HEADER SIGNALING PROTEIN 07-JUN-17 5XR8
TITLE CRYSTAL STRUCTURE OF THE HUMAN CB1 IN COMPLEX WITH AGONIST AM841
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CANNABINOID RECEPTOR 1,FLAVODOXIN,CANNABINOID RECEPTOR 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 99-306,UNP RESIDUES 3-148,UNP RESIDUES 332-
COMPND 5 414,UNP RESIDUES 99-306,UNP RESIDUES 3-148,UNP RESIDUES 332-414,UNP
COMPND 6 RESIDUES 99-306,UNP RESIDUES 3-148,UNP RESIDUES 332-414;
COMPND 7 SYNONYM: CB1,CANN6,CB1,CANN6;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, DESULFOVIBRIO VULGARIS (STRAIN
SOURCE 3 HILDENBOROUGH / ATCC 29579 / DSM 644 / NCIMB 8303);
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606, 882;
SOURCE 6 STRAIN: HILDENBOROUGH / ATCC 29579 / DSM 644 / NCIMB 8303;
SOURCE 7 GENE: CNR1, CNR, DVU_2680;
SOURCE 8 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 10 EXPRESSION_SYSTEM_CELL_LINE: HEK293F
KEYWDS MEMBRANE PROTEIN, HUMAN G PROTEIN-COUPLED RECEPTOR, STABILIZING
KEYWDS 2 AGONISTS, LIPIDIC CUBIC PHASE, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.HUA,K.VEMURI,P.S.NIKAS,R.B.LAPRAIRIE,Y.WU,L.QU,M.PU,A.KORDE,J.SHAN,
AUTHOR 2 J.H.HO,G.W.HAN,K.DING,X.LI,H.LIU,M.A.HANSON,S.ZHAO,L.M.BOHN,
AUTHOR 3 A.MAKRIYANNIS,R.C.STEVENS,Z.J.LIU
REVDAT 7 22-JAN-20 5XR8 1 COMPND SOURCE JRNL REMARK
REVDAT 7 2 1 DBREF SEQADV HETNAM FORMUL
REVDAT 7 3 1 HELIX SHEET ATOM
REVDAT 6 08-NOV-17 5XR8 1 SOURCE
REVDAT 5 18-OCT-17 5XR8 1 REMARK
REVDAT 4 16-AUG-17 5XR8 1 REMARK
REVDAT 3 09-AUG-17 5XR8 1 JRNL
REVDAT 2 19-JUL-17 5XR8 1 JRNL
REVDAT 1 12-JUL-17 5XR8 0
JRNL AUTH T.HUA,K.VEMURI,S.P.NIKAS,R.B.LAPRAIRIE,Y.WU,L.QU,M.PU,
JRNL AUTH 2 A.KORDE,S.JIANG,J.H.HO,G.W.HAN,K.DING,X.LI,H.LIU,M.A.HANSON,
JRNL AUTH 3 S.ZHAO,L.M.BOHN,A.MAKRIYANNIS,R.C.STEVENS,Z.J.LIU
JRNL TITL CRYSTAL STRUCTURES OF AGONIST-BOUND HUMAN CANNABINOID
JRNL TITL 2 RECEPTOR CB1.
JRNL REF NATURE V. 547 468 2017
JRNL REFN ESSN 1476-4687
JRNL PMID 28678776
JRNL DOI 10.1038/NATURE23272
REMARK 2
REMARK 2 RESOLUTION. 2.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 3 NUMBER OF REFLECTIONS : 13329
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.256
REMARK 3 R VALUE (WORKING SET) : 0.255
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.640
REMARK 3 FREE R VALUE TEST SET COUNT : 618
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 49.4866 - 4.6819 0.96 3613 177 0.2249 0.2420
REMARK 3 2 4.6819 - 3.7165 0.92 3282 155 0.2665 0.2671
REMARK 3 3 3.7165 - 3.2468 0.86 3046 159 0.3197 0.3998
REMARK 3 4 3.2468 - 2.9500 0.78 2770 127 0.3858 0.4094
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.480
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 43.260
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 : 0.002 3491
REMARK 3 ANGLE : 0.484 4764
REMARK 3 CHIRALITY : 0.036 561
REMARK 3 PLANARITY : 0.003 600
REMARK 3 DIHEDRAL : 15.503 2016
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 102 THROUGH 306 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.5828-149.0927 305.7149
REMARK 3 T TENSOR
REMARK 3 T11: 0.4816 T22: 0.3626
REMARK 3 T33: 0.7640 T12: 0.0670
REMARK 3 T13: -0.0421 T23: -0.0210
REMARK 3 L TENSOR
REMARK 3 L11: 5.2421 L22: 1.1492
REMARK 3 L33: 2.9624 L12: 1.0127
REMARK 3 L13: 0.3310 L23: 0.3575
REMARK 3 S TENSOR
REMARK 3 S11: 0.2469 S12: 0.3485 S13: 0.0282
REMARK 3 S21: 0.0083 S22: 0.1019 S23: 0.3089
REMARK 3 S31: 0.1342 S32: -0.2645 S33: -0.3070
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 307 THROUGH 335 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.983 -118.941 259.680
REMARK 3 T TENSOR
REMARK 3 T11: 0.8387 T22: 0.6905
REMARK 3 T33: 1.5988 T12: -0.0400
REMARK 3 T13: 0.0550 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 8.3074 L22: 7.2240
REMARK 3 L33: 5.4565 L12: -4.1474
REMARK 3 L13: 2.7337 L23: -4.6072
REMARK 3 S TENSOR
REMARK 3 S11: -0.4097 S12: -0.1339 S13: 0.3508
REMARK 3 S21: 1.0589 S22: 0.0256 S23: -0.4847
REMARK 3 S31: -0.4268 S32: -0.1613 S33: 0.4333
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 336 THROUGH 536 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.886 -126.754 276.328
REMARK 3 T TENSOR
REMARK 3 T11: 0.7203 T22: 0.6250
REMARK 3 T33: 0.8890 T12: -0.0255
REMARK 3 T13: 0.1857 T23: -0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 2.7720 L22: 2.1089
REMARK 3 L33: 4.3409 L12: 0.5375
REMARK 3 L13: 1.3216 L23: 2.9628
REMARK 3 S TENSOR
REMARK 3 S11: -0.2097 S12: 0.0659 S13: 0.2704
REMARK 3 S21: 0.3455 S22: -0.1191 S23: 1.0514
REMARK 3 S31: -0.6220 S32: 0.1866 S33: 0.3059
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THERE ARE SOME UNKNOWN DENSITIES LOCATED
REMARK 3 AT THE END OF THE SIDE CHAIN OF SER152, WHICH MIGHT BE
REMARK 3 PHOSPHORYLATION
REMARK 3 BUT NOT CHEMICALLY CONFIRMED YET. THEY HAVE NOT BEEN MODELLED; DUE
REMARK 3 TO LACK OF DENSITIES, LAST TWO C AND S ATOMS IN THE TAIL OF THE
REMARK 3 LIGAND 8D0 HAS BEEN DELETED DURING THE FINAL REFINEMENT.
REMARK 4
REMARK 4 5XR8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1300004013.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13367
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.950
REMARK 200 RESOLUTION RANGE LOW (A) : 49.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.2
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.0600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.970
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5TGZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE TRIHYDRATE PH
REMARK 280 6.2, 120 MM C6H5NA3O7, 30% PEG400 AND 100 MM GLYCINE, LIPIDIC
REMARK 280 CUBIC PHASE, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,-Y,-Z+1/2
REMARK 290 4555 -X+1/2,-Y,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 33.41500
REMARK 290 SMTRY2 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.82000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 33.41500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 69.82000
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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 99
REMARK 465 GLU A 100
REMARK 465 ASN A 101
REMARK 465 PRO A 454
REMARK 465 ASP A 455
REMARK 465 GLN A 456
REMARK 465 ALA A 457
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PHE A 102 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 148 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 183 CG CD CE NZ
REMARK 470 LYS A 308 CG CD CE NZ
REMARK 470 LEU A 379 CG CD1 CD2
REMARK 470 GLU A 385 CG CD OE1 OE2
REMARK 470 LYS A 392 CG CD CE NZ
REMARK 470 ARG A 450 CZ NH1 NH2
REMARK 470 ILE A 453 CG1 CG2 CD1
REMARK 470 ARG A 458 CG CD NE CZ NH1 NH2
REMARK 470 MET A 459 CG SD CE
REMARK 470 ARG A 522 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 524 CD CE NZ
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 SG CYS A 257 SG CYS A 264 1.34
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 261 97.33 -64.29
REMARK 500 SER A 315 80.52 56.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 8D0 A 1202
DBREF 5XR8 A 99 306 UNP P21554 CNR1_HUMAN 99 306
DBREF 5XR8 A 308 453 UNP P00323 FLAV_DESVH 3 148
DBREF 5XR8 A 356 536 UNP P21554 CNR1_HUMAN 332 414
SEQADV 5XR8 ALA A 210 UNP P21554 THR 210 ENGINEERED MUTATION
SEQADV 5XR8 LYS A 273 UNP P21554 GLU 273 ENGINEERED MUTATION
SEQADV 5XR8 VAL A 283 UNP P21554 THR 283 ENGINEERED MUTATION
SEQADV 5XR8 ALA A 307 UNP P21554 LINKER
SEQADV 5XR8 TRP A 403 UNP P00323 TYR 98 ENGINEERED MUTATION
SEQADV 5XR8 GLU A 462 UNP P21554 ARG 340 ENGINEERED MUTATION
SEQRES 1 A 438 GLY GLU ASN PHE MET ASP ILE GLU CYS PHE MET VAL LEU
SEQRES 2 A 438 ASN PRO SER GLN GLN LEU ALA ILE ALA VAL LEU SER LEU
SEQRES 3 A 438 THR LEU GLY THR PHE THR VAL LEU GLU ASN LEU LEU VAL
SEQRES 4 A 438 LEU CYS VAL ILE LEU HIS SER ARG SER LEU ARG CYS ARG
SEQRES 5 A 438 PRO SER TYR HIS PHE ILE GLY SER LEU ALA VAL ALA ASP
SEQRES 6 A 438 LEU LEU GLY SER VAL ILE PHE VAL TYR SER PHE ILE ASP
SEQRES 7 A 438 PHE HIS VAL PHE HIS ARG LYS ASP SER ARG ASN VAL PHE
SEQRES 8 A 438 LEU PHE LYS LEU GLY GLY VAL THR ALA SER PHE THR ALA
SEQRES 9 A 438 SER VAL GLY SER LEU PHE LEU ALA ALA ILE ASP ARG TYR
SEQRES 10 A 438 ILE SER ILE HIS ARG PRO LEU ALA TYR LYS ARG ILE VAL
SEQRES 11 A 438 THR ARG PRO LYS ALA VAL VAL ALA PHE CYS LEU MET TRP
SEQRES 12 A 438 THR ILE ALA ILE VAL ILE ALA VAL LEU PRO LEU LEU GLY
SEQRES 13 A 438 TRP ASN CYS GLU LYS LEU GLN SER VAL CYS SER ASP ILE
SEQRES 14 A 438 PHE PRO HIS ILE ASP LYS THR TYR LEU MET PHE TRP ILE
SEQRES 15 A 438 GLY VAL VAL SER VAL LEU LEU LEU PHE ILE VAL TYR ALA
SEQRES 16 A 438 TYR MET TYR ILE LEU TRP LYS ALA HIS SER HIS ALA VAL
SEQRES 17 A 438 ALA LYS ALA LEU ILE VAL TYR GLY SER THR THR GLY ASN
SEQRES 18 A 438 THR GLU TYR THR ALA GLU THR ILE ALA ARG GLU LEU ALA
SEQRES 19 A 438 ASP ALA GLY TYR GLU VAL ASP SER ARG ASP ALA ALA SER
SEQRES 20 A 438 VAL GLU ALA GLY GLY LEU PHE GLU GLY PHE ASP LEU VAL
SEQRES 21 A 438 LEU LEU GLY CYS SER THR TRP GLY ASP ASP SER ILE GLU
SEQRES 22 A 438 LEU GLN ASP ASP PHE ILE PRO LEU PHE ASP SER LEU GLU
SEQRES 23 A 438 GLU THR GLY ALA GLN GLY ARG LYS VAL ALA CYS PHE GLY
SEQRES 24 A 438 CYS GLY ASP SER SER TRP GLU TYR PHE CYS GLY ALA VAL
SEQRES 25 A 438 ASP ALA ILE GLU GLU LYS LEU LYS ASN LEU GLY ALA GLU
SEQRES 26 A 438 ILE VAL GLN ASP GLY LEU ARG ILE ASP GLY ASP PRO ARG
SEQRES 27 A 438 ALA ALA ARG ASP ASP ILE VAL GLY TRP ALA HIS ASP VAL
SEQRES 28 A 438 ARG GLY ALA ILE PRO ASP GLN ALA ARG MET ASP ILE GLU
SEQRES 29 A 438 LEU ALA LYS THR LEU VAL LEU ILE LEU VAL VAL LEU ILE
SEQRES 30 A 438 ILE CYS TRP GLY PRO LEU LEU ALA ILE MET VAL TYR ASP
SEQRES 31 A 438 VAL PHE GLY LYS MET ASN LYS LEU ILE LYS THR VAL PHE
SEQRES 32 A 438 ALA PHE CYS SER MET LEU CYS LEU LEU ASN SER THR VAL
SEQRES 33 A 438 ASN PRO ILE ILE TYR ALA LEU ARG SER LYS ASP LEU ARG
SEQRES 34 A 438 HIS ALA PHE ARG SER MET PHE PRO SER
HET FMN A1201 31
HET 8D0 A1202 29
HET CLR A1203 28
HET PEG A1204 7
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM 8D0 (6~{A}~{R},9~{R},10~{A}~{R})-9-(HYDROXYMETHYL)-3-(8-
HETNAM 2 8D0 ISOTHIOCYANATO-2-METHYL-OCTAN-2-YL)-6,6-DIMETHYL-
HETNAM 3 8D0 6~{A},7,8,9,10,10~{A}-HEXAHYDROBENZO[C]CHROMEN-1-OL
HETNAM CLR CHOLESTEROL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 2 FMN C17 H21 N4 O9 P
FORMUL 3 8D0 C26 H39 N O3 S
FORMUL 4 CLR C27 H46 O
FORMUL 5 PEG C4 H10 O3
FORMUL 6 HOH *(H2 O)
HELIX 1 AA1 ILE A 105 MET A 109 5 5
HELIX 2 AA2 ASN A 112 SER A 146 1 35
HELIX 3 AA3 TYR A 153 VAL A 179 1 27
HELIX 4 AA4 SER A 185 ARG A 220 1 36
HELIX 5 AA5 ALA A 223 VAL A 228 1 6
HELIX 6 AA6 THR A 229 GLY A 254 1 26
HELIX 7 AA7 ASP A 272 VAL A 306 1 35
HELIX 8 AA8 GLY A 318 GLY A 335 1 18
HELIX 9 AA9 ASP A 375 SER A 382 1 8
HELIX 10 AB1 LEU A 383 THR A 386 5 4
HELIX 11 AB2 CYS A 407 GLY A 421 1 15
HELIX 12 AB3 ALA A 438 ALA A 452 1 15
HELIX 13 AB4 ASP A 460 PHE A 490 1 31
HELIX 14 AB5 ASN A 494 TYR A 519 1 26
HELIX 15 AB6 SER A 523 MET A 533 1 11
SHEET 1 AA1 5 TYR A 336 ASP A 342 0
SHEET 2 AA1 5 ALA A 307 TYR A 313 1 N ALA A 309 O GLU A 337
SHEET 3 AA1 5 LEU A 357 GLY A 361 1 O LEU A 359 N LEU A 310
SHEET 4 AA1 5 VAL A 393 GLY A 399 1 O ALA A 394 N LEU A 360
SHEET 5 AA1 5 LEU A 429 ASP A 432 1 O ILE A 431 N GLY A 399
CRYST1 66.830 73.610 139.640 90.00 90.00 90.00 P 21 2 21 4
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 0.014963 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013585 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007161 0.00000
ATOM 1 N PHE A 102 -50.192-176.431 309.191 1.00178.23 N
ANISOU 1 N PHE A 102 23409 15777 28535 -1484 -3374 -23 N
ATOM 2 CA PHE A 102 -49.299-176.942 310.225 1.00178.03 C
ANISOU 2 CA PHE A 102 23472 15546 28628 -1364 -3467 280 C
ATOM 3 C PHE A 102 -47.847-176.901 309.761 1.00175.25 C
ANISOU 3 C PHE A 102 23106 15157 28325 -987 -3490 6 C
ATOM 4 O PHE A 102 -47.346-177.856 309.166 1.00174.37 O
ANISOU 4 O PHE A 102 23010 14771 28473 -863 -3575 -244 O
ATOM 5 CB PHE A 102 -49.690-178.368 310.616 1.00184.96 C
ANISOU 5 CB PHE A 102 24437 16023 29817 -1546 -3600 463 C
ATOM 6 N MET A 103 -47.177-175.786 310.039 1.00171.05 N
ANISOU 6 N MET A 103 22536 14911 27546 -814 -3409 46 N
ATOM 7 CA MET A 103 -45.788-175.573 309.660 1.00174.03 C
ANISOU 7 CA MET A 103 22880 15329 27916 -473 -3410 -195 C
ATOM 8 C MET A 103 -44.954-175.342 310.912 1.00171.97 C
ANISOU 8 C MET A 103 22660 15089 27593 -371 -3450 168 C
ATOM 9 O MET A 103 -45.419-174.718 311.871 1.00170.90 O
ANISOU 9 O MET A 103 22545 15114 27274 -529 -3407 523 O
ATOM 10 CB MET A 103 -45.650-174.373 308.713 1.00173.09 C
ANISOU 10 CB MET A 103 22661 15566 27540 -350 -3270 -529 C
ATOM 11 CG MET A 103 -46.721-174.294 307.630 1.00175.71 C
ANISOU 11 CG MET A 103 22934 15983 27845 -514 -3218 -807 C
ATOM 12 SD MET A 103 -46.321-175.206 306.126 1.00182.82 S
ANISOU 12 SD MET A 103 23776 16737 28949 -377 -3269 -1363 S
ATOM 13 CE MET A 103 -44.978-174.217 305.474 1.00178.10 C
ANISOU 13 CE MET A 103 23079 16454 28138 -36 -3181 -1662 C
ATOM 14 N ASP A 104 -43.723-175.847 310.902 1.00168.99 N
ANISOU 14 N ASP A 104 22281 14562 27365 -116 -3534 73 N
ATOM 15 CA ASP A 104 -42.828-175.639 312.032 1.00166.66 C
ANISOU 15 CA ASP A 104 22010 14302 27012 -2 -3586 391 C
ATOM 16 C ASP A 104 -42.342-174.195 312.060 1.00161.22 C
ANISOU 16 C ASP A 104 21260 14004 25992 119 -3448 325 C
ATOM 17 O ASP A 104 -42.032-173.607 311.020 1.00160.39 O
ANISOU 17 O ASP A 104 21080 14077 25783 263 -3350 -62 O
ATOM 18 CB ASP A 104 -41.638-176.596 311.953 1.00170.36 C
ANISOU 18 CB ASP A 104 22475 14501 27753 246 -3720 287 C
ATOM 19 CG ASP A 104 -40.809-176.600 313.222 1.00171.78 C
ANISOU 19 CG ASP A 104 22682 14669 27917 329 -3812 675 C
ATOM 20 OD1 ASP A 104 -41.402-176.594 314.321 1.00174.72 O
ANISOU 20 OD1 ASP A 104 23116 15049 28223 112 -3849 1124 O
ATOM 21 OD2 ASP A 104 -39.564-176.608 313.121 1.00170.27 O
ANISOU 21 OD2 ASP A 104 22440 14486 27769 602 -3850 533 O
ATOM 22 N ILE A 105 -42.281-173.620 313.263 1.00156.77 N
ANISOU 22 N ILE A 105 20725 13581 25260 47 -3441 710 N
ATOM 23 CA ILE A 105 -41.838-172.234 313.395 1.00148.86 C
ANISOU 23 CA ILE A 105 19673 12925 23961 146 -3311 668 C
ATOM 24 C ILE A 105 -40.358-172.111 313.053 1.00149.05 C
ANISOU 24 C ILE A 105 19641 12997 23994 467 -3327 428 C
ATOM 25 O ILE A 105 -39.940-171.162 312.380 1.00151.09 O
ANISOU 25 O ILE A 105 19831 13503 24073 602 -3203 145 O
ATOM 26 CB ILE A 105 -42.144-171.704 314.809 1.00140.88 C
ANISOU 26 CB ILE A 105 18701 12052 22776 -27 -3307 1138 C
ATOM 27 CG1 ILE A 105 -43.655-171.659 315.049 1.00135.76 C
ANISOU 27 CG1 ILE A 105 18077 11431 22076 -359 -3258 1337 C
ATOM 28 CG2 ILE A 105 -41.535-170.323 315.010 1.00134.21 C
ANISOU 28 CG2 ILE A 105 17810 11526 21660 98 -3187 1086 C
ATOM 29 CD1 ILE A 105 -44.044-171.099 316.402 1.00132.30 C
ANISOU 29 CD1 ILE A 105 17655 11179 21436 -565 -3236 1788 C
ATOM 30 N GLU A 106 -39.544-173.073 313.497 1.00146.61 N
ANISOU 30 N GLU A 106 19350 12455 23899 588 -3480 540 N
ATOM 31 CA GLU A 106 -38.116-173.029 313.206 1.00142.87 C
ANISOU 31 CA GLU A 106 18805 12026 23451 891 -3505 318 C
ATOM 32 C GLU A 106 -37.818-173.267 311.731 1.00139.69 C
ANISOU 32 C GLU A 106 18328 11608 23141 1043 -3459 -195 C
ATOM 33 O GLU A 106 -36.705-172.972 311.282 1.00136.64 O
ANISOU 33 O GLU A 106 17854 11356 22708 1278 -3433 -449 O
ATOM 34 CB GLU A 106 -37.371-174.051 314.067 1.00150.08 C
ANISOU 34 CB GLU A 106 19747 12679 24596 981 -3694 587 C
ATOM 35 CG GLU A 106 -37.611-173.874 315.557 1.00155.76 C
ANISOU 35 CG GLU A 106 20528 13449 25207 819 -3758 1124 C
ATOM 36 CD GLU A 106 -36.491-174.440 316.408 1.00164.75 C
ANISOU 36 CD GLU A 106 21652 14476 26467 986 -3922 1366 C
ATOM 37 OE1 GLU A 106 -35.672-175.222 315.880 1.00168.93 O
ANISOU 37 OE1 GLU A 106 22144 14799 27244 1206 -4007 1147 O
ATOM 38 OE2 GLU A 106 -36.425-174.094 317.606 1.00167.25 O
ANISOU 38 OE2 GLU A 106 21988 14931 26629 895 -3969 1778 O
ATOM 39 N CYS A 107 -38.784-173.791 310.971 1.00142.64 N
ANISOU 39 N CYS A 107 18720 11843 23632 905 -3450 -353 N
ATOM 40 CA CYS A 107 -38.604-173.918 309.529 1.00144.14 C
ANISOU 40 CA CYS A 107 18825 12075 23867 1020 -3398 -847 C
ATOM 41 C CYS A 107 -38.508-172.553 308.858 1.00130.85 C
ANISOU 41 C CYS A 107 17062 10796 21861 1068 -3226 -1076 C
ATOM 42 O CYS A 107 -37.878-172.423 307.803 1.00125.52 O
ANISOU 42 O CYS A 107 16284 10256 21152 1230 -3178 -1467 O
ATOM 43 CB CYS A 107 -39.752-174.732 308.928 1.00154.49 C
ANISOU 43 CB CYS A 107 20173 13164 25360 832 -3431 -947 C
ATOM 44 SG CYS A 107 -39.647-174.993 307.142 1.00160.84 S
ANISOU 44 SG CYS A 107 20864 14025 26223 940 -3383 -1561 S
ATOM 45 N PHE A 108 -39.122-171.531 309.452 1.00127.19 N
ANISOU 45 N PHE A 108 16634 10530 21162 926 -3131 -837 N
ATOM 46 CA PHE A 108 -39.026-170.166 308.950 1.00120.61 C
ANISOU 46 CA PHE A 108 15734 10057 20035 970 -2969 -1002 C
ATOM 47 C PHE A 108 -37.778-169.443 309.437 1.00118.06 C
ANISOU 47 C PHE A 108 15369 9921 19566 1159 -2935 -971 C
ATOM 48 O PHE A 108 -37.580-168.276 309.082 1.00111.71 O
ANISOU 48 O PHE A 108 14509 9409 18525 1203 -2799 -1096 O
ATOM 49 CB PHE A 108 -40.265-169.365 309.361 1.00110.86 C
ANISOU 49 CB PHE A 108 14548 8933 18642 739 -2880 -776 C
ATOM 50 CG PHE A 108 -41.536-169.841 308.725 1.00107.39 C
ANISOU 50 CG PHE A 108 14121 8385 18298 544 -2890 -854 C
ATOM 51 CD1 PHE A 108 -42.321-170.801 309.342 1.00110.03 C
ANISOU 51 CD1 PHE A 108 14536 8449 18822 353 -2994 -601 C
ATOM 52 CD2 PHE A 108 -41.951-169.324 307.511 1.00107.37 C
ANISOU 52 CD2 PHE A 108 14041 8562 18191 539 -2801 -1172 C
ATOM 53 CE1 PHE A 108 -43.495-171.238 308.757 1.00113.39 C
ANISOU 53 CE1 PHE A 108 14965 8784 19336 157 -3003 -683 C
ATOM 54 CE2 PHE A 108 -43.122-169.755 306.923 1.00110.83 C
ANISOU 54 CE2 PHE A 108 14479 8917 18716 352 -2821 -1254 C
ATOM 55 CZ PHE A 108 -43.896-170.714 307.545 1.00113.79 C
ANISOU 55 CZ PHE A 108 14933 9019 19283 158 -2919 -1018 C
ATOM 56 N MET A 109 -36.939-170.101 310.232 1.00123.59 N
ANISOU 56 N MET A 109 16089 10461 20410 1267 -3059 -805 N
ATOM 57 CA MET A 109 -35.772-169.484 310.857 1.00118.55 C
ANISOU 57 CA MET A 109 15410 9988 19648 1432 -3052 -733 C
ATOM 58 C MET A 109 -34.512-170.015 310.175 1.00126.98 C
ANISOU 58 C MET A 109 16374 11039 20832 1682 -3104 -1047 C
ATOM 59 O MET A 109 -33.933-171.018 310.598 1.00136.47 O
ANISOU 59 O MET A 109 17583 12004 22266 1783 -3253 -958 O
ATOM 60 CB MET A 109 -35.754-169.766 312.357 1.00114.59 C
ANISOU 60 CB MET A 109 14988 9352 19200 1363 -3168 -274 C
ATOM 61 CG MET A 109 -36.867-169.093 313.145 1.00108.91 C
ANISOU 61 CG MET A 109 14345 8710 18324 1118 -3107 44 C
ATOM 62 SD MET A 109 -36.738-169.445 314.911 1.00111.11 S
ANISOU 62 SD MET A 109 14695 8891 18632 1028 -3260 601 S
ATOM 63 CE MET A 109 -38.188-168.600 315.537 1.00112.34 C
ANISOU 63 CE MET A 109 14913 9182 18588 713 -3153 881 C
ATOM 64 N VAL A 110 -34.090-169.334 309.114 1.00125.16 N
ANISOU 64 N VAL A 110 16039 11071 20444 1779 -2983 -1407 N
ATOM 65 CA VAL A 110 -32.837-169.630 308.427 1.00131.82 C
ANISOU 65 CA VAL A 110 16756 11987 21344 2010 -3006 -1731 C
ATOM 66 C VAL A 110 -31.800-168.670 308.999 1.00134.52 C
ANISOU 66 C VAL A 110 17039 12584 21488 2131 -2956 -1667 C
ATOM 67 O VAL A 110 -31.740-167.498 308.615 1.00141.91 O
ANISOU 67 O VAL A 110 17926 13826 22168 2114 -2807 -1784 O
ATOM 68 CB VAL A 110 -32.972-169.488 306.910 1.00131.84 C
ANISOU 68 CB VAL A 110 16659 12157 21278 2026 -2913 -2160 C
ATOM 69 CG1 VAL A 110 -31.631-169.729 306.240 1.00133.63 C
ANISOU 69 CG1 VAL A 110 16733 12503 21537 2257 -2929 -2497 C
ATOM 70 CG2 VAL A 110 -34.021-170.456 306.379 1.00135.25 C
ANISOU 70 CG2 VAL A 110 17142 12334 21914 1901 -2973 -2233 C
ATOM 71 N LEU A 111 -30.982-169.161 309.930 1.00130.13 N
ANISOU 71 N LEU A 111 16483 11903 21059 2253 -3085 -1474 N
ATOM 72 CA LEU A 111 -30.198-168.285 310.802 1.00123.90 C
ANISOU 72 CA LEU A 111 15659 11323 20094 2328 -3066 -1312 C
ATOM 73 C LEU A 111 -28.781-168.825 310.957 1.00126.35 C
ANISOU 73 C LEU A 111 15857 11621 20528 2575 -3178 -1399 C
ATOM 74 O LEU A 111 -28.552-169.772 311.713 1.00137.08 O
ANISOU 74 O LEU A 111 17252 12722 22109 2634 -3344 -1166 O
ATOM 75 CB LEU A 111 -30.877-168.148 312.158 1.00119.88 C
ANISOU 75 CB LEU A 111 15273 10710 19564 2174 -3126 -848 C
ATOM 76 CG LEU A 111 -32.330-167.680 312.109 1.00112.19 C
ANISOU 76 CG LEU A 111 14404 9733 18490 1924 -3026 -736 C
ATOM 77 CD1 LEU A 111 -33.007-167.927 313.432 1.00113.36 C
ANISOU 77 CD1 LEU A 111 14665 9726 18680 1762 -3125 -270 C
ATOM 78 CD2 LEU A 111 -32.386-166.215 311.734 1.00101.31 C
ANISOU 78 CD2 LEU A 111 12983 8683 16829 1896 -2838 -885 C
ATOM 79 N ASN A 112 -27.840-168.210 310.261 1.00116.72 N
ANISOU 79 N ASN A 112 14493 10690 19164 2714 -3087 -1717 N
ATOM 80 CA ASN A 112 -26.416-168.437 310.486 1.00113.11 C
ANISOU 80 CA ASN A 112 13901 10313 18763 2949 -3168 -1799 C
ATOM 81 C ASN A 112 -25.908-167.431 311.512 1.00112.27 C
ANISOU 81 C ASN A 112 13766 10440 18450 2969 -3153 -1577 C
ATOM 82 O ASN A 112 -26.189-166.236 311.379 1.00111.33 O
ANISOU 82 O ASN A 112 13646 10574 18080 2867 -3003 -1625 O
ATOM 83 CB ASN A 112 -25.645-168.296 309.178 1.00109.58 C
ANISOU 83 CB ASN A 112 13289 10095 18253 3075 -3077 -2273 C
ATOM 84 CG ASN A 112 -24.139-168.336 309.365 1.00112.35 C
ANISOU 84 CG ASN A 112 13471 10604 18613 3311 -3134 -2388 C
ATOM 85 OD1 ASN A 112 -23.623-168.984 310.273 1.00112.21 O
ANISOU 85 OD1 ASN A 112 13453 10410 18770 3433 -3289 -2162 O
ATOM 86 ND2 ASN A 112 -23.423-167.643 308.487 1.00113.38 N
ANISOU 86 ND2 ASN A 112 13444 11086 18551 3374 -3009 -2734 N
ATOM 87 N PRO A 113 -25.199-167.874 312.560 1.00112.92 N
ANISOU 87 N PRO A 113 13820 10446 18637 3094 -3313 -1322 N
ATOM 88 CA PRO A 113 -24.703-166.920 313.572 1.00110.09 C
ANISOU 88 CA PRO A 113 13410 10346 18073 3113 -3321 -1113 C
ATOM 89 C PRO A 113 -24.038-165.679 312.996 1.00103.01 C
ANISOU 89 C PRO A 113 12372 9853 16914 3160 -3156 -1424 C
ATOM 90 O PRO A 113 -24.201-164.587 313.555 1.00109.98 O
ANISOU 90 O PRO A 113 13255 10946 17586 3076 -3091 -1310 O
ATOM 91 CB PRO A 113 -23.719-167.773 314.379 1.00112.98 C
ANISOU 91 CB PRO A 113 13698 10620 18611 3308 -3524 -915 C
ATOM 92 CG PRO A 113 -24.315-169.140 314.331 1.00113.32 C
ANISOU 92 CG PRO A 113 13859 10234 18963 3280 -3641 -787 C
ATOM 93 CD PRO A 113 -24.994-169.272 312.981 1.00112.10 C
ANISOU 93 CD PRO A 113 13744 9998 18850 3195 -3507 -1151 C
ATOM 94 N SER A 114 -23.300-165.809 311.892 1.00 96.08 N
ANISOU 94 N SER A 114 11362 9099 16044 3283 -3088 -1817 N
ATOM 95 CA SER A 114 -22.787-164.623 311.213 1.00 90.73 C
ANISOU 95 CA SER A 114 10554 8816 15104 3283 -2910 -2113 C
ATOM 96 C SER A 114 -23.915-163.864 310.523 1.00 99.03 C
ANISOU 96 C SER A 114 11709 9910 16008 3074 -2734 -2190 C
ATOM 97 O SER A 114 -24.000-162.634 310.621 1.00 99.47 O
ANISOU 97 O SER A 114 11744 10209 15842 2992 -2600 -2199 O
ATOM 98 CB SER A 114 -21.698-165.015 310.214 1.00 82.27 C
ANISOU 98 CB SER A 114 9300 7893 14067 3454 -2894 -2497 C
ATOM 99 OG SER A 114 -20.567-165.545 310.887 1.00 82.41 O
ANISOU 99 OG SER A 114 9195 7923 14195 3661 -3042 -2427 O
ATOM 100 N GLN A 115 -24.800-164.583 309.826 1.00100.71 N
ANISOU 100 N GLN A 115 12022 9890 16352 2989 -2734 -2247 N
ATOM 101 CA GLN A 115 -25.983-163.942 309.259 1.00 96.89 C
ANISOU 101 CA GLN A 115 11637 9432 15743 2788 -2588 -2266 C
ATOM 102 C GLN A 115 -26.886-163.381 310.350 1.00 84.49 C
ANISOU 102 C GLN A 115 10213 7771 14120 2637 -2583 -1908 C
ATOM 103 O GLN A 115 -27.635-162.429 310.106 1.00 74.36 O
ANISOU 103 O GLN A 115 8980 6597 12678 2493 -2436 -1909 O
ATOM 104 CB GLN A 115 -26.760-164.934 308.391 1.00110.42 C
ANISOU 104 CB GLN A 115 13410 10920 17624 2733 -2622 -2385 C
ATOM 105 CG GLN A 115 -26.032-165.375 307.130 1.00125.50 C
ANISOU 105 CG GLN A 115 15164 12960 19561 2856 -2606 -2793 C
ATOM 106 CD GLN A 115 -26.750-166.499 306.403 1.00141.11 C
ANISOU 106 CD GLN A 115 17185 14681 21748 2821 -2674 -2915 C
ATOM 107 OE1 GLN A 115 -27.624-167.161 306.965 1.00146.11 O
ANISOU 107 OE1 GLN A 115 17962 14996 22556 2731 -2763 -2674 O
ATOM 108 NE2 GLN A 115 -26.384-166.719 305.145 1.00147.33 N
ANISOU 108 NE2 GLN A 115 17835 15626 22516 2885 -2633 -3301 N
ATOM 109 N GLN A 116 -26.838-163.959 311.553 1.00 92.69 N
ANISOU 109 N GLN A 116 11311 8616 15292 2667 -2747 -1592 N
ATOM 110 CA GLN A 116 -27.606-163.406 312.664 1.00 95.88 C
ANISOU 110 CA GLN A 116 11827 8976 15628 2526 -2759 -1248 C
ATOM 111 C GLN A 116 -27.001-162.095 313.146 1.00 92.93 C
ANISOU 111 C GLN A 116 11362 8949 15000 2529 -2656 -1260 C
ATOM 112 O GLN A 116 -27.730-161.147 313.463 1.00 90.12 O
ANISOU 112 O GLN A 116 11076 8762 14403 2290 -2478 -1138 O
ATOM 113 CB GLN A 116 -27.679-164.411 313.813 1.00103.95 C
ANISOU 113 CB GLN A 116 12920 9744 16831 2534 -2974 -874 C
ATOM 114 CG GLN A 116 -28.474-165.667 313.503 1.00108.77 C
ANISOU 114 CG GLN A 116 13640 10014 17674 2455 -3048 -806 C
ATOM 115 CD GLN A 116 -28.540-166.612 314.686 1.00115.59 C
ANISOU 115 CD GLN A 116 14572 10637 18707 2442 -3255 -394 C
ATOM 116 OE1 GLN A 116 -28.600-166.180 315.838 1.00113.69 O
ANISOU 116 OE1 GLN A 116 14354 10479 18362 2381 -3321 -63 O
ATOM 117 NE2 GLN A 116 -28.522-167.909 314.410 1.00124.53 N
ANISOU 117 NE2 GLN A 116 15729 11484 20102 2494 -3365 -405 N
ATOM 118 N LEU A 117 -25.671-162.023 313.211 1.00 97.12 N
ANISOU 118 N LEU A 117 11727 9678 15494 2713 -2702 -1396 N
ATOM 119 CA LEU A 117 -25.017-160.790 313.634 1.00101.97 C
ANISOU 119 CA LEU A 117 12245 10728 15771 2611 -2538 -1411 C
ATOM 120 C LEU A 117 -25.255-159.672 312.626 1.00101.54 C
ANISOU 120 C LEU A 117 12174 10893 15514 2482 -2280 -1665 C
ATOM 121 O LEU A 117 -25.600-158.546 313.003 1.00103.25 O
ANISOU 121 O LEU A 117 12428 11321 15482 2264 -2096 -1578 O
ATOM 122 CB LEU A 117 -23.521-161.032 313.832 1.00101.88 C
ANISOU 122 CB LEU A 117 12036 10892 15782 2842 -2656 -1521 C
ATOM 123 CG LEU A 117 -22.701-159.824 314.286 1.00 95.03 C
ANISOU 123 CG LEU A 117 11041 10487 14577 2734 -2505 -1562 C
ATOM 124 CD1 LEU A 117 -23.287-159.221 315.552 1.00 85.44 C
ANISOU 124 CD1 LEU A 117 9927 9386 13149 2479 -2448 -1237 C
ATOM 125 CD2 LEU A 117 -21.250-160.220 314.506 1.00101.67 C
ANISOU 125 CD2 LEU A 117 11666 11497 15465 2977 -2654 -1656 C
ATOM 126 N ALA A 118 -25.082-159.969 311.335 1.00101.15 N
ANISOU 126 N ALA A 118 12061 10798 15573 2613 -2266 -1981 N
ATOM 127 CA ALA A 118 -25.318-158.962 310.305 1.00 97.17 C
ANISOU 127 CA ALA A 118 11533 10515 14873 2486 -2039 -2185 C
ATOM 128 C ALA A 118 -26.752-158.453 310.349 1.00 99.48 C
ANISOU 128 C ALA A 118 11996 10706 15098 2251 -1919 -2001 C
ATOM 129 O ALA A 118 -26.997-157.252 310.185 1.00105.22 O
ANISOU 129 O ALA A 118 12728 11645 15606 2078 -1717 -1995 O
ATOM 130 CB ALA A 118 -24.996-159.532 308.924 1.00 97.72 C
ANISOU 130 CB ALA A 118 11500 10566 15065 2656 -2066 -2544 C
ATOM 131 N ILE A 119 -27.713-159.351 310.570 1.00101.14 N
ANISOU 131 N ILE A 119 12335 10583 15510 2240 -2045 -1847 N
ATOM 132 CA ILE A 119 -29.101-158.929 310.741 1.00100.61 C
ANISOU 132 CA ILE A 119 12409 10434 15383 2018 -1943 -1653 C
ATOM 133 C ILE A 119 -29.225-158.010 311.951 1.00 94.44 C
ANISOU 133 C ILE A 119 11663 9823 14397 1846 -1837 -1410 C
ATOM 134 O ILE A 119 -29.854-156.948 311.885 1.00 93.28 O
ANISOU 134 O ILE A 119 11548 9807 14086 1675 -1646 -1379 O
ATOM 135 CB ILE A 119 -30.025-160.155 310.862 1.00104.39 C
ANISOU 135 CB ILE A 119 13005 10532 16125 2024 -2115 -1521 C
ATOM 136 CG1 ILE A 119 -30.248-160.794 309.490 1.00105.70 C
ANISOU 136 CG1 ILE A 119 13145 10597 16418 2092 -2138 -1794 C
ATOM 137 CG2 ILE A 119 -31.354-159.769 311.494 1.00106.08 C
ANISOU 137 CG2 ILE A 119 13346 10699 16261 1786 -2032 -1245 C
ATOM 138 CD1 ILE A 119 -30.954-159.889 308.507 1.00105.21 C
ANISOU 138 CD1 ILE A 119 13078 10690 16207 1982 -1962 -1928 C
ATOM 139 N ALA A 120 -28.611-158.401 313.070 1.00 96.08 N
ANISOU 139 N ALA A 120 11850 10041 14613 1893 -1962 -1245 N
ATOM 140 CA ALA A 120 -28.701-157.597 314.284 1.00 99.09 C
ANISOU 140 CA ALA A 120 12247 10621 14780 1719 -1869 -1041 C
ATOM 141 C ALA A 120 -28.010-156.250 314.112 1.00103.52 C
ANISOU 141 C ALA A 120 12712 11511 15110 1654 -1667 -1216 C
ATOM 142 O ALA A 120 -28.520-155.222 314.575 1.00100.85 O
ANISOU 142 O ALA A 120 12410 11304 14606 1463 -1493 -1153 O
ATOM 143 CB ALA A 120 -28.104-158.361 315.465 1.00103.74 C
ANISOU 143 CB ALA A 120 12811 11198 15408 1786 -2069 -821 C
ATOM 144 N VAL A 121 -26.852-156.233 313.448 1.00106.32 N
ANISOU 144 N VAL A 121 12936 11997 15462 1805 -1685 -1448 N
ATOM 145 CA VAL A 121 -26.119-154.983 313.257 1.00104.28 C
ANISOU 145 CA VAL A 121 12577 12050 14994 1722 -1500 -1607 C
ATOM 146 C VAL A 121 -26.928-154.017 312.399 1.00 97.15 C
ANISOU 146 C VAL A 121 11733 11153 14029 1580 -1293 -1675 C
ATOM 147 O VAL A 121 -27.147-152.859 312.774 1.00108.42 O
ANISOU 147 O VAL A 121 13178 12706 15313 1403 -1117 -1640 O
ATOM 148 CB VAL A 121 -24.734-155.259 312.645 1.00101.76 C
ANISOU 148 CB VAL A 121 12084 11890 14688 1912 -1567 -1844 C
ATOM 149 CG1 VAL A 121 -24.089-153.960 312.187 1.00103.84 C
ANISOU 149 CG1 VAL A 121 12247 12459 14747 1794 -1361 -2016 C
ATOM 150 CG2 VAL A 121 -23.839-155.964 313.653 1.00102.41 C
ANISOU 150 CG2 VAL A 121 12081 12026 14804 2042 -1759 -1748 C
ATOM 151 N LEU A 122 -27.390-154.481 311.236 1.00 83.67 N
ANISOU 151 N LEU A 122 10046 9308 12436 1656 -1316 -1778 N
ATOM 152 CA LEU A 122 -28.137-153.604 310.341 1.00 84.02 C
ANISOU 152 CA LEU A 122 10126 9382 12417 1534 -1142 -1816 C
ATOM 153 C LEU A 122 -29.462-153.165 310.949 1.00 97.95 C
ANISOU 153 C LEU A 122 12020 11017 14181 1372 -1059 -1602 C
ATOM 154 O LEU A 122 -29.925-152.050 310.683 1.00104.32 O
ANISOU 154 O LEU A 122 12841 11890 14904 1242 -883 -1586 O
ATOM 155 CB LEU A 122 -28.376-154.300 309.004 1.00 89.05 C
ANISOU 155 CB LEU A 122 10740 9939 13155 1643 -1205 -1973 C
ATOM 156 CG LEU A 122 -27.127-154.658 308.203 1.00100.89 C
ANISOU 156 CG LEU A 122 12082 11611 14642 1803 -1255 -2242 C
ATOM 157 CD1 LEU A 122 -27.506-155.433 306.951 1.00108.45 C
ANISOU 157 CD1 LEU A 122 13017 12491 15698 1898 -1320 -2422 C
ATOM 158 CD2 LEU A 122 -26.348-153.402 307.847 1.00104.86 C
ANISOU 158 CD2 LEU A 122 12478 12430 14934 1702 -1077 -2328 C
ATOM 159 N SER A 123 -30.085-154.014 311.766 1.00103.24 N
ANISOU 159 N SER A 123 12773 11504 14951 1375 -1185 -1431 N
ATOM 160 CA SER A 123 -31.385-153.666 312.328 1.00105.10 C
ANISOU 160 CA SER A 123 13107 11649 15178 1219 -1104 -1245 C
ATOM 161 C SER A 123 -31.265-152.792 313.569 1.00102.70 C
ANISOU 161 C SER A 123 12798 11500 14725 1082 -991 -1156 C
ATOM 162 O SER A 123 -32.150-151.968 313.821 1.00 96.86 O
ANISOU 162 O SER A 123 12096 10767 13939 946 -839 -1095 O
ATOM 163 CB SER A 123 -32.179-154.933 312.647 1.00105.57 C
ANISOU 163 CB SER A 123 13250 11467 15396 1241 -1276 -1088 C
ATOM 164 OG SER A 123 -31.387-155.867 313.358 1.00108.53 O
ANISOU 164 OG SER A 123 13607 11797 15832 1343 -1460 -1025 O
ATOM 165 N LEU A 124 -30.197-152.950 314.354 1.00104.74 N
ANISOU 165 N LEU A 124 12993 11895 14906 1118 -1062 -1163 N
ATOM 166 CA LEU A 124 -30.044-152.112 315.537 1.00105.09 C
ANISOU 166 CA LEU A 124 13016 12131 14784 970 -953 -1116 C
ATOM 167 C LEU A 124 -29.450-150.751 315.205 1.00104.76 C
ANISOU 167 C LEU A 124 12908 12262 14636 895 -758 -1300 C
ATOM 168 O LEU A 124 -29.687-149.785 315.939 1.00104.70 O
ANISOU 168 O LEU A 124 12900 12356 14527 739 -606 -1308 O
ATOM 169 CB LEU A 124 -29.191-152.820 316.591 1.00107.81 C
ANISOU 169 CB LEU A 124 13307 12592 15066 1016 -1119 -1022 C
ATOM 170 CG LEU A 124 -30.005-153.751 317.492 1.00110.09 C
ANISOU 170 CG LEU A 124 13671 12766 15394 972 -1253 -754 C
ATOM 171 CD1 LEU A 124 -29.176-154.305 318.637 1.00113.35 C
ANISOU 171 CD1 LEU A 124 14018 13339 15711 991 -1413 -611 C
ATOM 172 CD2 LEU A 124 -31.236-153.029 318.021 1.00108.68 C
ANISOU 172 CD2 LEU A 124 13550 12614 15130 771 -1081 -678 C
ATOM 173 N THR A 125 -28.684-150.648 314.121 1.00103.30 N
ANISOU 173 N THR A 125 12658 12115 14474 989 -756 -1457 N
ATOM 174 CA THR A 125 -28.208-149.343 313.684 1.00100.44 C
ANISOU 174 CA THR A 125 12241 11889 14031 890 -568 -1598 C
ATOM 175 C THR A 125 -29.348-148.580 313.025 1.00102.53 C
ANISOU 175 C THR A 125 12581 12012 14363 809 -419 -1556 C
ATOM 176 O THR A 125 -29.791-147.549 313.541 1.00105.02 O
ANISOU 176 O THR A 125 12921 12327 14655 669 -260 -1543 O
ATOM 177 CB THR A 125 -27.025-149.471 312.720 1.00 90.79 C
ANISOU 177 CB THR A 125 10907 10802 12789 996 -607 -1765 C
ATOM 178 OG1 THR A 125 -27.376-150.341 311.634 1.00 89.68 O
ANISOU 178 OG1 THR A 125 10783 10531 12760 1137 -708 -1783 O
ATOM 179 CG2 THR A 125 -25.798-150.016 313.444 1.00 83.83 C
ANISOU 179 CG2 THR A 125 9916 10098 11837 1076 -737 -1819 C
ATOM 180 N LEU A 126 -29.834-149.092 311.890 1.00 99.08 N
ANISOU 180 N LEU A 126 12168 11461 14017 901 -475 -1544 N
ATOM 181 CA LEU A 126 -30.920-148.425 311.177 1.00 99.30 C
ANISOU 181 CA LEU A 126 12247 11379 14105 840 -357 -1479 C
ATOM 182 C LEU A 126 -32.139-148.240 312.070 1.00101.66 C
ANISOU 182 C LEU A 126 12623 11554 14449 757 -303 -1343 C
ATOM 183 O LEU A 126 -32.793-147.192 312.027 1.00105.10 O
ANISOU 183 O LEU A 126 13073 11944 14916 669 -146 -1313 O
ATOM 184 CB LEU A 126 -31.295-149.215 309.924 1.00100.92 C
ANISOU 184 CB LEU A 126 12451 11519 14375 948 -458 -1490 C
ATOM 185 CG LEU A 126 -30.551-148.900 308.623 1.00102.73 C
ANISOU 185 CG LEU A 126 12592 11901 14542 979 -426 -1615 C
ATOM 186 CD1 LEU A 126 -29.054-149.134 308.762 1.00105.13 C
ANISOU 186 CD1 LEU A 126 12794 12386 14765 1038 -475 -1775 C
ATOM 187 CD2 LEU A 126 -31.120-149.726 307.477 1.00101.27 C
ANISOU 187 CD2 LEU A 126 12402 11671 14404 1066 -524 -1642 C
ATOM 188 N GLY A 127 -32.458-149.243 312.886 1.00103.54 N
ANISOU 188 N GLY A 127 12899 11740 14701 782 -431 -1255 N
ATOM 189 CA GLY A 127 -33.579-149.150 313.799 1.00101.84 C
ANISOU 189 CA GLY A 127 12735 11463 14497 687 -380 -1129 C
ATOM 190 C GLY A 127 -33.444-147.998 314.773 1.00 99.70 C
ANISOU 190 C GLY A 127 12437 11308 14138 556 -210 -1186 C
ATOM 191 O GLY A 127 -34.322-147.133 314.840 1.00 99.26 O
ANISOU 191 O GLY A 127 12390 11197 14129 483 -58 -1180 O
ATOM 192 N THR A 128 -32.344-147.972 315.528 1.00 98.72 N
ANISOU 192 N THR A 128 12264 11351 13895 529 -236 -1259 N
ATOM 193 CA THR A 128 -32.103-146.851 316.431 1.00104.40 C
ANISOU 193 CA THR A 128 12943 12205 14521 388 -70 -1365 C
ATOM 194 C THR A 128 -31.984-145.544 315.658 1.00104.41 C
ANISOU 194 C THR A 128 12929 12146 14596 346 107 -1487 C
ATOM 195 O THR A 128 -32.429-144.491 316.128 1.00105.47 O
ANISOU 195 O THR A 128 13059 12257 14758 237 279 -1557 O
ATOM 196 CB THR A 128 -30.842-147.102 317.261 1.00109.24 C
ANISOU 196 CB THR A 128 13486 13044 14977 366 -150 -1428 C
ATOM 197 OG1 THR A 128 -30.971-148.345 317.964 1.00111.75 O
ANISOU 197 OG1 THR A 128 13819 13397 15246 410 -335 -1262 O
ATOM 198 CG2 THR A 128 -30.631-145.981 318.268 1.00107.85 C
ANISOU 198 CG2 THR A 128 13258 13033 14687 193 20 -1570 C
ATOM 199 N PHE A 129 -31.400-145.595 314.460 1.00107.15 N
ANISOU 199 N PHE A 129 13261 12467 14984 426 67 -1511 N
ATOM 200 CA PHE A 129 -31.275-144.389 313.650 1.00111.46 C
ANISOU 200 CA PHE A 129 13792 12958 15600 371 219 -1571 C
ATOM 201 C PHE A 129 -32.636-143.921 313.147 1.00106.67 C
ANISOU 201 C PHE A 129 13237 12153 15141 378 304 -1462 C
ATOM 202 O PHE A 129 -32.926-142.719 313.157 1.00110.93 O
ANISOU 202 O PHE A 129 13774 12601 15773 298 467 -1492 O
ATOM 203 CB PHE A 129 -30.323-144.645 312.481 1.00122.05 C
ANISOU 203 CB PHE A 129 15084 14380 16909 442 149 -1608 C
ATOM 204 CG PHE A 129 -29.741-143.397 311.885 1.00135.76 C
ANISOU 204 CG PHE A 129 16779 16141 18661 337 295 -1671 C
ATOM 205 CD1 PHE A 129 -28.816-142.644 312.590 1.00143.91 C
ANISOU 205 CD1 PHE A 129 17759 17288 19631 208 386 -1808 C
ATOM 206 CD2 PHE A 129 -30.101-142.987 310.612 1.00141.58 C
ANISOU 206 CD2 PHE A 129 17522 16803 19471 350 335 -1582 C
ATOM 207 CE1 PHE A 129 -28.271-141.496 312.043 1.00148.63 C
ANISOU 207 CE1 PHE A 129 18322 17885 20265 86 519 -1854 C
ATOM 208 CE2 PHE A 129 -29.558-141.841 310.058 1.00146.48 C
ANISOU 208 CE2 PHE A 129 18104 17438 20112 234 462 -1595 C
ATOM 209 CZ PHE A 129 -28.643-141.094 310.774 1.00148.74 C
ANISOU 209 CZ PHE A 129 18351 17800 20363 98 556 -1731 C
ATOM 210 N THR A 130 -33.486-144.855 312.714 1.00100.78 N
ANISOU 210 N THR A 130 12527 11331 14434 473 191 -1338 N
ATOM 211 CA THR A 130 -34.801-144.478 312.202 1.00101.36 C
ANISOU 211 CA THR A 130 12624 11251 14637 488 254 -1226 C
ATOM 212 C THR A 130 -35.690-143.925 313.308 1.00102.73 C
ANISOU 212 C THR A 130 12802 11370 14860 416 375 -1233 C
ATOM 213 O THR A 130 -36.405-142.937 313.101 1.00107.15 O
ANISOU 213 O THR A 130 13350 11809 15551 400 509 -1216 O
ATOM 214 CB THR A 130 -35.473-145.678 311.534 1.00101.72 C
ANISOU 214 CB THR A 130 12693 11256 14699 585 96 -1119 C
ATOM 215 OG1 THR A 130 -34.583-146.248 310.567 1.00100.06 O
ANISOU 215 OG1 THR A 130 12460 11124 14434 657 -14 -1168 O
ATOM 216 CG2 THR A 130 -36.757-145.252 310.842 1.00101.94 C
ANISOU 216 CG2 THR A 130 12718 11170 14844 601 151 -1000 C
ATOM 217 N VAL A 131 -35.665-144.550 314.487 1.00102.20 N
ANISOU 217 N VAL A 131 12739 11404 14690 373 329 -1256 N
ATOM 218 CA VAL A 131 -36.501-144.084 315.588 1.00104.47 C
ANISOU 218 CA VAL A 131 13006 11704 14984 290 451 -1289 C
ATOM 219 C VAL A 131 -36.095-142.679 316.008 1.00108.97 C
ANISOU 219 C VAL A 131 13540 12269 15596 202 643 -1468 C
ATOM 220 O VAL A 131 -36.949-141.810 316.221 1.00118.59 O
ANISOU 220 O VAL A 131 14733 13384 16942 180 793 -1516 O
ATOM 221 CB VAL A 131 -36.434-145.069 316.769 1.00104.76 C
ANISOU 221 CB VAL A 131 13042 11904 14858 236 351 -1253 C
ATOM 222 CG1 VAL A 131 -37.236-144.539 317.948 1.00 99.48 C
ANISOU 222 CG1 VAL A 131 12327 11321 14150 125 495 -1317 C
ATOM 223 CG2 VAL A 131 -36.949-146.428 316.346 1.00109.57 C
ANISOU 223 CG2 VAL A 131 13695 12454 15482 310 164 -1069 C
ATOM 224 N LEU A 132 -34.788-142.428 316.120 1.00104.97 N
ANISOU 224 N LEU A 132 13019 11864 15001 151 641 -1584 N
ATOM 225 CA LEU A 132 -34.325-141.112 316.550 1.00100.48 C
ANISOU 225 CA LEU A 132 12415 11284 14481 38 819 -1778 C
ATOM 226 C LEU A 132 -34.678-140.036 315.531 1.00 95.93 C
ANISOU 226 C LEU A 132 11852 10463 14134 65 932 -1748 C
ATOM 227 O LEU A 132 -34.992-138.900 315.904 1.00 90.34 O
ANISOU 227 O LEU A 132 11123 9629 13572 1 1102 -1873 O
ATOM 228 CB LEU A 132 -32.818-141.140 316.803 1.00 96.79 C
ANISOU 228 CB LEU A 132 11914 11002 13862 -33 776 -1896 C
ATOM 229 CG LEU A 132 -32.371-141.904 318.051 1.00 94.98 C
ANISOU 229 CG LEU A 132 11645 11037 13405 -88 689 -1943 C
ATOM 230 CD1 LEU A 132 -30.862-141.820 318.221 1.00 96.47 C
ANISOU 230 CD1 LEU A 132 11775 11422 13458 -151 650 -2065 C
ATOM 231 CD2 LEU A 132 -33.086-141.377 319.286 1.00 95.10 C
ANISOU 231 CD2 LEU A 132 11627 11123 13385 -204 828 -2069 C
ATOM 232 N GLU A 133 -34.629-140.373 314.240 1.00 99.49 N
ANISOU 232 N GLU A 133 12328 10847 14625 158 837 -1585 N
ATOM 233 CA GLU A 133 -35.022-139.423 313.204 1.00106.41 C
ANISOU 233 CA GLU A 133 13210 11518 15703 183 919 -1490 C
ATOM 234 C GLU A 133 -36.476-139.000 313.373 1.00107.23 C
ANISOU 234 C GLU A 133 13306 11448 15989 240 1002 -1432 C
ATOM 235 O GLU A 133 -36.782-137.809 313.504 1.00110.21 O
ANISOU 235 O GLU A 133 13666 11642 16568 210 1153 -1494 O
ATOM 236 CB GLU A 133 -34.801-140.036 311.822 1.00110.09 C
ANISOU 236 CB GLU A 133 13685 12024 16122 266 785 -1320 C
ATOM 237 CG GLU A 133 -33.356-140.079 311.376 1.00118.35 C
ANISOU 237 CG GLU A 133 14707 13219 17040 211 745 -1384 C
ATOM 238 CD GLU A 133 -33.193-140.782 310.046 1.00127.71 C
ANISOU 238 CD GLU A 133 15879 14493 18151 295 616 -1258 C
ATOM 239 OE1 GLU A 133 -34.019-141.668 309.745 1.00131.09 O
ANISOU 239 OE1 GLU A 133 16324 14913 18571 399 511 -1166 O
ATOM 240 OE2 GLU A 133 -32.251-140.443 309.299 1.00131.35 O
ANISOU 240 OE2 GLU A 133 16302 15050 18557 243 626 -1264 O
ATOM 241 N ASN A 134 -37.391-139.971 313.378 1.00102.90 N
ANISOU 241 N ASN A 134 12760 10948 15390 322 903 -1322 N
ATOM 242 CA ASN A 134 -38.812-139.644 313.430 1.00 99.38 C
ANISOU 242 CA ASN A 134 12279 10373 15107 386 971 -1255 C
ATOM 243 C ASN A 134 -39.209-139.088 314.793 1.00 97.44 C
ANISOU 243 C ASN A 134 11989 10134 14898 320 1123 -1454 C
ATOM 244 O ASN A 134 -40.068-138.202 314.878 1.00 93.08 O
ANISOU 244 O ASN A 134 11387 9421 14557 360 1252 -1489 O
ATOM 245 CB ASN A 134 -39.641-140.876 313.077 1.00 91.92 C
ANISOU 245 CB ASN A 134 11336 9504 14084 461 822 -1096 C
ATOM 246 CG ASN A 134 -39.376-141.361 311.667 1.00 88.16 C
ANISOU 246 CG ASN A 134 10883 9034 13581 526 685 -939 C
ATOM 247 OD1 ASN A 134 -40.026-140.925 310.714 1.00 79.42 O
ANISOU 247 OD1 ASN A 134 9747 7832 12597 591 690 -797 O
ATOM 248 ND2 ASN A 134 -38.406-142.257 311.523 1.00 96.35 N
ANISOU 248 ND2 ASN A 134 11956 10201 14451 514 561 -970 N
ATOM 249 N LEU A 135 -38.596-139.590 315.869 1.00 98.49 N
ANISOU 249 N LEU A 135 12124 10470 14827 222 1108 -1594 N
ATOM 250 CA LEU A 135 -38.851-139.012 317.185 1.00 99.02 C
ANISOU 250 CA LEU A 135 12131 10606 14884 130 1262 -1820 C
ATOM 251 C LEU A 135 -38.440-137.546 317.227 1.00101.82 C
ANISOU 251 C LEU A 135 12468 10781 15438 81 1438 -2015 C
ATOM 252 O LEU A 135 -39.035-136.753 317.965 1.00102.94 O
ANISOU 252 O LEU A 135 12545 10864 15705 56 1602 -2210 O
ATOM 253 CB LEU A 135 -38.118-139.809 318.266 1.00 96.72 C
ANISOU 253 CB LEU A 135 11837 10609 14305 18 1194 -1904 C
ATOM 254 CG LEU A 135 -38.615-139.660 319.707 1.00 97.56 C
ANISOU 254 CG LEU A 135 11861 10908 14298 -89 1311 -2088 C
ATOM 255 CD1 LEU A 135 -40.070-140.085 319.822 1.00 94.88 C
ANISOU 255 CD1 LEU A 135 11478 10575 13999 -34 1319 -1976 C
ATOM 256 CD2 LEU A 135 -37.747-140.467 320.660 1.00 97.71 C
ANISOU 256 CD2 LEU A 135 11874 11243 14009 -206 1212 -2113 C
ATOM 257 N LEU A 136 -37.431-137.169 316.437 1.00101.65 N
ANISOU 257 N LEU A 136 12494 10669 15459 60 1409 -1977 N
ATOM 258 CA LEU A 136 -37.087-135.759 316.296 1.00102.59 C
ANISOU 258 CA LEU A 136 12606 10556 15816 4 1564 -2111 C
ATOM 259 C LEU A 136 -38.102-135.031 315.425 1.00108.80 C
ANISOU 259 C LEU A 136 13385 11033 16920 133 1615 -1954 C
ATOM 260 O LEU A 136 -38.493-133.899 315.733 1.00119.19 O
ANISOU 260 O LEU A 136 14665 12119 18503 130 1773 -2099 O
ATOM 261 CB LEU A 136 -35.681-135.618 315.712 1.00 99.81 C
ANISOU 261 CB LEU A 136 12294 10238 15391 -85 1514 -2093 C
ATOM 262 CG LEU A 136 -35.246-134.221 315.259 1.00101.21 C
ANISOU 262 CG LEU A 136 12480 10142 15833 -161 1643 -2147 C
ATOM 263 CD1 LEU A 136 -35.183-133.257 316.436 1.00100.29 C
ANISOU 263 CD1 LEU A 136 12321 9952 15833 -282 1826 -2489 C
ATOM 264 CD2 LEU A 136 -33.906-134.282 314.538 1.00101.00 C
ANISOU 264 CD2 LEU A 136 12476 10211 15687 -253 1570 -2077 C
ATOM 265 N VAL A 137 -38.545-135.667 314.337 1.00107.39 N
ANISOU 265 N VAL A 137 13230 10849 16727 249 1478 -1664 N
ATOM 266 CA VAL A 137 -39.508-135.034 313.438 1.00108.62 C
ANISOU 266 CA VAL A 137 13361 10753 17158 377 1499 -1469 C
ATOM 267 C VAL A 137 -40.816-134.757 314.169 1.00106.48 C
ANISOU 267 C VAL A 137 13007 10406 17044 462 1602 -1571 C
ATOM 268 O VAL A 137 -41.375-133.657 314.082 1.00107.88 O
ANISOU 268 O VAL A 137 13138 10339 17512 522 1708 -1584 O
ATOM 269 CB VAL A 137 -39.733-135.906 312.189 1.00107.67 C
ANISOU 269 CB VAL A 137 13260 10722 16928 465 1320 -1165 C
ATOM 270 CG1 VAL A 137 -40.829-135.311 311.318 1.00105.82 C
ANISOU 270 CG1 VAL A 137 12976 10282 16948 600 1325 -941 C
ATOM 271 CG2 VAL A 137 -38.442-136.046 311.401 1.00107.93 C
ANISOU 271 CG2 VAL A 137 13346 10841 16822 386 1241 -1091 C
ATOM 272 N LEU A 138 -41.322-135.753 314.901 1.00103.22 N
ANISOU 272 N LEU A 138 12564 10234 16421 459 1559 -1624 N
ATOM 273 CA LEU A 138 -42.549-135.554 315.665 1.00105.44 C
ANISOU 273 CA LEU A 138 12741 10514 16809 519 1667 -1743 C
ATOM 274 C LEU A 138 -42.374-134.461 316.712 1.00109.04 C
ANISOU 274 C LEU A 138 13146 10876 17409 450 1872 -2089 C
ATOM 275 O LEU A 138 -43.291-133.665 316.950 1.00114.21 O
ANISOU 275 O LEU A 138 13706 11400 18288 530 1983 -2173 O
ATOM 276 CB LEU A 138 -42.979-136.865 316.324 1.00108.34 C
ANISOU 276 CB LEU A 138 13087 11193 16885 478 1580 -1725 C
ATOM 277 CG LEU A 138 -43.452-137.977 315.384 1.00112.37 C
ANISOU 277 CG LEU A 138 13624 11774 17297 551 1390 -1426 C
ATOM 278 CD1 LEU A 138 -43.876-139.203 316.175 1.00117.34 C
ANISOU 278 CD1 LEU A 138 14234 12671 17678 481 1317 -1418 C
ATOM 279 CD2 LEU A 138 -44.590-137.486 314.503 1.00112.08 C
ANISOU 279 CD2 LEU A 138 13513 11559 17513 705 1399 -1259 C
ATOM 280 N CYS A 139 -41.201-134.401 317.346 1.00108.28 N
ANISOU 280 N CYS A 139 13096 10896 17150 290 1902 -2284 N
ATOM 281 CA CYS A 139 -40.952-133.351 318.328 1.00112.97 C
ANISOU 281 CA CYS A 139 13636 11435 17851 192 2087 -2638 C
ATOM 282 C CYS A 139 -40.930-131.978 317.669 1.00114.10 C
ANISOU 282 C CYS A 139 13785 11289 18281 222 2116 -2546 C
ATOM 283 O CYS A 139 -41.395-130.994 318.257 1.00118.84 O
ANISOU 283 O CYS A 139 14304 11803 19045 219 2234 -2729 O
ATOM 284 CB CYS A 139 -39.638-133.614 319.061 1.00116.23 C
ANISOU 284 CB CYS A 139 14087 12076 17997 -1 2086 -2837 C
ATOM 285 SG CYS A 139 -39.164-132.294 320.204 1.00127.79 S
ANISOU 285 SG CYS A 139 15479 13542 19533 -167 2277 -3254 S
ATOM 286 N VAL A 140 -40.400-131.896 316.448 1.00108.08 N
ANISOU 286 N VAL A 140 13106 10371 17587 249 2013 -2271 N
ATOM 287 CA VAL A 140 -40.350-130.619 315.742 1.00107.71 C
ANISOU 287 CA VAL A 140 13069 10036 17821 269 2038 -2148 C
ATOM 288 C VAL A 140 -41.754-130.149 315.382 1.00112.44 C
ANISOU 288 C VAL A 140 13589 10482 18651 450 2038 -1998 C
ATOM 289 O VAL A 140 -42.084-128.968 315.536 1.00124.73 O
ANISOU 289 O VAL A 140 15097 11833 20461 474 2119 -2069 O
ATOM 290 CB VAL A 140 -39.451-130.734 314.497 1.00101.00 C
ANISOU 290 CB VAL A 140 12314 9096 16966 239 1936 -1884 C
ATOM 291 CG1 VAL A 140 -39.629-129.526 313.595 1.00100.54 C
ANISOU 291 CG1 VAL A 140 12258 8729 17212 284 1943 -1669 C
ATOM 292 CG2 VAL A 140 -37.993-130.877 314.906 1.00 98.44 C
ANISOU 292 CG2 VAL A 140 12043 8887 16472 46 1963 -2081 C
ATOM 293 N ILE A 141 -42.604-131.065 314.911 1.00105.28 N
ANISOU 293 N ILE A 141 12659 9670 17673 581 1944 -1799 N
ATOM 294 CA ILE A 141 -43.952-130.687 314.491 1.00101.54 C
ANISOU 294 CA ILE A 141 12094 9081 17407 757 1931 -1640 C
ATOM 295 C ILE A 141 -44.747-130.142 315.671 1.00105.12 C
ANISOU 295 C ILE A 141 12429 9549 17964 780 2074 -1945 C
ATOM 296 O ILE A 141 -45.375-129.080 315.581 1.00 95.30 O
ANISOU 296 O ILE A 141 11116 8100 16993 870 2122 -1944 O
ATOM 297 CB ILE A 141 -44.667-131.884 313.839 1.00103.69 C
ANISOU 297 CB ILE A 141 12348 9494 17554 868 1805 -1402 C
ATOM 298 CG1 ILE A 141 -43.897-132.359 312.605 1.00102.73 C
ANISOU 298 CG1 ILE A 141 12326 9362 17343 850 1666 -1119 C
ATOM 299 CG2 ILE A 141 -46.092-131.513 313.468 1.00104.57 C
ANISOU 299 CG2 ILE A 141 12340 9524 17869 1046 1793 -1257 C
ATOM 300 CD1 ILE A 141 -44.419-133.659 312.024 1.00 98.40 C
ANISOU 300 CD1 ILE A 141 11766 8975 16646 930 1535 -931 C
ATOM 301 N LEU A 142 -44.734-130.863 316.795 1.00114.19 N
ANISOU 301 N LEU A 142 13541 10947 18900 699 2146 -2216 N
ATOM 302 CA LEU A 142 -45.461-130.402 317.975 1.00118.71 C
ANISOU 302 CA LEU A 142 13980 11590 19535 701 2297 -2542 C
ATOM 303 C LEU A 142 -44.889-129.089 318.492 1.00117.69 C
ANISOU 303 C LEU A 142 13846 11300 19571 609 2405 -2784 C
ATOM 304 O LEU A 142 -45.636-128.210 318.938 1.00123.16 O
ANISOU 304 O LEU A 142 14428 11886 20479 676 2502 -2952 O
ATOM 305 CB LEU A 142 -45.432-131.470 319.068 1.00120.33 C
ANISOU 305 CB LEU A 142 14144 12135 19441 600 2357 -2779 C
ATOM 306 CG LEU A 142 -46.610-132.447 319.102 1.00121.09 C
ANISOU 306 CG LEU A 142 14140 12397 19472 711 2343 -2697 C
ATOM 307 CD1 LEU A 142 -46.710-133.242 317.807 1.00121.15 C
ANISOU 307 CD1 LEU A 142 14225 12329 19477 813 2167 -2299 C
ATOM 308 CD2 LEU A 142 -46.492-133.377 320.299 1.00123.36 C
ANISOU 308 CD2 LEU A 142 14374 13032 19467 581 2435 -2963 C
ATOM 309 N HIS A 143 -43.564-128.940 318.444 1.00115.67 N
ANISOU 309 N HIS A 143 13696 11023 19228 454 2393 -2819 N
ATOM 310 CA HIS A 143 -42.962-127.645 318.741 1.00120.95 C
ANISOU 310 CA HIS A 143 14364 11496 20094 362 2484 -3006 C
ATOM 311 C HIS A 143 -43.381-126.607 317.708 1.00122.34 C
ANISOU 311 C HIS A 143 14551 11302 20632 498 2444 -2754 C
ATOM 312 O HIS A 143 -43.648-125.448 318.050 1.00122.58 O
ANISOU 312 O HIS A 143 14519 11123 20934 518 2536 -2919 O
ATOM 313 CB HIS A 143 -41.439-127.776 318.793 1.00122.50 C
ANISOU 313 CB HIS A 143 14664 11765 20116 164 2469 -3067 C
ATOM 314 CG HIS A 143 -40.725-126.477 318.995 1.00128.70 C
ANISOU 314 CG HIS A 143 15453 12339 21109 50 2557 -3238 C
ATOM 315 ND1 HIS A 143 -40.569-125.896 320.236 1.00133.02 N
ANISOU 315 ND1 HIS A 143 15911 12976 21654 -73 2696 -3649 N
ATOM 316 CD2 HIS A 143 -40.121-125.645 318.113 1.00130.15 C
ANISOU 316 CD2 HIS A 143 15712 12229 21512 28 2527 -3057 C
ATOM 317 CE1 HIS A 143 -39.901-124.763 320.109 1.00134.38 C
ANISOU 317 CE1 HIS A 143 16107 12901 22051 -160 2747 -3722 C
ATOM 318 NE2 HIS A 143 -39.618-124.588 318.831 1.00132.16 N
ANISOU 318 NE2 HIS A 143 15928 12376 21911 -103 2648 -3360 N
ATOM 319 N SER A 144 -43.455-127.010 316.435 1.00118.45 N
ANISOU 319 N SER A 144 14129 10730 20148 592 2305 -2354 N
ATOM 320 CA SER A 144 -43.921-126.102 315.391 1.00115.18 C
ANISOU 320 CA SER A 144 13714 9998 20053 725 2251 -2070 C
ATOM 321 C SER A 144 -45.424-125.860 315.485 1.00118.70 C
ANISOU 321 C SER A 144 14027 10389 20684 926 2266 -2057 C
ATOM 322 O SER A 144 -45.894-124.767 315.148 1.00114.23 O
ANISOU 322 O SER A 144 13419 9536 20446 1029 2279 -1987 O
ATOM 323 CB SER A 144 -43.549-126.653 314.013 1.00102.35 C
ANISOU 323 CB SER A 144 12182 8361 18346 748 2098 -1654 C
ATOM 324 OG SER A 144 -44.051-125.828 312.977 1.00101.68 O
ANISOU 324 OG SER A 144 12083 8003 18546 873 2036 -1345 O
ATOM 325 N ARG A 145 -46.188-126.861 315.938 1.00124.74 N
ANISOU 325 N ARG A 145 14719 11420 21255 983 2265 -2125 N
ATOM 326 CA ARG A 145 -47.618-126.669 316.159 1.00129.05 C
ANISOU 326 CA ARG A 145 15116 11956 21962 1162 2299 -2165 C
ATOM 327 C ARG A 145 -47.878-125.596 317.210 1.00131.51 C
ANISOU 327 C ARG A 145 15329 12156 22484 1155 2457 -2545 C
ATOM 328 O ARG A 145 -48.856-124.847 317.106 1.00137.67 O
ANISOU 328 O ARG A 145 16002 12759 23546 1322 2479 -2540 O
ATOM 329 CB ARG A 145 -48.271-127.988 316.576 1.00131.70 C
ANISOU 329 CB ARG A 145 15384 12622 22033 1186 2290 -2207 C
ATOM 330 CG ARG A 145 -49.774-127.889 316.788 1.00138.30 C
ANISOU 330 CG ARG A 145 16044 13492 23014 1367 2329 -2248 C
ATOM 331 CD ARG A 145 -50.327-129.028 317.634 1.00136.13 C
ANISOU 331 CD ARG A 145 15672 13568 22485 1337 2387 -2427 C
ATOM 332 NE ARG A 145 -49.950-128.902 319.039 1.00133.50 N
ANISOU 332 NE ARG A 145 15297 13402 22026 1186 2547 -2862 N
ATOM 333 CZ ARG A 145 -50.432-129.667 320.013 1.00127.76 C
ANISOU 333 CZ ARG A 145 14454 13003 21087 1134 2641 -3094 C
ATOM 334 NH1 ARG A 145 -50.031-129.482 321.263 1.00124.96 N
ANISOU 334 NH1 ARG A 145 14056 12832 20593 976 2782 -3485 N
ATOM 335 NH2 ARG A 145 -51.318-130.615 319.739 1.00125.81 N
ANISOU 335 NH2 ARG A 145 14120 12926 20757 1226 2598 -2934 N
ATOM 336 N SER A 146 -47.005-125.491 318.216 1.00129.66 N
ANISOU 336 N SER A 146 15118 12026 22119 965 2564 -2886 N
ATOM 337 CA SER A 146 -47.192-124.480 319.254 1.00135.24 C
ANISOU 337 CA SER A 146 15722 12653 23012 936 2718 -3285 C
ATOM 338 C SER A 146 -46.902-123.075 318.741 1.00141.99 C
ANISOU 338 C SER A 146 16612 13087 24252 972 2723 -3225 C
ATOM 339 O SER A 146 -47.317-122.091 319.367 1.00149.57 O
ANISOU 339 O SER A 146 17470 13889 25470 1013 2832 -3504 O
ATOM 340 CB SER A 146 -46.296-124.782 320.453 1.00133.01 C
ANISOU 340 CB SER A 146 15442 12640 22455 703 2822 -3661 C
ATOM 341 OG SER A 146 -44.966-125.039 320.043 1.00130.53 O
ANISOU 341 OG SER A 146 15280 12327 21991 548 2757 -3533 O
ATOM 342 N LEU A 147 -46.184-122.951 317.626 1.00138.00 N
ANISOU 342 N LEU A 147 16241 12394 23796 950 2610 -2877 N
ATOM 343 CA LEU A 147 -45.750-121.634 317.178 1.00136.43 C
ANISOU 343 CA LEU A 147 16088 11799 23951 944 2620 -2818 C
ATOM 344 C LEU A 147 -46.472-121.167 315.920 1.00139.75 C
ANISOU 344 C LEU A 147 16511 11938 24652 1147 2502 -2396 C
ATOM 345 O LEU A 147 -46.872-119.999 315.835 1.00148.98 O
ANISOU 345 O LEU A 147 17632 12771 26202 1247 2534 -2418 O
ATOM 346 CB LEU A 147 -44.233-121.638 316.945 1.00132.76 C
ANISOU 346 CB LEU A 147 15765 11323 23355 724 2604 -2777 C
ATOM 347 CG LEU A 147 -43.299-121.267 318.117 1.00133.62 C
ANISOU 347 CG LEU A 147 15866 11512 23391 505 2742 -3221 C
ATOM 348 CD1 LEU A 147 -43.489-122.155 319.345 1.00131.40 C
ANISOU 348 CD1 LEU A 147 15499 11646 22780 433 2821 -3564 C
ATOM 349 CD2 LEU A 147 -41.836-121.280 317.668 1.00134.21 C
ANISOU 349 CD2 LEU A 147 16078 11563 23355 307 2706 -3115 C
ATOM 350 N ARG A 148 -46.661-122.062 314.949 1.00135.13 N
ANISOU 350 N ARG A 148 15969 11488 23886 1211 2363 -2017 N
ATOM 351 CA ARG A 148 -47.296-121.740 313.677 1.00136.93 C
ANISOU 351 CA ARG A 148 16190 11514 24321 1385 2233 -1580 C
ATOM 352 C ARG A 148 -48.386-122.765 313.397 1.00138.17 C
ANISOU 352 C ARG A 148 16262 11928 24308 1538 2155 -1424 C
ATOM 353 O ARG A 148 -48.133-123.974 313.440 1.00138.02 O
ANISOU 353 O ARG A 148 16281 12216 23945 1463 2118 -1406 O
ATOM 354 CB ARG A 148 -46.276-121.720 312.537 1.00134.39 C
ANISOU 354 CB ARG A 148 16009 11095 23957 1279 2126 -1218 C
ATOM 355 N CYS A 149 -49.593-122.278 313.109 1.00140.30 N
ANISOU 355 N CYS A 149 16411 12065 24833 1755 2127 -1314 N
ATOM 356 CA CYS A 149 -50.750-123.110 312.802 1.00137.36 C
ANISOU 356 CA CYS A 149 15928 11912 24349 1916 2053 -1160 C
ATOM 357 C CYS A 149 -51.053-123.160 311.309 1.00141.53 C
ANISOU 357 C CYS A 149 16467 12373 24933 2027 1876 -645 C
ATOM 358 O CYS A 149 -52.113-123.656 310.917 1.00142.47 O
ANISOU 358 O CYS A 149 16474 12637 25022 2183 1801 -481 O
ATOM 359 CB CYS A 149 -51.980-122.605 313.565 1.00136.54 C
ANISOU 359 CB CYS A 149 15647 11765 24468 2092 2146 -1418 C
ATOM 360 SG CYS A 149 -52.519-120.920 313.137 1.00134.38 S
ANISOU 360 SG CYS A 149 15308 11011 24737 2284 2140 -1318 S
ATOM 361 N ARG A 150 -50.150-122.653 310.470 1.00149.31 N
ANISOU 361 N ARG A 150 17572 13165 25993 1940 1810 -386 N
ATOM 362 CA ARG A 150 -50.373-122.617 309.028 1.00159.37 C
ANISOU 362 CA ARG A 150 18847 14390 27316 2024 1644 119 C
ATOM 363 C ARG A 150 -49.960-123.919 308.343 1.00157.74 C
ANISOU 363 C ARG A 150 18700 14502 26734 1935 1538 335 C
ATOM 364 O ARG A 150 -50.744-124.451 307.547 1.00160.13 O
ANISOU 364 O ARG A 150 18920 14956 26966 2055 1416 621 O
ATOM 365 CB ARG A 150 -49.642-121.426 308.401 1.00170.00 C
ANISOU 365 CB ARG A 150 20278 15381 28933 1968 1621 327 C
ATOM 366 CG ARG A 150 -49.831-121.307 306.896 1.00175.34 C
ANISOU 366 CG ARG A 150 20945 16017 29658 2036 1448 878 C
ATOM 367 CD ARG A 150 -51.307-121.255 306.527 1.00180.74 C
ANISOU 367 CD ARG A 150 21461 16730 30480 2287 1366 1054 C
ATOM 368 NE ARG A 150 -51.510-121.114 305.088 1.00185.60 N
ANISOU 368 NE ARG A 150 22049 17341 31130 2347 1193 1596 N
ATOM 369 CZ ARG A 150 -52.697-121.159 304.492 1.00189.41 C
ANISOU 369 CZ ARG A 150 22383 17902 31684 2547 1083 1849 C
ATOM 370 NH1 ARG A 150 -52.786-121.020 303.176 1.00191.08 N
ANISOU 370 NH1 ARG A 150 22565 18140 31898 2575 921 2354 N
ATOM 371 NH2 ARG A 150 -53.797-121.345 305.210 1.00190.40 N
ANISOU 371 NH2 ARG A 150 22375 18103 31867 2714 1134 1601 N
ATOM 372 N PRO A 151 -48.765-124.466 308.592 1.00157.41 N
ANISOU 372 N PRO A 151 18787 14571 26450 1735 1573 209 N
ATOM 373 CA PRO A 151 -48.402-125.730 307.932 1.00153.52 C
ANISOU 373 CA PRO A 151 18342 14366 25622 1669 1469 398 C
ATOM 374 C PRO A 151 -49.282-126.874 308.416 1.00149.24 C
ANISOU 374 C PRO A 151 17712 14116 24877 1746 1462 261 C
ATOM 375 O PRO A 151 -49.427-127.099 309.620 1.00147.49 O
ANISOU 375 O PRO A 151 17467 13972 24601 1718 1579 -107 O
ATOM 376 CB PRO A 151 -46.935-125.935 308.331 1.00151.95 C
ANISOU 376 CB PRO A 151 18288 14190 25256 1449 1535 212 C
ATOM 377 CG PRO A 151 -46.787-125.178 309.596 1.00153.96 C
ANISOU 377 CG PRO A 151 18540 14298 25660 1402 1693 -191 C
ATOM 378 CD PRO A 151 -47.654-123.970 309.428 1.00157.55 C
ANISOU 378 CD PRO A 151 18905 14464 26491 1558 1700 -103 C
ATOM 379 N SER A 152 -49.870-127.599 307.461 1.00148.25 N
ANISOU 379 N SER A 152 17526 14164 24638 1832 1323 569 N
ATOM 380 CA SER A 152 -50.776-128.689 307.810 1.00146.11 C
ANISOU 380 CA SER A 152 17155 14160 24199 1905 1303 479 C
ATOM 381 C SER A 152 -50.038-129.806 308.537 1.00141.70 C
ANISOU 381 C SER A 152 16688 13804 23347 1754 1349 225 C
ATOM 382 O SER A 152 -50.483-130.275 309.591 1.00141.34 O
ANISOU 382 O SER A 152 16588 13879 23234 1754 1437 -60 O
ATOM 383 CB SER A 152 -51.462-129.226 306.551 1.00144.27 C
ANISOU 383 CB SER A 152 16834 14080 23901 2009 1131 872 C
ATOM 384 OG SER A 152 -50.539-129.893 305.707 1.00139.70 O
ANISOU 384 OG SER A 152 16354 13617 23110 1896 1033 1070 O
ATOM 385 N TYR A 153 -48.906-130.245 307.984 1.00136.73 N
ANISOU 385 N TYR A 153 16186 13217 22547 1627 1290 333 N
ATOM 386 CA TYR A 153 -48.104-131.342 308.527 1.00130.31 C
ANISOU 386 CA TYR A 153 15466 12587 21459 1493 1307 132 C
ATOM 387 C TYR A 153 -48.902-132.635 308.665 1.00122.52 C
ANISOU 387 C TYR A 153 14403 11847 20303 1547 1248 117 C
ATOM 388 O TYR A 153 -48.548-133.502 309.472 1.00117.44 O
ANISOU 388 O TYR A 153 13804 11339 19478 1459 1287 -111 O
ATOM 389 CB TYR A 153 -47.479-130.968 309.877 1.00132.65 C
ANISOU 389 CB TYR A 153 15819 12827 21753 1377 1465 -257 C
ATOM 390 CG TYR A 153 -46.364-129.951 309.789 1.00137.48 C
ANISOU 390 CG TYR A 153 16530 13229 22477 1267 1519 -281 C
ATOM 391 CD1 TYR A 153 -45.553-129.874 308.663 1.00137.70 C
ANISOU 391 CD1 TYR A 153 16635 13198 22487 1213 1431 -5 C
ATOM 392 CD2 TYR A 153 -46.121-129.067 310.833 1.00139.83 C
ANISOU 392 CD2 TYR A 153 16829 13393 22907 1207 1662 -584 C
ATOM 393 CE1 TYR A 153 -44.532-128.945 308.582 1.00138.74 C
ANISOU 393 CE1 TYR A 153 16846 13132 22737 1095 1488 -17 C
ATOM 394 CE2 TYR A 153 -45.104-128.136 310.760 1.00138.55 C
ANISOU 394 CE2 TYR A 153 16747 13031 22864 1093 1712 -612 C
ATOM 395 CZ TYR A 153 -44.313-128.078 309.633 1.00137.49 C
ANISOU 395 CZ TYR A 153 16693 12830 22718 1034 1625 -322 C
ATOM 396 OH TYR A 153 -43.299-127.152 309.560 1.00136.86 O
ANISOU 396 OH TYR A 153 16685 12547 22769 903 1681 -343 O
ATOM 397 N HIS A 154 -49.980-132.786 307.892 1.00119.75 N
ANISOU 397 N HIS A 154 13925 11559 20015 1685 1148 365 N
ATOM 398 CA HIS A 154 -50.770-134.010 307.964 1.00118.63 C
ANISOU 398 CA HIS A 154 13690 11647 19738 1728 1086 364 C
ATOM 399 C HIS A 154 -50.029-135.182 307.334 1.00114.62 C
ANISOU 399 C HIS A 154 13273 11306 18973 1632 959 461 C
ATOM 400 O HIS A 154 -50.098-136.310 307.836 1.00109.75 O
ANISOU 400 O HIS A 154 12681 10918 18101 1535 923 319 O
ATOM 401 CB HIS A 154 -52.124-133.803 307.288 1.00120.39 C
ANISOU 401 CB HIS A 154 13728 11917 20096 1895 1007 600 C
ATOM 402 CG HIS A 154 -53.059-132.932 308.066 1.00122.45 C
ANISOU 402 CG HIS A 154 13868 12079 20577 2002 1126 444 C
ATOM 403 ND1 HIS A 154 -53.835-131.958 307.476 1.00128.44 N
ANISOU 403 ND1 HIS A 154 14518 12723 21560 2151 1089 642 N
ATOM 404 CD2 HIS A 154 -53.347-132.891 309.389 1.00122.85 C
ANISOU 404 CD2 HIS A 154 13877 12141 20661 1986 1281 102 C
ATOM 405 CE1 HIS A 154 -54.557-131.351 308.401 1.00131.56 C
ANISOU 405 CE1 HIS A 154 14813 13045 22130 2233 1215 411 C
ATOM 406 NE2 HIS A 154 -54.280-131.899 309.571 1.00128.56 N
ANISOU 406 NE2 HIS A 154 14465 12753 21630 2131 1339 76 N
ATOM 407 N PHE A 155 -49.313-134.937 306.237 1.00115.24 N
ANISOU 407 N PHE A 155 13418 11359 19008 1600 866 694 N
ATOM 408 CA PHE A 155 -48.587-136.012 305.570 1.00113.34 C
ANISOU 408 CA PHE A 155 13270 11384 18411 1466 726 744 C
ATOM 409 C PHE A 155 -47.313-136.379 306.323 1.00114.19 C
ANISOU 409 C PHE A 155 13534 11500 18352 1315 787 483 C
ATOM 410 O PHE A 155 -47.027-137.564 306.530 1.00113.01 O
ANISOU 410 O PHE A 155 13441 11562 17937 1225 713 366 O
ATOM 411 CB PHE A 155 -48.259-135.612 304.131 1.00115.25 C
ANISOU 411 CB PHE A 155 13501 11660 18630 1471 614 1073 C
ATOM 412 CG PHE A 155 -47.073-136.336 303.558 1.00117.95 C
ANISOU 412 CG PHE A 155 13955 12206 18654 1318 530 1051 C
ATOM 413 CD1 PHE A 155 -45.879-135.671 303.339 1.00120.28 C
ANISOU 413 CD1 PHE A 155 14342 12396 18963 1230 581 1076 C
ATOM 414 CD2 PHE A 155 -47.149-137.685 303.252 1.00123.11 C
ANISOU 414 CD2 PHE A 155 14610 13154 19011 1259 403 987 C
ATOM 415 CE1 PHE A 155 -44.784-136.335 302.816 1.00123.57 C
ANISOU 415 CE1 PHE A 155 14834 13032 19086 1099 511 1033 C
ATOM 416 CE2 PHE A 155 -46.056-138.356 302.732 1.00124.79 C
ANISOU 416 CE2 PHE A 155 14908 13550 18958 1141 330 928 C
ATOM 417 CZ PHE A 155 -44.873-137.679 302.512 1.00125.24 C
ANISOU 417 CZ PHE A 155 15038 13535 19013 1068 386 949 C
ATOM 418 N ILE A 156 -46.534-135.377 306.736 1.00116.04 N
ANISOU 418 N ILE A 156 13833 11501 18756 1284 914 393 N
ATOM 419 CA ILE A 156 -45.249-135.660 307.366 1.00114.58 C
ANISOU 419 CA ILE A 156 13778 11355 18402 1134 961 163 C
ATOM 420 C ILE A 156 -45.445-136.265 308.753 1.00103.88 C
ANISOU 420 C ILE A 156 12431 10078 16960 1095 1033 -132 C
ATOM 421 O ILE A 156 -44.638-137.093 309.196 1.00 92.90 O
ANISOU 421 O ILE A 156 11124 8846 15326 983 996 -277 O
ATOM 422 CB ILE A 156 -44.386-134.385 307.410 1.00127.49 C
ANISOU 422 CB ILE A 156 15467 12726 20246 1086 1077 144 C
ATOM 423 CG1 ILE A 156 -42.961-134.715 307.857 1.00133.44 C
ANISOU 423 CG1 ILE A 156 16335 13579 20788 920 1100 -60 C
ATOM 424 CG2 ILE A 156 -45.007-133.336 308.318 1.00135.86 C
ANISOU 424 CG2 ILE A 156 16473 13547 21599 1150 1230 -7 C
ATOM 425 CD1 ILE A 156 -42.249-135.677 306.932 1.00139.64 C
ANISOU 425 CD1 ILE A 156 17160 14635 21260 853 947 53 C
ATOM 426 N GLY A 157 -46.515-135.883 309.453 1.00102.54 N
ANISOU 426 N GLY A 157 12160 9824 16979 1186 1130 -217 N
ATOM 427 CA GLY A 157 -46.778-136.476 310.752 1.00 99.06 C
ANISOU 427 CA GLY A 157 11704 9517 16420 1128 1199 -472 C
ATOM 428 C GLY A 157 -47.214-137.924 310.648 1.00 95.04 C
ANISOU 428 C GLY A 157 11190 9275 15647 1087 1054 -402 C
ATOM 429 O GLY A 157 -46.766-138.773 311.424 1.00 91.65 O
ANISOU 429 O GLY A 157 10823 8998 15000 973 1036 -542 O
ATOM 430 N SER A 158 -48.089-138.227 309.686 1.00 98.15 N
ANISOU 430 N SER A 158 11505 9726 16063 1172 942 -177 N
ATOM 431 CA SER A 158 -48.525-139.605 309.489 1.00102.93 C
ANISOU 431 CA SER A 158 12104 10561 16445 1118 797 -116 C
ATOM 432 C SER A 158 -47.362-140.496 309.073 1.00 99.17 C
ANISOU 432 C SER A 158 11767 10181 15733 1016 671 -119 C
ATOM 433 O SER A 158 -47.217-141.617 309.576 1.00101.24 O
ANISOU 433 O SER A 158 12080 10572 15815 926 601 -198 O
ATOM 434 CB SER A 158 -49.640-139.657 308.444 1.00109.63 C
ANISOU 434 CB SER A 158 12825 11466 17364 1219 699 115 C
ATOM 435 OG SER A 158 -49.976-140.996 308.121 1.00113.38 O
ANISOU 435 OG SER A 158 13301 12148 17630 1144 548 161 O
ATOM 436 N LEU A 159 -46.520-140.012 308.157 1.00 94.91 N
ANISOU 436 N LEU A 159 11279 9583 15201 1028 640 -28 N
ATOM 437 CA LEU A 159 -45.377-140.802 307.712 1.00 91.09 C
ANISOU 437 CA LEU A 159 10899 9211 14499 947 531 -59 C
ATOM 438 C LEU A 159 -44.397-141.046 308.853 1.00 93.07 C
ANISOU 438 C LEU A 159 11244 9462 14658 857 589 -277 C
ATOM 439 O LEU A 159 -43.835-142.141 308.976 1.00 99.90 O
ANISOU 439 O LEU A 159 12172 10444 15341 800 484 -342 O
ATOM 440 CB LEU A 159 -44.682-140.100 306.546 1.00 93.82 C
ANISOU 440 CB LEU A 159 11254 9531 14862 962 510 82 C
ATOM 441 CG LEU A 159 -43.538-140.859 305.872 1.00 96.70 C
ANISOU 441 CG LEU A 159 11686 10055 14999 893 400 47 C
ATOM 442 CD1 LEU A 159 -44.045-142.149 305.247 1.00 98.54 C
ANISOU 442 CD1 LEU A 159 11891 10472 15077 898 236 74 C
ATOM 443 CD2 LEU A 159 -42.859-139.985 304.830 1.00 99.05 C
ANISOU 443 CD2 LEU A 159 11973 10352 15309 880 413 193 C
ATOM 444 N ALA A 160 -44.185-140.041 309.705 1.00 93.48 N
ANISOU 444 N ALA A 160 11296 9382 14841 845 750 -399 N
ATOM 445 CA ALA A 160 -43.263-140.201 310.825 1.00 89.85 C
ANISOU 445 CA ALA A 160 10904 8964 14272 747 807 -611 C
ATOM 446 C ALA A 160 -43.821-141.162 311.867 1.00 86.13 C
ANISOU 446 C ALA A 160 10420 8626 13680 699 782 -688 C
ATOM 447 O ALA A 160 -43.099-142.030 312.371 1.00 87.32 O
ANISOU 447 O ALA A 160 10635 8893 13649 623 707 -755 O
ATOM 448 CB ALA A 160 -42.958-138.841 311.453 1.00 96.58 C
ANISOU 448 CB ALA A 160 11744 9652 15301 728 992 -752 C
ATOM 449 N VAL A 161 -45.106-141.017 312.208 1.00 88.48 N
ANISOU 449 N VAL A 161 10622 8918 14080 739 842 -665 N
ATOM 450 CA VAL A 161 -45.719-141.906 313.193 1.00 92.94 C
ANISOU 450 CA VAL A 161 11158 9636 14519 666 826 -710 C
ATOM 451 C VAL A 161 -45.663-143.351 312.715 1.00 92.37 C
ANISOU 451 C VAL A 161 11144 9662 14289 628 626 -585 C
ATOM 452 O VAL A 161 -45.342-144.265 313.485 1.00 88.20 O
ANISOU 452 O VAL A 161 10666 9239 13608 534 563 -617 O
ATOM 453 CB VAL A 161 -47.166-141.465 313.487 1.00 96.27 C
ANISOU 453 CB VAL A 161 11436 10059 15083 721 927 -704 C
ATOM 454 CG1 VAL A 161 -47.909-142.556 314.241 1.00 95.94 C
ANISOU 454 CG1 VAL A 161 11353 10211 14889 623 879 -685 C
ATOM 455 CG2 VAL A 161 -47.177-140.172 314.282 1.00101.67 C
ANISOU 455 CG2 VAL A 161 12058 10650 15922 744 1136 -904 C
ATOM 456 N ALA A 162 -45.970-143.579 311.436 1.00 93.04 N
ANISOU 456 N ALA A 162 11218 9716 14417 699 518 -441 N
ATOM 457 CA ALA A 162 -45.919-144.932 310.896 1.00 91.27 C
ANISOU 457 CA ALA A 162 11042 9563 14073 664 330 -366 C
ATOM 458 C ALA A 162 -44.498-145.480 310.918 1.00 88.21 C
ANISOU 458 C ALA A 162 10768 9185 13563 633 247 -444 C
ATOM 459 O ALA A 162 -44.277-146.640 311.284 1.00 83.51 O
ANISOU 459 O ALA A 162 10228 8631 12872 578 128 -448 O
ATOM 460 CB ALA A 162 -46.483-144.950 309.476 1.00 92.72 C
ANISOU 460 CB ALA A 162 11170 9752 14308 737 242 -232 C
ATOM 461 N ASP A 163 -43.519-144.655 310.538 1.00 90.66 N
ANISOU 461 N ASP A 163 11105 9454 13887 668 305 -497 N
ATOM 462 CA ASP A 163 -42.136-145.120 310.509 1.00 93.05 C
ANISOU 462 CA ASP A 163 11486 9796 14072 649 231 -584 C
ATOM 463 C ASP A 163 -41.604-145.368 311.915 1.00 87.36 C
ANISOU 463 C ASP A 163 10803 9121 13267 573 262 -687 C
ATOM 464 O ASP A 163 -40.847-146.319 312.139 1.00 83.37 O
ANISOU 464 O ASP A 163 10350 8667 12659 557 141 -715 O
ATOM 465 CB ASP A 163 -41.257-144.113 309.767 1.00102.70 C
ANISOU 465 CB ASP A 163 12707 10992 15322 676 298 -606 C
ATOM 466 CG ASP A 163 -41.524-144.095 308.272 1.00111.73 C
ANISOU 466 CG ASP A 163 13813 12160 16479 733 225 -483 C
ATOM 467 OD1 ASP A 163 -42.620-144.529 307.854 1.00112.72 O
ANISOU 467 OD1 ASP A 163 13893 12300 16636 761 162 -383 O
ATOM 468 OD2 ASP A 163 -40.639-143.645 307.514 1.00116.27 O
ANISOU 468 OD2 ASP A 163 14389 12773 17015 735 232 -484 O
ATOM 469 N LEU A 164 -41.990-144.528 312.876 1.00 91.47 N
ANISOU 469 N LEU A 164 11283 9638 13831 529 420 -751 N
ATOM 470 CA LEU A 164 -41.560-144.740 314.254 1.00 97.03 C
ANISOU 470 CA LEU A 164 12002 10449 14417 435 453 -849 C
ATOM 471 C LEU A 164 -42.187-146.006 314.825 1.00 95.82 C
ANISOU 471 C LEU A 164 11856 10374 14176 379 336 -746 C
ATOM 472 O LEU A 164 -41.480-146.908 315.290 1.00 94.27 O
ANISOU 472 O LEU A 164 11712 10243 13862 339 215 -726 O
ATOM 473 CB LEU A 164 -41.913-143.521 315.110 1.00102.59 C
ANISOU 473 CB LEU A 164 12640 11153 15185 393 663 -982 C
ATOM 474 CG LEU A 164 -41.066-143.261 316.361 1.00104.74 C
ANISOU 474 CG LEU A 164 12913 11559 15325 286 738 -1152 C
ATOM 475 CD1 LEU A 164 -41.281-141.839 316.844 1.00109.18 C
ANISOU 475 CD1 LEU A 164 13410 12064 16010 264 956 -1339 C
ATOM 476 CD2 LEU A 164 -41.369-144.247 317.483 1.00102.93 C
ANISOU 476 CD2 LEU A 164 12671 11522 14915 187 674 -1108 C
ATOM 477 N LEU A 165 -43.520-146.089 314.798 1.00 98.00 N
ANISOU 477 N LEU A 165 12072 10644 14519 371 364 -664 N
ATOM 478 CA LEU A 165 -44.201-147.273 315.312 1.00 95.38 C
ANISOU 478 CA LEU A 165 11741 10383 14115 286 257 -544 C
ATOM 479 C LEU A 165 -43.787-148.523 314.549 1.00 87.72 C
ANISOU 479 C LEU A 165 10854 9334 13141 315 41 -450 C
ATOM 480 O LEU A 165 -43.531-149.571 315.153 1.00 84.01 O
ANISOU 480 O LEU A 165 10435 8890 12597 246 -83 -376 O
ATOM 481 CB LEU A 165 -45.717-147.087 315.240 1.00 94.12 C
ANISOU 481 CB LEU A 165 11479 10244 14040 275 327 -482 C
ATOM 482 CG LEU A 165 -46.335-145.983 316.098 1.00 91.82 C
ANISOU 482 CG LEU A 165 11075 10037 13774 253 543 -598 C
ATOM 483 CD1 LEU A 165 -47.854-146.005 315.975 1.00 88.97 C
ANISOU 483 CD1 LEU A 165 10591 9721 13493 252 584 -524 C
ATOM 484 CD2 LEU A 165 -45.905-146.120 317.552 1.00 90.28 C
ANISOU 484 CD2 LEU A 165 10878 10023 13400 118 599 -676 C
ATOM 485 N GLY A 166 -43.713-148.429 313.220 1.00 85.37 N
ANISOU 485 N GLY A 166 10563 8945 12927 416 -10 -452 N
ATOM 486 CA GLY A 166 -43.337-149.589 312.429 1.00 89.97 C
ANISOU 486 CA GLY A 166 11206 9461 13516 449 -204 -421 C
ATOM 487 C GLY A 166 -41.952-150.102 312.772 1.00 92.48 C
ANISOU 487 C GLY A 166 11597 9777 13765 471 -295 -484 C
ATOM 488 O GLY A 166 -41.768-151.288 313.057 1.00 96.19 O
ANISOU 488 O GLY A 166 12117 10197 14232 447 -450 -428 O
ATOM 489 N SER A 167 -40.961-149.207 312.769 1.00 91.47 N
ANISOU 489 N SER A 167 11465 9696 13594 513 -203 -594 N
ATOM 490 CA SER A 167 -39.582-149.624 313.003 1.00 93.27 C
ANISOU 490 CA SER A 167 11733 9955 13753 547 -289 -667 C
ATOM 491 C SER A 167 -39.399-150.209 314.399 1.00 90.50 C
ANISOU 491 C SER A 167 11404 9665 13318 465 -338 -602 C
ATOM 492 O SER A 167 -38.715-151.226 314.565 1.00 88.84 O
ANISOU 492 O SER A 167 11231 9426 13097 499 -502 -570 O
ATOM 493 CB SER A 167 -38.634-148.445 312.790 1.00102.19 C
ANISOU 493 CB SER A 167 12835 11147 14845 572 -162 -794 C
ATOM 494 OG SER A 167 -37.292-148.818 313.046 1.00110.53 O
ANISOU 494 OG SER A 167 13903 12270 15822 602 -240 -873 O
ATOM 495 N VAL A 168 -40.000-149.583 315.415 1.00 92.10 N
ANISOU 495 N VAL A 168 11569 9963 13461 360 -201 -583 N
ATOM 496 CA VAL A 168 -39.833-150.064 316.787 1.00 96.47 C
ANISOU 496 CA VAL A 168 12124 10644 13887 255 -238 -508 C
ATOM 497 C VAL A 168 -40.334-151.496 316.913 1.00100.71 C
ANISOU 497 C VAL A 168 12708 11098 14461 220 -427 -315 C
ATOM 498 O VAL A 168 -39.633-152.376 317.425 1.00107.74 O
ANISOU 498 O VAL A 168 13634 11991 15310 218 -581 -224 O
ATOM 499 CB VAL A 168 -40.549-149.133 317.782 1.00 96.36 C
ANISOU 499 CB VAL A 168 12038 10783 13793 136 -40 -554 C
ATOM 500 CG1 VAL A 168 -40.588-149.773 319.160 1.00 94.23 C
ANISOU 500 CG1 VAL A 168 11753 10694 13354 -3 -91 -437 C
ATOM 501 CG2 VAL A 168 -39.851-147.792 317.852 1.00 98.53 C
ANISOU 501 CG2 VAL A 168 12276 11114 14048 152 129 -760 C
ATOM 502 N ILE A 169 -41.555-151.752 316.441 1.00 99.11 N
ANISOU 502 N ILE A 169 12497 10810 14352 190 -425 -239 N
ATOM 503 CA ILE A 169 -42.111-153.097 316.539 1.00 97.53 C
ANISOU 503 CA ILE A 169 12340 10506 14211 125 -599 -57 C
ATOM 504 C ILE A 169 -41.375-154.051 315.605 1.00 97.50 C
ANISOU 504 C ILE A 169 12407 10304 14335 251 -796 -83 C
ATOM 505 O ILE A 169 -41.149-155.219 315.945 1.00102.97 O
ANISOU 505 O ILE A 169 13155 10887 15083 231 -976 46 O
ATOM 506 CB ILE A 169 -43.623-153.073 316.252 1.00 96.67 C
ANISOU 506 CB ILE A 169 12181 10386 14163 45 -539 8 C
ATOM 507 CG1 ILE A 169 -44.303-151.979 317.075 1.00103.11 C
ANISOU 507 CG1 ILE A 169 12898 11405 14873 -41 -320 -29 C
ATOM 508 CG2 ILE A 169 -44.246-154.420 316.574 1.00 93.44 C
ANISOU 508 CG2 ILE A 169 11811 9889 13804 -78 -702 212 C
ATOM 509 CD1 ILE A 169 -45.780-151.821 316.778 1.00105.33 C
ANISOU 509 CD1 ILE A 169 13096 11707 15220 -95 -244 13 C
ATOM 510 N PHE A 170 -40.978-153.571 314.423 1.00 93.16 N
ANISOU 510 N PHE A 170 11846 9709 13841 381 -764 -252 N
ATOM 511 CA PHE A 170 -40.303-154.436 313.458 1.00 89.33 C
ANISOU 511 CA PHE A 170 11401 9074 13465 504 -932 -333 C
ATOM 512 C PHE A 170 -38.956-154.907 313.990 1.00 83.34 C
ANISOU 512 C PHE A 170 10668 8313 12683 580 -1042 -349 C
ATOM 513 O PHE A 170 -38.722-156.110 314.146 1.00 84.36 O
ANISOU 513 O PHE A 170 10845 8287 12920 608 -1232 -270 O
ATOM 514 CB PHE A 170 -40.124-153.707 312.124 1.00 87.02 C
ANISOU 514 CB PHE A 170 11066 8814 13183 604 -855 -506 C
ATOM 515 CG PHE A 170 -39.339-154.489 311.107 1.00 88.94 C
ANISOU 515 CG PHE A 170 11321 8969 13504 731 -1001 -646 C
ATOM 516 CD1 PHE A 170 -39.968-155.416 310.289 1.00 86.32 C
ANISOU 516 CD1 PHE A 170 11000 8504 13292 734 -1123 -672 C
ATOM 517 CD2 PHE A 170 -37.972-154.297 310.965 1.00 87.95 C
ANISOU 517 CD2 PHE A 170 11176 8911 13329 840 -1010 -780 C
ATOM 518 CE1 PHE A 170 -39.251-156.137 309.349 1.00 78.80 C
ANISOU 518 CE1 PHE A 170 10041 7484 12414 853 -1247 -853 C
ATOM 519 CE2 PHE A 170 -37.247-155.017 310.030 1.00 83.71 C
ANISOU 519 CE2 PHE A 170 10623 8322 12862 966 -1134 -944 C
ATOM 520 CZ PHE A 170 -37.888-155.937 309.220 1.00 81.41 C
ANISOU 520 CZ PHE A 170 10345 7894 12695 977 -1249 -993 C
ATOM 521 N VAL A 171 -38.054-153.961 314.266 1.00 80.26 N
ANISOU 521 N VAL A 171 10239 8085 12171 615 -932 -450 N
ATOM 522 CA VAL A 171 -36.700-154.306 314.693 1.00 79.05 C
ANISOU 522 CA VAL A 171 10079 7975 11980 700 -1032 -486 C
ATOM 523 C VAL A 171 -36.733-155.206 315.921 1.00 77.49 C
ANISOU 523 C VAL A 171 9916 7757 11772 629 -1169 -266 C
ATOM 524 O VAL A 171 -35.991-156.194 316.003 1.00 73.35 O
ANISOU 524 O VAL A 171 9409 7126 11336 727 -1360 -221 O
ATOM 525 CB VAL A 171 -35.881-153.026 314.949 1.00 86.84 C
ANISOU 525 CB VAL A 171 11006 9172 12817 694 -867 -619 C
ATOM 526 CG1 VAL A 171 -34.519-153.367 315.536 1.00 88.96 C
ANISOU 526 CG1 VAL A 171 11243 9537 13021 762 -973 -642 C
ATOM 527 CG2 VAL A 171 -35.727-152.230 313.663 1.00 86.19 C
ANISOU 527 CG2 VAL A 171 10891 9096 12760 760 -761 -792 C
ATOM 528 N TYR A 172 -37.599-154.891 316.889 1.00 81.56 N
ANISOU 528 N TYR A 172 10427 8383 12181 459 -1077 -120 N
ATOM 529 CA TYR A 172 -37.694-155.718 318.088 1.00 93.97 C
ANISOU 529 CA TYR A 172 12018 9982 13703 356 -1202 130 C
ATOM 530 C TYR A 172 -38.163-157.127 317.747 1.00102.15 C
ANISOU 530 C TYR A 172 13129 10734 14951 369 -1412 291 C
ATOM 531 O TYR A 172 -37.538-158.116 318.146 1.00100.98 O
ANISOU 531 O TYR A 172 13011 10474 14882 420 -1613 435 O
ATOM 532 CB TYR A 172 -38.631-155.067 319.107 1.00 92.60 C
ANISOU 532 CB TYR A 172 11803 10027 13353 153 -1039 225 C
ATOM 533 CG TYR A 172 -38.736-155.830 320.412 1.00 97.28 C
ANISOU 533 CG TYR A 172 12398 10729 13837 8 -1153 507 C
ATOM 534 CD1 TYR A 172 -37.773-155.685 321.403 1.00 99.78 C
ANISOU 534 CD1 TYR A 172 12668 11275 13968 -14 -1184 554 C
ATOM 535 CD2 TYR A 172 -39.797-156.694 320.652 1.00101.83 C
ANISOU 535 CD2 TYR A 172 13010 11201 14480 -127 -1236 744 C
ATOM 536 CE1 TYR A 172 -37.864-156.380 322.598 1.00105.46 C
ANISOU 536 CE1 TYR A 172 13377 12134 14560 -159 -1299 850 C
ATOM 537 CE2 TYR A 172 -39.897-157.393 321.843 1.00106.73 C
ANISOU 537 CE2 TYR A 172 13627 11938 14988 -284 -1345 1046 C
ATOM 538 CZ TYR A 172 -38.928-157.232 322.812 1.00109.27 C
ANISOU 538 CZ TYR A 172 13902 12504 15113 -296 -1379 1108 C
ATOM 539 OH TYR A 172 -39.022-157.926 323.999 1.00114.34 O
ANISOU 539 OH TYR A 172 14529 13300 15616 -464 -1498 1444 O
ATOM 540 N SER A 173 -39.264-157.238 317.001 1.00104.29 N
ANISOU 540 N SER A 173 13421 10874 15331 322 -1375 268 N
ATOM 541 CA SER A 173 -39.770-158.557 316.634 1.00103.86 C
ANISOU 541 CA SER A 173 13433 10533 15495 308 -1566 389 C
ATOM 542 C SER A 173 -38.811-159.277 315.695 1.00108.75 C
ANISOU 542 C SER A 173 14082 10928 16312 519 -1729 227 C
ATOM 543 O SER A 173 -38.622-160.493 315.809 1.00119.72 O
ANISOU 543 O SER A 173 15526 12067 17894 551 -1940 346 O
ATOM 544 CB SER A 173 -41.153-158.433 315.995 1.00 94.18 C
ANISOU 544 CB SER A 173 12199 9265 14321 202 -1481 366 C
ATOM 545 OG SER A 173 -42.099-157.932 316.923 1.00 88.06 O
ANISOU 545 OG SER A 173 11380 8692 13389 9 -1346 520 O
ATOM 546 N PHE A 174 -38.192-158.543 314.768 1.00101.90 N
ANISOU 546 N PHE A 174 13166 10143 15406 661 -1634 -45 N
ATOM 547 CA PHE A 174 -37.278-159.168 313.818 1.00 97.13 C
ANISOU 547 CA PHE A 174 12559 9383 14964 861 -1766 -247 C
ATOM 548 C PHE A 174 -36.061-159.752 314.526 1.00 99.68 C
ANISOU 548 C PHE A 174 12877 9669 15329 981 -1921 -177 C
ATOM 549 O PHE A 174 -35.640-160.876 314.231 1.00103.81 O
ANISOU 549 O PHE A 174 13424 9937 16082 1107 -2119 -200 O
ATOM 550 CB PHE A 174 -36.849-158.149 312.763 1.00 87.71 C
ANISOU 550 CB PHE A 174 11296 8362 13669 955 -1613 -522 C
ATOM 551 CG PHE A 174 -36.448-158.761 311.455 1.00 92.22 C
ANISOU 551 CG PHE A 174 11844 8807 14388 1106 -1707 -768 C
ATOM 552 CD1 PHE A 174 -37.410-159.195 310.557 1.00 99.45 C
ANISOU 552 CD1 PHE A 174 12776 9598 15411 1059 -1734 -837 C
ATOM 553 CD2 PHE A 174 -35.110-158.890 311.116 1.00 93.05 C
ANISOU 553 CD2 PHE A 174 11890 8954 14509 1289 -1765 -955 C
ATOM 554 CE1 PHE A 174 -37.047-159.755 309.347 1.00102.45 C
ANISOU 554 CE1 PHE A 174 13119 9902 15904 1185 -1814 -1103 C
ATOM 555 CE2 PHE A 174 -34.737-159.449 309.906 1.00 95.03 C
ANISOU 555 CE2 PHE A 174 12097 9129 14881 1427 -1839 -1222 C
ATOM 556 CZ PHE A 174 -35.708-159.882 309.020 1.00101.75 C
ANISOU 556 CZ PHE A 174 12970 9862 15831 1372 -1862 -1305 C
ATOM 557 N ILE A 175 -35.488-159.005 315.470 1.00100.34 N
ANISOU 557 N ILE A 175 12916 10005 15202 945 -1838 -100 N
ATOM 558 CA ILE A 175 -34.325-159.500 316.198 1.00108.82 C
ANISOU 558 CA ILE A 175 13961 11098 16286 1054 -1990 -12 C
ATOM 559 C ILE A 175 -34.735-160.582 317.188 1.00114.43 C
ANISOU 559 C ILE A 175 14737 11642 17099 964 -2178 337 C
ATOM 560 O ILE A 175 -34.022-161.576 317.372 1.00120.37 O
ANISOU 560 O ILE A 175 15495 12208 18032 1102 -2398 431 O
ATOM 561 CB ILE A 175 -33.599-158.334 316.891 1.00111.00 C
ANISOU 561 CB ILE A 175 14156 11733 16285 1016 -1842 -56 C
ATOM 562 CG1 ILE A 175 -33.037-157.375 315.845 1.00108.80 C
ANISOU 562 CG1 ILE A 175 13813 11580 15947 1110 -1686 -379 C
ATOM 563 CG2 ILE A 175 -32.484-158.845 317.789 1.00114.39 C
ANISOU 563 CG2 ILE A 175 14536 12237 16690 1103 -2009 79 C
ATOM 564 CD1 ILE A 175 -32.331-156.196 316.439 1.00108.77 C
ANISOU 564 CD1 ILE A 175 13731 11894 15702 1053 -1533 -451 C
ATOM 565 N ASP A 176 -35.890-160.414 317.838 1.00114.27 N
ANISOU 565 N ASP A 176 14756 11686 16974 733 -2098 546 N
ATOM 566 CA ASP A 176 -36.361-161.435 318.768 1.00115.38 C
ANISOU 566 CA ASP A 176 14955 11690 17194 606 -2271 914 C
ATOM 567 C ASP A 176 -36.694-162.729 318.036 1.00114.64 C
ANISOU 567 C ASP A 176 14943 11153 17461 672 -2468 939 C
ATOM 568 O ASP A 176 -36.426-163.824 318.544 1.00120.04 O
ANISOU 568 O ASP A 176 15672 11606 18332 697 -2697 1189 O
ATOM 569 CB ASP A 176 -37.577-160.923 319.539 1.00116.80 C
ANISOU 569 CB ASP A 176 15134 12081 17164 328 -2116 1094 C
ATOM 570 CG ASP A 176 -37.777-161.639 320.862 1.00120.38 C
ANISOU 570 CG ASP A 176 15604 12584 17553 157 -2254 1510 C
ATOM 571 OD1 ASP A 176 -37.218-162.741 321.040 1.00128.09 O
ANISOU 571 OD1 ASP A 176 16623 13314 18730 246 -2502 1706 O
ATOM 572 OD2 ASP A 176 -38.497-161.098 321.727 1.00116.39 O
ANISOU 572 OD2 ASP A 176 15058 12371 16795 -68 -2115 1645 O
ATOM 573 N PHE A 177 -37.269-162.625 316.835 1.00109.96 N
ANISOU 573 N PHE A 177 14367 10434 16980 699 -2391 681 N
ATOM 574 CA PHE A 177 -37.601-163.825 316.074 1.00112.86 C
ANISOU 574 CA PHE A 177 14802 10390 17690 749 -2567 639 C
ATOM 575 C PHE A 177 -36.350-164.483 315.501 1.00117.84 C
ANISOU 575 C PHE A 177 15412 10809 18552 1035 -2734 442 C
ATOM 576 O PHE A 177 -36.232-165.714 315.508 1.00121.41 O
ANISOU 576 O PHE A 177 15905 10966 19259 1077 -2918 527 O
ATOM 577 CB PHE A 177 -38.586-163.481 314.956 1.00109.33 C
ANISOU 577 CB PHE A 177 14353 9934 17255 681 -2433 406 C
ATOM 578 CG PHE A 177 -38.969-164.656 314.101 1.00114.04 C
ANISOU 578 CG PHE A 177 15004 10139 18186 708 -2597 302 C
ATOM 579 CD1 PHE A 177 -40.029-165.473 314.457 1.00117.06 C
ANISOU 579 CD1 PHE A 177 15453 10325 18700 494 -2680 540 C
ATOM 580 CD2 PHE A 177 -38.272-164.940 312.938 1.00113.27 C
ANISOU 580 CD2 PHE A 177 14850 10034 18153 899 -2596 -59 C
ATOM 581 CE1 PHE A 177 -40.384-166.551 313.670 1.00117.77 C
ANISOU 581 CE1 PHE A 177 15552 10223 18973 477 -2748 400 C
ATOM 582 CE2 PHE A 177 -38.619-166.018 312.150 1.00113.13 C
ANISOU 582 CE2 PHE A 177 14837 9835 18312 883 -2666 -199 C
ATOM 583 CZ PHE A 177 -39.677-166.824 312.515 1.00116.66 C
ANISOU 583 CZ PHE A 177 15355 10078 18895 677 -2744 22 C
ATOM 584 N HIS A 178 -35.409-163.684 314.999 1.00114.19 N
ANISOU 584 N HIS A 178 14861 10576 17951 1205 -2627 161 N
ATOM 585 CA HIS A 178 -34.224-164.227 314.341 1.00111.71 C
ANISOU 585 CA HIS A 178 14489 10137 17819 1477 -2747 -87 C
ATOM 586 C HIS A 178 -33.102-164.523 315.333 1.00111.76 C
ANISOU 586 C HIS A 178 14455 10160 17849 1614 -2905 106 C
ATOM 587 O HIS A 178 -32.652-165.665 315.445 1.00124.84 O
ANISOU 587 O HIS A 178 16110 11630 19693 1698 -3058 175 O
ATOM 588 CB HIS A 178 -33.740-163.265 313.250 1.00110.01 C
ANISOU 588 CB HIS A 178 14180 10161 17456 1590 -2575 -478 C
ATOM 589 CG HIS A 178 -34.539-163.338 311.984 1.00113.27 C
ANISOU 589 CG HIS A 178 14594 10568 17875 1516 -2469 -714 C
ATOM 590 ND1 HIS A 178 -35.899-163.117 311.949 1.00116.38 N
ANISOU 590 ND1 HIS A 178 15056 10911 18252 1316 -2403 -603 N
ATOM 591 CD2 HIS A 178 -34.169-163.608 310.710 1.00114.86 C
ANISOU 591 CD2 HIS A 178 14720 10828 18094 1615 -2434 -1051 C
ATOM 592 CE1 HIS A 178 -36.333-163.250 310.708 1.00116.94 C
ANISOU 592 CE1 HIS A 178 15094 11006 18331 1304 -2342 -855 C
ATOM 593 NE2 HIS A 178 -35.303-163.548 309.936 1.00115.55 N
ANISOU 593 NE2 HIS A 178 14833 10899 18172 1479 -2361 -1128 N
ATOM 594 N VAL A 179 -32.643-163.507 316.061 1.00104.68 N
ANISOU 594 N VAL A 179 13493 9650 16630 1559 -2775 178 N
ATOM 595 CA VAL A 179 -31.473-163.695 316.913 1.00106.02 C
ANISOU 595 CA VAL A 179 13587 9926 16768 1690 -2910 320 C
ATOM 596 C VAL A 179 -31.832-164.499 318.158 1.00104.49 C
ANISOU 596 C VAL A 179 13461 9602 16637 1570 -3094 793 C
ATOM 597 O VAL A 179 -31.037-165.321 318.632 1.00108.26 O
ANISOU 597 O VAL A 179 13908 9937 17289 1728 -3324 966 O
ATOM 598 CB VAL A 179 -30.851-162.334 317.271 1.00106.93 C
ANISOU 598 CB VAL A 179 13600 10515 16512 1647 -2710 215 C
ATOM 599 CG1 VAL A 179 -29.538-162.526 318.012 1.00106.33 C
ANISOU 599 CG1 VAL A 179 13416 10588 16399 1800 -2854 309 C
ATOM 600 CG2 VAL A 179 -30.640-161.505 316.012 1.00104.48 C
ANISOU 600 CG2 VAL A 179 13235 10325 16138 1719 -2519 -198 C
ATOM 601 N PHE A 180 -33.030-164.286 318.705 1.00101.79 N
ANISOU 601 N PHE A 180 13197 9320 16157 1288 -3002 1023 N
ATOM 602 CA PHE A 180 -33.444-164.961 319.929 1.00108.37 C
ANISOU 602 CA PHE A 180 14083 10103 16991 1120 -3154 1501 C
ATOM 603 C PHE A 180 -34.303-166.194 319.683 1.00114.96 C
ANISOU 603 C PHE A 180 15038 10461 18179 1054 -3325 1683 C
ATOM 604 O PHE A 180 -34.503-166.981 320.615 1.00116.24 O
ANISOU 604 O PHE A 180 15246 10500 18418 943 -3505 2113 O
ATOM 605 CB PHE A 180 -34.201-163.990 320.844 1.00105.68 C
ANISOU 605 CB PHE A 180 13727 10177 16251 825 -2948 1660 C
ATOM 606 CG PHE A 180 -33.334-162.913 321.429 1.00102.58 C
ANISOU 606 CG PHE A 180 13216 10245 15516 843 -2821 1565 C
ATOM 607 CD1 PHE A 180 -33.159-161.709 320.767 1.00101.63 C
ANISOU 607 CD1 PHE A 180 13041 10340 15234 879 -2579 1182 C
ATOM 608 CD2 PHE A 180 -32.690-163.108 322.640 1.00 99.44 C
ANISOU 608 CD2 PHE A 180 12755 10068 14959 811 -2951 1869 C
ATOM 609 CE1 PHE A 180 -32.358-160.719 321.304 1.00100.54 C
ANISOU 609 CE1 PHE A 180 12796 10601 14804 874 -2462 1079 C
ATOM 610 CE2 PHE A 180 -31.889-162.122 323.182 1.00 98.89 C
ANISOU 610 CE2 PHE A 180 12566 10440 14568 807 -2836 1754 C
ATOM 611 CZ PHE A 180 -31.722-160.926 322.514 1.00 99.67 C
ANISOU 611 CZ PHE A 180 12619 10722 14531 835 -2587 1346 C
ATOM 612 N HIS A 181 -34.807-166.381 318.460 1.00122.63 N
ANISOU 612 N HIS A 181 16055 11177 19360 1103 -3277 1375 N
ATOM 613 CA HIS A 181 -35.577-167.569 318.083 1.00130.53 C
ANISOU 613 CA HIS A 181 17131 11856 20607 999 -3345 1420 C
ATOM 614 C HIS A 181 -36.807-167.744 318.975 1.00132.45 C
ANISOU 614 C HIS A 181 17456 12071 20798 677 -3369 1843 C
ATOM 615 O HIS A 181 -37.019-168.795 319.583 1.00135.25 O
ANISOU 615 O HIS A 181 17853 12254 21282 570 -3511 2155 O
ATOM 616 CB HIS A 181 -34.703-168.828 318.111 1.00139.97 C
ANISOU 616 CB HIS A 181 18307 12832 22042 1169 -3519 1447 C
ATOM 617 CG HIS A 181 -33.250-168.567 317.862 1.00141.41 C
ANISOU 617 CG HIS A 181 18382 13137 22210 1467 -3542 1214 C
ATOM 618 ND1 HIS A 181 -32.743-168.308 316.607 1.00137.70 N
ANISOU 618 ND1 HIS A 181 17841 12716 21760 1646 -3430 728 N
ATOM 619 CD2 HIS A 181 -32.193-168.530 318.708 1.00145.22 C
ANISOU 619 CD2 HIS A 181 18796 13738 22641 1605 -3667 1409 C
ATOM 620 CE1 HIS A 181 -31.437-168.121 316.691 1.00139.76 C
ANISOU 620 CE1 HIS A 181 17997 13112 21993 1878 -3476 623 C
ATOM 621 NE2 HIS A 181 -31.079-168.250 317.956 1.00144.04 N
ANISOU 621 NE2 HIS A 181 18536 13693 22499 1868 -3623 1025 N
ATOM 622 N ARG A 182 -37.629-166.700 319.048 1.00132.82 N
ANISOU 622 N ARG A 182 17495 12383 20589 497 -3172 1820 N
ATOM 623 CA ARG A 182 -38.820-166.743 319.887 1.00133.69 C
ANISOU 623 CA ARG A 182 17636 12607 20554 163 -3124 2166 C
ATOM 624 C ARG A 182 -39.970-167.398 319.132 1.00132.87 C
ANISOU 624 C ARG A 182 17606 12178 20702 27 -3148 2116 C
ATOM 625 O ARG A 182 -40.278-167.018 317.997 1.00132.91 O
ANISOU 625 O ARG A 182 17595 12158 20748 96 -3029 1741 O
ATOM 626 CB ARG A 182 -39.217-165.338 320.340 1.00132.44 C
ANISOU 626 CB ARG A 182 17390 12978 19952 21 -2839 2097 C
ATOM 627 CG ARG A 182 -39.624-165.268 321.806 1.00137.02 C
ANISOU 627 CG ARG A 182 17942 13860 20260 -244 -2827 2515 C
ATOM 628 CD ARG A 182 -40.427-164.016 322.122 1.00136.41 C
ANISOU 628 CD ARG A 182 17780 14231 19817 -428 -2531 2405 C
ATOM 629 NE ARG A 182 -40.574-163.821 323.562 1.00140.45 N
ANISOU 629 NE ARG A 182 18230 15123 20011 -653 -2500 2733 N
ATOM 630 CZ ARG A 182 -41.429-162.971 324.121 1.00141.91 C
ANISOU 630 CZ ARG A 182 18331 15701 19889 -869 -2271 2721 C
ATOM 631 NH1 ARG A 182 -42.231-162.236 323.362 1.00140.41 N
ANISOU 631 NH1 ARG A 182 18113 15542 19695 -876 -2063 2424 N
ATOM 632 NH2 ARG A 182 -41.488-162.860 325.442 1.00142.78 N
ANISOU 632 NH2 ARG A 182 18369 16188 19692 -1077 -2254 3003 N
ATOM 633 N LYS A 183 -40.605-168.381 319.766 1.00132.35 N
ANISOU 633 N LYS A 183 17594 11947 20748 -187 -3275 2477 N
ATOM 634 CA LYS A 183 -41.747-169.089 319.199 1.00134.35 C
ANISOU 634 CA LYS A 183 17879 12016 21153 -366 -3255 2422 C
ATOM 635 C LYS A 183 -43.007-168.604 319.907 1.00130.21 C
ANISOU 635 C LYS A 183 17352 11685 20437 -718 -3163 2726 C
ATOM 636 O LYS A 183 -43.255-168.966 321.062 1.00133.68 O
ANISOU 636 O LYS A 183 17801 12208 20782 -935 -3238 3173 O
ATOM 637 CB LYS A 183 -41.581-170.600 319.341 1.00142.74 C
ANISOU 637 CB LYS A 183 18983 12771 22480 -365 -3439 2570 C
ATOM 638 N ASP A 184 -43.794-167.789 319.218 1.00126.27 N
ANISOU 638 N ASP A 184 16802 11361 19815 -775 -2961 2453 N
ATOM 639 CA ASP A 184 -45.032-167.254 319.761 1.00131.38 C
ANISOU 639 CA ASP A 184 17378 12351 20191 -1075 -2781 2604 C
ATOM 640 C ASP A 184 -46.230-168.035 319.232 1.00132.52 C
ANISOU 640 C ASP A 184 17554 12235 20563 -1294 -2838 2640 C
ATOM 641 O ASP A 184 -46.170-168.681 318.183 1.00133.17 O
ANISOU 641 O ASP A 184 17681 11991 20925 -1175 -2928 2386 O
ATOM 642 CB ASP A 184 -45.179-165.770 319.414 1.00132.82 C
ANISOU 642 CB ASP A 184 17449 12953 20064 -991 -2496 2280 C
ATOM 643 CG ASP A 184 -44.088-164.914 320.031 1.00135.67 C
ANISOU 643 CG ASP A 184 17765 13608 20174 -829 -2417 2242 C
ATOM 644 OD1 ASP A 184 -43.716-165.169 321.196 1.00139.18 O
ANISOU 644 OD1 ASP A 184 18211 14173 20496 -923 -2496 2566 O
ATOM 645 OD2 ASP A 184 -43.601-163.986 319.350 1.00132.23 O
ANISOU 645 OD2 ASP A 184 17287 13298 19658 -626 -2280 1896 O
ATOM 646 N SER A 185 -47.327-167.970 319.984 1.00130.29 N
ANISOU 646 N SER A 185 17214 12193 20097 -1618 -2751 2912 N
ATOM 647 CA SER A 185 -48.577-168.557 319.530 1.00128.00 C
ANISOU 647 CA SER A 185 16919 11748 19967 -1865 -2770 2939 C
ATOM 648 C SER A 185 -49.062-167.844 318.271 1.00118.58 C
ANISOU 648 C SER A 185 15652 10647 18756 -1748 -2611 2487 C
ATOM 649 O SER A 185 -48.595-166.757 317.921 1.00116.87 O
ANISOU 649 O SER A 185 15375 10681 18350 -1526 -2452 2212 O
ATOM 650 CB SER A 185 -49.637-168.476 320.628 1.00132.79 C
ANISOU 650 CB SER A 185 17440 12695 20319 -2235 -2675 3303 C
ATOM 651 OG SER A 185 -49.196-169.122 321.809 1.00142.04 O
ANISOU 651 OG SER A 185 18668 13830 21470 -2365 -2827 3761 O
ATOM 652 N ARG A 186 -50.016-168.475 317.583 1.00117.88 N
ANISOU 652 N ARG A 186 15562 10357 18869 -1916 -2665 2425 N
ATOM 653 CA ARG A 186 -50.503-167.923 316.322 1.00118.00 C
ANISOU 653 CA ARG A 186 15498 10458 18879 -1819 -2549 2020 C
ATOM 654 C ARG A 186 -51.090-166.530 316.517 1.00116.67 C
ANISOU 654 C ARG A 186 15171 10817 18341 -1826 -2277 1946 C
ATOM 655 O ARG A 186 -50.721-165.584 315.812 1.00116.10 O
ANISOU 655 O ARG A 186 15048 10903 18162 -1587 -2153 1643 O
ATOM 656 CB ARG A 186 -51.540-168.855 315.698 1.00121.37 C
ANISOU 656 CB ARG A 186 15927 10636 19552 -2055 -2653 1999 C
ATOM 657 CG ARG A 186 -52.422-168.162 314.673 1.00118.96 C
ANISOU 657 CG ARG A 186 15482 10583 19134 -2055 -2501 1687 C
ATOM 658 CD ARG A 186 -53.080-169.153 313.739 1.00124.30 C
ANISOU 658 CD ARG A 186 16173 10963 20092 -2200 -2638 1533 C
ATOM 659 NE ARG A 186 -53.813-170.190 314.459 1.00132.19 N
ANISOU 659 NE ARG A 186 17198 11874 21155 -2496 -2706 1838 N
ATOM 660 CZ ARG A 186 -55.092-170.097 314.805 1.00136.54 C
ANISOU 660 CZ ARG A 186 17633 12635 21612 -2829 -2637 2020 C
ATOM 661 NH1 ARG A 186 -55.786-169.009 314.501 1.00134.34 N
ANISOU 661 NH1 ARG A 186 17184 12745 21114 -2844 -2462 1897 N
ATOM 662 NH2 ARG A 186 -55.679-171.093 315.456 1.00143.45 N
ANISOU 662 NH2 ARG A 186 18537 13428 22539 -3092 -2700 2296 N
ATOM 663 N ASN A 187 -52.008-166.386 317.475 1.00113.46 N
ANISOU 663 N ASN A 187 14676 10689 17745 -2101 -2180 2220 N
ATOM 664 CA ASN A 187 -52.653-165.094 317.683 1.00104.69 C
ANISOU 664 CA ASN A 187 13394 10062 16320 -2104 -1920 2127 C
ATOM 665 C ASN A 187 -51.666-164.057 318.205 1.00100.46 C
ANISOU 665 C ASN A 187 12852 9753 15563 -1881 -1793 2056 C
ATOM 666 O ASN A 187 -51.738-162.881 317.828 1.00100.39 O
ANISOU 666 O ASN A 187 12745 9992 15406 -1724 -1605 1814 O
ATOM 667 CB ASN A 187 -53.835-165.247 318.639 1.00102.32 C
ANISOU 667 CB ASN A 187 12980 10029 15867 -2457 -1845 2420 C
ATOM 668 CG ASN A 187 -54.942-166.114 318.066 1.00 98.01 C
ANISOU 668 CG ASN A 187 12405 9319 15516 -2703 -1937 2457 C
ATOM 669 OD1 ASN A 187 -55.179-166.120 316.857 1.00 93.68 O
ANISOU 669 OD1 ASN A 187 11841 8638 15116 -2599 -1961 2177 O
ATOM 670 ND2 ASN A 187 -55.626-166.850 318.932 1.00 98.92 N
ANISOU 670 ND2 ASN A 187 12501 9468 15618 -3051 -1990 2808 N
ATOM 671 N VAL A 188 -50.734-164.472 319.068 1.00 97.54 N
ANISOU 671 N VAL A 188 12582 9300 15180 -1868 -1903 2269 N
ATOM 672 CA VAL A 188 -49.739-163.537 319.584 1.00 93.67 C
ANISOU 672 CA VAL A 188 12079 9033 14477 -1676 -1796 2191 C
ATOM 673 C VAL A 188 -48.779-163.106 318.482 1.00 90.69 C
ANISOU 673 C VAL A 188 11754 8491 14214 -1343 -1805 1844 C
ATOM 674 O VAL A 188 -48.312-161.960 318.469 1.00 82.96 O
ANISOU 674 O VAL A 188 10718 7745 13059 -1179 -1641 1652 O
ATOM 675 CB VAL A 188 -48.987-164.159 320.775 1.00 96.65 C
ANISOU 675 CB VAL A 188 12530 9391 14800 -1757 -1935 2530 C
ATOM 676 CG1 VAL A 188 -47.982-163.168 321.350 1.00 98.75 C
ANISOU 676 CG1 VAL A 188 12762 9937 14820 -1585 -1820 2432 C
ATOM 677 CG2 VAL A 188 -49.972-164.605 321.841 1.00 94.31 C
ANISOU 677 CG2 VAL A 188 12170 9297 14365 -2122 -1925 2900 C
ATOM 678 N PHE A 189 -48.467-164.002 317.544 1.00 96.80 N
ANISOU 678 N PHE A 189 12627 8871 15284 -1249 -1990 1745 N
ATOM 679 CA PHE A 189 -47.624-163.617 316.417 1.00 97.16 C
ANISOU 679 CA PHE A 189 12695 8806 15413 -954 -1989 1398 C
ATOM 680 C PHE A 189 -48.404-162.776 315.415 1.00 93.87 C
ANISOU 680 C PHE A 189 12173 8563 14930 -918 -1827 1140 C
ATOM 681 O PHE A 189 -47.928-161.725 314.970 1.00 89.34 O
ANISOU 681 O PHE A 189 11553 8158 14234 -728 -1693 926 O
ATOM 682 CB PHE A 189 -47.043-164.858 315.742 1.00 99.90 C
ANISOU 682 CB PHE A 189 13159 8702 16096 -862 -2233 1335 C
ATOM 683 CG PHE A 189 -46.249-164.554 314.505 1.00 95.13 C
ANISOU 683 CG PHE A 189 12556 8021 15568 -584 -2231 954 C
ATOM 684 CD1 PHE A 189 -44.933-164.128 314.596 1.00 91.51 C
ANISOU 684 CD1 PHE A 189 12114 7609 15047 -348 -2226 852 C
ATOM 685 CD2 PHE A 189 -46.820-164.689 313.249 1.00 91.26 C
ANISOU 685 CD2 PHE A 189 12032 7456 15187 -575 -2233 697 C
ATOM 686 CE1 PHE A 189 -44.201-163.844 313.457 1.00 86.96 C
ANISOU 686 CE1 PHE A 189 11519 7003 14517 -114 -2215 507 C
ATOM 687 CE2 PHE A 189 -46.097-164.407 312.108 1.00 85.59 C
ANISOU 687 CE2 PHE A 189 11296 6723 14500 -341 -2227 354 C
ATOM 688 CZ PHE A 189 -44.785-163.984 312.210 1.00 83.60 C
ANISOU 688 CZ PHE A 189 11060 6517 14185 -113 -2214 261 C
ATOM 689 N LEU A 190 -49.612-163.224 315.048 1.00 94.84 N
ANISOU 689 N LEU A 190 12249 8651 15134 -1108 -1845 1175 N
ATOM 690 CA LEU A 190 -50.445-162.441 314.139 1.00 97.40 C
ANISOU 690 CA LEU A 190 12449 9173 15386 -1082 -1706 972 C
ATOM 691 C LEU A 190 -50.800-161.085 314.734 1.00101.17 C
ANISOU 691 C LEU A 190 12803 10035 15604 -1068 -1466 989 C
ATOM 692 O LEU A 190 -51.083-160.138 313.992 1.00 95.13 O
ANISOU 692 O LEU A 190 11942 9431 14774 -947 -1337 804 O
ATOM 693 CB LEU A 190 -51.709-163.220 313.781 1.00 98.22 C
ANISOU 693 CB LEU A 190 12504 9203 15611 -1320 -1777 1031 C
ATOM 694 CG LEU A 190 -51.513-164.397 312.825 1.00 98.12 C
ANISOU 694 CG LEU A 190 12583 8815 15883 -1316 -1989 891 C
ATOM 695 CD1 LEU A 190 -52.830-165.116 312.600 1.00102.99 C
ANISOU 695 CD1 LEU A 190 13138 9390 16603 -1597 -2046 960 C
ATOM 696 CD2 LEU A 190 -50.924-163.924 311.503 1.00 91.35 C
ANISOU 696 CD2 LEU A 190 11707 7969 15034 -1061 -1973 539 C
ATOM 697 N PHE A 191 -50.796-160.972 316.064 1.00108.37 N
ANISOU 697 N PHE A 191 13704 11100 16370 -1192 -1407 1208 N
ATOM 698 CA PHE A 191 -50.913-159.662 316.693 1.00110.45 C
ANISOU 698 CA PHE A 191 13856 11711 16401 -1150 -1176 1166 C
ATOM 699 C PHE A 191 -49.700-158.801 316.362 1.00104.27 C
ANISOU 699 C PHE A 191 13117 10926 15575 -884 -1117 961 C
ATOM 700 O PHE A 191 -49.837-157.645 315.944 1.00106.83 O
ANISOU 700 O PHE A 191 13353 11406 15830 -758 -951 786 O
ATOM 701 CB PHE A 191 -51.069-159.819 318.206 1.00118.74 C
ANISOU 701 CB PHE A 191 14881 12957 17279 -1358 -1137 1422 C
ATOM 702 CG PHE A 191 -51.455-158.551 318.915 1.00125.46 C
ANISOU 702 CG PHE A 191 15582 14192 17895 -1364 -886 1349 C
ATOM 703 CD1 PHE A 191 -50.489-157.647 319.330 1.00127.52 C
ANISOU 703 CD1 PHE A 191 15854 14570 18028 -1209 -781 1223 C
ATOM 704 CD2 PHE A 191 -52.787-158.267 319.173 1.00127.33 C
ANISOU 704 CD2 PHE A 191 15653 14676 18052 -1527 -752 1383 C
ATOM 705 CE1 PHE A 191 -50.844-156.481 319.982 1.00127.05 C
ANISOU 705 CE1 PHE A 191 15654 14836 17783 -1216 -547 1113 C
ATOM 706 CE2 PHE A 191 -53.148-157.104 319.827 1.00128.52 C
ANISOU 706 CE2 PHE A 191 15650 15166 18015 -1514 -516 1275 C
ATOM 707 CZ PHE A 191 -52.175-156.209 320.232 1.00128.98 C
ANISOU 707 CZ PHE A 191 15732 15308 17966 -1358 -413 1131 C
ATOM 708 N LYS A 192 -48.499-159.356 316.540 1.00 92.78 N
ANISOU 708 N LYS A 192 11787 9289 14176 -796 -1257 989 N
ATOM 709 CA LYS A 192 -47.283-158.612 316.229 1.00 83.84 C
ANISOU 709 CA LYS A 192 10687 8168 13001 -562 -1210 796 C
ATOM 710 C LYS A 192 -47.161-158.365 314.730 1.00 83.21 C
ANISOU 710 C LYS A 192 10602 7977 13035 -389 -1219 551 C
ATOM 711 O LYS A 192 -46.881-157.240 314.297 1.00 81.13 O
ANISOU 711 O LYS A 192 10287 7847 12693 -252 -1076 387 O
ATOM 712 CB LYS A 192 -46.060-159.360 316.758 1.00 78.14 C
ANISOU 712 CB LYS A 192 10075 7293 12320 -507 -1376 893 C
ATOM 713 CG LYS A 192 -46.066-159.550 318.265 1.00 85.75 C
ANISOU 713 CG LYS A 192 11032 8422 13128 -680 -1376 1162 C
ATOM 714 CD LYS A 192 -44.841-160.316 318.738 1.00 91.82 C
ANISOU 714 CD LYS A 192 11897 9039 13953 -606 -1567 1287 C
ATOM 715 CE LYS A 192 -44.896-160.560 320.239 1.00 96.33 C
ANISOU 715 CE LYS A 192 12448 9813 14339 -804 -1586 1601 C
ATOM 716 NZ LYS A 192 -43.731-161.351 320.720 1.00102.59 N
ANISOU 716 NZ LYS A 192 13320 10461 15197 -726 -1798 1772 N
ATOM 717 N LEU A 193 -47.374-159.409 313.921 1.00 82.29 N
ANISOU 717 N LEU A 193 10534 7626 13106 -406 -1387 524 N
ATOM 718 CA LEU A 193 -47.301-159.245 312.473 1.00 82.29 C
ANISOU 718 CA LEU A 193 10512 7575 13181 -267 -1402 283 C
ATOM 719 C LEU A 193 -48.350-158.258 311.981 1.00 81.88 C
ANISOU 719 C LEU A 193 10327 7747 13035 -290 -1239 237 C
ATOM 720 O LEU A 193 -48.091-157.474 311.060 1.00 72.92 O
ANISOU 720 O LEU A 193 9146 6699 11863 -143 -1169 73 O
ATOM 721 CB LEU A 193 -47.465-160.599 311.778 1.00 85.28 C
ANISOU 721 CB LEU A 193 10949 7676 13777 -316 -1608 237 C
ATOM 722 CG LEU A 193 -47.094-160.683 310.291 1.00 81.69 C
ANISOU 722 CG LEU A 193 10478 7163 13396 -167 -1663 -52 C
ATOM 723 CD1 LEU A 193 -48.239-160.241 309.382 1.00 75.84 C
ANISOU 723 CD1 LEU A 193 9619 6597 12601 -232 -1590 -126 C
ATOM 724 CD2 LEU A 193 -45.842-159.861 310.009 1.00 78.88 C
ANISOU 724 CD2 LEU A 193 10125 6909 12937 54 -1590 -205 C
ATOM 725 N GLY A 194 -49.542-158.283 312.578 1.00 89.24 N
ANISOU 725 N GLY A 194 11184 8790 13933 -473 -1181 393 N
ATOM 726 CA GLY A 194 -50.551-157.301 312.220 1.00 95.15 C
ANISOU 726 CA GLY A 194 11783 9762 14608 -473 -1025 360 C
ATOM 727 C GLY A 194 -50.127-155.886 312.563 1.00 96.48 C
ANISOU 727 C GLY A 194 11904 10099 14655 -335 -832 301 C
ATOM 728 O GLY A 194 -50.434-154.941 311.833 1.00 97.53 O
ANISOU 728 O GLY A 194 11945 10337 14777 -225 -732 212 O
ATOM 729 N GLY A 195 -49.403-155.724 313.672 1.00 94.44 N
ANISOU 729 N GLY A 195 11703 9867 14313 -345 -786 353 N
ATOM 730 CA GLY A 195 -48.974-154.393 314.073 1.00 94.21 C
ANISOU 730 CA GLY A 195 11629 9983 14182 -238 -599 267 C
ATOM 731 C GLY A 195 -48.002-153.773 313.089 1.00 95.09 C
ANISOU 731 C GLY A 195 11780 10028 14323 -39 -593 104 C
ATOM 732 O GLY A 195 -48.164-152.621 312.677 1.00 98.92 O
ANISOU 732 O GLY A 195 12189 10596 14801 58 -454 27 O
ATOM 733 N VAL A 196 -46.979-154.531 312.692 1.00 96.73 N
ANISOU 733 N VAL A 196 12096 10083 14574 22 -745 56 N
ATOM 734 CA VAL A 196 -45.994-154.002 311.755 1.00 99.47 C
ANISOU 734 CA VAL A 196 12464 10406 14923 192 -738 -103 C
ATOM 735 C VAL A 196 -46.611-153.815 310.373 1.00 97.62 C
ANISOU 735 C VAL A 196 12161 10194 14737 243 -751 -167 C
ATOM 736 O VAL A 196 -46.345-152.817 309.692 1.00 99.43 O
ANISOU 736 O VAL A 196 12344 10501 14934 349 -658 -236 O
ATOM 737 CB VAL A 196 -44.752-154.913 311.707 1.00104.11 C
ANISOU 737 CB VAL A 196 13157 10853 15547 255 -898 -161 C
ATOM 738 CG1 VAL A 196 -43.946-154.772 312.985 1.00109.50 C
ANISOU 738 CG1 VAL A 196 13881 11578 16144 237 -867 -103 C
ATOM 739 CG2 VAL A 196 -45.154-156.362 311.498 1.00102.33 C
ANISOU 739 CG2 VAL A 196 12981 10448 15451 179 -1090 -109 C
ATOM 740 N THR A 197 -47.453-154.758 309.942 1.00 96.66 N
ANISOU 740 N THR A 197 12023 10016 14687 154 -869 -132 N
ATOM 741 CA THR A 197 -48.048-154.674 308.611 1.00 89.91 C
ANISOU 741 CA THR A 197 11086 9225 13852 184 -901 -197 C
ATOM 742 C THR A 197 -48.904-153.421 308.469 1.00 95.86 C
ANISOU 742 C THR A 197 11710 10150 14565 213 -742 -129 C
ATOM 743 O THR A 197 -48.808-152.699 307.470 1.00 94.02 O
ANISOU 743 O THR A 197 11416 10004 14304 315 -709 -171 O
ATOM 744 CB THR A 197 -48.877-155.927 308.327 1.00 81.46 C
ANISOU 744 CB THR A 197 10010 8071 12870 48 -1052 -181 C
ATOM 745 OG1 THR A 197 -48.031-157.084 308.382 1.00 82.86 O
ANISOU 745 OG1 THR A 197 10308 8039 13136 48 -1210 -257 O
ATOM 746 CG2 THR A 197 -49.518-155.842 306.953 1.00 47.25 C
ANISOU 746 CG2 THR A 197 5571 3856 8526 63 -1089 -263 C
ATOM 747 N ALA A 198 -49.747-153.143 309.468 1.00 95.70 N
ANISOU 747 N ALA A 198 11631 10185 14543 127 -643 -18 N
ATOM 748 CA ALA A 198 -50.584-151.948 309.421 1.00 94.82 C
ANISOU 748 CA ALA A 198 11380 10213 14433 179 -489 30 C
ATOM 749 C ALA A 198 -49.737-150.683 309.376 1.00 91.83 C
ANISOU 749 C ALA A 198 11016 9832 14041 325 -359 -25 C
ATOM 750 O ALA A 198 -50.026-149.760 308.603 1.00 83.44 O
ANISOU 750 O ALA A 198 9866 8826 13012 427 -299 -4 O
ATOM 751 CB ALA A 198 -51.524-151.917 310.626 1.00 95.94 C
ANISOU 751 CB ALA A 198 11446 10436 14569 59 -394 117 C
ATOM 752 N SER A 199 -48.682-150.625 310.195 1.00 89.46 N
ANISOU 752 N SER A 199 10822 9469 13699 329 -323 -81 N
ATOM 753 CA SER A 199 -47.827-149.442 310.229 1.00 85.41 C
ANISOU 753 CA SER A 199 10326 8947 13180 436 -197 -149 C
ATOM 754 C SER A 199 -47.168-149.201 308.878 1.00 87.62 C
ANISOU 754 C SER A 199 10620 9216 13457 538 -256 -187 C
ATOM 755 O SER A 199 -47.186-148.080 308.356 1.00 91.68 O
ANISOU 755 O SER A 199 11076 9750 14008 621 -161 -163 O
ATOM 756 CB SER A 199 -46.773-149.592 311.325 1.00 82.24 C
ANISOU 756 CB SER A 199 10023 8515 12708 399 -175 -211 C
ATOM 757 OG SER A 199 -47.378-149.706 312.601 1.00 87.30 O
ANISOU 757 OG SER A 199 10632 9224 13313 288 -106 -168 O
ATOM 758 N PHE A 200 -46.580-150.247 308.293 1.00 87.44 N
ANISOU 758 N PHE A 200 10665 9164 13395 528 -413 -245 N
ATOM 759 CA PHE A 200 -45.964-150.097 306.980 1.00 94.33 C
ANISOU 759 CA PHE A 200 11528 10086 14228 607 -467 -304 C
ATOM 760 C PHE A 200 -47.008-149.867 305.895 1.00 94.11 C
ANISOU 760 C PHE A 200 11380 10168 14208 617 -492 -222 C
ATOM 761 O PHE A 200 -46.741-149.147 304.925 1.00 87.83 O
ANISOU 761 O PHE A 200 10535 9463 13373 682 -470 -197 O
ATOM 762 CB PHE A 200 -45.108-151.322 306.656 1.00 99.95 C
ANISOU 762 CB PHE A 200 12318 10749 14909 604 -624 -434 C
ATOM 763 CG PHE A 200 -43.785-151.344 307.374 1.00108.37 C
ANISOU 763 CG PHE A 200 13473 11755 15947 640 -610 -516 C
ATOM 764 CD1 PHE A 200 -43.719-151.616 308.732 1.00110.68 C
ANISOU 764 CD1 PHE A 200 13824 11972 16257 583 -593 -471 C
ATOM 765 CD2 PHE A 200 -42.606-151.096 306.689 1.00112.23 C
ANISOU 765 CD2 PHE A 200 13968 12302 16371 718 -615 -632 C
ATOM 766 CE1 PHE A 200 -42.506-151.638 309.395 1.00110.72 C
ANISOU 766 CE1 PHE A 200 13891 11957 16220 614 -593 -536 C
ATOM 767 CE2 PHE A 200 -41.388-151.117 307.346 1.00114.02 C
ANISOU 767 CE2 PHE A 200 14252 12500 16568 750 -607 -711 C
ATOM 768 CZ PHE A 200 -41.338-151.389 308.701 1.00113.54 C
ANISOU 768 CZ PHE A 200 14249 12361 16530 703 -601 -661 C
ATOM 769 N THR A 201 -48.196-150.457 306.040 1.00 97.22 N
ANISOU 769 N THR A 201 11716 10579 14643 540 -542 -163 N
ATOM 770 CA THR A 201 -49.270-150.186 305.090 1.00102.83 C
ANISOU 770 CA THR A 201 12286 11428 15355 547 -566 -73 C
ATOM 771 C THR A 201 -49.740-148.742 305.204 1.00104.89 C
ANISOU 771 C THR A 201 12452 11722 15679 636 -415 58 C
ATOM 772 O THR A 201 -49.915-148.054 304.191 1.00111.33 O
ANISOU 772 O THR A 201 13179 12641 16482 707 -418 148 O
ATOM 773 CB THR A 201 -50.434-151.152 305.314 1.00102.34 C
ANISOU 773 CB THR A 201 12171 11386 15328 426 -650 -47 C
ATOM 774 OG1 THR A 201 -49.963-152.501 305.205 1.00 99.15 O
ANISOU 774 OG1 THR A 201 11865 10893 14914 346 -798 -172 O
ATOM 775 CG2 THR A 201 -51.528-150.918 304.283 1.00100.91 C
ANISOU 775 CG2 THR A 201 11821 11388 15130 429 -691 38 C
ATOM 776 N ALA A 202 -49.947-148.263 306.433 1.00 99.49 N
ANISOU 776 N ALA A 202 11777 10955 15069 633 -285 69 N
ATOM 777 CA ALA A 202 -50.323-146.866 306.621 1.00 95.93 C
ANISOU 777 CA ALA A 202 11238 10488 14725 733 -131 149 C
ATOM 778 C ALA A 202 -49.223-145.927 306.147 1.00 93.25 C
ANISOU 778 C ALA A 202 10956 10085 14391 819 -76 147 C
ATOM 779 O ALA A 202 -49.513-144.831 305.652 1.00 96.01 O
ANISOU 779 O ALA A 202 11222 10423 14836 913 -11 263 O
ATOM 780 CB ALA A 202 -50.655-146.599 308.089 1.00 93.56 C
ANISOU 780 CB ALA A 202 10931 10134 14485 700 7 98 C
ATOM 781 N SER A 203 -47.960-146.338 306.288 1.00 87.15 N
ANISOU 781 N SER A 203 10316 9269 13528 785 -106 30 N
ATOM 782 CA SER A 203 -46.851-145.534 305.785 1.00 83.91 C
ANISOU 782 CA SER A 203 9951 8831 13099 835 -60 22 C
ATOM 783 C SER A 203 -46.944-145.359 304.276 1.00 92.73 C
ANISOU 783 C SER A 203 10994 10081 14160 872 -144 139 C
ATOM 784 O SER A 203 -46.864-144.238 303.761 1.00102.60 O
ANISOU 784 O SER A 203 12196 11317 15469 929 -78 269 O
ATOM 785 CB SER A 203 -45.520-146.181 306.168 1.00 76.12 C
ANISOU 785 CB SER A 203 9091 7821 12010 791 -98 -136 C
ATOM 786 OG SER A 203 -44.451-145.612 305.431 1.00 74.15 O
ANISOU 786 OG SER A 203 8862 7606 11706 819 -83 -148 O
ATOM 787 N VAL A 204 -47.113-146.463 303.545 1.00 97.19 N
ANISOU 787 N VAL A 204 11542 10779 14607 828 -294 95 N
ATOM 788 CA VAL A 204 -47.244-146.366 302.099 1.00 99.52 C
ANISOU 788 CA VAL A 204 11744 11267 14801 841 -380 188 C
ATOM 789 C VAL A 204 -48.603-145.797 301.709 1.00 99.51 C
ANISOU 789 C VAL A 204 11593 11337 14879 883 -379 394 C
ATOM 790 O VAL A 204 -48.756-145.259 300.605 1.00 86.65 O
ANISOU 790 O VAL A 204 9867 9864 13193 913 -418 553 O
ATOM 791 CB VAL A 204 -46.989-147.741 301.451 1.00102.86 C
ANISOU 791 CB VAL A 204 12182 11820 15080 776 -536 22 C
ATOM 792 CG1 VAL A 204 -48.225-148.625 301.539 1.00106.95 C
ANISOU 792 CG1 VAL A 204 12640 12365 15630 718 -626 17 C
ATOM 793 CG2 VAL A 204 -46.524-147.573 300.017 1.00102.68 C
ANISOU 793 CG2 VAL A 204 12087 12038 14890 776 -598 43 C
ATOM 794 N GLY A 205 -49.597-145.893 302.596 1.00109.95 N
ANISOU 794 N GLY A 205 12877 12575 16323 884 -337 406 N
ATOM 795 CA GLY A 205 -50.842-145.181 302.374 1.00112.73 C
ANISOU 795 CA GLY A 205 13068 12978 16787 954 -312 595 C
ATOM 796 C GLY A 205 -50.682-143.682 302.513 1.00113.87 C
ANISOU 796 C GLY A 205 13189 12981 17096 1070 -178 734 C
ATOM 797 O GLY A 205 -51.370-142.914 301.834 1.00118.54 O
ANISOU 797 O GLY A 205 13643 13628 17767 1158 -191 947 O
ATOM 798 N SER A 206 -49.778-143.244 303.393 1.00104.23 N
ANISOU 798 N SER A 206 12093 11568 15940 1071 -56 618 N
ATOM 799 CA SER A 206 -49.446-141.826 303.470 1.00 99.34 C
ANISOU 799 CA SER A 206 11473 10779 15494 1158 69 719 C
ATOM 800 C SER A 206 -48.776-141.358 302.186 1.00 96.90 C
ANISOU 800 C SER A 206 11159 10557 15102 1161 6 888 C
ATOM 801 O SER A 206 -49.112-140.294 301.652 1.00103.49 O
ANISOU 801 O SER A 206 11908 11337 16077 1245 30 1117 O
ATOM 802 CB SER A 206 -48.550-141.561 304.681 1.00 94.37 C
ANISOU 802 CB SER A 206 10975 9964 14919 1123 204 520 C
ATOM 803 OG SER A 206 -49.178-141.961 305.886 1.00 92.06 O
ANISOU 803 OG SER A 206 10670 9639 14671 1102 267 380 O
ATOM 804 N LEU A 207 -47.830-142.146 301.668 1.00 84.95 N
ANISOU 804 N LEU A 207 9724 9190 13364 1069 -78 785 N
ATOM 805 CA LEU A 207 -47.223-141.811 300.385 1.00 85.00 C
ANISOU 805 CA LEU A 207 9700 9362 13236 1045 -141 935 C
ATOM 806 C LEU A 207 -48.254-141.830 299.266 1.00 89.35 C
ANISOU 806 C LEU A 207 10086 10138 13724 1075 -260 1161 C
ATOM 807 O LEU A 207 -48.124-141.087 298.285 1.00 84.03 O
ANISOU 807 O LEU A 207 9341 9573 13014 1085 -289 1405 O
ATOM 808 CB LEU A 207 -46.081-142.775 300.070 1.00 86.93 C
ANISOU 808 CB LEU A 207 10029 9759 13242 951 -206 726 C
ATOM 809 CG LEU A 207 -44.978-142.895 301.123 1.00 92.66 C
ANISOU 809 CG LEU A 207 10899 10316 13993 919 -117 502 C
ATOM 810 CD1 LEU A 207 -43.922-143.901 300.684 1.00 94.68 C
ANISOU 810 CD1 LEU A 207 11202 10743 14029 856 -202 303 C
ATOM 811 CD2 LEU A 207 -44.349-141.540 301.402 1.00 97.89 C
ANISOU 811 CD2 LEU A 207 11597 10802 14794 927 22 597 C
ATOM 812 N PHE A 208 -49.284-142.670 299.393 1.00 99.24 N
ANISOU 812 N PHE A 208 11267 11484 14955 1074 -336 1100 N
ATOM 813 CA PHE A 208 -50.363-142.663 298.412 1.00101.52 C
ANISOU 813 CA PHE A 208 11374 12007 15190 1101 -451 1309 C
ATOM 814 C PHE A 208 -51.168-141.374 298.493 1.00103.67 C
ANISOU 814 C PHE A 208 11534 12143 15712 1240 -388 1589 C
ATOM 815 O PHE A 208 -51.537-140.801 297.462 1.00107.15 O
ANISOU 815 O PHE A 208 11843 12746 16125 1282 -465 1875 O
ATOM 816 CB PHE A 208 -51.266-143.879 298.615 1.00 97.60 C
ANISOU 816 CB PHE A 208 10825 11630 14630 1045 -540 1156 C
ATOM 817 CG PHE A 208 -52.492-143.873 297.748 1.00 94.05 C
ANISOU 817 CG PHE A 208 10165 11433 14135 1066 -654 1352 C
ATOM 818 CD1 PHE A 208 -52.383-143.955 296.369 1.00 92.49 C
ANISOU 818 CD1 PHE A 208 9870 11561 13712 1018 -779 1472 C
ATOM 819 CD2 PHE A 208 -53.755-143.789 298.312 1.00 91.34 C
ANISOU 819 CD2 PHE A 208 9703 11047 13955 1127 -635 1409 C
ATOM 820 CE1 PHE A 208 -53.510-143.953 295.567 1.00 91.87 C
ANISOU 820 CE1 PHE A 208 9580 11758 13569 1030 -896 1659 C
ATOM 821 CE2 PHE A 208 -54.887-143.784 297.515 1.00 91.36 C
ANISOU 821 CE2 PHE A 208 9489 11311 13912 1149 -748 1592 C
ATOM 822 CZ PHE A 208 -54.764-143.867 296.140 1.00 91.77 C
ANISOU 822 CZ PHE A 208 9448 11684 13736 1100 -885 1723 C
ATOM 823 N LEU A 209 -51.446-140.900 299.711 1.00105.88 N
ANISOU 823 N LEU A 209 11852 12134 16243 1317 -251 1510 N
ATOM 824 CA LEU A 209 -52.154-139.633 299.865 1.00108.83 C
ANISOU 824 CA LEU A 209 12116 12325 16909 1474 -177 1730 C
ATOM 825 C LEU A 209 -51.277-138.448 299.473 1.00110.00 C
ANISOU 825 C LEU A 209 12325 12304 17168 1505 -121 1914 C
ATOM 826 O LEU A 209 -51.791-137.424 299.012 1.00111.23 O
ANISOU 826 O LEU A 209 12366 12375 17521 1626 -129 2208 O
ATOM 827 CB LEU A 209 -52.656-139.481 301.302 1.00101.57 C
ANISOU 827 CB LEU A 209 11206 11173 16213 1536 -32 1535 C
ATOM 828 CG LEU A 209 -53.795-140.418 301.716 1.00 95.44 C
ANISOU 828 CG LEU A 209 10320 10557 15384 1515 -77 1428 C
ATOM 829 CD1 LEU A 209 -54.133-140.244 303.189 1.00 95.89 C
ANISOU 829 CD1 LEU A 209 10389 10425 15620 1547 86 1221 C
ATOM 830 CD2 LEU A 209 -55.025-140.178 300.852 1.00 89.40 C
ANISOU 830 CD2 LEU A 209 9324 9980 14666 1614 -184 1686 C
ATOM 831 N ALA A 210 -49.960-138.565 299.649 1.00106.57 N
ANISOU 831 N ALA A 210 12058 11810 16621 1396 -68 1761 N
ATOM 832 CA ALA A 210 -49.058-137.532 299.151 1.00105.31 C
ANISOU 832 CA ALA A 210 11951 11538 16526 1379 -27 1946 C
ATOM 833 C ALA A 210 -49.041-137.506 297.630 1.00110.22 C
ANISOU 833 C ALA A 210 12471 12472 16936 1335 -174 2250 C
ATOM 834 O ALA A 210 -48.915-136.435 297.024 1.00110.92 O
ANISOU 834 O ALA A 210 12517 12482 17145 1364 -174 2570 O
ATOM 835 CB ALA A 210 -47.652-137.757 299.699 1.00106.19 C
ANISOU 835 CB ALA A 210 12241 11571 16536 1257 59 1689 C
ATOM 836 N ALA A 211 -49.180-138.670 296.997 1.00115.54 N
ANISOU 836 N ALA A 211 13096 13505 17298 1254 -302 2157 N
ATOM 837 CA ALA A 211 -49.222-138.716 295.541 1.00120.12 C
ANISOU 837 CA ALA A 211 13553 14458 17628 1196 -445 2412 C
ATOM 838 C ALA A 211 -50.473-138.029 295.011 1.00123.19 C
ANISOU 838 C ALA A 211 13751 14891 18163 1322 -524 2781 C
ATOM 839 O ALA A 211 -50.400-137.216 294.082 1.00128.95 O
ANISOU 839 O ALA A 211 14398 15721 18876 1324 -581 3151 O
ATOM 840 CB ALA A 211 -49.155-140.163 295.056 1.00122.17 C
ANISOU 840 CB ALA A 211 13793 15081 17545 1083 -559 2162 C
ATOM 841 N ILE A 212 -51.633-138.330 295.603 1.00119.94 N
ANISOU 841 N ILE A 212 13257 14417 17899 1426 -531 2704 N
ATOM 842 CA ILE A 212 -52.871-137.708 295.142 1.00127.28 C
ANISOU 842 CA ILE A 212 13977 15403 18981 1568 -611 3041 C
ATOM 843 C ILE A 212 -52.884-136.220 295.473 1.00130.23 C
ANISOU 843 C ILE A 212 14352 15377 19751 1722 -514 3298 C
ATOM 844 O ILE A 212 -53.524-135.428 294.771 1.00130.41 O
ANISOU 844 O ILE A 212 14216 15435 19900 1834 -599 3695 O
ATOM 845 CB ILE A 212 -54.100-138.432 295.730 1.00132.51 C
ANISOU 845 CB ILE A 212 14529 16120 19697 1629 -633 2868 C
ATOM 846 CG1 ILE A 212 -54.226-138.187 297.236 1.00133.69 C
ANISOU 846 CG1 ILE A 212 14771 15872 20153 1717 -456 2625 C
ATOM 847 CG2 ILE A 212 -54.024-139.923 295.457 1.00131.13 C
ANISOU 847 CG2 ILE A 212 14375 16274 19177 1458 -727 2592 C
ATOM 848 CD1 ILE A 212 -55.288-137.167 297.618 1.00138.06 C
ANISOU 848 CD1 ILE A 212 15164 16211 21080 1936 -406 2812 C
ATOM 849 N ASP A 213 -52.187-135.814 296.538 1.00128.38 N
ANISOU 849 N ASP A 213 14290 14756 19731 1729 -342 3079 N
ATOM 850 CA ASP A 213 -52.120-134.397 296.879 1.00127.26 C
ANISOU 850 CA ASP A 213 14163 14194 19996 1858 -240 3272 C
ATOM 851 C ASP A 213 -51.372-133.614 295.809 1.00126.04 C
ANISOU 851 C ASP A 213 14023 14073 19793 1787 -300 3652 C
ATOM 852 O ASP A 213 -51.801-132.523 295.413 1.00131.75 O
ANISOU 852 O ASP A 213 14649 14612 20797 1913 -332 4034 O
ATOM 853 CB ASP A 213 -51.453-134.219 298.244 1.00126.34 C
ANISOU 853 CB ASP A 213 14225 13710 20067 1841 -43 2902 C
ATOM 854 CG ASP A 213 -51.749-132.867 298.875 1.00130.74 C
ANISOU 854 CG ASP A 213 14762 13797 21115 2010 81 2985 C
ATOM 855 OD1 ASP A 213 -52.272-131.975 298.174 1.00133.03 O
ANISOU 855 OD1 ASP A 213 14942 14025 21576 2110 13 3341 O
ATOM 856 OD2 ASP A 213 -51.454-132.697 300.077 1.00130.62 O
ANISOU 856 OD2 ASP A 213 14849 13508 21274 2015 247 2653 O
ATOM 857 N ARG A 214 -50.260-134.159 295.320 1.00119.99 N
ANISOU 857 N ARG A 214 13363 13549 18678 1584 -321 3565 N
ATOM 858 CA ARG A 214 -49.462-133.481 294.310 1.00124.30 C
ANISOU 858 CA ARG A 214 13916 14188 19125 1473 -368 3912 C
ATOM 859 C ARG A 214 -49.871-133.839 292.887 1.00128.11 C
ANISOU 859 C ARG A 214 14223 15188 19264 1416 -563 4232 C
ATOM 860 O ARG A 214 -49.509-133.113 291.954 1.00131.26 O
ANISOU 860 O ARG A 214 14574 15691 19609 1348 -625 4639 O
ATOM 861 CB ARG A 214 -47.979-133.789 294.529 1.00122.85 C
ANISOU 861 CB ARG A 214 13914 14023 18742 1278 -273 3644 C
ATOM 862 CG ARG A 214 -47.500-133.391 295.918 1.00126.18 C
ANISOU 862 CG ARG A 214 14496 13974 19471 1310 -86 3334 C
ATOM 863 CD ARG A 214 -46.098-133.885 296.218 1.00128.54 C
ANISOU 863 CD ARG A 214 14951 14346 19543 1129 -7 3023 C
ATOM 864 NE ARG A 214 -45.753-133.669 297.621 1.00128.69 N
ANISOU 864 NE ARG A 214 15103 13985 19809 1156 157 2688 N
ATOM 865 CZ ARG A 214 -44.583-133.987 298.164 1.00124.31 C
ANISOU 865 CZ ARG A 214 14679 13423 19130 1026 243 2389 C
ATOM 866 NH1 ARG A 214 -43.632-134.539 297.423 1.00119.19 N
ANISOU 866 NH1 ARG A 214 14046 13109 18134 873 187 2369 N
ATOM 867 NH2 ARG A 214 -44.364-133.752 299.451 1.00123.94 N
ANISOU 867 NH2 ARG A 214 14731 13064 19298 1049 385 2100 N
ATOM 868 N TYR A 215 -50.619-134.930 292.696 1.00126.71 N
ANISOU 868 N TYR A 215 13942 15352 18849 1423 -662 4064 N
ATOM 869 CA TYR A 215 -51.153-135.228 291.370 1.00127.41 C
ANISOU 869 CA TYR A 215 13832 15955 18622 1374 -852 4355 C
ATOM 870 C TYR A 215 -52.316-134.307 291.028 1.00128.07 C
ANISOU 870 C TYR A 215 13726 15958 18977 1562 -945 4819 C
ATOM 871 O TYR A 215 -52.420-133.825 289.893 1.00127.66 O
ANISOU 871 O TYR A 215 13536 16184 18786 1528 -1079 5271 O
ATOM 872 CB TYR A 215 -51.587-136.694 291.288 1.00126.27 C
ANISOU 872 CB TYR A 215 13634 16182 18162 1307 -930 3998 C
ATOM 873 CG TYR A 215 -52.404-137.035 290.058 1.00127.12 C
ANISOU 873 CG TYR A 215 13503 16821 17976 1273 -1128 4246 C
ATOM 874 CD1 TYR A 215 -51.789-137.289 288.839 1.00124.47 C
ANISOU 874 CD1 TYR A 215 13101 16975 17215 1091 -1226 4361 C
ATOM 875 CD2 TYR A 215 -53.791-137.111 290.121 1.00128.75 C
ANISOU 875 CD2 TYR A 215 13530 17081 18308 1412 -1214 4349 C
ATOM 876 CE1 TYR A 215 -52.533-137.602 287.714 1.00125.96 C
ANISOU 876 CE1 TYR A 215 13056 17698 17103 1042 -1409 4571 C
ATOM 877 CE2 TYR A 215 -54.542-137.422 289.001 1.00129.19 C
ANISOU 877 CE2 TYR A 215 13350 17656 18080 1370 -1403 4570 C
ATOM 878 CZ TYR A 215 -53.908-137.667 287.801 1.00127.89 C
ANISOU 878 CZ TYR A 215 13130 17980 17485 1181 -1502 4680 C
ATOM 879 OH TYR A 215 -54.654-137.978 286.686 1.00128.79 O
ANISOU 879 OH TYR A 215 12993 18657 17284 1122 -1692 4884 O
ATOM 880 N ILE A 216 -53.202-134.053 291.994 1.00127.99 N
ANISOU 880 N ILE A 216 13689 15593 19349 1765 -879 4720 N
ATOM 881 CA ILE A 216 -54.331-133.161 291.750 1.00133.97 C
ANISOU 881 CA ILE A 216 14247 16239 20417 1983 -962 5134 C
ATOM 882 C ILE A 216 -53.849-131.734 291.515 1.00139.28 C
ANISOU 882 C ILE A 216 14973 16559 21387 2024 -926 5525 C
ATOM 883 O ILE A 216 -54.432-130.998 290.709 1.00142.96 O
ANISOU 883 O ILE A 216 15318 17126 21874 2054 -1022 5892 O
ATOM 884 CB ILE A 216 -55.334-133.245 292.917 1.00133.59 C
ANISOU 884 CB ILE A 216 14149 15903 20705 2184 -873 4866 C
ATOM 885 CG1 ILE A 216 -56.031-134.608 292.922 1.00127.81 C
ANISOU 885 CG1 ILE A 216 13322 15582 19660 2116 -947 4574 C
ATOM 886 CG2 ILE A 216 -56.365-132.129 292.838 1.00139.66 C
ANISOU 886 CG2 ILE A 216 14809 16487 21768 2347 -876 5088 C
ATOM 887 CD1 ILE A 216 -57.124-134.732 293.963 1.00123.69 C
ANISOU 887 CD1 ILE A 216 12706 14873 19419 2288 -874 4354 C
ATOM 888 N SER A 217 -52.770-131.325 292.189 1.00139.12 N
ANISOU 888 N SER A 217 15166 16151 21544 1964 -766 5366 N
ATOM 889 CA SER A 217 -52.245-129.977 291.997 1.00140.01 C
ANISOU 889 CA SER A 217 15371 15937 21888 1918 -703 5612 C
ATOM 890 C SER A 217 -51.756-129.759 290.570 1.00146.89 C
ANISOU 890 C SER A 217 16166 17189 22457 1759 -855 6113 C
ATOM 891 O SER A 217 -51.807-128.632 290.063 1.00155.71 O
ANISOU 891 O SER A 217 17264 18163 23736 1744 -875 6447 O
ATOM 892 CB SER A 217 -51.117-129.706 292.993 1.00131.18 C
ANISOU 892 CB SER A 217 14487 14392 20965 1845 -506 5302 C
ATOM 893 OG SER A 217 -50.067-130.646 292.847 1.00121.99 O
ANISOU 893 OG SER A 217 13422 13518 19410 1644 -494 5100 O
ATOM 894 N ILE A 218 -51.287-130.813 289.907 1.00147.23 N
ANISOU 894 N ILE A 218 16171 17762 22009 1599 -948 6082 N
ATOM 895 CA ILE A 218 -50.802-130.694 288.535 1.00151.73 C
ANISOU 895 CA ILE A 218 16652 18805 22194 1406 -1083 6499 C
ATOM 896 C ILE A 218 -51.922-130.921 287.527 1.00156.73 C
ANISOU 896 C ILE A 218 17016 19922 22613 1472 -1303 6853 C
ATOM 897 O ILE A 218 -52.049-130.175 286.554 1.00161.89 O
ANISOU 897 O ILE A 218 17571 20750 23188 1398 -1391 7284 O
ATOM 898 CB ILE A 218 -49.633-131.672 288.303 1.00149.22 C
ANISOU 898 CB ILE A 218 16442 18876 21379 1140 -1030 6119 C
ATOM 899 CG1 ILE A 218 -48.508-131.412 289.307 1.00147.25 C
ANISOU 899 CG1 ILE A 218 16438 18172 21339 1075 -823 5789 C
ATOM 900 CG2 ILE A 218 -49.116-131.557 286.875 1.00151.37 C
ANISOU 900 CG2 ILE A 218 16597 19703 21213 922 -1155 6519 C
ATOM 901 CD1 ILE A 218 -47.900-130.030 289.204 1.00150.17 C
ANISOU 901 CD1 ILE A 218 16877 18165 22016 1029 -768 6200 C
ATOM 902 N HIS A 219 -52.748-131.947 287.744 1.00158.94 N
ANISOU 902 N HIS A 219 17203 20447 22741 1540 -1348 6520 N
ATOM 903 CA HIS A 219 -53.806-132.260 286.789 1.00164.91 C
ANISOU 903 CA HIS A 219 17691 21719 23248 1572 -1556 6791 C
ATOM 904 C HIS A 219 -54.915-131.215 286.830 1.00169.94 C
ANISOU 904 C HIS A 219 18251 22060 24257 1743 -1549 7003 C
ATOM 905 O HIS A 219 -55.460-130.839 285.785 1.00172.17 O
ANISOU 905 O HIS A 219 18364 22672 24380 1707 -1684 7376 O
ATOM 906 CB HIS A 219 -54.367-133.655 287.073 1.00162.06 C
ANISOU 906 CB HIS A 219 17278 21662 22636 1553 -1577 6289 C
ATOM 907 CG HIS A 219 -54.980-134.319 285.879 1.00162.38 C
ANISOU 907 CG HIS A 219 17072 22419 22208 1449 -1785 6438 C
ATOM 908 ND1 HIS A 219 -54.250-134.659 284.760 1.00162.27 N
ANISOU 908 ND1 HIS A 219 17013 22960 21682 1201 -1865 6524 N
ATOM 909 CD2 HIS A 219 -56.251-134.716 285.633 1.00163.21 C
ANISOU 909 CD2 HIS A 219 16943 22807 22262 1546 -1925 6491 C
ATOM 910 CE1 HIS A 219 -55.046-135.231 283.874 1.00164.37 C
ANISOU 910 CE1 HIS A 219 17033 23822 21598 1148 -2048 6614 C
ATOM 911 NE2 HIS A 219 -56.265-135.279 284.380 1.00164.99 N
ANISOU 911 NE2 HIS A 219 16994 23744 21950 1352 -2092 6603 N
ATOM 912 N ARG A 220 -55.263-130.733 288.024 1.00172.44 N
ANISOU 912 N ARG A 220 18679 21783 25056 1927 -1396 6756 N
ATOM 913 CA ARG A 220 -56.344-129.766 288.217 1.00178.01 C
ANISOU 913 CA ARG A 220 19306 22189 26141 2119 -1384 6882 C
ATOM 914 C ARG A 220 -55.851-128.656 289.137 1.00175.98 C
ANISOU 914 C ARG A 220 19245 21250 26368 2194 -1200 6778 C
ATOM 915 O ARG A 220 -56.183-128.629 290.330 1.00174.96 O
ANISOU 915 O ARG A 220 19193 20744 26541 2333 -1060 6394 O
ATOM 916 CB ARG A 220 -57.589-130.441 288.796 1.00178.10 C
ANISOU 916 CB ARG A 220 19191 22274 26205 2281 -1396 6594 C
ATOM 917 CG ARG A 220 -57.921-131.791 288.172 1.00178.41 C
ANISOU 917 CG ARG A 220 19070 22954 25765 2176 -1548 6528 C
ATOM 918 CD ARG A 220 -58.963-131.670 287.075 1.00185.66 C
ANISOU 918 CD ARG A 220 19738 24313 26490 2188 -1731 6867 C
ATOM 919 NE ARG A 220 -60.297-131.442 287.622 1.00189.88 N
ANISOU 919 NE ARG A 220 20152 24679 27313 2403 -1717 6773 N
ATOM 920 CZ ARG A 220 -61.102-132.410 288.050 1.00190.18 C
ANISOU 920 CZ ARG A 220 20080 24918 27263 2444 -1738 6469 C
ATOM 921 NH1 ARG A 220 -62.300-132.113 288.535 1.00194.19 N
ANISOU 921 NH1 ARG A 220 20464 25285 28033 2638 -1721 6406 N
ATOM 922 NH2 ARG A 220 -60.709-133.676 287.995 1.00186.11 N
ANISOU 922 NH2 ARG A 220 19563 24751 26398 2286 -1781 6221 N
ATOM 923 N PRO A 221 -55.053-127.718 288.616 1.00170.81 N
ANISOU 923 N PRO A 221 18668 20450 25784 2084 -1196 7098 N
ATOM 924 CA PRO A 221 -54.544-126.645 289.489 1.00165.91 C
ANISOU 924 CA PRO A 221 18230 19185 25621 2131 -1026 6966 C
ATOM 925 C PRO A 221 -55.625-125.680 289.940 1.00163.82 C
ANISOU 925 C PRO A 221 17900 18543 25801 2364 -1001 6966 C
ATOM 926 O PRO A 221 -55.618-125.247 291.099 1.00161.98 O
ANISOU 926 O PRO A 221 17787 17836 25923 2468 -838 6609 O
ATOM 927 CB PRO A 221 -53.488-125.949 288.615 1.00168.84 C
ANISOU 927 CB PRO A 221 18659 19588 25902 1927 -1064 7369 C
ATOM 928 CG PRO A 221 -53.204-126.905 287.490 1.00168.39 C
ANISOU 928 CG PRO A 221 18487 20220 25276 1747 -1217 7595 C
ATOM 929 CD PRO A 221 -54.485-127.640 287.261 1.00170.46 C
ANISOU 929 CD PRO A 221 18548 20842 25377 1880 -1336 7553 C
ATOM 930 N LEU A 222 -56.559-125.327 289.053 1.00160.75 N
ANISOU 930 N LEU A 222 17311 18375 25390 2448 -1161 7350 N
ATOM 931 CA LEU A 222 -57.607-124.382 289.420 1.00160.19 C
ANISOU 931 CA LEU A 222 17160 17956 25750 2689 -1153 7380 C
ATOM 932 C LEU A 222 -58.601-124.992 290.400 1.00157.86 C
ANISOU 932 C LEU A 222 16803 17632 25546 2877 -1085 6945 C
ATOM 933 O LEU A 222 -59.201-124.268 291.202 1.00157.58 O
ANISOU 933 O LEU A 222 16767 17192 25913 3072 -997 6764 O
ATOM 934 CB LEU A 222 -58.334-123.888 288.168 1.00163.39 C
ANISOU 934 CB LEU A 222 17355 18637 26088 2728 -1355 7930 C
ATOM 935 CG LEU A 222 -57.746-122.690 287.413 1.00166.73 C
ANISOU 935 CG LEU A 222 17811 18871 26668 2640 -1410 8404 C
ATOM 936 CD1 LEU A 222 -56.347-122.979 286.886 1.00163.00 C
ANISOU 936 CD1 LEU A 222 17460 18604 25869 2342 -1401 8528 C
ATOM 937 CD2 LEU A 222 -58.671-122.275 286.278 1.00173.76 C
ANISOU 937 CD2 LEU A 222 18465 20053 27502 2711 -1614 8921 C
ATOM 938 N ALA A 223 -58.785-126.310 290.356 1.00155.94 N
ANISOU 938 N ALA A 223 16496 17823 24931 2815 -1126 6768 N
ATOM 939 CA ALA A 223 -59.728-126.999 291.225 1.00153.44 C
ANISOU 939 CA ALA A 223 16101 17544 24656 2960 -1073 6378 C
ATOM 940 C ALA A 223 -59.052-127.694 292.400 1.00151.50 C
ANISOU 940 C ALA A 223 16035 17127 24402 2894 -896 5869 C
ATOM 941 O ALA A 223 -59.719-128.422 293.141 1.00153.35 O
ANISOU 941 O ALA A 223 16209 17440 24619 2971 -847 5534 O
ATOM 942 CB ALA A 223 -60.543-128.013 290.420 1.00150.26 C
ANISOU 942 CB ALA A 223 15478 17747 23867 2938 -1250 6512 C
ATOM 943 N TYR A 224 -57.746-127.487 292.586 1.00151.65 N
ANISOU 943 N TYR A 224 16263 16928 24428 2745 -800 5812 N
ATOM 944 CA TYR A 224 -57.041-128.135 293.690 1.00148.49 C
ANISOU 944 CA TYR A 224 16034 16374 24011 2674 -636 5340 C
ATOM 945 C TYR A 224 -57.533-127.626 295.039 1.00149.87 C
ANISOU 945 C TYR A 224 16253 16140 24550 2826 -462 4942 C
ATOM 946 O TYR A 224 -57.670-128.405 295.990 1.00145.73 O
ANISOU 946 O TYR A 224 15757 15638 23976 2832 -362 4537 O
ATOM 947 CB TYR A 224 -55.534-127.916 293.549 1.00150.11 C
ANISOU 947 CB TYR A 224 16439 16440 24155 2483 -576 5389 C
ATOM 948 CG TYR A 224 -54.730-128.325 294.766 1.00148.91 C
ANISOU 948 CG TYR A 224 16479 16049 24050 2418 -390 4905 C
ATOM 949 CD1 TYR A 224 -54.364-129.649 294.967 1.00147.53 C
ANISOU 949 CD1 TYR A 224 16334 16140 23579 2332 -394 4682 C
ATOM 950 CD2 TYR A 224 -54.330-127.384 295.708 1.00151.15 C
ANISOU 950 CD2 TYR A 224 16905 15855 24669 2437 -219 4668 C
ATOM 951 CE1 TYR A 224 -53.627-130.026 296.076 1.00145.09 C
ANISOU 951 CE1 TYR A 224 16196 15623 23309 2270 -230 4254 C
ATOM 952 CE2 TYR A 224 -53.595-127.752 296.819 1.00148.33 C
ANISOU 952 CE2 TYR A 224 16711 15326 24321 2360 -53 4224 C
ATOM 953 CZ TYR A 224 -53.246-129.073 296.998 1.00144.08 C
ANISOU 953 CZ TYR A 224 16203 15056 23484 2278 -59 4027 C
ATOM 954 OH TYR A 224 -52.512-129.443 298.103 1.00139.14 O
ANISOU 954 OH TYR A 224 15736 14273 22860 2199 99 3599 O
ATOM 955 N LYS A 225 -57.799-126.322 295.145 1.00154.76 N
ANISOU 955 N LYS A 225 16870 16398 25533 2943 -427 5051 N
ATOM 956 CA LYS A 225 -58.255-125.757 296.409 1.00153.45 C
ANISOU 956 CA LYS A 225 16730 15866 25710 3088 -264 4665 C
ATOM 957 C LYS A 225 -59.669-126.193 296.766 1.00147.05 C
ANISOU 957 C LYS A 225 15716 15239 24918 3273 -289 4524 C
ATOM 958 O LYS A 225 -60.042-126.134 297.942 1.00140.24 O
ANISOU 958 O LYS A 225 14858 14200 24226 3362 -142 4121 O
ATOM 959 CB LYS A 225 -58.175-124.230 296.361 1.00163.55 C
ANISOU 959 CB LYS A 225 18045 16708 27389 3172 -238 4828 C
ATOM 960 CG LYS A 225 -56.765-123.686 296.524 1.00167.33 C
ANISOU 960 CG LYS A 225 18745 16894 27940 2992 -141 4789 C
ATOM 961 CD LYS A 225 -56.151-124.164 297.833 1.00165.06 C
ANISOU 961 CD LYS A 225 18608 16488 27619 2907 53 4243 C
ATOM 962 CE LYS A 225 -54.744-123.622 298.024 1.00165.25 C
ANISOU 962 CE LYS A 225 18840 16240 27709 2722 149 4184 C
ATOM 963 NZ LYS A 225 -54.139-124.101 299.299 1.00160.89 N
ANISOU 963 NZ LYS A 225 18422 15610 27098 2631 329 3654 N
ATOM 964 N ARG A 226 -60.459-126.633 295.785 1.00150.21 N
ANISOU 964 N ARG A 226 15924 16021 25128 3320 -471 4843 N
ATOM 965 CA ARG A 226 -61.818-127.081 296.068 1.00154.37 C
ANISOU 965 CA ARG A 226 16235 16762 25656 3484 -505 4723 C
ATOM 966 C ARG A 226 -61.856-128.526 296.550 1.00148.30 C
ANISOU 966 C ARG A 226 15453 16309 24586 3380 -474 4420 C
ATOM 967 O ARG A 226 -62.722-128.882 297.356 1.00148.48 O
ANISOU 967 O ARG A 226 15358 16386 24671 3483 -407 4135 O
ATOM 968 CB ARG A 226 -62.693-126.920 294.823 1.00163.45 C
ANISOU 968 CB ARG A 226 17166 18210 26728 3572 -721 5184 C
ATOM 969 CG ARG A 226 -64.174-127.191 295.057 1.00168.53 C
ANISOU 969 CG ARG A 226 17557 19058 27417 3764 -766 5093 C
ATOM 970 CD ARG A 226 -64.982-127.008 293.780 1.00174.17 C
ANISOU 970 CD ARG A 226 18053 20090 28035 3837 -989 5562 C
ATOM 971 NE ARG A 226 -64.644-128.004 292.768 1.00173.73 N
ANISOU 971 NE ARG A 226 17964 20526 27521 3630 -1137 5778 N
ATOM 972 CZ ARG A 226 -65.317-129.134 292.576 1.00173.22 C
ANISOU 972 CZ ARG A 226 17731 20929 27156 3584 -1225 5698 C
ATOM 973 NH1 ARG A 226 -66.373-129.415 293.327 1.00174.80 N
ANISOU 973 NH1 ARG A 226 17776 21173 27467 3727 -1178 5429 N
ATOM 974 NH2 ARG A 226 -64.936-129.983 291.631 1.00170.97 N
ANISOU 974 NH2 ARG A 226 17420 21088 26453 3385 -1362 5875 N
ATOM 975 N ILE A 227 -60.931-129.363 296.083 1.00143.67 N
ANISOU 975 N ILE A 227 14970 15934 23682 3177 -523 4475 N
ATOM 976 CA ILE A 227 -60.934-130.783 296.422 1.00136.83 C
ANISOU 976 CA ILE A 227 14083 15371 22534 3072 -522 4225 C
ATOM 977 C ILE A 227 -60.184-131.013 297.727 1.00131.90 C
ANISOU 977 C ILE A 227 13655 14472 21990 3003 -316 3782 C
ATOM 978 O ILE A 227 -60.783-131.385 298.743 1.00132.07 O
ANISOU 978 O ILE A 227 13619 14482 22082 3059 -211 3452 O
ATOM 979 CB ILE A 227 -60.328-131.625 295.284 1.00132.67 C
ANISOU 979 CB ILE A 227 13554 15233 21623 2899 -687 4475 C
ATOM 980 CG1 ILE A 227 -61.154-131.464 294.005 1.00136.05 C
ANISOU 980 CG1 ILE A 227 13762 16014 21916 2946 -896 4897 C
ATOM 981 CG2 ILE A 227 -60.242-133.091 295.690 1.00126.89 C
ANISOU 981 CG2 ILE A 227 12810 14764 20638 2787 -688 4190 C
ATOM 982 CD1 ILE A 227 -60.654-132.295 292.842 1.00134.96 C
ANISOU 982 CD1 ILE A 227 13584 16344 21352 2764 -1069 5126 C
ATOM 983 N VAL A 228 -58.872-130.796 297.710 1.00125.15 N
ANISOU 983 N VAL A 228 13017 13425 21110 2870 -258 3775 N
ATOM 984 CA VAL A 228 -58.028-131.057 298.873 1.00117.69 C
ANISOU 984 CA VAL A 228 12263 12258 20193 2776 -77 3368 C
ATOM 985 C VAL A 228 -58.223-129.922 299.873 1.00123.52 C
ANISOU 985 C VAL A 228 13049 12603 21280 2882 91 3142 C
ATOM 986 O VAL A 228 -57.854-128.776 299.608 1.00130.87 O
ANISOU 986 O VAL A 228 14047 13258 22420 2907 106 3299 O
ATOM 987 CB VAL A 228 -56.554-131.198 298.478 1.00111.08 C
ANISOU 987 CB VAL A 228 11624 11377 19206 2600 -80 3439 C
ATOM 988 CG1 VAL A 228 -55.749-131.795 299.627 1.00101.13 C
ANISOU 988 CG1 VAL A 228 10533 9995 17896 2491 77 3011 C
ATOM 989 CG2 VAL A 228 -56.420-132.042 297.218 1.00111.76 C
ANISOU 989 CG2 VAL A 228 11623 11872 18967 2520 -278 3751 C
ATOM 990 N THR A 229 -58.808-130.240 301.026 1.00119.71 N
ANISOU 990 N THR A 229 12517 12108 20861 2936 215 2774 N
ATOM 991 CA THR A 229 -59.018-129.278 302.096 1.00120.71 C
ANISOU 991 CA THR A 229 12665 11915 21284 3030 383 2493 C
ATOM 992 C THR A 229 -58.431-129.830 303.388 1.00114.46 C
ANISOU 992 C THR A 229 11997 11082 20410 2908 556 2046 C
ATOM 993 O THR A 229 -57.963-130.971 303.450 1.00108.98 O
ANISOU 993 O THR A 229 11362 10590 19456 2772 539 1970 O
ATOM 994 CB THR A 229 -60.507-128.962 302.295 1.00131.11 C
ANISOU 994 CB THR A 229 13742 13293 22780 3247 372 2479 C
ATOM 995 OG1 THR A 229 -61.163-130.100 302.867 1.00134.39 O
ANISOU 995 OG1 THR A 229 14031 14006 23023 3233 398 2264 O
ATOM 996 CG2 THR A 229 -61.168-128.616 300.969 1.00132.91 C
ANISOU 996 CG2 THR A 229 13821 13645 23033 3361 174 2940 C
ATOM 997 N ARG A 230 -58.460-128.999 304.433 1.00117.42 N
ANISOU 997 N ARG A 230 12402 11198 21015 2958 720 1748 N
ATOM 998 CA ARG A 230 -58.011-129.467 305.744 1.00119.79 C
ANISOU 998 CA ARG A 230 12787 11498 21229 2844 889 1315 C
ATOM 999 C ARG A 230 -58.952-130.516 306.325 1.00120.05 C
ANISOU 999 C ARG A 230 12651 11831 21131 2875 914 1144 C
ATOM 1000 O ARG A 230 -58.464-131.573 306.761 1.00118.38 O
ANISOU 1000 O ARG A 230 12509 11778 20693 2727 945 992 O
ATOM 1001 CB ARG A 230 -57.819-128.272 306.686 1.00126.27 C
ANISOU 1001 CB ARG A 230 13658 12000 22318 2881 1052 1035 C
ATOM 1002 CG ARG A 230 -57.202-128.612 308.040 1.00126.70 C
ANISOU 1002 CG ARG A 230 13808 12062 22271 2739 1229 593 C
ATOM 1003 CD ARG A 230 -58.266-128.796 309.113 1.00130.86 C
ANISOU 1003 CD ARG A 230 14150 12724 22846 2835 1349 280 C
ATOM 1004 NE ARG A 230 -59.151-127.639 309.207 1.00138.52 N
ANISOU 1004 NE ARG A 230 14979 13510 24141 3042 1383 253 N
ATOM 1005 CZ ARG A 230 -60.205-127.567 310.014 1.00142.83 C
ANISOU 1005 CZ ARG A 230 15328 14160 24781 3170 1483 2 C
ATOM 1006 NH1 ARG A 230 -60.508-128.590 310.801 1.00142.89 N
ANISOU 1006 NH1 ARG A 230 15249 14467 24574 3093 1565 -227 N
ATOM 1007 NH2 ARG A 230 -60.956-126.475 310.034 1.00146.88 N
ANISOU 1007 NH2 ARG A 230 15717 14483 25608 3375 1504 -17 N
ATOM 1008 N PRO A 231 -60.278-130.315 306.366 1.00121.83 N
ANISOU 1008 N PRO A 231 12645 12154 21490 3055 901 1163 N
ATOM 1009 CA PRO A 231 -61.135-131.380 306.917 1.00120.18 C
ANISOU 1009 CA PRO A 231 12254 12266 21145 3055 930 1006 C
ATOM 1010 C PRO A 231 -61.136-132.645 306.078 1.00119.22 C
ANISOU 1010 C PRO A 231 12097 12439 20763 2960 768 1243 C
ATOM 1011 O PRO A 231 -61.176-133.748 306.637 1.00121.37 O
ANISOU 1011 O PRO A 231 12328 12918 20869 2849 808 1079 O
ATOM 1012 CB PRO A 231 -62.523-130.725 306.963 1.00124.41 C
ANISOU 1012 CB PRO A 231 12535 12836 21899 3285 933 1016 C
ATOM 1013 CG PRO A 231 -62.469-129.658 305.936 1.00125.77 C
ANISOU 1013 CG PRO A 231 12744 12784 22257 3405 814 1340 C
ATOM 1014 CD PRO A 231 -61.070-129.127 305.999 1.00126.41 C
ANISOU 1014 CD PRO A 231 13101 12565 22364 3268 868 1305 C
ATOM 1015 N LYS A 232 -61.096-132.522 304.748 1.00116.86 N
ANISOU 1015 N LYS A 232 11797 12179 20425 2991 584 1625 N
ATOM 1016 CA LYS A 232 -61.054-133.712 303.903 1.00111.25 C
ANISOU 1016 CA LYS A 232 11044 11772 19455 2891 420 1834 C
ATOM 1017 C LYS A 232 -59.766-134.496 304.121 1.00100.87 C
ANISOU 1017 C LYS A 232 9950 10426 17949 2694 446 1714 C
ATOM 1018 O LYS A 232 -59.793-135.728 304.221 1.00 98.50 O
ANISOU 1018 O LYS A 232 9604 10351 17472 2591 403 1654 O
ATOM 1019 CB LYS A 232 -61.206-133.325 302.432 1.00118.78 C
ANISOU 1019 CB LYS A 232 11945 12801 20383 2954 222 2263 C
ATOM 1020 CG LYS A 232 -62.592-132.821 302.056 1.00132.50 C
ANISOU 1020 CG LYS A 232 13427 14660 22259 3147 148 2425 C
ATOM 1021 CD LYS A 232 -63.652-133.890 302.273 1.00140.62 C
ANISOU 1021 CD LYS A 232 14211 16059 23159 3141 109 2341 C
ATOM 1022 CE LYS A 232 -65.026-133.407 301.832 1.00148.39 C
ANISOU 1022 CE LYS A 232 14923 17202 24257 3332 22 2508 C
ATOM 1023 NZ LYS A 232 -65.053-133.044 300.388 1.00151.51 N
ANISOU 1023 NZ LYS A 232 15288 17692 24586 3370 -184 2937 N
ATOM 1024 N ALA A 233 -58.629-133.801 304.200 1.00 99.31 N
ANISOU 1024 N ALA A 233 9981 9953 17800 2636 512 1677 N
ATOM 1025 CA ALA A 233 -57.369-134.486 304.470 1.00 94.75 C
ANISOU 1025 CA ALA A 233 9610 9343 17045 2459 544 1539 C
ATOM 1026 C ALA A 233 -57.323-135.034 305.891 1.00 91.45 C
ANISOU 1026 C ALA A 233 9216 8927 16604 2387 707 1150 C
ATOM 1027 O ALA A 233 -56.700-136.076 306.131 1.00 83.80 O
ANISOU 1027 O ALA A 233 8370 8090 15380 2212 686 1032 O
ATOM 1028 CB ALA A 233 -56.188-133.547 304.224 1.00 93.83 C
ANISOU 1028 CB ALA A 233 9704 8958 16991 2405 580 1592 C
ATOM 1029 N VAL A 234 -57.968-134.353 306.842 1.00 99.53 N
ANISOU 1029 N VAL A 234 10152 9862 17804 2471 856 932 N
ATOM 1030 CA VAL A 234 -58.053-134.874 308.204 1.00101.40 C
ANISOU 1030 CA VAL A 234 10360 10164 18004 2400 1017 574 C
ATOM 1031 C VAL A 234 -58.850-136.173 308.220 1.00 99.15 C
ANISOU 1031 C VAL A 234 9930 10228 17514 2326 941 593 C
ATOM 1032 O VAL A 234 -58.436-137.171 308.822 1.00 97.49 O
ANISOU 1032 O VAL A 234 9846 10183 17012 2107 949 432 O
ATOM 1033 CB VAL A 234 -58.664-133.821 309.147 1.00109.83 C
ANISOU 1033 CB VAL A 234 11333 11114 19284 2507 1186 330 C
ATOM 1034 CG1 VAL A 234 -59.267-134.486 310.376 1.00112.40 C
ANISOU 1034 CG1 VAL A 234 11502 11647 19557 2465 1333 23 C
ATOM 1035 CG2 VAL A 234 -57.609-132.807 309.562 1.00113.06 C
ANISOU 1035 CG2 VAL A 234 11950 11230 19778 2452 1285 177 C
ATOM 1036 N VAL A 235 -59.999-136.181 307.542 1.00 99.69 N
ANISOU 1036 N VAL A 235 9765 10453 17658 2456 841 799 N
ATOM 1037 CA VAL A 235 -60.825-137.384 307.487 1.00104.88 C
ANISOU 1037 CA VAL A 235 10308 11489 18051 2321 745 815 C
ATOM 1038 C VAL A 235 -60.124-138.484 306.698 1.00107.26 C
ANISOU 1038 C VAL A 235 10802 11938 18014 2107 563 943 C
ATOM 1039 O VAL A 235 -60.132-139.654 307.099 1.00109.06 O
ANISOU 1039 O VAL A 235 11092 12366 17979 1894 531 828 O
ATOM 1040 CB VAL A 235 -62.205-137.050 306.892 1.00107.28 C
ANISOU 1040 CB VAL A 235 10293 11942 18528 2518 674 1007 C
ATOM 1041 CG1 VAL A 235 -62.960-138.323 306.541 1.00105.47 C
ANISOU 1041 CG1 VAL A 235 9957 12110 18004 2346 532 1075 C
ATOM 1042 CG2 VAL A 235 -63.012-136.201 307.865 1.00108.40 C
ANISOU 1042 CG2 VAL A 235 10210 11999 18980 2712 870 797 C
ATOM 1043 N ALA A 236 -59.500-138.127 305.571 1.00104.95 N
ANISOU 1043 N ALA A 236 10600 11548 17728 2156 443 1180 N
ATOM 1044 CA ALA A 236 -58.887-139.134 304.709 1.00 99.47 C
ANISOU 1044 CA ALA A 236 10050 11025 16718 1973 270 1278 C
ATOM 1045 C ALA A 236 -57.789-139.896 305.439 1.00 97.38 C
ANISOU 1045 C ALA A 236 10040 10709 16251 1770 320 1041 C
ATOM 1046 O ALA A 236 -57.715-141.128 305.359 1.00 97.84 O
ANISOU 1046 O ALA A 236 10165 10954 16056 1587 221 985 O
ATOM 1047 CB ALA A 236 -58.338-138.476 303.443 1.00 96.56 C
ANISOU 1047 CB ALA A 236 9720 10584 16386 2057 160 1563 C
ATOM 1048 N PHE A 237 -56.922-139.178 306.159 1.00 95.01 N
ANISOU 1048 N PHE A 237 9877 10150 16074 1798 467 900 N
ATOM 1049 CA PHE A 237 -55.846-139.845 306.886 1.00 98.78 C
ANISOU 1049 CA PHE A 237 10577 10595 16362 1618 509 689 C
ATOM 1050 C PHE A 237 -56.395-140.740 307.990 1.00100.44 C
ANISOU 1050 C PHE A 237 10749 10963 16448 1487 561 499 C
ATOM 1051 O PHE A 237 -55.888-141.847 308.209 1.00 99.82 O
ANISOU 1051 O PHE A 237 10808 10978 16140 1306 491 428 O
ATOM 1052 CB PHE A 237 -54.875-138.815 307.462 1.00104.67 C
ANISOU 1052 CB PHE A 237 11444 11058 17269 1668 660 567 C
ATOM 1053 CG PHE A 237 -53.769-138.431 306.521 1.00106.24 C
ANISOU 1053 CG PHE A 237 11785 11137 17445 1665 590 711 C
ATOM 1054 CD1 PHE A 237 -52.670-139.258 306.352 1.00105.03 C
ANISOU 1054 CD1 PHE A 237 11815 11057 17034 1507 515 651 C
ATOM 1055 CD2 PHE A 237 -53.825-137.243 305.811 1.00107.13 C
ANISOU 1055 CD2 PHE A 237 11835 11067 17802 1820 597 916 C
ATOM 1056 CE1 PHE A 237 -51.648-138.909 305.487 1.00106.85 C
ANISOU 1056 CE1 PHE A 237 12151 11224 17222 1492 461 770 C
ATOM 1057 CE2 PHE A 237 -52.807-136.887 304.945 1.00108.06 C
ANISOU 1057 CE2 PHE A 237 12073 11108 17878 1787 537 1072 C
ATOM 1058 CZ PHE A 237 -51.717-137.721 304.783 1.00109.22 C
ANISOU 1058 CZ PHE A 237 12390 11372 17739 1617 475 986 C
ATOM 1059 N CYS A 238 -57.431-140.279 308.697 1.00101.08 N
ANISOU 1059 N CYS A 238 10636 11083 16688 1574 683 421 N
ATOM 1060 CA CYS A 238 -58.050-141.109 309.725 1.00100.90 C
ANISOU 1060 CA CYS A 238 10546 11264 16529 1427 737 269 C
ATOM 1061 C CYS A 238 -58.597-142.399 309.127 1.00101.29 C
ANISOU 1061 C CYS A 238 10564 11548 16374 1280 557 396 C
ATOM 1062 O CYS A 238 -58.351-143.492 309.650 1.00101.06 O
ANISOU 1062 O CYS A 238 10642 11613 16144 1072 517 325 O
ATOM 1063 CB CYS A 238 -59.160-140.332 310.434 1.00107.14 C
ANISOU 1063 CB CYS A 238 11084 12100 17525 1563 900 162 C
ATOM 1064 SG CYS A 238 -58.610-138.943 311.450 1.00113.05 S
ANISOU 1064 SG CYS A 238 11851 12585 18517 1696 1145 -98 S
ATOM 1065 N LEU A 239 -59.338-142.291 308.020 1.00102.01 N
ANISOU 1065 N LEU A 239 10503 11733 16523 1377 439 590 N
ATOM 1066 CA LEU A 239 -59.863-143.487 307.370 1.00 98.74 C
ANISOU 1066 CA LEU A 239 10048 11548 15922 1225 263 684 C
ATOM 1067 C LEU A 239 -58.741-144.336 306.786 1.00101.17 C
ANISOU 1067 C LEU A 239 10599 11802 16039 1087 124 690 C
ATOM 1068 O LEU A 239 -58.825-145.570 306.787 1.00106.71 O
ANISOU 1068 O LEU A 239 11354 12615 16575 894 19 654 O
ATOM 1069 CB LEU A 239 -60.871-143.100 306.288 1.00 89.60 C
ANISOU 1069 CB LEU A 239 8653 10538 14854 1364 163 887 C
ATOM 1070 CG LEU A 239 -62.191-142.523 306.807 1.00 85.51 C
ANISOU 1070 CG LEU A 239 7840 10137 14512 1491 270 876 C
ATOM 1071 CD1 LEU A 239 -63.186-142.304 305.673 1.00 89.81 C
ANISOU 1071 CD1 LEU A 239 8136 10872 15114 1613 134 1102 C
ATOM 1072 CD2 LEU A 239 -62.782-143.429 307.876 1.00 76.01 C
ANISOU 1072 CD2 LEU A 239 6581 9117 13184 1285 336 716 C
ATOM 1073 N MET A 240 -57.680-143.696 306.290 1.00 97.45 N
ANISOU 1073 N MET A 240 10269 11157 15601 1180 124 724 N
ATOM 1074 CA MET A 240 -56.532-144.452 305.800 1.00 93.62 C
ANISOU 1074 CA MET A 240 9997 10634 14938 1065 13 691 C
ATOM 1075 C MET A 240 -55.901-145.272 306.920 1.00 93.62 C
ANISOU 1075 C MET A 240 10166 10568 14838 907 55 511 C
ATOM 1076 O MET A 240 -55.458-146.405 306.697 1.00 87.75 O
ANISOU 1076 O MET A 240 9541 9855 13946 767 -71 468 O
ATOM 1077 CB MET A 240 -55.512-143.499 305.174 1.00 90.62 C
ANISOU 1077 CB MET A 240 9713 10102 14616 1185 32 761 C
ATOM 1078 CG MET A 240 -54.357-144.174 304.447 1.00 89.49 C
ANISOU 1078 CG MET A 240 9744 9974 14285 1092 -87 733 C
ATOM 1079 SD MET A 240 -52.999-144.652 305.534 1.00 94.12 S
ANISOU 1079 SD MET A 240 10572 10395 14795 987 -17 509 S
ATOM 1080 CE MET A 240 -52.592-143.078 306.282 1.00 93.64 C
ANISOU 1080 CE MET A 240 10523 10117 14941 1118 190 485 C
ATOM 1081 N TRP A 241 -55.864-144.721 308.136 1.00 99.70 N
ANISOU 1081 N TRP A 241 10938 11254 15690 928 225 401 N
ATOM 1082 CA TRP A 241 -55.292-145.453 309.261 1.00100.06 C
ANISOU 1082 CA TRP A 241 11122 11277 15618 771 261 263 C
ATOM 1083 C TRP A 241 -56.204-146.589 309.710 1.00 93.92 C
ANISOU 1083 C TRP A 241 10272 10668 14746 596 201 276 C
ATOM 1084 O TRP A 241 -55.729-147.696 309.988 1.00 86.57 O
ANISOU 1084 O TRP A 241 9479 9723 13690 435 107 253 O
ATOM 1085 CB TRP A 241 -55.011-144.501 310.424 1.00107.74 C
ANISOU 1085 CB TRP A 241 12094 12165 16677 825 464 125 C
ATOM 1086 CG TRP A 241 -53.674-143.838 310.332 1.00110.32 C
ANISOU 1086 CG TRP A 241 12581 12306 17030 889 505 64 C
ATOM 1087 CD1 TRP A 241 -53.375-142.680 309.676 1.00111.38 C
ANISOU 1087 CD1 TRP A 241 12700 12294 17324 1048 552 112 C
ATOM 1088 CD2 TRP A 241 -52.447-144.296 310.915 1.00109.15 C
ANISOU 1088 CD2 TRP A 241 12620 12104 16746 785 496 -41 C
ATOM 1089 NE1 TRP A 241 -52.040-142.388 309.814 1.00111.00 N
ANISOU 1089 NE1 TRP A 241 12819 12114 17243 1030 583 30 N
ATOM 1090 CE2 TRP A 241 -51.448-143.365 310.570 1.00109.89 C
ANISOU 1090 CE2 TRP A 241 12797 12039 16916 879 548 -74 C
ATOM 1091 CE3 TRP A 241 -52.098-145.403 311.695 1.00108.15 C
ANISOU 1091 CE3 TRP A 241 12591 12050 16451 620 440 -89 C
ATOM 1092 CZ2 TRP A 241 -50.123-143.506 310.979 1.00109.40 C
ANISOU 1092 CZ2 TRP A 241 12897 11918 16753 814 551 -178 C
ATOM 1093 CZ3 TRP A 241 -50.782-145.542 312.100 1.00107.96 C
ANISOU 1093 CZ3 TRP A 241 12729 11955 16336 577 433 -174 C
ATOM 1094 CH2 TRP A 241 -49.811-144.598 311.741 1.00107.76 C
ANISOU 1094 CH2 TRP A 241 12768 11799 16375 675 491 -231 C
ATOM 1095 N THR A 242 -57.513-146.336 309.792 1.00 99.72 N
ANISOU 1095 N THR A 242 10783 11555 15553 622 251 320 N
ATOM 1096 CA THR A 242 -58.439-147.380 310.222 1.00102.90 C
ANISOU 1096 CA THR A 242 11095 12139 15865 428 203 343 C
ATOM 1097 C THR A 242 -58.447-148.543 309.238 1.00106.17 C
ANISOU 1097 C THR A 242 11573 12576 16192 306 -12 419 C
ATOM 1098 O THR A 242 -58.386-149.711 309.640 1.00110.97 O
ANISOU 1098 O THR A 242 12270 13186 16706 100 -94 413 O
ATOM 1099 CB THR A 242 -59.848-146.807 310.387 1.00100.14 C
ANISOU 1099 CB THR A 242 10457 11978 15613 496 299 365 C
ATOM 1100 OG1 THR A 242 -60.285-146.241 309.145 1.00101.62 O
ANISOU 1100 OG1 THR A 242 10519 12184 15907 669 224 479 O
ATOM 1101 CG2 THR A 242 -59.866-145.733 311.464 1.00100.35 C
ANISOU 1101 CG2 THR A 242 10408 11984 15735 606 524 230 C
ATOM 1102 N ILE A 243 -58.516-148.240 307.939 1.00 98.73 N
ANISOU 1102 N ILE A 243 10579 11651 15284 423 -108 492 N
ATOM 1103 CA ILE A 243 -58.473-149.294 306.929 1.00 89.58 C
ANISOU 1103 CA ILE A 243 9467 10537 14033 310 -307 515 C
ATOM 1104 C ILE A 243 -57.159-150.059 307.015 1.00 90.43 C
ANISOU 1104 C ILE A 243 9834 10460 14066 231 -382 423 C
ATOM 1105 O ILE A 243 -57.132-151.292 306.907 1.00 93.63 O
ANISOU 1105 O ILE A 243 10314 10845 14417 61 -514 385 O
ATOM 1106 CB ILE A 243 -58.694-148.701 305.526 1.00 87.31 C
ANISOU 1106 CB ILE A 243 9063 10352 13759 455 -387 611 C
ATOM 1107 CG1 ILE A 243 -60.119-148.159 305.394 1.00 86.61 C
ANISOU 1107 CG1 ILE A 243 8688 10469 13749 523 -353 719 C
ATOM 1108 CG2 ILE A 243 -58.420-149.743 304.451 1.00 84.60 C
ANISOU 1108 CG2 ILE A 243 8784 10066 13293 338 -582 576 C
ATOM 1109 CD1 ILE A 243 -60.392-147.490 304.064 1.00 89.61 C
ANISOU 1109 CD1 ILE A 243 8929 10975 14144 676 -438 864 C
ATOM 1110 N ALA A 244 -56.049-149.345 307.220 1.00 92.61 N
ANISOU 1110 N ALA A 244 10241 10590 14358 354 -301 379 N
ATOM 1111 CA ALA A 244 -54.765-150.017 307.386 1.00 95.59 C
ANISOU 1111 CA ALA A 244 10840 10810 14669 300 -365 286 C
ATOM 1112 C ALA A 244 -54.783-150.946 308.594 1.00 99.99 C
ANISOU 1112 C ALA A 244 11478 11315 15197 126 -368 263 C
ATOM 1113 O ALA A 244 -54.247-152.059 308.539 1.00104.90 O
ANISOU 1113 O ALA A 244 12234 11836 15788 21 -500 224 O
ATOM 1114 CB ALA A 244 -53.641-148.989 307.514 1.00 91.61 C
ANISOU 1114 CB ALA A 244 10432 10190 14185 447 -259 245 C
ATOM 1115 N ILE A 245 -55.404-150.512 309.692 1.00 98.52 N
ANISOU 1115 N ILE A 245 11202 11204 15026 92 -225 288 N
ATOM 1116 CA ILE A 245 -55.512-151.378 310.861 1.00100.09 C
ANISOU 1116 CA ILE A 245 11453 11409 15166 -102 -227 308 C
ATOM 1117 C ILE A 245 -56.477-152.525 310.586 1.00102.41 C
ANISOU 1117 C ILE A 245 11681 11771 15458 -292 -359 381 C
ATOM 1118 O ILE A 245 -56.195-153.681 310.921 1.00102.41 O
ANISOU 1118 O ILE A 245 11803 11668 15439 -459 -475 412 O
ATOM 1119 CB ILE A 245 -55.936-150.565 312.098 1.00100.08 C
ANISOU 1119 CB ILE A 245 11345 11533 15149 -103 -24 289 C
ATOM 1120 CG1 ILE A 245 -54.856-149.544 312.460 1.00 98.98 C
ANISOU 1120 CG1 ILE A 245 11295 11297 15018 47 97 186 C
ATOM 1121 CG2 ILE A 245 -56.213-151.491 313.275 1.00 99.00 C
ANISOU 1121 CG2 ILE A 245 11227 11477 14914 -340 -31 352 C
ATOM 1122 CD1 ILE A 245 -55.209-148.682 313.651 1.00 98.50 C
ANISOU 1122 CD1 ILE A 245 11121 11358 14945 53 308 107 C
ATOM 1123 N VAL A 246 -57.618-152.228 309.959 1.00101.74 N
ANISOU 1123 N VAL A 246 11397 11851 15410 -273 -352 417 N
ATOM 1124 CA VAL A 246 -58.636-153.251 309.726 1.00 97.15 C
ANISOU 1124 CA VAL A 246 10722 11367 14825 -477 -465 475 C
ATOM 1125 C VAL A 246 -58.069-154.394 308.892 1.00 93.02 C
ANISOU 1125 C VAL A 246 10352 10678 14314 -561 -671 429 C
ATOM 1126 O VAL A 246 -58.247-155.572 309.221 1.00 95.30 O
ANISOU 1126 O VAL A 246 10705 10887 14618 -778 -776 461 O
ATOM 1127 CB VAL A 246 -59.880-152.629 309.065 1.00 99.87 C
ANISOU 1127 CB VAL A 246 10802 11943 15200 -409 -431 511 C
ATOM 1128 CG1 VAL A 246 -60.727-153.703 308.404 1.00102.77 C
ANISOU 1128 CG1 VAL A 246 11086 12404 15559 -607 -591 537 C
ATOM 1129 CG2 VAL A 246 -60.700-151.873 310.097 1.00101.05 C
ANISOU 1129 CG2 VAL A 246 10766 12270 15357 -393 -240 536 C
ATOM 1130 N ILE A 247 -57.365-154.062 307.807 1.00 92.13 N
ANISOU 1130 N ILE A 247 10294 10509 14202 -397 -729 349 N
ATOM 1131 CA ILE A 247 -56.827-155.099 306.928 1.00100.12 C
ANISOU 1131 CA ILE A 247 11423 11395 15224 -458 -914 250 C
ATOM 1132 C ILE A 247 -55.800-155.951 307.665 1.00104.74 C
ANISOU 1132 C ILE A 247 12229 11723 15844 -527 -973 218 C
ATOM 1133 O ILE A 247 -55.785-157.182 307.536 1.00109.88 O
ANISOU 1133 O ILE A 247 12959 12230 16559 -680 -1122 179 O
ATOM 1134 CB ILE A 247 -56.230-154.468 305.657 1.00100.24 C
ANISOU 1134 CB ILE A 247 11428 11463 15195 -269 -943 170 C
ATOM 1135 CG1 ILE A 247 -57.309-153.720 304.875 1.00 99.96 C
ANISOU 1135 CG1 ILE A 247 11158 11691 15130 -210 -919 247 C
ATOM 1136 CG2 ILE A 247 -55.591-155.533 304.779 1.00103.69 C
ANISOU 1136 CG2 ILE A 247 11973 11794 15630 -325 -1118 11 C
ATOM 1137 CD1 ILE A 247 -56.794-153.069 303.613 1.00100.38 C
ANISOU 1137 CD1 ILE A 247 11183 11840 15116 -47 -954 222 C
ATOM 1138 N ALA A 248 -54.932-155.315 308.454 1.00100.85 N
ANISOU 1138 N ALA A 248 11832 11162 15324 -416 -863 233 N
ATOM 1139 CA ALA A 248 -53.874-156.045 309.140 1.00 98.78 C
ANISOU 1139 CA ALA A 248 11764 10683 15086 -453 -928 220 C
ATOM 1140 C ALA A 248 -54.371-156.818 310.355 1.00100.92 C
ANISOU 1140 C ALA A 248 12056 10918 15370 -671 -941 365 C
ATOM 1141 O ALA A 248 -53.674-157.725 310.820 1.00109.63 O
ANISOU 1141 O ALA A 248 13311 11819 16524 -740 -1051 397 O
ATOM 1142 CB ALA A 248 -52.761-155.087 309.562 1.00 98.97 C
ANISOU 1142 CB ALA A 248 11862 10686 15054 -278 -812 183 C
ATOM 1143 N VAL A 249 -55.547-156.479 310.886 1.00 98.35 N
ANISOU 1143 N VAL A 249 11571 10795 15003 -780 -836 467 N
ATOM 1144 CA VAL A 249 -56.112-157.239 311.997 1.00102.14 C
ANISOU 1144 CA VAL A 249 12046 11294 15467 -1027 -846 625 C
ATOM 1145 C VAL A 249 -56.895-158.456 311.509 1.00103.76 C
ANISOU 1145 C VAL A 249 12231 11422 15769 -1245 -1009 667 C
ATOM 1146 O VAL A 249 -57.072-159.416 312.274 1.00110.66 O
ANISOU 1146 O VAL A 249 13166 12202 16676 -1471 -1083 813 O
ATOM 1147 CB VAL A 249 -56.975-156.312 312.879 1.00108.04 C
ANISOU 1147 CB VAL A 249 12610 12331 16109 -1056 -640 687 C
ATOM 1148 CG1 VAL A 249 -57.729-157.087 313.949 1.00109.97 C
ANISOU 1148 CG1 VAL A 249 12806 12676 16303 -1348 -641 862 C
ATOM 1149 CG2 VAL A 249 -56.099-155.262 313.547 1.00113.01 C
ANISOU 1149 CG2 VAL A 249 13285 12992 16661 -885 -489 627 C
ATOM 1150 N LEU A 250 -57.325-158.463 310.246 1.00 98.12 N
ANISOU 1150 N LEU A 250 11436 10745 15102 -1196 -1075 546 N
ATOM 1151 CA LEU A 250 -58.045-159.605 309.682 1.00 98.19 C
ANISOU 1151 CA LEU A 250 11417 10684 15207 -1411 -1233 537 C
ATOM 1152 C LEU A 250 -57.383-160.953 309.952 1.00103.90 C
ANISOU 1152 C LEU A 250 12346 11060 16072 -1549 -1407 561 C
ATOM 1153 O LEU A 250 -58.098-161.890 310.340 1.00105.79 O
ANISOU 1153 O LEU A 250 12572 11234 16388 -1821 -1486 680 O
ATOM 1154 CB LEU A 250 -58.241-159.393 308.174 1.00 92.61 C
ANISOU 1154 CB LEU A 250 10620 10064 14505 -1300 -1297 357 C
ATOM 1155 CG LEU A 250 -59.196-158.275 307.760 1.00 89.44 C
ANISOU 1155 CG LEU A 250 9975 10003 14005 -1206 -1174 377 C
ATOM 1156 CD1 LEU A 250 -59.367-158.240 306.249 1.00 91.24 C
ANISOU 1156 CD1 LEU A 250 10114 10336 14217 -1133 -1273 233 C
ATOM 1157 CD2 LEU A 250 -60.539-158.442 308.452 1.00 92.77 C
ANISOU 1157 CD2 LEU A 250 10217 10621 14410 -1425 -1117 516 C
ATOM 1158 N PRO A 251 -56.063-161.132 309.776 1.00103.11 N
ANISOU 1158 N PRO A 251 12426 10721 16031 -1382 -1478 463 N
ATOM 1159 CA PRO A 251 -55.473-162.445 310.102 1.00105.02 C
ANISOU 1159 CA PRO A 251 12849 10604 16450 -1497 -1654 504 C
ATOM 1160 C PRO A 251 -55.681-162.857 311.548 1.00106.03 C
ANISOU 1160 C PRO A 251 13022 10695 16569 -1700 -1641 794 C
ATOM 1161 O PRO A 251 -55.876-164.046 311.828 1.00114.67 O
ANISOU 1161 O PRO A 251 14198 11547 17826 -1916 -1790 912 O
ATOM 1162 CB PRO A 251 -53.987-162.252 309.773 1.00102.17 C
ANISOU 1162 CB PRO A 251 12627 10080 16111 -1230 -1688 351 C
ATOM 1163 CG PRO A 251 -53.961-161.165 308.777 1.00 99.96 C
ANISOU 1163 CG PRO A 251 12237 10039 15703 -1032 -1585 172 C
ATOM 1164 CD PRO A 251 -55.061-160.231 309.175 1.00100.45 C
ANISOU 1164 CD PRO A 251 12123 10417 15625 -1090 -1419 304 C
ATOM 1165 N LEU A 252 -55.647-161.904 312.479 1.00102.07 N
ANISOU 1165 N LEU A 252 12465 10435 15882 -1648 -1467 913 N
ATOM 1166 CA LEU A 252 -55.880-162.234 313.880 1.00103.29 C
ANISOU 1166 CA LEU A 252 12633 10641 15972 -1860 -1440 1190 C
ATOM 1167 C LEU A 252 -57.334-162.620 314.120 1.00107.69 C
ANISOU 1167 C LEU A 252 13037 11366 16512 -2162 -1419 1329 C
ATOM 1168 O LEU A 252 -57.621-163.515 314.924 1.00 94.15 O
ANISOU 1168 O LEU A 252 11366 9568 14838 -2430 -1498 1571 O
ATOM 1169 CB LEU A 252 -55.477-161.053 314.763 1.00110.89 C
ANISOU 1169 CB LEU A 252 13549 11864 16720 -1729 -1244 1219 C
ATOM 1170 CG LEU A 252 -55.690-161.198 316.270 1.00117.52 C
ANISOU 1170 CG LEU A 252 14368 12868 17417 -1941 -1183 1483 C
ATOM 1171 CD1 LEU A 252 -54.991-162.436 316.786 1.00125.32 C
ANISOU 1171 CD1 LEU A 252 15542 13549 18525 -2064 -1387 1693 C
ATOM 1172 CD2 LEU A 252 -55.195-159.960 317.000 1.00114.31 C
ANISOU 1172 CD2 LEU A 252 13909 12720 16802 -1786 -985 1423 C
ATOM 1173 N LEU A 253 -58.265-161.959 313.430 1.00131.19 N
ANISOU 1173 N LEU A 253 15823 14594 19431 -2131 -1320 1198 N
ATOM 1174 CA LEU A 253 -59.678-162.293 313.573 1.00145.45 C
ANISOU 1174 CA LEU A 253 17449 16598 21216 -2412 -1298 1305 C
ATOM 1175 C LEU A 253 -59.994-163.629 312.911 1.00147.33 C
ANISOU 1175 C LEU A 253 17756 16556 21666 -2627 -1511 1299 C
ATOM 1176 O LEU A 253 -60.591-164.516 313.533 1.00151.17 O
ANISOU 1176 O LEU A 253 18240 16992 22207 -2947 -1576 1507 O
ATOM 1177 CB LEU A 253 -60.536-161.175 312.977 1.00153.28 C
ANISOU 1177 CB LEU A 253 18200 17938 22102 -2281 -1145 1163 C
ATOM 1178 CG LEU A 253 -62.008-161.482 312.696 1.00162.78 C
ANISOU 1178 CG LEU A 253 19181 19363 23306 -2519 -1147 1198 C
ATOM 1179 CD1 LEU A 253 -62.760-161.778 313.985 1.00167.56 C
ANISOU 1179 CD1 LEU A 253 19685 20168 23810 -2818 -1065 1435 C
ATOM 1180 CD2 LEU A 253 -62.658-160.333 311.938 1.00163.31 C
ANISOU 1180 CD2 LEU A 253 19018 19734 23299 -2312 -1027 1049 C
ATOM 1181 N GLY A 254 -59.607-163.783 311.657 1.00139.69 N
ANISOU 1181 N GLY A 254 16842 15415 20818 -2471 -1617 1055 N
ATOM 1182 CA GLY A 254 -59.795-165.022 310.925 1.00136.65 C
ANISOU 1182 CA GLY A 254 16525 14742 20654 -2648 -1819 970 C
ATOM 1183 C GLY A 254 -58.880-164.996 309.726 1.00133.50 C
ANISOU 1183 C GLY A 254 16220 14164 20341 -2386 -1907 669 C
ATOM 1184 O GLY A 254 -57.772-164.465 309.798 1.00134.99 O
ANISOU 1184 O GLY A 254 16515 14290 20485 -2121 -1868 613 O
ATOM 1185 N TRP A 255 -59.342-165.582 308.618 1.00130.88 N
ANISOU 1185 N TRP A 255 15834 13779 20117 -2476 -2023 461 N
ATOM 1186 CA TRP A 255 -58.668-165.460 307.318 1.00126.35 C
ANISOU 1186 CA TRP A 255 15285 13159 19564 -2249 -2087 137 C
ATOM 1187 C TRP A 255 -57.161-165.698 307.426 1.00131.56 C
ANISOU 1187 C TRP A 255 16163 13491 20332 -2030 -2151 57 C
ATOM 1188 O TRP A 255 -56.351-164.969 306.849 1.00128.84 O
ANISOU 1188 O TRP A 255 15828 13240 19886 -1754 -2098 -107 O
ATOM 1189 CB TRP A 255 -58.956-164.098 306.686 1.00116.01 C
ANISOU 1189 CB TRP A 255 13791 12273 18015 -2043 -1939 62 C
ATOM 1190 CG TRP A 255 -58.664-164.034 305.219 1.00118.37 C
ANISOU 1190 CG TRP A 255 14045 12642 18289 -1905 -2010 -243 C
ATOM 1191 CD1 TRP A 255 -58.165-165.032 304.433 1.00125.14 C
ANISOU 1191 CD1 TRP A 255 14999 13244 19306 -1939 -2175 -503 C
ATOM 1192 CD2 TRP A 255 -58.859-162.908 304.357 1.00119.40 C
ANISOU 1192 CD2 TRP A 255 14008 13141 18217 -1720 -1921 -319 C
ATOM 1193 NE1 TRP A 255 -58.035-164.597 303.137 1.00127.15 N
ANISOU 1193 NE1 TRP A 255 15147 13734 19431 -1799 -2184 -751 N
ATOM 1194 CE2 TRP A 255 -58.456-163.296 303.064 1.00123.88 C
ANISOU 1194 CE2 TRP A 255 14573 13702 18792 -1668 -2037 -615 C
ATOM 1195 CE3 TRP A 255 -59.337-161.608 304.552 1.00118.12 C
ANISOU 1195 CE3 TRP A 255 13689 13309 17882 -1591 -1758 -165 C
ATOM 1196 CZ2 TRP A 255 -58.517-162.433 301.972 1.00124.56 C
ANISOU 1196 CZ2 TRP A 255 14508 14134 18685 -1511 -2001 -719 C
ATOM 1197 CZ3 TRP A 255 -59.395-160.753 303.469 1.00119.21 C
ANISOU 1197 CZ3 TRP A 255 13688 13731 17875 -1417 -1730 -258 C
ATOM 1198 CH2 TRP A 255 -58.987-161.168 302.195 1.00123.05 C
ANISOU 1198 CH2 TRP A 255 14177 14237 18340 -1388 -1854 -512 C
ATOM 1199 N ASN A 256 -56.782-166.715 308.191 1.00141.38 N
ANISOU 1199 N ASN A 256 17574 14360 21786 -2157 -2268 195 N
ATOM 1200 CA ASN A 256 -55.390-167.122 308.328 1.00142.47 C
ANISOU 1200 CA ASN A 256 17906 14154 22072 -1961 -2361 130 C
ATOM 1201 C ASN A 256 -55.247-168.571 307.875 1.00148.34 C
ANISOU 1201 C ASN A 256 18760 14447 23156 -2087 -2580 -21 C
ATOM 1202 O ASN A 256 -56.231-169.246 307.563 1.00145.84 O
ANISOU 1202 O ASN A 256 18382 14080 22952 -2355 -2653 -52 O
ATOM 1203 CB ASN A 256 -54.895-166.926 309.766 1.00139.06 C
ANISOU 1203 CB ASN A 256 17571 13677 21590 -1948 -2309 463 C
ATOM 1204 CG ASN A 256 -55.704-167.714 310.777 1.00136.94 C
ANISOU 1204 CG ASN A 256 17320 13298 21414 -2288 -2365 793 C
ATOM 1205 OD1 ASN A 256 -55.486-168.909 310.968 1.00145.55 O
ANISOU 1205 OD1 ASN A 256 18544 13977 22782 -2419 -2546 868 O
ATOM 1206 ND2 ASN A 256 -56.633-167.040 311.446 1.00131.20 N
ANISOU 1206 ND2 ASN A 256 16450 12940 20462 -2434 -2207 997 N
ATOM 1207 N CYS A 257 -54.003-169.048 307.835 1.00156.48 N
ANISOU 1207 N CYS A 257 19945 15140 24368 -1888 -2686 -134 N
ATOM 1208 CA CYS A 257 -53.743-170.374 307.293 1.00163.75 C
ANISOU 1208 CA CYS A 257 20955 15727 25536 -1897 -2828 -339 C
ATOM 1209 C CYS A 257 -54.126-171.496 308.249 1.00165.07 C
ANISOU 1209 C CYS A 257 21222 15650 25848 -2109 -2891 -30 C
ATOM 1210 O CYS A 257 -54.334-172.627 307.797 1.00170.11 O
ANISOU 1210 O CYS A 257 21901 16062 26673 -2196 -2978 -172 O
ATOM 1211 CB CYS A 257 -52.269-170.525 306.904 1.00171.31 C
ANISOU 1211 CB CYS A 257 22000 16555 26534 -1545 -2852 -570 C
ATOM 1212 SG CYS A 257 -51.995-171.927 305.790 1.00182.23 S
ANISOU 1212 SG CYS A 257 23413 17681 28144 -1497 -2965 -972 S
ATOM 1213 N GLU A 258 -54.224-171.220 309.549 1.00155.81 N
ANISOU 1213 N GLU A 258 20083 14525 24591 -2205 -2849 384 N
ATOM 1214 CA GLU A 258 -54.589-172.260 310.503 1.00152.91 C
ANISOU 1214 CA GLU A 258 19800 13961 24339 -2424 -2915 713 C
ATOM 1215 C GLU A 258 -56.077-172.275 310.822 1.00151.50 C
ANISOU 1215 C GLU A 258 19510 13958 24095 -2810 -2871 914 C
ATOM 1216 O GLU A 258 -56.638-173.350 311.062 1.00158.47 O
ANISOU 1216 O GLU A 258 20436 14658 25118 -3036 -2940 1037 O
ATOM 1217 CB GLU A 258 -53.794-172.096 311.802 1.00153.58 C
ANISOU 1217 CB GLU A 258 19976 14024 24354 -2331 -2912 1068 C
ATOM 1218 CG GLU A 258 -52.294-172.282 311.648 1.00154.14 C
ANISOU 1218 CG GLU A 258 20146 13911 24508 -1973 -2973 917 C
ATOM 1219 CD GLU A 258 -51.581-172.400 312.983 1.00154.32 C
ANISOU 1219 CD GLU A 258 20254 13887 24496 -1931 -3011 1297 C
ATOM 1220 OE1 GLU A 258 -52.243-172.241 314.031 1.00153.60 O
ANISOU 1220 OE1 GLU A 258 20143 13935 24283 -2181 -2977 1676 O
ATOM 1221 OE2 GLU A 258 -50.359-172.658 312.983 1.00154.31 O
ANISOU 1221 OE2 GLU A 258 20318 13736 24576 -1659 -3077 1217 O
ATOM 1222 N LYS A 259 -56.728-171.109 310.831 1.00145.76 N
ANISOU 1222 N LYS A 259 18625 13590 23166 -2895 -2756 950 N
ATOM 1223 CA LYS A 259 -58.160-171.068 311.106 1.00140.81 C
ANISOU 1223 CA LYS A 259 17845 13199 22457 -3258 -2702 1125 C
ATOM 1224 C LYS A 259 -58.947-171.774 310.010 1.00136.38 C
ANISOU 1224 C LYS A 259 17216 12577 22024 -3412 -2770 843 C
ATOM 1225 O LYS A 259 -59.953-172.439 310.283 1.00142.00 O
ANISOU 1225 O LYS A 259 17879 13307 22767 -3729 -2779 987 O
ATOM 1226 CB LYS A 259 -58.626-169.620 311.250 1.00138.23 C
ANISOU 1226 CB LYS A 259 17326 13372 21823 -3212 -2512 1161 C
ATOM 1227 CG LYS A 259 -59.826-169.436 312.162 1.00140.13 C
ANISOU 1227 CG LYS A 259 17414 13943 21888 -3527 -2399 1474 C
ATOM 1228 CD LYS A 259 -59.470-169.778 313.599 1.00141.25 C
ANISOU 1228 CD LYS A 259 17668 13979 22022 -3658 -2416 1885 C
ATOM 1229 CE LYS A 259 -60.615-169.462 314.544 1.00144.04 C
ANISOU 1229 CE LYS A 259 17838 14753 22137 -3958 -2271 2175 C
ATOM 1230 NZ LYS A 259 -60.265-169.776 315.956 1.00147.44 N
ANISOU 1230 NZ LYS A 259 18362 15148 22511 -4107 -2286 2589 N
ATOM 1231 N LEU A 260 -58.501-171.642 308.766 1.00130.44 N
ANISOU 1231 N LEU A 260 16451 11781 21330 -3205 -2813 431 N
ATOM 1232 CA LEU A 260 -59.110-172.299 307.623 1.00138.42 C
ANISOU 1232 CA LEU A 260 17394 12755 22445 -3330 -2882 103 C
ATOM 1233 C LEU A 260 -58.150-173.346 307.077 1.00145.61 C
ANISOU 1233 C LEU A 260 18480 13274 23570 -3140 -2981 -159 C
ATOM 1234 O LEU A 260 -56.929-173.204 307.188 1.00145.11 O
ANISOU 1234 O LEU A 260 18533 13073 23531 -2832 -2990 -201 O
ATOM 1235 CB LEU A 260 -59.448-171.295 306.515 1.00140.77 C
ANISOU 1235 CB LEU A 260 17483 13397 22606 -3269 -2857 -192 C
ATOM 1236 CG LEU A 260 -60.605-170.297 306.614 1.00147.40 C
ANISOU 1236 CG LEU A 260 18077 14787 23141 -3378 -2701 -50 C
ATOM 1237 CD1 LEU A 260 -60.566-169.467 307.888 1.00149.21 C
ANISOU 1237 CD1 LEU A 260 18302 15220 23169 -3316 -2540 327 C
ATOM 1238 CD2 LEU A 260 -60.565-169.386 305.397 1.00146.18 C
ANISOU 1238 CD2 LEU A 260 17770 15014 22759 -3136 -2630 -359 C
ATOM 1239 N GLN A 261 -58.703-174.406 306.493 1.00150.53 N
ANISOU 1239 N GLN A 261 19109 13734 24353 -3329 -3051 -345 N
ATOM 1240 CA GLN A 261 -57.862-175.331 305.746 1.00151.92 C
ANISOU 1240 CA GLN A 261 19404 13585 24734 -3146 -3134 -682 C
ATOM 1241 C GLN A 261 -57.286-174.571 304.558 1.00149.36 C
ANISOU 1241 C GLN A 261 18988 13477 24285 -2889 -3117 -1097 C
ATOM 1242 O GLN A 261 -57.958-174.410 303.534 1.00149.52 O
ANISOU 1242 O GLN A 261 18855 13729 24226 -3007 -3123 -1392 O
ATOM 1243 CB GLN A 261 -58.656-176.562 305.299 1.00155.33 C
ANISOU 1243 CB GLN A 261 19843 13818 25356 -3429 -3201 -831 C
ATOM 1244 CG GLN A 261 -57.820-177.637 304.614 1.00158.45 C
ANISOU 1244 CG GLN A 261 20362 13841 26002 -3261 -3284 -1170 C
ATOM 1245 CD GLN A 261 -58.615-178.897 304.306 1.00163.64 C
ANISOU 1245 CD GLN A 261 21045 14254 26876 -3567 -3346 -1289 C
ATOM 1246 OE1 GLN A 261 -59.561-179.241 305.015 1.00166.29 O
ANISOU 1246 OE1 GLN A 261 21378 14563 27243 -3887 -3341 -984 O
ATOM 1247 NE2 GLN A 261 -58.232-179.590 303.239 1.00165.15 N
ANISOU 1247 NE2 GLN A 261 21255 14282 27212 -3479 -3397 -1744 N
ATOM 1248 N SER A 262 -56.056-174.076 304.691 1.00148.81 N
ANISOU 1248 N SER A 262 18991 13374 24176 -2550 -3096 -1116 N
ATOM 1249 CA SER A 262 -55.524-173.104 303.747 1.00148.23 C
ANISOU 1249 CA SER A 262 18814 13575 23931 -2316 -3057 -1428 C
ATOM 1250 C SER A 262 -54.100-173.462 303.350 1.00147.70 C
ANISOU 1250 C SER A 262 18846 13324 23950 -1978 -3080 -1677 C
ATOM 1251 O SER A 262 -53.406-174.205 304.045 1.00145.77 O
ANISOU 1251 O SER A 262 18745 12762 23878 -1878 -3121 -1523 O
ATOM 1252 CB SER A 262 -55.551-171.687 304.339 1.00148.11 C
ANISOU 1252 CB SER A 262 18729 13842 23706 -2255 -2968 -1171 C
ATOM 1253 OG SER A 262 -56.847-171.346 304.798 1.00150.73 O
ANISOU 1253 OG SER A 262 18940 14367 23963 -2562 -2938 -917 O
ATOM 1254 N VAL A 263 -53.649-172.855 302.268 1.00151.56 N
ANISOU 1254 N VAL A 263 19230 14051 24305 -1808 -3059 -2058 N
ATOM 1255 CA VAL A 263 -52.297-173.054 301.815 1.00153.78 C
ANISOU 1255 CA VAL A 263 19556 14272 24601 -1471 -3054 -2302 C
ATOM 1256 C VAL A 263 -51.514-171.910 302.425 1.00149.75 C
ANISOU 1256 C VAL A 263 19077 13880 23943 -1259 -2981 -2063 C
ATOM 1257 O VAL A 263 -51.821-170.753 302.199 1.00146.68 O
ANISOU 1257 O VAL A 263 18601 13767 23365 -1307 -2919 -1955 O
ATOM 1258 CB VAL A 263 -52.223-172.952 300.299 1.00155.69 C
ANISOU 1258 CB VAL A 263 19655 14779 24722 -1405 -3051 -2811 C
ATOM 1259 CG1 VAL A 263 -50.809-173.217 299.828 1.00157.32 C
ANISOU 1259 CG1 VAL A 263 19904 14831 25039 -1138 -3068 -3117 C
ATOM 1260 CG2 VAL A 263 -53.201-173.926 299.671 1.00157.89 C
ANISOU 1260 CG2 VAL A 263 19838 15128 25024 -1716 -3099 -2990 C
ATOM 1261 N CYS A 264 -50.511-172.244 303.217 1.00149.71 N
ANISOU 1261 N CYS A 264 19180 13671 24030 -1031 -2991 -1984 N
ATOM 1262 CA CYS A 264 -49.695-171.255 303.907 1.00146.95 C
ANISOU 1262 CA CYS A 264 18874 13410 23550 -858 -2924 -1723 C
ATOM 1263 C CYS A 264 -48.520-170.589 303.168 1.00141.16 C
ANISOU 1263 C CYS A 264 18077 12893 22666 -569 -2867 -2017 C
ATOM 1264 O CYS A 264 -48.125-171.012 302.088 1.00140.92 O
ANISOU 1264 O CYS A 264 17977 12914 22652 -474 -2888 -2414 O
ATOM 1265 CB CYS A 264 -49.294-171.810 305.265 1.00153.12 C
ANISOU 1265 CB CYS A 264 19793 13894 24491 -803 -2977 -1408 C
ATOM 1266 SG CYS A 264 -50.761-172.206 306.236 1.00160.62 S
ANISOU 1266 SG CYS A 264 20824 14640 25565 -1149 -3028 -948 S
ATOM 1267 N SER A 265 -47.992-169.524 303.772 1.00133.17 N
ANISOU 1267 N SER A 265 17078 12024 21494 -443 -2787 -1819 N
ATOM 1268 CA SER A 265 -46.879-168.760 303.232 1.00126.86 C
ANISOU 1268 CA SER A 265 16227 11436 20539 -179 -2720 -2034 C
ATOM 1269 C SER A 265 -45.565-169.287 303.790 1.00124.51 C
ANISOU 1269 C SER A 265 15999 10980 20328 39 -2746 -1985 C
ATOM 1270 O SER A 265 -45.466-169.601 304.979 1.00116.51 O
ANISOU 1270 O SER A 265 15085 9784 19401 6 -2778 -1645 O
ATOM 1271 CB SER A 265 -47.030-167.279 303.578 1.00121.37 C
ANISOU 1271 CB SER A 265 15502 10980 19633 -168 -2613 -1860 C
ATOM 1272 OG SER A 265 -45.867-166.554 303.223 1.00116.63 O
ANISOU 1272 OG SER A 265 14867 10562 18884 81 -2541 -2018 O
ATOM 1273 N ASP A 266 -44.554-169.376 302.930 1.00131.99 N
ANISOU 1273 N ASP A 266 16877 12029 21246 250 -2738 -2324 N
ATOM 1274 CA ASP A 266 -43.236-169.840 303.345 1.00140.35 C
ANISOU 1274 CA ASP A 266 17963 12974 22389 467 -2769 -2319 C
ATOM 1275 C ASP A 266 -42.355-168.718 303.862 1.00137.46 C
ANISOU 1275 C ASP A 266 17590 12818 21819 623 -2677 -2187 C
ATOM 1276 O ASP A 266 -41.218-168.977 304.271 1.00138.64 O
ANISOU 1276 O ASP A 266 17748 12916 22013 798 -2703 -2167 O
ATOM 1277 CB ASP A 266 -42.534-170.537 302.184 1.00150.87 C
ANISOU 1277 CB ASP A 266 19200 14325 23801 612 -2804 -2764 C
ATOM 1278 CG ASP A 266 -43.462-171.435 301.417 1.00161.26 C
ANISOU 1278 CG ASP A 266 20494 15512 25266 448 -2867 -2984 C
ATOM 1279 OD1 ASP A 266 -43.720-172.557 301.896 1.00166.29 O
ANISOU 1279 OD1 ASP A 266 21214 15804 26166 370 -2965 -2872 O
ATOM 1280 OD2 ASP A 266 -43.944-171.017 300.345 1.00163.84 O
ANISOU 1280 OD2 ASP A 266 20717 16092 25443 384 -2822 -3265 O
ATOM 1281 N ILE A 267 -42.839-167.482 303.832 1.00127.46 N
ANISOU 1281 N ILE A 267 16301 11785 20343 563 -2574 -2109 N
ATOM 1282 CA ILE A 267 -42.112-166.366 304.412 1.00112.76 C
ANISOU 1282 CA ILE A 267 14443 10104 18297 683 -2474 -1961 C
ATOM 1283 C ILE A 267 -42.838-165.741 305.592 1.00111.57 C
ANISOU 1283 C ILE A 267 14371 9921 18099 538 -2430 -1566 C
ATOM 1284 O ILE A 267 -42.183-165.102 306.432 1.00115.27 O
ANISOU 1284 O ILE A 267 14869 10462 18468 621 -2371 -1384 O
ATOM 1285 CB ILE A 267 -41.807-165.296 303.346 1.00105.92 C
ANISOU 1285 CB ILE A 267 13466 9562 17216 779 -2371 -2233 C
ATOM 1286 CG1 ILE A 267 -43.059-165.003 302.520 1.00105.94 C
ANISOU 1286 CG1 ILE A 267 13416 9651 17184 612 -2369 -2351 C
ATOM 1287 CG2 ILE A 267 -40.674-165.760 302.448 1.00105.10 C
ANISOU 1287 CG2 ILE A 267 13269 9554 17108 963 -2391 -2588 C
ATOM 1288 CD1 ILE A 267 -42.862-163.950 301.458 1.00104.67 C
ANISOU 1288 CD1 ILE A 267 13117 9947 16707 669 -2233 -2515 C
ATOM 1289 N PHE A 268 -44.152-165.904 305.707 1.00110.10 N
ANISOU 1289 N PHE A 268 14205 9648 17978 315 -2454 -1437 N
ATOM 1290 CA PHE A 268 -44.920-165.371 306.833 1.00107.96 C
ANISOU 1290 CA PHE A 268 13987 9362 17671 154 -2410 -1067 C
ATOM 1291 C PHE A 268 -45.724-166.502 307.458 1.00100.97 C
ANISOU 1291 C PHE A 268 13168 8227 16969 -57 -2518 -853 C
ATOM 1292 O PHE A 268 -46.634-167.050 306.800 1.00102.60 O
ANISOU 1292 O PHE A 268 13344 8368 17274 -211 -2570 -970 O
ATOM 1293 CB PHE A 268 -45.839-164.234 306.394 1.00105.86 C
ANISOU 1293 CB PHE A 268 13611 9477 17134 62 -2237 -1039 C
ATOM 1294 CG PHE A 268 -45.107-163.001 305.952 1.00103.81 C
ANISOU 1294 CG PHE A 268 13279 9539 16625 239 -2085 -1143 C
ATOM 1295 CD1 PHE A 268 -44.645-162.082 306.881 1.00105.36 C
ANISOU 1295 CD1 PHE A 268 13496 9864 16673 297 -1964 -939 C
ATOM 1296 CD2 PHE A 268 -44.885-162.758 304.606 1.00102.50 C
ANISOU 1296 CD2 PHE A 268 13017 9562 16366 326 -2064 -1444 C
ATOM 1297 CE1 PHE A 268 -43.970-160.949 306.476 1.00108.52 C
ANISOU 1297 CE1 PHE A 268 13833 10529 16871 436 -1827 -1029 C
ATOM 1298 CE2 PHE A 268 -44.212-161.628 304.197 1.00105.88 C
ANISOU 1298 CE2 PHE A 268 13379 10282 16568 462 -1929 -1502 C
ATOM 1299 CZ PHE A 268 -43.755-160.722 305.134 1.00109.63 C
ANISOU 1299 CZ PHE A 268 13886 10836 16931 515 -1811 -1292 C
ATOM 1300 N PRO A 269 -45.439-166.883 308.699 1.00 93.02 N
ANISOU 1300 N PRO A 269 12245 7090 16010 -87 -2560 -541 N
ATOM 1301 CA PRO A 269 -46.181-167.986 309.318 1.00 93.43 C
ANISOU 1301 CA PRO A 269 12360 6905 16235 -302 -2667 -307 C
ATOM 1302 C PRO A 269 -47.607-167.584 309.661 1.00 95.13 C
ANISOU 1302 C PRO A 269 12548 7196 16401 -588 -2617 -99 C
ATOM 1303 O PRO A 269 -47.893-166.429 309.989 1.00 87.68 O
ANISOU 1303 O PRO A 269 11550 6517 15248 -611 -2478 5 O
ATOM 1304 CB PRO A 269 -45.373-168.297 310.586 1.00 89.34 C
ANISOU 1304 CB PRO A 269 11920 6287 15739 -244 -2724 -8 C
ATOM 1305 CG PRO A 269 -44.044-167.592 310.395 1.00 83.10 C
ANISOU 1305 CG PRO A 269 11100 5648 14827 38 -2668 -182 C
ATOM 1306 CD PRO A 269 -44.354-166.394 309.563 1.00 79.24 C
ANISOU 1306 CD PRO A 269 10533 5411 14166 70 -2528 -398 C
ATOM 1307 N HIS A 270 -48.506-168.567 309.570 1.00103.23 N
ANISOU 1307 N HIS A 270 13586 8057 17581 -804 -2700 -48 N
ATOM 1308 CA HIS A 270 -49.908-168.424 309.957 1.00103.07 C
ANISOU 1308 CA HIS A 270 13521 8105 17535 -1120 -2671 172 C
ATOM 1309 C HIS A 270 -50.657-167.422 309.080 1.00 99.57 C
ANISOU 1309 C HIS A 270 12933 7994 16904 -1142 -2539 -21 C
ATOM 1310 O HIS A 270 -51.584-166.758 309.548 1.00 99.53 O
ANISOU 1310 O HIS A 270 12834 8285 16696 -1291 -2404 174 O
ATOM 1311 CB HIS A 270 -50.043-168.028 311.433 1.00104.81 C
ANISOU 1311 CB HIS A 270 13773 8401 17650 -1249 -2626 602 C
ATOM 1312 CG HIS A 270 -49.155-168.804 312.355 1.00110.55 C
ANISOU 1312 CG HIS A 270 14609 8946 18448 -1174 -2723 820 C
ATOM 1313 ND1 HIS A 270 -48.477-168.218 313.402 1.00109.73 N
ANISOU 1313 ND1 HIS A 270 14537 8946 18212 -1106 -2689 1057 N
ATOM 1314 CD2 HIS A 270 -48.839-170.120 312.392 1.00119.45 C
ANISOU 1314 CD2 HIS A 270 15811 9792 19780 -1162 -2862 843 C
ATOM 1315 CE1 HIS A 270 -47.779-169.139 314.043 1.00110.49 C
ANISOU 1315 CE1 HIS A 270 14714 8852 18416 -1055 -2815 1231 C
ATOM 1316 NE2 HIS A 270 -47.982-170.302 313.451 1.00119.62 N
ANISOU 1316 NE2 HIS A 270 15899 9759 19790 -1082 -2920 1109 N
ATOM 1317 N ILE A 271 -50.284-167.300 307.808 1.00100.18 N
ANISOU 1317 N ILE A 271 12961 8119 16982 -978 -2547 -399 N
ATOM 1318 CA ILE A 271 -50.927-166.357 306.898 1.00105.23 C
ANISOU 1318 CA ILE A 271 13443 9162 17377 -966 -2410 -559 C
ATOM 1319 C ILE A 271 -51.397-167.100 305.655 1.00118.19 C
ANISOU 1319 C ILE A 271 15027 10730 19150 -1053 -2520 -881 C
ATOM 1320 O ILE A 271 -50.639-167.876 305.063 1.00119.48 O
ANISOU 1320 O ILE A 271 15253 10630 19514 -949 -2647 -1159 O
ATOM 1321 CB ILE A 271 -49.991-165.192 306.519 1.00 91.25 C
ANISOU 1321 CB ILE A 271 11634 7656 15382 -686 -2278 -684 C
ATOM 1322 CG1 ILE A 271 -49.996-164.131 307.623 1.00 80.99 C
ANISOU 1322 CG1 ILE A 271 10326 6569 13879 -662 -2115 -388 C
ATOM 1323 CG2 ILE A 271 -50.401-164.570 305.189 1.00 81.72 C
ANISOU 1323 CG2 ILE A 271 10277 6768 14004 -644 -2212 -929 C
ATOM 1324 CD1 ILE A 271 -49.311-162.843 307.231 1.00 70.50 C
ANISOU 1324 CD1 ILE A 271 8939 5520 12327 -438 -1965 -489 C
ATOM 1325 N ASP A 272 -52.649-166.863 305.268 1.00127.81 N
ANISOU 1325 N ASP A 272 16109 12199 20254 -1243 -2470 -861 N
ATOM 1326 CA ASP A 272 -53.202-167.428 304.046 1.00133.73 C
ANISOU 1326 CA ASP A 272 16767 12978 21067 -1350 -2559 -1176 C
ATOM 1327 C ASP A 272 -52.699-166.656 302.833 1.00132.37 C
ANISOU 1327 C ASP A 272 16488 13132 20676 -1135 -2493 -1469 C
ATOM 1328 O ASP A 272 -52.629-165.423 302.850 1.00130.67 O
ANISOU 1328 O ASP A 272 16198 13251 20201 -1003 -2342 -1348 O
ATOM 1329 CB ASP A 272 -54.731-167.397 304.100 1.00137.66 C
ANISOU 1329 CB ASP A 272 17130 13681 21493 -1634 -2530 -1028 C
ATOM 1330 CG ASP A 272 -55.376-167.832 302.798 1.00140.62 C
ANISOU 1330 CG ASP A 272 17374 14183 21874 -1757 -2610 -1356 C
ATOM 1331 OD1 ASP A 272 -54.790-168.674 302.085 1.00144.85 O
ANISOU 1331 OD1 ASP A 272 17967 14476 22592 -1721 -2737 -1692 O
ATOM 1332 OD2 ASP A 272 -56.479-167.332 302.492 1.00138.57 O
ANISOU 1332 OD2 ASP A 272 16936 14281 21433 -1889 -2546 -1290 O
ATOM 1333 N LYS A 273 -52.345-167.392 301.774 1.00136.95 N
ANISOU 1333 N LYS A 273 17055 13613 21368 -1112 -2607 -1862 N
ATOM 1334 CA LYS A 273 -51.823-166.748 300.572 1.00139.12 C
ANISOU 1334 CA LYS A 273 17216 14231 21414 -933 -2554 -2150 C
ATOM 1335 C LYS A 273 -52.871-165.869 299.903 1.00139.79 C
ANISOU 1335 C LYS A 273 17102 14807 21206 -1022 -2465 -2088 C
ATOM 1336 O LYS A 273 -52.526-164.851 299.291 1.00145.03 O
ANISOU 1336 O LYS A 273 17670 15826 21607 -862 -2367 -2112 O
ATOM 1337 CB LYS A 273 -51.309-167.797 299.586 1.00146.86 C
ANISOU 1337 CB LYS A 273 18197 15034 22568 -915 -2693 -2622 C
ATOM 1338 CG LYS A 273 -50.153-168.636 300.108 1.00154.60 C
ANISOU 1338 CG LYS A 273 19349 15531 23862 -768 -2791 -2722 C
ATOM 1339 CD LYS A 273 -49.516-169.453 298.992 1.00163.74 C
ANISOU 1339 CD LYS A 273 20463 16680 25069 -665 -2841 -3189 C
ATOM 1340 CE LYS A 273 -50.561-170.235 298.211 1.00173.56 C
ANISOU 1340 CE LYS A 273 21620 17964 26362 -911 -2909 -3414 C
ATOM 1341 NZ LYS A 273 -49.948-171.102 297.167 1.00179.22 N
ANISOU 1341 NZ LYS A 273 22293 18690 27112 -811 -2928 -3860 N
ATOM 1342 N THR A 274 -54.149-166.243 300.003 1.00135.45 N
ANISOU 1342 N THR A 274 16476 14288 20702 -1280 -2505 -1992 N
ATOM 1343 CA THR A 274 -55.205-165.404 299.443 1.00129.00 C
ANISOU 1343 CA THR A 274 15448 13946 19621 -1354 -2431 -1899 C
ATOM 1344 C THR A 274 -55.243-164.044 300.130 1.00119.37 C
ANISOU 1344 C THR A 274 14201 12939 18217 -1209 -2260 -1546 C
ATOM 1345 O THR A 274 -55.414-163.012 299.470 1.00115.20 O
ANISOU 1345 O THR A 274 13527 12798 17445 -1103 -2178 -1510 O
ATOM 1346 CB THR A 274 -56.557-166.109 299.562 1.00131.31 C
ANISOU 1346 CB THR A 274 15657 14219 20017 -1669 -2506 -1850 C
ATOM 1347 OG1 THR A 274 -56.524-167.338 298.824 1.00133.73 O
ANISOU 1347 OG1 THR A 274 15979 14326 20507 -1812 -2665 -2225 O
ATOM 1348 CG2 THR A 274 -57.671-165.228 299.017 1.00131.01 C
ANISOU 1348 CG2 THR A 274 15374 14692 19711 -1728 -2438 -1737 C
ATOM 1349 N TYR A 275 -55.075-164.021 301.454 1.00116.05 N
ANISOU 1349 N TYR A 275 13912 12269 17911 -1206 -2208 -1284 N
ATOM 1350 CA TYR A 275 -54.987-162.746 302.157 1.00113.93 C
ANISOU 1350 CA TYR A 275 13626 12174 17487 -1060 -2038 -1007 C
ATOM 1351 C TYR A 275 -53.768-161.956 301.702 1.00117.94 C
ANISOU 1351 C TYR A 275 14172 12771 17869 -790 -1972 -1106 C
ATOM 1352 O TYR A 275 -53.839-160.732 301.537 1.00121.29 O
ANISOU 1352 O TYR A 275 14502 13472 18109 -665 -1847 -982 O
ATOM 1353 CB TYR A 275 -54.941-162.971 303.668 1.00113.72 C
ANISOU 1353 CB TYR A 275 13730 11889 17588 -1127 -2002 -747 C
ATOM 1354 CG TYR A 275 -54.574-161.723 304.440 1.00114.64 C
ANISOU 1354 CG TYR A 275 13854 12140 17565 -956 -1828 -537 C
ATOM 1355 CD1 TYR A 275 -55.533-160.768 304.750 1.00118.97 C
ANISOU 1355 CD1 TYR A 275 14250 12971 17984 -979 -1693 -347 C
ATOM 1356 CD2 TYR A 275 -53.266-161.493 304.847 1.00112.37 C
ANISOU 1356 CD2 TYR A 275 13709 11700 17287 -770 -1799 -553 C
ATOM 1357 CE1 TYR A 275 -55.201-159.621 305.448 1.00116.69 C
ANISOU 1357 CE1 TYR A 275 13962 12780 17595 -825 -1530 -198 C
ATOM 1358 CE2 TYR A 275 -52.925-160.351 305.542 1.00113.20 C
ANISOU 1358 CE2 TYR A 275 13815 11926 17270 -635 -1640 -395 C
ATOM 1359 CZ TYR A 275 -53.895-159.418 305.841 1.00112.04 C
ANISOU 1359 CZ TYR A 275 13526 12031 17011 -664 -1503 -228 C
ATOM 1360 OH TYR A 275 -53.555-158.281 306.539 1.00104.41 O
ANISOU 1360 OH TYR A 275 12558 11159 15953 -532 -1340 -110 O
ATOM 1361 N LEU A 276 -52.640-162.638 301.499 1.00118.39 N
ANISOU 1361 N LEU A 276 14358 12588 18038 -700 -2057 -1327 N
ATOM 1362 CA LEU A 276 -51.431-161.955 301.051 1.00117.04 C
ANISOU 1362 CA LEU A 276 14209 12520 17741 -464 -1996 -1439 C
ATOM 1363 C LEU A 276 -51.622-161.363 299.660 1.00119.50 C
ANISOU 1363 C LEU A 276 14348 13231 17824 -424 -1978 -1588 C
ATOM 1364 O LEU A 276 -51.252-160.212 299.408 1.00117.26 O
ANISOU 1364 O LEU A 276 14012 13188 17355 -281 -1865 -1489 O
ATOM 1365 CB LEU A 276 -50.244-162.918 301.075 1.00118.32 C
ANISOU 1365 CB LEU A 276 14511 12360 18086 -376 -2102 -1676 C
ATOM 1366 CG LEU A 276 -48.881-162.319 300.724 1.00117.93 C
ANISOU 1366 CG LEU A 276 14481 12406 17920 -140 -2042 -1803 C
ATOM 1367 CD1 LEU A 276 -48.584-161.116 301.605 1.00116.68 C
ANISOU 1367 CD1 LEU A 276 14356 12333 17644 -38 -1886 -1508 C
ATOM 1368 CD2 LEU A 276 -47.783-163.364 300.854 1.00117.34 C
ANISOU 1368 CD2 LEU A 276 14526 11993 18067 -45 -2158 -2034 C
ATOM 1369 N MET A 277 -52.207-162.141 298.744 1.00126.57 N
ANISOU 1369 N MET A 277 15150 14210 18729 -565 -2094 -1819 N
ATOM 1370 CA MET A 277 -52.502-161.621 297.412 1.00129.70 C
ANISOU 1370 CA MET A 277 15357 15048 18874 -560 -2091 -1939 C
ATOM 1371 C MET A 277 -53.410-160.400 297.486 1.00125.35 C
ANISOU 1371 C MET A 277 14670 14806 18153 -554 -1985 -1606 C
ATOM 1372 O MET A 277 -53.221-159.431 296.742 1.00125.76 O
ANISOU 1372 O MET A 277 14611 15186 17984 -445 -1925 -1549 O
ATOM 1373 CB MET A 277 -53.142-162.710 296.552 1.00141.30 C
ANISOU 1373 CB MET A 277 16735 16567 20386 -754 -2236 -2241 C
ATOM 1374 CG MET A 277 -53.598-162.224 295.187 1.00154.85 C
ANISOU 1374 CG MET A 277 18226 18802 21808 -787 -2249 -2346 C
ATOM 1375 SD MET A 277 -54.588-163.441 294.298 1.00172.52 S
ANISOU 1375 SD MET A 277 20326 21143 24079 -1064 -2414 -2685 S
ATOM 1376 CE MET A 277 -53.382-164.738 294.037 1.00177.93 C
ANISOU 1376 CE MET A 277 21157 21463 24987 -1025 -2513 -3185 C
ATOM 1377 N PHE A 278 -54.402-160.428 298.380 1.00121.64 N
ANISOU 1377 N PHE A 278 14192 14235 17790 -670 -1961 -1376 N
ATOM 1378 CA PHE A 278 -55.233-159.248 298.587 1.00118.83 C
ANISOU 1378 CA PHE A 278 13701 14133 17318 -630 -1849 -1071 C
ATOM 1379 C PHE A 278 -54.423-158.105 299.183 1.00115.83 C
ANISOU 1379 C PHE A 278 13402 13706 16902 -418 -1701 -887 C
ATOM 1380 O PHE A 278 -54.564-156.951 298.763 1.00119.77 O
ANISOU 1380 O PHE A 278 13787 14459 17261 -303 -1621 -733 O
ATOM 1381 CB PHE A 278 -56.421-159.587 299.487 1.00118.69 C
ANISOU 1381 CB PHE A 278 13643 14028 17425 -806 -1845 -900 C
ATOM 1382 CG PHE A 278 -57.121-158.379 300.048 1.00112.70 C
ANISOU 1382 CG PHE A 278 12771 13443 16607 -726 -1704 -597 C
ATOM 1383 CD1 PHE A 278 -57.958-157.613 299.252 1.00110.85 C
ANISOU 1383 CD1 PHE A 278 12310 13581 16229 -694 -1694 -498 C
ATOM 1384 CD2 PHE A 278 -56.942-158.011 301.372 1.00109.92 C
ANISOU 1384 CD2 PHE A 278 12524 12893 16348 -678 -1585 -420 C
ATOM 1385 CE1 PHE A 278 -58.601-156.502 299.766 1.00110.82 C
ANISOU 1385 CE1 PHE A 278 12188 13703 16215 -593 -1567 -237 C
ATOM 1386 CE2 PHE A 278 -57.582-156.901 301.892 1.00108.88 C
ANISOU 1386 CE2 PHE A 278 12273 12913 16182 -595 -1446 -193 C
ATOM 1387 CZ PHE A 278 -58.413-156.146 301.088 1.00109.69 C
ANISOU 1387 CZ PHE A 278 12152 13342 16182 -542 -1437 -106 C
ATOM 1388 N TRP A 279 -53.568-158.406 300.162 1.00109.30 N
ANISOU 1388 N TRP A 279 12767 12554 16209 -370 -1671 -893 N
ATOM 1389 CA TRP A 279 -52.726-157.367 300.744 1.00104.67 C
ANISOU 1389 CA TRP A 279 12258 11926 15587 -190 -1534 -758 C
ATOM 1390 C TRP A 279 -51.712-156.851 299.732 1.00104.85 C
ANISOU 1390 C TRP A 279 12267 12112 15462 -46 -1524 -884 C
ATOM 1391 O TRP A 279 -51.462-155.643 299.658 1.00109.36 O
ANISOU 1391 O TRP A 279 12797 12817 15936 78 -1411 -731 O
ATOM 1392 CB TRP A 279 -52.017-157.896 301.988 1.00103.01 C
ANISOU 1392 CB TRP A 279 12237 11372 15528 -188 -1525 -745 C
ATOM 1393 CG TRP A 279 -51.091-156.897 302.596 1.00 99.26 C
ANISOU 1393 CG TRP A 279 11838 10867 15011 -24 -1391 -647 C
ATOM 1394 CD1 TRP A 279 -51.381-156.013 303.590 1.00 93.40 C
ANISOU 1394 CD1 TRP A 279 11091 10128 14271 5 -1251 -438 C
ATOM 1395 CD2 TRP A 279 -49.720-156.668 302.240 1.00105.69 C
ANISOU 1395 CD2 TRP A 279 12727 11661 15771 122 -1380 -780 C
ATOM 1396 NE1 TRP A 279 -50.277-155.249 303.881 1.00 96.55 N
ANISOU 1396 NE1 TRP A 279 11566 10491 14628 149 -1157 -436 N
ATOM 1397 CE2 TRP A 279 -49.244-155.632 303.067 1.00102.57 C
ANISOU 1397 CE2 TRP A 279 12376 11245 15352 220 -1235 -630 C
ATOM 1398 CE3 TRP A 279 -48.850-157.240 301.306 1.00115.10 C
ANISOU 1398 CE3 TRP A 279 13935 12869 16929 173 -1474 -1035 C
ATOM 1399 CZ2 TRP A 279 -47.936-155.154 302.988 1.00107.35 C
ANISOU 1399 CZ2 TRP A 279 13045 11842 15900 352 -1186 -705 C
ATOM 1400 CZ3 TRP A 279 -47.552-156.765 301.229 1.00117.34 C
ANISOU 1400 CZ3 TRP A 279 14271 13164 17148 317 -1420 -1108 C
ATOM 1401 CH2 TRP A 279 -47.107-155.733 302.065 1.00113.53 C
ANISOU 1401 CH2 TRP A 279 13836 12658 16642 398 -1280 -933 C
ATOM 1402 N ILE A 280 -51.104-157.752 298.958 1.00102.68 N
ANISOU 1402 N ILE A 280 12016 11823 15175 -66 -1638 -1171 N
ATOM 1403 CA ILE A 280 -50.193-157.322 297.901 1.00101.17 C
ANISOU 1403 CA ILE A 280 11777 11859 14805 43 -1629 -1312 C
ATOM 1404 C ILE A 280 -50.933-156.465 296.882 1.00 99.53 C
ANISOU 1404 C ILE A 280 11373 12057 14388 29 -1611 -1182 C
ATOM 1405 O ILE A 280 -50.407-155.456 296.397 1.00 94.34 O
ANISOU 1405 O ILE A 280 10668 11600 13578 134 -1536 -1079 O
ATOM 1406 CB ILE A 280 -49.526-158.542 297.238 1.00104.31 C
ANISOU 1406 CB ILE A 280 12205 12193 15237 15 -1756 -1695 C
ATOM 1407 CG1 ILE A 280 -48.518-159.187 298.190 1.00110.09 C
ANISOU 1407 CG1 ILE A 280 13123 12533 16173 91 -1771 -1787 C
ATOM 1408 CG2 ILE A 280 -48.851-158.148 295.933 1.00100.79 C
ANISOU 1408 CG2 ILE A 280 11644 12105 14546 80 -1751 -1865 C
ATOM 1409 CD1 ILE A 280 -47.885-160.445 297.635 1.00116.97 C
ANISOU 1409 CD1 ILE A 280 14023 13273 17149 89 -1903 -2177 C
ATOM 1410 N GLY A 281 -52.172-156.842 296.559 1.00105.40 N
ANISOU 1410 N GLY A 281 11992 12932 15126 -109 -1686 -1162 N
ATOM 1411 CA GLY A 281 -52.922-156.105 295.555 1.00108.04 C
ANISOU 1411 CA GLY A 281 12115 13678 15256 -122 -1696 -1026 C
ATOM 1412 C GLY A 281 -53.148-154.656 295.938 1.00103.82 C
ANISOU 1412 C GLY A 281 11538 13202 14708 7 -1565 -665 C
ATOM 1413 O GLY A 281 -52.826-153.742 295.175 1.00101.68 O
ANISOU 1413 O GLY A 281 11183 13180 14272 93 -1533 -543 O
ATOM 1414 N VAL A 282 -53.695-154.427 297.134 1.00102.57 N
ANISOU 1414 N VAL A 282 11432 12812 14728 18 -1488 -492 N
ATOM 1415 CA VAL A 282 -53.985-153.061 297.566 1.00104.34 C
ANISOU 1415 CA VAL A 282 11605 13056 14983 148 -1358 -190 C
ATOM 1416 C VAL A 282 -52.694-152.264 297.722 1.00103.15 C
ANISOU 1416 C VAL A 282 11577 12798 14816 290 -1255 -158 C
ATOM 1417 O VAL A 282 -52.642-151.071 297.399 1.00106.60 O
ANISOU 1417 O VAL A 282 11945 13350 15210 398 -1183 52 O
ATOM 1418 CB VAL A 282 -54.817-153.075 298.864 1.00104.39 C
ANISOU 1418 CB VAL A 282 11627 12864 15173 115 -1286 -73 C
ATOM 1419 CG1 VAL A 282 -54.143-153.919 299.935 1.00106.60 C
ANISOU 1419 CG1 VAL A 282 12115 12812 15578 60 -1274 -217 C
ATOM 1420 CG2 VAL A 282 -55.058-151.658 299.365 1.00103.82 C
ANISOU 1420 CG2 VAL A 282 11500 12781 15168 268 -1139 181 C
ATOM 1421 N VAL A 283 -51.629-152.912 298.196 1.00101.14 N
ANISOU 1421 N VAL A 283 11499 12322 14609 288 -1254 -358 N
ATOM 1422 CA VAL A 283 -50.344-152.232 298.327 1.00100.05 C
ANISOU 1422 CA VAL A 283 11464 12109 14442 403 -1163 -357 C
ATOM 1423 C VAL A 283 -49.744-151.949 296.954 1.00106.23 C
ANISOU 1423 C VAL A 283 12160 13191 15010 423 -1204 -408 C
ATOM 1424 O VAL A 283 -49.157-150.885 296.726 1.00109.58 O
ANISOU 1424 O VAL A 283 12577 13688 15372 505 -1118 -261 O
ATOM 1425 CB VAL A 283 -49.391-153.061 299.209 1.00 98.93 C
ANISOU 1425 CB VAL A 283 11507 11677 14404 401 -1168 -552 C
ATOM 1426 CG1 VAL A 283 -47.971-152.524 299.120 1.00 97.26 C
ANISOU 1426 CG1 VAL A 283 11372 11455 14127 502 -1100 -607 C
ATOM 1427 CG2 VAL A 283 -49.870-153.054 300.652 1.00 98.92 C
ANISOU 1427 CG2 VAL A 283 11584 11428 14573 380 -1099 -435 C
ATOM 1428 N SER A 284 -49.891-152.886 296.015 1.00111.08 N
ANISOU 1428 N SER A 284 12699 14002 15504 332 -1333 -621 N
ATOM 1429 CA SER A 284 -49.326-152.682 294.685 1.00112.78 C
ANISOU 1429 CA SER A 284 12808 14571 15472 328 -1371 -695 C
ATOM 1430 C SER A 284 -50.078-151.599 293.922 1.00112.57 C
ANISOU 1430 C SER A 284 12605 14859 15308 338 -1362 -379 C
ATOM 1431 O SER A 284 -49.468-150.826 293.174 1.00115.98 O
ANISOU 1431 O SER A 284 12979 15519 15568 371 -1330 -266 O
ATOM 1432 CB SER A 284 -49.337-153.992 293.898 1.00116.22 C
ANISOU 1432 CB SER A 284 13192 15152 15817 220 -1508 -1052 C
ATOM 1433 OG SER A 284 -48.814-153.809 292.595 1.00117.57 O
ANISOU 1433 OG SER A 284 13234 15730 15709 201 -1538 -1150 O
ATOM 1434 N VAL A 285 -51.400-151.525 294.098 1.00109.97 N
ANISOU 1434 N VAL A 285 12176 14552 15055 307 -1395 -214 N
ATOM 1435 CA VAL A 285 -52.198-150.548 293.357 1.00109.81 C
ANISOU 1435 CA VAL A 285 11964 14833 14926 333 -1411 105 C
ATOM 1436 C VAL A 285 -51.755-149.129 293.694 1.00111.93 C
ANISOU 1436 C VAL A 285 12275 14977 15277 472 -1282 410 C
ATOM 1437 O VAL A 285 -51.451-148.326 292.804 1.00114.26 O
ANISOU 1437 O VAL A 285 12479 15522 15414 496 -1286 605 O
ATOM 1438 CB VAL A 285 -53.699-150.753 293.634 1.00102.05 C
ANISOU 1438 CB VAL A 285 10857 13873 14046 290 -1464 210 C
ATOM 1439 CG1 VAL A 285 -54.488-149.532 293.192 1.00 99.03 C
ANISOU 1439 CG1 VAL A 285 10289 13698 13639 380 -1456 600 C
ATOM 1440 CG2 VAL A 285 -54.205-151.993 292.910 1.00103.58 C
ANISOU 1440 CG2 VAL A 285 10952 14301 14103 120 -1613 -57 C
ATOM 1441 N LEU A 286 -51.709-148.799 294.987 1.00107.00 N
ANISOU 1441 N LEU A 286 11784 13971 14900 551 -1166 454 N
ATOM 1442 CA LEU A 286 -51.295-147.457 295.377 1.00107.63 C
ANISOU 1442 CA LEU A 286 11908 13891 15096 673 -1035 699 C
ATOM 1443 C LEU A 286 -49.835-147.201 295.024 1.00108.97 C
ANISOU 1443 C LEU A 286 12177 14082 15146 672 -990 626 C
ATOM 1444 O LEU A 286 -49.473-146.079 294.652 1.00112.78 O
ANISOU 1444 O LEU A 286 12630 14608 15613 724 -933 868 O
ATOM 1445 CB LEU A 286 -51.555-147.239 296.867 1.00104.79 C
ANISOU 1445 CB LEU A 286 11655 13157 15004 736 -916 699 C
ATOM 1446 CG LEU A 286 -51.055-148.238 297.908 1.00 97.11 C
ANISOU 1446 CG LEU A 286 10855 11939 14103 680 -894 421 C
ATOM 1447 CD1 LEU A 286 -49.597-147.989 298.264 1.00 94.81 C
ANISOU 1447 CD1 LEU A 286 10724 11492 13806 714 -813 318 C
ATOM 1448 CD2 LEU A 286 -51.926-148.162 299.153 1.00 89.55 C
ANISOU 1448 CD2 LEU A 286 9904 10771 13348 698 -818 469 C
ATOM 1449 N LEU A 287 -48.990-148.227 295.108 1.00105.80 N
ANISOU 1449 N LEU A 287 11881 13652 14668 613 -1020 301 N
ATOM 1450 CA LEU A 287 -47.599-148.060 294.703 1.00105.49 C
ANISOU 1450 CA LEU A 287 11900 13688 14492 609 -982 201 C
ATOM 1451 C LEU A 287 -47.492-147.789 293.209 1.00110.20 C
ANISOU 1451 C LEU A 287 12335 14732 14806 550 -1052 296 C
ATOM 1452 O LEU A 287 -46.730-146.913 292.781 1.00112.54 O
ANISOU 1452 O LEU A 287 12618 15133 15008 555 -990 453 O
ATOM 1453 CB LEU A 287 -46.783-149.296 295.076 1.00105.40 C
ANISOU 1453 CB LEU A 287 12006 13562 14480 581 -1016 -182 C
ATOM 1454 CG LEU A 287 -46.264-149.347 296.512 1.00103.85 C
ANISOU 1454 CG LEU A 287 11988 12971 14500 638 -927 -252 C
ATOM 1455 CD1 LEU A 287 -45.675-150.714 296.824 1.00106.39 C
ANISOU 1455 CD1 LEU A 287 12402 13177 14846 617 -1002 -594 C
ATOM 1456 CD2 LEU A 287 -45.230-148.256 296.728 1.00100.40 C
ANISOU 1456 CD2 LEU A 287 11607 12477 14064 688 -801 -139 C
ATOM 1457 N LEU A 288 -48.247-148.533 292.398 1.00111.50 N
ANISOU 1457 N LEU A 288 12363 15184 14817 472 -1180 204 N
ATOM 1458 CA LEU A 288 -48.254-148.273 290.963 1.00114.90 C
ANISOU 1458 CA LEU A 288 12611 16108 14939 398 -1255 309 C
ATOM 1459 C LEU A 288 -48.826-146.895 290.662 1.00118.41 C
ANISOU 1459 C LEU A 288 12953 16635 15404 449 -1231 796 C
ATOM 1460 O LEU A 288 -48.346-146.199 289.760 1.00120.19 O
ANISOU 1460 O LEU A 288 13090 17155 15423 411 -1233 998 O
ATOM 1461 CB LEU A 288 -49.042-149.359 290.230 1.00117.49 C
ANISOU 1461 CB LEU A 288 12802 16731 15108 292 -1400 89 C
ATOM 1462 CG LEU A 288 -48.381-150.737 290.168 1.00117.41 C
ANISOU 1462 CG LEU A 288 12856 16709 15047 230 -1446 -415 C
ATOM 1463 CD1 LEU A 288 -49.230-151.701 289.355 1.00122.65 C
ANISOU 1463 CD1 LEU A 288 13364 17679 15559 104 -1590 -629 C
ATOM 1464 CD2 LEU A 288 -46.973-150.638 289.599 1.00115.14 C
ANISOU 1464 CD2 LEU A 288 12574 16615 14558 223 -1397 -572 C
ATOM 1465 N PHE A 289 -49.849-146.478 291.412 1.00120.58 N
ANISOU 1465 N PHE A 289 13228 16654 15934 536 -1211 997 N
ATOM 1466 CA PHE A 289 -50.378-145.130 291.238 1.00125.19 C
ANISOU 1466 CA PHE A 289 13720 17235 16613 622 -1186 1455 C
ATOM 1467 C PHE A 289 -49.342-144.084 291.627 1.00124.96 C
ANISOU 1467 C PHE A 289 13818 16957 16702 677 -1050 1606 C
ATOM 1468 O PHE A 289 -49.193-143.064 290.943 1.00128.28 O
ANISOU 1468 O PHE A 289 14160 17516 17066 682 -1050 1952 O
ATOM 1469 CB PHE A 289 -51.655-144.946 292.055 1.00125.19 C
ANISOU 1469 CB PHE A 289 13682 16996 16890 721 -1177 1577 C
ATOM 1470 CG PHE A 289 -52.251-143.573 291.934 1.00129.14 C
ANISOU 1470 CG PHE A 289 14075 17443 17549 846 -1155 2028 C
ATOM 1471 CD1 PHE A 289 -53.136-143.276 290.910 1.00132.74 C
ANISOU 1471 CD1 PHE A 289 14300 18264 17869 847 -1286 2321 C
ATOM 1472 CD2 PHE A 289 -51.918-142.575 292.835 1.00128.69 C
ANISOU 1472 CD2 PHE A 289 14137 16970 17789 964 -1010 2156 C
ATOM 1473 CE1 PHE A 289 -53.682-142.012 290.792 1.00134.20 C
ANISOU 1473 CE1 PHE A 289 14380 18371 18239 984 -1281 2761 C
ATOM 1474 CE2 PHE A 289 -52.456-141.311 292.719 1.00131.65 C
ANISOU 1474 CE2 PHE A 289 14413 17246 18361 1093 -994 2556 C
ATOM 1475 CZ PHE A 289 -53.342-141.028 291.698 1.00134.19 C
ANISOU 1475 CZ PHE A 289 14509 17904 18573 1114 -1134 2874 C
ATOM 1476 N ILE A 290 -48.629-144.313 292.731 1.00116.96 N
ANISOU 1476 N ILE A 290 12997 15582 15859 706 -939 1364 N
ATOM 1477 CA ILE A 290 -47.533-143.425 293.113 1.00109.11 C
ANISOU 1477 CA ILE A 290 12124 14376 14957 728 -811 1443 C
ATOM 1478 C ILE A 290 -46.507-143.346 291.991 1.00110.18 C
ANISOU 1478 C ILE A 290 12208 14871 14785 619 -836 1458 C
ATOM 1479 O ILE A 290 -46.078-142.258 291.590 1.00110.89 O
ANISOU 1479 O ILE A 290 12274 14990 14867 603 -789 1758 O
ATOM 1480 CB ILE A 290 -46.891-143.899 294.429 1.00100.74 C
ANISOU 1480 CB ILE A 290 11257 12955 14065 755 -711 1131 C
ATOM 1481 CG1 ILE A 290 -47.827-143.637 295.610 1.00 94.53 C
ANISOU 1481 CG1 ILE A 290 10511 11823 13584 853 -648 1180 C
ATOM 1482 CG2 ILE A 290 -45.550-143.215 294.645 1.00 97.99 C
ANISOU 1482 CG2 ILE A 290 11014 12490 13727 735 -597 1130 C
ATOM 1483 CD1 ILE A 290 -47.326-144.215 296.911 1.00 87.07 C
ANISOU 1483 CD1 ILE A 290 9733 10587 12764 858 -571 890 C
ATOM 1484 N VAL A 291 -46.104-144.504 291.463 1.00114.14 N
ANISOU 1484 N VAL A 291 12681 15653 15034 534 -910 1127 N
ATOM 1485 CA VAL A 291 -45.140-144.523 290.369 1.00117.82 C
ANISOU 1485 CA VAL A 291 13067 16528 15173 423 -928 1086 C
ATOM 1486 C VAL A 291 -45.734-143.885 289.120 1.00123.20 C
ANISOU 1486 C VAL A 291 13549 17627 15636 359 -1015 1462 C
ATOM 1487 O VAL A 291 -45.064-143.111 288.427 1.00127.32 O
ANISOU 1487 O VAL A 291 14014 18370 15993 283 -987 1696 O
ATOM 1488 CB VAL A 291 -44.662-145.963 290.102 1.00115.23 C
ANISOU 1488 CB VAL A 291 12732 16395 14656 367 -989 596 C
ATOM 1489 CG1 VAL A 291 -43.794-146.012 288.855 1.00118.57 C
ANISOU 1489 CG1 VAL A 291 13022 17329 14701 247 -1010 526 C
ATOM 1490 CG2 VAL A 291 -43.898-146.496 291.305 1.00106.35 C
ANISOU 1490 CG2 VAL A 291 11798 14867 13743 435 -911 285 C
ATOM 1491 N TYR A 292 -46.999-144.186 288.818 1.00123.95 N
ANISOU 1491 N TYR A 292 13522 17854 15719 377 -1128 1548 N
ATOM 1492 CA TYR A 292 -47.641-143.590 287.650 1.00127.28 C
ANISOU 1492 CA TYR A 292 13733 18699 15927 323 -1232 1936 C
ATOM 1493 C TYR A 292 -47.736-142.076 287.786 1.00129.61 C
ANISOU 1493 C TYR A 292 14038 18776 16433 398 -1175 2459 C
ATOM 1494 O TYR A 292 -47.415-141.336 286.849 1.00133.52 O
ANISOU 1494 O TYR A 292 14425 19577 16729 316 -1205 2798 O
ATOM 1495 CB TYR A 292 -49.031-144.192 287.442 1.00126.83 C
ANISOU 1495 CB TYR A 292 13539 18796 15855 338 -1363 1920 C
ATOM 1496 CG TYR A 292 -49.970-143.291 286.669 1.00128.43 C
ANISOU 1496 CG TYR A 292 13540 19259 15998 358 -1462 2434 C
ATOM 1497 CD1 TYR A 292 -49.856-143.154 285.291 1.00130.42 C
ANISOU 1497 CD1 TYR A 292 13597 20111 15847 224 -1565 2621 C
ATOM 1498 CD2 TYR A 292 -50.969-142.575 287.317 1.00127.07 C
ANISOU 1498 CD2 TYR A 292 13357 18756 16169 515 -1455 2736 C
ATOM 1499 CE1 TYR A 292 -50.709-142.330 284.581 1.00132.46 C
ANISOU 1499 CE1 TYR A 292 13659 20622 16047 246 -1674 3134 C
ATOM 1500 CE2 TYR A 292 -51.827-141.749 286.616 1.00129.13 C
ANISOU 1500 CE2 TYR A 292 13419 19239 16406 560 -1559 3223 C
ATOM 1501 CZ TYR A 292 -51.693-141.631 285.248 1.00131.95 C
ANISOU 1501 CZ TYR A 292 13590 20183 16362 425 -1676 3441 C
ATOM 1502 OH TYR A 292 -52.546-140.810 284.546 1.00134.74 O
ANISOU 1502 OH TYR A 292 13735 20773 16688 473 -1798 3968 O
ATOM 1503 N ALA A 293 -48.181-141.597 288.951 1.00124.37 N
ANISOU 1503 N ALA A 293 13493 17582 16178 547 -1094 2528 N
ATOM 1504 CA ALA A 293 -48.383-140.164 289.139 1.00120.57 C
ANISOU 1504 CA ALA A 293 13015 16827 15967 641 -1043 2992 C
ATOM 1505 C ALA A 293 -47.079-139.396 288.968 1.00120.27 C
ANISOU 1505 C ALA A 293 13065 16742 15889 554 -945 3115 C
ATOM 1506 O ALA A 293 -47.011-138.433 288.196 1.00123.58 O
ANISOU 1506 O ALA A 293 13394 17306 16256 510 -979 3559 O
ATOM 1507 CB ALA A 293 -48.992-139.896 290.516 1.00114.44 C
ANISOU 1507 CB ALA A 293 12351 15499 15632 809 -950 2930 C
ATOM 1508 N TYR A 294 -46.027-139.818 289.672 1.00115.68 N
ANISOU 1508 N TYR A 294 12652 15973 15330 517 -832 2743 N
ATOM 1509 CA TYR A 294 -44.757-139.102 289.595 1.00116.44 C
ANISOU 1509 CA TYR A 294 12825 16021 15397 422 -729 2829 C
ATOM 1510 C TYR A 294 -44.139-139.212 288.205 1.00121.32 C
ANISOU 1510 C TYR A 294 13298 17231 15569 242 -798 2933 C
ATOM 1511 O TYR A 294 -43.542-138.249 287.710 1.00118.60 O
ANISOU 1511 O TYR A 294 12928 16958 15177 144 -762 3271 O
ATOM 1512 CB TYR A 294 -43.798-139.616 290.668 1.00110.93 C
ANISOU 1512 CB TYR A 294 12310 15038 14800 428 -606 2387 C
ATOM 1513 CG TYR A 294 -44.212-139.238 292.075 1.00112.39 C
ANISOU 1513 CG TYR A 294 12637 14656 15410 570 -509 2334 C
ATOM 1514 CD1 TYR A 294 -45.163-138.249 292.296 1.00113.00 C
ANISOU 1514 CD1 TYR A 294 12683 14465 15789 682 -503 2682 C
ATOM 1515 CD2 TYR A 294 -43.652-139.867 293.181 1.00116.34 C
ANISOU 1515 CD2 TYR A 294 13287 14911 16007 597 -427 1934 C
ATOM 1516 CE1 TYR A 294 -45.547-137.897 293.577 1.00114.50 C
ANISOU 1516 CE1 TYR A 294 12979 14175 16352 809 -402 2591 C
ATOM 1517 CE2 TYR A 294 -44.030-139.521 294.469 1.00115.88 C
ANISOU 1517 CE2 TYR A 294 13339 14395 16294 706 -333 1875 C
ATOM 1518 CZ TYR A 294 -44.978-138.535 294.660 1.00114.78 C
ANISOU 1518 CZ TYR A 294 13159 14016 16437 808 -314 2184 C
ATOM 1519 OH TYR A 294 -45.361-138.185 295.936 1.00110.17 O
ANISOU 1519 OH TYR A 294 12662 13013 16183 914 -209 2084 O
ATOM 1520 N MET A 295 -44.273-140.373 287.557 1.00127.23 N
ANISOU 1520 N MET A 295 13939 18419 15984 182 -893 2641 N
ATOM 1521 CA MET A 295 -43.861-140.476 286.161 1.00131.74 C
ANISOU 1521 CA MET A 295 14328 19631 16095 8 -966 2738 C
ATOM 1522 C MET A 295 -44.713-139.585 285.269 1.00130.70 C
ANISOU 1522 C MET A 295 14028 19739 15892 -17 -1075 3322 C
ATOM 1523 O MET A 295 -44.213-139.032 284.282 1.00131.32 O
ANISOU 1523 O MET A 295 13989 20219 15687 -172 -1098 3625 O
ATOM 1524 CB MET A 295 -43.937-141.928 285.686 1.00137.07 C
ANISOU 1524 CB MET A 295 14913 20706 16463 -41 -1048 2256 C
ATOM 1525 CG MET A 295 -42.827-142.825 286.215 1.00137.93 C
ANISOU 1525 CG MET A 295 15138 20720 16549 -47 -961 1706 C
ATOM 1526 SD MET A 295 -41.207-142.425 285.533 1.00141.01 S
ANISOU 1526 SD MET A 295 15475 21479 16626 -219 -865 1691 S
ATOM 1527 CE MET A 295 -41.474-142.773 283.797 1.00145.71 C
ANISOU 1527 CE MET A 295 15776 22930 16657 -398 -994 1751 C
ATOM 1528 N TYR A 296 -45.998-139.434 285.598 1.00131.55 N
ANISOU 1528 N TYR A 296 14107 19629 16248 131 -1148 3502 N
ATOM 1529 CA TYR A 296 -46.857-138.529 284.844 1.00138.56 C
ANISOU 1529 CA TYR A 296 14828 20691 17129 146 -1264 4092 C
ATOM 1530 C TYR A 296 -46.477-137.073 285.076 1.00135.95 C
ANISOU 1530 C TYR A 296 14577 19983 17095 172 -1186 4570 C
ATOM 1531 O TYR A 296 -46.687-136.230 284.196 1.00135.74 O
ANISOU 1531 O TYR A 296 14413 20189 16973 113 -1274 5112 O
ATOM 1532 CB TYR A 296 -48.320-138.771 285.217 1.00143.00 C
ANISOU 1532 CB TYR A 296 15323 21102 17908 316 -1355 4122 C
ATOM 1533 CG TYR A 296 -49.268-137.686 284.762 1.00150.51 C
ANISOU 1533 CG TYR A 296 16125 22058 19006 407 -1460 4749 C
ATOM 1534 CD1 TYR A 296 -49.649-137.583 283.431 1.00157.82 C
ANISOU 1534 CD1 TYR A 296 16809 23602 19555 296 -1624 5101 C
ATOM 1535 CD2 TYR A 296 -49.788-136.771 285.667 1.00152.06 C
ANISOU 1535 CD2 TYR A 296 16405 21652 19720 609 -1399 4982 C
ATOM 1536 CE1 TYR A 296 -50.519-136.593 283.013 1.00164.43 C
ANISOU 1536 CE1 TYR A 296 17496 24440 20539 395 -1739 5712 C
ATOM 1537 CE2 TYR A 296 -50.658-135.779 285.259 1.00158.90 C
ANISOU 1537 CE2 TYR A 296 17122 22486 20765 722 -1504 5554 C
ATOM 1538 CZ TYR A 296 -51.020-135.694 283.931 1.00164.90 C
ANISOU 1538 CZ TYR A 296 17646 23851 21157 620 -1681 5938 C
ATOM 1539 OH TYR A 296 -51.887-134.707 283.521 1.00169.21 O
ANISOU 1539 OH TYR A 296 18033 24366 21895 747 -1803 6545 O
ATOM 1540 N ILE A 297 -45.917-136.759 286.245 1.00131.34 N
ANISOU 1540 N ILE A 297 14209 18821 16874 248 -1029 4386 N
ATOM 1541 CA ILE A 297 -45.474-135.395 286.517 1.00130.06 C
ANISOU 1541 CA ILE A 297 14136 18260 17023 252 -943 4778 C
ATOM 1542 C ILE A 297 -44.247-135.059 285.680 1.00135.35 C
ANISOU 1542 C ILE A 297 14775 19282 17368 11 -912 4931 C
ATOM 1543 O ILE A 297 -44.168-133.990 285.064 1.00143.39 O
ANISOU 1543 O ILE A 297 15731 20332 18418 -67 -946 5477 O
ATOM 1544 CB ILE A 297 -45.195-135.211 288.019 1.00123.32 C
ANISOU 1544 CB ILE A 297 13505 16739 16613 377 -779 4476 C
ATOM 1545 CG1 ILE A 297 -46.478-135.393 288.832 1.00117.73 C
ANISOU 1545 CG1 ILE A 297 12799 15704 16230 605 -802 4388 C
ATOM 1546 CG2 ILE A 297 -44.583-133.845 288.284 1.00124.20 C
ANISOU 1546 CG2 ILE A 297 13713 16442 17034 344 -678 4809 C
ATOM 1547 CD1 ILE A 297 -46.257-135.373 290.328 1.00111.60 C
ANISOU 1547 CD1 ILE A 297 12219 14364 15821 712 -644 4034 C
ATOM 1548 N LEU A 298 -43.272-135.971 285.644 1.00134.39 N
ANISOU 1548 N LEU A 298 14687 19435 16938 -111 -850 4459 N
ATOM 1549 CA LEU A 298 -42.028-135.699 284.931 1.00138.86 C
ANISOU 1549 CA LEU A 298 15214 20359 17190 -346 -798 4541 C
ATOM 1550 C LEU A 298 -42.258-135.594 283.429 1.00147.26 C
ANISOU 1550 C LEU A 298 16037 22113 17801 -508 -936 4925 C
ATOM 1551 O LEU A 298 -41.656-134.744 282.763 1.00152.58 O
ANISOU 1551 O LEU A 298 16652 22979 18343 -689 -925 5343 O
ATOM 1552 CB LEU A 298 -41.001-136.785 285.244 1.00136.30 C
ANISOU 1552 CB LEU A 298 14949 20191 16649 -404 -709 3906 C
ATOM 1553 CG LEU A 298 -40.716-136.990 286.732 1.00135.65 C
ANISOU 1553 CG LEU A 298 15089 19494 16959 -258 -584 3517 C
ATOM 1554 CD1 LEU A 298 -39.723-138.120 286.939 1.00137.47 C
ANISOU 1554 CD1 LEU A 298 15348 19922 16962 -302 -527 2928 C
ATOM 1555 CD2 LEU A 298 -40.213-135.701 287.366 1.00135.20 C
ANISOU 1555 CD2 LEU A 298 15164 18945 17261 -281 -464 3799 C
ATOM 1556 N TRP A 299 -43.121-136.450 282.875 1.00151.68 N
ANISOU 1556 N TRP A 299 16448 23076 18108 -468 -1071 4797 N
ATOM 1557 CA TRP A 299 -43.423-136.360 281.451 1.00161.17 C
ANISOU 1557 CA TRP A 299 17398 24985 18853 -628 -1214 5162 C
ATOM 1558 C TRP A 299 -44.210-135.098 281.125 1.00168.83 C
ANISOU 1558 C TRP A 299 18302 25802 20043 -581 -1314 5918 C
ATOM 1559 O TRP A 299 -44.030-134.518 280.048 1.00174.74 O
ANISOU 1559 O TRP A 299 18890 27017 20487 -764 -1392 6404 O
ATOM 1560 CB TRP A 299 -44.193-137.599 280.994 1.00163.20 C
ANISOU 1560 CB TRP A 299 17508 25695 18807 -601 -1336 4799 C
ATOM 1561 CG TRP A 299 -44.479-137.611 279.523 1.00170.29 C
ANISOU 1561 CG TRP A 299 18125 27402 19175 -785 -1484 5103 C
ATOM 1562 CD1 TRP A 299 -43.665-138.082 278.534 1.00173.26 C
ANISOU 1562 CD1 TRP A 299 18346 28490 18994 -1022 -1479 4921 C
ATOM 1563 CD2 TRP A 299 -45.661-137.127 278.873 1.00176.34 C
ANISOU 1563 CD2 TRP A 299 18711 28390 19900 -749 -1662 5640 C
ATOM 1564 NE1 TRP A 299 -44.267-137.922 277.309 1.00179.81 N
ANISOU 1564 NE1 TRP A 299 18912 29994 19412 -1155 -1641 5311 N
ATOM 1565 CE2 TRP A 299 -45.493-137.338 277.490 1.00181.20 C
ANISOU 1565 CE2 TRP A 299 19070 29882 19898 -988 -1764 5773 C
ATOM 1566 CE3 TRP A 299 -46.845-136.537 279.327 1.00177.38 C
ANISOU 1566 CE3 TRP A 299 18855 28089 20452 -533 -1747 6013 C
ATOM 1567 CZ2 TRP A 299 -46.464-136.980 276.556 1.00185.45 C
ANISOU 1567 CZ2 TRP A 299 19368 30881 20215 -1025 -1958 6291 C
ATOM 1568 CZ3 TRP A 299 -47.808-136.181 278.398 1.00182.18 C
ANISOU 1568 CZ3 TRP A 299 19222 29130 20869 -549 -1940 6524 C
ATOM 1569 CH2 TRP A 299 -47.611-136.404 277.029 1.00186.19 C
ANISOU 1569 CH2 TRP A 299 19481 30517 20747 -798 -2050 6673 C
ATOM 1570 N LYS A 300 -45.080-134.658 282.038 1.00169.71 N
ANISOU 1570 N LYS A 300 18522 25276 20685 -337 -1315 6034 N
ATOM 1571 CA LYS A 300 -45.823-133.422 281.813 1.00171.77 C
ANISOU 1571 CA LYS A 300 18721 25306 21239 -251 -1408 6737 C
ATOM 1572 C LYS A 300 -44.911-132.207 281.916 1.00170.85 C
ANISOU 1572 C LYS A 300 18719 24849 21347 -359 -1308 7122 C
ATOM 1573 O LYS A 300 -45.021-131.270 281.116 1.00177.48 O
ANISOU 1573 O LYS A 300 19446 25834 22153 -450 -1405 7780 O
ATOM 1574 CB LYS A 300 -46.976-133.316 282.811 1.00169.88 C
ANISOU 1574 CB LYS A 300 18549 24478 21520 52 -1419 6685 C
ATOM 1575 CG LYS A 300 -47.888-132.117 282.595 1.00173.66 C
ANISOU 1575 CG LYS A 300 18934 24704 22346 197 -1532 7375 C
ATOM 1576 CD LYS A 300 -48.647-132.225 281.282 1.00175.62 C
ANISOU 1576 CD LYS A 300 18895 25644 22187 131 -1754 7795 C
ATOM 1577 CE LYS A 300 -49.600-131.054 281.099 1.00177.58 C
ANISOU 1577 CE LYS A 300 19048 25597 22827 295 -1855 8412 C
ATOM 1578 NZ LYS A 300 -50.381-131.163 279.836 1.00181.37 N
ANISOU 1578 NZ LYS A 300 19261 26721 22930 202 -2016 8656 N
ATOM 1579 N ALA A 301 -44.000-132.205 282.893 1.00165.65 N
ANISOU 1579 N ALA A 301 18278 23743 20919 -365 -1122 6736 N
ATOM 1580 CA ALA A 301 -43.069-131.094 283.043 1.00168.81 C
ANISOU 1580 CA ALA A 301 18790 23812 21536 -497 -1015 7041 C
ATOM 1581 C ALA A 301 -41.992-131.090 281.968 1.00171.46 C
ANISOU 1581 C ALA A 301 19015 24788 21343 -825 -1010 7191 C
ATOM 1582 O ALA A 301 -41.384-130.043 281.723 1.00175.35 O
ANISOU 1582 O ALA A 301 19535 25148 21941 -988 -973 7642 O
ATOM 1583 CB ALA A 301 -42.422-131.133 284.428 1.00167.37 C
ANISOU 1583 CB ALA A 301 18853 23013 21729 -419 -821 6548 C
ATOM 1584 N HIS A 302 -41.741-132.232 281.323 1.00169.62 N
ANISOU 1584 N HIS A 302 18649 25247 20552 -936 -1043 6814 N
ATOM 1585 CA HIS A 302 -40.734-132.280 280.269 1.00171.35 C
ANISOU 1585 CA HIS A 302 18727 26154 20225 -1251 -1030 6912 C
ATOM 1586 C HIS A 302 -41.183-131.522 279.027 1.00175.90 C
ANISOU 1586 C HIS A 302 19095 27181 20557 -1400 -1191 7673 C
ATOM 1587 O HIS A 302 -40.353-130.919 278.337 1.00179.55 O
ANISOU 1587 O HIS A 302 19488 27960 20773 -1673 -1164 8031 O
ATOM 1588 CB HIS A 302 -40.411-133.733 279.918 1.00168.86 C
ANISOU 1588 CB HIS A 302 18306 26450 19404 -1304 -1024 6256 C
ATOM 1589 CG HIS A 302 -39.383-133.881 278.841 1.00175.12 C
ANISOU 1589 CG HIS A 302 18921 28011 19604 -1618 -997 6266 C
ATOM 1590 ND1 HIS A 302 -39.708-133.930 277.502 1.00181.24 N
ANISOU 1590 ND1 HIS A 302 19434 29570 19859 -1793 -1135 6597 N
ATOM 1591 CD2 HIS A 302 -38.034-133.991 278.904 1.00174.97 C
ANISOU 1591 CD2 HIS A 302 18930 28142 19411 -1794 -845 5977 C
ATOM 1592 CE1 HIS A 302 -38.605-134.063 276.787 1.00184.00 C
ANISOU 1592 CE1 HIS A 302 19655 30524 19731 -2070 -1060 6501 C
ATOM 1593 NE2 HIS A 302 -37.575-134.102 277.614 1.00180.32 N
ANISOU 1593 NE2 HIS A 302 19358 29683 19472 -2070 -884 6125 N
ATOM 1594 N SER A 303 -42.483-131.534 278.728 1.00176.09 N
ANISOU 1594 N SER A 303 19007 27264 20637 -1235 -1364 7948 N
ATOM 1595 CA SER A 303 -42.971-130.835 277.544 1.00184.26 C
ANISOU 1595 CA SER A 303 19824 28754 21431 -1362 -1542 8706 C
ATOM 1596 C SER A 303 -42.978-129.325 277.743 1.00188.22 C
ANISOU 1596 C SER A 303 20422 28602 22491 -1341 -1522 9262 C
ATOM 1597 O SER A 303 -42.871-128.573 276.768 1.00192.61 O
ANISOU 1597 O SER A 303 20831 29419 22934 -1523 -1583 9668 O
ATOM 1598 CB SER A 303 -44.371-131.330 277.183 1.00188.12 C
ANISOU 1598 CB SER A 303 20143 29499 21835 -1181 -1731 8756 C
ATOM 1599 OG SER A 303 -44.385-132.737 277.012 1.00187.64 O
ANISOU 1599 OG SER A 303 19999 29954 21342 -1205 -1729 8086 O
ATOM 1600 N HIS A 304 -43.100-128.863 278.989 1.00188.42 N
ANISOU 1600 N HIS A 304 20682 27759 23149 -1120 -1429 9199 N
ATOM 1601 CA HIS A 304 -43.129-127.431 279.264 1.00191.05 C
ANISOU 1601 CA HIS A 304 21117 27395 24079 -1076 -1393 9558 C
ATOM 1602 C HIS A 304 -41.740-126.823 279.390 1.00190.71 C
ANISOU 1602 C HIS A 304 21201 27195 24064 -1334 -1245 9604 C
ATOM 1603 O HIS A 304 -41.602-125.601 279.256 1.00195.89 O
ANISOU 1603 O HIS A 304 21894 27466 25071 -1387 -1245 9953 O
ATOM 1604 CB HIS A 304 -43.917-127.150 280.546 1.00187.93 C
ANISOU 1604 CB HIS A 304 20896 26142 24368 -726 -1346 9391 C
ATOM 1605 CG HIS A 304 -45.390-127.386 280.420 1.00188.61 C
ANISOU 1605 CG HIS A 304 20843 26264 24554 -468 -1489 9427 C
ATOM 1606 ND1 HIS A 304 -46.318-126.705 281.177 1.00189.21 N
ANISOU 1606 ND1 HIS A 304 20989 25644 25258 -178 -1480 9442 N
ATOM 1607 CD2 HIS A 304 -46.095-128.230 279.629 1.00189.36 C
ANISOU 1607 CD2 HIS A 304 20723 27032 24193 -469 -1635 9413 C
ATOM 1608 CE1 HIS A 304 -47.532-127.116 280.857 1.00190.49 C
ANISOU 1608 CE1 HIS A 304 20983 26051 25345 -13 -1612 9463 C
ATOM 1609 NE2 HIS A 304 -47.425-128.042 279.920 1.00190.67 N
ANISOU 1609 NE2 HIS A 304 20834 26891 24721 -188 -1711 9450 N
ATOM 1610 N ALA A 305 -40.715-127.639 279.648 1.00184.12 N
ANISOU 1610 N ALA A 305 20428 26658 22869 -1498 -1117 9249 N
ATOM 1611 CA ALA A 305 -39.372-127.105 279.855 1.00181.46 C
ANISOU 1611 CA ALA A 305 20206 26174 22567 -1752 -954 9238 C
ATOM 1612 C ALA A 305 -38.852-126.413 278.602 1.00185.91 C
ANISOU 1612 C ALA A 305 20599 27214 22824 -2051 -1019 9636 C
ATOM 1613 O ALA A 305 -38.395-125.265 278.656 1.00190.48 O
ANISOU 1613 O ALA A 305 21261 27368 23744 -2155 -981 9909 O
ATOM 1614 CB ALA A 305 -38.424-128.224 280.287 1.00176.93 C
ANISOU 1614 CB ALA A 305 19679 25877 21668 -1824 -799 8476 C
ATOM 1615 N VAL A 306 -38.913-127.095 277.462 1.00182.55 N
ANISOU 1615 N VAL A 306 19927 27678 21754 -2198 -1120 9651 N
ATOM 1616 CA VAL A 306 -38.471-126.543 276.188 1.00184.40 C
ANISOU 1616 CA VAL A 306 19958 28463 21641 -2491 -1195 10015 C
ATOM 1617 C VAL A 306 -39.679-125.963 275.469 1.00184.51 C
ANISOU 1617 C VAL A 306 19818 28483 21804 -2369 -1396 10480 C
ATOM 1618 O VAL A 306 -40.722-126.621 275.358 1.00183.95 O
ANISOU 1618 O VAL A 306 19649 28601 21641 -2175 -1500 10385 O
ATOM 1619 CB VAL A 306 -37.777-127.610 275.325 1.00181.19 C
ANISOU 1619 CB VAL A 306 19338 29071 20433 -2742 -1171 9700 C
ATOM 1620 CG1 VAL A 306 -37.274-126.995 274.026 1.00187.13 C
ANISOU 1620 CG1 VAL A 306 19865 30393 20844 -3059 -1243 10072 C
ATOM 1621 CG2 VAL A 306 -36.634-128.253 276.095 1.00176.02 C
ANISOU 1621 CG2 VAL A 306 18821 28419 19640 -2833 -960 9191 C
ATOM 1622 N ALA A 307 -39.545-124.734 274.983 1.00186.61 N
ANISOU 1622 N ALA A 307 20057 28547 22301 -2488 -1452 10980 N
ATOM 1623 CA ALA A 307 -40.626-124.080 274.265 1.00188.67 C
ANISOU 1623 CA ALA A 307 20158 28813 22714 -2392 -1638 11467 C
ATOM 1624 C ALA A 307 -40.566-124.430 272.784 1.00189.41 C
ANISOU 1624 C ALA A 307 19924 29911 22132 -2657 -1757 11658 C
ATOM 1625 O ALA A 307 -39.495-124.688 272.226 1.00187.40 O
ANISOU 1625 O ALA A 307 19577 30226 21400 -2966 -1695 11556 O
ATOM 1626 CB ALA A 307 -40.564-122.566 274.454 1.00196.98 C
ANISOU 1626 CB ALA A 307 21334 29147 24361 -2380 -1650 11922 C
ATOM 1627 N LYS A 308 -41.735-124.442 272.150 1.00151.51 N
ANISOU 1627 N LYS A 308 18587 16564 22414 1203 1136 2415 N
ATOM 1628 CA LYS A 308 -41.875-124.826 270.752 1.00145.14 C
ANISOU 1628 CA LYS A 308 17405 15441 22302 782 1218 2307 C
ATOM 1629 C LYS A 308 -42.216-123.600 269.917 1.00139.91 C
ANISOU 1629 C LYS A 308 16806 14740 21612 712 1144 1844 C
ATOM 1630 O LYS A 308 -43.150-122.860 270.247 1.00141.93 O
ANISOU 1630 O LYS A 308 17210 15223 21495 957 1327 1800 O
ATOM 1631 CB LYS A 308 -42.955-125.897 270.586 1.00144.03 C
ANISOU 1631 CB LYS A 308 16908 15287 22528 679 1640 2763 C
ATOM 1632 N ALA A 309 -41.465-123.394 268.837 1.00138.66 N
ANISOU 1632 N ALA A 309 16519 14319 21847 424 906 1550 N
ATOM 1633 CA ALA A 309 -41.650-122.257 267.946 1.00136.81 C
ANISOU 1633 CA ALA A 309 16297 14028 21657 331 813 1173 C
ATOM 1634 C ALA A 309 -41.927-122.755 266.534 1.00135.06 C
ANISOU 1634 C ALA A 309 15722 13640 21953 42 966 1121 C
ATOM 1635 O ALA A 309 -41.191-123.602 266.015 1.00136.11 O
ANISOU 1635 O ALA A 309 15684 13593 22441 -110 902 1170 O
ATOM 1636 CB ALA A 309 -40.421-121.343 267.954 1.00135.61 C
ANISOU 1636 CB ALA A 309 16316 13754 21457 300 332 909 C
ATOM 1637 N LEU A 310 -42.982-122.227 265.920 1.00131.20 N
ANISOU 1637 N LEU A 310 15152 13221 21478 14 1150 1010 N
ATOM 1638 CA LEU A 310 -43.384-122.595 264.569 1.00126.40 C
ANISOU 1638 CA LEU A 310 14260 12491 21276 -221 1244 917 C
ATOM 1639 C LEU A 310 -43.078-121.448 263.618 1.00121.28 C
ANISOU 1639 C LEU A 310 13611 11834 20634 -278 1092 604 C
ATOM 1640 O LEU A 310 -43.500-120.310 263.853 1.00117.41 O
ANISOU 1640 O LEU A 310 13267 11451 19893 -158 1073 492 O
ATOM 1641 CB LEU A 310 -44.874-122.943 264.514 1.00127.58 C
ANISOU 1641 CB LEU A 310 14235 12732 21508 -244 1537 1112 C
ATOM 1642 CG LEU A 310 -45.472-123.187 263.126 1.00125.33 C
ANISOU 1642 CG LEU A 310 13695 12332 21592 -476 1551 970 C
ATOM 1643 CD1 LEU A 310 -44.758-124.322 262.414 1.00121.86 C
ANISOU 1643 CD1 LEU A 310 13165 11611 21527 -635 1407 896 C
ATOM 1644 CD2 LEU A 310 -46.959-123.477 263.228 1.00126.81 C
ANISOU 1644 CD2 LEU A 310 13659 12613 21909 -520 1779 1248 C
ATOM 1645 N ILE A 311 -42.351-121.750 262.546 1.00120.78 N
ANISOU 1645 N ILE A 311 13384 11652 20855 -414 999 496 N
ATOM 1646 CA ILE A 311 -41.961-120.765 261.544 1.00116.90 C
ANISOU 1646 CA ILE A 311 12815 11186 20413 -457 887 313 C
ATOM 1647 C ILE A 311 -42.522-121.198 260.197 1.00120.21 C
ANISOU 1647 C ILE A 311 13034 11617 21024 -540 1021 205 C
ATOM 1648 O ILE A 311 -42.290-122.330 259.758 1.00122.62 O
ANISOU 1648 O ILE A 311 13263 11808 21519 -564 1047 199 O
ATOM 1649 CB ILE A 311 -40.432-120.605 261.469 1.00108.55 C
ANISOU 1649 CB ILE A 311 11716 10060 19470 -463 651 358 C
ATOM 1650 CG1 ILE A 311 -39.872-120.146 262.817 1.00105.01 C
ANISOU 1650 CG1 ILE A 311 11498 9573 18830 -395 397 428 C
ATOM 1651 CG2 ILE A 311 -40.054-119.631 260.365 1.00107.83 C
ANISOU 1651 CG2 ILE A 311 11457 10022 19490 -505 579 297 C
ATOM 1652 CD1 ILE A 311 -38.372-119.925 262.816 1.00102.20 C
ANISOU 1652 CD1 ILE A 311 11039 9133 18660 -445 85 541 C
ATOM 1653 N VAL A 312 -43.262-120.301 259.547 1.00115.98 N
ANISOU 1653 N VAL A 312 12442 11199 20425 -554 1070 100 N
ATOM 1654 CA VAL A 312 -43.724-120.517 258.184 1.00110.16 C
ANISOU 1654 CA VAL A 312 11538 10517 19800 -603 1126 -29 C
ATOM 1655 C VAL A 312 -43.269-119.341 257.333 1.00 98.45 C
ANISOU 1655 C VAL A 312 9971 9167 18267 -560 1070 -72 C
ATOM 1656 O VAL A 312 -43.111-118.220 257.826 1.00102.43 O
ANISOU 1656 O VAL A 312 10542 9677 18700 -543 988 -20 O
ATOM 1657 CB VAL A 312 -45.257-120.695 258.099 1.00110.32 C
ANISOU 1657 CB VAL A 312 11486 10582 19847 -677 1240 -22 C
ATOM 1658 CG1 VAL A 312 -45.719-121.817 259.018 1.00 99.59 C
ANISOU 1658 CG1 VAL A 312 10137 9090 18613 -735 1304 158 C
ATOM 1659 CG2 VAL A 312 -45.961-119.396 258.434 1.00116.19 C
ANISOU 1659 CG2 VAL A 312 12260 11478 20411 -611 1312 16 C
ATOM 1660 N TYR A 313 -43.047-119.602 256.047 1.00 94.34 N
ANISOU 1660 N TYR A 313 9316 8743 17785 -511 1093 -155 N
ATOM 1661 CA TYR A 313 -42.547-118.565 255.157 1.00105.96 C
ANISOU 1661 CA TYR A 313 10644 10390 19226 -441 1082 -85 C
ATOM 1662 C TYR A 313 -42.977-118.855 253.729 1.00111.98 C
ANISOU 1662 C TYR A 313 11306 11344 19897 -338 1155 -217 C
ATOM 1663 O TYR A 313 -43.145-120.014 253.339 1.00113.17 O
ANISOU 1663 O TYR A 313 11524 11436 20040 -283 1148 -399 O
ATOM 1664 CB TYR A 313 -41.018-118.448 255.229 1.00113.71 C
ANISOU 1664 CB TYR A 313 11529 11362 20314 -374 1013 112 C
ATOM 1665 CG TYR A 313 -40.268-119.722 254.895 1.00117.57 C
ANISOU 1665 CG TYR A 313 11999 11838 20833 -229 1078 86 C
ATOM 1666 CD1 TYR A 313 -40.024-120.088 253.575 1.00119.30 C
ANISOU 1666 CD1 TYR A 313 12117 12259 20954 -1 1200 29 C
ATOM 1667 CD2 TYR A 313 -39.786-120.549 255.901 1.00119.45 C
ANISOU 1667 CD2 TYR A 313 12344 11874 21166 -260 1017 121 C
ATOM 1668 CE1 TYR A 313 -39.337-121.247 253.269 1.00120.97 C
ANISOU 1668 CE1 TYR A 313 12364 12435 21164 221 1260 -37 C
ATOM 1669 CE2 TYR A 313 -39.093-121.708 255.603 1.00120.09 C
ANISOU 1669 CE2 TYR A 313 12418 11904 21307 -90 1075 102 C
ATOM 1670 CZ TYR A 313 -38.871-122.051 254.285 1.00121.99 C
ANISOU 1670 CZ TYR A 313 12586 12313 21453 165 1197 3 C
ATOM 1671 OH TYR A 313 -38.183-123.202 253.979 1.00124.31 O
ANISOU 1671 OH TYR A 313 12923 12534 21776 421 1257 -58 O
ATOM 1672 N GLY A 314 -43.143-117.784 252.953 1.00114.63 N
ANISOU 1672 N GLY A 314 11504 11887 20164 -293 1183 -127 N
ATOM 1673 CA GLY A 314 -43.375-117.910 251.529 1.00118.04 C
ANISOU 1673 CA GLY A 314 11844 12581 20424 -124 1238 -212 C
ATOM 1674 C GLY A 314 -42.065-117.924 250.768 1.00121.73 C
ANISOU 1674 C GLY A 314 12173 13252 20826 128 1333 -33 C
ATOM 1675 O GLY A 314 -41.566-118.990 250.395 1.00132.86 O
ANISOU 1675 O GLY A 314 13662 14675 22142 330 1370 -172 O
ATOM 1676 N SER A 315 -41.502-116.739 250.537 1.00115.49 N
ANISOU 1676 N SER A 315 11155 12608 20116 143 1372 318 N
ATOM 1677 CA SER A 315 -40.166-116.575 249.972 1.00119.88 C
ANISOU 1677 CA SER A 315 11462 13379 20708 362 1489 675 C
ATOM 1678 C SER A 315 -40.007-117.277 248.629 1.00122.59 C
ANISOU 1678 C SER A 315 11793 14093 20694 776 1677 589 C
ATOM 1679 O SER A 315 -39.448-118.378 248.557 1.00129.81 O
ANISOU 1679 O SER A 315 12821 14991 21511 1000 1737 438 O
ATOM 1680 CB SER A 315 -39.100-117.081 250.947 1.00123.41 C
ANISOU 1680 CB SER A 315 11908 13596 21386 299 1421 788 C
ATOM 1681 OG SER A 315 -38.920-118.482 250.839 1.00131.15 O
ANISOU 1681 OG SER A 315 13060 14553 22220 497 1497 527 O
ATOM 1682 N THR A 316 -40.482-116.643 247.556 1.00119.29 N
ANISOU 1682 N THR A 316 11264 14013 20049 932 1760 678 N
ATOM 1683 CA THR A 316 -40.235-117.181 246.222 1.00121.73 C
ANISOU 1683 CA THR A 316 11584 14753 19916 1429 1938 626 C
ATOM 1684 C THR A 316 -38.744-117.182 245.908 1.00124.98 C
ANISOU 1684 C THR A 316 11708 15431 20347 1766 2193 1102 C
ATOM 1685 O THR A 316 -38.173-118.214 245.537 1.00130.00 O
ANISOU 1685 O THR A 316 12474 16184 20737 2166 2319 943 O
ATOM 1686 CB THR A 316 -40.998-116.375 245.169 1.00122.05 C
ANISOU 1686 CB THR A 316 11528 15160 19686 1547 1974 716 C
ATOM 1687 OG1 THR A 316 -42.400-116.636 245.280 1.00119.67 O
ANISOU 1687 OG1 THR A 316 11482 14669 19317 1322 1737 251 O
ATOM 1688 CG2 THR A 316 -40.522-116.745 243.770 1.00127.10 C
ANISOU 1688 CG2 THR A 316 12151 16350 19790 2166 2195 777 C
ATOM 1689 N THR A 317 -38.094-116.027 246.061 1.00124.47 N
ANISOU 1689 N THR A 317 11231 15441 20620 1621 2252 1724 N
ATOM 1690 CA THR A 317 -36.672-115.928 245.752 1.00122.97 C
ANISOU 1690 CA THR A 317 10639 15534 20549 1909 2494 2334 C
ATOM 1691 C THR A 317 -35.823-116.707 246.749 1.00114.43 C
ANISOU 1691 C THR A 317 9595 14137 19747 1816 2419 2296 C
ATOM 1692 O THR A 317 -34.751-117.209 246.391 1.00113.81 O
ANISOU 1692 O THR A 317 9308 14322 19615 2212 2664 2605 O
ATOM 1693 CB THR A 317 -36.242-114.461 245.732 1.00126.80 C
ANISOU 1693 CB THR A 317 10628 16077 21473 1682 2475 3064 C
ATOM 1694 OG1 THR A 317 -37.177-113.698 244.959 1.00127.39 O
ANISOU 1694 OG1 THR A 317 10699 16366 21337 1706 2501 3076 O
ATOM 1695 CG2 THR A 317 -34.858-114.317 245.121 1.00133.30 C
ANISOU 1695 CG2 THR A 317 10917 17327 22405 2047 2783 3845 C
ATOM 1696 N GLY A 318 -36.283-116.825 247.991 1.00112.53 N
ANISOU 1696 N GLY A 318 9604 13375 19776 1351 2110 1960 N
ATOM 1697 CA GLY A 318 -35.524-117.472 249.038 1.00114.01 C
ANISOU 1697 CA GLY A 318 9824 13258 20238 1227 1994 1962 C
ATOM 1698 C GLY A 318 -34.979-116.549 250.106 1.00114.69 C
ANISOU 1698 C GLY A 318 9685 13036 20854 790 1705 2335 C
ATOM 1699 O GLY A 318 -34.169-116.996 250.928 1.00111.35 O
ANISOU 1699 O GLY A 318 9216 12419 20672 710 1584 2445 O
ATOM 1700 N ASN A 319 -35.393-115.279 250.126 1.00113.01 N
ANISOU 1700 N ASN A 319 9355 12744 20839 521 1542 2517 N
ATOM 1701 CA ASN A 319 -34.896-114.346 251.131 1.00112.02 C
ANISOU 1701 CA ASN A 319 9087 12245 21231 121 1158 2803 C
ATOM 1702 C ASN A 319 -35.598-114.545 252.469 1.00104.49 C
ANISOU 1702 C ASN A 319 8607 10845 20251 -166 855 2274 C
ATOM 1703 O ASN A 319 -34.940-114.688 253.506 1.00104.09 O
ANISOU 1703 O ASN A 319 8594 10524 20433 -335 581 2322 O
ATOM 1704 CB ASN A 319 -35.068-112.905 250.646 1.00114.16 C
ANISOU 1704 CB ASN A 319 9085 12526 21766 -24 1059 3192 C
ATOM 1705 CG ASN A 319 -34.264-112.611 249.395 1.00115.46 C
ANISOU 1705 CG ASN A 319 8692 13174 22003 270 1373 3887 C
ATOM 1706 OD1 ASN A 319 -33.070-112.317 249.465 1.00116.32 O
ANISOU 1706 OD1 ASN A 319 8333 13300 22564 224 1300 4524 O
ATOM 1707 ND2 ASN A 319 -34.918-112.680 248.242 1.00114.82 N
ANISOU 1707 ND2 ASN A 319 8633 13518 21475 595 1716 3818 N
ATOM 1708 N THR A 320 -36.935-114.549 252.467 1.00 97.73 N
ANISOU 1708 N THR A 320 8091 9943 19099 -195 903 1814 N
ATOM 1709 CA THR A 320 -37.667-114.788 253.706 1.00102.00 C
ANISOU 1709 CA THR A 320 9048 10149 19557 -381 707 1386 C
ATOM 1710 C THR A 320 -37.371-116.174 254.261 1.00114.46 C
ANISOU 1710 C THR A 320 10793 11680 21017 -303 769 1194 C
ATOM 1711 O THR A 320 -37.422-116.379 255.479 1.00115.96 O
ANISOU 1711 O THR A 320 11222 11608 21229 -442 568 1045 O
ATOM 1712 CB THR A 320 -39.170-114.612 253.481 1.00 95.82 C
ANISOU 1712 CB THR A 320 8497 9400 18511 -381 813 1038 C
ATOM 1713 OG1 THR A 320 -39.403-113.421 252.719 1.00 87.92 O
ANISOU 1713 OG1 THR A 320 7294 8501 17611 -389 813 1266 O
ATOM 1714 CG2 THR A 320 -39.902-114.502 254.813 1.00 96.03 C
ANISOU 1714 CG2 THR A 320 8882 9121 18485 -529 632 745 C
ATOM 1715 N GLU A 321 -37.054-117.135 253.389 1.00123.18 N
ANISOU 1715 N GLU A 321 11797 13030 21974 -35 1038 1197 N
ATOM 1716 CA GLU A 321 -36.552-118.420 253.861 1.00127.43 C
ANISOU 1716 CA GLU A 321 12447 13477 22494 70 1075 1094 C
ATOM 1717 C GLU A 321 -35.191-118.254 254.520 1.00130.62 C
ANISOU 1717 C GLU A 321 12617 13796 23215 7 899 1495 C
ATOM 1718 O GLU A 321 -34.977-118.715 255.647 1.00133.50 O
ANISOU 1718 O GLU A 321 13149 13924 23652 -115 712 1424 O
ATOM 1719 CB GLU A 321 -36.470-119.420 252.708 1.00129.15 C
ANISOU 1719 CB GLU A 321 12654 13939 22479 448 1364 973 C
ATOM 1720 CG GLU A 321 -35.789-120.730 253.090 1.00131.06 C
ANISOU 1720 CG GLU A 321 12982 14056 22760 622 1407 916 C
ATOM 1721 CD GLU A 321 -35.869-121.781 251.999 1.00129.39 C
ANISOU 1721 CD GLU A 321 12893 13989 22280 1047 1627 655 C
ATOM 1722 OE1 GLU A 321 -35.898-122.984 252.335 1.00121.07 O
ANISOU 1722 OE1 GLU A 321 12071 12691 21240 1135 1600 403 O
ATOM 1723 OE2 GLU A 321 -35.904-121.406 250.808 1.00134.28 O
ANISOU 1723 OE2 GLU A 321 13401 14954 22664 1320 1801 699 O
ATOM 1724 N TYR A 322 -34.258-117.594 253.829 1.00132.01 N
ANISOU 1724 N TYR A 322 12366 14185 23605 94 943 1980 N
ATOM 1725 CA TYR A 322 -32.970-117.284 254.441 1.00137.05 C
ANISOU 1725 CA TYR A 322 12692 14726 24655 -30 695 2452 C
ATOM 1726 C TYR A 322 -33.154-116.461 255.709 1.00140.69 C
ANISOU 1726 C TYR A 322 13354 14791 25313 -423 197 2356 C
ATOM 1727 O TYR A 322 -32.413-116.634 256.684 1.00144.72 O
ANISOU 1727 O TYR A 322 13860 15105 26024 -552 -113 2476 O
ATOM 1728 CB TYR A 322 -32.072-116.546 253.449 1.00140.45 C
ANISOU 1728 CB TYR A 322 12550 15456 25358 90 818 3100 C
ATOM 1729 CG TYR A 322 -30.796-116.024 254.069 1.00141.62 C
ANISOU 1729 CG TYR A 322 12283 15457 26069 -131 461 3681 C
ATOM 1730 CD1 TYR A 322 -29.706-116.860 254.267 1.00142.50 C
ANISOU 1730 CD1 TYR A 322 12145 15670 26327 45 530 3988 C
ATOM 1731 CD2 TYR A 322 -30.685-114.696 254.462 1.00142.31 C
ANISOU 1731 CD2 TYR A 322 12223 15264 26584 -515 3 3929 C
ATOM 1732 CE1 TYR A 322 -28.540-116.388 254.838 1.00145.12 C
ANISOU 1732 CE1 TYR A 322 12044 15869 27225 -187 146 4566 C
ATOM 1733 CE2 TYR A 322 -29.524-114.217 255.034 1.00145.23 C
ANISOU 1733 CE2 TYR A 322 12203 15437 27540 -764 -439 4462 C
ATOM 1734 CZ TYR A 322 -28.455-115.066 255.219 1.00146.47 C
ANISOU 1734 CZ TYR A 322 12070 15740 27843 -614 -369 4799 C
ATOM 1735 OH TYR A 322 -27.295-114.593 255.786 1.00152.40 O
ANISOU 1735 OH TYR A 322 12379 16299 29229 -889 -863 5378 O
ATOM 1736 N THR A 323 -34.135-115.556 255.712 1.00139.85 N
ANISOU 1736 N THR A 323 13446 14568 25122 -571 97 2130 N
ATOM 1737 CA THR A 323 -34.494-114.859 256.941 1.00139.02 C
ANISOU 1737 CA THR A 323 13671 14084 25065 -822 -348 1903 C
ATOM 1738 C THR A 323 -34.976-115.849 257.993 1.00138.60 C
ANISOU 1738 C THR A 323 14045 13929 24687 -779 -339 1508 C
ATOM 1739 O THR A 323 -34.438-115.906 259.105 1.00141.33 O
ANISOU 1739 O THR A 323 14528 14070 25100 -875 -690 1518 O
ATOM 1740 CB THR A 323 -35.569-113.807 256.658 1.00133.45 C
ANISOU 1740 CB THR A 323 13122 13304 24279 -885 -366 1712 C
ATOM 1741 OG1 THR A 323 -35.101-112.898 255.655 1.00136.66 O
ANISOU 1741 OG1 THR A 323 13091 13810 25022 -922 -363 2165 O
ATOM 1742 CG2 THR A 323 -35.898-113.029 257.925 1.00130.07 C
ANISOU 1742 CG2 THR A 323 13088 12477 23857 -1040 -833 1449 C
ATOM 1743 N ALA A 324 -35.985-116.653 257.646 1.00136.32 N
ANISOU 1743 N ALA A 324 13946 13784 24065 -635 33 1200 N
ATOM 1744 CA ALA A 324 -36.489-117.662 258.573 1.00131.17 C
ANISOU 1744 CA ALA A 324 13622 13045 23172 -597 84 936 C
ATOM 1745 C ALA A 324 -35.389-118.627 258.994 1.00133.21 C
ANISOU 1745 C ALA A 324 13775 13281 23558 -538 33 1132 C
ATOM 1746 O ALA A 324 -35.329-119.039 260.158 1.00133.79 O
ANISOU 1746 O ALA A 324 14075 13217 23541 -570 -137 1076 O
ATOM 1747 CB ALA A 324 -37.656-118.419 257.942 1.00124.90 C
ANISOU 1747 CB ALA A 324 12935 12375 22148 -491 444 672 C
ATOM 1748 N GLU A 325 -34.508-118.999 258.061 1.00134.77 N
ANISOU 1748 N GLU A 325 13623 13647 23936 -400 200 1396 N
ATOM 1749 CA GLU A 325 -33.376-119.850 258.415 1.00137.51 C
ANISOU 1749 CA GLU A 325 13814 13985 24448 -302 162 1645 C
ATOM 1750 C GLU A 325 -32.426-119.131 259.365 1.00140.70 C
ANISOU 1750 C GLU A 325 14103 14237 25119 -508 -317 1935 C
ATOM 1751 O GLU A 325 -31.831-119.755 260.251 1.00143.98 O
ANISOU 1751 O GLU A 325 14567 14559 25579 -508 -492 2030 O
ATOM 1752 CB GLU A 325 -32.637-120.301 257.154 1.00137.72 C
ANISOU 1752 CB GLU A 325 13479 14275 24575 -13 486 1898 C
ATOM 1753 CG GLU A 325 -33.396-121.325 256.322 1.00139.97 C
ANISOU 1753 CG GLU A 325 13958 14645 24579 256 857 1546 C
ATOM 1754 CD GLU A 325 -32.730-121.605 254.989 1.00145.95 C
ANISOU 1754 CD GLU A 325 14430 15717 25308 653 1179 1743 C
ATOM 1755 OE1 GLU A 325 -31.708-120.954 254.684 1.00146.30 O
ANISOU 1755 OE1 GLU A 325 14046 15962 25580 706 1179 2246 O
ATOM 1756 OE2 GLU A 325 -33.230-122.475 254.245 1.00150.60 O
ANISOU 1756 OE2 GLU A 325 15220 16353 25649 937 1413 1413 O
ATOM 1757 N THR A 326 -32.270-117.816 259.197 1.00140.05 N
ANISOU 1757 N THR A 326 13871 14096 25247 -692 -588 2089 N
ATOM 1758 CA THR A 326 -31.499-117.034 260.156 1.00142.86 C
ANISOU 1758 CA THR A 326 14192 14204 25886 -932 -1190 2283 C
ATOM 1759 C THR A 326 -32.303-116.752 261.420 1.00143.08 C
ANISOU 1759 C THR A 326 14793 13991 25579 -1010 -1504 1838 C
ATOM 1760 O THR A 326 -31.731-116.702 262.516 1.00141.83 O
ANISOU 1760 O THR A 326 14780 13658 25452 -1094 -1972 1865 O
ATOM 1761 CB THR A 326 -31.035-115.721 259.518 1.00142.75 C
ANISOU 1761 CB THR A 326 13800 14129 26308 -1115 -1434 2640 C
ATOM 1762 OG1 THR A 326 -30.504-115.983 258.212 1.00141.77 O
ANISOU 1762 OG1 THR A 326 13155 14345 26366 -935 -996 3071 O
ATOM 1763 CG2 THR A 326 -29.953-115.070 260.365 1.00145.93 C
ANISOU 1763 CG2 THR A 326 14041 14240 27164 -1384 -2139 2951 C
ATOM 1764 N ILE A 327 -33.621-116.573 261.289 1.00143.40 N
ANISOU 1764 N ILE A 327 15158 14055 25274 -940 -1251 1453 N
ATOM 1765 CA ILE A 327 -34.475-116.391 262.461 1.00142.01 C
ANISOU 1765 CA ILE A 327 15517 13741 24699 -896 -1422 1073 C
ATOM 1766 C ILE A 327 -34.467-117.646 263.323 1.00143.47 C
ANISOU 1766 C ILE A 327 15889 14002 24620 -766 -1303 1038 C
ATOM 1767 O ILE A 327 -34.416-117.573 264.557 1.00143.74 O
ANISOU 1767 O ILE A 327 16262 13939 24415 -720 -1630 931 O
ATOM 1768 CB ILE A 327 -35.907-116.020 262.027 1.00136.74 C
ANISOU 1768 CB ILE A 327 15049 13143 23763 -812 -1090 773 C
ATOM 1769 CG1 ILE A 327 -35.960-114.606 261.444 1.00140.14 C
ANISOU 1769 CG1 ILE A 327 15379 13431 24435 -927 -1307 799 C
ATOM 1770 CG2 ILE A 327 -36.864-116.133 263.197 1.00135.15 C
ANISOU 1770 CG2 ILE A 327 15344 12918 23089 -654 -1087 464 C
ATOM 1771 CD1 ILE A 327 -35.943-113.514 262.485 1.00147.08 C
ANISOU 1771 CD1 ILE A 327 16635 13976 25272 -958 -1881 598 C
ATOM 1772 N ALA A 328 -34.503-118.819 262.684 1.00146.20 N
ANISOU 1772 N ALA A 328 16038 14511 25002 -673 -859 1133 N
ATOM 1773 CA ALA A 328 -34.645-120.070 263.422 1.00147.24 C
ANISOU 1773 CA ALA A 328 16332 14670 24944 -554 -705 1131 C
ATOM 1774 C ALA A 328 -33.417-120.367 264.273 1.00153.02 C
ANISOU 1774 C ALA A 328 17002 15339 25800 -568 -1072 1388 C
ATOM 1775 O ALA A 328 -33.541-120.912 265.376 1.00157.04 O
ANISOU 1775 O ALA A 328 17773 15841 26052 -482 -1157 1378 O
ATOM 1776 CB ALA A 328 -34.909-121.222 262.454 1.00143.43 C
ANISOU 1776 CB ALA A 328 15668 14273 24556 -452 -238 1143 C
ATOM 1777 N ARG A 329 -32.225-120.021 263.783 1.00152.80 N
ANISOU 1777 N ARG A 329 16590 15295 26170 -661 -1291 1685 N
ATOM 1778 CA ARG A 329 -31.008-120.422 264.481 1.00154.48 C
ANISOU 1778 CA ARG A 329 16648 15471 26574 -676 -1628 2003 C
ATOM 1779 C ARG A 329 -30.854-119.696 265.812 1.00155.27 C
ANISOU 1779 C ARG A 329 17090 15419 26488 -771 -2257 1897 C
ATOM 1780 O ARG A 329 -30.459-120.310 266.809 1.00157.42 O
ANISOU 1780 O ARG A 329 17502 15700 26610 -696 -2460 1990 O
ATOM 1781 CB ARG A 329 -29.790-120.205 263.586 1.00159.27 C
ANISOU 1781 CB ARG A 329 16675 16137 27702 -733 -1681 2443 C
ATOM 1782 CG ARG A 329 -29.448-121.445 262.780 1.00162.66 C
ANISOU 1782 CG ARG A 329 16826 16738 28238 -481 -1158 2632 C
ATOM 1783 CD ARG A 329 -28.609-121.138 261.558 1.00168.04 C
ANISOU 1783 CD ARG A 329 16951 17594 29302 -409 -987 3028 C
ATOM 1784 NE ARG A 329 -28.610-122.271 260.637 1.00168.87 N
ANISOU 1784 NE ARG A 329 16949 17869 29343 -51 -416 3027 N
ATOM 1785 CZ ARG A 329 -28.038-122.265 259.438 1.00170.43 C
ANISOU 1785 CZ ARG A 329 16733 18312 29712 186 -94 3321 C
ATOM 1786 NH1 ARG A 329 -27.411-121.181 259.004 1.00172.70 N
ANISOU 1786 NH1 ARG A 329 16585 18718 30314 54 -256 3742 N
ATOM 1787 NH2 ARG A 329 -28.096-123.346 258.672 1.00169.99 N
ANISOU 1787 NH2 ARG A 329 16704 18373 29512 588 378 3213 N
ATOM 1788 N GLU A 330 -31.160-118.395 265.857 1.00155.46 N
ANISOU 1788 N GLU A 330 17283 15287 26497 -899 -2603 1689 N
ATOM 1789 CA GLU A 330 -31.174-117.700 267.142 1.00154.68 C
ANISOU 1789 CA GLU A 330 17652 15011 26108 -898 -3227 1453 C
ATOM 1790 C GLU A 330 -32.140-118.371 268.110 1.00151.16 C
ANISOU 1790 C GLU A 330 17713 14718 25003 -613 -2970 1192 C
ATOM 1791 O GLU A 330 -31.805-118.592 269.279 1.00153.94 O
ANISOU 1791 O GLU A 330 18350 15081 25059 -498 -3336 1187 O
ATOM 1792 CB GLU A 330 -31.537-116.226 266.951 1.00152.78 C
ANISOU 1792 CB GLU A 330 17582 14521 25947 -1017 -3585 1200 C
ATOM 1793 CG GLU A 330 -32.190-115.561 268.166 1.00154.28 C
ANISOU 1793 CG GLU A 330 18475 14566 25579 -830 -3996 729 C
ATOM 1794 CD GLU A 330 -31.330-115.589 269.419 1.00158.74 C
ANISOU 1794 CD GLU A 330 19294 15016 26005 -806 -4716 732 C
ATOM 1795 OE1 GLU A 330 -31.824-116.056 270.468 1.00157.47 O
ANISOU 1795 OE1 GLU A 330 19617 15024 25191 -491 -4664 523 O
ATOM 1796 OE2 GLU A 330 -30.164-115.146 269.357 1.00163.67 O
ANISOU 1796 OE2 GLU A 330 19610 15403 27176 -1093 -5345 989 O
ATOM 1797 N LEU A 331 -33.337-118.718 267.636 1.00144.20 N
ANISOU 1797 N LEU A 331 16912 13980 23896 -488 -2351 1031 N
ATOM 1798 CA LEU A 331 -34.259-119.489 268.462 1.00143.82 C
ANISOU 1798 CA LEU A 331 17203 14115 23328 -229 -2019 946 C
ATOM 1799 C LEU A 331 -33.673-120.854 268.802 1.00148.82 C
ANISOU 1799 C LEU A 331 17660 14845 24040 -182 -1876 1279 C
ATOM 1800 O LEU A 331 -33.716-121.290 269.959 1.00153.10 O
ANISOU 1800 O LEU A 331 18483 15494 24196 9 -1980 1345 O
ATOM 1801 CB LEU A 331 -35.603-119.639 267.749 1.00140.97 C
ANISOU 1801 CB LEU A 331 16829 13861 22871 -171 -1417 809 C
ATOM 1802 CG LEU A 331 -36.340-118.339 267.427 1.00145.11 C
ANISOU 1802 CG LEU A 331 17533 14312 23290 -163 -1484 502 C
ATOM 1803 CD1 LEU A 331 -37.561-118.615 266.562 1.00144.01 C
ANISOU 1803 CD1 LEU A 331 17260 14300 23157 -148 -897 449 C
ATOM 1804 CD2 LEU A 331 -36.736-117.621 268.708 1.00151.00 C
ANISOU 1804 CD2 LEU A 331 18838 15055 23480 110 -1799 249 C
ATOM 1805 N ALA A 332 -33.109-121.540 267.805 1.00147.95 N
ANISOU 1805 N ALA A 332 17098 14711 24405 -301 -1632 1507 N
ATOM 1806 CA ALA A 332 -32.553-122.867 268.044 1.00149.57 C
ANISOU 1806 CA ALA A 332 17134 14953 24743 -221 -1480 1817 C
ATOM 1807 C ALA A 332 -31.321-122.794 268.942 1.00157.11 C
ANISOU 1807 C ALA A 332 18066 15889 25739 -234 -2039 2052 C
ATOM 1808 O ALA A 332 -31.179-123.591 269.877 1.00160.39 O
ANISOU 1808 O ALA A 332 18613 16380 25948 -89 -2071 2234 O
ATOM 1809 CB ALA A 332 -32.226-123.548 266.714 1.00143.79 C
ANISOU 1809 CB ALA A 332 15983 14187 24466 -253 -1106 1943 C
ATOM 1810 N ASP A 333 -30.429-121.827 268.689 1.00160.12 N
ANISOU 1810 N ASP A 333 18256 16165 26417 -419 -2521 2097 N
ATOM 1811 CA ASP A 333 -29.261-121.651 269.550 1.00163.58 C
ANISOU 1811 CA ASP A 333 18650 16553 26950 -479 -3178 2325 C
ATOM 1812 C ASP A 333 -29.677-121.256 270.962 1.00167.12 C
ANISOU 1812 C ASP A 333 19699 17024 26775 -330 -3605 2065 C
ATOM 1813 O ASP A 333 -29.051-121.677 271.940 1.00171.53 O
ANISOU 1813 O ASP A 333 20354 17646 27172 -240 -3966 2250 O
ATOM 1814 CB ASP A 333 -28.312-120.617 268.936 1.00167.79 C
ANISOU 1814 CB ASP A 333 18801 16924 28027 -755 -3648 2480 C
ATOM 1815 CG ASP A 333 -27.014-120.448 269.725 1.00178.82 C
ANISOU 1815 CG ASP A 333 20042 18237 29666 -880 -4408 2791 C
ATOM 1816 OD1 ASP A 333 -26.642-121.353 270.508 1.00180.87 O
ANISOU 1816 OD1 ASP A 333 20354 18614 29755 -732 -4456 2981 O
ATOM 1817 OD2 ASP A 333 -26.352-119.403 269.541 1.00185.13 O
ANISOU 1817 OD2 ASP A 333 20626 18834 30883 -1145 -4991 2891 O
ATOM 1818 N ALA A 334 -30.744-120.466 271.094 1.00166.58 N
ANISOU 1818 N ALA A 334 20053 16936 26303 -242 -3552 1646 N
ATOM 1819 CA ALA A 334 -31.215-120.109 272.428 1.00171.74 C
ANISOU 1819 CA ALA A 334 21335 17670 26248 34 -3882 1376 C
ATOM 1820 C ALA A 334 -31.748-121.328 273.171 1.00171.78 C
ANISOU 1820 C ALA A 334 21493 17972 25804 336 -3415 1577 C
ATOM 1821 O ALA A 334 -31.567-121.447 274.388 1.00175.93 O
ANISOU 1821 O ALA A 334 22381 18642 25821 584 -3752 1601 O
ATOM 1822 CB ALA A 334 -32.291-119.031 272.347 1.00172.57 C
ANISOU 1822 CB ALA A 334 21840 17707 26020 147 -3837 911 C
ATOM 1823 N GLY A 335 -32.408-122.239 272.460 1.00167.94 N
ANISOU 1823 N GLY A 335 20735 17567 25506 328 -2680 1745 N
ATOM 1824 CA GLY A 335 -32.991-123.406 273.091 1.00169.94 C
ANISOU 1824 CA GLY A 335 21065 18040 25463 569 -2228 2013 C
ATOM 1825 C GLY A 335 -34.473-123.548 272.815 1.00169.84 C
ANISOU 1825 C GLY A 335 21143 18140 25251 685 -1602 1921 C
ATOM 1826 O GLY A 335 -35.245-123.949 273.694 1.00173.80 O
ANISOU 1826 O GLY A 335 21882 18886 25267 979 -1343 2072 O
ATOM 1827 N TYR A 336 -34.879-123.218 271.592 1.00166.66 N
ANISOU 1827 N TYR A 336 20511 17588 25224 471 -1356 1731 N
ATOM 1828 CA TYR A 336 -36.260-123.334 271.146 1.00166.15 C
ANISOU 1828 CA TYR A 336 20441 17598 25092 516 -809 1662 C
ATOM 1829 C TYR A 336 -36.392-124.499 270.175 1.00167.74 C
ANISOU 1829 C TYR A 336 20233 17666 25837 333 -395 1866 C
ATOM 1830 O TYR A 336 -35.605-124.617 269.230 1.00167.28 O
ANISOU 1830 O TYR A 336 19893 17432 26236 146 -476 1834 O
ATOM 1831 CB TYR A 336 -36.729-122.044 270.467 1.00163.26 C
ANISOU 1831 CB TYR A 336 20162 17159 24712 438 -882 1265 C
ATOM 1832 CG TYR A 336 -37.414-121.053 271.380 1.00167.59 C
ANISOU 1832 CG TYR A 336 21200 17854 24624 749 -1020 1016 C
ATOM 1833 CD1 TYR A 336 -38.798-121.008 271.467 1.00167.75 C
ANISOU 1833 CD1 TYR A 336 21320 18071 24347 962 -542 1009 C
ATOM 1834 CD2 TYR A 336 -36.681-120.149 272.139 1.00173.07 C
ANISOU 1834 CD2 TYR A 336 22258 18474 25027 860 -1658 787 C
ATOM 1835 CE1 TYR A 336 -39.437-120.098 272.286 1.00171.75 C
ANISOU 1835 CE1 TYR A 336 22292 18740 24224 1352 -613 781 C
ATOM 1836 CE2 TYR A 336 -37.311-119.233 272.967 1.00176.94 C
ANISOU 1836 CE2 TYR A 336 23284 19066 24878 1235 -1815 481 C
ATOM 1837 CZ TYR A 336 -38.691-119.213 273.036 1.00175.65 C
ANISOU 1837 CZ TYR A 336 23227 19142 24370 1517 -1249 479 C
ATOM 1838 OH TYR A 336 -39.327-118.309 273.855 1.00178.47 O
ANISOU 1838 OH TYR A 336 24133 19633 24045 1992 -1350 182 O
ATOM 1839 N GLU A 337 -37.382-125.360 270.406 1.00171.32 N
ANISOU 1839 N GLU A 337 20651 18192 26251 417 28 2097 N
ATOM 1840 CA GLU A 337 -37.746-126.330 269.385 1.00170.26 C
ANISOU 1840 CA GLU A 337 20195 17847 26648 234 350 2180 C
ATOM 1841 C GLU A 337 -38.309-125.586 268.187 1.00167.20 C
ANISOU 1841 C GLU A 337 19724 17401 26406 81 441 1821 C
ATOM 1842 O GLU A 337 -39.264-124.813 268.320 1.00170.25 O
ANISOU 1842 O GLU A 337 20247 17939 26501 144 552 1690 O
ATOM 1843 CB GLU A 337 -38.777-127.325 269.910 1.00174.76 C
ANISOU 1843 CB GLU A 337 20706 18458 27235 305 711 2558 C
ATOM 1844 CG GLU A 337 -39.164-128.386 268.887 1.00176.77 C
ANISOU 1844 CG GLU A 337 20669 18389 28106 93 917 2611 C
ATOM 1845 CD GLU A 337 -40.650-128.684 268.886 1.00181.74 C
ANISOU 1845 CD GLU A 337 21186 19048 28818 41 1236 2805 C
ATOM 1846 OE1 GLU A 337 -41.267-128.659 269.973 1.00186.93 O
ANISOU 1846 OE1 GLU A 337 21912 19983 29130 231 1412 3167 O
ATOM 1847 OE2 GLU A 337 -41.203-128.936 267.796 1.00180.74 O
ANISOU 1847 OE2 GLU A 337 20889 18692 29092 -163 1301 2625 O
ATOM 1848 N VAL A 338 -37.714-125.810 267.018 1.00161.55 N
ANISOU 1848 N VAL A 338 18784 16494 26102 -65 413 1685 N
ATOM 1849 CA VAL A 338 -38.092-125.109 265.799 1.00156.67 C
ANISOU 1849 CA VAL A 338 18070 15857 25600 -180 476 1377 C
ATOM 1850 C VAL A 338 -38.678-126.106 264.809 1.00155.80 C
ANISOU 1850 C VAL A 338 17785 15566 25845 -260 720 1337 C
ATOM 1851 O VAL A 338 -38.205-127.242 264.692 1.00157.40 O
ANISOU 1851 O VAL A 338 17899 15571 26335 -235 743 1469 O
ATOM 1852 CB VAL A 338 -36.897-124.356 265.175 1.00154.19 C
ANISOU 1852 CB VAL A 338 17641 15533 25410 -224 218 1267 C
ATOM 1853 CG1 VAL A 338 -36.332-123.349 266.169 1.00153.62 C
ANISOU 1853 CG1 VAL A 338 17761 15545 25065 -190 -161 1278 C
ATOM 1854 CG2 VAL A 338 -35.806-125.322 264.717 1.00155.97 C
ANISOU 1854 CG2 VAL A 338 17644 15636 25983 -183 216 1428 C
ATOM 1855 N ASP A 339 -39.728-125.677 264.106 1.00152.63 N
ANISOU 1855 N ASP A 339 17355 15205 25433 -343 857 1143 N
ATOM 1856 CA ASP A 339 -40.374-126.463 263.058 1.00149.13 C
ANISOU 1856 CA ASP A 339 16781 14575 25308 -435 977 1025 C
ATOM 1857 C ASP A 339 -40.674-125.521 261.890 1.00144.52 C
ANISOU 1857 C ASP A 339 16146 14106 24659 -476 980 715 C
ATOM 1858 O ASP A 339 -41.830-125.219 261.593 1.00146.44 O
ANISOU 1858 O ASP A 339 16359 14408 24873 -561 1073 641 O
ATOM 1859 CB ASP A 339 -41.640-127.142 263.571 1.00149.11 C
ANISOU 1859 CB ASP A 339 16737 14500 25419 -522 1128 1251 C
ATOM 1860 CG ASP A 339 -42.273-128.055 262.536 1.00148.82 C
ANISOU 1860 CG ASP A 339 16576 14169 25802 -661 1115 1123 C
ATOM 1861 OD1 ASP A 339 -41.566-128.944 262.016 1.00150.61 O
ANISOU 1861 OD1 ASP A 339 16813 14118 26294 -615 1009 1020 O
ATOM 1862 OD2 ASP A 339 -43.475-127.877 262.240 1.00146.21 O
ANISOU 1862 OD2 ASP A 339 16146 13870 25536 -791 1177 1119 O
ATOM 1863 N SER A 340 -39.618-125.036 261.244 1.00140.89 N
ANISOU 1863 N SER A 340 15633 13708 24191 -402 886 606 N
ATOM 1864 CA SER A 340 -39.789-124.196 260.068 1.00142.29 C
ANISOU 1864 CA SER A 340 15727 14022 24317 -405 908 391 C
ATOM 1865 C SER A 340 -40.433-125.000 258.946 1.00140.55 C
ANISOU 1865 C SER A 340 15471 13690 24244 -394 982 179 C
ATOM 1866 O SER A 340 -40.051-126.145 258.680 1.00141.04 O
ANISOU 1866 O SER A 340 15552 13540 24496 -302 967 140 O
ATOM 1867 CB SER A 340 -38.444-123.635 259.602 1.00147.16 C
ANISOU 1867 CB SER A 340 16213 14744 24956 -303 820 453 C
ATOM 1868 OG SER A 340 -37.750-124.573 258.800 1.00152.26 O
ANISOU 1868 OG SER A 340 16768 15328 25757 -127 894 428 O
ATOM 1869 N ARG A 341 -41.423-124.398 258.292 1.00139.19 N
ANISOU 1869 N ARG A 341 15268 13632 23986 -470 1018 24 N
ATOM 1870 CA ARG A 341 -42.174-125.064 257.235 1.00136.65 C
ANISOU 1870 CA ARG A 341 14938 13204 23780 -482 991 -211 C
ATOM 1871 C ARG A 341 -42.471-124.080 256.115 1.00124.22 C
ANISOU 1871 C ARG A 341 13295 11889 22014 -433 1010 -381 C
ATOM 1872 O ARG A 341 -42.965-122.978 256.370 1.00118.05 O
ANISOU 1872 O ARG A 341 12462 11287 21105 -519 1057 -298 O
ATOM 1873 CB ARG A 341 -43.484-125.655 257.773 1.00142.95 C
ANISOU 1873 CB ARG A 341 15716 13825 24772 -692 972 -119 C
ATOM 1874 CG ARG A 341 -43.295-126.879 258.653 1.00151.18 C
ANISOU 1874 CG ARG A 341 16793 14564 26083 -733 943 88 C
ATOM 1875 CD ARG A 341 -44.623-127.432 259.144 1.00158.69 C
ANISOU 1875 CD ARG A 341 17629 15363 27304 -955 939 310 C
ATOM 1876 NE ARG A 341 -44.449-128.679 259.884 1.00168.56 N
ANISOU 1876 NE ARG A 341 18874 16284 28888 -1003 897 569 N
ATOM 1877 CZ ARG A 341 -45.443-129.359 260.444 1.00177.60 C
ANISOU 1877 CZ ARG A 341 19855 17249 30377 -1199 896 914 C
ATOM 1878 NH1 ARG A 341 -46.687-128.909 260.353 1.00176.84 N
ANISOU 1878 NH1 ARG A 341 19569 17298 30322 -1354 945 1038 N
ATOM 1879 NH2 ARG A 341 -45.195-130.487 261.099 1.00185.22 N
ANISOU 1879 NH2 ARG A 341 20799 17895 31683 -1233 853 1203 N
ATOM 1880 N ASP A 342 -42.166-124.480 254.882 1.00120.47 N
ANISOU 1880 N ASP A 342 12842 11440 21492 -243 974 -614 N
ATOM 1881 CA ASP A 342 -42.553-123.689 253.724 1.00112.83 C
ANISOU 1881 CA ASP A 342 11811 10747 20311 -162 988 -755 C
ATOM 1882 C ASP A 342 -44.070-123.570 253.669 1.00108.09 C
ANISOU 1882 C ASP A 342 11185 10111 19772 -393 897 -833 C
ATOM 1883 O ASP A 342 -44.794-124.534 253.930 1.00112.29 O
ANISOU 1883 O ASP A 342 11761 10360 20544 -544 761 -894 O
ATOM 1884 CB ASP A 342 -42.019-124.337 252.443 1.00119.62 C
ANISOU 1884 CB ASP A 342 12763 11659 21029 176 959 -1015 C
ATOM 1885 CG ASP A 342 -42.012-123.387 251.261 1.00123.63 C
ANISOU 1885 CG ASP A 342 13174 12574 21227 369 1041 -1042 C
ATOM 1886 OD1 ASP A 342 -42.859-122.468 251.218 1.00131.54 O
ANISOU 1886 OD1 ASP A 342 14072 13719 22187 179 1032 -977 O
ATOM 1887 OD2 ASP A 342 -41.154-123.565 250.370 1.00118.27 O
ANISOU 1887 OD2 ASP A 342 12509 12095 20332 757 1140 -1089 O
ATOM 1888 N ALA A 343 -44.554-122.372 253.333 1.00107.13 N
ANISOU 1888 N ALA A 343 10950 10263 19491 -425 960 -773 N
ATOM 1889 CA ALA A 343 -45.994-122.149 253.280 1.00108.33 C
ANISOU 1889 CA ALA A 343 11018 10433 19710 -616 899 -780 C
ATOM 1890 C ALA A 343 -46.668-122.974 252.192 1.00106.69 C
ANISOU 1890 C ALA A 343 10847 10138 19552 -617 658 -1068 C
ATOM 1891 O ALA A 343 -47.891-123.150 252.233 1.00107.12 O
ANISOU 1891 O ALA A 343 10794 10113 19795 -833 526 -1040 O
ATOM 1892 CB ALA A 343 -46.292-120.664 253.065 1.00108.01 C
ANISOU 1892 CB ALA A 343 10858 10688 19493 -596 1011 -657 C
ATOM 1893 N ALA A 344 -45.904-123.482 251.223 1.00103.86 N
ANISOU 1893 N ALA A 344 10640 9799 19025 -350 574 -1334 N
ATOM 1894 CA ALA A 344 -46.475-124.277 250.144 1.00109.31 C
ANISOU 1894 CA ALA A 344 11465 10378 19692 -279 257 -1705 C
ATOM 1895 C ALA A 344 -46.885-125.675 250.589 1.00124.44 C
ANISOU 1895 C ALA A 344 13489 11769 22025 -470 -28 -1830 C
ATOM 1896 O ALA A 344 -47.575-126.368 249.833 1.00125.46 O
ANISOU 1896 O ALA A 344 13727 11686 22255 -506 -417 -2140 O
ATOM 1897 CB ALA A 344 -45.480-124.370 248.985 1.00105.17 C
ANISOU 1897 CB ALA A 344 11120 10078 18762 192 289 -1957 C
ATOM 1898 N SER A 345 -46.484-126.106 251.796 1.00129.74 N
ANISOU 1898 N SER A 345 14130 12203 22963 -596 109 -1577 N
ATOM 1899 CA SER A 345 -46.783-127.447 252.308 1.00135.71 C
ANISOU 1899 CA SER A 345 14947 12431 24186 -780 -134 -1586 C
ATOM 1900 C SER A 345 -47.194-127.314 253.776 1.00137.94 C
ANISOU 1900 C SER A 345 15002 12670 24738 -1067 75 -1082 C
ATOM 1901 O SER A 345 -46.434-127.641 254.690 1.00139.20 O
ANISOU 1901 O SER A 345 15202 12726 24962 -1019 239 -881 O
ATOM 1902 CB SER A 345 -45.588-128.385 252.143 1.00134.61 C
ANISOU 1902 CB SER A 345 15074 12039 24033 -472 -172 -1810 C
ATOM 1903 OG SER A 345 -44.416-127.825 252.711 1.00129.05 O
ANISOU 1903 OG SER A 345 14329 11599 23104 -286 194 -1578 O
ATOM 1904 N VAL A 346 -48.414-126.827 254.002 1.00141.88 N
ANISOU 1904 N VAL A 346 15256 13290 25365 -1317 80 -849 N
ATOM 1905 CA VAL A 346 -48.944-126.652 255.348 1.00145.72 C
ANISOU 1905 CA VAL A 346 15522 13822 26024 -1494 324 -340 C
ATOM 1906 C VAL A 346 -50.389-127.128 255.390 1.00157.23 C
ANISOU 1906 C VAL A 346 16683 15105 27950 -1814 126 -87 C
ATOM 1907 O VAL A 346 -51.112-127.083 254.389 1.00157.37 O
ANISOU 1907 O VAL A 346 16631 15109 28055 -1917 -167 -298 O
ATOM 1908 CB VAL A 346 -48.850-125.185 255.830 1.00141.24 C
ANISOU 1908 CB VAL A 346 14909 13717 25038 -1360 678 -178 C
ATOM 1909 CG1 VAL A 346 -47.398-124.772 256.014 1.00137.79 C
ANISOU 1909 CG1 VAL A 346 14688 13387 24279 -1117 818 -296 C
ATOM 1910 CG2 VAL A 346 -49.562-124.256 254.857 1.00141.52 C
ANISOU 1910 CG2 VAL A 346 14841 14025 24903 -1356 628 -323 C
ATOM 1911 N GLU A 347 -50.803-127.592 256.566 1.00166.14 N
ANISOU 1911 N GLU A 347 17608 16126 29393 -1960 278 424 N
ATOM 1912 CA GLU A 347 -52.181-127.983 256.828 1.00175.72 C
ANISOU 1912 CA GLU A 347 18417 17233 31117 -2264 178 876 C
ATOM 1913 C GLU A 347 -52.851-126.888 257.648 1.00175.62 C
ANISOU 1913 C GLU A 347 18165 17724 30839 -2158 637 1324 C
ATOM 1914 O GLU A 347 -52.309-126.451 258.668 1.00173.29 O
ANISOU 1914 O GLU A 347 17991 17660 30193 -1924 1014 1510 O
ATOM 1915 CB GLU A 347 -52.234-129.322 257.565 1.00185.50 C
ANISOU 1915 CB GLU A 347 19530 18010 32943 -2464 56 1258 C
ATOM 1916 CG GLU A 347 -51.502-130.446 256.843 1.00192.86 C
ANISOU 1916 CG GLU A 347 20765 18370 34142 -2496 -402 785 C
ATOM 1917 CD GLU A 347 -51.138-131.598 257.762 1.00198.97 C
ANISOU 1917 CD GLU A 347 21508 18725 35367 -2578 -408 1157 C
ATOM 1918 OE1 GLU A 347 -51.693-131.672 258.878 1.00202.18 O
ANISOU 1918 OE1 GLU A 347 21576 19257 35988 -2687 -123 1861 O
ATOM 1919 OE2 GLU A 347 -50.289-132.427 257.369 1.00201.08 O
ANISOU 1919 OE2 GLU A 347 22088 18560 35752 -2485 -675 775 O
ATOM 1920 N ALA A 348 -54.027-126.447 257.196 1.00179.28 N
ANISOU 1920 N ALA A 348 18311 18353 31454 -2291 575 1480 N
ATOM 1921 CA ALA A 348 -54.673-125.282 257.795 1.00178.96 C
ANISOU 1921 CA ALA A 348 18084 18811 31103 -2095 1015 1824 C
ATOM 1922 C ALA A 348 -55.133-125.567 259.220 1.00182.26 C
ANISOU 1922 C ALA A 348 18247 19355 31648 -2026 1402 2533 C
ATOM 1923 O ALA A 348 -54.679-124.924 260.174 1.00180.80 O
ANISOU 1923 O ALA A 348 18265 19466 30966 -1682 1804 2627 O
ATOM 1924 CB ALA A 348 -55.851-124.839 256.928 1.00182.20 C
ANISOU 1924 CB ALA A 348 18162 19360 31706 -2247 840 1878 C
ATOM 1925 N GLY A 349 -56.042-126.526 259.381 1.00187.36 N
ANISOU 1925 N GLY A 349 18442 19783 32963 -2332 1261 3065 N
ATOM 1926 CA GLY A 349 -56.647-126.809 260.668 1.00191.57 C
ANISOU 1926 CA GLY A 349 18617 20512 33658 -2245 1672 3894 C
ATOM 1927 C GLY A 349 -55.667-127.220 261.747 1.00191.07 C
ANISOU 1927 C GLY A 349 18846 20424 33329 -2027 1914 4002 C
ATOM 1928 O GLY A 349 -54.910-128.180 261.578 1.00191.11 O
ANISOU 1928 O GLY A 349 19030 19973 33611 -2214 1604 3793 O
ATOM 1929 N GLY A 350 -55.678-126.496 262.864 1.00186.27 N
ANISOU 1929 N GLY A 350 18310 20306 32159 -1589 2448 4317 N
ATOM 1930 CA GLY A 350 -54.789-126.810 263.970 1.00180.19 C
ANISOU 1930 CA GLY A 350 17824 19586 31054 -1334 2665 4450 C
ATOM 1931 C GLY A 350 -53.323-126.647 263.645 1.00169.44 C
ANISOU 1931 C GLY A 350 17032 18019 29328 -1277 2425 3700 C
ATOM 1932 O GLY A 350 -52.488-127.377 264.191 1.00168.67 O
ANISOU 1932 O GLY A 350 17103 17732 29253 -1262 2380 3760 O
ATOM 1933 N LEU A 351 -52.983-125.703 262.765 1.00159.87 N
ANISOU 1933 N LEU A 351 16076 16858 27811 -1233 2277 3063 N
ATOM 1934 CA LEU A 351 -51.591-125.531 262.366 1.00154.42 C
ANISOU 1934 CA LEU A 351 15831 15996 26844 -1186 2057 2443 C
ATOM 1935 C LEU A 351 -50.730-125.024 263.515 1.00154.17 C
ANISOU 1935 C LEU A 351 16144 16195 26240 -824 2271 2455 C
ATOM 1936 O LEU A 351 -49.548-125.374 263.602 1.00152.03 O
ANISOU 1936 O LEU A 351 16127 15737 25901 -818 2107 2223 O
ATOM 1937 CB LEU A 351 -51.504-124.578 261.173 1.00151.63 C
ANISOU 1937 CB LEU A 351 15595 15698 26318 -1203 1889 1894 C
ATOM 1938 CG LEU A 351 -50.114-124.317 260.586 1.00149.88 C
ANISOU 1938 CG LEU A 351 15735 15353 25861 -1146 1683 1339 C
ATOM 1939 CD1 LEU A 351 -49.467-125.616 260.131 1.00150.86 C
ANISOU 1939 CD1 LEU A 351 15896 15064 26360 -1330 1408 1203 C
ATOM 1940 CD2 LEU A 351 -50.193-123.323 259.437 1.00148.18 C
ANISOU 1940 CD2 LEU A 351 15552 15263 25485 -1135 1579 952 C
ATOM 1941 N PHE A 352 -51.297-124.215 264.408 1.00159.69 N
ANISOU 1941 N PHE A 352 16866 17297 26512 -485 2610 2720 N
ATOM 1942 CA PHE A 352 -50.540-123.602 265.491 1.00164.71 C
ANISOU 1942 CA PHE A 352 17907 18152 26524 -88 2728 2646 C
ATOM 1943 C PHE A 352 -50.662-124.356 266.808 1.00172.82 C
ANISOU 1943 C PHE A 352 18879 19344 27440 119 2986 3241 C
ATOM 1944 O PHE A 352 -50.130-123.891 267.820 1.00172.77 O
ANISOU 1944 O PHE A 352 19231 19568 26845 508 3071 3214 O
ATOM 1945 CB PHE A 352 -50.987-122.151 265.704 1.00167.32 C
ANISOU 1945 CB PHE A 352 18429 18808 26338 279 2899 2472 C
ATOM 1946 CG PHE A 352 -50.711-121.239 264.538 1.00162.99 C
ANISOU 1946 CG PHE A 352 17980 18125 25823 138 2650 1922 C
ATOM 1947 CD1 PHE A 352 -50.006-121.682 263.430 1.00158.96 C
ANISOU 1947 CD1 PHE A 352 17425 17303 25672 -225 2330 1603 C
ATOM 1948 CD2 PHE A 352 -51.156-119.927 264.561 1.00164.06 C
ANISOU 1948 CD2 PHE A 352 18262 18461 25612 427 2755 1755 C
ATOM 1949 CE1 PHE A 352 -49.762-120.839 262.365 1.00156.26 C
ANISOU 1949 CE1 PHE A 352 17138 16908 25324 -304 2150 1194 C
ATOM 1950 CE2 PHE A 352 -50.912-119.079 263.500 1.00161.80 C
ANISOU 1950 CE2 PHE A 352 18029 18054 25393 299 2537 1337 C
ATOM 1951 CZ PHE A 352 -50.215-119.536 262.401 1.00157.77 C
ANISOU 1951 CZ PHE A 352 17431 17290 25225 -70 2248 1088 C
ATOM 1952 N GLU A 353 -51.343-125.501 266.818 1.00183.17 N
ANISOU 1952 N GLU A 353 19751 20533 29314 -126 3072 3795 N
ATOM 1953 CA GLU A 353 -51.619-126.214 268.060 1.00189.95 C
ANISOU 1953 CA GLU A 353 20457 21602 30114 86 3382 4524 C
ATOM 1954 C GLU A 353 -50.332-126.592 268.785 1.00186.52 C
ANISOU 1954 C GLU A 353 20393 21091 29385 222 3251 4416 C
ATOM 1955 O GLU A 353 -49.405-127.146 268.188 1.00182.91 O
ANISOU 1955 O GLU A 353 20035 20213 29251 -74 2898 4070 O
ATOM 1956 CB GLU A 353 -52.440-127.470 267.769 1.00199.21 C
ANISOU 1956 CB GLU A 353 21044 22502 32144 -323 3370 5142 C
ATOM 1957 CG GLU A 353 -52.370-128.518 268.869 1.00209.74 C
ANISOU 1957 CG GLU A 353 22201 23872 33617 -235 3568 5897 C
ATOM 1958 CD GLU A 353 -52.800-129.892 268.397 1.00216.18 C
ANISOU 1958 CD GLU A 353 22521 24164 35454 -763 3339 6350 C
ATOM 1959 OE1 GLU A 353 -53.898-130.343 268.787 1.00223.23 O
ANISOU 1959 OE1 GLU A 353 22861 25191 36765 -820 3592 7202 O
ATOM 1960 OE2 GLU A 353 -52.040-130.520 267.629 1.00213.88 O
ANISOU 1960 OE2 GLU A 353 22387 23309 35570 -1100 2888 5872 O
ATOM 1961 N GLY A 354 -50.282-126.286 270.080 1.00185.52 N
ANISOU 1961 N GLY A 354 20479 21401 28609 723 3536 4723 N
ATOM 1962 CA GLY A 354 -49.184-126.722 270.919 1.00183.10 C
ANISOU 1962 CA GLY A 354 20472 21086 28011 883 3418 4759 C
ATOM 1963 C GLY A 354 -47.900-125.940 270.783 1.00176.84 C
ANISOU 1963 C GLY A 354 20202 20184 26806 951 3030 4007 C
ATOM 1964 O GLY A 354 -46.852-126.415 271.230 1.00178.68 O
ANISOU 1964 O GLY A 354 20620 20305 26967 961 2822 3992 O
ATOM 1965 N PHE A 355 -47.942-124.753 270.185 1.00169.95 N
ANISOU 1965 N PHE A 355 19533 19328 25712 989 2908 3443 N
ATOM 1966 CA PHE A 355 -46.759-123.921 270.005 1.00161.28 C
ANISOU 1966 CA PHE A 355 18860 18093 24328 1011 2502 2800 C
ATOM 1967 C PHE A 355 -46.828-122.735 270.955 1.00161.10 C
ANISOU 1967 C PHE A 355 19299 18414 23498 1551 2525 2615 C
ATOM 1968 O PHE A 355 -47.785-121.953 270.910 1.00164.20 O
ANISOU 1968 O PHE A 355 19704 19018 23667 1788 2760 2582 O
ATOM 1969 CB PHE A 355 -46.635-123.443 268.559 1.00154.67 C
ANISOU 1969 CB PHE A 355 17917 16960 23892 648 2282 2310 C
ATOM 1970 CG PHE A 355 -46.065-124.472 267.629 1.00152.17 C
ANISOU 1970 CG PHE A 355 17355 16256 24206 222 2096 2266 C
ATOM 1971 CD1 PHE A 355 -44.700-124.705 267.591 1.00152.11 C
ANISOU 1971 CD1 PHE A 355 17503 16050 24241 150 1793 2061 C
ATOM 1972 CD2 PHE A 355 -46.890-125.205 266.794 1.00152.16 C
ANISOU 1972 CD2 PHE A 355 16977 16078 24758 -73 2191 2426 C
ATOM 1973 CE1 PHE A 355 -44.168-125.651 266.737 1.00152.30 C
ANISOU 1973 CE1 PHE A 355 17339 15735 24794 -135 1657 2005 C
ATOM 1974 CE2 PHE A 355 -46.364-126.153 265.937 1.00152.20 C
ANISOU 1974 CE2 PHE A 355 16848 15692 25289 -383 1976 2305 C
ATOM 1975 CZ PHE A 355 -45.001-126.376 265.908 1.00152.42 C
ANISOU 1975 CZ PHE A 355 17061 15552 25298 -377 1744 2088 C
ATOM 1976 N ASP A 356 -45.813-122.604 271.812 1.00157.12 N
ANISOU 1976 N ASP A 356 19192 17948 22561 1771 2242 2479 N
ATOM 1977 CA ASP A 356 -45.750-121.460 272.714 1.00156.02 C
ANISOU 1977 CA ASP A 356 19601 18052 21629 2308 2117 2182 C
ATOM 1978 C ASP A 356 -45.521-120.163 271.951 1.00147.91 C
ANISOU 1978 C ASP A 356 18785 16773 20642 2206 1778 1544 C
ATOM 1979 O ASP A 356 -45.957-119.096 272.397 1.00149.50 O
ANISOU 1979 O ASP A 356 19364 17122 20317 2645 1774 1285 O
ATOM 1980 CB ASP A 356 -44.647-121.671 273.751 1.00159.04 C
ANISOU 1980 CB ASP A 356 20357 18485 21588 2515 1768 2164 C
ATOM 1981 CG ASP A 356 -44.794-122.982 274.497 1.00162.60 C
ANISOU 1981 CG ASP A 356 20576 19172 22033 2611 2092 2857 C
ATOM 1982 OD1 ASP A 356 -45.942-123.438 274.681 1.00165.20 O
ANISOU 1982 OD1 ASP A 356 20604 19781 22382 2766 2636 3391 O
ATOM 1983 OD2 ASP A 356 -43.761-123.559 274.899 1.00163.76 O
ANISOU 1983 OD2 ASP A 356 20799 19222 22202 2525 1797 2930 O
ATOM 1984 N LEU A 357 -44.846-120.235 270.805 1.00138.29 N
ANISOU 1984 N LEU A 357 17330 15177 20036 1679 1505 1313 N
ATOM 1985 CA LEU A 357 -44.592-119.077 269.963 1.00130.12 C
ANISOU 1985 CA LEU A 357 16393 13897 19151 1528 1203 827 C
ATOM 1986 C LEU A 357 -44.741-119.490 268.507 1.00122.64 C
ANISOU 1986 C LEU A 357 14961 12756 18881 1043 1310 851 C
ATOM 1987 O LEU A 357 -44.349-120.596 268.126 1.00118.23 O
ANISOU 1987 O LEU A 357 14118 12088 18718 756 1342 1054 O
ATOM 1988 CB LEU A 357 -43.194-118.498 270.212 1.00129.08 C
ANISOU 1988 CB LEU A 357 16577 13512 18954 1467 578 485 C
ATOM 1989 CG LEU A 357 -42.840-117.225 269.445 1.00126.59 C
ANISOU 1989 CG LEU A 357 16349 12905 18846 1311 204 65 C
ATOM 1990 CD1 LEU A 357 -43.818-116.110 269.777 1.00130.46 C
ANISOU 1990 CD1 LEU A 357 17175 13486 18908 1726 301 -170 C
ATOM 1991 CD2 LEU A 357 -41.413-116.799 269.744 1.00129.49 C
ANISOU 1991 CD2 LEU A 357 16927 12999 19275 1189 -461 -139 C
ATOM 1992 N VAL A 358 -45.317-118.603 267.699 1.00122.76 N
ANISOU 1992 N VAL A 358 14914 12728 19003 998 1350 633 N
ATOM 1993 CA VAL A 358 -45.577-118.870 266.289 1.00119.14 C
ANISOU 1993 CA VAL A 358 14045 12145 19077 615 1438 625 C
ATOM 1994 C VAL A 358 -45.092-117.674 265.483 1.00117.97 C
ANISOU 1994 C VAL A 358 13968 11815 19041 511 1140 269 C
ATOM 1995 O VAL A 358 -45.578-116.554 265.674 1.00121.49 O
ANISOU 1995 O VAL A 358 14628 12288 19244 744 1116 96 O
ATOM 1996 CB VAL A 358 -47.067-119.136 266.021 1.00120.20 C
ANISOU 1996 CB VAL A 358 13895 12480 19295 653 1864 881 C
ATOM 1997 CG1 VAL A 358 -47.306-119.336 264.541 1.00117.70 C
ANISOU 1997 CG1 VAL A 358 13223 12028 19471 282 1848 799 C
ATOM 1998 CG2 VAL A 358 -47.535-120.353 266.798 1.00123.13 C
ANISOU 1998 CG2 VAL A 358 14108 13004 19672 715 2148 1357 C
ATOM 1999 N LEU A 359 -44.140-117.908 264.585 1.00116.41 N
ANISOU 1999 N LEU A 359 13578 11433 19219 200 931 201 N
ATOM 2000 CA LEU A 359 -43.546-116.854 263.773 1.00111.97 C
ANISOU 2000 CA LEU A 359 12992 10713 18839 76 656 -4 C
ATOM 2001 C LEU A 359 -44.027-116.997 262.337 1.00107.64 C
ANISOU 2001 C LEU A 359 12088 10213 18596 -121 849 12 C
ATOM 2002 O LEU A 359 -43.742-118.005 261.679 1.00102.99 O
ANISOU 2002 O LEU A 359 11269 9621 18240 -286 928 92 O
ATOM 2003 CB LEU A 359 -42.020-116.903 263.846 1.00115.12 C
ANISOU 2003 CB LEU A 359 13396 10932 19413 -64 275 -1 C
ATOM 2004 CG LEU A 359 -41.375-115.923 264.831 1.00123.36 C
ANISOU 2004 CG LEU A 359 14808 11811 20252 71 -180 -152 C
ATOM 2005 CD1 LEU A 359 -42.094-115.932 266.167 1.00125.00 C
ANISOU 2005 CD1 LEU A 359 15423 12154 19918 438 -94 -216 C
ATOM 2006 CD2 LEU A 359 -39.910-116.253 265.023 1.00128.13 C
ANISOU 2006 CD2 LEU A 359 15335 12273 21074 -93 -552 -40 C
ATOM 2007 N LEU A 360 -44.750-115.989 261.854 1.00113.03 N
ANISOU 2007 N LEU A 360 12758 10932 19255 -63 898 -82 N
ATOM 2008 CA LEU A 360 -45.340-115.996 260.520 1.00113.09 C
ANISOU 2008 CA LEU A 360 12458 11034 19477 -203 1056 -69 C
ATOM 2009 C LEU A 360 -44.581-115.010 259.643 1.00108.41 C
ANISOU 2009 C LEU A 360 11777 10348 19068 -291 835 -121 C
ATOM 2010 O LEU A 360 -44.751-113.794 259.776 1.00110.17 O
ANISOU 2010 O LEU A 360 12127 10479 19255 -196 708 -188 O
ATOM 2011 CB LEU A 360 -46.821-115.635 260.578 1.00117.09 C
ANISOU 2011 CB LEU A 360 12933 11700 19856 -60 1311 -31 C
ATOM 2012 CG LEU A 360 -47.666-116.479 261.527 1.00118.03 C
ANISOU 2012 CG LEU A 360 13069 11956 19821 66 1571 158 C
ATOM 2013 CD1 LEU A 360 -49.143-116.183 261.332 1.00119.93 C
ANISOU 2013 CD1 LEU A 360 13130 12396 20043 177 1848 297 C
ATOM 2014 CD2 LEU A 360 -47.373-117.944 261.304 1.00114.22 C
ANISOU 2014 CD2 LEU A 360 12399 11426 19572 -160 1593 281 C
ATOM 2015 N GLY A 361 -43.757-115.532 258.744 1.00107.88 N
ANISOU 2015 N GLY A 361 11482 10301 19207 -436 800 -54 N
ATOM 2016 CA GLY A 361 -43.006-114.718 257.800 1.00112.64 C
ANISOU 2016 CA GLY A 361 11897 10891 20011 -501 661 33 C
ATOM 2017 C GLY A 361 -43.572-114.873 256.400 1.00114.82 C
ANISOU 2017 C GLY A 361 11920 11394 20313 -509 864 52 C
ATOM 2018 O GLY A 361 -43.959-115.971 255.999 1.00114.59 O
ANISOU 2018 O GLY A 361 11833 11472 20233 -515 1014 -20 O
ATOM 2019 N CYS A 362 -43.624-113.767 255.664 1.00119.39 N
ANISOU 2019 N CYS A 362 12364 12019 20982 -501 822 150 N
ATOM 2020 CA CYS A 362 -44.134-113.804 254.303 1.00115.46 C
ANISOU 2020 CA CYS A 362 11638 11785 20446 -465 985 188 C
ATOM 2021 C CYS A 362 -43.515-112.678 253.496 1.00115.18 C
ANISOU 2021 C CYS A 362 11382 11801 20580 -452 909 451 C
ATOM 2022 O CYS A 362 -43.389-111.550 253.981 1.00117.26 O
ANISOU 2022 O CYS A 362 11701 11839 21015 -493 725 540 O
ATOM 2023 CB CYS A 362 -45.660-113.689 254.263 1.00108.26 C
ANISOU 2023 CB CYS A 362 10762 10961 19411 -437 1112 70 C
ATOM 2024 SG CYS A 362 -46.333-113.708 252.586 1.00101.95 S
ANISOU 2024 SG CYS A 362 9704 10500 18534 -391 1215 99 S
ATOM 2025 N SER A 363 -43.137-112.993 252.262 1.00115.52 N
ANISOU 2025 N SER A 363 11185 12133 20574 -363 1038 590 N
ATOM 2026 CA SER A 363 -42.612-111.988 251.354 1.00119.09 C
ANISOU 2026 CA SER A 363 11348 12725 21175 -314 1036 958 C
ATOM 2027 C SER A 363 -43.755-111.243 250.678 1.00118.74 C
ANISOU 2027 C SER A 363 11246 12828 21043 -264 1107 965 C
ATOM 2028 O SER A 363 -44.810-111.819 250.392 1.00119.10 O
ANISOU 2028 O SER A 363 11377 13028 20846 -218 1208 715 O
ATOM 2029 CB SER A 363 -41.715-112.635 250.301 1.00117.27 C
ANISOU 2029 CB SER A 363 10881 12835 20840 -127 1206 1160 C
ATOM 2030 OG SER A 363 -41.419-111.717 249.265 1.00118.19 O
ANISOU 2030 OG SER A 363 10672 13203 21032 -20 1285 1588 O
ATOM 2031 N THR A 364 -43.542-109.954 250.429 1.00113.68 N
ANISOU 2031 N THR A 364 10431 12106 20657 -290 1015 1292 N
ATOM 2032 CA THR A 364 -44.539-109.118 249.779 1.00108.38 C
ANISOU 2032 CA THR A 364 9670 11558 19952 -225 1073 1377 C
ATOM 2033 C THR A 364 -44.246-109.057 248.286 1.00103.19 C
ANISOU 2033 C THR A 364 8680 11364 19163 -53 1248 1721 C
ATOM 2034 O THR A 364 -43.111-108.789 247.879 1.00 96.42 O
ANISOU 2034 O THR A 364 7559 10590 18486 -17 1264 2138 O
ATOM 2035 CB THR A 364 -44.548-107.712 250.378 1.00108.59 C
ANISOU 2035 CB THR A 364 9733 11173 20354 -315 846 1533 C
ATOM 2036 OG1 THR A 364 -44.485-107.805 251.805 1.00110.23 O
ANISOU 2036 OG1 THR A 364 10292 10973 20618 -397 649 1224 O
ATOM 2037 CG2 THR A 364 -45.823-106.981 249.984 1.00 98.78 C
ANISOU 2037 CG2 THR A 364 8480 10001 19051 -217 922 1524 C
ATOM 2038 N TRP A 365 -45.271-109.322 247.475 1.00108.95 N
ANISOU 2038 N TRP A 365 9403 12424 19569 78 1370 1583 N
ATOM 2039 CA TRP A 365 -45.137-109.371 246.021 1.00124.87 C
ANISOU 2039 CA TRP A 365 11180 14959 21304 329 1529 1837 C
ATOM 2040 C TRP A 365 -46.225-108.511 245.377 1.00135.83 C
ANISOU 2040 C TRP A 365 12452 16514 22643 384 1533 1972 C
ATOM 2041 O TRP A 365 -47.067-108.987 244.617 1.00134.69 O
ANISOU 2041 O TRP A 365 12336 16706 22133 517 1558 1785 O
ATOM 2042 CB TRP A 365 -45.194-110.813 245.520 1.00129.47 C
ANISOU 2042 CB TRP A 365 11924 15827 21443 503 1596 1465 C
ATOM 2043 CG TRP A 365 -44.011-111.623 245.945 1.00133.88 C
ANISOU 2043 CG TRP A 365 12540 16287 22041 533 1636 1427 C
ATOM 2044 CD1 TRP A 365 -43.880-112.346 247.095 1.00136.22 C
ANISOU 2044 CD1 TRP A 365 13069 16210 22478 342 1535 1115 C
ATOM 2045 CD2 TRP A 365 -42.783-111.781 245.228 1.00135.25 C
ANISOU 2045 CD2 TRP A 365 12500 16777 22113 808 1815 1780 C
ATOM 2046 NE1 TRP A 365 -42.646-112.950 247.135 1.00137.32 N
ANISOU 2046 NE1 TRP A 365 13160 16383 22632 459 1610 1225 N
ATOM 2047 CE2 TRP A 365 -41.953-112.618 246.000 1.00137.66 C
ANISOU 2047 CE2 TRP A 365 12919 16852 22533 756 1796 1638 C
ATOM 2048 CE3 TRP A 365 -42.305-111.299 244.006 1.00136.63 C
ANISOU 2048 CE3 TRP A 365 12367 17450 22096 1137 2023 2264 C
ATOM 2049 CZ2 TRP A 365 -40.673-112.980 245.591 1.00139.31 C
ANISOU 2049 CZ2 TRP A 365 12932 17300 22700 1023 1977 1955 C
ATOM 2050 CZ3 TRP A 365 -41.034-111.663 243.602 1.00140.89 C
ANISOU 2050 CZ3 TRP A 365 12707 18261 22563 1428 2235 2604 C
ATOM 2051 CH2 TRP A 365 -40.233-112.495 244.391 1.00141.72 C
ANISOU 2051 CH2 TRP A 365 12919 18114 22814 1369 2211 2443 C
ATOM 2052 N GLY A 366 -46.191-107.216 245.681 1.00148.61 N
ANISOU 2052 N GLY A 366 13940 17861 24666 283 1459 2307 N
ATOM 2053 CA GLY A 366 -47.189-106.297 245.177 1.00158.38 C
ANISOU 2053 CA GLY A 366 15055 19189 25931 345 1461 2482 C
ATOM 2054 C GLY A 366 -46.769-105.538 243.936 1.00169.96 C
ANISOU 2054 C GLY A 366 16145 21030 27402 529 1573 3097 C
ATOM 2055 O GLY A 366 -46.153-104.472 244.031 1.00172.86 O
ANISOU 2055 O GLY A 366 16298 21142 28238 452 1509 3579 O
ATOM 2056 N ASP A 367 -47.097-106.079 242.761 1.00177.52 N
ANISOU 2056 N ASP A 367 17020 22585 27844 787 1708 3106 N
ATOM 2057 CA ASP A 367 -46.805-105.384 241.511 1.00184.85 C
ANISOU 2057 CA ASP A 367 17589 23985 28662 1045 1859 3733 C
ATOM 2058 C ASP A 367 -47.674-104.140 241.368 1.00186.58 C
ANISOU 2058 C ASP A 367 17649 24079 29165 999 1791 4035 C
ATOM 2059 O ASP A 367 -47.166-103.016 241.274 1.00190.10 O
ANISOU 2059 O ASP A 367 17808 24347 30074 960 1792 4638 O
ATOM 2060 CB ASP A 367 -47.010-106.330 240.326 1.00187.39 C
ANISOU 2060 CB ASP A 367 17961 24993 28244 1410 1972 3567 C
ATOM 2061 CG ASP A 367 -46.815-105.642 238.989 1.00192.84 C
ANISOU 2061 CG ASP A 367 18301 26284 28685 1767 2159 4229 C
ATOM 2062 OD1 ASP A 367 -45.948-104.748 238.898 1.00194.53 O
ANISOU 2062 OD1 ASP A 367 18155 26455 29303 1765 2291 4934 O
ATOM 2063 OD2 ASP A 367 -47.531-105.997 238.029 1.00196.56 O
ANISOU 2063 OD2 ASP A 367 18842 27269 28571 2050 2143 4078 O
ATOM 2064 N ASP A 368 -48.994-104.325 241.347 1.00178.84 N
ANISOU 2064 N ASP A 368 16820 23165 27967 1002 1710 3664 N
ATOM 2065 CA ASP A 368 -49.944-103.218 241.310 1.00174.56 C
ANISOU 2065 CA ASP A 368 16150 22483 27692 990 1653 3898 C
ATOM 2066 C ASP A 368 -50.460-102.890 242.708 1.00169.65 C
ANISOU 2066 C ASP A 368 15773 21198 27487 768 1525 3556 C
ATOM 2067 O ASP A 368 -50.314-101.760 243.180 1.00169.98 O
ANISOU 2067 O ASP A 368 15771 20779 28032 710 1448 3821 O
ATOM 2068 CB ASP A 368 -51.104-103.558 240.363 1.00176.73 C
ANISOU 2068 CB ASP A 368 16376 23298 27477 1175 1636 3791 C
ATOM 2069 CG ASP A 368 -51.932-102.341 239.980 1.00178.61 C
ANISOU 2069 CG ASP A 368 16371 23551 27942 1256 1626 4221 C
ATOM 2070 OD1 ASP A 368 -52.238-101.511 240.861 1.00178.11 O
ANISOU 2070 OD1 ASP A 368 16347 22935 28392 1126 1578 4253 O
ATOM 2071 OD2 ASP A 368 -52.279-102.217 238.787 1.00181.72 O
ANISOU 2071 OD2 ASP A 368 16557 24517 27970 1495 1654 4519 O
ATOM 2072 N SER A 369 -51.064-103.866 243.377 1.00166.33 N
ANISOU 2072 N SER A 369 15618 20715 26864 679 1489 2987 N
ATOM 2073 CA SER A 369 -51.536-103.727 244.746 1.00161.49 C
ANISOU 2073 CA SER A 369 15263 19579 26518 558 1429 2660 C
ATOM 2074 C SER A 369 -50.835-104.758 245.621 1.00157.24 C
ANISOU 2074 C SER A 369 14989 18844 25912 409 1402 2268 C
ATOM 2075 O SER A 369 -50.165-105.667 245.129 1.00155.51 O
ANISOU 2075 O SER A 369 14753 18897 25435 404 1431 2200 O
ATOM 2076 CB SER A 369 -53.059-103.894 244.826 1.00159.07 C
ANISOU 2076 CB SER A 369 14947 19411 26083 616 1454 2477 C
ATOM 2077 OG SER A 369 -53.463-105.141 244.290 1.00155.57 O
ANISOU 2077 OG SER A 369 14484 19373 25251 578 1423 2227 O
ATOM 2078 N ILE A 370 -50.999-104.606 246.937 1.00155.91 N
ANISOU 2078 N ILE A 370 15085 18210 25944 343 1352 2012 N
ATOM 2079 CA ILE A 370 -50.316-105.478 247.889 1.00150.12 C
ANISOU 2079 CA ILE A 370 14608 17261 25170 215 1311 1687 C
ATOM 2080 C ILE A 370 -50.724-106.922 247.640 1.00147.17 C
ANISOU 2080 C ILE A 370 14251 17219 24447 170 1380 1405 C
ATOM 2081 O ILE A 370 -51.914-107.261 247.659 1.00147.22 O
ANISOU 2081 O ILE A 370 14227 17364 24346 187 1421 1282 O
ATOM 2082 CB ILE A 370 -50.626-105.055 249.328 1.00147.29 C
ANISOU 2082 CB ILE A 370 14564 16425 24973 244 1251 1453 C
ATOM 2083 CG1 ILE A 370 -50.136-103.629 249.588 1.00150.20 C
ANISOU 2083 CG1 ILE A 370 14988 16343 25739 288 1062 1662 C
ATOM 2084 CG2 ILE A 370 -49.998-106.025 250.315 1.00143.51 C
ANISOU 2084 CG2 ILE A 370 14343 15787 24396 134 1212 1145 C
ATOM 2085 CD1 ILE A 370 -50.362-103.161 251.010 1.00151.02 C
ANISOU 2085 CD1 ILE A 370 15504 15950 25926 409 942 1355 C
ATOM 2086 N GLU A 371 -49.737-107.782 247.401 1.00145.14 N
ANISOU 2086 N GLU A 371 14023 17062 24060 117 1368 1331 N
ATOM 2087 CA GLU A 371 -49.980-109.201 247.191 1.00144.60 C
ANISOU 2087 CA GLU A 371 14028 17199 23715 82 1365 1023 C
ATOM 2088 C GLU A 371 -48.914-110.004 247.922 1.00142.25 C
ANISOU 2088 C GLU A 371 13916 16685 23448 -2 1350 852 C
ATOM 2089 O GLU A 371 -47.741-109.618 247.944 1.00139.79 O
ANISOU 2089 O GLU A 371 13564 16286 23263 11 1347 1053 O
ATOM 2090 CB GLU A 371 -49.984-109.558 245.700 1.00149.12 C
ANISOU 2090 CB GLU A 371 14443 18250 23967 234 1355 1090 C
ATOM 2091 CG GLU A 371 -51.132-108.945 244.911 1.00154.31 C
ANISOU 2091 CG GLU A 371 14909 19179 24544 317 1324 1244 C
ATOM 2092 CD GLU A 371 -51.036-109.230 243.423 1.00161.57 C
ANISOU 2092 CD GLU A 371 15719 20613 25057 536 1281 1313 C
ATOM 2093 OE1 GLU A 371 -51.600-108.447 242.629 1.00165.77 O
ANISOU 2093 OE1 GLU A 371 16047 21423 25513 660 1278 1592 O
ATOM 2094 OE2 GLU A 371 -50.394-110.232 243.043 1.00162.95 O
ANISOU 2094 OE2 GLU A 371 16034 20925 24955 633 1248 1087 O
ATOM 2095 N LEU A 372 -49.329-111.117 248.522 1.00146.37 N
ANISOU 2095 N LEU A 372 14596 17115 23903 -99 1326 544 N
ATOM 2096 CA LEU A 372 -48.431-111.955 249.298 1.00148.72 C
ANISOU 2096 CA LEU A 372 15073 17199 24236 -171 1311 389 C
ATOM 2097 C LEU A 372 -47.884-113.084 248.427 1.00145.52 C
ANISOU 2097 C LEU A 372 14675 17002 23616 -88 1288 247 C
ATOM 2098 O LEU A 372 -48.109-113.143 247.214 1.00142.80 O
ANISOU 2098 O LEU A 372 14229 16984 23045 60 1271 256 O
ATOM 2099 CB LEU A 372 -49.146-112.512 250.533 1.00153.68 C
ANISOU 2099 CB LEU A 372 15863 17590 24936 -287 1319 209 C
ATOM 2100 CG LEU A 372 -49.267-111.612 251.776 1.00159.12 C
ANISOU 2100 CG LEU A 372 16696 18010 25752 -264 1350 267 C
ATOM 2101 CD1 LEU A 372 -50.172-110.415 251.520 1.00164.96 C
ANISOU 2101 CD1 LEU A 372 17329 18807 26542 -156 1395 415 C
ATOM 2102 CD2 LEU A 372 -49.746-112.410 252.980 1.00157.87 C
ANISOU 2102 CD2 LEU A 372 16698 17715 25571 -301 1413 141 C
ATOM 2103 N GLN A 373 -47.131-113.983 249.052 1.00145.50 N
ANISOU 2103 N GLN A 373 14822 16812 23651 -131 1277 106 N
ATOM 2104 CA GLN A 373 -46.592-115.123 248.328 1.00147.40 C
ANISOU 2104 CA GLN A 373 15128 17184 23693 11 1253 -76 C
ATOM 2105 C GLN A 373 -47.707-116.099 247.980 1.00150.01 C
ANISOU 2105 C GLN A 373 15549 17513 23935 -46 1090 -394 C
ATOM 2106 O GLN A 373 -48.552-116.418 248.822 1.00149.53 O
ANISOU 2106 O GLN A 373 15518 17224 24074 -264 1031 -461 O
ATOM 2107 CB GLN A 373 -45.514-115.815 249.155 1.00144.34 C
ANISOU 2107 CB GLN A 373 14861 16559 23423 -13 1274 -110 C
ATOM 2108 CG GLN A 373 -45.046-117.135 248.569 1.00143.97 C
ANISOU 2108 CG GLN A 373 14940 16560 23200 171 1245 -355 C
ATOM 2109 CD GLN A 373 -44.554-117.005 247.139 1.00148.38 C
ANISOU 2109 CD GLN A 373 15416 17535 23428 531 1329 -290 C
ATOM 2110 OE1 GLN A 373 -44.079-115.945 246.722 1.00152.58 O
ANISOU 2110 OE1 GLN A 373 15721 18311 23942 632 1467 84 O
ATOM 2111 NE2 GLN A 373 -44.659-118.090 246.379 1.00150.12 N
ANISOU 2111 NE2 GLN A 373 15828 17829 23381 760 1230 -637 N
ATOM 2112 N ASP A 374 -47.701-116.571 246.729 1.00155.41 N
ANISOU 2112 N ASP A 374 16268 18457 24322 175 995 -561 N
ATOM 2113 CA ASP A 374 -48.745-117.476 246.257 1.00159.99 C
ANISOU 2113 CA ASP A 374 16946 18995 24850 111 710 -891 C
ATOM 2114 C ASP A 374 -48.836-118.733 247.110 1.00155.23 C
ANISOU 2114 C ASP A 374 16502 17967 24513 -89 569 -1117 C
ATOM 2115 O ASP A 374 -49.907-119.342 247.204 1.00156.53 O
ANISOU 2115 O ASP A 374 16650 17952 24872 -307 316 -1251 O
ATOM 2116 CB ASP A 374 -48.490-117.848 244.794 1.00170.17 C
ANISOU 2116 CB ASP A 374 18355 20615 25688 477 582 -1109 C
ATOM 2117 CG ASP A 374 -48.483-116.638 243.877 1.00176.34 C
ANISOU 2117 CG ASP A 374 18939 21871 26191 697 728 -805 C
ATOM 2118 OD1 ASP A 374 -49.245-115.685 244.143 1.00178.54 O
ANISOU 2118 OD1 ASP A 374 19005 22174 26659 498 765 -554 O
ATOM 2119 OD2 ASP A 374 -47.718-116.640 242.891 1.00178.80 O
ANISOU 2119 OD2 ASP A 374 19298 22546 26091 1109 828 -778 O
ATOM 2120 N ASP A 375 -47.729-119.138 247.731 1.00146.45 N
ANISOU 2120 N ASP A 375 15500 16684 23459 -27 709 -1102 N
ATOM 2121 CA ASP A 375 -47.765-120.270 248.646 1.00137.51 C
ANISOU 2121 CA ASP A 375 14495 15141 22613 -213 607 -1231 C
ATOM 2122 C ASP A 375 -48.381-119.896 249.987 1.00139.84 C
ANISOU 2122 C ASP A 375 14665 15261 23208 -507 717 -973 C
ATOM 2123 O ASP A 375 -49.005-120.742 250.637 1.00144.43 O
ANISOU 2123 O ASP A 375 15247 15566 24063 -716 604 -986 O
ATOM 2124 CB ASP A 375 -46.354-120.818 248.854 1.00126.79 C
ANISOU 2124 CB ASP A 375 13280 13691 21203 -8 726 -1263 C
ATOM 2125 CG ASP A 375 -45.638-121.081 247.544 1.00121.79 C
ANISOU 2125 CG ASP A 375 12764 13321 20189 417 719 -1455 C
ATOM 2126 OD1 ASP A 375 -46.314-121.447 246.560 1.00120.07 O
ANISOU 2126 OD1 ASP A 375 12662 13189 19771 532 477 -1752 O
ATOM 2127 OD2 ASP A 375 -44.400-120.915 247.498 1.00120.84 O
ANISOU 2127 OD2 ASP A 375 12613 13345 19956 668 944 -1287 O
ATOM 2128 N PHE A 376 -48.219-118.641 250.413 1.00139.12 N
ANISOU 2128 N PHE A 376 14469 15317 23072 -492 926 -717 N
ATOM 2129 CA PHE A 376 -48.740-118.196 251.701 1.00135.40 C
ANISOU 2129 CA PHE A 376 13955 14719 22771 -642 1049 -511 C
ATOM 2130 C PHE A 376 -50.224-117.874 251.657 1.00136.50 C
ANISOU 2130 C PHE A 376 13913 14947 23005 -753 1032 -410 C
ATOM 2131 O PHE A 376 -50.858-117.787 252.716 1.00138.78 O
ANISOU 2131 O PHE A 376 14153 15154 23424 -826 1155 -226 O
ATOM 2132 CB PHE A 376 -47.958-116.970 252.182 1.00129.62 C
ANISOU 2132 CB PHE A 376 13248 14032 21970 -546 1191 -338 C
ATOM 2133 CG PHE A 376 -47.879-116.848 253.675 1.00126.66 C
ANISOU 2133 CG PHE A 376 12994 13460 21671 -592 1268 -236 C
ATOM 2134 CD1 PHE A 376 -48.887-116.223 254.391 1.00123.25 C
ANISOU 2134 CD1 PHE A 376 12544 13042 21242 -583 1370 -121 C
ATOM 2135 CD2 PHE A 376 -46.790-117.354 254.360 1.00126.77 C
ANISOU 2135 CD2 PHE A 376 13146 13309 21710 -586 1244 -242 C
ATOM 2136 CE1 PHE A 376 -48.811-116.115 255.766 1.00121.50 C
ANISOU 2136 CE1 PHE A 376 12492 12694 20980 -523 1450 -48 C
ATOM 2137 CE2 PHE A 376 -46.709-117.247 255.734 1.00124.45 C
ANISOU 2137 CE2 PHE A 376 13002 12874 21410 -583 1280 -160 C
ATOM 2138 CZ PHE A 376 -47.720-116.625 256.438 1.00122.66 C
ANISOU 2138 CZ PHE A 376 12806 12683 21117 -530 1384 -79 C
ATOM 2139 N ILE A 377 -50.783-117.699 250.465 1.00136.65 N
ANISOU 2139 N ILE A 377 13819 15167 22935 -726 891 -490 N
ATOM 2140 CA ILE A 377 -52.182-117.303 250.312 1.00139.14 C
ANISOU 2140 CA ILE A 377 13899 15606 23361 -822 852 -342 C
ATOM 2141 C ILE A 377 -53.153-118.377 250.808 1.00140.87 C
ANISOU 2141 C ILE A 377 13987 15626 23910 -1062 711 -279 C
ATOM 2142 O ILE A 377 -54.101-118.041 251.536 1.00143.72 O
ANISOU 2142 O ILE A 377 14137 16027 24444 -1123 865 23 O
ATOM 2143 CB ILE A 377 -52.494-116.924 248.852 1.00143.45 C
ANISOU 2143 CB ILE A 377 14357 16437 23710 -726 673 -436 C
ATOM 2144 CG1 ILE A 377 -51.627-115.751 248.385 1.00143.30 C
ANISOU 2144 CG1 ILE A 377 14369 16640 23440 -494 853 -339 C
ATOM 2145 CG2 ILE A 377 -53.964-116.590 248.678 1.00145.85 C
ANISOU 2145 CG2 ILE A 377 14374 16869 24173 -842 588 -252 C
ATOM 2146 CD1 ILE A 377 -51.847-114.497 249.169 1.00145.12 C
ANISOU 2146 CD1 ILE A 377 14516 16852 23770 -469 1082 -66 C
ATOM 2147 N PRO A 378 -52.998-119.661 250.436 1.00139.81 N
ANISOU 2147 N PRO A 378 13948 15268 23907 -1181 416 -511 N
ATOM 2148 CA PRO A 378 -53.945-120.670 250.948 1.00139.99 C
ANISOU 2148 CA PRO A 378 13782 15033 24375 -1465 236 -354 C
ATOM 2149 C PRO A 378 -53.998-120.725 252.464 1.00139.56 C
ANISOU 2149 C PRO A 378 13656 14881 24491 -1503 570 6 C
ATOM 2150 O PRO A 378 -55.091-120.823 253.036 1.00144.41 O
ANISOU 2150 O PRO A 378 13957 15512 25400 -1642 638 386 O
ATOM 2151 CB PRO A 378 -53.417-121.976 250.341 1.00141.89 C
ANISOU 2151 CB PRO A 378 14253 14955 24702 -1518 -152 -735 C
ATOM 2152 CG PRO A 378 -52.721-121.543 249.109 1.00141.98 C
ANISOU 2152 CG PRO A 378 14485 15207 24252 -1236 -235 -1091 C
ATOM 2153 CD PRO A 378 -52.060-120.253 249.460 1.00140.05 C
ANISOU 2153 CD PRO A 378 14239 15259 23714 -1033 203 -900 C
ATOM 2154 N LEU A 379 -52.848-120.637 253.138 1.00136.06 N
ANISOU 2154 N LEU A 379 13473 14376 23847 -1350 783 -60 N
ATOM 2155 CA LEU A 379 -52.856-120.612 254.596 1.00136.36 C
ANISOU 2155 CA LEU A 379 13502 14378 23931 -1312 1085 259 C
ATOM 2156 C LEU A 379 -53.462-119.321 255.125 1.00141.43 C
ANISOU 2156 C LEU A 379 14049 15302 24387 -1127 1390 497 C
ATOM 2157 O LEU A 379 -54.095-119.322 256.187 1.00147.00 O
ANISOU 2157 O LEU A 379 14632 16068 25153 -1065 1635 850 O
ATOM 2158 CB LEU A 379 -51.438-120.790 255.136 1.00131.47 C
ANISOU 2158 CB LEU A 379 13195 13629 23127 -1187 1160 110 C
ATOM 2159 N PHE A 380 -53.287-118.217 254.395 1.00141.73 N
ANISOU 2159 N PHE A 380 14142 15516 24193 -992 1390 338 N
ATOM 2160 CA PHE A 380 -53.858-116.941 254.810 1.00145.23 C
ANISOU 2160 CA PHE A 380 14533 16162 24486 -779 1636 520 C
ATOM 2161 C PHE A 380 -55.381-116.990 254.800 1.00147.66 C
ANISOU 2161 C PHE A 380 14454 16629 25020 -834 1709 856 C
ATOM 2162 O PHE A 380 -56.034-116.519 255.738 1.00148.68 O
ANISOU 2162 O PHE A 380 14501 16887 25102 -628 2015 1156 O
ATOM 2163 CB PHE A 380 -53.339-115.830 253.895 1.00148.42 C
ANISOU 2163 CB PHE A 380 15030 16668 24696 -663 1568 330 C
ATOM 2164 CG PHE A 380 -54.130-114.554 253.965 1.00151.72 C
ANISOU 2164 CG PHE A 380 15345 17254 25048 -466 1737 500 C
ATOM 2165 CD1 PHE A 380 -53.884-113.623 254.962 1.00150.59 C
ANISOU 2165 CD1 PHE A 380 15428 17047 24741 -204 1924 530 C
ATOM 2166 CD2 PHE A 380 -55.099-114.271 253.018 1.00155.87 C
ANISOU 2166 CD2 PHE A 380 15576 17978 25668 -510 1665 607 C
ATOM 2167 CE1 PHE A 380 -54.603-112.439 255.020 1.00153.14 C
ANISOU 2167 CE1 PHE A 380 15704 17472 25012 39 2066 652 C
ATOM 2168 CE2 PHE A 380 -55.824-113.092 253.072 1.00158.05 C
ANISOU 2168 CE2 PHE A 380 15746 18398 25908 -293 1833 789 C
ATOM 2169 CZ PHE A 380 -55.574-112.174 254.075 1.00156.50 C
ANISOU 2169 CZ PHE A 380 15796 18104 25562 -3 2048 804 C
ATOM 2170 N ASP A 381 -55.937-117.523 253.731 1.00151.50 N
ANISOU 2170 N ASP A 381 14696 17123 25746 -1075 1411 824 N
ATOM 2171 CA ASP A 381 -57.375-117.600 253.593 1.00157.49 C
ANISOU 2171 CA ASP A 381 15008 18035 26795 -1169 1412 1200 C
ATOM 2172 C ASP A 381 -58.060-118.477 254.621 1.00164.45 C
ANISOU 2172 C ASP A 381 15642 18834 28008 -1279 1553 1634 C
ATOM 2173 O ASP A 381 -59.155-118.179 255.075 1.00167.12 O
ANISOU 2173 O ASP A 381 15626 19386 28484 -1173 1816 2115 O
ATOM 2174 CB ASP A 381 -57.740-118.037 252.184 1.00156.81 C
ANISOU 2174 CB ASP A 381 14748 17937 26896 -1425 939 1031 C
ATOM 2175 CG ASP A 381 -57.535-116.942 251.174 1.00152.32 C
ANISOU 2175 CG ASP A 381 14298 17581 25994 -1258 869 781 C
ATOM 2176 OD1 ASP A 381 -57.138-115.830 251.570 1.00148.89 O
ANISOU 2176 OD1 ASP A 381 13990 17276 25305 -988 1184 825 O
ATOM 2177 OD2 ASP A 381 -57.776-117.188 249.980 1.00153.47 O
ANISOU 2177 OD2 ASP A 381 14427 17754 26132 -1377 474 550 O
ATOM 2178 N SER A 382 -57.409-119.567 254.978 1.00170.53 N
ANISOU 2178 N SER A 382 16559 19312 28922 -1456 1409 1534 N
ATOM 2179 CA SER A 382 -57.972-120.532 255.901 1.00176.05 C
ANISOU 2179 CA SER A 382 16994 19899 29997 -1592 1514 2012 C
ATOM 2180 C SER A 382 -57.492-120.370 257.326 1.00174.02 C
ANISOU 2180 C SER A 382 16958 19746 29416 -1266 1976 2197 C
ATOM 2181 O SER A 382 -57.427-121.330 258.080 1.00179.25 O
ANISOU 2181 O SER A 382 17619 20238 30251 -1352 2013 2407 O
ATOM 2182 CB SER A 382 -57.693-121.943 255.397 1.00179.83 C
ANISOU 2182 CB SER A 382 17510 19948 30870 -1956 1054 1826 C
ATOM 2183 OG SER A 382 -56.302-122.190 255.382 1.00178.06 O
ANISOU 2183 OG SER A 382 17783 19561 30312 -1854 972 1299 O
ATOM 2184 N LEU A 383 -57.142-119.154 257.698 1.00164.72 N
ANISOU 2184 N LEU A 383 15993 18823 27768 -872 2290 2118 N
ATOM 2185 CA LEU A 383 -56.625-118.929 259.032 1.00157.69 C
ANISOU 2185 CA LEU A 383 15426 18012 26478 -511 2630 2174 C
ATOM 2186 C LEU A 383 -57.544-119.288 260.198 1.00157.06 C
ANISOU 2186 C LEU A 383 15032 18177 26466 -306 3036 2839 C
ATOM 2187 O LEU A 383 -57.092-119.863 261.180 1.00153.58 O
ANISOU 2187 O LEU A 383 14798 17782 25774 -73 3265 2988 O
ATOM 2188 CB LEU A 383 -56.174-117.480 259.154 1.00154.91 C
ANISOU 2188 CB LEU A 383 15439 17771 25649 -149 2737 1842 C
ATOM 2189 CG LEU A 383 -55.002-117.023 258.291 1.00151.47 C
ANISOU 2189 CG LEU A 383 15520 17239 24793 107 2786 1585 C
ATOM 2190 CD1 LEU A 383 -54.728-115.528 258.383 1.00149.27 C
ANISOU 2190 CD1 LEU A 383 15386 16681 24651 -200 2503 1359 C
ATOM 2191 CD2 LEU A 383 -53.763-117.838 258.623 1.00146.52 C
ANISOU 2191 CD2 LEU A 383 15227 16585 23858 351 2722 1219 C
ATOM 2192 N GLU A 384 -58.823-118.966 260.103 1.00161.40 N
ANISOU 2192 N GLU A 384 15052 18924 27348 -362 3136 3299 N
ATOM 2193 CA GLU A 384 -59.733-119.284 261.178 1.00170.02 C
ANISOU 2193 CA GLU A 384 15722 20294 28585 -170 3555 4077 C
ATOM 2194 C GLU A 384 -59.497-120.726 261.529 1.00175.83 C
ANISOU 2194 C GLU A 384 16231 20787 29790 -535 3415 4431 C
ATOM 2195 O GLU A 384 -59.532-121.113 262.691 1.00177.94 O
ANISOU 2195 O GLU A 384 16344 21258 30007 -296 3805 5017 O
ATOM 2196 CB GLU A 384 -61.172-119.095 260.721 1.00175.43 C
ANISOU 2196 CB GLU A 384 15792 21237 29624 -191 3654 4566 C
ATOM 2197 CG GLU A 384 -61.559-117.655 260.432 1.00174.35 C
ANISOU 2197 CG GLU A 384 15830 21367 29050 258 3874 4345 C
ATOM 2198 CD GLU A 384 -62.972-117.538 259.914 1.00170.28 C
ANISOU 2198 CD GLU A 384 15597 20613 28487 14 3419 3648 C
ATOM 2199 OE1 GLU A 384 -63.560-118.598 259.609 1.00167.95 O
ANISOU 2199 OE1 GLU A 384 15316 20005 28490 -477 2945 3358 O
ATOM 2200 OE2 GLU A 384 -63.482-116.410 259.806 1.00170.24 O
ANISOU 2200 OE2 GLU A 384 15807 20734 28142 354 3540 3410 O
ATOM 2201 N GLU A 385 -59.243-121.521 260.506 1.00179.63 N
ANISOU 2201 N GLU A 385 16708 20831 30712 -1067 2862 4096 N
ATOM 2202 CA GLU A 385 -58.974-122.932 260.686 1.00187.37 C
ANISOU 2202 CA GLU A 385 17583 21461 32149 -1401 2657 4319 C
ATOM 2203 C GLU A 385 -57.735-123.037 261.558 1.00188.32 C
ANISOU 2203 C GLU A 385 18231 21527 31796 -1151 2821 4079 C
ATOM 2204 O GLU A 385 -57.615-123.923 262.390 1.00192.81 O
ANISOU 2204 O GLU A 385 18679 22022 32559 -1179 2944 4537 O
ATOM 2205 CB GLU A 385 -58.739-123.605 259.341 1.00187.88 C
ANISOU 2205 CB GLU A 385 17626 21036 32723 -1934 1981 3894 C
ATOM 2206 N THR A 386 -56.810-122.112 261.366 1.00184.85 N
ANISOU 2206 N THR A 386 18338 21121 30776 -915 2799 3425 N
ATOM 2207 CA THR A 386 -55.588-122.084 262.141 1.00182.02 C
ANISOU 2207 CA THR A 386 18463 20759 29938 -642 2931 3226 C
ATOM 2208 C THR A 386 -56.082-121.811 263.530 1.00189.26 C
ANISOU 2208 C THR A 386 19366 22098 30448 -141 3460 3742 C
ATOM 2209 O THR A 386 -57.183-121.289 263.671 1.00194.22 O
ANISOU 2209 O THR A 386 19737 23069 30988 120 3775 4081 O
ATOM 2210 CB THR A 386 -54.736-120.900 261.719 1.00172.40 C
ANISOU 2210 CB THR A 386 17746 19494 28266 -508 2763 2508 C
ATOM 2211 OG1 THR A 386 -54.403-121.044 260.337 1.00167.68 O
ANISOU 2211 OG1 THR A 386 17090 18657 27963 -857 2368 2114 O
ATOM 2212 CG2 THR A 386 -53.477-120.832 262.550 1.00169.81 C
ANISOU 2212 CG2 THR A 386 17856 19030 27632 -393 2702 2265 C
ATOM 2213 N GLY A 387 -55.316-122.159 264.560 1.00190.34 N
ANISOU 2213 N GLY A 387 19781 22235 30304 46 3565 3823 N
ATOM 2214 CA GLY A 387 -55.821-121.946 265.903 1.00200.05 C
ANISOU 2214 CA GLY A 387 21095 23902 31011 615 4052 4270 C
ATOM 2215 C GLY A 387 -56.145-120.478 266.047 1.00205.64 C
ANISOU 2215 C GLY A 387 22102 24933 31099 1148 4277 4005 C
ATOM 2216 O GLY A 387 -57.235-120.120 266.481 1.00213.16 O
ANISOU 2216 O GLY A 387 22720 26224 32046 1410 4636 4436 O
ATOM 2217 N ALA A 388 -55.231-119.614 265.646 1.00203.99 N
ANISOU 2217 N ALA A 388 22499 24593 30416 1318 4046 3329 N
ATOM 2218 CA ALA A 388 -55.526-118.193 265.658 1.00203.77 C
ANISOU 2218 CA ALA A 388 22818 24679 29924 1724 4082 2921 C
ATOM 2219 C ALA A 388 -56.118-117.642 266.962 1.00209.61 C
ANISOU 2219 C ALA A 388 23572 25910 30161 2433 4617 3341 C
ATOM 2220 O ALA A 388 -57.096-116.884 266.909 1.00211.25 O
ANISOU 2220 O ALA A 388 23583 26315 30368 2662 4847 3462 O
ATOM 2221 CB ALA A 388 -56.435-117.859 264.480 1.00200.78 C
ANISOU 2221 CB ALA A 388 22182 24140 29966 1372 3881 2686 C
ATOM 2222 N GLN A 389 -55.663-118.101 268.119 1.00206.35 N
ANISOU 2222 N GLN A 389 23398 25726 29278 2839 4833 3588 N
ATOM 2223 CA GLN A 389 -56.285-117.585 269.331 1.00206.06 C
ANISOU 2223 CA GLN A 389 23457 26226 28610 3657 5380 3986 C
ATOM 2224 C GLN A 389 -55.437-117.553 270.576 1.00202.71 C
ANISOU 2224 C GLN A 389 23727 25895 27397 4170 5313 3716 C
ATOM 2225 O GLN A 389 -55.015-118.587 271.080 1.00204.17 O
ANISOU 2225 O GLN A 389 23862 26115 27599 4044 5311 4025 O
ATOM 2226 CB GLN A 389 -57.593-118.319 269.599 1.00209.75 C
ANISOU 2226 CB GLN A 389 23179 27082 29433 3664 5899 5007 C
ATOM 2227 CG GLN A 389 -58.644-118.020 268.550 1.00208.60 C
ANISOU 2227 CG GLN A 389 22382 27018 29859 3454 6065 5362 C
ATOM 2228 CD GLN A 389 -59.909-118.808 268.785 1.00209.01 C
ANISOU 2228 CD GLN A 389 22699 27314 29400 4105 6305 5105 C
ATOM 2229 OE1 GLN A 389 -59.877-119.867 269.402 1.00212.64 O
ANISOU 2229 OE1 GLN A 389 23627 28119 29049 4935 6632 5068 O
ATOM 2230 NE2 GLN A 389 -61.033-118.295 268.301 1.00206.21 N
ANISOU 2230 NE2 GLN A 389 22082 26775 29494 3774 6120 4905 N
ATOM 2231 N GLY A 390 -55.197-116.354 271.079 1.00198.48 N
ANISOU 2231 N GLY A 390 23846 25373 26196 4751 5212 3144 N
ATOM 2232 CA GLY A 390 -54.426-116.200 272.291 1.00196.46 C
ANISOU 2232 CA GLY A 390 24323 25201 25122 5308 5059 2822 C
ATOM 2233 C GLY A 390 -53.120-116.925 272.116 1.00186.90 C
ANISOU 2233 C GLY A 390 23299 23604 24112 4765 4513 2525 C
ATOM 2234 O GLY A 390 -52.599-117.515 273.052 1.00190.49 O
ANISOU 2234 O GLY A 390 24014 24252 24110 5045 4524 2684 O
ATOM 2235 N ARG A 391 -52.587-116.875 270.908 1.00173.96 N
ANISOU 2235 N ARG A 391 21513 21457 23126 4034 4054 2137 N
ATOM 2236 CA ARG A 391 -51.344-117.550 270.623 1.00167.08 C
ANISOU 2236 CA ARG A 391 20677 20228 22576 3479 3595 1949 C
ATOM 2237 C ARG A 391 -50.306-116.483 270.501 1.00158.91 C
ANISOU 2237 C ARG A 391 20164 18769 21445 3385 2967 1188 C
ATOM 2238 O ARG A 391 -50.496-115.531 269.757 1.00157.52 O
ANISOU 2238 O ARG A 391 20015 18382 21453 3300 2821 844 O
ATOM 2239 CB ARG A 391 -51.433-118.304 269.293 1.00165.58 C
ANISOU 2239 CB ARG A 391 19831 19818 23262 2728 3592 2209 C
ATOM 2240 CG ARG A 391 -52.410-119.478 269.240 1.00166.08 C
ANISOU 2240 CG ARG A 391 19891 19547 23666 2233 3204 2088 C
ATOM 2241 CD ARG A 391 -52.374-120.209 267.901 1.00165.12 C
ANISOU 2241 CD ARG A 391 19182 19224 24334 1623 3229 2347 C
ATOM 2242 NE ARG A 391 -53.307-121.338 267.771 1.00170.60 N
ANISOU 2242 NE ARG A 391 19406 20187 25227 1676 3678 3068 N
ATOM 2243 CZ ARG A 391 -53.106-122.583 268.202 1.00175.41 C
ANISOU 2243 CZ ARG A 391 19850 20865 25930 1658 3817 3585 C
ATOM 2244 NH1 ARG A 391 -51.975-122.923 268.800 1.00181.25 N
ANISOU 2244 NH1 ARG A 391 20084 21834 26948 1678 4216 4334 N
ATOM 2245 NH2 ARG A 391 -54.047-123.505 268.021 1.00174.67 N
ANISOU 2245 NH2 ARG A 391 20054 20607 25706 1612 3548 3417 N
ATOM 2246 N LYS A 392 -49.200-116.625 271.220 1.00155.06 N
ANISOU 2246 N LYS A 392 20046 18152 20718 3386 2575 989 N
ATOM 2247 CA LYS A 392 -48.161-115.627 271.115 1.00149.46 C
ANISOU 2247 CA LYS A 392 19743 17002 20041 3214 1903 371 C
ATOM 2248 C LYS A 392 -47.659-115.800 269.709 1.00140.50 C
ANISOU 2248 C LYS A 392 18173 15504 19704 2493 1692 276 C
ATOM 2249 O LYS A 392 -47.293-116.891 269.308 1.00133.15 O
ANISOU 2249 O LYS A 392 16896 14504 19190 2057 1686 504 O
ATOM 2250 CB LYS A 392 -47.043-115.905 272.109 1.00152.36 C
ANISOU 2250 CB LYS A 392 20487 17336 20066 3310 1513 286 C
ATOM 2251 N VAL A 393 -47.645-114.717 268.958 1.00139.37 N
ANISOU 2251 N VAL A 393 18060 15139 19755 2418 1529 -43 N
ATOM 2252 CA VAL A 393 -47.220-114.783 267.584 1.00130.79 C
ANISOU 2252 CA VAL A 393 16557 13802 19334 1840 1401 -89 C
ATOM 2253 C VAL A 393 -46.465-113.534 267.206 1.00129.81 C
ANISOU 2253 C VAL A 393 16705 13286 19333 1749 853 -517 C
ATOM 2254 O VAL A 393 -46.618-112.491 267.815 1.00133.28 O
ANISOU 2254 O VAL A 393 17615 13614 19413 2148 639 -816 O
ATOM 2255 CB VAL A 393 -48.422-114.968 266.653 1.00123.37 C
ANISOU 2255 CB VAL A 393 15187 13046 18642 1777 1846 138 C
ATOM 2256 CG1 VAL A 393 -49.494-113.961 266.987 1.00130.13 C
ANISOU 2256 CG1 VAL A 393 16293 13930 19223 2207 1916 -57 C
ATOM 2257 CG2 VAL A 393 -48.012-114.840 265.200 1.00115.74 C
ANISOU 2257 CG2 VAL A 393 13789 11902 18286 1213 1737 135 C
ATOM 2258 N ALA A 394 -45.645-113.670 266.184 1.00128.26 N
ANISOU 2258 N ALA A 394 16207 12864 19662 1248 608 -521 N
ATOM 2259 CA ALA A 394 -44.830-112.583 265.664 1.00126.92 C
ANISOU 2259 CA ALA A 394 16124 12324 19774 1072 115 -768 C
ATOM 2260 C ALA A 394 -44.676-112.767 264.163 1.00122.59 C
ANISOU 2260 C ALA A 394 15055 11755 19770 642 215 -611 C
ATOM 2261 O ALA A 394 -44.810-113.875 263.636 1.00122.83 O
ANISOU 2261 O ALA A 394 14741 11974 19955 444 508 -398 O
ATOM 2262 CB ALA A 394 -43.456-112.521 266.344 1.00129.43 C
ANISOU 2262 CB ALA A 394 16699 12387 20091 990 -456 -890 C
ATOM 2263 N CYS A 395 -44.394-111.668 263.474 1.00117.38 N
ANISOU 2263 N CYS A 395 14357 10851 19392 531 -53 -711 N
ATOM 2264 CA CYS A 395 -44.315-111.674 262.024 1.00114.22 C
ANISOU 2264 CA CYS A 395 13490 10493 19415 222 63 -540 C
ATOM 2265 C CYS A 395 -42.943-111.214 261.553 1.00123.46 C
ANISOU 2265 C CYS A 395 14515 11399 20996 -53 -371 -459 C
ATOM 2266 O CYS A 395 -42.202-110.543 262.274 1.00129.62 O
ANISOU 2266 O CYS A 395 15566 11863 21821 -36 -856 -575 O
ATOM 2267 CB CYS A 395 -45.397-110.781 261.405 1.00110.00 C
ANISOU 2267 CB CYS A 395 12895 9998 18904 348 248 -569 C
ATOM 2268 SG CYS A 395 -47.066-111.442 261.557 1.00111.88 S
ANISOU 2268 SG CYS A 395 13045 10629 18835 585 828 -479 S
ATOM 2269 N PHE A 396 -42.614-111.601 260.324 1.00125.92 N
ANISOU 2269 N PHE A 396 14381 11854 21607 -285 -210 -232 N
ATOM 2270 CA PHE A 396 -41.431-111.103 259.640 1.00127.62 C
ANISOU 2270 CA PHE A 396 14320 11915 22256 -511 -505 -9 C
ATOM 2271 C PHE A 396 -41.689-111.181 258.141 1.00120.22 C
ANISOU 2271 C PHE A 396 12960 11240 21477 -585 -185 202 C
ATOM 2272 O PHE A 396 -42.748-111.633 257.697 1.00116.12 O
ANISOU 2272 O PHE A 396 12402 10969 20747 -496 176 120 O
ATOM 2273 CB PHE A 396 -40.167-111.869 260.060 1.00132.40 C
ANISOU 2273 CB PHE A 396 14849 12480 22977 -637 -706 124 C
ATOM 2274 CG PHE A 396 -40.244-113.358 259.854 1.00135.25 C
ANISOU 2274 CG PHE A 396 15075 13133 23180 -617 -323 168 C
ATOM 2275 CD1 PHE A 396 -40.898-114.167 260.770 1.00136.96 C
ANISOU 2275 CD1 PHE A 396 15563 13427 23050 -479 -157 4 C
ATOM 2276 CD2 PHE A 396 -39.628-113.952 258.763 1.00135.02 C
ANISOU 2276 CD2 PHE A 396 14657 13287 23360 -698 -143 400 C
ATOM 2277 CE1 PHE A 396 -40.959-115.537 260.589 1.00134.90 C
ANISOU 2277 CE1 PHE A 396 15173 13340 22744 -490 131 69 C
ATOM 2278 CE2 PHE A 396 -39.682-115.321 258.577 1.00132.46 C
ANISOU 2278 CE2 PHE A 396 14271 13142 22917 -646 141 382 C
ATOM 2279 CZ PHE A 396 -40.349-116.115 259.492 1.00133.43 C
ANISOU 2279 CZ PHE A 396 14655 13257 22786 -576 249 216 C
ATOM 2280 N GLY A 397 -40.724-110.712 257.358 1.00118.58 N
ANISOU 2280 N GLY A 397 12417 10991 21646 -732 -340 516 N
ATOM 2281 CA GLY A 397 -40.883-110.728 255.918 1.00117.61 C
ANISOU 2281 CA GLY A 397 11913 11176 21599 -727 -41 751 C
ATOM 2282 C GLY A 397 -39.883-109.863 255.183 1.00122.00 C
ANISOU 2282 C GLY A 397 12085 11666 22602 -845 -231 1203 C
ATOM 2283 O GLY A 397 -39.267-108.969 255.772 1.00128.02 O
ANISOU 2283 O GLY A 397 12889 12038 23715 -985 -675 1313 O
ATOM 2284 N CYS A 398 -39.714-110.121 253.892 1.00119.67 N
ANISOU 2284 N CYS A 398 11413 11750 22307 -772 78 1495 N
ATOM 2285 CA CYS A 398 -38.788-109.375 253.058 1.00122.40 C
ANISOU 2285 CA CYS A 398 11294 12150 23062 -831 6 2067 C
ATOM 2286 C CYS A 398 -39.550-108.481 252.091 1.00127.10 C
ANISOU 2286 C CYS A 398 11733 12884 23673 -761 149 2236 C
ATOM 2287 O CYS A 398 -40.706-108.746 251.750 1.00122.03 O
ANISOU 2287 O CYS A 398 11261 12451 22653 -624 399 1934 O
ATOM 2288 CB CYS A 398 -37.864-110.318 252.284 1.00118.63 C
ANISOU 2288 CB CYS A 398 10468 12082 22524 -690 294 2378 C
ATOM 2289 SG CYS A 398 -36.653-111.157 253.325 1.00119.09 S
ANISOU 2289 SG CYS A 398 10554 11957 22740 -785 74 2396 S
ATOM 2290 N GLY A 399 -38.893-107.421 251.660 1.00139.86 N
ANISOU 2290 N GLY A 399 12990 14371 25781 -872 -39 2773 N
ATOM 2291 CA GLY A 399 -39.484-106.485 250.725 1.00146.08 C
ANISOU 2291 CA GLY A 399 13570 15274 26658 -807 74 3053 C
ATOM 2292 C GLY A 399 -38.424-105.681 250.012 1.00156.19 C
ANISOU 2292 C GLY A 399 14272 16572 28500 -897 -19 3862 C
ATOM 2293 O GLY A 399 -37.309-106.157 249.783 1.00161.96 O
ANISOU 2293 O GLY A 399 14653 17508 29375 -888 55 4268 O
ATOM 2294 N ASP A 400 -38.777-104.449 249.653 1.00158.15 N
ANISOU 2294 N ASP A 400 14378 16606 29105 -966 -168 4163 N
ATOM 2295 CA ASP A 400 -37.850-103.553 248.979 1.00157.74 C
ANISOU 2295 CA ASP A 400 13716 16516 29700 -1084 -284 5047 C
ATOM 2296 C ASP A 400 -38.350-102.126 249.144 1.00150.43 C
ANISOU 2296 C ASP A 400 12849 15020 29287 -1251 -673 5155 C
ATOM 2297 O ASP A 400 -39.557-101.877 249.088 1.00141.47 O
ANISOU 2297 O ASP A 400 12043 13881 27829 -1107 -558 4745 O
ATOM 2298 CB ASP A 400 -37.706-103.910 247.495 1.00160.57 C
ANISOU 2298 CB ASP A 400 13595 17677 29738 -762 299 5599 C
ATOM 2299 CG ASP A 400 -36.674-103.056 246.784 1.00168.48 C
ANISOU 2299 CG ASP A 400 13959 18730 31324 -810 248 6627 C
ATOM 2300 OD1 ASP A 400 -35.849-102.414 247.469 1.00171.34 O
ANISOU 2300 OD1 ASP A 400 14292 18519 32291 -1082 -283 6874 O
ATOM 2301 OD2 ASP A 400 -36.682-103.033 245.535 1.00172.08 O
ANISOU 2301 OD2 ASP A 400 14164 19801 31416 -473 683 7104 O
ATOM 2302 N SER A 401 -37.413-101.197 249.348 1.00151.71 N
ANISOU 2302 N SER A 401 12672 14671 30301 -1552 -1163 5735 N
ATOM 2303 CA SER A 401 -37.786 -99.803 249.560 1.00149.56 C
ANISOU 2303 CA SER A 401 12523 13762 30539 -1669 -1640 5793 C
ATOM 2304 C SER A 401 -38.421 -99.190 248.318 1.00145.12 C
ANISOU 2304 C SER A 401 11603 13541 29994 -1502 -1256 6312 C
ATOM 2305 O SER A 401 -39.222 -98.256 248.433 1.00141.77 O
ANISOU 2305 O SER A 401 11385 12666 29814 -1522 -1468 6178 O
ATOM 2306 CB SER A 401 -36.562 -98.990 249.983 1.00154.94 C
ANISOU 2306 CB SER A 401 13022 14033 31816 -1826 -2318 6169 C
ATOM 2307 OG SER A 401 -35.975 -99.521 251.159 1.00153.49 O
ANISOU 2307 OG SER A 401 13169 13570 31580 -1969 -2718 5693 O
ATOM 2308 N SER A 402 -38.095 -99.710 247.131 1.00148.63 N
ANISOU 2308 N SER A 402 11581 14798 30093 -1256 -693 6874 N
ATOM 2309 CA SER A 402 -38.577 -99.133 245.880 1.00155.78 C
ANISOU 2309 CA SER A 402 12161 16128 30901 -1022 -340 7435 C
ATOM 2310 C SER A 402 -40.086 -99.251 245.702 1.00146.39 C
ANISOU 2310 C SER A 402 11294 15133 29194 -843 -64 6860 C
ATOM 2311 O SER A 402 -40.632 -98.617 244.792 1.00146.60 O
ANISOU 2311 O SER A 402 11074 15409 29219 -684 136 7283 O
ATOM 2312 CB SER A 402 -37.870 -99.790 244.692 1.00163.63 C
ANISOU 2312 CB SER A 402 12811 17992 31369 -674 199 8033 C
ATOM 2313 OG SER A 402 -38.269 -99.194 243.469 1.00174.25 O
ANISOU 2313 OG SER A 402 13905 19762 32540 -416 508 8616 O
ATOM 2314 N TRP A 403 -40.767-100.030 246.533 1.00139.31 N
ANISOU 2314 N TRP A 403 11010 14163 27760 -793 -68 5917 N
ATOM 2315 CA TRP A 403 -42.203-100.223 246.414 1.00137.75 C
ANISOU 2315 CA TRP A 403 11189 14183 26969 -563 166 5345 C
ATOM 2316 C TRP A 403 -42.940 -99.378 247.447 1.00138.13 C
ANISOU 2316 C TRP A 403 11701 13471 27310 -654 -240 4874 C
ATOM 2317 O TRP A 403 -42.431 -99.112 248.539 1.00136.62 O
ANISOU 2317 O TRP A 403 11779 12627 27503 -858 -702 4627 O
ATOM 2318 CB TRP A 403 -42.564-101.701 246.576 1.00135.32 C
ANISOU 2318 CB TRP A 403 11192 14344 25878 -406 473 4697 C
ATOM 2319 CG TRP A 403 -41.835-102.581 245.603 1.00138.91 C
ANISOU 2319 CG TRP A 403 11291 15504 25983 -224 849 5056 C
ATOM 2320 CD1 TRP A 403 -40.596-103.129 245.764 1.00143.44 C
ANISOU 2320 CD1 TRP A 403 11668 16137 26697 -286 847 5291 C
ATOM 2321 CD2 TRP A 403 -42.295-103.001 244.312 1.00138.85 C
ANISOU 2321 CD2 TRP A 403 11104 16258 25394 117 1270 5217 C
ATOM 2322 NE1 TRP A 403 -40.257-103.868 244.656 1.00144.95 N
ANISOU 2322 NE1 TRP A 403 11583 17083 26408 45 1289 5582 N
ATOM 2323 CE2 TRP A 403 -41.283-103.806 243.750 1.00142.87 C
ANISOU 2323 CE2 TRP A 403 11358 17257 25668 304 1530 5511 C
ATOM 2324 CE3 TRP A 403 -43.464-102.777 243.578 1.00137.03 C
ANISOU 2324 CE3 TRP A 403 10914 16351 24798 315 1426 5137 C
ATOM 2325 CZ2 TRP A 403 -41.406-104.388 242.489 1.00143.89 C
ANISOU 2325 CZ2 TRP A 403 11344 18178 25151 729 1930 5665 C
ATOM 2326 CZ3 TRP A 403 -43.584-103.356 242.326 1.00138.06 C
ANISOU 2326 CZ3 TRP A 403 10878 17261 24317 675 1772 5303 C
ATOM 2327 CH2 TRP A 403 -42.561-104.151 241.795 1.00141.60 C
ANISOU 2327 CH2 TRP A 403 11143 18178 24483 901 2016 5536 C
ATOM 2328 N GLU A 404 -44.152 -98.953 247.081 1.00140.59 N
ANISOU 2328 N GLU A 404 12117 13891 27409 -454 -76 4750 N
ATOM 2329 CA GLU A 404 -44.923 -98.062 247.942 1.00147.26 C
ANISOU 2329 CA GLU A 404 13385 14062 28505 -422 -394 4360 C
ATOM 2330 C GLU A 404 -45.339 -98.744 249.240 1.00144.29 C
ANISOU 2330 C GLU A 404 13615 13477 27730 -364 -473 3514 C
ATOM 2331 O GLU A 404 -45.542 -98.069 250.256 1.00146.96 O
ANISOU 2331 O GLU A 404 14384 13149 28304 -331 -848 3150 O
ATOM 2332 CB GLU A 404 -46.155 -97.551 247.193 1.00150.56 C
ANISOU 2332 CB GLU A 404 13716 14744 28746 -171 -132 4477 C
ATOM 2333 CG GLU A 404 -46.929 -96.458 247.916 1.00155.45 C
ANISOU 2333 CG GLU A 404 14704 14669 29692 -52 -424 4207 C
ATOM 2334 CD GLU A 404 -46.741 -95.094 247.282 1.00162.85 C
ANISOU 2334 CD GLU A 404 15306 15218 31353 -99 -652 4894 C
ATOM 2335 OE1 GLU A 404 -45.997 -95.001 246.283 1.00165.49 O
ANISOU 2335 OE1 GLU A 404 15073 15875 31930 -234 -551 5649 O
ATOM 2336 OE2 GLU A 404 -47.340 -94.116 247.779 1.00166.98 O
ANISOU 2336 OE2 GLU A 404 16125 15116 32202 38 -916 4712 O
ATOM 2337 N TYR A 405 -45.464-100.068 249.232 1.00140.34 N
ANISOU 2337 N TYR A 405 13173 13524 26626 -315 -141 3207 N
ATOM 2338 CA TYR A 405 -45.945-100.829 250.384 1.00138.87 C
ANISOU 2338 CA TYR A 405 13491 13249 26024 -236 -130 2507 C
ATOM 2339 C TYR A 405 -44.815-101.728 250.867 1.00136.87 C
ANISOU 2339 C TYR A 405 13263 13007 25735 -424 -236 2422 C
ATOM 2340 O TYR A 405 -44.753-102.912 250.530 1.00135.39 O
ANISOU 2340 O TYR A 405 12979 13328 25134 -407 74 2342 O
ATOM 2341 CB TYR A 405 -47.180-101.615 250.014 1.00137.12 C
ANISOU 2341 CB TYR A 405 13292 13591 25217 -37 305 2259 C
ATOM 2342 CG TYR A 405 -48.178-100.782 249.251 1.00142.66 C
ANISOU 2342 CG TYR A 405 13816 14413 25976 136 436 2500 C
ATOM 2343 CD1 TYR A 405 -48.930 -99.807 249.893 1.00147.18 C
ANISOU 2343 CD1 TYR A 405 14664 14529 26729 317 296 2330 C
ATOM 2344 CD2 TYR A 405 -48.354-100.955 247.887 1.00144.87 C
ANISOU 2344 CD2 TYR A 405 13672 15270 26100 172 688 2899 C
ATOM 2345 CE1 TYR A 405 -49.836 -99.032 249.199 1.00151.12 C
ANISOU 2345 CE1 TYR A 405 14977 15129 27314 496 419 2588 C
ATOM 2346 CE2 TYR A 405 -49.258-100.187 247.184 1.00150.37 C
ANISOU 2346 CE2 TYR A 405 14188 16100 26847 334 785 3159 C
ATOM 2347 CZ TYR A 405 -49.997 -99.227 247.844 1.00153.11 C
ANISOU 2347 CZ TYR A 405 14768 15970 27437 479 657 3022 C
ATOM 2348 OH TYR A 405 -50.901 -98.459 247.147 1.00156.25 O
ANISOU 2348 OH TYR A 405 14963 16495 27911 662 760 3313 O
ATOM 2349 N PHE A 406 -43.916-101.152 251.662 1.00136.40 N
ANISOU 2349 N PHE A 406 13343 12344 26139 -597 -725 2436 N
ATOM 2350 CA PHE A 406 -42.783-101.894 252.202 1.00131.32 C
ANISOU 2350 CA PHE A 406 12703 11657 25537 -785 -898 2404 C
ATOM 2351 C PHE A 406 -43.294-102.958 253.164 1.00126.77 C
ANISOU 2351 C PHE A 406 12581 11214 24372 -652 -747 1770 C
ATOM 2352 O PHE A 406 -43.822-102.633 254.231 1.00128.85 O
ANISOU 2352 O PHE A 406 13339 11107 24511 -516 -952 1315 O
ATOM 2353 CB PHE A 406 -41.817-100.947 252.904 1.00136.40 C
ANISOU 2353 CB PHE A 406 13417 11558 26852 -1015 -1571 2539 C
ATOM 2354 CG PHE A 406 -40.524-101.593 253.297 1.00137.44 C
ANISOU 2354 CG PHE A 406 13407 11664 27151 -1245 -1792 2677 C
ATOM 2355 CD1 PHE A 406 -39.431-101.538 252.452 1.00140.94 C
ANISOU 2355 CD1 PHE A 406 13212 12279 28062 -1447 -1786 3421 C
ATOM 2356 CD2 PHE A 406 -40.402-102.266 254.502 1.00134.38 C
ANISOU 2356 CD2 PHE A 406 13487 11129 26443 -1220 -1974 2128 C
ATOM 2357 CE1 PHE A 406 -38.242-102.131 252.802 1.00139.66 C
ANISOU 2357 CE1 PHE A 406 12862 12118 28083 -1632 -1969 3609 C
ATOM 2358 CE2 PHE A 406 -39.211-102.866 254.856 1.00134.14 C
ANISOU 2358 CE2 PHE A 406 13299 11088 26580 -1423 -2187 2289 C
ATOM 2359 CZ PHE A 406 -38.128-102.798 254.004 1.00136.65 C
ANISOU 2359 CZ PHE A 406 12961 11557 27404 -1634 -2189 3027 C
ATOM 2360 N CYS A 407 -43.136-104.227 252.787 1.00117.82 N
ANISOU 2360 N CYS A 407 11289 10605 22873 -650 -388 1763 N
ATOM 2361 CA CYS A 407 -43.582-105.356 253.604 1.00105.33 C
ANISOU 2361 CA CYS A 407 10051 9171 20799 -555 -221 1275 C
ATOM 2362 C CYS A 407 -45.053-105.218 253.980 1.00103.43 C
ANISOU 2362 C CYS A 407 10109 8964 20225 -323 -31 923 C
ATOM 2363 O CYS A 407 -45.449-105.426 255.130 1.00104.31 O
ANISOU 2363 O CYS A 407 10631 8909 20095 -192 -85 544 O
ATOM 2364 CB CYS A 407 -42.715-105.516 254.855 1.00101.40 C
ANISOU 2364 CB CYS A 407 9848 8283 20397 -657 -611 1072 C
ATOM 2365 SG CYS A 407 -41.002-106.004 254.539 1.00105.51 S
ANISOU 2365 SG CYS A 407 9960 8855 21273 -911 -775 1513 S
ATOM 2366 N GLY A 408 -45.876-104.853 252.997 1.00103.95 N
ANISOU 2366 N GLY A 408 9941 9291 20265 -233 209 1101 N
ATOM 2367 CA GLY A 408 -47.309-104.799 253.227 1.00110.44 C
ANISOU 2367 CA GLY A 408 10932 10227 20803 -7 434 866 C
ATOM 2368 C GLY A 408 -47.907-106.138 253.604 1.00115.54 C
ANISOU 2368 C GLY A 408 11667 11200 21034 33 712 609 C
ATOM 2369 O GLY A 408 -48.990-106.179 254.201 1.00118.60 O
ANISOU 2369 O GLY A 408 12230 11625 21208 228 872 427 O
ATOM 2370 N ALA A 409 -47.226-107.236 253.254 1.00115.20 N
ANISOU 2370 N ALA A 409 11478 11387 20905 -126 777 639 N
ATOM 2371 CA ALA A 409 -47.647-108.569 253.675 1.00105.63 C
ANISOU 2371 CA ALA A 409 10355 10377 19402 -130 963 420 C
ATOM 2372 C ALA A 409 -47.682-108.676 255.193 1.00105.08 C
ANISOU 2372 C ALA A 409 10669 10045 19212 -34 888 181 C
ATOM 2373 O ALA A 409 -48.629-109.230 255.766 1.00101.42 O
ANISOU 2373 O ALA A 409 10302 9711 18524 85 1095 69 O
ATOM 2374 CB ALA A 409 -46.701-109.618 253.092 1.00 98.38 C
ANISOU 2374 CB ALA A 409 9274 9642 18464 -270 981 477 C
ATOM 2375 N VAL A 410 -46.657-108.139 255.860 1.00109.71 N
ANISOU 2375 N VAL A 410 11460 10276 19949 -67 571 143 N
ATOM 2376 CA VAL A 410 -46.591-108.204 257.317 1.00110.93 C
ANISOU 2376 CA VAL A 410 12040 10198 19910 78 436 -112 C
ATOM 2377 C VAL A 410 -47.760-107.450 257.939 1.00117.31 C
ANISOU 2377 C VAL A 410 13117 10936 20517 418 538 -268 C
ATOM 2378 O VAL A 410 -48.306-107.857 258.972 1.00120.05 O
ANISOU 2378 O VAL A 410 13735 11355 20523 660 685 -425 O
ATOM 2379 CB VAL A 410 -45.234-107.664 257.804 1.00107.12 C
ANISOU 2379 CB VAL A 410 11713 9311 19679 -45 -45 -121 C
ATOM 2380 CG1 VAL A 410 -45.121-107.748 259.318 1.00108.69 C
ANISOU 2380 CG1 VAL A 410 12409 9293 19596 146 -250 -424 C
ATOM 2381 CG2 VAL A 410 -44.097-108.423 257.130 1.00105.27 C
ANISOU 2381 CG2 VAL A 410 11133 9215 19650 -321 -68 122 C
ATOM 2382 N ASP A 411 -48.177-106.350 257.308 1.00118.58 N
ANISOU 2382 N ASP A 411 13187 10988 20879 490 496 -178 N
ATOM 2383 CA ASP A 411 -49.312-105.589 257.818 1.00122.75 C
ANISOU 2383 CA ASP A 411 13953 11455 21230 881 625 -304 C
ATOM 2384 C ASP A 411 -50.616-106.358 257.651 1.00120.91 C
ANISOU 2384 C ASP A 411 13491 11699 20749 1003 1115 -193 C
ATOM 2385 O ASP A 411 -51.448-106.385 258.567 1.00120.95 O
ANISOU 2385 O ASP A 411 13716 11791 20449 1364 1332 -282 O
ATOM 2386 CB ASP A 411 -49.392-104.237 257.111 1.00129.22 C
ANISOU 2386 CB ASP A 411 14693 12005 22401 913 441 -186 C
ATOM 2387 CG ASP A 411 -48.108-103.440 257.232 1.00133.94 C
ANISOU 2387 CG ASP A 411 15437 12068 23386 733 -111 -203 C
ATOM 2388 OD1 ASP A 411 -47.394-103.609 258.244 1.00138.46 O
ANISOU 2388 OD1 ASP A 411 16368 12379 23860 745 -414 -449 O
ATOM 2389 OD2 ASP A 411 -47.812-102.645 256.315 1.00133.32 O
ANISOU 2389 OD2 ASP A 411 15086 11832 23739 572 -266 78 O
ATOM 2390 N ALA A 412 -50.813-106.991 256.491 1.00121.74 N
ANISOU 2390 N ALA A 412 13146 12125 20984 730 1272 27 N
ATOM 2391 CA ALA A 412 -52.052-107.725 256.251 1.00120.88 C
ANISOU 2391 CA ALA A 412 12767 12413 20748 773 1623 163 C
ATOM 2392 C ALA A 412 -52.174-108.923 257.183 1.00120.47 C
ANISOU 2392 C ALA A 412 12805 12488 20480 781 1781 121 C
ATOM 2393 O ALA A 412 -53.274-109.251 257.644 1.00118.23 O
ANISOU 2393 O ALA A 412 12429 12426 20065 973 2073 254 O
ATOM 2394 CB ALA A 412 -52.124-108.173 254.791 1.00115.29 C
ANISOU 2394 CB ALA A 412 11632 11972 20201 483 1631 337 C
ATOM 2395 N ILE A 413 -51.055-109.588 257.473 1.00121.06 N
ANISOU 2395 N ILE A 413 13012 12436 20550 585 1605 9 N
ATOM 2396 CA ILE A 413 -51.084-110.745 258.363 1.00120.64 C
ANISOU 2396 CA ILE A 413 13036 12478 20324 587 1738 15 C
ATOM 2397 C ILE A 413 -51.357-110.307 259.797 1.00126.91 C
ANISOU 2397 C ILE A 413 14226 13204 20788 1005 1821 -73 C
ATOM 2398 O ILE A 413 -52.216-110.873 260.483 1.00128.76 O
ANISOU 2398 O ILE A 413 14417 13677 20830 1207 2135 94 O
ATOM 2399 CB ILE A 413 -49.769-111.536 258.253 1.00113.99 C
ANISOU 2399 CB ILE A 413 12222 11514 19574 304 1521 -61 C
ATOM 2400 CG1 ILE A 413 -49.599-112.090 256.838 1.00105.72 C
ANISOU 2400 CG1 ILE A 413 10823 10603 18744 14 1496 10 C
ATOM 2401 CG2 ILE A 413 -49.734-112.661 259.277 1.00113.57 C
ANISOU 2401 CG2 ILE A 413 12280 11514 19359 331 1634 -28 C
ATOM 2402 CD1 ILE A 413 -48.254-112.733 256.598 1.00101.66 C
ANISOU 2402 CD1 ILE A 413 10318 9991 18319 -175 1319 -39 C
ATOM 2403 N GLU A 414 -50.632-109.287 260.269 1.00131.39 N
ANISOU 2403 N GLU A 414 15187 13446 21289 1168 1519 -313 N
ATOM 2404 CA GLU A 414 -50.829-108.797 261.630 1.00139.56 C
ANISOU 2404 CA GLU A 414 16712 14393 21920 1654 1522 -492 C
ATOM 2405 C GLU A 414 -52.252-108.301 261.851 1.00150.37 C
ANISOU 2405 C GLU A 414 18057 15990 23087 2109 1912 -376 C
ATOM 2406 O GLU A 414 -52.765-108.368 262.974 1.00156.13 O
ANISOU 2406 O GLU A 414 19060 16879 23383 2587 2143 -379 O
ATOM 2407 CB GLU A 414 -49.828-107.683 261.939 1.00139.38 C
ANISOU 2407 CB GLU A 414 17122 13882 21953 1717 996 -813 C
ATOM 2408 CG GLU A 414 -48.402-108.164 262.142 1.00138.93 C
ANISOU 2408 CG GLU A 414 17148 13619 22018 1386 602 -893 C
ATOM 2409 CD GLU A 414 -47.405-107.023 262.206 1.00144.51 C
ANISOU 2409 CD GLU A 414 18136 13798 22975 1322 -4 -1109 C
ATOM 2410 OE1 GLU A 414 -47.726-105.922 261.708 1.00148.16 O
ANISOU 2410 OE1 GLU A 414 18604 14032 23659 1400 -115 -1139 O
ATOM 2411 OE2 GLU A 414 -46.302-107.227 262.756 1.00144.63 O
ANISOU 2411 OE2 GLU A 414 18337 13600 23015 1181 -404 -1211 O
ATOM 2412 N GLU A 415 -52.904-107.802 260.798 1.00152.43 N
ANISOU 2412 N GLU A 415 17977 16311 23628 2016 2009 -231 N
ATOM 2413 CA GLU A 415 -54.286-107.357 260.936 1.00156.08 C
ANISOU 2413 CA GLU A 415 18330 17020 23952 2448 2398 -49 C
ATOM 2414 C GLU A 415 -55.220-108.535 261.185 1.00154.43 C
ANISOU 2414 C GLU A 415 17735 17277 23663 2450 2844 341 C
ATOM 2415 O GLU A 415 -56.185-108.417 261.947 1.00157.77 O
ANISOU 2415 O GLU A 415 18180 17961 23803 2953 3229 535 O
ATOM 2416 CB GLU A 415 -54.715-106.579 259.693 1.00158.18 C
ANISOU 2416 CB GLU A 415 18279 17246 24575 2311 2356 59 C
ATOM 2417 CG GLU A 415 -56.014-105.804 259.863 1.00165.45 C
ANISOU 2417 CG GLU A 415 19152 18328 25383 2833 2688 211 C
ATOM 2418 CD GLU A 415 -55.888-104.654 260.847 1.00171.80 C
ANISOU 2418 CD GLU A 415 20596 18795 25887 3441 2574 -131 C
ATOM 2419 OE1 GLU A 415 -54.754-104.179 261.071 1.00171.98 O
ANISOU 2419 OE1 GLU A 415 21043 18351 25950 3339 2098 -491 O
ATOM 2420 OE2 GLU A 415 -56.924-104.225 261.397 1.00176.44 O
ANISOU 2420 OE2 GLU A 415 21262 19570 26207 4047 2935 -35 O
ATOM 2421 N LYS A 416 -54.947-109.680 260.555 1.00152.33 N
ANISOU 2421 N LYS A 416 17103 17108 23666 1920 2790 491 N
ATOM 2422 CA LYS A 416 -55.758-110.867 260.806 1.00155.19 C
ANISOU 2422 CA LYS A 416 17082 17809 24073 1846 3113 891 C
ATOM 2423 C LYS A 416 -55.428-111.505 262.149 1.00164.07 C
ANISOU 2423 C LYS A 416 18490 18996 24853 2081 3247 932 C
ATOM 2424 O LYS A 416 -56.308-112.097 262.784 1.00168.56 O
ANISOU 2424 O LYS A 416 18828 19889 25330 2295 3634 1351 O
ATOM 2425 CB LYS A 416 -55.568-111.888 259.685 1.00145.82 C
ANISOU 2425 CB LYS A 416 15482 16620 23302 1234 2927 975 C
ATOM 2426 CG LYS A 416 -56.628-111.831 258.601 1.00142.53 C
ANISOU 2426 CG LYS A 416 14565 16397 23194 1072 2981 1220 C
ATOM 2427 CD LYS A 416 -56.602-113.089 257.750 1.00137.67 C
ANISOU 2427 CD LYS A 416 13600 15788 22920 551 2783 1300 C
ATOM 2428 CE LYS A 416 -57.722-113.086 256.723 1.00137.33 C
ANISOU 2428 CE LYS A 416 13066 15943 23172 389 2753 1543 C
ATOM 2429 NZ LYS A 416 -57.655-114.271 255.823 1.00133.84 N
ANISOU 2429 NZ LYS A 416 12375 15438 23039 -91 2439 1513 N
ATOM 2430 N LEU A 417 -54.175-111.400 262.595 1.00169.65 N
ANISOU 2430 N LEU A 417 19652 19421 25384 2049 2927 569 N
ATOM 2431 CA LEU A 417 -53.781-112.030 263.851 1.00175.13 C
ANISOU 2431 CA LEU A 417 20632 20191 25719 2269 3004 607 C
ATOM 2432 C LEU A 417 -54.405-111.316 265.045 1.00180.67 C
ANISOU 2432 C LEU A 417 21710 21086 25849 3027 3286 616 C
ATOM 2433 O LEU A 417 -55.014-111.954 265.911 1.00185.30 O
ANISOU 2433 O LEU A 417 22208 22034 26164 3344 3687 997 O
ATOM 2434 CB LEU A 417 -52.257-112.057 263.966 1.00174.91 C
ANISOU 2434 CB LEU A 417 20964 19812 25683 2029 2528 232 C
ATOM 2435 CG LEU A 417 -51.546-112.899 262.905 1.00171.15 C
ANISOU 2435 CG LEU A 417 20149 19200 25679 1397 2312 250 C
ATOM 2436 CD1 LEU A 417 -50.041-112.761 263.032 1.00172.01 C
ANISOU 2436 CD1 LEU A 417 20565 18992 25799 1228 1868 -51 C
ATOM 2437 CD2 LEU A 417 -51.965-114.358 263.005 1.00169.42 C
ANISOU 2437 CD2 LEU A 417 19574 19185 25612 1193 2555 619 C
ATOM 2438 N LYS A 418 -54.262-109.990 265.110 1.00176.72 N
ANISOU 2438 N LYS A 418 21639 20345 25161 3368 3081 223 N
ATOM 2439 CA LYS A 418 -54.910-109.233 266.175 1.00176.07 C
ANISOU 2439 CA LYS A 418 21983 20428 24489 4196 3340 160 C
ATOM 2440 C LYS A 418 -56.423-109.199 266.016 1.00174.04 C
ANISOU 2440 C LYS A 418 21264 20607 24255 4522 3936 653 C
ATOM 2441 O LYS A 418 -57.128-108.897 266.985 1.00179.10 O
ANISOU 2441 O LYS A 418 22129 21559 24363 5283 4333 787 O
ATOM 2442 CB LYS A 418 -54.356-107.808 266.232 1.00175.20 C
ANISOU 2442 CB LYS A 418 22479 19833 24255 4465 2875 -429 C
ATOM 2443 CG LYS A 418 -53.038-107.693 266.979 1.00173.94 C
ANISOU 2443 CG LYS A 418 22932 19312 23845 4461 2315 -889 C
ATOM 2444 CD LYS A 418 -52.556-106.253 267.049 1.00174.39 C
ANISOU 2444 CD LYS A 418 23575 18805 23879 4707 1767 -1448 C
ATOM 2445 CE LYS A 418 -51.263-106.145 267.842 1.00173.77 C
ANISOU 2445 CE LYS A 418 24089 18346 23589 4687 1117 -1886 C
ATOM 2446 NZ LYS A 418 -50.755-104.747 267.900 1.00176.36 N
ANISOU 2446 NZ LYS A 418 24979 18015 24015 4859 457 -2423 N
ATOM 2447 N ASN A 419 -56.935-109.496 264.819 1.00166.39 N
ANISOU 2447 N ASN A 419 19656 19694 23871 4003 3996 943 N
ATOM 2448 CA ASN A 419 -58.377-109.632 264.645 1.00167.78 C
ANISOU 2448 CA ASN A 419 19271 20307 24170 4217 4518 1516 C
ATOM 2449 C ASN A 419 -58.912-110.799 265.462 1.00169.24 C
ANISOU 2449 C ASN A 419 19135 20936 24231 4338 4960 2106 C
ATOM 2450 O ASN A 419 -59.954-110.684 266.119 1.00175.08 O
ANISOU 2450 O ASN A 419 19705 22112 24704 4944 5498 2564 O
ATOM 2451 CB ASN A 419 -58.708-109.813 263.162 1.00164.68 C
ANISOU 2451 CB ASN A 419 18277 19855 24438 3566 4362 1673 C
ATOM 2452 CG ASN A 419 -60.198-109.749 262.877 1.00171.55 C
ANISOU 2452 CG ASN A 419 18550 21126 25506 3768 4797 2247 C
ATOM 2453 OD1 ASN A 419 -60.994-110.480 263.467 1.00176.19 O
ANISOU 2453 OD1 ASN A 419 18759 22111 26075 3941 5218 2821 O
ATOM 2454 ND2 ASN A 419 -60.582-108.867 261.962 1.00173.39 N
ANISOU 2454 ND2 ASN A 419 18645 21267 25968 3743 4694 2164 N
ATOM 2455 N LEU A 420 -58.209-111.927 265.439 1.00166.23 N
ANISOU 2455 N LEU A 420 18642 20456 24060 3800 4759 2158 N
ATOM 2456 CA LEU A 420 -58.633-113.129 266.140 1.00168.48 C
ANISOU 2456 CA LEU A 420 18571 21090 24355 3812 5117 2779 C
ATOM 2457 C LEU A 420 -58.146-113.180 267.582 1.00172.62 C
ANISOU 2457 C LEU A 420 19648 21773 24166 4406 5272 2720 C
ATOM 2458 O LEU A 420 -58.505-114.112 268.309 1.00179.08 O
ANISOU 2458 O LEU A 420 20193 22936 24913 4528 5631 3312 O
ATOM 2459 CB LEU A 420 -58.150-114.369 265.381 1.00161.25 C
ANISOU 2459 CB LEU A 420 17269 19941 24057 2964 4797 2873 C
ATOM 2460 CG LEU A 420 -58.516-114.387 263.895 1.00154.14 C
ANISOU 2460 CG LEU A 420 15904 18873 23790 2381 4543 2844 C
ATOM 2461 CD1 LEU A 420 -58.031-115.664 263.227 1.00147.63 C
ANISOU 2461 CD1 LEU A 420 14799 17801 23491 1659 4207 2875 C
ATOM 2462 CD2 LEU A 420 -60.017-114.215 263.705 1.00157.63 C
ANISOU 2462 CD2 LEU A 420 15759 19680 24454 2571 4929 3436 C
ATOM 2463 N GLY A 421 -57.344-112.210 268.013 1.00170.02 N
ANISOU 2463 N GLY A 421 20079 21194 23329 4776 4973 2052 N
ATOM 2464 CA GLY A 421 -56.895-112.137 269.386 1.00171.28 C
ANISOU 2464 CA GLY A 421 20854 21504 22719 5417 5038 1911 C
ATOM 2465 C GLY A 421 -55.526-112.714 269.668 1.00163.96 C
ANISOU 2465 C GLY A 421 20264 20278 21754 5033 4554 1586 C
ATOM 2466 O GLY A 421 -55.137-112.785 270.839 1.00167.41 O
ANISOU 2466 O GLY A 421 21189 20878 21540 5540 4575 1516 O
ATOM 2467 N ALA A 422 -54.787-113.129 268.642 1.00154.59 N
ANISOU 2467 N ALA A 422 18837 18696 21206 4208 4129 1404 N
ATOM 2468 CA ALA A 422 -53.449-113.668 268.848 1.00152.33 C
ANISOU 2468 CA ALA A 422 18816 18127 20937 3850 3677 1133 C
ATOM 2469 C ALA A 422 -52.520-112.568 269.348 1.00155.87 C
ANISOU 2469 C ALA A 422 20030 18253 20941 4167 3178 456 C
ATOM 2470 O ALA A 422 -52.382-111.522 268.704 1.00157.24 O
ANISOU 2470 O ALA A 422 20359 18094 21289 4103 2881 53 O
ATOM 2471 CB ALA A 422 -52.919-114.277 267.553 1.00144.69 C
ANISOU 2471 CB ALA A 422 17414 16837 20726 2999 3379 1095 C
ATOM 2472 N GLU A 423 -51.884-112.802 270.494 1.00158.05 N
ANISOU 2472 N GLU A 423 20775 18605 20673 4502 3040 355 N
ATOM 2473 CA GLU A 423 -51.028-111.794 271.112 1.00161.83 C
ANISOU 2473 CA GLU A 423 22029 18759 20702 4841 2472 -293 C
ATOM 2474 C GLU A 423 -49.772-111.600 270.273 1.00159.86 C
ANISOU 2474 C GLU A 423 21757 17942 21042 4125 1799 -659 C
ATOM 2475 O GLU A 423 -48.900-112.474 270.234 1.00154.63 O
ANISOU 2475 O GLU A 423 20931 17209 20611 3680 1599 -546 O
ATOM 2476 CB GLU A 423 -50.667-112.203 272.536 1.00165.48 C
ANISOU 2476 CB GLU A 423 22971 19496 20409 5373 2461 -269 C
ATOM 2477 CG GLU A 423 -49.865-111.150 273.288 1.00169.24 C
ANISOU 2477 CG GLU A 423 24324 19631 20348 5803 1792 -980 C
ATOM 2478 CD GLU A 423 -49.414-111.619 274.656 1.00173.03 C
ANISOU 2478 CD GLU A 423 25293 20402 20048 6304 1701 -972 C
ATOM 2479 OE1 GLU A 423 -48.209-111.495 274.961 1.00171.48 O
ANISOU 2479 OE1 GLU A 423 25487 19845 19824 6099 978 -1370 O
ATOM 2480 OE2 GLU A 423 -50.263-112.117 275.425 1.00178.00 O
ANISOU 2480 OE2 GLU A 423 25882 21646 20103 6912 2349 -511 O
ATOM 2481 N ILE A 424 -49.677-110.455 269.600 1.00165.79 N
ANISOU 2481 N ILE A 424 22638 18297 22056 4042 1469 -1036 N
ATOM 2482 CA ILE A 424 -48.475-110.089 268.854 1.00168.38 C
ANISOU 2482 CA ILE A 424 22943 18099 22934 3444 826 -1318 C
ATOM 2483 C ILE A 424 -47.492-109.497 269.860 1.00183.00 C
ANISOU 2483 C ILE A 424 25500 19624 24409 3709 156 -1783 C
ATOM 2484 O ILE A 424 -47.649-108.359 270.305 1.00187.99 O
ANISOU 2484 O ILE A 424 26688 20000 24739 4178 -141 -2205 O
ATOM 2485 CB ILE A 424 -48.779-109.118 267.713 1.00161.95 C
ANISOU 2485 CB ILE A 424 21924 17002 22607 3237 744 -1427 C
ATOM 2486 CG1 ILE A 424 -49.760-109.754 266.726 1.00156.09 C
ANISOU 2486 CG1 ILE A 424 20498 16607 22204 2979 1335 -979 C
ATOM 2487 CG2 ILE A 424 -47.498-108.712 267.002 1.00156.85 C
ANISOU 2487 CG2 ILE A 424 21212 15853 22529 2668 104 -1606 C
ATOM 2488 CD1 ILE A 424 -49.993-108.934 265.476 1.00153.40 C
ANISOU 2488 CD1 ILE A 424 19881 16047 22359 2717 1256 -1016 C
ATOM 2489 N VAL A 425 -46.470-110.274 270.225 1.00191.46 N
ANISOU 2489 N VAL A 425 26563 20674 25510 3421 -131 -1718 N
ATOM 2490 CA VAL A 425 -45.572-109.865 271.300 1.00197.58 C
ANISOU 2490 CA VAL A 425 27998 21205 25870 3689 -796 -2115 C
ATOM 2491 C VAL A 425 -44.659-108.734 270.842 1.00195.10 C
ANISOU 2491 C VAL A 425 27866 20212 26052 3366 -1613 -2510 C
ATOM 2492 O VAL A 425 -44.365-107.808 271.608 1.00202.61 O
ANISOU 2492 O VAL A 425 29496 20813 26673 3745 -2222 -2998 O
ATOM 2493 CB VAL A 425 -44.768-111.073 271.812 1.00200.95 C
ANISOU 2493 CB VAL A 425 28296 21835 26219 3470 -852 -1851 C
ATOM 2494 CG1 VAL A 425 -44.031-110.710 273.087 1.00208.21 C
ANISOU 2494 CG1 VAL A 425 29944 22618 26547 3874 -1500 -2236 C
ATOM 2495 CG2 VAL A 425 -45.688-112.262 272.042 1.00202.74 C
ANISOU 2495 CG2 VAL A 425 28177 22668 26187 3650 -29 -1325 C
ATOM 2496 N GLN A 426 -44.194-108.787 269.596 1.00184.93 N
ANISOU 2496 N GLN A 426 25982 18717 25566 2688 -1666 -2286 N
ATOM 2497 CA GLN A 426 -43.337-107.744 269.052 1.00182.49 C
ANISOU 2497 CA GLN A 426 25696 17789 25852 2328 -2385 -2492 C
ATOM 2498 C GLN A 426 -43.724-107.481 267.604 1.00177.27 C
ANISOU 2498 C GLN A 426 24438 17099 25816 1947 -2055 -2225 C
ATOM 2499 O GLN A 426 -44.309-108.334 266.930 1.00169.70 O
ANISOU 2499 O GLN A 426 22982 16568 24930 1797 -1400 -1877 O
ATOM 2500 CB GLN A 426 -41.851-108.120 269.155 1.00181.55 C
ANISOU 2500 CB GLN A 426 25442 17435 26102 1852 -2995 -2399 C
ATOM 2501 CG GLN A 426 -40.898-106.955 268.916 1.00182.44 C
ANISOU 2501 CG GLN A 426 25657 16856 26805 1546 -3889 -2589 C
ATOM 2502 CD GLN A 426 -39.445-107.352 269.049 1.00179.63 C
ANISOU 2502 CD GLN A 426 25086 16313 26850 1086 -4482 -2404 C
ATOM 2503 OE1 GLN A 426 -39.129-108.402 269.601 1.00177.03 O
ANISOU 2503 OE1 GLN A 426 24729 16330 26204 1117 -4327 -2265 O
ATOM 2504 NE2 GLN A 426 -38.551-106.513 268.538 1.00179.83 N
ANISOU 2504 NE2 GLN A 426 24912 15788 27627 655 -5163 -2331 N
ATOM 2505 N ASP A 427 -43.389-106.281 267.133 1.00179.14 N
ANISOU 2505 N ASP A 427 24741 16804 26519 1799 -2568 -2383 N
ATOM 2506 CA ASP A 427 -43.720-105.865 265.779 1.00175.21 C
ANISOU 2506 CA ASP A 427 23719 16265 26587 1491 -2317 -2118 C
ATOM 2507 C ASP A 427 -43.075-106.791 264.750 1.00164.38 C
ANISOU 2507 C ASP A 427 21634 15141 25683 920 -2084 -1649 C
ATOM 2508 O ASP A 427 -42.132-107.533 265.038 1.00163.46 O
ANISOU 2508 O ASP A 427 21417 15067 25622 691 -2275 -1535 O
ATOM 2509 CB ASP A 427 -43.268-104.425 265.536 1.00181.99 C
ANISOU 2509 CB ASP A 427 24759 16438 27951 1392 -3011 -2295 C
ATOM 2510 CG ASP A 427 -43.891-103.445 266.512 1.00191.34 C
ANISOU 2510 CG ASP A 427 26730 17294 28676 2026 -3304 -2839 C
ATOM 2511 OD1 ASP A 427 -45.010-103.714 266.996 1.00193.43 O
ANISOU 2511 OD1 ASP A 427 27239 17974 28280 2581 -2728 -2961 O
ATOM 2512 OD2 ASP A 427 -43.260-102.404 266.792 1.00196.99 O
ANISOU 2512 OD2 ASP A 427 27815 17322 29709 1994 -4126 -3125 O
ATOM 2513 N GLY A 428 -43.598-106.733 263.528 1.00154.25 N
ANISOU 2513 N GLY A 428 19868 14032 24707 741 -1673 -1380 N
ATOM 2514 CA GLY A 428 -43.087-107.585 262.471 1.00145.72 C
ANISOU 2514 CA GLY A 428 18168 13221 23977 316 -1416 -982 C
ATOM 2515 C GLY A 428 -41.734-107.110 261.970 1.00146.35 C
ANISOU 2515 C GLY A 428 17974 12958 24673 -82 -1939 -755 C
ATOM 2516 O GLY A 428 -41.468-105.911 261.868 1.00154.65 O
ANISOU 2516 O GLY A 428 19111 13556 26092 -139 -2405 -783 O
ATOM 2517 N LEU A 429 -40.868-108.071 261.657 1.00139.33 N
ANISOU 2517 N LEU A 429 16723 12276 23941 -347 -1864 -481 N
ATOM 2518 CA LEU A 429 -39.556-107.757 261.106 1.00137.39 C
ANISOU 2518 CA LEU A 429 16084 11814 24305 -706 -2260 -122 C
ATOM 2519 C LEU A 429 -39.681-107.484 259.613 1.00130.99 C
ANISOU 2519 C LEU A 429 14733 11192 23846 -852 -1934 263 C
ATOM 2520 O LEU A 429 -40.342-108.231 258.886 1.00127.73 O
ANISOU 2520 O LEU A 429 14116 11223 23191 -774 -1356 318 O
ATOM 2521 CB LEU A 429 -38.577-108.902 261.363 1.00136.98 C
ANISOU 2521 CB LEU A 429 15844 11949 24255 -847 -2262 57 C
ATOM 2522 CG LEU A 429 -37.138-108.685 260.889 1.00137.11 C
ANISOU 2522 CG LEU A 429 15384 11801 24910 -1182 -2645 521 C
ATOM 2523 CD1 LEU A 429 -36.571-107.398 261.463 1.00138.68 C
ANISOU 2523 CD1 LEU A 429 15775 11386 25529 -1329 -3464 474 C
ATOM 2524 CD2 LEU A 429 -36.270-109.871 261.274 1.00140.46 C
ANISOU 2524 CD2 LEU A 429 15671 12427 25270 -1238 -2613 666 C
ATOM 2525 N ARG A 430 -39.052-106.405 259.156 1.00132.27 N
ANISOU 2525 N ARG A 430 14663 11005 24590 -1057 -2343 550 N
ATOM 2526 CA ARG A 430 -39.200-105.940 257.783 1.00130.57 C
ANISOU 2526 CA ARG A 430 13957 10959 24694 -1143 -2068 967 C
ATOM 2527 C ARG A 430 -37.818-105.729 257.185 1.00132.84 C
ANISOU 2527 C ARG A 430 13679 11171 25622 -1445 -2328 1582 C
ATOM 2528 O ARG A 430 -37.034-104.925 257.700 1.00134.49 O
ANISOU 2528 O ARG A 430 13904 10852 26343 -1657 -2993 1705 O
ATOM 2529 CB ARG A 430 -40.023-104.651 257.743 1.00131.81 C
ANISOU 2529 CB ARG A 430 14340 10763 24979 -1034 -2242 823 C
ATOM 2530 CG ARG A 430 -41.333-104.764 258.509 1.00133.45 C
ANISOU 2530 CG ARG A 430 15109 11025 24572 -670 -2019 258 C
ATOM 2531 CD ARG A 430 -41.900-103.407 258.873 1.00140.97 C
ANISOU 2531 CD ARG A 430 16435 11464 25664 -495 -2374 23 C
ATOM 2532 NE ARG A 430 -42.909-102.958 257.920 1.00140.66 N
ANISOU 2532 NE ARG A 430 16184 11629 25631 -370 -1959 171 N
ATOM 2533 CZ ARG A 430 -44.206-103.223 258.031 1.00136.67 C
ANISOU 2533 CZ ARG A 430 15873 11434 24622 -42 -1491 -82 C
ATOM 2534 NH1 ARG A 430 -44.653-103.940 259.054 1.00132.75 N
ANISOU 2534 NH1 ARG A 430 15769 11094 23575 208 -1336 -455 N
ATOM 2535 NH2 ARG A 430 -45.057-102.772 257.120 1.00136.56 N
ANISOU 2535 NH2 ARG A 430 15616 11598 24673 45 -1177 105 N
ATOM 2536 N ILE A 431 -37.522-106.446 256.102 1.00134.95 N
ANISOU 2536 N ILE A 431 13444 11963 25867 -1438 -1829 1985 N
ATOM 2537 CA ILE A 431 -36.204-106.431 255.478 1.00142.54 C
ANISOU 2537 CA ILE A 431 13791 13010 27358 -1628 -1923 2666 C
ATOM 2538 C ILE A 431 -36.349-106.073 254.003 1.00147.12 C
ANISOU 2538 C ILE A 431 13861 13967 28072 -1553 -1502 3188 C
ATOM 2539 O ILE A 431 -37.317-106.476 253.349 1.00138.03 O
ANISOU 2539 O ILE A 431 12796 13220 26428 -1319 -996 2979 O
ATOM 2540 CB ILE A 431 -35.490-107.792 255.647 1.00139.88 C
ANISOU 2540 CB ILE A 431 13339 13016 26791 -1571 -1695 2701 C
ATOM 2541 CG1 ILE A 431 -35.368-108.153 257.129 1.00142.64 C
ANISOU 2541 CG1 ILE A 431 14193 13038 26965 -1619 -2107 2227 C
ATOM 2542 CG2 ILE A 431 -34.118-107.774 255.001 1.00137.74 C
ANISOU 2542 CG2 ILE A 431 12381 12889 27065 -1697 -1735 3476 C
ATOM 2543 CD1 ILE A 431 -34.561-107.157 257.938 1.00149.57 C
ANISOU 2543 CD1 ILE A 431 15118 13301 28411 -1895 -2934 2343 C
ATOM 2544 N ASP A 432 -35.390-105.305 253.485 1.00161.67 N
ANISOU 2544 N ASP A 432 15150 15681 30598 -1750 -1742 3912 N
ATOM 2545 CA ASP A 432 -35.311-104.963 252.072 1.00169.98 C
ANISOU 2545 CA ASP A 432 15625 17157 31801 -1645 -1334 4577 C
ATOM 2546 C ASP A 432 -34.031-105.530 251.475 1.00175.13 C
ANISOU 2546 C ASP A 432 15639 18224 32677 -1609 -1113 5290 C
ATOM 2547 O ASP A 432 -33.010-105.644 252.158 1.00174.05 O
ANISOU 2547 O ASP A 432 15453 17863 32817 -1745 -1504 5441 O
ATOM 2548 CB ASP A 432 -35.342-103.449 251.844 1.00177.88 C
ANISOU 2548 CB ASP A 432 16429 17697 33460 -1845 -1737 4991 C
ATOM 2549 CG ASP A 432 -34.494-102.686 252.846 1.00185.95 C
ANISOU 2549 CG ASP A 432 17600 18113 34940 -2052 -2560 4992 C
ATOM 2550 OD1 ASP A 432 -34.027-103.307 253.824 1.00185.14 O
ANISOU 2550 OD1 ASP A 432 17748 17853 34743 -2141 -2833 4654 O
ATOM 2551 OD2 ASP A 432 -34.311-101.463 252.664 1.00191.94 O
ANISOU 2551 OD2 ASP A 432 18212 18564 36153 -2118 -2962 5321 O
ATOM 2552 N GLY A 433 -34.091-105.866 250.191 1.00183.38 N
ANISOU 2552 N GLY A 433 16314 19940 33421 -1290 -491 5683 N
ATOM 2553 CA GLY A 433 -32.921-106.406 249.519 1.00189.50 C
ANISOU 2553 CA GLY A 433 16676 21202 34122 -1040 -190 6311 C
ATOM 2554 C GLY A 433 -32.564-107.772 250.061 1.00189.09 C
ANISOU 2554 C GLY A 433 16710 21320 33814 -952 -31 5957 C
ATOM 2555 O GLY A 433 -33.404-108.673 250.141 1.00185.08 O
ANISOU 2555 O GLY A 433 16673 20991 32657 -747 247 5249 O
ATOM 2556 N ASP A 434 -31.305-107.925 250.461 1.00190.02 N
ANISOU 2556 N ASP A 434 16634 21336 34229 -1019 -268 6366 N
ATOM 2557 CA ASP A 434 -30.841-109.197 250.995 1.00188.34 C
ANISOU 2557 CA ASP A 434 16455 21264 33841 -923 -141 6122 C
ATOM 2558 C ASP A 434 -30.696-109.122 252.507 1.00182.05 C
ANISOU 2558 C ASP A 434 15964 19824 33382 -1338 -815 5723 C
ATOM 2559 O ASP A 434 -30.105-108.160 253.030 1.00184.53 O
ANISOU 2559 O ASP A 434 16263 19678 34171 -1605 -1435 5993 O
ATOM 2560 CB ASP A 434 -29.507-109.597 250.369 1.00197.56 C
ANISOU 2560 CB ASP A 434 17203 22843 35017 -636 133 6868 C
ATOM 2561 CG ASP A 434 -29.641-109.982 248.902 1.00202.90 C
ANISOU 2561 CG ASP A 434 17708 24253 35130 -96 871 7136 C
ATOM 2562 OD1 ASP A 434 -30.772-110.282 248.458 1.00200.77 O
ANISOU 2562 OD1 ASP A 434 17655 24215 34411 97 1183 6617 O
ATOM 2563 OD2 ASP A 434 -28.611-109.993 248.198 1.00209.46 O
ANISOU 2563 OD2 ASP A 434 18204 25436 35944 160 1120 7869 O
ATOM 2564 N PRO A 435 -31.201-110.119 253.234 1.00173.92 N
ANISOU 2564 N PRO A 435 15485 18759 31836 -1248 -750 4984 N
ATOM 2565 CA PRO A 435 -31.036-110.145 254.691 1.00170.64 C
ANISOU 2565 CA PRO A 435 15461 17820 31554 -1533 -1355 4592 C
ATOM 2566 C PRO A 435 -29.654-110.580 255.141 1.00170.46 C
ANISOU 2566 C PRO A 435 15038 17779 31949 -1630 -1604 5071 C
ATOM 2567 O PRO A 435 -29.410-110.649 256.350 1.00170.82 O
ANISOU 2567 O PRO A 435 15389 17430 32085 -1844 -2145 4787 O
ATOM 2568 CB PRO A 435 -32.103-111.161 255.142 1.00168.39 C
ANISOU 2568 CB PRO A 435 15840 17630 30510 -1320 -1062 3761 C
ATOM 2569 CG PRO A 435 -32.784-111.666 253.873 1.00167.11 C
ANISOU 2569 CG PRO A 435 15614 17988 29890 -968 -377 3708 C
ATOM 2570 CD PRO A 435 -31.896-111.313 252.735 1.00170.47 C
ANISOU 2570 CD PRO A 435 15350 18767 30653 -846 -144 4511 C
ATOM 2571 N ARG A 436 -28.755-110.882 254.202 1.00171.11 N
ANISOU 2571 N ARG A 436 14462 18317 32235 -1422 -1210 5804 N
ATOM 2572 CA ARG A 436 -27.401-111.278 254.565 1.00173.70 C
ANISOU 2572 CA ARG A 436 14490 18671 32836 -1409 -1402 6301 C
ATOM 2573 C ARG A 436 -26.620-110.111 255.150 1.00175.41 C
ANISOU 2573 C ARG A 436 14642 18387 33617 -1749 -2197 6687 C
ATOM 2574 O ARG A 436 -25.762-110.311 256.016 1.00176.67 O
ANISOU 2574 O ARG A 436 14758 18322 34047 -1905 -2672 6817 O
ATOM 2575 CB ARG A 436 -26.687-111.851 253.340 1.00179.08 C
ANISOU 2575 CB ARG A 436 14723 19990 33327 -941 -705 6932 C
ATOM 2576 CG ARG A 436 -27.594-112.716 252.478 1.00178.57 C
ANISOU 2576 CG ARG A 436 14764 20429 32654 -499 39 6525 C
ATOM 2577 CD ARG A 436 -26.860-113.345 251.308 1.00185.31 C
ANISOU 2577 CD ARG A 436 15310 21922 33178 65 700 7049 C
ATOM 2578 NE ARG A 436 -27.790-114.027 250.412 1.00185.06 N
ANISOU 2578 NE ARG A 436 15462 22331 32522 542 1308 6597 N
ATOM 2579 CZ ARG A 436 -28.244-115.262 250.605 1.00184.12 C
ANISOU 2579 CZ ARG A 436 15759 22263 31935 822 1536 5929 C
ATOM 2580 NH1 ARG A 436 -29.094-115.800 249.740 1.00181.45 N
ANISOU 2580 NH1 ARG A 436 15781 22229 30930 1235 1964 5450 N
ATOM 2581 NH2 ARG A 436 -27.851-115.959 251.661 1.00185.50 N
ANISOU 2581 NH2 ARG A 436 16112 22134 32233 678 1273 5708 N
ATOM 2582 N ALA A 437 -26.897-108.892 254.688 1.00177.49 N
ANISOU 2582 N ALA A 437 14884 18465 34091 -1843 -2385 6883 N
ATOM 2583 CA ALA A 437 -26.340-107.707 255.322 1.00182.91 C
ANISOU 2583 CA ALA A 437 15569 18587 35339 -2147 -3243 7106 C
ATOM 2584 C ALA A 437 -27.106-107.316 256.576 1.00184.38 C
ANISOU 2584 C ALA A 437 16395 18216 35446 -2413 -3902 6242 C
ATOM 2585 O ALA A 437 -26.550-106.625 257.437 1.00190.84 O
ANISOU 2585 O ALA A 437 17322 18552 36635 -2641 -4726 6246 O
ATOM 2586 CB ALA A 437 -26.327-106.536 254.338 1.00184.38 C
ANISOU 2586 CB ALA A 437 15458 18766 35831 -2108 -3211 7685 C
ATOM 2587 N ALA A 438 -28.362-107.747 256.698 1.00180.03 N
ANISOU 2587 N ALA A 438 16300 17712 34393 -2358 -3563 5513 N
ATOM 2588 CA ALA A 438 -29.197-107.447 257.853 1.00181.58 C
ANISOU 2588 CA ALA A 438 17209 17408 34376 -2515 -4064 4683 C
ATOM 2589 C ALA A 438 -29.253-108.603 258.845 1.00179.48 C
ANISOU 2589 C ALA A 438 17288 17124 33783 -2528 -4082 4210 C
ATOM 2590 O ALA A 438 -30.250-108.757 259.560 1.00176.52 O
ANISOU 2590 O ALA A 438 17585 16564 32919 -2457 -4108 3474 O
ATOM 2591 CB ALA A 438 -30.607-107.066 257.402 1.00179.54 C
ANISOU 2591 CB ALA A 438 17281 17130 33807 -2426 -3704 4240 C
ATOM 2592 N ARG A 439 -28.201-109.426 258.899 1.00182.45 N
ANISOU 2592 N ARG A 439 17258 17749 34313 -2509 -4018 4642 N
ATOM 2593 CA ARG A 439 -28.175-110.528 259.856 1.00182.66 C
ANISOU 2593 CA ARG A 439 17621 17802 33981 -2454 -4042 4243 C
ATOM 2594 C ARG A 439 -28.209-110.024 261.292 1.00184.47 C
ANISOU 2594 C ARG A 439 18442 17468 34181 -2650 -4926 3748 C
ATOM 2595 O ARG A 439 -28.780-110.685 262.168 1.00182.68 O
ANISOU 2595 O ARG A 439 18831 17284 33294 -2449 -4866 3145 O
ATOM 2596 CB ARG A 439 -26.935-111.397 259.636 1.00187.43 C
ANISOU 2596 CB ARG A 439 17596 18737 34881 -2406 -3874 4891 C
ATOM 2597 CG ARG A 439 -26.939-112.196 258.344 1.00189.20 C
ANISOU 2597 CG ARG A 439 17403 19590 34895 -2032 -2929 5225 C
ATOM 2598 CD ARG A 439 -25.795-113.202 258.321 1.00195.86 C
ANISOU 2598 CD ARG A 439 17765 20746 35905 -1871 -2740 5737 C
ATOM 2599 NE ARG A 439 -24.493-112.560 258.484 1.00209.45 N
ANISOU 2599 NE ARG A 439 19058 22306 38218 -2054 -3275 6453 N
ATOM 2600 CZ ARG A 439 -23.723-112.162 257.476 1.00217.61 C
ANISOU 2600 CZ ARG A 439 19611 23584 39486 -1897 -3001 7226 C
ATOM 2601 NH1 ARG A 439 -22.553-111.586 257.718 1.00222.07 N
ANISOU 2601 NH1 ARG A 439 19883 23932 40561 -2065 -3515 7874 N
ATOM 2602 NH2 ARG A 439 -24.124-112.339 256.225 1.00218.95 N
ANISOU 2602 NH2 ARG A 439 19613 24212 39367 -1563 -2223 7372 N
ATOM 2603 N ASP A 440 -27.609-108.861 261.552 1.00189.19 N
ANISOU 2603 N ASP A 440 18964 17668 35252 -2864 -5691 3962 N
ATOM 2604 CA ASP A 440 -27.599-108.316 262.906 1.00193.18 C
ANISOU 2604 CA ASP A 440 20090 17632 35676 -2983 -6614 3442 C
ATOM 2605 C ASP A 440 -29.007-107.945 263.357 1.00190.59 C
ANISOU 2605 C ASP A 440 20565 17021 34828 -2847 -6601 2606 C
ATOM 2606 O ASP A 440 -29.408-108.251 264.486 1.00190.97 O
ANISOU 2606 O ASP A 440 21301 16939 34320 -2684 -6863 1991 O
ATOM 2607 CB ASP A 440 -26.671-107.104 262.975 1.00201.99 C
ANISOU 2607 CB ASP A 440 20973 18410 37363 -3149 -7407 3853 C
ATOM 2608 CG ASP A 440 -25.262-107.422 262.512 1.00207.79 C
ANISOU 2608 CG ASP A 440 20919 19388 38645 -3229 -7393 4775 C
ATOM 2609 OD1 ASP A 440 -24.853-108.597 262.616 1.00206.37 O
ANISOU 2609 OD1 ASP A 440 20520 19538 38353 -3178 -7054 4944 O
ATOM 2610 OD2 ASP A 440 -24.563-106.497 262.044 1.00214.44 O
ANISOU 2610 OD2 ASP A 440 21358 20071 40050 -3318 -7714 5367 O
ATOM 2611 N ASP A 441 -29.773-107.285 262.485 1.00189.27 N
ANISOU 2611 N ASP A 441 20354 16901 34660 -2764 -6207 2597 N
ATOM 2612 CA ASP A 441 -31.145-106.932 262.834 1.00186.26 C
ANISOU 2612 CA ASP A 441 20697 16307 33768 -2552 -6098 1867 C
ATOM 2613 C ASP A 441 -32.030-108.167 262.941 1.00179.07 C
ANISOU 2613 C ASP A 441 20088 15978 31972 -2165 -5250 1495 C
ATOM 2614 O ASP A 441 -33.015-108.159 263.689 1.00181.05 O
ANISOU 2614 O ASP A 441 21022 16193 31576 -1873 -5196 870 O
ATOM 2615 CB ASP A 441 -31.717-105.957 261.805 1.00187.42 C
ANISOU 2615 CB ASP A 441 20640 16441 34130 -2537 -5843 2033 C
ATOM 2616 CG ASP A 441 -30.878-104.702 261.663 1.00196.74 C
ANISOU 2616 CG ASP A 441 21527 17344 35882 -2708 -6518 2436 C
ATOM 2617 OD1 ASP A 441 -30.153-104.357 262.621 1.00204.14 O
ANISOU 2617 OD1 ASP A 441 22677 17922 36966 -2810 -7343 2329 O
ATOM 2618 OD2 ASP A 441 -30.944-104.060 260.594 1.00198.23 O
ANISOU 2618 OD2 ASP A 441 21270 17654 36393 -2729 -6254 2881 O
ATOM 2619 N ILE A 442 -31.699-109.231 262.209 1.00170.74 N
ANISOU 2619 N ILE A 442 18529 15446 30898 -2131 -4599 1895 N
ATOM 2620 CA ILE A 442 -32.487-110.459 262.273 1.00161.94 C
ANISOU 2620 CA ILE A 442 17659 14801 29069 -1814 -3871 1588 C
ATOM 2621 C ILE A 442 -32.334-111.116 263.639 1.00163.16 C
ANISOU 2621 C ILE A 442 18281 14913 28798 -1696 -4163 1263 C
ATOM 2622 O ILE A 442 -33.322-111.370 264.339 1.00162.65 O
ANISOU 2622 O ILE A 442 18785 14920 28093 -1423 -3979 769 O
ATOM 2623 CB ILE A 442 -32.083-111.418 261.141 1.00157.34 C
ANISOU 2623 CB ILE A 442 16472 14707 28604 -1769 -3202 2058 C
ATOM 2624 CG1 ILE A 442 -32.592-110.899 259.797 1.00151.03 C
ANISOU 2624 CG1 ILE A 442 15355 14082 27949 -1744 -2765 2260 C
ATOM 2625 CG2 ILE A 442 -32.612-112.816 261.411 1.00156.93 C
ANISOU 2625 CG2 ILE A 442 16666 15003 27958 -1505 -2660 1776 C
ATOM 2626 CD1 ILE A 442 -32.246-111.796 258.638 1.00149.01 C
ANISOU 2626 CD1 ILE A 442 14590 14331 27696 -1593 -2117 2657 C
ATOM 2627 N VAL A 443 -31.092-111.401 264.037 1.00163.84 N
ANISOU 2627 N VAL A 443 18095 14921 29236 -1876 -4608 1603 N
ATOM 2628 CA VAL A 443 -30.854-111.975 265.356 1.00162.74 C
ANISOU 2628 CA VAL A 443 18384 14750 28702 -1762 -4960 1348 C
ATOM 2629 C VAL A 443 -31.214-110.991 266.458 1.00166.09 C
ANISOU 2629 C VAL A 443 19507 14737 28862 -1693 -5694 813 C
ATOM 2630 O VAL A 443 -31.491-111.407 267.589 1.00168.14 O
ANISOU 2630 O VAL A 443 20321 15058 28505 -1433 -5830 443 O
ATOM 2631 CB VAL A 443 -29.391-112.439 265.494 1.00163.12 C
ANISOU 2631 CB VAL A 443 17927 14805 29245 -1979 -5328 1885 C
ATOM 2632 CG1 VAL A 443 -29.049-113.440 264.402 1.00159.08 C
ANISOU 2632 CG1 VAL A 443 16784 14741 28917 -1922 -4557 2375 C
ATOM 2633 CG2 VAL A 443 -28.443-111.250 265.453 1.00168.23 C
ANISOU 2633 CG2 VAL A 443 18265 14980 30677 -2364 -6200 2210 C
ATOM 2634 N GLY A 444 -31.219-109.691 266.158 1.00165.47 N
ANISOU 2634 N GLY A 444 19438 14215 29220 -1875 -6176 772 N
ATOM 2635 CA GLY A 444 -31.688-108.723 267.135 1.00169.19 C
ANISOU 2635 CA GLY A 444 20667 14228 29389 -1716 -6850 167 C
ATOM 2636 C GLY A 444 -33.184-108.820 267.359 1.00164.04 C
ANISOU 2636 C GLY A 444 20591 13815 27922 -1248 -6231 -364 C
ATOM 2637 O GLY A 444 -33.650-108.903 268.499 1.00165.52 O
ANISOU 2637 O GLY A 444 21467 14014 27408 -875 -6402 -850 O
ATOM 2638 N TRP A 445 -33.959-108.819 266.271 1.00160.31 N
ANISOU 2638 N TRP A 445 19818 13576 27515 -1230 -5495 -231 N
ATOM 2639 CA TRP A 445 -35.403-108.980 266.396 1.00157.07 C
ANISOU 2639 CA TRP A 445 19827 13438 26413 -814 -4862 -624 C
ATOM 2640 C TRP A 445 -35.767-110.353 266.943 1.00153.16 C
ANISOU 2640 C TRP A 445 19449 13450 25297 -561 -4305 -653 C
ATOM 2641 O TRP A 445 -36.778-110.496 267.640 1.00152.71 O
ANISOU 2641 O TRP A 445 19887 13571 24566 -150 -4025 -995 O
ATOM 2642 CB TRP A 445 -36.080-108.754 265.043 1.00153.27 C
ANISOU 2642 CB TRP A 445 18923 13119 26192 -894 -4247 -412 C
ATOM 2643 CG TRP A 445 -37.566-108.935 265.089 1.00153.29 C
ANISOU 2643 CG TRP A 445 19245 13416 25583 -510 -3606 -725 C
ATOM 2644 CD1 TRP A 445 -38.500-107.978 265.354 1.00157.29 C
ANISOU 2644 CD1 TRP A 445 20199 13716 25847 -223 -3676 -1097 C
ATOM 2645 CD2 TRP A 445 -38.290-110.153 264.871 1.00151.52 C
ANISOU 2645 CD2 TRP A 445 18883 13722 24967 -364 -2825 -648 C
ATOM 2646 NE1 TRP A 445 -39.761-108.522 265.312 1.00155.17 N
ANISOU 2646 NE1 TRP A 445 20024 13874 25059 93 -2948 -1200 N
ATOM 2647 CE2 TRP A 445 -39.659-109.856 265.018 1.00151.58 C
ANISOU 2647 CE2 TRP A 445 19207 13852 24536 -21 -2451 -923 C
ATOM 2648 CE3 TRP A 445 -37.913-111.464 264.566 1.00151.00 C
ANISOU 2648 CE3 TRP A 445 18452 14000 24923 -481 -2438 -360 C
ATOM 2649 CZ2 TRP A 445 -40.652-110.821 264.871 1.00149.27 C
ANISOU 2649 CZ2 TRP A 445 18820 14009 23888 146 -1743 -865 C
ATOM 2650 CZ3 TRP A 445 -38.901-112.421 264.419 1.00149.34 C
ANISOU 2650 CZ3 TRP A 445 18216 14174 24354 -309 -1771 -372 C
ATOM 2651 CH2 TRP A 445 -40.254-112.095 264.570 1.00148.91 C
ANISOU 2651 CH2 TRP A 445 18425 14229 23924 -29 -1448 -597 C
ATOM 2652 N ALA A 446 -34.959-111.370 266.643 1.00150.25 N
ANISOU 2652 N ALA A 446 18608 13314 25166 -770 -4127 -248 N
ATOM 2653 CA ALA A 446 -35.246-112.713 267.131 1.00147.34 C
ANISOU 2653 CA ALA A 446 18312 13356 24316 -561 -3636 -218 C
ATOM 2654 C ALA A 446 -34.906-112.855 268.611 1.00148.88 C
ANISOU 2654 C ALA A 446 19024 13494 24048 -346 -4139 -430 C
ATOM 2655 O ALA A 446 -35.613-113.551 269.348 1.00147.69 O
ANISOU 2655 O ALA A 446 19199 13645 23271 -3 -3773 -553 O
ATOM 2656 CB ALA A 446 -34.487-113.744 266.297 1.00145.74 C
ANISOU 2656 CB ALA A 446 17472 13375 24526 -794 -3293 257 C
ATOM 2657 N HIS A 447 -33.831-112.206 269.064 1.00153.99 N
ANISOU 2657 N HIS A 447 19736 13771 25005 -535 -5002 -434 N
ATOM 2658 CA HIS A 447 -33.535-112.197 270.492 1.00161.90 C
ANISOU 2658 CA HIS A 447 21319 14698 25498 -288 -5602 -711 C
ATOM 2659 C HIS A 447 -34.504-111.304 271.256 1.00166.05 C
ANISOU 2659 C HIS A 447 22627 15083 25382 161 -5795 -1306 C
ATOM 2660 O HIS A 447 -34.785-111.562 272.432 1.00168.61 O
ANISOU 2660 O HIS A 447 23529 15586 24949 600 -5899 -1573 O
ATOM 2661 CB HIS A 447 -32.093-111.748 270.732 1.00169.90 C
ANISOU 2661 CB HIS A 447 22154 15314 27086 -651 -6574 -539 C
ATOM 2662 CG HIS A 447 -31.757-111.541 272.177 1.00178.38 C
ANISOU 2662 CG HIS A 447 23895 16240 27642 -401 -7377 -901 C
ATOM 2663 ND1 HIS A 447 -31.796-110.303 272.780 1.00184.31 N
ANISOU 2663 ND1 HIS A 447 25258 16492 28279 -285 -8239 -1415 N
ATOM 2664 CD2 HIS A 447 -31.379-112.416 273.139 1.00181.45 C
ANISOU 2664 CD2 HIS A 447 24469 16909 27565 -206 -7482 -836 C
ATOM 2665 CE1 HIS A 447 -31.455-110.423 274.051 1.00190.83 C
ANISOU 2665 CE1 HIS A 447 26650 17318 28538 -8 -8861 -1692 C
ATOM 2666 NE2 HIS A 447 -31.197-111.695 274.294 1.00189.35 N
ANISOU 2666 NE2 HIS A 447 26196 17627 28122 40 -8399 -1317 N
ATOM 2667 N ASP A 448 -35.025-110.259 270.610 1.00166.75 N
ANISOU 2667 N ASP A 448 22749 14878 25730 118 -5820 -1495 N
ATOM 2668 CA ASP A 448 -35.981-109.379 271.276 1.00170.35 C
ANISOU 2668 CA ASP A 448 23953 15185 25587 617 -5960 -2067 C
ATOM 2669 C ASP A 448 -37.338-110.055 271.426 1.00164.12 C
ANISOU 2669 C ASP A 448 23313 14961 24084 1092 -4986 -2102 C
ATOM 2670 O ASP A 448 -37.963-109.984 272.491 1.00166.68 O
ANISOU 2670 O ASP A 448 24286 15453 23592 1678 -4970 -2442 O
ATOM 2671 CB ASP A 448 -36.114-108.064 270.507 1.00174.96 C
ANISOU 2671 CB ASP A 448 24487 15247 26742 424 -6282 -2203 C
ATOM 2672 CG ASP A 448 -34.886-107.185 270.638 1.00185.82 C
ANISOU 2672 CG ASP A 448 25861 15954 28788 33 -7422 -2225 C
ATOM 2673 OD1 ASP A 448 -34.166-107.311 271.650 1.00193.09 O
ANISOU 2673 OD1 ASP A 448 27134 16747 29483 94 -8122 -2394 O
ATOM 2674 OD2 ASP A 448 -34.642-106.365 269.727 1.00187.19 O
ANISOU 2674 OD2 ASP A 448 25653 15726 29743 -343 -7646 -2029 O
ATOM 2675 N VAL A 449 -37.817-110.713 270.366 1.00155.50 N
ANISOU 2675 N VAL A 449 21617 14177 23289 874 -4185 -1726 N
ATOM 2676 CA VAL A 449 -39.077-111.441 270.464 1.00149.76 C
ANISOU 2676 CA VAL A 449 20917 13958 22026 1237 -3311 -1657 C
ATOM 2677 C VAL A 449 -38.950-112.621 271.416 1.00150.58 C
ANISOU 2677 C VAL A 449 21132 14451 21630 1454 -3114 -1481 C
ATOM 2678 O VAL A 449 -39.954-113.077 271.975 1.00149.25 O
ANISOU 2678 O VAL A 449 21166 14681 20863 1896 -2564 -1448 O
ATOM 2679 CB VAL A 449 -39.553-111.891 269.067 1.00139.91 C
ANISOU 2679 CB VAL A 449 19004 12886 21269 909 -2637 -1319 C
ATOM 2680 CG1 VAL A 449 -38.699-113.035 268.541 1.00137.64 C
ANISOU 2680 CG1 VAL A 449 18164 12734 21398 512 -2492 -905 C
ATOM 2681 CG2 VAL A 449 -41.026-112.276 269.100 1.00135.06 C
ANISOU 2681 CG2 VAL A 449 18431 12674 20210 1266 -1869 -1289 C
ATOM 2682 N ARG A 450 -37.731-113.119 271.629 1.00155.10 N
ANISOU 2682 N ARG A 450 21537 14932 22461 1167 -3548 -1297 N
ATOM 2683 CA ARG A 450 -37.506-114.129 272.654 1.00163.66 C
ANISOU 2683 CA ARG A 450 22784 16343 23058 1403 -3482 -1131 C
ATOM 2684 C ARG A 450 -37.498-113.509 274.046 1.00180.88 C
ANISOU 2684 C ARG A 450 25764 18494 24469 1929 -4045 -1545 C
ATOM 2685 O ARG A 450 -37.986-114.119 275.004 1.00184.30 O
ANISOU 2685 O ARG A 450 26505 19347 24172 2411 -3735 -1477 O
ATOM 2686 CB ARG A 450 -36.191-114.860 272.385 1.00160.08 C
ANISOU 2686 CB ARG A 450 21859 15805 23157 951 -3759 -772 C
ATOM 2687 CG ARG A 450 -35.774-115.811 273.488 1.00160.55 C
ANISOU 2687 CG ARG A 450 22092 16138 22771 1171 -3835 -583 C
ATOM 2688 CD ARG A 450 -34.402-116.389 273.213 1.00157.71 C
ANISOU 2688 CD ARG A 450 21261 15651 23011 746 -4183 -232 C
ATOM 2689 NE ARG A 450 -33.390-115.349 273.055 1.00159.73 N
ANISOU 2689 NE ARG A 450 21498 15456 23735 440 -5056 -380 N
ATOM 2690 N GLY A 451 -36.957-112.296 274.172 1.00192.41 N
ANISOU 2690 N GLY A 451 27574 19454 26079 1873 -4894 -1962 N
ATOM 2691 CA GLY A 451 -36.911-111.649 275.474 1.00203.32 C
ANISOU 2691 CA GLY A 451 29810 20740 26702 2415 -5554 -2460 C
ATOM 2692 C GLY A 451 -38.287-111.266 275.984 1.00208.43 C
ANISOU 2692 C GLY A 451 31014 21669 26510 3155 -5050 -2769 C
ATOM 2693 O GLY A 451 -38.619-111.501 277.149 1.00217.96 O
ANISOU 2693 O GLY A 451 32785 23240 26788 3806 -5003 -2902 O
ATOM 2694 N ALA A 452 -39.106-110.671 275.121 1.00200.35 N
ANISOU 2694 N ALA A 452 29821 20523 25780 3112 -4645 -2841 N
ATOM 2695 CA ALA A 452 -40.464-110.286 275.490 1.00199.41 C
ANISOU 2695 CA ALA A 452 30128 20690 24950 3821 -4091 -3057 C
ATOM 2696 C ALA A 452 -41.338-111.534 275.522 1.00193.25 C
ANISOU 2696 C ALA A 452 28945 20615 23866 3997 -3034 -2502 C
ATOM 2697 O ALA A 452 -41.559-112.171 274.487 1.00187.51 O
ANISOU 2697 O ALA A 452 27494 19985 23766 3503 -2486 -2073 O
ATOM 2698 CB ALA A 452 -41.011-109.251 274.512 1.00193.88 C
ANISOU 2698 CB ALA A 452 29310 19610 24747 3679 -4036 -3253 C
ATOM 2699 N ILE A 453 -41.828-111.887 276.707 1.00200.09 N
ANISOU 2699 N ILE A 453 30278 21965 23782 4717 -2778 -2486 N
ATOM 2700 CA ILE A 453 -42.663-113.070 276.873 1.00199.73 C
ANISOU 2700 CA ILE A 453 29840 22580 23470 4913 -1818 -1866 C
ATOM 2701 C ILE A 453 -43.476-112.961 278.157 1.00207.62 C
ANISOU 2701 C ILE A 453 31470 24108 23310 5924 -1504 -1923 C
ATOM 2702 O ILE A 453 -43.677-113.951 278.862 1.00153.35 O
ANISOU 2702 O ILE A 453 24504 17781 15982 6211 -1052 -1434 O
ATOM 2703 CB ILE A 453 -41.818-114.357 276.873 1.00198.56 C
ANISOU 2703 CB ILE A 453 29220 22552 23671 4427 -1811 -1377 C
ATOM 2704 N ARG A 458 -38.135-124.395 282.018 1.00177.35 N
ANISOU 2704 N ARG A 458 31146 15366 20872 -3078 -6384 4226 N
ATOM 2705 CA ARG A 458 -37.471-125.481 282.728 1.00172.80 C
ANISOU 2705 CA ARG A 458 29913 15420 20325 -3245 -5786 4040 C
ATOM 2706 C ARG A 458 -38.311-125.959 283.909 1.00173.57 C
ANISOU 2706 C ARG A 458 29421 15460 21066 -2568 -5586 3587 C
ATOM 2707 O ARG A 458 -39.506-125.675 283.986 1.00177.01 O
ANISOU 2707 O ARG A 458 29885 15439 21931 -1946 -5932 3423 O
ATOM 2708 CB ARG A 458 -36.088-125.039 283.209 1.00172.25 C
ANISOU 2708 CB ARG A 458 30090 15500 19857 -3972 -5472 4175 C
ATOM 2709 N MET A 459 -37.680-126.687 284.828 1.00168.45 N
ANISOU 2709 N MET A 459 28242 15292 20470 -2697 -5035 3369 N
ATOM 2710 CA MET A 459 -38.377-127.221 285.988 1.00167.54 C
ANISOU 2710 CA MET A 459 27563 15192 20902 -2139 -4780 2953 C
ATOM 2711 C MET A 459 -37.400-127.346 287.147 1.00165.83 C
ANISOU 2711 C MET A 459 27158 15236 20612 -2449 -4296 2833 C
ATOM 2712 O MET A 459 -36.180-127.352 286.961 1.00164.81 O
ANISOU 2712 O MET A 459 27151 15447 20022 -3064 -4092 3016 O
ATOM 2713 CB MET A 459 -39.019-128.580 285.681 1.00163.70 C
ANISOU 2713 CB MET A 459 26372 15183 20644 -1761 -4602 2735 C
ATOM 2714 N ASP A 460 -37.953-127.440 288.354 1.00168.18 N
ANISOU 2714 N ASP A 460 27148 15394 21359 -2019 -4118 2498 N
ATOM 2715 CA ASP A 460 -37.149-127.647 289.556 1.00172.06 C
ANISOU 2715 CA ASP A 460 27408 16143 21825 -2220 -3657 2339 C
ATOM 2716 C ASP A 460 -36.562-129.050 289.507 1.00174.37 C
ANISOU 2716 C ASP A 460 27103 17187 21963 -2368 -3214 2263 C
ATOM 2717 O ASP A 460 -37.242-130.032 289.813 1.00170.06 O
ANISOU 2717 O ASP A 460 26016 16861 21737 -1954 -3024 2019 O
ATOM 2718 CB ASP A 460 -37.994-127.447 290.809 1.00175.66 C
ANISOU 2718 CB ASP A 460 27669 16283 22793 -1698 -3589 1989 C
ATOM 2719 CG ASP A 460 -38.447-126.011 290.985 1.00186.34 C
ANISOU 2719 CG ASP A 460 29613 16890 24298 -1560 -4024 2017 C
ATOM 2720 OD1 ASP A 460 -37.829-125.113 290.376 1.00194.37 O
ANISOU 2720 OD1 ASP A 460 31245 17637 24970 -1987 -4295 2336 O
ATOM 2721 OD2 ASP A 460 -39.417-125.780 291.739 1.00187.67 O
ANISOU 2721 OD2 ASP A 460 29637 16745 24925 -1037 -4098 1706 O
ATOM 2722 N ILE A 461 -35.289-129.152 289.116 1.00180.68 N
ANISOU 2722 N ILE A 461 27999 18386 22265 -2969 -3054 2453 N
ATOM 2723 CA ILE A 461 -34.681-130.467 288.949 1.00180.75 C
ANISOU 2723 CA ILE A 461 27464 19112 22102 -3107 -2695 2369 C
ATOM 2724 C ILE A 461 -34.529-131.170 290.291 1.00180.70 C
ANISOU 2724 C ILE A 461 26995 19342 22320 -2901 -2268 2066 C
ATOM 2725 O ILE A 461 -34.638-132.400 290.369 1.00180.90 O
ANISOU 2725 O ILE A 461 26494 19789 22451 -2708 -2022 1906 O
ATOM 2726 CB ILE A 461 -33.332-130.351 288.216 1.00181.78 C
ANISOU 2726 CB ILE A 461 27795 19644 21631 -3810 -2639 2592 C
ATOM 2727 CG1 ILE A 461 -32.339-129.520 289.029 1.00184.77 C
ANISOU 2727 CG1 ILE A 461 28476 19937 21793 -4227 -2496 2601 C
ATOM 2728 CG2 ILE A 461 -33.530-129.749 286.832 1.00184.24 C
ANISOU 2728 CG2 ILE A 461 28569 19750 21683 -4028 -3053 2911 C
ATOM 2729 CD1 ILE A 461 -30.919-129.608 288.524 1.00185.26 C
ANISOU 2729 CD1 ILE A 461 28577 20536 21278 -4923 -2329 2707 C
ATOM 2730 N GLU A 462 -34.286-130.415 291.366 1.00177.91 N
ANISOU 2730 N GLU A 462 26847 18711 22038 -2936 -2186 1983 N
ATOM 2731 CA GLU A 462 -34.204-131.031 292.686 1.00170.09 C
ANISOU 2731 CA GLU A 462 25458 17917 21251 -2721 -1801 1700 C
ATOM 2732 C GLU A 462 -35.532-131.667 293.072 1.00164.59 C
ANISOU 2732 C GLU A 462 24390 17091 21055 -2110 -1764 1474 C
ATOM 2733 O GLU A 462 -35.561-132.751 293.665 1.00162.98 O
ANISOU 2733 O GLU A 462 23722 17237 20968 -1937 -1434 1284 O
ATOM 2734 CB GLU A 462 -33.774-130.002 293.730 1.00173.20 C
ANISOU 2734 CB GLU A 462 26167 18008 21633 -2859 -1756 1643 C
ATOM 2735 CG GLU A 462 -32.270-129.781 293.802 1.00175.02 C
ANISOU 2735 CG GLU A 462 26539 18575 21384 -3459 -1587 1729 C
ATOM 2736 CD GLU A 462 -31.721-129.086 292.571 1.00180.15 C
ANISOU 2736 CD GLU A 462 27640 19172 21639 -3966 -1860 2037 C
ATOM 2737 OE1 GLU A 462 -32.435-128.237 291.999 1.00183.36 O
ANISOU 2737 OE1 GLU A 462 28471 19043 22153 -3878 -2241 2208 O
ATOM 2738 OE2 GLU A 462 -30.576-129.392 292.175 1.00180.42 O
ANISOU 2738 OE2 GLU A 462 27608 19705 21240 -4455 -1702 2096 O
ATOM 2739 N LEU A 463 -36.645-131.008 292.742 1.00162.65 N
ANISOU 2739 N LEU A 463 24351 16345 21102 -1782 -2110 1475 N
ATOM 2740 CA LEU A 463 -37.946-131.643 292.909 1.00159.13 C
ANISOU 2740 CA LEU A 463 23518 15833 21113 -1231 -2096 1235 C
ATOM 2741 C LEU A 463 -38.178-132.708 291.846 1.00159.10 C
ANISOU 2741 C LEU A 463 23195 16190 21068 -1182 -2107 1292 C
ATOM 2742 O LEU A 463 -38.856-133.707 292.109 1.00162.13 O
ANISOU 2742 O LEU A 463 23106 16763 21732 -860 -1907 1075 O
ATOM 2743 CB LEU A 463 -39.059-130.596 292.865 1.00163.13 C
ANISOU 2743 CB LEU A 463 24317 15717 21949 -866 -2495 1162 C
ATOM 2744 CG LEU A 463 -38.946-129.444 293.866 1.00167.92 C
ANISOU 2744 CG LEU A 463 25262 15900 22640 -868 -2548 1076 C
ATOM 2745 CD1 LEU A 463 -40.169-128.543 293.792 1.00172.47 C
ANISOU 2745 CD1 LEU A 463 26056 15881 23594 -415 -2973 936 C
ATOM 2746 CD2 LEU A 463 -38.745-129.971 295.280 1.00164.84 C
ANISOU 2746 CD2 LEU A 463 24507 15757 22368 -797 -2080 812 C
ATOM 2747 N ALA A 464 -37.618-132.517 290.649 1.00157.18 N
ANISOU 2747 N ALA A 464 23203 16054 20463 -1522 -2330 1573 N
ATOM 2748 CA ALA A 464 -37.735-133.531 289.607 1.00154.05 C
ANISOU 2748 CA ALA A 464 22495 16048 19988 -1509 -2338 1618 C
ATOM 2749 C ALA A 464 -36.872-134.747 289.921 1.00149.05 C
ANISOU 2749 C ALA A 464 21427 16020 19183 -1698 -1919 1532 C
ATOM 2750 O ALA A 464 -37.304-135.888 289.721 1.00149.55 O
ANISOU 2750 O ALA A 464 21040 16365 19416 -1472 -1782 1394 O
ATOM 2751 CB ALA A 464 -37.356-132.938 288.250 1.00156.72 C
ANISOU 2751 CB ALA A 464 23249 16349 19949 -1846 -2696 1939 C
ATOM 2752 N LYS A 465 -35.650-134.524 290.411 1.00145.49 N
ANISOU 2752 N LYS A 465 21108 15770 18402 -2103 -1728 1592 N
ATOM 2753 CA LYS A 465 -34.806-135.648 290.805 1.00141.73 C
ANISOU 2753 CA LYS A 465 20233 15849 17771 -2236 -1363 1471 C
ATOM 2754 C LYS A 465 -35.358-136.341 292.043 1.00134.99 C
ANISOU 2754 C LYS A 465 19035 14968 17285 -1849 -1067 1208 C
ATOM 2755 O LYS A 465 -35.246-137.566 292.175 1.00136.14 O
ANISOU 2755 O LYS A 465 18775 15484 17468 -1752 -835 1081 O
ATOM 2756 CB LYS A 465 -33.372-135.180 291.055 1.00147.57 C
ANISOU 2756 CB LYS A 465 21189 16817 18066 -2749 -1251 1554 C
ATOM 2757 CG LYS A 465 -32.429-136.305 291.453 1.00152.34 C
ANISOU 2757 CG LYS A 465 21391 18004 18487 -2864 -921 1398 C
ATOM 2758 CD LYS A 465 -31.265-135.799 292.285 1.00158.77 C
ANISOU 2758 CD LYS A 465 22362 18943 19020 -3200 -751 1356 C
ATOM 2759 CE LYS A 465 -30.462-136.959 292.854 1.00156.88 C
ANISOU 2759 CE LYS A 465 21712 19233 18663 -3193 -449 1150 C
ATOM 2760 NZ LYS A 465 -29.392-136.495 293.780 1.00158.74 N
ANISOU 2760 NZ LYS A 465 22065 19592 18655 -3456 -284 1060 N
ATOM 2761 N THR A 466 -35.949-135.573 292.964 1.00128.61 N
ANISOU 2761 N THR A 466 18400 13726 16739 -1637 -1077 1116 N
ATOM 2762 CA THR A 466 -36.553-136.175 294.150 1.00124.08 C
ANISOU 2762 CA THR A 466 17521 13126 16499 -1294 -790 860 C
ATOM 2763 C THR A 466 -37.613-137.195 293.763 1.00122.98 C
ANISOU 2763 C THR A 466 16988 13062 16678 -943 -759 730 C
ATOM 2764 O THR A 466 -37.660-138.295 294.326 1.00121.69 O
ANISOU 2764 O THR A 466 16474 13151 16613 -827 -458 581 O
ATOM 2765 CB THR A 466 -37.155-135.094 295.048 1.00124.70 C
ANISOU 2765 CB THR A 466 17840 12718 16821 -1106 -857 754 C
ATOM 2766 OG1 THR A 466 -36.141-134.148 295.406 1.00120.63 O
ANISOU 2766 OG1 THR A 466 17695 12128 16011 -1454 -883 867 O
ATOM 2767 CG2 THR A 466 -37.729-135.713 296.314 1.00127.89 C
ANISOU 2767 CG2 THR A 466 17927 13146 17517 -806 -526 481 C
ATOM 2768 N LEU A 467 -38.469-136.852 292.798 1.00123.83 N
ANISOU 2768 N LEU A 467 17162 12944 16942 -776 -1079 778 N
ATOM 2769 CA LEU A 467 -39.417-137.829 292.274 1.00121.04 C
ANISOU 2769 CA LEU A 467 16420 12706 16864 -479 -1069 646 C
ATOM 2770 C LEU A 467 -38.685-139.026 291.683 1.00118.89 C
ANISOU 2770 C LEU A 467 15871 12942 16359 -672 -921 706 C
ATOM 2771 O LEU A 467 -39.045-140.179 291.944 1.00118.90 O
ANISOU 2771 O LEU A 467 15484 13145 16549 -499 -688 540 O
ATOM 2772 CB LEU A 467 -40.324-137.178 291.230 1.00119.75 C
ANISOU 2772 CB LEU A 467 16412 12241 16845 -288 -1492 699 C
ATOM 2773 CG LEU A 467 -41.170-136.005 291.726 1.00119.77 C
ANISOU 2773 CG LEU A 467 16672 11711 17123 -21 -1709 590 C
ATOM 2774 CD1 LEU A 467 -42.161-135.574 290.658 1.00126.14 C
ANISOU 2774 CD1 LEU A 467 17572 12254 18104 248 -2147 595 C
ATOM 2775 CD2 LEU A 467 -41.885-136.365 293.021 1.00114.88 C
ANISOU 2775 CD2 LEU A 467 15745 11034 16869 271 -1396 261 C
ATOM 2776 N VAL A 468 -37.644-138.768 290.888 1.00119.75 N
ANISOU 2776 N VAL A 468 16180 13269 16050 -1047 -1055 925 N
ATOM 2777 CA VAL A 468 -36.814-139.855 290.373 1.00119.77 C
ANISOU 2777 CA VAL A 468 15912 13797 15800 -1246 -921 939 C
ATOM 2778 C VAL A 468 -36.204-140.641 291.526 1.00116.56 C
ANISOU 2778 C VAL A 468 15295 13618 15374 -1256 -553 793 C
ATOM 2779 O VAL A 468 -36.230-141.877 291.541 1.00119.36 O
ANISOU 2779 O VAL A 468 15293 14248 15810 -1140 -381 670 O
ATOM 2780 CB VAL A 468 -35.729-139.307 289.428 1.00119.62 C
ANISOU 2780 CB VAL A 468 16158 13998 15295 -1701 -1106 1165 C
ATOM 2781 CG1 VAL A 468 -34.799-140.425 288.985 1.00120.94 C
ANISOU 2781 CG1 VAL A 468 16004 14755 15194 -1900 -958 1114 C
ATOM 2782 CG2 VAL A 468 -36.363-138.631 288.225 1.00119.59 C
ANISOU 2782 CG2 VAL A 468 16387 13770 15281 -1686 -1490 1333 C
ATOM 2783 N LEU A 469 -35.656-139.931 292.515 1.00110.14 N
ANISOU 2783 N LEU A 469 14721 12675 14451 -1384 -445 800 N
ATOM 2784 CA LEU A 469 -35.084-140.597 293.681 1.00111.75 C
ANISOU 2784 CA LEU A 469 14772 13070 14616 -1372 -120 664 C
ATOM 2785 C LEU A 469 -36.134-141.424 294.410 1.00116.65 C
ANISOU 2785 C LEU A 469 15120 13564 15638 -997 87 479 C
ATOM 2786 O LEU A 469 -35.918-142.608 294.695 1.00120.18 O
ANISOU 2786 O LEU A 469 15302 14271 16089 -935 290 383 O
ATOM 2787 CB LEU A 469 -34.462-139.567 294.623 1.00117.99 C
ANISOU 2787 CB LEU A 469 15880 13700 15253 -1545 -64 687 C
ATOM 2788 CG LEU A 469 -33.950-140.115 295.957 1.00119.20 C
ANISOU 2788 CG LEU A 469 15922 14000 15368 -1497 253 539 C
ATOM 2789 CD1 LEU A 469 -32.842-141.133 295.730 1.00120.71 C
ANISOU 2789 CD1 LEU A 469 15903 14704 15258 -1661 351 507 C
ATOM 2790 CD2 LEU A 469 -33.475-138.988 296.862 1.00117.94 C
ANISOU 2790 CD2 LEU A 469 16074 13646 15092 -1641 284 542 C
ATOM 2791 N ILE A 470 -37.283-140.815 294.718 1.00116.80 N
ANISOU 2791 N ILE A 470 15204 13182 15992 -752 31 408 N
ATOM 2792 CA ILE A 470 -38.354-141.536 295.404 1.00115.27 C
ANISOU 2792 CA ILE A 470 14740 12882 16174 -436 245 201 C
ATOM 2793 C ILE A 470 -38.775-142.756 294.595 1.00116.24 C
ANISOU 2793 C ILE A 470 14519 13224 16422 -328 258 152 C
ATOM 2794 O ILE A 470 -38.941-143.856 295.137 1.00122.05 O
ANISOU 2794 O ILE A 470 15014 14089 17270 -234 517 31 O
ATOM 2795 CB ILE A 470 -39.548-140.601 295.671 1.00117.24 C
ANISOU 2795 CB ILE A 470 15082 12705 16759 -190 128 86 C
ATOM 2796 CG1 ILE A 470 -39.186-139.559 296.730 1.00121.19 C
ANISOU 2796 CG1 ILE A 470 15874 12991 17183 -260 181 73 C
ATOM 2797 CG2 ILE A 470 -40.767-141.400 296.106 1.00115.65 C
ANISOU 2797 CG2 ILE A 470 14539 12453 16948 107 331 -161 C
ATOM 2798 CD1 ILE A 470 -40.235-138.482 296.902 1.00124.02 C
ANISOU 2798 CD1 ILE A 470 16361 12918 17841 -23 -7 -52 C
ATOM 2799 N LEU A 471 -38.950-142.581 293.283 1.00110.59 N
ANISOU 2799 N LEU A 471 13797 12542 15678 -349 -31 247 N
ATOM 2800 CA LEU A 471 -39.293-143.717 292.435 1.00107.16 C
ANISOU 2800 CA LEU A 471 13027 12340 15347 -257 -40 188 C
ATOM 2801 C LEU A 471 -38.178-144.753 292.432 1.00107.35 C
ANISOU 2801 C LEU A 471 12913 12773 15101 -440 112 212 C
ATOM 2802 O LEU A 471 -38.442-145.956 292.537 1.00110.70 O
ANISOU 2802 O LEU A 471 13050 13335 15678 -318 278 87 O
ATOM 2803 CB LEU A 471 -39.602-143.246 291.015 1.00107.36 C
ANISOU 2803 CB LEU A 471 13106 12348 15339 -261 -402 295 C
ATOM 2804 CG LEU A 471 -40.897-142.442 290.878 1.00112.14 C
ANISOU 2804 CG LEU A 471 13780 12554 16276 19 -605 212 C
ATOM 2805 CD1 LEU A 471 -41.229-142.180 289.418 1.00115.55 C
ANISOU 2805 CD1 LEU A 471 14243 12997 16663 48 -976 312 C
ATOM 2806 CD2 LEU A 471 -42.042-143.150 291.582 1.00112.50 C
ANISOU 2806 CD2 LEU A 471 13492 12499 16752 324 -368 -71 C
ATOM 2807 N VAL A 472 -36.925-144.308 292.321 1.00105.10 N
ANISOU 2807 N VAL A 472 12831 12688 14417 -735 48 348 N
ATOM 2808 CA VAL A 472 -35.805-145.234 292.454 1.00104.49 C
ANISOU 2808 CA VAL A 472 12616 13011 14077 -880 181 314 C
ATOM 2809 C VAL A 472 -35.794-145.850 293.847 1.00104.96 C
ANISOU 2809 C VAL A 472 12630 13006 14244 -748 483 194 C
ATOM 2810 O VAL A 472 -35.534-147.048 294.009 1.00107.22 O
ANISOU 2810 O VAL A 472 12708 13499 14532 -682 610 101 O
ATOM 2811 CB VAL A 472 -34.475-144.526 292.132 1.00106.74 C
ANISOU 2811 CB VAL A 472 13114 13539 13904 -1242 66 435 C
ATOM 2812 CG1 VAL A 472 -33.294-145.377 292.573 1.00105.29 C
ANISOU 2812 CG1 VAL A 472 12795 13749 13462 -1348 217 334 C
ATOM 2813 CG2 VAL A 472 -34.380-144.236 290.644 1.00109.16 C
ANISOU 2813 CG2 VAL A 472 13426 14009 14039 -1415 -209 551 C
ATOM 2814 N VAL A 473 -36.100-145.050 294.871 1.00106.35 N
ANISOU 2814 N VAL A 473 13015 12883 14509 -702 589 190 N
ATOM 2815 CA VAL A 473 -36.148-145.574 296.235 1.00105.68 C
ANISOU 2815 CA VAL A 473 12918 12732 14502 -591 881 85 C
ATOM 2816 C VAL A 473 -37.266-146.601 296.374 1.00104.29 C
ANISOU 2816 C VAL A 473 12489 12454 14682 -354 1037 -43 C
ATOM 2817 O VAL A 473 -37.054-147.709 296.882 1.00102.89 O
ANISOU 2817 O VAL A 473 12204 12395 14493 -309 1220 -104 O
ATOM 2818 CB VAL A 473 -36.307-144.426 297.250 1.00104.42 C
ANISOU 2818 CB VAL A 473 13020 12288 14367 -595 952 82 C
ATOM 2819 CG1 VAL A 473 -36.877-144.948 298.558 1.00104.12 C
ANISOU 2819 CG1 VAL A 473 12932 12115 14514 -426 1257 -50 C
ATOM 2820 CG2 VAL A 473 -34.968-143.750 297.494 1.00103.43 C
ANISOU 2820 CG2 VAL A 473 13126 12323 13849 -855 902 166 C
ATOM 2821 N LEU A 474 -38.473-146.251 295.919 1.00105.48 N
ANISOU 2821 N LEU A 474 12551 12376 15149 -203 955 -97 N
ATOM 2822 CA LEU A 474 -39.605-147.160 296.068 1.00108.53 C
ANISOU 2822 CA LEU A 474 12677 12671 15887 -7 1124 -257 C
ATOM 2823 C LEU A 474 -39.399-148.440 295.268 1.00107.15 C
ANISOU 2823 C LEU A 474 12256 12750 15705 -7 1097 -271 C
ATOM 2824 O LEU A 474 -39.712-149.536 295.747 1.00104.28 O
ANISOU 2824 O LEU A 474 11751 12394 15478 61 1314 -369 O
ATOM 2825 CB LEU A 474 -40.902-146.468 295.650 1.00108.11 C
ANISOU 2825 CB LEU A 474 12546 12364 16166 169 999 -361 C
ATOM 2826 CG LEU A 474 -41.430-145.403 296.612 1.00105.11 C
ANISOU 2826 CG LEU A 474 12336 11694 15908 246 1068 -445 C
ATOM 2827 CD1 LEU A 474 -42.813-144.946 296.188 1.00106.19 C
ANISOU 2827 CD1 LEU A 474 12322 11608 16416 479 938 -624 C
ATOM 2828 CD2 LEU A 474 -41.448-145.924 298.042 1.00100.70 C
ANISOU 2828 CD2 LEU A 474 11780 11120 15360 236 1441 -543 C
ATOM 2829 N ILE A 475 -38.874-148.321 294.047 1.00106.59 N
ANISOU 2829 N ILE A 475 12146 12888 15467 -97 831 -180 N
ATOM 2830 CA ILE A 475 -38.582-149.510 293.251 1.00105.53 C
ANISOU 2830 CA ILE A 475 11763 13030 15305 -97 784 -220 C
ATOM 2831 C ILE A 475 -37.513-150.353 293.934 1.00107.58 C
ANISOU 2831 C ILE A 475 12057 13486 15331 -172 925 -226 C
ATOM 2832 O ILE A 475 -37.581-151.589 293.936 1.00113.79 O
ANISOU 2832 O ILE A 475 12665 14353 16216 -91 1013 -317 O
ATOM 2833 CB ILE A 475 -38.173-149.110 291.821 1.00107.06 C
ANISOU 2833 CB ILE A 475 11920 13445 15312 -208 470 -130 C
ATOM 2834 CG1 ILE A 475 -39.378-148.549 291.063 1.00113.12 C
ANISOU 2834 CG1 ILE A 475 12621 14009 16353 -64 300 -153 C
ATOM 2835 CG2 ILE A 475 -37.578-150.295 291.074 1.00104.08 C
ANISOU 2835 CG2 ILE A 475 11292 13427 14826 -239 416 -192 C
ATOM 2836 CD1 ILE A 475 -39.045-148.019 289.685 1.00115.19 C
ANISOU 2836 CD1 ILE A 475 12918 14448 16401 -185 -26 -32 C
ATOM 2837 N ILE A 476 -36.521-149.702 294.544 1.00107.31 N
ANISOU 2837 N ILE A 476 12264 13519 14991 -315 935 -143 N
ATOM 2838 CA ILE A 476 -35.469-150.439 295.237 1.00109.34 C
ANISOU 2838 CA ILE A 476 12566 13969 15010 -354 1035 -174 C
ATOM 2839 C ILE A 476 -36.016-151.108 296.493 1.00110.91 C
ANISOU 2839 C ILE A 476 12819 13933 15388 -216 1313 -233 C
ATOM 2840 O ILE A 476 -35.734-152.283 296.757 1.00107.65 O
ANISOU 2840 O ILE A 476 12345 13600 14959 -148 1382 -292 O
ATOM 2841 CB ILE A 476 -34.286-149.506 295.558 1.00110.08 C
ANISOU 2841 CB ILE A 476 12885 14214 14726 -551 971 -103 C
ATOM 2842 CG1 ILE A 476 -33.402-149.320 294.322 1.00108.03 C
ANISOU 2842 CG1 ILE A 476 12534 14323 14188 -743 725 -81 C
ATOM 2843 CG2 ILE A 476 -33.472-150.041 296.728 1.00108.56 C
ANISOU 2843 CG2 ILE A 476 12802 14099 14346 -526 1123 -158 C
ATOM 2844 CD1 ILE A 476 -32.236-148.384 294.543 1.00107.01 C
ANISOU 2844 CD1 ILE A 476 12608 14374 13678 -994 670 -35 C
ATOM 2845 N CYS A 477 -36.814-150.386 297.279 1.00114.71 N
ANISOU 2845 N CYS A 477 13428 14121 16035 -179 1468 -228 N
ATOM 2846 CA CYS A 477 -37.240-150.887 298.581 1.00117.29 C
ANISOU 2846 CA CYS A 477 13849 14258 16460 -107 1758 -278 C
ATOM 2847 C CYS A 477 -38.464-151.791 298.517 1.00123.33 C
ANISOU 2847 C CYS A 477 14417 14863 17580 2 1913 -381 C
ATOM 2848 O CYS A 477 -38.571-152.724 299.321 1.00127.18 O
ANISOU 2848 O CYS A 477 14957 15278 18087 22 2122 -409 O
ATOM 2849 CB CYS A 477 -37.520-149.717 299.527 1.00115.04 C
ANISOU 2849 CB CYS A 477 13766 13771 16175 -130 1875 -270 C
ATOM 2850 SG CYS A 477 -36.044-148.790 300.002 1.00113.04 S
ANISOU 2850 SG CYS A 477 13782 13677 15489 -282 1779 -179 S
ATOM 2851 N TRP A 478 -39.393-151.542 297.593 1.00123.28 N
ANISOU 2851 N TRP A 478 14199 14797 17845 63 1811 -444 N
ATOM 2852 CA TRP A 478 -40.611-152.337 297.512 1.00126.67 C
ANISOU 2852 CA TRP A 478 14407 15093 18628 151 1966 -585 C
ATOM 2853 C TRP A 478 -40.655-153.285 296.324 1.00129.32 C
ANISOU 2853 C TRP A 478 14486 15584 19066 192 1812 -628 C
ATOM 2854 O TRP A 478 -41.503-154.183 296.307 1.00131.56 O
ANISOU 2854 O TRP A 478 14592 15779 19616 237 1959 -751 O
ATOM 2855 CB TRP A 478 -41.845-151.424 297.461 1.00129.38 C
ANISOU 2855 CB TRP A 478 14653 15243 19264 234 1987 -706 C
ATOM 2856 CG TRP A 478 -42.022-150.619 298.703 1.00134.01 C
ANISOU 2856 CG TRP A 478 15440 15662 19817 215 2176 -730 C
ATOM 2857 CD1 TRP A 478 -41.724-149.300 298.873 1.00140.13 C
ANISOU 2857 CD1 TRP A 478 16396 16371 20475 209 2047 -674 C
ATOM 2858 CD2 TRP A 478 -42.525-151.083 299.961 1.00135.16 C
ANISOU 2858 CD2 TRP A 478 15635 15688 20031 181 2530 -823 C
ATOM 2859 NE1 TRP A 478 -42.018-148.909 300.157 1.00142.78 N
ANISOU 2859 NE1 TRP A 478 16862 16567 20821 200 2292 -750 N
ATOM 2860 CE2 TRP A 478 -42.510-149.986 300.846 1.00140.62 C
ANISOU 2860 CE2 TRP A 478 16509 16274 20645 175 2599 -840 C
ATOM 2861 CE3 TRP A 478 -42.990-152.317 300.425 1.00135.76 C
ANISOU 2861 CE3 TRP A 478 15638 15731 20214 134 2797 -894 C
ATOM 2862 CZ2 TRP A 478 -42.942-150.087 302.167 1.00142.41 C
ANISOU 2862 CZ2 TRP A 478 16822 16405 20885 128 2931 -936 C
ATOM 2863 CZ3 TRP A 478 -43.418-152.415 301.736 1.00139.10 C
ANISOU 2863 CZ3 TRP A 478 16181 16039 20634 59 3133 -965 C
ATOM 2864 CH2 TRP A 478 -43.391-151.307 302.592 1.00141.80 C
ANISOU 2864 CH2 TRP A 478 16678 16316 20883 59 3201 -990 C
ATOM 2865 N GLY A 479 -39.778-153.110 295.340 1.00128.24 N
ANISOU 2865 N GLY A 479 14317 15691 18719 156 1533 -548 N
ATOM 2866 CA GLY A 479 -39.717-154.003 294.209 1.00129.60 C
ANISOU 2866 CA GLY A 479 14235 16054 18953 193 1375 -607 C
ATOM 2867 C GLY A 479 -39.362-155.418 294.619 1.00131.54 C
ANISOU 2867 C GLY A 479 14461 16329 19188 211 1493 -657 C
ATOM 2868 O GLY A 479 -40.179-156.339 294.524 1.00134.06 O
ANISOU 2868 O GLY A 479 14613 16535 19787 269 1607 -771 O
ATOM 2869 N PRO A 480 -38.125-155.617 295.085 1.00132.39 N
ANISOU 2869 N PRO A 480 14751 16580 18971 163 1453 -588 N
ATOM 2870 CA PRO A 480 -37.721-156.967 295.514 1.00133.41 C
ANISOU 2870 CA PRO A 480 14916 16702 19072 214 1513 -635 C
ATOM 2871 C PRO A 480 -38.552-157.516 296.660 1.00132.49 C
ANISOU 2871 C PRO A 480 14945 16253 19144 220 1826 -642 C
ATOM 2872 O PRO A 480 -38.799-158.727 296.709 1.00140.07 O
ANISOU 2872 O PRO A 480 15868 17114 20239 256 1888 -704 O
ATOM 2873 CB PRO A 480 -36.251-156.777 295.919 1.00134.13 C
ANISOU 2873 CB PRO A 480 15200 17009 18754 180 1396 -579 C
ATOM 2874 CG PRO A 480 -35.800-155.578 295.154 1.00133.09 C
ANISOU 2874 CG PRO A 480 15015 17106 18446 77 1212 -531 C
ATOM 2875 CD PRO A 480 -36.995-154.673 295.088 1.00133.55 C
ANISOU 2875 CD PRO A 480 15057 16928 18757 64 1306 -490 C
ATOM 2876 N LEU A 481 -38.993-156.662 297.586 1.00124.14 N
ANISOU 2876 N LEU A 481 14059 15020 18090 167 2026 -590 N
ATOM 2877 CA LEU A 481 -39.768-157.146 298.725 1.00123.80 C
ANISOU 2877 CA LEU A 481 14158 14700 18181 128 2351 -607 C
ATOM 2878 C LEU A 481 -41.078-157.774 298.268 1.00123.16 C
ANISOU 2878 C LEU A 481 13820 14484 18491 128 2481 -749 C
ATOM 2879 O LEU A 481 -41.402-158.907 298.643 1.00123.95 O
ANISOU 2879 O LEU A 481 13967 14437 18690 87 2640 -782 O
ATOM 2880 CB LEU A 481 -40.033-156.005 299.706 1.00128.60 C
ANISOU 2880 CB LEU A 481 14942 15195 18724 74 2529 -571 C
ATOM 2881 CG LEU A 481 -40.664-156.439 301.032 1.00134.18 C
ANISOU 2881 CG LEU A 481 15836 15670 19475 -5 2886 -584 C
ATOM 2882 CD1 LEU A 481 -39.633-157.120 301.919 1.00135.42 C
ANISOU 2882 CD1 LEU A 481 16327 15821 19307 -18 2905 -460 C
ATOM 2883 CD2 LEU A 481 -41.303-155.261 301.748 1.00137.48 C
ANISOU 2883 CD2 LEU A 481 16295 15996 19946 -43 3063 -635 C
ATOM 2884 N LEU A 482 -41.848-157.050 297.451 1.00120.35 N
ANISOU 2884 N LEU A 482 13203 14167 18358 170 2402 -845 N
ATOM 2885 CA LEU A 482 -43.093-157.607 296.936 1.00117.37 C
ANISOU 2885 CA LEU A 482 12533 13704 18359 185 2502 -1026 C
ATOM 2886 C LEU A 482 -42.835-158.723 295.932 1.00116.40 C
ANISOU 2886 C LEU A 482 12222 13698 18308 231 2326 -1073 C
ATOM 2887 O LEU A 482 -43.675-159.616 295.774 1.00121.34 O
ANISOU 2887 O LEU A 482 12678 14218 19210 206 2461 -1213 O
ATOM 2888 CB LEU A 482 -43.943-156.508 296.300 1.00113.41 C
ANISOU 2888 CB LEU A 482 11808 13221 18062 265 2408 -1138 C
ATOM 2889 CG LEU A 482 -44.426-155.401 297.239 1.00111.23 C
ANISOU 2889 CG LEU A 482 11660 12807 17796 250 2574 -1165 C
ATOM 2890 CD1 LEU A 482 -45.339-154.434 296.502 1.00111.27 C
ANISOU 2890 CD1 LEU A 482 11431 12804 18043 378 2424 -1315 C
ATOM 2891 CD2 LEU A 482 -45.131-155.993 298.450 1.00113.76 C
ANISOU 2891 CD2 LEU A 482 12050 12953 18221 130 2976 -1261 C
ATOM 2892 N ALA A 483 -41.688-158.692 295.249 1.00110.05 N
ANISOU 2892 N ALA A 483 11429 13127 17257 283 2032 -986 N
ATOM 2893 CA ALA A 483 -41.364-159.755 294.303 1.00110.41 C
ANISOU 2893 CA ALA A 483 11281 13317 17353 341 1846 -1063 C
ATOM 2894 C ALA A 483 -41.259-161.099 295.009 1.00113.81 C
ANISOU 2894 C ALA A 483 11870 13562 17813 312 1994 -1074 C
ATOM 2895 O ALA A 483 -41.866-162.088 294.580 1.00115.94 O
ANISOU 2895 O ALA A 483 11962 13750 18340 318 2028 -1204 O
ATOM 2896 CB ALA A 483 -40.065-159.429 293.567 1.00108.35 C
ANISOU 2896 CB ALA A 483 11010 13383 16773 376 1526 -996 C
ATOM 2897 N ILE A 484 -40.496-161.151 296.105 1.00114.82 N
ANISOU 2897 N ILE A 484 12352 13603 17669 280 2070 -940 N
ATOM 2898 CA ILE A 484 -40.355-162.393 296.860 1.00116.25 C
ANISOU 2898 CA ILE A 484 12771 13563 17835 257 2182 -918 C
ATOM 2899 C ILE A 484 -41.711-162.866 297.365 1.00120.08 C
ANISOU 2899 C ILE A 484 13249 13751 18626 120 2523 -984 C
ATOM 2900 O ILE A 484 -41.995-164.070 297.393 1.00123.47 O
ANISOU 2900 O ILE A 484 13716 13999 19197 79 2583 -1035 O
ATOM 2901 CB ILE A 484 -39.355-162.205 298.016 1.00116.86 C
ANISOU 2901 CB ILE A 484 13254 13603 17543 259 2200 -761 C
ATOM 2902 CG1 ILE A 484 -38.013-161.689 297.491 1.00112.73 C
ANISOU 2902 CG1 ILE A 484 12694 13423 16716 365 1877 -745 C
ATOM 2903 CG2 ILE A 484 -39.170-163.508 298.776 1.00121.82 C
ANISOU 2903 CG2 ILE A 484 14188 13973 18126 254 2265 -719 C
ATOM 2904 CD1 ILE A 484 -37.396-162.557 296.417 1.00112.86 C
ANISOU 2904 CD1 ILE A 484 12494 13645 16741 487 1573 -872 C
ATOM 2905 N MET A 485 -42.574-161.929 297.760 1.00122.22 N
ANISOU 2905 N MET A 485 13463 13971 19002 37 2747 -1010 N
ATOM 2906 CA MET A 485 -43.902-162.306 298.228 1.00127.54 C
ANISOU 2906 CA MET A 485 14075 14423 19960 -119 3092 -1129 C
ATOM 2907 C MET A 485 -44.757-162.870 297.100 1.00128.30 C
ANISOU 2907 C MET A 485 13768 14557 20423 -97 3042 -1340 C
ATOM 2908 O MET A 485 -45.600-163.741 297.341 1.00127.94 O
ANISOU 2908 O MET A 485 13689 14324 20600 -243 3281 -1451 O
ATOM 2909 CB MET A 485 -44.588-161.105 298.877 1.00131.05 C
ANISOU 2909 CB MET A 485 14507 14854 20432 -179 3310 -1167 C
ATOM 2910 CG MET A 485 -43.834-160.536 300.066 1.00131.22 C
ANISOU 2910 CG MET A 485 14916 14837 20105 -214 3391 -984 C
ATOM 2911 SD MET A 485 -44.701-159.158 300.838 1.00131.82 S
ANISOU 2911 SD MET A 485 14949 14892 20242 -273 3643 -1079 S
ATOM 2912 CE MET A 485 -43.530-158.690 302.110 1.00131.36 C
ANISOU 2912 CE MET A 485 15360 14820 19729 -295 3672 -850 C
ATOM 2913 N VAL A 486 -44.556-162.395 295.868 1.00130.87 N
ANISOU 2913 N VAL A 486 13794 15128 20800 64 2740 -1403 N
ATOM 2914 CA VAL A 486 -45.279-162.961 294.733 1.00133.65 C
ANISOU 2914 CA VAL A 486 13756 15548 21476 110 2654 -1612 C
ATOM 2915 C VAL A 486 -44.796-164.379 294.450 1.00132.91 C
ANISOU 2915 C VAL A 486 13708 15394 21399 111 2556 -1623 C
ATOM 2916 O VAL A 486 -45.595-165.268 294.128 1.00136.18 O
ANISOU 2916 O VAL A 486 13937 15697 22108 45 2661 -1794 O
ATOM 2917 CB VAL A 486 -45.138-162.051 293.498 1.00133.39 C
ANISOU 2917 CB VAL A 486 13436 15803 21442 276 2337 -1654 C
ATOM 2918 CG1 VAL A 486 -45.704-162.733 292.262 1.00132.85 C
ANISOU 2918 CG1 VAL A 486 13040 15843 21592 335 2164 -1841 C
ATOM 2919 CG2 VAL A 486 -45.845-160.726 293.737 1.00134.61 C
ANISOU 2919 CG2 VAL A 486 13539 15948 21659 293 2420 -1688 C
ATOM 2920 N TYR A 487 -43.485-164.615 294.568 1.00128.63 N
ANISOU 2920 N TYR A 487 13405 14923 20547 192 2341 -1471 N
ATOM 2921 CA TYR A 487 -42.964-165.976 294.472 1.00128.48 C
ANISOU 2921 CA TYR A 487 13492 14800 20526 222 2226 -1491 C
ATOM 2922 C TYR A 487 -43.605-166.883 295.513 1.00130.85 C
ANISOU 2922 C TYR A 487 14073 14706 20938 31 2546 -1466 C
ATOM 2923 O TYR A 487 -43.822-168.074 295.264 1.00138.18 O
ANISOU 2923 O TYR A 487 14990 15466 22045 -2 2532 -1559 O
ATOM 2924 CB TYR A 487 -41.445-165.980 294.643 1.00130.33 C
ANISOU 2924 CB TYR A 487 13966 15175 20380 353 1956 -1360 C
ATOM 2925 CG TYR A 487 -40.660-165.576 293.416 1.00135.78 C
ANISOU 2925 CG TYR A 487 14360 16274 20954 508 1598 -1435 C
ATOM 2926 CD1 TYR A 487 -40.211-164.273 293.254 1.00137.38 C
ANISOU 2926 CD1 TYR A 487 14531 16732 20934 519 1513 -1347 C
ATOM 2927 CD2 TYR A 487 -40.353-166.502 292.428 1.00140.59 C
ANISOU 2927 CD2 TYR A 487 14736 17020 21661 621 1348 -1601 C
ATOM 2928 CE1 TYR A 487 -39.488-163.898 292.140 1.00138.29 C
ANISOU 2928 CE1 TYR A 487 14405 17235 20904 603 1207 -1407 C
ATOM 2929 CE2 TYR A 487 -39.629-166.138 291.308 1.00142.13 C
ANISOU 2929 CE2 TYR A 487 14654 17634 21717 729 1039 -1686 C
ATOM 2930 CZ TYR A 487 -39.199-164.834 291.170 1.00141.12 C
ANISOU 2930 CZ TYR A 487 14515 17762 21343 702 979 -1580 C
ATOM 2931 OH TYR A 487 -38.478-164.465 290.058 1.00141.31 O
ANISOU 2931 OH TYR A 487 14287 18214 21190 755 692 -1656 O
ATOM 2932 N ASP A 488 -43.909-166.338 296.691 1.00126.63 N
ANISOU 2932 N ASP A 488 13807 14018 20287 -115 2839 -1345 N
ATOM 2933 CA ASP A 488 -44.559-167.137 297.721 1.00127.09 C
ANISOU 2933 CA ASP A 488 14157 13722 20409 -353 3179 -1311 C
ATOM 2934 C ASP A 488 -46.019-167.408 297.382 1.00132.83 C
ANISOU 2934 C ASP A 488 14558 14376 21536 -530 3447 -1543 C
ATOM 2935 O ASP A 488 -46.542-168.478 297.715 1.00139.11 O
ANISOU 2935 O ASP A 488 15487 14900 22469 -730 3641 -1584 O
ATOM 2936 CB ASP A 488 -44.438-166.436 299.074 1.00124.34 C
ANISOU 2936 CB ASP A 488 14172 13283 19789 -467 3419 -1135 C
ATOM 2937 CG ASP A 488 -45.255-167.109 300.150 1.00123.60 C
ANISOU 2937 CG ASP A 488 14360 12864 19738 -772 3824 -1110 C
ATOM 2938 OD1 ASP A 488 -45.071-168.325 300.370 1.00125.07 O
ANISOU 2938 OD1 ASP A 488 14826 12787 19907 -852 3810 -1043 O
ATOM 2939 OD2 ASP A 488 -46.096-166.422 300.764 1.00123.41 O
ANISOU 2939 OD2 ASP A 488 14279 12849 19761 -941 4151 -1171 O
ATOM 2940 N VAL A 489 -46.688-166.466 296.714 1.00134.70 N
ANISOU 2940 N VAL A 489 14376 14845 21960 -461 3445 -1710 N
ATOM 2941 CA VAL A 489 -48.094-166.660 296.367 1.00139.20 C
ANISOU 2941 CA VAL A 489 14583 15392 22915 -599 3680 -1987 C
ATOM 2942 C VAL A 489 -48.225-167.680 295.241 1.00140.82 C
ANISOU 2942 C VAL A 489 14516 15614 23374 -537 3493 -2152 C
ATOM 2943 O VAL A 489 -48.954-168.672 295.359 1.00140.94 O
ANISOU 2943 O VAL A 489 14510 15425 23615 -743 3707 -2286 O
ATOM 2944 CB VAL A 489 -48.746-165.316 295.993 1.00138.19 C
ANISOU 2944 CB VAL A 489 14106 15497 22903 -490 3678 -2137 C
ATOM 2945 CG1 VAL A 489 -50.152-165.537 295.472 1.00142.11 C
ANISOU 2945 CG1 VAL A 489 14251 16017 23729 -575 3783 -2452 C
ATOM 2946 CG2 VAL A 489 -48.768-164.379 297.197 1.00136.13 C
ANISOU 2946 CG2 VAL A 489 14100 15188 22435 -577 3905 -2025 C
ATOM 2947 N PHE A 490 -47.516-167.457 294.138 1.00141.17 N
ANISOU 2947 N PHE A 490 14351 15912 23375 -276 3098 -2156 N
ATOM 2948 CA PHE A 490 -47.526-168.373 292.999 1.00145.54 C
ANISOU 2948 CA PHE A 490 14623 16534 24143 -184 2878 -2327 C
ATOM 2949 C PHE A 490 -46.373-169.352 293.156 1.00148.03 C
ANISOU 2949 C PHE A 490 15266 16719 24259 -126 2672 -2179 C
ATOM 2950 O PHE A 490 -45.207-168.967 293.030 1.00149.26 O
ANISOU 2950 O PHE A 490 15543 17051 24118 54 2394 -2035 O
ATOM 2951 CB PHE A 490 -47.404-167.611 291.681 1.00146.33 C
ANISOU 2951 CB PHE A 490 14466 17006 24126 30 2470 -2376 C
ATOM 2952 CG PHE A 490 -48.567-166.708 291.385 1.00149.22 C
ANISOU 2952 CG PHE A 490 14760 17472 24464 -2 2454 -2461 C
ATOM 2953 CD1 PHE A 490 -49.734-166.801 292.121 1.00150.85 C
ANISOU 2953 CD1 PHE A 490 14950 17484 24881 -197 2810 -2604 C
ATOM 2954 CD2 PHE A 490 -48.500-165.774 290.362 1.00150.80 C
ANISOU 2954 CD2 PHE A 490 14905 17964 24430 162 2094 -2419 C
ATOM 2955 CE1 PHE A 490 -50.812-165.977 291.858 1.00154.01 C
ANISOU 2955 CE1 PHE A 490 15255 17988 25275 -186 2765 -2732 C
ATOM 2956 CE2 PHE A 490 -49.581-164.942 290.088 1.00153.50 C
ANISOU 2956 CE2 PHE A 490 15166 18368 24788 175 2071 -2519 C
ATOM 2957 CZ PHE A 490 -50.740-165.045 290.840 1.00155.04 C
ANISOU 2957 CZ PHE A 490 15320 18378 25209 19 2386 -2690 C
ATOM 2958 N GLY A 491 -46.695-170.619 293.406 1.00147.48 N
ANISOU 2958 N GLY A 491 15337 16344 24354 -277 2791 -2239 N
ATOM 2959 CA GLY A 491 -45.631-171.567 293.662 1.00151.62 C
ANISOU 2959 CA GLY A 491 16228 16687 24692 -198 2573 -2108 C
ATOM 2960 C GLY A 491 -45.007-171.353 295.033 1.00153.89 C
ANISOU 2960 C GLY A 491 17073 16771 24627 -271 2690 -1821 C
ATOM 2961 O GLY A 491 -45.589-170.733 295.931 1.00155.19 O
ANISOU 2961 O GLY A 491 17381 16850 24735 -464 3026 -1732 O
ATOM 2962 N LYS A 492 -43.796-171.889 295.187 1.00156.07 N
ANISOU 2962 N LYS A 492 17654 16988 24658 -97 2391 -1703 N
ATOM 2963 CA LYS A 492 -43.056-171.786 296.436 1.00155.68 C
ANISOU 2963 CA LYS A 492 18149 16756 24245 -114 2430 -1444 C
ATOM 2964 C LYS A 492 -41.594-171.500 296.119 1.00153.44 C
ANISOU 2964 C LYS A 492 17891 16751 23659 199 2011 -1404 C
ATOM 2965 O LYS A 492 -41.171-171.500 294.958 1.00151.53 O
ANISOU 2965 O LYS A 492 17268 16820 23485 396 1709 -1575 O
ATOM 2966 CB LYS A 492 -43.198-173.059 297.289 1.00157.92 C
ANISOU 2966 CB LYS A 492 18938 16533 24530 -285 2543 -1343 C
ATOM 2967 CG LYS A 492 -44.640-173.388 297.681 1.00157.56 C
ANISOU 2967 CG LYS A 492 18891 16220 24753 -669 3002 -1397 C
ATOM 2968 CD LYS A 492 -44.760-173.851 299.128 1.00156.56 C
ANISOU 2968 CD LYS A 492 19404 15672 24411 -942 3278 -1159 C
ATOM 2969 CE LYS A 492 -46.096-173.412 299.732 1.00154.93 C
ANISOU 2969 CE LYS A 492 19116 15421 24330 -1333 3815 -1203 C
ATOM 2970 NZ LYS A 492 -46.091-173.382 301.224 1.00155.89 N
ANISOU 2970 NZ LYS A 492 19817 15285 24129 -1584 4105 -950 N
ATOM 2971 N MET A 493 -40.819-171.254 297.168 1.00153.05 N
ANISOU 2971 N MET A 493 18280 16614 23256 232 2001 -1197 N
ATOM 2972 CA MET A 493 -39.439-170.813 297.043 1.00150.16 C
ANISOU 2972 CA MET A 493 17942 16548 22565 495 1655 -1174 C
ATOM 2973 C MET A 493 -38.513-171.764 297.787 1.00146.45 C
ANISOU 2973 C MET A 493 17969 15812 21862 633 1439 -1088 C
ATOM 2974 O MET A 493 -38.945-172.603 298.581 1.00151.00 O
ANISOU 2974 O MET A 493 18961 15936 22476 491 1594 -974 O
ATOM 2975 CB MET A 493 -39.270-169.389 297.581 1.00156.45 C
ANISOU 2975 CB MET A 493 18760 17563 23122 447 1805 -1039 C
ATOM 2976 CG MET A 493 -39.616-169.245 299.054 1.00165.38 C
ANISOU 2976 CG MET A 493 20362 18380 24097 256 2136 -826 C
ATOM 2977 SD MET A 493 -39.836-167.519 299.509 1.00169.60 S
ANISOU 2977 SD MET A 493 20797 19155 24488 162 2372 -738 S
ATOM 2978 CE MET A 493 -40.957-166.995 298.217 1.00170.11 C
ANISOU 2978 CE MET A 493 20250 19425 24957 106 2445 -941 C
ATOM 2979 N ASN A 494 -37.221-171.612 297.522 1.00139.28 N
ANISOU 2979 N ASN A 494 17026 15196 20697 906 1068 -1156 N
ATOM 2980 CA ASN A 494 -36.197-172.419 298.164 1.00138.56 C
ANISOU 2980 CA ASN A 494 17371 14917 20360 1114 781 -1123 C
ATOM 2981 C ASN A 494 -35.720-171.721 299.437 1.00133.02 C
ANISOU 2981 C ASN A 494 17081 14176 19285 1087 902 -901 C
ATOM 2982 O ASN A 494 -36.280-170.709 299.869 1.00130.72 O
ANISOU 2982 O ASN A 494 16758 13952 18959 882 1236 -771 O
ATOM 2983 CB ASN A 494 -35.055-172.685 297.187 1.00138.64 C
ANISOU 2983 CB ASN A 494 17076 15305 20297 1437 304 -1387 C
ATOM 2984 CG ASN A 494 -34.358-171.414 296.748 1.00134.31 C
ANISOU 2984 CG ASN A 494 16186 15322 19523 1489 232 -1449 C
ATOM 2985 OD1 ASN A 494 -33.591-170.825 297.506 1.00132.08 O
ANISOU 2985 OD1 ASN A 494 16131 15146 18907 1546 201 -1355 O
ATOM 2986 ND2 ASN A 494 -34.621-170.983 295.519 1.00133.49 N
ANISOU 2986 ND2 ASN A 494 15549 15581 19588 1456 202 -1608 N
ATOM 2987 N LYS A 495 -34.661-172.259 300.048 1.00131.27 N
ANISOU 2987 N LYS A 495 17243 13853 18779 1320 606 -884 N
ATOM 2988 CA LYS A 495 -34.137-171.714 301.296 1.00125.93 C
ANISOU 2988 CA LYS A 495 16989 13130 17727 1325 682 -690 C
ATOM 2989 C LYS A 495 -33.360-170.421 301.082 1.00117.71 C
ANISOU 2989 C LYS A 495 15644 12622 16457 1406 615 -762 C
ATOM 2990 O LYS A 495 -33.394-169.534 301.942 1.00116.26 O
ANISOU 2990 O LYS A 495 15639 12465 16069 1284 847 -598 O
ATOM 2991 CB LYS A 495 -33.257-172.763 301.979 1.00126.69 C
ANISOU 2991 CB LYS A 495 17605 12936 17596 1582 339 -672 C
ATOM 2992 CG LYS A 495 -32.440-172.267 303.162 1.00123.88 C
ANISOU 2992 CG LYS A 495 17654 12609 16805 1683 298 -534 C
ATOM 2993 CD LYS A 495 -30.962-172.180 302.806 1.00116.40 C
ANISOU 2993 CD LYS A 495 16542 12070 15616 2066 -180 -786 C
ATOM 2994 CE LYS A 495 -30.094-172.094 304.051 1.00109.66 C
ANISOU 2994 CE LYS A 495 16191 11138 14337 2237 -314 -682 C
ATOM 2995 NZ LYS A 495 -28.644-172.039 303.717 1.00103.62 N
ANISOU 2995 NZ LYS A 495 15233 10802 13337 2616 -787 -985 N
ATOM 2996 N LEU A 496 -32.665-170.291 299.950 1.00115.28 N
ANISOU 2996 N LEU A 496 14883 12747 16171 1584 311 -1014 N
ATOM 2997 CA LEU A 496 -31.899-169.075 299.690 1.00116.61 C
ANISOU 2997 CA LEU A 496 14774 13428 16106 1611 250 -1089 C
ATOM 2998 C LEU A 496 -32.809-167.857 299.598 1.00118.86 C
ANISOU 2998 C LEU A 496 14858 13802 16503 1326 628 -953 C
ATOM 2999 O LEU A 496 -32.456-166.772 300.077 1.00115.56 O
ANISOU 2999 O LEU A 496 14481 13572 15854 1263 727 -874 O
ATOM 3000 CB LEU A 496 -31.087-169.227 298.404 1.00111.63 C
ANISOU 3000 CB LEU A 496 13673 13260 15481 1796 -118 -1401 C
ATOM 3001 CG LEU A 496 -30.339-167.994 297.895 1.00104.93 C
ANISOU 3001 CG LEU A 496 12481 12984 14406 1757 -178 -1505 C
ATOM 3002 CD1 LEU A 496 -29.001-167.835 298.606 1.00106.91 C
ANISOU 3002 CD1 LEU A 496 12930 13438 14253 1946 -405 -1594 C
ATOM 3003 CD2 LEU A 496 -30.151-168.063 296.385 1.00102.52 C
ANISOU 3003 CD2 LEU A 496 11633 13098 14224 1788 -385 -1765 C
ATOM 3004 N ILE A 497 -33.983-168.017 298.984 1.00119.77 N
ANISOU 3004 N ILE A 497 14750 13778 16978 1166 823 -949 N
ATOM 3005 CA ILE A 497 -34.908-166.897 298.841 1.00115.25 C
ANISOU 3005 CA ILE A 497 13970 13277 16542 938 1141 -861 C
ATOM 3006 C ILE A 497 -35.392-166.431 300.208 1.00115.95 C
ANISOU 3006 C ILE A 497 14447 13088 16522 776 1482 -643 C
ATOM 3007 O ILE A 497 -35.562-165.229 300.445 1.00117.43 O
ANISOU 3007 O ILE A 497 14567 13416 16634 667 1652 -576 O
ATOM 3008 CB ILE A 497 -36.082-167.289 297.925 1.00118.00 C
ANISOU 3008 CB ILE A 497 13996 13533 17307 834 1254 -947 C
ATOM 3009 CG1 ILE A 497 -35.566-168.003 296.673 1.00121.06 C
ANISOU 3009 CG1 ILE A 497 14050 14158 17791 1012 899 -1178 C
ATOM 3010 CG2 ILE A 497 -36.881-166.062 297.533 1.00118.15 C
ANISOU 3010 CG2 ILE A 497 13727 13710 17457 674 1469 -922 C
ATOM 3011 CD1 ILE A 497 -34.629-167.163 295.829 1.00121.90 C
ANISOU 3011 CD1 ILE A 497 13830 14797 17688 1096 655 -1298 C
ATOM 3012 N LYS A 498 -35.625-167.373 301.127 1.00118.56 N
ANISOU 3012 N LYS A 498 15202 13014 16831 748 1580 -534 N
ATOM 3013 CA LYS A 498 -35.947-167.002 302.501 1.00122.87 C
ANISOU 3013 CA LYS A 498 16154 13328 17201 593 1887 -334 C
ATOM 3014 C LYS A 498 -34.838-166.154 303.109 1.00130.85 C
ANISOU 3014 C LYS A 498 17309 14583 17823 714 1764 -292 C
ATOM 3015 O LYS A 498 -35.108-165.152 303.782 1.00129.46 O
ANISOU 3015 O LYS A 498 17199 14446 17545 579 2013 -197 O
ATOM 3016 CB LYS A 498 -36.178-168.253 303.349 1.00128.04 C
ANISOU 3016 CB LYS A 498 17306 13521 17825 547 1948 -212 C
ATOM 3017 CG LYS A 498 -37.338-169.126 302.906 1.00129.43 C
ANISOU 3017 CG LYS A 498 17392 13409 18375 367 2122 -250 C
ATOM 3018 CD LYS A 498 -37.489-170.315 303.840 1.00134.42 C
ANISOU 3018 CD LYS A 498 18603 13551 18919 279 2182 -96 C
ATOM 3019 CE LYS A 498 -38.670-171.187 303.457 1.00136.58 C
ANISOU 3019 CE LYS A 498 18808 13525 19562 43 2389 -141 C
ATOM 3020 NZ LYS A 498 -38.812-172.347 304.381 1.00140.38 N
ANISOU 3020 NZ LYS A 498 19914 13492 19930 -90 2449 34 N
ATOM 3021 N THR A 499 -33.582-166.543 302.880 1.00138.35 N
ANISOU 3021 N THR A 499 18291 15717 18559 972 1373 -398 N
ATOM 3022 CA THR A 499 -32.459-165.748 303.362 1.00139.51 C
ANISOU 3022 CA THR A 499 18519 16151 18339 1089 1234 -414 C
ATOM 3023 C THR A 499 -32.413-164.393 302.668 1.00131.44 C
ANISOU 3023 C THR A 499 17084 15521 17336 989 1285 -481 C
ATOM 3024 O THR A 499 -32.202-163.362 303.319 1.00130.50 O
ANISOU 3024 O THR A 499 17057 15505 17021 914 1416 -409 O
ATOM 3025 CB THR A 499 -31.148-166.505 303.144 1.00145.76 C
ANISOU 3025 CB THR A 499 19360 17100 18923 1399 782 -586 C
ATOM 3026 OG1 THR A 499 -31.284-167.849 303.625 1.00151.76 O
ANISOU 3026 OG1 THR A 499 20512 17436 19714 1504 688 -526 O
ATOM 3027 CG2 THR A 499 -30.009-165.824 303.885 1.00146.62 C
ANISOU 3027 CG2 THR A 499 19626 17458 18625 1518 659 -613 C
ATOM 3028 N VAL A 500 -32.612-164.375 301.348 1.00116.46 N
ANISOU 3028 N VAL A 500 14752 13831 15666 981 1171 -617 N
ATOM 3029 CA VAL A 500 -32.638-163.109 300.619 1.00101.83 C
ANISOU 3029 CA VAL A 500 12553 12308 13829 865 1203 -655 C
ATOM 3030 C VAL A 500 -33.788-162.240 301.109 1.00102.31 C
ANISOU 3030 C VAL A 500 12661 12168 14046 656 1574 -505 C
ATOM 3031 O VAL A 500 -33.626-161.032 301.324 1.00105.51 O
ANISOU 3031 O VAL A 500 13048 12721 14321 571 1649 -463 O
ATOM 3032 CB VAL A 500 -32.724-163.363 299.102 1.00 90.90 C
ANISOU 3032 CB VAL A 500 10724 11163 12651 892 1009 -820 C
ATOM 3033 CG1 VAL A 500 -32.922-162.054 298.351 1.00 76.83 C
ANISOU 3033 CG1 VAL A 500 8649 9653 10891 741 1054 -815 C
ATOM 3034 CG2 VAL A 500 -31.471-164.071 298.614 1.00 96.74 C
ANISOU 3034 CG2 VAL A 500 11367 12188 13200 1103 627 -1027 C
ATOM 3035 N PHE A 501 -34.964-162.840 301.307 1.00 94.96 N
ANISOU 3035 N PHE A 501 11787 10898 13394 564 1808 -449 N
ATOM 3036 CA PHE A 501 -36.095-162.076 301.823 1.00 97.85 C
ANISOU 3036 CA PHE A 501 12170 11095 13914 377 2164 -365 C
ATOM 3037 C PHE A 501 -35.809-161.544 303.221 1.00104.63 C
ANISOU 3037 C PHE A 501 13399 11863 14492 329 2337 -241 C
ATOM 3038 O PHE A 501 -36.226-160.431 303.565 1.00110.13 O
ANISOU 3038 O PHE A 501 14059 12589 15196 224 2524 -214 O
ATOM 3039 CB PHE A 501 -37.359-162.932 301.828 1.00 98.77 C
ANISOU 3039 CB PHE A 501 12271 10898 14359 263 2396 -373 C
ATOM 3040 CG PHE A 501 -38.545-162.240 302.424 1.00 98.45 C
ANISOU 3040 CG PHE A 501 12225 10709 14474 71 2773 -345 C
ATOM 3041 CD1 PHE A 501 -39.221-161.261 301.713 1.00 97.32 C
ANISOU 3041 CD1 PHE A 501 11728 10703 14547 35 2815 -436 C
ATOM 3042 CD2 PHE A 501 -38.981-162.559 303.700 1.00104.03 C
ANISOU 3042 CD2 PHE A 501 13286 11147 15093 -69 3071 -246 C
ATOM 3043 CE1 PHE A 501 -40.312-160.615 302.262 1.00103.14 C
ANISOU 3043 CE1 PHE A 501 12430 11321 15438 -107 3133 -467 C
ATOM 3044 CE2 PHE A 501 -40.074-161.918 304.254 1.00108.13 C
ANISOU 3044 CE2 PHE A 501 13759 11579 15747 -252 3425 -273 C
ATOM 3045 CZ PHE A 501 -40.739-160.943 303.535 1.00107.93 C
ANISOU 3045 CZ PHE A 501 13344 11700 15963 -255 3450 -403 C
ATOM 3046 N ALA A 502 -35.105-162.327 304.043 1.00107.05 N
ANISOU 3046 N ALA A 502 14075 12052 14548 422 2258 -177 N
ATOM 3047 CA ALA A 502 -34.695-161.834 305.355 1.00108.04 C
ANISOU 3047 CA ALA A 502 14558 12135 14360 403 2381 -70 C
ATOM 3048 C ALA A 502 -33.834-160.585 305.220 1.00107.37 C
ANISOU 3048 C ALA A 502 14336 12393 14068 448 2248 -124 C
ATOM 3049 O ALA A 502 -34.030-159.603 305.946 1.00 98.50 O
ANISOU 3049 O ALA A 502 13301 11270 12853 348 2448 -73 O
ATOM 3050 CB ALA A 502 -33.947-162.926 306.119 1.00108.39 C
ANISOU 3050 CB ALA A 502 15024 12016 14141 546 2228 -7 C
ATOM 3051 N PHE A 503 -32.878-160.602 304.288 1.00112.59 N
ANISOU 3051 N PHE A 503 14773 13358 14650 578 1917 -246 N
ATOM 3052 CA PHE A 503 -32.116-159.395 303.992 1.00110.08 C
ANISOU 3052 CA PHE A 503 14292 13382 14153 556 1803 -309 C
ATOM 3053 C PHE A 503 -32.983-158.342 303.316 1.00106.62 C
ANISOU 3053 C PHE A 503 13579 12970 13960 392 1942 -297 C
ATOM 3054 O PHE A 503 -32.768-157.142 303.518 1.00108.64 O
ANISOU 3054 O PHE A 503 13834 13344 14102 307 1984 -282 O
ATOM 3055 CB PHE A 503 -30.908-159.735 303.118 1.00110.38 C
ANISOU 3055 CB PHE A 503 14133 13776 14032 696 1431 -476 C
ATOM 3056 CG PHE A 503 -29.821-160.477 303.846 1.00115.65 C
ANISOU 3056 CG PHE A 503 15063 14487 14393 901 1231 -541 C
ATOM 3057 CD1 PHE A 503 -29.613-160.274 305.201 1.00117.23 C
ANISOU 3057 CD1 PHE A 503 15638 14546 14358 921 1356 -444 C
ATOM 3058 CD2 PHE A 503 -29.008-161.377 303.176 1.00118.04 C
ANISOU 3058 CD2 PHE A 503 15233 14980 14635 1092 896 -722 C
ATOM 3059 CE1 PHE A 503 -28.613-160.955 305.876 1.00117.11 C
ANISOU 3059 CE1 PHE A 503 15885 14564 14048 1142 1136 -511 C
ATOM 3060 CE2 PHE A 503 -28.007-162.060 303.845 1.00119.75 C
ANISOU 3060 CE2 PHE A 503 15693 15230 14575 1326 666 -816 C
ATOM 3061 CZ PHE A 503 -27.810-161.848 305.196 1.00118.27 C
ANISOU 3061 CZ PHE A 503 15902 14885 14149 1356 779 -702 C
ATOM 3062 N CYS A 504 -33.965-158.766 302.517 1.00104.01 N
ANISOU 3062 N CYS A 504 13029 12522 13969 357 1994 -314 N
ATOM 3063 CA CYS A 504 -34.885-157.821 301.896 1.00102.52 C
ANISOU 3063 CA CYS A 504 12599 12326 14029 241 2100 -318 C
ATOM 3064 C CYS A 504 -35.929-157.294 302.870 1.00 97.48 C
ANISOU 3064 C CYS A 504 12102 11422 13516 139 2438 -259 C
ATOM 3065 O CYS A 504 -36.491-156.220 302.632 1.00 96.72 O
ANISOU 3065 O CYS A 504 11871 11329 13548 72 2501 -276 O
ATOM 3066 CB CYS A 504 -35.575-158.463 300.691 1.00105.93 C
ANISOU 3066 CB CYS A 504 12720 12753 14776 260 2022 -394 C
ATOM 3067 SG CYS A 504 -34.478-158.735 299.279 1.00104.90 S
ANISOU 3067 SG CYS A 504 12311 13025 14522 345 1624 -510 S
ATOM 3068 N SER A 505 -36.211-158.025 303.953 1.00 93.76 N
ANISOU 3068 N SER A 505 11905 10721 12998 121 2646 -202 N
ATOM 3069 CA SER A 505 -37.030-157.454 305.016 1.00 93.63 C
ANISOU 3069 CA SER A 505 12036 10522 13018 4 2977 -172 C
ATOM 3070 C SER A 505 -36.335-156.261 305.655 1.00 99.48 C
ANISOU 3070 C SER A 505 12908 11393 13495 2 2959 -148 C
ATOM 3071 O SER A 505 -36.999-155.321 306.107 1.00101.87 O
ANISOU 3071 O SER A 505 13193 11628 13884 -77 3151 -178 O
ATOM 3072 CB SER A 505 -37.352-158.515 306.069 1.00 83.81 C
ANISOU 3072 CB SER A 505 11108 9031 11706 -54 3199 -100 C
ATOM 3073 OG SER A 505 -38.224-159.505 305.548 1.00 76.74 O
ANISOU 3073 OG SER A 505 10086 7970 11101 -109 3280 -138 O
ATOM 3074 N MET A 506 -35.000-156.281 305.698 1.00102.62 N
ANISOU 3074 N MET A 506 13423 11990 13577 93 2723 -129 N
ATOM 3075 CA MET A 506 -34.239-155.119 306.134 1.00103.80 C
ANISOU 3075 CA MET A 506 13655 12303 13480 76 2672 -134 C
ATOM 3076 C MET A 506 -34.330-153.972 305.139 1.00 98.37 C
ANISOU 3076 C MET A 506 12705 11749 12922 14 2549 -180 C
ATOM 3077 O MET A 506 -34.120-152.815 305.520 1.00 93.03 O
ANISOU 3077 O MET A 506 12091 11113 12143 -47 2576 -185 O
ATOM 3078 CB MET A 506 -32.771-155.500 306.337 1.00110.13 C
ANISOU 3078 CB MET A 506 14602 13325 13917 188 2432 -151 C
ATOM 3079 CG MET A 506 -32.527-156.536 307.419 1.00118.93 C
ANISOU 3079 CG MET A 506 16057 14292 14837 281 2493 -94 C
ATOM 3080 SD MET A 506 -32.807-155.859 309.063 1.00127.04 S
ANISOU 3080 SD MET A 506 17413 15179 15678 201 2802 -27 S
ATOM 3081 CE MET A 506 -32.003-154.270 308.887 1.00130.22 C
ANISOU 3081 CE MET A 506 17678 15867 15932 161 2682 -117 C
ATOM 3082 N LEU A 507 -34.642-154.272 303.876 1.00 98.29 N
ANISOU 3082 N LEU A 507 12424 11794 13126 24 2405 -211 N
ATOM 3083 CA LEU A 507 -34.611-153.253 302.832 1.00 97.93 C
ANISOU 3083 CA LEU A 507 12174 11886 13150 -39 2238 -230 C
ATOM 3084 C LEU A 507 -35.741-152.246 303.003 1.00103.81 C
ANISOU 3084 C LEU A 507 12884 12418 14139 -90 2398 -239 C
ATOM 3085 O LEU A 507 -35.559-151.052 302.742 1.00109.53 O
ANISOU 3085 O LEU A 507 13611 13185 14819 -152 2297 -230 O
ATOM 3086 CB LEU A 507 -34.682-153.923 301.461 1.00 98.50 C
ANISOU 3086 CB LEU A 507 11973 12084 13370 -5 2042 -269 C
ATOM 3087 CG LEU A 507 -34.222-153.137 300.235 1.00 96.11 C
ANISOU 3087 CG LEU A 507 11490 12022 13004 -83 1791 -277 C
ATOM 3088 CD1 LEU A 507 -32.785-152.678 300.404 1.00 91.69 C
ANISOU 3088 CD1 LEU A 507 11039 11747 12052 -155 1645 -289 C
ATOM 3089 CD2 LEU A 507 -34.365-154.001 298.995 1.00 96.20 C
ANISOU 3089 CD2 LEU A 507 11230 12164 13159 -34 1627 -334 C
ATOM 3090 N CYS A 508 -36.918-152.706 303.435 1.00108.58 N
ANISOU 3090 N CYS A 508 13458 12794 15003 -71 2639 -277 N
ATOM 3091 CA CYS A 508 -38.014-151.776 303.682 1.00114.22 C
ANISOU 3091 CA CYS A 508 14112 13331 15954 -90 2789 -348 C
ATOM 3092 C CYS A 508 -37.753-150.923 304.916 1.00108.10 C
ANISOU 3092 C CYS A 508 13573 12507 14993 -130 2932 -348 C
ATOM 3093 O CYS A 508 -38.203-149.773 304.980 1.00109.14 O
ANISOU 3093 O CYS A 508 13680 12555 15235 -134 2932 -410 O
ATOM 3094 CB CYS A 508 -39.328-152.536 303.839 1.00128.67 C
ANISOU 3094 CB CYS A 508 15808 14983 18096 -87 3031 -442 C
ATOM 3095 SG CYS A 508 -39.480-153.378 305.424 1.00146.27 S
ANISOU 3095 SG CYS A 508 18310 17084 20182 -162 3389 -421 S
ATOM 3096 N LEU A 509 -37.042-151.469 305.906 1.00104.11 N
ANISOU 3096 N LEU A 509 13305 12045 14208 -141 3034 -292 N
ATOM 3097 CA LEU A 509 -36.664-150.674 307.070 1.00103.52 C
ANISOU 3097 CA LEU A 509 13453 11964 13915 -173 3149 -300 C
ATOM 3098 C LEU A 509 -35.751-149.522 306.672 1.00 99.18 C
ANISOU 3098 C LEU A 509 12925 11556 13204 -201 2912 -287 C
ATOM 3099 O LEU A 509 -35.828-148.429 307.246 1.00 96.23 O
ANISOU 3099 O LEU A 509 12638 11121 12805 -233 2968 -336 O
ATOM 3100 CB LEU A 509 -35.982-151.564 308.109 1.00101.63 C
ANISOU 3100 CB LEU A 509 13480 11762 13371 -160 3252 -234 C
ATOM 3101 CG LEU A 509 -35.467-150.866 309.367 1.00 95.06 C
ANISOU 3101 CG LEU A 509 12893 10963 12263 -181 3362 -247 C
ATOM 3102 CD1 LEU A 509 -36.628-150.350 310.201 1.00 93.72 C
ANISOU 3102 CD1 LEU A 509 12726 10622 12260 -240 3668 -338 C
ATOM 3103 CD2 LEU A 509 -34.586-151.805 310.178 1.00 95.06 C
ANISOU 3103 CD2 LEU A 509 13168 11032 11919 -129 3361 -172 C
ATOM 3104 N LEU A 510 -34.878-149.752 305.688 1.00 96.80 N
ANISOU 3104 N LEU A 510 12544 11454 12783 -209 2650 -239 N
ATOM 3105 CA LEU A 510 -34.033-148.680 305.176 1.00 94.91 C
ANISOU 3105 CA LEU A 510 12316 11365 12380 -297 2432 -229 C
ATOM 3106 C LEU A 510 -34.871-147.558 304.578 1.00 95.00 C
ANISOU 3106 C LEU A 510 12242 11205 12649 -334 2373 -242 C
ATOM 3107 O LEU A 510 -34.523-146.378 304.704 1.00103.62 O
ANISOU 3107 O LEU A 510 13448 12276 13648 -417 2295 -244 O
ATOM 3108 CB LEU A 510 -33.063-149.235 304.134 1.00 98.35 C
ANISOU 3108 CB LEU A 510 12635 12082 12653 -324 2182 -208 C
ATOM 3109 CG LEU A 510 -32.198-148.210 303.400 1.00102.11 C
ANISOU 3109 CG LEU A 510 13099 12754 12942 -482 1960 -199 C
ATOM 3110 CD1 LEU A 510 -30.992-147.823 304.244 1.00107.86 C
ANISOU 3110 CD1 LEU A 510 14003 13669 13311 -547 1957 -248 C
ATOM 3111 CD2 LEU A 510 -31.773-148.736 302.037 1.00101.34 C
ANISOU 3111 CD2 LEU A 510 12791 12902 12811 -524 1735 -197 C
ATOM 3112 N ASN A 511 -35.978-147.909 303.918 1.00 93.71 N
ANISOU 3112 N ASN A 511 11887 10906 12813 -265 2388 -266 N
ATOM 3113 CA ASN A 511 -36.876-146.889 303.385 1.00103.33 C
ANISOU 3113 CA ASN A 511 13029 11936 14296 -246 2303 -307 C
ATOM 3114 C ASN A 511 -37.413-145.996 304.497 1.00105.22 C
ANISOU 3114 C ASN A 511 13393 11977 14610 -218 2474 -406 C
ATOM 3115 O ASN A 511 -37.479-144.771 304.341 1.00108.09 O
ANISOU 3115 O ASN A 511 13834 12220 15014 -236 2335 -424 O
ATOM 3116 CB ASN A 511 -38.025-147.548 302.622 1.00111.49 C
ANISOU 3116 CB ASN A 511 13809 12881 15672 -146 2314 -365 C
ATOM 3117 CG ASN A 511 -38.821-146.558 301.794 1.00119.90 C
ANISOU 3117 CG ASN A 511 14784 13787 16984 -92 2127 -408 C
ATOM 3118 OD1 ASN A 511 -38.321-145.496 301.423 1.00122.75 O
ANISOU 3118 OD1 ASN A 511 15284 14131 17224 -161 1914 -337 O
ATOM 3119 ND2 ASN A 511 -40.069-146.903 301.498 1.00122.91 N
ANISOU 3119 ND2 ASN A 511 14945 14046 17709 29 2193 -536 N
ATOM 3120 N SER A 512 -37.794-146.590 305.632 1.00105.64 N
ANISOU 3120 N SER A 512 13482 11989 14668 -184 2769 -477 N
ATOM 3121 CA SER A 512 -38.241-145.789 306.767 1.00112.23 C
ANISOU 3121 CA SER A 512 14418 12687 15536 -168 2952 -601 C
ATOM 3122 C SER A 512 -37.123-144.907 307.303 1.00114.13 C
ANISOU 3122 C SER A 512 14891 13001 15473 -246 2867 -557 C
ATOM 3123 O SER A 512 -37.391-143.875 307.928 1.00110.47 O
ANISOU 3123 O SER A 512 14507 12410 15058 -234 2908 -664 O
ATOM 3124 CB SER A 512 -38.778-146.693 307.877 1.00121.57 C
ANISOU 3124 CB SER A 512 15617 13858 16717 -165 3301 -670 C
ATOM 3125 OG SER A 512 -39.895-147.446 307.434 1.00125.46 O
ANISOU 3125 OG SER A 512 15885 14276 17509 -128 3409 -747 O
ATOM 3126 N THR A 513 -35.867-145.295 307.074 1.00116.64 N
ANISOU 3126 N THR A 513 15299 13536 15482 -323 2744 -436 N
ATOM 3127 CA THR A 513 -34.745-144.465 307.497 1.00116.28 C
ANISOU 3127 CA THR A 513 15443 13598 15141 -420 2655 -423 C
ATOM 3128 C THR A 513 -34.543-143.280 306.559 1.00107.44 C
ANISOU 3128 C THR A 513 14342 12414 14065 -519 2389 -389 C
ATOM 3129 O THR A 513 -34.294-142.159 307.015 1.00109.46 O
ANISOU 3129 O THR A 513 14750 12581 14258 -582 2355 -436 O
ATOM 3130 CB THR A 513 -33.467-145.303 307.574 1.00118.60 C
ANISOU 3130 CB THR A 513 15797 14181 15085 -460 2604 -359 C
ATOM 3131 OG1 THR A 513 -33.680-146.429 308.436 1.00120.13 O
ANISOU 3131 OG1 THR A 513 16036 14381 15228 -363 2818 -365 O
ATOM 3132 CG2 THR A 513 -32.314-144.469 308.112 1.00120.87 C
ANISOU 3132 CG2 THR A 513 16254 14612 15058 -566 2537 -394 C
ATOM 3133 N VAL A 514 -34.659-143.505 305.247 1.00 96.88 N
ANISOU 3133 N VAL A 514 12873 11109 12828 -543 2192 -305 N
ATOM 3134 CA VAL A 514 -34.383-142.449 304.276 1.00 99.24 C
ANISOU 3134 CA VAL A 514 13240 11356 13109 -675 1920 -235 C
ATOM 3135 C VAL A 514 -35.578-141.543 304.013 1.00106.00 C
ANISOU 3135 C VAL A 514 14101 11869 14306 -573 1836 -285 C
ATOM 3136 O VAL A 514 -35.415-140.502 303.358 1.00101.57 O
ANISOU 3136 O VAL A 514 13677 11184 13730 -676 1596 -220 O
ATOM 3137 CB VAL A 514 -33.904-143.040 302.935 1.00 97.07 C
ANISOU 3137 CB VAL A 514 12837 11305 12742 -765 1724 -126 C
ATOM 3138 CG1 VAL A 514 -32.746-144.000 303.165 1.00 95.88 C
ANISOU 3138 CG1 VAL A 514 12648 11508 12276 -821 1774 -131 C
ATOM 3139 CG2 VAL A 514 -35.052-143.730 302.217 1.00 92.41 C
ANISOU 3139 CG2 VAL A 514 12028 10607 12477 -605 1715 -132 C
ATOM 3140 N ASN A 515 -36.773-141.899 304.497 1.00111.02 N
ANISOU 3140 N ASN A 515 14597 12346 15238 -380 2014 -415 N
ATOM 3141 CA ASN A 515 -37.936-141.046 304.248 1.00114.62 C
ANISOU 3141 CA ASN A 515 15020 12497 16033 -241 1907 -525 C
ATOM 3142 C ASN A 515 -37.849-139.712 304.979 1.00116.60 C
ANISOU 3142 C ASN A 515 15488 12545 16271 -253 1863 -611 C
ATOM 3143 O ASN A 515 -38.082-138.670 304.339 1.00120.78 O
ANISOU 3143 O ASN A 515 16137 12842 16912 -242 1587 -593 O
ATOM 3144 CB ASN A 515 -39.225-141.801 304.586 1.00116.67 C
ANISOU 3144 CB ASN A 515 15029 12694 16605 -54 2128 -698 C
ATOM 3145 CG ASN A 515 -39.631-142.774 303.498 1.00117.29 C
ANISOU 3145 CG ASN A 515 14883 12862 16819 -9 2060 -643 C
ATOM 3146 OD1 ASN A 515 -39.175-142.673 302.357 1.00113.46 O
ANISOU 3146 OD1 ASN A 515 14417 12437 16254 -77 1797 -495 O
ATOM 3147 ND2 ASN A 515 -40.497-143.719 303.842 1.00121.99 N
ANISOU 3147 ND2 ASN A 515 15264 13476 17610 82 2304 -772 N
ATOM 3148 N PRO A 516 -37.533-139.648 306.280 1.00115.77 N
ANISOU 3148 N PRO A 516 15461 12494 16031 -271 2099 -708 N
ATOM 3149 CA PRO A 516 -37.398-138.328 306.922 1.00119.05 C
ANISOU 3149 CA PRO A 516 16080 12718 16436 -288 2032 -806 C
ATOM 3150 C PRO A 516 -36.296-137.473 306.321 1.00117.81 C
ANISOU 3150 C PRO A 516 16171 12551 16040 -507 1767 -644 C
ATOM 3151 O PRO A 516 -36.290-136.254 306.535 1.00128.64 O
ANISOU 3151 O PRO A 516 17738 13683 17455 -530 1626 -705 O
ATOM 3152 CB PRO A 516 -37.108-138.672 308.390 1.00117.51 C
ANISOU 3152 CB PRO A 516 15904 12674 16072 -290 2357 -920 C
ATOM 3153 CG PRO A 516 -36.604-140.068 308.367 1.00112.47 C
ANISOU 3153 CG PRO A 516 15177 12323 15234 -342 2512 -797 C
ATOM 3154 CD PRO A 516 -37.350-140.736 307.257 1.00111.92 C
ANISOU 3154 CD PRO A 516 14905 12219 15401 -266 2423 -742 C
ATOM 3155 N ILE A 517 -35.364-138.068 305.578 1.00105.84 N
ANISOU 3155 N ILE A 517 14652 11293 14268 -684 1695 -461 N
ATOM 3156 CA ILE A 517 -34.379-137.277 304.853 1.00103.78 C
ANISOU 3156 CA ILE A 517 14606 11054 13773 -945 1448 -317 C
ATOM 3157 C ILE A 517 -34.955-136.782 303.528 1.00105.18 C
ANISOU 3157 C ILE A 517 14832 11006 14125 -946 1140 -202 C
ATOM 3158 O ILE A 517 -34.556-135.725 303.027 1.00110.68 O
ANISOU 3158 O ILE A 517 15789 11538 14725 -1131 901 -105 O
ATOM 3159 CB ILE A 517 -33.095-138.102 304.650 1.00111.83 C
ANISOU 3159 CB ILE A 517 15572 12499 14420 -1144 1503 -224 C
ATOM 3160 CG1 ILE A 517 -32.515-138.517 306.004 1.00118.12 C
ANISOU 3160 CG1 ILE A 517 16364 13489 15026 -1111 1763 -344 C
ATOM 3161 CG2 ILE A 517 -32.061-137.326 303.846 1.00115.42 C
ANISOU 3161 CG2 ILE A 517 16216 13036 14603 -1471 1276 -102 C
ATOM 3162 CD1 ILE A 517 -31.230-139.314 305.905 1.00119.02 C
ANISOU 3162 CD1 ILE A 517 16421 14025 14776 -1255 1786 -310 C
ATOM 3163 N ILE A 518 -35.912-137.513 302.956 1.00107.02 N
ANISOU 3163 N ILE A 518 14839 11215 14608 -747 1134 -213 N
ATOM 3164 CA ILE A 518 -36.471-137.136 301.661 1.00112.50 C
ANISOU 3164 CA ILE A 518 15569 11725 15452 -720 825 -110 C
ATOM 3165 C ILE A 518 -37.522-136.045 301.818 1.00116.66 C
ANISOU 3165 C ILE A 518 16218 11807 16299 -510 653 -236 C
ATOM 3166 O ILE A 518 -37.509-135.041 301.097 1.00122.06 O
ANISOU 3166 O ILE A 518 17167 12232 16978 -583 329 -128 O
ATOM 3167 CB ILE A 518 -37.048-138.375 300.950 1.00117.67 C
ANISOU 3167 CB ILE A 518 15910 12554 16245 -584 871 -101 C
ATOM 3168 CG1 ILE A 518 -35.924-139.301 300.484 1.00114.29 C
ANISOU 3168 CG1 ILE A 518 15398 12540 15488 -799 925 33 C
ATOM 3169 CG2 ILE A 518 -37.915-137.960 299.774 1.00125.50 C
ANISOU 3169 CG2 ILE A 518 16908 13315 17461 -466 560 -55 C
ATOM 3170 CD1 ILE A 518 -36.417-140.581 299.847 1.00111.75 C
ANISOU 3170 CD1 ILE A 518 14768 12395 15299 -669 977 24 C
ATOM 3171 N TYR A 519 -38.450-136.220 302.758 1.00116.57 N
ANISOU 3171 N TYR A 519 16029 11702 16561 -251 856 -481 N
ATOM 3172 CA TYR A 519 -39.581-135.311 302.907 1.00118.35 C
ANISOU 3172 CA TYR A 519 16288 11544 17135 9 692 -681 C
ATOM 3173 C TYR A 519 -39.383-134.294 304.026 1.00117.05 C
ANISOU 3173 C TYR A 519 16323 11193 16959 6 735 -828 C
ATOM 3174 O TYR A 519 -39.514-133.089 303.794 1.00116.06 O
ANISOU 3174 O TYR A 519 16463 10716 16919 36 431 -839 O
ATOM 3175 CB TYR A 519 -40.865-136.113 303.151 1.00119.93 C
ANISOU 3175 CB TYR A 519 16112 11784 17674 298 879 -926 C
ATOM 3176 CG TYR A 519 -41.120-137.183 302.112 1.00121.94 C
ANISOU 3176 CG TYR A 519 16138 12226 17968 314 858 -819 C
ATOM 3177 CD1 TYR A 519 -41.761-136.881 300.918 1.00123.36 C
ANISOU 3177 CD1 TYR A 519 16312 12231 18329 448 517 -787 C
ATOM 3178 CD2 TYR A 519 -40.716-138.495 302.326 1.00123.68 C
ANISOU 3178 CD2 TYR A 519 16163 12787 18041 210 1156 -758 C
ATOM 3179 CE1 TYR A 519 -41.993-137.856 299.965 1.00126.30 C
ANISOU 3179 CE1 TYR A 519 16459 12792 18737 466 497 -709 C
ATOM 3180 CE2 TYR A 519 -40.945-139.477 301.380 1.00124.39 C
ANISOU 3180 CE2 TYR A 519 16039 13040 18182 228 1129 -682 C
ATOM 3181 CZ TYR A 519 -41.583-139.152 300.202 1.00127.57 C
ANISOU 3181 CZ TYR A 519 16409 13294 18768 351 809 -664 C
ATOM 3182 OH TYR A 519 -41.812-140.128 299.258 1.00129.48 O
ANISOU 3182 OH TYR A 519 16421 13715 19060 373 781 -609 O
ATOM 3183 N ALA A 520 -39.073-134.758 305.239 1.00116.87 N
ANISOU 3183 N ALA A 520 16194 11386 16824 -27 1093 -944 N
ATOM 3184 CA ALA A 520 -38.960-133.846 306.374 1.00117.03 C
ANISOU 3184 CA ALA A 520 16360 11260 16845 -7 1159 -1126 C
ATOM 3185 C ALA A 520 -37.779-132.899 306.214 1.00120.73 C
ANISOU 3185 C ALA A 520 17195 11640 17036 -283 963 -952 C
ATOM 3186 O ALA A 520 -37.891-131.704 306.511 1.00130.99 O
ANISOU 3186 O ALA A 520 18717 12619 18434 -248 783 -1059 O
ATOM 3187 CB ALA A 520 -38.840-134.636 307.676 1.00116.84 C
ANISOU 3187 CB ALA A 520 16158 11525 16711 -2 1588 -1266 C
ATOM 3188 N LEU A 521 -36.638-133.411 305.751 1.00114.22 N
ANISOU 3188 N LEU A 521 16430 11102 15866 -568 994 -712 N
ATOM 3189 CA LEU A 521 -35.479-132.548 305.545 1.00115.51 C
ANISOU 3189 CA LEU A 521 16919 11229 15741 -887 831 -566 C
ATOM 3190 C LEU A 521 -35.729-131.549 304.423 1.00121.49 C
ANISOU 3190 C LEU A 521 17958 11609 16594 -948 418 -425 C
ATOM 3191 O LEU A 521 -35.265-130.405 304.489 1.00124.52 O
ANISOU 3191 O LEU A 521 18677 11743 16894 -1122 236 -395 O
ATOM 3192 CB LEU A 521 -34.240-133.390 305.250 1.00109.48 C
ANISOU 3192 CB LEU A 521 16099 10913 14586 -1169 955 -395 C
ATOM 3193 CG LEU A 521 -32.924-132.626 305.099 1.00110.01 C
ANISOU 3193 CG LEU A 521 16445 11050 14306 -1555 848 -288 C
ATOM 3194 CD1 LEU A 521 -32.526-131.978 306.418 1.00115.47 C
ANISOU 3194 CD1 LEU A 521 17243 11698 14933 -1573 994 -475 C
ATOM 3195 CD2 LEU A 521 -31.825-133.546 304.592 1.00105.31 C
ANISOU 3195 CD2 LEU A 521 15725 10934 13354 -1799 932 -163 C
ATOM 3196 N ARG A 522 -36.462-131.962 303.387 1.00123.02 N
ANISOU 3196 N ARG A 522 18044 11744 16953 -811 255 -336 N
ATOM 3197 CA ARG A 522 -36.797-131.062 302.290 1.00124.47 C
ANISOU 3197 CA ARG A 522 18518 11552 17223 -831 -168 -194 C
ATOM 3198 C ARG A 522 -37.872-130.051 302.662 1.00124.30 C
ANISOU 3198 C ARG A 522 18619 11036 17575 -508 -384 -412 C
ATOM 3199 O ARG A 522 -38.098-129.106 301.898 1.00129.96 O
ANISOU 3199 O ARG A 522 19669 11356 18355 -511 -783 -305 O
ATOM 3200 CB ARG A 522 -37.248-131.866 301.070 1.00126.13 C
ANISOU 3200 CB ARG A 522 18554 11887 17482 -761 -282 -53 C
ATOM 3201 N SER A 523 -38.535-130.223 303.803 1.00118.39 N
ANISOU 3201 N SER A 523 17620 10302 17060 -232 -147 -725 N
ATOM 3202 CA SER A 523 -39.558-129.280 304.244 1.00120.88 C
ANISOU 3202 CA SER A 523 17994 10195 17738 98 -340 -1008 C
ATOM 3203 C SER A 523 -38.895-127.988 304.702 1.00121.80 C
ANISOU 3203 C SER A 523 18521 10009 17749 -73 -505 -1005 C
ATOM 3204 O SER A 523 -38.204-127.963 305.726 1.00120.87 O
ANISOU 3204 O SER A 523 18388 10074 17462 -221 -232 -1089 O
ATOM 3205 CB SER A 523 -40.395-129.888 305.365 1.00120.38 C
ANISOU 3205 CB SER A 523 17517 10312 17909 385 8 -1368 C
ATOM 3206 OG SER A 523 -41.271-128.922 305.923 1.00123.15 O
ANISOU 3206 OG SER A 523 17899 10306 18584 688 -158 -1703 O
ATOM 3207 N LYS A 524 -39.103-126.911 303.942 1.00122.83 N
ANISOU 3207 N LYS A 524 19038 9661 17971 -53 -965 -911 N
ATOM 3208 CA LYS A 524 -38.532-125.624 304.321 1.00124.24 C
ANISOU 3208 CA LYS A 524 19649 9482 18076 -223 -1160 -910 C
ATOM 3209 C LYS A 524 -39.085-125.141 305.655 1.00125.83 C
ANISOU 3209 C LYS A 524 19714 9555 18542 67 -1042 -1329 C
ATOM 3210 O LYS A 524 -38.373-124.478 306.417 1.00130.33 O
ANISOU 3210 O LYS A 524 20478 10061 18981 -120 -977 -1387 O
ATOM 3211 CB LYS A 524 -38.798-124.591 303.225 1.00125.08 C
ANISOU 3211 CB LYS A 524 20233 9038 18256 -220 -1715 -730 C
ATOM 3212 CG LYS A 524 -38.040-123.288 303.399 1.00127.04 C
ANISOU 3212 CG LYS A 524 21016 8892 18360 -507 -1942 -642 C
ATOM 3213 N ASP A 525 -40.343-125.470 305.959 1.00124.70 N
ANISOU 3213 N ASP A 525 19215 9405 18762 508 -1003 -1651 N
ATOM 3214 CA ASP A 525 -40.938-125.025 307.216 1.00129.20 C
ANISOU 3214 CA ASP A 525 19614 9896 19581 787 -883 -2095 C
ATOM 3215 C ASP A 525 -40.368-125.790 308.404 1.00120.54 C
ANISOU 3215 C ASP A 525 18232 9297 18269 632 -340 -2188 C
ATOM 3216 O ASP A 525 -40.140-125.207 309.471 1.00115.56 O
ANISOU 3216 O ASP A 525 17643 8630 17633 633 -231 -2415 O
ATOM 3217 CB ASP A 525 -42.459-125.176 307.162 1.00137.84 C
ANISOU 3217 CB ASP A 525 20375 10889 21109 1280 -989 -2454 C
ATOM 3218 CG ASP A 525 -43.108-124.213 306.188 1.00150.99 C
ANISOU 3218 CG ASP A 525 22352 11992 23026 1526 -1592 -2455 C
ATOM 3219 OD1 ASP A 525 -42.566-123.105 305.992 1.00162.32 O
ANISOU 3219 OD1 ASP A 525 24287 13001 24387 1389 -1932 -2316 O
ATOM 3220 OD2 ASP A 525 -44.165-124.565 305.622 1.00150.69 O
ANISOU 3220 OD2 ASP A 525 22073 11927 23254 1855 -1737 -2602 O
ATOM 3221 N LEU A 526 -40.134-127.096 308.244 1.00115.37 N
ANISOU 3221 N LEU A 526 17304 9101 17432 509 -14 -2022 N
ATOM 3222 CA LEU A 526 -39.603-127.888 309.350 1.00108.85 C
ANISOU 3222 CA LEU A 526 16248 8729 16380 381 471 -2090 C
ATOM 3223 C LEU A 526 -38.209-127.421 309.747 1.00108.09 C
ANISOU 3223 C LEU A 526 16443 8700 15927 26 518 -1933 C
ATOM 3224 O LEU A 526 -37.913-127.277 310.940 1.00106.38 O
ANISOU 3224 O LEU A 526 16172 8624 15625 13 759 -2135 O
ATOM 3225 CB LEU A 526 -39.586-129.371 308.979 1.00100.64 C
ANISOU 3225 CB LEU A 526 14919 8106 15213 319 745 -1917 C
ATOM 3226 CG LEU A 526 -40.927-130.104 309.047 1.00 97.30 C
ANISOU 3226 CG LEU A 526 14098 7769 15103 633 886 -2160 C
ATOM 3227 CD1 LEU A 526 -40.760-131.542 308.599 1.00100.35 C
ANISOU 3227 CD1 LEU A 526 14265 8527 15338 520 1125 -1947 C
ATOM 3228 CD2 LEU A 526 -41.507-130.049 310.452 1.00 91.23 C
ANISOU 3228 CD2 LEU A 526 13105 7105 14454 800 1186 -2560 C
ATOM 3229 N ARG A 527 -37.340-127.174 308.762 1.00108.88 N
ANISOU 3229 N ARG A 527 16843 8724 15801 -278 296 -1594 N
ATOM 3230 CA ARG A 527 -36.000-126.685 309.067 1.00107.30 C
ANISOU 3230 CA ARG A 527 16908 8603 15259 -651 331 -1474 C
ATOM 3231 C ARG A 527 -36.046-125.349 309.796 1.00111.09 C
ANISOU 3231 C ARG A 527 17631 8703 15874 -601 173 -1708 C
ATOM 3232 O ARG A 527 -35.177-125.066 310.629 1.00112.65 O
ANISOU 3232 O ARG A 527 17900 9048 15854 -797 340 -1782 O
ATOM 3233 CB ARG A 527 -35.177-126.571 307.784 1.00109.76 C
ANISOU 3233 CB ARG A 527 17498 8885 15319 -1010 100 -1101 C
ATOM 3234 CG ARG A 527 -34.830-127.914 307.159 1.00111.28 C
ANISOU 3234 CG ARG A 527 17442 9535 15303 -1120 286 -889 C
ATOM 3235 CD ARG A 527 -34.002-127.750 305.894 1.00113.64 C
ANISOU 3235 CD ARG A 527 18000 9847 15330 -1501 64 -557 C
ATOM 3236 NE ARG A 527 -34.776-127.157 304.807 1.00119.48 N
ANISOU 3236 NE ARG A 527 18964 10150 16282 -1402 -333 -430 N
ATOM 3237 CZ ARG A 527 -34.287-126.898 303.600 1.00127.27 C
ANISOU 3237 CZ ARG A 527 20224 11068 17063 -1710 -582 -132 C
ATOM 3238 NH1 ARG A 527 -35.064-126.357 302.670 1.00133.03 N
ANISOU 3238 NH1 ARG A 527 21181 11377 17986 -1577 -965 -24 N
ATOM 3239 NH2 ARG A 527 -33.020-127.177 303.321 1.00128.93 N
ANISOU 3239 NH2 ARG A 527 20480 11646 16859 -2151 -455 37 N
ATOM 3240 N HIS A 528 -37.048-124.518 309.499 1.00112.44 N
ANISOU 3240 N HIS A 528 17927 8386 16408 -321 -166 -1851 N
ATOM 3241 CA HIS A 528 -37.240-123.292 310.266 1.00116.08 C
ANISOU 3241 CA HIS A 528 18579 8470 17054 -200 -328 -2139 C
ATOM 3242 C HIS A 528 -37.613-123.605 311.709 1.00110.25 C
ANISOU 3242 C HIS A 528 17478 8012 16399 23 42 -2529 C
ATOM 3243 O HIS A 528 -37.141-122.940 312.639 1.00109.69 O
ANISOU 3243 O HIS A 528 17507 7907 16263 -49 110 -2717 O
ATOM 3244 CB HIS A 528 -38.317-122.425 309.614 1.00129.62 C
ANISOU 3244 CB HIS A 528 20484 9606 19161 118 -807 -2244 C
ATOM 3245 CG HIS A 528 -38.012-122.035 308.200 1.00137.62 C
ANISOU 3245 CG HIS A 528 21913 10298 20076 -98 -1206 -1853 C
ATOM 3246 ND1 HIS A 528 -36.787-122.263 307.611 1.00139.99 N
ANISOU 3246 ND1 HIS A 528 22424 10802 19962 -594 -1138 -1468 N
ATOM 3247 CD2 HIS A 528 -38.776-121.434 307.257 1.00142.52 C
ANISOU 3247 CD2 HIS A 528 22785 10425 20939 111 -1684 -1799 C
ATOM 3248 CE1 HIS A 528 -36.809-121.818 306.367 1.00143.87 C
ANISOU 3248 CE1 HIS A 528 23287 10949 20430 -716 -1534 -1179 C
ATOM 3249 NE2 HIS A 528 -38.004-121.310 306.128 1.00144.99 N
ANISOU 3249 NE2 HIS A 528 23480 10646 20962 -284 -1883 -1356 N
ATOM 3250 N ALA A 529 -38.458-124.618 311.915 1.00110.08 N
ANISOU 3250 N ALA A 529 17041 8280 16506 272 291 -2660 N
ATOM 3251 CA ALA A 529 -38.851-124.995 313.267 1.00107.64 C
ANISOU 3251 CA ALA A 529 16392 8270 16235 443 672 -3015 C
ATOM 3252 C ALA A 529 -37.701-125.641 314.027 1.00106.70 C
ANISOU 3252 C ALA A 529 16235 8611 15693 153 1055 -2894 C
ATOM 3253 O ALA A 529 -37.626-125.518 315.255 1.00105.28 O
ANISOU 3253 O ALA A 529 15946 8601 15454 200 1297 -3163 O
ATOM 3254 CB ALA A 529 -40.054-125.936 313.222 1.00103.53 C
ANISOU 3254 CB ALA A 529 15459 7938 15939 727 848 -3174 C
ATOM 3255 N PHE A 530 -36.802-126.331 313.320 1.00107.76 N
ANISOU 3255 N PHE A 530 16451 8968 15526 -132 1100 -2518 N
ATOM 3256 CA PHE A 530 -35.642-126.919 313.981 1.00110.90 C
ANISOU 3256 CA PHE A 530 16825 9797 15515 -384 1405 -2423 C
ATOM 3257 C PHE A 530 -34.677-125.842 314.463 1.00116.12 C
ANISOU 3257 C PHE A 530 17769 10338 16014 -601 1307 -2487 C
ATOM 3258 O PHE A 530 -34.129-125.941 315.567 1.00116.00 O
ANISOU 3258 O PHE A 530 17685 10599 15791 -649 1563 -2642 O
ATOM 3259 CB PHE A 530 -34.934-127.890 313.039 1.00111.00 C
ANISOU 3259 CB PHE A 530 16832 10078 15266 -611 1435 -2056 C
ATOM 3260 CG PHE A 530 -33.665-128.462 313.604 1.00115.59 C
ANISOU 3260 CG PHE A 530 17404 11095 15422 -852 1681 -1974 C
ATOM 3261 CD1 PHE A 530 -33.678-129.161 314.800 1.00111.24 C
ANISOU 3261 CD1 PHE A 530 16650 10872 14743 -738 2030 -2140 C
ATOM 3262 CD2 PHE A 530 -32.461-128.310 312.934 1.00121.47 C
ANISOU 3262 CD2 PHE A 530 18343 11935 15875 -1195 1556 -1750 C
ATOM 3263 CE1 PHE A 530 -32.513-129.692 315.324 1.00109.59 C
ANISOU 3263 CE1 PHE A 530 16448 11054 14138 -916 2213 -2082 C
ATOM 3264 CE2 PHE A 530 -31.291-128.840 313.451 1.00120.89 C
ANISOU 3264 CE2 PHE A 530 18228 12288 15415 -1384 1757 -1729 C
ATOM 3265 CZ PHE A 530 -31.318-129.532 314.648 1.00114.87 C
ANISOU 3265 CZ PHE A 530 17277 11826 14542 -1221 2069 -1895 C
ATOM 3266 N ARG A 531 -34.455-124.806 313.651 1.00116.34 N
ANISOU 3266 N ARG A 531 18133 9950 16119 -745 933 -2371 N
ATOM 3267 CA ARG A 531 -33.573-123.727 314.075 1.00112.64 C
ANISOU 3267 CA ARG A 531 17955 9326 15517 -982 830 -2444 C
ATOM 3268 C ARG A 531 -34.204-122.898 315.185 1.00117.88 C
ANISOU 3268 C ARG A 531 18583 9772 16435 -716 829 -2857 C
ATOM 3269 O ARG A 531 -33.487-122.324 316.013 1.00119.75 O
ANISOU 3269 O ARG A 531 18916 10061 16523 -856 905 -3016 O
ATOM 3270 CB ARG A 531 -33.209-122.844 312.881 1.00114.97 C
ANISOU 3270 CB ARG A 531 18667 9199 15816 -1245 426 -2192 C
ATOM 3271 CG ARG A 531 -32.090-121.854 313.165 1.00118.92 C
ANISOU 3271 CG ARG A 531 19490 9590 16106 -1610 347 -2208 C
ATOM 3272 CD ARG A 531 -31.470-121.338 311.880 1.00117.28 C
ANISOU 3272 CD ARG A 531 19678 9131 15750 -2009 46 -1869 C
ATOM 3273 NE ARG A 531 -30.108-120.860 312.094 1.00103.60 N
ANISOU 3273 NE ARG A 531 18146 7545 13674 -2479 110 -1842 N
ATOM 3274 CZ ARG A 531 -29.234-120.637 311.117 1.00104.20 C
ANISOU 3274 CZ ARG A 531 18497 7617 13478 -2953 -21 -1559 C
ATOM 3275 NH1 ARG A 531 -28.014-120.205 311.404 1.00105.08 N
ANISOU 3275 NH1 ARG A 531 18744 7902 13281 -3386 68 -1599 N
ATOM 3276 NH2 ARG A 531 -29.578-120.851 309.853 1.00104.13 N
ANISOU 3276 NH2 ARG A 531 18616 7458 13492 -3009 -232 -1257 N
ATOM 3277 N SER A 532 -35.538-122.831 315.226 1.00121.01 N
ANISOU 3277 N SER A 532 18814 9953 17212 -330 744 -3072 N
ATOM 3278 CA SER A 532 -36.219-122.110 316.295 1.00127.31 C
ANISOU 3278 CA SER A 532 19514 10597 18261 -47 754 -3524 C
ATOM 3279 C SER A 532 -36.035-122.782 317.649 1.00127.79 C
ANISOU 3279 C SER A 532 19266 11171 18116 -13 1218 -3744 C
ATOM 3280 O SER A 532 -36.262-122.141 318.681 1.00129.60 O
ANISOU 3280 O SER A 532 19436 11360 18444 128 1273 -4118 O
ATOM 3281 CB SER A 532 -37.709-121.980 315.979 1.00129.95 C
ANISOU 3281 CB SER A 532 19685 10650 19040 367 562 -3746 C
ATOM 3282 OG SER A 532 -38.338-123.250 315.966 1.00128.13 O
ANISOU 3282 OG SER A 532 19074 10801 18809 499 859 -3726 O
ATOM 3283 N MET A 533 -35.633-124.057 317.666 1.00125.00 N
ANISOU 3283 N MET A 533 18732 11290 17472 -133 1536 -3525 N
ATOM 3284 CA MET A 533 -35.344-124.740 318.922 1.00123.27 C
ANISOU 3284 CA MET A 533 18293 11549 16994 -130 1955 -3678 C
ATOM 3285 C MET A 533 -34.169-124.115 319.666 1.00119.15 C
ANISOU 3285 C MET A 533 17950 11127 16196 -346 1993 -3754 C
ATOM 3286 O MET A 533 -34.081-124.258 320.890 1.00114.76 O
ANISOU 3286 O MET A 533 17250 10860 15494 -280 2266 -3999 O
ATOM 3287 CB MET A 533 -35.056-126.220 318.660 1.00128.52 C
ANISOU 3287 CB MET A 533 18804 12634 17392 -223 2217 -3387 C
ATOM 3288 CG MET A 533 -36.154-126.969 317.914 1.00134.34 C
ANISOU 3288 CG MET A 533 19344 13322 18376 -42 2214 -3304 C
ATOM 3289 SD MET A 533 -37.444-127.615 318.996 1.00138.37 S
ANISOU 3289 SD MET A 533 19473 14066 19036 240 2581 -3661 S
ATOM 3290 CE MET A 533 -36.486-128.677 320.074 1.00135.43 C
ANISOU 3290 CE MET A 533 19066 14240 18151 64 3008 -3558 C
ATOM 3291 N PHE A 534 -33.260-123.415 318.954 1.00122.58 N
ANISOU 3291 N PHE A 534 18697 11339 16539 -625 1727 -3561 N
ATOM 3292 CA PHE A 534 -32.038-122.803 319.454 1.00126.76 C
ANISOU 3292 CA PHE A 534 19410 11956 16798 -897 1733 -3612 C
ATOM 3293 C PHE A 534 -32.294-121.378 319.947 1.00134.84 C
ANISOU 3293 C PHE A 534 20601 12558 18073 -821 1519 -3936 C
ATOM 3294 O PHE A 534 -33.202-120.697 319.457 1.00138.51 O
ANISOU 3294 O PHE A 534 21164 12547 18916 -635 1231 -4014 O
ATOM 3295 CB PHE A 534 -30.975-122.782 318.359 1.00126.10 C
ANISOU 3295 CB PHE A 534 19567 11856 16487 -1283 1565 -3258 C
ATOM 3296 CG PHE A 534 -30.674-124.137 317.782 1.00127.96 C
ANISOU 3296 CG PHE A 534 19643 12489 16488 -1354 1728 -2962 C
ATOM 3297 CD1 PHE A 534 -30.294-124.271 316.456 1.00130.57 C
ANISOU 3297 CD1 PHE A 534 20121 12737 16753 -1592 1534 -2631 C
ATOM 3298 CD2 PHE A 534 -30.763-125.275 318.567 1.00124.98 C
ANISOU 3298 CD2 PHE A 534 18984 12561 15942 -1190 2066 -3018 C
ATOM 3299 CE1 PHE A 534 -30.014-125.515 315.925 1.00125.66 C
ANISOU 3299 CE1 PHE A 534 19332 12485 15927 -1641 1668 -2394 C
ATOM 3300 CE2 PHE A 534 -30.485-126.519 318.042 1.00118.46 C
ANISOU 3300 CE2 PHE A 534 18032 12061 14916 -1239 2186 -2759 C
ATOM 3301 CZ PHE A 534 -30.109-126.640 316.720 1.00119.38 C
ANISOU 3301 CZ PHE A 534 18262 12105 14995 -1452 1985 -2463 C
ATOM 3302 N PRO A 535 -31.498-120.910 320.923 1.00136.33 N
ANISOU 3302 N PRO A 535 20826 12912 18062 -943 1636 -4151 N
ATOM 3303 CA PRO A 535 -31.685-119.548 321.444 1.00141.59 C
ANISOU 3303 CA PRO A 535 21651 13179 18967 -877 1431 -4488 C
ATOM 3304 C PRO A 535 -31.381-118.471 320.416 1.00143.26 C
ANISOU 3304 C PRO A 535 22284 12825 19323 -1112 1009 -4322 C
ATOM 3305 O PRO A 535 -30.942-118.762 319.297 1.00139.53 O
ANISOU 3305 O PRO A 535 21981 12311 18725 -1368 894 -3940 O
ATOM 3306 CB PRO A 535 -30.703-119.483 322.624 1.00139.23 C
ANISOU 3306 CB PRO A 535 21287 13275 18340 -1014 1682 -4699 C
ATOM 3307 CG PRO A 535 -30.428-120.926 322.981 1.00131.87 C
ANISOU 3307 CG PRO A 535 20086 12954 17063 -993 2051 -4556 C
ATOM 3308 CD PRO A 535 -30.491-121.667 321.688 1.00131.12 C
ANISOU 3308 CD PRO A 535 20031 12826 16961 -1089 1963 -4142 C
ATOM 3309 N SER A 536 -31.641-117.220 320.775 1.00146.93 N
ANISOU 3309 N SER A 536 22937 12841 20051 -1030 765 -4613 N
ATOM 3310 CA SER A 536 -31.365-116.095 319.888 1.00149.82 C
ANISOU 3310 CA SER A 536 23775 12600 20552 -1267 339 -4469 C
ATOM 3311 C SER A 536 -30.889-114.857 320.640 1.00151.93 C
ANISOU 3311 C SER A 536 24253 12600 20874 -1376 217 -4789 C
ATOM 3312 O SER A 536 -29.927-114.911 321.401 1.00150.59 O
ANISOU 3312 O SER A 536 24003 12809 20405 -1596 464 -4903 O
ATOM 3313 CB SER A 536 -32.608-115.742 319.075 1.00151.29 C
ANISOU 3313 CB SER A 536 24080 12239 21163 -956 -29 -4438 C
ATOM 3314 OG SER A 536 -33.694-115.354 319.904 1.00153.18 O
ANISOU 3314 OG SER A 536 24106 12336 21760 -489 -68 -4902 O
TER 3315 SER A 536
HETATM 3316 N1 FMN A1201 -41.524-105.577 248.200 1.00103.11 N
HETATM 3317 C2 FMN A1201 -42.286-104.876 249.091 1.00 99.93 C
HETATM 3318 O2 FMN A1201 -41.831-104.493 250.175 1.00102.21 O
HETATM 3319 N3 FMN A1201 -43.601-104.572 248.786 1.00 98.24 N
HETATM 3320 C4 FMN A1201 -44.264-104.913 247.623 1.00100.58 C
HETATM 3321 O4 FMN A1201 -45.442-104.589 247.464 1.00 99.33 O
HETATM 3322 C4A FMN A1201 -43.449-105.654 246.677 1.00103.17 C
HETATM 3323 N5 FMN A1201 -43.985-106.006 245.544 1.00104.85 N
HETATM 3324 C5A FMN A1201 -43.197-106.696 244.634 1.00102.47 C
HETATM 3325 C6 FMN A1201 -43.747-107.046 243.401 1.00 99.98 C
HETATM 3326 C7 FMN A1201 -42.987-107.703 242.439 1.00102.62 C
HETATM 3327 C7M FMN A1201 -43.612-108.058 241.115 1.00 99.45 C
HETATM 3328 C8 FMN A1201 -41.646-108.023 242.714 1.00106.12 C
HETATM 3329 C8M FMN A1201 -40.785-108.703 241.683 1.00109.73 C
HETATM 3330 C9 FMN A1201 -41.100-107.688 243.950 1.00104.42 C
HETATM 3331 C9A FMN A1201 -41.861-107.026 244.907 1.00104.23 C
HETATM 3332 N10 FMN A1201 -41.323-106.637 246.150 1.00106.27 N
HETATM 3333 C10 FMN A1201 -42.084-105.942 247.059 1.00103.91 C
HETATM 3334 C1' FMN A1201 -39.934-106.982 246.482 1.00111.98 C
HETATM 3335 C2' FMN A1201 -39.803-108.332 247.178 1.00116.67 C
HETATM 3336 O2' FMN A1201 -40.592-108.352 248.368 1.00118.84 O
HETATM 3337 C3' FMN A1201 -38.342-108.608 247.537 1.00117.59 C
HETATM 3338 O3' FMN A1201 -37.653-109.021 246.362 1.00110.63 O
HETATM 3339 C4' FMN A1201 -38.192-109.700 248.597 1.00122.32 C
HETATM 3340 O4' FMN A1201 -36.855-109.703 249.099 1.00123.68 O
HETATM 3341 C5' FMN A1201 -38.569-111.076 248.092 1.00125.45 C
HETATM 3342 O5' FMN A1201 -38.536-111.992 249.206 1.00126.52 O
HETATM 3343 P FMN A1201 -38.423-113.582 249.070 1.00118.69 P
HETATM 3344 O1P FMN A1201 -39.471-114.088 248.141 1.00111.49 O
HETATM 3345 O2P FMN A1201 -38.558-114.135 250.494 1.00114.43 O1-
HETATM 3346 O3P FMN A1201 -37.006-113.878 248.581 1.00117.28 O1-
HETATM 3347 C1 8D0 A1202 -42.678-157.964 308.565 1.00 90.95 C
HETATM 3348 C2 8D0 A1202 -42.185-157.808 307.250 1.00 98.68 C
HETATM 3349 C3 8D0 A1202 -41.225-158.728 306.787 1.00 94.79 C
HETATM 3350 C4 8D0 A1202 -40.767-159.781 307.599 1.00 89.59 C
HETATM 3351 C5 8D0 A1202 -41.266-159.937 308.922 1.00 85.94 C
HETATM 3352 N1 8D0 A1202 -49.883-159.610 305.995 1.00 81.39 N
HETATM 3353 C10 8D0 A1202 -40.860-162.472 309.213 1.00 96.19 C
HETATM 3354 C11 8D0 A1202 -40.386-163.598 310.154 1.00 97.07 C
HETATM 3355 C12 8D0 A1202 -41.153-163.564 311.492 1.00 93.82 C
HETATM 3356 C13 8D0 A1202 -41.128-162.161 312.122 1.00 89.63 C
HETATM 3357 C14 8D0 A1202 -40.513-164.953 309.434 1.00 96.61 C
HETATM 3358 C15 8D0 A1202 -40.887-158.894 312.040 1.00 84.60 C
HETATM 3359 C16 8D0 A1202 -43.037-159.836 312.927 1.00 79.15 C
HETATM 3360 C17 8D0 A1202 -42.646-156.676 306.315 1.00101.71 C
HETATM 3361 C18 8D0 A1202 -43.870-157.135 305.473 1.00100.83 C
HETATM 3362 C19 8D0 A1202 -41.528-156.222 305.351 1.00 99.49 C
HETATM 3363 C20 8D0 A1202 -43.035-155.439 307.155 1.00101.39 C
HETATM 3364 C21 8D0 A1202 -45.148-157.478 306.270 1.00102.24 C
HETATM 3365 C22 8D0 A1202 -46.437-157.247 305.470 1.00105.85 C
HETATM 3366 C23 8D0 A1202 -46.680-158.341 304.420 1.00104.32 C
HETATM 3367 C24 8D0 A1202 -48.121-158.874 304.455 1.00 98.97 C
HETATM 3368 C25 8D0 A1202 -48.463-159.601 305.766 1.00 92.44 C
HETATM 3369 C6 8D0 A1202 -42.235-159.011 309.392 1.00 83.40 C
HETATM 3370 C7 8D0 A1202 -40.823-161.065 309.859 1.00 92.80 C
HETATM 3371 C8 8D0 A1202 -41.720-161.149 311.119 1.00 92.27 C
HETATM 3372 C9 8D0 A1202 -42.113-159.763 311.692 1.00 84.95 C
HETATM 3373 O1 8D0 A1202 -42.791-159.059 310.652 1.00 79.91 O
HETATM 3374 O2 8D0 A1202 -40.569-164.744 308.038 1.00 92.58 O
HETATM 3375 O3 8D0 A1202 -39.835-160.613 307.049 1.00 93.50 O
HETATM 3376 C1 CLR A1203 -51.283-139.354 312.194 1.00104.94 C
HETATM 3377 C2 CLR A1203 -51.296-137.964 311.555 1.00106.12 C
HETATM 3378 C3 CLR A1203 -52.374-137.926 310.475 1.00111.00 C
HETATM 3379 C4 CLR A1203 -53.740-138.044 311.153 1.00109.48 C
HETATM 3380 C5 CLR A1203 -53.772-139.350 311.932 1.00108.48 C
HETATM 3381 C6 CLR A1203 -54.886-140.019 311.945 1.00105.75 C
HETATM 3382 C7 CLR A1203 -55.015-141.395 312.535 1.00103.28 C
HETATM 3383 C8 CLR A1203 -54.037-141.599 313.700 1.00102.53 C
HETATM 3384 C9 CLR A1203 -52.637-141.114 313.309 1.00103.50 C
HETATM 3385 C10 CLR A1203 -52.633-139.664 312.854 1.00104.07 C
HETATM 3386 C11 CLR A1203 -51.651-141.330 314.453 1.00103.39 C
HETATM 3387 C12 CLR A1203 -51.567-142.817 314.829 1.00102.10 C
HETATM 3388 C13 CLR A1203 -52.957-143.374 315.166 1.00102.64 C
HETATM 3389 C14 CLR A1203 -53.901-143.093 313.957 1.00103.60 C
HETATM 3390 C15 CLR A1203 -55.176-143.824 314.389 1.00102.58 C
HETATM 3391 C16 CLR A1203 -54.604-145.156 314.943 1.00102.20 C
HETATM 3392 C17 CLR A1203 -53.114-144.895 315.301 1.00102.97 C
HETATM 3393 C18 CLR A1203 -53.538-142.665 316.395 1.00102.22 C
HETATM 3394 C19 CLR A1203 -52.773-138.782 314.098 1.00 97.24 C
HETATM 3395 C20 CLR A1203 -52.820-145.459 316.703 1.00102.51 C
HETATM 3396 C21 CLR A1203 -51.333-145.391 317.065 1.00100.76 C
HETATM 3397 C22 CLR A1203 -53.230-146.935 316.743 1.00106.68 C
HETATM 3398 C23 CLR A1203 -52.374-147.741 315.760 1.00110.60 C
HETATM 3399 C24 CLR A1203 -51.804-148.987 316.443 1.00109.92 C
HETATM 3400 C25 CLR A1203 -51.618-150.104 315.414 1.00102.80 C
HETATM 3401 C26 CLR A1203 -50.863-151.267 316.062 1.00107.03 C
HETATM 3402 C27 CLR A1203 -50.833-149.589 314.204 1.00 91.03 C
HETATM 3403 O1 CLR A1203 -52.289-136.690 309.760 1.00116.69 O
HETATM 3404 C1 PEG A1204 -53.380-130.083 313.708 1.00114.37 C
HETATM 3405 O1 PEG A1204 -54.683-129.570 313.667 1.00116.00 O
HETATM 3406 C2 PEG A1204 -52.901-130.379 312.288 1.00113.60 C
HETATM 3407 O2 PEG A1204 -51.600-130.895 312.321 1.00112.27 O
HETATM 3408 C3 PEG A1204 -51.483-132.092 313.040 1.00109.17 C
HETATM 3409 C4 PEG A1204 -50.276-132.887 312.543 1.00 98.00 C
HETATM 3410 O4 PEG A1204 -50.124-134.037 313.329 1.00 84.96 O
HETATM 3411 O HOH A1301 -52.768-134.689 301.305 1.00 61.12 O
CONECT 3316 3317 3333
CONECT 3317 3316 3318 3319
CONECT 3318 3317
CONECT 3319 3317 3320
CONECT 3320 3319 3321 3322
CONECT 3321 3320
CONECT 3322 3320 3323 3333
CONECT 3323 3322 3324
CONECT 3324 3323 3325 3331
CONECT 3325 3324 3326
CONECT 3326 3325 3327 3328
CONECT 3327 3326
CONECT 3328 3326 3329 3330
CONECT 3329 3328
CONECT 3330 3328 3331
CONECT 3331 3324 3330 3332
CONECT 3332 3331 3333 3334
CONECT 3333 3316 3322 3332
CONECT 3334 3332 3335
CONECT 3335 3334 3336 3337
CONECT 3336 3335
CONECT 3337 3335 3338 3339
CONECT 3338 3337
CONECT 3339 3337 3340 3341
CONECT 3340 3339
CONECT 3341 3339 3342
CONECT 3342 3341 3343
CONECT 3343 3342 3344 3345 3346
CONECT 3344 3343
CONECT 3345 3343
CONECT 3346 3343
CONECT 3347 3348 3369
CONECT 3348 3347 3349 3360
CONECT 3349 3348 3350
CONECT 3350 3349 3351 3375
CONECT 3351 3350 3369 3370
CONECT 3352 3368
CONECT 3353 3354 3370
CONECT 3354 3353 3355 3357
CONECT 3355 3354 3356
CONECT 3356 3355 3371
CONECT 3357 3354 3374
CONECT 3358 3372
CONECT 3359 3372
CONECT 3360 3348 3361 3362 3363
CONECT 3361 3360 3364
CONECT 3362 3360
CONECT 3363 3360
CONECT 3364 3361 3365
CONECT 3365 3364 3366
CONECT 3366 3365 3367
CONECT 3367 3366 3368
CONECT 3368 3352 3367
CONECT 3369 3347 3351 3373
CONECT 3370 3351 3353 3371
CONECT 3371 3356 3370 3372
CONECT 3372 3358 3359 3371 3373
CONECT 3373 3369 3372
CONECT 3374 3357
CONECT 3375 3350
CONECT 3376 3377 3385
CONECT 3377 3376 3378
CONECT 3378 3377 3379 3403
CONECT 3379 3378 3380
CONECT 3380 3379 3381 3385
CONECT 3381 3380 3382
CONECT 3382 3381 3383
CONECT 3383 3382 3384 3389
CONECT 3384 3383 3385 3386
CONECT 3385 3376 3380 3384 3394
CONECT 3386 3384 3387
CONECT 3387 3386 3388
CONECT 3388 3387 3389 3392 3393
CONECT 3389 3383 3388 3390
CONECT 3390 3389 3391
CONECT 3391 3390 3392
CONECT 3392 3388 3391 3395
CONECT 3393 3388
CONECT 3394 3385
CONECT 3395 3392 3396 3397
CONECT 3396 3395
CONECT 3397 3395 3398
CONECT 3398 3397 3399
CONECT 3399 3398 3400
CONECT 3400 3399 3401 3402
CONECT 3401 3400
CONECT 3402 3400
CONECT 3403 3378
CONECT 3404 3405 3406
CONECT 3405 3404
CONECT 3406 3404 3407
CONECT 3407 3406 3408
CONECT 3408 3407 3409
CONECT 3409 3408 3410
CONECT 3410 3409
MASTER 316 0 4 15 5 0 0 6 3410 1 95 34
END