HEADER MEMBRANE PROTEIN 23-JAN-18 6FKD
TITLE CRYSTAL STRUCTURE OF N2C/D282C STABILIZED OPSIN BOUND TO RS16
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 6FKD 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 11-APR-18 6FKD 1 JRNL
REVDAT 1 04-APR-18 6FKD 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. 2.49 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) : 2.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.76
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 44048
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) : 0.228
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 2206
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 46.0120 - 6.2695 0.99 2712 141 0.2244 0.2545
REMARK 3 2 6.2695 - 4.9782 1.00 2638 147 0.2186 0.2411
REMARK 3 3 4.9782 - 4.3495 1.00 2637 150 0.1900 0.1893
REMARK 3 4 4.3495 - 3.9520 1.00 2628 148 0.1904 0.2005
REMARK 3 5 3.9520 - 3.6689 1.00 2626 141 0.1939 0.2218
REMARK 3 6 3.6689 - 3.4527 1.00 2632 122 0.2092 0.2515
REMARK 3 7 3.4527 - 3.2798 1.00 2630 142 0.2340 0.2447
REMARK 3 8 3.2798 - 3.1371 1.00 2605 146 0.2396 0.2421
REMARK 3 9 3.1371 - 3.0163 1.00 2602 124 0.2602 0.2962
REMARK 3 10 3.0163 - 2.9123 0.99 2612 127 0.2754 0.3579
REMARK 3 11 2.9123 - 2.8212 1.00 2604 143 0.2843 0.3261
REMARK 3 12 2.8212 - 2.7406 0.99 2557 151 0.2976 0.3684
REMARK 3 13 2.7406 - 2.6684 0.99 2643 121 0.3221 0.3699
REMARK 3 14 2.6684 - 2.6033 0.99 2567 127 0.3331 0.3971
REMARK 3 15 2.6033 - 2.5442 0.99 2608 134 0.3517 0.4179
REMARK 3 16 2.5442 - 2.4900 0.98 2541 142 0.3687 0.3917
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 2901
REMARK 3 ANGLE : 0.802 3949
REMARK 3 CHIRALITY : 0.044 457
REMARK 3 PLANARITY : 0.005 461
REMARK 3 DIHEDRAL : 13.885 1700
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):-230.8356 39.8301 39.7455
REMARK 3 T TENSOR
REMARK 3 T11: 0.4392 T22: 0.3707
REMARK 3 T33: 0.5885 T12: 0.0189
REMARK 3 T13: -0.0750 T23: 0.0453
REMARK 3 L TENSOR
REMARK 3 L11: 1.9036 L22: 3.1673
REMARK 3 L33: 1.0537 L12: 1.3009
REMARK 3 L13: -0.0125 L23: 0.0353
REMARK 3 S TENSOR
REMARK 3 S11: -0.0815 S12: 0.1493 S13: 0.1586
REMARK 3 S21: -0.2698 S22: 0.0620 S23: 0.2377
REMARK 3 S31: 0.0148 S32: -0.0999 S33: 0.0224
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 6FKD 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_1200008395.
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 : 44126
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.490
REMARK 200 RESOLUTION RANGE LOW (A) : 45.760
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) : 0.15270
REMARK 200 R SYM (I) : 0.15270
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.60
REMARK 200 R MERGE FOR SHELL (I) : 3.03700
REMARK 200 R SYM FOR SHELL (I) : 3.03700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.780
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 (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
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 121.71550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.27248
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 37.26067
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 121.71550
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 70.27248
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 37.26067
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 121.71550
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 70.27248
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 37.26067
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 121.71550
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 70.27248
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.26067
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 121.71550
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 70.27248
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 37.26067
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 121.71550
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 70.27248
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.26067
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 140.54495
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 74.52133
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 140.54495
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 74.52133
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 140.54495
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 74.52133
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 140.54495
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 74.52133
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 140.54495
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 74.52133
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 140.54495
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 74.52133
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: 3550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 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 IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 186 O4 BOG A 408 1.27
REMARK 500 O LEU A 128 O HOH A 501 1.96
REMARK 500 OE1 GLN A 184 O HOH A 502 2.12
REMARK 500 OE1 GLU A 239 O HOH A 503 2.19
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 50.65 -99.50
REMARK 500 SER A 176 -161.98 63.85
REMARK 500 PRO A 194 47.51 -83.50
REMARK 500 HIS A 195 105.21 -56.10
REMARK 500 PHE A 212 -54.93 -144.36
REMARK 500 PRO A 285 7.96 -65.63
REMARK 500 PHE A 287 -70.84 -74.01
REMARK 500 CYS A 322 32.07 -91.16
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6FKD A 1 348 UNP P02699 OPSD_BOVIN 1 348
SEQADV 6FKD ACE A 0 UNP P02699 ACETYLATION
SEQADV 6FKD CYS A 2 UNP P02699 ASN 2 CONFLICT
SEQADV 6FKD 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 BOG A 407 20
HET BOG A 408 20
HET BOG A 409 20
HET BOG A 410 20
HET BOG A 411 20
HET DL2 A 412 25
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 BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETNAM DL2 5-CHLORANYL-2-(2-OXIDANYLIDENE-2-SPIRO[1,3-
HETNAM 2 DL2 BENZODIOXOLE-2,4'-PIPERIDINE]-1'-YL-ETHYL)-3~{H}-
HETNAM 3 DL2 PYRIDIN-6-ONE
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 BOG 5(C14 H28 O6)
FORMUL 9 DL2 C18 H17 CL N2 O4
FORMUL 10 HOH *25(H2 O)
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 LEU A 72 5 3
HELIX 4 AA4 ASN A 73 GLY A 90 1 18
HELIX 5 AA5 GLY A 90 LEU A 99 1 10
HELIX 6 AA6 PHE A 105 LYS A 141 1 37
HELIX 7 AA7 GLY A 149 ALA A 169 1 21
HELIX 8 AA8 PRO A 170 VAL A 173 5 4
HELIX 9 AA9 HIS A 195 THR A 198 5 4
HELIX 10 AB1 ASN A 199 HIS A 211 1 13
HELIX 11 AB2 PHE A 212 GLN A 236 1 25
HELIX 12 AB3 SER A 240 THR A 277 1 38
HELIX 13 AB4 MET A 288 LYS A 296 1 9
HELIX 14 AB5 THR A 297 ILE A 307 1 11
HELIX 15 AB6 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 2.03
SSBOND 2 CYS A 110 CYS A 187 1555 1555 2.05
LINK C ACE A 0 N MET A 1 1555 1555 1.34
LINK ND2 ASN A 15 C1 NAG B 1 1555 1555 1.44
LINK SG CYS A 322 C1 PLM A 401 1555 1555 1.72
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.43
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.43
LINK O3 BMA B 3 C1 MAN B 4 1555 1555 1.44
LINK O6 BMA B 3 C1 MAN B 5 1555 1555 1.44
CRYST1 243.431 243.431 111.782 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 0.004108 0.002372 0.000000 0.00000
SCALE2 0.000000 0.004743 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008946 0.00000
HETATM 1 C ACE A 0 -231.901 71.319 40.065 1.00102.13 C
ANISOU 1 C ACE A 0 12036 8519 18252 817 -1234 1179 C
HETATM 2 O ACE A 0 -232.988 71.452 39.496 1.00121.78 O
ANISOU 2 O ACE A 0 14409 10979 20885 884 -1368 1284 O
HETATM 3 CH3 ACE A 0 -231.836 71.354 41.570 1.00 89.35 C
ANISOU 3 CH3 ACE A 0 10364 6859 16727 844 -980 873 C
ATOM 4 N MET A 1 -230.785 71.173 39.334 1.00 85.19 N
ANISOU 4 N MET A 1 10066 6436 15868 705 -1314 1335 N
ATOM 5 CA MET A 1 -229.381 70.987 39.725 1.00 89.75 C
ANISOU 5 CA MET A 1 10786 7101 16216 590 -1192 1256 C
ATOM 6 C MET A 1 -229.180 69.937 40.812 1.00 87.75 C
ANISOU 6 C MET A 1 10510 7070 15762 579 -1009 1014 C
ATOM 7 O MET A 1 -228.579 70.205 41.849 1.00102.82 O
ANISOU 7 O MET A 1 12442 8975 17649 537 -842 815 O
ATOM 8 CB MET A 1 -228.766 72.314 40.172 1.00 89.87 C
ANISOU 8 CB MET A 1 10840 6900 16407 554 -1113 1192 C
ATOM 9 CG MET A 1 -228.648 73.334 39.057 1.00 89.79 C
ANISOU 9 CG MET A 1 10896 6786 16435 511 -1269 1423 C
ATOM 10 SD MET A 1 -228.071 72.610 37.508 1.00 94.17 S
ANISOU 10 SD MET A 1 11611 7491 16678 397 -1458 1728 S
ATOM 11 CE MET A 1 -226.479 71.922 37.983 1.00 83.48 C
ANISOU 11 CE MET A 1 10376 6361 14983 256 -1280 1596 C
ATOM 12 N CYS A 2 -229.692 68.736 40.560 1.00 74.16 N
ANISOU 12 N CYS A 2 8753 5536 13889 606 -1052 1041 N
ATOM 13 CA CYS A 2 -229.675 67.694 41.578 1.00 79.55 C
ANISOU 13 CA CYS A 2 9406 6412 14408 605 -896 831 C
ATOM 14 C CYS A 2 -228.294 67.067 41.722 1.00 82.68 C
ANISOU 14 C CYS A 2 9935 7021 14459 481 -828 794 C
ATOM 15 O CYS A 2 -227.864 66.757 42.840 1.00 93.52 O
ANISOU 15 O CYS A 2 11316 8479 15737 446 -679 596 O
ATOM 16 CB CYS A 2 -230.725 66.634 41.241 1.00 82.83 C
ANISOU 16 CB CYS A 2 9731 6937 14802 674 -970 877 C
ATOM 17 SG CYS A 2 -232.436 67.251 41.215 1.00 94.62 S
ANISOU 17 SG CYS A 2 11017 8186 16748 830 -1042 897 S
ATOM 18 N GLY A 3 -227.583 66.884 40.613 1.00 67.33 N
ANISOU 18 N GLY A 3 8093 5157 12332 405 -935 980 N
ATOM 19 CA GLY A 3 -226.289 66.236 40.661 1.00 73.98 C
ANISOU 19 CA GLY A 3 9033 6195 12883 295 -868 952 C
ATOM 20 C GLY A 3 -225.206 66.973 39.905 1.00 71.57 C
ANISOU 20 C GLY A 3 8835 5838 12521 190 -904 1083 C
ATOM 21 O GLY A 3 -225.345 68.164 39.603 1.00 69.75 O
ANISOU 21 O GLY A 3 8615 5398 12489 194 -958 1166 O
ATOM 22 N THR A 4 -224.114 66.271 39.608 1.00 67.07 N
ANISOU 22 N THR A 4 8338 5449 11697 93 -865 1102 N
ATOM 23 CA THR A 4 -223.025 66.786 38.789 1.00 55.58 C
ANISOU 23 CA THR A 4 6983 3978 10156 -24 -877 1229 C
ATOM 24 C THR A 4 -222.851 65.851 37.599 1.00 61.10 C
ANISOU 24 C THR A 4 7756 4836 10624 -76 -930 1373 C
ATOM 25 O THR A 4 -222.579 64.662 37.781 1.00 64.26 O
ANISOU 25 O THR A 4 8141 5426 10848 -80 -872 1297 O
ATOM 26 CB THR A 4 -221.730 66.892 39.598 1.00 66.76 C
ANISOU 26 CB THR A 4 8406 5451 11509 -111 -753 1094 C
ATOM 27 OG1 THR A 4 -221.973 67.648 40.788 1.00 56.81 O
ANISOU 27 OG1 THR A 4 7094 4058 10436 -73 -698 934 O
ATOM 28 CG2 THR A 4 -220.638 67.578 38.794 1.00 67.47 C
ANISOU 28 CG2 THR A 4 8582 5497 11558 -237 -750 1219 C
ATOM 29 N GLU A 5 -223.045 66.380 36.393 1.00 66.99 N
ANISOU 29 N GLU A 5 8588 5495 11369 -120 -1042 1578 N
ATOM 30 CA GLU A 5 -222.822 65.641 35.159 1.00 57.13 C
ANISOU 30 CA GLU A 5 7445 4380 9880 -202 -1085 1719 C
ATOM 31 C GLU A 5 -221.356 65.684 34.750 1.00 80.48 C
ANISOU 31 C GLU A 5 10490 7413 12677 -347 -970 1737 C
ATOM 32 O GLU A 5 -220.625 66.636 35.047 1.00 75.20 O
ANISOU 32 O GLU A 5 9826 6638 12109 -402 -916 1724 O
ATOM 33 CB GLU A 5 -223.634 66.221 34.008 1.00 55.98 C
ANISOU 33 CB GLU A 5 7382 4109 9781 -216 -1269 1948 C
ATOM 34 CG GLU A 5 -225.116 66.296 34.221 1.00 66.48 C
ANISOU 34 CG GLU A 5 8610 5335 11313 -78 -1408 1966 C
ATOM 35 CD GLU A 5 -225.785 67.017 33.089 1.00 77.39 C
ANISOU 35 CD GLU A 5 10070 6566 12767 -104 -1618 2216 C
ATOM 36 OE1 GLU A 5 -225.607 68.254 32.970 1.00 80.37 O
ANISOU 36 OE1 GLU A 5 10479 6746 13313 -127 -1661 2310 O
ATOM 37 OE2 GLU A 5 -226.462 66.339 32.295 1.00 89.89 O
ANISOU 37 OE2 GLU A 5 11694 8226 14233 -113 -1750 2327 O
ATOM 38 N GLY A 6 -220.950 64.658 34.016 1.00 78.19 N
ANISOU 38 N GLY A 6 10265 7296 12147 -415 -927 1766 N
ATOM 39 CA GLY A 6 -219.670 64.632 33.359 1.00 76.29 C
ANISOU 39 CA GLY A 6 10111 7125 11750 -562 -813 1805 C
ATOM 40 C GLY A 6 -219.712 63.640 32.221 1.00 70.51 C
ANISOU 40 C GLY A 6 9488 6536 10767 -633 -811 1883 C
ATOM 41 O GLY A 6 -220.718 62.955 32.000 1.00 71.28 O
ANISOU 41 O GLY A 6 9589 6681 10813 -566 -911 1903 O
ATOM 42 N PRO A 7 -218.622 63.542 31.463 1.00 66.83 N
ANISOU 42 N PRO A 7 9113 6136 10143 -779 -686 1920 N
ATOM 43 CA PRO A 7 -218.536 62.490 30.443 1.00 75.12 C
ANISOU 43 CA PRO A 7 10271 7333 10938 -859 -638 1952 C
ATOM 44 C PRO A 7 -218.485 61.126 31.114 1.00 77.24 C
ANISOU 44 C PRO A 7 10423 7754 11170 -768 -556 1772 C
ATOM 45 O PRO A 7 -217.597 60.856 31.928 1.00 77.75 O
ANISOU 45 O PRO A 7 10370 7868 11305 -747 -428 1633 O
ATOM 46 CB PRO A 7 -217.230 62.816 29.708 1.00 73.08 C
ANISOU 46 CB PRO A 7 10105 7093 10569 -1036 -474 1994 C
ATOM 47 CG PRO A 7 -216.949 64.275 30.051 1.00 63.80 C
ANISOU 47 CG PRO A 7 8916 5743 9582 -1060 -510 2062 C
ATOM 48 CD PRO A 7 -217.420 64.388 31.469 1.00 60.59 C
ANISOU 48 CD PRO A 7 8334 5286 9402 -889 -570 1929 C
ATOM 49 N ASN A 8 -219.472 60.283 30.800 1.00 69.88 N
ANISOU 49 N ASN A 8 9522 6887 10143 -717 -650 1785 N
ATOM 50 CA ASN A 8 -219.557 58.897 31.264 1.00 68.77 C
ANISOU 50 CA ASN A 8 9298 6884 9946 -642 -588 1638 C
ATOM 51 C ASN A 8 -219.951 58.762 32.729 1.00 62.42 C
ANISOU 51 C ASN A 8 8321 6064 9330 -489 -616 1507 C
ATOM 52 O ASN A 8 -219.689 57.714 33.331 1.00 62.66 O
ANISOU 52 O ASN A 8 8268 6200 9339 -438 -538 1375 O
ATOM 53 CB ASN A 8 -218.243 58.131 31.052 1.00 57.25 C
ANISOU 53 CB ASN A 8 7834 5539 8378 -722 -377 1540 C
ATOM 54 CG ASN A 8 -217.805 58.106 29.618 1.00 73.83 C
ANISOU 54 CG ASN A 8 10115 7672 10265 -891 -301 1636 C
ATOM 55 OD1 ASN A 8 -218.622 58.006 28.701 1.00 93.42 O
ANISOU 55 OD1 ASN A 8 12743 10156 12597 -942 -411 1747 O
ATOM 56 ND2 ASN A 8 -216.497 58.186 29.409 1.00 78.98 N
ANISOU 56 ND2 ASN A 8 10760 8350 10899 -990 -108 1592 N
ATOM 57 N PHE A 9 -220.546 59.779 33.351 1.00 56.59 N
ANISOU 57 N PHE A 9 7530 5193 8777 -420 -716 1533 N
ATOM 58 CA PHE A 9 -221.031 59.571 34.710 1.00 69.03 C
ANISOU 58 CA PHE A 9 8965 6763 10501 -291 -727 1397 C
ATOM 59 C PHE A 9 -222.077 60.613 35.075 1.00 66.29 C
ANISOU 59 C PHE A 9 8582 6254 10350 -215 -852 1445 C
ATOM 60 O PHE A 9 -222.250 61.627 34.398 1.00 61.05 O
ANISOU 60 O PHE A 9 7988 5464 9742 -258 -933 1584 O
ATOM 61 CB PHE A 9 -219.895 59.584 35.743 1.00 57.80 C
ANISOU 61 CB PHE A 9 7453 5370 9137 -298 -602 1261 C
ATOM 62 CG PHE A 9 -219.134 60.887 35.817 1.00 64.00 C
ANISOU 62 CG PHE A 9 8252 6038 10028 -366 -574 1297 C
ATOM 63 CD1 PHE A 9 -217.901 61.022 35.182 1.00 51.22 C
ANISOU 63 CD1 PHE A 9 6678 4449 8333 -488 -471 1334 C
ATOM 64 CD2 PHE A 9 -219.631 61.966 36.548 1.00 57.10 C
ANISOU 64 CD2 PHE A 9 7339 5016 9341 -314 -635 1281 C
ATOM 65 CE1 PHE A 9 -217.185 62.218 35.260 1.00 72.91 C
ANISOU 65 CE1 PHE A 9 9433 7084 11183 -561 -443 1367 C
ATOM 66 CE2 PHE A 9 -218.922 63.165 36.626 1.00 57.26 C
ANISOU 66 CE2 PHE A 9 7376 4916 9465 -384 -609 1308 C
ATOM 67 CZ PHE A 9 -217.698 63.289 35.979 1.00 59.82 C
ANISOU 67 CZ PHE A 9 7747 5277 9706 -510 -520 1357 C
ATOM 68 N TYR A 10 -222.768 60.328 36.175 1.00 70.03 N
ANISOU 68 N TYR A 10 8943 6726 10937 -104 -858 1323 N
ATOM 69 CA TYR A 10 -223.673 61.257 36.834 1.00 60.84 C
ANISOU 69 CA TYR A 10 7709 5405 10002 -18 -923 1307 C
ATOM 70 C TYR A 10 -223.530 61.012 38.331 1.00 61.44 C
ANISOU 70 C TYR A 10 7686 5512 10145 37 -823 1111 C
ATOM 71 O TYR A 10 -223.917 59.948 38.824 1.00 69.23 O
ANISOU 71 O TYR A 10 8625 6610 11068 84 -799 1023 O
ATOM 72 CB TYR A 10 -225.122 61.055 36.370 1.00 57.57 C
ANISOU 72 CB TYR A 10 7271 4952 9651 55 -1063 1388 C
ATOM 73 CG TYR A 10 -226.126 61.865 37.164 1.00 63.88 C
ANISOU 73 CG TYR A 10 7959 5589 10724 162 -1102 1339 C
ATOM 74 CD1 TYR A 10 -226.297 63.225 36.931 1.00 73.36 C
ANISOU 74 CD1 TYR A 10 9166 6589 12117 167 -1171 1432 C
ATOM 75 CD2 TYR A 10 -226.883 61.276 38.163 1.00 63.47 C
ANISOU 75 CD2 TYR A 10 7795 5573 10747 252 -1055 1194 C
ATOM 76 CE1 TYR A 10 -227.209 63.970 37.668 1.00 71.38 C
ANISOU 76 CE1 TYR A 10 8802 6171 12148 270 -1185 1369 C
ATOM 77 CE2 TYR A 10 -227.797 62.010 38.898 1.00 64.16 C
ANISOU 77 CE2 TYR A 10 7775 5506 11096 343 -1057 1127 C
ATOM 78 CZ TYR A 10 -227.956 63.352 38.649 1.00 69.93 C
ANISOU 78 CZ TYR A 10 8502 6032 12035 357 -1118 1209 C
ATOM 79 OH TYR A 10 -228.860 64.072 39.395 1.00 83.31 O
ANISOU 79 OH TYR A 10 10078 7558 14018 454 -1098 1124 O
ATOM 80 N VAL A 11 -222.960 61.970 39.052 1.00 64.35 N
ANISOU 80 N VAL A 11 8038 5783 10629 16 -769 1045 N
ATOM 81 CA VAL A 11 -222.837 61.889 40.504 1.00 56.48 C
ANISOU 81 CA VAL A 11 6973 4800 9686 44 -685 861 C
ATOM 82 C VAL A 11 -224.096 62.501 41.115 1.00 72.14 C
ANISOU 82 C VAL A 11 8892 6643 11873 138 -705 802 C
ATOM 83 O VAL A 11 -224.436 63.647 40.779 1.00 63.97 O
ANISOU 83 O VAL A 11 7862 5432 11013 153 -754 871 O
ATOM 84 CB VAL A 11 -221.575 62.603 41.002 1.00 54.89 C
ANISOU 84 CB VAL A 11 6790 4564 9501 -42 -620 806 C
ATOM 85 CG1 VAL A 11 -221.455 62.521 42.529 1.00 55.00 C
ANISOU 85 CG1 VAL A 11 6758 4596 9542 -35 -552 617 C
ATOM 86 CG2 VAL A 11 -220.353 62.000 40.342 1.00 52.18 C
ANISOU 86 CG2 VAL A 11 6483 4349 8995 -130 -587 864 C
ATOM 87 N PRO A 12 -224.818 61.787 41.957 1.00 77.20 N
ANISOU 87 N PRO A 12 9472 7345 12516 199 -665 682 N
ATOM 88 CA PRO A 12 -226.054 62.349 42.537 1.00 60.29 C
ANISOU 88 CA PRO A 12 7252 5064 10592 286 -655 609 C
ATOM 89 C PRO A 12 -225.775 63.282 43.712 1.00 62.27 C
ANISOU 89 C PRO A 12 7497 5201 10962 265 -552 450 C
ATOM 90 O PRO A 12 -226.253 63.083 44.832 1.00 75.17 O
ANISOU 90 O PRO A 12 9093 6842 12626 287 -457 284 O
ATOM 91 CB PRO A 12 -226.828 61.085 42.945 1.00 57.65 C
ANISOU 91 CB PRO A 12 6865 4862 10178 335 -631 540 C
ATOM 92 CG PRO A 12 -225.747 60.073 43.252 1.00 61.27 C
ANISOU 92 CG PRO A 12 7379 5505 10396 263 -586 498 C
ATOM 93 CD PRO A 12 -224.660 60.346 42.246 1.00 57.04 C
ANISOU 93 CD PRO A 12 6913 4983 9775 193 -633 628 C
ATOM 94 N PHE A 13 -224.998 64.333 43.455 1.00 64.79 N
ANISOU 94 N PHE A 13 7865 5409 11342 209 -564 495 N
ATOM 95 CA PHE A 13 -224.676 65.324 44.474 1.00 59.40 C
ANISOU 95 CA PHE A 13 7192 4600 10776 174 -475 347 C
ATOM 96 C PHE A 13 -224.400 66.657 43.788 1.00 63.03 C
ANISOU 96 C PHE A 13 7680 4864 11403 154 -527 456 C
ATOM 97 O PHE A 13 -223.822 66.686 42.700 1.00 73.59 O
ANISOU 97 O PHE A 13 9067 6228 12664 109 -608 629 O
ATOM 98 CB PHE A 13 -223.471 64.869 45.305 1.00 59.20 C
ANISOU 98 CB PHE A 13 7220 4717 10557 68 -414 239 C
ATOM 99 CG PHE A 13 -223.253 65.663 46.568 1.00 61.59 C
ANISOU 99 CG PHE A 13 7546 4922 10934 15 -320 51 C
ATOM 100 CD1 PHE A 13 -223.950 65.355 47.726 1.00 56.97 C
ANISOU 100 CD1 PHE A 13 6947 4353 10346 33 -224 -129 C
ATOM 101 CD2 PHE A 13 -222.330 66.698 46.602 1.00 64.15 C
ANISOU 101 CD2 PHE A 13 7916 5140 11317 -70 -319 47 C
ATOM 102 CE1 PHE A 13 -223.743 66.072 48.887 1.00 60.01 C
ANISOU 102 CE1 PHE A 13 7379 4652 10770 -37 -128 -315 C
ATOM 103 CE2 PHE A 13 -222.111 67.422 47.764 1.00 52.76 C
ANISOU 103 CE2 PHE A 13 6511 3607 9930 -135 -236 -138 C
ATOM 104 CZ PHE A 13 -222.813 67.115 48.903 1.00 61.21 C
ANISOU 104 CZ PHE A 13 7581 4696 10980 -122 -140 -322 C
ATOM 105 N SER A 14 -224.823 67.755 44.418 1.00 58.59 N
ANISOU 105 N SER A 14 7092 4098 11071 181 -472 351 N
ATOM 106 CA SER A 14 -224.641 69.078 43.834 1.00 55.59 C
ANISOU 106 CA SER A 14 6737 3500 10885 167 -523 452 C
ATOM 107 C SER A 14 -223.199 69.540 43.997 1.00 65.03 C
ANISOU 107 C SER A 14 8017 4712 11978 32 -493 434 C
ATOM 108 O SER A 14 -222.598 69.383 45.062 1.00 68.05 O
ANISOU 108 O SER A 14 8422 5168 12268 -36 -403 261 O
ATOM 109 CB SER A 14 -225.582 70.092 44.484 1.00 57.51 C
ANISOU 109 CB SER A 14 6915 3497 11441 247 -460 330 C
ATOM 110 OG SER A 14 -225.176 71.438 44.216 1.00 59.28 O
ANISOU 110 OG SER A 14 7177 3497 11849 210 -482 382 O
ATOM 111 N ASN A 15 -222.647 70.132 42.938 1.00 62.17 N
ANISOU 111 N ASN A 15 7707 4279 11635 -20 -573 619 N
ATOM 112 CA ASN A 15 -221.284 70.644 42.975 1.00 59.62 C
ANISOU 112 CA ASN A 15 7450 3956 11246 -155 -545 620 C
ATOM 113 C ASN A 15 -221.220 72.137 43.285 1.00 58.57 C
ANISOU 113 C ASN A 15 7338 3559 11358 -182 -522 576 C
ATOM 114 O ASN A 15 -220.208 72.779 42.983 1.00 66.21 O
ANISOU 114 O ASN A 15 8362 4476 12319 -294 -526 636 O
ATOM 115 CB ASN A 15 -220.576 70.359 41.650 1.00 57.94 C
ANISOU 115 CB ASN A 15 7293 3834 10885 -225 -615 837 C
ATOM 116 CG ASN A 15 -219.069 70.394 41.778 1.00 68.24 C
ANISOU 116 CG ASN A 15 8633 5227 12069 -368 -561 812 C
ATOM 117 OD1 ASN A 15 -218.529 70.309 42.884 1.00 59.75 O
ANISOU 117 OD1 ASN A 15 7535 4200 10966 -412 -496 637 O
ATOM 118 ND2 ASN A 15 -218.377 70.513 40.650 1.00 62.17 N
ANISOU 118 ND2 ASN A 15 7920 4477 11225 -452 -589 988 N
ATOM 119 N LYS A 16 -222.269 72.711 43.888 1.00 59.76 N
ANISOU 119 N LYS A 16 7439 3530 11739 -86 -486 464 N
ATOM 120 CA LYS A 16 -222.225 74.147 44.177 1.00 75.12 C
ANISOU 120 CA LYS A 16 9402 5198 13940 -108 -455 411 C
ATOM 121 C LYS A 16 -221.112 74.508 45.157 1.00 62.06 C
ANISOU 121 C LYS A 16 7805 3563 12211 -246 -361 232 C
ATOM 122 O LYS A 16 -220.662 75.659 45.170 1.00 87.61 O
ANISOU 122 O LYS A 16 11083 6601 15602 -313 -352 228 O
ATOM 123 CB LYS A 16 -223.574 74.634 44.707 1.00 73.37 C
ANISOU 123 CB LYS A 16 9099 4775 14004 27 -406 295 C
ATOM 124 CG LYS A 16 -224.054 73.935 45.964 1.00 83.03 C
ANISOU 124 CG LYS A 16 10282 6112 15156 57 -271 43 C
ATOM 125 CD LYS A 16 -225.497 74.302 46.272 1.00 74.23 C
ANISOU 125 CD LYS A 16 9059 4805 14341 203 -215 -45 C
ATOM 126 CE LYS A 16 -226.011 73.529 47.472 1.00 98.25 C
ANISOU 126 CE LYS A 16 12070 7974 17286 218 -64 -289 C
ATOM 127 NZ LYS A 16 -227.442 73.828 47.753 1.00118.10 N
ANISOU 127 NZ LYS A 16 14457 10307 20109 359 16 -385 N
ATOM 128 N THR A 17 -220.642 73.547 45.952 1.00 68.30 N
ANISOU 128 N THR A 17 8601 4582 12769 -299 -308 97 N
ATOM 129 CA THR A 17 -219.511 73.741 46.853 1.00 65.76 C
ANISOU 129 CA THR A 17 8332 4311 12342 -446 -256 -51 C
ATOM 130 C THR A 17 -218.180 73.306 46.246 1.00 68.85 C
ANISOU 130 C THR A 17 8741 4868 12550 -559 -318 82 C
ATOM 131 O THR A 17 -217.147 73.409 46.915 1.00 81.89 O
ANISOU 131 O THR A 17 10418 6574 14122 -689 -301 -17 O
ATOM 132 CB THR A 17 -219.742 72.993 48.178 1.00 78.18 C
ANISOU 132 CB THR A 17 9908 6021 13775 -456 -175 -277 C
ATOM 133 OG1 THR A 17 -220.084 71.619 47.920 1.00 86.63 O
ANISOU 133 OG1 THR A 17 10936 7316 14664 -387 -208 -209 O
ATOM 134 CG2 THR A 17 -220.861 73.650 48.972 1.00 61.38 C
ANISOU 134 CG2 THR A 17 7774 3698 11848 -387 -65 -463 C
ATOM 135 N GLY A 18 -218.174 72.831 45.003 1.00 62.52 N
ANISOU 135 N GLY A 18 7925 4145 11685 -522 -386 298 N
ATOM 136 CA GLY A 18 -216.933 72.464 44.345 1.00 70.16 C
ANISOU 136 CA GLY A 18 8902 5252 12504 -630 -413 418 C
ATOM 137 C GLY A 18 -216.275 71.178 44.807 1.00 67.83 C
ANISOU 137 C GLY A 18 8569 5218 11986 -665 -403 354 C
ATOM 138 O GLY A 18 -215.152 70.894 44.376 1.00 62.17 O
ANISOU 138 O GLY A 18 7837 4606 11179 -760 -409 427 O
ATOM 139 N VAL A 19 -216.932 70.372 45.653 1.00 62.44 N
ANISOU 139 N VAL A 19 7863 4636 11224 -594 -385 225 N
ATOM 140 CA VAL A 19 -216.273 69.185 46.214 1.00 71.96 C
ANISOU 140 CA VAL A 19 9038 6071 12234 -635 -391 164 C
ATOM 141 C VAL A 19 -216.497 67.905 45.416 1.00 64.12 C
ANISOU 141 C VAL A 19 8008 5253 11102 -560 -415 283 C
ATOM 142 O VAL A 19 -215.842 66.892 45.704 1.00 77.21 O
ANISOU 142 O VAL A 19 9629 7088 12618 -591 -425 261 O
ATOM 143 CB VAL A 19 -216.717 68.916 47.666 1.00 62.26 C
ANISOU 143 CB VAL A 19 7827 4874 10957 -633 -359 -43 C
ATOM 144 CG1 VAL A 19 -216.535 70.174 48.511 1.00 55.70 C
ANISOU 144 CG1 VAL A 19 7049 3863 10251 -720 -322 -189 C
ATOM 145 CG2 VAL A 19 -218.161 68.423 47.707 1.00 53.31 C
ANISOU 145 CG2 VAL A 19 6681 3741 9834 -493 -328 -67 C
ATOM 146 N VAL A 20 -217.391 67.908 44.427 1.00 73.36 N
ANISOU 146 N VAL A 20 9186 6372 12313 -466 -433 409 N
ATOM 147 CA VAL A 20 -217.670 66.690 43.673 1.00 69.98 C
ANISOU 147 CA VAL A 20 8738 6105 11745 -405 -456 508 C
ATOM 148 C VAL A 20 -216.466 66.331 42.809 1.00 68.04 C
ANISOU 148 C VAL A 20 8489 5962 11401 -493 -449 619 C
ATOM 149 O VAL A 20 -215.816 67.204 42.220 1.00 63.63 O
ANISOU 149 O VAL A 20 7959 5309 10909 -576 -440 701 O
ATOM 150 CB VAL A 20 -218.941 66.863 42.823 1.00 67.25 C
ANISOU 150 CB VAL A 20 8408 5670 11475 -301 -500 619 C
ATOM 151 CG1 VAL A 20 -219.201 65.609 41.975 1.00 60.19 C
ANISOU 151 CG1 VAL A 20 7509 4942 10420 -258 -529 720 C
ATOM 152 CG2 VAL A 20 -220.141 67.170 43.715 1.00 57.27 C
ANISOU 152 CG2 VAL A 20 7116 4300 10342 -208 -483 492 C
ATOM 153 N ARG A 21 -216.156 65.036 42.743 1.00 66.00 N
ANISOU 153 N ARG A 21 8192 5888 10995 -480 -440 617 N
ATOM 154 CA ARG A 21 -215.079 64.516 41.915 1.00 55.03 C
ANISOU 154 CA ARG A 21 6782 4603 9522 -551 -406 703 C
ATOM 155 C ARG A 21 -215.616 63.412 41.013 1.00 62.51 C
ANISOU 155 C ARG A 21 7744 5664 10342 -486 -404 784 C
ATOM 156 O ARG A 21 -216.647 62.795 41.296 1.00 66.64 O
ANISOU 156 O ARG A 21 8268 6225 10829 -390 -438 750 O
ATOM 157 CB ARG A 21 -213.928 63.979 42.775 1.00 58.18 C
ANISOU 157 CB ARG A 21 7101 5109 9897 -615 -392 606 C
ATOM 158 CG ARG A 21 -213.351 65.016 43.722 1.00 61.16 C
ANISOU 158 CG ARG A 21 7470 5384 10382 -700 -408 515 C
ATOM 159 CD ARG A 21 -212.529 66.031 42.975 1.00 51.34 C
ANISOU 159 CD ARG A 21 6238 4041 9229 -804 -373 600 C
ATOM 160 NE ARG A 21 -212.006 67.050 43.876 1.00 73.08 N
ANISOU 160 NE ARG A 21 8989 6686 12092 -893 -393 507 N
ATOM 161 CZ ARG A 21 -212.569 68.236 44.083 1.00 62.95 C
ANISOU 161 CZ ARG A 21 7775 5223 10921 -896 -400 482 C
ATOM 162 NH1 ARG A 21 -212.007 69.088 44.923 1.00 64.02 N
ANISOU 162 NH1 ARG A 21 7912 5267 11146 -993 -413 381 N
ATOM 163 NH2 ARG A 21 -213.690 68.572 43.454 1.00 58.43 N
ANISOU 163 NH2 ARG A 21 7264 4553 10383 -807 -402 556 N
ATOM 164 N SER A 22 -214.905 63.177 39.915 1.00 48.63 N
ANISOU 164 N SER A 22 6004 3957 8517 -553 -354 885 N
ATOM 165 CA SER A 22 -215.243 62.075 39.020 1.00 71.05 C
ANISOU 165 CA SER A 22 8870 6911 11216 -517 -337 947 C
ATOM 166 C SER A 22 -215.269 60.757 39.793 1.00 55.51 C
ANISOU 166 C SER A 22 6824 5079 9187 -451 -335 840 C
ATOM 167 O SER A 22 -214.340 60.483 40.563 1.00 60.10 O
ANISOU 167 O SER A 22 7323 5710 9801 -483 -314 760 O
ATOM 168 CB SER A 22 -214.230 61.979 37.883 1.00 57.28 C
ANISOU 168 CB SER A 22 7151 5209 9404 -625 -243 1032 C
ATOM 169 OG SER A 22 -214.346 60.725 37.238 1.00 66.08 O
ANISOU 169 OG SER A 22 8276 6451 10380 -600 -201 1042 O
ATOM 170 N PRO A 23 -216.309 59.928 39.633 1.00 65.08 N
ANISOU 170 N PRO A 23 8060 6347 10320 -363 -371 845 N
ATOM 171 CA PRO A 23 -216.326 58.616 40.304 1.00 61.71 C
ANISOU 171 CA PRO A 23 7570 6044 9832 -308 -369 758 C
ATOM 172 C PRO A 23 -215.272 57.652 39.791 1.00 59.84 C
ANISOU 172 C PRO A 23 7288 5913 9534 -349 -291 762 C
ATOM 173 O PRO A 23 -215.134 56.555 40.345 1.00 64.60 O
ANISOU 173 O PRO A 23 7830 6604 10109 -308 -293 699 O
ATOM 174 CB PRO A 23 -217.740 58.085 40.009 1.00 53.72 C
ANISOU 174 CB PRO A 23 6603 5048 8761 -220 -420 783 C
ATOM 175 CG PRO A 23 -218.141 58.770 38.750 1.00 68.23 C
ANISOU 175 CG PRO A 23 8527 6812 10584 -249 -441 913 C
ATOM 176 CD PRO A 23 -217.529 60.155 38.837 1.00 63.26 C
ANISOU 176 CD PRO A 23 7910 6062 10065 -317 -431 939 C
ATOM 177 N PHE A 24 -214.542 58.026 38.744 1.00 65.73 N
ANISOU 177 N PHE A 24 8064 6643 10267 -434 -215 835 N
ATOM 178 CA PHE A 24 -213.420 57.251 38.246 1.00 58.37 C
ANISOU 178 CA PHE A 24 7074 5791 9314 -485 -107 823 C
ATOM 179 C PHE A 24 -212.082 57.672 38.838 1.00 61.81 C
ANISOU 179 C PHE A 24 7395 6209 9880 -553 -71 780 C
ATOM 180 O PHE A 24 -211.091 56.971 38.617 1.00 73.11 O
ANISOU 180 O PHE A 24 8735 7700 11344 -583 17 754 O
ATOM 181 CB PHE A 24 -213.335 57.360 36.720 1.00 49.02 C
ANISOU 181 CB PHE A 24 5991 4605 8027 -561 -15 917 C
ATOM 182 CG PHE A 24 -214.588 56.939 36.014 1.00 63.56 C
ANISOU 182 CG PHE A 24 7951 6467 9733 -516 -68 973 C
ATOM 183 CD1 PHE A 24 -215.054 55.636 36.121 1.00 67.78 C
ANISOU 183 CD1 PHE A 24 8466 7089 10198 -442 -75 918 C
ATOM 184 CD2 PHE A 24 -215.297 57.837 35.239 1.00 56.48 C
ANISOU 184 CD2 PHE A 24 7181 5491 8788 -553 -126 1088 C
ATOM 185 CE1 PHE A 24 -216.215 55.233 35.471 1.00 55.68 C
ANISOU 185 CE1 PHE A 24 7035 5575 8546 -412 -135 967 C
ATOM 186 CE2 PHE A 24 -216.457 57.443 34.585 1.00 69.19 C
ANISOU 186 CE2 PHE A 24 8889 7116 10283 -519 -203 1149 C
ATOM 187 CZ PHE A 24 -216.912 56.138 34.703 1.00 71.95 C
ANISOU 187 CZ PHE A 24 9215 7564 10560 -451 -205 1084 C
ATOM 188 N GLU A 25 -212.013 58.783 39.584 1.00 60.79 N
ANISOU 188 N GLU A 25 7260 5993 9843 -582 -135 766 N
ATOM 189 CA GLU A 25 -210.724 59.324 39.996 1.00 57.59 C
ANISOU 189 CA GLU A 25 6757 5562 9564 -671 -109 738 C
ATOM 190 C GLU A 25 -210.532 59.503 41.496 1.00 65.01 C
ANISOU 190 C GLU A 25 7628 6489 10583 -664 -217 648 C
ATOM 191 O GLU A 25 -209.379 59.552 41.938 1.00 68.85 O
ANISOU 191 O GLU A 25 8002 6986 11172 -731 -219 617 O
ATOM 192 CB GLU A 25 -210.471 60.683 39.323 1.00 49.46 C
ANISOU 192 CB GLU A 25 5794 4421 8577 -770 -66 813 C
ATOM 193 CG GLU A 25 -210.240 60.626 37.811 1.00 70.91 C
ANISOU 193 CG GLU A 25 8579 7149 11212 -836 60 909 C
ATOM 194 CD GLU A 25 -209.805 61.979 37.222 1.00108.75 C
ANISOU 194 CD GLU A 25 13434 11828 16057 -958 104 993 C
ATOM 195 OE1 GLU A 25 -210.026 63.038 37.860 1.00 93.16 O
ANISOU 195 OE1 GLU A 25 11479 9744 14173 -967 20 989 O
ATOM 196 OE2 GLU A 25 -209.231 61.985 36.111 1.00128.63 O
ANISOU 196 OE2 GLU A 25 15989 14361 18524 -1054 235 1058 O
ATOM 197 N ALA A 26 -211.597 59.606 42.290 1.00 54.04 N
ANISOU 197 N ALA A 26 6303 5079 9153 -597 -304 603 N
ATOM 198 CA ALA A 26 -211.409 60.053 43.665 1.00 51.64 C
ANISOU 198 CA ALA A 26 5974 4743 8903 -627 -392 514 C
ATOM 199 C ALA A 26 -212.604 59.628 44.494 1.00 58.47 C
ANISOU 199 C ALA A 26 6899 5629 9688 -542 -452 451 C
ATOM 200 O ALA A 26 -213.709 59.500 43.958 1.00 57.89 O
ANISOU 200 O ALA A 26 6893 5544 9560 -466 -432 483 O
ATOM 201 CB ALA A 26 -211.228 61.583 43.725 1.00 48.01 C
ANISOU 201 CB ALA A 26 5558 4148 8535 -708 -391 514 C
ATOM 202 N PRO A 27 -212.429 59.437 45.801 1.00 63.95 N
ANISOU 202 N PRO A 27 7575 6351 10373 -566 -529 363 N
ATOM 203 CA PRO A 27 -213.504 58.857 46.615 1.00 66.10 C
ANISOU 203 CA PRO A 27 7904 6660 10552 -500 -566 299 C
ATOM 204 C PRO A 27 -214.706 59.776 46.746 1.00 60.40 C
ANISOU 204 C PRO A 27 7274 5832 9843 -466 -538 257 C
ATOM 205 O PRO A 27 -214.584 61.001 46.796 1.00 69.65 O
ANISOU 205 O PRO A 27 8476 6889 11100 -518 -525 236 O
ATOM 206 CB PRO A 27 -212.836 58.621 47.977 1.00 67.16 C
ANISOU 206 CB PRO A 27 8015 6836 10666 -575 -659 224 C
ATOM 207 CG PRO A 27 -211.634 59.488 47.988 1.00 61.21 C
ANISOU 207 CG PRO A 27 7208 6030 10019 -682 -680 228 C
ATOM 208 CD PRO A 27 -211.186 59.625 46.564 1.00 47.97 C
ANISOU 208 CD PRO A 27 5475 4336 8415 -668 -592 326 C
ATOM 209 N GLN A 28 -215.881 59.157 46.824 1.00 71.21 N
ANISOU 209 N GLN A 28 8677 7232 11146 -378 -527 241 N
ATOM 210 CA GLN A 28 -217.161 59.869 46.837 1.00 61.58 C
ANISOU 210 CA GLN A 28 7515 5910 9971 -323 -493 207 C
ATOM 211 C GLN A 28 -217.717 60.014 48.250 1.00 59.53 C
ANISOU 211 C GLN A 28 7302 5633 9684 -343 -487 65 C
ATOM 212 O GLN A 28 -218.883 59.706 48.499 1.00 74.99 O
ANISOU 212 O GLN A 28 9279 7589 11624 -276 -454 21 O
ATOM 213 CB GLN A 28 -218.158 59.152 45.938 1.00 66.93 C
ANISOU 213 CB GLN A 28 8190 6625 10615 -221 -479 282 C
ATOM 214 CG GLN A 28 -217.658 58.926 44.529 1.00 67.13 C
ANISOU 214 CG GLN A 28 8199 6677 10629 -220 -473 412 C
ATOM 215 CD GLN A 28 -217.658 60.197 43.719 1.00 68.78 C
ANISOU 215 CD GLN A 28 8442 6756 10936 -244 -463 485 C
ATOM 216 OE1 GLN A 28 -218.676 60.887 43.631 1.00 59.61 O
ANISOU 216 OE1 GLN A 28 7310 5487 9851 -195 -475 491 O
ATOM 217 NE2 GLN A 28 -216.510 60.526 43.131 1.00 67.01 N
ANISOU 217 NE2 GLN A 28 8206 6529 10725 -323 -442 545 N
ATOM 218 N TYR A 29 -216.905 60.503 49.189 1.00 60.59 N
ANISOU 218 N TYR A 29 7458 5751 9814 -449 -515 -15 N
ATOM 219 CA TYR A 29 -217.314 60.572 50.590 1.00 55.50 C
ANISOU 219 CA TYR A 29 6884 5104 9100 -502 -506 -160 C
ATOM 220 C TYR A 29 -218.259 61.729 50.896 1.00 66.51 C
ANISOU 220 C TYR A 29 8332 6344 10595 -489 -419 -266 C
ATOM 221 O TYR A 29 -218.625 61.904 52.065 1.00 61.26 O
ANISOU 221 O TYR A 29 7741 5662 9874 -547 -379 -410 O
ATOM 222 CB TYR A 29 -216.086 60.652 51.504 1.00 56.71 C
ANISOU 222 CB TYR A 29 7054 5297 9197 -640 -588 -207 C
ATOM 223 CG TYR A 29 -215.206 59.416 51.452 1.00 67.00 C
ANISOU 223 CG TYR A 29 8290 6742 10425 -651 -683 -119 C
ATOM 224 CD1 TYR A 29 -215.758 58.139 51.373 1.00 64.74 C
ANISOU 224 CD1 TYR A 29 7991 6556 10050 -573 -686 -78 C
ATOM 225 CD2 TYR A 29 -213.822 59.531 51.463 1.00 60.10 C
ANISOU 225 CD2 TYR A 29 7352 5888 9595 -737 -768 -76 C
ATOM 226 CE1 TYR A 29 -214.947 57.009 51.316 1.00 56.92 C
ANISOU 226 CE1 TYR A 29 6931 5672 9023 -575 -770 1 C
ATOM 227 CE2 TYR A 29 -213.008 58.425 51.402 1.00 46.72 C
ANISOU 227 CE2 TYR A 29 5572 4302 7879 -737 -852 3 C
ATOM 228 CZ TYR A 29 -213.571 57.164 51.328 1.00 56.79 C
ANISOU 228 CZ TYR A 29 6841 5665 9072 -653 -852 41 C
ATOM 229 OH TYR A 29 -212.739 56.074 51.266 1.00 61.51 O
ANISOU 229 OH TYR A 29 7346 6348 9678 -647 -934 118 O
ATOM 230 N TYR A 30 -218.660 62.518 49.892 1.00 74.65 N
ANISOU 230 N TYR A 30 9334 7254 11775 -420 -386 -199 N
ATOM 231 CA TYR A 30 -219.764 63.458 50.072 1.00 75.10 C
ANISOU 231 CA TYR A 30 9415 7152 11970 -371 -304 -284 C
ATOM 232 C TYR A 30 -221.110 62.786 49.854 1.00 75.30 C
ANISOU 232 C TYR A 30 9405 7201 12004 -252 -262 -275 C
ATOM 233 O TYR A 30 -222.127 63.290 50.344 1.00 86.84 O
ANISOU 233 O TYR A 30 10872 8555 13567 -215 -176 -385 O
ATOM 234 CB TYR A 30 -219.621 64.668 49.134 1.00 73.25 C
ANISOU 234 CB TYR A 30 9163 6752 11915 -355 -309 -202 C
ATOM 235 CG TYR A 30 -219.109 64.305 47.761 1.00 71.95 C
ANISOU 235 CG TYR A 30 8956 6646 11737 -327 -373 -9 C
ATOM 236 CD1 TYR A 30 -219.974 63.884 46.760 1.00 66.23 C
ANISOU 236 CD1 TYR A 30 8200 5929 11035 -220 -388 106 C
ATOM 237 CD2 TYR A 30 -217.752 64.355 47.475 1.00 55.49 C
ANISOU 237 CD2 TYR A 30 6862 4610 9611 -419 -413 52 C
ATOM 238 CE1 TYR A 30 -219.498 63.532 45.509 1.00 63.84 C
ANISOU 238 CE1 TYR A 30 7884 5685 10687 -217 -434 270 C
ATOM 239 CE2 TYR A 30 -217.272 64.001 46.236 1.00 53.36 C
ANISOU 239 CE2 TYR A 30 6561 4395 9319 -408 -438 210 C
ATOM 240 CZ TYR A 30 -218.143 63.591 45.256 1.00 57.54 C
ANISOU 240 CZ TYR A 30 7086 4934 9843 -312 -445 315 C
ATOM 241 OH TYR A 30 -217.652 63.240 44.018 1.00 63.89 O
ANISOU 241 OH TYR A 30 7885 5795 10598 -323 -458 460 O
ATOM 242 N LEU A 31 -221.131 61.654 49.138 1.00 67.20 N
ANISOU 242 N LEU A 31 8338 6307 10887 -198 -314 -156 N
ATOM 243 CA LEU A 31 -222.351 60.859 49.016 1.00 62.47 C
ANISOU 243 CA LEU A 31 7705 5752 10278 -103 -287 -152 C
ATOM 244 C LEU A 31 -222.649 60.096 50.294 1.00 61.61 C
ANISOU 244 C LEU A 31 7636 5735 10037 -145 -237 -282 C
ATOM 245 O LEU A 31 -223.818 59.870 50.627 1.00 70.30 O
ANISOU 245 O LEU A 31 8721 6818 11174 -92 -163 -350 O
ATOM 246 CB LEU A 31 -222.230 59.858 47.865 1.00 56.12 C
ANISOU 246 CB LEU A 31 6861 5058 9403 -50 -357 6 C
ATOM 247 CG LEU A 31 -221.999 60.380 46.452 1.00 66.52 C
ANISOU 247 CG LEU A 31 8162 6313 10801 -22 -408 158 C
ATOM 248 CD1 LEU A 31 -221.811 59.211 45.504 1.00 57.22 C
ANISOU 248 CD1 LEU A 31 6969 5268 9505 3 -454 275 C
ATOM 249 CD2 LEU A 31 -223.169 61.267 46.017 1.00 63.13 C
ANISOU 249 CD2 LEU A 31 7707 5724 10556 56 -403 180 C
ATOM 250 N ALA A 32 -221.610 59.666 51.001 1.00 67.80 N
ANISOU 250 N ALA A 32 8470 6618 10674 -246 -281 -309 N
ATOM 251 CA ALA A 32 -221.777 58.778 52.139 1.00 56.74 C
ANISOU 251 CA ALA A 32 7125 5322 9110 -303 -264 -395 C
ATOM 252 C ALA A 32 -220.495 58.789 52.946 1.00 57.41 C
ANISOU 252 C ALA A 32 7271 5462 9078 -438 -340 -424 C
ATOM 253 O ALA A 32 -219.405 58.986 52.401 1.00 62.10 O
ANISOU 253 O ALA A 32 7827 6063 9705 -462 -422 -338 O
ATOM 254 CB ALA A 32 -222.120 57.353 51.695 1.00 44.19 C
ANISOU 254 CB ALA A 32 5494 3860 7435 -237 -300 -301 C
ATOM 255 N GLU A 33 -220.644 58.585 54.250 1.00 46.83 N
ANISOU 255 N GLU A 33 6029 4160 7604 -536 -313 -545 N
ATOM 256 CA GLU A 33 -219.495 58.491 55.132 1.00 52.49 C
ANISOU 256 CA GLU A 33 6816 4938 8189 -681 -416 -566 C
ATOM 257 C GLU A 33 -218.623 57.289 54.750 1.00 69.79 C
ANISOU 257 C GLU A 33 8944 7258 10316 -666 -555 -415 C
ATOM 258 O GLU A 33 -219.108 56.320 54.147 1.00 54.59 O
ANISOU 258 O GLU A 33 6963 5394 8385 -566 -548 -333 O
ATOM 259 CB GLU A 33 -219.973 58.352 56.574 1.00 58.34 C
ANISOU 259 CB GLU A 33 7698 5706 8762 -799 -360 -714 C
ATOM 260 CG GLU A 33 -220.681 59.566 57.101 1.00 61.38 C
ANISOU 260 CG GLU A 33 8152 5954 9214 -837 -206 -895 C
ATOM 261 CD GLU A 33 -219.718 60.693 57.344 1.00 93.57 C
ANISOU 261 CD GLU A 33 12272 9948 13334 -943 -255 -949 C
ATOM 262 OE1 GLU A 33 -218.727 60.467 58.073 1.00112.52 O
ANISOU 262 OE1 GLU A 33 14744 12423 15584 -1085 -382 -945 O
ATOM 263 OE2 GLU A 33 -219.935 61.791 56.790 1.00106.24 O
ANISOU 263 OE2 GLU A 33 13831 11406 15129 -887 -182 -983 O
ATOM 264 N PRO A 34 -217.325 57.330 55.074 1.00 61.99 N
ANISOU 264 N PRO A 34 7952 6303 9297 -765 -684 -379 N
ATOM 265 CA PRO A 34 -216.482 56.146 54.821 1.00 46.24 C
ANISOU 265 CA PRO A 34 5882 4416 7272 -750 -814 -245 C
ATOM 266 C PRO A 34 -217.038 54.861 55.427 1.00 56.66 C
ANISOU 266 C PRO A 34 7253 5831 8444 -746 -837 -229 C
ATOM 267 O PRO A 34 -217.052 53.826 54.746 1.00 49.37 O
ANISOU 267 O PRO A 34 6251 4964 7545 -652 -860 -125 O
ATOM 268 CB PRO A 34 -215.134 56.549 55.430 1.00 47.50 C
ANISOU 268 CB PRO A 34 6043 4579 7426 -887 -953 -243 C
ATOM 269 CG PRO A 34 -215.093 58.060 55.272 1.00 55.39 C
ANISOU 269 CG PRO A 34 7063 5457 8527 -925 -879 -329 C
ATOM 270 CD PRO A 34 -216.527 58.540 55.364 1.00 48.96 C
ANISOU 270 CD PRO A 34 6326 4571 7704 -870 -714 -439 C
ATOM 271 N TRP A 35 -217.544 54.906 56.666 1.00 49.97 N
ANISOU 271 N TRP A 35 6548 4997 7442 -853 -816 -335 N
ATOM 272 CA TRP A 35 -218.097 53.704 57.288 1.00 51.97 C
ANISOU 272 CA TRP A 35 6867 5336 7542 -869 -832 -315 C
ATOM 273 C TRP A 35 -219.300 53.152 56.521 1.00 70.90 C
ANISOU 273 C TRP A 35 9211 7735 9991 -725 -704 -299 C
ATOM 274 O TRP A 35 -219.574 51.949 56.587 1.00 59.94 O
ANISOU 274 O TRP A 35 7824 6420 8532 -698 -735 -231 O
ATOM 275 CB TRP A 35 -218.480 53.984 58.745 1.00 57.41 C
ANISOU 275 CB TRP A 35 7743 6033 8037 -1033 -802 -448 C
ATOM 276 CG TRP A 35 -219.721 54.824 58.947 1.00 69.96 C
ANISOU 276 CG TRP A 35 9397 7544 9641 -1024 -586 -613 C
ATOM 277 CD1 TRP A 35 -219.768 56.170 59.159 1.00 66.00 C
ANISOU 277 CD1 TRP A 35 8938 6938 9202 -1074 -498 -748 C
ATOM 278 CD2 TRP A 35 -221.085 54.365 58.988 1.00 68.58 C
ANISOU 278 CD2 TRP A 35 9240 7375 9444 -963 -427 -667 C
ATOM 279 NE1 TRP A 35 -221.067 56.581 59.319 1.00 66.27 N
ANISOU 279 NE1 TRP A 35 9005 6905 9269 -1039 -290 -885 N
ATOM 280 CE2 TRP A 35 -221.897 55.496 59.219 1.00 73.53 C
ANISOU 280 CE2 TRP A 35 9904 7895 10141 -972 -243 -837 C
ATOM 281 CE3 TRP A 35 -221.696 53.114 58.846 1.00 69.92 C
ANISOU 281 CE3 TRP A 35 9387 7621 9560 -904 -420 -590 C
ATOM 282 CZ2 TRP A 35 -223.293 55.416 59.307 1.00 67.66 C
ANISOU 282 CZ2 TRP A 35 9158 7120 9430 -919 -51 -932 C
ATOM 283 CZ3 TRP A 35 -223.089 53.033 58.938 1.00 67.54 C
ANISOU 283 CZ3 TRP A 35 9094 7296 9271 -862 -234 -682 C
ATOM 284 CH2 TRP A 35 -223.868 54.180 59.165 1.00 66.82 C
ANISOU 284 CH2 TRP A 35 9023 7100 9266 -868 -52 -851 C
ATOM 285 N GLN A 36 -220.032 54.000 55.794 1.00 66.31 N
ANISOU 285 N GLN A 36 8582 7070 9544 -636 -573 -352 N
ATOM 286 CA GLN A 36 -221.121 53.481 54.972 1.00 68.74 C
ANISOU 286 CA GLN A 36 8821 7377 9918 -503 -483 -319 C
ATOM 287 C GLN A 36 -220.590 52.777 53.732 1.00 56.12 C
ANISOU 287 C GLN A 36 7108 5817 8399 -401 -560 -171 C
ATOM 288 O GLN A 36 -221.214 51.830 53.236 1.00 52.92 O
ANISOU 288 O GLN A 36 6665 5453 7987 -323 -542 -118 O
ATOM 289 CB GLN A 36 -222.080 54.610 54.595 1.00 47.14 C
ANISOU 289 CB GLN A 36 6062 4526 7321 -442 -344 -408 C
ATOM 290 CG GLN A 36 -222.760 55.185 55.818 1.00 65.01 C
ANISOU 290 CG GLN A 36 8436 6746 9520 -537 -225 -580 C
ATOM 291 CD GLN A 36 -223.449 56.511 55.559 1.00 75.02 C
ANISOU 291 CD GLN A 36 9672 7866 10965 -489 -98 -682 C
ATOM 292 OE1 GLN A 36 -222.963 57.353 54.793 1.00 70.14 O
ANISOU 292 OE1 GLN A 36 8997 7168 10486 -446 -135 -637 O
ATOM 293 NE2 GLN A 36 -224.589 56.706 56.206 1.00 65.65 N
ANISOU 293 NE2 GLN A 36 8521 6633 9791 -500 61 -820 N
ATOM 294 N PHE A 37 -219.448 53.224 53.216 1.00 49.90 N
ANISOU 294 N PHE A 37 6264 5010 7686 -410 -633 -113 N
ATOM 295 CA PHE A 37 -218.783 52.463 52.170 1.00 51.18 C
ANISOU 295 CA PHE A 37 6326 5213 7906 -339 -690 11 C
ATOM 296 C PHE A 37 -218.315 51.116 52.712 1.00 61.32 C
ANISOU 296 C PHE A 37 7611 6585 9101 -365 -788 68 C
ATOM 297 O PHE A 37 -218.450 50.087 52.039 1.00 53.56 O
ANISOU 297 O PHE A 37 6576 5641 8135 -287 -789 139 O
ATOM 298 CB PHE A 37 -217.627 53.277 51.589 1.00 42.05 C
ANISOU 298 CB PHE A 37 5107 4014 6857 -361 -726 49 C
ATOM 299 CG PHE A 37 -218.058 54.251 50.527 1.00 50.90 C
ANISOU 299 CG PHE A 37 6202 5052 8088 -300 -640 56 C
ATOM 300 CD1 PHE A 37 -218.473 55.538 50.866 1.00 55.07 C
ANISOU 300 CD1 PHE A 37 6779 5482 8663 -332 -587 -29 C
ATOM 301 CD2 PHE A 37 -218.070 53.877 49.187 1.00 43.66 C
ANISOU 301 CD2 PHE A 37 5221 4145 7224 -218 -615 147 C
ATOM 302 CE1 PHE A 37 -218.890 56.439 49.884 1.00 57.38 C
ANISOU 302 CE1 PHE A 37 7048 5681 9073 -274 -529 -3 C
ATOM 303 CE2 PHE A 37 -218.486 54.778 48.196 1.00 58.70 C
ANISOU 303 CE2 PHE A 37 7120 5969 9214 -176 -559 175 C
ATOM 304 CZ PHE A 37 -218.896 56.058 48.547 1.00 47.20 C
ANISOU 304 CZ PHE A 37 5704 4409 7822 -200 -526 109 C
ATOM 305 N SER A 38 -217.825 51.099 53.957 1.00 42.62 N
ANISOU 305 N SER A 38 5317 4241 6637 -482 -875 37 N
ATOM 306 CA SER A 38 -217.435 49.847 54.597 1.00 70.33 C
ANISOU 306 CA SER A 38 8843 7819 10061 -519 -992 105 C
ATOM 307 C SER A 38 -218.628 48.912 54.750 1.00 60.68 C
ANISOU 307 C SER A 38 7675 6633 8748 -479 -925 100 C
ATOM 308 O SER A 38 -218.532 47.715 54.448 1.00 61.19 O
ANISOU 308 O SER A 38 7695 6733 8821 -426 -972 185 O
ATOM 309 CB SER A 38 -216.806 50.120 55.962 1.00 49.88 C
ANISOU 309 CB SER A 38 6351 5245 7357 -677 -1112 76 C
ATOM 310 OG SER A 38 -215.658 50.918 55.847 1.00 54.19 O
ANISOU 310 OG SER A 38 6833 5757 7998 -723 -1190 86 O
ATOM 311 N MET A 39 -219.760 49.439 55.234 1.00 65.55 N
ANISOU 311 N MET A 39 8382 7231 9293 -506 -805 -8 N
ATOM 312 CA MET A 39 -220.963 48.617 55.340 1.00 60.81 C
ANISOU 312 CA MET A 39 7817 6659 8627 -473 -723 -21 C
ATOM 313 C MET A 39 -221.412 48.119 53.973 1.00 61.14 C
ANISOU 313 C MET A 39 7747 6695 8787 -329 -677 41 C
ATOM 314 O MET A 39 -221.901 46.986 53.856 1.00 52.39 O
ANISOU 314 O MET A 39 6635 5626 7646 -294 -677 86 O
ATOM 315 CB MET A 39 -222.083 49.383 56.040 1.00 54.23 C
ANISOU 315 CB MET A 39 7074 5794 7738 -525 -577 -163 C
ATOM 316 CG MET A 39 -221.889 49.552 57.544 1.00 57.93 C
ANISOU 316 CG MET A 39 7701 6286 8024 -697 -599 -237 C
ATOM 317 SD MET A 39 -221.338 48.040 58.382 1.00 70.25 S
ANISOU 317 SD MET A 39 9345 7938 9411 -790 -765 -118 S
ATOM 318 CE MET A 39 -222.636 46.882 57.922 1.00 70.99 C
ANISOU 318 CE MET A 39 9403 8056 9513 -695 -656 -89 C
ATOM 319 N LEU A 40 -221.214 48.920 52.919 1.00 45.92 N
ANISOU 319 N LEU A 40 5739 4719 6990 -257 -646 49 N
ATOM 320 CA LEU A 40 -221.420 48.386 51.575 1.00 56.86 C
ANISOU 320 CA LEU A 40 7038 6108 8460 -146 -629 121 C
ATOM 321 C LEU A 40 -220.479 47.217 51.303 1.00 67.97 C
ANISOU 321 C LEU A 40 8399 7560 9868 -131 -719 214 C
ATOM 322 O LEU A 40 -220.902 46.191 50.758 1.00 68.36 O
ANISOU 322 O LEU A 40 8425 7633 9917 -73 -707 255 O
ATOM 323 CB LEU A 40 -221.234 49.479 50.524 1.00 39.03 C
ANISOU 323 CB LEU A 40 4724 3788 6317 -99 -593 129 C
ATOM 324 CG LEU A 40 -221.426 48.926 49.107 1.00 55.68 C
ANISOU 324 CG LEU A 40 6771 5905 8479 -10 -579 204 C
ATOM 325 CD1 LEU A 40 -222.821 48.309 48.959 1.00 58.81 C
ANISOU 325 CD1 LEU A 40 7178 6316 8852 39 -532 190 C
ATOM 326 CD2 LEU A 40 -221.187 49.985 48.053 1.00 59.05 C
ANISOU 326 CD2 LEU A 40 7166 6273 8997 16 -554 231 C
ATOM 327 N ALA A 41 -219.204 47.348 51.693 1.00 54.71 N
ANISOU 327 N ALA A 41 6698 5882 8206 -186 -812 244 N
ATOM 328 CA ALA A 41 -218.248 46.258 51.524 1.00 54.58 C
ANISOU 328 CA ALA A 41 6615 5889 8234 -168 -902 330 C
ATOM 329 C ALA A 41 -218.664 45.031 52.331 1.00 51.95 C
ANISOU 329 C ALA A 41 6340 5592 7807 -191 -957 359 C
ATOM 330 O ALA A 41 -218.633 43.906 51.826 1.00 46.08 O
ANISOU 330 O ALA A 41 5550 4854 7103 -130 -967 415 O
ATOM 331 CB ALA A 41 -216.846 46.723 51.936 1.00 49.89 C
ANISOU 331 CB ALA A 41 5972 5282 7701 -233 -1007 356 C
ATOM 332 N ALA A 42 -219.054 45.235 53.594 1.00 45.12 N
ANISOU 332 N ALA A 42 5588 4745 6811 -289 -985 319 N
ATOM 333 CA ALA A 42 -219.467 44.122 54.442 1.00 44.08 C
ANISOU 333 CA ALA A 42 5536 4646 6568 -336 -1036 355 C
ATOM 334 C ALA A 42 -220.655 43.377 53.844 1.00 59.37 C
ANISOU 334 C ALA A 42 7469 6589 8499 -260 -930 346 C
ATOM 335 O ALA A 42 -220.740 42.146 53.930 1.00 66.91 O
ANISOU 335 O ALA A 42 8429 7554 9438 -248 -975 411 O
ATOM 336 CB ALA A 42 -219.807 44.638 55.838 1.00 41.90 C
ANISOU 336 CB ALA A 42 5408 4389 6123 -476 -1047 291 C
ATOM 337 N TYR A 43 -221.582 44.109 53.234 1.00 52.53 N
ANISOU 337 N TYR A 43 6589 5708 7660 -212 -800 272 N
ATOM 338 CA TYR A 43 -222.725 43.483 52.582 1.00 63.29 C
ANISOU 338 CA TYR A 43 7933 7076 9038 -144 -715 265 C
ATOM 339 C TYR A 43 -222.287 42.643 51.390 1.00 57.00 C
ANISOU 339 C TYR A 43 7050 6273 8335 -53 -741 337 C
ATOM 340 O TYR A 43 -222.805 41.539 51.182 1.00 62.74 O
ANISOU 340 O TYR A 43 7780 7010 9050 -27 -734 365 O
ATOM 341 CB TYR A 43 -223.710 44.570 52.158 1.00 61.16 C
ANISOU 341 CB TYR A 43 7648 6778 8812 -111 -599 183 C
ATOM 342 CG TYR A 43 -224.952 44.100 51.450 1.00 65.90 C
ANISOU 342 CG TYR A 43 8213 7378 9449 -46 -525 175 C
ATOM 343 CD1 TYR A 43 -225.747 43.091 51.978 1.00 64.70 C
ANISOU 343 CD1 TYR A 43 8099 7255 9230 -76 -500 174 C
ATOM 344 CD2 TYR A 43 -225.360 44.706 50.272 1.00 79.82 C
ANISOU 344 CD2 TYR A 43 9906 9107 11313 31 -490 175 C
ATOM 345 CE1 TYR A 43 -226.901 42.682 51.328 1.00 71.29 C
ANISOU 345 CE1 TYR A 43 8889 8086 10113 -25 -441 165 C
ATOM 346 CE2 TYR A 43 -226.504 44.310 49.621 1.00 82.78 C
ANISOU 346 CE2 TYR A 43 10244 9480 11727 80 -450 175 C
ATOM 347 CZ TYR A 43 -227.272 43.301 50.149 1.00 78.94 C
ANISOU 347 CZ TYR A 43 9781 9023 11188 53 -424 165 C
ATOM 348 OH TYR A 43 -228.411 42.923 49.482 1.00 75.22 O
ANISOU 348 OH TYR A 43 9261 8549 10771 95 -393 164 O
ATOM 349 N MET A 44 -221.351 43.157 50.586 1.00 57.02 N
ANISOU 349 N MET A 44 6981 6255 8430 -14 -757 357 N
ATOM 350 CA MET A 44 -220.803 42.369 49.484 1.00 59.43 C
ANISOU 350 CA MET A 44 7211 6549 8819 55 -760 407 C
ATOM 351 C MET A 44 -220.095 41.123 50.005 1.00 63.95 C
ANISOU 351 C MET A 44 7769 7119 9410 46 -850 470 C
ATOM 352 O MET A 44 -220.150 40.058 49.383 1.00 59.63 O
ANISOU 352 O MET A 44 7192 6558 8906 97 -835 496 O
ATOM 353 CB MET A 44 -219.830 43.211 48.656 1.00 56.96 C
ANISOU 353 CB MET A 44 6831 6214 8598 75 -744 413 C
ATOM 354 CG MET A 44 -220.453 44.417 47.979 1.00 55.93 C
ANISOU 354 CG MET A 44 6714 6069 8469 88 -669 374 C
ATOM 355 SD MET A 44 -221.728 43.954 46.796 1.00 60.13 S
ANISOU 355 SD MET A 44 7258 6605 8983 149 -601 374 S
ATOM 356 CE MET A 44 -223.162 44.699 47.562 1.00 55.11 C
ANISOU 356 CE MET A 44 6669 5961 8308 132 -573 316 C
ATOM 357 N PHE A 45 -219.402 41.244 51.135 1.00 54.47 N
ANISOU 357 N PHE A 45 6591 5921 8184 -24 -954 498 N
ATOM 358 CA PHE A 45 -218.715 40.089 51.694 1.00 59.85 C
ANISOU 358 CA PHE A 45 7256 6586 8900 -36 -1072 579 C
ATOM 359 C PHE A 45 -219.716 39.014 52.103 1.00 62.96 C
ANISOU 359 C PHE A 45 7730 6988 9206 -48 -1066 598 C
ATOM 360 O PHE A 45 -219.513 37.825 51.827 1.00 58.53 O
ANISOU 360 O PHE A 45 7132 6392 8716 -4 -1098 652 O
ATOM 361 CB PHE A 45 -217.855 40.529 52.878 1.00 44.60 C
ANISOU 361 CB PHE A 45 5349 4658 6937 -131 -1213 616 C
ATOM 362 CG PHE A 45 -216.993 39.442 53.458 1.00 51.30 C
ANISOU 362 CG PHE A 45 6163 5474 7852 -146 -1375 724 C
ATOM 363 CD1 PHE A 45 -215.974 38.867 52.709 1.00 56.51 C
ANISOU 363 CD1 PHE A 45 6673 6081 8718 -64 -1405 772 C
ATOM 364 CD2 PHE A 45 -217.167 39.030 54.770 1.00 51.32 C
ANISOU 364 CD2 PHE A 45 6285 5493 7721 -250 -1499 779 C
ATOM 365 CE1 PHE A 45 -215.163 37.877 53.248 1.00 46.17 C
ANISOU 365 CE1 PHE A 45 5310 4721 7513 -67 -1566 879 C
ATOM 366 CE2 PHE A 45 -216.355 38.036 55.321 1.00 55.47 C
ANISOU 366 CE2 PHE A 45 6780 5976 8320 -267 -1679 902 C
ATOM 367 CZ PHE A 45 -215.351 37.467 54.560 1.00 45.77 C
ANISOU 367 CZ PHE A 45 5379 4682 7332 -167 -1720 955 C
ATOM 368 N LEU A 46 -220.809 39.421 52.753 1.00 53.77 N
ANISOU 368 N LEU A 46 6669 5859 7900 -110 -1011 545 N
ATOM 369 CA LEU A 46 -221.869 38.484 53.108 1.00 57.85 C
ANISOU 369 CA LEU A 46 7259 6386 8334 -132 -978 553 C
ATOM 370 C LEU A 46 -222.401 37.767 51.874 1.00 65.91 C
ANISOU 370 C LEU A 46 8217 7388 9438 -37 -901 545 C
ATOM 371 O LEU A 46 -222.509 36.533 51.852 1.00 61.35 O
ANISOU 371 O LEU A 46 7645 6784 8880 -24 -930 595 O
ATOM 372 CB LEU A 46 -222.997 39.222 53.821 1.00 59.16 C
ANISOU 372 CB LEU A 46 7519 6589 8368 -206 -885 470 C
ATOM 373 CG LEU A 46 -224.195 38.366 54.225 1.00 64.53 C
ANISOU 373 CG LEU A 46 8269 7284 8967 -245 -823 465 C
ATOM 374 CD1 LEU A 46 -223.766 37.398 55.296 1.00 46.11 C
ANISOU 374 CD1 LEU A 46 6028 4949 6544 -335 -941 557 C
ATOM 375 CD2 LEU A 46 -225.347 39.233 54.713 1.00 56.16 C
ANISOU 375 CD2 LEU A 46 7262 6250 7828 -300 -688 357 C
ATOM 376 N LEU A 47 -222.713 38.528 50.821 1.00 56.22 N
ANISOU 376 N LEU A 47 6937 6166 8259 23 -811 486 N
ATOM 377 CA LEU A 47 -223.223 37.918 49.600 1.00 47.94 C
ANISOU 377 CA LEU A 47 5847 5103 7263 93 -749 475 C
ATOM 378 C LEU A 47 -222.213 36.946 49.002 1.00 57.71 C
ANISOU 378 C LEU A 47 7025 6296 8604 143 -787 522 C
ATOM 379 O LEU A 47 -222.579 35.837 48.599 1.00 58.30 O
ANISOU 379 O LEU A 47 7105 6347 8701 167 -771 532 O
ATOM 380 CB LEU A 47 -223.610 38.995 48.592 1.00 46.08 C
ANISOU 380 CB LEU A 47 5579 4877 7052 131 -674 424 C
ATOM 381 CG LEU A 47 -224.784 39.884 49.042 1.00 65.08 C
ANISOU 381 CG LEU A 47 8019 7304 9406 101 -621 369 C
ATOM 382 CD1 LEU A 47 -224.999 41.061 48.107 1.00 55.53 C
ANISOU 382 CD1 LEU A 47 6771 6082 8245 140 -579 340 C
ATOM 383 CD2 LEU A 47 -226.063 39.083 49.171 1.00 53.84 C
ANISOU 383 CD2 LEU A 47 6619 5891 7949 89 -583 354 C
ATOM 384 N ILE A 48 -220.937 37.347 48.931 1.00 62.67 N
ANISOU 384 N ILE A 48 7591 6906 9314 156 -829 544 N
ATOM 385 CA ILE A 48 -219.900 36.467 48.387 1.00 53.16 C
ANISOU 385 CA ILE A 48 6305 5646 8249 208 -847 577 C
ATOM 386 C ILE A 48 -219.817 35.179 49.197 1.00 55.01 C
ANISOU 386 C ILE A 48 6557 5837 8507 196 -940 645 C
ATOM 387 O ILE A 48 -219.773 34.077 48.641 1.00 54.32 O
ANISOU 387 O ILE A 48 6442 5694 8503 243 -916 651 O
ATOM 388 CB ILE A 48 -218.535 37.185 48.359 1.00 58.96 C
ANISOU 388 CB ILE A 48 6950 6365 9088 213 -882 592 C
ATOM 389 CG1 ILE A 48 -218.548 38.375 47.402 1.00 64.77 C
ANISOU 389 CG1 ILE A 48 7669 7127 9812 223 -781 534 C
ATOM 390 CG2 ILE A 48 -217.408 36.211 47.948 1.00 43.97 C
ANISOU 390 CG2 ILE A 48 4939 4392 7375 268 -898 623 C
ATOM 391 CD1 ILE A 48 -217.434 39.386 47.691 1.00 63.89 C
ANISOU 391 CD1 ILE A 48 7494 7013 9767 195 -823 546 C
ATOM 392 N MET A 49 -219.798 35.305 50.527 1.00 59.13 N
ANISOU 392 N MET A 49 7140 6377 8951 123 -1049 698 N
ATOM 393 CA MET A 49 -219.536 34.163 51.392 1.00 45.27 C
ANISOU 393 CA MET A 49 5410 4572 7219 96 -1171 792 C
ATOM 394 C MET A 49 -220.709 33.185 51.424 1.00 66.65 C
ANISOU 394 C MET A 49 8199 7273 9854 83 -1125 792 C
ATOM 395 O MET A 49 -220.503 31.982 51.606 1.00 61.64 O
ANISOU 395 O MET A 49 7560 6566 9293 95 -1190 861 O
ATOM 396 CB MET A 49 -219.193 34.655 52.799 1.00 58.31 C
ANISOU 396 CB MET A 49 7131 6253 8771 -7 -1308 853 C
ATOM 397 CG MET A 49 -217.851 35.398 52.918 1.00 69.58 C
ANISOU 397 CG MET A 49 8466 7670 10301 -7 -1401 877 C
ATOM 398 SD MET A 49 -216.396 34.324 52.789 1.00 66.20 S
ANISOU 398 SD MET A 49 7884 7132 10137 61 -1541 985 S
ATOM 399 CE MET A 49 -216.077 34.447 51.030 1.00 68.27 C
ANISOU 399 CE MET A 49 8002 7365 10572 187 -1347 883 C
ATOM 400 N LEU A 50 -221.937 33.674 51.261 1.00 58.68 N
ANISOU 400 N LEU A 50 7252 6324 8720 57 -1018 719 N
ATOM 401 CA LEU A 50 -223.083 32.790 51.129 1.00 53.60 C
ANISOU 401 CA LEU A 50 6662 5673 8031 46 -961 707 C
ATOM 402 C LEU A 50 -223.312 32.375 49.682 1.00 67.19 C
ANISOU 402 C LEU A 50 8322 7367 9841 127 -870 650 C
ATOM 403 O LEU A 50 -223.652 31.218 49.409 1.00 78.74 O
ANISOU 403 O LEU A 50 9797 8779 11344 139 -862 663 O
ATOM 404 CB LEU A 50 -224.342 33.462 51.688 1.00 56.40 C
ANISOU 404 CB LEU A 50 7095 6098 8235 -27 -889 654 C
ATOM 405 CG LEU A 50 -224.303 33.883 53.162 1.00 59.67 C
ANISOU 405 CG LEU A 50 7606 6547 8518 -138 -945 685 C
ATOM 406 CD1 LEU A 50 -225.620 34.503 53.579 1.00 59.58 C
ANISOU 406 CD1 LEU A 50 7655 6592 8390 -202 -826 604 C
ATOM 407 CD2 LEU A 50 -223.966 32.717 54.067 1.00 64.25 C
ANISOU 407 CD2 LEU A 50 8257 7083 9071 -200 -1063 798 C
ATOM 408 N GLY A 51 -223.093 33.296 48.746 1.00 58.19 N
ANISOU 408 N GLY A 51 7129 6255 8727 172 -806 589 N
ATOM 409 CA GLY A 51 -223.516 33.072 47.377 1.00 63.04 C
ANISOU 409 CA GLY A 51 7721 6861 9371 217 -716 528 C
ATOM 410 C GLY A 51 -222.576 32.223 46.558 1.00 59.08 C
ANISOU 410 C GLY A 51 7163 6285 8999 274 -697 524 C
ATOM 411 O GLY A 51 -223.027 31.495 45.667 1.00 69.96 O
ANISOU 411 O GLY A 51 8556 7635 10389 289 -635 480 O
ATOM 412 N PHE A 52 -221.262 32.301 46.824 1.00 55.35 N
ANISOU 412 N PHE A 52 6620 5773 8637 302 -743 561 N
ATOM 413 CA PHE A 52 -220.346 31.405 46.117 1.00 60.82 C
ANISOU 413 CA PHE A 52 7239 6375 9495 361 -707 547 C
ATOM 414 C PHE A 52 -220.541 29.946 46.508 1.00 54.82 C
ANISOU 414 C PHE A 52 6498 5529 8802 368 -754 588 C
ATOM 415 O PHE A 52 -220.722 29.111 45.605 1.00 71.32 O
ANISOU 415 O PHE A 52 8590 7562 10946 396 -669 529 O
ATOM 416 CB PHE A 52 -218.887 31.827 46.313 1.00 53.63 C
ANISOU 416 CB PHE A 52 6218 5432 8727 391 -747 578 C
ATOM 417 CG PHE A 52 -217.916 30.828 45.751 1.00 59.72 C
ANISOU 417 CG PHE A 52 6889 6090 9713 457 -706 564 C
ATOM 418 CD1 PHE A 52 -217.749 30.706 44.380 1.00 68.20 C
ANISOU 418 CD1 PHE A 52 7941 7142 10830 486 -543 462 C
ATOM 419 CD2 PHE A 52 -217.220 29.964 46.584 1.00 72.16 C
ANISOU 419 CD2 PHE A 52 8399 7571 11449 482 -827 651 C
ATOM 420 CE1 PHE A 52 -216.881 29.763 43.850 1.00 67.88 C
ANISOU 420 CE1 PHE A 52 7805 6984 11001 544 -472 425 C
ATOM 421 CE2 PHE A 52 -216.346 29.020 46.058 1.00 59.35 C
ANISOU 421 CE2 PHE A 52 6664 5821 10065 553 -780 631 C
ATOM 422 CZ PHE A 52 -216.181 28.920 44.692 1.00 68.73 C
ANISOU 422 CZ PHE A 52 7823 6985 11305 587 -588 507 C
ATOM 423 N PRO A 53 -220.495 29.555 47.792 1.00 55.76 N
ANISOU 423 N PRO A 53 6642 5626 8918 335 -885 688 N
ATOM 424 CA PRO A 53 -220.595 28.115 48.098 1.00 66.26 C
ANISOU 424 CA PRO A 53 7990 6852 10335 342 -935 741 C
ATOM 425 C PRO A 53 -221.905 27.503 47.636 1.00 71.10 C
ANISOU 425 C PRO A 53 8689 7474 10852 313 -856 686 C
ATOM 426 O PRO A 53 -221.898 26.464 46.966 1.00 76.20 O
ANISOU 426 O PRO A 53 9323 8027 11602 347 -805 650 O
ATOM 427 CB PRO A 53 -220.450 28.062 49.627 1.00 59.04 C
ANISOU 427 CB PRO A 53 7121 5938 9372 279 -1102 870 C
ATOM 428 CG PRO A 53 -219.909 29.357 50.030 1.00 60.24 C
ANISOU 428 CG PRO A 53 7249 6171 9469 257 -1143 876 C
ATOM 429 CD PRO A 53 -220.375 30.356 49.021 1.00 61.73 C
ANISOU 429 CD PRO A 53 7431 6443 9581 274 -997 758 C
ATOM 430 N ILE A 54 -223.033 28.136 47.966 1.00 69.31 N
ANISOU 430 N ILE A 54 8541 7349 10445 247 -839 672 N
ATOM 431 CA ILE A 54 -224.340 27.602 47.594 1.00 61.88 C
ANISOU 431 CA ILE A 54 7664 6421 9426 209 -778 626 C
ATOM 432 C ILE A 54 -224.415 27.367 46.090 1.00 63.33 C
ANISOU 432 C ILE A 54 7824 6582 9656 252 -673 524 C
ATOM 433 O ILE A 54 -224.784 26.281 45.631 1.00 75.38 O
ANISOU 433 O ILE A 54 9376 8038 11229 249 -643 495 O
ATOM 434 CB ILE A 54 -225.455 28.546 48.079 1.00 64.58 C
ANISOU 434 CB ILE A 54 8056 6876 9605 143 -759 611 C
ATOM 435 CG1 ILE A 54 -225.500 28.569 49.606 1.00 72.39 C
ANISOU 435 CG1 ILE A 54 9104 7880 10519 71 -840 699 C
ATOM 436 CG2 ILE A 54 -226.808 28.116 47.543 1.00 79.46 C
ANISOU 436 CG2 ILE A 54 9975 8777 11439 108 -695 557 C
ATOM 437 CD1 ILE A 54 -226.507 29.549 50.158 1.00 76.70 C
ANISOU 437 CD1 ILE A 54 9694 8526 10924 4 -792 664 C
ATOM 438 N ASN A 55 -224.047 28.371 45.299 1.00 61.80 N
ANISOU 438 N ASN A 55 7594 6443 9443 280 -617 467 N
ATOM 439 CA ASN A 55 -224.168 28.222 43.853 1.00 61.44 C
ANISOU 439 CA ASN A 55 7557 6389 9399 293 -517 371 C
ATOM 440 C ASN A 55 -223.105 27.293 43.288 1.00 59.73 C
ANISOU 440 C ASN A 55 7295 6056 9343 345 -462 335 C
ATOM 441 O ASN A 55 -223.362 26.588 42.308 1.00 70.07 O
ANISOU 441 O ASN A 55 8641 7320 10661 337 -381 252 O
ATOM 442 CB ASN A 55 -224.100 29.592 43.179 1.00 57.00 C
ANISOU 442 CB ASN A 55 6985 5914 8757 292 -475 335 C
ATOM 443 CG ASN A 55 -225.309 30.448 43.495 1.00 65.77 C
ANISOU 443 CG ASN A 55 8130 7117 9740 248 -510 349 C
ATOM 444 OD1 ASN A 55 -226.398 30.211 42.979 1.00 65.74 O
ANISOU 444 OD1 ASN A 55 8167 7134 9675 212 -500 317 O
ATOM 445 ND2 ASN A 55 -225.126 31.444 44.351 1.00 73.32 N
ANISOU 445 ND2 ASN A 55 9064 8122 10673 247 -551 392 N
ATOM 446 N PHE A 56 -221.903 27.293 43.868 1.00 65.36 N
ANISOU 446 N PHE A 56 7925 6715 10195 395 -503 388 N
ATOM 447 CA PHE A 56 -220.873 26.381 43.392 1.00 68.00 C
ANISOU 447 CA PHE A 56 8187 6917 10732 455 -444 351 C
ATOM 448 C PHE A 56 -221.196 24.946 43.793 1.00 70.27 C
ANISOU 448 C PHE A 56 8501 7087 11110 458 -488 381 C
ATOM 449 O PHE A 56 -221.064 24.024 42.980 1.00 71.25 O
ANISOU 449 O PHE A 56 8626 7110 11337 479 -391 297 O
ATOM 450 CB PHE A 56 -219.503 26.800 43.925 1.00 54.93 C
ANISOU 450 CB PHE A 56 6408 5228 9235 508 -495 409 C
ATOM 451 CG PHE A 56 -218.396 25.898 43.489 1.00 61.91 C
ANISOU 451 CG PHE A 56 7183 5962 10376 580 -430 371 C
ATOM 452 CD1 PHE A 56 -217.841 26.025 42.225 1.00 67.52 C
ANISOU 452 CD1 PHE A 56 7856 6653 11147 600 -250 244 C
ATOM 453 CD2 PHE A 56 -217.925 24.902 44.330 1.00 70.13 C
ANISOU 453 CD2 PHE A 56 8164 6873 11609 621 -543 463 C
ATOM 454 CE1 PHE A 56 -216.823 25.180 41.813 1.00 74.25 C
ANISOU 454 CE1 PHE A 56 8595 7353 12263 668 -159 188 C
ATOM 455 CE2 PHE A 56 -216.913 24.055 43.925 1.00 73.12 C
ANISOU 455 CE2 PHE A 56 8421 7091 12270 699 -479 424 C
ATOM 456 CZ PHE A 56 -216.359 24.194 42.666 1.00 75.83 C
ANISOU 456 CZ PHE A 56 8711 7412 12688 726 -275 276 C
ATOM 457 N LEU A 57 -221.634 24.747 45.040 1.00 60.74 N
ANISOU 457 N LEU A 57 7329 5888 9862 425 -623 498 N
ATOM 458 CA LEU A 57 -222.038 23.422 45.491 1.00 65.21 C
ANISOU 458 CA LEU A 57 7937 6343 10497 411 -674 546 C
ATOM 459 C LEU A 57 -223.164 22.859 44.633 1.00 68.53 C
ANISOU 459 C LEU A 57 8443 6765 10829 366 -580 447 C
ATOM 460 O LEU A 57 -223.261 21.640 44.460 1.00 76.56 O
ANISOU 460 O LEU A 57 9479 7654 11956 371 -563 431 O
ATOM 461 CB LEU A 57 -222.456 23.473 46.963 1.00 65.37 C
ANISOU 461 CB LEU A 57 8011 6398 10427 351 -823 687 C
ATOM 462 CG LEU A 57 -222.785 22.133 47.621 1.00 92.51 C
ANISOU 462 CG LEU A 57 11502 9715 13935 322 -899 772 C
ATOM 463 CD1 LEU A 57 -221.614 21.160 47.483 1.00 91.77 C
ANISOU 463 CD1 LEU A 57 11314 9435 14120 410 -931 802 C
ATOM 464 CD2 LEU A 57 -223.138 22.347 49.081 1.00100.89 C
ANISOU 464 CD2 LEU A 57 12637 10830 14866 238 -1034 912 C
ATOM 465 N THR A 58 -224.014 23.728 44.081 1.00 62.51 N
ANISOU 465 N THR A 58 7729 6137 9884 318 -529 384 N
ATOM 466 CA THR A 58 -225.037 23.272 43.146 1.00 72.22 C
ANISOU 466 CA THR A 58 9031 7374 11033 267 -457 289 C
ATOM 467 C THR A 58 -224.408 22.646 41.907 1.00 76.38 C
ANISOU 467 C THR A 58 9554 7806 11662 299 -336 168 C
ATOM 468 O THR A 58 -224.863 21.599 41.432 1.00 80.18 O
ANISOU 468 O THR A 58 10088 8202 12175 269 -295 106 O
ATOM 469 CB THR A 58 -225.949 24.438 42.755 1.00 64.76 C
ANISOU 469 CB THR A 58 8120 6584 9902 217 -448 260 C
ATOM 470 OG1 THR A 58 -226.794 24.783 43.861 1.00 61.63 O
ANISOU 470 OG1 THR A 58 7738 6256 9422 172 -527 343 O
ATOM 471 CG2 THR A 58 -226.808 24.078 41.550 1.00 60.13 C
ANISOU 471 CG2 THR A 58 7601 6007 9240 162 -388 157 C
ATOM 472 N LEU A 59 -223.363 23.274 41.366 1.00 79.34 N
ANISOU 472 N LEU A 59 9868 8189 12089 349 -265 124 N
ATOM 473 CA LEU A 59 -222.675 22.698 40.216 1.00 76.78 C
ANISOU 473 CA LEU A 59 9538 7769 11868 372 -117 -6 C
ATOM 474 C LEU A 59 -221.907 21.447 40.602 1.00 82.91 C
ANISOU 474 C LEU A 59 10246 8356 12901 438 -110 4 C
ATOM 475 O LEU A 59 -221.776 20.525 39.791 1.00 79.49 O
ANISOU 475 O LEU A 59 9838 7806 12558 438 7 -114 O
ATOM 476 CB LEU A 59 -221.726 23.726 39.603 1.00 63.44 C
ANISOU 476 CB LEU A 59 7793 6135 10177 399 -27 -52 C
ATOM 477 CG LEU A 59 -222.407 25.038 39.200 1.00 75.86 C
ANISOU 477 CG LEU A 59 9430 7878 11516 337 -43 -47 C
ATOM 478 CD1 LEU A 59 -221.403 26.053 38.661 1.00 61.25 C
ANISOU 478 CD1 LEU A 59 7527 6071 9673 357 44 -77 C
ATOM 479 CD2 LEU A 59 -223.524 24.771 38.189 1.00 67.91 C
ANISOU 479 CD2 LEU A 59 8554 6909 10339 248 -5 -133 C
ATOM 480 N TYR A 60 -221.397 21.396 41.830 1.00 75.07 N
ANISOU 480 N TYR A 60 9172 7322 12031 489 -242 143 N
ATOM 481 CA TYR A 60 -220.511 20.305 42.203 1.00 73.17 C
ANISOU 481 CA TYR A 60 8842 6886 12072 564 -259 175 C
ATOM 482 C TYR A 60 -221.287 19.006 42.391 1.00 87.73 C
ANISOU 482 C TYR A 60 10765 8614 13954 532 -290 184 C
ATOM 483 O TYR A 60 -220.884 17.952 41.884 1.00 82.72 O
ANISOU 483 O TYR A 60 10106 7806 13516 572 -202 104 O
ATOM 484 CB TYR A 60 -219.738 20.670 43.467 1.00 60.17 C
ANISOU 484 CB TYR A 60 7096 5232 10534 612 -425 341 C
ATOM 485 CG TYR A 60 -218.684 19.644 43.804 1.00 79.04 C
ANISOU 485 CG TYR A 60 9364 7411 13257 701 -464 389 C
ATOM 486 CD1 TYR A 60 -217.557 19.496 43.008 1.00 85.11 C
ANISOU 486 CD1 TYR A 60 10002 8072 14264 782 -325 282 C
ATOM 487 CD2 TYR A 60 -218.821 18.815 44.906 1.00 93.73 C
ANISOU 487 CD2 TYR A 60 11238 9168 15206 699 -637 542 C
ATOM 488 CE1 TYR A 60 -216.593 18.554 43.304 1.00 98.58 C
ANISOU 488 CE1 TYR A 60 11570 9565 16321 875 -360 324 C
ATOM 489 CE2 TYR A 60 -217.861 17.869 45.210 1.00101.80 C
ANISOU 489 CE2 TYR A 60 12141 9977 16560 785 -696 603 C
ATOM 490 CZ TYR A 60 -216.749 17.741 44.406 1.00104.24 C
ANISOU 490 CZ TYR A 60 12298 10174 17136 881 -560 492 C
ATOM 491 OH TYR A 60 -215.788 16.799 44.706 1.00120.15 O
ANISOU 491 OH TYR A 60 14167 11957 19527 978 -619 552 O
ATOM 492 N VAL A 61 -222.410 19.061 43.112 1.00 76.51 N
ANISOU 492 N VAL A 61 9437 7279 12355 455 -400 273 N
ATOM 493 CA VAL A 61 -223.182 17.854 43.362 1.00 73.20 C
ANISOU 493 CA VAL A 61 9093 6752 11967 410 -433 295 C
ATOM 494 C VAL A 61 -223.831 17.336 42.093 1.00 82.50 C
ANISOU 494 C VAL A 61 10350 7905 13089 361 -291 122 C
ATOM 495 O VAL A 61 -224.124 16.140 41.997 1.00 95.16 O
ANISOU 495 O VAL A 61 11997 9363 14798 344 -275 94 O
ATOM 496 CB VAL A 61 -224.238 18.094 44.453 1.00 69.36 C
ANISOU 496 CB VAL A 61 8682 6371 11300 325 -563 425 C
ATOM 497 CG1 VAL A 61 -223.562 18.593 45.719 1.00 78.77 C
ANISOU 497 CG1 VAL A 61 9822 7586 12520 351 -706 589 C
ATOM 498 CG2 VAL A 61 -225.299 19.066 43.965 1.00 73.31 C
ANISOU 498 CG2 VAL A 61 9243 7064 11550 251 -516 356 C
ATOM 499 N THR A 62 -224.061 18.200 41.106 1.00 80.36 N
ANISOU 499 N THR A 62 10112 7768 12653 329 -196 10 N
ATOM 500 CA THR A 62 -224.569 17.720 39.827 1.00 85.19 C
ANISOU 500 CA THR A 62 10813 8355 13198 267 -70 -158 C
ATOM 501 C THR A 62 -223.520 16.883 39.102 1.00 78.85 C
ANISOU 501 C THR A 62 9972 7369 12618 328 79 -285 C
ATOM 502 O THR A 62 -223.870 15.962 38.354 1.00 83.49 O
ANISOU 502 O THR A 62 10639 7855 13227 280 170 -411 O
ATOM 503 CB THR A 62 -225.035 18.909 38.982 1.00 68.54 C
ANISOU 503 CB THR A 62 8758 6434 10849 206 -30 -223 C
ATOM 504 OG1 THR A 62 -226.043 19.617 39.709 1.00 75.98 O
ANISOU 504 OG1 THR A 62 9717 7521 11633 159 -159 -112 O
ATOM 505 CG2 THR A 62 -225.630 18.457 37.659 1.00 70.83 C
ANISOU 505 CG2 THR A 62 9166 6714 11031 114 73 -385 C
ATOM 506 N VAL A 63 -222.236 17.164 39.337 1.00 76.49 N
ANISOU 506 N VAL A 63 9545 7015 12503 430 107 -258 N
ATOM 507 CA VAL A 63 -221.175 16.334 38.773 1.00 71.79 C
ANISOU 507 CA VAL A 63 8877 6221 12180 503 257 -375 C
ATOM 508 C VAL A 63 -221.128 14.970 39.456 1.00 78.40 C
ANISOU 508 C VAL A 63 9685 6840 13264 547 187 -312 C
ATOM 509 O VAL A 63 -220.821 13.956 38.814 1.00 74.01 O
ANISOU 509 O VAL A 63 9131 6098 12891 567 323 -447 O
ATOM 510 CB VAL A 63 -219.818 17.057 38.875 1.00 68.04 C
ANISOU 510 CB VAL A 63 8245 5746 11862 599 299 -354 C
ATOM 511 CG1 VAL A 63 -218.712 16.190 38.307 1.00 67.96 C
ANISOU 511 CG1 VAL A 63 8131 5516 12175 681 472 -484 C
ATOM 512 CG2 VAL A 63 -219.859 18.382 38.149 1.00 62.40 C
ANISOU 512 CG2 VAL A 63 7571 5231 10906 546 376 -415 C
ATOM 513 N GLN A 64 -221.444 14.911 40.752 1.00 83.10 N
ANISOU 513 N GLN A 64 10265 7447 13864 553 -18 -111 N
ATOM 514 CA GLN A 64 -221.288 13.691 41.536 1.00 88.32 C
ANISOU 514 CA GLN A 64 10895 7896 14768 595 -116 -9 C
ATOM 515 C GLN A 64 -222.543 12.826 41.602 1.00 88.40 C
ANISOU 515 C GLN A 64 11046 7868 14674 495 -149 -10 C
ATOM 516 O GLN A 64 -222.473 11.713 42.136 1.00 91.90 O
ANISOU 516 O GLN A 64 11483 8113 15321 517 -215 63 O
ATOM 517 CB GLN A 64 -220.850 14.032 42.968 1.00 91.01 C
ANISOU 517 CB GLN A 64 11155 8253 15171 638 -333 227 C
ATOM 518 CG GLN A 64 -219.381 14.403 43.112 1.00 95.66 C
ANISOU 518 CG GLN A 64 11564 8777 16005 757 -340 259 C
ATOM 519 CD GLN A 64 -218.912 14.357 44.556 1.00 96.73 C
ANISOU 519 CD GLN A 64 11632 8865 16256 790 -586 502 C
ATOM 520 OE1 GLN A 64 -219.696 14.085 45.468 1.00 96.86 O
ANISOU 520 OE1 GLN A 64 11754 8906 16142 715 -738 646 O
ATOM 521 NE2 GLN A 64 -217.629 14.618 44.770 1.00 90.90 N
ANISOU 521 NE2 GLN A 64 10721 8056 15762 890 -628 551 N
ATOM 522 N HIS A 65 -223.681 13.282 41.078 1.00 68.36 N
ANISOU 522 N HIS A 65 8627 5500 11845 383 -115 -84 N
ATOM 523 CA HIS A 65 -224.942 12.572 41.272 1.00 65.09 C
ANISOU 523 CA HIS A 65 8330 5072 11329 276 -169 -63 C
ATOM 524 C HIS A 65 -225.707 12.480 39.958 1.00 83.04 C
ANISOU 524 C HIS A 65 10712 7397 13444 181 -37 -263 C
ATOM 525 O HIS A 65 -226.297 13.467 39.508 1.00 76.60 O
ANISOU 525 O HIS A 65 9938 6784 12383 119 -32 -299 O
ATOM 526 CB HIS A 65 -225.766 13.250 42.361 1.00 58.61 C
ANISOU 526 CB HIS A 65 7536 4421 10310 214 -325 109 C
ATOM 527 CG HIS A 65 -225.091 13.243 43.700 1.00 72.63 C
ANISOU 527 CG HIS A 65 9243 6143 12209 274 -471 311 C
ATOM 528 ND1 HIS A 65 -225.395 12.328 44.685 1.00 70.76 N
ANISOU 528 ND1 HIS A 65 9047 5784 12054 239 -588 457 N
ATOM 529 CD2 HIS A 65 -224.109 14.027 44.206 1.00 78.16 C
ANISOU 529 CD2 HIS A 65 9847 6891 12960 354 -532 396 C
ATOM 530 CE1 HIS A 65 -224.641 12.558 45.746 1.00 74.71 C
ANISOU 530 CE1 HIS A 65 9488 6264 12634 290 -725 629 C
ATOM 531 NE2 HIS A 65 -223.851 13.583 45.480 1.00 73.63 N
ANISOU 531 NE2 HIS A 65 9263 6229 12486 361 -696 592 N
ATOM 532 N LYS A 66 -225.728 11.274 39.373 1.00 95.62 N
ANISOU 532 N LYS A 66 12354 8796 15180 162 55 -385 N
ATOM 533 CA LYS A 66 -226.300 11.082 38.042 1.00 88.94 C
ANISOU 533 CA LYS A 66 11625 7973 14195 61 186 -594 C
ATOM 534 C LYS A 66 -227.781 11.436 37.999 1.00 77.84 C
ANISOU 534 C LYS A 66 10315 6744 12518 -78 92 -567 C
ATOM 535 O LYS A 66 -228.283 11.873 36.957 1.00 82.88 O
ANISOU 535 O LYS A 66 11036 7499 12957 -167 148 -695 O
ATOM 536 CB LYS A 66 -226.090 9.636 37.581 1.00 93.01 C
ANISOU 536 CB LYS A 66 12182 8225 14932 58 294 -725 C
ATOM 537 CG LYS A 66 -226.549 9.372 36.148 1.00 94.19 C
ANISOU 537 CG LYS A 66 12470 8380 14938 -59 444 -966 C
ATOM 538 CD LYS A 66 -226.361 7.925 35.732 1.00102.40 C
ANISOU 538 CD LYS A 66 13559 9145 16204 -69 561 -1110 C
ATOM 539 CE LYS A 66 -226.637 7.753 34.241 1.00111.89 C
ANISOU 539 CE LYS A 66 14912 10356 17244 -194 733 -1373 C
ATOM 540 NZ LYS A 66 -225.812 8.699 33.421 1.00111.36 N
ANISOU 540 NZ LYS A 66 14833 10402 17078 -167 880 -1484 N
ATOM 541 N LYS A 67 -228.493 11.258 39.111 1.00 71.40 N
ANISOU 541 N LYS A 67 9487 5946 11694 -107 -52 -400 N
ATOM 542 CA LYS A 67 -229.926 11.530 39.125 1.00 79.27 C
ANISOU 542 CA LYS A 67 10547 7092 12479 -237 -131 -377 C
ATOM 543 C LYS A 67 -230.254 12.999 38.868 1.00 84.13 C
ANISOU 543 C LYS A 67 11143 7954 12870 -253 -162 -364 C
ATOM 544 O LYS A 67 -231.373 13.303 38.441 1.00 85.45 O
ANISOU 544 O LYS A 67 11357 8241 12869 -361 -203 -396 O
ATOM 545 CB LYS A 67 -230.523 11.090 40.463 1.00 85.39 C
ANISOU 545 CB LYS A 67 11307 7835 13303 -266 -252 -197 C
ATOM 546 CG LYS A 67 -230.423 9.593 40.732 1.00 87.42 C
ANISOU 546 CG LYS A 67 11600 7841 13774 -275 -245 -190 C
ATOM 547 CD LYS A 67 -231.326 8.807 39.807 1.00 78.80 C
ANISOU 547 CD LYS A 67 10606 6692 12642 -400 -192 -343 C
ATOM 548 CE LYS A 67 -231.378 7.342 40.212 1.00101.61 C
ANISOU 548 CE LYS A 67 13536 9330 15742 -424 -198 -316 C
ATOM 549 NZ LYS A 67 -232.409 6.587 39.443 1.00105.00 N
ANISOU 549 NZ LYS A 67 14064 9712 16119 -571 -167 -451 N
ATOM 550 N LEU A 68 -229.317 13.917 39.115 1.00 87.43 N
ANISOU 550 N LEU A 68 11485 8440 13296 -151 -152 -313 N
ATOM 551 CA LEU A 68 -229.622 15.334 38.950 1.00 79.31 C
ANISOU 551 CA LEU A 68 10435 7628 12072 -163 -187 -288 C
ATOM 552 C LEU A 68 -229.549 15.790 37.499 1.00 76.30 C
ANISOU 552 C LEU A 68 10119 7313 11560 -206 -98 -444 C
ATOM 553 O LEU A 68 -230.159 16.809 37.158 1.00 76.34 O
ANISOU 553 O LEU A 68 10135 7486 11383 -255 -148 -432 O
ATOM 554 CB LEU A 68 -228.680 16.190 39.800 1.00 68.74 C
ANISOU 554 CB LEU A 68 8998 6339 10782 -53 -219 -171 C
ATOM 555 CG LEU A 68 -228.739 15.960 41.314 1.00 67.42 C
ANISOU 555 CG LEU A 68 8787 6139 10691 -30 -329 4 C
ATOM 556 CD1 LEU A 68 -227.659 16.757 42.036 1.00 52.66 C
ANISOU 556 CD1 LEU A 68 6831 4304 8874 70 -365 102 C
ATOM 557 CD2 LEU A 68 -230.109 16.276 41.893 1.00 58.00 C
ANISOU 557 CD2 LEU A 68 7619 5070 9350 -127 -407 75 C
ATOM 558 N ARG A 69 -228.850 15.053 36.636 1.00 69.28 N
ANISOU 558 N ARG A 69 9280 6287 10756 -200 35 -591 N
ATOM 559 CA ARG A 69 -228.585 15.531 35.283 1.00 72.99 C
ANISOU 559 CA ARG A 69 9828 6818 11086 -249 143 -740 C
ATOM 560 C ARG A 69 -229.727 15.219 34.322 1.00 79.06 C
ANISOU 560 C ARG A 69 10734 7629 11676 -408 119 -843 C
ATOM 561 O ARG A 69 -229.514 14.650 33.247 1.00 93.26 O
ANISOU 561 O ARG A 69 12644 9351 13441 -477 239 -1014 O
ATOM 562 CB ARG A 69 -227.267 14.947 34.769 1.00 64.26 C
ANISOU 562 CB ARG A 69 8714 5550 10153 -180 327 -870 C
ATOM 563 CG ARG A 69 -226.065 15.362 35.606 1.00 67.17 C
ANISOU 563 CG ARG A 69 8930 5884 10708 -28 337 -769 C
ATOM 564 CD ARG A 69 -224.751 14.949 34.960 1.00 69.85 C
ANISOU 564 CD ARG A 69 9235 6075 11231 38 537 -912 C
ATOM 565 NE ARG A 69 -224.564 13.503 34.947 1.00 82.73 N
ANISOU 565 NE ARG A 69 10874 7470 13089 57 610 -996 N
ATOM 566 CZ ARG A 69 -224.046 12.810 35.956 1.00 87.25 C
ANISOU 566 CZ ARG A 69 11331 7879 13941 166 551 -890 C
ATOM 567 NH1 ARG A 69 -223.904 11.492 35.855 1.00 76.48 N
ANISOU 567 NH1 ARG A 69 9980 6283 12794 179 622 -973 N
ATOM 568 NH2 ARG A 69 -223.675 13.434 37.067 1.00 74.12 N
ANISOU 568 NH2 ARG A 69 9547 6277 12339 254 413 -698 N
ATOM 569 N THR A 70 -230.935 15.610 34.696 1.00 80.02 N
ANISOU 569 N THR A 70 10846 7872 11686 -473 -34 -744 N
ATOM 570 CA THR A 70 -232.118 15.526 33.857 1.00 87.53 C
ANISOU 570 CA THR A 70 11898 8891 12467 -628 -106 -809 C
ATOM 571 C THR A 70 -232.351 16.853 33.139 1.00 94.60 C
ANISOU 571 C THR A 70 12822 9971 13152 -671 -161 -793 C
ATOM 572 O THR A 70 -231.932 17.909 33.626 1.00 91.79 O
ANISOU 572 O THR A 70 12378 9707 12792 -579 -181 -693 O
ATOM 573 CB THR A 70 -233.346 15.171 34.698 1.00 76.31 C
ANISOU 573 CB THR A 70 10426 7486 11085 -677 -242 -705 C
ATOM 574 OG1 THR A 70 -233.577 16.200 35.666 1.00 85.59 O
ANISOU 574 OG1 THR A 70 11481 8787 12253 -609 -329 -547 O
ATOM 575 CG2 THR A 70 -233.107 13.870 35.426 1.00 81.38 C
ANISOU 575 CG2 THR A 70 11054 7939 11929 -644 -196 -701 C
ATOM 576 N PRO A 71 -233.002 16.827 31.968 1.00 88.07 N
ANISOU 576 N PRO A 71 12124 9192 12147 -817 -197 -888 N
ATOM 577 CA PRO A 71 -233.164 18.076 31.198 1.00 80.40 C
ANISOU 577 CA PRO A 71 11197 8379 10973 -868 -262 -861 C
ATOM 578 C PRO A 71 -233.931 19.159 31.938 1.00 83.83 C
ANISOU 578 C PRO A 71 11501 8949 11403 -826 -425 -690 C
ATOM 579 O PRO A 71 -233.578 20.342 31.835 1.00 90.01 O
ANISOU 579 O PRO A 71 12256 9831 12114 -779 -442 -626 O
ATOM 580 CB PRO A 71 -233.907 17.608 29.938 1.00 85.72 C
ANISOU 580 CB PRO A 71 12042 9060 11469 -1057 -310 -979 C
ATOM 581 CG PRO A 71 -233.517 16.166 29.795 1.00 72.12 C
ANISOU 581 CG PRO A 71 10393 7157 9851 -1082 -168 -1131 C
ATOM 582 CD PRO A 71 -233.452 15.649 31.206 1.00 74.69 C
ANISOU 582 CD PRO A 71 10562 7394 10424 -951 -169 -1033 C
ATOM 583 N LEU A 72 -234.964 18.786 32.695 1.00 75.92 N
ANISOU 583 N LEU A 72 10415 7944 10488 -844 -532 -619 N
ATOM 584 CA LEU A 72 -235.720 19.742 33.496 1.00 73.75 C
ANISOU 584 CA LEU A 72 10001 7780 10243 -802 -656 -474 C
ATOM 585 C LEU A 72 -234.857 20.451 34.534 1.00 84.94 C
ANISOU 585 C LEU A 72 11313 9213 11746 -649 -593 -385 C
ATOM 586 O LEU A 72 -235.299 21.449 35.118 1.00 80.12 O
ANISOU 586 O LEU A 72 10600 8697 11143 -608 -668 -281 O
ATOM 587 CB LEU A 72 -236.884 19.020 34.177 1.00 67.97 C
ANISOU 587 CB LEU A 72 9198 7017 9611 -857 -734 -437 C
ATOM 588 CG LEU A 72 -238.100 19.826 34.636 1.00 87.41 C
ANISOU 588 CG LEU A 72 11528 9587 12096 -876 -873 -329 C
ATOM 589 CD1 LEU A 72 -238.551 20.838 33.581 1.00 82.29 C
ANISOU 589 CD1 LEU A 72 10906 9047 11314 -937 -999 -316 C
ATOM 590 CD2 LEU A 72 -239.236 18.870 34.981 1.00 80.49 C
ANISOU 590 CD2 LEU A 72 10610 8662 11308 -972 -928 -333 C
ATOM 591 N ASN A 73 -233.642 19.965 34.772 1.00 70.10 N
ANISOU 591 N ASN A 73 9452 7238 9945 -569 -460 -426 N
ATOM 592 CA ASN A 73 -232.734 20.554 35.739 1.00 65.90 C
ANISOU 592 CA ASN A 73 8826 6713 9501 -436 -415 -343 C
ATOM 593 C ASN A 73 -231.666 21.427 35.099 1.00 64.74 C
ANISOU 593 C ASN A 73 8704 6608 9287 -388 -341 -373 C
ATOM 594 O ASN A 73 -230.945 22.118 35.825 1.00 61.70 O
ANISOU 594 O ASN A 73 8236 6247 8961 -288 -322 -300 O
ATOM 595 CB ASN A 73 -232.049 19.454 36.558 1.00 71.16 C
ANISOU 595 CB ASN A 73 9468 7232 10337 -371 -341 -343 C
ATOM 596 CG ASN A 73 -232.905 18.952 37.693 1.00 65.14 C
ANISOU 596 CG ASN A 73 8649 6449 9653 -388 -414 -252 C
ATOM 597 OD1 ASN A 73 -233.930 19.540 38.021 1.00 75.74 O
ANISOU 597 OD1 ASN A 73 9943 7894 10942 -430 -500 -190 O
ATOM 598 ND2 ASN A 73 -232.473 17.865 38.318 1.00 81.50 N
ANISOU 598 ND2 ASN A 73 10722 8380 11865 -358 -375 -241 N
ATOM 599 N TYR A 74 -231.526 21.386 33.770 1.00 55.17 N
ANISOU 599 N TYR A 74 7613 5401 7948 -470 -294 -480 N
ATOM 600 CA TYR A 74 -230.533 22.217 33.100 1.00 55.69 C
ANISOU 600 CA TYR A 74 7715 5508 7936 -447 -206 -510 C
ATOM 601 C TYR A 74 -230.705 23.691 33.460 1.00 73.79 C
ANISOU 601 C TYR A 74 9932 7928 10178 -403 -300 -386 C
ATOM 602 O TYR A 74 -229.721 24.393 33.726 1.00 78.06 O
ANISOU 602 O TYR A 74 10421 8483 10756 -321 -235 -355 O
ATOM 603 CB TYR A 74 -230.629 22.041 31.581 1.00 66.72 C
ANISOU 603 CB TYR A 74 9284 6915 9151 -583 -162 -634 C
ATOM 604 CG TYR A 74 -230.156 20.716 31.021 1.00 71.41 C
ANISOU 604 CG TYR A 74 9975 7371 9788 -628 -12 -798 C
ATOM 605 CD1 TYR A 74 -229.899 19.626 31.846 1.00 84.00 C
ANISOU 605 CD1 TYR A 74 11496 8827 11592 -552 40 -816 C
ATOM 606 CD2 TYR A 74 -229.955 20.562 29.653 1.00 75.55 C
ANISOU 606 CD2 TYR A 74 10673 7893 10139 -755 81 -938 C
ATOM 607 CE1 TYR A 74 -229.467 18.414 31.320 1.00 79.58 C
ANISOU 607 CE1 TYR A 74 11018 8118 11100 -587 183 -973 C
ATOM 608 CE2 TYR A 74 -229.521 19.358 29.119 1.00 83.26 C
ANISOU 608 CE2 TYR A 74 11744 8731 11161 -802 242 -1112 C
ATOM 609 CZ TYR A 74 -229.278 18.288 29.954 1.00 87.58 C
ANISOU 609 CZ TYR A 74 12199 9129 11948 -710 294 -1131 C
ATOM 610 OH TYR A 74 -228.849 17.091 29.415 1.00 95.55 O
ANISOU 610 OH TYR A 74 13295 9979 13029 -750 460 -1310 O
ATOM 611 N ILE A 75 -231.950 24.175 33.489 1.00 66.49 N
ANISOU 611 N ILE A 75 8988 7086 9189 -458 -454 -314 N
ATOM 612 CA ILE A 75 -232.182 25.599 33.718 1.00 70.69 C
ANISOU 612 CA ILE A 75 9452 7721 9686 -422 -541 -207 C
ATOM 613 C ILE A 75 -231.784 25.994 35.133 1.00 72.80 C
ANISOU 613 C ILE A 75 9583 7985 10092 -299 -522 -126 C
ATOM 614 O ILE A 75 -231.456 27.160 35.388 1.00 66.84 O
ANISOU 614 O ILE A 75 8777 7289 9330 -245 -537 -61 O
ATOM 615 CB ILE A 75 -233.651 25.968 33.416 1.00 63.92 C
ANISOU 615 CB ILE A 75 8583 6932 8772 -504 -713 -152 C
ATOM 616 CG1 ILE A 75 -233.789 27.477 33.201 1.00 66.91 C
ANISOU 616 CG1 ILE A 75 8928 7398 9096 -486 -799 -60 C
ATOM 617 CG2 ILE A 75 -234.573 25.505 34.535 1.00 49.71 C
ANISOU 617 CG2 ILE A 75 6665 5116 7106 -481 -768 -107 C
ATOM 618 CD1 ILE A 75 -233.026 27.995 31.992 1.00 61.58 C
ANISOU 618 CD1 ILE A 75 8389 6747 8260 -541 -758 -90 C
ATOM 619 N LEU A 76 -231.798 25.045 36.074 1.00 58.30 N
ANISOU 619 N LEU A 76 7699 6078 8376 -264 -496 -124 N
ATOM 620 CA LEU A 76 -231.361 25.344 37.433 1.00 63.14 C
ANISOU 620 CA LEU A 76 8211 6686 9095 -170 -485 -46 C
ATOM 621 C LEU A 76 -229.843 25.409 37.535 1.00 75.68 C
ANISOU 621 C LEU A 76 9790 8226 10740 -90 -387 -62 C
ATOM 622 O LEU A 76 -229.312 26.168 38.354 1.00 65.88 O
ANISOU 622 O LEU A 76 8477 7014 9541 -22 -394 7 O
ATOM 623 CB LEU A 76 -231.900 24.297 38.404 1.00 61.73 C
ANISOU 623 CB LEU A 76 8002 6443 9008 -179 -502 -22 C
ATOM 624 CG LEU A 76 -233.417 24.269 38.564 1.00 60.19 C
ANISOU 624 CG LEU A 76 7778 6296 8796 -254 -589 3 C
ATOM 625 CD1 LEU A 76 -233.833 23.081 39.413 1.00 63.66 C
ANISOU 625 CD1 LEU A 76 8210 6657 9322 -281 -581 17 C
ATOM 626 CD2 LEU A 76 -233.895 25.576 39.188 1.00 67.01 C
ANISOU 626 CD2 LEU A 76 8552 7255 9654 -223 -638 78 C
ATOM 627 N LEU A 77 -229.134 24.613 36.732 1.00 67.94 N
ANISOU 627 N LEU A 77 8874 7164 9776 -103 -289 -158 N
ATOM 628 CA LEU A 77 -227.691 24.785 36.637 1.00 67.74 C
ANISOU 628 CA LEU A 77 8821 7095 9823 -32 -182 -185 C
ATOM 629 C LEU A 77 -227.361 26.129 36.012 1.00 70.46 C
ANISOU 629 C LEU A 77 9178 7536 10058 -40 -169 -174 C
ATOM 630 O LEU A 77 -226.426 26.816 36.445 1.00 62.10 O
ANISOU 630 O LEU A 77 8048 6487 9061 28 -139 -134 O
ATOM 631 CB LEU A 77 -227.079 23.647 35.825 1.00 66.43 C
ANISOU 631 CB LEU A 77 8718 6811 9712 -52 -53 -313 C
ATOM 632 CG LEU A 77 -227.335 22.250 36.381 1.00 69.34 C
ANISOU 632 CG LEU A 77 9080 7056 10211 -44 -61 -326 C
ATOM 633 CD1 LEU A 77 -226.815 21.208 35.413 1.00 78.85 C
ANISOU 633 CD1 LEU A 77 10358 8136 11466 -73 81 -477 C
ATOM 634 CD2 LEU A 77 -226.660 22.116 37.731 1.00 70.11 C
ANISOU 634 CD2 LEU A 77 9062 7095 10483 59 -98 -223 C
ATOM 635 N ASN A 78 -228.127 26.515 34.987 1.00 70.04 N
ANISOU 635 N ASN A 78 9219 7550 9844 -133 -206 -200 N
ATOM 636 CA ASN A 78 -227.992 27.838 34.389 1.00 70.91 C
ANISOU 636 CA ASN A 78 9355 7750 9839 -155 -223 -164 C
ATOM 637 C ASN A 78 -228.182 28.932 35.428 1.00 69.27 C
ANISOU 637 C ASN A 78 9038 7601 9680 -87 -313 -49 C
ATOM 638 O ASN A 78 -227.406 29.893 35.477 1.00 64.80 O
ANISOU 638 O ASN A 78 8440 7063 9118 -48 -281 -17 O
ATOM 639 CB ASN A 78 -229.007 27.999 33.264 1.00 75.36 C
ANISOU 639 CB ASN A 78 10036 8368 10228 -276 -303 -180 C
ATOM 640 CG ASN A 78 -228.699 29.172 32.378 1.00 70.79 C
ANISOU 640 CG ASN A 78 9525 7857 9514 -323 -302 -154 C
ATOM 641 OD1 ASN A 78 -227.571 29.321 31.919 1.00 74.80 O
ANISOU 641 OD1 ASN A 78 10069 8346 10006 -321 -163 -206 O
ATOM 642 ND2 ASN A 78 -229.693 30.031 32.147 1.00 64.19 N
ANISOU 642 ND2 ASN A 78 8699 7092 8597 -366 -457 -66 N
ATOM 643 N LEU A 79 -229.212 28.802 36.267 1.00 63.17 N
ANISOU 643 N LEU A 79 8210 6844 8947 -79 -414 6 N
ATOM 644 CA LEU A 79 -229.393 29.733 37.375 1.00 60.57 C
ANISOU 644 CA LEU A 79 7784 6559 8673 -20 -472 93 C
ATOM 645 C LEU A 79 -228.149 29.806 38.246 1.00 59.11 C
ANISOU 645 C LEU A 79 7537 6338 8584 60 -409 111 C
ATOM 646 O LEU A 79 -227.734 30.897 38.651 1.00 71.13 O
ANISOU 646 O LEU A 79 9012 7899 10114 97 -420 158 O
ATOM 647 CB LEU A 79 -230.597 29.313 38.215 1.00 49.86 C
ANISOU 647 CB LEU A 79 6380 5207 7360 -34 -545 125 C
ATOM 648 CG LEU A 79 -230.844 30.113 39.492 1.00 63.67 C
ANISOU 648 CG LEU A 79 8038 6989 9163 12 -576 193 C
ATOM 649 CD1 LEU A 79 -231.225 31.585 39.174 1.00 40.29 C
ANISOU 649 CD1 LEU A 79 5048 4092 6170 18 -627 231 C
ATOM 650 CD2 LEU A 79 -231.911 29.418 40.341 1.00 49.60 C
ANISOU 650 CD2 LEU A 79 6220 5197 7427 -18 -605 206 C
ATOM 651 N ALA A 80 -227.553 28.652 38.559 1.00 63.50 N
ANISOU 651 N ALA A 80 8088 6811 9228 84 -356 78 N
ATOM 652 CA ALA A 80 -226.376 28.635 39.420 1.00 53.05 C
ANISOU 652 CA ALA A 80 6694 5443 8021 157 -328 110 C
ATOM 653 C ALA A 80 -225.228 29.395 38.779 1.00 62.72 C
ANISOU 653 C ALA A 80 7904 6678 9251 180 -252 86 C
ATOM 654 O ALA A 80 -224.531 30.162 39.452 1.00 63.76 O
ANISOU 654 O ALA A 80 7967 6827 9432 224 -268 137 O
ATOM 655 CB ALA A 80 -225.966 27.197 39.723 1.00 49.92 C
ANISOU 655 CB ALA A 80 6291 4934 7743 178 -297 86 C
ATOM 656 N VAL A 81 -225.030 29.205 37.473 1.00 57.18 N
ANISOU 656 N VAL A 81 7272 5964 8488 137 -163 3 N
ATOM 657 CA VAL A 81 -223.975 29.916 36.768 1.00 64.26 C
ANISOU 657 CA VAL A 81 8167 6872 9378 139 -65 -28 C
ATOM 658 C VAL A 81 -224.261 31.415 36.742 1.00 73.63 C
ANISOU 658 C VAL A 81 9356 8152 10468 123 -129 41 C
ATOM 659 O VAL A 81 -223.366 32.233 36.990 1.00 67.54 O
ANISOU 659 O VAL A 81 8525 7391 9747 156 -101 69 O
ATOM 660 CB VAL A 81 -223.807 29.330 35.355 1.00 61.59 C
ANISOU 660 CB VAL A 81 7934 6503 8966 69 61 -143 C
ATOM 661 CG1 VAL A 81 -222.889 30.214 34.524 1.00 72.38 C
ANISOU 661 CG1 VAL A 81 9320 7897 10282 42 172 -171 C
ATOM 662 CG2 VAL A 81 -223.244 27.913 35.442 1.00 58.83 C
ANISOU 662 CG2 VAL A 81 7556 6030 8766 104 153 -224 C
ATOM 663 N ALA A 82 -225.512 31.796 36.466 1.00 71.85 N
ANISOU 663 N ALA A 82 9188 7985 10126 72 -223 72 N
ATOM 664 CA ALA A 82 -225.876 33.211 36.433 1.00 64.49 C
ANISOU 664 CA ALA A 82 8253 7121 9132 63 -293 142 C
ATOM 665 C ALA A 82 -225.560 33.884 37.758 1.00 62.71 C
ANISOU 665 C ALA A 82 7922 6901 9004 132 -333 202 C
ATOM 666 O ALA A 82 -224.967 34.971 37.792 1.00 64.17 O
ANISOU 666 O ALA A 82 8081 7105 9194 145 -323 234 O
ATOM 667 CB ALA A 82 -227.359 33.369 36.100 1.00 57.24 C
ANISOU 667 CB ALA A 82 7378 6242 8128 11 -409 173 C
ATOM 668 N ASP A 83 -225.943 33.242 38.866 1.00 50.21 N
ANISOU 668 N ASP A 83 6290 5299 7488 164 -377 218 N
ATOM 669 CA ASP A 83 -225.628 33.784 40.182 1.00 55.42 C
ANISOU 669 CA ASP A 83 6876 5965 8216 209 -414 268 C
ATOM 670 C ASP A 83 -224.123 33.927 40.390 1.00 69.04 C
ANISOU 670 C ASP A 83 8551 7659 10024 246 -363 268 C
ATOM 671 O ASP A 83 -223.682 34.836 41.103 1.00 74.72 O
ANISOU 671 O ASP A 83 9223 8396 10770 263 -392 306 O
ATOM 672 CB ASP A 83 -226.228 32.903 41.281 1.00 55.31 C
ANISOU 672 CB ASP A 83 6845 5932 8238 213 -459 285 C
ATOM 673 CG ASP A 83 -227.762 32.897 41.275 1.00 68.23 C
ANISOU 673 CG ASP A 83 8500 7601 9822 174 -507 287 C
ATOM 674 OD1 ASP A 83 -228.394 33.765 40.626 1.00 60.05 O
ANISOU 674 OD1 ASP A 83 7472 6604 8740 156 -533 292 O
ATOM 675 OD2 ASP A 83 -228.339 32.013 41.940 1.00 64.72 O
ANISOU 675 OD2 ASP A 83 8055 7137 9398 159 -524 292 O
ATOM 676 N LEU A 84 -223.321 33.045 39.782 1.00 57.77 N
ANISOU 676 N LEU A 84 7123 6175 8653 255 -282 218 N
ATOM 677 CA LEU A 84 -221.875 33.172 39.895 1.00 61.46 C
ANISOU 677 CA LEU A 84 7513 6603 9236 291 -226 214 C
ATOM 678 C LEU A 84 -221.349 34.372 39.110 1.00 66.64 C
ANISOU 678 C LEU A 84 8177 7298 9845 266 -166 207 C
ATOM 679 O LEU A 84 -220.388 35.016 39.545 1.00 55.63 O
ANISOU 679 O LEU A 84 6705 5898 8533 288 -162 232 O
ATOM 680 CB LEU A 84 -221.210 31.869 39.447 1.00 55.61 C
ANISOU 680 CB LEU A 84 6754 5773 8603 313 -137 151 C
ATOM 681 CG LEU A 84 -221.355 30.750 40.491 1.00 58.39 C
ANISOU 681 CG LEU A 84 7071 6060 9054 349 -213 187 C
ATOM 682 CD1 LEU A 84 -220.680 29.463 40.040 1.00 59.52 C
ANISOU 682 CD1 LEU A 84 7185 6090 9342 380 -125 122 C
ATOM 683 CD2 LEU A 84 -220.780 31.212 41.826 1.00 52.79 C
ANISOU 683 CD2 LEU A 84 6281 5355 8423 381 -317 276 C
ATOM 684 N PHE A 85 -221.968 34.698 37.970 1.00 64.34 N
ANISOU 684 N PHE A 85 7983 7043 9421 209 -131 181 N
ATOM 685 CA PHE A 85 -221.663 35.955 37.292 1.00 63.67 C
ANISOU 685 CA PHE A 85 7926 6997 9269 171 -100 200 C
ATOM 686 C PHE A 85 -221.981 37.150 38.182 1.00 68.66 C
ANISOU 686 C PHE A 85 8517 7663 9906 191 -203 274 C
ATOM 687 O PHE A 85 -221.254 38.147 38.172 1.00 71.01 O
ANISOU 687 O PHE A 85 8785 7966 10230 185 -180 298 O
ATOM 688 CB PHE A 85 -222.443 36.059 35.982 1.00 65.54 C
ANISOU 688 CB PHE A 85 8294 7265 9342 92 -86 183 C
ATOM 689 CG PHE A 85 -221.812 35.327 34.834 1.00 70.46 C
ANISOU 689 CG PHE A 85 8985 7860 9926 40 62 94 C
ATOM 690 CD1 PHE A 85 -221.761 33.944 34.819 1.00 75.68 C
ANISOU 690 CD1 PHE A 85 9645 8468 10644 56 119 17 C
ATOM 691 CD2 PHE A 85 -221.286 36.024 33.758 1.00 77.58 C
ANISOU 691 CD2 PHE A 85 9963 8782 10733 -35 157 82 C
ATOM 692 CE1 PHE A 85 -221.182 33.264 33.758 1.00 73.29 C
ANISOU 692 CE1 PHE A 85 9407 8126 10314 3 280 -88 C
ATOM 693 CE2 PHE A 85 -220.707 35.353 32.697 1.00 76.45 C
ANISOU 693 CE2 PHE A 85 9895 8612 10542 -100 323 -19 C
ATOM 694 CZ PHE A 85 -220.657 33.970 32.696 1.00 67.51 C
ANISOU 694 CZ PHE A 85 8755 7422 9475 -78 391 -113 C
ATOM 695 N MET A 86 -223.075 37.080 38.948 1.00 65.81 N
ANISOU 695 N MET A 86 8157 7320 9528 206 -303 303 N
ATOM 696 CA MET A 86 -223.378 38.166 39.875 1.00 62.71 C
ANISOU 696 CA MET A 86 7727 6948 9154 222 -375 351 C
ATOM 697 C MET A 86 -222.343 38.232 40.991 1.00 60.99 C
ANISOU 697 C MET A 86 7430 6710 9033 253 -381 360 C
ATOM 698 O MET A 86 -221.908 39.322 41.384 1.00 70.88 O
ANISOU 698 O MET A 86 8654 7969 10309 250 -397 383 O
ATOM 699 CB MET A 86 -224.790 38.001 40.460 1.00 45.60 C
ANISOU 699 CB MET A 86 5568 4797 6960 224 -451 362 C
ATOM 700 CG MET A 86 -225.919 38.194 39.465 1.00 67.31 C
ANISOU 700 CG MET A 86 8373 7565 9636 191 -487 372 C
ATOM 701 SD MET A 86 -227.554 37.690 40.075 1.00 68.35 S
ANISOU 701 SD MET A 86 8485 7707 9777 191 -558 372 S
ATOM 702 CE MET A 86 -227.754 38.714 41.534 1.00 59.84 C
ANISOU 702 CE MET A 86 7339 6630 8768 221 -572 384 C
ATOM 703 N VAL A 87 -221.938 37.071 41.511 1.00 55.75 N
ANISOU 703 N VAL A 87 6733 6016 8434 276 -382 349 N
ATOM 704 CA VAL A 87 -220.996 37.023 42.627 1.00 63.59 C
ANISOU 704 CA VAL A 87 7654 6986 9523 297 -426 377 C
ATOM 705 C VAL A 87 -219.630 37.578 42.225 1.00 69.80 C
ANISOU 705 C VAL A 87 8371 7752 10396 300 -372 373 C
ATOM 706 O VAL A 87 -218.989 38.296 43.001 1.00 56.41 O
ANISOU 706 O VAL A 87 6624 6059 8749 295 -424 403 O
ATOM 707 CB VAL A 87 -220.887 35.580 43.160 1.00 56.41 C
ANISOU 707 CB VAL A 87 6726 6030 8679 320 -454 384 C
ATOM 708 CG1 VAL A 87 -219.602 35.395 43.954 1.00 50.75 C
ANISOU 708 CG1 VAL A 87 5918 5268 8095 342 -503 422 C
ATOM 709 CG2 VAL A 87 -222.102 35.235 44.024 1.00 57.74 C
ANISOU 709 CG2 VAL A 87 6948 6220 8769 300 -522 406 C
ATOM 710 N PHE A 88 -219.159 37.259 41.019 1.00 62.19 N
ANISOU 710 N PHE A 88 7410 6768 9452 298 -261 329 N
ATOM 711 CA PHE A 88 -217.806 37.619 40.608 1.00 66.07 C
ANISOU 711 CA PHE A 88 7820 7232 10050 296 -180 314 C
ATOM 712 C PHE A 88 -217.762 38.848 39.715 1.00 72.35 C
ANISOU 712 C PHE A 88 8664 8062 10763 246 -115 312 C
ATOM 713 O PHE A 88 -216.877 39.694 39.873 1.00 82.97 O
ANISOU 713 O PHE A 88 9944 9402 12177 232 -102 329 O
ATOM 714 CB PHE A 88 -217.134 36.446 39.884 1.00 57.89 C
ANISOU 714 CB PHE A 88 6744 6135 9116 318 -64 251 C
ATOM 715 CG PHE A 88 -216.821 35.281 40.772 1.00 66.85 C
ANISOU 715 CG PHE A 88 7800 7205 10394 374 -130 268 C
ATOM 716 CD1 PHE A 88 -215.724 35.313 41.621 1.00 77.48 C
ANISOU 716 CD1 PHE A 88 9012 8510 11916 405 -194 311 C
ATOM 717 CD2 PHE A 88 -217.608 34.140 40.746 1.00 69.28 C
ANISOU 717 CD2 PHE A 88 8167 7487 10670 388 -142 249 C
ATOM 718 CE1 PHE A 88 -215.424 34.231 42.438 1.00 71.58 C
ANISOU 718 CE1 PHE A 88 8197 7692 11309 452 -282 348 C
ATOM 719 CE2 PHE A 88 -217.315 33.058 41.559 1.00 61.75 C
ANISOU 719 CE2 PHE A 88 7149 6459 9854 435 -212 279 C
ATOM 720 CZ PHE A 88 -216.223 33.104 42.406 1.00 65.33 C
ANISOU 720 CZ PHE A 88 7473 6868 10481 468 -287 335 C
ATOM 721 N GLY A 89 -218.687 38.959 38.764 1.00 71.65 N
ANISOU 721 N GLY A 89 8690 8002 10530 209 -86 300 N
ATOM 722 CA GLY A 89 -218.756 40.164 37.961 1.00 66.24 C
ANISOU 722 CA GLY A 89 8069 7343 9757 153 -55 324 C
ATOM 723 C GLY A 89 -219.196 41.373 38.756 1.00 72.15 C
ANISOU 723 C GLY A 89 8809 8106 10497 158 -163 382 C
ATOM 724 O GLY A 89 -218.739 42.488 38.495 1.00 81.62 O
ANISOU 724 O GLY A 89 10009 9302 11700 124 -142 410 O
ATOM 725 N GLY A 90 -220.064 41.172 39.745 1.00 73.65 N
ANISOU 725 N GLY A 90 8993 8306 10683 194 -265 395 N
ATOM 726 CA GLY A 90 -220.638 42.280 40.480 1.00 50.52 C
ANISOU 726 CA GLY A 90 6067 5383 7747 195 -345 428 C
ATOM 727 C GLY A 90 -220.163 42.418 41.912 1.00 64.14 C
ANISOU 727 C GLY A 90 7724 7100 9545 211 -401 427 C
ATOM 728 O GLY A 90 -219.520 43.417 42.256 1.00 71.87 O
ANISOU 728 O GLY A 90 8672 8066 10568 191 -410 438 O
ATOM 729 N PHE A 91 -220.466 41.426 42.758 1.00 57.80 N
ANISOU 729 N PHE A 91 6909 6303 8748 233 -445 418 N
ATOM 730 CA PHE A 91 -220.241 41.596 44.192 1.00 52.48 C
ANISOU 730 CA PHE A 91 6209 5630 8102 225 -519 426 C
ATOM 731 C PHE A 91 -218.751 41.703 44.516 1.00 56.73 C
ANISOU 731 C PHE A 91 6666 6146 8740 215 -534 440 C
ATOM 732 O PHE A 91 -218.361 42.438 45.431 1.00 54.88 O
ANISOU 732 O PHE A 91 6418 5912 8521 184 -594 448 O
ATOM 733 CB PHE A 91 -220.856 40.439 44.993 1.00 50.56 C
ANISOU 733 CB PHE A 91 5987 5394 7831 234 -565 428 C
ATOM 734 CG PHE A 91 -222.309 40.142 44.692 1.00 54.54 C
ANISOU 734 CG PHE A 91 6546 5915 8261 239 -549 412 C
ATOM 735 CD1 PHE A 91 -223.145 41.089 44.120 1.00 57.79 C
ANISOU 735 CD1 PHE A 91 6983 6335 8640 237 -530 403 C
ATOM 736 CD2 PHE A 91 -222.845 38.894 45.018 1.00 62.44 C
ANISOU 736 CD2 PHE A 91 7565 6915 9243 244 -565 413 C
ATOM 737 CE1 PHE A 91 -224.478 40.798 43.857 1.00 56.39 C
ANISOU 737 CE1 PHE A 91 6833 6168 8425 241 -533 393 C
ATOM 738 CE2 PHE A 91 -224.181 38.596 44.762 1.00 53.10 C
ANISOU 738 CE2 PHE A 91 6419 5748 8010 241 -554 397 C
ATOM 739 CZ PHE A 91 -224.997 39.547 44.177 1.00 59.35 C
ANISOU 739 CZ PHE A 91 7219 6551 8781 240 -541 386 C
ATOM 740 N THR A 92 -217.905 40.957 43.800 1.00 54.16 N
ANISOU 740 N THR A 92 6284 5798 8497 237 -479 437 N
ATOM 741 CA THR A 92 -216.481 40.934 44.125 1.00 49.65 C
ANISOU 741 CA THR A 92 5603 5196 8065 235 -497 453 C
ATOM 742 C THR A 92 -215.808 42.234 43.703 1.00 59.35 C
ANISOU 742 C THR A 92 6802 6424 9324 197 -452 450 C
ATOM 743 O THR A 92 -215.052 42.838 44.474 1.00 49.31 O
ANISOU 743 O THR A 92 5472 5144 8120 167 -522 468 O
ATOM 744 CB THR A 92 -215.809 39.731 43.462 1.00 51.40 C
ANISOU 744 CB THR A 92 5754 5376 8401 275 -427 436 C
ATOM 745 OG1 THR A 92 -216.229 38.540 44.128 1.00 73.43 O
ANISOU 745 OG1 THR A 92 8555 8148 11196 305 -499 454 O
ATOM 746 CG2 THR A 92 -214.293 39.825 43.569 1.00 54.87 C
ANISOU 746 CG2 THR A 92 6048 5774 9028 276 -422 446 C
ATOM 747 N THR A 93 -216.079 42.677 42.478 1.00 60.41 N
ANISOU 747 N THR A 93 6986 6565 9403 185 -345 432 N
ATOM 748 CA THR A 93 -215.646 43.994 42.040 1.00 67.91 C
ANISOU 748 CA THR A 93 7936 7508 10357 138 -304 441 C
ATOM 749 C THR A 93 -216.084 45.077 43.019 1.00 71.53 C
ANISOU 749 C THR A 93 8428 7969 10780 114 -400 455 C
ATOM 750 O THR A 93 -215.279 45.918 43.441 1.00 66.74 O
ANISOU 750 O THR A 93 7771 7345 10243 75 -425 462 O
ATOM 751 CB THR A 93 -216.209 44.274 40.653 1.00 69.01 C
ANISOU 751 CB THR A 93 8168 7656 10395 116 -206 439 C
ATOM 752 OG1 THR A 93 -215.784 43.239 39.760 1.00 65.85 O
ANISOU 752 OG1 THR A 93 7754 7252 10015 123 -96 404 O
ATOM 753 CG2 THR A 93 -215.700 45.604 40.157 1.00 95.56 C
ANISOU 753 CG2 THR A 93 11539 11002 13767 58 -162 463 C
ATOM 754 N THR A 94 -217.363 45.060 43.401 1.00 63.61 N
ANISOU 754 N THR A 94 7506 6983 9681 132 -447 451 N
ATOM 755 CA THR A 94 -217.909 46.124 44.238 1.00 58.72 C
ANISOU 755 CA THR A 94 6926 6354 9032 109 -504 442 C
ATOM 756 C THR A 94 -217.313 46.103 45.637 1.00 59.50 C
ANISOU 756 C THR A 94 6990 6455 9163 78 -591 432 C
ATOM 757 O THR A 94 -217.176 47.157 46.264 1.00 60.71 O
ANISOU 757 O THR A 94 7158 6588 9321 33 -622 414 O
ATOM 758 CB THR A 94 -219.432 46.001 44.305 1.00 49.11 C
ANISOU 758 CB THR A 94 5781 5147 7731 136 -514 429 C
ATOM 759 OG1 THR A 94 -219.980 46.296 43.016 1.00 60.14 O
ANISOU 759 OG1 THR A 94 7218 6535 9099 147 -467 453 O
ATOM 760 CG2 THR A 94 -220.023 46.944 45.351 1.00 42.63 C
ANISOU 760 CG2 THR A 94 4991 4306 6900 115 -550 397 C
ATOM 761 N LEU A 95 -216.962 44.921 46.147 1.00 52.51 N
ANISOU 761 N LEU A 95 6068 5586 8297 93 -640 445 N
ATOM 762 CA LEU A 95 -216.219 44.862 47.401 1.00 51.35 C
ANISOU 762 CA LEU A 95 5890 5439 8182 48 -751 458 C
ATOM 763 C LEU A 95 -214.912 45.635 47.286 1.00 65.30 C
ANISOU 763 C LEU A 95 7567 7180 10062 9 -763 469 C
ATOM 764 O LEU A 95 -214.491 46.317 48.227 1.00 63.90 O
ANISOU 764 O LEU A 95 7395 6998 9887 -56 -849 464 O
ATOM 765 CB LEU A 95 -215.944 43.405 47.778 1.00 46.05 C
ANISOU 765 CB LEU A 95 5181 4771 7546 76 -812 495 C
ATOM 766 CG LEU A 95 -215.083 43.104 49.012 1.00 52.51 C
ANISOU 766 CG LEU A 95 5960 5582 8408 28 -963 539 C
ATOM 767 CD1 LEU A 95 -215.644 43.769 50.242 1.00 55.07 C
ANISOU 767 CD1 LEU A 95 6397 5932 8594 -53 -1036 518 C
ATOM 768 CD2 LEU A 95 -214.954 41.603 49.261 1.00 55.65 C
ANISOU 768 CD2 LEU A 95 6327 5964 8854 66 -1026 591 C
ATOM 769 N TYR A 96 -214.269 45.557 46.125 1.00 54.96 N
ANISOU 769 N TYR A 96 6183 5854 8845 35 -669 477 N
ATOM 770 CA TYR A 96 -212.948 46.136 45.965 1.00 66.53 C
ANISOU 770 CA TYR A 96 7539 7292 10446 -4 -665 487 C
ATOM 771 C TYR A 96 -213.037 47.651 45.802 1.00 67.12 C
ANISOU 771 C TYR A 96 7662 7349 10490 -60 -633 471 C
ATOM 772 O TYR A 96 -212.388 48.400 46.540 1.00 56.97 O
ANISOU 772 O TYR A 96 6346 6048 9254 -123 -709 468 O
ATOM 773 CB TYR A 96 -212.256 45.472 44.777 1.00 53.09 C
ANISOU 773 CB TYR A 96 5744 5573 8854 33 -543 488 C
ATOM 774 CG TYR A 96 -210.858 45.963 44.532 1.00 68.33 C
ANISOU 774 CG TYR A 96 7535 7472 10955 -8 -510 494 C
ATOM 775 CD1 TYR A 96 -209.799 45.510 45.302 1.00 68.59 C
ANISOU 775 CD1 TYR A 96 7424 7483 11154 -13 -617 519 C
ATOM 776 CD2 TYR A 96 -210.592 46.873 43.522 1.00 64.96 C
ANISOU 776 CD2 TYR A 96 7116 7033 10531 -48 -379 481 C
ATOM 777 CE1 TYR A 96 -208.514 45.961 45.081 1.00 65.39 C
ANISOU 777 CE1 TYR A 96 6866 7044 10933 -53 -589 523 C
ATOM 778 CE2 TYR A 96 -209.312 47.322 43.290 1.00 66.80 C
ANISOU 778 CE2 TYR A 96 7215 7237 10930 -96 -333 483 C
ATOM 779 CZ TYR A 96 -208.277 46.865 44.073 1.00 53.84 C
ANISOU 779 CZ TYR A 96 5411 5575 9472 -96 -434 499 C
ATOM 780 OH TYR A 96 -206.997 47.309 43.850 1.00 71.29 O
ANISOU 780 OH TYR A 96 7462 7751 11874 -146 -390 500 O
ATOM 781 N THR A 97 -213.877 48.112 44.870 1.00 58.91 N
ANISOU 781 N THR A 97 6706 6305 9370 -42 -537 463 N
ATOM 782 CA THR A 97 -214.088 49.544 44.669 1.00 58.37 C
ANISOU 782 CA THR A 97 6692 6201 9284 -86 -513 459 C
ATOM 783 C THR A 97 -214.668 50.208 45.911 1.00 53.43 C
ANISOU 783 C THR A 97 6130 5562 8608 -115 -602 423 C
ATOM 784 O THR A 97 -214.264 51.319 46.273 1.00 65.83 O
ANISOU 784 O THR A 97 7703 7092 10218 -176 -622 406 O
ATOM 785 CB THR A 97 -215.016 49.760 43.485 1.00 50.37 C
ANISOU 785 CB THR A 97 5763 5180 8194 -58 -428 477 C
ATOM 786 OG1 THR A 97 -216.275 49.143 43.779 1.00 54.62 O
ANISOU 786 OG1 THR A 97 6367 5744 8642 -5 -461 463 O
ATOM 787 CG2 THR A 97 -214.431 49.115 42.232 1.00 51.98 C
ANISOU 787 CG2 THR A 97 5932 5399 8418 -55 -320 498 C
ATOM 788 N SER A 98 -215.626 49.547 46.570 1.00 54.69 N
ANISOU 788 N SER A 98 6348 5752 8680 -82 -641 401 N
ATOM 789 CA SER A 98 -216.192 50.076 47.811 1.00 67.36 C
ANISOU 789 CA SER A 98 8024 7348 10223 -122 -698 348 C
ATOM 790 C SER A 98 -215.115 50.562 48.776 1.00 55.03 C
ANISOU 790 C SER A 98 6433 5776 8701 -210 -787 334 C
ATOM 791 O SER A 98 -215.244 51.640 49.366 1.00 59.48 O
ANISOU 791 O SER A 98 7051 6300 9249 -270 -797 281 O
ATOM 792 CB SER A 98 -217.047 49.011 48.499 1.00 66.04 C
ANISOU 792 CB SER A 98 7905 7226 9961 -96 -728 335 C
ATOM 793 OG SER A 98 -217.848 49.591 49.512 1.00 94.60 O
ANISOU 793 OG SER A 98 11608 10830 13504 -138 -734 268 O
ATOM 794 N LEU A 99 -214.054 49.773 48.958 1.00 59.12 N
ANISOU 794 N LEU A 99 6860 6320 9282 -222 -860 378 N
ATOM 795 CA LEU A 99 -213.008 50.062 49.931 1.00 54.54 C
ANISOU 795 CA LEU A 99 6241 5736 8746 -313 -983 380 C
ATOM 796 C LEU A 99 -212.048 51.155 49.469 1.00 65.98 C
ANISOU 796 C LEU A 99 7617 7139 10315 -364 -960 379 C
ATOM 797 O LEU A 99 -211.203 51.590 50.265 1.00 55.49 O
ANISOU 797 O LEU A 99 6256 5799 9028 -454 -1068 374 O
ATOM 798 CB LEU A 99 -212.242 48.776 50.245 1.00 67.28 C
ANISOU 798 CB LEU A 99 7761 7379 10423 -297 -1087 443 C
ATOM 799 CG LEU A 99 -213.110 47.754 50.982 1.00 65.08 C
ANISOU 799 CG LEU A 99 7573 7139 10015 -279 -1140 451 C
ATOM 800 CD1 LEU A 99 -212.412 46.420 51.156 1.00 51.45 C
ANISOU 800 CD1 LEU A 99 5753 5420 8375 -249 -1240 528 C
ATOM 801 CD2 LEU A 99 -213.461 48.347 52.327 1.00 68.77 C
ANISOU 801 CD2 LEU A 99 8168 7617 10343 -385 -1226 405 C
ATOM 802 N HIS A 100 -212.142 51.578 48.203 1.00 49.62 N
ANISOU 802 N HIS A 100 5523 5039 8291 -321 -829 391 N
ATOM 803 CA HIS A 100 -211.547 52.821 47.731 1.00 58.36 C
ANISOU 803 CA HIS A 100 6603 6089 9481 -379 -781 387 C
ATOM 804 C HIS A 100 -212.513 53.996 47.790 1.00 63.67 C
ANISOU 804 C HIS A 100 7399 6706 10088 -393 -738 341 C
ATOM 805 O HIS A 100 -212.067 55.148 47.843 1.00 63.78 O
ANISOU 805 O HIS A 100 7415 6659 10162 -464 -735 323 O
ATOM 806 CB HIS A 100 -211.078 52.679 46.282 1.00 59.67 C
ANISOU 806 CB HIS A 100 6695 6249 9729 -346 -654 434 C
ATOM 807 CG HIS A 100 -210.022 51.640 46.084 1.00 73.40 C
ANISOU 807 CG HIS A 100 8287 8018 11585 -330 -659 464 C
ATOM 808 ND1 HIS A 100 -210.309 50.295 46.018 1.00 73.08 N
ANISOU 808 ND1 HIS A 100 8228 8018 11522 -253 -662 476 N
ATOM 809 CD2 HIS A 100 -208.680 51.748 45.939 1.00 59.75 C
ANISOU 809 CD2 HIS A 100 6408 6271 10024 -379 -657 481 C
ATOM 810 CE1 HIS A 100 -209.189 49.617 45.841 1.00 70.18 C
ANISOU 810 CE1 HIS A 100 7704 7648 11312 -247 -660 497 C
ATOM 811 NE2 HIS A 100 -208.186 50.475 45.792 1.00 71.67 N
ANISOU 811 NE2 HIS A 100 7803 7804 11623 -322 -656 500 N
ATOM 812 N GLY A 101 -213.819 53.735 47.749 1.00 57.55 N
ANISOU 812 N GLY A 101 6712 5939 9213 -327 -702 322 N
ATOM 813 CA GLY A 101 -214.802 54.795 47.751 1.00 47.09 C
ANISOU 813 CA GLY A 101 5480 4545 7868 -323 -656 280 C
ATOM 814 C GLY A 101 -215.136 55.350 46.391 1.00 56.29 C
ANISOU 814 C GLY A 101 6653 5659 9075 -283 -571 337 C
ATOM 815 O GLY A 101 -215.759 56.415 46.315 1.00 58.10 O
ANISOU 815 O GLY A 101 6940 5803 9335 -286 -546 318 O
ATOM 816 N TYR A 102 -214.743 54.666 45.316 1.00 50.11 N
ANISOU 816 N TYR A 102 5823 4918 8298 -254 -526 405 N
ATOM 817 CA TYR A 102 -215.077 55.079 43.955 1.00 49.63 C
ANISOU 817 CA TYR A 102 5797 4820 8238 -236 -453 472 C
ATOM 818 C TYR A 102 -214.683 53.951 43.013 1.00 55.84 C
ANISOU 818 C TYR A 102 6545 5677 8993 -212 -397 516 C
ATOM 819 O TYR A 102 -214.060 52.968 43.419 1.00 64.27 O
ANISOU 819 O TYR A 102 7540 6804 10077 -203 -412 495 O
ATOM 820 CB TYR A 102 -214.383 56.386 43.556 1.00 48.56 C
ANISOU 820 CB TYR A 102 5662 4601 8187 -312 -424 500 C
ATOM 821 CG TYR A 102 -212.875 56.285 43.377 1.00 46.98 C
ANISOU 821 CG TYR A 102 5364 4424 8061 -383 -394 514 C
ATOM 822 CD1 TYR A 102 -212.019 56.267 44.473 1.00 46.97 C
ANISOU 822 CD1 TYR A 102 5287 4436 8123 -432 -464 463 C
ATOM 823 CD2 TYR A 102 -212.309 56.235 42.103 1.00 50.07 C
ANISOU 823 CD2 TYR A 102 5740 4821 8465 -413 -294 578 C
ATOM 824 CE1 TYR A 102 -210.631 56.193 44.302 1.00 52.68 C
ANISOU 824 CE1 TYR A 102 5891 5172 8954 -496 -445 480 C
ATOM 825 CE2 TYR A 102 -210.938 56.166 41.924 1.00 50.57 C
ANISOU 825 CE2 TYR A 102 5693 4897 8625 -479 -243 581 C
ATOM 826 CZ TYR A 102 -210.100 56.146 43.023 1.00 57.98 C
ANISOU 826 CZ TYR A 102 6528 5843 9660 -514 -322 534 C
ATOM 827 OH TYR A 102 -208.735 56.072 42.828 1.00 64.52 O
ANISOU 827 OH TYR A 102 7219 6677 10620 -578 -278 541 O
ATOM 828 N PHE A 103 -215.033 54.119 41.739 1.00 57.27 N
ANISOU 828 N PHE A 103 6782 5843 9133 -210 -334 577 N
ATOM 829 CA PHE A 103 -214.879 53.046 40.755 1.00 51.73 C
ANISOU 829 CA PHE A 103 6078 5204 8372 -194 -263 602 C
ATOM 830 C PHE A 103 -213.486 53.120 40.147 1.00 52.06 C
ANISOU 830 C PHE A 103 6052 5248 8481 -265 -165 615 C
ATOM 831 O PHE A 103 -213.277 53.708 39.082 1.00 58.69 O
ANISOU 831 O PHE A 103 6946 6059 9295 -325 -86 668 O
ATOM 832 CB PHE A 103 -215.958 53.129 39.684 1.00 50.24 C
ANISOU 832 CB PHE A 103 6001 5006 8083 -178 -253 661 C
ATOM 833 CG PHE A 103 -216.050 51.897 38.847 1.00 55.13 C
ANISOU 833 CG PHE A 103 6640 5692 8614 -162 -194 663 C
ATOM 834 CD1 PHE A 103 -216.738 50.786 39.311 1.00 54.45 C
ANISOU 834 CD1 PHE A 103 6544 5655 8490 -92 -236 622 C
ATOM 835 CD2 PHE A 103 -215.423 51.829 37.616 1.00 56.68 C
ANISOU 835 CD2 PHE A 103 6874 5898 8763 -230 -83 696 C
ATOM 836 CE1 PHE A 103 -216.814 49.639 38.557 1.00 61.09 C
ANISOU 836 CE1 PHE A 103 7408 6547 9258 -82 -179 613 C
ATOM 837 CE2 PHE A 103 -215.491 50.679 36.858 1.00 66.38 C
ANISOU 837 CE2 PHE A 103 8132 7182 9907 -226 -13 676 C
ATOM 838 CZ PHE A 103 -216.192 49.583 37.328 1.00 71.12 C
ANISOU 838 CZ PHE A 103 8718 7823 10480 -148 -65 634 C
ATOM 839 N VAL A 104 -212.525 52.473 40.814 1.00 59.15 N
ANISOU 839 N VAL A 104 6827 6176 9472 -263 -170 572 N
ATOM 840 CA VAL A 104 -211.113 52.632 40.473 1.00 64.31 C
ANISOU 840 CA VAL A 104 7372 6820 10245 -330 -85 572 C
ATOM 841 C VAL A 104 -210.716 52.019 39.140 1.00 67.64 C
ANISOU 841 C VAL A 104 7795 7265 10641 -352 78 580 C
ATOM 842 O VAL A 104 -209.576 52.206 38.708 1.00 86.01 O
ANISOU 842 O VAL A 104 10032 9576 13070 -417 186 575 O
ATOM 843 CB VAL A 104 -210.229 52.018 41.569 1.00 72.36 C
ANISOU 843 CB VAL A 104 8240 7857 11396 -316 -161 532 C
ATOM 844 CG1 VAL A 104 -210.356 52.822 42.842 1.00 73.79 C
ANISOU 844 CG1 VAL A 104 8432 8011 11594 -341 -303 517 C
ATOM 845 CG2 VAL A 104 -210.629 50.557 41.799 1.00 57.07 C
ANISOU 845 CG2 VAL A 104 6286 5971 9428 -229 -188 511 C
ATOM 846 N PHE A 105 -211.609 51.295 38.478 1.00 62.80 N
ANISOU 846 N PHE A 105 7281 6685 9894 -309 107 584 N
ATOM 847 CA PHE A 105 -211.277 50.620 37.231 1.00 58.28 C
ANISOU 847 CA PHE A 105 6734 6137 9273 -342 271 572 C
ATOM 848 C PHE A 105 -211.507 51.483 35.999 1.00 68.97 C
ANISOU 848 C PHE A 105 8234 7472 10501 -437 354 635 C
ATOM 849 O PHE A 105 -211.292 51.007 34.880 1.00 65.37 O
ANISOU 849 O PHE A 105 7836 7037 9963 -491 502 623 O
ATOM 850 CB PHE A 105 -212.083 49.319 37.112 1.00 57.87 C
ANISOU 850 CB PHE A 105 6726 6129 9133 -266 257 539 C
ATOM 851 CG PHE A 105 -211.779 48.326 38.197 1.00 62.13 C
ANISOU 851 CG PHE A 105 7132 6681 9794 -184 186 490 C
ATOM 852 CD1 PHE A 105 -210.467 47.986 38.496 1.00 69.30 C
ANISOU 852 CD1 PHE A 105 7870 7572 10890 -189 239 457 C
ATOM 853 CD2 PHE A 105 -212.799 47.746 38.934 1.00 67.91 C
ANISOU 853 CD2 PHE A 105 7904 7435 10465 -109 60 487 C
ATOM 854 CE1 PHE A 105 -210.177 47.073 39.504 1.00 65.53 C
ANISOU 854 CE1 PHE A 105 7272 7094 10533 -119 145 434 C
ATOM 855 CE2 PHE A 105 -212.515 46.833 39.941 1.00 66.75 C
ANISOU 855 CE2 PHE A 105 7653 7294 10416 -48 -16 460 C
ATOM 856 CZ PHE A 105 -211.202 46.500 40.227 1.00 56.60 C
ANISOU 856 CZ PHE A 105 6206 5986 9313 -53 14 440 C
ATOM 857 N GLY A 106 -211.943 52.730 36.168 1.00 83.38 N
ANISOU 857 N GLY A 106 10128 9247 12306 -466 266 700 N
ATOM 858 CA GLY A 106 -212.118 53.626 35.049 1.00 70.08 C
ANISOU 858 CA GLY A 106 8584 7528 10516 -563 320 784 C
ATOM 859 C GLY A 106 -213.311 53.265 34.190 1.00 80.86 C
ANISOU 859 C GLY A 106 10114 8917 11693 -557 284 832 C
ATOM 860 O GLY A 106 -213.996 52.264 34.427 1.00 75.47 O
ANISOU 860 O GLY A 106 9429 8281 10966 -475 234 790 O
ATOM 861 N PRO A 107 -213.586 54.084 33.170 1.00 85.28 N
ANISOU 861 N PRO A 107 10823 9440 12138 -652 295 931 N
ATOM 862 CA PRO A 107 -214.778 53.844 32.334 1.00 78.05 C
ANISOU 862 CA PRO A 107 10072 8542 11043 -660 220 999 C
ATOM 863 C PRO A 107 -214.764 52.519 31.595 1.00 73.78 C
ANISOU 863 C PRO A 107 9581 8082 10370 -681 327 935 C
ATOM 864 O PRO A 107 -215.839 51.968 31.322 1.00 87.93 O
ANISOU 864 O PRO A 107 11458 9902 12050 -647 232 953 O
ATOM 865 CB PRO A 107 -214.765 55.031 31.359 1.00 79.86 C
ANISOU 865 CB PRO A 107 10449 8708 11186 -787 221 1130 C
ATOM 866 CG PRO A 107 -213.359 55.549 31.396 1.00 67.69 C
ANISOU 866 CG PRO A 107 8829 7144 9745 -870 376 1104 C
ATOM 867 CD PRO A 107 -212.901 55.334 32.805 1.00 66.40 C
ANISOU 867 CD PRO A 107 8462 6982 9785 -761 347 1002 C
ATOM 868 N THR A 108 -213.589 51.991 31.250 1.00 88.61 N
ANISOU 868 N THR A 108 11403 9991 12273 -739 528 856 N
ATOM 869 CA THR A 108 -213.530 50.686 30.597 1.00 78.66 C
ANISOU 869 CA THR A 108 10183 8793 10912 -754 653 770 C
ATOM 870 C THR A 108 -213.999 49.583 31.537 1.00 76.20 C
ANISOU 870 C THR A 108 9759 8509 10685 -609 568 689 C
ATOM 871 O THR A 108 -214.872 48.780 31.185 1.00 72.54 O
ANISOU 871 O THR A 108 9384 8080 10098 -589 522 675 O
ATOM 872 CB THR A 108 -212.113 50.406 30.102 1.00 83.24 C
ANISOU 872 CB THR A 108 10697 9380 11551 -840 909 688 C
ATOM 873 OG1 THR A 108 -211.791 51.324 29.052 1.00 94.94 O
ANISOU 873 OG1 THR A 108 12325 10843 12903 -1003 1007 766 O
ATOM 874 CG2 THR A 108 -212.004 48.988 29.575 1.00 90.56 C
ANISOU 874 CG2 THR A 108 11638 10352 12418 -838 1054 570 C
ATOM 875 N GLY A 109 -213.440 49.536 32.748 1.00 70.77 N
ANISOU 875 N GLY A 109 8884 7805 10201 -519 535 643 N
ATOM 876 CA GLY A 109 -213.936 48.606 33.743 1.00 69.50 C
ANISOU 876 CA GLY A 109 8633 7663 10110 -393 431 590 C
ATOM 877 C GLY A 109 -215.402 48.791 34.048 1.00 71.92 C
ANISOU 877 C GLY A 109 9025 7972 10329 -338 246 647 C
ATOM 878 O GLY A 109 -216.054 47.860 34.530 1.00 82.76 O
ANISOU 878 O GLY A 109 10374 9371 11699 -259 181 606 O
ATOM 879 N CYS A 110 -215.939 49.976 33.762 1.00 68.38 N
ANISOU 879 N CYS A 110 8668 7488 9826 -380 164 742 N
ATOM 880 CA CYS A 110 -217.346 50.248 34.016 1.00 62.42 C
ANISOU 880 CA CYS A 110 7970 6718 9028 -326 -8 798 C
ATOM 881 C CYS A 110 -218.232 49.492 33.038 1.00 60.37 C
ANISOU 881 C CYS A 110 7839 6499 8600 -354 -30 816 C
ATOM 882 O CYS A 110 -219.251 48.913 33.429 1.00 58.25 O
ANISOU 882 O CYS A 110 7561 6247 8325 -283 -134 803 O
ATOM 883 CB CYS A 110 -217.597 51.756 33.931 1.00 63.69 C
ANISOU 883 CB CYS A 110 8180 6805 9215 -361 -88 899 C
ATOM 884 SG CYS A 110 -219.231 52.283 34.450 1.00 67.36 S
ANISOU 884 SG CYS A 110 8660 7219 9715 -276 -290 957 S
ATOM 885 N ASN A 111 -217.869 49.509 31.751 1.00 48.45 N
ANISOU 885 N ASN A 111 6459 5004 6946 -474 69 846 N
ATOM 886 CA ASN A 111 -218.625 48.750 30.762 1.00 59.44 C
ANISOU 886 CA ASN A 111 7993 6437 8152 -527 51 853 C
ATOM 887 C ASN A 111 -218.485 47.249 30.999 1.00 71.27 C
ANISOU 887 C ASN A 111 9434 7984 9663 -476 135 725 C
ATOM 888 O ASN A 111 -219.451 46.497 30.835 1.00 70.00 O
ANISOU 888 O ASN A 111 9324 7849 9422 -456 52 715 O
ATOM 889 CB ASN A 111 -218.166 49.125 29.351 1.00 59.72 C
ANISOU 889 CB ASN A 111 8206 6480 8007 -694 155 906 C
ATOM 890 CG ASN A 111 -218.857 50.370 28.824 1.00 75.42 C
ANISOU 890 CG ASN A 111 10317 8419 9921 -758 -1 1070 C
ATOM 891 OD1 ASN A 111 -219.950 50.719 29.263 1.00 91.87 O
ANISOU 891 OD1 ASN A 111 12376 10469 12063 -680 -198 1139 O
ATOM 892 ND2 ASN A 111 -218.228 51.035 27.868 1.00 78.26 N
ANISOU 892 ND2 ASN A 111 10808 8765 10163 -904 91 1136 N
ATOM 893 N LEU A 112 -217.293 46.803 31.405 1.00 75.59 N
ANISOU 893 N LEU A 112 9860 8532 10329 -452 290 632 N
ATOM 894 CA LEU A 112 -217.069 45.390 31.690 1.00 72.75 C
ANISOU 894 CA LEU A 112 9427 8192 10021 -394 368 516 C
ATOM 895 C LEU A 112 -217.847 44.945 32.921 1.00 66.92 C
ANISOU 895 C LEU A 112 8590 7455 9384 -266 214 510 C
ATOM 896 O LEU A 112 -218.614 43.976 32.867 1.00 58.98 O
ANISOU 896 O LEU A 112 7618 6468 8322 -238 171 475 O
ATOM 897 CB LEU A 112 -215.576 45.135 31.884 1.00 68.81 C
ANISOU 897 CB LEU A 112 8795 7675 9675 -392 551 434 C
ATOM 898 CG LEU A 112 -214.781 44.699 30.659 1.00 71.70 C
ANISOU 898 CG LEU A 112 9237 8047 9959 -505 785 360 C
ATOM 899 CD1 LEU A 112 -213.321 45.077 30.829 1.00 74.25 C
ANISOU 899 CD1 LEU A 112 9415 8339 10458 -523 945 323 C
ATOM 900 CD2 LEU A 112 -214.933 43.195 30.467 1.00 65.36 C
ANISOU 900 CD2 LEU A 112 8436 7250 9147 -471 861 247 C
ATOM 901 N GLU A 113 -217.647 45.634 34.047 1.00 62.39 N
ANISOU 901 N GLU A 113 7899 6856 8950 -200 136 537 N
ATOM 902 CA GLU A 113 -218.329 45.243 35.273 1.00 55.51 C
ANISOU 902 CA GLU A 113 6946 5986 8158 -98 10 525 C
ATOM 903 C GLU A 113 -219.829 45.456 35.156 1.00 73.39 C
ANISOU 903 C GLU A 113 9294 8257 10333 -86 -128 579 C
ATOM 904 O GLU A 113 -220.604 44.768 35.828 1.00 72.13 O
ANISOU 904 O GLU A 113 9100 8110 10194 -23 -201 555 O
ATOM 905 CB GLU A 113 -217.758 46.020 36.458 1.00 49.06 C
ANISOU 905 CB GLU A 113 6014 5143 7486 -58 -35 535 C
ATOM 906 CG GLU A 113 -218.256 45.567 37.818 1.00 65.91 C
ANISOU 906 CG GLU A 113 8073 7281 9690 24 -139 511 C
ATOM 907 CD GLU A 113 -219.390 46.415 38.360 1.00 88.37 C
ANISOU 907 CD GLU A 113 10949 10111 12518 48 -258 551 C
ATOM 908 OE1 GLU A 113 -220.048 47.128 37.574 1.00 80.57 O
ANISOU 908 OE1 GLU A 113 10043 9107 11465 16 -287 607 O
ATOM 909 OE2 GLU A 113 -219.615 46.377 39.587 1.00105.88 O
ANISOU 909 OE2 GLU A 113 13109 12326 14795 92 -321 528 O
ATOM 910 N GLY A 114 -220.257 46.390 34.312 1.00 66.31 N
ANISOU 910 N GLY A 114 8500 7346 9349 -150 -170 660 N
ATOM 911 CA GLY A 114 -221.672 46.613 34.113 1.00 54.51 C
ANISOU 911 CA GLY A 114 7065 5846 7800 -140 -317 724 C
ATOM 912 C GLY A 114 -222.287 45.543 33.240 1.00 65.40 C
ANISOU 912 C GLY A 114 8540 7267 9043 -182 -322 704 C
ATOM 913 O GLY A 114 -223.394 45.069 33.507 1.00 63.40 O
ANISOU 913 O GLY A 114 8273 7022 8792 -140 -427 705 O
ATOM 914 N PHE A 115 -221.570 45.154 32.186 1.00 60.06 N
ANISOU 914 N PHE A 115 7961 6612 8246 -275 -198 677 N
ATOM 915 CA PHE A 115 -222.021 44.054 31.345 1.00 67.88 C
ANISOU 915 CA PHE A 115 9057 7640 9095 -331 -179 633 C
ATOM 916 C PHE A 115 -222.206 42.777 32.166 1.00 80.29 C
ANISOU 916 C PHE A 115 10532 9222 10753 -243 -164 537 C
ATOM 917 O PHE A 115 -223.312 42.225 32.239 1.00 65.20 O
ANISOU 917 O PHE A 115 8637 7324 8814 -225 -273 541 O
ATOM 918 CB PHE A 115 -221.030 43.834 30.198 1.00 58.82 C
ANISOU 918 CB PHE A 115 8024 6507 7817 -451 2 588 C
ATOM 919 CG PHE A 115 -221.438 42.742 29.250 1.00 76.68 C
ANISOU 919 CG PHE A 115 10423 8802 9912 -533 40 526 C
ATOM 920 CD1 PHE A 115 -222.352 42.991 28.239 1.00 76.39 C
ANISOU 920 CD1 PHE A 115 10561 8786 9680 -642 -83 607 C
ATOM 921 CD2 PHE A 115 -220.920 41.461 29.378 1.00 74.85 C
ANISOU 921 CD2 PHE A 115 10146 8569 9725 -505 185 389 C
ATOM 922 CE1 PHE A 115 -222.739 41.987 27.370 1.00 79.32 C
ANISOU 922 CE1 PHE A 115 11072 9187 9880 -735 -57 542 C
ATOM 923 CE2 PHE A 115 -221.304 40.450 28.511 1.00 69.40 C
ANISOU 923 CE2 PHE A 115 9589 7897 8882 -588 228 316 C
ATOM 924 CZ PHE A 115 -222.213 40.713 27.507 1.00 70.09 C
ANISOU 924 CZ PHE A 115 9863 8016 8753 -709 109 387 C
ATOM 925 N PHE A 116 -221.137 42.306 32.820 1.00 58.39 N
ANISOU 925 N PHE A 116 7649 6436 8102 -190 -41 460 N
ATOM 926 CA PHE A 116 -221.195 40.995 33.465 1.00 69.35 C
ANISOU 926 CA PHE A 116 8964 7820 9565 -122 -21 378 C
ATOM 927 C PHE A 116 -222.118 40.975 34.680 1.00 70.83 C
ANISOU 927 C PHE A 116 9067 8007 9838 -34 -165 409 C
ATOM 928 O PHE A 116 -222.780 39.958 34.923 1.00 69.33 O
ANISOU 928 O PHE A 116 8875 7822 9646 -9 -200 373 O
ATOM 929 CB PHE A 116 -219.786 40.526 33.829 1.00 56.14 C
ANISOU 929 CB PHE A 116 7185 6119 8026 -89 128 305 C
ATOM 930 CG PHE A 116 -219.008 40.064 32.641 1.00 62.84 C
ANISOU 930 CG PHE A 116 8109 6961 8806 -172 313 230 C
ATOM 931 CD1 PHE A 116 -219.344 38.876 32.006 1.00 59.86 C
ANISOU 931 CD1 PHE A 116 7812 6580 8351 -204 373 148 C
ATOM 932 CD2 PHE A 116 -217.978 40.833 32.124 1.00 56.56 C
ANISOU 932 CD2 PHE A 116 7314 6160 8016 -233 438 233 C
ATOM 933 CE1 PHE A 116 -218.652 38.446 30.884 1.00 66.65 C
ANISOU 933 CE1 PHE A 116 8758 7430 9137 -295 569 58 C
ATOM 934 CE2 PHE A 116 -217.281 40.414 31.005 1.00 65.71 C
ANISOU 934 CE2 PHE A 116 8551 7313 9104 -326 639 150 C
ATOM 935 CZ PHE A 116 -217.618 39.213 30.382 1.00 62.91 C
ANISOU 935 CZ PHE A 116 8283 6953 8666 -357 711 56 C
ATOM 936 N ALA A 117 -222.191 42.067 35.445 1.00 59.77 N
ANISOU 936 N ALA A 117 7604 6596 8510 3 -238 466 N
ATOM 937 CA ALA A 117 -223.161 42.116 36.536 1.00 65.97 C
ANISOU 937 CA ALA A 117 8327 7380 9361 69 -351 483 C
ATOM 938 C ALA A 117 -224.586 42.131 36.002 1.00 68.99 C
ANISOU 938 C ALA A 117 8770 7772 9670 47 -458 523 C
ATOM 939 O ALA A 117 -225.477 41.495 36.577 1.00 69.63 O
ANISOU 939 O ALA A 117 8815 7860 9781 82 -514 505 O
ATOM 940 CB ALA A 117 -222.919 43.333 37.423 1.00 51.70 C
ANISOU 940 CB ALA A 117 6452 5548 7644 100 -387 517 C
ATOM 941 N THR A 118 -224.820 42.852 34.906 1.00 62.15 N
ANISOU 941 N THR A 118 7996 6904 8716 -18 -495 586 N
ATOM 942 CA THR A 118 -226.168 42.930 34.356 1.00 71.75 C
ANISOU 942 CA THR A 118 9259 8122 9881 -44 -630 643 C
ATOM 943 C THR A 118 -226.552 41.630 33.669 1.00 71.47 C
ANISOU 943 C THR A 118 9298 8119 9738 -94 -623 595 C
ATOM 944 O THR A 118 -227.693 41.167 33.791 1.00 70.51 O
ANISOU 944 O THR A 118 9156 8003 9631 -85 -723 600 O
ATOM 945 CB THR A 118 -226.268 44.100 33.379 1.00 55.77 C
ANISOU 945 CB THR A 118 7322 6076 7791 -110 -699 746 C
ATOM 946 OG1 THR A 118 -226.021 45.321 34.084 1.00 66.56 O
ANISOU 946 OG1 THR A 118 8613 7395 9282 -59 -711 786 O
ATOM 947 CG2 THR A 118 -227.643 44.153 32.722 1.00 49.15 C
ANISOU 947 CG2 THR A 118 6529 5234 6912 -145 -869 822 C
ATOM 948 N LEU A 119 -225.612 41.038 32.931 1.00 73.68 N
ANISOU 948 N LEU A 119 9661 8413 9919 -155 -496 538 N
ATOM 949 CA LEU A 119 -225.862 39.756 32.289 1.00 71.30 C
ANISOU 949 CA LEU A 119 9441 8130 9519 -210 -464 468 C
ATOM 950 C LEU A 119 -226.225 38.694 33.320 1.00 79.94 C
ANISOU 950 C LEU A 119 10434 9216 10723 -130 -465 406 C
ATOM 951 O LEU A 119 -227.186 37.939 33.137 1.00 69.95 O
ANISOU 951 O LEU A 119 9196 7959 9423 -154 -537 391 O
ATOM 952 CB LEU A 119 -224.634 39.330 31.484 1.00 67.27 C
ANISOU 952 CB LEU A 119 9015 7620 8924 -277 -281 392 C
ATOM 953 CG LEU A 119 -224.791 38.102 30.585 1.00 71.18 C
ANISOU 953 CG LEU A 119 9630 8124 9291 -361 -219 302 C
ATOM 954 CD1 LEU A 119 -225.409 38.484 29.246 1.00 73.00 C
ANISOU 954 CD1 LEU A 119 10046 8386 9304 -504 -301 358 C
ATOM 955 CD2 LEU A 119 -223.454 37.402 30.390 1.00 67.36 C
ANISOU 955 CD2 LEU A 119 9143 7613 8839 -366 7 184 C
ATOM 956 N GLY A 120 -225.471 38.633 34.419 1.00 74.31 N
ANISOU 956 N GLY A 120 9608 8483 10142 -47 -397 377 N
ATOM 957 CA GLY A 120 -225.733 37.616 35.425 1.00 67.16 C
ANISOU 957 CA GLY A 120 8625 7564 9329 15 -400 332 C
ATOM 958 C GLY A 120 -227.144 37.691 35.975 1.00 69.99 C
ANISOU 958 C GLY A 120 8943 7934 9715 34 -529 371 C
ATOM 959 O GLY A 120 -227.865 36.689 36.015 1.00 66.63 O
ANISOU 959 O GLY A 120 8525 7507 9283 21 -557 340 O
ATOM 960 N GLY A 121 -227.561 38.887 36.397 1.00 57.07 N
ANISOU 960 N GLY A 121 7257 6300 8128 61 -600 434 N
ATOM 961 CA GLY A 121 -228.883 39.034 36.977 1.00 58.60 C
ANISOU 961 CA GLY A 121 7386 6493 8385 85 -698 460 C
ATOM 962 C GLY A 121 -229.984 38.863 35.955 1.00 59.12 C
ANISOU 962 C GLY A 121 7505 6570 8390 24 -804 493 C
ATOM 963 O GLY A 121 -231.088 38.429 36.290 1.00 62.90 O
ANISOU 963 O GLY A 121 7929 7048 8921 29 -869 490 O
ATOM 964 N GLU A 122 -229.694 39.179 34.696 1.00 63.95 N
ANISOU 964 N GLU A 122 8226 7190 8884 -46 -825 526 N
ATOM 965 CA GLU A 122 -230.665 39.003 33.631 1.00 56.77 C
ANISOU 965 CA GLU A 122 7391 6293 7887 -126 -951 566 C
ATOM 966 C GLU A 122 -230.809 37.534 33.217 1.00 75.32 C
ANISOU 966 C GLU A 122 9809 8658 10152 -184 -918 486 C
ATOM 967 O GLU A 122 -231.916 37.110 32.862 1.00 71.25 O
ANISOU 967 O GLU A 122 9299 8150 9623 -231 -1035 502 O
ATOM 968 CB GLU A 122 -230.275 39.888 32.446 1.00 64.30 C
ANISOU 968 CB GLU A 122 8466 7249 8717 -203 -990 639 C
ATOM 969 CG GLU A 122 -231.453 40.421 31.635 1.00 83.30 C
ANISOU 969 CG GLU A 122 10906 9650 11094 -264 -1193 745 C
ATOM 970 CD GLU A 122 -232.283 41.452 32.380 1.00 70.70 C
ANISOU 970 CD GLU A 122 9158 8010 9696 -177 -1303 822 C
ATOM 971 OE1 GLU A 122 -231.905 41.856 33.495 1.00 79.19 O
ANISOU 971 OE1 GLU A 122 10125 9062 10900 -82 -1210 787 O
ATOM 972 OE2 GLU A 122 -233.324 41.865 31.841 1.00 88.76 O
ANISOU 972 OE2 GLU A 122 11433 10277 12016 -209 -1485 914 O
ATOM 973 N ILE A 123 -229.728 36.741 33.270 1.00 73.64 N
ANISOU 973 N ILE A 123 9636 8439 9904 -181 -763 399 N
ATOM 974 CA ILE A 123 -229.851 35.301 33.039 1.00 52.69 C
ANISOU 974 CA ILE A 123 7033 5778 7209 -221 -717 311 C
ATOM 975 C ILE A 123 -230.631 34.648 34.176 1.00 66.11 C
ANISOU 975 C ILE A 123 8616 7463 9039 -161 -754 299 C
ATOM 976 O ILE A 123 -231.494 33.790 33.942 1.00 60.76 O
ANISOU 976 O ILE A 123 7958 6783 8343 -211 -811 273 O
ATOM 977 CB ILE A 123 -228.470 34.636 32.860 1.00 58.76 C
ANISOU 977 CB ILE A 123 7850 6520 7955 -220 -534 219 C
ATOM 978 CG1 ILE A 123 -227.751 35.143 31.614 1.00 51.54 C
ANISOU 978 CG1 ILE A 123 7070 5623 6891 -308 -467 213 C
ATOM 979 CG2 ILE A 123 -228.605 33.101 32.756 1.00 56.10 C
ANISOU 979 CG2 ILE A 123 7550 6150 7616 -247 -479 120 C
ATOM 980 CD1 ILE A 123 -226.245 34.885 31.638 1.00 47.02 C
ANISOU 980 CD1 ILE A 123 6488 5018 6358 -282 -266 133 C
ATOM 981 N ALA A 124 -230.339 35.031 35.422 1.00 57.89 N
ANISOU 981 N ALA A 124 7462 6412 8121 -69 -718 316 N
ATOM 982 CA ALA A 124 -231.112 34.511 36.547 1.00 53.95 C
ANISOU 982 CA ALA A 124 6867 5903 7727 -31 -742 310 C
ATOM 983 C ALA A 124 -232.597 34.786 36.359 1.00 70.16 C
ANISOU 983 C ALA A 124 8876 7972 9809 -62 -872 353 C
ATOM 984 O ALA A 124 -233.428 33.876 36.474 1.00 67.22 O
ANISOU 984 O ALA A 124 8486 7594 9461 -95 -904 327 O
ATOM 985 CB ALA A 124 -230.622 35.119 37.859 1.00 51.06 C
ANISOU 985 CB ALA A 124 6412 5532 7458 49 -695 328 C
ATOM 986 N LEU A 125 -232.940 36.041 36.048 1.00 71.59 N
ANISOU 986 N LEU A 125 9031 8163 10009 -55 -954 421 N
ATOM 987 CA LEU A 125 -234.334 36.432 35.864 1.00 66.93 C
ANISOU 987 CA LEU A 125 8368 7572 9491 -74 -1093 474 C
ATOM 988 C LEU A 125 -235.030 35.553 34.833 1.00 63.42 C
ANISOU 988 C LEU A 125 7995 7138 8962 -171 -1189 466 C
ATOM 989 O LEU A 125 -236.105 35.004 35.095 1.00 62.48 O
ANISOU 989 O LEU A 125 7800 7016 8923 -191 -1250 458 O
ATOM 990 CB LEU A 125 -234.415 37.904 35.449 1.00 65.61 C
ANISOU 990 CB LEU A 125 8183 7392 9354 -56 -1177 560 C
ATOM 991 CG LEU A 125 -235.791 38.380 34.966 1.00 64.84 C
ANISOU 991 CG LEU A 125 8013 7279 9346 -80 -1356 635 C
ATOM 992 CD1 LEU A 125 -236.849 38.181 36.046 1.00 54.70 C
ANISOU 992 CD1 LEU A 125 6559 5977 8249 -32 -1347 606 C
ATOM 993 CD2 LEU A 125 -235.735 39.840 34.521 1.00 68.81 C
ANISOU 993 CD2 LEU A 125 8509 7749 9886 -60 -1445 734 C
ATOM 994 N TRP A 126 -234.433 35.413 33.650 1.00 63.55 N
ANISOU 994 N TRP A 126 8165 7169 8812 -247 -1197 462 N
ATOM 995 CA TRP A 126 -235.059 34.634 32.592 1.00 61.11 C
ANISOU 995 CA TRP A 126 7954 6872 8392 -363 -1295 449 C
ATOM 996 C TRP A 126 -234.967 33.130 32.823 1.00 76.98 C
ANISOU 996 C TRP A 126 9997 8868 10384 -390 -1201 343 C
ATOM 997 O TRP A 126 -235.695 32.379 32.166 1.00 76.40 O
ANISOU 997 O TRP A 126 9979 8797 10253 -486 -1287 320 O
ATOM 998 CB TRP A 126 -234.453 35.014 31.233 1.00 52.40 C
ANISOU 998 CB TRP A 126 7032 5789 7090 -459 -1320 473 C
ATOM 999 CG TRP A 126 -234.927 36.374 30.792 1.00 72.76 C
ANISOU 999 CG TRP A 126 9591 8370 9685 -467 -1482 605 C
ATOM 1000 CD1 TRP A 126 -234.228 37.541 30.854 1.00 77.05 C
ANISOU 1000 CD1 TRP A 126 10134 8904 10238 -418 -1447 665 C
ATOM 1001 CD2 TRP A 126 -236.227 36.712 30.280 1.00 73.26 C
ANISOU 1001 CD2 TRP A 126 9616 8431 9790 -521 -1715 701 C
ATOM 1002 NE1 TRP A 126 -234.999 38.582 30.394 1.00 86.05 N
ANISOU 1002 NE1 TRP A 126 11248 10027 11419 -438 -1641 795 N
ATOM 1003 CE2 TRP A 126 -236.231 38.102 30.037 1.00 73.37 C
ANISOU 1003 CE2 TRP A 126 9610 8424 9841 -497 -1814 824 C
ATOM 1004 CE3 TRP A 126 -237.383 35.975 29.994 1.00 70.03 C
ANISOU 1004 CE3 TRP A 126 9178 8027 9405 -592 -1858 701 C
ATOM 1005 CZ2 TRP A 126 -237.344 38.771 29.521 1.00 76.02 C
ANISOU 1005 CZ2 TRP A 126 9894 8737 10251 -532 -2060 953 C
ATOM 1006 CZ3 TRP A 126 -238.490 36.643 29.477 1.00 76.54 C
ANISOU 1006 CZ3 TRP A 126 9944 8839 10300 -633 -2106 826 C
ATOM 1007 CH2 TRP A 126 -238.460 38.026 29.247 1.00 72.80 C
ANISOU 1007 CH2 TRP A 126 9447 8338 9876 -598 -2208 954 C
ATOM 1008 N SER A 127 -234.105 32.674 33.737 1.00 78.21 N
ANISOU 1008 N SER A 127 10120 9000 10596 -313 -1042 284 N
ATOM 1009 CA SER A 127 -234.135 31.270 34.128 1.00 71.78 C
ANISOU 1009 CA SER A 127 9313 8152 9809 -325 -970 203 C
ATOM 1010 C SER A 127 -235.375 30.966 34.963 1.00 75.27 C
ANISOU 1010 C SER A 127 9627 8589 10382 -316 -1040 225 C
ATOM 1011 O SER A 127 -236.011 29.920 34.781 1.00 66.18 O
ANISOU 1011 O SER A 127 8495 7419 9230 -383 -1068 183 O
ATOM 1012 CB SER A 127 -232.859 30.900 34.888 1.00 60.38 C
ANISOU 1012 CB SER A 127 7861 6672 8409 -246 -807 156 C
ATOM 1013 OG SER A 127 -231.727 30.892 34.032 1.00 59.61 O
ANISOU 1013 OG SER A 127 7874 6565 8210 -269 -714 109 O
ATOM 1014 N LEU A 128 -235.742 31.872 35.877 1.00 63.99 N
ANISOU 1014 N LEU A 128 8068 7175 9072 -243 -1056 282 N
ATOM 1015 CA LEU A 128 -236.998 31.712 36.603 1.00 66.19 C
ANISOU 1015 CA LEU A 128 8216 7451 9484 -246 -1105 297 C
ATOM 1016 C LEU A 128 -238.193 31.756 35.664 1.00 71.35 C
ANISOU 1016 C LEU A 128 8849 8116 10146 -328 -1274 330 C
ATOM 1017 O LEU A 128 -239.185 31.050 35.886 1.00 75.52 O
ANISOU 1017 O LEU A 128 9308 8634 10753 -375 -1314 314 O
ATOM 1018 CB LEU A 128 -237.130 32.789 37.677 1.00 58.51 C
ANISOU 1018 CB LEU A 128 7116 6482 8631 -160 -1069 335 C
ATOM 1019 CG LEU A 128 -235.971 32.862 38.673 1.00 57.98 C
ANISOU 1019 CG LEU A 128 7069 6408 8553 -92 -931 314 C
ATOM 1020 CD1 LEU A 128 -236.323 33.776 39.832 1.00 58.06 C
ANISOU 1020 CD1 LEU A 128 6963 6421 8676 -35 -890 331 C
ATOM 1021 CD2 LEU A 128 -235.605 31.472 39.173 1.00 65.14 C
ANISOU 1021 CD2 LEU A 128 8026 7288 9437 -113 -851 266 C
ATOM 1022 N VAL A 129 -238.112 32.558 34.604 1.00 71.54 N
ANISOU 1022 N VAL A 129 8935 8158 10089 -358 -1383 384 N
ATOM 1023 CA VAL A 129 -239.196 32.611 33.631 1.00 70.92 C
ANISOU 1023 CA VAL A 129 8852 8090 10006 -450 -1580 433 C
ATOM 1024 C VAL A 129 -239.259 31.309 32.841 1.00 72.08 C
ANISOU 1024 C VAL A 129 9135 8237 10017 -570 -1600 364 C
ATOM 1025 O VAL A 129 -240.333 30.716 32.677 1.00 79.95 O
ANISOU 1025 O VAL A 129 10078 9228 11073 -643 -1710 361 O
ATOM 1026 CB VAL A 129 -239.031 33.835 32.713 1.00 60.91 C
ANISOU 1026 CB VAL A 129 7638 6835 8669 -462 -1704 527 C
ATOM 1027 CG1 VAL A 129 -240.128 33.869 31.650 1.00 53.41 C
ANISOU 1027 CG1 VAL A 129 6698 5892 7703 -573 -1945 598 C
ATOM 1028 CG2 VAL A 129 -239.041 35.117 33.541 1.00 67.47 C
ANISOU 1028 CG2 VAL A 129 8324 7646 9664 -342 -1681 587 C
ATOM 1029 N VAL A 130 -238.107 30.835 32.354 1.00 61.78 N
ANISOU 1029 N VAL A 130 8000 6929 8545 -595 -1485 297 N
ATOM 1030 CA VAL A 130 -238.084 29.630 31.527 1.00 70.79 C
ANISOU 1030 CA VAL A 130 9290 8056 9550 -715 -1483 210 C
ATOM 1031 C VAL A 130 -238.479 28.403 32.345 1.00 68.26 C
ANISOU 1031 C VAL A 130 8903 7693 9341 -710 -1412 141 C
ATOM 1032 O VAL A 130 -239.197 27.522 31.858 1.00 63.75 O
ANISOU 1032 O VAL A 130 8372 7107 8743 -818 -1489 100 O
ATOM 1033 CB VAL A 130 -236.702 29.463 30.864 1.00 67.71 C
ANISOU 1033 CB VAL A 130 9082 7660 8985 -735 -1339 139 C
ATOM 1034 CG1 VAL A 130 -236.468 28.011 30.416 1.00 63.92 C
ANISOU 1034 CG1 VAL A 130 8730 7134 8421 -823 -1251 8 C
ATOM 1035 CG2 VAL A 130 -236.591 30.394 29.676 1.00 58.25 C
ANISOU 1035 CG2 VAL A 130 8007 6505 7620 -816 -1446 202 C
ATOM 1036 N LEU A 131 -238.028 28.327 33.598 1.00 62.54 N
ANISOU 1036 N LEU A 131 8083 6944 8734 -598 -1273 134 N
ATOM 1037 CA LEU A 131 -238.423 27.213 34.450 1.00 59.19 C
ANISOU 1037 CA LEU A 131 7600 6475 8413 -600 -1211 89 C
ATOM 1038 C LEU A 131 -239.938 27.164 34.625 1.00 68.83 C
ANISOU 1038 C LEU A 131 8691 7710 9753 -655 -1342 128 C
ATOM 1039 O LEU A 131 -240.534 26.080 34.652 1.00 80.96 O
ANISOU 1039 O LEU A 131 10230 9211 11321 -732 -1353 83 O
ATOM 1040 CB LEU A 131 -237.725 27.311 35.807 1.00 48.88 C
ANISOU 1040 CB LEU A 131 6223 5150 7200 -483 -1068 101 C
ATOM 1041 CG LEU A 131 -238.023 26.151 36.762 1.00 60.88 C
ANISOU 1041 CG LEU A 131 7705 6615 8812 -493 -998 72 C
ATOM 1042 CD1 LEU A 131 -237.640 24.813 36.144 1.00 55.03 C
ANISOU 1042 CD1 LEU A 131 7094 5805 8011 -560 -957 -13 C
ATOM 1043 CD2 LEU A 131 -237.326 26.344 38.091 1.00 62.74 C
ANISOU 1043 CD2 LEU A 131 7889 6838 9111 -396 -885 101 C
ATOM 1044 N ALA A 132 -240.582 28.328 34.731 1.00 69.63 N
ANISOU 1044 N ALA A 132 8666 7850 9940 -619 -1440 210 N
ATOM 1045 CA ALA A 132 -242.032 28.349 34.881 1.00 66.14 C
ANISOU 1045 CA ALA A 132 8066 7411 9651 -665 -1562 246 C
ATOM 1046 C ALA A 132 -242.722 27.895 33.602 1.00 74.68 C
ANISOU 1046 C ALA A 132 9218 8499 10656 -804 -1747 244 C
ATOM 1047 O ALA A 132 -243.738 27.192 33.655 1.00 72.97 O
ANISOU 1047 O ALA A 132 8924 8268 10535 -882 -1817 229 O
ATOM 1048 CB ALA A 132 -242.506 29.745 35.283 1.00 55.62 C
ANISOU 1048 CB ALA A 132 6571 6100 8464 -582 -1614 327 C
ATOM 1049 N ILE A 133 -242.183 28.281 32.444 1.00 69.47 N
ANISOU 1049 N ILE A 133 8715 7863 9816 -851 -1830 259 N
ATOM 1050 CA ILE A 133 -242.752 27.830 31.177 1.00 63.50 C
ANISOU 1050 CA ILE A 133 8069 7117 8941 -1009 -2012 254 C
ATOM 1051 C ILE A 133 -242.622 26.322 31.046 1.00 76.16 C
ANISOU 1051 C ILE A 133 9788 8680 10468 -1099 -1927 134 C
ATOM 1052 O ILE A 133 -243.546 25.638 30.588 1.00 83.13 O
ANISOU 1052 O ILE A 133 10669 9554 11364 -1225 -2059 115 O
ATOM 1053 CB ILE A 133 -242.073 28.550 29.998 1.00 68.61 C
ANISOU 1053 CB ILE A 133 8898 7799 9373 -1057 -2087 291 C
ATOM 1054 CG1 ILE A 133 -242.324 30.058 30.066 1.00 70.98 C
ANISOU 1054 CG1 ILE A 133 9078 8121 9769 -977 -2203 426 C
ATOM 1055 CG2 ILE A 133 -242.547 27.973 28.673 1.00 59.30 C
ANISOU 1055 CG2 ILE A 133 7882 6632 8018 -1248 -2262 270 C
ATOM 1056 CD1 ILE A 133 -241.702 30.817 28.922 1.00 55.79 C
ANISOU 1056 CD1 ILE A 133 7339 6227 7633 -1037 -2286 483 C
ATOM 1057 N GLU A 134 -241.470 25.780 31.445 1.00 76.27 N
ANISOU 1057 N GLU A 134 9899 8658 10421 -1039 -1713 52 N
ATOM 1058 CA GLU A 134 -241.223 24.354 31.283 1.00 68.28 C
ANISOU 1058 CA GLU A 134 9007 7584 9352 -1115 -1620 -67 C
ATOM 1059 C GLU A 134 -242.118 23.534 32.205 1.00 72.62 C
ANISOU 1059 C GLU A 134 9415 8092 10084 -1124 -1611 -75 C
ATOM 1060 O GLU A 134 -242.773 22.581 31.766 1.00 58.96 O
ANISOU 1060 O GLU A 134 7728 6328 8345 -1251 -1679 -130 O
ATOM 1061 CB GLU A 134 -239.746 24.063 31.537 1.00 67.82 C
ANISOU 1061 CB GLU A 134 9054 7483 9233 -1030 -1400 -139 C
ATOM 1062 CG GLU A 134 -238.829 24.680 30.496 1.00 68.17 C
ANISOU 1062 CG GLU A 134 9259 7560 9083 -1053 -1379 -157 C
ATOM 1063 CD GLU A 134 -237.367 24.405 30.771 1.00 73.74 C
ANISOU 1063 CD GLU A 134 10033 8215 9771 -963 -1155 -231 C
ATOM 1064 OE1 GLU A 134 -237.031 24.067 31.926 1.00 92.31 O
ANISOU 1064 OE1 GLU A 134 12280 10521 12273 -853 -1047 -225 O
ATOM 1065 OE2 GLU A 134 -236.556 24.521 29.828 1.00 66.42 O
ANISOU 1065 OE2 GLU A 134 9263 7291 8682 -1012 -1088 -291 O
ATOM 1066 N ARG A 135 -242.165 23.900 33.489 1.00 65.46 N
ANISOU 1066 N ARG A 135 8348 7186 9337 -1005 -1522 -22 N
ATOM 1067 CA ARG A 135 -243.085 23.248 34.416 1.00 63.43 C
ANISOU 1067 CA ARG A 135 7952 6898 9251 -1026 -1503 -18 C
ATOM 1068 C ARG A 135 -244.529 23.355 33.934 1.00 75.87 C
ANISOU 1068 C ARG A 135 9411 8501 10915 -1132 -1699 18 C
ATOM 1069 O ARG A 135 -245.311 22.406 34.073 1.00 79.75 O
ANISOU 1069 O ARG A 135 9861 8954 11486 -1226 -1721 -16 O
ATOM 1070 CB ARG A 135 -242.929 23.858 35.808 1.00 57.24 C
ANISOU 1070 CB ARG A 135 7029 6125 8593 -898 -1381 37 C
ATOM 1071 CG ARG A 135 -241.602 23.521 36.468 1.00 59.62 C
ANISOU 1071 CG ARG A 135 7426 6385 8840 -810 -1205 10 C
ATOM 1072 CD ARG A 135 -241.380 24.346 37.718 1.00 59.39 C
ANISOU 1072 CD ARG A 135 7288 6385 8895 -698 -1113 69 C
ATOM 1073 NE ARG A 135 -240.341 23.780 38.570 1.00 69.00 N
ANISOU 1073 NE ARG A 135 8573 7549 10093 -640 -970 58 N
ATOM 1074 CZ ARG A 135 -239.854 24.387 39.645 1.00 65.99 C
ANISOU 1074 CZ ARG A 135 8145 7186 9741 -553 -885 101 C
ATOM 1075 NH1 ARG A 135 -240.304 25.585 39.984 1.00 65.54 N
ANISOU 1075 NH1 ARG A 135 7975 7192 9734 -511 -904 142 N
ATOM 1076 NH2 ARG A 135 -238.918 23.803 40.376 1.00 69.46 N
ANISOU 1076 NH2 ARG A 135 8652 7573 10168 -513 -789 105 N
ATOM 1077 N TYR A 136 -244.900 24.500 33.359 1.00 80.10 N
ANISOU 1077 N TYR A 136 9886 9095 11453 -1122 -1853 94 N
ATOM 1078 CA TYR A 136 -246.246 24.654 32.821 1.00 78.09 C
ANISOU 1078 CA TYR A 136 9508 8859 11303 -1222 -2074 143 C
ATOM 1079 C TYR A 136 -246.483 23.709 31.652 1.00 81.01 C
ANISOU 1079 C TYR A 136 10040 9213 11525 -1396 -2206 83 C
ATOM 1080 O TYR A 136 -247.565 23.123 31.529 1.00 84.60 O
ANISOU 1080 O TYR A 136 10404 9652 12087 -1507 -2325 78 O
ATOM 1081 CB TYR A 136 -246.477 26.105 32.390 1.00 65.10 C
ANISOU 1081 CB TYR A 136 7780 7262 9694 -1170 -2229 251 C
ATOM 1082 CG TYR A 136 -247.647 26.283 31.450 1.00 69.91 C
ANISOU 1082 CG TYR A 136 8316 7885 10360 -1292 -2516 317 C
ATOM 1083 CD1 TYR A 136 -248.948 26.323 31.932 1.00 76.13 C
ANISOU 1083 CD1 TYR A 136 8846 8659 11421 -1305 -2603 356 C
ATOM 1084 CD2 TYR A 136 -247.452 26.414 30.081 1.00 63.38 C
ANISOU 1084 CD2 TYR A 136 7678 7085 9318 -1403 -2701 341 C
ATOM 1085 CE1 TYR A 136 -250.026 26.482 31.079 1.00 77.99 C
ANISOU 1085 CE1 TYR A 136 8992 8901 11738 -1417 -2890 427 C
ATOM 1086 CE2 TYR A 136 -248.526 26.576 29.216 1.00 70.65 C
ANISOU 1086 CE2 TYR A 136 8540 8018 10284 -1529 -2998 417 C
ATOM 1087 CZ TYR A 136 -249.810 26.611 29.722 1.00 75.32 C
ANISOU 1087 CZ TYR A 136 8854 8591 11175 -1530 -3102 464 C
ATOM 1088 OH TYR A 136 -250.881 26.772 28.871 1.00 83.07 O
ANISOU 1088 OH TYR A 136 9756 9578 12231 -1654 -3421 550 O
ATOM 1089 N VAL A 137 -245.488 23.558 30.774 1.00 75.75 N
ANISOU 1089 N VAL A 137 9616 8550 10617 -1433 -2179 29 N
ATOM 1090 CA VAL A 137 -245.641 22.679 29.617 1.00 84.26 C
ANISOU 1090 CA VAL A 137 10881 9611 11523 -1614 -2285 -50 C
ATOM 1091 C VAL A 137 -245.716 21.221 30.058 1.00 87.67 C
ANISOU 1091 C VAL A 137 11344 9961 12005 -1669 -2158 -161 C
ATOM 1092 O VAL A 137 -246.530 20.443 29.546 1.00 89.82 O
ANISOU 1092 O VAL A 137 11640 10210 12278 -1824 -2284 -203 O
ATOM 1093 CB VAL A 137 -244.495 22.913 28.614 1.00 74.98 C
ANISOU 1093 CB VAL A 137 9963 8453 10072 -1644 -2242 -96 C
ATOM 1094 CG1 VAL A 137 -244.453 21.813 27.563 1.00 70.41 C
ANISOU 1094 CG1 VAL A 137 9614 7839 9299 -1832 -2271 -222 C
ATOM 1095 CG2 VAL A 137 -244.642 24.270 27.946 1.00 68.50 C
ANISOU 1095 CG2 VAL A 137 9137 7707 9182 -1644 -2427 29 C
ATOM 1096 N VAL A 138 -244.887 20.837 31.032 1.00 80.09 N
ANISOU 1096 N VAL A 138 10382 8950 11098 -1547 -1921 -202 N
ATOM 1097 CA VAL A 138 -244.816 19.445 31.460 1.00 72.46 C
ANISOU 1097 CA VAL A 138 9464 7886 10180 -1591 -1794 -297 C
ATOM 1098 C VAL A 138 -246.088 19.031 32.198 1.00 85.11 C
ANISOU 1098 C VAL A 138 10870 9473 11994 -1640 -1852 -258 C
ATOM 1099 O VAL A 138 -246.592 17.916 32.010 1.00 86.81 O
ANISOU 1099 O VAL A 138 11127 9623 12234 -1766 -1875 -326 O
ATOM 1100 CB VAL A 138 -243.557 19.225 32.317 1.00 63.67 C
ANISOU 1100 CB VAL A 138 8394 6717 9079 -1445 -1555 -324 C
ATOM 1101 CG1 VAL A 138 -243.595 17.870 32.980 1.00 77.85 C
ANISOU 1101 CG1 VAL A 138 10202 8400 10976 -1474 -1440 -384 C
ATOM 1102 CG2 VAL A 138 -242.312 19.341 31.459 1.00 60.88 C
ANISOU 1102 CG2 VAL A 138 8242 6357 8535 -1429 -1476 -397 C
ATOM 1103 N VAL A 139 -246.634 19.913 33.035 1.00 75.37 N
ANISOU 1103 N VAL A 139 9421 8293 10923 -1549 -1865 -156 N
ATOM 1104 CA VAL A 139 -247.800 19.574 33.847 1.00 70.34 C
ANISOU 1104 CA VAL A 139 8581 7640 10506 -1591 -1876 -126 C
ATOM 1105 C VAL A 139 -249.100 19.818 33.088 1.00 79.11 C
ANISOU 1105 C VAL A 139 9569 8789 11699 -1715 -2124 -89 C
ATOM 1106 O VAL A 139 -249.905 18.899 32.911 1.00 85.93 O
ANISOU 1106 O VAL A 139 10406 9612 12631 -1854 -2193 -129 O
ATOM 1107 CB VAL A 139 -247.794 20.356 35.170 1.00 65.92 C
ANISOU 1107 CB VAL A 139 7845 7108 10092 -1447 -1740 -54 C
ATOM 1108 CG1 VAL A 139 -249.126 20.180 35.899 1.00 79.15 C
ANISOU 1108 CG1 VAL A 139 9291 8779 12003 -1505 -1750 -25 C
ATOM 1109 CG2 VAL A 139 -246.663 19.875 36.038 1.00 61.94 C
ANISOU 1109 CG2 VAL A 139 7453 6553 9530 -1358 -1521 -82 C
ATOM 1110 N CYS A 140 -249.318 21.056 32.639 1.00 80.46 N
ANISOU 1110 N CYS A 140 9660 9032 11881 -1669 -2272 -5 N
ATOM 1111 CA CYS A 140 -250.577 21.410 31.992 1.00 73.78 C
ANISOU 1111 CA CYS A 140 8662 8216 11156 -1772 -2535 57 C
ATOM 1112 C CYS A 140 -250.731 20.807 30.603 1.00 78.36 C
ANISOU 1112 C CYS A 140 9430 8793 11549 -1956 -2742 14 C
ATOM 1113 O CYS A 140 -251.846 20.828 30.069 1.00 92.48 O
ANISOU 1113 O CYS A 140 11101 10595 13442 -2077 -2982 59 O
ATOM 1114 CB CYS A 140 -250.710 22.931 31.890 1.00 69.97 C
ANISOU 1114 CB CYS A 140 8046 7790 10748 -1665 -2647 172 C
ATOM 1115 SG CYS A 140 -250.672 23.794 33.466 1.00 89.80 S
ANISOU 1115 SG CYS A 140 10328 10304 13487 -1467 -2420 212 S
ATOM 1116 N LYS A 141 -249.657 20.289 30.009 1.00 79.91 N
ANISOU 1116 N LYS A 141 9909 8971 11482 -1988 -2656 -76 N
ATOM 1117 CA LYS A 141 -249.649 19.692 28.675 1.00 87.88 C
ANISOU 1117 CA LYS A 141 11147 9974 12268 -2176 -2810 -145 C
ATOM 1118 C LYS A 141 -250.459 20.516 27.661 1.00 96.53 C
ANISOU 1118 C LYS A 141 12203 11138 13336 -2280 -3143 -39 C
ATOM 1119 O LYS A 141 -251.466 20.035 27.134 1.00 98.78 O
ANISOU 1119 O LYS A 141 12446 11416 13669 -2448 -3358 -38 O
ATOM 1120 CB LYS A 141 -250.145 18.251 28.723 1.00 80.69 C
ANISOU 1120 CB LYS A 141 10271 8985 11402 -2318 -2784 -252 C
ATOM 1121 CG LYS A 141 -249.313 17.352 29.623 1.00 88.70 C
ANISOU 1121 CG LYS A 141 11353 9913 12437 -2232 -2483 -346 C
ATOM 1122 CD LYS A 141 -249.927 15.972 29.763 1.00 87.69 C
ANISOU 1122 CD LYS A 141 11232 9693 12395 -2372 -2467 -433 C
ATOM 1123 CE LYS A 141 -249.146 15.113 30.749 1.00 95.37 C
ANISOU 1123 CE LYS A 141 12253 10564 13419 -2279 -2186 -496 C
ATOM 1124 NZ LYS A 141 -249.891 13.859 31.079 1.00110.66 N
ANISOU 1124 NZ LYS A 141 14152 12404 15489 -2407 -2171 -551 N
ATOM 1125 N PRO A 142 -250.039 21.751 27.370 1.00104.20 N
ANISOU 1125 N PRO A 142 13187 12168 14237 -2190 -3205 59 N
ATOM 1126 CA PRO A 142 -250.786 22.560 26.392 1.00103.42 C
ANISOU 1126 CA PRO A 142 13058 12121 14115 -2291 -3547 184 C
ATOM 1127 C PRO A 142 -250.642 22.068 24.966 1.00102.04 C
ANISOU 1127 C PRO A 142 13188 11963 13620 -2516 -3717 129 C
ATOM 1128 O PRO A 142 -251.490 22.397 24.129 1.00109.22 O
ANISOU 1128 O PRO A 142 14080 12905 14516 -2658 -4046 225 O
ATOM 1129 CB PRO A 142 -250.180 23.959 26.562 1.00 92.37 C
ANISOU 1129 CB PRO A 142 11621 10761 12714 -2123 -3517 294 C
ATOM 1130 CG PRO A 142 -248.791 23.693 27.019 1.00 87.87 C
ANISOU 1130 CG PRO A 142 11216 10175 11994 -2013 -3189 187 C
ATOM 1131 CD PRO A 142 -248.864 22.471 27.893 1.00 91.42 C
ANISOU 1131 CD PRO A 142 11613 10563 12559 -2003 -2986 70 C
ATOM 1132 N MET A 143 -249.599 21.300 24.661 1.00102.99 N
ANISOU 1132 N MET A 143 13585 12057 13488 -2559 -3505 -23 N
ATOM 1133 CA MET A 143 -249.397 20.730 23.337 1.00101.84 C
ANISOU 1133 CA MET A 143 13758 11919 13018 -2787 -3613 -113 C
ATOM 1134 C MET A 143 -249.761 19.251 23.369 1.00124.59 C
ANISOU 1134 C MET A 143 16694 14727 15920 -2922 -3555 -268 C
ATOM 1135 O MET A 143 -249.358 18.527 24.286 1.00126.03 O
ANISOU 1135 O MET A 143 16821 14838 16228 -2813 -3286 -363 O
ATOM 1136 CB MET A 143 -247.954 20.935 22.876 1.00 88.74 C
ANISOU 1136 CB MET A 143 12377 10271 11070 -2755 -3398 -193 C
ATOM 1137 CG MET A 143 -247.628 22.406 22.644 1.00102.12 C
ANISOU 1137 CG MET A 143 14057 12038 12708 -2665 -3490 -34 C
ATOM 1138 SD MET A 143 -245.885 22.800 22.413 1.00108.64 S
ANISOU 1138 SD MET A 143 15128 12873 13277 -2578 -3186 -111 S
ATOM 1139 CE MET A 143 -245.220 22.484 24.047 1.00 95.93 C
ANISOU 1139 CE MET A 143 13308 11199 11944 -2308 -2834 -173 C
ATOM 1140 N SER A 144 -250.529 18.814 22.367 1.00130.64 N
ANISOU 1140 N SER A 144 17573 15504 16562 -3166 -3821 -286 N
ATOM 1141 CA SER A 144 -251.181 17.508 22.376 1.00139.50 C
ANISOU 1141 CA SER A 144 18698 16554 17750 -3318 -3840 -406 C
ATOM 1142 C SER A 144 -250.205 16.350 22.552 1.00144.61 C
ANISOU 1142 C SER A 144 19551 17105 18288 -3312 -3505 -618 C
ATOM 1143 O SER A 144 -250.247 15.646 23.566 1.00149.04 O
ANISOU 1143 O SER A 144 19969 17587 19073 -3214 -3316 -668 O
ATOM 1144 CB SER A 144 -251.988 17.318 21.089 1.00149.37 C
ANISOU 1144 CB SER A 144 20100 17840 18815 -3607 -4196 -398 C
ATOM 1145 OG SER A 144 -251.167 17.475 19.945 1.00156.79 O
ANISOU 1145 OG SER A 144 21401 18815 19356 -3736 -4197 -463 O
ATOM 1146 N ASN A 145 -249.335 16.132 21.569 1.00143.25 N
ANISOU 1146 N ASN A 145 19716 16930 17784 -3424 -3426 -742 N
ATOM 1147 CA ASN A 145 -248.375 15.030 21.595 1.00136.43 C
ANISOU 1147 CA ASN A 145 19056 15957 16826 -3428 -3109 -958 C
ATOM 1148 C ASN A 145 -246.976 15.634 21.674 1.00127.25 C
ANISOU 1148 C ASN A 145 17999 14807 15542 -3260 -2850 -980 C
ATOM 1149 O ASN A 145 -246.275 15.772 20.671 1.00130.60 O
ANISOU 1149 O ASN A 145 18701 15255 15665 -3368 -2805 -1065 O
ATOM 1150 CB ASN A 145 -248.540 14.125 20.364 1.00141.27 C
ANISOU 1150 CB ASN A 145 19976 16532 17168 -3722 -3197 -1129 C
ATOM 1151 CG ASN A 145 -249.915 13.489 20.289 1.00142.84 C
ANISOU 1151 CG ASN A 145 20065 16712 17498 -3900 -3461 -1112 C
ATOM 1152 OD1 ASN A 145 -250.595 13.327 21.304 1.00141.39 O
ANISOU 1152 OD1 ASN A 145 19586 16499 17637 -3794 -3474 -1032 O
ATOM 1153 ND2 ASN A 145 -250.331 13.122 19.083 1.00148.23 N
ANISOU 1153 ND2 ASN A 145 20988 17410 17922 -4186 -3671 -1190 N
ATOM 1154 N PHE A 146 -246.573 15.997 22.891 1.00114.01 N
ANISOU 1154 N PHE A 146 16100 13116 14103 -3006 -2675 -903 N
ATOM 1155 CA PHE A 146 -245.302 16.661 23.137 1.00100.17 C
ANISOU 1155 CA PHE A 146 14390 11378 12291 -2826 -2448 -898 C
ATOM 1156 C PHE A 146 -244.602 16.004 24.317 1.00 99.95 C
ANISOU 1156 C PHE A 146 14256 11243 12478 -2636 -2154 -961 C
ATOM 1157 O PHE A 146 -245.241 15.659 25.317 1.00 93.97 O
ANISOU 1157 O PHE A 146 13283 10448 11971 -2565 -2164 -904 O
ATOM 1158 CB PHE A 146 -245.503 18.161 23.411 1.00 96.57 C
ANISOU 1158 CB PHE A 146 13760 11037 11895 -2701 -2593 -689 C
ATOM 1159 CG PHE A 146 -244.221 18.920 23.622 1.00 96.60 C
ANISOU 1159 CG PHE A 146 13808 11063 11835 -2532 -2380 -675 C
ATOM 1160 CD1 PHE A 146 -243.483 19.374 22.541 1.00 91.50 C
ANISOU 1160 CD1 PHE A 146 13412 10461 10892 -2625 -2359 -715 C
ATOM 1161 CD2 PHE A 146 -243.759 19.187 24.902 1.00 93.76 C
ANISOU 1161 CD2 PHE A 146 13244 10678 11702 -2297 -2202 -622 C
ATOM 1162 CE1 PHE A 146 -242.305 20.074 22.732 1.00 94.27 C
ANISOU 1162 CE1 PHE A 146 13790 10829 11201 -2478 -2159 -704 C
ATOM 1163 CE2 PHE A 146 -242.583 19.887 25.098 1.00 91.10 C
ANISOU 1163 CE2 PHE A 146 12939 10360 11317 -2151 -2021 -609 C
ATOM 1164 CZ PHE A 146 -241.855 20.330 24.011 1.00 93.65 C
ANISOU 1164 CZ PHE A 146 13492 10723 11368 -2238 -1997 -651 C
ATOM 1165 N ARG A 147 -243.286 15.834 24.192 1.00 99.02 N
ANISOU 1165 N ARG A 147 14288 11072 12262 -2562 -1894 -1074 N
ATOM 1166 CA ARG A 147 -242.448 15.280 25.246 1.00100.30 C
ANISOU 1166 CA ARG A 147 14364 11125 12620 -2376 -1626 -1121 C
ATOM 1167 C ARG A 147 -241.233 16.179 25.424 1.00 99.80 C
ANISOU 1167 C ARG A 147 14303 11101 12514 -2208 -1463 -1084 C
ATOM 1168 O ARG A 147 -240.525 16.465 24.452 1.00110.08 O
ANISOU 1168 O ARG A 147 15804 12429 13592 -2278 -1397 -1164 O
ATOM 1169 CB ARG A 147 -242.017 13.845 24.912 1.00107.01 C
ANISOU 1169 CB ARG A 147 15389 11818 13452 -2466 -1449 -1332 C
ATOM 1170 CG ARG A 147 -241.080 13.212 25.930 1.00118.86 C
ANISOU 1170 CG ARG A 147 16813 13183 15167 -2278 -1188 -1375 C
ATOM 1171 CD ARG A 147 -241.809 12.854 27.213 1.00123.95 C
ANISOU 1171 CD ARG A 147 17229 13789 16077 -2194 -1239 -1261 C
ATOM 1172 NE ARG A 147 -240.928 12.207 28.183 1.00128.63 N
ANISOU 1172 NE ARG A 147 17767 14245 16864 -2033 -1019 -1283 N
ATOM 1173 CZ ARG A 147 -240.310 12.843 29.173 1.00132.38 C
ANISOU 1173 CZ ARG A 147 18097 14747 17456 -1835 -939 -1164 C
ATOM 1174 NH1 ARG A 147 -240.475 14.150 29.333 1.00129.77 N
ANISOU 1174 NH1 ARG A 147 17662 14571 17074 -1768 -1040 -1028 N
ATOM 1175 NH2 ARG A 147 -239.528 12.170 30.007 1.00132.49 N
ANISOU 1175 NH2 ARG A 147 18073 14624 17643 -1708 -770 -1177 N
ATOM 1176 N PHE A 148 -240.996 16.625 26.659 1.00 87.23 N
ANISOU 1176 N PHE A 148 12498 9515 11131 -2003 -1396 -968 N
ATOM 1177 CA PHE A 148 -239.928 17.579 26.949 1.00 87.23 C
ANISOU 1177 CA PHE A 148 12466 9560 11119 -1840 -1270 -911 C
ATOM 1178 C PHE A 148 -238.609 16.829 27.087 1.00 89.32 C
ANISOU 1178 C PHE A 148 12817 9700 11423 -1759 -992 -1050 C
ATOM 1179 O PHE A 148 -238.430 16.036 28.017 1.00 93.00 O
ANISOU 1179 O PHE A 148 13189 10057 12091 -1666 -887 -1064 O
ATOM 1180 CB PHE A 148 -240.245 18.370 28.218 1.00 80.57 C
ANISOU 1180 CB PHE A 148 11367 8770 10474 -1671 -1320 -739 C
ATOM 1181 CG PHE A 148 -239.193 19.376 28.584 1.00 77.32 C
ANISOU 1181 CG PHE A 148 10914 8403 10061 -1510 -1207 -677 C
ATOM 1182 CD1 PHE A 148 -239.140 20.609 27.948 1.00 79.72 C
ANISOU 1182 CD1 PHE A 148 11252 8816 10222 -1525 -1307 -599 C
ATOM 1183 CD2 PHE A 148 -238.254 19.093 29.567 1.00 82.38 C
ANISOU 1183 CD2 PHE A 148 11483 8970 10849 -1351 -1015 -687 C
ATOM 1184 CE1 PHE A 148 -238.165 21.541 28.281 1.00 78.09 C
ANISOU 1184 CE1 PHE A 148 11006 8644 10020 -1386 -1201 -545 C
ATOM 1185 CE2 PHE A 148 -237.275 20.023 29.906 1.00 89.07 C
ANISOU 1185 CE2 PHE A 148 12286 9856 11700 -1213 -922 -631 C
ATOM 1186 CZ PHE A 148 -237.233 21.248 29.262 1.00 77.80 C
ANISOU 1186 CZ PHE A 148 10891 8538 10131 -1232 -1008 -566 C
ATOM 1187 N GLY A 149 -237.676 17.089 26.177 1.00 79.47 N
ANISOU 1187 N GLY A 149 11741 8460 9995 -1796 -870 -1145 N
ATOM 1188 CA GLY A 149 -236.422 16.365 26.181 1.00 68.21 C
ANISOU 1188 CA GLY A 149 10387 6903 8627 -1728 -597 -1295 C
ATOM 1189 C GLY A 149 -235.198 17.246 26.290 1.00 86.05 C
ANISOU 1189 C GLY A 149 12617 9197 10880 -1592 -447 -1266 C
ATOM 1190 O GLY A 149 -235.295 18.427 26.638 1.00 85.86 O
ANISOU 1190 O GLY A 149 12487 9292 10844 -1516 -551 -1109 O
ATOM 1191 N GLU A 150 -234.034 16.667 25.985 1.00 93.08 N
ANISOU 1191 N GLU A 150 13595 9976 11797 -1564 -196 -1423 N
ATOM 1192 CA GLU A 150 -232.774 17.392 26.102 1.00 89.35 C
ANISOU 1192 CA GLU A 150 13078 9518 11354 -1435 -30 -1412 C
ATOM 1193 C GLU A 150 -232.723 18.579 25.146 1.00 92.23 C
ANISOU 1193 C GLU A 150 13564 10031 11449 -1535 -84 -1374 C
ATOM 1194 O GLU A 150 -232.245 19.659 25.513 1.00 88.77 O
ANISOU 1194 O GLU A 150 13026 9671 11030 -1426 -88 -1254 O
ATOM 1195 CB GLU A 150 -231.607 16.436 25.843 1.00 88.67 C
ANISOU 1195 CB GLU A 150 13055 9263 11372 -1404 258 -1610 C
ATOM 1196 CG GLU A 150 -230.229 17.033 26.072 1.00103.91 C
ANISOU 1196 CG GLU A 150 14902 11182 13399 -1259 447 -1607 C
ATOM 1197 CD GLU A 150 -229.109 16.065 25.740 1.00111.90 C
ANISOU 1197 CD GLU A 150 15959 12012 14546 -1233 739 -1816 C
ATOM 1198 OE1 GLU A 150 -229.360 15.084 25.007 1.00124.63 O
ANISOU 1198 OE1 GLU A 150 17731 13528 16095 -1368 819 -1994 O
ATOM 1199 OE2 GLU A 150 -227.977 16.284 26.216 1.00112.88 O
ANISOU 1199 OE2 GLU A 150 15950 12082 14857 -1079 888 -1806 O
ATOM 1200 N ASN A 151 -233.209 18.396 23.914 1.00 90.18 N
ANISOU 1200 N ASN A 151 13530 9805 10928 -1753 -135 -1471 N
ATOM 1201 CA ASN A 151 -233.179 19.476 22.932 1.00 87.95 C
ANISOU 1201 CA ASN A 151 13397 9656 10362 -1876 -202 -1425 C
ATOM 1202 C ASN A 151 -234.003 20.672 23.392 1.00 98.22 C
ANISOU 1202 C ASN A 151 14558 11092 11668 -1824 -477 -1184 C
ATOM 1203 O ASN A 151 -233.575 21.824 23.247 1.00 95.99 O
ANISOU 1203 O ASN A 151 14271 10897 11306 -1789 -487 -1085 O
ATOM 1204 CB ASN A 151 -233.684 18.969 21.582 1.00100.18 C
ANISOU 1204 CB ASN A 151 15230 11216 11619 -2144 -244 -1562 C
ATOM 1205 CG ASN A 151 -232.814 17.873 21.010 1.00113.89 C
ANISOU 1205 CG ASN A 151 17126 12813 13333 -2211 63 -1826 C
ATOM 1206 OD1 ASN A 151 -231.599 18.029 20.889 1.00108.53 O
ANISOU 1206 OD1 ASN A 151 16461 12093 12684 -2142 326 -1915 O
ATOM 1207 ND2 ASN A 151 -233.432 16.746 20.663 1.00120.70 N
ANISOU 1207 ND2 ASN A 151 18102 13592 14167 -2345 38 -1962 N
ATOM 1208 N HIS A 152 -235.192 20.424 23.945 1.00 97.00 N
ANISOU 1208 N HIS A 152 14284 10948 11622 -1822 -694 -1093 N
ATOM 1209 CA HIS A 152 -236.013 21.530 24.425 1.00 86.39 C
ANISOU 1209 CA HIS A 152 12784 9714 10327 -1764 -938 -879 C
ATOM 1210 C HIS A 152 -235.354 22.235 25.604 1.00 82.26 C
ANISOU 1210 C HIS A 152 12048 9195 10012 -1534 -849 -775 C
ATOM 1211 O HIS A 152 -235.437 23.463 25.724 1.00 81.46 O
ANISOU 1211 O HIS A 152 11876 9182 9893 -1482 -954 -631 O
ATOM 1212 CB HIS A 152 -237.404 21.033 24.811 1.00 71.91 C
ANISOU 1212 CB HIS A 152 10845 7876 8600 -1810 -1154 -823 C
ATOM 1213 CG HIS A 152 -238.113 20.306 23.714 1.00 88.77 C
ANISOU 1213 CG HIS A 152 13180 10006 10545 -2046 -1269 -921 C
ATOM 1214 ND1 HIS A 152 -238.212 18.931 23.675 1.00 89.65 N
ANISOU 1214 ND1 HIS A 152 13359 10006 10700 -2115 -1175 -1081 N
ATOM 1215 CD2 HIS A 152 -238.768 20.762 22.619 1.00 86.05 C
ANISOU 1215 CD2 HIS A 152 12987 9746 9962 -2239 -1484 -878 C
ATOM 1216 CE1 HIS A 152 -238.894 18.572 22.603 1.00 82.65 C
ANISOU 1216 CE1 HIS A 152 12660 9140 9603 -2346 -1319 -1145 C
ATOM 1217 NE2 HIS A 152 -239.243 19.663 21.945 1.00 94.47 N
ANISOU 1217 NE2 HIS A 152 14215 10760 10920 -2428 -1516 -1020 N
ATOM 1218 N ALA A 153 -234.699 21.476 26.487 1.00 79.69 N
ANISOU 1218 N ALA A 153 11623 8766 9888 -1401 -668 -842 N
ATOM 1219 CA ALA A 153 -234.044 22.085 27.640 1.00 84.00 C
ANISOU 1219 CA ALA A 153 11981 9314 10622 -1200 -596 -745 C
ATOM 1220 C ALA A 153 -232.873 22.961 27.220 1.00 83.36 C
ANISOU 1220 C ALA A 153 11953 9268 10451 -1162 -462 -750 C
ATOM 1221 O ALA A 153 -232.572 23.958 27.888 1.00 71.81 O
ANISOU 1221 O ALA A 153 10360 7856 9067 -1040 -484 -630 O
ATOM 1222 CB ALA A 153 -233.573 21.008 28.615 1.00 82.27 C
ANISOU 1222 CB ALA A 153 11664 8966 10628 -1086 -453 -806 C
ATOM 1223 N ILE A 154 -232.204 22.607 26.124 1.00 78.86 N
ANISOU 1223 N ILE A 154 11577 8668 9718 -1274 -312 -896 N
ATOM 1224 CA ILE A 154 -231.088 23.414 25.652 1.00 79.19 C
ANISOU 1224 CA ILE A 154 11677 8743 9669 -1260 -164 -910 C
ATOM 1225 C ILE A 154 -231.598 24.698 25.011 1.00 84.90 C
ANISOU 1225 C ILE A 154 12474 9597 10187 -1351 -345 -776 C
ATOM 1226 O ILE A 154 -231.011 25.772 25.194 1.00 86.45 O
ANISOU 1226 O ILE A 154 12613 9843 10392 -1276 -320 -685 O
ATOM 1227 CB ILE A 154 -230.212 22.592 24.691 1.00 76.77 C
ANISOU 1227 CB ILE A 154 11554 8354 9262 -1362 88 -1125 C
ATOM 1228 CG1 ILE A 154 -229.558 21.433 25.445 1.00 70.95 C
ANISOU 1228 CG1 ILE A 154 10702 7462 8791 -1234 271 -1237 C
ATOM 1229 CG2 ILE A 154 -229.151 23.465 24.057 1.00 76.72 C
ANISOU 1229 CG2 ILE A 154 11626 8392 9131 -1385 247 -1144 C
ATOM 1230 CD1 ILE A 154 -228.819 20.476 24.552 1.00 76.16 C
ANISOU 1230 CD1 ILE A 154 11524 8012 9402 -1328 527 -1471 C
ATOM 1231 N MET A 155 -232.701 24.612 24.261 1.00 81.49 N
ANISOU 1231 N MET A 155 12167 9214 9581 -1516 -545 -754 N
ATOM 1232 CA MET A 155 -233.325 25.819 23.726 1.00 80.63 C
ANISOU 1232 CA MET A 155 12107 9215 9313 -1596 -769 -595 C
ATOM 1233 C MET A 155 -233.682 26.791 24.843 1.00 84.15 C
ANISOU 1233 C MET A 155 12308 9698 9968 -1421 -901 -414 C
ATOM 1234 O MET A 155 -233.436 27.997 24.729 1.00 92.40 O
ANISOU 1234 O MET A 155 13342 10799 10966 -1395 -951 -298 O
ATOM 1235 CB MET A 155 -234.572 25.462 22.918 1.00 85.89 C
ANISOU 1235 CB MET A 155 12904 9916 9816 -1790 -1005 -584 C
ATOM 1236 CG MET A 155 -234.308 24.836 21.561 1.00104.43 C
ANISOU 1236 CG MET A 155 15555 12255 11870 -2018 -918 -742 C
ATOM 1237 SD MET A 155 -235.843 24.265 20.791 1.00127.43 S
ANISOU 1237 SD MET A 155 18595 15197 14625 -2245 -1227 -731 S
ATOM 1238 CE MET A 155 -236.799 25.785 20.765 1.00122.82 C
ANISOU 1238 CE MET A 155 17911 14722 14033 -2242 -1590 -447 C
ATOM 1239 N GLY A 156 -234.255 26.281 25.935 1.00 73.30 N
ANISOU 1239 N GLY A 156 10745 8286 8822 -1309 -947 -393 N
ATOM 1240 CA GLY A 156 -234.586 27.146 27.055 1.00 68.67 C
ANISOU 1240 CA GLY A 156 9934 7727 8431 -1152 -1039 -246 C
ATOM 1241 C GLY A 156 -233.378 27.863 27.627 1.00 73.62 C
ANISOU 1241 C GLY A 156 10489 8350 9134 -1012 -875 -225 C
ATOM 1242 O GLY A 156 -233.439 29.059 27.924 1.00 79.17 O
ANISOU 1242 O GLY A 156 11108 9101 9874 -947 -958 -99 O
ATOM 1243 N VAL A 157 -232.264 27.143 27.793 1.00 81.54 N
ANISOU 1243 N VAL A 157 11515 9285 10180 -964 -645 -348 N
ATOM 1244 CA VAL A 157 -231.049 27.759 28.324 1.00 76.72 C
ANISOU 1244 CA VAL A 157 10826 8665 9659 -838 -492 -333 C
ATOM 1245 C VAL A 157 -230.536 28.821 27.361 1.00 72.16 C
ANISOU 1245 C VAL A 157 10372 8148 8898 -915 -475 -298 C
ATOM 1246 O VAL A 157 -230.241 29.956 27.754 1.00 74.34 O
ANISOU 1246 O VAL A 157 10564 8462 9221 -839 -504 -191 O
ATOM 1247 CB VAL A 157 -229.977 26.689 28.602 1.00 70.86 C
ANISOU 1247 CB VAL A 157 10073 7822 9027 -780 -262 -474 C
ATOM 1248 CG1 VAL A 157 -228.626 27.354 28.879 1.00 75.50 C
ANISOU 1248 CG1 VAL A 157 10598 8402 9687 -682 -105 -468 C
ATOM 1249 CG2 VAL A 157 -230.396 25.815 29.769 1.00 61.57 C
ANISOU 1249 CG2 VAL A 157 8757 6581 8054 -685 -293 -467 C
ATOM 1250 N ALA A 158 -230.434 28.465 26.079 1.00 61.00 N
ANISOU 1250 N ALA A 158 9174 6741 7263 -1083 -425 -390 N
ATOM 1251 CA ALA A 158 -230.002 29.419 25.068 1.00 63.53 C
ANISOU 1251 CA ALA A 158 9649 7120 7371 -1191 -409 -352 C
ATOM 1252 C ALA A 158 -230.898 30.651 25.054 1.00 80.26 C
ANISOU 1252 C ALA A 158 11732 9311 9452 -1202 -672 -157 C
ATOM 1253 O ALA A 158 -230.416 31.780 24.885 1.00 88.42 O
ANISOU 1253 O ALA A 158 12778 10379 10441 -1192 -668 -67 O
ATOM 1254 CB ALA A 158 -229.986 28.741 23.698 1.00 58.75 C
ANISOU 1254 CB ALA A 158 9308 6514 6502 -1403 -340 -483 C
ATOM 1255 N PHE A 159 -232.201 30.456 25.257 1.00 84.06 N
ANISOU 1255 N PHE A 159 12156 9806 9978 -1217 -898 -90 N
ATOM 1256 CA PHE A 159 -233.139 31.572 25.232 1.00 76.17 C
ANISOU 1256 CA PHE A 159 11099 8856 8987 -1221 -1158 93 C
ATOM 1257 C PHE A 159 -232.832 32.590 26.327 1.00 72.11 C
ANISOU 1257 C PHE A 159 10381 8337 8681 -1039 -1143 193 C
ATOM 1258 O PHE A 159 -232.965 33.799 26.109 1.00 84.54 O
ANISOU 1258 O PHE A 159 11951 9937 10231 -1042 -1261 327 O
ATOM 1259 CB PHE A 159 -234.566 31.045 25.364 1.00 65.70 C
ANISOU 1259 CB PHE A 159 9705 7531 7727 -1258 -1378 127 C
ATOM 1260 CG PHE A 159 -235.605 32.118 25.454 1.00 69.90 C
ANISOU 1260 CG PHE A 159 10128 8092 8339 -1240 -1646 311 C
ATOM 1261 CD1 PHE A 159 -236.047 32.771 24.313 1.00 68.74 C
ANISOU 1261 CD1 PHE A 159 10133 7983 8003 -1392 -1849 418 C
ATOM 1262 CD2 PHE A 159 -236.153 32.466 26.677 1.00 63.51 C
ANISOU 1262 CD2 PHE A 159 9067 7264 7801 -1079 -1695 375 C
ATOM 1263 CE1 PHE A 159 -237.013 33.759 24.390 1.00 68.19 C
ANISOU 1263 CE1 PHE A 159 9943 7919 8046 -1366 -2111 596 C
ATOM 1264 CE2 PHE A 159 -237.117 33.453 26.762 1.00 67.80 C
ANISOU 1264 CE2 PHE A 159 9490 7815 8455 -1055 -1925 530 C
ATOM 1265 CZ PHE A 159 -237.548 34.100 25.615 1.00 70.51 C
ANISOU 1265 CZ PHE A 159 9964 8184 8643 -1190 -2140 645 C
ATOM 1266 N THR A 160 -232.425 32.127 27.513 1.00 71.51 N
ANISOU 1266 N THR A 160 10142 8221 8807 -890 -1007 133 N
ATOM 1267 CA THR A 160 -232.099 33.069 28.582 1.00 69.30 C
ANISOU 1267 CA THR A 160 9688 7938 8705 -735 -988 213 C
ATOM 1268 C THR A 160 -230.874 33.899 28.220 1.00 76.76 C
ANISOU 1268 C THR A 160 10700 8891 9574 -733 -857 223 C
ATOM 1269 O THR A 160 -230.816 35.094 28.522 1.00 71.05 O
ANISOU 1269 O THR A 160 9907 8179 8910 -676 -917 331 O
ATOM 1270 CB THR A 160 -231.872 32.332 29.905 1.00 71.22 C
ANISOU 1270 CB THR A 160 9774 8139 9148 -602 -878 150 C
ATOM 1271 OG1 THR A 160 -230.713 31.497 29.804 1.00 74.37 O
ANISOU 1271 OG1 THR A 160 10233 8496 9527 -597 -667 25 O
ATOM 1272 CG2 THR A 160 -233.084 31.478 30.263 1.00 69.45 C
ANISOU 1272 CG2 THR A 160 9487 7903 8998 -617 -989 139 C
ATOM 1273 N TRP A 161 -229.891 33.282 27.560 1.00 73.47 N
ANISOU 1273 N TRP A 161 10415 8460 9039 -801 -667 105 N
ATOM 1274 CA ATRP A 161 -228.701 34.005 27.124 0.48 68.56 C
ANISOU 1274 CA ATRP A 161 9861 7846 8345 -821 -519 102 C
ATOM 1275 CA BTRP A 161 -228.711 34.035 27.156 0.52 68.37 C
ANISOU 1275 CA BTRP A 161 9830 7821 8325 -816 -523 106 C
ATOM 1276 C TRP A 161 -229.037 35.048 26.066 1.00 80.49 C
ANISOU 1276 C TRP A 161 11523 9403 9656 -952 -652 217 C
ATOM 1277 O TRP A 161 -228.376 36.092 25.985 1.00 79.40 O
ANISOU 1277 O TRP A 161 11389 9273 9507 -941 -609 286 O
ATOM 1278 CB ATRP A 161 -227.666 33.022 26.576 0.48 65.82 C
ANISOU 1278 CB ATRP A 161 9616 7463 7928 -878 -269 -69 C
ATOM 1279 CB BTRP A 161 -227.604 33.080 26.709 0.52 65.49 C
ANISOU 1279 CB BTRP A 161 9552 7419 7911 -859 -265 -63 C
ATOM 1280 CG ATRP A 161 -227.206 31.994 27.563 0.48 65.81 C
ANISOU 1280 CG ATRP A 161 9469 7395 8140 -749 -142 -170 C
ATOM 1281 CG BTRP A 161 -226.980 32.357 27.863 0.52 66.11 C
ANISOU 1281 CG BTRP A 161 9454 7436 8229 -705 -137 -138 C
ATOM 1282 CD1ATRP A 161 -227.492 31.948 28.898 0.48 63.50 C
ANISOU 1282 CD1ATRP A 161 8983 7083 8060 -601 -215 -116 C
ATOM 1283 CD1BTRP A 161 -227.490 31.277 28.522 0.52 62.32 C
ANISOU 1283 CD1BTRP A 161 8898 6913 7868 -648 -165 -189 C
ATOM 1284 CD2ATRP A 161 -226.372 30.860 27.293 0.48 64.12 C
ANISOU 1284 CD2ATRP A 161 9298 7115 7951 -764 80 -337 C
ATOM 1285 CD2BTRP A 161 -225.739 32.674 28.512 0.52 68.29 C
ANISOU 1285 CD2BTRP A 161 9608 7681 8659 -596 19 -154 C
ATOM 1286 NE1ATRP A 161 -226.887 30.860 29.474 0.48 64.69 N
ANISOU 1286 NE1ATRP A 161 9060 7161 8357 -527 -76 -221 N
ATOM 1287 NE1BTRP A 161 -226.644 30.898 29.536 0.52 66.11 N
ANISOU 1287 NE1BTRP A 161 9227 7335 8557 -513 -45 -227 N
ATOM 1288 CE2ATRP A 161 -226.193 30.175 28.510 0.48 67.53 C
ANISOU 1288 CE2ATRP A 161 9550 7483 8625 -615 105 -358 C
ATOM 1289 CE2BTRP A 161 -225.561 31.737 29.550 0.52 69.37 C
ANISOU 1289 CE2BTRP A 161 9603 7755 9000 -478 62 -207 C
ATOM 1290 CE3ATRP A 161 -225.758 30.360 26.140 0.48 61.36 C
ANISOU 1290 CE3ATRP A 161 9125 6746 7446 -896 267 -476 C
ATOM 1291 CE3BTRP A 161 -224.761 33.654 28.313 0.52 67.82 C
ANISOU 1291 CE3BTRP A 161 9544 7636 8588 -597 118 -123 C
ATOM 1292 CZ2ATRP A 161 -225.425 29.015 28.606 0.48 66.47 C
ANISOU 1292 CZ2ATRP A 161 9391 7255 8609 -580 291 -499 C
ATOM 1293 CZ2BTRP A 161 -224.444 31.750 30.386 0.52 61.80 C
ANISOU 1293 CZ2BTRP A 161 8497 6749 8233 -361 179 -224 C
ATOM 1294 CZ3ATRP A 161 -224.997 29.210 26.238 0.48 51.23 C
ANISOU 1294 CZ3ATRP A 161 7810 5368 6287 -858 479 -638 C
ATOM 1295 CZ3BTRP A 161 -223.654 33.666 29.144 0.52 60.25 C
ANISOU 1295 CZ3BTRP A 161 8429 6634 7831 -480 247 -152 C
ATOM 1296 CH2ATRP A 161 -224.837 28.551 27.461 0.48 54.64 C
ANISOU 1296 CH2ATRP A 161 8046 5727 6988 -694 479 -642 C
ATOM 1297 CH2BTRP A 161 -223.504 32.719 30.166 0.52 60.06 C
ANISOU 1297 CH2BTRP A 161 8263 6549 8007 -363 267 -198 C
ATOM 1298 N VAL A 162 -230.049 34.774 25.237 1.00 78.10 N
ANISOU 1298 N VAL A 162 11351 9126 9195 -1086 -824 247 N
ATOM 1299 CA VAL A 162 -230.451 35.739 24.219 1.00 76.99 C
ANISOU 1299 CA VAL A 162 11367 9025 8863 -1224 -994 382 C
ATOM 1300 C VAL A 162 -231.184 36.913 24.860 1.00 78.26 C
ANISOU 1300 C VAL A 162 11363 9178 9193 -1118 -1210 561 C
ATOM 1301 O VAL A 162 -230.949 38.075 24.510 1.00 82.83 O
ANISOU 1301 O VAL A 162 11990 9760 9724 -1145 -1267 682 O
ATOM 1302 CB VAL A 162 -231.303 35.051 23.135 1.00 77.67 C
ANISOU 1302 CB VAL A 162 11648 9138 8725 -1415 -1136 362 C
ATOM 1303 CG1 VAL A 162 -231.873 36.080 22.166 1.00 78.25 C
ANISOU 1303 CG1 VAL A 162 11870 9246 8615 -1558 -1376 540 C
ATOM 1304 CG2 VAL A 162 -230.478 34.015 22.387 1.00 65.19 C
ANISOU 1304 CG2 VAL A 162 10259 7554 6955 -1538 -890 170 C
ATOM 1305 N MET A 163 -232.069 36.634 25.821 1.00 77.07 N
ANISOU 1305 N MET A 163 11017 9009 9256 -1000 -1318 574 N
ATOM 1306 CA MET A 163 -232.776 37.716 26.501 1.00 80.66 C
ANISOU 1306 CA MET A 163 11298 9442 9906 -892 -1490 718 C
ATOM 1307 C MET A 163 -231.824 38.566 27.336 1.00 83.92 C
ANISOU 1307 C MET A 163 11602 9832 10453 -760 -1345 729 C
ATOM 1308 O MET A 163 -231.949 39.797 27.369 1.00 84.48 O
ANISOU 1308 O MET A 163 11633 9881 10585 -730 -1447 855 O
ATOM 1309 CB MET A 163 -233.894 37.145 27.374 1.00 74.11 C
ANISOU 1309 CB MET A 163 10284 8598 9277 -806 -1592 704 C
ATOM 1310 CG MET A 163 -235.065 36.582 26.589 1.00 76.46 C
ANISOU 1310 CG MET A 163 10650 8912 9489 -934 -1803 734 C
ATOM 1311 SD MET A 163 -235.768 37.813 25.476 1.00 81.86 S
ANISOU 1311 SD MET A 163 11430 9598 10074 -1049 -2102 941 S
ATOM 1312 CE MET A 163 -235.280 37.140 23.891 1.00 81.42 C
ANISOU 1312 CE MET A 163 11719 9594 9623 -1295 -2079 884 C
ATOM 1313 N ALA A 164 -230.868 37.929 28.016 1.00 71.81 N
ANISOU 1313 N ALA A 164 10015 8291 8977 -685 -1120 601 N
ATOM 1314 CA ALA A 164 -229.911 38.675 28.825 1.00 65.04 C
ANISOU 1314 CA ALA A 164 9055 7413 8245 -573 -992 605 C
ATOM 1315 C ALA A 164 -229.001 39.530 27.953 1.00 80.48 C
ANISOU 1315 C ALA A 164 11147 9375 10056 -659 -925 652 C
ATOM 1316 O ALA A 164 -228.720 40.685 28.291 1.00 82.20 O
ANISOU 1316 O ALA A 164 11305 9571 10358 -606 -945 737 O
ATOM 1317 CB ALA A 164 -229.093 37.717 29.688 1.00 63.37 C
ANISOU 1317 CB ALA A 164 8759 7188 8131 -487 -795 471 C
ATOM 1318 N LEU A 165 -228.533 38.985 26.826 1.00 79.77 N
ANISOU 1318 N LEU A 165 11252 9310 9746 -803 -832 590 N
ATOM 1319 CA LEU A 165 -227.785 39.798 25.874 1.00 67.43 C
ANISOU 1319 CA LEU A 165 9848 7758 8013 -918 -771 642 C
ATOM 1320 C LEU A 165 -228.641 40.921 25.302 1.00 75.41 C
ANISOU 1320 C LEU A 165 10928 8766 8959 -986 -1021 830 C
ATOM 1321 O LEU A 165 -228.126 42.013 25.036 1.00 76.43 O
ANISOU 1321 O LEU A 165 11102 8880 9058 -1014 -1013 924 O
ATOM 1322 CB LEU A 165 -227.237 38.918 24.747 1.00 67.89 C
ANISOU 1322 CB LEU A 165 10119 7844 7831 -1081 -612 524 C
ATOM 1323 CG LEU A 165 -226.021 38.051 25.095 1.00 80.26 C
ANISOU 1323 CG LEU A 165 11632 9391 9472 -1029 -317 344 C
ATOM 1324 CD1 LEU A 165 -225.699 37.116 23.948 1.00 83.99 C
ANISOU 1324 CD1 LEU A 165 12317 9877 9717 -1196 -164 209 C
ATOM 1325 CD2 LEU A 165 -224.809 38.903 25.442 1.00 72.18 C
ANISOU 1325 CD2 LEU A 165 10530 8350 8545 -973 -159 358 C
ATOM 1326 N ALA A 166 -229.943 40.680 25.112 1.00 77.90 N
ANISOU 1326 N ALA A 166 11242 9086 9269 -1013 -1253 894 N
ATOM 1327 CA ALA A 166 -230.832 41.720 24.602 1.00 73.89 C
ANISOU 1327 CA ALA A 166 10772 8559 8744 -1065 -1524 1087 C
ATOM 1328 C ALA A 166 -230.959 42.893 25.563 1.00 76.45 C
ANISOU 1328 C ALA A 166 10897 8822 9328 -908 -1587 1185 C
ATOM 1329 O ALA A 166 -231.397 43.973 25.152 1.00 77.95 O
ANISOU 1329 O ALA A 166 11116 8971 9530 -939 -1773 1352 O
ATOM 1330 CB ALA A 166 -232.216 41.139 24.316 1.00 65.46 C
ANISOU 1330 CB ALA A 166 9701 7502 7670 -1113 -1764 1126 C
ATOM 1331 N CYS A 167 -230.613 42.702 26.834 1.00 73.34 N
ANISOU 1331 N CYS A 167 10311 8413 9144 -746 -1445 1087 N
ATOM 1332 CA CYS A 167 -230.564 43.788 27.802 1.00 70.45 C
ANISOU 1332 CA CYS A 167 9775 7988 9006 -608 -1458 1146 C
ATOM 1333 C CYS A 167 -229.148 44.282 28.058 1.00 76.99 C
ANISOU 1333 C CYS A 167 10615 8809 9827 -588 -1248 1103 C
ATOM 1334 O CYS A 167 -228.919 45.494 28.084 1.00 70.17 O
ANISOU 1334 O CYS A 167 9740 7896 9024 -573 -1287 1203 O
ATOM 1335 CB CYS A 167 -231.193 43.351 29.129 1.00 65.56 C
ANISOU 1335 CB CYS A 167 8936 7353 8620 -458 -1454 1073 C
ATOM 1336 SG CYS A 167 -230.602 44.291 30.573 1.00 77.46 S
ANISOU 1336 SG CYS A 167 10261 8808 10364 -298 -1339 1050 S
ATOM 1337 N ALA A 168 -228.188 43.366 28.221 1.00 65.89 N
ANISOU 1337 N ALA A 168 9228 7444 8365 -590 -1031 959 N
ATOM 1338 CA ALA A 168 -226.864 43.745 28.698 1.00 67.66 C
ANISOU 1338 CA ALA A 168 9405 7656 8647 -546 -836 906 C
ATOM 1339 C ALA A 168 -225.991 44.356 27.607 1.00 78.39 C
ANISOU 1339 C ALA A 168 10935 9019 9829 -682 -752 953 C
ATOM 1340 O ALA A 168 -225.088 45.142 27.915 1.00 72.73 O
ANISOU 1340 O ALA A 168 10174 8276 9184 -658 -652 967 O
ATOM 1341 CB ALA A 168 -226.162 42.532 29.304 1.00 59.02 C
ANISOU 1341 CB ALA A 168 8242 6586 7599 -490 -650 745 C
ATOM 1342 N ALA A 169 -226.245 44.026 26.344 1.00 75.10 N
ANISOU 1342 N ALA A 169 10722 8637 9177 -840 -790 979 N
ATOM 1343 CA ALA A 169 -225.352 44.413 25.256 1.00 63.13 C
ANISOU 1343 CA ALA A 169 9398 7136 7454 -999 -667 999 C
ATOM 1344 C ALA A 169 -225.648 45.778 24.624 1.00 75.04 C
ANISOU 1344 C ALA A 169 11012 8607 8891 -1083 -833 1195 C
ATOM 1345 O ALA A 169 -224.692 46.499 24.307 1.00 79.41 O
ANISOU 1345 O ALA A 169 11630 9147 9396 -1148 -706 1224 O
ATOM 1346 CB ALA A 169 -225.354 43.329 24.173 1.00 54.34 C
ANISOU 1346 CB ALA A 169 8485 6076 6086 -1156 -589 908 C
ATOM 1347 N PRO A 170 -226.907 46.177 24.406 1.00 79.51 N
ANISOU 1347 N PRO A 170 11596 9150 9467 -1090 -1113 1337 N
ATOM 1348 CA PRO A 170 -227.177 47.487 23.750 1.00 73.14 C
ANISOU 1348 CA PRO A 170 10896 8289 8607 -1175 -1292 1544 C
ATOM 1349 C PRO A 170 -226.444 48.659 24.392 1.00 74.92 C
ANISOU 1349 C PRO A 170 11014 8445 9008 -1091 -1215 1591 C
ATOM 1350 O PRO A 170 -225.967 49.545 23.667 1.00 74.14 O
ANISOU 1350 O PRO A 170 11060 8317 8793 -1211 -1214 1706 O
ATOM 1351 CB PRO A 170 -228.701 47.635 23.877 1.00 73.12 C
ANISOU 1351 CB PRO A 170 10814 8247 8721 -1118 -1605 1663 C
ATOM 1352 CG PRO A 170 -229.190 46.230 23.823 1.00 68.35 C
ANISOU 1352 CG PRO A 170 10216 7713 8040 -1132 -1594 1535 C
ATOM 1353 CD PRO A 170 -228.155 45.394 24.545 1.00 69.99 C
ANISOU 1353 CD PRO A 170 10337 7960 8297 -1053 -1292 1327 C
ATOM 1354 N PRO A 171 -226.326 48.736 25.726 1.00 68.53 N
ANISOU 1354 N PRO A 171 9968 7604 8466 -905 -1154 1510 N
ATOM 1355 CA PRO A 171 -225.566 49.864 26.304 1.00 58.27 C
ANISOU 1355 CA PRO A 171 8584 6237 7318 -848 -1078 1544 C
ATOM 1356 C PRO A 171 -224.101 49.924 25.881 1.00 68.66 C
ANISOU 1356 C PRO A 171 9994 7583 8511 -950 -828 1484 C
ATOM 1357 O PRO A 171 -223.482 50.984 26.023 1.00 93.51 O
ANISOU 1357 O PRO A 171 13124 10672 11734 -956 -789 1548 O
ATOM 1358 CB PRO A 171 -225.695 49.642 27.818 1.00 73.14 C
ANISOU 1358 CB PRO A 171 10221 8104 9465 -654 -1039 1432 C
ATOM 1359 CG PRO A 171 -226.931 48.850 27.977 1.00 70.67 C
ANISOU 1359 CG PRO A 171 9855 7813 9181 -602 -1184 1415 C
ATOM 1360 CD PRO A 171 -226.989 47.950 26.786 1.00 61.11 C
ANISOU 1360 CD PRO A 171 8837 6677 7705 -752 -1180 1405 C
ATOM 1361 N LEU A 172 -223.516 48.832 25.384 1.00 75.54 N
ANISOU 1361 N LEU A 172 10951 8534 9215 -1030 -648 1356 N
ATOM 1362 CA LEU A 172 -222.150 48.878 24.873 1.00 71.12 C
ANISOU 1362 CA LEU A 172 10476 7998 8549 -1141 -393 1294 C
ATOM 1363 C LEU A 172 -222.071 49.437 23.460 1.00 79.19 C
ANISOU 1363 C LEU A 172 11766 9024 9299 -1360 -413 1419 C
ATOM 1364 O LEU A 172 -220.973 49.776 23.006 1.00 92.41 O
ANISOU 1364 O LEU A 172 13515 10701 10893 -1468 -208 1400 O
ATOM 1365 CB LEU A 172 -221.510 47.481 24.879 1.00 61.32 C
ANISOU 1365 CB LEU A 172 9213 6821 7263 -1142 -166 1093 C
ATOM 1366 CG LEU A 172 -221.473 46.623 26.147 1.00 66.90 C
ANISOU 1366 CG LEU A 172 9691 7534 8195 -956 -122 956 C
ATOM 1367 CD1 LEU A 172 -220.997 45.216 25.814 1.00 62.36 C
ANISOU 1367 CD1 LEU A 172 9149 7006 7540 -992 72 786 C
ATOM 1368 CD2 LEU A 172 -220.582 47.229 27.210 1.00 58.33 C
ANISOU 1368 CD2 LEU A 172 8413 6408 7341 -846 -35 931 C
ATOM 1369 N VAL A 173 -223.197 49.530 22.753 1.00 83.63 N
ANISOU 1369 N VAL A 173 12473 9585 9717 -1438 -656 1552 N
ATOM 1370 CA VAL A 173 -223.221 49.901 21.344 1.00 77.40 C
ANISOU 1370 CA VAL A 173 11977 8810 8621 -1673 -703 1679 C
ATOM 1371 C VAL A 173 -224.037 51.161 21.078 1.00 78.30 C
ANISOU 1371 C VAL A 173 12148 8838 8765 -1698 -1005 1930 C
ATOM 1372 O VAL A 173 -224.081 51.624 19.934 1.00 90.76 O
ANISOU 1372 O VAL A 173 13979 10414 10091 -1901 -1083 2075 O
ATOM 1373 CB VAL A 173 -223.729 48.729 20.473 1.00 81.79 C
ANISOU 1373 CB VAL A 173 12716 9449 8913 -1804 -720 1610 C
ATOM 1374 CG1 VAL A 173 -223.342 48.905 19.021 1.00101.07 C
ANISOU 1374 CG1 VAL A 173 15489 11927 10988 -2083 -653 1674 C
ATOM 1375 CG2 VAL A 173 -223.157 47.424 20.969 1.00 84.89 C
ANISOU 1375 CG2 VAL A 173 12994 9895 9365 -1724 -467 1361 C
ATOM 1376 N GLY A 174 -224.681 51.743 22.091 1.00 72.13 N
ANISOU 1376 N GLY A 174 11145 7976 8285 -1504 -1175 1989 N
ATOM 1377 CA GLY A 174 -225.317 53.030 21.880 1.00 77.25 C
ANISOU 1377 CA GLY A 174 11824 8514 9013 -1515 -1433 2221 C
ATOM 1378 C GLY A 174 -226.768 53.209 22.286 1.00 88.95 C
ANISOU 1378 C GLY A 174 13173 9930 10695 -1386 -1747 2324 C
ATOM 1379 O GLY A 174 -227.302 54.313 22.141 1.00 93.22 O
ANISOU 1379 O GLY A 174 13716 10356 11347 -1380 -1966 2520 O
ATOM 1380 N TRP A 175 -227.430 52.157 22.774 1.00 87.65 N
ANISOU 1380 N TRP A 175 12886 9823 10593 -1287 -1772 2200 N
ATOM 1381 CA TRP A 175 -228.777 52.271 23.332 1.00 74.69 C
ANISOU 1381 CA TRP A 175 11067 8117 9192 -1146 -2028 2265 C
ATOM 1382 C TRP A 175 -228.647 52.191 24.850 1.00 75.25 C
ANISOU 1382 C TRP A 175 10861 8165 9565 -926 -1889 2108 C
ATOM 1383 O TRP A 175 -228.319 51.132 25.395 1.00 74.76 O
ANISOU 1383 O TRP A 175 10728 8189 9488 -872 -1712 1922 O
ATOM 1384 CB TRP A 175 -229.701 51.182 22.791 1.00 81.63 C
ANISOU 1384 CB TRP A 175 12012 9073 9930 -1210 -2171 2249 C
ATOM 1385 CG TRP A 175 -231.164 51.515 22.917 1.00 84.71 C
ANISOU 1385 CG TRP A 175 12275 9383 10528 -1132 -2497 2388 C
ATOM 1386 CD1 TRP A 175 -231.706 52.747 23.131 1.00 78.61 C
ANISOU 1386 CD1 TRP A 175 11399 8470 10000 -1053 -2693 2558 C
ATOM 1387 CD2 TRP A 175 -232.267 50.598 22.845 1.00 86.49 C
ANISOU 1387 CD2 TRP A 175 12446 9652 10765 -1124 -2660 2364 C
ATOM 1388 NE1 TRP A 175 -233.076 52.659 23.191 1.00 86.09 N
ANISOU 1388 NE1 TRP A 175 12216 9369 11125 -990 -2965 2641 N
ATOM 1389 CE2 TRP A 175 -233.446 51.351 23.018 1.00 89.11 C
ANISOU 1389 CE2 TRP A 175 12625 9867 11364 -1037 -2953 2527 C
ATOM 1390 CE3 TRP A 175 -232.371 49.216 22.650 1.00 79.73 C
ANISOU 1390 CE3 TRP A 175 11646 8911 9736 -1183 -2584 2217 C
ATOM 1391 CZ2 TRP A 175 -234.712 50.769 23.001 1.00 88.54 C
ANISOU 1391 CZ2 TRP A 175 12448 9800 11394 -1011 -3172 2550 C
ATOM 1392 CZ3 TRP A 175 -233.630 48.640 22.632 1.00 77.97 C
ANISOU 1392 CZ3 TRP A 175 11337 8694 9596 -1164 -2805 2241 C
ATOM 1393 CH2 TRP A 175 -234.782 49.415 22.808 1.00 84.58 C
ANISOU 1393 CH2 TRP A 175 12012 9422 10703 -1081 -3096 2407 C
ATOM 1394 N SER A 176 -228.903 53.314 25.525 1.00 75.89 N
ANISOU 1394 N SER A 176 10797 8122 9915 -808 -1972 2185 N
ATOM 1395 CA SER A 176 -228.561 53.512 26.932 1.00 72.87 C
ANISOU 1395 CA SER A 176 10196 7706 9787 -635 -1819 2047 C
ATOM 1396 C SER A 176 -227.044 53.469 27.109 1.00 81.07 C
ANISOU 1396 C SER A 176 11281 8796 10727 -678 -1544 1936 C
ATOM 1397 O SER A 176 -226.297 53.618 26.135 1.00 73.91 O
ANISOU 1397 O SER A 176 10565 7917 9601 -835 -1478 1994 O
ATOM 1398 CB SER A 176 -229.252 52.477 27.825 1.00 63.71 C
ANISOU 1398 CB SER A 176 8863 6600 8744 -509 -1800 1899 C
ATOM 1399 OG SER A 176 -229.025 52.755 29.197 1.00 83.45 O
ANISOU 1399 OG SER A 176 11170 9059 11477 -358 -1677 1782 O
ATOM 1400 N ARG A 177 -226.575 53.264 28.338 1.00 64.74 N
ANISOU 1400 N ARG A 177 9041 6738 8820 -551 -1385 1779 N
ATOM 1401 CA ARG A 177 -225.146 53.296 28.611 1.00 59.00 C
ANISOU 1401 CA ARG A 177 8319 6044 8053 -579 -1149 1682 C
ATOM 1402 C ARG A 177 -224.911 52.760 30.014 1.00 66.31 C
ANISOU 1402 C ARG A 177 9053 6999 9144 -437 -1030 1510 C
ATOM 1403 O ARG A 177 -225.817 52.755 30.852 1.00 71.08 O
ANISOU 1403 O ARG A 177 9523 7567 9917 -318 -1122 1483 O
ATOM 1404 CB ARG A 177 -224.584 54.718 28.488 1.00 66.31 C
ANISOU 1404 CB ARG A 177 9280 6865 9049 -620 -1152 1792 C
ATOM 1405 CG ARG A 177 -225.108 55.653 29.560 1.00 65.49 C
ANISOU 1405 CG ARG A 177 9008 6640 9235 -478 -1238 1801 C
ATOM 1406 CD ARG A 177 -224.550 57.039 29.425 1.00 74.01 C
ANISOU 1406 CD ARG A 177 10127 7601 10393 -523 -1241 1905 C
ATOM 1407 NE ARG A 177 -225.093 57.930 30.443 1.00 81.95 N
ANISOU 1407 NE ARG A 177 10977 8475 11684 -390 -1313 1897 N
ATOM 1408 CZ ARG A 177 -224.588 59.123 30.724 1.00 82.31 C
ANISOU 1408 CZ ARG A 177 11009 8402 11864 -394 -1289 1936 C
ATOM 1409 NH1 ARG A 177 -223.525 59.556 30.064 1.00 71.21 N
ANISOU 1409 NH1 ARG A 177 9728 6997 10331 -526 -1199 1997 N
ATOM 1410 NH2 ARG A 177 -225.139 59.873 31.667 1.00 82.21 N
ANISOU 1410 NH2 ARG A 177 10858 8263 12115 -273 -1340 1905 N
ATOM 1411 N TYR A 178 -223.679 52.310 30.258 1.00 60.54 N
ANISOU 1411 N TYR A 178 8309 6327 8365 -459 -825 1397 N
ATOM 1412 CA TYR A 178 -223.243 51.950 31.600 1.00 57.24 C
ANISOU 1412 CA TYR A 178 7724 5926 8099 -346 -723 1256 C
ATOM 1413 C TYR A 178 -222.553 53.147 32.244 1.00 59.42 C
ANISOU 1413 C TYR A 178 7934 6121 8522 -326 -684 1268 C
ATOM 1414 O TYR A 178 -221.772 53.842 31.592 1.00 64.46 O
ANISOU 1414 O TYR A 178 8656 6731 9105 -423 -627 1333 O
ATOM 1415 CB TYR A 178 -222.295 50.747 31.575 1.00 63.24 C
ANISOU 1415 CB TYR A 178 8481 6781 8767 -371 -545 1130 C
ATOM 1416 CG TYR A 178 -222.976 49.455 31.214 1.00 70.90 C
ANISOU 1416 CG TYR A 178 9491 7820 9627 -372 -570 1083 C
ATOM 1417 CD1 TYR A 178 -223.855 48.839 32.100 1.00 73.62 C
ANISOU 1417 CD1 TYR A 178 9728 8176 10070 -264 -645 1028 C
ATOM 1418 CD2 TYR A 178 -222.748 48.851 29.988 1.00 77.13 C
ANISOU 1418 CD2 TYR A 178 10435 8661 10210 -494 -509 1086 C
ATOM 1419 CE1 TYR A 178 -224.489 47.657 31.769 1.00 66.91 C
ANISOU 1419 CE1 TYR A 178 8913 7382 9128 -273 -671 986 C
ATOM 1420 CE2 TYR A 178 -223.377 47.666 29.649 1.00 75.98 C
ANISOU 1420 CE2 TYR A 178 10334 8570 9963 -505 -534 1034 C
ATOM 1421 CZ TYR A 178 -224.244 47.076 30.542 1.00 71.74 C
ANISOU 1421 CZ TYR A 178 9678 8039 9541 -391 -621 988 C
ATOM 1422 OH TYR A 178 -224.865 45.899 30.201 1.00 74.91 O
ANISOU 1422 OH TYR A 178 10123 8488 9850 -410 -646 936 O
ATOM 1423 N ILE A 179 -222.876 53.397 33.511 1.00 47.57 N
ANISOU 1423 N ILE A 179 6294 4580 7199 -213 -711 1203 N
ATOM 1424 CA ILE A 179 -222.279 54.459 34.319 1.00 55.28 C
ANISOU 1424 CA ILE A 179 7200 5478 8325 -190 -675 1185 C
ATOM 1425 C ILE A 179 -222.262 53.985 35.766 1.00 54.74 C
ANISOU 1425 C ILE A 179 6999 5437 8363 -96 -634 1047 C
ATOM 1426 O ILE A 179 -223.050 53.099 36.132 1.00 65.59 O
ANISOU 1426 O ILE A 179 8333 6859 9728 -35 -668 997 O
ATOM 1427 CB ILE A 179 -223.052 55.792 34.211 1.00 66.35 C
ANISOU 1427 CB ILE A 179 8614 6743 9851 -173 -806 1295 C
ATOM 1428 CG1 ILE A 179 -224.497 55.635 34.692 1.00 69.21 C
ANISOU 1428 CG1 ILE A 179 8901 7073 10325 -69 -927 1286 C
ATOM 1429 CG2 ILE A 179 -222.997 56.387 32.801 1.00 47.12 C
ANISOU 1429 CG2 ILE A 179 6331 4268 7305 -286 -867 1458 C
ATOM 1430 CD1 ILE A 179 -225.248 56.970 34.761 1.00 64.47 C
ANISOU 1430 CD1 ILE A 179 8271 6311 9913 -28 -1044 1374 C
ATOM 1431 N PRO A 180 -221.394 54.526 36.620 1.00 58.31 N
ANISOU 1431 N PRO A 180 7387 5861 8907 -94 -568 987 N
ATOM 1432 CA PRO A 180 -221.505 54.222 38.050 1.00 51.46 C
ANISOU 1432 CA PRO A 180 6417 5007 8126 -22 -556 870 C
ATOM 1433 C PRO A 180 -222.882 54.609 38.561 1.00 64.36 C
ANISOU 1433 C PRO A 180 8018 6574 9861 54 -643 865 C
ATOM 1434 O PRO A 180 -223.512 55.547 38.067 1.00 59.62 O
ANISOU 1434 O PRO A 180 7444 5876 9334 59 -716 949 O
ATOM 1435 CB PRO A 180 -220.401 55.076 38.686 1.00 49.89 C
ANISOU 1435 CB PRO A 180 6183 4762 8010 -61 -503 834 C
ATOM 1436 CG PRO A 180 -219.401 55.269 37.588 1.00 49.67 C
ANISOU 1436 CG PRO A 180 6212 4745 7915 -153 -439 905 C
ATOM 1437 CD PRO A 180 -220.198 55.334 36.313 1.00 50.74 C
ANISOU 1437 CD PRO A 180 6454 4865 7961 -177 -497 1019 C
ATOM 1438 N GLU A 181 -223.369 53.848 39.532 1.00 60.92 N
ANISOU 1438 N GLU A 181 7522 6187 9440 111 -632 770 N
ATOM 1439 CA GLU A 181 -224.689 54.085 40.086 1.00 54.46 C
ANISOU 1439 CA GLU A 181 6653 5311 8727 180 -681 742 C
ATOM 1440 C GLU A 181 -224.590 54.207 41.599 1.00 55.81 C
ANISOU 1440 C GLU A 181 6770 5474 8961 200 -621 614 C
ATOM 1441 O GLU A 181 -223.602 53.800 42.215 1.00 53.52 O
ANISOU 1441 O GLU A 181 6480 5245 8608 165 -570 556 O
ATOM 1442 CB GLU A 181 -225.670 52.969 39.688 1.00 57.59 C
ANISOU 1442 CB GLU A 181 7043 5774 9063 212 -727 757 C
ATOM 1443 CG GLU A 181 -225.324 51.611 40.264 1.00 75.87 C
ANISOU 1443 CG GLU A 181 9345 8203 11279 212 -668 675 C
ATOM 1444 CD GLU A 181 -225.923 50.460 39.461 1.00 88.63 C
ANISOU 1444 CD GLU A 181 10987 9887 12799 212 -706 709 C
ATOM 1445 OE1 GLU A 181 -226.753 50.721 38.560 1.00105.85 O
ANISOU 1445 OE1 GLU A 181 13192 12035 14993 211 -794 792 O
ATOM 1446 OE2 GLU A 181 -225.558 49.295 39.730 1.00 72.18 O
ANISOU 1446 OE2 GLU A 181 8905 7885 10636 207 -660 657 O
ATOM 1447 N GLY A 182 -225.625 54.796 42.188 1.00 65.28 N
ANISOU 1447 N GLY A 182 7922 6589 10292 250 -628 569 N
ATOM 1448 CA GLY A 182 -225.701 54.958 43.625 1.00 55.39 C
ANISOU 1448 CA GLY A 182 6639 5322 9086 254 -556 435 C
ATOM 1449 C GLY A 182 -224.466 55.576 44.239 1.00 67.59 C
ANISOU 1449 C GLY A 182 8214 6851 10614 191 -517 387 C
ATOM 1450 O GLY A 182 -224.105 56.729 43.952 1.00 54.88 O
ANISOU 1450 O GLY A 182 6618 5141 9091 171 -525 418 O
ATOM 1451 N MET A 183 -223.797 54.801 45.087 1.00 55.18 N
ANISOU 1451 N MET A 183 6654 5375 8937 152 -487 319 N
ATOM 1452 CA MET A 183 -222.586 55.274 45.736 1.00 67.63 C
ANISOU 1452 CA MET A 183 8251 6948 10496 80 -473 276 C
ATOM 1453 C MET A 183 -221.380 55.237 44.806 1.00 60.46 C
ANISOU 1453 C MET A 183 7345 6070 9555 42 -494 367 C
ATOM 1454 O MET A 183 -220.260 55.482 45.262 1.00 66.31 O
ANISOU 1454 O MET A 183 8083 6821 10292 -22 -493 342 O
ATOM 1455 CB MET A 183 -222.336 54.470 47.013 1.00 68.58 C
ANISOU 1455 CB MET A 183 8384 7152 10521 42 -459 186 C
ATOM 1456 CG MET A 183 -223.328 54.812 48.123 1.00 59.53 C
ANISOU 1456 CG MET A 183 7255 5960 9404 42 -402 67 C
ATOM 1457 SD MET A 183 -223.269 53.727 49.574 1.00 72.21 S
ANISOU 1457 SD MET A 183 8909 7672 10857 -21 -388 -20 S
ATOM 1458 CE MET A 183 -221.573 53.897 50.117 1.00 77.81 C
ANISOU 1458 CE MET A 183 9649 8415 11502 -122 -459 -15 C
ATOM 1459 N GLN A 184 -221.600 54.947 43.519 1.00 49.97 N
ANISOU 1459 N GLN A 184 6025 4755 8205 68 -511 467 N
ATOM 1460 CA GLN A 184 -220.627 55.113 42.442 1.00 54.69 C
ANISOU 1460 CA GLN A 184 6641 5360 8779 21 -503 554 C
ATOM 1461 C GLN A 184 -219.530 54.051 42.459 1.00 61.10 C
ANISOU 1461 C GLN A 184 7424 6276 9515 -9 -474 543 C
ATOM 1462 O GLN A 184 -218.467 54.251 41.864 1.00 67.80 O
ANISOU 1462 O GLN A 184 8265 7127 10368 -63 -438 582 O
ATOM 1463 CB GLN A 184 -220.002 56.519 42.465 1.00 58.82 C
ANISOU 1463 CB GLN A 184 7176 5780 9395 -32 -496 567 C
ATOM 1464 CG GLN A 184 -221.018 57.667 42.465 1.00 51.58 C
ANISOU 1464 CG GLN A 184 6277 4728 8595 3 -524 577 C
ATOM 1465 CD GLN A 184 -221.840 57.729 41.190 1.00 64.45 C
ANISOU 1465 CD GLN A 184 7940 6324 10225 36 -575 700 C
ATOM 1466 OE1 GLN A 184 -221.332 58.116 40.135 1.00 57.61 O
ANISOU 1466 OE1 GLN A 184 7123 5435 9330 -16 -585 805 O
ATOM 1467 NE2 GLN A 184 -223.119 57.337 41.278 1.00 52.44 N
ANISOU 1467 NE2 GLN A 184 6394 4800 8731 110 -613 689 N
ATOM 1468 N CYS A 185 -219.762 52.914 43.113 1.00 56.91 N
ANISOU 1468 N CYS A 185 6871 5822 8932 22 -482 492 N
ATOM 1469 CA CYS A 185 -218.778 51.842 43.140 1.00 71.39 C
ANISOU 1469 CA CYS A 185 8664 7734 10729 7 -465 487 C
ATOM 1470 C CYS A 185 -219.138 50.672 42.241 1.00 75.77 C
ANISOU 1470 C CYS A 185 9233 8346 11211 41 -443 519 C
ATOM 1471 O CYS A 185 -218.264 49.852 41.945 1.00 76.68 O
ANISOU 1471 O CYS A 185 9311 8505 11319 30 -405 520 O
ATOM 1472 CB CYS A 185 -218.592 51.324 44.565 1.00 55.35 C
ANISOU 1472 CB CYS A 185 6603 5737 8690 2 -506 420 C
ATOM 1473 SG CYS A 185 -217.870 52.539 45.645 1.00 73.62 S
ANISOU 1473 SG CYS A 185 8911 7996 11067 -70 -536 369 S
ATOM 1474 N SER A 186 -220.401 50.565 41.835 1.00 77.31 N
ANISOU 1474 N SER A 186 9471 8535 11369 80 -466 538 N
ATOM 1475 CA SER A 186 -220.850 49.579 40.867 1.00 67.72 C
ANISOU 1475 CA SER A 186 8289 7367 10076 96 -456 569 C
ATOM 1476 C SER A 186 -221.347 50.323 39.637 1.00 73.04 C
ANISOU 1476 C SER A 186 9030 7999 10725 74 -472 648 C
ATOM 1477 O SER A 186 -221.785 51.475 39.730 1.00 72.88 O
ANISOU 1477 O SER A 186 9018 7904 10769 76 -512 678 O
ATOM 1478 CB SER A 186 -221.976 48.675 41.420 1.00 76.45 C
ANISOU 1478 CB SER A 186 9388 8504 11154 146 -492 533 C
ATOM 1479 OG SER A 186 -222.109 48.719 42.837 1.00 95.68 O
ANISOU 1479 OG SER A 186 11790 10938 13626 159 -507 471 O
ATOM 1480 N CYS A 187 -221.278 49.660 38.485 1.00 62.39 N
ANISOU 1480 N CYS A 187 7736 6689 9281 45 -445 684 N
ATOM 1481 CA CYS A 187 -221.749 50.231 37.231 1.00 53.14 C
ANISOU 1481 CA CYS A 187 6655 5487 8048 1 -479 775 C
ATOM 1482 C CYS A 187 -222.969 49.471 36.725 1.00 59.75 C
ANISOU 1482 C CYS A 187 7534 6354 8815 20 -549 795 C
ATOM 1483 O CYS A 187 -223.109 48.265 36.949 1.00 65.43 O
ANISOU 1483 O CYS A 187 8234 7131 9496 44 -526 735 O
ATOM 1484 CB CYS A 187 -220.640 50.228 36.175 1.00 51.95 C
ANISOU 1484 CB CYS A 187 6565 5355 7817 -86 -382 803 C
ATOM 1485 SG CYS A 187 -219.438 51.587 36.365 1.00 66.92 S
ANISOU 1485 SG CYS A 187 8434 7188 9805 -140 -327 827 S
ATOM 1486 N GLY A 188 -223.861 50.192 36.050 1.00 65.78 N
ANISOU 1486 N GLY A 188 8349 7067 9577 7 -649 886 N
ATOM 1487 CA GLY A 188 -225.103 49.597 35.599 1.00 51.96 C
ANISOU 1487 CA GLY A 188 6622 5335 7786 21 -746 915 C
ATOM 1488 C GLY A 188 -225.781 50.416 34.521 1.00 53.88 C
ANISOU 1488 C GLY A 188 6946 5522 8005 -25 -870 1047 C
ATOM 1489 O GLY A 188 -225.260 51.430 34.055 1.00 66.94 O
ANISOU 1489 O GLY A 188 8654 7121 9659 -74 -871 1123 O
ATOM 1490 N ILE A 189 -226.964 49.938 34.117 1.00 69.44 N
ANISOU 1490 N ILE A 189 8923 7502 9958 -17 -986 1084 N
ATOM 1491 CA ILE A 189 -227.787 50.657 33.157 1.00 64.36 C
ANISOU 1491 CA ILE A 189 8342 6798 9314 -57 -1152 1227 C
ATOM 1492 C ILE A 189 -228.108 52.028 33.727 1.00 61.19 C
ANISOU 1492 C ILE A 189 7855 6274 9121 8 -1210 1276 C
ATOM 1493 O ILE A 189 -228.300 52.193 34.938 1.00 78.69 O
ANISOU 1493 O ILE A 189 9943 8458 11495 99 -1157 1184 O
ATOM 1494 CB ILE A 189 -229.093 49.900 32.848 1.00 74.16 C
ANISOU 1494 CB ILE A 189 9563 8064 10550 -48 -1285 1248 C
ATOM 1495 CG1 ILE A 189 -228.830 48.442 32.462 1.00 82.75 C
ANISOU 1495 CG1 ILE A 189 10724 9262 11454 -103 -1212 1169 C
ATOM 1496 CG2 ILE A 189 -229.904 50.619 31.763 1.00 55.81 C
ANISOU 1496 CG2 ILE A 189 7308 5675 8222 -103 -1492 1418 C
ATOM 1497 CD1 ILE A 189 -228.398 48.257 31.048 1.00 90.28 C
ANISOU 1497 CD1 ILE A 189 11866 10255 12180 -241 -1226 1235 C
ATOM 1498 N ASP A 190 -228.191 53.016 32.843 1.00 59.77 N
ANISOU 1498 N ASP A 190 7756 6016 8939 -47 -1318 1422 N
ATOM 1499 CA ASP A 190 -228.440 54.400 33.239 1.00 67.03 C
ANISOU 1499 CA ASP A 190 8607 6792 10069 8 -1377 1481 C
ATOM 1500 C ASP A 190 -229.943 54.633 33.264 1.00 58.73 C
ANISOU 1500 C ASP A 190 7454 5658 9203 81 -1552 1545 C
ATOM 1501 O ASP A 190 -230.557 54.903 32.230 1.00 66.83 O
ANISOU 1501 O ASP A 190 8546 6641 10206 31 -1734 1700 O
ATOM 1502 CB ASP A 190 -227.738 55.354 32.280 1.00 57.37 C
ANISOU 1502 CB ASP A 190 7522 5511 8767 -93 -1409 1619 C
ATOM 1503 CG ASP A 190 -228.024 56.820 32.579 1.00 72.71 C
ANISOU 1503 CG ASP A 190 9405 7281 10941 -42 -1486 1697 C
ATOM 1504 OD1 ASP A 190 -228.545 57.150 33.667 1.00 76.74 O
ANISOU 1504 OD1 ASP A 190 9763 7719 11675 73 -1467 1609 O
ATOM 1505 OD2 ASP A 190 -227.700 57.651 31.710 1.00 72.74 O
ANISOU 1505 OD2 ASP A 190 9524 7214 10899 -126 -1556 1844 O
ATOM 1506 N TYR A 191 -230.539 54.523 34.451 1.00 62.10 N
ANISOU 1506 N TYR A 191 7719 6059 9816 191 -1499 1425 N
ATOM 1507 CA TYR A 191 -231.917 54.941 34.671 1.00 77.13 C
ANISOU 1507 CA TYR A 191 9482 7854 11968 276 -1628 1462 C
ATOM 1508 C TYR A 191 -232.010 56.322 35.299 1.00 72.25 C
ANISOU 1508 C TYR A 191 8775 7068 11609 349 -1613 1461 C
ATOM 1509 O TYR A 191 -233.113 56.779 35.592 1.00 77.08 O
ANISOU 1509 O TYR A 191 9243 7564 12478 434 -1692 1473 O
ATOM 1510 CB TYR A 191 -232.646 53.938 35.567 1.00 66.43 C
ANISOU 1510 CB TYR A 191 8001 6568 10672 341 -1559 1322 C
ATOM 1511 CG TYR A 191 -232.467 52.508 35.152 1.00 63.58 C
ANISOU 1511 CG TYR A 191 7720 6363 10073 276 -1540 1291 C
ATOM 1512 CD1 TYR A 191 -231.626 51.663 35.859 1.00 60.91 C
ANISOU 1512 CD1 TYR A 191 7407 6132 9603 268 -1365 1154 C
ATOM 1513 CD2 TYR A 191 -233.139 52.001 34.048 1.00 83.06 C
ANISOU 1513 CD2 TYR A 191 10242 8862 12455 218 -1708 1400 C
ATOM 1514 CE1 TYR A 191 -231.459 50.343 35.476 1.00 78.67 C
ANISOU 1514 CE1 TYR A 191 9726 8504 11662 214 -1342 1121 C
ATOM 1515 CE2 TYR A 191 -232.983 50.686 33.658 1.00 89.94 C
ANISOU 1515 CE2 TYR A 191 11195 9865 13113 152 -1681 1356 C
ATOM 1516 CZ TYR A 191 -232.143 49.860 34.373 1.00 86.24 C
ANISOU 1516 CZ TYR A 191 10743 9489 12536 156 -1490 1214 C
ATOM 1517 OH TYR A 191 -231.988 48.554 33.974 1.00 83.93 O
ANISOU 1517 OH TYR A 191 10527 9305 12057 96 -1459 1167 O
ATOM 1518 N TYR A 192 -230.881 56.990 35.515 1.00 79.28 N
ANISOU 1518 N TYR A 192 9736 7934 12454 316 -1509 1439 N
ATOM 1519 CA TYR A 192 -230.815 58.196 36.326 1.00 82.05 C
ANISOU 1519 CA TYR A 192 10010 8133 13034 378 -1450 1390 C
ATOM 1520 C TYR A 192 -230.706 59.462 35.495 1.00 72.77 C
ANISOU 1520 C TYR A 192 8896 6804 11951 348 -1577 1563 C
ATOM 1521 O TYR A 192 -230.697 60.557 36.058 1.00 67.40 O
ANISOU 1521 O TYR A 192 8155 5969 11486 398 -1543 1535 O
ATOM 1522 CB TYR A 192 -229.624 58.095 37.286 1.00 70.80 C
ANISOU 1522 CB TYR A 192 8612 6776 11512 355 -1251 1236 C
ATOM 1523 CG TYR A 192 -229.440 56.681 37.770 1.00 76.47 C
ANISOU 1523 CG TYR A 192 9327 7669 12061 347 -1155 1118 C
ATOM 1524 CD1 TYR A 192 -230.371 56.100 38.624 1.00 77.05 C
ANISOU 1524 CD1 TYR A 192 9285 7762 12229 417 -1118 1008 C
ATOM 1525 CD2 TYR A 192 -228.364 55.909 37.346 1.00 67.11 C
ANISOU 1525 CD2 TYR A 192 8248 6617 10632 266 -1098 1118 C
ATOM 1526 CE1 TYR A 192 -230.228 54.799 39.060 1.00 67.29 C
ANISOU 1526 CE1 TYR A 192 8053 6672 10841 403 -1041 915 C
ATOM 1527 CE2 TYR A 192 -228.217 54.605 37.777 1.00 88.09 C
ANISOU 1527 CE2 TYR A 192 10896 9413 13162 265 -1022 1019 C
ATOM 1528 CZ TYR A 192 -229.155 54.054 38.634 1.00 73.31 C
ANISOU 1528 CZ TYR A 192 8921 7556 11377 332 -1002 925 C
ATOM 1529 OH TYR A 192 -229.018 52.755 39.070 1.00 85.24 O
ANISOU 1529 OH TYR A 192 10432 9192 12764 325 -934 840 O
ATOM 1530 N THR A 193 -230.661 59.334 34.171 1.00 74.67 N
ANISOU 1530 N THR A 193 9264 7075 12033 259 -1724 1741 N
ATOM 1531 CA THR A 193 -230.230 60.373 33.276 1.00 62.07 C
ANISOU 1531 CA THR A 193 7787 5371 10428 185 -1823 1918 C
ATOM 1532 C THR A 193 -231.001 60.243 31.969 1.00 73.78 C
ANISOU 1532 C THR A 193 9346 6841 11844 127 -2066 2127 C
ATOM 1533 O THR A 193 -231.030 59.142 31.393 1.00 88.02 O
ANISOU 1533 O THR A 193 11232 8801 13411 58 -2087 2131 O
ATOM 1534 CB THR A 193 -228.725 60.236 33.021 1.00 66.70 C
ANISOU 1534 CB THR A 193 8525 6061 10758 68 -1676 1893 C
ATOM 1535 OG1 THR A 193 -227.981 60.895 34.053 1.00 74.16 O
ANISOU 1535 OG1 THR A 193 9412 6947 11820 102 -1518 1766 O
ATOM 1536 CG2 THR A 193 -228.344 60.763 31.657 1.00 54.17 C
ANISOU 1536 CG2 THR A 193 7120 4439 9024 -65 -1792 2103 C
ATOM 1537 N PRO A 194 -231.631 61.335 31.468 1.00 78.84 N
ANISOU 1537 N PRO A 194 9972 7293 12692 145 -2263 2307 N
ATOM 1538 CA PRO A 194 -232.321 61.309 30.172 1.00 68.15 C
ANISOU 1538 CA PRO A 194 8711 5916 11266 68 -2534 2539 C
ATOM 1539 C PRO A 194 -231.380 61.535 28.988 1.00 88.23 C
ANISOU 1539 C PRO A 194 11516 8503 13504 -115 -2570 2698 C
ATOM 1540 O PRO A 194 -231.651 62.349 28.105 1.00119.07 O
ANISOU 1540 O PRO A 194 15516 12283 17444 -180 -2781 2926 O
ATOM 1541 CB PRO A 194 -233.331 62.451 30.309 1.00 85.90 C
ANISOU 1541 CB PRO A 194 10806 7918 13914 179 -2718 2655 C
ATOM 1542 CG PRO A 194 -232.600 63.455 31.145 1.00 61.12 C
ANISOU 1542 CG PRO A 194 7629 4656 10936 231 -2541 2559 C
ATOM 1543 CD PRO A 194 -231.741 62.658 32.114 1.00 76.21 C
ANISOU 1543 CD PRO A 194 9531 6743 12684 236 -2251 2304 C
ATOM 1544 N HIS A 195 -230.253 60.818 28.984 1.00 95.85 N
ANISOU 1544 N HIS A 195 12598 9640 14181 -204 -2356 2578 N
ATOM 1545 CA HIS A 195 -229.208 60.976 27.975 1.00 79.89 C
ANISOU 1545 CA HIS A 195 10817 7673 11866 -385 -2315 2684 C
ATOM 1546 C HIS A 195 -229.777 60.780 26.578 1.00 82.65 C
ANISOU 1546 C HIS A 195 11344 8042 12016 -522 -2555 2899 C
ATOM 1547 O HIS A 195 -230.066 59.651 26.173 1.00102.81 O
ANISOU 1547 O HIS A 195 13951 10743 14368 -574 -2575 2858 O
ATOM 1548 CB HIS A 195 -228.070 59.982 28.230 1.00 75.94 C
ANISOU 1548 CB HIS A 195 10368 7364 11121 -440 -2044 2493 C
ATOM 1549 CG HIS A 195 -226.719 60.474 27.808 1.00 93.59 C
ANISOU 1549 CG HIS A 195 12754 9611 13196 -573 -1892 2520 C
ATOM 1550 ND1 HIS A 195 -225.988 59.876 26.802 1.00 96.81 N
ANISOU 1550 ND1 HIS A 195 13364 10148 13273 -746 -1809 2547 N
ATOM 1551 CD2 HIS A 195 -225.957 61.496 28.267 1.00 92.74 C
ANISOU 1551 CD2 HIS A 195 12619 9398 13220 -567 -1794 2513 C
ATOM 1552 CE1 HIS A 195 -224.840 60.513 26.654 1.00 73.76 C
ANISOU 1552 CE1 HIS A 195 10524 7204 10298 -839 -1662 2560 C
ATOM 1553 NE2 HIS A 195 -224.795 61.499 27.532 1.00 83.89 N
ANISOU 1553 NE2 HIS A 195 11670 8345 11857 -733 -1659 2544 N
ATOM 1554 N GLU A 196 -229.952 61.872 25.837 1.00 88.52 N
ANISOU 1554 N GLU A 196 12189 8633 12811 -592 -2750 3134 N
ATOM 1555 CA GLU A 196 -230.607 61.772 24.540 1.00 88.77 C
ANISOU 1555 CA GLU A 196 12394 8667 12669 -729 -3027 3365 C
ATOM 1556 C GLU A 196 -229.691 61.173 23.484 1.00 93.08 C
ANISOU 1556 C GLU A 196 13230 9378 12760 -959 -2923 3389 C
ATOM 1557 O GLU A 196 -230.175 60.603 22.499 1.00103.96 O
ANISOU 1557 O GLU A 196 14766 10832 13903 -1090 -3093 3498 O
ATOM 1558 CB GLU A 196 -231.104 63.147 24.091 1.00 90.74 C
ANISOU 1558 CB GLU A 196 12664 8683 13131 -734 -3290 3630 C
ATOM 1559 CG GLU A 196 -232.155 63.760 25.003 1.00 92.23 C
ANISOU 1559 CG GLU A 196 12550 8709 13785 -511 -3388 3585 C
ATOM 1560 CD GLU A 196 -232.697 65.077 24.461 1.00135.64 C
ANISOU 1560 CD GLU A 196 18021 14066 19451 -519 -3573 3735 C
ATOM 1561 OE1 GLU A 196 -232.485 65.372 23.262 1.00141.33 O
ANISOU 1561 OE1 GLU A 196 18968 14812 19921 -701 -3705 3918 O
ATOM 1562 OE2 GLU A 196 -233.333 65.824 25.234 1.00149.79 O
ANISOU 1562 OE2 GLU A 196 19571 15716 21625 -350 -3581 3666 O
ATOM 1563 N GLU A 197 -228.373 61.293 23.669 1.00 89.05 N
ANISOU 1563 N GLU A 197 12789 8921 12126 -1019 -2642 3280 N
ATOM 1564 CA GLU A 197 -227.438 60.770 22.679 1.00 86.86 C
ANISOU 1564 CA GLU A 197 12774 8788 11441 -1240 -2500 3285 C
ATOM 1565 C GLU A 197 -227.532 59.256 22.575 1.00 94.12 C
ANISOU 1565 C GLU A 197 13712 9902 12147 -1262 -2402 3116 C
ATOM 1566 O GLU A 197 -227.314 58.692 21.497 1.00105.53 O
ANISOU 1566 O GLU A 197 15396 11454 13246 -1457 -2397 3161 O
ATOM 1567 CB GLU A 197 -226.007 61.191 23.021 1.00 94.99 C
ANISOU 1567 CB GLU A 197 13822 9826 12445 -1280 -2201 3182 C
ATOM 1568 CG GLU A 197 -225.710 62.679 22.845 1.00112.54 C
ANISOU 1568 CG GLU A 197 16100 11863 14797 -1326 -2275 3367 C
ATOM 1569 CD GLU A 197 -226.221 63.540 23.992 1.00120.72 C
ANISOU 1569 CD GLU A 197 16884 12720 16264 -1109 -2350 3344 C
ATOM 1570 OE1 GLU A 197 -226.655 62.989 25.024 1.00116.01 O
ANISOU 1570 OE1 GLU A 197 16067 12158 15854 -929 -2299 3160 O
ATOM 1571 OE2 GLU A 197 -226.188 64.780 23.858 1.00136.07 O
ANISOU 1571 OE2 GLU A 197 18860 14481 18361 -1128 -2453 3508 O
ATOM 1572 N THR A 198 -227.863 58.583 23.678 1.00 78.47 N
ANISOU 1572 N THR A 198 11493 7962 10359 -1075 -2321 2919 N
ATOM 1573 CA THR A 198 -228.046 57.138 23.683 1.00 88.76 C
ANISOU 1573 CA THR A 198 12791 9429 11506 -1076 -2243 2760 C
ATOM 1574 C THR A 198 -229.501 56.718 23.868 1.00 93.11 C
ANISOU 1574 C THR A 198 13211 9959 12207 -975 -2489 2793 C
ATOM 1575 O THR A 198 -229.756 55.551 24.179 1.00 86.19 O
ANISOU 1575 O THR A 198 12269 9196 11284 -932 -2419 2637 O
ATOM 1576 CB THR A 198 -227.178 56.494 24.767 1.00 78.37 C
ANISOU 1576 CB THR A 198 11323 8196 10257 -968 -1936 2501 C
ATOM 1577 OG1 THR A 198 -227.322 57.213 25.998 1.00 86.38 O
ANISOU 1577 OG1 THR A 198 12110 9100 11611 -785 -1924 2451 O
ATOM 1578 CG2 THR A 198 -225.725 56.506 24.347 1.00 63.72 C
ANISOU 1578 CG2 THR A 198 9612 6404 8194 -1105 -1681 2447 C
ATOM 1579 N ASN A 199 -230.456 57.634 23.689 1.00 95.32 N
ANISOU 1579 N ASN A 199 13442 10088 12688 -935 -2773 2992 N
ATOM 1580 CA ASN A 199 -231.887 57.329 23.751 1.00 85.69 C
ANISOU 1580 CA ASN A 199 12086 8831 11639 -852 -3033 3050 C
ATOM 1581 C ASN A 199 -232.244 56.523 25.004 1.00 82.37 C
ANISOU 1581 C ASN A 199 11411 8465 11420 -667 -2890 2817 C
ATOM 1582 O ASN A 199 -232.834 55.443 24.941 1.00 85.04 O
ANISOU 1582 O ASN A 199 11723 8904 11685 -672 -2929 2743 O
ATOM 1583 CB ASN A 199 -232.328 56.601 22.484 1.00 81.76 C
ANISOU 1583 CB ASN A 199 11808 8432 10825 -1042 -3220 3161 C
ATOM 1584 CG ASN A 199 -232.259 57.485 21.264 1.00 93.64 C
ANISOU 1584 CG ASN A 199 13560 9861 12159 -1228 -3433 3432 C
ATOM 1585 OD1 ASN A 199 -232.895 58.536 21.214 1.00117.18 O
ANISOU 1585 OD1 ASN A 199 16469 12669 15384 -1175 -3678 3631 O
ATOM 1586 ND2 ASN A 199 -231.467 57.079 20.281 1.00 94.99 N
ANISOU 1586 ND2 ASN A 199 14026 10150 11915 -1452 -3330 3442 N
ATOM 1587 N ASN A 200 -231.878 57.087 26.158 1.00 80.52 N
ANISOU 1587 N ASN A 200 11000 8156 11437 -517 -2724 2703 N
ATOM 1588 CA ASN A 200 -232.091 56.406 27.431 1.00 76.41 C
ANISOU 1588 CA ASN A 200 10261 7683 11086 -359 -2562 2481 C
ATOM 1589 C ASN A 200 -233.572 56.144 27.701 1.00 76.32 C
ANISOU 1589 C ASN A 200 10065 7624 11311 -256 -2758 2503 C
ATOM 1590 O ASN A 200 -233.930 55.110 28.278 1.00 99.72 O
ANISOU 1590 O ASN A 200 12924 10683 14284 -199 -2674 2349 O
ATOM 1591 CB ASN A 200 -231.478 57.227 28.568 1.00 65.83 C
ANISOU 1591 CB ASN A 200 8791 6255 9966 -241 -2380 2377 C
ATOM 1592 CG ASN A 200 -229.965 57.099 28.632 1.00 77.95 C
ANISOU 1592 CG ASN A 200 10445 7879 11292 -318 -2129 2278 C
ATOM 1593 OD1 ASN A 200 -229.310 56.750 27.647 1.00 75.52 O
ANISOU 1593 OD1 ASN A 200 10340 7659 10694 -473 -2098 2330 O
ATOM 1594 ND2 ASN A 200 -229.403 57.379 29.802 1.00 72.92 N
ANISOU 1594 ND2 ASN A 200 9681 7217 10807 -218 -1944 2129 N
ATOM 1595 N GLU A 201 -234.445 57.067 27.294 1.00 81.47 N
ANISOU 1595 N GLU A 201 10664 8118 12172 -234 -3020 2697 N
ATOM 1596 CA GLU A 201 -235.865 56.948 27.614 1.00 85.71 C
ANISOU 1596 CA GLU A 201 10980 8582 13004 -122 -3202 2719 C
ATOM 1597 C GLU A 201 -236.460 55.675 27.027 1.00 83.19 C
ANISOU 1597 C GLU A 201 10713 8405 12491 -208 -3311 2712 C
ATOM 1598 O GLU A 201 -237.079 54.878 27.741 1.00 82.50 O
ANISOU 1598 O GLU A 201 10454 8369 12523 -120 -3248 2568 O
ATOM 1599 CB GLU A 201 -236.610 58.180 27.103 1.00 93.63 C
ANISOU 1599 CB GLU A 201 11932 9377 14265 -100 -3492 2959 C
ATOM 1600 CG GLU A 201 -238.089 58.197 27.419 1.00111.18 C
ANISOU 1600 CG GLU A 201 13891 11494 16858 25 -3688 2993 C
ATOM 1601 CD GLU A 201 -238.764 59.462 26.934 1.00125.68 C
ANISOU 1601 CD GLU A 201 15651 13180 18920 28 -3875 3134 C
ATOM 1602 OE1 GLU A 201 -238.047 60.418 26.565 1.00130.72 O
ANISOU 1602 OE1 GLU A 201 16427 13748 19495 -26 -3868 3230 O
ATOM 1603 OE2 GLU A 201 -240.012 59.500 26.920 1.00135.58 O
ANISOU 1603 OE2 GLU A 201 16705 14388 20420 77 -4019 3142 O
ATOM 1604 N SER A 202 -236.267 55.462 25.724 1.00 74.01 N
ANISOU 1604 N SER A 202 9800 7307 11015 -394 -3466 2862 N
ATOM 1605 CA SER A 202 -236.855 54.305 25.064 1.00 74.01 C
ANISOU 1605 CA SER A 202 9874 7430 10817 -499 -3594 2863 C
ATOM 1606 C SER A 202 -236.279 52.996 25.594 1.00 82.69 C
ANISOU 1606 C SER A 202 10989 8700 11728 -499 -3308 2614 C
ATOM 1607 O SER A 202 -236.955 51.962 25.547 1.00 81.76 O
ANISOU 1607 O SER A 202 10828 8662 11574 -516 -3364 2550 O
ATOM 1608 CB SER A 202 -236.651 54.409 23.555 1.00 77.33 C
ANISOU 1608 CB SER A 202 10599 7883 10900 -725 -3797 3066 C
ATOM 1609 OG SER A 202 -235.272 54.421 23.234 1.00 94.98 O
ANISOU 1609 OG SER A 202 13064 10198 12825 -838 -3562 3011 O
ATOM 1610 N PHE A 203 -235.047 53.017 26.113 1.00 72.81 N
ANISOU 1610 N PHE A 203 9791 7496 10377 -479 -3012 2475 N
ATOM 1611 CA PHE A 203 -234.493 51.803 26.709 1.00 75.33 C
ANISOU 1611 CA PHE A 203 10100 7954 10567 -460 -2752 2247 C
ATOM 1612 C PHE A 203 -235.123 51.511 28.066 1.00 68.25 C
ANISOU 1612 C PHE A 203 8930 7033 9968 -281 -2666 2102 C
ATOM 1613 O PHE A 203 -235.337 50.346 28.414 1.00 73.50 O
ANISOU 1613 O PHE A 203 9552 7795 10580 -270 -2583 1967 O
ATOM 1614 CB PHE A 203 -232.970 51.908 26.842 1.00 68.19 C
ANISOU 1614 CB PHE A 203 9318 7101 9490 -498 -2479 2154 C
ATOM 1615 CG PHE A 203 -232.308 50.599 27.189 1.00 59.88 C
ANISOU 1615 CG PHE A 203 8293 6186 8274 -509 -2242 1950 C
ATOM 1616 CD1 PHE A 203 -232.001 49.681 26.197 1.00 69.50 C
ANISOU 1616 CD1 PHE A 203 9715 7510 9181 -666 -2219 1930 C
ATOM 1617 CD2 PHE A 203 -232.014 50.277 28.503 1.00 70.49 C
ANISOU 1617 CD2 PHE A 203 9463 7543 9776 -369 -2047 1779 C
ATOM 1618 CE1 PHE A 203 -231.401 48.471 26.507 1.00 65.57 C
ANISOU 1618 CE1 PHE A 203 9231 7116 8567 -667 -2001 1742 C
ATOM 1619 CE2 PHE A 203 -231.410 49.070 28.822 1.00 75.71 C
ANISOU 1619 CE2 PHE A 203 10144 8313 10308 -377 -1851 1611 C
ATOM 1620 CZ PHE A 203 -231.104 48.166 27.822 1.00 73.05 C
ANISOU 1620 CZ PHE A 203 9993 8067 9695 -517 -1827 1592 C
ATOM 1621 N VAL A 204 -235.407 52.550 28.856 1.00 79.31 N
ANISOU 1621 N VAL A 204 10154 8301 11678 -147 -2671 2120 N
ATOM 1622 CA VAL A 204 -236.096 52.350 30.131 1.00 86.39 C
ANISOU 1622 CA VAL A 204 10801 9166 12859 8 -2583 1983 C
ATOM 1623 C VAL A 204 -237.488 51.770 29.900 1.00 87.82 C
ANISOU 1623 C VAL A 204 10859 9344 13165 15 -2783 2026 C
ATOM 1624 O VAL A 204 -237.932 50.866 30.620 1.00 73.46 O
ANISOU 1624 O VAL A 204 8919 7587 11406 66 -2685 1884 O
ATOM 1625 CB VAL A 204 -236.156 53.676 30.912 1.00 77.31 C
ANISOU 1625 CB VAL A 204 9502 7854 12017 132 -2550 1993 C
ATOM 1626 CG1 VAL A 204 -237.129 53.571 32.075 1.00 77.91 C
ANISOU 1626 CG1 VAL A 204 9318 7876 12409 274 -2492 1872 C
ATOM 1627 CG2 VAL A 204 -234.770 54.050 31.409 1.00 77.01 C
ANISOU 1627 CG2 VAL A 204 9553 7838 11869 130 -2316 1902 C
ATOM 1628 N ILE A 205 -238.198 52.283 28.894 1.00 70.80 N
ANISOU 1628 N ILE A 205 8734 7113 11055 -44 -3077 2231 N
ATOM 1629 CA ILE A 205 -239.504 51.732 28.549 1.00 75.50 C
ANISOU 1629 CA ILE A 205 9216 7706 11765 -57 -3303 2291 C
ATOM 1630 C ILE A 205 -239.357 50.293 28.070 1.00 87.10 C
ANISOU 1630 C ILE A 205 10833 9346 12916 -182 -3269 2210 C
ATOM 1631 O ILE A 205 -240.118 49.401 28.468 1.00 86.93 O
ANISOU 1631 O ILE A 205 10678 9369 12981 -154 -3267 2118 O
ATOM 1632 CB ILE A 205 -240.186 52.610 27.489 1.00 61.65 C
ANISOU 1632 CB ILE A 205 7488 5832 10106 -113 -3657 2552 C
ATOM 1633 CG1 ILE A 205 -240.348 54.034 28.014 1.00 65.21 C
ANISOU 1633 CG1 ILE A 205 7775 6087 10915 24 -3679 2623 C
ATOM 1634 CG2 ILE A 205 -241.534 52.013 27.061 1.00 65.62 C
ANISOU 1634 CG2 ILE A 205 7869 6335 10729 -143 -3925 2628 C
ATOM 1635 CD1 ILE A 205 -240.939 54.966 26.998 1.00 65.66 C
ANISOU 1635 CD1 ILE A 205 7859 6003 11087 -25 -4036 2899 C
ATOM 1636 N TYR A 206 -238.371 50.048 27.204 1.00 77.24 N
ANISOU 1636 N TYR A 206 9862 8186 11301 -328 -3229 2237 N
ATOM 1637 CA TYR A 206 -238.111 48.691 26.739 1.00 74.92 C
ANISOU 1637 CA TYR A 206 9725 8040 10701 -450 -3162 2138 C
ATOM 1638 C TYR A 206 -237.811 47.759 27.905 1.00 70.30 C
ANISOU 1638 C TYR A 206 9025 7526 10159 -353 -2882 1908 C
ATOM 1639 O TYR A 206 -238.291 46.620 27.938 1.00 80.89 O
ANISOU 1639 O TYR A 206 10344 8940 11449 -385 -2881 1822 O
ATOM 1640 CB TYR A 206 -236.959 48.695 25.734 1.00 76.61 C
ANISOU 1640 CB TYR A 206 10247 8323 10539 -613 -3099 2176 C
ATOM 1641 CG TYR A 206 -236.265 47.364 25.602 1.00 79.42 C
ANISOU 1641 CG TYR A 206 10745 8818 10615 -697 -2891 2002 C
ATOM 1642 CD1 TYR A 206 -236.872 46.304 24.945 1.00 76.98 C
ANISOU 1642 CD1 TYR A 206 10520 8581 10148 -814 -3007 1984 C
ATOM 1643 CD2 TYR A 206 -234.997 47.166 26.135 1.00 85.12 C
ANISOU 1643 CD2 TYR A 206 11508 9586 11248 -661 -2583 1855 C
ATOM 1644 CE1 TYR A 206 -236.238 45.078 24.826 1.00 80.68 C
ANISOU 1644 CE1 TYR A 206 11117 9156 10384 -887 -2806 1814 C
ATOM 1645 CE2 TYR A 206 -234.353 45.945 26.022 1.00 79.92 C
ANISOU 1645 CE2 TYR A 206 10960 9031 10374 -726 -2392 1696 C
ATOM 1646 CZ TYR A 206 -234.978 44.905 25.365 1.00 81.27 C
ANISOU 1646 CZ TYR A 206 11218 9263 10396 -837 -2496 1672 C
ATOM 1647 OH TYR A 206 -234.342 43.688 25.250 1.00 77.91 O
ANISOU 1647 OH TYR A 206 10901 8922 9778 -898 -2297 1506 O
ATOM 1648 N MET A 207 -237.035 48.230 28.883 1.00 73.86 N
ANISOU 1648 N MET A 207 9406 7951 10707 -243 -2655 1813 N
ATOM 1649 CA MET A 207 -236.749 47.412 30.059 1.00 73.23 C
ANISOU 1649 CA MET A 207 9222 7929 10672 -156 -2410 1614 C
ATOM 1650 C MET A 207 -237.998 47.181 30.890 1.00 70.48 C
ANISOU 1650 C MET A 207 8630 7540 10610 -56 -2458 1568 C
ATOM 1651 O MET A 207 -238.221 46.074 31.392 1.00 79.41 O
ANISOU 1651 O MET A 207 9714 8741 11719 -51 -2360 1445 O
ATOM 1652 CB MET A 207 -235.678 48.074 30.917 1.00 56.18 C
ANISOU 1652 CB MET A 207 7044 5743 8557 -75 -2192 1539 C
ATOM 1653 CG MET A 207 -234.292 47.905 30.376 1.00 71.33 C
ANISOU 1653 CG MET A 207 9172 7732 10200 -166 -2057 1515 C
ATOM 1654 SD MET A 207 -233.779 46.189 30.442 1.00 72.16 S
ANISOU 1654 SD MET A 207 9357 7970 10092 -219 -1886 1350 S
ATOM 1655 CE MET A 207 -233.701 45.919 32.216 1.00 50.77 C
ANISOU 1655 CE MET A 207 6445 5255 7592 -66 -1695 1193 C
ATOM 1656 N PHE A 208 -238.811 48.224 31.062 1.00 70.78 N
ANISOU 1656 N PHE A 208 8506 7454 10935 23 -2595 1664 N
ATOM 1657 CA PHE A 208 -240.004 48.106 31.887 1.00 66.07 C
ANISOU 1657 CA PHE A 208 7653 6803 10647 122 -2612 1611 C
ATOM 1658 C PHE A 208 -240.966 47.076 31.318 1.00 75.13 C
ANISOU 1658 C PHE A 208 8775 8006 11763 43 -2776 1635 C
ATOM 1659 O PHE A 208 -241.541 46.275 32.064 1.00 72.35 O
ANISOU 1659 O PHE A 208 8287 7688 11515 79 -2682 1517 O
ATOM 1660 CB PHE A 208 -240.693 49.461 32.004 1.00 67.81 C
ANISOU 1660 CB PHE A 208 7703 6859 11204 215 -2744 1720 C
ATOM 1661 CG PHE A 208 -241.837 49.470 32.967 1.00 67.78 C
ANISOU 1661 CG PHE A 208 7414 6782 11557 327 -2705 1639 C
ATOM 1662 CD1 PHE A 208 -241.602 49.512 34.331 1.00 79.09 C
ANISOU 1662 CD1 PHE A 208 8744 8208 13100 421 -2430 1462 C
ATOM 1663 CD2 PHE A 208 -243.143 49.434 32.514 1.00 70.96 C
ANISOU 1663 CD2 PHE A 208 7653 7123 12185 328 -2942 1739 C
ATOM 1664 CE1 PHE A 208 -242.651 49.519 35.230 1.00 75.46 C
ANISOU 1664 CE1 PHE A 208 8032 7681 12958 508 -2361 1373 C
ATOM 1665 CE2 PHE A 208 -244.199 49.444 33.410 1.00 79.89 C
ANISOU 1665 CE2 PHE A 208 8502 8181 13670 428 -2880 1653 C
ATOM 1666 CZ PHE A 208 -243.951 49.484 34.770 1.00 78.05 C
ANISOU 1666 CZ PHE A 208 8180 7944 13532 516 -2574 1463 C
ATOM 1667 N VAL A 209 -241.142 47.071 29.997 1.00 70.99 N
ANISOU 1667 N VAL A 209 8395 7495 11083 -79 -3023 1787 N
ATOM 1668 CA VAL A 209 -242.117 46.182 29.380 1.00 75.31 C
ANISOU 1668 CA VAL A 209 8922 8086 11608 -170 -3218 1824 C
ATOM 1669 C VAL A 209 -241.550 44.774 29.224 1.00 91.56 C
ANISOU 1669 C VAL A 209 11151 10284 13353 -271 -3077 1691 C
ATOM 1670 O VAL A 209 -242.139 43.795 29.697 1.00 85.29 O
ANISOU 1670 O VAL A 209 10253 9530 12623 -266 -3027 1588 O
ATOM 1671 CB VAL A 209 -242.579 46.750 28.029 1.00 76.49 C
ANISOU 1671 CB VAL A 209 9168 8188 11707 -280 -3567 2049 C
ATOM 1672 CG1 VAL A 209 -243.539 45.781 27.370 1.00 69.40 C
ANISOU 1672 CG1 VAL A 209 8265 7343 10761 -395 -3782 2081 C
ATOM 1673 CG2 VAL A 209 -243.222 48.134 28.206 1.00 69.13 C
ANISOU 1673 CG2 VAL A 209 8036 7088 11141 -166 -3726 2190 C
ATOM 1674 N VAL A 210 -240.395 44.654 28.570 1.00 87.15 N
ANISOU 1674 N VAL A 210 10854 9790 12470 -365 -2997 1687 N
ATOM 1675 CA VAL A 210 -239.894 43.347 28.157 1.00 70.73 C
ANISOU 1675 CA VAL A 210 8957 7824 10095 -481 -2897 1578 C
ATOM 1676 C VAL A 210 -239.207 42.617 29.307 1.00 80.30 C
ANISOU 1676 C VAL A 210 10117 9079 11313 -392 -2587 1385 C
ATOM 1677 O VAL A 210 -239.327 41.393 29.441 1.00 85.41 O
ANISOU 1677 O VAL A 210 10783 9786 11884 -432 -2514 1275 O
ATOM 1678 CB VAL A 210 -238.960 43.517 26.946 1.00 72.38 C
ANISOU 1678 CB VAL A 210 9461 8074 9964 -629 -2921 1644 C
ATOM 1679 CG1 VAL A 210 -238.100 42.277 26.744 1.00 71.53 C
ANISOU 1679 CG1 VAL A 210 9533 8066 9580 -715 -2714 1485 C
ATOM 1680 CG2 VAL A 210 -239.780 43.820 25.698 1.00 57.42 C
ANISOU 1680 CG2 VAL A 210 7662 6161 7995 -769 -3262 1828 C
ATOM 1681 N HIS A 211 -238.481 43.337 30.157 1.00 70.11 N
ANISOU 1681 N HIS A 211 8767 7755 10118 -279 -2413 1347 N
ATOM 1682 CA HIS A 211 -237.667 42.712 31.191 1.00 61.80 C
ANISOU 1682 CA HIS A 211 7696 6744 9041 -213 -2141 1186 C
ATOM 1683 C HIS A 211 -238.217 42.946 32.587 1.00 62.86 C
ANISOU 1683 C HIS A 211 7599 6832 9453 -78 -2050 1121 C
ATOM 1684 O HIS A 211 -237.488 42.767 33.571 1.00 71.22 O
ANISOU 1684 O HIS A 211 8640 7908 10513 -15 -1841 1014 O
ATOM 1685 CB HIS A 211 -236.223 43.217 31.108 1.00 70.82 C
ANISOU 1685 CB HIS A 211 8976 7899 10036 -213 -1988 1172 C
ATOM 1686 CG HIS A 211 -235.552 42.914 29.804 1.00 69.98 C
ANISOU 1686 CG HIS A 211 9108 7842 9638 -357 -2014 1206 C
ATOM 1687 ND1 HIS A 211 -234.758 41.804 29.615 1.00 64.74 N
ANISOU 1687 ND1 HIS A 211 8571 7247 8780 -418 -1853 1086 N
ATOM 1688 CD2 HIS A 211 -235.569 43.571 28.619 1.00 75.42 C
ANISOU 1688 CD2 HIS A 211 9942 8519 10196 -463 -2175 1342 C
ATOM 1689 CE1 HIS A 211 -234.307 41.794 28.373 1.00 64.70 C
ANISOU 1689 CE1 HIS A 211 8778 7272 8535 -556 -1890 1130 C
ATOM 1690 NE2 HIS A 211 -234.788 42.852 27.746 1.00 57.64 N
ANISOU 1690 NE2 HIS A 211 7910 6335 7656 -595 -2089 1290 N
ATOM 1691 N PHE A 212 -239.478 43.343 32.700 1.00 65.75 N
ANISOU 1691 N PHE A 212 7790 7136 10058 -41 -2200 1182 N
ATOM 1692 CA PHE A 212 -240.074 43.561 34.009 1.00 71.09 C
ANISOU 1692 CA PHE A 212 8247 7763 11002 73 -2088 1104 C
ATOM 1693 C PHE A 212 -241.543 43.144 33.992 1.00 77.74 C
ANISOU 1693 C PHE A 212 8912 8580 12044 65 -2225 1122 C
ATOM 1694 O PHE A 212 -241.951 42.305 34.801 1.00 71.87 O
ANISOU 1694 O PHE A 212 8076 7867 11363 77 -2104 1014 O
ATOM 1695 CB PHE A 212 -239.893 45.021 34.427 1.00 61.93 C
ANISOU 1695 CB PHE A 212 7006 6505 10019 168 -2067 1147 C
ATOM 1696 CG PHE A 212 -240.328 45.318 35.836 1.00 74.83 C
ANISOU 1696 CG PHE A 212 8446 8087 11899 273 -1903 1039 C
ATOM 1697 CD1 PHE A 212 -239.646 44.781 36.912 1.00 61.63 C
ANISOU 1697 CD1 PHE A 212 6806 6472 10140 293 -1670 900 C
ATOM 1698 CD2 PHE A 212 -241.405 46.165 36.083 1.00 75.23 C
ANISOU 1698 CD2 PHE A 212 8287 8024 12273 347 -1982 1077 C
ATOM 1699 CE1 PHE A 212 -240.036 45.064 38.210 1.00 67.52 C
ANISOU 1699 CE1 PHE A 212 7403 7175 11076 365 -1511 796 C
ATOM 1700 CE2 PHE A 212 -241.800 46.450 37.376 1.00 72.95 C
ANISOU 1700 CE2 PHE A 212 7831 7685 12203 431 -1800 956 C
ATOM 1701 CZ PHE A 212 -241.115 45.900 38.441 1.00 76.71 C
ANISOU 1701 CZ PHE A 212 8367 8230 12549 431 -1561 814 C
ATOM 1702 N ILE A 213 -242.338 43.695 33.066 1.00 64.88 N
ANISOU 1702 N ILE A 213 7236 6896 10520 34 -2485 1266 N
ATOM 1703 CA ILE A 213 -243.753 43.328 32.989 1.00 75.95 C
ANISOU 1703 CA ILE A 213 8448 8269 12142 21 -2640 1294 C
ATOM 1704 C ILE A 213 -243.913 41.895 32.483 1.00 82.52 C
ANISOU 1704 C ILE A 213 9387 9199 12769 -103 -2682 1251 C
ATOM 1705 O ILE A 213 -244.555 41.063 33.132 1.00 86.92 O
ANISOU 1705 O ILE A 213 9818 9775 13432 -100 -2601 1158 O
ATOM 1706 CB ILE A 213 -244.540 44.310 32.103 1.00 71.64 C
ANISOU 1706 CB ILE A 213 7817 7625 11779 18 -2943 1479 C
ATOM 1707 CG1 ILE A 213 -244.587 45.714 32.713 1.00 76.16 C
ANISOU 1707 CG1 ILE A 213 8236 8068 12633 155 -2897 1509 C
ATOM 1708 CG2 ILE A 213 -245.958 43.800 31.910 1.00 63.16 C
ANISOU 1708 CG2 ILE A 213 6547 6529 10921 -14 -3130 1514 C
ATOM 1709 CD1 ILE A 213 -245.278 45.784 34.053 1.00 74.85 C
ANISOU 1709 CD1 ILE A 213 7806 7845 12787 270 -2707 1376 C
ATOM 1710 N ILE A 214 -243.354 41.600 31.296 1.00 86.63 N
ANISOU 1710 N ILE A 214 10147 9775 12994 -224 -2803 1316 N
ATOM 1711 CA ILE A 214 -243.475 40.257 30.713 1.00 84.57 C
ANISOU 1711 CA ILE A 214 10012 9595 12526 -356 -2845 1266 C
ATOM 1712 C ILE A 214 -243.036 39.152 31.676 1.00 85.91 C
ANISOU 1712 C ILE A 214 10187 9818 12637 -331 -2575 1092 C
ATOM 1713 O ILE A 214 -243.768 38.162 31.812 1.00 79.14 O
ANISOU 1713 O ILE A 214 9262 8981 11826 -381 -2594 1036 O
ATOM 1714 CB ILE A 214 -242.734 40.190 29.368 1.00 74.49 C
ANISOU 1714 CB ILE A 214 9025 8367 10910 -495 -2954 1334 C
ATOM 1715 CG1 ILE A 214 -243.409 41.062 28.315 1.00 60.22 C
ANISOU 1715 CG1 ILE A 214 7225 6510 9147 -561 -3282 1530 C
ATOM 1716 CG2 ILE A 214 -242.639 38.748 28.871 1.00 70.14 C
ANISOU 1716 CG2 ILE A 214 8632 7895 10122 -629 -2928 1239 C
ATOM 1717 CD1 ILE A 214 -244.892 40.908 28.274 1.00 86.11 C
ANISOU 1717 CD1 ILE A 214 10285 9746 12686 -571 -3513 1593 C
ATOM 1718 N PRO A 215 -241.875 39.236 32.345 1.00 77.01 N
ANISOU 1718 N PRO A 215 9139 8710 11412 -265 -2336 1009 N
ATOM 1719 CA PRO A 215 -241.525 38.158 33.285 1.00 72.43 C
ANISOU 1719 CA PRO A 215 8557 8168 10795 -246 -2113 866 C
ATOM 1720 C PRO A 215 -242.587 37.916 34.342 1.00 77.73 C
ANISOU 1720 C PRO A 215 8997 8811 11725 -192 -2063 816 C
ATOM 1721 O PRO A 215 -242.857 36.758 34.689 1.00 88.92 O
ANISOU 1721 O PRO A 215 10409 10257 13120 -236 -1992 736 O
ATOM 1722 CB PRO A 215 -240.208 38.649 33.903 1.00 67.53 C
ANISOU 1722 CB PRO A 215 8011 7553 10096 -168 -1913 821 C
ATOM 1723 CG PRO A 215 -239.621 39.521 32.866 1.00 70.44 C
ANISOU 1723 CG PRO A 215 8514 7914 10337 -201 -2018 920 C
ATOM 1724 CD PRO A 215 -240.791 40.234 32.251 1.00 73.52 C
ANISOU 1724 CD PRO A 215 8798 8253 10882 -219 -2269 1048 C
ATOM 1725 N LEU A 216 -243.203 38.977 34.864 1.00 67.24 N
ANISOU 1725 N LEU A 216 7478 7417 10652 -102 -2085 856 N
ATOM 1726 CA LEU A 216 -244.224 38.795 35.890 1.00 69.66 C
ANISOU 1726 CA LEU A 216 7559 7692 11217 -58 -2003 794 C
ATOM 1727 C LEU A 216 -245.455 38.103 35.324 1.00 77.93 C
ANISOU 1727 C LEU A 216 8502 8739 12370 -142 -2182 827 C
ATOM 1728 O LEU A 216 -246.046 37.237 35.979 1.00 77.83 O
ANISOU 1728 O LEU A 216 8393 8739 12439 -167 -2086 747 O
ATOM 1729 CB LEU A 216 -244.609 40.140 36.500 1.00 71.89 C
ANISOU 1729 CB LEU A 216 7657 7888 11769 54 -1974 816 C
ATOM 1730 CG LEU A 216 -245.610 40.067 37.655 1.00 77.01 C
ANISOU 1730 CG LEU A 216 8068 8497 12696 100 -1837 729 C
ATOM 1731 CD1 LEU A 216 -244.874 39.739 38.937 1.00 86.11 C
ANISOU 1731 CD1 LEU A 216 9285 9685 13746 125 -1552 601 C
ATOM 1732 CD2 LEU A 216 -246.357 41.373 37.797 1.00 80.32 C
ANISOU 1732 CD2 LEU A 216 8270 8804 13444 192 -1895 775 C
ATOM 1733 N ILE A 217 -245.854 38.468 34.105 1.00 74.79 N
ANISOU 1733 N ILE A 217 8127 8324 11966 -198 -2452 951 N
ATOM 1734 CA ILE A 217 -247.066 37.904 33.524 1.00 75.08 C
ANISOU 1734 CA ILE A 217 8052 8355 12122 -286 -2662 997 C
ATOM 1735 C ILE A 217 -246.873 36.424 33.203 1.00 79.14 C
ANISOU 1735 C ILE A 217 8727 8944 12399 -410 -2634 922 C
ATOM 1736 O ILE A 217 -247.776 35.604 33.418 1.00 76.24 O
ANISOU 1736 O ILE A 217 8238 8579 12152 -465 -2655 880 O
ATOM 1737 CB ILE A 217 -247.475 38.718 32.287 1.00 66.26 C
ANISOU 1737 CB ILE A 217 6941 7197 11038 -327 -2986 1168 C
ATOM 1738 CG1 ILE A 217 -247.717 40.172 32.677 1.00 68.69 C
ANISOU 1738 CG1 ILE A 217 7067 7405 11629 -192 -3006 1240 C
ATOM 1739 CG2 ILE A 217 -248.738 38.167 31.653 1.00 69.19 C
ANISOU 1739 CG2 ILE A 217 7189 7560 11539 -429 -3241 1227 C
ATOM 1740 CD1 ILE A 217 -248.240 40.995 31.527 1.00 62.27 C
ANISOU 1740 CD1 ILE A 217 6231 6529 10898 -229 -3351 1431 C
ATOM 1741 N VAL A 218 -245.690 36.053 32.711 1.00 77.67 N
ANISOU 1741 N VAL A 218 8808 8811 11892 -458 -2571 894 N
ATOM 1742 CA VAL A 218 -245.438 34.660 32.352 1.00 81.05 C
ANISOU 1742 CA VAL A 218 9400 9290 12104 -573 -2534 812 C
ATOM 1743 C VAL A 218 -245.355 33.795 33.602 1.00 72.43 C
ANISOU 1743 C VAL A 218 8243 8203 11075 -530 -2285 686 C
ATOM 1744 O VAL A 218 -245.964 32.721 33.677 1.00 75.11 O
ANISOU 1744 O VAL A 218 8552 8549 11439 -609 -2290 633 O
ATOM 1745 CB VAL A 218 -244.164 34.546 31.499 1.00 72.40 C
ANISOU 1745 CB VAL A 218 8594 8235 10678 -630 -2506 804 C
ATOM 1746 CG1 VAL A 218 -243.804 33.089 31.295 1.00 75.06 C
ANISOU 1746 CG1 VAL A 218 9090 8605 10826 -728 -2413 690 C
ATOM 1747 CG2 VAL A 218 -244.374 35.227 30.161 1.00 61.82 C
ANISOU 1747 CG2 VAL A 218 7352 6897 9240 -718 -2774 935 C
ATOM 1748 N ILE A 219 -244.614 34.260 34.606 1.00 65.71 N
ANISOU 1748 N ILE A 219 7376 7346 10247 -417 -2074 644 N
ATOM 1749 CA ILE A 219 -244.489 33.515 35.854 1.00 69.55 C
ANISOU 1749 CA ILE A 219 7818 7834 10773 -386 -1847 543 C
ATOM 1750 C ILE A 219 -245.852 33.315 36.509 1.00 78.32 C
ANISOU 1750 C ILE A 219 8694 8918 12148 -396 -1850 527 C
ATOM 1751 O ILE A 219 -246.139 32.246 37.062 1.00 86.00 O
ANISOU 1751 O ILE A 219 9653 9896 13128 -448 -1749 459 O
ATOM 1752 CB ILE A 219 -243.495 34.227 36.786 1.00 66.65 C
ANISOU 1752 CB ILE A 219 7475 7464 10385 -275 -1657 516 C
ATOM 1753 CG1 ILE A 219 -242.065 33.850 36.384 1.00 78.07 C
ANISOU 1753 CG1 ILE A 219 9153 8940 11572 -286 -1589 491 C
ATOM 1754 CG2 ILE A 219 -243.763 33.878 38.240 1.00 58.81 C
ANISOU 1754 CG2 ILE A 219 6373 6461 9511 -240 -1459 440 C
ATOM 1755 CD1 ILE A 219 -240.978 34.634 37.108 1.00 79.89 C
ANISOU 1755 CD1 ILE A 219 9416 9168 11769 -188 -1442 480 C
ATOM 1756 N PHE A 220 -246.721 34.326 36.439 1.00 73.47 N
ANISOU 1756 N PHE A 220 7884 8263 11769 -350 -1962 592 N
ATOM 1757 CA PHE A 220 -248.023 34.233 37.091 1.00 68.16 C
ANISOU 1757 CA PHE A 220 6954 7555 11389 -352 -1940 568 C
ATOM 1758 C PHE A 220 -248.988 33.349 36.314 1.00 71.08 C
ANISOU 1758 C PHE A 220 7273 7930 11804 -475 -2131 592 C
ATOM 1759 O PHE A 220 -249.696 32.527 36.906 1.00 68.23 O
ANISOU 1759 O PHE A 220 6802 7565 11556 -527 -2045 530 O
ATOM 1760 CB PHE A 220 -248.619 35.622 37.276 1.00 66.41 C
ANISOU 1760 CB PHE A 220 6519 7268 11448 -252 -1989 621 C
ATOM 1761 CG PHE A 220 -248.409 36.178 38.643 1.00 86.72 C
ANISOU 1761 CG PHE A 220 9007 9815 14128 -157 -1722 537 C
ATOM 1762 CD1 PHE A 220 -247.210 36.788 38.981 1.00 95.28 C
ANISOU 1762 CD1 PHE A 220 10242 10910 15049 -87 -1605 522 C
ATOM 1763 CD2 PHE A 220 -249.403 36.083 39.599 1.00 90.11 C
ANISOU 1763 CD2 PHE A 220 9212 10210 14816 -151 -1580 466 C
ATOM 1764 CE1 PHE A 220 -247.012 37.302 40.246 1.00 98.41 C
ANISOU 1764 CE1 PHE A 220 10581 11285 15525 -18 -1369 439 C
ATOM 1765 CE2 PHE A 220 -249.211 36.595 40.865 1.00101.42 C
ANISOU 1765 CE2 PHE A 220 10592 11621 16321 -85 -1321 375 C
ATOM 1766 CZ PHE A 220 -248.015 37.211 41.188 1.00103.93 C
ANISOU 1766 CZ PHE A 220 11077 11952 16460 -20 -1224 363 C
ATOM 1767 N PHE A 221 -249.048 33.521 34.992 1.00 70.08 N
ANISOU 1767 N PHE A 221 7230 7810 11586 -537 -2396 685 N
ATOM 1768 CA PHE A 221 -249.902 32.672 34.168 1.00 67.15 C
ANISOU 1768 CA PHE A 221 6842 7449 11225 -676 -2604 708 C
ATOM 1769 C PHE A 221 -249.500 31.208 34.304 1.00 80.77 C
ANISOU 1769 C PHE A 221 8734 9209 12744 -771 -2476 605 C
ATOM 1770 O PHE A 221 -250.308 30.358 34.695 1.00 80.63 O
ANISOU 1770 O PHE A 221 8601 9181 12854 -837 -2445 555 O
ATOM 1771 CB PHE A 221 -249.831 33.125 32.706 1.00 74.90 C
ANISOU 1771 CB PHE A 221 7949 8438 12070 -746 -2906 827 C
ATOM 1772 CG PHE A 221 -250.541 32.206 31.746 1.00 76.07 C
ANISOU 1772 CG PHE A 221 8142 8606 12157 -917 -3136 846 C
ATOM 1773 CD1 PHE A 221 -251.870 32.418 31.417 1.00 69.65 C
ANISOU 1773 CD1 PHE A 221 7093 7755 11618 -962 -3382 930 C
ATOM 1774 CD2 PHE A 221 -249.874 31.131 31.166 1.00 72.88 C
ANISOU 1774 CD2 PHE A 221 8009 8247 11434 -1036 -3109 775 C
ATOM 1775 CE1 PHE A 221 -252.527 31.568 30.532 1.00 73.34 C
ANISOU 1775 CE1 PHE A 221 7603 8240 12022 -1135 -3613 947 C
ATOM 1776 CE2 PHE A 221 -250.523 30.280 30.285 1.00 82.12 C
ANISOU 1776 CE2 PHE A 221 9236 9429 12535 -1207 -3316 778 C
ATOM 1777 CZ PHE A 221 -251.850 30.499 29.967 1.00 75.68 C
ANISOU 1777 CZ PHE A 221 8194 8587 11974 -1263 -3577 867 C
ATOM 1778 N CYS A 222 -248.239 30.901 33.991 1.00 83.37 N
ANISOU 1778 N CYS A 222 9331 9572 12775 -777 -2394 570 N
ATOM 1779 CA CYS A 222 -247.757 29.525 34.036 1.00 70.80 C
ANISOU 1779 CA CYS A 222 7910 7993 10999 -858 -2278 473 C
ATOM 1780 C CYS A 222 -248.034 28.877 35.387 1.00 72.60 C
ANISOU 1780 C CYS A 222 8019 8201 11365 -829 -2057 398 C
ATOM 1781 O CYS A 222 -248.682 27.829 35.470 1.00 83.00 O
ANISOU 1781 O CYS A 222 9303 9504 12730 -927 -2060 354 O
ATOM 1782 CB CYS A 222 -246.263 29.494 33.717 1.00 58.05 C
ANISOU 1782 CB CYS A 222 6553 6400 9105 -830 -2173 441 C
ATOM 1783 SG CYS A 222 -245.921 29.764 31.962 1.00 81.53 S
ANISOU 1783 SG CYS A 222 9743 9402 11832 -938 -2408 499 S
ATOM 1784 N TYR A 223 -247.551 29.494 36.464 1.00 69.04 N
ANISOU 1784 N TYR A 223 7517 7746 10969 -709 -1863 383 N
ATOM 1785 CA TYR A 223 -247.722 28.878 37.772 1.00 70.87 C
ANISOU 1785 CA TYR A 223 7677 7963 11286 -701 -1645 317 C
ATOM 1786 C TYR A 223 -249.181 28.858 38.201 1.00 75.00 C
ANISOU 1786 C TYR A 223 7942 8465 12092 -742 -1664 317 C
ATOM 1787 O TYR A 223 -249.609 27.917 38.874 1.00 81.32 O
ANISOU 1787 O TYR A 223 8704 9251 12943 -809 -1547 265 O
ATOM 1788 CB TYR A 223 -246.857 29.591 38.808 1.00 62.42 C
ANISOU 1788 CB TYR A 223 6631 6899 10187 -583 -1448 301 C
ATOM 1789 CG TYR A 223 -245.424 29.117 38.775 1.00 71.80 C
ANISOU 1789 CG TYR A 223 8057 8098 11126 -564 -1362 276 C
ATOM 1790 CD1 TYR A 223 -245.130 27.765 38.644 1.00 73.16 C
ANISOU 1790 CD1 TYR A 223 8362 8254 11180 -643 -1331 232 C
ATOM 1791 CD2 TYR A 223 -244.365 30.014 38.850 1.00 64.90 C
ANISOU 1791 CD2 TYR A 223 7263 7239 10158 -468 -1315 295 C
ATOM 1792 CE1 TYR A 223 -243.823 27.314 38.605 1.00 69.81 C
ANISOU 1792 CE1 TYR A 223 8130 7823 10571 -617 -1251 207 C
ATOM 1793 CE2 TYR A 223 -243.048 29.573 38.807 1.00 56.24 C
ANISOU 1793 CE2 TYR A 223 6357 6145 8866 -450 -1238 272 C
ATOM 1794 CZ TYR A 223 -242.783 28.221 38.686 1.00 74.75 C
ANISOU 1794 CZ TYR A 223 8817 8468 11118 -520 -1205 227 C
ATOM 1795 OH TYR A 223 -241.482 27.761 38.646 1.00 66.14 O
ANISOU 1795 OH TYR A 223 7890 7363 9877 -493 -1125 201 O
ATOM 1796 N GLY A 224 -249.958 29.874 37.829 1.00 76.46 N
ANISOU 1796 N GLY A 224 7938 8635 12479 -704 -1808 377 N
ATOM 1797 CA GLY A 224 -251.370 29.847 38.157 1.00 62.38 C
ANISOU 1797 CA GLY A 224 5879 6821 11003 -743 -1833 374 C
ATOM 1798 C GLY A 224 -252.087 28.737 37.416 1.00 81.66 C
ANISOU 1798 C GLY A 224 8319 9262 13446 -892 -1997 375 C
ATOM 1799 O GLY A 224 -252.900 28.007 37.994 1.00 77.94 O
ANISOU 1799 O GLY A 224 7715 8773 13125 -964 -1910 328 O
ATOM 1800 N GLN A 225 -251.779 28.585 36.129 1.00 78.09 N
ANISOU 1800 N GLN A 225 8028 8829 12813 -953 -2227 424 N
ATOM 1801 CA GLN A 225 -252.397 27.532 35.341 1.00 70.41 C
ANISOU 1801 CA GLN A 225 7087 7855 11810 -1111 -2398 417 C
ATOM 1802 C GLN A 225 -251.952 26.159 35.825 1.00 77.04 C
ANISOU 1802 C GLN A 225 8086 8691 12496 -1183 -2214 321 C
ATOM 1803 O GLN A 225 -252.725 25.196 35.761 1.00 85.14 O
ANISOU 1803 O GLN A 225 9053 9696 13599 -1307 -2256 289 O
ATOM 1804 CB GLN A 225 -252.063 27.741 33.864 1.00 61.10 C
ANISOU 1804 CB GLN A 225 6087 6700 10430 -1174 -2670 483 C
ATOM 1805 CG GLN A 225 -253.139 27.269 32.895 1.00 94.83 C
ANISOU 1805 CG GLN A 225 10286 10965 14778 -1331 -2960 524 C
ATOM 1806 CD GLN A 225 -254.301 28.240 32.750 1.00 97.19 C
ANISOU 1806 CD GLN A 225 10281 11237 15411 -1301 -3169 630 C
ATOM 1807 OE1 GLN A 225 -254.537 29.096 33.604 1.00103.14 O
ANISOU 1807 OE1 GLN A 225 10822 11962 16406 -1166 -3043 644 O
ATOM 1808 NE2 GLN A 225 -255.035 28.107 31.654 1.00111.15 N
ANISOU 1808 NE2 GLN A 225 12026 13005 17202 -1433 -3496 704 N
ATOM 1809 N LEU A 226 -250.730 26.062 36.349 1.00 81.58 N
ANISOU 1809 N LEU A 226 8847 9274 12875 -1107 -2015 280 N
ATOM 1810 CA LEU A 226 -250.243 24.799 36.893 1.00 78.52 C
ANISOU 1810 CA LEU A 226 8604 8863 12367 -1159 -1841 204 C
ATOM 1811 C LEU A 226 -250.965 24.438 38.188 1.00 83.40 C
ANISOU 1811 C LEU A 226 9049 9458 13183 -1172 -1656 175 C
ATOM 1812 O LEU A 226 -251.412 23.297 38.363 1.00 77.57 O
ANISOU 1812 O LEU A 226 8317 8687 12470 -1284 -1622 135 O
ATOM 1813 CB LEU A 226 -248.735 24.886 37.116 1.00 62.95 C
ANISOU 1813 CB LEU A 226 6851 6899 10169 -1066 -1699 184 C
ATOM 1814 CG LEU A 226 -247.998 23.651 37.615 1.00 69.01 C
ANISOU 1814 CG LEU A 226 7788 7625 10807 -1098 -1537 121 C
ATOM 1815 CD1 LEU A 226 -246.589 23.671 37.051 1.00 75.73 C
ANISOU 1815 CD1 LEU A 226 8868 8478 11429 -1044 -1518 103 C
ATOM 1816 CD2 LEU A 226 -247.967 23.599 39.144 1.00 59.60 C
ANISOU 1816 CD2 LEU A 226 6520 6420 9704 -1047 -1316 116 C
ATOM 1817 N VAL A 227 -251.061 25.392 39.122 1.00 70.01 N
ANISOU 1817 N VAL A 227 7209 7773 11618 -1068 -1520 187 N
ATOM 1818 CA VAL A 227 -251.790 25.143 40.363 1.00 67.56 C
ANISOU 1818 CA VAL A 227 6737 7445 11488 -1096 -1322 152 C
ATOM 1819 C VAL A 227 -253.233 24.759 40.059 1.00 81.92 C
ANISOU 1819 C VAL A 227 8332 9241 13551 -1208 -1432 151 C
ATOM 1820 O VAL A 227 -253.825 23.909 40.736 1.00 79.78 O
ANISOU 1820 O VAL A 227 7997 8947 13370 -1304 -1304 112 O
ATOM 1821 CB VAL A 227 -251.721 26.370 41.287 1.00 67.31 C
ANISOU 1821 CB VAL A 227 6586 7426 11565 -975 -1167 150 C
ATOM 1822 CG1 VAL A 227 -252.678 26.201 42.448 1.00 70.66 C
ANISOU 1822 CG1 VAL A 227 6817 7831 12199 -1027 -963 103 C
ATOM 1823 CG2 VAL A 227 -250.291 26.593 41.792 1.00 63.23 C
ANISOU 1823 CG2 VAL A 227 6290 6928 10807 -887 -1036 145 C
ATOM 1824 N PHE A 228 -253.815 25.367 39.025 1.00 72.93 N
ANISOU 1824 N PHE A 228 7073 8109 12529 -1208 -1682 203 N
ATOM 1825 CA PHE A 228 -255.181 25.026 38.656 1.00 73.39 C
ANISOU 1825 CA PHE A 228 6902 8143 12839 -1319 -1825 213 C
ATOM 1826 C PHE A 228 -255.269 23.589 38.159 1.00 82.26 C
ANISOU 1826 C PHE A 228 8168 9252 13835 -1478 -1899 180 C
ATOM 1827 O PHE A 228 -256.164 22.837 38.562 1.00 85.34 O
ANISOU 1827 O PHE A 228 8420 9614 14392 -1587 -1844 148 O
ATOM 1828 CB PHE A 228 -255.697 26.001 37.598 1.00 76.43 C
ANISOU 1828 CB PHE A 228 7148 8530 13361 -1287 -2119 297 C
ATOM 1829 CG PHE A 228 -257.060 25.662 37.088 1.00 81.79 C
ANISOU 1829 CG PHE A 228 7590 9183 14302 -1407 -2321 322 C
ATOM 1830 CD1 PHE A 228 -258.189 26.001 37.814 1.00 90.85 C
ANISOU 1830 CD1 PHE A 228 8397 10296 15827 -1396 -2230 309 C
ATOM 1831 CD2 PHE A 228 -257.216 24.989 35.887 1.00 96.78 C
ANISOU 1831 CD2 PHE A 228 9605 11090 16077 -1542 -2595 351 C
ATOM 1832 CE1 PHE A 228 -259.450 25.678 37.349 1.00 87.61 C
ANISOU 1832 CE1 PHE A 228 7743 9857 15689 -1508 -2423 335 C
ATOM 1833 CE2 PHE A 228 -258.475 24.663 35.416 1.00 89.82 C
ANISOU 1833 CE2 PHE A 228 8502 10184 15440 -1665 -2804 379 C
ATOM 1834 CZ PHE A 228 -259.591 25.010 36.147 1.00 85.80 C
ANISOU 1834 CZ PHE A 228 7631 9639 15330 -1644 -2725 376 C
ATOM 1835 N THR A 229 -254.335 23.184 37.294 1.00 74.30 N
ANISOU 1835 N THR A 229 7437 8255 12538 -1498 -2006 179 N
ATOM 1836 CA THR A 229 -254.341 21.820 36.775 1.00 67.35 C
ANISOU 1836 CA THR A 229 6715 7346 11531 -1649 -2066 132 C
ATOM 1837 C THR A 229 -254.141 20.799 37.890 1.00 74.38 C
ANISOU 1837 C THR A 229 7665 8194 12403 -1683 -1804 73 C
ATOM 1838 O THR A 229 -254.858 19.794 37.963 1.00 85.86 O
ANISOU 1838 O THR A 229 9071 9607 13946 -1821 -1806 41 O
ATOM 1839 CB THR A 229 -253.260 21.668 35.704 1.00 75.15 C
ANISOU 1839 CB THR A 229 7999 8347 12209 -1652 -2181 122 C
ATOM 1840 OG1 THR A 229 -253.668 22.356 34.517 1.00 86.16 O
ANISOU 1840 OG1 THR A 229 9355 9772 13607 -1685 -2469 184 O
ATOM 1841 CG2 THR A 229 -253.018 20.206 35.376 1.00 68.42 C
ANISOU 1841 CG2 THR A 229 7344 7443 11208 -1786 -2164 45 C
ATOM 1842 N VAL A 230 -253.185 21.051 38.782 1.00 76.74 N
ANISOU 1842 N VAL A 230 8069 8498 12590 -1569 -1589 67 N
ATOM 1843 CA VAL A 230 -252.918 20.107 39.862 1.00 73.78 C
ANISOU 1843 CA VAL A 230 7776 8079 12178 -1607 -1360 34 C
ATOM 1844 C VAL A 230 -254.116 20.009 40.800 1.00 76.92 C
ANISOU 1844 C VAL A 230 7930 8466 12829 -1678 -1234 29 C
ATOM 1845 O VAL A 230 -254.445 18.924 41.299 1.00 84.21 O
ANISOU 1845 O VAL A 230 8878 9340 13779 -1794 -1134 5 O
ATOM 1846 CB VAL A 230 -251.631 20.508 40.604 1.00 67.86 C
ANISOU 1846 CB VAL A 230 7184 7341 11258 -1474 -1189 44 C
ATOM 1847 CG1 VAL A 230 -251.470 19.705 41.872 1.00 65.62 C
ANISOU 1847 CG1 VAL A 230 6958 7015 10959 -1516 -965 36 C
ATOM 1848 CG2 VAL A 230 -250.433 20.309 39.697 1.00 66.89 C
ANISOU 1848 CG2 VAL A 230 7306 7211 10900 -1431 -1280 34 C
ATOM 1849 N LYS A 231 -254.804 21.130 41.037 1.00 71.75 N
ANISOU 1849 N LYS A 231 7034 7849 12380 -1614 -1231 47 N
ATOM 1850 CA LYS A 231 -255.927 21.116 41.971 1.00 68.47 C
ANISOU 1850 CA LYS A 231 6369 7420 12225 -1678 -1071 25 C
ATOM 1851 C LYS A 231 -257.150 20.407 41.394 1.00 71.91 C
ANISOU 1851 C LYS A 231 6633 7825 12863 -1831 -1217 17 C
ATOM 1852 O LYS A 231 -257.890 19.755 42.141 1.00 71.68 O
ANISOU 1852 O LYS A 231 6492 7766 12976 -1942 -1062 -12 O
ATOM 1853 CB LYS A 231 -256.279 22.542 42.398 1.00 72.12 C
ANISOU 1853 CB LYS A 231 6613 7914 12877 -1557 -1005 31 C
ATOM 1854 CG LYS A 231 -255.312 23.128 43.434 1.00 71.81 C
ANISOU 1854 CG LYS A 231 6705 7897 12684 -1447 -773 17 C
ATOM 1855 CD LYS A 231 -255.771 24.488 43.935 1.00 72.42 C
ANISOU 1855 CD LYS A 231 6555 7986 12976 -1344 -676 0 C
ATOM 1856 CE LYS A 231 -254.844 25.011 45.025 1.00 81.67 C
ANISOU 1856 CE LYS A 231 7871 9180 13981 -1262 -441 -25 C
ATOM 1857 NZ LYS A 231 -254.871 24.139 46.230 1.00 73.34 N
ANISOU 1857 NZ LYS A 231 6903 8116 12846 -1374 -186 -61 N
ATOM 1858 N GLU A 232 -257.381 20.514 40.082 1.00 68.08 N
ANISOU 1858 N GLU A 232 6131 7347 12388 -1855 -1516 45 N
ATOM 1859 CA GLU A 232 -258.492 19.787 39.478 1.00 71.26 C
ANISOU 1859 CA GLU A 232 6389 7720 12966 -2018 -1685 39 C
ATOM 1860 C GLU A 232 -258.219 18.287 39.456 1.00 90.91 C
ANISOU 1860 C GLU A 232 9094 10158 15290 -2158 -1642 -4 C
ATOM 1861 O GLU A 232 -259.129 17.481 39.690 1.00 86.93 O
ANISOU 1861 O GLU A 232 8463 9613 14952 -2305 -1614 -28 O
ATOM 1862 CB GLU A 232 -258.765 20.299 38.063 1.00 85.58 C
ANISOU 1862 CB GLU A 232 8160 9555 14800 -2024 -2041 90 C
ATOM 1863 CG GLU A 232 -259.031 21.795 37.978 1.00129.20 C
ANISOU 1863 CG GLU A 232 13474 15110 20507 -1883 -2120 150 C
ATOM 1864 CD GLU A 232 -260.044 22.278 39.001 1.00143.85 C
ANISOU 1864 CD GLU A 232 14982 16945 22730 -1857 -1938 133 C
ATOM 1865 OE1 GLU A 232 -261.145 21.689 39.077 1.00145.35 O
ANISOU 1865 OE1 GLU A 232 14959 17104 23163 -1987 -1961 115 O
ATOM 1866 OE2 GLU A 232 -259.734 23.248 39.730 1.00138.90 O
ANISOU 1866 OE2 GLU A 232 14295 16329 22153 -1713 -1760 129 O
ATOM 1867 N ALA A 233 -256.971 17.892 39.181 1.00 78.37 N
ANISOU 1867 N ALA A 233 7821 8560 13394 -2116 -1631 -17 N
ATOM 1868 CA ALA A 233 -256.646 16.471 39.158 1.00 74.59 C
ANISOU 1868 CA ALA A 233 7551 8010 12779 -2235 -1584 -61 C
ATOM 1869 C ALA A 233 -256.779 15.863 40.549 1.00 76.75 C
ANISOU 1869 C ALA A 233 7803 8240 13117 -2276 -1302 -68 C
ATOM 1870 O ALA A 233 -257.382 14.792 40.718 1.00 73.31 O
ANISOU 1870 O ALA A 233 7351 7741 12763 -2431 -1270 -91 O
ATOM 1871 CB ALA A 233 -255.244 16.257 38.593 1.00 63.08 C
ANISOU 1871 CB ALA A 233 6413 6540 11016 -2164 -1612 -80 C
ATOM 1872 N ALA A 234 -256.245 16.552 41.564 1.00 70.79 N
ANISOU 1872 N ALA A 234 7055 7519 12322 -2152 -1098 -44 N
ATOM 1873 CA ALA A 234 -256.414 16.091 42.941 1.00 81.06 C
ANISOU 1873 CA ALA A 234 8343 8791 13667 -2206 -829 -41 C
ATOM 1874 C ALA A 234 -257.889 15.957 43.304 1.00 89.89 C
ANISOU 1874 C ALA A 234 9173 9902 15079 -2338 -772 -58 C
ATOM 1875 O ALA A 234 -258.275 15.021 44.013 1.00 87.19 O
ANISOU 1875 O ALA A 234 8844 9506 14779 -2473 -621 -64 O
ATOM 1876 CB ALA A 234 -255.714 17.043 43.911 1.00 63.16 C
ANISOU 1876 CB ALA A 234 6109 6574 11315 -2064 -642 -19 C
ATOM 1877 N ALA A 235 -258.728 16.882 42.821 1.00 79.83 N
ANISOU 1877 N ALA A 235 7628 8675 14027 -2305 -894 -61 N
ATOM 1878 CA ALA A 235 -260.146 16.857 43.160 1.00 81.60 C
ANISOU 1878 CA ALA A 235 7535 8890 14580 -2417 -836 -82 C
ATOM 1879 C ALA A 235 -260.819 15.578 42.683 1.00 82.58 C
ANISOU 1879 C ALA A 235 7651 8951 14776 -2613 -944 -97 C
ATOM 1880 O ALA A 235 -261.825 15.157 43.262 1.00 80.64 O
ANISOU 1880 O ALA A 235 7208 8678 14755 -2745 -815 -118 O
ATOM 1881 CB ALA A 235 -260.849 18.075 42.566 1.00 70.58 C
ANISOU 1881 CB ALA A 235 5848 7537 13432 -2331 -1001 -70 C
ATOM 1882 N GLN A 236 -260.290 14.953 41.636 1.00 79.57 N
ANISOU 1882 N GLN A 236 7480 8543 14211 -2644 -1167 -97 N
ATOM 1883 CA GLN A 236 -260.852 13.726 41.096 1.00 84.94 C
ANISOU 1883 CA GLN A 236 8184 9154 14937 -2835 -1285 -124 C
ATOM 1884 C GLN A 236 -260.292 12.469 41.746 1.00 72.04 C
ANISOU 1884 C GLN A 236 6798 7433 13140 -2921 -1105 -136 C
ATOM 1885 O GLN A 236 -260.740 11.368 41.407 1.00 96.77 O
ANISOU 1885 O GLN A 236 9963 10489 16315 -3089 -1173 -163 O
ATOM 1886 CB GLN A 236 -260.626 13.667 39.581 1.00 88.95 C
ANISOU 1886 CB GLN A 236 8802 9666 15327 -2850 -1618 -133 C
ATOM 1887 CG GLN A 236 -261.638 14.453 38.759 1.00 83.82 C
ANISOU 1887 CG GLN A 236 7869 9067 14912 -2868 -1879 -108 C
ATOM 1888 CD GLN A 236 -263.005 13.778 38.706 1.00109.67 C
ANISOU 1888 CD GLN A 236 10893 12299 18477 -3066 -1948 -125 C
ATOM 1889 OE1 GLN A 236 -263.652 13.568 39.729 1.00109.49 O
ANISOU 1889 OE1 GLN A 236 10689 12254 18660 -3120 -1717 -136 O
ATOM 1890 NE2 GLN A 236 -263.447 13.438 37.505 1.00118.12 N
ANISOU 1890 NE2 GLN A 236 11961 13359 19559 -3188 -2265 -130 N
ATOM 1891 N GLN A 237 -259.337 12.603 42.668 1.00 70.18 N
ANISOU 1891 N GLN A 237 6736 7198 12729 -2817 -891 -111 N
ATOM 1892 CA GLN A 237 -258.721 11.471 43.362 1.00 74.59 C
ANISOU 1892 CA GLN A 237 7538 7665 13139 -2884 -731 -97 C
ATOM 1893 C GLN A 237 -258.591 11.790 44.850 1.00 79.04 C
ANISOU 1893 C GLN A 237 8092 8251 13690 -2855 -437 -56 C
ATOM 1894 O GLN A 237 -257.512 11.710 45.432 1.00 88.15 O
ANISOU 1894 O GLN A 237 9472 9386 14634 -2774 -334 -18 O
ATOM 1895 CB GLN A 237 -257.344 11.125 42.803 1.00 82.63 C
ANISOU 1895 CB GLN A 237 8869 8638 13886 -2788 -818 -99 C
ATOM 1896 CG GLN A 237 -257.293 10.728 41.343 1.00102.46 C
ANISOU 1896 CG GLN A 237 11461 11120 16348 -2831 -1078 -155 C
ATOM 1897 CD GLN A 237 -255.944 10.134 40.975 1.00114.69 C
ANISOU 1897 CD GLN A 237 13327 12592 17656 -2764 -1091 -175 C
ATOM 1898 OE1 GLN A 237 -255.261 9.558 41.822 1.00114.32 O
ANISOU 1898 OE1 GLN A 237 13434 12470 17531 -2743 -925 -140 O
ATOM 1899 NE2 GLN A 237 -255.551 10.275 39.714 1.00122.17 N
ANISOU 1899 NE2 GLN A 237 14374 13553 18492 -2736 -1286 -228 N
ATOM 1900 N GLN A 238 -259.715 12.128 45.480 1.00 89.46 N
ANISOU 1900 N GLN A 238 9145 9605 15240 -2935 -300 -68 N
ATOM 1901 CA GLN A 238 -259.669 12.653 46.836 1.00 87.16 C
ANISOU 1901 CA GLN A 238 8828 9354 14934 -2911 -13 -49 C
ATOM 1902 C GLN A 238 -259.369 11.597 47.900 1.00 87.03 C
ANISOU 1902 C GLN A 238 9022 9260 14785 -3038 192 -1 C
ATOM 1903 O GLN A 238 -258.917 11.961 48.988 1.00105.41 O
ANISOU 1903 O GLN A 238 11444 11617 16989 -3006 400 31 O
ATOM 1904 CB GLN A 238 -260.981 13.362 47.153 1.00 90.03 C
ANISOU 1904 CB GLN A 238 8831 9770 15608 -2960 95 -93 C
ATOM 1905 CG GLN A 238 -261.192 14.642 46.382 1.00 96.42 C
ANISOU 1905 CG GLN A 238 9429 10652 16554 -2806 -72 -118 C
ATOM 1906 CD GLN A 238 -262.088 15.589 47.125 1.00115.04 C
ANISOU 1906 CD GLN A 238 11482 13055 19173 -2795 132 -161 C
ATOM 1907 OE1 GLN A 238 -262.098 15.609 48.352 1.00122.30 O
ANISOU 1907 OE1 GLN A 238 12435 13980 20054 -2843 436 -175 O
ATOM 1908 NE2 GLN A 238 -262.858 16.374 46.391 1.00129.33 N
ANISOU 1908 NE2 GLN A 238 12994 14890 21257 -2739 -31 -182 N
ATOM 1909 N GLU A 239 -259.595 10.310 47.637 1.00 83.79 N
ANISOU 1909 N GLU A 239 8699 8747 14392 -3189 135 10 N
ATOM 1910 CA GLU A 239 -259.212 9.294 48.615 1.00 95.52 C
ANISOU 1910 CA GLU A 239 10409 10140 15743 -3304 304 77 C
ATOM 1911 C GLU A 239 -257.727 8.949 48.572 1.00 95.18 C
ANISOU 1911 C GLU A 239 10692 10039 15433 -3187 230 135 C
ATOM 1912 O GLU A 239 -257.255 8.192 49.429 1.00 89.76 O
ANISOU 1912 O GLU A 239 10210 9271 14624 -3258 348 213 O
ATOM 1913 CB GLU A 239 -260.003 8.012 48.393 1.00 97.04 C
ANISOU 1913 CB GLU A 239 10576 10222 16072 -3516 278 71 C
ATOM 1914 CG GLU A 239 -259.675 7.373 47.031 1.00 89.08 C
ANISOU 1914 CG GLU A 239 9664 9140 15042 -3497 -2 34 C
ATOM 1915 CD GLU A 239 -260.522 7.979 45.950 1.00121.30 C
ANISOU 1915 CD GLU A 239 13480 13294 19315 -3487 -194 -42 C
ATOM 1916 OE1 GLU A 239 -260.055 8.866 45.209 1.00 73.70 O
ANISOU 1916 OE1 GLU A 239 7439 7342 13222 -3322 -349 -65 O
ATOM 1917 OE2 GLU A 239 -261.699 7.586 45.875 1.00170.15 O
ANISOU 1917 OE2 GLU A 239 19460 19461 25730 -3655 -192 -71 O
ATOM 1918 N SER A 240 -256.985 9.447 47.591 1.00 93.97 N
ANISOU 1918 N SER A 240 10589 9917 15198 -3019 35 104 N
ATOM 1919 CA SER A 240 -255.533 9.285 47.588 1.00 92.51 C
ANISOU 1919 CA SER A 240 10677 9685 14786 -2888 -13 151 C
ATOM 1920 C SER A 240 -254.934 10.339 48.510 1.00 78.24 C
ANISOU 1920 C SER A 240 8897 7973 12856 -2766 122 194 C
ATOM 1921 O SER A 240 -254.798 11.503 48.131 1.00 84.90 O
ANISOU 1921 O SER A 240 9635 8923 13701 -2627 70 155 O
ATOM 1922 CB SER A 240 -254.981 9.405 46.174 1.00 87.08 C
ANISOU 1922 CB SER A 240 10037 8994 14057 -2774 -247 90 C
ATOM 1923 OG SER A 240 -253.576 9.257 46.167 1.00 91.96 O
ANISOU 1923 OG SER A 240 10893 9560 14487 -2645 -274 126 O
ATOM 1924 N ALA A 241 -254.580 9.932 49.736 1.00 86.93 N
ANISOU 1924 N ALA A 241 10150 9033 13846 -2831 289 279 N
ATOM 1925 CA ALA A 241 -254.014 10.876 50.700 1.00 88.03 C
ANISOU 1925 CA ALA A 241 10341 9260 13847 -2746 421 318 C
ATOM 1926 C ALA A 241 -252.704 11.471 50.204 1.00 94.77 C
ANISOU 1926 C ALA A 241 11315 10137 14554 -2537 283 326 C
ATOM 1927 O ALA A 241 -252.415 12.646 50.468 1.00 88.33 O
ANISOU 1927 O ALA A 241 10450 9428 13684 -2424 327 309 O
ATOM 1928 CB ALA A 241 -253.795 10.196 52.051 1.00 78.37 C
ANISOU 1928 CB ALA A 241 9305 7975 12497 -2879 590 424 C
ATOM 1929 N THR A 242 -251.901 10.680 49.487 1.00 85.02 N
ANISOU 1929 N THR A 242 10236 8799 13269 -2488 129 343 N
ATOM 1930 CA THR A 242 -250.637 11.189 48.968 1.00 86.66 C
ANISOU 1930 CA THR A 242 10549 9022 13355 -2297 13 343 C
ATOM 1931 C THR A 242 -250.867 12.197 47.849 1.00 91.35 C
ANISOU 1931 C THR A 242 10982 9717 14008 -2187 -102 249 C
ATOM 1932 O THR A 242 -250.160 13.210 47.767 1.00 85.24 O
ANISOU 1932 O THR A 242 10215 9022 13150 -2039 -126 245 O
ATOM 1933 CB THR A 242 -249.764 10.035 48.482 1.00 85.40 C
ANISOU 1933 CB THR A 242 10581 8708 13158 -2281 -95 370 C
ATOM 1934 OG1 THR A 242 -250.368 9.437 47.331 1.00 93.70 O
ANISOU 1934 OG1 THR A 242 11572 9707 14324 -2342 -204 283 O
ATOM 1935 CG2 THR A 242 -249.618 8.988 49.574 1.00 83.11 C
ANISOU 1935 CG2 THR A 242 10446 8298 12835 -2401 -4 484 C
ATOM 1936 N THR A 243 -251.846 11.937 46.974 1.00 87.14 N
ANISOU 1936 N THR A 243 10309 9180 13620 -2267 -188 180 N
ATOM 1937 CA THR A 243 -252.205 12.926 45.960 1.00 87.63 C
ANISOU 1937 CA THR A 243 10209 9339 13747 -2186 -316 111 C
ATOM 1938 C THR A 243 -252.590 14.254 46.605 1.00 87.71 C
ANISOU 1938 C THR A 243 10051 9470 13806 -2123 -209 113 C
ATOM 1939 O THR A 243 -252.198 15.325 46.123 1.00 84.31 O
ANISOU 1939 O THR A 243 9576 9114 13342 -1984 -285 94 O
ATOM 1940 CB THR A 243 -253.347 12.404 45.086 1.00 79.97 C
ANISOU 1940 CB THR A 243 9100 8344 12941 -2316 -430 53 C
ATOM 1941 OG1 THR A 243 -252.971 11.153 44.503 1.00 93.14 O
ANISOU 1941 OG1 THR A 243 10940 9887 14560 -2382 -514 36 O
ATOM 1942 CG2 THR A 243 -253.658 13.381 43.966 1.00 72.74 C
ANISOU 1942 CG2 THR A 243 8040 7517 12080 -2240 -605 4 C
ATOM 1943 N GLN A 244 -253.342 14.200 47.710 1.00 82.14 N
ANISOU 1943 N GLN A 244 9257 8775 13178 -2231 -20 129 N
ATOM 1944 CA GLN A 244 -253.700 15.419 48.424 1.00 81.45 C
ANISOU 1944 CA GLN A 244 9020 8786 13141 -2181 122 112 C
ATOM 1945 C GLN A 244 -252.474 16.064 49.063 1.00 94.20 C
ANISOU 1945 C GLN A 244 10805 10436 14552 -2056 181 152 C
ATOM 1946 O GLN A 244 -252.317 17.291 49.018 1.00 92.49 O
ANISOU 1946 O GLN A 244 10502 10299 14343 -1935 186 124 O
ATOM 1947 CB GLN A 244 -254.767 15.113 49.475 1.00 77.18 C
ANISOU 1947 CB GLN A 244 8365 8240 12719 -2349 343 106 C
ATOM 1948 CG GLN A 244 -256.016 14.453 48.907 1.00 75.46 C
ANISOU 1948 CG GLN A 244 7959 7983 12729 -2488 290 67 C
ATOM 1949 CD GLN A 244 -256.585 15.214 47.727 1.00 81.65 C
ANISOU 1949 CD GLN A 244 8515 8816 13692 -2408 98 12 C
ATOM 1950 OE1 GLN A 244 -256.785 14.652 46.653 1.00 82.39 O
ANISOU 1950 OE1 GLN A 244 8599 8871 13835 -2443 -107 0 O
ATOM 1951 NE2 GLN A 244 -256.853 16.502 47.923 1.00 86.48 N
ANISOU 1951 NE2 GLN A 244 8950 9506 14403 -2309 158 -20 N
ATOM 1952 N LYS A 245 -251.591 15.255 49.657 1.00 96.36 N
ANISOU 1952 N LYS A 245 11316 10642 14655 -2084 215 224 N
ATOM 1953 CA LYS A 245 -250.353 15.797 50.211 1.00 95.05 C
ANISOU 1953 CA LYS A 245 11313 10502 14300 -1970 236 273 C
ATOM 1954 C LYS A 245 -249.489 16.413 49.117 1.00 87.98 C
ANISOU 1954 C LYS A 245 10434 9631 13361 -1793 58 248 C
ATOM 1955 O LYS A 245 -248.942 17.509 49.292 1.00 83.96 O
ANISOU 1955 O LYS A 245 9918 9194 12787 -1677 73 242 O
ATOM 1956 CB LYS A 245 -249.581 14.707 50.955 1.00 98.24 C
ANISOU 1956 CB LYS A 245 11957 10809 14561 -2038 262 372 C
ATOM 1957 CG LYS A 245 -249.527 14.907 52.464 1.00110.47 C
ANISOU 1957 CG LYS A 245 13596 12388 15988 -2125 448 432 C
ATOM 1958 CD LYS A 245 -248.606 13.891 53.127 1.00118.59 C
ANISOU 1958 CD LYS A 245 14877 13313 16869 -2175 420 558 C
ATOM 1959 CE LYS A 245 -248.482 14.148 54.624 1.00123.52 C
ANISOU 1959 CE LYS A 245 15624 13976 17331 -2277 582 628 C
ATOM 1960 NZ LYS A 245 -247.445 13.285 55.263 1.00121.32 N
ANISOU 1960 NZ LYS A 245 15597 13596 16904 -2309 509 776 N
ATOM 1961 N ALA A 246 -249.371 15.731 47.975 1.00 77.40 N
ANISOU 1961 N ALA A 246 9124 8231 12054 -1784 -100 227 N
ATOM 1962 CA ALA A 246 -248.609 16.284 46.861 1.00 70.54 C
ANISOU 1962 CA ALA A 246 8280 7386 11135 -1640 -254 195 C
ATOM 1963 C ALA A 246 -249.236 17.574 46.346 1.00 87.42 C
ANISOU 1963 C ALA A 246 10221 9628 13367 -1576 -297 146 C
ATOM 1964 O ALA A 246 -248.523 18.505 45.953 1.00100.27 O
ANISOU 1964 O ALA A 246 11866 11307 14927 -1443 -357 142 O
ATOM 1965 CB ALA A 246 -248.499 15.258 45.735 1.00 54.07 C
ANISOU 1965 CB ALA A 246 6270 5212 9062 -1676 -393 163 C
ATOM 1966 N GLU A 247 -250.569 17.649 46.335 1.00 94.83 N
ANISOU 1966 N GLU A 247 10961 10589 14481 -1669 -273 113 N
ATOM 1967 CA GLU A 247 -251.231 18.877 45.907 1.00 80.80 C
ANISOU 1967 CA GLU A 247 8972 8891 12839 -1605 -322 78 C
ATOM 1968 C GLU A 247 -250.888 20.038 46.832 1.00 72.59 C
ANISOU 1968 C GLU A 247 7904 7912 11764 -1513 -178 82 C
ATOM 1969 O GLU A 247 -250.629 21.154 46.369 1.00 67.71 O
ANISOU 1969 O GLU A 247 7225 7344 11157 -1392 -250 72 O
ATOM 1970 CB GLU A 247 -252.745 18.663 45.843 1.00 69.14 C
ANISOU 1970 CB GLU A 247 7262 7410 11596 -1729 -311 46 C
ATOM 1971 CG GLU A 247 -253.539 19.887 45.405 1.00 84.06 C
ANISOU 1971 CG GLU A 247 8898 9360 13682 -1665 -376 18 C
ATOM 1972 CD GLU A 247 -253.927 20.783 46.570 1.00103.42 C
ANISOU 1972 CD GLU A 247 11213 11849 16233 -1640 -152 -5 C
ATOM 1973 OE1 GLU A 247 -254.402 20.253 47.597 1.00115.65 O
ANISOU 1973 OE1 GLU A 247 12747 13380 17816 -1756 52 -18 O
ATOM 1974 OE2 GLU A 247 -253.746 22.015 46.462 1.00 95.00 O
ANISOU 1974 OE2 GLU A 247 10066 10825 15205 -1513 -169 -14 O
ATOM 1975 N LYS A 248 -250.885 19.795 48.146 1.00 67.98 N
ANISOU 1975 N LYS A 248 7378 7323 11131 -1582 24 98 N
ATOM 1976 CA LYS A 248 -250.629 20.876 49.090 1.00 74.53 C
ANISOU 1976 CA LYS A 248 8192 8209 11917 -1522 177 86 C
ATOM 1977 C LYS A 248 -249.204 21.403 48.956 1.00 84.16 C
ANISOU 1977 C LYS A 248 9582 9446 12948 -1383 101 119 C
ATOM 1978 O LYS A 248 -248.978 22.618 49.019 1.00 77.78 O
ANISOU 1978 O LYS A 248 8714 8690 12148 -1281 120 95 O
ATOM 1979 CB LYS A 248 -250.898 20.400 50.517 1.00 81.81 C
ANISOU 1979 CB LYS A 248 9181 9120 12784 -1658 407 97 C
ATOM 1980 CG LYS A 248 -252.366 20.140 50.822 1.00 93.84 C
ANISOU 1980 CG LYS A 248 10500 10636 14517 -1797 540 47 C
ATOM 1981 CD LYS A 248 -252.556 19.603 52.235 1.00102.44 C
ANISOU 1981 CD LYS A 248 11695 11714 15512 -1955 781 64 C
ATOM 1982 CE LYS A 248 -254.003 19.206 52.491 1.00108.92 C
ANISOU 1982 CE LYS A 248 12313 12519 16551 -2110 927 14 C
ATOM 1983 NZ LYS A 248 -254.149 18.410 53.742 1.00111.72 N
ANISOU 1983 NZ LYS A 248 12815 12850 16785 -2297 1142 49 N
ATOM 1984 N GLU A 249 -248.231 20.511 48.755 1.00 78.24 N
ANISOU 1984 N GLU A 249 9033 8645 12051 -1378 18 173 N
ATOM 1985 CA GLU A 249 -246.845 20.955 48.708 1.00 96.19 C
ANISOU 1985 CA GLU A 249 11454 10929 14166 -1254 -39 206 C
ATOM 1986 C GLU A 249 -246.514 21.646 47.392 1.00 92.58 C
ANISOU 1986 C GLU A 249 10945 10497 13733 -1131 -201 178 C
ATOM 1987 O GLU A 249 -245.693 22.571 47.378 1.00 81.99 O
ANISOU 1987 O GLU A 249 9640 9196 12319 -1020 -217 184 O
ATOM 1988 CB GLU A 249 -245.896 19.781 48.974 1.00105.15 C
ANISOU 1988 CB GLU A 249 12798 11983 15172 -1283 -67 274 C
ATOM 1989 CG GLU A 249 -246.010 18.612 48.016 1.00133.48 C
ANISOU 1989 CG GLU A 249 16422 15488 18807 -1324 -180 268 C
ATOM 1990 CD GLU A 249 -245.252 17.383 48.505 1.00149.73 C
ANISOU 1990 CD GLU A 249 18666 17439 20785 -1369 -176 338 C
ATOM 1991 OE1 GLU A 249 -245.013 17.277 49.728 1.00154.95 O
ANISOU 1991 OE1 GLU A 249 19412 18094 21369 -1418 -79 406 O
ATOM 1992 OE2 GLU A 249 -244.895 16.524 47.670 1.00150.15 O
ANISOU 1992 OE2 GLU A 249 18788 17407 20854 -1361 -273 327 O
ATOM 1993 N VAL A 250 -247.148 21.244 46.288 1.00 77.37 N
ANISOU 1993 N VAL A 250 8944 8552 11901 -1163 -325 151 N
ATOM 1994 CA VAL A 250 -246.955 21.975 45.038 1.00 72.31 C
ANISOU 1994 CA VAL A 250 8261 7944 11270 -1072 -483 132 C
ATOM 1995 C VAL A 250 -247.515 23.386 45.160 1.00 81.58 C
ANISOU 1995 C VAL A 250 9257 9182 12558 -1008 -462 117 C
ATOM 1996 O VAL A 250 -246.879 24.365 44.751 1.00 89.86 O
ANISOU 1996 O VAL A 250 10321 10265 13558 -898 -521 125 O
ATOM 1997 CB VAL A 250 -247.593 21.222 43.859 1.00 68.91 C
ANISOU 1997 CB VAL A 250 7801 7480 10901 -1148 -632 108 C
ATOM 1998 CG1 VAL A 250 -247.553 22.087 42.611 1.00 63.99 C
ANISOU 1998 CG1 VAL A 250 7133 6899 10280 -1080 -801 100 C
ATOM 1999 CG2 VAL A 250 -246.877 19.910 43.617 1.00 65.49 C
ANISOU 1999 CG2 VAL A 250 7559 6966 10358 -1192 -650 108 C
ATOM 2000 N THR A 251 -248.717 23.510 45.727 1.00 68.17 N
ANISOU 2000 N THR A 251 7381 7491 11029 -1078 -369 92 N
ATOM 2001 CA THR A 251 -249.305 24.828 45.934 1.00 74.00 C
ANISOU 2001 CA THR A 251 7929 8267 11919 -1015 -325 67 C
ATOM 2002 C THR A 251 -248.440 25.669 46.861 1.00 76.32 C
ANISOU 2002 C THR A 251 8309 8589 12100 -936 -190 63 C
ATOM 2003 O THR A 251 -248.168 26.843 46.582 1.00 80.84 O
ANISOU 2003 O THR A 251 8830 9185 12701 -828 -231 59 O
ATOM 2004 CB THR A 251 -250.717 24.687 46.503 1.00 64.61 C
ANISOU 2004 CB THR A 251 6529 7068 10951 -1115 -207 26 C
ATOM 2005 OG1 THR A 251 -251.516 23.916 45.598 1.00 64.09 O
ANISOU 2005 OG1 THR A 251 6378 6976 10998 -1197 -356 32 O
ATOM 2006 CG2 THR A 251 -251.352 26.054 46.701 1.00 59.49 C
ANISOU 2006 CG2 THR A 251 5662 6438 10504 -1041 -150 -12 C
ATOM 2007 N ARG A 252 -247.998 25.080 47.976 1.00 67.47 N
ANISOU 2007 N ARG A 252 7328 7460 10847 -998 -39 72 N
ATOM 2008 CA ARG A 252 -247.176 25.821 48.924 1.00 79.79 C
ANISOU 2008 CA ARG A 252 8987 9049 12282 -947 78 70 C
ATOM 2009 C ARG A 252 -245.875 26.286 48.277 1.00 76.75 C
ANISOU 2009 C ARG A 252 8723 8674 11764 -824 -56 106 C
ATOM 2010 O ARG A 252 -245.400 27.397 48.545 1.00 65.25 O
ANISOU 2010 O ARG A 252 7264 7246 10283 -743 -23 91 O
ATOM 2011 CB ARG A 252 -246.898 24.958 50.154 1.00 81.23 C
ANISOU 2011 CB ARG A 252 9325 9216 12322 -1059 222 95 C
ATOM 2012 CG ARG A 252 -246.263 25.719 51.305 1.00110.24 C
ANISOU 2012 CG ARG A 252 13096 12924 15866 -1048 357 86 C
ATOM 2013 CD ARG A 252 -246.322 24.920 52.597 1.00127.29 C
ANISOU 2013 CD ARG A 252 15391 15073 17902 -1199 511 112 C
ATOM 2014 NE ARG A 252 -245.988 25.731 53.766 1.00135.22 N
ANISOU 2014 NE ARG A 252 16473 16116 18788 -1225 664 82 N
ATOM 2015 CZ ARG A 252 -246.885 26.360 54.520 1.00145.32 C
ANISOU 2015 CZ ARG A 252 17651 17421 20145 -1294 874 -9 C
ATOM 2016 NH1 ARG A 252 -246.491 27.073 55.567 1.00149.81 N
ANISOU 2016 NH1 ARG A 252 18322 18021 20577 -1329 1012 -46 N
ATOM 2017 NH2 ARG A 252 -248.177 26.274 54.232 1.00147.73 N
ANISOU 2017 NH2 ARG A 252 17747 17712 20670 -1335 952 -70 N
ATOM 2018 N MET A 253 -245.308 25.463 47.391 1.00 65.74 N
ANISOU 2018 N MET A 253 7432 7251 10296 -814 -198 143 N
ATOM 2019 CA MET A 253 -244.054 25.812 46.735 1.00 58.67 C
ANISOU 2019 CA MET A 253 6649 6361 9283 -709 -305 169 C
ATOM 2020 C MET A 253 -244.254 26.879 45.668 1.00 68.14 C
ANISOU 2020 C MET A 253 7742 7588 10561 -626 -420 156 C
ATOM 2021 O MET A 253 -243.386 27.737 45.477 1.00 82.93 O
ANISOU 2021 O MET A 253 9661 9481 12367 -533 -448 167 O
ATOM 2022 CB MET A 253 -243.412 24.563 46.133 1.00 53.40 C
ANISOU 2022 CB MET A 253 6121 5639 8528 -733 -390 195 C
ATOM 2023 CG MET A 253 -242.444 23.880 47.077 1.00 78.22 C
ANISOU 2023 CG MET A 253 9422 8745 11552 -747 -324 240 C
ATOM 2024 SD MET A 253 -241.031 24.939 47.472 1.00 96.17 S
ANISOU 2024 SD MET A 253 11774 11054 13713 -631 -318 265 S
ATOM 2025 CE MET A 253 -240.343 24.045 48.863 1.00105.41 C
ANISOU 2025 CE MET A 253 13097 12178 14777 -697 -249 336 C
ATOM 2026 N VAL A 254 -245.379 26.844 44.953 1.00 70.19 N
ANISOU 2026 N VAL A 254 7858 7844 10966 -664 -500 141 N
ATOM 2027 CA VAL A 254 -245.645 27.899 43.979 1.00 71.22 C
ANISOU 2027 CA VAL A 254 7884 7994 11183 -594 -632 149 C
ATOM 2028 C VAL A 254 -245.818 29.234 44.690 1.00 79.29 C
ANISOU 2028 C VAL A 254 8791 9031 12303 -523 -535 132 C
ATOM 2029 O VAL A 254 -245.311 30.270 44.239 1.00 74.58 O
ANISOU 2029 O VAL A 254 8198 8444 11694 -432 -601 151 O
ATOM 2030 CB VAL A 254 -246.877 27.546 43.124 1.00 64.71 C
ANISOU 2030 CB VAL A 254 6919 7156 10511 -664 -763 150 C
ATOM 2031 CG1 VAL A 254 -247.321 28.751 42.293 1.00 70.95 C
ANISOU 2031 CG1 VAL A 254 7574 7957 11428 -598 -907 178 C
ATOM 2032 CG2 VAL A 254 -246.574 26.360 42.231 1.00 59.47 C
ANISOU 2032 CG2 VAL A 254 6396 6473 9727 -732 -876 155 C
ATOM 2033 N ILE A 255 -246.522 29.224 45.823 1.00 68.07 N
ANISOU 2033 N ILE A 255 7278 7606 10980 -572 -363 88 N
ATOM 2034 CA ILE A 255 -246.715 30.444 46.596 1.00 64.96 C
ANISOU 2034 CA ILE A 255 6782 7214 10684 -518 -234 46 C
ATOM 2035 C ILE A 255 -245.373 31.015 47.037 1.00 70.88 C
ANISOU 2035 C ILE A 255 7699 7984 11249 -451 -192 55 C
ATOM 2036 O ILE A 255 -245.126 32.221 46.919 1.00 73.26 O
ANISOU 2036 O ILE A 255 7955 8283 11599 -363 -204 47 O
ATOM 2037 CB ILE A 255 -247.641 30.166 47.791 1.00 58.59 C
ANISOU 2037 CB ILE A 255 5881 6400 9979 -611 -20 -18 C
ATOM 2038 CG1 ILE A 255 -249.065 29.887 47.309 1.00 74.00 C
ANISOU 2038 CG1 ILE A 255 7608 8327 12182 -662 -64 -33 C
ATOM 2039 CG2 ILE A 255 -247.648 31.333 48.743 1.00 65.15 C
ANISOU 2039 CG2 ILE A 255 6659 7230 10865 -570 156 -84 C
ATOM 2040 CD1 ILE A 255 -250.000 29.481 48.421 1.00 78.86 C
ANISOU 2040 CD1 ILE A 255 8126 8934 12904 -773 164 -99 C
ATOM 2041 N ILE A 256 -244.482 30.157 47.539 1.00 75.04 N
ANISOU 2041 N ILE A 256 8413 8520 11577 -493 -153 78 N
ATOM 2042 CA ILE A 256 -243.166 30.611 47.983 1.00 64.07 C
ANISOU 2042 CA ILE A 256 7174 7148 10024 -439 -132 94 C
ATOM 2043 C ILE A 256 -242.396 31.223 46.820 1.00 71.89 C
ANISOU 2043 C ILE A 256 8190 8141 10985 -338 -288 130 C
ATOM 2044 O ILE A 256 -241.834 32.321 46.936 1.00 70.70 O
ANISOU 2044 O ILE A 256 8045 7997 10821 -267 -277 124 O
ATOM 2045 CB ILE A 256 -242.390 29.452 48.632 1.00 64.35 C
ANISOU 2045 CB ILE A 256 7389 7178 9885 -505 -100 132 C
ATOM 2046 CG1 ILE A 256 -242.975 29.126 50.004 1.00 55.88 C
ANISOU 2046 CG1 ILE A 256 6327 6109 8796 -615 78 103 C
ATOM 2047 CG2 ILE A 256 -240.901 29.784 48.759 1.00 60.84 C
ANISOU 2047 CG2 ILE A 256 7085 6741 9289 -439 -141 168 C
ATOM 2048 CD1 ILE A 256 -242.406 27.857 50.600 1.00 61.68 C
ANISOU 2048 CD1 ILE A 256 7231 6823 9383 -698 84 163 C
ATOM 2049 N MET A 257 -242.380 30.537 45.673 1.00 57.56 N
ANISOU 2049 N MET A 257 6399 6316 9155 -343 -427 163 N
ATOM 2050 CA MET A 257 -241.673 31.073 44.513 1.00 58.60 C
ANISOU 2050 CA MET A 257 6574 6452 9237 -271 -562 195 C
ATOM 2051 C MET A 257 -242.250 32.416 44.093 1.00 68.94 C
ANISOU 2051 C MET A 257 7746 7762 10687 -212 -614 198 C
ATOM 2052 O MET A 257 -241.507 33.386 43.888 1.00 73.92 O
ANISOU 2052 O MET A 257 8411 8396 11280 -140 -637 215 O
ATOM 2053 CB MET A 257 -241.712 30.078 43.357 1.00 54.94 C
ANISOU 2053 CB MET A 257 6169 5978 8728 -314 -686 212 C
ATOM 2054 CG MET A 257 -240.892 28.824 43.622 1.00 63.24 C
ANISOU 2054 CG MET A 257 7368 7006 9653 -349 -645 212 C
ATOM 2055 SD MET A 257 -241.127 27.569 42.354 1.00 83.69 S
ANISOU 2055 SD MET A 257 10023 9565 12212 -420 -758 201 S
ATOM 2056 CE MET A 257 -240.194 26.203 43.071 1.00 88.05 C
ANISOU 2056 CE MET A 257 10719 10060 12676 -444 -671 201 C
ATOM 2057 N VAL A 258 -243.580 32.500 43.983 1.00 66.25 N
ANISOU 2057 N VAL A 258 7237 7405 10529 -241 -635 185 N
ATOM 2058 CA VAL A 258 -244.193 33.724 43.483 1.00 63.75 C
ANISOU 2058 CA VAL A 258 6769 7066 10385 -180 -715 202 C
ATOM 2059 C VAL A 258 -244.011 34.862 44.479 1.00 71.86 C
ANISOU 2059 C VAL A 258 7747 8077 11478 -118 -570 159 C
ATOM 2060 O VAL A 258 -243.715 35.999 44.091 1.00 64.48 O
ANISOU 2060 O VAL A 258 6788 7120 10589 -41 -629 184 O
ATOM 2061 CB VAL A 258 -245.670 33.485 43.136 1.00 67.96 C
ANISOU 2061 CB VAL A 258 7110 7576 11135 -227 -784 203 C
ATOM 2062 CG1 VAL A 258 -246.333 34.811 42.820 1.00 68.67 C
ANISOU 2062 CG1 VAL A 258 7016 7621 11453 -153 -856 224 C
ATOM 2063 CG2 VAL A 258 -245.747 32.560 41.931 1.00 61.41 C
ANISOU 2063 CG2 VAL A 258 6352 6760 10221 -291 -968 249 C
ATOM 2064 N ILE A 259 -244.119 34.568 45.777 1.00 66.50 N
ANISOU 2064 N ILE A 259 7077 7406 10784 -162 -377 93 N
ATOM 2065 CA ILE A 259 -243.885 35.600 46.784 1.00 64.83 C
ANISOU 2065 CA ILE A 259 6850 7180 10601 -124 -223 33 C
ATOM 2066 C ILE A 259 -242.435 36.060 46.747 1.00 69.78 C
ANISOU 2066 C ILE A 259 7645 7825 11042 -74 -255 63 C
ATOM 2067 O ILE A 259 -242.147 37.260 46.807 1.00 66.65 O
ANISOU 2067 O ILE A 259 7221 7402 10699 -7 -242 49 O
ATOM 2068 CB ILE A 259 -244.277 35.092 48.183 1.00 76.99 C
ANISOU 2068 CB ILE A 259 8402 8732 12120 -214 -6 -43 C
ATOM 2069 CG1 ILE A 259 -245.796 35.059 48.336 1.00 81.85 C
ANISOU 2069 CG1 ILE A 259 8799 9315 12986 -251 72 -96 C
ATOM 2070 CG2 ILE A 259 -243.654 35.969 49.267 1.00 76.15 C
ANISOU 2070 CG2 ILE A 259 8369 8625 11938 -203 148 -106 C
ATOM 2071 CD1 ILE A 259 -246.243 34.539 49.677 1.00 88.24 C
ANISOU 2071 CD1 ILE A 259 9625 10137 13766 -361 308 -175 C
ATOM 2072 N ALA A 260 -241.498 35.114 46.648 1.00 73.22 N
ANISOU 2072 N ALA A 260 8246 8296 11278 -105 -295 102 N
ATOM 2073 CA ALA A 260 -240.093 35.490 46.565 1.00 61.39 C
ANISOU 2073 CA ALA A 260 6885 6811 9628 -59 -329 131 C
ATOM 2074 C ALA A 260 -239.803 36.293 45.308 1.00 69.17 C
ANISOU 2074 C ALA A 260 7849 7783 10650 14 -472 180 C
ATOM 2075 O ALA A 260 -238.917 37.155 45.313 1.00 91.65 O
ANISOU 2075 O ALA A 260 10748 10626 13449 64 -474 190 O
ATOM 2076 CB ALA A 260 -239.206 34.250 46.614 1.00 58.55 C
ANISOU 2076 CB ALA A 260 6677 6474 9097 -99 -352 165 C
ATOM 2077 N PHE A 261 -240.525 36.031 44.220 1.00 57.28 N
ANISOU 2077 N PHE A 261 6276 6268 9220 8 -598 218 N
ATOM 2078 CA PHE A 261 -240.322 36.839 43.025 1.00 65.10 C
ANISOU 2078 CA PHE A 261 7262 7244 10231 58 -743 278 C
ATOM 2079 C PHE A 261 -240.893 38.239 43.209 1.00 69.62 C
ANISOU 2079 C PHE A 261 7695 7765 10992 120 -736 273 C
ATOM 2080 O PHE A 261 -240.354 39.207 42.663 1.00 68.04 O
ANISOU 2080 O PHE A 261 7522 7542 10788 171 -805 317 O
ATOM 2081 CB PHE A 261 -240.948 36.157 41.812 1.00 51.74 C
ANISOU 2081 CB PHE A 261 5556 5557 8545 12 -899 324 C
ATOM 2082 CG PHE A 261 -240.766 36.911 40.531 1.00 66.69 C
ANISOU 2082 CG PHE A 261 7475 7439 10427 36 -1064 400 C
ATOM 2083 CD1 PHE A 261 -239.635 36.714 39.756 1.00 64.85 C
ANISOU 2083 CD1 PHE A 261 7409 7232 10000 24 -1105 428 C
ATOM 2084 CD2 PHE A 261 -241.727 37.817 40.095 1.00 71.96 C
ANISOU 2084 CD2 PHE A 261 7996 8061 11284 63 -1176 447 C
ATOM 2085 CE1 PHE A 261 -239.458 37.409 38.568 1.00 68.19 C
ANISOU 2085 CE1 PHE A 261 7878 7647 10384 23 -1246 502 C
ATOM 2086 CE2 PHE A 261 -241.558 38.515 38.911 1.00 72.63 C
ANISOU 2086 CE2 PHE A 261 8123 8131 11343 70 -1347 538 C
ATOM 2087 CZ PHE A 261 -240.420 38.310 38.145 1.00 73.25 C
ANISOU 2087 CZ PHE A 261 8394 8246 11192 42 -1378 565 C
ATOM 2088 N LEU A 262 -241.976 38.367 43.972 1.00 66.36 N
ANISOU 2088 N LEU A 262 7131 7322 10759 113 -642 216 N
ATOM 2089 CA LEU A 262 -242.544 39.687 44.208 1.00 80.05 C
ANISOU 2089 CA LEU A 262 8718 8987 12712 178 -612 195 C
ATOM 2090 C LEU A 262 -241.682 40.497 45.165 1.00 83.82 C
ANISOU 2090 C LEU A 262 9270 9454 13125 209 -467 135 C
ATOM 2091 O LEU A 262 -241.666 41.731 45.086 1.00 74.15 O
ANISOU 2091 O LEU A 262 7985 8164 12026 274 -476 136 O
ATOM 2092 CB LEU A 262 -243.970 39.559 44.745 1.00 74.87 C
ANISOU 2092 CB LEU A 262 7861 8294 12293 158 -528 134 C
ATOM 2093 CG LEU A 262 -245.024 39.051 43.761 1.00 74.46 C
ANISOU 2093 CG LEU A 262 7679 8230 12381 134 -699 198 C
ATOM 2094 CD1 LEU A 262 -246.318 38.758 44.494 1.00 77.05 C
ANISOU 2094 CD1 LEU A 262 7810 8531 12936 99 -572 121 C
ATOM 2095 CD2 LEU A 262 -245.256 40.062 42.643 1.00 71.26 C
ANISOU 2095 CD2 LEU A 262 7191 7764 12120 201 -907 295 C
ATOM 2096 N ILE A 263 -240.963 39.827 46.073 1.00 66.97 N
ANISOU 2096 N ILE A 263 7270 7374 10802 156 -346 88 N
ATOM 2097 CA ILE A 263 -240.072 40.535 46.990 1.00 71.02 C
ANISOU 2097 CA ILE A 263 7873 7884 11228 164 -231 36 C
ATOM 2098 C ILE A 263 -238.949 41.216 46.216 1.00 71.69 C
ANISOU 2098 C ILE A 263 8044 7963 11231 218 -347 104 C
ATOM 2099 O ILE A 263 -238.443 42.269 46.622 1.00 68.96 O
ANISOU 2099 O ILE A 263 7716 7582 10904 250 -296 73 O
ATOM 2100 CB ILE A 263 -239.540 39.559 48.064 1.00 78.99 C
ANISOU 2100 CB ILE A 263 9016 8953 12043 81 -120 -1 C
ATOM 2101 CG1 ILE A 263 -240.626 39.258 49.097 1.00 69.95 C
ANISOU 2101 CG1 ILE A 263 7794 7802 10982 14 50 -90 C
ATOM 2102 CG2 ILE A 263 -238.291 40.099 48.758 1.00 59.22 C
ANISOU 2102 CG2 ILE A 263 6647 6463 9393 77 -74 -20 C
ATOM 2103 CD1 ILE A 263 -240.236 38.155 50.079 1.00 74.61 C
ANISOU 2103 CD1 ILE A 263 8526 8447 11373 -89 136 -101 C
ATOM 2104 N CYS A 264 -238.576 40.661 45.071 1.00 70.08 N
ANISOU 2104 N CYS A 264 7896 7788 10942 220 -493 190 N
ATOM 2105 CA CYS A 264 -237.589 41.294 44.211 1.00 71.66 C
ANISOU 2105 CA CYS A 264 8175 7982 11071 258 -593 256 C
ATOM 2106 C CYS A 264 -238.219 42.227 43.186 1.00 80.74 C
ANISOU 2106 C CYS A 264 9232 9072 12375 305 -721 322 C
ATOM 2107 O CYS A 264 -237.575 43.189 42.747 1.00 98.52 O
ANISOU 2107 O CYS A 264 11522 11291 14622 340 -769 365 O
ATOM 2108 CB CYS A 264 -236.772 40.218 43.498 1.00 60.37 C
ANISOU 2108 CB CYS A 264 6871 6610 9457 223 -660 303 C
ATOM 2109 SG CYS A 264 -235.449 40.844 42.474 1.00 76.90 S
ANISOU 2109 SG CYS A 264 9073 8704 11441 247 -740 370 S
ATOM 2110 N TRP A 265 -239.467 41.974 42.802 1.00 79.50 N
ANISOU 2110 N TRP A 265 8949 8892 12365 300 -789 339 N
ATOM 2111 CA TRP A 265 -240.117 42.720 41.736 1.00 75.36 C
ANISOU 2111 CA TRP A 265 8336 8307 11990 333 -957 428 C
ATOM 2112 C TRP A 265 -240.795 43.996 42.221 1.00 79.40 C
ANISOU 2112 C TRP A 265 8687 8714 12766 404 -915 401 C
ATOM 2113 O TRP A 265 -240.688 45.034 41.561 1.00 75.69 O
ANISOU 2113 O TRP A 265 8201 8175 12381 449 -1025 478 O
ATOM 2114 CB TRP A 265 -241.127 41.809 41.035 1.00 60.21 C
ANISOU 2114 CB TRP A 265 6351 6409 10117 286 -1080 468 C
ATOM 2115 CG TRP A 265 -241.734 42.333 39.770 1.00 67.45 C
ANISOU 2115 CG TRP A 265 7210 7279 11139 292 -1306 586 C
ATOM 2116 CD1 TRP A 265 -241.292 42.114 38.496 1.00 66.80 C
ANISOU 2116 CD1 TRP A 265 7264 7231 10887 242 -1474 682 C
ATOM 2117 CD2 TRP A 265 -242.929 43.121 39.651 1.00 66.65 C
ANISOU 2117 CD2 TRP A 265 6900 7084 11341 340 -1397 624 C
ATOM 2118 NE1 TRP A 265 -242.127 42.732 37.592 1.00 67.82 N
ANISOU 2118 NE1 TRP A 265 7301 7299 11170 246 -1685 793 N
ATOM 2119 CE2 TRP A 265 -243.139 43.354 38.275 1.00 60.31 C
ANISOU 2119 CE2 TRP A 265 6125 6262 10528 314 -1652 764 C
ATOM 2120 CE3 TRP A 265 -243.833 43.661 40.574 1.00 75.83 C
ANISOU 2120 CE3 TRP A 265 7853 8168 12791 399 -1283 549 C
ATOM 2121 CZ2 TRP A 265 -244.210 44.108 37.801 1.00 64.71 C
ANISOU 2121 CZ2 TRP A 265 6499 6721 11366 352 -1825 852 C
ATOM 2122 CZ3 TRP A 265 -244.906 44.407 40.098 1.00 74.91 C
ANISOU 2122 CZ3 TRP A 265 7535 7946 12980 447 -1430 619 C
ATOM 2123 CH2 TRP A 265 -245.083 44.623 38.725 1.00 66.06 C
ANISOU 2123 CH2 TRP A 265 6439 6806 11856 427 -1714 779 C
ATOM 2124 N LEU A 266 -241.485 43.934 43.357 1.00 72.40 N
ANISOU 2124 N LEU A 266 7688 7807 12014 407 -748 290 N
ATOM 2125 CA LEU A 266 -242.284 45.070 43.801 1.00 77.87 C
ANISOU 2125 CA LEU A 266 8201 8383 13001 474 -686 244 C
ATOM 2126 C LEU A 266 -241.454 46.305 44.148 1.00 92.07 C
ANISOU 2126 C LEU A 266 10061 10119 14802 522 -623 219 C
ATOM 2127 O LEU A 266 -241.937 47.420 43.888 1.00 71.59 O
ANISOU 2127 O LEU A 266 7342 7405 12453 593 -673 244 O
ATOM 2128 CB LEU A 266 -243.168 44.642 44.978 1.00 68.30 C
ANISOU 2128 CB LEU A 266 6871 7170 11911 446 -481 110 C
ATOM 2129 CG LEU A 266 -244.381 43.778 44.637 1.00 82.16 C
ANISOU 2129 CG LEU A 266 8478 8937 13802 414 -544 129 C
ATOM 2130 CD1 LEU A 266 -244.946 43.117 45.896 1.00 62.55 C
ANISOU 2130 CD1 LEU A 266 5943 6482 11341 353 -304 -7 C
ATOM 2131 CD2 LEU A 266 -245.443 44.624 43.939 1.00 73.23 C
ANISOU 2131 CD2 LEU A 266 7119 7687 13017 487 -684 191 C
ATOM 2132 N PRO A 267 -240.246 46.204 44.725 1.00 85.59 N
ANISOU 2132 N PRO A 267 9413 9360 13745 488 -526 174 N
ATOM 2133 CA PRO A 267 -239.474 47.436 44.960 1.00 68.32 C
ANISOU 2133 CA PRO A 267 7277 7106 11575 527 -488 157 C
ATOM 2134 C PRO A 267 -239.254 48.269 43.706 1.00 81.88 C
ANISOU 2134 C PRO A 267 8995 8757 13358 574 -682 295 C
ATOM 2135 O PRO A 267 -239.353 49.503 43.769 1.00 83.29 O
ANISOU 2135 O PRO A 267 9110 8817 13722 631 -675 291 O
ATOM 2136 CB PRO A 267 -238.161 46.903 45.543 1.00 67.59 C
ANISOU 2136 CB PRO A 267 7375 7114 11193 465 -410 122 C
ATOM 2137 CG PRO A 267 -238.572 45.712 46.307 1.00 70.34 C
ANISOU 2137 CG PRO A 267 7728 7539 11458 404 -306 53 C
ATOM 2138 CD PRO A 267 -239.654 45.064 45.454 1.00 83.09 C
ANISOU 2138 CD PRO A 267 9228 9156 13186 413 -420 118 C
ATOM 2139 N TYR A 268 -238.972 47.637 42.564 1.00 68.91 N
ANISOU 2139 N TYR A 268 7434 7180 11568 544 -850 416 N
ATOM 2140 CA TYR A 268 -238.836 48.404 41.330 1.00 76.91 C
ANISOU 2140 CA TYR A 268 8467 8133 12622 566 -1041 559 C
ATOM 2141 C TYR A 268 -240.145 49.100 40.975 1.00 82.27 C
ANISOU 2141 C TYR A 268 8950 8687 13623 626 -1151 612 C
ATOM 2142 O TYR A 268 -240.149 50.269 40.571 1.00 72.87 O
ANISOU 2142 O TYR A 268 7723 7379 12584 676 -1236 685 O
ATOM 2143 CB TYR A 268 -238.385 47.499 40.189 1.00 64.50 C
ANISOU 2143 CB TYR A 268 7031 6661 10816 499 -1180 660 C
ATOM 2144 CG TYR A 268 -236.967 47.005 40.321 1.00 81.43 C
ANISOU 2144 CG TYR A 268 9354 8899 12687 452 -1094 629 C
ATOM 2145 CD1 TYR A 268 -236.695 45.772 40.900 1.00 77.58 C
ANISOU 2145 CD1 TYR A 268 8916 8507 12051 412 -993 551 C
ATOM 2146 CD2 TYR A 268 -235.897 47.765 39.855 1.00 60.74 C
ANISOU 2146 CD2 TYR A 268 6843 6260 9975 446 -1117 686 C
ATOM 2147 CE1 TYR A 268 -235.397 45.308 41.017 1.00 70.14 C
ANISOU 2147 CE1 TYR A 268 8115 7635 10900 377 -927 530 C
ATOM 2148 CE2 TYR A 268 -234.602 47.310 39.963 1.00 57.40 C
ANISOU 2148 CE2 TYR A 268 6555 5914 9338 405 -1037 657 C
ATOM 2149 CZ TYR A 268 -234.354 46.077 40.546 1.00 80.45 C
ANISOU 2149 CZ TYR A 268 9507 8924 12136 376 -946 579 C
ATOM 2150 OH TYR A 268 -233.062 45.607 40.665 1.00 73.56 O
ANISOU 2150 OH TYR A 268 8747 8114 11090 344 -878 556 O
ATOM 2151 N ALA A 269 -241.266 48.397 41.129 1.00 73.14 N
ANISOU 2151 N ALA A 269 7654 7543 12594 623 -1155 581 N
ATOM 2152 CA ALA A 269 -242.564 49.011 40.874 1.00 78.66 C
ANISOU 2152 CA ALA A 269 8129 8114 13646 686 -1257 625 C
ATOM 2153 C ALA A 269 -242.870 50.100 41.896 1.00 77.81 C
ANISOU 2153 C ALA A 269 7884 7873 13810 765 -1081 509 C
ATOM 2154 O ALA A 269 -243.453 51.135 41.552 1.00 86.78 O
ANISOU 2154 O ALA A 269 8876 8855 15240 840 -1178 571 O
ATOM 2155 CB ALA A 269 -243.658 47.941 40.871 1.00 73.72 C
ANISOU 2155 CB ALA A 269 7374 7537 13099 652 -1283 605 C
ATOM 2156 N GLY A 270 -242.480 49.890 43.155 1.00 72.24 N
ANISOU 2156 N GLY A 270 7226 7212 13009 744 -824 341 N
ATOM 2157 CA GLY A 270 -242.643 50.936 44.154 1.00 78.79 C
ANISOU 2157 CA GLY A 270 7966 7919 14053 799 -632 208 C
ATOM 2158 C GLY A 270 -241.887 52.204 43.798 1.00 93.54 C
ANISOU 2158 C GLY A 270 9904 9683 15956 845 -698 269 C
ATOM 2159 O GLY A 270 -242.433 53.307 43.866 1.00100.44 O
ANISOU 2159 O GLY A 270 10632 10386 17146 924 -692 257 O
ATOM 2160 N VAL A 271 -240.616 52.062 43.408 1.00 88.65 N
ANISOU 2160 N VAL A 271 9500 9155 15028 794 -758 336 N
ATOM 2161 CA VAL A 271 -239.833 53.215 42.970 1.00 84.09 C
ANISOU 2161 CA VAL A 271 9001 8486 14462 820 -831 410 C
ATOM 2162 C VAL A 271 -240.383 53.775 41.662 1.00 86.16 C
ANISOU 2162 C VAL A 271 9187 8646 14905 865 -1090 602 C
ATOM 2163 O VAL A 271 -240.470 54.996 41.486 1.00 92.92 O
ANISOU 2163 O VAL A 271 9983 9338 15983 926 -1139 648 O
ATOM 2164 CB VAL A 271 -238.346 52.834 42.841 1.00 74.25 C
ANISOU 2164 CB VAL A 271 7987 7369 12854 745 -825 434 C
ATOM 2165 CG1 VAL A 271 -237.588 53.926 42.117 1.00 75.63 C
ANISOU 2165 CG1 VAL A 271 8243 7459 13035 757 -934 546 C
ATOM 2166 CG2 VAL A 271 -237.734 52.572 44.218 1.00 63.21 C
ANISOU 2166 CG2 VAL A 271 6663 6037 11317 703 -594 258 C
ATOM 2167 N ALA A 272 -240.748 52.897 40.720 1.00 82.17 N
ANISOU 2167 N ALA A 272 8693 8227 14302 826 -1270 723 N
ATOM 2168 CA ALA A 272 -241.373 53.340 39.475 1.00 93.82 C
ANISOU 2168 CA ALA A 272 10102 9612 15933 847 -1546 917 C
ATOM 2169 C ALA A 272 -242.560 54.253 39.750 1.00112.66 C
ANISOU 2169 C ALA A 272 12230 11802 18775 953 -1566 907 C
ATOM 2170 O ALA A 272 -242.664 55.347 39.183 1.00111.80 O
ANISOU 2170 O ALA A 272 12080 11537 18863 1004 -1713 1030 O
ATOM 2171 CB ALA A 272 -241.825 52.134 38.651 1.00102.21 C
ANISOU 2171 CB ALA A 272 11189 10799 16849 779 -1708 1004 C
ATOM 2172 N PHE A 273 -243.466 53.811 40.628 1.00104.33 N
ANISOU 2172 N PHE A 273 10994 10742 17905 984 -1410 761 N
ATOM 2173 CA PHE A 273 -244.605 54.629 41.025 1.00103.64 C
ANISOU 2173 CA PHE A 273 10633 10460 18284 1088 -1375 713 C
ATOM 2174 C PHE A 273 -244.183 55.953 41.649 1.00109.74 C
ANISOU 2174 C PHE A 273 11400 11071 19225 1156 -1230 630 C
ATOM 2175 O PHE A 273 -244.956 56.916 41.599 1.00107.12 O
ANISOU 2175 O PHE A 273 10865 10533 19304 1253 -1276 652 O
ATOM 2176 CB PHE A 273 -245.489 53.851 42.003 1.00 84.76 C
ANISOU 2176 CB PHE A 273 8077 8113 16014 1086 -1163 535 C
ATOM 2177 CG PHE A 273 -246.819 54.502 42.267 1.00110.22 C
ANISOU 2177 CG PHE A 273 10980 11144 19753 1188 -1138 492 C
ATOM 2178 CD1 PHE A 273 -247.769 54.592 41.262 1.00116.00 C
ANISOU 2178 CD1 PHE A 273 11539 11796 20739 1221 -1422 666 C
ATOM 2179 CD2 PHE A 273 -247.124 55.018 43.517 1.00115.56 C
ANISOU 2179 CD2 PHE A 273 11537 11721 20649 1235 -826 271 C
ATOM 2180 CE1 PHE A 273 -248.996 55.188 41.495 1.00107.97 C
ANISOU 2180 CE1 PHE A 273 10284 10648 20090 1249 -1372 611 C
ATOM 2181 CE2 PHE A 273 -248.354 55.614 43.757 1.00113.63 C
ANISOU 2181 CE2 PHE A 273 11013 11312 20850 1302 -770 212 C
ATOM 2182 CZ PHE A 273 -249.289 55.700 42.744 1.00106.90 C
ANISOU 2182 CZ PHE A 273 10030 10420 20169 1292 -1040 383 C
ATOM 2183 N TYR A 274 -242.986 56.023 42.237 1.00102.18 N
ANISOU 2183 N TYR A 274 10651 10193 17979 1104 -1064 534 N
ATOM 2184 CA TYR A 274 -242.447 57.267 42.775 1.00111.35 C
ANISOU 2184 CA TYR A 274 11842 11210 19255 1146 -940 457 C
ATOM 2185 C TYR A 274 -241.760 58.123 41.717 1.00120.27 C
ANISOU 2185 C TYR A 274 13087 12260 20351 1151 -1163 657 C
ATOM 2186 O TYR A 274 -241.237 59.190 42.052 1.00125.57 O
ANISOU 2186 O TYR A 274 13797 12803 21111 1178 -1084 613 O
ATOM 2187 CB TYR A 274 -241.464 56.966 43.909 1.00121.09 C
ANISOU 2187 CB TYR A 274 13250 12564 20195 1073 -679 269 C
ATOM 2188 CG TYR A 274 -241.534 57.940 45.065 1.00125.52 C
ANISOU 2188 CG TYR A 274 13750 12977 20964 1110 -430 68 C
ATOM 2189 CD1 TYR A 274 -242.259 57.634 46.208 1.00128.69 C
ANISOU 2189 CD1 TYR A 274 14039 13376 21480 1107 -175 -143 C
ATOM 2190 CD2 TYR A 274 -240.876 59.163 45.015 1.00126.74 C
ANISOU 2190 CD2 TYR A 274 13970 12991 21195 1135 -438 82 C
ATOM 2191 CE1 TYR A 274 -242.328 58.516 47.267 1.00133.47 C
ANISOU 2191 CE1 TYR A 274 14608 13845 22258 1124 73 -346 C
ATOM 2192 CE2 TYR A 274 -240.937 60.049 46.067 1.00130.94 C
ANISOU 2192 CE2 TYR A 274 14459 13380 21912 1159 -204 -117 C
ATOM 2193 CZ TYR A 274 -241.666 59.723 47.190 1.00136.01 C
ANISOU 2193 CZ TYR A 274 14997 14024 22655 1152 55 -337 C
ATOM 2194 OH TYR A 274 -241.729 60.609 48.241 1.00144.17 O
ANISOU 2194 OH TYR A 274 16005 14913 23858 1160 308 -554 O
ATOM 2195 N ILE A 275 -241.725 57.678 40.461 1.00123.54 N
ANISOU 2195 N ILE A 275 13572 12746 20623 1110 -1431 869 N
ATOM 2196 CA ILE A 275 -241.291 58.521 39.360 1.00124.08 C
ANISOU 2196 CA ILE A 275 13732 12719 20692 1105 -1663 1082 C
ATOM 2197 C ILE A 275 -242.444 58.870 38.419 1.00127.24 C
ANISOU 2197 C ILE A 275 13968 12997 21379 1148 -1934 1264 C
ATOM 2198 O ILE A 275 -242.420 59.941 37.800 1.00126.18 O
ANISOU 2198 O ILE A 275 13859 12755 21328 1138 -2063 1386 O
ATOM 2199 CB ILE A 275 -240.120 57.868 38.587 1.00102.76 C
ANISOU 2199 CB ILE A 275 11303 10209 17533 984 -1745 1185 C
ATOM 2200 CG1 ILE A 275 -238.958 57.575 39.538 1.00 90.16 C
ANISOU 2200 CG1 ILE A 275 9854 8735 15668 935 -1488 1008 C
ATOM 2201 CG2 ILE A 275 -239.605 58.775 37.471 1.00 90.59 C
ANISOU 2201 CG2 ILE A 275 9883 8572 15964 956 -1959 1402 C
ATOM 2202 CD1 ILE A 275 -237.762 56.919 38.861 1.00 92.53 C
ANISOU 2202 CD1 ILE A 275 10392 9210 15557 825 -1535 1086 C
ATOM 2203 N PHE A 276 -243.462 58.011 38.309 1.00130.94 N
ANISOU 2203 N PHE A 276 14295 13532 21926 1146 -1997 1261 N
ATOM 2204 CA PHE A 276 -244.707 58.415 37.662 1.00136.00 C
ANISOU 2204 CA PHE A 276 14765 14093 22817 1145 -2185 1366 C
ATOM 2205 C PHE A 276 -245.324 59.603 38.393 1.00141.49 C
ANISOU 2205 C PHE A 276 15272 14603 23884 1222 -2034 1249 C
ATOM 2206 O PHE A 276 -245.608 60.644 37.789 1.00141.38 O
ANISOU 2206 O PHE A 276 15226 14462 24031 1223 -2184 1370 O
ATOM 2207 CB PHE A 276 -245.677 57.231 37.612 1.00139.00 C
ANISOU 2207 CB PHE A 276 15009 14570 23235 1127 -2237 1347 C
ATOM 2208 CG PHE A 276 -246.943 57.506 36.846 1.00142.33 C
ANISOU 2208 CG PHE A 276 15267 14916 23897 1108 -2464 1473 C
ATOM 2209 CD1 PHE A 276 -246.942 57.522 35.460 1.00141.71 C
ANISOU 2209 CD1 PHE A 276 15310 14864 23668 1021 -2791 1710 C
ATOM 2210 CD2 PHE A 276 -248.139 57.728 37.512 1.00142.68 C
ANISOU 2210 CD2 PHE A 276 15039 14857 24316 1165 -2347 1352 C
ATOM 2211 CE1 PHE A 276 -248.105 57.767 34.753 1.00147.19 C
ANISOU 2211 CE1 PHE A 276 15859 15481 24587 994 -3017 1831 C
ATOM 2212 CE2 PHE A 276 -249.307 57.973 36.811 1.00146.75 C
ANISOU 2212 CE2 PHE A 276 15393 15288 25076 1146 -2565 1472 C
ATOM 2213 CZ PHE A 276 -249.290 57.993 35.430 1.00150.16 C
ANISOU 2213 CZ PHE A 276 15949 15745 25360 1061 -2910 1715 C
ATOM 2214 N THR A 277 -245.533 59.464 39.699 1.00141.07 N
ANISOU 2214 N THR A 277 15102 14531 23969 1278 -1732 1009 N
ATOM 2215 CA THR A 277 -245.788 60.587 40.585 1.00131.21 C
ANISOU 2215 CA THR A 277 13732 13115 23006 1339 -1519 852 C
ATOM 2216 C THR A 277 -244.466 61.038 41.205 1.00145.94 C
ANISOU 2216 C THR A 277 15788 14970 24691 1342 -1343 754 C
ATOM 2217 O THR A 277 -243.432 60.389 41.043 1.00151.82 O
ANISOU 2217 O THR A 277 16732 15837 25115 1302 -1367 795 O
ATOM 2218 CB THR A 277 -246.805 60.202 41.664 1.00122.39 C
ANISOU 2218 CB THR A 277 12392 11976 22135 1376 -1270 633 C
ATOM 2219 OG1 THR A 277 -246.134 59.603 42.779 1.00120.11 O
ANISOU 2219 OG1 THR A 277 12191 11772 21673 1374 -986 429 O
ATOM 2220 CG2 THR A 277 -247.806 59.200 41.111 1.00120.24 C
ANISOU 2220 CG2 THR A 277 11989 11786 21909 1348 -1430 720 C
ATOM 2221 N HIS A 278 -244.503 62.172 41.910 1.00143.18 N
ANISOU 2221 N HIS A 278 15378 14466 24561 1382 -1169 624 N
ATOM 2222 CA HIS A 278 -243.313 62.727 42.571 1.00144.93 C
ANISOU 2222 CA HIS A 278 15769 14652 24646 1376 -995 513 C
ATOM 2223 C HIS A 278 -242.148 62.885 41.593 1.00156.67 C
ANISOU 2223 C HIS A 278 17487 16184 25858 1326 -1206 719 C
ATOM 2224 O HIS A 278 -240.992 62.621 41.927 1.00169.61 O
ANISOU 2224 O HIS A 278 19309 17885 27251 1292 -1116 670 O
ATOM 2225 CB HIS A 278 -242.881 61.867 43.763 1.00147.20 C
ANISOU 2225 CB HIS A 278 16114 15036 24780 1364 -717 287 C
ATOM 2226 CG HIS A 278 -243.844 61.865 44.908 1.00148.53 C
ANISOU 2226 CG HIS A 278 16095 15149 25191 1392 -440 45 C
ATOM 2227 ND1 HIS A 278 -245.046 61.191 44.872 1.00160.76 N
ANISOU 2227 ND1 HIS A 278 17446 16735 26899 1405 -447 36 N
ATOM 2228 CD2 HIS A 278 -243.768 62.432 46.136 1.00148.48 C
ANISOU 2228 CD2 HIS A 278 16080 15054 25280 1392 -132 -206 C
ATOM 2229 CE1 HIS A 278 -245.675 61.355 46.022 1.00166.70 C
ANISOU 2229 CE1 HIS A 278 18070 17424 27844 1414 -147 -207 C
ATOM 2230 NE2 HIS A 278 -244.922 62.104 46.806 1.00161.52 N
ANISOU 2230 NE2 HIS A 278 17533 16695 27143 1403 51 -360 N
ATOM 2231 N GLN A 279 -242.453 63.317 40.367 1.00165.87 N
ANISOU 2231 N GLN A 279 18647 17312 27066 1309 -1487 952 N
ATOM 2232 CA GLN A 279 -241.425 63.378 39.331 1.00176.48 C
ANISOU 2232 CA GLN A 279 20216 18709 28128 1241 -1689 1160 C
ATOM 2233 C GLN A 279 -240.449 64.531 39.553 1.00180.16 C
ANISOU 2233 C GLN A 279 20804 19060 28588 1233 -1609 1139 C
ATOM 2234 O GLN A 279 -239.284 64.442 39.146 1.00187.43 O
ANISOU 2234 O GLN A 279 21936 20039 29239 1170 -1658 1228 O
ATOM 2235 CB GLN A 279 -242.090 63.482 37.953 1.00181.58 C
ANISOU 2235 CB GLN A 279 20837 19351 28806 1205 -2012 1412 C
ATOM 2236 CG GLN A 279 -241.202 64.003 36.821 1.00189.83 C
ANISOU 2236 CG GLN A 279 22098 20391 29636 1126 -2219 1636 C
ATOM 2237 CD GLN A 279 -240.039 63.080 36.480 1.00197.31 C
ANISOU 2237 CD GLN A 279 23283 21503 30182 1048 -2232 1691 C
ATOM 2238 OE1 GLN A 279 -239.979 61.935 36.930 1.00199.00 O
ANISOU 2238 OE1 GLN A 279 23497 21845 30268 1052 -2137 1593 O
ATOM 2239 NE2 GLN A 279 -239.108 63.581 35.674 1.00197.73 N
ANISOU 2239 NE2 GLN A 279 23539 21547 30044 970 -2344 1852 N
ATOM 2240 N GLY A 280 -240.885 65.596 40.227 1.00169.75 N
ANISOU 2240 N GLY A 280 19356 17575 27567 1289 -1473 1013 N
ATOM 2241 CA GLY A 280 -240.090 66.814 40.263 1.00160.44 C
ANISOU 2241 CA GLY A 280 18279 16265 26417 1276 -1442 1024 C
ATOM 2242 C GLY A 280 -238.804 66.699 41.062 1.00154.03 C
ANISOU 2242 C GLY A 280 17641 15491 25392 1239 -1242 879 C
ATOM 2243 O GLY A 280 -237.758 67.194 40.636 1.00158.06 O
ANISOU 2243 O GLY A 280 18324 15980 25752 1182 -1304 979 O
ATOM 2244 N SER A 281 -238.858 66.052 42.225 1.00152.31 N
ANISOU 2244 N SER A 281 17384 15326 25159 1257 -1003 646 N
ATOM 2245 CA SER A 281 -237.761 66.129 43.183 1.00147.90 C
ANISOU 2245 CA SER A 281 16969 14765 24461 1217 -792 470 C
ATOM 2246 C SER A 281 -236.544 65.330 42.709 1.00135.29 C
ANISOU 2246 C SER A 281 15588 13356 22460 1121 -874 575 C
ATOM 2247 O SER A 281 -236.579 64.612 41.704 1.00131.96 O
ANISOU 2247 O SER A 281 15206 13061 21870 1094 -1067 763 O
ATOM 2248 CB SER A 281 -238.215 65.635 44.557 1.00147.65 C
ANISOU 2248 CB SER A 281 16851 14751 24497 1239 -511 187 C
ATOM 2249 OG SER A 281 -239.130 66.543 45.150 1.00153.38 O
ANISOU 2249 OG SER A 281 17410 15328 25538 1289 -371 45 O
ATOM 2250 N CYS A 282 -235.450 65.481 43.457 1.00130.38 N
ANISOU 2250 N CYS A 282 15113 12800 21625 1037 -711 435 N
ATOM 2251 CA CYS A 282 -234.197 64.778 43.222 1.00131.17 C
ANISOU 2251 CA CYS A 282 15408 13125 21304 919 -733 485 C
ATOM 2252 C CYS A 282 -234.192 63.435 43.948 1.00126.84 C
ANISOU 2252 C CYS A 282 14879 12809 20505 876 -608 348 C
ATOM 2253 O CYS A 282 -234.914 63.224 44.923 1.00134.47 O
ANISOU 2253 O CYS A 282 15747 13761 21583 909 -445 165 O
ATOM 2254 CB CYS A 282 -233.002 65.609 43.699 1.00144.07 C
ANISOU 2254 CB CYS A 282 17174 14706 22858 844 -637 408 C
ATOM 2255 SG CYS A 282 -232.939 67.343 43.175 1.00150.95 S
ANISOU 2255 SG CYS A 282 18032 15266 24056 884 -726 517 S
ATOM 2256 N PHE A 283 -233.350 62.526 43.466 1.00127.83 N
ANISOU 2256 N PHE A 283 15134 13142 20292 795 -676 435 N
ATOM 2257 CA PHE A 283 -233.201 61.204 44.062 1.00132.82 C
ANISOU 2257 CA PHE A 283 15804 13992 20671 747 -583 334 C
ATOM 2258 C PHE A 283 -231.793 61.079 44.625 1.00136.09 C
ANISOU 2258 C PHE A 283 16370 14517 20820 646 -496 260 C
ATOM 2259 O PHE A 283 -230.813 61.258 43.894 1.00145.21 O
ANISOU 2259 O PHE A 283 17626 15705 21843 593 -586 381 O
ATOM 2260 CB PHE A 283 -233.458 60.099 43.034 1.00130.83 C
ANISOU 2260 CB PHE A 283 15558 13883 20267 742 -737 490 C
ATOM 2261 CG PHE A 283 -234.815 60.162 42.401 1.00131.99 C
ANISOU 2261 CG PHE A 283 15554 13932 20666 828 -863 585 C
ATOM 2262 CD1 PHE A 283 -235.874 60.773 43.052 1.00127.64 C
ANISOU 2262 CD1 PHE A 283 14832 13215 20448 915 -779 478 C
ATOM 2263 CD2 PHE A 283 -235.030 59.601 41.154 1.00133.69 C
ANISOU 2263 CD2 PHE A 283 15793 14215 20789 815 -1064 777 C
ATOM 2264 CE1 PHE A 283 -237.118 60.830 42.470 1.00133.87 C
ANISOU 2264 CE1 PHE A 283 15454 13904 21505 997 -908 573 C
ATOM 2265 CE2 PHE A 283 -236.271 59.654 40.566 1.00137.45 C
ANISOU 2265 CE2 PHE A 283 16125 14600 21499 883 -1210 876 C
ATOM 2266 CZ PHE A 283 -237.320 60.269 41.227 1.00141.36 C
ANISOU 2266 CZ PHE A 283 16427 14927 22357 980 -1140 780 C
ATOM 2267 N GLY A 284 -231.692 60.754 45.911 1.00130.99 N
ANISOU 2267 N GLY A 284 15742 13932 20097 607 -326 66 N
ATOM 2268 CA GLY A 284 -230.408 60.558 46.538 1.00130.79 C
ANISOU 2268 CA GLY A 284 15849 14016 19830 505 -266 -3 C
ATOM 2269 C GLY A 284 -229.663 59.376 45.948 1.00132.52 C
ANISOU 2269 C GLY A 284 16141 14433 19779 458 -355 107 C
ATOM 2270 O GLY A 284 -230.180 58.651 45.090 1.00119.37 O
ANISOU 2270 O GLY A 284 14438 12828 18088 496 -450 221 O
ATOM 2271 N PRO A 285 -228.425 59.147 46.413 1.00131.88 N
ANISOU 2271 N PRO A 285 16159 14448 19501 370 -326 69 N
ATOM 2272 CA PRO A 285 -227.653 57.993 45.928 1.00130.18 C
ANISOU 2272 CA PRO A 285 15998 14407 19057 329 -390 155 C
ATOM 2273 C PRO A 285 -228.255 56.652 46.319 1.00144.37 C
ANISOU 2273 C PRO A 285 17772 16333 20748 341 -362 114 C
ATOM 2274 O PRO A 285 -227.631 55.610 46.094 1.00151.36 O
ANISOU 2274 O PRO A 285 18700 17353 21456 308 -398 162 O
ATOM 2275 CB PRO A 285 -226.280 58.187 46.585 1.00115.92 C
ANISOU 2275 CB PRO A 285 14272 12645 17127 237 -357 98 C
ATOM 2276 CG PRO A 285 -226.549 59.019 47.790 1.00114.84 C
ANISOU 2276 CG PRO A 285 14141 12407 17085 213 -251 -65 C
ATOM 2277 CD PRO A 285 -227.669 59.943 47.397 1.00120.39 C
ANISOU 2277 CD PRO A 285 14765 12939 18041 300 -240 -58 C
ATOM 2278 N ILE A 286 -229.459 56.654 46.892 1.00149.26 N
ANISOU 2278 N ILE A 286 18319 16901 21490 384 -290 24 N
ATOM 2279 CA ILE A 286 -230.075 55.446 47.424 1.00140.46 C
ANISOU 2279 CA ILE A 286 17187 15897 20285 380 -241 -31 C
ATOM 2280 C ILE A 286 -231.471 55.188 46.873 1.00135.46 C
ANISOU 2280 C ILE A 286 16436 15224 19808 459 -269 8 C
ATOM 2281 O ILE A 286 -232.039 54.134 47.156 1.00139.85 O
ANISOU 2281 O ILE A 286 16969 15870 20299 453 -239 -20 O
ATOM 2282 CB ILE A 286 -230.107 55.466 48.968 1.00129.99 C
ANISOU 2282 CB ILE A 286 15901 14581 18907 316 -91 -210 C
ATOM 2283 CG1 ILE A 286 -230.879 56.682 49.481 1.00125.69 C
ANISOU 2283 CG1 ILE A 286 15296 13868 18592 347 20 -330 C
ATOM 2284 CG2 ILE A 286 -228.697 55.479 49.537 1.00129.11 C
ANISOU 2284 CG2 ILE A 286 15908 14535 18614 222 -101 -233 C
ATOM 2285 CD1 ILE A 286 -232.328 56.406 49.831 1.00123.10 C
ANISOU 2285 CD1 ILE A 286 14858 13503 18411 395 122 -411 C
ATOM 2286 N PHE A 287 -232.036 56.096 46.073 1.00134.57 N
ANISOU 2286 N PHE A 287 16246 14975 19908 527 -342 84 N
ATOM 2287 CA PHE A 287 -233.473 56.032 45.784 1.00127.58 C
ANISOU 2287 CA PHE A 287 15218 14022 19234 603 -362 98 C
ATOM 2288 C PHE A 287 -233.839 54.903 44.819 1.00122.08 C
ANISOU 2288 C PHE A 287 14508 13434 18442 610 -493 225 C
ATOM 2289 O PHE A 287 -234.490 53.928 45.206 1.00108.25 O
ANISOU 2289 O PHE A 287 12713 11762 16657 604 -444 172 O
ATOM 2290 CB PHE A 287 -233.960 57.378 45.251 1.00125.32 C
ANISOU 2290 CB PHE A 287 14846 13537 19233 675 -423 154 C
ATOM 2291 CG PHE A 287 -235.380 57.667 45.593 1.00124.71 C
ANISOU 2291 CG PHE A 287 14594 13339 19452 752 -363 81 C
ATOM 2292 CD1 PHE A 287 -235.705 58.691 46.472 1.00127.46 C
ANISOU 2292 CD1 PHE A 287 14880 13530 20020 781 -210 -70 C
ATOM 2293 CD2 PHE A 287 -236.394 56.898 45.056 1.00114.28 C
ANISOU 2293 CD2 PHE A 287 13163 12056 18203 791 -447 150 C
ATOM 2294 CE1 PHE A 287 -237.019 58.955 46.789 1.00127.33 C
ANISOU 2294 CE1 PHE A 287 14680 13389 20310 856 -131 -151 C
ATOM 2295 CE2 PHE A 287 -237.705 57.152 45.367 1.00132.44 C
ANISOU 2295 CE2 PHE A 287 15274 14239 20807 863 -388 82 C
ATOM 2296 CZ PHE A 287 -238.021 58.181 46.238 1.00138.39 C
ANISOU 2296 CZ PHE A 287 15953 14831 21799 899 -222 -71 C
ATOM 2297 N MET A 288 -233.470 55.036 43.542 1.00119.44 N
ANISOU 2297 N MET A 288 14219 13100 18065 610 -655 390 N
ATOM 2298 CA MET A 288 -233.676 53.949 42.587 1.00102.09 C
ANISOU 2298 CA MET A 288 12042 11011 15735 593 -775 500 C
ATOM 2299 C MET A 288 -232.717 52.786 42.818 1.00101.67 C
ANISOU 2299 C MET A 288 12102 11123 15404 525 -722 467 C
ATOM 2300 O MET A 288 -232.909 51.708 42.246 1.00113.12 O
ANISOU 2300 O MET A 288 13573 12669 16740 506 -783 517 O
ATOM 2301 CB MET A 288 -233.537 54.479 41.152 1.00116.06 C
ANISOU 2301 CB MET A 288 13854 12728 17515 590 -955 682 C
ATOM 2302 CG MET A 288 -233.684 53.451 40.017 1.00116.14 C
ANISOU 2302 CG MET A 288 13918 12845 17364 550 -1088 798 C
ATOM 2303 SD MET A 288 -235.297 52.636 39.887 1.00124.19 S
ANISOU 2303 SD MET A 288 14795 13875 18516 587 -1167 803 S
ATOM 2304 CE MET A 288 -235.133 51.800 38.313 1.00103.27 C
ANISOU 2304 CE MET A 288 12270 11324 15643 509 -1350 960 C
ATOM 2305 N THR A 289 -231.712 52.964 43.663 1.00 90.45 N
ANISOU 2305 N THR A 289 10750 9729 13888 487 -618 382 N
ATOM 2306 CA THR A 289 -230.752 51.915 43.950 1.00 90.52 C
ANISOU 2306 CA THR A 289 10849 9874 13673 430 -581 358 C
ATOM 2307 C THR A 289 -231.141 51.055 45.148 1.00 90.64 C
ANISOU 2307 C THR A 289 10847 9954 13639 412 -477 240 C
ATOM 2308 O THR A 289 -230.391 50.138 45.497 1.00 88.60 O
ANISOU 2308 O THR A 289 10656 9795 13212 366 -457 226 O
ATOM 2309 CB THR A 289 -229.392 52.545 44.182 1.00 87.84 C
ANISOU 2309 CB THR A 289 10586 9528 13262 387 -552 348 C
ATOM 2310 OG1 THR A 289 -229.480 53.377 45.337 1.00 87.42 O
ANISOU 2310 OG1 THR A 289 10514 9400 13303 384 -457 231 O
ATOM 2311 CG2 THR A 289 -229.026 53.417 42.995 1.00 70.47 C
ANISOU 2311 CG2 THR A 289 8412 7258 11105 390 -641 470 C
ATOM 2312 N ILE A 290 -232.278 51.326 45.786 1.00 76.54 N
ANISOU 2312 N ILE A 290 8971 8106 12005 442 -407 160 N
ATOM 2313 CA ILE A 290 -232.784 50.467 46.858 1.00 74.63 C
ANISOU 2313 CA ILE A 290 8720 7926 11710 409 -298 55 C
ATOM 2314 C ILE A 290 -233.255 49.143 46.263 1.00 83.36 C
ANISOU 2314 C ILE A 290 9810 9120 12744 408 -364 119 C
ATOM 2315 O ILE A 290 -232.869 48.082 46.777 1.00 69.86 O
ANISOU 2315 O ILE A 290 8166 7506 10874 358 -331 96 O
ATOM 2316 CB ILE A 290 -233.907 51.146 47.661 1.00 74.05 C
ANISOU 2316 CB ILE A 290 8545 7753 11836 434 -175 -64 C
ATOM 2317 CG1 ILE A 290 -233.339 52.045 48.752 1.00 88.22 C
ANISOU 2317 CG1 ILE A 290 10402 9496 13620 391 -54 -186 C
ATOM 2318 CG2 ILE A 290 -234.796 50.114 48.324 1.00 75.01 C
ANISOU 2318 CG2 ILE A 290 8627 7937 11936 405 -85 -133 C
ATOM 2319 CD1 ILE A 290 -234.332 53.105 49.231 1.00 86.75 C
ANISOU 2319 CD1 ILE A 290 10108 9164 13689 433 66 -299 C
ATOM 2320 N PRO A 291 -234.076 49.131 45.198 1.00 81.42 N
ANISOU 2320 N PRO A 291 9484 8841 12611 454 -469 205 N
ATOM 2321 CA PRO A 291 -234.441 47.832 44.613 1.00 74.59 C
ANISOU 2321 CA PRO A 291 8623 8061 11657 436 -536 258 C
ATOM 2322 C PRO A 291 -233.235 47.042 44.137 1.00 70.78 C
ANISOU 2322 C PRO A 291 8266 7670 10957 395 -580 312 C
ATOM 2323 O PRO A 291 -233.171 45.825 44.352 1.00 79.10 O
ANISOU 2323 O PRO A 291 9355 8802 11897 361 -561 297 O
ATOM 2324 CB PRO A 291 -235.379 48.217 43.456 1.00 74.75 C
ANISOU 2324 CB PRO A 291 8551 8016 11835 481 -673 355 C
ATOM 2325 CG PRO A 291 -235.910 49.544 43.828 1.00 78.73 C
ANISOU 2325 CG PRO A 291 8953 8389 12571 536 -635 318 C
ATOM 2326 CD PRO A 291 -234.764 50.235 44.501 1.00 74.90 C
ANISOU 2326 CD PRO A 291 8563 7892 12005 517 -545 261 C
ATOM 2327 N ALA A 292 -232.265 47.702 43.505 1.00 71.03 N
ANISOU 2327 N ALA A 292 8361 7684 10943 395 -630 372 N
ATOM 2328 CA ALA A 292 -231.052 46.997 43.104 1.00 62.84 C
ANISOU 2328 CA ALA A 292 7425 6723 9728 357 -643 406 C
ATOM 2329 C ALA A 292 -230.275 46.518 44.321 1.00 71.48 C
ANISOU 2329 C ALA A 292 8559 7865 10735 326 -553 329 C
ATOM 2330 O ALA A 292 -229.777 45.382 44.343 1.00 66.60 O
ANISOU 2330 O ALA A 292 7986 7315 10006 300 -551 334 O
ATOM 2331 CB ALA A 292 -230.185 47.891 42.226 1.00 45.96 C
ANISOU 2331 CB ALA A 292 5338 4550 7575 351 -692 480 C
ATOM 2332 N PHE A 293 -230.180 47.363 45.353 1.00 56.58 N
ANISOU 2332 N PHE A 293 6661 5935 8902 321 -485 259 N
ATOM 2333 CA PHE A 293 -229.523 46.958 46.593 1.00 71.15 C
ANISOU 2333 CA PHE A 293 8558 7825 10651 271 -420 192 C
ATOM 2334 C PHE A 293 -230.059 45.622 47.097 1.00 64.59 C
ANISOU 2334 C PHE A 293 7734 7057 9750 246 -395 170 C
ATOM 2335 O PHE A 293 -229.290 44.701 47.391 1.00 67.26 O
ANISOU 2335 O PHE A 293 8128 7451 9977 213 -410 187 O
ATOM 2336 CB PHE A 293 -229.701 48.040 47.659 1.00 70.82 C
ANISOU 2336 CB PHE A 293 8511 7723 10675 254 -338 98 C
ATOM 2337 CG PHE A 293 -228.842 47.842 48.880 1.00 83.83 C
ANISOU 2337 CG PHE A 293 10239 9412 12200 180 -300 41 C
ATOM 2338 CD1 PHE A 293 -227.475 48.097 48.832 1.00 75.44 C
ANISOU 2338 CD1 PHE A 293 9223 8363 11078 153 -352 75 C
ATOM 2339 CD2 PHE A 293 -229.401 47.421 50.079 1.00 77.81 C
ANISOU 2339 CD2 PHE A 293 9507 8675 11383 124 -216 -42 C
ATOM 2340 CE1 PHE A 293 -226.679 47.924 49.953 1.00 67.35 C
ANISOU 2340 CE1 PHE A 293 8268 7374 9949 77 -349 37 C
ATOM 2341 CE2 PHE A 293 -228.611 47.249 51.204 1.00 86.59 C
ANISOU 2341 CE2 PHE A 293 10714 9826 12362 37 -206 -80 C
ATOM 2342 CZ PHE A 293 -227.244 47.501 51.140 1.00 77.89 C
ANISOU 2342 CZ PHE A 293 9652 8735 11209 16 -286 -36 C
ATOM 2343 N PHE A 294 -231.382 45.489 47.182 1.00 66.94 N
ANISOU 2343 N PHE A 294 7966 7336 10133 261 -360 139 N
ATOM 2344 CA PHE A 294 -231.935 44.288 47.794 1.00 72.99 C
ANISOU 2344 CA PHE A 294 8741 8154 10838 222 -318 112 C
ATOM 2345 C PHE A 294 -232.079 43.134 46.806 1.00 59.92 C
ANISOU 2345 C PHE A 294 7083 6538 9144 234 -397 183 C
ATOM 2346 O PHE A 294 -231.985 41.976 47.219 1.00 70.32 O
ANISOU 2346 O PHE A 294 8443 7901 10374 196 -385 184 O
ATOM 2347 CB PHE A 294 -233.262 44.615 48.473 1.00 64.33 C
ANISOU 2347 CB PHE A 294 7568 7019 9856 216 -217 28 C
ATOM 2348 CG PHE A 294 -233.103 45.421 49.732 1.00 77.84 C
ANISOU 2348 CG PHE A 294 9316 8702 11557 172 -101 -74 C
ATOM 2349 CD1 PHE A 294 -232.581 44.842 50.879 1.00 69.92 C
ANISOU 2349 CD1 PHE A 294 8422 7754 10391 83 -50 -112 C
ATOM 2350 CD2 PHE A 294 -233.468 46.764 49.768 1.00 94.57 C
ANISOU 2350 CD2 PHE A 294 11372 10730 13829 209 -50 -131 C
ATOM 2351 CE1 PHE A 294 -232.434 45.583 52.043 1.00 83.29 C
ANISOU 2351 CE1 PHE A 294 10174 9425 12046 19 54 -213 C
ATOM 2352 CE2 PHE A 294 -233.320 47.513 50.932 1.00 78.01 C
ANISOU 2352 CE2 PHE A 294 9324 8601 11717 156 71 -246 C
ATOM 2353 CZ PHE A 294 -232.804 46.922 52.069 1.00 82.17 C
ANISOU 2353 CZ PHE A 294 9974 9196 12052 53 125 -291 C
ATOM 2354 N ALA A 295 -232.266 43.417 45.512 1.00 55.73 N
ANISOU 2354 N ALA A 295 6519 5986 8669 275 -480 245 N
ATOM 2355 CA ALA A 295 -232.299 42.359 44.500 1.00 52.05 C
ANISOU 2355 CA ALA A 295 6077 5557 8143 269 -551 301 C
ATOM 2356 C ALA A 295 -231.018 41.532 44.447 1.00 67.23 C
ANISOU 2356 C ALA A 295 8085 7521 9938 249 -553 319 C
ATOM 2357 O ALA A 295 -231.053 40.399 43.954 1.00 67.67 O
ANISOU 2357 O ALA A 295 8168 7602 9942 234 -577 336 O
ATOM 2358 CB ALA A 295 -232.548 42.949 43.109 1.00 40.70 C
ANISOU 2358 CB ALA A 295 4621 4090 6751 294 -649 370 C
ATOM 2359 N LYS A 296 -229.884 42.079 44.900 1.00 68.01 N
ANISOU 2359 N LYS A 296 8219 7617 10006 248 -532 314 N
ATOM 2360 CA LYS A 296 -228.639 41.316 44.885 1.00 61.91 C
ANISOU 2360 CA LYS A 296 7499 6870 9157 235 -538 333 C
ATOM 2361 C LYS A 296 -228.765 40.047 45.710 1.00 63.56 C
ANISOU 2361 C LYS A 296 7729 7102 9320 206 -523 319 C
ATOM 2362 O LYS A 296 -228.173 39.015 45.364 1.00 52.81 O
ANISOU 2362 O LYS A 296 6393 5746 7926 206 -540 342 O
ATOM 2363 CB LYS A 296 -227.482 42.162 45.423 1.00 56.45 C
ANISOU 2363 CB LYS A 296 6819 6167 8462 229 -528 329 C
ATOM 2364 CG LYS A 296 -227.060 43.334 44.561 1.00 63.59 C
ANISOU 2364 CG LYS A 296 7715 7041 9405 247 -541 355 C
ATOM 2365 CD LYS A 296 -226.010 44.168 45.290 1.00 55.25 C
ANISOU 2365 CD LYS A 296 6665 5970 8358 229 -529 340 C
ATOM 2366 CE LYS A 296 -225.814 45.519 44.621 1.00 59.04 C
ANISOU 2366 CE LYS A 296 7136 6404 8893 239 -533 362 C
ATOM 2367 NZ LYS A 296 -225.638 45.391 43.142 1.00 69.25 N
ANISOU 2367 NZ LYS A 296 8445 7699 10168 247 -553 422 N
ATOM 2368 N THR A 297 -229.530 40.111 46.803 1.00 54.18 N
ANISOU 2368 N THR A 297 6535 5917 8135 176 -481 280 N
ATOM 2369 CA THR A 297 -229.739 38.966 47.680 1.00 68.95 C
ANISOU 2369 CA THR A 297 8442 7806 9951 130 -465 277 C
ATOM 2370 C THR A 297 -230.362 37.771 46.953 1.00 66.76 C
ANISOU 2370 C THR A 297 8155 7530 9679 133 -484 296 C
ATOM 2371 O THR A 297 -230.219 36.634 47.416 1.00 64.95 O
ANISOU 2371 O THR A 297 7966 7303 9410 102 -489 314 O
ATOM 2372 CB THR A 297 -230.589 39.423 48.873 1.00 66.48 C
ANISOU 2372 CB THR A 297 8130 7496 9635 82 -389 219 C
ATOM 2373 OG1 THR A 297 -229.809 40.328 49.661 1.00 65.45 O
ANISOU 2373 OG1 THR A 297 8038 7363 9469 58 -377 196 O
ATOM 2374 CG2 THR A 297 -230.976 38.273 49.760 1.00 94.98 C
ANISOU 2374 CG2 THR A 297 11789 11124 13176 15 -362 221 C
ATOM 2375 N SER A 298 -231.002 37.990 45.801 1.00 63.26 N
ANISOU 2375 N SER A 298 7669 7080 9285 162 -508 300 N
ATOM 2376 CA SER A 298 -231.519 36.876 45.015 1.00 59.60 C
ANISOU 2376 CA SER A 298 7210 6618 8817 151 -538 311 C
ATOM 2377 C SER A 298 -230.434 35.867 44.652 1.00 74.03 C
ANISOU 2377 C SER A 298 9096 8436 10596 154 -553 332 C
ATOM 2378 O SER A 298 -230.749 34.705 44.362 1.00 64.26 O
ANISOU 2378 O SER A 298 7879 7187 9350 133 -560 330 O
ATOM 2379 CB SER A 298 -232.182 37.390 43.740 1.00 57.22 C
ANISOU 2379 CB SER A 298 6872 6312 8556 169 -591 324 C
ATOM 2380 OG SER A 298 -231.207 37.781 42.786 1.00 57.02 O
ANISOU 2380 OG SER A 298 6889 6284 8491 189 -619 350 O
ATOM 2381 N ALA A 299 -229.165 36.281 44.659 1.00 49.33 N
ANISOU 2381 N ALA A 299 5985 5302 7457 179 -553 346 N
ATOM 2382 CA ALA A 299 -228.083 35.342 44.398 1.00 46.34 C
ANISOU 2382 CA ALA A 299 5633 4898 7075 190 -555 359 C
ATOM 2383 C ALA A 299 -227.968 34.299 45.496 1.00 53.31 C
ANISOU 2383 C ALA A 299 6537 5760 7957 167 -564 378 C
ATOM 2384 O ALA A 299 -227.384 33.237 45.265 1.00 54.37 O
ANISOU 2384 O ALA A 299 6685 5853 8119 177 -571 389 O
ATOM 2385 CB ALA A 299 -226.759 36.090 44.243 1.00 53.43 C
ANISOU 2385 CB ALA A 299 6520 5790 7990 218 -550 370 C
ATOM 2386 N VAL A 300 -228.522 34.575 46.671 1.00 57.79 N
ANISOU 2386 N VAL A 300 7112 6348 8496 129 -560 382 N
ATOM 2387 CA VAL A 300 -228.514 33.644 47.788 1.00 49.42 C
ANISOU 2387 CA VAL A 300 6096 5273 7410 82 -575 415 C
ATOM 2388 C VAL A 300 -229.860 32.932 47.947 1.00 69.65 C
ANISOU 2388 C VAL A 300 8668 7838 9959 35 -542 399 C
ATOM 2389 O VAL A 300 -229.908 31.705 48.031 1.00 57.10 O
ANISOU 2389 O VAL A 300 7108 6210 8375 13 -558 426 O
ATOM 2390 CB VAL A 300 -228.115 34.381 49.083 1.00 55.22 C
ANISOU 2390 CB VAL A 300 6861 6029 8091 42 -585 428 C
ATOM 2391 CG1 VAL A 300 -228.110 33.415 50.259 1.00 59.85 C
ANISOU 2391 CG1 VAL A 300 7517 6600 8622 -29 -616 480 C
ATOM 2392 CG2 VAL A 300 -226.757 35.049 48.912 1.00 61.93 C
ANISOU 2392 CG2 VAL A 300 7687 6871 8970 81 -629 446 C
ATOM 2393 N TYR A 301 -230.978 33.673 47.993 1.00 58.53 N
ANISOU 2393 N TYR A 301 7222 6463 8556 17 -494 355 N
ATOM 2394 CA TYR A 301 -232.232 33.010 48.345 1.00 65.36 C
ANISOU 2394 CA TYR A 301 8081 7330 9425 -41 -452 340 C
ATOM 2395 C TYR A 301 -232.852 32.249 47.176 1.00 70.82 C
ANISOU 2395 C TYR A 301 8741 8002 10164 -30 -478 331 C
ATOM 2396 O TYR A 301 -233.600 31.295 47.415 1.00 64.47 O
ANISOU 2396 O TYR A 301 7945 7183 9367 -83 -461 333 O
ATOM 2397 CB TYR A 301 -233.253 33.997 48.947 1.00 52.76 C
ANISOU 2397 CB TYR A 301 6436 5762 7848 -70 -374 287 C
ATOM 2398 CG TYR A 301 -233.763 35.103 48.043 1.00 58.99 C
ANISOU 2398 CG TYR A 301 7134 6556 8723 -12 -379 252 C
ATOM 2399 CD1 TYR A 301 -234.657 34.839 47.012 1.00 59.63 C
ANISOU 2399 CD1 TYR A 301 7149 6631 8879 2 -413 248 C
ATOM 2400 CD2 TYR A 301 -233.388 36.425 48.259 1.00 51.64 C
ANISOU 2400 CD2 TYR A 301 6187 5628 7806 20 -361 229 C
ATOM 2401 CE1 TYR A 301 -235.128 35.854 46.198 1.00 79.24 C
ANISOU 2401 CE1 TYR A 301 9553 9109 11446 48 -446 239 C
ATOM 2402 CE2 TYR A 301 -233.861 37.450 47.453 1.00 57.56 C
ANISOU 2402 CE2 TYR A 301 6855 6364 8650 72 -377 213 C
ATOM 2403 CZ TYR A 301 -234.726 37.158 46.424 1.00 70.31 C
ANISOU 2403 CZ TYR A 301 8405 7971 10337 87 -427 226 C
ATOM 2404 OH TYR A 301 -235.199 38.159 45.615 1.00 75.84 O
ANISOU 2404 OH TYR A 301 9030 8651 11136 133 -473 233 O
ATOM 2405 N ASN A 302 -232.550 32.620 45.930 1.00 63.67 N
ANISOU 2405 N ASN A 302 7813 7096 9281 23 -518 323 N
ATOM 2406 CA ASN A 302 -233.061 31.839 44.805 1.00 45.12 C
ANISOU 2406 CA ASN A 302 5463 4729 6950 12 -551 310 C
ATOM 2407 C ASN A 302 -232.529 30.410 44.795 1.00 62.47 C
ANISOU 2407 C ASN A 302 7723 6875 9136 -5 -555 322 C
ATOM 2408 O ASN A 302 -233.349 29.478 44.723 1.00 67.47 O
ANISOU 2408 O ASN A 302 8361 7489 9787 -54 -556 312 O
ATOM 2409 CB ASN A 302 -232.778 32.556 43.480 1.00 47.64 C
ANISOU 2409 CB ASN A 302 5777 5061 7263 50 -592 303 C
ATOM 2410 CG ASN A 302 -233.899 33.499 43.082 1.00 64.12 C
ANISOU 2410 CG ASN A 302 7791 7173 9398 48 -625 299 C
ATOM 2411 OD1 ASN A 302 -235.009 33.409 43.606 1.00 72.94 O
ANISOU 2411 OD1 ASN A 302 8846 8295 10573 17 -611 287 O
ATOM 2412 ND2 ASN A 302 -233.621 34.397 42.143 1.00 65.21 N
ANISOU 2412 ND2 ASN A 302 7931 7320 9525 75 -670 314 N
ATOM 2413 N PRO A 303 -231.215 30.151 44.864 1.00 63.10 N
ANISOU 2413 N PRO A 303 7840 6921 9212 33 -558 342 N
ATOM 2414 CA PRO A 303 -230.777 28.750 44.973 1.00 56.34 C
ANISOU 2414 CA PRO A 303 7029 5993 8386 23 -563 357 C
ATOM 2415 C PRO A 303 -231.284 28.064 46.226 1.00 65.86 C
ANISOU 2415 C PRO A 303 8259 7180 9585 -36 -563 401 C
ATOM 2416 O PRO A 303 -231.480 26.841 46.213 1.00 71.67 O
ANISOU 2416 O PRO A 303 9029 7851 10351 -67 -568 411 O
ATOM 2417 CB PRO A 303 -229.241 28.848 44.959 1.00 59.15 C
ANISOU 2417 CB PRO A 303 7387 6313 8775 84 -569 376 C
ATOM 2418 CG PRO A 303 -228.934 30.266 45.324 1.00 61.61 C
ANISOU 2418 CG PRO A 303 7667 6688 9053 105 -572 387 C
ATOM 2419 CD PRO A 303 -230.065 31.077 44.787 1.00 56.69 C
ANISOU 2419 CD PRO A 303 7020 6123 8397 88 -560 351 C
ATOM 2420 N VAL A 304 -231.513 28.807 47.312 1.00 58.34 N
ANISOU 2420 N VAL A 304 7303 6276 8588 -64 -549 425 N
ATOM 2421 CA VAL A 304 -232.080 28.187 48.507 1.00 59.38 C
ANISOU 2421 CA VAL A 304 7479 6397 8685 -146 -532 464 C
ATOM 2422 C VAL A 304 -233.485 27.671 48.212 1.00 73.39 C
ANISOU 2422 C VAL A 304 9226 8175 10482 -204 -491 428 C
ATOM 2423 O VAL A 304 -233.866 26.580 48.650 1.00 72.89 O
ANISOU 2423 O VAL A 304 9206 8066 10422 -268 -486 459 O
ATOM 2424 CB VAL A 304 -232.074 29.178 49.689 1.00 56.13 C
ANISOU 2424 CB VAL A 304 7085 6043 8200 -182 -503 475 C
ATOM 2425 CG1 VAL A 304 -232.857 28.610 50.849 1.00 63.46 C
ANISOU 2425 CG1 VAL A 304 8072 6972 9069 -293 -456 501 C
ATOM 2426 CG2 VAL A 304 -230.648 29.487 50.138 1.00 54.78 C
ANISOU 2426 CG2 VAL A 304 6948 5858 8006 -148 -568 526 C
ATOM 2427 N ILE A 305 -234.257 28.429 47.427 1.00 65.33 N
ANISOU 2427 N ILE A 305 8130 7201 9493 -185 -475 370 N
ATOM 2428 CA ILE A 305 -235.654 28.093 47.166 1.00 74.26 C
ANISOU 2428 CA ILE A 305 9207 8340 10671 -242 -451 337 C
ATOM 2429 C ILE A 305 -235.773 27.034 46.074 1.00 55.76 C
ANISOU 2429 C ILE A 305 6881 5946 8360 -250 -500 322 C
ATOM 2430 O ILE A 305 -236.490 26.043 46.233 1.00 73.42 O
ANISOU 2430 O ILE A 305 9126 8148 10622 -321 -489 323 O
ATOM 2431 CB ILE A 305 -236.444 29.367 46.806 1.00 69.48 C
ANISOU 2431 CB ILE A 305 8497 7789 10112 -218 -437 293 C
ATOM 2432 CG1 ILE A 305 -236.640 30.231 48.048 1.00 62.20 C
ANISOU 2432 CG1 ILE A 305 7558 6901 9174 -240 -351 282 C
ATOM 2433 CG2 ILE A 305 -237.791 29.011 46.199 1.00 72.93 C
ANISOU 2433 CG2 ILE A 305 8852 8225 10632 -265 -450 263 C
ATOM 2434 CD1 ILE A 305 -237.023 31.644 47.730 1.00 63.06 C
ANISOU 2434 CD1 ILE A 305 7572 7041 9348 -188 -340 242 C
ATOM 2435 N TYR A 306 -235.075 27.223 44.954 1.00 50.16 N
ANISOU 2435 N TYR A 306 6185 5229 7643 -190 -546 301 N
ATOM 2436 CA TYR A 306 -235.223 26.364 43.784 1.00 52.96 C
ANISOU 2436 CA TYR A 306 6570 5542 8011 -210 -583 264 C
ATOM 2437 C TYR A 306 -234.358 25.104 43.814 1.00 63.25 C
ANISOU 2437 C TYR A 306 7953 6752 9328 -206 -572 271 C
ATOM 2438 O TYR A 306 -234.729 24.099 43.194 1.00 75.42 O
ANISOU 2438 O TYR A 306 9527 8237 10891 -252 -582 234 O
ATOM 2439 CB TYR A 306 -234.897 27.151 42.513 1.00 50.98 C
ANISOU 2439 CB TYR A 306 6318 5324 7727 -169 -622 232 C
ATOM 2440 CG TYR A 306 -235.961 28.153 42.152 1.00 68.55 C
ANISOU 2440 CG TYR A 306 8462 7614 9971 -183 -666 230 C
ATOM 2441 CD1 TYR A 306 -235.993 29.414 42.743 1.00 75.26 C
ANISOU 2441 CD1 TYR A 306 9248 8509 10839 -139 -649 252 C
ATOM 2442 CD2 TYR A 306 -236.949 27.834 41.236 1.00 74.05 C
ANISOU 2442 CD2 TYR A 306 9141 8314 10682 -243 -734 206 C
ATOM 2443 CE1 TYR A 306 -236.983 30.324 42.423 1.00 71.06 C
ANISOU 2443 CE1 TYR A 306 8623 8012 10364 -142 -693 253 C
ATOM 2444 CE2 TYR A 306 -237.934 28.738 40.909 1.00 83.73 C
ANISOU 2444 CE2 TYR A 306 10273 9585 11958 -252 -798 219 C
ATOM 2445 CZ TYR A 306 -237.949 29.975 41.502 1.00 72.87 C
ANISOU 2445 CZ TYR A 306 8821 8241 10624 -195 -775 244 C
ATOM 2446 OH TYR A 306 -238.944 30.845 41.154 1.00 68.37 O
ANISOU 2446 OH TYR A 306 8142 7693 10141 -196 -844 259 O
ATOM 2447 N ILE A 307 -233.214 25.125 44.483 1.00 61.88 N
ANISOU 2447 N ILE A 307 7805 6548 9158 -155 -561 314 N
ATOM 2448 CA ILE A 307 -232.296 23.995 44.493 1.00 65.45 C
ANISOU 2448 CA ILE A 307 8310 6893 9666 -133 -561 328 C
ATOM 2449 C ILE A 307 -232.232 23.345 45.867 1.00 68.55 C
ANISOU 2449 C ILE A 307 8733 7236 10077 -168 -575 415 C
ATOM 2450 O ILE A 307 -232.406 22.134 45.997 1.00 65.25 O
ANISOU 2450 O ILE A 307 8356 6725 9711 -208 -581 432 O
ATOM 2451 CB ILE A 307 -230.890 24.418 44.012 1.00 65.57 C
ANISOU 2451 CB ILE A 307 8320 6890 9705 -45 -553 314 C
ATOM 2452 CG1 ILE A 307 -230.935 24.820 42.538 1.00 55.23 C
ANISOU 2452 CG1 ILE A 307 7016 5612 8359 -37 -529 228 C
ATOM 2453 CG2 ILE A 307 -229.898 23.280 44.176 1.00 59.93 C
ANISOU 2453 CG2 ILE A 307 7630 6046 9097 -11 -552 335 C
ATOM 2454 CD1 ILE A 307 -229.816 25.755 42.139 1.00 58.47 C
ANISOU 2454 CD1 ILE A 307 7405 6051 8761 31 -505 218 C
ATOM 2455 N MET A 308 -232.001 24.143 46.909 1.00 67.51 N
ANISOU 2455 N MET A 308 8593 7161 9895 -167 -584 473 N
ATOM 2456 CA MET A 308 -231.826 23.585 48.244 1.00 62.94 C
ANISOU 2456 CA MET A 308 8071 6542 9303 -217 -611 569 C
ATOM 2457 C MET A 308 -233.119 22.996 48.793 1.00 69.12 C
ANISOU 2457 C MET A 308 8881 7327 10054 -328 -574 581 C
ATOM 2458 O MET A 308 -233.080 22.029 49.560 1.00 80.86 O
ANISOU 2458 O MET A 308 10437 8740 11549 -387 -598 658 O
ATOM 2459 CB MET A 308 -231.285 24.656 49.183 1.00 68.76 C
ANISOU 2459 CB MET A 308 8811 7348 9966 -210 -629 613 C
ATOM 2460 CG MET A 308 -230.466 24.110 50.316 1.00 95.31 C
ANISOU 2460 CG MET A 308 12242 10649 13322 -237 -704 728 C
ATOM 2461 SD MET A 308 -228.890 24.971 50.419 1.00118.30 S
ANISOU 2461 SD MET A 308 15118 13570 16260 -148 -777 759 S
ATOM 2462 CE MET A 308 -228.423 25.028 48.691 1.00103.14 C
ANISOU 2462 CE MET A 308 13110 11622 14456 -34 -732 656 C
ATOM 2463 N MET A 309 -234.265 23.563 48.429 1.00 83.29 N
ANISOU 2463 N MET A 309 10619 9200 11829 -362 -520 512 N
ATOM 2464 CA MET A 309 -235.537 22.998 48.853 1.00 82.77 C
ANISOU 2464 CA MET A 309 10553 9134 11762 -470 -472 512 C
ATOM 2465 C MET A 309 -236.009 21.876 47.943 1.00 84.07 C
ANISOU 2465 C MET A 309 10718 9223 12002 -495 -488 476 C
ATOM 2466 O MET A 309 -236.974 21.187 48.285 1.00 97.32 O
ANISOU 2466 O MET A 309 12401 10879 13698 -594 -455 484 O
ATOM 2467 CB MET A 309 -236.591 24.099 48.930 1.00 77.04 C
ANISOU 2467 CB MET A 309 9738 8511 11020 -495 -406 453 C
ATOM 2468 CG MET A 309 -236.316 25.081 50.044 1.00 73.78 C
ANISOU 2468 CG MET A 309 9345 8161 10527 -504 -361 476 C
ATOM 2469 SD MET A 309 -237.662 26.234 50.325 1.00 91.88 S
ANISOU 2469 SD MET A 309 11526 10542 12841 -544 -249 396 S
ATOM 2470 CE MET A 309 -237.109 26.930 51.876 1.00103.76 C
ANISOU 2470 CE MET A 309 13123 12087 14214 -593 -185 427 C
ATOM 2471 N ASN A 310 -235.360 21.690 46.801 1.00 87.12 N
ANISOU 2471 N ASN A 310 11104 9568 12431 -421 -528 429 N
ATOM 2472 CA ASN A 310 -235.597 20.525 45.961 1.00 95.33 C
ANISOU 2472 CA ASN A 310 12173 10515 13535 -451 -542 386 C
ATOM 2473 C ASN A 310 -235.189 19.263 46.717 1.00 86.01 C
ANISOU 2473 C ASN A 310 11069 9206 12404 -484 -552 463 C
ATOM 2474 O ASN A 310 -234.041 19.132 47.149 1.00 87.46 O
ANISOU 2474 O ASN A 310 11288 9331 12613 -422 -583 524 O
ATOM 2475 CB ASN A 310 -234.803 20.688 44.663 1.00101.91 C
ANISOU 2475 CB ASN A 310 13009 11330 14381 -370 -558 312 C
ATOM 2476 CG ASN A 310 -235.101 19.620 43.641 1.00102.04 C
ANISOU 2476 CG ASN A 310 13066 11260 14444 -412 -559 236 C
ATOM 2477 OD1 ASN A 310 -235.181 18.435 43.963 1.00 98.40 O
ANISOU 2477 OD1 ASN A 310 12652 10687 14047 -457 -555 257 O
ATOM 2478 ND2 ASN A 310 -235.246 20.036 42.384 1.00 87.63 N
ANISOU 2478 ND2 ASN A 310 11236 9479 12578 -408 -569 149 N
ATOM 2479 N LYS A 311 -236.140 18.343 46.897 1.00 99.79 N
ANISOU 2479 N LYS A 311 12836 10901 14179 -587 -537 468 N
ATOM 2480 CA LYS A 311 -235.875 17.140 47.685 1.00112.15 C
ANISOU 2480 CA LYS A 311 14483 12335 15794 -635 -553 559 C
ATOM 2481 C LYS A 311 -234.678 16.361 47.149 1.00101.76 C
ANISOU 2481 C LYS A 311 13207 10875 14583 -548 -593 555 C
ATOM 2482 O LYS A 311 -233.916 15.774 47.929 1.00 81.17 O
ANISOU 2482 O LYS A 311 10649 8163 12027 -532 -638 661 O
ATOM 2483 CB LYS A 311 -237.124 16.254 47.712 1.00115.34 C
ANISOU 2483 CB LYS A 311 14897 12699 16228 -764 -523 546 C
ATOM 2484 CG LYS A 311 -236.983 14.959 48.495 1.00120.26 C
ANISOU 2484 CG LYS A 311 15615 13174 16906 -833 -541 648 C
ATOM 2485 CD LYS A 311 -238.253 14.126 48.386 1.00120.17 C
ANISOU 2485 CD LYS A 311 15604 13124 16933 -968 -503 620 C
ATOM 2486 CE LYS A 311 -238.152 12.834 49.177 1.00120.12 C
ANISOU 2486 CE LYS A 311 15701 12958 16980 -1048 -521 733 C
ATOM 2487 NZ LYS A 311 -239.371 11.993 49.014 1.00119.21 N
ANISOU 2487 NZ LYS A 311 15583 12796 16915 -1188 -480 701 N
ATOM 2488 N GLN A 312 -234.483 16.370 45.830 1.00 98.18 N
ANISOU 2488 N GLN A 312 12730 10408 14166 -495 -577 436 N
ATOM 2489 CA GLN A 312 -233.373 15.644 45.224 1.00 94.30 C
ANISOU 2489 CA GLN A 312 12265 9772 13793 -414 -577 401 C
ATOM 2490 C GLN A 312 -232.034 16.271 45.601 1.00 98.22 C
ANISOU 2490 C GLN A 312 12730 10272 14315 -300 -603 457 C
ATOM 2491 O GLN A 312 -231.224 15.654 46.305 1.00 88.62 O
ANISOU 2491 O GLN A 312 11532 8936 13203 -264 -650 554 O
ATOM 2492 CB GLN A 312 -233.554 15.609 43.705 1.00106.77 C
ANISOU 2492 CB GLN A 312 13845 11355 15368 -412 -533 243 C
ATOM 2493 CG GLN A 312 -233.294 14.256 43.068 1.00115.47 C
ANISOU 2493 CG GLN A 312 15005 12272 16596 -423 -503 171 C
ATOM 2494 CD GLN A 312 -233.457 14.289 41.561 1.00126.68 C
ANISOU 2494 CD GLN A 312 16453 13709 17972 -444 -453 4 C
ATOM 2495 OE1 GLN A 312 -233.808 15.322 40.983 1.00123.29 O
ANISOU 2495 OE1 GLN A 312 16000 13431 17414 -454 -460 -40 O
ATOM 2496 NE2 GLN A 312 -233.202 13.157 40.914 1.00136.63 N
ANISOU 2496 NE2 GLN A 312 17773 14804 19334 -460 -405 -90 N
ATOM 2497 N PHE A 313 -231.793 17.510 45.145 1.00 99.33 N
ANISOU 2497 N PHE A 313 12821 10547 14374 -247 -584 407 N
ATOM 2498 CA PHE A 313 -230.531 18.196 45.418 1.00 91.68 C
ANISOU 2498 CA PHE A 313 11811 9590 13432 -147 -604 449 C
ATOM 2499 C PHE A 313 -230.150 18.113 46.892 1.00 89.28 C
ANISOU 2499 C PHE A 313 11525 9262 13137 -157 -684 605 C
ATOM 2500 O PHE A 313 -228.990 17.842 47.229 1.00 75.29 O
ANISOU 2500 O PHE A 313 9734 7395 11478 -86 -736 670 O
ATOM 2501 CB PHE A 313 -230.613 19.666 44.986 1.00 81.41 C
ANISOU 2501 CB PHE A 313 10464 8454 12013 -121 -581 399 C
ATOM 2502 CG PHE A 313 -230.478 19.892 43.490 1.00 89.30 C
ANISOU 2502 CG PHE A 313 11457 9469 13002 -94 -520 266 C
ATOM 2503 CD1 PHE A 313 -229.226 20.007 42.900 1.00 87.44 C
ANISOU 2503 CD1 PHE A 313 11198 9183 12841 -8 -479 221 C
ATOM 2504 CD2 PHE A 313 -231.603 20.028 42.680 1.00 88.77 C
ANISOU 2504 CD2 PHE A 313 11409 9469 12849 -166 -507 189 C
ATOM 2505 CE1 PHE A 313 -229.096 20.231 41.525 1.00 80.50 C
ANISOU 2505 CE1 PHE A 313 10339 8324 11925 -5 -405 96 C
ATOM 2506 CE2 PHE A 313 -231.478 20.254 41.304 1.00 80.03 C
ANISOU 2506 CE2 PHE A 313 10325 8382 11700 -164 -465 77 C
ATOM 2507 CZ PHE A 313 -230.219 20.355 40.729 1.00 64.03 C
ANISOU 2507 CZ PHE A 313 8298 6308 9721 -89 -405 28 C
ATOM 2508 N ARG A 314 -231.119 18.318 47.786 1.00 78.35 N
ANISOU 2508 N ARG A 314 10176 7956 11637 -255 -695 666 N
ATOM 2509 CA ARG A 314 -230.800 18.401 49.208 1.00 84.29 C
ANISOU 2509 CA ARG A 314 10972 8711 12344 -292 -767 810 C
ATOM 2510 C ARG A 314 -230.093 17.138 49.688 1.00 91.16 C
ANISOU 2510 C ARG A 314 11887 9397 13351 -284 -849 920 C
ATOM 2511 O ARG A 314 -229.035 17.214 50.324 1.00 87.89 O
ANISOU 2511 O ARG A 314 11469 8937 12987 -237 -944 1022 O
ATOM 2512 CB ARG A 314 -232.069 18.662 50.016 1.00 77.40 C
ANISOU 2512 CB ARG A 314 10144 7937 11329 -421 -728 836 C
ATOM 2513 CG ARG A 314 -231.817 19.240 51.397 1.00 78.96 C
ANISOU 2513 CG ARG A 314 10396 8196 11407 -476 -771 947 C
ATOM 2514 CD ARG A 314 -233.061 19.139 52.276 1.00100.73 C
ANISOU 2514 CD ARG A 314 13217 11010 14044 -627 -707 975 C
ATOM 2515 NE ARG A 314 -234.282 19.548 51.583 1.00100.44 N
ANISOU 2515 NE ARG A 314 13107 11059 13995 -652 -598 850 N
ATOM 2516 CZ ARG A 314 -235.199 18.706 51.115 1.00109.16 C
ANISOU 2516 CZ ARG A 314 14203 12115 15160 -710 -557 811 C
ATOM 2517 NH1 ARG A 314 -235.043 17.397 51.260 1.00118.51 N
ANISOU 2517 NH1 ARG A 314 15455 13157 16415 -748 -601 882 N
ATOM 2518 NH2 ARG A 314 -236.274 19.172 50.498 1.00121.64 N
ANISOU 2518 NH2 ARG A 314 15698 13776 16742 -732 -483 707 N
ATOM 2519 N ASN A 315 -230.643 15.963 49.355 1.00 97.14 N
ANISOU 2519 N ASN A 315 12681 10037 14190 -328 -827 902 N
ATOM 2520 CA ASN A 315 -230.011 14.710 49.761 1.00 91.03 C
ANISOU 2520 CA ASN A 315 11948 9063 13578 -317 -907 1008 C
ATOM 2521 C ASN A 315 -228.681 14.497 49.044 1.00 84.08 C
ANISOU 2521 C ASN A 315 10988 8061 12899 -170 -924 967 C
ATOM 2522 O ASN A 315 -227.707 14.040 49.656 1.00 93.32 O
ANISOU 2522 O ASN A 315 12148 9103 14207 -121 -1032 1091 O
ATOM 2523 CB ASN A 315 -230.958 13.535 49.509 1.00106.51 C
ANISOU 2523 CB ASN A 315 13965 10918 15587 -404 -866 983 C
ATOM 2524 CG ASN A 315 -232.302 13.706 50.201 1.00116.33 C
ANISOU 2524 CG ASN A 315 15268 12275 16658 -556 -829 1016 C
ATOM 2525 OD1 ASN A 315 -232.465 14.573 51.062 1.00125.11 O
ANISOU 2525 OD1 ASN A 315 16398 13521 17618 -603 -838 1077 O
ATOM 2526 ND2 ASN A 315 -233.274 12.879 49.824 1.00106.10 N
ANISOU 2526 ND2 ASN A 315 14000 10921 15392 -640 -776 965 N
ATOM 2527 N CYS A 316 -228.624 14.808 47.746 1.00 73.73 N
ANISOU 2527 N CYS A 316 9618 6781 11613 -108 -818 796 N
ATOM 2528 CA CYS A 316 -227.352 14.791 47.028 1.00 84.57 C
ANISOU 2528 CA CYS A 316 10907 8063 13162 23 -795 733 C
ATOM 2529 C CYS A 316 -226.291 15.626 47.742 1.00 84.93 C
ANISOU 2529 C CYS A 316 10889 8157 13222 90 -884 836 C
ATOM 2530 O CYS A 316 -225.198 15.130 48.035 1.00 87.40 O
ANISOU 2530 O CYS A 316 11145 8323 13739 168 -959 913 O
ATOM 2531 CB CYS A 316 -227.549 15.286 45.595 1.00114.16 C
ANISOU 2531 CB CYS A 316 14629 11888 16857 47 -660 538 C
ATOM 2532 SG CYS A 316 -228.649 14.275 44.590 1.00119.87 S
ANISOU 2532 SG CYS A 316 15428 12542 17576 -37 -569 399 S
ATOM 2533 N MET A 317 -226.607 16.888 48.062 1.00 82.47 N
ANISOU 2533 N MET A 317 10579 8042 12712 57 -887 842 N
ATOM 2534 CA MET A 317 -225.611 17.768 48.675 1.00 83.12 C
ANISOU 2534 CA MET A 317 10606 8180 12796 108 -969 921 C
ATOM 2535 C MET A 317 -225.196 17.283 50.059 1.00 85.50 C
ANISOU 2535 C MET A 317 10950 8401 13137 71 -1136 1119 C
ATOM 2536 O MET A 317 -224.034 17.456 50.453 1.00 77.51 O
ANISOU 2536 O MET A 317 9869 7336 12243 136 -1240 1202 O
ATOM 2537 CB MET A 317 -226.145 19.200 48.746 1.00 85.90 C
ANISOU 2537 CB MET A 317 10966 8745 12928 68 -929 877 C
ATOM 2538 CG MET A 317 -226.384 19.837 47.374 1.00109.35 C
ANISOU 2538 CG MET A 317 13891 11795 15861 108 -797 709 C
ATOM 2539 SD MET A 317 -227.305 21.385 47.435 1.00109.09 S
ANISOU 2539 SD MET A 317 13871 11983 15595 52 -757 665 S
ATOM 2540 CE MET A 317 -226.691 22.015 48.995 1.00111.61 C
ANISOU 2540 CE MET A 317 14203 12345 15857 29 -875 811 C
ATOM 2541 N VAL A 318 -226.117 16.670 50.807 1.00 76.86 N
ANISOU 2541 N VAL A 318 9967 7291 11943 -44 -1170 1203 N
ATOM 2542 CA VAL A 318 -225.768 16.156 52.129 1.00 86.35 C
ANISOU 2542 CA VAL A 318 11241 8413 13154 -105 -1339 1407 C
ATOM 2543 C VAL A 318 -224.751 15.032 52.001 1.00102.37 C
ANISOU 2543 C VAL A 318 13209 10207 15482 -12 -1434 1483 C
ATOM 2544 O VAL A 318 -223.766 14.965 52.748 1.00112.32 O
ANISOU 2544 O VAL A 318 14442 11392 16843 16 -1602 1634 O
ATOM 2545 CB VAL A 318 -227.026 15.688 52.879 1.00 82.39 C
ANISOU 2545 CB VAL A 318 10883 7940 12482 -264 -1326 1471 C
ATOM 2546 CG1 VAL A 318 -226.629 14.892 54.119 1.00 74.33 C
ANISOU 2546 CG1 VAL A 318 9958 6795 11489 -337 -1507 1695 C
ATOM 2547 CG2 VAL A 318 -227.889 16.879 53.252 1.00 81.29 C
ANISOU 2547 CG2 VAL A 318 10789 8022 12077 -355 -1245 1417 C
ATOM 2548 N THR A 319 -224.975 14.132 51.045 1.00 97.39 N
ANISOU 2548 N THR A 319 12551 9446 15007 35 -1332 1376 N
ATOM 2549 CA THR A 319 -224.029 13.049 50.812 1.00 96.13 C
ANISOU 2549 CA THR A 319 12317 9039 15170 136 -1391 1418 C
ATOM 2550 C THR A 319 -222.674 13.586 50.372 1.00 93.26 C
ANISOU 2550 C THR A 319 11792 8649 14994 279 -1400 1377 C
ATOM 2551 O THR A 319 -221.627 13.090 50.808 1.00 87.18 O
ANISOU 2551 O THR A 319 10941 7712 14470 351 -1540 1502 O
ATOM 2552 CB THR A 319 -224.586 12.097 49.760 1.00 90.36 C
ANISOU 2552 CB THR A 319 11597 8187 14550 149 -1245 1268 C
ATOM 2553 OG1 THR A 319 -225.851 11.587 50.199 1.00102.80 O
ANISOU 2553 OG1 THR A 319 13308 9783 15966 7 -1241 1312 O
ATOM 2554 CG2 THR A 319 -223.639 10.961 49.555 1.00 96.83 C
ANISOU 2554 CG2 THR A 319 12337 8730 15725 254 -1289 1301 C
ATOM 2555 N THR A 320 -222.673 14.596 49.501 1.00 77.70 N
ANISOU 2555 N THR A 320 9764 6832 12925 316 -1257 1209 N
ATOM 2556 CA THR A 320 -221.418 15.158 49.017 1.00 75.73 C
ANISOU 2556 CA THR A 320 9360 6566 12846 439 -1237 1156 C
ATOM 2557 C THR A 320 -220.663 15.850 50.142 1.00 89.00 C
ANISOU 2557 C THR A 320 11005 8304 14506 433 -1429 1328 C
ATOM 2558 O THR A 320 -219.450 15.661 50.301 1.00 91.48 O
ANISOU 2558 O THR A 320 11187 8490 15081 526 -1527 1399 O
ATOM 2559 CB THR A 320 -221.692 16.131 47.871 1.00 75.84 C
ANISOU 2559 CB THR A 320 9353 6744 12718 452 -1046 954 C
ATOM 2560 OG1 THR A 320 -222.248 15.412 46.765 1.00 68.58 O
ANISOU 2560 OG1 THR A 320 8467 5753 11836 452 -884 792 O
ATOM 2561 CG2 THR A 320 -220.412 16.832 47.430 1.00 71.85 C
ANISOU 2561 CG2 THR A 320 8694 6242 12364 558 -1013 904 C
ATOM 2562 N LEU A 321 -221.368 16.646 50.937 1.00 90.28 N
ANISOU 2562 N LEU A 321 11281 8650 14371 319 -1484 1392 N
ATOM 2563 CA LEU A 321 -220.755 17.358 52.047 1.00 95.86 C
ANISOU 2563 CA LEU A 321 11989 9427 15008 283 -1665 1545 C
ATOM 2564 C LEU A 321 -220.213 16.384 53.083 1.00103.66 C
ANISOU 2564 C LEU A 321 12998 10239 16149 263 -1895 1767 C
ATOM 2565 O LEU A 321 -219.163 16.618 53.680 1.00100.64 O
ANISOU 2565 O LEU A 321 12539 9816 15885 294 -2072 1892 O
ATOM 2566 CB LEU A 321 -221.761 18.317 52.681 1.00 83.50 C
ANISOU 2566 CB LEU A 321 10563 8079 13085 148 -1645 1545 C
ATOM 2567 CG LEU A 321 -222.024 19.549 51.816 1.00 79.02 C
ANISOU 2567 CG LEU A 321 9949 7683 12393 178 -1476 1365 C
ATOM 2568 CD1 LEU A 321 -223.103 20.424 52.427 1.00 73.73 C
ANISOU 2568 CD1 LEU A 321 9403 7200 11411 53 -1440 1354 C
ATOM 2569 CD2 LEU A 321 -220.723 20.321 51.617 1.00 70.62 C
ANISOU 2569 CD2 LEU A 321 8744 6629 11462 269 -1520 1357 C
ATOM 2570 N CYS A 322 -220.923 15.278 53.276 1.00109.62 N
ANISOU 2570 N CYS A 322 13855 10881 16914 208 -1902 1822 N
ATOM 2571 CA CYS A 322 -220.532 14.304 54.260 1.00121.30 C
ANISOU 2571 CA CYS A 322 15380 12185 18524 174 -2127 2050 C
ATOM 2572 C CYS A 322 -219.615 13.181 53.774 1.00125.85 C
ANISOU 2572 C CYS A 322 15809 12484 19524 316 -2174 2077 C
ATOM 2573 O CYS A 322 -219.641 12.034 54.233 1.00132.28 O
ANISOU 2573 O CYS A 322 16673 13104 20483 296 -2296 2221 O
ATOM 2574 CB CYS A 322 -221.716 13.721 55.020 1.00131.91 C
ANISOU 2574 CB CYS A 322 16933 13543 19645 10 -2150 2147 C
ATOM 2575 SG CYS A 322 -221.700 14.273 56.698 1.00143.34 S
ANISOU 2575 SG CYS A 322 18546 15107 20811 -165 -2377 2377 S
ATOM 2576 N CYS A 323 -218.779 13.540 52.803 1.00118.08 N
ANISOU 2576 N CYS A 323 14637 11475 18754 461 -2064 1929 N
ATOM 2577 CA CYS A 323 -217.739 12.654 52.283 1.00117.50 C
ANISOU 2577 CA CYS A 323 14381 11141 19122 613 -2078 1923 C
ATOM 2578 C CYS A 323 -218.292 11.312 51.804 1.00111.22 C
ANISOU 2578 C CYS A 323 13635 10149 18474 627 -1983 1872 C
ATOM 2579 O CYS A 323 -217.606 10.293 51.855 1.00117.14 O
ANISOU 2579 O CYS A 323 14286 10751 19470 687 -2026 1901 O
ATOM 2580 CB CYS A 323 -216.665 12.424 53.349 1.00127.70 C
ANISOU 2580 CB CYS A 323 15591 12389 20540 613 -2341 2127 C
ATOM 2581 SG CYS A 323 -216.324 13.874 54.375 1.00128.44 S
ANISOU 2581 SG CYS A 323 15724 12690 20388 525 -2541 2268 S
ATOM 2582 N GLY A 324 -219.542 11.317 51.351 1.00102.40 N
ANISOU 2582 N GLY A 324 12661 9143 17101 538 -1813 1742 N
ATOM 2583 CA GLY A 324 -220.169 10.148 50.786 1.00 83.57 C
ANISOU 2583 CA GLY A 324 10334 6594 14827 534 -1701 1662 C
ATOM 2584 C GLY A 324 -221.158 9.449 51.695 1.00 98.63 C
ANISOU 2584 C GLY A 324 12429 8472 16574 388 -1813 1824 C
ATOM 2585 O GLY A 324 -222.041 8.744 51.195 1.00103.24 O
ANISOU 2585 O GLY A 324 13096 8999 17131 339 -1687 1726 O
ATOM 2586 N LYS A 325 -221.037 9.621 53.007 1.00116.29 N
ANISOU 2586 N LYS A 325 14744 10745 18697 302 -2044 2066 N
ATOM 2587 CA LYS A 325 -221.896 8.922 53.951 1.00120.13 C
ANISOU 2587 CA LYS A 325 15421 11191 19032 147 -2153 2240 C
ATOM 2588 C LYS A 325 -223.133 9.750 54.279 1.00124.25 C
ANISOU 2588 C LYS A 325 16100 11990 19121 -16 -2056 2191 C
ATOM 2589 O LYS A 325 -223.125 10.981 54.182 1.00121.05 O
ANISOU 2589 O LYS A 325 15665 11806 18524 -16 -1995 2103 O
ATOM 2590 CB LYS A 325 -221.129 8.594 55.234 1.00117.03 C
ANISOU 2590 CB LYS A 325 15044 10758 18665 108 -2423 2494 C
ATOM 2591 CG LYS A 325 -219.984 7.607 55.045 1.00121.21 C
ANISOU 2591 CG LYS A 325 15396 11111 19546 244 -2482 2500 C
ATOM 2592 CD LYS A 325 -220.497 6.202 54.757 1.00118.75 C
ANISOU 2592 CD LYS A 325 15136 10611 19374 236 -2412 2477 C
ATOM 2593 CE LYS A 325 -219.372 5.175 54.811 1.00125.47 C
ANISOU 2593 CE LYS A 325 15828 11279 20567 349 -2508 2526 C
ATOM 2594 NZ LYS A 325 -218.389 5.351 53.706 1.00123.77 N
ANISOU 2594 NZ LYS A 325 15375 11008 20644 531 -2365 2327 N
ATOM 2595 N ASN A 326 -224.200 9.053 54.668 1.00132.68 N
ANISOU 2595 N ASN A 326 17324 13029 20058 -155 -2036 2248 N
ATOM 2596 CA ASN A 326 -225.485 9.669 55.011 1.00136.74 C
ANISOU 2596 CA ASN A 326 17978 13775 20203 -320 -1928 2202 C
ATOM 2597 C ASN A 326 -226.016 10.537 53.870 1.00134.58 C
ANISOU 2597 C ASN A 326 17625 13683 19826 -270 -1699 1935 C
ATOM 2598 O ASN A 326 -227.195 10.463 53.516 1.00135.94 O
ANISOU 2598 O ASN A 326 17857 13934 19860 -356 -1554 1826 O
ATOM 2599 CB ASN A 326 -225.362 10.499 56.295 1.00139.29 C
ANISOU 2599 CB ASN A 326 18402 14254 20267 -435 -2070 2367 C
ATOM 2600 CG ASN A 326 -226.711 10.799 56.932 1.00143.66 C
ANISOU 2600 CG ASN A 326 19127 14981 20477 -635 -1972 2368 C
ATOM 2601 OD1 ASN A 326 -227.753 10.726 56.279 1.00143.09 O
ANISOU 2601 OD1 ASN A 326 19056 14969 20344 -668 -1781 2209 O
ATOM 2602 ND2 ASN A 326 -226.693 11.139 58.216 1.00144.83 N
ANISOU 2602 ND2 ASN A 326 19417 15208 20403 -780 -2102 2543 N
TER 2603 ASN A 326
HETATM 2604 C1 NAG B 1 -216.937 70.545 40.735 1.00 56.34 C
ANISOU 2604 C1 NAG B 1 7190 3816 10401 -589 -526 964 C
HETATM 2605 C2 NAG B 1 -216.251 69.835 39.558 1.00 57.71 C
ANISOU 2605 C2 NAG B 1 7396 4141 10390 -660 -515 1114 C
HETATM 2606 C3 NAG B 1 -214.733 70.025 39.620 1.00 66.76 C
ANISOU 2606 C3 NAG B 1 8526 5335 11506 -807 -438 1091 C
HETATM 2607 C4 NAG B 1 -214.340 71.476 39.858 1.00 65.98 C
ANISOU 2607 C4 NAG B 1 8457 5025 11588 -890 -436 1090 C
HETATM 2608 C5 NAG B 1 -215.126 72.039 41.038 1.00 69.45 C
ANISOU 2608 C5 NAG B 1 8875 5329 12185 -807 -462 933 C
HETATM 2609 C6 NAG B 1 -214.903 73.514 41.275 1.00 60.09 C
ANISOU 2609 C6 NAG B 1 7727 3902 11202 -876 -460 920 C
HETATM 2610 C7 NAG B 1 -216.948 67.738 38.476 1.00 62.00 C
ANISOU 2610 C7 NAG B 1 7947 4972 10639 -572 -540 1212 C
HETATM 2611 C8 NAG B 1 -217.179 66.265 38.663 1.00 51.89 C
ANISOU 2611 C8 NAG B 1 6618 3891 9205 -506 -523 1144 C
HETATM 2612 N2 NAG B 1 -216.560 68.414 39.564 1.00 53.98 N
ANISOU 2612 N2 NAG B 1 6885 3873 9752 -591 -510 1079 N
HETATM 2613 O3 NAG B 1 -214.137 69.551 38.417 1.00 58.72 O
ANISOU 2613 O3 NAG B 1 7546 4419 10345 -884 -398 1233 O
HETATM 2614 O4 NAG B 1 -212.963 71.463 40.208 1.00 71.86 O
ANISOU 2614 O4 NAG B 1 9151 5842 12312 -1017 -370 1024 O
HETATM 2615 O5 NAG B 1 -216.524 71.881 40.789 1.00 59.35 O
ANISOU 2615 O5 NAG B 1 7607 3997 10947 -666 -521 979 O
HETATM 2616 O6 NAG B 1 -215.103 74.244 40.074 1.00 71.25 O
ANISOU 2616 O6 NAG B 1 9217 5171 12683 -901 -504 1132 O
HETATM 2617 O7 NAG B 1 -217.112 68.292 37.392 1.00 71.65 O
ANISOU 2617 O7 NAG B 1 9256 6106 11861 -615 -584 1383 O
HETATM 2618 C1 NAG B 2 -212.171 72.415 39.491 1.00 61.39 C
ANISOU 2618 C1 NAG B 2 7872 4401 11051 -1154 -337 1139 C
HETATM 2619 C2 NAG B 2 -210.943 72.654 40.364 1.00 60.05 C
ANISOU 2619 C2 NAG B 2 7622 4254 10942 -1269 -293 1007 C
HETATM 2620 C3 NAG B 2 -209.994 73.627 39.679 1.00 61.92 C
ANISOU 2620 C3 NAG B 2 7891 4378 11258 -1431 -244 1115 C
HETATM 2621 C4 NAG B 2 -209.677 73.157 38.268 1.00 62.10 C
ANISOU 2621 C4 NAG B 2 7956 4493 11145 -1486 -178 1292 C
HETATM 2622 C5 NAG B 2 -210.962 72.927 37.493 1.00 61.73 C
ANISOU 2622 C5 NAG B 2 8014 4425 11017 -1373 -242 1418 C
HETATM 2623 C6 NAG B 2 -210.710 72.400 36.100 1.00 62.04 C
ANISOU 2623 C6 NAG B 2 8126 4566 10882 -1443 -180 1583 C
HETATM 2624 C7 NAG B 2 -211.404 72.406 42.774 1.00 76.33 C
ANISOU 2624 C7 NAG B 2 9610 6339 13053 -1183 -352 670 C
HETATM 2625 C8 NAG B 2 -211.825 73.119 44.025 1.00 59.64 C
ANISOU 2625 C8 NAG B 2 7520 4093 11047 -1175 -374 494 C
HETATM 2626 N2 NAG B 2 -211.329 73.161 41.672 1.00 63.35 N
ANISOU 2626 N2 NAG B 2 8027 4573 11472 -1231 -335 834 N
HETATM 2627 O3 NAG B 2 -208.797 73.728 40.440 1.00 66.69 O
ANISOU 2627 O3 NAG B 2 8397 5023 11919 -1545 -211 997 O
HETATM 2628 O4 NAG B 2 -208.939 74.148 37.573 1.00 66.69 O
ANISOU 2628 O4 NAG B 2 8592 4950 11798 -1644 -125 1409 O
HETATM 2629 O5 NAG B 2 -211.760 71.960 38.187 1.00 59.86 O
ANISOU 2629 O5 NAG B 2 7721 4303 10720 -1219 -289 1302 O
HETATM 2630 O6 NAG B 2 -211.902 72.007 35.439 1.00 63.38 O
ANISOU 2630 O6 NAG B 2 8386 4745 10951 -1342 -262 1689 O
HETATM 2631 O7 NAG B 2 -211.138 71.202 42.766 1.00 70.17 O
ANISOU 2631 O7 NAG B 2 8767 5760 12134 -1155 -345 662 O
HETATM 2632 C1 BMA B 3 -207.610 73.713 37.277 1.00 85.94 C
ANISOU 2632 C1 BMA B 3 10943 7520 14190 -1775 -6 1402 C
HETATM 2633 C2 BMA B 3 -207.162 74.739 36.281 1.00 87.38 C
ANISOU 2633 C2 BMA B 3 11227 7560 14412 -1933 53 1567 C
HETATM 2634 C3 BMA B 3 -205.700 74.517 35.919 1.00 98.66 C
ANISOU 2634 C3 BMA B 3 12560 9090 15836 -2099 205 1564 C
HETATM 2635 C4 BMA B 3 -204.816 74.371 37.175 1.00120.08 C
ANISOU 2635 C4 BMA B 3 15086 11857 18683 -2121 195 1374 C
HETATM 2636 C5 BMA B 3 -205.423 73.354 38.155 1.00128.43 C
ANISOU 2636 C5 BMA B 3 16069 13045 19684 -1948 103 1229 C
HETATM 2637 C6 BMA B 3 -204.697 73.332 39.478 1.00134.51 C
ANISOU 2637 C6 BMA B 3 16691 13844 20572 -1978 48 1057 C
HETATM 2638 O2 BMA B 3 -207.287 76.041 36.863 1.00 80.08 O
ANISOU 2638 O2 BMA B 3 10337 6408 13680 -1965 -16 1546 O
HETATM 2639 O3 BMA B 3 -205.221 75.572 35.098 1.00100.54 O
ANISOU 2639 O3 BMA B 3 12895 9183 16125 -2269 270 1709 O
HETATM 2640 O4 BMA B 3 -203.529 73.926 36.802 1.00137.51 O
ANISOU 2640 O4 BMA B 3 17167 14183 20900 -2248 335 1368 O
HETATM 2641 O5 BMA B 3 -206.787 73.733 38.417 1.00115.41 O
ANISOU 2641 O5 BMA B 3 14538 11282 18030 -1817 -9 1236 O
HETATM 2642 O6 BMA B 3 -205.077 74.513 40.168 1.00140.96 O
ANISOU 2642 O6 BMA B 3 17580 14466 21511 -1997 -36 1007 O
HETATM 2643 C1 MAN B 4 -205.355 75.218 33.704 1.00 90.71 C
ANISOU 2643 C1 MAN B 4 11777 7999 14690 -2327 358 1879 C
HETATM 2644 C2 MAN B 4 -204.417 76.136 32.935 1.00 97.01 C
ANISOU 2644 C2 MAN B 4 12634 8692 15534 -2553 481 2001 C
HETATM 2645 C3 MAN B 4 -204.926 77.585 33.035 1.00 98.07 C
ANISOU 2645 C3 MAN B 4 12893 8555 15814 -2582 359 2101 C
HETATM 2646 C4 MAN B 4 -206.401 77.707 32.570 1.00 96.37 C
ANISOU 2646 C4 MAN B 4 12851 8249 15517 -2451 204 2239 C
HETATM 2647 C5 MAN B 4 -207.276 76.706 33.321 1.00 99.47 C
ANISOU 2647 C5 MAN B 4 13160 8769 15865 -2228 109 2098 C
HETATM 2648 C6 MAN B 4 -208.700 76.633 32.752 1.00 98.43 C
ANISOU 2648 C6 MAN B 4 13172 8581 15647 -2103 -34 2237 C
HETATM 2649 O2 MAN B 4 -204.451 75.791 31.559 1.00105.37 O
ANISOU 2649 O2 MAN B 4 13837 9819 16380 -2644 587 2161 O
HETATM 2650 O3 MAN B 4 -204.096 78.497 32.311 1.00109.38 O
ANISOU 2650 O3 MAN B 4 14397 9873 17291 -2803 466 2231 O
HETATM 2651 O4 MAN B 4 -206.896 79.017 32.821 1.00109.48 O
ANISOU 2651 O4 MAN B 4 14592 9638 17367 -2448 82 2307 O
HETATM 2652 O5 MAN B 4 -206.685 75.379 33.220 1.00 98.18 O
ANISOU 2652 O5 MAN B 4 12891 8863 15550 -2225 231 2006 O
HETATM 2653 O6 MAN B 4 -209.552 75.889 33.644 1.00 90.90 O
ANISOU 2653 O6 MAN B 4 12125 7707 14707 -1897 -124 2087 O
HETATM 2654 C1 MAN B 5 -204.606 74.449 41.526 1.00146.38 C
ANISOU 2654 C1 MAN B 5 18163 15183 22269 -2020 -114 830 C
HETATM 2655 C2 MAN B 5 -205.623 75.241 42.411 1.00143.35 C
ANISOU 2655 C2 MAN B 5 17891 14635 21941 -1952 -207 732 C
HETATM 2656 C3 MAN B 5 -205.437 76.774 42.288 1.00144.71 C
ANISOU 2656 C3 MAN B 5 18142 14560 22282 -2072 -198 763 C
HETATM 2657 C4 MAN B 5 -203.944 77.203 42.231 1.00149.10 C
ANISOU 2657 C4 MAN B 5 18597 15111 22943 -2275 -155 769 C
HETATM 2658 C5 MAN B 5 -203.191 76.348 41.202 1.00145.14 C
ANISOU 2658 C5 MAN B 5 18002 14781 22364 -2313 -50 890 C
HETATM 2659 C6 MAN B 5 -201.719 76.695 41.070 1.00127.30 C
ANISOU 2659 C6 MAN B 5 15613 12524 20230 -2510 14 899 C
HETATM 2660 O2 MAN B 5 -205.479 74.930 43.799 1.00149.11 O
ANISOU 2660 O2 MAN B 5 18561 15428 22667 -1949 -292 547 O
HETATM 2661 O3 MAN B 5 -206.101 77.461 43.344 1.00141.71 O
ANISOU 2661 O3 MAN B 5 17829 14031 21982 -2036 -268 617 O
HETATM 2662 O4 MAN B 5 -203.835 78.584 41.877 1.00147.68 O
ANISOU 2662 O4 MAN B 5 18508 14695 22909 -2386 -132 834 O
HETATM 2663 O5 MAN B 5 -203.293 74.967 41.600 1.00150.27 O
ANISOU 2663 O5 MAN B 5 18557 15648 22892 -2198 -79 819 O
HETATM 2664 O6 MAN B 5 -201.213 75.997 39.934 1.00116.25 O
ANISOU 2664 O6 MAN B 5 14157 11253 18761 -2538 153 1018 O
HETATM 2665 C1 PLM A 401 -222.705 15.674 56.692 1.00115.68 C
ANISOU 2665 C1 PLM A 401 15126 11902 16925 -264 -2188 2215 C
HETATM 2666 O2 PLM A 401 -223.775 15.776 56.087 1.00110.67 O
ANISOU 2666 O2 PLM A 401 14521 11352 16176 -288 -1982 2060 O
HETATM 2667 C2 PLM A 401 -221.952 16.807 57.331 1.00111.35 C
ANISOU 2667 C2 PLM A 401 14564 11477 16267 -286 -2309 2267 C
HETATM 2668 C3 PLM A 401 -220.440 16.657 57.262 1.00105.81 C
ANISOU 2668 C3 PLM A 401 13697 10636 15869 -157 -2496 2361 C
HETATM 2669 C4 PLM A 401 -219.702 17.503 58.287 1.00 92.62 C
ANISOU 2669 C4 PLM A 401 12062 9054 14077 -234 -2702 2491 C
HETATM 2670 C5 PLM A 401 -219.954 18.992 58.121 1.00 84.64 C
ANISOU 2670 C5 PLM A 401 11052 8273 12836 -260 -2562 2330 C
HETATM 2671 C6 PLM A 401 -219.883 19.701 59.459 1.00 86.04 C
ANISOU 2671 C6 PLM A 401 11390 8569 12732 -434 -2725 2454 C
HETATM 2672 C7 PLM A 401 -219.313 21.100 59.358 1.00 81.93 C
ANISOU 2672 C7 PLM A 401 10790 8189 12150 -410 -2709 2357 C
HETATM 2673 C8 PLM A 401 -220.362 22.104 58.938 1.00 79.87 C
ANISOU 2673 C8 PLM A 401 10579 8113 11654 -441 -2443 2147 C
HETATM 2674 C9 PLM A 401 -219.912 23.526 59.218 1.00 78.14 C
ANISOU 2674 C9 PLM A 401 10347 8035 11306 -475 -2459 2087 C
HETATM 2675 CA PLM A 401 -220.540 24.493 58.237 1.00 82.60 C
ANISOU 2675 CA PLM A 401 10844 8722 11820 -405 -2196 1859 C
HETATM 2676 CB PLM A 401 -220.725 25.871 58.840 1.00 89.04 C
ANISOU 2676 CB PLM A 401 11746 9697 12388 -511 -2162 1791 C
HETATM 2677 CC PLM A 401 -219.403 26.573 59.070 1.00 89.64 C
ANISOU 2677 CC PLM A 401 11733 9773 12554 -488 -2332 1841 C
HETATM 2678 CD PLM A 401 -219.639 27.983 59.573 1.00 88.52 C
ANISOU 2678 CD PLM A 401 11679 9781 12174 -591 -2273 1746 C
HETATM 2679 CE PLM A 401 -218.523 28.946 59.217 1.00 77.83 C
ANISOU 2679 CE PLM A 401 10176 8444 10950 -520 -2333 1707 C
HETATM 2680 CF PLM A 401 -219.025 30.370 59.362 1.00 82.58 C
ANISOU 2680 CF PLM A 401 10847 9184 11346 -588 -2192 1560 C
HETATM 2681 CG PLM A 401 -218.027 31.408 58.922 1.00 68.10 C
ANISOU 2681 CG PLM A 401 8870 7369 9636 -523 -2221 1504 C
HETATM 2682 C1 BOG A 407 -229.934 45.020 38.637 1.00 80.37 C
ANISOU 2682 C1 BOG A 407 9903 9076 11558 234 -857 642 C
HETATM 2683 O1 BOG A 407 -230.634 44.150 39.525 1.00 85.87 O
ANISOU 2683 O1 BOG A 407 10536 9796 12294 256 -828 576 O
HETATM 2684 C2 BOG A 407 -230.206 46.471 39.011 1.00 82.42 C
ANISOU 2684 C2 BOG A 407 10103 9256 11956 272 -881 668 C
HETATM 2685 O2 BOG A 407 -231.609 46.720 38.908 1.00 80.40 O
ANISOU 2685 O2 BOG A 407 9767 8955 11826 301 -970 698 O
HETATM 2686 C3 BOG A 407 -229.405 47.424 38.134 1.00 80.29 C
ANISOU 2686 C3 BOG A 407 9908 8953 11645 240 -906 746 C
HETATM 2687 O3 BOG A 407 -229.546 48.758 38.635 1.00 92.12 O
ANISOU 2687 O3 BOG A 407 11350 10361 13289 278 -914 758 O
HETATM 2688 C4 BOG A 407 -227.934 47.024 38.158 1.00 74.26 C
ANISOU 2688 C4 BOG A 407 9207 8239 10768 205 -803 709 C
HETATM 2689 O4 BOG A 407 -227.203 47.772 37.183 1.00 68.21 O
ANISOU 2689 O4 BOG A 407 8520 7451 9945 154 -811 783 O
HETATM 2690 C5 BOG A 407 -227.766 45.549 37.814 1.00 75.03 C
ANISOU 2690 C5 BOG A 407 9348 8411 10748 177 -770 672 C
HETATM 2691 O5 BOG A 407 -228.536 44.740 38.699 1.00 71.69 O
ANISOU 2691 O5 BOG A 407 8859 8009 10372 213 -767 612 O
HETATM 2692 C6 BOG A 407 -226.300 45.135 37.895 1.00 62.52 C
ANISOU 2692 C6 BOG A 407 7793 6859 9102 155 -661 630 C
HETATM 2693 O6 BOG A 407 -225.927 45.063 39.275 1.00 68.70 O
ANISOU 2693 O6 BOG A 407 8503 7641 9958 197 -614 568 O
HETATM 2694 C1' BOG A 407 -230.796 42.863 38.930 1.00 83.26 C
ANISOU 2694 C1' BOG A 407 10254 9516 11867 218 -844 569 C
HETATM 2695 C2' BOG A 407 -231.866 42.063 39.659 1.00 73.85 C
ANISOU 2695 C2' BOG A 407 8988 8334 10735 230 -843 523 C
HETATM 2696 C3' BOG A 407 -231.990 40.673 39.038 1.00 80.74 C
ANISOU 2696 C3' BOG A 407 9919 9249 11510 184 -859 510 C
HETATM 2697 C4' BOG A 407 -232.954 39.786 39.824 1.00 77.67 C
ANISOU 2697 C4' BOG A 407 9463 8869 11179 184 -844 465 C
HETATM 2698 C5' BOG A 407 -232.909 38.344 39.324 1.00 88.67 C
ANISOU 2698 C5' BOG A 407 10921 10289 12478 136 -844 441 C
HETATM 2699 C6' BOG A 407 -233.826 37.442 40.149 1.00 90.16 C
ANISOU 2699 C6' BOG A 407 11048 10481 12726 126 -823 402 C
HETATM 2700 C7' BOG A 407 -235.282 37.890 40.063 1.00 83.46 C
ANISOU 2700 C7' BOG A 407 10094 9618 12000 123 -900 423 C
HETATM 2701 C8' BOG A 407 -236.069 37.369 41.244 1.00 69.68 C
ANISOU 2701 C8' BOG A 407 8265 7871 10340 119 -828 373 C
HETATM 2702 C1 BOG A 408 -225.726 51.278 45.842 1.00 93.22 C
ANISOU 2702 C1 BOG A 408 11436 10426 13556 220 -471 259 C
HETATM 2703 O1 BOG A 408 -226.571 52.409 46.057 1.00 86.63 O
ANISOU 2703 O1 BOG A 408 10571 9484 12859 247 -442 217 O
HETATM 2704 C2 BOG A 408 -226.382 50.340 44.824 1.00106.49 C
ANISOU 2704 C2 BOG A 408 13101 12152 15208 259 -512 330 C
HETATM 2705 O2 BOG A 408 -227.595 49.815 45.384 1.00 79.10 O
ANISOU 2705 O2 BOG A 408 9598 8693 11765 283 -485 277 O
HETATM 2706 C3 BOG A 408 -225.454 49.203 44.386 1.00107.43 C
ANISOU 2706 C3 BOG A 408 13250 12360 15210 236 -529 371 C
HETATM 2707 O3 BOG A 408 -226.081 48.482 43.313 1.00103.70 O
ANISOU 2707 O3 BOG A 408 12779 11914 14707 259 -565 429 O
HETATM 2708 C4 BOG A 408 -224.115 49.799 43.943 1.00 98.45 C
ANISOU 2708 C4 BOG A 408 12132 11210 14067 202 -530 409 C
HETATM 2709 O4 BOG A 408 -223.172 48.789 43.520 1.00101.80 O
ANISOU 2709 O4 BOG A 408 12562 11700 14417 184 -525 435 O
HETATM 2710 C5 BOG A 408 -223.534 50.669 45.065 1.00 86.33 C
ANISOU 2710 C5 BOG A 408 10595 9636 12570 166 -510 345 C
HETATM 2711 O5 BOG A 408 -224.434 51.720 45.420 1.00 85.48 O
ANISOU 2711 O5 BOG A 408 10479 9442 12557 184 -492 304 O
HETATM 2712 C6 BOG A 408 -222.200 51.310 44.687 1.00 66.77 C
ANISOU 2712 C6 BOG A 408 8122 7140 10110 123 -512 380 C
HETATM 2713 O6 BOG A 408 -222.226 51.741 43.318 1.00 59.31 O
ANISOU 2713 O6 BOG A 408 7191 6162 9182 130 -518 464 O
HETATM 2714 C1' BOG A 408 -226.653 52.745 47.440 1.00 87.63 C
ANISOU 2714 C1' BOG A 408 10715 9591 12990 209 -366 93 C
HETATM 2715 C2' BOG A 408 -228.054 52.379 47.929 1.00101.21 C
ANISOU 2715 C2' BOG A 408 12390 11302 14764 241 -303 26 C
HETATM 2716 C3' BOG A 408 -228.018 51.941 49.387 1.00101.27 C
ANISOU 2716 C3' BOG A 408 12451 11360 14666 169 -221 -91 C
HETATM 2717 C4' BOG A 408 -229.388 51.532 49.914 1.00 96.82 C
ANISOU 2717 C4' BOG A 408 11843 10792 14151 184 -130 -167 C
HETATM 2718 C5' BOG A 408 -229.245 51.073 51.361 1.00 93.04 C
ANISOU 2718 C5' BOG A 408 11454 10372 13526 85 -45 -272 C
HETATM 2719 C6' BOG A 408 -230.569 50.638 51.967 1.00 88.66 C
ANISOU 2719 C6' BOG A 408 10863 9817 13006 78 76 -359 C
HETATM 2720 C7' BOG A 408 -230.335 50.224 53.412 1.00 95.63 C
ANISOU 2720 C7' BOG A 408 11868 10760 13705 -48 159 -455 C
HETATM 2721 C8' BOG A 408 -231.650 49.998 54.123 1.00103.77 C
ANISOU 2721 C8' BOG A 408 12872 11778 14779 -75 324 -567 C
HETATM 2722 C1 BOG A 409 -206.510 52.746 49.543 1.00104.29 C
ANISOU 2722 C1 BOG A 409 11903 11888 15834 -646 -1183 473 C
HETATM 2723 O1 BOG A 409 -206.551 51.447 48.958 1.00100.77 O
ANISOU 2723 O1 BOG A 409 11380 11469 15437 -537 -1128 513 O
HETATM 2724 C2 BOG A 409 -205.053 53.205 49.545 1.00105.12 C
ANISOU 2724 C2 BOG A 409 11826 11960 16157 -731 -1239 496 C
HETATM 2725 O2 BOG A 409 -204.320 52.399 50.483 1.00 97.36 O
ANISOU 2725 O2 BOG A 409 10732 10995 15264 -756 -1448 544 O
HETATM 2726 C3 BOG A 409 -204.916 54.684 49.889 1.00106.26 C
ANISOU 2726 C3 BOG A 409 12038 12058 16276 -852 -1260 449 C
HETATM 2727 O3 BOG A 409 -203.565 55.109 49.668 1.00116.45 O
ANISOU 2727 O3 BOG A 409 13142 13314 17791 -930 -1280 472 O
HETATM 2728 C4 BOG A 409 -205.851 55.513 49.023 1.00101.59 C
ANISOU 2728 C4 BOG A 409 11585 11432 15583 -820 -1073 413 C
HETATM 2729 O4 BOG A 409 -205.771 56.887 49.418 1.00 99.55 O
ANISOU 2729 O4 BOG A 409 11399 11112 15314 -930 -1097 364 O
HETATM 2730 C5 BOG A 409 -207.278 54.999 49.179 1.00104.59 C
ANISOU 2730 C5 BOG A 409 12129 11846 15764 -731 -1046 390 C
HETATM 2731 O5 BOG A 409 -207.355 53.625 48.798 1.00 98.76 O
ANISOU 2731 O5 BOG A 409 11326 11161 15039 -630 -1026 434 O
HETATM 2732 C6 BOG A 409 -208.277 55.798 48.342 1.00102.38 C
ANISOU 2732 C6 BOG A 409 11974 11521 15403 -693 -891 368 C
HETATM 2733 O6 BOG A 409 -209.604 55.579 48.841 1.00 81.43 O
ANISOU 2733 O6 BOG A 409 9469 8886 12584 -640 -901 328 O
HETATM 2734 C1' BOG A 409 -207.679 50.670 49.336 1.00 72.25 C
ANISOU 2734 C1' BOG A 409 7900 7897 11655 -472 -1152 508 C
HETATM 2735 C2' BOG A 409 -207.411 49.240 48.876 1.00 79.93 C
ANISOU 2735 C2' BOG A 409 8760 8882 12729 -376 -1130 554 C
HETATM 2736 C3' BOG A 409 -208.561 48.313 49.253 1.00 73.89 C
ANISOU 2736 C3' BOG A 409 8124 8153 11798 -313 -1157 557 C
HETATM 2737 C4' BOG A 409 -208.327 46.904 48.724 1.00 75.48 C
ANISOU 2737 C4' BOG A 409 8220 8348 12110 -216 -1121 594 C
HETATM 2738 C5' BOG A 409 -209.377 45.969 49.305 1.00 84.44 C
ANISOU 2738 C5' BOG A 409 9479 9513 13090 -174 -1182 608 C
HETATM 2739 C6' BOG A 409 -209.076 44.503 49.025 1.00 84.23 C
ANISOU 2739 C6' BOG A 409 9350 9464 13191 -89 -1187 651 C
HETATM 2740 C7' BOG A 409 -210.230 43.652 49.549 1.00 82.09 C
ANISOU 2740 C7' BOG A 409 9221 9219 12750 -59 -1232 663 C
HETATM 2741 C8' BOG A 409 -210.011 42.173 49.305 1.00 87.21 C
ANISOU 2741 C8' BOG A 409 9783 9829 13525 25 -1240 706 C
HETATM 2742 C1 BOG A 410 -255.273 27.589 47.852 1.00112.15 C
ANISOU 2742 C1 BOG A 410 11451 13042 18118 -1123 208 -194 C
HETATM 2743 O1 BOG A 410 -254.164 28.420 47.521 1.00111.77 O
ANISOU 2743 O1 BOG A 410 11554 13013 17900 -985 107 -159 O
HETATM 2744 C2 BOG A 410 -255.077 27.028 49.260 1.00110.84 C
ANISOU 2744 C2 BOG A 410 11431 12893 17792 -1233 511 -246 C
HETATM 2745 O2 BOG A 410 -254.011 26.077 49.243 1.00112.38 O
ANISOU 2745 O2 BOG A 410 11932 13108 17658 -1272 443 -180 O
HETATM 2746 C3 BOG A 410 -256.321 26.321 49.778 1.00125.04 C
ANISOU 2746 C3 BOG A 410 13049 14667 19794 -1387 678 -297 C
HETATM 2747 O3 BOG A 410 -256.150 26.034 51.172 1.00129.01 O
ANISOU 2747 O3 BOG A 410 13691 15185 20140 -1494 986 -349 O
HETATM 2748 C4 BOG A 410 -257.557 27.183 49.564 1.00134.20 C
ANISOU 2748 C4 BOG A 410 13832 15787 21371 -1345 704 -359 C
HETATM 2749 O4 BOG A 410 -258.724 26.431 49.919 1.00141.69 O
ANISOU 2749 O4 BOG A 410 14594 16711 22529 -1497 840 -402 O
HETATM 2750 C5 BOG A 410 -257.647 27.610 48.102 1.00129.46 C
ANISOU 2750 C5 BOG A 410 13112 15170 20908 -1233 348 -283 C
HETATM 2751 O5 BOG A 410 -256.481 28.350 47.742 1.00122.41 O
ANISOU 2751 O5 BOG A 410 12407 14299 19803 -1094 228 -239 O
HETATM 2752 C6 BOG A 410 -258.892 28.450 47.837 1.00131.63 C
ANISOU 2752 C6 BOG A 410 12992 15388 21634 -1184 330 -321 C
HETATM 2753 O6 BOG A 410 -260.061 27.644 48.038 1.00132.79 O
ANISOU 2753 O6 BOG A 410 12931 15511 22011 -1329 415 -356 O
HETATM 2754 C1' BOG A 410 -254.239 28.902 46.179 1.00100.45 C
ANISOU 2754 C1' BOG A 410 10034 11567 16565 -899 -186 -93 C
HETATM 2755 C2' BOG A 410 -252.927 29.606 45.847 1.00 87.58 C
ANISOU 2755 C2' BOG A 410 8608 9961 14707 -778 -275 -51 C
HETATM 2756 C3' BOG A 410 -252.736 29.743 44.343 1.00 74.99 C
ANISOU 2756 C3' BOG A 410 7033 8366 13092 -730 -597 36 C
HETATM 2757 C4' BOG A 410 -251.433 30.469 44.039 1.00 80.42 C
ANISOU 2757 C4' BOG A 410 7917 9076 13563 -620 -659 73 C
HETATM 2758 C5' BOG A 410 -251.351 30.762 42.549 1.00 82.39 C
ANISOU 2758 C5' BOG A 410 8176 9324 13805 -585 -962 159 C
HETATM 2759 C6' BOG A 410 -250.086 31.541 42.213 1.00 80.90 C
ANISOU 2759 C6' BOG A 410 8169 9153 13416 -484 -1011 196 C
HETATM 2760 C7' BOG A 410 -250.273 32.235 40.870 1.00 83.12 C
ANISOU 2760 C7' BOG A 410 8400 9420 13763 -446 -1289 285 C
HETATM 2761 C8' BOG A 410 -248.950 32.543 40.219 1.00 75.97 C
ANISOU 2761 C8' BOG A 410 7734 8542 12588 -398 -1369 331 C
HETATM 2762 C1 BOG A 411 -223.607 57.382 63.753 1.00121.60 C
ANISOU 2762 C1 BOG A 411 16645 13872 15687 -1574 298 -1574 C
HETATM 2763 O1 BOG A 411 -224.064 56.036 63.890 1.00112.71 O
ANISOU 2763 O1 BOG A 411 15531 12866 14429 -1566 280 -1473 O
HETATM 2764 C2 BOG A 411 -222.269 57.500 64.487 1.00123.53 C
ANISOU 2764 C2 BOG A 411 17038 14173 15724 -1767 84 -1544 C
HETATM 2765 O2 BOG A 411 -222.465 57.321 65.898 1.00122.53 O
ANISOU 2765 O2 BOG A 411 17163 14102 15290 -2003 149 -1675 O
HETATM 2766 C3 BOG A 411 -221.597 58.840 64.210 1.00123.31 C
ANISOU 2766 C3 BOG A 411 16977 14024 15850 -1772 60 -1614 C
HETATM 2767 O3 BOG A 411 -220.313 58.897 64.846 1.00129.79 O
ANISOU 2767 O3 BOG A 411 17914 14903 16496 -1953 -165 -1571 O
HETATM 2768 C4 BOG A 411 -221.446 59.003 62.705 1.00111.49 C
ANISOU 2768 C4 BOG A 411 15234 12471 14654 -1538 5 -1467 C
HETATM 2769 O4 BOG A 411 -220.785 60.240 62.410 1.00112.79 O
ANISOU 2769 O4 BOG A 411 15369 12519 14968 -1549 -23 -1515 O
HETATM 2770 C5 BOG A 411 -222.826 58.944 62.053 1.00111.23 C
ANISOU 2770 C5 BOG A 411 15080 12375 14807 -1359 212 -1503 C
HETATM 2771 O5 BOG A 411 -223.490 57.710 62.360 1.00119.27 O
ANISOU 2771 O5 BOG A 411 16127 13508 15683 -1360 245 -1458 O
HETATM 2772 C6 BOG A 411 -222.745 59.093 60.536 1.00107.52 C
ANISOU 2772 C6 BOG A 411 14391 11852 14609 -1144 149 -1349 C
HETATM 2773 O6 BOG A 411 -221.672 59.973 60.187 1.00115.88 O
ANISOU 2773 O6 BOG A 411 15426 12847 15757 -1168 34 -1317 O
HETATM 2774 C1' BOG A 411 -225.226 55.729 63.120 1.00111.74 C
ANISOU 2774 C1' BOG A 411 15248 12710 14499 -1385 431 -1463 C
HETATM 2775 C2' BOG A 411 -225.304 54.212 62.979 1.00107.54 C
ANISOU 2775 C2' BOG A 411 14698 12310 13854 -1357 322 -1291 C
HETATM 2776 C3' BOG A 411 -226.684 53.720 62.558 1.00 99.60 C
ANISOU 2776 C3' BOG A 411 13580 11289 12973 -1236 503 -1313 C
HETATM 2777 C4' BOG A 411 -226.704 52.194 62.535 1.00 87.49 C
ANISOU 2777 C4' BOG A 411 12056 9882 11306 -1237 392 -1151 C
HETATM 2778 C5' BOG A 411 -228.118 51.664 62.752 1.00102.90 C
ANISOU 2778 C5' BOG A 411 13989 11838 13270 -1226 608 -1228 C
HETATM 2779 C6' BOG A 411 -228.124 50.178 63.108 1.00108.68 C
ANISOU 2779 C6' BOG A 411 14798 12691 13805 -1294 519 -1097 C
HETATM 2780 C7' BOG A 411 -229.462 49.753 63.711 1.00103.99 C
ANISOU 2780 C7' BOG A 411 14247 12106 13158 -1359 764 -1211 C
HETATM 2781 C8' BOG A 411 -229.413 48.324 64.208 1.00 97.93 C
ANISOU 2781 C8' BOG A 411 13592 11449 12167 -1461 674 -1081 C
HETATM 2782 C10 DL2 A 412 -234.989 48.626 36.057 1.00 71.10 C
ANISOU 2782 C10 DL2 A 412 8459 7558 11000 305 -1531 1064 C
HETATM 2783 C11 DL2 A 412 -234.274 47.399 35.519 1.00 87.59 C
ANISOU 2783 C11 DL2 A 412 10692 9767 12820 221 -1488 1036 C
HETATM 2784 C13 DL2 A 412 -233.980 45.012 35.975 1.00 91.55 C
ANISOU 2784 C13 DL2 A 412 11246 10426 13111 175 -1338 876 C
HETATM 2785 C15 DL2 A 412 -235.485 43.087 36.590 1.00 70.16 C
ANISOU 2785 C15 DL2 A 412 8422 7779 10458 166 -1341 776 C
HETATM 2786 C17 DL2 A 412 -237.475 41.819 37.228 1.00 76.19 C
ANISOU 2786 C17 DL2 A 412 8996 8551 11401 163 -1384 715 C
HETATM 2787 C19 DL2 A 412 -235.014 43.065 37.879 1.00 63.27 C
ANISOU 2787 C19 DL2 A 412 7502 6908 9629 218 -1181 685 C
HETATM 2788 C21 DL2 A 412 -236.210 46.136 36.436 1.00 74.12 C
ANISOU 2788 C21 DL2 A 412 8766 8081 11315 270 -1508 939 C
HETATM 2789 C22 DL2 A 412 -236.970 47.061 35.489 1.00 72.83 C
ANISOU 2789 C22 DL2 A 412 8567 7832 11274 267 -1720 1085 C
HETATM 2790 C23 DL2 A 412 -236.943 41.814 38.550 1.00 74.55 C
ANISOU 2790 C23 DL2 A 412 8759 8348 11218 212 -1203 623 C
HETATM 2791 C25 DL2 A 412 -235.770 42.403 38.891 1.00 64.97 C
ANISOU 2791 C25 DL2 A 412 7615 7133 9938 238 -1113 608 C
HETATM 2792 C1 DL2 A 412 -238.263 51.291 34.421 1.00 93.82 C
ANISOU 2792 C1 DL2 A 412 11014 10059 14576 403 -2150 1462 C
HETATM 2793 C2 DL2 A 412 -237.668 50.274 35.115 1.00 86.67 C
ANISOU 2793 C2 DL2 A 412 10157 9278 13494 387 -1948 1308 C
HETATM 2794 C3 DL2 A 412 -237.868 50.097 36.495 1.00 88.14 C
ANISOU 2794 C3 DL2 A 412 10211 9461 13816 462 -1753 1144 C
HETATM 2795 C4 DL2 A 412 -238.667 50.925 37.239 1.00 97.43 C
ANISOU 2795 C4 DL2 A 412 11199 10511 15310 556 -1723 1106 C
HETATM 2796 C5 DL2 A 412 -239.274 51.969 36.531 1.00 94.82 C
ANISOU 2796 C5 DL2 A 412 10795 10040 15192 590 -1916 1251 C
HETATM 2797 C6 DL2 A 412 -239.083 52.143 35.176 1.00 97.33 C
ANISOU 2797 C6 DL2 A 412 11245 10360 15377 517 -2137 1434 C
HETATM 2798 O7 DL2 A 412 -237.162 49.014 36.916 1.00 80.77 O
ANISOU 2798 O7 DL2 A 412 9371 8657 12661 419 -1606 1037 O
HETATM 2799 C8 DL2 A 412 -236.490 48.502 35.768 1.00 80.85 C
ANISOU 2799 C8 DL2 A 412 9564 8748 12408 324 -1690 1119 C
HETATM 2800 O9 DL2 A 412 -236.822 49.304 34.645 1.00 75.75 O
ANISOU 2800 O9 DL2 A 412 8953 8029 11802 295 -1899 1285 O
HETATM 2801 N12 DL2 A 412 -234.744 46.169 36.177 1.00 86.96 N
ANISOU 2801 N12 DL2 A 412 10552 9753 12737 231 -1419 932 N
HETATM 2802 C14 DL2 A 412 -234.729 43.776 35.489 1.00 82.36 C
ANISOU 2802 C14 DL2 A 412 10097 9316 11882 121 -1407 865 C
HETATM 2803 N16 DL2 A 412 -236.686 42.497 36.256 1.00 78.97 N
ANISOU 2803 N16 DL2 A 412 9471 8897 11636 137 -1452 795 N
HETATM 2804 O18 DL2 A 412 -238.529 41.300 36.890 1.00 69.55 O
ANISOU 2804 O18 DL2 A 412 8088 7711 10626 130 -1486 733 O
HETATM 2805 O20 DL2 A 412 -232.757 45.018 36.169 1.00 90.52 O
ANISOU 2805 O20 DL2 A 412 11192 10322 12878 167 -1220 837 O
HETATM 2806 CL DL2 A 412 -237.906 41.009 39.667 1.00 80.77 CL
ANISOU 2806 CL DL2 A 412 9424 9144 12120 216 -1113 536 CL
HETATM 2807 O HOH A 501 -239.542 30.320 37.670 1.00 69.94 O
HETATM 2808 O HOH A 502 -222.019 57.722 38.171 1.00 54.36 O
HETATM 2809 O HOH A 503 -259.358 7.551 43.601 1.00 69.99 O
HETATM 2810 O HOH A 504 -213.804 60.992 35.079 1.00 58.02 O
HETATM 2811 O HOH A 505 -227.436 47.345 34.965 1.00 55.98 O
HETATM 2812 O HOH A 506 -222.509 62.487 30.652 1.00 60.18 O
HETATM 2813 O HOH A 507 -230.607 46.902 34.903 1.00 68.47 O
HETATM 2814 O HOH A 508 -217.614 66.705 35.683 1.00 65.03 O
HETATM 2815 O HOH A 509 -222.828 10.252 44.095 1.00 70.27 O
HETATM 2816 O HOH A 510 -211.071 69.036 41.554 1.00 77.04 O
HETATM 2817 O HOH A 511 -239.425 33.105 42.522 1.00 70.64 O
HETATM 2818 O HOH A 512 -221.913 51.955 28.257 1.00 72.60 O
HETATM 2819 O HOH A 513 -213.472 62.661 48.364 1.00 66.40 O
HETATM 2820 O HOH A 514 -231.099 44.265 34.327 1.00 76.11 O
HETATM 2821 O HOH A 515 -225.457 57.813 39.112 1.00 64.25 O
HETATM 2822 O HOH A 516 -216.949 57.138 58.016 1.00 69.75 O
HETATM 2823 O HOH A 517 -231.147 35.153 41.271 1.00 71.29 O
HETATM 2824 O HOH A 518 -214.870 60.775 32.094 1.00 70.20 O
HETATM 2825 O HOH A 519 -235.900 43.148 47.116 1.00 60.62 O
HETATM 2826 O HOH A 520 -219.881 70.923 38.245 1.00 58.07 O
HETATM 2827 O HOH A 521 -224.122 62.618 32.361 1.00 72.70 O
HETATM 2828 O HOH A 522 -214.075 65.970 47.871 1.00 65.16 O
HETATM 2829 O HOH A 523 -229.601 75.575 46.637 1.00 77.38 O
HETATM 2830 O HOH A 524 -235.836 44.463 45.209 1.00 66.72 O
HETATM 2831 O HOH A 525 -211.468 62.255 50.276 1.00 76.29 O
CONECT 1 2 3 4
CONECT 2 1
CONECT 3 1
CONECT 4 1
CONECT 17 2255
CONECT 118 2604
CONECT 884 1485
CONECT 1485 884
CONECT 2255 17
CONECT 2575 2665
CONECT 2604 118 2605 2615
CONECT 2605 2604 2606 2612
CONECT 2606 2605 2607 2613
CONECT 2607 2606 2608 2614
CONECT 2608 2607 2609 2615
CONECT 2609 2608 2616
CONECT 2610 2611 2612 2617
CONECT 2611 2610
CONECT 2612 2605 2610
CONECT 2613 2606
CONECT 2614 2607 2618
CONECT 2615 2604 2608
CONECT 2616 2609
CONECT 2617 2610
CONECT 2618 2614 2619 2629
CONECT 2619 2618 2620 2626
CONECT 2620 2619 2621 2627
CONECT 2621 2620 2622 2628
CONECT 2622 2621 2623 2629
CONECT 2623 2622 2630
CONECT 2624 2625 2626 2631
CONECT 2625 2624
CONECT 2626 2619 2624
CONECT 2627 2620
CONECT 2628 2621 2632
CONECT 2629 2618 2622
CONECT 2630 2623
CONECT 2631 2624
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 2643
CONECT 2640 2635
CONECT 2641 2632 2636
CONECT 2642 2637 2654
CONECT 2643 2639 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 2642 2655 2663
CONECT 2655 2654 2656 2660
CONECT 2656 2655 2657 2661
CONECT 2657 2656 2658 2662
CONECT 2658 2657 2659 2663
CONECT 2659 2658 2664
CONECT 2660 2655
CONECT 2661 2656
CONECT 2662 2657
CONECT 2663 2654 2658
CONECT 2664 2659
CONECT 2665 2575 2666 2667
CONECT 2666 2665
CONECT 2667 2665 2668
CONECT 2668 2667 2669
CONECT 2669 2668 2670
CONECT 2670 2669 2671
CONECT 2671 2670 2672
CONECT 2672 2671 2673
CONECT 2673 2672 2674
CONECT 2674 2673 2675
CONECT 2675 2674 2676
CONECT 2676 2675 2677
CONECT 2677 2676 2678
CONECT 2678 2677 2679
CONECT 2679 2678 2680
CONECT 2680 2679 2681
CONECT 2681 2680
CONECT 2682 2683 2684 2691
CONECT 2683 2682 2694
CONECT 2684 2682 2685 2686
CONECT 2685 2684
CONECT 2686 2684 2687 2688
CONECT 2687 2686
CONECT 2688 2686 2689 2690
CONECT 2689 2688
CONECT 2690 2688 2691 2692
CONECT 2691 2682 2690
CONECT 2692 2690 2693
CONECT 2693 2692
CONECT 2694 2683 2695
CONECT 2695 2694 2696
CONECT 2696 2695 2697
CONECT 2697 2696 2698
CONECT 2698 2697 2699
CONECT 2699 2698 2700
CONECT 2700 2699 2701
CONECT 2701 2700
CONECT 2702 2703 2704 2711
CONECT 2703 2702 2714
CONECT 2704 2702 2705 2706
CONECT 2705 2704
CONECT 2706 2704 2707 2708
CONECT 2707 2706
CONECT 2708 2706 2709 2710
CONECT 2709 2708
CONECT 2710 2708 2711 2712
CONECT 2711 2702 2710
CONECT 2712 2710 2713
CONECT 2713 2712
CONECT 2714 2703 2715
CONECT 2715 2714 2716
CONECT 2716 2715 2717
CONECT 2717 2716 2718
CONECT 2718 2717 2719
CONECT 2719 2718 2720
CONECT 2720 2719 2721
CONECT 2721 2720
CONECT 2722 2723 2724 2731
CONECT 2723 2722 2734
CONECT 2724 2722 2725 2726
CONECT 2725 2724
CONECT 2726 2724 2727 2728
CONECT 2727 2726
CONECT 2728 2726 2729 2730
CONECT 2729 2728
CONECT 2730 2728 2731 2732
CONECT 2731 2722 2730
CONECT 2732 2730 2733
CONECT 2733 2732
CONECT 2734 2723 2735
CONECT 2735 2734 2736
CONECT 2736 2735 2737
CONECT 2737 2736 2738
CONECT 2738 2737 2739
CONECT 2739 2738 2740
CONECT 2740 2739 2741
CONECT 2741 2740
CONECT 2742 2743 2744 2751
CONECT 2743 2742 2754
CONECT 2744 2742 2745 2746
CONECT 2745 2744
CONECT 2746 2744 2747 2748
CONECT 2747 2746
CONECT 2748 2746 2749 2750
CONECT 2749 2748
CONECT 2750 2748 2751 2752
CONECT 2751 2742 2750
CONECT 2752 2750 2753
CONECT 2753 2752
CONECT 2754 2743 2755
CONECT 2755 2754 2756
CONECT 2756 2755 2757
CONECT 2757 2756 2758
CONECT 2758 2757 2759
CONECT 2759 2758 2760
CONECT 2760 2759 2761
CONECT 2761 2760
CONECT 2762 2763 2764 2771
CONECT 2763 2762 2774
CONECT 2764 2762 2765 2766
CONECT 2765 2764
CONECT 2766 2764 2767 2768
CONECT 2767 2766
CONECT 2768 2766 2769 2770
CONECT 2769 2768
CONECT 2770 2768 2771 2772
CONECT 2771 2762 2770
CONECT 2772 2770 2773
CONECT 2773 2772
CONECT 2774 2763 2775
CONECT 2775 2774 2776
CONECT 2776 2775 2777
CONECT 2777 2776 2778
CONECT 2778 2777 2779
CONECT 2779 2778 2780
CONECT 2780 2779 2781
CONECT 2781 2780
CONECT 2782 2783 2799
CONECT 2783 2782 2801
CONECT 2784 2801 2802 2805
CONECT 2785 2787 2802 2803
CONECT 2786 2790 2803 2804
CONECT 2787 2785 2791
CONECT 2788 2789 2801
CONECT 2789 2788 2799
CONECT 2790 2786 2791 2806
CONECT 2791 2787 2790
CONECT 2792 2793 2797
CONECT 2793 2792 2794 2800
CONECT 2794 2793 2795 2798
CONECT 2795 2794 2796
CONECT 2796 2795 2797
CONECT 2797 2792 2796
CONECT 2798 2794 2799
CONECT 2799 2782 2789 2798 2800
CONECT 2800 2793 2799
CONECT 2801 2783 2784 2788
CONECT 2802 2784 2785
CONECT 2803 2785 2786
CONECT 2804 2786
CONECT 2805 2784
CONECT 2806 2790
MASTER 345 0 13 15 4 0 0 6 2819 1 213 27
END