HEADER MEMBRANE PROTEIN 23-JAN-18 6FK9
TITLE CRYSTAL STRUCTURE OF N2C/D282C STABILIZED OPSIN BOUND TO RS09
CAVEAT 6FK9 NED DENSITY ABOVE LIGAND IN THE CHANNEL
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 6FK9 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 11-APR-18 6FK9 1 JRNL
REVDAT 1 04-APR-18 6FK9 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. 2.63 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) : 2.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.63
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 37419
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 1904
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 47.6336 - 6.3341 1.00 2596 163 0.2309 0.2351
REMARK 3 2 6.3341 - 5.0293 1.00 2570 144 0.2246 0.2539
REMARK 3 3 5.0293 - 4.3941 1.00 2560 131 0.1926 0.2250
REMARK 3 4 4.3941 - 3.9926 1.00 2532 147 0.1919 0.2202
REMARK 3 5 3.9926 - 3.7065 1.00 2525 153 0.2045 0.2471
REMARK 3 6 3.7065 - 3.4881 1.00 2565 122 0.2248 0.2635
REMARK 3 7 3.4881 - 3.3134 1.00 2531 119 0.2379 0.2752
REMARK 3 8 3.3134 - 3.1692 1.00 2530 148 0.2643 0.3057
REMARK 3 9 3.1692 - 3.0472 1.00 2531 122 0.2962 0.2740
REMARK 3 10 3.0472 - 2.9421 1.00 2527 125 0.3160 0.3804
REMARK 3 11 2.9421 - 2.8501 1.00 2506 136 0.3273 0.3749
REMARK 3 12 2.8501 - 2.7687 1.00 2529 146 0.3574 0.3838
REMARK 3 13 2.7687 - 2.6958 0.99 2508 121 0.3770 0.4165
REMARK 3 14 2.6958 - 2.6300 0.99 2505 127 0.4163 0.4949
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) : 0.490
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.720
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 2883
REMARK 3 ANGLE : 0.713 3925
REMARK 3 CHIRALITY : 0.044 454
REMARK 3 PLANARITY : 0.004 461
REMARK 3 DIHEDRAL : 11.623 1686
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):-230.6592 39.6603 39.5208
REMARK 3 T TENSOR
REMARK 3 T11: 0.5381 T22: 0.4326
REMARK 3 T33: 0.5751 T12: 0.0048
REMARK 3 T13: -0.0908 T23: 0.0480
REMARK 3 L TENSOR
REMARK 3 L11: 1.9470 L22: 2.5529
REMARK 3 L33: 1.0114 L12: 1.2126
REMARK 3 L13: -0.0866 L23: -0.0613
REMARK 3 S TENSOR
REMARK 3 S11: -0.0865 S12: 0.1578 S13: 0.1891
REMARK 3 S21: -0.3290 S22: 0.0549 S23: 0.2153
REMARK 3 S31: 0.0189 S32: -0.0564 S33: 0.0445
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 6FK9 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_1200008391.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-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 : 37496
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.630
REMARK 200 RESOLUTION RANGE LOW (A) : 47.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.51
REMARK 200 R MERGE (I) : 0.13660
REMARK 200 R SYM (I) : 0.13660
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 11.93
REMARK 200 R MERGE FOR SHELL (I) : 1.00790
REMARK 200 R SYM FOR SHELL (I) : 1.00790
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.530
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 121.59650
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.20377
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 37.22933
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 121.59650
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 70.20377
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 37.22933
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 121.59650
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 70.20377
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 37.22933
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 121.59650
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 70.20377
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.22933
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 121.59650
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 70.20377
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 37.22933
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 121.59650
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 70.20377
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.22933
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 140.40754
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 74.45867
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 140.40754
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 74.45867
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 140.40754
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 74.45867
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 140.40754
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 74.45867
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 140.40754
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 74.45867
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 140.40754
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 74.45867
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: 3340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17580 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 1.25
REMARK 500 OH TYR A 268 O2 BOG A 407 1.26
REMARK 500 O SER A 14 O HOH A 1000 2.14
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 51.17 -95.87
REMARK 500 SER A 176 -164.02 63.26
REMARK 500 PHE A 212 -34.71 -132.15
REMARK 500 ILE A 307 -55.71 -123.88
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6FK9 A 1 348 UNP P02699 OPSD_BOVIN 1 348
SEQADV 6FK9 ACE A 0 UNP P02699 ACETYLATION
SEQADV 6FK9 CYS A 2 UNP P02699 ASN 2 CONFLICT
SEQADV 6FK9 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 DNK A 411 26
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 DNK (2~{S})-3-METHYL-2-PHENYL-1-SPIRO[1,3-BENZODIOXOLE-2,
HETNAM 2 DNK 4'-PIPERIDINE]-1'-YL-BUTAN-1-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 4(C14 H28 O6)
FORMUL 8 DNK C22 H25 N O3
FORMUL 9 HOH *3(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 GLY A 90 1 21
HELIX 4 AA4 GLY A 90 HIS A 100 1 11
HELIX 5 AA5 PHE A 105 LYS A 141 1 37
HELIX 6 AA6 GLY A 149 ALA A 169 1 21
HELIX 7 AA7 ALA A 169 GLY A 174 1 6
HELIX 8 AA8 HIS A 195 THR A 198 5 4
HELIX 9 AA9 ASN A 199 HIS A 211 1 13
HELIX 10 AB1 ILE A 213 GLN A 237 1 25
HELIX 11 AB2 SER A 240 THR A 277 1 38
HELIX 12 AB3 THR A 289 LYS A 296 1 8
HELIX 13 AB4 THR A 297 ILE A 307 1 11
HELIX 14 AB5 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 2.04
LINK C ACE A 0 N MET A 1 1555 1555 1.33
LINK ND2 ASN A 15 C1 NAG B 1 1555 1555 1.45
LINK SG CYS A 322 C1 PLM A 401 1555 1555 1.73
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.44
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 243.193 243.193 111.688 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 0.004112 0.002374 0.000000 0.00000
SCALE2 0.000000 0.004748 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008954 0.00000
HETATM 1 C ACE A 0 -232.007 71.341 40.030 1.00122.71 C
ANISOU 1 C ACE A 0 14831 10948 20843 494 -1281 1254 C
HETATM 2 O ACE A 0 -232.107 70.597 39.059 1.00138.08 O
ANISOU 2 O ACE A 0 16834 13047 22584 477 -1443 1452 O
HETATM 3 CH3 ACE A 0 -233.191 72.067 40.604 1.00140.04 C
ANISOU 3 CH3 ACE A 0 16834 12875 23499 625 -1237 1152 C
ATOM 4 N MET A 1 -230.850 71.571 40.643 1.00 98.93 N
ANISOU 4 N MET A 1 11920 7993 17674 394 -1131 1111 N
ATOM 5 CA MET A 1 -229.562 70.990 40.273 1.00 96.22 C
ANISOU 5 CA MET A 1 11742 7887 16930 264 -1129 1168 C
ATOM 6 C MET A 1 -229.237 69.819 41.177 1.00 97.85 C
ANISOU 6 C MET A 1 11962 8358 16856 234 -987 952 C
ATOM 7 O MET A 1 -228.714 70.000 42.275 1.00112.61 O
ANISOU 7 O MET A 1 13837 10241 18707 188 -819 726 O
ATOM 8 CB MET A 1 -228.462 72.037 40.373 1.00103.04 C
ANISOU 8 CB MET A 1 12691 8631 17828 165 -1066 1160 C
ATOM 9 CG MET A 1 -228.392 72.964 39.212 1.00101.62 C
ANISOU 9 CG MET A 1 12560 8263 17789 145 -1230 1437 C
ATOM 10 SD MET A 1 -227.456 72.256 37.863 1.00105.45 S
ANISOU 10 SD MET A 1 13219 8987 17860 22 -1356 1694 S
ATOM 11 CE MET A 1 -228.182 73.228 36.568 1.00124.69 C
ANISOU 11 CE MET A 1 15658 11163 20554 53 -1596 2032 C
ATOM 12 N CYS A 2 -229.555 68.614 40.719 1.00101.79 N
ANISOU 12 N CYS A 2 12473 9064 17138 253 -1063 1024 N
ATOM 13 CA CYS A 2 -229.589 67.474 41.624 1.00105.90 C
ANISOU 13 CA CYS A 2 12976 9799 17464 253 -944 826 C
ATOM 14 C CYS A 2 -228.196 66.906 41.870 1.00 95.52 C
ANISOU 14 C CYS A 2 11781 8698 15814 137 -865 768 C
ATOM 15 O CYS A 2 -227.811 66.670 43.021 1.00107.08 O
ANISOU 15 O CYS A 2 13241 10241 17203 100 -720 554 O
ATOM 16 CB CYS A 2 -230.532 66.411 41.067 1.00125.04 C
ANISOU 16 CB CYS A 2 15355 12341 19815 319 -1054 919 C
ATOM 17 SG CYS A 2 -232.246 66.954 41.041 1.00133.61 S
ANISOU 17 SG CYS A 2 16251 13189 21326 463 -1128 945 S
ATOM 18 N GLY A 3 -227.427 66.694 40.805 1.00 85.21 N
ANISOU 18 N GLY A 3 10581 7483 14311 71 -959 957 N
ATOM 19 CA GLY A 3 -226.087 66.147 40.897 1.00 85.46 C
ANISOU 19 CA GLY A 3 10707 7708 14054 -33 -891 924 C
ATOM 20 C GLY A 3 -225.074 66.819 39.990 1.00 90.26 C
ANISOU 20 C GLY A 3 11413 8274 14606 -127 -936 1089 C
ATOM 21 O GLY A 3 -225.242 67.984 39.611 1.00100.68 O
ANISOU 21 O GLY A 3 12732 9380 16141 -127 -989 1187 O
ATOM 22 N THR A 4 -224.010 66.097 39.639 1.00 84.74 N
ANISOU 22 N THR A 4 10794 7771 13633 -210 -910 1123 N
ATOM 23 CA THR A 4 -222.915 66.636 38.839 1.00 80.19 C
ANISOU 23 CA THR A 4 10308 7183 12976 -318 -919 1259 C
ATOM 24 C THR A 4 -222.743 65.778 37.593 1.00 62.59 C
ANISOU 24 C THR A 4 8166 5107 10510 -351 -990 1430 C
ATOM 25 O THR A 4 -222.425 64.591 37.692 1.00 73.16 O
ANISOU 25 O THR A 4 9513 6647 11637 -355 -943 1367 O
ATOM 26 CB THR A 4 -221.615 66.686 39.645 1.00 81.33 C
ANISOU 26 CB THR A 4 10457 7411 13034 -408 -790 1118 C
ATOM 27 OG1 THR A 4 -221.789 67.541 40.778 1.00 76.82 O
ANISOU 27 OG1 THR A 4 9826 6692 12672 -397 -724 953 O
ATOM 28 CG2 THR A 4 -220.481 67.232 38.804 1.00 59.16 C
ANISOU 28 CG2 THR A 4 7729 4592 10156 -525 -787 1257 C
ATOM 29 N GLU A 5 -222.963 66.382 36.428 1.00 76.97 N
ANISOU 29 N GLU A 5 10056 6824 12365 -383 -1103 1645 N
ATOM 30 CA GLU A 5 -222.808 65.705 35.153 1.00 68.35 C
ANISOU 30 CA GLU A 5 9072 5862 11037 -442 -1171 1815 C
ATOM 31 C GLU A 5 -221.352 65.700 34.717 1.00 85.13 C
ANISOU 31 C GLU A 5 11283 8088 12976 -574 -1071 1846 C
ATOM 32 O GLU A 5 -220.529 66.492 35.179 1.00 99.83 O
ANISOU 32 O GLU A 5 13129 9875 14926 -630 -992 1797 O
ATOM 33 CB GLU A 5 -223.626 66.385 34.062 1.00 80.38 C
ANISOU 33 CB GLU A 5 10647 7235 12657 -444 -1347 2050 C
ATOM 34 CG GLU A 5 -225.104 66.099 34.051 1.00 72.55 C
ANISOU 34 CG GLU A 5 9582 6189 11794 -328 -1480 2078 C
ATOM 35 CD GLU A 5 -225.785 66.828 32.916 1.00 96.38 C
ANISOU 35 CD GLU A 5 12655 9057 14910 -348 -1679 2341 C
ATOM 36 OE1 GLU A 5 -225.387 67.980 32.627 1.00103.86 O
ANISOU 36 OE1 GLU A 5 13642 9838 15982 -404 -1703 2455 O
ATOM 37 OE2 GLU A 5 -226.705 66.251 32.303 1.00125.22 O
ANISOU 37 OE2 GLU A 5 16312 12753 18513 -316 -1820 2442 O
ATOM 38 N GLY A 6 -221.053 64.809 33.786 1.00 93.29 N
ANISOU 38 N GLY A 6 12407 9285 13755 -632 -1073 1928 N
ATOM 39 CA GLY A 6 -219.724 64.680 33.250 1.00 84.12 C
ANISOU 39 CA GLY A 6 11321 8230 12411 -759 -964 1959 C
ATOM 40 C GLY A 6 -219.682 63.574 32.223 1.00 74.66 C
ANISOU 40 C GLY A 6 10221 7205 10942 -805 -965 2027 C
ATOM 41 O GLY A 6 -220.637 62.805 32.072 1.00105.40 O
ANISOU 41 O GLY A 6 14114 11151 14783 -735 -1048 2027 O
ATOM 42 N PRO A 7 -218.580 63.471 31.482 1.00 70.26 N
ANISOU 42 N PRO A 7 9749 6737 10211 -933 -863 2080 N
ATOM 43 CA PRO A 7 -218.472 62.399 30.483 1.00 83.44 C
ANISOU 43 CA PRO A 7 11523 8570 11612 -992 -834 2121 C
ATOM 44 C PRO A 7 -218.384 61.049 31.177 1.00 87.52 C
ANISOU 44 C PRO A 7 11956 9240 12059 -907 -749 1933 C
ATOM 45 O PRO A 7 -217.480 60.811 31.984 1.00 85.23 O
ANISOU 45 O PRO A 7 11573 9006 11806 -895 -621 1795 O
ATOM 46 CB PRO A 7 -217.181 62.739 29.731 1.00 80.20 C
ANISOU 46 CB PRO A 7 11196 8199 11076 -1150 -704 2188 C
ATOM 47 CG PRO A 7 -216.886 64.166 30.079 1.00 61.21 C
ANISOU 47 CG PRO A 7 8761 5619 8877 -1183 -725 2248 C
ATOM 48 CD PRO A 7 -217.394 64.339 31.476 1.00 65.34 C
ANISOU 48 CD PRO A 7 9133 6063 9631 -1040 -761 2101 C
ATOM 49 N ASN A 8 -219.352 60.181 30.878 1.00 87.74 N
ANISOU 49 N ASN A 8 12013 9327 11996 -852 -834 1938 N
ATOM 50 CA ASN A 8 -219.453 58.796 31.328 1.00 57.53 C
ANISOU 50 CA ASN A 8 8135 5641 8084 -779 -775 1789 C
ATOM 51 C ASN A 8 -219.870 58.637 32.783 1.00 76.40 C
ANISOU 51 C ASN A 8 10374 8004 10651 -647 -783 1638 C
ATOM 52 O ASN A 8 -219.667 57.538 33.341 1.00 91.97 O
ANISOU 52 O ASN A 8 12290 10090 12566 -597 -710 1506 O
ATOM 53 CB ASN A 8 -218.149 58.016 31.146 1.00 65.51 C
ANISOU 53 CB ASN A 8 9154 6790 8947 -843 -590 1704 C
ATOM 54 CG ASN A 8 -217.596 58.130 29.754 1.00 84.85 C
ANISOU 54 CG ASN A 8 11754 9279 11204 -993 -535 1824 C
ATOM 55 OD1 ASN A 8 -218.323 58.396 28.798 1.00120.12 O
ANISOU 55 OD1 ASN A 8 16348 13714 15577 -1051 -653 1970 O
ATOM 56 ND2 ASN A 8 -216.294 57.921 29.626 1.00 77.08 N
ANISOU 56 ND2 ASN A 8 10757 8368 10160 -1065 -354 1767 N
ATOM 57 N PHE A 9 -220.429 59.661 33.426 1.00 67.74 N
ANISOU 57 N PHE A 9 9214 6759 9766 -596 -860 1648 N
ATOM 58 CA PHE A 9 -220.873 59.485 34.801 1.00 71.19 C
ANISOU 58 CA PHE A 9 9524 7178 10349 -488 -851 1493 C
ATOM 59 C PHE A 9 -221.894 60.545 35.179 1.00 70.26 C
ANISOU 59 C PHE A 9 9356 6879 10461 -428 -956 1526 C
ATOM 60 O PHE A 9 -221.993 61.601 34.549 1.00 77.58 O
ANISOU 60 O PHE A 9 10332 7674 11472 -471 -1026 1664 O
ATOM 61 CB PHE A 9 -219.693 59.505 35.788 1.00 76.97 C
ANISOU 61 CB PHE A 9 10182 7956 11109 -508 -720 1358 C
ATOM 62 CG PHE A 9 -218.957 60.817 35.848 1.00 80.39 C
ANISOU 62 CG PHE A 9 10615 8273 11655 -580 -691 1398 C
ATOM 63 CD1 PHE A 9 -217.764 60.984 35.158 1.00 81.80 C
ANISOU 63 CD1 PHE A 9 10846 8498 11738 -690 -609 1461 C
ATOM 64 CD2 PHE A 9 -219.440 61.873 36.614 1.00 78.93 C
ANISOU 64 CD2 PHE A 9 10376 7931 11684 -544 -732 1362 C
ATOM 65 CE1 PHE A 9 -217.073 62.176 35.216 1.00 73.60 C
ANISOU 65 CE1 PHE A 9 9806 7352 10807 -767 -580 1499 C
ATOM 66 CE2 PHE A 9 -218.754 63.069 36.672 1.00 66.08 C
ANISOU 66 CE2 PHE A 9 8752 6187 10167 -618 -704 1393 C
ATOM 67 CZ PHE A 9 -217.569 63.219 35.971 1.00 78.54 C
ANISOU 67 CZ PHE A 9 10383 7815 11642 -731 -634 1467 C
ATOM 68 N TYR A 10 -222.650 60.233 36.229 1.00 77.38 N
ANISOU 68 N TYR A 10 10159 7770 11471 -329 -960 1395 N
ATOM 69 CA TYR A 10 -223.571 61.159 36.878 1.00 65.92 C
ANISOU 69 CA TYR A 10 8628 6146 10272 -259 -1014 1367 C
ATOM 70 C TYR A 10 -223.445 60.924 38.376 1.00 77.27 C
ANISOU 70 C TYR A 10 9972 7617 11771 -217 -910 1157 C
ATOM 71 O TYR A 10 -223.812 59.848 38.870 1.00 91.38 O
ANISOU 71 O TYR A 10 11724 9519 13477 -170 -888 1063 O
ATOM 72 CB TYR A 10 -225.012 60.942 36.404 1.00 70.29 C
ANISOU 72 CB TYR A 10 9162 6650 10895 -186 -1151 1448 C
ATOM 73 CG TYR A 10 -226.016 61.774 37.166 1.00 77.90 C
ANISOU 73 CG TYR A 10 10014 7436 12149 -98 -1183 1393 C
ATOM 74 CD1 TYR A 10 -226.247 63.101 36.826 1.00 83.81 C
ANISOU 74 CD1 TYR A 10 10756 7979 13107 -100 -1254 1503 C
ATOM 75 CD2 TYR A 10 -226.726 61.236 38.229 1.00 62.82 C
ANISOU 75 CD2 TYR A 10 8003 5553 10313 -18 -1132 1228 C
ATOM 76 CE1 TYR A 10 -227.151 63.864 37.523 1.00 77.11 C
ANISOU 76 CE1 TYR A 10 9794 6950 12553 -14 -1266 1439 C
ATOM 77 CE2 TYR A 10 -227.629 61.989 38.931 1.00 86.91 C
ANISOU 77 CE2 TYR A 10 10947 8439 13637 57 -1132 1157 C
ATOM 78 CZ TYR A 10 -227.841 63.303 38.574 1.00 82.21 C
ANISOU 78 CZ TYR A 10 10337 7633 13267 64 -1196 1257 C
ATOM 79 OH TYR A 10 -228.747 64.057 39.278 1.00 80.41 O
ANISOU 79 OH TYR A 10 9990 7222 13341 146 -1180 1174 O
ATOM 80 N VAL A 11 -222.912 61.906 39.092 1.00 65.60 N
ANISOU 80 N VAL A 11 8463 6038 10423 -247 -849 1085 N
ATOM 81 CA VAL A 11 -222.754 61.827 40.541 1.00 76.14 C
ANISOU 81 CA VAL A 11 9728 7396 11805 -234 -755 885 C
ATOM 82 C VAL A 11 -223.995 62.441 41.183 1.00 80.87 C
ANISOU 82 C VAL A 11 10252 7840 12633 -155 -770 810 C
ATOM 83 O VAL A 11 -224.254 63.633 40.976 1.00 70.60 O
ANISOU 83 O VAL A 11 8943 6350 11532 -151 -800 861 O
ATOM 84 CB VAL A 11 -221.485 62.551 41.006 1.00 73.74 C
ANISOU 84 CB VAL A 11 9433 7072 11513 -327 -679 833 C
ATOM 85 CG1 VAL A 11 -221.415 62.584 42.527 1.00 66.27 C
ANISOU 85 CG1 VAL A 11 8429 6139 10614 -332 -599 628 C
ATOM 86 CG2 VAL A 11 -220.254 61.885 40.422 1.00 55.16 C
ANISOU 86 CG2 VAL A 11 7126 4874 8959 -400 -647 895 C
ATOM 87 N PRO A 12 -224.779 61.680 41.946 1.00 86.44 N
ANISOU 87 N PRO A 12 10900 8609 13334 -94 -743 690 N
ATOM 88 CA PRO A 12 -225.984 62.256 42.556 1.00 76.95 C
ANISOU 88 CA PRO A 12 9614 7256 12369 -20 -733 605 C
ATOM 89 C PRO A 12 -225.659 63.194 43.710 1.00 71.44 C
ANISOU 89 C PRO A 12 8888 6452 11802 -58 -623 436 C
ATOM 90 O PRO A 12 -226.051 62.948 44.855 1.00 79.58 O
ANISOU 90 O PRO A 12 9874 7509 12852 -49 -532 256 O
ATOM 91 CB PRO A 12 -226.755 61.021 43.029 1.00 66.49 C
ANISOU 91 CB PRO A 12 8246 6062 10956 33 -717 523 C
ATOM 92 CG PRO A 12 -225.679 60.025 43.310 1.00 70.91 C
ANISOU 92 CG PRO A 12 8862 6823 11256 -31 -671 485 C
ATOM 93 CD PRO A 12 -224.629 60.250 42.264 1.00 63.30 C
ANISOU 93 CD PRO A 12 7976 5881 10196 -90 -714 632 C
ATOM 94 N PHE A 13 -224.958 64.285 43.412 1.00 65.83 N
ANISOU 94 N PHE A 13 8213 5620 11179 -113 -627 489 N
ATOM 95 CA PHE A 13 -224.582 65.250 44.435 1.00 64.65 C
ANISOU 95 CA PHE A 13 8051 5358 11156 -166 -526 328 C
ATOM 96 C PHE A 13 -224.257 66.568 43.754 1.00 70.81 C
ANISOU 96 C PHE A 13 8855 5938 12111 -194 -567 442 C
ATOM 97 O PHE A 13 -223.505 66.587 42.773 1.00 73.69 O
ANISOU 97 O PHE A 13 9284 6344 12371 -243 -632 610 O
ATOM 98 CB PHE A 13 -223.387 64.741 45.246 1.00 66.32 C
ANISOU 98 CB PHE A 13 8302 5743 11152 -269 -454 216 C
ATOM 99 CG PHE A 13 -223.068 65.571 46.460 1.00 71.55 C
ANISOU 99 CG PHE A 13 8960 6322 11904 -342 -350 20 C
ATOM 100 CD1 PHE A 13 -223.712 65.336 47.662 1.00 62.70 C
ANISOU 100 CD1 PHE A 13 7807 5218 10797 -336 -259 -179 C
ATOM 101 CD2 PHE A 13 -222.104 66.565 46.407 1.00 67.22 C
ANISOU 101 CD2 PHE A 13 8447 5682 11412 -434 -338 30 C
ATOM 102 CE1 PHE A 13 -223.414 66.086 48.783 1.00 64.69 C
ANISOU 102 CE1 PHE A 13 8074 5399 11106 -424 -158 -372 C
ATOM 103 CE2 PHE A 13 -221.799 67.321 47.526 1.00 63.91 C
ANISOU 103 CE2 PHE A 13 8034 5185 11064 -517 -246 -160 C
ATOM 104 CZ PHE A 13 -222.454 67.084 48.714 1.00 66.14 C
ANISOU 104 CZ PHE A 13 8295 5488 11348 -515 -155 -365 C
ATOM 105 N SER A 14 -224.832 67.658 44.262 1.00 77.83 N
ANISOU 105 N SER A 14 9694 6605 13272 -166 -520 349 N
ATOM 106 CA SER A 14 -224.614 68.965 43.658 1.00 60.65 C
ANISOU 106 CA SER A 14 7537 4206 11300 -188 -562 459 C
ATOM 107 C SER A 14 -223.161 69.387 43.816 1.00 70.37 C
ANISOU 107 C SER A 14 8842 5478 12418 -324 -516 439 C
ATOM 108 O SER A 14 -222.524 69.103 44.832 1.00 78.20 O
ANISOU 108 O SER A 14 9842 6583 13286 -396 -422 263 O
ATOM 109 CB SER A 14 -225.525 70.014 44.292 1.00 81.73 C
ANISOU 109 CB SER A 14 10127 6615 14311 -126 -501 333 C
ATOM 110 OG SER A 14 -225.022 71.325 44.055 1.00 66.76 O
ANISOU 110 OG SER A 14 8261 4505 12599 -179 -504 381 O
ATOM 111 N ASN A 15 -222.640 70.087 42.809 1.00 80.88 N
ANISOU 111 N ASN A 15 10226 6712 13794 -368 -588 628 N
ATOM 112 CA ASN A 15 -221.263 70.561 42.824 1.00 76.37 C
ANISOU 112 CA ASN A 15 9713 6162 13140 -503 -548 633 C
ATOM 113 C ASN A 15 -221.147 72.031 43.225 1.00 79.76 C
ANISOU 113 C ASN A 15 10140 6331 13834 -549 -502 565 C
ATOM 114 O ASN A 15 -220.105 72.646 42.981 1.00 79.48 O
ANISOU 114 O ASN A 15 10155 6262 13783 -661 -492 618 O
ATOM 115 CB ASN A 15 -220.613 70.340 41.454 1.00 85.89 C
ANISOU 115 CB ASN A 15 10992 7449 14195 -552 -632 878 C
ATOM 116 CG ASN A 15 -219.106 70.286 41.531 1.00 80.67 C
ANISOU 116 CG ASN A 15 10370 6913 13369 -689 -572 862 C
ATOM 117 OD1 ASN A 15 -218.543 70.208 42.623 1.00 60.67 O
ANISOU 117 OD1 ASN A 15 7809 4445 10799 -743 -490 676 O
ATOM 118 ND2 ASN A 15 -218.435 70.320 40.376 1.00100.52 N
ANISOU 118 ND2 ASN A 15 12948 9464 15780 -755 -612 1058 N
ATOM 119 N LYS A 16 -222.189 72.610 43.830 1.00 85.40 N
ANISOU 119 N LYS A 16 10792 6852 14805 -467 -464 443 N
ATOM 120 CA LYS A 16 -222.104 74.018 44.216 1.00 83.47 C
ANISOU 120 CA LYS A 16 10544 6336 14835 -507 -408 364 C
ATOM 121 C LYS A 16 -220.984 74.255 45.227 1.00 78.61 C
ANISOU 121 C LYS A 16 9966 5786 14115 -653 -298 167 C
ATOM 122 O LYS A 16 -220.339 75.307 45.202 1.00 85.95 O
ANISOU 122 O LYS A 16 10930 6555 15170 -744 -278 170 O
ATOM 123 CB LYS A 16 -223.449 74.505 44.768 1.00 83.50 C
ANISOU 123 CB LYS A 16 10458 6124 15145 -387 -360 236 C
ATOM 124 CG LYS A 16 -223.946 73.760 45.984 1.00 97.07 C
ANISOU 124 CG LYS A 16 12130 7973 16779 -361 -242 -21 C
ATOM 125 CD LYS A 16 -225.379 74.132 46.331 1.00 88.10 C
ANISOU 125 CD LYS A 16 10887 6632 15955 -228 -192 -119 C
ATOM 126 CE LYS A 16 -225.884 73.222 47.445 1.00111.89 C
ANISOU 126 CE LYS A 16 13863 9812 18836 -214 -72 -352 C
ATOM 127 NZ LYS A 16 -227.351 73.310 47.675 1.00129.28 N
ANISOU 127 NZ LYS A 16 15942 11865 21314 -75 -23 -431 N
ATOM 128 N THR A 17 -220.736 73.282 46.114 1.00 79.45 N
ANISOU 128 N THR A 17 10069 6125 13993 -685 -237 5 N
ATOM 129 CA THR A 17 -219.589 73.316 47.020 1.00 80.68 C
ANISOU 129 CA THR A 17 10262 6392 14002 -837 -168 -152 C
ATOM 130 C THR A 17 -218.257 73.213 46.287 1.00 78.92 C
ANISOU 130 C THR A 17 10079 6285 13620 -941 -228 12 C
ATOM 131 O THR A 17 -217.227 73.620 46.832 1.00 80.27 O
ANISOU 131 O THR A 17 10272 6476 13749 -1080 -189 -77 O
ATOM 132 CB THR A 17 -219.675 72.158 48.025 1.00121.47 C
ANISOU 132 CB THR A 17 15416 11797 18942 -844 -121 -316 C
ATOM 133 OG1 THR A 17 -221.041 71.768 48.208 1.00145.46 O
ANISOU 133 OG1 THR A 17 18404 14800 22065 -710 -96 -372 O
ATOM 134 CG2 THR A 17 -219.073 72.557 49.372 1.00134.15 C
ANISOU 134 CG2 THR A 17 17051 13412 20506 -987 -27 -563 C
ATOM 135 N GLY A 18 -218.243 72.636 45.088 1.00 91.24 N
ANISOU 135 N GLY A 18 11649 7935 15083 -887 -314 241 N
ATOM 136 CA GLY A 18 -217.012 72.341 44.390 1.00 81.41 C
ANISOU 136 CA GLY A 18 10435 6833 13665 -982 -345 382 C
ATOM 137 C GLY A 18 -216.303 71.079 44.832 1.00 86.11 C
ANISOU 137 C GLY A 18 11009 7715 13993 -1017 -332 323 C
ATOM 138 O GLY A 18 -215.186 70.824 44.366 1.00 83.67 O
ANISOU 138 O GLY A 18 10706 7526 13560 -1101 -339 414 O
ATOM 139 N VAL A 19 -216.908 70.275 45.710 1.00 91.01 N
ANISOU 139 N VAL A 19 11600 8444 14533 -957 -310 177 N
ATOM 140 CA VAL A 19 -216.199 69.130 46.280 1.00 72.86 C
ANISOU 140 CA VAL A 19 9281 6400 12003 -1000 -306 116 C
ATOM 141 C VAL A 19 -216.319 67.881 45.427 1.00 81.00 C
ANISOU 141 C VAL A 19 10304 7603 12869 -917 -353 259 C
ATOM 142 O VAL A 19 -215.543 66.937 45.618 1.00 84.80 O
ANISOU 142 O VAL A 19 10762 8283 13176 -952 -356 256 O
ATOM 143 CB VAL A 19 -216.689 68.817 47.705 1.00 60.79 C
ANISOU 143 CB VAL A 19 7740 4921 10438 -1004 -259 -108 C
ATOM 144 CG1 VAL A 19 -216.510 70.022 48.619 1.00 61.76 C
ANISOU 144 CG1 VAL A 19 7883 4881 10702 -1109 -197 -281 C
ATOM 145 CG2 VAL A 19 -218.145 68.347 47.678 1.00 66.23 C
ANISOU 145 CG2 VAL A 19 8415 5581 11170 -860 -253 -127 C
ATOM 146 N VAL A 20 -217.273 67.843 44.500 1.00 79.76 N
ANISOU 146 N VAL A 20 10164 7370 12770 -811 -394 385 N
ATOM 147 CA VAL A 20 -217.485 66.646 43.707 1.00 71.16 C
ANISOU 147 CA VAL A 20 9080 6439 11520 -740 -436 503 C
ATOM 148 C VAL A 20 -216.209 66.300 42.944 1.00 71.35 C
ANISOU 148 C VAL A 20 9118 6585 11406 -821 -431 621 C
ATOM 149 O VAL A 20 -215.386 67.174 42.633 1.00 81.10 O
ANISOU 149 O VAL A 20 10368 7741 12704 -916 -413 673 O
ATOM 150 CB VAL A 20 -218.698 66.819 42.772 1.00 64.16 C
ANISOU 150 CB VAL A 20 8214 5433 10730 -636 -501 633 C
ATOM 151 CG1 VAL A 20 -218.918 65.574 41.909 1.00 57.62 C
ANISOU 151 CG1 VAL A 20 7406 4770 9719 -580 -547 749 C
ATOM 152 CG2 VAL A 20 -219.960 67.124 43.593 1.00 62.64 C
ANISOU 152 CG2 VAL A 20 7978 5116 10704 -550 -488 500 C
ATOM 153 N ARG A 21 -216.016 65.004 42.698 1.00 59.52 N
ANISOU 153 N ARG A 21 7607 5278 9729 -787 -434 650 N
ATOM 154 CA ARG A 21 -214.909 64.481 41.909 1.00 60.30 C
ANISOU 154 CA ARG A 21 7709 5503 9701 -845 -409 751 C
ATOM 155 C ARG A 21 -215.422 63.351 41.027 1.00 63.48 C
ANISOU 155 C ARG A 21 8140 6012 9965 -766 -431 842 C
ATOM 156 O ARG A 21 -216.488 62.775 41.270 1.00 68.00 O
ANISOU 156 O ARG A 21 8714 6601 10523 -671 -469 804 O
ATOM 157 CB ARG A 21 -213.764 63.949 42.777 1.00 57.32 C
ANISOU 157 CB ARG A 21 7259 5268 9254 -912 -373 651 C
ATOM 158 CG ARG A 21 -213.172 64.950 43.739 1.00 60.37 C
ANISOU 158 CG ARG A 21 7617 5574 9748 -1012 -360 546 C
ATOM 159 CD ARG A 21 -212.247 65.907 43.026 1.00 55.88 C
ANISOU 159 CD ARG A 21 7058 4922 9251 -1117 -331 640 C
ATOM 160 NE ARG A 21 -212.796 67.258 42.994 1.00 96.46 N
ANISOU 160 NE ARG A 21 12249 9843 14560 -1136 -340 643 N
ATOM 161 CZ ARG A 21 -212.590 68.168 43.936 1.00 79.09 C
ANISOU 161 CZ ARG A 21 10036 7538 12476 -1210 -329 519 C
ATOM 162 NH1 ARG A 21 -211.845 67.876 44.993 1.00 82.17 N
ANISOU 162 NH1 ARG A 21 10371 8038 12813 -1284 -323 390 N
ATOM 163 NH2 ARG A 21 -213.132 69.369 43.823 1.00 99.57 N
ANISOU 163 NH2 ARG A 21 12675 9913 15244 -1216 -331 525 N
ATOM 164 N SER A 22 -214.639 63.031 40.011 1.00 63.59 N
ANISOU 164 N SER A 22 8180 6100 9880 -816 -396 952 N
ATOM 165 CA SER A 22 -215.012 61.967 39.100 1.00 75.19 C
ANISOU 165 CA SER A 22 9693 7673 11204 -764 -402 1029 C
ATOM 166 C SER A 22 -215.092 60.643 39.852 1.00 80.21 C
ANISOU 166 C SER A 22 10269 8456 11753 -696 -393 920 C
ATOM 167 O SER A 22 -214.185 60.332 40.637 1.00 71.17 O
ANISOU 167 O SER A 22 9048 7390 10603 -730 -355 837 O
ATOM 168 CB SER A 22 -214.010 61.836 37.969 1.00 76.09 C
ANISOU 168 CB SER A 22 9844 7848 11218 -850 -333 1137 C
ATOM 169 OG SER A 22 -214.396 60.747 37.162 1.00 76.27 O
ANISOU 169 OG SER A 22 9916 7972 11090 -806 -330 1184 O
ATOM 170 N PRO A 23 -216.137 59.837 39.642 1.00 77.48 N
ANISOU 170 N PRO A 23 9951 8146 11343 -607 -437 926 N
ATOM 171 CA PRO A 23 -216.193 58.539 40.321 1.00 80.20 C
ANISOU 171 CA PRO A 23 10244 8623 11604 -549 -428 834 C
ATOM 172 C PRO A 23 -215.138 57.562 39.830 1.00 72.09 C
ANISOU 172 C PRO A 23 9197 7727 10466 -576 -358 856 C
ATOM 173 O PRO A 23 -214.994 56.472 40.392 1.00 71.06 O
ANISOU 173 O PRO A 23 9015 7700 10285 -534 -349 790 O
ATOM 174 CB PRO A 23 -217.613 58.037 40.016 1.00 72.47 C
ANISOU 174 CB PRO A 23 9308 7630 10598 -459 -491 855 C
ATOM 175 CG PRO A 23 -218.019 58.754 38.785 1.00 71.53 C
ANISOU 175 CG PRO A 23 9270 7416 10491 -481 -532 993 C
ATOM 176 CD PRO A 23 -217.385 60.116 38.899 1.00 83.73 C
ANISOU 176 CD PRO A 23 10812 8846 12156 -556 -514 1016 C
ATOM 177 N PHE A 24 -214.404 57.930 38.785 1.00 75.14 N
ANISOU 177 N PHE A 24 9621 8105 10824 -648 -303 947 N
ATOM 178 CA PHE A 24 -213.293 57.134 38.303 1.00 76.97 C
ANISOU 178 CA PHE A 24 9817 8445 10981 -684 -207 955 C
ATOM 179 C PHE A 24 -211.944 57.580 38.851 1.00 73.19 C
ANISOU 179 C PHE A 24 9239 7981 10589 -760 -153 921 C
ATOM 180 O PHE A 24 -210.966 56.846 38.703 1.00 86.69 O
ANISOU 180 O PHE A 24 10879 9781 12280 -777 -74 907 O
ATOM 181 CB PHE A 24 -213.241 57.180 36.777 1.00 62.70 C
ANISOU 181 CB PHE A 24 8116 6637 9072 -737 -154 1066 C
ATOM 182 CG PHE A 24 -214.490 56.701 36.108 1.00 66.36 C
ANISOU 182 CG PHE A 24 8681 7098 9437 -682 -220 1113 C
ATOM 183 CD1 PHE A 24 -214.955 55.408 36.299 1.00 63.21 C
ANISOU 183 CD1 PHE A 24 8267 6783 8966 -602 -227 1051 C
ATOM 184 CD2 PHE A 24 -215.184 57.539 35.256 1.00 66.76 C
ANISOU 184 CD2 PHE A 24 8839 7056 9471 -718 -284 1230 C
ATOM 185 CE1 PHE A 24 -216.112 54.964 35.651 1.00 59.59 C
ANISOU 185 CE1 PHE A 24 7901 6324 8418 -564 -294 1094 C
ATOM 186 CE2 PHE A 24 -216.325 57.111 34.610 1.00 68.55 C
ANISOU 186 CE2 PHE A 24 9153 7282 9611 -678 -365 1285 C
ATOM 187 CZ PHE A 24 -216.790 55.819 34.807 1.00 76.21 C
ANISOU 187 CZ PHE A 24 10106 8344 10506 -604 -368 1211 C
ATOM 188 N GLU A 25 -211.862 58.758 39.478 1.00 70.54 N
ANISOU 188 N GLU A 25 8888 7551 10362 -809 -192 904 N
ATOM 189 CA GLU A 25 -210.588 59.341 39.875 1.00 68.52 C
ANISOU 189 CA GLU A 25 8547 7296 10193 -904 -149 884 C
ATOM 190 C GLU A 25 -210.376 59.466 41.379 1.00 66.60 C
ANISOU 190 C GLU A 25 8218 7063 10023 -912 -210 773 C
ATOM 191 O GLU A 25 -209.228 59.393 41.826 1.00 85.08 O
ANISOU 191 O GLU A 25 10455 9460 12410 -974 -190 747 O
ATOM 192 CB GLU A 25 -210.413 60.743 39.260 1.00 52.99 C
ANISOU 192 CB GLU A 25 6640 5202 8291 -997 -132 963 C
ATOM 193 CG GLU A 25 -210.108 60.782 37.758 1.00 80.19 C
ANISOU 193 CG GLU A 25 10161 8651 11656 -1052 -49 1087 C
ATOM 194 CD GLU A 25 -209.763 62.199 37.243 1.00114.22 C
ANISOU 194 CD GLU A 25 14523 12834 16040 -1166 -32 1176 C
ATOM 195 OE1 GLU A 25 -210.069 63.209 37.924 1.00 85.39 O
ANISOU 195 OE1 GLU A 25 10872 9062 12511 -1179 -99 1150 O
ATOM 196 OE2 GLU A 25 -209.177 62.300 36.144 1.00127.97 O
ANISOU 196 OE2 GLU A 25 16312 14593 17720 -1249 58 1271 O
ATOM 197 N ALA A 26 -211.428 59.681 42.170 1.00 64.61 N
ANISOU 197 N ALA A 26 8004 6760 9786 -862 -283 706 N
ATOM 198 CA ALA A 26 -211.260 60.093 43.560 1.00 56.57 C
ANISOU 198 CA ALA A 26 6937 5730 8827 -906 -332 596 C
ATOM 199 C ALA A 26 -212.441 59.609 44.382 1.00 57.46 C
ANISOU 199 C ALA A 26 7081 5852 8898 -825 -384 512 C
ATOM 200 O ALA A 26 -213.545 59.459 43.846 1.00 61.06 O
ANISOU 200 O ALA A 26 7601 6265 9333 -744 -390 543 O
ATOM 201 CB ALA A 26 -211.131 61.623 43.677 1.00 64.50 C
ANISOU 201 CB ALA A 26 7970 6589 9947 -994 -330 584 C
ATOM 202 N PRO A 27 -212.254 59.384 45.681 1.00 65.56 N
ANISOU 202 N PRO A 27 8065 6935 9911 -857 -424 410 N
ATOM 203 CA PRO A 27 -213.328 58.791 46.484 1.00 72.95 C
ANISOU 203 CA PRO A 27 9031 7899 10789 -793 -457 330 C
ATOM 204 C PRO A 27 -214.513 59.726 46.644 1.00 62.25 C
ANISOU 204 C PRO A 27 7742 6403 9507 -771 -447 272 C
ATOM 205 O PRO A 27 -214.367 60.943 46.760 1.00 89.58 O
ANISOU 205 O PRO A 27 11220 9747 13070 -835 -432 240 O
ATOM 206 CB PRO A 27 -212.659 58.506 47.835 1.00 63.48 C
ANISOU 206 CB PRO A 27 7781 6789 9550 -872 -505 245 C
ATOM 207 CG PRO A 27 -211.453 59.363 47.865 1.00 65.20 C
ANISOU 207 CG PRO A 27 7951 6981 9842 -986 -505 255 C
ATOM 208 CD PRO A 27 -211.010 59.556 46.449 1.00 54.89 C
ANISOU 208 CD PRO A 27 6634 5639 8585 -964 -448 373 C
ATOM 209 N GLN A 28 -215.697 59.124 46.656 1.00 72.95 N
ANISOU 209 N GLN A 28 9127 7765 10826 -677 -454 255 N
ATOM 210 CA GLN A 28 -216.976 59.828 46.706 1.00 72.42 C
ANISOU 210 CA GLN A 28 9101 7565 10852 -629 -441 208 C
ATOM 211 C GLN A 28 -217.499 59.930 48.137 1.00 80.15 C
ANISOU 211 C GLN A 28 10082 8542 11829 -660 -424 45 C
ATOM 212 O GLN A 28 -218.651 59.602 48.424 1.00 74.91 O
ANISOU 212 O GLN A 28 9429 7864 11169 -594 -410 -8 O
ATOM 213 CB GLN A 28 -217.980 59.122 45.802 1.00 63.25 C
ANISOU 213 CB GLN A 28 7959 6410 9665 -517 -459 291 C
ATOM 214 CG GLN A 28 -217.501 58.990 44.364 1.00 61.80 C
ANISOU 214 CG GLN A 28 7795 6235 9451 -506 -468 444 C
ATOM 215 CD GLN A 28 -217.555 60.300 43.610 1.00 77.34 C
ANISOU 215 CD GLN A 28 9797 8047 11540 -532 -470 518 C
ATOM 216 OE1 GLN A 28 -218.553 61.020 43.667 1.00 76.04 O
ANISOU 216 OE1 GLN A 28 9646 7748 11496 -493 -488 501 O
ATOM 217 NE2 GLN A 28 -216.478 60.620 42.901 1.00 82.77 N
ANISOU 217 NE2 GLN A 28 10493 8743 12212 -601 -449 604 N
ATOM 218 N TYR A 29 -216.647 60.411 49.048 1.00 77.15 N
ANISOU 218 N TYR A 29 9696 8178 11440 -775 -422 -40 N
ATOM 219 CA TYR A 29 -216.969 60.447 50.473 1.00 83.34 C
ANISOU 219 CA TYR A 29 10501 8987 12178 -840 -403 -202 C
ATOM 220 C TYR A 29 -217.919 61.574 50.851 1.00 78.68 C
ANISOU 220 C TYR A 29 9943 8225 11725 -842 -333 -325 C
ATOM 221 O TYR A 29 -218.277 61.693 52.028 1.00 77.70 O
ANISOU 221 O TYR A 29 9848 8109 11564 -906 -290 -482 O
ATOM 222 CB TYR A 29 -215.687 60.555 51.302 1.00 80.63 C
ANISOU 222 CB TYR A 29 10145 8727 11765 -981 -442 -244 C
ATOM 223 CG TYR A 29 -214.876 59.278 51.332 1.00 76.51 C
ANISOU 223 CG TYR A 29 9575 8380 11114 -981 -512 -155 C
ATOM 224 CD1 TYR A 29 -215.490 58.044 51.495 1.00 94.31 C
ANISOU 224 CD1 TYR A 29 11833 10733 13268 -907 -528 -136 C
ATOM 225 CD2 TYR A 29 -213.499 59.308 51.186 1.00 77.00 C
ANISOU 225 CD2 TYR A 29 9578 8498 11180 -1054 -560 -88 C
ATOM 226 CE1 TYR A 29 -214.750 56.876 51.517 1.00 94.25 C
ANISOU 226 CE1 TYR A 29 11777 10863 13171 -900 -593 -52 C
ATOM 227 CE2 TYR A 29 -212.755 58.151 51.208 1.00 81.96 C
ANISOU 227 CE2 TYR A 29 10143 9267 11730 -1043 -622 -6 C
ATOM 228 CZ TYR A 29 -213.381 56.939 51.371 1.00 83.76 C
ANISOU 228 CZ TYR A 29 10380 9579 11865 -964 -640 13 C
ATOM 229 OH TYR A 29 -212.629 55.790 51.389 1.00 87.34 O
ANISOU 229 OH TYR A 29 10765 10152 12268 -948 -702 98 O
ATOM 230 N TYR A 30 -218.327 62.409 49.895 1.00 86.27 N
ANISOU 230 N TYR A 30 10902 9029 12848 -780 -318 -259 N
ATOM 231 CA TYR A 30 -219.405 63.353 50.161 1.00 93.20 C
ANISOU 231 CA TYR A 30 11790 9726 13897 -748 -252 -364 C
ATOM 232 C TYR A 30 -220.767 62.707 49.944 1.00 88.40 C
ANISOU 232 C TYR A 30 11160 9114 13313 -622 -240 -356 C
ATOM 233 O TYR A 30 -221.760 63.167 50.516 1.00109.44 O
ANISOU 233 O TYR A 30 13817 11672 16096 -598 -168 -484 O
ATOM 234 CB TYR A 30 -219.249 64.602 49.285 1.00 74.80 C
ANISOU 234 CB TYR A 30 9461 7205 11756 -742 -256 -286 C
ATOM 235 CG TYR A 30 -218.809 64.292 47.879 1.00 73.67 C
ANISOU 235 CG TYR A 30 9312 7096 11584 -695 -325 -72 C
ATOM 236 CD1 TYR A 30 -219.738 64.021 46.879 1.00 73.20 C
ANISOU 236 CD1 TYR A 30 9247 6992 11575 -577 -362 49 C
ATOM 237 CD2 TYR A 30 -217.462 64.241 47.555 1.00 60.07 C
ANISOU 237 CD2 TYR A 30 7589 5455 9779 -778 -351 5 C
ATOM 238 CE1 TYR A 30 -219.333 63.718 45.590 1.00 70.66 C
ANISOU 238 CE1 TYR A 30 8941 6710 11197 -555 -419 236 C
ATOM 239 CE2 TYR A 30 -217.046 63.934 46.273 1.00 66.54 C
ANISOU 239 CE2 TYR A 30 8411 6310 10559 -749 -388 185 C
ATOM 240 CZ TYR A 30 -217.984 63.673 45.295 1.00 72.35 C
ANISOU 240 CZ TYR A 30 9163 7005 11320 -643 -420 297 C
ATOM 241 OH TYR A 30 -217.572 63.374 44.017 1.00 72.88 O
ANISOU 241 OH TYR A 30 9253 7114 11322 -635 -450 466 O
ATOM 242 N LEU A 31 -220.831 61.649 49.127 1.00 82.01 N
ANISOU 242 N LEU A 31 10338 8417 12405 -546 -303 -215 N
ATOM 243 CA LEU A 31 -222.061 60.869 48.995 1.00 81.54 C
ANISOU 243 CA LEU A 31 10256 8381 12344 -443 -302 -209 C
ATOM 244 C LEU A 31 -222.383 60.125 50.279 1.00 76.49 C
ANISOU 244 C LEU A 31 9623 7854 11585 -482 -251 -354 C
ATOM 245 O LEU A 31 -223.549 60.032 50.677 1.00 82.62 O
ANISOU 245 O LEU A 31 10378 8587 12426 -434 -195 -440 O
ATOM 246 CB LEU A 31 -221.942 59.863 47.849 1.00 64.72 C
ANISOU 246 CB LEU A 31 8125 6353 10114 -376 -379 -36 C
ATOM 247 CG LEU A 31 -221.786 60.377 46.422 1.00 79.98 C
ANISOU 247 CG LEU A 31 10069 8199 12122 -340 -435 131 C
ATOM 248 CD1 LEU A 31 -221.652 59.204 45.476 1.00 76.20 C
ANISOU 248 CD1 LEU A 31 9604 7848 11499 -297 -489 261 C
ATOM 249 CD2 LEU A 31 -222.979 61.238 46.060 1.00 87.68 C
ANISOU 249 CD2 LEU A 31 11020 8989 13306 -268 -443 143 C
ATOM 250 N ALA A 32 -221.371 59.551 50.920 1.00 82.16 N
ANISOU 250 N ALA A 32 10367 8719 12130 -573 -272 -373 N
ATOM 251 CA ALA A 32 -221.590 58.778 52.132 1.00 66.93 C
ANISOU 251 CA ALA A 32 8461 6911 10059 -630 -242 -485 C
ATOM 252 C ALA A 32 -220.304 58.731 52.928 1.00 69.90 C
ANISOU 252 C ALA A 32 8867 7390 10301 -765 -279 -516 C
ATOM 253 O ALA A 32 -219.206 58.790 52.370 1.00 70.30 O
ANISOU 253 O ALA A 32 8900 7471 10342 -786 -343 -412 O
ATOM 254 CB ALA A 32 -222.059 57.359 51.824 1.00 48.21 C
ANISOU 254 CB ALA A 32 6075 4660 7581 -551 -281 -401 C
ATOM 255 N GLU A 33 -220.462 58.614 54.249 1.00 59.04 N
ANISOU 255 N GLU A 33 7537 6074 8821 -867 -238 -658 N
ATOM 256 CA GLU A 33 -219.324 58.504 55.138 1.00 66.72 C
ANISOU 256 CA GLU A 33 8544 7158 9650 -1014 -294 -687 C
ATOM 257 C GLU A 33 -218.471 57.297 54.749 1.00 87.68 C
ANISOU 257 C GLU A 33 11160 9960 12193 -987 -409 -523 C
ATOM 258 O GLU A 33 -218.956 56.363 54.105 1.00 90.08 O
ANISOU 258 O GLU A 33 11438 10303 12487 -873 -423 -430 O
ATOM 259 CB GLU A 33 -219.804 58.378 56.581 1.00 72.40 C
ANISOU 259 CB GLU A 33 9335 7934 10238 -1131 -235 -854 C
ATOM 260 CG GLU A 33 -220.492 59.616 57.096 1.00 75.75 C
ANISOU 260 CG GLU A 33 9797 8208 10777 -1181 -102 -1047 C
ATOM 261 CD GLU A 33 -219.508 60.717 57.397 1.00108.68 C
ANISOU 261 CD GLU A 33 13995 12319 14979 -1308 -117 -1111 C
ATOM 262 OE1 GLU A 33 -218.695 60.541 58.329 1.00120.57 O
ANISOU 262 OE1 GLU A 33 15555 13943 16314 -1465 -175 -1152 O
ATOM 263 OE2 GLU A 33 -219.535 61.750 56.694 1.00125.33 O
ANISOU 263 OE2 GLU A 33 16072 14262 17284 -1257 -81 -1110 O
ATOM 264 N PRO A 34 -217.186 57.309 55.109 1.00 74.34 N
ANISOU 264 N PRO A 34 9460 8347 10439 -1092 -492 -488 N
ATOM 265 CA PRO A 34 -216.350 56.137 54.807 1.00 64.35 C
ANISOU 265 CA PRO A 34 8140 7210 9099 -1062 -595 -339 C
ATOM 266 C PRO A 34 -216.887 54.848 55.402 1.00 67.35 C
ANISOU 266 C PRO A 34 8546 7702 9342 -1046 -622 -325 C
ATOM 267 O PRO A 34 -216.811 53.800 54.751 1.00 75.61 O
ANISOU 267 O PRO A 34 9546 8799 10381 -948 -660 -204 O
ATOM 268 CB PRO A 34 -214.987 56.523 55.397 1.00 61.92 C
ANISOU 268 CB PRO A 34 7812 6955 8760 -1205 -679 -336 C
ATOM 269 CG PRO A 34 -214.970 58.008 55.331 1.00 53.26 C
ANISOU 269 CG PRO A 34 6740 5724 7773 -1263 -614 -435 C
ATOM 270 CD PRO A 34 -216.387 58.437 55.617 1.00 65.86 C
ANISOU 270 CD PRO A 34 8404 7225 9394 -1228 -498 -569 C
ATOM 271 N TRP A 35 -217.449 54.892 56.616 1.00 65.54 N
ANISOU 271 N TRP A 35 8394 7506 9002 -1147 -592 -450 N
ATOM 272 CA TRP A 35 -217.950 53.659 57.216 1.00 67.27 C
ANISOU 272 CA TRP A 35 8646 7832 9082 -1148 -617 -426 C
ATOM 273 C TRP A 35 -219.115 53.081 56.427 1.00 76.04 C
ANISOU 273 C TRP A 35 9738 8901 10254 -994 -547 -397 C
ATOM 274 O TRP A 35 -219.302 51.860 56.403 1.00 84.33 O
ANISOU 274 O TRP A 35 10781 10029 11232 -948 -590 -314 O
ATOM 275 CB TRP A 35 -218.360 53.885 58.672 1.00 68.03 C
ANISOU 275 CB TRP A 35 8845 7974 9029 -1309 -580 -574 C
ATOM 276 CG TRP A 35 -219.577 54.740 58.871 1.00 79.11 C
ANISOU 276 CG TRP A 35 10295 9268 10496 -1305 -416 -749 C
ATOM 277 CD1 TRP A 35 -219.601 56.084 59.089 1.00 74.58 C
ANISOU 277 CD1 TRP A 35 9747 8584 10005 -1370 -335 -891 C
ATOM 278 CD2 TRP A 35 -220.945 54.305 58.900 1.00 90.73 C
ANISOU 278 CD2 TRP A 35 11780 10718 11976 -1233 -309 -804 C
ATOM 279 NE1 TRP A 35 -220.893 56.517 59.240 1.00 78.93 N
ANISOU 279 NE1 TRP A 35 10320 9039 10631 -1335 -179 -1033 N
ATOM 280 CE2 TRP A 35 -221.739 55.445 59.129 1.00 94.75 C
ANISOU 280 CE2 TRP A 35 12311 11100 12591 -1252 -162 -981 C
ATOM 281 CE3 TRP A 35 -221.573 53.065 58.749 1.00 95.85 C
ANISOU 281 CE3 TRP A 35 12416 11434 12568 -1157 -322 -723 C
ATOM 282 CZ2 TRP A 35 -223.130 55.384 59.209 1.00 85.44 C
ANISOU 282 CZ2 TRP A 35 11126 9863 11473 -1193 -26 -1077 C
ATOM 283 CZ3 TRP A 35 -222.955 53.006 58.831 1.00 85.93 C
ANISOU 283 CZ3 TRP A 35 11165 10128 11356 -1109 -192 -817 C
ATOM 284 CH2 TRP A 35 -223.716 54.158 59.057 1.00 81.61 C
ANISOU 284 CH2 TRP A 35 10625 9459 10926 -1125 -46 -991 C
ATOM 285 N GLN A 36 -219.903 53.933 55.773 1.00 79.29 N
ANISOU 285 N GLN A 36 10137 9182 10807 -918 -451 -457 N
ATOM 286 CA GLN A 36 -220.990 53.423 54.946 1.00 71.12 C
ANISOU 286 CA GLN A 36 9074 8105 9842 -777 -407 -416 C
ATOM 287 C GLN A 36 -220.447 52.715 53.716 1.00 64.59 C
ANISOU 287 C GLN A 36 8192 7301 9048 -671 -480 -250 C
ATOM 288 O GLN A 36 -221.030 51.729 53.254 1.00 64.44 O
ANISOU 288 O GLN A 36 8161 7313 9009 -586 -487 -188 O
ATOM 289 CB GLN A 36 -221.933 54.561 54.562 1.00 65.47 C
ANISOU 289 CB GLN A 36 8348 7236 9293 -726 -307 -507 C
ATOM 290 CG GLN A 36 -222.737 55.067 55.748 1.00 79.78 C
ANISOU 290 CG GLN A 36 10207 9018 11086 -813 -197 -692 C
ATOM 291 CD GLN A 36 -223.386 56.404 55.489 1.00 85.50 C
ANISOU 291 CD GLN A 36 10910 9566 12010 -779 -100 -795 C
ATOM 292 OE1 GLN A 36 -222.748 57.330 54.985 1.00 74.17 O
ANISOU 292 OE1 GLN A 36 9461 8042 10677 -780 -123 -770 O
ATOM 293 NE2 GLN A 36 -224.664 56.514 55.830 1.00106.89 N
ANISOU 293 NE2 GLN A 36 13607 12213 14794 -749 13 -908 N
ATOM 294 N PHE A 37 -219.328 53.198 53.172 1.00 56.15 N
ANISOU 294 N PHE A 37 7090 6216 8028 -683 -524 -185 N
ATOM 295 CA PHE A 37 -218.664 52.440 52.118 1.00 69.76 C
ANISOU 295 CA PHE A 37 8764 7977 9765 -605 -575 -43 C
ATOM 296 C PHE A 37 -218.152 51.115 52.662 1.00 72.33 C
ANISOU 296 C PHE A 37 9076 8425 9980 -624 -646 16 C
ATOM 297 O PHE A 37 -218.240 50.081 51.988 1.00 62.75 O
ANISOU 297 O PHE A 37 7840 7241 8760 -537 -661 101 O
ATOM 298 CB PHE A 37 -217.517 53.244 51.506 1.00 49.54 C
ANISOU 298 CB PHE A 37 6164 5377 7281 -632 -591 6 C
ATOM 299 CG PHE A 37 -217.953 54.263 50.492 1.00 67.91 C
ANISOU 299 CG PHE A 37 8497 7575 9729 -580 -538 14 C
ATOM 300 CD1 PHE A 37 -218.286 55.553 50.881 1.00 67.52 C
ANISOU 300 CD1 PHE A 37 8475 7421 9760 -631 -494 -83 C
ATOM 301 CD2 PHE A 37 -218.008 53.938 49.143 1.00 71.83 C
ANISOU 301 CD2 PHE A 37 8980 8052 10261 -490 -533 121 C
ATOM 302 CE1 PHE A 37 -218.679 56.497 49.947 1.00 70.73 C
ANISOU 302 CE1 PHE A 37 8884 7695 10296 -582 -461 -56 C
ATOM 303 CE2 PHE A 37 -218.401 54.883 48.199 1.00 67.41 C
ANISOU 303 CE2 PHE A 37 8436 7375 9802 -456 -505 151 C
ATOM 304 CZ PHE A 37 -218.736 56.161 48.603 1.00 66.80 C
ANISOU 304 CZ PHE A 37 8376 7185 9821 -497 -476 72 C
ATOM 305 N SER A 38 -217.638 51.125 53.896 1.00 61.77 N
ANISOU 305 N SER A 38 7759 7155 8555 -743 -697 -26 N
ATOM 306 CA SER A 38 -217.182 49.891 54.523 1.00 69.54 C
ANISOU 306 CA SER A 38 8734 8248 9441 -771 -785 45 C
ATOM 307 C SER A 38 -218.335 48.921 54.726 1.00 75.95 C
ANISOU 307 C SER A 38 9589 9084 10183 -723 -756 38 C
ATOM 308 O SER A 38 -218.168 47.706 54.560 1.00 72.70 O
ANISOU 308 O SER A 38 9154 8723 9748 -673 -807 133 O
ATOM 309 CB SER A 38 -216.505 50.195 55.857 1.00 47.07 C
ANISOU 309 CB SER A 38 5917 5469 6497 -933 -860 4 C
ATOM 310 OG SER A 38 -215.432 51.090 55.676 1.00 78.83 O
ANISOU 310 OG SER A 38 9891 9467 10592 -986 -891 10 O
ATOM 311 N MET A 39 -219.510 49.439 55.100 1.00 72.31 N
ANISOU 311 N MET A 39 9186 8582 9706 -740 -667 -78 N
ATOM 312 CA MET A 39 -220.681 48.580 55.239 1.00 71.66 C
ANISOU 312 CA MET A 39 9134 8517 9577 -697 -626 -91 C
ATOM 313 C MET A 39 -221.127 48.037 53.890 1.00 69.89 C
ANISOU 313 C MET A 39 8865 8246 9443 -550 -610 -15 C
ATOM 314 O MET A 39 -221.548 46.879 53.794 1.00 61.87 O
ANISOU 314 O MET A 39 7853 7268 8387 -506 -627 38 O
ATOM 315 CB MET A 39 -221.818 49.337 55.917 1.00 55.09 C
ANISOU 315 CB MET A 39 7087 6375 7471 -749 -516 -245 C
ATOM 316 CG MET A 39 -221.619 49.549 57.410 1.00 74.25 C
ANISOU 316 CG MET A 39 9590 8870 9751 -918 -516 -335 C
ATOM 317 SD MET A 39 -221.238 48.024 58.310 1.00 77.73 S
ANISOU 317 SD MET A 39 10075 9453 10005 -996 -626 -231 S
ATOM 318 CE MET A 39 -222.532 46.917 57.741 1.00 83.54 C
ANISOU 318 CE MET A 39 10796 10175 10771 -875 -567 -195 C
ATOM 319 N LEU A 40 -221.047 48.856 52.839 1.00 65.61 N
ANISOU 319 N LEU A 40 8291 7621 9017 -485 -583 -5 N
ATOM 320 CA LEU A 40 -221.245 48.332 51.492 1.00 67.48 C
ANISOU 320 CA LEU A 40 8498 7828 9312 -370 -585 81 C
ATOM 321 C LEU A 40 -220.280 47.190 51.216 1.00 80.33 C
ANISOU 321 C LEU A 40 10098 9523 10903 -347 -646 184 C
ATOM 322 O LEU A 40 -220.665 46.156 50.655 1.00 69.81 O
ANISOU 322 O LEU A 40 8764 8201 9559 -278 -649 234 O
ATOM 323 CB LEU A 40 -221.060 49.442 50.459 1.00 55.68 C
ANISOU 323 CB LEU A 40 6986 6243 7926 -333 -561 95 C
ATOM 324 CG LEU A 40 -221.083 48.966 49.004 1.00 66.06 C
ANISOU 324 CG LEU A 40 8289 7538 9273 -242 -568 190 C
ATOM 325 CD1 LEU A 40 -222.414 48.297 48.690 1.00 68.47 C
ANISOU 325 CD1 LEU A 40 8611 7833 9573 -179 -557 185 C
ATOM 326 CD2 LEU A 40 -220.808 50.116 48.046 1.00 81.07 C
ANISOU 326 CD2 LEU A 40 10186 9355 11261 -231 -552 219 C
ATOM 327 N ALA A 41 -219.018 47.361 51.617 1.00 68.54 N
ANISOU 327 N ALA A 41 8572 8066 9403 -407 -696 214 N
ATOM 328 CA ALA A 41 -218.029 46.304 51.457 1.00 54.95 C
ANISOU 328 CA ALA A 41 6801 6396 7683 -385 -755 311 C
ATOM 329 C ALA A 41 -218.402 45.072 52.270 1.00 67.10 C
ANISOU 329 C ALA A 41 8363 7993 9141 -396 -802 336 C
ATOM 330 O ALA A 41 -218.268 43.942 51.790 1.00 59.88 O
ANISOU 330 O ALA A 41 7422 7084 8245 -328 -817 407 O
ATOM 331 CB ALA A 41 -216.652 46.820 51.870 1.00 57.37 C
ANISOU 331 CB ALA A 41 7052 6729 8019 -459 -811 337 C
ATOM 332 N ALA A 42 -218.874 45.272 53.503 1.00 56.92 N
ANISOU 332 N ALA A 42 7129 6742 7757 -490 -817 276 N
ATOM 333 CA ALA A 42 -219.267 44.139 54.332 1.00 53.37 C
ANISOU 333 CA ALA A 42 6716 6348 7214 -522 -861 308 C
ATOM 334 C ALA A 42 -220.450 43.397 53.727 1.00 61.01 C
ANISOU 334 C ALA A 42 7705 7285 8190 -435 -800 302 C
ATOM 335 O ALA A 42 -220.524 42.165 53.801 1.00 82.81 O
ANISOU 335 O ALA A 42 10468 10067 10928 -410 -838 371 O
ATOM 336 CB ALA A 42 -219.599 44.612 55.747 1.00 45.37 C
ANISOU 336 CB ALA A 42 5777 5386 6077 -663 -868 230 C
ATOM 337 N TYR A 43 -221.383 44.128 53.119 1.00 59.94 N
ANISOU 337 N TYR A 43 7582 7092 8099 -392 -716 227 N
ATOM 338 CA TYR A 43 -222.531 43.484 52.494 1.00 73.57 C
ANISOU 338 CA TYR A 43 9319 8789 9844 -318 -671 223 C
ATOM 339 C TYR A 43 -222.097 42.653 51.292 1.00 70.31 C
ANISOU 339 C TYR A 43 8874 8356 9485 -223 -692 309 C
ATOM 340 O TYR A 43 -222.594 41.540 51.084 1.00 62.30 O
ANISOU 340 O TYR A 43 7871 7344 8455 -185 -696 341 O
ATOM 341 CB TYR A 43 -223.562 44.545 52.101 1.00 62.72 C
ANISOU 341 CB TYR A 43 7948 7350 8533 -295 -596 136 C
ATOM 342 CG TYR A 43 -224.811 44.000 51.465 1.00 73.66 C
ANISOU 342 CG TYR A 43 9331 8704 9951 -227 -564 131 C
ATOM 343 CD1 TYR A 43 -225.538 42.991 52.076 1.00 77.40 C
ANISOU 343 CD1 TYR A 43 9827 9217 10364 -251 -557 126 C
ATOM 344 CD2 TYR A 43 -225.278 44.511 50.261 1.00 84.51 C
ANISOU 344 CD2 TYR A 43 10683 10011 11417 -153 -551 140 C
ATOM 345 CE1 TYR A 43 -226.690 42.491 51.498 1.00 72.66 C
ANISOU 345 CE1 TYR A 43 9216 8588 9802 -198 -533 121 C
ATOM 346 CE2 TYR A 43 -226.430 44.019 49.674 1.00 92.06 C
ANISOU 346 CE2 TYR A 43 11632 10942 12406 -102 -543 142 C
ATOM 347 CZ TYR A 43 -227.130 43.009 50.298 1.00 86.02 C
ANISOU 347 CZ TYR A 43 10878 10216 11589 -124 -531 127 C
ATOM 348 OH TYR A 43 -228.274 42.518 49.719 1.00110.51 O
ANISOU 348 OH TYR A 43 13965 13293 14732 -82 -528 128 O
ATOM 349 N MET A 44 -221.165 43.179 50.491 1.00 64.70 N
ANISOU 349 N MET A 44 8126 7621 8837 -193 -694 340 N
ATOM 350 CA MET A 44 -220.611 42.401 49.386 1.00 66.64 C
ANISOU 350 CA MET A 44 8344 7849 9126 -119 -691 406 C
ATOM 351 C MET A 44 -219.885 41.165 49.900 1.00 71.60 C
ANISOU 351 C MET A 44 8943 8511 9750 -119 -745 472 C
ATOM 352 O MET A 44 -219.944 40.095 49.283 1.00 68.86 O
ANISOU 352 O MET A 44 8593 8144 9427 -59 -734 507 O
ATOM 353 CB MET A 44 -219.657 43.260 48.550 1.00 61.45 C
ANISOU 353 CB MET A 44 7651 7165 8531 -108 -668 422 C
ATOM 354 CG MET A 44 -220.281 44.476 47.884 1.00 67.76 C
ANISOU 354 CG MET A 44 8479 7913 9354 -103 -627 383 C
ATOM 355 SD MET A 44 -221.523 44.047 46.663 1.00 80.21 S
ANISOU 355 SD MET A 44 10102 9450 10924 -35 -600 388 S
ATOM 356 CE MET A 44 -223.015 44.452 47.570 1.00 73.51 C
ANISOU 356 CE MET A 44 9272 8587 10071 -55 -602 315 C
ATOM 357 N PHE A 45 -219.181 41.295 51.022 1.00 73.85 N
ANISOU 357 N PHE A 45 9208 8841 10012 -190 -811 494 N
ATOM 358 CA PHE A 45 -218.481 40.148 51.584 1.00 68.93 C
ANISOU 358 CA PHE A 45 8549 8241 9400 -194 -887 579 C
ATOM 359 C PHE A 45 -219.469 39.087 52.052 1.00 70.52 C
ANISOU 359 C PHE A 45 8808 8449 9538 -196 -899 590 C
ATOM 360 O PHE A 45 -219.235 37.888 51.867 1.00 68.76 O
ANISOU 360 O PHE A 45 8563 8203 9360 -148 -925 657 O
ATOM 361 CB PHE A 45 -217.580 40.611 52.727 1.00 58.33 C
ANISOU 361 CB PHE A 45 7180 6952 8033 -292 -979 609 C
ATOM 362 CG PHE A 45 -216.791 39.509 53.374 1.00 63.08 C
ANISOU 362 CG PHE A 45 7734 7573 8661 -304 -1090 720 C
ATOM 363 CD1 PHE A 45 -215.793 38.848 52.676 1.00 55.27 C
ANISOU 363 CD1 PHE A 45 6642 6542 7814 -222 -1101 793 C
ATOM 364 CD2 PHE A 45 -217.025 39.161 54.695 1.00 68.97 C
ANISOU 364 CD2 PHE A 45 8535 8374 9295 -404 -1180 755 C
ATOM 365 CE1 PHE A 45 -215.057 37.839 53.277 1.00 55.39 C
ANISOU 365 CE1 PHE A 45 6596 6557 7891 -224 -1213 906 C
ATOM 366 CE2 PHE A 45 -216.294 38.159 55.305 1.00 68.87 C
ANISOU 366 CE2 PHE A 45 8479 8372 9315 -420 -1306 881 C
ATOM 367 CZ PHE A 45 -215.309 37.494 54.597 1.00 53.70 C
ANISOU 367 CZ PHE A 45 6441 6397 7567 -323 -1329 961 C
ATOM 368 N LEU A 46 -220.586 39.514 52.647 1.00 68.62 N
ANISOU 368 N LEU A 46 8636 8231 9207 -253 -869 520 N
ATOM 369 CA LEU A 46 -221.644 38.579 53.015 1.00 65.66 C
ANISOU 369 CA LEU A 46 8313 7860 8774 -262 -859 521 C
ATOM 370 C LEU A 46 -222.172 37.835 51.794 1.00 71.63 C
ANISOU 370 C LEU A 46 9063 8559 9593 -161 -811 525 C
ATOM 371 O LEU A 46 -222.335 36.610 51.823 1.00 67.85 O
ANISOU 371 O LEU A 46 8595 8065 9121 -141 -833 576 O
ATOM 372 CB LEU A 46 -222.782 39.325 53.714 1.00 63.51 C
ANISOU 372 CB LEU A 46 8098 7613 8419 -335 -802 423 C
ATOM 373 CG LEU A 46 -223.935 38.419 54.151 1.00 61.12 C
ANISOU 373 CG LEU A 46 7844 7321 8058 -360 -777 417 C
ATOM 374 CD1 LEU A 46 -223.424 37.396 55.133 1.00 56.80 C
ANISOU 374 CD1 LEU A 46 7325 6814 7441 -427 -864 513 C
ATOM 375 CD2 LEU A 46 -225.069 39.213 54.767 1.00 64.53 C
ANISOU 375 CD2 LEU A 46 8312 7769 8438 -427 -693 303 C
ATOM 376 N LEU A 47 -222.453 38.563 50.711 1.00 70.30 N
ANISOU 376 N LEU A 47 8885 8356 9468 -108 -751 474 N
ATOM 377 CA LEU A 47 -222.995 37.933 49.512 1.00 61.23 C
ANISOU 377 CA LEU A 47 7747 7162 8357 -35 -713 471 C
ATOM 378 C LEU A 47 -221.996 36.979 48.868 1.00 74.22 C
ANISOU 378 C LEU A 47 9361 8776 10064 21 -720 530 C
ATOM 379 O LEU A 47 -222.401 35.962 48.297 1.00 73.76 O
ANISOU 379 O LEU A 47 9323 8682 10020 60 -702 535 O
ATOM 380 CB LEU A 47 -223.430 39.002 48.509 1.00 63.06 C
ANISOU 380 CB LEU A 47 7983 7365 8610 -7 -668 421 C
ATOM 381 CG LEU A 47 -224.590 39.892 48.964 1.00 71.29 C
ANISOU 381 CG LEU A 47 9040 8409 9637 -42 -648 355 C
ATOM 382 CD1 LEU A 47 -224.854 40.995 47.959 1.00 67.40 C
ANISOU 382 CD1 LEU A 47 8542 7874 9194 -11 -626 333 C
ATOM 383 CD2 LEU A 47 -225.835 39.054 49.160 1.00 61.82 C
ANISOU 383 CD2 LEU A 47 7863 7211 8416 -46 -639 337 C
ATOM 384 N ILE A 48 -220.698 37.285 48.942 1.00 72.43 N
ANISOU 384 N ILE A 48 9077 8555 9888 23 -740 567 N
ATOM 385 CA ILE A 48 -219.695 36.397 48.360 1.00 67.52 C
ANISOU 385 CA ILE A 48 8402 7894 9359 81 -730 614 C
ATOM 386 C ILE A 48 -219.554 35.130 49.195 1.00 73.27 C
ANISOU 386 C ILE A 48 9117 8609 10112 79 -796 683 C
ATOM 387 O ILE A 48 -219.484 34.019 48.656 1.00 65.34 O
ANISOU 387 O ILE A 48 8106 7546 9174 135 -771 700 O
ATOM 388 CB ILE A 48 -218.347 37.127 48.210 1.00 75.52 C
ANISOU 388 CB ILE A 48 9336 8914 10444 81 -728 635 C
ATOM 389 CG1 ILE A 48 -218.477 38.305 47.243 1.00 74.88 C
ANISOU 389 CG1 ILE A 48 9279 8831 10343 81 -657 579 C
ATOM 390 CG2 ILE A 48 -217.268 36.161 47.726 1.00 59.27 C
ANISOU 390 CG2 ILE A 48 7200 6807 8514 143 -707 680 C
ATOM 391 CD1 ILE A 48 -217.299 39.252 47.266 1.00 71.35 C
ANISOU 391 CD1 ILE A 48 8762 8398 9951 56 -657 594 C
ATOM 392 N MET A 49 -219.517 35.274 50.522 1.00 72.87 N
ANISOU 392 N MET A 49 9071 8608 10007 6 -882 725 N
ATOM 393 CA MET A 49 -219.332 34.116 51.390 1.00 68.21 C
ANISOU 393 CA MET A 49 8476 8006 9433 -11 -966 816 C
ATOM 394 C MET A 49 -220.531 33.176 51.359 1.00 74.15 C
ANISOU 394 C MET A 49 9301 8731 10140 -8 -941 804 C
ATOM 395 O MET A 49 -220.363 31.963 51.514 1.00 72.49 O
ANISOU 395 O MET A 49 9082 8469 9992 16 -979 874 O
ATOM 396 CB MET A 49 -219.049 34.574 52.821 1.00 68.08 C
ANISOU 396 CB MET A 49 8470 8063 9333 -118 -1070 866 C
ATOM 397 CG MET A 49 -217.739 35.336 53.002 1.00 78.32 C
ANISOU 397 CG MET A 49 9683 9386 10689 -136 -1125 898 C
ATOM 398 SD MET A 49 -216.240 34.346 52.774 1.00 85.07 S
ANISOU 398 SD MET A 49 10401 10176 11747 -60 -1197 1020 S
ATOM 399 CE MET A 49 -215.921 34.570 51.021 1.00 77.88 C
ANISOU 399 CE MET A 49 9434 9199 10958 57 -1038 933 C
ATOM 400 N LEU A 50 -221.740 33.703 51.173 1.00 74.46 N
ANISOU 400 N LEU A 50 9404 8796 10092 -33 -881 719 N
ATOM 401 CA LEU A 50 -222.920 32.857 51.046 1.00 68.23 C
ANISOU 401 CA LEU A 50 8672 7981 9272 -34 -852 700 C
ATOM 402 C LEU A 50 -223.222 32.485 49.603 1.00 79.28 C
ANISOU 402 C LEU A 50 10075 9319 10730 45 -781 649 C
ATOM 403 O LEU A 50 -223.804 31.426 49.351 1.00 95.15 O
ANISOU 403 O LEU A 50 12116 11282 12756 58 -770 653 O
ATOM 404 CB LEU A 50 -224.146 33.550 51.647 1.00 63.20 C
ANISOU 404 CB LEU A 50 8085 7399 8529 -107 -823 634 C
ATOM 405 CG LEU A 50 -224.089 33.891 53.137 1.00 77.03 C
ANISOU 405 CG LEU A 50 9864 9220 10184 -215 -870 659 C
ATOM 406 CD1 LEU A 50 -225.388 34.542 53.596 1.00 56.48 C
ANISOU 406 CD1 LEU A 50 7304 6658 7499 -281 -802 566 C
ATOM 407 CD2 LEU A 50 -223.783 32.660 53.970 1.00 67.32 C
ANISOU 407 CD2 LEU A 50 8657 7984 8939 -257 -951 770 C
ATOM 408 N GLY A 51 -222.835 33.324 48.649 1.00 77.30 N
ANISOU 408 N GLY A 51 9802 9067 10502 83 -735 603 N
ATOM 409 CA GLY A 51 -223.234 33.124 47.272 1.00 63.26 C
ANISOU 409 CA GLY A 51 8051 7246 8739 129 -670 550 C
ATOM 410 C GLY A 51 -222.362 32.167 46.495 1.00 69.76 C
ANISOU 410 C GLY A 51 8853 8001 9652 188 -632 562 C
ATOM 411 O GLY A 51 -222.876 31.336 45.742 1.00 87.99 O
ANISOU 411 O GLY A 51 11206 10261 11966 206 -594 528 O
ATOM 412 N PHE A 52 -221.045 32.273 46.650 1.00 77.33 N
ANISOU 412 N PHE A 52 9739 8951 10692 215 -636 603 N
ATOM 413 CA PHE A 52 -220.164 31.356 45.932 1.00 80.47 C
ANISOU 413 CA PHE A 52 10097 9270 11208 277 -579 604 C
ATOM 414 C PHE A 52 -220.338 29.907 46.367 1.00 71.59 C
ANISOU 414 C PHE A 52 8976 8073 10152 296 -610 646 C
ATOM 415 O PHE A 52 -220.507 29.044 45.489 1.00 72.80 O
ANISOU 415 O PHE A 52 9160 8152 10347 330 -538 596 O
ATOM 416 CB PHE A 52 -218.703 31.790 46.074 1.00 66.88 C
ANISOU 416 CB PHE A 52 8270 7550 9591 302 -579 645 C
ATOM 417 CG PHE A 52 -217.736 30.780 45.542 1.00 76.51 C
ANISOU 417 CG PHE A 52 9420 8677 10974 371 -517 650 C
ATOM 418 CD1 PHE A 52 -217.614 30.578 44.180 1.00 80.95 C
ANISOU 418 CD1 PHE A 52 10009 9193 11555 401 -382 561 C
ATOM 419 CD2 PHE A 52 -216.970 30.013 46.400 1.00 81.10 C
ANISOU 419 CD2 PHE A 52 9909 9210 11695 400 -593 742 C
ATOM 420 CE1 PHE A 52 -216.729 29.643 43.679 1.00 82.23 C
ANISOU 420 CE1 PHE A 52 10102 9259 11882 464 -298 544 C
ATOM 421 CE2 PHE A 52 -216.082 29.075 45.905 1.00 78.03 C
ANISOU 421 CE2 PHE A 52 9437 8715 11496 475 -528 743 C
ATOM 422 CZ PHE A 52 -215.963 28.891 44.543 1.00 79.91 C
ANISOU 422 CZ PHE A 52 9698 8904 11762 509 -368 633 C
ATOM 423 N PRO A 53 -220.297 29.560 47.659 1.00 68.96 N
ANISOU 423 N PRO A 53 8622 7752 9829 267 -712 737 N
ATOM 424 CA PRO A 53 -220.457 28.139 48.017 1.00 81.60 C
ANISOU 424 CA PRO A 53 10231 9268 11505 283 -745 791 C
ATOM 425 C PRO A 53 -221.753 27.543 47.499 1.00 79.41 C
ANISOU 425 C PRO A 53 10049 8963 11159 264 -698 725 C
ATOM 426 O PRO A 53 -221.722 26.537 46.783 1.00 88.92 O
ANISOU 426 O PRO A 53 11266 10071 12450 307 -641 693 O
ATOM 427 CB PRO A 53 -220.406 28.157 49.553 1.00 71.12 C
ANISOU 427 CB PRO A 53 8895 7989 10137 219 -875 905 C
ATOM 428 CG PRO A 53 -219.720 29.395 49.897 1.00 72.72 C
ANISOU 428 CG PRO A 53 9048 8275 10305 194 -906 913 C
ATOM 429 CD PRO A 53 -220.120 30.394 48.857 1.00 72.15 C
ANISOU 429 CD PRO A 53 9006 8241 10167 205 -805 796 C
ATOM 430 N ILE A 54 -222.892 28.164 47.812 1.00 75.80 N
ANISOU 430 N ILE A 54 9653 8586 10563 199 -715 696 N
ATOM 431 CA ILE A 54 -224.186 27.605 47.430 1.00 79.50 C
ANISOU 431 CA ILE A 54 10196 9035 10978 171 -688 643 C
ATOM 432 C ILE A 54 -224.253 27.369 45.926 1.00 78.39 C
ANISOU 432 C ILE A 54 10085 8842 10858 210 -602 550 C
ATOM 433 O ILE A 54 -224.713 26.318 45.468 1.00 89.50 O
ANISOU 433 O ILE A 54 11535 10174 12296 211 -575 520 O
ATOM 434 CB ILE A 54 -225.325 28.523 47.910 1.00 71.26 C
ANISOU 434 CB ILE A 54 9183 8085 9808 102 -707 615 C
ATOM 435 CG1 ILE A 54 -225.279 28.680 49.429 1.00 72.46 C
ANISOU 435 CG1 ILE A 54 9326 8290 9915 40 -774 691 C
ATOM 436 CG2 ILE A 54 -226.667 27.958 47.501 1.00 87.96 C
ANISOU 436 CG2 ILE A 54 11352 10180 11888 70 -686 564 C
ATOM 437 CD1 ILE A 54 -226.410 29.518 49.980 1.00 80.30 C
ANISOU 437 CD1 ILE A 54 10345 9364 10801 -31 -765 646 C
ATOM 438 N ASN A 55 -223.784 28.330 45.134 1.00 75.11 N
ANISOU 438 N ASN A 55 9657 8463 10420 231 -556 503 N
ATOM 439 CA ASN A 55 -223.894 28.191 43.686 1.00 72.56 C
ANISOU 439 CA ASN A 55 9384 8106 10078 242 -474 415 C
ATOM 440 C ASN A 55 -222.827 27.262 43.124 1.00 73.38 C
ANISOU 440 C ASN A 55 9463 8111 10307 298 -394 394 C
ATOM 441 O ASN A 55 -223.087 26.521 42.169 1.00 90.89 O
ANISOU 441 O ASN A 55 11743 10266 12525 295 -324 317 O
ATOM 442 CB ASN A 55 -223.818 29.564 43.020 1.00 61.52 C
ANISOU 442 CB ASN A 55 7994 6780 8601 230 -453 383 C
ATOM 443 CG ASN A 55 -224.985 30.452 43.399 1.00 79.17 C
ANISOU 443 CG ASN A 55 10248 9088 10743 182 -518 388 C
ATOM 444 OD1 ASN A 55 -226.097 30.266 42.911 1.00 74.36 O
ANISOU 444 OD1 ASN A 55 9693 8480 10080 149 -532 352 O
ATOM 445 ND2 ASN A 55 -224.738 31.423 44.269 1.00 81.67 N
ANISOU 445 ND2 ASN A 55 10516 9461 11054 176 -556 427 N
ATOM 446 N PHE A 56 -221.617 27.296 43.682 1.00 71.15 N
ANISOU 446 N PHE A 56 9086 7808 10138 346 -400 454 N
ATOM 447 CA PHE A 56 -220.592 26.379 43.205 1.00 80.61 C
ANISOU 447 CA PHE A 56 10234 8895 11497 409 -316 433 C
ATOM 448 C PHE A 56 -220.902 24.954 43.635 1.00 85.71 C
ANISOU 448 C PHE A 56 10892 9434 12241 425 -342 462 C
ATOM 449 O PHE A 56 -220.678 24.006 42.873 1.00 85.18 O
ANISOU 449 O PHE A 56 10841 9256 12269 457 -247 392 O
ATOM 450 CB PHE A 56 -219.210 26.794 43.706 1.00 66.01 C
ANISOU 450 CB PHE A 56 8257 7049 9776 457 -329 500 C
ATOM 451 CG PHE A 56 -218.139 25.817 43.344 1.00 70.67 C
ANISOU 451 CG PHE A 56 8764 7510 10578 532 -245 487 C
ATOM 452 CD1 PHE A 56 -217.513 25.889 42.111 1.00 65.00 C
ANISOU 452 CD1 PHE A 56 8039 6757 9902 556 -85 379 C
ATOM 453 CD2 PHE A 56 -217.788 24.797 44.215 1.00 74.88 C
ANISOU 453 CD2 PHE A 56 9227 7948 11276 575 -320 581 C
ATOM 454 CE1 PHE A 56 -216.540 24.977 41.761 1.00 77.57 C
ANISOU 454 CE1 PHE A 56 9543 8217 11712 628 17 348 C
ATOM 455 CE2 PHE A 56 -216.819 23.880 43.873 1.00 76.02 C
ANISOU 455 CE2 PHE A 56 9278 7952 11653 655 -241 568 C
ATOM 456 CZ PHE A 56 -216.192 23.969 42.644 1.00 85.62 C
ANISOU 456 CZ PHE A 56 10476 9130 12926 686 -62 442 C
ATOM 457 N LEU A 57 -221.407 24.784 44.858 1.00 76.71 N
ANISOU 457 N LEU A 57 9750 8319 11079 394 -463 562 N
ATOM 458 CA LEU A 57 -221.794 23.457 45.316 1.00 66.35 C
ANISOU 458 CA LEU A 57 8460 6903 9847 394 -498 605 C
ATOM 459 C LEU A 57 -222.902 22.880 44.448 1.00 79.42 C
ANISOU 459 C LEU A 57 10223 8523 11432 356 -436 500 C
ATOM 460 O LEU A 57 -222.953 21.665 44.235 1.00 84.67 O
ANISOU 460 O LEU A 57 10909 9060 12202 373 -403 482 O
ATOM 461 CB LEU A 57 -222.232 23.513 46.779 1.00 69.39 C
ANISOU 461 CB LEU A 57 8844 7345 10176 340 -633 731 C
ATOM 462 CG LEU A 57 -222.402 22.181 47.500 1.00103.57 C
ANISOU 462 CG LEU A 57 13183 11565 14604 334 -694 823 C
ATOM 463 CD1 LEU A 57 -221.054 21.497 47.629 1.00107.37 C
ANISOU 463 CD1 LEU A 57 13561 11924 15312 420 -708 897 C
ATOM 464 CD2 LEU A 57 -223.032 22.403 48.863 1.00115.31 C
ANISOU 464 CD2 LEU A 57 14701 13138 15972 246 -810 930 C
ATOM 465 N THR A 58 -223.793 23.731 43.939 1.00 78.09 N
ANISOU 465 N THR A 58 10119 8458 11096 301 -428 434 N
ATOM 466 CA THR A 58 -224.812 23.261 43.007 1.00 83.66 C
ANISOU 466 CA THR A 58 10921 9138 11729 254 -385 335 C
ATOM 467 C THR A 58 -224.181 22.671 41.752 1.00 84.58 C
ANISOU 467 C THR A 58 11067 9158 11910 285 -258 227 C
ATOM 468 O THR A 58 -224.609 21.618 41.270 1.00 92.76 O
ANISOU 468 O THR A 58 12166 10099 12979 265 -216 162 O
ATOM 469 CB THR A 58 -225.762 24.399 42.636 1.00 69.25 C
ANISOU 469 CB THR A 58 9139 7438 9736 195 -415 299 C
ATOM 470 OG1 THR A 58 -226.602 24.708 43.753 1.00 74.18 O
ANISOU 470 OG1 THR A 58 9747 8128 10310 153 -505 369 O
ATOM 471 CG2 THR A 58 -226.621 23.992 41.455 1.00 69.84 C
ANISOU 471 CG2 THR A 58 9310 7490 9737 142 -377 196 C
ATOM 472 N LEU A 59 -223.166 23.341 41.200 1.00 86.06 N
ANISOU 472 N LEU A 59 11215 9369 12117 325 -185 196 N
ATOM 473 CA LEU A 59 -222.467 22.792 40.046 1.00 81.21 C
ANISOU 473 CA LEU A 59 10624 8663 11568 348 -36 82 C
ATOM 474 C LEU A 59 -221.666 21.553 40.419 1.00 84.76 C
ANISOU 474 C LEU A 59 11002 8953 12251 423 9 99 C
ATOM 475 O LEU A 59 -221.560 20.617 39.620 1.00 78.92 O
ANISOU 475 O LEU A 59 10309 8094 11582 427 124 -10 O
ATOM 476 CB LEU A 59 -221.549 23.847 39.434 1.00 80.31 C
ANISOU 476 CB LEU A 59 10474 8615 11423 364 41 52 C
ATOM 477 CG LEU A 59 -222.214 25.149 38.986 1.00 80.41 C
ANISOU 477 CG LEU A 59 10553 8770 11229 295 -2 46 C
ATOM 478 CD1 LEU A 59 -221.190 26.081 38.363 1.00 67.68 C
ANISOU 478 CD1 LEU A 59 8908 7202 9604 306 88 22 C
ATOM 479 CD2 LEU A 59 -223.338 24.843 38.013 1.00 91.38 C
ANISOU 479 CD2 LEU A 59 12083 10166 12471 211 7 -43 C
ATOM 480 N TYR A 60 -221.102 21.525 41.626 1.00 82.15 N
ANISOU 480 N TYR A 60 10560 8609 12045 477 -85 235 N
ATOM 481 CA TYR A 60 -220.235 20.420 42.011 1.00 88.25 C
ANISOU 481 CA TYR A 60 11242 9219 13069 557 -64 278 C
ATOM 482 C TYR A 60 -221.035 19.155 42.294 1.00 97.11 C
ANISOU 482 C TYR A 60 12428 10225 14243 536 -99 289 C
ATOM 483 O TYR A 60 -220.681 18.068 41.823 1.00100.96 O
ANISOU 483 O TYR A 60 12911 10547 14900 578 -3 223 O
ATOM 484 CB TYR A 60 -219.405 20.809 43.230 1.00 74.55 C
ANISOU 484 CB TYR A 60 9374 7513 11440 604 -184 441 C
ATOM 485 CG TYR A 60 -218.373 19.774 43.591 1.00 80.53 C
ANISOU 485 CG TYR A 60 10010 8098 12488 697 -178 505 C
ATOM 486 CD1 TYR A 60 -217.270 19.562 42.777 1.00 89.91 C
ANISOU 486 CD1 TYR A 60 11109 9188 13863 774 -27 418 C
ATOM 487 CD2 TYR A 60 -218.502 19.005 44.739 1.00 86.78 C
ANISOU 487 CD2 TYR A 60 10774 8820 13379 703 -321 656 C
ATOM 488 CE1 TYR A 60 -216.322 18.616 43.095 1.00104.05 C
ANISOU 488 CE1 TYR A 60 12767 10806 15961 869 -21 477 C
ATOM 489 CE2 TYR A 60 -217.560 18.059 45.067 1.00 99.21 C
ANISOU 489 CE2 TYR A 60 12229 10222 15243 792 -334 734 C
ATOM 490 CZ TYR A 60 -216.471 17.867 44.242 1.00113.94 C
ANISOU 490 CZ TYR A 60 13989 11983 17321 882 -185 642 C
ATOM 491 OH TYR A 60 -215.527 16.919 44.566 1.00129.13 O
ANISOU 491 OH TYR A 60 15772 13719 19574 981 -198 721 O
ATOM 492 N VAL A 61 -222.113 19.280 43.069 1.00 95.72 N
ANISOU 492 N VAL A 61 12309 10129 13932 467 -225 367 N
ATOM 493 CA VAL A 61 -222.939 18.127 43.412 1.00 85.69 C
ANISOU 493 CA VAL A 61 11100 8758 12700 430 -265 390 C
ATOM 494 C VAL A 61 -223.561 17.511 42.166 1.00 92.39 C
ANISOU 494 C VAL A 61 12058 9538 13509 389 -149 221 C
ATOM 495 O VAL A 61 -223.718 16.287 42.082 1.00101.93 O
ANISOU 495 O VAL A 61 13297 10589 14844 392 -117 195 O
ATOM 496 CB VAL A 61 -223.997 18.549 44.451 1.00 80.72 C
ANISOU 496 CB VAL A 61 10506 8250 11913 349 -402 492 C
ATOM 497 CG1 VAL A 61 -225.082 17.521 44.567 1.00 94.39 C
ANISOU 497 CG1 VAL A 61 12320 9906 13638 284 -422 485 C
ATOM 498 CG2 VAL A 61 -223.335 18.754 45.808 1.00 92.81 C
ANISOU 498 CG2 VAL A 61 11948 9806 13508 373 -521 667 C
ATOM 499 N THR A 62 -223.897 18.333 41.169 1.00 88.88 N
ANISOU 499 N THR A 62 11678 9202 12890 343 -88 107 N
ATOM 500 CA THR A 62 -224.433 17.800 39.920 1.00 91.95 C
ANISOU 500 CA THR A 62 12184 9538 13216 284 14 -57 C
ATOM 501 C THR A 62 -223.425 16.893 39.216 1.00 88.71 C
ANISOU 501 C THR A 62 11759 8954 12995 346 175 -163 C
ATOM 502 O THR A 62 -223.819 15.943 38.529 1.00 92.90 O
ANISOU 502 O THR A 62 12379 9371 13548 304 254 -282 O
ATOM 503 CB THR A 62 -224.864 18.957 39.013 1.00 80.29 C
ANISOU 503 CB THR A 62 10776 8218 11513 217 29 -133 C
ATOM 504 OG1 THR A 62 -225.768 19.803 39.732 1.00108.58 O
ANISOU 504 OG1 THR A 62 14351 11942 14964 174 -112 -35 O
ATOM 505 CG2 THR A 62 -225.573 18.454 37.765 1.00 68.15 C
ANISOU 505 CG2 THR A 62 9379 6649 9867 125 100 -288 C
ATOM 506 N VAL A 63 -222.126 17.151 39.392 1.00 86.03 N
ANISOU 506 N VAL A 63 11299 8581 12806 443 229 -128 N
ATOM 507 CA VAL A 63 -221.100 16.318 38.770 1.00 78.98 C
ANISOU 507 CA VAL A 63 10363 7512 12134 513 399 -232 C
ATOM 508 C VAL A 63 -220.974 14.968 39.470 1.00 91.74 C
ANISOU 508 C VAL A 63 11927 8926 14004 572 368 -167 C
ATOM 509 O VAL A 63 -220.518 13.991 38.860 1.00 93.01 O
ANISOU 509 O VAL A 63 12089 8902 14348 610 515 -284 O
ATOM 510 CB VAL A 63 -219.754 17.076 38.758 1.00 76.69 C
ANISOU 510 CB VAL A 63 9937 7256 11946 596 463 -207 C
ATOM 511 CG1 VAL A 63 -218.642 16.235 38.160 1.00 62.01 C
ANISOU 511 CG1 VAL A 63 8002 5205 10352 679 655 -318 C
ATOM 512 CG2 VAL A 63 -219.885 18.380 37.983 1.00 67.28 C
ANISOU 512 CG2 VAL A 63 8810 6248 10505 528 503 -273 C
ATOM 513 N GLN A 64 -221.401 14.869 40.725 1.00 90.62 N
ANISOU 513 N GLN A 64 11749 8806 13876 572 187 14 N
ATOM 514 CA GLN A 64 -221.217 13.648 41.493 1.00 90.64 C
ANISOU 514 CA GLN A 64 11700 8617 14123 624 134 114 C
ATOM 515 C GLN A 64 -222.434 12.732 41.507 1.00 92.69 C
ANISOU 515 C GLN A 64 12085 8806 14328 538 101 87 C
ATOM 516 O GLN A 64 -222.314 11.591 41.966 1.00101.83 O
ANISOU 516 O GLN A 64 13217 9772 15700 573 80 149 O
ATOM 517 CB GLN A 64 -220.828 13.985 42.935 1.00 83.82 C
ANISOU 517 CB GLN A 64 10723 7805 13319 663 -51 348 C
ATOM 518 CG GLN A 64 -219.409 14.507 43.080 1.00 98.48 C
ANISOU 518 CG GLN A 64 12419 9661 15338 766 -33 401 C
ATOM 519 CD GLN A 64 -218.921 14.456 44.511 1.00105.96 C
ANISOU 519 CD GLN A 64 13254 10600 16406 804 -225 639 C
ATOM 520 OE1 GLN A 64 -219.707 14.275 45.442 1.00106.38 O
ANISOU 520 OE1 GLN A 64 13368 10694 16359 735 -372 767 O
ATOM 521 NE2 GLN A 64 -217.615 14.607 44.695 1.00111.10 N
ANISOU 521 NE2 GLN A 64 13741 11199 17273 902 -226 702 N
ATOM 522 N HIS A 65 -223.588 13.182 41.013 1.00 63.94 N
ANISOU 522 N HIS A 65 8569 5300 10424 425 91 4 N
ATOM 523 CA HIS A 65 -224.828 12.426 41.151 1.00 71.77 C
ANISOU 523 CA HIS A 65 9665 6250 11354 329 36 -1 C
ATOM 524 C HIS A 65 -225.551 12.365 39.815 1.00 79.93 C
ANISOU 524 C HIS A 65 10834 7305 12231 235 139 -208 C
ATOM 525 O HIS A 65 -226.013 13.392 39.311 1.00 87.04 O
ANISOU 525 O HIS A 65 11781 8387 12905 174 124 -256 O
ATOM 526 CB HIS A 65 -225.713 13.045 42.233 1.00 66.37 C
ANISOU 526 CB HIS A 65 8980 5728 10509 264 -134 154 C
ATOM 527 CG HIS A 65 -225.048 13.116 43.574 1.00 81.55 C
ANISOU 527 CG HIS A 65 10795 7645 12547 328 -248 359 C
ATOM 528 ND1 HIS A 65 -225.335 12.236 44.596 1.00 85.02 N
ANISOU 528 ND1 HIS A 65 11232 7983 13088 307 -346 504 N
ATOM 529 CD2 HIS A 65 -224.097 13.952 44.055 1.00 83.26 C
ANISOU 529 CD2 HIS A 65 10907 7942 12786 398 -288 449 C
ATOM 530 CE1 HIS A 65 -224.595 12.532 45.651 1.00 88.01 C
ANISOU 530 CE1 HIS A 65 11517 8389 13535 357 -449 679 C
ATOM 531 NE2 HIS A 65 -223.835 13.569 45.349 1.00 84.14 N
ANISOU 531 NE2 HIS A 65 10960 8008 13002 413 -418 645 N
ATOM 532 N LYS A 66 -225.653 11.155 39.250 1.00 91.98 N
ANISOU 532 N LYS A 66 12427 8639 13881 215 236 -325 N
ATOM 533 CA LYS A 66 -226.285 10.987 37.943 1.00 93.28 C
ANISOU 533 CA LYS A 66 12735 8812 13896 108 335 -533 C
ATOM 534 C LYS A 66 -227.748 11.395 37.971 1.00 86.39 C
ANISOU 534 C LYS A 66 11946 8097 12783 -25 206 -513 C
ATOM 535 O LYS A 66 -228.269 11.902 36.970 1.00 89.61 O
ANISOU 535 O LYS A 66 12449 8614 12985 -117 229 -634 O
ATOM 536 CB LYS A 66 -226.158 9.535 37.463 1.00107.32 C
ANISOU 536 CB LYS A 66 14571 10337 15869 103 459 -663 C
ATOM 537 CG LYS A 66 -225.010 9.284 36.486 1.00122.23 C
ANISOU 537 CG LYS A 66 16454 12102 17885 166 677 -839 C
ATOM 538 CD LYS A 66 -225.481 8.704 35.145 1.00125.58 C
ANISOU 538 CD LYS A 66 17050 12459 18205 44 821 -1090 C
ATOM 539 CE LYS A 66 -224.339 8.707 34.127 1.00123.82 C
ANISOU 539 CE LYS A 66 16830 12162 18056 89 1060 -1278 C
ATOM 540 NZ LYS A 66 -224.709 8.094 32.824 1.00118.07 N
ANISOU 540 NZ LYS A 66 16283 11360 17220 -44 1220 -1538 N
ATOM 541 N LYS A 67 -228.423 11.189 39.101 1.00 76.75 N
ANISOU 541 N LYS A 67 10686 6887 11587 -43 68 -356 N
ATOM 542 CA LYS A 67 -229.856 11.450 39.153 1.00 96.05 C
ANISOU 542 CA LYS A 67 13191 9458 13846 -169 -40 -345 C
ATOM 543 C LYS A 67 -230.177 12.919 38.912 1.00 95.33 C
ANISOU 543 C LYS A 67 13086 9600 13535 -194 -99 -333 C
ATOM 544 O LYS A 67 -231.284 13.246 38.471 1.00 97.40 O
ANISOU 544 O LYS A 67 13406 9966 13636 -302 -161 -377 O
ATOM 545 CB LYS A 67 -230.419 10.980 40.494 1.00101.61 C
ANISOU 545 CB LYS A 67 13848 10132 14628 -184 -154 -175 C
ATOM 546 CG LYS A 67 -230.424 9.468 40.635 1.00107.10 C
ANISOU 546 CG LYS A 67 14580 10590 15522 -195 -116 -187 C
ATOM 547 CD LYS A 67 -231.143 8.834 39.458 1.00 98.55 C
ANISOU 547 CD LYS A 67 13621 9441 14381 -305 -49 -381 C
ATOM 548 CE LYS A 67 -230.639 7.432 39.188 1.00115.65 C
ANISOU 548 CE LYS A 67 15828 11336 16779 -279 58 -461 C
ATOM 549 NZ LYS A 67 -231.105 6.950 37.860 1.00123.88 N
ANISOU 549 NZ LYS A 67 17004 12322 17743 -386 152 -688 N
ATOM 550 N LEU A 68 -229.222 13.816 39.177 1.00 88.41 N
ANISOU 550 N LEU A 68 12128 8799 12664 -98 -87 -271 N
ATOM 551 CA LEU A 68 -229.473 15.241 39.001 1.00 88.33 C
ANISOU 551 CA LEU A 68 12102 8993 12467 -116 -142 -250 C
ATOM 552 C LEU A 68 -229.376 15.677 37.548 1.00 87.40 C
ANISOU 552 C LEU A 68 12074 8924 12211 -164 -63 -403 C
ATOM 553 O LEU A 68 -229.927 16.723 37.193 1.00 96.41 O
ANISOU 553 O LEU A 68 13231 10221 13179 -215 -129 -397 O
ATOM 554 CB LEU A 68 -228.497 16.066 39.837 1.00 83.45 C
ANISOU 554 CB LEU A 68 11369 8437 11901 -11 -163 -128 C
ATOM 555 CG LEU A 68 -228.538 15.856 41.350 1.00 87.03 C
ANISOU 555 CG LEU A 68 11742 8878 12448 20 -260 42 C
ATOM 556 CD1 LEU A 68 -227.410 16.619 42.007 1.00 84.09 C
ANISOU 556 CD1 LEU A 68 11267 8556 12127 115 -274 141 C
ATOM 557 CD2 LEU A 68 -229.872 16.283 41.927 1.00 70.64 C
ANISOU 557 CD2 LEU A 68 9676 6924 10240 -70 -366 99 C
ATOM 558 N ARG A 69 -228.706 14.903 36.697 1.00 73.73 N
ANISOU 558 N ARG A 69 10404 7058 10551 -157 79 -539 N
ATOM 559 CA ARG A 69 -228.515 15.325 35.318 1.00 79.60 C
ANISOU 559 CA ARG A 69 11248 7854 11141 -218 172 -686 C
ATOM 560 C ARG A 69 -229.739 15.083 34.440 1.00 85.15 C
ANISOU 560 C ARG A 69 12088 8594 11669 -374 121 -785 C
ATOM 561 O ARG A 69 -229.621 14.488 33.371 1.00 97.09 O
ANISOU 561 O ARG A 69 13721 10033 13135 -447 232 -950 O
ATOM 562 CB ARG A 69 -227.315 14.626 34.698 1.00 86.08 C
ANISOU 562 CB ARG A 69 12087 8520 12100 -163 370 -816 C
ATOM 563 CG ARG A 69 -226.004 14.940 35.366 1.00 82.72 C
ANISOU 563 CG ARG A 69 11516 8062 11852 -15 424 -729 C
ATOM 564 CD ARG A 69 -224.847 14.215 34.695 1.00104.28 C
ANISOU 564 CD ARG A 69 14245 10625 14750 40 638 -872 C
ATOM 565 NE ARG A 69 -223.617 14.318 35.478 1.00125.71 N
ANISOU 565 NE ARG A 69 16790 13279 17696 190 669 -770 N
ATOM 566 CZ ARG A 69 -223.145 13.352 36.260 1.00124.66 C
ANISOU 566 CZ ARG A 69 16561 12967 17839 285 669 -705 C
ATOM 567 NH1 ARG A 69 -223.801 12.207 36.354 1.00 92.56 N
ANISOU 567 NH1 ARG A 69 12559 8759 13851 246 656 -737 N
ATOM 568 NH2 ARG A 69 -222.014 13.524 36.936 1.00146.05 N
ANISOU 568 NH2 ARG A 69 19107 15632 20753 413 675 -600 N
ATOM 569 N THR A 70 -230.896 15.547 34.884 1.00 86.94 N
ANISOU 569 N THR A 70 12294 8936 11805 -431 -43 -691 N
ATOM 570 CA THR A 70 -232.114 15.528 34.092 1.00 90.30 C
ANISOU 570 CA THR A 70 12822 9425 12064 -581 -129 -757 C
ATOM 571 C THR A 70 -232.250 16.828 33.304 1.00109.18 C
ANISOU 571 C THR A 70 15249 11986 14250 -629 -185 -752 C
ATOM 572 O THR A 70 -231.819 17.891 33.772 1.00108.19 O
ANISOU 572 O THR A 70 15033 11954 14121 -546 -212 -649 O
ATOM 573 CB THR A 70 -233.323 15.343 35.000 1.00101.97 C
ANISOU 573 CB THR A 70 14234 10928 13581 -618 -274 -653 C
ATOM 574 OG1 THR A 70 -233.358 16.397 35.969 1.00114.35 O
ANISOU 574 OG1 THR A 70 15675 12614 15158 -541 -356 -503 O
ATOM 575 CG2 THR A 70 -233.239 14.007 35.729 1.00119.42 C
ANISOU 575 CG2 THR A 70 16428 12963 15984 -591 -226 -648 C
ATOM 576 N PRO A 71 -232.826 16.760 32.098 1.00102.47 N
ANISOU 576 N PRO A 71 14536 11171 13226 -772 -208 -858 N
ATOM 577 CA PRO A 71 -232.998 17.987 31.300 1.00 97.60 C
ANISOU 577 CA PRO A 71 13965 10710 12408 -832 -282 -834 C
ATOM 578 C PRO A 71 -233.809 19.059 32.004 1.00 94.40 C
ANISOU 578 C PRO A 71 13438 10433 11996 -804 -460 -673 C
ATOM 579 O PRO A 71 -233.523 20.253 31.839 1.00104.84 O
ANISOU 579 O PRO A 71 14734 11860 13240 -775 -493 -606 O
ATOM 580 CB PRO A 71 -233.698 17.477 30.033 1.00 90.69 C
ANISOU 580 CB PRO A 71 13262 9837 11358 -1016 -312 -964 C
ATOM 581 CG PRO A 71 -233.280 16.052 29.936 1.00 89.61 C
ANISOU 581 CG PRO A 71 13193 9525 11331 -1024 -157 -1108 C
ATOM 582 CD PRO A 71 -233.211 15.558 31.340 1.00 90.66 C
ANISOU 582 CD PRO A 71 13175 9567 11705 -892 -158 -1011 C
ATOM 583 N LEU A 72 -234.803 18.669 32.805 1.00 80.77 N
ANISOU 583 N LEU A 72 11632 8693 10362 -815 -562 -613 N
ATOM 584 CA LEU A 72 -235.563 19.636 33.586 1.00 85.22 C
ANISOU 584 CA LEU A 72 12064 9364 10953 -781 -700 -475 C
ATOM 585 C LEU A 72 -234.685 20.390 34.578 1.00 88.01 C
ANISOU 585 C LEU A 72 12304 9741 11395 -635 -648 -380 C
ATOM 586 O LEU A 72 -235.084 21.455 35.065 1.00 83.27 O
ANISOU 586 O LEU A 72 11608 9236 10794 -602 -736 -282 O
ATOM 587 CB LEU A 72 -236.700 18.925 34.321 1.00 87.82 C
ANISOU 587 CB LEU A 72 12327 9658 11382 -824 -780 -445 C
ATOM 588 CG LEU A 72 -237.841 19.790 34.857 1.00106.20 C
ANISOU 588 CG LEU A 72 14529 12091 13729 -837 -927 -338 C
ATOM 589 CD1 LEU A 72 -238.486 20.571 33.724 1.00112.67 C
ANISOU 589 CD1 LEU A 72 15394 13007 14409 -931 -1058 -340 C
ATOM 590 CD2 LEU A 72 -238.869 18.929 35.574 1.00101.02 C
ANISOU 590 CD2 LEU A 72 13813 11388 13182 -890 -969 -325 C
ATOM 591 N ASN A 73 -233.500 19.868 34.885 1.00 76.95 N
ANISOU 591 N ASN A 73 10906 8250 10083 -550 -509 -410 N
ATOM 592 CA ASN A 73 -232.594 20.511 35.823 1.00 80.63 C
ANISOU 592 CA ASN A 73 11266 8736 10634 -423 -468 -320 C
ATOM 593 C ASN A 73 -231.519 21.347 35.142 1.00 74.34 C
ANISOU 593 C ASN A 73 10497 7982 9766 -384 -393 -342 C
ATOM 594 O ASN A 73 -230.836 22.115 35.828 1.00 70.46 O
ANISOU 594 O ASN A 73 9916 7531 9326 -294 -381 -264 O
ATOM 595 CB ASN A 73 -231.935 19.461 36.726 1.00 76.59 C
ANISOU 595 CB ASN A 73 10712 8096 10294 -348 -387 -307 C
ATOM 596 CG ASN A 73 -232.858 18.978 37.823 1.00 78.00 C
ANISOU 596 CG ASN A 73 10827 8258 10551 -365 -467 -231 C
ATOM 597 OD1 ASN A 73 -233.870 19.612 38.120 1.00114.36 O
ANISOU 597 OD1 ASN A 73 15386 12960 15106 -408 -570 -178 O
ATOM 598 ND2 ASN A 73 -232.508 17.860 38.442 1.00 96.57 N
ANISOU 598 ND2 ASN A 73 13171 10481 13039 -334 -417 -220 N
ATOM 599 N TYR A 74 -231.349 21.217 33.821 1.00 66.12 N
ANISOU 599 N TYR A 74 9585 6938 8601 -464 -337 -450 N
ATOM 600 CA TYR A 74 -230.358 22.025 33.115 1.00 65.30 C
ANISOU 600 CA TYR A 74 9517 6880 8414 -447 -253 -472 C
ATOM 601 C TYR A 74 -230.538 23.511 33.415 1.00 73.20 C
ANISOU 601 C TYR A 74 10445 8006 9363 -419 -359 -351 C
ATOM 602 O TYR A 74 -229.557 24.235 33.621 1.00 76.87 O
ANISOU 602 O TYR A 74 10857 8495 9855 -345 -296 -314 O
ATOM 603 CB TYR A 74 -230.444 21.793 31.602 1.00 62.26 C
ANISOU 603 CB TYR A 74 9304 6501 7850 -579 -205 -596 C
ATOM 604 CG TYR A 74 -229.954 20.453 31.082 1.00 80.83 C
ANISOU 604 CG TYR A 74 11749 8720 10244 -610 -45 -753 C
ATOM 605 CD1 TYR A 74 -229.737 19.375 31.932 1.00 96.69 C
ANISOU 605 CD1 TYR A 74 13687 10594 12456 -530 12 -766 C
ATOM 606 CD2 TYR A 74 -229.707 20.273 29.725 1.00 78.25 C
ANISOU 606 CD2 TYR A 74 11587 8392 9751 -727 54 -891 C
ATOM 607 CE1 TYR A 74 -229.294 18.153 31.442 1.00 98.68 C
ANISOU 607 CE1 TYR A 74 14019 10702 12774 -553 164 -915 C
ATOM 608 CE2 TYR A 74 -229.262 19.060 29.228 1.00 90.07 C
ANISOU 608 CE2 TYR A 74 13172 9755 11294 -760 222 -1056 C
ATOM 609 CZ TYR A 74 -229.057 18.004 30.088 1.00101.50 C
ANISOU 609 CZ TYR A 74 14535 11057 12974 -665 277 -1070 C
ATOM 610 OH TYR A 74 -228.616 16.797 29.587 1.00112.23 O
ANISOU 610 OH TYR A 74 15975 12261 14406 -692 450 -1239 O
ATOM 611 N ILE A 75 -231.786 23.983 33.454 1.00 77.25 N
ANISOU 611 N ILE A 75 10942 8590 9820 -476 -519 -291 N
ATOM 612 CA ILE A 75 -232.019 25.409 33.650 1.00 81.66 C
ANISOU 612 CA ILE A 75 11432 9248 10346 -452 -617 -185 C
ATOM 613 C ILE A 75 -231.589 25.837 35.046 1.00 80.12 C
ANISOU 613 C ILE A 75 11094 9055 10294 -332 -601 -104 C
ATOM 614 O ILE A 75 -231.203 26.992 35.256 1.00 73.41 O
ANISOU 614 O ILE A 75 10191 8263 9440 -287 -616 -40 O
ATOM 615 CB ILE A 75 -233.495 25.756 33.374 1.00 82.68 C
ANISOU 615 CB ILE A 75 11558 9436 10422 -537 -792 -140 C
ATOM 616 CG1 ILE A 75 -233.663 27.267 33.214 1.00 75.33 C
ANISOU 616 CG1 ILE A 75 10583 8590 9449 -525 -888 -43 C
ATOM 617 CG2 ILE A 75 -234.391 25.236 34.481 1.00 82.41 C
ANISOU 617 CG2 ILE A 75 11416 9376 10519 -513 -848 -109 C
ATOM 618 CD1 ILE A 75 -232.893 27.829 32.047 1.00 68.00 C
ANISOU 618 CD1 ILE A 75 9773 7694 8369 -574 -845 -59 C
ATOM 619 N LEU A 76 -231.624 24.918 36.015 1.00 65.90 N
ANISOU 619 N LEU A 76 9238 7188 8614 -290 -573 -104 N
ATOM 620 CA LEU A 76 -231.147 25.239 37.355 1.00 65.13 C
ANISOU 620 CA LEU A 76 9023 7094 8629 -196 -560 -27 C
ATOM 621 C LEU A 76 -229.631 25.359 37.402 1.00 80.92 C
ANISOU 621 C LEU A 76 11009 9065 10673 -121 -449 -32 C
ATOM 622 O LEU A 76 -229.101 26.151 38.189 1.00 71.22 O
ANISOU 622 O LEU A 76 9696 7876 9489 -59 -456 37 O
ATOM 623 CB LEU A 76 -231.617 24.185 38.353 1.00 73.81 C
ANISOU 623 CB LEU A 76 10083 8131 9830 -192 -570 -11 C
ATOM 624 CG LEU A 76 -233.122 24.134 38.598 1.00 77.05 C
ANISOU 624 CG LEU A 76 10469 8575 10230 -261 -673 7 C
ATOM 625 CD1 LEU A 76 -233.454 23.003 39.554 1.00 78.36 C
ANISOU 625 CD1 LEU A 76 10609 8671 10492 -268 -661 23 C
ATOM 626 CD2 LEU A 76 -233.592 25.465 39.145 1.00 74.03 C
ANISOU 626 CD2 LEU A 76 9996 8287 9844 -241 -742 76 C
ATOM 627 N LEU A 77 -228.915 24.567 36.599 1.00 80.86 N
ANISOU 627 N LEU A 77 11074 8983 10666 -128 -340 -120 N
ATOM 628 CA LEU A 77 -227.478 24.773 36.476 1.00 83.16 C
ANISOU 628 CA LEU A 77 11338 9250 11010 -62 -223 -133 C
ATOM 629 C LEU A 77 -227.183 26.118 35.828 1.00 83.57 C
ANISOU 629 C LEU A 77 11407 9396 10949 -81 -227 -115 C
ATOM 630 O LEU A 77 -226.277 26.840 36.264 1.00 77.76 O
ANISOU 630 O LEU A 77 10596 8685 10266 -19 -196 -66 O
ATOM 631 CB LEU A 77 -226.846 23.636 35.673 1.00 79.12 C
ANISOU 631 CB LEU A 77 10899 8629 10535 -72 -83 -251 C
ATOM 632 CG LEU A 77 -226.970 22.242 36.292 1.00 85.26 C
ANISOU 632 CG LEU A 77 11656 9281 11456 -44 -67 -267 C
ATOM 633 CD1 LEU A 77 -226.453 21.179 35.343 1.00 93.63 C
ANISOU 633 CD1 LEU A 77 12800 10222 12553 -65 83 -408 C
ATOM 634 CD2 LEU A 77 -226.217 22.195 37.604 1.00 80.08 C
ANISOU 634 CD2 LEU A 77 10867 8592 10970 62 -81 -162 C
ATOM 635 N ASN A 78 -227.950 26.471 34.791 1.00 73.89 N
ANISOU 635 N ASN A 78 10284 8222 9569 -176 -276 -145 N
ATOM 636 CA ASN A 78 -227.803 27.777 34.159 1.00 80.52 C
ANISOU 636 CA ASN A 78 11150 9146 10297 -207 -303 -106 C
ATOM 637 C ASN A 78 -228.046 28.895 35.159 1.00 82.15 C
ANISOU 637 C ASN A 78 11242 9410 10559 -151 -403 5 C
ATOM 638 O ASN A 78 -227.398 29.946 35.098 1.00 78.21 O
ANISOU 638 O ASN A 78 10717 8952 10046 -129 -386 47 O
ATOM 639 CB ASN A 78 -228.771 27.901 32.984 1.00 84.22 C
ANISOU 639 CB ASN A 78 11747 9658 10596 -330 -383 -131 C
ATOM 640 CG ASN A 78 -228.596 29.194 32.223 1.00 71.13 C
ANISOU 640 CG ASN A 78 10135 8076 8815 -376 -416 -78 C
ATOM 641 OD1 ASN A 78 -227.497 29.517 31.776 1.00 81.87 O
ANISOU 641 OD1 ASN A 78 11525 9439 10143 -371 -295 -103 O
ATOM 642 ND2 ASN A 78 -229.680 29.951 32.083 1.00 72.90 N
ANISOU 642 ND2 ASN A 78 10358 8355 8984 -421 -582 1 N
ATOM 643 N LEU A 79 -228.984 28.687 36.084 1.00 72.78 N
ANISOU 643 N LEU A 79 9991 8224 9439 -135 -496 44 N
ATOM 644 CA LEU A 79 -229.199 29.657 37.149 1.00 61.46 C
ANISOU 644 CA LEU A 79 8449 6835 8068 -86 -564 127 C
ATOM 645 C LEU A 79 -227.968 29.780 38.037 1.00 65.87 C
ANISOU 645 C LEU A 79 8930 7379 8719 -6 -490 152 C
ATOM 646 O LEU A 79 -227.572 30.891 38.407 1.00 81.26 O
ANISOU 646 O LEU A 79 10826 9370 10679 21 -504 201 O
ATOM 647 CB LEU A 79 -230.421 29.261 37.974 1.00 65.77 C
ANISOU 647 CB LEU A 79 8944 7380 8666 -97 -647 147 C
ATOM 648 CG LEU A 79 -230.644 30.051 39.262 1.00 69.49 C
ANISOU 648 CG LEU A 79 9306 7886 9210 -53 -686 209 C
ATOM 649 CD1 LEU A 79 -231.008 31.482 38.931 1.00 70.27 C
ANISOU 649 CD1 LEU A 79 9382 8037 9283 -60 -749 247 C
ATOM 650 CD2 LEU A 79 -231.724 29.404 40.118 1.00 59.65 C
ANISOU 650 CD2 LEU A 79 8017 6631 8018 -75 -728 213 C
ATOM 651 N ALA A 80 -227.338 28.650 38.377 1.00 78.05 N
ANISOU 651 N ALA A 80 10463 8853 10340 28 -419 124 N
ATOM 652 CA ALA A 80 -226.180 28.683 39.267 1.00 69.38 C
ANISOU 652 CA ALA A 80 9279 7737 9347 99 -375 163 C
ATOM 653 C ALA A 80 -224.994 29.380 38.611 1.00 78.53 C
ANISOU 653 C ALA A 80 10432 8909 10497 118 -292 150 C
ATOM 654 O ALA A 80 -224.240 30.096 39.282 1.00 76.01 O
ANISOU 654 O ALA A 80 10033 8617 10232 158 -296 203 O
ATOM 655 CB ALA A 80 -225.802 27.268 39.694 1.00 65.58 C
ANISOU 655 CB ALA A 80 8783 7162 8974 132 -330 149 C
ATOM 656 N VAL A 81 -224.814 29.188 37.304 1.00 75.17 N
ANISOU 656 N VAL A 81 10098 8469 9997 76 -213 78 N
ATOM 657 CA VAL A 81 -223.753 29.892 36.591 1.00 80.47 C
ANISOU 657 CA VAL A 81 10773 9159 10642 75 -120 61 C
ATOM 658 C VAL A 81 -224.017 31.393 36.599 1.00 81.94 C
ANISOU 658 C VAL A 81 10952 9427 10755 51 -198 129 C
ATOM 659 O VAL A 81 -223.117 32.200 36.863 1.00 76.95 O
ANISOU 659 O VAL A 81 10255 8816 10165 80 -167 165 O
ATOM 660 CB VAL A 81 -223.624 29.349 35.156 1.00 72.46 C
ANISOU 660 CB VAL A 81 9882 8117 9532 9 -9 -41 C
ATOM 661 CG1 VAL A 81 -222.684 30.222 34.347 1.00 72.58 C
ANISOU 661 CG1 VAL A 81 9920 8169 9490 -19 88 -52 C
ATOM 662 CG2 VAL A 81 -223.142 27.901 35.180 1.00 61.38 C
ANISOU 662 CG2 VAL A 81 8470 6607 8244 45 98 -121 C
ATOM 663 N ALA A 82 -225.264 31.784 36.321 1.00 85.22 N
ANISOU 663 N ALA A 82 11423 9880 11076 -1 -305 150 N
ATOM 664 CA ALA A 82 -225.626 33.197 36.298 1.00 65.96 C
ANISOU 664 CA ALA A 82 8972 7497 8592 -19 -387 217 C
ATOM 665 C ALA A 82 -225.321 33.867 37.627 1.00 69.05 C
ANISOU 665 C ALA A 82 9245 7902 9089 43 -420 272 C
ATOM 666 O ALA A 82 -224.783 34.981 37.664 1.00 79.49 O
ANISOU 666 O ALA A 82 10537 9248 10416 47 -416 310 O
ATOM 667 CB ALA A 82 -227.107 33.350 35.963 1.00 62.53 C
ANISOU 667 CB ALA A 82 8585 7083 8091 -72 -512 237 C
ATOM 668 N ASP A 83 -225.667 33.206 38.730 1.00 61.73 N
ANISOU 668 N ASP A 83 8259 6959 8238 78 -452 276 N
ATOM 669 CA ASP A 83 -225.363 33.755 40.045 1.00 79.98 C
ANISOU 669 CA ASP A 83 10475 9289 10626 116 -481 320 C
ATOM 670 C ASP A 83 -223.863 33.929 40.239 1.00 84.19 C
ANISOU 670 C ASP A 83 10955 9815 11218 150 -410 332 C
ATOM 671 O ASP A 83 -223.420 34.900 40.866 1.00 81.66 O
ANISOU 671 O ASP A 83 10577 9524 10927 157 -431 367 O
ATOM 672 CB ASP A 83 -225.944 32.851 41.128 1.00 76.74 C
ANISOU 672 CB ASP A 83 10031 8863 10263 127 -518 325 C
ATOM 673 CG ASP A 83 -227.458 32.850 41.129 1.00 88.75 C
ANISOU 673 CG ASP A 83 11574 10398 11751 91 -588 318 C
ATOM 674 OD1 ASP A 83 -228.057 33.526 40.264 1.00 90.26 O
ANISOU 674 OD1 ASP A 83 11800 10604 11889 62 -624 315 O
ATOM 675 OD2 ASP A 83 -228.049 32.171 41.992 1.00 81.74 O
ANISOU 675 OD2 ASP A 83 10662 9501 10893 85 -611 321 O
ATOM 676 N LEU A 84 -223.062 33.001 39.703 1.00 76.44 N
ANISOU 676 N LEU A 84 9984 8789 10270 168 -322 296 N
ATOM 677 CA LEU A 84 -221.614 33.126 39.814 1.00 70.59 C
ANISOU 677 CA LEU A 84 9171 8035 9615 202 -249 305 C
ATOM 678 C LEU A 84 -221.104 34.331 39.030 1.00 79.00 C
ANISOU 678 C LEU A 84 10254 9137 10627 171 -205 308 C
ATOM 679 O LEU A 84 -220.157 35.001 39.461 1.00 64.88 O
ANISOU 679 O LEU A 84 8386 7362 8902 186 -191 340 O
ATOM 680 CB LEU A 84 -220.944 31.837 39.349 1.00 68.10 C
ANISOU 680 CB LEU A 84 8854 7646 9375 233 -148 254 C
ATOM 681 CG LEU A 84 -221.135 30.661 40.309 1.00 69.13 C
ANISOU 681 CG LEU A 84 8942 7723 9601 272 -194 276 C
ATOM 682 CD1 LEU A 84 -220.419 29.421 39.797 1.00 75.26 C
ANISOU 682 CD1 LEU A 84 9708 8403 10486 311 -84 221 C
ATOM 683 CD2 LEU A 84 -220.648 31.024 41.708 1.00 62.64 C
ANISOU 683 CD2 LEU A 84 8015 6926 8858 299 -278 363 C
ATOM 684 N PHE A 85 -221.727 34.630 37.885 1.00 69.60 N
ANISOU 684 N PHE A 85 9169 7960 9316 117 -194 283 N
ATOM 685 CA PHE A 85 -221.435 35.882 37.188 1.00 75.73 C
ANISOU 685 CA PHE A 85 9978 8771 10027 73 -178 308 C
ATOM 686 C PHE A 85 -221.692 37.085 38.088 1.00 76.12 C
ANISOU 686 C PHE A 85 9966 8848 10108 82 -275 371 C
ATOM 687 O PHE A 85 -220.870 38.005 38.156 1.00 83.83 O
ANISOU 687 O PHE A 85 10901 9836 11115 75 -247 399 O
ATOM 688 CB PHE A 85 -222.276 35.993 35.916 1.00 79.38 C
ANISOU 688 CB PHE A 85 10575 9245 10340 -1 -194 295 C
ATOM 689 CG PHE A 85 -221.702 35.266 34.736 1.00 75.81 C
ANISOU 689 CG PHE A 85 10207 8776 9819 -45 -60 222 C
ATOM 690 CD1 PHE A 85 -221.437 33.911 34.796 1.00 83.78 C
ANISOU 690 CD1 PHE A 85 11208 9737 10888 -13 20 147 C
ATOM 691 CD2 PHE A 85 -221.451 35.940 33.555 1.00 86.44 C
ANISOU 691 CD2 PHE A 85 11651 10150 11041 -127 -8 227 C
ATOM 692 CE1 PHE A 85 -220.917 33.248 33.707 1.00 94.43 C
ANISOU 692 CE1 PHE A 85 12638 11061 12182 -58 165 59 C
ATOM 693 CE2 PHE A 85 -220.933 35.280 32.462 1.00 93.65 C
ANISOU 693 CE2 PHE A 85 12657 11052 11873 -185 136 144 C
ATOM 694 CZ PHE A 85 -220.667 33.932 32.539 1.00 87.96 C
ANISOU 694 CZ PHE A 85 11921 10279 11221 -149 231 50 C
ATOM 695 N MET A 86 -222.827 37.095 38.791 1.00 76.05 N
ANISOU 695 N MET A 86 9950 8845 10101 91 -376 386 N
ATOM 696 CA MET A 86 -223.100 38.167 39.741 1.00 71.81 C
ANISOU 696 CA MET A 86 9355 8324 9607 98 -447 422 C
ATOM 697 C MET A 86 -222.082 38.194 40.873 1.00 81.35 C
ANISOU 697 C MET A 86 10468 9539 10900 125 -429 431 C
ATOM 698 O MET A 86 -221.724 39.272 41.359 1.00 89.54 O
ANISOU 698 O MET A 86 11465 10589 11967 114 -448 453 O
ATOM 699 CB MET A 86 -224.509 38.016 40.317 1.00 58.98 C
ANISOU 699 CB MET A 86 7729 6700 7981 100 -532 419 C
ATOM 700 CG MET A 86 -225.614 38.093 39.286 1.00 80.96 C
ANISOU 700 CG MET A 86 10585 9477 10698 68 -582 424 C
ATOM 701 SD MET A 86 -227.255 37.770 39.974 1.00 83.57 S
ANISOU 701 SD MET A 86 10886 9804 11062 71 -670 413 S
ATOM 702 CE MET A 86 -227.264 38.840 41.412 1.00 84.69 C
ANISOU 702 CE MET A 86 10935 9952 11293 92 -680 417 C
ATOM 703 N VAL A 87 -221.616 37.027 41.313 1.00 81.28 N
ANISOU 703 N VAL A 87 10425 9517 10939 156 -405 421 N
ATOM 704 CA VAL A 87 -220.743 36.967 42.482 1.00 75.33 C
ANISOU 704 CA VAL A 87 9581 8772 10267 174 -423 448 C
ATOM 705 C VAL A 87 -219.334 37.435 42.135 1.00 82.77 C
ANISOU 705 C VAL A 87 10466 9714 11270 176 -360 460 C
ATOM 706 O VAL A 87 -218.694 38.143 42.922 1.00 70.27 O
ANISOU 706 O VAL A 87 8815 8154 9732 163 -394 489 O
ATOM 707 CB VAL A 87 -220.751 35.542 43.070 1.00 71.04 C
ANISOU 707 CB VAL A 87 9017 8203 9772 204 -437 454 C
ATOM 708 CG1 VAL A 87 -219.610 35.349 44.068 1.00 70.96 C
ANISOU 708 CG1 VAL A 87 8909 8194 9858 220 -463 503 C
ATOM 709 CG2 VAL A 87 -222.089 35.263 43.747 1.00 67.33 C
ANISOU 709 CG2 VAL A 87 8586 7746 9251 185 -505 452 C
ATOM 710 N PHE A 88 -218.830 37.062 40.957 1.00 75.04 N
ANISOU 710 N PHE A 88 9512 8710 10289 182 -260 432 N
ATOM 711 CA PHE A 88 -217.467 37.417 40.582 1.00 76.11 C
ANISOU 711 CA PHE A 88 9580 8841 10496 180 -176 435 C
ATOM 712 C PHE A 88 -217.415 38.664 39.716 1.00 90.90 C
ANISOU 712 C PHE A 88 11507 10736 12296 127 -138 439 C
ATOM 713 O PHE A 88 -216.479 39.461 39.841 1.00109.67 O
ANISOU 713 O PHE A 88 13817 13123 14728 108 -113 461 O
ATOM 714 CB PHE A 88 -216.793 36.248 39.857 1.00 66.95 C
ANISOU 714 CB PHE A 88 8404 7633 9400 213 -58 390 C
ATOM 715 CG PHE A 88 -216.571 35.048 40.728 1.00 74.91 C
ANISOU 715 CG PHE A 88 9336 8600 10526 272 -94 405 C
ATOM 716 CD1 PHE A 88 -215.583 35.061 41.700 1.00 75.86 C
ANISOU 716 CD1 PHE A 88 9323 8719 10783 299 -140 461 C
ATOM 717 CD2 PHE A 88 -217.346 33.908 40.578 1.00 77.73 C
ANISOU 717 CD2 PHE A 88 9757 8917 10862 292 -95 373 C
ATOM 718 CE1 PHE A 88 -215.375 33.963 42.508 1.00 85.02 C
ANISOU 718 CE1 PHE A 88 10414 9833 12054 347 -194 498 C
ATOM 719 CE2 PHE A 88 -217.139 32.804 41.383 1.00 83.70 C
ANISOU 719 CE2 PHE A 88 10446 9621 11734 342 -134 402 C
ATOM 720 CZ PHE A 88 -216.151 32.834 42.347 1.00 88.27 C
ANISOU 720 CZ PHE A 88 10894 10196 12449 371 -188 471 C
ATOM 721 N GLY A 89 -218.403 38.850 38.841 1.00 81.42 N
ANISOU 721 N GLY A 89 10423 9536 10975 94 -145 426 N
ATOM 722 CA GLY A 89 -218.439 40.047 38.024 1.00 74.01 C
ANISOU 722 CA GLY A 89 9546 8610 9963 36 -132 452 C
ATOM 723 C GLY A 89 -218.887 41.279 38.775 1.00 77.43 C
ANISOU 723 C GLY A 89 9957 9050 10414 25 -233 496 C
ATOM 724 O GLY A 89 -218.416 42.384 38.490 1.00 86.48 O
ANISOU 724 O GLY A 89 11102 10193 11564 -14 -217 528 O
ATOM 725 N GLY A 90 -219.783 41.118 39.744 1.00 75.73 N
ANISOU 725 N GLY A 90 9724 8836 10216 54 -325 493 N
ATOM 726 CA GLY A 90 -220.336 42.259 40.445 1.00 69.43 C
ANISOU 726 CA GLY A 90 8908 8032 9439 42 -403 512 C
ATOM 727 C GLY A 90 -219.896 42.378 41.888 1.00 79.40 C
ANISOU 727 C GLY A 90 10084 9311 10774 51 -435 502 C
ATOM 728 O GLY A 90 -219.325 43.399 42.281 1.00 85.03 O
ANISOU 728 O GLY A 90 10759 10022 11528 23 -440 512 O
ATOM 729 N PHE A 91 -220.148 41.341 42.691 1.00 64.92 N
ANISOU 729 N PHE A 91 8226 7493 8948 78 -462 486 N
ATOM 730 CA PHE A 91 -219.926 41.463 44.131 1.00 53.50 C
ANISOU 730 CA PHE A 91 6720 6069 7537 65 -513 483 C
ATOM 731 C PHE A 91 -218.442 41.585 44.452 1.00 69.84 C
ANISOU 731 C PHE A 91 8711 8154 9673 53 -498 508 C
ATOM 732 O PHE A 91 -218.047 42.376 45.318 1.00 71.74 O
ANISOU 732 O PHE A 91 8912 8411 9935 12 -537 509 O
ATOM 733 CB PHE A 91 -220.534 40.269 44.869 1.00 61.21 C
ANISOU 733 CB PHE A 91 7701 7059 8497 84 -549 477 C
ATOM 734 CG PHE A 91 -222.007 40.068 44.617 1.00 83.10 C
ANISOU 734 CG PHE A 91 10533 9820 11222 91 -564 451 C
ATOM 735 CD1 PHE A 91 -222.794 41.093 44.108 1.00 82.42 C
ANISOU 735 CD1 PHE A 91 10478 9714 11125 80 -572 439 C
ATOM 736 CD2 PHE A 91 -222.609 38.848 44.899 1.00 76.01 C
ANISOU 736 CD2 PHE A 91 9651 8923 10306 105 -579 447 C
ATOM 737 CE1 PHE A 91 -224.142 40.904 43.875 1.00 73.79 C
ANISOU 737 CE1 PHE A 91 9417 8606 10013 87 -598 422 C
ATOM 738 CE2 PHE A 91 -223.960 38.653 44.670 1.00 74.31 C
ANISOU 738 CE2 PHE A 91 9478 8698 10060 105 -595 423 C
ATOM 739 CZ PHE A 91 -224.729 39.682 44.157 1.00 71.86 C
ANISOU 739 CZ PHE A 91 9184 8373 9748 97 -607 411 C
ATOM 740 N THR A 92 -217.605 40.802 43.768 1.00 73.65 N
ANISOU 740 N THR A 92 9161 8626 10197 83 -438 522 N
ATOM 741 CA THR A 92 -216.168 40.849 44.014 1.00 58.88 C
ANISOU 741 CA THR A 92 7189 6762 8422 77 -421 548 C
ATOM 742 C THR A 92 -215.594 42.206 43.633 1.00 72.21 C
ANISOU 742 C THR A 92 8864 8451 10123 29 -390 552 C
ATOM 743 O THR A 92 -214.882 42.840 44.424 1.00 60.55 O
ANISOU 743 O THR A 92 7317 6992 8696 -10 -434 568 O
ATOM 744 CB THR A 92 -215.479 39.733 43.231 1.00 60.86 C
ANISOU 744 CB THR A 92 7402 6985 8739 125 -336 546 C
ATOM 745 OG1 THR A 92 -215.667 38.487 43.914 1.00 68.60 O
ANISOU 745 OG1 THR A 92 8359 7953 9755 166 -386 562 O
ATOM 746 CG2 THR A 92 -213.997 40.013 43.093 1.00 79.11 C
ANISOU 746 CG2 THR A 92 9598 9293 11167 118 -284 566 C
ATOM 747 N THR A 93 -215.899 42.667 42.417 1.00 75.94 N
ANISOU 747 N THR A 93 9408 8902 10543 20 -320 542 N
ATOM 748 CA THR A 93 -215.433 43.976 41.979 1.00 70.93 C
ANISOU 748 CA THR A 93 8776 8258 9917 -33 -290 557 C
ATOM 749 C THR A 93 -215.896 45.071 42.931 1.00 73.64 C
ANISOU 749 C THR A 93 9124 8597 10259 -69 -374 552 C
ATOM 750 O THR A 93 -215.098 45.923 43.343 1.00 60.19 O
ANISOU 750 O THR A 93 7364 6893 8610 -117 -382 560 O
ATOM 751 CB THR A 93 -215.929 44.261 40.562 1.00 70.34 C
ANISOU 751 CB THR A 93 8806 8161 9759 -50 -227 563 C
ATOM 752 OG1 THR A 93 -215.648 43.142 39.715 1.00 77.43 O
ANISOU 752 OG1 THR A 93 9720 9062 10637 -26 -137 543 O
ATOM 753 CG2 THR A 93 -215.228 45.469 40.007 1.00 85.37 C
ANISOU 753 CG2 THR A 93 10709 10050 11679 -111 -179 592 C
ATOM 754 N THR A 94 -217.174 45.043 43.318 1.00 58.03 N
ANISOU 754 N THR A 94 7207 6612 8231 -53 -431 530 N
ATOM 755 CA THR A 94 -217.720 46.110 44.150 1.00 67.96 C
ANISOU 755 CA THR A 94 8473 7851 9496 -87 -484 505 C
ATOM 756 C THR A 94 -217.101 46.107 45.542 1.00 66.20 C
ANISOU 756 C THR A 94 8185 7665 9301 -124 -533 486 C
ATOM 757 O THR A 94 -216.873 47.174 46.123 1.00 66.89 O
ANISOU 757 O THR A 94 8261 7739 9415 -180 -552 463 O
ATOM 758 CB THR A 94 -219.242 45.991 44.230 1.00 60.55 C
ANISOU 758 CB THR A 94 7595 6893 8517 -59 -517 479 C
ATOM 759 OG1 THR A 94 -219.813 46.329 42.958 1.00 68.06 O
ANISOU 759 OG1 THR A 94 8608 7804 9449 -46 -501 510 O
ATOM 760 CG2 THR A 94 -219.795 46.922 45.297 1.00 48.42 C
ANISOU 760 CG2 THR A 94 6054 5335 7009 -91 -551 429 C
ATOM 761 N LEU A 95 -216.808 44.926 46.092 1.00 69.89 N
ANISOU 761 N LEU A 95 8615 8176 9765 -103 -561 499 N
ATOM 762 CA LEU A 95 -216.071 44.872 47.352 1.00 71.90 C
ANISOU 762 CA LEU A 95 8809 8473 10038 -152 -628 505 C
ATOM 763 C LEU A 95 -214.736 45.598 47.236 1.00 79.73 C
ANISOU 763 C LEU A 95 9722 9464 11106 -197 -621 528 C
ATOM 764 O LEU A 95 -214.311 46.296 48.165 1.00 72.13 O
ANISOU 764 O LEU A 95 8735 8521 10150 -271 -677 514 O
ATOM 765 CB LEU A 95 -215.851 43.419 47.769 1.00 55.67 C
ANISOU 765 CB LEU A 95 6717 6447 7987 -117 -667 544 C
ATOM 766 CG LEU A 95 -214.888 43.146 48.925 1.00 60.33 C
ANISOU 766 CG LEU A 95 7230 7081 8610 -166 -760 586 C
ATOM 767 CD1 LEU A 95 -215.361 43.819 50.199 1.00 62.37 C
ANISOU 767 CD1 LEU A 95 7539 7376 8784 -257 -828 546 C
ATOM 768 CD2 LEU A 95 -214.750 41.652 49.141 1.00 64.57 C
ANISOU 768 CD2 LEU A 95 7734 7624 9176 -116 -799 643 C
ATOM 769 N TYR A 96 -214.068 45.456 46.096 1.00 66.83 N
ANISOU 769 N TYR A 96 8054 7811 9528 -165 -545 558 N
ATOM 770 CA TYR A 96 -212.753 46.056 45.930 1.00 73.63 C
ANISOU 770 CA TYR A 96 8824 8673 10477 -209 -523 582 C
ATOM 771 C TYR A 96 -212.850 47.565 45.736 1.00 78.99 C
ANISOU 771 C TYR A 96 9546 9317 11151 -272 -504 559 C
ATOM 772 O TYR A 96 -212.134 48.333 46.390 1.00 71.04 O
ANISOU 772 O TYR A 96 8486 8317 10189 -345 -545 555 O
ATOM 773 CB TYR A 96 -212.046 45.393 44.754 1.00 56.67 C
ANISOU 773 CB TYR A 96 6628 6513 8392 -161 -419 607 C
ATOM 774 CG TYR A 96 -210.651 45.895 44.518 1.00 64.09 C
ANISOU 774 CG TYR A 96 7454 7453 9443 -205 -376 631 C
ATOM 775 CD1 TYR A 96 -209.592 45.454 45.302 1.00 65.91 C
ANISOU 775 CD1 TYR A 96 7543 7711 9787 -214 -438 664 C
ATOM 776 CD2 TYR A 96 -210.387 46.801 43.499 1.00 52.97 C
ANISOU 776 CD2 TYR A 96 6074 6017 8034 -244 -278 630 C
ATOM 777 CE1 TYR A 96 -208.305 45.910 45.080 1.00 62.40 C
ANISOU 777 CE1 TYR A 96 6974 7267 9467 -257 -398 687 C
ATOM 778 CE2 TYR A 96 -209.105 47.259 43.267 1.00 66.06 C
ANISOU 778 CE2 TYR A 96 7622 7677 9802 -293 -225 650 C
ATOM 779 CZ TYR A 96 -208.069 46.815 44.058 1.00 70.62 C
ANISOU 779 CZ TYR A 96 8045 8282 10506 -297 -282 674 C
ATOM 780 OH TYR A 96 -206.797 47.283 43.816 1.00 74.10 O
ANISOU 780 OH TYR A 96 8358 8723 11075 -349 -229 693 O
ATOM 781 N THR A 97 -213.734 48.002 44.835 1.00 61.25 N
ANISOU 781 N THR A 97 7393 7025 8854 -251 -452 551 N
ATOM 782 CA THR A 97 -213.948 49.430 44.615 1.00 56.05 C
ANISOU 782 CA THR A 97 6780 6310 8206 -303 -442 541 C
ATOM 783 C THR A 97 -214.479 50.117 45.868 1.00 54.42 C
ANISOU 783 C THR A 97 6592 6092 7994 -346 -512 482 C
ATOM 784 O THR A 97 -214.082 51.248 46.181 1.00 58.98 O
ANISOU 784 O THR A 97 7160 6633 8617 -416 -519 462 O
ATOM 785 CB THR A 97 -214.922 49.631 43.460 1.00 55.52 C
ANISOU 785 CB THR A 97 6811 6193 8089 -268 -402 561 C
ATOM 786 OG1 THR A 97 -216.150 48.956 43.773 1.00 58.17 O
ANISOU 786 OG1 THR A 97 7196 6537 8370 -212 -443 533 O
ATOM 787 CG2 THR A 97 -214.344 49.069 42.167 1.00 54.82 C
ANISOU 787 CG2 THR A 97 6727 6119 7982 -254 -315 606 C
ATOM 788 N SER A 98 -215.396 49.459 46.582 1.00 54.92 N
ANISOU 788 N SER A 98 6688 6179 7999 -315 -553 446 N
ATOM 789 CA SER A 98 -215.953 50.025 47.807 1.00 66.32 C
ANISOU 789 CA SER A 98 8158 7618 9423 -366 -596 373 C
ATOM 790 C SER A 98 -214.854 50.484 48.761 1.00 66.11 C
ANISOU 790 C SER A 98 8077 7625 9417 -462 -644 356 C
ATOM 791 O SER A 98 -214.914 51.590 49.315 1.00 58.99 O
ANISOU 791 O SER A 98 7199 6683 8532 -534 -647 294 O
ATOM 792 CB SER A 98 -216.853 48.991 48.490 1.00 69.70 C
ANISOU 792 CB SER A 98 8616 8091 9777 -333 -626 347 C
ATOM 793 OG SER A 98 -217.525 49.540 49.608 1.00 96.69 O
ANISOU 793 OG SER A 98 12072 11502 13163 -389 -639 262 O
ATOM 794 N LEU A 99 -213.841 49.645 48.965 1.00 73.90 N
ANISOU 794 N LEU A 99 8985 8677 10415 -467 -685 410 N
ATOM 795 CA LEU A 99 -212.787 49.958 49.922 1.00 62.96 C
ANISOU 795 CA LEU A 99 7536 7334 9050 -565 -760 410 C
ATOM 796 C LEU A 99 -211.883 51.088 49.452 1.00 74.61 C
ANISOU 796 C LEU A 99 8966 8768 10614 -623 -729 415 C
ATOM 797 O LEU A 99 -211.110 51.621 50.258 1.00 65.99 O
ANISOU 797 O LEU A 99 7833 7700 9542 -725 -792 398 O
ATOM 798 CB LEU A 99 -211.968 48.702 50.213 1.00 74.30 C
ANISOU 798 CB LEU A 99 8882 8841 10508 -544 -827 485 C
ATOM 799 CG LEU A 99 -212.786 47.621 50.920 1.00 66.54 C
ANISOU 799 CG LEU A 99 7950 7899 9432 -514 -877 486 C
ATOM 800 CD1 LEU A 99 -211.998 46.337 51.070 1.00 67.57 C
ANISOU 800 CD1 LEU A 99 7987 8073 9614 -477 -943 577 C
ATOM 801 CD2 LEU A 99 -213.238 48.128 52.273 1.00 63.43 C
ANISOU 801 CD2 LEU A 99 7626 7537 8936 -622 -940 419 C
ATOM 802 N HIS A 100 -211.952 51.449 48.173 1.00 71.50 N
ANISOU 802 N HIS A 100 8585 8315 10266 -574 -638 443 N
ATOM 803 CA HIS A 100 -211.338 52.671 47.679 1.00 67.68 C
ANISOU 803 CA HIS A 100 8085 7772 9856 -637 -596 446 C
ATOM 804 C HIS A 100 -212.281 53.860 47.736 1.00 77.53 C
ANISOU 804 C HIS A 100 9430 8929 11098 -662 -575 385 C
ATOM 805 O HIS A 100 -211.822 55.005 47.662 1.00 84.90 O
ANISOU 805 O HIS A 100 10360 9801 12096 -735 -560 372 O
ATOM 806 CB HIS A 100 -210.879 52.489 46.235 1.00 67.94 C
ANISOU 806 CB HIS A 100 8093 7788 9933 -591 -503 517 C
ATOM 807 CG HIS A 100 -209.775 51.496 46.066 1.00 74.31 C
ANISOU 807 CG HIS A 100 8781 8660 10795 -571 -493 566 C
ATOM 808 ND1 HIS A 100 -209.994 50.137 46.030 1.00 92.67 N
ANISOU 808 ND1 HIS A 100 11089 11030 13093 -487 -499 584 N
ATOM 809 CD2 HIS A 100 -208.442 51.667 45.908 1.00 73.54 C
ANISOU 809 CD2 HIS A 100 8563 8578 10801 -623 -472 600 C
ATOM 810 CE1 HIS A 100 -208.842 49.513 45.863 1.00102.56 C
ANISOU 810 CE1 HIS A 100 12213 12315 14441 -480 -480 625 C
ATOM 811 NE2 HIS A 100 -207.885 50.420 45.786 1.00 95.58 N
ANISOU 811 NE2 HIS A 100 11258 11419 13640 -561 -463 636 N
ATOM 812 N GLY A 101 -213.584 53.614 47.848 1.00 69.75 N
ANISOU 812 N GLY A 101 8523 7923 10058 -601 -572 347 N
ATOM 813 CA GLY A 101 -214.558 54.676 47.849 1.00 60.92 C
ANISOU 813 CA GLY A 101 7477 6702 8970 -605 -547 291 C
ATOM 814 C GLY A 101 -214.864 55.265 46.493 1.00 75.30 C
ANISOU 814 C GLY A 101 9333 8433 10844 -563 -497 358 C
ATOM 815 O GLY A 101 -215.451 56.355 46.430 1.00 61.96 O
ANISOU 815 O GLY A 101 7686 6633 9222 -576 -484 330 O
ATOM 816 N TYR A 102 -214.484 54.594 45.409 1.00 60.63 N
ANISOU 816 N TYR A 102 7463 6612 8961 -520 -468 446 N
ATOM 817 CA TYR A 102 -214.827 55.048 44.065 1.00 61.15 C
ANISOU 817 CA TYR A 102 7586 6608 9042 -495 -430 523 C
ATOM 818 C TYR A 102 -214.467 53.935 43.092 1.00 65.37 C
ANISOU 818 C TYR A 102 8114 7216 9507 -454 -389 588 C
ATOM 819 O TYR A 102 -213.776 52.978 43.448 1.00 80.72 O
ANISOU 819 O TYR A 102 9992 9245 11432 -445 -383 577 O
ATOM 820 CB TYR A 102 -214.125 56.365 43.702 1.00 62.84 C
ANISOU 820 CB TYR A 102 7800 6739 9338 -577 -403 554 C
ATOM 821 CG TYR A 102 -212.629 56.288 43.442 1.00 63.23 C
ANISOU 821 CG TYR A 102 7776 6844 9405 -643 -360 591 C
ATOM 822 CD1 TYR A 102 -211.708 56.431 44.476 1.00 72.60 C
ANISOU 822 CD1 TYR A 102 8878 8070 10635 -712 -388 538 C
ATOM 823 CD2 TYR A 102 -212.138 56.119 42.152 1.00 63.09 C
ANISOU 823 CD2 TYR A 102 7771 6836 9364 -650 -289 677 C
ATOM 824 CE1 TYR A 102 -210.342 56.390 44.235 1.00 68.21 C
ANISOU 824 CE1 TYR A 102 8232 7558 10125 -772 -352 575 C
ATOM 825 CE2 TYR A 102 -210.771 56.072 41.901 1.00 53.05 C
ANISOU 825 CE2 TYR A 102 6416 5609 8130 -712 -229 703 C
ATOM 826 CZ TYR A 102 -209.877 56.208 42.946 1.00 63.26 C
ANISOU 826 CZ TYR A 102 7606 6937 9495 -768 -263 654 C
ATOM 827 OH TYR A 102 -208.519 56.162 42.695 1.00 63.39 O
ANISOU 827 OH TYR A 102 7516 6994 9575 -828 -207 683 O
ATOM 828 N PHE A 103 -214.949 54.066 41.858 1.00 62.14 N
ANISOU 828 N PHE A 103 7779 6767 9066 -434 -364 658 N
ATOM 829 CA PHE A 103 -214.799 52.995 40.874 1.00 67.97 C
ANISOU 829 CA PHE A 103 8539 7569 9720 -402 -314 701 C
ATOM 830 C PHE A 103 -213.425 53.115 40.221 1.00 74.92 C
ANISOU 830 C PHE A 103 9378 8473 10615 -467 -224 740 C
ATOM 831 O PHE A 103 -213.250 53.808 39.214 1.00 67.12 O
ANISOU 831 O PHE A 103 8449 7442 9611 -520 -179 806 O
ATOM 832 CB PHE A 103 -215.915 53.038 39.838 1.00 55.61 C
ANISOU 832 CB PHE A 103 7079 5960 8090 -374 -336 758 C
ATOM 833 CG PHE A 103 -215.964 51.819 38.975 1.00 63.10 C
ANISOU 833 CG PHE A 103 8066 6976 8932 -346 -292 776 C
ATOM 834 CD1 PHE A 103 -216.630 50.680 39.409 1.00 54.47 C
ANISOU 834 CD1 PHE A 103 6963 5930 7801 -276 -323 727 C
ATOM 835 CD2 PHE A 103 -215.313 51.791 37.749 1.00 59.16 C
ANISOU 835 CD2 PHE A 103 7616 6493 8369 -400 -207 832 C
ATOM 836 CE1 PHE A 103 -216.663 49.540 38.630 1.00 54.76 C
ANISOU 836 CE1 PHE A 103 7039 6018 7749 -255 -277 730 C
ATOM 837 CE2 PHE A 103 -215.343 50.650 36.964 1.00 77.61 C
ANISOU 837 CE2 PHE A 103 9997 8888 10604 -385 -150 826 C
ATOM 838 CZ PHE A 103 -216.023 49.519 37.406 1.00 59.46 C
ANISOU 838 CZ PHE A 103 7687 6626 8280 -309 -188 773 C
ATOM 839 N VAL A 104 -212.446 52.400 40.789 1.00 58.31 N
ANISOU 839 N VAL A 104 7168 6439 8549 -465 -198 705 N
ATOM 840 CA VAL A 104 -211.043 52.593 40.414 1.00 73.57 C
ANISOU 840 CA VAL A 104 9020 8391 10541 -529 -112 728 C
ATOM 841 C VAL A 104 -210.665 52.007 39.064 1.00 67.42 C
ANISOU 841 C VAL A 104 8274 7638 9705 -534 13 763 C
ATOM 842 O VAL A 104 -209.560 52.269 38.581 1.00 89.49 O
ANISOU 842 O VAL A 104 11010 10441 12549 -598 111 782 O
ATOM 843 CB VAL A 104 -210.083 51.975 41.447 1.00 67.69 C
ANISOU 843 CB VAL A 104 8129 7707 9882 -524 -136 689 C
ATOM 844 CG1 VAL A 104 -210.134 52.744 42.751 1.00 70.13 C
ANISOU 844 CG1 VAL A 104 8408 7998 10239 -566 -242 652 C
ATOM 845 CG2 VAL A 104 -210.433 50.510 41.668 1.00 57.33 C
ANISOU 845 CG2 VAL A 104 6799 6449 8534 -433 -151 666 C
ATOM 846 N PHE A 105 -211.531 51.221 38.437 1.00 70.35 N
ANISOU 846 N PHE A 105 8736 8023 9971 -481 20 764 N
ATOM 847 CA PHE A 105 -211.179 50.585 37.174 1.00 67.17 C
ANISOU 847 CA PHE A 105 8378 7648 9493 -499 150 777 C
ATOM 848 C PHE A 105 -211.503 51.448 35.963 1.00 75.26 C
ANISOU 848 C PHE A 105 9543 8634 10419 -580 185 850 C
ATOM 849 O PHE A 105 -211.316 50.991 34.830 1.00 72.67 O
ANISOU 849 O PHE A 105 9286 8333 9991 -618 295 860 O
ATOM 850 CB PHE A 105 -211.881 49.223 37.052 1.00 66.45 C
ANISOU 850 CB PHE A 105 8325 7593 9331 -418 144 735 C
ATOM 851 CG PHE A 105 -211.534 48.267 38.162 1.00 69.52 C
ANISOU 851 CG PHE A 105 8585 8015 9815 -344 109 682 C
ATOM 852 CD1 PHE A 105 -210.233 47.821 38.325 1.00 71.41 C
ANISOU 852 CD1 PHE A 105 8684 8278 10170 -346 192 662 C
ATOM 853 CD2 PHE A 105 -212.505 47.815 39.042 1.00 74.22 C
ANISOU 853 CD2 PHE A 105 9193 8612 10394 -278 -9 660 C
ATOM 854 CE1 PHE A 105 -209.904 46.939 39.347 1.00 83.11 C
ANISOU 854 CE1 PHE A 105 10046 9782 11749 -281 136 636 C
ATOM 855 CE2 PHE A 105 -212.180 46.932 40.068 1.00 74.42 C
ANISOU 855 CE2 PHE A 105 9113 8668 10495 -224 -52 629 C
ATOM 856 CZ PHE A 105 -210.880 46.494 40.216 1.00 80.29 C
ANISOU 856 CZ PHE A 105 9723 9431 11353 -225 10 624 C
ATOM 857 N GLY A 106 -211.979 52.671 36.166 1.00 83.15 N
ANISOU 857 N GLY A 106 10586 9565 11441 -613 96 901 N
ATOM 858 CA GLY A 106 -212.221 53.574 35.067 1.00 73.72 C
ANISOU 858 CA GLY A 106 9518 8320 10170 -696 109 995 C
ATOM 859 C GLY A 106 -213.418 53.177 34.228 1.00 90.00 C
ANISOU 859 C GLY A 106 11723 10382 12091 -679 54 1038 C
ATOM 860 O GLY A 106 -214.090 52.172 34.490 1.00 85.03 O
ANISOU 860 O GLY A 106 11093 9790 11425 -599 15 985 O
ATOM 861 N PRO A 107 -213.705 53.972 33.195 1.00 92.44 N
ANISOU 861 N PRO A 107 12160 10645 12317 -763 41 1144 N
ATOM 862 CA PRO A 107 -214.881 53.690 32.355 1.00 83.15 C
ANISOU 862 CA PRO A 107 11124 9467 11004 -763 -42 1205 C
ATOM 863 C PRO A 107 -214.819 52.355 31.636 1.00 76.22 C
ANISOU 863 C PRO A 107 10302 8681 9976 -769 50 1151 C
ATOM 864 O PRO A 107 -215.871 51.768 31.356 1.00102.09 O
ANISOU 864 O PRO A 107 13652 11970 13166 -735 -36 1156 O
ATOM 865 CB PRO A 107 -214.893 54.865 31.365 1.00 81.49 C
ANISOU 865 CB PRO A 107 11034 9191 10736 -879 -65 1347 C
ATOM 866 CG PRO A 107 -213.498 55.386 31.373 1.00 79.91 C
ANISOU 866 CG PRO A 107 10774 8995 10593 -959 76 1339 C
ATOM 867 CD PRO A 107 -213.009 55.198 32.776 1.00 73.96 C
ANISOU 867 CD PRO A 107 9843 8249 10010 -871 83 1226 C
ATOM 868 N THR A 108 -213.621 51.854 31.324 1.00 94.11 N
ANISOU 868 N THR A 108 12528 11004 12223 -814 228 1093 N
ATOM 869 CA THR A 108 -213.511 50.545 30.684 1.00 94.28 C
ANISOU 869 CA THR A 108 12596 11100 12127 -816 340 1018 C
ATOM 870 C THR A 108 -213.997 49.437 31.612 1.00 84.43 C
ANISOU 870 C THR A 108 11258 9872 10948 -684 284 923 C
ATOM 871 O THR A 108 -214.792 48.579 31.213 1.00 88.42 O
ANISOU 871 O THR A 108 11846 10403 11347 -664 253 897 O
ATOM 872 CB THR A 108 -212.068 50.293 30.252 1.00107.27 C
ANISOU 872 CB THR A 108 14187 12786 13786 -883 561 963 C
ATOM 873 OG1 THR A 108 -211.677 51.294 29.306 1.00130.79 O
ANISOU 873 OG1 THR A 108 17270 15750 16674 -1025 621 1057 O
ATOM 874 CG2 THR A 108 -211.934 48.925 29.610 1.00112.02 C
ANISOU 874 CG2 THR A 108 14830 13446 14287 -882 698 864 C
ATOM 875 N GLY A 109 -213.534 49.443 32.862 1.00 72.72 N
ANISOU 875 N GLY A 109 9613 8379 9637 -605 263 875 N
ATOM 876 CA GLY A 109 -214.037 48.478 33.822 1.00 77.30 C
ANISOU 876 CA GLY A 109 10118 8974 10278 -492 195 804 C
ATOM 877 C GLY A 109 -215.505 48.671 34.131 1.00 75.77 C
ANISOU 877 C GLY A 109 9986 8749 10053 -446 25 837 C
ATOM 878 O GLY A 109 -216.183 47.728 34.552 1.00 85.44 O
ANISOU 878 O GLY A 109 11200 9993 11272 -375 -23 787 O
ATOM 879 N CYS A 110 -216.014 49.890 33.933 1.00 72.09 N
ANISOU 879 N CYS A 110 9578 8227 9586 -488 -63 923 N
ATOM 880 CA CYS A 110 -217.428 50.159 34.167 1.00 85.63 C
ANISOU 880 CA CYS A 110 11334 9898 11304 -443 -220 959 C
ATOM 881 C CYS A 110 -218.297 49.375 33.197 1.00 84.63 C
ANISOU 881 C CYS A 110 11326 9801 11028 -459 -253 978 C
ATOM 882 O CYS A 110 -219.357 48.861 33.573 1.00 91.44 O
ANISOU 882 O CYS A 110 12182 10662 11899 -395 -349 956 O
ATOM 883 CB CYS A 110 -217.695 51.659 34.041 1.00 85.95 C
ANISOU 883 CB CYS A 110 11404 9852 11401 -486 -298 1056 C
ATOM 884 SG CYS A 110 -219.257 52.215 34.728 1.00 92.02 S
ANISOU 884 SG CYS A 110 12154 10537 12274 -409 -475 1079 S
ATOM 885 N ASN A 111 -217.860 49.276 31.940 1.00 66.91 N
ANISOU 885 N ASN A 111 9195 7589 8639 -557 -170 1015 N
ATOM 886 CA ASN A 111 -218.593 48.479 30.965 1.00 75.40 C
ANISOU 886 CA ASN A 111 10400 8701 9547 -596 -194 1021 C
ATOM 887 C ASN A 111 -218.409 46.988 31.210 1.00 88.70 C
ANISOU 887 C ASN A 111 12046 10440 11215 -541 -104 895 C
ATOM 888 O ASN A 111 -219.312 46.201 30.916 1.00 96.62 O
ANISOU 888 O ASN A 111 13113 11461 12137 -532 -166 875 O
ATOM 889 CB ASN A 111 -218.149 48.849 29.554 1.00 68.53 C
ANISOU 889 CB ASN A 111 9681 7852 8504 -740 -122 1092 C
ATOM 890 CG ASN A 111 -218.683 50.193 29.112 1.00 85.64 C
ANISOU 890 CG ASN A 111 11923 9955 10660 -803 -259 1248 C
ATOM 891 OD1 ASN A 111 -219.371 50.878 29.868 1.00114.02 O
ANISOU 891 OD1 ASN A 111 15443 13479 14400 -728 -397 1291 O
ATOM 892 ND2 ASN A 111 -218.367 50.581 27.883 1.00 78.69 N
ANISOU 892 ND2 ASN A 111 11193 9093 9613 -945 -215 1333 N
ATOM 893 N LEU A 112 -217.255 46.586 31.747 1.00 88.39 N
ANISOU 893 N LEU A 112 11898 10419 11268 -507 33 816 N
ATOM 894 CA LEU A 112 -217.025 45.180 32.063 1.00 77.49 C
ANISOU 894 CA LEU A 112 10463 9069 9912 -444 113 706 C
ATOM 895 C LEU A 112 -217.898 44.730 33.226 1.00 76.83 C
ANISOU 895 C LEU A 112 10300 8970 9922 -338 -15 681 C
ATOM 896 O LEU A 112 -218.690 43.788 33.094 1.00 86.39 O
ANISOU 896 O LEU A 112 11557 10192 11076 -314 -52 644 O
ATOM 897 CB LEU A 112 -215.547 44.949 32.379 1.00 93.65 C
ANISOU 897 CB LEU A 112 12388 11124 12069 -431 274 646 C
ATOM 898 CG LEU A 112 -214.592 44.836 31.193 1.00 90.16 C
ANISOU 898 CG LEU A 112 12011 10707 11539 -530 467 619 C
ATOM 899 CD1 LEU A 112 -213.185 44.625 31.699 1.00 90.94 C
ANISOU 899 CD1 LEU A 112 11943 10804 11805 -496 609 563 C
ATOM 900 CD2 LEU A 112 -215.009 43.692 30.290 1.00 89.48 C
ANISOU 900 CD2 LEU A 112 12046 10643 11308 -561 539 548 C
ATOM 901 N GLU A 113 -217.755 45.383 34.386 1.00 62.42 N
ANISOU 901 N GLU A 113 8360 7122 8235 -285 -77 695 N
ATOM 902 CA GLU A 113 -218.607 45.046 35.521 1.00 79.01 C
ANISOU 902 CA GLU A 113 10398 9213 10410 -203 -187 671 C
ATOM 903 C GLU A 113 -220.074 45.207 35.156 1.00 77.16 C
ANISOU 903 C GLU A 113 10248 8960 10110 -207 -312 712 C
ATOM 904 O GLU A 113 -220.896 44.329 35.437 1.00 87.79 O
ANISOU 904 O GLU A 113 11595 10316 11445 -164 -360 675 O
ATOM 905 CB GLU A 113 -218.274 45.909 36.737 1.00 72.16 C
ANISOU 905 CB GLU A 113 9421 8323 9673 -175 -231 677 C
ATOM 906 CG GLU A 113 -219.502 46.117 37.627 1.00 81.27 C
ANISOU 906 CG GLU A 113 10557 9453 10871 -127 -355 673 C
ATOM 907 CD GLU A 113 -219.163 46.498 39.046 1.00110.88 C
ANISOU 907 CD GLU A 113 14202 13198 14729 -100 -379 640 C
ATOM 908 OE1 GLU A 113 -217.985 46.796 39.319 1.00127.03 O
ANISOU 908 OE1 GLU A 113 16186 15253 16825 -123 -324 636 O
ATOM 909 OE2 GLU A 113 -220.079 46.492 39.893 1.00124.55 O
ANISOU 909 OE2 GLU A 113 15912 14918 16493 -65 -450 614 O
ATOM 910 N GLY A 114 -220.416 46.325 34.516 1.00 62.09 N
ANISOU 910 N GLY A 114 8404 7018 8169 -261 -371 797 N
ATOM 911 CA GLY A 114 -221.797 46.545 34.127 1.00 73.60 C
ANISOU 911 CA GLY A 114 9924 8449 9591 -265 -508 853 C
ATOM 912 C GLY A 114 -222.344 45.404 33.297 1.00 79.00 C
ANISOU 912 C GLY A 114 10701 9174 10140 -293 -513 831 C
ATOM 913 O GLY A 114 -223.378 44.820 33.629 1.00 78.79 O
ANISOU 913 O GLY A 114 10658 9147 10130 -251 -597 808 O
ATOM 914 N PHE A 115 -221.636 45.052 32.224 1.00 61.88 N
ANISOU 914 N PHE A 115 8634 7044 7836 -373 -410 825 N
ATOM 915 CA PHE A 115 -222.091 43.974 31.353 1.00 78.65 C
ANISOU 915 CA PHE A 115 10866 9205 9813 -421 -400 788 C
ATOM 916 C PHE A 115 -222.267 42.674 32.131 1.00 87.13 C
ANISOU 916 C PHE A 115 11868 10290 10948 -339 -369 682 C
ATOM 917 O PHE A 115 -223.364 42.104 32.173 1.00 91.28 O
ANISOU 917 O PHE A 115 12412 10815 11453 -325 -467 674 O
ATOM 918 CB PHE A 115 -221.107 43.783 30.199 1.00 74.57 C
ANISOU 918 CB PHE A 115 10462 8725 9148 -526 -247 768 C
ATOM 919 CG PHE A 115 -221.474 42.664 29.273 1.00 93.13 C
ANISOU 919 CG PHE A 115 12940 11112 11334 -592 -212 707 C
ATOM 920 CD1 PHE A 115 -222.351 42.879 28.225 1.00 94.22 C
ANISOU 920 CD1 PHE A 115 13230 11267 11303 -698 -329 782 C
ATOM 921 CD2 PHE A 115 -220.942 41.398 29.447 1.00 93.01 C
ANISOU 921 CD2 PHE A 115 12894 11106 11338 -556 -70 576 C
ATOM 922 CE1 PHE A 115 -222.692 41.853 27.371 1.00 98.07 C
ANISOU 922 CE1 PHE A 115 13847 11791 11622 -778 -300 716 C
ATOM 923 CE2 PHE A 115 -221.281 40.369 28.597 1.00 92.13 C
ANISOU 923 CE2 PHE A 115 12908 11018 11081 -624 -28 504 C
ATOM 924 CZ PHE A 115 -222.156 40.596 27.556 1.00 90.75 C
ANISOU 924 CZ PHE A 115 12894 10869 10716 -741 -140 568 C
ATOM 925 N PHE A 116 -221.196 42.196 32.770 1.00 64.30 N
ANISOU 925 N PHE A 116 8885 7402 8142 -288 -240 610 N
ATOM 926 CA PHE A 116 -221.244 40.874 33.389 1.00 73.11 C
ANISOU 926 CA PHE A 116 9947 8520 9313 -222 -203 522 C
ATOM 927 C PHE A 116 -222.215 40.827 34.562 1.00 72.62 C
ANISOU 927 C PHE A 116 9802 8442 9349 -147 -331 531 C
ATOM 928 O PHE A 116 -222.912 39.822 34.750 1.00 81.72 O
ANISOU 928 O PHE A 116 10962 9594 10494 -124 -362 489 O
ATOM 929 CB PHE A 116 -219.843 40.440 33.817 1.00 59.14 C
ANISOU 929 CB PHE A 116 8083 6747 7639 -183 -56 463 C
ATOM 930 CG PHE A 116 -219.026 39.917 32.684 1.00 66.34 C
ANISOU 930 CG PHE A 116 9070 7669 8467 -247 109 406 C
ATOM 931 CD1 PHE A 116 -219.397 38.747 32.042 1.00 77.28 C
ANISOU 931 CD1 PHE A 116 10544 9052 9769 -270 158 330 C
ATOM 932 CD2 PHE A 116 -217.910 40.603 32.236 1.00 59.86 C
ANISOU 932 CD2 PHE A 116 8238 6856 7649 -295 225 419 C
ATOM 933 CE1 PHE A 116 -218.663 38.258 30.981 1.00 81.50 C
ANISOU 933 CE1 PHE A 116 11157 9590 10220 -339 333 256 C
ATOM 934 CE2 PHE A 116 -217.170 40.120 31.175 1.00 62.41 C
ANISOU 934 CE2 PHE A 116 8632 7189 7893 -363 403 352 C
ATOM 935 CZ PHE A 116 -217.546 38.944 30.547 1.00 66.40 C
ANISOU 935 CZ PHE A 116 9229 7690 8310 -386 463 264 C
ATOM 936 N ALA A 117 -222.280 41.895 35.359 1.00 68.46 N
ANISOU 936 N ALA A 117 9198 7898 8913 -118 -395 579 N
ATOM 937 CA ALA A 117 -223.265 41.936 36.434 1.00 73.16 C
ANISOU 937 CA ALA A 117 9725 8480 9594 -62 -497 577 C
ATOM 938 C ALA A 117 -224.682 41.964 35.869 1.00 69.81 C
ANISOU 938 C ALA A 117 9361 8046 9120 -85 -612 612 C
ATOM 939 O ALA A 117 -225.554 41.211 36.318 1.00 66.36 O
ANISOU 939 O ALA A 117 8899 7610 8703 -57 -660 579 O
ATOM 940 CB ALA A 117 -223.015 43.143 37.339 1.00 69.79 C
ANISOU 940 CB ALA A 117 9215 8030 9271 -41 -523 604 C
ATOM 941 N THR A 118 -224.926 42.820 34.872 1.00 74.91 N
ANISOU 941 N THR A 118 10081 8678 9704 -144 -667 687 N
ATOM 942 CA THR A 118 -226.236 42.851 34.228 1.00 74.11 C
ANISOU 942 CA THR A 118 10032 8566 9559 -175 -799 738 C
ATOM 943 C THR A 118 -226.538 41.530 33.529 1.00 73.49 C
ANISOU 943 C THR A 118 10040 8524 9358 -217 -785 689 C
ATOM 944 O THR A 118 -227.666 41.028 33.598 1.00 73.08 O
ANISOU 944 O THR A 118 9979 8471 9318 -212 -880 684 O
ATOM 945 CB THR A 118 -226.305 44.016 33.237 1.00 62.15 C
ANISOU 945 CB THR A 118 8592 7027 7994 -242 -871 849 C
ATOM 946 OG1 THR A 118 -226.193 45.261 33.942 1.00 84.31 O
ANISOU 946 OG1 THR A 118 11313 9779 10942 -199 -895 890 O
ATOM 947 CG2 THR A 118 -227.608 43.993 32.456 1.00 57.19 C
ANISOU 947 CG2 THR A 118 8022 6392 7317 -287 -1031 920 C
ATOM 948 N LEU A 119 -225.541 40.950 32.855 1.00 77.23 N
ANISOU 948 N LEU A 119 10594 9027 9725 -263 -659 642 N
ATOM 949 CA LEU A 119 -225.746 39.673 32.175 1.00 86.37 C
ANISOU 949 CA LEU A 119 11841 10207 10767 -310 -622 574 C
ATOM 950 C LEU A 119 -226.116 38.579 33.168 1.00 82.06 C
ANISOU 950 C LEU A 119 11213 9649 10317 -235 -613 499 C
ATOM 951 O LEU A 119 -227.093 37.849 32.971 1.00 87.27 O
ANISOU 951 O LEU A 119 11906 10310 10942 -257 -685 479 O
ATOM 952 CB LEU A 119 -224.491 39.281 31.395 1.00 83.16 C
ANISOU 952 CB LEU A 119 11517 9820 10261 -364 -450 517 C
ATOM 953 CG LEU A 119 -224.608 38.047 30.500 1.00 82.17 C
ANISOU 953 CG LEU A 119 11512 9709 10000 -435 -386 430 C
ATOM 954 CD1 LEU A 119 -225.362 38.391 29.229 1.00 84.51 C
ANISOU 954 CD1 LEU A 119 11966 10036 10108 -565 -491 491 C
ATOM 955 CD2 LEU A 119 -223.238 37.488 30.173 1.00 81.74 C
ANISOU 955 CD2 LEU A 119 11476 9652 9931 -445 -170 336 C
ATOM 956 N GLY A 120 -225.347 38.461 34.250 1.00 75.13 N
ANISOU 956 N GLY A 120 10227 8759 9558 -156 -534 465 N
ATOM 957 CA GLY A 120 -225.637 37.449 35.252 1.00 84.27 C
ANISOU 957 CA GLY A 120 11313 9904 10802 -94 -530 412 C
ATOM 958 C GLY A 120 -227.021 37.589 35.857 1.00 79.78 C
ANISOU 958 C GLY A 120 10697 9331 10286 -77 -660 439 C
ATOM 959 O GLY A 120 -227.743 36.601 36.009 1.00 89.87 O
ANISOU 959 O GLY A 120 11979 10602 11564 -78 -686 402 O
ATOM 960 N GLY A 121 -227.410 38.814 36.216 1.00 69.45 N
ANISOU 960 N GLY A 121 9334 8015 9037 -62 -734 499 N
ATOM 961 CA GLY A 121 -228.745 39.025 36.749 1.00 79.24 C
ANISOU 961 CA GLY A 121 10513 9243 10353 -45 -841 517 C
ATOM 962 C GLY A 121 -229.831 38.740 35.728 1.00 81.71 C
ANISOU 962 C GLY A 121 10892 9558 10598 -103 -947 544 C
ATOM 963 O GLY A 121 -230.897 38.225 36.070 1.00 65.03 O
ANISOU 963 O GLY A 121 8736 7440 8533 -99 -1010 529 O
ATOM 964 N GLU A 122 -229.578 39.073 34.462 1.00 75.57 N
ANISOU 964 N GLU A 122 10222 8790 9701 -172 -971 589 N
ATOM 965 CA GLU A 122 -230.566 38.823 33.421 1.00 65.85 C
ANISOU 965 CA GLU A 122 9069 7569 8382 -249 -1092 625 C
ATOM 966 C GLU A 122 -230.724 37.332 33.143 1.00 85.86 C
ANISOU 966 C GLU A 122 11669 10121 10835 -287 -1051 540 C
ATOM 967 O GLU A 122 -231.844 36.852 32.927 1.00 77.05 O
ANISOU 967 O GLU A 122 10554 9006 9716 -324 -1157 543 O
ATOM 968 CB GLU A 122 -230.176 39.571 32.148 1.00 73.49 C
ANISOU 968 CB GLU A 122 10157 8549 9216 -333 -1126 702 C
ATOM 969 CG GLU A 122 -230.550 41.042 32.154 1.00 74.52 C
ANISOU 969 CG GLU A 122 10235 8644 9437 -318 -1238 818 C
ATOM 970 CD GLU A 122 -232.048 41.261 32.047 1.00 92.10 C
ANISOU 970 CD GLU A 122 12403 10844 11745 -324 -1426 886 C
ATOM 971 OE1 GLU A 122 -232.646 41.798 33.004 1.00101.11 O
ANISOU 971 OE1 GLU A 122 13400 11940 13076 -241 -1461 894 O
ATOM 972 OE2 GLU A 122 -232.630 40.884 31.006 1.00 95.09 O
ANISOU 972 OE2 GLU A 122 12879 11248 12001 -417 -1535 928 O
ATOM 973 N ILE A 123 -229.613 36.586 33.125 1.00 82.08 N
ANISOU 973 N ILE A 123 11237 9647 10304 -282 -898 462 N
ATOM 974 CA ILE A 123 -229.687 35.141 32.904 1.00 71.71 C
ANISOU 974 CA ILE A 123 9982 8327 8937 -311 -841 370 C
ATOM 975 C ILE A 123 -230.485 34.483 34.020 1.00 72.36 C
ANISOU 975 C ILE A 123 9960 8389 9146 -255 -879 346 C
ATOM 976 O ILE A 123 -231.333 33.617 33.774 1.00 76.44 O
ANISOU 976 O ILE A 123 10507 8899 9637 -300 -932 313 O
ATOM 977 CB ILE A 123 -228.275 34.535 32.785 1.00 70.32 C
ANISOU 977 CB ILE A 123 9845 8139 8734 -297 -657 291 C
ATOM 978 CG1 ILE A 123 -227.556 35.079 31.556 1.00 59.11 C
ANISOU 978 CG1 ILE A 123 8546 6745 7168 -379 -600 302 C
ATOM 979 CG2 ILE A 123 -228.342 33.010 32.693 1.00 55.67 C
ANISOU 979 CG2 ILE A 123 8034 6251 6865 -312 -590 190 C
ATOM 980 CD1 ILE A 123 -226.090 34.715 31.500 1.00 51.56 C
ANISOU 980 CD1 ILE A 123 7594 5773 6224 -355 -403 229 C
ATOM 981 N ALA A 124 -230.228 34.887 35.264 1.00 67.58 N
ANISOU 981 N ALA A 124 9234 7773 8670 -168 -850 360 N
ATOM 982 CA ALA A 124 -231.013 34.380 36.383 1.00 69.16 C
ANISOU 982 CA ALA A 124 9341 7961 8977 -129 -878 345 C
ATOM 983 C ALA A 124 -232.491 34.690 36.190 1.00 78.46 C
ANISOU 983 C ALA A 124 10484 9144 10185 -164 -1018 383 C
ATOM 984 O ALA A 124 -233.347 33.808 36.328 1.00 81.85 O
ANISOU 984 O ALA A 124 10902 9566 10634 -190 -1054 353 O
ATOM 985 CB ALA A 124 -230.501 34.977 37.693 1.00 62.49 C
ANISOU 985 CB ALA A 124 8391 7115 8238 -55 -832 359 C
ATOM 986 N LEU A 125 -232.804 35.943 35.852 1.00 79.47 N
ANISOU 986 N LEU A 125 10586 9275 10332 -166 -1101 454 N
ATOM 987 CA LEU A 125 -234.191 36.345 35.642 1.00 77.59 C
ANISOU 987 CA LEU A 125 10290 9030 10160 -190 -1247 504 C
ATOM 988 C LEU A 125 -234.888 35.440 34.632 1.00 82.02 C
ANISOU 988 C LEU A 125 10937 9605 10622 -281 -1331 495 C
ATOM 989 O LEU A 125 -235.957 34.886 34.910 1.00 73.41 O
ANISOU 989 O LEU A 125 9785 8509 9600 -297 -1395 480 O
ATOM 990 CB LEU A 125 -234.246 37.799 35.179 1.00 73.18 C
ANISOU 990 CB LEU A 125 9715 8458 9632 -185 -1331 597 C
ATOM 991 CG LEU A 125 -235.616 38.236 34.667 1.00 67.56 C
ANISOU 991 CG LEU A 125 8950 7729 8991 -217 -1508 672 C
ATOM 992 CD1 LEU A 125 -236.608 38.225 35.809 1.00 58.18 C
ANISOU 992 CD1 LEU A 125 7598 6516 7994 -160 -1513 641 C
ATOM 993 CD2 LEU A 125 -235.538 39.609 34.027 1.00 80.84 C
ANISOU 993 CD2 LEU A 125 10640 9384 10691 -222 -1601 781 C
ATOM 994 N TRP A 126 -234.290 35.266 33.454 1.00 69.16 N
ANISOU 994 N TRP A 126 9456 7996 8827 -353 -1325 495 N
ATOM 995 CA TRP A 126 -234.952 34.471 32.428 1.00 75.90 C
ANISOU 995 CA TRP A 126 10411 8866 9563 -462 -1412 480 C
ATOM 996 C TRP A 126 -234.911 32.981 32.741 1.00 82.89 C
ANISOU 996 C TRP A 126 11325 9736 10434 -474 -1320 371 C
ATOM 997 O TRP A 126 -235.784 32.234 32.282 1.00 82.71 O
ANISOU 997 O TRP A 126 11337 9715 10374 -553 -1404 348 O
ATOM 998 CB TRP A 126 -234.336 34.766 31.064 1.00 69.48 C
ANISOU 998 CB TRP A 126 9764 8081 8553 -557 -1422 506 C
ATOM 999 CG TRP A 126 -234.700 36.134 30.583 1.00 90.55 C
ANISOU 999 CG TRP A 126 12417 10756 11233 -575 -1567 640 C
ATOM 1000 CD1 TRP A 126 -233.892 37.230 30.540 1.00104.81 C
ANISOU 1000 CD1 TRP A 126 14228 12556 13038 -542 -1527 700 C
ATOM 1001 CD2 TRP A 126 -235.982 36.560 30.109 1.00 90.33 C
ANISOU 1001 CD2 TRP A 126 12352 10729 11242 -627 -1786 740 C
ATOM 1002 NE1 TRP A 126 -234.587 38.310 30.052 1.00103.91 N
ANISOU 1002 NE1 TRP A 126 14093 12432 12957 -570 -1704 834 N
ATOM 1003 CE2 TRP A 126 -235.873 37.925 29.781 1.00 92.52 C
ANISOU 1003 CE2 TRP A 126 12617 10991 11544 -619 -1871 865 C
ATOM 1004 CE3 TRP A 126 -237.210 35.917 29.923 1.00 93.53 C
ANISOU 1004 CE3 TRP A 126 12724 11138 11675 -684 -1925 741 C
ATOM 1005 CZ2 TRP A 126 -236.946 38.660 29.276 1.00 94.93 C
ANISOU 1005 CZ2 TRP A 126 12875 11280 11912 -657 -2098 999 C
ATOM 1006 CZ3 TRP A 126 -238.273 36.647 29.421 1.00 92.39 C
ANISOU 1006 CZ3 TRP A 126 12525 10988 11592 -726 -2150 869 C
ATOM 1007 CH2 TRP A 126 -238.134 38.005 29.104 1.00 90.54 C
ANISOU 1007 CH2 TRP A 126 12276 10733 11392 -708 -2238 1001 C
ATOM 1008 N SER A 127 -233.923 32.525 33.518 1.00 75.65 N
ANISOU 1008 N SER A 127 10389 8797 9557 -401 -1159 309 N
ATOM 1009 CA SER A 127 -233.917 31.128 33.941 1.00 83.01 C
ANISOU 1009 CA SER A 127 11333 9695 10512 -401 -1081 222 C
ATOM 1010 C SER A 127 -235.133 30.817 34.805 1.00 82.28 C
ANISOU 1010 C SER A 127 11124 9592 10545 -389 -1157 234 C
ATOM 1011 O SER A 127 -235.757 29.761 34.654 1.00 75.71 O
ANISOU 1011 O SER A 127 10322 8741 9704 -447 -1179 186 O
ATOM 1012 CB SER A 127 -232.624 30.801 34.687 1.00 70.67 C
ANISOU 1012 CB SER A 127 9751 8103 8998 -318 -919 180 C
ATOM 1013 OG SER A 127 -231.530 30.720 33.788 1.00 73.91 O
ANISOU 1013 OG SER A 127 10272 8511 9301 -344 -820 139 O
ATOM 1014 N LEU A 128 -235.490 31.732 35.710 1.00 71.15 N
ANISOU 1014 N LEU A 128 9584 8194 9257 -323 -1188 290 N
ATOM 1015 CA LEU A 128 -236.719 31.570 36.481 1.00 70.89 C
ANISOU 1015 CA LEU A 128 9432 8156 9349 -322 -1248 298 C
ATOM 1016 C LEU A 128 -237.939 31.554 35.570 1.00 80.47 C
ANISOU 1016 C LEU A 128 10645 9379 10550 -407 -1407 327 C
ATOM 1017 O LEU A 128 -238.884 30.790 35.795 1.00 91.24 O
ANISOU 1017 O LEU A 128 11963 10733 11971 -449 -1447 302 O
ATOM 1018 CB LEU A 128 -236.843 32.684 37.519 1.00 53.60 C
ANISOU 1018 CB LEU A 128 7108 5971 7288 -244 -1235 338 C
ATOM 1019 CG LEU A 128 -235.776 32.691 38.610 1.00 74.95 C
ANISOU 1019 CG LEU A 128 9796 8671 10010 -175 -1099 314 C
ATOM 1020 CD1 LEU A 128 -236.212 33.561 39.784 1.00 76.75 C
ANISOU 1020 CD1 LEU A 128 9894 8904 10365 -128 -1083 327 C
ATOM 1021 CD2 LEU A 128 -235.494 31.267 39.053 1.00 76.63 C
ANISOU 1021 CD2 LEU A 128 10051 8862 10201 -189 -1023 262 C
ATOM 1022 N VAL A 129 -237.929 32.388 34.532 1.00 63.62 N
ANISOU 1022 N VAL A 129 8563 7265 8343 -442 -1507 388 N
ATOM 1023 CA VAL A 129 -239.021 32.394 33.568 1.00 76.23 C
ANISOU 1023 CA VAL A 129 10173 8877 9914 -537 -1687 435 C
ATOM 1024 C VAL A 129 -239.058 31.086 32.783 1.00 79.47 C
ANISOU 1024 C VAL A 129 10724 9290 10180 -646 -1688 361 C
ATOM 1025 O VAL A 129 -240.123 30.486 32.606 1.00 77.66 O
ANISOU 1025 O VAL A 129 10463 9060 9984 -717 -1791 353 O
ATOM 1026 CB VAL A 129 -238.893 33.608 32.633 1.00 65.81 C
ANISOU 1026 CB VAL A 129 8896 7574 8533 -559 -1802 536 C
ATOM 1027 CG1 VAL A 129 -239.988 33.574 31.593 1.00 63.56 C
ANISOU 1027 CG1 VAL A 129 8634 7307 8209 -672 -2014 600 C
ATOM 1028 CG2 VAL A 129 -238.945 34.897 33.432 1.00 56.06 C
ANISOU 1028 CG2 VAL A 129 7514 6315 7469 -452 -1801 600 C
ATOM 1029 N VAL A 130 -237.901 30.626 32.301 1.00 66.80 N
ANISOU 1029 N VAL A 130 9270 7684 8427 -664 -1566 298 N
ATOM 1030 CA VAL A 130 -237.854 29.411 31.492 1.00 78.42 C
ANISOU 1030 CA VAL A 130 10890 9145 9760 -773 -1543 207 C
ATOM 1031 C VAL A 130 -238.235 28.190 32.327 1.00 84.68 C
ANISOU 1031 C VAL A 130 11628 9890 10655 -758 -1478 132 C
ATOM 1032 O VAL A 130 -238.967 27.309 31.860 1.00 68.36 O
ANISOU 1032 O VAL A 130 9610 7812 8550 -860 -1543 86 O
ATOM 1033 CB VAL A 130 -236.463 29.264 30.845 1.00 78.69 C
ANISOU 1033 CB VAL A 130 11081 9178 9641 -785 -1395 145 C
ATOM 1034 CG1 VAL A 130 -236.218 27.835 30.377 1.00 60.79 C
ANISOU 1034 CG1 VAL A 130 8943 6870 7285 -862 -1299 13 C
ATOM 1035 CG2 VAL A 130 -236.322 30.231 29.672 1.00 67.67 C
ANISOU 1035 CG2 VAL A 130 9788 7835 8088 -864 -1487 215 C
ATOM 1036 N LEU A 131 -237.767 28.123 33.576 1.00 68.70 N
ANISOU 1036 N LEU A 131 9508 7838 8758 -645 -1358 124 N
ATOM 1037 CA LEU A 131 -238.172 27.022 34.442 1.00 75.27 C
ANISOU 1037 CA LEU A 131 10287 8623 9689 -638 -1306 76 C
ATOM 1038 C LEU A 131 -239.684 27.006 34.634 1.00 84.54 C
ANISOU 1038 C LEU A 131 11351 9812 10957 -692 -1443 111 C
ATOM 1039 O LEU A 131 -240.303 25.936 34.664 1.00 88.97 O
ANISOU 1039 O LEU A 131 11924 10341 11539 -760 -1455 61 O
ATOM 1040 CB LEU A 131 -237.455 27.114 35.791 1.00 53.97 C
ANISOU 1040 CB LEU A 131 7504 5904 7098 -521 -1179 87 C
ATOM 1041 CG LEU A 131 -237.770 25.985 36.778 1.00 70.33 C
ANISOU 1041 CG LEU A 131 9532 7925 9264 -519 -1120 56 C
ATOM 1042 CD1 LEU A 131 -237.542 24.633 36.131 1.00 68.67 C
ANISOU 1042 CD1 LEU A 131 9448 7649 8994 -585 -1074 -29 C
ATOM 1043 CD2 LEU A 131 -236.929 26.116 38.025 1.00 68.99 C
ANISOU 1043 CD2 LEU A 131 9304 7743 9166 -420 -1011 81 C
ATOM 1044 N ALA A 132 -240.297 28.187 34.757 1.00 79.94 N
ANISOU 1044 N ALA A 132 10652 9269 10450 -662 -1546 194 N
ATOM 1045 CA ALA A 132 -241.748 28.260 34.895 1.00 70.52 C
ANISOU 1045 CA ALA A 132 9328 8086 9379 -707 -1678 230 C
ATOM 1046 C ALA A 132 -242.446 27.755 33.642 1.00 84.64 C
ANISOU 1046 C ALA A 132 11202 9887 11071 -844 -1830 224 C
ATOM 1047 O ALA A 132 -243.473 27.072 33.723 1.00 90.25 O
ANISOU 1047 O ALA A 132 11852 10587 11854 -915 -1899 206 O
ATOM 1048 CB ALA A 132 -242.177 29.695 35.195 1.00 64.98 C
ANISOU 1048 CB ALA A 132 8481 7407 8802 -638 -1751 318 C
ATOM 1049 N ILE A 133 -241.909 28.091 32.470 1.00 76.35 N
ANISOU 1049 N ILE A 133 10296 8862 9850 -898 -1885 238 N
ATOM 1050 CA ILE A 133 -242.503 27.622 31.226 1.00 73.35 C
ANISOU 1050 CA ILE A 133 10027 8503 9339 -1052 -2036 229 C
ATOM 1051 C ILE A 133 -242.319 26.117 31.080 1.00 85.86 C
ANISOU 1051 C ILE A 133 11733 10045 10844 -1130 -1940 102 C
ATOM 1052 O ILE A 133 -243.238 25.404 30.661 1.00 91.11 O
ANISOU 1052 O ILE A 133 12410 10707 11500 -1249 -2050 76 O
ATOM 1053 CB ILE A 133 -241.904 28.379 30.030 1.00 66.50 C
ANISOU 1053 CB ILE A 133 9307 7679 8281 -1106 -2103 277 C
ATOM 1054 CG1 ILE A 133 -242.115 29.880 30.198 1.00 79.90 C
ANISOU 1054 CG1 ILE A 133 10878 9398 10084 -1026 -2204 413 C
ATOM 1055 CG2 ILE A 133 -242.533 27.903 28.734 1.00 70.64 C
ANISOU 1055 CG2 ILE A 133 9964 8235 8642 -1290 -2271 271 C
ATOM 1056 CD1 ILE A 133 -241.504 30.704 29.087 1.00 73.23 C
ANISOU 1056 CD1 ILE A 133 10176 8591 9057 -1080 -2270 482 C
ATOM 1057 N GLU A 134 -241.129 25.613 31.417 1.00 77.94 N
ANISOU 1057 N GLU A 134 10815 9000 9797 -1066 -1740 23 N
ATOM 1058 CA GLU A 134 -240.872 24.182 31.306 1.00 75.91 C
ANISOU 1058 CA GLU A 134 10670 8678 9494 -1126 -1634 -100 C
ATOM 1059 C GLU A 134 -241.808 23.390 32.210 1.00 84.56 C
ANISOU 1059 C GLU A 134 11645 9732 10753 -1132 -1647 -111 C
ATOM 1060 O GLU A 134 -242.448 22.426 31.771 1.00 69.28 O
ANISOU 1060 O GLU A 134 9766 7766 8790 -1252 -1698 -173 O
ATOM 1061 CB GLU A 134 -239.409 23.883 31.640 1.00 80.09 C
ANISOU 1061 CB GLU A 134 11271 9157 10004 -1031 -1419 -164 C
ATOM 1062 CG GLU A 134 -238.411 24.450 30.637 1.00 77.93 C
ANISOU 1062 CG GLU A 134 11137 8916 9556 -1050 -1372 -181 C
ATOM 1063 CD GLU A 134 -236.973 24.115 30.980 1.00 90.43 C
ANISOU 1063 CD GLU A 134 12762 10441 11154 -954 -1155 -248 C
ATOM 1064 OE1 GLU A 134 -236.720 23.626 32.104 1.00106.96 O
ANISOU 1064 OE1 GLU A 134 14762 12477 13400 -855 -1066 -250 O
ATOM 1065 OE2 GLU A 134 -236.093 24.337 30.119 1.00 95.96 O
ANISOU 1065 OE2 GLU A 134 13589 11155 11717 -983 -1077 -292 O
ATOM 1066 N ARG A 135 -241.921 23.802 33.475 1.00 74.46 N
ANISOU 1066 N ARG A 135 10202 8451 9637 -1018 -1598 -52 N
ATOM 1067 CA ARG A 135 -242.812 23.110 34.401 1.00 80.23 C
ANISOU 1067 CA ARG A 135 10816 9149 10518 -1032 -1594 -56 C
ATOM 1068 C ARG A 135 -244.263 23.189 33.938 1.00 82.79 C
ANISOU 1068 C ARG A 135 11056 9509 10892 -1141 -1781 -24 C
ATOM 1069 O ARG A 135 -245.029 22.235 34.109 1.00 84.47 O
ANISOU 1069 O ARG A 135 11243 9685 11165 -1223 -1801 -63 O
ATOM 1070 CB ARG A 135 -242.656 23.689 35.806 1.00 64.95 C
ANISOU 1070 CB ARG A 135 8735 7222 8722 -906 -1504 0 C
ATOM 1071 CG ARG A 135 -241.325 23.346 36.467 1.00 68.56 C
ANISOU 1071 CG ARG A 135 9257 7633 9160 -813 -1331 -25 C
ATOM 1072 CD ARG A 135 -241.064 24.219 37.691 1.00 64.27 C
ANISOU 1072 CD ARG A 135 8590 7121 8709 -702 -1267 38 C
ATOM 1073 NE ARG A 135 -239.986 23.690 38.525 1.00 75.71 N
ANISOU 1073 NE ARG A 135 10079 8522 10166 -633 -1126 28 N
ATOM 1074 CZ ARG A 135 -239.487 24.315 39.586 1.00 73.15 C
ANISOU 1074 CZ ARG A 135 9685 8221 9888 -547 -1059 74 C
ATOM 1075 NH1 ARG A 135 -239.959 25.502 39.940 1.00 69.93 N
ANISOU 1075 NH1 ARG A 135 9167 7875 9528 -516 -1098 116 N
ATOM 1076 NH2 ARG A 135 -238.511 23.760 40.288 1.00 86.56 N
ANISOU 1076 NH2 ARG A 135 11422 9874 11594 -498 -958 77 N
ATOM 1077 N TYR A 136 -244.656 24.313 33.339 1.00 85.09 N
ANISOU 1077 N TYR A 136 11297 9864 11170 -1146 -1929 55 N
ATOM 1078 CA TYR A 136 -246.029 24.449 32.863 1.00 86.30 C
ANISOU 1078 CA TYR A 136 11349 10048 11392 -1246 -2132 103 C
ATOM 1079 C TYR A 136 -246.307 23.509 31.699 1.00 88.57 C
ANISOU 1079 C TYR A 136 11795 10329 11528 -1416 -2232 39 C
ATOM 1080 O TYR A 136 -247.408 22.956 31.591 1.00102.91 O
ANISOU 1080 O TYR A 136 13541 12141 13418 -1521 -2346 33 O
ATOM 1081 CB TYR A 136 -246.303 25.901 32.462 1.00 77.94 C
ANISOU 1081 CB TYR A 136 10203 9044 10368 -1207 -2279 218 C
ATOM 1082 CG TYR A 136 -247.509 26.086 31.568 1.00 76.37 C
ANISOU 1082 CG TYR A 136 9945 8878 10194 -1329 -2533 285 C
ATOM 1083 CD1 TYR A 136 -248.784 26.191 32.103 1.00 97.04 C
ANISOU 1083 CD1 TYR A 136 12337 11492 13043 -1334 -2625 329 C
ATOM 1084 CD2 TYR A 136 -247.370 26.169 30.186 1.00 79.05 C
ANISOU 1084 CD2 TYR A 136 10454 9255 10329 -1449 -2683 306 C
ATOM 1085 CE1 TYR A 136 -249.889 26.362 31.287 1.00107.56 C
ANISOU 1085 CE1 TYR A 136 13596 12851 14423 -1446 -2876 401 C
ATOM 1086 CE2 TYR A 136 -248.472 26.340 29.362 1.00 87.63 C
ANISOU 1086 CE2 TYR A 136 11489 10375 11432 -1574 -2944 383 C
ATOM 1087 CZ TYR A 136 -249.727 26.437 29.919 1.00 95.67 C
ANISOU 1087 CZ TYR A 136 12264 11384 12704 -1567 -3047 435 C
ATOM 1088 OH TYR A 136 -250.823 26.610 29.107 1.00 99.21 O
ANISOU 1088 OH TYR A 136 12641 11862 13192 -1690 -3324 522 O
ATOM 1089 N VAL A 137 -245.330 23.327 30.808 1.00 85.85 N
ANISOU 1089 N VAL A 137 11664 9985 10971 -1456 -2185 -18 N
ATOM 1090 CA VAL A 137 -245.523 22.436 29.667 1.00 94.87 C
ANISOU 1090 CA VAL A 137 12983 11120 11942 -1633 -2259 -101 C
ATOM 1091 C VAL A 137 -245.614 20.989 30.131 1.00100.28 C
ANISOU 1091 C VAL A 137 13702 11718 12681 -1675 -2140 -217 C
ATOM 1092 O VAL A 137 -246.455 20.216 29.653 1.00115.75 O
ANISOU 1092 O VAL A 137 15691 13664 14624 -1824 -2247 -262 O
ATOM 1093 CB VAL A 137 -244.388 22.633 28.642 1.00 79.19 C
ANISOU 1093 CB VAL A 137 11222 9153 9714 -1667 -2199 -148 C
ATOM 1094 CG1 VAL A 137 -244.501 21.626 27.508 1.00 78.35 C
ANISOU 1094 CG1 VAL A 137 11323 9032 9414 -1862 -2237 -265 C
ATOM 1095 CG2 VAL A 137 -244.417 24.039 28.090 1.00 67.68 C
ANISOU 1095 CG2 VAL A 137 9742 7778 8196 -1654 -2345 -17 C
ATOM 1096 N VAL A 138 -244.765 20.607 31.085 1.00 88.20 N
ANISOU 1096 N VAL A 138 12165 10123 11226 -1550 -1929 -257 N
ATOM 1097 CA VAL A 138 -244.705 19.223 31.532 1.00 79.54 C
ANISOU 1097 CA VAL A 138 11113 8924 10185 -1581 -1807 -355 C
ATOM 1098 C VAL A 138 -245.961 18.845 32.313 1.00 92.98 C
ANISOU 1098 C VAL A 138 12645 10616 12069 -1619 -1878 -316 C
ATOM 1099 O VAL A 138 -246.503 17.745 32.145 1.00 93.09 O
ANISOU 1099 O VAL A 138 12703 10569 12099 -1737 -1894 -388 O
ATOM 1100 CB VAL A 138 -243.424 19.005 32.355 1.00 70.37 C
ANISOU 1100 CB VAL A 138 9977 7695 9065 -1432 -1586 -380 C
ATOM 1101 CG1 VAL A 138 -243.422 17.628 32.981 1.00 92.80 C
ANISOU 1101 CG1 VAL A 138 12839 10417 12004 -1450 -1475 -449 C
ATOM 1102 CG2 VAL A 138 -242.193 19.197 31.468 1.00 60.72 C
ANISOU 1102 CG2 VAL A 138 8928 6471 7673 -1418 -1499 -443 C
ATOM 1103 N VAL A 139 -246.458 19.745 33.159 1.00 84.29 N
ANISOU 1103 N VAL A 139 11345 9568 11112 -1528 -1912 -211 N
ATOM 1104 CA VAL A 139 -247.625 19.428 33.981 1.00 83.23 C
ANISOU 1104 CA VAL A 139 11034 9425 11163 -1562 -1947 -180 C
ATOM 1105 C VAL A 139 -248.917 19.622 33.196 1.00 91.82 C
ANISOU 1105 C VAL A 139 12042 10566 12279 -1695 -2174 -148 C
ATOM 1106 O VAL A 139 -249.688 18.678 32.994 1.00 97.10 O
ANISOU 1106 O VAL A 139 12713 11199 12980 -1829 -2233 -196 O
ATOM 1107 CB VAL A 139 -247.624 20.269 35.270 1.00 79.54 C
ANISOU 1107 CB VAL A 139 10389 8988 10846 -1419 -1861 -100 C
ATOM 1108 CG1 VAL A 139 -248.926 20.058 36.033 1.00 77.38 C
ANISOU 1108 CG1 VAL A 139 9920 8717 10764 -1469 -1893 -73 C
ATOM 1109 CG2 VAL A 139 -246.436 19.893 36.130 1.00 74.90 C
ANISOU 1109 CG2 VAL A 139 9876 8344 10239 -1313 -1658 -124 C
ATOM 1110 N CYS A 140 -249.178 20.852 32.750 1.00 86.92 N
ANISOU 1110 N CYS A 140 11343 10024 11660 -1665 -2315 -59 N
ATOM 1111 CA CYS A 140 -250.453 21.173 32.119 1.00 84.79 C
ANISOU 1111 CA CYS A 140 10954 9803 11460 -1775 -2554 2 C
ATOM 1112 C CYS A 140 -250.635 20.519 30.756 1.00 94.07 C
ANISOU 1112 C CYS A 140 12310 10986 12448 -1961 -2707 -51 C
ATOM 1113 O CYS A 140 -251.763 20.505 30.253 1.00112.89 O
ANISOU 1113 O CYS A 140 14601 13402 14891 -2085 -2918 -10 O
ATOM 1114 CB CYS A 140 -250.604 22.689 31.987 1.00 94.63 C
ANISOU 1114 CB CYS A 140 12072 11113 12769 -1685 -2671 124 C
ATOM 1115 SG CYS A 140 -250.507 23.572 33.559 1.00109.21 S
ANISOU 1115 SG CYS A 140 13701 12952 14841 -1485 -2498 172 S
ATOM 1116 N LYS A 141 -249.572 19.983 30.159 1.00 95.08 N
ANISOU 1116 N LYS A 141 12684 11084 12358 -1991 -2605 -146 N
ATOM 1117 CA LYS A 141 -249.637 19.289 28.877 1.00102.07 C
ANISOU 1117 CA LYS A 141 13775 11971 13036 -2182 -2711 -227 C
ATOM 1118 C LYS A 141 -250.440 20.067 27.827 1.00109.17 C
ANISOU 1118 C LYS A 141 14650 12963 13866 -2301 -3004 -127 C
ATOM 1119 O LYS A 141 -251.479 19.592 27.361 1.00128.64 O
ANISOU 1119 O LYS A 141 17081 15441 16354 -2463 -3187 -128 O
ATOM 1120 CB LYS A 141 -250.208 17.889 29.058 1.00 96.71 C
ANISOU 1120 CB LYS A 141 13116 11215 12416 -2303 -2679 -331 C
ATOM 1121 CG LYS A 141 -249.398 16.992 29.982 1.00 99.81 C
ANISOU 1121 CG LYS A 141 13559 11498 12865 -2207 -2411 -422 C
ATOM 1122 CD LYS A 141 -250.087 15.656 30.225 1.00111.84 C
ANISOU 1122 CD LYS A 141 15081 12934 14478 -2330 -2394 -504 C
ATOM 1123 CE LYS A 141 -249.311 14.803 31.219 1.00118.83 C
ANISOU 1123 CE LYS A 141 16004 13702 15446 -2229 -2145 -564 C
ATOM 1124 NZ LYS A 141 -250.061 13.570 31.583 1.00134.22 N
ANISOU 1124 NZ LYS A 141 17927 15558 17511 -2344 -2131 -620 N
ATOM 1125 N PRO A 142 -249.987 21.266 27.445 1.00112.43 N
ANISOU 1125 N PRO A 142 15077 13439 14204 -2231 -3065 -29 N
ATOM 1126 CA PRO A 142 -250.753 22.048 26.462 1.00110.49 C
ANISOU 1126 CA PRO A 142 14804 13274 13903 -2344 -3365 95 C
ATOM 1127 C PRO A 142 -250.575 21.580 25.031 1.00112.24 C
ANISOU 1127 C PRO A 142 15299 13532 13814 -2561 -3482 32 C
ATOM 1128 O PRO A 142 -251.376 21.970 24.171 1.00130.99 O
ANISOU 1128 O PRO A 142 17665 15973 16133 -2704 -3766 131 O
ATOM 1129 CB PRO A 142 -250.209 23.469 26.648 1.00106.10 C
ANISOU 1129 CB PRO A 142 14180 12753 13381 -2183 -3358 220 C
ATOM 1130 CG PRO A 142 -248.801 23.259 27.083 1.00 96.95 C
ANISOU 1130 CG PRO A 142 13160 11553 12124 -2064 -3066 119 C
ATOM 1131 CD PRO A 142 -248.787 21.989 27.904 1.00112.42 C
ANISOU 1131 CD PRO A 142 15106 13433 14175 -2051 -2879 -12 C
ATOM 1132 N MET A 143 -249.562 20.768 24.744 1.00113.38 N
ANISOU 1132 N MET A 143 15684 13634 13761 -2597 -3274 -127 N
ATOM 1133 CA MET A 143 -249.336 20.232 23.410 1.00127.18 C
ANISOU 1133 CA MET A 143 17713 15409 15199 -2818 -3338 -223 C
ATOM 1134 C MET A 143 -249.721 18.757 23.378 1.00145.63 C
ANISOU 1134 C MET A 143 20127 17673 17533 -2956 -3285 -387 C
ATOM 1135 O MET A 143 -249.451 18.013 24.326 1.00146.60 O
ANISOU 1135 O MET A 143 20189 17699 17813 -2848 -3070 -476 O
ATOM 1136 CB MET A 143 -247.879 20.441 22.984 1.00111.69 C
ANISOU 1136 CB MET A 143 15976 13447 13014 -2773 -3128 -299 C
ATOM 1137 CG MET A 143 -247.545 21.918 22.764 1.00120.91 C
ANISOU 1137 CG MET A 143 17107 14695 14141 -2687 -3217 -131 C
ATOM 1138 SD MET A 143 -245.851 22.308 22.265 1.00121.00 S
ANISOU 1138 SD MET A 143 17355 14714 13904 -2639 -2974 -201 S
ATOM 1139 CE MET A 143 -244.954 22.038 23.791 1.00 97.69 C
ANISOU 1139 CE MET A 143 14258 11659 11202 -2366 -2647 -270 C
ATOM 1140 N SER A 144 -250.361 18.346 22.280 1.00155.64 N
ANISOU 1140 N SER A 144 21534 18985 18619 -3204 -3491 -421 N
ATOM 1141 CA SER A 144 -251.022 17.044 22.228 1.00168.53 C
ANISOU 1141 CA SER A 144 23199 20552 20281 -3361 -3507 -552 C
ATOM 1142 C SER A 144 -250.034 15.902 22.431 1.00166.41 C
ANISOU 1142 C SER A 144 23112 20162 19955 -3337 -3186 -768 C
ATOM 1143 O SER A 144 -250.171 15.102 23.364 1.00168.68 O
ANISOU 1143 O SER A 144 23292 20345 20452 -3261 -3047 -828 O
ATOM 1144 CB SER A 144 -251.761 16.891 20.897 1.00185.58 C
ANISOU 1144 CB SER A 144 25510 22791 22210 -3652 -3794 -554 C
ATOM 1145 OG SER A 144 -250.898 17.153 19.804 1.00194.67 O
ANISOU 1145 OG SER A 144 26951 23996 23019 -3758 -3764 -609 O
ATOM 1146 N ASN A 145 -249.034 15.802 21.558 1.00160.30 N
ANISOU 1146 N ASN A 145 22609 19390 18906 -3408 -3063 -885 N
ATOM 1147 CA ASN A 145 -248.042 14.728 21.604 1.00155.70 C
ANISOU 1147 CA ASN A 145 22207 18680 18272 -3394 -2755 -1102 C
ATOM 1148 C ASN A 145 -246.666 15.369 21.748 1.00147.00 C
ANISOU 1148 C ASN A 145 21162 17577 17115 -3214 -2530 -1102 C
ATOM 1149 O ASN A 145 -245.931 15.518 20.770 1.00151.97 O
ANISOU 1149 O ASN A 145 22020 18242 17480 -3310 -2463 -1185 O
ATOM 1150 CB ASN A 145 -248.128 13.839 20.348 1.00165.26 C
ANISOU 1150 CB ASN A 145 23705 19877 19209 -3677 -2785 -1288 C
ATOM 1151 CG ASN A 145 -249.514 13.258 20.133 1.00170.34 C
ANISOU 1151 CG ASN A 145 24293 20532 19896 -3878 -3037 -1281 C
ATOM 1152 OD1 ASN A 145 -250.262 13.027 21.084 1.00170.35 O
ANISOU 1152 OD1 ASN A 145 24058 20490 20177 -3795 -3086 -1209 O
ATOM 1153 ND2 ASN A 145 -249.862 13.014 18.874 1.00172.43 N
ANISOU 1153 ND2 ASN A 145 24779 20858 19877 -4157 -3198 -1359 N
ATOM 1154 N PHE A 146 -246.317 15.746 22.978 1.00131.93 N
ANISOU 1154 N PHE A 146 19046 15630 15451 -2964 -2409 -1012 N
ATOM 1155 CA PHE A 146 -245.045 16.395 23.262 1.00111.59 C
ANISOU 1155 CA PHE A 146 16484 13052 12862 -2781 -2208 -995 C
ATOM 1156 C PHE A 146 -244.370 15.734 24.457 1.00107.06 C
ANISOU 1156 C PHE A 146 15815 12343 12519 -2587 -1954 -1052 C
ATOM 1157 O PHE A 146 -245.029 15.391 25.444 1.00106.79 O
ANISOU 1157 O PHE A 146 15601 12262 12712 -2520 -1984 -998 O
ATOM 1158 CB PHE A 146 -245.228 17.894 23.537 1.00108.17 C
ANISOU 1158 CB PHE A 146 15886 12735 12477 -2665 -2357 -780 C
ATOM 1159 CG PHE A 146 -243.934 18.650 23.660 1.00103.90 C
ANISOU 1159 CG PHE A 146 15382 12207 11890 -2510 -2176 -761 C
ATOM 1160 CD1 PHE A 146 -243.240 19.047 22.529 1.00110.48 C
ANISOU 1160 CD1 PHE A 146 16430 13099 12448 -2613 -2150 -802 C
ATOM 1161 CD2 PHE A 146 -243.413 18.964 24.903 1.00102.94 C
ANISOU 1161 CD2 PHE A 146 15082 12041 11991 -2275 -2032 -701 C
ATOM 1162 CE1 PHE A 146 -242.050 19.741 22.636 1.00114.87 C
ANISOU 1162 CE1 PHE A 146 17009 13665 12971 -2479 -1978 -785 C
ATOM 1163 CE2 PHE A 146 -242.222 19.659 25.016 1.00104.97 C
ANISOU 1163 CE2 PHE A 146 15364 12309 12212 -2142 -1876 -682 C
ATOM 1164 CZ PHE A 146 -241.540 20.047 23.881 1.00106.09 C
ANISOU 1164 CZ PHE A 146 15707 12506 12098 -2241 -1846 -725 C
ATOM 1165 N ARG A 147 -243.052 15.565 24.356 1.00100.77 N
ANISOU 1165 N ARG A 147 15137 11484 11666 -2505 -1708 -1156 N
ATOM 1166 CA ARG A 147 -242.221 15.033 25.429 1.00116.23 C
ANISOU 1166 CA ARG A 147 17012 13313 13836 -2313 -1473 -1193 C
ATOM 1167 C ARG A 147 -241.007 15.934 25.604 1.00112.36 C
ANISOU 1167 C ARG A 147 16506 12857 13327 -2149 -1335 -1143 C
ATOM 1168 O ARG A 147 -240.268 16.176 24.645 1.00117.44 O
ANISOU 1168 O ARG A 147 17319 13532 13770 -2213 -1253 -1223 O
ATOM 1169 CB ARG A 147 -241.775 13.597 25.131 1.00125.25 C
ANISOU 1169 CB ARG A 147 18313 14296 14981 -2386 -1284 -1405 C
ATOM 1170 CG ARG A 147 -240.743 13.044 26.105 1.00139.49 C
ANISOU 1170 CG ARG A 147 20050 15953 16999 -2189 -1040 -1439 C
ATOM 1171 CD ARG A 147 -241.377 12.607 27.417 1.00149.47 C
ANISOU 1171 CD ARG A 147 21122 17151 18519 -2097 -1082 -1340 C
ATOM 1172 NE ARG A 147 -240.381 12.106 28.361 1.00152.17 N
ANISOU 1172 NE ARG A 147 21403 17356 19059 -1917 -876 -1347 N
ATOM 1173 CZ ARG A 147 -239.946 12.783 29.420 1.00151.63 C
ANISOU 1173 CZ ARG A 147 21173 17319 19120 -1731 -850 -1203 C
ATOM 1174 NH1 ARG A 147 -240.426 13.991 29.682 1.00147.68 N
ANISOU 1174 NH1 ARG A 147 20553 16974 18584 -1694 -998 -1054 N
ATOM 1175 NH2 ARG A 147 -239.035 12.247 30.222 1.00152.71 N
ANISOU 1175 NH2 ARG A 147 21266 17327 19431 -1587 -683 -1206 N
ATOM 1176 N PHE A 148 -240.798 16.419 26.828 1.00 98.52 N
ANISOU 1176 N PHE A 148 14555 11101 11777 -1950 -1301 -1017 N
ATOM 1177 CA PHE A 148 -239.701 17.342 27.100 1.00100.76 C
ANISOU 1177 CA PHE A 148 14799 11421 12063 -1794 -1190 -955 C
ATOM 1178 C PHE A 148 -238.377 16.589 27.129 1.00100.08 C
ANISOU 1178 C PHE A 148 14800 11208 12016 -1719 -923 -1094 C
ATOM 1179 O PHE A 148 -238.157 15.734 27.994 1.00110.07 O
ANISOU 1179 O PHE A 148 15996 12349 13476 -1629 -815 -1122 O
ATOM 1180 CB PHE A 148 -239.937 18.064 28.423 1.00 99.84 C
ANISOU 1180 CB PHE A 148 14449 11337 12146 -1624 -1243 -789 C
ATOM 1181 CG PHE A 148 -238.912 19.116 28.728 1.00 92.49 C
ANISOU 1181 CG PHE A 148 13468 10454 11219 -1475 -1159 -714 C
ATOM 1182 CD1 PHE A 148 -238.875 20.294 27.999 1.00 87.75 C
ANISOU 1182 CD1 PHE A 148 12905 9970 10466 -1511 -1257 -643 C
ATOM 1183 CD2 PHE A 148 -237.989 18.932 29.747 1.00 96.56 C
ANISOU 1183 CD2 PHE A 148 13900 10896 11895 -1309 -993 -706 C
ATOM 1184 CE1 PHE A 148 -237.934 21.268 28.274 1.00 84.79 C
ANISOU 1184 CE1 PHE A 148 12484 9632 10101 -1384 -1178 -576 C
ATOM 1185 CE2 PHE A 148 -237.043 19.903 30.030 1.00 96.20 C
ANISOU 1185 CE2 PHE A 148 13803 10895 11855 -1184 -924 -639 C
ATOM 1186 CZ PHE A 148 -237.016 21.073 29.292 1.00 88.65 C
ANISOU 1186 CZ PHE A 148 12884 10051 10749 -1221 -1009 -580 C
ATOM 1187 N GLY A 149 -237.487 16.916 26.191 1.00 90.92 N
ANISOU 1187 N GLY A 149 13787 10077 10683 -1759 -814 -1173 N
ATOM 1188 CA GLY A 149 -236.257 16.186 26.002 1.00 84.47 C
ANISOU 1188 CA GLY A 149 13061 9136 9898 -1713 -550 -1329 C
ATOM 1189 C GLY A 149 -235.020 17.034 26.247 1.00 96.51 C
ANISOU 1189 C GLY A 149 14527 10690 11454 -1561 -416 -1278 C
ATOM 1190 O GLY A 149 -235.094 18.214 26.596 1.00101.22 O
ANISOU 1190 O GLY A 149 15019 11400 12040 -1490 -525 -1120 O
ATOM 1191 N GLU A 150 -233.869 16.386 26.061 1.00110.97 N
ANISOU 1191 N GLU A 150 16418 12403 13340 -1514 -169 -1420 N
ATOM 1192 CA GLU A 150 -232.589 17.069 26.211 1.00 92.18 C
ANISOU 1192 CA GLU A 150 13985 10037 11003 -1382 -17 -1395 C
ATOM 1193 C GLU A 150 -232.456 18.207 25.209 1.00108.24 C
ANISOU 1193 C GLU A 150 16127 12224 12776 -1483 -59 -1367 C
ATOM 1194 O GLU A 150 -231.970 19.291 25.551 1.00107.42 O
ANISOU 1194 O GLU A 150 15928 12200 12688 -1383 -76 -1242 O
ATOM 1195 CB GLU A 150 -231.448 16.066 26.038 1.00 98.20 C
ANISOU 1195 CB GLU A 150 14795 10633 11885 -1334 261 -1574 C
ATOM 1196 CG GLU A 150 -230.052 16.651 26.141 1.00113.09 C
ANISOU 1196 CG GLU A 150 16614 12516 13839 -1205 440 -1567 C
ATOM 1197 CD GLU A 150 -228.989 15.697 25.629 1.00135.93 C
ANISOU 1197 CD GLU A 150 19579 15250 16817 -1198 728 -1778 C
ATOM 1198 OE1 GLU A 150 -229.353 14.679 25.000 1.00149.72 O
ANISOU 1198 OE1 GLU A 150 21468 16903 18516 -1322 794 -1947 O
ATOM 1199 OE2 GLU A 150 -227.789 15.964 25.856 1.00138.67 O
ANISOU 1199 OE2 GLU A 150 19835 15560 17294 -1071 893 -1779 O
ATOM 1200 N ASN A 151 -232.883 17.978 23.966 1.00117.02 N
ANISOU 1200 N ASN A 151 17447 13376 13638 -1694 -82 -1479 N
ATOM 1201 CA ASN A 151 -232.815 19.029 22.956 1.00114.15 C
ANISOU 1201 CA ASN A 151 17211 13160 13002 -1818 -141 -1439 C
ATOM 1202 C ASN A 151 -233.654 20.235 23.358 1.00110.56 C
ANISOU 1202 C ASN A 151 16637 12838 12532 -1788 -416 -1207 C
ATOM 1203 O ASN A 151 -233.252 21.383 23.135 1.00110.26 O
ANISOU 1203 O ASN A 151 16594 12897 12405 -1769 -441 -1103 O
ATOM 1204 CB ASN A 151 -233.271 18.487 21.600 1.00128.45 C
ANISOU 1204 CB ASN A 151 19278 14994 14532 -2077 -150 -1592 C
ATOM 1205 CG ASN A 151 -232.216 17.631 20.926 1.00140.11 C
ANISOU 1205 CG ASN A 151 20907 16363 15966 -2129 167 -1838 C
ATOM 1206 OD1 ASN A 151 -231.210 17.266 21.534 1.00144.35 O
ANISOU 1206 OD1 ASN A 151 21336 16783 16730 -1959 386 -1897 O
ATOM 1207 ND2 ASN A 151 -232.443 17.305 19.658 1.00145.13 N
ANISOU 1207 ND2 ASN A 151 21794 17035 16315 -2372 192 -1986 N
ATOM 1208 N HIS A 152 -234.821 19.999 23.961 1.00113.21 N
ANISOU 1208 N HIS A 152 16870 13173 12974 -1782 -614 -1125 N
ATOM 1209 CA HIS A 152 -235.683 21.112 24.343 1.00100.94 C
ANISOU 1209 CA HIS A 152 15187 11730 11437 -1752 -865 -918 C
ATOM 1210 C HIS A 152 -235.085 21.911 25.494 1.00102.39 C
ANISOU 1210 C HIS A 152 15169 11913 11820 -1533 -819 -793 C
ATOM 1211 O HIS A 152 -235.140 23.145 25.493 1.00107.38 O
ANISOU 1211 O HIS A 152 15747 12639 12414 -1503 -928 -651 O
ATOM 1212 CB HIS A 152 -237.074 20.600 24.713 1.00 93.79 C
ANISOU 1212 CB HIS A 152 14206 10814 10615 -1805 -1064 -878 C
ATOM 1213 CG HIS A 152 -237.808 19.969 23.571 1.00101.02 C
ANISOU 1213 CG HIS A 152 15311 11750 11324 -2040 -1163 -976 C
ATOM 1214 ND1 HIS A 152 -238.100 18.624 23.528 1.00 88.88 N
ANISOU 1214 ND1 HIS A 152 13838 10108 9824 -2116 -1099 -1128 N
ATOM 1215 CD2 HIS A 152 -238.306 20.499 22.429 1.00108.13 C
ANISOU 1215 CD2 HIS A 152 16354 12759 11970 -2229 -1332 -940 C
ATOM 1216 CE1 HIS A 152 -238.749 18.352 22.409 1.00113.97 C
ANISOU 1216 CE1 HIS A 152 17194 13334 12776 -2345 -1219 -1194 C
ATOM 1217 NE2 HIS A 152 -238.886 19.473 21.724 1.00117.91 N
ANISOU 1217 NE2 HIS A 152 17745 13967 13088 -2421 -1369 -1076 N
ATOM 1218 N ALA A 153 -234.508 21.225 26.484 1.00 97.34 N
ANISOU 1218 N ALA A 153 14424 11166 11396 -1387 -666 -838 N
ATOM 1219 CA ALA A 153 -233.926 21.925 27.624 1.00101.78 C
ANISOU 1219 CA ALA A 153 14804 11730 12138 -1195 -628 -724 C
ATOM 1220 C ALA A 153 -232.757 22.808 27.206 1.00104.44 C
ANISOU 1220 C ALA A 153 15178 12112 12393 -1157 -511 -713 C
ATOM 1221 O ALA A 153 -232.515 23.854 27.821 1.00 96.20 O
ANISOU 1221 O ALA A 153 14012 11121 11419 -1051 -554 -586 O
ATOM 1222 CB ALA A 153 -233.477 20.921 28.685 1.00101.11 C
ANISOU 1222 CB ALA A 153 14621 11516 12281 -1069 -496 -771 C
ATOM 1223 N ILE A 154 -232.024 22.407 26.167 1.00 93.20 N
ANISOU 1223 N ILE A 154 13922 10666 10825 -1251 -350 -854 N
ATOM 1224 CA ILE A 154 -230.884 23.197 25.718 1.00 91.56 C
ANISOU 1224 CA ILE A 154 13753 10499 10538 -1231 -215 -854 C
ATOM 1225 C ILE A 154 -231.355 24.501 25.086 1.00 97.56 C
ANISOU 1225 C ILE A 154 14565 11394 11108 -1321 -390 -722 C
ATOM 1226 O ILE A 154 -230.751 25.561 25.295 1.00102.52 O
ANISOU 1226 O ILE A 154 15127 12071 11755 -1247 -375 -624 O
ATOM 1227 CB ILE A 154 -230.014 22.373 24.752 1.00 87.70 C
ANISOU 1227 CB ILE A 154 13431 9945 9947 -1321 28 -1058 C
ATOM 1228 CG1 ILE A 154 -229.402 21.174 25.477 1.00 87.31 C
ANISOU 1228 CG1 ILE A 154 13295 9735 10142 -1198 208 -1170 C
ATOM 1229 CG2 ILE A 154 -228.929 23.238 24.140 1.00 76.37 C
ANISOU 1229 CG2 ILE A 154 12050 8567 8399 -1335 168 -1060 C
ATOM 1230 CD1 ILE A 154 -228.703 20.199 24.555 1.00 88.70 C
ANISOU 1230 CD1 ILE A 154 13627 9818 10258 -1288 453 -1395 C
ATOM 1231 N MET A 155 -232.439 24.448 24.306 1.00 86.14 N
ANISOU 1231 N MET A 155 13237 10005 9487 -1488 -569 -709 N
ATOM 1232 CA MET A 155 -232.998 25.670 23.738 1.00 83.90 C
ANISOU 1232 CA MET A 155 12991 9838 9048 -1573 -774 -556 C
ATOM 1233 C MET A 155 -233.375 26.662 24.829 1.00 85.18 C
ANISOU 1233 C MET A 155 12934 10023 9406 -1415 -916 -376 C
ATOM 1234 O MET A 155 -233.118 27.864 24.700 1.00103.37 O
ANISOU 1234 O MET A 155 15218 12386 11670 -1396 -970 -255 O
ATOM 1235 CB MET A 155 -234.217 25.347 22.878 1.00 97.05 C
ANISOU 1235 CB MET A 155 14786 11552 10537 -1769 -979 -556 C
ATOM 1236 CG MET A 155 -233.905 24.696 21.549 1.00123.45 C
ANISOU 1236 CG MET A 155 18393 14906 13606 -1978 -872 -717 C
ATOM 1237 SD MET A 155 -235.413 24.125 20.736 1.00149.83 S
ANISOU 1237 SD MET A 155 21865 18292 16773 -2209 -1134 -725 S
ATOM 1238 CE MET A 155 -236.433 25.598 20.831 1.00148.04 C
ANISOU 1238 CE MET A 155 21516 18172 16561 -2201 -1484 -442 C
ATOM 1239 N GLY A 156 -233.981 26.175 25.913 1.00 70.67 N
ANISOU 1239 N GLY A 156 10938 8134 7781 -1310 -967 -360 N
ATOM 1240 CA GLY A 156 -234.346 27.062 27.005 1.00 76.46 C
ANISOU 1240 CA GLY A 156 11468 8884 8701 -1169 -1074 -214 C
ATOM 1241 C GLY A 156 -233.152 27.789 27.590 1.00 83.35 C
ANISOU 1241 C GLY A 156 12261 9749 9658 -1031 -932 -180 C
ATOM 1242 O GLY A 156 -233.225 28.985 27.883 1.00 95.73 O
ANISOU 1242 O GLY A 156 13743 11361 11269 -976 -1021 -52 O
ATOM 1243 N VAL A 157 -232.034 27.079 27.764 1.00 86.41 N
ANISOU 1243 N VAL A 157 12670 10073 10088 -976 -711 -295 N
ATOM 1244 CA VAL A 157 -230.829 27.711 28.292 1.00 82.22 C
ANISOU 1244 CA VAL A 157 12059 9536 9646 -855 -576 -267 C
ATOM 1245 C VAL A 157 -230.314 28.753 27.311 1.00 81.81 C
ANISOU 1245 C VAL A 157 12111 9554 9420 -933 -566 -224 C
ATOM 1246 O VAL A 157 -230.075 29.911 27.674 1.00 80.60 O
ANISOU 1246 O VAL A 157 11874 9438 9313 -868 -613 -109 O
ATOM 1247 CB VAL A 157 -229.756 26.654 28.604 1.00 75.82 C
ANISOU 1247 CB VAL A 157 11238 8631 8938 -786 -351 -397 C
ATOM 1248 CG1 VAL A 157 -228.438 27.334 28.952 1.00 77.67 C
ANISOU 1248 CG1 VAL A 157 11398 8866 9249 -685 -215 -371 C
ATOM 1249 CG2 VAL A 157 -230.211 25.759 29.739 1.00 67.17 C
ANISOU 1249 CG2 VAL A 157 10027 7462 8034 -698 -375 -403 C
ATOM 1250 N ALA A 158 -230.148 28.354 26.048 1.00 68.79 N
ANISOU 1250 N ALA A 158 10656 7923 7560 -1086 -501 -316 N
ATOM 1251 CA ALA A 158 -229.702 29.292 25.025 1.00 75.24 C
ANISOU 1251 CA ALA A 158 11599 8811 8176 -1191 -491 -271 C
ATOM 1252 C ALA A 158 -230.626 30.493 24.935 1.00 88.85 C
ANISOU 1252 C ALA A 158 13294 10605 9859 -1222 -746 -86 C
ATOM 1253 O ALA A 158 -230.176 31.609 24.648 1.00 98.58 O
ANISOU 1253 O ALA A 158 14543 11881 11034 -1232 -758 11 O
ATOM 1254 CB ALA A 158 -229.622 28.591 23.670 1.00 66.42 C
ANISOU 1254 CB ALA A 158 10718 7710 6809 -1385 -406 -404 C
ATOM 1255 N PHE A 159 -231.917 30.286 25.188 1.00 87.01 N
ANISOU 1255 N PHE A 159 13009 10375 9675 -1236 -949 -33 N
ATOM 1256 CA PHE A 159 -232.872 31.381 25.106 1.00 84.58 C
ANISOU 1256 CA PHE A 159 12652 10117 9369 -1258 -1199 143 C
ATOM 1257 C PHE A 159 -232.603 32.431 26.175 1.00 84.17 C
ANISOU 1257 C PHE A 159 12411 10048 9523 -1090 -1207 250 C
ATOM 1258 O PHE A 159 -232.761 33.631 25.928 1.00 95.19 O
ANISOU 1258 O PHE A 159 13795 11474 10901 -1102 -1328 388 O
ATOM 1259 CB PHE A 159 -234.287 30.832 25.229 1.00 74.36 C
ANISOU 1259 CB PHE A 159 11311 8819 8124 -1300 -1395 160 C
ATOM 1260 CG PHE A 159 -235.335 31.884 25.308 1.00 72.79 C
ANISOU 1260 CG PHE A 159 11011 8649 7997 -1294 -1650 338 C
ATOM 1261 CD1 PHE A 159 -235.739 32.558 24.169 1.00 83.90 C
ANISOU 1261 CD1 PHE A 159 12544 10114 9222 -1442 -1828 448 C
ATOM 1262 CD2 PHE A 159 -235.931 32.194 26.517 1.00 64.98 C
ANISOU 1262 CD2 PHE A 159 9800 7624 7264 -1148 -1713 397 C
ATOM 1263 CE1 PHE A 159 -236.715 33.531 24.233 1.00 78.32 C
ANISOU 1263 CE1 PHE A 159 11726 9416 8616 -1429 -2075 624 C
ATOM 1264 CE2 PHE A 159 -236.909 33.167 26.587 1.00 78.36 C
ANISOU 1264 CE2 PHE A 159 11385 9330 9060 -1136 -1934 550 C
ATOM 1265 CZ PHE A 159 -237.301 33.836 25.441 1.00 73.92 C
ANISOU 1265 CZ PHE A 159 10932 8812 8343 -1269 -2122 668 C
ATOM 1266 N THR A 160 -232.204 32.000 27.373 1.00 72.83 N
ANISOU 1266 N THR A 160 10831 8560 8282 -942 -1085 191 N
ATOM 1267 CA THR A 160 -231.835 32.961 28.406 1.00 72.74 C
ANISOU 1267 CA THR A 160 10658 8535 8446 -799 -1072 272 C
ATOM 1268 C THR A 160 -230.621 33.772 27.979 1.00 73.69 C
ANISOU 1268 C THR A 160 10835 8673 8489 -804 -955 294 C
ATOM 1269 O THR A 160 -230.579 34.991 28.176 1.00 87.07 O
ANISOU 1269 O THR A 160 12469 10378 10235 -766 -1025 408 O
ATOM 1270 CB THR A 160 -231.557 32.249 29.731 1.00 86.92 C
ANISOU 1270 CB THR A 160 12316 10278 10432 -665 -962 203 C
ATOM 1271 OG1 THR A 160 -230.462 31.338 29.571 1.00 89.98 O
ANISOU 1271 OG1 THR A 160 12769 10633 10786 -661 -760 80 O
ATOM 1272 CG2 THR A 160 -232.792 31.484 30.202 1.00 79.12 C
ANISOU 1272 CG2 THR A 160 11266 9272 9526 -668 -1071 189 C
ATOM 1273 N TRP A 161 -229.627 33.114 27.379 1.00 80.29 N
ANISOU 1273 N TRP A 161 11787 9506 9214 -855 -767 180 N
ATOM 1274 CA ATRP A 161 -228.432 33.823 26.935 0.56 78.30 C
ANISOU 1274 CA ATRP A 161 11585 9272 8891 -872 -632 190 C
ATOM 1275 CA BTRP A 161 -228.435 33.832 26.944 0.44 78.49 C
ANISOU 1275 CA BTRP A 161 11608 9296 8917 -871 -634 191 C
ATOM 1276 C TRP A 161 -228.776 34.876 25.890 1.00 91.75 C
ANISOU 1276 C TRP A 161 13411 11032 10417 -1000 -766 312 C
ATOM 1277 O TRP A 161 -228.234 35.987 25.913 1.00 96.46 O
ANISOU 1277 O TRP A 161 13981 11640 11031 -980 -758 403 O
ATOM 1278 CB ATRP A 161 -227.408 32.830 26.384 0.56 73.29 C
ANISOU 1278 CB ATRP A 161 11052 8617 8177 -917 -395 30 C
ATOM 1279 CB BTRP A 161 -227.392 32.852 26.412 0.44 74.11 C
ANISOU 1279 CB BTRP A 161 11152 8721 8286 -913 -394 32 C
ATOM 1280 CG ATRP A 161 -226.924 31.827 27.396 0.56 79.08 C
ANISOU 1280 CG ATRP A 161 11660 9279 9109 -785 -264 -71 C
ATOM 1281 CG BTRP A 161 -226.782 31.989 27.472 0.44 79.19 C
ANISOU 1281 CG BTRP A 161 11658 9294 9137 -772 -255 -60 C
ATOM 1282 CD1ATRP A 161 -227.214 31.798 28.732 0.56 74.51 C
ANISOU 1282 CD1ATRP A 161 10906 8666 8739 -646 -330 -26 C
ATOM 1283 CD1BTRP A 161 -227.222 30.767 27.888 0.44 78.16 C
ANISOU 1283 CD1BTRP A 161 11503 9110 9085 -741 -245 -146 C
ATOM 1284 CD2ATRP A 161 -226.062 30.707 27.150 0.56 82.18 C
ANISOU 1284 CD2ATRP A 161 12094 9615 9514 -787 -45 -230 C
ATOM 1285 CD2BTRP A 161 -225.609 32.279 28.244 0.44 81.15 C
ANISOU 1285 CD2BTRP A 161 11775 9513 9544 -652 -119 -61 C
ATOM 1286 NE1ATRP A 161 -226.587 30.731 29.330 0.56 73.50 N
ANISOU 1286 NE1ATRP A 161 10715 8470 8743 -566 -187 -127 N
ATOM 1287 NE1BTRP A 161 -226.399 30.278 28.875 0.44 78.09 N
ANISOU 1287 NE1BTRP A 161 11360 9037 9274 -606 -118 -191 N
ATOM 1288 CE2ATRP A 161 -225.873 30.046 28.381 0.56 80.79 C
ANISOU 1288 CE2ATRP A 161 11759 9369 9568 -641 -11 -253 C
ATOM 1289 CE2BTRP A 161 -225.401 31.187 29.111 0.44 81.79 C
ANISOU 1289 CE2BTRP A 161 11758 9524 9796 -551 -44 -140 C
ATOM 1290 CE3ATRP A 161 -225.431 30.201 26.009 0.56 70.19 C
ANISOU 1290 CE3ATRP A 161 10735 8094 7839 -904 133 -357 C
ATOM 1291 CE3BTRP A 161 -224.717 33.355 28.288 0.44 64.14 C
ANISOU 1291 CE3BTRP A 161 9577 7384 7409 -629 -61 2 C
ATOM 1292 CZ2ATRP A 161 -225.080 28.905 28.500 0.56 76.38 C
ANISOU 1292 CZ2ATRP A 161 11182 8727 9113 -595 177 -384 C
ATOM 1293 CZ2BTRP A 161 -224.337 31.140 30.011 0.44 79.61 C
ANISOU 1293 CZ2BTRP A 161 11338 9205 9704 -428 69 -148 C
ATOM 1294 CZ3ATRP A 161 -224.646 29.070 26.131 0.56 60.05 C
ANISOU 1294 CZ3ATRP A 161 9429 6725 6664 -855 343 -509 C
ATOM 1295 CZ3BTRP A 161 -223.662 33.306 29.181 0.44 66.22 C
ANISOU 1295 CZ3BTRP A 161 9695 7609 7858 -508 60 -19 C
ATOM 1296 CH2ATRP A 161 -224.477 28.434 27.366 0.56 65.13 C
ANISOU 1296 CH2ATRP A 161 9898 7288 7562 -696 356 -515 C
ATOM 1297 CH2BTRP A 161 -223.481 32.207 30.030 0.44 69.53 C
ANISOU 1297 CH2BTRP A 161 10015 7962 8442 -410 116 -89 C
ATOM 1298 N VAL A 162 -229.678 34.545 24.966 1.00 90.84 N
ANISOU 1298 N VAL A 162 13433 10952 10131 -1142 -900 322 N
ATOM 1299 CA VAL A 162 -230.088 35.516 23.958 1.00 78.36 C
ANISOU 1299 CA VAL A 162 11975 9423 8375 -1278 -1063 462 C
ATOM 1300 C VAL A 162 -230.830 36.677 24.605 1.00 85.39 C
ANISOU 1300 C VAL A 162 12710 10295 9439 -1186 -1271 636 C
ATOM 1301 O VAL A 162 -230.573 37.844 24.292 1.00 97.37 O
ANISOU 1301 O VAL A 162 14248 11820 10928 -1209 -1325 763 O
ATOM 1302 CB VAL A 162 -230.934 34.833 22.871 1.00 78.04 C
ANISOU 1302 CB VAL A 162 12114 9426 8113 -1461 -1183 437 C
ATOM 1303 CG1 VAL A 162 -231.616 35.872 22.000 1.00 70.79 C
ANISOU 1303 CG1 VAL A 162 11288 8556 7052 -1591 -1426 625 C
ATOM 1304 CG2 VAL A 162 -230.057 33.922 22.031 1.00 76.64 C
ANISOU 1304 CG2 VAL A 162 12124 9266 7730 -1582 -951 263 C
ATOM 1305 N MET A 163 -231.754 36.381 25.523 1.00 86.15 N
ANISOU 1305 N MET A 163 12648 10357 9728 -1083 -1377 640 N
ATOM 1306 CA MET A 163 -232.486 37.449 26.197 1.00 88.38 C
ANISOU 1306 CA MET A 163 12768 10608 10204 -989 -1548 781 C
ATOM 1307 C MET A 163 -231.555 38.315 27.034 1.00 99.13 C
ANISOU 1307 C MET A 163 14019 11935 11709 -863 -1426 800 C
ATOM 1308 O MET A 163 -231.682 39.545 27.045 1.00 91.10 O
ANISOU 1308 O MET A 163 12957 10898 10759 -843 -1528 931 O
ATOM 1309 CB MET A 163 -233.596 36.863 27.071 1.00 82.17 C
ANISOU 1309 CB MET A 163 11830 9793 9598 -910 -1642 753 C
ATOM 1310 CG MET A 163 -234.790 36.319 26.303 1.00 90.50 C
ANISOU 1310 CG MET A 163 12952 10874 10559 -1034 -1835 780 C
ATOM 1311 SD MET A 163 -235.606 37.592 25.326 1.00 94.05 S
ANISOU 1311 SD MET A 163 13442 11339 10953 -1136 -2122 999 S
ATOM 1312 CE MET A 163 -235.004 37.193 23.688 1.00106.13 C
ANISOU 1312 CE MET A 163 15279 12946 12099 -1364 -2093 975 C
ATOM 1313 N ALA A 164 -230.614 37.690 27.746 1.00 86.67 N
ANISOU 1313 N ALA A 164 12394 10345 10191 -780 -1217 674 N
ATOM 1314 CA ALA A 164 -229.704 38.455 28.591 1.00 82.82 C
ANISOU 1314 CA ALA A 164 11798 9831 9840 -670 -1109 687 C
ATOM 1315 C ALA A 164 -228.774 39.322 27.757 1.00 94.38 C
ANISOU 1315 C ALA A 164 13369 11314 11177 -746 -1048 746 C
ATOM 1316 O ALA A 164 -228.468 40.459 28.135 1.00106.73 O
ANISOU 1316 O ALA A 164 14861 12852 12838 -695 -1067 831 O
ATOM 1317 CB ALA A 164 -228.900 37.517 29.484 1.00 83.97 C
ANISOU 1317 CB ALA A 164 11871 9959 10074 -578 -922 554 C
ATOM 1318 N LEU A 165 -228.302 38.801 26.622 1.00 86.44 N
ANISOU 1318 N LEU A 165 12541 10351 9952 -877 -962 696 N
ATOM 1319 CA LEU A 165 -227.524 39.629 25.711 1.00 79.18 C
ANISOU 1319 CA LEU A 165 11743 9457 8884 -979 -908 761 C
ATOM 1320 C LEU A 165 -228.372 40.768 25.163 1.00 87.42 C
ANISOU 1320 C LEU A 165 12829 10499 9887 -1047 -1143 948 C
ATOM 1321 O LEU A 165 -227.877 41.884 24.967 1.00 87.95 O
ANISOU 1321 O LEU A 165 12910 10553 9954 -1065 -1146 1052 O
ATOM 1322 CB LEU A 165 -226.952 38.779 24.576 1.00 75.50 C
ANISOU 1322 CB LEU A 165 11473 9039 8175 -1125 -759 654 C
ATOM 1323 CG LEU A 165 -225.779 37.868 24.940 1.00 92.83 C
ANISOU 1323 CG LEU A 165 13628 11218 10423 -1065 -487 481 C
ATOM 1324 CD1 LEU A 165 -225.445 36.928 23.791 1.00 95.44 C
ANISOU 1324 CD1 LEU A 165 14154 11583 10525 -1216 -343 353 C
ATOM 1325 CD2 LEU A 165 -224.564 38.695 25.323 1.00 81.81 C
ANISOU 1325 CD2 LEU A 165 12150 9809 9124 -1006 -347 504 C
ATOM 1326 N ALA A 166 -229.663 40.513 24.941 1.00 79.43 N
ANISOU 1326 N ALA A 166 11825 9490 8863 -1082 -1350 1000 N
ATOM 1327 CA ALA A 166 -230.552 41.552 24.435 1.00 80.67 C
ANISOU 1327 CA ALA A 166 12001 9634 9018 -1139 -1600 1193 C
ATOM 1328 C ALA A 166 -230.676 42.725 25.398 1.00 88.74 C
ANISOU 1328 C ALA A 166 12837 10578 10301 -996 -1662 1288 C
ATOM 1329 O ALA A 166 -231.034 43.829 24.973 1.00 84.48 O
ANISOU 1329 O ALA A 166 12312 10004 9781 -1033 -1824 1456 O
ATOM 1330 CB ALA A 166 -231.935 40.967 24.143 1.00 69.89 C
ANISOU 1330 CB ALA A 166 10640 8281 7633 -1190 -1812 1221 C
ATOM 1331 N CYS A 167 -230.390 42.516 26.681 1.00 90.21 N
ANISOU 1331 N CYS A 167 12857 10731 10689 -841 -1541 1186 N
ATOM 1332 CA CYS A 167 -230.413 43.589 27.664 1.00 93.11 C
ANISOU 1332 CA CYS A 167 13058 11025 11295 -715 -1566 1244 C
ATOM 1333 C CYS A 167 -229.027 44.117 28.003 1.00 91.02 C
ANISOU 1333 C CYS A 167 12786 10751 11045 -682 -1379 1210 C
ATOM 1334 O CYS A 167 -228.849 45.329 28.133 1.00 80.90 O
ANISOU 1334 O CYS A 167 11464 9416 9859 -661 -1421 1309 O
ATOM 1335 CB CYS A 167 -231.100 43.120 28.951 1.00 90.29 C
ANISOU 1335 CB CYS A 167 12518 10636 11150 -579 -1570 1160 C
ATOM 1336 SG CYS A 167 -230.663 44.110 30.400 1.00106.21 S
ANISOU 1336 SG CYS A 167 14352 12582 13422 -430 -1488 1144 S
ATOM 1337 N ALA A 168 -228.035 43.238 28.138 1.00 85.36 N
ANISOU 1337 N ALA A 168 12100 10078 10253 -680 -1176 1073 N
ATOM 1338 CA ALA A 168 -226.729 43.654 28.629 1.00 76.52 C
ANISOU 1338 CA ALA A 168 10934 8950 9191 -636 -1001 1032 C
ATOM 1339 C ALA A 168 -225.833 44.233 27.541 1.00 86.24 C
ANISOU 1339 C ALA A 168 12308 10205 10254 -760 -927 1091 C
ATOM 1340 O ALA A 168 -224.915 44.996 27.858 1.00 82.70 O
ANISOU 1340 O ALA A 168 11812 9733 9875 -736 -834 1108 O
ATOM 1341 CB ALA A 168 -226.025 42.473 29.299 1.00 74.80 C
ANISOU 1341 CB ALA A 168 10661 8757 9004 -571 -822 872 C
ATOM 1342 N ALA A 169 -226.077 43.904 26.276 1.00 90.99 N
ANISOU 1342 N ALA A 169 13088 10854 10628 -904 -965 1123 N
ATOM 1343 CA ALA A 169 -225.195 44.323 25.190 1.00 81.68 C
ANISOU 1343 CA ALA A 169 12069 9711 9255 -1047 -866 1165 C
ATOM 1344 C ALA A 169 -225.539 45.678 24.564 1.00 96.06 C
ANISOU 1344 C ALA A 169 13960 11500 11038 -1128 -1034 1366 C
ATOM 1345 O ALA A 169 -224.613 46.415 24.202 1.00 89.42 O
ANISOU 1345 O ALA A 169 13173 10657 10147 -1192 -934 1414 O
ATOM 1346 CB ALA A 169 -225.166 43.251 24.096 1.00 75.86 C
ANISOU 1346 CB ALA A 169 11517 9046 8260 -1188 -793 1081 C
ATOM 1347 N PRO A 170 -226.814 46.044 24.386 1.00 99.35 N
ANISOU 1347 N PRO A 170 14376 11885 11487 -1136 -1286 1494 N
ATOM 1348 CA PRO A 170 -227.135 47.343 23.754 1.00 94.82 C
ANISOU 1348 CA PRO A 170 13866 11264 10895 -1213 -1462 1706 C
ATOM 1349 C PRO A 170 -226.453 48.526 24.427 1.00 94.71 C
ANISOU 1349 C PRO A 170 13744 11171 11072 -1133 -1404 1758 C
ATOM 1350 O PRO A 170 -226.068 49.478 23.731 1.00 84.85 O
ANISOU 1350 O PRO A 170 12595 9899 9744 -1235 -1432 1896 O
ATOM 1351 CB PRO A 170 -228.662 47.431 23.883 1.00 89.71 C
ANISOU 1351 CB PRO A 170 13147 10573 10367 -1168 -1734 1804 C
ATOM 1352 CG PRO A 170 -229.092 46.035 23.817 1.00 94.62 C
ANISOU 1352 CG PRO A 170 13796 11266 10889 -1182 -1709 1668 C
ATOM 1353 CD PRO A 170 -228.040 45.235 24.547 1.00 95.13 C
ANISOU 1353 CD PRO A 170 13803 11360 10983 -1102 -1433 1465 C
ATOM 1354 N PRO A 171 -226.297 48.544 25.760 1.00 89.05 N
ANISOU 1354 N PRO A 171 12831 10406 10597 -965 -1329 1658 N
ATOM 1355 CA PRO A 171 -225.553 49.668 26.357 1.00 75.41 C
ANISOU 1355 CA PRO A 171 11017 8606 9030 -912 -1263 1693 C
ATOM 1356 C PRO A 171 -224.123 49.797 25.861 1.00 82.95 C
ANISOU 1356 C PRO A 171 12064 9607 9847 -1008 -1058 1665 C
ATOM 1357 O PRO A 171 -223.568 50.901 25.903 1.00116.02 O
ANISOU 1357 O PRO A 171 16240 13735 14107 -1026 -1041 1749 O
ATOM 1358 CB PRO A 171 -225.603 49.361 27.859 1.00 89.20 C
ANISOU 1358 CB PRO A 171 12562 10324 11007 -740 -1200 1556 C
ATOM 1359 CG PRO A 171 -226.864 48.620 28.026 1.00 85.30 C
ANISOU 1359 CG PRO A 171 12028 9839 10544 -693 -1333 1534 C
ATOM 1360 CD PRO A 171 -226.970 47.752 26.810 1.00 87.16 C
ANISOU 1360 CD PRO A 171 12440 10162 10514 -827 -1344 1539 C
ATOM 1361 N LEU A 172 -223.504 48.713 25.389 1.00 82.08 N
ANISOU 1361 N LEU A 172 12041 9591 9555 -1073 -892 1544 N
ATOM 1362 CA LEU A 172 -222.149 48.820 24.855 1.00 75.32 C
ANISOU 1362 CA LEU A 172 11264 8777 8579 -1172 -678 1510 C
ATOM 1363 C LEU A 172 -222.130 49.356 23.426 1.00 88.18 C
ANISOU 1363 C LEU A 172 13111 10432 9962 -1371 -723 1653 C
ATOM 1364 O LEU A 172 -221.135 49.955 23.012 1.00100.63 O
ANISOU 1364 O LEU A 172 14745 12014 11477 -1461 -589 1688 O
ATOM 1365 CB LEU A 172 -221.448 47.460 24.886 1.00 65.54 C
ANISOU 1365 CB LEU A 172 10023 7614 7266 -1163 -461 1316 C
ATOM 1366 CG LEU A 172 -221.424 46.639 26.170 1.00 74.81 C
ANISOU 1366 CG LEU A 172 11011 8776 8635 -992 -408 1171 C
ATOM 1367 CD1 LEU A 172 -220.894 45.249 25.861 1.00 68.43 C
ANISOU 1367 CD1 LEU A 172 10246 8031 7724 -1014 -223 1008 C
ATOM 1368 CD2 LEU A 172 -220.562 47.315 27.214 1.00 68.43 C
ANISOU 1368 CD2 LEU A 172 10038 7923 8038 -897 -329 1154 C
ATOM 1369 N VAL A 173 -223.199 49.148 22.658 1.00 99.15 N
ANISOU 1369 N VAL A 173 14627 11843 11204 -1453 -911 1743 N
ATOM 1370 CA VAL A 173 -223.227 49.562 21.254 1.00101.39 C
ANISOU 1370 CA VAL A 173 15144 12164 11214 -1667 -972 1887 C
ATOM 1371 C VAL A 173 -223.684 51.010 21.095 1.00 99.56 C
ANISOU 1371 C VAL A 173 14920 11838 11072 -1691 -1188 2126 C
ATOM 1372 O VAL A 173 -223.171 51.730 20.233 1.00134.34 O
ANISOU 1372 O VAL A 173 19475 16248 15321 -1849 -1167 2252 O
ATOM 1373 CB VAL A 173 -224.124 48.600 20.448 1.00120.13 C
ANISOU 1373 CB VAL A 173 17665 14613 13366 -1769 -1084 1872 C
ATOM 1374 CG1 VAL A 173 -224.274 49.074 19.006 1.00141.41 C
ANISOU 1374 CG1 VAL A 173 20617 17352 15760 -2009 -1189 2043 C
ATOM 1375 CG2 VAL A 173 -223.542 47.204 20.472 1.00118.52 C
ANISOU 1375 CG2 VAL A 173 17479 14489 13066 -1767 -842 1634 C
ATOM 1376 N GLY A 174 -224.638 51.481 21.898 1.00 86.80 N
ANISOU 1376 N GLY A 174 13143 10124 9712 -1543 -1389 2194 N
ATOM 1377 CA GLY A 174 -225.077 52.859 21.793 1.00 84.77 C
ANISOU 1377 CA GLY A 174 12874 9751 9585 -1549 -1588 2414 C
ATOM 1378 C GLY A 174 -226.484 53.144 22.284 1.00101.90 C
ANISOU 1378 C GLY A 174 14911 11827 11981 -1427 -1855 2504 C
ATOM 1379 O GLY A 174 -226.943 54.291 22.231 1.00108.50 O
ANISOU 1379 O GLY A 174 15715 12542 12968 -1416 -2035 2690 O
ATOM 1380 N TRP A 175 -227.185 52.115 22.757 1.00 94.81 N
ANISOU 1380 N TRP A 175 13927 10972 11124 -1337 -1881 2376 N
ATOM 1381 CA TRP A 175 -228.528 52.270 23.308 1.00 81.68 C
ANISOU 1381 CA TRP A 175 12112 9226 9697 -1214 -2105 2432 C
ATOM 1382 C TRP A 175 -228.424 52.192 24.825 1.00 79.58 C
ANISOU 1382 C TRP A 175 11618 8908 9711 -1013 -1979 2265 C
ATOM 1383 O TRP A 175 -228.168 51.119 25.382 1.00 87.71 O
ANISOU 1383 O TRP A 175 12602 10016 10710 -957 -1828 2076 O
ATOM 1384 CB TRP A 175 -229.480 51.212 22.758 1.00 92.10 C
ANISOU 1384 CB TRP A 175 13497 10629 10869 -1273 -2237 2419 C
ATOM 1385 CG TRP A 175 -230.936 51.555 22.952 1.00 96.99 C
ANISOU 1385 CG TRP A 175 13987 11159 11705 -1198 -2518 2542 C
ATOM 1386 CD1 TRP A 175 -231.458 52.776 23.272 1.00 90.99 C
ANISOU 1386 CD1 TRP A 175 13103 10250 11218 -1116 -2676 2695 C
ATOM 1387 CD2 TRP A 175 -232.049 50.659 22.844 1.00102.67 C
ANISOU 1387 CD2 TRP A 175 14675 11924 12411 -1196 -2665 2517 C
ATOM 1388 NE1 TRP A 175 -232.828 52.696 23.365 1.00103.85 N
ANISOU 1388 NE1 TRP A 175 14614 11828 13017 -1058 -2909 2768 N
ATOM 1389 CE2 TRP A 175 -233.216 51.407 23.107 1.00105.95 C
ANISOU 1389 CE2 TRP A 175 14933 12217 13106 -1110 -2910 2663 C
ATOM 1390 CE3 TRP A 175 -232.173 49.297 22.548 1.00 89.76 C
ANISOU 1390 CE3 TRP A 175 13124 10412 10570 -1262 -2608 2381 C
ATOM 1391 CZ2 TRP A 175 -234.488 50.839 23.084 1.00102.91 C
ANISOU 1391 CZ2 TRP A 175 14464 11839 12799 -1090 -3103 2682 C
ATOM 1392 CZ3 TRP A 175 -233.434 48.736 22.525 1.00 92.19 C
ANISOU 1392 CZ3 TRP A 175 13362 10725 10940 -1249 -2803 2399 C
ATOM 1393 CH2 TRP A 175 -234.576 49.505 22.792 1.00106.92 C
ANISOU 1393 CH2 TRP A 175 15063 12478 13086 -1165 -3050 2551 C
ATOM 1394 N SER A 176 -228.638 53.333 25.483 1.00 89.32 N
ANISOU 1394 N SER A 176 12717 10003 11216 -914 -2046 2338 N
ATOM 1395 CA SER A 176 -228.347 53.535 26.899 1.00 86.42 C
ANISOU 1395 CA SER A 176 12162 9578 11096 -755 -1911 2192 C
ATOM 1396 C SER A 176 -226.848 53.392 27.139 1.00 87.86 C
ANISOU 1396 C SER A 176 12383 9823 11177 -784 -1659 2074 C
ATOM 1397 O SER A 176 -226.057 53.441 26.190 1.00 89.53 O
ANISOU 1397 O SER A 176 12755 10092 11172 -922 -1592 2131 O
ATOM 1398 CB SER A 176 -229.148 52.572 27.782 1.00 75.28 C
ANISOU 1398 CB SER A 176 10613 8198 9793 -636 -1910 2045 C
ATOM 1399 OG SER A 176 -229.015 52.911 29.154 1.00 89.80 O
ANISOU 1399 OG SER A 176 12277 9969 11871 -497 -1809 1927 O
ATOM 1400 N ARG A 177 -226.443 53.221 28.394 1.00 79.45 N
ANISOU 1400 N ARG A 177 11172 8749 10265 -664 -1518 1913 N
ATOM 1401 CA ARG A 177 -225.026 53.249 28.727 1.00 70.07 C
ANISOU 1401 CA ARG A 177 9986 7601 9036 -682 -1305 1818 C
ATOM 1402 C ARG A 177 -224.841 52.728 30.140 1.00 66.81 C
ANISOU 1402 C ARG A 177 9414 7203 8768 -553 -1193 1637 C
ATOM 1403 O ARG A 177 -225.772 52.741 30.951 1.00 75.69 O
ANISOU 1403 O ARG A 177 10421 8275 10061 -450 -1274 1601 O
ATOM 1404 CB ARG A 177 -224.452 54.666 28.614 1.00 70.89 C
ANISOU 1404 CB ARG A 177 10101 7602 9231 -724 -1307 1931 C
ATOM 1405 CG ARG A 177 -224.975 55.617 29.682 1.00 72.31 C
ANISOU 1405 CG ARG A 177 10125 7641 9709 -604 -1375 1927 C
ATOM 1406 CD ARG A 177 -224.417 57.009 29.503 1.00 93.76 C
ANISOU 1406 CD ARG A 177 12864 10241 12519 -655 -1380 2041 C
ATOM 1407 NE ARG A 177 -224.976 57.926 30.486 1.00 98.37 N
ANISOU 1407 NE ARG A 177 13304 10673 13398 -545 -1439 2026 N
ATOM 1408 CZ ARG A 177 -224.448 59.103 30.783 1.00 74.51 C
ANISOU 1408 CZ ARG A 177 10255 7532 10522 -555 -1409 2061 C
ATOM 1409 NH1 ARG A 177 -223.342 59.497 30.174 1.00 83.29 N
ANISOU 1409 NH1 ARG A 177 11468 8666 11511 -672 -1324 2124 N
ATOM 1410 NH2 ARG A 177 -225.019 59.874 31.696 1.00 97.69 N
ANISOU 1410 NH2 ARG A 177 13063 10325 13731 -455 -1449 2023 N
ATOM 1411 N TYR A 178 -223.616 52.288 30.427 1.00 65.66 N
ANISOU 1411 N TYR A 178 9263 7127 8559 -566 -1006 1529 N
ATOM 1412 CA TYR A 178 -223.213 51.908 31.773 1.00 68.11 C
ANISOU 1412 CA TYR A 178 9432 7451 8995 -465 -903 1378 C
ATOM 1413 C TYR A 178 -222.498 53.076 32.435 1.00 74.67 C
ANISOU 1413 C TYR A 178 10191 8204 9975 -455 -857 1384 C
ATOM 1414 O TYR A 178 -221.566 53.649 31.857 1.00 82.26 O
ANISOU 1414 O TYR A 178 11213 9160 10880 -541 -789 1441 O
ATOM 1415 CB TYR A 178 -222.292 50.685 31.765 1.00 74.43 C
ANISOU 1415 CB TYR A 178 10247 8364 9671 -479 -743 1261 C
ATOM 1416 CG TYR A 178 -222.971 49.386 31.411 1.00 82.50 C
ANISOU 1416 CG TYR A 178 11315 9454 10577 -472 -767 1213 C
ATOM 1417 CD1 TYR A 178 -223.842 48.766 32.298 1.00 84.36 C
ANISOU 1417 CD1 TYR A 178 11459 9688 10906 -376 -826 1142 C
ATOM 1418 CD2 TYR A 178 -222.724 48.765 30.195 1.00 84.74 C
ANISOU 1418 CD2 TYR A 178 11742 9804 10653 -574 -720 1229 C
ATOM 1419 CE1 TYR A 178 -224.461 47.572 31.975 1.00 77.58 C
ANISOU 1419 CE1 TYR A 178 10643 8885 9950 -377 -848 1097 C
ATOM 1420 CE2 TYR A 178 -223.334 47.570 29.863 1.00 80.63 C
ANISOU 1420 CE2 TYR A 178 11271 9338 10026 -578 -740 1173 C
ATOM 1421 CZ TYR A 178 -224.200 46.978 30.756 1.00 77.38 C
ANISOU 1421 CZ TYR A 178 10760 8918 9723 -477 -809 1111 C
ATOM 1422 OH TYR A 178 -224.806 45.792 30.425 1.00 78.90 O
ANISOU 1422 OH TYR A 178 11001 9158 9818 -489 -829 1056 O
ATOM 1423 N ILE A 179 -222.941 53.428 33.637 1.00 66.01 N
ANISOU 1423 N ILE A 179 8972 7046 9065 -362 -886 1317 N
ATOM 1424 CA ILE A 179 -222.280 54.442 34.455 1.00 66.73 C
ANISOU 1424 CA ILE A 179 8988 7064 9302 -353 -834 1288 C
ATOM 1425 C ILE A 179 -222.238 53.946 35.887 1.00 56.93 C
ANISOU 1425 C ILE A 179 7630 5854 8148 -274 -778 1135 C
ATOM 1426 O ILE A 179 -223.060 53.115 36.294 1.00 72.19 O
ANISOU 1426 O ILE A 179 9527 7823 10077 -212 -811 1077 O
ATOM 1427 CB ILE A 179 -223.007 55.804 34.397 1.00 76.11 C
ANISOU 1427 CB ILE A 179 10164 8098 10655 -343 -949 1386 C
ATOM 1428 CG1 ILE A 179 -224.415 55.717 34.997 1.00 73.67 C
ANISOU 1428 CG1 ILE A 179 9774 7731 10486 -245 -1050 1353 C
ATOM 1429 CG2 ILE A 179 -223.112 56.303 32.971 1.00 63.64 C
ANISOU 1429 CG2 ILE A 179 8713 6485 8983 -433 -1032 1565 C
ATOM 1430 CD1 ILE A 179 -225.176 57.030 34.918 1.00 72.95 C
ANISOU 1430 CD1 ILE A 179 9652 7469 10597 -223 -1161 1449 C
ATOM 1431 N PRO A 180 -221.276 54.425 36.673 1.00 62.60 N
ANISOU 1431 N PRO A 180 8289 6562 8934 -287 -697 1073 N
ATOM 1432 CA PRO A 180 -221.343 54.175 38.117 1.00 57.41 C
ANISOU 1432 CA PRO A 180 7532 5920 8363 -229 -668 941 C
ATOM 1433 C PRO A 180 -222.697 54.617 38.655 1.00 63.86 C
ANISOU 1433 C PRO A 180 8305 6646 9313 -165 -749 920 C
ATOM 1434 O PRO A 180 -223.186 55.702 38.337 1.00 82.86 O
ANISOU 1434 O PRO A 180 10719 8930 11834 -167 -810 989 O
ATOM 1435 CB PRO A 180 -220.196 55.020 38.685 1.00 55.68 C
ANISOU 1435 CB PRO A 180 7273 5672 8211 -280 -602 910 C
ATOM 1436 CG PRO A 180 -219.239 55.175 37.545 1.00 50.26 C
ANISOU 1436 CG PRO A 180 6652 5009 7436 -359 -554 1002 C
ATOM 1437 CD PRO A 180 -220.061 55.173 36.285 1.00 47.91 C
ANISOU 1437 CD PRO A 180 6454 4685 7064 -370 -627 1119 C
ATOM 1438 N GLU A 181 -223.317 53.748 39.437 1.00 62.41 N
ANISOU 1438 N GLU A 181 8073 6516 9125 -110 -747 828 N
ATOM 1439 CA GLU A 181 -224.614 54.009 40.030 1.00 61.56 C
ANISOU 1439 CA GLU A 181 7907 6334 9148 -49 -796 785 C
ATOM 1440 C GLU A 181 -224.468 54.116 41.544 1.00 61.21 C
ANISOU 1440 C GLU A 181 7793 6294 9169 -41 -725 642 C
ATOM 1441 O GLU A 181 -223.411 53.838 42.108 1.00 72.94 O
ANISOU 1441 O GLU A 181 9276 7853 10585 -79 -663 590 O
ATOM 1442 CB GLU A 181 -225.613 52.910 39.657 1.00 60.39 C
ANISOU 1442 CB GLU A 181 7766 6244 8937 -8 -851 799 C
ATOM 1443 CG GLU A 181 -225.369 51.592 40.371 1.00 83.84 C
ANISOU 1443 CG GLU A 181 10719 9334 11803 3 -790 704 C
ATOM 1444 CD GLU A 181 -225.930 50.402 39.614 1.00109.81 C
ANISOU 1444 CD GLU A 181 14050 12691 14982 15 -833 740 C
ATOM 1445 OE1 GLU A 181 -226.485 50.611 38.512 1.00124.60 O
ANISOU 1445 OE1 GLU A 181 15971 14529 16842 4 -917 839 O
ATOM 1446 OE2 GLU A 181 -225.809 49.261 40.116 1.00 95.33 O
ANISOU 1446 OE2 GLU A 181 12205 10941 13073 26 -791 674 O
ATOM 1447 N GLY A 182 -225.551 54.532 42.193 1.00 70.64 N
ANISOU 1447 N GLY A 182 8928 7408 10503 3 -736 580 N
ATOM 1448 CA GLY A 182 -225.570 54.723 43.634 1.00 54.57 C
ANISOU 1448 CA GLY A 182 6842 5369 8522 -5 -660 433 C
ATOM 1449 C GLY A 182 -224.358 55.431 44.200 1.00 70.92 C
ANISOU 1449 C GLY A 182 8925 7433 10589 -73 -605 386 C
ATOM 1450 O GLY A 182 -224.077 56.580 43.846 1.00 71.65 O
ANISOU 1450 O GLY A 182 9025 7415 10783 -94 -613 426 O
ATOM 1451 N MET A 183 -223.617 54.752 45.076 1.00 67.72 N
ANISOU 1451 N MET A 183 8519 7139 10071 -114 -560 312 N
ATOM 1452 CA MET A 183 -222.420 55.327 45.673 1.00 70.50 C
ANISOU 1452 CA MET A 183 8874 7501 10412 -191 -524 269 C
ATOM 1453 C MET A 183 -221.225 55.337 44.737 1.00 68.37 C
ANISOU 1453 C MET A 183 8629 7265 10084 -225 -537 375 C
ATOM 1454 O MET A 183 -220.114 55.621 45.188 1.00 66.84 O
ANISOU 1454 O MET A 183 8422 7100 9873 -293 -513 350 O
ATOM 1455 CB MET A 183 -222.073 54.588 46.966 1.00 70.37 C
ANISOU 1455 CB MET A 183 8845 7595 10298 -234 -495 167 C
ATOM 1456 CG MET A 183 -223.201 54.636 47.974 1.00 67.01 C
ANISOU 1456 CG MET A 183 8404 7140 9915 -225 -455 46 C
ATOM 1457 SD MET A 183 -223.014 53.470 49.327 1.00 82.76 S
ANISOU 1457 SD MET A 183 10408 9284 11752 -279 -437 -38 S
ATOM 1458 CE MET A 183 -221.723 54.230 50.299 1.00 77.01 C
ANISOU 1458 CE MET A 183 9696 8574 10991 -403 -427 -106 C
ATOM 1459 N GLN A 184 -221.440 55.035 43.455 1.00 65.64 N
ANISOU 1459 N GLN A 184 8316 6918 9706 -190 -570 489 N
ATOM 1460 CA GLN A 184 -220.480 55.139 42.349 1.00 65.46 C
ANISOU 1460 CA GLN A 184 8330 6911 9630 -228 -565 596 C
ATOM 1461 C GLN A 184 -219.425 54.042 42.386 1.00 74.93 C
ANISOU 1461 C GLN A 184 9516 8243 10712 -248 -525 591 C
ATOM 1462 O GLN A 184 -218.451 54.104 41.622 1.00 72.26 O
ANISOU 1462 O GLN A 184 9191 7927 10339 -290 -491 654 O
ATOM 1463 CB GLN A 184 -219.774 56.500 42.309 1.00 68.91 C
ANISOU 1463 CB GLN A 184 8769 7253 10161 -293 -547 614 C
ATOM 1464 CG GLN A 184 -220.710 57.702 42.313 1.00 68.83 C
ANISOU 1464 CG GLN A 184 8763 7081 10308 -273 -581 619 C
ATOM 1465 CD GLN A 184 -221.710 57.667 41.181 1.00 74.05 C
ANISOU 1465 CD GLN A 184 9464 7689 10983 -222 -653 734 C
ATOM 1466 OE1 GLN A 184 -221.365 57.900 40.017 1.00 67.75 O
ANISOU 1466 OE1 GLN A 184 8726 6877 10141 -256 -678 863 O
ATOM 1467 NE2 GLN A 184 -222.962 57.370 41.511 1.00 64.87 N
ANISOU 1467 NE2 GLN A 184 8269 6502 9878 -150 -688 693 N
ATOM 1468 N CYS A 185 -219.589 53.036 43.245 1.00 78.55 N
ANISOU 1468 N CYS A 185 9941 8783 11120 -220 -525 521 N
ATOM 1469 CA CYS A 185 -218.656 51.921 43.297 1.00 77.91 C
ANISOU 1469 CA CYS A 185 9834 8810 10959 -226 -499 525 C
ATOM 1470 C CYS A 185 -219.007 50.794 42.337 1.00 83.53 C
ANISOU 1470 C CYS A 185 10583 9568 11586 -178 -494 572 C
ATOM 1471 O CYS A 185 -218.116 50.035 41.943 1.00 93.19 O
ANISOU 1471 O CYS A 185 11792 10852 12764 -184 -450 593 O
ATOM 1472 CB CYS A 185 -218.587 51.359 44.712 1.00 80.15 C
ANISOU 1472 CB CYS A 185 10072 9155 11228 -232 -514 443 C
ATOM 1473 SG CYS A 185 -217.799 52.474 45.863 1.00 89.63 S
ANISOU 1473 SG CYS A 185 11234 10331 12489 -320 -517 378 S
ATOM 1474 N SER A 186 -220.275 50.642 41.974 1.00 89.03 N
ANISOU 1474 N SER A 186 11321 10233 12272 -135 -534 583 N
ATOM 1475 CA SER A 186 -220.698 49.646 41.000 1.00 73.35 C
ANISOU 1475 CA SER A 186 9386 8285 10200 -106 -539 624 C
ATOM 1476 C SER A 186 -221.285 50.346 39.781 1.00 84.32 C
ANISOU 1476 C SER A 186 10845 9610 11583 -120 -578 710 C
ATOM 1477 O SER A 186 -221.701 51.507 39.845 1.00 80.37 O
ANISOU 1477 O SER A 186 10342 9022 11173 -127 -617 734 O
ATOM 1478 CB SER A 186 -221.712 48.662 41.608 1.00 73.06 C
ANISOU 1478 CB SER A 186 9335 8280 10144 -55 -571 573 C
ATOM 1479 OG SER A 186 -222.592 49.291 42.535 1.00114.00 O
ANISOU 1479 OG SER A 186 14487 13417 15411 -42 -602 522 O
ATOM 1480 N CYS A 187 -221.314 49.615 38.662 1.00 65.30 N
ANISOU 1480 N CYS A 187 8504 7240 9067 -130 -569 757 N
ATOM 1481 CA CYS A 187 -221.770 50.130 37.379 1.00 73.51 C
ANISOU 1481 CA CYS A 187 9632 8238 10060 -167 -617 855 C
ATOM 1482 C CYS A 187 -222.990 49.357 36.894 1.00 86.85 C
ANISOU 1482 C CYS A 187 11364 9942 11692 -140 -693 870 C
ATOM 1483 O CYS A 187 -223.145 48.166 37.181 1.00 79.04 O
ANISOU 1483 O CYS A 187 10362 9015 10654 -110 -670 807 O
ATOM 1484 CB CYS A 187 -220.652 50.053 36.331 1.00 75.33 C
ANISOU 1484 CB CYS A 187 9928 8506 10186 -239 -533 900 C
ATOM 1485 SG CYS A 187 -219.372 51.313 36.552 1.00110.43 S
ANISOU 1485 SG CYS A 187 14336 12911 14713 -296 -468 923 S
ATOM 1486 N GLY A 188 -223.855 50.044 36.155 1.00 71.31 N
ANISOU 1486 N GLY A 188 9444 7913 9740 -157 -794 962 N
ATOM 1487 CA GLY A 188 -225.073 49.413 35.691 1.00 56.77 C
ANISOU 1487 CA GLY A 188 7630 6079 7860 -140 -889 986 C
ATOM 1488 C GLY A 188 -225.758 50.222 34.612 1.00 65.38 C
ANISOU 1488 C GLY A 188 8788 7106 8947 -184 -1014 1122 C
ATOM 1489 O GLY A 188 -225.220 51.210 34.112 1.00 62.80 O
ANISOU 1489 O GLY A 188 8505 6729 8625 -234 -1016 1205 O
ATOM 1490 N ILE A 189 -226.960 49.769 34.241 1.00 90.49 N
ANISOU 1490 N ILE A 189 11976 10285 12121 -171 -1128 1154 N
ATOM 1491 CA ILE A 189 -227.761 50.505 33.272 1.00 70.46 C
ANISOU 1491 CA ILE A 189 9489 7682 9601 -210 -1284 1301 C
ATOM 1492 C ILE A 189 -228.046 51.889 33.818 1.00 71.90 C
ANISOU 1492 C ILE A 189 9581 7733 10004 -161 -1333 1345 C
ATOM 1493 O ILE A 189 -228.267 52.070 35.023 1.00 85.04 O
ANISOU 1493 O ILE A 189 11126 9357 11828 -83 -1283 1245 O
ATOM 1494 CB ILE A 189 -229.078 49.773 32.961 1.00 87.47 C
ANISOU 1494 CB ILE A 189 11633 9854 11748 -198 -1413 1320 C
ATOM 1495 CG1 ILE A 189 -228.824 48.303 32.634 1.00101.89 C
ANISOU 1495 CG1 ILE A 189 13536 11799 13380 -237 -1345 1240 C
ATOM 1496 CG2 ILE A 189 -229.794 50.442 31.795 1.00 76.15 C
ANISOU 1496 CG2 ILE A 189 10266 8365 10302 -260 -1598 1495 C
ATOM 1497 CD1 ILE A 189 -228.225 48.086 31.274 1.00 94.10 C
ANISOU 1497 CD1 ILE A 189 12719 10868 12165 -357 -1338 1308 C
ATOM 1498 N ASP A 190 -228.042 52.877 32.928 1.00 80.16 N
ANISOU 1498 N ASP A 190 10693 8706 11059 -217 -1426 1496 N
ATOM 1499 CA ASP A 190 -228.284 54.272 33.287 1.00 84.72 C
ANISOU 1499 CA ASP A 190 11196 9132 11860 -178 -1479 1556 C
ATOM 1500 C ASP A 190 -229.750 54.582 33.016 1.00 82.30 C
ANISOU 1500 C ASP A 190 10825 8733 11711 -134 -1664 1652 C
ATOM 1501 O ASP A 190 -230.143 54.905 31.894 1.00 91.31 O
ANISOU 1501 O ASP A 190 12045 9843 12805 -196 -1818 1822 O
ATOM 1502 CB ASP A 190 -227.360 55.198 32.505 1.00 87.00 C
ANISOU 1502 CB ASP A 190 11590 9380 12086 -268 -1471 1675 C
ATOM 1503 CG ASP A 190 -227.777 56.654 32.595 1.00 85.13 C
ANISOU 1503 CG ASP A 190 11297 8964 12086 -240 -1566 1778 C
ATOM 1504 OD1 ASP A 190 -228.293 57.073 33.654 1.00 78.67 O
ANISOU 1504 OD1 ASP A 190 10341 8054 11497 -142 -1549 1688 O
ATOM 1505 OD2 ASP A 190 -227.583 57.380 31.600 1.00 93.82 O
ANISOU 1505 OD2 ASP A 190 12496 10009 13142 -321 -1651 1946 O
ATOM 1506 N TYR A 191 -230.572 54.458 34.055 1.00 77.21 N
ANISOU 1506 N TYR A 191 10033 8048 11256 -34 -1651 1545 N
ATOM 1507 CA TYR A 191 -231.922 55.000 34.051 1.00 87.89 C
ANISOU 1507 CA TYR A 191 11272 9276 12847 30 -1800 1616 C
ATOM 1508 C TYR A 191 -232.027 56.211 34.963 1.00 87.20 C
ANISOU 1508 C TYR A 191 11063 9026 13043 105 -1750 1568 C
ATOM 1509 O TYR A 191 -233.133 56.668 35.261 1.00111.64 O
ANISOU 1509 O TYR A 191 14023 12001 16394 182 -1826 1580 O
ATOM 1510 CB TYR A 191 -232.944 53.924 34.442 1.00 91.48 C
ANISOU 1510 CB TYR A 191 11641 9796 13322 77 -1822 1532 C
ATOM 1511 CG TYR A 191 -232.517 53.014 35.570 1.00 84.10 C
ANISOU 1511 CG TYR A 191 10675 8964 12317 107 -1639 1333 C
ATOM 1512 CD1 TYR A 191 -232.846 53.306 36.887 1.00100.01 C
ANISOU 1512 CD1 TYR A 191 12554 10919 14525 185 -1537 1195 C
ATOM 1513 CD2 TYR A 191 -231.796 51.856 35.316 1.00 85.06 C
ANISOU 1513 CD2 TYR A 191 10904 9235 12180 50 -1568 1285 C
ATOM 1514 CE1 TYR A 191 -232.458 52.474 37.923 1.00100.53 C
ANISOU 1514 CE1 TYR A 191 12606 11083 14509 195 -1386 1031 C
ATOM 1515 CE2 TYR A 191 -231.401 51.019 36.345 1.00 92.07 C
ANISOU 1515 CE2 TYR A 191 11761 10205 13016 77 -1420 1125 C
ATOM 1516 CZ TYR A 191 -231.736 51.336 37.647 1.00100.27 C
ANISOU 1516 CZ TYR A 191 12676 11193 14230 144 -1339 1008 C
ATOM 1517 OH TYR A 191 -231.355 50.513 38.681 1.00120.79 O
ANISOU 1517 OH TYR A 191 15256 13877 16763 155 -1209 867 O
ATOM 1518 N TYR A 192 -230.890 56.739 35.405 1.00103.85 N
ANISOU 1518 N TYR A 192 13212 11124 15121 81 -1617 1508 N
ATOM 1519 CA TYR A 192 -230.830 57.952 36.204 1.00106.61 C
ANISOU 1519 CA TYR A 192 13473 11315 15717 130 -1559 1456 C
ATOM 1520 C TYR A 192 -230.647 59.207 35.364 1.00103.17 C
ANISOU 1520 C TYR A 192 13086 10732 15380 95 -1665 1637 C
ATOM 1521 O TYR A 192 -230.857 60.312 35.873 1.00101.84 O
ANISOU 1521 O TYR A 192 12834 10391 15471 144 -1653 1620 O
ATOM 1522 CB TYR A 192 -229.679 57.852 37.212 1.00 77.66 C
ANISOU 1522 CB TYR A 192 9823 7718 11968 110 -1367 1289 C
ATOM 1523 CG TYR A 192 -229.426 56.437 37.673 1.00 87.22 C
ANISOU 1523 CG TYR A 192 11050 9112 12979 104 -1279 1168 C
ATOM 1524 CD1 TYR A 192 -230.260 55.832 38.603 1.00 85.84 C
ANISOU 1524 CD1 TYR A 192 10774 8961 12881 167 -1237 1039 C
ATOM 1525 CD2 TYR A 192 -228.361 55.701 37.168 1.00 76.66 C
ANISOU 1525 CD2 TYR A 192 9825 7914 11389 32 -1231 1185 C
ATOM 1526 CE1 TYR A 192 -230.038 54.540 39.027 1.00 88.79 C
ANISOU 1526 CE1 TYR A 192 11166 9488 13080 157 -1166 943 C
ATOM 1527 CE2 TYR A 192 -228.131 54.408 37.585 1.00100.97 C
ANISOU 1527 CE2 TYR A 192 12911 11138 14315 33 -1157 1082 C
ATOM 1528 CZ TYR A 192 -228.975 53.830 38.516 1.00103.36 C
ANISOU 1528 CZ TYR A 192 13120 11458 14692 95 -1132 969 C
ATOM 1529 OH TYR A 192 -228.760 52.538 38.943 1.00109.06 O
ANISOU 1529 OH TYR A 192 13854 12314 15270 92 -1066 880 O
ATOM 1530 N THR A 193 -230.261 59.063 34.098 1.00 96.76 N
ANISOU 1530 N THR A 193 12415 9980 14369 2 -1763 1806 N
ATOM 1531 CA THR A 193 -229.931 60.181 33.234 1.00 87.76 C
ANISOU 1531 CA THR A 193 11354 8721 13271 -60 -1858 1994 C
ATOM 1532 C THR A 193 -230.769 60.121 31.965 1.00 93.28 C
ANISOU 1532 C THR A 193 12110 9404 13930 -101 -2087 2214 C
ATOM 1533 O THR A 193 -230.803 59.075 31.302 1.00107.63 O
ANISOU 1533 O THR A 193 14020 11379 15496 -163 -2124 2238 O
ATOM 1534 CB THR A 193 -228.431 60.165 32.862 1.00 67.51 C
ANISOU 1534 CB THR A 193 8934 6253 10466 -173 -1739 1999 C
ATOM 1535 OG1 THR A 193 -227.644 60.527 34.003 1.00 90.45 O
ANISOU 1535 OG1 THR A 193 11777 9135 13455 -146 -1565 1831 O
ATOM 1536 CG2 THR A 193 -228.142 61.109 31.714 1.00 89.56 C
ANISOU 1536 CG2 THR A 193 11842 8954 13234 -269 -1853 2225 C
ATOM 1537 N PRO A 194 -231.441 61.184 31.597 1.00 97.10 N
ANISOU 1537 N PRO A 194 12545 9699 14651 -75 -2247 2376 N
ATOM 1538 CA PRO A 194 -232.160 61.221 30.307 1.00 97.89 C
ANISOU 1538 CA PRO A 194 12715 9780 14700 -136 -2497 2622 C
ATOM 1539 C PRO A 194 -231.225 61.573 29.157 1.00104.24 C
ANISOU 1539 C PRO A 194 13729 10621 15254 -294 -2537 2800 C
ATOM 1540 O PRO A 194 -231.337 62.613 28.501 1.00133.97 O
ANISOU 1540 O PRO A 194 17536 14239 19128 -336 -2685 3010 O
ATOM 1541 CB PRO A 194 -233.219 62.298 30.557 1.00 97.59 C
ANISOU 1541 CB PRO A 194 12507 9497 15075 -28 -2640 2714 C
ATOM 1542 CG PRO A 194 -232.545 63.246 31.484 1.00 81.60 C
ANISOU 1542 CG PRO A 194 10427 7341 13238 21 -2467 2595 C
ATOM 1543 CD PRO A 194 -231.636 62.423 32.371 1.00 93.27 C
ANISOU 1543 CD PRO A 194 11929 8992 14516 13 -2217 2344 C
ATOM 1544 N HIS A 195 -230.265 60.684 28.904 1.00100.58 N
ANISOU 1544 N HIS A 195 13403 10356 14457 -388 -2395 2714 N
ATOM 1545 CA HIS A 195 -229.201 60.925 27.930 1.00 91.61 C
ANISOU 1545 CA HIS A 195 12467 9279 13063 -548 -2364 2834 C
ATOM 1546 C HIS A 195 -229.785 60.783 26.531 1.00 99.46 C
ANISOU 1546 C HIS A 195 13603 10306 13880 -668 -2592 3067 C
ATOM 1547 O HIS A 195 -230.012 59.671 26.049 1.00119.48 O
ANISOU 1547 O HIS A 195 16215 13002 16180 -723 -2614 3036 O
ATOM 1548 CB HIS A 195 -228.044 59.960 28.158 1.00 85.80 C
ANISOU 1548 CB HIS A 195 11803 8735 12063 -598 -2125 2649 C
ATOM 1549 CG HIS A 195 -226.699 60.544 27.859 1.00104.97 C
ANISOU 1549 CG HIS A 195 14340 11168 14377 -706 -1990 2679 C
ATOM 1550 ND1 HIS A 195 -225.805 59.953 26.991 1.00104.19 N
ANISOU 1550 ND1 HIS A 195 14412 11223 13954 -851 -1894 2694 N
ATOM 1551 CD2 HIS A 195 -226.094 61.667 28.315 1.00107.97 C
ANISOU 1551 CD2 HIS A 195 14679 11414 14932 -696 -1925 2688 C
ATOM 1552 CE1 HIS A 195 -224.707 60.685 26.926 1.00 95.25 C
ANISOU 1552 CE1 HIS A 195 13328 10055 12807 -924 -1775 2718 C
ATOM 1553 NE2 HIS A 195 -224.857 61.732 27.719 1.00105.17 N
ANISOU 1553 NE2 HIS A 195 14461 11139 14361 -835 -1798 2718 N
ATOM 1554 N GLU A 196 -230.035 61.915 25.874 1.00113.80 N
ANISOU 1554 N GLU A 196 15462 11966 15811 -717 -2771 3307 N
ATOM 1555 CA GLU A 196 -230.651 61.884 24.551 1.00116.81 C
ANISOU 1555 CA GLU A 196 15982 12368 16034 -843 -3026 3559 C
ATOM 1556 C GLU A 196 -229.743 61.225 23.520 1.00110.41 C
ANISOU 1556 C GLU A 196 15423 11754 14776 -1045 -2943 3585 C
ATOM 1557 O GLU A 196 -230.233 60.629 22.555 1.00121.00 O
ANISOU 1557 O GLU A 196 16891 13196 15886 -1159 -3097 3696 O
ATOM 1558 CB GLU A 196 -231.012 63.304 24.106 1.00115.00 C
ANISOU 1558 CB GLU A 196 15748 11913 16035 -858 -3234 3825 C
ATOM 1559 CG GLU A 196 -231.901 64.064 25.080 1.00129.09 C
ANISOU 1559 CG GLU A 196 17279 13472 18299 -660 -3303 3798 C
ATOM 1560 CD GLU A 196 -232.183 65.486 24.619 1.00164.44 C
ANISOU 1560 CD GLU A 196 21751 17703 23025 -673 -3503 4066 C
ATOM 1561 OE1 GLU A 196 -231.934 65.793 23.432 1.00165.67 O
ANISOU 1561 OE1 GLU A 196 22093 17895 22957 -841 -3631 4287 O
ATOM 1562 OE2 GLU A 196 -232.648 66.301 25.442 1.00178.21 O
ANISOU 1562 OE2 GLU A 196 23299 19232 25180 -519 -3506 4029 O
ATOM 1563 N GLU A 197 -228.424 61.315 23.710 1.00105.82 N
ANISOU 1563 N GLU A 197 14909 11227 14069 -1097 -2695 3477 N
ATOM 1564 CA GLU A 197 -227.492 60.842 22.692 1.00112.32 C
ANISOU 1564 CA GLU A 197 15967 12214 14496 -1297 -2592 3507 C
ATOM 1565 C GLU A 197 -227.508 59.326 22.575 1.00112.95 C
ANISOU 1565 C GLU A 197 16094 12499 14322 -1320 -2495 3333 C
ATOM 1566 O GLU A 197 -227.187 58.785 21.511 1.00125.36 O
ANISOU 1566 O GLU A 197 17872 14206 15553 -1497 -2482 3383 O
ATOM 1567 CB GLU A 197 -226.080 61.337 23.006 1.00109.19 C
ANISOU 1567 CB GLU A 197 15595 11813 14080 -1336 -2341 3425 C
ATOM 1568 CG GLU A 197 -226.035 62.774 23.490 1.00119.11 C
ANISOU 1568 CG GLU A 197 16755 12848 15654 -1272 -2392 3526 C
ATOM 1569 CD GLU A 197 -224.665 63.175 23.993 1.00146.81 C
ANISOU 1569 CD GLU A 197 20253 16356 19171 -1295 -2137 3407 C
ATOM 1570 OE1 GLU A 197 -223.660 62.812 23.344 1.00163.02 O
ANISOU 1570 OE1 GLU A 197 22455 18545 20939 -1446 -1983 3392 O
ATOM 1571 OE2 GLU A 197 -224.594 63.848 25.044 1.00147.57 O
ANISOU 1571 OE2 GLU A 197 20188 16317 19567 -1169 -2086 3320 O
ATOM 1572 N THR A 198 -227.876 58.628 23.647 1.00105.39 N
ANISOU 1572 N THR A 198 14958 11564 13521 -1154 -2419 3125 N
ATOM 1573 CA THR A 198 -228.001 57.177 23.631 1.00110.24 C
ANISOU 1573 CA THR A 198 15598 12348 13941 -1158 -2341 2960 C
ATOM 1574 C THR A 198 -229.447 56.704 23.725 1.00105.60 C
ANISOU 1574 C THR A 198 14915 11744 13464 -1081 -2556 2986 C
ATOM 1575 O THR A 198 -229.680 55.499 23.860 1.00 94.80 O
ANISOU 1575 O THR A 198 13541 10497 11982 -1065 -2501 2840 O
ATOM 1576 CB THR A 198 -227.184 56.563 24.772 1.00 98.48 C
ANISOU 1576 CB THR A 198 13991 10919 12509 -1047 -2069 2694 C
ATOM 1577 OG1 THR A 198 -227.561 57.166 26.016 1.00106.37 O
ANISOU 1577 OG1 THR A 198 14778 11786 13853 -873 -2076 2630 O
ATOM 1578 CG2 THR A 198 -225.710 56.788 24.542 1.00 73.59 C
ANISOU 1578 CG2 THR A 198 10936 7816 9209 -1145 -1849 2656 C
ATOM 1579 N ASN A 199 -230.416 57.616 23.654 1.00101.34 N
ANISOU 1579 N ASN A 199 14293 11050 13162 -1034 -2799 3171 N
ATOM 1580 CA ASN A 199 -231.839 57.295 23.773 1.00 95.41 C
ANISOU 1580 CA ASN A 199 13417 10262 12573 -953 -3015 3211 C
ATOM 1581 C ASN A 199 -232.111 56.445 25.016 1.00 98.06 C
ANISOU 1581 C ASN A 199 13568 10637 13054 -791 -2867 2955 C
ATOM 1582 O ASN A 199 -232.624 55.326 24.946 1.00 92.48 O
ANISOU 1582 O ASN A 199 12862 10042 12233 -799 -2887 2869 O
ATOM 1583 CB ASN A 199 -232.350 56.601 22.510 1.00 89.47 C
ANISOU 1583 CB ASN A 199 12842 9629 11525 -1121 -3201 3338 C
ATOM 1584 CG ASN A 199 -232.189 57.456 21.276 1.00104.97 C
ANISOU 1584 CG ASN A 199 14998 11553 13335 -1297 -3376 3615 C
ATOM 1585 OD1 ASN A 199 -233.078 58.231 20.922 1.00125.40 O
ANISOU 1585 OD1 ASN A 199 17536 14010 16100 -1293 -3655 3843 O
ATOM 1586 ND2 ASN A 199 -231.045 57.328 20.616 1.00101.40 N
ANISOU 1586 ND2 ASN A 199 14760 11207 12558 -1458 -3212 3602 N
ATOM 1587 N ASN A 200 -231.751 57.007 26.172 1.00 87.90 N
ANISOU 1587 N ASN A 200 12129 9254 12015 -656 -2716 2835 N
ATOM 1588 CA ASN A 200 -232.005 56.322 27.434 1.00 93.43 C
ANISOU 1588 CA ASN A 200 12657 9981 12860 -511 -2576 2604 C
ATOM 1589 C ASN A 200 -233.496 56.079 27.647 1.00 99.35 C
ANISOU 1589 C ASN A 200 13254 10678 13817 -425 -2758 2630 C
ATOM 1590 O ASN A 200 -233.894 55.031 28.168 1.00114.86 O
ANISOU 1590 O ASN A 200 15150 12732 15760 -375 -2696 2477 O
ATOM 1591 CB ASN A 200 -231.423 57.130 28.594 1.00 82.69 C
ANISOU 1591 CB ASN A 200 11174 8513 11731 -404 -2410 2491 C
ATOM 1592 CG ASN A 200 -229.920 57.002 28.690 1.00 87.00 C
ANISOU 1592 CG ASN A 200 11827 9149 12081 -468 -2185 2393 C
ATOM 1593 OD1 ASN A 200 -229.262 56.577 27.741 1.00 90.51 O
ANISOU 1593 OD1 ASN A 200 12446 9705 12238 -602 -2156 2444 O
ATOM 1594 ND2 ASN A 200 -229.367 57.365 29.843 1.00 92.80 N
ANISOU 1594 ND2 ASN A 200 12453 9835 12973 -381 -2020 2246 N
ATOM 1595 N GLU A 201 -234.334 57.032 27.237 1.00 94.55 N
ANISOU 1595 N GLU A 201 12584 9918 13424 -409 -2987 2831 N
ATOM 1596 CA GLU A 201 -235.763 56.932 27.509 1.00 93.14 C
ANISOU 1596 CA GLU A 201 12219 9665 13507 -313 -3156 2858 C
ATOM 1597 C GLU A 201 -236.376 55.723 26.814 1.00100.15 C
ANISOU 1597 C GLU A 201 13176 10703 14172 -400 -3279 2874 C
ATOM 1598 O GLU A 201 -237.214 55.024 27.396 1.00102.42 O
ANISOU 1598 O GLU A 201 13318 11014 14581 -320 -3282 2763 O
ATOM 1599 CB GLU A 201 -236.461 58.221 27.078 1.00109.03 C
ANISOU 1599 CB GLU A 201 14153 11472 15799 -288 -3395 3096 C
ATOM 1600 CG GLU A 201 -237.954 58.250 27.334 1.00122.67 C
ANISOU 1600 CG GLU A 201 15657 13096 17855 -182 -3580 3141 C
ATOM 1601 CD GLU A 201 -238.567 59.596 27.004 1.00140.44 C
ANISOU 1601 CD GLU A 201 17807 15115 20440 -137 -3801 3373 C
ATOM 1602 OE1 GLU A 201 -237.803 60.569 26.828 1.00146.52 O
ANISOU 1602 OE1 GLU A 201 18663 15787 21223 -165 -3768 3462 O
ATOM 1603 OE2 GLU A 201 -239.810 59.681 26.917 1.00148.67 O
ANISOU 1603 OE2 GLU A 201 18676 16065 21746 -74 -4009 3471 O
ATOM 1604 N SER A 202 -235.962 55.450 25.576 1.00 94.48 N
ANISOU 1604 N SER A 202 12688 10089 13120 -574 -3369 3003 N
ATOM 1605 CA SER A 202 -236.500 54.293 24.870 1.00 88.13 C
ANISOU 1605 CA SER A 202 11975 9430 12082 -678 -3480 3007 C
ATOM 1606 C SER A 202 -235.998 52.983 25.471 1.00 92.67 C
ANISOU 1606 C SER A 202 12571 10155 12484 -660 -3232 2744 C
ATOM 1607 O SER A 202 -236.728 51.986 25.477 1.00 93.70 O
ANISOU 1607 O SER A 202 12664 10362 12576 -666 -3287 2676 O
ATOM 1608 CB SER A 202 -236.147 54.369 23.385 1.00 90.12 C
ANISOU 1608 CB SER A 202 12488 9755 11997 -891 -3626 3202 C
ATOM 1609 OG SER A 202 -234.752 54.234 23.183 1.00107.85 O
ANISOU 1609 OG SER A 202 14919 12093 13968 -977 -3390 3115 O
ATOM 1610 N PHE A 203 -234.769 52.961 25.988 1.00 80.82 N
ANISOU 1610 N PHE A 203 11121 8691 10894 -640 -2967 2600 N
ATOM 1611 CA PHE A 203 -234.259 51.728 26.575 1.00 79.97 C
ANISOU 1611 CA PHE A 203 11025 8711 10647 -617 -2743 2367 C
ATOM 1612 C PHE A 203 -234.958 51.411 27.889 1.00 82.44 C
ANISOU 1612 C PHE A 203 11110 8981 11230 -455 -2682 2217 C
ATOM 1613 O PHE A 203 -235.239 50.242 28.181 1.00 71.03 O
ANISOU 1613 O PHE A 203 9648 7629 9713 -447 -2624 2084 O
ATOM 1614 CB PHE A 203 -232.749 51.820 26.782 1.00 77.90 C
ANISOU 1614 CB PHE A 203 10859 8494 10245 -639 -2493 2268 C
ATOM 1615 CG PHE A 203 -232.103 50.499 27.093 1.00 78.49 C
ANISOU 1615 CG PHE A 203 10982 8704 10137 -647 -2285 2064 C
ATOM 1616 CD1 PHE A 203 -231.844 49.589 26.082 1.00 79.18 C
ANISOU 1616 CD1 PHE A 203 11256 8912 9917 -789 -2274 2055 C
ATOM 1617 CD2 PHE A 203 -231.757 50.168 28.392 1.00 63.79 C
ANISOU 1617 CD2 PHE A 203 8984 6840 8412 -520 -2102 1883 C
ATOM 1618 CE1 PHE A 203 -231.248 48.371 26.360 1.00 83.93 C
ANISOU 1618 CE1 PHE A 203 11893 9615 10381 -788 -2079 1866 C
ATOM 1619 CE2 PHE A 203 -231.156 48.954 28.676 1.00 80.63 C
ANISOU 1619 CE2 PHE A 203 11156 9082 10398 -525 -1926 1715 C
ATOM 1620 CZ PHE A 203 -230.905 48.052 27.659 1.00 83.32 C
ANISOU 1620 CZ PHE A 203 11667 9526 10463 -651 -1912 1705 C
ATOM 1621 N VAL A 204 -235.237 52.435 28.699 1.00 90.28 N
ANISOU 1621 N VAL A 204 11935 9831 12535 -334 -2683 2230 N
ATOM 1622 CA VAL A 204 -235.951 52.215 29.955 1.00 92.19 C
ANISOU 1622 CA VAL A 204 11964 10028 13036 -193 -2614 2085 C
ATOM 1623 C VAL A 204 -237.328 51.623 29.683 1.00 93.99 C
ANISOU 1623 C VAL A 204 12101 10264 13345 -192 -2800 2131 C
ATOM 1624 O VAL A 204 -237.775 50.704 30.381 1.00 76.36 O
ANISOU 1624 O VAL A 204 9779 8089 11146 -144 -2720 1984 O
ATOM 1625 CB VAL A 204 -236.044 53.529 30.754 1.00 79.07 C
ANISOU 1625 CB VAL A 204 10151 8195 11699 -80 -2584 2094 C
ATOM 1626 CG1 VAL A 204 -236.902 53.336 31.993 1.00 86.51 C
ANISOU 1626 CG1 VAL A 204 10875 9086 12908 48 -2512 1944 C
ATOM 1627 CG2 VAL A 204 -234.657 54.005 31.138 1.00 72.01 C
ANISOU 1627 CG2 VAL A 204 9337 7303 10720 -88 -2388 2023 C
ATOM 1628 N ILE A 205 -238.016 52.133 28.659 1.00 83.99 N
ANISOU 1628 N ILE A 205 10857 8942 12114 -254 -3060 2345 N
ATOM 1629 CA ILE A 205 -239.310 51.575 28.276 1.00 79.04 C
ANISOU 1629 CA ILE A 205 10146 8329 11555 -273 -3268 2409 C
ATOM 1630 C ILE A 205 -239.147 50.133 27.813 1.00 88.58 C
ANISOU 1630 C ILE A 205 11504 9715 12437 -385 -3231 2320 C
ATOM 1631 O ILE A 205 -239.903 49.241 28.216 1.00 83.90 O
ANISOU 1631 O ILE A 205 10812 9166 11901 -357 -3233 2222 O
ATOM 1632 CB ILE A 205 -239.965 52.443 27.188 1.00 73.95 C
ANISOU 1632 CB ILE A 205 9515 7592 10990 -337 -3579 2683 C
ATOM 1633 CG1 ILE A 205 -240.171 53.869 27.689 1.00 83.86 C
ANISOU 1633 CG1 ILE A 205 10604 8643 12614 -213 -3609 2766 C
ATOM 1634 CG2 ILE A 205 -241.293 51.850 26.768 1.00 67.74 C
ANISOU 1634 CG2 ILE A 205 8634 6826 10277 -368 -3815 2758 C
ATOM 1635 CD1 ILE A 205 -240.591 54.825 26.602 1.00 69.01 C
ANISOU 1635 CD1 ILE A 205 8760 6657 10805 -279 -3909 3058 C
ATOM 1636 N TYR A 206 -238.159 49.886 26.952 1.00 80.51 N
ANISOU 1636 N TYR A 206 10724 8790 11078 -517 -3188 2348 N
ATOM 1637 CA TYR A 206 -237.915 48.527 26.482 1.00 80.74 C
ANISOU 1637 CA TYR A 206 10907 8973 10799 -627 -3128 2246 C
ATOM 1638 C TYR A 206 -237.575 47.597 27.640 1.00 75.52 C
ANISOU 1638 C TYR A 206 10168 8363 10164 -533 -2876 2005 C
ATOM 1639 O TYR A 206 -238.039 46.452 27.685 1.00 85.68 O
ANISOU 1639 O TYR A 206 11453 9724 11378 -560 -2871 1910 O
ATOM 1640 CB TYR A 206 -236.794 48.526 25.446 1.00 72.18 C
ANISOU 1640 CB TYR A 206 10086 7969 9369 -780 -3074 2294 C
ATOM 1641 CG TYR A 206 -236.081 47.207 25.338 1.00 85.75 C
ANISOU 1641 CG TYR A 206 11946 9824 10811 -849 -2879 2113 C
ATOM 1642 CD1 TYR A 206 -236.652 46.144 24.656 1.00 88.37 C
ANISOU 1642 CD1 TYR A 206 12371 10245 10960 -963 -2975 2091 C
ATOM 1643 CD2 TYR A 206 -234.836 47.020 25.922 1.00 97.84 C
ANISOU 1643 CD2 TYR A 206 13509 11385 12282 -802 -2602 1963 C
ATOM 1644 CE1 TYR A 206 -236.002 44.930 24.556 1.00 90.21 C
ANISOU 1644 CE1 TYR A 206 12731 10582 10964 -1022 -2786 1916 C
ATOM 1645 CE2 TYR A 206 -234.179 45.814 25.830 1.00 85.30 C
ANISOU 1645 CE2 TYR A 206 12032 9901 10479 -853 -2424 1801 C
ATOM 1646 CZ TYR A 206 -234.763 44.773 25.145 1.00 86.38 C
ANISOU 1646 CZ TYR A 206 12265 10113 10444 -960 -2509 1774 C
ATOM 1647 OH TYR A 206 -234.100 43.572 25.057 1.00 83.90 O
ANISOU 1647 OH TYR A 206 12058 9882 9939 -1008 -2319 1604 O
ATOM 1648 N MET A 207 -236.760 48.072 28.583 1.00 65.83 N
ANISOU 1648 N MET A 207 8881 7093 9039 -431 -2673 1910 N
ATOM 1649 CA MET A 207 -236.451 47.282 29.771 1.00 81.52 C
ANISOU 1649 CA MET A 207 10788 9120 11068 -343 -2454 1702 C
ATOM 1650 C MET A 207 -237.706 47.021 30.584 1.00 85.10 C
ANISOU 1650 C MET A 207 11035 9530 11770 -253 -2509 1652 C
ATOM 1651 O MET A 207 -237.949 45.896 31.036 1.00 92.38 O
ANISOU 1651 O MET A 207 11933 10518 12649 -248 -2432 1525 O
ATOM 1652 CB MET A 207 -235.412 48.002 30.630 1.00 68.29 C
ANISOU 1652 CB MET A 207 9078 7399 9470 -263 -2264 1633 C
ATOM 1653 CG MET A 207 -234.004 47.884 30.115 1.00 83.99 C
ANISOU 1653 CG MET A 207 11246 9457 11208 -342 -2131 1615 C
ATOM 1654 SD MET A 207 -233.509 46.168 30.068 1.00100.95 S
ANISOU 1654 SD MET A 207 13497 11743 13118 -392 -1983 1453 S
ATOM 1655 CE MET A 207 -233.570 45.753 31.814 1.00 84.54 C
ANISOU 1655 CE MET A 207 11234 9648 11239 -248 -1825 1281 C
ATOM 1656 N PHE A 208 -238.514 48.060 30.782 1.00 76.91 N
ANISOU 1656 N PHE A 208 9842 8369 11010 -183 -2635 1749 N
ATOM 1657 CA PHE A 208 -239.715 47.917 31.591 1.00 83.19 C
ANISOU 1657 CA PHE A 208 10419 9111 12078 -94 -2665 1694 C
ATOM 1658 C PHE A 208 -240.694 46.936 30.963 1.00 88.67 C
ANISOU 1658 C PHE A 208 11112 9871 12709 -170 -2826 1728 C
ATOM 1659 O PHE A 208 -241.300 46.121 31.664 1.00 91.15 O
ANISOU 1659 O PHE A 208 11318 10215 13101 -136 -2761 1610 O
ATOM 1660 CB PHE A 208 -240.370 49.279 31.786 1.00 75.36 C
ANISOU 1660 CB PHE A 208 9258 7958 11418 -8 -2772 1801 C
ATOM 1661 CG PHE A 208 -241.654 49.222 32.541 1.00 76.42 C
ANISOU 1661 CG PHE A 208 9150 8023 11863 81 -2798 1748 C
ATOM 1662 CD1 PHE A 208 -241.661 48.958 33.900 1.00 74.79 C
ANISOU 1662 CD1 PHE A 208 8828 7815 11772 165 -2575 1554 C
ATOM 1663 CD2 PHE A 208 -242.856 49.436 31.895 1.00 78.51 C
ANISOU 1663 CD2 PHE A 208 9299 8225 12305 71 -3048 1895 C
ATOM 1664 CE1 PHE A 208 -242.842 48.911 34.602 1.00 86.69 C
ANISOU 1664 CE1 PHE A 208 10112 9261 13564 236 -2574 1495 C
ATOM 1665 CE2 PHE A 208 -244.043 49.389 32.590 1.00 85.22 C
ANISOU 1665 CE2 PHE A 208 9904 9008 13467 153 -3059 1841 C
ATOM 1666 CZ PHE A 208 -244.037 49.125 33.946 1.00 87.21 C
ANISOU 1666 CZ PHE A 208 10046 9260 13829 235 -2809 1634 C
ATOM 1667 N VAL A 209 -240.846 46.983 29.641 1.00 80.12 N
ANISOU 1667 N VAL A 209 10158 8816 11470 -288 -3037 1889 N
ATOM 1668 CA VAL A 209 -241.826 46.127 28.981 1.00 83.06 C
ANISOU 1668 CA VAL A 209 10530 9245 11782 -377 -3221 1933 C
ATOM 1669 C VAL A 209 -241.301 44.703 28.829 1.00 98.25 C
ANISOU 1669 C VAL A 209 12618 11306 13407 -465 -3092 1790 C
ATOM 1670 O VAL A 209 -241.946 43.742 29.263 1.00 94.17 O
ANISOU 1670 O VAL A 209 12021 10825 12933 -460 -3068 1689 O
ATOM 1671 CB VAL A 209 -242.224 46.727 27.622 1.00 85.47 C
ANISOU 1671 CB VAL A 209 10921 9530 12023 -489 -3517 2168 C
ATOM 1672 CG1 VAL A 209 -243.068 45.744 26.853 1.00 76.37 C
ANISOU 1672 CG1 VAL A 209 9812 8460 10744 -615 -3706 2202 C
ATOM 1673 CG2 VAL A 209 -242.971 48.043 27.818 1.00 78.39 C
ANISOU 1673 CG2 VAL A 209 9819 8472 11492 -388 -3673 2317 C
ATOM 1674 N VAL A 210 -240.127 44.541 28.218 1.00 97.95 N
ANISOU 1674 N VAL A 210 12805 11337 13077 -549 -2998 1777 N
ATOM 1675 CA VAL A 210 -239.670 43.209 27.832 1.00 74.27 C
ANISOU 1675 CA VAL A 210 9974 8451 9793 -650 -2901 1659 C
ATOM 1676 C VAL A 210 -239.068 42.458 29.013 1.00 82.61 C
ANISOU 1676 C VAL A 210 10981 9529 10878 -556 -2633 1458 C
ATOM 1677 O VAL A 210 -239.321 41.263 29.195 1.00 94.90 O
ANISOU 1677 O VAL A 210 12549 11138 12371 -583 -2580 1346 O
ATOM 1678 CB VAL A 210 -238.679 43.314 26.658 1.00 77.57 C
ANISOU 1678 CB VAL A 210 10649 8931 9895 -788 -2894 1717 C
ATOM 1679 CG1 VAL A 210 -237.841 42.050 26.548 1.00 86.01 C
ANISOU 1679 CG1 VAL A 210 11874 10092 10715 -850 -2692 1545 C
ATOM 1680 CG2 VAL A 210 -239.425 43.569 25.360 1.00 60.39 C
ANISOU 1680 CG2 VAL A 210 8567 6770 7609 -936 -3184 1901 C
ATOM 1681 N HIS A 211 -238.267 43.125 29.834 1.00 89.21 N
ANISOU 1681 N HIS A 211 11765 10323 11808 -452 -2470 1415 N
ATOM 1682 CA HIS A 211 -237.536 42.437 30.893 1.00 71.10 C
ANISOU 1682 CA HIS A 211 9450 8058 9509 -381 -2229 1244 C
ATOM 1683 C HIS A 211 -238.110 42.671 32.284 1.00 68.57 C
ANISOU 1683 C HIS A 211 8917 7679 9458 -254 -2163 1177 C
ATOM 1684 O HIS A 211 -237.493 42.240 33.264 1.00 83.06 O
ANISOU 1684 O HIS A 211 10731 9533 11297 -198 -1976 1052 O
ATOM 1685 CB HIS A 211 -236.058 42.857 30.870 1.00 75.83 C
ANISOU 1685 CB HIS A 211 10158 8669 9984 -377 -2069 1222 C
ATOM 1686 CG HIS A 211 -235.368 42.612 29.562 1.00 83.02 C
ANISOU 1686 CG HIS A 211 11284 9640 10619 -509 -2082 1264 C
ATOM 1687 ND1 HIS A 211 -234.588 41.499 29.328 1.00 80.29 N
ANISOU 1687 ND1 HIS A 211 11066 9365 10077 -562 -1933 1147 N
ATOM 1688 CD2 HIS A 211 -235.326 43.346 28.425 1.00 84.78 C
ANISOU 1688 CD2 HIS A 211 11622 9860 10729 -606 -2216 1409 C
ATOM 1689 CE1 HIS A 211 -234.104 41.553 28.100 1.00 80.53 C
ANISOU 1689 CE1 HIS A 211 11280 9436 9879 -690 -1958 1200 C
ATOM 1690 NE2 HIS A 211 -234.538 42.664 27.531 1.00 79.40 N
ANISOU 1690 NE2 HIS A 211 11142 9258 9769 -725 -2134 1365 N
ATOM 1691 N PHE A 212 -239.262 43.329 32.402 1.00 86.61 N
ANISOU 1691 N PHE A 212 11044 9892 11973 -214 -2309 1254 N
ATOM 1692 CA PHE A 212 -239.806 43.597 33.727 1.00 94.72 C
ANISOU 1692 CA PHE A 212 11871 10860 13257 -103 -2218 1173 C
ATOM 1693 C PHE A 212 -241.282 43.230 33.809 1.00103.26 C
ANISOU 1693 C PHE A 212 12797 11921 14517 -103 -2343 1186 C
ATOM 1694 O PHE A 212 -241.745 42.757 34.850 1.00112.15 O
ANISOU 1694 O PHE A 212 13800 13046 15764 -54 -2231 1073 O
ATOM 1695 CB PHE A 212 -239.580 45.065 34.113 1.00 96.05 C
ANISOU 1695 CB PHE A 212 11956 10927 13610 -22 -2201 1223 C
ATOM 1696 CG PHE A 212 -239.949 45.382 35.539 1.00 99.16 C
ANISOU 1696 CG PHE A 212 12172 11263 14240 80 -2062 1109 C
ATOM 1697 CD1 PHE A 212 -239.125 44.994 36.582 1.00 88.54 C
ANISOU 1697 CD1 PHE A 212 10856 9963 12823 107 -1850 968 C
ATOM 1698 CD2 PHE A 212 -241.106 46.087 35.836 1.00110.94 C
ANISOU 1698 CD2 PHE A 212 13467 12653 16031 142 -2142 1142 C
ATOM 1699 CE1 PHE A 212 -239.455 45.287 37.893 1.00 93.68 C
ANISOU 1699 CE1 PHE A 212 11366 10570 13659 177 -1718 859 C
ATOM 1700 CE2 PHE A 212 -241.440 46.385 37.148 1.00108.76 C
ANISOU 1700 CE2 PHE A 212 13036 12324 15963 222 -1987 1017 C
ATOM 1701 CZ PHE A 212 -240.611 45.983 38.177 1.00104.90 C
ANISOU 1701 CZ PHE A 212 12602 11893 15363 231 -1774 874 C
ATOM 1702 N ILE A 213 -242.027 43.418 32.725 1.00 92.03 N
ANISOU 1702 N ILE A 213 11377 10484 13106 -167 -2577 1326 N
ATOM 1703 CA ILE A 213 -243.457 43.106 32.692 1.00 83.32 C
ANISOU 1703 CA ILE A 213 10111 9359 12188 -175 -2726 1357 C
ATOM 1704 C ILE A 213 -243.714 41.715 32.126 1.00 92.72 C
ANISOU 1704 C ILE A 213 11406 10648 13174 -291 -2779 1319 C
ATOM 1705 O ILE A 213 -244.464 40.930 32.708 1.00 82.39 O
ANISOU 1705 O ILE A 213 9987 9354 11963 -286 -2743 1235 O
ATOM 1706 CB ILE A 213 -244.239 44.180 31.900 1.00 84.84 C
ANISOU 1706 CB ILE A 213 10210 9462 12561 -176 -2983 1548 C
ATOM 1707 CG1 ILE A 213 -244.184 45.543 32.603 1.00 91.34 C
ANISOU 1707 CG1 ILE A 213 10888 10157 13659 -48 -2920 1567 C
ATOM 1708 CG2 ILE A 213 -245.682 43.735 31.699 1.00 75.80 C
ANISOU 1708 CG2 ILE A 213 8903 8308 11590 -205 -3164 1593 C
ATOM 1709 CD1 ILE A 213 -244.931 45.605 33.923 1.00 98.97 C
ANISOU 1709 CD1 ILE A 213 11616 11062 14928 61 -2780 1439 C
ATOM 1710 N ILE A 214 -243.100 41.398 30.982 1.00 90.10 N
ANISOU 1710 N ILE A 214 11295 10381 12557 -405 -2855 1375 N
ATOM 1711 CA ILE A 214 -243.249 40.061 30.402 1.00 79.91 C
ANISOU 1711 CA ILE A 214 10130 9177 11054 -527 -2888 1320 C
ATOM 1712 C ILE A 214 -242.815 38.953 31.360 1.00 90.08 C
ANISOU 1712 C ILE A 214 11431 10503 12293 -493 -2650 1137 C
ATOM 1713 O ILE A 214 -243.572 37.984 31.524 1.00 92.36 O
ANISOU 1713 O ILE A 214 11668 10814 12611 -534 -2673 1078 O
ATOM 1714 CB ILE A 214 -242.513 39.991 29.051 1.00 77.56 C
ANISOU 1714 CB ILE A 214 10088 8939 10441 -661 -2966 1389 C
ATOM 1715 CG1 ILE A 214 -243.171 40.910 28.017 1.00 58.92 C
ANISOU 1715 CG1 ILE A 214 7722 6549 8116 -729 -3254 1595 C
ATOM 1716 CG2 ILE A 214 -242.416 38.556 28.564 1.00 69.68 C
ANISOU 1716 CG2 ILE A 214 9246 8024 9205 -783 -2932 1285 C
ATOM 1717 CD1 ILE A 214 -244.668 40.823 27.988 1.00 98.50 C
ANISOU 1717 CD1 ILE A 214 12545 11530 13349 -739 -3473 1667 C
ATOM 1718 N PRO A 215 -241.636 39.010 32.002 1.00 87.29 N
ANISOU 1718 N PRO A 215 11141 10155 11869 -428 -2433 1051 N
ATOM 1719 CA PRO A 215 -241.275 37.915 32.921 1.00 80.86 C
ANISOU 1719 CA PRO A 215 10333 9371 11021 -401 -2235 899 C
ATOM 1720 C PRO A 215 -242.301 37.693 34.015 1.00 83.00 C
ANISOU 1720 C PRO A 215 10400 9611 11526 -343 -2205 847 C
ATOM 1721 O PRO A 215 -242.558 36.546 34.403 1.00101.90 O
ANISOU 1721 O PRO A 215 12795 12031 13891 -375 -2139 759 O
ATOM 1722 CB PRO A 215 -239.924 38.367 33.494 1.00 81.32 C
ANISOU 1722 CB PRO A 215 10447 9425 11026 -328 -2047 854 C
ATOM 1723 CG PRO A 215 -239.359 39.262 32.450 1.00 88.83 C
ANISOU 1723 CG PRO A 215 11510 10373 11867 -367 -2134 961 C
ATOM 1724 CD PRO A 215 -240.542 39.996 31.887 1.00 85.09 C
ANISOU 1724 CD PRO A 215 10940 9859 11532 -388 -2365 1094 C
ATOM 1725 N LEU A 216 -242.910 38.769 34.515 1.00 80.16 N
ANISOU 1725 N LEU A 216 9863 9188 11406 -264 -2244 896 N
ATOM 1726 CA LEU A 216 -243.902 38.630 35.572 1.00 77.82 C
ANISOU 1726 CA LEU A 216 9364 8861 11344 -214 -2190 834 C
ATOM 1727 C LEU A 216 -245.172 37.966 35.058 1.00 90.54 C
ANISOU 1727 C LEU A 216 10894 10481 13026 -290 -2354 867 C
ATOM 1728 O LEU A 216 -245.739 37.096 35.729 1.00 96.40 O
ANISOU 1728 O LEU A 216 11560 11239 13829 -306 -2278 782 O
ATOM 1729 CB LEU A 216 -244.222 39.997 36.169 1.00 84.03 C
ANISOU 1729 CB LEU A 216 9979 9563 12386 -112 -2177 865 C
ATOM 1730 CG LEU A 216 -245.250 39.972 37.298 1.00 84.32 C
ANISOU 1730 CG LEU A 216 9796 9561 12681 -62 -2090 786 C
ATOM 1731 CD1 LEU A 216 -244.596 39.576 38.604 1.00 92.85 C
ANISOU 1731 CD1 LEU A 216 10903 10670 13705 -31 -1841 647 C
ATOM 1732 CD2 LEU A 216 -245.931 41.309 37.431 1.00 84.28 C
ANISOU 1732 CD2 LEU A 216 9600 9451 12972 19 -2153 845 C
ATOM 1733 N ILE A 217 -245.636 38.363 33.871 1.00 78.23 N
ANISOU 1733 N ILE A 217 9351 8914 11459 -349 -2588 997 N
ATOM 1734 CA ILE A 217 -246.865 37.784 33.335 1.00 77.65 C
ANISOU 1734 CA ILE A 217 9193 8851 11460 -433 -2774 1041 C
ATOM 1735 C ILE A 217 -246.677 36.295 33.069 1.00 88.64 C
ANISOU 1735 C ILE A 217 10738 10316 12625 -542 -2732 952 C
ATOM 1736 O ILE A 217 -247.538 35.471 33.403 1.00 85.92 O
ANISOU 1736 O ILE A 217 10296 9979 12371 -582 -2738 899 O
ATOM 1737 CB ILE A 217 -247.305 38.536 32.066 1.00 72.19 C
ANISOU 1737 CB ILE A 217 8511 8140 10779 -490 -3058 1218 C
ATOM 1738 CG1 ILE A 217 -247.537 40.016 32.370 1.00 86.78 C
ANISOU 1738 CG1 ILE A 217 10189 9888 12896 -373 -3100 1310 C
ATOM 1739 CG2 ILE A 217 -248.571 37.920 31.500 1.00 74.42 C
ANISOU 1739 CG2 ILE A 217 8701 8438 11138 -590 -3273 1269 C
ATOM 1740 CD1 ILE A 217 -248.530 40.260 33.481 1.00 94.61 C
ANISOU 1740 CD1 ILE A 217 10896 10810 14241 -275 -3025 1251 C
ATOM 1741 N VAL A 218 -245.542 35.928 32.473 1.00 77.72 N
ANISOU 1741 N VAL A 218 9593 8978 10957 -593 -2676 928 N
ATOM 1742 CA VAL A 218 -245.295 34.528 32.141 1.00 90.15 C
ANISOU 1742 CA VAL A 218 11325 10604 12324 -696 -2627 836 C
ATOM 1743 C VAL A 218 -245.235 33.685 33.407 1.00 84.18 C
ANISOU 1743 C VAL A 218 10504 9840 11640 -642 -2417 706 C
ATOM 1744 O VAL A 218 -245.874 32.631 33.506 1.00 81.79 O
ANISOU 1744 O VAL A 218 10182 9547 11348 -711 -2426 649 O
ATOM 1745 CB VAL A 218 -244.008 34.395 31.314 1.00 73.40 C
ANISOU 1745 CB VAL A 218 9457 8520 9911 -748 -2573 823 C
ATOM 1746 CG1 VAL A 218 -243.573 32.950 31.274 1.00 74.68 C
ANISOU 1746 CG1 VAL A 218 9762 8709 9904 -817 -2450 693 C
ATOM 1747 CG2 VAL A 218 -244.244 34.910 29.915 1.00 66.95 C
ANISOU 1747 CG2 VAL A 218 8740 7727 8971 -857 -2804 950 C
ATOM 1748 N ILE A 219 -244.470 34.143 34.396 1.00 67.96 N
ANISOU 1748 N ILE A 219 8421 7767 9633 -531 -2232 663 N
ATOM 1749 CA ILE A 219 -244.339 33.401 35.644 1.00 81.34 C
ANISOU 1749 CA ILE A 219 10070 9458 11377 -490 -2039 555 C
ATOM 1750 C ILE A 219 -245.695 33.238 36.318 1.00 89.30 C
ANISOU 1750 C ILE A 219 10871 10446 12612 -494 -2065 543 C
ATOM 1751 O ILE A 219 -246.021 32.163 36.838 1.00100.01 O
ANISOU 1751 O ILE A 219 12218 11811 13972 -537 -1990 471 O
ATOM 1752 CB ILE A 219 -243.317 34.095 36.562 1.00 73.99 C
ANISOU 1752 CB ILE A 219 9140 8516 10457 -382 -1867 528 C
ATOM 1753 CG1 ILE A 219 -241.901 33.835 36.045 1.00 89.52 C
ANISOU 1753 CG1 ILE A 219 11310 10505 12197 -391 -1797 510 C
ATOM 1754 CG2 ILE A 219 -243.470 33.626 37.995 1.00 74.76 C
ANISOU 1754 CG2 ILE A 219 9145 8607 10653 -344 -1700 444 C
ATOM 1755 CD1 ILE A 219 -240.813 34.379 36.936 1.00 96.53 C
ANISOU 1755 CD1 ILE A 219 12204 11388 13085 -300 -1636 482 C
ATOM 1756 N PHE A 220 -246.517 34.289 36.300 1.00 83.67 N
ANISOU 1756 N PHE A 220 9983 9699 12107 -451 -2171 613 N
ATOM 1757 CA PHE A 220 -247.826 34.202 36.937 1.00 80.29 C
ANISOU 1757 CA PHE A 220 9332 9247 11927 -451 -2181 595 C
ATOM 1758 C PHE A 220 -248.776 33.311 36.148 1.00 80.31 C
ANISOU 1758 C PHE A 220 9320 9269 11925 -571 -2352 620 C
ATOM 1759 O PHE A 220 -249.541 32.538 36.735 1.00 82.54 O
ANISOU 1759 O PHE A 220 9500 9551 12308 -611 -2298 560 O
ATOM 1760 CB PHE A 220 -248.418 35.595 37.110 1.00 77.50 C
ANISOU 1760 CB PHE A 220 8781 8833 11831 -365 -2241 660 C
ATOM 1761 CG PHE A 220 -248.202 36.174 38.475 1.00 92.50 C
ANISOU 1761 CG PHE A 220 10581 10702 13863 -267 -2021 577 C
ATOM 1762 CD1 PHE A 220 -247.001 36.778 38.808 1.00109.87 C
ANISOU 1762 CD1 PHE A 220 12895 12902 15950 -202 -1904 559 C
ATOM 1763 CD2 PHE A 220 -249.205 36.120 39.426 1.00102.57 C
ANISOU 1763 CD2 PHE A 220 11649 11951 15370 -253 -1925 512 C
ATOM 1764 CE1 PHE A 220 -246.806 37.315 40.069 1.00111.96 C
ANISOU 1764 CE1 PHE A 220 13081 13142 16319 -131 -1708 477 C
ATOM 1765 CE2 PHE A 220 -249.016 36.654 40.686 1.00106.23 C
ANISOU 1765 CE2 PHE A 220 12038 12392 15933 -183 -1711 423 C
ATOM 1766 CZ PHE A 220 -247.816 37.255 41.007 1.00110.26 C
ANISOU 1766 CZ PHE A 220 12674 12903 16315 -125 -1609 406 C
ATOM 1767 N PHE A 221 -248.746 33.402 34.819 1.00 76.81 N
ANISOU 1767 N PHE A 221 8984 8843 11356 -643 -2558 707 N
ATOM 1768 CA PHE A 221 -249.632 32.566 34.014 1.00 81.72 C
ANISOU 1768 CA PHE A 221 9607 9488 11954 -777 -2739 729 C
ATOM 1769 C PHE A 221 -249.256 31.096 34.135 1.00 87.01 C
ANISOU 1769 C PHE A 221 10434 10188 12440 -859 -2621 616 C
ATOM 1770 O PHE A 221 -250.100 30.253 34.455 1.00102.24 O
ANISOU 1770 O PHE A 221 12272 12113 14462 -923 -2622 571 O
ATOM 1771 CB PHE A 221 -249.592 33.009 32.554 1.00 80.51 C
ANISOU 1771 CB PHE A 221 9567 9355 11666 -856 -2987 850 C
ATOM 1772 CG PHE A 221 -250.259 32.049 31.610 1.00 74.65 C
ANISOU 1772 CG PHE A 221 8894 8651 10818 -1022 -3170 859 C
ATOM 1773 CD1 PHE A 221 -251.633 32.075 31.427 1.00 81.02 C
ANISOU 1773 CD1 PHE A 221 9497 9445 11841 -1075 -3369 927 C
ATOM 1774 CD2 PHE A 221 -249.510 31.127 30.893 1.00 76.88 C
ANISOU 1774 CD2 PHE A 221 9441 8977 10794 -1131 -3143 794 C
ATOM 1775 CE1 PHE A 221 -252.248 31.196 30.553 1.00 78.01 C
ANISOU 1775 CE1 PHE A 221 9182 9101 11356 -1244 -3551 934 C
ATOM 1776 CE2 PHE A 221 -250.119 30.245 30.018 1.00 88.94 C
ANISOU 1776 CE2 PHE A 221 11045 10534 12212 -1299 -3307 788 C
ATOM 1777 CZ PHE A 221 -251.489 30.280 29.847 1.00 82.38 C
ANISOU 1777 CZ PHE A 221 10019 9699 11582 -1361 -3520 861 C
ATOM 1778 N CYS A 222 -247.987 30.775 33.875 1.00 96.66 N
ANISOU 1778 N CYS A 222 11882 11428 13417 -859 -2516 571 N
ATOM 1779 CA CYS A 222 -247.537 29.387 33.905 1.00 80.91 C
ANISOU 1779 CA CYS A 222 10043 9440 11260 -931 -2405 466 C
ATOM 1780 C CYS A 222 -247.803 28.749 35.262 1.00 83.95 C
ANISOU 1780 C CYS A 222 10318 9800 11780 -890 -2228 389 C
ATOM 1781 O CYS A 222 -248.412 27.677 35.347 1.00 98.98 O
ANISOU 1781 O CYS A 222 12212 11695 13702 -978 -2231 340 O
ATOM 1782 CB CYS A 222 -246.052 29.313 33.555 1.00 75.86 C
ANISOU 1782 CB CYS A 222 9626 8809 10388 -907 -2291 430 C
ATOM 1783 SG CYS A 222 -245.696 29.568 31.801 1.00 91.46 S
ANISOU 1783 SG CYS A 222 11805 10823 12122 -1021 -2470 487 S
ATOM 1784 N TYR A 223 -247.368 29.403 36.341 1.00 77.82 N
ANISOU 1784 N TYR A 223 9463 9012 11093 -770 -2073 380 N
ATOM 1785 CA TYR A 223 -247.564 28.815 37.662 1.00 85.21 C
ANISOU 1785 CA TYR A 223 10318 9933 12126 -749 -1899 313 C
ATOM 1786 C TYR A 223 -249.031 28.812 38.070 1.00 86.57 C
ANISOU 1786 C TYR A 223 10267 10097 12530 -786 -1950 319 C
ATOM 1787 O TYR A 223 -249.460 27.933 38.821 1.00 91.64 O
ANISOU 1787 O TYR A 223 10866 10730 13222 -832 -1849 264 O
ATOM 1788 CB TYR A 223 -246.721 29.548 38.699 1.00 76.82 C
ANISOU 1788 CB TYR A 223 9241 8869 11079 -632 -1729 299 C
ATOM 1789 CG TYR A 223 -245.283 29.104 38.695 1.00 84.91 C
ANISOU 1789 CG TYR A 223 10463 9894 11903 -607 -1623 268 C
ATOM 1790 CD1 TYR A 223 -244.952 27.768 38.878 1.00 91.50 C
ANISOU 1790 CD1 TYR A 223 11408 10712 12645 -661 -1546 214 C
ATOM 1791 CD2 TYR A 223 -244.257 30.014 38.512 1.00 81.44 C
ANISOU 1791 CD2 TYR A 223 10091 9464 11389 -530 -1599 296 C
ATOM 1792 CE1 TYR A 223 -243.637 27.355 38.876 1.00100.60 C
ANISOU 1792 CE1 TYR A 223 12718 11852 13652 -629 -1450 188 C
ATOM 1793 CE2 TYR A 223 -242.944 29.611 38.513 1.00 85.41 C
ANISOU 1793 CE2 TYR A 223 10750 9965 11736 -505 -1500 268 C
ATOM 1794 CZ TYR A 223 -242.637 28.282 38.693 1.00 93.86 C
ANISOU 1794 CZ TYR A 223 11914 11014 12733 -551 -1426 214 C
ATOM 1795 OH TYR A 223 -241.321 27.885 38.692 1.00105.95 O
ANISOU 1795 OH TYR A 223 13581 12531 14145 -517 -1329 189 O
ATOM 1796 N GLY A 224 -249.806 29.780 37.583 1.00 76.93 N
ANISOU 1796 N GLY A 224 8896 8871 11461 -769 -2105 392 N
ATOM 1797 CA GLY A 224 -251.236 29.766 37.845 1.00 73.13 C
ANISOU 1797 CA GLY A 224 8182 8376 11227 -807 -2168 401 C
ATOM 1798 C GLY A 224 -251.922 28.555 37.241 1.00 89.23 C
ANISOU 1798 C GLY A 224 10252 10426 13226 -950 -2281 387 C
ATOM 1799 O GLY A 224 -252.608 27.803 37.939 1.00 89.48 O
ANISOU 1799 O GLY A 224 10187 10449 13363 -1003 -2196 333 O
ATOM 1800 N GLN A 225 -251.755 28.356 35.927 1.00 78.61 N
ANISOU 1800 N GLN A 225 9050 9099 11720 -1029 -2472 432 N
ATOM 1801 CA GLN A 225 -252.339 27.196 35.266 1.00 89.46 C
ANISOU 1801 CA GLN A 225 10481 10481 13028 -1182 -2587 408 C
ATOM 1802 C GLN A 225 -251.844 25.891 35.876 1.00 94.74 C
ANISOU 1802 C GLN A 225 11283 11133 13581 -1223 -2398 302 C
ATOM 1803 O GLN A 225 -252.592 24.909 35.934 1.00109.25 O
ANISOU 1803 O GLN A 225 13083 12958 15471 -1331 -2418 263 O
ATOM 1804 CB GLN A 225 -252.019 27.248 33.774 1.00 85.28 C
ANISOU 1804 CB GLN A 225 10132 9980 12291 -1267 -2795 460 C
ATOM 1805 CG GLN A 225 -252.591 28.467 33.064 1.00 96.81 C
ANISOU 1805 CG GLN A 225 11468 11452 13865 -1250 -3027 594 C
ATOM 1806 CD GLN A 225 -254.099 28.400 32.916 1.00116.10 C
ANISOU 1806 CD GLN A 225 13675 13888 16548 -1326 -3216 647 C
ATOM 1807 OE1 GLN A 225 -254.845 28.736 33.838 1.00129.40 O
ANISOU 1807 OE1 GLN A 225 15109 15543 18514 -1255 -3143 644 O
ATOM 1808 NE2 GLN A 225 -254.555 27.957 31.751 1.00121.56 N
ANISOU 1808 NE2 GLN A 225 14446 14610 17133 -1481 -3455 691 N
ATOM 1809 N LEU A 226 -250.594 25.864 36.339 1.00 90.15 N
ANISOU 1809 N LEU A 226 10851 10544 12859 -1140 -2221 262 N
ATOM 1810 CA LEU A 226 -250.049 24.657 36.949 1.00 93.15 C
ANISOU 1810 CA LEU A 226 11354 10892 13147 -1167 -2050 179 C
ATOM 1811 C LEU A 226 -250.770 24.326 38.251 1.00100.12 C
ANISOU 1811 C LEU A 226 12071 11760 14211 -1166 -1917 154 C
ATOM 1812 O LEU A 226 -251.237 23.197 38.445 1.00106.48 O
ANISOU 1812 O LEU A 226 12888 12537 15033 -1265 -1890 112 O
ATOM 1813 CB LEU A 226 -248.547 24.831 37.179 1.00 73.81 C
ANISOU 1813 CB LEU A 226 9070 8437 10539 -1069 -1907 160 C
ATOM 1814 CG LEU A 226 -247.768 23.647 37.741 1.00 75.09 C
ANISOU 1814 CG LEU A 226 9370 8551 10608 -1079 -1743 93 C
ATOM 1815 CD1 LEU A 226 -246.408 23.568 37.069 1.00 82.17 C
ANISOU 1815 CD1 LEU A 226 10473 9436 11310 -1043 -1707 70 C
ATOM 1816 CD2 LEU A 226 -247.610 23.779 39.247 1.00 82.23 C
ANISOU 1816 CD2 LEU A 226 10184 9451 11607 -1003 -1569 94 C
ATOM 1817 N VAL A 227 -250.864 25.301 39.160 1.00 80.17 N
ANISOU 1817 N VAL A 227 9397 9247 11818 -1066 -1824 174 N
ATOM 1818 CA VAL A 227 -251.592 25.074 40.405 1.00 72.99 C
ANISOU 1818 CA VAL A 227 8329 8330 11072 -1079 -1681 144 C
ATOM 1819 C VAL A 227 -253.043 24.740 40.116 1.00 94.52 C
ANISOU 1819 C VAL A 227 10878 11054 13980 -1183 -1797 149 C
ATOM 1820 O VAL A 227 -253.657 23.925 40.814 1.00102.65 O
ANISOU 1820 O VAL A 227 11844 12071 15089 -1261 -1702 112 O
ATOM 1821 CB VAL A 227 -251.476 26.295 41.334 1.00 78.48 C
ANISOU 1821 CB VAL A 227 8899 9042 11879 -963 -1561 149 C
ATOM 1822 CG1 VAL A 227 -252.316 26.086 42.580 1.00 79.29 C
ANISOU 1822 CG1 VAL A 227 8838 9143 12146 -998 -1402 105 C
ATOM 1823 CG2 VAL A 227 -250.027 26.534 41.707 1.00 74.21 C
ANISOU 1823 CG2 VAL A 227 8531 8506 11159 -876 -1447 142 C
ATOM 1824 N PHE A 228 -253.608 25.345 39.074 1.00 96.94 N
ANISOU 1824 N PHE A 228 11103 11372 14356 -1196 -2011 205 N
ATOM 1825 CA PHE A 228 -254.976 25.022 38.691 1.00 92.40 C
ANISOU 1825 CA PHE A 228 10351 10795 13961 -1303 -2156 222 C
ATOM 1826 C PHE A 228 -255.084 23.583 38.203 1.00 92.66 C
ANISOU 1826 C PHE A 228 10526 10815 13867 -1451 -2206 181 C
ATOM 1827 O PHE A 228 -256.004 22.853 38.589 1.00 91.87 O
ANISOU 1827 O PHE A 228 10309 10700 13898 -1548 -2183 153 O
ATOM 1828 CB PHE A 228 -255.453 25.996 37.617 1.00 83.17 C
ANISOU 1828 CB PHE A 228 9083 9640 12879 -1288 -2407 313 C
ATOM 1829 CG PHE A 228 -256.812 25.683 37.085 1.00 94.06 C
ANISOU 1829 CG PHE A 228 10282 11019 14439 -1405 -2600 347 C
ATOM 1830 CD1 PHE A 228 -257.943 26.006 37.812 1.00 98.18 C
ANISOU 1830 CD1 PHE A 228 10504 11524 15275 -1392 -2555 346 C
ATOM 1831 CD2 PHE A 228 -256.962 25.061 35.856 1.00104.07 C
ANISOU 1831 CD2 PHE A 228 11673 12302 15567 -1538 -2823 373 C
ATOM 1832 CE1 PHE A 228 -259.200 25.718 37.324 1.00 90.01 C
ANISOU 1832 CE1 PHE A 228 9281 10488 14432 -1501 -2740 382 C
ATOM 1833 CE2 PHE A 228 -258.216 24.769 35.362 1.00 99.98 C
ANISOU 1833 CE2 PHE A 228 10985 11787 15216 -1658 -3021 409 C
ATOM 1834 CZ PHE A 228 -259.337 25.099 36.097 1.00 96.59 C
ANISOU 1834 CZ PHE A 228 10240 11341 15121 -1636 -2985 419 C
ATOM 1835 N THR A 229 -254.150 23.158 37.349 1.00 85.92 N
ANISOU 1835 N THR A 229 9922 9957 12765 -1476 -2264 169 N
ATOM 1836 CA THR A 229 -254.168 21.787 36.846 1.00 80.53 C
ANISOU 1836 CA THR A 229 9394 9245 11958 -1617 -2297 113 C
ATOM 1837 C THR A 229 -253.947 20.784 37.972 1.00 77.54 C
ANISOU 1837 C THR A 229 9056 8819 11585 -1630 -2076 51 C
ATOM 1838 O THR A 229 -254.649 19.772 38.071 1.00 90.75 O
ANISOU 1838 O THR A 229 10703 10460 13317 -1754 -2079 17 O
ATOM 1839 CB THR A 229 -253.107 21.626 35.757 1.00 72.38 C
ANISOU 1839 CB THR A 229 8626 8213 10662 -1630 -2364 96 C
ATOM 1840 OG1 THR A 229 -253.575 22.224 34.542 1.00 83.32 O
ANISOU 1840 OG1 THR A 229 9994 9641 12023 -1689 -2613 157 O
ATOM 1841 CG2 THR A 229 -252.779 20.160 35.517 1.00 60.48 C
ANISOU 1841 CG2 THR A 229 7313 6649 9019 -1741 -2308 7 C
ATOM 1842 N VAL A 230 -252.981 21.064 38.843 1.00 84.78 N
ANISOU 1842 N VAL A 230 10038 9731 12444 -1512 -1890 46 N
ATOM 1843 CA VAL A 230 -252.669 20.144 39.933 1.00 80.25 C
ANISOU 1843 CA VAL A 230 9522 9113 11858 -1527 -1694 10 C
ATOM 1844 C VAL A 230 -253.837 20.047 40.909 1.00 87.15 C
ANISOU 1844 C VAL A 230 10180 9994 12938 -1582 -1617 11 C
ATOM 1845 O VAL A 230 -254.190 18.954 41.369 1.00 89.00 O
ANISOU 1845 O VAL A 230 10433 10185 13197 -1683 -1545 -14 O
ATOM 1846 CB VAL A 230 -251.367 20.583 40.624 1.00 66.70 C
ANISOU 1846 CB VAL A 230 7913 7399 10033 -1393 -1541 19 C
ATOM 1847 CG1 VAL A 230 -251.227 19.935 41.978 1.00 57.77 C
ANISOU 1847 CG1 VAL A 230 6787 6238 8926 -1403 -1350 12 C
ATOM 1848 CG2 VAL A 230 -250.186 20.235 39.737 1.00 75.81 C
ANISOU 1848 CG2 VAL A 230 9295 8521 10987 -1369 -1575 -2 C
ATOM 1849 N LYS A 231 -254.461 21.185 41.238 1.00 89.09 N
ANISOU 1849 N LYS A 231 10214 10287 13348 -1520 -1621 38 N
ATOM 1850 CA LYS A 231 -255.605 21.159 42.147 1.00 82.07 C
ANISOU 1850 CA LYS A 231 9101 9406 12675 -1574 -1527 26 C
ATOM 1851 C LYS A 231 -256.822 20.518 41.499 1.00 91.85 C
ANISOU 1851 C LYS A 231 10220 10632 14046 -1715 -1676 23 C
ATOM 1852 O LYS A 231 -257.677 19.956 42.195 1.00 81.99 O
ANISOU 1852 O LYS A 231 8844 9372 12937 -1808 -1583 1 O
ATOM 1853 CB LYS A 231 -255.950 22.573 42.610 1.00 70.59 C
ANISOU 1853 CB LYS A 231 7444 7990 11388 -1465 -1484 40 C
ATOM 1854 CG LYS A 231 -255.040 23.119 43.691 1.00 79.17 C
ANISOU 1854 CG LYS A 231 8598 9091 12392 -1362 -1278 24 C
ATOM 1855 CD LYS A 231 -255.496 24.497 44.122 1.00 72.03 C
ANISOU 1855 CD LYS A 231 7481 8209 11678 -1268 -1228 19 C
ATOM 1856 CE LYS A 231 -254.602 25.055 45.214 1.00 83.54 C
ANISOU 1856 CE LYS A 231 9016 9685 13042 -1184 -1024 -8 C
ATOM 1857 NZ LYS A 231 -254.657 24.233 46.452 1.00 83.86 N
ANISOU 1857 NZ LYS A 231 9097 9732 13036 -1271 -816 -46 N
ATOM 1858 N GLU A 232 -256.924 20.607 40.177 1.00 90.81 N
ANISOU 1858 N GLU A 232 10128 10506 13869 -1747 -1909 48 N
ATOM 1859 CA GLU A 232 -258.031 19.978 39.472 1.00 77.35 C
ANISOU 1859 CA GLU A 232 8326 8792 12269 -1897 -2082 48 C
ATOM 1860 C GLU A 232 -257.887 18.463 39.491 1.00100.04 C
ANISOU 1860 C GLU A 232 11372 11611 15028 -2030 -2030 -7 C
ATOM 1861 O GLU A 232 -258.842 17.738 39.796 1.00104.41 O
ANISOU 1861 O GLU A 232 11808 12144 15721 -2154 -2015 -26 O
ATOM 1862 CB GLU A 232 -258.078 20.504 38.040 1.00 91.75 C
ANISOU 1862 CB GLU A 232 10181 10643 14036 -1909 -2356 96 C
ATOM 1863 CG GLU A 232 -259.383 20.317 37.315 1.00112.81 C
ANISOU 1863 CG GLU A 232 12672 13321 16868 -2044 -2582 125 C
ATOM 1864 CD GLU A 232 -259.307 20.837 35.895 1.00135.53 C
ANISOU 1864 CD GLU A 232 15622 16231 19643 -2068 -2865 188 C
ATOM 1865 OE1 GLU A 232 -258.212 20.759 35.297 1.00149.05 O
ANISOU 1865 OE1 GLU A 232 17598 17945 21088 -2046 -2873 172 O
ATOM 1866 OE2 GLU A 232 -260.331 21.335 35.382 1.00136.85 O
ANISOU 1866 OE2 GLU A 232 15577 16421 19997 -2114 -3078 257 O
ATOM 1867 N ALA A 233 -256.687 17.967 39.177 1.00100.89 N
ANISOU 1867 N ALA A 233 11751 11684 14898 -2003 -1992 -34 N
ATOM 1868 CA ALA A 233 -256.462 16.527 39.152 1.00 94.11 C
ANISOU 1868 CA ALA A 233 11066 10748 13943 -2117 -1940 -89 C
ATOM 1869 C ALA A 233 -256.591 15.925 40.543 1.00 86.78 C
ANISOU 1869 C ALA A 233 10094 9783 13097 -2135 -1720 -93 C
ATOM 1870 O ALA A 233 -257.169 14.843 40.708 1.00 83.96 O
ANISOU 1870 O ALA A 233 9736 9370 12794 -2273 -1699 -119 O
ATOM 1871 CB ALA A 233 -255.088 16.222 38.559 1.00 79.40 C
ANISOU 1871 CB ALA A 233 9483 8845 11838 -2065 -1926 -121 C
ATOM 1872 N ALA A 234 -256.066 16.613 41.559 1.00 76.53 N
ANISOU 1872 N ALA A 234 8764 8514 11798 -2009 -1556 -65 N
ATOM 1873 CA ALA A 234 -256.159 16.097 42.920 1.00 85.57 C
ANISOU 1873 CA ALA A 234 9885 9635 12992 -2040 -1347 -60 C
ATOM 1874 C ALA A 234 -257.606 15.997 43.380 1.00 95.74 C
ANISOU 1874 C ALA A 234 10931 10945 14502 -2154 -1323 -65 C
ATOM 1875 O ALA A 234 -257.943 15.116 44.180 1.00 99.53 O
ANISOU 1875 O ALA A 234 11413 11384 15020 -2258 -1194 -68 O
ATOM 1876 CB ALA A 234 -255.355 16.981 43.878 1.00 63.41 C
ANISOU 1876 CB ALA A 234 7090 6872 10131 -1899 -1193 -33 C
ATOM 1877 N ALA A 235 -258.474 16.880 42.879 1.00 85.96 N
ANISOU 1877 N ALA A 235 9475 9762 13424 -2141 -1448 -59 N
ATOM 1878 CA ALA A 235 -259.883 16.830 43.255 1.00 89.83 C
ANISOU 1878 CA ALA A 235 9702 10269 14162 -2245 -1429 -67 C
ATOM 1879 C ALA A 235 -260.545 15.548 42.773 1.00 93.19 C
ANISOU 1879 C ALA A 235 10152 10639 14618 -2428 -1521 -87 C
ATOM 1880 O ALA A 235 -261.490 15.066 43.404 1.00111.89 O
ANISOU 1880 O ALA A 235 12367 12998 17148 -2544 -1430 -98 O
ATOM 1881 CB ALA A 235 -260.622 18.044 42.697 1.00 80.93 C
ANISOU 1881 CB ALA A 235 8331 9196 13224 -2182 -1575 -46 C
ATOM 1882 N GLN A 236 -260.061 14.982 41.666 1.00 88.79 N
ANISOU 1882 N GLN A 236 9789 10043 13906 -2465 -1688 -100 N
ATOM 1883 CA GLN A 236 -260.585 13.723 41.156 1.00 82.45 C
ANISOU 1883 CA GLN A 236 9043 9175 13109 -2646 -1775 -133 C
ATOM 1884 C GLN A 236 -260.072 12.508 41.921 1.00 88.88 C
ANISOU 1884 C GLN A 236 10040 9898 13834 -2708 -1594 -151 C
ATOM 1885 O GLN A 236 -260.609 11.413 41.739 1.00 93.24 O
ANISOU 1885 O GLN A 236 10617 10382 14428 -2869 -1625 -179 O
ATOM 1886 CB GLN A 236 -260.231 13.565 39.677 1.00 82.78 C
ANISOU 1886 CB GLN A 236 9245 9204 13003 -2678 -2007 -157 C
ATOM 1887 CG GLN A 236 -261.049 14.430 38.737 1.00 82.67 C
ANISOU 1887 CG GLN A 236 9046 9264 13099 -2694 -2251 -124 C
ATOM 1888 CD GLN A 236 -262.406 13.827 38.416 1.00100.17 C
ANISOU 1888 CD GLN A 236 11086 11474 15501 -2883 -2385 -134 C
ATOM 1889 OE1 GLN A 236 -262.726 12.716 38.838 1.00 91.96 O
ANISOU 1889 OE1 GLN A 236 10076 10369 14494 -3012 -2293 -173 O
ATOM 1890 NE2 GLN A 236 -263.208 14.560 37.655 1.00109.52 N
ANISOU 1890 NE2 GLN A 236 12080 12720 16815 -2906 -2616 -88 N
ATOM 1891 N GLN A 237 -259.043 12.671 42.754 1.00 75.08 N
ANISOU 1891 N GLN A 237 8419 8141 11968 -2590 -1420 -128 N
ATOM 1892 CA GLN A 237 -258.449 11.587 43.539 1.00 78.66 C
ANISOU 1892 CA GLN A 237 9050 8501 12337 -2633 -1261 -118 C
ATOM 1893 C GLN A 237 -258.373 11.986 45.009 1.00 89.87 C
ANISOU 1893 C GLN A 237 10399 9963 13786 -2586 -1043 -70 C
ATOM 1894 O GLN A 237 -257.333 11.865 45.667 1.00 80.21 O
ANISOU 1894 O GLN A 237 9338 8711 12428 -2510 -927 -35 O
ATOM 1895 CB GLN A 237 -257.058 11.221 43.023 1.00 91.23 C
ANISOU 1895 CB GLN A 237 10914 10022 13726 -2547 -1283 -130 C
ATOM 1896 CG GLN A 237 -256.989 10.984 41.521 1.00108.73 C
ANISOU 1896 CG GLN A 237 13229 12211 15873 -2588 -1481 -193 C
ATOM 1897 CD GLN A 237 -255.785 10.154 41.137 1.00123.94 C
ANISOU 1897 CD GLN A 237 15427 14023 17641 -2559 -1452 -229 C
ATOM 1898 OE1 GLN A 237 -255.424 9.212 41.843 1.00125.69 O
ANISOU 1898 OE1 GLN A 237 15751 14141 17865 -2589 -1326 -212 O
ATOM 1899 NE2 GLN A 237 -255.148 10.502 40.025 1.00131.83 N
ANISOU 1899 NE2 GLN A 237 16543 15035 18510 -2502 -1562 -275 N
ATOM 1900 N GLN A 238 -259.488 12.466 45.546 1.00 91.60 N
ANISOU 1900 N GLN A 238 10371 10249 14185 -2640 -983 -72 N
ATOM 1901 CA GLN A 238 -259.513 12.830 46.957 1.00 87.05 C
ANISOU 1901 CA GLN A 238 9731 9718 13628 -2624 -756 -45 C
ATOM 1902 C GLN A 238 -259.375 11.617 47.864 1.00 92.05 C
ANISOU 1902 C GLN A 238 10500 10274 14201 -2748 -610 -7 C
ATOM 1903 O GLN A 238 -259.081 11.783 49.052 1.00102.06 O
ANISOU 1903 O GLN A 238 11797 11570 15411 -2741 -426 30 O
ATOM 1904 CB GLN A 238 -260.798 13.586 47.289 1.00 85.15 C
ANISOU 1904 CB GLN A 238 9180 9556 13618 -2663 -705 -73 C
ATOM 1905 CG GLN A 238 -260.941 14.904 46.564 1.00101.12 C
ANISOU 1905 CG GLN A 238 11050 11646 15726 -2529 -836 -91 C
ATOM 1906 CD GLN A 238 -262.008 15.774 47.182 1.00115.96 C
ANISOU 1906 CD GLN A 238 12625 13590 17846 -2532 -726 -119 C
ATOM 1907 OE1 GLN A 238 -262.146 15.826 48.401 1.00123.92 O
ANISOU 1907 OE1 GLN A 238 13593 14622 18871 -2566 -489 -132 O
ATOM 1908 NE2 GLN A 238 -262.775 16.458 46.345 1.00136.46 N
ANISOU 1908 NE2 GLN A 238 15003 16212 20634 -2503 -896 -128 N
ATOM 1909 N GLU A 239 -259.567 10.406 47.335 1.00 81.60 N
ANISOU 1909 N GLU A 239 9270 8849 12887 -2871 -692 -12 N
ATOM 1910 CA GLU A 239 -259.348 9.204 48.131 1.00 99.38 C
ANISOU 1910 CA GLU A 239 11671 11003 15086 -2984 -571 40 C
ATOM 1911 C GLU A 239 -257.871 8.973 48.434 1.00101.21 C
ANISOU 1911 C GLU A 239 12156 11174 15125 -2872 -536 96 C
ATOM 1912 O GLU A 239 -257.548 8.178 49.322 1.00113.69 O
ANISOU 1912 O GLU A 239 13860 12685 16653 -2941 -422 167 O
ATOM 1913 CB GLU A 239 -259.935 7.976 47.419 1.00 95.94 C
ANISOU 1913 CB GLU A 239 11268 10457 14728 -3144 -675 11 C
ATOM 1914 CG GLU A 239 -259.241 7.588 46.107 1.00 91.72 C
ANISOU 1914 CG GLU A 239 10904 9841 14105 -3093 -858 -36 C
ATOM 1915 CD GLU A 239 -259.729 8.385 44.903 1.00105.20 C
ANISOU 1915 CD GLU A 239 12479 11629 15863 -3057 -1048 -102 C
ATOM 1916 OE1 GLU A 239 -260.331 9.463 45.098 1.00107.54 O
ANISOU 1916 OE1 GLU A 239 12560 12044 16256 -3009 -1043 -99 O
ATOM 1917 OE2 GLU A 239 -259.513 7.928 43.758 1.00 91.90 O
ANISOU 1917 OE2 GLU A 239 10911 9883 14124 -3084 -1204 -157 O
ATOM 1918 N SER A 240 -256.974 9.651 47.722 1.00 97.15 N
ANISOU 1918 N SER A 240 11715 10683 14513 -2708 -634 73 N
ATOM 1919 CA SER A 240 -255.533 9.496 47.901 1.00100.80 C
ANISOU 1919 CA SER A 240 12395 11089 14817 -2589 -613 121 C
ATOM 1920 C SER A 240 -255.016 10.598 48.820 1.00 94.06 C
ANISOU 1920 C SER A 240 11509 10344 13887 -2475 -505 162 C
ATOM 1921 O SER A 240 -254.993 11.773 48.439 1.00101.05 O
ANISOU 1921 O SER A 240 12293 11326 14775 -2365 -549 122 O
ATOM 1922 CB SER A 240 -254.813 9.543 46.556 1.00 96.23 C
ANISOU 1922 CB SER A 240 11923 10466 14172 -2491 -768 63 C
ATOM 1923 OG SER A 240 -253.424 9.746 46.744 1.00 99.49 O
ANISOU 1923 OG SER A 240 12491 10856 14455 -2346 -738 102 O
ATOM 1924 N ALA A 241 -254.582 10.213 50.024 1.00 88.97 N
ANISOU 1924 N ALA A 241 10958 9678 13170 -2511 -372 247 N
ATOM 1925 CA ALA A 241 -254.024 11.185 50.959 1.00 94.56 C
ANISOU 1925 CA ALA A 241 11663 10486 13781 -2424 -269 284 C
ATOM 1926 C ALA A 241 -252.718 11.775 50.446 1.00105.71 C
ANISOU 1926 C ALA A 241 13182 11900 15082 -2240 -351 286 C
ATOM 1927 O ALA A 241 -252.424 12.948 50.706 1.00 97.26 O
ANISOU 1927 O ALA A 241 12054 10933 13966 -2140 -318 272 O
ATOM 1928 CB ALA A 241 -253.804 10.541 52.326 1.00 88.78 C
ANISOU 1928 CB ALA A 241 11036 9727 12970 -2527 -131 388 C
ATOM 1929 N THR A 242 -251.927 10.982 49.718 1.00100.41 N
ANISOU 1929 N THR A 242 12663 11109 14377 -2198 -446 297 N
ATOM 1930 CA THR A 242 -250.650 11.475 49.211 1.00 90.26 C
ANISOU 1930 CA THR A 242 11477 9819 12998 -2031 -510 295 C
ATOM 1931 C THR A 242 -250.851 12.480 48.085 1.00 98.47 C
ANISOU 1931 C THR A 242 12421 10936 14057 -1943 -609 204 C
ATOM 1932 O THR A 242 -250.151 13.499 48.026 1.00107.23 O
ANISOU 1932 O THR A 242 13528 12116 15099 -1812 -616 202 O
ATOM 1933 CB THR A 242 -249.785 10.313 48.729 1.00 88.64 C
ANISOU 1933 CB THR A 242 11449 9452 12777 -2015 -562 318 C
ATOM 1934 OG1 THR A 242 -250.291 9.830 47.480 1.00101.02 O
ANISOU 1934 OG1 THR A 242 13014 10959 14411 -2060 -659 224 O
ATOM 1935 CG2 THR A 242 -249.794 9.184 49.744 1.00 89.21 C
ANISOU 1935 CG2 THR A 242 11606 9424 12866 -2127 -489 421 C
ATOM 1936 N THR A 243 -251.787 12.202 47.171 1.00 88.67 N
ANISOU 1936 N THR A 243 11105 9679 12906 -2021 -697 136 N
ATOM 1937 CA THR A 243 -252.100 13.168 46.121 1.00 89.24 C
ANISOU 1937 CA THR A 243 11078 9829 13000 -1959 -812 70 C
ATOM 1938 C THR A 243 -252.486 14.514 46.719 1.00 88.55 C
ANISOU 1938 C THR A 243 10823 9870 12952 -1899 -756 76 C
ATOM 1939 O THR A 243 -252.065 15.567 46.225 1.00 86.51 O
ANISOU 1939 O THR A 243 10540 9673 12658 -1780 -813 60 O
ATOM 1940 CB THR A 243 -253.222 12.637 45.229 1.00 80.25 C
ANISOU 1940 CB THR A 243 9863 8663 11963 -2085 -922 12 C
ATOM 1941 OG1 THR A 243 -252.817 11.396 44.646 1.00 84.42 O
ANISOU 1941 OG1 THR A 243 10562 9060 12452 -2144 -964 -11 O
ATOM 1942 CG2 THR A 243 -253.531 13.620 44.114 1.00 95.03 C
ANISOU 1942 CG2 THR A 243 11643 10613 13850 -2032 -1070 -34 C
ATOM 1943 N GLN A 244 -253.269 14.498 47.797 1.00 83.68 N
ANISOU 1943 N GLN A 244 10095 9290 12410 -1986 -631 95 N
ATOM 1944 CA GLN A 244 -253.608 15.741 48.476 1.00 94.36 C
ANISOU 1944 CA GLN A 244 11294 10751 13808 -1934 -542 84 C
ATOM 1945 C GLN A 244 -252.376 16.364 49.123 1.00 98.71 C
ANISOU 1945 C GLN A 244 11958 11334 14215 -1817 -471 121 C
ATOM 1946 O GLN A 244 -252.229 17.592 49.134 1.00100.86 O
ANISOU 1946 O GLN A 244 12150 11680 14493 -1716 -463 96 O
ATOM 1947 CB GLN A 244 -254.709 15.484 49.505 1.00 87.69 C
ANISOU 1947 CB GLN A 244 10316 9932 13069 -2074 -395 82 C
ATOM 1948 CG GLN A 244 -255.924 14.780 48.923 1.00 78.84 C
ANISOU 1948 CG GLN A 244 9077 8776 12104 -2205 -464 51 C
ATOM 1949 CD GLN A 244 -256.408 15.428 47.639 1.00 89.51 C
ANISOU 1949 CD GLN A 244 10300 10152 13559 -2150 -645 3 C
ATOM 1950 OE1 GLN A 244 -256.696 16.624 47.604 1.00110.89 O
ANISOU 1950 OE1 GLN A 244 12852 12932 16350 -2066 -648 -20 O
ATOM 1951 NE2 GLN A 244 -256.494 14.642 46.574 1.00 70.60 N
ANISOU 1951 NE2 GLN A 244 7974 7690 11159 -2204 -802 -9 N
ATOM 1952 N LYS A 245 -251.474 15.536 49.657 1.00 86.97 N
ANISOU 1952 N LYS A 245 10651 9784 12609 -1830 -428 185 N
ATOM 1953 CA LYS A 245 -250.232 16.065 50.213 1.00 97.96 C
ANISOU 1953 CA LYS A 245 12151 11203 13867 -1724 -388 230 C
ATOM 1954 C LYS A 245 -249.350 16.660 49.123 1.00 97.64 C
ANISOU 1954 C LYS A 245 12159 11158 13782 -1576 -508 204 C
ATOM 1955 O LYS A 245 -248.787 17.748 49.297 1.00 80.81 O
ANISOU 1955 O LYS A 245 10009 9094 11600 -1473 -491 200 O
ATOM 1956 CB LYS A 245 -249.478 14.975 50.974 1.00102.92 C
ANISOU 1956 CB LYS A 245 12951 11751 14403 -1775 -344 323 C
ATOM 1957 CG LYS A 245 -249.925 14.797 52.416 1.00130.94 C
ANISOU 1957 CG LYS A 245 16490 15341 17920 -1901 -197 375 C
ATOM 1958 CD LYS A 245 -248.997 13.852 53.169 1.00148.16 C
ANISOU 1958 CD LYS A 245 18854 17445 19996 -1936 -184 496 C
ATOM 1959 CE LYS A 245 -249.424 13.692 54.621 1.00156.10 C
ANISOU 1959 CE LYS A 245 19873 18502 20936 -2084 -41 559 C
ATOM 1960 NZ LYS A 245 -248.498 12.799 55.371 1.00156.21 N
ANISOU 1960 NZ LYS A 245 20068 18438 20846 -2123 -57 703 N
ATOM 1961 N ALA A 246 -249.219 15.963 47.993 1.00 83.88 N
ANISOU 1961 N ALA A 246 10484 9335 12049 -1575 -620 181 N
ATOM 1962 CA ALA A 246 -248.444 16.504 46.882 1.00 71.63 C
ANISOU 1962 CA ALA A 246 8986 7785 10445 -1456 -723 149 C
ATOM 1963 C ALA A 246 -249.046 17.807 46.370 1.00 96.24 C
ANISOU 1963 C ALA A 246 11952 10998 13618 -1407 -779 106 C
ATOM 1964 O ALA A 246 -248.322 18.772 46.103 1.00104.43 O
ANISOU 1964 O ALA A 246 13002 12077 14598 -1292 -802 106 O
ATOM 1965 CB ALA A 246 -248.356 15.478 45.756 1.00 61.01 C
ANISOU 1965 CB ALA A 246 7744 6340 9099 -1496 -817 112 C
ATOM 1966 N GLU A 247 -250.372 17.854 46.224 1.00101.26 N
ANISOU 1966 N GLU A 247 12435 11658 14380 -1493 -806 76 N
ATOM 1967 CA GLU A 247 -251.019 19.082 45.775 1.00 92.20 C
ANISOU 1967 CA GLU A 247 11121 10586 13325 -1445 -870 49 C
ATOM 1968 C GLU A 247 -250.758 20.229 46.744 1.00 82.85 C
ANISOU 1968 C GLU A 247 9865 9470 12144 -1363 -753 57 C
ATOM 1969 O GLU A 247 -250.563 21.375 46.322 1.00 83.21 O
ANISOU 1969 O GLU A 247 9854 9557 12206 -1264 -805 48 O
ATOM 1970 CB GLU A 247 -252.522 18.850 45.601 1.00 83.49 C
ANISOU 1970 CB GLU A 247 9841 9489 12392 -1559 -911 24 C
ATOM 1971 CG GLU A 247 -253.331 20.108 45.333 1.00 98.60 C
ANISOU 1971 CG GLU A 247 11541 11467 14455 -1512 -966 8 C
ATOM 1972 CD GLU A 247 -253.829 20.765 46.607 1.00117.84 C
ANISOU 1972 CD GLU A 247 13826 13951 16998 -1508 -789 -8 C
ATOM 1973 OE1 GLU A 247 -254.188 20.031 47.555 1.00120.25 O
ANISOU 1973 OE1 GLU A 247 14129 14246 17314 -1609 -650 -11 O
ATOM 1974 OE2 GLU A 247 -253.848 22.014 46.663 1.00115.96 O
ANISOU 1974 OE2 GLU A 247 13479 13754 16828 -1411 -780 -19 O
ATOM 1975 N LYS A 248 -250.759 19.942 48.048 1.00 72.77 N
ANISOU 1975 N LYS A 248 8598 8203 10846 -1415 -595 72 N
ATOM 1976 CA LYS A 248 -250.530 20.992 49.035 1.00 76.09 C
ANISOU 1976 CA LYS A 248 8967 8690 11254 -1361 -470 64 C
ATOM 1977 C LYS A 248 -249.111 21.536 48.931 1.00 83.07 C
ANISOU 1977 C LYS A 248 9985 9582 11996 -1239 -496 91 C
ATOM 1978 O LYS A 248 -248.898 22.754 48.934 1.00102.07 O
ANISOU 1978 O LYS A 248 12330 12034 14418 -1149 -489 68 O
ATOM 1979 CB LYS A 248 -250.802 20.465 50.446 1.00 84.43 C
ANISOU 1979 CB LYS A 248 10037 9761 12281 -1473 -297 77 C
ATOM 1980 CG LYS A 248 -252.280 20.384 50.824 1.00103.75 C
ANISOU 1980 CG LYS A 248 12297 12228 14894 -1587 -212 31 C
ATOM 1981 CD LYS A 248 -252.461 19.866 52.248 1.00123.21 C
ANISOU 1981 CD LYS A 248 14803 14713 17296 -1714 -24 48 C
ATOM 1982 CE LYS A 248 -253.929 19.796 52.648 1.00131.43 C
ANISOU 1982 CE LYS A 248 15649 15776 18512 -1835 88 -8 C
ATOM 1983 NZ LYS A 248 -254.089 19.240 54.023 1.00138.57 N
ANISOU 1983 NZ LYS A 248 16616 16704 19329 -1982 281 12 N
ATOM 1984 N GLU A 249 -248.126 20.646 48.824 1.00 86.73 N
ANISOU 1984 N GLU A 249 10625 9991 12338 -1233 -526 138 N
ATOM 1985 CA GLU A 249 -246.744 21.106 48.795 1.00101.01 C
ANISOU 1985 CA GLU A 249 12547 11803 14028 -1123 -542 167 C
ATOM 1986 C GLU A 249 -246.395 21.760 47.462 1.00 98.65 C
ANISOU 1986 C GLU A 249 12246 11504 13732 -1024 -666 142 C
ATOM 1987 O GLU A 249 -245.574 22.683 47.428 1.00 96.44 O
ANISOU 1987 O GLU A 249 11987 11256 13399 -927 -668 147 O
ATOM 1988 CB GLU A 249 -245.797 19.947 49.118 1.00 95.82 C
ANISOU 1988 CB GLU A 249 12056 11075 13274 -1142 -533 231 C
ATOM 1989 CG GLU A 249 -245.845 18.783 48.150 1.00121.32 C
ANISOU 1989 CG GLU A 249 15359 14210 16528 -1174 -617 226 C
ATOM 1990 CD GLU A 249 -245.119 17.556 48.681 1.00139.68 C
ANISOU 1990 CD GLU A 249 17822 16442 18806 -1208 -588 294 C
ATOM 1991 OE1 GLU A 249 -245.033 17.401 49.919 1.00135.18 O
ANISOU 1991 OE1 GLU A 249 17271 15891 18200 -1258 -506 357 O
ATOM 1992 OE2 GLU A 249 -244.633 16.747 47.861 1.00143.16 O
ANISOU 1992 OE2 GLU A 249 18355 16788 19250 -1189 -646 285 O
ATOM 1993 N VAL A 250 -247.010 21.319 46.363 1.00 83.04 N
ANISOU 1993 N VAL A 250 10250 9494 11809 -1060 -773 117 N
ATOM 1994 CA VAL A 250 -246.801 21.994 45.083 1.00 75.75 C
ANISOU 1994 CA VAL A 250 9329 8581 10874 -992 -898 100 C
ATOM 1995 C VAL A 250 -247.363 23.408 45.135 1.00 85.49 C
ANISOU 1995 C VAL A 250 10404 9879 12201 -940 -910 90 C
ATOM 1996 O VAL A 250 -246.715 24.370 44.704 1.00 82.53 O
ANISOU 1996 O VAL A 250 10046 9526 11786 -847 -950 99 O
ATOM 1997 CB VAL A 250 -247.429 21.186 43.934 1.00 85.52 C
ANISOU 1997 CB VAL A 250 10587 9774 12133 -1071 -1018 75 C
ATOM 1998 CG1 VAL A 250 -247.561 22.050 42.689 1.00 86.93 C
ANISOU 1998 CG1 VAL A 250 10735 9984 12310 -1032 -1160 67 C
ATOM 1999 CG2 VAL A 250 -246.595 19.955 43.638 1.00 75.88 C
ANISOU 1999 CG2 VAL A 250 9545 8471 10816 -1093 -1008 69 C
ATOM 2000 N THR A 251 -248.580 23.555 45.660 1.00 92.71 N
ANISOU 2000 N THR A 251 11156 10814 13257 -1000 -870 70 N
ATOM 2001 CA THR A 251 -249.160 24.884 45.806 1.00 87.37 C
ANISOU 2001 CA THR A 251 10309 10178 12711 -945 -862 54 C
ATOM 2002 C THR A 251 -248.303 25.754 46.712 1.00 89.24 C
ANISOU 2002 C THR A 251 10577 10446 12885 -866 -742 49 C
ATOM 2003 O THR A 251 -248.074 26.934 46.420 1.00 84.66 O
ANISOU 2003 O THR A 251 9948 9880 12341 -777 -775 48 O
ATOM 2004 CB THR A 251 -250.581 24.780 46.354 1.00 79.46 C
ANISOU 2004 CB THR A 251 9116 9184 11890 -1029 -803 22 C
ATOM 2005 OG1 THR A 251 -251.371 23.992 45.459 1.00 93.22 O
ANISOU 2005 OG1 THR A 251 10825 10899 13695 -1110 -935 29 O
ATOM 2006 CG2 THR A 251 -251.203 26.162 46.487 1.00 77.36 C
ANISOU 2006 CG2 THR A 251 8654 8939 11799 -963 -786 -3 C
ATOM 2007 N ARG A 252 -247.807 25.181 47.810 1.00 82.14 N
ANISOU 2007 N ARG A 252 9768 9553 11888 -907 -612 53 N
ATOM 2008 CA ARG A 252 -246.991 25.953 48.739 1.00 90.81 C
ANISOU 2008 CA ARG A 252 10906 10687 12910 -855 -505 49 C
ATOM 2009 C ARG A 252 -245.685 26.397 48.091 1.00 90.64 C
ANISOU 2009 C ARG A 252 11001 10659 12778 -752 -585 81 C
ATOM 2010 O ARG A 252 -245.228 27.525 48.311 1.00 96.01 O
ANISOU 2010 O ARG A 252 11659 11366 13456 -681 -557 67 O
ATOM 2011 CB ARG A 252 -246.726 25.135 50.002 1.00 81.34 C
ANISOU 2011 CB ARG A 252 9797 9499 11611 -942 -378 67 C
ATOM 2012 CG ARG A 252 -246.026 25.908 51.102 1.00113.80 C
ANISOU 2012 CG ARG A 252 13947 13658 15634 -923 -266 57 C
ATOM 2013 CD ARG A 252 -246.369 25.355 52.478 1.00140.94 C
ANISOU 2013 CD ARG A 252 17410 17126 19016 -1050 -118 56 C
ATOM 2014 NE ARG A 252 -245.680 26.082 53.541 1.00157.79 N
ANISOU 2014 NE ARG A 252 19600 19313 21040 -1054 -19 44 N
ATOM 2015 CZ ARG A 252 -246.108 27.227 54.065 1.00168.48 C
ANISOU 2015 CZ ARG A 252 20854 20708 22453 -1050 92 -43 C
ATOM 2016 NH1 ARG A 252 -245.413 27.817 55.028 1.00169.65 N
ANISOU 2016 NH1 ARG A 252 21077 20904 22478 -1070 176 -59 N
ATOM 2017 NH2 ARG A 252 -247.229 27.784 53.627 1.00174.18 N
ANISOU 2017 NH2 ARG A 252 21396 21415 23368 -1029 114 -116 N
ATOM 2018 N MET A 253 -245.078 25.531 47.278 1.00 80.08 N
ANISOU 2018 N MET A 253 9786 9282 11359 -747 -674 115 N
ATOM 2019 CA MET A 253 -243.824 25.888 46.623 1.00 74.19 C
ANISOU 2019 CA MET A 253 9146 8528 10515 -657 -732 139 C
ATOM 2020 C MET A 253 -244.035 26.967 45.572 1.00 82.27 C
ANISOU 2020 C MET A 253 10104 9563 11593 -595 -831 130 C
ATOM 2021 O MET A 253 -243.236 27.905 45.471 1.00 91.59 O
ANISOU 2021 O MET A 253 11306 10759 12734 -516 -832 140 O
ATOM 2022 CB MET A 253 -243.185 24.653 45.996 1.00 71.81 C
ANISOU 2022 CB MET A 253 8983 8168 10133 -674 -779 160 C
ATOM 2023 CG MET A 253 -242.152 24.004 46.882 1.00 95.28 C
ANISOU 2023 CG MET A 253 12061 11119 13022 -671 -706 201 C
ATOM 2024 SD MET A 253 -240.771 25.113 47.225 1.00107.96 S
ANISOU 2024 SD MET A 253 13702 12765 14553 -567 -680 223 S
ATOM 2025 CE MET A 253 -240.030 24.269 48.616 1.00111.34 C
ANISOU 2025 CE MET A 253 14211 13178 14914 -607 -606 288 C
ATOM 2026 N VAL A 254 -245.095 26.846 44.772 1.00 77.78 N
ANISOU 2026 N VAL A 254 9454 8983 11115 -636 -926 122 N
ATOM 2027 CA VAL A 254 -245.374 27.863 43.763 1.00 77.60 C
ANISOU 2027 CA VAL A 254 9366 8967 11150 -588 -1046 136 C
ATOM 2028 C VAL A 254 -245.557 29.220 44.426 1.00 83.57 C
ANISOU 2028 C VAL A 254 9997 9744 12012 -524 -985 125 C
ATOM 2029 O VAL A 254 -245.090 30.248 43.921 1.00 83.57 O
ANISOU 2029 O VAL A 254 9999 9743 12009 -451 -1039 148 O
ATOM 2030 CB VAL A 254 -246.604 27.465 42.927 1.00 62.26 C
ANISOU 2030 CB VAL A 254 7340 7012 9304 -661 -1173 138 C
ATOM 2031 CG1 VAL A 254 -247.109 28.655 42.133 1.00 78.22 C
ANISOU 2031 CG1 VAL A 254 9252 9040 11429 -617 -1302 172 C
ATOM 2032 CG2 VAL A 254 -246.254 26.331 41.990 1.00 69.47 C
ANISOU 2032 CG2 VAL A 254 8406 7900 10091 -721 -1250 138 C
ATOM 2033 N ILE A 255 -246.217 29.237 45.583 1.00 72.04 N
ANISOU 2033 N ILE A 255 8434 8295 10644 -557 -861 85 N
ATOM 2034 CA ILE A 255 -246.408 30.481 46.317 1.00 68.94 C
ANISOU 2034 CA ILE A 255 7924 7911 10357 -506 -771 50 C
ATOM 2035 C ILE A 255 -245.063 31.055 46.739 1.00 80.92 C
ANISOU 2035 C ILE A 255 9559 9445 11743 -445 -711 54 C
ATOM 2036 O ILE A 255 -244.774 32.235 46.511 1.00 85.42 O
ANISOU 2036 O ILE A 255 10092 10004 12358 -370 -733 55 O
ATOM 2037 CB ILE A 255 -247.337 30.245 47.521 1.00 74.03 C
ANISOU 2037 CB ILE A 255 8457 8570 11102 -578 -618 -11 C
ATOM 2038 CG1 ILE A 255 -248.779 30.059 47.040 1.00 75.62 C
ANISOU 2038 CG1 ILE A 255 8483 8749 11500 -621 -684 -19 C
ATOM 2039 CG2 ILE A 255 -247.233 31.388 48.513 1.00 68.22 C
ANISOU 2039 CG2 ILE A 255 7656 7845 10421 -540 -475 -71 C
ATOM 2040 CD1 ILE A 255 -249.736 29.667 48.133 1.00 78.27 C
ANISOU 2040 CD1 ILE A 255 8706 9097 11935 -709 -524 -81 C
ATOM 2041 N ILE A 256 -244.211 30.217 47.339 1.00 76.79 N
ANISOU 2041 N ILE A 256 9173 8939 11063 -477 -647 64 N
ATOM 2042 CA ILE A 256 -242.875 30.650 47.755 1.00 72.00 C
ANISOU 2042 CA ILE A 256 8674 8351 10333 -429 -606 77 C
ATOM 2043 C ILE A 256 -242.117 31.247 46.576 1.00 79.58 C
ANISOU 2043 C ILE A 256 9683 9294 11260 -349 -718 114 C
ATOM 2044 O ILE A 256 -241.535 32.334 46.671 1.00 78.67 O
ANISOU 2044 O ILE A 256 9562 9183 11145 -289 -703 111 O
ATOM 2045 CB ILE A 256 -242.102 29.473 48.379 1.00 73.33 C
ANISOU 2045 CB ILE A 256 8975 8526 10359 -478 -562 108 C
ATOM 2046 CG1 ILE A 256 -242.701 29.099 49.733 1.00 63.02 C
ANISOU 2046 CG1 ILE A 256 7640 7249 9057 -569 -435 80 C
ATOM 2047 CG2 ILE A 256 -240.617 29.805 48.515 1.00 72.05 C
ANISOU 2047 CG2 ILE A 256 8919 8375 10082 -421 -563 140 C
ATOM 2048 CD1 ILE A 256 -241.940 28.017 50.463 1.00 83.59 C
ANISOU 2048 CD1 ILE A 256 10376 9856 11528 -624 -404 133 C
ATOM 2049 N MET A 257 -242.120 30.541 45.443 1.00 73.14 N
ANISOU 2049 N MET A 257 8925 8457 10408 -358 -825 146 N
ATOM 2050 CA MET A 257 -241.394 31.015 44.270 1.00 72.05 C
ANISOU 2050 CA MET A 257 8854 8309 10213 -304 -921 181 C
ATOM 2051 C MET A 257 -241.951 32.340 43.782 1.00 80.11 C
ANISOU 2051 C MET A 257 9768 9322 11349 -261 -988 193 C
ATOM 2052 O MET A 257 -241.198 33.284 43.512 1.00 77.75 O
ANISOU 2052 O MET A 257 9497 9020 11023 -202 -1001 214 O
ATOM 2053 CB MET A 257 -241.450 29.967 43.162 1.00 64.25 C
ANISOU 2053 CB MET A 257 7953 7301 9159 -348 -1011 195 C
ATOM 2054 CG MET A 257 -240.637 28.731 43.479 1.00 78.34 C
ANISOU 2054 CG MET A 257 9857 9068 10842 -370 -949 189 C
ATOM 2055 SD MET A 257 -240.916 27.393 42.313 1.00 95.05 S
ANISOU 2055 SD MET A 257 12066 11142 12907 -440 -1027 175 S
ATOM 2056 CE MET A 257 -239.919 26.104 43.076 1.00106.28 C
ANISOU 2056 CE MET A 257 13594 12520 14267 -443 -924 174 C
ATOM 2057 N VAL A 258 -243.277 32.432 43.677 1.00 84.10 N
ANISOU 2057 N VAL A 258 10140 9815 12001 -289 -1034 185 N
ATOM 2058 CA VAL A 258 -243.898 33.648 43.170 1.00 69.67 C
ANISOU 2058 CA VAL A 258 8190 7961 10321 -244 -1118 211 C
ATOM 2059 C VAL A 258 -243.724 34.793 44.162 1.00 83.95 C
ANISOU 2059 C VAL A 258 9921 9758 12219 -187 -1001 171 C
ATOM 2060 O VAL A 258 -243.490 35.942 43.768 1.00 84.12 O
ANISOU 2060 O VAL A 258 9914 9749 12299 -125 -1049 200 O
ATOM 2061 CB VAL A 258 -245.378 33.384 42.842 1.00 74.10 C
ANISOU 2061 CB VAL A 258 8606 8505 11045 -291 -1203 216 C
ATOM 2062 CG1 VAL A 258 -246.100 34.685 42.554 1.00 76.20 C
ANISOU 2062 CG1 VAL A 258 8708 8728 11517 -235 -1278 246 C
ATOM 2063 CG2 VAL A 258 -245.484 32.444 41.649 1.00 65.78 C
ANISOU 2063 CG2 VAL A 258 7646 7459 9888 -356 -1349 259 C
ATOM 2064 N ILE A 259 -243.814 34.500 45.463 1.00 78.64 N
ANISOU 2064 N ILE A 259 9226 9106 11549 -216 -845 103 N
ATOM 2065 CA ILE A 259 -243.547 35.528 46.468 1.00 83.42 C
ANISOU 2065 CA ILE A 259 9786 9706 12205 -182 -717 46 C
ATOM 2066 C ILE A 259 -242.102 35.998 46.368 1.00 93.77 C
ANISOU 2066 C ILE A 259 11229 11028 13372 -138 -720 72 C
ATOM 2067 O ILE A 259 -241.815 37.200 46.399 1.00 77.80 O
ANISOU 2067 O ILE A 259 9173 8975 11414 -84 -709 63 O
ATOM 2068 CB ILE A 259 -243.861 35.009 47.882 1.00 88.94 C
ANISOU 2068 CB ILE A 259 10467 10438 12886 -252 -547 -31 C
ATOM 2069 CG1 ILE A 259 -245.365 34.799 48.067 1.00 89.82 C
ANISOU 2069 CG1 ILE A 259 10411 10532 13184 -293 -515 -73 C
ATOM 2070 CG2 ILE A 259 -243.303 35.972 48.928 1.00 79.20 C
ANISOU 2070 CG2 ILE A 259 9243 9212 11638 -237 -413 -97 C
ATOM 2071 CD1 ILE A 259 -246.192 36.017 47.761 1.00 97.88 C
ANISOU 2071 CD1 ILE A 259 11250 11490 14449 -229 -538 -94 C
ATOM 2072 N ALA A 260 -241.169 35.050 46.252 1.00 91.86 N
ANISOU 2072 N ALA A 260 11132 10821 12951 -161 -732 104 N
ATOM 2073 CA ALA A 260 -239.763 35.411 46.122 1.00 70.58 C
ANISOU 2073 CA ALA A 260 8547 8136 10133 -122 -734 132 C
ATOM 2074 C ALA A 260 -239.530 36.283 44.897 1.00 82.50 C
ANISOU 2074 C ALA A 260 10060 9614 11674 -67 -845 184 C
ATOM 2075 O ALA A 260 -238.801 37.279 44.967 1.00 85.24 O
ANISOU 2075 O ALA A 260 10421 9949 12018 -26 -827 188 O
ATOM 2076 CB ALA A 260 -238.898 34.154 46.051 1.00 58.84 C
ANISOU 2076 CB ALA A 260 7191 6674 8491 -150 -737 161 C
ATOM 2077 N PHE A 261 -240.141 35.927 43.766 1.00 64.20 N
ANISOU 2077 N PHE A 261 7735 7280 9377 -79 -965 228 N
ATOM 2078 CA PHE A 261 -239.957 36.731 42.563 1.00 68.03 C
ANISOU 2078 CA PHE A 261 8239 7740 9871 -47 -1083 294 C
ATOM 2079 C PHE A 261 -240.466 38.148 42.774 1.00 81.58 C
ANISOU 2079 C PHE A 261 9829 9406 11764 3 -1090 296 C
ATOM 2080 O PHE A 261 -239.847 39.113 42.313 1.00 76.25 O
ANISOU 2080 O PHE A 261 9183 8704 11085 42 -1127 339 O
ATOM 2081 CB PHE A 261 -240.662 36.079 41.378 1.00 68.72 C
ANISOU 2081 CB PHE A 261 8342 7826 9943 -92 -1222 341 C
ATOM 2082 CG PHE A 261 -240.506 36.834 40.090 1.00 73.11 C
ANISOU 2082 CG PHE A 261 8938 8363 10478 -84 -1360 423 C
ATOM 2083 CD1 PHE A 261 -239.392 36.640 39.289 1.00 74.01 C
ANISOU 2083 CD1 PHE A 261 9208 8499 10413 -98 -1372 450 C
ATOM 2084 CD2 PHE A 261 -241.479 37.725 39.671 1.00 77.57 C
ANISOU 2084 CD2 PHE A 261 9382 8884 11208 -67 -1475 478 C
ATOM 2085 CE1 PHE A 261 -239.249 37.324 38.097 1.00 74.90 C
ANISOU 2085 CE1 PHE A 261 9375 8601 10482 -111 -1492 531 C
ATOM 2086 CE2 PHE A 261 -241.340 38.413 38.480 1.00 88.32 C
ANISOU 2086 CE2 PHE A 261 10792 10227 12539 -73 -1619 574 C
ATOM 2087 CZ PHE A 261 -240.222 38.210 37.692 1.00 80.06 C
ANISOU 2087 CZ PHE A 261 9922 9213 11283 -102 -1625 601 C
ATOM 2088 N LEU A 262 -241.591 38.291 43.477 1.00 78.52 N
ANISOU 2088 N LEU A 262 9295 8995 11546 2 -1045 247 N
ATOM 2089 CA LEU A 262 -242.142 39.618 43.724 1.00 93.75 C
ANISOU 2089 CA LEU A 262 11085 10855 13682 56 -1034 234 C
ATOM 2090 C LEU A 262 -241.246 40.438 44.644 1.00100.64 C
ANISOU 2090 C LEU A 262 11991 11720 14530 85 -901 174 C
ATOM 2091 O LEU A 262 -241.182 41.666 44.509 1.00 98.67 O
ANISOU 2091 O LEU A 262 11688 11403 14399 136 -916 186 O
ATOM 2092 CB LEU A 262 -243.547 39.504 44.316 1.00 78.03 C
ANISOU 2092 CB LEU A 262 8917 8838 11893 43 -987 176 C
ATOM 2093 CG LEU A 262 -244.672 39.033 43.397 1.00 83.41 C
ANISOU 2093 CG LEU A 262 9509 9505 12679 19 -1142 240 C
ATOM 2094 CD1 LEU A 262 -245.949 38.841 44.201 1.00 79.31 C
ANISOU 2094 CD1 LEU A 262 8806 8967 12362 0 -1053 164 C
ATOM 2095 CD2 LEU A 262 -244.885 40.026 42.264 1.00 74.81 C
ANISOU 2095 CD2 LEU A 262 8370 8349 11705 68 -1321 346 C
ATOM 2096 N ILE A 263 -240.545 39.784 45.575 1.00 90.71 N
ANISOU 2096 N ILE A 263 10820 10524 13121 45 -782 117 N
ATOM 2097 CA ILE A 263 -239.684 40.512 46.504 1.00 83.92 C
ANISOU 2097 CA ILE A 263 9999 9667 12222 53 -668 59 C
ATOM 2098 C ILE A 263 -238.516 41.167 45.770 1.00 78.07 C
ANISOU 2098 C ILE A 263 9349 8913 11403 90 -736 124 C
ATOM 2099 O ILE A 263 -238.021 42.219 46.184 1.00 83.03 O
ANISOU 2099 O ILE A 263 9969 9506 12071 112 -684 93 O
ATOM 2100 CB ILE A 263 -239.207 39.571 47.627 1.00 80.42 C
ANISOU 2100 CB ILE A 263 9635 9299 11624 -13 -557 6 C
ATOM 2101 CG1 ILE A 263 -240.389 39.136 48.490 1.00 93.67 C
ANISOU 2101 CG1 ILE A 263 11218 10985 13387 -63 -459 -69 C
ATOM 2102 CG2 ILE A 263 -238.173 40.240 48.506 1.00 75.97 C
ANISOU 2102 CG2 ILE A 263 9132 8751 10983 -23 -469 -39 C
ATOM 2103 CD1 ILE A 263 -239.994 38.264 49.663 1.00 96.04 C
ANISOU 2103 CD1 ILE A 263 11603 11356 13530 -145 -352 -108 C
ATOM 2104 N CYS A 264 -238.064 40.574 44.671 1.00 75.89 N
ANISOU 2104 N CYS A 264 9160 8660 11016 88 -843 208 N
ATOM 2105 CA CYS A 264 -237.042 41.187 43.835 1.00 77.48 C
ANISOU 2105 CA CYS A 264 9443 8848 11147 113 -903 275 C
ATOM 2106 C CYS A 264 -237.634 42.113 42.780 1.00 98.00 C
ANISOU 2106 C CYS A 264 11988 11377 13870 145 -1026 350 C
ATOM 2107 O CYS A 264 -236.914 42.960 42.234 1.00115.38 O
ANISOU 2107 O CYS A 264 14235 13548 16054 164 -1062 403 O
ATOM 2108 CB CYS A 264 -236.206 40.090 43.164 1.00 75.41 C
ANISOU 2108 CB CYS A 264 9310 8643 10700 85 -935 316 C
ATOM 2109 SG CYS A 264 -235.063 40.657 41.899 1.00117.00 S
ANISOU 2109 SG CYS A 264 14683 13903 15871 96 -1001 399 S
ATOM 2110 N TRP A 265 -238.931 41.985 42.500 1.00 92.56 N
ANISOU 2110 N TRP A 265 11195 10658 13315 146 -1097 365 N
ATOM 2111 CA TRP A 265 -239.584 42.682 41.398 1.00 93.31 C
ANISOU 2111 CA TRP A 265 11237 10689 13528 166 -1254 464 C
ATOM 2112 C TRP A 265 -240.273 43.961 41.862 1.00103.58 C
ANISOU 2112 C TRP A 265 12382 11886 15087 225 -1236 445 C
ATOM 2113 O TRP A 265 -240.133 45.011 41.226 1.00108.77 O
ANISOU 2113 O TRP A 265 13032 12471 15826 257 -1322 526 O
ATOM 2114 CB TRP A 265 -240.590 41.740 40.727 1.00 94.17 C
ANISOU 2114 CB TRP A 265 11316 10823 13642 125 -1369 502 C
ATOM 2115 CG TRP A 265 -241.238 42.279 39.478 1.00100.18 C
ANISOU 2115 CG TRP A 265 12042 11534 14487 123 -1568 627 C
ATOM 2116 CD1 TRP A 265 -240.807 42.116 38.191 1.00102.51 C
ANISOU 2116 CD1 TRP A 265 12472 11857 14620 74 -1702 728 C
ATOM 2117 CD2 TRP A 265 -242.445 43.049 39.400 1.00101.71 C
ANISOU 2117 CD2 TRP A 265 12054 11639 14950 162 -1661 669 C
ATOM 2118 NE1 TRP A 265 -241.666 42.744 37.320 1.00100.70 N
ANISOU 2118 NE1 TRP A 265 12169 11569 14522 72 -1891 844 N
ATOM 2119 CE2 TRP A 265 -242.680 43.324 38.037 1.00 96.74 C
ANISOU 2119 CE2 TRP A 265 11463 10991 14304 133 -1877 815 C
ATOM 2120 CE3 TRP A 265 -243.347 43.537 40.351 1.00 99.51 C
ANISOU 2120 CE3 TRP A 265 11581 11293 14933 215 -1578 596 C
ATOM 2121 CZ2 TRP A 265 -243.780 44.065 37.602 1.00 86.84 C
ANISOU 2121 CZ2 TRP A 265 10048 9646 13299 163 -2036 908 C
ATOM 2122 CZ3 TRP A 265 -244.438 44.271 39.917 1.00 98.40 C
ANISOU 2122 CZ3 TRP A 265 11270 11055 15061 253 -1713 671 C
ATOM 2123 CH2 TRP A 265 -244.644 44.528 38.555 1.00 88.58 C
ANISOU 2123 CH2 TRP A 265 10059 9790 13808 231 -1951 835 C
ATOM 2124 N LEU A 266 -241.003 43.887 42.974 1.00 99.05 N
ANISOU 2124 N LEU A 266 11688 11299 14647 234 -1115 337 N
ATOM 2125 CA LEU A 266 -241.766 45.040 43.447 1.00 95.12 C
ANISOU 2125 CA LEU A 266 11025 10690 14427 291 -1073 296 C
ATOM 2126 C LEU A 266 -240.921 46.264 43.796 1.00120.41 C
ANISOU 2126 C LEU A 266 14259 13828 17662 327 -1003 270 C
ATOM 2127 O LEU A 266 -241.386 47.385 43.524 1.00120.29 O
ANISOU 2127 O LEU A 266 14138 13691 17876 383 -1053 305 O
ATOM 2128 CB LEU A 266 -242.620 44.624 44.650 1.00 86.55 C
ANISOU 2128 CB LEU A 266 9822 9616 13448 274 -916 161 C
ATOM 2129 CG LEU A 266 -243.900 43.844 44.346 1.00 93.70 C
ANISOU 2129 CG LEU A 266 10607 10530 14464 256 -987 181 C
ATOM 2130 CD1 LEU A 266 -244.631 43.492 45.631 1.00 86.19 C
ANISOU 2130 CD1 LEU A 266 9550 9593 13606 227 -796 37 C
ATOM 2131 CD2 LEU A 266 -244.800 44.645 43.424 1.00 85.48 C
ANISOU 2131 CD2 LEU A 266 9416 9381 13681 313 -1155 283 C
ATOM 2132 N PRO A 267 -239.731 46.149 44.412 1.00115.22 N
ANISOU 2132 N PRO A 267 13731 13234 16813 295 -895 213 N
ATOM 2133 CA PRO A 267 -238.950 47.366 44.686 1.00 98.40 C
ANISOU 2133 CA PRO A 267 11626 11035 14725 320 -841 191 C
ATOM 2134 C PRO A 267 -238.704 48.225 43.456 1.00108.85 C
ANISOU 2134 C PRO A 267 12970 12280 16107 355 -996 332 C
ATOM 2135 O PRO A 267 -238.855 49.452 43.524 1.00121.14 O
ANISOU 2135 O PRO A 267 14454 13713 17860 400 -990 331 O
ATOM 2136 CB PRO A 267 -237.648 46.805 45.268 1.00106.41 C
ANISOU 2136 CB PRO A 267 12789 12158 15485 265 -754 146 C
ATOM 2137 CG PRO A 267 -238.061 45.556 45.924 1.00108.62 C
ANISOU 2137 CG PRO A 267 13070 12528 15674 221 -689 84 C
ATOM 2138 CD PRO A 267 -239.107 44.968 45.037 1.00113.42 C
ANISOU 2138 CD PRO A 267 13612 13129 16355 235 -809 158 C
ATOM 2139 N TYR A 268 -238.342 47.616 42.326 1.00 96.70 N
ANISOU 2139 N TYR A 268 11535 10803 14403 327 -1130 453 N
ATOM 2140 CA TYR A 268 -238.170 48.395 41.106 1.00 94.29 C
ANISOU 2140 CA TYR A 268 11264 10432 14131 340 -1284 600 C
ATOM 2141 C TYR A 268 -239.481 49.038 40.661 1.00 94.89 C
ANISOU 2141 C TYR A 268 11184 10389 14482 388 -1409 672 C
ATOM 2142 O TYR A 268 -239.473 50.115 40.057 1.00104.01 O
ANISOU 2142 O TYR A 268 12319 11435 15764 417 -1506 774 O
ATOM 2143 CB TYR A 268 -237.603 47.511 39.998 1.00 87.62 C
ANISOU 2143 CB TYR A 268 10569 9686 13036 281 -1385 697 C
ATOM 2144 CG TYR A 268 -236.139 47.141 40.138 1.00 95.55 C
ANISOU 2144 CG TYR A 268 11720 10775 13808 243 -1288 664 C
ATOM 2145 CD1 TYR A 268 -235.745 46.004 40.839 1.00 97.61 C
ANISOU 2145 CD1 TYR A 268 12024 11136 13926 218 -1182 571 C
ATOM 2146 CD2 TYR A 268 -235.154 47.908 39.532 1.00 90.54 C
ANISOU 2146 CD2 TYR A 268 11176 10117 13109 229 -1310 738 C
ATOM 2147 CE1 TYR A 268 -234.402 45.656 40.946 1.00 92.24 C
ANISOU 2147 CE1 TYR A 268 11458 10523 13066 190 -1106 551 C
ATOM 2148 CE2 TYR A 268 -233.821 47.573 39.634 1.00109.94 C
ANISOU 2148 CE2 TYR A 268 13745 12648 15381 195 -1221 709 C
ATOM 2149 CZ TYR A 268 -233.447 46.445 40.338 1.00113.52 C
ANISOU 2149 CZ TYR A 268 14223 13194 15714 180 -1124 616 C
ATOM 2150 OH TYR A 268 -232.108 46.121 40.426 1.00113.47 O
ANISOU 2150 OH TYR A 268 14307 13251 15555 154 -1046 597 O
ATOM 2151 N ALA A 269 -240.618 48.409 40.964 1.00 89.48 N
ANISOU 2151 N ALA A 269 10376 9714 13908 397 -1411 627 N
ATOM 2152 CA ALA A 269 -241.907 48.996 40.604 1.00 99.73 C
ANISOU 2152 CA ALA A 269 11493 10894 15505 448 -1531 693 C
ATOM 2153 C ALA A 269 -242.307 50.122 41.552 1.00104.94 C
ANISOU 2153 C ALA A 269 11997 11414 16463 522 -1402 592 C
ATOM 2154 O ALA A 269 -242.871 51.131 41.115 1.00105.80 O
ANISOU 2154 O ALA A 269 11989 11377 16835 581 -1506 677 O
ATOM 2155 CB ALA A 269 -242.995 47.921 40.574 1.00 85.62 C
ANISOU 2155 CB ALA A 269 9614 9165 13751 425 -1577 679 C
ATOM 2156 N GLY A 270 -242.050 49.966 42.852 1.00105.46 N
ANISOU 2156 N GLY A 270 12060 11515 16497 513 -1178 412 N
ATOM 2157 CA GLY A 270 -242.330 51.049 43.783 1.00104.87 C
ANISOU 2157 CA GLY A 270 11862 11308 16677 566 -1028 289 C
ATOM 2158 C GLY A 270 -241.458 52.267 43.540 1.00112.41 C
ANISOU 2158 C GLY A 270 12885 12163 17664 590 -1045 335 C
ATOM 2159 O GLY A 270 -241.930 53.406 43.604 1.00113.27 O
ANISOU 2159 O GLY A 270 12866 12100 18070 656 -1041 331 O
ATOM 2160 N VAL A 271 -240.171 52.048 43.272 1.00110.07 N
ANISOU 2160 N VAL A 271 12781 11962 17080 536 -1057 376 N
ATOM 2161 CA VAL A 271 -239.281 53.166 42.981 1.00105.13 C
ANISOU 2161 CA VAL A 271 12226 11248 16470 546 -1077 430 C
ATOM 2162 C VAL A 271 -239.674 53.826 41.666 1.00111.31 C
ANISOU 2162 C VAL A 271 12975 11920 17397 583 -1298 633 C
ATOM 2163 O VAL A 271 -239.634 55.054 41.540 1.00131.27 O
ANISOU 2163 O VAL A 271 15457 14290 20131 625 -1321 674 O
ATOM 2164 CB VAL A 271 -237.814 52.695 42.977 1.00 92.69 C
ANISOU 2164 CB VAL A 271 10848 9808 14561 474 -1037 429 C
ATOM 2165 CG1 VAL A 271 -236.959 53.579 42.086 1.00 81.06 C
ANISOU 2165 CG1 VAL A 271 9467 8272 13060 467 -1135 563 C
ATOM 2166 CG2 VAL A 271 -237.266 52.703 44.391 1.00 71.68 C
ANISOU 2166 CG2 VAL A 271 8210 7188 11836 442 -827 240 C
ATOM 2167 N ALA A 272 -240.078 53.029 40.673 1.00 99.94 N
ANISOU 2167 N ALA A 272 11561 10557 15856 558 -1469 767 N
ATOM 2168 CA ALA A 272 -240.501 53.611 39.403 1.00103.23 C
ANISOU 2168 CA ALA A 272 11956 10879 16388 573 -1703 976 C
ATOM 2169 C ALA A 272 -241.807 54.379 39.549 1.00114.80 C
ANISOU 2169 C ALA A 272 13189 12166 18264 662 -1759 993 C
ATOM 2170 O ALA A 272 -241.954 55.471 38.991 1.00115.99 O
ANISOU 2170 O ALA A 272 13291 12159 18621 703 -1881 1122 O
ATOM 2171 CB ALA A 272 -240.645 52.528 38.346 1.00106.75 C
ANISOU 2171 CB ALA A 272 12496 11458 16607 505 -1870 1099 C
ATOM 2172 N PHE A 273 -242.775 53.820 40.283 1.00123.72 N
ANISOU 2172 N PHE A 273 14165 13311 19533 691 -1670 869 N
ATOM 2173 CA PHE A 273 -243.988 54.566 40.597 1.00125.94 C
ANISOU 2173 CA PHE A 273 14197 13413 20242 784 -1674 847 C
ATOM 2174 C PHE A 273 -243.683 55.879 41.310 1.00133.35 C
ANISOU 2174 C PHE A 273 15081 14179 21406 844 -1526 750 C
ATOM 2175 O PHE A 273 -244.507 56.797 41.275 1.00136.69 O
ANISOU 2175 O PHE A 273 15314 14405 22217 931 -1569 781 O
ATOM 2176 CB PHE A 273 -244.929 53.711 41.446 1.00115.00 C
ANISOU 2176 CB PHE A 273 12667 12087 18939 789 -1542 690 C
ATOM 2177 CG PHE A 273 -246.266 54.350 41.699 1.00128.34 C
ANISOU 2177 CG PHE A 273 14075 13601 21089 881 -1543 667 C
ATOM 2178 CD1 PHE A 273 -247.225 54.406 40.699 1.00134.21 C
ANISOU 2178 CD1 PHE A 273 14679 14274 22041 914 -1800 855 C
ATOM 2179 CD2 PHE A 273 -246.567 54.892 42.938 1.00137.60 C
ANISOU 2179 CD2 PHE A 273 15117 14675 22490 930 -1286 453 C
ATOM 2180 CE1 PHE A 273 -248.457 54.994 40.928 1.00134.45 C
ANISOU 2180 CE1 PHE A 273 14423 14129 22531 1007 -1806 839 C
ATOM 2181 CE2 PHE A 273 -247.796 55.480 43.173 1.00143.54 C
ANISOU 2181 CE2 PHE A 273 15593 15252 23693 1020 -1264 417 C
ATOM 2182 CZ PHE A 273 -248.742 55.531 42.167 1.00137.14 C
ANISOU 2182 CZ PHE A 273 14624 14365 23120 1066 -1527 614 C
ATOM 2183 N TYR A 274 -242.520 55.976 41.975 1.00134.89 N
ANISOU 2183 N TYR A 274 15433 14437 21382 799 -1352 629 N
ATOM 2184 CA TYR A 274 -241.986 57.210 42.535 1.00130.19 C
ANISOU 2184 CA TYR A 274 14839 13694 20934 829 -1228 546 C
ATOM 2185 C TYR A 274 -241.232 58.038 41.501 1.00136.00 C
ANISOU 2185 C TYR A 274 15687 14351 21637 821 -1397 743 C
ATOM 2186 O TYR A 274 -240.719 59.112 41.832 1.00130.84 O
ANISOU 2186 O TYR A 274 15047 13563 21103 839 -1316 698 O
ATOM 2187 CB TYR A 274 -241.063 56.903 43.716 1.00132.48 C
ANISOU 2187 CB TYR A 274 15251 14099 20987 764 -985 336 C
ATOM 2188 CG TYR A 274 -241.266 57.800 44.910 1.00132.54 C
ANISOU 2188 CG TYR A 274 15159 13966 21234 795 -760 126 C
ATOM 2189 CD1 TYR A 274 -241.978 57.355 46.010 1.00127.77 C
ANISOU 2189 CD1 TYR A 274 14452 13395 20701 790 -563 -76 C
ATOM 2190 CD2 TYR A 274 -240.739 59.086 44.943 1.00142.21 C
ANISOU 2190 CD2 TYR A 274 16402 15025 22606 817 -733 121 C
ATOM 2191 CE1 TYR A 274 -242.166 58.155 47.106 1.00139.87 C
ANISOU 2191 CE1 TYR A 274 15907 14803 22433 802 -338 -288 C
ATOM 2192 CE2 TYR A 274 -240.923 59.899 46.039 1.00144.55 C
ANISOU 2192 CE2 TYR A 274 16617 15186 23118 835 -515 -91 C
ATOM 2193 CZ TYR A 274 -241.639 59.425 47.118 1.00146.13 C
ANISOU 2193 CZ TYR A 274 16721 15428 23373 825 -313 -301 C
ATOM 2194 OH TYR A 274 -241.834 60.219 48.219 1.00153.14 O
ANISOU 2194 OH TYR A 274 17541 16186 24461 827 -76 -531 O
ATOM 2195 N ILE A 275 -241.173 57.556 40.256 1.00147.22 N
ANISOU 2195 N ILE A 275 17194 15851 22891 783 -1625 955 N
ATOM 2196 CA ILE A 275 -240.690 58.342 39.129 1.00149.78 C
ANISOU 2196 CA ILE A 275 17610 16091 23209 767 -1814 1174 C
ATOM 2197 C ILE A 275 -241.826 58.747 38.189 1.00163.30 C
ANISOU 2197 C ILE A 275 19180 17667 25201 820 -2066 1380 C
ATOM 2198 O ILE A 275 -241.799 59.847 37.629 1.00172.05 O
ANISOU 2198 O ILE A 275 20271 18600 26501 849 -2190 1531 O
ATOM 2199 CB ILE A 275 -239.586 57.582 38.379 1.00130.58 C
ANISOU 2199 CB ILE A 275 15417 13854 20343 658 -1873 1264 C
ATOM 2200 CG1 ILE A 275 -238.311 57.564 39.218 1.00115.87 C
ANISOU 2200 CG1 ILE A 275 13680 12071 18273 614 -1656 1102 C
ATOM 2201 CG2 ILE A 275 -239.325 58.212 37.020 1.00112.68 C
ANISOU 2201 CG2 ILE A 275 13245 11521 18048 621 -2101 1520 C
ATOM 2202 CD1 ILE A 275 -237.161 56.889 38.549 1.00112.74 C
ANISOU 2202 CD1 ILE A 275 13496 11847 17495 517 -1685 1173 C
ATOM 2203 N PHE A 276 -242.825 57.884 37.985 1.00160.80 N
ANISOU 2203 N PHE A 276 18759 17420 24918 827 -2160 1403 N
ATOM 2204 CA PHE A 276 -244.010 58.306 37.235 1.00170.70 C
ANISOU 2204 CA PHE A 276 19836 18530 26492 884 -2401 1588 C
ATOM 2205 C PHE A 276 -244.759 59.419 37.968 1.00179.14 C
ANISOU 2205 C PHE A 276 20660 19348 28056 1011 -2312 1506 C
ATOM 2206 O PHE A 276 -245.111 60.446 37.373 1.00186.71 O
ANISOU 2206 O PHE A 276 21530 20105 29305 1066 -2483 1680 O
ATOM 2207 CB PHE A 276 -244.916 57.104 36.998 1.00180.29 C
ANISOU 2207 CB PHE A 276 20977 19879 27647 858 -2497 1599 C
ATOM 2208 CG PHE A 276 -245.706 57.183 35.744 1.00190.89 C
ANISOU 2208 CG PHE A 276 22261 21171 29098 844 -2831 1863 C
ATOM 2209 CD1 PHE A 276 -245.171 56.744 34.548 1.00191.67 C
ANISOU 2209 CD1 PHE A 276 22579 21398 28850 727 -3032 2049 C
ATOM 2210 CD2 PHE A 276 -246.989 57.688 35.763 1.00196.56 C
ANISOU 2210 CD2 PHE A 276 22702 21714 30267 940 -2945 1923 C
ATOM 2211 CE1 PHE A 276 -245.902 56.814 33.393 1.00195.81 C
ANISOU 2211 CE1 PHE A 276 23066 21886 29447 692 -3355 2297 C
ATOM 2212 CE2 PHE A 276 -247.724 57.761 34.615 1.00198.61 C
ANISOU 2212 CE2 PHE A 276 22901 21929 30632 919 -3280 2182 C
ATOM 2213 CZ PHE A 276 -247.184 57.324 33.425 1.00199.85 C
ANISOU 2213 CZ PHE A 276 23297 22224 30412 788 -3494 2374 C
ATOM 2214 N THR A 277 -245.033 59.224 39.254 1.00181.29 N
ANISOU 2214 N THR A 277 20821 19622 28437 1053 -2042 1244 N
ATOM 2215 CA THR A 277 -245.496 60.282 40.137 1.00177.29 C
ANISOU 2215 CA THR A 277 20121 18888 28351 1157 -1874 1101 C
ATOM 2216 C THR A 277 -244.389 60.604 41.134 1.00172.69 C
ANISOU 2216 C THR A 277 19683 18333 27599 1120 -1601 888 C
ATOM 2217 O THR A 277 -243.493 59.791 41.368 1.00171.88 O
ANISOU 2217 O THR A 277 19776 18442 27088 1027 -1514 816 O
ATOM 2218 CB THR A 277 -246.787 59.886 40.871 1.00183.77 C
ANISOU 2218 CB THR A 277 20684 19676 29464 1222 -1761 950 C
ATOM 2219 OG1 THR A 277 -246.560 58.724 41.680 1.00178.51 O
ANISOU 2219 OG1 THR A 277 20104 19233 28491 1149 -1561 755 O
ATOM 2220 CG2 THR A 277 -247.907 59.594 39.877 1.00192.88 C
ANISOU 2220 CG2 THR A 277 21675 20798 30812 1254 -2053 1169 C
ATOM 2221 N HIS A 278 -244.453 61.805 41.717 1.00172.52 N
ANISOU 2221 N HIS A 278 19559 18085 27904 1191 -1472 789 N
ATOM 2222 CA HIS A 278 -243.361 62.334 42.543 1.00180.69 C
ANISOU 2222 CA HIS A 278 20737 19112 28806 1146 -1250 614 C
ATOM 2223 C HIS A 278 -242.061 62.407 41.740 1.00203.07 C
ANISOU 2223 C HIS A 278 23821 22038 31299 1061 -1380 779 C
ATOM 2224 O HIS A 278 -240.993 62.013 42.212 1.00213.50 O
ANISOU 2224 O HIS A 278 25322 23517 32283 974 -1248 670 O
ATOM 2225 CB HIS A 278 -243.155 61.508 43.819 1.00173.51 C
ANISOU 2225 CB HIS A 278 19874 18378 27676 1086 -973 336 C
ATOM 2226 CG HIS A 278 -244.235 61.670 44.846 1.00170.22 C
ANISOU 2226 CG HIS A 278 19234 17850 27591 1150 -762 117 C
ATOM 2227 ND1 HIS A 278 -245.510 61.177 44.674 1.00179.70 N
ANISOU 2227 ND1 HIS A 278 20227 19036 29015 1209 -824 148 N
ATOM 2228 CD2 HIS A 278 -244.216 62.243 46.073 1.00167.49 C
ANISOU 2228 CD2 HIS A 278 18846 17411 27382 1149 -476 -150 C
ATOM 2229 CE1 HIS A 278 -246.235 61.453 45.744 1.00184.96 C
ANISOU 2229 CE1 HIS A 278 20722 19599 29956 1250 -574 -89 C
ATOM 2230 NE2 HIS A 278 -245.473 62.100 46.608 1.00179.49 N
ANISOU 2230 NE2 HIS A 278 20133 18858 29207 1211 -356 -278 N
ATOM 2231 N GLN A 279 -242.154 62.920 40.512 1.00214.46 N
ANISOU 2231 N GLN A 279 25270 23378 32835 1079 -1644 1051 N
ATOM 2232 CA GLN A 279 -241.021 62.886 39.594 1.00222.81 C
ANISOU 2232 CA GLN A 279 26564 24537 33557 985 -1779 1230 C
ATOM 2233 C GLN A 279 -240.031 64.020 39.839 1.00224.01 C
ANISOU 2233 C GLN A 279 26810 24556 33747 966 -1685 1198 C
ATOM 2234 O GLN A 279 -238.834 63.859 39.570 1.00237.76 O
ANISOU 2234 O GLN A 279 28758 26427 35155 870 -1675 1234 O
ATOM 2235 CB GLN A 279 -241.533 62.926 38.149 1.00230.17 C
ANISOU 2235 CB GLN A 279 27487 25430 34535 985 -2107 1543 C
ATOM 2236 CG GLN A 279 -240.513 63.335 37.086 1.00236.96 C
ANISOU 2236 CG GLN A 279 28563 26307 35164 896 -2261 1762 C
ATOM 2237 CD GLN A 279 -239.436 62.289 36.837 1.00241.38 C
ANISOU 2237 CD GLN A 279 29356 27144 35213 772 -2214 1741 C
ATOM 2238 OE1 GLN A 279 -239.382 61.258 37.504 1.00244.27 O
ANISOU 2238 OE1 GLN A 279 29732 27686 35392 756 -2069 1564 O
ATOM 2239 NE2 GLN A 279 -238.571 62.558 35.866 1.00240.89 N
ANISOU 2239 NE2 GLN A 279 29480 27112 34934 682 -2333 1926 N
ATOM 2240 N GLY A 280 -240.496 65.148 40.376 1.00204.26 N
ANISOU 2240 N GLY A 280 24156 21796 31657 1053 -1602 1118 N
ATOM 2241 CA GLY A 280 -239.682 66.354 40.371 1.00186.20 C
ANISOU 2241 CA GLY A 280 21948 19338 29460 1037 -1568 1139 C
ATOM 2242 C GLY A 280 -238.437 66.268 41.236 1.00178.41 C
ANISOU 2242 C GLY A 280 21126 18477 28186 944 -1341 934 C
ATOM 2243 O GLY A 280 -237.358 66.701 40.822 1.00180.32 O
ANISOU 2243 O GLY A 280 21529 18726 28260 868 -1376 1024 O
ATOM 2244 N SER A 281 -238.563 65.716 42.441 1.00174.79 N
ANISOU 2244 N SER A 281 20628 18119 27666 937 -1111 663 N
ATOM 2245 CA SER A 281 -237.491 65.811 43.422 1.00173.04 C
ANISOU 2245 CA SER A 281 20533 17974 27239 851 -895 451 C
ATOM 2246 C SER A 281 -236.269 64.993 43.007 1.00154.37 C
ANISOU 2246 C SER A 281 18381 15865 24408 738 -947 533 C
ATOM 2247 O SER A 281 -236.352 64.039 42.227 1.00162.50 O
ANISOU 2247 O SER A 281 19457 17059 25225 722 -1089 680 O
ATOM 2248 CB SER A 281 -237.979 65.355 44.800 1.00184.56 C
ANISOU 2248 CB SER A 281 21910 19492 28722 855 -649 155 C
ATOM 2249 OG SER A 281 -238.779 66.347 45.418 1.00194.50 O
ANISOU 2249 OG SER A 281 22999 20492 30408 936 -520 12 O
ATOM 2250 N CYS A 282 -235.119 65.392 43.543 1.00134.93 N
ANISOU 2250 N CYS A 282 16040 13425 21800 655 -825 428 N
ATOM 2251 CA CYS A 282 -233.879 64.666 43.320 1.00129.29 C
ANISOU 2251 CA CYS A 282 15505 12942 20679 549 -839 471 C
ATOM 2252 C CYS A 282 -233.857 63.388 44.150 1.00121.92 C
ANISOU 2252 C CYS A 282 14591 12240 19492 513 -723 309 C
ATOM 2253 O CYS A 282 -234.448 63.311 45.230 1.00120.66 O
ANISOU 2253 O CYS A 282 14346 12061 19438 533 -567 104 O
ATOM 2254 CB CYS A 282 -232.674 65.535 43.689 1.00146.88 C
ANISOU 2254 CB CYS A 282 17834 15111 22862 468 -750 407 C
ATOM 2255 SG CYS A 282 -232.661 67.219 43.008 1.00151.56 S
ANISOU 2255 SG CYS A 282 18402 15386 23796 499 -840 551 S
ATOM 2256 N PHE A 283 -233.151 62.384 43.643 1.00133.38 N
ANISOU 2256 N PHE A 283 16160 13906 20611 454 -792 402 N
ATOM 2257 CA PHE A 283 -233.033 61.092 44.305 1.00133.63 C
ANISOU 2257 CA PHE A 283 16225 14159 20391 416 -708 286 C
ATOM 2258 C PHE A 283 -231.603 60.905 44.790 1.00126.95 C
ANISOU 2258 C PHE A 283 15510 13444 19282 314 -627 218 C
ATOM 2259 O PHE A 283 -230.661 60.971 43.993 1.00133.97 O
ANISOU 2259 O PHE A 283 16496 14376 20030 269 -707 354 O
ATOM 2260 CB PHE A 283 -233.420 59.960 43.360 1.00137.88 C
ANISOU 2260 CB PHE A 283 16779 14834 20776 433 -851 438 C
ATOM 2261 CG PHE A 283 -234.715 60.184 42.645 1.00147.74 C
ANISOU 2261 CG PHE A 283 17906 15957 22273 519 -984 556 C
ATOM 2262 CD1 PHE A 283 -235.834 60.627 43.330 1.00149.57 C
ANISOU 2262 CD1 PHE A 283 17973 16046 22811 594 -910 440 C
ATOM 2263 CD2 PHE A 283 -234.812 59.960 41.283 1.00159.68 C
ANISOU 2263 CD2 PHE A 283 19464 17490 23717 518 -1185 784 C
ATOM 2264 CE1 PHE A 283 -237.029 60.835 42.669 1.00154.68 C
ANISOU 2264 CE1 PHE A 283 18483 16570 23718 678 -1046 559 C
ATOM 2265 CE2 PHE A 283 -236.002 60.168 40.616 1.00165.79 C
ANISOU 2265 CE2 PHE A 283 20121 18150 24720 587 -1336 910 C
ATOM 2266 CZ PHE A 283 -237.113 60.606 41.310 1.00161.72 C
ANISOU 2266 CZ PHE A 283 19422 17489 24537 674 -1274 803 C
ATOM 2267 N GLY A 284 -231.446 60.658 46.086 1.00130.48 N
ANISOU 2267 N GLY A 284 15957 13957 19661 270 -470 12 N
ATOM 2268 CA GLY A 284 -230.154 60.345 46.644 1.00133.26 C
ANISOU 2268 CA GLY A 284 16418 14451 19765 170 -410 -51 C
ATOM 2269 C GLY A 284 -229.572 59.096 46.017 1.00126.38 C
ANISOU 2269 C GLY A 284 15621 13779 18620 147 -495 68 C
ATOM 2270 O GLY A 284 -230.280 58.311 45.374 1.00122.58 O
ANISOU 2270 O GLY A 284 15112 13348 18113 199 -574 158 O
ATOM 2271 N PRO A 285 -228.263 58.889 46.185 1.00121.19 N
ANISOU 2271 N PRO A 285 15051 13230 17767 67 -478 67 N
ATOM 2272 CA PRO A 285 -227.645 57.670 45.640 1.00122.91 C
ANISOU 2272 CA PRO A 285 15329 13627 17744 48 -537 163 C
ATOM 2273 C PRO A 285 -228.271 56.409 46.189 1.00143.16 C
ANISOU 2273 C PRO A 285 17872 16317 20205 65 -510 98 C
ATOM 2274 O PRO A 285 -228.234 55.360 45.531 1.00156.24 O
ANISOU 2274 O PRO A 285 19557 18081 21726 80 -573 189 O
ATOM 2275 CB PRO A 285 -226.178 57.802 46.070 1.00106.66 C
ANISOU 2275 CB PRO A 285 13334 11641 15552 -43 -496 131 C
ATOM 2276 CG PRO A 285 -226.223 58.685 47.275 1.00106.26 C
ANISOU 2276 CG PRO A 285 13261 11505 15608 -86 -397 -37 C
ATOM 2277 CD PRO A 285 -227.314 59.674 46.991 1.00112.22 C
ANISOU 2277 CD PRO A 285 13951 12063 16624 -16 -397 -39 C
ATOM 2278 N ILE A 286 -228.859 56.488 47.378 1.00144.95 N
ANISOU 2278 N ILE A 286 18056 16527 20493 54 -409 -63 N
ATOM 2279 CA ILE A 286 -229.456 55.315 47.991 1.00138.70 C
ANISOU 2279 CA ILE A 286 17248 15851 19600 55 -372 -127 C
ATOM 2280 C ILE A 286 -230.806 54.990 47.356 1.00133.48 C
ANISOU 2280 C ILE A 286 16508 15142 19066 140 -423 -72 C
ATOM 2281 O ILE A 286 -231.094 53.826 47.065 1.00145.75 O
ANISOU 2281 O ILE A 286 18071 16804 20505 153 -467 -22 O
ATOM 2282 CB ILE A 286 -229.555 55.514 49.516 1.00136.51 C
ANISOU 2282 CB ILE A 286 16969 15585 19315 -13 -233 -322 C
ATOM 2283 CG1 ILE A 286 -230.477 56.682 49.871 1.00144.44 C
ANISOU 2283 CG1 ILE A 286 17893 16410 20578 19 -147 -433 C
ATOM 2284 CG2 ILE A 286 -228.167 55.730 50.118 1.00134.22 C
ANISOU 2284 CG2 ILE A 286 16760 15361 18878 -112 -214 -360 C
ATOM 2285 CD1 ILE A 286 -231.826 56.240 50.393 1.00146.26 C
ANISOU 2285 CD1 ILE A 286 18040 16632 20900 53 -68 -528 C
ATOM 2286 N PHE A 287 -231.628 56.005 47.077 1.00119.37 N
ANISOU 2286 N PHE A 287 14638 13186 17531 199 -430 -71 N
ATOM 2287 CA PHE A 287 -233.028 55.756 46.738 1.00124.73 C
ANISOU 2287 CA PHE A 287 15211 13810 18372 274 -467 -47 C
ATOM 2288 C PHE A 287 -233.178 55.085 45.378 1.00136.87 C
ANISOU 2288 C PHE A 287 16770 15398 19836 308 -632 143 C
ATOM 2289 O PHE A 287 -233.868 54.065 45.253 1.00127.63 O
ANISOU 2289 O PHE A 287 15572 14309 18614 323 -662 157 O
ATOM 2290 CB PHE A 287 -233.813 57.060 46.769 1.00121.46 C
ANISOU 2290 CB PHE A 287 14687 13183 18279 334 -442 -84 C
ATOM 2291 CG PHE A 287 -235.219 56.920 46.284 1.00122.26 C
ANISOU 2291 CG PHE A 287 14655 13209 18590 418 -507 -31 C
ATOM 2292 CD1 PHE A 287 -236.210 56.458 47.130 1.00129.32 C
ANISOU 2292 CD1 PHE A 287 15451 14119 19566 430 -394 -170 C
ATOM 2293 CD2 PHE A 287 -235.552 57.247 44.980 1.00132.30 C
ANISOU 2293 CD2 PHE A 287 15897 14396 19974 474 -686 163 C
ATOM 2294 CE1 PHE A 287 -237.509 56.326 46.690 1.00142.24 C
ANISOU 2294 CE1 PHE A 287 16944 15685 21417 506 -458 -121 C
ATOM 2295 CE2 PHE A 287 -236.847 57.117 44.531 1.00145.64 C
ANISOU 2295 CE2 PHE A 287 17452 16017 21867 546 -770 223 C
ATOM 2296 CZ PHE A 287 -237.829 56.656 45.387 1.00150.58 C
ANISOU 2296 CZ PHE A 287 17961 16655 22596 566 -655 79 C
ATOM 2297 N MET A 288 -232.574 55.665 44.337 1.00148.59 N
ANISOU 2297 N MET A 288 18311 16832 21316 308 -737 287 N
ATOM 2298 CA MET A 288 -232.637 55.053 43.013 1.00144.88 C
ANISOU 2298 CA MET A 288 17889 16419 20742 315 -887 461 C
ATOM 2299 C MET A 288 -232.127 53.621 43.036 1.00134.14 C
ANISOU 2299 C MET A 288 16608 15246 19114 273 -871 450 C
ATOM 2300 O MET A 288 -232.522 52.804 42.196 1.00126.43 O
ANISOU 2300 O MET A 288 15652 14330 18055 278 -967 541 O
ATOM 2301 CB MET A 288 -231.823 55.877 42.014 1.00144.20 C
ANISOU 2301 CB MET A 288 17881 16270 20638 290 -971 604 C
ATOM 2302 CG MET A 288 -232.466 57.182 41.610 1.00154.71 C
ANISOU 2302 CG MET A 288 19140 17401 22244 338 -1043 679 C
ATOM 2303 SD MET A 288 -231.297 58.319 40.837 1.00172.32 S
ANISOU 2303 SD MET A 288 21472 19547 24457 286 -1088 807 S
ATOM 2304 CE MET A 288 -230.007 58.404 42.078 1.00162.65 C
ANISOU 2304 CE MET A 288 20293 18391 23114 223 -906 628 C
ATOM 2305 N THR A 289 -231.266 53.296 43.999 1.00120.14 N
ANISOU 2305 N THR A 289 14877 13558 17212 226 -758 340 N
ATOM 2306 CA THR A 289 -230.559 52.028 44.031 1.00105.28 C
ANISOU 2306 CA THR A 289 13071 11835 15097 187 -745 342 C
ATOM 2307 C THR A 289 -230.927 51.174 45.240 1.00106.50 C
ANISOU 2307 C THR A 289 13196 12070 15201 173 -655 214 C
ATOM 2308 O THR A 289 -230.246 50.175 45.510 1.00108.49 O
ANISOU 2308 O THR A 289 13505 12440 15277 138 -634 204 O
ATOM 2309 CB THR A 289 -229.059 52.299 44.000 1.00101.64 C
ANISOU 2309 CB THR A 289 12687 11413 14517 135 -717 359 C
ATOM 2310 OG1 THR A 289 -228.689 52.990 45.197 1.00106.57 O
ANISOU 2310 OG1 THR A 289 13290 12006 15196 104 -622 238 O
ATOM 2311 CG2 THR A 289 -228.720 53.170 42.801 1.00 94.92 C
ANISOU 2311 CG2 THR A 289 11874 10481 13711 135 -794 490 C
ATOM 2312 N ILE A 290 -231.972 51.548 45.985 1.00102.43 N
ANISOU 2312 N ILE A 290 12591 11486 14843 195 -596 116 N
ATOM 2313 CA ILE A 290 -232.518 50.639 46.996 1.00 92.84 C
ANISOU 2313 CA ILE A 290 11352 10350 13573 172 -513 11 C
ATOM 2314 C ILE A 290 -232.980 49.332 46.370 1.00100.63 C
ANISOU 2314 C ILE A 290 12349 11421 14467 186 -586 85 C
ATOM 2315 O ILE A 290 -232.683 48.268 46.929 1.00 97.00 O
ANISOU 2315 O ILE A 290 11933 11069 13852 146 -548 52 O
ATOM 2316 CB ILE A 290 -233.612 51.343 47.810 1.00 90.70 C
ANISOU 2316 CB ILE A 290 10975 9981 13508 189 -416 -114 C
ATOM 2317 CG1 ILE A 290 -232.993 52.261 48.867 1.00 96.34 C
ANISOU 2317 CG1 ILE A 290 11714 10657 14236 136 -299 -242 C
ATOM 2318 CG2 ILE A 290 -234.516 50.324 48.480 1.00 81.67 C
ANISOU 2318 CG2 ILE A 290 9789 8908 12335 173 -353 -187 C
ATOM 2319 CD1 ILE A 290 -234.001 53.082 49.636 1.00 97.90 C
ANISOU 2319 CD1 ILE A 290 11810 10735 14652 149 -176 -387 C
ATOM 2320 N PRO A 291 -233.696 49.315 45.234 1.00 99.89 N
ANISOU 2320 N PRO A 291 12219 11280 14454 232 -698 188 N
ATOM 2321 CA PRO A 291 -234.045 48.016 44.635 1.00 87.71 C
ANISOU 2321 CA PRO A 291 10703 9822 12800 228 -766 247 C
ATOM 2322 C PRO A 291 -232.833 47.183 44.251 1.00 85.79 C
ANISOU 2322 C PRO A 291 10581 9681 12336 192 -781 296 C
ATOM 2323 O PRO A 291 -232.804 45.976 44.522 1.00 85.28 O
ANISOU 2323 O PRO A 291 10546 9702 12154 169 -760 275 O
ATOM 2324 CB PRO A 291 -234.879 48.411 43.408 1.00 90.28 C
ANISOU 2324 CB PRO A 291 10983 10070 13251 268 -904 360 C
ATOM 2325 CG PRO A 291 -235.442 49.736 43.754 1.00100.66 C
ANISOU 2325 CG PRO A 291 12192 11248 14807 311 -880 326 C
ATOM 2326 CD PRO A 291 -234.360 50.425 44.526 1.00104.05 C
ANISOU 2326 CD PRO A 291 12673 11670 15193 285 -773 251 C
ATOM 2327 N ALA A 292 -231.832 47.794 43.617 1.00 80.39 N
ANISOU 2327 N ALA A 292 9959 8979 11605 185 -810 361 N
ATOM 2328 CA ALA A 292 -230.610 47.067 43.299 1.00 68.68 C
ANISOU 2328 CA ALA A 292 8570 7583 9941 153 -800 393 C
ATOM 2329 C ALA A 292 -229.950 46.533 44.561 1.00 81.33 C
ANISOU 2329 C ALA A 292 10180 9255 11466 124 -708 306 C
ATOM 2330 O ALA A 292 -229.506 45.377 44.602 1.00 62.54 O
ANISOU 2330 O ALA A 292 7842 6953 8967 109 -700 313 O
ATOM 2331 CB ALA A 292 -229.648 47.972 42.533 1.00 70.53 C
ANISOU 2331 CB ALA A 292 8856 7781 10162 141 -823 466 C
ATOM 2332 N PHE A 293 -229.907 47.351 45.615 1.00 82.01 N
ANISOU 2332 N PHE A 293 10228 9309 11624 108 -642 225 N
ATOM 2333 CA PHE A 293 -229.226 46.945 46.839 1.00 93.25 C
ANISOU 2333 CA PHE A 293 11671 10802 12956 59 -574 153 C
ATOM 2334 C PHE A 293 -229.795 45.648 47.398 1.00 70.86 C
ANISOU 2334 C PHE A 293 8836 8037 10050 45 -556 125 C
ATOM 2335 O PHE A 293 -229.071 44.873 48.032 1.00 91.95 O
ANISOU 2335 O PHE A 293 11545 10782 12608 7 -540 121 O
ATOM 2336 CB PHE A 293 -229.307 48.063 47.880 1.00 95.47 C
ANISOU 2336 CB PHE A 293 11920 11032 13321 28 -501 52 C
ATOM 2337 CG PHE A 293 -228.388 47.864 49.047 1.00103.89 C
ANISOU 2337 CG PHE A 293 13027 12173 14275 -46 -454 -6 C
ATOM 2338 CD1 PHE A 293 -227.021 48.070 48.912 1.00108.21 C
ANISOU 2338 CD1 PHE A 293 13609 12747 14758 -73 -481 39 C
ATOM 2339 CD2 PHE A 293 -228.884 47.468 50.277 1.00103.73 C
ANISOU 2339 CD2 PHE A 293 13006 12197 14210 -100 -388 -98 C
ATOM 2340 CE1 PHE A 293 -226.166 47.886 49.982 1.00100.77 C
ANISOU 2340 CE1 PHE A 293 12694 11874 13718 -148 -463 0 C
ATOM 2341 CE2 PHE A 293 -228.034 47.283 51.353 1.00118.42 C
ANISOU 2341 CE2 PHE A 293 14915 14131 15948 -185 -367 -136 C
ATOM 2342 CZ PHE A 293 -226.672 47.494 51.206 1.00107.64 C
ANISOU 2342 CZ PHE A 293 13577 12792 14530 -207 -415 -83 C
ATOM 2343 N PHE A 294 -231.073 45.378 47.155 1.00 81.30 N
ANISOU 2343 N PHE A 294 10112 9333 11447 72 -568 117 N
ATOM 2344 CA PHE A 294 -231.691 44.169 47.677 1.00 89.71 C
ANISOU 2344 CA PHE A 294 11175 10457 12456 51 -546 91 C
ATOM 2345 C PHE A 294 -231.917 43.100 46.618 1.00 82.50 C
ANISOU 2345 C PHE A 294 10288 9566 11494 75 -621 169 C
ATOM 2346 O PHE A 294 -232.040 41.923 46.968 1.00 93.08 O
ANISOU 2346 O PHE A 294 11650 10958 12758 52 -610 165 O
ATOM 2347 CB PHE A 294 -233.014 44.522 48.364 1.00 99.27 C
ANISOU 2347 CB PHE A 294 12302 11627 13789 45 -482 3 C
ATOM 2348 CG PHE A 294 -232.837 45.315 49.629 1.00117.04 C
ANISOU 2348 CG PHE A 294 14546 13869 16054 -5 -377 -106 C
ATOM 2349 CD1 PHE A 294 -231.872 44.950 50.557 1.00121.69 C
ANISOU 2349 CD1 PHE A 294 15208 14536 16491 -75 -344 -128 C
ATOM 2350 CD2 PHE A 294 -233.617 46.432 49.886 1.00130.13 C
ANISOU 2350 CD2 PHE A 294 16124 15436 17883 13 -314 -186 C
ATOM 2351 CE1 PHE A 294 -231.699 45.676 51.722 1.00137.90 C
ANISOU 2351 CE1 PHE A 294 17273 16590 18532 -143 -253 -233 C
ATOM 2352 CE2 PHE A 294 -233.448 47.164 51.051 1.00135.18 C
ANISOU 2352 CE2 PHE A 294 16770 16064 18528 -46 -201 -308 C
ATOM 2353 CZ PHE A 294 -232.488 46.785 51.969 1.00141.10 C
ANISOU 2353 CZ PHE A 294 17612 16906 19095 -132 -172 -333 C
ATOM 2354 N ALA A 295 -231.956 43.473 45.340 1.00 81.64 N
ANISOU 2354 N ALA A 295 10186 9415 11418 110 -697 240 N
ATOM 2355 CA ALA A 295 -232.034 42.474 44.284 1.00 72.95 C
ANISOU 2355 CA ALA A 295 9135 8341 10244 114 -763 303 C
ATOM 2356 C ALA A 295 -230.747 41.664 44.162 1.00 94.72 C
ANISOU 2356 C ALA A 295 11970 11151 12867 100 -742 325 C
ATOM 2357 O ALA A 295 -230.776 40.558 43.609 1.00 75.88 O
ANISOU 2357 O ALA A 295 9627 8790 10412 95 -762 346 O
ATOM 2358 CB ALA A 295 -232.360 43.148 42.951 1.00 69.62 C
ANISOU 2358 CB ALA A 295 8718 7867 9868 134 -855 379 C
ATOM 2359 N LYS A 296 -229.623 42.191 44.659 1.00 97.79 N
ANISOU 2359 N LYS A 296 12370 11551 13233 93 -700 318 N
ATOM 2360 CA LYS A 296 -228.382 41.424 44.669 1.00 84.25 C
ANISOU 2360 CA LYS A 296 10701 9881 11429 85 -678 338 C
ATOM 2361 C LYS A 296 -228.517 40.160 45.508 1.00 82.97 C
ANISOU 2361 C LYS A 296 10542 9759 11224 69 -659 317 C
ATOM 2362 O LYS A 296 -227.917 39.127 45.180 1.00 74.08 O
ANISOU 2362 O LYS A 296 9450 8648 10047 75 -659 344 O
ATOM 2363 CB LYS A 296 -227.229 42.284 45.197 1.00 88.96 C
ANISOU 2363 CB LYS A 296 11287 10481 12030 71 -648 334 C
ATOM 2364 CG LYS A 296 -226.820 43.443 44.304 1.00 92.83 C
ANISOU 2364 CG LYS A 296 11787 10929 12556 78 -661 370 C
ATOM 2365 CD LYS A 296 -225.694 44.245 44.945 1.00 90.98 C
ANISOU 2365 CD LYS A 296 11536 10699 12334 53 -630 357 C
ATOM 2366 CE LYS A 296 -225.352 45.471 44.116 1.00 99.99 C
ANISOU 2366 CE LYS A 296 12685 11785 13519 51 -638 395 C
ATOM 2367 NZ LYS A 296 -225.064 45.104 42.699 1.00110.43 N
ANISOU 2367 NZ LYS A 296 14061 13111 14788 59 -652 463 N
ATOM 2368 N THR A 297 -229.306 40.222 46.587 1.00 57.10 N
ANISOU 2368 N THR A 297 7232 6492 7972 43 -636 268 N
ATOM 2369 CA THR A 297 -229.479 39.083 47.484 1.00 60.73 C
ANISOU 2369 CA THR A 297 7703 6989 8382 10 -619 259 C
ATOM 2370 C THR A 297 -230.093 37.874 46.782 1.00 73.42 C
ANISOU 2370 C THR A 297 9331 8588 9976 22 -645 281 C
ATOM 2371 O THR A 297 -229.963 36.752 47.281 1.00 62.00 O
ANISOU 2371 O THR A 297 7908 7159 8489 2 -640 295 O
ATOM 2372 CB THR A 297 -230.334 39.516 48.683 1.00 62.85 C
ANISOU 2372 CB THR A 297 7938 7270 8674 -37 -570 191 C
ATOM 2373 OG1 THR A 297 -229.679 40.596 49.351 1.00 88.91 O
ANISOU 2373 OG1 THR A 297 11233 10575 11974 -61 -543 158 O
ATOM 2374 CG2 THR A 297 -230.511 38.394 49.683 1.00 83.12 C
ANISOU 2374 CG2 THR A 297 10529 9880 11171 -91 -551 191 C
ATOM 2375 N SER A 298 -230.730 38.068 45.623 1.00 74.88 N
ANISOU 2375 N SER A 298 9515 8742 10196 47 -682 291 N
ATOM 2376 CA SER A 298 -231.278 36.940 44.876 1.00 59.69 C
ANISOU 2376 CA SER A 298 7622 6810 8250 45 -713 304 C
ATOM 2377 C SER A 298 -230.225 35.886 44.564 1.00 76.22 C
ANISOU 2377 C SER A 298 9774 8905 10280 52 -699 329 C
ATOM 2378 O SER A 298 -230.575 34.714 44.386 1.00 75.08 O
ANISOU 2378 O SER A 298 9658 8750 10120 40 -704 327 O
ATOM 2379 CB SER A 298 -231.924 37.414 43.575 1.00 61.10 C
ANISOU 2379 CB SER A 298 7803 6960 8452 56 -775 324 C
ATOM 2380 OG SER A 298 -230.943 37.806 42.624 1.00 80.26 O
ANISOU 2380 OG SER A 298 10284 9381 10831 70 -783 358 O
ATOM 2381 N ALA A 299 -228.944 36.269 44.491 1.00 51.99 N
ANISOU 2381 N ALA A 299 6716 5841 7195 72 -678 349 N
ATOM 2382 CA ALA A 299 -227.895 35.289 44.237 1.00 48.12 C
ANISOU 2382 CA ALA A 299 6259 5341 6684 88 -653 367 C
ATOM 2383 C ALA A 299 -227.750 34.287 45.373 1.00 64.27 C
ANISOU 2383 C ALA A 299 8293 7390 8735 76 -649 382 C
ATOM 2384 O ALA A 299 -227.091 33.257 45.189 1.00 58.90 O
ANISOU 2384 O ALA A 299 7632 6681 8068 94 -635 400 O
ATOM 2385 CB ALA A 299 -226.558 35.987 43.992 1.00 64.36 C
ANISOU 2385 CB ALA A 299 8306 7403 8746 109 -626 386 C
ATOM 2386 N VAL A 300 -228.352 34.552 46.526 1.00 59.54 N
ANISOU 2386 N VAL A 300 7668 6820 8133 40 -656 374 N
ATOM 2387 CA VAL A 300 -228.291 33.662 47.676 1.00 60.13 C
ANISOU 2387 CA VAL A 300 7748 6906 8193 5 -661 402 C
ATOM 2388 C VAL A 300 -229.613 32.929 47.889 1.00 81.74 C
ANISOU 2388 C VAL A 300 10496 9636 10926 -32 -658 382 C
ATOM 2389 O VAL A 300 -229.630 31.711 48.070 1.00 89.56 O
ANISOU 2389 O VAL A 300 11513 10599 11916 -44 -665 412 O
ATOM 2390 CB VAL A 300 -227.873 34.432 48.947 1.00 64.19 C
ANISOU 2390 CB VAL A 300 8242 7469 8679 -37 -663 408 C
ATOM 2391 CG1 VAL A 300 -227.952 33.530 50.165 1.00 60.55 C
ANISOU 2391 CG1 VAL A 300 7803 7027 8177 -96 -679 448 C
ATOM 2392 CG2 VAL A 300 -226.467 34.986 48.776 1.00 74.92 C
ANISOU 2392 CG2 VAL A 300 9581 8831 10053 -8 -676 437 C
ATOM 2393 N TYR A 301 -230.739 33.653 47.862 1.00 78.20 N
ANISOU 2393 N TYR A 301 10018 9202 10493 -51 -646 334 N
ATOM 2394 CA TYR A 301 -231.995 33.007 48.232 1.00 78.98 C
ANISOU 2394 CA TYR A 301 10108 9300 10601 -97 -634 313 C
ATOM 2395 C TYR A 301 -232.635 32.252 47.073 1.00 81.88 C
ANISOU 2395 C TYR A 301 10490 9627 10994 -83 -664 308 C
ATOM 2396 O TYR A 301 -233.399 31.311 47.313 1.00 86.33 O
ANISOU 2396 O TYR A 301 11060 10178 11564 -125 -661 306 O
ATOM 2397 CB TYR A 301 -232.987 34.017 48.836 1.00 69.43 C
ANISOU 2397 CB TYR A 301 8839 8115 9425 -128 -595 256 C
ATOM 2398 CG TYR A 301 -233.488 35.131 47.935 1.00 79.92 C
ANISOU 2398 CG TYR A 301 10117 9423 10827 -85 -614 225 C
ATOM 2399 CD1 TYR A 301 -234.421 34.886 46.934 1.00 89.99 C
ANISOU 2399 CD1 TYR A 301 11368 10669 12154 -72 -659 224 C
ATOM 2400 CD2 TYR A 301 -233.074 36.442 48.132 1.00 81.06 C
ANISOU 2400 CD2 TYR A 301 10236 9570 10994 -66 -596 203 C
ATOM 2401 CE1 TYR A 301 -234.891 35.909 46.128 1.00 94.70 C
ANISOU 2401 CE1 TYR A 301 11917 11241 12823 -38 -699 218 C
ATOM 2402 CE2 TYR A 301 -233.544 37.470 47.338 1.00 82.54 C
ANISOU 2402 CE2 TYR A 301 10375 9722 11264 -27 -623 191 C
ATOM 2403 CZ TYR A 301 -234.449 37.199 46.335 1.00 89.15 C
ANISOU 2403 CZ TYR A 301 11189 10532 12153 -12 -680 207 C
ATOM 2404 OH TYR A 301 -234.913 38.226 45.542 1.00 89.18 O
ANISOU 2404 OH TYR A 301 11144 10495 12244 23 -730 217 O
ATOM 2405 N ASN A 302 -232.349 32.624 45.826 1.00 73.27 N
ANISOU 2405 N ASN A 302 9415 8517 9908 -41 -694 306 N
ATOM 2406 CA ASN A 302 -232.869 31.830 44.712 1.00 65.84 C
ANISOU 2406 CA ASN A 302 8509 7542 8964 -48 -727 297 C
ATOM 2407 C ASN A 302 -232.325 30.407 44.710 1.00 65.58 C
ANISOU 2407 C ASN A 302 8535 7470 8914 -53 -709 310 C
ATOM 2408 O ASN A 302 -233.128 29.467 44.571 1.00 78.89 O
ANISOU 2408 O ASN A 302 10236 9128 10610 -92 -721 296 O
ATOM 2409 CB ASN A 302 -232.601 32.530 43.376 1.00 50.91 C
ANISOU 2409 CB ASN A 302 6645 5645 7053 -22 -761 296 C
ATOM 2410 CG ASN A 302 -233.716 33.472 42.981 1.00 72.36 C
ANISOU 2410 CG ASN A 302 9309 8371 9814 -33 -817 292 C
ATOM 2411 OD1 ASN A 302 -234.833 33.380 43.490 1.00 84.87 O
ANISOU 2411 OD1 ASN A 302 10832 9959 11457 -59 -827 276 O
ATOM 2412 ND2 ASN A 302 -233.422 34.381 42.056 1.00 82.46 N
ANISOU 2412 ND2 ASN A 302 10606 9649 11077 -14 -853 313 N
ATOM 2413 N PRO A 303 -231.018 30.160 44.860 1.00 77.46 N
ANISOU 2413 N PRO A 303 10062 8958 10412 -17 -682 336 N
ATOM 2414 CA PRO A 303 -230.572 28.760 44.953 1.00 71.24 C
ANISOU 2414 CA PRO A 303 9312 8110 9646 -16 -666 353 C
ATOM 2415 C PRO A 303 -231.101 28.052 46.185 1.00 72.90 C
ANISOU 2415 C PRO A 303 9512 8318 9869 -62 -672 388 C
ATOM 2416 O PRO A 303 -231.280 26.830 46.155 1.00 85.03 O
ANISOU 2416 O PRO A 303 11083 9794 11433 -81 -671 397 O
ATOM 2417 CB PRO A 303 -229.041 28.873 44.975 1.00 73.11 C
ANISOU 2417 CB PRO A 303 9542 8331 9905 39 -640 383 C
ATOM 2418 CG PRO A 303 -228.740 30.233 44.455 1.00 87.76 C
ANISOU 2418 CG PRO A 303 11380 10235 11732 60 -637 366 C
ATOM 2419 CD PRO A 303 -229.876 31.093 44.867 1.00 78.71 C
ANISOU 2419 CD PRO A 303 10204 9138 10565 25 -667 353 C
ATOM 2420 N VAL A 304 -231.368 28.783 47.271 1.00 75.93 N
ANISOU 2420 N VAL A 304 9857 8762 10229 -93 -673 405 N
ATOM 2421 CA VAL A 304 -231.982 28.164 48.443 1.00 73.33 C
ANISOU 2421 CA VAL A 304 9531 8443 9888 -161 -667 435 C
ATOM 2422 C VAL A 304 -233.385 27.673 48.112 1.00 79.04 C
ANISOU 2422 C VAL A 304 10249 9152 10631 -209 -662 394 C
ATOM 2423 O VAL A 304 -233.779 26.566 48.494 1.00 80.55 O
ANISOU 2423 O VAL A 304 10468 9306 10832 -257 -659 420 O
ATOM 2424 CB VAL A 304 -231.994 29.149 49.627 1.00 64.94 C
ANISOU 2424 CB VAL A 304 8440 7455 8779 -200 -650 439 C
ATOM 2425 CG1 VAL A 304 -232.803 28.579 50.776 1.00 73.50 C
ANISOU 2425 CG1 VAL A 304 9538 8561 9829 -294 -625 457 C
ATOM 2426 CG2 VAL A 304 -230.583 29.441 50.082 1.00 67.06 C
ANISOU 2426 CG2 VAL A 304 8716 7737 9028 -173 -674 493 C
ATOM 2427 N ILE A 305 -234.157 28.481 47.388 1.00 69.56 N
ANISOU 2427 N ILE A 305 9008 7975 9447 -200 -668 338 N
ATOM 2428 CA ILE A 305 -235.542 28.128 47.095 1.00 77.91 C
ANISOU 2428 CA ILE A 305 10036 9025 10541 -250 -677 303 C
ATOM 2429 C ILE A 305 -235.616 27.081 45.992 1.00 78.04 C
ANISOU 2429 C ILE A 305 10108 8978 10566 -252 -712 292 C
ATOM 2430 O ILE A 305 -236.233 26.025 46.167 1.00 76.03 O
ANISOU 2430 O ILE A 305 9869 8687 10332 -307 -710 294 O
ATOM 2431 CB ILE A 305 -236.340 29.390 46.732 1.00 68.75 C
ANISOU 2431 CB ILE A 305 8798 7903 9422 -239 -690 261 C
ATOM 2432 CG1 ILE A 305 -236.505 30.265 47.970 1.00 73.17 C
ANISOU 2432 CG1 ILE A 305 9303 8511 9987 -258 -629 246 C
ATOM 2433 CG2 ILE A 305 -237.688 29.019 46.136 1.00 76.00 C
ANISOU 2433 CG2 ILE A 305 9673 8805 10399 -281 -727 232 C
ATOM 2434 CD1 ILE A 305 -237.076 31.598 47.674 1.00 68.35 C
ANISOU 2434 CD1 ILE A 305 8609 7915 9444 -229 -633 205 C
ATOM 2435 N TYR A 306 -234.982 27.351 44.848 1.00 67.94 N
ANISOU 2435 N TYR A 306 8865 7683 9266 -203 -736 276 N
ATOM 2436 CA TYR A 306 -235.097 26.476 43.684 1.00 65.26 C
ANISOU 2436 CA TYR A 306 8590 7288 8917 -220 -759 243 C
ATOM 2437 C TYR A 306 -234.214 25.236 43.736 1.00 80.92 C
ANISOU 2437 C TYR A 306 10642 9193 10913 -206 -720 252 C
ATOM 2438 O TYR A 306 -234.482 24.279 42.998 1.00 83.48 O
ANISOU 2438 O TYR A 306 11021 9455 11241 -239 -723 212 O
ATOM 2439 CB TYR A 306 -234.787 27.257 42.402 1.00 60.50 C
ANISOU 2439 CB TYR A 306 8016 6702 8268 -193 -790 217 C
ATOM 2440 CG TYR A 306 -235.862 28.243 42.021 1.00 78.85 C
ANISOU 2440 CG TYR A 306 10280 9076 10605 -216 -859 215 C
ATOM 2441 CD1 TYR A 306 -235.860 29.531 42.541 1.00 70.99 C
ANISOU 2441 CD1 TYR A 306 9211 8125 9637 -179 -858 237 C
ATOM 2442 CD2 TYR A 306 -236.886 27.884 41.156 1.00 72.88 C
ANISOU 2442 CD2 TYR A 306 9533 8310 9846 -277 -931 191 C
ATOM 2443 CE1 TYR A 306 -236.844 30.431 42.207 1.00 86.53 C
ANISOU 2443 CE1 TYR A 306 11108 10117 11653 -190 -923 240 C
ATOM 2444 CE2 TYR A 306 -237.877 28.783 40.816 1.00 92.67 C
ANISOU 2444 CE2 TYR A 306 11966 10852 12392 -294 -1013 205 C
ATOM 2445 CZ TYR A 306 -237.849 30.054 41.346 1.00 82.58 C
ANISOU 2445 CZ TYR A 306 10606 9607 11164 -243 -1006 231 C
ATOM 2446 OH TYR A 306 -238.827 30.956 41.015 1.00 92.47 O
ANISOU 2446 OH TYR A 306 11769 10873 12490 -249 -1088 250 O
ATOM 2447 N ILE A 307 -233.167 25.211 44.566 1.00 76.44 N
ANISOU 2447 N ILE A 307 10066 8616 10361 -162 -688 303 N
ATOM 2448 CA ILE A 307 -232.238 24.086 44.532 1.00 81.58 C
ANISOU 2448 CA ILE A 307 10762 9174 11059 -133 -657 319 C
ATOM 2449 C ILE A 307 -232.116 23.437 45.899 1.00 77.74 C
ANISOU 2449 C ILE A 307 10263 8665 10611 -153 -663 402 C
ATOM 2450 O ILE A 307 -232.336 22.232 46.052 1.00 75.57 O
ANISOU 2450 O ILE A 307 10022 8306 10385 -183 -661 418 O
ATOM 2451 CB ILE A 307 -230.855 24.520 44.005 1.00 65.85 C
ANISOU 2451 CB ILE A 307 8774 7172 9075 -56 -623 314 C
ATOM 2452 CG1 ILE A 307 -230.980 25.065 42.585 1.00 72.71 C
ANISOU 2452 CG1 ILE A 307 9680 8062 9884 -58 -613 238 C
ATOM 2453 CG2 ILE A 307 -229.892 23.357 44.035 1.00 63.80 C
ANISOU 2453 CG2 ILE A 307 8535 6801 8905 -17 -585 331 C
ATOM 2454 CD1 ILE A 307 -229.688 25.569 42.017 1.00 67.95 C
ANISOU 2454 CD1 ILE A 307 9081 7457 9281 2 -562 227 C
ATOM 2455 N MET A 308 -231.761 24.235 46.912 1.00 72.69 N
ANISOU 2455 N MET A 308 9581 8096 9942 -148 -674 457 N
ATOM 2456 CA MET A 308 -231.621 23.694 48.257 1.00 77.05 C
ANISOU 2456 CA MET A 308 10135 8640 10501 -188 -692 548 C
ATOM 2457 C MET A 308 -232.905 23.036 48.744 1.00 75.18 C
ANISOU 2457 C MET A 308 9915 8399 10253 -280 -688 551 C
ATOM 2458 O MET A 308 -232.855 22.077 49.524 1.00 85.49 O
ANISOU 2458 O MET A 308 11251 9653 11579 -323 -701 627 O
ATOM 2459 CB MET A 308 -231.208 24.791 49.236 1.00 83.40 C
ANISOU 2459 CB MET A 308 10905 9540 11245 -195 -704 587 C
ATOM 2460 CG MET A 308 -229.770 25.235 49.124 1.00114.29 C
ANISOU 2460 CG MET A 308 14795 13448 15182 -120 -720 618 C
ATOM 2461 SD MET A 308 -228.676 24.091 49.968 1.00134.92 S
ANISOU 2461 SD MET A 308 17417 15980 17869 -110 -773 748 S
ATOM 2462 CE MET A 308 -227.109 24.931 49.777 1.00136.58 C
ANISOU 2462 CE MET A 308 17566 16209 18119 -27 -790 768 C
ATOM 2463 N MET A 309 -234.061 23.531 48.311 1.00 78.14 N
ANISOU 2463 N MET A 309 10262 8822 10605 -317 -674 477 N
ATOM 2464 CA MET A 309 -235.327 22.936 48.714 1.00 98.45 C
ANISOU 2464 CA MET A 309 12832 11392 13184 -409 -661 471 C
ATOM 2465 C MET A 309 -235.776 21.807 47.794 1.00 96.42 C
ANISOU 2465 C MET A 309 12613 11041 12982 -428 -673 436 C
ATOM 2466 O MET A 309 -236.739 21.109 48.128 1.00110.48 O
ANISOU 2466 O MET A 309 14395 12801 14783 -511 -665 440 O
ATOM 2467 CB MET A 309 -236.412 24.011 48.793 1.00 96.59 C
ANISOU 2467 CB MET A 309 12523 11247 12930 -443 -641 412 C
ATOM 2468 CG MET A 309 -236.256 24.904 50.006 1.00 99.45 C
ANISOU 2468 CG MET A 309 12857 11691 13238 -466 -605 435 C
ATOM 2469 SD MET A 309 -237.531 26.162 50.141 1.00113.40 S
ANISOU 2469 SD MET A 309 14522 13538 15026 -496 -557 350 S
ATOM 2470 CE MET A 309 -237.378 26.564 51.871 1.00120.34 C
ANISOU 2470 CE MET A 309 15414 14489 15821 -575 -484 377 C
ATOM 2471 N ASN A 310 -235.112 21.614 46.657 1.00 99.89 N
ANISOU 2471 N ASN A 310 13088 11423 13443 -364 -682 394 N
ATOM 2472 CA ASN A 310 -235.349 20.439 45.829 1.00 99.92 C
ANISOU 2472 CA ASN A 310 13149 11322 13494 -388 -682 351 C
ATOM 2473 C ASN A 310 -234.935 19.185 46.590 1.00 83.85 C
ANISOU 2473 C ASN A 310 11153 9180 11525 -404 -672 427 C
ATOM 2474 O ASN A 310 -233.863 19.134 47.197 1.00 92.18 O
ANISOU 2474 O ASN A 310 12208 10210 12606 -349 -673 502 O
ATOM 2475 CB ASN A 310 -234.565 20.558 44.521 1.00108.59 C
ANISOU 2475 CB ASN A 310 14287 12384 14587 -323 -670 282 C
ATOM 2476 CG ASN A 310 -235.000 19.552 43.477 1.00115.90 C
ANISOU 2476 CG ASN A 310 15282 13220 15535 -369 -665 202 C
ATOM 2477 OD1 ASN A 310 -235.437 18.450 43.806 1.00118.91 O
ANISOU 2477 OD1 ASN A 310 15689 13518 15972 -423 -662 215 O
ATOM 2478 ND2 ASN A 310 -234.884 19.928 42.207 1.00107.33 N
ANISOU 2478 ND2 ASN A 310 14236 12150 14395 -361 -664 119 N
ATOM 2479 N LYS A 311 -235.794 18.164 46.556 1.00 94.01 N
ANISOU 2479 N LYS A 311 12470 10398 12851 -483 -672 416 N
ATOM 2480 CA LYS A 311 -235.585 17.003 47.418 1.00113.70 C
ANISOU 2480 CA LYS A 311 15001 12789 15412 -516 -672 508 C
ATOM 2481 C LYS A 311 -234.322 16.235 47.038 1.00111.63 C
ANISOU 2481 C LYS A 311 14779 12388 15247 -431 -661 524 C
ATOM 2482 O LYS A 311 -233.577 15.782 47.917 1.00 86.21 O
ANISOU 2482 O LYS A 311 11562 9110 12085 -407 -681 639 O
ATOM 2483 CB LYS A 311 -236.803 16.081 47.371 1.00123.25 C
ANISOU 2483 CB LYS A 311 16232 13945 16652 -627 -669 485 C
ATOM 2484 CG LYS A 311 -236.749 14.953 48.394 1.00126.29 C
ANISOU 2484 CG LYS A 311 16657 14231 17097 -683 -672 599 C
ATOM 2485 CD LYS A 311 -238.007 14.099 48.371 1.00127.96 C
ANISOU 2485 CD LYS A 311 16886 14395 17339 -805 -664 576 C
ATOM 2486 CE LYS A 311 -237.959 13.022 49.446 1.00136.48 C
ANISOU 2486 CE LYS A 311 18012 15375 18470 -873 -668 707 C
ATOM 2487 NZ LYS A 311 -239.154 12.133 49.403 1.00141.77 N
ANISOU 2487 NZ LYS A 311 18700 15986 19181 -1001 -653 685 N
ATOM 2488 N GLN A 312 -234.061 16.081 45.740 1.00106.29 N
ANISOU 2488 N GLN A 312 14132 11656 14597 -389 -630 411 N
ATOM 2489 CA GLN A 312 -232.899 15.306 45.320 1.00111.40 C
ANISOU 2489 CA GLN A 312 14808 12155 15362 -309 -592 403 C
ATOM 2490 C GLN A 312 -231.599 16.064 45.582 1.00113.46 C
ANISOU 2490 C GLN A 312 15016 12456 15637 -203 -590 455 C
ATOM 2491 O GLN A 312 -230.652 15.504 46.148 1.00112.37 O
ANISOU 2491 O GLN A 312 14858 12221 15618 -146 -599 545 O
ATOM 2492 CB GLN A 312 -233.031 14.913 43.846 1.00116.09 C
ANISOU 2492 CB GLN A 312 15464 12682 15963 -316 -537 247 C
ATOM 2493 CG GLN A 312 -233.604 15.993 42.947 1.00137.28 C
ANISOU 2493 CG GLN A 312 18149 15505 18504 -345 -548 154 C
ATOM 2494 CD GLN A 312 -233.813 15.510 41.522 1.00146.12 C
ANISOU 2494 CD GLN A 312 19354 16563 19601 -386 -507 6 C
ATOM 2495 OE1 GLN A 312 -234.254 16.267 40.655 1.00151.18 O
ANISOU 2495 OE1 GLN A 312 20014 17302 20125 -422 -528 -65 O
ATOM 2496 NE2 GLN A 312 -233.497 14.244 41.274 1.00139.77 N
ANISOU 2496 NE2 GLN A 312 18607 15588 18910 -389 -451 -38 N
ATOM 2497 N PHE A 313 -231.537 17.343 45.185 1.00102.30 N
ANISOU 2497 N PHE A 313 13573 11180 14118 -179 -587 408 N
ATOM 2498 CA PHE A 313 -230.331 18.139 45.410 1.00 94.99 C
ANISOU 2498 CA PHE A 313 12592 10299 13202 -91 -585 452 C
ATOM 2499 C PHE A 313 -229.906 18.102 46.871 1.00 95.73 C
ANISOU 2499 C PHE A 313 12644 10404 13325 -89 -648 605 C
ATOM 2500 O PHE A 313 -228.715 17.980 47.182 1.00107.03 O
ANISOU 2500 O PHE A 313 14034 11781 14850 -16 -660 674 O
ATOM 2501 CB PHE A 313 -230.554 19.594 44.983 1.00 87.09 C
ANISOU 2501 CB PHE A 313 11568 9451 12073 -89 -586 399 C
ATOM 2502 CG PHE A 313 -230.398 19.843 43.502 1.00 96.92 C
ANISOU 2502 CG PHE A 313 12852 10690 13285 -70 -531 275 C
ATOM 2503 CD1 PHE A 313 -229.143 20.031 42.946 1.00 96.22 C
ANISOU 2503 CD1 PHE A 313 12750 10566 13244 9 -470 246 C
ATOM 2504 CD2 PHE A 313 -231.510 19.924 42.672 1.00107.70 C
ANISOU 2504 CD2 PHE A 313 14264 12090 14565 -143 -542 190 C
ATOM 2505 CE1 PHE A 313 -228.994 20.275 41.583 1.00 87.34 C
ANISOU 2505 CE1 PHE A 313 11677 9444 12064 7 -405 130 C
ATOM 2506 CE2 PHE A 313 -231.369 20.168 41.308 1.00 96.20 C
ANISOU 2506 CE2 PHE A 313 12863 10638 13049 -147 -502 85 C
ATOM 2507 CZ PHE A 313 -230.106 20.343 40.765 1.00 79.68 C
ANISOU 2507 CZ PHE A 313 10775 8514 10986 -76 -426 52 C
ATOM 2508 N ARG A 314 -230.874 18.194 47.780 1.00 81.61 N
ANISOU 2508 N ARG A 314 10865 8686 11457 -179 -689 660 N
ATOM 2509 CA ARG A 314 -230.571 18.332 49.200 1.00 90.46 C
ANISOU 2509 CA ARG A 314 11967 9851 12552 -209 -749 800 C
ATOM 2510 C ARG A 314 -229.799 17.126 49.718 1.00106.39 C
ANISOU 2510 C ARG A 314 13995 11721 14709 -185 -791 919 C
ATOM 2511 O ARG A 314 -228.733 17.270 50.329 1.00100.83 O
ANISOU 2511 O ARG A 314 13251 11009 14050 -138 -846 1023 O
ATOM 2512 CB ARG A 314 -231.875 18.520 49.973 1.00 97.36 C
ANISOU 2512 CB ARG A 314 12860 10816 13315 -328 -754 814 C
ATOM 2513 CG ARG A 314 -231.749 19.037 51.395 1.00 98.12 C
ANISOU 2513 CG ARG A 314 12952 11010 13321 -389 -796 923 C
ATOM 2514 CD ARG A 314 -233.078 18.872 52.142 1.00115.73 C
ANISOU 2514 CD ARG A 314 15211 13295 15468 -522 -772 932 C
ATOM 2515 NE ARG A 314 -234.217 19.379 51.373 1.00124.71 N
ANISOU 2515 NE ARG A 314 16318 14487 16579 -541 -714 798 N
ATOM 2516 CZ ARG A 314 -235.057 18.616 50.677 1.00137.01 C
ANISOU 2516 CZ ARG A 314 17890 15976 18192 -572 -694 740 C
ATOM 2517 NH1 ARG A 314 -234.890 17.301 50.649 1.00146.03 N
ANISOU 2517 NH1 ARG A 314 19082 16982 19420 -586 -711 794 N
ATOM 2518 NH2 ARG A 314 -236.058 19.166 50.002 1.00141.88 N
ANISOU 2518 NH2 ARG A 314 18466 16652 18790 -592 -666 632 N
ATOM 2519 N ASN A 315 -230.325 15.920 49.476 1.00114.11 N
ANISOU 2519 N ASN A 315 15020 12568 15768 -219 -775 912 N
ATOM 2520 CA ASN A 315 -229.663 14.713 49.963 1.00109.60 C
ANISOU 2520 CA ASN A 315 14457 11829 15355 -196 -819 1034 C
ATOM 2521 C ASN A 315 -228.300 14.530 49.313 1.00 97.55 C
ANISOU 2521 C ASN A 315 12876 10192 13996 -61 -798 1016 C
ATOM 2522 O ASN A 315 -227.339 14.109 49.970 1.00104.91 O
ANISOU 2522 O ASN A 315 13766 11040 15055 -13 -867 1153 O
ATOM 2523 CB ASN A 315 -230.540 13.490 49.704 1.00127.83 C
ANISOU 2523 CB ASN A 315 16831 14009 17730 -261 -792 1008 C
ATOM 2524 CG ASN A 315 -231.890 13.587 50.379 1.00132.56 C
ANISOU 2524 CG ASN A 315 17471 14708 18188 -402 -802 1030 C
ATOM 2525 OD1 ASN A 315 -232.046 14.278 51.386 1.00142.00 O
ANISOU 2525 OD1 ASN A 315 18658 16037 19260 -460 -840 1111 O
ATOM 2526 ND2 ASN A 315 -232.876 12.891 49.828 1.00121.07 N
ANISOU 2526 ND2 ASN A 315 16059 13189 16755 -467 -760 948 N
ATOM 2527 N CYS A 316 -228.195 14.840 48.020 1.00 85.06 N
ANISOU 2527 N CYS A 316 11290 8608 12420 -5 -704 851 N
ATOM 2528 CA CYS A 316 -226.915 14.703 47.334 1.00 90.13 C
ANISOU 2528 CA CYS A 316 11875 9149 13221 116 -652 811 C
ATOM 2529 C CYS A 316 -225.863 15.634 47.928 1.00 96.21 C
ANISOU 2529 C CYS A 316 12557 10010 13989 174 -708 902 C
ATOM 2530 O CYS A 316 -224.700 15.245 48.086 1.00108.31 O
ANISOU 2530 O CYS A 316 14014 11435 15705 262 -726 974 O
ATOM 2531 CB CYS A 316 -227.095 14.967 45.842 1.00 78.92 C
ANISOU 2531 CB CYS A 316 10490 7737 11760 133 -532 611 C
ATOM 2532 SG CYS A 316 -228.135 13.744 45.002 1.00 88.63 S
ANISOU 2532 SG CYS A 316 11824 8832 13019 62 -467 487 S
ATOM 2533 N MET A 317 -226.254 16.864 48.275 1.00 95.37 N
ANISOU 2533 N MET A 317 12451 10094 13692 126 -738 901 N
ATOM 2534 CA MET A 317 -225.310 17.790 48.893 1.00 90.18 C
ANISOU 2534 CA MET A 317 11717 9528 13017 162 -797 983 C
ATOM 2535 C MET A 317 -224.889 17.313 50.278 1.00 95.79 C
ANISOU 2535 C MET A 317 12407 10207 13781 134 -927 1181 C
ATOM 2536 O MET A 317 -223.724 17.468 50.661 1.00 97.84 O
ANISOU 2536 O MET A 317 12584 10447 14143 194 -990 1274 O
ATOM 2537 CB MET A 317 -225.916 19.189 48.968 1.00102.00 C
ANISOU 2537 CB MET A 317 13229 11220 14306 107 -793 927 C
ATOM 2538 CG MET A 317 -226.206 19.788 47.611 1.00120.45 C
ANISOU 2538 CG MET A 317 15583 13595 16589 133 -693 761 C
ATOM 2539 SD MET A 317 -226.819 21.474 47.682 1.00126.25 S
ANISOU 2539 SD MET A 317 16316 14528 17125 85 -698 711 S
ATOM 2540 CE MET A 317 -227.435 21.637 46.012 1.00123.74 C
ANISOU 2540 CE MET A 317 16046 14205 16763 92 -606 544 C
ATOM 2541 N VAL A 318 -225.817 16.732 51.041 1.00 91.58 N
ANISOU 2541 N VAL A 318 11947 9670 13179 34 -975 1254 N
ATOM 2542 CA VAL A 318 -225.448 16.150 52.330 1.00 95.85 C
ANISOU 2542 CA VAL A 318 12490 10169 13761 -12 -1106 1458 C
ATOM 2543 C VAL A 318 -224.442 15.026 52.132 1.00101.50 C
ANISOU 2543 C VAL A 318 13145 10673 14749 89 -1139 1539 C
ATOM 2544 O VAL A 318 -223.435 14.938 52.846 1.00106.07 O
ANISOU 2544 O VAL A 318 13657 11217 15429 121 -1254 1696 O
ATOM 2545 CB VAL A 318 -226.701 15.661 53.081 1.00 98.84 C
ANISOU 2545 CB VAL A 318 12969 10573 14013 -151 -1127 1511 C
ATOM 2546 CG1 VAL A 318 -226.308 14.991 54.395 1.00107.52 C
ANISOU 2546 CG1 VAL A 318 14090 11622 15141 -215 -1269 1739 C
ATOM 2547 CG2 VAL A 318 -227.652 16.818 53.329 1.00 93.73 C
ANISOU 2547 CG2 VAL A 318 12358 10127 13130 -243 -1084 1426 C
ATOM 2548 N THR A 319 -224.694 14.155 51.153 1.00107.23 N
ANISOU 2548 N THR A 319 13889 11246 15608 138 -1039 1432 N
ATOM 2549 CA THR A 319 -223.765 13.069 50.861 1.00104.52 C
ANISOU 2549 CA THR A 319 13480 10676 15555 244 -1040 1479 C
ATOM 2550 C THR A 319 -222.401 13.604 50.443 1.00 96.06 C
ANISOU 2550 C THR A 319 12279 9594 14624 369 -1020 1458 C
ATOM 2551 O THR A 319 -221.365 13.076 50.860 1.00 94.50 O
ANISOU 2551 O THR A 319 11985 9269 14653 443 -1101 1594 O
ATOM 2552 CB THR A 319 -224.347 12.176 49.769 1.00100.67 C
ANISOU 2552 CB THR A 319 13049 10042 15159 260 -906 1321 C
ATOM 2553 OG1 THR A 319 -225.577 11.602 50.226 1.00120.27 O
ANISOU 2553 OG1 THR A 319 15638 12521 17537 138 -935 1358 O
ATOM 2554 CG2 THR A 319 -223.386 11.072 49.429 1.00101.80 C
ANISOU 2554 CG2 THR A 319 13121 9934 15625 374 -882 1346 C
ATOM 2555 N THR A 320 -222.383 14.657 49.625 1.00 92.90 N
ANISOU 2555 N THR A 320 11868 9324 14105 390 -918 1298 N
ATOM 2556 CA THR A 320 -221.115 15.212 49.162 1.00 86.67 C
ANISOU 2556 CA THR A 320 10956 8532 13442 497 -879 1265 C
ATOM 2557 C THR A 320 -220.376 15.925 50.286 1.00101.61 C
ANISOU 2557 C THR A 320 12771 10531 15306 485 -1035 1437 C
ATOM 2558 O THR A 320 -219.166 15.737 50.458 1.00111.02 O
ANISOU 2558 O THR A 320 13832 11634 16715 571 -1086 1526 O
ATOM 2559 CB THR A 320 -221.358 16.159 47.987 1.00 79.07 C
ANISOU 2559 CB THR A 320 10022 7684 12338 503 -733 1060 C
ATOM 2560 OG1 THR A 320 -221.887 15.419 46.883 1.00 95.45 O
ANISOU 2560 OG1 THR A 320 12167 9647 14452 510 -595 901 O
ATOM 2561 CG2 THR A 320 -220.064 16.834 47.562 1.00 84.94 C
ANISOU 2561 CG2 THR A 320 10640 8442 13191 595 -686 1030 C
ATOM 2562 N LEU A 321 -221.085 16.737 51.066 1.00105.68 N
ANISOU 2562 N LEU A 321 13359 11229 15565 372 -1110 1481 N
ATOM 2563 CA LEU A 321 -220.482 17.445 52.190 1.00106.28 C
ANISOU 2563 CA LEU A 321 13388 11419 15575 329 -1260 1633 C
ATOM 2564 C LEU A 321 -219.983 16.475 53.258 1.00118.57 C
ANISOU 2564 C LEU A 321 14915 12861 17275 316 -1430 1861 C
ATOM 2565 O LEU A 321 -219.002 16.749 53.949 1.00125.13 O
ANISOU 2565 O LEU A 321 15657 13713 18174 327 -1566 2003 O
ATOM 2566 CB LEU A 321 -221.482 18.432 52.797 1.00 99.50 C
ANISOU 2566 CB LEU A 321 12632 10765 14409 198 -1278 1608 C
ATOM 2567 CG LEU A 321 -221.795 19.640 51.912 1.00 97.38 C
ANISOU 2567 CG LEU A 321 12370 10624 14006 210 -1153 1422 C
ATOM 2568 CD1 LEU A 321 -222.783 20.581 52.587 1.00 92.53 C
ANISOU 2568 CD1 LEU A 321 11840 10187 13129 87 -1169 1401 C
ATOM 2569 CD2 LEU A 321 -220.504 20.360 51.553 1.00 78.26 C
ANISOU 2569 CD2 LEU A 321 9828 8219 11688 296 -1149 1409 C
ATOM 2570 N CYS A 322 -220.652 15.335 53.383 1.00118.05 N
ANISOU 2570 N CYS A 322 14923 12670 17262 287 -1434 1906 N
ATOM 2571 CA CYS A 322 -220.278 14.364 54.374 1.00129.66 C
ANISOU 2571 CA CYS A 322 16381 14018 18866 264 -1602 2138 C
ATOM 2572 C CYS A 322 -219.432 13.202 53.859 1.00131.36 C
ANISOU 2572 C CYS A 322 16487 13972 19452 404 -1593 2178 C
ATOM 2573 O CYS A 322 -219.418 12.083 54.382 1.00134.29 O
ANISOU 2573 O CYS A 322 16869 14179 19975 397 -1691 2337 O
ATOM 2574 CB CYS A 322 -221.459 13.835 55.179 1.00144.48 C
ANISOU 2574 CB CYS A 322 18409 15918 20569 117 -1653 2223 C
ATOM 2575 SG CYS A 322 -221.489 14.526 56.808 1.00156.78 S
ANISOU 2575 SG CYS A 322 20031 17670 21867 -51 -1842 2418 S
ATOM 2576 N CYS A 323 -218.711 13.495 52.779 1.00119.24 N
ANISOU 2576 N CYS A 323 14843 12392 18071 533 -1459 2024 N
ATOM 2577 CA CYS A 323 -217.714 12.587 52.216 1.00115.31 C
ANISOU 2577 CA CYS A 323 14207 11653 17953 682 -1419 2031 C
ATOM 2578 C CYS A 323 -218.291 11.231 51.819 1.00107.48 C
ANISOU 2578 C CYS A 323 13280 10443 17114 701 -1346 1997 C
ATOM 2579 O CYS A 323 -217.582 10.227 51.807 1.00113.33 O
ANISOU 2579 O CYS A 323 13923 10950 18188 798 -1374 2082 O
ATOM 2580 CB CYS A 323 -216.568 12.389 53.209 1.00124.73 C
ANISOU 2580 CB CYS A 323 15260 12782 19348 718 -1634 2284 C
ATOM 2581 SG CYS A 323 -216.051 13.906 54.043 1.00132.63 S
ANISOU 2581 SG CYS A 323 16221 14053 20119 640 -1779 2372 S
ATOM 2582 N GLY A 324 -219.581 11.205 51.499 1.00 98.75 N
ANISOU 2582 N GLY A 324 12333 9404 15782 606 -1254 1873 N
ATOM 2583 CA GLY A 324 -220.235 10.010 51.005 1.00 84.16 C
ANISOU 2583 CA GLY A 324 10561 7365 14049 606 -1167 1805 C
ATOM 2584 C GLY A 324 -221.188 9.347 51.972 1.00106.00 C
ANISOU 2584 C GLY A 324 13450 10116 16710 478 -1287 1962 C
ATOM 2585 O GLY A 324 -221.995 8.514 51.540 1.00114.86 O
ANISOU 2585 O GLY A 324 14662 11120 17858 444 -1204 1880 O
ATOM 2586 N LYS A 325 -221.131 9.682 53.256 1.00124.24 N
ANISOU 2586 N LYS A 325 15774 12540 18893 391 -1476 2180 N
ATOM 2587 CA LYS A 325 -221.953 9.039 54.269 1.00138.18 C
ANISOU 2587 CA LYS A 325 17658 14291 20553 252 -1593 2351 C
ATOM 2588 C LYS A 325 -223.169 9.899 54.593 1.00142.49 C
ANISOU 2588 C LYS A 325 18333 15087 20719 97 -1558 2279 C
ATOM 2589 O LYS A 325 -223.129 11.127 54.481 1.00144.74 O
ANISOU 2589 O LYS A 325 18601 15576 20819 88 -1524 2184 O
ATOM 2590 CB LYS A 325 -221.138 8.776 55.536 1.00142.11 C
ANISOU 2590 CB LYS A 325 18105 14748 21142 231 -1830 2653 C
ATOM 2591 CG LYS A 325 -219.904 7.915 55.303 1.00151.66 C
ANISOU 2591 CG LYS A 325 19158 15693 22771 393 -1885 2751 C
ATOM 2592 CD LYS A 325 -220.286 6.522 54.813 1.00157.28 C
ANISOU 2592 CD LYS A 325 19905 16131 23723 433 -1807 2722 C
ATOM 2593 CE LYS A 325 -219.059 5.683 54.481 1.00158.04 C
ANISOU 2593 CE LYS A 325 19830 15943 24277 610 -1829 2788 C
ATOM 2594 NZ LYS A 325 -218.302 6.236 53.324 1.00158.02 N
ANISOU 2594 NZ LYS A 325 19693 15939 24407 759 -1650 2557 N
ATOM 2595 N ASN A 326 -224.250 9.234 54.996 1.00145.10 N
ANISOU 2595 N ASN A 326 18786 15390 20954 -27 -1562 2323 N
ATOM 2596 CA ASN A 326 -225.522 9.890 55.301 1.00152.43 C
ANISOU 2596 CA ASN A 326 19827 16527 21561 -178 -1510 2249 C
ATOM 2597 C ASN A 326 -226.010 10.711 54.109 1.00154.26 C
ANISOU 2597 C ASN A 326 20048 16868 21696 -134 -1338 1977 C
ATOM 2598 O ASN A 326 -227.138 10.540 53.647 1.00154.69 O
ANISOU 2598 O ASN A 326 20174 16939 21660 -200 -1239 1850 O
ATOM 2599 CB ASN A 326 -225.395 10.780 56.544 1.00155.35 C
ANISOU 2599 CB ASN A 326 20222 17103 21701 -288 -1636 2393 C
ATOM 2600 CG ASN A 326 -226.743 11.231 57.086 1.00158.18 C
ANISOU 2600 CG ASN A 326 20700 17641 21761 -463 -1583 2349 C
ATOM 2601 OD1 ASN A 326 -227.746 11.248 56.372 1.00161.96 O
ANISOU 2601 OD1 ASN A 326 21213 18140 22186 -483 -1444 2173 O
ATOM 2602 ND2 ASN A 326 -226.770 11.603 58.361 1.00158.17 N
ANISOU 2602 ND2 ASN A 326 20759 17771 21568 -599 -1693 2506 N
TER 2603 ASN A 326
HETATM 2604 C1 NAG B 1 -216.989 70.277 40.448 1.00 88.73 C
ANISOU 2604 C1 NAG B 1 11471 8086 14158 -886 -544 1040 C
HETATM 2605 C2 NAG B 1 -216.216 70.032 39.155 1.00 96.84 C
ANISOU 2605 C2 NAG B 1 12564 9205 15025 -963 -557 1239 C
HETATM 2606 C3 NAG B 1 -214.731 69.943 39.447 1.00 90.80 C
ANISOU 2606 C3 NAG B 1 11777 8560 14164 -1089 -467 1180 C
HETATM 2607 C4 NAG B 1 -214.284 71.288 40.006 1.00 91.59 C
ANISOU 2607 C4 NAG B 1 11868 8470 14462 -1177 -439 1120 C
HETATM 2608 C5 NAG B 1 -215.094 71.660 41.257 1.00 89.38 C
ANISOU 2608 C5 NAG B 1 11542 8074 14343 -1109 -436 924 C
HETATM 2609 C6 NAG B 1 -214.863 73.090 41.689 1.00 72.41 C
ANISOU 2609 C6 NAG B 1 9400 5692 12420 -1188 -411 868 C
HETATM 2610 C7 NAG B 1 -216.804 67.648 38.485 1.00 68.81 C
ANISOU 2610 C7 NAG B 1 9022 5996 11126 -845 -589 1281 C
HETATM 2611 C8 NAG B 1 -216.370 67.123 39.814 1.00 98.64 C
ANISOU 2611 C8 NAG B 1 12718 9885 14876 -840 -520 1070 C
HETATM 2612 N2 NAG B 1 -216.698 68.966 38.273 1.00 60.32 N
ANISOU 2612 N2 NAG B 1 7976 4720 10223 -902 -607 1352 N
HETATM 2613 O3 NAG B 1 -214.002 69.607 38.272 1.00 80.39 O
ANISOU 2613 O3 NAG B 1 10512 7343 12691 -1162 -449 1343 O
HETATM 2614 O4 NAG B 1 -212.904 71.239 40.351 1.00 86.15 O
ANISOU 2614 O4 NAG B 1 11142 7890 13702 -1302 -367 1060 O
HETATM 2615 O5 NAG B 1 -216.519 71.524 41.062 1.00 68.58 O
ANISOU 2615 O5 NAG B 1 8910 5355 11791 -968 -499 957 O
HETATM 2616 O6 NAG B 1 -215.147 74.005 40.639 1.00 75.96 O
ANISOU 2616 O6 NAG B 1 9910 5942 13009 -1195 -464 1066 O
HETATM 2617 O7 NAG B 1 -217.243 66.901 37.615 1.00 89.68 O
ANISOU 2617 O7 NAG B 1 11711 8725 13638 -808 -636 1389 O
HETATM 2618 C1 NAG B 2 -212.119 72.183 39.602 1.00 64.30 C
ANISOU 2618 C1 NAG B 2 8417 5016 10996 -1428 -346 1192 C
HETATM 2619 C2 NAG B 2 -210.897 72.507 40.448 1.00 64.69 C
ANISOU 2619 C2 NAG B 2 8400 5104 11074 -1556 -282 1062 C
HETATM 2620 C3 NAG B 2 -210.014 73.512 39.722 1.00 70.32 C
ANISOU 2620 C3 NAG B 2 9149 5705 11863 -1702 -248 1191 C
HETATM 2621 C4 NAG B 2 -209.683 73.023 38.318 1.00 66.55 C
ANISOU 2621 C4 NAG B 2 8725 5330 11230 -1731 -225 1395 C
HETATM 2622 C5 NAG B 2 -210.945 72.613 37.563 1.00 66.04 C
ANISOU 2622 C5 NAG B 2 8740 5245 11108 -1603 -302 1513 C
HETATM 2623 C6 NAG B 2 -210.641 71.955 36.239 1.00 72.97 C
ANISOU 2623 C6 NAG B 2 9683 6257 11785 -1641 -274 1686 C
HETATM 2624 C7 NAG B 2 -211.267 72.257 42.862 1.00 85.42 C
ANISOU 2624 C7 NAG B 2 10934 7769 13752 -1515 -280 685 C
HETATM 2625 C8 NAG B 2 -211.689 72.939 44.128 1.00 96.99 C
ANISOU 2625 C8 NAG B 2 12394 9106 15352 -1529 -270 481 C
HETATM 2626 N2 NAG B 2 -211.277 73.012 41.758 1.00 70.40 N
ANISOU 2626 N2 NAG B 2 9092 5724 11932 -1543 -287 863 N
HETATM 2627 O3 NAG B 2 -208.812 73.693 40.462 1.00 82.70 O
ANISOU 2627 O3 NAG B 2 10640 7334 13448 -1828 -194 1076 O
HETATM 2628 O4 NAG B 2 -209.033 74.063 37.600 1.00 83.18 O
ANISOU 2628 O4 NAG B 2 10884 7305 13415 -1871 -195 1532 O
HETATM 2629 O5 NAG B 2 -211.700 71.667 38.334 1.00 68.60 O
ANISOU 2629 O5 NAG B 2 9012 5674 11380 -1465 -332 1372 O
HETATM 2630 O6 NAG B 2 -211.643 72.217 35.266 1.00 73.93 O
ANISOU 2630 O6 NAG B 2 9917 6272 11903 -1597 -365 1866 O
HETATM 2631 O7 NAG B 2 -210.939 71.075 42.839 1.00 96.29 O
ANISOU 2631 O7 NAG B 2 12268 9363 14954 -1485 -277 688 O
HETATM 2632 C1 BMA B 3 -207.721 73.663 37.173 1.00108.91 C
ANISOU 2632 C1 BMA B 3 14099 10726 16556 -1992 -96 1567 C
HETATM 2633 C2 BMA B 3 -207.264 74.729 36.184 1.00113.32 C
ANISOU 2633 C2 BMA B 3 14743 11139 17175 -2136 -67 1752 C
HETATM 2634 C3 BMA B 3 -205.837 74.441 35.760 1.00117.66 C
ANISOU 2634 C3 BMA B 3 15235 11840 17632 -2281 60 1779 C
HETATM 2635 C4 BMA B 3 -204.922 74.248 36.971 1.00137.46 C
ANISOU 2635 C4 BMA B 3 17584 14439 20204 -2321 95 1581 C
HETATM 2636 C5 BMA B 3 -205.500 73.179 37.897 1.00146.27 C
ANISOU 2636 C5 BMA B 3 18633 15689 21253 -2166 40 1422 C
HETATM 2637 C6 BMA B 3 -204.707 73.038 39.166 1.00153.86 C
ANISOU 2637 C6 BMA B 3 19455 16730 22274 -2212 41 1238 C
HETATM 2638 O2 BMA B 3 -207.264 76.008 36.805 1.00108.00 O
ANISOU 2638 O2 BMA B 3 14070 10237 16728 -2194 -96 1704 O
HETATM 2639 O3 BMA B 3 -205.332 75.478 34.949 1.00114.90 O
ANISOU 2639 O3 BMA B 3 14959 11354 17342 -2437 101 1938 O
HETATM 2640 O4 BMA B 3 -203.645 73.831 36.533 1.00155.56 O
ANISOU 2640 O4 BMA B 3 19796 16885 22425 -2436 213 1610 O
HETATM 2641 O5 BMA B 3 -206.827 73.578 38.265 1.00127.82 O
ANISOU 2641 O5 BMA B 3 16372 13199 18996 -2050 -58 1393 O
HETATM 2642 O6 BMA B 3 -204.762 74.287 39.826 1.00159.00 O
ANISOU 2642 O6 BMA B 3 20128 17182 23104 -2286 3 1173 O
HETATM 2643 C1 MAN B 4 -205.294 75.042 33.577 1.00114.09 C
ANISOU 2643 C1 MAN B 4 14957 11340 17052 -2479 154 2121 C
HETATM 2644 C2 MAN B 4 -204.286 75.946 32.862 1.00114.46 C
ANISOU 2644 C2 MAN B 4 15042 11311 17137 -2688 250 2253 C
HETATM 2645 C3 MAN B 4 -204.804 77.385 32.862 1.00123.13 C
ANISOU 2645 C3 MAN B 4 16234 12116 18432 -2731 153 2355 C
HETATM 2646 C4 MAN B 4 -206.237 77.462 32.295 1.00129.26 C
ANISOU 2646 C4 MAN B 4 17150 12779 19185 -2610 12 2496 C
HETATM 2647 C5 MAN B 4 -207.160 76.469 33.029 1.00125.16 C
ANISOU 2647 C5 MAN B 4 16567 12362 18625 -2402 -62 2341 C
HETATM 2648 C6 MAN B 4 -208.558 76.379 32.419 1.00107.94 C
ANISOU 2648 C6 MAN B 4 14501 10101 16411 -2282 -201 2479 C
HETATM 2649 O2 MAN B 4 -204.150 75.582 31.489 1.00112.76 O
ANISOU 2649 O2 MAN B 4 14940 11186 16717 -2766 325 2431 O
HETATM 2650 O3 MAN B 4 -203.940 78.260 32.139 1.00133.43 O
ANISOU 2650 O3 MAN B 4 17592 13336 19770 -2933 235 2500 O
HETATM 2651 O4 MAN B 4 -206.748 78.774 32.459 1.00133.91 O
ANISOU 2651 O4 MAN B 4 17795 13075 20009 -2624 -85 2567 O
HETATM 2652 O5 MAN B 4 -206.570 75.143 32.994 1.00130.83 O
ANISOU 2652 O5 MAN B 4 17211 13359 19138 -2385 39 2250 O
HETATM 2653 O6 MAN B 4 -209.463 75.842 33.400 1.00 87.07 O
ANISOU 2653 O6 MAN B 4 11778 7474 13830 -2096 -273 2308 O
HETATM 2654 C1 MAN B 5 -204.359 74.077 41.193 1.00163.47 C
ANISOU 2654 C1 MAN B 5 20590 17822 23699 -2308 -30 977 C
HETATM 2655 C2 MAN B 5 -205.335 74.896 42.101 1.00165.26 C
ANISOU 2655 C2 MAN B 5 20883 17855 24052 -2268 -94 848 C
HETATM 2656 C3 MAN B 5 -204.988 76.397 42.113 1.00161.69 C
ANISOU 2656 C3 MAN B 5 20473 17168 23794 -2410 -79 857 C
HETATM 2657 C4 MAN B 5 -203.466 76.653 42.187 1.00167.42 C
ANISOU 2657 C4 MAN B 5 21101 17965 24546 -2598 -35 855 C
HETATM 2658 C5 MAN B 5 -202.765 75.853 41.090 1.00162.17 C
ANISOU 2658 C5 MAN B 5 20388 17475 23755 -2608 33 1015 C
HETATM 2659 C6 MAN B 5 -201.265 76.056 41.046 1.00150.74 C
ANISOU 2659 C6 MAN B 5 18823 16099 22353 -2787 93 1027 C
HETATM 2660 O2 MAN B 5 -205.285 74.456 43.462 1.00173.01 O
ANISOU 2660 O2 MAN B 5 21798 18934 25002 -2262 -137 648 O
HETATM 2661 O3 MAN B 5 -205.651 77.072 43.177 1.00152.79 O
ANISOU 2661 O3 MAN B 5 19379 15884 22791 -2397 -117 684 O
HETATM 2662 O4 MAN B 5 -203.190 78.038 42.012 1.00170.74 O
ANISOU 2662 O4 MAN B 5 21573 18155 25145 -2732 -15 891 O
HETATM 2663 O5 MAN B 5 -203.007 74.468 41.345 1.00162.29 O
ANISOU 2663 O5 MAN B 5 20346 17705 23613 -2478 13 964 O
HETATM 2664 O6 MAN B 5 -200.773 75.383 39.890 1.00143.16 O
ANISOU 2664 O6 MAN B 5 17837 15272 21286 -2789 186 1177 O
HETATM 2665 C1 PLM A 401 -222.453 15.952 56.663 1.00138.39 C
ANISOU 2665 C1 PLM A 401 17780 15591 19210 -140 -1715 2221 C
HETATM 2666 O2 PLM A 401 -223.555 15.991 56.116 1.00136.86 O
ANISOU 2666 O2 PLM A 401 17657 15428 18917 -170 -1578 2070 O
HETATM 2667 C2 PLM A 401 -221.575 17.160 56.843 1.00140.54 C
ANISOU 2667 C2 PLM A 401 17975 15997 19425 -121 -1764 2213 C
HETATM 2668 C3 PLM A 401 -220.171 16.837 57.319 1.00131.24 C
ANISOU 2668 C3 PLM A 401 16683 14735 18449 -63 -1937 2403 C
HETATM 2669 C4 PLM A 401 -219.759 17.646 58.535 1.00114.93 C
ANISOU 2669 C4 PLM A 401 14639 12832 16197 -188 -2100 2535 C
HETATM 2670 C5 PLM A 401 -219.819 19.141 58.278 1.00 99.95 C
ANISOU 2670 C5 PLM A 401 12736 11120 14120 -206 -2009 2366 C
HETATM 2671 C6 PLM A 401 -219.838 19.905 59.587 1.00102.11 C
ANISOU 2671 C6 PLM A 401 13090 11569 14136 -380 -2136 2460 C
HETATM 2672 C7 PLM A 401 -219.215 21.282 59.470 1.00100.42 C
ANISOU 2672 C7 PLM A 401 12811 11488 13855 -371 -2124 2366 C
HETATM 2673 C8 PLM A 401 -220.188 22.294 58.903 1.00 89.09 C
ANISOU 2673 C8 PLM A 401 11437 10168 12245 -387 -1929 2133 C
HETATM 2674 C9 PLM A 401 -219.709 23.711 59.139 1.00 87.77 C
ANISOU 2674 C9 PLM A 401 11244 10146 11957 -430 -1940 2066 C
HETATM 2675 CA PLM A 401 -220.567 24.701 58.375 1.00105.63 C
ANISOU 2675 CA PLM A 401 13536 12485 14113 -410 -1746 1839 C
HETATM 2676 CB PLM A 401 -220.579 26.065 59.031 1.00100.16 C
ANISOU 2676 CB PLM A 401 12885 11952 13219 -522 -1751 1775 C
HETATM 2677 CC PLM A 401 -219.265 26.794 58.844 1.00105.63 C
ANISOU 2677 CC PLM A 401 13461 12662 14013 -467 -1822 1792 C
HETATM 2678 CD PLM A 401 -219.369 28.213 59.362 1.00106.96 C
ANISOU 2678 CD PLM A 401 13676 12975 13988 -576 -1801 1696 C
HETATM 2679 CE PLM A 401 -218.185 29.066 58.960 1.00100.53 C
ANISOU 2679 CE PLM A 401 12742 12174 13282 -515 -1835 1676 C
HETATM 2680 CF PLM A 401 -218.514 30.535 59.127 1.00 90.36 C
ANISOU 2680 CF PLM A 401 11503 11001 11829 -594 -1756 1529 C
HETATM 2681 CG PLM A 401 -217.473 31.404 58.477 1.00 89.00 C
ANISOU 2681 CG PLM A 401 11209 10826 11780 -519 -1752 1485 C
HETATM 2682 C1 BOG A 407 -229.405 44.815 38.965 1.00112.45 C
ANISOU 2682 C1 BOG A 407 14419 13263 15044 69 -963 648 C
HETATM 2683 O1 BOG A 407 -229.886 43.878 39.921 1.00113.21 O
ANISOU 2683 O1 BOG A 407 14464 13392 15158 91 -928 570 O
HETATM 2684 C2 BOG A 407 -229.798 46.229 39.367 1.00113.73 C
ANISOU 2684 C2 BOG A 407 14510 13341 15362 94 -992 666 C
HETATM 2685 O2 BOG A 407 -231.223 46.320 39.546 1.00112.10 O
ANISOU 2685 O2 BOG A 407 14224 13089 15279 124 -1064 665 O
HETATM 2686 C3 BOG A 407 -229.301 47.220 38.323 1.00110.18 C
ANISOU 2686 C3 BOG A 407 14122 12848 14894 63 -1039 767 C
HETATM 2687 O3 BOG A 407 -229.498 48.542 38.836 1.00101.13 O
ANISOU 2687 O3 BOG A 407 12906 11608 13913 90 -1048 773 O
HETATM 2688 C4 BOG A 407 -227.819 47.001 38.004 1.00103.52 C
ANISOU 2688 C4 BOG A 407 13356 12059 13920 23 -951 767 C
HETATM 2689 O4 BOG A 407 -227.489 47.645 36.767 1.00 98.91 O
ANISOU 2689 O4 BOG A 407 12857 11451 13274 -30 -995 871 O
HETATM 2690 C5 BOG A 407 -227.453 45.531 37.829 1.00108.82 C
ANISOU 2690 C5 BOG A 407 14076 12816 14457 10 -898 720 C
HETATM 2691 O5 BOG A 407 -227.987 44.719 38.873 1.00109.26 O
ANISOU 2691 O5 BOG A 407 14066 12895 14554 48 -878 640 O
HETATM 2692 C6 BOG A 407 -225.938 45.353 37.784 1.00108.00 C
ANISOU 2692 C6 BOG A 407 14004 12752 14280 -13 -789 700 C
HETATM 2693 O6 BOG A 407 -225.398 45.483 39.104 1.00118.07 O
ANISOU 2693 O6 BOG A 407 15197 14032 15631 18 -730 636 O
HETATM 2694 C1' BOG A 407 -229.792 42.558 39.403 1.00104.70 C
ANISOU 2694 C1' BOG A 407 13451 12367 13964 69 -921 561 C
HETATM 2695 C2' BOG A 407 -230.769 41.664 40.150 1.00 97.69 C
ANISOU 2695 C2' BOG A 407 12509 11493 13115 82 -926 507 C
HETATM 2696 C3' BOG A 407 -230.910 40.336 39.423 1.00105.67 C
ANISOU 2696 C3' BOG A 407 13591 12539 14021 52 -941 503 C
HETATM 2697 C4' BOG A 407 -232.108 39.556 39.943 1.00109.17 C
ANISOU 2697 C4' BOG A 407 13980 12984 14514 52 -969 467 C
HETATM 2698 C5' BOG A 407 -232.406 38.391 39.009 1.00113.73 C
ANISOU 2698 C5' BOG A 407 14636 13580 14996 9 -1006 468 C
HETATM 2699 C6' BOG A 407 -233.351 37.386 39.654 1.00109.81 C
ANISOU 2699 C6' BOG A 407 14092 13089 14541 1 -1009 424 C
HETATM 2700 C7' BOG A 407 -234.775 37.923 39.716 1.00102.49 C
ANISOU 2700 C7' BOG A 407 13070 12139 13733 0 -1097 443 C
HETATM 2701 C8' BOG A 407 -235.586 37.160 40.738 1.00 91.37 C
ANISOU 2701 C8' BOG A 407 11588 10736 12391 -4 -1059 388 C
HETATM 2702 C1 BOG A 408 -225.807 51.040 46.074 1.00121.72 C
ANISOU 2702 C1 BOG A 408 15328 14227 16694 -17 -566 222 C
HETATM 2703 O1 BOG A 408 -226.745 52.053 46.422 1.00107.68 O
ANISOU 2703 O1 BOG A 408 13507 12337 15071 0 -542 160 O
HETATM 2704 C2 BOG A 408 -226.421 50.146 44.999 1.00126.02 C
ANISOU 2704 C2 BOG A 408 15886 14796 17198 33 -623 307 C
HETATM 2705 O2 BOG A 408 -227.575 49.481 45.528 1.00116.97 O
ANISOU 2705 O2 BOG A 408 14706 13667 16069 57 -614 252 O
HETATM 2706 C3 BOG A 408 -225.423 49.126 44.475 1.00127.21 C
ANISOU 2706 C3 BOG A 408 16083 15042 17209 20 -631 365 C
HETATM 2707 O3 BOG A 408 -225.994 48.450 43.348 1.00119.20 O
ANISOU 2707 O3 BOG A 408 15098 14036 16155 51 -679 436 O
HETATM 2708 C4 BOG A 408 -224.155 49.860 44.060 1.00133.19 C
ANISOU 2708 C4 BOG A 408 16860 15786 17961 -17 -618 409 C
HETATM 2709 O4 BOG A 408 -223.157 48.935 43.597 1.00130.65 O
ANISOU 2709 O4 BOG A 408 16563 15544 17536 -27 -604 451 O
HETATM 2710 C5 BOG A 408 -223.619 50.671 45.236 1.00120.89 C
ANISOU 2710 C5 BOG A 408 15272 14209 16450 -63 -579 330 C
HETATM 2711 O5 BOG A 408 -224.590 51.642 45.630 1.00120.39 O
ANISOU 2711 O5 BOG A 408 15184 14048 16510 -52 -571 274 O
HETATM 2712 C6 BOG A 408 -222.306 51.369 44.894 1.00101.70 C
ANISOU 2712 C6 BOG A 408 12851 11769 14023 -110 -567 371 C
HETATM 2713 O6 BOG A 408 -222.356 51.896 43.563 1.00 87.95 O
ANISOU 2713 O6 BOG A 408 11142 9966 12307 -97 -589 466 O
HETATM 2714 C1' BOG A 408 -226.288 52.827 47.523 1.00101.50 C
ANISOU 2714 C1' BOG A 408 12719 11529 14316 -59 -476 53 C
HETATM 2715 C2' BOG A 408 -227.224 52.576 48.697 1.00108.77 C
ANISOU 2715 C2' BOG A 408 13611 12461 15254 -72 -404 -77 C
HETATM 2716 C3' BOG A 408 -228.519 51.916 48.241 1.00114.91 C
ANISOU 2716 C3' BOG A 408 14345 13231 16084 -3 -426 -50 C
HETATM 2717 C4' BOG A 408 -229.531 51.895 49.377 1.00126.59 C
ANISOU 2717 C4' BOG A 408 15781 14697 17620 -20 -329 -191 C
HETATM 2718 C5' BOG A 408 -229.040 51.069 50.558 1.00117.80 C
ANISOU 2718 C5' BOG A 408 14721 13713 16326 -106 -278 -262 C
HETATM 2719 C6' BOG A 408 -229.981 51.227 51.744 1.00105.73 C
ANISOU 2719 C6' BOG A 408 13164 12167 14839 -149 -157 -418 C
HETATM 2720 C7' BOG A 408 -229.655 50.203 52.819 1.00101.30 C
ANISOU 2720 C7' BOG A 408 12669 11747 14075 -242 -127 -458 C
HETATM 2721 C8' BOG A 408 -230.370 50.551 54.104 1.00108.69 C
ANISOU 2721 C8' BOG A 408 13605 12672 15021 -322 17 -630 C
HETATM 2722 C1 BOG A 409 -255.102 27.808 47.561 1.00135.52 C
ANISOU 2722 C1 BOG A 409 15245 16293 19954 -1020 -606 -138 C
HETATM 2723 O1 BOG A 409 -254.033 28.704 47.266 1.00123.22 O
ANISOU 2723 O1 BOG A 409 13800 14734 18285 -900 -655 -113 O
HETATM 2724 C2 BOG A 409 -255.055 27.435 49.042 1.00138.27 C
ANISOU 2724 C2 BOG A 409 15633 16673 20232 -1097 -339 -207 C
HETATM 2725 O2 BOG A 409 -253.914 26.607 49.285 1.00140.68 O
ANISOU 2725 O2 BOG A 409 16204 16997 20251 -1127 -324 -169 O
HETATM 2726 C3 BOG A 409 -256.305 26.689 49.488 1.00141.74 C
ANISOU 2726 C3 BOG A 409 15915 17113 20828 -1228 -247 -244 C
HETATM 2727 O3 BOG A 409 -256.305 26.579 50.915 1.00139.00 O
ANISOU 2727 O3 BOG A 409 15594 16799 20421 -1303 21 -313 O
HETATM 2728 C4 BOG A 409 -257.555 27.423 49.023 1.00154.36 C
ANISOU 2728 C4 BOG A 409 17208 18678 22764 -1196 -308 -267 C
HETATM 2729 O4 BOG A 409 -258.722 26.662 49.355 1.00161.55 O
ANISOU 2729 O4 BOG A 409 17961 19589 23833 -1325 -232 -299 O
HETATM 2730 C5 BOG A 409 -257.481 27.628 47.515 1.00150.38 C
ANISOU 2730 C5 BOG A 409 16699 18145 22292 -1126 -610 -178 C
HETATM 2731 O5 BOG A 409 -256.341 28.428 47.203 1.00144.32 O
ANISOU 2731 O5 BOG A 409 16080 17377 21378 -1005 -668 -148 O
HETATM 2732 C6 BOG A 409 -258.746 28.288 46.979 1.00148.62 C
ANISOU 2732 C6 BOG A 409 16165 17883 22420 -1100 -716 -173 C
HETATM 2733 O6 BOG A 409 -259.815 27.335 47.007 1.00149.28 O
ANISOU 2733 O6 BOG A 409 16119 17970 22633 -1234 -718 -183 O
HETATM 2734 C1' BOG A 409 -254.005 29.031 45.880 1.00109.78 C
ANISOU 2734 C1' BOG A 409 12091 13009 16613 -845 -903 -39 C
HETATM 2735 C2' BOG A 409 -252.736 29.817 45.584 1.00 98.65 C
ANISOU 2735 C2' BOG A 409 10836 11600 15045 -737 -940 -8 C
HETATM 2736 C3' BOG A 409 -252.459 29.837 44.089 1.00 83.81 C
ANISOU 2736 C3' BOG A 409 9035 9709 13098 -714 -1192 78 C
HETATM 2737 C4' BOG A 409 -251.109 30.483 43.817 1.00 86.06 C
ANISOU 2737 C4' BOG A 409 9494 10000 13205 -623 -1207 106 C
HETATM 2738 C5' BOG A 409 -250.789 30.414 42.332 1.00 89.66 C
ANISOU 2738 C5' BOG A 409 10056 10454 13559 -625 -1436 186 C
HETATM 2739 C6' BOG A 409 -249.728 31.442 41.969 1.00 87.50 C
ANISOU 2739 C6' BOG A 409 9879 10175 13190 -526 -1465 224 C
HETATM 2740 C7' BOG A 409 -249.685 31.635 40.460 1.00 94.40 C
ANISOU 2740 C7' BOG A 409 10814 11045 14006 -539 -1701 311 C
HETATM 2741 C8' BOG A 409 -248.726 32.737 40.087 1.00 90.03 C
ANISOU 2741 C8' BOG A 409 10341 10483 13381 -449 -1727 357 C
HETATM 2742 C1 BOG A 410 -206.340 53.041 49.522 1.00113.80 C
ANISOU 2742 C1 BOG A 410 13461 13777 16000 -946 -822 548 C
HETATM 2743 O1 BOG A 410 -206.220 51.722 48.988 1.00106.38 O
ANISOU 2743 O1 BOG A 410 12455 12870 15093 -832 -792 611 O
HETATM 2744 C2 BOG A 410 -204.957 53.695 49.533 1.00121.52 C
ANISOU 2744 C2 BOG A 410 14303 14759 17111 -1049 -843 576 C
HETATM 2745 O2 BOG A 410 -204.109 52.984 50.447 1.00127.21 O
ANISOU 2745 O2 BOG A 410 14893 15559 17881 -1087 -985 624 O
HETATM 2746 C3 BOG A 410 -205.025 55.167 49.921 1.00123.88 C
ANISOU 2746 C3 BOG A 410 14673 15001 17393 -1175 -853 505 C
HETATM 2747 O3 BOG A 410 -203.736 55.767 49.736 1.00139.97 O
ANISOU 2747 O3 BOG A 410 16579 17035 19567 -1269 -854 537 O
HETATM 2748 C4 BOG A 410 -206.035 55.876 49.033 1.00124.48 C
ANISOU 2748 C4 BOG A 410 14888 14980 17430 -1126 -728 470 C
HETATM 2749 O4 BOG A 410 -206.149 57.249 49.437 1.00129.94 O
ANISOU 2749 O4 BOG A 410 15647 15597 18129 -1237 -735 399 O
HETATM 2750 C5 BOG A 410 -207.394 55.179 49.118 1.00129.15 C
ANISOU 2750 C5 BOG A 410 15595 15575 17901 -1020 -722 443 C
HETATM 2751 O5 BOG A 410 -207.305 53.790 48.770 1.00120.61 O
ANISOU 2751 O5 BOG A 410 14454 14557 16815 -915 -717 506 O
HETATM 2752 C6 BOG A 410 -208.461 55.864 48.262 1.00118.39 C
ANISOU 2752 C6 BOG A 410 14357 14112 16515 -968 -623 421 C
HETATM 2753 O6 BOG A 410 -209.745 55.458 48.756 1.00 98.51 O
ANISOU 2753 O6 BOG A 410 11937 11595 13896 -907 -645 367 O
HETATM 2754 C1' BOG A 410 -207.380 50.925 49.223 1.00 91.17 C
ANISOU 2754 C1' BOG A 410 10633 10957 13051 -752 -807 593 C
HETATM 2755 C2' BOG A 410 -207.018 49.490 48.868 1.00 79.26 C
ANISOU 2755 C2' BOG A 410 9031 9480 11603 -651 -799 660 C
HETATM 2756 C3' BOG A 410 -208.176 48.548 49.152 1.00 83.79 C
ANISOU 2756 C3' BOG A 410 9706 10067 12063 -574 -823 649 C
HETATM 2757 C4' BOG A 410 -207.825 47.115 48.761 1.00 79.49 C
ANISOU 2757 C4' BOG A 410 9073 9533 11595 -473 -807 710 C
HETATM 2758 C5' BOG A 410 -208.782 46.164 49.469 1.00 80.94 C
ANISOU 2758 C5' BOG A 410 9337 9741 11675 -432 -881 713 C
HETATM 2759 C6' BOG A 410 -208.612 44.702 49.064 1.00 79.23 C
ANISOU 2759 C6' BOG A 410 9055 9513 11534 -325 -860 767 C
HETATM 2760 C7' BOG A 410 -209.708 43.851 49.705 1.00 82.50 C
ANISOU 2760 C7' BOG A 410 9571 9943 11832 -295 -922 767 C
HETATM 2761 C8' BOG A 410 -209.838 42.486 49.061 1.00 87.72 C
ANISOU 2761 C8' BOG A 410 10207 10569 12554 -182 -866 797 C
HETATM 2762 C10 DNK A 411 -234.265 48.641 35.254 1.00117.19 C
ANISOU 2762 C10 DNK A 411 14894 13494 16140 59 -1694 1178 C
HETATM 2763 C11 DNK A 411 -233.601 47.683 36.257 1.00104.34 C
ANISOU 2763 C11 DNK A 411 13270 11954 14421 75 -1515 1019 C
HETATM 2764 C13 DNK A 411 -232.815 45.317 36.115 1.00111.96 C
ANISOU 2764 C13 DNK A 411 14375 13102 15061 11 -1394 902 C
HETATM 2765 C15 DNK A 411 -231.700 43.007 36.052 1.00100.23 C
ANISOU 2765 C15 DNK A 411 13027 11760 13297 -40 -1235 774 C
HETATM 2766 C16 DNK A 411 -231.981 41.499 36.073 1.00 99.02 C
ANISOU 2766 C16 DNK A 411 12904 11659 13062 -59 -1209 705 C
HETATM 2767 C17 DNK A 411 -230.668 43.318 34.954 1.00 92.77 C
ANISOU 2767 C17 DNK A 411 12210 10833 12205 -101 -1214 830 C
HETATM 2768 C18 DNK A 411 -234.148 43.289 36.707 1.00 88.01 C
ANISOU 2768 C18 DNK A 411 11279 10140 12020 13 -1397 789 C
HETATM 2769 C19 DNK A 411 -235.256 42.641 36.143 1.00 93.82 C
ANISOU 2769 C19 DNK A 411 12006 10887 12756 -21 -1514 817 C
HETATM 2770 C20 DNK A 411 -236.297 42.193 36.951 1.00 88.97 C
ANISOU 2770 C20 DNK A 411 11269 10264 12273 9 -1513 759 C
HETATM 2771 C21 DNK A 411 -236.253 42.388 38.324 1.00 82.96 C
ANISOU 2771 C21 DNK A 411 10408 9485 11626 68 -1390 671 C
HETATM 2772 C22 DNK A 411 -235.159 43.037 38.883 1.00 90.63 C
ANISOU 2772 C22 DNK A 411 11403 10450 12583 96 -1285 643 C
HETATM 2773 C23 DNK A 411 -234.114 43.493 38.083 1.00 81.16 C
ANISOU 2773 C23 DNK A 411 10311 9255 11272 72 -1292 704 C
HETATM 2774 C25 DNK A 411 -235.242 45.925 35.511 1.00104.34 C
ANISOU 2774 C25 DNK A 411 13265 12034 14345 28 -1671 1032 C
HETATM 2775 C26 DNK A 411 -235.741 46.832 34.402 1.00110.44 C
ANISOU 2775 C26 DNK A 411 14055 12741 15166 -4 -1858 1195 C
HETATM 2776 C1 DNK A 411 -238.450 50.437 34.522 1.00107.11 C
ANISOU 2776 C1 DNK A 411 13196 11890 15609 178 -2221 1470 C
HETATM 2777 C2 DNK A 411 -237.481 49.541 34.902 1.00109.65 C
ANISOU 2777 C2 DNK A 411 13633 12338 15692 144 -2052 1346 C
HETATM 2778 C3 DNK A 411 -237.477 48.907 36.166 1.00102.15 C
ANISOU 2778 C3 DNK A 411 12609 11431 14773 190 -1874 1167 C
HETATM 2779 C4 DNK A 411 -238.437 49.138 37.101 1.00102.84 C
ANISOU 2779 C4 DNK A 411 12514 11447 15113 264 -1835 1089 C
HETATM 2780 C5 DNK A 411 -239.425 50.043 36.713 1.00105.18 C
ANISOU 2780 C5 DNK A 411 12682 11613 15669 306 -1985 1196 C
HETATM 2781 C6 DNK A 411 -239.436 50.680 35.482 1.00101.65 C
ANISOU 2781 C6 DNK A 411 12296 11113 15212 271 -2181 1387 C
HETATM 2782 O7 DNK A 411 -236.403 48.086 36.264 1.00103.31 O
ANISOU 2782 O7 DNK A 411 12889 11691 14673 145 -1753 1094 O
HETATM 2783 C8 DNK A 411 -235.714 48.195 35.025 1.00113.88 C
ANISOU 2783 C8 DNK A 411 14386 13062 15822 68 -1834 1211 C
HETATM 2784 O9 DNK A 411 -236.403 49.116 34.185 1.00112.51 O
ANISOU 2784 O9 DNK A 411 14185 12795 15771 60 -2024 1373 O
HETATM 2785 N12 DNK A 411 -233.860 46.250 35.951 1.00107.06 N
ANISOU 2785 N12 DNK A 411 13668 12395 14616 36 -1522 981 N
HETATM 2786 C14 DNK A 411 -233.022 43.802 35.821 1.00 95.35 C
ANISOU 2786 C14 DNK A 411 12331 11078 12818 -28 -1387 852 C
HETATM 2787 O24 DNK A 411 -231.727 45.759 36.498 1.00118.71 O
ANISOU 2787 O24 DNK A 411 15252 13958 15896 20 -1291 875 O
HETATM 2788 O HOH A1000 -221.653 70.510 46.184 1.00 74.74 O
HETATM 2789 O HOH A1001 -213.585 60.638 34.935 1.00 71.59 O
HETATM 2790 O HOH A1002 -213.863 53.324 51.827 1.00 59.24 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 2783
CONECT 2763 2762 2785
CONECT 2764 2785 2786 2787
CONECT 2765 2766 2767 2786
CONECT 2766 2765
CONECT 2767 2765
CONECT 2768 2769 2773 2786
CONECT 2769 2768 2770
CONECT 2770 2769 2771
CONECT 2771 2770 2772
CONECT 2772 2771 2773
CONECT 2773 2768 2772
CONECT 2774 2775 2785
CONECT 2775 2774 2783
CONECT 2776 2777 2781
CONECT 2777 2776 2778 2784
CONECT 2778 2777 2779 2782
CONECT 2779 2778 2780
CONECT 2780 2779 2781
CONECT 2781 2776 2780
CONECT 2782 2778 2783
CONECT 2783 2762 2775 2782 2784
CONECT 2784 2777 2783
CONECT 2785 2763 2764 2774
CONECT 2786 2764 2765 2768
CONECT 2787 2764
MASTER 338 0 12 14 4 0 0 6 2778 1 194 27
END