HEADER CHAPERONE 07-JUL-17 5ODX
TITLE CRYSTAL STRUCTURE OF HSP90-ALPHA N-DOMAIN IN COMPLEX WITH INDAZOLE
TITLE 2 DERIVATIVE
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
EXPDTA X-RAY DIFFRACTION
AUTHOR M.AMARAL,D.SCHUETZ
REVDAT 5 16-OCT-19 5ODX 1 REMARK
REVDAT 4 19-DEC-18 5ODX 1 REMARK LINK
REVDAT 3 06-JUN-18 5ODX 1 JRNL
REVDAT 2 23-MAY-18 5ODX 1 JRNL
REVDAT 1 18-APR-18 5ODX 0
JRNL AUTH D.A.SCHUETZ,L.RICHTER,M.AMARAL,M.GRANDITS,U.GRADLER,D.MUSIL,
JRNL AUTH 2 H.P.BUCHSTALLER,H.M.EGGENWEILER,M.FRECH,G.F.ECKER
JRNL TITL LIGAND DESOLVATION STEERS ON-RATE AND IMPACTS DRUG RESIDENCE
JRNL TITL 2 TIME OF HEAT SHOCK PROTEIN 90 (HSP90) INHIBITORS.
JRNL REF J. MED. CHEM. V. 61 4397 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 29701469
JRNL DOI 10.1021/ACS.JMEDCHEM.8B00080
REMARK 2
REMARK 2 RESOLUTION. 1.82 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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 27970
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1398
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 14
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.81
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.88
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.04
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2857
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.4140
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2714
REMARK 3 BIN R VALUE (WORKING SET) : 0.4120
REMARK 3 BIN FREE R VALUE : 0.4450
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.01
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 143
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 : 44
REMARK 3 SOLVENT ATOMS : 228
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.16720
REMARK 3 B22 (A**2) : 1.06320
REMARK 3 B33 (A**2) : -2.23040
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) : 0.116
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.106
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.108
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.101
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 : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1735 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2343 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 616 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 48 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 246 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1735 ; 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 : 234 ; 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 : 2245 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.50
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.33
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): 0.6818 29.5850 28.7655
REMARK 3 T TENSOR
REMARK 3 T11: -0.0350 T22: -0.0365
REMARK 3 T33: -0.0553 T12: -0.0058
REMARK 3 T13: -0.0329 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 1.2368 L22: 1.0765
REMARK 3 L33: 1.1950 L12: -0.2708
REMARK 3 L13: -0.0402 L23: -0.2156
REMARK 3 S TENSOR
REMARK 3 S11: 0.0216 S12: -0.0565 S13: -0.0457
REMARK 3 S21: 0.0226 S22: -0.0028 S23: 0.0094
REMARK 3 S31: 0.0277 S32: 0.0600 S33: -0.0188
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5ODX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1200005655.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28017
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.819
REMARK 200 RESOLUTION RANGE LOW (A) : 48.779
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.570
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM FLUORIDE, 0.1 M BIS TRIS
REMARK 280 PROPANE, PH 8.5, 20 % W/V PEG 3350, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 277.15K
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 34.94000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.41850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 48.77900
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.94000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.41850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.77900
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.94000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 44.41850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.77900
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.94000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 44.41850
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 48.77900
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: 270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 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 GLU A 15
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: 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 CE MET A 130 NE2 GLN A 133 1.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 S DMS A 302 S DMS A 303 2565 0.09
REMARK 500 C2 DMS A 302 C1 DMS A 303 2565 0.09
REMARK 500 C1 DMS A 302 O DMS A 303 2565 0.16
REMARK 500 O DMS A 302 C2 DMS A 303 2565 0.17
REMARK 500 O DMS A 302 S DMS A 303 2565 1.54
REMARK 500 S DMS A 302 O DMS A 303 2565 1.55
REMARK 500 C1 DMS A 302 S DMS A 303 2565 1.62
REMARK 500 S DMS A 302 C2 DMS A 303 2565 1.63
REMARK 500 C2 DMS A 302 S DMS A 303 2565 1.70
REMARK 500 S DMS A 302 C1 DMS A 303 2565 1.72
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 ASN A 105 -51.60 -130.29
REMARK 500 ALA A 166 -144.20 62.58
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 9RZ A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DMS A 302 and DMS A
REMARK 800 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DMS A 302 and DMS A
REMARK 800 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DMS A 302 and DMS A
REMARK 800 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DMS A 302 and DMS A
REMARK 800 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DMS A 302 and DMS A
REMARK 800 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues DMS A 302 and DMS A
REMARK 800 303
DBREF 5ODX A 9 236 UNP P07900 HS90A_HUMAN 9 236
SEQADV 5ODX GLY A 8 UNP P07900 EXPRESSION TAG
SEQRES 1 A 229 GLY ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE
SEQRES 2 A 229 ALA PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE
SEQRES 3 A 229 ILE ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG
SEQRES 4 A 229 GLU LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE
SEQRES 5 A 229 ARG TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER
SEQRES 6 A 229 GLY LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN
SEQRES 7 A 229 ASP ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET
SEQRES 8 A 229 THR LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE ALA
SEQRES 9 A 229 LYS SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA
SEQRES 10 A 229 GLY ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY
SEQRES 11 A 229 PHE TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL
SEQRES 12 A 229 ILE THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU
SEQRES 13 A 229 SER SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR
SEQRES 14 A 229 GLY GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS
SEQRES 15 A 229 LEU LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG
SEQRES 16 A 229 ILE LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY
SEQRES 17 A 229 TYR PRO ILE THR LEU PHE VAL GLU LYS GLU ARG ASP LYS
SEQRES 18 A 229 GLU VAL SER ASP ASP GLU ALA GLU
HET 9RZ A 301 36
HET DMS A 302 4
HET DMS A 303 4
HETNAM 9RZ 3-[(3~{S})-3-METHOXYPIPERIDIN-1-YL]CARBONYL-~{N}-
HETNAM 2 9RZ METHYL-~{N}-(4-MORPHOLIN-4-YLPHENYL)-6-OXIDANYL-1~{H}-
HETNAM 3 9RZ INDAZOLE-5-CARBOXAMIDE
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 2 9RZ C26 H31 N5 O5
FORMUL 3 DMS 2(C2 H6 O S)
FORMUL 5 HOH *228(H2 O)
HELIX 1 AA1 GLN A 23 THR A 36 1 14
HELIX 2 AA2 GLU A 42 LEU A 64 1 23
HELIX 3 AA3 THR A 65 ASP A 71 5 7
HELIX 4 AA4 THR A 99 ASN A 105 1 7
HELIX 5 AA5 ASN A 105 ALA A 124 1 20
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 GLU A 192 LEU A 198 5 7
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 GLN A 159 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
SITE 1 AC1 15 ASN A 51 ASP A 54 ALA A 55 ASP A 93
SITE 2 AC1 15 ILE A 96 GLY A 97 MET A 98 GLY A 135
SITE 3 AC1 15 PHE A 138 VAL A 150 TRP A 162 THR A 184
SITE 4 AC1 15 VAL A 186 HOH A 444 HOH A 473
SITE 1 AC2 2 HOH A 461 HOH A 551
SITE 1 AC3 2 HOH A 461 HOH A 551
SITE 1 AC4 2 HOH A 461 HOH A 551
SITE 1 AC5 2 HOH A 461 HOH A 551
SITE 1 AC6 2 HOH A 461 HOH A 551
SITE 1 AC7 2 HOH A 461 HOH A 551
CRYST1 69.880 88.837 97.558 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 0.014310 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011257 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010250 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
