HEADER CHAPERONE 21-MAR-06 2GFD
TITLE GRP94 IN COMPLEX WITH THE NOVEL HSP90 INHIBITOR RADAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOPLASMIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN OF GRP94 RESIDUES (69-337);
COMPND 5 SYNONYM: 94 KDA GLUCOSE-REGULATED PROTEIN, GRP94;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANIS LUPUS FAMILIARIS;
SOURCE 3 ORGANISM_COMMON: DOG;
SOURCE 4 ORGANISM_TAXID: 9615;
SOURCE 5 STRAIN: FAMILIARIS;
SOURCE 6 GENE: TRA1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PGEX-NB-GRP94
KEYWDS GRP94, HSP82, HSP90, HTPG, CHAPERONE, LIGAND, RADICICOL,
KEYWDS 2 GELDANAMYCIN, RADESTER, RADAMIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.M.IMMORMINO,D.T.GEWIRTH
REVDAT 5 30-AUG-23 2GFD 1 REMARK SEQADV
REVDAT 4 02-AUG-17 2GFD 1 SOURCE
REVDAT 3 24-NOV-10 2GFD 1 JRNL
REVDAT 2 24-FEB-09 2GFD 1 VERSN
REVDAT 1 03-APR-07 2GFD 0
JRNL AUTH R.M.IMMORMINO,L.E.METZGER,P.N.REARDON,D.E.DOLLINS,B.S.BLAGG,
JRNL AUTH 2 D.T.GEWIRTH
JRNL TITL DIFFERENT POSES FOR LIGAND AND CHAPERONE IN INHIBITOR-BOUND
JRNL TITL 2 HSP90 AND GRP94: IMPLICATIONS FOR PARALOG-SPECIFIC DRUG
JRNL TITL 3 DESIGN.
JRNL REF J.MOL.BIOL. V. 388 1033 2009
JRNL REFN ISSN 0022-2836
JRNL PMID 19361515
JRNL DOI 10.1016/J.JMB.2009.03.071
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2313774.130
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 24181
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 SET) : 0.211
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2443
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.44
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3590
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 378
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3352
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 124
REMARK 3 SOLVENT ATOMS : 284
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.43000
REMARK 3 B22 (A**2) : 4.81000
REMARK 3 B33 (A**2) : 3.62000
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) : 0.27
REMARK 3 ESD FROM SIGMAA (A) : 0.28
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.660
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.440 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.350 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.080 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.100 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 53.27
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : 1PE_XPLOR_PARAM.PARAM
REMARK 3 PARAMETER FILE 4 : PG4_XPLOR_PARAM.PARAM
REMARK 3 PARAMETER FILE 5 : SEMI_WEAK_RAD.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : 1PE_XPLOR_TOP.TOP
REMARK 3 TOPOLOGY FILE 4 : PG4_XPLOR_TOP.TOP
REMARK 3 TOPOLOGY FILE 5 : RADAMIDE.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GFD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037047.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99997
REMARK 200 MONOCHROMATOR : SAGITAL CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29502
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.38600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.610
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1YT1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8.0 25-30% PEG MME 550
REMARK 280 10-50 MM MGCL2 .5-1UL LIGAND (IN DMSO) PER 50 PROTEIN FOR FINAL
REMARK 280 CONC ~5-10MM , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 32.74500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 47.79000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.28500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.79000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.74500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.28500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 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 300 REMARK: EACH PROTOMER IN THE ASYMMETRICT UNIT COMPRISES AN ASSUMED
REMARK 300 BIOLOGICAL MOLECULE
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 65
REMARK 465 SER A 66
REMARK 465 HIS A 67
REMARK 465 MET A 68
REMARK 465 LEU A 69
REMARK 465 ARG A 70
REMARK 465 GLU A 71
REMARK 465 LYS A 72
REMARK 465 SER A 73
REMARK 465 ALA A 167
REMARK 465 SER A 169
REMARK 465 ALA A 181
REMARK 465 GLN A 182
REMARK 465 GLU A 183
REMARK 465 ASP A 184
REMARK 465 GLY A 185
REMARK 465 GLN A 186
REMARK 465 GLY A 287
REMARK 465 GLY A 288
REMARK 465 GLY A 289
REMARK 465 GLY A 290
REMARK 465 GLY B 65
REMARK 465 SER B 66
REMARK 465 HIS B 67
REMARK 465 MET B 68
REMARK 465 LEU B 69
REMARK 465 ARG B 70
REMARK 465 GLU B 71
REMARK 465 LYS B 72
REMARK 465 SER B 73
REMARK 465 LYS B 168
REMARK 465 SER B 169
REMARK 465 GLU B 183
REMARK 465 ASP B 184
REMARK 465 GLY B 185
REMARK 465 GLN B 186
REMARK 465 GLY B 287
REMARK 465 GLY B 288
REMARK 465 GLY B 289
REMARK 465 GLY B 290
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TYR A 94 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 95 CG CD CE NZ
REMARK 470 GLU A 130 CG CD OE1 OE2
REMARK 470 LYS A 140 CG CD CE NZ
REMARK 470 LYS A 168 CG CD CE NZ
REMARK 470 GLU A 180 CG CD OE1 OE2
REMARK 470 GLU A 190 CG CD OE1 OE2
REMARK 470 GLU A 253 CG CD OE1 OE2
REMARK 470 ASP A 262 CG OD1 OD2
REMARK 470 LYS A 269 CG CD CE NZ
REMARK 470 GLN A 273 CG CD OE1 NE2
REMARK 470 LYS A 285 CG CD CE NZ
REMARK 470 LYS A 328 CG CD CE NZ
REMARK 470 LYS B 75 CG CD CE NZ
REMARK 470 LYS B 140 CG CD CE NZ
REMARK 470 GLU B 141 CG CD OE1 OE2
REMARK 470 GLU B 157 CG CD OE1 OE2
REMARK 470 GLU B 173 CG CD OE1 OE2
REMARK 470 GLU B 180 CG CD OE1 OE2
REMARK 470 GLN B 182 CG CD OE1 NE2
REMARK 470 GLU B 190 CG CD OE1 OE2
REMARK 470 GLN B 194 CG CD OE1 NE2
REMARK 470 LYS B 285 CG CD CE NZ
REMARK 470 LYS B 328 CG CD CE NZ
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 96 59.67 -140.53
REMARK 500 ASN A 129 115.53 -170.29
REMARK 500 SER A 227 -12.68 89.72
REMARK 500 GLU A 229 175.50 173.03
REMARK 500 ASN B 96 56.38 -144.21
REMARK 500 ASN B 129 112.63 -173.32
REMARK 500 THR B 150 45.30 -106.92
REMARK 500 SER B 227 -7.57 88.05
REMARK 500 GLU B 229 178.54 173.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 ONLY FRAGMENTS OF PEG400 WERE IDENTIFIED AND IN
REMARK 600 MANY CASES SEVERAL ATOMS WERE MISSING DUE TO LACK OF
REMARK 600 ELECTRON DENSITY.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RDA A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RDA B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2FYP RELATED DB: PDB
REMARK 900 GRP94 IN COMPLEX WITH THE NOVEL HSP90 INHIBITOR RADESTER AMINE
REMARK 900 RELATED ID: 2FXS RELATED DB: PDB
REMARK 900 YEAST HSP82 IN COMPLEX WITH THE NOVEL HSP90 INHIBITOR RADAMIDE
REMARK 900 RELATED ID: 1ZWH RELATED DB: PDB
REMARK 900 YEAST HSP82 IN COMPLEX WITH THE NOVEL HSP90 INHIBITOR RADESTER AMINE
REMARK 900 RELATED ID: 1QY8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE N-DOMAIN OF THE ER HSP90 CHAPERONE GRP94
REMARK 900 IN COMPLEX WITH RADICICOL
REMARK 900 RELATED ID: 1U0Z RELATED DB: PDB
REMARK 900 N-DOMAIN OF GRP94 LACKING THE CHARGED DOMAIN IN COMPLEX WITH
REMARK 900 RADICICOL
REMARK 900 RELATED ID: 1OSF RELATED DB: PDB
REMARK 900 HUMAN HSP90 IN COMPLEX WITH 17-DESMETHOXY-17-N, N-
REMARK 900 DIMETHYLAMINOETHYLAMINO-GELDANAMYCIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE DATABASE RESIDUES 287-327 WERE DELETED
REMARK 999 AND REPLACED BY 4 GLYCINES.
DBREF 2GFD A 69 286 UNP P41148 ENPL_CANFA 69 286
DBREF 2GFD A 328 337 UNP P41148 ENPL_CANFA 328 337
DBREF 2GFD B 69 286 UNP P41148 ENPL_CANFA 69 286
DBREF 2GFD B 328 337 UNP P41148 ENPL_CANFA 328 337
SEQADV 2GFD GLY A 65 UNP P41148 CLONING ARTIFACT
SEQADV 2GFD SER A 66 UNP P41148 CLONING ARTIFACT
SEQADV 2GFD HIS A 67 UNP P41148 CLONING ARTIFACT
SEQADV 2GFD MET A 68 UNP P41148 CLONING ARTIFACT
SEQADV 2GFD GLY A 287 UNP P41148 SEE REMARK 999
SEQADV 2GFD GLY A 288 UNP P41148 SEE REMARK 999
SEQADV 2GFD GLY A 289 UNP P41148 SEE REMARK 999
SEQADV 2GFD GLY A 290 UNP P41148 SEE REMARK 999
SEQADV 2GFD GLY B 65 UNP P41148 CLONING ARTIFACT
SEQADV 2GFD SER B 66 UNP P41148 CLONING ARTIFACT
SEQADV 2GFD HIS B 67 UNP P41148 CLONING ARTIFACT
SEQADV 2GFD MET B 68 UNP P41148 CLONING ARTIFACT
SEQADV 2GFD GLY B 287 UNP P41148 SEE REMARK 999
SEQADV 2GFD GLY B 288 UNP P41148 SEE REMARK 999
SEQADV 2GFD GLY B 289 UNP P41148 SEE REMARK 999
SEQADV 2GFD GLY B 290 UNP P41148 SEE REMARK 999
SEQRES 1 A 236 GLY SER HIS MET LEU ARG GLU LYS SER GLU LYS PHE ALA
SEQRES 2 A 236 PHE GLN ALA GLU VAL ASN ARG MET MET LYS LEU ILE ILE
SEQRES 3 A 236 ASN SER LEU TYR LYS ASN LYS GLU ILE PHE LEU ARG GLU
SEQRES 4 A 236 LEU ILE SER ASN ALA SER ASP ALA LEU ASP LYS ILE ARG
SEQRES 5 A 236 LEU ILE SER LEU THR ASP GLU ASN ALA LEU ALA GLY ASN
SEQRES 6 A 236 GLU GLU LEU THR VAL LYS ILE LYS CYS ASP LYS GLU LYS
SEQRES 7 A 236 ASN LEU LEU HIS VAL THR ASP THR GLY VAL GLY MET THR
SEQRES 8 A 236 ARG GLU GLU LEU VAL LYS ASN LEU GLY THR ILE ALA LYS
SEQRES 9 A 236 SER GLY THR SER GLU PHE LEU ASN LYS MET THR GLU ALA
SEQRES 10 A 236 GLN GLU ASP GLY GLN SER THR SER GLU LEU ILE GLY GLN
SEQRES 11 A 236 PHE GLY VAL GLY PHE TYR SER ALA PHE LEU VAL ALA ASP
SEQRES 12 A 236 LYS VAL ILE VAL THR SER LYS HIS ASN ASN ASP THR GLN
SEQRES 13 A 236 HIS ILE TRP GLU SER ASP SER ASN GLU PHE SER VAL ILE
SEQRES 14 A 236 ALA ASP PRO ARG GLY ASN THR LEU GLY ARG GLY THR THR
SEQRES 15 A 236 ILE THR LEU VAL LEU LYS GLU GLU ALA SER ASP TYR LEU
SEQRES 16 A 236 GLU LEU ASP THR ILE LYS ASN LEU VAL LYS LYS TYR SER
SEQRES 17 A 236 GLN PHE ILE ASN PHE PRO ILE TYR VAL TRP SER SER LYS
SEQRES 18 A 236 THR GLY GLY GLY GLY LYS THR VAL TRP ASP TRP GLU LEU
SEQRES 19 A 236 MET ASN
SEQRES 1 B 236 GLY SER HIS MET LEU ARG GLU LYS SER GLU LYS PHE ALA
SEQRES 2 B 236 PHE GLN ALA GLU VAL ASN ARG MET MET LYS LEU ILE ILE
SEQRES 3 B 236 ASN SER LEU TYR LYS ASN LYS GLU ILE PHE LEU ARG GLU
SEQRES 4 B 236 LEU ILE SER ASN ALA SER ASP ALA LEU ASP LYS ILE ARG
SEQRES 5 B 236 LEU ILE SER LEU THR ASP GLU ASN ALA LEU ALA GLY ASN
SEQRES 6 B 236 GLU GLU LEU THR VAL LYS ILE LYS CYS ASP LYS GLU LYS
SEQRES 7 B 236 ASN LEU LEU HIS VAL THR ASP THR GLY VAL GLY MET THR
SEQRES 8 B 236 ARG GLU GLU LEU VAL LYS ASN LEU GLY THR ILE ALA LYS
SEQRES 9 B 236 SER GLY THR SER GLU PHE LEU ASN LYS MET THR GLU ALA
SEQRES 10 B 236 GLN GLU ASP GLY GLN SER THR SER GLU LEU ILE GLY GLN
SEQRES 11 B 236 PHE GLY VAL GLY PHE TYR SER ALA PHE LEU VAL ALA ASP
SEQRES 12 B 236 LYS VAL ILE VAL THR SER LYS HIS ASN ASN ASP THR GLN
SEQRES 13 B 236 HIS ILE TRP GLU SER ASP SER ASN GLU PHE SER VAL ILE
SEQRES 14 B 236 ALA ASP PRO ARG GLY ASN THR LEU GLY ARG GLY THR THR
SEQRES 15 B 236 ILE THR LEU VAL LEU LYS GLU GLU ALA SER ASP TYR LEU
SEQRES 16 B 236 GLU LEU ASP THR ILE LYS ASN LEU VAL LYS LYS TYR SER
SEQRES 17 B 236 GLN PHE ILE ASN PHE PRO ILE TYR VAL TRP SER SER LYS
SEQRES 18 B 236 THR GLY GLY GLY GLY LYS THR VAL TRP ASP TRP GLU LEU
SEQRES 19 B 236 MET ASN
HET RDA A1001 56
HET PG4 A 501 13
HET PG4 A 502 13
HET RDA B1002 56
HET PG4 B 504 13
HET PG4 B 505 13
HET 1PE B 601 16
HETNAM RDA METHYL 3-CHLORO-2-{3-[(2,5-DIHYDROXY-4-METHOXYPHENYL)
HETNAM 2 RDA AMINO]-3-OXOPROPYL}-4,6-DIHYDROXYBENZOATE
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM 1PE PENTAETHYLENE GLYCOL
HETSYN 1PE PEG400
FORMUL 3 RDA 2(C18 H18 CL N O8)
FORMUL 4 PG4 4(C8 H18 O5)
FORMUL 9 1PE C10 H22 O6
FORMUL 10 HOH *284(H2 O)
HELIX 1 1 GLN A 79 LEU A 93 1 15
HELIX 2 2 GLU A 98 ASP A 122 1 25
HELIX 3 3 ASN A 124 ASN A 129 5 6
HELIX 4 4 THR A 155 THR A 165 1 11
HELIX 5 5 GLY A 170 GLU A 180 1 11
HELIX 6 6 THR A 188 GLY A 196 1 9
HELIX 7 7 VAL A 197 LEU A 204 5 8
HELIX 8 8 GLU A 253 LEU A 259 5 7
HELIX 9 9 GLU A 260 SER A 272 1 13
HELIX 10 10 GLN B 79 TYR B 94 1 16
HELIX 11 11 GLU B 98 ASP B 122 1 25
HELIX 12 12 ASN B 124 ASN B 129 5 6
HELIX 13 13 THR B 155 THR B 165 1 11
HELIX 14 14 GLY B 170 GLN B 182 1 13
HELIX 15 15 THR B 188 GLY B 196 1 9
HELIX 16 16 VAL B 197 LEU B 204 5 8
HELIX 17 17 GLU B 253 LEU B 259 5 7
HELIX 18 18 GLU B 260 SER B 272 1 13
SHEET 1 A 9 LYS A 75 PHE A 76 0
SHEET 2 A 9 PHE A 230 ALA A 234 -1 O PHE A 230 N PHE A 76
SHEET 3 A 9 HIS A 221 SER A 225 -1 N ILE A 222 O ILE A 233
SHEET 4 A 9 ALA A 206 LYS A 214 -1 N VAL A 211 O TRP A 223
SHEET 5 A 9 GLY A 244 LEU A 251 -1 O THR A 248 N ILE A 210
SHEET 6 A 9 LEU A 144 ASP A 149 -1 N LEU A 145 O LEU A 249
SHEET 7 A 9 VAL A 134 ASP A 139 -1 N LYS A 135 O THR A 148
SHEET 8 A 9 ILE A 279 LYS A 285 1 O TYR A 280 N VAL A 134
SHEET 9 A 9 VAL A 330 LEU A 335 -1 O ASP A 332 N SER A 283
SHEET 1 B 9 LYS B 75 PHE B 76 0
SHEET 2 B 9 PHE B 230 ALA B 234 -1 O PHE B 230 N PHE B 76
SHEET 3 B 9 HIS B 221 SER B 225 -1 N ILE B 222 O ILE B 233
SHEET 4 B 9 ALA B 206 LYS B 214 -1 N VAL B 211 O TRP B 223
SHEET 5 B 9 GLY B 244 LEU B 251 -1 O THR B 248 N ILE B 210
SHEET 6 B 9 LEU B 144 ASP B 149 -1 N LEU B 145 O LEU B 249
SHEET 7 B 9 VAL B 134 ASP B 139 -1 N LYS B 135 O THR B 148
SHEET 8 B 9 ILE B 279 LYS B 285 1 O TYR B 280 N ILE B 136
SHEET 9 B 9 VAL B 330 LEU B 335 -1 O VAL B 330 N LYS B 285
SITE 1 AC1 17 ASN A 107 ALA A 111 ASP A 149 MET A 154
SITE 2 AC1 17 ASN A 162 ILE A 166 LYS A 168 GLY A 196
SITE 3 AC1 17 VAL A 197 PHE A 199 TYR A 200 THR A 245
SITE 4 AC1 17 ILE A 247 HOH A1004 HOH A1005 HOH A1007
SITE 5 AC1 17 HOH A1084
SITE 1 AC2 18 ASN B 107 ALA B 111 ASP B 149 MET B 154
SITE 2 AC2 18 ASN B 162 LEU B 163 ILE B 166 GLY B 196
SITE 3 AC2 18 VAL B 197 PHE B 199 TYR B 200 THR B 245
SITE 4 AC2 18 ILE B 247 HOH B1003 HOH B1006 HOH B1043
SITE 5 AC2 18 HOH B1093 HOH B1140
SITE 1 AC3 11 THR A 212 ARG A 237 THR A 248 PG4 A 502
SITE 2 AC3 11 HOH A1003 HOH A1029 HOH A1046 HOH A1078
SITE 3 AC3 11 HOH A1095 HOH A1101 HOH A1120
SITE 1 AC4 5 LYS A 137 HIS A 146 THR A 148 PG4 A 501
SITE 2 AC4 5 HOH A1074
SITE 1 AC5 8 THR B 212 ARG B 237 THR B 240 THR B 246
SITE 2 AC5 8 THR B 248 HOH B1032 HOH B1120 HOH B1123
SITE 1 AC6 3 LYS B 137 THR B 148 TRP B 282
SITE 1 AC7 8 ASN A 83 LYS A 87 ILE A 90 ASN B 83
SITE 2 AC7 8 LYS B 87 ILE B 90 SER B 227 HOH B1069
CRYST1 65.490 84.570 95.580 90.00 90.00 90.00 P 21 21 21 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 0.015270 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011825 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010462 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
