HEADER CHAPERONE 02-MAR-04 1UY7
TITLE HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(4-METHOXY-BENZYL)-9H-PURIN-6-YLAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 1-235;
COMPND 5 SYNONYM: HSP 86;
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 ORGAN: SKIN;
SOURCE 6 TISSUE: MELANOMA;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET19;
SOURCE 11 OTHER_DETAILS: CLONED FROM IMAGE\:4026275
KEYWDS HSP90, ATPASE, PU4, CHAPERONE, ATP-BINDING, HEAT SHOCK
EXPDTA X-RAY DIFFRACTION
AUTHOR L.WRIGHT,X.BARRIL,B.DYMOCK,L.SHERIDAN,A.SURGENOR,M.BESWICK,
AUTHOR 2 M.DRYSDALE,A.COLLIER,A.MASSEY,N.DAVIES,A.FINK,C.FROMONT,W.AHERNE,
AUTHOR 3 K.BOXALL,S.SHARP,P.WORKMAN,R.E.HUBBARD
REVDAT 3 13-DEC-23 1UY7 1 REMARK
REVDAT 2 24-FEB-09 1UY7 1 VERSN
REVDAT 1 01-JUL-04 1UY7 0
JRNL AUTH L.WRIGHT,X.BARRIL,B.DYMOCK,L.SHERIDAN,A.SURGENOR,M.BESWICK,
JRNL AUTH 2 M.DRYSDALE,A.COLLIER,A.MASSEY,N.DAVIES,A.FINK,C.FROMONT,
JRNL AUTH 3 W.AHERNE,K.BOXALL,S.SHARP,P.WORKMAN,R.E.HUBBARD
JRNL TITL STRUCTURE-ACTIVITY RELATIONSHIPS IN PURINE-BASED INHIBITOR
JRNL TITL 2 BINDING TO HSP90 ISOFORMS
JRNL REF CHEM.BIOL. V. 11 775 2004
JRNL REFN ISSN 1074-5521
JRNL PMID 15217611
JRNL DOI 10.1016/J.CHEMBIOL.2004.03.033
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 22464
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1211
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1550
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3290
REMARK 3 BIN FREE R VALUE SET COUNT : 85
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1636
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 269
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.31000
REMARK 3 B22 (A**2) : 0.58000
REMARK 3 B33 (A**2) : -0.27000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.130
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.271
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1697 ; 0.027 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2289 ; 2.392 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 207 ; 5.569 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 319 ;15.400 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 260 ; 0.157 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1253 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 827 ; 0.236 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 242 ; 0.252 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 34 ; 0.268 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.840 ; 0.500
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1029 ; 1.353 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1666 ; 2.330 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 668 ; 3.716 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 623 ; 5.937 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. RESIDUE GLU A223 WAS THE LAST RESIDUE THAT WAS
REMARK 3 VISIBLE IN ELECTRON DENSITY.
REMARK 4
REMARK 4 1UY7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1290014610.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC BLUE MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23950
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.30300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.000
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 1YER
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG MME 2000, 0.1M NA CACODYLATE,
REMARK 280 PH6.5, 0.2M MGCL2., PH 6.50
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 33.35400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.33700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 49.25550
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.35400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.33700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 49.25550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.35400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.33700
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 49.25550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.35400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 45.33700
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 49.25550
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 MOLECULAR CHAPERONE HAS ATPASE ACTIVITY
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 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 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 LYS A 224 CA C O CB CG CD CE
REMARK 470 LYS A 224 NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU A 120 O HOH A 2154 2.10
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 O HOH A 2014 O HOH A 2120 3555 0.00
REMARK 500 O HOH A 2015 O HOH A 2118 3555 0.56
REMARK 500 O HOH A 2016 O HOH A 2016 3555 0.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LYS A 191 CE LYS A 191 NZ 0.180
REMARK 500 TYR A 216 CD1 TYR A 216 CE1 -0.109
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ALA A 124 N - CA - C ANGL. DEV. = -25.4 DEGREES
REMARK 500 ASP A 175 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 LYS A 191 CD - CE - NZ ANGL. DEV. = 17.0 DEGREES
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 TYR A 38 112.84 -161.70
REMARK 500 LEU A 122 -3.83 -50.86
REMARK 500 ALA A 124 1.98 123.18
REMARK 500 ALA A 166 -150.69 64.62
REMARK 500 ARG A 182 132.49 -177.92
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 A2013 DISTANCE = 6.69 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PU4 A1224
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BYQ RELATED DB: PDB
REMARK 900 HSP90 N-TERMINAL DOMAIN BOUND TO ADP-MG
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 900 RELATED ID: 1YER RELATED DB: PDB
REMARK 900 HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "CLOSED" CONFORMATION
REMARK 900 RELATED ID: 1YES RELATED DB: PDB
REMARK 900 HUMAN HSP90 GELDANAMYCIN-BINDING DOMAIN, "OPEN" CONFORMATION
REMARK 900 RELATED ID: 1YET RELATED DB: PDB
REMARK 900 GELDANAMYCIN BOUND TO THE HSP90 GELDANAMYCIN- BINDING DOMAIN
REMARK 900 RELATED ID: 1UY6 RELATED DB: PDB
REMARK 900 HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(3,4,5-TRIMETHOXY-BENZYL)-9H-PURIN-
REMARK 900 6-YLAMINE
REMARK 900 RELATED ID: 1UY8 RELATED DB: PDB
REMARK 900 HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(3-TRIMETHOXY-BENZYL)-9H-PURIN-
REMARK 900 6YLAMINE
REMARK 900 RELATED ID: 1UY9 RELATED DB: PDB
REMARK 900 HUMAN HSP90-ALPHA WITH 8-BENZO[1,3]DIOXOL-,5-YLMETHYL-9-BUTYL- 9H-
REMARK 900 PURIN-6-YLAMINE
REMARK 900 RELATED ID: 1UYC RELATED DB: PDB
REMARK 900 HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(2,5-DIMETHOXY-BENZYL)-9H-PURIN-6-
REMARK 900 YLAMINE
REMARK 900 RELATED ID: 1UYD RELATED DB: PDB
REMARK 900 HUMAN HSP90-ALPHA WITH 9-BUTYL-8- (2-CHLORO-3,4,5-TRIMETHOXY-BENZYL)
REMARK 900 -9H-PURIN-6-YLAMINE
REMARK 900 RELATED ID: 1UYE RELATED DB: PDB
REMARK 900 HUMAN HSP90-ALPHA WITH 8-(2-CHLORO-3,4,5-TRIMETHOXY-BENZYL) -9-PENT-
REMARK 900 4-YLNYL-9H-PURIN-6-YLAMINE
REMARK 900 RELATED ID: 1UYF RELATED DB: PDB
REMARK 900 HUMAN HSP90-ALPHA WITH 8-(2-CHLORO-3,4,5-TRIMETHOXY-BENZYL) -2-
REMARK 900 FLUORO-9-PENT-4-YLNYL-9H-PURIN-6-YLAMINE
REMARK 900 RELATED ID: 1UYG RELATED DB: PDB
REMARK 900 HUMAN HSP90-ALPHA WITH 8-(2,5-DIMETHOXY-BENZYL)-2-FLUORO-9H-PURIN-6-
REMARK 900 YLAMINE
REMARK 900 RELATED ID: 1UYH RELATED DB: PDB
REMARK 900 HUMAN HSP90-ALPHA WITH 9-BUTYL-8-(2,5-DIMETHOXY-BENZYL)-2- FLUORO-
REMARK 900 9H-PURIN-6-YLAMINE
REMARK 900 RELATED ID: 1UYI RELATED DB: PDB
REMARK 900 HUMAN HSP90-ALPHA WITH 8-(2,5-DIMETHOXY-BENZYL)-2-FLUORO-9- PENT-9H-
REMARK 900 PURIN-6-YLAMINE
REMARK 900 RELATED ID: 1UYK RELATED DB: PDB
REMARK 900 HUMAN HSP90-ALPHA WITH 8-BENZO[1,3]DIOXOL-,5-YLMETHYL-9-BUTYL -2-
REMARK 900 FLUORO-9H-PURIN-6-YLAMINE
REMARK 900 RELATED ID: 1UYL RELATED DB: PDB
REMARK 900 STRUCTURE-ACTIVITY RELATIONSHIPS IN PURINE-BASED INHIBITOR BINDING
REMARK 900 TO HSP90 ISOFORMS
REMARK 900 RELATED ID: 1UYM RELATED DB: PDB
REMARK 900 HUMAN HSP90-BETA WITH PU3 (9-BUTYL-8(3,4,5-TRIMETHOXY-BENZYL)-9H-
REMARK 900 PURIN-6-YLAMINE)
DBREF 1UY7 A 1 1 PDB 1UY7 1UY7 1 1
DBREF 1UY7 A 2 236 UNP P07900 HS9A_HUMAN 1 235
SEQADV 1UY7 SER A 63 UNP P07900 THR 62 CONFLICT
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 PU4 A1224 23
HETNAM PU4 9-BUTYL-8-(4-METHOXYBENZYL)-9H-PURIN-6-AMINE
FORMUL 2 PU4 C17 H21 N5 O
FORMUL 3 HOH *269(H2 O)
HELIX 1 1 GLN A 23 THR A 36 1 14
HELIX 2 2 ASN A 40 GLU A 42 5 3
HELIX 3 3 ILE A 43 ASP A 66 1 24
HELIX 4 4 PRO A 67 ASP A 71 5 5
HELIX 5 5 THR A 99 ASN A 105 1 7
HELIX 6 6 ASN A 105 LEU A 122 1 18
HELIX 7 7 ASP A 127 GLY A 135 5 9
HELIX 8 8 VAL A 136 LEU A 143 5 8
HELIX 9 9 GLU A 192 LEU A 198 5 7
HELIX 10 10 GLU A 199 SER A 211 1 13
SHEET 1 AA 8 GLU A 18 ALA A 21 0
SHEET 2 AA 8 SER A 169 THR A 174 -1 O PHE A 170 N PHE A 20
SHEET 3 AA 8 TYR A 160 SER A 164 -1 O ALA A 161 N ARG A 173
SHEET 4 AA 8 ALA A 145 LYS A 153 -1 O VAL A 148 N SER A 164
SHEET 5 AA 8 GLY A 183 LEU A 190 -1 O GLY A 183 N LYS A 153
SHEET 6 AA 8 THR A 88 ASP A 93 -1 O LEU A 89 N LEU A 188
SHEET 7 AA 8 ILE A 78 ASN A 83 -1 O ASN A 79 N VAL A 92
SHEET 8 AA 8 ILE A 218 LEU A 220 1 O THR A 219 N LEU A 80
SITE 1 AC1 12 ASN A 51 ALA A 55 ASP A 93 MET A 98
SITE 2 AC1 12 LEU A 107 PHE A 138 TRP A 162 THR A 184
SITE 3 AC1 12 HOH A2138 HOH A2174 HOH A2268 HOH A2269
CRYST1 66.708 90.674 98.511 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 0.014991 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011028 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010151 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
