HEADER MEMBRANE PROTEIN 23-JAN-18 6FK8
TITLE CRYSTAL STRUCTURE OF N2C/D282C STABILIZED OPSIN BOUND TO RS08
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RHODOPSIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-326;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: RHO;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCMV-TET O
KEYWDS RHODOPSIN, G PROTEIN-COUPLED RECEPTORS, RETINITIS PIGMENTOSA,
KEYWDS 2 SIGNALING PROTEIN, SENSORY TRANSDUCTION, PHOTORECEPTOR PROTEIN,
KEYWDS 3 KINTEGRAL MEMBRANE PROTEIN, VISION, MEMBRANE, RECEPTOR, TRANSDUCER
KEYWDS 4 PHOTORECEPTOR, SMALL MOLECULE COMPLEX, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.MATTLE,J.STANDFUSS,R.DAWSON
REVDAT 3 29-JUL-20 6FK8 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 11-APR-18 6FK8 1 JRNL
REVDAT 1 04-APR-18 6FK8 0
JRNL AUTH D.MATTLE,B.KUHN,J.AEBI,M.BEDOUCHA,D.KEKILLI,N.GROZINGER,
JRNL AUTH 2 A.ALKER,M.G.RUDOLPH,G.SCHMID,G.F.X.SCHERTLER,M.HENNIG,
JRNL AUTH 3 J.STANDFUSS,R.J.P.DAWSON
JRNL TITL LIGAND CHANNEL IN PHARMACOLOGICALLY STABILIZED RHODOPSIN.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 3640 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 29555765
JRNL DOI 10.1073/PNAS.1718084115
REMARK 2
REMARK 2 RESOLUTION. 2.87 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 28426
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.220
REMARK 3 FREE R VALUE TEST SET COUNT : 1483
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 47.4145 - 6.3783 1.00 2535 131 0.2217 0.2109
REMARK 3 2 6.3783 - 5.0645 1.00 2470 149 0.2275 0.2442
REMARK 3 3 5.0645 - 4.4248 1.00 2443 142 0.1866 0.2278
REMARK 3 4 4.4248 - 4.0205 1.00 2472 130 0.1885 0.2194
REMARK 3 5 4.0205 - 3.7325 1.00 2449 131 0.2082 0.2104
REMARK 3 6 3.7325 - 3.5125 1.00 2436 130 0.2312 0.2382
REMARK 3 7 3.5125 - 3.3366 1.00 2454 132 0.2487 0.2880
REMARK 3 8 3.3366 - 3.1914 1.00 2435 133 0.2854 0.3008
REMARK 3 9 3.1914 - 3.0686 1.00 2422 127 0.3278 0.3818
REMARK 3 10 3.0686 - 2.9627 1.00 2431 137 0.3606 0.4382
REMARK 3 11 2.9627 - 2.8701 0.99 2396 141 0.3721 0.4159
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.410
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 : 0.009 2827
REMARK 3 ANGLE : 1.253 3853
REMARK 3 CHIRALITY : 0.068 443
REMARK 3 PLANARITY : 0.008 459
REMARK 3 DIHEDRAL : 13.920 1650
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 27.9754 389.1563 39.0769
REMARK 3 T TENSOR
REMARK 3 T11: 0.4265 T22: 0.5314
REMARK 3 T33: 0.7398 T12: 0.0420
REMARK 3 T13: 0.1173 T23: 0.0726
REMARK 3 L TENSOR
REMARK 3 L11: 1.8019 L22: 3.8798
REMARK 3 L33: 1.4290 L12: -1.1533
REMARK 3 L13: 0.1205 L23: -0.0648
REMARK 3 S TENSOR
REMARK 3 S11: 0.0870 S12: 0.2095 S13: 0.1114
REMARK 3 S21: -0.2679 S22: -0.1133 S23: -0.3453
REMARK 3 S31: -0.0598 S32: 0.0638 S33: 0.0055
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 6FK8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1200008389.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS (VERSION OCT 15
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28482
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.870
REMARK 200 RESOLUTION RANGE LOW (A) : 45.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.50
REMARK 200 R MERGE (I) : 0.19260
REMARK 200 R SYM (I) : 0.19260
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.2800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.87
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.50
REMARK 200 R MERGE FOR SHELL (I) : 3.53100
REMARK 200 R SYM FOR SHELL (I) : 3.53100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.720
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 4J4Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 84.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 8.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SEE PUBLICATION, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 121.09150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.91221
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 36.98900
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 121.09150
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 69.91221
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 36.98900
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 121.09150
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 69.91221
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 36.98900
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 121.09150
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 69.91221
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 36.98900
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 121.09150
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 69.91221
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 36.98900
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 121.09150
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 69.91221
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 36.98900
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 139.82442
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 73.97800
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 139.82442
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 73.97800
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 139.82442
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 73.97800
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 139.82442
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 73.97800
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 139.82442
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 73.97800
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 139.82442
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 73.97800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 O ACE A 0 LIES ON A SPECIAL POSITION.
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 PRO A 327
REMARK 465 LEU A 328
REMARK 465 GLY A 329
REMARK 465 ASP A 330
REMARK 465 ASP A 331
REMARK 465 GLU A 332
REMARK 465 ALA A 333
REMARK 465 SER A 334
REMARK 465 THR A 335
REMARK 465 THR A 336
REMARK 465 VAL A 337
REMARK 465 SER A 338
REMARK 465 LYS A 339
REMARK 465 THR A 340
REMARK 465 GLU A 341
REMARK 465 THR A 342
REMARK 465 SER A 343
REMARK 465 GLN A 344
REMARK 465 VAL A 345
REMARK 465 ALA A 346
REMARK 465 PRO A 347
REMARK 465 ALA A 348
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 C ACE A 0 O ACE A 0 16455 1.26
REMARK 500 O ACE A 0 CH3 ACE A 0 16455 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 MET A 1 CA - CB - CG ANGL. DEV. = -10.3 DEGREES
REMARK 500 TYR A 274 CB - CG - CD2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 TYR A 274 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
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 GLN A 28 45.23 -95.19
REMARK 500 ALA A 32 143.06 -172.75
REMARK 500 LYS A 141 67.59 38.46
REMARK 500 SER A 176 -156.24 64.50
REMARK 500 PRO A 194 52.54 -92.46
REMARK 500 PHE A 212 -49.33 -136.52
REMARK 500 HIS A 278 40.01 35.28
REMARK 500 PHE A 287 -176.11 93.98
REMARK 500 MET A 288 6.98 -68.79
REMARK 500 ILE A 307 -58.38 -122.89
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6FK8 A 1 348 UNP P02699 OPSD_BOVIN 1 348
SEQADV 6FK8 ACE A 0 UNP P02699 ACETYLATION
SEQADV 6FK8 CYS A 2 UNP P02699 ASN 2 CONFLICT
SEQADV 6FK8 CYS A 282 UNP P02699 ASP 282 CONFLICT
SEQRES 1 A 349 ACE MET CYS GLY THR GLU GLY PRO ASN PHE TYR VAL PRO
SEQRES 2 A 349 PHE SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU
SEQRES 3 A 349 ALA PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER
SEQRES 4 A 349 MET LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY
SEQRES 5 A 349 PHE PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN
SEQRES 6 A 349 HIS LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU
SEQRES 7 A 349 ASN LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY
SEQRES 8 A 349 PHE THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE
SEQRES 9 A 349 VAL PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE
SEQRES 10 A 349 ALA THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL
SEQRES 11 A 349 VAL LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO
SEQRES 12 A 349 MET SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET
SEQRES 13 A 349 GLY VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA
SEQRES 14 A 349 ALA PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU
SEQRES 15 A 349 GLY MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO
SEQRES 16 A 349 HIS GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET
SEQRES 17 A 349 PHE VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE
SEQRES 18 A 349 PHE CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA
SEQRES 19 A 349 ALA ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA
SEQRES 20 A 349 GLU LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE
SEQRES 21 A 349 ALA PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA
SEQRES 22 A 349 PHE TYR ILE PHE THR HIS GLN GLY SER CYS PHE GLY PRO
SEQRES 23 A 349 ILE PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER
SEQRES 24 A 349 ALA VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS
SEQRES 25 A 349 GLN PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY
SEQRES 26 A 349 LYS ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL
SEQRES 27 A 349 SER LYS THR GLU THR SER GLN VAL ALA PRO ALA
HET ACE A 0 3
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET MAN B 4 11
HET MAN B 5 11
HET PLM A 401 17
HET DNZ A 407 27
HET BOG A 408 20
HET BOG A 409 20
HETNAM ACE ACETYL GROUP
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM PLM PALMITIC ACID
HETNAM DNZ (2~{R},3~{S})-3-AZANYL-2-(4-CHLOROPHENYL)-1-SPIRO[1,3-
HETNAM 2 DNZ BENZODIOXOLE-2,4'-PIPERIDINE]-1'-YL-BUTAN-1-ONE
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
FORMUL 1 ACE C2 H4 O
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 2 BMA C6 H12 O6
FORMUL 2 MAN 2(C6 H12 O6)
FORMUL 3 PLM C16 H32 O2
FORMUL 4 DNZ C21 H23 CL N2 O3
FORMUL 5 BOG 2(C14 H28 O6)
HELIX 1 AA1 GLU A 33 HIS A 65 1 33
HELIX 2 AA2 LYS A 66 ARG A 69 5 4
HELIX 3 AA3 THR A 70 GLY A 90 1 21
HELIX 4 AA4 GLY A 90 LEU A 99 1 10
HELIX 5 AA5 PHE A 105 LYS A 141 1 37
HELIX 6 AA6 GLY A 149 ALA A 169 1 21
HELIX 7 AA7 PRO A 170 VAL A 173 5 4
HELIX 8 AA8 ASN A 199 HIS A 211 1 13
HELIX 9 AA9 PHE A 212 GLN A 236 1 25
HELIX 10 AB1 SER A 240 THR A 277 1 38
HELIX 11 AB2 MET A 288 LYS A 296 1 9
HELIX 12 AB3 THR A 297 ILE A 307 1 11
HELIX 13 AB4 ASN A 310 CYS A 322 1 13
SHEET 1 AA1 2 THR A 4 GLY A 6 0
SHEET 2 AA1 2 PHE A 9 VAL A 11 -1 O VAL A 11 N THR A 4
SHEET 1 AA2 2 TYR A 178 GLU A 181 0
SHEET 2 AA2 2 SER A 186 ILE A 189 -1 O SER A 186 N GLU A 181
SSBOND 1 CYS A 2 CYS A 282 1555 1555 2.02
SSBOND 2 CYS A 110 CYS A 187 1555 1555 2.05
LINK C ACE A 0 N MET A 1 1555 1555 1.35
LINK ND2 ASN A 15 C1 NAG B 1 1555 1555 1.45
LINK SG CYS A 322 C1 PLM A 401 1555 1555 1.72
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.42
LINK O3 BMA B 3 C1 MAN B 4 1555 1555 1.43
LINK O6 BMA B 3 C1 MAN B 5 1555 1555 1.45
CISPEP 1 GLY A 284 PRO A 285 0 -0.32
CISPEP 2 ILE A 286 PHE A 287 0 -0.20
CRYST1 242.183 242.183 110.967 90.00 90.00 120.00 H 3 2 18
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 0.004129 0.002384 0.000000 0.00000
SCALE2 0.000000 0.004768 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009012 0.00000
HETATM 1 C ACE A 0 55.757 374.842 38.040 1.00149.97 C
ANISOU 1 C ACE A 0 13817 17769 25395 1863 2450 868 C
HETATM 2 O ACE A 0 55.200 375.259 36.989 1.00163.04 O
ANISOU 2 O ACE A 0 16078 18782 27087 2342 1749 -1010 O
HETATM 3 CH3 ACE A 0 56.556 376.068 38.444 1.00142.71 C
ANISOU 3 CH3 ACE A 0 12633 16799 24791 1698 2353 927 C
ATOM 4 N MET A 1 55.174 374.265 39.112 1.00137.50 N
ANISOU 4 N MET A 1 12319 16177 23747 1893 2118 796 N
ATOM 5 CA MET A 1 54.335 373.034 39.216 1.00125.60 C
ANISOU 5 CA MET A 1 11052 14675 21994 2037 2067 726 C
ATOM 6 C MET A 1 53.389 372.874 40.433 1.00128.76 C
ANISOU 6 C MET A 1 11575 15059 22290 2010 1711 683 C
ATOM 7 O MET A 1 53.521 371.921 41.205 1.00124.85 O
ANISOU 7 O MET A 1 11096 14507 21835 2117 1484 641 O
ATOM 8 CB MET A 1 55.130 371.767 39.107 1.00117.73 C
ANISOU 8 CB MET A 1 10006 13632 21096 2216 2094 688 C
ATOM 9 CG MET A 1 54.133 370.790 38.504 1.00114.01 C
ANISOU 9 CG MET A 1 9838 13169 20310 2344 2240 632 C
ATOM 10 SD MET A 1 54.745 369.471 37.525 1.00123.08 S
ANISOU 10 SD MET A 1 11047 14287 21431 2566 2503 586 S
ATOM 11 CE MET A 1 55.603 370.438 36.295 1.00129.04 C
ANISOU 11 CE MET A 1 11654 15099 22276 2514 2888 669 C
ATOM 12 N CYS A 2 52.496 373.830 40.638 1.00135.16 N
ANISOU 12 N CYS A 2 12466 15910 22978 1875 1659 703 N
ATOM 13 CA CYS A 2 51.619 373.846 41.805 1.00138.92 C
ANISOU 13 CA CYS A 2 13092 16378 23313 1822 1322 670 C
ATOM 14 C CYS A 2 50.432 372.880 41.729 1.00123.62 C
ANISOU 14 C CYS A 2 11545 14459 20967 1862 1314 620 C
ATOM 15 O CYS A 2 50.018 372.358 42.772 1.00131.01 O
ANISOU 15 O CYS A 2 12630 15360 21787 1869 1028 592 O
ATOM 16 CB CYS A 2 51.091 375.254 42.028 1.00152.17 C
ANISOU 16 CB CYS A 2 14791 18100 24926 1632 1260 697 C
ATOM 17 SG CYS A 2 52.397 376.391 42.455 1.00163.29 S
ANISOU 17 SG CYS A 2 15803 19456 26784 1536 1144 734 S
ATOM 18 N GLY A 3 49.863 372.620 40.552 1.00104.02 N
ANISOU 18 N GLY A 3 9240 12018 18265 1892 1608 609 N
ATOM 19 CA GLY A 3 48.689 371.753 40.515 1.00 84.01 C
ANISOU 19 CA GLY A 3 7058 9484 15376 1909 1567 552 C
ATOM 20 C GLY A 3 48.692 370.501 39.656 1.00 80.15 C
ANISOU 20 C GLY A 3 6699 8956 14800 2069 1754 498 C
ATOM 21 O GLY A 3 49.765 370.029 39.276 1.00 83.25 O
ANISOU 21 O GLY A 3 6896 9305 15429 2211 1888 501 O
ATOM 22 N THR A 4 47.514 369.939 39.349 1.00 77.94 N
ANISOU 22 N THR A 4 6737 8679 14199 2052 1761 442 N
ATOM 23 CA THR A 4 47.392 368.778 38.464 1.00 76.09 C
ANISOU 23 CA THR A 4 6665 8394 13852 2196 1925 369 C
ATOM 24 C THR A 4 46.474 369.071 37.288 1.00 70.85 C
ANISOU 24 C THR A 4 6226 7793 12900 2162 2124 328 C
ATOM 25 O THR A 4 45.308 369.409 37.482 1.00 81.64 O
ANISOU 25 O THR A 4 7779 9196 14043 2031 2011 316 O
ATOM 26 CB THR A 4 46.776 367.584 39.210 1.00 67.89 C
ANISOU 26 CB THR A 4 5827 7259 12708 2224 1706 321 C
ATOM 27 OG1 THR A 4 47.590 367.160 40.304 1.00 68.98 O
ANISOU 27 OG1 THR A 4 5804 7326 13079 2286 1502 357 O
ATOM 28 CG2 THR A 4 46.645 366.423 38.276 1.00 69.29 C
ANISOU 28 CG2 THR A 4 6176 7366 12785 2366 1861 231 C
ATOM 29 N GLU A 5 46.994 368.914 36.073 1.00 73.97 N
ANISOU 29 N GLU A 5 6612 8197 13297 2293 2417 305 N
ATOM 30 CA GLU A 5 46.220 369.123 34.863 1.00 69.09 C
ANISOU 30 CA GLU A 5 6231 7631 12387 2300 2605 259 C
ATOM 31 C GLU A 5 45.618 367.812 34.403 1.00 84.96 C
ANISOU 31 C GLU A 5 8515 9561 14206 2406 2585 132 C
ATOM 32 O GLU A 5 46.203 366.738 34.560 1.00 95.67 O
ANISOU 32 O GLU A 5 9840 10821 15690 2541 2574 88 O
ATOM 33 CB GLU A 5 47.056 369.680 33.715 1.00 84.21 C
ANISOU 33 CB GLU A 5 8039 9595 14361 2403 2959 305 C
ATOM 34 CG GLU A 5 48.037 370.777 34.039 1.00 94.83 C
ANISOU 34 CG GLU A 5 9044 10979 16007 2340 3039 432 C
ATOM 35 CD GLU A 5 48.884 371.139 32.835 1.00105.83 C
ANISOU 35 CD GLU A 5 10341 12399 17471 2465 3439 488 C
ATOM 36 OE1 GLU A 5 49.918 370.472 32.607 1.00109.38 O
ANISOU 36 OE1 GLU A 5 10632 12796 18133 2630 3598 483 O
ATOM 37 OE2 GLU A 5 48.491 372.069 32.099 1.00121.38 O
ANISOU 37 OE2 GLU A 5 12408 14438 19274 2409 3607 540 O
ATOM 38 N GLY A 6 44.463 367.924 33.770 1.00 93.27 N
ANISOU 38 N GLY A 6 9832 10646 14962 2351 2581 69 N
ATOM 39 CA GLY A 6 43.893 366.836 33.032 1.00 93.31 C
ANISOU 39 CA GLY A 6 10108 10574 14772 2457 2596 -67 C
ATOM 40 C GLY A 6 43.082 367.388 31.891 1.00 88.27 C
ANISOU 40 C GLY A 6 9694 10008 13837 2448 2707 -115 C
ATOM 41 O GLY A 6 43.047 368.600 31.643 1.00 93.44 O
ANISOU 41 O GLY A 6 10286 10770 14446 2373 2802 -27 O
ATOM 42 N PRO A 7 42.473 366.496 31.119 1.00 85.74 N
ANISOU 42 N PRO A 7 9645 9620 13313 2541 2697 -258 N
ATOM 43 CA PRO A 7 41.466 366.938 30.150 1.00 86.96 C
ANISOU 43 CA PRO A 7 10050 9830 13161 2520 2712 -323 C
ATOM 44 C PRO A 7 40.267 367.556 30.857 1.00 90.07 C
ANISOU 44 C PRO A 7 10458 10267 13497 2298 2466 -291 C
ATOM 45 O PRO A 7 39.633 366.922 31.708 1.00 95.37 O
ANISOU 45 O PRO A 7 11143 10860 14232 2200 2237 -325 O
ATOM 46 CB PRO A 7 41.109 365.645 29.411 1.00 85.20 C
ANISOU 46 CB PRO A 7 10096 9488 12788 2664 2681 -506 C
ATOM 47 CG PRO A 7 41.483 364.551 30.349 1.00 80.43 C
ANISOU 47 CG PRO A 7 9390 8754 12416 2675 2553 -525 C
ATOM 48 CD PRO A 7 42.644 365.035 31.129 1.00 81.94 C
ANISOU 48 CD PRO A 7 9261 8992 12881 2669 2644 -374 C
ATOM 49 N ASN A 8 39.997 368.828 30.534 1.00 82.72 N
ANISOU 49 N ASN A 8 9513 9455 12460 2224 2535 -212 N
ATOM 50 CA ASN A 8 38.843 369.600 30.998 1.00 70.79 C
ANISOU 50 CA ASN A 8 8029 8002 10868 2037 2346 -180 C
ATOM 51 C ASN A 8 38.933 370.043 32.452 1.00 72.73 C
ANISOU 51 C ASN A 8 8045 8260 11330 1877 2203 -70 C
ATOM 52 O ASN A 8 37.900 370.404 33.032 1.00 87.01 O
ANISOU 52 O ASN A 8 9884 10088 13090 1729 2022 -60 O
ATOM 53 CB ASN A 8 37.516 368.841 30.837 1.00 78.77 C
ANISOU 53 CB ASN A 8 9264 8942 11725 1994 2129 -320 C
ATOM 54 CG ASN A 8 37.314 368.279 29.457 1.00 92.19 C
ANISOU 54 CG ASN A 8 11227 10607 13193 2157 2204 -464 C
ATOM 55 OD1 ASN A 8 37.550 368.953 28.454 1.00 98.33 O
ANISOU 55 OD1 ASN A 8 12099 11464 13799 2254 2384 -446 O
ATOM 56 ND2 ASN A 8 36.821 367.045 29.396 1.00 99.70 N
ANISOU 56 ND2 ASN A 8 12322 11429 14131 2188 2056 -609 N
ATOM 57 N PHE A 9 40.106 370.025 33.088 1.00 69.16 N
ANISOU 57 N PHE A 9 7369 7793 11115 1909 2267 9 N
ATOM 58 CA PHE A 9 40.174 370.528 34.460 1.00 76.74 C
ANISOU 58 CA PHE A 9 8142 8767 12249 1768 2106 104 C
ATOM 59 C PHE A 9 41.598 370.912 34.852 1.00 80.10 C
ANISOU 59 C PHE A 9 8298 9202 12933 1813 2208 198 C
ATOM 60 O PHE A 9 42.577 370.517 34.211 1.00 76.41 O
ANISOU 60 O PHE A 9 7766 8712 12555 1961 2399 189 O
ATOM 61 CB PHE A 9 39.592 369.513 35.466 1.00 85.97 C
ANISOU 61 CB PHE A 9 9367 9839 13457 1717 1876 62 C
ATOM 62 CG PHE A 9 40.302 368.174 35.506 1.00 82.07 C
ANISOU 62 CG PHE A 9 8874 9229 13079 1857 1889 7 C
ATOM 63 CD1 PHE A 9 39.749 367.068 34.884 1.00 83.64 C
ANISOU 63 CD1 PHE A 9 9280 9335 13164 1927 1873 -116 C
ATOM 64 CD2 PHE A 9 41.489 368.011 36.217 1.00 77.99 C
ANISOU 64 CD2 PHE A 9 8149 8683 12800 1917 1890 73 C
ATOM 65 CE1 PHE A 9 40.382 365.819 34.939 1.00 78.50 C
ANISOU 65 CE1 PHE A 9 8642 8560 12626 2061 1881 -170 C
ATOM 66 CE2 PHE A 9 42.120 366.780 36.274 1.00 82.70 C
ANISOU 66 CE2 PHE A 9 8746 9165 13511 2056 1894 26 C
ATOM 67 CZ PHE A 9 41.559 365.677 35.633 1.00 77.31 C
ANISOU 67 CZ PHE A 9 8284 8386 12704 2129 1897 -94 C
ATOM 68 N TYR A 10 41.687 371.674 35.947 1.00 78.95 N
ANISOU 68 N TYR A 10 7993 9084 12920 1688 2068 282 N
ATOM 69 CA TYR A 10 42.959 372.019 36.585 1.00 68.84 C
ANISOU 69 CA TYR A 10 6436 7795 11926 1704 2077 360 C
ATOM 70 C TYR A 10 42.701 372.041 38.090 1.00 68.60 C
ANISOU 70 C TYR A 10 6357 7738 11972 1601 1795 387 C
ATOM 71 O TYR A 10 42.098 372.984 38.607 1.00 82.49 O
ANISOU 71 O TYR A 10 8126 9547 13670 1468 1692 426 O
ATOM 72 CB TYR A 10 43.485 373.372 36.102 1.00 73.24 C
ANISOU 72 CB TYR A 10 6840 8425 12563 1661 2248 447 C
ATOM 73 CG TYR A 10 44.713 373.819 36.872 1.00 77.10 C
ANISOU 73 CG TYR A 10 7015 8890 13387 1648 2208 521 C
ATOM 74 CD1 TYR A 10 45.970 373.246 36.607 1.00 80.06 C
ANISOU 74 CD1 TYR A 10 7201 9218 14001 1787 2346 530 C
ATOM 75 CD2 TYR A 10 44.624 374.772 37.877 1.00 64.45 C
ANISOU 75 CD2 TYR A 10 5305 7305 11879 1506 2019 572 C
ATOM 76 CE1 TYR A 10 47.096 373.625 37.305 1.00 72.24 C
ANISOU 76 CE1 TYR A 10 5899 8198 13352 1776 2284 590 C
ATOM 77 CE2 TYR A 10 45.744 375.151 38.593 1.00 73.65 C
ANISOU 77 CE2 TYR A 10 6185 8435 13363 1496 1940 621 C
ATOM 78 CZ TYR A 10 46.981 374.574 38.301 1.00 81.08 C
ANISOU 78 CZ TYR A 10 6918 9328 14559 1627 2066 631 C
ATOM 79 OH TYR A 10 48.097 374.952 39.015 1.00 87.00 O
ANISOU 79 OH TYR A 10 7359 10036 15662 1615 1962 673 O
ATOM 80 N VAL A 11 43.154 371.007 38.791 1.00 67.39 N
ANISOU 80 N VAL A 11 6169 7499 11937 1676 1675 369 N
ATOM 81 CA VAL A 11 43.069 370.960 40.252 1.00 73.34 C
ANISOU 81 CA VAL A 11 6891 8217 12757 1613 1414 405 C
ATOM 82 C VAL A 11 44.248 371.699 40.877 1.00 82.88 C
ANISOU 82 C VAL A 11 7827 9436 14229 1612 1349 467 C
ATOM 83 O VAL A 11 45.405 371.318 40.652 1.00 83.51 O
ANISOU 83 O VAL A 11 7723 9476 14532 1728 1423 472 O
ATOM 84 CB VAL A 11 43.012 369.509 40.757 1.00 67.61 C
ANISOU 84 CB VAL A 11 6273 7381 12036 1702 1301 370 C
ATOM 85 CG1 VAL A 11 43.069 369.471 42.284 1.00 60.40 C
ANISOU 85 CG1 VAL A 11 5338 6428 11184 1667 1044 424 C
ATOM 86 CG2 VAL A 11 41.768 368.814 40.221 1.00 67.10 C
ANISOU 86 CG2 VAL A 11 6466 7286 11743 1677 1333 303 C
ATOM 87 N PRO A 12 44.012 372.762 41.660 1.00 81.29 N
ANISOU 87 N PRO A 12 7581 9275 14029 1489 1206 509 N
ATOM 88 CA PRO A 12 45.126 373.521 42.257 1.00 72.05 C
ANISOU 88 CA PRO A 12 6145 8098 13131 1478 1111 552 C
ATOM 89 C PRO A 12 45.773 372.806 43.441 1.00 69.94 C
ANISOU 89 C PRO A 12 5811 7752 13009 1556 861 552 C
ATOM 90 O PRO A 12 45.841 373.322 44.561 1.00 73.74 O
ANISOU 90 O PRO A 12 6265 8224 13528 1504 622 568 O
ATOM 91 CB PRO A 12 44.444 374.838 42.645 1.00 59.96 C
ANISOU 91 CB PRO A 12 4655 6627 11501 1324 1033 576 C
ATOM 92 CG PRO A 12 43.069 374.452 42.941 1.00 64.03 C
ANISOU 92 CG PRO A 12 5449 7155 11723 1277 965 552 C
ATOM 93 CD PRO A 12 42.715 373.412 41.911 1.00 71.73 C
ANISOU 93 CD PRO A 12 6551 8117 12584 1356 1143 511 C
ATOM 94 N PHE A 13 46.296 371.611 43.185 1.00 70.98 N
ANISOU 94 N PHE A 13 5926 7820 13222 1698 911 531 N
ATOM 95 CA PHE A 13 46.971 370.823 44.205 1.00 65.23 C
ANISOU 95 CA PHE A 13 5140 7005 12638 1801 683 537 C
ATOM 96 C PHE A 13 47.968 369.908 43.514 1.00 80.91 C
ANISOU 96 C PHE A 13 6977 8934 14830 1966 829 518 C
ATOM 97 O PHE A 13 47.679 369.377 42.440 1.00 84.44 O
ANISOU 97 O PHE A 13 7523 9385 15177 2016 1067 484 O
ATOM 98 CB PHE A 13 45.966 370.021 45.032 1.00 64.01 C
ANISOU 98 CB PHE A 13 5277 6804 12239 1797 521 536 C
ATOM 99 CG PHE A 13 46.538 369.399 46.274 1.00 65.34 C
ANISOU 99 CG PHE A 13 5435 6887 12506 1895 248 561 C
ATOM 100 CD1 PHE A 13 46.616 370.120 47.450 1.00 65.36 C
ANISOU 100 CD1 PHE A 13 5428 6899 12507 1847 -9 587 C
ATOM 101 CD2 PHE A 13 46.924 368.067 46.285 1.00 66.68 C
ANISOU 101 CD2 PHE A 13 5641 6956 12740 2045 237 556 C
ATOM 102 CE1 PHE A 13 47.109 369.541 48.600 1.00 66.80 C
ANISOU 102 CE1 PHE A 13 5638 7001 12744 1954 -278 610 C
ATOM 103 CE2 PHE A 13 47.406 367.480 47.435 1.00 68.04 C
ANISOU 103 CE2 PHE A 13 5830 7043 12980 2147 -24 589 C
ATOM 104 CZ PHE A 13 47.505 368.216 48.592 1.00 68.14 C
ANISOU 104 CZ PHE A 13 5838 7073 12979 2105 -285 618 C
ATOM 105 N SER A 14 49.140 369.733 44.119 1.00 72.37 N
ANISOU 105 N SER A 14 5662 7797 14040 2061 679 534 N
ATOM 106 CA SER A 14 50.185 368.961 43.470 1.00 77.69 C
ANISOU 106 CA SER A 14 6149 8416 14955 2228 831 521 C
ATOM 107 C SER A 14 49.920 367.477 43.668 1.00 83.44 C
ANISOU 107 C SER A 14 7082 9048 15572 2361 774 492 C
ATOM 108 O SER A 14 49.508 367.037 44.741 1.00 95.25 O
ANISOU 108 O SER A 14 8741 10491 16960 2360 518 508 O
ATOM 109 CB SER A 14 51.556 369.352 44.015 1.00 84.99 C
ANISOU 109 CB SER A 14 6709 9309 16276 2282 684 547 C
ATOM 110 OG SER A 14 52.483 368.294 43.914 1.00 83.62 O
ANISOU 110 OG SER A 14 6397 9050 16325 2475 702 535 O
ATOM 111 N ASN A 15 50.209 366.692 42.639 1.00 88.78 N
ANISOU 111 N ASN A 15 7757 9690 16287 2487 1019 453 N
ATOM 112 CA ASN A 15 49.962 365.260 42.672 1.00 83.85 C
ANISOU 112 CA ASN A 15 7331 8954 15572 2616 993 415 C
ATOM 113 C ASN A 15 51.205 364.454 43.054 1.00 76.39 C
ANISOU 113 C ASN A 15 6182 7908 14933 2813 901 423 C
ATOM 114 O ASN A 15 51.282 363.266 42.736 1.00 77.44 O
ANISOU 114 O ASN A 15 6421 7940 15060 2959 967 383 O
ATOM 115 CB ASN A 15 49.385 364.816 41.324 1.00 83.14 C
ANISOU 115 CB ASN A 15 7421 8871 15297 2646 1290 345 C
ATOM 116 CG ASN A 15 48.590 363.541 41.423 1.00 72.79 C
ANISOU 116 CG ASN A 15 6409 7446 13801 2695 1228 297 C
ATOM 117 OD1 ASN A 15 48.233 363.111 42.513 1.00 72.28 O
ANISOU 117 OD1 ASN A 15 6457 7314 13694 2670 985 335 O
ATOM 118 ND2 ASN A 15 48.282 362.938 40.283 1.00 83.95 N
ANISOU 118 ND2 ASN A 15 7969 8829 15099 2764 1447 213 N
ATOM 119 N LYS A 16 52.222 365.095 43.650 1.00 84.21 N
ANISOU 119 N LYS A 16 6864 8916 16217 2826 756 465 N
ATOM 120 CA LYS A 16 53.458 364.376 43.973 1.00 80.81 C
ANISOU 120 CA LYS A 16 6198 8390 16115 3023 658 470 C
ATOM 121 C LYS A 16 53.208 363.199 44.918 1.00 81.07 C
ANISOU 121 C LYS A 16 6453 8299 16051 3128 399 478 C
ATOM 122 O LYS A 16 53.988 362.241 44.929 1.00 93.32 O
ANISOU 122 O LYS A 16 7926 9754 17776 3312 377 467 O
ATOM 123 CB LYS A 16 54.495 365.323 44.595 1.00 82.41 C
ANISOU 123 CB LYS A 16 6101 8651 16560 2952 470 501 C
ATOM 124 CG LYS A 16 53.979 366.234 45.675 1.00105.13 C
ANISOU 124 CG LYS A 16 8999 11549 19397 2827 177 535 C
ATOM 125 CD LYS A 16 55.064 367.127 46.264 1.00109.80 C
ANISOU 125 CD LYS A 16 9309 12179 20233 2754 -31 541 C
ATOM 126 CE LYS A 16 54.511 367.919 47.454 1.00114.90 C
ANISOU 126 CE LYS A 16 10025 12825 20807 2660 -370 558 C
ATOM 127 NZ LYS A 16 54.912 369.359 47.484 1.00114.75 N
ANISOU 127 NZ LYS A 16 9790 12876 20932 2488 -407 553 N
ATOM 128 N THR A 17 52.138 363.260 45.717 1.00 91.83 N
ANISOU 128 N THR A 17 8108 9664 17121 3008 214 505 N
ATOM 129 CA THR A 17 51.700 362.200 46.621 1.00 79.04 C
ANISOU 129 CA THR A 17 6752 7921 15357 3083 1 536 C
ATOM 130 C THR A 17 50.669 361.269 45.996 1.00 85.95 C
ANISOU 130 C THR A 17 7939 8731 15987 3073 184 502 C
ATOM 131 O THR A 17 50.258 360.298 46.642 1.00 90.00 O
ANISOU 131 O THR A 17 8682 9119 16395 3131 50 535 O
ATOM 132 CB THR A 17 51.142 362.801 47.928 1.00 89.56 C
ANISOU 132 CB THR A 17 8230 9283 16517 2969 -294 597 C
ATOM 133 OG1 THR A 17 49.983 363.620 47.658 1.00 93.60 O
ANISOU 133 OG1 THR A 17 8902 9900 16763 2762 -176 591 O
ATOM 134 CG2 THR A 17 52.202 363.592 48.668 1.00 90.70 C
ANISOU 134 CG2 THR A 17 8088 9459 16915 3000 -545 614 C
ATOM 135 N GLY A 18 50.234 361.541 44.768 1.00 85.06 N
ANISOU 135 N GLY A 18 7850 8687 15783 3003 475 438 N
ATOM 136 CA GLY A 18 49.336 360.639 44.082 1.00 82.36 C
ANISOU 136 CA GLY A 18 7783 8269 15242 3006 628 381 C
ATOM 137 C GLY A 18 47.892 360.677 44.517 1.00 82.81 C
ANISOU 137 C GLY A 18 8137 8325 15002 2834 553 404 C
ATOM 138 O GLY A 18 47.136 359.785 44.125 1.00 93.61 O
ANISOU 138 O GLY A 18 9733 9593 16241 2837 626 361 O
ATOM 139 N VAL A 19 47.473 361.668 45.313 1.00 86.80 N
ANISOU 139 N VAL A 19 8645 8926 15410 2688 412 467 N
ATOM 140 CA VAL A 19 46.113 361.668 45.857 1.00 70.22 C
ANISOU 140 CA VAL A 19 6816 6816 13048 2539 344 504 C
ATOM 141 C VAL A 19 45.099 362.457 45.030 1.00 68.05 C
ANISOU 141 C VAL A 19 6610 6656 12590 2367 515 456 C
ATOM 142 O VAL A 19 43.889 362.358 45.300 1.00 72.66 O
ANISOU 142 O VAL A 19 7407 7221 12979 2247 495 474 O
ATOM 143 CB VAL A 19 46.093 362.240 47.290 1.00 69.93 C
ANISOU 143 CB VAL A 19 6799 6806 12965 2493 89 600 C
ATOM 144 CG1 VAL A 19 47.084 361.503 48.167 1.00 72.27 C
ANISOU 144 CG1 VAL A 19 7044 6990 13427 2675 -120 652 C
ATOM 145 CG2 VAL A 19 46.365 363.739 47.267 1.00 69.04 C
ANISOU 145 CG2 VAL A 19 6492 6854 12885 2389 77 595 C
ATOM 146 N VAL A 20 45.537 363.198 44.010 1.00 75.66 N
ANISOU 146 N VAL A 20 7403 7727 13617 2359 691 401 N
ATOM 147 CA VAL A 20 44.617 364.038 43.255 1.00 74.86 C
ANISOU 147 CA VAL A 20 7370 7737 13335 2209 832 365 C
ATOM 148 C VAL A 20 43.732 363.173 42.367 1.00 75.18 C
ANISOU 148 C VAL A 20 7628 7706 13231 2209 957 282 C
ATOM 149 O VAL A 20 44.193 362.200 41.753 1.00 76.83 O
ANISOU 149 O VAL A 20 7857 7817 13516 2351 1045 219 O
ATOM 150 CB VAL A 20 45.410 365.062 42.424 1.00 73.31 C
ANISOU 150 CB VAL A 20 6939 7661 13253 2216 995 349 C
ATOM 151 CG1 VAL A 20 44.492 365.865 41.508 1.00 67.51 C
ANISOU 151 CG1 VAL A 20 6298 7032 12320 2089 1154 312 C
ATOM 152 CG2 VAL A 20 46.194 365.972 43.333 1.00 79.57 C
ANISOU 152 CG2 VAL A 20 7512 8509 14212 2190 840 420 C
ATOM 153 N ARG A 21 42.460 363.571 42.252 1.00 73.21 N
ANISOU 153 N ARG A 21 7533 7501 12781 2053 963 272 N
ATOM 154 CA ARG A 21 41.456 362.882 41.450 1.00 70.41 C
ANISOU 154 CA ARG A 21 7382 7079 12290 2021 1040 184 C
ATOM 155 C ARG A 21 40.739 363.900 40.572 1.00 67.09 C
ANISOU 155 C ARG A 21 6983 6793 11714 1909 1149 139 C
ATOM 156 O ARG A 21 40.673 365.080 40.914 1.00 77.64 O
ANISOU 156 O ARG A 21 8225 8253 13020 1813 1129 200 O
ATOM 157 CB ARG A 21 40.446 362.168 42.344 1.00 63.27 C
ANISOU 157 CB ARG A 21 6658 6058 11323 1938 901 228 C
ATOM 158 CG ARG A 21 41.082 361.189 43.287 1.00 64.74 C
ANISOU 158 CG ARG A 21 6855 6102 11639 2051 783 293 C
ATOM 159 CD ARG A 21 41.665 360.030 42.538 1.00 72.73 C
ANISOU 159 CD ARG A 21 7898 6982 12756 2212 858 205 C
ATOM 160 NE ARG A 21 42.201 359.013 43.443 1.00 86.23 N
ANISOU 160 NE ARG A 21 9639 8534 14590 2328 736 273 N
ATOM 161 CZ ARG A 21 43.497 358.831 43.679 1.00 82.43 C
ANISOU 161 CZ ARG A 21 9003 8038 14281 2493 702 296 C
ATOM 162 NH1 ARG A 21 43.893 357.877 44.502 1.00 87.60 N
ANISOU 162 NH1 ARG A 21 9712 8539 15034 2604 574 360 N
ATOM 163 NH2 ARG A 21 44.403 359.581 43.068 1.00 85.77 N
ANISOU 163 NH2 ARG A 21 9209 8587 14791 2553 802 260 N
ATOM 164 N SER A 22 40.211 363.436 39.444 1.00 69.85 N
ANISOU 164 N SER A 22 7471 7108 11962 1932 1250 27 N
ATOM 165 CA SER A 22 39.407 364.280 38.580 1.00 61.65 C
ANISOU 165 CA SER A 22 6494 6179 10752 1840 1327 -22 C
ATOM 166 C SER A 22 38.297 364.916 39.407 1.00 72.59 C
ANISOU 166 C SER A 22 7914 7611 12056 1657 1201 46 C
ATOM 167 O SER A 22 37.616 364.212 40.171 1.00 69.23 O
ANISOU 167 O SER A 22 7582 7080 11643 1598 1084 71 O
ATOM 168 CB SER A 22 38.825 363.460 37.425 1.00 63.05 C
ANISOU 168 CB SER A 22 6863 6274 10821 1893 1384 -166 C
ATOM 169 OG SER A 22 37.827 364.122 36.668 1.00 64.79 O
ANISOU 169 OG SER A 22 7183 6575 10861 1801 1401 -221 O
ATOM 170 N PRO A 23 38.105 366.239 39.315 1.00 70.60 N
ANISOU 170 N PRO A 23 7587 7505 11731 1569 1234 87 N
ATOM 171 CA PRO A 23 36.985 366.870 40.025 1.00 75.14 C
ANISOU 171 CA PRO A 23 8204 8125 12221 1409 1132 141 C
ATOM 172 C PRO A 23 35.618 366.441 39.483 1.00 74.44 C
ANISOU 172 C PRO A 23 8277 7987 12019 1331 1106 62 C
ATOM 173 O PRO A 23 34.598 366.880 40.029 1.00 65.28 O
ANISOU 173 O PRO A 23 7143 6853 10806 1202 1037 103 O
ATOM 174 CB PRO A 23 37.238 368.381 39.834 1.00 77.71 C
ANISOU 174 CB PRO A 23 8411 8607 12509 1361 1193 186 C
ATOM 175 CG PRO A 23 38.028 368.449 38.550 1.00 74.09 C
ANISOU 175 CG PRO A 23 7917 8182 12051 1476 1364 127 C
ATOM 176 CD PRO A 23 38.875 367.215 38.526 1.00 67.40 C
ANISOU 176 CD PRO A 23 7063 7221 11326 1618 1383 91 C
ATOM 177 N PHE A 24 35.578 365.687 38.378 1.00 75.03 N
ANISOU 177 N PHE A 24 8454 7995 12058 1412 1161 -58 N
ATOM 178 CA PHE A 24 34.339 365.116 37.889 1.00 69.66 C
ANISOU 178 CA PHE A 24 7922 7235 11310 1346 1095 -153 C
ATOM 179 C PHE A 24 34.043 363.709 38.415 1.00 72.96 C
ANISOU 179 C PHE A 24 8423 7459 11841 1344 1009 -171 C
ATOM 180 O PHE A 24 32.967 363.180 38.112 1.00 81.07 O
ANISOU 180 O PHE A 24 9552 8393 12858 1269 937 -246 O
ATOM 181 CB PHE A 24 34.339 365.068 36.362 1.00 58.83 C
ANISOU 181 CB PHE A 24 6655 5883 9815 1437 1171 -293 C
ATOM 182 CG PHE A 24 34.567 366.394 35.719 1.00 65.32 C
ANISOU 182 CG PHE A 24 7427 6877 10515 1447 1275 -268 C
ATOM 183 CD1 PHE A 24 33.704 367.443 35.952 1.00 68.17 C
ANISOU 183 CD1 PHE A 24 7758 7339 10806 1316 1224 -216 C
ATOM 184 CD2 PHE A 24 35.572 366.562 34.788 1.00 71.07 C
ANISOU 184 CD2 PHE A 24 8154 7654 11195 1596 1439 -300 C
ATOM 185 CE1 PHE A 24 33.894 368.664 35.346 1.00 65.94 C
ANISOU 185 CE1 PHE A 24 7442 7196 10415 1326 1320 -186 C
ATOM 186 CE2 PHE A 24 35.760 367.772 34.157 1.00 67.09 C
ANISOU 186 CE2 PHE A 24 7618 7292 10583 1605 1556 -262 C
ATOM 187 CZ PHE A 24 34.912 368.829 34.443 1.00 72.92 C
ANISOU 187 CZ PHE A 24 8328 8122 11254 1466 1487 -204 C
ATOM 188 N GLU A 25 34.928 363.094 39.213 1.00 71.85 N
ANISOU 188 N GLU A 25 8237 7241 11823 1420 1002 -101 N
ATOM 189 CA GLU A 25 34.782 361.676 39.569 1.00 65.88 C
ANISOU 189 CA GLU A 25 7578 6277 11176 1447 939 -119 C
ATOM 190 C GLU A 25 34.886 361.373 41.055 1.00 60.62 C
ANISOU 190 C GLU A 25 6885 5542 10604 1415 869 33 C
ATOM 191 O GLU A 25 34.353 360.347 41.480 1.00 85.26 O
ANISOU 191 O GLU A 25 10103 8488 13803 1382 815 48 O
ATOM 192 CB GLU A 25 35.797 360.776 38.843 1.00 62.64 C
ANISOU 192 CB GLU A 25 7204 5773 10822 1632 999 -216 C
ATOM 193 CG GLU A 25 35.942 360.868 37.310 1.00 95.82 C
ANISOU 193 CG GLU A 25 11476 10020 14914 1727 1094 -375 C
ATOM 194 CD GLU A 25 36.797 359.685 36.739 1.00115.21 C
ANISOU 194 CD GLU A 25 14005 12329 17440 1918 1149 -477 C
ATOM 195 OE1 GLU A 25 37.815 359.288 37.365 1.00 92.79 O
ANISOU 195 OE1 GLU A 25 11077 9444 14735 2022 1170 -403 O
ATOM 196 OE2 GLU A 25 36.444 359.138 35.667 1.00130.91 O
ANISOU 196 OE2 GLU A 25 16150 14240 19351 1976 1158 -638 O
ATOM 197 N ALA A 26 35.500 362.225 41.866 1.00 65.12 N
ANISOU 197 N ALA A 26 7344 6233 11166 1422 862 146 N
ATOM 198 CA ALA A 26 35.805 361.833 43.234 1.00 60.10 C
ANISOU 198 CA ALA A 26 6715 5522 10599 1441 782 280 C
ATOM 199 C ALA A 26 36.061 363.089 44.048 1.00 73.42 C
ANISOU 199 C ALA A 26 8302 7367 12228 1401 748 379 C
ATOM 200 O ALA A 26 36.574 364.080 43.510 1.00 70.03 O
ANISOU 200 O ALA A 26 7754 7084 11771 1414 795 344 O
ATOM 201 CB ALA A 26 37.028 360.907 43.279 1.00 65.24 C
ANISOU 201 CB ALA A 26 7349 6065 11374 1617 769 273 C
ATOM 202 N PRO A 27 35.825 363.039 45.356 1.00 69.69 N
ANISOU 202 N PRO A 27 7882 6856 11740 1371 669 504 N
ATOM 203 CA PRO A 27 35.828 364.262 46.169 1.00 72.17 C
ANISOU 203 CA PRO A 27 8141 7310 11970 1319 623 583 C
ATOM 204 C PRO A 27 37.208 364.869 46.368 1.00 73.24 C
ANISOU 204 C PRO A 27 8133 7530 12167 1424 563 592 C
ATOM 205 O PRO A 27 38.209 364.159 46.503 1.00 89.39 O
ANISOU 205 O PRO A 27 10142 9496 14325 1556 515 596 O
ATOM 206 CB PRO A 27 35.245 363.806 47.510 1.00 64.87 C
ANISOU 206 CB PRO A 27 7357 6290 11002 1293 564 713 C
ATOM 207 CG PRO A 27 35.115 362.378 47.462 1.00 59.54 C
ANISOU 207 CG PRO A 27 6786 5423 10413 1336 574 720 C
ATOM 208 CD PRO A 27 35.288 361.883 46.075 1.00 59.86 C
ANISOU 208 CD PRO A 27 6783 5429 10533 1363 637 576 C
ATOM 209 N GLN A 28 37.248 366.198 46.398 1.00 70.08 N
ANISOU 209 N GLN A 28 7637 7278 11711 1363 559 594 N
ATOM 210 CA GLN A 28 38.514 366.925 46.441 1.00 73.45 C
ANISOU 210 CA GLN A 28 7890 7784 12234 1435 510 589 C
ATOM 211 C GLN A 28 38.899 367.281 47.877 1.00 75.57 C
ANISOU 211 C GLN A 28 8173 8052 12487 1465 334 676 C
ATOM 212 O GLN A 28 39.280 368.424 48.155 1.00 73.28 O
ANISOU 212 O GLN A 28 7780 7860 12203 1436 272 679 O
ATOM 213 CB GLN A 28 38.422 368.180 45.586 1.00 66.14 C
ANISOU 213 CB GLN A 28 6852 7000 11279 1356 605 539 C
ATOM 214 CG GLN A 28 38.048 367.924 44.144 1.00 72.15 C
ANISOU 214 CG GLN A 28 7629 7770 12015 1346 766 450 C
ATOM 215 CD GLN A 28 39.146 367.271 43.345 1.00 77.83 C
ANISOU 215 CD GLN A 28 8259 8445 12867 1482 844 396 C
ATOM 216 OE1 GLN A 28 40.214 367.837 43.147 1.00 77.41 O
ANISOU 216 OE1 GLN A 28 8034 8449 12930 1540 875 401 O
ATOM 217 NE2 GLN A 28 38.869 366.076 42.849 1.00 85.84 N
ANISOU 217 NE2 GLN A 28 9388 9350 13879 1536 885 339 N
ATOM 218 N TYR A 29 38.780 366.325 48.828 1.00 73.63 N
ANISOU 218 N TYR A 29 8075 7687 12214 1526 243 750 N
ATOM 219 CA TYR A 29 39.009 366.667 50.249 1.00 77.55 C
ANISOU 219 CA TYR A 29 8644 8182 12641 1567 67 835 C
ATOM 220 C TYR A 29 40.498 366.890 50.600 1.00 77.97 C
ANISOU 220 C TYR A 29 8536 8243 12845 1692 -102 823 C
ATOM 221 O TYR A 29 40.773 366.996 51.801 1.00 79.45 O
ANISOU 221 O TYR A 29 8808 8406 12973 1756 -288 885 O
ATOM 222 CB TYR A 29 38.414 365.610 51.194 1.00 81.92 C
ANISOU 222 CB TYR A 29 9429 8600 13098 1606 34 937 C
ATOM 223 CG TYR A 29 36.898 365.498 51.176 1.00 87.75 C
ANISOU 223 CG TYR A 29 10315 9320 13706 1474 177 974 C
ATOM 224 CD1 TYR A 29 36.093 366.539 51.623 1.00 89.74 C
ANISOU 224 CD1 TYR A 29 10613 9672 13813 1377 199 999 C
ATOM 225 CD2 TYR A 29 36.275 364.351 50.720 1.00 93.10 C
ANISOU 225 CD2 TYR A 29 11074 9869 14428 1450 284 979 C
ATOM 226 CE1 TYR A 29 34.714 366.428 51.609 1.00 90.41 C
ANISOU 226 CE1 TYR A 29 10802 9735 13813 1262 336 1035 C
ATOM 227 CE2 TYR A 29 34.900 364.238 50.705 1.00 91.76 C
ANISOU 227 CE2 TYR A 29 11005 9670 14188 1323 405 1012 C
ATOM 228 CZ TYR A 29 34.124 365.274 51.142 1.00 85.80 C
ANISOU 228 CZ TYR A 29 10274 9024 13303 1230 436 1043 C
ATOM 229 OH TYR A 29 32.756 365.137 51.101 1.00 85.71 O
ANISOU 229 OH TYR A 29 10332 8978 13257 1108 564 1077 O
ATOM 230 N TYR A 30 41.427 367.000 49.647 1.00 86.05 N
ANISOU 230 N TYR A 30 9340 9298 14058 1733 -48 751 N
ATOM 231 CA TYR A 30 42.805 367.424 49.900 1.00 85.84 C
ANISOU 231 CA TYR A 30 9102 9291 14224 1825 -196 735 C
ATOM 232 C TYR A 30 42.995 368.902 49.582 1.00 84.92 C
ANISOU 232 C TYR A 30 8815 9301 14151 1724 -180 694 C
ATOM 233 O TYR A 30 44.016 369.483 49.962 1.00 95.39 O
ANISOU 233 O TYR A 30 9962 10642 15640 1768 -332 683 O
ATOM 234 CB TYR A 30 43.792 366.578 49.073 1.00 69.36 C
ANISOU 234 CB TYR A 30 6855 7141 12358 1949 -121 694 C
ATOM 235 CG TYR A 30 43.287 366.337 47.675 1.00 69.28 C
ANISOU 235 CG TYR A 30 6844 7152 12327 1896 141 630 C
ATOM 236 CD1 TYR A 30 43.401 367.330 46.706 1.00 72.40 C
ANISOU 236 CD1 TYR A 30 7085 7661 12763 1821 289 580 C
ATOM 237 CD2 TYR A 30 42.597 365.186 47.349 1.00 62.96 C
ANISOU 237 CD2 TYR A 30 6223 6252 11447 1915 230 622 C
ATOM 238 CE1 TYR A 30 42.912 367.150 45.432 1.00 71.57 C
ANISOU 238 CE1 TYR A 30 7014 7577 12601 1790 512 520 C
ATOM 239 CE2 TYR A 30 42.092 365.002 46.075 1.00 62.27 C
ANISOU 239 CE2 TYR A 30 6158 6180 11323 1872 435 546 C
ATOM 240 CZ TYR A 30 42.252 365.986 45.123 1.00 70.71 C
ANISOU 240 CZ TYR A 30 7087 7372 12407 1818 571 494 C
ATOM 241 OH TYR A 30 41.752 365.813 43.854 1.00 74.03 O
ANISOU 241 OH TYR A 30 7563 7808 12759 1795 760 416 O
ATOM 242 N LEU A 31 42.030 369.503 48.882 1.00 78.40 N
ANISOU 242 N LEU A 31 8036 8553 13199 1592 -7 671 N
ATOM 243 CA LEU A 31 41.946 370.949 48.708 1.00 77.09 C
ANISOU 243 CA LEU A 31 7769 8495 13028 1483 8 649 C
ATOM 244 C LEU A 31 41.446 371.627 49.971 1.00 83.06 C
ANISOU 244 C LEU A 31 8662 9268 13630 1440 -169 684 C
ATOM 245 O LEU A 31 41.755 372.800 50.202 1.00 94.71 O
ANISOU 245 O LEU A 31 10037 10799 15151 1388 -252 663 O
ATOM 246 CB LEU A 31 40.986 371.300 47.570 1.00 69.81 C
ANISOU 246 CB LEU A 31 6886 7641 11998 1374 236 618 C
ATOM 247 CG LEU A 31 41.233 370.822 46.146 1.00 75.18 C
ANISOU 247 CG LEU A 31 7484 8322 12758 1406 445 569 C
ATOM 248 CD1 LEU A 31 40.170 371.378 45.194 1.00 65.83 C
ANISOU 248 CD1 LEU A 31 6375 7214 11424 1297 614 539 C
ATOM 249 CD2 LEU A 31 42.631 371.257 45.718 1.00 81.29 C
ANISOU 249 CD2 LEU A 31 7994 9114 13777 1468 470 557 C
ATOM 250 N ALA A 32 40.654 370.920 50.775 1.00 79.54 N
ANISOU 250 N ALA A 32 8455 8766 13002 1462 -212 738 N
ATOM 251 CA ALA A 32 39.885 371.518 51.855 1.00 67.29 C
ANISOU 251 CA ALA A 32 7086 7235 11245 1421 -306 777 C
ATOM 252 C ALA A 32 39.242 370.407 52.673 1.00 70.75 C
ANISOU 252 C ALA A 32 7772 7580 11528 1481 -320 860 C
ATOM 253 O ALA A 32 38.832 369.385 52.121 1.00 77.22 O
ANISOU 253 O ALA A 32 8638 8339 12363 1480 -183 877 O
ATOM 254 CB ALA A 32 38.809 372.467 51.303 1.00 59.89 C
ANISOU 254 CB ALA A 32 6167 6391 10197 1277 -149 754 C
ATOM 255 N GLU A 33 39.179 370.613 53.988 1.00 67.16 N
ANISOU 255 N GLU A 33 7486 7104 10926 1539 -486 911 N
ATOM 256 CA GLU A 33 38.509 369.682 54.880 1.00 71.48 C
ANISOU 256 CA GLU A 33 8299 7562 11300 1599 -478 1015 C
ATOM 257 C GLU A 33 37.028 369.567 54.512 1.00 80.35 C
ANISOU 257 C GLU A 33 9527 8696 12305 1475 -236 1051 C
ATOM 258 O GLU A 33 36.467 370.467 53.876 1.00 85.71 O
ANISOU 258 O GLU A 33 10118 9471 12977 1356 -130 995 O
ATOM 259 CB GLU A 33 38.652 370.129 56.333 1.00 84.51 C
ANISOU 259 CB GLU A 33 10138 9203 12771 1691 -686 1058 C
ATOM 260 CG GLU A 33 40.078 370.277 56.809 1.00 90.25 C
ANISOU 260 CG GLU A 33 10764 9908 13621 1818 -975 1015 C
ATOM 261 CD GLU A 33 40.785 368.950 56.846 1.00112.68 C
ANISOU 261 CD GLU A 33 13604 12635 16574 1949 -1040 1063 C
ATOM 262 OE1 GLU A 33 40.110 367.941 57.132 1.00121.06 O
ANISOU 262 OE1 GLU A 33 14871 13610 17515 1981 -930 1163 O
ATOM 263 OE2 GLU A 33 42.008 368.910 56.580 1.00127.61 O
ANISOU 263 OE2 GLU A 33 15280 14514 18693 2022 -1192 1005 O
ATOM 264 N PRO A 34 36.388 368.432 54.824 1.00 78.84 N
ANISOU 264 N PRO A 34 9507 8397 12051 1497 -144 1143 N
ATOM 265 CA PRO A 34 34.939 368.327 54.586 1.00 75.52 C
ANISOU 265 CA PRO A 34 9171 7973 11550 1374 72 1183 C
ATOM 266 C PRO A 34 34.143 369.486 55.158 1.00 76.57 C
ANISOU 266 C PRO A 34 9380 8201 11512 1313 105 1196 C
ATOM 267 O PRO A 34 33.294 370.048 54.458 1.00 79.47 O
ANISOU 267 O PRO A 34 9666 8638 11890 1189 244 1152 O
ATOM 268 CB PRO A 34 34.581 367.001 55.257 1.00 72.88 C
ANISOU 268 CB PRO A 34 9036 7483 11172 1436 117 1310 C
ATOM 269 CG PRO A 34 35.780 366.205 55.165 1.00 61.04 C
ANISOU 269 CG PRO A 34 7488 5905 9799 1561 -19 1297 C
ATOM 270 CD PRO A 34 36.962 367.141 55.221 1.00 61.07 C
ANISOU 270 CD PRO A 34 7346 6009 9850 1625 -217 1211 C
ATOM 271 N TRP A 35 34.418 369.878 56.408 1.00 72.29 N
ANISOU 271 N TRP A 35 9000 7660 10806 1413 -32 1246 N
ATOM 272 CA TRP A 35 33.698 370.997 57.008 1.00 72.72 C
ANISOU 272 CA TRP A 35 9150 7796 10683 1378 -1 1248 C
ATOM 273 C TRP A 35 33.826 372.279 56.196 1.00 76.57 C
ANISOU 273 C TRP A 35 9433 8408 11253 1282 -17 1124 C
ATOM 274 O TRP A 35 32.914 373.115 56.218 1.00 88.30 O
ANISOU 274 O TRP A 35 10944 9960 12647 1207 88 1115 O
ATOM 275 CB TRP A 35 34.153 371.208 58.454 1.00 79.26 C
ANISOU 275 CB TRP A 35 10206 8598 11310 1528 -185 1299 C
ATOM 276 CG TRP A 35 35.479 371.889 58.651 1.00 85.63 C
ANISOU 276 CG TRP A 35 10918 9441 12175 1607 -471 1200 C
ATOM 277 CD1 TRP A 35 36.664 371.279 58.953 1.00 78.84 C
ANISOU 277 CD1 TRP A 35 10044 8515 11396 1733 -687 1200 C
ATOM 278 CD2 TRP A 35 35.757 373.295 58.599 1.00 86.56 C
ANISOU 278 CD2 TRP A 35 10936 9654 12300 1566 -583 1089 C
ATOM 279 NE1 TRP A 35 37.655 372.209 59.086 1.00 75.37 N
ANISOU 279 NE1 TRP A 35 9482 8123 11031 1766 -930 1093 N
ATOM 280 CE2 TRP A 35 37.128 373.456 58.871 1.00 80.76 C
ANISOU 280 CE2 TRP A 35 10114 8899 11672 1660 -869 1024 C
ATOM 281 CE3 TRP A 35 34.982 374.433 58.349 1.00 84.66 C
ANISOU 281 CE3 TRP A 35 10664 9501 12003 1460 -475 1039 C
ATOM 282 CZ2 TRP A 35 37.741 374.705 58.893 1.00 72.65 C
ANISOU 282 CZ2 TRP A 35 8964 7927 10712 1637 -1047 910 C
ATOM 283 CZ3 TRP A 35 35.592 375.671 58.373 1.00 70.60 C
ANISOU 283 CZ3 TRP A 35 8782 7774 10268 1447 -646 930 C
ATOM 284 CH2 TRP A 35 36.958 375.796 58.643 1.00 66.97 C
ANISOU 284 CH2 TRP A 35 8233 7284 9930 1528 -928 866 C
ATOM 285 N GLN A 36 34.921 372.454 55.464 1.00 74.95 N
ANISOU 285 N GLN A 36 9021 8228 11230 1286 -129 1036 N
ATOM 286 CA GLN A 36 35.007 373.638 54.623 1.00 65.92 C
ANISOU 286 CA GLN A 36 7688 7186 10173 1190 -110 938 C
ATOM 287 C GLN A 36 34.154 373.508 53.376 1.00 66.99 C
ANISOU 287 C GLN A 36 7722 7356 10377 1070 106 917 C
ATOM 288 O GLN A 36 33.614 374.514 52.896 1.00 66.68 O
ANISOU 288 O GLN A 36 7617 7397 10320 982 177 873 O
ATOM 289 CB GLN A 36 36.462 373.905 54.252 1.00 70.20 C
ANISOU 289 CB GLN A 36 8030 7736 10907 1233 -275 865 C
ATOM 290 CG GLN A 36 37.266 374.292 55.470 1.00 78.94 C
ANISOU 290 CG GLN A 36 9219 8816 11958 1341 -535 859 C
ATOM 291 CD GLN A 36 38.743 374.130 55.292 1.00 84.20 C
ANISOU 291 CD GLN A 36 9693 9451 12849 1412 -718 812 C
ATOM 292 OE1 GLN A 36 39.209 373.460 54.368 1.00 82.77 O
ANISOU 292 OE1 GLN A 36 9349 9253 12848 1410 -632 803 O
ATOM 293 NE2 GLN A 36 39.501 374.728 56.195 1.00 93.76 N
ANISOU 293 NE2 GLN A 36 10920 10646 14056 1486 -980 775 N
ATOM 294 N PHE A 37 33.968 372.289 52.862 1.00 70.09 N
ANISOU 294 N PHE A 37 8115 7676 10839 1069 200 944 N
ATOM 295 CA PHE A 37 32.986 372.126 51.796 1.00 63.94 C
ANISOU 295 CA PHE A 37 7280 6916 10100 960 379 917 C
ATOM 296 C PHE A 37 31.576 372.374 52.323 1.00 69.30 C
ANISOU 296 C PHE A 37 8081 7603 10648 895 492 976 C
ATOM 297 O PHE A 37 30.736 372.958 51.626 1.00 64.77 O
ANISOU 297 O PHE A 37 7439 7092 10080 799 592 937 O
ATOM 298 CB PHE A 37 33.086 370.740 51.180 1.00 52.88 C
ANISOU 298 CB PHE A 37 5868 5415 8807 979 434 919 C
ATOM 299 CG PHE A 37 34.160 370.609 50.159 1.00 69.61 C
ANISOU 299 CG PHE A 37 7826 7548 11074 1016 407 836 C
ATOM 300 CD1 PHE A 37 35.449 370.249 50.544 1.00 70.82 C
ANISOU 300 CD1 PHE A 37 7939 7660 11310 1132 277 842 C
ATOM 301 CD2 PHE A 37 33.908 370.883 48.818 1.00 63.03 C
ANISOU 301 CD2 PHE A 37 6883 6770 10295 950 511 755 C
ATOM 302 CE1 PHE A 37 36.465 370.128 49.601 1.00 74.37 C
ANISOU 302 CE1 PHE A 37 8221 8120 11917 1177 281 773 C
ATOM 303 CE2 PHE A 37 34.933 370.770 47.868 1.00 65.57 C
ANISOU 303 CE2 PHE A 37 7069 7104 10740 1002 520 688 C
ATOM 304 CZ PHE A 37 36.208 370.396 48.266 1.00 69.70 C
ANISOU 304 CZ PHE A 37 7533 7585 11366 1113 419 700 C
ATOM 305 N SER A 38 31.305 371.945 53.560 1.00 57.91 N
ANISOU 305 N SER A 38 6822 6094 9086 956 482 1077 N
ATOM 306 CA SER A 38 30.013 372.225 54.171 1.00 63.69 C
ANISOU 306 CA SER A 38 7671 6832 9696 910 616 1146 C
ATOM 307 C SER A 38 29.780 373.723 54.322 1.00 70.97 C
ANISOU 307 C SER A 38 8569 7869 10527 886 595 1095 C
ATOM 308 O SER A 38 28.661 374.206 54.102 1.00 70.19 O
ANISOU 308 O SER A 38 8449 7812 10408 807 729 1097 O
ATOM 309 CB SER A 38 29.910 371.540 55.527 1.00 54.95 C
ANISOU 309 CB SER A 38 6794 5632 8455 1007 621 1277 C
ATOM 310 OG SER A 38 30.156 370.171 55.383 1.00 64.17 O
ANISOU 310 OG SER A 38 7986 6677 9720 1032 635 1328 O
ATOM 311 N MET A 39 30.822 374.468 54.720 1.00 71.60 N
ANISOU 311 N MET A 39 8648 7991 10568 956 418 1046 N
ATOM 312 CA MET A 39 30.697 375.915 54.868 1.00 51.94 C
ANISOU 312 CA MET A 39 6140 5589 8008 935 378 987 C
ATOM 313 C MET A 39 30.487 376.563 53.513 1.00 61.03 C
ANISOU 313 C MET A 39 7088 6813 9288 825 446 907 C
ATOM 314 O MET A 39 29.717 377.528 53.387 1.00 53.32 O
ANISOU 314 O MET A 39 6099 5897 8264 773 514 884 O
ATOM 315 CB MET A 39 31.909 376.498 55.563 1.00 53.62 C
ANISOU 315 CB MET A 39 6382 5802 8188 1026 147 941 C
ATOM 316 CG MET A 39 31.979 376.184 57.039 1.00 67.92 C
ANISOU 316 CG MET A 39 8447 7556 9803 1155 58 1011 C
ATOM 317 SD MET A 39 30.499 376.612 57.954 1.00 71.46 S
ANISOU 317 SD MET A 39 9121 8018 10012 1167 238 1084 S
ATOM 318 CE MET A 39 30.146 378.270 57.303 1.00 70.05 C
ANISOU 318 CE MET A 39 8796 7943 9876 1071 252 969 C
ATOM 319 N LEU A 40 31.140 376.023 52.477 1.00 60.41 N
ANISOU 319 N LEU A 40 6863 6724 9364 804 437 867 N
ATOM 320 CA LEU A 40 30.769 376.423 51.126 1.00 65.79 C
ANISOU 320 CA LEU A 40 7397 7465 10136 713 532 807 C
ATOM 321 C LEU A 40 29.287 376.188 50.885 1.00 71.11 C
ANISOU 321 C LEU A 40 8107 8139 10774 643 682 835 C
ATOM 322 O LEU A 40 28.601 377.055 50.330 1.00 70.13 O
ANISOU 322 O LEU A 40 7924 8080 10643 581 739 800 O
ATOM 323 CB LEU A 40 31.585 375.631 50.105 1.00 62.72 C
ANISOU 323 CB LEU A 40 6892 7049 9889 725 530 769 C
ATOM 324 CG LEU A 40 31.332 375.975 48.631 1.00 59.73 C
ANISOU 324 CG LEU A 40 6392 6726 9576 659 623 705 C
ATOM 325 CD1 LEU A 40 31.313 377.454 48.313 1.00 47.87 C
ANISOU 325 CD1 LEU A 40 4821 5309 8057 617 622 673 C
ATOM 326 CD2 LEU A 40 32.267 375.177 47.715 1.00 79.97 C
ANISOU 326 CD2 LEU A 40 8868 9257 12258 701 632 666 C
ATOM 327 N ALA A 41 28.766 375.040 51.339 1.00 67.93 N
ANISOU 327 N ALA A 41 7795 7651 10363 652 744 903 N
ATOM 328 CA ALA A 41 27.349 374.739 51.165 1.00 62.53 C
ANISOU 328 CA ALA A 41 7119 6947 9693 576 886 936 C
ATOM 329 C ALA A 41 26.501 375.733 51.933 1.00 68.07 C
ANISOU 329 C ALA A 41 7882 7701 10282 570 948 971 C
ATOM 330 O ALA A 41 25.502 376.243 51.420 1.00 68.22 O
ANISOU 330 O ALA A 41 7826 7763 10332 502 1030 949 O
ATOM 331 CB ALA A 41 27.049 373.316 51.633 1.00 60.68 C
ANISOU 331 CB ALA A 41 6972 6587 9496 586 947 1019 C
ATOM 332 N ALA A 42 26.877 375.990 53.189 1.00 62.72 N
ANISOU 332 N ALA A 42 7351 7013 9467 656 901 1024 N
ATOM 333 CA ALA A 42 26.124 376.910 54.027 1.00 50.00 C
ANISOU 333 CA ALA A 42 5833 5441 7722 678 967 1054 C
ATOM 334 C ALA A 42 26.067 378.308 53.426 1.00 66.40 C
ANISOU 334 C ALA A 42 7807 7614 9807 641 928 963 C
ATOM 335 O ALA A 42 25.010 378.950 53.418 1.00 76.97 O
ANISOU 335 O ALA A 42 9130 8990 11125 609 1035 968 O
ATOM 336 CB ALA A 42 26.758 376.981 55.417 1.00 51.31 C
ANISOU 336 CB ALA A 42 6205 5578 7713 801 879 1101 C
ATOM 337 N TYR A 43 27.186 378.781 52.889 1.00 59.08 N
ANISOU 337 N TYR A 43 6798 6719 8930 645 785 887 N
ATOM 338 CA TYR A 43 27.211 380.088 52.252 1.00 62.76 C
ANISOU 338 CA TYR A 43 7167 7257 9421 606 755 814 C
ATOM 339 C TYR A 43 26.235 380.120 51.073 1.00 66.59 C
ANISOU 339 C TYR A 43 7530 7778 9994 521 868 795 C
ATOM 340 O TYR A 43 25.493 381.094 50.890 1.00 77.02 O
ANISOU 340 O TYR A 43 8824 9147 11294 497 913 776 O
ATOM 341 CB TYR A 43 28.636 380.412 51.810 1.00 69.80 C
ANISOU 341 CB TYR A 43 7970 8156 10396 618 609 755 C
ATOM 342 CG TYR A 43 28.776 381.783 51.232 1.00 69.44 C
ANISOU 342 CG TYR A 43 7835 8163 10386 579 581 696 C
ATOM 343 CD1 TYR A 43 28.167 382.850 51.869 1.00 70.26 C
ANISOU 343 CD1 TYR A 43 8018 8285 10392 591 585 686 C
ATOM 344 CD2 TYR A 43 29.475 382.024 50.065 1.00 78.68 C
ANISOU 344 CD2 TYR A 43 8857 9355 11684 538 570 657 C
ATOM 345 CE1 TYR A 43 28.269 384.123 51.387 1.00 78.53 C
ANISOU 345 CE1 TYR A 43 8997 9361 11479 558 558 637 C
ATOM 346 CE2 TYR A 43 29.579 383.311 49.563 1.00 79.37 C
ANISOU 346 CE2 TYR A 43 8876 9475 11806 503 560 622 C
ATOM 347 CZ TYR A 43 28.967 384.349 50.232 1.00 82.32 C
ANISOU 347 CZ TYR A 43 9329 9856 12093 509 546 612 C
ATOM 348 OH TYR A 43 29.067 385.626 49.760 1.00 94.29 O
ANISOU 348 OH TYR A 43 10786 11386 13654 476 534 581 O
ATOM 349 N MET A 44 26.242 379.062 50.248 1.00 63.64 N
ANISOU 349 N MET A 44 7087 7374 9719 485 896 792 N
ATOM 350 CA MET A 44 25.311 378.962 49.122 1.00 68.04 C
ANISOU 350 CA MET A 44 7545 7952 10354 414 968 761 C
ATOM 351 C MET A 44 23.861 378.952 49.612 1.00 75.51 C
ANISOU 351 C MET A 44 8510 8887 11293 385 1081 809 C
ATOM 352 O MET A 44 22.963 379.477 48.942 1.00 71.84 O
ANISOU 352 O MET A 44 7962 8462 10871 341 1118 779 O
ATOM 353 CB MET A 44 25.608 377.689 48.313 1.00 68.11 C
ANISOU 353 CB MET A 44 7513 7906 10458 396 961 739 C
ATOM 354 CG MET A 44 26.904 377.645 47.500 1.00 68.00 C
ANISOU 354 CG MET A 44 7447 7908 10482 427 890 684 C
ATOM 355 SD MET A 44 27.198 379.026 46.383 1.00 75.11 S
ANISOU 355 SD MET A 44 8260 8903 11378 413 877 624 S
ATOM 356 CE MET A 44 28.399 379.906 47.353 1.00 73.41 C
ANISOU 356 CE MET A 44 8055 8698 11140 458 793 644 C
ATOM 357 N PHE A 45 23.600 378.280 50.736 1.00 71.77 N
ANISOU 357 N PHE A 45 8140 8351 10778 413 1146 892 N
ATOM 358 CA PHE A 45 22.249 378.269 51.279 1.00 68.48 C
ANISOU 358 CA PHE A 45 7731 7916 10372 391 1292 956 C
ATOM 359 C PHE A 45 21.816 379.681 51.662 1.00 67.85 C
ANISOU 359 C PHE A 45 7669 7911 10202 424 1317 941 C
ATOM 360 O PHE A 45 20.714 380.123 51.311 1.00 62.39 O
ANISOU 360 O PHE A 45 6884 7245 9575 386 1396 934 O
ATOM 361 CB PHE A 45 22.205 377.309 52.469 1.00 68.37 C
ANISOU 361 CB PHE A 45 7855 7814 10308 433 1377 1066 C
ATOM 362 CG PHE A 45 20.826 377.079 53.038 1.00 68.71 C
ANISOU 362 CG PHE A 45 7896 7816 10395 408 1571 1157 C
ATOM 363 CD1 PHE A 45 19.828 376.485 52.283 1.00 62.86 C
ANISOU 363 CD1 PHE A 45 6998 7030 9853 308 1642 1155 C
ATOM 364 CD2 PHE A 45 20.568 377.365 54.373 1.00 67.92 C
ANISOU 364 CD2 PHE A 45 7958 7707 10142 492 1685 1248 C
ATOM 365 CE1 PHE A 45 18.576 376.263 52.823 1.00 59.50 C
ANISOU 365 CE1 PHE A 45 6538 6557 9513 278 1834 1247 C
ATOM 366 CE2 PHE A 45 19.318 377.117 54.930 1.00 65.32 C
ANISOU 366 CE2 PHE A 45 7621 7332 9864 476 1904 1350 C
ATOM 367 CZ PHE A 45 18.324 376.570 54.157 1.00 56.21 C
ANISOU 367 CZ PHE A 45 6273 6135 8948 363 1985 1354 C
ATOM 368 N LEU A 46 22.712 380.423 52.315 1.00 64.64 N
ANISOU 368 N LEU A 46 7369 7529 9660 496 1229 923 N
ATOM 369 CA LEU A 46 22.457 381.821 52.650 1.00 65.82 C
ANISOU 369 CA LEU A 46 7551 7734 9724 534 1227 890 C
ATOM 370 C LEU A 46 22.114 382.631 51.402 1.00 70.46 C
ANISOU 370 C LEU A 46 7985 8379 10407 475 1200 821 C
ATOM 371 O LEU A 46 21.138 383.392 51.386 1.00 63.03 O
ANISOU 371 O LEU A 46 7010 7467 9471 476 1275 818 O
ATOM 372 CB LEU A 46 23.668 382.400 53.378 1.00 60.67 C
ANISOU 372 CB LEU A 46 7023 7080 8950 609 1083 857 C
ATOM 373 CG LEU A 46 23.528 383.831 53.853 1.00 58.75 C
ANISOU 373 CG LEU A 46 6844 6866 8610 657 1056 811 C
ATOM 374 CD1 LEU A 46 22.401 383.861 54.847 1.00 54.84 C
ANISOU 374 CD1 LEU A 46 6467 6361 8008 718 1222 874 C
ATOM 375 CD2 LEU A 46 24.815 384.234 54.540 1.00 57.41 C
ANISOU 375 CD2 LEU A 46 6785 6672 8354 721 874 766 C
ATOM 376 N LEU A 47 22.925 382.502 50.350 1.00 67.54 N
ANISOU 376 N LEU A 47 7533 8023 10107 437 1101 770 N
ATOM 377 CA LEU A 47 22.654 383.271 49.144 1.00 62.60 C
ANISOU 377 CA LEU A 47 6795 7448 9542 398 1078 716 C
ATOM 378 C LEU A 47 21.316 382.876 48.530 1.00 62.76 C
ANISOU 378 C LEU A 47 6722 7472 9653 351 1155 722 C
ATOM 379 O LEU A 47 20.619 383.727 47.975 1.00 69.14 O
ANISOU 379 O LEU A 47 7466 8319 10484 346 1160 696 O
ATOM 380 CB LEU A 47 23.802 383.101 48.145 1.00 65.64 C
ANISOU 380 CB LEU A 47 7128 7841 9972 380 989 674 C
ATOM 381 CG LEU A 47 25.124 383.734 48.623 1.00 65.65 C
ANISOU 381 CG LEU A 47 7171 7835 9937 416 897 660 C
ATOM 382 CD1 LEU A 47 26.298 383.266 47.790 1.00 68.83 C
ANISOU 382 CD1 LEU A 47 7507 8231 10412 406 846 638 C
ATOM 383 CD2 LEU A 47 25.053 385.257 48.651 1.00 61.78 C
ANISOU 383 CD2 LEU A 47 6684 7371 9420 423 872 636 C
ATOM 384 N ILE A 48 20.964 381.585 48.561 1.00 75.84 N
ANISOU 384 N ILE A 48 8359 9075 11382 318 1200 751 N
ATOM 385 CA ILE A 48 19.664 381.137 48.040 1.00 75.25 C
ANISOU 385 CA ILE A 48 8174 8983 11436 263 1256 751 C
ATOM 386 C ILE A 48 18.522 381.717 48.875 1.00 75.35 C
ANISOU 386 C ILE A 48 8171 9002 11455 282 1379 802 C
ATOM 387 O ILE A 48 17.553 382.275 48.343 1.00 65.80 O
ANISOU 387 O ILE A 48 6853 7822 10325 267 1388 778 O
ATOM 388 CB ILE A 48 19.585 379.603 47.988 1.00 69.66 C
ANISOU 388 CB ILE A 48 7451 8189 10828 216 1276 773 C
ATOM 389 CG1 ILE A 48 20.553 379.050 46.938 1.00 71.17 C
ANISOU 389 CG1 ILE A 48 7641 8374 11027 208 1162 703 C
ATOM 390 CG2 ILE A 48 18.172 379.213 47.601 1.00 59.86 C
ANISOU 390 CG2 ILE A 48 6077 6912 9755 151 1326 772 C
ATOM 391 CD1 ILE A 48 21.021 377.639 47.210 1.00 62.33 C
ANISOU 391 CD1 ILE A 48 6567 7160 9956 197 1169 729 C
ATOM 392 N MET A 49 18.614 381.581 50.203 1.00 72.47 N
ANISOU 392 N MET A 49 7924 8608 11003 329 1477 877 N
ATOM 393 CA MET A 49 17.493 381.951 51.054 1.00 66.71 C
ANISOU 393 CA MET A 49 7194 7874 10281 359 1638 939 C
ATOM 394 C MET A 49 17.272 383.450 51.083 1.00 72.50 C
ANISOU 394 C MET A 49 7934 8674 10940 416 1624 896 C
ATOM 395 O MET A 49 16.137 383.892 51.276 1.00 79.93 O
ANISOU 395 O MET A 49 8801 9624 11946 432 1739 919 O
ATOM 396 CB MET A 49 17.705 381.441 52.481 1.00 74.55 C
ANISOU 396 CB MET A 49 8356 8815 11154 420 1756 1035 C
ATOM 397 CG MET A 49 17.772 379.928 52.673 1.00 80.34 C
ANISOU 397 CG MET A 49 9103 9458 11965 375 1809 1107 C
ATOM 398 SD MET A 49 16.141 379.162 52.421 1.00 80.64 S
ANISOU 398 SD MET A 49 8944 9427 12267 281 1985 1171 S
ATOM 399 CE MET A 49 16.112 378.878 50.644 1.00 81.60 C
ANISOU 399 CE MET A 49 8870 9558 12575 177 1789 1044 C
ATOM 400 N LEU A 50 18.319 384.243 50.873 1.00 73.31 N
ANISOU 400 N LEU A 50 8109 8812 10934 447 1490 836 N
ATOM 401 CA LEU A 50 18.149 385.685 50.745 1.00 67.74 C
ANISOU 401 CA LEU A 50 7405 8151 10183 491 1460 790 C
ATOM 402 C LEU A 50 17.920 386.093 49.294 1.00 71.55 C
ANISOU 402 C LEU A 50 7747 8670 10769 443 1369 735 C
ATOM 403 O LEU A 50 17.079 386.949 49.012 1.00 87.90 O
ANISOU 403 O LEU A 50 9751 10765 12880 466 1391 720 O
ATOM 404 CB LEU A 50 19.392 386.406 51.271 1.00 60.34 C
ANISOU 404 CB LEU A 50 6612 7212 9102 542 1355 755 C
ATOM 405 CG LEU A 50 19.735 386.266 52.761 1.00 61.20 C
ANISOU 405 CG LEU A 50 6908 7285 9058 622 1396 789 C
ATOM 406 CD1 LEU A 50 20.998 387.060 53.112 1.00 48.32 C
ANISOU 406 CD1 LEU A 50 5391 5644 7325 662 1235 727 C
ATOM 407 CD2 LEU A 50 18.586 386.578 53.716 1.00 53.26 C
ANISOU 407 CD2 LEU A 50 5968 6275 7994 696 1574 835 C
ATOM 408 N GLY A 51 18.617 385.455 48.362 1.00 62.58 N
ANISOU 408 N GLY A 51 6573 7534 9669 391 1273 706 N
ATOM 409 CA GLY A 51 18.586 385.869 46.976 1.00 59.66 C
ANISOU 409 CA GLY A 51 6122 7198 9347 368 1181 656 C
ATOM 410 C GLY A 51 17.354 385.498 46.190 1.00 68.10 C
ANISOU 410 C GLY A 51 7059 8271 10545 337 1181 640 C
ATOM 411 O GLY A 51 16.932 386.278 45.334 1.00 72.71 O
ANISOU 411 O GLY A 51 7592 8887 11146 355 1120 608 O
ATOM 412 N PHE A 52 16.787 384.308 46.422 1.00 75.99 N
ANISOU 412 N PHE A 52 8000 9226 11647 290 1233 662 N
ATOM 413 CA PHE A 52 15.544 383.963 45.735 1.00 76.65 C
ANISOU 413 CA PHE A 52 7931 9296 11895 253 1213 639 C
ATOM 414 C PHE A 52 14.413 384.899 46.135 1.00 75.92 C
ANISOU 414 C PHE A 52 7757 9226 11863 294 1287 662 C
ATOM 415 O PHE A 52 13.771 385.478 45.242 1.00 76.08 O
ANISOU 415 O PHE A 52 7687 9274 11945 309 1198 617 O
ATOM 416 CB PHE A 52 15.171 382.499 45.956 1.00 71.97 C
ANISOU 416 CB PHE A 52 7280 8627 11439 183 1258 662 C
ATOM 417 CG PHE A 52 13.848 382.151 45.360 1.00 71.68 C
ANISOU 417 CG PHE A 52 7062 8558 11614 135 1226 633 C
ATOM 418 CD1 PHE A 52 13.687 382.095 43.985 1.00 74.85 C
ANISOU 418 CD1 PHE A 52 7409 8972 12059 123 1047 538 C
ATOM 419 CD2 PHE A 52 12.744 381.950 46.165 1.00 74.20 C
ANISOU 419 CD2 PHE A 52 7264 8834 12093 113 1372 700 C
ATOM 420 CE1 PHE A 52 12.448 381.802 43.425 1.00 73.71 C
ANISOU 420 CE1 PHE A 52 7089 8791 12127 83 975 497 C
ATOM 421 CE2 PHE A 52 11.511 381.652 45.613 1.00 71.56 C
ANISOU 421 CE2 PHE A 52 6726 8461 12001 62 1329 670 C
ATOM 422 CZ PHE A 52 11.367 381.580 44.238 1.00 71.32 C
ANISOU 422 CZ PHE A 52 6636 8439 12024 46 1110 561 C
ATOM 423 N PRO A 53 14.072 385.053 47.421 1.00 75.05 N
ANISOU 423 N PRO A 53 7679 9100 11738 326 1451 730 N
ATOM 424 CA PRO A 53 12.899 385.884 47.741 1.00 80.54 C
ANISOU 424 CA PRO A 53 8277 9810 12513 375 1541 748 C
ATOM 425 C PRO A 53 13.042 387.314 47.240 1.00 87.07 C
ANISOU 425 C PRO A 53 9139 10690 13254 444 1450 701 C
ATOM 426 O PRO A 53 12.146 387.811 46.550 1.00 98.87 O
ANISOU 426 O PRO A 53 10504 12201 14860 462 1397 674 O
ATOM 427 CB PRO A 53 12.829 385.817 49.277 1.00 65.68 C
ANISOU 427 CB PRO A 53 6495 7903 10559 422 1746 830 C
ATOM 428 CG PRO A 53 13.588 384.615 49.639 1.00 74.17 C
ANISOU 428 CG PRO A 53 7657 8932 11592 371 1760 866 C
ATOM 429 CD PRO A 53 14.697 384.520 48.641 1.00 68.49 C
ANISOU 429 CD PRO A 53 6984 8235 10805 338 1563 794 C
ATOM 430 N ILE A 54 14.181 387.961 47.500 1.00 77.94 N
ANISOU 430 N ILE A 54 8148 9549 11916 479 1413 690 N
ATOM 431 CA ILE A 54 14.349 389.360 47.115 1.00 67.05 C
ANISOU 431 CA ILE A 54 6812 8196 10469 540 1343 657 C
ATOM 432 C ILE A 54 14.179 389.528 45.614 1.00 68.94 C
ANISOU 432 C ILE A 54 6969 8459 10765 522 1196 616 C
ATOM 433 O ILE A 54 13.446 390.406 45.149 1.00 86.33 O
ANISOU 433 O ILE A 54 9112 10676 13015 574 1160 603 O
ATOM 434 CB ILE A 54 15.722 389.880 47.575 1.00 74.91 C
ANISOU 434 CB ILE A 54 7980 9182 11301 558 1306 647 C
ATOM 435 CG1 ILE A 54 15.854 389.788 49.091 1.00 78.64 C
ANISOU 435 CG1 ILE A 54 8568 9627 11683 601 1423 677 C
ATOM 436 CG2 ILE A 54 15.941 391.307 47.122 1.00 84.13 C
ANISOU 436 CG2 ILE A 54 9188 10353 12425 606 1235 620 C
ATOM 437 CD1 ILE A 54 17.179 390.300 49.590 1.00 74.36 C
ANISOU 437 CD1 ILE A 54 8185 9065 11002 621 1348 652 C
ATOM 438 N ASN A 55 14.812 388.665 44.833 1.00 66.49 N
ANISOU 438 N ASN A 55 6666 8150 10445 464 1110 594 N
ATOM 439 CA ASN A 55 14.703 388.824 43.388 1.00 71.48 C
ANISOU 439 CA ASN A 55 7265 8804 11089 468 970 552 C
ATOM 440 C ASN A 55 13.361 388.326 42.875 1.00 76.13 C
ANISOU 440 C ASN A 55 7692 9388 11845 457 917 525 C
ATOM 441 O ASN A 55 12.808 388.897 41.927 1.00 72.55 O
ANISOU 441 O ASN A 55 7198 8954 11415 501 802 495 O
ATOM 442 CB ASN A 55 15.872 388.124 42.698 1.00 67.92 C
ANISOU 442 CB ASN A 55 6895 8354 10556 430 906 531 C
ATOM 443 CG ASN A 55 17.195 388.793 43.012 1.00 78.19 C
ANISOU 443 CG ASN A 55 8320 9656 11734 444 934 555 C
ATOM 444 OD1 ASN A 55 17.533 389.814 42.423 1.00 93.43 O
ANISOU 444 OD1 ASN A 55 10298 11596 13605 482 897 561 O
ATOM 445 ND2 ASN A 55 17.931 388.247 43.969 1.00 71.73 N
ANISOU 445 ND2 ASN A 55 7549 8815 10889 416 993 574 N
ATOM 446 N PHE A 56 12.829 387.252 43.461 1.00 75.62 N
ANISOU 446 N PHE A 56 7534 9288 11911 398 988 537 N
ATOM 447 CA PHE A 56 11.510 386.817 43.027 1.00 76.91 C
ANISOU 447 CA PHE A 56 7509 9430 12285 376 932 510 C
ATOM 448 C PHE A 56 10.459 387.859 43.387 1.00 76.97 C
ANISOU 448 C PHE A 56 7411 9453 12383 446 987 533 C
ATOM 449 O PHE A 56 9.598 388.196 42.564 1.00 74.31 O
ANISOU 449 O PHE A 56 6954 9123 12155 478 859 492 O
ATOM 450 CB PHE A 56 11.146 385.468 43.640 1.00 64.46 C
ANISOU 450 CB PHE A 56 5839 7788 10864 289 1022 533 C
ATOM 451 CG PHE A 56 9.808 384.995 43.215 1.00 70.80 C
ANISOU 451 CG PHE A 56 6419 8550 11931 251 958 502 C
ATOM 452 CD1 PHE A 56 9.634 384.365 41.992 1.00 76.54 C
ANISOU 452 CD1 PHE A 56 7097 9253 12730 215 744 411 C
ATOM 453 CD2 PHE A 56 8.697 385.251 44.011 1.00 73.15 C
ANISOU 453 CD2 PHE A 56 6553 8829 12412 262 1105 559 C
ATOM 454 CE1 PHE A 56 8.372 383.963 41.587 1.00 81.49 C
ANISOU 454 CE1 PHE A 56 7501 9830 13631 178 648 367 C
ATOM 455 CE2 PHE A 56 7.440 384.866 43.616 1.00 73.04 C
ANISOU 455 CE2 PHE A 56 6295 8770 12688 223 1040 531 C
ATOM 456 CZ PHE A 56 7.272 384.218 42.404 1.00 79.89 C
ANISOU 456 CZ PHE A 56 7101 9606 13648 176 795 431 C
ATOM 457 N LEU A 57 10.530 388.387 44.610 1.00 75.25 N
ANISOU 457 N LEU A 57 7245 9236 12111 484 1169 593 N
ATOM 458 CA LEU A 57 9.589 389.409 45.049 1.00 76.11 C
ANISOU 458 CA LEU A 57 7272 9353 12292 568 1250 614 C
ATOM 459 C LEU A 57 9.636 390.634 44.137 1.00 76.73 C
ANISOU 459 C LEU A 57 7393 9463 12297 647 1101 576 C
ATOM 460 O LEU A 57 8.606 391.262 43.879 1.00 86.88 O
ANISOU 460 O LEU A 57 8548 10752 13710 711 1071 568 O
ATOM 461 CB LEU A 57 9.884 389.773 46.502 1.00 77.72 C
ANISOU 461 CB LEU A 57 7593 9549 12388 613 1460 671 C
ATOM 462 CG LEU A 57 8.921 390.694 47.223 1.00 95.78 C
ANISOU 462 CG LEU A 57 9817 11834 14741 713 1603 697 C
ATOM 463 CD1 LEU A 57 7.549 390.036 47.216 1.00 96.78 C
ANISOU 463 CD1 LEU A 57 9683 11938 15151 685 1680 723 C
ATOM 464 CD2 LEU A 57 9.405 390.914 48.642 1.00104.34 C
ANISOU 464 CD2 LEU A 57 11079 12905 15662 764 1792 740 C
ATOM 465 N THR A 58 10.823 390.983 43.635 1.00 74.42 N
ANISOU 465 N THR A 58 7277 9187 11813 647 1016 562 N
ATOM 466 CA THR A 58 10.936 392.086 42.683 1.00 76.65 C
ANISOU 466 CA THR A 58 7618 9485 12020 718 886 545 C
ATOM 467 C THR A 58 10.102 391.828 41.432 1.00 80.30 C
ANISOU 467 C THR A 58 7962 9958 12589 732 706 501 C
ATOM 468 O THR A 58 9.450 392.739 40.911 1.00 87.47 O
ANISOU 468 O THR A 58 8833 10871 13531 819 621 497 O
ATOM 469 CB THR A 58 12.398 392.299 42.288 1.00 71.07 C
ANISOU 469 CB THR A 58 7100 8783 11122 698 846 549 C
ATOM 470 OG1 THR A 58 13.146 392.765 43.414 1.00 72.82 O
ANISOU 470 OG1 THR A 58 7429 8983 11254 700 968 576 O
ATOM 471 CG2 THR A 58 12.492 393.309 41.163 1.00 65.25 C
ANISOU 471 CG2 THR A 58 6430 8051 10313 767 725 550 C
ATOM 472 N LEU A 59 10.141 390.601 40.912 1.00 83.49 N
ANISOU 472 N LEU A 59 8322 10358 13043 657 626 463 N
ATOM 473 CA LEU A 59 9.304 390.264 39.769 1.00 81.91 C
ANISOU 473 CA LEU A 59 8014 10156 12951 673 424 401 C
ATOM 474 C LEU A 59 7.843 390.231 40.175 1.00 86.93 C
ANISOU 474 C LEU A 59 8403 10771 13856 683 438 397 C
ATOM 475 O LEU A 59 6.964 390.590 39.381 1.00 88.75 O
ANISOU 475 O LEU A 59 8529 11003 14191 745 267 357 O
ATOM 476 CB LEU A 59 9.750 388.933 39.164 1.00 85.92 C
ANISOU 476 CB LEU A 59 8552 10648 13446 592 331 345 C
ATOM 477 CG LEU A 59 11.236 388.945 38.794 1.00 84.56 C
ANISOU 477 CG LEU A 59 8605 10496 13026 591 349 356 C
ATOM 478 CD1 LEU A 59 11.690 387.678 38.081 1.00 76.05 C
ANISOU 478 CD1 LEU A 59 7576 9399 11920 537 254 291 C
ATOM 479 CD2 LEU A 59 11.467 390.158 37.898 1.00 83.01 C
ANISOU 479 CD2 LEU A 59 8535 10331 12676 695 260 369 C
ATOM 480 N TYR A 60 7.564 389.815 41.407 1.00 91.70 N
ANISOU 480 N TYR A 60 8911 11351 14579 632 645 444 N
ATOM 481 CA TYR A 60 6.181 389.582 41.792 1.00 90.81 C
ANISOU 481 CA TYR A 60 8534 11208 14763 626 692 450 C
ATOM 482 C TYR A 60 5.448 390.898 42.025 1.00 94.26 C
ANISOU 482 C TYR A 60 8904 11663 15249 749 734 475 C
ATOM 483 O TYR A 60 4.314 391.070 41.564 1.00101.55 O
ANISOU 483 O TYR A 60 9617 12573 16393 791 624 446 O
ATOM 484 CB TYR A 60 6.112 388.683 43.027 1.00 79.28 C
ANISOU 484 CB TYR A 60 7009 9707 13406 541 933 511 C
ATOM 485 CG TYR A 60 4.694 388.331 43.378 1.00 89.09 C
ANISOU 485 CG TYR A 60 7954 10904 14993 521 1009 530 C
ATOM 486 CD1 TYR A 60 3.978 387.413 42.622 1.00 93.74 C
ANISOU 486 CD1 TYR A 60 8339 11441 15837 442 837 471 C
ATOM 487 CD2 TYR A 60 4.068 388.908 44.474 1.00 94.75 C
ANISOU 487 CD2 TYR A 60 8589 11619 15793 585 1256 605 C
ATOM 488 CE1 TYR A 60 2.672 387.094 42.935 1.00 98.23 C
ANISOU 488 CE1 TYR A 60 8598 11955 16771 413 906 491 C
ATOM 489 CE2 TYR A 60 2.768 388.589 44.803 1.00 99.47 C
ANISOU 489 CE2 TYR A 60 8889 12170 16733 569 1358 635 C
ATOM 490 CZ TYR A 60 2.068 387.683 44.029 1.00103.83 C
ANISOU 490 CZ TYR A 60 9210 12668 17573 476 1181 582 C
ATOM 491 OH TYR A 60 0.763 387.363 44.355 1.00110.34 O
ANISOU 491 OH TYR A 60 9702 13433 18790 450 1284 615 O
ATOM 492 N VAL A 61 6.072 391.837 42.747 1.00 91.45 N
ANISOU 492 N VAL A 61 8718 11325 14705 813 881 521 N
ATOM 493 CA VAL A 61 5.415 393.115 42.992 1.00 88.96 C
ANISOU 493 CA VAL A 61 8360 11013 14429 940 926 538 C
ATOM 494 C VAL A 61 5.286 393.941 41.724 1.00 92.32 C
ANISOU 494 C VAL A 61 8818 11452 14809 1025 682 500 C
ATOM 495 O VAL A 61 4.422 394.817 41.651 1.00 99.36 O
ANISOU 495 O VAL A 61 9604 12335 15812 1134 657 503 O
ATOM 496 CB VAL A 61 6.152 393.926 44.071 1.00 79.96 C
ANISOU 496 CB VAL A 61 7417 9870 13092 991 1119 580 C
ATOM 497 CG1 VAL A 61 6.271 393.102 45.349 1.00 78.31 C
ANISOU 497 CG1 VAL A 61 7212 9648 12896 930 1355 624 C
ATOM 498 CG2 VAL A 61 7.498 394.392 43.560 1.00 81.54 C
ANISOU 498 CG2 VAL A 61 7868 10081 13034 983 1015 569 C
ATOM 499 N THR A 62 6.128 393.705 40.722 1.00 93.91 N
ANISOU 499 N THR A 62 9174 11669 14840 992 511 471 N
ATOM 500 CA THR A 62 5.954 394.416 39.461 1.00 97.03 C
ANISOU 500 CA THR A 62 9620 12072 15176 1085 282 446 C
ATOM 501 C THR A 62 4.702 393.938 38.731 1.00101.92 C
ANISOU 501 C THR A 62 10007 12684 16034 1104 81 387 C
ATOM 502 O THR A 62 4.047 394.721 38.031 1.00110.47 O
ANISOU 502 O THR A 62 11051 13765 17158 1221 -84 375 O
ATOM 503 CB THR A 62 7.215 394.268 38.612 1.00 92.00 C
ANISOU 503 CB THR A 62 9225 11450 14280 1056 190 442 C
ATOM 504 OG1 THR A 62 8.282 394.967 39.262 1.00 98.69 O
ANISOU 504 OG1 THR A 62 10255 12291 14953 1054 352 497 O
ATOM 505 CG2 THR A 62 7.029 394.840 37.223 1.00 85.29 C
ANISOU 505 CG2 THR A 62 8457 10607 13344 1159 -44 424 C
ATOM 506 N VAL A 63 4.329 392.672 38.923 1.00 92.92 N
ANISOU 506 N VAL A 63 8704 11528 15074 994 85 352 N
ATOM 507 CA VAL A 63 3.103 392.150 38.327 1.00 91.92 C
ANISOU 507 CA VAL A 63 8319 11375 15231 994 -114 286 C
ATOM 508 C VAL A 63 1.865 392.761 38.994 1.00 97.82 C
ANISOU 508 C VAL A 63 8804 12105 16258 1064 -15 317 C
ATOM 509 O VAL A 63 0.833 392.964 38.337 1.00 97.51 O
ANISOU 509 O VAL A 63 8573 12050 16425 1133 -223 271 O
ATOM 510 CB VAL A 63 3.126 390.607 38.388 1.00 78.97 C
ANISOU 510 CB VAL A 63 6583 9698 13724 842 -124 241 C
ATOM 511 CG1 VAL A 63 1.851 390.006 37.844 1.00 64.20 C
ANISOU 511 CG1 VAL A 63 4418 7778 12196 821 -338 164 C
ATOM 512 CG2 VAL A 63 4.305 390.080 37.590 1.00 72.79 C
ANISOU 512 CG2 VAL A 63 6062 8931 12663 804 -241 198 C
ATOM 513 N GLN A 64 1.941 393.079 40.289 1.00 96.91 N
ANISOU 513 N GLN A 64 8681 11989 16152 1063 295 393 N
ATOM 514 CA GLN A 64 0.779 393.545 41.040 1.00 97.54 C
ANISOU 514 CA GLN A 64 8510 12049 16503 1133 447 428 C
ATOM 515 C GLN A 64 0.595 395.058 41.050 1.00 94.58 C
ANISOU 515 C GLN A 64 8207 11685 16044 1303 453 451 C
ATOM 516 O GLN A 64 -0.471 395.526 41.470 1.00103.76 O
ANISOU 516 O GLN A 64 9144 12829 17450 1390 538 468 O
ATOM 517 CB GLN A 64 0.826 393.043 42.487 1.00 99.74 C
ANISOU 517 CB GLN A 64 8746 12311 16839 1064 802 500 C
ATOM 518 CG GLN A 64 0.553 391.560 42.612 1.00109.61 C
ANISOU 518 CG GLN A 64 9823 13520 18304 909 830 495 C
ATOM 519 CD GLN A 64 0.208 391.151 44.027 1.00112.20 C
ANISOU 519 CD GLN A 64 10047 13817 18765 872 1197 587 C
ATOM 520 OE1 GLN A 64 0.472 391.885 44.984 1.00112.22 O
ANISOU 520 OE1 GLN A 64 10188 13841 18610 957 1436 645 O
ATOM 521 NE2 GLN A 64 -0.396 389.978 44.168 1.00113.30 N
ANISOU 521 NE2 GLN A 64 9952 13898 19199 751 1245 601 N
ATOM 522 N HIS A 65 1.581 395.837 40.613 1.00 86.51 N
ANISOU 522 N HIS A 65 7479 10681 14708 1355 379 456 N
ATOM 523 CA HIS A 65 1.581 397.285 40.816 1.00 82.03 C
ANISOU 523 CA HIS A 65 7023 10104 14043 1503 431 489 C
ATOM 524 C HIS A 65 1.832 397.981 39.487 1.00 93.24 C
ANISOU 524 C HIS A 65 8591 11524 15312 1588 150 472 C
ATOM 525 O HIS A 65 2.948 397.927 38.965 1.00 94.07 O
ANISOU 525 O HIS A 65 8944 11641 15156 1542 88 478 O
ATOM 526 CB HIS A 65 2.631 397.682 41.852 1.00 64.10 C
ANISOU 526 CB HIS A 65 4990 7827 11537 1483 675 531 C
ATOM 527 CG HIS A 65 2.305 397.221 43.240 1.00 80.99 C
ANISOU 527 CG HIS A 65 7025 9960 13787 1448 969 560 C
ATOM 528 ND1 HIS A 65 1.631 398.009 44.150 1.00 89.91 N
ANISOU 528 ND1 HIS A 65 8086 11065 15009 1567 1168 584 N
ATOM 529 CD2 HIS A 65 2.503 396.028 43.853 1.00 92.60 C
ANISOU 529 CD2 HIS A 65 8451 11438 15294 1320 1107 575 C
ATOM 530 CE1 HIS A 65 1.467 397.337 45.277 1.00 99.28 C
ANISOU 530 CE1 HIS A 65 9211 12251 16259 1519 1429 617 C
ATOM 531 NE2 HIS A 65 1.986 396.132 45.122 1.00100.04 N
ANISOU 531 NE2 HIS A 65 9320 12364 16327 1366 1394 618 N
ATOM 532 N LYS A 66 0.786 398.609 38.928 1.00104.90 N
ANISOU 532 N LYS A 66 9915 12985 16960 1721 -14 457 N
ATOM 533 CA LYS A 66 0.881 399.148 37.571 1.00109.66 C
ANISOU 533 CA LYS A 66 10655 13584 17428 1817 -310 445 C
ATOM 534 C LYS A 66 1.971 400.205 37.467 1.00100.02 C
ANISOU 534 C LYS A 66 9763 12341 15898 1869 -249 506 C
ATOM 535 O LYS A 66 2.613 400.336 36.417 1.00 95.86 O
ANISOU 535 O LYS A 66 9448 11818 15157 1888 -417 518 O
ATOM 536 CB LYS A 66 -0.460 399.728 37.089 1.00117.84 C
ANISOU 536 CB LYS A 66 11467 14597 18709 1972 -501 424 C
ATOM 537 CG LYS A 66 -0.438 400.022 35.571 1.00123.80 C
ANISOU 537 CG LYS A 66 12367 15350 19320 2071 -855 404 C
ATOM 538 CD LYS A 66 -1.775 400.428 34.960 1.00129.71 C
ANISOU 538 CD LYS A 66 12888 16076 20319 2227 -1115 369 C
ATOM 539 CE LYS A 66 -1.747 400.296 33.422 1.00128.49 C
ANISOU 539 CE LYS A 66 12884 15928 20009 2301 -1503 327 C
ATOM 540 NZ LYS A 66 -1.566 398.887 32.931 1.00123.86 N
ANISOU 540 NZ LYS A 66 12269 15370 19421 2161 -1648 239 N
ATOM 541 N LYS A 67 2.195 400.968 38.536 1.00 92.78 N
ANISOU 541 N LYS A 67 8900 11393 14960 1898 -8 546 N
ATOM 542 CA LYS A 67 3.105 402.096 38.431 1.00 97.66 C
ANISOU 542 CA LYS A 67 9799 11963 15344 1954 28 599 C
ATOM 543 C LYS A 67 4.569 401.681 38.356 1.00103.19 C
ANISOU 543 C LYS A 67 10735 12676 15795 1821 87 619 C
ATOM 544 O LYS A 67 5.409 402.517 38.004 1.00106.96 O
ANISOU 544 O LYS A 67 11442 13108 16090 1851 82 669 O
ATOM 545 CB LYS A 67 2.877 403.051 39.607 1.00104.54 C
ANISOU 545 CB LYS A 67 10663 12781 16278 2033 244 615 C
ATOM 546 CG LYS A 67 1.484 403.671 39.627 1.00110.57 C
ANISOU 546 CG LYS A 67 11208 13519 17286 2196 198 605 C
ATOM 547 CD LYS A 67 1.327 404.599 38.425 1.00113.10 C
ANISOU 547 CD LYS A 67 11634 13796 17543 2335 -47 637 C
ATOM 548 CE LYS A 67 -0.049 405.231 38.351 1.00123.86 C
ANISOU 548 CE LYS A 67 12774 15129 19159 2513 -129 627 C
ATOM 549 NZ LYS A 67 -0.387 405.597 36.944 1.00131.64 N
ANISOU 549 NZ LYS A 67 13804 16101 20113 2628 -449 645 N
ATOM 550 N LEU A 68 4.903 400.429 38.684 1.00104.88 N
ANISOU 550 N LEU A 68 10891 12941 16017 1678 150 586 N
ATOM 551 CA LEU A 68 6.278 399.967 38.531 1.00 90.82 C
ANISOU 551 CA LEU A 68 9312 11174 14021 1563 190 601 C
ATOM 552 C LEU A 68 6.628 399.664 37.080 1.00 88.93 C
ANISOU 552 C LEU A 68 9187 10956 13646 1570 -20 602 C
ATOM 553 O LEU A 68 7.808 399.716 36.716 1.00 91.59 O
ANISOU 553 O LEU A 68 9730 11286 13783 1523 10 638 O
ATOM 554 CB LEU A 68 6.530 398.723 39.383 1.00 82.96 C
ANISOU 554 CB LEU A 68 8230 10215 13075 1422 327 570 C
ATOM 555 CG LEU A 68 6.351 398.871 40.896 1.00 80.31 C
ANISOU 555 CG LEU A 68 7834 9862 12818 1414 565 575 C
ATOM 556 CD1 LEU A 68 6.592 397.544 41.608 1.00 79.13 C
ANISOU 556 CD1 LEU A 68 7620 9744 12702 1283 684 561 C
ATOM 557 CD2 LEU A 68 7.268 399.947 41.445 1.00 65.42 C
ANISOU 557 CD2 LEU A 68 6162 7924 10769 1444 668 605 C
ATOM 558 N ARG A 69 5.632 399.377 36.237 1.00 80.59 N
ANISOU 558 N ARG A 69 8006 9918 12695 1638 -233 562 N
ATOM 559 CA ARG A 69 5.883 398.939 34.865 1.00 80.56 C
ANISOU 559 CA ARG A 69 8127 9938 12545 1658 -450 544 C
ATOM 560 C ARG A 69 6.147 400.125 33.931 1.00 85.41 C
ANISOU 560 C ARG A 69 8962 10514 12975 1798 -547 617 C
ATOM 561 O ARG A 69 5.498 400.311 32.903 1.00 84.05 O
ANISOU 561 O ARG A 69 8809 10341 12784 1919 -782 604 O
ATOM 562 CB ARG A 69 4.711 398.096 34.385 1.00 80.14 C
ANISOU 562 CB ARG A 69 7854 9908 12688 1673 -668 455 C
ATOM 563 CG ARG A 69 4.484 396.871 35.259 1.00 79.71 C
ANISOU 563 CG ARG A 69 7588 9872 12827 1524 -556 399 C
ATOM 564 CD ARG A 69 3.520 395.879 34.637 1.00 84.92 C
ANISOU 564 CD ARG A 69 8048 10536 13682 1508 -794 302 C
ATOM 565 NE ARG A 69 2.188 396.441 34.438 1.00 99.27 N
ANISOU 565 NE ARG A 69 9652 12334 15733 1627 -953 282 N
ATOM 566 CZ ARG A 69 1.216 396.431 35.348 1.00101.50 C
ANISOU 566 CZ ARG A 69 9637 12599 16328 1615 -841 281 C
ATOM 567 NH1 ARG A 69 0.039 396.962 35.056 1.00107.72 N
ANISOU 567 NH1 ARG A 69 10225 13367 17338 1737 -1005 261 N
ATOM 568 NH2 ARG A 69 1.421 395.913 36.549 1.00 98.43 N
ANISOU 568 NH2 ARG A 69 9158 12211 16031 1494 -559 307 N
ATOM 569 N THR A 70 7.198 400.887 34.263 1.00 95.47 N
ANISOU 569 N THR A 70 10421 11747 14105 1776 -370 697 N
ATOM 570 CA THR A 70 7.653 402.003 33.443 1.00106.24 C
ANISOU 570 CA THR A 70 12018 13055 15294 1885 -409 791 C
ATOM 571 C THR A 70 8.961 401.631 32.749 1.00109.24 C
ANISOU 571 C THR A 70 12623 13445 15438 1821 -357 837 C
ATOM 572 O THR A 70 9.715 400.792 33.254 1.00117.06 O
ANISOU 572 O THR A 70 13592 14469 16417 1683 -233 806 O
ATOM 573 CB THR A 70 7.866 403.282 34.268 1.00110.79 C
ANISOU 573 CB THR A 70 12636 13546 15913 1914 -249 855 C
ATOM 574 OG1 THR A 70 8.815 403.046 35.313 1.00114.30 O
ANISOU 574 OG1 THR A 70 13091 13983 16354 1772 -36 849 O
ATOM 575 CG2 THR A 70 6.557 403.728 34.897 1.00117.66 C
ANISOU 575 CG2 THR A 70 13297 14401 17008 2007 -283 814 C
ATOM 576 N PRO A 71 9.240 402.208 31.575 1.00101.10 N
ANISOU 576 N PRO A 71 11811 12384 14217 1931 -444 916 N
ATOM 577 CA PRO A 71 10.432 401.786 30.816 1.00100.32 C
ANISOU 577 CA PRO A 71 11924 12299 13894 1888 -377 964 C
ATOM 578 C PRO A 71 11.734 401.907 31.592 1.00 97.52 C
ANISOU 578 C PRO A 71 11607 11911 13535 1748 -120 1015 C
ATOM 579 O PRO A 71 12.601 401.033 31.470 1.00101.14 O
ANISOU 579 O PRO A 71 12107 12409 13912 1656 -42 998 O
ATOM 580 CB PRO A 71 10.400 402.710 29.592 1.00102.91 C
ANISOU 580 CB PRO A 71 12490 12576 14035 2057 -472 1071 C
ATOM 581 CG PRO A 71 8.978 403.026 29.418 1.00 99.21 C
ANISOU 581 CG PRO A 71 11907 12108 13680 2191 -703 1023 C
ATOM 582 CD PRO A 71 8.409 403.139 30.802 1.00 96.04 C
ANISOU 582 CD PRO A 71 11239 11701 13552 2115 -620 963 C
ATOM 583 N LEU A 72 11.891 402.956 32.403 1.00 94.49 N
ANISOU 583 N LEU A 72 11206 11446 13250 1735 -2 1067 N
ATOM 584 CA LEU A 72 13.107 403.116 33.190 1.00 95.52 C
ANISOU 584 CA LEU A 72 11361 11531 13402 1603 204 1100 C
ATOM 585 C LEU A 72 13.307 401.983 34.197 1.00 92.45 C
ANISOU 585 C LEU A 72 10813 11210 13104 1466 268 998 C
ATOM 586 O LEU A 72 14.404 401.852 34.761 1.00 80.54 O
ANISOU 586 O LEU A 72 9324 9679 11598 1355 408 1012 O
ATOM 587 CB LEU A 72 13.055 404.462 33.926 1.00 99.29 C
ANISOU 587 CB LEU A 72 11846 11894 13985 1628 276 1145 C
ATOM 588 CG LEU A 72 14.342 405.255 34.183 1.00104.58 C
ANISOU 588 CG LEU A 72 12632 12453 14651 1551 437 1232 C
ATOM 589 CD1 LEU A 72 15.261 405.282 32.960 1.00105.72 C
ANISOU 589 CD1 LEU A 72 12955 12577 14636 1559 490 1350 C
ATOM 590 CD2 LEU A 72 14.031 406.663 34.679 1.00101.21 C
ANISOU 590 CD2 LEU A 72 12236 11895 14325 1614 453 1268 C
ATOM 591 N ASN A 73 12.271 401.188 34.460 1.00 92.25 N
ANISOU 591 N ASN A 73 10624 11255 13171 1474 167 903 N
ATOM 592 CA ASN A 73 12.354 400.070 35.388 1.00 83.24 C
ANISOU 592 CA ASN A 73 9340 10169 12118 1354 231 820 C
ATOM 593 C ASN A 73 12.610 398.727 34.709 1.00 79.63 C
ANISOU 593 C ASN A 73 8889 9783 11586 1305 168 773 C
ATOM 594 O ASN A 73 12.949 397.764 35.404 1.00 82.82 O
ANISOU 594 O ASN A 73 9210 10217 12041 1197 240 723 O
ATOM 595 CB ASN A 73 11.096 400.008 36.254 1.00 80.12 C
ANISOU 595 CB ASN A 73 8746 9789 11908 1379 206 756 C
ATOM 596 CG ASN A 73 11.112 401.049 37.343 1.00 88.86 C
ANISOU 596 CG ASN A 73 9849 10829 13086 1394 330 777 C
ATOM 597 OD1 ASN A 73 12.136 401.686 37.579 1.00106.92 O
ANISOU 597 OD1 ASN A 73 12266 13054 15305 1358 423 824 O
ATOM 598 ND2 ASN A 73 9.992 401.226 38.020 1.00 93.54 N
ANISOU 598 ND2 ASN A 73 10290 11423 13829 1450 333 737 N
ATOM 599 N TYR A 74 12.458 398.634 33.382 1.00 74.40 N
ANISOU 599 N TYR A 74 8339 9137 10793 1392 33 785 N
ATOM 600 CA TYR A 74 12.683 397.361 32.699 1.00 74.94 C
ANISOU 600 CA TYR A 74 8437 9261 10777 1362 -39 722 C
ATOM 601 C TYR A 74 14.071 396.798 33.018 1.00 81.97 C
ANISOU 601 C TYR A 74 9387 10155 11604 1250 136 742 C
ATOM 602 O TYR A 74 14.224 395.593 33.244 1.00 85.19 O
ANISOU 602 O TYR A 74 9725 10599 12044 1171 136 669 O
ATOM 603 CB TYR A 74 12.511 397.506 31.182 1.00 72.23 C
ANISOU 603 CB TYR A 74 8275 8924 10244 1497 -197 741 C
ATOM 604 CG TYR A 74 11.113 397.781 30.668 1.00 82.07 C
ANISOU 604 CG TYR A 74 9461 10174 11547 1621 -437 697 C
ATOM 605 CD1 TYR A 74 10.082 398.139 31.527 1.00 96.01 C
ANISOU 605 CD1 TYR A 74 11010 11928 13541 1619 -470 667 C
ATOM 606 CD2 TYR A 74 10.823 397.668 29.307 1.00 85.96 C
ANISOU 606 CD2 TYR A 74 10119 10680 11862 1753 -636 682 C
ATOM 607 CE1 TYR A 74 8.799 398.394 31.045 1.00106.44 C
ANISOU 607 CE1 TYR A 74 12245 13248 14948 1738 -698 627 C
ATOM 608 CE2 TYR A 74 9.545 397.912 28.817 1.00 98.34 C
ANISOU 608 CE2 TYR A 74 11624 12246 13493 1875 -893 633 C
ATOM 609 CZ TYR A 74 8.536 398.278 29.690 1.00110.91 C
ANISOU 609 CZ TYR A 74 12965 13825 15349 1863 -925 607 C
ATOM 610 OH TYR A 74 7.262 398.529 29.212 1.00121.33 O
ANISOU 610 OH TYR A 74 14192 15139 16768 1989 -1186 559 O
ATOM 611 N ILE A 75 15.103 397.649 33.010 1.00 87.75 N
ANISOU 611 N ILE A 75 10240 10839 12264 1243 280 842 N
ATOM 612 CA ILE A 75 16.460 397.153 33.235 1.00 86.03 C
ANISOU 612 CA ILE A 75 10059 10618 12010 1146 435 864 C
ATOM 613 C ILE A 75 16.597 396.586 34.642 1.00 83.44 C
ANISOU 613 C ILE A 75 9573 10298 11834 1026 503 805 C
ATOM 614 O ILE A 75 17.421 395.694 34.881 1.00 84.25 O
ANISOU 614 O ILE A 75 9661 10419 11931 947 573 781 O
ATOM 615 CB ILE A 75 17.501 398.265 32.973 1.00 81.80 C
ANISOU 615 CB ILE A 75 9652 10009 11418 1154 576 990 C
ATOM 616 CG1 ILE A 75 18.892 397.659 32.753 1.00 72.61 C
ANISOU 616 CG1 ILE A 75 8539 8850 10202 1087 718 1020 C
ATOM 617 CG2 ILE A 75 17.526 399.276 34.112 1.00 74.71 C
ANISOU 617 CG2 ILE A 75 8682 9041 10666 1108 638 1014 C
ATOM 618 CD1 ILE A 75 18.982 396.782 31.510 1.00 68.92 C
ANISOU 618 CD1 ILE A 75 8193 8437 9558 1158 680 1002 C
ATOM 619 N LEU A 76 15.794 397.084 35.590 1.00 77.19 N
ANISOU 619 N LEU A 76 8672 9489 11168 1025 489 783 N
ATOM 620 CA LEU A 76 15.807 396.545 36.947 1.00 72.98 C
ANISOU 620 CA LEU A 76 8016 8962 10749 936 558 733 C
ATOM 621 C LEU A 76 15.168 395.165 37.017 1.00 81.25 C
ANISOU 621 C LEU A 76 8953 10065 11852 899 496 653 C
ATOM 622 O LEU A 76 15.594 394.325 37.816 1.00 86.51 O
ANISOU 622 O LEU A 76 9569 10741 12561 814 566 626 O
ATOM 623 CB LEU A 76 15.106 397.496 37.903 1.00 72.40 C
ANISOU 623 CB LEU A 76 7883 8850 10775 968 582 734 C
ATOM 624 CG LEU A 76 15.807 398.819 38.138 1.00 71.40 C
ANISOU 624 CG LEU A 76 7856 8641 10632 981 649 797 C
ATOM 625 CD1 LEU A 76 15.002 399.607 39.134 1.00 76.42 C
ANISOU 625 CD1 LEU A 76 8437 9238 11361 1027 667 774 C
ATOM 626 CD2 LEU A 76 17.200 398.560 38.667 1.00 66.02 C
ANISOU 626 CD2 LEU A 76 7212 7934 9937 881 742 807 C
ATOM 627 N LEU A 77 14.106 394.931 36.239 1.00 81.42 N
ANISOU 627 N LEU A 77 8932 10113 11892 963 353 615 N
ATOM 628 CA LEU A 77 13.558 393.582 36.154 1.00 83.93 C
ANISOU 628 CA LEU A 77 9146 10461 12282 918 275 534 C
ATOM 629 C LEU A 77 14.578 392.626 35.555 1.00 78.93 C
ANISOU 629 C LEU A 77 8615 9842 11533 876 286 515 C
ATOM 630 O LEU A 77 14.720 391.487 36.019 1.00 75.70 O
ANISOU 630 O LEU A 77 8139 9437 11188 796 313 468 O
ATOM 631 CB LEU A 77 12.271 393.577 35.333 1.00 88.36 C
ANISOU 631 CB LEU A 77 9640 11034 12900 999 81 485 C
ATOM 632 CG LEU A 77 11.099 394.359 35.912 1.00 89.44 C
ANISOU 632 CG LEU A 77 9631 11157 13196 1050 64 493 C
ATOM 633 CD1 LEU A 77 9.985 394.406 34.898 1.00 92.11 C
ANISOU 633 CD1 LEU A 77 9916 11501 13579 1145 -163 447 C
ATOM 634 CD2 LEU A 77 10.627 393.721 37.213 1.00 83.33 C
ANISOU 634 CD2 LEU A 77 8673 10379 12609 963 178 470 C
ATOM 635 N ASN A 78 15.270 393.068 34.501 1.00 76.77 N
ANISOU 635 N ASN A 78 8510 9569 11090 941 276 556 N
ATOM 636 CA ASN A 78 16.374 392.306 33.925 1.00 77.49 C
ANISOU 636 CA ASN A 78 8712 9669 11060 921 329 551 C
ATOM 637 C ASN A 78 17.401 391.942 34.983 1.00 77.36 C
ANISOU 637 C ASN A 78 8649 9641 11105 817 486 572 C
ATOM 638 O ASN A 78 17.875 390.802 35.042 1.00 72.83 O
ANISOU 638 O ASN A 78 8064 9074 10535 767 506 526 O
ATOM 639 CB ASN A 78 17.038 393.114 32.814 1.00 76.73 C
ANISOU 639 CB ASN A 78 8807 9566 10781 1013 362 629 C
ATOM 640 CG ASN A 78 17.870 392.267 31.896 1.00 82.27 C
ANISOU 640 CG ASN A 78 9640 10284 11336 1037 390 610 C
ATOM 641 OD1 ASN A 78 17.410 391.244 31.402 1.00 89.88 O
ANISOU 641 OD1 ASN A 78 10612 11267 12271 1056 265 511 O
ATOM 642 ND2 ASN A 78 19.109 392.687 31.656 1.00 88.07 N
ANISOU 642 ND2 ASN A 78 10472 11000 11989 1040 559 700 N
ATOM 643 N LEU A 79 17.768 392.917 35.817 1.00 77.98 N
ANISOU 643 N LEU A 79 8708 9690 11230 792 584 635 N
ATOM 644 CA LEU A 79 18.679 392.659 36.926 1.00 72.50 C
ANISOU 644 CA LEU A 79 7970 8977 10600 704 697 646 C
ATOM 645 C LEU A 79 18.155 391.542 37.817 1.00 72.14 C
ANISOU 645 C LEU A 79 7813 8945 10652 644 682 582 C
ATOM 646 O LEU A 79 18.910 390.648 38.214 1.00 75.71 O
ANISOU 646 O LEU A 79 8257 9394 11115 588 731 568 O
ATOM 647 CB LEU A 79 18.861 393.938 37.736 1.00 70.28 C
ANISOU 647 CB LEU A 79 7687 8650 10365 700 757 698 C
ATOM 648 CG LEU A 79 19.688 393.817 39.004 1.00 66.38 C
ANISOU 648 CG LEU A 79 7159 8128 9935 625 833 695 C
ATOM 649 CD1 LEU A 79 21.099 393.389 38.606 1.00 59.57 C
ANISOU 649 CD1 LEU A 79 6334 7257 9044 587 893 721 C
ATOM 650 CD2 LEU A 79 19.696 395.113 39.799 1.00 61.56 C
ANISOU 650 CD2 LEU A 79 6562 7460 9368 634 858 721 C
ATOM 651 N ALA A 80 16.858 391.585 38.146 1.00 82.93 N
ANISOU 651 N ALA A 80 9087 10319 12105 659 624 553 N
ATOM 652 CA ALA A 80 16.254 390.567 39.006 1.00 78.20 C
ANISOU 652 CA ALA A 80 8373 9719 11622 601 637 512 C
ATOM 653 C ALA A 80 16.336 389.192 38.356 1.00 78.14 C
ANISOU 653 C ALA A 80 8360 9715 11616 568 574 455 C
ATOM 654 O ALA A 80 16.632 388.193 39.026 1.00 79.59 O
ANISOU 654 O ALA A 80 8510 9881 11852 503 626 443 O
ATOM 655 CB ALA A 80 14.807 390.932 39.332 1.00 74.58 C
ANISOU 655 CB ALA A 80 7793 9260 11283 631 603 500 C
ATOM 656 N VAL A 81 16.005 389.114 37.061 1.00 74.33 N
ANISOU 656 N VAL A 81 7923 9246 11073 623 449 415 N
ATOM 657 CA VAL A 81 16.106 387.848 36.338 1.00 81.00 C
ANISOU 657 CA VAL A 81 8792 10081 11901 608 369 342 C
ATOM 658 C VAL A 81 17.550 387.348 36.328 1.00 83.09 C
ANISOU 658 C VAL A 81 9156 10343 12073 586 471 360 C
ATOM 659 O VAL A 81 17.816 386.157 36.550 1.00 71.74 O
ANISOU 659 O VAL A 81 7697 8879 10681 535 479 318 O
ATOM 660 CB VAL A 81 15.540 388.019 34.915 1.00 69.64 C
ANISOU 660 CB VAL A 81 7428 8657 10375 699 199 290 C
ATOM 661 CG1 VAL A 81 15.853 386.800 34.059 1.00 66.66 C
ANISOU 661 CG1 VAL A 81 7131 8263 9933 705 116 203 C
ATOM 662 CG2 VAL A 81 14.038 388.210 34.982 1.00 60.83 C
ANISOU 662 CG2 VAL A 81 6168 7535 9411 711 67 253 C
ATOM 663 N ALA A 82 18.507 388.250 36.097 1.00 82.48 N
ANISOU 663 N ALA A 82 9174 10279 11886 622 556 427 N
ATOM 664 CA ALA A 82 19.903 387.831 36.038 1.00 73.31 C
ANISOU 664 CA ALA A 82 8078 9111 10667 608 658 449 C
ATOM 665 C ALA A 82 20.333 387.242 37.368 1.00 68.85 C
ANISOU 665 C ALA A 82 7429 8522 10209 526 729 456 C
ATOM 666 O ALA A 82 20.953 386.174 37.417 1.00 73.04 O
ANISOU 666 O ALA A 82 7966 9035 10750 502 751 428 O
ATOM 667 CB ALA A 82 20.802 389.010 35.666 1.00 66.65 C
ANISOU 667 CB ALA A 82 7314 8269 9739 647 751 534 C
ATOM 668 N ASP A 83 19.971 387.910 38.461 1.00 64.03 N
ANISOU 668 N ASP A 83 6755 7905 9668 496 759 492 N
ATOM 669 CA ASP A 83 20.262 387.367 39.779 1.00 77.00 C
ANISOU 669 CA ASP A 83 8349 9524 11384 438 816 502 C
ATOM 670 C ASP A 83 19.645 385.991 39.982 1.00 75.92 C
ANISOU 670 C ASP A 83 8158 9366 11323 399 786 456 C
ATOM 671 O ASP A 83 20.201 385.174 40.724 1.00 78.00 O
ANISOU 671 O ASP A 83 8419 9601 11618 363 831 463 O
ATOM 672 CB ASP A 83 19.771 388.313 40.866 1.00 82.18 C
ANISOU 672 CB ASP A 83 8974 10175 12078 436 850 536 C
ATOM 673 CG ASP A 83 20.531 389.607 40.877 1.00 86.42 C
ANISOU 673 CG ASP A 83 9564 10703 12569 459 878 579 C
ATOM 674 OD1 ASP A 83 21.618 389.652 40.270 1.00 89.57 O
ANISOU 674 OD1 ASP A 83 10004 11097 12931 460 897 597 O
ATOM 675 OD2 ASP A 83 20.060 390.563 41.526 1.00 90.84 O
ANISOU 675 OD2 ASP A 83 10119 11251 13145 476 889 595 O
ATOM 676 N LEU A 84 18.474 385.732 39.388 1.00 71.55 N
ANISOU 676 N LEU A 84 7554 8813 10818 405 702 410 N
ATOM 677 CA LEU A 84 17.853 384.420 39.558 1.00 65.88 C
ANISOU 677 CA LEU A 84 6767 8051 10212 354 669 365 C
ATOM 678 C LEU A 84 18.593 383.340 38.769 1.00 72.16 C
ANISOU 678 C LEU A 84 7633 8821 10963 356 628 308 C
ATOM 679 O LEU A 84 18.709 382.205 39.243 1.00 70.78 O
ANISOU 679 O LEU A 84 7436 8592 10865 308 648 295 O
ATOM 680 CB LEU A 84 16.375 384.492 39.169 1.00 54.60 C
ANISOU 680 CB LEU A 84 5236 6618 8891 354 571 324 C
ATOM 681 CG LEU A 84 15.472 385.112 40.247 1.00 61.87 C
ANISOU 681 CG LEU A 84 6049 7541 9919 340 649 378 C
ATOM 682 CD1 LEU A 84 14.016 385.183 39.792 1.00 69.35 C
ANISOU 682 CD1 LEU A 84 6859 8480 11011 346 547 336 C
ATOM 683 CD2 LEU A 84 15.590 384.408 41.608 1.00 56.14 C
ANISOU 683 CD2 LEU A 84 5293 6774 9265 282 784 430 C
ATOM 684 N PHE A 85 19.135 383.681 37.591 1.00 72.52 N
ANISOU 684 N PHE A 85 7778 8897 10877 423 587 282 N
ATOM 685 CA PHE A 85 20.078 382.795 36.906 1.00 71.16 C
ANISOU 685 CA PHE A 85 7696 8705 10635 449 592 238 C
ATOM 686 C PHE A 85 21.258 382.448 37.799 1.00 74.93 C
ANISOU 686 C PHE A 85 8171 9165 11133 420 708 290 C
ATOM 687 O PHE A 85 21.702 381.296 37.834 1.00 77.36 O
ANISOU 687 O PHE A 85 8495 9426 11474 409 713 255 O
ATOM 688 CB PHE A 85 20.590 383.452 35.625 1.00 67.93 C
ANISOU 688 CB PHE A 85 7412 8339 10059 542 585 233 C
ATOM 689 CG PHE A 85 19.668 383.296 34.462 1.00 79.71 C
ANISOU 689 CG PHE A 85 8962 9832 11491 598 431 148 C
ATOM 690 CD1 PHE A 85 18.454 383.959 34.437 1.00 87.16 C
ANISOU 690 CD1 PHE A 85 9841 10790 12485 600 326 143 C
ATOM 691 CD2 PHE A 85 20.026 382.527 33.376 1.00 86.98 C
ANISOU 691 CD2 PHE A 85 10012 10736 12302 666 380 66 C
ATOM 692 CE1 PHE A 85 17.604 383.825 33.372 1.00 87.57 C
ANISOU 692 CE1 PHE A 85 9942 10838 12491 660 148 56 C
ATOM 693 CE2 PHE A 85 19.178 382.396 32.300 1.00 85.57 C
ANISOU 693 CE2 PHE A 85 9910 10552 12051 731 205 -27 C
ATOM 694 CZ PHE A 85 17.969 383.044 32.299 1.00 84.01 C
ANISOU 694 CZ PHE A 85 9637 10368 11916 726 76 -33 C
ATOM 695 N MET A 86 21.776 383.433 38.531 1.00 76.20 N
ANISOU 695 N MET A 86 8315 9353 11283 415 786 368 N
ATOM 696 CA MET A 86 22.873 383.152 39.445 1.00 68.64 C
ANISOU 696 CA MET A 86 7349 8375 10356 394 860 410 C
ATOM 697 C MET A 86 22.405 382.278 40.595 1.00 78.78 C
ANISOU 697 C MET A 86 8587 9611 11733 341 860 417 C
ATOM 698 O MET A 86 23.132 381.382 41.038 1.00 91.08 O
ANISOU 698 O MET A 86 10157 11128 13321 334 883 421 O
ATOM 699 CB MET A 86 23.434 384.458 39.991 1.00 66.60 C
ANISOU 699 CB MET A 86 7083 8141 10081 397 908 476 C
ATOM 700 CG MET A 86 24.226 385.274 38.993 1.00 76.36 C
ANISOU 700 CG MET A 86 8361 9401 11250 442 949 500 C
ATOM 701 SD MET A 86 24.563 386.901 39.678 1.00 83.75 S
ANISOU 701 SD MET A 86 9276 10337 12207 427 979 569 S
ATOM 702 CE MET A 86 25.604 386.465 41.073 1.00 89.05 C
ANISOU 702 CE MET A 86 9903 10969 12963 390 984 581 C
ATOM 703 N VAL A 87 21.203 382.540 41.107 1.00 81.07 N
ANISOU 703 N VAL A 87 8826 9902 12076 311 849 427 N
ATOM 704 CA VAL A 87 20.711 381.792 42.258 1.00 83.82 C
ANISOU 704 CA VAL A 87 9138 10200 12512 265 889 458 C
ATOM 705 C VAL A 87 20.481 380.326 41.891 1.00 86.46 C
ANISOU 705 C VAL A 87 9459 10463 12927 233 855 412 C
ATOM 706 O VAL A 87 20.811 379.420 42.666 1.00 86.33 O
ANISOU 706 O VAL A 87 9459 10387 12955 211 897 444 O
ATOM 707 CB VAL A 87 19.453 382.469 42.832 1.00 79.40 C
ANISOU 707 CB VAL A 87 8513 9654 12003 251 916 487 C
ATOM 708 CG1 VAL A 87 18.568 381.460 43.537 1.00 84.18 C
ANISOU 708 CG1 VAL A 87 9056 10193 12734 198 964 509 C
ATOM 709 CG2 VAL A 87 19.864 383.578 43.793 1.00 81.02 C
ANISOU 709 CG2 VAL A 87 8760 9889 12134 281 975 541 C
ATOM 710 N PHE A 88 19.949 380.066 40.695 1.00 74.76 N
ANISOU 710 N PHE A 88 7966 8978 11462 237 765 333 N
ATOM 711 CA PHE A 88 19.546 378.714 40.326 1.00 71.35 C
ANISOU 711 CA PHE A 88 7518 8460 11132 200 706 270 C
ATOM 712 C PHE A 88 20.574 378.001 39.462 1.00 75.89 C
ANISOU 712 C PHE A 88 8189 9013 11634 248 673 205 C
ATOM 713 O PHE A 88 20.872 376.829 39.707 1.00 81.74 O
ANISOU 713 O PHE A 88 8945 9668 12442 228 680 191 O
ATOM 714 CB PHE A 88 18.209 378.742 39.578 1.00 71.63 C
ANISOU 714 CB PHE A 88 7477 8483 11256 177 592 200 C
ATOM 715 CG PHE A 88 17.037 379.060 40.448 1.00 84.09 C
ANISOU 715 CG PHE A 88 8925 10051 12975 122 639 257 C
ATOM 716 CD1 PHE A 88 16.595 378.149 41.401 1.00 86.76 C
ANISOU 716 CD1 PHE A 88 9195 10299 13470 50 718 306 C
ATOM 717 CD2 PHE A 88 16.393 380.285 40.341 1.00 84.95 C
ANISOU 717 CD2 PHE A 88 8984 10232 13061 152 625 272 C
ATOM 718 CE1 PHE A 88 15.509 378.447 42.212 1.00 85.66 C
ANISOU 718 CE1 PHE A 88 8933 10149 13466 8 799 371 C
ATOM 719 CE2 PHE A 88 15.317 380.592 41.151 1.00 81.89 C
ANISOU 719 CE2 PHE A 88 8469 9835 12812 117 690 325 C
ATOM 720 CZ PHE A 88 14.874 379.671 42.084 1.00 84.84 C
ANISOU 720 CZ PHE A 88 8770 10125 13342 45 787 376 C
ATOM 721 N GLY A 89 21.160 378.692 38.484 1.00 68.80 N
ANISOU 721 N GLY A 89 7361 8183 10597 321 656 176 N
ATOM 722 CA GLY A 89 22.223 378.098 37.701 1.00 69.05 C
ANISOU 722 CA GLY A 89 7488 8200 10549 385 666 127 C
ATOM 723 C GLY A 89 23.525 377.953 38.451 1.00 80.13 C
ANISOU 723 C GLY A 89 8895 9598 11951 399 771 194 C
ATOM 724 O GLY A 89 24.345 377.108 38.087 1.00 87.66 O
ANISOU 724 O GLY A 89 9899 10510 12897 443 789 157 O
ATOM 725 N GLY A 90 23.710 378.717 39.519 1.00 81.57 N
ANISOU 725 N GLY A 90 9027 9815 12151 371 826 284 N
ATOM 726 CA GLY A 90 24.992 378.792 40.183 1.00 77.42 C
ANISOU 726 CA GLY A 90 8500 9291 11625 394 891 341 C
ATOM 727 C GLY A 90 24.955 378.332 41.622 1.00 74.51 C
ANISOU 727 C GLY A 90 8109 8874 11327 355 902 399 C
ATOM 728 O GLY A 90 25.570 377.318 41.963 1.00 83.25 O
ANISOU 728 O GLY A 90 9236 9918 12479 370 907 402 O
ATOM 729 N PHE A 91 24.198 379.033 42.469 1.00 65.59 N
ANISOU 729 N PHE A 91 6955 7767 10199 317 912 449 N
ATOM 730 CA PHE A 91 24.258 378.736 43.896 1.00 72.85 C
ANISOU 730 CA PHE A 91 7890 8645 11143 304 939 517 C
ATOM 731 C PHE A 91 23.619 377.384 44.197 1.00 74.46 C
ANISOU 731 C PHE A 91 8101 8757 11432 269 951 522 C
ATOM 732 O PHE A 91 24.050 376.689 45.124 1.00 78.63 O
ANISOU 732 O PHE A 91 8674 9225 11975 281 972 575 O
ATOM 733 CB PHE A 91 23.598 379.860 44.716 1.00 76.01 C
ANISOU 733 CB PHE A 91 8285 9090 11505 292 966 563 C
ATOM 734 CG PHE A 91 24.038 381.260 44.339 1.00 77.42 C
ANISOU 734 CG PHE A 91 8453 9339 11624 316 950 555 C
ATOM 735 CD1 PHE A 91 25.298 381.499 43.790 1.00 83.92 C
ANISOU 735 CD1 PHE A 91 9273 10177 12434 346 933 541 C
ATOM 736 CD2 PHE A 91 23.220 382.350 44.601 1.00 83.56 C
ANISOU 736 CD2 PHE A 91 9219 10154 12375 310 965 569 C
ATOM 737 CE1 PHE A 91 25.710 382.789 43.468 1.00 78.37 C
ANISOU 737 CE1 PHE A 91 8556 9519 11704 358 933 548 C
ATOM 738 CE2 PHE A 91 23.630 383.652 44.281 1.00 81.06 C
ANISOU 738 CE2 PHE A 91 8901 9881 12015 330 950 567 C
ATOM 739 CZ PHE A 91 24.869 383.868 43.714 1.00 75.74 C
ANISOU 739 CZ PHE A 91 8225 9214 11339 347 935 560 C
ATOM 740 N THR A 92 22.569 377.018 43.464 1.00 72.30 N
ANISOU 740 N THR A 92 7785 8459 11226 225 928 471 N
ATOM 741 CA THR A 92 21.873 375.765 43.728 1.00 71.55 C
ANISOU 741 CA THR A 92 7677 8254 11255 173 938 476 C
ATOM 742 C THR A 92 22.735 374.589 43.304 1.00 75.05 C
ANISOU 742 C THR A 92 8174 8619 11724 201 904 433 C
ATOM 743 O THR A 92 22.925 373.638 44.074 1.00 74.32 O
ANISOU 743 O THR A 92 8116 8432 11689 194 939 487 O
ATOM 744 CB THR A 92 20.513 375.738 43.035 1.00 65.47 C
ANISOU 744 CB THR A 92 6821 7467 10586 114 894 420 C
ATOM 745 OG1 THR A 92 19.654 376.680 43.677 1.00 75.77 O
ANISOU 745 OG1 THR A 92 8066 8825 11899 94 951 479 O
ATOM 746 CG2 THR A 92 19.900 374.377 43.096 1.00 77.99 C
ANISOU 746 CG2 THR A 92 8379 8916 12338 50 886 408 C
ATOM 747 N THR A 93 23.254 374.633 42.071 1.00 75.99 N
ANISOU 747 N THR A 93 8313 8770 11791 246 847 340 N
ATOM 748 CA THR A 93 24.188 373.607 41.627 1.00 76.46 C
ANISOU 748 CA THR A 93 8428 8761 11860 297 831 292 C
ATOM 749 C THR A 93 25.392 373.485 42.552 1.00 73.48 C
ANISOU 749 C THR A 93 8078 8379 11464 348 876 369 C
ATOM 750 O THR A 93 25.809 372.370 42.892 1.00 79.02 O
ANISOU 750 O THR A 93 8817 8978 12227 367 876 380 O
ATOM 751 CB THR A 93 24.704 373.964 40.234 1.00 76.39 C
ANISOU 751 CB THR A 93 8455 8814 11757 365 802 199 C
ATOM 752 OG1 THR A 93 23.614 374.166 39.333 1.00 72.62 O
ANISOU 752 OG1 THR A 93 7971 8347 11273 338 727 120 O
ATOM 753 CG2 THR A 93 25.620 372.877 39.708 1.00 90.44 C
ANISOU 753 CG2 THR A 93 10297 10520 13548 435 802 138 C
ATOM 754 N THR A 94 25.887 374.606 43.066 1.00 58.22 N
ANISOU 754 N THR A 94 6125 6538 9458 368 900 426 N
ATOM 755 CA THR A 94 27.072 374.546 43.909 1.00 63.35 C
ANISOU 755 CA THR A 94 6790 7180 10100 423 904 484 C
ATOM 756 C THR A 94 26.756 374.039 45.305 1.00 69.22 C
ANISOU 756 C THR A 94 7582 7855 10864 406 914 573 C
ATOM 757 O THR A 94 27.597 373.380 45.928 1.00 72.88 O
ANISOU 757 O THR A 94 8086 8259 11344 460 894 612 O
ATOM 758 CB THR A 94 27.737 375.914 43.943 1.00 59.75 C
ANISOU 758 CB THR A 94 6294 6827 9583 446 904 501 C
ATOM 759 OG1 THR A 94 28.244 376.176 42.630 1.00 71.28 O
ANISOU 759 OG1 THR A 94 7726 8329 11027 480 924 438 O
ATOM 760 CG2 THR A 94 28.914 375.935 44.926 1.00 50.69 C
ANISOU 760 CG2 THR A 94 5146 5664 8449 498 870 553 C
ATOM 761 N LEU A 95 25.567 374.346 45.820 1.00 70.58 N
ANISOU 761 N LEU A 95 7755 8031 11032 345 953 614 N
ATOM 762 CA LEU A 95 25.129 373.721 47.059 1.00 72.62 C
ANISOU 762 CA LEU A 95 8077 8207 11306 334 1001 711 C
ATOM 763 C LEU A 95 25.099 372.209 46.906 1.00 79.92 C
ANISOU 763 C LEU A 95 9031 8995 12339 324 1005 711 C
ATOM 764 O LEU A 95 25.463 371.465 47.828 1.00 81.15 O
ANISOU 764 O LEU A 95 9268 9066 12497 360 1021 793 O
ATOM 765 CB LEU A 95 23.753 374.256 47.447 1.00 62.70 C
ANISOU 765 CB LEU A 95 6792 6972 10057 271 1076 751 C
ATOM 766 CG LEU A 95 23.009 373.575 48.598 1.00 62.05 C
ANISOU 766 CG LEU A 95 6768 6796 10011 249 1178 864 C
ATOM 767 CD1 LEU A 95 23.861 373.581 49.851 1.00 63.97 C
ANISOU 767 CD1 LEU A 95 7145 7029 10130 336 1178 951 C
ATOM 768 CD2 LEU A 95 21.636 374.211 48.852 1.00 56.68 C
ANISOU 768 CD2 LEU A 95 6027 6147 9363 193 1274 898 C
ATOM 769 N TYR A 96 24.715 371.735 45.721 1.00 71.53 N
ANISOU 769 N TYR A 96 7919 7901 11360 285 976 615 N
ATOM 770 CA TYR A 96 24.518 370.304 45.568 1.00 73.44 C
ANISOU 770 CA TYR A 96 8188 7989 11726 263 973 603 C
ATOM 771 C TYR A 96 25.849 369.587 45.378 1.00 72.81 C
ANISOU 771 C TYR A 96 8165 7863 11639 356 930 577 C
ATOM 772 O TYR A 96 26.082 368.539 45.991 1.00 71.00 O
ANISOU 772 O TYR A 96 8000 7507 11471 376 942 635 O
ATOM 773 CB TYR A 96 23.553 370.041 44.415 1.00 57.37 C
ANISOU 773 CB TYR A 96 6090 5920 9789 192 929 494 C
ATOM 774 CG TYR A 96 23.312 368.588 44.180 1.00 62.78 C
ANISOU 774 CG TYR A 96 6802 6428 10625 159 906 461 C
ATOM 775 CD1 TYR A 96 22.378 367.894 44.939 1.00 62.37 C
ANISOU 775 CD1 TYR A 96 6734 6245 10721 74 969 548 C
ATOM 776 CD2 TYR A 96 24.010 367.899 43.202 1.00 74.24 C
ANISOU 776 CD2 TYR A 96 8299 7827 12082 218 833 345 C
ATOM 777 CE1 TYR A 96 22.158 366.550 44.740 1.00 64.21 C
ANISOU 777 CE1 TYR A 96 6988 6289 11119 34 946 521 C
ATOM 778 CE2 TYR A 96 23.785 366.560 42.981 1.00 74.61 C
ANISOU 778 CE2 TYR A 96 8381 7692 12275 191 800 302 C
ATOM 779 CZ TYR A 96 22.862 365.888 43.755 1.00 71.00 C
ANISOU 779 CZ TYR A 96 7901 7096 11981 93 849 390 C
ATOM 780 OH TYR A 96 22.638 364.556 43.530 1.00 82.59 O
ANISOU 780 OH TYR A 96 9401 8359 13619 56 813 349 O
ATOM 781 N THR A 97 26.738 370.154 44.560 1.00 61.91 N
ANISOU 781 N THR A 97 6756 6577 10190 419 893 499 N
ATOM 782 CA THR A 97 28.058 369.565 44.341 1.00 57.94 C
ANISOU 782 CA THR A 97 6277 6038 9698 520 869 474 C
ATOM 783 C THR A 97 28.933 369.711 45.572 1.00 50.40 C
ANISOU 783 C THR A 97 5347 5091 8713 581 856 577 C
ATOM 784 O THR A 97 29.695 368.801 45.910 1.00 62.92 O
ANISOU 784 O THR A 97 6973 6584 10349 653 831 601 O
ATOM 785 CB THR A 97 28.744 370.207 43.153 1.00 57.38 C
ANISOU 785 CB THR A 97 6161 6068 9574 573 868 381 C
ATOM 786 OG1 THR A 97 28.813 371.631 43.368 1.00 60.33 O
ANISOU 786 OG1 THR A 97 6480 6577 9866 557 880 417 O
ATOM 787 CG2 THR A 97 27.963 369.894 41.902 1.00 50.33 C
ANISOU 787 CG2 THR A 97 5287 5151 8686 543 854 266 C
ATOM 788 N SER A 98 28.896 370.878 46.209 1.00 59.01 N
ANISOU 788 N SER A 98 6415 6285 9719 567 854 628 N
ATOM 789 CA SER A 98 29.667 371.065 47.431 1.00 76.61 C
ANISOU 789 CA SER A 98 8686 8516 11904 632 807 713 C
ATOM 790 C SER A 98 29.416 369.957 48.465 1.00 65.66 C
ANISOU 790 C SER A 98 7417 6998 10534 652 815 809 C
ATOM 791 O SER A 98 30.356 369.502 49.130 1.00 61.58 O
ANISOU 791 O SER A 98 6950 6430 10017 744 749 855 O
ATOM 792 CB SER A 98 29.324 372.443 48.016 1.00 84.27 C
ANISOU 792 CB SER A 98 9648 9594 12774 601 805 744 C
ATOM 793 OG SER A 98 29.709 372.574 49.367 1.00 96.87 O
ANISOU 793 OG SER A 98 11331 11175 14299 658 752 826 O
ATOM 794 N LEU A 99 28.187 369.441 48.550 1.00 62.98 N
ANISOU 794 N LEU A 99 7115 6585 10230 571 894 843 N
ATOM 795 CA LEU A 99 27.883 368.374 49.504 1.00 63.66 C
ANISOU 795 CA LEU A 99 7316 6527 10344 582 934 955 C
ATOM 796 C LEU A 99 28.321 366.990 49.053 1.00 65.91 C
ANISOU 796 C LEU A 99 7626 6665 10751 616 911 929 C
ATOM 797 O LEU A 99 28.369 366.071 49.878 1.00 55.15 O
ANISOU 797 O LEU A 99 6373 5170 9411 652 928 1032 O
ATOM 798 CB LEU A 99 26.393 368.340 49.805 1.00 73.49 C
ANISOU 798 CB LEU A 99 8569 7732 11621 476 1052 1016 C
ATOM 799 CG LEU A 99 25.952 369.547 50.602 1.00 72.50 C
ANISOU 799 CG LEU A 99 8464 7721 11361 472 1097 1074 C
ATOM 800 CD1 LEU A 99 24.452 369.557 50.694 1.00 52.92 C
ANISOU 800 CD1 LEU A 99 5947 5210 8952 367 1230 1119 C
ATOM 801 CD2 LEU A 99 26.619 369.475 51.964 1.00 67.20 C
ANISOU 801 CD2 LEU A 99 7950 7025 10557 580 1075 1187 C
ATOM 802 N HIS A 100 28.695 366.843 47.798 1.00 67.07 N
ANISOU 802 N HIS A 100 7693 6827 10963 620 875 799 N
ATOM 803 CA HIS A 100 29.406 365.674 47.323 1.00 66.67 C
ANISOU 803 CA HIS A 100 7668 6653 11010 690 840 752 C
ATOM 804 C HIS A 100 30.917 365.847 47.430 1.00 75.55 C
ANISOU 804 C HIS A 100 8768 7829 12107 824 768 742 C
ATOM 805 O HIS A 100 31.648 364.850 47.484 1.00 82.66 O
ANISOU 805 O HIS A 100 9709 8615 13082 914 735 747 O
ATOM 806 CB HIS A 100 29.024 365.441 45.868 1.00 69.23 C
ANISOU 806 CB HIS A 100 7938 6966 11401 645 842 603 C
ATOM 807 CG HIS A 100 27.611 364.987 45.680 1.00 72.49 C
ANISOU 807 CG HIS A 100 8357 7283 11903 519 875 593 C
ATOM 808 ND1 HIS A 100 27.154 363.757 46.101 1.00 90.03 N
ANISOU 808 ND1 HIS A 100 10646 9306 14254 484 897 648 N
ATOM 809 CD2 HIS A 100 26.553 365.603 45.106 1.00 72.97 C
ANISOU 809 CD2 HIS A 100 8350 7408 11967 418 884 535 C
ATOM 810 CE1 HIS A 100 25.877 363.632 45.794 1.00 88.09 C
ANISOU 810 CE1 HIS A 100 10357 9004 14109 356 919 622 C
ATOM 811 NE2 HIS A 100 25.490 364.738 45.186 1.00 90.57 N
ANISOU 811 NE2 HIS A 100 10587 9480 14347 319 903 550 N
ATOM 812 N GLY A 101 31.392 367.091 47.448 1.00 79.20 N
ANISOU 812 N GLY A 101 9154 8450 12490 838 742 728 N
ATOM 813 CA GLY A 101 32.797 367.404 47.509 1.00 72.25 C
ANISOU 813 CA GLY A 101 8205 7621 11624 948 671 715 C
ATOM 814 C GLY A 101 33.468 367.440 46.166 1.00 71.18 C
ANISOU 814 C GLY A 101 7966 7527 11554 988 704 599 C
ATOM 815 O GLY A 101 34.702 367.502 46.110 1.00 70.66 O
ANISOU 815 O GLY A 101 7818 7479 11549 1088 667 587 O
ATOM 816 N TYR A 102 32.696 367.474 45.084 1.00 69.33 N
ANISOU 816 N TYR A 102 7728 7309 11304 921 773 514 N
ATOM 817 CA TYR A 102 33.253 367.577 43.742 1.00 68.03 C
ANISOU 817 CA TYR A 102 7501 7191 11158 973 825 405 C
ATOM 818 C TYR A 102 32.113 367.799 42.766 1.00 73.90 C
ANISOU 818 C TYR A 102 8277 7961 11839 886 865 324 C
ATOM 819 O TYR A 102 30.934 367.720 43.123 1.00 84.04 O
ANISOU 819 O TYR A 102 9608 9212 13111 786 848 348 O
ATOM 820 CB TYR A 102 34.041 366.329 43.338 1.00 61.88 C
ANISOU 820 CB TYR A 102 6746 6289 10475 1088 831 356 C
ATOM 821 CG TYR A 102 33.220 365.049 43.131 1.00 67.75 C
ANISOU 821 CG TYR A 102 7610 6870 11261 1060 823 315 C
ATOM 822 CD1 TYR A 102 32.826 364.257 44.207 1.00 57.95 C
ANISOU 822 CD1 TYR A 102 6449 5499 10071 1034 778 408 C
ATOM 823 CD2 TYR A 102 32.852 364.635 41.846 1.00 64.27 C
ANISOU 823 CD2 TYR A 102 7214 6394 10812 1065 857 181 C
ATOM 824 CE1 TYR A 102 32.099 363.088 44.000 1.00 72.39 C
ANISOU 824 CE1 TYR A 102 8373 7156 11976 997 776 375 C
ATOM 825 CE2 TYR A 102 32.132 363.488 41.634 1.00 61.51 C
ANISOU 825 CE2 TYR A 102 6965 5878 10528 1034 826 127 C
ATOM 826 CZ TYR A 102 31.754 362.707 42.707 1.00 74.57 C
ANISOU 826 CZ TYR A 102 8673 7393 12268 992 789 226 C
ATOM 827 OH TYR A 102 31.031 361.541 42.476 1.00 79.10 O
ANISOU 827 OH TYR A 102 9336 7776 12943 948 763 175 O
ATOM 828 N PHE A 103 32.484 368.058 41.517 1.00 66.24 N
ANISOU 828 N PHE A 103 7284 7049 10836 936 920 230 N
ATOM 829 CA PHE A 103 31.498 368.472 40.528 1.00 65.44 C
ANISOU 829 CA PHE A 103 7220 6995 10649 875 934 150 C
ATOM 830 C PHE A 103 30.876 367.238 39.901 1.00 71.69 C
ANISOU 830 C PHE A 103 8114 7648 11477 877 899 49 C
ATOM 831 O PHE A 103 31.320 366.750 38.857 1.00 73.30 O
ANISOU 831 O PHE A 103 8372 7820 11658 971 928 -57 O
ATOM 832 CB PHE A 103 32.121 369.382 39.481 1.00 59.09 C
ANISOU 832 CB PHE A 103 6376 6312 9763 937 1014 108 C
ATOM 833 CG PHE A 103 31.111 370.098 38.670 1.00 68.34 C
ANISOU 833 CG PHE A 103 7589 7555 10823 878 1009 56 C
ATOM 834 CD1 PHE A 103 30.463 371.210 39.191 1.00 64.96 C
ANISOU 834 CD1 PHE A 103 7109 7216 10356 783 987 124 C
ATOM 835 CD2 PHE A 103 30.759 369.638 37.416 1.00 76.76 C
ANISOU 835 CD2 PHE A 103 8757 8590 11817 925 1009 -67 C
ATOM 836 CE1 PHE A 103 29.503 371.866 38.457 1.00 75.38 C
ANISOU 836 CE1 PHE A 103 8462 8596 11583 739 968 79 C
ATOM 837 CE2 PHE A 103 29.792 370.290 36.677 1.00 81.89 C
ANISOU 837 CE2 PHE A 103 9454 9302 12358 882 972 -118 C
ATOM 838 CZ PHE A 103 29.166 371.408 37.193 1.00 74.80 C
ANISOU 838 CZ PHE A 103 8487 8495 11439 788 952 -40 C
ATOM 839 N VAL A 104 29.767 366.786 40.498 1.00 68.05 N
ANISOU 839 N VAL A 104 7682 7100 11075 770 840 76 N
ATOM 840 CA VAL A 104 29.228 365.461 40.200 1.00 73.40 C
ANISOU 840 CA VAL A 104 8441 7599 11847 755 790 -1 C
ATOM 841 C VAL A 104 28.524 365.392 38.859 1.00 74.72 C
ANISOU 841 C VAL A 104 8665 7758 11967 745 739 -158 C
ATOM 842 O VAL A 104 28.087 364.306 38.462 1.00 88.04 O
ANISOU 842 O VAL A 104 10426 9287 13739 736 674 -252 O
ATOM 843 CB VAL A 104 28.229 365.015 41.280 1.00 64.50 C
ANISOU 843 CB VAL A 104 7311 6367 10829 633 764 95 C
ATOM 844 CG1 VAL A 104 28.943 364.668 42.543 1.00 59.74 C
ANISOU 844 CG1 VAL A 104 6716 5717 10267 675 794 233 C
ATOM 845 CG2 VAL A 104 27.258 366.141 41.527 1.00 59.79 C
ANISOU 845 CG2 VAL A 104 6646 5891 10182 527 770 141 C
ATOM 846 N PHE A 105 28.430 366.500 38.133 1.00 70.03 N
ANISOU 846 N PHE A 105 8052 7317 11238 756 755 -192 N
ATOM 847 CA PHE A 105 27.656 366.545 36.906 1.00 65.81 C
ANISOU 847 CA PHE A 105 7589 6783 10631 754 680 -335 C
ATOM 848 C PHE A 105 28.520 366.368 35.667 1.00 74.24 C
ANISOU 848 C PHE A 105 8765 7870 11573 911 724 -452 C
ATOM 849 O PHE A 105 27.988 366.411 34.551 1.00 79.34 O
ANISOU 849 O PHE A 105 9511 8520 12115 942 655 -582 O
ATOM 850 CB PHE A 105 26.920 367.891 36.805 1.00 60.77 C
ANISOU 850 CB PHE A 105 6889 6295 9904 685 667 -298 C
ATOM 851 CG PHE A 105 25.913 368.122 37.903 1.00 76.64 C
ANISOU 851 CG PHE A 105 8800 8290 12028 541 639 -198 C
ATOM 852 CD1 PHE A 105 24.849 367.249 38.102 1.00 78.37 C
ANISOU 852 CD1 PHE A 105 9010 8363 12403 443 553 -233 C
ATOM 853 CD2 PHE A 105 26.018 369.236 38.725 1.00 76.14 C
ANISOU 853 CD2 PHE A 105 8653 8352 11925 508 706 -69 C
ATOM 854 CE1 PHE A 105 23.927 367.468 39.119 1.00 66.62 C
ANISOU 854 CE1 PHE A 105 7425 6861 11028 320 567 -125 C
ATOM 855 CE2 PHE A 105 25.082 369.470 39.737 1.00 74.33 C
ANISOU 855 CE2 PHE A 105 8350 8111 11781 395 705 24 C
ATOM 856 CZ PHE A 105 24.044 368.584 39.932 1.00 70.44 C
ANISOU 856 CZ PHE A 105 7843 7480 11441 305 650 3 C
ATOM 857 N GLY A 106 29.839 366.193 35.823 1.00 73.02 N
ANISOU 857 N GLY A 106 8596 7727 11421 1022 838 -408 N
ATOM 858 CA GLY A 106 30.675 365.898 34.682 1.00 73.69 C
ANISOU 858 CA GLY A 106 8784 7812 11404 1185 913 -514 C
ATOM 859 C GLY A 106 30.963 367.103 33.807 1.00 80.39 C
ANISOU 859 C GLY A 106 9647 8826 12071 1249 1009 -510 C
ATOM 860 O GLY A 106 30.482 368.215 34.054 1.00 75.57 O
ANISOU 860 O GLY A 106 8965 8330 11417 1161 1000 -432 O
ATOM 861 N PRO A 107 31.817 366.913 32.798 1.00 83.63 N
ANISOU 861 N PRO A 107 10153 9247 12377 1414 1126 -582 N
ATOM 862 CA PRO A 107 32.204 368.057 31.951 1.00 81.09 C
ANISOU 862 CA PRO A 107 9854 9073 11881 1488 1259 -552 C
ATOM 863 C PRO A 107 31.026 368.727 31.256 1.00 81.37 C
ANISOU 863 C PRO A 107 9994 9169 11756 1439 1151 -609 C
ATOM 864 O PRO A 107 31.039 369.952 31.090 1.00 92.16 O
ANISOU 864 O PRO A 107 11320 10664 13032 1422 1221 -522 O
ATOM 865 CB PRO A 107 33.192 367.437 30.947 1.00 87.40 C
ANISOU 865 CB PRO A 107 10775 9835 12596 1690 1408 -639 C
ATOM 866 CG PRO A 107 33.051 365.942 31.090 1.00 82.75 C
ANISOU 866 CG PRO A 107 10266 9068 12107 1718 1300 -757 C
ATOM 867 CD PRO A 107 32.585 365.696 32.489 1.00 76.50 C
ANISOU 867 CD PRO A 107 9328 8218 11520 1549 1173 -668 C
ATOM 868 N THR A 108 30.016 367.965 30.823 1.00 98.14 N
ANISOU 868 N THR A 108 12246 11189 13853 1418 970 -754 N
ATOM 869 CA THR A 108 28.821 368.567 30.227 1.00 96.41 C
ANISOU 869 CA THR A 108 12105 11017 13511 1369 824 -814 C
ATOM 870 C THR A 108 28.072 369.441 31.230 1.00 92.01 C
ANISOU 870 C THR A 108 11368 10528 13063 1194 765 -687 C
ATOM 871 O THR A 108 27.709 370.586 30.929 1.00 86.10 O
ANISOU 871 O THR A 108 10615 9897 12203 1181 771 -637 O
ATOM 872 CB THR A 108 27.898 367.481 29.677 1.00 96.63 C
ANISOU 872 CB THR A 108 12272 10895 13548 1369 610 -1006 C
ATOM 873 OG1 THR A 108 28.535 366.823 28.573 1.00107.22 O
ANISOU 873 OG1 THR A 108 13827 12184 14729 1559 661 -1144 O
ATOM 874 CG2 THR A 108 26.578 368.076 29.229 1.00 91.47 C
ANISOU 874 CG2 THR A 108 11653 10277 12823 1300 418 -1064 C
ATOM 875 N GLY A 109 27.829 368.921 32.434 1.00 90.80 N
ANISOU 875 N GLY A 109 11081 10298 13123 1070 718 -628 N
ATOM 876 CA GLY A 109 27.258 369.763 33.470 1.00 85.10 C
ANISOU 876 CA GLY A 109 10201 9644 12491 928 702 -497 C
ATOM 877 C GLY A 109 28.115 370.975 33.764 1.00 84.69 C
ANISOU 877 C GLY A 109 10066 9734 12378 953 856 -360 C
ATOM 878 O GLY A 109 27.601 372.029 34.144 1.00 86.61 O
ANISOU 878 O GLY A 109 10232 10065 12610 875 844 -281 O
ATOM 879 N CYS A 110 29.428 370.851 33.560 1.00 91.06 N
ANISOU 879 N CYS A 110 10881 10556 13163 1063 1002 -336 N
ATOM 880 CA CYS A 110 30.338 371.953 33.837 1.00 86.69 C
ANISOU 880 CA CYS A 110 10225 10114 12600 1079 1147 -208 C
ATOM 881 C CYS A 110 30.097 373.105 32.872 1.00 84.92 C
ANISOU 881 C CYS A 110 10068 9998 12200 1116 1195 -200 C
ATOM 882 O CYS A 110 30.104 374.273 33.279 1.00 83.36 O
ANISOU 882 O CYS A 110 9778 9885 12009 1056 1232 -94 O
ATOM 883 CB CYS A 110 31.783 371.469 33.757 1.00 86.30 C
ANISOU 883 CB CYS A 110 10146 10040 12604 1194 1292 -191 C
ATOM 884 SG CYS A 110 32.964 372.693 34.275 1.00 85.49 S
ANISOU 884 SG CYS A 110 9866 10040 12576 1191 1444 -36 S
ATOM 885 N ASN A 111 29.847 372.791 31.594 1.00 76.96 N
ANISOU 885 N ASN A 111 9240 8976 11025 1222 1182 -315 N
ATOM 886 CA ASN A 111 29.560 373.833 30.614 1.00 79.72 C
ANISOU 886 CA ASN A 111 9694 9419 11179 1278 1217 -304 C
ATOM 887 C ASN A 111 28.216 374.491 30.885 1.00 87.10 C
ANISOU 887 C ASN A 111 10598 10385 12110 1163 1046 -299 C
ATOM 888 O ASN A 111 28.077 375.707 30.726 1.00 93.74 O
ANISOU 888 O ASN A 111 11426 11316 12876 1153 1088 -215 O
ATOM 889 CB ASN A 111 29.584 373.262 29.195 1.00 76.70 C
ANISOU 889 CB ASN A 111 9549 9007 10588 1441 1224 -439 C
ATOM 890 CG ASN A 111 30.977 373.077 28.675 1.00 83.20 C
ANISOU 890 CG ASN A 111 10412 9837 11362 1589 1467 -411 C
ATOM 891 OD1 ASN A 111 31.947 373.334 29.386 1.00 94.38 O
ANISOU 891 OD1 ASN A 111 11653 11275 12933 1561 1612 -293 O
ATOM 892 ND2 ASN A 111 31.095 372.666 27.423 1.00 83.68 N
ANISOU 892 ND2 ASN A 111 10705 9880 11209 1757 1512 -518 N
ATOM 893 N LEU A 112 27.214 373.695 31.251 1.00 85.10 N
ANISOU 893 N LEU A 112 10332 10049 11953 1081 860 -386 N
ATOM 894 CA LEU A 112 25.898 374.226 31.537 1.00 77.19 C
ANISOU 894 CA LEU A 112 9274 9067 10988 974 704 -384 C
ATOM 895 C LEU A 112 25.917 375.170 32.730 1.00 73.27 C
ANISOU 895 C LEU A 112 8601 8634 10604 865 768 -234 C
ATOM 896 O LEU A 112 25.534 376.346 32.611 1.00 68.31 O
ANISOU 896 O LEU A 112 7957 8089 9910 852 769 -173 O
ATOM 897 CB LEU A 112 24.935 373.063 31.797 1.00 81.45 C
ANISOU 897 CB LEU A 112 9797 9481 11668 897 522 -496 C
ATOM 898 CG LEU A 112 24.214 372.539 30.571 1.00 81.59 C
ANISOU 898 CG LEU A 112 9982 9442 11576 969 346 -670 C
ATOM 899 CD1 LEU A 112 23.943 371.085 30.774 1.00 83.39 C
ANISOU 899 CD1 LEU A 112 10215 9511 11961 927 237 -783 C
ATOM 900 CD2 LEU A 112 22.930 373.336 30.380 1.00 74.96 C
ANISOU 900 CD2 LEU A 112 9104 8650 10729 913 185 -681 C
ATOM 901 N GLU A 113 26.430 374.694 33.869 1.00 64.15 N
ANISOU 901 N GLU A 113 7333 7436 9605 803 821 -172 N
ATOM 902 CA GLU A 113 26.467 375.522 35.064 1.00 67.57 C
ANISOU 902 CA GLU A 113 7627 7918 10128 714 864 -45 C
ATOM 903 C GLU A 113 27.409 376.698 34.884 1.00 75.93 C
ANISOU 903 C GLU A 113 8666 9069 11116 761 998 46 C
ATOM 904 O GLU A 113 27.132 377.802 35.363 1.00 83.51 O
ANISOU 904 O GLU A 113 9560 10087 12082 707 1003 124 O
ATOM 905 CB GLU A 113 26.889 374.671 36.264 1.00 72.83 C
ANISOU 905 CB GLU A 113 8216 8508 10947 665 879 -3 C
ATOM 906 CG GLU A 113 26.799 375.374 37.607 1.00 85.95 C
ANISOU 906 CG GLU A 113 9768 10204 12686 581 896 111 C
ATOM 907 CD GLU A 113 28.067 376.085 38.010 1.00 99.64 C
ANISOU 907 CD GLU A 113 11446 11992 14422 616 993 195 C
ATOM 908 OE1 GLU A 113 29.104 375.824 37.382 1.00103.80 O
ANISOU 908 OE1 GLU A 113 11992 12516 14931 700 1068 177 O
ATOM 909 OE2 GLU A 113 28.029 376.917 38.946 1.00117.55 O
ANISOU 909 OE2 GLU A 113 13648 14298 16720 564 994 274 O
ATOM 910 N GLY A 114 28.519 376.490 34.183 1.00 78.31 N
ANISOU 910 N GLY A 114 9019 9373 11361 864 1116 38 N
ATOM 911 CA GLY A 114 29.395 377.604 33.874 1.00 71.64 C
ANISOU 911 CA GLY A 114 8147 8600 10473 906 1261 130 C
ATOM 912 C GLY A 114 28.720 378.640 33.004 1.00 66.91 C
ANISOU 912 C GLY A 114 7638 8065 9720 930 1253 141 C
ATOM 913 O GLY A 114 28.757 379.836 33.300 1.00 81.11 O
ANISOU 913 O GLY A 114 9373 9912 11532 887 1293 235 O
ATOM 914 N PHE A 115 28.059 378.188 31.935 1.00 65.10 N
ANISOU 914 N PHE A 115 7567 7825 9342 1003 1180 38 N
ATOM 915 CA PHE A 115 27.415 379.130 31.025 1.00 80.95 C
ANISOU 915 CA PHE A 115 9688 9888 11180 1051 1151 46 C
ATOM 916 C PHE A 115 26.350 379.938 31.758 1.00 86.74 C
ANISOU 916 C PHE A 115 10325 10648 11985 941 1029 86 C
ATOM 917 O PHE A 115 26.349 381.174 31.700 1.00 95.84 O
ANISOU 917 O PHE A 115 11465 11852 13097 938 1083 178 O
ATOM 918 CB PHE A 115 26.820 378.401 29.818 1.00 74.36 C
ANISOU 918 CB PHE A 115 9055 9026 10172 1157 1042 -95 C
ATOM 919 CG PHE A 115 26.005 379.281 28.919 1.00 71.42 C
ANISOU 919 CG PHE A 115 8815 8704 9617 1216 960 -98 C
ATOM 920 CD1 PHE A 115 26.622 380.019 27.913 1.00 84.37 C
ANISOU 920 CD1 PHE A 115 10606 10393 11058 1345 1116 -32 C
ATOM 921 CD2 PHE A 115 24.633 379.392 29.078 1.00 73.16 C
ANISOU 921 CD2 PHE A 115 9005 8918 9875 1151 737 -157 C
ATOM 922 CE1 PHE A 115 25.881 380.851 27.075 1.00 89.49 C
ANISOU 922 CE1 PHE A 115 11400 11080 11520 1416 1035 -23 C
ATOM 923 CE2 PHE A 115 23.883 380.224 28.249 1.00 78.19 C
ANISOU 923 CE2 PHE A 115 9761 9597 10349 1220 640 -159 C
ATOM 924 CZ PHE A 115 24.508 380.953 27.245 1.00 82.14 C
ANISOU 924 CZ PHE A 115 10439 10146 10626 1357 781 -92 C
ATOM 925 N PHE A 116 25.431 379.261 32.453 1.00 75.16 N
ANISOU 925 N PHE A 116 8786 9136 10635 854 878 23 N
ATOM 926 CA PHE A 116 24.299 379.977 33.033 1.00 75.98 C
ANISOU 926 CA PHE A 116 8804 9262 10802 769 773 51 C
ATOM 927 C PHE A 116 24.741 380.864 34.188 1.00 75.64 C
ANISOU 927 C PHE A 116 8632 9249 10860 696 869 173 C
ATOM 928 O PHE A 116 24.229 381.978 34.347 1.00 77.32 O
ANISOU 928 O PHE A 116 8815 9503 11061 675 854 229 O
ATOM 929 CB PHE A 116 23.215 378.992 33.461 1.00 75.69 C
ANISOU 929 CB PHE A 116 8710 9158 10891 695 618 -37 C
ATOM 930 CG PHE A 116 22.368 378.547 32.322 1.00 79.53 C
ANISOU 930 CG PHE A 116 9308 9618 11293 753 453 -165 C
ATOM 931 CD1 PHE A 116 21.511 379.443 31.697 1.00 81.75 C
ANISOU 931 CD1 PHE A 116 9627 9947 11486 788 350 -173 C
ATOM 932 CD2 PHE A 116 22.482 377.261 31.813 1.00 77.54 C
ANISOU 932 CD2 PHE A 116 9140 9285 11037 788 388 -286 C
ATOM 933 CE1 PHE A 116 20.752 379.052 30.608 1.00 79.89 C
ANISOU 933 CE1 PHE A 116 9508 9685 11161 857 164 -302 C
ATOM 934 CE2 PHE A 116 21.725 376.861 30.722 1.00 72.18 C
ANISOU 934 CE2 PHE A 116 8585 8572 10270 852 206 -425 C
ATOM 935 CZ PHE A 116 20.860 377.759 30.117 1.00 71.72 C
ANISOU 935 CZ PHE A 116 8561 8567 10120 888 84 -434 C
ATOM 936 N ALA A 117 25.697 380.402 35.001 1.00 78.72 N
ANISOU 936 N ALA A 117 8951 9611 11349 666 953 210 N
ATOM 937 CA ALA A 117 26.184 381.255 36.081 1.00 85.50 C
ANISOU 937 CA ALA A 117 9705 10489 12292 609 1014 309 C
ATOM 938 C ALA A 117 26.989 382.434 35.524 1.00 88.98 C
ANISOU 938 C ALA A 117 10162 10973 12674 653 1127 385 C
ATOM 939 O ALA A 117 26.935 383.544 36.074 1.00 78.25 O
ANISOU 939 O ALA A 117 8748 9631 11350 610 1137 453 O
ATOM 940 CB ALA A 117 27.005 380.436 37.077 1.00 82.24 C
ANISOU 940 CB ALA A 117 9221 10029 11996 580 1042 323 C
ATOM 941 N THR A 118 27.740 382.222 34.436 1.00 81.63 N
ANISOU 941 N THR A 118 9312 10047 11657 742 1225 377 N
ATOM 942 CA THR A 118 28.465 383.339 33.840 1.00 79.90 C
ANISOU 942 CA THR A 118 9110 9855 11393 783 1362 468 C
ATOM 943 C THR A 118 27.502 384.296 33.145 1.00 81.32 C
ANISOU 943 C THR A 118 9388 10069 11440 810 1314 485 C
ATOM 944 O THR A 118 27.670 385.519 33.224 1.00 79.00 O
ANISOU 944 O THR A 118 9069 9784 11163 791 1372 577 O
ATOM 945 CB THR A 118 29.540 382.825 32.868 1.00 77.11 C
ANISOU 945 CB THR A 118 8821 9495 10983 886 1518 469 C
ATOM 946 OG1 THR A 118 30.417 381.919 33.553 1.00 80.08 O
ANISOU 946 OG1 THR A 118 9092 9833 11502 870 1547 451 O
ATOM 947 CG2 THR A 118 30.354 383.973 32.244 1.00 73.24 C
ANISOU 947 CG2 THR A 118 8338 9019 10471 926 1702 587 C
ATOM 948 N LEU A 119 26.489 383.753 32.459 1.00 87.23 N
ANISOU 948 N LEU A 119 10247 10825 12069 857 1191 394 N
ATOM 949 CA LEU A 119 25.462 384.588 31.837 1.00 90.98 C
ANISOU 949 CA LEU A 119 10810 11329 12428 893 1103 399 C
ATOM 950 C LEU A 119 24.713 385.430 32.871 1.00 90.98 C
ANISOU 950 C LEU A 119 10690 11335 12545 799 1027 440 C
ATOM 951 O LEU A 119 24.489 386.628 32.666 1.00 89.28 O
ANISOU 951 O LEU A 119 10500 11136 12289 816 1045 512 O
ATOM 952 CB LEU A 119 24.495 383.706 31.042 1.00 84.59 C
ANISOU 952 CB LEU A 119 10116 10514 11510 953 938 269 C
ATOM 953 CG LEU A 119 23.510 384.363 30.067 1.00 76.10 C
ANISOU 953 CG LEU A 119 9174 9466 10276 1035 817 251 C
ATOM 954 CD1 LEU A 119 24.218 384.841 28.806 1.00 77.06 C
ANISOU 954 CD1 LEU A 119 9496 9609 10176 1175 949 307 C
ATOM 955 CD2 LEU A 119 22.390 383.395 29.698 1.00 66.82 C
ANISOU 955 CD2 LEU A 119 8037 8265 9088 1049 589 99 C
ATOM 956 N GLY A 120 24.296 384.816 33.980 1.00 86.07 N
ANISOU 956 N GLY A 120 9949 10693 12062 711 953 398 N
ATOM 957 CA GLY A 120 23.601 385.575 35.013 1.00 79.37 C
ANISOU 957 CA GLY A 120 8999 9847 11311 639 907 435 C
ATOM 958 C GLY A 120 24.402 386.757 35.527 1.00 78.68 C
ANISOU 958 C GLY A 120 8872 9757 11264 616 1011 535 C
ATOM 959 O GLY A 120 23.922 387.893 35.541 1.00 90.87 O
ANISOU 959 O GLY A 120 10422 11308 12795 620 997 580 O
ATOM 960 N GLY A 121 25.662 386.515 35.890 1.00 79.23 N
ANISOU 960 N GLY A 121 8899 9806 11398 596 1109 567 N
ATOM 961 CA GLY A 121 26.490 387.583 36.429 1.00 72.36 C
ANISOU 961 CA GLY A 121 7970 8914 10609 561 1184 649 C
ATOM 962 C GLY A 121 26.808 388.644 35.395 1.00 70.84 C
ANISOU 962 C GLY A 121 7848 8722 10347 611 1278 726 C
ATOM 963 O GLY A 121 26.985 389.817 35.732 1.00 64.56 O
ANISOU 963 O GLY A 121 7022 7897 9611 581 1304 792 O
ATOM 964 N GLU A 122 26.984 388.228 34.139 1.00 69.25 N
ANISOU 964 N GLU A 122 7753 8539 10017 696 1340 722 N
ATOM 965 CA GLU A 122 27.248 389.182 33.071 1.00 70.30 C
ANISOU 965 CA GLU A 122 7989 8669 10053 763 1450 812 C
ATOM 966 C GLU A 122 26.029 390.070 32.810 1.00 78.64 C
ANISOU 966 C GLU A 122 9121 9737 11022 790 1346 823 C
ATOM 967 O GLU A 122 26.174 391.286 32.631 1.00 77.15 O
ANISOU 967 O GLU A 122 8956 9517 10839 796 1410 919 O
ATOM 968 CB GLU A 122 27.680 388.431 31.821 1.00 74.53 C
ANISOU 968 CB GLU A 122 8655 9225 10440 870 1545 797 C
ATOM 969 CG GLU A 122 29.142 388.070 31.862 1.00 75.53 C
ANISOU 969 CG GLU A 122 8701 9326 10671 865 1723 842 C
ATOM 970 CD GLU A 122 30.054 389.239 31.595 1.00 92.34 C
ANISOU 970 CD GLU A 122 10797 11414 12873 858 1908 984 C
ATOM 971 OE1 GLU A 122 30.049 389.755 30.455 1.00101.22 O
ANISOU 971 OE1 GLU A 122 12072 12541 13844 950 2025 1059 O
ATOM 972 OE2 GLU A 122 30.779 389.640 32.529 1.00 96.38 O
ANISOU 972 OE2 GLU A 122 11137 11881 13602 761 1932 1024 O
ATOM 973 N ILE A 123 24.821 389.481 32.765 1.00 84.01 N
ANISOU 973 N ILE A 123 9830 10450 11639 810 1182 727 N
ATOM 974 CA ILE A 123 23.608 390.274 32.534 1.00 78.84 C
ANISOU 974 CA ILE A 123 9222 9805 10927 845 1064 730 C
ATOM 975 C ILE A 123 23.413 391.274 33.664 1.00 74.19 C
ANISOU 975 C ILE A 123 8523 9188 10480 769 1057 775 C
ATOM 976 O ILE A 123 23.058 392.436 33.430 1.00 77.24 O
ANISOU 976 O ILE A 123 8954 9553 10840 802 1054 839 O
ATOM 977 CB ILE A 123 22.359 389.371 32.381 1.00 66.14 C
ANISOU 977 CB ILE A 123 7617 8227 9287 865 877 609 C
ATOM 978 CG1 ILE A 123 22.425 388.477 31.144 1.00 62.14 C
ANISOU 978 CG1 ILE A 123 7259 7736 8615 961 844 544 C
ATOM 979 CG2 ILE A 123 21.065 390.173 32.390 1.00 54.47 C
ANISOU 979 CG2 ILE A 123 6128 6755 7812 891 743 607 C
ATOM 980 CD1 ILE A 123 21.431 387.352 31.200 1.00 56.57 C
ANISOU 980 CD1 ILE A 123 6516 7032 7945 945 660 408 C
ATOM 981 N ALA A 124 23.674 390.851 34.901 1.00 68.71 N
ANISOU 981 N ALA A 124 7701 8481 9923 679 1055 741 N
ATOM 982 CA ALA A 124 23.608 391.781 36.020 1.00 70.98 C
ANISOU 982 CA ALA A 124 7912 8734 10325 620 1051 772 C
ATOM 983 C ALA A 124 24.585 392.935 35.809 1.00 82.06 C
ANISOU 983 C ALA A 124 9335 10080 11763 614 1161 872 C
ATOM 984 O ALA A 124 24.187 394.107 35.801 1.00 91.45 O
ANISOU 984 O ALA A 124 10555 11234 12959 630 1151 920 O
ATOM 985 CB ALA A 124 23.884 391.041 37.331 1.00 67.41 C
ANISOU 985 CB ALA A 124 7358 8275 9982 544 1034 723 C
ATOM 986 N LEU A 125 25.874 392.611 35.631 1.00 76.29 N
ANISOU 986 N LEU A 125 8578 9330 11078 591 1273 907 N
ATOM 987 CA LEU A 125 26.899 393.610 35.343 1.00 75.28 C
ANISOU 987 CA LEU A 125 8444 9134 11023 575 1400 1011 C
ATOM 988 C LEU A 125 26.446 394.629 34.309 1.00 76.31 C
ANISOU 988 C LEU A 125 8701 9245 11047 647 1443 1097 C
ATOM 989 O LEU A 125 26.515 395.840 34.537 1.00 81.92 O
ANISOU 989 O LEU A 125 9407 9883 11836 622 1463 1164 O
ATOM 990 CB LEU A 125 28.176 392.925 34.856 1.00 79.48 C
ANISOU 990 CB LEU A 125 8943 9664 11591 577 1537 1042 C
ATOM 991 CG LEU A 125 29.265 393.890 34.379 1.00 77.21 C
ANISOU 991 CG LEU A 125 8633 9300 11404 562 1707 1168 C
ATOM 992 CD1 LEU A 125 29.688 394.806 35.515 1.00 74.94 C
ANISOU 992 CD1 LEU A 125 8222 8925 11328 460 1657 1180 C
ATOM 993 CD2 LEU A 125 30.448 393.134 33.805 1.00 72.76 C
ANISOU 993 CD2 LEU A 125 8028 8741 10877 584 1869 1200 C
ATOM 994 N TRP A 126 26.009 394.153 33.147 1.00 71.48 N
ANISOU 994 N TRP A 126 8219 8688 10252 745 1451 1095 N
ATOM 995 CA TRP A 126 25.668 395.078 32.078 1.00 73.13 C
ANISOU 995 CA TRP A 126 8579 8876 10331 836 1494 1189 C
ATOM 996 C TRP A 126 24.338 395.775 32.348 1.00 80.96 C
ANISOU 996 C TRP A 126 9595 9868 11299 862 1335 1163 C
ATOM 997 O TRP A 126 24.103 396.869 31.820 1.00 86.89 O
ANISOU 997 O TRP A 126 10441 10569 12002 917 1360 1256 O
ATOM 998 CB TRP A 126 25.690 394.336 30.739 1.00 69.04 C
ANISOU 998 CB TRP A 126 8222 8412 9598 954 1543 1189 C
ATOM 999 CG TRP A 126 27.114 394.063 30.296 1.00 87.75 C
ANISOU 999 CG TRP A 126 10588 10758 11997 953 1768 1264 C
ATOM 1000 CD1 TRP A 126 27.774 392.869 30.372 1.00 95.55 C
ANISOU 1000 CD1 TRP A 126 11517 11779 13007 942 1816 1197 C
ATOM 1001 CD2 TRP A 126 28.046 394.996 29.716 1.00 92.94 C
ANISOU 1001 CD2 TRP A 126 11286 11343 12685 968 1990 1426 C
ATOM 1002 NE1 TRP A 126 29.054 393.000 29.890 1.00 94.43 N
ANISOU 1002 NE1 TRP A 126 11366 11599 12915 955 2053 1302 N
ATOM 1003 CE2 TRP A 126 29.247 394.289 29.474 1.00 94.23 C
ANISOU 1003 CE2 TRP A 126 11395 11507 12901 965 2172 1448 C
ATOM 1004 CE3 TRP A 126 27.984 396.356 29.378 1.00 86.89 C
ANISOU 1004 CE3 TRP A 126 10591 10499 11924 983 2062 1562 C
ATOM 1005 CZ2 TRP A 126 30.371 394.890 28.913 1.00 96.94 C
ANISOU 1005 CZ2 TRP A 126 11736 11781 13315 973 2436 1604 C
ATOM 1006 CZ3 TRP A 126 29.105 396.954 28.815 1.00 85.32 C
ANISOU 1006 CZ3 TRP A 126 10406 10223 11790 985 2321 1722 C
ATOM 1007 CH2 TRP A 126 30.283 396.222 28.594 1.00 97.58 C
ANISOU 1007 CH2 TRP A 126 11885 11782 13408 976 2512 1743 C
ATOM 1008 N SER A 127 23.468 395.176 33.168 1.00 79.52 N
ANISOU 1008 N SER A 127 9323 9730 11161 829 1185 1047 N
ATOM 1009 CA SER A 127 22.266 395.882 33.605 1.00 78.18 C
ANISOU 1009 CA SER A 127 9135 9553 11018 849 1058 1024 C
ATOM 1010 C SER A 127 22.628 397.122 34.409 1.00 76.64 C
ANISOU 1010 C SER A 127 8894 9269 10958 794 1110 1084 C
ATOM 1011 O SER A 127 21.989 398.169 34.262 1.00 78.15 O
ANISOU 1011 O SER A 127 9137 9418 11140 845 1072 1128 O
ATOM 1012 CB SER A 127 21.355 394.953 34.404 1.00 69.43 C
ANISOU 1012 CB SER A 127 7919 8499 9961 816 931 902 C
ATOM 1013 OG SER A 127 20.765 394.004 33.536 1.00 69.43 O
ANISOU 1013 OG SER A 127 7972 8558 9849 877 842 840 O
ATOM 1014 N LEU A 128 23.613 397.009 35.306 1.00 74.58 N
ANISOU 1014 N LEU A 128 8536 8971 10830 695 1173 1076 N
ATOM 1015 CA LEU A 128 24.064 398.180 36.052 1.00 72.84 C
ANISOU 1015 CA LEU A 128 8279 8647 10749 639 1201 1118 C
ATOM 1016 C LEU A 128 24.716 399.201 35.131 1.00 77.58 C
ANISOU 1016 C LEU A 128 8961 9162 11355 660 1322 1253 C
ATOM 1017 O LEU A 128 24.605 400.413 35.354 1.00 74.95 O
ANISOU 1017 O LEU A 128 8650 8731 11096 656 1319 1302 O
ATOM 1018 CB LEU A 128 25.064 397.787 37.130 1.00 62.62 C
ANISOU 1018 CB LEU A 128 6870 7326 9596 538 1215 1074 C
ATOM 1019 CG LEU A 128 24.619 396.792 38.177 1.00 67.06 C
ANISOU 1019 CG LEU A 128 7366 7954 10161 513 1123 961 C
ATOM 1020 CD1 LEU A 128 25.684 396.744 39.273 1.00 66.88 C
ANISOU 1020 CD1 LEU A 128 7260 7875 10276 429 1117 932 C
ATOM 1021 CD2 LEU A 128 23.235 397.158 38.697 1.00 72.27 C
ANISOU 1021 CD2 LEU A 128 8044 8631 10786 558 1032 912 C
ATOM 1022 N VAL A 129 25.430 398.726 34.112 1.00 76.84 N
ANISOU 1022 N VAL A 129 8917 9091 11188 686 1443 1320 N
ATOM 1023 CA VAL A 129 26.000 399.627 33.119 1.00 79.65 C
ANISOU 1023 CA VAL A 129 9370 9366 11527 722 1595 1471 C
ATOM 1024 C VAL A 129 24.886 400.335 32.358 1.00 76.82 C
ANISOU 1024 C VAL A 129 9170 9007 11013 840 1532 1519 C
ATOM 1025 O VAL A 129 24.896 401.564 32.208 1.00 83.05 O
ANISOU 1025 O VAL A 129 10015 9688 11853 851 1575 1620 O
ATOM 1026 CB VAL A 129 26.947 398.857 32.178 1.00 72.10 C
ANISOU 1026 CB VAL A 129 8448 8446 10500 749 1762 1529 C
ATOM 1027 CG1 VAL A 129 27.445 399.759 31.060 1.00 69.35 C
ANISOU 1027 CG1 VAL A 129 8228 8016 10104 806 1952 1707 C
ATOM 1028 CG2 VAL A 129 28.105 398.299 32.966 1.00 67.83 C
ANISOU 1028 CG2 VAL A 129 7729 7888 10155 636 1819 1492 C
ATOM 1029 N VAL A 130 23.918 399.566 31.855 1.00 73.14 N
ANISOU 1029 N VAL A 130 8776 8649 10367 933 1415 1446 N
ATOM 1030 CA VAL A 130 22.860 400.148 31.031 1.00 85.81 C
ANISOU 1030 CA VAL A 130 10532 10257 11816 1064 1326 1485 C
ATOM 1031 C VAL A 130 21.975 401.074 31.866 1.00 83.17 C
ANISOU 1031 C VAL A 130 10138 9869 11592 1056 1206 1457 C
ATOM 1032 O VAL A 130 21.576 402.153 31.407 1.00 78.92 O
ANISOU 1032 O VAL A 130 9706 9259 11021 1133 1198 1547 O
ATOM 1033 CB VAL A 130 22.051 399.025 30.348 1.00 84.15 C
ANISOU 1033 CB VAL A 130 10390 10166 11419 1157 1194 1389 C
ATOM 1034 CG1 VAL A 130 20.686 399.513 29.908 1.00 69.44 C
ANISOU 1034 CG1 VAL A 130 8610 8315 9457 1277 1014 1375 C
ATOM 1035 CG2 VAL A 130 22.830 398.452 29.165 1.00 87.10 C
ANISOU 1035 CG2 VAL A 130 10912 10567 11616 1226 1327 1448 C
ATOM 1036 N LEU A 131 21.660 400.677 33.106 1.00 77.91 N
ANISOU 1036 N LEU A 131 9316 9232 11054 976 1121 1336 N
ATOM 1037 CA LEU A 131 20.893 401.560 33.980 1.00 71.26 C
ANISOU 1037 CA LEU A 131 8424 8335 10318 977 1037 1304 C
ATOM 1038 C LEU A 131 21.598 402.900 34.153 1.00 80.03 C
ANISOU 1038 C LEU A 131 9571 9296 11542 941 1132 1406 C
ATOM 1039 O LEU A 131 20.955 403.955 34.134 1.00 84.94 O
ANISOU 1039 O LEU A 131 10249 9842 12182 1006 1086 1444 O
ATOM 1040 CB LEU A 131 20.641 400.901 35.336 1.00 62.72 C
ANISOU 1040 CB LEU A 131 7191 7298 9341 899 976 1174 C
ATOM 1041 CG LEU A 131 19.844 401.767 36.327 1.00 67.39 C
ANISOU 1041 CG LEU A 131 7740 7834 10029 916 912 1130 C
ATOM 1042 CD1 LEU A 131 18.513 402.202 35.734 1.00 69.64 C
ANISOU 1042 CD1 LEU A 131 8069 8139 10253 1045 812 1138 C
ATOM 1043 CD2 LEU A 131 19.606 401.055 37.639 1.00 61.31 C
ANISOU 1043 CD2 LEU A 131 6854 7112 9329 857 880 1014 C
ATOM 1044 N ALA A 132 22.929 402.885 34.246 1.00 84.39 N
ANISOU 1044 N ALA A 132 10088 9791 12187 843 1263 1457 N
ATOM 1045 CA ALA A 132 23.655 404.134 34.431 1.00 76.14 C
ANISOU 1045 CA ALA A 132 9054 8581 11295 789 1347 1550 C
ATOM 1046 C ALA A 132 23.624 404.957 33.155 1.00 85.27 C
ANISOU 1046 C ALA A 132 10372 9666 12359 880 1440 1715 C
ATOM 1047 O ALA A 132 23.527 406.190 33.205 1.00 88.63 O
ANISOU 1047 O ALA A 132 10853 9953 12871 891 1450 1788 O
ATOM 1048 CB ALA A 132 25.102 403.852 34.843 1.00 65.61 C
ANISOU 1048 CB ALA A 132 7607 7198 10122 656 1453 1561 C
ATOM 1049 N ILE A 133 23.717 404.294 32.000 1.00 81.56 N
ANISOU 1049 N ILE A 133 10002 9281 11705 954 1510 1776 N
ATOM 1050 CA ILE A 133 23.597 405.011 30.736 1.00 77.76 C
ANISOU 1050 CA ILE A 133 9718 8743 11084 1072 1593 1937 C
ATOM 1051 C ILE A 133 22.214 405.628 30.614 1.00 88.68 C
ANISOU 1051 C ILE A 133 11191 10125 12377 1196 1421 1918 C
ATOM 1052 O ILE A 133 22.066 406.775 30.180 1.00 99.01 O
ANISOU 1052 O ILE A 133 12620 11312 13687 1260 1456 2044 O
ATOM 1053 CB ILE A 133 23.879 404.075 29.554 1.00 74.56 C
ANISOU 1053 CB ILE A 133 9432 8442 10456 1154 1682 1981 C
ATOM 1054 CG1 ILE A 133 25.310 403.539 29.607 1.00 77.13 C
ANISOU 1054 CG1 ILE A 133 9660 8755 10889 1046 1883 2018 C
ATOM 1055 CG2 ILE A 133 23.608 404.798 28.257 1.00 64.14 C
ANISOU 1055 CG2 ILE A 133 8357 7071 8941 1307 1746 2144 C
ATOM 1056 CD1 ILE A 133 25.687 402.736 28.373 1.00 72.01 C
ANISOU 1056 CD1 ILE A 133 9157 8188 10015 1146 2015 2077 C
ATOM 1057 N GLU A 134 21.179 404.885 31.018 1.00 89.29 N
ANISOU 1057 N GLU A 134 11199 10327 12401 1234 1236 1766 N
ATOM 1058 CA GLU A 134 19.818 405.382 30.852 1.00 83.71 C
ANISOU 1058 CA GLU A 134 10548 9629 11630 1364 1065 1742 C
ATOM 1059 C GLU A 134 19.574 406.592 31.749 1.00 81.12 C
ANISOU 1059 C GLU A 134 10169 9167 11484 1337 1045 1747 C
ATOM 1060 O GLU A 134 19.139 407.649 31.277 1.00 82.16 O
ANISOU 1060 O GLU A 134 10422 9202 11594 1437 1025 1844 O
ATOM 1061 CB GLU A 134 18.801 404.269 31.145 1.00 79.52 C
ANISOU 1061 CB GLU A 134 9912 9248 11054 1391 887 1578 C
ATOM 1062 CG GLU A 134 18.776 403.120 30.133 1.00 84.28 C
ANISOU 1062 CG GLU A 134 10595 9968 11458 1451 850 1553 C
ATOM 1063 CD GLU A 134 17.797 402.008 30.506 1.00103.28 C
ANISOU 1063 CD GLU A 134 12870 12496 13875 1452 671 1385 C
ATOM 1064 OE1 GLU A 134 17.277 402.023 31.645 1.00118.65 O
ANISOU 1064 OE1 GLU A 134 14648 14446 15987 1391 620 1298 O
ATOM 1065 OE2 GLU A 134 17.552 401.111 29.663 1.00104.91 O
ANISOU 1065 OE2 GLU A 134 13148 12786 13928 1518 588 1341 O
ATOM 1066 N ARG A 135 19.903 406.470 33.039 1.00 74.43 N
ANISOU 1066 N ARG A 135 9164 8303 10811 1211 1052 1644 N
ATOM 1067 CA ARG A 135 19.771 407.602 33.953 1.00 70.05 C
ANISOU 1067 CA ARG A 135 8581 7610 10424 1187 1034 1629 C
ATOM 1068 C ARG A 135 20.583 408.805 33.486 1.00 79.37 C
ANISOU 1068 C ARG A 135 9871 8604 11682 1167 1157 1789 C
ATOM 1069 O ARG A 135 20.141 409.950 33.632 1.00 81.93 O
ANISOU 1069 O ARG A 135 10256 8796 12076 1224 1122 1825 O
ATOM 1070 CB ARG A 135 20.166 407.195 35.373 1.00 64.23 C
ANISOU 1070 CB ARG A 135 7692 6883 9828 1061 1023 1493 C
ATOM 1071 CG ARG A 135 19.242 406.153 36.014 1.00 64.17 C
ANISOU 1071 CG ARG A 135 7577 7031 9774 1084 919 1347 C
ATOM 1072 CD ARG A 135 19.877 405.572 37.275 1.00 67.78 C
ANISOU 1072 CD ARG A 135 7922 7505 10327 961 936 1240 C
ATOM 1073 NE ARG A 135 18.938 404.910 38.184 1.00 69.78 N
ANISOU 1073 NE ARG A 135 8086 7856 10573 986 862 1112 N
ATOM 1074 CZ ARG A 135 19.333 404.241 39.263 1.00 75.99 C
ANISOU 1074 CZ ARG A 135 8796 8676 11401 905 869 1021 C
ATOM 1075 NH1 ARG A 135 20.629 404.150 39.525 1.00 80.41 N
ANISOU 1075 NH1 ARG A 135 9347 9183 12021 797 916 1032 N
ATOM 1076 NH2 ARG A 135 18.459 403.655 40.070 1.00 74.45 N
ANISOU 1076 NH2 ARG A 135 8532 8561 11194 934 833 927 N
ATOM 1077 N TYR A 136 21.776 408.572 32.933 1.00 86.23 N
ANISOU 1077 N TYR A 136 10759 9446 12558 1088 1313 1889 N
ATOM 1078 CA TYR A 136 22.582 409.678 32.415 1.00 81.68 C
ANISOU 1078 CA TYR A 136 10275 8680 12079 1061 1463 2064 C
ATOM 1079 C TYR A 136 21.866 410.392 31.277 1.00 85.80 C
ANISOU 1079 C TYR A 136 11002 9158 12440 1228 1461 2207 C
ATOM 1080 O TYR A 136 21.891 411.623 31.195 1.00 95.51 O
ANISOU 1080 O TYR A 136 12315 10205 13769 1248 1499 2314 O
ATOM 1081 CB TYR A 136 23.943 409.161 31.951 1.00 74.51 C
ANISOU 1081 CB TYR A 136 9331 7770 11209 960 1656 2153 C
ATOM 1082 CG TYR A 136 24.703 410.115 31.076 1.00 74.94 C
ANISOU 1082 CG TYR A 136 9500 7652 11321 957 1856 2374 C
ATOM 1083 CD1 TYR A 136 25.343 411.218 31.618 1.00 90.56 C
ANISOU 1083 CD1 TYR A 136 11423 9411 13573 847 1912 2428 C
ATOM 1084 CD2 TYR A 136 24.761 409.935 29.700 1.00 76.03 C
ANISOU 1084 CD2 TYR A 136 9815 7832 11239 1072 1991 2531 C
ATOM 1085 CE1 TYR A 136 26.041 412.114 30.818 1.00 96.09 C
ANISOU 1085 CE1 TYR A 136 12218 9931 14359 833 2116 2648 C
ATOM 1086 CE2 TYR A 136 25.455 410.831 28.883 1.00 85.14 C
ANISOU 1086 CE2 TYR A 136 11091 8818 12442 1078 2210 2759 C
ATOM 1087 CZ TYR A 136 26.093 411.916 29.453 1.00 95.74 C
ANISOU 1087 CZ TYR A 136 12352 9935 14089 951 2280 2824 C
ATOM 1088 OH TYR A 136 26.781 412.811 28.661 1.00102.81 O
ANISOU 1088 OH TYR A 136 13355 10643 15065 944 2514 3063 O
ATOM 1089 N VAL A 137 21.214 409.632 30.396 1.00 91.86 N
ANISOU 1089 N VAL A 137 11861 10080 12960 1357 1401 2207 N
ATOM 1090 CA VAL A 137 20.511 410.209 29.251 1.00 95.36 C
ANISOU 1090 CA VAL A 137 12523 10496 13215 1540 1367 2336 C
ATOM 1091 C VAL A 137 19.313 411.029 29.722 1.00105.33 C
ANISOU 1091 C VAL A 137 13782 11703 14536 1635 1186 2281 C
ATOM 1092 O VAL A 137 19.070 412.144 29.237 1.00108.54 O
ANISOU 1092 O VAL A 137 14338 11965 14936 1732 1199 2415 O
ATOM 1093 CB VAL A 137 20.103 409.088 28.273 1.00 76.84 C
ANISOU 1093 CB VAL A 137 10271 8333 10591 1655 1304 2311 C
ATOM 1094 CG1 VAL A 137 19.192 409.605 27.178 1.00 70.05 C
ANISOU 1094 CG1 VAL A 137 9638 7461 9516 1869 1198 2409 C
ATOM 1095 CG2 VAL A 137 21.340 408.464 27.653 1.00 67.73 C
ANISOU 1095 CG2 VAL A 137 9164 7204 9365 1594 1523 2399 C
ATOM 1096 N VAL A 138 18.543 410.483 30.668 1.00101.22 N
ANISOU 1096 N VAL A 138 13093 11288 14077 1617 1030 2089 N
ATOM 1097 CA VAL A 138 17.308 411.111 31.124 1.00 95.38 C
ANISOU 1097 CA VAL A 138 12325 10520 13393 1726 866 2021 C
ATOM 1098 C VAL A 138 17.584 412.412 31.880 1.00 97.77 C
ANISOU 1098 C VAL A 138 12630 10615 13904 1679 920 2052 C
ATOM 1099 O VAL A 138 16.786 413.357 31.811 1.00110.05 O
ANISOU 1099 O VAL A 138 14256 12074 15485 1805 839 2085 O
ATOM 1100 CB VAL A 138 16.527 410.091 31.972 1.00 85.73 C
ANISOU 1100 CB VAL A 138 10909 9464 12200 1705 735 1820 C
ATOM 1101 CG1 VAL A 138 15.414 410.758 32.729 1.00 97.04 C
ANISOU 1101 CG1 VAL A 138 12268 10853 13749 1789 619 1738 C
ATOM 1102 CG2 VAL A 138 15.987 408.975 31.078 1.00 72.14 C
ANISOU 1102 CG2 VAL A 138 9208 7916 10287 1786 631 1789 C
ATOM 1103 N VAL A 139 18.709 412.499 32.583 1.00 86.12 N
ANISOU 1103 N VAL A 139 11081 9055 12586 1506 1042 2038 N
ATOM 1104 CA VAL A 139 19.029 413.640 33.445 1.00 80.32 C
ANISOU 1104 CA VAL A 139 10334 8114 12071 1442 1065 2028 C
ATOM 1105 C VAL A 139 19.916 414.667 32.743 1.00 85.50 C
ANISOU 1105 C VAL A 139 11124 8555 12805 1408 1214 2231 C
ATOM 1106 O VAL A 139 19.636 415.866 32.782 1.00 98.90 O
ANISOU 1106 O VAL A 139 12913 10066 14599 1466 1198 2293 O
ATOM 1107 CB VAL A 139 19.667 413.150 34.762 1.00 75.18 C
ANISOU 1107 CB VAL A 139 9515 7482 11566 1278 1067 1868 C
ATOM 1108 CG1 VAL A 139 20.166 414.324 35.599 1.00 70.68 C
ANISOU 1108 CG1 VAL A 139 8953 6678 11224 1203 1077 1849 C
ATOM 1109 CG2 VAL A 139 18.640 412.369 35.543 1.00 70.75 C
ANISOU 1109 CG2 VAL A 139 8844 7092 10944 1333 939 1688 C
ATOM 1110 N CYS A 140 20.993 414.226 32.095 1.00 81.47 N
ANISOU 1110 N CYS A 140 10627 8057 12271 1317 1375 2343 N
ATOM 1111 CA CYS A 140 21.917 415.159 31.463 1.00 86.81 C
ANISOU 1111 CA CYS A 140 11408 8519 13056 1267 1557 2552 C
ATOM 1112 C CYS A 140 21.475 415.606 30.074 1.00 97.68 C
ANISOU 1112 C CYS A 140 13021 9866 14227 1442 1614 2757 C
ATOM 1113 O CYS A 140 22.107 416.512 29.517 1.00105.28 O
ANISOU 1113 O CYS A 140 14099 10628 15276 1424 1777 2956 O
ATOM 1114 CB CYS A 140 23.323 414.547 31.383 1.00 95.67 C
ANISOU 1114 CB CYS A 140 12426 9649 14273 1098 1738 2598 C
ATOM 1115 SG CYS A 140 24.037 414.000 32.974 1.00105.67 S
ANISOU 1115 SG CYS A 140 13431 10937 15783 894 1661 2372 S
ATOM 1116 N LYS A 141 20.399 415.023 29.523 1.00102.21 N
ANISOU 1116 N LYS A 141 13670 10620 14543 1614 1474 2715 N
ATOM 1117 CA LYS A 141 19.807 415.380 28.231 1.00107.43 C
ANISOU 1117 CA LYS A 141 14575 11274 14968 1816 1464 2882 C
ATOM 1118 C LYS A 141 20.870 415.720 27.182 1.00115.83 C
ANISOU 1118 C LYS A 141 15811 12220 15978 1800 1728 3134 C
ATOM 1119 O LYS A 141 20.996 416.884 26.783 1.00126.18 O
ANISOU 1119 O LYS A 141 17272 13317 17352 1845 1821 3317 O
ATOM 1120 CB LYS A 141 18.834 416.553 28.430 1.00106.35 C
ANISOU 1120 CB LYS A 141 14514 10994 14900 1945 1326 2896 C
ATOM 1121 CG LYS A 141 17.696 416.271 29.423 1.00104.76 C
ANISOU 1121 CG LYS A 141 14147 10905 14754 1988 1093 2662 C
ATOM 1122 CD LYS A 141 16.810 417.491 29.682 1.00110.76 C
ANISOU 1122 CD LYS A 141 14969 11504 15613 2118 980 2674 C
ATOM 1123 CE LYS A 141 15.772 417.202 30.776 1.00114.59 C
ANISOU 1123 CE LYS A 141 15264 12092 16181 2152 799 2442 C
ATOM 1124 NZ LYS A 141 15.018 418.415 31.223 1.00118.52 N
ANISOU 1124 NZ LYS A 141 15798 12418 16817 2267 715 2431 N
ATOM 1125 N PRO A 142 21.675 414.747 26.736 1.00119.85 N
ANISOU 1125 N PRO A 142 16300 12849 16386 1738 1875 3157 N
ATOM 1126 CA PRO A 142 22.699 415.034 25.716 1.00115.30 C
ANISOU 1126 CA PRO A 142 15886 12166 15757 1735 2168 3409 C
ATOM 1127 C PRO A 142 22.209 415.033 24.274 1.00125.46 C
ANISOU 1127 C PRO A 142 17490 13501 16677 1971 2190 3574 C
ATOM 1128 O PRO A 142 22.983 415.410 23.383 1.00136.92 O
ANISOU 1128 O PRO A 142 19117 14842 18063 1997 2458 3813 O
ATOM 1129 CB PRO A 142 23.722 413.916 25.938 1.00110.84 C
ANISOU 1129 CB PRO A 142 15148 11723 15244 1582 2306 3338 C
ATOM 1130 CG PRO A 142 22.895 412.767 26.418 1.00113.18 C
ANISOU 1130 CG PRO A 142 15332 12259 15414 1615 2057 3088 C
ATOM 1131 CD PRO A 142 21.781 413.366 27.248 1.00120.37 C
ANISOU 1131 CD PRO A 142 16180 13134 16421 1653 1807 2958 C
ATOM 1132 N MET A 143 20.970 414.631 24.010 1.00130.71 N
ANISOU 1132 N MET A 143 18237 14317 17108 2149 1921 3460 N
ATOM 1133 CA MET A 143 20.340 414.756 22.700 1.00147.53 C
ANISOU 1133 CA MET A 143 20690 16478 18888 2402 1867 3596 C
ATOM 1134 C MET A 143 19.186 415.739 22.840 1.00169.55 C
ANISOU 1134 C MET A 143 23545 19170 21708 2540 1638 3597 C
ATOM 1135 O MET A 143 18.360 415.602 23.748 1.00167.15 O
ANISOU 1135 O MET A 143 23039 18932 21540 2516 1403 3389 O
ATOM 1136 CB MET A 143 19.875 413.405 22.147 1.00141.57 C
ANISOU 1136 CB MET A 143 19984 15975 17832 2511 1716 3457 C
ATOM 1137 CG MET A 143 20.948 412.317 22.175 1.00141.68 C
ANISOU 1137 CG MET A 143 19892 16096 17843 2371 1915 3412 C
ATOM 1138 SD MET A 143 20.372 410.687 21.647 1.00139.20 S
ANISOU 1138 SD MET A 143 19620 16057 17212 2485 1710 3213 S
ATOM 1139 CE MET A 143 20.070 411.006 19.897 1.00142.89 C
ANISOU 1139 CE MET A 143 20560 16506 17225 2790 1730 3422 C
ATOM 1140 N SER A 144 19.114 416.724 21.943 1.00187.17 N
ANISOU 1140 N SER A 144 26062 21240 23813 2696 1717 3837 N
ATOM 1141 CA SER A 144 18.264 417.871 22.239 1.00200.28 C
ANISOU 1141 CA SER A 144 27758 22746 25595 2790 1556 3863 C
ATOM 1142 C SER A 144 16.788 417.531 22.095 1.00196.99 C
ANISOU 1142 C SER A 144 27355 22483 25009 2995 1188 3707 C
ATOM 1143 O SER A 144 15.964 418.001 22.888 1.00201.31 O
ANISOU 1143 O SER A 144 27752 22991 25746 3009 998 3584 O
ATOM 1144 CB SER A 144 18.630 419.036 21.314 1.00215.94 C
ANISOU 1144 CB SER A 144 30052 24492 27501 2902 1753 4181 C
ATOM 1145 OG SER A 144 18.778 418.600 19.970 1.00223.56 O
ANISOU 1145 OG SER A 144 31322 25539 28080 3076 1841 4338 O
ATOM 1146 N ASN A 145 16.422 416.748 21.089 1.00185.94 N
ANISOU 1146 N ASN A 145 26135 21247 23265 3163 1080 3707 N
ATOM 1147 CA ASN A 145 15.024 416.417 20.837 1.00170.50 C
ANISOU 1147 CA ASN A 145 24194 19426 21161 3366 707 3565 C
ATOM 1148 C ASN A 145 14.654 414.984 21.230 1.00159.59 C
ANISOU 1148 C ASN A 145 22582 18292 19761 3296 532 3297 C
ATOM 1149 O ASN A 145 13.861 414.336 20.545 1.00159.00 O
ANISOU 1149 O ASN A 145 22600 18358 19456 3465 282 3215 O
ATOM 1150 CB ASN A 145 14.634 416.751 19.400 1.00168.49 C
ANISOU 1150 CB ASN A 145 24336 19143 20539 3651 626 3751 C
ATOM 1151 CG ASN A 145 14.671 418.257 19.137 1.00165.54 C
ANISOU 1151 CG ASN A 145 24168 18509 20220 3749 730 4000 C
ATOM 1152 OD1 ASN A 145 14.394 419.059 20.036 1.00161.10 O
ANISOU 1152 OD1 ASN A 145 23430 17815 19966 3676 698 3963 O
ATOM 1153 ND2 ASN A 145 14.986 418.644 17.907 1.00166.91 N
ANISOU 1153 ND2 ASN A 145 24729 18600 20089 3926 853 4253 N
ATOM 1154 N PHE A 146 15.211 414.463 22.329 1.00150.62 N
ANISOU 1154 N PHE A 146 21153 17205 18873 3051 645 3155 N
ATOM 1155 CA PHE A 146 15.162 413.036 22.653 1.00134.62 C
ANISOU 1155 CA PHE A 146 18935 15391 16824 2956 558 2940 C
ATOM 1156 C PHE A 146 14.303 412.795 23.887 1.00123.25 C
ANISOU 1156 C PHE A 146 17167 14019 15645 2875 365 2712 C
ATOM 1157 O PHE A 146 14.419 413.508 24.889 1.00118.41 O
ANISOU 1157 O PHE A 146 16402 13292 15297 2766 440 2698 O
ATOM 1158 CB PHE A 146 16.556 412.447 22.905 1.00127.61 C
ANISOU 1158 CB PHE A 146 17977 14520 15988 2747 855 2961 C
ATOM 1159 CG PHE A 146 16.557 410.945 23.092 1.00119.39 C
ANISOU 1159 CG PHE A 146 16786 13688 14890 2672 774 2760 C
ATOM 1160 CD1 PHE A 146 16.603 410.084 22.008 1.00117.81 C
ANISOU 1160 CD1 PHE A 146 16781 13604 14376 2792 739 2763 C
ATOM 1161 CD2 PHE A 146 16.516 410.398 24.370 1.00113.33 C
ANISOU 1161 CD2 PHE A 146 15697 12986 14378 2489 737 2569 C
ATOM 1162 CE1 PHE A 146 16.598 408.707 22.196 1.00114.83 C
ANISOU 1162 CE1 PHE A 146 16267 13396 13966 2721 659 2573 C
ATOM 1163 CE2 PHE A 146 16.513 409.024 24.561 1.00103.99 C
ANISOU 1163 CE2 PHE A 146 14380 11975 13157 2419 669 2396 C
ATOM 1164 CZ PHE A 146 16.553 408.181 23.473 1.00107.51 C
ANISOU 1164 CZ PHE A 146 15008 12526 13314 2530 627 2396 C
ATOM 1165 N ARG A 147 13.471 411.754 23.810 1.00120.58 N
ANISOU 1165 N ARG A 147 16724 13859 15233 2929 126 2533 N
ATOM 1166 CA ARG A 147 12.634 411.307 24.918 1.00125.38 C
ANISOU 1166 CA ARG A 147 17011 14552 16076 2854 -35 2318 C
ATOM 1167 C ARG A 147 12.745 409.792 25.040 1.00121.12 C
ANISOU 1167 C ARG A 147 16334 14194 15493 2752 -78 2152 C
ATOM 1168 O ARG A 147 12.461 409.069 24.078 1.00120.91 O
ANISOU 1168 O ARG A 147 16436 14264 15239 2864 -223 2124 O
ATOM 1169 CB ARG A 147 11.172 411.719 24.710 1.00136.06 C
ANISOU 1169 CB ARG A 147 18339 15908 17450 3055 -334 2269 C
ATOM 1170 CG ARG A 147 10.187 411.012 25.633 1.00141.96 C
ANISOU 1170 CG ARG A 147 18755 16773 18411 3004 -510 2046 C
ATOM 1171 CD ARG A 147 10.186 411.696 26.998 1.00146.75 C
ANISOU 1171 CD ARG A 147 19161 17289 19309 2892 -382 2006 C
ATOM 1172 NE ARG A 147 9.218 411.129 27.934 1.00150.05 N
ANISOU 1172 NE ARG A 147 19272 17805 19938 2860 -506 1817 N
ATOM 1173 CZ ARG A 147 9.529 410.268 28.899 1.00148.47 C
ANISOU 1173 CZ ARG A 147 18866 17689 19856 2676 -403 1691 C
ATOM 1174 NH1 ARG A 147 10.789 409.881 29.066 1.00143.58 N
ANISOU 1174 NH1 ARG A 147 18305 17073 19178 2511 -200 1722 N
ATOM 1175 NH2 ARG A 147 8.584 409.801 29.707 1.00146.53 N
ANISOU 1175 NH2 ARG A 147 18354 17519 19800 2664 -496 1541 N
ATOM 1176 N PHE A 148 13.149 409.316 26.217 1.00117.24 N
ANISOU 1176 N PHE A 148 15598 13738 15212 2549 36 2039 N
ATOM 1177 CA PHE A 148 13.417 407.899 26.448 1.00114.72 C
ANISOU 1177 CA PHE A 148 15146 13565 14877 2429 36 1897 C
ATOM 1178 C PHE A 148 12.111 407.140 26.662 1.00110.80 C
ANISOU 1178 C PHE A 148 14463 13186 14451 2482 -236 1717 C
ATOM 1179 O PHE A 148 11.394 407.389 27.637 1.00113.20 O
ANISOU 1179 O PHE A 148 14549 13480 14981 2452 -291 1633 O
ATOM 1180 CB PHE A 148 14.329 407.752 27.668 1.00114.36 C
ANISOU 1180 CB PHE A 148 14921 13497 15034 2207 248 1857 C
ATOM 1181 CG PHE A 148 14.604 406.332 28.065 1.00113.18 C
ANISOU 1181 CG PHE A 148 14621 13483 14898 2080 255 1714 C
ATOM 1182 CD1 PHE A 148 15.575 405.587 27.418 1.00107.57 C
ANISOU 1182 CD1 PHE A 148 14024 12820 14029 2039 375 1751 C
ATOM 1183 CD2 PHE A 148 13.899 405.747 29.110 1.00116.44 C
ANISOU 1183 CD2 PHE A 148 14784 13968 15492 2008 159 1552 C
ATOM 1184 CE1 PHE A 148 15.824 404.277 27.793 1.00105.82 C
ANISOU 1184 CE1 PHE A 148 13668 12710 13830 1930 376 1619 C
ATOM 1185 CE2 PHE A 148 14.145 404.437 29.491 1.00109.11 C
ANISOU 1185 CE2 PHE A 148 13726 13148 14583 1892 170 1433 C
ATOM 1186 CZ PHE A 148 15.110 403.703 28.829 1.00104.88 C
ANISOU 1186 CZ PHE A 148 13306 12653 13892 1853 268 1463 C
ATOM 1187 N GLY A 149 11.836 406.165 25.791 1.00106.39 N
ANISOU 1187 N GLY A 149 13979 12732 13712 2553 -393 1651 N
ATOM 1188 CA GLY A 149 10.588 405.431 25.878 1.00103.40 C
ANISOU 1188 CA GLY A 149 13417 12447 13424 2601 -671 1483 C
ATOM 1189 C GLY A 149 10.690 403.920 25.868 1.00111.24 C
ANISOU 1189 C GLY A 149 14314 13558 14395 2505 -726 1335 C
ATOM 1190 O GLY A 149 11.767 403.363 26.085 1.00107.77 O
ANISOU 1190 O GLY A 149 13897 13139 13911 2371 -520 1344 O
ATOM 1191 N GLU A 150 9.559 403.251 25.623 1.00123.19 N
ANISOU 1191 N GLU A 150 15708 15137 15962 2573 -1012 1196 N
ATOM 1192 CA GLU A 150 9.502 401.791 25.702 1.00118.70 C
ANISOU 1192 CA GLU A 150 15015 14660 15425 2473 -1090 1039 C
ATOM 1193 C GLU A 150 10.507 401.123 24.763 1.00112.81 C
ANISOU 1193 C GLU A 150 14534 13945 14385 2487 -1019 1062 C
ATOM 1194 O GLU A 150 11.212 400.195 25.169 1.00112.62 O
ANISOU 1194 O GLU A 150 14442 13962 14387 2341 -880 1003 O
ATOM 1195 CB GLU A 150 8.075 401.300 25.453 1.00128.07 C
ANISOU 1195 CB GLU A 150 16037 15885 16738 2558 -1437 895 C
ATOM 1196 CG GLU A 150 7.909 399.803 25.689 1.00131.58 C
ANISOU 1196 CG GLU A 150 16308 16399 17287 2433 -1519 726 C
ATOM 1197 CD GLU A 150 6.535 399.284 25.321 1.00139.26 C
ANISOU 1197 CD GLU A 150 17117 17392 18404 2512 -1884 581 C
ATOM 1198 OE1 GLU A 150 5.658 400.100 24.962 1.00144.08 O
ANISOU 1198 OE1 GLU A 150 17720 17971 19053 2669 -2080 607 O
ATOM 1199 OE2 GLU A 150 6.326 398.057 25.427 1.00140.31 O
ANISOU 1199 OE2 GLU A 150 17111 17561 18640 2414 -1979 440 O
ATOM 1200 N ASN A 151 10.562 401.543 23.491 1.00115.71 N
ANISOU 1200 N ASN A 151 15214 14290 14461 2676 -1114 1145 N
ATOM 1201 CA ASN A 151 11.455 400.863 22.548 1.00117.81 C
ANISOU 1201 CA ASN A 151 15749 14587 14426 2716 -1039 1159 C
ATOM 1202 C ASN A 151 12.916 401.006 22.968 1.00117.53 C
ANISOU 1202 C ASN A 151 15756 14525 14375 2579 -647 1280 C
ATOM 1203 O ASN A 151 13.694 400.050 22.862 1.00122.77 O
ANISOU 1203 O ASN A 151 16453 15233 14960 2505 -531 1231 O
ATOM 1204 CB ASN A 151 11.268 401.383 21.119 1.00124.58 C
ANISOU 1204 CB ASN A 151 16973 15419 14942 2968 -1185 1247 C
ATOM 1205 CG ASN A 151 9.869 401.166 20.583 1.00134.46 C
ANISOU 1205 CG ASN A 151 18199 16694 16193 3122 -1619 1111 C
ATOM 1206 OD1 ASN A 151 9.023 400.564 21.243 1.00138.28 O
ANISOU 1206 OD1 ASN A 151 18372 17214 16954 3031 -1802 949 O
ATOM 1207 ND2 ASN A 151 9.625 401.635 19.364 1.00138.61 N
ANISOU 1207 ND2 ASN A 151 19058 17196 16412 3362 -1787 1180 N
ATOM 1208 N HIS A 152 13.309 402.189 23.445 1.00109.45 N
ANISOU 1208 N HIS A 152 14723 13417 13446 2545 -451 1434 N
ATOM 1209 CA HIS A 152 14.685 402.392 23.894 1.00 97.32 C
ANISOU 1209 CA HIS A 152 13192 11838 11948 2404 -102 1546 C
ATOM 1210 C HIS A 152 15.016 401.486 25.076 1.00100.24 C
ANISOU 1210 C HIS A 152 13278 12260 12549 2192 -21 1418 C
ATOM 1211 O HIS A 152 16.111 400.917 25.147 1.00104.38 O
ANISOU 1211 O HIS A 152 13819 12800 13042 2096 182 1433 O
ATOM 1212 CB HIS A 152 14.920 403.861 24.241 1.00 92.35 C
ANISOU 1212 CB HIS A 152 12585 11086 11418 2402 48 1714 C
ATOM 1213 CG HIS A 152 14.675 404.798 23.099 1.00104.09 C
ANISOU 1213 CG HIS A 152 14371 12503 12677 2612 -3 1868 C
ATOM 1214 ND1 HIS A 152 13.529 405.557 22.990 1.00109.49 N
ANISOU 1214 ND1 HIS A 152 15058 13149 13394 2748 -231 1873 N
ATOM 1215 CD2 HIS A 152 15.426 405.094 22.011 1.00111.38 C
ANISOU 1215 CD2 HIS A 152 15607 13383 13329 2722 154 2033 C
ATOM 1216 CE1 HIS A 152 13.585 406.280 21.886 1.00119.27 C
ANISOU 1216 CE1 HIS A 152 16611 14321 14384 2934 -231 2033 C
ATOM 1217 NE2 HIS A 152 14.726 406.019 21.274 1.00122.60 N
ANISOU 1217 NE2 HIS A 152 17234 14739 14610 2922 12 2138 N
ATOM 1218 N ALA A 153 14.086 401.344 26.019 1.00102.58 N
ANISOU 1218 N ALA A 153 13316 12579 13081 2127 -166 1300 N
ATOM 1219 CA ALA A 153 14.350 400.522 27.196 1.00104.78 C
ANISOU 1219 CA ALA A 153 13346 12899 13568 1939 -83 1193 C
ATOM 1220 C ALA A 153 14.462 399.042 26.844 1.00102.22 C
ANISOU 1220 C ALA A 153 13017 12658 13165 1909 -155 1066 C
ATOM 1221 O ALA A 153 15.208 398.306 27.504 1.00 98.04 O
ANISOU 1221 O ALA A 153 12382 12151 12718 1767 -11 1026 O
ATOM 1222 CB ALA A 153 13.255 400.734 28.242 1.00100.82 C
ANISOU 1222 CB ALA A 153 12589 12397 13321 1900 -199 1110 C
ATOM 1223 N ILE A 154 13.734 398.586 25.821 1.00 97.30 N
ANISOU 1223 N ILE A 154 12512 12071 12386 2046 -392 995 N
ATOM 1224 CA ILE A 154 13.908 397.216 25.340 1.00 97.97 C
ANISOU 1224 CA ILE A 154 12640 12214 12368 2035 -468 871 C
ATOM 1225 C ILE A 154 15.302 397.021 24.748 1.00101.96 C
ANISOU 1225 C ILE A 154 13364 12717 12658 2043 -226 959 C
ATOM 1226 O ILE A 154 15.994 396.048 25.077 1.00107.31 O
ANISOU 1226 O ILE A 154 13978 13423 13374 1937 -115 897 O
ATOM 1227 CB ILE A 154 12.795 396.839 24.339 1.00 92.16 C
ANISOU 1227 CB ILE A 154 12001 11503 11513 2193 -812 762 C
ATOM 1228 CG1 ILE A 154 11.449 396.699 25.054 1.00 86.90 C
ANISOU 1228 CG1 ILE A 154 11038 10844 11138 2147 -1038 647 C
ATOM 1229 CG2 ILE A 154 13.129 395.559 23.603 1.00 84.89 C
ANISOU 1229 CG2 ILE A 154 11215 10620 10420 2218 -884 645 C
ATOM 1230 CD1 ILE A 154 10.277 397.057 24.194 1.00 91.67 C
ANISOU 1230 CD1 ILE A 154 11710 11440 11680 2328 -1369 604 C
ATOM 1231 N MET A 155 15.727 397.924 23.853 1.00 92.67 N
ANISOU 1231 N MET A 155 12449 11500 11260 2178 -131 1112 N
ATOM 1232 CA MET A 155 17.105 397.902 23.359 1.00 91.48 C
ANISOU 1232 CA MET A 155 12482 11332 10942 2183 159 1229 C
ATOM 1233 C MET A 155 18.122 397.733 24.488 1.00 89.72 C
ANISOU 1233 C MET A 155 12043 11096 10950 1979 413 1253 C
ATOM 1234 O MET A 155 18.995 396.860 24.424 1.00 95.69 O
ANISOU 1234 O MET A 155 12808 11880 11669 1928 551 1222 O
ATOM 1235 CB MET A 155 17.422 399.171 22.572 1.00101.37 C
ANISOU 1235 CB MET A 155 13985 12515 12016 2318 287 1435 C
ATOM 1236 CG MET A 155 17.022 399.143 21.115 1.00119.44 C
ANISOU 1236 CG MET A 155 16615 14818 13949 2556 139 1451 C
ATOM 1237 SD MET A 155 17.059 400.817 20.426 1.00138.85 S
ANISOU 1237 SD MET A 155 19329 17173 16256 2712 243 1705 S
ATOM 1238 CE MET A 155 18.812 401.186 20.535 1.00135.86 C
ANISOU 1238 CE MET A 155 18987 16726 15906 2602 734 1907 C
ATOM 1239 N GLY A 156 18.007 398.539 25.545 1.00 86.65 N
ANISOU 1239 N GLY A 156 11462 10659 10801 1870 460 1298 N
ATOM 1240 CA GLY A 156 18.932 398.403 26.659 1.00 83.52 C
ANISOU 1240 CA GLY A 156 10872 10244 10619 1687 658 1307 C
ATOM 1241 C GLY A 156 18.976 397.000 27.230 1.00 87.64 C
ANISOU 1241 C GLY A 156 11237 10835 11228 1586 607 1150 C
ATOM 1242 O GLY A 156 20.053 396.478 27.523 1.00 93.18 O
ANISOU 1242 O GLY A 156 11892 11538 11973 1497 784 1159 O
ATOM 1243 N VAL A 157 17.816 396.360 27.379 1.00 89.26 N
ANISOU 1243 N VAL A 157 11350 11088 11476 1600 366 1008 N
ATOM 1244 CA VAL A 157 17.793 395.018 27.954 1.00 81.78 C
ANISOU 1244 CA VAL A 157 10253 10187 10633 1498 319 867 C
ATOM 1245 C VAL A 157 18.425 394.028 26.985 1.00 83.82 C
ANISOU 1245 C VAL A 157 10680 10475 10692 1560 350 825 C
ATOM 1246 O VAL A 157 19.312 393.247 27.357 1.00 81.27 O
ANISOU 1246 O VAL A 157 10300 10160 10419 1474 487 801 O
ATOM 1247 CB VAL A 157 16.355 394.613 28.321 1.00 75.49 C
ANISOU 1247 CB VAL A 157 9301 9416 9966 1493 67 738 C
ATOM 1248 CG1 VAL A 157 16.314 393.157 28.759 1.00 77.08 C
ANISOU 1248 CG1 VAL A 157 9375 9647 10265 1396 19 603 C
ATOM 1249 CG2 VAL A 157 15.845 395.491 29.446 1.00 70.55 C
ANISOU 1249 CG2 VAL A 157 8493 8761 9551 1427 88 775 C
ATOM 1250 N ALA A 158 17.962 394.040 25.730 1.00 81.75 N
ANISOU 1250 N ALA A 158 10640 10225 10195 1725 212 810 N
ATOM 1251 CA ALA A 158 18.580 393.235 24.683 1.00 77.76 C
ANISOU 1251 CA ALA A 158 10355 9741 9451 1822 254 777 C
ATOM 1252 C ALA A 158 20.094 393.406 24.682 1.00 89.18 C
ANISOU 1252 C ALA A 158 11854 11167 10863 1787 591 907 C
ATOM 1253 O ALA A 158 20.845 392.432 24.537 1.00 95.34 O
ANISOU 1253 O ALA A 158 12660 11964 11602 1773 694 854 O
ATOM 1254 CB ALA A 158 17.992 393.618 23.324 1.00 69.25 C
ANISOU 1254 CB ALA A 158 9564 8665 8084 2034 93 789 C
ATOM 1255 N PHE A 159 20.556 394.649 24.841 1.00 89.26 N
ANISOU 1255 N PHE A 159 11871 11129 10912 1774 766 1077 N
ATOM 1256 CA PHE A 159 21.986 394.923 24.821 1.00 84.32 C
ANISOU 1256 CA PHE A 159 11269 10469 10301 1734 1088 1214 C
ATOM 1257 C PHE A 159 22.718 394.130 25.895 1.00 84.10 C
ANISOU 1257 C PHE A 159 11003 10450 10503 1567 1182 1149 C
ATOM 1258 O PHE A 159 23.805 393.598 25.641 1.00 93.45 O
ANISOU 1258 O PHE A 159 12215 11635 11658 1566 1379 1176 O
ATOM 1259 CB PHE A 159 22.235 396.416 24.988 1.00 77.99 C
ANISOU 1259 CB PHE A 159 10468 9590 9574 1717 1223 1394 C
ATOM 1260 CG PHE A 159 23.678 396.769 25.053 1.00 76.79 C
ANISOU 1260 CG PHE A 159 10292 9382 9505 1652 1546 1538 C
ATOM 1261 CD1 PHE A 159 24.430 396.855 23.894 1.00 77.82 C
ANISOU 1261 CD1 PHE A 159 10651 9495 9421 1777 1762 1662 C
ATOM 1262 CD2 PHE A 159 24.288 397.022 26.269 1.00 71.37 C
ANISOU 1262 CD2 PHE A 159 9353 8651 9114 1475 1635 1552 C
ATOM 1263 CE1 PHE A 159 25.771 397.177 23.942 1.00 76.91 C
ANISOU 1263 CE1 PHE A 159 10479 9318 9423 1713 2079 1804 C
ATOM 1264 CE2 PHE A 159 25.630 397.348 26.324 1.00 74.68 C
ANISOU 1264 CE2 PHE A 159 9719 9006 9650 1410 1912 1679 C
ATOM 1265 CZ PHE A 159 26.372 397.427 25.157 1.00 77.02 C
ANISOU 1265 CZ PHE A 159 10211 9284 9769 1523 2143 1809 C
ATOM 1266 N THR A 160 22.149 394.048 27.104 1.00 73.06 N
ANISOU 1266 N THR A 160 9373 9055 9330 1437 1052 1069 N
ATOM 1267 CA THR A 160 22.806 393.276 28.153 1.00 78.33 C
ANISOU 1267 CA THR A 160 9839 9728 10195 1294 1122 1009 C
ATOM 1268 C THR A 160 22.899 391.808 27.763 1.00 85.34 C
ANISOU 1268 C THR A 160 10769 10660 10997 1325 1073 883 C
ATOM 1269 O THR A 160 23.903 391.149 28.048 1.00 92.91 O
ANISOU 1269 O THR A 160 11662 11614 12023 1272 1215 878 O
ATOM 1270 CB THR A 160 22.083 393.430 29.501 1.00 80.71 C
ANISOU 1270 CB THR A 160 9926 10025 10717 1174 995 949 C
ATOM 1271 OG1 THR A 160 20.778 392.832 29.447 1.00 82.16 O
ANISOU 1271 OG1 THR A 160 10089 10248 10880 1205 762 824 O
ATOM 1272 CG2 THR A 160 21.991 394.885 29.930 1.00 74.60 C
ANISOU 1272 CG2 THR A 160 9120 9193 10031 1151 1037 1058 C
ATOM 1273 N TRP A 161 21.880 391.287 27.076 1.00 85.91 N
ANISOU 1273 N TRP A 161 10952 10763 10928 1418 860 775 N
ATOM 1274 CA TRP A 161 21.918 389.888 26.661 1.00 85.98 C
ANISOU 1274 CA TRP A 161 11017 10793 10857 1452 790 638 C
ATOM 1275 C TRP A 161 22.991 389.652 25.608 1.00 92.22 C
ANISOU 1275 C TRP A 161 12018 11584 11436 1570 988 690 C
ATOM 1276 O TRP A 161 23.636 388.593 25.594 1.00 88.11 O
ANISOU 1276 O TRP A 161 11492 11066 10920 1562 1058 619 O
ATOM 1277 CB TRP A 161 20.556 389.460 26.132 1.00 82.81 C
ANISOU 1277 CB TRP A 161 10684 10407 10373 1525 489 502 C
ATOM 1278 CG TRP A 161 19.482 389.526 27.149 1.00 89.38 C
ANISOU 1278 CG TRP A 161 11287 11236 11439 1413 318 446 C
ATOM 1279 CD1 TRP A 161 19.628 389.713 28.495 1.00 86.18 C
ANISOU 1279 CD1 TRP A 161 10653 10820 11271 1265 404 483 C
ATOM 1280 CD2 TRP A 161 18.080 389.417 26.909 1.00102.79 C
ANISOU 1280 CD2 TRP A 161 12960 12937 13158 1452 35 344 C
ATOM 1281 NE1 TRP A 161 18.401 389.722 29.109 1.00 78.93 N
ANISOU 1281 NE1 TRP A 161 9579 9901 10510 1214 225 419 N
ATOM 1282 CE2 TRP A 161 17.432 389.543 28.156 1.00102.76 C
ANISOU 1282 CE2 TRP A 161 12697 12926 13422 1320 -3 335 C
ATOM 1283 CE3 TRP A 161 17.305 389.221 25.758 1.00102.99 C
ANISOU 1283 CE3 TRP A 161 13159 12967 13007 1594 -199 255 C
ATOM 1284 CZ2 TRP A 161 16.041 389.482 28.282 1.00110.67 C
ANISOU 1284 CZ2 TRP A 161 13578 13923 14549 1318 -240 251 C
ATOM 1285 CZ3 TRP A 161 15.927 389.156 25.887 1.00 98.92 C
ANISOU 1285 CZ3 TRP A 161 12518 12444 12625 1587 -473 159 C
ATOM 1286 CH2 TRP A 161 15.309 389.287 27.138 1.00102.90 C
ANISOU 1286 CH2 TRP A 161 12732 12939 13425 1445 -479 163 C
ATOM 1287 N VAL A 162 23.190 390.621 24.714 1.00 92.75 N
ANISOU 1287 N VAL A 162 12281 11643 11315 1690 1093 818 N
ATOM 1288 CA VAL A 162 24.240 390.488 23.713 1.00 90.61 C
ANISOU 1288 CA VAL A 162 12219 11369 10840 1813 1333 894 C
ATOM 1289 C VAL A 162 25.613 390.531 24.380 1.00 93.15 C
ANISOU 1289 C VAL A 162 12365 11664 11364 1702 1624 994 C
ATOM 1290 O VAL A 162 26.482 389.698 24.093 1.00 96.77 O
ANISOU 1290 O VAL A 162 12854 12127 11786 1738 1776 967 O
ATOM 1291 CB VAL A 162 24.082 391.566 22.628 1.00 83.02 C
ANISOU 1291 CB VAL A 162 11522 10395 9629 1973 1390 1031 C
ATOM 1292 CG1 VAL A 162 25.341 391.684 21.802 1.00 81.24 C
ANISOU 1292 CG1 VAL A 162 11468 10152 9247 2075 1732 1169 C
ATOM 1293 CG2 VAL A 162 22.892 391.245 21.751 1.00 81.85 C
ANISOU 1293 CG2 VAL A 162 11593 10275 9233 2126 1089 906 C
ATOM 1294 N MET A 163 25.841 391.511 25.267 1.00 91.01 N
ANISOU 1294 N MET A 163 11906 11356 11316 1573 1696 1103 N
ATOM 1295 CA MET A 163 27.120 391.557 25.978 1.00 95.11 C
ANISOU 1295 CA MET A 163 12232 11841 12066 1458 1924 1181 C
ATOM 1296 C MET A 163 27.358 390.298 26.802 1.00101.01 C
ANISOU 1296 C MET A 163 12806 12610 12964 1369 1856 1042 C
ATOM 1297 O MET A 163 28.482 389.783 26.843 1.00107.52 O
ANISOU 1297 O MET A 163 13564 13422 13866 1358 2041 1063 O
ATOM 1298 CB MET A 163 27.204 392.788 26.885 1.00 89.87 C
ANISOU 1298 CB MET A 163 11399 11121 11628 1330 1951 1286 C
ATOM 1299 CG MET A 163 27.345 394.121 26.185 1.00 92.71 C
ANISOU 1299 CG MET A 163 11895 11425 11908 1394 2094 1465 C
ATOM 1300 SD MET A 163 28.630 394.064 24.925 1.00 95.66 S
ANISOU 1300 SD MET A 163 12439 11776 12132 1519 2453 1612 S
ATOM 1301 CE MET A 163 27.637 394.020 23.436 1.00 92.38 C
ANISOU 1301 CE MET A 163 12410 11407 11283 1754 2348 1598 C
ATOM 1302 N ALA A 164 26.316 389.787 27.465 1.00 94.74 N
ANISOU 1302 N ALA A 164 11932 11840 12226 1308 1600 907 N
ATOM 1303 CA ALA A 164 26.492 388.605 28.304 1.00 83.74 C
ANISOU 1303 CA ALA A 164 10384 10452 10980 1221 1537 792 C
ATOM 1304 C ALA A 164 26.758 387.368 27.461 1.00 91.85 C
ANISOU 1304 C ALA A 164 11552 11495 11854 1328 1556 695 C
ATOM 1305 O ALA A 164 27.564 386.512 27.844 1.00102.18 O
ANISOU 1305 O ALA A 164 12767 12790 13267 1295 1641 659 O
ATOM 1306 CB ALA A 164 25.277 388.397 29.199 1.00 82.46 C
ANISOU 1306 CB ALA A 164 10108 10300 10923 1133 1292 692 C
ATOM 1307 N LEU A 165 26.073 387.237 26.324 1.00 89.04 N
ANISOU 1307 N LEU A 165 11427 11157 11245 1467 1458 640 N
ATOM 1308 CA LEU A 165 26.385 386.123 25.441 1.00 87.07 C
ANISOU 1308 CA LEU A 165 11349 10910 10822 1590 1483 541 C
ATOM 1309 C LEU A 165 27.797 386.264 24.901 1.00 89.13 C
ANISOU 1309 C LEU A 165 11673 11163 11029 1668 1812 658 C
ATOM 1310 O LEU A 165 28.512 385.268 24.755 1.00 95.22 O
ANISOU 1310 O LEU A 165 12453 11924 11802 1710 1910 596 O
ATOM 1311 CB LEU A 165 25.368 386.025 24.302 1.00 85.80 C
ANISOU 1311 CB LEU A 165 11452 10765 10383 1739 1286 451 C
ATOM 1312 CG LEU A 165 24.030 385.390 24.703 1.00 78.89 C
ANISOU 1312 CG LEU A 165 10502 9884 9589 1675 947 284 C
ATOM 1313 CD1 LEU A 165 23.033 385.480 23.572 1.00 79.11 C
ANISOU 1313 CD1 LEU A 165 10774 9920 9363 1826 723 202 C
ATOM 1314 CD2 LEU A 165 24.207 383.952 25.144 1.00 73.93 C
ANISOU 1314 CD2 LEU A 165 9785 9223 9081 1617 893 143 C
ATOM 1315 N ALA A 166 28.240 387.500 24.670 1.00 90.15 N
ANISOU 1315 N ALA A 166 11821 11284 11147 1680 1997 835 N
ATOM 1316 CA ALA A 166 29.568 387.713 24.117 1.00 87.22 C
ANISOU 1316 CA ALA A 166 11491 10895 10754 1751 2340 968 C
ATOM 1317 C ALA A 166 30.666 387.280 25.081 1.00 94.93 C
ANISOU 1317 C ALA A 166 12190 11846 12034 1629 2475 983 C
ATOM 1318 O ALA A 166 31.777 386.977 24.634 1.00 99.52 O
ANISOU 1318 O ALA A 166 12779 12414 12621 1701 2737 1040 O
ATOM 1319 CB ALA A 166 29.743 389.190 23.751 1.00 74.83 C
ANISOU 1319 CB ALA A 166 9978 9300 9153 1767 2502 1167 C
ATOM 1320 N CYS A 167 30.394 387.254 26.387 1.00 91.74 N
ANISOU 1320 N CYS A 167 11546 11433 11878 1460 2309 937 N
ATOM 1321 CA CYS A 167 31.351 386.683 27.326 1.00 90.81 C
ANISOU 1321 CA CYS A 167 11189 11292 12025 1363 2379 926 C
ATOM 1322 C CYS A 167 31.130 385.185 27.525 1.00 93.18 C
ANISOU 1322 C CYS A 167 11494 11600 12308 1383 2241 756 C
ATOM 1323 O CYS A 167 32.087 384.402 27.476 1.00 91.66 O
ANISOU 1323 O CYS A 167 11250 11390 12185 1423 2380 739 O
ATOM 1324 CB CYS A 167 31.284 387.411 28.668 1.00 85.26 C
ANISOU 1324 CB CYS A 167 10250 10563 11582 1188 2280 967 C
ATOM 1325 SG CYS A 167 31.894 386.408 30.037 1.00 95.21 S
ANISOU 1325 SG CYS A 167 11261 11804 13111 1076 2203 884 S
ATOM 1326 N ALA A 168 29.871 384.776 27.734 1.00 78.87 N
ANISOU 1326 N ALA A 168 9738 9803 10426 1356 1973 633 N
ATOM 1327 CA ALA A 168 29.550 383.449 28.252 1.00 71.22 C
ANISOU 1327 CA ALA A 168 8720 8818 9522 1322 1813 484 C
ATOM 1328 C ALA A 168 29.556 382.375 27.173 1.00 85.15 C
ANISOU 1328 C ALA A 168 10696 10575 11084 1473 1817 368 C
ATOM 1329 O ALA A 168 29.749 381.193 27.485 1.00 82.08 O
ANISOU 1329 O ALA A 168 10266 10150 10771 1467 1769 265 O
ATOM 1330 CB ALA A 168 28.184 383.459 28.938 1.00 70.51 C
ANISOU 1330 CB ALA A 168 8579 8732 9478 1224 1544 410 C
ATOM 1331 N ALA A 169 29.354 382.754 25.923 1.00 88.68 N
ANISOU 1331 N ALA A 169 11384 11044 11267 1618 1868 380 N
ATOM 1332 CA ALA A 169 29.170 381.794 24.845 1.00 83.96 C
ANISOU 1332 CA ALA A 169 11036 10434 10431 1779 1824 244 C
ATOM 1333 C ALA A 169 30.470 381.366 24.160 1.00 87.20 C
ANISOU 1333 C ALA A 169 11535 10834 10764 1919 2120 279 C
ATOM 1334 O ALA A 169 30.544 380.218 23.714 1.00 83.45 O
ANISOU 1334 O ALA A 169 11186 10327 10195 2017 2084 139 O
ATOM 1335 CB ALA A 169 28.201 382.355 23.801 1.00 72.30 C
ANISOU 1335 CB ALA A 169 9816 8984 8669 1893 1692 221 C
ATOM 1336 N PRO A 170 31.492 382.218 24.010 1.00 93.11 N
ANISOU 1336 N PRO A 170 12226 11596 11555 1940 2419 457 N
ATOM 1337 CA PRO A 170 32.748 381.760 23.355 1.00 95.97 C
ANISOU 1337 CA PRO A 170 12649 11944 11870 2082 2731 495 C
ATOM 1338 C PRO A 170 33.393 380.551 24.024 1.00 92.15 C
ANISOU 1338 C PRO A 170 11998 11420 11596 2048 2734 401 C
ATOM 1339 O PRO A 170 33.881 379.665 23.309 1.00 92.38 O
ANISOU 1339 O PRO A 170 12174 11427 11497 2206 2852 322 O
ATOM 1340 CB PRO A 170 33.656 382.999 23.429 1.00 89.80 C
ANISOU 1340 CB PRO A 170 11731 11168 11221 2042 3022 721 C
ATOM 1341 CG PRO A 170 32.715 384.119 23.393 1.00 84.24 C
ANISOU 1341 CG PRO A 170 11092 10486 10428 1987 2883 786 C
ATOM 1342 CD PRO A 170 31.510 383.685 24.187 1.00 86.83 C
ANISOU 1342 CD PRO A 170 11355 10820 10816 1868 2507 635 C
ATOM 1343 N PRO A 171 33.475 380.473 25.364 1.00 83.74 N
ANISOU 1343 N PRO A 171 10642 10336 10837 1866 2620 409 N
ATOM 1344 CA PRO A 171 34.088 379.276 25.980 1.00 82.54 C
ANISOU 1344 CA PRO A 171 10353 10137 10870 1853 2612 325 C
ATOM 1345 C PRO A 171 33.373 377.985 25.644 1.00 93.06 C
ANISOU 1345 C PRO A 171 11866 11430 12063 1923 2413 125 C
ATOM 1346 O PRO A 171 33.932 376.898 25.849 1.00107.08 O
ANISOU 1346 O PRO A 171 13597 13152 13936 1964 2440 47 O
ATOM 1347 CB PRO A 171 34.019 379.571 27.484 1.00 78.53 C
ANISOU 1347 CB PRO A 171 9557 9620 10659 1648 2469 371 C
ATOM 1348 CG PRO A 171 33.887 381.010 27.581 1.00 81.45 C
ANISOU 1348 CG PRO A 171 9872 10028 11047 1573 2516 510 C
ATOM 1349 CD PRO A 171 33.075 381.432 26.407 1.00 85.63 C
ANISOU 1349 CD PRO A 171 10679 10591 11266 1680 2499 495 C
ATOM 1350 N LEU A 172 32.151 378.083 25.137 1.00 88.35 N
ANISOU 1350 N LEU A 172 11463 10846 11260 1939 2201 38 N
ATOM 1351 CA LEU A 172 31.388 376.944 24.670 1.00 79.76 C
ANISOU 1351 CA LEU A 172 10565 9706 10034 2009 1988 -163 C
ATOM 1352 C LEU A 172 31.869 376.468 23.302 1.00 90.30 C
ANISOU 1352 C LEU A 172 12194 11029 11088 2247 2145 -234 C
ATOM 1353 O LEU A 172 31.595 375.327 22.926 1.00102.61 O
ANISOU 1353 O LEU A 172 13904 12521 12563 2329 2015 -414 O
ATOM 1354 CB LEU A 172 29.920 377.370 24.618 1.00 73.01 C
ANISOU 1354 CB LEU A 172 9783 8869 9090 1939 1698 -220 C
ATOM 1355 CG LEU A 172 29.081 377.107 25.874 1.00 69.88 C
ANISOU 1355 CG LEU A 172 9167 8441 8945 1736 1456 -257 C
ATOM 1356 CD1 LEU A 172 27.583 377.240 25.612 1.00 72.06 C
ANISOU 1356 CD1 LEU A 172 9532 8714 9134 1702 1161 -355 C
ATOM 1357 CD2 LEU A 172 29.441 375.831 26.598 1.00 76.92 C
ANISOU 1357 CD2 LEU A 172 9946 9249 10033 1686 1424 -338 C
ATOM 1358 N VAL A 173 32.556 377.324 22.533 1.00 94.12 N
ANISOU 1358 N VAL A 173 12777 11566 11417 2367 2426 -97 N
ATOM 1359 CA VAL A 173 32.846 377.027 21.134 1.00 95.97 C
ANISOU 1359 CA VAL A 173 13350 11799 11316 2617 2580 -154 C
ATOM 1360 C VAL A 173 34.342 377.201 20.846 1.00 93.93 C
ANISOU 1360 C VAL A 173 13032 11550 11105 2726 3012 -10 C
ATOM 1361 O VAL A 173 34.768 377.207 19.683 1.00 96.06 O
ANISOU 1361 O VAL A 173 13572 11830 11095 2946 3240 2 O
ATOM 1362 CB VAL A 173 31.999 377.946 20.216 1.00 96.71 C
ANISOU 1362 CB VAL A 173 13710 11942 11092 2701 2497 -126 C
ATOM 1363 CG1 VAL A 173 32.031 377.506 18.756 1.00110.38 C
ANISOU 1363 CG1 VAL A 173 15861 13663 12416 2977 2566 -230 C
ATOM 1364 CG2 VAL A 173 30.569 377.997 20.674 1.00 95.89 C
ANISOU 1364 CG2 VAL A 173 13571 11833 11029 2561 2088 -230 C
ATOM 1365 N GLY A 174 35.177 377.281 21.879 1.00 84.29 N
ANISOU 1365 N GLY A 174 11465 10322 10241 2589 3132 95 N
ATOM 1366 CA GLY A 174 36.607 377.180 21.646 1.00 87.06 C
ANISOU 1366 CA GLY A 174 11722 10663 10694 2696 3513 197 C
ATOM 1367 C GLY A 174 37.438 378.403 21.991 1.00 99.27 C
ANISOU 1367 C GLY A 174 13021 12242 12455 2606 3775 436 C
ATOM 1368 O GLY A 174 38.655 378.374 21.763 1.00103.73 O
ANISOU 1368 O GLY A 174 13480 12793 13141 2693 4112 534 O
ATOM 1369 N TRP A 175 36.872 379.494 22.505 1.00 99.39 N
ANISOU 1369 N TRP A 175 12932 12288 12543 2441 3648 535 N
ATOM 1370 CA TRP A 175 37.655 380.618 23.010 1.00 90.97 C
ANISOU 1370 CA TRP A 175 11595 11227 11744 2323 3850 744 C
ATOM 1371 C TRP A 175 37.491 380.638 24.523 1.00 80.86 C
ANISOU 1371 C TRP A 175 9998 9930 10795 2094 3596 724 C
ATOM 1372 O TRP A 175 36.433 381.014 25.037 1.00 83.73 O
ANISOU 1372 O TRP A 175 10374 10312 11129 1971 3320 686 O
ATOM 1373 CB TRP A 175 37.206 381.928 22.370 1.00 98.75 C
ANISOU 1373 CB TRP A 175 12737 12244 12541 2334 3928 883 C
ATOM 1374 CG TRP A 175 38.216 383.026 22.476 1.00103.46 C
ANISOU 1374 CG TRP A 175 13121 12821 13369 2274 4238 1111 C
ATOM 1375 CD1 TRP A 175 39.557 382.892 22.682 1.00101.41 C
ANISOU 1375 CD1 TRP A 175 12610 12524 13397 2277 4520 1201 C
ATOM 1376 CD2 TRP A 175 37.961 384.432 22.387 1.00113.47 C
ANISOU 1376 CD2 TRP A 175 14393 14088 14633 2198 4290 1276 C
ATOM 1377 NE1 TRP A 175 40.154 384.126 22.726 1.00110.66 N
ANISOU 1377 NE1 TRP A 175 13619 13668 14760 2196 4742 1412 N
ATOM 1378 CE2 TRP A 175 39.196 385.090 22.546 1.00115.36 C
ANISOU 1378 CE2 TRP A 175 14377 14280 15174 2146 4610 1463 C
ATOM 1379 CE3 TRP A 175 36.808 385.198 22.181 1.00110.80 C
ANISOU 1379 CE3 TRP A 175 14242 13773 14082 2172 4093 1285 C
ATOM 1380 CZ2 TRP A 175 39.314 386.477 22.505 1.00111.60 C
ANISOU 1380 CZ2 TRP A 175 13839 13769 14792 2061 4742 1658 C
ATOM 1381 CZ3 TRP A 175 36.926 386.573 22.140 1.00110.44 C
ANISOU 1381 CZ3 TRP A 175 14147 13702 14113 2102 4225 1479 C
ATOM 1382 CH2 TRP A 175 38.169 387.200 22.302 1.00113.27 C
ANISOU 1382 CH2 TRP A 175 14261 14004 14773 2043 4548 1663 C
ATOM 1383 N SER A 176 38.569 380.279 25.217 1.00 78.23 N
ANISOU 1383 N SER A 176 9386 9562 10776 2051 3703 758 N
ATOM 1384 CA SER A 176 38.574 379.891 26.621 1.00 79.51 C
ANISOU 1384 CA SER A 176 9289 9698 11225 1889 3464 704 C
ATOM 1385 C SER A 176 37.771 378.605 26.799 1.00 81.82 C
ANISOU 1385 C SER A 176 9719 9972 11397 1915 3206 510 C
ATOM 1386 O SER A 176 37.600 377.830 25.847 1.00 84.41 O
ANISOU 1386 O SER A 176 10291 10292 11490 2078 3254 407 O
ATOM 1387 CB SER A 176 38.046 380.994 27.537 1.00 81.55 C
ANISOU 1387 CB SER A 176 9404 9969 11611 1692 3288 779 C
ATOM 1388 OG SER A 176 38.549 380.794 28.850 1.00 88.82 O
ANISOU 1388 OG SER A 176 10040 10856 12850 1565 3165 777 O
ATOM 1389 N ARG A 177 37.266 378.374 28.006 1.00 70.43 N
ANISOU 1389 N ARG A 177 8136 8513 10112 1761 2934 460 N
ATOM 1390 CA ARG A 177 36.612 377.111 28.300 1.00 78.54 C
ANISOU 1390 CA ARG A 177 9250 9498 11092 1768 2710 297 C
ATOM 1391 C ARG A 177 36.069 377.189 29.717 1.00 80.78 C
ANISOU 1391 C ARG A 177 9364 9771 11559 1582 2458 297 C
ATOM 1392 O ARG A 177 36.532 377.996 30.528 1.00 77.17 O
ANISOU 1392 O ARG A 177 8699 9327 11297 1476 2473 406 O
ATOM 1393 CB ARG A 177 37.565 375.921 28.179 1.00 78.45 C
ANISOU 1393 CB ARG A 177 9206 9429 11172 1892 2828 235 C
ATOM 1394 CG ARG A 177 38.673 375.968 29.172 1.00 73.03 C
ANISOU 1394 CG ARG A 177 8212 8718 10818 1829 2888 323 C
ATOM 1395 CD ARG A 177 39.533 374.754 29.065 1.00 91.62 C
ANISOU 1395 CD ARG A 177 10535 11010 13269 1962 2983 256 C
ATOM 1396 NE ARG A 177 40.592 374.838 30.056 1.00 98.92 N
ANISOU 1396 NE ARG A 177 11146 11909 14531 1905 3007 342 N
ATOM 1397 CZ ARG A 177 41.402 373.844 30.373 1.00 86.78 C
ANISOU 1397 CZ ARG A 177 9499 10307 13166 1988 3031 302 C
ATOM 1398 NH1 ARG A 177 41.267 372.676 29.775 1.00 96.28 N
ANISOU 1398 NH1 ARG A 177 10890 11458 14233 2128 3047 176 N
ATOM 1399 NH2 ARG A 177 42.320 374.027 31.306 1.00 80.38 N
ANISOU 1399 NH2 ARG A 177 8398 9476 12668 1933 3015 381 N
ATOM 1400 N TYR A 178 35.104 376.328 30.014 1.00 78.98 N
ANISOU 1400 N TYR A 178 9230 9507 11273 1547 2230 172 N
ATOM 1401 CA TYR A 178 34.629 376.196 31.381 1.00 80.42 C
ANISOU 1401 CA TYR A 178 9270 9665 11620 1394 2021 174 C
ATOM 1402 C TYR A 178 35.318 375.011 32.035 1.00 77.72 C
ANISOU 1402 C TYR A 178 8834 9247 11449 1420 2000 132 C
ATOM 1403 O TYR A 178 35.474 373.952 31.423 1.00 93.95 O
ANISOU 1403 O TYR A 178 11006 11247 13442 1535 2031 34 O
ATOM 1404 CB TYR A 178 33.111 376.004 31.441 1.00 82.88 C
ANISOU 1404 CB TYR A 178 9707 9971 11813 1323 1795 86 C
ATOM 1405 CG TYR A 178 32.344 377.230 31.055 1.00 78.54 C
ANISOU 1405 CG TYR A 178 9216 9492 11134 1283 1771 135 C
ATOM 1406 CD1 TYR A 178 32.278 378.319 31.903 1.00 77.35 C
ANISOU 1406 CD1 TYR A 178 8920 9380 11091 1165 1750 243 C
ATOM 1407 CD2 TYR A 178 31.699 377.307 29.831 1.00 86.80 C
ANISOU 1407 CD2 TYR A 178 10479 10560 11943 1376 1758 70 C
ATOM 1408 CE1 TYR A 178 31.582 379.459 31.545 1.00 78.05 C
ANISOU 1408 CE1 TYR A 178 9064 9522 11069 1137 1730 290 C
ATOM 1409 CE2 TYR A 178 31.001 378.433 29.467 1.00 88.33 C
ANISOU 1409 CE2 TYR A 178 10732 10812 12017 1353 1726 121 C
ATOM 1410 CZ TYR A 178 30.944 379.505 30.330 1.00 78.12 C
ANISOU 1410 CZ TYR A 178 9280 9552 10850 1232 1719 235 C
ATOM 1411 OH TYR A 178 30.239 380.621 29.975 1.00 70.44 O
ANISOU 1411 OH TYR A 178 8369 8627 9769 1217 1685 286 O
ATOM 1412 N ILE A 179 35.755 375.212 33.274 1.00 60.77 N
ANISOU 1412 N ILE A 179 6490 7089 9511 1326 1939 205 N
ATOM 1413 CA ILE A 179 36.382 374.158 34.070 1.00 64.42 C
ANISOU 1413 CA ILE A 179 6857 7475 10144 1347 1885 183 C
ATOM 1414 C ILE A 179 35.951 374.372 35.508 1.00 65.93 C
ANISOU 1414 C ILE A 179 6950 7657 10445 1209 1699 229 C
ATOM 1415 O ILE A 179 35.591 375.490 35.899 1.00 72.09 O
ANISOU 1415 O ILE A 179 7680 8495 11218 1113 1662 294 O
ATOM 1416 CB ILE A 179 37.929 374.170 33.978 1.00 68.04 C
ANISOU 1416 CB ILE A 179 7150 7925 10777 1440 2066 244 C
ATOM 1417 CG1 ILE A 179 38.514 375.517 34.379 1.00 78.27 C
ANISOU 1417 CG1 ILE A 179 8259 9276 12205 1363 2125 367 C
ATOM 1418 CG2 ILE A 179 38.416 373.912 32.559 1.00 58.95 C
ANISOU 1418 CG2 ILE A 179 6109 6781 9510 1601 2294 207 C
ATOM 1419 CD1 ILE A 179 40.011 375.442 34.521 1.00 79.29 C
ANISOU 1419 CD1 ILE A 179 8171 9377 12578 1432 2258 425 C
ATOM 1420 N PRO A 180 36.013 373.332 36.333 1.00 68.11 N
ANISOU 1420 N PRO A 180 7209 7854 10818 1209 1588 202 N
ATOM 1421 CA PRO A 180 35.869 373.554 37.773 1.00 73.04 C
ANISOU 1421 CA PRO A 180 7743 8467 11544 1109 1441 265 C
ATOM 1422 C PRO A 180 36.861 374.606 38.252 1.00 74.15 C
ANISOU 1422 C PRO A 180 7701 8653 11819 1089 1477 355 C
ATOM 1423 O PRO A 180 37.953 374.760 37.701 1.00 91.54 O
ANISOU 1423 O PRO A 180 9799 10863 14119 1166 1615 376 O
ATOM 1424 CB PRO A 180 36.148 372.172 38.377 1.00 68.40 C
ANISOU 1424 CB PRO A 180 7170 7772 11048 1160 1365 235 C
ATOM 1425 CG PRO A 180 35.709 371.220 37.320 1.00 61.47 C
ANISOU 1425 CG PRO A 180 6444 6841 10071 1229 1410 129 C
ATOM 1426 CD PRO A 180 36.079 371.893 36.005 1.00 65.03 C
ANISOU 1426 CD PRO A 180 6915 7368 10426 1302 1581 110 C
ATOM 1427 N GLU A 181 36.470 375.334 39.291 1.00 57.22 N
ANISOU 1427 N GLU A 181 5518 6531 9692 988 1353 405 N
ATOM 1428 CA GLU A 181 37.297 376.407 39.805 1.00 60.44 C
ANISOU 1428 CA GLU A 181 5764 6968 10234 954 1347 474 C
ATOM 1429 C GLU A 181 37.251 376.323 41.317 1.00 62.91 C
ANISOU 1429 C GLU A 181 6055 7245 10604 909 1155 498 C
ATOM 1430 O GLU A 181 36.378 375.673 41.893 1.00 79.79 O
ANISOU 1430 O GLU A 181 8315 9354 12648 886 1063 481 O
ATOM 1431 CB GLU A 181 36.822 377.813 39.392 1.00 52.66 C
ANISOU 1431 CB GLU A 181 4782 6051 9174 878 1400 510 C
ATOM 1432 CG GLU A 181 35.502 378.229 40.017 1.00 74.12 C
ANISOU 1432 CG GLU A 181 7609 8793 11762 786 1278 504 C
ATOM 1433 CD GLU A 181 34.815 379.367 39.286 1.00 96.53 C
ANISOU 1433 CD GLU A 181 10496 11692 14489 741 1345 522 C
ATOM 1434 OE1 GLU A 181 35.512 380.123 38.572 1.00116.18 O
ANISOU 1434 OE1 GLU A 181 12915 14201 17027 759 1473 564 O
ATOM 1435 OE2 GLU A 181 33.585 379.529 39.461 1.00 89.97 O
ANISOU 1435 OE2 GLU A 181 9767 10882 13536 689 1275 503 O
ATOM 1436 N GLY A 182 38.240 376.940 41.949 1.00 67.93 N
ANISOU 1436 N GLY A 182 6534 7874 11403 905 1096 538 N
ATOM 1437 CA GLY A 182 38.276 376.963 43.395 1.00 56.65 C
ANISOU 1437 CA GLY A 182 5107 6412 10007 882 895 555 C
ATOM 1438 C GLY A 182 38.382 375.547 43.910 1.00 58.32 C
ANISOU 1438 C GLY A 182 5383 6553 10223 959 821 542 C
ATOM 1439 O GLY A 182 39.267 374.765 43.539 1.00 71.94 O
ANISOU 1439 O GLY A 182 7028 8235 12071 1050 866 530 O
ATOM 1440 N MET A 183 37.448 375.217 44.773 1.00 62.38 N
ANISOU 1440 N MET A 183 6049 7047 10607 926 721 552 N
ATOM 1441 CA MET A 183 37.341 373.911 45.387 1.00 67.92 C
ANISOU 1441 CA MET A 183 6850 7666 11292 986 652 560 C
ATOM 1442 C MET A 183 36.715 372.898 44.434 1.00 63.62 C
ANISOU 1442 C MET A 183 6396 7088 10690 1001 771 517 C
ATOM 1443 O MET A 183 36.366 371.797 44.864 1.00 61.84 O
ANISOU 1443 O MET A 183 6275 6778 10443 1029 730 525 O
ATOM 1444 CB MET A 183 36.532 374.059 46.670 1.00 71.57 C
ANISOU 1444 CB MET A 183 7447 8115 11630 943 533 603 C
ATOM 1445 CG MET A 183 37.285 374.906 47.673 1.00 64.14 C
ANISOU 1445 CG MET A 183 6442 7186 10743 957 376 625 C
ATOM 1446 SD MET A 183 36.436 375.352 49.189 1.00 77.14 S
ANISOU 1446 SD MET A 183 8270 8829 12209 931 246 668 S
ATOM 1447 CE MET A 183 35.229 374.071 49.399 1.00 80.34 C
ANISOU 1447 CE MET A 183 8868 9174 12483 930 331 713 C
ATOM 1448 N GLN A 184 36.519 373.291 43.166 1.00 69.09 N
ANISOU 1448 N GLN A 184 7066 7836 11350 983 908 473 N
ATOM 1449 CA GLN A 184 36.185 372.412 42.049 1.00 79.19 C
ANISOU 1449 CA GLN A 184 8421 9082 12585 1023 1011 407 C
ATOM 1450 C GLN A 184 34.721 371.999 42.093 1.00 78.36 C
ANISOU 1450 C GLN A 184 8466 8949 12357 948 982 384 C
ATOM 1451 O GLN A 184 34.320 371.044 41.432 1.00 84.83 O
ANISOU 1451 O GLN A 184 9372 9706 13156 974 1012 320 O
ATOM 1452 CB GLN A 184 37.097 371.176 41.974 1.00 82.45 C
ANISOU 1452 CB GLN A 184 8813 9402 13112 1143 1019 384 C
ATOM 1453 CG GLN A 184 38.606 371.470 41.936 1.00 67.26 C
ANISOU 1453 CG GLN A 184 6704 7493 11361 1229 1052 407 C
ATOM 1454 CD GLN A 184 39.056 372.231 40.685 1.00 73.17 C
ANISOU 1454 CD GLN A 184 7366 8316 12120 1249 1232 388 C
ATOM 1455 OE1 GLN A 184 39.064 371.711 39.557 1.00 59.61 O
ANISOU 1455 OE1 GLN A 184 5710 6588 10351 1321 1371 330 O
ATOM 1456 NE2 GLN A 184 39.439 373.479 40.889 1.00 83.75 N
ANISOU 1456 NE2 GLN A 184 8577 9722 13521 1191 1234 440 N
ATOM 1457 N CYS A 185 33.906 372.723 42.849 1.00 78.67 N
ANISOU 1457 N CYS A 185 8532 9028 12331 856 923 430 N
ATOM 1458 CA CYS A 185 32.484 372.459 42.964 1.00 71.08 C
ANISOU 1458 CA CYS A 185 7675 8043 11289 777 907 421 C
ATOM 1459 C CYS A 185 31.641 373.365 42.088 1.00 83.88 C
ANISOU 1459 C CYS A 185 9301 9748 12820 717 953 383 C
ATOM 1460 O CYS A 185 30.428 373.146 41.991 1.00 97.37 O
ANISOU 1460 O CYS A 185 11071 11438 14489 653 936 362 O
ATOM 1461 CB CYS A 185 32.052 372.647 44.415 1.00 69.83 C
ANISOU 1461 CB CYS A 185 7553 7870 11110 731 833 504 C
ATOM 1462 SG CYS A 185 32.717 371.384 45.463 1.00 78.62 S
ANISOU 1462 SG CYS A 185 8718 8860 12295 808 764 558 S
ATOM 1463 N SER A 186 32.239 374.380 41.466 1.00 76.25 N
ANISOU 1463 N SER A 186 8266 8866 11838 736 1008 382 N
ATOM 1464 CA SER A 186 31.517 375.199 40.512 1.00 72.98 C
ANISOU 1464 CA SER A 186 7878 8524 11327 702 1053 351 C
ATOM 1465 C SER A 186 32.430 375.467 39.332 1.00 70.84 C
ANISOU 1465 C SER A 186 7580 8289 11047 781 1163 326 C
ATOM 1466 O SER A 186 33.649 375.310 39.414 1.00 72.58 O
ANISOU 1466 O SER A 186 7718 8495 11365 844 1211 348 O
ATOM 1467 CB SER A 186 31.041 376.551 41.088 1.00 84.83 C
ANISOU 1467 CB SER A 186 9345 10095 12791 630 1028 406 C
ATOM 1468 OG SER A 186 31.891 377.067 42.097 1.00 99.94 O
ANISOU 1468 OG SER A 186 11184 12012 14775 631 991 466 O
ATOM 1469 N CYS A 187 31.808 375.818 38.211 1.00 68.08 N
ANISOU 1469 N CYS A 187 7304 7981 10581 789 1207 281 N
ATOM 1470 CA CYS A 187 32.484 375.933 36.932 1.00 65.99 C
ANISOU 1470 CA CYS A 187 7069 7744 10261 883 1336 255 C
ATOM 1471 C CYS A 187 32.428 377.385 36.472 1.00 71.86 C
ANISOU 1471 C CYS A 187 7793 8570 10939 861 1403 312 C
ATOM 1472 O CYS A 187 31.452 378.096 36.741 1.00 73.80 O
ANISOU 1472 O CYS A 187 8059 8850 11130 786 1328 327 O
ATOM 1473 CB CYS A 187 31.869 375.004 35.897 1.00 71.49 C
ANISOU 1473 CB CYS A 187 7914 8401 10846 943 1323 145 C
ATOM 1474 SG CYS A 187 32.294 373.253 36.132 1.00 80.03 S
ANISOU 1474 SG CYS A 187 9026 9359 12022 1004 1291 73 S
ATOM 1475 N GLY A 188 33.474 377.816 35.766 1.00 60.71 N
ANISOU 1475 N GLY A 188 6341 7183 9545 932 1558 351 N
ATOM 1476 CA GLY A 188 33.507 379.175 35.268 1.00 62.56 C
ANISOU 1476 CA GLY A 188 6565 7476 9730 916 1646 421 C
ATOM 1477 C GLY A 188 34.547 379.354 34.187 1.00 74.76 C
ANISOU 1477 C GLY A 188 8109 9032 11266 1020 1860 458 C
ATOM 1478 O GLY A 188 35.170 378.397 33.730 1.00 66.09 O
ANISOU 1478 O GLY A 188 7032 7903 10177 1118 1943 413 O
ATOM 1479 N ILE A 189 34.685 380.603 33.730 1.00 91.41 N
ANISOU 1479 N ILE A 189 10205 11178 13349 1006 1967 544 N
ATOM 1480 CA ILE A 189 35.692 380.897 32.721 1.00 87.96 C
ANISOU 1480 CA ILE A 189 9759 10745 12915 1102 2212 608 C
ATOM 1481 C ILE A 189 37.051 380.511 33.274 1.00 89.49 C
ANISOU 1481 C ILE A 189 9743 10896 13362 1113 2290 641 C
ATOM 1482 O ILE A 189 37.314 380.687 34.474 1.00 82.63 O
ANISOU 1482 O ILE A 189 8713 10002 12680 1019 2158 659 O
ATOM 1483 CB ILE A 189 35.677 382.392 32.368 1.00 91.55 C
ANISOU 1483 CB ILE A 189 10206 11225 13356 1061 2311 722 C
ATOM 1484 CG1 ILE A 189 34.258 382.869 32.045 1.00100.64 C
ANISOU 1484 CG1 ILE A 189 11536 12414 14287 1041 2184 692 C
ATOM 1485 CG2 ILE A 189 36.629 382.671 31.215 1.00 81.42 C
ANISOU 1485 CG2 ILE A 189 8942 9940 12055 1170 2604 806 C
ATOM 1486 CD1 ILE A 189 33.863 382.686 30.619 1.00103.19 C
ANISOU 1486 CD1 ILE A 189 12092 12766 14350 1173 2278 665 C
ATOM 1487 N ASP A 190 37.884 379.890 32.429 1.00 92.54 N
ANISOU 1487 N ASP A 190 10144 11269 13749 1243 2488 637 N
ATOM 1488 CA ASP A 190 39.247 379.505 32.798 1.00 84.54 C
ANISOU 1488 CA ASP A 190 8913 10212 12997 1278 2587 671 C
ATOM 1489 C ASP A 190 40.180 380.702 32.611 1.00 85.10 C
ANISOU 1489 C ASP A 190 8804 10278 13253 1245 2779 809 C
ATOM 1490 O ASP A 190 40.657 380.945 31.506 1.00 93.75 O
ANISOU 1490 O ASP A 190 9944 11382 14294 1340 3048 872 O
ATOM 1491 CB ASP A 190 39.714 378.337 31.933 1.00 90.50 C
ANISOU 1491 CB ASP A 190 9758 10947 13679 1445 2740 607 C
ATOM 1492 CG ASP A 190 41.132 377.884 32.265 1.00 85.77 C
ANISOU 1492 CG ASP A 190 8919 10300 13368 1501 2852 640 C
ATOM 1493 OD1 ASP A 190 41.682 378.336 33.286 1.00 76.37 O
ANISOU 1493 OD1 ASP A 190 7495 9086 12434 1402 2753 695 O
ATOM 1494 OD2 ASP A 190 41.734 377.144 31.461 1.00 96.26 O
ANISOU 1494 OD2 ASP A 190 10291 11612 14673 1654 3045 613 O
ATOM 1495 N TYR A 191 40.407 381.515 33.642 1.00 86.91 N
ANISOU 1495 N TYR A 191 8845 10484 13691 1111 2651 861 N
ATOM 1496 CA TYR A 191 41.515 382.471 33.637 1.00 97.57 C
ANISOU 1496 CA TYR A 191 9961 11796 15314 1069 2808 980 C
ATOM 1497 C TYR A 191 42.751 381.955 34.391 1.00103.69 C
ANISOU 1497 C TYR A 191 10459 12515 16424 1076 2772 976 C
ATOM 1498 O TYR A 191 43.657 382.736 34.670 1.00112.69 O
ANISOU 1498 O TYR A 191 11355 13605 17856 1012 2826 1059 O
ATOM 1499 CB TYR A 191 41.113 383.870 34.107 1.00104.55 C
ANISOU 1499 CB TYR A 191 10808 12669 16246 927 2714 1044 C
ATOM 1500 CG TYR A 191 40.209 383.933 35.276 1.00103.35 C
ANISOU 1500 CG TYR A 191 10706 12526 16037 829 2401 968 C
ATOM 1501 CD1 TYR A 191 40.697 384.346 36.493 1.00112.63 C
ANISOU 1501 CD1 TYR A 191 11690 13651 17454 732 2221 968 C
ATOM 1502 CD2 TYR A 191 38.852 383.692 35.153 1.00106.57 C
ANISOU 1502 CD2 TYR A 191 11351 12987 16154 834 2290 902 C
ATOM 1503 CE1 TYR A 191 39.897 384.422 37.579 1.00122.91 C
ANISOU 1503 CE1 TYR A 191 13059 14959 18683 660 1960 904 C
ATOM 1504 CE2 TYR A 191 38.022 383.775 36.249 1.00122.17 C
ANISOU 1504 CE2 TYR A 191 13362 14967 18091 749 2039 846 C
ATOM 1505 CZ TYR A 191 38.557 384.149 37.468 1.00131.30 C
ANISOU 1505 CZ TYR A 191 14349 16076 19463 668 1886 851 C
ATOM 1506 OH TYR A 191 37.768 384.251 38.592 1.00138.74 O
ANISOU 1506 OH TYR A 191 15347 17021 20347 601 1657 800 O
ATOM 1507 N TYR A 192 42.832 380.653 34.672 1.00118.18 N
ANISOU 1507 N TYR A 192 12321 14345 18239 1158 2684 885 N
ATOM 1508 CA TYR A 192 43.710 380.048 35.683 1.00125.89 C
ANISOU 1508 CA TYR A 192 13076 15267 19490 1162 2538 857 C
ATOM 1509 C TYR A 192 44.785 379.202 35.055 1.00122.66 C
ANISOU 1509 C TYR A 192 12551 14830 19225 1309 2751 862 C
ATOM 1510 O TYR A 192 45.811 378.951 35.703 1.00131.38 O
ANISOU 1510 O TYR A 192 13402 15882 20636 1322 2691 872 O
ATOM 1511 CB TYR A 192 42.990 379.137 36.692 1.00125.76 C
ANISOU 1511 CB TYR A 192 13176 15245 19361 1149 2245 756 C
ATOM 1512 CG TYR A 192 41.736 379.660 37.277 1.00119.67 C
ANISOU 1512 CG TYR A 192 12567 14506 18397 1036 2050 732 C
ATOM 1513 CD1 TYR A 192 41.764 380.597 38.306 1.00126.31 C
ANISOU 1513 CD1 TYR A 192 13301 15330 19362 919 1873 760 C
ATOM 1514 CD2 TYR A 192 40.533 379.118 36.909 1.00114.68 C
ANISOU 1514 CD2 TYR A 192 12186 13910 17478 1055 2018 669 C
ATOM 1515 CE1 TYR A 192 40.595 381.049 38.871 1.00131.37 C
ANISOU 1515 CE1 TYR A 192 14095 15998 19821 833 1711 735 C
ATOM 1516 CE2 TYR A 192 39.371 379.550 37.461 1.00128.77 C
ANISOU 1516 CE2 TYR A 192 14096 15720 19112 960 1853 649 C
ATOM 1517 CZ TYR A 192 39.399 380.519 38.448 1.00132.22 C
ANISOU 1517 CZ TYR A 192 14433 16148 19656 853 1712 686 C
ATOM 1518 OH TYR A 192 38.225 380.971 39.006 1.00128.62 O
ANISOU 1518 OH TYR A 192 14105 15717 19048 772 1569 668 O
ATOM 1519 N THR A 193 44.642 378.901 33.803 1.00108.59 N
ANISOU 1519 N THR A 193 10933 13078 17249 1424 3006 864 N
ATOM 1520 CA THR A 193 45.560 378.059 33.120 1.00 95.62 C
ANISOU 1520 CA THR A 193 9223 11410 15697 1587 3236 860 C
ATOM 1521 C THR A 193 45.906 378.848 31.893 1.00105.99 C
ANISOU 1521 C THR A 193 10553 12745 16973 1637 3595 968 C
ATOM 1522 O THR A 193 45.058 379.572 31.362 1.00114.79 O
ANISOU 1522 O THR A 193 11871 13904 17839 1593 3632 997 O
ATOM 1523 CB THR A 193 44.821 376.772 32.657 1.00 81.66 C
ANISOU 1523 CB THR A 193 7745 9652 13630 1710 3200 732 C
ATOM 1524 OG1 THR A 193 44.125 376.160 33.746 1.00 84.08 O
ANISOU 1524 OG1 THR A 193 8112 9939 13896 1639 2866 645 O
ATOM 1525 CG2 THR A 193 45.714 375.747 31.951 1.00104.22 C
ANISOU 1525 CG2 THR A 193 10574 12473 16552 1907 3429 701 C
ATOM 1526 N PRO A 194 47.123 378.730 31.410 1.00100.24 N
ANISOU 1526 N PRO A 194 9619 11983 16484 1738 3874 1037 N
ATOM 1527 CA PRO A 194 47.513 379.465 30.209 1.00 95.57 C
ANISOU 1527 CA PRO A 194 9050 11404 15859 1800 4268 1163 C
ATOM 1528 C PRO A 194 47.284 378.616 28.978 1.00111.07 C
ANISOU 1528 C PRO A 194 11311 13399 17493 2011 4503 1108 C
ATOM 1529 O PRO A 194 48.191 378.394 28.168 1.00136.44 O
ANISOU 1529 O PRO A 194 14510 16594 20737 2123 4776 1157 O
ATOM 1530 CB PRO A 194 48.988 379.765 30.484 1.00 96.88 C
ANISOU 1530 CB PRO A 194 8901 11501 16409 1737 4313 1246 C
ATOM 1531 CG PRO A 194 49.439 378.470 31.151 1.00104.79 C
ANISOU 1531 CG PRO A 194 9792 12476 17549 1821 4145 1132 C
ATOM 1532 CD PRO A 194 48.270 378.007 32.001 1.00 99.69 C
ANISOU 1532 CD PRO A 194 9255 11853 16768 1798 3850 1021 C
ATOM 1533 N HIS A 195 46.064 378.102 28.863 1.00111.54 N
ANISOU 1533 N HIS A 195 11700 13497 17183 2026 4299 982 N
ATOM 1534 CA HIS A 195 45.697 377.171 27.813 1.00115.45 C
ANISOU 1534 CA HIS A 195 12513 14009 17343 2222 4428 883 C
ATOM 1535 C HIS A 195 45.968 377.825 26.471 1.00120.69 C
ANISOU 1535 C HIS A 195 13316 14699 17840 2342 4826 997 C
ATOM 1536 O HIS A 195 45.645 378.998 26.261 1.00132.68 O
ANISOU 1536 O HIS A 195 14866 16244 19301 2248 4881 1111 O
ATOM 1537 CB HIS A 195 44.238 376.754 27.953 1.00122.06 C
ANISOU 1537 CB HIS A 195 13653 14873 17850 2176 4110 742 C
ATOM 1538 CG HIS A 195 43.938 375.386 27.427 1.00132.02 C
ANISOU 1538 CG HIS A 195 15158 16110 18893 2343 4084 581 C
ATOM 1539 ND1 HIS A 195 43.194 375.171 26.288 1.00140.22 N
ANISOU 1539 ND1 HIS A 195 16561 17174 19542 2469 4150 504 N
ATOM 1540 CD2 HIS A 195 44.265 374.160 27.901 1.00129.41 C
ANISOU 1540 CD2 HIS A 195 14769 15718 18683 2407 3978 475 C
ATOM 1541 CE1 HIS A 195 43.083 373.871 26.076 1.00137.05 C
ANISOU 1541 CE1 HIS A 195 16312 16723 19039 2598 4084 348 C
ATOM 1542 NE2 HIS A 195 43.724 373.235 27.040 1.00130.18 N
ANISOU 1542 NE2 HIS A 195 15188 15797 18477 2562 3990 333 N
ATOM 1543 N GLU A 196 46.631 377.102 25.589 1.00124.44 N
ANISOU 1543 N GLU A 196 13867 15160 18255 2559 5125 980 N
ATOM 1544 CA GLU A 196 47.007 377.691 24.317 1.00128.20 C
ANISOU 1544 CA GLU A 196 14505 15655 18552 2666 5489 1101 C
ATOM 1545 C GLU A 196 46.074 377.256 23.205 1.00130.99 C
ANISOU 1545 C GLU A 196 15320 16048 18403 2867 5572 999 C
ATOM 1546 O GLU A 196 45.900 377.989 22.227 1.00137.07 O
ANISOU 1546 O GLU A 196 16310 16848 18920 2933 5791 1099 O
ATOM 1547 CB GLU A 196 48.466 377.347 23.987 1.00122.92 C
ANISOU 1547 CB GLU A 196 13663 14939 18102 2725 5699 1163 C
ATOM 1548 CG GLU A 196 49.450 378.089 24.895 1.00123.35 C
ANISOU 1548 CG GLU A 196 13289 14945 18632 2517 5630 1289 C
ATOM 1549 CD GLU A 196 50.907 377.748 24.626 1.00151.72 C
ANISOU 1549 CD GLU A 196 16681 18484 22482 2575 5828 1348 C
ATOM 1550 OE1 GLU A 196 51.212 377.173 23.556 1.00155.17 O
ANISOU 1550 OE1 GLU A 196 17324 18927 22707 2770 6089 1335 O
ATOM 1551 OE2 GLU A 196 51.751 378.052 25.497 1.00164.02 O
ANISOU 1551 OE2 GLU A 196 17877 19990 24453 2431 5713 1402 O
ATOM 1552 N GLU A 197 45.510 376.054 23.330 1.00129.37 N
ANISOU 1552 N GLU A 197 15294 15828 18035 2935 5324 795 N
ATOM 1553 CA GLU A 197 44.652 375.488 22.296 1.00129.81 C
ANISOU 1553 CA GLU A 197 15807 15900 17614 3106 5298 655 C
ATOM 1554 C GLU A 197 43.361 376.279 22.128 1.00120.29 C
ANISOU 1554 C GLU A 197 14837 14747 16120 2999 5071 652 C
ATOM 1555 O GLU A 197 42.787 376.292 21.033 1.00117.13 O
ANISOU 1555 O GLU A 197 14814 14372 15316 3151 5137 606 O
ATOM 1556 CB GLU A 197 44.349 374.035 22.640 1.00134.41 C
ANISOU 1556 CB GLU A 197 16473 16428 18168 3163 5042 435 C
ATOM 1557 CG GLU A 197 45.596 373.191 22.810 1.00142.05 C
ANISOU 1557 CG GLU A 197 17218 17336 19420 3289 5246 428 C
ATOM 1558 CD GLU A 197 45.274 371.797 23.271 1.00157.03 C
ANISOU 1558 CD GLU A 197 19185 19161 21321 3325 4967 224 C
ATOM 1559 OE1 GLU A 197 44.615 371.063 22.505 1.00164.12 O
ANISOU 1559 OE1 GLU A 197 20449 20034 21876 3467 4903 59 O
ATOM 1560 OE2 GLU A 197 45.661 371.443 24.405 1.00162.61 O
ANISOU 1560 OE2 GLU A 197 19591 19825 22370 3212 4797 227 O
ATOM 1561 N THR A 198 42.874 376.907 23.205 1.00120.10 N
ANISOU 1561 N THR A 198 14607 14736 16289 2753 4790 691 N
ATOM 1562 CA THR A 198 41.672 377.741 23.185 1.00118.41 C
ANISOU 1562 CA THR A 198 14561 14568 15863 2637 4569 700 C
ATOM 1563 C THR A 198 41.974 379.235 23.345 1.00118.35 C
ANISOU 1563 C THR A 198 14376 14581 16012 2509 4717 915 C
ATOM 1564 O THR A 198 41.068 380.014 23.667 1.00108.28 O
ANISOU 1564 O THR A 198 13144 13333 14667 2371 4500 936 O
ATOM 1565 CB THR A 198 40.660 377.280 24.236 1.00101.06 C
ANISOU 1565 CB THR A 198 12323 12361 13714 2470 4119 560 C
ATOM 1566 OG1 THR A 198 41.288 377.150 25.516 1.00 98.53 O
ANISOU 1566 OG1 THR A 198 11640 12007 13791 2326 4026 592 O
ATOM 1567 CG2 THR A 198 40.077 375.951 23.826 1.00 92.57 C
ANISOU 1567 CG2 THR A 198 11507 11253 12413 2597 3960 348 C
ATOM 1568 N ASN A 199 43.228 379.640 23.154 1.00118.50 N
ANISOU 1568 N ASN A 199 14181 14576 16269 2550 5079 1074 N
ATOM 1569 CA ASN A 199 43.652 381.036 23.230 1.00115.31 C
ANISOU 1569 CA ASN A 199 13595 14164 16056 2434 5261 1288 C
ATOM 1570 C ASN A 199 43.117 381.738 24.480 1.00111.48 C
ANISOU 1570 C ASN A 199 12900 13673 15782 2176 4916 1294 C
ATOM 1571 O ASN A 199 42.433 382.761 24.409 1.00116.14 O
ANISOU 1571 O ASN A 199 13586 14280 16263 2088 4846 1367 O
ATOM 1572 CB ASN A 199 43.214 381.778 21.968 1.00118.22 C
ANISOU 1572 CB ASN A 199 14306 14562 16051 2557 5479 1388 C
ATOM 1573 CG ASN A 199 43.981 381.353 20.752 1.00125.36 C
ANISOU 1573 CG ASN A 199 15383 15462 16786 2814 5910 1438 C
ATOM 1574 OD1 ASN A 199 45.192 381.546 20.667 1.00136.22 O
ANISOU 1574 OD1 ASN A 199 16532 16790 18437 2804 6174 1569 O
ATOM 1575 ND2 ASN A 199 43.284 380.747 19.801 1.00127.48 N
ANISOU 1575 ND2 ASN A 199 16079 15765 16593 3011 5879 1313 N
ATOM 1576 N ASN A 200 43.425 381.150 25.640 1.00100.71 N
ANISOU 1576 N ASN A 200 11270 12283 14713 2071 4697 1212 N
ATOM 1577 CA ASN A 200 42.901 381.666 26.903 1.00 97.94 C
ANISOU 1577 CA ASN A 200 10752 11927 14535 1850 4354 1194 C
ATOM 1578 C ASN A 200 43.392 383.087 27.167 1.00110.26 C
ANISOU 1578 C ASN A 200 12093 13452 16350 1711 4469 1373 C
ATOM 1579 O ASN A 200 42.636 383.928 27.672 1.00116.93 O
ANISOU 1579 O ASN A 200 12958 14302 17170 1570 4263 1389 O
ATOM 1580 CB ASN A 200 43.309 380.747 28.054 1.00 88.87 C
ANISOU 1580 CB ASN A 200 9370 10746 13650 1795 4137 1091 C
ATOM 1581 CG ASN A 200 42.423 379.529 28.160 1.00 94.21 C
ANISOU 1581 CG ASN A 200 10265 11439 14091 1852 3893 906 C
ATOM 1582 OD1 ASN A 200 41.775 379.138 27.186 1.00 97.24 O
ANISOU 1582 OD1 ASN A 200 10957 11851 14137 1978 3941 837 O
ATOM 1583 ND2 ASN A 200 42.379 378.922 29.346 1.00 90.70 N
ANISOU 1583 ND2 ASN A 200 9671 10967 13823 1762 3622 825 N
ATOM 1584 N GLU A 201 44.673 383.350 26.883 1.00108.63 N
ANISOU 1584 N GLU A 201 11655 13196 16423 1747 4792 1504 N
ATOM 1585 CA GLU A 201 45.277 384.654 27.141 1.00109.31 C
ANISOU 1585 CA GLU A 201 11491 13219 16821 1607 4914 1677 C
ATOM 1586 C GLU A 201 44.450 385.785 26.543 1.00108.55 C
ANISOU 1586 C GLU A 201 11632 13136 16476 1574 4962 1775 C
ATOM 1587 O GLU A 201 44.087 386.743 27.237 1.00112.94 O
ANISOU 1587 O GLU A 201 12097 13660 17156 1403 4774 1811 O
ATOM 1588 CB GLU A 201 46.706 384.684 26.600 1.00123.33 C
ANISOU 1588 CB GLU A 201 13104 14927 18827 1652 5206 1787 C
ATOM 1589 CG GLU A 201 47.504 385.914 27.013 1.00133.80 C
ANISOU 1589 CG GLU A 201 14167 16148 20521 1465 5206 1926 C
ATOM 1590 CD GLU A 201 48.921 385.896 26.471 1.00146.91 C
ANISOU 1590 CD GLU A 201 15680 17728 22410 1502 5454 2024 C
ATOM 1591 OE1 GLU A 201 49.306 384.886 25.842 1.00151.07 O
ANISOU 1591 OE1 GLU A 201 16300 18288 22813 1672 5616 1979 O
ATOM 1592 OE2 GLU A 201 49.646 386.898 26.664 1.00152.31 O
ANISOU 1592 OE2 GLU A 201 16158 18307 23405 1367 5491 2142 O
ATOM 1593 N SER A 202 44.148 385.694 25.245 1.00 99.03 N
ANISOU 1593 N SER A 202 10750 11970 14908 1751 5209 1817 N
ATOM 1594 CA SER A 202 43.446 386.789 24.585 1.00 90.81 C
ANISOU 1594 CA SER A 202 9945 10932 13627 1746 5279 1932 C
ATOM 1595 C SER A 202 42.007 386.920 25.070 1.00 94.70 C
ANISOU 1595 C SER A 202 10625 11474 13881 1664 4867 1805 C
ATOM 1596 O SER A 202 41.444 388.018 25.032 1.00107.10 O
ANISOU 1596 O SER A 202 12272 13027 15395 1586 4820 1893 O
ATOM 1597 CB SER A 202 43.484 386.594 23.073 1.00 98.40 C
ANISOU 1597 CB SER A 202 11238 11923 14225 1983 5631 2002 C
ATOM 1598 OG SER A 202 42.723 385.466 22.695 1.00108.63 O
ANISOU 1598 OG SER A 202 12830 13293 15151 2130 5460 1809 O
ATOM 1599 N PHE A 203 41.399 385.838 25.554 1.00 93.18 N
ANISOU 1599 N PHE A 203 10497 11333 13575 1678 4573 1606 N
ATOM 1600 CA PHE A 203 40.068 385.984 26.128 1.00 91.94 C
ANISOU 1600 CA PHE A 203 10462 11213 13258 1584 4196 1496 C
ATOM 1601 C PHE A 203 40.133 386.712 27.464 1.00 91.82 C
ANISOU 1601 C PHE A 203 10163 11153 13572 1368 3988 1518 C
ATOM 1602 O PHE A 203 39.248 387.512 27.783 1.00 89.71 O
ANISOU 1602 O PHE A 203 9965 10889 13231 1276 3806 1524 O
ATOM 1603 CB PHE A 203 39.404 384.617 26.298 1.00 88.82 C
ANISOU 1603 CB PHE A 203 10198 10866 12682 1648 3955 1289 C
ATOM 1604 CG PHE A 203 37.945 384.699 26.661 1.00 89.49 C
ANISOU 1604 CG PHE A 203 10439 10990 12574 1579 3611 1182 C
ATOM 1605 CD1 PHE A 203 36.979 384.873 25.680 1.00 91.95 C
ANISOU 1605 CD1 PHE A 203 11071 11340 12525 1685 3581 1160 C
ATOM 1606 CD2 PHE A 203 37.543 384.632 27.987 1.00 78.87 C
ANISOU 1606 CD2 PHE A 203 8917 9636 11413 1418 3320 1109 C
ATOM 1607 CE1 PHE A 203 35.643 384.960 26.014 1.00 85.55 C
ANISOU 1607 CE1 PHE A 203 10368 10560 11579 1623 3266 1065 C
ATOM 1608 CE2 PHE A 203 36.212 384.715 28.328 1.00 78.00 C
ANISOU 1608 CE2 PHE A 203 8928 9558 11152 1359 3038 1023 C
ATOM 1609 CZ PHE A 203 35.259 384.885 27.343 1.00 85.98 C
ANISOU 1609 CZ PHE A 203 10221 10606 11841 1456 3009 1000 C
ATOM 1610 N VAL A 204 41.178 386.453 28.253 1.00 96.59 N
ANISOU 1610 N VAL A 204 10452 11710 14538 1297 4005 1523 N
ATOM 1611 CA VAL A 204 41.334 387.148 29.528 1.00 95.90 C
ANISOU 1611 CA VAL A 204 10108 11570 14762 1106 3796 1532 C
ATOM 1612 C VAL A 204 41.541 388.643 29.294 1.00100.70 C
ANISOU 1612 C VAL A 204 10658 12110 15495 1021 3944 1701 C
ATOM 1613 O VAL A 204 40.976 389.482 30.006 1.00 98.57 O
ANISOU 1613 O VAL A 204 10362 11811 15277 891 3735 1697 O
ATOM 1614 CB VAL A 204 42.493 386.525 30.328 1.00 84.18 C
ANISOU 1614 CB VAL A 204 8304 10040 13639 1072 3777 1501 C
ATOM 1615 CG1 VAL A 204 42.805 387.354 31.556 1.00 74.06 C
ANISOU 1615 CG1 VAL A 204 6762 8688 12689 890 3575 1519 C
ATOM 1616 CG2 VAL A 204 42.152 385.105 30.728 1.00 84.26 C
ANISOU 1616 CG2 VAL A 204 8386 10101 13528 1140 3582 1335 C
ATOM 1617 N ILE A 205 42.401 388.995 28.331 1.00100.15 N
ANISOU 1617 N ILE A 205 10556 11999 15499 1094 4320 1856 N
ATOM 1618 CA ILE A 205 42.576 390.393 27.944 1.00 94.14 C
ANISOU 1618 CA ILE A 205 9775 11158 14838 1027 4505 2039 C
ATOM 1619 C ILE A 205 41.243 390.983 27.493 1.00 94.92 C
ANISOU 1619 C ILE A 205 10204 11298 14563 1055 4396 2041 C
ATOM 1620 O ILE A 205 40.845 392.076 27.917 1.00101.02 O
ANISOU 1620 O ILE A 205 10952 12013 15418 934 4280 2094 O
ATOM 1621 CB ILE A 205 43.661 390.512 26.860 1.00 88.97 C
ANISOU 1621 CB ILE A 205 9070 10456 14277 1132 4975 2216 C
ATOM 1622 CG1 ILE A 205 44.952 389.893 27.372 1.00 84.86 C
ANISOU 1622 CG1 ILE A 205 8208 9890 14146 1102 5023 2191 C
ATOM 1623 CG2 ILE A 205 43.936 391.964 26.500 1.00 76.07 C
ANISOU 1623 CG2 ILE A 205 7389 8713 12800 1049 5192 2428 C
ATOM 1624 CD1 ILE A 205 46.063 389.910 26.361 1.00 85.68 C
ANISOU 1624 CD1 ILE A 205 8322 9931 14300 1191 5347 2311 C
ATOM 1625 N TYR A 206 40.523 390.254 26.634 1.00 91.18 N
ANISOU 1625 N TYR A 206 10045 10917 13681 1222 4412 1974 N
ATOM 1626 CA TYR A 206 39.258 390.764 26.121 1.00 87.50 C
ANISOU 1626 CA TYR A 206 9892 10491 12862 1269 4295 1972 C
ATOM 1627 C TYR A 206 38.238 390.908 27.242 1.00 83.77 C
ANISOU 1627 C TYR A 206 9384 10039 12406 1137 3889 1838 C
ATOM 1628 O TYR A 206 37.494 391.894 27.300 1.00 87.57 O
ANISOU 1628 O TYR A 206 9955 10498 12820 1086 3787 1886 O
ATOM 1629 CB TYR A 206 38.720 389.828 25.037 1.00 85.48 C
ANISOU 1629 CB TYR A 206 9968 10324 12186 1479 4343 1893 C
ATOM 1630 CG TYR A 206 37.221 389.868 24.911 1.00 93.28 C
ANISOU 1630 CG TYR A 206 11222 11374 12848 1509 4049 1788 C
ATOM 1631 CD1 TYR A 206 36.583 390.915 24.260 1.00 94.45 C
ANISOU 1631 CD1 TYR A 206 11581 11507 12800 1550 4082 1900 C
ATOM 1632 CD2 TYR A 206 36.433 388.883 25.501 1.00100.66 C
ANISOU 1632 CD2 TYR A 206 12175 12369 13703 1491 3728 1583 C
ATOM 1633 CE1 TYR A 206 35.203 390.961 24.164 1.00 94.77 C
ANISOU 1633 CE1 TYR A 206 11836 11600 12573 1582 3794 1800 C
ATOM 1634 CE2 TYR A 206 35.053 388.924 25.419 1.00 98.61 C
ANISOU 1634 CE2 TYR A 206 12116 12156 13196 1509 3457 1487 C
ATOM 1635 CZ TYR A 206 34.445 389.962 24.747 1.00 98.77 C
ANISOU 1635 CZ TYR A 206 12331 12168 13029 1557 3483 1591 C
ATOM 1636 OH TYR A 206 33.075 389.998 24.664 1.00103.02 O
ANISOU 1636 OH TYR A 206 13045 12750 13348 1582 3199 1493 O
ATOM 1637 N MET A 207 38.200 389.936 28.154 1.00 84.07 N
ANISOU 1637 N MET A 207 9292 10113 12536 1090 3666 1679 N
ATOM 1638 CA MET A 207 37.364 390.077 29.337 1.00 83.19 C
ANISOU 1638 CA MET A 207 9121 10011 12478 963 3319 1569 C
ATOM 1639 C MET A 207 37.783 391.277 30.157 1.00 83.73 C
ANISOU 1639 C MET A 207 8977 9985 12851 805 3286 1654 C
ATOM 1640 O MET A 207 36.939 392.054 30.618 1.00 86.34 O
ANISOU 1640 O MET A 207 9362 10303 13142 734 3107 1642 O
ATOM 1641 CB MET A 207 37.486 388.834 30.213 1.00 84.37 C
ANISOU 1641 CB MET A 207 9150 10194 12713 941 3136 1416 C
ATOM 1642 CG MET A 207 36.699 387.649 29.754 1.00 96.47 C
ANISOU 1642 CG MET A 207 10893 11803 13956 1055 3041 1284 C
ATOM 1643 SD MET A 207 34.984 388.083 29.561 1.00110.63 S
ANISOU 1643 SD MET A 207 12932 13647 15456 1059 2817 1228 S
ATOM 1644 CE MET A 207 34.506 388.242 31.282 1.00104.24 C
ANISOU 1644 CE MET A 207 11935 12821 14852 887 2516 1150 C
ATOM 1645 N PHE A 208 39.093 391.453 30.320 1.00 88.09 N
ANISOU 1645 N PHE A 208 9283 10462 13727 755 3459 1738 N
ATOM 1646 CA PHE A 208 39.602 392.481 31.210 1.00 86.57 C
ANISOU 1646 CA PHE A 208 8856 10161 13876 594 3387 1790 C
ATOM 1647 C PHE A 208 39.227 393.854 30.667 1.00 92.61 C
ANISOU 1647 C PHE A 208 9735 10857 14595 567 3494 1930 C
ATOM 1648 O PHE A 208 38.766 394.729 31.406 1.00 96.03 O
ANISOU 1648 O PHE A 208 10140 11234 15113 459 3304 1913 O
ATOM 1649 CB PHE A 208 41.112 392.355 31.348 1.00 84.96 C
ANISOU 1649 CB PHE A 208 8350 9880 14052 555 3562 1856 C
ATOM 1650 CG PHE A 208 41.713 393.390 32.225 1.00 87.92 C
ANISOU 1650 CG PHE A 208 8471 10125 14812 389 3470 1898 C
ATOM 1651 CD1 PHE A 208 41.409 393.358 33.580 1.00 85.01 C
ANISOU 1651 CD1 PHE A 208 8018 9747 14534 292 3113 1757 C
ATOM 1652 CD2 PHE A 208 42.464 394.436 31.735 1.00 91.57 C
ANISOU 1652 CD2 PHE A 208 8806 10463 15523 330 3717 2071 C
ATOM 1653 CE1 PHE A 208 41.930 394.279 34.451 1.00 87.08 C
ANISOU 1653 CE1 PHE A 208 8070 9883 15135 147 2981 1765 C
ATOM 1654 CE2 PHE A 208 42.972 395.393 32.609 1.00 93.84 C
ANISOU 1654 CE2 PHE A 208 8858 10611 16187 164 3586 2087 C
ATOM 1655 CZ PHE A 208 42.699 395.312 33.970 1.00 89.55 C
ANISOU 1655 CZ PHE A 208 8237 10063 15725 77 3202 1922 C
ATOM 1656 N VAL A 209 39.434 394.056 29.363 1.00 95.42 N
ANISOU 1656 N VAL A 209 10237 11211 14808 677 3809 2073 N
ATOM 1657 CA VAL A 209 39.165 395.351 28.741 1.00 96.47 C
ANISOU 1657 CA VAL A 209 10495 11265 14896 669 3949 2235 C
ATOM 1658 C VAL A 209 37.665 395.600 28.641 1.00 99.61 C
ANISOU 1658 C VAL A 209 11171 11729 14948 718 3727 2167 C
ATOM 1659 O VAL A 209 37.156 396.620 29.116 1.00109.21 O
ANISOU 1659 O VAL A 209 12389 12877 16230 630 3590 2188 O
ATOM 1660 CB VAL A 209 39.818 395.431 27.353 1.00 90.84 C
ANISOU 1660 CB VAL A 209 9888 10531 14095 796 4370 2419 C
ATOM 1661 CG1 VAL A 209 39.400 396.711 26.678 1.00 85.40 C
ANISOU 1661 CG1 VAL A 209 9383 9763 13304 808 4500 2591 C
ATOM 1662 CG2 VAL A 209 41.336 395.342 27.455 1.00 83.35 C
ANISOU 1662 CG2 VAL A 209 8619 9498 13553 737 4621 2510 C
ATOM 1663 N VAL A 210 36.938 394.676 28.010 1.00 97.09 N
ANISOU 1663 N VAL A 210 11085 11532 14271 864 3684 2080 N
ATOM 1664 CA VAL A 210 35.573 394.958 27.573 1.00 85.96 C
ANISOU 1664 CA VAL A 210 9956 10177 12527 944 3530 2048 C
ATOM 1665 C VAL A 210 34.574 394.739 28.704 1.00 86.54 C
ANISOU 1665 C VAL A 210 9983 10297 12602 862 3160 1873 C
ATOM 1666 O VAL A 210 33.625 395.510 28.862 1.00 93.78 O
ANISOU 1666 O VAL A 210 10995 11200 13436 845 3008 1873 O
ATOM 1667 CB VAL A 210 35.233 394.113 26.333 1.00 78.40 C
ANISOU 1667 CB VAL A 210 9280 9315 11195 1144 3632 2028 C
ATOM 1668 CG1 VAL A 210 33.756 394.153 26.062 1.00 73.80 C
ANISOU 1668 CG1 VAL A 210 8944 8798 10298 1219 3384 1941 C
ATOM 1669 CG2 VAL A 210 35.975 394.647 25.131 1.00 67.98 C
ANISOU 1669 CG2 VAL A 210 8083 7940 9806 1249 4014 2234 C
ATOM 1670 N HIS A 211 34.754 393.689 29.500 1.00 84.20 N
ANISOU 1670 N HIS A 211 9545 10050 12397 819 3022 1730 N
ATOM 1671 CA HIS A 211 33.804 393.314 30.540 1.00 77.64 C
ANISOU 1671 CA HIS A 211 8687 9267 11544 759 2706 1572 C
ATOM 1672 C HIS A 211 34.288 393.668 31.938 1.00 78.50 C
ANISOU 1672 C HIS A 211 8552 9310 11964 606 2579 1538 C
ATOM 1673 O HIS A 211 33.671 393.255 32.923 1.00 77.83 O
ANISOU 1673 O HIS A 211 8431 9261 11879 559 2346 1411 O
ATOM 1674 CB HIS A 211 33.516 391.815 30.450 1.00 74.88 C
ANISOU 1674 CB HIS A 211 8396 9013 11042 833 2620 1432 C
ATOM 1675 CG HIS A 211 32.934 391.392 29.140 1.00 78.62 C
ANISOU 1675 CG HIS A 211 9133 9549 11191 991 2684 1426 C
ATOM 1676 ND1 HIS A 211 31.578 391.250 28.944 1.00 72.55 N
ANISOU 1676 ND1 HIS A 211 8534 8835 10198 1041 2478 1338 N
ATOM 1677 CD2 HIS A 211 33.512 391.171 27.935 1.00 89.15 C
ANISOU 1677 CD2 HIS A 211 10601 10888 12383 1121 2929 1502 C
ATOM 1678 CE1 HIS A 211 31.349 390.902 27.690 1.00 79.71 C
ANISOU 1678 CE1 HIS A 211 9672 9779 10834 1194 2557 1342 C
ATOM 1679 NE2 HIS A 211 32.505 390.856 27.054 1.00 87.98 N
ANISOU 1679 NE2 HIS A 211 10721 10800 11906 1252 2841 1443 N
ATOM 1680 N PHE A 212 35.361 394.442 32.050 1.00 82.33 N
ANISOU 1680 N PHE A 212 8874 9690 12718 530 2724 1648 N
ATOM 1681 CA PHE A 212 35.850 394.832 33.364 1.00 86.06 C
ANISOU 1681 CA PHE A 212 9126 10085 13488 391 2571 1602 C
ATOM 1682 C PHE A 212 36.224 396.310 33.383 1.00 95.64 C
ANISOU 1682 C PHE A 212 10273 11159 14907 305 2646 1723 C
ATOM 1683 O PHE A 212 35.834 397.046 34.294 1.00 99.16 O
ANISOU 1683 O PHE A 212 10688 11545 15444 221 2454 1674 O
ATOM 1684 CB PHE A 212 37.055 393.977 33.735 1.00 88.18 C
ANISOU 1684 CB PHE A 212 9181 10346 13978 368 2617 1572 C
ATOM 1685 CG PHE A 212 37.488 394.104 35.164 1.00 94.27 C
ANISOU 1685 CG PHE A 212 9752 11055 15010 252 2396 1487 C
ATOM 1686 CD1 PHE A 212 36.680 393.663 36.194 1.00 94.28 C
ANISOU 1686 CD1 PHE A 212 9808 11110 14903 238 2129 1348 C
ATOM 1687 CD2 PHE A 212 38.704 394.689 35.478 1.00 95.27 C
ANISOU 1687 CD2 PHE A 212 9641 11062 15497 160 2454 1550 C
ATOM 1688 CE1 PHE A 212 37.093 393.768 37.512 1.00 89.11 C
ANISOU 1688 CE1 PHE A 212 9007 10399 14453 154 1921 1269 C
ATOM 1689 CE2 PHE A 212 39.115 394.808 36.788 1.00 90.01 C
ANISOU 1689 CE2 PHE A 212 8807 10332 15060 66 2214 1457 C
ATOM 1690 CZ PHE A 212 38.306 394.347 37.808 1.00 88.64 C
ANISOU 1690 CZ PHE A 212 8727 10221 14732 71 1945 1316 C
ATOM 1691 N ILE A 213 37.006 396.745 32.395 1.00 95.96 N
ANISOU 1691 N ILE A 213 10294 11136 15031 327 2935 1885 N
ATOM 1692 CA ILE A 213 37.461 398.134 32.344 1.00 96.89 C
ANISOU 1692 CA ILE A 213 10335 11095 15385 235 3038 2022 C
ATOM 1693 C ILE A 213 36.348 399.043 31.831 1.00 96.33 C
ANISOU 1693 C ILE A 213 10510 11011 15082 286 3023 2083 C
ATOM 1694 O ILE A 213 35.998 400.046 32.463 1.00 95.23 O
ANISOU 1694 O ILE A 213 10355 10775 15054 204 2882 2075 O
ATOM 1695 CB ILE A 213 38.728 398.260 31.475 1.00 89.71 C
ANISOU 1695 CB ILE A 213 9301 10109 14677 240 3390 2195 C
ATOM 1696 CG1 ILE A 213 39.927 397.587 32.153 1.00 91.19 C
ANISOU 1696 CG1 ILE A 213 9182 10273 15194 168 3376 2137 C
ATOM 1697 CG2 ILE A 213 39.033 399.728 31.219 1.00 70.50 C
ANISOU 1697 CG2 ILE A 213 6834 7500 12452 156 3530 2363 C
ATOM 1698 CD1 ILE A 213 40.337 398.191 33.472 1.00 93.12 C
ANISOU 1698 CD1 ILE A 213 9194 10398 15789 6 3130 2060 C
ATOM 1699 N ILE A 214 35.819 398.723 30.643 1.00 93.86 N
ANISOU 1699 N ILE A 214 10433 10784 14445 433 3166 2146 N
ATOM 1700 CA ILE A 214 34.771 399.549 30.037 1.00 88.15 C
ANISOU 1700 CA ILE A 214 9956 10051 13487 507 3148 2214 C
ATOM 1701 C ILE A 214 33.561 399.729 30.956 1.00 95.61 C
ANISOU 1701 C ILE A 214 10946 11033 14349 480 2821 2066 C
ATOM 1702 O ILE A 214 33.099 400.872 31.110 1.00 90.21 O
ANISOU 1702 O ILE A 214 10315 10253 13707 450 2765 2117 O
ATOM 1703 CB ILE A 214 34.360 398.947 28.680 1.00 77.42 C
ANISOU 1703 CB ILE A 214 8859 8799 11759 691 3297 2265 C
ATOM 1704 CG1 ILE A 214 35.433 399.148 27.613 1.00 68.27 C
ANISOU 1704 CG1 ILE A 214 7719 7576 10646 744 3680 2464 C
ATOM 1705 CG2 ILE A 214 33.010 399.505 28.219 1.00 63.14 C
ANISOU 1705 CG2 ILE A 214 7311 7018 9661 789 3164 2272 C
ATOM 1706 CD1 ILE A 214 36.178 400.408 27.736 1.00 94.43 C
ANISOU 1706 CD1 ILE A 214 10895 10707 14277 627 3842 2633 C
ATOM 1707 N PRO A 215 33.024 398.681 31.616 1.00 92.38 N
ANISOU 1707 N PRO A 215 10514 10744 13842 490 2612 1888 N
ATOM 1708 CA PRO A 215 31.918 398.921 32.559 1.00 81.55 C
ANISOU 1708 CA PRO A 215 9165 9393 12426 461 2338 1763 C
ATOM 1709 C PRO A 215 32.246 399.932 33.634 1.00 91.11 C
ANISOU 1709 C PRO A 215 10235 10470 13912 333 2244 1754 C
ATOM 1710 O PRO A 215 31.407 400.783 33.953 1.00 97.98 O
ANISOU 1710 O PRO A 215 11185 11296 14749 334 2125 1741 O
ATOM 1711 CB PRO A 215 31.673 397.536 33.160 1.00 77.46 C
ANISOU 1711 CB PRO A 215 8595 8999 11837 469 2192 1601 C
ATOM 1712 CG PRO A 215 32.031 396.619 32.086 1.00 89.42 C
ANISOU 1712 CG PRO A 215 10186 10588 13202 565 2355 1634 C
ATOM 1713 CD PRO A 215 33.223 397.237 31.405 1.00 90.94 C
ANISOU 1713 CD PRO A 215 10325 10683 13546 551 2628 1802 C
ATOM 1714 N LEU A 216 33.459 399.877 34.189 1.00 93.68 N
ANISOU 1714 N LEU A 216 10353 10721 14521 228 2285 1756 N
ATOM 1715 CA LEU A 216 33.814 400.812 35.249 1.00 88.11 C
ANISOU 1715 CA LEU A 216 9517 9873 14086 106 2158 1724 C
ATOM 1716 C LEU A 216 33.882 402.235 34.712 1.00 92.37 C
ANISOU 1716 C LEU A 216 10109 10256 14729 80 2278 1873 C
ATOM 1717 O LEU A 216 33.432 403.174 35.379 1.00 95.42 O
ANISOU 1717 O LEU A 216 10520 10546 15189 36 2133 1833 O
ATOM 1718 CB LEU A 216 35.148 400.416 35.877 1.00 83.08 C
ANISOU 1718 CB LEU A 216 8635 9182 13749 7 2156 1693 C
ATOM 1719 CG LEU A 216 35.652 401.333 37.002 1.00 80.99 C
ANISOU 1719 CG LEU A 216 8226 8755 13791 -121 1990 1640 C
ATOM 1720 CD1 LEU A 216 34.902 401.071 38.313 1.00 74.95 C
ANISOU 1720 CD1 LEU A 216 7510 8043 12926 -118 1695 1454 C
ATOM 1721 CD2 LEU A 216 37.155 401.242 37.197 1.00 77.00 C
ANISOU 1721 CD2 LEU A 216 7458 8151 13648 -220 2052 1671 C
ATOM 1722 N ILE A 217 34.442 402.414 33.510 1.00 88.78 N
ANISOU 1722 N ILE A 217 9688 9767 14278 115 2555 2048 N
ATOM 1723 CA ILE A 217 34.576 403.753 32.939 1.00 87.96 C
ANISOU 1723 CA ILE A 217 9641 9497 14283 91 2703 2218 C
ATOM 1724 C ILE A 217 33.196 404.340 32.645 1.00 91.26 C
ANISOU 1724 C ILE A 217 10305 9939 14430 192 2605 2222 C
ATOM 1725 O ILE A 217 32.906 405.495 32.982 1.00 86.28 O
ANISOU 1725 O ILE A 217 9703 9167 13912 149 2535 2249 O
ATOM 1726 CB ILE A 217 35.462 403.707 31.679 1.00 82.52 C
ANISOU 1726 CB ILE A 217 8955 8775 13625 128 3057 2421 C
ATOM 1727 CG1 ILE A 217 36.867 403.226 32.029 1.00 88.59 C
ANISOU 1727 CG1 ILE A 217 9435 9498 14725 23 3154 2421 C
ATOM 1728 CG2 ILE A 217 35.573 405.063 31.046 1.00 72.84 C
ANISOU 1728 CG2 ILE A 217 7809 7368 12501 110 3234 2621 C
ATOM 1729 CD1 ILE A 217 37.476 403.975 33.180 1.00 90.91 C
ANISOU 1729 CD1 ILE A 217 9498 9622 15421 -150 2990 2360 C
ATOM 1730 N VAL A 218 32.319 403.549 32.020 1.00 95.52 N
ANISOU 1730 N VAL A 218 11020 10649 14625 333 2585 2188 N
ATOM 1731 CA VAL A 218 30.986 404.041 31.681 1.00 87.77 C
ANISOU 1731 CA VAL A 218 10254 9698 13398 442 2477 2189 C
ATOM 1732 C VAL A 218 30.200 404.364 32.942 1.00 81.83 C
ANISOU 1732 C VAL A 218 9454 8933 12706 395 2205 2029 C
ATOM 1733 O VAL A 218 29.574 405.425 33.047 1.00 82.70 O
ANISOU 1733 O VAL A 218 9649 8946 12827 413 2140 2060 O
ATOM 1734 CB VAL A 218 30.252 403.020 30.793 1.00 75.02 C
ANISOU 1734 CB VAL A 218 8811 8263 11430 597 2475 2159 C
ATOM 1735 CG1 VAL A 218 28.813 403.418 30.617 1.00 75.19 C
ANISOU 1735 CG1 VAL A 218 9009 8324 11234 705 2304 2124 C
ATOM 1736 CG2 VAL A 218 30.912 402.980 29.432 1.00 72.09 C
ANISOU 1736 CG2 VAL A 218 8560 7879 10952 679 2763 2339 C
ATOM 1737 N ILE A 219 30.255 403.478 33.935 1.00 79.29 N
ANISOU 1737 N ILE A 219 9001 8697 12427 343 2057 1864 N
ATOM 1738 CA ILE A 219 29.537 403.734 35.177 1.00 80.90 C
ANISOU 1738 CA ILE A 219 9177 8893 12669 312 1825 1716 C
ATOM 1739 C ILE A 219 30.049 405.005 35.846 1.00 86.43 C
ANISOU 1739 C ILE A 219 9808 9391 13639 211 1793 1737 C
ATOM 1740 O ILE A 219 29.257 405.842 36.293 1.00 92.60 O
ANISOU 1740 O ILE A 219 10667 10107 14408 236 1676 1698 O
ATOM 1741 CB ILE A 219 29.607 402.503 36.101 1.00 73.17 C
ANISOU 1741 CB ILE A 219 8089 8034 11679 281 1697 1556 C
ATOM 1742 CG1 ILE A 219 28.630 401.437 35.599 1.00 76.11 C
ANISOU 1742 CG1 ILE A 219 8560 8583 11775 390 1663 1505 C
ATOM 1743 CG2 ILE A 219 29.357 402.876 37.546 1.00 72.08 C
ANISOU 1743 CG2 ILE A 219 7895 7841 11649 225 1501 1422 C
ATOM 1744 CD1 ILE A 219 28.541 400.210 36.485 1.00 82.22 C
ANISOU 1744 CD1 ILE A 219 9248 9466 12525 368 1545 1360 C
ATOM 1745 N PHE A 220 31.370 405.192 35.900 1.00 87.86 N
ANISOU 1745 N PHE A 220 9838 9459 14085 99 1894 1797 N
ATOM 1746 CA PHE A 220 31.897 406.379 36.573 1.00 89.59 C
ANISOU 1746 CA PHE A 220 9978 9464 14597 -11 1835 1800 C
ATOM 1747 C PHE A 220 31.561 407.655 35.808 1.00 91.69 C
ANISOU 1747 C PHE A 220 10377 9585 14875 20 1946 1954 C
ATOM 1748 O PHE A 220 31.175 408.665 36.413 1.00 84.96 O
ANISOU 1748 O PHE A 220 9567 8596 14117 -2 1821 1910 O
ATOM 1749 CB PHE A 220 33.404 406.261 36.781 1.00 78.98 C
ANISOU 1749 CB PHE A 220 8410 8022 13577 -144 1906 1828 C
ATOM 1750 CG PHE A 220 33.779 405.808 38.156 1.00 95.62 C
ANISOU 1750 CG PHE A 220 10380 10136 15815 -216 1672 1640 C
ATOM 1751 CD1 PHE A 220 33.690 404.472 38.511 1.00111.58 C
ANISOU 1751 CD1 PHE A 220 12371 12341 17684 -173 1602 1534 C
ATOM 1752 CD2 PHE A 220 34.207 406.719 39.104 1.00108.44 C
ANISOU 1752 CD2 PHE A 220 11924 11572 17705 -318 1510 1565 C
ATOM 1753 CE1 PHE A 220 34.035 404.050 39.787 1.00117.98 C
ANISOU 1753 CE1 PHE A 220 13082 13154 18591 -222 1384 1372 C
ATOM 1754 CE2 PHE A 220 34.553 406.303 40.380 1.00118.14 C
ANISOU 1754 CE2 PHE A 220 13059 12806 19025 -364 1274 1386 C
ATOM 1755 CZ PHE A 220 34.472 404.966 40.718 1.00118.43 C
ANISOU 1755 CZ PHE A 220 13074 13032 18892 -311 1216 1297 C
ATOM 1756 N PHE A 221 31.678 407.622 34.480 1.00 84.29 N
ANISOU 1756 N PHE A 221 9530 8670 13826 85 2179 2135 N
ATOM 1757 CA PHE A 221 31.371 408.804 33.685 1.00 76.78 C
ANISOU 1757 CA PHE A 221 8731 7577 12865 131 2299 2305 C
ATOM 1758 C PHE A 221 29.901 409.189 33.794 1.00 88.50 C
ANISOU 1758 C PHE A 221 10401 9109 14116 255 2131 2240 C
ATOM 1759 O PHE A 221 29.571 410.313 34.184 1.00102.52 O
ANISOU 1759 O PHE A 221 12222 10724 16005 240 2051 2243 O
ATOM 1760 CB PHE A 221 31.742 408.543 32.226 1.00 70.26 C
ANISOU 1760 CB PHE A 221 8002 6790 11903 208 2586 2510 C
ATOM 1761 CG PHE A 221 31.338 409.643 31.282 1.00 77.94 C
ANISOU 1761 CG PHE A 221 9179 7636 12797 289 2720 2705 C
ATOM 1762 CD1 PHE A 221 32.211 410.675 30.972 1.00 83.43 C
ANISOU 1762 CD1 PHE A 221 9828 8098 13772 196 2918 2889 C
ATOM 1763 CD2 PHE A 221 30.085 409.625 30.672 1.00 83.12 C
ANISOU 1763 CD2 PHE A 221 10073 8400 13109 464 2647 2713 C
ATOM 1764 CE1 PHE A 221 31.839 411.677 30.093 1.00 82.78 C
ANISOU 1764 CE1 PHE A 221 9955 7889 13610 280 3051 3086 C
ATOM 1765 CE2 PHE A 221 29.705 410.626 29.791 1.00 81.91 C
ANISOU 1765 CE2 PHE A 221 10127 8128 12867 559 2755 2899 C
ATOM 1766 CZ PHE A 221 30.583 411.650 29.500 1.00 84.15 C
ANISOU 1766 CZ PHE A 221 10385 8178 13411 470 2965 3092 C
ATOM 1767 N CYS A 222 29.004 408.247 33.515 1.00 87.42 N
ANISOU 1767 N CYS A 222 10355 9184 13677 376 2061 2168 N
ATOM 1768 CA CYS A 222 27.581 408.557 33.541 1.00 86.13 C
ANISOU 1768 CA CYS A 222 10340 9072 13313 503 1908 2113 C
ATOM 1769 C CYS A 222 27.158 409.113 34.896 1.00 86.19 C
ANISOU 1769 C CYS A 222 10285 9003 13461 454 1708 1958 C
ATOM 1770 O CYS A 222 26.532 410.174 34.971 1.00 99.17 O
ANISOU 1770 O CYS A 222 12025 10529 15127 503 1652 1982 O
ATOM 1771 CB CYS A 222 26.782 407.307 33.177 1.00 84.63 C
ANISOU 1771 CB CYS A 222 10202 9115 12837 612 1841 2031 C
ATOM 1772 SG CYS A 222 26.894 406.911 31.413 1.00 89.84 S
ANISOU 1772 SG CYS A 222 11042 9849 13245 740 2041 2209 S
ATOM 1773 N TYR A 223 27.522 408.433 35.982 1.00 80.61 N
ANISOU 1773 N TYR A 223 9433 8352 12843 368 1601 1800 N
ATOM 1774 CA TYR A 223 27.091 408.896 37.295 1.00 82.46 C
ANISOU 1774 CA TYR A 223 9642 8523 13164 346 1413 1643 C
ATOM 1775 C TYR A 223 27.838 410.145 37.733 1.00 86.90 C
ANISOU 1775 C TYR A 223 10172 8835 14011 243 1406 1670 C
ATOM 1776 O TYR A 223 27.274 410.984 38.447 1.00101.34 O
ANISOU 1776 O TYR A 223 12062 10558 15886 269 1281 1588 O
ATOM 1777 CB TYR A 223 27.276 407.784 38.323 1.00 85.56 C
ANISOU 1777 CB TYR A 223 9922 9044 13543 300 1301 1476 C
ATOM 1778 CG TYR A 223 26.163 406.776 38.270 1.00 92.83 C
ANISOU 1778 CG TYR A 223 10887 10175 14209 407 1249 1404 C
ATOM 1779 CD1 TYR A 223 24.843 407.186 38.162 1.00 99.26 C
ANISOU 1779 CD1 TYR A 223 11808 11019 14888 526 1188 1389 C
ATOM 1780 CD2 TYR A 223 26.431 405.416 38.256 1.00 88.96 C
ANISOU 1780 CD2 TYR A 223 10324 9842 13636 390 1262 1359 C
ATOM 1781 CE1 TYR A 223 23.811 406.266 38.094 1.00105.37 C
ANISOU 1781 CE1 TYR A 223 12593 11971 15473 614 1136 1325 C
ATOM 1782 CE2 TYR A 223 25.411 404.494 38.188 1.00 94.57 C
ANISOU 1782 CE2 TYR A 223 11064 10721 14146 476 1211 1296 C
ATOM 1783 CZ TYR A 223 24.100 404.922 38.106 1.00 97.96 C
ANISOU 1783 CZ TYR A 223 11580 11175 14465 582 1147 1279 C
ATOM 1784 OH TYR A 223 23.075 404.009 38.034 1.00 97.16 O
ANISOU 1784 OH TYR A 223 11480 11228 14209 656 1091 1215 O
ATOM 1785 N GLY A 224 29.083 410.311 37.299 1.00 84.64 N
ANISOU 1785 N GLY A 224 9787 8437 13934 131 1542 1784 N
ATOM 1786 CA GLY A 224 29.788 411.537 37.620 1.00 83.84 C
ANISOU 1786 CA GLY A 224 9642 8071 14142 22 1536 1821 C
ATOM 1787 C GLY A 224 29.121 412.734 36.981 1.00 89.69 C
ANISOU 1787 C GLY A 224 10552 8671 14856 99 1595 1947 C
ATOM 1788 O GLY A 224 28.831 413.732 37.645 1.00 93.60 O
ANISOU 1788 O GLY A 224 11095 8997 15473 91 1472 1879 O
ATOM 1789 N GLN A 225 28.874 412.641 35.673 1.00 88.52 N
ANISOU 1789 N GLN A 225 10512 8585 14538 188 1779 2131 N
ATOM 1790 CA GLN A 225 28.174 413.693 34.951 1.00 86.16 C
ANISOU 1790 CA GLN A 225 10399 8169 14170 290 1834 2269 C
ATOM 1791 C GLN A 225 26.823 413.981 35.585 1.00 98.05 C
ANISOU 1791 C GLN A 225 12008 9719 15528 412 1629 2125 C
ATOM 1792 O GLN A 225 26.434 415.143 35.753 1.00110.35 O
ANISOU 1792 O GLN A 225 13657 11093 17179 443 1579 2146 O
ATOM 1793 CB GLN A 225 28.010 413.275 33.492 1.00 75.66 C
ANISOU 1793 CB GLN A 225 9196 6953 12597 403 2028 2458 C
ATOM 1794 CG GLN A 225 29.295 413.405 32.675 1.00 93.98 C
ANISOU 1794 CG GLN A 225 11463 9161 15084 309 2300 2664 C
ATOM 1795 CD GLN A 225 29.878 414.805 32.690 1.00108.69 C
ANISOU 1795 CD GLN A 225 13320 10714 17264 211 2386 2795 C
ATOM 1796 OE1 GLN A 225 31.090 414.980 32.829 1.00114.44 O
ANISOU 1796 OE1 GLN A 225 13877 11299 18306 50 2505 2854 O
ATOM 1797 NE2 GLN A 225 29.020 415.810 32.536 1.00114.13 N
ANISOU 1797 NE2 GLN A 225 14187 11285 17893 307 2325 2845 N
ATOM 1798 N LEU A 226 26.089 412.926 35.927 1.00 93.96 N
ANISOU 1798 N LEU A 226 11472 9437 14793 486 1521 1985 N
ATOM 1799 CA LEU A 226 24.764 413.090 36.506 1.00 91.94 C
ANISOU 1799 CA LEU A 226 11288 9242 14404 611 1355 1856 C
ATOM 1800 C LEU A 226 24.821 413.865 37.821 1.00 96.79 C
ANISOU 1800 C LEU A 226 11872 9695 15210 554 1216 1707 C
ATOM 1801 O LEU A 226 24.054 414.817 38.025 1.00 97.98 O
ANISOU 1801 O LEU A 226 12126 9732 15371 643 1149 1689 O
ATOM 1802 CB LEU A 226 24.119 411.711 36.694 1.00 73.92 C
ANISOU 1802 CB LEU A 226 8955 7228 11904 669 1286 1737 C
ATOM 1803 CG LEU A 226 22.662 411.622 37.147 1.00 75.88 C
ANISOU 1803 CG LEU A 226 9245 7580 12004 808 1148 1620 C
ATOM 1804 CD1 LEU A 226 22.108 410.302 36.661 1.00 79.46 C
ANISOU 1804 CD1 LEU A 226 9670 8274 12246 869 1140 1595 C
ATOM 1805 CD2 LEU A 226 22.528 411.735 38.660 1.00 70.42 C
ANISOU 1805 CD2 LEU A 226 8495 6854 11407 772 1026 1432 C
ATOM 1806 N VAL A 227 25.752 413.499 38.712 1.00 87.10 N
ANISOU 1806 N VAL A 227 10515 8443 14138 418 1164 1596 N
ATOM 1807 CA VAL A 227 25.868 414.214 39.981 1.00 83.10 C
ANISOU 1807 CA VAL A 227 10004 7775 13796 373 1008 1438 C
ATOM 1808 C VAL A 227 26.247 415.660 39.715 1.00 93.62 C
ANISOU 1808 C VAL A 227 11397 8815 15359 328 1039 1536 C
ATOM 1809 O VAL A 227 25.770 416.580 40.388 1.00105.78 O
ANISOU 1809 O VAL A 227 13025 10204 16962 375 925 1441 O
ATOM 1810 CB VAL A 227 26.870 413.528 40.922 1.00 76.29 C
ANISOU 1810 CB VAL A 227 8999 6935 13053 242 921 1305 C
ATOM 1811 CG1 VAL A 227 27.187 414.446 42.089 1.00 75.93 C
ANISOU 1811 CG1 VAL A 227 8974 6672 13206 189 752 1156 C
ATOM 1812 CG2 VAL A 227 26.330 412.201 41.401 1.00 77.87 C
ANISOU 1812 CG2 VAL A 227 9169 7396 13021 304 870 1190 C
ATOM 1813 N PHE A 228 27.134 415.880 38.747 1.00 93.43 N
ANISOU 1813 N PHE A 228 11329 8692 15476 238 1206 1729 N
ATOM 1814 CA PHE A 228 27.521 417.240 38.399 1.00 92.17 C
ANISOU 1814 CA PHE A 228 11226 8237 15558 186 1266 1854 C
ATOM 1815 C PHE A 228 26.306 418.042 37.933 1.00 93.69 C
ANISOU 1815 C PHE A 228 11615 8385 15600 358 1266 1922 C
ATOM 1816 O PHE A 228 26.068 419.163 38.398 1.00 95.05 O
ANISOU 1816 O PHE A 228 11867 8334 15914 373 1179 1877 O
ATOM 1817 CB PHE A 228 28.607 417.197 37.325 1.00 84.45 C
ANISOU 1817 CB PHE A 228 10170 7192 14726 78 1498 2081 C
ATOM 1818 CG PHE A 228 29.026 418.543 36.843 1.00100.06 C
ANISOU 1818 CG PHE A 228 12202 8857 16960 19 1603 2250 C
ATOM 1819 CD1 PHE A 228 30.048 419.234 37.467 1.00100.01 C
ANISOU 1819 CD1 PHE A 228 12066 8587 17346 -160 1551 2209 C
ATOM 1820 CD2 PHE A 228 28.404 419.117 35.744 1.00102.93 C
ANISOU 1820 CD2 PHE A 228 12749 9178 17182 145 1747 2455 C
ATOM 1821 CE1 PHE A 228 30.425 420.474 37.013 1.00 97.12 C
ANISOU 1821 CE1 PHE A 228 11745 7912 17244 -224 1655 2373 C
ATOM 1822 CE2 PHE A 228 28.782 420.350 35.289 1.00 93.35 C
ANISOU 1822 CE2 PHE A 228 11600 7664 16205 95 1858 2629 C
ATOM 1823 CZ PHE A 228 29.791 421.031 35.924 1.00 95.28 C
ANISOU 1823 CZ PHE A 228 11706 7639 16859 -96 1822 2591 C
ATOM 1824 N THR A 229 25.524 417.475 37.009 1.00 90.26 N
ANISOU 1824 N THR A 229 11262 8151 14883 497 1348 2022 N
ATOM 1825 CA THR A 229 24.311 418.134 36.524 1.00 87.08 C
ANISOU 1825 CA THR A 229 11033 7728 14327 681 1324 2083 C
ATOM 1826 C THR A 229 23.330 418.430 37.659 1.00 88.89 C
ANISOU 1826 C THR A 229 11291 7959 14525 774 1131 1870 C
ATOM 1827 O THR A 229 22.731 419.509 37.705 1.00 94.06 O
ANISOU 1827 O THR A 229 12064 8443 15231 867 1086 1885 O
ATOM 1828 CB THR A 229 23.662 417.281 35.430 1.00 82.30 C
ANISOU 1828 CB THR A 229 10488 7363 13417 813 1397 2187 C
ATOM 1829 OG1 THR A 229 24.503 417.286 34.271 1.00 92.61 O
ANISOU 1829 OG1 THR A 229 11830 8620 14738 764 1605 2414 O
ATOM 1830 CG2 THR A 229 22.303 417.797 35.050 1.00 69.01 C
ANISOU 1830 CG2 THR A 229 8956 5694 11569 1018 1320 2213 C
ATOM 1831 N VAL A 230 23.131 417.483 38.572 1.00 90.80 N
ANISOU 1831 N VAL A 230 11436 8387 14675 765 1031 1678 N
ATOM 1832 CA VAL A 230 22.146 417.703 39.625 1.00 81.91 C
ANISOU 1832 CA VAL A 230 10349 7279 13494 876 886 1489 C
ATOM 1833 C VAL A 230 22.626 418.770 40.607 1.00 90.77 C
ANISOU 1833 C VAL A 230 11508 8132 14849 809 791 1377 C
ATOM 1834 O VAL A 230 21.856 419.657 40.998 1.00 96.74 O
ANISOU 1834 O VAL A 230 12373 8764 15619 926 722 1314 O
ATOM 1835 CB VAL A 230 21.849 416.358 40.316 1.00 68.45 C
ANISOU 1835 CB VAL A 230 8543 5838 11625 882 832 1336 C
ATOM 1836 CG1 VAL A 230 21.037 416.541 41.581 1.00 63.77 C
ANISOU 1836 CG1 VAL A 230 7985 5251 10995 978 714 1134 C
ATOM 1837 CG2 VAL A 230 21.090 415.471 39.351 1.00 62.73 C
ANISOU 1837 CG2 VAL A 230 7806 5348 10679 981 892 1425 C
ATOM 1838 N LYS A 231 23.899 418.703 41.022 1.00 91.27 N
ANISOU 1838 N LYS A 231 11479 8092 15110 626 773 1341 N
ATOM 1839 CA LYS A 231 24.482 419.755 41.856 1.00 90.84 C
ANISOU 1839 CA LYS A 231 11456 7748 15311 544 659 1237 C
ATOM 1840 C LYS A 231 24.418 421.123 41.187 1.00 90.33 C
ANISOU 1840 C LYS A 231 11502 7406 15412 564 717 1384 C
ATOM 1841 O LYS A 231 24.150 422.139 41.845 1.00 85.98 O
ANISOU 1841 O LYS A 231 11055 6638 14975 608 606 1278 O
ATOM 1842 CB LYS A 231 25.921 419.405 42.240 1.00 86.42 C
ANISOU 1842 CB LYS A 231 10746 7122 14969 336 624 1197 C
ATOM 1843 CG LYS A 231 26.053 418.123 43.035 1.00 84.27 C
ANISOU 1843 CG LYS A 231 10381 7088 14550 320 541 1039 C
ATOM 1844 CD LYS A 231 27.127 418.292 44.087 1.00 81.48 C
ANISOU 1844 CD LYS A 231 9957 6576 14427 180 370 879 C
ATOM 1845 CE LYS A 231 27.411 417.010 44.821 1.00 80.38 C
ANISOU 1845 CE LYS A 231 9729 6657 14155 159 290 747 C
ATOM 1846 NZ LYS A 231 26.655 417.011 46.111 1.00 84.28 N
ANISOU 1846 NZ LYS A 231 10359 7188 14474 286 126 520 N
ATOM 1847 N GLU A 232 24.702 421.174 39.888 1.00 85.22 N
ANISOU 1847 N GLU A 232 10851 6748 14780 538 894 1632 N
ATOM 1848 CA GLU A 232 24.716 422.453 39.195 1.00 88.60 C
ANISOU 1848 CA GLU A 232 11396 6899 15369 553 971 1804 C
ATOM 1849 C GLU A 232 23.315 423.041 39.147 1.00 97.29 C
ANISOU 1849 C GLU A 232 12664 7999 16303 777 915 1785 C
ATOM 1850 O GLU A 232 23.128 424.243 39.368 1.00106.68 O
ANISOU 1850 O GLU A 232 13965 8920 17649 814 863 1777 O
ATOM 1851 CB GLU A 232 25.299 422.258 37.800 1.00 95.49 C
ANISOU 1851 CB GLU A 232 12250 7788 16242 499 1198 2085 C
ATOM 1852 CG GLU A 232 25.931 423.490 37.199 1.00116.85 C
ANISOU 1852 CG GLU A 232 15017 10153 19226 418 1316 2284 C
ATOM 1853 CD GLU A 232 26.560 423.188 35.858 1.00129.21 C
ANISOU 1853 CD GLU A 232 16571 11755 20768 373 1576 2567 C
ATOM 1854 OE1 GLU A 232 26.202 422.147 35.270 1.00146.21 O
ANISOU 1854 OE1 GLU A 232 18727 14200 22626 462 1642 2608 O
ATOM 1855 OE2 GLU A 232 27.435 423.958 35.412 1.00120.04 O
ANISOU 1855 OE2 GLU A 232 15396 10326 19888 248 1721 2743 O
ATOM 1856 N ALA A 233 22.321 422.197 38.863 1.00 94.06 N
ANISOU 1856 N ALA A 233 12261 7880 15596 929 918 1773 N
ATOM 1857 CA ALA A 233 20.938 422.645 38.787 1.00 86.49 C
ANISOU 1857 CA ALA A 233 11424 6947 14491 1153 861 1754 C
ATOM 1858 C ALA A 233 20.444 423.077 40.159 1.00 91.05 C
ANISOU 1858 C ALA A 233 12028 7446 15120 1214 710 1507 C
ATOM 1859 O ALA A 233 19.758 424.100 40.290 1.00 89.36 O
ANISOU 1859 O ALA A 233 11937 7059 14957 1347 663 1490 O
ATOM 1860 CB ALA A 233 20.054 421.538 38.215 1.00 72.25 C
ANISOU 1860 CB ALA A 233 9583 5473 12397 1280 880 1782 C
ATOM 1861 N ALA A 234 20.762 422.290 41.192 1.00 89.83 N
ANISOU 1861 N ALA A 234 11776 7419 14936 1137 637 1312 N
ATOM 1862 CA ALA A 234 20.323 422.638 42.538 1.00 88.68 C
ANISOU 1862 CA ALA A 234 11685 7209 14801 1211 506 1071 C
ATOM 1863 C ALA A 234 20.941 423.952 42.986 1.00 94.69 C
ANISOU 1863 C ALA A 234 12544 7605 15828 1144 428 1021 C
ATOM 1864 O ALA A 234 20.301 424.721 43.707 1.00 98.45 O
ANISOU 1864 O ALA A 234 13140 7946 16319 1273 342 882 O
ATOM 1865 CB ALA A 234 20.686 421.515 43.519 1.00 76.04 C
ANISOU 1865 CB ALA A 234 9983 5801 13106 1136 447 894 C
ATOM 1866 N ALA A 235 22.179 424.225 42.562 1.00 93.07 N
ANISOU 1866 N ALA A 235 12284 7226 15850 945 461 1132 N
ATOM 1867 CA ALA A 235 22.850 425.468 42.925 1.00 86.85 C
ANISOU 1867 CA ALA A 235 11567 6064 15368 852 381 1094 C
ATOM 1868 C ALA A 235 22.113 426.680 42.378 1.00 97.14 C
ANISOU 1868 C ALA A 235 13032 7152 16726 993 417 1205 C
ATOM 1869 O ALA A 235 22.153 427.758 42.982 1.00113.41 O
ANISOU 1869 O ALA A 235 15203 8919 18970 1006 310 1097 O
ATOM 1870 CB ALA A 235 24.286 425.461 42.412 1.00 82.31 C
ANISOU 1870 CB ALA A 235 10864 5354 15056 607 446 1231 C
ATOM 1871 N GLN A 236 21.441 426.524 41.237 1.00 88.97 N
ANISOU 1871 N GLN A 236 12024 6248 15533 1108 552 1417 N
ATOM 1872 CA GLN A 236 20.646 427.584 40.635 1.00 89.02 C
ANISOU 1872 CA GLN A 236 12188 6079 15557 1273 581 1541 C
ATOM 1873 C GLN A 236 19.266 427.717 41.268 1.00 92.04 C
ANISOU 1873 C GLN A 236 12650 6553 15769 1519 491 1376 C
ATOM 1874 O GLN A 236 18.497 428.602 40.868 1.00 98.27 O
ANISOU 1874 O GLN A 236 13566 7200 16571 1685 494 1455 O
ATOM 1875 CB GLN A 236 20.484 427.309 39.139 1.00 88.21 C
ANISOU 1875 CB GLN A 236 12097 6092 15328 1316 742 1832 C
ATOM 1876 CG GLN A 236 21.575 427.894 38.266 1.00 96.27 C
ANISOU 1876 CG GLN A 236 13137 6869 16572 1153 880 2074 C
ATOM 1877 CD GLN A 236 21.567 429.395 38.205 1.00107.35 C
ANISOU 1877 CD GLN A 236 14694 7878 18215 1181 865 2145 C
ATOM 1878 OE1 GLN A 236 20.561 430.040 38.485 1.00115.24 O
ANISOU 1878 OE1 GLN A 236 15818 8804 19162 1374 774 2069 O
ATOM 1879 NE2 GLN A 236 22.704 429.967 37.838 1.00113.50 N
ANISOU 1879 NE2 GLN A 236 15456 8387 19284 986 965 2295 N
ATOM 1880 N GLN A 237 18.932 426.860 42.229 1.00 82.08 N
ANISOU 1880 N GLN A 237 11315 5519 14353 1553 424 1162 N
ATOM 1881 CA GLN A 237 17.631 426.868 42.889 1.00 88.89 C
ANISOU 1881 CA GLN A 237 12226 6491 15059 1784 375 1007 C
ATOM 1882 C GLN A 237 17.827 426.639 44.376 1.00 90.78 C
ANISOU 1882 C GLN A 237 12471 6737 15283 1761 273 726 C
ATOM 1883 O GLN A 237 17.140 425.834 45.005 1.00 88.95 O
ANISOU 1883 O GLN A 237 12191 6749 14856 1863 277 598 O
ATOM 1884 CB GLN A 237 16.674 425.821 42.326 1.00 99.11 C
ANISOU 1884 CB GLN A 237 13418 8134 16107 1908 441 1077 C
ATOM 1885 CG GLN A 237 16.207 426.069 40.913 1.00112.70 C
ANISOU 1885 CG GLN A 237 15170 9864 17787 2000 506 1325 C
ATOM 1886 CD GLN A 237 15.000 425.229 40.571 1.00119.21 C
ANISOU 1886 CD GLN A 237 15906 10992 18397 2170 512 1334 C
ATOM 1887 OE1 GLN A 237 14.104 425.058 41.401 1.00117.97 O
ANISOU 1887 OE1 GLN A 237 15712 10934 18179 2308 477 1166 O
ATOM 1888 NE2 GLN A 237 14.959 424.708 39.348 1.00122.17 N
ANISOU 1888 NE2 GLN A 237 16250 11507 18662 2169 559 1527 N
ATOM 1889 N GLN A 238 18.734 427.404 44.972 1.00 95.93 N
ANISOU 1889 N GLN A 238 13201 7101 16148 1639 175 626 N
ATOM 1890 CA GLN A 238 19.045 427.186 46.374 1.00100.18 C
ANISOU 1890 CA GLN A 238 13773 7632 16658 1615 49 354 C
ATOM 1891 C GLN A 238 17.923 427.634 47.299 1.00101.21 C
ANISOU 1891 C GLN A 238 14047 7740 16666 1863 13 160 C
ATOM 1892 O GLN A 238 17.973 427.324 48.494 1.00 96.34 O
ANISOU 1892 O GLN A 238 13488 7170 15948 1894 -67 -67 O
ATOM 1893 CB GLN A 238 20.329 427.931 46.691 1.00105.19 C
ANISOU 1893 CB GLN A 238 14445 7939 17582 1416 -76 296 C
ATOM 1894 CG GLN A 238 21.554 427.279 46.110 1.00112.41 C
ANISOU 1894 CG GLN A 238 15186 8907 18618 1163 -41 432 C
ATOM 1895 CD GLN A 238 22.808 427.919 46.618 1.00123.73 C
ANISOU 1895 CD GLN A 238 16621 10029 20363 965 -191 335 C
ATOM 1896 OE1 GLN A 238 22.872 428.333 47.765 1.00126.25 O
ANISOU 1896 OE1 GLN A 238 17054 10202 20711 1003 -370 85 O
ATOM 1897 NE2 GLN A 238 23.802 428.049 45.753 1.00132.29 N
ANISOU 1897 NE2 GLN A 238 17582 10990 21692 761 -119 534 N
ATOM 1898 N GLU A 239 16.903 428.317 46.766 1.00108.02 N
ANISOU 1898 N GLU A 239 14974 8544 17524 2053 77 250 N
ATOM 1899 CA GLU A 239 15.717 428.693 47.525 1.00106.62 C
ANISOU 1899 CA GLU A 239 14905 8371 17234 2316 81 91 C
ATOM 1900 C GLU A 239 14.781 427.517 47.765 1.00105.99 C
ANISOU 1900 C GLU A 239 14705 8665 16901 2440 182 61 C
ATOM 1901 O GLU A 239 13.886 427.613 48.609 1.00103.01 O
ANISOU 1901 O GLU A 239 14396 8329 16416 2645 210 -96 O
ATOM 1902 CB GLU A 239 14.942 429.836 46.829 1.00 86.33 C
ANISOU 1902 CB GLU A 239 12427 5600 14774 2487 110 208 C
ATOM 1903 CG GLU A 239 14.362 429.566 45.400 1.00 93.50 C
ANISOU 1903 CG GLU A 239 13223 6663 15641 2537 212 484 C
ATOM 1904 CD GLU A 239 15.408 429.563 44.263 1.00105.40 C
ANISOU 1904 CD GLU A 239 14686 8093 17270 2315 235 720 C
ATOM 1905 OE1 GLU A 239 16.618 429.487 44.559 1.00115.42 O
ANISOU 1905 OE1 GLU A 239 15941 9257 18656 2091 191 680 O
ATOM 1906 OE2 GLU A 239 15.021 429.620 43.065 1.00 95.71 O
ANISOU 1906 OE2 GLU A 239 13436 6910 16018 2372 301 949 O
ATOM 1907 N SER A 240 14.994 426.395 47.093 1.00113.79 N
ANISOU 1907 N SER A 240 15519 9915 17801 2321 244 199 N
ATOM 1908 CA SER A 240 14.097 425.252 47.190 1.00116.99 C
ANISOU 1908 CA SER A 240 15789 10659 18002 2421 340 193 C
ATOM 1909 C SER A 240 14.726 424.229 48.124 1.00108.56 C
ANISOU 1909 C SER A 240 14687 9748 16815 2302 321 54 C
ATOM 1910 O SER A 240 15.696 423.562 47.756 1.00115.32 O
ANISOU 1910 O SER A 240 15453 10675 17688 2096 299 126 O
ATOM 1911 CB SER A 240 13.837 424.652 45.813 1.00120.94 C
ANISOU 1911 CB SER A 240 16137 11342 18473 2387 404 426 C
ATOM 1912 OG SER A 240 13.052 423.481 45.925 1.00120.57 O
ANISOU 1912 OG SER A 240 15942 11608 18259 2455 476 409 O
ATOM 1913 N ALA A 241 14.186 424.130 49.344 1.00106.98 N
ANISOU 1913 N ALA A 241 14568 9588 16490 2445 337 -143 N
ATOM 1914 CA ALA A 241 14.727 423.206 50.337 1.00105.15 C
ANISOU 1914 CA ALA A 241 14344 9490 16119 2365 315 -282 C
ATOM 1915 C ALA A 241 14.639 421.758 49.879 1.00116.74 C
ANISOU 1915 C ALA A 241 15610 11278 17469 2279 404 -168 C
ATOM 1916 O ALA A 241 15.489 420.940 50.253 1.00117.83 O
ANISOU 1916 O ALA A 241 15717 11506 17548 2130 361 -208 O
ATOM 1917 CB ALA A 241 14.002 423.374 51.670 1.00 97.60 C
ANISOU 1917 CB ALA A 241 13539 8528 15016 2576 353 -492 C
ATOM 1918 N THR A 242 13.634 421.422 49.063 1.00114.14 N
ANISOU 1918 N THR A 242 15141 11111 17117 2372 512 -32 N
ATOM 1919 CA THR A 242 13.491 420.044 48.605 1.00104.15 C
ANISOU 1919 CA THR A 242 13686 10133 15752 2296 584 64 C
ATOM 1920 C THR A 242 14.483 419.720 47.497 1.00 99.62 C
ANISOU 1920 C THR A 242 13030 9572 15250 2087 535 222 C
ATOM 1921 O THR A 242 15.046 418.618 47.463 1.00 99.57 O
ANISOU 1921 O THR A 242 12927 9731 15173 1951 545 243 O
ATOM 1922 CB THR A 242 12.082 419.797 48.075 1.00 98.96 C
ANISOU 1922 CB THR A 242 12896 9632 15072 2464 685 145 C
ATOM 1923 OG1 THR A 242 11.814 420.724 47.023 1.00 95.86 O
ANISOU 1923 OG1 THR A 242 12516 9104 14803 2519 644 271 O
ATOM 1924 CG2 THR A 242 11.061 420.041 49.181 1.00 97.36 C
ANISOU 1924 CG2 THR A 242 12749 9433 14810 2680 776 -1 C
ATOM 1925 N THR A 243 14.708 420.675 46.592 1.00 94.19 N
ANISOU 1925 N THR A 243 12387 8701 14701 2070 497 341 N
ATOM 1926 CA THR A 243 15.772 420.544 45.604 1.00 91.71 C
ANISOU 1926 CA THR A 243 12027 8351 14469 1878 477 494 C
ATOM 1927 C THR A 243 17.102 420.212 46.276 1.00 90.56 C
ANISOU 1927 C THR A 243 11890 8154 14365 1685 412 404 C
ATOM 1928 O THR A 243 17.825 419.308 45.837 1.00 83.29 O
ANISOU 1928 O THR A 243 10860 7363 13425 1535 432 480 O
ATOM 1929 CB THR A 243 15.857 421.830 44.777 1.00 87.80 C
ANISOU 1929 CB THR A 243 11626 7603 14129 1903 457 619 C
ATOM 1930 OG1 THR A 243 14.776 421.856 43.841 1.00 82.63 O
ANISOU 1930 OG1 THR A 243 10931 7046 13419 2055 503 750 O
ATOM 1931 CG2 THR A 243 17.150 421.897 44.004 1.00 94.34 C
ANISOU 1931 CG2 THR A 243 12438 8329 15078 1694 456 759 C
ATOM 1932 N GLN A 244 17.458 420.952 47.329 1.00 96.89 N
ANISOU 1932 N GLN A 244 12825 8755 15233 1696 319 236 N
ATOM 1933 CA GLN A 244 18.668 420.619 48.074 1.00108.10 C
ANISOU 1933 CA GLN A 244 14253 10127 16695 1532 218 125 C
ATOM 1934 C GLN A 244 18.571 419.227 48.689 1.00105.77 C
ANISOU 1934 C GLN A 244 13881 10106 16201 1527 249 55 C
ATOM 1935 O GLN A 244 19.543 418.466 48.656 1.00103.37 O
ANISOU 1935 O GLN A 244 13489 9872 15915 1364 213 72 O
ATOM 1936 CB GLN A 244 18.947 421.694 49.127 1.00107.28 C
ANISOU 1936 CB GLN A 244 14330 9749 16681 1572 82 -67 C
ATOM 1937 CG GLN A 244 18.919 423.095 48.544 1.00 95.99 C
ANISOU 1937 CG GLN A 244 12985 8029 15456 1593 60 4 C
ATOM 1938 CD GLN A 244 19.775 423.211 47.283 1.00 97.80 C
ANISOU 1938 CD GLN A 244 13103 8184 15873 1408 98 225 C
ATOM 1939 OE1 GLN A 244 19.362 423.817 46.298 1.00102.62 O
ANISOU 1939 OE1 GLN A 244 13725 8717 16549 1458 176 393 O
ATOM 1940 NE2 GLN A 244 21.008 422.713 47.351 1.00 95.30 N
ANISOU 1940 NE2 GLN A 244 12691 7863 15655 1201 42 225 N
ATOM 1941 N LYS A 245 17.413 418.881 49.267 1.00108.09 N
ANISOU 1941 N LYS A 245 14203 10547 16321 1707 325 -20 N
ATOM 1942 CA LYS A 245 17.222 417.533 49.807 1.00106.97 C
ANISOU 1942 CA LYS A 245 13988 10658 15996 1709 382 -62 C
ATOM 1943 C LYS A 245 17.342 416.480 48.712 1.00 93.30 C
ANISOU 1943 C LYS A 245 12066 9130 14253 1598 453 110 C
ATOM 1944 O LYS A 245 18.044 415.476 48.875 1.00 92.15 O
ANISOU 1944 O LYS A 245 11850 9105 14056 1477 438 106 O
ATOM 1945 CB LYS A 245 15.866 417.414 50.505 1.00115.29 C
ANISOU 1945 CB LYS A 245 15086 11818 16902 1927 493 -141 C
ATOM 1946 CG LYS A 245 15.879 417.772 51.987 1.00133.15 C
ANISOU 1946 CG LYS A 245 17549 13982 19059 2035 448 -350 C
ATOM 1947 CD LYS A 245 14.455 417.872 52.534 1.00145.71 C
ANISOU 1947 CD LYS A 245 19181 15646 20537 2275 600 -403 C
ATOM 1948 CE LYS A 245 14.340 418.950 53.613 1.00150.24 C
ANISOU 1948 CE LYS A 245 20004 16006 21073 2431 550 -592 C
ATOM 1949 NZ LYS A 245 12.929 419.185 54.030 1.00149.23 N
ANISOU 1949 NZ LYS A 245 19903 15929 20868 2682 726 -628 N
ATOM 1950 N ALA A 246 16.702 416.720 47.564 1.00 78.82 N
ANISOU 1950 N ALA A 246 10160 7324 12463 1644 517 258 N
ATOM 1951 CA ALA A 246 16.800 415.776 46.455 1.00 75.29 C
ANISOU 1951 CA ALA A 246 9562 7055 11988 1557 571 411 C
ATOM 1952 C ALA A 246 18.240 415.637 45.973 1.00 93.44 C
ANISOU 1952 C ALA A 246 11831 9288 14384 1355 528 481 C
ATOM 1953 O ALA A 246 18.715 414.522 45.725 1.00102.45 O
ANISOU 1953 O ALA A 246 12868 10588 15469 1254 553 520 O
ATOM 1954 CB ALA A 246 15.898 416.220 45.309 1.00 62.89 C
ANISOU 1954 CB ALA A 246 7960 5492 10442 1663 612 548 C
ATOM 1955 N GLU A 247 18.945 416.760 45.820 1.00 95.91 N
ANISOU 1955 N GLU A 247 12223 9354 14863 1296 472 501 N
ATOM 1956 CA GLU A 247 20.348 416.715 45.421 1.00 88.79 C
ANISOU 1956 CA GLU A 247 11270 8362 14102 1101 446 570 C
ATOM 1957 C GLU A 247 21.172 415.863 46.379 1.00 86.90 C
ANISOU 1957 C GLU A 247 10987 8195 13838 998 374 442 C
ATOM 1958 O GLU A 247 21.938 414.994 45.947 1.00 88.60 O
ANISOU 1958 O GLU A 247 11086 8516 14064 873 402 512 O
ATOM 1959 CB GLU A 247 20.907 418.136 45.350 1.00 98.06 C
ANISOU 1959 CB GLU A 247 12538 9226 15496 1057 389 584 C
ATOM 1960 CG GLU A 247 22.390 418.222 45.044 1.00100.24 C
ANISOU 1960 CG GLU A 247 12739 9368 15979 848 366 649 C
ATOM 1961 CD GLU A 247 23.217 418.355 46.307 1.00103.85 C
ANISOU 1961 CD GLU A 247 13219 9699 16540 765 203 453 C
ATOM 1962 OE1 GLU A 247 22.912 419.258 47.122 1.00 97.86 O
ANISOU 1962 OE1 GLU A 247 12599 8763 15818 844 98 310 O
ATOM 1963 OE2 GLU A 247 24.163 417.551 46.483 1.00101.17 O
ANISOU 1963 OE2 GLU A 247 12767 9433 16240 632 169 436 O
ATOM 1964 N LYS A 248 21.040 416.110 47.687 1.00 90.22 N
ANISOU 1964 N LYS A 248 11513 8551 14214 1063 276 252 N
ATOM 1965 CA LYS A 248 21.810 415.351 48.669 1.00 96.42 C
ANISOU 1965 CA LYS A 248 12289 9391 14956 988 180 124 C
ATOM 1966 C LYS A 248 21.537 413.853 48.571 1.00102.83 C
ANISOU 1966 C LYS A 248 12993 10485 15591 987 267 165 C
ATOM 1967 O LYS A 248 22.450 413.035 48.726 1.00107.18 O
ANISOU 1967 O LYS A 248 13466 11100 16156 871 223 158 O
ATOM 1968 CB LYS A 248 21.488 415.848 50.082 1.00 97.55 C
ANISOU 1968 CB LYS A 248 12612 9436 15016 1107 73 -86 C
ATOM 1969 CG LYS A 248 22.178 417.140 50.515 1.00110.50 C
ANISOU 1969 CG LYS A 248 14367 10768 16849 1066 -88 -191 C
ATOM 1970 CD LYS A 248 21.954 417.377 52.013 1.00121.95 C
ANISOU 1970 CD LYS A 248 16020 12154 18163 1193 -210 -425 C
ATOM 1971 CE LYS A 248 22.443 418.745 52.475 1.00122.31 C
ANISOU 1971 CE LYS A 248 16208 11874 18389 1183 -386 -557 C
ATOM 1972 NZ LYS A 248 22.236 418.949 53.944 1.00123.70 N
ANISOU 1972 NZ LYS A 248 16617 11988 18395 1329 -516 -801 N
ATOM 1973 N GLU A 249 20.301 413.473 48.273 1.00100.84 N
ANISOU 1973 N GLU A 249 12724 10393 15199 1113 386 213 N
ATOM 1974 CA GLU A 249 19.985 412.052 48.270 1.00 96.76 C
ANISOU 1974 CA GLU A 249 12108 10121 14533 1112 460 238 C
ATOM 1975 C GLU A 249 20.366 411.382 46.950 1.00 93.81 C
ANISOU 1975 C GLU A 249 11591 9852 14199 1007 523 400 C
ATOM 1976 O GLU A 249 20.796 410.222 46.957 1.00101.51 O
ANISOU 1976 O GLU A 249 12483 10969 15119 933 538 411 O
ATOM 1977 CB GLU A 249 18.514 411.875 48.664 1.00 99.08 C
ANISOU 1977 CB GLU A 249 12428 10530 14688 1287 553 202 C
ATOM 1978 CG GLU A 249 17.479 412.161 47.604 1.00119.70 C
ANISOU 1978 CG GLU A 249 14972 13185 17322 1372 634 317 C
ATOM 1979 CD GLU A 249 16.083 412.333 48.208 1.00141.65 C
ANISOU 1979 CD GLU A 249 17780 16013 20027 1559 709 253 C
ATOM 1980 OE1 GLU A 249 15.990 412.600 49.428 1.00144.54 O
ANISOU 1980 OE1 GLU A 249 18267 16321 20332 1635 704 119 O
ATOM 1981 OE2 GLU A 249 15.082 412.241 47.464 1.00149.10 O
ANISOU 1981 OE2 GLU A 249 18629 17042 20980 1639 770 334 O
ATOM 1982 N VAL A 250 20.252 412.087 45.822 1.00 83.18 N
ANISOU 1982 N VAL A 250 10234 8431 12940 1007 562 526 N
ATOM 1983 CA VAL A 250 20.814 411.580 44.572 1.00 73.30 C
ANISOU 1983 CA VAL A 250 8888 7245 11719 911 624 678 C
ATOM 1984 C VAL A 250 22.313 411.368 44.721 1.00 79.43 C
ANISOU 1984 C VAL A 250 9611 7950 12620 746 584 675 C
ATOM 1985 O VAL A 250 22.862 410.349 44.283 1.00 87.51 O
ANISOU 1985 O VAL A 250 10536 9098 13616 668 628 729 O
ATOM 1986 CB VAL A 250 20.491 412.522 43.402 1.00 80.27 C
ANISOU 1986 CB VAL A 250 9811 8027 12660 957 671 820 C
ATOM 1987 CG1 VAL A 250 21.277 412.120 42.158 1.00 79.18 C
ANISOU 1987 CG1 VAL A 250 9613 7924 12549 859 749 980 C
ATOM 1988 CG2 VAL A 250 19.008 412.504 43.120 1.00 69.56 C
ANISOU 1988 CG2 VAL A 250 8467 6775 11186 1123 695 831 C
ATOM 1989 N THR A 251 23.012 412.375 45.250 1.00 88.25 N
ANISOU 1989 N THR A 251 10783 8848 13900 692 498 618 N
ATOM 1990 CA THR A 251 24.454 412.253 45.429 1.00 90.83 C
ANISOU 1990 CA THR A 251 11031 9084 14396 532 439 608 C
ATOM 1991 C THR A 251 24.780 411.060 46.320 1.00 85.45 C
ANISOU 1991 C THR A 251 10303 8550 13614 508 373 495 C
ATOM 1992 O THR A 251 25.586 410.196 45.955 1.00 74.00 O
ANISOU 1992 O THR A 251 8733 7183 12202 412 403 550 O
ATOM 1993 CB THR A 251 25.017 413.550 46.016 1.00 87.40 C
ANISOU 1993 CB THR A 251 10667 8374 14169 486 318 530 C
ATOM 1994 OG1 THR A 251 24.725 414.623 45.122 1.00 90.04 O
ANISOU 1994 OG1 THR A 251 11048 8562 14601 508 396 657 O
ATOM 1995 CG2 THR A 251 26.526 413.469 46.151 1.00 83.87 C
ANISOU 1995 CG2 THR A 251 10102 7815 13950 312 243 522 C
ATOM 1996 N ARG A 252 24.106 410.966 47.472 1.00 91.58 N
ANISOU 1996 N ARG A 252 11184 9363 14248 613 300 348 N
ATOM 1997 CA ARG A 252 24.382 409.888 48.417 1.00 99.64 C
ANISOU 1997 CA ARG A 252 12197 10506 15155 609 235 246 C
ATOM 1998 C ARG A 252 24.074 408.523 47.813 1.00 94.81 C
ANISOU 1998 C ARG A 252 11481 10126 14416 606 355 336 C
ATOM 1999 O ARG A 252 24.758 407.539 48.118 1.00 97.01 O
ANISOU 1999 O ARG A 252 11696 10487 14678 544 320 315 O
ATOM 2000 CB ARG A 252 23.629 410.128 49.726 1.00106.85 C
ANISOU 2000 CB ARG A 252 13278 11406 15915 746 169 87 C
ATOM 2001 CG ARG A 252 24.301 409.442 50.903 1.00127.80 C
ANISOU 2001 CG ARG A 252 15978 14083 18496 732 38 -40 C
ATOM 2002 CD ARG A 252 23.525 409.557 52.209 1.00144.03 C
ANISOU 2002 CD ARG A 252 18232 16144 20350 891 4 -186 C
ATOM 2003 NE ARG A 252 23.988 408.610 53.227 1.00160.71 N
ANISOU 2003 NE ARG A 252 20403 18333 22327 904 -84 -273 N
ATOM 2004 CZ ARG A 252 25.230 408.513 53.707 1.00173.22 C
ANISOU 2004 CZ ARG A 252 21983 19830 24002 817 -280 -348 C
ATOM 2005 NH1 ARG A 252 25.496 407.603 54.636 1.00179.39 N
ANISOU 2005 NH1 ARG A 252 22840 20694 24625 859 -354 -417 N
ATOM 2006 NH2 ARG A 252 26.213 409.293 53.273 1.00174.89 N
ANISOU 2006 NH2 ARG A 252 22109 19867 24474 690 -402 -350 N
ATOM 2007 N MET A 253 23.077 408.453 46.931 1.00 91.88 N
ANISOU 2007 N MET A 253 11091 9850 13970 673 479 433 N
ATOM 2008 CA MET A 253 22.731 407.185 46.298 1.00 83.99 C
ANISOU 2008 CA MET A 253 9998 9053 12862 672 573 507 C
ATOM 2009 C MET A 253 23.747 406.790 45.234 1.00 82.57 C
ANISOU 2009 C MET A 253 9711 8884 12778 555 618 620 C
ATOM 2010 O MET A 253 24.091 405.611 45.106 1.00 89.56 O
ANISOU 2010 O MET A 253 10519 9896 13612 514 644 633 O
ATOM 2011 CB MET A 253 21.337 407.285 45.683 1.00 85.67 C
ANISOU 2011 CB MET A 253 10220 9347 12983 786 657 560 C
ATOM 2012 CG MET A 253 20.243 406.772 46.587 1.00100.95 C
ANISOU 2012 CG MET A 253 12183 11388 14787 893 680 476 C
ATOM 2013 SD MET A 253 20.424 405.001 46.910 1.00111.17 S
ANISOU 2013 SD MET A 253 13395 12866 15980 842 710 463 S
ATOM 2014 CE MET A 253 19.822 404.956 48.592 1.00110.89 C
ANISOU 2014 CE MET A 253 13472 12831 15832 946 708 334 C
ATOM 2015 N VAL A 254 24.240 407.754 44.460 1.00 85.83 N
ANISOU 2015 N VAL A 254 10123 9158 13332 509 644 709 N
ATOM 2016 CA VAL A 254 25.273 407.441 43.477 1.00 86.55 C
ANISOU 2016 CA VAL A 254 10116 9244 13523 406 720 827 C
ATOM 2017 C VAL A 254 26.514 406.928 44.190 1.00 82.89 C
ANISOU 2017 C VAL A 254 9565 8753 13177 298 643 760 C
ATOM 2018 O VAL A 254 27.193 406.003 43.724 1.00 84.92 O
ANISOU 2018 O VAL A 254 9720 9098 13448 241 701 811 O
ATOM 2019 CB VAL A 254 25.580 408.675 42.605 1.00 83.75 C
ANISOU 2019 CB VAL A 254 9790 8718 13314 379 782 949 C
ATOM 2020 CG1 VAL A 254 26.932 408.517 41.883 1.00 88.43 C
ANISOU 2020 CG1 VAL A 254 10272 9255 14073 253 870 1059 C
ATOM 2021 CG2 VAL A 254 24.457 408.922 41.621 1.00 75.94 C
ANISOU 2021 CG2 VAL A 254 8878 7787 12187 493 864 1046 C
ATOM 2022 N ILE A 255 26.845 407.548 45.317 1.00 80.35 N
ANISOU 2022 N ILE A 255 9285 8299 12945 280 499 638 N
ATOM 2023 CA ILE A 255 28.008 407.131 46.082 1.00 80.92 C
ANISOU 2023 CA ILE A 255 9280 8330 13138 191 379 557 C
ATOM 2024 C ILE A 255 27.861 405.680 46.530 1.00 88.60 C
ANISOU 2024 C ILE A 255 10231 9497 13937 226 371 509 C
ATOM 2025 O ILE A 255 28.794 404.877 46.399 1.00 88.87 O
ANISOU 2025 O ILE A 255 10146 9573 14046 154 368 531 O
ATOM 2026 CB ILE A 255 28.182 408.090 47.272 1.00 77.38 C
ANISOU 2026 CB ILE A 255 8925 7703 12771 196 192 408 C
ATOM 2027 CG1 ILE A 255 28.690 409.443 46.766 1.00 79.87 C
ANISOU 2027 CG1 ILE A 255 9219 7789 13338 119 191 466 C
ATOM 2028 CG2 ILE A 255 29.125 407.490 48.293 1.00 72.31 C
ANISOU 2028 CG2 ILE A 255 8242 7053 12181 148 19 289 C
ATOM 2029 CD1 ILE A 255 28.958 410.447 47.849 1.00 77.94 C
ANISOU 2029 CD1 ILE A 255 9066 7336 13212 112 -13 311 C
ATOM 2030 N ILE A 256 26.667 405.308 47.011 1.00 87.07 N
ANISOU 2030 N ILE A 256 10141 9416 13524 339 386 456 N
ATOM 2031 CA ILE A 256 26.417 403.931 47.444 1.00 79.58 C
ANISOU 2031 CA ILE A 256 9183 8637 12416 373 397 425 C
ATOM 2032 C ILE A 256 26.552 402.959 46.281 1.00 80.84 C
ANISOU 2032 C ILE A 256 9229 8925 12563 336 524 540 C
ATOM 2033 O ILE A 256 27.142 401.880 46.415 1.00 73.40 O
ANISOU 2033 O ILE A 256 8219 8059 11612 301 513 534 O
ATOM 2034 CB ILE A 256 25.020 403.819 48.086 1.00 70.94 C
ANISOU 2034 CB ILE A 256 8207 7624 11123 500 427 370 C
ATOM 2035 CG1 ILE A 256 25.025 404.419 49.482 1.00 67.10 C
ANISOU 2035 CG1 ILE A 256 7862 7037 10596 558 298 232 C
ATOM 2036 CG2 ILE A 256 24.524 402.366 48.110 1.00 64.56 C
ANISOU 2036 CG2 ILE A 256 7363 6995 10170 528 501 390 C
ATOM 2037 CD1 ILE A 256 23.654 404.668 49.989 1.00 74.26 C
ANISOU 2037 CD1 ILE A 256 8885 7985 11346 693 365 192 C
ATOM 2038 N MET A 257 26.041 403.342 45.112 1.00 81.66 N
ANISOU 2038 N MET A 257 9324 9042 12660 352 638 642 N
ATOM 2039 CA MET A 257 26.078 402.440 43.971 1.00 78.38 C
ANISOU 2039 CA MET A 257 8839 8745 12197 340 752 738 C
ATOM 2040 C MET A 257 27.501 402.240 43.496 1.00 82.38 C
ANISOU 2040 C MET A 257 9236 9203 12862 242 783 795 C
ATOM 2041 O MET A 257 27.919 401.109 43.215 1.00 94.76 O
ANISOU 2041 O MET A 257 10735 10869 14400 224 824 811 O
ATOM 2042 CB MET A 257 25.227 403.011 42.849 1.00 81.06 C
ANISOU 2042 CB MET A 257 9224 9094 12480 400 840 830 C
ATOM 2043 CG MET A 257 23.771 402.790 43.054 1.00 89.67 C
ANISOU 2043 CG MET A 257 10368 10279 13422 501 831 789 C
ATOM 2044 SD MET A 257 22.835 403.809 41.923 1.00102.37 S
ANISOU 2044 SD MET A 257 12043 11853 15001 586 879 882 S
ATOM 2045 CE MET A 257 21.195 403.558 42.636 1.00110.87 C
ANISOU 2045 CE MET A 257 13137 13022 15968 699 842 795 C
ATOM 2046 N VAL A 258 28.252 403.338 43.390 1.00 77.28 N
ANISOU 2046 N VAL A 258 8564 8394 12403 179 773 829 N
ATOM 2047 CA VAL A 258 29.625 403.277 42.912 1.00 77.67 C
ANISOU 2047 CA VAL A 258 8482 8376 12654 80 826 898 C
ATOM 2048 C VAL A 258 30.501 402.518 43.902 1.00 84.56 C
ANISOU 2048 C VAL A 258 9264 9257 13608 32 699 800 C
ATOM 2049 O VAL A 258 31.373 401.735 43.507 1.00 86.67 O
ANISOU 2049 O VAL A 258 9409 9566 13956 -10 758 842 O
ATOM 2050 CB VAL A 258 30.125 404.701 42.638 1.00 78.69 C
ANISOU 2050 CB VAL A 258 8599 8304 12997 18 843 960 C
ATOM 2051 CG1 VAL A 258 31.608 404.714 42.409 1.00 86.96 C
ANISOU 2051 CG1 VAL A 258 9474 9252 14314 -98 882 1015 C
ATOM 2052 CG2 VAL A 258 29.401 405.246 41.428 1.00 74.54 C
ANISOU 2052 CG2 VAL A 258 8161 7784 12375 77 996 1093 C
ATOM 2053 N ILE A 259 30.270 402.720 45.204 1.00 87.41 N
ANISOU 2053 N ILE A 259 9696 9580 13937 55 523 666 N
ATOM 2054 CA ILE A 259 31.070 402.026 46.207 1.00 83.52 C
ANISOU 2054 CA ILE A 259 9148 9089 13497 30 373 569 C
ATOM 2055 C ILE A 259 30.714 400.545 46.194 1.00 86.38 C
ANISOU 2055 C ILE A 259 9514 9633 13673 84 424 571 C
ATOM 2056 O ILE A 259 31.581 399.673 46.309 1.00 91.03 O
ANISOU 2056 O ILE A 259 10001 10253 14332 54 394 566 O
ATOM 2057 CB ILE A 259 30.822 402.630 47.603 1.00 81.92 C
ANISOU 2057 CB ILE A 259 9071 8798 13255 68 170 423 C
ATOM 2058 CG1 ILE A 259 31.452 404.019 47.754 1.00 80.44 C
ANISOU 2058 CG1 ILE A 259 8860 8394 13308 -4 69 393 C
ATOM 2059 CG2 ILE A 259 31.299 401.658 48.694 1.00 73.92 C
ANISOU 2059 CG2 ILE A 259 8066 7835 12184 92 16 323 C
ATOM 2060 CD1 ILE A 259 32.888 404.098 47.348 1.00 93.24 C
ANISOU 2060 CD1 ILE A 259 10274 9911 15240 -129 52 442 C
ATOM 2061 N ALA A 260 29.423 400.242 46.054 1.00 89.51 N
ANISOU 2061 N ALA A 260 10020 10140 13851 165 498 578 N
ATOM 2062 CA ALA A 260 28.993 398.858 45.917 1.00 82.27 C
ANISOU 2062 CA ALA A 260 9101 9377 12781 207 559 588 C
ATOM 2063 C ALA A 260 29.630 398.206 44.703 1.00 85.54 C
ANISOU 2063 C ALA A 260 9401 9841 13259 168 685 682 C
ATOM 2064 O ALA A 260 30.101 397.066 44.780 1.00 94.25 O
ANISOU 2064 O ALA A 260 10447 11010 14353 166 685 673 O
ATOM 2065 CB ALA A 260 27.469 398.784 45.818 1.00 62.75 C
ANISOU 2065 CB ALA A 260 6731 6993 10119 288 624 589 C
ATOM 2066 N PHE A 261 29.678 398.924 43.579 1.00 80.99 N
ANISOU 2066 N PHE A 261 8805 9226 12743 150 801 776 N
ATOM 2067 CA PHE A 261 30.273 398.352 42.379 1.00 80.03 C
ANISOU 2067 CA PHE A 261 8604 9148 12655 134 947 870 C
ATOM 2068 C PHE A 261 31.760 398.130 42.590 1.00 90.91 C
ANISOU 2068 C PHE A 261 9830 10459 14251 62 929 874 C
ATOM 2069 O PHE A 261 32.319 397.132 42.124 1.00 88.27 O
ANISOU 2069 O PHE A 261 9421 10190 13926 68 1005 901 O
ATOM 2070 CB PHE A 261 30.025 399.274 41.188 1.00 73.14 C
ANISOU 2070 CB PHE A 261 7773 8233 11784 145 1081 981 C
ATOM 2071 CG PHE A 261 30.586 398.774 39.887 1.00 72.63 C
ANISOU 2071 CG PHE A 261 7669 8210 11718 153 1257 1086 C
ATOM 2072 CD1 PHE A 261 29.826 397.950 39.075 1.00 78.62 C
ANISOU 2072 CD1 PHE A 261 8510 9095 12268 232 1321 1100 C
ATOM 2073 CD2 PHE A 261 31.850 399.138 39.461 1.00 82.11 C
ANISOU 2073 CD2 PHE A 261 8753 9316 13128 88 1362 1169 C
ATOM 2074 CE1 PHE A 261 30.311 397.489 37.866 1.00 82.94 C
ANISOU 2074 CE1 PHE A 261 9058 9679 12776 262 1483 1185 C
ATOM 2075 CE2 PHE A 261 32.349 398.673 38.248 1.00 89.94 C
ANISOU 2075 CE2 PHE A 261 9727 10349 14098 117 1558 1272 C
ATOM 2076 CZ PHE A 261 31.573 397.847 37.451 1.00 88.42 C
ANISOU 2076 CZ PHE A 261 9652 10287 13656 212 1616 1276 C
ATOM 2077 N LEU A 262 32.418 399.055 43.291 1.00 94.62 N
ANISOU 2077 N LEU A 262 10246 10791 14915 -1 819 840 N
ATOM 2078 CA LEU A 262 33.837 398.881 43.559 1.00 94.57 C
ANISOU 2078 CA LEU A 262 10066 10708 15159 -73 770 834 C
ATOM 2079 C LEU A 262 34.077 397.749 44.546 1.00 98.74 C
ANISOU 2079 C LEU A 262 10579 11304 15634 -43 623 734 C
ATOM 2080 O LEU A 262 35.083 397.041 44.433 1.00110.25 O
ANISOU 2080 O LEU A 262 11892 12767 17231 -64 634 749 O
ATOM 2081 CB LEU A 262 34.424 400.173 44.118 1.00 91.68 C
ANISOU 2081 CB LEU A 262 9645 10157 15032 -152 650 804 C
ATOM 2082 CG LEU A 262 34.643 401.314 43.138 1.00 79.92 C
ANISOU 2082 CG LEU A 262 8117 8550 13701 -209 805 927 C
ATOM 2083 CD1 LEU A 262 34.985 402.561 43.931 1.00 78.34 C
ANISOU 2083 CD1 LEU A 262 7898 8154 13713 -281 635 861 C
ATOM 2084 CD2 LEU A 262 35.717 400.958 42.121 1.00 69.84 C
ANISOU 2084 CD2 LEU A 262 6662 7264 12611 -255 1003 1053 C
ATOM 2085 N ILE A 263 33.155 397.540 45.494 1.00 96.77 N
ANISOU 2085 N ILE A 263 10480 11105 15183 17 501 644 N
ATOM 2086 CA ILE A 263 33.327 396.448 46.450 1.00 98.22 C
ANISOU 2086 CA ILE A 263 10682 11348 15291 58 374 566 C
ATOM 2087 C ILE A 263 33.334 395.131 45.697 1.00 93.10 C
ANISOU 2087 C ILE A 263 9990 10819 14567 88 510 622 C
ATOM 2088 O ILE A 263 34.000 394.171 46.098 1.00 92.79 O
ANISOU 2088 O ILE A 263 9888 10801 14568 102 446 597 O
ATOM 2089 CB ILE A 263 32.263 396.513 47.567 1.00 89.75 C
ANISOU 2089 CB ILE A 263 9800 10301 14001 128 264 479 C
ATOM 2090 CG1 ILE A 263 32.658 397.588 48.581 1.00 90.71 C
ANISOU 2090 CG1 ILE A 263 9962 10283 14219 111 67 387 C
ATOM 2091 CG2 ILE A 263 32.117 395.198 48.281 1.00 75.49 C
ANISOU 2091 CG2 ILE A 263 8050 8583 12049 189 212 443 C
ATOM 2092 CD1 ILE A 263 31.573 397.948 49.552 1.00 93.91 C
ANISOU 2092 CD1 ILE A 263 10576 10696 14411 193 0 308 C
ATOM 2093 N CYS A 264 32.555 395.048 44.630 1.00 89.22 N
ANISOU 2093 N CYS A 264 9545 10400 13955 110 681 691 N
ATOM 2094 CA CYS A 264 32.611 393.892 43.757 1.00 90.19 C
ANISOU 2094 CA CYS A 264 9635 10617 14017 141 811 736 C
ATOM 2095 C CYS A 264 33.828 393.960 42.834 1.00 99.71 C
ANISOU 2095 C CYS A 264 10688 11780 15419 104 934 812 C
ATOM 2096 O CYS A 264 34.426 392.927 42.507 1.00111.31 O
ANISOU 2096 O CYS A 264 12084 13291 16918 127 991 823 O
ATOM 2097 CB CYS A 264 31.327 393.800 42.948 1.00 92.36 C
ANISOU 2097 CB CYS A 264 10026 10975 14092 187 918 766 C
ATOM 2098 SG CYS A 264 31.300 392.372 41.935 1.00101.20 S
ANISOU 2098 SG CYS A 264 11140 12195 15116 233 1040 792 S
ATOM 2099 N TRP A 265 34.184 395.168 42.376 1.00 95.68 N
ANISOU 2099 N TRP A 265 10129 11176 15050 52 996 874 N
ATOM 2100 CA TRP A 265 35.149 395.317 41.287 1.00 96.06 C
ANISOU 2100 CA TRP A 265 10049 11186 15264 26 1183 979 C
ATOM 2101 C TRP A 265 36.593 395.286 41.774 1.00104.89 C
ANISOU 2101 C TRP A 265 10954 12212 16688 -35 1122 970 C
ATOM 2102 O TRP A 265 37.449 394.667 41.129 1.00100.05 O
ANISOU 2102 O TRP A 265 10213 11613 16187 -24 1260 1025 O
ATOM 2103 CB TRP A 265 34.857 396.617 40.527 1.00 90.62 C
ANISOU 2103 CB TRP A 265 9410 10425 14597 0 1300 1073 C
ATOM 2104 CG TRP A 265 35.701 396.868 39.307 1.00 92.93 C
ANISOU 2104 CG TRP A 265 9610 10674 15025 -13 1541 1210 C
ATOM 2105 CD1 TRP A 265 35.385 396.583 38.005 1.00 88.25 C
ANISOU 2105 CD1 TRP A 265 9115 10152 14262 61 1754 1302 C
ATOM 2106 CD2 TRP A 265 36.966 397.541 39.272 1.00 96.33 C
ANISOU 2106 CD2 TRP A 265 9843 10965 15793 -102 1604 1277 C
ATOM 2107 NE1 TRP A 265 36.400 396.991 37.167 1.00 83.26 N
ANISOU 2107 NE1 TRP A 265 8372 9443 13819 35 1972 1432 N
ATOM 2108 CE2 TRP A 265 37.379 397.588 37.920 1.00 92.07 C
ANISOU 2108 CE2 TRP A 265 9288 10426 15270 -73 1893 1425 C
ATOM 2109 CE3 TRP A 265 37.802 398.090 40.255 1.00 89.38 C
ANISOU 2109 CE3 TRP A 265 8796 9953 15213 -199 1436 1223 C
ATOM 2110 CZ2 TRP A 265 38.590 398.160 37.532 1.00 93.04 C
ANISOU 2110 CZ2 TRP A 265 9214 10420 15717 -146 2052 1536 C
ATOM 2111 CZ3 TRP A 265 38.997 398.660 39.865 1.00 89.00 C
ANISOU 2111 CZ3 TRP A 265 8536 9771 15508 -281 1559 1318 C
ATOM 2112 CH2 TRP A 265 39.380 398.693 38.516 1.00 93.12 C
ANISOU 2112 CH2 TRP A 265 9027 10295 16058 -259 1881 1481 C
ATOM 2113 N LEU A 266 36.884 395.961 42.889 1.00107.77 N
ANISOU 2113 N LEU A 266 11276 12476 17197 -92 911 894 N
ATOM 2114 CA LEU A 266 38.266 396.068 43.352 1.00104.11 C
ANISOU 2114 CA LEU A 266 10589 11903 17065 -157 815 877 C
ATOM 2115 C LEU A 266 38.909 394.738 43.735 1.00117.74 C
ANISOU 2115 C LEU A 266 12223 13693 18821 -109 746 831 C
ATOM 2116 O LEU A 266 40.121 394.592 43.501 1.00122.82 O
ANISOU 2116 O LEU A 266 12640 14277 19750 -142 789 868 O
ATOM 2117 CB LEU A 266 38.367 397.058 44.520 1.00 98.60 C
ANISOU 2117 CB LEU A 266 9897 11075 16491 -215 556 780 C
ATOM 2118 CG LEU A 266 38.280 398.543 44.166 1.00 98.57 C
ANISOU 2118 CG LEU A 266 9892 10936 16622 -293 609 832 C
ATOM 2119 CD1 LEU A 266 38.047 399.421 45.397 1.00 91.27 C
ANISOU 2119 CD1 LEU A 266 9054 9900 15725 -319 332 703 C
ATOM 2120 CD2 LEU A 266 39.562 398.942 43.454 1.00 90.37 C
ANISOU 2120 CD2 LEU A 266 8596 9780 15961 -383 747 936 C
ATOM 2121 N PRO A 267 38.216 393.771 44.364 1.00114.73 N
ANISOU 2121 N PRO A 267 11988 13414 18189 -32 640 756 N
ATOM 2122 CA PRO A 267 38.883 392.483 44.609 1.00101.53 C
ANISOU 2122 CA PRO A 267 10229 11789 16560 20 596 730 C
ATOM 2123 C PRO A 267 39.461 391.852 43.352 1.00102.89 C
ANISOU 2123 C PRO A 267 10280 12002 16811 45 852 824 C
ATOM 2124 O PRO A 267 40.610 391.402 43.388 1.00106.31 O
ANISOU 2124 O PRO A 267 10514 12397 17482 47 843 830 O
ATOM 2125 CB PRO A 267 37.772 391.643 45.250 1.00 92.46 C
ANISOU 2125 CB PRO A 267 9299 10740 15092 96 510 667 C
ATOM 2126 CG PRO A 267 36.970 392.637 45.971 1.00 89.29 C
ANISOU 2126 CG PRO A 267 9040 10301 14584 74 387 617 C
ATOM 2127 CD PRO A 267 36.940 393.855 45.096 1.00 99.36 C
ANISOU 2127 CD PRO A 267 10271 11517 15964 7 526 686 C
ATOM 2128 N TYR A 268 38.736 391.848 42.231 1.00102.06 N
ANISOU 2128 N TYR A 268 10289 11967 16522 73 1075 893 N
ATOM 2129 CA TYR A 268 39.328 391.375 40.979 1.00103.83 C
ANISOU 2129 CA TYR A 268 10426 12219 16807 111 1336 983 C
ATOM 2130 C TYR A 268 40.563 392.191 40.616 1.00 97.28 C
ANISOU 2130 C TYR A 268 9358 11274 16330 41 1445 1066 C
ATOM 2131 O TYR A 268 41.571 391.641 40.161 1.00 86.71 O
ANISOU 2131 O TYR A 268 7845 9925 15177 68 1577 1110 O
ATOM 2132 CB TYR A 268 38.290 391.379 39.868 1.00105.57 C
ANISOU 2132 CB TYR A 268 10842 12521 16748 161 1522 1035 C
ATOM 2133 CG TYR A 268 37.238 390.344 40.109 1.00 97.92 C
ANISOU 2133 CG TYR A 268 10051 11656 15499 229 1437 956 C
ATOM 2134 CD1 TYR A 268 36.048 390.673 40.733 1.00106.38 C
ANISOU 2134 CD1 TYR A 268 11276 12752 16390 216 1297 903 C
ATOM 2135 CD2 TYR A 268 37.422 389.042 39.671 1.00 88.79 C
ANISOU 2135 CD2 TYR A 268 8904 10560 14272 307 1512 939 C
ATOM 2136 CE1 TYR A 268 35.072 389.720 40.951 1.00107.14 C
ANISOU 2136 CE1 TYR A 268 11511 12930 16267 267 1236 842 C
ATOM 2137 CE2 TYR A 268 36.454 388.085 39.870 1.00101.28 C
ANISOU 2137 CE2 TYR A 268 10638 12214 15629 356 1435 870 C
ATOM 2138 CZ TYR A 268 35.278 388.429 40.514 1.00103.94 C
ANISOU 2138 CZ TYR A 268 11108 12573 15812 330 1301 827 C
ATOM 2139 OH TYR A 268 34.306 387.484 40.723 1.00 98.86 O
ANISOU 2139 OH TYR A 268 10591 11988 14983 368 1240 770 O
ATOM 2140 N ALA A 269 40.469 393.516 40.730 1.00112.77 N
ANISOU 2140 N ALA A 269 11310 13141 18396 -46 1417 1097 N
ATOM 2141 CA ALA A 269 41.585 394.382 40.357 1.00115.12 C
ANISOU 2141 CA ALA A 269 11374 13305 19060 -130 1534 1189 C
ATOM 2142 C ALA A 269 42.788 394.162 41.275 1.00114.73 C
ANISOU 2142 C ALA A 269 11063 13170 19359 -175 1339 1124 C
ATOM 2143 O ALA A 269 43.932 394.132 40.809 1.00114.36 O
ANISOU 2143 O ALA A 269 10765 13059 19630 -200 1486 1199 O
ATOM 2144 CB ALA A 269 41.147 395.847 40.370 1.00109.08 C
ANISOU 2144 CB ALA A 269 10674 12437 18334 -215 1516 1226 C
ATOM 2145 N GLY A 270 42.554 394.030 42.583 1.00113.43 N
ANISOU 2145 N GLY A 270 10954 12997 19147 -179 1008 986 N
ATOM 2146 CA GLY A 270 43.647 393.718 43.495 1.00117.20 C
ANISOU 2146 CA GLY A 270 11212 13401 19920 -198 777 910 C
ATOM 2147 C GLY A 270 44.315 392.394 43.168 1.00132.52 C
ANISOU 2147 C GLY A 270 13029 15414 21909 -109 874 928 C
ATOM 2148 O GLY A 270 45.544 392.297 43.129 1.00148.57 O
ANISOU 2148 O GLY A 270 14773 17370 24308 -132 883 952 O
ATOM 2149 N VAL A 271 43.513 391.352 42.943 1.00126.72 N
ANISOU 2149 N VAL A 271 12503 14818 20829 -6 942 913 N
ATOM 2150 CA VAL A 271 44.053 390.028 42.643 1.00114.42 C
ANISOU 2150 CA VAL A 271 10864 13323 19287 91 1028 919 C
ATOM 2151 C VAL A 271 44.781 390.038 41.298 1.00115.33 C
ANISOU 2151 C VAL A 271 10813 13429 19579 103 1383 1044 C
ATOM 2152 O VAL A 271 45.884 389.495 41.170 1.00128.71 O
ANISOU 2152 O VAL A 271 12268 15092 21543 138 1441 1065 O
ATOM 2153 CB VAL A 271 42.950 388.958 42.676 1.00103.04 C
ANISOU 2153 CB VAL A 271 9696 12011 17444 188 1021 872 C
ATOM 2154 CG1 VAL A 271 43.530 387.676 42.192 1.00105.09 C
ANISOU 2154 CG1 VAL A 271 9877 12315 17737 288 1145 885 C
ATOM 2155 CG2 VAL A 271 42.382 388.792 44.077 1.00 92.30 C
ANISOU 2155 CG2 VAL A 271 8481 10653 15934 195 698 763 C
ATOM 2156 N ALA A 272 44.185 390.673 40.282 1.00111.79 N
ANISOU 2156 N ALA A 272 10491 13003 18981 87 1631 1136 N
ATOM 2157 CA ALA A 272 44.805 390.769 38.960 1.00123.50 C
ANISOU 2157 CA ALA A 272 11864 14475 20585 113 2002 1272 C
ATOM 2158 C ALA A 272 46.157 391.463 39.027 1.00135.23 C
ANISOU 2158 C ALA A 272 12996 15817 22566 24 2052 1339 C
ATOM 2159 O ALA A 272 47.092 391.087 38.308 1.00135.59 O
ANISOU 2159 O ALA A 272 12847 15848 22824 70 2304 1423 O
ATOM 2160 CB ALA A 272 43.890 391.537 38.012 1.00131.30 C
ANISOU 2160 CB ALA A 272 13074 15490 21323 106 2206 1359 C
ATOM 2161 N PHE A 273 46.272 392.475 39.890 1.00143.31 N
ANISOU 2161 N PHE A 273 13931 16728 23792 -100 1814 1299 N
ATOM 2162 CA PHE A 273 47.538 393.168 40.125 1.00147.49 C
ANISOU 2162 CA PHE A 273 14102 17097 24842 -206 1789 1339 C
ATOM 2163 C PHE A 273 48.584 392.196 40.655 1.00157.38 C
ANISOU 2163 C PHE A 273 15100 18342 26355 -152 1656 1275 C
ATOM 2164 O PHE A 273 49.774 392.323 40.360 1.00163.45 O
ANISOU 2164 O PHE A 273 15690 19014 27399 -172 1738 1321 O
ATOM 2165 CB PHE A 273 47.337 394.317 41.112 1.00136.31 C
ANISOU 2165 CB PHE A 273 12687 15557 23547 -335 1478 1262 C
ATOM 2166 CG PHE A 273 48.598 395.092 41.423 1.00142.98 C
ANISOU 2166 CG PHE A 273 13170 16212 24946 -459 1398 1281 C
ATOM 2167 CD1 PHE A 273 49.207 395.878 40.451 1.00143.38 C
ANISOU 2167 CD1 PHE A 273 13165 16156 25156 -510 1687 1423 C
ATOM 2168 CD2 PHE A 273 49.164 395.055 42.691 1.00147.64 C
ANISOU 2168 CD2 PHE A 273 13604 16720 25773 -496 989 1135 C
ATOM 2169 CE1 PHE A 273 50.359 396.602 40.736 1.00140.57 C
ANISOU 2169 CE1 PHE A 273 12583 15613 25216 -606 1582 1420 C
ATOM 2170 CE2 PHE A 273 50.321 395.782 42.980 1.00147.89 C
ANISOU 2170 CE2 PHE A 273 13421 16565 26208 -590 862 1121 C
ATOM 2171 CZ PHE A 273 50.914 396.554 41.997 1.00142.28 C
ANISOU 2171 CZ PHE A 273 12636 15746 25677 -649 1167 1265 C
ATOM 2172 N TYR A 274 48.155 391.242 41.479 1.00157.01 N
ANISOU 2172 N TYR A 274 15200 18384 26072 -68 1394 1146 N
ATOM 2173 CA TYR A 274 49.054 390.238 42.033 1.00154.13 C
ANISOU 2173 CA TYR A 274 14633 18016 25912 5 1240 1082 C
ATOM 2174 C TYR A 274 49.581 389.392 40.856 1.00153.70 C
ANISOU 2174 C TYR A 274 14536 18021 25844 111 1605 1175 C
ATOM 2175 O TYR A 274 50.671 388.833 40.952 1.00156.95 O
ANISOU 2175 O TYR A 274 14777 18389 26468 154 1572 1160 O
ATOM 2176 CB TYR A 274 48.341 389.449 43.132 1.00147.67 C
ANISOU 2176 CB TYR A 274 14056 17275 24778 79 903 942 C
ATOM 2177 CG TYR A 274 49.261 388.787 44.154 1.00144.11 C
ANISOU 2177 CG TYR A 274 13409 16773 24573 127 590 850 C
ATOM 2178 CD1 TYR A 274 49.494 389.472 45.344 1.00143.88 C
ANISOU 2178 CD1 TYR A 274 13325 16641 24700 55 203 750 C
ATOM 2179 CD2 TYR A 274 49.901 387.571 43.973 1.00147.98 C
ANISOU 2179 CD2 TYR A 274 13778 17303 25144 249 651 855 C
ATOM 2180 CE1 TYR A 274 50.313 388.995 46.325 1.00151.25 C
ANISOU 2180 CE1 TYR A 274 14099 17517 25851 103 -130 659 C
ATOM 2181 CE2 TYR A 274 50.753 387.061 44.987 1.00155.36 C
ANISOU 2181 CE2 TYR A 274 14533 18177 26320 299 320 770 C
ATOM 2182 CZ TYR A 274 50.948 387.793 46.160 1.00158.17 C
ANISOU 2182 CZ TYR A 274 14845 18435 26816 225 -78 673 C
ATOM 2183 OH TYR A 274 51.766 387.345 47.184 1.00162.06 O
ANISOU 2183 OH TYR A 274 15183 18862 27529 284 -443 581 O
ATOM 2184 N ILE A 275 48.714 389.056 39.887 1.00148.74 N
ANISOU 2184 N ILE A 275 14121 17506 24888 185 1895 1238 N
ATOM 2185 CA ILE A 275 49.070 388.305 38.664 1.00149.55 C
ANISOU 2185 CA ILE A 275 14280 17665 24877 301 2247 1314 C
ATOM 2186 C ILE A 275 50.166 389.011 37.841 1.00176.31 C
ANISOU 2186 C ILE A 275 17533 20949 28510 252 2496 1431 C
ATOM 2187 O ILE A 275 51.019 388.349 37.240 1.00181.07 O
ANISOU 2187 O ILE A 275 18060 21551 29189 339 2682 1467 O
ATOM 2188 CB ILE A 275 47.857 387.931 37.781 1.00121.93 C
ANISOU 2188 CB ILE A 275 11082 14295 20951 389 2471 1342 C
ATOM 2189 CG1 ILE A 275 47.056 386.803 38.402 1.00113.95 C
ANISOU 2189 CG1 ILE A 275 10301 13377 19617 471 2235 1211 C
ATOM 2190 CG2 ILE A 275 48.294 387.519 36.353 1.00111.57 C
ANISOU 2190 CG2 ILE A 275 9828 13013 19550 499 2874 1440 C
ATOM 2191 CD1 ILE A 275 45.879 386.354 37.548 1.00111.65 C
ANISOU 2191 CD1 ILE A 275 10357 13197 18870 551 2388 1208 C
ATOM 2192 N PHE A 276 50.200 390.348 37.829 1.00190.18 N
ANISOU 2192 N PHE A 276 19245 22603 30413 119 2501 1494 N
ATOM 2193 CA PHE A 276 51.183 391.071 37.013 1.00203.34 C
ANISOU 2193 CA PHE A 276 20790 24154 32315 76 2759 1623 C
ATOM 2194 C PHE A 276 52.498 391.137 37.782 1.00207.00 C
ANISOU 2194 C PHE A 276 20944 24485 33220 15 2547 1574 C
ATOM 2195 O PHE A 276 53.523 390.639 37.303 1.00214.94 O
ANISOU 2195 O PHE A 276 21812 25462 34393 76 2713 1619 O
ATOM 2196 CB PHE A 276 50.647 392.498 36.757 1.00210.42 C
ANISOU 2196 CB PHE A 276 21769 24974 33207 -41 2828 1709 C
ATOM 2197 CG PHE A 276 50.988 393.121 35.402 1.00215.57 C
ANISOU 2197 CG PHE A 276 22479 25574 33855 -25 3241 1888 C
ATOM 2198 CD1 PHE A 276 50.040 393.147 34.380 1.00212.80 C
ANISOU 2198 CD1 PHE A 276 22411 25322 33122 56 3511 1974 C
ATOM 2199 CD2 PHE A 276 52.195 393.787 35.193 1.00217.82 C
ANISOU 2199 CD2 PHE A 276 22542 25697 34521 -92 3341 1972 C
ATOM 2200 CE1 PHE A 276 50.318 393.760 33.156 1.00212.11 C
ANISOU 2200 CE1 PHE A 276 22404 25181 33006 85 3878 2145 C
ATOM 2201 CE2 PHE A 276 52.475 394.401 33.968 1.00216.21 C
ANISOU 2201 CE2 PHE A 276 22403 25437 34312 -69 3727 2149 C
ATOM 2202 CZ PHE A 276 51.534 394.385 32.953 1.00213.74 C
ANISOU 2202 CZ PHE A 276 22393 25230 33591 24 3994 2236 C
ATOM 2203 N THR A 277 52.505 391.715 38.980 1.00198.66 N
ANISOU 2203 N THR A 277 19779 23345 32359 -96 2172 1476 N
ATOM 2204 CA THR A 277 53.733 391.652 39.760 1.00186.70 C
ANISOU 2204 CA THR A 277 17983 21710 31245 -134 1929 1409 C
ATOM 2205 C THR A 277 53.668 390.277 40.431 1.00185.19 C
ANISOU 2205 C THR A 277 17804 21628 30930 -14 1719 1291 C
ATOM 2206 O THR A 277 52.764 389.508 40.127 1.00175.82 O
ANISOU 2206 O THR A 277 16827 20588 29388 85 1820 1283 O
ATOM 2207 CB THR A 277 53.841 392.827 40.732 1.00176.25 C
ANISOU 2207 CB THR A 277 16549 20234 30183 -286 1602 1342 C
ATOM 2208 OG1 THR A 277 52.711 392.849 41.612 1.00163.09 O
ANISOU 2208 OG1 THR A 277 15046 18637 28282 -300 1317 1231 O
ATOM 2209 CG2 THR A 277 53.909 394.149 39.965 1.00177.12 C
ANISOU 2209 CG2 THR A 277 16655 20226 30418 -392 1847 1475 C
ATOM 2210 N HIS A 278 54.623 389.906 41.292 1.00190.68 N
ANISOU 2210 N HIS A 278 18285 22250 31913 -9 1436 1203 N
ATOM 2211 CA HIS A 278 54.557 388.604 41.979 1.00192.50 C
ANISOU 2211 CA HIS A 278 18542 22574 32026 116 1218 1097 C
ATOM 2212 C HIS A 278 53.962 387.467 41.133 1.00203.83 C
ANISOU 2212 C HIS A 278 20167 24167 33112 263 1507 1138 C
ATOM 2213 O HIS A 278 53.197 386.648 41.651 1.00201.94 O
ANISOU 2213 O HIS A 278 20073 24026 32628 348 1349 1061 O
ATOM 2214 CB HIS A 278 53.701 388.737 43.250 1.00180.69 C
ANISOU 2214 CB HIS A 278 17155 21099 30400 90 804 969 C
ATOM 2215 CG HIS A 278 54.335 389.529 44.352 1.00180.88 C
ANISOU 2215 CG HIS A 278 17010 20972 30746 -12 409 876 C
ATOM 2216 ND1 HIS A 278 54.785 390.821 44.184 1.00187.59 N
ANISOU 2216 ND1 HIS A 278 17738 21673 31865 -155 439 916 N
ATOM 2217 CD2 HIS A 278 54.547 389.226 45.655 1.00179.79 C
ANISOU 2217 CD2 HIS A 278 16831 20799 30684 19 -45 737 C
ATOM 2218 CE1 HIS A 278 55.277 391.268 45.326 1.00188.79 C
ANISOU 2218 CE1 HIS A 278 17770 21701 32261 -213 17 795 C
ATOM 2219 NE2 HIS A 278 55.142 390.319 46.236 1.00184.93 N
ANISOU 2219 NE2 HIS A 278 17337 21283 31647 -105 -288 684 N
ATOM 2220 N GLN A 279 54.301 387.409 39.838 1.00214.22 N
ANISOU 2220 N GLN A 279 21493 25497 34402 303 1923 1257 N
ATOM 2221 CA GLN A 279 53.945 386.269 38.984 1.00214.09 C
ANISOU 2221 CA GLN A 279 21642 25608 34093 460 2192 1282 C
ATOM 2222 C GLN A 279 54.502 384.929 39.467 1.00213.07 C
ANISOU 2222 C GLN A 279 21428 25507 34021 589 2045 1199 C
ATOM 2223 O GLN A 279 53.805 383.908 39.394 1.00215.18 O
ANISOU 2223 O GLN A 279 21874 25880 34005 710 2063 1154 O
ATOM 2224 CB GLN A 279 54.404 386.546 37.549 1.00216.45 C
ANISOU 2224 CB GLN A 279 21952 25893 34397 486 2645 1423 C
ATOM 2225 CG GLN A 279 54.220 385.387 36.565 1.00214.46 C
ANISOU 2225 CG GLN A 279 21864 25752 33869 661 2940 1443 C
ATOM 2226 CD GLN A 279 52.768 385.053 36.268 1.00207.79 C
ANISOU 2226 CD GLN A 279 21334 25036 32581 722 2990 1413 C
ATOM 2227 OE1 GLN A 279 51.852 385.737 36.720 1.00206.40 O
ANISOU 2227 OE1 GLN A 279 21257 24875 32292 631 2840 1395 O
ATOM 2228 NE2 GLN A 279 52.555 383.991 35.496 1.00203.44 N
ANISOU 2228 NE2 GLN A 279 20939 24571 31786 882 3201 1404 N
ATOM 2229 N GLY A 280 55.755 384.900 39.917 1.00203.31 N
ANISOU 2229 N GLY A 280 19924 24169 33156 572 1909 1182 N
ATOM 2230 CA GLY A 280 56.456 383.677 40.284 1.00191.75 C
ANISOU 2230 CA GLY A 280 18353 22714 31789 700 1795 1120 C
ATOM 2231 C GLY A 280 55.686 382.449 40.745 1.00181.15 C
ANISOU 2231 C GLY A 280 17194 21475 30161 836 1646 1033 C
ATOM 2232 O GLY A 280 55.640 381.436 40.041 1.00176.94 O
ANISOU 2232 O GLY A 280 16756 21009 29466 975 1870 1045 O
ATOM 2233 N SER A 281 55.062 382.540 41.916 1.00178.78 N
ANISOU 2233 N SER A 281 16957 21177 29793 803 1271 945 N
ATOM 2234 CA SER A 281 54.333 381.433 42.520 1.00173.50 C
ANISOU 2234 CA SER A 281 16457 20580 28883 929 1089 870 C
ATOM 2235 C SER A 281 52.975 381.188 41.848 1.00159.69 C
ANISOU 2235 C SER A 281 14992 18940 26744 969 1313 892 C
ATOM 2236 O SER A 281 52.496 381.969 41.021 1.00143.27 O
ANISOU 2236 O SER A 281 12996 16888 24551 893 1566 959 O
ATOM 2237 CB SER A 281 54.148 381.692 44.013 1.00172.86 C
ANISOU 2237 CB SER A 281 16361 20455 28863 891 613 779 C
ATOM 2238 OG SER A 281 55.260 381.234 44.769 1.00176.62 O
ANISOU 2238 OG SER A 281 16647 20855 29606 944 345 725 O
ATOM 2239 N CYS A 282 52.384 380.040 42.191 1.00165.99 N
ANISOU 2239 N CYS A 282 15940 19786 27342 1101 1218 838 N
ATOM 2240 CA CYS A 282 51.039 379.641 41.786 1.00166.76 C
ANISOU 2240 CA CYS A 282 16314 19969 27080 1150 1350 834 C
ATOM 2241 C CYS A 282 50.297 379.174 43.035 1.00172.13 C
ANISOU 2241 C CYS A 282 17233 20655 27514 1153 975 752 C
ATOM 2242 O CYS A 282 50.848 378.407 43.828 1.00178.55 O
ANISOU 2242 O CYS A 282 17969 21421 28451 1244 744 710 O
ATOM 2243 CB CYS A 282 51.088 378.534 40.710 1.00169.15 C
ANISOU 2243 CB CYS A 282 16711 20310 27249 1299 1660 846 C
ATOM 2244 SG CYS A 282 52.556 377.388 40.705 1.00161.92 S
ANISOU 2244 SG CYS A 282 15608 19335 26579 1441 1656 824 S
ATOM 2245 N PHE A 283 49.071 379.652 43.247 1.00176.79 N
ANISOU 2245 N PHE A 283 18109 21296 27767 1062 914 735 N
ATOM 2246 CA PHE A 283 48.433 379.410 44.538 1.00187.23 C
ANISOU 2246 CA PHE A 283 19635 22612 28891 1055 569 672 C
ATOM 2247 C PHE A 283 46.955 379.059 44.399 1.00190.95 C
ANISOU 2247 C PHE A 283 20473 23156 28924 1043 629 657 C
ATOM 2248 O PHE A 283 46.266 379.538 43.496 1.00182.56 O
ANISOU 2248 O PHE A 283 19514 22148 27701 985 855 685 O
ATOM 2249 CB PHE A 283 48.615 380.619 45.470 1.00187.49 C
ANISOU 2249 CB PHE A 283 19579 22598 29062 941 303 648 C
ATOM 2250 CG PHE A 283 49.893 380.574 46.274 1.00187.98 C
ANISOU 2250 CG PHE A 283 19355 22569 29500 982 36 618 C
ATOM 2251 CD1 PHE A 283 49.879 380.210 47.612 1.00186.72 C
ANISOU 2251 CD1 PHE A 283 19304 22373 29268 1037 -344 552 C
ATOM 2252 CD2 PHE A 283 51.109 380.879 45.690 1.00189.84 C
ANISOU 2252 CD2 PHE A 283 19214 22750 30168 977 166 657 C
ATOM 2253 CE1 PHE A 283 51.054 380.162 48.351 1.00187.92 C
ANISOU 2253 CE1 PHE A 283 19200 22437 29766 1088 -627 515 C
ATOM 2254 CE2 PHE A 283 52.281 380.828 46.429 1.00190.39 C
ANISOU 2254 CE2 PHE A 283 18993 22727 30618 1016 -104 622 C
ATOM 2255 CZ PHE A 283 52.257 380.473 47.753 1.00189.11 C
ANISOU 2255 CZ PHE A 283 18947 22531 30374 1073 -517 544 C
ATOM 2256 N GLY A 284 46.484 378.216 45.320 1.00201.59 N
ANISOU 2256 N GLY A 284 22011 24493 30090 1101 417 618 N
ATOM 2257 CA GLY A 284 45.113 377.725 45.337 1.00206.48 C
ANISOU 2257 CA GLY A 284 22953 25160 30340 1093 450 606 C
ATOM 2258 C GLY A 284 44.703 377.047 46.644 1.00208.36 C
ANISOU 2258 C GLY A 284 23376 25365 30425 1140 183 583 C
ATOM 2259 O GLY A 284 45.527 376.909 47.551 1.00229.54 O
ANISOU 2259 O GLY A 284 25955 27989 33269 1198 -52 571 O
ATOM 2260 N PRO A 285 43.427 376.620 46.758 1.00178.64 N
ANISOU 2260 N PRO A 285 19888 21631 26356 1122 216 583 N
ATOM 2261 CA PRO A 285 42.354 376.733 45.762 1.00168.21 C
ANISOU 2261 CA PRO A 285 18702 20373 24838 1060 446 586 C
ATOM 2262 C PRO A 285 41.964 378.183 45.485 1.00195.66 C
ANISOU 2262 C PRO A 285 22152 23902 28287 941 499 595 C
ATOM 2263 O PRO A 285 41.411 378.502 44.430 1.00197.60 O
ANISOU 2263 O PRO A 285 22439 24198 28441 900 703 604 O
ATOM 2264 CB PRO A 285 41.192 375.980 46.417 1.00149.03 C
ANISOU 2264 CB PRO A 285 16537 17935 22152 1065 373 585 C
ATOM 2265 CG PRO A 285 41.454 376.090 47.876 1.00145.44 C
ANISOU 2265 CG PRO A 285 16121 17438 21701 1090 109 592 C
ATOM 2266 CD PRO A 285 42.944 375.994 48.004 1.00156.24 C
ANISOU 2266 CD PRO A 285 17253 18757 23353 1167 5 584 C
ATOM 2267 N ILE A 286 42.290 379.050 46.438 1.00212.59 N
ANISOU 2267 N ILE A 286 24238 26023 30513 898 299 588 N
ATOM 2268 CA ILE A 286 41.933 380.460 46.403 1.00211.60 C
ANISOU 2268 CA ILE A 286 24103 25923 30374 789 304 591 C
ATOM 2269 C ILE A 286 43.186 381.312 46.693 1.00218.61 C
ANISOU 2269 C ILE A 286 24734 26751 31576 761 184 585 C
ATOM 2270 O ILE A 286 43.592 381.309 47.854 1.00230.28 O
ANISOU 2270 O ILE A 286 26206 28178 33109 789 -85 549 O
ATOM 2271 CB ILE A 286 40.826 380.754 47.443 1.00201.95 C
ANISOU 2271 CB ILE A 286 23116 24714 28903 756 153 571 C
ATOM 2272 CG1 ILE A 286 39.732 379.668 47.438 1.00192.34 C
ANISOU 2272 CG1 ILE A 286 22119 23524 27438 793 225 580 C
ATOM 2273 CG2 ILE A 286 40.241 382.072 47.187 1.00202.56 C
ANISOU 2273 CG2 ILE A 286 23216 24821 28929 656 208 572 C
ATOM 2274 CD1 ILE A 286 38.334 380.149 47.888 1.00181.11 C
ANISOU 2274 CD1 ILE A 286 20905 22139 25768 736 220 580 C
ATOM 2275 N PHE A 287 43.855 382.037 45.767 1.00207.98 N
ANISOU 2275 N PHE A 287 23174 25396 30452 711 353 620 N
ATOM 2276 CA PHE A 287 43.702 382.286 44.300 1.00188.19 C
ANISOU 2276 CA PHE A 287 20634 22935 27937 687 680 675 C
ATOM 2277 C PHE A 287 42.896 383.554 44.035 1.00170.52 C
ANISOU 2277 C PHE A 287 18487 20720 25582 579 741 695 C
ATOM 2278 O PHE A 287 42.565 384.297 44.961 1.00169.35 O
ANISOU 2278 O PHE A 287 18398 20546 25399 519 541 661 O
ATOM 2279 CB PHE A 287 43.089 381.114 43.511 1.00183.50 C
ANISOU 2279 CB PHE A 287 20200 22397 27126 769 861 675 C
ATOM 2280 CG PHE A 287 43.795 380.821 42.199 1.00181.27 C
ANISOU 2280 CG PHE A 287 19783 22121 26970 828 1145 717 C
ATOM 2281 CD1 PHE A 287 44.389 381.839 41.459 1.00182.02 C
ANISOU 2281 CD1 PHE A 287 19706 22203 27249 776 1323 780 C
ATOM 2282 CD2 PHE A 287 43.879 379.522 41.718 1.00177.81 C
ANISOU 2282 CD2 PHE A 287 19400 21690 26470 943 1245 696 C
ATOM 2283 CE1 PHE A 287 45.037 381.571 40.268 1.00182.25 C
ANISOU 2283 CE1 PHE A 287 19630 22238 27378 846 1615 830 C
ATOM 2284 CE2 PHE A 287 44.533 379.243 40.530 1.00176.86 C
ANISOU 2284 CE2 PHE A 287 19180 21574 26446 1019 1518 728 C
ATOM 2285 CZ PHE A 287 45.110 380.269 39.803 1.00181.17 C
ANISOU 2285 CZ PHE A 287 19563 22118 27156 975 1713 799 C
ATOM 2286 N MET A 288 42.639 383.812 42.742 1.00157.01 N
ANISOU 2286 N MET A 288 16793 19050 23812 569 1020 750 N
ATOM 2287 CA MET A 288 41.675 384.794 42.244 1.00142.17 C
ANISOU 2287 CA MET A 288 15052 17206 21761 497 1117 778 C
ATOM 2288 C MET A 288 40.242 384.373 42.537 1.00142.75 C
ANISOU 2288 C MET A 288 15395 17342 21502 507 1047 733 C
ATOM 2289 O MET A 288 39.225 384.985 42.108 1.00143.72 O
ANISOU 2289 O MET A 288 15661 17506 21441 468 1117 747 O
ATOM 2290 CB MET A 288 41.880 385.020 40.739 1.00135.58 C
ANISOU 2290 CB MET A 288 14179 16394 20940 516 1436 855 C
ATOM 2291 CG MET A 288 40.962 386.072 40.079 1.00128.48 C
ANISOU 2291 CG MET A 288 13422 15523 19871 458 1549 901 C
ATOM 2292 SD MET A 288 41.588 387.704 39.610 1.00125.85 S
ANISOU 2292 SD MET A 288 12929 15113 19777 361 1682 1003 S
ATOM 2293 CE MET A 288 42.695 387.355 38.246 1.00119.81 C
ANISOU 2293 CE MET A 288 12009 14339 19176 436 2036 1103 C
ATOM 2294 N THR A 289 40.030 383.305 43.294 1.00136.32 N
ANISOU 2294 N THR A 289 14664 16533 20600 562 908 684 N
ATOM 2295 CA THR A 289 38.656 382.996 43.579 1.00115.13 C
ANISOU 2295 CA THR A 289 12209 13894 17640 558 864 656 C
ATOM 2296 C THR A 289 38.158 383.679 44.849 1.00108.15 C
ANISOU 2296 C THR A 289 11406 12993 16694 510 660 629 C
ATOM 2297 O THR A 289 37.029 383.408 45.265 1.00100.30 O
ANISOU 2297 O THR A 289 10589 12029 15491 510 624 612 O
ATOM 2298 CB THR A 289 38.501 381.473 43.605 1.00100.20 C
ANISOU 2298 CB THR A 289 10398 12008 15665 639 864 630 C
ATOM 2299 OG1 THR A 289 39.008 380.974 44.830 1.00103.08 O
ANISOU 2299 OG1 THR A 289 10740 12324 16102 674 664 611 O
ATOM 2300 CG2 THR A 289 39.303 380.848 42.493 1.00 84.56 C
ANISOU 2300 CG2 THR A 289 8314 10025 13789 708 1045 643 C
ATOM 2301 N ILE A 290 39.000 384.483 45.536 1.00106.63 N
ANISOU 2301 N ILE A 290 11087 12740 16688 477 517 619 N
ATOM 2302 CA ILE A 290 38.494 385.308 46.642 1.00 99.31 C
ANISOU 2302 CA ILE A 290 10264 11790 15679 440 333 582 C
ATOM 2303 C ILE A 290 37.482 386.320 46.120 1.00105.00 C
ANISOU 2303 C ILE A 290 11077 12543 16273 377 444 600 C
ATOM 2304 O ILE A 290 36.401 386.451 46.718 1.00102.26 O
ANISOU 2304 O ILE A 290 10906 12223 15726 379 392 577 O
ATOM 2305 CB ILE A 290 39.651 385.994 47.391 1.00100.53 C
ANISOU 2305 CB ILE A 290 10261 11857 16079 418 133 550 C
ATOM 2306 CG1 ILE A 290 40.424 385.045 48.294 1.00 98.48 C
ANISOU 2306 CG1 ILE A 290 9967 11561 15891 498 -63 517 C
ATOM 2307 CG2 ILE A 290 39.119 387.145 48.225 1.00103.71 C
ANISOU 2307 CG2 ILE A 290 10775 12226 16403 371 -16 506 C
ATOM 2308 CD1 ILE A 290 41.597 385.682 48.978 1.00103.09 C
ANISOU 2308 CD1 ILE A 290 10375 12051 16743 482 -292 473 C
ATOM 2309 N PRO A 291 37.743 387.042 45.015 1.00108.16 N
ANISOU 2309 N PRO A 291 11375 12941 16779 332 611 648 N
ATOM 2310 CA PRO A 291 36.721 387.944 44.470 1.00114.04 C
ANISOU 2310 CA PRO A 291 12227 13717 17387 290 711 672 C
ATOM 2311 C PRO A 291 35.444 387.226 44.096 1.00101.36 C
ANISOU 2311 C PRO A 291 10792 12193 15528 328 792 667 C
ATOM 2312 O PRO A 291 34.353 387.734 44.375 1.00108.82 O
ANISOU 2312 O PRO A 291 11862 13159 16324 313 765 654 O
ATOM 2313 CB PRO A 291 37.423 388.582 43.260 1.00115.39 C
ANISOU 2313 CB PRO A 291 12258 13863 17723 258 899 744 C
ATOM 2314 CG PRO A 291 38.851 388.493 43.575 1.00106.26 C
ANISOU 2314 CG PRO A 291 10888 12635 16851 248 837 745 C
ATOM 2315 CD PRO A 291 39.018 387.204 44.292 1.00106.39 C
ANISOU 2315 CD PRO A 291 10929 12674 16822 319 713 692 C
ATOM 2316 N ALA A 292 35.555 386.056 43.467 1.00 87.10 N
ANISOU 2316 N ALA A 292 8984 10423 13688 380 886 673 N
ATOM 2317 CA ALA A 292 34.367 385.315 43.062 1.00 83.46 C
ANISOU 2317 CA ALA A 292 8668 10021 13021 409 943 658 C
ATOM 2318 C ALA A 292 33.529 384.929 44.270 1.00 78.12 C
ANISOU 2318 C ALA A 292 8106 9346 12228 411 810 623 C
ATOM 2319 O ALA A 292 32.294 385.022 44.244 1.00 54.52 O
ANISOU 2319 O ALA A 292 5226 6393 9096 400 829 616 O
ATOM 2320 CB ALA A 292 34.770 384.069 42.272 1.00 78.44 C
ANISOU 2320 CB ALA A 292 8013 9399 12391 470 1042 653 C
ATOM 2321 N PHE A 293 34.178 384.419 45.312 1.00 81.16 N
ANISOU 2321 N PHE A 293 8471 9691 12676 436 682 606 N
ATOM 2322 CA PHE A 293 33.459 384.106 46.538 1.00 82.82 C
ANISOU 2322 CA PHE A 293 8813 9894 12761 452 571 589 C
ATOM 2323 C PHE A 293 32.578 385.292 46.940 1.00 77.59 C
ANISOU 2323 C PHE A 293 8230 9243 12007 417 551 582 C
ATOM 2324 O PHE A 293 31.368 385.146 47.137 1.00 87.81 O
ANISOU 2324 O PHE A 293 9634 10568 13162 418 591 584 O
ATOM 2325 CB PHE A 293 34.444 383.662 47.628 1.00 88.63 C
ANISOU 2325 CB PHE A 293 9527 10575 13574 498 409 576 C
ATOM 2326 CG PHE A 293 33.781 383.043 48.839 1.00 93.64 C
ANISOU 2326 CG PHE A 293 10329 11197 14054 542 325 577 C
ATOM 2327 CD1 PHE A 293 33.614 381.654 48.888 1.00 82.91 C
ANISOU 2327 CD1 PHE A 293 9022 9826 12652 586 359 599 C
ATOM 2328 CD2 PHE A 293 33.386 383.798 49.932 1.00 98.28 C
ANISOU 2328 CD2 PHE A 293 11032 11771 14541 551 221 559 C
ATOM 2329 CE1 PHE A 293 33.023 381.034 49.964 1.00 79.46 C
ANISOU 2329 CE1 PHE A 293 8745 9366 12081 629 312 623 C
ATOM 2330 CE2 PHE A 293 32.800 383.176 51.035 1.00102.78 C
ANISOU 2330 CE2 PHE A 293 11774 12325 14951 609 177 577 C
ATOM 2331 CZ PHE A 293 32.624 381.788 51.047 1.00 97.62 C
ANISOU 2331 CZ PHE A 293 11166 11661 14264 644 230 618 C
ATOM 2332 N PHE A 294 33.175 386.480 47.081 1.00 90.70 N
ANISOU 2332 N PHE A 294 9826 10868 13767 385 489 571 N
ATOM 2333 CA PHE A 294 32.407 387.656 47.491 1.00 90.57 C
ANISOU 2333 CA PHE A 294 9891 10847 13675 362 462 556 C
ATOM 2334 C PHE A 294 31.573 388.292 46.373 1.00 82.55 C
ANISOU 2334 C PHE A 294 8877 9873 12616 330 605 584 C
ATOM 2335 O PHE A 294 30.512 388.862 46.661 1.00 85.90 O
ANISOU 2335 O PHE A 294 9396 10312 12931 332 612 576 O
ATOM 2336 CB PHE A 294 33.360 388.714 48.047 1.00106.21 C
ANISOU 2336 CB PHE A 294 11807 12750 15797 337 323 524 C
ATOM 2337 CG PHE A 294 33.946 388.354 49.375 1.00115.64 C
ANISOU 2337 CG PHE A 294 13050 13898 16990 385 126 477 C
ATOM 2338 CD1 PHE A 294 33.183 387.700 50.333 1.00112.25 C
ANISOU 2338 CD1 PHE A 294 12797 13492 16363 449 88 468 C
ATOM 2339 CD2 PHE A 294 35.272 388.659 49.663 1.00120.88 C
ANISOU 2339 CD2 PHE A 294 13583 14487 17858 372 -23 447 C
ATOM 2340 CE1 PHE A 294 33.733 387.366 51.561 1.00117.89 C
ANISOU 2340 CE1 PHE A 294 13591 14160 17043 514 -99 432 C
ATOM 2341 CE2 PHE A 294 35.829 388.322 50.887 1.00118.70 C
ANISOU 2341 CE2 PHE A 294 13364 14164 17573 431 -241 396 C
ATOM 2342 CZ PHE A 294 35.062 387.678 51.837 1.00116.19 C
ANISOU 2342 CZ PHE A 294 13257 13874 17016 509 -281 389 C
ATOM 2343 N ALA A 295 31.983 388.191 45.101 1.00 72.21 N
ANISOU 2343 N ALA A 295 7478 8580 11378 316 723 621 N
ATOM 2344 CA ALA A 295 31.154 388.776 44.046 1.00 74.73 C
ANISOU 2344 CA ALA A 295 7831 8936 11625 306 839 650 C
ATOM 2345 C ALA A 295 29.793 388.098 43.931 1.00 90.12 C
ANISOU 2345 C ALA A 295 9879 10945 13416 331 868 635 C
ATOM 2346 O ALA A 295 28.860 388.687 43.371 1.00 83.46 O
ANISOU 2346 O ALA A 295 9079 10129 12502 331 913 645 O
ATOM 2347 CB ALA A 295 31.877 388.703 42.702 1.00 73.41 C
ANISOU 2347 CB ALA A 295 7584 8776 11532 308 971 696 C
ATOM 2348 N LYS A 296 29.672 386.863 44.432 1.00 97.03 N
ANISOU 2348 N LYS A 296 10780 11831 14256 352 840 614 N
ATOM 2349 CA LYS A 296 28.407 386.142 44.377 1.00 85.23 C
ANISOU 2349 CA LYS A 296 9354 10372 12659 362 868 603 C
ATOM 2350 C LYS A 296 27.350 386.874 45.177 1.00 75.98 C
ANISOU 2350 C LYS A 296 8246 9205 11420 359 844 600 C
ATOM 2351 O LYS A 296 26.161 386.840 44.834 1.00 66.62 O
ANISOU 2351 O LYS A 296 7081 8050 10181 359 884 598 O
ATOM 2352 CB LYS A 296 28.558 384.681 44.815 1.00 91.35 C
ANISOU 2352 CB LYS A 296 10144 11130 13433 380 851 594 C
ATOM 2353 CG LYS A 296 29.297 383.801 43.811 1.00 92.62 C
ANISOU 2353 CG LYS A 296 10257 11290 13645 399 899 586 C
ATOM 2354 CD LYS A 296 29.432 382.376 44.321 1.00101.67 C
ANISOU 2354 CD LYS A 296 11427 12400 14801 422 873 577 C
ATOM 2355 CE LYS A 296 30.527 381.606 43.609 1.00104.75 C
ANISOU 2355 CE LYS A 296 11762 12772 15267 460 906 566 C
ATOM 2356 NZ LYS A 296 29.859 380.692 42.613 1.00109.93 N
ANISOU 2356 NZ LYS A 296 12461 13432 15875 472 962 530 N
ATOM 2357 N THR A 297 27.760 387.486 46.290 1.00 74.78 N
ANISOU 2357 N THR A 297 8125 9016 11273 366 770 592 N
ATOM 2358 CA THR A 297 26.835 388.208 47.155 1.00 78.96 C
ANISOU 2358 CA THR A 297 8734 9541 11725 384 758 582 C
ATOM 2359 C THR A 297 26.159 389.391 46.459 1.00 81.43 C
ANISOU 2359 C THR A 297 9036 9868 12036 375 798 585 C
ATOM 2360 O THR A 297 25.160 389.906 46.972 1.00 76.07 O
ANISOU 2360 O THR A 297 8411 9194 11298 400 816 578 O
ATOM 2361 CB THR A 297 27.629 388.719 48.360 1.00 75.33 C
ANISOU 2361 CB THR A 297 8329 9027 11267 405 645 555 C
ATOM 2362 OG1 THR A 297 28.345 387.632 48.929 1.00 76.77 O
ANISOU 2362 OG1 THR A 297 8523 9192 11454 426 590 558 O
ATOM 2363 CG2 THR A 297 26.733 389.278 49.403 1.00 89.48 C
ANISOU 2363 CG2 THR A 297 10240 10810 12948 449 641 538 C
ATOM 2364 N SER A 298 26.609 389.775 45.266 1.00 78.26 N
ANISOU 2364 N SER A 298 8571 9471 11692 352 829 604 N
ATOM 2365 CA SER A 298 25.902 390.822 44.555 1.00 76.56 C
ANISOU 2365 CA SER A 298 8363 9264 11460 358 866 620 C
ATOM 2366 C SER A 298 24.496 390.402 44.154 1.00 78.73 C
ANISOU 2366 C SER A 298 8652 9594 11670 380 905 617 C
ATOM 2367 O SER A 298 23.670 391.274 43.872 1.00 89.32 O
ANISOU 2367 O SER A 298 10006 10940 12991 402 914 623 O
ATOM 2368 CB SER A 298 26.688 391.229 43.315 1.00 80.39 C
ANISOU 2368 CB SER A 298 8802 9741 12004 341 912 659 C
ATOM 2369 OG SER A 298 26.580 390.230 42.321 1.00 78.42 O
ANISOU 2369 OG SER A 298 8540 9541 11716 355 965 665 O
ATOM 2370 N ALA A 299 24.197 389.097 44.127 1.00 67.81 N
ANISOU 2370 N ALA A 299 7254 8238 10273 376 918 606 N
ATOM 2371 CA ALA A 299 22.830 388.658 43.865 1.00 62.29 C
ANISOU 2371 CA ALA A 299 6542 7572 9555 385 938 595 C
ATOM 2372 C ALA A 299 21.889 389.058 44.986 1.00 70.88 C
ANISOU 2372 C ALA A 299 7650 8653 10630 405 958 597 C
ATOM 2373 O ALA A 299 20.668 389.036 44.790 1.00 63.06 O
ANISOU 2373 O ALA A 299 6620 7682 9656 417 982 594 O
ATOM 2374 CB ALA A 299 22.771 387.156 43.637 1.00 70.21 C
ANISOU 2374 CB ALA A 299 7522 8579 10574 366 943 580 C
ATOM 2375 N VAL A 300 22.429 389.342 46.168 1.00 74.91 N
ANISOU 2375 N VAL A 300 8219 9129 11112 417 949 597 N
ATOM 2376 CA VAL A 300 21.648 389.801 47.312 1.00 69.71 C
ANISOU 2376 CA VAL A 300 7618 8459 10411 459 986 596 C
ATOM 2377 C VAL A 300 21.712 391.319 47.476 1.00 81.06 C
ANISOU 2377 C VAL A 300 9097 9868 11833 491 956 577 C
ATOM 2378 O VAL A 300 20.679 391.969 47.631 1.00 91.43 O
ANISOU 2378 O VAL A 300 10414 11187 13138 533 1001 575 O
ATOM 2379 CB VAL A 300 22.090 389.067 48.594 1.00 71.03 C
ANISOU 2379 CB VAL A 300 7867 8600 10522 476 988 603 C
ATOM 2380 CG1 VAL A 300 21.389 389.632 49.803 1.00 63.30 C
ANISOU 2380 CG1 VAL A 300 6984 7605 9464 542 1041 602 C
ATOM 2381 CG2 VAL A 300 21.792 387.566 48.457 1.00 78.26 C
ANISOU 2381 CG2 VAL A 300 8742 9525 11469 447 1037 632 C
ATOM 2382 N TYR A 301 22.915 391.920 47.436 1.00 88.32 N
ANISOU 2382 N TYR A 301 10039 10746 12773 473 881 563 N
ATOM 2383 CA TYR A 301 23.000 393.339 47.806 1.00 84.59 C
ANISOU 2383 CA TYR A 301 9622 10218 12299 500 841 538 C
ATOM 2384 C TYR A 301 22.678 394.271 46.642 1.00 80.86 C
ANISOU 2384 C TYR A 301 9104 9742 11877 495 857 561 C
ATOM 2385 O TYR A 301 22.223 395.395 46.881 1.00 82.25 O
ANISOU 2385 O TYR A 301 9324 9876 12050 535 852 546 O
ATOM 2386 CB TYR A 301 24.371 393.694 48.429 1.00 76.18 C
ANISOU 2386 CB TYR A 301 8597 9083 11264 481 734 505 C
ATOM 2387 CG TYR A 301 25.605 393.606 47.536 1.00 84.32 C
ANISOU 2387 CG TYR A 301 9535 10096 12408 415 699 528 C
ATOM 2388 CD1 TYR A 301 25.837 394.533 46.529 1.00 87.45 C
ANISOU 2388 CD1 TYR A 301 9882 10461 12885 385 720 559 C
ATOM 2389 CD2 TYR A 301 26.559 392.605 47.730 1.00 91.33 C
ANISOU 2389 CD2 TYR A 301 10386 10989 13327 392 659 528 C
ATOM 2390 CE1 TYR A 301 26.962 394.447 45.721 1.00 86.54 C
ANISOU 2390 CE1 TYR A 301 9679 10325 12878 332 728 595 C
ATOM 2391 CE2 TYR A 301 27.689 392.518 46.931 1.00 85.31 C
ANISOU 2391 CE2 TYR A 301 9523 10207 12684 342 652 552 C
ATOM 2392 CZ TYR A 301 27.881 393.441 45.924 1.00 84.23 C
ANISOU 2392 CZ TYR A 301 9334 10044 12626 311 699 589 C
ATOM 2393 OH TYR A 301 28.995 393.379 45.116 1.00 90.71 O
ANISOU 2393 OH TYR A 301 10053 10842 13572 269 732 628 O
ATOM 2394 N ASN A 302 22.866 393.840 45.391 1.00 73.65 N
ANISOU 2394 N ASN A 302 8121 8866 10996 462 877 598 N
ATOM 2395 CA ASN A 302 22.409 394.677 44.281 1.00 73.53 C
ANISOU 2395 CA ASN A 302 8093 8850 10995 480 894 630 C
ATOM 2396 C ASN A 302 20.907 394.929 44.295 1.00 82.13 C
ANISOU 2396 C ASN A 302 9177 9970 12058 539 915 623 C
ATOM 2397 O ASN A 302 20.508 396.101 44.194 1.00 86.14 O
ANISOU 2397 O ASN A 302 9715 10438 12578 580 908 630 O
ATOM 2398 CB ASN A 302 22.852 394.103 42.932 1.00 69.50 C
ANISOU 2398 CB ASN A 302 7545 8376 10487 457 916 668 C
ATOM 2399 CG ASN A 302 24.237 394.552 42.531 1.00 82.68 C
ANISOU 2399 CG ASN A 302 9206 9990 12217 417 928 704 C
ATOM 2400 OD1 ASN A 302 24.762 395.547 43.043 1.00 77.49 O
ANISOU 2400 OD1 ASN A 302 8563 9255 11623 400 902 705 O
ATOM 2401 ND2 ASN A 302 24.831 393.834 41.586 1.00 93.32 N
ANISOU 2401 ND2 ASN A 302 10527 11369 13560 405 971 732 N
ATOM 2402 N PRO A 303 20.027 393.928 44.411 1.00 80.94 N
ANISOU 2402 N PRO A 303 8979 9877 11898 546 941 611 N
ATOM 2403 CA PRO A 303 18.596 394.260 44.526 1.00 78.90 C
ANISOU 2403 CA PRO A 303 8683 9636 11659 604 966 605 C
ATOM 2404 C PRO A 303 18.272 395.090 45.752 1.00 74.91 C
ANISOU 2404 C PRO A 303 8237 9089 11138 656 1005 585 C
ATOM 2405 O PRO A 303 17.348 395.909 45.695 1.00 80.60 O
ANISOU 2405 O PRO A 303 8943 9799 11883 721 1020 583 O
ATOM 2406 CB PRO A 303 17.901 392.889 44.570 1.00 81.93 C
ANISOU 2406 CB PRO A 303 8988 10069 12074 580 995 599 C
ATOM 2407 CG PRO A 303 18.974 391.897 44.831 1.00 81.04 C
ANISOU 2407 CG PRO A 303 8904 9955 11935 522 993 598 C
ATOM 2408 CD PRO A 303 20.242 392.473 44.302 1.00 78.32 C
ANISOU 2408 CD PRO A 303 8607 9583 11566 503 949 607 C
ATOM 2409 N VAL A 304 18.984 394.899 46.866 1.00 72.04 N
ANISOU 2409 N VAL A 304 7950 8696 10727 646 1013 563 N
ATOM 2410 CA VAL A 304 18.768 395.762 48.027 1.00 76.13 C
ANISOU 2410 CA VAL A 304 8564 9162 11198 714 1035 529 C
ATOM 2411 C VAL A 304 19.041 397.218 47.669 1.00 85.99 C
ANISOU 2411 C VAL A 304 9858 10341 12474 737 977 515 C
ATOM 2412 O VAL A 304 18.300 398.118 48.074 1.00 95.10 O
ANISOU 2412 O VAL A 304 11052 11460 13622 815 1007 493 O
ATOM 2413 CB VAL A 304 19.621 395.299 49.224 1.00 68.74 C
ANISOU 2413 CB VAL A 304 7733 8200 10184 709 1015 501 C
ATOM 2414 CG1 VAL A 304 19.591 396.347 50.327 1.00 66.06 C
ANISOU 2414 CG1 VAL A 304 7532 7791 9775 790 1003 445 C
ATOM 2415 CG2 VAL A 304 19.135 393.952 49.751 1.00 57.13 C
ANISOU 2415 CG2 VAL A 304 6244 6781 8681 708 1103 529 C
ATOM 2416 N ILE A 305 20.113 397.479 46.916 1.00 86.06 N
ANISOU 2416 N ILE A 305 9858 10316 12524 672 908 533 N
ATOM 2417 CA ILE A 305 20.514 398.861 46.662 1.00 76.13 C
ANISOU 2417 CA ILE A 305 8649 8965 11314 680 860 531 C
ATOM 2418 C ILE A 305 19.676 399.486 45.551 1.00 71.46 C
ANISOU 2418 C ILE A 305 8018 8381 10753 721 882 580 C
ATOM 2419 O ILE A 305 19.119 400.569 45.731 1.00 85.12 O
ANISOU 2419 O ILE A 305 9794 10051 12499 788 881 567 O
ATOM 2420 CB ILE A 305 22.029 398.915 46.335 1.00 81.26 C
ANISOU 2420 CB ILE A 305 9289 9560 12028 592 799 546 C
ATOM 2421 CG1 ILE A 305 22.872 398.622 47.576 1.00 79.86 C
ANISOU 2421 CG1 ILE A 305 9166 9343 11834 573 729 481 C
ATOM 2422 CG2 ILE A 305 22.446 400.217 45.652 1.00 81.11 C
ANISOU 2422 CG2 ILE A 305 9284 9438 12096 577 777 580 C
ATOM 2423 CD1 ILE A 305 24.291 398.343 47.259 1.00 73.83 C
ANISOU 2423 CD1 ILE A 305 8344 8546 11161 486 673 497 C
ATOM 2424 N TYR A 306 19.454 398.766 44.451 1.00 70.31 N
ANISOU 2424 N TYR A 306 7798 8311 10606 700 895 627 N
ATOM 2425 CA TYR A 306 18.771 399.320 43.287 1.00 70.77 C
ANISOU 2425 CA TYR A 306 7839 8376 10675 749 885 675 C
ATOM 2426 C TYR A 306 17.264 399.151 43.309 1.00 81.44 C
ANISOU 2426 C TYR A 306 9126 9782 12033 826 895 659 C
ATOM 2427 O TYR A 306 16.570 399.816 42.530 1.00 94.86 O
ANISOU 2427 O TYR A 306 10819 11473 13749 892 863 688 O
ATOM 2428 CB TYR A 306 19.308 398.674 42.006 1.00 63.77 C
ANISOU 2428 CB TYR A 306 6931 7534 9764 707 877 727 C
ATOM 2429 CG TYR A 306 20.701 399.115 41.631 1.00 79.55 C
ANISOU 2429 CG TYR A 306 8972 9464 11788 647 893 773 C
ATOM 2430 CD1 TYR A 306 21.831 398.466 42.133 1.00 84.66 C
ANISOU 2430 CD1 TYR A 306 9596 10107 12464 570 902 754 C
ATOM 2431 CD2 TYR A 306 20.887 400.133 40.711 1.00 80.01 C
ANISOU 2431 CD2 TYR A 306 9084 9458 11859 672 904 847 C
ATOM 2432 CE1 TYR A 306 23.100 398.874 41.770 1.00 82.84 C
ANISOU 2432 CE1 TYR A 306 9368 9807 12300 512 924 800 C
ATOM 2433 CE2 TYR A 306 22.153 400.535 40.334 1.00 91.29 C
ANISOU 2433 CE2 TYR A 306 10531 10812 13343 611 947 906 C
ATOM 2434 CZ TYR A 306 23.252 399.907 40.862 1.00 86.24 C
ANISOU 2434 CZ TYR A 306 9841 10169 12758 528 958 880 C
ATOM 2435 OH TYR A 306 24.493 400.332 40.467 1.00 91.79 O
ANISOU 2435 OH TYR A 306 10530 10790 13557 466 1009 943 O
ATOM 2436 N ILE A 307 16.737 398.285 44.159 1.00 73.37 N
ANISOU 2436 N ILE A 307 8053 8812 11014 824 940 621 N
ATOM 2437 CA ILE A 307 15.310 398.002 44.115 1.00 77.37 C
ANISOU 2437 CA ILE A 307 8456 9367 11573 883 962 613 C
ATOM 2438 C ILE A 307 14.716 398.301 45.482 1.00 73.35 C
ANISOU 2438 C ILE A 307 7961 8836 11073 943 1055 580 C
ATOM 2439 O ILE A 307 13.806 399.123 45.616 1.00 79.66 O
ANISOU 2439 O ILE A 307 8738 9611 11917 1035 1079 574 O
ATOM 2440 CB ILE A 307 15.014 396.567 43.649 1.00 71.35 C
ANISOU 2440 CB ILE A 307 7592 8681 10837 829 950 613 C
ATOM 2441 CG1 ILE A 307 15.418 396.414 42.188 1.00 75.82 C
ANISOU 2441 CG1 ILE A 307 8170 9267 11371 808 856 636 C
ATOM 2442 CG2 ILE A 307 13.538 396.282 43.738 1.00 64.06 C
ANISOU 2442 CG2 ILE A 307 6532 7791 10018 878 973 602 C
ATOM 2443 CD1 ILE A 307 15.471 395.000 41.739 1.00 86.24 C
ANISOU 2443 CD1 ILE A 307 9432 10641 12696 748 831 619 C
ATOM 2444 N MET A 308 15.231 397.630 46.507 1.00 73.32 N
ANISOU 2444 N MET A 308 8007 8837 11017 905 1112 561 N
ATOM 2445 CA MET A 308 14.698 397.780 47.853 1.00 78.99 C
ANISOU 2445 CA MET A 308 8772 9536 11704 975 1221 534 C
ATOM 2446 C MET A 308 14.881 399.195 48.425 1.00 78.44 C
ANISOU 2446 C MET A 308 8833 9379 11590 1056 1210 493 C
ATOM 2447 O MET A 308 14.155 399.572 49.350 1.00 77.97 O
ANISOU 2447 O MET A 308 8814 9301 11510 1154 1309 467 O
ATOM 2448 CB MET A 308 15.402 396.751 48.735 1.00 87.22 C
ANISOU 2448 CB MET A 308 9879 10593 12668 923 1259 530 C
ATOM 2449 CG MET A 308 14.797 395.358 48.649 1.00104.87 C
ANISOU 2449 CG MET A 308 11993 12892 14960 878 1330 567 C
ATOM 2450 SD MET A 308 13.659 394.900 49.933 1.00127.69 S
ANISOU 2450 SD MET A 308 14867 15791 17858 951 1532 590 S
ATOM 2451 CE MET A 308 14.696 395.095 51.384 1.00124.51 C
ANISOU 2451 CE MET A 308 14714 15340 17255 997 1551 559 C
ATOM 2452 N MET A 309 15.840 399.978 47.922 1.00 88.15 N
ANISOU 2452 N MET A 309 10134 10544 12814 1020 1102 487 N
ATOM 2453 CA MET A 309 16.005 401.375 48.326 1.00 99.76 C
ANISOU 2453 CA MET A 309 11721 11906 14276 1086 1071 445 C
ATOM 2454 C MET A 309 15.256 402.357 47.431 1.00106.29 C
ANISOU 2454 C MET A 309 12501 12700 15182 1151 1052 475 C
ATOM 2455 O MET A 309 15.172 403.541 47.769 1.00117.74 O
ANISOU 2455 O MET A 309 14043 14051 16641 1225 1039 441 O
ATOM 2456 CB MET A 309 17.489 401.749 48.413 1.00 97.83 C
ANISOU 2456 CB MET A 309 11573 11579 14018 1006 965 422 C
ATOM 2457 CG MET A 309 18.204 401.006 49.536 1.00101.13 C
ANISOU 2457 CG MET A 309 12070 12006 14350 978 955 373 C
ATOM 2458 SD MET A 309 19.851 401.621 49.964 1.00106.93 S
ANISOU 2458 SD MET A 309 12913 12615 15100 910 801 314 S
ATOM 2459 CE MET A 309 20.030 400.881 51.591 1.00107.96 C
ANISOU 2459 CE MET A 309 13180 12763 15076 964 799 240 C
ATOM 2460 N ASN A 310 14.749 401.888 46.298 1.00106.26 N
ANISOU 2460 N ASN A 310 12373 12768 15232 1133 1034 533 N
ATOM 2461 CA ASN A 310 13.842 402.647 45.443 1.00101.69 C
ANISOU 2461 CA ASN A 310 11740 12175 14723 1216 1004 566 C
ATOM 2462 C ASN A 310 12.509 402.854 46.173 1.00 94.52 C
ANISOU 2462 C ASN A 310 10768 11279 13865 1337 1096 534 C
ATOM 2463 O ASN A 310 11.916 401.889 46.659 1.00 95.55 O
ANISOU 2463 O ASN A 310 10802 11487 14016 1332 1181 527 O
ATOM 2464 CB ASN A 310 13.653 401.868 44.134 1.00101.61 C
ANISOU 2464 CB ASN A 310 11624 12248 14734 1171 940 619 C
ATOM 2465 CG ASN A 310 12.801 402.586 43.116 1.00109.30 C
ANISOU 2465 CG ASN A 310 12558 13209 15762 1264 870 657 C
ATOM 2466 OD1 ASN A 310 11.709 403.075 43.418 1.00114.36 O
ANISOU 2466 OD1 ASN A 310 13137 13839 16476 1371 894 640 O
ATOM 2467 ND2 ASN A 310 13.267 402.583 41.866 1.00101.86 N
ANISOU 2467 ND2 ASN A 310 11651 12272 14781 1235 785 713 N
ATOM 2468 N LYS A 311 12.059 404.112 46.283 1.00100.52 N
ANISOU 2468 N LYS A 311 11581 11953 14659 1448 1095 519 N
ATOM 2469 CA LYS A 311 10.899 404.430 47.117 1.00117.19 C
ANISOU 2469 CA LYS A 311 13650 14061 16818 1582 1209 482 C
ATOM 2470 C LYS A 311 9.646 403.692 46.664 1.00115.26 C
ANISOU 2470 C LYS A 311 13184 13914 16694 1614 1244 515 C
ATOM 2471 O LYS A 311 8.832 403.263 47.497 1.00106.32 O
ANISOU 2471 O LYS A 311 11967 12819 15609 1668 1388 499 O
ATOM 2472 CB LYS A 311 10.611 405.944 47.071 1.00125.66 C
ANISOU 2472 CB LYS A 311 14808 15013 17925 1705 1180 465 C
ATOM 2473 CG LYS A 311 9.744 406.476 48.217 1.00127.04 C
ANISOU 2473 CG LYS A 311 15009 15149 18112 1857 1319 404 C
ATOM 2474 CD LYS A 311 9.738 408.012 48.234 1.00130.70 C
ANISOU 2474 CD LYS A 311 15604 15464 18594 1968 1273 372 C
ATOM 2475 CE LYS A 311 8.896 408.570 49.385 1.00132.02 C
ANISOU 2475 CE LYS A 311 15819 15585 18759 2140 1421 299 C
ATOM 2476 NZ LYS A 311 8.871 410.063 49.409 1.00130.91 N
ANISOU 2476 NZ LYS A 311 15813 15282 18643 2257 1371 258 N
ATOM 2477 N GLN A 312 9.450 403.565 45.346 1.00114.00 N
ANISOU 2477 N GLN A 312 12933 13787 16595 1590 1113 562 N
ATOM 2478 CA GLN A 312 8.249 402.890 44.862 1.00120.94 C
ANISOU 2478 CA GLN A 312 13590 14745 17617 1619 1101 577 C
ATOM 2479 C GLN A 312 8.202 401.431 45.284 1.00117.72 C
ANISOU 2479 C GLN A 312 13078 14419 17230 1517 1180 574 C
ATOM 2480 O GLN A 312 7.261 401.010 45.970 1.00121.92 O
ANISOU 2480 O GLN A 312 13469 14978 17876 1557 1312 569 O
ATOM 2481 CB GLN A 312 8.074 402.968 43.333 1.00132.22 C
ANISOU 2481 CB GLN A 312 14968 16191 19078 1624 911 616 C
ATOM 2482 CG GLN A 312 8.376 404.224 42.593 1.00136.49 C
ANISOU 2482 CG GLN A 312 15642 16648 19569 1696 808 650 C
ATOM 2483 CD GLN A 312 8.634 403.894 41.141 1.00141.03 C
ANISOU 2483 CD GLN A 312 16231 17258 20094 1660 642 696 C
ATOM 2484 OE1 GLN A 312 9.787 403.660 40.745 1.00148.21 O
ANISOU 2484 OE1 GLN A 312 17269 18164 20880 1563 624 723 O
ATOM 2485 NE2 GLN A 312 7.570 403.774 40.364 1.00133.74 N
ANISOU 2485 NE2 GLN A 312 15172 16372 19270 1741 521 700 N
ATOM 2486 N PHE A 313 9.229 400.650 44.910 1.00104.23 N
ANISOU 2486 N PHE A 313 11437 12741 15424 1387 1118 583 N
ATOM 2487 CA PHE A 313 9.222 399.211 45.165 1.00 94.17 C
ANISOU 2487 CA PHE A 313 10071 11532 14178 1287 1170 584 C
ATOM 2488 C PHE A 313 9.007 398.937 46.639 1.00 96.38 C
ANISOU 2488 C PHE A 313 10366 11807 14449 1309 1371 576 C
ATOM 2489 O PHE A 313 8.229 398.051 46.999 1.00 98.99 O
ANISOU 2489 O PHE A 313 10545 12173 14893 1292 1473 592 O
ATOM 2490 CB PHE A 313 10.551 398.591 44.707 1.00 82.83 C
ANISOU 2490 CB PHE A 313 8747 10110 12615 1166 1091 590 C
ATOM 2491 CG PHE A 313 10.672 398.363 43.200 1.00 94.37 C
ANISOU 2491 CG PHE A 313 10179 11599 14078 1135 923 604 C
ATOM 2492 CD1 PHE A 313 10.179 397.198 42.615 1.00100.28 C
ANISOU 2492 CD1 PHE A 313 10792 12402 14908 1082 862 593 C
ATOM 2493 CD2 PHE A 313 11.360 399.267 42.383 1.00 96.42 C
ANISOU 2493 CD2 PHE A 313 10569 11820 14247 1158 831 629 C
ATOM 2494 CE1 PHE A 313 10.320 396.965 41.227 1.00 94.32 C
ANISOU 2494 CE1 PHE A 313 10049 11669 14119 1072 695 592 C
ATOM 2495 CE2 PHE A 313 11.506 399.040 41.003 1.00 89.38 C
ANISOU 2495 CE2 PHE A 313 9690 10953 13318 1149 696 650 C
ATOM 2496 CZ PHE A 313 10.984 397.887 40.428 1.00 82.59 C
ANISOU 2496 CZ PHE A 313 8714 10156 12513 1114 621 624 C
ATOM 2497 N ARG A 314 9.672 399.698 47.508 1.00 91.39 N
ANISOU 2497 N ARG A 314 9923 11119 13683 1352 1430 551 N
ATOM 2498 CA ARG A 314 9.578 399.424 48.936 1.00 97.12 C
ANISOU 2498 CA ARG A 314 10719 11838 14346 1390 1614 541 C
ATOM 2499 C ARG A 314 8.128 399.465 49.396 1.00109.72 C
ANISOU 2499 C ARG A 314 12156 13445 16086 1496 1780 557 C
ATOM 2500 O ARG A 314 7.658 398.547 50.077 1.00110.19 O
ANISOU 2500 O ARG A 314 12141 13536 16190 1481 1943 590 O
ATOM 2501 CB ARG A 314 10.466 400.393 49.714 1.00100.29 C
ANISOU 2501 CB ARG A 314 11362 12162 14582 1440 1606 490 C
ATOM 2502 CG ARG A 314 10.983 399.858 51.041 1.00101.50 C
ANISOU 2502 CG ARG A 314 11668 12310 14587 1441 1718 473 C
ATOM 2503 CD ARG A 314 11.589 400.978 51.893 1.00112.57 C
ANISOU 2503 CD ARG A 314 13306 13620 15845 1529 1696 398 C
ATOM 2504 NE ARG A 314 12.385 401.905 51.080 1.00117.61 N
ANISOU 2504 NE ARG A 314 13995 14192 16499 1486 1509 372 N
ATOM 2505 CZ ARG A 314 11.998 403.109 50.664 1.00119.03 C
ANISOU 2505 CZ ARG A 314 14179 14304 16743 1564 1468 353 C
ATOM 2506 NH1 ARG A 314 10.799 403.582 50.977 1.00128.83 N
ANISOU 2506 NH1 ARG A 314 15366 15539 18043 1702 1591 347 N
ATOM 2507 NH2 ARG A 314 12.818 403.839 49.921 1.00113.60 N
ANISOU 2507 NH2 ARG A 314 13544 13545 16072 1508 1314 350 N
ATOM 2508 N ASN A 315 7.390 400.511 49.004 1.00116.84 N
ANISOU 2508 N ASN A 315 12995 14316 17082 1607 1750 544 N
ATOM 2509 CA ASN A 315 6.009 400.634 49.465 1.00116.68 C
ANISOU 2509 CA ASN A 315 12805 14302 17227 1724 1921 559 C
ATOM 2510 C ASN A 315 5.116 399.588 48.811 1.00 99.45 C
ANISOU 2510 C ASN A 315 10334 12180 15274 1654 1908 601 C
ATOM 2511 O ASN A 315 4.259 398.991 49.472 1.00104.02 O
ANISOU 2511 O ASN A 315 10762 12773 15986 1676 2107 636 O
ATOM 2512 CB ASN A 315 5.464 402.029 49.152 1.00127.61 C
ANISOU 2512 CB ASN A 315 14186 15628 18671 1870 1871 531 C
ATOM 2513 CG ASN A 315 6.315 403.138 49.725 1.00133.95 C
ANISOU 2513 CG ASN A 315 15269 16346 19280 1935 1857 477 C
ATOM 2514 OD1 ASN A 315 7.383 402.895 50.279 1.00142.81 O
ANISOU 2514 OD1 ASN A 315 16583 17454 20223 1865 1853 454 O
ATOM 2515 ND2 ASN A 315 5.858 404.375 49.560 1.00129.72 N
ANISOU 2515 ND2 ASN A 315 14754 15740 18793 2070 1829 452 N
ATOM 2516 N CYS A 316 5.345 399.305 47.532 1.00 84.94 N
ANISOU 2516 N CYS A 316 8426 10367 13482 1568 1680 599 N
ATOM 2517 CA CYS A 316 4.620 398.226 46.873 1.00 95.95 C
ANISOU 2517 CA CYS A 316 9568 11804 15084 1488 1622 619 C
ATOM 2518 C CYS A 316 4.924 396.871 47.507 1.00109.26 C
ANISOU 2518 C CYS A 316 11243 13511 16758 1366 1750 648 C
ATOM 2519 O CYS A 316 4.016 396.056 47.701 1.00119.79 O
ANISOU 2519 O CYS A 316 12356 14852 18306 1335 1854 679 O
ATOM 2520 CB CYS A 316 4.962 398.232 45.386 1.00 96.08 C
ANISOU 2520 CB CYS A 316 9582 11837 15087 1437 1339 598 C
ATOM 2521 SG CYS A 316 4.345 399.722 44.549 1.00 90.50 S
ANISOU 2521 SG CYS A 316 8853 11095 14436 1596 1184 586 S
ATOM 2522 N MET A 317 6.192 396.619 47.858 1.00109.22 N
ANISOU 2522 N MET A 317 11468 13505 16523 1298 1746 644 N
ATOM 2523 CA MET A 317 6.551 395.344 48.476 1.00104.84 C
ANISOU 2523 CA MET A 317 10931 12962 15942 1195 1858 678 C
ATOM 2524 C MET A 317 5.881 395.187 49.838 1.00104.43 C
ANISOU 2524 C MET A 317 10861 12894 15925 1265 2150 726 C
ATOM 2525 O MET A 317 5.460 394.082 50.201 1.00104.87 O
ANISOU 2525 O MET A 317 10796 12948 16100 1198 2283 780 O
ATOM 2526 CB MET A 317 8.076 395.206 48.586 1.00114.91 C
ANISOU 2526 CB MET A 317 12454 14235 16971 1128 1778 661 C
ATOM 2527 CG MET A 317 8.681 394.316 47.484 1.00123.11 C
ANISOU 2527 CG MET A 317 13456 15298 18021 1000 1593 650 C
ATOM 2528 SD MET A 317 10.404 394.497 46.928 1.00117.85 S
ANISOU 2528 SD MET A 317 13011 14632 17134 937 1426 622 S
ATOM 2529 CE MET A 317 10.821 396.147 47.460 1.00114.27 C
ANISOU 2529 CE MET A 317 12735 14133 16548 1047 1439 598 C
ATOM 2530 N VAL A 318 5.828 396.266 50.630 1.00102.34 N
ANISOU 2530 N VAL A 318 10735 12604 15545 1403 2264 709 N
ATOM 2531 CA VAL A 318 5.130 396.232 51.919 1.00103.09 C
ANISOU 2531 CA VAL A 318 10838 12682 15650 1505 2567 754 C
ATOM 2532 C VAL A 318 3.647 395.927 51.731 1.00116.22 C
ANISOU 2532 C VAL A 318 12170 14349 17639 1528 2698 803 C
ATOM 2533 O VAL A 318 3.063 395.108 52.453 1.00124.60 O
ANISOU 2533 O VAL A 318 13132 15403 18808 1515 2940 879 O
ATOM 2534 CB VAL A 318 5.331 397.558 52.673 1.00 95.63 C
ANISOU 2534 CB VAL A 318 10118 11700 14518 1668 2633 703 C
ATOM 2535 CG1 VAL A 318 4.480 397.590 53.931 1.00 96.11 C
ANISOU 2535 CG1 VAL A 318 10188 11744 14586 1805 2966 748 C
ATOM 2536 CG2 VAL A 318 6.789 397.749 53.020 1.00 96.61 C
ANISOU 2536 CG2 VAL A 318 10550 11804 14353 1636 2512 655 C
ATOM 2537 N THR A 319 3.010 396.613 50.778 1.00115.44 N
ANISOU 2537 N THR A 319 11894 14254 17715 1569 2542 765 N
ATOM 2538 CA THR A 319 1.604 396.359 50.469 1.00108.72 C
ANISOU 2538 CA THR A 319 10690 13402 17216 1589 2610 798 C
ATOM 2539 C THR A 319 1.372 394.898 50.108 1.00104.79 C
ANISOU 2539 C THR A 319 9990 12909 16916 1422 2589 840 C
ATOM 2540 O THR A 319 0.384 394.292 50.537 1.00111.49 O
ANISOU 2540 O THR A 319 10598 13736 18026 1412 2795 905 O
ATOM 2541 CB THR A 319 1.131 397.275 49.344 1.00108.29 C
ANISOU 2541 CB THR A 319 10506 13349 17291 1655 2368 742 C
ATOM 2542 OG1 THR A 319 1.140 398.634 49.799 1.00108.97 O
ANISOU 2542 OG1 THR A 319 10749 13408 17248 1825 2433 712 O
ATOM 2543 CG2 THR A 319 -0.268 396.908 48.929 1.00118.71 C
ANISOU 2543 CG2 THR A 319 11435 14665 19005 1661 2382 765 C
ATOM 2544 N THR A 320 2.285 394.312 49.335 1.00 95.68 N
ANISOU 2544 N THR A 320 8930 11772 15654 1290 2353 806 N
ATOM 2545 CA THR A 320 2.100 392.944 48.869 1.00 95.82 C
ANISOU 2545 CA THR A 320 8769 11779 15859 1133 2291 827 C
ATOM 2546 C THR A 320 2.336 391.934 49.985 1.00106.24 C
ANISOU 2546 C THR A 320 10162 13073 17134 1070 2557 911 C
ATOM 2547 O THR A 320 1.599 390.946 50.100 1.00115.53 O
ANISOU 2547 O THR A 320 11110 14210 18577 987 2670 968 O
ATOM 2548 CB THR A 320 3.052 392.682 47.702 1.00 86.85 C
ANISOU 2548 CB THR A 320 7744 10665 14590 1037 1972 759 C
ATOM 2549 OG1 THR A 320 2.626 393.437 46.564 1.00 93.93 O
ANISOU 2549 OG1 THR A 320 8540 11578 15573 1094 1727 697 O
ATOM 2550 CG2 THR A 320 3.095 391.210 47.345 1.00 91.04 C
ANISOU 2550 CG2 THR A 320 8164 11172 15255 877 1913 767 C
ATOM 2551 N LEU A 321 3.328 392.174 50.833 1.00107.60 N
ANISOU 2551 N LEU A 321 10648 13253 16983 1112 2655 923 N
ATOM 2552 CA LEU A 321 3.621 391.263 51.931 1.00111.26 C
ANISOU 2552 CA LEU A 321 11229 13689 17357 1077 2895 1009 C
ATOM 2553 C LEU A 321 2.505 391.308 52.976 1.00122.04 C
ANISOU 2553 C LEU A 321 12476 15025 18870 1174 3255 1101 C
ATOM 2554 O LEU A 321 2.187 390.300 53.606 1.00127.91 O
ANISOU 2554 O LEU A 321 13158 15727 19715 1118 3479 1203 O
ATOM 2555 CB LEU A 321 4.985 391.595 52.551 1.00104.54 C
ANISOU 2555 CB LEU A 321 10750 12852 16117 1117 2867 985 C
ATOM 2556 CG LEU A 321 6.132 391.193 51.615 1.00 97.32 C
ANISOU 2556 CG LEU A 321 9925 11955 15097 996 2572 924 C
ATOM 2557 CD1 LEU A 321 7.509 391.512 52.192 1.00 88.06 C
ANISOU 2557 CD1 LEU A 321 9081 10788 13589 1027 2522 897 C
ATOM 2558 CD2 LEU A 321 6.002 389.720 51.235 1.00 91.73 C
ANISOU 2558 CD2 LEU A 321 9065 11219 14567 846 2555 967 C
ATOM 2559 N CYS A 322 1.899 392.478 53.140 1.00131.39 N
ANISOU 2559 N CYS A 322 13625 16222 20074 1325 3324 1073 N
ATOM 2560 CA CYS A 322 0.803 392.632 54.064 1.00146.92 C
ANISOU 2560 CA CYS A 322 15468 18164 22192 1440 3680 1156 C
ATOM 2561 C CYS A 322 -0.591 392.449 53.474 1.00143.70 C
ANISOU 2561 C CYS A 322 14621 17735 22243 1414 3713 1182 C
ATOM 2562 O CYS A 322 -1.606 392.965 53.951 1.00150.15 O
ANISOU 2562 O CYS A 322 15326 18537 23188 1522 3906 1211 O
ATOM 2563 CB CYS A 322 0.820 393.964 54.795 1.00158.93 C
ANISOU 2563 CB CYS A 322 17201 19695 23492 1649 3803 1117 C
ATOM 2564 SG CYS A 322 1.311 393.774 56.480 1.00164.12 S
ANISOU 2564 SG CYS A 322 18223 20331 23804 1759 4145 1191 S
ATOM 2565 N CYS A 323 -0.624 391.675 52.394 1.00132.04 N
ANISOU 2565 N CYS A 323 12942 16250 20977 1249 3455 1151 N
ATOM 2566 CA CYS A 323 -1.861 391.198 51.793 1.00124.60 C
ANISOU 2566 CA CYS A 323 11629 15268 20446 1164 3390 1158 C
ATOM 2567 C CYS A 323 -2.781 392.375 51.469 1.00112.86 C
ANISOU 2567 C CYS A 323 9999 13799 19084 1298 3322 1103 C
ATOM 2568 O CYS A 323 -3.989 392.323 51.700 1.00107.31 O
ANISOU 2568 O CYS A 323 9097 13059 18618 1302 3428 1136 O
ATOM 2569 CB CYS A 323 -2.559 390.197 52.724 1.00130.40 C
ANISOU 2569 CB CYS A 323 12312 15929 21305 1086 3676 1276 C
ATOM 2570 SG CYS A 323 -1.432 389.230 53.781 1.00136.38 S
ANISOU 2570 SG CYS A 323 13381 16664 21771 1039 3916 1382 S
ATOM 2571 N GLY A 324 -2.183 393.436 50.927 1.00105.90 N
ANISOU 2571 N GLY A 324 9219 12965 18052 1411 3147 1024 N
ATOM 2572 CA GLY A 324 -2.915 394.586 50.457 1.00100.28 C
ANISOU 2572 CA GLY A 324 8390 12265 17449 1545 3030 965 C
ATOM 2573 C GLY A 324 -3.142 395.717 51.437 1.00129.82 C
ANISOU 2573 C GLY A 324 12287 16006 21032 1743 3279 978 C
ATOM 2574 O GLY A 324 -3.521 396.813 51.002 1.00129.64 O
ANISOU 2574 O GLY A 324 12216 15988 21054 1874 3160 921 O
ATOM 2575 N LYS A 325 -2.857 395.536 52.720 1.00158.41 N
ANISOU 2575 N LYS A 325 16124 19616 24448 1785 3603 1044 N
ATOM 2576 CA LYS A 325 -3.174 396.548 53.714 1.00167.30 C
ANISOU 2576 CA LYS A 325 17409 20733 25426 1983 3852 1047 C
ATOM 2577 C LYS A 325 -1.880 397.147 54.248 1.00168.40 C
ANISOU 2577 C LYS A 325 17923 20879 25182 2093 3898 1010 C
ATOM 2578 O LYS A 325 -0.850 396.474 54.312 1.00165.46 O
ANISOU 2578 O LYS A 325 17761 20519 24588 1968 3805 1013 O
ATOM 2579 CB LYS A 325 -3.983 395.937 54.871 1.00170.75 C
ANISOU 2579 CB LYS A 325 17829 21137 25910 1979 4205 1152 C
ATOM 2580 CG LYS A 325 -5.400 395.452 54.526 1.00173.44 C
ANISOU 2580 CG LYS A 325 17800 21448 26652 1893 4205 1193 C
ATOM 2581 CD LYS A 325 -6.448 396.560 54.540 1.00175.46 C
ANISOU 2581 CD LYS A 325 17921 21701 27045 2053 4243 1157 C
ATOM 2582 CE LYS A 325 -7.855 395.984 54.371 1.00176.71 C
ANISOU 2582 CE LYS A 325 17716 21819 27609 1968 4288 1210 C
ATOM 2583 NZ LYS A 325 -8.004 395.222 53.099 1.00175.68 N
ANISOU 2583 NZ LYS A 325 17315 21680 27754 1785 3946 1171 N
ATOM 2584 N ASN A 326 -1.938 398.426 54.615 1.00173.35 N
ANISOU 2584 N ASN A 326 18706 21490 25668 2285 3946 951 N
ATOM 2585 CA ASN A 326 -0.763 399.153 55.105 1.00174.12 C
ANISOU 2585 CA ASN A 326 19239 21575 25343 2351 3870 876 C
ATOM 2586 C ASN A 326 0.427 399.008 54.152 1.00169.64 C
ANISOU 2586 C ASN A 326 18800 21027 24628 2187 3485 816 C
ATOM 2587 O ASN A 326 1.035 399.997 53.738 1.00164.89 O
ANISOU 2587 O ASN A 326 18369 20405 23877 2231 3269 732 O
ATOM 2588 CB ASN A 326 -0.377 398.675 56.510 1.00174.17 C
ANISOU 2588 CB ASN A 326 19519 21572 25086 2401 4176 930 C
ATOM 2589 CG ASN A 326 0.705 399.536 57.149 1.00171.00 C
ANISOU 2589 CG ASN A 326 19559 21141 24271 2503 4101 835 C
ATOM 2590 OD1 ASN A 326 1.136 400.545 56.586 1.00168.53 O
ANISOU 2590 OD1 ASN A 326 19338 20806 23890 2535 3849 735 O
ATOM 2591 ND2 ASN A 326 1.145 399.139 58.337 1.00168.90 N
ANISOU 2591 ND2 ASN A 326 19575 20866 23734 2557 4312 867 N
TER 2592 ASN A 326
HETATM 2593 C1 NAG B 1 47.553 361.690 40.350 1.00 79.26 C
ANISOU 2593 C1 NAG B 1 7647 8101 14368 2806 1379 157 C
HETATM 2594 C2 NAG B 1 46.621 361.410 39.146 1.00 72.46 C
ANISOU 2594 C2 NAG B 1 7030 7236 13267 2783 1558 50 C
HETATM 2595 C3 NAG B 1 46.041 359.988 39.223 1.00 80.68 C
ANISOU 2595 C3 NAG B 1 8318 8097 14240 2843 1476 -18 C
HETATM 2596 C4 NAG B 1 47.090 358.929 39.559 1.00 86.75 C
ANISOU 2596 C4 NAG B 1 8999 8725 15236 3049 1439 -15 C
HETATM 2597 C5 NAG B 1 47.939 359.352 40.752 1.00 83.19 C
ANISOU 2597 C5 NAG B 1 8309 8304 14994 3060 1262 107 C
HETATM 2598 C6 NAG B 1 49.089 358.413 41.033 1.00 78.41 C
ANISOU 2598 C6 NAG B 1 7576 7572 14644 3283 1222 113 C
HETATM 2599 C7 NAG B 1 45.129 363.071 38.041 1.00 72.36 C
ANISOU 2599 C7 NAG B 1 7169 7437 12886 2533 1715 19 C
HETATM 2600 C8 NAG B 1 44.033 364.060 38.281 1.00 67.03 C
ANISOU 2600 C8 NAG B 1 6573 6865 12031 2326 1636 54 C
HETATM 2601 N2 NAG B 1 45.549 362.396 39.122 1.00 70.05 N
ANISOU 2601 N2 NAG B 1 6819 7045 12752 2580 1534 67 N
HETATM 2602 O3 NAG B 1 45.483 359.649 37.960 1.00 83.07 O
ANISOU 2602 O3 NAG B 1 8811 8380 14373 2874 1645 -146 O
HETATM 2603 O4 NAG B 1 46.396 357.740 39.917 1.00 81.95 O
ANISOU 2603 O4 NAG B 1 8632 7938 14565 3057 1313 -45 O
HETATM 2604 O5 NAG B 1 48.519 360.628 40.480 1.00 75.50 O
ANISOU 2604 O5 NAG B 1 7089 7495 14103 3012 1364 143 O
HETATM 2605 O6 NAG B 1 50.007 358.352 39.948 1.00 86.65 O
ANISOU 2605 O6 NAG B 1 8462 8636 15825 3446 1478 47 O
HETATM 2606 O7 NAG B 1 45.590 362.881 36.924 1.00 79.72 O
ANISOU 2606 O7 NAG B 1 8107 8374 13811 2663 1936 -49 O
HETATM 2607 C1 NAG B 2 46.809 356.561 39.201 1.00 77.84 C
ANISOU 2607 C1 NAG B 2 8197 7266 14112 3253 1419 -150 C
HETATM 2608 C2 NAG B 2 46.399 355.378 40.081 1.00 78.32 C
ANISOU 2608 C2 NAG B 2 8432 7120 14208 3265 1221 -120 C
HETATM 2609 C3 NAG B 2 46.782 354.073 39.404 1.00 80.81 C
ANISOU 2609 C3 NAG B 2 8857 7244 14602 3470 1308 -236 C
HETATM 2610 C4 NAG B 2 46.170 354.013 38.014 1.00 80.84 C
ANISOU 2610 C4 NAG B 2 9035 7258 14424 3464 1486 -401 C
HETATM 2611 C5 NAG B 2 46.604 355.223 37.203 1.00 80.37 C
ANISOU 2611 C5 NAG B 2 8811 7421 14305 3463 1689 -414 C
HETATM 2612 C6 NAG B 2 45.944 355.246 35.843 1.00 80.48 C
ANISOU 2612 C6 NAG B 2 9032 7456 14092 3464 1849 -570 C
HETATM 2613 C7 NAG B 2 46.329 355.834 42.498 1.00 93.39 C
ANISOU 2613 C7 NAG B 2 10262 9042 16179 3129 844 136 C
HETATM 2614 C8 NAG B 2 47.122 355.895 43.766 1.00 77.74 C
ANISOU 2614 C8 NAG B 2 8147 7048 14344 3201 640 265 C
HETATM 2615 N2 NAG B 2 47.004 355.474 41.401 1.00 78.54 N
ANISOU 2615 N2 NAG B 2 8316 7141 14386 3287 1029 24 N
HETATM 2616 O3 NAG B 2 46.284 352.997 40.191 1.00 82.30 O
ANISOU 2616 O3 NAG B 2 9228 7223 14818 3460 1131 -199 O
HETATM 2617 O4 NAG B 2 46.655 352.881 37.309 1.00 87.94 O
ANISOU 2617 O4 NAG B 2 10033 7988 15394 3682 1585 -526 O
HETATM 2618 O5 NAG B 2 46.199 356.417 37.886 1.00 77.92 O
ANISOU 2618 O5 NAG B 2 8391 7276 13938 3257 1595 -295 O
HETATM 2619 O6 NAG B 2 46.383 356.286 34.981 1.00 80.50 O
ANISOU 2619 O6 NAG B 2 8917 7646 14023 3494 2074 -577 O
HETATM 2620 O7 NAG B 2 45.127 356.090 42.470 1.00102.88 O
ANISOU 2620 O7 NAG B 2 11628 10268 17193 2947 838 131 O
HETATM 2621 C1 BMA B 3 45.661 351.899 37.066 1.00106.53 C
ANISOU 2621 C1 BMA B 3 12679 10148 17651 3638 1505 -632 C
HETATM 2622 C2 BMA B 3 46.346 350.851 36.334 1.00119.09 C
ANISOU 2622 C2 BMA B 3 14346 11577 19327 3889 1619 -765 C
HETATM 2623 C3 BMA B 3 45.269 349.987 35.774 1.00130.59 C
ANISOU 2623 C3 BMA B 3 16116 12845 20658 3837 1558 -919 C
HETATM 2624 C4 BMA B 3 44.485 349.270 36.921 1.00143.65 C
ANISOU 2624 C4 BMA B 3 17878 14307 22394 3689 1318 -823 C
HETATM 2625 C5 BMA B 3 44.210 350.221 38.150 1.00140.90 C
ANISOU 2625 C5 BMA B 3 17373 14116 22046 3487 1196 -609 C
HETATM 2626 C6 BMA B 3 44.079 349.479 39.500 1.00143.41 C
ANISOU 2626 C6 BMA B 3 17734 14254 22501 3453 1008 -455 C
HETATM 2627 O2 BMA B 3 47.190 350.078 37.185 1.00122.27 O
ANISOU 2627 O2 BMA B 3 14650 11838 19969 4036 1530 -678 O
HETATM 2628 O3 BMA B 3 45.860 349.061 34.873 1.00124.23 O
ANISOU 2628 O3 BMA B 3 15422 11891 19888 4087 1686 -1083 O
HETATM 2629 O4 BMA B 3 43.231 348.811 36.442 1.00147.62 O
ANISOU 2629 O4 BMA B 3 18631 14678 22780 3553 1244 -948 O
HETATM 2630 O5 BMA B 3 45.218 351.304 38.274 1.00131.08 O
ANISOU 2630 O5 BMA B 3 15852 13109 20843 3547 1287 -521 O
HETATM 2631 O6 BMA B 3 45.376 349.371 40.098 1.00155.54 O
ANISOU 2631 O6 BMA B 3 19087 15798 24212 3645 993 -358 O
HETATM 2632 C1 MAN B 4 45.830 349.322 33.464 1.00126.57 C
ANISOU 2632 C1 MAN B 4 15836 12265 19991 4182 1882 -1259 C
HETATM 2633 C2 MAN B 4 46.229 347.924 33.019 1.00128.71 C
ANISOU 2633 C2 MAN B 4 16279 12271 20352 4419 1909 -1412 C
HETATM 2634 C3 MAN B 4 47.767 347.726 32.777 1.00133.41 C
ANISOU 2634 C3 MAN B 4 16688 12884 21118 4724 2128 -1402 C
HETATM 2635 C4 MAN B 4 48.478 349.009 32.298 1.00129.66 C
ANISOU 2635 C4 MAN B 4 15977 12699 20589 4762 2373 -1335 C
HETATM 2636 C5 MAN B 4 48.100 350.087 33.232 1.00133.51 C
ANISOU 2636 C5 MAN B 4 16275 13367 21086 4499 2236 -1147 C
HETATM 2637 C6 MAN B 4 48.907 351.409 33.019 1.00126.77 C
ANISOU 2637 C6 MAN B 4 15127 12781 20258 4511 2446 -1039 C
HETATM 2638 O2 MAN B 4 45.643 347.706 31.740 1.00130.11 O
ANISOU 2638 O2 MAN B 4 16731 12403 20301 4468 1980 -1637 O
HETATM 2639 O3 MAN B 4 48.050 346.621 31.909 1.00135.88 O
ANISOU 2639 O3 MAN B 4 17215 12990 21422 4973 2228 -1602 O
HETATM 2640 O4 MAN B 4 49.882 348.825 32.327 1.00126.27 O
ANISOU 2640 O4 MAN B 4 15312 12277 20386 5007 2542 -1287 O
HETATM 2641 O5 MAN B 4 46.699 350.329 33.039 1.00140.98 O
ANISOU 2641 O5 MAN B 4 17447 14323 21797 4269 2104 -1207 O
HETATM 2642 O6 MAN B 4 48.453 352.452 33.892 1.00113.15 O
ANISOU 2642 O6 MAN B 4 13255 11213 18523 4254 2295 -881 O
HETATM 2643 C1 MAN B 5 45.263 348.858 41.453 1.00161.75 C
ANISOU 2643 C1 MAN B 5 19922 16449 25088 3614 804 -187 C
HETATM 2644 C2 MAN B 5 46.746 348.740 42.050 1.00161.11 C
ANISOU 2644 C2 MAN B 5 19630 16374 25209 3849 757 -97 C
HETATM 2645 C3 MAN B 5 47.416 347.365 41.791 1.00167.40 C
ANISOU 2645 C3 MAN B 5 20506 16917 26183 4098 771 -167 C
HETATM 2646 C4 MAN B 5 46.425 346.186 41.905 1.00164.92 C
ANISOU 2646 C4 MAN B 5 20498 16314 25848 4031 700 -190 C
HETATM 2647 C5 MAN B 5 45.248 346.454 40.969 1.00160.86 C
ANISOU 2647 C5 MAN B 5 20128 15836 25155 3836 789 -334 C
HETATM 2648 C6 MAN B 5 44.275 345.298 40.845 1.00141.35 C
ANISOU 2648 C6 MAN B 5 17934 13070 22703 3765 732 -400 C
HETATM 2649 O2 MAN B 5 46.782 348.937 43.466 1.00158.91 O
ANISOU 2649 O2 MAN B 5 19322 16103 24953 3797 563 100 O
HETATM 2650 O3 MAN B 5 48.531 347.156 42.654 1.00173.17 O
ANISOU 2650 O3 MAN B 5 21075 17616 27104 4282 656 -45 O
HETATM 2651 O4 MAN B 5 47.060 344.969 41.534 1.00161.48 O
ANISOU 2651 O4 MAN B 5 20139 15641 25576 4270 727 -279 O
HETATM 2652 O5 MAN B 5 44.528 347.616 41.464 1.00167.29 O
ANISOU 2652 O5 MAN B 5 20877 16865 25819 3595 747 -228 O
HETATM 2653 O6 MAN B 5 43.588 345.456 39.606 1.00126.36 O
ANISOU 2653 O6 MAN B 5 16134 11202 20674 3686 826 -606 O
HETATM 2654 C1 PLM A 401 3.019 393.722 56.295 1.00138.49 C
ANISOU 2654 C1 PLM A 401 15325 17103 20192 1679 3834 1109 C
HETATM 2655 O2 PLM A 401 3.627 394.412 55.479 1.00125.07 O
ANISOU 2655 O2 PLM A 401 13673 15421 18425 1655 3534 1006 O
HETATM 2656 C2 PLM A 401 3.529 392.418 56.834 1.00137.10 C
ANISOU 2656 C2 PLM A 401 15255 16909 19927 1580 3933 1200 C
HETATM 2657 C3 PLM A 401 2.542 391.262 56.909 1.00138.39 C
ANISOU 2657 C3 PLM A 401 15135 17039 20408 1492 4169 1332 C
HETATM 2658 C4 PLM A 401 2.962 390.365 58.056 1.00132.54 C
ANISOU 2658 C4 PLM A 401 14632 16263 19464 1503 4408 1446 C
HETATM 2659 C5 PLM A 401 4.396 389.921 57.838 1.00119.20 C
ANISOU 2659 C5 PLM A 401 13184 14583 17522 1409 4129 1393 C
HETATM 2660 C6 PLM A 401 4.990 389.377 59.114 1.00114.35 C
ANISOU 2660 C6 PLM A 401 12904 13940 16606 1482 4322 1481 C
HETATM 2661 C7 PLM A 401 5.795 388.122 58.914 1.00109.90 C
ANISOU 2661 C7 PLM A 401 12390 13348 16020 1331 4197 1526 C
HETATM 2662 C8 PLM A 401 7.153 388.461 58.358 1.00105.43 C
ANISOU 2662 C8 PLM A 401 11994 12819 15246 1288 3819 1394 C
HETATM 2663 C9 PLM A 401 8.183 387.460 58.829 1.00106.96 C
ANISOU 2663 C9 PLM A 401 12412 12982 15247 1244 3770 1445 C
HETATM 2664 CA PLM A 401 9.524 387.748 58.189 1.00112.20 C
ANISOU 2664 CA PLM A 401 13190 13678 15763 1190 3400 1317 C
HETATM 2665 CB PLM A 401 10.612 386.925 58.841 1.00110.59 C
ANISOU 2665 CB PLM A 401 13243 13443 15333 1190 3348 1359 C
HETATM 2666 CC PLM A 401 10.737 385.520 58.304 1.00105.91 C
ANISOU 2666 CC PLM A 401 12509 12809 14922 1034 3315 1429 C
HETATM 2667 CD PLM A 401 11.831 384.827 59.087 1.00 99.99 C
ANISOU 2667 CD PLM A 401 12046 12024 13921 1072 3268 1473 C
HETATM 2668 CE PLM A 401 12.344 383.594 58.386 1.00 94.91 C
ANISOU 2668 CE PLM A 401 11298 11342 13422 921 3136 1497 C
HETATM 2669 CF PLM A 401 13.678 383.198 58.972 1.00 90.14 C
ANISOU 2669 CF PLM A 401 10972 10718 12558 972 2991 1495 C
HETATM 2670 CG PLM A 401 14.205 381.925 58.367 1.00 91.61 C
ANISOU 2670 CG PLM A 401 11074 10853 12879 845 2881 1524 C
HETATM 2671 C10 DNZ A 407 31.655 388.327 35.445 1.00135.32 C
ANISOU 2671 C10 DNZ A 407 15718 16773 18923 581 1703 888 C
HETATM 2672 C13 DNZ A 407 33.056 390.288 36.189 1.00144.44 C
ANISOU 2672 C13 DNZ A 407 16663 17809 20409 461 1780 1024 C
HETATM 2673 C15 DNZ A 407 33.187 392.694 36.475 1.00130.63 C
ANISOU 2673 C15 DNZ A 407 14863 15936 18833 360 1796 1144 C
HETATM 2674 C16 DNZ A 407 33.027 392.500 37.837 1.00125.80 C
ANISOU 2674 C16 DNZ A 407 14190 15315 18293 305 1601 1052 C
HETATM 2675 C18 DNZ A 407 32.918 391.247 38.403 1.00130.22 C
ANISOU 2675 C18 DNZ A 407 14740 15930 18806 325 1508 964 C
HETATM 2676 C19 DNZ A 407 32.955 390.135 37.571 1.00138.13 C
ANISOU 2676 C19 DNZ A 407 15789 16993 19701 397 1600 954 C
HETATM 2677 C21 DNZ A 407 39.987 389.199 34.738 1.00157.63 C
ANISOU 2677 C21 DNZ A 407 17485 19259 23147 520 2613 1318 C
HETATM 2678 C22 DNZ A 407 40.079 389.761 36.017 1.00160.07 C
ANISOU 2678 C22 DNZ A 407 17660 19508 23650 402 2373 1275 C
HETATM 2679 C24 DNZ A 407 41.268 390.159 36.526 1.00163.09 C
ANISOU 2679 C24 DNZ A 407 17774 19796 24397 330 2366 1310 C
HETATM 2680 C25 DNZ A 407 42.347 389.942 35.671 1.00163.27 C
ANISOU 2680 C25 DNZ A 407 17648 19791 24595 381 2644 1403 C
HETATM 2681 C26 DNZ A 407 42.328 389.181 34.563 1.00162.16 C
ANISOU 2681 C26 DNZ A 407 17627 19719 24266 511 2883 1434 C
HETATM 2682 C27 DNZ A 407 41.090 388.854 34.002 1.00158.89 C
ANISOU 2682 C27 DNZ A 407 17520 19397 23454 585 2871 1392 C
HETATM 2683 C1 DNZ A 407 36.829 390.298 35.136 1.00155.49 C
ANISOU 2683 C1 DNZ A 407 17667 19074 22337 469 2263 1227 C
HETATM 2684 C2 DNZ A 407 37.942 389.354 35.593 1.00160.11 C
ANISOU 2684 C2 DNZ A 407 18067 19644 23124 476 2264 1190 C
HETATM 2685 C3 DNZ A 407 37.423 388.073 36.260 1.00165.89 C
ANISOU 2685 C3 DNZ A 407 18859 20435 23737 511 2079 1062 C
HETATM 2686 C4 DNZ A 407 36.470 387.350 35.305 1.00166.33 C
ANISOU 2686 C4 DNZ A 407 19140 20569 23490 609 2135 1024 C
HETATM 2687 N5 DNZ A 407 35.381 388.260 34.947 1.00164.13 N
ANISOU 2687 N5 DNZ A 407 19014 20311 23037 593 2108 1050 N
HETATM 2688 C6 DNZ A 407 35.826 389.510 34.281 1.00158.14 C
ANISOU 2688 C6 DNZ A 407 18234 19503 22348 577 2283 1179 C
HETATM 2689 C7 DNZ A 407 34.199 388.150 35.659 1.00156.00 C
ANISOU 2689 C7 DNZ A 407 18069 19313 21891 560 1900 969 C
HETATM 2690 O8 DNZ A 407 34.130 387.303 36.556 1.00153.66 O
ANISOU 2690 O8 DNZ A 407 17730 19023 21631 541 1761 890 O
HETATM 2691 C9 DNZ A 407 33.049 389.076 35.287 1.00145.34 C
ANISOU 2691 C9 DNZ A 407 16860 17982 20381 557 1864 992 C
HETATM 2692 N11 DNZ A 407 30.532 389.173 35.066 1.00130.86 N
ANISOU 2692 N11 DNZ A 407 15270 16228 18224 592 1656 905 N
HETATM 2693 C12 DNZ A 407 31.598 387.041 34.596 1.00134.47 C
ANISOU 2693 C12 DNZ A 407 15705 16706 18683 673 1749 829 C
HETATM 2694 C14 DNZ A 407 33.142 391.581 35.641 1.00141.80 C
ANISOU 2694 C14 DNZ A 407 16349 17425 20102 447 1882 1126 C
HETATM 2695 CL DNZ A 407 33.024 393.860 38.877 1.00116.71 CL
ANISOU 2695 CL DNZ A 407 12990 14064 17291 219 1473 1048 CL
HETATM 2696 O20 DNZ A 407 38.692 388.893 34.478 1.00158.04 O
ANISOU 2696 O20 DNZ A 407 17790 19391 22868 569 2527 1255 O
HETATM 2697 O23 DNZ A 407 38.824 389.966 36.522 1.00158.27 O
ANISOU 2697 O23 DNZ A 407 17610 19321 23204 377 2176 1205 O
HETATM 2698 C1 BOG A 408 31.989 384.827 38.698 1.00133.41 C
ANISOU 2698 C1 BOG A 408 15296 16505 18887 517 1347 666 C
HETATM 2699 O1 BOG A 408 31.524 385.749 39.679 1.00133.64 O
ANISOU 2699 O1 BOG A 408 15312 16525 18942 453 1247 678 O
HETATM 2700 C2 BOG A 408 33.489 384.589 38.789 1.00132.78 C
ANISOU 2700 C2 BOG A 408 15085 16388 18979 534 1412 694 C
HETATM 2701 O2 BOG A 408 34.220 385.816 38.673 1.00132.14 O
ANISOU 2701 O2 BOG A 408 14908 16279 19021 499 1479 766 O
HETATM 2702 C3 BOG A 408 33.931 383.673 37.660 1.00132.92 C
ANISOU 2702 C3 BOG A 408 15135 16416 18952 622 1547 681 C
HETATM 2703 O3 BOG A 408 35.220 383.160 38.013 1.00142.46 O
ANISOU 2703 O3 BOG A 408 16203 17584 20342 645 1577 691 O
HETATM 2704 C4 BOG A 408 32.983 382.504 37.380 1.00119.17 C
ANISOU 2704 C4 BOG A 408 13527 14692 17060 662 1490 599 C
HETATM 2705 O4 BOG A 408 33.052 382.221 35.976 1.00101.81 O
ANISOU 2705 O4 BOG A 408 11425 12513 14745 751 1624 586 O
HETATM 2706 C5 BOG A 408 31.511 382.760 37.703 1.00124.69 C
ANISOU 2706 C5 BOG A 408 14318 15416 17644 612 1370 568 C
HETATM 2707 O5 BOG A 408 31.332 383.576 38.855 1.00128.27 O
ANISOU 2707 O5 BOG A 408 14711 15860 18164 537 1281 600 O
HETATM 2708 C6 BOG A 408 30.780 381.451 37.956 1.00125.46 C
ANISOU 2708 C6 BOG A 408 14478 15494 17696 618 1280 492 C
HETATM 2709 O6 BOG A 408 30.076 381.563 39.196 1.00124.25 O
ANISOU 2709 O6 BOG A 408 14305 15330 17572 548 1166 497 O
HETATM 2710 C1' BOG A 408 30.274 386.291 39.264 1.00134.41 C
ANISOU 2710 C1' BOG A 408 15506 16657 18908 450 1234 674 C
HETATM 2711 C2' BOG A 408 30.047 387.618 39.970 1.00129.23 C
ANISOU 2711 C2' BOG A 408 14830 15978 18291 400 1183 704 C
HETATM 2712 C3' BOG A 408 29.170 388.543 39.139 1.00124.72 C
ANISOU 2712 C3' BOG A 408 14337 15431 17621 415 1218 732 C
HETATM 2713 C4' BOG A 408 29.612 389.981 39.349 1.00120.35 C
ANISOU 2713 C4' BOG A 408 13745 14827 17157 379 1236 789 C
HETATM 2714 C5' BOG A 408 28.517 390.970 38.981 1.00115.76 C
ANISOU 2714 C5' BOG A 408 13247 14255 16483 393 1223 809 C
HETATM 2715 C6' BOG A 408 29.014 392.387 39.229 1.00107.11 C
ANISOU 2715 C6' BOG A 408 12117 13084 15496 354 1239 865 C
HETATM 2716 C7' BOG A 408 27.846 393.346 39.382 1.00103.65 C
ANISOU 2716 C7' BOG A 408 11753 12641 14990 367 1183 863 C
HETATM 2717 C8' BOG A 408 28.174 394.385 40.431 1.00103.01 C
ANISOU 2717 C8' BOG A 408 11636 12475 15028 317 1118 857 C
HETATM 2718 C1 BOG A 409 29.787 416.235 47.560 1.00137.78 C
ANISOU 2718 C1 BOG A 409 16826 13789 21734 -76 -234 300 C
HETATM 2719 O1 BOG A 409 30.131 414.865 47.351 1.00126.45 O
ANISOU 2719 O1 BOG A 409 15257 12599 20189 -104 -164 349 O
HETATM 2720 C2 BOG A 409 29.310 416.488 48.994 1.00137.86 C
ANISOU 2720 C2 BOG A 409 17027 13755 21598 39 -463 45 C
HETATM 2721 O2 BOG A 409 28.032 415.875 49.193 1.00125.38 O
ANISOU 2721 O2 BOG A 409 15576 12412 19649 220 -370 23 O
HETATM 2722 C3 BOG A 409 29.152 417.975 49.302 1.00153.68 C
ANISOU 2722 C3 BOG A 409 19169 15456 23766 55 -572 -37 C
HETATM 2723 O3 BOG A 409 28.998 418.141 50.719 1.00154.09 O
ANISOU 2723 O3 BOG A 409 19396 15448 23704 148 -815 -298 O
HETATM 2724 C4 BOG A 409 30.325 418.812 48.788 1.00162.41 C
ANISOU 2724 C4 BOG A 409 20124 16273 25309 -145 -607 45 C
HETATM 2725 O4 BOG A 409 29.985 420.206 48.845 1.00163.39 O
ANISOU 2725 O4 BOG A 409 20390 16118 25572 -117 -657 11 O
HETATM 2726 C5 BOG A 409 30.643 418.446 47.339 1.00159.63 C
ANISOU 2726 C5 BOG A 409 19591 16010 25052 -238 -331 326 C
HETATM 2727 O5 BOG A 409 30.920 417.046 47.233 1.00150.05 O
ANISOU 2727 O5 BOG A 409 18250 15072 23691 -251 -270 358 O
HETATM 2728 C6 BOG A 409 31.817 419.246 46.782 1.00158.70 C
ANISOU 2728 C6 BOG A 409 19307 15605 25388 -440 -313 439 C
HETATM 2729 O6 BOG A 409 31.989 418.903 45.401 1.00154.36 O
ANISOU 2729 O6 BOG A 409 18633 15152 24865 -489 -15 714 O
HETATM 2730 C1' BOG A 409 30.631 414.669 46.026 1.00116.58 C
ANISOU 2730 C1' BOG A 409 13850 11376 19071 -198 55 577 C
HETATM 2731 C2' BOG A 409 30.607 413.186 45.673 1.00108.54 C
ANISOU 2731 C2' BOG A 409 12743 10649 17848 -173 166 635 C
HETATM 2732 C3' BOG A 409 30.626 412.964 44.165 1.00 97.22 C
ANISOU 2732 C3' BOG A 409 11235 9292 16410 -193 437 875 C
HETATM 2733 C4' BOG A 409 30.281 411.516 43.838 1.00 93.36 C
ANISOU 2733 C4' BOG A 409 10715 9099 15658 -127 533 905 C
HETATM 2734 C5' BOG A 409 30.378 411.279 42.338 1.00 89.83 C
ANISOU 2734 C5' BOG A 409 10220 8721 15190 -134 787 1128 C
HETATM 2735 C6' BOG A 409 30.494 409.792 42.016 1.00 80.19 C
ANISOU 2735 C6' BOG A 409 8920 7745 13802 -114 865 1147 C
HETATM 2736 C7' BOG A 409 30.890 409.652 40.552 1.00 76.77 C
ANISOU 2736 C7' BOG A 409 8441 7336 13392 -132 1114 1361 C
HETATM 2737 C8' BOG A 409 30.851 408.222 40.074 1.00 71.13 C
ANISOU 2737 C8' BOG A 409 7687 6860 12480 -86 1204 1382 C
CONECT 1 2 3 4
CONECT 2 1
CONECT 3 1
CONECT 4 1
CONECT 17 2244
CONECT 118 2593
CONECT 884 1474
CONECT 1474 884
CONECT 2244 17
CONECT 2564 2654
CONECT 2593 118 2594 2604
CONECT 2594 2593 2595 2601
CONECT 2595 2594 2596 2602
CONECT 2596 2595 2597 2603
CONECT 2597 2596 2598 2604
CONECT 2598 2597 2605
CONECT 2599 2600 2601 2606
CONECT 2600 2599
CONECT 2601 2594 2599
CONECT 2602 2595
CONECT 2603 2596 2607
CONECT 2604 2593 2597
CONECT 2605 2598
CONECT 2606 2599
CONECT 2607 2603 2608 2618
CONECT 2608 2607 2609 2615
CONECT 2609 2608 2610 2616
CONECT 2610 2609 2611 2617
CONECT 2611 2610 2612 2618
CONECT 2612 2611 2619
CONECT 2613 2614 2615 2620
CONECT 2614 2613
CONECT 2615 2608 2613
CONECT 2616 2609
CONECT 2617 2610 2621
CONECT 2618 2607 2611
CONECT 2619 2612
CONECT 2620 2613
CONECT 2621 2617 2622 2630
CONECT 2622 2621 2623 2627
CONECT 2623 2622 2624 2628
CONECT 2624 2623 2625 2629
CONECT 2625 2624 2626 2630
CONECT 2626 2625 2631
CONECT 2627 2622
CONECT 2628 2623 2632
CONECT 2629 2624
CONECT 2630 2621 2625
CONECT 2631 2626 2643
CONECT 2632 2628 2633 2641
CONECT 2633 2632 2634 2638
CONECT 2634 2633 2635 2639
CONECT 2635 2634 2636 2640
CONECT 2636 2635 2637 2641
CONECT 2637 2636 2642
CONECT 2638 2633
CONECT 2639 2634
CONECT 2640 2635
CONECT 2641 2632 2636
CONECT 2642 2637
CONECT 2643 2631 2644 2652
CONECT 2644 2643 2645 2649
CONECT 2645 2644 2646 2650
CONECT 2646 2645 2647 2651
CONECT 2647 2646 2648 2652
CONECT 2648 2647 2653
CONECT 2649 2644
CONECT 2650 2645
CONECT 2651 2646
CONECT 2652 2643 2647
CONECT 2653 2648
CONECT 2654 2564 2655 2656
CONECT 2655 2654
CONECT 2656 2654 2657
CONECT 2657 2656 2658
CONECT 2658 2657 2659
CONECT 2659 2658 2660
CONECT 2660 2659 2661
CONECT 2661 2660 2662
CONECT 2662 2661 2663
CONECT 2663 2662 2664
CONECT 2664 2663 2665
CONECT 2665 2664 2666
CONECT 2666 2665 2667
CONECT 2667 2666 2668
CONECT 2668 2667 2669
CONECT 2669 2668 2670
CONECT 2670 2669
CONECT 2671 2691 2692 2693
CONECT 2672 2676 2691 2694
CONECT 2673 2674 2694
CONECT 2674 2673 2675 2695
CONECT 2675 2674 2676
CONECT 2676 2672 2675
CONECT 2677 2678 2682 2696
CONECT 2678 2677 2679 2697
CONECT 2679 2678 2680
CONECT 2680 2679 2681
CONECT 2681 2680 2682
CONECT 2682 2677 2681
CONECT 2683 2684 2688
CONECT 2684 2683 2685 2696 2697
CONECT 2685 2684 2686
CONECT 2686 2685 2687
CONECT 2687 2686 2688 2689
CONECT 2688 2683 2687
CONECT 2689 2687 2690 2691
CONECT 2690 2689
CONECT 2691 2671 2672 2689
CONECT 2692 2671
CONECT 2693 2671
CONECT 2694 2672 2673
CONECT 2695 2674
CONECT 2696 2677 2684
CONECT 2697 2678 2684
CONECT 2698 2699 2700 2707
CONECT 2699 2698 2710
CONECT 2700 2698 2701 2702
CONECT 2701 2700
CONECT 2702 2700 2703 2704
CONECT 2703 2702
CONECT 2704 2702 2705 2706
CONECT 2705 2704
CONECT 2706 2704 2707 2708
CONECT 2707 2698 2706
CONECT 2708 2706 2709
CONECT 2709 2708
CONECT 2710 2699 2711
CONECT 2711 2710 2712
CONECT 2712 2711 2713
CONECT 2713 2712 2714
CONECT 2714 2713 2715
CONECT 2715 2714 2716
CONECT 2716 2715 2717
CONECT 2717 2716
CONECT 2718 2719 2720 2727
CONECT 2719 2718 2730
CONECT 2720 2718 2721 2722
CONECT 2721 2720
CONECT 2722 2720 2723 2724
CONECT 2723 2722
CONECT 2724 2722 2725 2726
CONECT 2725 2724
CONECT 2726 2724 2727 2728
CONECT 2727 2718 2726
CONECT 2728 2726 2729
CONECT 2729 2728
CONECT 2730 2719 2731
CONECT 2731 2730 2732
CONECT 2732 2731 2733
CONECT 2733 2732 2734
CONECT 2734 2733 2735
CONECT 2735 2734 2736
CONECT 2736 2735 2737
CONECT 2737 2736
MASTER 378 0 10 13 4 0 0 6 2736 1 155 27
END