HEADER CHAPERONE 22-NOV-17 6F1N
TITLE ESTIMATION OF RELATIVE DRUG-TARGET RESIDENCE TIMES BY RANDOM
TITLE 2 ACCELERATION MOLECULAR DYNAMICS SIMULATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HEAT SHOCK 86 KDA,HSP86,LIPOPOLYSACCHARIDE-ASSOCIATED
COMPND 5 PROTEIN 2,LPS-ASSOCIATED PROTEIN 2,RENAL CARCINOMA ANTIGEN NY-REN-38;
COMPND 6 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: HSP90AA1, HSP90A, HSPC1, HSPCA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CHAPERONE PROTEIN, ATP BINDING, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.MUSIL,M.LEHMANN,H.-M.EGGENWEILER
REVDAT 2 18-JUL-18 6F1N 1 JRNL
REVDAT 1 30-MAY-18 6F1N 0
JRNL AUTH D.B.KOKH,M.AMARAL,J.BOMKE,U.GRADLER,D.MUSIL,H.P.BUCHSTALLER,
JRNL AUTH 2 M.K.DREYER,M.FRECH,M.LOWINSKI,F.VALLEE,M.BIANCIOTTO,A.RAK,
JRNL AUTH 3 R.C.WADE
JRNL TITL ESTIMATION OF DRUG-TARGET RESIDENCE TIMES BY TAU-RANDOM
JRNL TITL 2 ACCELERATION MOLECULAR DYNAMICS SIMULATIONS.
JRNL REF J CHEM THEORY COMPUT V. 14 3859 2018
JRNL REFN ISSN 1549-9626
JRNL PMID 29768913
JRNL DOI 10.1021/ACS.JCTC.8B00230
REMARK 2
REMARK 2 RESOLUTION. 2.09 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.9
REMARK 3 NUMBER OF REFLECTIONS : 14935
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.213
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 756
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.09
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 34.90
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1107
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2207
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1050
REMARK 3 BIN R VALUE (WORKING SET) : 0.2206
REMARK 3 BIN FREE R VALUE : 0.2243
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.15
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 57
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1644
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 81
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.75940
REMARK 3 B22 (A**2) : -8.16780
REMARK 3 B33 (A**2) : 3.40850
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.270
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.207
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.163
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.202
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.162
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1718 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2323 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 613 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 49 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 244 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1718 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 232 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2022 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.08
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.18
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.72
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 65.1076 30.2461 29.0075
REMARK 3 T TENSOR
REMARK 3 T11: -0.1316 T22: -0.1624
REMARK 3 T33: -0.1943 T12: -0.0095
REMARK 3 T13: -0.0141 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 5.9857 L22: 1.5720
REMARK 3 L33: 3.9022 L12: -0.8165
REMARK 3 L13: -1.2564 L23: 0.5813
REMARK 3 S TENSOR
REMARK 3 S11: 0.1933 S12: 0.0164 S13: 0.2996
REMARK 3 S21: -0.1346 S22: -0.0459 S23: -0.0270
REMARK 3 S31: -0.3521 S32: 0.1168 S33: -0.1474
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6F1N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1200007631.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14942
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.090
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 (%) : 84.2
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 30.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.60
REMARK 200 R MERGE FOR SHELL (I) : 0.23900
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: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NA-CACODYLATE, PH 6.5 30% PEG8000 0.2
REMARK 280 M AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 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 1.000000 0.000000 0.000000 32.83600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.06000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 49.55450
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.83600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.06000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 49.55450
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.83600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.06000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 49.55450
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.83600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 45.06000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 49.55450
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 THR A 5
REMARK 465 GLN A 6
REMARK 465 THR A 7
REMARK 465 GLN A 8
REMARK 465 ASP A 9
REMARK 465 GLN A 10
REMARK 465 PRO A 11
REMARK 465 MET A 12
REMARK 465 GLU A 13
REMARK 465 GLU A 14
REMARK 465 LYS A 224
REMARK 465 GLU A 225
REMARK 465 ARG A 226
REMARK 465 ASP A 227
REMARK 465 LYS A 228
REMARK 465 GLU A 229
REMARK 465 VAL A 230
REMARK 465 SER A 231
REMARK 465 ASP A 232
REMARK 465 ASP A 233
REMARK 465 GLU A 234
REMARK 465 ALA A 235
REMARK 465 GLU A 236
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 ILE A 110 41.92 -104.15
REMARK 500 ALA A 166 -145.59 64.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C8W A 302
DBREF 6F1N A 1 236 UNP P07900 HS90A_HUMAN 123 358
SEQRES 1 A 236 MET PRO GLU GLU THR GLN THR GLN ASP GLN PRO MET GLU
SEQRES 2 A 236 GLU GLU GLU VAL GLU THR PHE ALA PHE GLN ALA GLU ILE
SEQRES 3 A 236 ALA GLN LEU MET SER LEU ILE ILE ASN THR PHE TYR SER
SEQRES 4 A 236 ASN LYS GLU ILE PHE LEU ARG GLU LEU ILE SER ASN SER
SEQRES 5 A 236 SER ASP ALA LEU ASP LYS ILE ARG TYR GLU SER LEU THR
SEQRES 6 A 236 ASP PRO SER LYS LEU ASP SER GLY LYS GLU LEU HIS ILE
SEQRES 7 A 236 ASN LEU ILE PRO ASN LYS GLN ASP ARG THR LEU THR ILE
SEQRES 8 A 236 VAL ASP THR GLY ILE GLY MET THR LYS ALA ASP LEU ILE
SEQRES 9 A 236 ASN ASN LEU GLY THR ILE ALA LYS SER GLY THR LYS ALA
SEQRES 10 A 236 PHE MET GLU ALA LEU GLN ALA GLY ALA ASP ILE SER MET
SEQRES 11 A 236 ILE GLY GLN PHE GLY VAL GLY PHE TYR SER ALA TYR LEU
SEQRES 12 A 236 VAL ALA GLU LYS VAL THR VAL ILE THR LYS HIS ASN ASP
SEQRES 13 A 236 ASP GLU GLN TYR ALA TRP GLU SER SER ALA GLY GLY SER
SEQRES 14 A 236 PHE THR VAL ARG THR ASP THR GLY GLU PRO MET GLY ARG
SEQRES 15 A 236 GLY THR LYS VAL ILE LEU HIS LEU LYS GLU ASP GLN THR
SEQRES 16 A 236 GLU TYR LEU GLU GLU ARG ARG ILE LYS GLU ILE VAL LYS
SEQRES 17 A 236 LYS HIS SER GLN PHE ILE GLY TYR PRO ILE THR LEU PHE
SEQRES 18 A 236 VAL GLU LYS GLU ARG ASP LYS GLU VAL SER ASP ASP GLU
SEQRES 19 A 236 ALA GLU
HET SO4 A 301 5
HET C8W A 302 31
HETNAM SO4 SULFATE ION
HETNAM C8W 4-[5-[2-AMINOCARBONYL-3,6-BIS(AZANYL)-5-CYANO-THIENO[2,
HETNAM 2 C8W 3-B]PYRIDIN-4-YL]-2-METHOXY-PHENOXY]BUTANOIC ACID
FORMUL 2 SO4 O4 S 2-
FORMUL 3 C8W C20 H19 N5 O5 S
FORMUL 4 HOH *81(H2 O)
HELIX 1 AA1 GLN A 23 THR A 36 1 14
HELIX 2 AA2 GLU A 42 ASP A 66 1 25
HELIX 3 AA3 PRO A 67 ASP A 71 5 5
HELIX 4 AA4 THR A 99 ASN A 105 1 7
HELIX 5 AA5 ILE A 110 LEU A 122 1 13
HELIX 6 AA6 ASP A 127 GLY A 135 5 9
HELIX 7 AA7 VAL A 136 LEU A 143 5 8
HELIX 8 AA8 GLN A 194 LEU A 198 5 5
HELIX 9 AA9 GLU A 199 SER A 211 1 13
SHEET 1 AA1 8 GLU A 18 ALA A 21 0
SHEET 2 AA1 8 SER A 169 THR A 174 -1 O PHE A 170 N PHE A 20
SHEET 3 AA1 8 TYR A 160 SER A 164 -1 N ALA A 161 O ARG A 173
SHEET 4 AA1 8 ALA A 145 LYS A 153 -1 N VAL A 150 O TRP A 162
SHEET 5 AA1 8 GLY A 183 LEU A 190 -1 O ILE A 187 N THR A 149
SHEET 6 AA1 8 THR A 88 ASP A 93 -1 N ILE A 91 O VAL A 186
SHEET 7 AA1 8 ILE A 78 ASN A 83 -1 N ILE A 81 O THR A 90
SHEET 8 AA1 8 ILE A 218 LEU A 220 1 O THR A 219 N LEU A 80
CISPEP 1 GLU A 15 GLU A 16 0 1.36
SITE 1 AC1 5 GLU A 75 HIS A 77 ASN A 79 SER A 169
SITE 2 AC1 5 THR A 219
SITE 1 AC2 17 ASN A 51 SER A 52 ALA A 55 ASP A 93
SITE 2 AC2 17 ILE A 96 GLY A 97 MET A 98 ASN A 106
SITE 3 AC2 17 LEU A 107 GLY A 108 THR A 109 GLY A 135
SITE 4 AC2 17 PHE A 138 TYR A 139 THR A 184 HOH A 421
SITE 5 AC2 17 HOH A 439
CRYST1 65.672 90.120 99.109 90.00 90.00 90.00 I 2 2 2 8
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 0.015227 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011096 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010090 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
