examples/data/5v9o.pdb
HEADER HYDROLASE/HYDROLASE INHIBITOR 23-MAR-17 5V9O
TITLE KRAS G12C INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GTPASE KRAS;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: K-RAS 2,KI-RAS,C-K-RAS,C-KI-RAS;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: KRAS, KRAS2, RASK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333
KEYWDS KRAS MUTANT INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.WESTOVER,J.LU
REVDAT 2 30-AUG-17 5V9O 1 JRNL
REVDAT 1 23-AUG-17 5V9O 0
JRNL AUTH M.ZENG,J.LU,L.LI,F.FERU,C.QUAN,T.W.GERO,S.B.FICARRO,Y.XIONG,
JRNL AUTH 2 C.AMBROGIO,R.M.PARANAL,M.CATALANO,J.SHAO,K.K.WONG,J.A.MARTO,
JRNL AUTH 3 E.S.FISCHER,P.A.JANNE,D.A.SCOTT,K.D.WESTOVER,N.S.GRAY
JRNL TITL POTENT AND SELECTIVE COVALENT QUINAZOLINE INHIBITORS OF KRAS
JRNL TITL 2 G12C.
JRNL REF CELL CHEM BIOL V. 24 1005 2017
JRNL REFN ESSN 2451-9456
JRNL PMID 28781124
JRNL DOI 10.1016/J.CHEMBIOL.2017.06.017
REMARK 2
REMARK 2 RESOLUTION. 1.56 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.08
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 34369
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.770
REMARK 3 FREE R VALUE TEST SET COUNT : 1982
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 45.0983 - 3.7581 1.00 2484 156 0.1693 0.1656
REMARK 3 2 3.7581 - 2.9831 1.00 2396 150 0.1598 0.1857
REMARK 3 3 2.9831 - 2.6061 1.00 2385 147 0.1965 0.2066
REMARK 3 4 2.6061 - 2.3678 1.00 2360 142 0.1725 0.2077
REMARK 3 5 2.3678 - 2.1981 1.00 2347 144 0.1671 0.1844
REMARK 3 6 2.1981 - 2.0685 1.00 2371 145 0.1670 0.2114
REMARK 3 7 2.0685 - 1.9649 1.00 2341 141 0.1724 0.2030
REMARK 3 8 1.9649 - 1.8794 1.00 2346 145 0.1759 0.1958
REMARK 3 9 1.8794 - 1.8070 1.00 2348 148 0.1867 0.2136
REMARK 3 10 1.8070 - 1.7447 1.00 2347 143 0.1914 0.2167
REMARK 3 11 1.7447 - 1.6901 1.00 2315 138 0.2055 0.2150
REMARK 3 12 1.6901 - 1.6418 1.00 2331 141 0.2232 0.2264
REMARK 3 13 1.6418 - 1.5986 0.98 2286 144 0.2530 0.2826
REMARK 3 14 1.5986 - 1.5596 0.73 1730 98 0.3035 0.2843
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.840
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.88
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 : 0.006 1443
REMARK 3 ANGLE : 1.019 1957
REMARK 3 CHIRALITY : 0.054 212
REMARK 3 PLANARITY : 0.006 247
REMARK 3 DIHEDRAL : 19.567 861
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5V9O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227094.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35091
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.560
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 31.80
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.56
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 19.00
REMARK 200 R MERGE FOR SHELL (I) : 2.19200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 4OBE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH9.0, AMMONIUM SULFATE
REMARK 280 1.6M, EVAPORATION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 3
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 510 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 523 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 529 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 530 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 0
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 O HOH A 344 O HOH A 486 1.97
REMARK 500 O HOH A 400 O HOH A 491 1.99
REMARK 500 O HOH A 450 O HOH A 522 2.03
REMARK 500 O HOH A 440 O HOH A 491 2.04
REMARK 500 O HOH A 444 O HOH A 517 2.05
REMARK 500 O HOH A 470 O HOH A 517 2.09
REMARK 500 O HOH A 403 O HOH A 439 2.09
REMARK 500 O HOH A 309 O HOH A 403 2.15
REMARK 500 O HOH A 476 O HOH A 503 2.15
REMARK 500 O HOH A 474 O HOH A 493 2.15
REMARK 500 NZ LYS A 5 O HOH A 301 2.16
REMARK 500 O HOH A 324 O HOH A 390 2.18
REMARK 500 O HOH A 416 O HOH A 517 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 31 41.37 -141.12
REMARK 500 ASP A 33 116.71 -39.53
REMARK 500 ALA A 59 -24.79 -150.46
REMARK 500 LYS A 117 33.93 71.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 529 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A 530 DISTANCE = 5.85 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 17 OG
REMARK 620 2 GDP A 201 O1B 91.2
REMARK 620 3 HOH A 337 O 84.1 96.1
REMARK 620 4 HOH A 365 O 91.8 170.5 93.2
REMARK 620 5 HOH A 335 O 91.8 84.9 175.8 85.9
REMARK 620 6 HOH A 373 O 173.2 91.2 89.3 86.8 94.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 91G A 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5V9L RELATED DB: PDB
DBREF 5V9O A 1 168 UNP P01116 RASK_HUMAN 1 168
SEQADV 5V9O GLY A 0 UNP P01116 EXPRESSION TAG
SEQADV 5V9O CYS A 12 UNP P01116 GLY 12 ENGINEERED MUTATION
SEQRES 1 A 169 GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA CYS
SEQRES 2 A 169 GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN
SEQRES 3 A 169 ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP
SEQRES 4 A 169 SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS
SEQRES 5 A 169 LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR
SEQRES 6 A 169 SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY
SEQRES 7 A 169 PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE
SEQRES 8 A 169 GLU ASP ILE HIS HIS TYR ARG GLU GLN ILE LYS ARG VAL
SEQRES 9 A 169 LYS ASP SER GLU ASP VAL PRO MET VAL LEU VAL GLY ASN
SEQRES 10 A 169 LYS CYS ASP LEU PRO SER ARG THR VAL ASP THR LYS GLN
SEQRES 11 A 169 ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO PHE ILE
SEQRES 12 A 169 GLU THR SER ALA LYS THR ARG GLN GLY VAL ASP ASP ALA
SEQRES 13 A 169 PHE TYR THR LEU VAL ARG GLU ILE ARG LYS HIS LYS GLU
HET GDP A 201 28
HET MG A 202 1
HET 91G A 203 40
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM 91G N~3~-[6-CHLORO-7-(3-HYDROXYNAPHTHALEN-1-YL)-4-(4-
HETNAM 2 91G PROPANOYLPIPERAZIN-1-YL)QUINAZOLIN-2-YL]-N,N-DIMETHYL-
HETNAM 3 91G BETA-ALANINAMIDE
FORMUL 2 GDP C10 H15 N5 O11 P2
FORMUL 3 MG MG 2+
FORMUL 4 91G C30 H33 CL N6 O3
FORMUL 5 HOH *230(H2 O)
HELIX 1 AA1 GLY A 15 ASN A 26 1 12
HELIX 2 AA2 SER A 65 THR A 74 1 10
HELIX 3 AA3 ASN A 86 LYS A 104 1 19
HELIX 4 AA4 ASP A 126 GLY A 138 1 13
HELIX 5 AA5 GLY A 151 GLU A 168 1 18
SHEET 1 AA1 6 ASP A 38 ILE A 46 0
SHEET 2 AA1 6 GLU A 49 ASP A 57 -1 O LEU A 53 N LYS A 42
SHEET 3 AA1 6 GLU A 3 VAL A 9 1 N VAL A 8 O LEU A 56
SHEET 4 AA1 6 GLY A 77 ALA A 83 1 O LEU A 79 N VAL A 9
SHEET 5 AA1 6 MET A 111 ASN A 116 1 O ASN A 116 N PHE A 82
SHEET 6 AA1 6 PHE A 141 GLU A 143 1 O ILE A 142 N LEU A 113
LINK OG SER A 17 MG MG A 202 1555 1555 2.03
LINK O1B GDP A 201 MG MG A 202 1555 1555 2.08
LINK MG MG A 202 O HOH A 337 1555 1555 2.08
LINK MG MG A 202 O HOH A 365 1555 1555 2.10
LINK MG MG A 202 O HOH A 335 1555 1555 2.18
LINK MG MG A 202 O HOH A 373 1555 1555 2.12
LINK SG CYS A 12 C20 91G A 203 1555 1555 1.41
SITE 1 AC1 27 GLY A 13 VAL A 14 GLY A 15 LYS A 16
SITE 2 AC1 27 SER A 17 ALA A 18 PHE A 28 VAL A 29
SITE 3 AC1 27 ASP A 30 ASN A 116 LYS A 117 ASP A 119
SITE 4 AC1 27 LEU A 120 SER A 145 ALA A 146 LYS A 147
SITE 5 AC1 27 MG A 202 91G A 203 HOH A 321 HOH A 330
SITE 6 AC1 27 HOH A 335 HOH A 337 HOH A 373 HOH A 374
SITE 7 AC1 27 HOH A 398 HOH A 412 HOH A 431
SITE 1 AC2 6 SER A 17 GDP A 201 HOH A 335 HOH A 337
SITE 2 AC2 6 HOH A 365 HOH A 373
SITE 1 AC3 18 GLY A 10 CYS A 12 LYS A 16 ALA A 59
SITE 2 AC3 18 GLY A 60 GLN A 61 GLU A 62 GLU A 63
SITE 3 AC3 18 ARG A 68 ASP A 69 MET A 72 ASP A 92
SITE 4 AC3 18 HIS A 95 TYR A 96 GLN A 99 ILE A 100
SITE 5 AC3 18 GDP A 201 HOH A 338
CRYST1 90.159 90.159 90.159 90.00 90.00 90.00 P 2 3 12
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 0.011092 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011092 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011092 0.00000
ATOM 1 N MET A 1 -19.398 -21.550 47.643 1.00 39.77 N
ANISOU 1 N MET A 1 3805 6179 5126 -686 -1339 523 N
ATOM 2 CA MET A 1 -18.018 -22.022 47.715 1.00 29.80 C
ANISOU 2 CA MET A 1 2783 4851 3687 -754 -1218 512 C
ATOM 3 C MET A 1 -17.608 -22.327 49.152 1.00 26.11 C
ANISOU 3 C MET A 1 2226 4414 3280 -744 -1004 482 C
ATOM 4 O MET A 1 -18.222 -21.846 50.103 1.00 27.92 O
ANISOU 4 O MET A 1 2235 4700 3673 -645 -923 475 O
ATOM 5 CB MET A 1 -17.059 -20.994 47.114 1.00 33.41 C
ANISOU 5 CB MET A 1 3432 5229 4034 -648 -1252 552 C
ATOM 6 CG MET A 1 -16.952 -19.721 47.925 1.00 33.81 C
ANISOU 6 CG MET A 1 3358 5280 4210 -444 -1205 582 C
ATOM 7 SD MET A 1 -15.916 -18.469 47.157 1.00 28.30 S
ANISOU 7 SD MET A 1 2905 4466 3383 -337 -1257 632 S
ATOM 8 CE MET A 1 -16.840 -18.082 45.684 1.00 33.68 C
ANISOU 8 CE MET A 1 3618 5133 4046 -350 -1502 678 C
ATOM 9 N THR A 2 -16.555 -23.125 49.298 1.00 22.81 N
ANISOU 9 N THR A 2 1996 3947 2725 -847 -902 451 N
ATOM 10 CA THR A 2 -16.081 -23.516 50.618 1.00 21.97 C
ANISOU 10 CA THR A 2 1851 3850 2646 -856 -706 423 C
ATOM 11 C THR A 2 -15.389 -22.347 51.305 1.00 19.54 C
ANISOU 11 C THR A 2 1557 3501 2365 -649 -594 432 C
ATOM 12 O THR A 2 -14.668 -21.566 50.674 1.00 19.38 O
ANISOU 12 O THR A 2 1675 3421 2269 -560 -650 452 O
ATOM 13 CB THR A 2 -15.121 -24.703 50.503 1.00 20.51 C
ANISOU 13 CB THR A 2 1911 3559 2322 -982 -630 367 C
ATOM 14 OG1 THR A 2 -15.783 -25.788 49.840 1.00 27.35 O
ANISOU 14 OG1 THR A 2 2805 4422 3163 -1153 -719 345 O
ATOM 15 CG2 THR A 2 -14.651 -25.167 51.882 1.00 21.03 C
ANISOU 15 CG2 THR A 2 1995 3577 2419 -965 -423 340 C
ATOM 16 N GLU A 3 -15.604 -22.228 52.610 1.00 18.10 N
ANISOU 16 N GLU A 3 1249 3350 2280 -590 -428 414 N
ATOM 17 CA GLU A 3 -14.920 -21.238 53.425 1.00 16.84 C
ANISOU 17 CA GLU A 3 1122 3141 2134 -415 -302 406 C
ATOM 18 C GLU A 3 -13.977 -21.952 54.386 1.00 16.98 C
ANISOU 18 C GLU A 3 1293 3084 2073 -456 -129 366 C
ATOM 19 O GLU A 3 -14.358 -22.952 55.006 1.00 22.18 O
ANISOU 19 O GLU A 3 1919 3769 2741 -582 -52 353 O
ATOM 20 CB GLU A 3 -15.931 -20.380 54.190 1.00 21.52 C
ANISOU 20 CB GLU A 3 1453 3824 2898 -297 -253 405 C
ATOM 21 CG GLU A 3 -15.365 -19.075 54.745 1.00 31.54 C
ANISOU 21 CG GLU A 3 2754 5035 4195 -95 -184 398 C
ATOM 22 CD GLU A 3 -16.457 -18.158 55.272 1.00 42.01 C
ANISOU 22 CD GLU A 3 3834 6420 5708 38 -155 373 C
ATOM 23 OE1 GLU A 3 -17.643 -18.516 55.126 1.00 41.96 O
ANISOU 23 OE1 GLU A 3 3661 6469 5812 -22 -200 348 O
ATOM 24 OE2 GLU A 3 -16.130 -17.085 55.827 1.00 43.43 O
ANISOU 24 OE2 GLU A 3 4037 6538 5926 199 -82 347 O
ATOM 25 N TYR A 4 -12.753 -21.450 54.498 1.00 14.92 N
ANISOU 25 N TYR A 4 1203 2727 1740 -360 -81 355 N
ATOM 26 CA TYR A 4 -11.734 -22.027 55.367 1.00 14.58 C
ANISOU 26 CA TYR A 4 1308 2599 1632 -377 46 324 C
ATOM 27 C TYR A 4 -11.409 -21.040 56.475 1.00 13.41 C
ANISOU 27 C TYR A 4 1140 2442 1514 -240 160 315 C
ATOM 28 O TYR A 4 -11.004 -19.906 56.203 1.00 14.66 O
ANISOU 28 O TYR A 4 1318 2573 1681 -114 133 319 O
ATOM 29 CB TYR A 4 -10.469 -22.373 54.585 1.00 14.35 C
ANISOU 29 CB TYR A 4 1485 2464 1504 -393 10 299 C
ATOM 30 CG TYR A 4 -10.707 -23.413 53.526 1.00 14.98 C
ANISOU 30 CG TYR A 4 1621 2537 1534 -537 -84 285 C
ATOM 31 CD1 TYR A 4 -10.876 -24.745 53.873 1.00 16.05 C
ANISOU 31 CD1 TYR A 4 1794 2642 1664 -669 -56 266 C
ATOM 32 CD2 TYR A 4 -10.782 -23.066 52.184 1.00 14.68 C
ANISOU 32 CD2 TYR A 4 1620 2515 1443 -556 -207 293 C
ATOM 33 CE1 TYR A 4 -11.105 -25.711 52.907 1.00 19.29 C
ANISOU 33 CE1 TYR A 4 2270 3032 2028 -809 -142 240 C
ATOM 34 CE2 TYR A 4 -11.010 -24.024 51.209 1.00 14.60 C
ANISOU 34 CE2 TYR A 4 1682 2497 1367 -703 -294 268 C
ATOM 35 CZ TYR A 4 -11.171 -25.343 51.584 1.00 16.92 C
ANISOU 35 CZ TYR A 4 2004 2755 1668 -826 -258 234 C
ATOM 36 OH TYR A 4 -11.397 -26.304 50.637 1.00 17.82 O
ANISOU 36 OH TYR A 4 2205 2848 1718 -978 -342 197 O
ATOM 37 N LYS A 5 -11.561 -21.479 57.722 1.00 14.89 N
ANISOU 37 N LYS A 5 1315 2642 1702 -279 285 303 N
ATOM 38 CA LYS A 5 -11.209 -20.660 58.874 1.00 13.03 C
ANISOU 38 CA LYS A 5 1094 2391 1464 -175 401 282 C
ATOM 39 C LYS A 5 -9.746 -20.912 59.224 1.00 13.35 C
ANISOU 39 C LYS A 5 1347 2307 1419 -161 410 270 C
ATOM 40 O LYS A 5 -9.405 -21.973 59.759 1.00 13.18 O
ANISOU 40 O LYS A 5 1437 2209 1362 -244 422 264 O
ATOM 41 CB LYS A 5 -12.119 -20.986 60.053 1.00 16.01 C
ANISOU 41 CB LYS A 5 1412 2794 1877 -232 512 252 C
ATOM 42 CG LYS A 5 -11.792 -20.209 61.307 1.00 30.19 C
ANISOU 42 CG LYS A 5 3294 4516 3662 -149 613 202 C
ATOM 43 CD LYS A 5 -11.829 -18.723 61.045 1.00 39.14 C
ANISOU 43 CD LYS A 5 4349 5666 4858 6 603 175 C
ATOM 44 CE LYS A 5 -10.642 -18.047 61.694 1.00 43.58 C
ANISOU 44 CE LYS A 5 5085 6116 5358 69 614 141 C
ATOM 45 NZ LYS A 5 -10.598 -16.611 61.333 1.00 53.19 N
ANISOU 45 NZ LYS A 5 6254 7324 6633 216 585 127 N
ATOM 46 N LEU A 6 -8.886 -19.937 58.931 1.00 10.74 N
ANISOU 46 N LEU A 6 1075 1927 1078 -46 385 261 N
ATOM 47 CA LEU A 6 -7.457 -20.017 59.213 1.00 8.72 C
ANISOU 47 CA LEU A 6 990 1535 788 -24 367 226 C
ATOM 48 C LEU A 6 -7.121 -19.134 60.405 1.00 13.57 C
ANISOU 48 C LEU A 6 1644 2095 1417 37 407 183 C
ATOM 49 O LEU A 6 -7.679 -18.044 60.557 1.00 16.08 O
ANISOU 49 O LEU A 6 1887 2453 1770 117 435 177 O
ATOM 50 CB LEU A 6 -6.624 -19.578 58.006 1.00 11.10 C
ANISOU 50 CB LEU A 6 1340 1808 1070 16 305 228 C
ATOM 51 CG LEU A 6 -7.047 -20.166 56.664 1.00 11.74 C
ANISOU 51 CG LEU A 6 1401 1926 1132 -60 231 245 C
ATOM 52 CD1 LEU A 6 -6.102 -19.709 55.546 1.00 12.99 C
ANISOU 52 CD1 LEU A 6 1650 2035 1252 -39 188 228 C
ATOM 53 CD2 LEU A 6 -7.082 -21.674 56.758 1.00 14.73 C
ANISOU 53 CD2 LEU A 6 1824 2280 1494 -176 232 233 C
ATOM 54 N VAL A 7 -6.212 -19.601 61.257 1.00 9.30 N
ANISOU 54 N VAL A 7 1210 1480 845 -4 396 157 N
ATOM 55 CA VAL A 7 -5.822 -18.858 62.447 1.00 9.98 C
ANISOU 55 CA VAL A 7 1328 1546 918 22 409 126 C
ATOM 56 C VAL A 7 -4.311 -18.700 62.423 1.00 10.85 C
ANISOU 56 C VAL A 7 1506 1581 1036 57 338 120 C
ATOM 57 O VAL A 7 -3.582 -19.697 62.342 1.00 9.71 O
ANISOU 57 O VAL A 7 1408 1402 880 28 300 136 O
ATOM 58 CB VAL A 7 -6.268 -19.556 63.743 1.00 8.64 C
ANISOU 58 CB VAL A 7 1182 1420 682 -66 453 131 C
ATOM 59 CG1 VAL A 7 -5.848 -18.727 64.949 1.00 10.50 C
ANISOU 59 CG1 VAL A 7 1453 1652 885 -29 463 107 C
ATOM 60 CG2 VAL A 7 -7.775 -19.756 63.753 1.00 10.31 C
ANISOU 60 CG2 VAL A 7 1321 1679 917 -111 555 122 C
ATOM 61 N VAL A 8 -3.840 -17.456 62.495 1.00 8.41 N
ANISOU 61 N VAL A 8 1201 1240 754 126 330 99 N
ATOM 62 CA VAL A 8 -2.414 -17.146 62.477 1.00 6.86 C
ANISOU 62 CA VAL A 8 1055 976 576 154 284 89 C
ATOM 63 C VAL A 8 -1.943 -16.964 63.912 1.00 9.34 C
ANISOU 63 C VAL A 8 1432 1268 850 152 288 81 C
ATOM 64 O VAL A 8 -2.419 -16.065 64.619 1.00 8.84 O
ANISOU 64 O VAL A 8 1370 1219 768 168 325 62 O
ATOM 65 CB VAL A 8 -2.138 -15.874 61.660 1.00 9.39 C
ANISOU 65 CB VAL A 8 1362 1273 931 209 274 84 C
ATOM 66 CG1 VAL A 8 -0.639 -15.615 61.551 1.00 9.16 C
ANISOU 66 CG1 VAL A 8 1374 1186 919 216 242 70 C
ATOM 67 CG2 VAL A 8 -2.778 -15.995 60.284 1.00 9.60 C
ANISOU 67 CG2 VAL A 8 1347 1335 966 211 272 103 C
ATOM 68 N VAL A 9 -0.997 -17.803 64.348 1.00 7.93 N
ANISOU 68 N VAL A 9 1319 1046 648 137 251 93 N
ATOM 69 CA VAL A 9 -0.512 -17.795 65.725 1.00 6.49 C
ANISOU 69 CA VAL A 9 1226 837 403 123 235 97 C
ATOM 70 C VAL A 9 1.008 -17.701 65.719 1.00 9.94 C
ANISOU 70 C VAL A 9 1732 1199 846 162 172 90 C
ATOM 71 O VAL A 9 1.666 -17.926 64.702 1.00 9.58 O
ANISOU 71 O VAL A 9 1666 1129 844 198 158 83 O
ATOM 72 CB VAL A 9 -0.960 -19.038 66.527 1.00 7.98 C
ANISOU 72 CB VAL A 9 1467 1036 528 55 228 139 C
ATOM 73 CG1 VAL A 9 -2.479 -19.126 66.544 1.00 11.19 C
ANISOU 73 CG1 VAL A 9 1798 1538 917 13 303 144 C
ATOM 74 CG2 VAL A 9 -0.370 -20.306 65.940 1.00 10.58 C
ANISOU 74 CG2 VAL A 9 1835 1306 880 48 170 171 C
ATOM 75 N GLY A 10 1.553 -17.423 66.898 1.00 10.54 N
ANISOU 75 N GLY A 10 1899 1244 863 150 131 88 N
ATOM 76 CA GLY A 10 2.979 -17.228 67.071 1.00 10.17 C
ANISOU 76 CA GLY A 10 1924 1131 809 181 37 78 C
ATOM 77 C GLY A 10 3.288 -16.063 67.991 1.00 10.55 C
ANISOU 77 C GLY A 10 2032 1169 809 172 27 47 C
ATOM 78 O GLY A 10 2.421 -15.223 68.283 1.00 10.02 O
ANISOU 78 O GLY A 10 1939 1139 729 165 114 27 O
ATOM 79 N ALA A 11 4.541 -15.999 68.441 1.00 9.97 N
ANISOU 79 N ALA A 11 2033 1038 718 175 -101 42 N
ATOM 80 CA ALA A 11 4.965 -15.018 69.426 1.00 11.88 C
ANISOU 80 CA ALA A 11 2354 1257 901 145 -139 12 C
ATOM 81 C ALA A 11 4.804 -13.579 68.941 1.00 11.98 C
ANISOU 81 C ALA A 11 2333 1283 936 173 -46 -41 C
ATOM 82 O ALA A 11 4.678 -13.276 67.747 1.00 10.09 O
ANISOU 82 O ALA A 11 2005 1060 767 214 20 -51 O
ATOM 83 CB ALA A 11 6.426 -15.262 69.814 1.00 13.23 C
ANISOU 83 CB ALA A 11 2570 1364 1091 138 -341 15 C
ATOM 84 N CYS A 12 4.828 -12.671 69.910 1.00 12.92 N
ANISOU 84 N CYS A 12 2528 1384 998 140 -46 -70 N
ATOM 85 CA CYS A 12 4.751 -11.252 69.609 1.00 13.56 C
ANISOU 85 CA CYS A 12 2594 1452 1106 159 19 -115 C
ATOM 86 C CYS A 12 5.894 -10.836 68.693 1.00 13.54 C
ANISOU 86 C CYS A 12 2562 1413 1168 168 -40 -147 C
ATOM 87 O CYS A 12 7.056 -11.181 68.933 1.00 15.06 O
ANISOU 87 O CYS A 12 2783 1571 1368 137 -181 -171 O
ATOM 88 CB CYS A 12 4.803 -10.452 70.905 1.00 18.09 C
ANISOU 88 CB CYS A 12 3279 1999 1595 114 6 -150 C
ATOM 89 SG CYS A 12 4.134 -8.802 70.759 1.00 27.06 S
ANISOU 89 SG CYS A 12 4404 3127 2752 149 127 -199 S
ATOM 90 N GLY A 13 5.558 -10.118 67.624 1.00 9.22 N
ANISOU 90 N GLY A 13 1938 872 692 197 48 -150 N
ATOM 91 CA GLY A 13 6.546 -9.521 66.753 1.00 12.00 C
ANISOU 91 CA GLY A 13 2259 1184 1118 179 29 -189 C
ATOM 92 C GLY A 13 7.102 -10.409 65.657 1.00 11.86 C
ANISOU 92 C GLY A 13 2116 1190 1199 181 22 -177 C
ATOM 93 O GLY A 13 8.009 -9.971 64.935 1.00 13.42 O
ANISOU 93 O GLY A 13 2241 1371 1487 137 19 -203 O
ATOM 94 N VAL A 14 6.591 -11.629 65.493 1.00 10.17 N
ANISOU 94 N VAL A 14 1860 1021 983 215 31 -139 N
ATOM 95 CA VAL A 14 7.139 -12.524 64.472 1.00 9.21 C
ANISOU 95 CA VAL A 14 1609 921 970 215 30 -137 C
ATOM 96 C VAL A 14 6.684 -12.161 63.062 1.00 9.13 C
ANISOU 96 C VAL A 14 1556 936 978 215 144 -131 C
ATOM 97 O VAL A 14 7.300 -12.611 62.083 1.00 10.22 O
ANISOU 97 O VAL A 14 1600 1088 1195 192 170 -153 O
ATOM 98 CB VAL A 14 6.781 -13.999 64.744 1.00 8.67 C
ANISOU 98 CB VAL A 14 1531 868 896 242 -11 -100 C
ATOM 99 CG1 VAL A 14 7.389 -14.473 66.051 1.00 10.82 C
ANISOU 99 CG1 VAL A 14 1859 1100 1152 231 -157 -90 C
ATOM 100 CG2 VAL A 14 5.262 -14.256 64.715 1.00 10.78 C
ANISOU 100 CG2 VAL A 14 1853 1177 1065 265 75 -55 C
ATOM 101 N GLY A 15 5.608 -11.392 62.935 1.00 9.62 N
ANISOU 101 N GLY A 15 1660 1014 982 226 193 -92 N
ATOM 102 CA GLY A 15 5.091 -11.033 61.632 1.00 9.27 C
ANISOU 102 CA GLY A 15 1576 990 955 211 244 -57 C
ATOM 103 C GLY A 15 3.682 -11.507 61.319 1.00 7.76 C
ANISOU 103 C GLY A 15 1351 842 756 233 244 -2 C
ATOM 104 O GLY A 15 3.311 -11.554 60.140 1.00 8.60 O
ANISOU 104 O GLY A 15 1433 962 873 222 262 18 O
ATOM 105 N LYS A 16 2.894 -11.873 62.335 1.00 7.72 N
ANISOU 105 N LYS A 16 1352 851 729 258 230 10 N
ATOM 106 CA LYS A 16 1.534 -12.349 62.071 1.00 8.24 C
ANISOU 106 CA LYS A 16 1373 956 801 272 239 39 C
ATOM 107 C LYS A 16 0.722 -11.300 61.330 1.00 8.88 C
ANISOU 107 C LYS A 16 1461 1029 883 310 262 61 C
ATOM 108 O LYS A 16 0.085 -11.596 60.308 1.00 8.55 O
ANISOU 108 O LYS A 16 1389 1013 847 320 265 86 O
ATOM 109 CB LYS A 16 0.832 -12.721 63.377 1.00 7.60 C
ANISOU 109 CB LYS A 16 1306 893 690 278 249 33 C
ATOM 110 CG LYS A 16 1.546 -13.815 64.154 1.00 7.08 C
ANISOU 110 CG LYS A 16 1277 820 594 256 223 26 C
ATOM 111 CD LYS A 16 0.801 -14.190 65.427 1.00 9.60 C
ANISOU 111 CD LYS A 16 1630 1160 856 236 241 24 C
ATOM 112 CE LYS A 16 0.704 -13.034 66.431 1.00 11.27 C
ANISOU 112 CE LYS A 16 1901 1355 1025 244 264 -6 C
ATOM 113 NZ LYS A 16 2.017 -12.547 66.963 1.00 8.36 N
ANISOU 113 NZ LYS A 16 1624 930 624 242 215 -27 N
ATOM 114 N SER A 17 0.720 -10.067 61.844 1.00 6.64 N
ANISOU 114 N SER A 17 1236 704 581 342 279 51 N
ATOM 115 CA SER A 17 -0.061 -9.007 61.222 1.00 8.48 C
ANISOU 115 CA SER A 17 1500 914 807 407 303 73 C
ATOM 116 C SER A 17 0.502 -8.643 59.856 1.00 10.45 C
ANISOU 116 C SER A 17 1803 1124 1042 401 307 100 C
ATOM 117 O SER A 17 -0.251 -8.451 58.897 1.00 9.99 O
ANISOU 117 O SER A 17 1762 1067 966 458 316 137 O
ATOM 118 CB SER A 17 -0.098 -7.784 62.142 1.00 8.98 C
ANISOU 118 CB SER A 17 1620 926 865 436 319 34 C
ATOM 119 OG SER A 17 -0.767 -8.108 63.351 1.00 9.86 O
ANISOU 119 OG SER A 17 1698 1074 975 443 341 1 O
ATOM 120 N ALA A 18 1.822 -8.566 59.743 1.00 8.17 N
ANISOU 120 N ALA A 18 1547 800 756 334 307 75 N
ATOM 121 CA ALA A 18 2.416 -8.207 58.458 1.00 9.62 C
ANISOU 121 CA ALA A 18 1796 943 916 292 334 86 C
ATOM 122 C ALA A 18 2.145 -9.272 57.403 1.00 10.94 C
ANISOU 122 C ALA A 18 1880 1186 1092 247 317 100 C
ATOM 123 O ALA A 18 1.873 -8.944 56.242 1.00 9.95 O
ANISOU 123 O ALA A 18 1791 1060 931 214 305 136 O
ATOM 124 CB ALA A 18 3.916 -7.970 58.612 1.00 12.09 C
ANISOU 124 CB ALA A 18 2132 1224 1236 204 356 38 C
ATOM 125 N LEU A 19 2.234 -10.550 57.775 1.00 9.38 N
ANISOU 125 N LEU A 19 1584 1048 932 226 297 74 N
ATOM 126 CA LEU A 19 1.897 -11.599 56.827 1.00 8.44 C
ANISOU 126 CA LEU A 19 1410 988 810 184 284 76 C
ATOM 127 C LEU A 19 0.449 -11.477 56.386 1.00 8.24 C
ANISOU 127 C LEU A 19 1390 989 752 233 266 125 C
ATOM 128 O LEU A 19 0.141 -11.548 55.192 1.00 9.82 O
ANISOU 128 O LEU A 19 1608 1213 909 188 247 153 O
ATOM 129 CB LEU A 19 2.144 -12.973 57.442 1.00 8.46 C
ANISOU 129 CB LEU A 19 1342 1025 849 169 267 46 C
ATOM 130 CG LEU A 19 3.607 -13.421 57.553 1.00 8.39 C
ANISOU 130 CG LEU A 19 1312 1008 868 132 287 -4 C
ATOM 131 CD1 LEU A 19 3.706 -14.658 58.433 1.00 11.03 C
ANISOU 131 CD1 LEU A 19 1615 1350 1226 152 264 -20 C
ATOM 132 CD2 LEU A 19 4.187 -13.724 56.181 1.00 9.66 C
ANISOU 132 CD2 LEU A 19 1459 1189 1021 71 323 -33 C
ATOM 133 N THR A 20 -0.453 -11.285 57.348 1.00 8.42 N
ANISOU 133 N THR A 20 1397 1015 786 321 271 140 N
ATOM 134 CA THR A 20 -1.873 -11.220 57.030 1.00 10.07 C
ANISOU 134 CA THR A 20 1587 1273 966 395 267 195 C
ATOM 135 C THR A 20 -2.189 -10.011 56.157 1.00 10.40 C
ANISOU 135 C THR A 20 1701 1264 986 432 219 261 C
ATOM 136 O THR A 20 -2.912 -10.126 55.163 1.00 10.63 O
ANISOU 136 O THR A 20 1718 1321 1000 417 148 316 O
ATOM 137 CB THR A 20 -2.681 -11.183 58.323 1.00 11.29 C
ANISOU 137 CB THR A 20 1691 1450 1147 476 303 184 C
ATOM 138 OG1 THR A 20 -2.378 -12.353 59.105 1.00 10.33 O
ANISOU 138 OG1 THR A 20 1521 1347 1056 385 286 144 O
ATOM 139 CG2 THR A 20 -4.178 -11.127 58.009 1.00 13.87 C
ANISOU 139 CG2 THR A 20 1929 1837 1505 554 290 222 C
ATOM 140 N ILE A 21 -1.646 -8.838 56.507 1.00 10.20 N
ANISOU 140 N ILE A 21 1751 1148 975 459 227 249 N
ATOM 141 CA ILE A 21 -1.921 -7.641 55.714 1.00 10.35 C
ANISOU 141 CA ILE A 21 1834 1093 1007 466 152 298 C
ATOM 142 C ILE A 21 -1.283 -7.733 54.322 1.00 10.76 C
ANISOU 142 C ILE A 21 1946 1148 994 329 117 330 C
ATOM 143 O ILE A 21 -1.844 -7.227 53.340 1.00 12.35 O
ANISOU 143 O ILE A 21 2185 1326 1181 313 26 402 O
ATOM 144 CB ILE A 21 -1.462 -6.385 56.492 1.00 12.78 C
ANISOU 144 CB ILE A 21 2208 1300 1349 503 171 263 C
ATOM 145 CG1 ILE A 21 -2.259 -6.232 57.791 1.00 16.89 C
ANISOU 145 CG1 ILE A 21 2652 1835 1929 608 206 210 C
ATOM 146 CG2 ILE A 21 -1.598 -5.141 55.635 1.00 12.26 C
ANISOU 146 CG2 ILE A 21 2223 1139 1297 490 85 320 C
ATOM 147 CD1 ILE A 21 -3.751 -6.104 57.608 1.00 20.09 C
ANISOU 147 CD1 ILE A 21 2958 2263 2412 703 155 237 C
ATOM 148 N GLN A 22 -0.128 -8.395 54.184 1.00 9.61 N
ANISOU 148 N GLN A 22 1797 1035 820 226 182 275 N
ATOM 149 CA GLN A 22 0.383 -8.613 52.834 1.00 10.43 C
ANISOU 149 CA GLN A 22 1931 1165 866 98 172 287 C
ATOM 150 C GLN A 22 -0.584 -9.466 52.028 1.00 9.54 C
ANISOU 150 C GLN A 22 1780 1128 718 82 116 325 C
ATOM 151 O GLN A 22 -0.885 -9.150 50.868 1.00 13.27 O
ANISOU 151 O GLN A 22 2308 1602 1131 29 57 384 O
ATOM 152 CB GLN A 22 1.762 -9.267 52.866 1.00 11.28 C
ANISOU 152 CB GLN A 22 2001 1299 984 16 256 204 C
ATOM 153 CG GLN A 22 2.904 -8.301 53.096 1.00 13.51 C
ANISOU 153 CG GLN A 22 2349 1511 1272 -30 303 183 C
ATOM 154 CD GLN A 22 3.256 -7.455 51.864 1.00 14.21 C
ANISOU 154 CD GLN A 22 2537 1568 1295 -131 296 222 C
ATOM 155 OE1 GLN A 22 2.463 -7.301 50.929 1.00 13.39 O
ANISOU 155 OE1 GLN A 22 2477 1473 1139 -142 232 286 O
ATOM 156 NE2 GLN A 22 4.465 -6.913 51.864 1.00 16.82 N
ANISOU 156 NE2 GLN A 22 2905 1859 1626 -216 360 185 N
ATOM 157 N LEU A 23 -1.110 -10.529 52.640 1.00 10.87 N
ANISOU 157 N LEU A 23 1862 1354 914 123 129 295 N
ATOM 158 CA LEU A 23 -2.066 -11.374 51.934 1.00 10.43 C
ANISOU 158 CA LEU A 23 1778 1368 818 97 72 331 C
ATOM 159 C LEU A 23 -3.306 -10.588 51.529 1.00 11.78 C
ANISOU 159 C LEU A 23 1972 1520 985 164 -50 435 C
ATOM 160 O LEU A 23 -3.772 -10.683 50.386 1.00 14.34 O
ANISOU 160 O LEU A 23 2322 1877 1250 108 -131 493 O
ATOM 161 CB LEU A 23 -2.455 -12.568 52.798 1.00 11.83 C
ANISOU 161 CB LEU A 23 1865 1596 1032 131 109 286 C
ATOM 162 CG LEU A 23 -3.388 -13.549 52.088 1.00 12.40 C
ANISOU 162 CG LEU A 23 1921 1739 1052 86 52 318 C
ATOM 163 CD1 LEU A 23 -2.616 -14.442 51.154 1.00 17.93 C
ANISOU 163 CD1 LEU A 23 2632 2475 1705 -19 88 265 C
ATOM 164 CD2 LEU A 23 -4.067 -14.370 53.129 1.00 14.90 C
ANISOU 164 CD2 LEU A 23 2139 2108 1414 150 84 306 C
ATOM 165 N ILE A 24 -3.855 -9.798 52.457 1.00 11.02 N
ANISOU 165 N ILE A 24 1843 1374 970 303 -64 452 N
ATOM 166 CA ILE A 24 -5.150 -9.164 52.226 1.00 13.83 C
ANISOU 166 CA ILE A 24 2155 1712 1388 402 -193 530 C
ATOM 167 C ILE A 24 -5.014 -7.890 51.395 1.00 15.66 C
ANISOU 167 C ILE A 24 2484 1850 1616 375 -281 599 C
ATOM 168 O ILE A 24 -5.807 -7.650 50.474 1.00 18.29 O
ANISOU 168 O ILE A 24 2811 2192 1946 375 -406 686 O
ATOM 169 CB ILE A 24 -5.836 -8.885 53.579 1.00 11.91 C
ANISOU 169 CB ILE A 24 1788 1469 1268 567 -144 492 C
ATOM 170 CG1 ILE A 24 -6.064 -10.190 54.342 1.00 13.89 C
ANISOU 170 CG1 ILE A 24 1923 1834 1522 562 -51 440 C
ATOM 171 CG2 ILE A 24 -7.143 -8.115 53.365 1.00 15.97 C
ANISOU 171 CG2 ILE A 24 2211 1952 1905 675 -272 538 C
ATOM 172 CD1 ILE A 24 -6.985 -11.177 53.633 1.00 15.35 C
ANISOU 172 CD1 ILE A 24 2014 2120 1700 506 -130 472 C
ATOM 173 N GLN A 25 -4.029 -7.046 51.713 1.00 16.51 N
ANISOU 173 N GLN A 25 2676 1876 1722 358 -213 567 N
ATOM 174 CA GLN A 25 -3.942 -5.696 51.172 1.00 15.13 C
ANISOU 174 CA GLN A 25 2591 1598 1559 357 -280 629 C
ATOM 175 C GLN A 25 -2.729 -5.453 50.284 1.00 19.07 C
ANISOU 175 C GLN A 25 3218 2084 1945 206 -231 628 C
ATOM 176 O GLN A 25 -2.652 -4.395 49.648 1.00 21.03 O
ANISOU 176 O GLN A 25 3567 2249 2174 184 -289 687 O
ATOM 177 CB GLN A 25 -3.934 -4.677 52.322 1.00 18.04 C
ANISOU 177 CB GLN A 25 2957 1865 2034 472 -252 586 C
ATOM 178 CG GLN A 25 -5.204 -4.711 53.171 1.00 25.28 C
ANISOU 178 CG GLN A 25 3730 2789 3086 635 -281 563 C
ATOM 179 CD GLN A 25 -5.142 -3.781 54.373 1.00 29.95 C
ANISOU 179 CD GLN A 25 4314 3296 3770 733 -217 486 C
ATOM 180 OE1 GLN A 25 -4.235 -2.959 54.490 1.00 38.63 O
ANISOU 180 OE1 GLN A 25 5529 4309 4840 687 -189 474 O
ATOM 181 NE2 GLN A 25 -6.110 -3.909 55.271 1.00 39.29 N
ANISOU 181 NE2 GLN A 25 5357 4510 5063 852 -186 425 N
ATOM 182 N ASN A 26 -1.777 -6.382 50.240 1.00 19.18 N
ANISOU 182 N ASN A 26 3109 3010 1170 -492 -514 174 N
ATOM 183 CA ASN A 26 -0.601 -6.283 49.373 1.00 19.35 C
ANISOU 183 CA ASN A 26 3316 2971 1064 -561 -427 243 C
ATOM 184 C ASN A 26 0.272 -5.073 49.703 1.00 20.01 C
ANISOU 184 C ASN A 26 3518 2773 1310 -361 -409 501 C
ATOM 185 O ASN A 26 0.865 -4.453 48.818 1.00 27.84 O
ANISOU 185 O ASN A 26 4559 3785 2234 -325 -368 630 O
ATOM 186 CB ASN A 26 -1.001 -6.282 47.897 1.00 26.93 C
ANISOU 186 CB ASN A 26 4184 4308 1741 -615 -506 232 C
ATOM 187 CG ASN A 26 -1.422 -7.646 47.427 1.00 40.52 C
ANISOU 187 CG ASN A 26 5804 6220 3370 -905 -410 -122 C
ATOM 188 OD1 ASN A 26 -0.596 -8.553 47.320 1.00 43.33 O
ANISOU 188 OD1 ASN A 26 6284 6381 3800 -1085 -170 -306 O
ATOM 189 ND2 ASN A 26 -2.714 -7.813 47.163 1.00 48.87 N
ANISOU 189 ND2 ASN A 26 6620 7632 4316 -942 -557 -222 N
ATOM 190 N HIS A 27 0.381 -4.736 50.980 1.00 16.22 N
ANISOU 190 N HIS A 27 3045 2031 1085 -246 -389 522 N
ATOM 191 CA HIS A 27 1.454 -3.841 51.389 1.00 21.96 C
ANISOU 191 CA HIS A 27 3823 2507 2013 -177 -285 597 C
ATOM 192 C HIS A 27 1.984 -4.271 52.745 1.00 14.31 C
ANISOU 192 C HIS A 27 2834 1365 1237 -172 -210 465 C
ATOM 193 O HIS A 27 1.398 -5.109 53.438 1.00 13.38 O
ANISOU 193 O HIS A 27 2684 1256 1142 -164 -213 369 O
ATOM 194 CB HIS A 27 1.038 -2.359 51.386 1.00 33.10 C
ANISOU 194 CB HIS A 27 5204 3850 3521 2 -313 789 C
ATOM 195 CG HIS A 27 -0.230 -2.065 52.120 1.00 38.75 C
ANISOU 195 CG HIS A 27 5822 4593 4309 173 -420 835 C
ATOM 196 ND1 HIS A 27 -0.281 -1.905 53.487 1.00 45.48 N
ANISOU 196 ND1 HIS A 27 6639 5272 5369 215 -385 722 N
ATOM 197 CD2 HIS A 27 -1.490 -1.854 51.668 1.00 47.00 C
ANISOU 197 CD2 HIS A 27 6759 5867 5230 330 -558 984 C
ATOM 198 CE1 HIS A 27 -1.523 -1.636 53.851 1.00 47.39 C
ANISOU 198 CE1 HIS A 27 6786 5578 5643 382 -475 789 C
ATOM 199 NE2 HIS A 27 -2.276 -1.600 52.766 1.00 52.95 N
ANISOU 199 NE2 HIS A 27 7423 6538 6157 463 -595 954 N
ATOM 200 N PHE A 28 3.140 -3.721 53.087 1.00 15.43 N
ANISOU 200 N PHE A 28 2966 1400 1495 -184 -124 448 N
ATOM 201 CA PHE A 28 3.886 -4.091 54.283 1.00 12.78 C
ANISOU 201 CA PHE A 28 2584 1010 1262 -170 -70 345 C
ATOM 202 C PHE A 28 3.606 -3.080 55.385 1.00 13.84 C
ANISOU 202 C PHE A 28 2680 1056 1523 -103 -112 327 C
ATOM 203 O PHE A 28 3.790 -1.877 55.176 1.00 17.72 O
ANISOU 203 O PHE A 28 3213 1442 2077 -135 -81 372 O
ATOM 204 CB PHE A 28 5.381 -4.117 53.947 1.00 13.21 C
ANISOU 204 CB PHE A 28 2671 1056 1294 -278 45 338 C
ATOM 205 CG PHE A 28 6.275 -4.504 55.090 1.00 12.73 C
ANISOU 205 CG PHE A 28 2484 1059 1293 -228 83 245 C
ATOM 206 CD1 PHE A 28 6.083 -5.691 55.780 1.00 12.01 C
ANISOU 206 CD1 PHE A 28 2342 1027 1193 -79 109 223 C
ATOM 207 CD2 PHE A 28 7.350 -3.698 55.433 1.00 13.42 C
ANISOU 207 CD2 PHE A 28 2473 1195 1430 -327 114 174 C
ATOM 208 CE1 PHE A 28 6.922 -6.053 56.816 1.00 14.61 C
ANISOU 208 CE1 PHE A 28 2523 1501 1527 47 130 193 C
ATOM 209 CE2 PHE A 28 8.196 -4.051 56.472 1.00 17.13 C
ANISOU 209 CE2 PHE A 28 2736 1874 1897 -259 107 75 C
ATOM 210 CZ PHE A 28 7.983 -5.237 57.162 1.00 13.97 C
ANISOU 210 CZ PHE A 28 2285 1573 1451 -32 98 117 C
ATOM 211 N VAL A 29 3.167 -3.558 56.553 1.00 12.61 N
ANISOU 211 N VAL A 29 2472 918 1402 -18 -138 256 N
ATOM 212 CA VAL A 29 2.908 -2.678 57.695 1.00 14.04 C
ANISOU 212 CA VAL A 29 2647 1015 1671 27 -158 198 C
ATOM 213 C VAL A 29 4.079 -2.762 58.666 1.00 15.72 C
ANISOU 213 C VAL A 29 2815 1297 1859 -16 -136 78 C
ATOM 214 O VAL A 29 4.475 -3.860 59.085 1.00 17.12 O
ANISOU 214 O VAL A 29 2912 1638 1956 65 -124 77 O
ATOM 215 CB VAL A 29 1.575 -3.017 58.397 1.00 18.34 C
ANISOU 215 CB VAL A 29 3124 1603 2242 141 -187 178 C
ATOM 216 CG1 VAL A 29 0.393 -2.562 57.555 1.00 21.34 C
ANISOU 216 CG1 VAL A 29 3486 1976 2648 194 -231 276 C
ATOM 217 CG2 VAL A 29 1.460 -4.497 58.737 1.00 17.82 C
ANISOU 217 CG2 VAL A 29 3036 1627 2108 174 -148 157 C
ATOM 218 N ASP A 30 4.620 -1.597 59.032 1.00 17.55 N
ANISOU 218 N ASP A 30 3049 1466 2155 -141 -101 -38 N
ATOM 219 CA ASP A 30 5.784 -1.478 59.905 1.00 21.40 C
ANISOU 219 CA ASP A 30 3375 2173 2582 -244 -94 -225 C
ATOM 220 C ASP A 30 5.424 -1.391 61.379 1.00 20.37 C
ANISOU 220 C ASP A 30 3177 2174 2387 -180 -139 -371 C
ATOM 221 O ASP A 30 6.245 -1.757 62.232 1.00 18.34 O
ANISOU 221 O ASP A 30 2735 2256 1978 -173 -189 -478 O
ATOM 222 CB ASP A 30 6.594 -0.221 59.555 1.00 25.23 C
ANISOU 222 CB ASP A 30 3884 2541 3162 -513 18 -361 C
ATOM 223 CG ASP A 30 7.227 -0.295 58.184 1.00 34.53 C
ANISOU 223 CG ASP A 30 5109 3654 4355 -605 94 -231 C
ATOM 224 OD1 ASP A 30 8.110 -1.156 57.983 1.00 34.91 O
ANISOU 224 OD1 ASP A 30 4990 3960 4313 -597 79 -232 O
ATOM 225 OD2 ASP A 30 6.858 0.523 57.313 1.00 36.86 O
ANISOU 225 OD2 ASP A 30 5614 3649 4742 -657 193 -108 O
ATOM 226 N GLU A 31 4.244 -0.861 61.703 1.00 14.10 N
ANISOU 226 N GLU A 31 2509 1165 1684 -121 -115 -377 N
ATOM 227 CA GLU A 31 3.881 -0.551 63.080 1.00 15.44 C
ANISOU 227 CA GLU A 31 2646 1426 1794 -102 -109 -560 C
ATOM 228 C GLU A 31 2.422 -0.883 63.341 1.00 14.08 C
ANISOU 228 C GLU A 31 2551 1129 1669 94 -102 -452 C
ATOM 229 O GLU A 31 1.710 -0.131 64.016 1.00 15.16 O
ANISOU 229 O GLU A 31 2744 1142 1875 105 -29 -577 O
ATOM 230 CB GLU A 31 4.137 0.922 63.412 1.00 17.70 C
ANISOU 230 CB GLU A 31 2995 1541 2188 -329 14 -821 C
ATOM 231 CG GLU A 31 5.583 1.399 63.219 1.00 25.18 C
ANISOU 231 CG GLU A 31 3833 2624 3109 -619 54 -1010 C
ATOM 232 CD GLU A 31 6.560 0.763 64.198 1.00 28.75 C
ANISOU 232 CD GLU A 31 4000 3634 3289 -655 -77 -1176 C
ATOM 233 OE1 GLU A 31 6.112 0.248 65.243 1.00 28.56 O
ANISOU 233 OE1 GLU A 31 3922 3842 3086 -489 -158 -1188 O
ATOM 234 OE2 GLU A 31 7.782 0.774 63.918 1.00 28.21 O
ANISOU 234 OE2 GLU A 31 3742 3811 3164 -831 -91 -1275 O
ATOM 235 N TYR A 32 1.955 -2.010 62.825 1.00 12.81 N
ANISOU 235 N TYR A 32 2383 1002 1481 224 -140 -256 N
ATOM 236 CA TYR A 32 0.582 -2.423 63.075 1.00 12.26 C
ANISOU 236 CA TYR A 32 2334 874 1452 356 -112 -193 C
ATOM 237 C TYR A 32 0.431 -2.757 64.554 1.00 12.44 C
ANISOU 237 C TYR A 32 2324 1065 1338 423 -67 -290 C
ATOM 238 O TYR A 32 1.167 -3.596 65.084 1.00 12.56 O
ANISOU 238 O TYR A 32 2298 1301 1174 474 -75 -248 O
ATOM 239 CB TYR A 32 0.229 -3.615 62.188 1.00 10.51 C
ANISOU 239 CB TYR A 32 2106 668 1218 390 -117 -36 C
ATOM 240 CG TYR A 32 -1.218 -4.043 62.238 1.00 14.87 C
ANISOU 240 CG TYR A 32 2602 1221 1827 433 -72 -13 C
ATOM 241 CD1 TYR A 32 -1.663 -4.890 63.241 1.00 12.35 C
ANISOU 241 CD1 TYR A 32 2304 943 1446 501 35 -34 C
ATOM 242 CD2 TYR A 32 -2.123 -3.639 61.274 1.00 19.25 C
ANISOU 242 CD2 TYR A 32 3107 1735 2473 436 -125 37 C
ATOM 243 CE1 TYR A 32 -2.970 -5.305 63.303 1.00 15.98 C
ANISOU 243 CE1 TYR A 32 2705 1396 1970 501 114 -51 C
ATOM 244 CE2 TYR A 32 -3.454 -4.058 61.326 1.00 22.14 C
ANISOU 244 CE2 TYR A 32 3390 2143 2878 484 -99 20 C
ATOM 245 CZ TYR A 32 -3.859 -4.896 62.351 1.00 16.92 C
ANISOU 245 CZ TYR A 32 2718 1519 2191 477 38 -48 C
ATOM 246 OH TYR A 32 -5.158 -5.349 62.435 1.00 23.74 O
ANISOU 246 OH TYR A 32 3449 2465 3108 450 113 -104 O
ATOM 247 N ASP A 33 -0.484 -2.054 65.228 1.00 13.43 N
ANISOU 247 N ASP A 33 2471 1101 1531 453 -1 -403 N
ATOM 248 CA ASP A 33 -0.710 -2.124 66.669 1.00 14.68 C
ANISOU 248 CA ASP A 33 2621 1421 1536 494 69 -532 C
ATOM 249 C ASP A 33 -0.592 -3.566 67.146 1.00 14.24 C
ANISOU 249 C ASP A 33 2553 1571 1285 605 93 -373 C
ATOM 250 O ASP A 33 -1.388 -4.422 66.747 1.00 13.36 O
ANISOU 250 O ASP A 33 2464 1360 1253 659 168 -235 O
ATOM 251 CB ASP A 33 -2.086 -1.540 66.997 1.00 15.53 C
ANISOU 251 CB ASP A 33 2746 1358 1796 562 183 -605 C
ATOM 252 CG ASP A 33 -2.326 -1.359 68.485 1.00 21.07 C
ANISOU 252 CG ASP A 33 3462 2207 2335 574 293 -791 C
ATOM 253 OD1 ASP A 33 -1.773 -2.121 69.302 1.00 18.46 O
ANISOU 253 OD1 ASP A 33 3123 2162 1728 594 278 -766 O
ATOM 254 OD2 ASP A 33 -3.101 -0.449 68.832 1.00 20.84 O
ANISOU 254 OD2 ASP A 33 3417 2041 2460 569 402 -924 O
ATOM 255 N PRO A 34 0.384 -3.858 68.005 1.00 15.49 N
ANISOU 255 N PRO A 34 2674 2031 1179 644 55 -390 N
ATOM 256 CA PRO A 34 0.610 -5.252 68.431 1.00 15.84 C
ANISOU 256 CA PRO A 34 2746 2240 1033 830 120 -156 C
ATOM 257 C PRO A 34 -0.544 -5.881 69.188 1.00 16.47 C
ANISOU 257 C PRO A 34 2925 2260 1073 923 310 -78 C
ATOM 258 O PRO A 34 -0.563 -7.115 69.311 1.00 16.91 O
ANISOU 258 O PRO A 34 3059 2295 1070 1055 447 153 O
ATOM 259 CB PRO A 34 1.858 -5.146 69.320 1.00 21.77 C
ANISOU 259 CB PRO A 34 3381 3432 1458 891 8 -201 C
ATOM 260 CG PRO A 34 2.553 -3.901 68.862 1.00 30.04 C
ANISOU 260 CG PRO A 34 4320 4494 2600 653 -123 -465 C
ATOM 261 CD PRO A 34 1.461 -2.955 68.453 1.00 17.20 C
ANISOU 261 CD PRO A 34 2800 2474 1260 514 -45 -612 C
ATOM 262 N THR A 35 -1.479 -5.095 69.727 1.00 17.35 N
ANISOU 262 N THR A 35 3038 2313 1241 854 367 -263 N
ATOM 263 CA THR A 35 -2.567 -5.614 70.548 1.00 18.16 C
ANISOU 263 CA THR A 35 3202 2397 1300 911 573 -218 C
ATOM 264 C THR A 35 -3.833 -5.895 69.756 1.00 19.93 C
ANISOU 264 C THR A 35 3410 2347 1814 848 696 -204 C
ATOM 265 O THR A 35 -4.785 -6.436 70.323 1.00 18.57 O
ANISOU 265 O THR A 35 3243 2152 1660 830 882 -168 O
ATOM 266 CB THR A 35 -2.906 -4.635 71.679 1.00 21.85 C
ANISOU 266 CB THR A 35 3631 3001 1669 853 594 -450 C
ATOM 267 OG1 THR A 35 -3.462 -3.436 71.123 1.00 22.40 O
ANISOU 267 OG1 THR A 35 3659 2848 2004 763 577 -667 O
ATOM 268 CG2 THR A 35 -1.654 -4.294 72.475 1.00 27.08 C
ANISOU 268 CG2 THR A 35 4240 4016 2032 829 451 -529 C
ATOM 269 N ILE A 36 -3.868 -5.564 68.469 1.00 15.43 N
ANISOU 269 N ILE A 36 2766 1622 1474 766 568 -220 N
ATOM 270 CA ILE A 36 -5.103 -5.623 67.694 1.00 15.67 C
ANISOU 270 CA ILE A 36 2692 1521 1741 697 619 -249 C
ATOM 271 C ILE A 36 -5.259 -7.002 67.065 1.00 14.90 C
ANISOU 271 C ILE A 36 2629 1360 1672 613 740 -132 C
ATOM 272 O ILE A 36 -4.425 -7.436 66.261 1.00 13.87 O
ANISOU 272 O ILE A 36 2553 1187 1530 589 666 -45 O
ATOM 273 CB ILE A 36 -5.132 -4.526 66.621 1.00 14.47 C
ANISOU 273 CB ILE A 36 2445 1284 1768 684 430 -298 C
ATOM 274 CG1 ILE A 36 -5.188 -3.151 67.284 1.00 17.32 C
ANISOU 274 CG1 ILE A 36 2810 1606 2164 745 423 -446 C
ATOM 275 CG2 ILE A 36 -6.292 -4.752 65.666 1.00 15.21 C
ANISOU 275 CG2 ILE A 36 2374 1376 2030 644 429 -287 C
ATOM 276 CD1 ILE A 36 -6.426 -2.913 68.125 1.00 18.91 C
ANISOU 276 CD1 ILE A 36 2924 1832 2429 797 582 -550 C
ATOM 277 N GLU A 37 -6.364 -7.664 67.396 1.00 16.26 N
ANISOU 277 N GLU A 37 2766 1510 1903 538 965 -166 N
ATOM 278 CA GLU A 37 -6.716 -8.978 66.876 1.00 16.96 C
ANISOU 278 CA GLU A 37 2899 1492 2053 379 1177 -133 C
ATOM 279 C GLU A 37 -7.953 -8.821 66.000 1.00 17.67 C
ANISOU 279 C GLU A 37 2726 1661 2328 194 1144 -309 C
ATOM 280 O GLU A 37 -9.000 -8.377 66.479 1.00 19.46 O
ANISOU 280 O GLU A 37 2778 1990 2625 195 1202 -415 O
ATOM 281 CB GLU A 37 -6.961 -9.924 68.053 1.00 18.99 C
ANISOU 281 CB GLU A 37 3310 1685 2221 384 1474 -24 C
ATOM 282 CG GLU A 37 -7.401 -11.323 67.743 1.00 20.75 C
ANISOU 282 CG GLU A 37 3626 1702 2557 184 1752 -3 C
ATOM 283 CD GLU A 37 -7.336 -12.182 68.987 1.00 29.43 C
ANISOU 283 CD GLU A 37 4932 2669 3580 289 1954 172 C
ATOM 284 OE1 GLU A 37 -6.211 -12.541 69.391 1.00 23.27 O
ANISOU 284 OE1 GLU A 37 4315 1851 2677 534 1906 373 O
ATOM 285 OE2 GLU A 37 -8.401 -12.452 69.594 1.00 28.20 O
ANISOU 285 OE2 GLU A 37 4745 2490 3481 166 2152 95 O
ATOM 286 N ASP A 38 -7.835 -9.153 64.714 1.00 14.19 N
ANISOU 286 N ASP A 38 2121 1882 1389 874 515 -17 N
ATOM 287 CA ASP A 38 -8.934 -8.927 63.784 1.00 14.51 C
ANISOU 287 CA ASP A 38 2073 1981 1460 919 529 22 C
ATOM 288 C ASP A 38 -8.983 -10.075 62.792 1.00 14.57 C
ANISOU 288 C ASP A 38 2036 2033 1466 810 526 113 C
ATOM 289 O ASP A 38 -8.020 -10.833 62.647 1.00 14.36 O
ANISOU 289 O ASP A 38 2068 1952 1437 720 497 147 O
ATOM 290 CB ASP A 38 -8.781 -7.588 63.039 1.00 15.08 C
ANISOU 290 CB ASP A 38 2235 1897 1598 1022 477 15 C
ATOM 291 CG ASP A 38 -10.105 -7.043 62.490 1.00 20.69 C
ANISOU 291 CG ASP A 38 2895 2670 2296 1209 429 -13 C
ATOM 292 OD1 ASP A 38 -11.167 -7.687 62.639 1.00 18.85 O
ANISOU 292 OD1 ASP A 38 2469 2660 2032 1231 456 -70 O
ATOM 293 OD2 ASP A 38 -10.073 -5.955 61.886 1.00 20.65 O
ANISOU 293 OD2 ASP A 38 3067 2486 2294 1335 358 -10 O
ATOM 294 N SER A 39 -10.126 -10.200 62.117 1.00 14.38 N
ANISOU 294 N SER A 39 1891 2130 1442 844 537 111 N
ATOM 295 CA SER A 39 -10.328 -11.201 61.080 1.00 13.65 C
ANISOU 295 CA SER A 39 1739 2093 1353 749 532 177 C
ATOM 296 C SER A 39 -10.504 -10.525 59.729 1.00 14.25 C
ANISOU 296 C SER A 39 1821 2117 1476 867 444 206 C
ATOM 297 O SER A 39 -11.007 -9.401 59.635 1.00 15.69 O
ANISOU 297 O SER A 39 2035 2268 1659 1056 384 150 O
ATOM 298 CB SER A 39 -11.554 -12.078 61.368 1.00 20.75 C
ANISOU 298 CB SER A 39 2488 3209 2187 650 631 104 C
ATOM 299 OG SER A 39 -11.332 -12.927 62.483 1.00 20.49 O
ANISOU 299 OG SER A 39 2572 3165 2047 490 730 110 O
ATOM 300 N TYR A 40 -10.112 -11.246 58.681 1.00 13.04 N
ANISOU 300 N TYR A 40 1679 1939 1335 774 422 287 N
ATOM 301 CA TYR A 40 -10.140 -10.747 57.314 1.00 13.36 C
ANISOU 301 CA TYR A 40 1798 1901 1376 855 344 336 C
ATOM 302 C TYR A 40 -10.664 -11.840 56.405 1.00 17.59 C
ANISOU 302 C TYR A 40 2203 2575 1904 794 329 353 C
ATOM 303 O TYR A 40 -10.344 -13.013 56.595 1.00 20.16 O
ANISOU 303 O TYR A 40 2474 2949 2238 624 384 375 O
ATOM 304 CB TYR A 40 -8.751 -10.333 56.829 1.00 15.33 C
ANISOU 304 CB TYR A 40 2243 1945 1638 748 361 397 C
ATOM 305 CG TYR A 40 -8.066 -9.361 57.736 1.00 15.13 C
ANISOU 305 CG TYR A 40 2333 1789 1627 745 399 345 C
ATOM 306 CD1 TYR A 40 -7.316 -9.801 58.814 1.00 17.22 C
ANISOU 306 CD1 TYR A 40 2527 2091 1923 657 437 283 C
ATOM 307 CD2 TYR A 40 -8.196 -7.994 57.541 1.00 21.51 C
ANISOU 307 CD2 TYR A 40 3358 2420 2395 855 377 340 C
ATOM 308 CE1 TYR A 40 -6.689 -8.912 59.656 1.00 20.32 C
ANISOU 308 CE1 TYR A 40 2998 2391 2333 657 463 200 C
ATOM 309 CE2 TYR A 40 -7.573 -7.094 58.380 1.00 28.66 C
ANISOU 309 CE2 TYR A 40 4377 3198 3316 826 423 273 C
ATOM 310 CZ TYR A 40 -6.820 -7.561 59.436 1.00 23.86 C
ANISOU 310 CZ TYR A 40 3629 2673 2763 718 472 193 C
ATOM 311 OH TYR A 40 -6.202 -6.672 60.280 1.00 35.02 O
ANISOU 311 OH TYR A 40 5127 3985 4194 693 509 92 O
ATOM 312 N ARG A 41 -11.452 -11.457 55.410 1.00 15.03 N
ANISOU 312 N ARG A 41 1864 2298 1547 955 232 329 N
ATOM 313 CA ARG A 41 -11.938 -12.414 54.436 1.00 15.22 C
ANISOU 313 CA ARG A 41 1758 2461 1564 908 203 321 C
ATOM 314 C ARG A 41 -11.322 -12.110 53.076 1.00 18.27 C
ANISOU 314 C ARG A 41 2353 2688 1901 938 130 428 C
ATOM 315 O ARG A 41 -11.055 -10.950 52.735 1.00 22.81 O
ANISOU 315 O ARG A 41 3187 3070 2409 1067 74 472 O
ATOM 316 CB ARG A 41 -13.465 -12.405 54.367 1.00 19.45 C
ANISOU 316 CB ARG A 41 2048 3261 2083 1070 141 132 C
ATOM 317 CG ARG A 41 -14.129 -12.744 55.700 1.00 23.01 C
ANISOU 317 CG ARG A 41 2290 3900 2553 969 271 -14 C
ATOM 318 CD ARG A 41 -15.644 -12.567 55.625 1.00 33.55 C
ANISOU 318 CD ARG A 41 3365 5505 3879 1087 202 -283 C
ATOM 319 NE ARG A 41 -16.328 -13.823 55.329 1.00 41.62 N
ANISOU 319 NE ARG A 41 4182 6721 4911 847 280 -398 N
ATOM 320 CZ ARG A 41 -17.576 -13.905 54.882 1.00 51.24 C
ANISOU 320 CZ ARG A 41 5196 8152 6121 892 195 -639 C
ATOM 321 NH1 ARG A 41 -18.277 -12.799 54.666 1.00 58.04 N
ANISOU 321 NH1 ARG A 41 6038 9069 6945 1196 7 -791 N
ATOM 322 NH2 ARG A 41 -18.123 -15.091 54.644 1.00 48.56 N
ANISOU 322 NH2 ARG A 41 4708 7953 5788 633 288 -744 N
ATOM 323 N LYS A 42 -11.076 -13.169 52.311 1.00 13.65 N
ANISOU 323 N LYS A 42 1701 2160 1326 794 147 466 N
ATOM 324 CA LYS A 42 -10.480 -13.021 50.988 1.00 13.79 C
ANISOU 324 CA LYS A 42 1908 2054 1277 779 107 553 C
ATOM 325 C LYS A 42 -10.889 -14.203 50.123 1.00 13.18 C
ANISOU 325 C LYS A 42 1666 2139 1204 720 76 530 C
ATOM 326 O LYS A 42 -10.755 -15.353 50.546 1.00 16.73 O
ANISOU 326 O LYS A 42 1957 2679 1721 549 146 507 O
ATOM 327 CB LYS A 42 -8.953 -12.934 51.087 1.00 16.11 C
ANISOU 327 CB LYS A 42 2350 2180 1590 572 218 611 C
ATOM 328 CG LYS A 42 -8.240 -12.744 49.750 1.00 18.05 C
ANISOU 328 CG LYS A 42 2797 2312 1751 473 237 658 C
ATOM 329 CD LYS A 42 -6.732 -12.737 49.932 1.00 22.59 C
ANISOU 329 CD LYS A 42 3412 2811 2360 230 372 614 C
ATOM 330 CE LYS A 42 -6.007 -12.617 48.594 1.00 21.67 C
ANISOU 330 CE LYS A 42 3437 2630 2167 59 419 595 C
ATOM 331 NZ LYS A 42 -6.306 -11.335 47.921 1.00 26.52 N
ANISOU 331 NZ LYS A 42 4359 3051 2665 106 399 629 N
ATOM 332 N GLN A 43 -11.394 -13.915 48.925 1.00 14.54 N
ANISOU 332 N GLN A 43 1923 2324 1279 875 -43 530 N
ATOM 333 CA GLN A 43 -11.697 -14.954 47.952 1.00 16.04 C
ANISOU 333 CA GLN A 43 1978 2657 1460 822 -82 500 C
ATOM 334 C GLN A 43 -10.463 -15.221 47.101 1.00 13.91 C
ANISOU 334 C GLN A 43 1890 2245 1152 645 -17 608 C
ATOM 335 O GLN A 43 -9.856 -14.286 46.575 1.00 15.99 O
ANISOU 335 O GLN A 43 2438 2305 1331 634 -4 659 O
ATOM 336 CB GLN A 43 -12.876 -14.539 47.077 1.00 16.81 C
ANISOU 336 CB GLN A 43 2061 2867 1458 1106 -268 395 C
ATOM 337 CG GLN A 43 -13.263 -15.573 46.043 1.00 17.05 C
ANISOU 337 CG GLN A 43 1936 3067 1476 1065 -322 331 C
ATOM 338 CD GLN A 43 -14.450 -15.130 45.216 1.00 21.62 C
ANISOU 338 CD GLN A 43 2507 3720 1986 1307 -491 151 C
ATOM 339 OE1 GLN A 43 -15.539 -14.912 45.745 1.00 25.56 O
ANISOU 339 OE1 GLN A 43 2806 4390 2514 1439 -544 -53 O
ATOM 340 NE2 GLN A 43 -14.247 -14.980 43.915 1.00 20.81 N
ANISOU 340 NE2 GLN A 43 2631 3496 1778 1357 -566 200 N
ATOM 341 N VAL A 44 -10.079 -16.494 46.993 1.00 13.28 N
ANISOU 341 N VAL A 44 1649 2252 1144 461 37 587 N
ATOM 342 CA VAL A 44 -8.872 -16.883 46.273 1.00 13.21 C
ANISOU 342 CA VAL A 44 1735 2168 1116 295 100 622 C
ATOM 343 C VAL A 44 -9.148 -18.129 45.449 1.00 12.29 C
ANISOU 343 C VAL A 44 1474 2186 1009 242 56 578 C
ATOM 344 O VAL A 44 -10.087 -18.884 45.712 1.00 15.66 O
ANISOU 344 O VAL A 44 1715 2750 1486 256 19 513 O
ATOM 345 CB VAL A 44 -7.678 -17.142 47.214 1.00 12.27 C
ANISOU 345 CB VAL A 44 1588 1986 1087 143 199 591 C
ATOM 346 CG1 VAL A 44 -7.345 -15.885 48.003 1.00 16.84 C
ANISOU 346 CG1 VAL A 44 2303 2437 1660 170 252 610 C
ATOM 347 CG2 VAL A 44 -7.987 -18.308 48.142 1.00 12.60 C
ANISOU 347 CG2 VAL A 44 1465 2105 1217 111 184 545 C
ATOM 348 N VAL A 45 -8.300 -18.336 44.445 1.00 11.44 N
ANISOU 348 N VAL A 45 1457 2046 843 145 85 585 N
ATOM 349 CA VAL A 45 -8.289 -19.546 43.633 1.00 11.51 C
ANISOU 349 CA VAL A 45 1350 2163 862 78 52 531 C
ATOM 350 C VAL A 45 -7.058 -20.356 44.016 1.00 10.73 C
ANISOU 350 C VAL A 45 1191 2042 844 -67 112 459 C
ATOM 351 O VAL A 45 -5.923 -19.874 43.883 1.00 11.76 O
ANISOU 351 O VAL A 45 1394 2122 951 -154 193 417 O
ATOM 352 CB VAL A 45 -8.274 -19.218 42.134 1.00 12.48 C
ANISOU 352 CB VAL A 45 1625 2288 828 107 21 557 C
ATOM 353 CG1 VAL A 45 -8.247 -20.516 41.331 1.00 13.08 C
ANISOU 353 CG1 VAL A 45 1558 2487 925 36 -15 483 C
ATOM 354 CG2 VAL A 45 -9.473 -18.353 41.757 1.00 14.11 C
ANISOU 354 CG2 VAL A 45 1943 2490 929 338 -105 588 C
ATOM 355 N ILE A 46 -7.269 -21.583 44.482 1.00 10.31 N
ANISOU 355 N ILE A 46 1025 2025 866 -93 70 407 N
ATOM 356 CA ILE A 46 -6.169 -22.463 44.880 1.00 10.30 C
ANISOU 356 CA ILE A 46 1012 1985 916 -141 57 308 C
ATOM 357 C ILE A 46 -6.335 -23.773 44.120 1.00 9.50 C
ANISOU 357 C ILE A 46 869 1931 811 -173 -8 247 C
ATOM 358 O ILE A 46 -7.371 -24.437 44.251 1.00 11.80 O
ANISOU 358 O ILE A 46 1144 2234 1107 -201 -29 269 O
ATOM 359 CB ILE A 46 -6.141 -22.702 46.398 1.00 11.49 C
ANISOU 359 CB ILE A 46 1209 2043 1113 -110 44 308 C
ATOM 360 CG1 ILE A 46 -5.987 -21.365 47.140 1.00 10.12 C
ANISOU 360 CG1 ILE A 46 1066 1831 948 -76 107 353 C
ATOM 361 CG2 ILE A 46 -5.000 -23.662 46.778 1.00 11.44 C
ANISOU 361 CG2 ILE A 46 1244 1982 1121 -70 -40 171 C
ATOM 362 CD1 ILE A 46 -6.182 -21.454 48.657 1.00 12.76 C
ANISOU 362 CD1 ILE A 46 1460 2087 1303 -38 102 369 C
ATOM 363 N ASP A 47 -5.323 -24.136 43.325 1.00 10.58 N
ANISOU 363 N ASP A 47 976 2111 933 -192 -23 134 N
ATOM 364 CA ASP A 47 -5.380 -25.333 42.477 1.00 13.98 C
ANISOU 364 CA ASP A 47 1372 2586 1352 -209 -93 56 C
ATOM 365 C ASP A 47 -6.652 -25.346 41.639 1.00 13.51 C
ANISOU 365 C ASP A 47 1278 2605 1250 -236 -95 136 C
ATOM 366 O ASP A 47 -7.323 -26.374 41.486 1.00 14.47 O
ANISOU 366 O ASP A 47 1377 2735 1385 -274 -143 102 O
ATOM 367 CB ASP A 47 -5.264 -26.610 43.315 1.00 12.04 C
ANISOU 367 CB ASP A 47 1216 2220 1140 -169 -190 -9 C
ATOM 368 CG ASP A 47 -3.973 -26.678 44.081 1.00 14.45 C
ANISOU 368 CG ASP A 47 1554 2472 1465 -58 -257 -146 C
ATOM 369 OD1 ASP A 47 -2.952 -26.177 43.573 1.00 14.70 O
ANISOU 369 OD1 ASP A 47 1456 2625 1504 -53 -227 -286 O
ATOM 370 OD2 ASP A 47 -3.966 -27.233 45.196 1.00 14.89 O
ANISOU 370 OD2 ASP A 47 1776 2373 1509 19 -336 -146 O
ATOM 371 N GLY A 48 -7.003 -24.174 41.112 1.00 12.55 N
ANISOU 371 N GLY A 48 1177 2532 1058 -206 -54 219 N
ATOM 372 CA GLY A 48 -8.126 -24.050 40.206 1.00 12.19 C
ANISOU 372 CA GLY A 48 1103 2588 941 -154 -108 246 C
ATOM 373 C GLY A 48 -9.490 -24.071 40.854 1.00 12.75 C
ANISOU 373 C GLY A 48 1074 2715 1055 -111 -142 245 C
ATOM 374 O GLY A 48 -10.490 -24.076 40.129 1.00 17.16 O
ANISOU 374 O GLY A 48 1544 3412 1565 -42 -216 191 O
ATOM 375 N GLU A 49 -9.565 -24.073 42.186 1.00 13.09 N
ANISOU 375 N GLU A 49 1115 2683 1175 -149 -89 265 N
ATOM 376 CA GLU A 49 -10.825 -24.142 42.911 1.00 13.93 C
ANISOU 376 CA GLU A 49 1105 2872 1314 -169 -70 215 C
ATOM 377 C GLU A 49 -10.967 -22.889 43.763 1.00 12.93 C
ANISOU 377 C GLU A 49 1011 2712 1189 -61 -45 281 C
ATOM 378 O GLU A 49 -10.139 -22.638 44.652 1.00 12.75 O
ANISOU 378 O GLU A 49 1100 2547 1197 -87 10 349 O
ATOM 379 CB GLU A 49 -10.889 -25.406 43.775 1.00 17.44 C
ANISOU 379 CB GLU A 49 1584 3236 1807 -361 -2 164 C
ATOM 380 CG GLU A 49 -12.260 -25.684 44.380 1.00 27.88 C
ANISOU 380 CG GLU A 49 2771 4685 3139 -493 79 47 C
ATOM 381 CD GLU A 49 -12.278 -26.953 45.215 1.00 43.99 C
ANISOU 381 CD GLU A 49 4979 6572 5164 -743 188 15 C
ATOM 382 OE1 GLU A 49 -12.630 -26.879 46.412 1.00 45.37 O
ANISOU 382 OE1 GLU A 49 5232 6688 5319 -843 299 23 O
ATOM 383 OE2 GLU A 49 -11.930 -28.025 44.675 1.00 54.48 O
ANISOU 383 OE2 GLU A 49 6411 7814 6474 -839 161 -19 O
ATOM 384 N THR A 50 -12.008 -22.111 43.486 1.00 14.91 N
ANISOU 384 N THR A 50 1166 3101 1398 92 -110 228 N
ATOM 385 CA THR A 50 -12.259 -20.885 44.227 1.00 13.54 C
ANISOU 385 CA THR A 50 1034 2897 1213 236 -114 263 C
ATOM 386 C THR A 50 -12.780 -21.200 45.621 1.00 13.59 C
ANISOU 386 C THR A 50 922 2944 1296 116 -7 195 C
ATOM 387 O THR A 50 -13.633 -22.074 45.801 1.00 18.64 O
ANISOU 387 O THR A 50 1385 3734 1962 -27 47 47 O
ATOM 388 CB THR A 50 -13.270 -20.016 43.476 1.00 19.57 C
ANISOU 388 CB THR A 50 1752 3800 1883 508 -269 178 C
ATOM 389 OG1 THR A 50 -12.789 -19.760 42.150 1.00 20.53 O
ANISOU 389 OG1 THR A 50 2071 3852 1879 603 -359 255 O
ATOM 390 CG2 THR A 50 -13.486 -18.694 44.194 1.00 19.48 C
ANISOU 390 CG2 THR A 50 1836 3723 1843 702 -302 205 C
ATOM 391 N CYS A 51 -12.267 -20.476 46.612 1.00 12.79 N
ANISOU 391 N CYS A 51 936 2709 1213 143 45 283 N
ATOM 392 CA CYS A 51 -12.727 -20.631 47.980 1.00 14.15 C
ANISOU 392 CA CYS A 51 1047 2907 1422 39 154 227 C
ATOM 393 C CYS A 51 -12.635 -19.287 48.690 1.00 13.58 C
ANISOU 393 C CYS A 51 1037 2775 1346 206 141 272 C
ATOM 394 O CYS A 51 -12.077 -18.319 48.169 1.00 14.35 O
ANISOU 394 O CYS A 51 1281 2763 1409 363 66 363 O
ATOM 395 CB CYS A 51 -11.922 -21.697 48.723 1.00 15.22 C
ANISOU 395 CB CYS A 51 1338 2877 1568 -170 245 289 C
ATOM 396 SG CYS A 51 -10.157 -21.331 48.840 1.00 15.55 S
ANISOU 396 SG CYS A 51 1595 2693 1621 -95 199 423 S
ATOM 397 N LEU A 52 -13.195 -19.242 49.893 1.00 13.60 N
ANISOU 397 N LEU A 52 963 2838 1365 142 236 197 N
ATOM 398 CA LEU A 52 -13.153 -18.058 50.736 1.00 13.66 C
ANISOU 398 CA LEU A 52 1022 2795 1374 288 234 217 C
ATOM 399 C LEU A 52 -12.271 -18.350 51.939 1.00 13.64 C
ANISOU 399 C LEU A 52 1182 2621 1381 145 338 309 C
ATOM 400 O LEU A 52 -12.450 -19.373 52.605 1.00 15.81 O
ANISOU 400 O LEU A 52 1476 2902 1629 -59 445 275 O
ATOM 401 CB LEU A 52 -14.557 -17.658 51.193 1.00 16.59 C
ANISOU 401 CB LEU A 52 1145 3418 1741 373 245 0 C
ATOM 402 CG LEU A 52 -14.673 -16.294 51.877 1.00 25.36 C
ANISOU 402 CG LEU A 52 2297 4494 2846 600 197 -15 C
ATOM 403 CD1 LEU A 52 -14.195 -15.188 50.944 1.00 29.72 C
ANISOU 403 CD1 LEU A 52 3065 4875 3351 873 23 99 C
ATOM 404 CD2 LEU A 52 -16.104 -16.043 52.321 1.00 30.27 C
ANISOU 404 CD2 LEU A 52 2675 5358 3469 653 189 -293 C
ATOM 405 N LEU A 53 -11.313 -17.468 52.204 1.00 12.81 N
ANISOU 405 N LEU A 53 1230 2352 1287 247 305 406 N
ATOM 406 CA LEU A 53 -10.485 -17.569 53.396 1.00 14.23 C
ANISOU 406 CA LEU A 53 1542 2398 1466 179 361 447 C
ATOM 407 C LEU A 53 -11.027 -16.629 54.452 1.00 12.74 C
ANISOU 407 C LEU A 53 1323 2245 1271 263 403 399 C
ATOM 408 O LEU A 53 -11.325 -15.467 54.164 1.00 17.51 O
ANISOU 408 O LEU A 53 1907 2860 1887 437 345 383 O
ATOM 409 CB LEU A 53 -9.029 -17.216 53.113 1.00 11.73 C
ANISOU 409 CB LEU A 53 1356 1928 1173 208 314 505 C
ATOM 410 CG LEU A 53 -8.392 -17.950 51.937 1.00 13.93 C
ANISOU 410 CG LEU A 53 1640 2197 1457 149 271 516 C
ATOM 411 CD1 LEU A 53 -6.918 -17.623 51.847 1.00 16.20 C
ANISOU 411 CD1 LEU A 53 1999 2393 1764 135 261 484 C
ATOM 412 CD2 LEU A 53 -8.618 -19.434 52.108 1.00 14.50 C
ANISOU 412 CD2 LEU A 53 1717 2287 1505 41 273 494 C
ATOM 413 N ASP A 54 -11.138 -17.134 55.669 1.00 12.16 N
ANISOU 413 N ASP A 54 1300 2167 1154 149 496 373 N
ATOM 414 CA ASP A 54 -11.566 -16.373 56.836 1.00 12.59 C
ANISOU 414 CA ASP A 54 1337 2259 1186 199 558 313 C
ATOM 415 C ASP A 54 -10.394 -16.450 57.810 1.00 14.36 C
ANISOU 415 C ASP A 54 1779 2300 1378 189 549 380 C
ATOM 416 O ASP A 54 -10.198 -17.486 58.446 1.00 16.09 O
ANISOU 416 O ASP A 54 2160 2451 1504 62 593 395 O
ATOM 417 CB ASP A 54 -12.848 -16.979 57.399 1.00 15.35 C
ANISOU 417 CB ASP A 54 1560 2801 1470 31 705 176 C
ATOM 418 CG ASP A 54 -13.434 -16.181 58.539 1.00 23.98 C
ANISOU 418 CG ASP A 54 2595 3974 2542 75 776 65 C
ATOM 419 OD1 ASP A 54 -12.811 -15.196 58.986 1.00 22.21 O
ANISOU 419 OD1 ASP A 54 2447 3652 2338 248 715 120 O
ATOM 420 OD2 ASP A 54 -14.527 -16.568 59.003 1.00 30.48 O
ANISOU 420 OD2 ASP A 54 3321 4909 3351 -77 881 -91 O
ATOM 421 N ILE A 55 -9.606 -15.376 57.916 1.00 11.58 N
ANISOU 421 N ILE A 55 1464 1856 1079 325 485 396 N
ATOM 422 CA ILE A 55 -8.296 -15.421 58.576 1.00 12.05 C
ANISOU 422 CA ILE A 55 1669 1780 1128 344 436 398 C
ATOM 423 C ILE A 55 -8.328 -14.596 59.852 1.00 11.67 C
ANISOU 423 C ILE A 55 1665 1714 1054 413 467 351 C
ATOM 424 O ILE A 55 -8.573 -13.385 59.808 1.00 13.25 O
ANISOU 424 O ILE A 55 1808 1920 1308 504 473 327 O
ATOM 425 CB ILE A 55 -7.186 -14.900 57.659 1.00 13.21 C
ANISOU 425 CB ILE A 55 1805 1860 1354 374 373 388 C
ATOM 426 CG1 ILE A 55 -7.091 -15.786 56.421 1.00 16.79 C
ANISOU 426 CG1 ILE A 55 2221 2340 1818 306 342 420 C
ATOM 427 CG2 ILE A 55 -5.856 -14.855 58.412 1.00 13.61 C
ANISOU 427 CG2 ILE A 55 1921 1844 1406 405 318 291 C
ATOM 428 CD1 ILE A 55 -6.520 -15.089 55.270 1.00 17.55 C
ANISOU 428 CD1 ILE A 55 2300 2408 1959 292 339 418 C
ATOM 429 N LEU A 56 -8.007 -15.232 60.973 1.00 11.56 N
ANISOU 429 N LEU A 56 1806 1650 937 391 468 334 N
ATOM 430 CA LEU A 56 -7.866 -14.547 62.253 1.00 12.17 C
ANISOU 430 CA LEU A 56 1953 1704 966 463 482 279 C
ATOM 431 C LEU A 56 -6.390 -14.270 62.516 1.00 11.84 C
ANISOU 431 C LEU A 56 1968 1574 957 568 355 202 C
ATOM 432 O LEU A 56 -5.579 -15.201 62.577 1.00 12.00 O
ANISOU 432 O LEU A 56 2103 1539 916 602 247 168 O
ATOM 433 CB LEU A 56 -8.441 -15.375 63.399 1.00 13.62 C
ANISOU 433 CB LEU A 56 2330 1881 963 373 565 285 C
ATOM 434 CG LEU A 56 -8.166 -14.757 64.778 1.00 14.29 C
ANISOU 434 CG LEU A 56 2529 1935 967 462 563 224 C
ATOM 435 CD1 LEU A 56 -8.887 -13.417 64.945 1.00 15.55 C
ANISOU 435 CD1 LEU A 56 2478 2210 1220 512 642 162 C
ATOM 436 CD2 LEU A 56 -8.562 -15.700 65.899 1.00 16.06 C
ANISOU 436 CD2 LEU A 56 3000 2094 1008 331 608 229 C
ATOM 437 N ASP A 57 -6.056 -13.000 62.711 1.00 11.84 N
ANISOU 437 N ASP A 57 1893 1567 1040 627 361 133 N
ATOM 438 CA ASP A 57 -4.710 -12.563 63.075 1.00 12.09 C
ANISOU 438 CA ASP A 57 1922 1562 1108 688 274 -17 C
ATOM 439 C ASP A 57 -4.690 -12.378 64.593 1.00 13.01 C
ANISOU 439 C ASP A 57 2151 1670 1123 787 248 -82 C
ATOM 440 O ASP A 57 -5.218 -11.387 65.103 1.00 13.33 O
ANISOU 440 O ASP A 57 2167 1714 1182 803 322 -88 O
ATOM 441 CB ASP A 57 -4.393 -11.274 62.309 1.00 12.03 C
ANISOU 441 CB ASP A 57 1822 1520 1227 627 336 -61 C
ATOM 442 CG ASP A 57 -3.142 -10.581 62.786 1.00 12.84 C
ANISOU 442 CG ASP A 57 1889 1614 1375 622 307 -274 C
ATOM 443 OD1 ASP A 57 -2.221 -11.278 63.238 1.00 13.80 O
ANISOU 443 OD1 ASP A 57 1979 1799 1465 689 192 -428 O
ATOM 444 OD2 ASP A 57 -3.075 -9.323 62.668 1.00 13.42 O
ANISOU 444 OD2 ASP A 57 1981 1613 1505 557 392 -316 O
ATOM 445 N THR A 58 -4.118 -13.348 65.325 1.00 14.75 N
ANISOU 445 N THR A 58 2317 1872 1414 919 770 511 N
ATOM 446 CA THR A 58 -4.178 -13.313 66.790 1.00 14.85 C
ANISOU 446 CA THR A 58 2417 1807 1420 897 826 471 C
ATOM 447 C THR A 58 -3.228 -12.281 67.383 1.00 15.09 C
ANISOU 447 C THR A 58 2669 1613 1450 867 940 347 C
ATOM 448 O THR A 58 -2.194 -11.941 66.800 1.00 14.61 O
ANISOU 448 O THR A 58 2676 1443 1431 797 915 263 O
ATOM 449 CB THR A 58 -3.842 -14.679 67.412 1.00 13.98 C
ANISOU 449 CB THR A 58 2243 1727 1340 716 657 409 C
ATOM 450 OG1 THR A 58 -2.487 -15.075 67.098 1.00 13.02 O
ANISOU 450 OG1 THR A 58 2168 1490 1290 596 565 299 O
ATOM 451 CG2 THR A 58 -4.821 -15.742 66.945 1.00 14.23 C
ANISOU 451 CG2 THR A 58 2082 1946 1380 668 566 490 C
ATOM 452 N ALA A 59 -3.572 -11.817 68.588 1.00 16.13 N
ANISOU 452 N ALA A 59 2892 1690 1547 847 1029 327 N
ATOM 453 CA ALA A 59 -2.729 -10.857 69.293 1.00 17.02 C
ANISOU 453 CA ALA A 59 3200 1629 1638 711 1111 182 C
ATOM 454 C ALA A 59 -2.832 -10.974 70.810 1.00 18.17 C
ANISOU 454 C ALA A 59 3433 1805 1666 596 1149 99 C
ATOM 455 O ALA A 59 -1.916 -10.556 71.523 1.00 19.72 O
ANISOU 455 O ALA A 59 3768 1953 1773 398 1164 -56 O
ATOM 456 CB ALA A 59 -3.079 -9.427 68.867 1.00 18.66 C
ANISOU 456 CB ALA A 59 3499 1676 1916 793 1288 252 C
ATOM 457 N GLY A 60 -3.947 -11.495 71.320 1.00 18.30 N
ANISOU 457 N GLY A 60 3362 1932 1661 690 1166 205 N
ATOM 458 CA GLY A 60 -4.108 -11.597 72.763 1.00 19.50 C
ANISOU 458 CA GLY A 60 3596 2132 1682 573 1207 141 C
ATOM 459 C GLY A 60 -3.205 -12.663 73.357 1.00 18.70 C
ANISOU 459 C GLY A 60 3482 2188 1435 394 1034 113 C
ATOM 460 O GLY A 60 -2.849 -13.640 72.703 1.00 18.63 O
ANISOU 460 O GLY A 60 3313 2248 1519 400 847 197 O
ATOM 461 N GLN A 61 -2.840 -12.484 74.630 1.00 23.45 N
ANISOU 461 N GLN A 61 4196 2856 1857 203 1042 19 N
ATOM 462 CA GLN A 61 -1.909 -13.397 75.288 1.00 23.17 C
ANISOU 462 CA GLN A 61 4100 3019 1683 12 828 59 C
ATOM 463 C GLN A 61 -2.588 -14.437 76.168 1.00 22.69 C
ANISOU 463 C GLN A 61 3925 3127 1568 31 755 221 C
ATOM 464 O GLN A 61 -1.916 -15.369 76.629 1.00 22.77 O
ANISOU 464 O GLN A 61 3797 3302 1551 -70 550 341 O
ATOM 465 CB GLN A 61 -0.908 -12.613 76.147 1.00 26.65 C
ANISOU 465 CB GLN A 61 4707 3528 1892 -277 839 -121 C
ATOM 466 CG GLN A 61 -1.543 -11.981 77.365 1.00 34.21 C
ANISOU 466 CG GLN A 61 5773 4500 2726 -353 979 -220 C
ATOM 467 CD GLN A 61 -0.545 -11.259 78.251 1.00 46.84 C
ANISOU 467 CD GLN A 61 7493 6182 4123 -678 960 -407 C
ATOM 468 OE1 GLN A 61 0.667 -11.384 78.077 1.00 49.67 O
ANISOU 468 OE1 GLN A 61 7794 6672 4408 -872 790 -428 O
ATOM 469 NE2 GLN A 61 -1.056 -10.494 79.208 1.00 51.29 N
ANISOU 469 NE2 GLN A 61 8214 6679 4596 -763 1142 -536 N
ATOM 470 N GLU A 62 -3.881 -14.298 76.435 1.00 21.04 N
ANISOU 470 N GLU A 62 3744 2885 1367 167 928 258 N
ATOM 471 CA GLU A 62 -4.531 -15.168 77.404 1.00 23.36 C
ANISOU 471 CA GLU A 62 3957 3334 1584 155 897 395 C
ATOM 472 C GLU A 62 -4.602 -16.609 76.905 1.00 20.31 C
ANISOU 472 C GLU A 62 3331 3002 1382 222 715 594 C
ATOM 473 O GLU A 62 -4.776 -16.873 75.716 1.00 18.81 O
ANISOU 473 O GLU A 62 3029 2719 1398 324 679 614 O
ATOM 474 CB GLU A 62 -5.933 -14.652 77.718 1.00 27.72 C
ANISOU 474 CB GLU A 62 4516 3821 2195 279 1096 380 C
ATOM 475 CG GLU A 62 -6.735 -15.564 78.626 1.00 31.34 C
ANISOU 475 CG GLU A 62 4885 4424 2600 271 1087 519 C
ATOM 476 CD GLU A 62 -8.001 -14.914 79.129 1.00 42.37 C
ANISOU 476 CD GLU A 62 6305 5758 4036 384 1304 503 C
ATOM 477 OE1 GLU A 62 -8.323 -15.095 80.322 1.00 45.41 O
ANISOU 477 OE1 GLU A 62 6737 6240 4276 302 1365 509 O
ATOM 478 OE2 GLU A 62 -8.667 -14.220 78.331 1.00 49.15 O
ANISOU 478 OE2 GLU A 62 7124 6484 5066 564 1415 514 O
ATOM 479 N GLU A 63 -4.474 -17.551 77.839 1.00 21.17 N
ANISOU 479 N GLU A 63 3365 3260 1417 145 618 740 N
ATOM 480 CA GLU A 63 -4.622 -18.960 77.510 1.00 22.16 C
ANISOU 480 CA GLU A 63 3289 3381 1749 196 516 929 C
ATOM 481 C GLU A 63 -5.254 -19.669 78.697 1.00 21.97 C
ANISOU 481 C GLU A 63 3233 3485 1629 174 553 1089 C
ATOM 482 O GLU A 63 -5.419 -19.091 79.775 1.00 23.58 O
ANISOU 482 O GLU A 63 3562 3789 1607 93 611 1026 O
ATOM 483 CB GLU A 63 -3.279 -19.594 77.125 1.00 21.56 C
ANISOU 483 CB GLU A 63 3111 3293 1786 148 347 1004 C
ATOM 484 CG GLU A 63 -2.133 -19.286 78.069 1.00 21.61 C
ANISOU 484 CG GLU A 63 3145 3495 1571 7 235 1042 C
ATOM 485 CD GLU A 63 -0.854 -19.992 77.654 1.00 21.60 C
ANISOU 485 CD GLU A 63 2976 3503 1727 8 90 1192 C
ATOM 486 OE1 GLU A 63 -0.229 -20.657 78.511 1.00 23.43 O
ANISOU 486 OE1 GLU A 63 3083 3922 1897 -29 -6 1422 O
ATOM 487 OE2 GLU A 63 -0.491 -19.899 76.463 1.00 20.07 O
ANISOU 487 OE2 GLU A 63 2762 3129 1733 63 92 1095 O
ATOM 488 N TYR A 64 -5.599 -20.937 78.487 1.00 21.79 N
ANISOU 488 N TYR A 64 3056 3412 1811 210 527 1245 N
ATOM 489 CA TYR A 64 -6.277 -21.758 79.493 1.00 23.31 C
ANISOU 489 CA TYR A 64 3198 3662 1996 192 565 1371 C
ATOM 490 C TYR A 64 -7.481 -21.009 80.061 1.00 24.08 C
ANISOU 490 C TYR A 64 3380 3810 1960 211 713 1279 C
ATOM 491 O TYR A 64 -7.617 -20.780 81.266 1.00 25.82 O
ANISOU 491 O TYR A 64 3696 4134 1982 148 752 1278 O
ATOM 492 CB TYR A 64 -5.312 -22.205 80.601 1.00 25.08 C
ANISOU 492 CB TYR A 64 3411 4014 2104 122 454 1500 C
ATOM 493 CG TYR A 64 -4.256 -23.165 80.095 1.00 24.95 C
ANISOU 493 CG TYR A 64 3255 3925 2301 156 357 1647 C
ATOM 494 CD1 TYR A 64 -3.071 -22.692 79.550 1.00 24.31 C
ANISOU 494 CD1 TYR A 64 3163 3859 2214 137 251 1608 C
ATOM 495 CD2 TYR A 64 -4.456 -24.539 80.136 1.00 25.82 C
ANISOU 495 CD2 TYR A 64 3247 3926 2636 209 413 1821 C
ATOM 496 CE1 TYR A 64 -2.111 -23.552 79.064 1.00 24.85 C
ANISOU 496 CE1 TYR A 64 3091 3841 2509 193 205 1748 C
ATOM 497 CE2 TYR A 64 -3.490 -25.414 79.654 1.00 26.20 C
ANISOU 497 CE2 TYR A 64 3183 3859 2912 265 396 1947 C
ATOM 498 CZ TYR A 64 -2.320 -24.911 79.120 1.00 26.98 C
ANISOU 498 CZ TYR A 64 3258 3980 3013 267 294 1913 C
ATOM 499 OH TYR A 64 -1.346 -25.762 78.634 1.00 30.65 O
ANISOU 499 OH TYR A 64 3599 4324 3723 344 315 2040 O
ATOM 500 N SER A 65 -8.356 -20.620 79.139 1.00 23.12 N
ANISOU 500 N SER A 65 3211 3622 1953 299 805 1213 N
ATOM 501 CA SER A 65 -9.590 -19.907 79.439 1.00 24.07 C
ANISOU 501 CA SER A 65 3349 3766 2030 371 969 1160 C
ATOM 502 C SER A 65 -10.660 -20.448 78.505 1.00 23.68 C
ANISOU 502 C SER A 65 3095 3726 2176 432 1002 1242 C
ATOM 503 O SER A 65 -10.408 -20.581 77.304 1.00 22.39 O
ANISOU 503 O SER A 65 2854 3533 2122 434 938 1231 O
ATOM 504 CB SER A 65 -9.415 -18.396 79.248 1.00 34.78 C
ANISOU 504 CB SER A 65 4860 5060 3293 424 1065 985 C
ATOM 505 OG SER A 65 -10.608 -17.703 79.564 1.00 35.93 O
ANISOU 505 OG SER A 65 5011 5194 3447 528 1255 967 O
ATOM 506 N ALA A 66 -11.840 -20.764 79.052 1.00 25.12 N
ANISOU 506 N ALA A 66 3185 3979 2381 449 1102 1325 N
ATOM 507 CA ALA A 66 -12.819 -21.545 78.297 1.00 25.37 C
ANISOU 507 CA ALA A 66 2987 4081 2572 421 1109 1425 C
ATOM 508 C ALA A 66 -13.251 -20.839 77.014 1.00 24.88 C
ANISOU 508 C ALA A 66 2802 4083 2568 501 1105 1398 C
ATOM 509 O ALA A 66 -13.461 -21.492 75.987 1.00 24.63 O
ANISOU 509 O ALA A 66 2602 4127 2629 396 1039 1433 O
ATOM 510 CB ALA A 66 -14.037 -21.848 79.167 1.00 27.37 C
ANISOU 510 CB ALA A 66 3155 4418 2826 430 1225 1520 C
ATOM 511 N MET A 67 -13.416 -19.515 77.061 1.00 25.22 N
ANISOU 511 N MET A 67 2926 4100 2556 667 1192 1343 N
ATOM 512 CA MET A 67 -13.939 -18.794 75.902 1.00 25.37 C
ANISOU 512 CA MET A 67 2805 4197 2639 788 1197 1381 C
ATOM 513 C MET A 67 -12.940 -18.787 74.756 1.00 23.53 C
ANISOU 513 C MET A 67 2598 3926 2415 736 1074 1304 C
ATOM 514 O MET A 67 -13.299 -19.047 73.601 1.00 23.57 O
ANISOU 514 O MET A 67 2406 4084 2465 692 998 1361 O
ATOM 515 CB MET A 67 -14.304 -17.364 76.285 1.00 26.98 C
ANISOU 515 CB MET A 67 3124 4306 2823 1000 1369 1368 C
ATOM 516 CG MET A 67 -15.529 -17.262 77.163 1.00 29.06 C
ANISOU 516 CG MET A 67 3317 4623 3101 1087 1521 1480 C
ATOM 517 SD MET A 67 -15.179 -17.710 78.865 1.00 32.63 S
ANISOU 517 SD MET A 67 3984 4994 3420 952 1590 1384 S
ATOM 518 CE MET A 67 -13.934 -16.490 79.291 1.00 40.17 C
ANISOU 518 CE MET A 67 5291 5738 4234 942 1667 1161 C
ATOM 519 N ARG A 68 -11.682 -18.460 75.044 1.00 22.24 N
ANISOU 519 N ARG A 68 2668 3592 2190 717 1050 1173 N
ATOM 520 CA ARG A 68 -10.693 -18.478 73.973 1.00 20.63 C
ANISOU 520 CA ARG A 68 2496 3337 2004 673 944 1107 C
ATOM 521 C ARG A 68 -10.484 -19.887 73.438 1.00 20.08 C
ANISOU 521 C ARG A 68 2313 3275 2043 475 790 1097 C
ATOM 522 O ARG A 68 -10.354 -20.085 72.224 1.00 19.61 O
ANISOU 522 O ARG A 68 2172 3237 2042 406 699 1041 O
ATOM 523 CB ARG A 68 -9.368 -17.889 74.440 1.00 22.78 C
ANISOU 523 CB ARG A 68 3018 3441 2196 661 930 970 C
ATOM 524 CG ARG A 68 -8.458 -17.598 73.252 1.00 26.45 C
ANISOU 524 CG ARG A 68 3511 3817 2721 649 826 869 C
ATOM 525 CD ARG A 68 -7.281 -16.732 73.619 1.00 29.92 C
ANISOU 525 CD ARG A 68 4174 4121 3075 638 847 736 C
ATOM 526 NE ARG A 68 -6.833 -15.948 72.472 1.00 26.10 N
ANISOU 526 NE ARG A 68 3724 3552 2639 703 853 665 N
ATOM 527 CZ ARG A 68 -5.640 -15.371 72.382 1.00 29.13 C
ANISOU 527 CZ ARG A 68 4259 3813 2996 645 830 535 C
ATOM 528 NH1 ARG A 68 -5.331 -14.669 71.297 1.00 21.52 N
ANISOU 528 NH1 ARG A 68 3322 2768 2086 715 860 491 N
ATOM 529 NH2 ARG A 68 -4.751 -15.514 73.365 1.00 21.68 N
ANISOU 529 NH2 ARG A 68 3417 2863 1957 503 771 471 N
ATOM 530 N ASP A 69 -10.450 -20.880 74.326 1.00 20.53 N
ANISOU 530 N ASP A 69 2379 3295 2125 375 791 1149 N
ATOM 531 CA ASP A 69 -10.257 -22.253 73.877 1.00 20.58 C
ANISOU 531 CA ASP A 69 2317 3229 2274 190 725 1138 C
ATOM 532 C ASP A 69 -11.415 -22.715 72.998 1.00 23.22 C
ANISOU 532 C ASP A 69 2441 3726 2654 59 729 1147 C
ATOM 533 O ASP A 69 -11.201 -23.376 71.976 1.00 21.76 O
ANISOU 533 O ASP A 69 2224 3499 2546 -117 674 1043 O
ATOM 534 CB ASP A 69 -10.069 -23.171 75.087 1.00 21.38 C
ANISOU 534 CB ASP A 69 2466 3256 2403 144 773 1253 C
ATOM 535 CG ASP A 69 -8.779 -22.871 75.837 1.00 20.81 C
ANISOU 535 CG ASP A 69 2550 3101 2254 214 721 1268 C
ATOM 536 OD1 ASP A 69 -7.842 -22.347 75.193 1.00 19.62 O
ANISOU 536 OD1 ASP A 69 2466 2881 2108 239 639 1161 O
ATOM 537 OD2 ASP A 69 -8.697 -23.157 77.051 1.00 21.83 O
ANISOU 537 OD2 ASP A 69 2721 3272 2303 224 757 1399 O
ATOM 538 N GLN A 70 -12.649 -22.356 73.364 1.00 23.06 N
ANISOU 538 N GLN A 70 2270 3918 2572 121 806 1270 N
ATOM 539 CA GLN A 70 -13.791 -22.720 72.531 1.00 24.70 C
ANISOU 539 CA GLN A 70 2217 4377 2789 -30 784 1311 C
ATOM 540 C GLN A 70 -13.692 -22.065 71.165 1.00 25.55 C
ANISOU 540 C GLN A 70 2246 4621 2839 -19 681 1255 C
ATOM 541 O GLN A 70 -14.010 -22.684 70.144 1.00 25.48 O
ANISOU 541 O GLN A 70 2101 4761 2820 -266 597 1188 O
ATOM 542 CB GLN A 70 -15.103 -22.326 73.210 1.00 26.61 C
ANISOU 542 CB GLN A 70 2278 4842 2989 85 892 1495 C
ATOM 543 CG GLN A 70 -16.322 -22.560 72.323 1.00 35.35 C
ANISOU 543 CG GLN A 70 3077 6271 4083 -61 816 1556 C
ATOM 544 CD GLN A 70 -17.591 -21.919 72.862 1.00 43.87 C
ANISOU 544 CD GLN A 70 4003 7517 5147 138 876 1731 C
ATOM 545 OE1 GLN A 70 -17.652 -20.704 73.075 1.00 40.38 O
ANISOU 545 OE1 GLN A 70 3623 7036 4683 442 945 1810 O
ATOM 546 NE2 GLN A 70 -18.617 -22.737 73.077 1.00 50.11 N
ANISOU 546 NE2 GLN A 70 4609 8465 5966 -43 877 1789 N
ATOM 547 N TYR A 71 -13.236 -20.815 71.121 1.00 23.37 N
ANISOU 547 N TYR A 71 2072 4299 2509 239 703 1275 N
ATOM 548 CA TYR A 71 -13.125 -20.145 69.838 1.00 23.32 C
ANISOU 548 CA TYR A 71 1996 4418 2446 279 624 1263 C
ATOM 549 C TYR A 71 -12.059 -20.802 68.970 1.00 22.09 C
ANISOU 549 C TYR A 71 1971 4097 2324 76 509 1051 C
ATOM 550 O TYR A 71 -12.273 -21.024 67.772 1.00 25.54 O
ANISOU 550 O TYR A 71 2288 4718 2699 -91 418 1005 O
ATOM 551 CB TYR A 71 -12.815 -18.663 70.036 1.00 23.14 C
ANISOU 551 CB TYR A 71 2095 4308 2390 601 736 1328 C
ATOM 552 CG TYR A 71 -12.664 -17.960 68.716 1.00 27.41 C
ANISOU 552 CG TYR A 71 2564 4971 2879 668 676 1359 C
ATOM 553 CD1 TYR A 71 -11.435 -17.915 68.072 1.00 37.11 C
ANISOU 553 CD1 TYR A 71 3978 6005 4117 603 591 1177 C
ATOM 554 CD2 TYR A 71 -13.760 -17.389 68.081 1.00 30.84 C
ANISOU 554 CD2 TYR A 71 2730 5723 3264 793 682 1588 C
ATOM 555 CE1 TYR A 71 -11.302 -17.307 66.848 1.00 41.96 C
ANISOU 555 CE1 TYR A 71 4531 6743 4667 654 544 1216 C
ATOM 556 CE2 TYR A 71 -13.631 -16.770 66.858 1.00 35.36 C
ANISOU 556 CE2 TYR A 71 3220 6448 3768 858 621 1661 C
ATOM 557 CZ TYR A 71 -12.399 -16.729 66.249 1.00 39.76 C
ANISOU 557 CZ TYR A 71 3982 6817 4309 784 568 1472 C
ATOM 558 OH TYR A 71 -12.251 -16.116 65.029 1.00 45.16 O
ANISOU 558 OH TYR A 71 4595 7658 4907 846 520 1555 O
ATOM 559 N MET A 72 -10.902 -21.120 69.557 1.00 20.45 N
ANISOU 559 N MET A 72 1999 3571 2201 81 523 937 N
ATOM 560 CA MET A 72 -9.800 -21.660 68.768 1.00 19.51 C
ANISOU 560 CA MET A 72 2006 3261 2146 -55 465 766 C
ATOM 561 C MET A 72 -10.123 -23.040 68.215 1.00 24.35 C
ANISOU 561 C MET A 72 2558 3877 2817 -371 472 669 C
ATOM 562 O MET A 72 -9.590 -23.426 67.165 1.00 24.70 O
ANISOU 562 O MET A 72 2664 3848 2874 -530 455 514 O
ATOM 563 CB MET A 72 -8.529 -21.702 69.612 1.00 20.67 C
ANISOU 563 CB MET A 72 2355 3121 2377 38 488 735 C
ATOM 564 CG MET A 72 -7.987 -20.328 69.935 1.00 17.01 C
ANISOU 564 CG MET A 72 2001 2628 1835 254 493 747 C
ATOM 565 SD MET A 72 -7.603 -19.420 68.435 1.00 19.52 S
ANISOU 565 SD MET A 72 2327 2980 2108 306 451 668 S
ATOM 566 CE MET A 72 -6.920 -17.948 69.133 1.00 15.73 C
ANISOU 566 CE MET A 72 2024 2382 1572 517 530 668 C
ATOM 567 N ARG A 73 -10.993 -23.788 68.893 1.00 22.33 N
ANISOU 567 N ARG A 73 2202 3686 2595 -487 530 741 N
ATOM 568 CA ARG A 73 -11.438 -25.071 68.369 1.00 28.55 C
ANISOU 568 CA ARG A 73 2942 4476 3431 -841 580 628 C
ATOM 569 C ARG A 73 -12.123 -24.921 67.018 1.00 27.83 C
ANISOU 569 C ARG A 73 2681 4723 3170 -1066 484 547 C
ATOM 570 O ARG A 73 -12.149 -25.882 66.241 1.00 30.55 O
ANISOU 570 O ARG A 73 3060 5036 3511 -1423 527 357 O
ATOM 571 CB ARG A 73 -12.374 -25.754 69.374 1.00 27.60 C
ANISOU 571 CB ARG A 73 2719 4403 3365 -923 670 746 C
ATOM 572 CG ARG A 73 -12.567 -27.247 69.131 1.00 33.10 C
ANISOU 572 CG ARG A 73 3452 4948 4175 -1299 803 613 C
ATOM 573 CD ARG A 73 -13.174 -27.946 70.336 1.00 37.24 C
ANISOU 573 CD ARG A 73 3947 5395 4808 -1317 935 755 C
ATOM 574 NE ARG A 73 -14.630 -27.913 70.336 1.00 45.48 N
ANISOU 574 NE ARG A 73 4723 6808 5750 -1499 913 824 N
ATOM 575 CZ ARG A 73 -15.394 -28.828 69.751 1.00 48.36 C
ANISOU 575 CZ ARG A 73 5013 7243 6118 -1889 960 680 C
ATOM 576 NH1 ARG A 73 -14.836 -29.845 69.109 1.00 51.49 N
ANISOU 576 NH1 ARG A 73 5620 7326 6618 -2125 1065 447 N
ATOM 577 NH2 ARG A 73 -16.715 -28.723 69.800 1.00 48.35 N
ANISOU 577 NH2 ARG A 73 4773 7572 6027 -1968 890 749 N
ATOM 578 N THR A 74 -12.659 -23.733 66.712 1.00 26.94 N
ANISOU 578 N THR A 74 2393 4938 2906 -874 378 697 N
ATOM 579 CA THR A 74 -13.325 -23.525 65.432 1.00 27.93 C
ANISOU 579 CA THR A 74 2306 5476 2830 -1067 261 694 C
ATOM 580 C THR A 74 -12.343 -23.282 64.295 1.00 31.02 C
ANISOU 580 C THR A 74 2855 5774 3156 -1107 213 528 C
ATOM 581 O THR A 74 -12.742 -23.358 63.128 1.00 29.17 O
ANISOU 581 O THR A 74 2492 5869 2724 -1359 120 472 O
ATOM 582 CB THR A 74 -14.306 -22.351 65.501 1.00 28.85 C
ANISOU 582 CB THR A 74 2137 5994 2829 -799 204 999 C
ATOM 583 OG1 THR A 74 -13.590 -21.109 65.496 1.00 26.84 O
ANISOU 583 OG1 THR A 74 2012 5597 2589 -419 223 1079 O
ATOM 584 CG2 THR A 74 -15.167 -22.442 66.760 1.00 29.46 C
ANISOU 584 CG2 THR A 74 2090 6109 2994 -686 298 1177 C
ATOM 585 N GLY A 75 -11.085 -22.977 64.600 1.00 15.65 N
ANISOU 585 N GLY A 75 1389 2461 2097 -134 489 537 N
ATOM 586 CA GLY A 75 -10.078 -22.875 63.562 1.00 13.91 C
ANISOU 586 CA GLY A 75 1232 2213 1841 -178 409 489 C
ATOM 587 C GLY A 75 -9.925 -24.190 62.825 1.00 15.86 C
ANISOU 587 C GLY A 75 1486 2460 2081 -338 399 423 C
ATOM 588 O GLY A 75 -9.828 -25.255 63.441 1.00 16.71 O
ANISOU 588 O GLY A 75 1631 2487 2231 -378 462 400 O
ATOM 589 N GLU A 76 -9.909 -24.134 61.497 1.00 13.06 N
ANISOU 589 N GLU A 76 1082 2199 1681 -442 324 391 N
ATOM 590 CA GLU A 76 -9.746 -25.340 60.702 1.00 14.66 C
ANISOU 590 CA GLU A 76 1283 2408 1880 -611 328 271 C
ATOM 591 C GLU A 76 -8.296 -25.619 60.353 1.00 12.09 C
ANISOU 591 C GLU A 76 1064 1989 1540 -631 335 157 C
ATOM 592 O GLU A 76 -7.949 -26.776 60.076 1.00 14.20 O
ANISOU 592 O GLU A 76 1353 2177 1867 -730 379 31 O
ATOM 593 CB GLU A 76 -10.564 -25.235 59.414 1.00 13.99 C
ANISOU 593 CB GLU A 76 1103 2490 1723 -711 237 259 C
ATOM 594 CG GLU A 76 -12.046 -25.265 59.666 1.00 16.10 C
ANISOU 594 CG GLU A 76 1264 2828 2026 -709 232 339 C
ATOM 595 CD GLU A 76 -12.818 -25.108 58.390 1.00 28.75 C
ANISOU 595 CD GLU A 76 2772 4618 3535 -806 131 354 C
ATOM 596 OE1 GLU A 76 -12.972 -23.955 57.939 1.00 21.59 O
ANISOU 596 OE1 GLU A 76 1809 3820 2576 -750 49 483 O
ATOM 597 OE2 GLU A 76 -13.234 -26.137 57.822 1.00 34.02 O
ANISOU 597 OE2 GLU A 76 3420 5323 4184 -940 134 247 O
ATOM 598 N GLY A 77 -7.461 -24.590 60.344 1.00 11.16 N
ANISOU 598 N GLY A 77 1008 1861 1372 -529 294 190 N
ATOM 599 CA GLY A 77 -6.036 -24.744 60.113 1.00 10.49 C
ANISOU 599 CA GLY A 77 1019 1687 1278 -526 302 92 C
ATOM 600 C GLY A 77 -5.304 -23.611 60.777 1.00 11.68 C
ANISOU 600 C GLY A 77 1245 1778 1415 -370 282 164 C
ATOM 601 O GLY A 77 -5.832 -22.501 60.924 1.00 10.35 O
ANISOU 601 O GLY A 77 1038 1664 1231 -293 245 266 O
ATOM 602 N PHE A 78 -4.077 -23.885 61.197 1.00 8.76 N
ANISOU 602 N PHE A 78 969 1289 1072 -325 310 105 N
ATOM 603 CA PHE A 78 -3.271 -22.938 61.952 1.00 9.29 C
ANISOU 603 CA PHE A 78 1109 1297 1125 -195 297 146 C
ATOM 604 C PHE A 78 -1.962 -22.642 61.240 1.00 9.90 C
ANISOU 604 C PHE A 78 1232 1363 1168 -215 266 78 C
ATOM 605 O PHE A 78 -1.220 -23.560 60.875 1.00 9.36 O
ANISOU 605 O PHE A 78 1179 1245 1131 -277 296 -21 O
ATOM 606 CB PHE A 78 -3.010 -23.481 63.360 1.00 9.69 C
ANISOU 606 CB PHE A 78 1212 1246 1222 -118 351 173 C
ATOM 607 CG PHE A 78 -4.248 -23.554 64.195 1.00 10.36 C
ANISOU 607 CG PHE A 78 1251 1369 1318 -91 390 250 C
ATOM 608 CD1 PHE A 78 -5.103 -24.635 64.090 1.00 11.43 C
ANISOU 608 CD1 PHE A 78 1329 1506 1507 -175 426 261 C
ATOM 609 CD2 PHE A 78 -4.585 -22.514 65.041 1.00 12.81 C
ANISOU 609 CD2 PHE A 78 1561 1713 1593 9 401 293 C
ATOM 610 CE1 PHE A 78 -6.275 -24.691 64.838 1.00 13.60 C
ANISOU 610 CE1 PHE A 78 1548 1832 1789 -159 467 338 C
ATOM 611 CE2 PHE A 78 -5.746 -22.559 65.792 1.00 11.99 C
ANISOU 611 CE2 PHE A 78 1398 1661 1495 30 453 346 C
ATOM 612 CZ PHE A 78 -6.591 -23.649 65.697 1.00 15.21 C
ANISOU 612 CZ PHE A 78 1749 2087 1944 -53 483 381 C
ATOM 613 N LEU A 79 -1.679 -21.356 61.040 1.00 8.00 N
ANISOU 613 N LEU A 79 998 1156 884 -166 216 129 N
ATOM 614 CA LEU A 79 -0.395 -20.914 60.520 1.00 7.28 C
ANISOU 614 CA LEU A 79 950 1056 760 -176 190 84 C
ATOM 615 C LEU A 79 0.467 -20.601 61.733 1.00 10.38 C
ANISOU 615 C LEU A 79 1421 1337 1185 -64 208 79 C
ATOM 616 O LEU A 79 0.174 -19.657 62.472 1.00 8.87 O
ANISOU 616 O LEU A 79 1241 1125 1006 21 203 129 O
ATOM 617 CB LEU A 79 -0.586 -19.692 59.623 1.00 11.27 C
ANISOU 617 CB LEU A 79 1406 1656 1219 -200 122 172 C
ATOM 618 CG LEU A 79 0.439 -19.470 58.527 1.00 12.35 C
ANISOU 618 CG LEU A 79 1545 1866 1283 -288 91 137 C
ATOM 619 CD1 LEU A 79 0.271 -20.511 57.435 1.00 9.95 C
ANISOU 619 CD1 LEU A 79 1185 1696 900 -448 106 40 C
ATOM 620 CD2 LEU A 79 0.267 -18.085 57.976 1.00 12.64 C
ANISOU 620 CD2 LEU A 79 1534 1960 1309 -281 21 285 C
ATOM 621 N CYS A 80 1.497 -21.419 61.969 1.00 7.58 N
ANISOU 621 N CYS A 80 1106 918 856 -68 233 11 N
ATOM 622 CA CYS A 80 2.325 -21.331 63.167 1.00 6.57 C
ANISOU 622 CA CYS A 80 1032 720 743 20 240 22 C
ATOM 623 C CYS A 80 3.610 -20.615 62.792 1.00 6.75 C
ANISOU 623 C CYS A 80 1083 739 743 23 206 -20 C
ATOM 624 O CYS A 80 4.498 -21.206 62.164 1.00 8.88 O
ANISOU 624 O CYS A 80 1343 994 1037 -23 216 -85 O
ATOM 625 CB CYS A 80 2.602 -22.718 63.731 1.00 8.87 C
ANISOU 625 CB CYS A 80 1320 941 1108 21 281 22 C
ATOM 626 SG CYS A 80 1.113 -23.577 64.229 1.00 13.43 S
ANISOU 626 SG CYS A 80 1860 1518 1726 3 326 88 S
ATOM 627 N VAL A 81 3.714 -19.345 63.192 1.00 6.48 N
ANISOU 627 N VAL A 81 1072 708 681 72 179 4 N
ATOM 628 CA VAL A 81 4.731 -18.427 62.687 1.00 7.44 C
ANISOU 628 CA VAL A 81 1208 827 791 57 143 -19 C
ATOM 629 C VAL A 81 5.798 -18.206 63.747 1.00 8.07 C
ANISOU 629 C VAL A 81 1329 872 865 109 136 -52 C
ATOM 630 O VAL A 81 5.480 -17.908 64.903 1.00 8.84 O
ANISOU 630 O VAL A 81 1445 968 944 163 148 -49 O
ATOM 631 CB VAL A 81 4.117 -17.076 62.283 1.00 6.82 C
ANISOU 631 CB VAL A 81 1108 753 729 63 116 41 C
ATOM 632 CG1 VAL A 81 5.175 -16.194 61.625 1.00 7.19 C
ANISOU 632 CG1 VAL A 81 1160 794 778 26 80 41 C
ATOM 633 CG2 VAL A 81 2.904 -17.290 61.358 1.00 9.36 C
ANISOU 633 CG2 VAL A 81 1365 1146 1045 12 107 109 C
ATOM 634 N PHE A 82 7.063 -18.323 63.347 1.00 8.22 N
ANISOU 634 N PHE A 82 1349 889 886 81 120 -92 N
ATOM 635 CA PHE A 82 8.173 -17.808 64.130 1.00 7.04 C
ANISOU 635 CA PHE A 82 1221 731 723 108 95 -120 C
ATOM 636 C PHE A 82 9.016 -16.926 63.215 1.00 8.40 C
ANISOU 636 C PHE A 82 1386 904 901 56 70 -145 C
ATOM 637 O PHE A 82 8.838 -16.920 61.999 1.00 8.89 O
ANISOU 637 O PHE A 82 1423 995 961 -5 74 -131 O
ATOM 638 CB PHE A 82 9.028 -18.936 64.744 1.00 7.99 C
ANISOU 638 CB PHE A 82 1322 852 861 132 95 -115 C
ATOM 639 CG PHE A 82 9.824 -19.712 63.727 1.00 9.88 C
ANISOU 639 CG PHE A 82 1519 1070 1164 93 113 -154 C
ATOM 640 CD1 PHE A 82 9.226 -20.712 62.975 1.00 8.47 C
ANISOU 640 CD1 PHE A 82 1312 867 1039 60 161 -176 C
ATOM 641 CD2 PHE A 82 11.174 -19.421 63.506 1.00 7.80 C
ANISOU 641 CD2 PHE A 82 1232 818 912 79 93 -193 C
ATOM 642 CE1 PHE A 82 9.963 -21.433 62.021 1.00 10.09 C
ANISOU 642 CE1 PHE A 82 1466 1057 1312 13 202 -260 C
ATOM 643 CE2 PHE A 82 11.909 -20.124 62.560 1.00 9.69 C
ANISOU 643 CE2 PHE A 82 1417 1047 1219 42 130 -256 C
ATOM 644 CZ PHE A 82 11.305 -21.131 61.815 1.00 10.91 C
ANISOU 644 CZ PHE A 82 1543 1174 1429 9 191 -302 C
ATOM 645 N ALA A 83 9.936 -16.170 63.800 1.00 7.75 N
ANISOU 645 N ALA A 83 1318 812 814 63 44 -178 N
ATOM 646 CA ALA A 83 10.881 -15.369 63.035 1.00 8.20 C
ANISOU 646 CA ALA A 83 1362 868 887 6 23 -194 C
ATOM 647 C ALA A 83 12.255 -16.024 63.076 1.00 7.88 C
ANISOU 647 C ALA A 83 1290 862 843 -7 15 -235 C
ATOM 648 O ALA A 83 12.697 -16.493 64.128 1.00 9.72 O
ANISOU 648 O ALA A 83 1518 1109 1065 37 -1 -243 O
ATOM 649 CB ALA A 83 10.966 -13.938 63.567 1.00 9.48 C
ANISOU 649 CB ALA A 83 1546 974 1083 7 6 -216 C
ATOM 650 N ILE A 84 12.934 -16.052 61.927 1.00 10.81 N
ANISOU 650 N ILE A 84 1623 1264 1219 -73 25 -249 N
ATOM 651 CA ILE A 84 14.184 -16.805 61.851 1.00 10.82 C
ANISOU 651 CA ILE A 84 1570 1292 1248 -77 36 -298 C
ATOM 652 C ILE A 84 15.322 -16.130 62.598 1.00 12.83 C
ANISOU 652 C ILE A 84 1814 1557 1505 -75 -9 -314 C
ATOM 653 O ILE A 84 16.398 -16.726 62.744 1.00 12.00 O
ANISOU 653 O ILE A 84 1646 1478 1436 -63 -12 -336 O
ATOM 654 CB ILE A 84 14.596 -17.056 60.388 1.00 10.24 C
ANISOU 654 CB ILE A 84 1445 1279 1168 -163 81 -342 C
ATOM 655 CG1 ILE A 84 14.836 -15.741 59.652 1.00 13.19 C
ANISOU 655 CG1 ILE A 84 1820 1696 1497 -249 58 -304 C
ATOM 656 CG2 ILE A 84 13.536 -17.886 59.690 1.00 11.51 C
ANISOU 656 CG2 ILE A 84 1602 1458 1312 -187 127 -355 C
ATOM 657 CD1 ILE A 84 15.743 -15.920 58.459 1.00 22.68 C
ANISOU 657 CD1 ILE A 84 2948 2998 2670 -345 102 -357 C
ATOM 658 N ASN A 85 15.107 -14.912 63.086 1.00 10.76 N
ANISOU 658 N ASN A 85 1596 1270 1224 -89 -41 -311 N
ATOM 659 CA ASN A 85 16.065 -14.218 63.936 1.00 11.33 C
ANISOU 659 CA ASN A 85 1657 1359 1288 -106 -84 -354 C
ATOM 660 C ASN A 85 15.573 -14.100 65.374 1.00 12.63 C
ANISOU 660 C ASN A 85 1856 1540 1403 -62 -105 -377 C
ATOM 661 O ASN A 85 15.980 -13.191 66.102 1.00 12.63 O
ANISOU 661 O ASN A 85 1862 1554 1383 -99 -130 -445 O
ATOM 662 CB ASN A 85 16.360 -12.833 63.369 1.00 14.66 C
ANISOU 662 CB ASN A 85 2087 1735 1749 -185 -90 -367 C
ATOM 663 CG ASN A 85 15.173 -11.899 63.472 1.00 15.02 C
ANISOU 663 CG ASN A 85 2185 1685 1836 -175 -76 -351 C
ATOM 664 OD1 ASN A 85 14.019 -12.331 63.490 1.00 14.76 O
ANISOU 664 OD1 ASN A 85 2178 1638 1792 -121 -54 -314 O
ATOM 665 ND2 ASN A 85 15.453 -10.602 63.559 1.00 19.10 N
ANISOU 665 ND2 ASN A 85 2706 2123 2430 -226 -82 -380 N
ATOM 666 N ASN A 86 14.697 -15.016 65.798 1.00 9.67 N
ANISOU 666 N ASN A 86 1496 1177 1002 1 -88 -332 N
ATOM 667 CA ASN A 86 14.124 -14.974 67.142 1.00 10.12 C
ANISOU 667 CA ASN A 86 1576 1286 982 30 -97 -345 C
ATOM 668 C ASN A 86 14.040 -16.415 67.638 1.00 12.26 C
ANISOU 668 C ASN A 86 1813 1614 1233 84 -105 -248 C
ATOM 669 O ASN A 86 13.033 -17.103 67.429 1.00 11.29 O
ANISOU 669 O ASN A 86 1708 1450 1133 122 -67 -196 O
ATOM 670 CB ASN A 86 12.768 -14.280 67.129 1.00 11.42 C
ANISOU 670 CB ASN A 86 1788 1384 1167 41 -48 -370 C
ATOM 671 CG ASN A 86 12.162 -14.127 68.520 1.00 14.16 C
ANISOU 671 CG ASN A 86 2139 1806 1436 48 -29 -411 C
ATOM 672 OD1 ASN A 86 12.527 -14.827 69.464 1.00 13.79 O
ANISOU 672 OD1 ASN A 86 2083 1882 1275 58 -64 -390 O
ATOM 673 ND2 ASN A 86 11.217 -13.205 68.644 1.00 24.29 N
ANISOU 673 ND2 ASN A 86 3421 3031 2777 42 24 -468 N
ATOM 674 N THR A 87 15.111 -16.859 68.302 1.00 9.69 N
ANISOU 674 N THR A 87 1424 1379 880 84 -160 -207 N
ATOM 675 CA THR A 87 15.164 -18.231 68.798 1.00 9.12 C
ANISOU 675 CA THR A 87 1293 1340 832 140 -176 -71 C
ATOM 676 C THR A 87 13.991 -18.526 69.722 1.00 9.98 C
ANISOU 676 C THR A 87 1436 1504 853 159 -160 -13 C
ATOM 677 O THR A 87 13.371 -19.594 69.624 1.00 11.56 O
ANISOU 677 O THR A 87 1622 1648 1121 204 -131 87 O
ATOM 678 CB THR A 87 16.496 -18.469 69.504 1.00 10.79 C
ANISOU 678 CB THR A 87 1409 1667 1023 133 -255 -6 C
ATOM 679 OG1 THR A 87 17.552 -18.370 68.539 1.00 14.57 O
ANISOU 679 OG1 THR A 87 1839 2088 1609 122 -253 -55 O
ATOM 680 CG2 THR A 87 16.529 -19.854 70.181 1.00 13.53 C
ANISOU 680 CG2 THR A 87 1673 2046 1420 196 -283 187 C
ATOM 681 N LYS A 88 13.662 -17.591 70.623 1.00 9.61 N
ANISOU 681 N LYS A 88 1424 1564 662 116 -167 -91 N
ATOM 682 CA LYS A 88 12.544 -17.821 71.529 1.00 9.48 C
ANISOU 682 CA LYS A 88 1429 1630 543 122 -137 -55 C
ATOM 683 C LYS A 88 11.249 -18.082 70.764 1.00 9.67 C
ANISOU 683 C LYS A 88 1501 1515 657 163 -63 -51 C
ATOM 684 O LYS A 88 10.472 -18.974 71.135 1.00 11.27 O
ANISOU 684 O LYS A 88 1693 1737 853 189 -40 57 O
ATOM 685 CB LYS A 88 12.381 -16.642 72.479 1.00 12.98 C
ANISOU 685 CB LYS A 88 1896 2190 845 53 -126 -201 C
ATOM 686 CG LYS A 88 11.239 -16.821 73.451 1.00 22.64 C
ANISOU 686 CG LYS A 88 3128 3483 1991 41 -75 -179 C
ATOM 687 CD LYS A 88 11.173 -15.695 74.471 1.00 37.62 C
ANISOU 687 CD LYS A 88 5034 5433 3826 -25 -46 -331 C
ATOM 688 CE LYS A 88 10.152 -16.011 75.559 1.00 45.93 C
ANISOU 688 CE LYS A 88 6074 6597 4781 -40 4 -313 C
ATOM 689 NZ LYS A 88 8.835 -16.428 74.989 1.00 45.46 N
ANISOU 689 NZ LYS A 88 6049 6434 4789 17 74 -280 N
ATOM 690 N SER A 89 11.005 -17.331 69.687 1.00 10.43 N
ANISOU 690 N SER A 89 1639 1484 840 160 -30 -148 N
ATOM 691 CA SER A 89 9.761 -17.536 68.950 1.00 10.59 C
ANISOU 691 CA SER A 89 1686 1409 930 186 27 -132 C
ATOM 692 C SER A 89 9.721 -18.913 68.309 1.00 9.85 C
ANISOU 692 C SER A 89 1560 1256 926 207 34 -32 C
ATOM 693 O SER A 89 8.647 -19.509 68.191 1.00 11.36 O
ANISOU 693 O SER A 89 1755 1419 1144 221 74 13 O
ATOM 694 CB SER A 89 9.564 -16.446 67.895 1.00 8.74 C
ANISOU 694 CB SER A 89 1478 1075 768 168 44 -212 C
ATOM 695 OG SER A 89 10.413 -16.622 66.776 1.00 8.81 O
ANISOU 695 OG SER A 89 1470 1035 842 144 22 -202 O
ATOM 696 N PHE A 90 10.875 -19.440 67.901 1.00 8.52 N
ANISOU 696 N PHE A 90 1351 1063 825 207 5 -11 N
ATOM 697 CA PHE A 90 10.918 -20.796 67.370 1.00 8.07 C
ANISOU 697 CA PHE A 90 1247 925 895 227 31 52 C
ATOM 698 C PHE A 90 10.648 -21.814 68.466 1.00 11.43 C
ANISOU 698 C PHE A 90 1633 1380 1328 262 23 199 C
ATOM 699 O PHE A 90 9.875 -22.761 68.271 1.00 12.26 O
ANISOU 699 O PHE A 90 1725 1409 1523 271 67 254 O
ATOM 700 CB PHE A 90 12.273 -21.032 66.703 1.00 7.69 C
ANISOU 700 CB PHE A 90 1143 839 940 223 19 19 C
ATOM 701 CG PHE A 90 12.461 -22.419 66.172 1.00 9.18 C
ANISOU 701 CG PHE A 90 1264 921 1304 246 65 46 C
ATOM 702 CD1 PHE A 90 11.723 -22.870 65.088 1.00 9.63 C
ANISOU 702 CD1 PHE A 90 1330 901 1428 210 136 -34 C
ATOM 703 CD2 PHE A 90 13.388 -23.275 66.747 1.00 12.17 C
ANISOU 703 CD2 PHE A 90 1552 1273 1799 297 41 149 C
ATOM 704 CE1 PHE A 90 11.907 -24.155 64.587 1.00 11.26 C
ANISOU 704 CE1 PHE A 90 1466 991 1823 218 199 -55 C
ATOM 705 CE2 PHE A 90 13.578 -24.565 66.253 1.00 18.42 C
ANISOU 705 CE2 PHE A 90 2263 1920 2814 326 101 161 C
ATOM 706 CZ PHE A 90 12.843 -25.007 65.167 1.00 15.20 C
ANISOU 706 CZ PHE A 90 1874 1419 2482 283 190 37 C
ATOM 707 N GLU A 91 11.258 -21.627 69.638 1.00 9.16 N
ANISOU 707 N GLU A 91 1319 1220 942 267 -37 274 N
ATOM 708 CA GLU A 91 11.000 -22.514 70.766 1.00 9.98 C
ANISOU 708 CA GLU A 91 1374 1398 1020 283 -58 457 C
ATOM 709 C GLU A 91 9.538 -22.474 71.182 1.00 11.20 C
ANISOU 709 C GLU A 91 1575 1592 1089 268 -6 466 C
ATOM 710 O GLU A 91 8.982 -23.499 71.596 1.00 15.43 O
ANISOU 710 O GLU A 91 2073 2111 1678 278 11 618 O
ATOM 711 CB GLU A 91 11.909 -22.127 71.933 1.00 12.08 C
ANISOU 711 CB GLU A 91 1593 1860 1135 262 -143 524 C
ATOM 712 CG GLU A 91 13.384 -22.270 71.576 1.00 12.99 C
ANISOU 712 CG GLU A 91 1634 1945 1356 282 -199 545 C
ATOM 713 CD GLU A 91 14.319 -21.645 72.599 1.00 15.05 C
ANISOU 713 CD GLU A 91 1849 2426 1444 236 -292 570 C
ATOM 714 OE1 GLU A 91 13.872 -20.771 73.370 1.00 14.44 O
ANISOU 714 OE1 GLU A 91 1822 2511 1155 173 -296 484 O
ATOM 715 OE2 GLU A 91 15.506 -22.034 72.630 1.00 15.54 O
ANISOU 715 OE2 GLU A 91 1811 2505 1590 257 -355 663 O
ATOM 716 N ASP A 92 8.896 -21.308 71.056 1.00 11.70 N
ANISOU 716 N ASP A 92 1707 1691 1048 245 24 313 N
ATOM 717 CA ASP A 92 7.486 -21.170 71.397 1.00 11.63 C
ANISOU 717 CA ASP A 92 1726 1719 975 237 84 303 C
ATOM 718 C ASP A 92 6.579 -21.993 70.490 1.00 9.59 C
ANISOU 718 C ASP A 92 1466 1318 860 248 135 336 C
ATOM 719 O ASP A 92 5.425 -22.225 70.857 1.00 11.19 O
ANISOU 719 O ASP A 92 1666 1553 1031 241 181 375 O
ATOM 720 CB ASP A 92 7.044 -19.701 71.322 1.00 12.60 C
ANISOU 720 CB ASP A 92 1899 1865 1022 224 115 124 C
ATOM 721 CG ASP A 92 7.590 -18.846 72.464 1.00 19.17 C
ANISOU 721 CG ASP A 92 2729 2865 1688 186 93 47 C
ATOM 722 OD1 ASP A 92 8.119 -19.390 73.456 1.00 23.47 O
ANISOU 722 OD1 ASP A 92 3227 3545 2144 151 47 149 O
ATOM 723 OD2 ASP A 92 7.473 -17.603 72.360 1.00 24.20 O
ANISOU 723 OD2 ASP A 92 3390 3468 2336 164 120 -119 O
ATOM 724 N ILE A 93 7.058 -22.417 69.313 1.00 10.30 N
ANISOU 724 N ILE A 93 1547 1270 1097 252 135 301 N
ATOM 725 CA ILE A 93 6.221 -23.227 68.424 1.00 10.06 C
ANISOU 725 CA ILE A 93 1504 1127 1192 235 187 299 C
ATOM 726 C ILE A 93 5.724 -24.469 69.151 1.00 10.88 C
ANISOU 726 C ILE A 93 1562 1209 1362 238 210 455 C
ATOM 727 O ILE A 93 4.582 -24.894 68.962 1.00 12.38 O
ANISOU 727 O ILE A 93 1747 1370 1587 213 258 469 O
ATOM 728 CB ILE A 93 6.992 -23.588 67.141 1.00 10.54 C
ANISOU 728 CB ILE A 93 1545 1074 1384 218 194 212 C
ATOM 729 CG1 ILE A 93 7.266 -22.331 66.305 1.00 9.91 C
ANISOU 729 CG1 ILE A 93 1506 1030 1231 195 176 87 C
ATOM 730 CG2 ILE A 93 6.238 -24.646 66.312 1.00 12.32 C
ANISOU 730 CG2 ILE A 93 1740 1195 1746 178 256 189 C
ATOM 731 CD1 ILE A 93 6.020 -21.622 65.759 1.00 11.14 C
ANISOU 731 CD1 ILE A 93 1687 1214 1331 167 195 45 C
ATOM 732 N HIS A 94 6.560 -25.060 70.013 1.00 13.19 N
ANISOU 732 N HIS A 94 1808 1526 1679 263 170 599 N
ATOM 733 CA HIS A 94 6.092 -26.215 70.772 1.00 15.53 C
ANISOU 733 CA HIS A 94 2042 1815 2044 248 177 758 C
ATOM 734 C HIS A 94 4.848 -25.870 71.578 1.00 16.00 C
ANISOU 734 C HIS A 94 2122 2015 1943 216 201 782 C
ATOM 735 O HIS A 94 3.883 -26.640 71.611 1.00 17.12 O
ANISOU 735 O HIS A 94 2236 2113 2157 187 240 831 O
ATOM 736 CB HIS A 94 7.174 -26.731 71.719 1.00 18.82 C
ANISOU 736 CB HIS A 94 2385 2288 2478 261 108 892 C
ATOM 737 CG HIS A 94 6.628 -27.606 72.807 1.00 31.18 C
ANISOU 737 CG HIS A 94 3888 3912 4046 232 104 1050 C
ATOM 738 ND1 HIS A 94 6.104 -28.859 72.562 1.00 37.74 N
ANISOU 738 ND1 HIS A 94 4667 4599 5072 221 148 1107 N
ATOM 739 CD2 HIS A 94 6.481 -27.392 74.138 1.00 35.39 C
ANISOU 739 CD2 HIS A 94 4397 4644 4407 201 66 1153 C
ATOM 740 CE1 HIS A 94 5.683 -29.389 73.698 1.00 38.85 C
ANISOU 740 CE1 HIS A 94 4753 4837 5171 195 133 1266 C
ATOM 741 NE2 HIS A 94 5.895 -28.518 74.669 1.00 33.00 N
ANISOU 741 NE2 HIS A 94 4026 4312 4200 180 83 1296 N
ATOM 742 N HIS A 95 4.860 -24.704 72.227 1.00 16.39 N
ANISOU 742 N HIS A 95 2210 2234 1783 213 184 722 N
ATOM 743 CA HIS A 95 3.733 -24.277 73.048 1.00 12.82 C
ANISOU 743 CA HIS A 95 1763 1919 1188 178 221 697 C
ATOM 744 C HIS A 95 2.478 -24.072 72.208 1.00 14.48 C
ANISOU 744 C HIS A 95 1996 2056 1450 182 293 619 C
ATOM 745 O HIS A 95 1.385 -24.512 72.589 1.00 12.49 O
ANISOU 745 O HIS A 95 1713 1834 1199 151 331 665 O
ATOM 746 CB HIS A 95 4.110 -22.993 73.775 1.00 14.61 C
ANISOU 746 CB HIS A 95 2019 2307 1224 164 204 577 C
ATOM 747 CG HIS A 95 3.059 -22.488 74.708 1.00 16.67 C
ANISOU 747 CG HIS A 95 2274 2701 1357 123 256 516 C
ATOM 748 ND1 HIS A 95 2.931 -22.950 76.000 1.00 20.07 N
ANISOU 748 ND1 HIS A 95 2660 3274 1693 74 246 614 N
ATOM 749 CD2 HIS A 95 2.109 -21.538 74.551 1.00 19.00 C
ANISOU 749 CD2 HIS A 95 2590 3007 1622 128 325 365 C
ATOM 750 CE1 HIS A 95 1.930 -22.323 76.590 1.00 24.41 C
ANISOU 750 CE1 HIS A 95 3211 3918 2144 46 315 514 C
ATOM 751 NE2 HIS A 95 1.420 -21.456 75.736 1.00 18.22 N
ANISOU 751 NE2 HIS A 95 2465 3047 1411 81 366 360 N
ATOM 752 N TYR A 96 2.617 -23.404 71.059 1.00 12.65 N
ANISOU 752 N TYR A 96 1810 1732 1265 210 304 499 N
ATOM 753 CA TYR A 96 1.467 -23.190 70.182 1.00 9.89 C
ANISOU 753 CA TYR A 96 1459 1324 974 199 349 423 C
ATOM 754 C TYR A 96 0.930 -24.509 69.649 1.00 9.78 C
ANISOU 754 C TYR A 96 1406 1204 1105 160 376 501 C
ATOM 755 O TYR A 96 -0.283 -24.721 69.625 1.00 11.82 O
ANISOU 755 O TYR A 96 1634 1483 1374 132 422 520 O
ATOM 756 CB TYR A 96 1.838 -22.226 69.044 1.00 11.31 C
ANISOU 756 CB TYR A 96 1671 1441 1185 209 322 285 C
ATOM 757 CG TYR A 96 1.994 -20.836 69.601 1.00 10.55 C
ANISOU 757 CG TYR A 96 1601 1421 986 240 320 196 C
ATOM 758 CD1 TYR A 96 0.882 -20.143 70.059 1.00 14.00 C
ANISOU 758 CD1 TYR A 96 2018 1920 1382 256 376 154 C
ATOM 759 CD2 TYR A 96 3.243 -20.239 69.725 1.00 11.93 C
ANISOU 759 CD2 TYR A 96 1807 1602 1125 248 274 140 C
ATOM 760 CE1 TYR A 96 1.002 -18.888 70.610 1.00 16.64 C
ANISOU 760 CE1 TYR A 96 2365 2298 1661 280 397 39 C
ATOM 761 CE2 TYR A 96 3.373 -18.979 70.282 1.00 14.41 C
ANISOU 761 CE2 TYR A 96 2139 1971 1367 260 284 32 C
ATOM 762 CZ TYR A 96 2.243 -18.315 70.726 1.00 15.80 C
ANISOU 762 CZ TYR A 96 2295 2186 1521 276 351 -27 C
ATOM 763 OH TYR A 96 2.332 -17.063 71.293 1.00 18.68 O
ANISOU 763 OH TYR A 96 2649 2573 1876 267 368 -166 O
ATOM 764 N ARG A 97 1.816 -25.426 69.251 1.00 10.86 N
ANISOU 764 N ARG A 97 1529 1222 1375 153 356 537 N
ATOM 765 CA ARG A 97 1.338 -26.737 68.819 1.00 12.92 C
ANISOU 765 CA ARG A 97 1743 1354 1813 107 399 588 C
ATOM 766 C ARG A 97 0.603 -27.456 69.945 1.00 14.81 C
ANISOU 766 C ARG A 97 1933 1655 2039 88 403 722 C
ATOM 767 O ARG A 97 -0.447 -28.065 69.719 1.00 15.32 O
ANISOU 767 O ARG A 97 1965 1683 2174 38 444 732 O
ATOM 768 CB ARG A 97 2.492 -27.593 68.309 1.00 18.39 C
ANISOU 768 CB ARG A 97 2406 1896 2684 112 385 571 C
ATOM 769 CG ARG A 97 2.050 -29.016 68.014 1.00 21.80 C
ANISOU 769 CG ARG A 97 2769 2202 3312 63 423 580 C
ATOM 770 CD ARG A 97 2.659 -29.560 66.751 1.00 24.80 C
ANISOU 770 CD ARG A 97 3122 2446 3856 32 454 419 C
ATOM 771 NE ARG A 97 2.418 -30.997 66.624 1.00 34.43 N
ANISOU 771 NE ARG A 97 4264 3545 5274 -3 495 420 N
ATOM 772 CZ ARG A 97 1.696 -31.562 65.660 1.00 47.31 C
ANISOU 772 CZ ARG A 97 5869 5115 6992 -84 553 281 C
ATOM 773 NH1 ARG A 97 1.145 -30.818 64.710 1.00 47.80 N
ANISOU 773 NH1 ARG A 97 5970 5244 6948 -151 568 138 N
ATOM 774 NH2 ARG A 97 1.540 -32.880 65.635 1.00 46.16 N
ANISOU 774 NH2 ARG A 97 5650 4851 7038 -106 595 283 N
ATOM 775 N GLU A 98 1.128 -27.374 71.168 1.00 12.99 N
ANISOU 775 N GLU A 98 1693 1536 1705 111 358 819 N
ATOM 776 CA GLU A 98 0.435 -27.986 72.294 1.00 14.80 C
ANISOU 776 CA GLU A 98 1876 1852 1895 79 362 945 C
ATOM 777 C GLU A 98 -0.908 -27.322 72.569 1.00 12.98 C
ANISOU 777 C GLU A 98 1655 1744 1534 54 411 894 C
ATOM 778 O GLU A 98 -1.847 -28.000 72.997 1.00 14.02 O
ANISOU 778 O GLU A 98 1744 1892 1690 12 441 969 O
ATOM 779 CB GLU A 98 1.322 -27.947 73.530 1.00 16.97 C
ANISOU 779 CB GLU A 98 2130 2255 2064 90 303 1050 C
ATOM 780 CG GLU A 98 2.438 -28.972 73.464 1.00 27.92 C
ANISOU 780 CG GLU A 98 3460 3520 3627 112 260 1155 C
ATOM 781 CD GLU A 98 1.944 -30.379 73.138 1.00 35.22 C
ANISOU 781 CD GLU A 98 4323 4278 4782 92 296 1229 C
ATOM 782 OE1 GLU A 98 1.181 -30.956 73.948 1.00 40.51 O
ANISOU 782 OE1 GLU A 98 4950 5006 5437 56 308 1350 O
ATOM 783 OE2 GLU A 98 2.317 -30.905 72.064 1.00 27.22 O
ANISOU 783 OE2 GLU A 98 3298 3078 3966 104 319 1149 O
ATOM 784 N GLN A 99 -1.032 -26.012 72.339 1.00 13.76 N
ANISOU 784 N GLN A 99 1796 1919 1512 82 424 765 N
ATOM 785 CA GLN A 99 -2.331 -25.381 72.564 1.00 12.06 C
ANISOU 785 CA GLN A 99 1565 1801 1215 70 480 703 C
ATOM 786 C GLN A 99 -3.336 -25.823 71.506 1.00 11.68 C
ANISOU 786 C GLN A 99 1487 1656 1295 43 518 687 C
ATOM 787 O GLN A 99 -4.503 -26.087 71.821 1.00 13.71 O
ANISOU 787 O GLN A 99 1697 1966 1547 8 558 714 O
ATOM 788 CB GLN A 99 -2.210 -23.850 72.580 1.00 13.01 C
ANISOU 788 CB GLN A 99 1720 2000 1224 115 492 555 C
ATOM 789 CG GLN A 99 -1.305 -23.289 73.666 1.00 12.87 C
ANISOU 789 CG GLN A 99 1725 2101 1063 114 463 529 C
ATOM 790 CD GLN A 99 -1.573 -23.894 75.030 1.00 17.93 C
ANISOU 790 CD GLN A 99 2331 2873 1609 59 468 630 C
ATOM 791 OE1 GLN A 99 -2.700 -23.876 75.513 1.00 17.44 O
ANISOU 791 OE1 GLN A 99 2235 2885 1506 32 529 621 O
ATOM 792 NE2 GLN A 99 -0.534 -24.444 75.657 1.00 24.04 N
ANISOU 792 NE2 GLN A 99 3099 3683 2352 44 403 738 N
ATOM 793 N ILE A 100 -2.892 -25.935 70.252 1.00 12.14 N
ANISOU 793 N ILE A 100 1564 1586 1461 44 507 637 N
ATOM 794 CA ILE A 100 -3.764 -26.439 69.194 1.00 12.44 C
ANISOU 794 CA ILE A 100 1563 1551 1614 -14 538 607 C
ATOM 795 C ILE A 100 -4.228 -27.846 69.525 1.00 15.63 C
ANISOU 795 C ILE A 100 1919 1889 2129 -78 554 698 C
ATOM 796 O ILE A 100 -5.418 -28.170 69.430 1.00 18.80 O
ANISOU 796 O ILE A 100 2270 2319 2555 -132 586 705 O
ATOM 797 CB ILE A 100 -3.038 -26.395 67.839 1.00 14.59 C
ANISOU 797 CB ILE A 100 1861 1717 1966 -32 515 502 C
ATOM 798 CG1 ILE A 100 -2.768 -24.945 67.437 1.00 11.48 C
ANISOU 798 CG1 ILE A 100 1502 1393 1467 23 473 404 C
ATOM 799 CG2 ILE A 100 -3.864 -27.109 66.777 1.00 14.76 C
ANISOU 799 CG2 ILE A 100 1826 1686 2095 -131 537 444 C
ATOM 800 CD1 ILE A 100 -1.695 -24.793 66.355 1.00 11.66 C
ANISOU 800 CD1 ILE A 100 1559 1347 1525 10 427 306 C
ATOM 801 N LYS A 101 -3.290 -28.706 69.922 1.00 14.23 N
ANISOU 801 N LYS A 101 1748 1623 2037 -70 528 774 N
ATOM 802 CA LYS A 101 -3.656 -30.069 70.290 1.00 15.11 C
ANISOU 802 CA LYS A 101 1808 1653 2282 -119 542 872 C
ATOM 803 C LYS A 101 -4.549 -30.101 71.522 1.00 17.80 C
ANISOU 803 C LYS A 101 2120 2137 2507 -133 555 983 C
ATOM 804 O LYS A 101 -5.426 -30.964 71.625 1.00 22.06 O
ANISOU 804 O LYS A 101 2612 2642 3129 -193 585 1039 O
ATOM 805 CB LYS A 101 -2.401 -30.902 70.507 1.00 23.51 C
ANISOU 805 CB LYS A 101 2860 2596 3477 -87 508 939 C
ATOM 806 CG LYS A 101 -1.668 -31.217 69.208 1.00 28.50 C
ANISOU 806 CG LYS A 101 3494 3057 4276 -94 520 800 C
ATOM 807 CD LYS A 101 -0.350 -31.923 69.483 1.00 38.53 C
ANISOU 807 CD LYS A 101 4732 4223 5684 -44 491 857 C
ATOM 808 CE LYS A 101 -0.543 -33.116 70.404 1.00 45.48 C
ANISOU 808 CE LYS A 101 5542 5076 6661 -47 487 1042 C
ATOM 809 NZ LYS A 101 0.762 -33.681 70.846 1.00 52.44 N
ANISOU 809 NZ LYS A 101 6369 5897 7660 11 450 1139 N
ATOM 810 N ARG A 102 -4.355 -29.167 72.454 1.00 15.85 N
ANISOU 810 N ARG A 102 1897 2055 2069 -91 539 997 N
ATOM 811 CA ARG A 102 -5.164 -29.156 73.667 1.00 16.33 C
ANISOU 811 CA ARG A 102 1926 2272 2005 -118 564 1074 C
ATOM 812 C ARG A 102 -6.613 -28.796 73.368 1.00 16.28 C
ANISOU 812 C ARG A 102 1889 2321 1975 -150 625 1003 C
ATOM 813 O ARG A 102 -7.534 -29.423 73.906 1.00 21.63 O
ANISOU 813 O ARG A 102 2518 3042 2659 -203 660 1081 O
ATOM 814 CB ARG A 102 -4.578 -28.181 74.690 1.00 17.42 C
ANISOU 814 CB ARG A 102 2094 2583 1943 -83 545 1055 C
ATOM 815 CG ARG A 102 -5.429 -28.046 75.943 1.00 18.25 C
ANISOU 815 CG ARG A 102 2163 2872 1899 -123 588 1098 C
ATOM 816 CD ARG A 102 -4.756 -27.170 76.996 1.00 18.57 C
ANISOU 816 CD ARG A 102 2226 3088 1743 -111 572 1058 C
ATOM 817 NE ARG A 102 -4.655 -25.788 76.539 1.00 17.83 N
ANISOU 817 NE ARG A 102 2177 3011 1588 -66 595 862 N
ATOM 818 CZ ARG A 102 -5.647 -24.908 76.630 1.00 17.29 C
ANISOU 818 CZ ARG A 102 2094 3014 1463 -61 674 731 C
ATOM 819 NH1 ARG A 102 -6.808 -25.266 77.176 1.00 18.60 N
ANISOU 819 NH1 ARG A 102 2205 3258 1605 -104 737 771 N
ATOM 820 NH2 ARG A 102 -5.482 -23.668 76.180 1.00 16.30 N
ANISOU 820 NH2 ARG A 102 1996 2873 1323 -12 693 562 N
ATOM 821 N VAL A 103 -6.839 -27.792 72.520 1.00 16.02 N
ANISOU 821 N VAL A 103 1869 2294 1922 -118 635 866 N
ATOM 822 CA VAL A 103 -8.205 -27.318 72.322 1.00 16.04 C
ANISOU 822 CA VAL A 103 1818 2373 1904 -133 687 807 C
ATOM 823 C VAL A 103 -8.938 -28.123 71.250 1.00 16.97 C
ANISOU 823 C VAL A 103 1888 2391 2168 -203 693 806 C
ATOM 824 O VAL A 103 -10.160 -28.276 71.329 1.00 20.62 O
ANISOU 824 O VAL A 103 2285 2912 2638 -246 733 813 O
ATOM 825 CB VAL A 103 -8.248 -25.809 72.004 1.00 17.04 C
ANISOU 825 CB VAL A 103 1952 2563 1960 -60 696 678 C
ATOM 826 CG1 VAL A 103 -7.540 -25.011 73.097 1.00 18.93 C
ANISOU 826 CG1 VAL A 103 2235 2902 2057 -16 701 642 C
ATOM 827 CG2 VAL A 103 -7.679 -25.500 70.629 1.00 20.98 C
ANISOU 827 CG2 VAL A 103 2475 2957 2538 -38 656 617 C
ATOM 828 N LYS A 104 -8.220 -28.680 70.279 1.00 20.94 N
ANISOU 828 N LYS A 104 2952 3166 1837 -507 871 877 N
ATOM 829 CA LYS A 104 -8.856 -29.457 69.222 1.00 20.99 C
ANISOU 829 CA LYS A 104 2826 3114 2035 -627 894 890 C
ATOM 830 C LYS A 104 -9.059 -30.895 69.678 1.00 23.17 C
ANISOU 830 C LYS A 104 3142 3246 2414 -732 1005 1034 C
ATOM 831 O LYS A 104 -8.136 -31.524 70.205 1.00 26.75 O
ANISOU 831 O LYS A 104 3735 3603 2827 -715 982 1133 O
ATOM 832 CB LYS A 104 -8.009 -29.434 67.949 1.00 19.16 C
ANISOU 832 CB LYS A 104 2575 2836 1870 -643 759 813 C
ATOM 833 CG LYS A 104 -7.808 -28.054 67.336 1.00 22.65 C
ANISOU 833 CG LYS A 104 2980 3391 2234 -549 666 672 C
ATOM 834 CD LYS A 104 -9.092 -27.526 66.706 1.00 22.41 C
ANISOU 834 CD LYS A 104 2767 3486 2260 -587 706 618 C
ATOM 835 CE LYS A 104 -9.277 -28.017 65.274 1.00 22.01 C
ANISOU 835 CE LYS A 104 2589 3471 2301 -735 625 556 C
ATOM 836 NZ LYS A 104 -10.615 -27.649 64.726 1.00 19.79 N
ANISOU 836 NZ LYS A 104 2083 3368 2070 -777 635 549 N
ATOM 837 N ASP A 105 -10.269 -31.416 69.473 1.00 25.61 N
ANISOU 837 N ASP A 105 3324 3544 2861 -859 1119 1044 N
ATOM 838 CA ASP A 105 -10.511 -32.827 69.755 1.00 26.91 C
ANISOU 838 CA ASP A 105 3530 3526 3168 -992 1234 1131 C
ATOM 839 C ASP A 105 -9.793 -33.723 68.755 1.00 26.81 C
ANISOU 839 C ASP A 105 3407 3407 3372 -1047 1097 1218 C
ATOM 840 O ASP A 105 -9.389 -34.838 69.102 1.00 30.25 O
ANISOU 840 O ASP A 105 3994 3694 3806 -1203 1108 1289 O
ATOM 841 CB ASP A 105 -12.011 -33.126 69.742 1.00 28.83 C
ANISOU 841 CB ASP A 105 3594 3811 3549 -1108 1360 1138 C
ATOM 842 CG ASP A 105 -12.766 -32.411 70.850 1.00 37.38 C
ANISOU 842 CG ASP A 105 4700 5060 4441 -1077 1443 1152 C
ATOM 843 OD1 ASP A 105 -12.128 -31.981 71.838 1.00 33.13 O
ANISOU 843 OD1 ASP A 105 4320 4582 3686 -978 1417 1197 O
ATOM 844 OD2 ASP A 105 -14.003 -32.286 70.736 1.00 40.73 O
ANISOU 844 OD2 ASP A 105 4954 5568 4953 -1147 1532 1134 O
ATOM 845 N SER A 106 -9.623 -33.255 67.521 1.00 30.35 N
ANISOU 845 N SER A 106 3841 3842 3847 -1105 1045 1011 N
ATOM 846 CA SER A 106 -8.991 -34.067 66.490 1.00 35.99 C
ANISOU 846 CA SER A 106 4614 4351 4711 -1225 1005 895 C
ATOM 847 C SER A 106 -7.503 -34.230 66.776 1.00 35.84 C
ANISOU 847 C SER A 106 4751 4198 4670 -1076 957 1005 C
ATOM 848 O SER A 106 -6.840 -33.305 67.248 1.00 34.43 O
ANISOU 848 O SER A 106 4608 4167 4307 -915 867 1079 O
ATOM 849 CB SER A 106 -9.204 -33.426 65.116 1.00 42.58 C
ANISOU 849 CB SER A 106 5380 5298 5499 -1322 904 624 C
ATOM 850 OG SER A 106 -8.620 -34.206 64.086 1.00 49.98 O
ANISOU 850 OG SER A 106 6390 6030 6571 -1439 909 453 O
ATOM 851 N GLU A 107 -6.977 -35.423 66.499 1.00 41.71 N
ANISOU 851 N GLU A 107 5582 4659 5606 -1115 1026 1001 N
ATOM 852 CA GLU A 107 -5.555 -35.674 66.706 1.00 48.40 C
ANISOU 852 CA GLU A 107 6546 5367 6476 -934 999 1114 C
ATOM 853 C GLU A 107 -4.703 -35.161 65.555 1.00 47.77 C
ANISOU 853 C GLU A 107 6493 5238 6421 -879 932 938 C
ATOM 854 O GLU A 107 -3.519 -34.866 65.758 1.00 50.39 O
ANISOU 854 O GLU A 107 6871 5568 6708 -700 857 1036 O
ATOM 855 CB GLU A 107 -5.314 -37.172 66.911 1.00 59.32 C
ANISOU 855 CB GLU A 107 7990 6456 8093 -932 1154 1210 C
ATOM 856 CG GLU A 107 -6.003 -38.056 65.882 1.00 67.02 C
ANISOU 856 CG GLU A 107 8963 7213 9289 -1131 1287 972 C
ATOM 857 CD GLU A 107 -6.270 -39.456 66.401 1.00 80.34 C
ANISOU 857 CD GLU A 107 10683 8669 11174 -1190 1479 1082 C
ATOM 858 OE1 GLU A 107 -5.813 -39.774 67.520 1.00 84.80 O
ANISOU 858 OE1 GLU A 107 11257 9267 11697 -1074 1503 1364 O
ATOM 859 OE2 GLU A 107 -6.942 -40.237 65.693 1.00 85.66 O
ANISOU 859 OE2 GLU A 107 11377 9139 12031 -1361 1616 873 O
ATOM 860 N ASP A 108 -5.281 -35.038 64.365 1.00 39.77 N
ANISOU 860 N ASP A 108 5443 4220 5447 -1044 944 666 N
ATOM 861 CA ASP A 108 -4.597 -34.534 63.178 1.00 32.70 C
ANISOU 861 CA ASP A 108 4584 3312 4530 -1034 883 457 C
ATOM 862 C ASP A 108 -5.227 -33.189 62.826 1.00 30.51 C
ANISOU 862 C ASP A 108 4217 3350 4025 -1100 756 345 C
ATOM 863 O ASP A 108 -6.346 -33.134 62.308 1.00 32.48 O
ANISOU 863 O ASP A 108 4352 3755 4235 -1279 735 200 O
ATOM 864 CB ASP A 108 -4.718 -35.536 62.034 1.00 37.68 C
ANISOU 864 CB ASP A 108 5251 3748 5316 -1187 985 207 C
ATOM 865 CG ASP A 108 -4.218 -34.983 60.715 1.00 45.51 C
ANISOU 865 CG ASP A 108 6259 4818 6216 -1225 912 -47 C
ATOM 866 OD1 ASP A 108 -3.122 -34.383 60.694 1.00 49.85 O
ANISOU 866 OD1 ASP A 108 6853 5353 6733 -1050 855 14 O
ATOM 867 OD2 ASP A 108 -4.928 -35.145 59.700 1.00 55.03 O
ANISOU 867 OD2 ASP A 108 7420 6131 7357 -1431 901 -294 O
ATOM 868 N VAL A 109 -4.528 -32.105 63.125 1.00 17.73 N
ANISOU 868 N VAL A 109 2607 1878 2251 -906 628 419 N
ATOM 869 CA VAL A 109 -5.032 -30.755 62.881 1.00 15.99 C
ANISOU 869 CA VAL A 109 2275 1963 1838 -860 489 339 C
ATOM 870 C VAL A 109 -4.190 -30.115 61.789 1.00 14.54 C
ANISOU 870 C VAL A 109 2103 1804 1617 -780 381 196 C
ATOM 871 O VAL A 109 -2.960 -30.070 61.916 1.00 13.68 O
ANISOU 871 O VAL A 109 2082 1574 1540 -634 357 251 O
ATOM 872 CB VAL A 109 -5.005 -29.894 64.158 1.00 15.24 C
ANISOU 872 CB VAL A 109 2182 2017 1590 -705 458 502 C
ATOM 873 CG1 VAL A 109 -5.483 -28.486 63.838 1.00 15.49 C
ANISOU 873 CG1 VAL A 109 2112 2285 1489 -638 383 415 C
ATOM 874 CG2 VAL A 109 -5.872 -30.527 65.226 1.00 17.05 C
ANISOU 874 CG2 VAL A 109 2399 2249 1830 -786 585 655 C
ATOM 875 N PRO A 110 -4.802 -29.596 60.717 1.00 14.18 N
ANISOU 875 N PRO A 110 1946 1944 1497 -865 313 47 N
ATOM 876 CA PRO A 110 -4.033 -28.899 59.671 1.00 13.13 C
ANISOU 876 CA PRO A 110 1818 1865 1305 -778 221 -57 C
ATOM 877 C PRO A 110 -3.223 -27.733 60.222 1.00 12.80 C
ANISOU 877 C PRO A 110 1802 1860 1200 -543 154 42 C
ATOM 878 O PRO A 110 -3.753 -26.837 60.888 1.00 10.53 O
ANISOU 878 O PRO A 110 1454 1714 833 -467 144 119 O
ATOM 879 CB PRO A 110 -5.120 -28.428 58.699 1.00 13.51 C
ANISOU 879 CB PRO A 110 1690 2204 1241 -902 153 -140 C
ATOM 880 CG PRO A 110 -6.203 -29.453 58.848 1.00 15.73 C
ANISOU 880 CG PRO A 110 1911 2492 1573 -1153 226 -180 C
ATOM 881 CD PRO A 110 -6.213 -29.779 60.333 1.00 15.69 C
ANISOU 881 CD PRO A 110 1981 2321 1658 -1072 322 -13 C
ATOM 882 N MET A 111 -1.917 -27.768 59.960 1.00 11.38 N
ANISOU 882 N MET A 111 1714 1538 1070 -444 136 27 N
ATOM 883 CA MET A 111 -0.967 -26.775 60.445 1.00 10.07 C
ANISOU 883 CA MET A 111 1574 1395 859 -271 72 95 C
ATOM 884 C MET A 111 0.123 -26.595 59.410 1.00 10.30 C
ANISOU 884 C MET A 111 1626 1354 933 -206 44 18 C
ATOM 885 O MET A 111 0.510 -27.553 58.737 1.00 12.01 O
ANISOU 885 O MET A 111 1893 1421 1248 -262 107 -47 O
ATOM 886 CB MET A 111 -0.273 -27.202 61.742 1.00 12.38 C
ANISOU 886 CB MET A 111 1934 1598 1172 -213 79 250 C
ATOM 887 CG MET A 111 -1.131 -27.344 62.939 1.00 17.92 C
ANISOU 887 CG MET A 111 2634 2378 1797 -258 119 353 C
ATOM 888 SD MET A 111 -0.012 -27.849 64.250 1.00 19.99 S
ANISOU 888 SD MET A 111 2956 2601 2038 -183 93 576 S
ATOM 889 CE MET A 111 -1.148 -28.692 65.333 1.00 36.80 C
ANISOU 889 CE MET A 111 5099 4744 4141 -276 206 724 C
ATOM 890 N VAL A 112 0.663 -25.379 59.339 1.00 7.43 N
ANISOU 890 N VAL A 112 1238 1069 515 -93 -14 23 N
ATOM 891 CA VAL A 112 1.865 -25.106 58.564 1.00 6.94 C
ANISOU 891 CA VAL A 112 1192 940 505 -13 -31 -13 C
ATOM 892 C VAL A 112 2.836 -24.336 59.440 1.00 9.23 C
ANISOU 892 C VAL A 112 1487 1231 789 80 -84 62 C
ATOM 893 O VAL A 112 2.435 -23.426 60.169 1.00 10.09 O
ANISOU 893 O VAL A 112 1568 1434 831 77 -93 66 O
ATOM 894 CB VAL A 112 1.533 -24.331 57.272 1.00 8.09 C
ANISOU 894 CB VAL A 112 1276 1210 586 -6 -37 -93 C
ATOM 895 CG1 VAL A 112 2.808 -23.809 56.586 1.00 11.44 C
ANISOU 895 CG1 VAL A 112 1713 1577 1058 93 -38 -106 C
ATOM 896 CG2 VAL A 112 0.738 -25.210 56.324 1.00 9.21 C
ANISOU 896 CG2 VAL A 112 1404 1405 689 -155 -7 -195 C
ATOM 897 N LEU A 113 4.108 -24.723 59.398 1.00 7.83 N
ANISOU 897 N LEU A 113 1316 954 706 137 -98 114 N
ATOM 898 CA LEU A 113 5.165 -24.004 60.102 1.00 7.37 C
ANISOU 898 CA LEU A 113 1225 946 631 184 -173 179 C
ATOM 899 C LEU A 113 5.725 -22.931 59.180 1.00 8.50 C
ANISOU 899 C LEU A 113 1337 1094 800 230 -167 93 C
ATOM 900 O LEU A 113 6.124 -23.232 58.051 1.00 7.99 O
ANISOU 900 O LEU A 113 1265 953 819 272 -117 61 O
ATOM 901 CB LEU A 113 6.276 -24.967 60.529 1.00 7.81 C
ANISOU 901 CB LEU A 113 1246 928 794 236 -193 341 C
ATOM 902 CG LEU A 113 7.445 -24.363 61.311 1.00 8.10 C
ANISOU 902 CG LEU A 113 1197 1071 808 226 -301 410 C
ATOM 903 CD1 LEU A 113 6.961 -23.836 62.657 1.00 12.60 C
ANISOU 903 CD1 LEU A 113 1797 1792 1197 155 -340 371 C
ATOM 904 CD2 LEU A 113 8.545 -25.396 61.492 1.00 11.19 C
ANISOU 904 CD2 LEU A 113 1518 1398 1335 302 -285 552 C
ATOM 905 N VAL A 114 5.765 -21.691 59.662 1.00 7.46 N
ANISOU 905 N VAL A 114 1182 1031 620 200 -176 47 N
ATOM 906 CA VAL A 114 6.211 -20.554 58.867 1.00 7.40 C
ANISOU 906 CA VAL A 114 1161 1007 643 252 -144 -11 C
ATOM 907 C VAL A 114 7.393 -19.899 59.562 1.00 7.24 C
ANISOU 907 C VAL A 114 1105 1008 636 204 -198 -16 C
ATOM 908 O VAL A 114 7.271 -19.436 60.701 1.00 9.06 O
ANISOU 908 O VAL A 114 1364 1317 763 108 -225 -59 O
ATOM 909 CB VAL A 114 5.085 -19.538 58.651 1.00 7.36 C
ANISOU 909 CB VAL A 114 1158 1023 617 259 -51 -58 C
ATOM 910 CG1 VAL A 114 5.615 -18.285 57.953 1.00 10.26 C
ANISOU 910 CG1 VAL A 114 1508 1341 1051 321 26 -82 C
ATOM 911 CG2 VAL A 114 3.942 -20.175 57.856 1.00 8.65 C
ANISOU 911 CG2 VAL A 114 1278 1219 790 256 -28 -31 C
ATOM 912 N GLY A 115 8.544 -19.888 58.885 1.00 7.33 N
ANISOU 912 N GLY A 115 1049 975 762 247 -207 18 N
ATOM 913 CA GLY A 115 9.699 -19.147 59.346 1.00 8.39 C
ANISOU 913 CA GLY A 115 1110 1152 924 175 -256 6 C
ATOM 914 C GLY A 115 9.772 -17.819 58.619 1.00 9.63 C
ANISOU 914 C GLY A 115 1278 1224 1158 177 -139 -88 C
ATOM 915 O GLY A 115 10.164 -17.760 57.448 1.00 9.21 O
ANISOU 915 O GLY A 115 1188 1098 1212 271 -71 -50 O
ATOM 916 N ASN A 116 9.376 -16.748 59.293 1.00 7.62 N
ANISOU 916 N ASN A 116 1080 960 854 77 -77 -207 N
ATOM 917 CA ASN A 116 9.259 -15.437 58.669 1.00 7.47 C
ANISOU 917 CA ASN A 116 1085 806 948 98 96 -272 C
ATOM 918 C ASN A 116 10.528 -14.595 58.883 1.00 8.74 C
ANISOU 918 C ASN A 116 1188 933 1198 -42 108 -351 C
ATOM 919 O ASN A 116 11.412 -14.924 59.682 1.00 9.69 O
ANISOU 919 O ASN A 116 1238 1190 1252 -184 -42 -369 O
ATOM 920 CB ASN A 116 8.023 -14.717 59.225 1.00 7.62 C
ANISOU 920 CB ASN A 116 1205 771 921 83 235 -357 C
ATOM 921 CG ASN A 116 7.692 -13.436 58.480 1.00 10.61 C
ANISOU 921 CG ASN A 116 1568 1016 1449 152 410 -313 C
ATOM 922 OD1 ASN A 116 7.698 -13.407 57.246 1.00 10.61 O
ANISOU 922 OD1 ASN A 116 1496 1031 1505 251 398 -171 O
ATOM 923 ND2 ASN A 116 7.403 -12.376 59.219 1.00 11.10 N
ANISOU 923 ND2 ASN A 116 1680 996 1543 57 535 -401 N
ATOM 924 N LYS A 117 10.591 -13.473 58.151 1.00 8.86 N
ANISOU 924 N LYS A 117 1199 1173 994 -172 352 -204 N
ATOM 925 CA LYS A 117 11.707 -12.510 58.157 1.00 9.48 C
ANISOU 925 CA LYS A 117 1290 1227 1086 -258 432 -350 C
ATOM 926 C LYS A 117 12.950 -13.077 57.476 1.00 10.12 C
ANISOU 926 C LYS A 117 1241 1384 1219 -304 425 -456 C
ATOM 927 O LYS A 117 14.083 -12.738 57.840 1.00 13.24 O
ANISOU 927 O LYS A 117 1537 1801 1694 -382 415 -520 O
ATOM 928 CB LYS A 117 12.046 -12.009 59.576 1.00 11.95 C
ANISOU 928 CB LYS A 117 1700 1465 1377 -242 379 -416 C
ATOM 929 CG LYS A 117 10.838 -11.491 60.366 1.00 10.69 C
ANISOU 929 CG LYS A 117 1734 1222 1105 -75 456 -273 C
ATOM 930 CD LYS A 117 11.239 -10.580 61.517 1.00 11.75 C
ANISOU 930 CD LYS A 117 2153 1187 1124 -37 419 -358 C
ATOM 931 CE LYS A 117 10.026 -10.229 62.394 1.00 13.89 C
ANISOU 931 CE LYS A 117 2676 1378 1222 259 562 -177 C
ATOM 932 NZ LYS A 117 10.352 -9.233 63.461 1.00 15.15 N
ANISOU 932 NZ LYS A 117 3209 1323 1225 330 479 -231 N
ATOM 933 N CYS A 118 12.759 -13.900 56.443 1.00 10.34 N
ANISOU 933 N CYS A 118 1296 1438 1195 -242 424 -430 N
ATOM 934 CA ACYS A 118 13.896 -14.524 55.771 0.50 12.38 C
ANISOU 934 CA ACYS A 118 1496 1765 1443 -171 482 -488 C
ATOM 935 CA BCYS A 118 13.908 -14.511 55.785 0.50 12.46 C
ANISOU 935 CA BCYS A 118 1503 1776 1456 -173 483 -489 C
ATOM 936 C CYS A 118 14.704 -13.534 54.939 1.00 12.89 C
ANISOU 936 C CYS A 118 1479 1867 1553 -214 681 -445 C
ATOM 937 O CYS A 118 15.752 -13.916 54.395 1.00 15.89 O
ANISOU 937 O CYS A 118 1761 2334 1941 -107 802 -415 O
ATOM 938 CB ACYS A 118 13.426 -15.709 54.909 0.50 14.35 C
ANISOU 938 CB ACYS A 118 1950 1957 1544 -43 395 -476 C
ATOM 939 CB BCYS A 118 13.446 -15.695 54.949 0.50 14.34 C
ANISOU 939 CB BCYS A 118 1940 1960 1549 -45 396 -478 C
ATOM 940 SG ACYS A 118 12.385 -15.358 53.458 0.50 16.08 S
ANISOU 940 SG ACYS A 118 2431 2049 1631 -56 391 -373 S
ATOM 941 SG BCYS A 118 13.034 -17.073 56.001 0.50 13.14 S
ANISOU 941 SG BCYS A 118 1809 1790 1395 -6 145 -504 S
ATOM 942 N ASP A 119 14.246 -12.283 54.830 1.00 13.41 N
ANISOU 942 N ASP A 119 1580 1871 1645 -337 738 -401 N
ATOM 943 CA ASP A 119 15.020 -11.235 54.179 1.00 16.16 C
ANISOU 943 CA ASP A 119 1828 2241 2070 -422 898 -330 C
ATOM 944 C ASP A 119 16.206 -10.784 55.024 1.00 16.77 C
ANISOU 944 C ASP A 119 1683 2359 2331 -570 829 -299 C
ATOM 945 O ASP A 119 17.100 -10.107 54.506 1.00 19.61 O
ANISOU 945 O ASP A 119 1872 2766 2814 -654 924 -163 O
ATOM 946 CB ASP A 119 14.118 -10.035 53.902 1.00 15.79 C
ANISOU 946 CB ASP A 119 1940 2075 1986 -488 890 -283 C
ATOM 947 CG ASP A 119 13.423 -9.531 55.166 1.00 14.60 C
ANISOU 947 CG ASP A 119 1893 1833 1823 -571 818 -326 C
ATOM 948 OD1 ASP A 119 12.461 -10.187 55.628 1.00 12.91 O
ANISOU 948 OD1 ASP A 119 1757 1610 1540 -468 747 -317 O
ATOM 949 OD2 ASP A 119 13.847 -8.490 55.708 1.00 17.15 O
ANISOU 949 OD2 ASP A 119 2257 2064 2194 -701 781 -329 O
ATOM 950 N LEU A 120 16.224 -11.142 56.357 1.00 14.62 N
ANISOU 950 N LEU A 120 1415 2053 2087 -612 625 -384 N
ATOM 951 CA LEU A 120 17.238 -10.624 57.277 1.00 17.62 C
ANISOU 951 CA LEU A 120 1660 2407 2629 -801 454 -346 C
ATOM 952 C LEU A 120 18.480 -11.516 57.292 1.00 22.41 C
ANISOU 952 C LEU A 120 1946 3189 3380 -753 452 -256 C
ATOM 953 O LEU A 120 18.366 -12.743 57.217 1.00 23.06 O
ANISOU 953 O LEU A 120 2022 3361 3377 -543 505 -319 O
ATOM 954 CB LEU A 120 16.675 -10.528 58.694 1.00 17.47 C
ANISOU 954 CB LEU A 120 1881 2233 2523 -828 235 -470 C
ATOM 955 CG LEU A 120 15.540 -9.524 58.909 1.00 15.06 C
ANISOU 955 CG LEU A 120 1921 1742 2060 -815 258 -501 C
ATOM 956 CD1 LEU A 120 15.100 -9.519 60.363 1.00 20.19 C
ANISOU 956 CD1 LEU A 120 2850 2242 2580 -739 93 -584 C
ATOM 957 CD2 LEU A 120 15.956 -8.127 58.485 1.00 17.91 C
ANISOU 957 CD2 LEU A 120 2348 1978 2478 -1018 244 -425 C
ATOM 958 N PRO A 121 19.667 -10.915 57.444 1.00 25.02 N
ANISOU 958 N PRO A 121 2008 3558 3940 -950 365 -67 N
ATOM 959 CA PRO A 121 20.918 -11.689 57.372 1.00 26.01 C
ANISOU 959 CA PRO A 121 1760 3878 4244 -892 371 106 C
ATOM 960 C PRO A 121 21.257 -12.404 58.670 1.00 30.71 C
ANISOU 960 C PRO A 121 2362 4434 4874 -957 72 7 C
ATOM 961 O PRO A 121 21.976 -13.412 58.688 1.00 33.96 O
ANISOU 961 O PRO A 121 2544 5006 5355 -839 85 102 O
ATOM 962 CB PRO A 121 21.959 -10.613 57.048 1.00 33.09 C
ANISOU 962 CB PRO A 121 2474 4793 5306 -1061 345 349 C
ATOM 963 CG PRO A 121 21.406 -9.376 57.711 1.00 28.50 C
ANISOU 963 CG PRO A 121 2160 3951 4719 -1340 120 264 C
ATOM 964 CD PRO A 121 19.911 -9.468 57.561 1.00 24.99 C
ANISOU 964 CD PRO A 121 2022 3414 4058 -1244 240 52 C
ATOM 965 N SER A 122 20.775 -11.854 59.775 1.00 34.31 N
ANISOU 965 N SER A 122 3164 4669 5205 -1070 -163 -192 N
ATOM 966 CA SER A 122 21.040 -12.406 61.096 1.00 48.64 C
ANISOU 966 CA SER A 122 5099 6389 6992 -1135 -473 -278 C
ATOM 967 C SER A 122 20.052 -13.535 61.330 1.00 49.46 C
ANISOU 967 C SER A 122 5280 6556 6955 -872 -410 -463 C
ATOM 968 O SER A 122 18.922 -13.296 61.771 1.00 53.08 O
ANISOU 968 O SER A 122 6048 6869 7251 -819 -551 -591 O
ATOM 969 CB SER A 122 20.911 -11.332 62.170 1.00 54.16 C
ANISOU 969 CB SER A 122 6235 6788 7554 -1246 -667 -400 C
ATOM 970 OG SER A 122 19.728 -10.575 61.978 1.00 62.22 O
ANISOU 970 OG SER A 122 7502 7704 8436 -1176 -856 -513 O
ATOM 971 N ARG A 123 20.480 -14.763 61.042 1.00 43.76 N
ANISOU 971 N ARG A 123 4348 6036 6241 -659 -183 -421 N
ATOM 972 CA ARG A 123 19.607 -15.922 61.134 1.00 25.22 C
ANISOU 972 CA ARG A 123 2140 3720 3722 -417 -128 -572 C
ATOM 973 C ARG A 123 20.100 -16.832 62.246 1.00 23.32 C
ANISOU 973 C ARG A 123 1815 3517 3529 -383 -312 -589 C
ATOM 974 O ARG A 123 21.188 -17.412 62.146 1.00 28.94 O
ANISOU 974 O ARG A 123 2256 4368 4370 -338 -283 -431 O
ATOM 975 CB ARG A 123 19.558 -16.658 59.805 1.00 33.50 C
ANISOU 975 CB ARG A 123 3156 4883 4689 -188 137 -525 C
ATOM 976 CG ARG A 123 18.682 -17.829 59.831 1.00 26.27 C
ANISOU 976 CG ARG A 123 2347 3996 3638 42 125 -619 C
ATOM 977 CD ARG A 123 18.503 -18.502 58.479 1.00 25.28 C
ANISOU 977 CD ARG A 123 2406 3866 3334 270 315 -606 C
ATOM 978 NE ARG A 123 17.318 -19.334 58.623 1.00 28.15 N
ANISOU 978 NE ARG A 123 3063 4100 3534 318 165 -724 N
ATOM 979 CZ ARG A 123 16.543 -19.737 57.636 1.00 23.41 C
ANISOU 979 CZ ARG A 123 2739 3385 2771 378 171 -724 C
ATOM 980 NH1 ARG A 123 16.816 -19.402 56.377 1.00 31.15 N
ANISOU 980 NH1 ARG A 123 3793 4359 3683 442 359 -660 N
ATOM 981 NH2 ARG A 123 15.488 -20.482 57.920 1.00 23.87 N
ANISOU 981 NH2 ARG A 123 3000 3326 2745 363 -37 -753 N
ATOM 982 N THR A 124 19.313 -16.937 63.317 1.00 16.17 N
ANISOU 982 N THR A 124 1196 2465 2483 -353 -451 -694 N
ATOM 983 CA THR A 124 19.718 -17.753 64.452 1.00 17.61 C
ANISOU 983 CA THR A 124 1411 2635 2645 -296 -580 -678 C
ATOM 984 C THR A 124 18.988 -19.086 64.495 1.00 18.12 C
ANISOU 984 C THR A 124 1572 2723 2591 -73 -491 -761 C
ATOM 985 O THR A 124 19.386 -19.962 65.272 1.00 21.51 O
ANISOU 985 O THR A 124 1998 3160 3015 -8 -551 -749 O
ATOM 986 CB THR A 124 19.493 -17.008 65.780 1.00 17.96 C
ANISOU 986 CB THR A 124 1735 2499 2590 -405 -760 -680 C
ATOM 987 OG1 THR A 124 18.153 -16.488 65.810 1.00 18.17 O
ANISOU 987 OG1 THR A 124 2030 2407 2466 -326 -672 -746 O
ATOM 988 CG2 THR A 124 20.505 -15.886 65.958 1.00 20.51 C
ANISOU 988 CG2 THR A 124 1999 2794 3000 -676 -929 -595 C
ATOM 989 N VAL A 125 17.928 -19.242 63.703 1.00 13.63 N
ANISOU 989 N VAL A 125 1098 2149 1932 13 -382 -811 N
ATOM 990 CA VAL A 125 17.215 -20.505 63.538 1.00 11.46 C
ANISOU 990 CA VAL A 125 919 1867 1568 171 -357 -822 C
ATOM 991 C VAL A 125 17.488 -20.998 62.120 1.00 14.00 C
ANISOU 991 C VAL A 125 1153 2316 1849 271 -310 -898 C
ATOM 992 O VAL A 125 17.008 -20.401 61.149 1.00 14.57 O
ANISOU 992 O VAL A 125 1313 2345 1877 240 -202 -854 O
ATOM 993 CB VAL A 125 15.707 -20.351 63.790 1.00 13.40 C
ANISOU 993 CB VAL A 125 1334 2002 1754 177 -343 -717 C
ATOM 994 CG1 VAL A 125 15.006 -21.700 63.632 1.00 15.14 C
ANISOU 994 CG1 VAL A 125 1630 2183 1938 261 -375 -645 C
ATOM 995 CG2 VAL A 125 15.444 -19.750 65.172 1.00 13.81 C
ANISOU 995 CG2 VAL A 125 1472 1984 1792 160 -389 -686 C
ATOM 996 N ASP A 126 18.248 -22.091 62.001 1.00 15.77 N
ANISOU 996 N ASP A 126 1334 2613 2046 441 -299 -908 N
ATOM 997 CA ASP A 126 18.644 -22.640 60.708 1.00 16.40 C
ANISOU 997 CA ASP A 126 1512 2712 2007 651 -131 -862 C
ATOM 998 C ASP A 126 17.456 -23.234 59.969 1.00 14.25 C
ANISOU 998 C ASP A 126 1613 2255 1547 679 -221 -863 C
ATOM 999 O ASP A 126 16.500 -23.722 60.578 1.00 16.35 O
ANISOU 999 O ASP A 126 1966 2409 1836 577 -401 -809 O
ATOM 1000 CB ASP A 126 19.693 -23.745 60.881 1.00 18.08 C
ANISOU 1000 CB ASP A 126 1685 2995 2188 847 -95 -807 C
ATOM 1001 CG ASP A 126 20.989 -23.242 61.464 1.00 38.80 C
ANISOU 1001 CG ASP A 126 3939 5772 5031 778 -29 -668 C
ATOM 1002 OD1 ASP A 126 21.264 -22.028 61.365 1.00 44.83 O
ANISOU 1002 OD1 ASP A 126 4490 6592 5953 619 28 -575 O
ATOM 1003 OD2 ASP A 126 21.742 -24.072 62.011 1.00 40.74 O
ANISOU 1003 OD2 ASP A 126 4120 6058 5303 857 -62 -615 O
ATOM 1004 N THR A 127 17.549 -23.232 58.635 1.00 16.13 N
ANISOU 1004 N THR A 127 1780 2671 1678 331 650 -660 N
ATOM 1005 CA THR A 127 16.544 -23.923 57.830 1.00 15.46 C
ANISOU 1005 CA THR A 127 1899 2355 1621 421 610 -703 C
ATOM 1006 C THR A 127 16.390 -25.371 58.272 1.00 17.73 C
ANISOU 1006 C THR A 127 2055 2533 2149 647 512 -762 C
ATOM 1007 O THR A 127 15.265 -25.859 58.437 1.00 16.07 O
ANISOU 1007 O THR A 127 1986 2166 1952 680 374 -732 O
ATOM 1008 CB THR A 127 16.927 -23.866 56.353 1.00 18.67 C
ANISOU 1008 CB THR A 127 2448 2713 1932 405 726 -775 C
ATOM 1009 OG1 THR A 127 16.903 -22.506 55.907 1.00 23.07 O
ANISOU 1009 OG1 THR A 127 3130 3326 2308 282 714 -670 O
ATOM 1010 CG2 THR A 127 15.953 -24.706 55.513 1.00 21.84 C
ANISOU 1010 CG2 THR A 127 3057 2950 2290 446 680 -846 C
ATOM 1011 N LYS A 128 17.515 -26.062 58.498 1.00 18.39 N
ANISOU 1011 N LYS A 128 1861 2657 2471 811 560 -780 N
ATOM 1012 CA LYS A 128 17.470 -27.476 58.864 1.00 21.52 C
ANISOU 1012 CA LYS A 128 2174 2831 3171 1029 464 -727 C
ATOM 1013 C LYS A 128 16.771 -27.691 60.201 1.00 22.07 C
ANISOU 1013 C LYS A 128 2229 2859 3298 1002 175 -507 C
ATOM 1014 O LYS A 128 16.032 -28.668 60.364 1.00 20.69 O
ANISOU 1014 O LYS A 128 2176 2441 3243 1092 59 -485 O
ATOM 1015 CB LYS A 128 18.882 -28.063 58.909 1.00 26.73 C
ANISOU 1015 CB LYS A 128 2511 3529 4117 1209 580 -656 C
ATOM 1016 CG LYS A 128 18.905 -29.552 59.236 1.00 32.87 C
ANISOU 1016 CG LYS A 128 3265 4056 5168 1447 517 -535 C
ATOM 1017 CD LYS A 128 20.319 -30.068 59.454 1.00 38.77 C
ANISOU 1017 CD LYS A 128 3627 4937 6167 1661 534 -397 C
ATOM 1018 CE LYS A 128 20.342 -31.587 59.561 1.00 45.21 C
ANISOU 1018 CE LYS A 128 4496 5465 7217 1901 512 -375 C
ATOM 1019 NZ LYS A 128 19.366 -32.099 60.558 1.00 43.71 N
ANISOU 1019 NZ LYS A 128 4492 5098 7019 1849 259 -219 N
ATOM 1020 N GLN A 129 17.015 -26.812 61.180 1.00 17.40 N
ANISOU 1020 N GLN A 129 1539 2487 2585 804 76 -327 N
ATOM 1021 CA GLN A 129 16.320 -26.918 62.463 1.00 20.06 C
ANISOU 1021 CA GLN A 129 1942 2779 2899 668 -152 -114 C
ATOM 1022 C GLN A 129 14.812 -26.906 62.269 1.00 17.79 C
ANISOU 1022 C GLN A 129 1956 2300 2502 623 -167 -170 C
ATOM 1023 O GLN A 129 14.080 -27.706 62.867 1.00 15.93 O
ANISOU 1023 O GLN A 129 1790 1898 2363 641 -329 -74 O
ATOM 1024 CB GLN A 129 16.697 -25.757 63.379 1.00 19.51 C
ANISOU 1024 CB GLN A 129 1847 2961 2606 353 -165 17 C
ATOM 1025 CG GLN A 129 18.090 -25.705 63.890 1.00 30.81 C
ANISOU 1025 CG GLN A 129 2946 4656 4106 276 -253 182 C
ATOM 1026 CD GLN A 129 18.252 -24.507 64.797 1.00 28.07 C
ANISOU 1026 CD GLN A 129 2698 4535 3433 -157 -251 280 C
ATOM 1027 OE1 GLN A 129 18.693 -23.446 64.362 1.00 26.38 O
ANISOU 1027 OE1 GLN A 129 2528 4481 3014 -317 -55 167 O
ATOM 1028 NE2 GLN A 129 17.868 -24.664 66.061 1.00 27.47 N
ANISOU 1028 NE2 GLN A 129 2714 4450 3275 -396 -441 475 N
ATOM 1029 N ALA A 130 14.330 -25.959 61.468 1.00 12.50 N
ANISOU 1029 N ALA A 130 1447 1669 1634 545 -8 -284 N
ATOM 1030 CA ALA A 130 12.896 -25.804 61.260 1.00 11.09 C
ANISOU 1030 CA ALA A 130 1473 1359 1382 498 -30 -263 C
ATOM 1031 C ALA A 130 12.340 -26.933 60.404 1.00 12.20 C
ANISOU 1031 C ALA A 130 1697 1333 1606 619 -107 -359 C
ATOM 1032 O ALA A 130 11.237 -27.432 60.667 1.00 13.22 O
ANISOU 1032 O ALA A 130 1915 1337 1770 587 -236 -279 O
ATOM 1033 CB ALA A 130 12.609 -24.450 60.614 1.00 13.35 C
ANISOU 1033 CB ALA A 130 1872 1729 1471 398 145 -286 C
ATOM 1034 N GLN A 131 13.082 -27.340 59.371 1.00 13.41 N
ANISOU 1034 N GLN A 131 1845 1477 1772 717 5 -545 N
ATOM 1035 CA GLN A 131 12.655 -28.481 58.564 1.00 14.93 C
ANISOU 1035 CA GLN A 131 2193 1476 2005 766 -11 -681 C
ATOM 1036 C GLN A 131 12.528 -29.732 59.419 1.00 16.10 C
ANISOU 1036 C GLN A 131 2303 1436 2378 841 -142 -580 C
ATOM 1037 O GLN A 131 11.573 -30.507 59.267 1.00 19.02 O
ANISOU 1037 O GLN A 131 2838 1656 2731 770 -237 -582 O
ATOM 1038 CB GLN A 131 13.640 -28.730 57.421 1.00 21.97 C
ANISOU 1038 CB GLN A 131 3092 2369 2888 774 236 -869 C
ATOM 1039 CG GLN A 131 13.598 -27.717 56.298 1.00 24.99 C
ANISOU 1039 CG GLN A 131 3594 2901 3001 592 361 -950 C
ATOM 1040 CD GLN A 131 14.661 -27.981 55.241 1.00 31.57 C
ANISOU 1040 CD GLN A 131 4511 3706 3779 620 604 -1080 C
ATOM 1041 OE1 GLN A 131 15.675 -28.622 55.516 1.00 32.24 O
ANISOU 1041 OE1 GLN A 131 4442 3738 4071 824 712 -1111 O
ATOM 1042 NE2 GLN A 131 14.433 -27.483 54.026 1.00 29.40 N
ANISOU 1042 NE2 GLN A 131 4362 3572 3237 508 554 -1169 N
ATOM 1043 N ASP A 132 13.488 -29.949 60.324 1.00 16.59 N
ANISOU 1043 N ASP A 132 2148 1526 2631 953 -163 -462 N
ATOM 1044 CA ASP A 132 13.444 -31.129 61.179 1.00 22.26 C
ANISOU 1044 CA ASP A 132 2837 2090 3530 997 -278 -307 C
ATOM 1045 C ASP A 132 12.232 -31.094 62.102 1.00 18.60 C
ANISOU 1045 C ASP A 132 2472 1624 2972 819 -471 -165 C
ATOM 1046 O ASP A 132 11.568 -32.119 62.299 1.00 21.15 O
ANISOU 1046 O ASP A 132 2905 1800 3331 778 -537 -136 O
ATOM 1047 CB ASP A 132 14.739 -31.249 61.983 1.00 25.27 C
ANISOU 1047 CB ASP A 132 2939 2562 4101 1127 -301 -137 C
ATOM 1048 CG ASP A 132 15.927 -31.671 61.125 1.00 30.74 C
ANISOU 1048 CG ASP A 132 3510 3220 4948 1346 -62 -238 C
ATOM 1049 OD1 ASP A 132 15.721 -32.120 59.973 1.00 31.99 O
ANISOU 1049 OD1 ASP A 132 3876 3209 5069 1380 146 -451 O
ATOM 1050 OD2 ASP A 132 17.075 -31.564 61.610 1.00 37.18 O
ANISOU 1050 OD2 ASP A 132 4031 4199 5895 1458 -83 -99 O
ATOM 1051 N LEU A 133 11.920 -29.922 62.665 1.00 16.95 N
ANISOU 1051 N LEU A 133 2238 1562 2639 703 -520 -87 N
ATOM 1052 CA LEU A 133 10.749 -29.806 63.531 1.00 14.43 C
ANISOU 1052 CA LEU A 133 2007 1237 2238 515 -604 34 C
ATOM 1053 C LEU A 133 9.467 -30.057 62.744 1.00 16.78 C
ANISOU 1053 C LEU A 133 2437 1470 2468 458 -607 -29 C
ATOM 1054 O LEU A 133 8.582 -30.798 63.198 1.00 15.17 O
ANISOU 1054 O LEU A 133 2284 1203 2276 359 -690 24 O
ATOM 1055 CB LEU A 133 10.711 -28.427 64.193 1.00 13.60 C
ANISOU 1055 CB LEU A 133 1897 1245 2026 401 -570 123 C
ATOM 1056 CG LEU A 133 9.542 -28.220 65.156 1.00 15.96 C
ANISOU 1056 CG LEU A 133 2291 1504 2269 204 -566 237 C
ATOM 1057 CD1 LEU A 133 9.652 -29.204 66.324 1.00 19.89 C
ANISOU 1057 CD1 LEU A 133 2776 1971 2812 96 -704 330 C
ATOM 1058 CD2 LEU A 133 9.468 -26.776 65.647 1.00 18.59 C
ANISOU 1058 CD2 LEU A 133 2674 1931 2460 40 -356 271 C
ATOM 1059 N ALA A 134 9.361 -29.468 61.550 1.00 13.83 N
ANISOU 1059 N ALA A 134 2127 1113 2014 510 -552 -133 N
ATOM 1060 CA ALA A 134 8.201 -29.725 60.703 1.00 13.06 C
ANISOU 1060 CA ALA A 134 2166 956 1840 429 -635 -147 C
ATOM 1061 C ALA A 134 8.084 -31.205 60.353 1.00 14.18 C
ANISOU 1061 C ALA A 134 2460 900 2028 419 -717 -258 C
ATOM 1062 O ALA A 134 6.980 -31.758 60.334 1.00 16.23 O
ANISOU 1062 O ALA A 134 2824 1088 2254 271 -858 -199 O
ATOM 1063 CB ALA A 134 8.274 -28.877 59.434 1.00 13.56 C
ANISOU 1063 CB ALA A 134 2258 1162 1732 392 -532 -217 C
ATOM 1064 N ARG A 135 9.213 -31.869 60.064 1.00 15.75 N
ANISOU 1064 N ARG A 135 2651 1026 2309 545 -583 -394 N
ATOM 1065 CA ARG A 135 9.165 -33.297 59.770 1.00 18.83 C
ANISOU 1065 CA ARG A 135 3189 1202 2762 533 -552 -484 C
ATOM 1066 C ARG A 135 8.696 -34.087 60.985 1.00 18.24 C
ANISOU 1066 C ARG A 135 3077 1069 2786 495 -683 -314 C
ATOM 1067 O ARG A 135 7.954 -35.067 60.846 1.00 20.33 O
ANISOU 1067 O ARG A 135 3516 1187 3023 383 -741 -340 O
ATOM 1068 CB ARG A 135 10.537 -33.783 59.292 1.00 22.16 C
ANISOU 1068 CB ARG A 135 3569 1514 3336 712 -298 -623 C
ATOM 1069 CG ARG A 135 10.534 -35.194 58.731 1.00 30.00 C
ANISOU 1069 CG ARG A 135 4766 2215 4417 695 -144 -771 C
ATOM 1070 CD ARG A 135 11.889 -35.567 58.121 1.00 45.35 C
ANISOU 1070 CD ARG A 135 6653 4008 6569 883 204 -917 C
ATOM 1071 NE ARG A 135 11.910 -36.945 57.629 1.00 59.08 N
ANISOU 1071 NE ARG A 135 8500 5455 8494 856 325 -1120 N
ATOM 1072 CZ ARG A 135 11.729 -37.295 56.358 1.00 63.60 C
ANISOU 1072 CZ ARG A 135 9321 5973 8871 766 322 -1446 C
ATOM 1073 NH1 ARG A 135 11.515 -36.370 55.431 1.00 63.63 N
ANISOU 1073 NH1 ARG A 135 9406 6220 8549 591 360 -1533 N
ATOM 1074 NH2 ARG A 135 11.766 -38.575 56.011 1.00 65.77 N
ANISOU 1074 NH2 ARG A 135 9843 5962 9183 781 417 -1573 N
ATOM 1075 N SER A 136 9.094 -33.658 62.188 1.00 16.97 N
ANISOU 1075 N SER A 136 2721 1035 2691 528 -724 -153 N
ATOM 1076 CA SER A 136 8.658 -34.356 63.394 1.00 19.60 C
ANISOU 1076 CA SER A 136 3044 1339 3063 442 -837 -14 C
ATOM 1077 C SER A 136 7.148 -34.252 63.565 1.00 17.13 C
ANISOU 1077 C SER A 136 2805 1077 2625 240 -950 25 C
ATOM 1078 O SER A 136 6.480 -35.242 63.894 1.00 21.35 O
ANISOU 1078 O SER A 136 3442 1509 3161 151 -1037 55 O
ATOM 1079 CB SER A 136 9.376 -33.795 64.618 1.00 25.35 C
ANISOU 1079 CB SER A 136 3605 2202 3823 435 -859 128 C
ATOM 1080 OG SER A 136 8.914 -34.435 65.795 1.00 31.51 O
ANISOU 1080 OG SER A 136 4413 2948 4611 312 -977 243 O
ATOM 1081 N TYR A 137 6.593 -33.062 63.330 1.00 16.17 N
ANISOU 1081 N TYR A 137 2624 1102 2417 173 -932 48 N
ATOM 1082 CA TYR A 137 5.152 -32.855 63.385 1.00 14.33 C
ANISOU 1082 CA TYR A 137 2400 915 2129 7 -1012 132 C
ATOM 1083 C TYR A 137 4.427 -33.404 62.163 1.00 18.87 C
ANISOU 1083 C TYR A 137 3156 1376 2636 -88 -1154 101 C
ATOM 1084 O TYR A 137 3.199 -33.549 62.201 1.00 19.86 O
ANISOU 1084 O TYR A 137 3285 1528 2733 -276 -1278 222 O
ATOM 1085 CB TYR A 137 4.833 -31.360 63.497 1.00 13.64 C
ANISOU 1085 CB TYR A 137 2168 983 2030 -6 -880 211 C
ATOM 1086 CG TYR A 137 5.302 -30.662 64.757 1.00 15.59 C
ANISOU 1086 CG TYR A 137 2331 1310 2284 -8 -733 253 C
ATOM 1087 CD1 TYR A 137 5.528 -31.355 65.942 1.00 17.79 C
ANISOU 1087 CD1 TYR A 137 2633 1554 2572 -76 -791 277 C
ATOM 1088 CD2 TYR A 137 5.495 -29.290 64.756 1.00 15.85 C
ANISOU 1088 CD2 TYR A 137 2307 1422 2293 28 -562 290 C
ATOM 1089 CE1 TYR A 137 5.944 -30.690 67.091 1.00 18.89 C
ANISOU 1089 CE1 TYR A 137 2760 1742 2675 -146 -717 336 C
ATOM 1090 CE2 TYR A 137 5.910 -28.621 65.892 1.00 18.23 C
ANISOU 1090 CE2 TYR A 137 2620 1740 2567 -32 -448 330 C
ATOM 1091 CZ TYR A 137 6.133 -29.320 67.052 1.00 19.88 C
ANISOU 1091 CZ TYR A 137 2867 1925 2761 -139 -540 353 C
ATOM 1092 OH TYR A 137 6.543 -28.630 68.172 1.00 20.38 O
ANISOU 1092 OH TYR A 137 2981 2020 2742 -273 -442 396 O
ATOM 1093 N GLY A 138 5.146 -33.683 61.079 1.00 15.25 N
ANISOU 1093 N GLY A 138 1803 1466 2526 70 -497 322 N
ATOM 1094 CA GLY A 138 4.497 -34.103 59.845 1.00 15.82 C
ANISOU 1094 CA GLY A 138 2181 1338 2491 62 -476 167 C
ATOM 1095 C GLY A 138 3.716 -33.009 59.144 1.00 13.98 C
ANISOU 1095 C GLY A 138 2058 1214 2041 -15 -530 52 C
ATOM 1096 O GLY A 138 2.613 -33.267 58.639 1.00 16.29 O
ANISOU 1096 O GLY A 138 2515 1473 2203 -129 -648 -1 O
ATOM 1097 N ILE A 139 4.260 -31.796 59.102 1.00 11.85 N
ANISOU 1097 N ILE A 139 1689 1076 1736 30 -455 41 N
ATOM 1098 CA ILE A 139 3.555 -30.649 58.529 1.00 10.74 C
ANISOU 1098 CA ILE A 139 1613 1039 1430 -28 -498 -28 C
ATOM 1099 C ILE A 139 4.506 -29.912 57.589 1.00 10.35 C
ANISOU 1099 C ILE A 139 1634 955 1342 59 -322 -99 C
ATOM 1100 O ILE A 139 5.733 -30.052 57.690 1.00 14.51 O
ANISOU 1100 O ILE A 139 2085 1442 1985 163 -175 -64 O
ATOM 1101 CB ILE A 139 3.035 -29.694 59.623 1.00 11.55 C
ANISOU 1101 CB ILE A 139 1517 1349 1523 -66 -452 38 C
ATOM 1102 CG1 ILE A 139 4.198 -29.047 60.373 1.00 11.88 C
ANISOU 1102 CG1 ILE A 139 1420 1480 1615 -38 -385 69 C
ATOM 1103 CG2 ILE A 139 2.111 -30.431 60.571 1.00 11.61 C
ANISOU 1103 CG2 ILE A 139 1479 1385 1547 -109 -439 91 C
ATOM 1104 CD1 ILE A 139 3.727 -28.010 61.395 1.00 13.18 C
ANISOU 1104 CD1 ILE A 139 1542 1749 1718 -71 -300 62 C
ATOM 1105 N PRO A 140 3.958 -29.132 56.658 1.00 11.28 N
ANISOU 1105 N PRO A 140 1877 1100 1307 14 -335 -163 N
ATOM 1106 CA PRO A 140 4.820 -28.358 55.757 1.00 10.62 C
ANISOU 1106 CA PRO A 140 1855 1005 1174 80 -177 -216 C
ATOM 1107 C PRO A 140 5.533 -27.236 56.483 1.00 13.08 C
ANISOU 1107 C PRO A 140 1959 1448 1561 118 -134 -153 C
ATOM 1108 O PRO A 140 5.034 -26.687 57.466 1.00 9.97 O
ANISOU 1108 O PRO A 140 1431 1169 1190 62 -233 -103 O
ATOM 1109 CB PRO A 140 3.839 -27.783 54.727 1.00 9.55 C
ANISOU 1109 CB PRO A 140 1814 924 889 -14 -233 -219 C
ATOM 1110 CG PRO A 140 2.660 -28.685 54.779 1.00 12.89 C
ANISOU 1110 CG PRO A 140 2257 1338 1301 -104 -348 -170 C
ATOM 1111 CD PRO A 140 2.555 -29.093 56.223 1.00 11.95 C
ANISOU 1111 CD PRO A 140 1993 1248 1301 -87 -426 -119 C
ATOM 1112 N PHE A 141 6.715 -26.893 55.964 1.00 9.47 N
ANISOU 1112 N PHE A 141 1496 971 1130 197 30 -155 N
ATOM 1113 CA PHE A 141 7.493 -25.739 56.403 1.00 9.68 C
ANISOU 1113 CA PHE A 141 1366 1115 1196 195 72 -94 C
ATOM 1114 C PHE A 141 7.676 -24.784 55.232 1.00 7.53 C
ANISOU 1114 C PHE A 141 1203 842 817 205 157 -140 C
ATOM 1115 O PHE A 141 8.040 -25.218 54.128 1.00 10.18 O
ANISOU 1115 O PHE A 141 1683 1092 1094 261 277 -192 O
ATOM 1116 CB PHE A 141 8.856 -26.191 56.944 1.00 8.66 C
ANISOU 1116 CB PHE A 141 1068 1001 1222 259 171 19 C
ATOM 1117 CG PHE A 141 9.802 -25.063 57.235 1.00 11.40 C
ANISOU 1117 CG PHE A 141 1273 1470 1588 219 212 102 C
ATOM 1118 CD1 PHE A 141 9.428 -24.023 58.083 1.00 8.11 C
ANISOU 1118 CD1 PHE A 141 799 1162 1119 85 101 104 C
ATOM 1119 CD2 PHE A 141 11.065 -25.037 56.671 1.00 14.94 C
ANISOU 1119 CD2 PHE A 141 1658 1915 2103 305 375 184 C
ATOM 1120 CE1 PHE A 141 10.311 -22.974 58.350 1.00 10.80 C
ANISOU 1120 CE1 PHE A 141 1049 1596 1458 4 130 174 C
ATOM 1121 CE2 PHE A 141 11.943 -24.005 56.934 1.00 13.65 C
ANISOU 1121 CE2 PHE A 141 1359 1876 1952 235 389 287 C
ATOM 1122 CZ PHE A 141 11.562 -22.970 57.785 1.00 12.79 C
ANISOU 1122 CZ PHE A 141 1220 1865 1773 66 252 276 C
ATOM 1123 N ILE A 142 7.408 -23.498 55.465 1.00 10.06 N
ANISOU 1123 N ILE A 142 1471 1245 1105 144 110 -123 N
ATOM 1124 CA ILE A 142 7.567 -22.451 54.457 1.00 7.93 C
ANISOU 1124 CA ILE A 142 1277 982 754 142 175 -133 C
ATOM 1125 C ILE A 142 8.382 -21.317 55.064 1.00 10.64 C
ANISOU 1125 C ILE A 142 1496 1394 1151 102 208 -76 C
ATOM 1126 O ILE A 142 8.062 -20.837 56.157 1.00 12.04 O
ANISOU 1126 O ILE A 142 1601 1609 1365 31 139 -66 O
ATOM 1127 CB ILE A 142 6.210 -21.899 53.963 1.00 11.23 C
ANISOU 1127 CB ILE A 142 1795 1395 1076 93 74 -145 C
ATOM 1128 CG1 ILE A 142 5.221 -23.022 53.616 1.00 20.32 C
ANISOU 1128 CG1 ILE A 142 3063 2496 2162 68 10 -178 C
ATOM 1129 CG2 ILE A 142 6.424 -20.950 52.762 1.00 13.64 C
ANISOU 1129 CG2 ILE A 142 2167 1712 1304 82 133 -120 C
ATOM 1130 CD1 ILE A 142 5.445 -23.630 52.285 1.00 33.68 C
ANISOU 1130 CD1 ILE A 142 4720 4219 3856 3 -131 -123 C
ATOM 1131 N GLU A 143 9.418 -20.880 54.351 1.00 9.73 N
ANISOU 1131 N GLU A 143 1374 1295 1029 127 322 -38 N
ATOM 1132 CA GLU A 143 10.172 -19.687 54.726 1.00 8.94 C
ANISOU 1132 CA GLU A 143 1185 1255 957 51 343 28 C
ATOM 1133 C GLU A 143 9.601 -18.479 53.997 1.00 10.34 C
ANISOU 1133 C GLU A 143 1464 1398 1065 21 339 9 C
ATOM 1134 O GLU A 143 9.458 -18.500 52.769 1.00 11.90 O
ANISOU 1134 O GLU A 143 1760 1578 1184 66 382 3 O
ATOM 1135 CB GLU A 143 11.656 -19.855 54.398 1.00 12.67 C
ANISOU 1135 CB GLU A 143 1553 1781 1480 89 466 130 C
ATOM 1136 CG GLU A 143 12.351 -20.818 55.335 1.00 16.53 C
ANISOU 1136 CG GLU A 143 1874 2318 2088 102 464 224 C
ATOM 1137 CD GLU A 143 13.851 -20.882 55.136 1.00 30.61 C
ANISOU 1137 CD GLU A 143 3514 4160 3958 133 554 373 C
ATOM 1138 OE1 GLU A 143 14.366 -20.270 54.176 1.00 38.00 O
ANISOU 1138 OE1 GLU A 143 4495 5093 4850 158 633 377 O
ATOM 1139 OE2 GLU A 143 14.514 -21.549 55.955 1.00 30.33 O
ANISOU 1139 OE2 GLU A 143 3336 4162 4027 122 503 483 O
ATOM 1140 N THR A 144 9.275 -17.426 54.750 1.00 8.12 N
ANISOU 1140 N THR A 144 1172 1101 811 -64 298 8 N
ATOM 1141 CA THR A 144 8.577 -16.273 54.196 1.00 8.46 C
ANISOU 1141 CA THR A 144 1299 1078 838 -72 303 16 C
ATOM 1142 C THR A 144 9.298 -14.981 54.552 1.00 8.09 C
ANISOU 1142 C THR A 144 1247 1005 820 -175 348 48 C
ATOM 1143 O THR A 144 10.080 -14.922 55.502 1.00 9.09 O
ANISOU 1143 O THR A 144 1317 1174 962 -281 343 51 O
ATOM 1144 CB THR A 144 7.136 -16.157 54.713 1.00 8.30 C
ANISOU 1144 CB THR A 144 1308 999 847 -51 247 -14 C
ATOM 1145 OG1 THR A 144 7.152 -15.951 56.136 1.00 9.99 O
ANISOU 1145 OG1 THR A 144 1492 1202 1101 -124 249 -64 O
ATOM 1146 CG2 THR A 144 6.333 -17.412 54.386 1.00 8.98 C
ANISOU 1146 CG2 THR A 144 1405 1114 894 9 170 -26 C
ATOM 1147 N SER A 145 8.999 -13.930 53.794 1.00 9.09 N
ANISOU 1147 N SER A 145 1441 1062 952 -169 380 90 N
ATOM 1148 CA SER A 145 9.306 -12.564 54.212 1.00 8.89 C
ANISOU 1148 CA SER A 145 1461 947 971 -273 426 103 C
ATOM 1149 C SER A 145 8.076 -11.715 53.957 1.00 10.86 C
ANISOU 1149 C SER A 145 1784 1054 1289 -208 455 123 C
ATOM 1150 O SER A 145 7.733 -11.453 52.801 1.00 11.23 O
ANISOU 1150 O SER A 145 1834 1098 1335 -145 449 220 O
ATOM 1151 CB SER A 145 10.501 -11.985 53.466 1.00 9.96 C
ANISOU 1151 CB SER A 145 1574 1128 1081 -339 460 195 C
ATOM 1152 OG SER A 145 10.594 -10.588 53.735 1.00 13.44 O
ANISOU 1152 OG SER A 145 2097 1442 1568 -449 498 211 O
ATOM 1153 N ALA A 146 7.413 -11.279 55.025 1.00 10.34 N
ANISOU 1153 N ALA A 146 1772 874 1284 -226 501 53 N
ATOM 1154 CA ALA A 146 6.348 -10.305 54.829 1.00 11.73 C
ANISOU 1154 CA ALA A 146 2000 881 1574 -141 581 107 C
ATOM 1155 C ALA A 146 6.881 -9.007 54.231 1.00 13.59 C
ANISOU 1155 C ALA A 146 2290 1018 1857 -187 634 174 C
ATOM 1156 O ALA A 146 6.139 -8.297 53.548 1.00 16.47 O
ANISOU 1156 O ALA A 146 2633 1308 2317 -90 655 282 O
ATOM 1157 CB ALA A 146 5.615 -10.038 56.147 1.00 11.61 C
ANISOU 1157 CB ALA A 146 2040 761 1611 -136 669 2 C
ATOM 1158 N LYS A 147 8.168 -8.689 54.444 1.00 11.74 N
ANISOU 1158 N LYS A 147 2082 823 1555 -336 619 134 N
ATOM 1159 CA LYS A 147 8.706 -7.431 53.941 1.00 13.93 C
ANISOU 1159 CA LYS A 147 2397 1025 1872 -390 638 196 C
ATOM 1160 C LYS A 147 8.806 -7.449 52.422 1.00 15.22 C
ANISOU 1160 C LYS A 147 2492 1259 2033 -332 601 361 C
ATOM 1161 O LYS A 147 8.359 -6.510 51.753 1.00 16.86 O
ANISOU 1161 O LYS A 147 2706 1374 2326 -284 616 462 O
ATOM 1162 CB LYS A 147 10.070 -7.146 54.566 1.00 15.63 C
ANISOU 1162 CB LYS A 147 2630 1300 2007 -579 600 148 C
ATOM 1163 CG LYS A 147 10.688 -5.826 54.103 1.00 15.49 C
ANISOU 1163 CG LYS A 147 2657 1198 2029 -659 609 220 C
ATOM 1164 CD LYS A 147 11.940 -5.484 54.890 1.00 20.14 C
ANISOU 1164 CD LYS A 147 3269 1844 2540 -859 556 184 C
ATOM 1165 CE LYS A 147 12.540 -4.169 54.412 1.00 28.56 C
ANISOU 1165 CE LYS A 147 4391 2805 3654 -948 565 258 C
ATOM 1166 NZ LYS A 147 13.801 -3.851 55.132 1.00 39.62 N
ANISOU 1166 NZ LYS A 147 5800 4287 4967 -1157 494 254 N
ATOM 1167 N THR A 148 9.367 -8.528 51.860 1.00 14.46 N
ANISOU 1167 N THR A 148 2329 1341 1825 -333 556 391 N
ATOM 1168 CA THR A 148 9.553 -8.651 50.416 1.00 16.86 C
ANISOU 1168 CA THR A 148 2588 1754 2063 -295 530 521 C
ATOM 1169 C THR A 148 8.404 -9.376 49.729 1.00 14.42 C
ANISOU 1169 C THR A 148 2269 1494 1717 -184 485 569 C
ATOM 1170 O THR A 148 8.344 -9.377 48.495 1.00 18.51 O
ANISOU 1170 O THR A 148 2774 2103 2157 -182 446 677 O
ATOM 1171 CB THR A 148 10.856 -9.394 50.101 1.00 15.75 C
ANISOU 1171 CB THR A 148 2381 1796 1809 -342 530 518 C
ATOM 1172 OG1 THR A 148 10.715 -10.765 50.487 1.00 15.93 O
ANISOU 1172 OG1 THR A 148 2377 1902 1774 -280 520 425 O
ATOM 1173 CG2 THR A 148 12.031 -8.786 50.852 1.00 20.53 C
ANISOU 1173 CG2 THR A 148 2949 2401 2449 -474 528 513 C
ATOM 1174 N ARG A 149 7.507 -9.986 50.495 1.00 13.99 N
ANISOU 1174 N ARG A 149 2207 1409 1700 -120 460 490 N
ATOM 1175 CA ARG A 149 6.320 -10.758 50.102 1.00 15.68 C
ANISOU 1175 CA ARG A 149 2394 1680 1885 -43 380 535 C
ATOM 1176 C ARG A 149 6.678 -12.184 49.673 1.00 17.28 C
ANISOU 1176 C ARG A 149 2606 2039 1919 -53 325 456 C
ATOM 1177 O ARG A 149 5.766 -12.964 49.331 1.00 18.23 O
ANISOU 1177 O ARG A 149 2734 2214 1979 -35 240 479 O
ATOM 1178 CB ARG A 149 5.483 -10.067 49.010 1.00 17.69 C
ANISOU 1178 CB ARG A 149 2620 1926 2174 -25 333 739 C
ATOM 1179 CG ARG A 149 3.989 -10.140 49.287 1.00 24.96 C
ANISOU 1179 CG ARG A 149 3468 2821 3194 49 271 805 C
ATOM 1180 CD ARG A 149 3.172 -9.339 48.273 1.00 27.70 C
ANISOU 1180 CD ARG A 149 3745 3184 3595 53 206 980 C
ATOM 1181 NE ARG A 149 3.416 -7.899 48.349 1.00 34.22 N
ANISOU 1181 NE ARG A 149 4563 3866 4573 81 299 1028 N
ATOM 1182 CZ ARG A 149 4.102 -7.199 47.451 1.00 38.30 C
ANISOU 1182 CZ ARG A 149 5107 4394 5050 16 293 1099 C
ATOM 1183 NH1 ARG A 149 4.257 -5.891 47.612 1.00 37.29 N
ANISOU 1183 NH1 ARG A 149 4981 4115 5071 38 375 1140 N
ATOM 1184 NH2 ARG A 149 4.628 -7.799 46.390 1.00 40.55 N
ANISOU 1184 NH2 ARG A 149 5431 4837 5140 -74 221 1119 N
ATOM 1185 N GLN A 150 7.951 -12.574 49.730 1.00 10.72 N
ANISOU 1185 N GLN A 150 1777 1271 1025 -86 379 378 N
ATOM 1186 CA GLN A 150 8.350 -13.932 49.375 1.00 10.72 C
ANISOU 1186 CA GLN A 150 1800 1371 902 -65 384 301 C
ATOM 1187 C GLN A 150 7.601 -14.958 50.214 1.00 10.97 C
ANISOU 1187 C GLN A 150 1823 1388 957 -26 320 212 C
ATOM 1188 O GLN A 150 7.624 -14.898 51.445 1.00 12.01 O
ANISOU 1188 O GLN A 150 1898 1479 1187 -26 319 159 O
ATOM 1189 CB GLN A 150 9.858 -14.102 49.583 1.00 13.32 C
ANISOU 1189 CB GLN A 150 2076 1754 1232 -76 482 276 C
ATOM 1190 CG GLN A 150 10.706 -13.359 48.596 1.00 18.52 C
ANISOU 1190 CG GLN A 150 2718 2466 1853 -115 532 364 C
ATOM 1191 CD GLN A 150 10.808 -14.096 47.287 1.00 25.42 C
ANISOU 1191 CD GLN A 150 3641 3424 2595 -91 552 345 C
ATOM 1192 OE1 GLN A 150 11.439 -15.153 47.206 1.00 22.81 O
ANISOU 1192 OE1 GLN A 150 3297 3127 2242 -41 615 269 O
ATOM 1193 NE2 GLN A 150 10.179 -13.553 46.256 1.00 25.16 N
ANISOU 1193 NE2 GLN A 150 3665 3416 2480 -136 504 424 N
ATOM 1194 N GLY A 151 6.915 -15.887 49.544 1.00 10.21 N
ANISOU 1194 N GLY A 151 1799 1331 751 -24 259 200 N
ATOM 1195 CA GLY A 151 6.313 -17.016 50.215 1.00 8.78 C
ANISOU 1195 CA GLY A 151 1619 1141 575 -3 194 123 C
ATOM 1196 C GLY A 151 5.026 -16.739 50.955 1.00 10.71 C
ANISOU 1196 C GLY A 151 1801 1353 915 6 100 174 C
ATOM 1197 O GLY A 151 4.460 -17.672 51.533 1.00 9.82 O
ANISOU 1197 O GLY A 151 1678 1247 807 12 34 130 O
ATOM 1198 N VAL A 152 4.525 -15.505 50.938 1.00 12.78 N
ANISOU 1198 N VAL A 152 1652 1614 1589 -400 734 81 N
ATOM 1199 CA VAL A 152 3.354 -15.178 51.756 1.00 11.52 C
ANISOU 1199 CA VAL A 152 1635 1259 1482 -263 695 69 C
ATOM 1200 C VAL A 152 2.127 -15.943 51.271 1.00 12.13 C
ANISOU 1200 C VAL A 152 1718 1415 1477 -44 629 203 C
ATOM 1201 O VAL A 152 1.476 -16.660 52.044 1.00 11.09 O
ANISOU 1201 O VAL A 152 1559 1337 1316 74 550 130 O
ATOM 1202 CB VAL A 152 3.101 -13.662 51.761 1.00 13.96 C
ANISOU 1202 CB VAL A 152 2132 1220 1952 -338 821 137 C
ATOM 1203 CG1 VAL A 152 1.788 -13.354 52.473 1.00 16.79 C
ANISOU 1203 CG1 VAL A 152 2606 1381 2394 -122 842 127 C
ATOM 1204 CG2 VAL A 152 4.252 -12.933 52.441 1.00 16.03 C
ANISOU 1204 CG2 VAL A 152 2407 1390 2292 -630 866 -60 C
ATOM 1205 N ASP A 153 1.787 -15.797 49.988 1.00 13.64 N
ANISOU 1205 N ASP A 153 1940 1641 1601 -28 651 416 N
ATOM 1206 CA ASP A 153 0.642 -16.536 49.464 1.00 13.38 C
ANISOU 1206 CA ASP A 153 1873 1737 1474 106 511 500 C
ATOM 1207 C ASP A 153 0.871 -18.039 49.566 1.00 11.81 C
ANISOU 1207 C ASP A 153 1592 1717 1180 99 418 320 C
ATOM 1208 O ASP A 153 -0.056 -18.795 49.879 1.00 13.20 O
ANISOU 1208 O ASP A 153 1740 1923 1353 178 320 304 O
ATOM 1209 CB ASP A 153 0.355 -16.140 48.015 1.00 20.10 C
ANISOU 1209 CB ASP A 153 2759 2650 2229 49 454 675 C
ATOM 1210 CG ASP A 153 0.019 -14.667 47.859 1.00 32.98 C
ANISOU 1210 CG ASP A 153 4471 4057 4002 87 500 882 C
ATOM 1211 OD1 ASP A 153 -0.370 -14.021 48.856 1.00 33.32 O
ANISOU 1211 OD1 ASP A 153 4545 3868 4248 200 578 865 O
ATOM 1212 OD2 ASP A 153 0.147 -14.153 46.728 1.00 38.15 O
ANISOU 1212 OD2 ASP A 153 5189 4744 4561 1 473 1045 O
ATOM 1213 N ASP A 154 2.102 -18.491 49.306 1.00 11.79 N
ANISOU 1213 N ASP A 154 1537 1801 1140 4 465 190 N
ATOM 1214 CA ASP A 154 2.389 -19.922 49.346 1.00 10.57 C
ANISOU 1214 CA ASP A 154 1344 1692 981 40 415 42 C
ATOM 1215 C ASP A 154 2.123 -20.499 50.730 1.00 11.44 C
ANISOU 1215 C ASP A 154 1415 1757 1173 125 324 -9 C
ATOM 1216 O ASP A 154 1.605 -21.614 50.854 1.00 11.10 O
ANISOU 1216 O ASP A 154 1385 1710 1124 174 250 -28 O
ATOM 1217 CB ASP A 154 3.835 -20.168 48.919 1.00 12.29 C
ANISOU 1217 CB ASP A 154 1493 1949 1228 24 533 -31 C
ATOM 1218 CG ASP A 154 4.131 -21.638 48.636 1.00 15.99 C
ANISOU 1218 CG ASP A 154 1946 2429 1702 103 528 -138 C
ATOM 1219 OD1 ASP A 154 3.469 -22.248 47.756 1.00 13.84 O
ANISOU 1219 OD1 ASP A 154 1785 2163 1312 95 528 -155 O
ATOM 1220 OD2 ASP A 154 5.057 -22.176 49.270 1.00 15.01 O
ANISOU 1220 OD2 ASP A 154 1694 2318 1692 173 532 -201 O
ATOM 1221 N ALA A 155 2.443 -19.743 51.783 1.00 9.09 N
ANISOU 1221 N ALA A 155 1093 1440 922 120 350 -29 N
ATOM 1222 CA ALA A 155 2.197 -20.225 53.140 1.00 8.35 C
ANISOU 1222 CA ALA A 155 992 1344 838 174 265 -70 C
ATOM 1223 C ALA A 155 0.711 -20.426 53.395 1.00 9.04 C
ANISOU 1223 C ALA A 155 1144 1372 919 221 216 4 C
ATOM 1224 O ALA A 155 0.290 -21.482 53.879 1.00 10.47 O
ANISOU 1224 O ALA A 155 1319 1575 1085 256 145 20 O
ATOM 1225 CB ALA A 155 2.774 -19.237 54.150 1.00 8.30 C
ANISOU 1225 CB ALA A 155 979 1342 833 90 291 -158 C
ATOM 1226 N PHE A 156 -0.099 -19.408 53.093 1.00 7.71 N
ANISOU 1226 N PHE A 156 1017 1142 770 252 285 79 N
ATOM 1227 CA PHE A 156 -1.533 -19.514 53.332 1.00 6.97 C
ANISOU 1227 CA PHE A 156 913 1045 690 333 270 168 C
ATOM 1228 C PHE A 156 -2.166 -20.580 52.439 1.00 10.39 C
ANISOU 1228 C PHE A 156 1286 1581 1081 329 183 230 C
ATOM 1229 O PHE A 156 -3.002 -21.366 52.908 1.00 9.81 O
ANISOU 1229 O PHE A 156 1166 1557 1006 328 148 244 O
ATOM 1230 CB PHE A 156 -2.204 -18.158 53.108 1.00 9.97 C
ANISOU 1230 CB PHE A 156 1317 1320 1152 442 406 279 C
ATOM 1231 CG PHE A 156 -2.013 -17.192 54.233 1.00 9.45 C
ANISOU 1231 CG PHE A 156 1333 1096 1160 428 513 142 C
ATOM 1232 CD1 PHE A 156 -2.835 -17.241 55.354 1.00 10.09 C
ANISOU 1232 CD1 PHE A 156 1398 1194 1241 445 528 72 C
ATOM 1233 CD2 PHE A 156 -1.022 -16.217 54.175 1.00 10.75 C
ANISOU 1233 CD2 PHE A 156 1606 1097 1382 365 630 57 C
ATOM 1234 CE1 PHE A 156 -2.675 -16.325 56.393 1.00 10.31 C
ANISOU 1234 CE1 PHE A 156 1519 1108 1292 420 640 -98 C
ATOM 1235 CE2 PHE A 156 -0.870 -15.292 55.213 1.00 11.75 C
ANISOU 1235 CE2 PHE A 156 1847 1056 1562 303 728 -121 C
ATOM 1236 CZ PHE A 156 -1.697 -15.359 56.327 1.00 11.43 C
ANISOU 1236 CZ PHE A 156 1788 1071 1482 342 723 -202 C
ATOM 1237 N TYR A 157 -1.781 -20.628 51.153 1.00 9.76 N
ANISOU 1237 N TYR A 157 1219 1541 949 270 165 242 N
ATOM 1238 CA TYR A 157 -2.354 -21.622 50.243 1.00 9.93 C
ANISOU 1238 CA TYR A 157 1237 1646 889 191 86 242 C
ATOM 1239 C TYR A 157 -1.955 -23.034 50.660 1.00 10.47 C
ANISOU 1239 C TYR A 157 1350 1695 935 165 70 125 C
ATOM 1240 O TYR A 157 -2.753 -23.973 50.534 1.00 10.02 O
ANISOU 1240 O TYR A 157 1310 1679 817 102 8 129 O
ATOM 1241 CB TYR A 157 -1.913 -21.378 48.796 1.00 8.14 C
ANISOU 1241 CB TYR A 157 1072 1473 547 111 90 256 C
ATOM 1242 CG TYR A 157 -2.531 -20.228 48.055 1.00 17.05 C
ANISOU 1242 CG TYR A 157 2180 2639 1660 123 65 434 C
ATOM 1243 CD1 TYR A 157 -3.047 -19.128 48.721 1.00 16.31 C
ANISOU 1243 CD1 TYR A 157 2020 2471 1705 244 103 561 C
ATOM 1244 CD2 TYR A 157 -2.598 -20.257 46.662 1.00 21.14 C
ANISOU 1244 CD2 TYR A 157 2759 3256 2017 33 23 484 C
ATOM 1245 CE1 TYR A 157 -3.597 -18.048 47.993 1.00 23.19 C
ANISOU 1245 CE1 TYR A 157 2876 3335 2602 285 85 760 C
ATOM 1246 CE2 TYR A 157 -3.150 -19.207 45.938 1.00 27.41 C
ANISOU 1246 CE2 TYR A 157 3536 4088 2789 52 -22 692 C
ATOM 1247 CZ TYR A 157 -3.649 -18.109 46.611 1.00 33.15 C
ANISOU 1247 CZ TYR A 157 4185 4710 3701 185 1 841 C
ATOM 1248 OH TYR A 157 -4.199 -17.070 45.889 1.00 40.25 O
ANISOU 1248 OH TYR A 157 5071 5607 4614 234 -42 1076 O
ATOM 1249 N THR A 158 -0.721 -23.209 51.144 1.00 7.59 N
ANISOU 1249 N THR A 158 995 1275 613 213 116 39 N
ATOM 1250 CA THR A 158 -0.311 -24.525 51.625 1.00 7.85 C
ANISOU 1250 CA THR A 158 1067 1272 642 272 112 -40 C
ATOM 1251 C THR A 158 -1.201 -24.975 52.772 1.00 10.87 C
ANISOU 1251 C THR A 158 1459 1626 1047 270 49 52 C
ATOM 1252 O THR A 158 -1.592 -26.149 52.848 1.00 9.28 O
ANISOU 1252 O THR A 158 1320 1331 875 223 6 50 O
ATOM 1253 CB THR A 158 1.157 -24.505 52.053 1.00 8.87 C
ANISOU 1253 CB THR A 158 1130 1372 869 345 141 -97 C
ATOM 1254 OG1 THR A 158 1.983 -24.219 50.913 1.00 10.41 O
ANISOU 1254 OG1 THR A 158 1302 1587 1068 290 228 -169 O
ATOM 1255 CG2 THR A 158 1.565 -25.870 52.599 1.00 9.43 C
ANISOU 1255 CG2 THR A 158 1215 1338 1030 470 114 -127 C
ATOM 1256 N LEU A 159 -1.570 -24.047 53.658 1.00 8.33 N
ANISOU 1256 N LEU A 159 1079 1330 756 275 62 112 N
ATOM 1257 CA LEU A 159 -2.433 -24.421 54.775 1.00 9.38 C
ANISOU 1257 CA LEU A 159 1207 1467 890 240 53 182 C
ATOM 1258 C LEU A 159 -3.801 -24.877 54.282 1.00 9.50 C
ANISOU 1258 C LEU A 159 1186 1537 888 158 33 263 C
ATOM 1259 O LEU A 159 -4.352 -25.863 54.795 1.00 9.91 O
ANISOU 1259 O LEU A 159 1262 1588 917 79 8 349 O
ATOM 1260 CB LEU A 159 -2.558 -23.252 55.743 1.00 7.53 C
ANISOU 1260 CB LEU A 159 945 1256 661 266 109 166 C
ATOM 1261 CG LEU A 159 -3.409 -23.503 56.992 1.00 9.29 C
ANISOU 1261 CG LEU A 159 1170 1526 832 227 145 213 C
ATOM 1262 CD1 LEU A 159 -2.918 -24.734 57.751 1.00 9.98 C
ANISOU 1262 CD1 LEU A 159 1330 1600 862 174 74 271 C
ATOM 1263 CD2 LEU A 159 -3.374 -22.270 57.893 1.00 12.33 C
ANISOU 1263 CD2 LEU A 159 1588 1918 1178 235 231 132 C
ATOM 1264 N VAL A 160 -4.368 -24.172 53.293 1.00 9.79 N
ANISOU 1264 N VAL A 160 1146 1645 930 152 28 283 N
ATOM 1265 CA VAL A 160 -5.629 -24.612 52.698 1.00 10.25 C
ANISOU 1265 CA VAL A 160 1107 1837 952 39 -44 383 C
ATOM 1266 C VAL A 160 -5.488 -26.012 52.111 1.00 9.46 C
ANISOU 1266 C VAL A 160 1125 1684 785 -132 -134 308 C
ATOM 1267 O VAL A 160 -6.376 -26.860 52.280 1.00 10.94 O
ANISOU 1267 O VAL A 160 1279 1885 992 -304 -186 351 O
ATOM 1268 CB VAL A 160 -6.113 -23.602 51.645 1.00 10.50 C
ANISOU 1268 CB VAL A 160 1039 1958 994 69 -65 443 C
ATOM 1269 CG1 VAL A 160 -7.315 -24.158 50.881 1.00 11.73 C
ANISOU 1269 CG1 VAL A 160 1072 2289 1096 -96 -189 537 C
ATOM 1270 CG2 VAL A 160 -6.470 -22.281 52.323 1.00 14.23 C
ANISOU 1270 CG2 VAL A 160 1414 2432 1562 238 59 532 C
ATOM 1271 N ARG A 161 -4.375 -26.279 51.417 1.00 9.27 N
ANISOU 1271 N ARG A 161 1242 1557 723 -103 -120 155 N
ATOM 1272 CA ARG A 161 -4.160 -27.616 50.871 1.00 9.23 C
ANISOU 1272 CA ARG A 161 1395 1400 713 -233 -143 -2 C
ATOM 1273 C ARG A 161 -4.137 -28.654 51.982 1.00 11.65 C
ANISOU 1273 C ARG A 161 1777 1487 1164 -238 -131 42 C
ATOM 1274 O ARG A 161 -4.663 -29.760 51.817 1.00 13.48 O
ANISOU 1274 O ARG A 161 2112 1574 1435 -426 -167 -4 O
ATOM 1275 CB ARG A 161 -2.860 -27.668 50.065 1.00 10.51 C
ANISOU 1275 CB ARG A 161 1666 1487 839 -138 -54 -190 C
ATOM 1276 CG ARG A 161 -2.923 -26.831 48.805 1.00 10.24 C
ANISOU 1276 CG ARG A 161 1611 1677 601 -202 -61 -210 C
ATOM 1277 CD ARG A 161 -1.681 -26.938 47.919 1.00 12.75 C
ANISOU 1277 CD ARG A 161 2016 1956 872 -133 76 -393 C
ATOM 1278 NE ARG A 161 -1.899 -26.126 46.732 1.00 13.21 N
ANISOU 1278 NE ARG A 161 2043 2176 801 -188 46 -304 N
ATOM 1279 CZ ARG A 161 -1.365 -24.928 46.527 1.00 13.11 C
ANISOU 1279 CZ ARG A 161 1976 2203 803 -108 99 -179 C
ATOM 1280 NH1 ARG A 161 -0.516 -24.402 47.405 1.00 13.54 N
ANISOU 1280 NH1 ARG A 161 1977 2165 1003 0 183 -150 N
ATOM 1281 NH2 ARG A 161 -1.673 -24.266 45.428 1.00 13.52 N
ANISOU 1281 NH2 ARG A 161 2033 2383 721 -181 63 -89 N
ATOM 1282 N GLU A 162 -3.538 -28.310 53.123 1.00 10.31 N
ANISOU 1282 N GLU A 162 1573 1289 1055 -67 -92 142 N
ATOM 1283 CA GLU A 162 -3.527 -29.236 54.253 1.00 9.62 C
ANISOU 1283 CA GLU A 162 1562 1036 1058 -73 -103 265 C
ATOM 1284 C GLU A 162 -4.936 -29.498 54.774 1.00 11.21 C
ANISOU 1284 C GLU A 162 1707 1320 1234 -282 -113 412 C
ATOM 1285 O GLU A 162 -5.262 -30.629 55.142 1.00 12.63 O
ANISOU 1285 O GLU A 162 1997 1310 1491 -423 -126 493 O
ATOM 1286 CB GLU A 162 -2.624 -28.702 55.368 1.00 11.01 C
ANISOU 1286 CB GLU A 162 1697 1265 1220 110 -99 357 C
ATOM 1287 CG GLU A 162 -1.149 -28.753 55.019 1.00 13.37 C
ANISOU 1287 CG GLU A 162 1998 1479 1603 298 -99 254 C
ATOM 1288 CD GLU A 162 -0.647 -30.176 54.845 1.00 16.25 C
ANISOU 1288 CD GLU A 162 2489 1537 2149 368 -104 243 C
ATOM 1289 OE1 GLU A 162 -0.608 -30.931 55.844 1.00 19.23 O
ANISOU 1289 OE1 GLU A 162 2929 1779 2599 403 -166 444 O
ATOM 1290 OE2 GLU A 162 -0.303 -30.546 53.701 1.00 19.29 O
ANISOU 1290 OE2 GLU A 162 2932 1800 2599 390 -28 36 O
ATOM 1291 N ILE A 163 -5.794 -28.473 54.799 1.00 10.64 N
ANISOU 1291 N ILE A 163 1447 1512 1084 -301 -86 465 N
ATOM 1292 CA ILE A 163 -7.178 -28.693 55.213 1.00 11.40 C
ANISOU 1292 CA ILE A 163 1405 1747 1181 -492 -66 605 C
ATOM 1293 C ILE A 163 -7.906 -29.574 54.207 1.00 13.42 C
ANISOU 1293 C ILE A 163 1663 1967 1469 -768 -168 551 C
ATOM 1294 O ILE A 163 -8.666 -30.470 54.582 1.00 16.06 O
ANISOU 1294 O ILE A 163 1995 2251 1855 -1016 -171 644 O
ATOM 1295 CB ILE A 163 -7.910 -27.353 55.395 1.00 11.65 C
ANISOU 1295 CB ILE A 163 1193 2055 1179 -382 14 665 C
ATOM 1296 CG1 ILE A 163 -7.233 -26.518 56.484 1.00 11.86 C
ANISOU 1296 CG1 ILE A 163 1277 2052 1176 -163 120 606 C
ATOM 1297 CG2 ILE A 163 -9.388 -27.585 55.731 1.00 14.18 C
ANISOU 1297 CG2 ILE A 163 1300 2545 1544 -534 45 776 C
ATOM 1298 CD1 ILE A 163 -7.750 -25.088 56.530 1.00 14.90 C
ANISOU 1298 CD1 ILE A 163 1513 2553 1596 -3 205 574 C
ATOM 1299 N ARG A 164 -7.726 -29.301 52.912 1.00 13.25 N
ANISOU 1299 N ARG A 164 1648 1998 1387 -777 -254 402 N
ATOM 1300 CA ARG A 164 -8.393 -30.106 51.897 1.00 15.79 C
ANISOU 1300 CA ARG A 164 1999 2331 1670 -1095 -376 301 C
ATOM 1301 C ARG A 164 -7.982 -31.568 51.996 1.00 18.71 C
ANISOU 1301 C ARG A 164 2662 2305 2141 -1254 -353 176 C
ATOM 1302 O ARG A 164 -8.819 -32.466 51.853 1.00 21.59 O
ANISOU 1302 O ARG A 164 3052 2608 2544 -1581 -408 164 O
ATOM 1303 CB ARG A 164 -8.089 -29.549 50.506 1.00 15.69 C
ANISOU 1303 CB ARG A 164 2001 2467 1492 -1076 -463 157 C
ATOM 1304 CG ARG A 164 -8.788 -28.242 50.224 1.00 15.25 C
ANISOU 1304 CG ARG A 164 1651 2773 1372 -973 -527 345 C
ATOM 1305 CD ARG A 164 -8.341 -27.653 48.881 1.00 15.49 C
ANISOU 1305 CD ARG A 164 1757 2865 1263 -885 -541 263 C
ATOM 1306 NE ARG A 164 -9.164 -26.509 48.516 1.00 16.23 N
ANISOU 1306 NE ARG A 164 1619 3168 1380 -765 -561 471 N
ATOM 1307 CZ ARG A 164 -8.932 -25.718 47.472 1.00 17.60 C
ANISOU 1307 CZ ARG A 164 1808 3409 1470 -686 -578 495 C
ATOM 1308 NH1 ARG A 164 -7.889 -25.937 46.675 1.00 16.83 N
ANISOU 1308 NH1 ARG A 164 1925 3228 1241 -707 -552 318 N
ATOM 1309 NH2 ARG A 164 -9.752 -24.708 47.223 1.00 18.20 N
ANISOU 1309 NH2 ARG A 164 1686 3632 1596 -584 -610 708 N
ATOM 1310 N LYS A 165 -6.694 -31.826 52.244 1.00 16.69 N
ANISOU 1310 N LYS A 165 2614 1766 1963 -1006 -265 95 N
ATOM 1311 CA LYS A 165 -6.232 -33.202 52.391 1.00 20.81 C
ANISOU 1311 CA LYS A 165 3418 1837 2653 -1069 -220 12 C
ATOM 1312 C LYS A 165 -6.832 -33.853 53.631 1.00 22.01 C
ANISOU 1312 C LYS A 165 3582 1855 2924 -1202 -206 284 C
ATOM 1313 O LYS A 165 -7.171 -35.040 53.609 1.00 25.35 O
ANISOU 1313 O LYS A 165 4134 2019 3477 -1365 -186 248 O
ATOM 1314 CB LYS A 165 -4.705 -33.235 52.451 1.00 21.19 C
ANISOU 1314 CB LYS A 165 3589 1665 2797 -704 -131 -73 C
ATOM 1315 CG LYS A 165 -4.026 -32.856 51.149 1.00 26.56 C
ANISOU 1315 CG LYS A 165 4306 2418 3367 -619 -83 -366 C
ATOM 1316 CD LYS A 165 -2.520 -32.756 51.328 1.00 30.81 C
ANISOU 1316 CD LYS A 165 4860 2813 4032 -247 26 -408 C
ATOM 1317 CE LYS A 165 -1.831 -32.473 50.010 1.00 39.59 C
ANISOU 1317 CE LYS A 165 6009 4007 5028 -187 136 -706 C
ATOM 1318 NZ LYS A 165 -0.349 -32.493 50.149 1.00 47.91 N
ANISOU 1318 NZ LYS A 165 6992 4950 6261 164 259 -742 N
ATOM 1319 N HIS A 166 -6.976 -33.085 54.715 1.00 18.77 N
ANISOU 1319 N HIS A 166 2991 1690 2451 -1063 -175 527 N
ATOM 1320 CA HIS A 166 -7.558 -33.609 55.949 1.00 20.53 C
ANISOU 1320 CA HIS A 166 3186 1907 2709 -1139 -118 770 C
ATOM 1321 C HIS A 166 -9.040 -33.932 55.776 1.00 26.18 C
ANISOU 1321 C HIS A 166 3736 2795 3418 -1453 -120 782 C
ATOM 1322 O HIS A 166 -9.523 -34.957 56.277 1.00 28.90 O
ANISOU 1322 O HIS A 166 4152 2971 3858 -1609 -74 874 O
ATOM 1323 CB HIS A 166 -7.354 -32.598 57.079 1.00 22.52 C
ANISOU 1323 CB HIS A 166 3294 2441 2823 -910 -56 920 C
ATOM 1324 CG HIS A 166 -8.116 -32.916 58.327 1.00 28.96 C
ANISOU 1324 CG HIS A 166 4044 3372 3589 -981 40 1088 C
ATOM 1325 ND1 HIS A 166 -7.666 -33.824 59.261 1.00 33.01 N
ANISOU 1325 ND1 HIS A 166 4728 3685 4129 -936 70 1246 N
ATOM 1326 CD2 HIS A 166 -9.293 -32.441 58.800 1.00 29.72 C
ANISOU 1326 CD2 HIS A 166 3924 3761 3607 -1079 128 1129 C
ATOM 1327 CE1 HIS A 166 -8.539 -33.905 60.250 1.00 34.48 C
ANISOU 1327 CE1 HIS A 166 4838 4043 4221 -1051 171 1375 C
ATOM 1328 NE2 HIS A 166 -9.535 -33.075 59.996 1.00 35.09 N
ANISOU 1328 NE2 HIS A 166 4676 4412 4246 -1131 219 1291 N
ATOM 1329 N LYS A 167 -9.780 -33.072 55.068 1.00 26.32 N
ANISOU 1329 N LYS A 167 3507 3157 3337 -1529 -178 714 N
ATOM 1330 CA LYS A 167 -11.215 -33.286 54.928 1.00 32.04 C
ANISOU 1330 CA LYS A 167 4009 4104 4059 -1770 -203 750 C
ATOM 1331 C LYS A 167 -11.519 -34.422 53.961 1.00 37.70 C
ANISOU 1331 C LYS A 167 4875 4613 4835 -2065 -297 576 C
ATOM 1332 O LYS A 167 -12.570 -35.062 54.073 1.00 39.40 O
ANISOU 1332 O LYS A 167 4997 4872 5102 -2320 -301 626 O
ATOM 1333 CB LYS A 167 -11.902 -31.989 54.494 1.00 31.58 C
ANISOU 1333 CB LYS A 167 3617 4477 3906 -1667 -246 773 C
ATOM 1334 CG LYS A 167 -11.830 -30.892 55.552 1.00 35.93 C
ANISOU 1334 CG LYS A 167 4018 5203 4429 -1373 -99 897 C
ATOM 1335 CD LYS A 167 -12.897 -29.825 55.362 1.00 37.50 C
ANISOU 1335 CD LYS A 167 3876 5750 4624 -1260 -89 954 C
ATOM 1336 CE LYS A 167 -12.696 -29.043 54.083 1.00 35.86 C
ANISOU 1336 CE LYS A 167 3599 5660 4366 -1164 -230 898 C
ATOM 1337 NZ LYS A 167 -13.797 -28.067 53.866 1.00 39.14 N
ANISOU 1337 NZ LYS A 167 3707 6350 4815 -1032 -232 1005 N
ATOM 1338 N GLU A 168 -10.613 -34.702 53.031 1.00 42.56 N
ANISOU 1338 N GLU A 168 5730 4996 5443 -2033 -348 346 N
ATOM 1339 CA GLU A 168 -10.769 -35.834 52.127 1.00 51.46 C
ANISOU 1339 CA GLU A 168 7055 5875 6623 -2270 -392 113 C
ATOM 1340 C GLU A 168 -10.155 -37.083 52.747 1.00 54.43 C
ANISOU 1340 C GLU A 168 7726 5718 7238 -2232 -277 119 C
ATOM 1341 O GLU A 168 -10.567 -38.203 52.449 1.00 61.26 O
ANISOU 1341 O GLU A 168 8718 6325 8234 -2469 -271 23 O
ATOM 1342 CB GLU A 168 -10.122 -35.540 50.771 1.00 58.61 C
ANISOU 1342 CB GLU A 168 8068 6824 7378 -2213 -456 -174 C
ATOM 1343 CG GLU A 168 -8.601 -35.561 50.791 1.00 65.36 C
ANISOU 1343 CG GLU A 168 9170 7363 8299 -1911 -350 -306 C
ATOM 1344 CD GLU A 168 -7.990 -34.986 49.525 1.00 73.11 C
ANISOU 1344 CD GLU A 168 10180 8522 9075 -1811 -373 -543 C
ATOM 1345 OE1 GLU A 168 -8.750 -34.460 48.685 1.00 79.39 O
ANISOU 1345 OE1 GLU A 168 10793 9711 9660 -1948 -493 -533 O
ATOM 1346 OE2 GLU A 168 -6.751 -35.056 49.371 1.00 71.62 O
ANISOU 1346 OE2 GLU A 168 10171 8102 8941 -1564 -259 -703 O
TER 1347 GLU A 168
HETATM 1348 PB GDP A 201 2.980 -9.603 65.146 1.00 9.59 P
HETATM 1349 O1B GDP A 201 1.673 -9.215 64.546 1.00 8.16 O
HETATM 1350 O2B GDP A 201 3.360 -11.066 64.993 1.00 9.06 O
HETATM 1351 O3B GDP A 201 3.158 -9.155 66.590 1.00 11.84 O
HETATM 1352 O3A GDP A 201 4.146 -8.844 64.331 1.00 10.03 O
HETATM 1353 PA GDP A 201 4.040 -7.726 63.160 1.00 10.57 P
HETATM 1354 O1A GDP A 201 3.421 -8.303 61.927 1.00 10.21 O
HETATM 1355 O2A GDP A 201 3.423 -6.464 63.730 1.00 14.52 O
HETATM 1356 O5' GDP A 201 5.579 -7.445 62.886 1.00 10.78 O
HETATM 1357 C5' GDP A 201 6.484 -7.055 63.928 1.00 12.49 C
HETATM 1358 C4' GDP A 201 7.596 -6.175 63.375 1.00 12.23 C
HETATM 1359 O4' GDP A 201 8.432 -6.966 62.517 1.00 11.56 O
HETATM 1360 C3' GDP A 201 7.031 -5.031 62.544 1.00 13.97 C
HETATM 1361 O3' GDP A 201 7.943 -3.940 62.655 1.00 17.37 O
HETATM 1362 C2' GDP A 201 7.098 -5.557 61.124 1.00 13.08 C
HETATM 1363 O2' GDP A 201 7.218 -4.528 60.133 1.00 17.77 O
HETATM 1364 C1' GDP A 201 8.333 -6.435 61.200 1.00 13.94 C
HETATM 1365 N9 GDP A 201 8.285 -7.548 60.230 1.00 11.80 N
HETATM 1366 C8 GDP A 201 7.274 -8.387 59.995 1.00 13.08 C
HETATM 1367 N7 GDP A 201 7.558 -9.276 59.037 1.00 10.29 N
HETATM 1368 C5 GDP A 201 8.829 -8.971 58.637 1.00 8.86 C
HETATM 1369 C6 GDP A 201 9.695 -9.527 57.680 1.00 10.92 C
HETATM 1370 O6 GDP A 201 9.344 -10.516 56.970 1.00 10.58 O
HETATM 1371 N1 GDP A 201 10.923 -9.050 57.491 1.00 10.22 N
HETATM 1372 C2 GDP A 201 11.277 -8.000 58.255 1.00 11.45 C
HETATM 1373 N2 GDP A 201 12.522 -7.496 58.062 1.00 13.63 N
HETATM 1374 N3 GDP A 201 10.526 -7.384 59.202 1.00 11.37 N
HETATM 1375 C4 GDP A 201 9.278 -7.897 59.384 1.00 11.24 C
HETATM 1376 MG MG A 202 -0.043 -8.267 65.237 1.00 10.43 MG
HETATM 1377 N12 91G A 203 0.761 -14.377 72.547 1.00 17.16 N
HETATM 1378 C13 91G A 203 1.290 -13.150 73.186 1.00 14.34 C
HETATM 1379 C17 91G A 203 0.891 -14.425 71.092 1.00 19.01 C
HETATM 1380 C20 91G A 203 2.760 -8.864 70.429 1.00 7.09 C
HETATM 1381 C24 91G A 203 3.552 -18.062 77.492 1.00 53.21 C
HETATM 1382 C28 91G A 203 4.256 -17.926 74.669 1.00 69.12 C
HETATM 1383 CL01 91G A 203 -3.547 -17.269 70.416 1.00 17.01 CL
HETATM 1384 C02 91G A 203 -2.486 -17.367 71.771 1.00 12.92 C
HETATM 1385 C03 91G A 203 -2.568 -18.457 72.662 1.00 13.41 C
HETATM 1386 C04 91G A 203 -1.737 -18.476 73.757 1.00 13.66 C
HETATM 1387 C05 91G A 203 -0.731 -17.490 73.950 1.00 17.10 C
HETATM 1388 C06 91G A 203 -0.595 -16.431 73.024 1.00 12.71 C
HETATM 1389 C07 91G A 203 -1.512 -16.397 71.907 1.00 14.62 C
HETATM 1390 N08 91G A 203 0.071 -17.624 75.044 1.00 17.65 N
HETATM 1391 C09 91G A 203 0.995 -16.707 75.223 1.00 18.29 C
HETATM 1392 N10 91G A 203 1.199 -15.659 74.403 1.00 15.55 N
HETATM 1393 C11 91G A 203 0.452 -15.490 73.296 1.00 14.49 C
HETATM 1394 C14 91G A 203 0.674 -11.919 72.554 1.00 15.20 C
HETATM 1395 N15 91G A 203 0.798 -11.929 71.088 1.00 15.06 N
HETATM 1396 C16 91G A 203 0.291 -13.176 70.451 1.00 21.99 C
HETATM 1397 C18 91G A 203 1.249 -10.894 70.368 1.00 20.02 C
HETATM 1398 C19 91G A 203 1.683 -9.664 71.141 1.00 16.83 C
HETATM 1399 O21 91G A 203 1.331 -10.948 69.142 1.00 13.31 O
HETATM 1400 N22 91G A 203 1.809 -16.776 76.299 1.00 24.85 N
HETATM 1401 C23 91G A 203 2.080 -17.993 77.054 1.00 39.46 C
HETATM 1402 C25 91G A 203 4.330 -19.189 76.795 1.00 60.95 C
HETATM 1403 N26 91G A 203 4.632 -19.059 75.489 1.00 66.04 N
HETATM 1404 C27 91G A 203 5.393 -20.111 74.841 1.00 64.90 C
HETATM 1405 O29 91G A 203 4.679 -20.129 77.422 1.00 59.43 O
HETATM 1406 C30 91G A 203 -3.665 -19.488 72.663 1.00 13.81 C
HETATM 1407 C31 91G A 203 -4.564 -19.470 73.724 1.00 15.42 C
HETATM 1408 C32 91G A 203 -5.586 -20.399 73.810 1.00 15.26 C
HETATM 1409 O33 91G A 203 -6.431 -20.290 74.923 1.00 16.63 O
HETATM 1410 C34 91G A 203 -5.774 -21.374 72.855 1.00 15.05 C
HETATM 1411 C35 91G A 203 -4.886 -21.450 71.734 1.00 11.65 C
HETATM 1412 C36 91G A 203 -3.810 -20.495 71.634 1.00 13.36 C
HETATM 1413 C37 91G A 203 -2.933 -20.587 70.513 1.00 11.43 C
HETATM 1414 C38 91G A 203 -3.129 -21.574 69.546 1.00 10.78 C
HETATM 1415 C39 91G A 203 -4.176 -22.499 69.636 1.00 13.44 C
HETATM 1416 C40 91G A 203 -5.054 -22.442 70.718 1.00 10.86 C
HETATM 1417 O HOH A 301 -12.260 -15.335 61.855 1.00 29.22 O
HETATM 1418 O HOH A 302 -12.366 -25.350 48.086 1.00 21.08 O
HETATM 1419 O HOH A 303 -1.329 -28.099 78.736 1.00 38.90 O
HETATM 1420 O HOH A 304 6.623 -29.951 70.511 1.00 26.78 O
HETATM 1421 O HOH A 305 8.322 -15.239 72.923 1.00 32.53 O
HETATM 1422 O HOH A 306 8.776 1.977 62.034 1.00 33.60 O
HETATM 1423 O HOH A 307 -8.175 -15.316 70.511 1.00 29.92 O
HETATM 1424 O HOH A 308 21.738 -20.341 63.121 1.00 39.55 O
HETATM 1425 O HOH A 309 2.924 -32.401 68.609 1.00 39.99 O
HETATM 1426 O HOH A 310 3.692 -13.995 48.203 1.00 17.61 O
HETATM 1427 O HOH A 311 -10.262 -30.869 73.238 1.00 31.08 O
HETATM 1428 O HOH A 312 -5.942 -28.203 46.564 1.00 16.66 O
HETATM 1429 O HOH A 313 -14.729 -23.971 47.195 1.00 25.12 O
HETATM 1430 O HOH A 314 14.352 -21.407 60.067 1.00 27.48 O
HETATM 1431 O HOH A 315 7.277 -6.013 49.437 1.00 27.03 O
HETATM 1432 O HOH A 316 14.198 -18.523 52.251 1.00 27.82 O
HETATM 1433 O HOH A 317 12.464 -16.723 49.020 1.00 21.57 O
HETATM 1434 O HOH A 318 -0.120 -29.322 51.404 1.00 30.82 O
HETATM 1435 O HOH A 319 -7.464 -9.299 49.307 1.00 27.07 O
HETATM 1436 O HOH A 320 -3.740 -32.566 58.920 1.00 25.75 O
HETATM 1437 O HOH A 321 9.334 -2.741 59.670 1.00 27.04 O
HETATM 1438 O HOH A 322 -3.644 0.441 71.234 1.00 46.64 O
HETATM 1439 O HOH A 323 -0.448 -1.299 71.406 1.00 37.41 O
HETATM 1440 O HOH A 324 -10.663 -35.274 62.843 1.00 46.29 O
HETATM 1441 O HOH A 325 -14.256 -13.016 59.159 1.00 29.72 O
HETATM 1442 O HOH A 326 -12.027 -21.061 40.003 1.00 26.51 O
HETATM 1443 O HOH A 327 -5.211 -7.970 63.391 1.00 16.94 O
HETATM 1444 O HOH A 328 -0.690 -30.086 58.333 1.00 15.77 O
HETATM 1445 O HOH A 329 -10.370 -23.729 79.002 1.00 17.16 O
HETATM 1446 O HOH A 330 3.768 -4.484 65.435 1.00 19.08 O
HETATM 1447 O HOH A 331 10.317 -25.699 52.890 1.00 29.47 O
HETATM 1448 O HOH A 332 -11.495 -6.976 58.723 1.00 33.30 O
HETATM 1449 O HOH A 333 -1.489 -8.415 73.003 1.00 26.62 O
HETATM 1450 O HOH A 334 8.740 -10.915 46.382 1.00 37.43 O
HETATM 1451 O HOH A 335 1.115 -6.435 65.021 1.00 10.96 O
HETATM 1452 O HOH A 336 -14.108 -25.866 55.302 1.00 31.95 O
HETATM 1453 O HOH A 337 -1.222 -9.973 65.315 1.00 10.41 O
HETATM 1454 O HOH A 338 4.725 -16.510 72.287 1.00 19.23 O
HETATM 1455 O HOH A 339 19.719 -19.898 68.413 1.00 32.69 O
HETATM 1456 O HOH A 340 13.046 -11.985 50.863 1.00 24.19 O
HETATM 1457 O HOH A 341 -10.577 -22.396 38.069 1.00 27.82 O
HETATM 1458 O HOH A 342 -4.147 1.040 66.892 1.00 27.93 O
HETATM 1459 O HOH A 343 15.659 -6.672 55.000 1.00 22.65 O
HETATM 1460 O HOH A 344 -15.545 -25.917 71.847 1.00 36.36 O
HETATM 1461 O HOH A 345 5.634 0.007 54.774 1.00 39.25 O
HETATM 1462 O HOH A 346 -8.073 -11.756 72.148 1.00 38.14 O
HETATM 1463 O HOH A 347 23.442 -16.346 63.106 1.00 28.44 O
HETATM 1464 O HOH A 348 -15.308 -22.661 57.826 1.00 37.30 O
HETATM 1465 O HOH A 349 11.866 -20.638 75.132 1.00 27.35 O
HETATM 1466 O HOH A 350 7.455 -23.710 73.796 1.00 30.76 O
HETATM 1467 O HOH A 351 -16.631 -15.991 60.576 1.00 35.11 O
HETATM 1468 O HOH A 352 0.702 -33.202 56.471 1.00 33.11 O
HETATM 1469 O HOH A 353 -9.819 -28.720 60.150 1.00 20.56 O
HETATM 1470 O HOH A 354 1.396 -32.547 53.072 1.00 36.07 O
HETATM 1471 O HOH A 355 -1.531 -25.951 41.288 1.00 15.90 O
HETATM 1472 O HOH A 356 11.596 -17.527 51.433 1.00 28.56 O
HETATM 1473 O HOH A 357 -11.555 -27.669 73.563 1.00 22.97 O
HETATM 1474 O HOH A 358 1.057 -22.085 46.533 1.00 15.81 O
HETATM 1475 O HOH A 359 -12.527 -11.711 64.589 1.00 16.52 O
HETATM 1476 O HOH A 360 -5.124 -8.297 72.272 1.00 32.89 O
HETATM 1477 O HOH A 361 14.842 -28.992 65.136 1.00 30.00 O
HETATM 1478 O HOH A 362 -11.091 -32.162 50.389 1.00 35.06 O
HETATM 1479 O HOH A 363 -7.523 -32.158 72.884 1.00 30.69 O
HETATM 1480 O HOH A 364 12.173 -10.910 64.904 1.00 20.05 O
HETATM 1481 O HOH A 365 -1.567 -7.037 65.998 1.00 10.63 O
HETATM 1482 O HOH A 366 -1.685 -30.422 74.239 1.00 24.16 O
HETATM 1483 O HOH A 367 -15.452 -19.064 58.392 1.00 42.84 O
HETATM 1484 O HOH A 368 7.636 -31.746 56.698 1.00 19.91 O
HETATM 1485 O HOH A 369 -2.290 -32.642 64.748 1.00 29.87 O
HETATM 1486 O HOH A 370 -3.657 -32.522 56.293 1.00 23.52 O
HETATM 1487 O HOH A 371 10.207 -11.866 66.455 1.00 25.12 O
HETATM 1488 O HOH A 372 -5.565 -2.076 72.289 1.00 40.16 O
HETATM 1489 O HOH A 373 0.530 -8.601 67.247 1.00 9.56 O
HETATM 1490 O HOH A 374 4.301 -6.712 67.214 1.00 16.75 O
HETATM 1491 O HOH A 375 2.129 -6.209 55.884 1.00 11.96 O
HETATM 1492 O HOH A 376 6.271 -18.074 67.554 1.00 10.33 O
HETATM 1493 O HOH A 377 -8.033 -28.790 42.651 1.00 29.08 O
HETATM 1494 O HOH A 378 8.178 -0.207 67.042 1.00 36.54 O
HETATM 1495 O HOH A 379 19.454 -15.253 56.696 1.00 41.09 O
HETATM 1496 O HOH A 380 7.096 -36.406 58.558 1.00 34.96 O
HETATM 1497 O HOH A 381 -0.435 -16.154 68.652 1.00 10.81 O
HETATM 1498 O HOH A 382 -0.800 -31.634 62.879 1.00 40.69 O
HETATM 1499 O HOH A 383 15.400 -18.801 74.630 1.00 14.33 O
HETATM 1500 O HOH A 384 10.249 -30.812 56.823 1.00 25.83 O
HETATM 1501 O HOH A 385 12.726 -34.665 62.359 1.00 28.32 O
HETATM 1502 O HOH A 386 -11.603 -28.551 62.267 1.00 36.16 O
HETATM 1503 O HOH A 387 8.479 -3.711 51.818 1.00 26.55 O
HETATM 1504 O HOH A 388 7.342 -7.123 46.622 1.00 40.67 O
HETATM 1505 O HOH A 389 -0.813 -20.451 81.251 1.00 25.77 O
HETATM 1506 O HOH A 390 -9.110 -36.788 63.078 1.00 44.13 O
HETATM 1507 O HOH A 391 -8.753 -11.689 46.454 1.00 30.21 O
HETATM 1508 O HOH A 392 6.481 -26.510 52.154 1.00 19.37 O
HETATM 1509 O HOH A 393 -9.267 -27.523 39.778 1.00 31.42 O
HETATM 1510 O HOH A 394 4.358 -25.339 76.525 1.00 36.68 O
HETATM 1511 O HOH A 395 15.563 -4.554 57.255 1.00 42.27 O
HETATM 1512 O HOH A 396 -15.826 -24.789 69.505 1.00 28.22 O
HETATM 1513 O HOH A 397 4.903 2.581 57.730 1.00 34.00 O
HETATM 1514 O HOH A 398 3.598 -4.287 61.861 1.00 13.76 O
HETATM 1515 O HOH A 399 -9.980 -9.392 50.567 1.00 26.80 O
HETATM 1516 O HOH A 400 -3.642 -10.008 75.878 1.00 32.86 O
HETATM 1517 O HOH A 401 -8.626 -5.278 54.909 1.00 43.75 O
HETATM 1518 O HOH A 402 -5.097 -3.039 48.923 1.00 40.25 O
HETATM 1519 O HOH A 403 3.202 -34.252 67.560 1.00 34.92 O
HETATM 1520 O HOH A 404 -7.808 -4.154 61.796 1.00 28.56 O
HETATM 1521 O HOH A 405 -5.649 -19.087 82.663 1.00 27.12 O
HETATM 1522 O HOH A 406 14.512 -10.946 67.208 1.00 22.23 O
HETATM 1523 O HOH A 407 -1.849 -11.200 48.272 1.00 31.52 O
HETATM 1524 O HOH A 408 24.814 -12.974 58.233 1.00 32.35 O
HETATM 1525 O HOH A 409 19.966 -22.167 57.419 1.00 27.55 O
HETATM 1526 O HOH A 410 -19.143 -29.655 71.126 1.00 40.07 O
HETATM 1527 O HOH A 411 6.758 -15.880 46.624 1.00 12.38 O
HETATM 1528 O HOH A 412 11.669 -7.064 61.997 1.00 17.18 O
HETATM 1529 O HOH A 413 0.121 -35.331 50.734 1.00 46.42 O
HETATM 1530 O HOH A 414 10.095 -1.062 55.814 1.00 34.94 O
HETATM 1531 O HOH A 415 23.198 -18.324 60.197 1.00 37.66 O
HETATM 1532 O HOH A 416 5.059 -4.483 50.075 1.00 32.40 O
HETATM 1533 O HOH A 417 -10.674 -29.363 42.361 1.00 42.25 O
HETATM 1534 O HOH A 418 18.568 -13.163 53.875 1.00 32.90 O
HETATM 1535 O HOH A 419 -13.498 -8.697 61.113 1.00 22.91 O
HETATM 1536 O HOH A 420 13.540 -13.211 71.734 1.00 27.46 O
HETATM 1537 O HOH A 421 5.240 -13.479 72.735 1.00 20.82 O
HETATM 1538 O HOH A 422 -11.784 -28.677 58.366 1.00 30.51 O
HETATM 1539 O HOH A 423 8.055 -28.732 54.047 1.00 19.63 O
HETATM 1540 O HOH A 424 -0.948 -28.291 44.193 1.00 19.35 O
HETATM 1541 O HOH A 425 -14.321 -27.824 65.623 1.00 36.49 O
HETATM 1542 O HOH A 426 -18.218 -26.271 51.499 1.00 49.62 O
HETATM 1543 O HOH A 427 -13.578 -24.476 76.125 1.00 19.40 O
HETATM 1544 O HOH A 428 9.826 -13.736 71.244 1.00 32.67 O
HETATM 1545 O HOH A 429 -17.711 -23.884 53.958 1.00 27.35 O
HETATM 1546 O HOH A 430 4.091 -16.926 47.676 1.00 16.81 O
HETATM 1547 O HOH A 431 13.724 -5.015 59.284 1.00 23.23 O
HETATM 1548 O HOH A 432 -3.075 -16.703 80.377 1.00 26.56 O
HETATM 1549 O HOH A 433 13.609 -8.196 63.678 1.00 38.46 O
HETATM 1550 O HOH A 434 17.523 -16.360 54.920 1.00 51.74 O
HETATM 1551 O HOH A 435 17.155 -13.025 51.821 1.00 37.96 O
HETATM 1552 O HOH A 436 -13.202 -29.742 73.641 1.00 30.26 O
HETATM 1553 O HOH A 437 9.804 -7.216 65.711 1.00 31.59 O
HETATM 1554 O HOH A 438 -6.748 -32.150 48.221 1.00 31.66 O
HETATM 1555 O HOH A 439 2.858 -35.359 69.298 1.00 42.67 O
HETATM 1556 O HOH A 440 -5.942 -12.194 75.460 1.00 32.85 O
HETATM 1557 O HOH A 441 -2.774 -30.095 45.333 1.00 36.83 O
HETATM 1558 O HOH A 442 2.894 0.798 58.070 1.00 28.33 O
HETATM 1559 O HOH A 443 -14.249 -23.324 41.654 1.00 25.16 O
HETATM 1560 O HOH A 444 4.491 -1.946 50.878 1.00 33.09 O
HETATM 1561 O HOH A 445 1.540 0.051 60.366 1.00 22.76 O
HETATM 1562 O HOH A 446 20.253 -24.927 57.424 1.00 25.26 O
HETATM 1563 O HOH A 447 10.869 -36.907 65.926 1.00 41.44 O
HETATM 1564 O HOH A 448 11.003 -4.524 63.195 1.00 34.42 O
HETATM 1565 O HOH A 449 4.500 -26.131 50.667 1.00 41.34 O
HETATM 1566 O HOH A 450 -11.868 -10.879 48.143 1.00 28.98 O
HETATM 1567 O HOH A 451 6.418 -34.233 67.790 1.00 36.45 O
HETATM 1568 O HOH A 452 -13.128 -26.530 62.895 1.00 41.74 O
HETATM 1569 O HOH A 453 -1.061 -32.006 60.081 1.00 30.36 O
HETATM 1570 O HOH A 454 18.480 -7.238 55.222 1.00 32.03 O
HETATM 1571 O HOH A 455 19.806 -18.964 55.129 1.00 46.77 O
HETATM 1572 O HOH A 456 12.747 -24.726 53.215 1.00 32.86 O
HETATM 1573 O HOH A 457 -9.116 -37.783 65.094 1.00 46.10 O
HETATM 1574 O HOH A 458 -2.921 -18.871 81.972 1.00 27.85 O
HETATM 1575 O HOH A 459 -6.537 -31.972 75.852 1.00 34.54 O
HETATM 1576 O HOH A 460 10.032 -1.417 61.881 1.00 41.79 O
HETATM 1577 O HOH A 461 -8.862 -30.899 62.572 1.00 37.60 O
HETATM 1578 O HOH A 462 -15.673 -19.660 40.367 1.00 45.62 O
HETATM 1579 O HOH A 463 3.471 -32.263 55.424 1.00 27.03 O
HETATM 1580 O HOH A 464 -5.002 -30.080 48.447 1.00 20.12 O
HETATM 1581 O HOH A 465 -14.184 -10.345 58.862 1.00 26.20 O
HETATM 1582 O HOH A 466 -14.692 -33.307 56.078 1.00 47.79 O
HETATM 1583 O HOH A 467 0.302 -30.248 47.625 1.00 35.59 O
HETATM 1584 O HOH A 468 11.213 -10.267 46.214 1.00 41.92 O
HETATM 1585 O HOH A 469 -9.462 -17.909 82.810 1.00 41.67 O
HETATM 1586 O HOH A 470 4.662 -2.680 48.807 1.00 45.01 O
HETATM 1587 O HOH A 471 6.291 -3.186 65.595 1.00 35.70 O
HETATM 1588 O HOH A 472 6.793 -13.470 45.497 1.00 32.25 O
HETATM 1589 O HOH A 473 -11.911 -8.013 55.056 1.00 39.73 O
HETATM 1590 O HOH A 474 -20.590 -18.977 45.594 1.00 43.50 O
HETATM 1591 O HOH A 475 -15.158 -16.532 40.914 1.00 33.37 O
HETATM 1592 O HOH A 476 4.551 -4.688 44.330 1.00 45.90 O
HETATM 1593 O HOH A 477 -13.847 -9.007 56.279 1.00 41.97 O
HETATM 1594 O HOH A 478 8.073 -7.937 69.974 1.00 40.83 O
HETATM 1595 O HOH A 479 1.804 -26.915 76.711 1.00 42.63 O
HETATM 1596 O HOH A 480 -3.417 -32.477 74.171 1.00 36.78 O
HETATM 1597 O HOH A 481 0.514 -19.496 46.230 1.00 29.72 O
HETATM 1598 O HOH A 482 -13.618 -25.853 73.780 1.00 27.20 O
HETATM 1599 O HOH A 483 11.653 -3.334 58.046 1.00 35.93 O
HETATM 1600 O HOH A 484 4.850 -34.738 56.147 1.00 43.76 O
HETATM 1601 O HOH A 485 -16.060 -25.703 45.896 1.00 39.62 O
HETATM 1602 O HOH A 486 -17.220 -26.509 72.703 1.00 31.15 O
HETATM 1603 O HOH A 487 -15.731 -26.310 67.168 1.00 41.83 O
HETATM 1604 O HOH A 488 -7.729 -8.146 46.668 1.00 43.57 O
HETATM 1605 O HOH A 489 21.721 -16.824 57.205 1.00 46.61 O
HETATM 1606 O HOH A 490 -14.480 -9.422 52.372 1.00 41.43 O
HETATM 1607 O HOH A 491 -5.454 -10.529 76.526 1.00 31.42 O
HETATM 1608 O HOH A 492 20.276 -28.048 62.665 1.00 42.04 O
HETATM 1609 O HOH A 493 -20.831 -17.973 47.485 1.00 49.99 O
HETATM 1610 O HOH A 494 -2.474 -30.651 47.469 1.00 38.99 O
HETATM 1611 O HOH A 495 -10.083 -26.829 75.784 1.00 19.54 O
HETATM 1612 O HOH A 496 10.896 -28.731 55.093 1.00 32.18 O
HETATM 1613 O HOH A 497 -2.674 -0.808 73.962 1.00 37.27 O
HETATM 1614 O HOH A 498 -17.947 -31.636 67.425 1.00 45.85 O
HETATM 1615 O HOH A 499 -14.065 -28.522 60.895 1.00 45.68 O
HETATM 1616 O HOH A 500 -16.057 -21.743 41.039 1.00 36.72 O
HETATM 1617 O HOH A 501 13.544 -11.042 47.594 1.00 49.80 O
HETATM 1618 O HOH A 502 -7.648 -29.604 44.921 1.00 29.26 O
HETATM 1619 O HOH A 503 6.648 -4.391 44.676 1.00 47.68 O
HETATM 1620 O HOH A 504 -1.639 -29.618 77.154 1.00 41.87 O
HETATM 1621 O HOH A 505 -1.560 -28.342 40.289 1.00 35.59 O
HETATM 1622 O HOH A 506 -5.971 2.586 68.602 1.00 34.99 O
HETATM 1623 O HOH A 507 15.573 -10.737 50.635 1.00 36.73 O
HETATM 1624 O HOH A 508 5.723 -6.269 69.333 1.00 34.29 O
HETATM 1625 O HOH A 509 7.016 -34.328 56.802 1.00 37.08 O
HETATM 1626 O HOH A 510 16.862 -16.862 73.297 0.33 20.00 O
HETATM 1627 O HOH A 511 0.870 -7.115 73.362 1.00 44.58 O
HETATM 1628 O HOH A 512 7.502 -31.046 53.902 1.00 26.39 O
HETATM 1629 O HOH A 513 6.336 -32.594 70.367 1.00 27.58 O
HETATM 1630 O HOH A 514 -13.579 -31.412 59.918 1.00 46.01 O
HETATM 1631 O HOH A 515 -3.596 -7.736 74.436 1.00 37.21 O
HETATM 1632 O HOH A 516 13.460 -6.978 65.592 1.00 51.81 O
HETATM 1633 O HOH A 517 6.267 -2.656 50.141 1.00 31.74 O
HETATM 1634 O HOH A 518 4.555 -30.924 52.579 1.00 38.21 O
HETATM 1635 O HOH A 519 -4.064 -28.690 39.364 1.00 40.78 O
HETATM 1636 O HOH A 520 11.244 -5.942 47.966 1.00 46.61 O
HETATM 1637 O HOH A 521 4.544 -12.617 74.630 1.00 47.00 O
HETATM 1638 O HOH A 522 -12.154 -8.987 48.806 1.00 42.78 O
HETATM 1639 O HOH A 523 24.698 -24.698 65.461 0.33 46.15 O
HETATM 1640 O HOH A 524 -18.102 -26.323 53.825 1.00 51.97 O
HETATM 1641 O HOH A 525 9.838 -1.737 53.502 1.00 34.73 O
HETATM 1642 O HOH A 526 12.378 -16.181 78.376 1.00 47.35 O
HETATM 1643 O HOH A 527 20.694 -15.343 53.596 1.00 45.47 O
HETATM 1644 O HOH A 528 3.167 -5.930 72.767 1.00 45.76 O
HETATM 1645 O HOH A 529 1.085 0.000 45.080 0.50 46.63 O
HETATM 1646 O HOH A 530 14.597 -14.597 75.562 0.33 28.37 O
CONECT 89 1380
CONECT 119 1376
CONECT 1348 1349 1350 1351 1352
CONECT 1349 1348 1376
CONECT 1350 1348
CONECT 1351 1348
CONECT 1352 1348 1353
CONECT 1353 1352 1354 1355 1356
CONECT 1354 1353
CONECT 1355 1353
CONECT 1356 1353 1357
CONECT 1357 1356 1358
CONECT 1358 1357 1359 1360
CONECT 1359 1358 1364
CONECT 1360 1358 1361 1362
CONECT 1361 1360
CONECT 1362 1360 1363 1364
CONECT 1363 1362
CONECT 1364 1359 1362 1365
CONECT 1365 1364 1366 1375
CONECT 1366 1365 1367
CONECT 1367 1366 1368
CONECT 1368 1367 1369 1375
CONECT 1369 1368 1370 1371
CONECT 1370 1369
CONECT 1371 1369 1372
CONECT 1372 1371 1373 1374
CONECT 1373 1372
CONECT 1374 1372 1375
CONECT 1375 1365 1368 1374
CONECT 1376 119 1349 1451 1453
CONECT 1376 1481 1489
CONECT 1377 1378 1379 1393
CONECT 1378 1377 1394
CONECT 1379 1377 1396
CONECT 1380 89 1398
CONECT 1381 1401 1402
CONECT 1382 1403
CONECT 1383 1384
CONECT 1384 1383 1385 1389
CONECT 1385 1384 1386 1406
CONECT 1386 1385 1387
CONECT 1387 1386 1388 1390
CONECT 1388 1387 1389 1393
CONECT 1389 1384 1388
CONECT 1390 1387 1391
CONECT 1391 1390 1392 1400
CONECT 1392 1391 1393
CONECT 1393 1377 1388 1392
CONECT 1394 1378 1395
CONECT 1395 1394 1396 1397
CONECT 1396 1379 1395
CONECT 1397 1395 1398 1399
CONECT 1398 1380 1397
CONECT 1399 1397
CONECT 1400 1391 1401
CONECT 1401 1381 1400
CONECT 1402 1381 1403 1405
CONECT 1403 1382 1402 1404
CONECT 1404 1403
CONECT 1405 1402
CONECT 1406 1385 1407 1412
CONECT 1407 1406 1408
CONECT 1408 1407 1409 1410
CONECT 1409 1408
CONECT 1410 1408 1411
CONECT 1411 1410 1412 1416
CONECT 1412 1406 1411 1413
CONECT 1413 1412 1414
CONECT 1414 1413 1415
CONECT 1415 1414 1416
CONECT 1416 1411 1415
CONECT 1451 1376
CONECT 1453 1376
CONECT 1481 1376
CONECT 1489 1376
MASTER 339 0 3 5 6 0 14 6 1642 1 76 13
END