068 3.258 235.562 19.063 1.00 75.09 C
ANISOU 1987 CD1 LEU A1068 8499 5047 14985 1086 2715 -159 C
ATOM 1988 CD2 LEU A1068 3.859 233.518 20.382 1.00 73.00 C
ANISOU 1988 CD2 LEU A1068 8075 4832 14831 1138 2698 -77 C
ATOM 1989 N VAL A1069 5.166 236.955 23.478 1.00 84.15 N
ANISOU 1989 N VAL A1069 9328 6517 16127 1291 2964 -394 N
ATOM 1990 CA VAL A1069 4.568 237.162 24.793 1.00 91.78 C
ANISOU 1990 CA VAL A1069 10169 7569 17132 1383 2993 -337 C
ATOM 1991 C VAL A1069 4.454 238.650 25.099 1.00 90.11 C
ANISOU 1991 C VAL A1069 9970 7410 16858 1405 3048 -417 C
ATOM 1992 O VAL A1069 3.452 239.106 25.664 1.00 89.91 O
ANISOU 1992 O VAL A1069 9881 7418 16864 1465 3058 -341 O
ATOM 1993 CB VAL A1069 5.378 236.418 25.872 1.00 98.00 C
ANISOU 1993 CB VAL A1069 10867 8446 17922 1424 3005 -364 C
ATOM 1994 CG1 VAL A1069 4.815 236.704 27.256 1.00 94.58 C
ANISOU 1994 CG1 VAL A1069 10308 8125 17501 1521 3030 -314 C
ATOM 1995 CG2 VAL A1069 5.377 234.922 25.595 1.00103.89 C
ANISOU 1995 CG2 VAL A1069 11594 9140 18740 1406 2947 -271 C
ATOM 1996 N GLY A1070 5.469 239.430 24.725 1.00 94.46 N
ANISOU 1996 N GLY A1070 10604 7974 17314 1356 3081 -565 N
ATOM 1997 CA GLY A1070 5.411 240.863 24.961 1.00 94.25 C
ANISOU 1997 CA GLY A1070 10594 7996 17219 1371 3128 -643 C
ATOM 1998 C GLY A1070 4.295 241.539 24.188 1.00 93.97 C
ANISOU 1998 C GLY A1070 10611 7887 17205 1358 3117 -582 C
ATOM 1999 O GLY A1070 3.638 242.451 24.696 1.00 97.11 O
ANISOU 1999 O GLY A1070 10973 8328 17596 1405 3147 -571 O
ATOM 2000 N GLN A1071 4.066 241.102 22.947 1.00 83.36 N
ANISOU 2000 N GLN A1071 9355 6439 15879 1293 3070 -542 N
ATOM 2001 CA GLN A1071 2.991 241.683 22.149 1.00 85.76 C
ANISOU 2001 CA GLN A1071 9716 6675 16196 1277 3049 -479 C
ATOM 2002 C GLN A1071 1.619 241.289 22.679 1.00 89.57 C
ANISOU 2002 C GLN A1071 10105 7151 16776 1342 3027 -319 C
ATOM 2003 O GLN A1071 0.670 242.075 22.579 1.00 97.12 O
ANISOU 2003 O GLN A1071 11066 8094 17742 1361 3034 -276 O
ATOM 2004 CB GLN A1071 3.136 241.267 20.686 1.00 88.17 C
ANISOU 2004 CB GLN A1071 10142 6884 16474 1192 2991 -478 C
ATOM 2005 CG GLN A1071 4.266 241.969 19.954 1.00 87.46 C
ANISOU 2005 CG GLN A1071 10160 6797 16273 1125 3007 -627 C
ATOM 2006 CD GLN A1071 4.434 241.472 18.534 1.00 87.47 C
ANISOU 2006 CD GLN A1071 10279 6720 16236 1046 2940 -620 C
ATOM 2007 OE1 GLN A1071 4.011 240.367 18.197 1.00 91.22 O
ANISOU 2007 OE1 GLN A1071 10750 7147 16765 1037 2880 -521 O
ATOM 2008 NE2 GLN A1071 5.052 242.290 17.691 1.00 85.78 N
ANISOU 2008 NE2 GLN A1071 10170 6501 15922 990 2942 -723 N
ATOM 2009 N ILE A1072 1.489 240.083 23.236 1.00 86.11 N
ANISOU 2009 N ILE A1072 9582 6726 16409 1375 2998 -226 N
ATOM 2010 CA ILE A1072 0.234 239.699 23.874 1.00 79.87 C
ANISOU 2010 CA ILE A1072 8689 5950 15706 1443 2975 -68 C
ATOM 2011 C ILE A1072 -0.006 240.545 25.118 1.00 86.75 C
ANISOU 2011 C ILE A1072 9467 6930 16563 1524 3031 -87 C
ATOM 2012 O ILE A1072 -1.135 240.974 25.386 1.00 76.14 O
ANISOU 2012 O ILE A1072 8079 5597 15255 1569 3028 5 O
ATOM 2013 CB ILE A1072 0.236 238.195 24.201 1.00 72.68 C
ANISOU 2013 CB ILE A1072 7709 5040 14866 1458 2926 34 C
ATOM 2014 CG1 ILE A1072 0.273 237.370 22.915 1.00 71.91 C
ANISOU 2014 CG1 ILE A1072 7708 4837 14778 1379 2857 70 C
ATOM 2015 CG2 ILE A1072 -0.982 237.823 25.032 1.00 74.49 C
ANISOU 2015 CG2 ILE A1072 7817 5309 15174 1535 2902 197 C
ATOM 2016 CD1 ILE A1072 0.307 235.880 23.154 1.00 71.17 C
ANISOU 2016 CD1 ILE A1072 7553 4739 14748 1386 2803 168 C
ATOM 2017 N ASP A1073 1.051 240.804 25.894 1.00 94.91 N
ANISOU 2017 N ASP A1073 10471 8054 17536 1543 3077 -205 N
ATOM 2018 CA ASP A1073 0.919 241.666 27.064 1.00 99.43 C
ANISOU 2018 CA ASP A1073 10965 8746 18068 1616 3123 -237 C
ATOM 2019 C ASP A1073 0.513 243.079 26.665 1.00 95.97 C
ANISOU 2019 C ASP A1073 10589 8292 17584 1604 3155 -290 C
ATOM 2020 O ASP A1073 -0.232 243.748 27.391 1.00 93.90 O
ANISOU 2020 O ASP A1073 10262 8096 17319 1667 3174 -252 O
ATOM 2021 CB ASP A1073 2.228 241.690 27.855 1.00105.21 C
ANISOU 2021 CB ASP A1073 11672 9580 18723 1628 3155 -365 C
ATOM 2022 CG ASP A1073 2.531 240.364 28.523 1.00119.46 C
ANISOU 2022 CG ASP A1073 13392 11428 20571 1659 3127 -306 C
ATOM 2023 OD1 ASP A1073 1.583 239.590 28.774 1.00122.48 O
ANISOU 2023 OD1 ASP A1073 13700 11802 21036 1698 3089 -156 O
ATOM 2024 OD2 ASP A1073 3.719 240.099 28.805 1.00121.97 O
ANISOU 2024 OD2 ASP A1073 13717 11792 20835 1643 3139 -408 O
ATOM 2025 N ASP A1074 0.997 243.553 25.514 1.00 96.55 N
ANISOU 2025 N ASP A1074 10788 8285 17613 1524 3158 -377 N
ATOM 2026 CA ASP A1074 0.593 244.869 25.029 1.00 94.87 C
ANISOU 2026 CA ASP A1074 10641 8049 17355 1507 3183 -423 C
ATOM 2027 C ASP A1074 -0.904 244.910 24.751 1.00 94.58 C
ANISOU 2027 C ASP A1074 10586 7957 17392 1530 3154 -280 C
ATOM 2028 O ASP A1074 -1.606 245.827 25.191 1.00106.26 O
ANISOU 2028 O ASP A1074 12032 9477 18864 1575 3180 -265 O
ATOM 2029 CB ASP A1074 1.383 245.234 23.771 1.00101.03 C
ANISOU 2029 CB ASP A1074 11560 8757 18069 1413 3178 -529 C
ATOM 2030 CG ASP A1074 2.875 245.342 24.025 1.00103.40 C
ANISOU 2030 CG ASP A1074 11883 9119 18286 1386 3206 -673 C
ATOM 2031 OD1 ASP A1074 3.283 245.347 25.206 1.00103.59 O
ANISOU 2031 OD1 ASP A1074 11821 9247 18291 1442 3233 -705 O
ATOM 2032 OD2 ASP A1074 3.640 245.430 23.041 1.00101.72 O
ANISOU 2032 OD2 ASP A1074 11774 8856 18017 1310 3194 -752 O
ATOM 2033 N ALA A1075 -1.412 243.914 24.022 1.00 92.57 N
ANISOU 2033 N ALA A1075 10354 7614 17205 1500 3095 -172 N
ATOM 2034 CA ALA A1075 -2.838 243.870 23.726 1.00 91.60 C
ANISOU 2034 CA ALA A1075 10216 7439 17148 1518 3057 -28 C
ATOM 2035 C ALA A1075 -3.662 243.533 24.962 1.00 92.74 C
ANISOU 2035 C ALA A1075 10216 7663 17355 1611 3056 92 C
ATOM 2036 O ALA A1075 -4.813 243.970 25.073 1.00 91.94 O
ANISOU 2036 O ALA A1075 10084 7561 17287 1646 3048 185 O
ATOM 2037 CB ALA A1075 -3.112 242.860 22.612 1.00 92.14 C
ANISOU 2037 CB ALA A1075 10352 7404 17254 1457 2981 54 C
ATOM 2038 N LEU A1076 -3.101 242.758 25.894 1.00100.91 N
ANISOU 2038 N LEU A1076 11163 8775 18402 1651 3060 96 N
ATOM 2039 CA LEU A1076 -3.824 242.449 27.124 1.00101.23 C
ANISOU 2039 CA LEU A1076 11064 8915 18484 1741 3054 207 C
ATOM 2040 C LEU A1076 -4.037 243.700 27.965 1.00105.02 C
ANISOU 2040 C LEU A1076 11500 9496 18907 1798 3107 151 C
ATOM 2041 O LEU A1076 -5.104 243.881 28.563 1.00 97.08 O
ANISOU 2041 O LEU A1076 10414 8540 17932 1860 3097 259 O
ATOM 2042 CB LEU A1076 -3.072 241.391 27.929 1.00 93.30 C
ANISOU 2042 CB LEU A1076 9982 7983 17486 1768 3045 208 C
ATOM 2043 CG LEU A1076 -3.567 239.954 27.784 1.00 93.85 C
ANISOU 2043 CG LEU A1076 10006 8009 17643 1767 2976 360 C
ATOM 2044 CD1 LEU A1076 -2.672 239.015 28.571 1.00 95.40 C
ANISOU 2044 CD1 LEU A1076 10134 8281 17833 1790 2974 338 C
ATOM 2045 CD2 LEU A1076 -5.012 239.844 28.248 1.00 87.10 C
ANISOU 2045 CD2 LEU A1076 9063 7186 16847 1826 2941 532 C
ATOM 2046 N LYS A1077 -3.030 244.574 28.023 1.00111.72 N
ANISOU 2046 N LYS A1077 12402 10382 19667 1778 3158 -14 N
ATOM 2047 CA LYS A1077 -3.163 245.805 28.795 1.00117.13 C
ANISOU 2047 CA LYS A1077 13053 11167 20284 1827 3203 -76 C
ATOM 2048 C LYS A1077 -4.180 246.745 28.162 1.00121.20 C
ANISOU 2048 C LYS A1077 13617 11617 20815 1817 3208 -39 C
ATOM 2049 O LYS A1077 -4.952 247.402 28.870 1.00126.15 O
ANISOU 2049 O LYS A1077 14179 12318 21434 1878 3221 2 O
ATOM 2050 CB LYS A1077 -1.803 246.491 28.926 1.00119.84 C
ANISOU 2050 CB LYS A1077 13451 11562 20522 1799 3246 -260 C
ATOM 2051 CG LYS A1077 -1.840 247.777 29.730 1.00127.72 C
ANISOU 2051 CG LYS A1077 14420 12673 21437 1845 3286 -333 C
ATOM 2052 CD LYS A1077 -0.451 248.352 29.932 1.00134.85 C
ANISOU 2052 CD LYS A1077 15369 13638 22230 1818 3317 -505 C
ATOM 2053 CE LYS A1077 -0.517 249.662 30.698 1.00138.37 C
ANISOU 2053 CE LYS A1077 15791 14196 22587 1863 3348 -574 C
ATOM 2054 NZ LYS A1077 -1.257 250.717 29.950 1.00142.68 N
ANISOU 2054 NZ LYS A1077 16403 14669 23139 1839 3365 -572 N
ATOM 2055 N LEU A1078 -4.197 246.822 26.829 1.00118.69 N
ANISOU 2055 N LEU A1078 13416 11169 20512 1740 3193 -54 N
ATOM 2056 CA LEU A1078 -5.194 247.642 26.151 1.00112.63 C
ANISOU 2056 CA LEU A1078 12700 10335 19759 1726 3190 -12 C
ATOM 2057 C LEU A1078 -6.593 247.058 26.297 1.00113.25 C
ANISOU 2057 C LEU A1078 12706 10394 19929 1769 3143 174 C
ATOM 2058 O LEU A1078 -7.580 247.803 26.264 1.00118.22 O
ANISOU 2058 O LEU A1078 13331 11019 20570 1793 3146 227 O
ATOM 2059 CB LEU A1078 -4.830 247.794 24.674 1.00110.72 C
ANISOU 2059 CB LEU A1078 12603 9971 19494 1630 3174 -73 C
ATOM 2060 CG LEU A1078 -3.484 248.466 24.394 1.00113.85 C
ANISOU 2060 CG LEU A1078 13081 10384 19792 1580 3215 -253 C
ATOM 2061 CD1 LEU A1078 -3.110 248.359 22.922 1.00111.56 C
ANISOU 2061 CD1 LEU A1078 12927 9983 19476 1484 3183 -295 C
ATOM 2062 CD2 LEU A1078 -3.510 249.920 24.840 1.00113.92 C
ANISOU 2062 CD2 LEU A1078 13091 10460 19734 1606 3267 -338 C
ATOM 2063 N ALA A1079 -6.703 245.737 26.457 1.00115.97 N
ANISOU 2063 N ALA A1079 12996 10731 20335 1778 3095 279 N
ATOM 2064 CA ALA A1079 -8.017 245.130 26.642 1.00117.82 C
ANISOU 2064 CA ALA A1079 13156 10958 20650 1817 3042 464 C
ATOM 2065 C ALA A1079 -8.542 245.375 28.051 1.00121.40 C
ANISOU 2065 C ALA A1079 13474 11552 21100 1913 3060 520 C
ATOM 2066 O ALA A1079 -9.737 245.631 28.239 1.00118.84 O
ANISOU 2066 O ALA A1079 13104 11241 20811 1951 3040 634 O
ATOM 2067 CB ALA A1079 -7.953 243.633 26.339 1.00118.48 C
ANISOU 2067 CB ALA A1079 13228 10995 20795 1792 2978 560 C
ATOM 2068 N ASN A1080 -7.665 245.305 29.056 1.00127.97 N
ANISOU 2068 N ASN A1080 14244 12499 21882 1951 3093 440 N
ATOM 2069 CA ASN A1080 -8.078 245.583 30.426 1.00134.06 C
ANISOU 2069 CA ASN A1080 14892 13423 22622 2039 3104 477 C
ATOM 2070 C ASN A1080 -8.480 247.039 30.624 1.00139.17 C
ANISOU 2070 C ASN A1080 15552 14111 23215 2063 3147 418 C
ATOM 2071 O ASN A1080 -9.258 247.335 31.537 1.00139.05 O
ANISOU 2071 O ASN A1080 15443 14201 23189 2131 3143 488 O
ATOM 2072 CB ASN A1080 -6.958 245.209 31.397 1.00132.72 C
ANISOU 2072 CB ASN A1080 14666 13372 22390 2067 3122 390 C
ATOM 2073 CG ASN A1080 -6.714 243.715 31.452 1.00128.17 C
ANISOU 2073 CG ASN A1080 14048 12781 21870 2060 3075 471 C
ATOM 2074 OD1 ASN A1080 -7.636 242.919 31.276 1.00127.15 O
ANISOU 2074 OD1 ASN A1080 13879 12612 21819 2068 3021 630 O
ATOM 2075 ND2 ASN A1080 -5.468 243.325 31.695 1.00128.82 N
ANISOU 2075 ND2 ASN A1080 14140 12898 21908 2045 3091 365 N
ATOM 2076 N GLU A1081 -7.970 247.949 29.795 1.00143.72 N
ANISOU 2076 N GLU A1081 16243 14613 23751 2007 3185 291 N
ATOM 2077 CA GLU A1081 -8.367 249.349 29.846 1.00143.45 C
ANISOU 2077 CA GLU A1081 16233 14602 23668 2021 3223 235 C
ATOM 2078 C GLU A1081 -9.647 249.627 29.071 1.00144.56 C
ANISOU 2078 C GLU A1081 16407 14646 23874 2008 3198 346 C
ATOM 2079 O GLU A1081 -10.071 250.786 29.001 1.00152.93 O
ANISOU 2079 O GLU A1081 17492 15711 24901 2017 3227 309 O
ATOM 2080 CB GLU A1081 -7.236 250.235 29.313 1.00144.21 C
ANISOU 2080 CB GLU A1081 16439 14672 23684 1964 3269 51 C
ATOM 2081 CG GLU A1081 -5.973 250.214 30.162 1.00147.46 C
ANISOU 2081 CG GLU A1081 16820 15197 24011 1979 3294 -72 C
ATOM 2082 CD GLU A1081 -4.809 250.926 29.498 1.00150.44 C
ANISOU 2082 CD GLU A1081 17313 15536 24313 1911 3329 -241 C
ATOM 2083 OE1 GLU A1081 -4.899 251.213 28.286 1.00151.87 O
ANISOU 2083 OE1 GLU A1081 17599 15592 24513 1843 3328 -259 O
ATOM 2084 OE2 GLU A1081 -3.803 251.197 30.188 1.00151.01 O
ANISOU 2084 OE2 GLU A1081 17369 15708 24299 1922 3351 -354 O
ATOM 2085 N GLY A1082 -10.268 248.601 28.491 1.00139.37 N
ANISOU 2085 N GLY A1082 15750 13903 23302 1987 3142 480 N
ATOM 2086 CA GLY A1082 -11.495 248.759 27.743 1.00138.83 C
ANISOU 2086 CA GLY A1082 15714 13745 23289 1972 3106 594 C
ATOM 2087 C GLY A1082 -11.331 249.238 26.318 1.00142.27 C
ANISOU 2087 C GLY A1082 16298 14046 23713 1886 3105 526 C
ATOM 2088 O GLY A1082 -12.342 249.464 25.640 1.00150.57 O
ANISOU 2088 O GLY A1082 17387 15025 24798 1869 3072 610 O
ATOM 2089 N LYS A1083 -10.100 249.404 25.837 1.00135.36 N
ANISOU 2089 N LYS A1083 15508 13140 22782 1831 3135 377 N
ATOM 2090 CA LYS A1083 -9.858 249.876 24.475 1.00127.92 C
ANISOU 2090 CA LYS A1083 14710 12084 21808 1746 3129 303 C
ATOM 2091 C LYS A1083 -9.869 248.664 23.552 1.00125.86 C
ANISOU 2091 C LYS A1083 14502 11729 21591 1687 3060 375 C
ATOM 2092 O LYS A1083 -8.863 247.968 23.403 1.00129.21 O
ANISOU 2092 O LYS A1083 14950 12144 21999 1653 3056 316 O
ATOM 2093 CB LYS A1083 -8.545 250.645 24.398 1.00128.37 C
ANISOU 2093 CB LYS A1083 14833 12167 21775 1711 3186 114 C
ATOM 2094 CG LYS A1083 -8.462 251.809 25.378 1.00119.21 C
ANISOU 2094 CG LYS A1083 13620 11116 20559 1769 3247 37 C
ATOM 2095 CD LYS A1083 -7.116 252.515 25.307 1.00118.17 C
ANISOU 2095 CD LYS A1083 13554 11016 20330 1730 3293 -145 C
ATOM 2096 CE LYS A1083 -7.019 253.618 26.349 1.00125.91 C
ANISOU 2096 CE LYS A1083 14477 12118 21244 1788 3342 -218 C
ATOM 2097 NZ LYS A1083 -5.711 254.329 26.302 1.00130.07 N
ANISOU 2097 NZ LYS A1083 15068 12684 21668 1749 3379 -390 N
ATOM 2098 N VAL A1084 -11.017 248.414 22.927 1.00121.20 N
ANISOU 2098 N VAL A1084 13933 11072 21047 1674 2999 504 N
ATOM 2099 CA VAL A1084 -11.192 247.200 22.137 1.00123.81 C
ANISOU 2099 CA VAL A1084 14303 11329 21412 1623 2918 594 C
ATOM 2100 C VAL A1084 -10.509 247.331 20.782 1.00123.61 C
ANISOU 2100 C VAL A1084 14429 11216 21320 1529 2898 491 C
ATOM 2101 O VAL A1084 -9.748 246.450 20.367 1.00130.67 O
ANISOU 2101 O VAL A1084 15361 12083 22204 1484 2868 465 O
ATOM 2102 CB VAL A1084 -12.689 246.877 21.983 1.00131.34 C
ANISOU 2102 CB VAL A1084 15223 12257 22424 1641 2851 771 C
ATOM 2103 CG1 VAL A1084 -12.874 245.486 21.399 1.00131.00 C
ANISOU 2103 CG1 VAL A1084 15198 12164 22414 1598 2760 876 C
ATOM 2104 CG2 VAL A1084 -13.398 247.009 23.321 1.00140.20 C
ANISOU 2104 CG2 VAL A1084 16198 13478 23592 1736 2876 861 C
ATOM 2105 N LYS A1085 -10.777 248.429 20.071 1.00127.70 N
ANISOU 2105 N LYS A1085 15037 11696 21788 1498 2909 433 N
ATOM 2106 CA LYS A1085 -10.206 248.610 18.740 1.00132.08 C
ANISOU 2106 CA LYS A1085 15739 12179 22266 1409 2881 343 C
ATOM 2107 C LYS A1085 -8.685 248.686 18.793 1.00138.12 C
ANISOU 2107 C LYS A1085 16537 12969 22971 1381 2929 187 C
ATOM 2108 O LYS A1085 -7.998 248.174 17.901 1.00127.32 O
ANISOU 2108 O LYS A1085 15260 11559 21559 1314 2890 140 O
ATOM 2109 CB LYS A1085 -10.784 249.869 18.098 1.00132.87 C
ANISOU 2109 CB LYS A1085 15918 12248 22320 1391 2889 308 C
ATOM 2110 CG LYS A1085 -12.290 249.826 17.897 1.00130.81 C
ANISOU 2110 CG LYS A1085 15640 11956 22106 1409 2832 457 C
ATOM 2111 CD LYS A1085 -12.653 249.272 16.530 1.00127.87 C
ANISOU 2111 CD LYS A1085 15384 11505 21698 1334 2733 504 C
ATOM 2112 CE LYS A1085 -14.143 249.410 16.270 1.00126.72 C
ANISOU 2112 CE LYS A1085 15234 11333 21582 1346 2676 636 C
ATOM 2113 NZ LYS A1085 -14.482 249.290 14.826 1.00127.19 N
ANISOU 2113 NZ LYS A1085 15431 11322 21575 1269 2586 646 N
ATOM 2114 N GLU A1086 -8.141 249.318 19.835 1.00151.05 N
ANISOU 2114 N GLU A1086 18105 14688 24601 1431 3010 107 N
ATOM 2115 CA GLU A1086 -6.692 249.444 19.952 1.00152.53 C
ANISOU 2115 CA GLU A1086 18320 14911 24724 1405 3054 -42 C
ATOM 2116 C GLU A1086 -6.040 248.113 20.307 1.00141.78 C
ANISOU 2116 C GLU A1086 16909 13564 23398 1406 3033 -18 C
ATOM 2117 O GLU A1086 -4.888 247.867 19.928 1.00138.19 O
ANISOU 2117 O GLU A1086 16511 13104 22890 1357 3037 -119 O
ATOM 2118 CB GLU A1086 -6.349 250.511 20.993 1.00159.97 C
ANISOU 2118 CB GLU A1086 19201 15945 25634 1458 3136 -132 C
ATOM 2119 CG GLU A1086 -4.887 250.917 21.026 1.00169.06 C
ANISOU 2119 CG GLU A1086 20396 17139 26699 1424 3179 -297 C
ATOM 2120 CD GLU A1086 -4.633 252.081 21.963 1.00177.69 C
ANISOU 2120 CD GLU A1086 21443 18328 27744 1471 3247 -385 C
ATOM 2121 OE1 GLU A1086 -5.601 252.792 22.306 1.00179.19 O
ANISOU 2121 OE1 GLU A1086 21595 18534 27955 1517 3262 -334 O
ATOM 2122 OE2 GLU A1086 -3.466 252.282 22.360 1.00183.14 O
ANISOU 2122 OE2 GLU A1086 22134 19081 28371 1463 3280 -503 O
ATOM 2123 N ALA A1087 -6.756 247.244 21.024 1.00130.72 N
ANISOU 2123 N ALA A1087 15402 12184 22083 1462 3008 118 N
ATOM 2124 CA ALA A1087 -6.226 245.925 21.353 1.00118.63 C
ANISOU 2124 CA ALA A1087 13820 10664 20590 1465 2982 155 C
ATOM 2125 C ALA A1087 -6.276 244.987 20.153 1.00106.14 C
ANISOU 2125 C ALA A1087 12326 8992 19008 1392 2899 205 C
ATOM 2126 O ALA A1087 -5.385 244.148 19.982 1.00108.79 O
ANISOU 2126 O ALA A1087 12680 9321 19333 1360 2883 168 O
ATOM 2127 CB ALA A1087 -6.997 245.324 22.529 1.00117.62 C
ANISOU 2127 CB ALA A1087 13545 10599 20544 1549 2976 290 C
ATOM 2128 N GLN A1088 -7.311 245.111 19.318 1.00 97.60 N
ANISOU 2128 N GLN A1088 11302 7848 17932 1366 2842 289 N
ATOM 2129 CA GLN A1088 -7.397 244.282 18.120 1.00 95.01 C
ANISOU 2129 CA GLN A1088 11070 7445 17584 1295 2753 333 C
ATOM 2130 C GLN A1088 -6.277 244.612 17.143 1.00103.94 C
ANISOU 2130 C GLN A1088 12330 8547 18616 1220 2756 186 C
ATOM 2131 O GLN A1088 -5.708 243.713 16.511 1.00105.91 O
ANISOU 2131 O GLN A1088 12635 8768 18840 1169 2704 178 O
ATOM 2132 CB GLN A1088 -8.760 244.461 17.453 1.00 93.38 C
ANISOU 2132 CB GLN A1088 10902 7190 17387 1284 2688 445 C
ATOM 2133 CG GLN A1088 -9.929 243.946 18.274 1.00101.79 C
ANISOU 2133 CG GLN A1088 11846 8283 18545 1349 2663 612 C
ATOM 2134 CD GLN A1088 -11.270 244.307 17.666 1.00108.60 C
ANISOU 2134 CD GLN A1088 12748 9107 19409 1339 2606 711 C
ATOM 2135 OE1 GLN A1088 -11.589 245.483 17.490 1.00108.47 O
ANISOU 2135 OE1 GLN A1088 12768 9084 19361 1344 2642 662 O
ATOM 2136 NE2 GLN A1088 -12.062 243.294 17.336 1.00101.80 N
ANISOU 2136 NE2 GLN A1088 11879 8223 18579 1325 2514 850 N
ATOM 2137 N ALA A1089 -5.948 245.899 17.002 1.00103.06 N
ANISOU 2137 N ALA A1089 12268 8448 18441 1211 2812 72 N
ATOM 2138 CA ALA A1089 -4.844 246.289 16.132 1.00102.75 C
ANISOU 2138 CA ALA A1089 12345 8394 18300 1143 2816 -68 C
ATOM 2139 C ALA A1089 -3.507 245.832 16.702 1.00101.21 C
ANISOU 2139 C ALA A1089 12114 8248 18094 1143 2858 -159 C
ATOM 2140 O ALA A1089 -2.609 245.434 15.951 1.00107.35 O
ANISOU 2140 O ALA A1089 12973 9006 18810 1083 2828 -226 O
ATOM 2141 CB ALA A1089 -4.853 247.802 15.919 1.00 95.91 C
ANISOU 2141 CB ALA A1089 11531 7539 17371 1137 2865 -159 C
ATOM 2142 N ALA A1090 -3.356 245.882 18.029 1.00 94.62 N
ANISOU 2142 N ALA A1090 11159 7482 17311 1211 2923 -163 N
ATOM 2143 CA ALA A1090 -2.134 245.385 18.651 1.00 97.25 C
ANISOU 2143 CA ALA A1090 11451 7867 17634 1216 2958 -243 C
ATOM 2144 C ALA A1090 -2.014 243.874 18.514 1.00 96.47 C
ANISOU 2144 C ALA A1090 11332 7739 17583 1201 2898 -164 C
ATOM 2145 O ALA A1090 -0.901 243.349 18.400 1.00 84.78 O
ANISOU 2145 O ALA A1090 9875 6269 16068 1168 2898 -239 O
ATOM 2146 CB ALA A1090 -2.087 245.789 20.124 1.00 96.87 C
ANISOU 2146 CB ALA A1090 11278 7910 17619 1297 3030 -258 C
ATOM 2147 N ALA A1091 -3.144 243.162 18.525 1.00 95.79 N
ANISOU 2147 N ALA A1091 11202 7620 17573 1225 2843 -10 N
ATOM 2148 CA ALA A1091 -3.124 241.721 18.312 1.00 92.75 C
ANISOU 2148 CA ALA A1091 10804 7206 17229 1206 2775 75 C
ATOM 2149 C ALA A1091 -2.851 241.361 16.859 1.00100.39 C
ANISOU 2149 C ALA A1091 11911 8107 18127 1119 2701 52 C
ATOM 2150 O ALA A1091 -2.481 240.217 16.577 1.00100.20 O
ANISOU 2150 O ALA A1091 11897 8064 18110 1091 2648 83 O
ATOM 2151 CB ALA A1091 -4.448 241.103 18.764 1.00 88.16 C
ANISOU 2151 CB ALA A1091 10135 6621 16742 1256 2730 253 C
ATOM 2152 N GLU A1092 -3.026 242.307 15.934 1.00108.76 N
ANISOU 2152 N GLU A1092 13078 9135 19112 1078 2691 -1 N
ATOM 2153 CA GLU A1092 -2.719 242.033 14.535 1.00117.11 C
ANISOU 2153 CA GLU A1092 14273 10140 20084 998 2616 -30 C
ATOM 2154 C GLU A1092 -1.216 241.968 14.299 1.00112.52 C
ANISOU 2154 C GLU A1092 13741 9580 19431 957 2641 -167 C
ATOM 2155 O GLU A1092 -0.764 241.285 13.373 1.00110.80 O
ANISOU 2155 O GLU A1092 13609 9331 19159 899 2574 -178 O
ATOM 2156 CB GLU A1092 -3.354 243.096 13.638 1.00125.73 C
ANISOU 2156 CB GLU A1092 15462 11198 21112 970 2596 -45 C
ATOM 2157 CG GLU A1092 -3.637 242.617 12.224 1.00132.23 C
ANISOU 2157 CG GLU A1092 16412 11964 21867 902 2488 -8 C
ATOM 2158 CD GLU A1092 -4.714 241.550 12.179 1.00139.44 C
ANISOU 2158 CD GLU A1092 17291 12849 22843 912 2408 151 C
ATOM 2159 OE1 GLU A1092 -5.634 241.597 13.023 1.00147.14 O
ANISOU 2159 OE1 GLU A1092 18163 13838 23905 970 2430 246 O
ATOM 2160 OE2 GLU A1092 -4.638 240.660 11.305 1.00136.56 O
ANISOU 2160 OE2 GLU A1092 17000 12452 22434 861 2319 183 O
ATOM 2161 N GLN A1093 -0.430 242.664 15.125 1.00114.86 N
ANISOU 2161 N GLN A1093 13988 9934 19720 985 2731 -271 N
ATOM 2162 CA GLN A1093 1.023 242.584 15.023 1.00115.01 C
ANISOU 2162 CA GLN A1093 14043 9984 19674 950 2755 -398 C
ATOM 2163 C GLN A1093 1.540 241.183 15.318 1.00112.59 C
ANISOU 2163 C GLN A1093 13689 9679 19410 949 2727 -363 C
ATOM 2164 O GLN A1093 2.660 240.849 14.915 1.00113.46 O
ANISOU 2164 O GLN A1093 13851 9798 19459 905 2719 -447 O
ATOM 2165 CB GLN A1093 1.672 243.586 15.980 1.00125.60 C
ANISOU 2165 CB GLN A1093 15328 11397 20999 986 2853 -506 C
ATOM 2166 CG GLN A1093 1.100 244.992 15.897 1.00127.95 C
ANISOU 2166 CG GLN A1093 15650 11699 21265 998 2888 -534 C
ATOM 2167 CD GLN A1093 1.438 245.684 14.593 1.00135.10 C
ANISOU 2167 CD GLN A1093 16695 12574 22062 929 2855 -607 C
ATOM 2168 OE1 GLN A1093 2.601 245.974 14.314 1.00138.05 O
ANISOU 2168 OE1 GLN A1093 17120 12978 22356 891 2871 -721 O
ATOM 2169 NE2 GLN A1093 0.420 245.952 13.784 1.00137.52 N
ANISOU 2169 NE2 GLN A1093 17063 12826 22362 913 2804 -539 N
ATOM 2170 N LEU A1094 0.750 240.361 16.014 1.00109.98 N
ANISOU 2170 N LEU A1094 13261 9346 19182 997 2711 -238 N
ATOM 2171 CA LEU A1094 1.178 239.005 16.337 1.00104.01 C
ANISOU 2171 CA LEU A1094 12454 8594 18473 1000 2682 -195 C
ATOM 2172 C LEU A1094 1.402 238.168 15.086 1.00116.51 C
ANISOU 2172 C LEU A1094 14145 10124 20002 928 2590 -178 C
ATOM 2173 O LEU A1094 2.257 237.274 15.085 1.00126.31 O
ANISOU 2173 O LEU A1094 15383 11371 21236 907 2575 -205 O
ATOM 2174 CB LEU A1094 0.143 238.335 17.241 1.00 96.47 C
ANISOU 2174 CB LEU A1094 11374 7646 17632 1065 2671 -46 C
ATOM 2175 CG LEU A1094 -0.025 238.929 18.639 1.00 93.22 C
ANISOU 2175 CG LEU A1094 10838 7303 17276 1147 2754 -50 C
ATOM 2176 CD1 LEU A1094 -1.350 238.502 19.242 1.00 99.91 C
ANISOU 2176 CD1 LEU A1094 11588 8153 18221 1207 2726 115 C
ATOM 2177 CD2 LEU A1094 1.127 238.503 19.530 1.00 85.85 C
ANISOU 2177 CD2 LEU A1094 9837 6431 16348 1169 2802 -127 C
ATOM 2178 N LYS A1095 0.650 238.437 14.016 1.00115.92 N
ANISOU 2178 N LYS A1095 14165 9998 19880 890 2526 -135 N
ATOM 2179 CA LYS A1095 0.799 237.650 12.796 1.00120.52 C
ANISOU 2179 CA LYS A1095 14856 10537 20398 824 2429 -116 C
ATOM 2180 C LYS A1095 2.163 237.857 12.151 1.00111.29 C
ANISOU 2180 C LYS A1095 13778 9381 19126 770 2436 -255 C
ATOM 2181 O LYS A1095 2.683 236.944 11.502 1.00113.94 O
ANISOU 2181 O LYS A1095 14171 9700 19422 727 2373 -255 O
ATOM 2182 CB LYS A1095 -0.319 237.990 11.811 1.00123.93 C
ANISOU 2182 CB LYS A1095 15374 10921 20792 798 2357 -46 C
ATOM 2183 CG LYS A1095 -1.693 237.527 12.267 1.00134.89 C
ANISOU 2183 CG LYS A1095 16684 12295 22273 840 2323 111 C
ATOM 2184 CD LYS A1095 -2.764 237.869 11.247 1.00146.14 C
ANISOU 2184 CD LYS A1095 18202 13676 23649 809 2247 174 C
ATOM 2185 CE LYS A1095 -4.114 237.323 11.675 1.00156.25 C
ANISOU 2185 CE LYS A1095 19404 14948 25016 847 2205 336 C
ATOM 2186 NZ LYS A1095 -5.197 237.713 10.730 1.00159.47 N
ANISOU 2186 NZ LYS A1095 19899 15317 25374 819 2133 396 N
ATOM 2187 N THR A1096 2.757 239.041 12.318 1.00102.15 N
ANISOU 2187 N THR A1096 12635 8257 17921 773 2509 -371 N
ATOM 2188 CA THR A1096 4.114 239.257 11.825 1.00 96.42 C
ANISOU 2188 CA THR A1096 11982 7555 17099 727 2520 -501 C
ATOM 2189 C THR A1096 5.113 238.393 12.582 1.00 85.08 C
ANISOU 2189 C THR A1096 10473 6155 15697 738 2551 -536 C
ATOM 2190 O THR A1096 5.994 237.772 11.975 1.00 86.48 O
ANISOU 2190 O THR A1096 10712 6331 15817 693 2511 -579 O
ATOM 2191 CB THR A1096 4.487 240.735 11.940 1.00 95.90 C
ANISOU 2191 CB THR A1096 11935 7525 16977 731 2591 -609 C
ATOM 2192 OG1 THR A1096 3.572 241.522 11.168 1.00105.45 O
ANISOU 2192 OG1 THR A1096 13217 8698 18150 717 2558 -577 O
ATOM 2193 CG2 THR A1096 5.904 240.970 11.436 1.00 83.41 C
ANISOU 2193 CG2 THR A1096 10425 5975 15292 683 2598 -737 C
ATOM 2194 N THR A1097 4.986 238.335 13.910 1.00 85.09 N
ANISOU 2194 N THR A1097 10346 6193 15791 801 2619 -517 N
ATOM 2195 CA THR A1097 5.870 237.490 14.705 1.00 84.45 C
ANISOU 2195 CA THR A1097 10189 6149 15748 817 2646 -544 C
ATOM 2196 C THR A1097 5.639 236.014 14.402 1.00 85.40 C
ANISOU 2196 C THR A1097 10306 6231 15912 802 2567 -444 C
ATOM 2197 O THR A1097 6.586 235.219 14.396 1.00 87.70 O
ANISOU 2197 O THR A1097 10599 6536 16189 780 2556 -483 O
ATOM 2198 CB THR A1097 5.663 237.775 16.194 1.00 88.69 C
ANISOU 2198 CB THR A1097 10589 6739 16369 893 2726 -535 C
ATOM 2199 OG1 THR A1097 5.881 239.168 16.448 1.00 89.93 O
ANISOU 2199 OG1 THR A1097 10757 6938 16476 905 2794 -629 O
ATOM 2200 CG2 THR A1097 6.628 236.959 17.043 1.00 89.37 C
ANISOU 2200 CG2 THR A1097 10600 6872 16486 912 2754 -571 C
ATOM 2201 N ARG A1098 4.387 235.632 14.139 1.00 90.87 N
ANISOU 2201 N ARG A1098 10994 6879 16653 812 2509 -313 N
ATOM 2202 CA ARG A1098 4.075 234.234 13.860 1.00 80.76 C
ANISOU 2202 CA ARG A1098 9708 5565 15410 798 2427 -207 C
ATOM 2203 C ARG A1098 4.695 233.776 12.546 1.00 89.44 C
ANISOU 2203 C ARG A1098 10941 6636 16407 723 2350 -248 C
ATOM 2204 O ARG A1098 5.199 232.651 12.449 1.00 94.43 O
ANISOU 2204 O ARG A1098 11570 7264 17044 703 2309 -231 O
ATOM 2205 CB ARG A1098 2.561 234.039 13.838 1.00 77.52 C
ANISOU 2205 CB ARG A1098 9269 5122 15063 823 2376 -57 C
ATOM 2206 CG ARG A1098 2.113 232.649 13.429 1.00 85.90 C
ANISOU 2206 CG ARG A1098 10337 6152 16150 802 2279 60 C
ATOM 2207 CD ARG A1098 0.695 232.691 12.901 1.00100.26 C
ANISOU 2207 CD ARG A1098 12185 7934 17976 799 2209 183 C
ATOM 2208 NE ARG A1098 0.584 233.587 11.753 1.00108.66 N
ANISOU 2208 NE ARG A1098 13383 8969 18934 751 2182 124 N
ATOM 2209 CZ ARG A1098 -0.568 234.000 11.236 1.00108.14 C
ANISOU 2209 CZ ARG A1098 13359 8875 18855 747 2136 198 C
ATOM 2210 NH1 ARG A1098 -1.716 233.604 11.767 1.00110.00 N
ANISOU 2210 NH1 ARG A1098 13511 9108 19175 786 2112 334 N
ATOM 2211 NH2 ARG A1098 -0.571 234.816 10.190 1.00105.39 N
ANISOU 2211 NH2 ARG A1098 13134 8504 18405 703 2111 137 N
ATOM 2212 N ASN A1099 4.672 234.637 11.527 1.00103.95 N
ANISOU 2212 N ASN A1099 12895 8455 18147 681 2327 -301 N
ATOM 2213 CA ASN A1099 5.219 234.278 10.224 1.00107.12 C
ANISOU 2213 CA ASN A1099 13429 8834 18439 613 2248 -336 C
ATOM 2214 C ASN A1099 6.743 234.276 10.228 1.00107.57 C
ANISOU 2214 C ASN A1099 13507 8929 18437 588 2284 -464 C
ATOM 2215 O ASN A1099 7.366 233.425 9.584 1.00113.89 O
ANISOU 2215 O ASN A1099 14366 9720 19187 546 2224 -473 O
ATOM 2216 CB ASN A1099 4.699 235.237 9.152 1.00105.49 C
ANISOU 2216 CB ASN A1099 13336 8600 18144 580 2209 -349 C
ATOM 2217 CG ASN A1099 3.188 235.236 9.054 1.00114.11 C
ANISOU 2217 CG ASN A1099 14418 9655 19284 599 2165 -224 C
ATOM 2218 OD1 ASN A1099 2.532 234.258 9.413 1.00116.47 O
ANISOU 2218 OD1 ASN A1099 14656 9940 19658 618 2128 -112 O
ATOM 2219 ND2 ASN A1099 2.626 236.334 8.564 1.00121.70 N
ANISOU 2219 ND2 ASN A1099 15437 10602 20200 593 2166 -238 N
ATOM 2220 N ALA A1100 7.362 235.214 10.944 1.00107.52 N
ANISOU 2220 N ALA A1100 13454 8969 18431 613 2379 -562 N
ATOM 2221 CA ALA A1100 8.811 235.342 10.887 1.00102.03 C
ANISOU 2221 CA ALA A1100 12785 8315 17665 586 2410 -686 C
ATOM 2222 C ALA A1100 9.531 234.453 11.894 1.00103.40 C
ANISOU 2222 C ALA A1100 12859 8523 17906 611 2449 -699 C
ATOM 2223 O ALA A1100 10.724 234.186 11.714 1.00106.66 O
ANISOU 2223 O ALA A1100 13301 8962 18261 581 2451 -781 O
ATOM 2224 CB ALA A1100 9.221 236.799 11.108 1.00103.91 C
ANISOU 2224 CB ALA A1100 13031 8595 17855 594 2486 -791 C
ATOM 2225 N TYR A1101 8.845 233.986 12.938 1.00101.27 N
ANISOU 2225 N TYR A1101 12471 8253 17752 667 2476 -616 N
ATOM 2226 CA TYR A1101 9.514 233.226 13.989 1.00107.40 C
ANISOU 2226 CA TYR A1101 13146 9068 18595 697 2517 -631 C
ATOM 2227 C TYR A1101 8.789 231.931 14.336 1.00140.16 C
ANISOU 2227 C TYR A1101 17225 13188 22843 722 2468 -497 C
ATOM 2228 O TYR A1101 9.383 230.849 14.285 1.00104.31 O
ANISOU 2228 O TYR A1101 12678 8645 18309 704 2434 -490 O
ATOM 2229 CB TYR A1101 9.657 234.081 15.250 1.00101.69 C
ANISOU 2229 CB TYR A1101 12322 8402 17912 754 2617 -685 C
ATOM 2230 CG TYR A1101 10.586 235.263 15.105 1.00108.86 C
ANISOU 2230 CG TYR A1101 13283 9356 18722 731 2670 -826 C
ATOM 2231 CD1 TYR A1101 11.961 235.109 15.225 1.00111.43 C
ANISOU 2231 CD1 TYR A1101 13619 9728 18993 707 2691 -930 C
ATOM 2232 CD2 TYR A1101 10.088 236.537 14.863 1.00104.68 C
ANISOU 2232 CD2 TYR A1101 12791 8826 18154 734 2695 -850 C
ATOM 2233 CE1 TYR A1101 12.815 236.189 15.100 1.00112.24 C
ANISOU 2233 CE1 TYR A1101 13767 9877 19002 686 2733 -1051 C
ATOM 2234 CE2 TYR A1101 10.934 237.623 14.737 1.00101.43 C
ANISOU 2234 CE2 TYR A1101 12426 8461 17652 713 2738 -972 C
ATOM 2235 CZ TYR A1101 12.296 237.444 14.856 1.00111.05 C
ANISOU 2235 CZ TYR A1101 13652 9727 18815 689 2755 -1070 C
ATOM 2236 OH TYR A1101 13.139 238.524 14.731 1.00119.48 O
ANISOU 2236 OH TYR A1101 14764 10844 19789 667 2792 -1184 O
ATOM 2237 N ILE A1102 7.507 232.033 14.693 1.00154.02 N
ANISOU 2237 N ILE A1102 20434 18735 19350 1093 -891 1717 N
ATOM 2238 CA ILE A1102 6.807 230.906 15.304 1.00145.72 C
ANISOU 2238 CA ILE A1102 19273 17722 18371 1110 -914 1712 C
ATOM 2239 C ILE A1102 6.633 229.768 14.304 1.00145.69 C
ANISOU 2239 C ILE A1102 19266 17761 18330 1076 -917 1762 C
ATOM 2240 O ILE A1102 6.887 228.600 14.622 1.00151.12 O
ANISOU 2240 O ILE A1102 19884 18475 19059 1043 -896 1736 O
ATOM 2241 CB ILE A1102 5.456 231.364 15.879 1.00146.92 C
ANISOU 2241 CB ILE A1102 19352 17890 18583 1177 -967 1746 C
ATOM 2242 CG1 ILE A1102 5.655 232.570 16.799 1.00151.78 C
ANISOU 2242 CG1 ILE A1102 19965 18465 19239 1208 -967 1722 C
ATOM 2243 CG2 ILE A1102 4.785 230.226 16.632 1.00144.23 C
ANISOU 2243 CG2 ILE A1102 18871 17602 18327 1180 -961 1727 C
ATOM 2244 CD1 ILE A1102 6.617 232.316 17.938 1.00151.66 C
ANISOU 2244 CD1 ILE A1102 19895 18436 19294 1189 -918 1656 C
ATOM 2245 N GLN A1103 6.193 230.087 13.085 1.00146.83 N
ANISOU 2245 N GLN A1103 19450 17923 18416 1064 -942 1846 N
ATOM 2246 CA GLN A1103 5.976 229.042 12.089 1.00144.32 C
ANISOU 2246 CA GLN A1103 19090 17655 18089 996 -963 1907 C
ATOM 2247 C GLN A1103 7.286 228.366 11.703 1.00135.52 C
ANISOU 2247 C GLN A1103 18000 16538 16953 915 -916 1906 C
ATOM 2248 O GLN A1103 7.321 227.152 11.467 1.00137.34 O
ANISOU 2248 O GLN A1103 18175 16805 17204 858 -924 1912 O
ATOM 2249 CB GLN A1103 5.286 229.619 10.853 1.00146.56 C
ANISOU 2249 CB GLN A1103 19410 17956 18321 983 -1013 1993 C
ATOM 2250 CG GLN A1103 5.001 228.582 9.776 1.00149.34 C
ANISOU 2250 CG GLN A1103 19723 18356 18665 896 -1059 2050 C
ATOM 2251 CD GLN A1103 4.295 229.162 8.567 1.00152.18 C
ANISOU 2251 CD GLN A1103 20117 18729 18975 875 -1123 2128 C
ATOM 2252 OE1 GLN A1103 3.703 230.240 8.635 1.00157.94 O
ANISOU 2252 OE1 GLN A1103 20878 19443 19689 946 -1136 2143 O
ATOM 2253 NE2 GLN A1103 4.357 228.447 7.450 1.00149.13 N
ANISOU 2253 NE2 GLN A1103 19730 18370 18561 775 -1167 2173 N
ATOM 2254 N LYS A1104 8.377 229.133 11.636 1.00134.56 N
ANISOU 2254 N LYS A1104 17964 16375 16789 906 -866 1899 N
ATOM 2255 CA LYS A1104 9.672 228.539 11.318 1.00133.54 C
ANISOU 2255 CA LYS A1104 17860 16244 16637 828 -816 1894 C
ATOM 2256 C LYS A1104 10.143 227.596 12.417 1.00129.87 C
ANISOU 2256 C LYS A1104 17339 15775 16230 835 -786 1814 C
ATOM 2257 O LYS A1104 10.885 226.647 12.140 1.00133.42 O
ANISOU 2257 O LYS A1104 17777 16243 16673 769 -760 1812 O
ATOM 2258 CB LYS A1104 10.713 229.633 11.078 1.00139.41 C
ANISOU 2258 CB LYS A1104 18697 16945 17328 820 -760 1904 C
ATOM 2259 CG LYS A1104 10.475 230.453 9.823 1.00147.50 C
ANISOU 2259 CG LYS A1104 19768 17979 18298 781 -786 1992 C
ATOM 2260 CD LYS A1104 11.612 231.431 9.585 1.00150.74 C
ANISOU 2260 CD LYS A1104 20246 18359 18671 754 -721 2009 C
ATOM 2261 CE LYS A1104 11.396 232.220 8.307 1.00154.49 C
ANISOU 2261 CE LYS A1104 20767 18837 19094 692 -767 2089 C
ATOM 2262 NZ LYS A1104 10.125 232.994 8.345 1.00162.03 N
ANISOU 2262 NZ LYS A1104 21716 19793 20053 784 -809 2120 N
ATOM 2263 N TYR A1105 9.725 227.833 13.661 1.00125.45 N
ANISOU 2263 N TYR A1105 16737 15196 15731 905 -794 1746 N
ATOM 2264 CA TYR A1105 10.141 226.956 14.748 1.00122.56 C
ANISOU 2264 CA TYR A1105 16297 14834 15435 905 -767 1670 C
ATOM 2265 C TYR A1105 9.248 225.728 14.859 1.00117.86 C
ANISOU 2265 C TYR A1105 15596 14296 14889 905 -786 1677 C
ATOM 2266 O TYR A1105 9.738 224.626 15.131 1.00113.59 O
ANISOU 2266 O TYR A1105 15007 13776 14377 875 -756 1649 O
ATOM 2267 CB TYR A1105 10.149 227.713 16.073 1.00128.97 C
ANISOU 2267 CB TYR A1105 17085 15611 16308 956 -768 1593 C
ATOM 2268 CG TYR A1105 10.444 226.802 17.235 1.00139.26 C
ANISOU 2268 CG TYR A1105 18284 16934 17694 959 -731 1519 C
ATOM 2269 CD1 TYR A1105 11.703 226.245 17.389 1.00138.28 C
ANISOU 2269 CD1 TYR A1105 18159 16804 17579 915 -679 1489 C
ATOM 2270 CD2 TYR A1105 9.461 226.476 18.162 1.00139.18 C
ANISOU 2270 CD2 TYR A1105 18176 16955 17750 1006 -740 1480 C
ATOM 2271 CE1 TYR A1105 11.986 225.402 18.436 1.00132.69 C
ANISOU 2271 CE1 TYR A1105 17352 16121 16943 926 -632 1422 C
ATOM 2272 CE2 TYR A1105 9.736 225.630 19.220 1.00134.45 C
ANISOU 2272 CE2 TYR A1105 17474 16385 17226 1011 -687 1425 C
ATOM 2273 CZ TYR A1105 11.002 225.098 19.348 1.00129.26 C
ANISOU 2273 CZ TYR A1105 16827 15717 16568 973 -638 1382 C
ATOM 2274 OH TYR A1105 11.299 224.257 20.388 1.00124.59 O
ANISOU 2274 OH TYR A1105 16144 15155 16040 984 -580 1316 O
ATOM 2275 N LEU A1106 7.945 225.904 14.665 1.00120.41 N
ANISOU 2275 N LEU A1106 15884 14644 15221 939 -837 1712 N
ATOM 2276 CA LEU A1106 6.967 224.821 14.767 1.00119.65 C
ANISOU 2276 CA LEU A1106 15688 14600 15172 938 -862 1722 C
ATOM 2277 C LEU A1106 7.367 223.569 13.995 1.00126.61 C
ANISOU 2277 C LEU A1106 16550 15516 16039 860 -859 1757 C
ATOM 2278 O LEU A1106 7.326 222.466 14.534 1.00138.88 O
ANISOU 2278 O LEU A1106 18028 17096 17642 854 -841 1725 O
ATOM 2279 CB LEU A1106 5.603 225.307 14.275 1.00124.33 C
ANISOU 2279 CB LEU A1106 16270 15213 15755 968 -924 1775 C
ATOM 2280 CG LEU A1106 4.674 224.292 13.600 1.00127.11 C
ANISOU 2280 CG LEU A1106 16554 15621 16122 931 -971 1829 C
ATOM 2281 CD1 LEU A1106 4.048 223.343 14.613 1.00129.56 C
ANISOU 2281 CD1 LEU A1106 16757 15962 16509 957 -958 1783 C
ATOM 2282 CD2 LEU A1106 3.597 225.003 12.787 1.00127.60 C
ANISOU 2282 CD2 LEU A1106 16635 15694 16152 947 -1037 1894 C
ATOM 2283 N GLU A 219 8.791 224.788 11.510 1.00112.89 N
ANISOU 2283 N GLU A 219 15017 13744 14132 735 -872 1871 N
ATOM 2284 CA GLU A 219 8.766 223.426 10.993 1.00107.87 C
ANISOU 2284 CA GLU A 219 14333 13152 13502 658 -896 1890 C
ATOM 2285 C GLU A 219 9.965 222.634 11.505 1.00 98.87 C
ANISOU 2285 C GLU A 219 13190 12005 12370 629 -834 1837 C
ATOM 2286 O GLU A 219 10.105 221.449 11.205 1.00101.43 O
ANISOU 2286 O GLU A 219 13479 12363 12698 567 -846 1841 O
ATOM 2287 CB GLU A 219 8.744 223.432 9.461 1.00120.25 C
ANISOU 2287 CB GLU A 219 15953 14738 14999 558 -954 1960 C
ATOM 2288 CG GLU A 219 7.463 223.992 8.854 1.00130.88 C
ANISOU 2288 CG GLU A 219 17291 16099 16339 580 -1026 2016 C
ATOM 2289 CD GLU A 219 7.700 225.237 8.015 1.00140.39 C
ANISOU 2289 CD GLU A 219 18590 17275 17475 562 -1039 2057 C
ATOM 2290 OE1 GLU A 219 8.874 225.559 7.736 1.00143.58 O
ANISOU 2290 OE1 GLU A 219 19068 17654 17833 510 -998 2048 O
ATOM 2291 OE2 GLU A 219 6.709 225.897 7.636 1.00144.20 O
ANISOU 2291 OE2 GLU A 219 19075 17763 17951 597 -1088 2098 O
ATOM 2292 N ARG A 220 10.826 223.291 12.287 1.00 92.55 N
ANISOU 2292 N ARG A 220 12431 11161 11574 674 -772 1785 N
ATOM 2293 CA ARG A 220 12.034 222.624 12.766 1.00 89.54 C
ANISOU 2293 CA ARG A 220 12053 10769 11197 648 -711 1733 C
ATOM 2294 C ARG A 220 11.724 221.638 13.885 1.00 87.74 C
ANISOU 2294 C ARG A 220 11722 10561 11053 694 -694 1675 C
ATOM 2295 O ARG A 220 12.275 220.532 13.912 1.00 94.50 O
ANISOU 2295 O ARG A 220 12553 11438 11916 654 -670 1658 O
ATOM 2296 CB ARG A 220 13.061 223.654 13.231 1.00 92.01 C
ANISOU 2296 CB ARG A 220 12443 11027 11491 673 -657 1694 C
ATOM 2297 CG ARG A 220 13.735 224.404 12.101 1.00105.21 C
ANISOU 2297 CG ARG A 220 14216 12685 13075 608 -646 1748 C
ATOM 2298 CD ARG A 220 14.773 225.369 12.643 1.00121.34 C
ANISOU 2298 CD ARG A 220 16332 14672 15101 635 -585 1706 C
ATOM 2299 NE ARG A 220 15.326 226.225 11.599 1.00129.81 N
ANISOU 2299 NE ARG A 220 17477 15743 16104 577 -562 1768 N
ATOM 2300 CZ ARG A 220 16.089 227.288 11.832 1.00133.86 C
ANISOU 2300 CZ ARG A 220 18033 16223 16606 593 -501 1755 C
ATOM 2301 NH1 ARG A 220 16.391 227.632 13.078 1.00134.85 N
ANISOU 2301 NH1 ARG A 220 18172 16294 16772 640 -496 1645 N
ATOM 2302 NH2 ARG A 220 16.547 228.010 10.820 1.00135.89 N
ANISOU 2302 NH2 ARG A 220 18336 16482 16812 511 -503 1822 N
ATOM 2303 N ALA A 221 10.858 222.022 14.827 1.00 85.70 N
ANISOU 2303 N ALA A 221 11406 10299 10857 772 -704 1640 N
ATOM 2304 CA ALA A 221 10.460 221.091 15.878 1.00 78.45 C
ANISOU 2304 CA ALA A 221 10382 9407 10017 809 -684 1585 C
ATOM 2305 C ALA A 221 9.736 219.885 15.292 1.00 82.13 C
ANISOU 2305 C ALA A 221 10791 9925 10490 770 -719 1631 C
ATOM 2306 O ALA A 221 9.926 218.753 15.752 1.00 87.08 O
ANISOU 2306 O ALA A 221 11357 10574 11154 763 -690 1599 O
ATOM 2307 CB ALA A 221 9.582 221.802 16.909 1.00 72.64 C
ANISOU 2307 CB ALA A 221 9598 8664 9336 884 -693 1543 C
ATOM 2308 N ARG A 222 8.905 220.109 14.272 1.00 80.05 N
ANISOU 2308 N ARG A 222 10544 9681 10193 741 -783 1704 N
ATOM 2309 CA ARG A 222 8.257 218.998 13.585 1.00 82.82 C
ANISOU 2309 CA ARG A 222 10842 10078 10546 685 -831 1751 C
ATOM 2310 C ARG A 222 9.267 218.163 12.809 1.00 87.73 C
ANISOU 2310 C ARG A 222 11504 10710 11119 591 -826 1767 C
ATOM 2311 O ARG A 222 9.108 216.942 12.695 1.00 82.73 O
ANISOU 2311 O ARG A 222 10819 10112 10504 551 -841 1771 O
ATOM 2312 CB ARG A 222 7.172 219.530 12.650 1.00 85.43 C
ANISOU 2312 CB ARG A 222 11183 10425 10851 671 -907 1823 C
ATOM 2313 CG ARG A 222 6.327 218.465 11.974 1.00 96.16 C
ANISOU 2313 CG ARG A 222 12483 11833 12220 614 -968 1869 C
ATOM 2314 CD ARG A 222 5.400 219.100 10.949 1.00109.31 C
ANISOU 2314 CD ARG A 222 14172 13511 13851 594 -1045 1938 C
ATOM 2315 NE ARG A 222 4.607 220.179 11.531 1.00120.05 N
ANISOU 2315 NE ARG A 222 15524 14855 15236 686 -1045 1931 N
ATOM 2316 CZ ARG A 222 3.867 221.030 10.828 1.00127.30 C
ANISOU 2316 CZ ARG A 222 16473 15772 16122 695 -1100 1981 C
ATOM 2317 NH1 ARG A 222 3.817 220.936 9.506 1.00129.97 N
ANISOU 2317 NH1 ARG A 222 16852 16126 16406 614 -1160 2041 N
ATOM 2318 NH2 ARG A 222 3.178 221.980 11.446 1.00127.97 N
ANISOU 2318 NH2 ARG A 222 16553 15842 16227 781 -1098 1967 N
ATOM 2319 N SER A 223 10.314 218.800 12.279 1.00 96.67 N
ANISOU 2319 N SER A 223 12732 11814 12186 550 -808 1772 N
ATOM 2320 CA SER A 223 11.325 218.068 11.523 1.00 90.79 C
ANISOU 2320 CA SER A 223 12036 11079 11380 447 -806 1779 C
ATOM 2321 C SER A 223 12.182 217.203 12.438 1.00 76.30 C
ANISOU 2321 C SER A 223 10169 9241 9579 466 -737 1716 C
ATOM 2322 O SER A 223 12.576 216.094 12.061 1.00 79.46 O
ANISOU 2322 O SER A 223 10566 9669 9956 394 -746 1716 O
ATOM 2323 CB SER A 223 12.199 219.043 10.735 1.00 92.64 C
ANISOU 2323 CB SER A 223 12384 11283 11531 391 -800 1797 C
ATOM 2324 OG SER A 223 13.228 218.363 10.037 1.00 95.48 O
ANISOU 2324 OG SER A 223 12803 11653 11820 276 -799 1788 O
ATOM 2325 N THR A 224 12.485 217.693 13.642 1.00 68.11 N
ANISOU 2325 N THR A 224 9112 8172 8593 560 -672 1656 N
ATOM 2326 CA THR A 224 13.302 216.915 14.568 1.00 65.52 C
ANISOU 2326 CA THR A 224 8749 7841 8304 587 -602 1589 C
ATOM 2327 C THR A 224 12.555 215.683 15.067 1.00 69.06 C
ANISOU 2327 C THR A 224 9096 8329 8816 607 -610 1574 C
ATOM 2328 O THR A 224 13.140 214.599 15.177 1.00 72.25 O
ANISOU 2328 O THR A 224 9482 8749 9221 581 -581 1552 O
ATOM 2329 CB THR A 224 13.742 217.791 15.741 1.00 65.10 C
ANISOU 2329 CB THR A 224 8691 7747 8296 670 -543 1519 C
ATOM 2330 OG1 THR A 224 14.436 218.942 15.243 1.00 77.18 O
ANISOU 2330 OG1 THR A 224 10321 9238 9766 646 -538 1537 O
ATOM 2331 CG2 THR A 224 14.666 217.018 16.670 1.00 61.30 C
ANISOU 2331 CG2 THR A 224 8169 7267 7856 697 -463 1443 C
ATOM 2332 N LEU A 225 11.262 215.827 15.368 1.00 70.98 N
ANISOU 2332 N LEU A 225 9274 8587 9107 652 -646 1586 N
ATOM 2333 CA LEU A 225 10.481 214.684 15.831 1.00 66.23 C
ANISOU 2333 CA LEU A 225 8579 8023 8564 666 -651 1574 C
ATOM 2334 C LEU A 225 10.403 213.599 14.766 1.00 79.12 C
ANISOU 2334 C LEU A 225 10212 9691 10158 573 -704 1631 C
ATOM 2335 O LEU A 225 10.565 212.411 15.068 1.00 87.10 O
ANISOU 2335 O LEU A 225 11178 10724 11194 561 -684 1608 O
ATOM 2336 CB LEU A 225 9.080 215.134 16.241 1.00 65.43 C
ANISOU 2336 CB LEU A 225 8418 7933 8509 718 -684 1583 C
ATOM 2337 CG LEU A 225 8.912 215.524 17.709 1.00 62.27 C
ANISOU 2337 CG LEU A 225 7972 7518 8171 802 -630 1501 C
ATOM 2338 CD1 LEU A 225 7.541 216.130 17.947 1.00 65.46 C
ANISOU 2338 CD1 LEU A 225 8338 7932 8602 842 -670 1519 C
ATOM 2339 CD2 LEU A 225 9.126 214.313 18.603 1.00 68.91 C
ANISOU 2339 CD2 LEU A 225 8745 8376 9060 816 -576 1441 C
ATOM 2340 N GLN A 226 10.160 213.987 13.511 1.00 81.02 N
ANISOU 2340 N GLN A 226 10508 9940 10336 499 -774 1699 N
ATOM 2341 CA GLN A 226 10.094 213.005 12.434 1.00 83.75 C
ANISOU 2341 CA GLN A 226 10864 10323 10636 391 -837 1743 C
ATOM 2342 C GLN A 226 11.427 212.296 12.239 1.00 84.28 C
ANISOU 2342 C GLN A 226 10985 10388 10649 323 -806 1713 C
ATOM 2343 O GLN A 226 11.453 211.120 11.857 1.00 87.04 O
ANISOU 2343 O GLN A 226 11321 10770 10981 253 -837 1718 O
ATOM 2344 CB GLN A 226 9.649 213.678 11.138 1.00 91.07 C
ANISOU 2344 CB GLN A 226 11849 11256 11499 321 -917 1807 C
ATOM 2345 CG GLN A 226 8.227 214.207 11.183 1.00107.72 C
ANISOU 2345 CG GLN A 226 13901 13374 13653 376 -960 1843 C
ATOM 2346 CD GLN A 226 7.899 215.099 10.004 1.00121.57 C
ANISOU 2346 CD GLN A 226 15721 15125 15344 326 -1026 1900 C
ATOM 2347 OE1 GLN A 226 8.767 215.412 9.189 1.00123.37 O
ANISOU 2347 OE1 GLN A 226 16041 15340 15493 251 -1035 1907 O
ATOM 2348 NE2 GLN A 226 6.642 215.517 9.909 1.00122.89 N
ANISOU 2348 NE2 GLN A 226 15845 15305 15542 366 -1072 1936 N
ATOM 2349 N LYS A 227 12.541 212.988 12.494 1.00 74.82 N
ANISOU 2349 N LYS A 227 9853 9154 9421 338 -748 1680 N
ATOM 2350 CA LYS A 227 13.841 212.328 12.445 1.00 69.95 C
ANISOU 2350 CA LYS A 227 9289 8536 8752 279 -709 1643 C
ATOM 2351 C LYS A 227 14.014 211.351 13.601 1.00 77.90 C
ANISOU 2351 C LYS A 227 10216 9550 9834 354 -642 1590 C
ATOM 2352 O LYS A 227 14.667 210.313 13.441 1.00 74.07 O
ANISOU 2352 O LYS A 227 9747 9092 9304 292 -603 1490 O
ATOM 2353 CB LYS A 227 14.964 213.365 12.449 1.00 66.08 C
ANISOU 2353 CB LYS A 227 8889 8007 8211 277 -654 1610 C
ATOM 2354 CG LYS A 227 15.062 214.170 11.163 1.00 79.89 C
ANISOU 2354 CG LYS A 227 10742 9749 9863 175 -717 1656 C
ATOM 2355 CD LYS A 227 16.176 215.203 11.231 1.00 91.92 C
ANISOU 2355 CD LYS A 227 12352 11234 11337 173 -647 1601 C
ATOM 2356 CE LYS A 227 16.254 216.011 9.943 1.00101.27 C
ANISOU 2356 CE LYS A 227 13645 12410 12423 70 -709 1649 C
ATOM 2357 NZ LYS A 227 17.290 217.080 10.005 1.00106.54 N
ANISOU 2357 NZ LYS A 227 14399 13037 13043 67 -644 1603 N
ATOM 2358 N GLU A 228 13.441 211.659 14.767 1.00 77.75 N
ANISOU 2358 N GLU A 228 10117 9516 9909 477 -595 1556 N
ATOM 2359 CA GLU A 228 13.467 210.703 15.868 1.00 69.69 C
ANISOU 2359 CA GLU A 228 9017 8503 8958 546 -534 1495 C
ATOM 2360 C GLU A 228 12.556 209.513 15.598 1.00 64.92 C
ANISOU 2360 C GLU A 228 8350 7940 8376 507 -589 1527 C
ATOM 2361 O GLU A 228 12.860 208.393 16.024 1.00 65.63 O
ANISOU 2361 O GLU A 228 8406 8044 8487 514 -556 1494 O
ATOM 2362 CB GLU A 228 13.079 211.392 17.176 1.00 71.63 C
ANISOU 2362 CB GLU A 228 9207 8727 9283 658 -480 1430 C
ATOM 2363 CG GLU A 228 14.239 212.078 17.878 1.00 83.24 C
ANISOU 2363 CG GLU A 228 10714 10161 10754 708 -397 1359 C
ATOM 2364 CD GLU A 228 13.849 212.646 19.228 1.00 97.07 C
ANISOU 2364 CD GLU A 228 12404 11900 12578 790 -356 1280 C
ATOM 2365 OE1 GLU A 228 13.069 213.622 19.262 1.00104.63 O
ANISOU 2365 OE1 GLU A 228 13360 12848 13545 805 -397 1302 O
ATOM 2366 OE2 GLU A 228 14.316 212.110 20.256 1.00 97.95 O
ANISOU 2366 OE2 GLU A 228 12472 12014 12729 833 -285 1193 O
ATOM 2367 N VAL A 229 11.438 209.731 14.901 1.00 67.16 N
ANISOU 2367 N VAL A 229 8619 8244 8656 469 -671 1588 N
ATOM 2368 CA VAL A 229 10.591 208.614 14.493 1.00 60.43 C
ANISOU 2368 CA VAL A 229 7713 7433 7816 418 -731 1624 C
ATOM 2369 C VAL A 229 11.314 207.751 13.468 1.00 67.11 C
ANISOU 2369 C VAL A 229 8622 8300 8576 295 -776 1644 C
ATOM 2370 O VAL A 229 11.263 206.516 13.528 1.00 79.93 O
ANISOU 2370 O VAL A 229 10213 9950 10207 263 -779 1622 O
ATOM 2371 CB VAL A 229 9.248 209.127 13.942 1.00 60.88 C
ANISOU 2371 CB VAL A 229 7742 7507 7885 407 -805 1684 C
ATOM 2372 CG1 VAL A 229 8.364 207.959 13.526 1.00 55.67 C
ANISOU 2372 CG1 VAL A 229 7022 6888 7240 352 -866 1720 C
ATOM 2373 CG2 VAL A 229 8.545 209.986 14.969 1.00 63.57 C
ANISOU 2373 CG2 VAL A 229 8033 7829 8293 515 -765 1656 C
ATOM 2374 N HIS A 230 11.998 208.387 12.513 1.00 70.87 N
ANISOU 2374 N HIS A 230 9200 8769 8959 213 -801 1653 N
ATOM 2375 CA HIS A 230 12.719 207.640 11.488 1.00 73.57 C
ANISOU 2375 CA HIS A 230 9618 9140 9193 78 -806 1573 C
ATOM 2376 C HIS A 230 13.829 206.796 12.100 1.00 68.32 C
ANISOU 2376 C HIS A 230 8965 8480 8513 83 -702 1432 C
ATOM 2377 O HIS A 230 14.019 205.635 11.718 1.00 63.43 O
ANISOU 2377 O HIS A 230 8353 7895 7854 9 -705 1371 O
ATOM 2378 CB HIS A 230 13.287 208.603 10.444 1.00 89.86 C
ANISOU 2378 CB HIS A 230 11792 11193 11159 -3 -831 1580 C
ATOM 2379 CG HIS A 230 13.807 207.926 9.214 1.00107.08 C
ANISOU 2379 CG HIS A 230 14050 13410 13227 -149 -859 1524 C
ATOM 2380 ND1 HIS A 230 15.105 207.475 9.104 1.00112.86 N
ANISOU 2380 ND1 HIS A 230 14846 14150 13885 -205 -783 1393 N
ATOM 2381 CD2 HIS A 230 13.205 207.630 8.038 1.00113.60 C
ANISOU 2381 CD2 HIS A 230 14898 14265 13999 -248 -956 1579 C
ATOM 2382 CE1 HIS A 230 15.279 206.927 7.915 1.00116.04 C
ANISOU 2382 CE1 HIS A 230 15308 14588 14195 -333 -832 1371 C
ATOM 2383 NE2 HIS A 230 14.142 207.009 7.248 1.00115.24 N
ANISOU 2383 NE2 HIS A 230 15184 14499 14105 -362 -937 1483 N
ATOM 2384 N ALA A 231 14.575 207.361 13.053 1.00 59.18 N
ANISOU 2384 N ALA A 231 7810 7290 7386 172 -611 1377 N
ATOM 2385 CA ALA A 231 15.603 206.584 13.735 1.00 54.67 C
ANISOU 2385 CA ALA A 231 7243 6721 6806 192 -510 1242 C
ATOM 2386 C ALA A 231 14.995 205.481 14.590 1.00 56.08 C
ANISOU 2386 C ALA A 231 7328 6913 7068 254 -496 1237 C
ATOM 2387 O ALA A 231 15.637 204.448 14.812 1.00 54.64 O
ANISOU 2387 O ALA A 231 7153 6747 6861 234 -442 1131 O
ATOM 2388 CB ALA A 231 16.475 207.496 14.598 1.00 48.22 C
ANISOU 2388 CB ALA A 231 6446 5866 6011 281 -418 1189 C
ATOM 2389 N ALA A 232 13.767 205.676 15.078 1.00 58.56 N
ANISOU 2389 N ALA A 232 7554 7219 7478 330 -544 1348 N
ATOM 2390 CA ALA A 232 13.148 204.658 15.919 1.00 61.41 C
ANISOU 2390 CA ALA A 232 7824 7590 7920 390 -529 1348 C
ATOM 2391 C ALA A 232 12.675 203.470 15.090 1.00 67.88 C
ANISOU 2391 C ALA A 232 8640 8452 8700 283 -593 1350 C
ATOM 2392 O ALA A 232 12.785 202.319 15.528 1.00 55.86 O
ANISOU 2392 O ALA A 232 7089 6943 7193 286 -556 1286 O
ATOM 2393 CB ALA A 232 11.990 205.262 16.713 1.00 48.47 C
ANISOU 2393 CB ALA A 232 6089 5932 6395 505 -558 1464 C
ATOM 2394 N LYS A 233 12.146 203.727 13.889 1.00 62.68 N
ANISOU 2394 N LYS A 233 8013 7814 7989 188 -689 1423 N
ATOM 2395 CA LYS A 233 11.743 202.629 13.013 1.00 55.73 C
ANISOU 2395 CA LYS A 233 7136 6974 7064 80 -753 1423 C
ATOM 2396 C LYS A 233 12.950 201.822 12.551 1.00 54.37 C
ANISOU 2396 C LYS A 233 7044 6820 6795 -8 -705 1290 C
ATOM 2397 O LYS A 233 12.869 200.595 12.426 1.00 61.75 O
ANISOU 2397 O LYS A 233 7965 7781 7716 -56 -711 1246 O
ATOM 2398 CB LYS A 233 10.963 203.165 11.813 1.00 58.43 C
ANISOU 2398 CB LYS A 233 7498 7333 7368 2 -866 1528 C
ATOM 2399 CG LYS A 233 9.529 203.553 12.130 1.00 73.99 C
ANISOU 2399 CG LYS A 233 9376 9303 9434 70 -934 1660 C
ATOM 2400 CD LYS A 233 8.800 204.023 10.883 1.00 84.35 C
ANISOU 2400 CD LYS A 233 10715 10635 10700 -11 -1048 1755 C
ATOM 2401 CE LYS A 233 7.390 204.487 11.207 1.00 86.62 C
ANISOU 2401 CE LYS A 233 10912 10926 11075 61 -1074 1811 C
ATOM 2402 NZ LYS A 233 6.691 205.038 10.012 1.00 90.14 N
ANISOU 2402 NZ LYS A 233 11385 11389 11476 -7 -1161 1868 N
ATOM 2403 N SER A 234 14.070 202.481 12.343 1.00 47.75 N
ANISOU 2403 N SER A 234 6286 5967 5889 -26 -655 1223 N
ATOM 2404 CA SER A 234 15.252 201.772 11.925 1.00 42.35 C
ANISOU 2404 CA SER A 234 5677 5302 5110 -106 -607 1092 C
ATOM 2405 C SER A 234 15.684 200.795 12.996 1.00 53.58 C
ANISOU 2405 C SER A 234 7063 6723 6573 -39 -522 996 C
ATOM 2406 O SER A 234 16.035 199.672 12.702 1.00 63.96 O
ANISOU 2406 O SER A 234 8398 8064 7838 -103 -516 920 O
ATOM 2407 CB SER A 234 16.369 202.744 11.617 1.00 36.61 C
ANISOU 2407 CB SER A 234 5039 4561 4312 -127 -562 1038 C
ATOM 2408 OG SER A 234 16.039 203.512 10.495 1.00 49.12 O
ANISOU 2408 OG SER A 234 6672 6149 5843 -205 -642 1117 O
ATOM 2409 N ALA A 235 15.673 201.233 14.244 1.00 42.49 N
ANISOU 2409 N ALA A 235 5604 5285 5255 90 -458 998 N
ATOM 2410 CA ALA A 235 16.051 200.385 15.349 1.00 42.02 C
ANISOU 2410 CA ALA A 235 5508 5219 5241 167 -375 911 C
ATOM 2411 C ALA A 235 15.097 199.222 15.498 1.00 48.67 C
ANISOU 2411 C ALA A 235 6283 6080 6130 160 -415 947 C
ATOM 2412 O ALA A 235 15.503 198.118 15.770 1.00 41.16 O
ANISOU 2412 O ALA A 235 5337 5141 5163 150 -375 858 O
ATOM 2413 CB ALA A 235 16.113 201.192 16.620 1.00 26.03 C
ANISOU 2413 CB ALA A 235 3434 3153 3303 310 -306 922 C
ATOM 2414 N ALA A 236 13.816 199.497 15.315 1.00 44.30 N
ANISOU 2414 N ALA A 236 5668 5529 5636 165 -496 1077 N
ATOM 2415 CA ALA A 236 12.753 198.512 15.417 1.00 47.19 C
ANISOU 2415 CA ALA A 236 5963 5914 6054 157 -544 1128 C
ATOM 2416 C ALA A 236 12.867 197.446 14.367 1.00 58.77 C
ANISOU 2416 C ALA A 236 7476 7418 7435 25 -591 1086 C
ATOM 2417 O ALA A 236 12.505 196.311 14.585 1.00 51.78 O
ANISOU 2417 O ALA A 236 6556 6546 6571 13 -594 1067 O
ATOM 2418 CB ALA A 236 11.402 199.176 15.347 1.00 39.44 C
ANISOU 2418 CB ALA A 236 4910 4931 5145 186 -624 1276 C
ATOM 2419 N ILE A 237 13.293 197.837 13.184 1.00 52.35 N
ANISOU 2419 N ILE A 237 6742 6622 6528 -77 -635 1081 N
ATOM 2420 CA ILE A 237 13.484 196.891 12.115 1.00 46.65 C
ANISOU 2420 CA ILE A 237 6071 5936 5717 -205 -681 1038 C
ATOM 2421 C ILE A 237 14.561 195.893 12.471 1.00 47.21 C
ANISOU 2421 C ILE A 237 6184 6013 5741 -213 -601 894 C
ATOM 2422 O ILE A 237 14.437 194.738 12.175 1.00 44.39 O
ANISOU 2422 O ILE A 237 5829 5680 5358 -272 -622 859 O
ATOM 2423 CB ILE A 237 13.859 197.597 10.824 1.00 39.53 C
ANISOU 2423 CB ILE A 237 5252 5049 4718 -306 -734 1052 C
ATOM 2424 CG1 ILE A 237 12.637 198.251 10.233 1.00 44.91 C
ANISOU 2424 CG1 ILE A 237 5895 5735 5432 -324 -835 1195 C
ATOM 2425 CG2 ILE A 237 14.383 196.609 9.824 1.00 40.29 C
ANISOU 2425 CG2 ILE A 237 5414 5182 4710 -432 -759 976 C
ATOM 2426 CD1 ILE A 237 12.952 199.086 9.027 1.00 49.15 C
ANISOU 2426 CD1 ILE A 237 6515 6280 5879 -411 -887 1219 C
ATOM 2427 N ILE A 238 15.635 196.345 13.093 1.00 38.51 N
ANISOU 2427 N ILE A 238 5116 4890 4625 -153 -510 807 N
ATOM 2428 CA ILE A 238 16.698 195.457 13.492 1.00 46.63 C
ANISOU 2428 CA ILE A 238 6185 5924 5610 -149 -431 665 C
ATOM 2429 C ILE A 238 16.200 194.462 14.507 1.00 42.49 C
ANISOU 2429 C ILE A 238 5591 5390 5164 -76 -400 654 C
ATOM 2430 O ILE A 238 16.542 193.305 14.461 1.00 66.23 O
ANISOU 2430 O ILE A 238 8621 8413 8132 -114 -384 573 O
ATOM 2431 CB ILE A 238 17.839 196.228 14.140 1.00 45.00 C
ANISOU 2431 CB ILE A 238 6013 5693 5391 -77 -336 582 C
ATOM 2432 CG1 ILE A 238 18.394 197.255 13.180 1.00 37.78 C
ANISOU 2432 CG1 ILE A 238 5172 4786 4398 -148 -358 588 C
ATOM 2433 CG2 ILE A 238 18.946 195.285 14.544 1.00 54.49 C
ANISOU 2433 CG2 ILE A 238 7257 6905 6544 -70 -255 430 C
ATOM 2434 CD1 ILE A 238 18.884 196.656 11.898 1.00 42.14 C
ANISOU 2434 CD1 ILE A 238 5802 5378 4832 -289 -401 535 C
ATOM 2435 N ALA A 239 15.413 194.929 15.452 1.00 34.68 N
ANISOU 2435 N ALA A 239 4519 4372 4284 31 -389 734 N
ATOM 2436 CA ALA A 239 14.864 194.062 16.462 1.00 44.75 C
ANISOU 2436 CA ALA A 239 5725 5637 5641 104 -359 734 C
ATOM 2437 C ALA A 239 13.917 193.055 15.858 1.00 45.38 C
ANISOU 2437 C ALA A 239 5777 5743 5721 22 -439 786 C
ATOM 2438 O ALA A 239 13.923 191.914 16.229 1.00 39.89 O
ANISOU 2438 O ALA A 239 5074 5052 5031 22 -415 732 O
ATOM 2439 CB ALA A 239 14.165 194.879 17.519 1.00 46.23 C
ANISOU 2439 CB ALA A 239 5828 5791 5945 232 -338 819 C
ATOM 2440 N GLY A 240 13.083 193.490 14.934 1.00 41.68 N
ANISOU 2440 N GLY A 240 5296 5294 5247 -47 -535 892 N
ATOM 2441 CA GLY A 240 12.137 192.605 14.305 1.00 36.26 C
ANISOU 2441 CA GLY A 240 4580 4635 4561 -129 -616 946 C
ATOM 2442 C GLY A 240 12.820 191.569 13.468 1.00 49.03 C
ANISOU 2442 C GLY A 240 6274 6280 6074 -240 -627 852 C
ATOM 2443 O GLY A 240 12.369 190.454 13.369 1.00 54.46 O
ANISOU 2443 O GLY A 240 6943 6983 6764 -283 -653 845 O
ATOM 2444 N LEU A 241 13.896 191.959 12.820 1.00 35.39 N
ANISOU 2444 N LEU A 241 4633 4561 4252 -291 -610 780 N
ATOM 2445 CA LEU A 241 14.657 191.043 12.006 1.00 38.37 C
ANISOU 2445 CA LEU A 241 5089 4968 4522 -395 -617 683 C
ATOM 2446 C LEU A 241 15.289 189.952 12.837 1.00 48.47 C
ANISOU 2446 C LEU A 241 6378 6238 5799 -352 -538 567 C
ATOM 2447 O LEU A 241 15.374 188.822 12.420 1.00 44.79 O
ANISOU 2447 O LEU A 241 5940 5794 5284 -422 -559 516 O
ATOM 2448 CB LEU A 241 15.706 191.779 11.205 1.00 31.73 C
ANISOU 2448 CB LEU A 241 4336 4138 3582 -452 -609 629 C
ATOM 2449 CG LEU A 241 15.205 192.514 9.979 1.00 40.00 C
ANISOU 2449 CG LEU A 241 5404 5204 4590 -541 -704 723 C
ATOM 2450 CD1 LEU A 241 16.368 193.200 9.312 1.00 39.88 C
ANISOU 2450 CD1 LEU A 241 5480 5196 4475 -591 -680 656 C
ATOM 2451 CD2 LEU A 241 14.552 191.546 9.026 1.00 47.31 C
ANISOU 2451 CD2 LEU A 241 6331 6164 5480 -649 -792 753 C
ATOM 2452 N PHE A 242 15.758 190.301 14.020 1.00 44.48 N
ANISOU 2452 N PHE A 242 5853 5701 5346 -234 -448 523 N
ATOM 2453 CA PHE A 242 16.367 189.336 14.897 1.00 41.08 C
ANISOU 2453 CA PHE A 242 5432 5259 4917 -179 -368 413 C
ATOM 2454 C PHE A 242 15.349 188.303 15.277 1.00 44.31 C
ANISOU 2454 C PHE A 242 5780 5666 5389 -173 -395 459 C
ATOM 2455 O PHE A 242 15.618 187.127 15.237 1.00 43.79 O
ANISOU 2455 O PHE A 242 5744 5610 5283 -209 -385 384 O
ATOM 2456 CB PHE A 242 16.861 190.047 16.147 1.00 33.29 C
ANISOU 2456 CB PHE A 242 4422 4236 3991 -42 -273 380 C
ATOM 2457 CG PHE A 242 17.391 189.137 17.209 1.00 30.70 C
ANISOU 2457 CG PHE A 242 4094 3890 3680 36 -187 275 C
ATOM 2458 CD1 PHE A 242 16.550 188.548 18.096 1.00 35.67 C
ANISOU 2458 CD1 PHE A 242 4653 4500 4400 103 -176 318 C
ATOM 2459 CD2 PHE A 242 18.729 188.924 17.342 1.00 27.70 C
ANISOU 2459 CD2 PHE A 242 3785 3514 3225 45 -116 134 C
ATOM 2460 CE1 PHE A 242 17.028 187.733 19.079 1.00 39.45 C
ANISOU 2460 CE1 PHE A 242 5137 4960 4893 177 -97 224 C
ATOM 2461 CE2 PHE A 242 19.216 188.106 18.318 1.00 28.48 C
ANISOU 2461 CE2 PHE A 242 3888 3597 3337 122 -39 37 C
ATOM 2462 CZ PHE A 242 18.363 187.512 19.192 1.00 33.40 C
ANISOU 2462 CZ PHE A 242 4444 4196 4050 189 -29 83 C
ATOM 2463 N ALA A 243 14.156 188.750 15.620 1.00 41.81 N
ANISOU 2463 N ALA A 243 5378 5338 5171 -130 -433 584 N
ATOM 2464 CA ALA A 243 13.105 187.844 15.992 1.00 36.52 C
ANISOU 2464 CA ALA A 243 4643 4667 4567 -125 -460 636 C
ATOM 2465 C ALA A 243 12.727 186.960 14.828 1.00 49.54 C
ANISOU 2465 C ALA A 243 6319 6351 6152 -260 -545 647 C
ATOM 2466 O ALA A 243 12.604 185.774 14.968 1.00 41.26 O
ANISOU 2466 O ALA A 243 5274 5307 5097 -285 -542 606 O
ATOM 2467 CB ALA A 243 11.914 188.621 16.493 1.00 21.13 C
ANISOU 2467 CB ALA A 243 2595 2704 2729 -57 -489 770 C
ATOM 2468 N LEU A 244 12.626 187.528 13.644 1.00 51.30 N
ANISOU 2468 N LEU A 244 6571 6600 6319 -350 -620 695 N
ATOM 2469 CA LEU A 244 12.268 186.755 12.478 1.00 45.84 C
ANISOU 2469 CA LEU A 244 5907 5944 5565 -479 -706 707 C
ATOM 2470 C LEU A 244 13.299 185.689 12.190 1.00 53.97 C
ANISOU 2470 C LEU A 244 7020 6987 6499 -536 -674 573 C
ATOM 2471 O LEU A 244 12.974 184.598 11.790 1.00 44.91 O
ANISOU 2471 O LEU A 244 5881 5857 5327 -606 -713 561 O
ATOM 2472 CB LEU A 244 12.194 187.676 11.284 1.00 56.73 C
ANISOU 2472 CB LEU A 244 7317 7347 6892 -557 -780 768 C
ATOM 2473 CG LEU A 244 11.209 187.275 10.207 1.00 70.15 C
ANISOU 2473 CG LEU A 244 8998 9079 8576 -664 -891 849 C
ATOM 2474 CD1 LEU A 244 9.846 187.777 10.632 1.00 71.82 C
ANISOU 2474 CD1 LEU A 244 9107 9284 8899 -609 -933 983 C
ATOM 2475 CD2 LEU A 244 11.626 187.901 8.893 1.00 60.93 C
ANISOU 2475 CD2 LEU A 244 7900 7936 7313 -758 -949 855 C
ATOM 2476 N CYS A 245 14.559 186.044 12.315 1.00 51.14 N
ANISOU 2476 N CYS A 245 6728 6623 6081 -511 -607 473 N
ATOM 2477 CA CYS A 245 15.642 185.112 12.104 1.00 42.15 C
ANISOU 2477 CA CYS A 245 5671 5498 4848 -553 -569 335 C
ATOM 2478 C CYS A 245 15.813 184.059 13.179 1.00 50.54 C
ANISOU 2478 C CYS A 245 6722 6537 5942 -483 -501 260 C
ATOM 2479 O CYS A 245 16.392 183.038 12.927 1.00 47.90 O
ANISOU 2479 O CYS A 245 6446 6216 5536 -531 -492 165 O
ATOM 2480 CB CYS A 245 16.945 185.850 11.889 1.00 45.26 C
ANISOU 2480 CB CYS A 245 6136 5896 5164 -549 -519 248 C
ATOM 2481 SG CYS A 245 17.014 186.795 10.370 1.00 56.86 S
ANISOU 2481 SG CYS A 245 7652 7398 6555 -663 -601 303 S
ATOM 2482 N TRP A 246 15.370 184.327 14.394 1.00 49.42 N
ANISOU 2482 N TRP A 246 6511 6360 5904 -367 -449 297 N
ATOM 2483 CA TRP A 246 15.568 183.372 15.472 1.00 40.40 C
ANISOU 2483 CA TRP A 246 5364 5194 4794 -293 -377 224 C
ATOM 2484 C TRP A 246 14.362 182.572 15.896 1.00 45.89 C
ANISOU 2484 C TRP A 246 5990 5878 5568 -287 -407 297 C
ATOM 2485 O TRP A 246 14.505 181.575 16.555 1.00 50.09 O
ANISOU 2485 O TRP A 246 6532 6394 6107 -254 -362 234 O
ATOM 2486 CB TRP A 246 16.156 184.071 16.691 1.00 40.59 C
ANISOU 2486 CB TRP A 246 5371 5183 4869 -155 -278 183 C
ATOM 2487 CG TRP A 246 17.606 184.321 16.610 1.00 46.96 C
ANISOU 2487 CG TRP A 246 6257 5996 5589 -146 -217 55 C
ATOM 2488 CD1 TRP A 246 18.206 185.422 16.132 1.00 46.67 C
ANISOU 2488 CD1 TRP A 246 6250 5970 5512 -159 -216 51 C
ATOM 2489 CD2 TRP A 246 18.645 183.449 17.024 1.00 39.92 C
ANISOU 2489 CD2 TRP A 246 5428 5102 4638 -120 -149 -89 C
ATOM 2490 NE1 TRP A 246 19.553 185.307 16.228 1.00 43.31 N
ANISOU 2490 NE1 TRP A 246 5898 5551 5009 -145 -149 -87 N
ATOM 2491 CE2 TRP A 246 19.848 184.093 16.767 1.00 27.88 C
ANISOU 2491 CE2 TRP A 246 3964 3590 3039 -120 -108 -177 C
ATOM 2492 CE3 TRP A 246 18.672 182.183 17.589 1.00 35.96 C
ANISOU 2492 CE3 TRP A 246 4939 4589 4137 -97 -119 -154 C
ATOM 2493 CZ2 TRP A 246 21.052 183.522 17.044 1.00 23.05 C
ANISOU 2493 CZ2 TRP A 246 3420 2984 2356 -96 -41 -327 C
ATOM 2494 CZ3 TRP A 246 19.857 181.627 17.861 1.00 30.07 C
ANISOU 2494 CZ3 TRP A 246 4263 3844 3319 -72 -53 -300 C
ATOM 2495 CH2 TRP A 246 21.036 182.290 17.594 1.00 33.01 C
ANISOU 2495 CH2 TRP A 246 4690 4232 3618 -70 -15 -387 C
ATOM 2496 N LEU A 247 13.175 183.014 15.543 1.00 45.23 N
ANISOU 2496 N LEU A 247 5838 5804 5545 -315 -480 430 N
ATOM 2497 CA LEU A 247 11.958 182.301 15.927 1.00 52.64 C
ANISOU 2497 CA LEU A 247 6703 6736 6563 -314 -511 506 C
ATOM 2498 C LEU A 247 11.863 180.899 15.336 1.00 43.95 C
ANISOU 2498 C LEU A 247 5643 5652 5403 -413 -551 461 C
ATOM 2499 O LEU A 247 11.512 179.969 16.082 1.00 39.56 O
ANISOU 2499 O LEU A 247 5064 5077 4889 -381 -520 445 O
ATOM 2500 CB LEU A 247 10.727 183.135 15.563 1.00 43.32 C
ANISOU 2500 CB LEU A 247 5441 5568 5451 -329 -588 655 C
ATOM 2501 CG LEU A 247 10.327 184.201 16.583 1.00 55.24 C
ANISOU 2501 CG LEU A 247 6875 7050 7064 -204 -546 723 C
ATOM 2502 CD1 LEU A 247 9.070 184.921 16.125 1.00 65.83 C
ANISOU 2502 CD1 LEU A 247 8138 8409 8463 -228 -633 868 C
ATOM 2503 CD2 LEU A 247 10.136 183.586 17.962 1.00 51.12 C
ANISOU 2503 CD2 LEU A 247 6308 6494 6620 -102 -470 699 C
ATOM 2504 N PRO A 248 12.186 180.688 14.074 1.00 34.72 N
ANISOU 2504 N PRO A 248 4536 4519 4138 -530 -614 438 N
ATOM 2505 CA PRO A 248 12.074 179.357 13.485 1.00 34.06 C
ANISOU 2505 CA PRO A 248 4491 4452 3998 -626 -656 398 C
ATOM 2506 C PRO A 248 12.815 178.280 14.248 1.00 32.72 C
ANISOU 2506 C PRO A 248 4371 4259 3801 -583 -579 276 C
ATOM 2507 O PRO A 248 12.258 177.253 14.519 1.00 29.75 O
ANISOU 2507 O PRO A 248 3980 3874 3450 -599 -587 280 O
ATOM 2508 CB PRO A 248 12.663 179.558 12.113 1.00 31.79 C
ANISOU 2508 CB PRO A 248 4276 4202 3601 -735 -714 369 C
ATOM 2509 CG PRO A 248 12.260 180.925 11.776 1.00 28.12 C
ANISOU 2509 CG PRO A 248 3769 3745 3170 -725 -750 468 C
ATOM 2510 CD PRO A 248 12.293 181.714 13.039 1.00 33.86 C
ANISOU 2510 CD PRO A 248 4445 4436 3985 -589 -671 484 C
ATOM 2511 N LEU A 249 14.041 178.555 14.638 1.00 42.15 N
ANISOU 2511 N LEU A 249 5623 5443 4949 -524 -503 171 N
ATOM 2512 CA LEU A 249 14.839 177.616 15.419 1.00 34.57 C
ANISOU 2512 CA LEU A 249 4715 4461 3960 -470 -424 47 C
ATOM 2513 C LEU A 249 14.206 177.363 16.783 1.00 32.21 C
ANISOU 2513 C LEU A 249 4349 4120 3770 -362 -367 79 C
ATOM 2514 O LEU A 249 14.101 176.214 17.228 1.00 44.64 O
ANISOU 2514 O LEU A 249 5940 5677 5345 -357 -346 35 O
ATOM 2515 CB LEU A 249 16.263 178.150 15.565 1.00 40.46 C
ANISOU 2515 CB LEU A 249 5527 5207 4638 -421 -355 -67 C
ATOM 2516 CG LEU A 249 17.332 177.244 16.173 1.00 37.52 C
ANISOU 2516 CG LEU A 249 5226 4821 4208 -373 -277 -217 C
ATOM 2517 CD1 LEU A 249 17.089 175.777 15.850 1.00 36.17 C
ANISOU 2517 CD1 LEU A 249 5093 4655 3994 -446 -313 -253 C
ATOM 2518 CD2 LEU A 249 18.665 177.679 15.620 1.00 45.97 C
ANISOU 2518 CD2 LEU A 249 6375 5917 5175 -394 -254 -322 C
ATOM 2519 N HIS A 250 13.768 178.427 17.459 1.00 37.75 N
ANISOU 2519 N HIS A 250 4976 4803 4563 -274 -342 158 N
ATOM 2520 CA HIS A 250 13.137 178.261 18.763 1.00 33.34 C
ANISOU 2520 CA HIS A 250 4350 4207 4112 -168 -287 194 C
ATOM 2521 C HIS A 250 11.807 177.525 18.659 1.00 51.29 C
ANISOU 2521 C HIS A 250 6563 6483 6442 -223 -348 287 C
ATOM 2522 O HIS A 250 11.451 176.761 19.564 1.00 41.43 O
ANISOU 2522 O HIS A 250 5292 5205 5244 -172 -305 278 O
ATOM 2523 CB HIS A 250 12.941 179.622 19.427 1.00 36.16 C
ANISOU 2523 CB HIS A 250 4639 4547 4552 -67 -255 262 C
ATOM 2524 CG HIS A 250 14.209 180.230 19.940 1.00 45.86 C
ANISOU 2524 CG HIS A 250 5915 5761 5748 18 -171 163 C
ATOM 2525 ND1 HIS A 250 14.882 179.731 21.034 1.00 48.47 N
ANISOU 2525 ND1 HIS A 250 6271 6060 6085 117 -77 65 N
ATOM 2526 CD2 HIS A 250 14.923 181.298 19.514 1.00 36.67 C
ANISOU 2526 CD2 HIS A 250 4778 4611 4544 20 -166 146 C
ATOM 2527 CE1 HIS A 250 15.958 180.463 21.259 1.00 33.76 C
ANISOU 2527 CE1 HIS A 250 4446 4193 4189 176 -19 -11 C
ATOM 2528 NE2 HIS A 250 16.006 181.421 20.350 1.00 31.15 N
ANISOU 2528 NE2 HIS A 250 4117 3889 3829 116 -70 37 N
ATOM 2529 N ILE A 251 11.065 177.738 17.571 1.00 47.13 N
ANISOU 2529 N ILE A 251 6011 5991 5906 -327 -446 375 N
ATOM 2530 CA ILE A 251 9.778 177.068 17.415 1.00 50.32 C
ANISOU 2530 CA ILE A 251 6355 6402 6362 -384 -507 464 C
ATOM 2531 C ILE A 251 9.977 175.575 17.180 1.00 52.87 C
ANISOU 2531 C ILE A 251 6741 6724 6622 -454 -513 386 C
ATOM 2532 O ILE A 251 9.192 174.749 17.661 1.00 61.36 O
ANISOU 2532 O ILE A 251 7778 7784 7750 -456 -513 416 O
ATOM 2533 CB ILE A 251 8.968 177.727 16.282 1.00 41.11 C
ANISOU 2533 CB ILE A 251 5146 5275 5197 -474 -612 574 C
ATOM 2534 CG1 ILE A 251 8.539 179.138 16.685 1.00 42.40 C
ANISOU 2534 CG1 ILE A 251 5235 5434 5442 -393 -607 666 C
ATOM 2535 CG2 ILE A 251 7.743 176.894 15.931 1.00 44.24 C
ANISOU 2535 CG2 ILE A 251 5493 5687 5629 -554 -683 649 C
ATOM 2536 CD1 ILE A 251 7.788 179.877 15.596 1.00 53.06 C
ANISOU 2536 CD1 ILE A 251 6549 6821 6791 -471 -708 773 C
ATOM 2537 N ILE A 252 11.032 175.202 16.452 1.00 39.31 N
ANISOU 2537 N ILE A 252 5122 5023 4791 -513 -518 283 N
ATOM 2538 CA ILE A 252 11.322 173.785 16.241 1.00 41.74 C
ANISOU 2538 CA ILE A 252 5499 5329 5032 -574 -521 200 C
ATOM 2539 C ILE A 252 11.667 173.110 17.562 1.00 30.63 C
ANISOU 2539 C ILE A 252 4106 3876 3655 -471 -425 126 C
ATOM 2540 O ILE A 252 11.240 171.979 17.828 1.00 43.66 O
ANISOU 2540 O ILE A 252 5764 5510 5314 -494 -426 114 O
ATOM 2541 CB ILE A 252 12.449 173.613 15.205 1.00 37.84 C
ANISOU 2541 CB ILE A 252 5106 4864 4406 -650 -544 101 C
ATOM 2542 CG1 ILE A 252 11.999 174.123 13.834 1.00 30.45 C
ANISOU 2542 CG1 ILE A 252 4159 3974 3439 -764 -647 178 C
ATOM 2543 CG2 ILE A 252 12.866 172.155 15.108 1.00 26.29 C
ANISOU 2543 CG2 ILE A 252 3722 3396 2872 -697 -538 1 C
ATOM 2544 CD1 ILE A 252 13.073 174.046 12.775 1.00 22.30 C
ANISOU 2544 CD1 ILE A 252 3223 2973 2278 -841 -671 89 C
ATOM 2545 N ASN A 253 12.440 173.791 18.413 1.00 30.54 N
ANISOU 2545 N ASN A 253 4101 3842 3660 -356 -341 74 N
ATOM 2546 CA ASN A 253 12.740 173.251 19.735 1.00 31.53 C
ANISOU 2546 CA ASN A 253 4236 3922 3821 -245 -247 9 C
ATOM 2547 C ASN A 253 11.467 173.018 20.538 1.00 34.24 C
ANISOU 2547 C ASN A 253 4489 4240 4280 -208 -243 109 C
ATOM 2548 O ASN A 253 11.369 172.042 21.291 1.00 50.21 O
ANISOU 2548 O ASN A 253 6528 6231 6319 -174 -199 69 O
ATOM 2549 CB ASN A 253 13.678 174.192 20.493 1.00 38.99 C
ANISOU 2549 CB ASN A 253 5189 4850 4775 -125 -162 -48 C
ATOM 2550 CG ASN A 253 15.084 174.190 19.933 1.00 43.31 C
ANISOU 2550 CG ASN A 253 5836 5417 5204 -147 -144 -176 C
ATOM 2551 OD1 ASN A 253 15.461 173.300 19.176 1.00 42.17 O
ANISOU 2551 OD1 ASN A 253 5764 5292 4968 -236 -180 -241 O
ATOM 2552 ND2 ASN A 253 15.873 175.187 20.315 1.00 42.18 N
ANISOU 2552 ND2 ASN A 253 5696 5270 5060 -66 -88 -215 N
ATOM 2553 N CYS A 254 10.479 173.904 20.391 1.00 39.53 N
ANISOU 2553 N CYS A 254 5066 4926 5030 -213 -289 238 N
ATOM 2554 CA CYS A 254 9.236 173.750 21.140 1.00 45.67 C
ANISOU 2554 CA CYS A 254 5749 5685 5918 -178 -288 336 C
ATOM 2555 C CYS A 254 8.466 172.514 20.690 1.00 48.98 C
ANISOU 2555 C CYS A 254 6172 6112 6326 -282 -343 358 C
ATOM 2556 O CYS A 254 7.910 171.790 21.522 1.00 52.77 O
ANISOU 2556 O CYS A 254 6626 6563 6863 -248 -308 370 O
ATOM 2557 CB CYS A 254 8.376 175.005 20.997 1.00 37.70 C
ANISOU 2557 CB CYS A 254 4640 4695 4988 -163 -331 466 C
ATOM 2558 SG CYS A 254 9.079 176.484 21.764 1.00 55.37 S
ANISOU 2558 SG CYS A 254 6857 6915 7264 -24 -259 457 S
ATOM 2559 N PHE A 255 8.423 172.255 19.380 1.00 51.25 N
ANISOU 2559 N PHE A 255 6494 6437 6540 -410 -430 364 N
ATOM 2560 CA PHE A 255 7.753 171.054 18.889 1.00 50.90 C
ANISOU 2560 CA PHE A 255 6460 6401 6479 -515 -485 377 C
ATOM 2561 C PHE A 255 8.402 169.793 19.442 1.00 52.91 C
ANISOU 2561 C PHE A 255 6798 6620 6684 -497 -425 263 C
ATOM 2562 O PHE A 255 7.709 168.858 19.859 1.00 63.88 O
ANISOU 2562 O PHE A 255 8172 7991 8111 -513 -421 281 O
ATOM 2563 CB PHE A 255 7.759 171.031 17.361 1.00 60.88 C
ANISOU 2563 CB PHE A 255 7757 7712 7662 -649 -585 390 C
ATOM 2564 CG PHE A 255 6.595 171.744 16.742 1.00 65.92 C
ANISOU 2564 CG PHE A 255 8302 8385 8359 -702 -669 525 C
ATOM 2565 CD1 PHE A 255 6.674 173.094 16.441 1.00 54.49 C
ANISOU 2565 CD1 PHE A 255 6820 6956 6926 -674 -687 577 C
ATOM 2566 CD2 PHE A 255 5.421 171.065 16.462 1.00 63.73 C
ANISOU 2566 CD2 PHE A 255 7972 8120 8121 -780 -730 599 C
ATOM 2567 CE1 PHE A 255 5.603 173.754 15.872 1.00 60.47 C
ANISOU 2567 CE1 PHE A 255 7495 7746 7735 -718 -766 700 C
ATOM 2568 CE2 PHE A 255 4.346 171.717 15.893 1.00 76.08 C
ANISOU 2568 CE2 PHE A 255 9450 9719 9738 -825 -809 720 C
ATOM 2569 CZ PHE A 255 4.437 173.065 15.597 1.00 73.71 C
ANISOU 2569 CZ PHE A 255 9118 9438 9450 -793 -828 770 C
ATOM 2570 N THR A 256 9.734 169.753 19.459 1.00 41.06 N
ANISOU 2570 N THR A 256 5390 5113 5100 -462 -377 142 N
ATOM 2571 CA THR A 256 10.434 168.579 19.967 1.00 49.11 C
ANISOU 2571 CA THR A 256 6497 6100 6064 -438 -320 24 C
ATOM 2572 C THR A 256 10.254 168.435 21.471 1.00 58.08 C
ANISOU 2572 C THR A 256 7601 7185 7283 -312 -228 20 C
ATOM 2573 O THR A 256 10.111 167.317 21.982 1.00 61.14 O
ANISOU 2573 O THR A 256 8022 7541 7668 -309 -200 -18 O
ATOM 2574 CB THR A 256 11.914 168.670 19.611 1.00 48.00 C
ANISOU 2574 CB THR A 256 6456 5969 5812 -426 -293 -105 C
ATOM 2575 OG1 THR A 256 12.046 168.702 18.187 1.00 52.64 O
ANISOU 2575 OG1 THR A 256 7077 6604 6319 -551 -380 -101 O
ATOM 2576 CG2 THR A 256 12.678 167.478 20.165 1.00 51.99 C
ANISOU 2576 CG2 THR A 256 7055 6441 6257 -393 -234 -233 C
ATOM 2577 N PHE A 257 10.252 169.553 22.196 1.00 52.16 N
ANISOU 2577 N PHE A 257 6788 6426 6606 -206 -180 59 N
ATOM 2578 CA PHE A 257 10.080 169.496 23.641 1.00 50.62 C
ANISOU 2578 CA PHE A 257 6558 6183 6492 -80 -92 59 C
ATOM 2579 C PHE A 257 8.628 169.224 24.018 1.00 51.18 C
ANISOU 2579 C PHE A 257 6535 6246 6664 -98 -116 176 C
ATOM 2580 O PHE A 257 8.350 168.377 24.874 1.00 58.16 O
ANISOU 2580 O PHE A 257 7426 7092 7581 -60 -67 159 O
ATOM 2581 CB PHE A 257 10.555 170.801 24.277 1.00 44.16 C
ANISOU 2581 CB PHE A 257 5701 5358 5718 39 -35 62 C
ATOM 2582 CG PHE A 257 10.487 170.803 25.778 1.00 51.02 C
ANISOU 2582 CG PHE A 257 6539 6179 6667 178 60 54 C
ATOM 2583 CD1 PHE A 257 11.351 170.017 26.524 1.00 34.63 C
ANISOU 2583 CD1 PHE A 257 4544 4066 4548 247 138 -67 C
ATOM 2584 CD2 PHE A 257 9.560 171.590 26.443 1.00 42.23 C
ANISOU 2584 CD2 PHE A 257 5316 5059 5670 243 70 165 C
ATOM 2585 CE1 PHE A 257 11.293 170.018 27.905 1.00 35.65 C
ANISOU 2585 CE1 PHE A 257 4646 4150 4749 377 225 -76 C
ATOM 2586 CE2 PHE A 257 9.498 171.598 27.824 1.00 42.57 C
ANISOU 2586 CE2 PHE A 257 5329 5059 5787 372 157 158 C
ATOM 2587 CZ PHE A 257 10.366 170.811 28.557 1.00 48.69 C
ANISOU 2587 CZ PHE A 257 6187 5795 6519 439 236 38 C
ATOM 2588 N PHE A 258 7.686 169.933 23.393 1.00 47.90 N
ANISOU 2588 N PHE A 258 6035 5867 6299 -156 -190 296 N
ATOM 2589 CA PHE A 258 6.304 169.843 23.844 1.00 47.79 C
ANISOU 2589 CA PHE A 258 5919 5849 6390 -158 -207 410 C
ATOM 2590 C PHE A 258 5.568 168.662 23.226 1.00 59.48 C
ANISOU 2590 C PHE A 258 7411 7340 7849 -283 -270 431 C
ATOM 2591 O PHE A 258 4.646 168.123 23.849 1.00 69.88 O
ANISOU 2591 O PHE A 258 8675 8639 9237 -278 -257 484 O
ATOM 2592 CB PHE A 258 5.570 171.145 23.537 1.00 47.78 C
ANISOU 2592 CB PHE A 258 5815 5882 6458 -153 -257 530 C
ATOM 2593 CG PHE A 258 5.939 172.282 24.449 1.00 57.22 C
ANISOU 2593 CG PHE A 258 6972 7059 7710 -14 -189 536 C
ATOM 2594 CD1 PHE A 258 6.007 172.102 25.826 1.00 55.04 C
ANISOU 2594 CD1 PHE A 258 6681 6737 7494 106 -95 511 C
ATOM 2595 CD2 PHE A 258 6.211 173.536 23.929 1.00 52.42 C
ANISOU 2595 CD2 PHE A 258 6344 6478 7095 -3 -218 568 C
ATOM 2596 CE1 PHE A 258 6.344 173.159 26.666 1.00 43.85 C
ANISOU 2596 CE1 PHE A 258 5228 5304 6131 236 -33 517 C
ATOM 2597 CE2 PHE A 258 6.549 174.594 24.754 1.00 48.68 C
ANISOU 2597 CE2 PHE A 258 5836 5986 6673 123 -157 575 C
ATOM 2598 CZ PHE A 258 6.616 174.408 26.126 1.00 44.33 C
ANISOU 2598 CZ PHE A 258 5268 5392 6184 244 -65 549 C
ATOM 2599 N CYS A 259 5.952 168.239 22.021 1.00 63.54 N
ANISOU 2599 N CYS A 259 7993 7884 8267 -396 -337 391 N
ATOM 2600 CA CYS A 259 5.288 167.139 21.323 1.00 68.87 C
ANISOU 2600 CA CYS A 259 8682 8572 8915 -523 -403 409 C
ATOM 2601 C CYS A 259 6.299 166.036 21.046 1.00 66.79 C
ANISOU 2601 C CYS A 259 8548 8291 8539 -561 -387 278 C
ATOM 2602 O CYS A 259 6.887 165.980 19.953 1.00 79.61 O
ANISOU 2602 O CYS A 259 10233 9945 10069 -640 -442 234 O
ATOM 2603 CB CYS A 259 4.643 167.619 20.027 1.00 76.30 C
ANISOU 2603 CB CYS A 259 9576 9567 9846 -635 -513 494 C
ATOM 2604 SG CYS A 259 3.714 166.325 19.188 1.00 98.41 S
ANISOU 2604 SG CYS A 259 12382 12387 12624 -790 -599 525 S
ATOM 2605 N PRO A 260 6.538 165.135 22.004 1.00 64.93 N
ANISOU 2605 N PRO A 260 8359 8007 8306 -504 -314 213 N
ATOM 2606 CA PRO A 260 7.403 163.981 21.723 1.00 63.98 C
ANISOU 2606 CA PRO A 260 8362 7870 8077 -545 -306 91 C
ATOM 2607 C PRO A 260 6.759 162.959 20.804 1.00 79.62 C
ANISOU 2607 C PRO A 260 10363 9868 10020 -688 -388 114 C
ATOM 2608 O PRO A 260 7.468 162.081 20.295 1.00 92.95 O
ANISOU 2608 O PRO A 260 12155 11554 11608 -742 -402 19 O
ATOM 2609 CB PRO A 260 7.664 163.392 23.113 1.00 64.69 C
ANISOU 2609 CB PRO A 260 8483 7900 8196 -434 -203 32 C
ATOM 2610 CG PRO A 260 6.454 163.754 23.893 1.00 69.62 C
ANISOU 2610 CG PRO A 260 8992 8513 8949 -394 -187 148 C
ATOM 2611 CD PRO A 260 6.020 165.112 23.383 1.00 74.47 C
ANISOU 2611 CD PRO A 260 9510 9172 9612 -400 -237 246 C
ATOM 2612 N ASP A 261 5.447 163.036 20.580 1.00 80.27 N
ANISOU 2612 N ASP A 261 10349 9970 10179 -751 -444 233 N
ATOM 2613 CA ASP A 261 4.782 162.154 19.631 1.00 74.51 C
ANISOU 2613 CA ASP A 261 9630 9263 9418 -892 -530 261 C
ATOM 2614 C ASP A 261 4.827 162.676 18.201 1.00 66.77 C
ANISOU 2614 C ASP A 261 8646 8341 8383 -991 -627 289 C
ATOM 2615 O ASP A 261 4.557 161.909 17.270 1.00 62.44 O
ANISOU 2615 O ASP A 261 8130 7813 7783 -1111 -700 288 O
ATOM 2616 CB ASP A 261 3.326 161.930 20.047 1.00 90.18 C
ANISOU 2616 CB ASP A 261 11512 11244 11508 -919 -545 372 C
ATOM 2617 CG ASP A 261 3.195 160.988 21.227 1.00 99.00 C
ANISOU 2617 CG ASP A 261 12655 12303 12657 -864 -465 337 C
ATOM 2618 OD1 ASP A 261 4.035 160.071 21.355 1.00101.44 O
ANISOU 2618 OD1 ASP A 261 13077 12579 12885 -860 -431 227 O
ATOM 2619 OD2 ASP A 261 2.249 161.163 22.023 1.00101.05 O
ANISOU 2619 OD2 ASP A 261 12823 12551 13020 -824 -437 418 O
ATOM 2620 N CYS A 262 5.147 163.953 18.003 1.00 72.52 N
ANISOU 2620 N CYS A 262 9337 9094 9122 -945 -631 316 N
ATOM 2621 CA CYS A 262 5.310 164.477 16.656 1.00 74.36 C
ANISOU 2621 CA CYS A 262 9579 9379 9296 -1033 -717 334 C
ATOM 2622 C CYS A 262 6.586 163.926 16.035 1.00 75.23 C
ANISOU 2622 C CYS A 262 9817 9493 9276 -1067 -718 208 C
ATOM 2623 O CYS A 262 7.578 163.676 16.723 1.00 74.34 O
ANISOU 2623 O CYS A 262 9775 9347 9124 -987 -640 105 O
ATOM 2624 CB CYS A 262 5.360 166.006 16.669 1.00 82.60 C
ANISOU 2624 CB CYS A 262 10557 10445 10383 -968 -715 393 C
ATOM 2625 SG CYS A 262 3.854 166.827 17.228 1.00 89.12 S
ANISOU 2625 SG CYS A 262 11228 11279 11356 -930 -728 549 S
ATOM 2626 N SER A 263 6.551 163.726 14.722 1.00 88.70 N
ANISOU 2626 N SER A 263 11550 11239 10912 -1187 -809 213 N
ATOM 2627 CA SER A 263 7.733 163.244 14.024 1.00 98.05 C
ANISOU 2627 CA SER A 263 12852 12434 11969 -1227 -819 97 C
ATOM 2628 C SER A 263 8.834 164.295 14.072 1.00 97.74 C
ANISOU 2628 C SER A 263 12840 12404 11894 -1152 -776 44 C
ATOM 2629 O SER A 263 8.566 165.499 14.060 1.00 91.56 O
ANISOU 2629 O SER A 263 11985 11638 11164 -1117 -782 118 O
ATOM 2630 CB SER A 263 7.394 162.889 12.577 1.00107.24 C
ANISOU 2630 CB SER A 263 14031 13643 13072 -1372 -930 123 C
ATOM 2631 OG SER A 263 6.480 161.807 12.525 1.00115.25 O
ANISOU 2631 OG SER A 263 15032 14647 14110 -1445 -967 157 O
ATOM 2632 N HIS A 264 10.077 163.825 14.144 1.00105.29 N
ANISOU 2632 N HIS A 264 13901 13349 12756 -1125 -732 -87 N
ATOM 2633 CA HIS A 264 11.233 164.706 14.232 1.00104.47 C
ANISOU 2633 CA HIS A 264 13834 13254 12608 -1054 -683 -156 C
ATOM 2634 C HIS A 264 11.271 165.671 13.052 1.00104.77 C
ANISOU 2634 C HIS A 264 13851 13343 12614 -1123 -756 -107 C
ATOM 2635 O HIS A 264 10.884 165.333 11.930 1.00115.77 O
ANISOU 2635 O HIS A 264 15253 14769 13964 -1240 -845 -75 O
ATOM 2636 CB HIS A 264 12.515 163.875 14.259 1.00117.97 C
ANISOU 2636 CB HIS A 264 15665 14952 14205 -1040 -643 -309 C
ATOM 2637 CG HIS A 264 13.696 164.593 14.830 1.00129.26 C
ANISOU 2637 CG HIS A 264 17128 16375 15608 -933 -562 -395 C
ATOM 2638 ND1 HIS A 264 14.035 164.519 16.163 1.00133.09 N
ANISOU 2638 ND1 HIS A 264 17618 16815 16136 -806 -463 -445 N
ATOM 2639 CD2 HIS A 264 14.625 165.388 14.248 1.00137.02 C
ANISOU 2639 CD2 HIS A 264 18143 17392 16525 -934 -564 -443 C
ATOM 2640 CE1 HIS A 264 15.120 165.239 16.379 1.00134.33 C
ANISOU 2640 CE1 HIS A 264 17806 16979 16255 -733 -409 -520 C
ATOM 2641 NE2 HIS A 264 15.498 165.778 15.234 1.00136.14 N
ANISOU 2641 NE2 HIS A 264 18053 17256 16419 -810 -467 -521 N
ATOM 2642 N ALA A 265 11.736 166.886 13.317 1.00 96.45 N
ANISOU 2642 N ALA A 265 12773 12294 11581 -1048 -716 -100 N
ATOM 2643 CA ALA A 265 11.922 167.856 12.245 1.00 86.29 C
ANISOU 2643 CA ALA A 265 11479 11052 10255 -1104 -775 -65 C
ATOM 2644 C ALA A 265 13.009 167.361 11.299 1.00 78.84 C
ANISOU 2644 C ALA A 265 10644 10137 9175 -1175 -800 -176 C
ATOM 2645 O ALA A 265 14.084 166.958 11.758 1.00 80.31 O
ANISOU 2645 O ALA A 265 10904 10308 9301 -1121 -734 -297 O
ATOM 2646 CB ALA A 265 12.294 169.223 12.811 1.00 85.88 C
ANISOU 2646 CB ALA A 265 11387 10994 10249 -1003 -718 -46 C
ATOM 2647 N PRO A 266 12.775 167.375 9.986 1.00 64.86 N
ANISOU 2647 N PRO A 266 8884 8410 7351 -1293 -894 -140 N
ATOM 2648 CA PRO A 266 13.753 166.798 9.057 1.00 54.57 C
ANISOU 2648 CA PRO A 266 7677 7133 5923 -1356 -916 -241 C
ATOM 2649 C PRO A 266 15.100 167.496 9.158 1.00 55.22 C
ANISOU 2649 C PRO A 266 7790 7217 5974 -1259 -827 -324 C
ATOM 2650 O PRO A 266 15.192 168.671 9.520 1.00 72.03 O
ANISOU 2650 O PRO A 266 9904 9353 8111 -1241 -826 -303 O
ATOM 2651 CB PRO A 266 13.110 167.011 7.682 1.00 58.54 C
ANISOU 2651 CB PRO A 266 8145 7673 6424 -1449 -1001 -151 C
ATOM 2652 CG PRO A 266 12.127 168.115 7.882 1.00 67.58 C
ANISOU 2652 CG PRO A 266 9203 8826 7647 -1461 -1051 -27 C
ATOM 2653 CD PRO A 266 11.624 167.968 9.285 1.00 66.01 C
ANISOU 2653 CD PRO A 266 8948 8581 7553 -1359 -979 -3 C
ATOM 2654 N LEU A 267 16.155 166.744 8.839 1.00 61.35 N
ANISOU 2654 N LEU A 267 8597 7987 6727 -1188 -753 -412 N
ATOM 2655 CA LEU A 267 17.511 167.251 9.018 1.00 61.87 C
ANISOU 2655 CA LEU A 267 8672 8052 6784 -1079 -665 -491 C
ATOM 2656 C LEU A 267 17.759 168.494 8.172 1.00 57.18 C
ANISOU 2656 C LEU A 267 8065 7490 6172 -1110 -689 -452 C
ATOM 2657 O LEU A 267 18.421 169.436 8.620 1.00 66.84 O
ANISOU 2657 O LEU A 267 9286 8712 7397 -1048 -641 -482 O
ATOM 2658 CB LEU A 267 18.523 166.158 8.677 1.00 72.00 C
ANISOU 2658 CB LEU A 267 9962 9330 8063 -1003 -610 -569 C
ATOM 2659 CG LEU A 267 19.964 166.407 9.125 1.00 60.26 C
ANISOU 2659 CG LEU A 267 8462 7840 6595 -864 -524 -651 C
ATOM 2660 CD1 LEU A 267 20.071 166.342 10.640 1.00 53.95 C
ANISOU 2660 CD1 LEU A 267 7662 7009 5827 -775 -464 -694 C
ATOM 2661 CD2 LEU A 267 20.921 165.422 8.469 1.00 58.16 C
ANISOU 2661 CD2 LEU A 267 8186 7583 6332 -804 -504 -701 C
ATOM 2662 N TRP A 268 17.233 168.516 6.944 1.00 54.41 N
ANISOU 2662 N TRP A 268 7705 7164 5805 -1203 -761 -386 N
ATOM 2663 CA TRP A 268 17.437 169.676 6.082 1.00 57.68 C
ANISOU 2663 CA TRP A 268 8111 7606 6201 -1236 -785 -345 C
ATOM 2664 C TRP A 268 16.769 170.917 6.661 1.00 63.02 C
ANISOU 2664 C TRP A 268 8765 8288 6892 -1266 -829 -276 C
ATOM 2665 O TRP A 268 17.309 172.025 6.561 1.00 56.25 O
ANISOU 2665 O TRP A 268 7909 7441 6023 -1243 -808 -279 O
ATOM 2666 CB TRP A 268 16.914 169.387 4.673 1.00 65.07 C
ANISOU 2666 CB TRP A 268 9041 8564 7118 -1326 -855 -284 C
ATOM 2667 CG TRP A 268 15.425 169.217 4.592 1.00 67.14 C
ANISOU 2667 CG TRP A 268 9274 8833 7403 -1422 -952 -183 C
ATOM 2668 CD1 TRP A 268 14.725 168.053 4.722 1.00 67.14 C
ANISOU 2668 CD1 TRP A 268 9271 8822 7419 -1455 -980 -171 C
ATOM 2669 CD2 TRP A 268 14.453 170.245 4.355 1.00 69.86 C
ANISOU 2669 CD2 TRP A 268 9577 9198 7769 -1492 -1038 -71 C
ATOM 2670 NE1 TRP A 268 13.379 168.292 4.585 1.00 71.83 N
ANISOU 2670 NE1 TRP A 268 9817 9428 8046 -1541 -1075 -61 N
ATOM 2671 CE2 TRP A 268 13.185 169.630 4.359 1.00 69.29 C
ANISOU 2671 CE2 TRP A 268 9467 9128 7734 -1560 -1114 6 C
ATOM 2672 CE3 TRP A 268 14.532 171.625 4.143 1.00 78.08 C
ANISOU 2672 CE3 TRP A 268 10604 10256 8806 -1499 -1058 -25 C
ATOM 2673 CZ2 TRP A 268 12.006 170.346 4.158 1.00 71.08 C
ANISOU 2673 CZ2 TRP A 268 9629 9374 8004 -1626 -1210 130 C
ATOM 2674 CZ3 TRP A 268 13.359 172.335 3.944 1.00 80.81 C
ANISOU 2674 CZ3 TRP A 268 10895 10621 9189 -1565 -1156 99 C
ATOM 2675 CH2 TRP A 268 12.114 171.694 3.953 1.00 75.32 C
ANISOU 2675 CH2 TRP A 268 10150 9929 8540 -1623 -1231 176 C
ATOM 2676 N LEU A 269 15.594 170.752 7.275 1.00 58.96 N
ANISOU 2676 N LEU A 269 8223 7768 6412 -1316 -894 -208 N
ATOM 2677 CA LEU A 269 14.912 171.892 7.876 1.00 60.93 C
ANISOU 2677 CA LEU A 269 8412 8015 6724 -1298 -918 -118 C
ATOM 2678 C LEU A 269 15.664 172.406 9.096 1.00 62.34 C
ANISOU 2678 C LEU A 269 8591 8161 6934 -1166 -808 -180 C
ATOM 2679 O LEU A 269 15.655 173.612 9.367 1.00 54.21 O
ANISOU 2679 O LEU A 269 7518 7126 5952 -1110 -783 -130 O
ATOM 2680 CB LEU A 269 13.480 171.515 8.253 1.00 51.08 C
ANISOU 2680 CB LEU A 269 7079 6749 5582 -1301 -954 -7 C
ATOM 2681 CG LEU A 269 12.609 172.667 8.752 1.00 49.39 C
ANISOU 2681 CG LEU A 269 6764 6521 5481 -1239 -950 116 C
ATOM 2682 CD1 LEU A 269 12.586 173.787 7.722 1.00 49.85 C
ANISOU 2682 CD1 LEU A 269 6817 6614 5511 -1292 -1011 178 C
ATOM 2683 CD2 LEU A 269 11.203 172.179 9.053 1.00 51.03 C
ANISOU 2683 CD2 LEU A 269 6890 6717 5783 -1252 -989 217 C
ATOM 2684 N MET A 270 16.325 171.509 9.831 1.00 57.37 N
ANISOU 2684 N MET A 270 8011 7509 6277 -1115 -742 -290 N
ATOM 2685 CA MET A 270 17.137 171.931 10.967 1.00 55.70 C
ANISOU 2685 CA MET A 270 7807 7268 6086 -988 -636 -363 C
ATOM 2686 C MET A 270 18.233 172.890 10.528 1.00 55.34 C
ANISOU 2686 C MET A 270 7806 7250 5972 -984 -613 -422 C
ATOM 2687 O MET A 270 18.359 173.998 11.064 1.00 53.46 O
ANISOU 2687 O MET A 270 7528 6999 5786 -907 -566 -393 O
ATOM 2688 CB MET A 270 17.743 170.712 11.664 1.00 56.61 C
ANISOU 2688 CB MET A 270 7985 7361 6164 -945 -578 -484 C
ATOM 2689 CG MET A 270 16.818 170.032 12.653 1.00 62.98 C
ANISOU 2689 CG MET A 270 8741 8124 7066 -893 -556 -435 C
ATOM 2690 SD MET A 270 16.057 171.222 13.772 1.00 91.70 S
ANISOU 2690 SD MET A 270 12266 11728 10850 -777 -506 -324 S
ATOM 2691 CE MET A 270 17.487 172.109 14.404 1.00 89.45 C
ANISOU 2691 CE MET A 270 12019 11436 10531 -667 -407 -432 C
ATOM 2692 N TYR A 271 19.036 172.479 9.546 1.00 47.19 N
ANISOU 2692 N TYR A 271 6789 6235 4907 -987 -596 -468 N
ATOM 2693 CA TYR A 271 20.138 173.313 9.090 1.00 54.48 C
ANISOU 2693 CA TYR A 271 7710 7170 5819 -938 -546 -504 C
ATOM 2694 C TYR A 271 19.658 174.552 8.350 1.00 48.88 C
ANISOU 2694 C TYR A 271 6999 6488 5086 -1025 -616 -419 C
ATOM 2695 O TYR A 271 20.401 175.535 8.271 1.00 36.45 O
ANISOU 2695 O TYR A 271 5427 4919 3502 -988 -576 -439 O
ATOM 2696 CB TYR A 271 21.083 172.486 8.219 1.00 52.95 C
ANISOU 2696 CB TYR A 271 7512 6983 5624 -902 -516 -556 C
ATOM 2697 CG TYR A 271 21.796 171.416 9.010 1.00 70.85 C
ANISOU 2697 CG TYR A 271 9768 9227 7925 -788 -450 -637 C
ATOM 2698 CD1 TYR A 271 22.840 171.742 9.862 1.00 81.05 C
ANISOU 2698 CD1 TYR A 271 11039 10505 9251 -658 -374 -699 C
ATOM 2699 CD2 TYR A 271 21.415 170.085 8.926 1.00 91.21 C
ANISOU 2699 CD2 TYR A 271 12352 11797 10506 -804 -469 -643 C
ATOM 2700 CE1 TYR A 271 23.495 170.777 10.597 1.00 94.21 C
ANISOU 2700 CE1 TYR A 271 12684 12154 10958 -544 -331 -757 C
ATOM 2701 CE2 TYR A 271 22.064 169.110 9.659 1.00 95.99 C
ANISOU 2701 CE2 TYR A 271 12944 12382 11144 -695 -417 -709 C
ATOM 2702 CZ TYR A 271 23.103 169.462 10.494 1.00102.55 C
ANISOU 2702 CZ TYR A 271 13749 13204 12014 -564 -352 -762 C
ATOM 2703 OH TYR A 271 23.756 168.497 11.228 1.00110.31 O
ANISOU 2703 OH TYR A 271 14706 14170 13035 -448 -318 -813 O
ATOM 2704 N LEU A 272 18.435 174.534 7.818 1.00 44.11 N
ANISOU 2704 N LEU A 272 6380 5901 4480 -1133 -722 -316 N
ATOM 2705 CA LEU A 272 17.873 175.754 7.248 1.00 45.44 C
ANISOU 2705 CA LEU A 272 6530 6094 4639 -1203 -800 -217 C
ATOM 2706 C LEU A 272 17.573 176.776 8.337 1.00 48.01 C
ANISOU 2706 C LEU A 272 6791 6387 5065 -1094 -746 -161 C
ATOM 2707 O LEU A 272 17.813 177.975 8.155 1.00 50.46 O
ANISOU 2707 O LEU A 272 7093 6702 5378 -1078 -738 -129 O
ATOM 2708 CB LEU A 272 16.610 175.433 6.450 1.00 50.36 C
ANISOU 2708 CB LEU A 272 7116 6735 5283 -1303 -912 -105 C
ATOM 2709 CG LEU A 272 15.975 176.604 5.698 1.00 48.81 C
ANISOU 2709 CG LEU A 272 6878 6555 5112 -1344 -977 15 C
ATOM 2710 CD1 LEU A 272 16.961 177.193 4.701 1.00 51.78 C
ANISOU 2710 CD1 LEU A 272 7309 6952 5414 -1371 -959 -31 C
ATOM 2711 CD2 LEU A 272 14.700 176.164 4.998 1.00 39.70 C
ANISOU 2711 CD2 LEU A 272 5678 5416 3989 -1428 -1078 121 C
ATOM 2712 N ALA A 273 17.053 176.319 9.480 1.00 43.91 N
ANISOU 2712 N ALA A 273 6221 5829 4633 -1010 -701 -146 N
ATOM 2713 CA ALA A 273 16.750 177.235 10.575 1.00 40.50 C
ANISOU 2713 CA ALA A 273 5719 5363 4306 -893 -642 -91 C
ATOM 2714 C ALA A 273 18.024 177.758 11.228 1.00 51.13 C
ANISOU 2714 C ALA A 273 7108 6698 5621 -806 -545 -198 C
ATOM 2715 O ALA A 273 18.092 178.931 11.614 1.00 46.60 O
ANISOU 2715 O ALA A 273 6499 6111 5094 -741 -512 -159 O
ATOM 2716 CB ALA A 273 15.861 176.542 11.607 1.00 45.84 C
ANISOU 2716 CB ALA A 273 6333 6004 5081 -830 -620 -49 C
ATOM 2717 N ILE A 274 19.039 176.901 11.367 1.00 52.24 N
ANISOU 2717 N ILE A 274 7323 6843 5682 -801 -499 -336 N
ATOM 2718 CA ILE A 274 20.322 177.340 11.913 1.00 47.20 C
ANISOU 2718 CA ILE A 274 6729 6200 5003 -725 -410 -451 C
ATOM 2719 C ILE A 274 20.959 178.374 10.995 1.00 48.40 C
ANISOU 2719 C ILE A 274 6915 6386 5088 -780 -429 -457 C
ATOM 2720 O ILE A 274 21.458 179.412 11.447 1.00 48.05 O
ANISOU 2720 O ILE A 274 6860 6331 5064 -712 -373 -468 O
ATOM 2721 CB ILE A 274 21.256 176.135 12.127 1.00 53.99 C
ANISOU 2721 CB ILE A 274 7654 7062 5796 -707 -363 -594 C
ATOM 2722 CG1 ILE A 274 20.646 175.147 13.119 1.00 45.63 C
ANISOU 2722 CG1 ILE A 274 6578 5967 4791 -656 -340 -597 C
ATOM 2723 CG2 ILE A 274 22.623 176.598 12.608 1.00 52.98 C
ANISOU 2723 CG2 ILE A 274 7500 6925 5707 -569 -260 -670 C
ATOM 2724 CD1 ILE A 274 21.445 173.879 13.258 1.00 51.51 C
ANISOU 2724 CD1 ILE A 274 7325 6703 5541 -589 -292 -684 C
ATOM 2725 N VAL A 275 20.956 178.097 9.690 1.00 49.76 N
ANISOU 2725 N VAL A 275 7124 6596 5186 -899 -505 -447 N
ATOM 2726 CA VAL A 275 21.505 179.038 8.717 1.00 44.32 C
ANISOU 2726 CA VAL A 275 6440 5928 4473 -928 -511 -429 C
ATOM 2727 C VAL A 275 20.731 180.352 8.746 1.00 49.39 C
ANISOU 2727 C VAL A 275 7052 6569 5145 -947 -557 -315 C
ATOM 2728 O VAL A 275 21.318 181.437 8.644 1.00 36.01 O
ANISOU 2728 O VAL A 275 5371 4878 3432 -930 -528 -324 O
ATOM 2729 CB VAL A 275 21.509 178.398 7.315 1.00 35.51 C
ANISOU 2729 CB VAL A 275 5321 4830 3341 -998 -556 -408 C
ATOM 2730 CG1 VAL A 275 21.422 179.457 6.225 1.00 41.11 C
ANISOU 2730 CG1 VAL A 275 6041 5562 4018 -1074 -607 -341 C
ATOM 2731 CG2 VAL A 275 22.756 177.538 7.137 1.00 30.59 C
ANISOU 2731 CG2 VAL A 275 4688 4199 2737 -912 -477 -504 C
ATOM 2732 N LEU A 276 19.407 180.278 8.901 1.00 41.54 N
ANISOU 2732 N LEU A 276 5983 5556 4243 -944 -607 -191 N
ATOM 2733 CA LEU A 276 18.606 181.495 8.988 1.00 39.26 C
ANISOU 2733 CA LEU A 276 5626 5252 4038 -913 -631 -61 C
ATOM 2734 C LEU A 276 18.966 182.306 10.229 1.00 50.11 C
ANISOU 2734 C LEU A 276 6968 6591 5482 -780 -537 -77 C
ATOM 2735 O LEU A 276 19.011 183.542 10.183 1.00 43.40 O
ANISOU 2735 O LEU A 276 6103 5735 4653 -755 -530 -27 O
ATOM 2736 CB LEU A 276 17.120 181.142 8.988 1.00 41.26 C
ANISOU 2736 CB LEU A 276 5803 5497 4377 -931 -700 65 C
ATOM 2737 CG LEU A 276 16.154 182.320 9.118 1.00 40.65 C
ANISOU 2737 CG LEU A 276 5647 5405 4392 -894 -731 205 C
ATOM 2738 CD1 LEU A 276 16.286 183.266 7.935 1.00 24.39 C
ANISOU 2738 CD1 LEU A 276 3622 3374 2273 -974 -791 249 C
ATOM 2739 CD2 LEU A 276 14.730 181.818 9.255 1.00 48.22 C
ANISOU 2739 CD2 LEU A 276 6527 6358 5436 -903 -790 313 C
ATOM 2740 N ALA A 277 19.233 181.627 11.346 1.00 46.38 N
ANISOU 2740 N ALA A 277 6487 6092 5043 -692 -463 -148 N
ATOM 2741 CA ALA A 277 19.611 182.335 12.565 1.00 38.28 C
ANISOU 2741 CA ALA A 277 5431 5031 4082 -560 -371 -171 C
ATOM 2742 C ALA A 277 20.970 183.008 12.414 1.00 38.81 C
ANISOU 2742 C ALA A 277 5564 5113 4071 -550 -314 -274 C
ATOM 2743 O ALA A 277 21.189 184.102 12.947 1.00 40.88 O
ANISOU 2743 O ALA A 277 5801 5355 4376 -476 -267 -256 O
ATOM 2744 CB ALA A 277 19.615 181.372 13.752 1.00 26.58 C
ANISOU 2744 CB ALA A 277 3933 3520 2647 -471 -306 -230 C
ATOM 2745 N HIS A 278 21.895 182.370 11.693 1.00 33.88 N
ANISOU 2745 N HIS A 278 5021 4523 3330 -625 -318 -385 N
ATOM 2746 CA HIS A 278 23.199 182.980 11.462 1.00 29.79 C
ANISOU 2746 CA HIS A 278 4566 4024 2729 -628 -268 -487 C
ATOM 2747 C HIS A 278 23.105 184.165 10.512 1.00 45.74 C
ANISOU 2747 C HIS A 278 6592 6061 4725 -696 -317 -410 C
ATOM 2748 O HIS A 278 23.896 185.109 10.621 1.00 50.46 O
ANISOU 2748 O HIS A 278 7212 6659 5301 -667 -267 -451 O
ATOM 2749 CB HIS A 278 24.179 181.944 10.913 1.00 35.56 C
ANISOU 2749 CB HIS A 278 5321 4775 3416 -639 -249 -588 C
ATOM 2750 CG HIS A 278 24.533 180.869 11.892 1.00 48.00 C
ANISOU 2750 CG HIS A 278 6864 6326 5049 -527 -188 -655 C
ATOM 2751 ND1 HIS A 278 25.171 179.706 11.520 1.00 50.46 N
ANISOU 2751 ND1 HIS A 278 7146 6640 5387 -489 -186 -693 N
ATOM 2752 CD2 HIS A 278 24.342 180.783 13.229 1.00 48.70 C
ANISOU 2752 CD2 HIS A 278 6943 6384 5177 -439 -131 -684 C
ATOM 2753 CE1 HIS A 278 25.356 178.948 12.586 1.00 55.80 C
ANISOU 2753 CE1 HIS A 278 7795 7292 6114 -384 -143 -734 C
ATOM 2754 NE2 HIS A 278 24.862 179.579 13.637 1.00 47.76 N
ANISOU 2754 NE2 HIS A 278 6784 6253 5109 -351 -104 -732 N
ATOM 2755 N THR A 279 22.146 184.137 9.582 1.00 40.03 N
ANISOU 2755 N THR A 279 5852 5352 4006 -787 -415 -301 N
ATOM 2756 CA THR A 279 22.007 185.213 8.607 1.00 43.97 C
ANISOU 2756 CA THR A 279 6362 5867 4477 -857 -470 -224 C
ATOM 2757 C THR A 279 21.673 186.545 9.265 1.00 40.38 C
ANISOU 2757 C THR A 279 5854 5378 4111 -770 -439 -142 C
ATOM 2758 O THR A 279 21.931 187.600 8.673 1.00 40.30 O
ANISOU 2758 O THR A 279 5869 5376 4069 -804 -453 -112 O
ATOM 2759 CB THR A 279 20.934 184.845 7.576 1.00 45.92 C
ANISOU 2759 CB THR A 279 6594 6133 4720 -960 -582 -119 C
ATOM 2760 OG1 THR A 279 21.143 183.500 7.134 1.00 61.74 O
ANISOU 2760 OG1 THR A 279 8640 8163 6656 -1027 -607 -193 O
ATOM 2761 CG2 THR A 279 21.002 185.764 6.368 1.00 40.19 C
ANISOU 2761 CG2 THR A 279 5905 5432 3933 -1051 -641 -68 C
ATOM 2762 N ASN A 280 21.115 186.525 10.478 1.00 36.68 N
ANISOU 2762 N ASN A 280 5314 4871 3751 -658 -398 -106 N
ATOM 2763 CA ASN A 280 20.856 187.769 11.193 1.00 38.29 C
ANISOU 2763 CA ASN A 280 5468 5042 4040 -565 -364 -36 C
ATOM 2764 C ASN A 280 22.134 188.554 11.458 1.00 45.37 C
ANISOU 2764 C ASN A 280 6413 5936 4890 -525 -282 -132 C
ATOM 2765 O ASN A 280 22.072 189.774 11.648 1.00 59.86 O
ANISOU 2765 O ASN A 280 8228 7751 6764 -482 -269 -75 O
ATOM 2766 CB ASN A 280 20.137 187.486 12.511 1.00 32.25 C
ANISOU 2766 CB ASN A 280 4622 4238 3394 -447 -325 3 C
ATOM 2767 CG ASN A 280 19.782 188.755 13.261 1.00 42.81 C
ANISOU 2767 CG ASN A 280 5901 5541 4824 -348 -296 83 C
ATOM 2768 OD1 ASN A 280 18.892 189.500 12.850 1.00 56.79 O
ANISOU 2768 OD1 ASN A 280 7633 7309 6636 -369 -360 208 O
ATOM 2769 ND2 ASN A 280 20.478 189.009 14.363 1.00 27.02 N
ANISOU 2769 ND2 ASN A 280 3896 3516 2855 -237 -199 9 N
ATOM 2770 N SER A 281 23.289 187.891 11.468 1.00 40.22 N
ANISOU 2770 N SER A 281 5823 5304 4154 -537 -229 -278 N
ATOM 2771 CA SER A 281 24.557 188.590 11.626 1.00 46.29 C
ANISOU 2771 CA SER A 281 6641 6077 4868 -510 -154 -380 C
ATOM 2772 C SER A 281 24.998 189.323 10.364 1.00 50.70 C
ANISOU 2772 C SER A 281 7261 6668 5335 -621 -196 -372 C
ATOM 2773 O SER A 281 26.081 189.919 10.368 1.00 48.55 O
ANISOU 2773 O SER A 281 7034 6404 5008 -615 -137 -458 O
ATOM 2774 CB SER A 281 25.650 187.605 12.042 1.00 51.16 C
ANISOU 2774 CB SER A 281 7305 6711 5421 -486 -85 -544 C
ATOM 2775 OG SER A 281 25.362 187.014 13.297 1.00 55.04 O
ANISOU 2775 OG SER A 281 7748 7169 5996 -374 -34 -561 O
ATOM 2776 N VAL A 282 24.207 189.296 9.292 1.00 44.66 N
ANISOU 2776 N VAL A 282 6498 5920 4552 -721 -295 -275 N
ATOM 2777 CA VAL A 282 24.615 189.858 8.008 1.00 40.41 C
ANISOU 2777 CA VAL A 282 6024 5413 3917 -835 -340 -271 C
ATOM 2778 C VAL A 282 23.772 191.089 7.723 1.00 42.09 C
ANISOU 2778 C VAL A 282 6204 5603 4185 -837 -390 -125 C
ATOM 2779 O VAL A 282 24.200 192.009 7.016 1.00 55.48 O
ANISOU 2779 O VAL A 282 7947 7308 5824 -891 -400 -116 O
ATOM 2780 CB VAL A 282 24.463 188.822 6.877 1.00 41.77 C
ANISOU 2780 CB VAL A 282 6237 5627 4007 -957 -418 -283 C
ATOM 2781 CG1 VAL A 282 24.916 189.399 5.530 1.00 40.85 C
ANISOU 2781 CG1 VAL A 282 6157 5529 3833 -1045 -446 -269 C
ATOM 2782 CG2 VAL A 282 25.224 187.554 7.213 1.00 45.51 C
ANISOU 2782 CG2 VAL A 282 6688 6099 4505 -899 -350 -398 C
ATOM 2783 N VAL A 283 22.564 191.110 8.283 1.00 41.89 N
ANISOU 2783 N VAL A 283 6099 5549 4270 -776 -422 -13 N
ATOM 2784 CA VAL A 283 21.553 192.042 7.807 1.00 46.58 C
ANISOU 2784 CA VAL A 283 6660 6130 4909 -796 -495 136 C
ATOM 2785 C VAL A 283 21.736 193.439 8.389 1.00 57.71 C
ANISOU 2785 C VAL A 283 8056 7505 6366 -716 -447 171 C
ATOM 2786 O VAL A 283 21.427 194.427 7.716 1.00 63.88 O
ANISOU 2786 O VAL A 283 8853 8283 7136 -756 -496 256 O
ATOM 2787 CB VAL A 283 20.140 191.498 8.089 1.00 38.92 C
ANISOU 2787 CB VAL A 283 5607 5147 4032 -771 -556 245 C
ATOM 2788 CG1 VAL A 283 19.875 190.240 7.269 1.00 33.17 C
ANISOU 2788 CG1 VAL A 283 4901 4456 3248 -872 -621 227 C
ATOM 2789 CG2 VAL A 283 19.936 191.238 9.579 1.00 45.39 C
ANISOU 2789 CG2 VAL A 283 6358 5933 4955 -638 -485 231 C
ATOM 2790 N ASN A 284 22.214 193.548 9.615 1.00 54.54 N
ANISOU 2790 N ASN A 284 7627 7077 6017 -602 -355 110 N
ATOM 2791 CA ASN A 284 22.355 194.855 10.240 1.00 58.68 C
ANISOU 2791 CA ASN A 284 8135 7566 6593 -519 -308 144 C
ATOM 2792 C ASN A 284 23.118 195.903 9.451 1.00 55.76 C
ANISOU 2792 C ASN A 284 7838 7205 6143 -583 -305 127 C
ATOM 2793 O ASN A 284 22.612 196.992 9.270 1.00 53.24 O
ANISOU 2793 O ASN A 284 7508 6864 5856 -574 -338 229 O
ATOM 2794 CB ASN A 284 22.884 194.733 11.659 1.00 54.07 C
ANISOU 2794 CB ASN A 284 7518 6957 6069 -390 -205 63 C
ATOM 2795 CG ASN A 284 21.952 193.957 12.538 1.00 69.22 C
ANISOU 2795 CG ASN A 284 9357 8858 8087 -314 -209 108 C
ATOM 2796 OD1 ASN A 284 20.984 193.405 12.062 1.00 72.19 O
ANISOU 2796 OD1 ASN A 284 9704 9245 8480 -364 -287 187 O
ATOM 2797 ND2 ASN A 284 22.240 193.901 13.816 1.00 60.90 N
ANISOU 2797 ND2 ASN A 284 8266 7777 7097 -193 -126 56 N
ATOM 2798 N PRO A 285 24.303 195.587 8.956 1.00 46.47 N
ANISOU 2798 N PRO A 285 6736 6060 4859 -649 -269 2 N
ATOM 2799 CA PRO A 285 25.047 196.605 8.193 1.00 58.23 C
ANISOU 2799 CA PRO A 285 8298 7558 6269 -714 -262 -15 C
ATOM 2800 C PRO A 285 24.313 197.106 6.961 1.00 63.95 C
ANISOU 2800 C PRO A 285 9047 8291 6961 -813 -364 102 C
ATOM 2801 O PRO A 285 24.560 198.236 6.522 1.00 72.50 O
ANISOU 2801 O PRO A 285 10169 9362 8014 -840 -367 136 O
ATOM 2802 CB PRO A 285 26.346 195.881 7.817 1.00 55.86 C
ANISOU 2802 CB PRO A 285 8068 7300 5855 -777 -215 -174 C
ATOM 2803 CG PRO A 285 26.499 194.837 8.854 1.00 51.79 C
ANISOU 2803 CG PRO A 285 7513 6783 5384 -693 -160 -255 C
ATOM 2804 CD PRO A 285 25.115 194.374 9.165 1.00 51.14 C
ANISOU 2804 CD PRO A 285 7353 6679 5397 -656 -221 -138 C
ATOM 2805 N PHE A 286 23.423 196.297 6.383 1.00 58.20 N
ANISOU 2805 N PHE A 286 8297 7581 6237 -869 -449 164 N
ATOM 2806 CA PHE A 286 22.622 196.767 5.258 1.00 65.85 C
ANISOU 2806 CA PHE A 286 9282 8557 7183 -954 -550 282 C
ATOM 2807 C PHE A 286 21.555 197.754 5.713 1.00 75.73 C
ANISOU 2807 C PHE A 286 10471 9767 8538 -877 -581 423 C
ATOM 2808 O PHE A 286 21.269 198.734 5.015 1.00 86.25 O
ANISOU 2808 O PHE A 286 11832 11090 9849 -918 -631 505 O
ATOM 2809 CB PHE A 286 21.981 195.582 4.538 1.00 69.35 C
ANISOU 2809 CB PHE A 286 9716 9033 7601 -1033 -630 303 C
ATOM 2810 CG PHE A 286 22.937 194.807 3.685 1.00 75.12 C
ANISOU 2810 CG PHE A 286 10524 9809 8209 -1138 -628 189 C
ATOM 2811 CD1 PHE A 286 23.691 193.776 4.224 1.00 69.37 C
ANISOU 2811 CD1 PHE A 286 9801 9097 7457 -1116 -564 60 C
ATOM 2812 CD2 PHE A 286 23.086 195.113 2.343 1.00 80.25 C
ANISOU 2812 CD2 PHE A 286 11242 10486 8763 -1257 -689 210 C
ATOM 2813 CE1 PHE A 286 24.575 193.064 3.436 1.00 73.51 C
ANISOU 2813 CE1 PHE A 286 10397 9667 7867 -1210 -564 -47 C
ATOM 2814 CE2 PHE A 286 23.967 194.407 1.549 1.00 84.61 C
ANISOU 2814 CE2 PHE A 286 11864 11083 9201 -1353 -687 105 C
ATOM 2815 CZ PHE A 286 24.714 193.382 2.096 1.00 85.58 C
ANISOU 2815 CZ PHE A 286 11962 11209 9346 -1302 -606 -19 C
ATOM 2816 N ILE A 287 20.961 197.512 6.866 1.00 72.86 N
ANISOU 2816 N ILE A 287 10023 9377 8282 -767 -555 451 N
ATOM 2817 CA ILE A 287 19.943 198.409 7.353 1.00 69.48 C
ANISOU 2817 CA ILE A 287 9532 8914 7955 -687 -583 580 C
ATOM 2818 C ILE A 287 20.541 199.780 7.589 1.00 77.07 C
ANISOU 2818 C ILE A 287 10527 9845 8912 -646 -534 580 C
ATOM 2819 O ILE A 287 19.984 200.777 7.178 1.00 74.79 O
ANISOU 2819 O ILE A 287 10244 9539 8636 -653 -585 684 O
ATOM 2820 CB ILE A 287 19.293 197.856 8.606 1.00 56.79 C
ANISOU 2820 CB ILE A 287 7831 7287 6462 -574 -554 598 C
ATOM 2821 CG1 ILE A 287 18.853 196.432 8.335 1.00 40.59 C
ANISOU 2821 CG1 ILE A 287 5757 5264 4400 -626 -596 581 C
ATOM 2822 CG2 ILE A 287 18.103 198.704 8.998 1.00 63.27 C
ANISOU 2822 CG2 ILE A 287 8580 8077 7384 -501 -599 741 C
ATOM 2823 CD1 ILE A 287 18.131 196.274 7.031 1.00 36.02 C
ANISOU 2823 CD1 ILE A 287 5197 4714 3775 -740 -706 661 C
ATOM 2824 N TYR A 288 21.690 199.834 8.240 1.00 75.09 N
ANISOU 2824 N TYR A 288 10303 9588 8641 -603 -434 462 N
ATOM 2825 CA TYR A 288 22.348 201.117 8.464 1.00 60.72 C
ANISOU 2825 CA TYR A 288 8519 7740 6812 -569 -381 451 C
ATOM 2826 C TYR A 288 22.631 201.827 7.148 1.00 56.96 C
ANISOU 2826 C TYR A 288 8128 7276 6236 -685 -430 477 C
ATOM 2827 O TYR A 288 22.446 203.045 7.038 1.00 66.76 O
ANISOU 2827 O TYR A 288 9386 8488 7491 -669 -443 551 O
ATOM 2828 CB TYR A 288 23.645 200.912 9.243 1.00 61.30 C
ANISOU 2828 CB TYR A 288 8614 7815 6864 -521 -267 301 C
ATOM 2829 CG TYR A 288 23.458 200.190 10.553 1.00 62.76 C
ANISOU 2829 CG TYR A 288 8722 7986 7139 -404 -213 266 C
ATOM 2830 CD1 TYR A 288 22.426 200.531 11.413 1.00 62.95 C
ANISOU 2830 CD1 TYR A 288 8661 7974 7283 -298 -226 369 C
ATOM 2831 CD2 TYR A 288 24.309 199.157 10.925 1.00 67.50 C
ANISOU 2831 CD2 TYR A 288 9335 8609 7703 -398 -149 128 C
ATOM 2832 CE1 TYR A 288 22.252 199.873 12.611 1.00 65.65 C
ANISOU 2832 CE1 TYR A 288 8935 8302 7707 -192 -175 338 C
ATOM 2833 CE2 TYR A 288 24.139 198.488 12.121 1.00 70.94 C
ANISOU 2833 CE2 TYR A 288 9706 9029 8219 -291 -99 95 C
ATOM 2834 CZ TYR A 288 23.109 198.850 12.961 1.00 66.81 C
ANISOU 2834 CZ TYR A 288 9100 8469 7816 -189 -111 201 C
ATOM 2835 OH TYR A 288 22.937 198.188 14.156 1.00 73.56 O
ANISOU 2835 OH TYR A 288 9892 9308 8749 -82 -60 170 O
ATOM 2836 N ALA A 289 23.081 201.082 6.136 1.00 54.94 N
ANISOU 2836 N ALA A 289 7931 7064 5879 -803 -459 416 N
ATOM 2837 CA ALA A 289 23.415 201.701 4.858 1.00 65.60 C
ANISOU 2837 CA ALA A 289 9367 8429 7127 -918 -502 433 C
ATOM 2838 C ALA A 289 22.171 202.230 4.157 1.00 75.61 C
ANISOU 2838 C ALA A 289 10622 9685 8421 -947 -609 589 C
ATOM 2839 O ALA A 289 22.192 203.326 3.586 1.00 72.30 O
ANISOU 2839 O ALA A 289 10253 9248 7968 -980 -633 645 O
ATOM 2840 CB ALA A 289 24.152 200.703 3.965 1.00 55.74 C
ANISOU 2840 CB ALA A 289 8179 7233 5766 -1033 -509 331 C
ATOM 2841 N TYR A 290 21.072 201.474 4.201 1.00 81.32 N
ANISOU 2841 N TYR A 290 11278 10416 9203 -934 -675 659 N
ATOM 2842 CA TYR A 290 19.863 201.872 3.493 1.00 83.76 C
ANISOU 2842 CA TYR A 290 11571 10722 9533 -964 -782 801 C
ATOM 2843 C TYR A 290 19.013 202.875 4.265 1.00 88.44 C
ANISOU 2843 C TYR A 290 12103 11269 10232 -854 -791 912 C
ATOM 2844 O TYR A 290 18.191 203.564 3.651 1.00104.10 O
ANISOU 2844 O TYR A 290 14091 13243 12221 -874 -872 1027 O
ATOM 2845 CB TYR A 290 19.016 200.640 3.159 1.00 86.15 C
ANISOU 2845 CB TYR A 290 11827 11056 9852 -1003 -853 830 C
ATOM 2846 CG TYR A 290 19.510 199.850 1.966 1.00 98.68 C
ANISOU 2846 CG TYR A 290 13482 12688 11323 -1137 -889 767 C
ATOM 2847 CD1 TYR A 290 19.240 200.272 0.672 1.00108.76 C
ANISOU 2847 CD1 TYR A 290 14816 13979 12528 -1236 -972 831 C
ATOM 2848 CD2 TYR A 290 20.235 198.677 2.133 1.00106.78 C
ANISOU 2848 CD2 TYR A 290 14518 13744 12311 -1161 -843 645 C
ATOM 2849 CE1 TYR A 290 19.685 199.553 -0.424 1.00113.25 C
ANISOU 2849 CE1 TYR A 290 15448 14591 12992 -1357 -1006 775 C
ATOM 2850 CE2 TYR A 290 20.685 197.951 1.043 1.00111.77 C
ANISOU 2850 CE2 TYR A 290 15212 14420 12837 -1281 -878 588 C
ATOM 2851 CZ TYR A 290 20.407 198.394 -0.233 1.00113.80 C
ANISOU 2851 CZ TYR A 290 15523 14691 13026 -1379 -959 653 C
ATOM 2852 OH TYR A 290 20.851 197.676 -1.321 1.00113.73 O
ANISOU 2852 OH TYR A 290 15576 14725 12910 -1497 -995 597 O
ATOM 2853 N ARG A 291 19.186 202.984 5.585 1.00 74.66 N
ANISOU 2853 N ARG A 291 10301 9496 8569 -735 -712 881 N
ATOM 2854 CA ARG A 291 18.297 203.802 6.398 1.00 64.97 C
ANISOU 2854 CA ARG A 291 9006 8230 7451 -622 -723 986 C
ATOM 2855 C ARG A 291 18.974 204.940 7.150 1.00 61.43 C
ANISOU 2855 C ARG A 291 8575 7741 7025 -542 -643 962 C
ATOM 2856 O ARG A 291 18.266 205.776 7.722 1.00 63.13 O
ANISOU 2856 O ARG A 291 8744 7921 7322 -453 -657 1055 O
ATOM 2857 CB ARG A 291 17.544 202.928 7.415 1.00 53.58 C
ANISOU 2857 CB ARG A 291 7458 6788 6114 -534 -714 1001 C
ATOM 2858 CG ARG A 291 16.627 201.885 6.796 1.00 51.59 C
ANISOU 2858 CG ARG A 291 7170 6570 5862 -598 -800 1047 C
ATOM 2859 CD ARG A 291 15.613 201.397 7.815 1.00 56.39 C
ANISOU 2859 CD ARG A 291 7667 7169 6590 -499 -805 1102 C
ATOM 2860 NE ARG A 291 14.904 202.521 8.418 1.00 69.28 N
ANISOU 2860 NE ARG A 291 9251 8766 8309 -400 -816 1205 N
ATOM 2861 CZ ARG A 291 13.795 203.056 7.920 1.00 75.56 C
ANISOU 2861 CZ ARG A 291 10019 9561 9130 -407 -909 1333 C
ATOM 2862 NH1 ARG A 291 13.260 202.563 6.812 1.00 74.49 N
ANISOU 2862 NH1 ARG A 291 9901 9459 8945 -509 -999 1372 N
ATOM 2863 NH2 ARG A 291 13.220 204.083 8.531 1.00 73.13 N
ANISOU 2863 NH2 ARG A 291 9668 9220 8898 -310 -914 1418 N
ATOM 2864 N ILE A 292 20.303 205.005 7.180 1.00 57.20 N
ANISOU 2864 N ILE A 292 8104 7209 6421 -569 -561 841 N
ATOM 2865 CA ILE A 292 21.017 206.035 7.927 1.00 61.75 C
ANISOU 2865 CA ILE A 292 8698 7748 7017 -495 -479 807 C
ATOM 2866 C ILE A 292 22.012 206.701 6.988 1.00 70.11 C
ANISOU 2866 C ILE A 292 9867 8813 7960 -595 -465 757 C
ATOM 2867 O ILE A 292 22.936 206.045 6.494 1.00 76.98 O
ANISOU 2867 O ILE A 292 10790 9719 8742 -677 -434 647 O
ATOM 2868 CB ILE A 292 21.733 205.462 9.161 1.00 70.49 C
ANISOU 2868 CB ILE A 292 9763 8852 8168 -406 -374 692 C
ATOM 2869 CG1 ILE A 292 20.726 204.759 10.073 1.00 66.94 C
ANISOU 2869 CG1 ILE A 292 9207 8396 7831 -311 -389 743 C
ATOM 2870 CG2 ILE A 292 22.458 206.564 9.919 1.00 75.77 C
ANISOU 2870 CG2 ILE A 292 10448 9482 8858 -328 -292 658 C
ATOM 2871 CD1 ILE A 292 21.346 204.097 11.276 1.00 66.79 C
ANISOU 2871 CD1 ILE A 292 9148 8374 7856 -222 -291 635 C
ATOM 2872 N ARG A 293 21.826 208.002 6.749 1.00 83.53 N
ANISOU 2872 N ARG A 293 11601 10478 9659 -588 -487 836 N
ATOM 2873 CA ARG A 293 22.683 208.710 5.802 1.00 89.68 C
ANISOU 2873 CA ARG A 293 12488 11259 10327 -688 -479 802 C
ATOM 2874 C ARG A 293 24.126 208.768 6.288 1.00 84.27 C
ANISOU 2874 C ARG A 293 11842 10577 9600 -682 -364 656 C
ATOM 2875 O ARG A 293 25.062 208.635 5.490 1.00 89.79 O
ANISOU 2875 O ARG A 293 12620 11304 10190 -787 -344 572 O
ATOM 2876 CB ARG A 293 22.151 210.123 5.561 1.00105.81 C
ANISOU 2876 CB ARG A 293 14560 13258 12385 -669 -523 920 C
ATOM 2877 CG ARG A 293 20.711 210.197 5.076 1.00120.30 C
ANISOU 2877 CG ARG A 293 16359 15090 14261 -669 -639 1067 C
ATOM 2878 CD ARG A 293 20.364 211.618 4.651 1.00124.53 C
ANISOU 2878 CD ARG A 293 16947 15584 14784 -668 -682 1170 C
ATOM 2879 NE ARG A 293 18.937 211.794 4.400 1.00128.98 N
ANISOU 2879 NE ARG A 293 17464 16141 15402 -640 -788 1312 N
ATOM 2880 CZ ARG A 293 18.393 212.920 3.950 1.00140.26 C
ANISOU 2880 CZ ARG A 293 18932 17537 16824 -637 -847 1418 C
ATOM 2881 NH1 ARG A 293 19.158 213.972 3.694 1.00145.73 N
ANISOU 2881 NH1 ARG A 293 19715 18199 17457 -664 -811 1401 N
ATOM 2882 NH2 ARG A 293 17.084 212.994 3.752 1.00143.07 N
ANISOU 2882 NH2 ARG A 293 19238 17892 17230 -608 -944 1541 N
ATOM 2883 N GLU A 294 24.328 208.968 7.593 1.00 72.75 N
ANISOU 2883 N GLU A 294 10326 9091 8225 -559 -288 622 N
ATOM 2884 CA GLU A 294 25.681 209.140 8.111 1.00 67.17 C
ANISOU 2884 CA GLU A 294 9654 8384 7483 -543 -177 486 C
ATOM 2885 C GLU A 294 26.489 207.851 8.004 1.00 64.64 C
ANISOU 2885 C GLU A 294 9342 8115 7103 -594 -136 348 C
ATOM 2886 O GLU A 294 27.687 207.888 7.696 1.00 58.12 O
ANISOU 2886 O GLU A 294 8582 7312 6190 -655 -76 233 O
ATOM 2887 CB GLU A 294 25.629 209.631 9.557 1.00 76.74 C
ANISOU 2887 CB GLU A 294 10798 9554 8804 -392 -110 487 C
ATOM 2888 CG GLU A 294 26.929 210.252 10.042 1.00 85.92 C
ANISOU 2888 CG GLU A 294 12004 10706 9936 -371 -4 374 C
ATOM 2889 CD GLU A 294 27.263 211.543 9.318 1.00 92.16 C
ANISOU 2889 CD GLU A 294 12880 11472 10663 -435 -14 412 C
ATOM 2890 OE1 GLU A 294 26.325 212.251 8.896 1.00 99.72 O
ANISOU 2890 OE1 GLU A 294 13844 12402 11644 -439 -93 547 O
ATOM 2891 OE2 GLU A 294 28.464 211.851 9.168 1.00 91.76 O
ANISOU 2891 OE2 GLU A 294 12894 11431 10539 -483 56 305 O
ATOM 2892 N PHE A 295 25.855 206.702 8.254 1.00 69.23 N
ANISOU 2892 N PHE A 295 9859 8717 7729 -570 -167 356 N
ATOM 2893 CA PHE A 295 26.545 205.429 8.073 1.00 60.32 C
ANISOU 2893 CA PHE A 295 8743 7637 6539 -622 -138 232 C
ATOM 2894 C PHE A 295 26.839 205.164 6.602 1.00 51.21 C
ANISOU 2894 C PHE A 295 7671 6524 5263 -776 -194 217 C
ATOM 2895 O PHE A 295 27.946 204.739 6.250 1.00 47.09 O
ANISOU 2895 O PHE A 295 7204 6039 4650 -842 -146 90 O
ATOM 2896 CB PHE A 295 25.713 204.287 8.657 1.00 60.30 C
ANISOU 2896 CB PHE A 295 8655 7642 6613 -563 -164 255 C
ATOM 2897 CG PHE A 295 26.051 203.955 10.082 1.00 59.08 C
ANISOU 2897 CG PHE A 295 8440 7472 6536 -435 -75 180 C
ATOM 2898 CD1 PHE A 295 27.219 203.275 10.391 1.00 65.51 C
ANISOU 2898 CD1 PHE A 295 9278 8313 7298 -437 7 24 C
ATOM 2899 CD2 PHE A 295 25.195 204.310 11.111 1.00 56.09 C
ANISOU 2899 CD2 PHE A 295 7979 7052 6279 -311 -73 265 C
ATOM 2900 CE1 PHE A 295 27.532 202.963 11.704 1.00 63.58 C
ANISOU 2900 CE1 PHE A 295 8981 8054 7123 -316 88 -47 C
ATOM 2901 CE2 PHE A 295 25.500 204.000 12.425 1.00 58.06 C
ANISOU 2901 CE2 PHE A 295 8175 7287 6600 -191 9 197 C
ATOM 2902 CZ PHE A 295 26.670 203.327 12.722 1.00 56.29 C
ANISOU 2902 CZ PHE A 295 7978 7088 6323 -193 90 41 C
ATOM 2903 N ARG A 296 25.858 205.410 5.731 1.00 58.87 N
ANISOU 2903 N ARG A 296 8649 7491 6229 -833 -295 343 N
ATOM 2904 CA ARG A 296 26.032 205.117 4.312 1.00 61.09 C
ANISOU 2904 CA ARG A 296 9004 7810 6396 -977 -356 338 C
ATOM 2905 C ARG A 296 27.137 205.969 3.702 1.00 65.36 C
ANISOU 2905 C ARG A 296 9641 8354 6837 -1053 -313 276 C
ATOM 2906 O ARG A 296 27.948 205.473 2.912 1.00 64.84 O
ANISOU 2906 O ARG A 296 9638 8332 6666 -1156 -304 186 O
ATOM 2907 CB ARG A 296 24.714 205.335 3.572 1.00 62.36 C
ANISOU 2907 CB ARG A 296 9152 7962 6580 -1010 -472 491 C
ATOM 2908 CG ARG A 296 24.783 205.061 2.082 1.00 77.84 C
ANISOU 2908 CG ARG A 296 11187 9959 8429 -1155 -543 498 C
ATOM 2909 CD ARG A 296 23.434 205.282 1.416 1.00 88.09 C
ANISOU 2909 CD ARG A 296 12467 11248 9756 -1177 -659 651 C
ATOM 2910 NE ARG A 296 23.011 206.678 1.456 1.00 96.71 N
ANISOU 2910 NE ARG A 296 13574 12293 10880 -1138 -678 754 N
ATOM 2911 CZ ARG A 296 22.097 207.161 2.292 1.00 88.69 C
ANISOU 2911 CZ ARG A 296 12485 11238 9975 -1026 -692 848 C
ATOM 2912 NH1 ARG A 296 21.778 208.447 2.253 1.00102.86 N
ANISOU 2912 NH1 ARG A 296 14304 12991 11788 -996 -711 937 N
ATOM 2913 NH2 ARG A 296 21.501 206.358 3.163 1.00 62.93 N
ANISOU 2913 NH2 ARG A 296 9127 7979 6805 -944 -688 854 N
ATOM 2914 N GLN A 297 27.172 207.232 4.081 1.00 66.89 N
ANISOU 2914 N GLN A 297 9847 8503 7064 -1002 -285 323 N
ATOM 2915 CA GLN A 297 28.182 208.115 3.569 1.00 72.99 C
ANISOU 2915 CA GLN A 297 10710 9273 7748 -1069 -241 270 C
ATOM 2916 C GLN A 297 29.529 207.667 4.059 1.00 62.82 C
ANISOU 2916 C GLN A 297 9437 8015 6418 -1065 -135 101 C
ATOM 2917 O GLN A 297 30.488 207.658 3.325 1.00 61.82 O
ANISOU 2917 O GLN A 297 9385 7921 6183 -1165 -110 15 O
ATOM 2918 CB GLN A 297 27.889 209.539 3.990 1.00 85.60 C
ANISOU 2918 CB GLN A 297 12312 10812 9400 -1003 -232 357 C
ATOM 2919 CG GLN A 297 26.745 210.152 3.205 1.00100.80 C
ANISOU 2919 CG GLN A 297 14254 12714 11333 -1036 -340 515 C
ATOM 2920 CD GLN A 297 26.395 211.541 3.674 1.00109.89 C
ANISOU 2920 CD GLN A 297 15408 13805 12542 -961 -335 605 C
ATOM 2921 OE1 GLN A 297 27.125 212.138 4.452 1.00112.63 O
ANISOU 2921 OE1 GLN A 297 15758 14127 12909 -903 -249 544 O
ATOM 2922 NE2 GLN A 297 25.273 212.062 3.203 1.00109.06 N
ANISOU 2922 NE2 GLN A 297 15301 13675 12463 -961 -429 748 N
ATOM 2923 N THR A 298 29.603 207.299 5.321 1.00 61.75 N
ANISOU 2923 N THR A 298 9228 7867 6366 -947 -73 53 N
ATOM 2924 CA THR A 298 30.846 206.820 5.879 1.00 59.00 C
ANISOU 2924 CA THR A 298 8886 7547 5984 -930 27 -111 C
ATOM 2925 C THR A 298 31.291 205.524 5.243 1.00 60.07 C
ANISOU 2925 C THR A 298 9034 7741 6047 -1010 15 -204 C
ATOM 2926 O THR A 298 32.466 205.302 5.075 1.00 59.18 O
ANISOU 2926 O THR A 298 8866 7638 5983 -998 75 -306 O
ATOM 2927 CB THR A 298 30.791 206.693 7.389 1.00 56.66 C
ANISOU 2927 CB THR A 298 8508 7224 5798 -779 94 -141 C
ATOM 2928 OG1 THR A 298 30.206 207.875 7.923 1.00 60.96 O
ANISOU 2928 OG1 THR A 298 9027 7710 6424 -700 91 -35 O
ATOM 2929 CG2 THR A 298 32.175 206.557 7.927 1.00 53.56 C
ANISOU 2929 CG2 THR A 298 8135 6853 5363 -760 203 -307 C
ATOM 2930 N PHE A 299 30.357 204.642 4.912 1.00 72.02 N
ANISOU 2930 N PHE A 299 10521 9271 7572 -1032 -65 -141 N
ATOM 2931 CA PHE A 299 30.731 203.381 4.282 1.00 74.21 C
ANISOU 2931 CA PHE A 299 10768 9589 7841 -1080 -78 -214 C
ATOM 2932 C PHE A 299 31.398 203.637 2.944 1.00 73.57 C
ANISOU 2932 C PHE A 299 10704 9515 7732 -1172 -89 -225 C
ATOM 2933 O PHE A 299 32.364 202.984 2.606 1.00 69.25 O
ANISOU 2933 O PHE A 299 10101 8985 7225 -1164 -46 -309 O
ATOM 2934 CB PHE A 299 29.530 202.455 4.060 1.00 68.53 C
ANISOU 2934 CB PHE A 299 10048 8891 7098 -1115 -173 -138 C
ATOM 2935 CG PHE A 299 28.959 201.858 5.314 1.00 60.30 C
ANISOU 2935 CG PHE A 299 8913 7827 6169 -988 -151 -129 C
ATOM 2936 CD1 PHE A 299 29.718 201.715 6.447 1.00 63.77 C
ANISOU 2936 CD1 PHE A 299 9327 8261 6642 -894 -51 -237 C
ATOM 2937 CD2 PHE A 299 27.644 201.476 5.356 1.00 49.35 C
ANISOU 2937 CD2 PHE A 299 7466 6426 4859 -961 -229 -11 C
ATOM 2938 CE1 PHE A 299 29.180 201.187 7.595 1.00 54.28 C
ANISOU 2938 CE1 PHE A 299 8042 7037 5545 -776 -30 -225 C
ATOM 2939 CE2 PHE A 299 27.103 200.939 6.494 1.00 56.73 C
ANISOU 2939 CE2 PHE A 299 8316 7341 5898 -848 -207 0 C
ATOM 2940 CZ PHE A 299 27.872 200.794 7.616 1.00 50.58 C
ANISOU 2940 CZ PHE A 299 7514 6553 5149 -755 -107 -106 C
ATOM 2941 N ARG A 300 30.880 204.582 2.174 1.00 79.29 N
ANISOU 2941 N ARG A 300 11506 10228 8394 -1252 -150 -129 N
ATOM 2942 CA ARG A 300 31.470 204.899 0.888 1.00 86.04 C
ANISOU 2942 CA ARG A 300 12388 11086 9219 -1342 -159 -137 C
ATOM 2943 C ARG A 300 32.889 205.409 1.035 1.00 80.82 C
ANISOU 2943 C ARG A 300 11702 10415 8591 -1311 -60 -233 C
ATOM 2944 O ARG A 300 33.771 205.006 0.301 1.00 73.34 O
ANISOU 2944 O ARG A 300 10723 9485 7658 -1340 -35 -287 O
ATOM 2945 CB ARG A 300 30.640 205.960 0.188 1.00 97.87 C
ANISOU 2945 CB ARG A 300 13970 12564 10650 -1416 -240 -9 C
ATOM 2946 CG ARG A 300 29.208 205.547 -0.050 1.00108.63 C
ANISOU 2946 CG ARG A 300 15342 13938 11994 -1439 -355 114 C
ATOM 2947 CD ARG A 300 28.473 206.570 -0.890 1.00115.69 C
ANISOU 2947 CD ARG A 300 16301 14810 12846 -1500 -438 250 C
ATOM 2948 NE ARG A 300 27.065 206.233 -1.026 1.00121.86 N
ANISOU 2948 NE ARG A 300 17054 15592 13657 -1492 -545 382 N
ATOM 2949 CZ ARG A 300 26.572 205.505 -2.015 1.00129.97 C
ANISOU 2949 CZ ARG A 300 18079 16647 14656 -1568 -624 412 C
ATOM 2950 NH1 ARG A 300 27.374 205.047 -2.961 1.00129.73 N
ANISOU 2950 NH1 ARG A 300 18056 16635 14601 -1640 -597 320 N
ATOM 2951 NH2 ARG A 300 25.278 205.240 -2.062 1.00136.28 N
ANISOU 2951 NH2 ARG A 300 18834 17441 15504 -1547 -716 531 N
ATOM 2952 N LYS A 301 33.116 206.275 2.010 1.00 80.23 N
ANISOU 2952 N LYS A 301 11635 10314 8536 -1245 -5 -246 N
ATOM 2953 CA LYS A 301 34.442 206.826 2.216 1.00 75.30 C
ANISOU 2953 CA LYS A 301 10977 9680 7953 -1210 82 -327 C
ATOM 2954 C LYS A 301 35.436 205.759 2.564 1.00 67.35 C
ANISOU 2954 C LYS A 301 9862 8701 7026 -1135 134 -424 C
ATOM 2955 O LYS A 301 36.551 205.790 2.105 1.00 68.77 O
ANISOU 2955 O LYS A 301 10008 8893 7230 -1141 169 -472 O
ATOM 2956 CB LYS A 301 34.436 207.856 3.332 1.00 77.65 C
ANISOU 2956 CB LYS A 301 11293 9943 8268 -1137 132 -324 C
ATOM 2957 CG LYS A 301 33.579 209.066 3.053 1.00 77.39 C
ANISOU 2957 CG LYS A 301 11369 9877 8159 -1191 83 -213 C
ATOM 2958 CD LYS A 301 34.152 210.290 3.735 1.00 84.08 C
ANISOU 2958 CD LYS A 301 12236 10688 9024 -1141 154 -233 C
ATOM 2959 CE LYS A 301 33.197 211.466 3.634 1.00 90.37 C
ANISOU 2959 CE LYS A 301 13135 11446 9754 -1166 105 -99 C
ATOM 2960 NZ LYS A 301 32.655 211.628 2.259 1.00 86.41 N
ANISOU 2960 NZ LYS A 301 12696 10950 9187 -1281 11 -9 N
ATOM 2961 N ILE A 302 35.046 204.830 3.411 1.00 66.88 N
ANISOU 2961 N ILE A 302 9748 8651 7010 -1057 136 -445 N
ATOM 2962 CA ILE A 302 35.944 203.756 3.782 1.00 67.35 C
ANISOU 2962 CA ILE A 302 9705 8736 7149 -973 171 -523 C
ATOM 2963 C ILE A 302 36.273 202.871 2.601 1.00 66.84 C
ANISOU 2963 C ILE A 302 9628 8701 7067 -1034 139 -530 C
ATOM 2964 O ILE A 302 37.397 202.439 2.438 1.00 66.19 O
ANISOU 2964 O ILE A 302 9485 8636 7029 -994 168 -583 O
ATOM 2965 CB ILE A 302 35.359 202.884 4.891 1.00 56.15 C
ANISOU 2965 CB ILE A 302 8238 7320 5777 -881 173 -537 C
ATOM 2966 CG1 ILE A 302 35.070 203.725 6.114 1.00 52.76 C
ANISOU 2966 CG1 ILE A 302 7816 6860 5371 -807 213 -532 C
ATOM 2967 CG2 ILE A 302 36.338 201.796 5.264 1.00 58.77 C
ANISOU 2967 CG2 ILE A 302 8467 7674 6189 -786 197 -606 C
ATOM 2968 CD1 ILE A 302 34.189 203.042 7.119 1.00 50.67 C
ANISOU 2968 CD1 ILE A 302 7530 6591 5130 -737 209 -526 C
ATOM 2969 N ILE A 303 35.275 202.596 1.783 1.00 63.35 N
ANISOU 2969 N ILE A 303 9244 8265 6562 -1127 73 -470 N
ATOM 2970 CA ILE A 303 35.464 201.733 0.641 1.00 71.68 C
ANISOU 2970 CA ILE A 303 10290 9346 7599 -1186 41 -472 C
ATOM 2971 C ILE A 303 36.279 202.383 -0.458 1.00 93.07 C
ANISOU 2971 C ILE A 303 13029 12057 10277 -1259 52 -473 C
ATOM 2972 O ILE A 303 37.243 201.807 -0.946 1.00 94.65 O
ANISOU 2972 O ILE A 303 13183 12278 10502 -1244 74 -518 O
ATOM 2973 CB ILE A 303 34.121 201.324 0.046 1.00 70.67 C
ANISOU 2973 CB ILE A 303 10213 9222 7415 -1266 -44 -396 C
ATOM 2974 CG1 ILE A 303 33.388 200.394 0.992 1.00 60.69 C
ANISOU 2974 CG1 ILE A 303 8911 7964 6185 -1199 -58 -401 C
ATOM 2975 CG2 ILE A 303 34.327 200.636 -1.284 1.00 69.96 C
ANISOU 2975 CG2 ILE A 303 10125 9156 7301 -1338 -76 -392 C
ATOM 2976 CD1 ILE A 303 31.907 200.355 0.728 1.00 62.19 C
ANISOU 2976 CD1 ILE A 303 9155 8153 6321 -1268 -150 -306 C
ATOM 2977 N ARG A 304 35.889 203.585 -0.854 1.00107.73 N
ANISOU 2977 N ARG A 304 14966 13891 12075 -1335 33 -419 N
ATOM 2978 CA ARG A 304 36.605 204.284 -1.918 1.00110.75 C
ANISOU 2978 CA ARG A 304 15386 14272 12422 -1413 44 -416 C
ATOM 2979 C ARG A 304 38.073 204.476 -1.558 1.00111.16 C
ANISOU 2979 C ARG A 304 15376 14329 12530 -1347 120 -492 C
ATOM 2980 O ARG A 304 38.967 204.119 -2.334 1.00116.12 O
ANISOU 2980 O ARG A 304 15979 14978 13163 -1366 134 -522 O
ATOM 2981 CB ARG A 304 35.939 205.631 -2.203 1.00114.15 C
ANISOU 2981 CB ARG A 304 15916 14670 12787 -1490 11 -343 C
ATOM 2982 CG ARG A 304 34.547 205.529 -2.808 1.00125.85 C
ANISOU 2982 CG ARG A 304 17460 16147 14208 -1565 -87 -247 C
ATOM 2983 CD ARG A 304 33.938 206.907 -3.020 1.00135.39 C
ANISOU 2983 CD ARG A 304 18763 17321 15358 -1621 -127 -164 C
ATOM 2984 NE ARG A 304 32.560 206.835 -3.498 1.00144.66 N
ANISOU 2984 NE ARG A 304 19985 18494 16487 -1673 -234 -56 N
ATOM 2985 CZ ARG A 304 31.787 207.895 -3.714 1.00148.76 C
ANISOU 2985 CZ ARG A 304 20578 18984 16961 -1709 -294 45 C
ATOM 2986 NH1 ARG A 304 30.545 207.735 -4.149 1.00145.75 N
ANISOU 2986 NH1 ARG A 304 20218 18605 16555 -1740 -399 153 N
ATOM 2987 NH2 ARG A 304 32.256 209.116 -3.493 1.00152.53 N
ANISOU 2987 NH2 ARG A 304 21101 19429 17423 -1704 -252 44 N
ATOM 2988 N SER A 305 38.330 205.039 -0.395 1.00111.37 N
ANISOU 2988 N SER A 305 15377 14338 12600 -1265 165 -518 N
ATOM 2989 CA SER A 305 39.699 205.228 0.014 1.00115.13 C
ANISOU 2989 CA SER A 305 15788 14821 13136 -1195 225 -581 C
ATOM 2990 C SER A 305 40.358 203.870 0.130 1.00115.41 C
ANISOU 2990 C SER A 305 15758 14883 13211 -1165 242 -630 C
ATOM 2991 O SER A 305 40.631 203.399 1.228 1.00118.43 O
ANISOU 2991 O SER A 305 16086 15264 13649 -1085 273 -666 O
ATOM 2992 CB SER A 305 39.763 205.973 1.337 1.00119.71 C
ANISOU 2992 CB SER A 305 16348 15377 13760 -1109 265 -595 C
ATOM 2993 OG SER A 305 39.265 207.287 1.181 1.00121.33 O
ANISOU 2993 OG SER A 305 16642 15548 13909 -1178 264 -550 O
TER 2994 SER A 305
HETATM 2995 NA NA A2400 23.198 189.530 16.658 1.00 62.78 NA
HETATM 2996 C10 8JN A2401 22.190 171.293 15.602 1.00 74.95 C
HETATM 2997 C13 8JN A2401 20.304 172.803 17.581 1.00 47.66 C
HETATM 2998 C14 8JN A2401 19.389 173.610 18.283 1.00 43.39 C
HETATM 2999 C16 8JN A2401 18.363 171.597 17.809 1.00 59.90 C
HETATM 3000 C18 8JN A2401 17.288 170.444 17.727 1.00 80.64 C
HETATM 3001 C21 8JN A2401 15.447 169.654 19.346 1.00 93.60 C
HETATM 3002 C22 8JN A2401 16.960 169.580 19.024 1.00 84.99 C
HETATM 3003 C23 8JN A2401 17.209 168.182 18.548 1.00 79.37 C
HETATM 3004 C24 8JN A2401 16.490 168.166 17.105 1.00 88.23 C
HETATM 3005 C25 8JN A2401 17.369 169.284 16.538 1.00 84.75 C
HETATM 3006 C26 8JN A2401 15.022 168.649 17.123 1.00 94.79 C
HETATM 3007 C27 8JN A2401 19.737 175.014 18.756 1.00 39.51 C
HETATM 3008 C01 8JN A2401 22.172 179.345 15.781 1.00 81.74 C
HETATM 3009 C02 8JN A2401 22.414 178.165 16.774 1.00 70.77 C
HETATM 3010 C03 8JN A2401 21.273 178.010 17.829 1.00 62.94 C
HETATM 3011 C04 8JN A2401 21.513 176.886 18.886 1.00 45.42 C
HETATM 3012 N05 8JN A2401 21.078 175.446 18.422 1.00 41.79 N
HETATM 3013 C06 8JN A2401 22.057 174.651 17.703 1.00 58.08 C
HETATM 3014 O07 8JN A2401 23.147 175.068 17.463 1.00 72.88 O
HETATM 3015 N08 8JN A2401 21.624 173.294 17.284 1.00 50.13 N
HETATM 3016 C09 8JN A2401 22.714 172.478 16.511 1.00 67.25 C
HETATM 3017 C11 8JN A2401 23.267 170.451 14.824 1.00 74.18 C
HETATM 3018 O12 8JN A2401 24.236 171.315 14.282 1.00 69.12 O
HETATM 3019 N15 8JN A2401 18.205 172.848 18.410 1.00 51.44 N
HETATM 3020 N17 8JN A2401 19.646 171.569 17.303 1.00 53.72 N
HETATM 3021 C19 8JN A2401 15.843 170.854 17.252 1.00 84.79 C
HETATM 3022 C20 8JN A2401 14.875 169.875 17.986 1.00 90.23 C
HETATM 3023 O28 8JN A2401 19.015 175.726 19.342 1.00 56.04 O
HETATM 3024 C1 CLR A2402 37.963 169.695 22.027 1.00 68.31 C
HETATM 3025 C2 CLR A2402 37.736 168.205 22.362 1.00 72.69 C
HETATM 3026 C3 CLR A2402 38.077 167.895 23.795 1.00 80.65 C
HETATM 3027 C4 CLR A2402 37.317 168.819 24.763 1.00 79.95 C
HETATM 3028 C5 CLR A2402 37.464 170.279 24.410 1.00 72.57 C
HETATM 3029 C6 CLR A2402 37.736 171.151 25.400 1.00 70.57 C
HETATM 3030 C7 CLR A2402 37.840 172.659 25.235 1.00 78.92 C
HETATM 3031 C8 CLR A2402 37.467 173.124 23.830 1.00 70.51 C
HETATM 3032 C9 CLR A2402 37.888 172.098 22.771 1.00 70.82 C
HETATM 3033 C10 CLR A2402 37.280 170.698 22.966 1.00 70.94 C
HETATM 3034 C11 CLR A2402 37.668 172.681 21.374 1.00 61.03 C
HETATM 3035 C12 CLR A2402 38.273 174.079 21.179 1.00 65.89 C
HETATM 3036 C13 CLR A2402 37.889 175.100 22.218 1.00 66.74 C
HETATM 3037 C14 CLR A2402 38.185 174.432 23.556 1.00 72.58 C
HETATM 3038 C15 CLR A2402 37.986 175.551 24.571 1.00 76.85 C
HETATM 3039 C16 CLR A2402 38.525 176.768 23.825 1.00 70.26 C
HETATM 3040 C17 CLR A2402 38.700 176.403 22.349 1.00 64.04 C
HETATM 3041 C18 CLR A2402 36.393 175.487 22.050 1.00 66.93 C
HETATM 3042 C19 CLR A2402 35.753 170.698 22.676 1.00 67.75 C
HETATM 3043 C20 CLR A2402 38.395 177.627 21.470 1.00 54.58 C
HETATM 3044 C21 CLR A2402 38.671 177.388 19.985 1.00 52.95 C
HETATM 3045 C22 CLR A2402 39.221 178.845 21.946 1.00 58.08 C
HETATM 3046 C23 CLR A2402 39.292 180.027 20.966 1.00 61.40 C
HETATM 3047 C24 CLR A2402 40.176 181.140 21.536 1.00 73.34 C
HETATM 3048 C25 CLR A2402 39.947 182.518 20.896 1.00 69.70 C
HETATM 3049 C26 CLR A2402 40.691 183.617 21.653 1.00 67.19 C
HETATM 3050 C27 CLR A2402 40.340 182.545 19.420 1.00 68.35 C
HETATM 3051 O1 CLR A2402 37.742 166.532 24.105 1.00 85.66 O
HETATM 3052 C1 CLR A2403 7.917 170.070 13.523 1.00 87.06 C
HETATM 3053 C2 CLR A2403 7.836 168.540 13.712 1.00 90.59 C
HETATM 3054 C3 CLR A2403 6.515 167.964 13.271 1.00 91.33 C
HETATM 3055 C4 CLR A2403 6.150 168.410 11.844 1.00 87.79 C
HETATM 3056 C5 CLR A2403 6.272 169.901 11.663 1.00 93.05 C
HETATM 3057 C6 CLR A2403 5.239 170.564 11.107 1.00 96.84 C
HETATM 3058 C7 CLR A2403 5.243 172.045 10.769 1.00 97.42 C
HETATM 3059 C8 CLR A2403 6.636 172.648 10.902 1.00 99.91 C
HETATM 3060 C9 CLR A2403 7.346 172.096 12.145 1.00 95.29 C
HETATM 3061 C10 CLR A2403 7.549 170.573 12.122 1.00 93.33 C
HETATM 3062 C11 CLR A2403 8.636 172.874 12.405 1.00 98.80 C
HETATM 3063 C12 CLR A2403 8.459 174.397 12.377 1.00 98.86 C
HETATM 3064 C13 CLR A2403 7.795 174.940 11.140 1.00 98.82 C
HETATM 3065 C14 CLR A2403 6.496 174.153 11.021 1.00105.29 C
HETATM 3066 C15 CLR A2403 5.735 174.857 9.902 1.00105.01 C
HETATM 3067 C16 CLR A2403 6.145 176.316 10.078 1.00106.29 C
HETATM 3068 C17 CLR A2403 7.256 176.384 11.125 1.00 99.55 C
HETATM 3069 C18 CLR A2403 8.733 174.755 9.914 1.00 91.66 C
HETATM 3070 C19 CLR A2403 8.678 170.172 11.132 1.00 99.22 C
HETATM 3071 C20 CLR A2403 8.171 177.585 10.838 1.00 95.40 C
HETATM 3072 C21 CLR A2403 9.292 177.726 11.863 1.00 95.64 C
HETATM 3073 C22 CLR A2403 7.353 178.897 10.810 1.00 94.64 C
HETATM 3074 C23 CLR A2403 8.129 180.171 11.184 1.00 94.94 C
HETATM 3075 C24 CLR A2403 7.168 181.335 11.445 1.00 98.47 C
HETATM 3076 C25 CLR A2403 7.795 182.731 11.296 1.00 90.48 C
HETATM 3077 C26 CLR A2403 8.408 183.222 12.606 1.00 86.46 C
HETATM 3078 C27 CLR A2403 8.835 182.791 10.179 1.00 85.83 C
HETATM 3079 O1 CLR A2403 6.575 166.528 13.288 1.00 93.04 O
HETATM 3080 C1 CLR A2404 2.886 172.624 21.563 1.00 63.53 C
HETATM 3081 C2 CLR A2404 2.611 171.105 21.476 1.00 60.33 C
HETATM 3082 C3 CLR A2404 1.728 170.739 20.312 1.00 53.43 C
HETATM 3083 C4 CLR A2404 2.245 171.341 18.990 1.00 57.50 C
HETATM 3084 C5 CLR A2404 2.566 172.813 19.108 1.00 66.91 C
HETATM 3085 C6 CLR A2404 2.070 173.662 18.185 1.00 63.42 C
HETATM 3086 C7 CLR A2404 2.365 175.151 18.133 1.00 68.28 C
HETATM 3087 C8 CLR A2404 3.528 175.518 19.047 1.00 64.68 C
HETATM 3088 C9 CLR A2404 3.415 174.792 20.392 1.00 61.12 C
HETATM 3089 C10 CLR A2404 3.423 173.260 20.275 1.00 68.34 C
HETATM 3090 C11 CLR A2404 4.477 175.319 21.359 1.00 60.71 C
HETATM 3091 C12 CLR A2404 4.586 176.848 21.425 1.00 65.21 C
HETATM 3092 C13 CLR A2404 4.683 177.547 20.095 1.00 73.29 C
HETATM 3093 C14 CLR A2404 3.506 177.012 19.293 1.00 69.46 C
HETATM 3094 C15 CLR A2404 3.440 177.912 18.062 1.00 69.94 C
HETATM 3095 C16 CLR A2404 3.922 179.258 18.594 1.00 72.25 C
HETATM 3096 C17 CLR A2404 4.435 179.063 20.021 1.00 75.24 C
HETATM 3097 C18 CLR A2404 6.053 177.239 19.425 1.00 69.22 C
HETATM 3098 C19 CLR A2404 4.866 172.748 20.019 1.00 66.32 C
HETATM 3099 C20 CLR A2404 5.550 180.079 20.320 1.00 65.91 C
HETATM 3100 C21 CLR A2404 6.092 179.992 21.748 1.00 63.09 C
HETATM 3101 C22 CLR A2404 5.016 181.507 20.084 1.00 68.38 C
HETATM 3102 C23 CLR A2404 6.073 182.618 20.040 1.00 60.54 C
HETATM 3103 C24 CLR A2404 5.393 183.981 20.194 1.00 68.11 C
HETATM 3104 C25 CLR A2404 5.545 184.907 18.978 1.00 77.21 C
HETATM 3105 C26 CLR A2404 6.867 185.666 19.016 1.00 83.11 C
HETATM 3106 C27 CLR A2404 5.420 184.160 17.652 1.00 82.85 C
HETATM 3107 O1 CLR A2404 1.669 169.307 20.184 1.00 51.26 O
HETATM 3108 C1 OLA A2405 36.505 166.504 12.943 1.00 95.97 C
HETATM 3109 O1 OLA A2405 35.992 165.350 12.940 1.00 99.10 O
HETATM 3110 O2 OLA A2405 37.371 166.752 13.798 1.00 97.08 O
HETATM 3111 C2 OLA A2405 36.093 167.569 11.944 1.00 90.57 C
HETATM 3112 C3 OLA A2405 35.247 168.668 12.593 1.00 78.35 C
HETATM 3113 C4 OLA A2405 35.476 170.046 11.984 1.00 74.29 C
HETATM 3114 C5 OLA A2405 36.764 170.701 12.442 1.00 70.54 C
HETATM 3115 C6 OLA A2405 37.131 171.977 11.698 1.00 62.07 C
HETATM 3116 C7 OLA A2405 35.892 172.739 11.234 1.00 56.21 C
HETATM 3117 C8 OLA A2405 36.026 174.251 11.267 1.00 46.32 C
HETATM 3118 C9 OLA A2405 35.973 174.786 9.844 1.00 49.84 C
HETATM 3119 C10 OLA A2405 36.508 175.956 9.428 1.00 61.11 C
HETATM 3120 C11 OLA A2405 37.248 176.905 10.347 1.00 74.53 C
HETATM 3121 C12 OLA A2405 38.268 177.777 9.591 1.00 68.54 C
HETATM 3122 C13 OLA A2405 39.038 178.746 10.512 1.00 73.70 C
HETATM 3123 C14 OLA A2405 38.194 179.951 10.957 1.00 72.92 C
HETATM 3124 C15 OLA A2405 38.880 180.847 12.006 1.00 70.89 C
HETATM 3125 C16 OLA A2405 39.592 182.067 11.395 1.00 75.65 C
HETATM 3126 C17 OLA A2405 39.272 183.389 12.113 1.00 73.67 C
HETATM 3127 C18 OLA A2405 39.620 184.623 11.266 1.00 55.76 C
HETATM 3128 C1 OLA A2406 8.330 166.240 7.973 1.00103.27 C
HETATM 3129 O1 OLA A2406 7.965 165.278 7.243 1.00106.69 O
HETATM 3130 O2 OLA A2406 8.365 166.051 9.200 1.00105.26 O
HETATM 3131 C2 OLA A2406 8.720 167.586 7.394 1.00 92.60 C
HETATM 3132 C3 OLA A2406 7.503 168.468 7.105 1.00 90.79 C
HETATM 3133 C4 OLA A2406 7.808 169.628 6.165 1.00 97.79 C
HETATM 3134 C5 OLA A2406 7.653 170.991 6.812 1.00 90.26 C
HETATM 3135 C6 OLA A2406 8.531 172.086 6.221 1.00 84.91 C
HETATM 3136 C7 OLA A2406 7.735 173.359 5.935 1.00 88.08 C
HETATM 3137 C8 OLA A2406 8.500 174.651 6.159 1.00 93.69 C
HETATM 3138 C9 OLA A2406 8.188 175.618 5.026 1.00 96.58 C
HETATM 3139 C10 OLA A2406 9.080 176.107 4.134 1.00 91.78 C
HETATM 3140 C11 OLA A2406 10.553 175.752 4.134 1.00 79.03 C
HETATM 3141 C12 OLA A2406 11.427 176.911 3.617 1.00 76.81 C
HETATM 3142 C13 OLA A2406 11.374 177.091 2.086 1.00 71.45 C
HETATM 3143 C1 OLA A2407 5.535 198.873 15.614 1.00107.90 C
HETATM 3144 O1 OLA A2407 5.947 199.791 14.885 1.00110.42 O
HETATM 3145 O2 OLA A2407 4.408 198.369 15.347 1.00114.70 O
HETATM 3146 C2 OLA A2407 6.371 198.389 16.783 1.00 92.55 C
HETATM 3147 C3 OLA A2407 7.734 197.851 16.341 1.00 81.64 C
HETATM 3148 C4 OLA A2407 8.066 196.481 16.921 1.00 80.65 C
HETATM 3149 C5 OLA A2407 9.449 195.987 16.545 1.00 66.27 C
HETATM 3150 C6 OLA A2407 10.165 195.195 17.630 1.00 58.07 C
HETATM 3151 C7 OLA A2407 10.221 193.709 17.290 1.00 63.59 C
HETATM 3152 C8 OLA A2407 10.381 192.790 18.486 1.00 59.56 C
HETATM 3153 C9 OLA A2407 9.661 191.481 18.203 1.00 54.95 C
HETATM 3154 C10 OLA A2407 8.434 191.151 18.663 1.00 59.17 C
HETATM 3155 C11 OLA A2407 7.752 189.834 18.365 1.00 58.52 C
HETATM 3156 C12 OLA A2407 8.215 188.730 19.336 1.00 46.89 C
HETATM 3157 C1 OLA A2408 36.446 170.000 29.615 1.00115.49 C
HETATM 3158 O1 OLA A2408 37.451 169.825 28.907 1.00117.82 O
HETATM 3159 O2 OLA A2408 35.814 168.976 30.001 1.00116.61 O
HETATM 3160 C2 OLA A2408 36.011 171.403 29.992 1.00106.75 C
HETATM 3161 C3 OLA A2408 36.324 172.418 28.890 1.00 88.41 C
HETATM 3162 C4 OLA A2408 37.241 173.545 29.347 1.00 88.53 C
HETATM 3163 C5 OLA A2408 36.915 174.885 28.716 1.00 89.40 C
HETATM 3164 C6 OLA A2408 37.488 176.093 29.446 1.00 90.73 C
HETATM 3165 C7 OLA A2408 38.384 176.932 28.537 1.00 91.79 C
HETATM 3166 C8 OLA A2408 37.673 178.043 27.785 1.00 85.09 C
HETATM 3167 C9 OLA A2408 38.444 179.342 27.969 1.00 80.43 C
HETATM 3168 C1 OLA A2409 21.207 190.948 3.206 1.00 52.03 C
HETATM 3169 C2 OLA A2409 20.857 189.547 3.670 1.00 56.00 C
HETATM 3170 C3 OLA A2409 21.371 188.471 2.707 1.00 46.35 C
HETATM 3171 C4 OLA A2409 22.284 187.435 3.357 1.00 58.73 C
HETATM 3172 C5 OLA A2409 22.394 186.135 2.580 1.00 56.69 C
HETATM 3173 C6 OLA A2409 23.679 185.345 2.805 1.00 57.98 C
HETATM 3174 C7 OLA A2409 23.564 183.901 2.317 1.00 54.50 C
HETATM 3175 C1 OLA A2410 24.347 167.372 7.656 1.00106.41 C
HETATM 3176 O1 OLA A2410 24.766 168.453 8.099 1.00106.59 O
HETATM 3177 O2 OLA A2410 24.845 166.314 8.130 1.00100.90 O
HETATM 3178 C2 OLA A2410 23.276 167.347 6.582 1.00110.05 C
HETATM 3179 C3 OLA A2410 22.798 168.754 6.211 1.00105.08 C
HETATM 3180 C4 OLA A2410 21.700 168.768 5.153 1.00 98.95 C
HETATM 3181 C5 OLA A2410 22.072 169.545 3.905 1.00 86.28 C
HETATM 3182 C6 OLA A2410 20.937 170.347 3.283 1.00 79.04 C
HETATM 3183 C7 OLA A2410 21.341 171.800 3.047 1.00 70.63 C
HETATM 3184 C8 OLA A2410 20.287 172.824 3.425 1.00 59.82 C
HETATM 3185 C9 OLA A2410 20.965 173.960 4.177 1.00 56.68 C
HETATM 3186 C10 OLA A2410 21.227 175.188 3.678 1.00 48.92 C
HETATM 3187 C11 OLA A2410 20.870 175.609 2.268 1.00 59.94 C
HETATM 3188 C12 OLA A2410 20.070 176.926 2.243 1.00 64.80 C
HETATM 3189 C13 OLA A2410 20.704 178.020 1.359 1.00 59.33 C
HETATM 3190 C14 OLA A2410 20.048 179.400 1.527 1.00 69.99 C
HETATM 3191 C15 OLA A2410 20.935 180.432 2.253 1.00 78.82 C
HETATM 3192 C1 OLA A2411 27.840 201.554 40.011 1.00 89.53 C
HETATM 3193 O1 OLA A2411 27.245 202.659 39.881 1.00 84.14 O
HETATM 3194 O2 OLA A2411 28.949 201.558 40.572 1.00 83.92 O
HETATM 3195 C2 OLA A2411 27.237 200.256 39.507 1.00 86.85 C
HETATM 3196 C3 OLA A2411 28.052 199.033 39.937 1.00 79.95 C
HETATM 3197 C4 OLA A2411 27.708 197.770 39.154 1.00 77.56 C
HETATM 3198 C5 OLA A2411 26.423 197.106 39.610 1.00 73.94 C
HETATM 3199 C6 OLA A2411 25.689 196.317 38.533 1.00 75.76 C
HETATM 3200 C7 OLA A2411 24.372 195.740 39.048 1.00 74.50 C
HETATM 3201 C8 OLA A2411 23.756 194.664 38.172 1.00 71.84 C
HETATM 3202 C9 OLA A2411 24.244 193.298 38.635 1.00 81.06 C
HETATM 3203 C10 OLA A2411 23.489 192.179 38.724 1.00 85.48 C
HETATM 3204 C11 OLA A2411 24.022 190.840 39.190 1.00 83.02 C
HETATM 3205 C12 OLA A2411 22.911 189.936 39.761 1.00 75.68 C
HETATM 3206 C13 OLA A2411 23.192 188.432 39.576 1.00 63.40 C
HETATM 3207 C14 OLA A2411 22.252 187.761 38.564 1.00 61.54 C
HETATM 3208 C15 OLA A2411 22.937 186.680 37.707 1.00 63.17 C
HETATM 3209 C16 OLA A2411 21.982 185.982 36.721 1.00 58.03 C
HETATM 3210 C17 OLA A2411 22.244 184.474 36.589 1.00 46.68 C
HETATM 3211 C18 OLA A2411 22.211 183.997 35.130 1.00 46.75 C
HETATM 3212 C4 OLA A2412 33.425 196.103 2.921 1.00 74.01 C
HETATM 3213 C5 OLA A2412 32.715 195.296 1.851 1.00 74.71 C
HETATM 3214 C6 OLA A2412 31.194 195.327 1.923 1.00 74.02 C
HETATM 3215 C7 OLA A2412 30.647 194.242 2.847 1.00 67.71 C
HETATM 3216 C8 OLA A2412 29.145 194.275 3.060 1.00 66.03 C
HETATM 3217 C9 OLA A2412 28.620 192.847 3.068 1.00 64.24 C
HETATM 3218 C10 OLA A2412 27.766 192.323 3.976 1.00 63.44 C
HETATM 3219 C1 OLA A2413 15.705 168.013 0.464 1.00 95.80 C
HETATM 3220 O1 OLA A2413 14.446 168.089 0.418 1.00 94.86 O
HETATM 3221 O2 OLA A2413 16.205 166.974 0.926 1.00 83.69 O
HETATM 3222 C2 OLA A2413 16.595 169.140 -0.027 1.00 94.09 C
HETATM 3223 C3 OLA A2413 16.471 170.400 0.835 1.00 78.99 C
HETATM 3224 C4 OLA A2413 16.318 171.682 0.024 1.00 69.96 C
HETATM 3225 C5 OLA A2413 16.676 172.937 0.796 1.00 73.37 C
HETATM 3226 C6 OLA A2413 16.100 174.230 0.232 1.00 58.21 C
HETATM 3227 C1 OLA A2414 33.701 170.586 2.364 1.00 54.70 C
HETATM 3228 C2 OLA A2414 33.038 171.899 1.997 1.00 62.60 C
HETATM 3229 C3 OLA A2414 33.823 172.660 0.925 1.00 66.28 C
HETATM 3230 C4 OLA A2414 34.553 173.890 1.455 1.00 69.08 C
HETATM 3231 C5 OLA A2414 34.601 175.042 0.469 1.00 57.71 C
HETATM 3232 C6 OLA A2414 34.314 176.418 1.058 1.00 55.44 C
HETATM 3233 C7 OLA A2414 34.257 177.502 -0.018 1.00 64.03 C
HETATM 3234 C8 OLA A2414 33.640 178.819 0.423 1.00 64.37 C
HETATM 3235 C9 OLA A2414 32.684 179.310 -0.656 1.00 58.08 C
HETATM 3236 C1 OLA A2415 28.861 201.548 35.275 1.00 94.66 C
HETATM 3237 O1 OLA A2415 29.761 202.384 34.981 1.00 99.24 O
HETATM 3238 O2 OLA A2415 27.680 201.866 35.055 1.00 80.52 O
HETATM 3239 C2 OLA A2415 29.191 200.196 35.880 1.00 91.59 C
HETATM 3240 C3 OLA A2415 30.540 199.658 35.392 1.00 82.94 C
HETATM 3241 C4 OLA A2415 31.146 198.602 36.309 1.00 82.79 C
HETATM 3242 C5 OLA A2415 31.268 197.231 35.670 1.00 83.19 C
HETATM 3243 C6 OLA A2415 30.904 196.068 36.585 1.00 71.49 C
HETATM 3244 C7 OLA A2415 31.086 194.718 35.894 1.00 73.98 C
HETATM 3245 C8 OLA A2415 31.187 193.529 36.833 1.00 79.79 C
HETATM 3246 C9 OLA A2415 30.127 192.502 36.457 1.00 72.32 C
HETATM 3247 C10 OLA A2415 28.939 192.325 37.077 1.00 64.36 C
HETATM 3248 C11 OLA A2415 27.925 191.283 36.652 1.00 69.17 C
HETATM 3249 C12 OLA A2415 26.474 191.767 36.839 1.00 60.59 C
HETATM 3250 C1 OLA A2416 43.612 205.536 13.177 1.00 86.20 C
HETATM 3251 O1 OLA A2416 43.856 206.177 12.118 1.00 90.80 O
HETATM 3252 O2 OLA A2416 42.982 206.118 14.077 1.00 79.25 O
HETATM 3253 C2 OLA A2416 44.064 204.101 13.364 1.00 85.68 C
HETATM 3254 C3 OLA A2416 43.314 203.404 14.502 1.00 87.02 C
HETATM 3255 C4 OLA A2416 43.168 201.900 14.304 1.00 86.64 C
HETATM 3256 C5 OLA A2416 42.379 201.221 15.406 1.00 97.99 C
HETATM 3257 C6 OLA A2416 40.897 201.026 15.110 1.00102.18 C
HETATM 3258 C7 OLA A2416 40.167 200.392 16.291 1.00103.33 C
HETATM 3259 C8 OLA A2416 39.330 199.173 15.947 1.00 99.53 C
HETATM 3260 C9 OLA A2416 38.070 199.630 15.226 1.00 90.49 C
HETATM 3261 C10 OLA A2416 37.445 198.963 14.230 1.00 86.78 C
HETATM 3262 C11 OLA A2416 37.924 197.635 13.682 1.00 77.76 C
HETATM 3263 C12 OLA A2416 37.517 196.457 14.588 1.00 68.38 C
HETATM 3264 C13 OLA A2416 37.277 195.145 13.816 1.00 68.40 C
HETATM 3265 C14 OLA A2416 37.602 193.887 14.635 1.00 56.61 C
HETATM 3266 C15 OLA A2416 38.341 192.799 13.831 1.00 63.52 C
HETATM 3267 C1 OLA A2417 8.617 198.133 12.218 1.00 84.86 C
HETATM 3268 O1 OLA A2417 8.531 199.284 11.757 1.00 80.47 O
HETATM 3269 O2 OLA A2417 8.148 197.925 13.370 1.00 78.77 O
HETATM 3270 C2 OLA A2417 9.267 197.023 11.414 1.00 83.82 C
HETATM 3271 C3 OLA A2417 9.720 195.868 12.314 1.00 79.91 C
HETATM 3272 C4 OLA A2417 9.361 194.486 11.780 1.00 76.71 C
HETATM 3273 C5 OLA A2417 10.264 194.001 10.662 1.00 75.43 C
HETATM 3274 C6 OLA A2417 10.183 192.505 10.384 1.00 74.73 C
HETATM 3275 C7 OLA A2417 8.944 191.884 11.025 1.00 77.50 C
HETATM 3276 C8 OLA A2417 9.203 191.120 12.311 1.00 76.70 C
HETATM 3277 C9 OLA A2417 8.068 191.392 13.287 1.00 76.72 C
HETATM 3278 C10 OLA A2417 7.405 190.453 13.996 1.00 75.50 C
HETATM 3279 C11 OLA A2417 7.712 188.973 13.908 1.00 77.95 C
HETATM 3280 C12 OLA A2417 7.967 188.357 15.297 1.00 87.05 C
HETATM 3281 C1 OLA A2418 31.768 170.851 36.605 1.00 96.52 C
HETATM 3282 O1 OLA A2418 32.229 169.717 36.299 1.00104.31 O
HETATM 3283 O2 OLA A2418 30.559 170.933 36.879 1.00100.56 O
HETATM 3284 C2 OLA A2418 32.643 172.087 36.642 1.00 83.98 C
HETATM 3285 C3 OLA A2418 31.834 173.363 36.400 1.00 66.81 C
HETATM 3286 C4 OLA A2418 32.694 174.620 36.372 1.00 67.60 C
HETATM 3287 C5 OLA A2418 31.885 175.902 36.399 1.00 68.54 C
HETATM 3288 C6 OLA A2418 32.416 176.969 37.345 1.00 66.60 C
HETATM 3289 C7 OLA A2418 31.548 178.225 37.323 1.00 73.16 C
HETATM 3290 C8 OLA A2418 31.550 179.026 38.612 1.00 72.15 C
HETATM 3291 C9 OLA A2418 31.250 180.484 38.294 1.00 57.91 C
HETATM 3292 C10 OLA A2418 30.910 181.432 39.196 1.00 68.27 C
HETATM 3293 C11 OLA A2418 30.622 182.872 38.829 1.00 75.45 C
HETATM 3294 C12 OLA A2418 29.440 182.989 37.847 1.00 83.41 C
HETATM 3295 C13 OLA A2418 29.732 183.899 36.636 1.00 82.00 C
HETATM 3296 C14 OLA A2418 28.472 184.563 36.056 1.00 73.12 C
HETATM 3297 C15 OLA A2418 28.433 186.093 36.235 1.00 65.54 C
HETATM 3298 C16 OLA A2418 27.763 186.542 37.545 1.00 65.64 C
HETATM 3299 C17 OLA A2418 26.276 186.897 37.385 1.00 67.58 C
HETATM 3300 C18 OLA A2418 25.982 188.370 37.707 1.00 62.74 C
HETATM 3301 C1 OLA A2419 35.345 171.472 33.819 1.00100.72 C
HETATM 3302 O1 OLA A2419 36.555 171.597 33.563 1.00 95.49 O
HETATM 3303 O2 OLA A2419 34.880 170.301 33.897 1.00102.02 O
HETATM 3304 C2 OLA A2419 34.475 172.696 34.032 1.00 93.25 C
HETATM 3305 C3 OLA A2419 34.282 173.514 32.752 1.00 76.41 C
HETATM 3306 C4 OLA A2419 34.478 175.012 32.959 1.00 74.29 C
HETATM 3307 C5 OLA A2419 33.180 175.791 33.056 1.00 70.81 C
HETATM 3308 C6 OLA A2419 33.336 177.300 33.206 1.00 65.19 C
HETATM 3309 C7 OLA A2419 32.048 178.037 32.842 1.00 61.63 C
HETATM 3310 C8 OLA A2419 31.925 179.451 33.383 1.00 53.45 C
HETATM 3311 C9 OLA A2419 30.565 180.007 32.982 1.00 63.43 C
HETATM 3312 C10 OLA A2419 30.105 181.262 33.194 1.00 60.92 C
HETATM 3313 C11 OLA A2419 30.890 182.356 33.887 1.00 58.21 C
HETATM 3314 C12 OLA A2419 30.596 183.747 33.287 1.00 69.21 C
HETATM 3315 C13 OLA A2419 31.758 184.749 33.448 1.00 70.12 C
HETATM 3316 C14 OLA A2419 31.826 185.801 32.328 1.00 70.00 C
HETATM 3317 C15 OLA A2419 33.262 186.172 31.907 1.00 65.49 C
HETATM 3318 C1 OLA A2420 33.880 197.997 26.895 1.00 88.11 C
HETATM 3319 O1 OLA A2420 34.893 198.224 26.178 1.00101.99 O
HETATM 3320 O2 OLA A2420 32.993 198.865 26.936 1.00 97.78 O
HETATM 3321 C2 OLA A2420 33.730 196.715 27.689 1.00 64.50 C
HETATM 3322 C3 OLA A2420 33.790 195.477 26.792 1.00 57.11 C
HETATM 3323 C4 OLA A2420 33.033 194.287 27.368 1.00 69.43 C
HETATM 3324 C5 OLA A2420 33.899 193.065 27.606 1.00 57.23 C
HETATM 3325 C6 OLA A2420 33.605 192.298 28.890 1.00 54.14 C
HETATM 3326 C7 OLA A2420 33.801 190.792 28.719 1.00 40.77 C
HETATM 3327 C8 OLA A2420 33.366 189.953 29.909 1.00 42.53 C
HETATM 3328 C9 OLA A2420 33.446 188.475 29.550 1.00 54.00 C
HETATM 3329 C3 OLA A2421 21.645 204.117 28.862 1.00 66.51 C
HETATM 3330 C4 OLA A2421 20.236 203.731 28.429 1.00 67.50 C
HETATM 3331 C5 OLA A2421 20.134 202.334 27.849 1.00 67.69 C
HETATM 3332 C6 OLA A2421 20.624 201.220 28.766 1.00 75.22 C
HETATM 3333 C7 OLA A2421 19.467 200.477 29.431 1.00 61.30 C
HETATM 3334 C8 OLA A2421 19.805 199.081 29.924 1.00 55.23 C
HETATM 3335 C9 OLA A2421 19.191 198.064 28.973 1.00 58.28 C
HETATM 3336 C10 OLA A2421 19.307 196.720 29.062 1.00 56.22 C
HETATM 3337 C11 OLA A2421 20.087 196.017 30.153 1.00 52.70 C
HETATM 3338 C1 OLA A2422 33.658 201.027 31.903 1.00113.91 C
HETATM 3339 O1 OLA A2422 34.420 201.742 31.195 1.00116.80 O
HETATM 3340 O2 OLA A2422 33.183 201.537 32.931 1.00120.14 O
HETATM 3341 C2 OLA A2422 33.322 199.597 31.525 1.00107.33 C
HETATM 3342 C3 OLA A2422 33.698 198.601 32.624 1.00103.65 C
HETATM 3343 C4 OLA A2422 35.159 198.170 32.571 1.00 99.82 C
HETATM 3344 C5 OLA A2422 35.349 196.750 32.079 1.00100.33 C
HETATM 3345 C6 OLA A2422 35.177 195.675 33.143 1.00 99.93 C
HETATM 3346 C7 OLA A2422 35.551 194.297 32.604 1.00 93.76 C
HETATM 3347 C8 OLA A2422 34.470 193.241 32.738 1.00 97.08 C
HETATM 3348 C9 OLA A2422 34.883 192.010 31.944 1.00 98.20 C
HETATM 3349 C10 OLA A2422 35.242 190.813 32.464 1.00 96.38 C
HETATM 3350 C11 OLA A2422 35.287 190.519 33.950 1.00 90.16 C
HETATM 3351 C12 OLA A2422 35.311 189.006 34.248 1.00 84.25 C
HETATM 3352 C1 OLA A2423 33.648 166.821 7.037 1.00104.78 C
HETATM 3353 O1 OLA A2423 32.407 166.897 7.034 1.00105.35 O
HETATM 3354 O2 OLA A2423 34.174 165.678 7.153 1.00110.66 O
HETATM 3355 C2 OLA A2423 34.490 168.075 6.905 1.00 95.74 C
HETATM 3356 C3 OLA A2423 34.634 168.810 8.241 1.00 83.56 C
HETATM 3357 C4 OLA A2423 34.743 170.324 8.100 1.00 76.15 C
HETATM 3358 C5 OLA A2423 35.952 170.770 7.299 1.00 76.09 C
HETATM 3359 C6 OLA A2423 35.980 172.251 6.938 1.00 70.53 C
HETATM 3360 C7 OLA A2423 36.559 172.493 5.544 1.00 70.50 C
HETATM 3361 C8 OLA A2423 36.633 173.951 5.125 1.00 55.05 C
HETATM 3362 C1 OLA A2424 42.120 165.042 13.299 1.00 90.85 C
HETATM 3363 O1 OLA A2424 43.112 164.378 12.949 1.00 91.40 O
HETATM 3364 O2 OLA A2424 41.261 164.489 14.044 1.00 98.70 O
HETATM 3365 C2 OLA A2424 41.960 166.475 12.833 1.00 74.37 C
HETATM 3366 C3 OLA A2424 41.178 167.328 13.837 1.00 70.77 C
HETATM 3367 C4 OLA A2424 40.634 168.623 13.244 1.00 69.94 C
HETATM 3368 C5 OLA A2424 41.164 169.875 13.914 1.00 64.19 C
HETATM 3369 C6 OLA A2424 40.290 171.112 13.744 1.00 73.61 C
HETATM 3370 C7 OLA A2424 40.995 172.202 12.937 1.00 69.56 C
HETATM 3371 C8 OLA A2424 40.901 173.607 13.508 1.00 62.35 C
HETATM 3372 C9 OLA A2424 41.211 174.605 12.400 1.00 69.98 C
HETATM 3373 C10 OLA A2424 41.821 175.804 12.546 1.00 71.14 C
HETATM 3374 C11 OLA A2424 42.299 176.349 13.875 1.00 64.04 C
HETATM 3375 C12 OLA A2424 43.470 177.338 13.710 1.00 71.81 C
HETATM 3376 C13 OLA A2424 43.056 178.707 13.132 1.00 68.51 C
HETATM 3377 C14 OLA A2424 43.616 179.897 13.928 1.00 56.98 C
HETATM 3378 C3 OLA A2425 18.049 196.379 3.387 1.00 74.63 C
HETATM 3379 C4 OLA A2425 17.206 195.111 3.323 1.00 79.46 C
HETATM 3380 C5 OLA A2425 18.027 193.837 3.306 1.00 77.16 C
HETATM 3381 C6 OLA A2425 17.790 192.901 4.485 1.00 76.44 C
HETATM 3382 C7 OLA A2425 16.881 191.733 4.107 1.00 80.71 C
HETATM 3383 C8 OLA A2425 16.028 191.182 5.237 1.00 75.61 C
HETATM 3384 C9 OLA A2425 15.110 190.097 4.690 1.00 73.08 C
HETATM 3385 C10 OLA A2425 15.250 188.764 4.880 1.00 70.90 C
HETATM 3386 C11 OLA A2425 16.373 188.145 5.687 1.00 58.26 C
HETATM 3387 C12 OLA A2425 16.639 186.679 5.296 1.00 45.24 C
HETATM 3388 C9 OLC A2426 3.323 183.079 24.724 1.00 80.04 C
HETATM 3389 C8 OLC A2426 4.109 181.814 24.523 1.00 78.16 C
HETATM 3390 C24 OLC A2426 1.923 168.411 25.427 1.00 79.23 C
HETATM 3391 C7 OLC A2426 3.793 180.626 25.474 1.00 65.68 C
HETATM 3392 C6 OLC A2426 3.251 179.357 24.772 1.00 60.02 C
HETATM 3393 C5 OLC A2426 3.152 178.097 25.669 1.00 58.46 C
HETATM 3394 C4 OLC A2426 3.070 176.763 24.891 1.00 68.76 C
HETATM 3395 C3 OLC A2426 2.858 175.520 25.779 1.00 62.60 C
HETATM 3396 C2 OLC A2426 2.426 174.247 25.014 1.00 63.35 C
HETATM 3397 C21 OLC A2426 2.605 170.823 25.550 1.00 71.06 C
HETATM 3398 C1 OLC A2426 2.296 173.105 25.989 1.00 78.18 C
HETATM 3399 C22 OLC A2426 1.835 169.705 26.282 1.00 76.47 C
HETATM 3400 O19 OLC A2426 2.624 173.129 27.162 1.00 94.49 O
HETATM 3401 O25 OLC A2426 2.647 167.518 26.228 1.00 76.36 O
HETATM 3402 O23 OLC A2426 2.490 169.489 27.491 1.00 81.69 O
HETATM 3403 O20 OLC A2426 1.758 171.956 25.479 1.00 72.06 O
HETATM 3404 C10 OLC A2427 5.495 181.813 28.915 1.00 91.42 C
HETATM 3405 C9 OLC A2427 4.780 180.675 28.952 1.00 87.32 C
HETATM 3406 C11 OLC A2427 5.598 182.809 27.798 1.00 78.40 C
HETATM 3407 C8 OLC A2427 4.684 179.688 30.083 1.00 73.05 C
HETATM 3408 C24 OLC A2427 6.177 168.283 27.892 1.00 87.64 C
HETATM 3409 C12 OLC A2427 6.118 184.216 28.177 1.00 70.82 C
HETATM 3410 C7 OLC A2427 3.824 178.423 29.843 1.00 71.46 C
HETATM 3411 C13 OLC A2427 5.352 185.384 27.502 1.00 73.70 C
HETATM 3412 C6 OLC A2427 4.455 177.101 30.330 1.00 79.42 C
HETATM 3413 C5 OLC A2427 3.835 175.812 29.710 1.00 75.47 C
HETATM 3414 C4 OLC A2427 2.978 174.966 30.683 1.00 74.32 C
HETATM 3415 C3 OLC A2427 2.966 173.472 30.350 1.00 71.10 C
HETATM 3416 C2 OLC A2427 3.737 172.591 31.351 1.00 84.44 C
HETATM 3417 C21 OLC A2427 5.169 170.186 29.176 1.00102.69 C
HETATM 3418 C1 OLC A2427 3.806 171.176 30.817 1.00 92.85 C
HETATM 3419 C22 OLC A2427 5.839 168.800 29.313 1.00 94.98 C
HETATM 3420 O19 OLC A2427 2.862 170.422 30.654 1.00 94.65 O
HETATM 3421 O25 OLC A2427 7.338 167.520 28.079 1.00 87.06 O
HETATM 3422 O23 OLC A2427 7.026 168.984 30.022 1.00 98.35 O
HETATM 3423 O20 OLC A2427 5.059 170.737 30.483 1.00101.64 O
HETATM 3424 C10 OLC A2428 37.550 176.612 14.825 1.00 62.10 C
HETATM 3425 C9 OLC A2428 36.943 175.495 15.241 1.00 49.46 C
HETATM 3426 C11 OLC A2428 38.197 177.660 15.671 1.00 55.06 C
HETATM 3427 C8 OLC A2428 36.751 175.052 16.650 1.00 51.89 C
HETATM 3428 C24 OLC A2428 39.072 163.142 20.009 1.00106.62 C
HETATM 3429 C12 OLC A2428 38.688 178.939 14.948 1.00 64.66 C
HETATM 3430 C7 OLC A2428 37.594 173.852 17.140 1.00 62.88 C
HETATM 3431 C13 OLC A2428 39.154 180.068 15.910 1.00 71.90 C
HETATM 3432 C6 OLC A2428 37.041 172.471 16.743 1.00 63.72 C
HETATM 3433 C5 OLC A2428 37.440 171.310 17.686 1.00 64.35 C
HETATM 3434 C4 OLC A2428 38.331 170.226 17.041 1.00 65.37 C
HETATM 3435 C3 OLC A2428 38.350 168.907 17.824 1.00 63.56 C
HETATM 3436 C2 OLC A2428 38.926 167.705 17.065 1.00 71.04 C
HETATM 3437 C21 OLC A2428 38.485 164.203 17.814 1.00 95.39 C
HETATM 3438 C1 OLC A2428 38.889 166.507 17.976 1.00 83.88 C
HETATM 3439 C22 OLC A2428 39.448 163.210 18.495 1.00108.14 C
HETATM 3440 O19 OLC A2428 38.572 166.515 19.154 1.00 92.67 O
HETATM 3441 O25 OLC A2428 39.162 161.780 20.327 1.00108.21 O
HETATM 3442 O23 OLC A2428 39.240 161.964 17.903 1.00113.69 O
HETATM 3443 O20 OLC A2428 39.252 165.324 17.401 1.00 88.21 O
HETATM 3444 C10 OLC A2429 33.437 191.213 23.117 1.00 61.65 C
HETATM 3445 C9 OLC A2429 33.301 192.479 22.692 1.00 53.75 C
HETATM 3446 C11 OLC A2429 33.379 190.687 24.521 1.00 58.62 C
HETATM 3447 C8 OLC A2429 33.047 193.700 23.510 1.00 43.49 C
HETATM 3448 C24 OLC A2429 32.643 205.884 25.672 1.00101.29 C
HETATM 3449 C12 OLC A2429 33.306 189.150 24.662 1.00 50.56 C
HETATM 3450 C7 OLC A2429 33.644 195.026 22.984 1.00 57.85 C
HETATM 3451 C13 OLC A2429 34.373 188.402 23.829 1.00 53.74 C
HETATM 3452 C6 OLC A2429 32.713 195.841 22.060 1.00 56.18 C
HETATM 3453 C14 OLC A2429 34.451 186.874 24.088 1.00 66.20 C
HETATM 3454 C5 OLC A2429 31.866 196.899 22.794 1.00 55.90 C
HETATM 3455 C4 OLC A2429 31.900 198.315 22.185 1.00 47.94 C
HETATM 3456 C3 OLC A2429 31.596 199.415 23.214 1.00 52.38 C
HETATM 3457 C2 OLC A2429 31.750 200.857 22.701 1.00 67.20 C
HETATM 3458 C21 OLC A2429 32.575 203.496 24.914 1.00 96.28 C
HETATM 3459 C1 OLC A2429 32.748 201.582 23.571 1.00 87.93 C
HETATM 3460 C22 OLC A2429 33.425 204.781 24.900 1.00100.56 C
HETATM 3461 O19 OLC A2429 33.635 201.065 24.229 1.00 90.70 O
HETATM 3462 O25 OLC A2429 33.567 206.376 26.605 1.00106.93 O
HETATM 3463 O23 OLC A2429 34.607 204.491 25.581 1.00106.86 O
HETATM 3464 O20 OLC A2429 32.614 202.941 23.607 1.00 97.32 O
HETATM 3465 C10 OLC A2430 36.841 190.641 18.851 1.00 68.01 C
HETATM 3466 C9 OLC A2430 35.683 191.319 18.841 1.00 56.94 C
HETATM 3467 C11 OLC A2430 37.239 189.516 19.760 1.00 78.01 C
HETATM 3468 C8 OLC A2430 35.289 192.442 17.941 1.00 49.62 C
HETATM 3469 C24 OLC A2430 33.797 204.739 20.747 1.00105.50 C
HETATM 3470 C7 OLC A2430 34.887 193.768 18.639 1.00 50.56 C
HETATM 3471 C6 OLC A2430 35.213 195.045 17.847 1.00 50.49 C
HETATM 3472 C5 OLC A2430 34.896 196.359 18.585 1.00 57.91 C
HETATM 3473 C4 OLC A2430 36.044 197.386 18.564 1.00 70.50 C
HETATM 3474 C3 OLC A2430 35.729 198.636 17.739 1.00 71.51 C
HETATM 3475 C2 OLC A2430 36.165 199.951 18.386 1.00 78.74 C
HETATM 3476 C21 OLC A2430 34.051 202.769 19.224 1.00 98.70 C
HETATM 3477 C1 OLC A2430 35.103 200.984 18.130 1.00 93.27 C
HETATM 3478 C22 OLC A2430 34.342 204.273 19.370 1.00103.72 C
HETATM 3479 O19 OLC A2430 34.146 200.859 17.386 1.00 99.86 O
HETATM 3480 O25 OLC A2430 34.228 206.070 20.853 1.00106.52 O
HETATM 3481 O23 OLC A2430 35.728 204.412 19.363 1.00108.47 O
HETATM 3482 O20 OLC A2430 35.259 202.153 18.810 1.00 98.62 O
HETATM 3483 O1 TAR A2431 19.205 168.137 32.697 0.50126.39 O
HETATM 3484 O11 TAR A2431 17.245 168.914 33.257 0.50121.45 O1-
HETATM 3485 C1 TAR A2431 18.402 168.537 33.580 0.50124.26 C
HETATM 3486 C2 TAR A2431 18.830 168.566 35.031 0.50124.25 C
HETATM 3487 O2 TAR A2431 18.317 167.412 35.656 0.50123.11 O
HETATM 3488 C3 TAR A2431 20.334 168.555 35.197 0.50124.27 C
HETATM 3489 O3 TAR A2431 20.837 167.402 34.562 0.50123.19 O
HETATM 3490 C4 TAR A2431 20.762 168.511 36.648 0.50124.34 C
HETATM 3491 O4 TAR A2431 21.921 168.880 36.974 0.50121.76 O
HETATM 3492 O41 TAR A2431 19.960 168.101 37.527 0.50126.63 O1-
HETATM 3493 O HOH A2501 18.869 191.678 13.385 1.00 61.05 O
HETATM 3494 O HOH A2502 25.189 173.119 13.320 1.00 35.30 O
HETATM 3495 O HOH A2503 28.602 171.071 35.715 1.00 88.05 O
HETATM 3496 O HOH A2504 24.552 174.927 15.403 1.00 65.01 O
HETATM 3497 O HOH A2505 14.705 177.450 22.043 1.00 41.52 O
HETATM 3498 O HOH A2506 24.590 196.332 14.460 1.00 60.84 O
HETATM 3499 O HOH A2507 19.200 182.317 22.638 1.00 26.77 O
HETATM 3500 O HOH A2508 25.446 178.251 15.729 1.00 53.05 O
HETATM 3501 O HOH A2509 16.058 180.032 12.714 1.00 52.94 O
HETATM 3502 O HOH A2510 30.924 210.393 0.816 1.00 57.61 O
HETATM 3503 O HOH A2511 23.775 191.693 12.010 1.00 65.84 O
HETATM 3504 O HOH A2512 28.185 178.073 19.972 1.00 40.35 O
HETATM 3505 O HOH A2513 25.339 175.263 18.891 1.00 44.19 O
HETATM 3506 O HOH A2514 22.032 187.392 15.779 1.00 42.16 O
HETATM 3507 O HOH A2515 16.358 197.498 19.421 1.00 52.21 O
HETATM 3508 O HOH A2516 -18.913 239.880 26.319 1.00 77.86 O
HETATM 3509 O HOH A2517 25.815 192.775 21.427 1.00 27.34 O
HETATM 3510 O HOH A2518 25.244 194.054 13.650 1.00 49.71 O
HETATM 3511 O HOH A2519 27.626 177.377 16.953 1.00 34.32 O
HETATM 3512 O HOH A2520 27.750 160.096 22.837 1.00 58.07 O
HETATM 3513 O HOH A2521 21.030 191.985 15.315 1.00 66.67 O
HETATM 3514 O HOH A2522 17.855 183.440 20.710 1.00 51.36 O
HETATM 3515 O HOH A2523 26.137 162.007 22.647 1.00 71.06 O
HETATM 3516 O HOH A2524 26.974 191.868 6.918 1.00 48.38 O
HETATM 3517 O HOH A2525 10.868 168.799 15.659 1.00 46.43 O
HETATM 3518 O HOH A2526 20.575 183.190 24.624 1.00 49.84 O
HETATM 3519 O HOH A2527 25.787 161.636 24.958 1.00 59.07 O
HETATM 3520 O HOH A2528 24.887 168.653 16.925 1.00 44.56 O
HETATM 3521 O HOH A2529 23.979 163.895 2.095 1.00 59.21 O
HETATM 3522 O HOH A2530 25.797 192.666 25.775 1.00 61.70 O
HETATM 3523 O HOH A2531 23.094 185.653 14.507 1.00 41.75 O
HETATM 3524 O HOH A2532 27.593 174.796 17.812 1.00 52.10 O
HETATM 3525 O HOH A2533 17.091 167.204 26.409 1.00 40.76 O
HETATM 3526 O HOH A2534 24.252 187.288 17.135 1.00 48.95 O
HETATM 3527 O HOH A2535 25.546 195.339 25.388 1.00 54.86 O
HETATM 3528 O HOH A2536 26.992 161.721 14.140 1.00 67.64 O
HETATM 3529 O HOH A2537 14.796 168.074 28.598 1.00 46.99 O
CONECT 397 2995
CONECT 533 1181
CONECT 549 1090
CONECT 569 1225
CONECT 674 2995
CONECT 1090 549
CONECT 1181 533
CONECT 1225 569
CONECT 2604 2625
CONECT 2625 2604
CONECT 2995 397 674 3506 3526
CONECT 2996 3016 3017
CONECT 2997 2998 3015 3020
CONECT 2998 2997 3007 3019
CONECT 2999 3000 3019 3020
CONECT 3000 2999 3002 3005 3021
CONECT 3001 3002 3022
CONECT 3002 3000 3001 3003
CONECT 3003 3002 3004
CONECT 3004 3003 3005 3006
CONECT 3005 3000 3004
CONECT 3006 3004 3022
CONECT 3007 2998 3012 3023
CONECT 3008 3009
CONECT 3009 3008 3010
CONECT 3010 3009 3011
CONECT 3011 3010 3012
CONECT 3012 3007 3011 3013
CONECT 3013 3012 3014 3015
CONECT 3014 3013
CONECT 3015 2997 3013 3016
CONECT 3016 2996 3015
CONECT 3017 2996 3018
CONECT 3018 3017
CONECT 3019 2998 2999
CONECT 3020 2997 2999
CONECT 3021 3000 3022
CONECT 3022 3001 3006 3021
CONECT 3023 3007
CONECT 3024 3025 3033
CONECT 3025 3024 3026
CONECT 3026 3025 3027 3051
CONECT 3027 3026 3028
CONECT 3028 3027 3029 3033
CONECT 3029 3028 3030
CONECT 3030 3029 3031
CONECT 3031 3030 3032 3037
CONECT 3032 3031 3033 3034
CONECT 3033 3024 3028 3032 3042
CONECT 3034 3032 3035
CONECT 3035 3034 3036
CONECT 3036 3035 3037 3040 3041
CONECT 3037 3031 3036 3038
CONECT 3038 3037 3039
CONECT 3039 3038 3040
CONECT 3040 3036 3039 3043
CONECT 3041 3036
CONECT 3042 3033
CONECT 3043 3040 3044 3045
CONECT 3044 3043
CONECT 3045 3043 3046
CONECT 3046 3045 3047
CONECT 3047 3046 3048
CONECT 3048 3047 3049 3050
CONECT 3049 3048
CONECT 3050 3048
CONECT 3051 3026
CONECT 3052 3053 3061
CONECT 3053 3052 3054
CONECT 3054 3053 3055 3079
CONECT 3055 3054 3056
CONECT 3056 3055 3057 3061
CONECT 3057 3056 3058
CONECT 3058 3057 3059
CONECT 3059 3058 3060 3065
CONECT 3060 3059 3061 3062
CONECT 3061 3052 3056 3060 3070
CONECT 3062 3060 3063
CONECT 3063 3062 3064
CONECT 3064 3063 3065 3068 3069
CONECT 3065 3059 3064 3066
CONECT 3066 3065 3067
CONECT 3067 3066 3068
CONECT 3068 3064 3067 3071
CONECT 3069 3064
CONECT 3070 3061
CONECT 3071 3068 3072 3073
CONECT 3072 3071
CONECT 3073 3071 3074
CONECT 3074 3073 3075
CONECT 3075 3074 3076
CONECT 3076 3075 3077 3078
CONECT 3077 3076
CONECT 3078 3076
CONECT 3079 3054
CONECT 3080 3081 3089
CONECT 3081 3080 3082
CONECT 3082 3081 3083 3107
CONECT 3083 3082 3084
CONECT 3084 3083 3085 3089
CONECT 3085 3084 3086
CONECT 3086 3085 3087
CONECT 3087 3086 3088 3093
CONECT 3088 3087 3089 3090
CONECT 3089 3080 3084 3088 3098
CONECT 3090 3088 3091
CONECT 3091 3090 3092
CONECT 3092 3091 3093 3096 3097
CONECT 3093 3087 3092 3094
CONECT 3094 3093 3095
CONECT 3095 3094 3096
CONECT 3096 3092 3095 3099
CONECT 3097 3092
CONECT 3098 3089
CONECT 3099 3096 3100 3101
CONECT 3100 3099
CONECT 3101 3099 3102
CONECT 3102 3101 3103
CONECT 3103 3102 3104
CONECT 3104 3103 3105 3106
CONECT 3105 3104
CONECT 3106 3104
CONECT 3107 3082
CONECT 3108 3109 3110 3111
CONECT 3109 3108
CONECT 3110 3108
CONECT 3111 3108 3112
CONECT 3112 3111 3113
CONECT 3113 3112 3114
CONECT 3114 3113 3115
CONECT 3115 3114 3116
CONECT 3116 3115 3117
CONECT 3117 3116 3118
CONECT 3118 3117 3119
CONECT 3119 3118 3120
CONECT 3120 3119 3121
CONECT 3121 3120 3122
CONECT 3122 3121 3123
CONECT 3123 3122 3124
CONECT 3124 3123 3125
CONECT 3125 3124 3126
CONECT 3126 3125 3127
CONECT 3127 3126
CONECT 3128 3129 3130 3131
CONECT 3129 3128
CONECT 3130 3128
CONECT 3131 3128 3132
CONECT 3132 3131 3133
CONECT 3133 3132 3134
CONECT 3134 3133 3135
CONECT 3135 3134 3136
CONECT 3136 3135 3137
CONECT 3137 3136 3138
CONECT 3138 3137 3139
CONECT 3139 3138 3140
CONECT 3140 3139 3141
CONECT 3141 3140 3142
CONECT 3142 3141
CONECT 3143 3144 3145 3146
CONECT 3144 3143
CONECT 3145 3143
CONECT 3146 3143 3147
CONECT 3147 3146 3148
CONECT 3148 3147 3149
CONECT 3149 3148 3150
CONECT 3150 3149 3151
CONECT 3151 3150 3152
CONECT 3152 3151 3153
CONECT 3153 3152 3154
CONECT 3154 3153 3155
CONECT 3155 3154 3156
CONECT 3156 3155
CONECT 3157 3158 3159 3160
CONECT 3158 3157
CONECT 3159 3157
CONECT 3160 3157 3161
CONECT 3161 3160 3162
CONECT 3162 3161 3163
CONECT 3163 3162 3164
CONECT 3164 3163 3165
CONECT 3165 3164 3166
CONECT 3166 3165 3167
CONECT 3167 3166
CONECT 3168 3169
CONECT 3169 3168 3170
CONECT 3170 3169 3171
CONECT 3171 3170 3172
CONECT 3172 3171 3173
CONECT 3173 3172 3174
CONECT 3174 3173
CONECT 3175 3176 3177 3178
CONECT 3176 3175
CONECT 3177 3175
CONECT 3178 3175 3179
CONECT 3179 3178 3180
CONECT 3180 3179 3181
CONECT 3181 3180 3182
CONECT 3182 3181 3183
CONECT 3183 3182 3184
CONECT 3184 3183 3185
CONECT 3185 3184 3186
CONECT 3186 3185 3187
CONECT 3187 3186 3188
CONECT 3188 3187 3189
CONECT 3189 3188 3190
CONECT 3190 3189 3191
CONECT 3191 3190
CONECT 3192 3193 3194 3195
CONECT 3193 3192
CONECT 3194 3192
CONECT 3195 3192 3196
CONECT 3196 3195 3197
CONECT 3197 3196 3198
CONECT 3198 3197 3199
CONECT 3199 3198 3200
CONECT 3200 3199 3201
CONECT 3201 3200 3202
CONECT 3202 3201 3203
CONECT 3203 3202 3204
CONECT 3204 3203 3205
CONECT 3205 3204 3206
CONECT 3206 3205 3207
CONECT 3207 3206 3208
CONECT 3208 3207 3209
CONECT 3209 3208 3210
CONECT 3210 3209 3211
CONECT 3211 3210
CONECT 3212 3213
CONECT 3213 3212 3214
CONECT 3214 3213 3215
CONECT 3215 3214 3216
CONECT 3216 3215 3217
CONECT 3217 3216 3218
CONECT 3218 3217
CONECT 3219 3220 3221 3222
CONECT 3220 3219
CONECT 3221 3219
CONECT 3222 3219 3223
CONECT 3223 3222 3224
CONECT 3224 3223 3225
CONECT 3225 3224 3226
CONECT 3226 3225
CONECT 3227 3228
CONECT 3228 3227 3229
CONECT 3229 3228 3230
CONECT 3230 3229 3231
CONECT 3231 3230 3232
CONECT 3232 3231 3233
CONECT 3233 3232 3234
CONECT 3234 3233 3235
CONECT 3235 3234
CONECT 3236 3237 3238 3239
CONECT 3237 3236
CONECT 3238 3236
CONECT 3239 3236 3240
CONECT 3240 3239 3241
CONECT 3241 3240 3242
CONECT 3242 3241 3243
CONECT 3243 3242 3244
CONECT 3244 3243 3245
CONECT 3245 3244 3246
CONECT 3246 3245 3247
CONECT 3247 3246 3248
CONECT 3248 3247 3249
CONECT 3249 3248
CONECT 3250 3251 3252 3253
CONECT 3251 3250
CONECT 3252 3250
CONECT 3253 3250 3254
CONECT 3254 3253 3255
CONECT 3255 3254 3256
CONECT 3256 3255 3257
CONECT 3257 3256 3258
CONECT 3258 3257 3259
CONECT 3259 3258 3260
CONECT 3260 3259 3261
CONECT 3261 3260 3262
CONECT 3262 3261 3263
CONECT 3263 3262 3264
CONECT 3264 3263 3265
CONECT 3265 3264 3266
CONECT 3266 3265
CONECT 3267 3268 3269 3270
CONECT 3268 3267
CONECT 3269 3267
CONECT 3270 3267 3271
CONECT 3271 3270 3272
CONECT 3272 3271 3273
CONECT 3273 3272 3274
CONECT 3274 3273 3275
CONECT 3275 3274 3276
CONECT 3276 3275 3277
CONECT 3277 3276 3278
CONECT 3278 3277 3279
CONECT 3279 3278 3280
CONECT 3280 3279
CONECT 3281 3282 3283 3284
CONECT 3282 3281
CONECT 3283 3281
CONECT 3284 3281 3285
CONECT 3285 3284 3286
CONECT 3286 3285 3287
CONECT 3287 3286 3288
CONECT 3288 3287 3289
CONECT 3289 3288 3290
CONECT 3290 3289 3291
CONECT 3291 3290 3292
CONECT 3292 3291 3293
CONECT 3293 3292 3294
CONECT 3294 3293 3295
CONECT 3295 3294 3296
CONECT 3296 3295 3297
CONECT 3297 3296 3298
CONECT 3298 3297 3299
CONECT 3299 3298 3300
CONECT 3300 3299
CONECT 3301 3302 3303 3304
CONECT 3302 3301
CONECT 3303 3301
CONECT 3304 3301 3305
CONECT 3305 3304 3306
CONECT 3306 3305 3307
CONECT 3307 3306 3308
CONECT 3308 3307 3309
CONECT 3309 3308 3310
CONECT 3310 3309 3311
CONECT 3311 3310 3312
CONECT 3312 3311 3313
CONECT 3313 3312 3314
CONECT 3314 3313 3315
CONECT 3315 3314 3316
CONECT 3316 3315 3317
CONECT 3317 3316
CONECT 3318 3319 3320 3321
CONECT 3319 3318
CONECT 3320 3318
CONECT 3321 3318 3322
CONECT 3322 3321 3323
CONECT 3323 3322 3324
CONECT 3324 3323 3325
CONECT 3325 3324 3326
CONECT 3326 3325 3327
CONECT 3327 3326 3328
CONECT 3328 3327
CONECT 3329 3330
CONECT 3330 3329 3331
CONECT 3331 3330 3332
CONECT 3332 3331 3333
CONECT 3333 3332 3334
CONECT 3334 3333 3335
CONECT 3335 3334 3336
CONECT 3336 3335 3337
CONECT 3337 3336
CONECT 3338 3339 3340 3341
CONECT 3339 3338
CONECT 3340 3338
CONECT 3341 3338 3342
CONECT 3342 3341 3343
CONECT 3343 3342 3344
CONECT 3344 3343 3345
CONECT 3345 3344 3346
CONECT 3346 3345 3347
CONECT 3347 3346 3348
CONECT 3348 3347 3349
CONECT 3349 3348 3350
CONECT 3350 3349 3351
CONECT 3351 3350
CONECT 3352 3353 3354 3355
CONECT 3353 3352
CONECT 3354 3352
CONECT 3355 3352 3356
CONECT 3356 3355 3357
CONECT 3357 3356 3358
CONECT 3358 3357 3359
CONECT 3359 3358 3360
CONECT 3360 3359 3361
CONECT 3361 3360
CONECT 3362 3363 3364 3365
CONECT 3363 3362
CONECT 3364 3362
CONECT 3365 3362 3366
CONECT 3366 3365 3367
CONECT 3367 3366 3368
CONECT 3368 3367 3369
CONECT 3369 3368 3370
CONECT 3370 3369 3371
CONECT 3371 3370 3372
CONECT 3372 3371 3373
CONECT 3373 3372 3374
CONECT 3374 3373 3375
CONECT 3375 3374 3376
CONECT 3376 3375 3377
CONECT 3377 3376
CONECT 3378 3379
CONECT 3379 3378 3380
CONECT 3380 3379 3381
CONECT 3381 3380 3382
CONECT 3382 3381 3383
CONECT 3383 3382 3384
CONECT 3384 3383 3385
CONECT 3385 3384 3386
CONECT 3386 3385 3387
CONECT 3387 3386
CONECT 3388 3389
CONECT 3389 3388 3391
CONECT 3390 3399 3401
CONECT 3391 3389 3392
CONECT 3392 3391 3393
CONECT 3393 3392 3394
CONECT 3394 3393 3395
CONECT 3395 3394 3396
CONECT 3396 3395 3398
CONECT 3397 3399 3403
CONECT 3398 3396 3400 3403
CONECT 3399 3390 3397 3402
CONECT 3400 3398
CONECT 3401 3390
CONECT 3402 3399
CONECT 3403 3397 3398
CONECT 3404 3405 3406
CONECT 3405 3404 3407
CONECT 3406 3404 3409
CONECT 3407 3405 3410
CONECT 3408 3419 3421
CONECT 3409 3406 3411
CONECT 3410 3407 3412
CONECT 3411 3409
CONECT 3412 3410 3413
CONECT 3413 3412 3414
CONECT 3414 3413 3415
CONECT 3415 3414 3416
CONECT 3416 3415 3418
CONECT 3417 3419 3423
CONECT 3418 3416 3420 3423
CONECT 3419 3408 3417 3422
CONECT 3420 3418
CONECT 3421 3408
CONECT 3422 3419
CONECT 3423 3417 3418
CONECT 3424 3425 3426
CONECT 3425 3424 3427
CONECT 3426 3424 3429
CONECT 3427 3425 3430
CONECT 3428 3439 3441
CONECT 3429 3426 3431
CONECT 3430 3427 3432
CONECT 3431 3429
CONECT 3432 3430 3433
CONECT 3433 3432 3434
CONECT 3434 3433 3435
CONECT 3435 3434 3436
CONECT 3436 3435 3438
CONECT 3437 3439 3443
CONECT 3438 3436 3440 3443
CONECT 3439 3428 3437 3442
CONECT 3440 3438
CONECT 3441 3428
CONECT 3442 3439
CONECT 3443 3437 3438
CONECT 3444 3445 3446
CONECT 3445 3444 3447
CONECT 3446 3444 3449
CONECT 3447 3445 3450
CONECT 3448 3460 3462
CONECT 3449 3446 3451
CONECT 3450 3447 3452
CONECT 3451 3449 3453
CONECT 3452 3450 3454
CONECT 3453 3451
CONECT 3454 3452 3455
CONECT 3455 3454 3456
CONECT 3456 3455 3457
CONECT 3457 3456 3459
CONECT 3458 3460 3464
CONECT 3459 3457 3461 3464
CONECT 3460 3448 3458 3463
CONECT 3461 3459
CONECT 3462 3448
CONECT 3463 3460
CONECT 3464 3458 3459
CONECT 3465 3466 3467
CONECT 3466 3465 3468
CONECT 3467 3465
CONECT 3468 3466 3470
CONECT 3469 3478 3480
CONECT 3470 3468 3471
CONECT 3471 3470 3472
CONECT 3472 3471 3473
CONECT 3473 3472 3474
CONECT 3474 3473 3475
CONECT 3475 3474 3477
CONECT 3476 3478 3482
CONECT 3477 3475 3479 3482
CONECT 3478 3469 3476 3481
CONECT 3479 3477
CONECT 3480 3469
CONECT 3481 3478
CONECT 3482 3476 3477
CONECT 3483 3485
CONECT 3484 3485
CONECT 3485 3483 3484 3486
CONECT 3486 3485 3487 3488
CONECT 3487 3486
CONECT 3488 3486 3489 3490
CONECT 3489 3488
CONECT 3490 3488 3491 3492
CONECT 3491 3490
CONECT 3492 3490
CONECT 3506 2995
CONECT 3526 2995
MASTER 522 0 32 21 2 0 46 6 3528 1 510 34
END