HEADER CHAPERONE 15-OCT-09 3K99
TITLE HSP90 N-TERMINAL DOMAIN IN COMPLEX WITH 4-(1,3-DIHYDRO-2H-ISOINDOL-2-
TITLE 2 YLCARBONYL)BENZENE-1,3-DIOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN (UNP RESIDUES 9-225);
COMPND 5 SYNONYM: HSP 86, 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 HSP90, N-TERMINAL DOMAIN, ATP BINDING DOMAIN, INHIBITION,
KEYWDS 2 ACETYLATION, ALTERNATIVE SPLICING, ATP-BINDING, CHAPERONE,
KEYWDS 3 CYTOPLASM, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, STRESS RESPONSE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.S.GAJIWALA,J.F.DAVIES II
REVDAT 2 21-FEB-24 3K99 1 REMARK SEQADV
REVDAT 1 09-FEB-10 3K99 0
JRNL AUTH P.P.KUNG,B.HUANG,G.ZHANG,J.Z.ZHOU,J.WANG,J.A.DIGITS,
JRNL AUTH 2 J.SKAPTASON,S.YAMAZAKI,D.NEUL,M.ZIENTEK,J.ELLERAAS,P.MEHTA,
JRNL AUTH 3 M.J.YIN,M.J.HICKEY,K.S.GAJIWALA,C.RODGERS,J.F.DAVIES,
JRNL AUTH 4 M.R.GEHRING
JRNL TITL DIHYDROXYPHENYLISOINDOLINE AMIDES AS ORALLY BIOAVAILABLE
JRNL TITL 2 INHIBITORS OF THE HEAT SHOCK PROTEIN 90 (HSP90) MOLECULAR
JRNL TITL 3 CHAPERONE.
JRNL REF J.MED.CHEM. V. 53 499 2010
JRNL REFN ISSN 0022-2623
JRNL PMID 19908836
JRNL DOI 10.1021/JM901209Q
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 318081.090
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 48679
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2449
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.2090
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.2070
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 2540
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0050
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 50748
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7238
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 354
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.015
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6838
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 389
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.53000
REMARK 3 B22 (A**2) : -3.50000
REMARK 3 B33 (A**2) : -2.02000
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) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 0.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.580
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) : 1.320 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.010 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.150 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.140 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.37
REMARK 3 BSOL : 45.06
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.P
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.P
REMARK 3 PARAMETER FILE 3 : WATER_REP.PAR
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : PFI.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : PFI.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3K99 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000055706.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 98
REMARK 200 PH : 4.2
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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50822
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : 0.07900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.42400
REMARK 200 R SYM FOR SHELL (I) : 0.42400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% ETHYLENE GLYCOL, 0.1 M PHOSPHATE
REMARK 280 -CITRATE, PH 4.2, 30 MM TCEP, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
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 23.38650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 109.66250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.47900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 109.66250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.38650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.47900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 -1.000000 0.000000 0.000000 93.54600
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 -41.47900
REMARK 350 BIOMT3 1 0.000000 0.000000 -1.000000 109.66250
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 46.77300
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -41.47900
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 109.66250
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 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 8
REMARK 465 GLU A 227
REMARK 465 HIS A 228
REMARK 465 HIS A 229
REMARK 465 HIS A 230
REMARK 465 HIS A 231
REMARK 465 HIS A 232
REMARK 465 HIS A 233
REMARK 465 HIS A 234
REMARK 465 HIS A 235
REMARK 465 HIS A 236
REMARK 465 HIS A 237
REMARK 465 HIS A 238
REMARK 465 HIS A 239
REMARK 465 MET B 8
REMARK 465 ASP B 9
REMARK 465 GLN B 10
REMARK 465 GLU B 227
REMARK 465 HIS B 228
REMARK 465 HIS B 229
REMARK 465 HIS B 230
REMARK 465 HIS B 231
REMARK 465 HIS B 232
REMARK 465 HIS B 233
REMARK 465 HIS B 234
REMARK 465 HIS B 235
REMARK 465 HIS B 236
REMARK 465 HIS B 237
REMARK 465 HIS B 238
REMARK 465 HIS B 239
REMARK 465 MET C 8
REMARK 465 ASP C 9
REMARK 465 GLN C 10
REMARK 465 GLU C 227
REMARK 465 HIS C 228
REMARK 465 HIS C 229
REMARK 465 HIS C 230
REMARK 465 HIS C 231
REMARK 465 HIS C 232
REMARK 465 HIS C 233
REMARK 465 HIS C 234
REMARK 465 HIS C 235
REMARK 465 HIS C 236
REMARK 465 HIS C 237
REMARK 465 HIS C 238
REMARK 465 HIS C 239
REMARK 465 MET D 8
REMARK 465 ASP D 9
REMARK 465 GLU D 227
REMARK 465 HIS D 228
REMARK 465 HIS D 229
REMARK 465 HIS D 230
REMARK 465 HIS D 231
REMARK 465 HIS D 232
REMARK 465 HIS D 233
REMARK 465 HIS D 234
REMARK 465 HIS D 235
REMARK 465 HIS D 236
REMARK 465 HIS D 237
REMARK 465 HIS D 238
REMARK 465 HIS D 239
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 ALA A 166 -142.60 71.86
REMARK 500 ARG A 182 144.69 -177.98
REMARK 500 ASN B 40 47.70 -103.05
REMARK 500 ALA B 166 -144.54 68.21
REMARK 500 ARG B 182 140.14 -172.07
REMARK 500 ALA C 166 -146.35 64.84
REMARK 500 ARG C 182 141.63 -175.71
REMARK 500 GLU D 13 138.96 -177.88
REMARK 500 ASN D 40 70.22 -106.68
REMARK 500 THR D 94 41.55 -104.64
REMARK 500 ASP D 157 -162.20 -166.70
REMARK 500 ALA D 166 -141.72 72.73
REMARK 500 ARG D 182 142.88 -173.01
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 PFT A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PFT B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PFT C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PFT D 901
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3K97 RELATED DB: PDB
REMARK 900 RELATED ID: 3K98 RELATED DB: PDB
DBREF 3K99 A 9 225 UNP P07900 HS90A_HUMAN 9 225
DBREF 3K99 B 9 225 UNP P07900 HS90A_HUMAN 9 225
DBREF 3K99 C 9 225 UNP P07900 HS90A_HUMAN 9 225
DBREF 3K99 D 9 225 UNP P07900 HS90A_HUMAN 9 225
SEQADV 3K99 MET A 8 UNP P07900 INITIATING METHIONINE
SEQADV 3K99 LEU A 226 UNP P07900 EXPRESSION TAG
SEQADV 3K99 GLU A 227 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS A 228 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS A 229 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS A 230 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS A 231 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS A 232 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS A 233 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS A 234 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS A 235 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS A 236 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS A 237 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS A 238 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS A 239 UNP P07900 EXPRESSION TAG
SEQADV 3K99 MET B 8 UNP P07900 INITIATING METHIONINE
SEQADV 3K99 LEU B 226 UNP P07900 EXPRESSION TAG
SEQADV 3K99 GLU B 227 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS B 228 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS B 229 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS B 230 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS B 231 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS B 232 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS B 233 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS B 234 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS B 235 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS B 236 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS B 237 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS B 238 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS B 239 UNP P07900 EXPRESSION TAG
SEQADV 3K99 MET C 8 UNP P07900 INITIATING METHIONINE
SEQADV 3K99 LEU C 226 UNP P07900 EXPRESSION TAG
SEQADV 3K99 GLU C 227 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS C 228 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS C 229 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS C 230 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS C 231 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS C 232 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS C 233 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS C 234 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS C 235 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS C 236 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS C 237 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS C 238 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS C 239 UNP P07900 EXPRESSION TAG
SEQADV 3K99 MET D 8 UNP P07900 INITIATING METHIONINE
SEQADV 3K99 LEU D 226 UNP P07900 EXPRESSION TAG
SEQADV 3K99 GLU D 227 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS D 228 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS D 229 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS D 230 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS D 231 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS D 232 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS D 233 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS D 234 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS D 235 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS D 236 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS D 237 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS D 238 UNP P07900 EXPRESSION TAG
SEQADV 3K99 HIS D 239 UNP P07900 EXPRESSION TAG
SEQRES 1 A 232 MET ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE
SEQRES 2 A 232 ALA PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE
SEQRES 3 A 232 ILE ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG
SEQRES 4 A 232 GLU LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE
SEQRES 5 A 232 ARG TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER
SEQRES 6 A 232 GLY LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN
SEQRES 7 A 232 ASP ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET
SEQRES 8 A 232 THR LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE ALA
SEQRES 9 A 232 LYS SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA
SEQRES 10 A 232 GLY ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY
SEQRES 11 A 232 PHE TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL
SEQRES 12 A 232 ILE THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU
SEQRES 13 A 232 SER SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR
SEQRES 14 A 232 GLY GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS
SEQRES 15 A 232 LEU LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG
SEQRES 16 A 232 ILE LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY
SEQRES 17 A 232 TYR PRO ILE THR LEU PHE VAL GLU LYS GLU LEU GLU HIS
SEQRES 18 A 232 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 232 MET ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE
SEQRES 2 B 232 ALA PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE
SEQRES 3 B 232 ILE ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG
SEQRES 4 B 232 GLU LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE
SEQRES 5 B 232 ARG TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER
SEQRES 6 B 232 GLY LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN
SEQRES 7 B 232 ASP ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET
SEQRES 8 B 232 THR LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE ALA
SEQRES 9 B 232 LYS SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA
SEQRES 10 B 232 GLY ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY
SEQRES 11 B 232 PHE TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL
SEQRES 12 B 232 ILE THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU
SEQRES 13 B 232 SER SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR
SEQRES 14 B 232 GLY GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS
SEQRES 15 B 232 LEU LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG
SEQRES 16 B 232 ILE LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY
SEQRES 17 B 232 TYR PRO ILE THR LEU PHE VAL GLU LYS GLU LEU GLU HIS
SEQRES 18 B 232 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 C 232 MET ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE
SEQRES 2 C 232 ALA PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE
SEQRES 3 C 232 ILE ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG
SEQRES 4 C 232 GLU LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE
SEQRES 5 C 232 ARG TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER
SEQRES 6 C 232 GLY LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN
SEQRES 7 C 232 ASP ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET
SEQRES 8 C 232 THR LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE ALA
SEQRES 9 C 232 LYS SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA
SEQRES 10 C 232 GLY ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY
SEQRES 11 C 232 PHE TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL
SEQRES 12 C 232 ILE THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU
SEQRES 13 C 232 SER SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR
SEQRES 14 C 232 GLY GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS
SEQRES 15 C 232 LEU LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG
SEQRES 16 C 232 ILE LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY
SEQRES 17 C 232 TYR PRO ILE THR LEU PHE VAL GLU LYS GLU LEU GLU HIS
SEQRES 18 C 232 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 D 232 MET ASP GLN PRO MET GLU GLU GLU GLU VAL GLU THR PHE
SEQRES 2 D 232 ALA PHE GLN ALA GLU ILE ALA GLN LEU MET SER LEU ILE
SEQRES 3 D 232 ILE ASN THR PHE TYR SER ASN LYS GLU ILE PHE LEU ARG
SEQRES 4 D 232 GLU LEU ILE SER ASN SER SER ASP ALA LEU ASP LYS ILE
SEQRES 5 D 232 ARG TYR GLU SER LEU THR ASP PRO SER LYS LEU ASP SER
SEQRES 6 D 232 GLY LYS GLU LEU HIS ILE ASN LEU ILE PRO ASN LYS GLN
SEQRES 7 D 232 ASP ARG THR LEU THR ILE VAL ASP THR GLY ILE GLY MET
SEQRES 8 D 232 THR LYS ALA ASP LEU ILE ASN ASN LEU GLY THR ILE ALA
SEQRES 9 D 232 LYS SER GLY THR LYS ALA PHE MET GLU ALA LEU GLN ALA
SEQRES 10 D 232 GLY ALA ASP ILE SER MET ILE GLY GLN PHE GLY VAL GLY
SEQRES 11 D 232 PHE TYR SER ALA TYR LEU VAL ALA GLU LYS VAL THR VAL
SEQRES 12 D 232 ILE THR LYS HIS ASN ASP ASP GLU GLN TYR ALA TRP GLU
SEQRES 13 D 232 SER SER ALA GLY GLY SER PHE THR VAL ARG THR ASP THR
SEQRES 14 D 232 GLY GLU PRO MET GLY ARG GLY THR LYS VAL ILE LEU HIS
SEQRES 15 D 232 LEU LYS GLU ASP GLN THR GLU TYR LEU GLU GLU ARG ARG
SEQRES 16 D 232 ILE LYS GLU ILE VAL LYS LYS HIS SER GLN PHE ILE GLY
SEQRES 17 D 232 TYR PRO ILE THR LEU PHE VAL GLU LYS GLU LEU GLU HIS
SEQRES 18 D 232 HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
HET PFT A 901 19
HET PFT B 901 19
HET PFT C 901 19
HET PFT D 901 19
HETNAM PFT 4-(1,3-DIHYDRO-2H-ISOINDOL-2-YLCARBONYL)BENZENE-1,3-
HETNAM 2 PFT DIOL
FORMUL 5 PFT 4(C15 H13 N O3)
FORMUL 9 HOH *389(H2 O)
HELIX 1 1 GLN A 23 THR A 36 1 14
HELIX 2 2 GLU A 42 ASP A 66 1 25
HELIX 3 3 PRO A 67 ASP A 71 5 5
HELIX 4 4 THR A 99 ASN A 105 1 7
HELIX 5 5 GLY A 114 ALA A 124 1 11
HELIX 6 6 ILE A 128 GLY A 135 5 8
HELIX 7 7 VAL A 136 LEU A 143 5 8
HELIX 8 8 GLU A 192 LEU A 198 5 7
HELIX 9 9 GLU A 199 SER A 211 1 13
HELIX 10 10 GLN B 23 THR B 36 1 14
HELIX 11 11 GLU B 42 LEU B 64 1 23
HELIX 12 12 THR B 65 GLY B 73 5 9
HELIX 13 13 THR B 99 LEU B 107 1 9
HELIX 14 14 GLY B 114 GLN B 123 1 10
HELIX 15 15 ASP B 127 GLY B 135 5 9
HELIX 16 16 VAL B 136 LEU B 143 5 8
HELIX 17 17 GLU B 192 LEU B 198 5 7
HELIX 18 18 GLU B 199 SER B 211 1 13
HELIX 19 19 GLN C 23 ASN C 35 1 13
HELIX 20 20 GLU C 42 ASP C 66 1 25
HELIX 21 21 PRO C 67 GLY C 73 5 7
HELIX 22 22 THR C 99 LEU C 107 1 9
HELIX 23 23 GLY C 114 GLY C 125 1 12
HELIX 24 24 ASP C 127 GLY C 135 5 9
HELIX 25 25 VAL C 136 LEU C 143 5 8
HELIX 26 26 GLU C 192 LEU C 198 5 7
HELIX 27 27 GLU C 199 SER C 211 1 13
HELIX 28 28 GLN D 23 THR D 36 1 14
HELIX 29 29 GLU D 42 ASP D 66 1 25
HELIX 30 30 PRO D 67 ASP D 71 5 5
HELIX 31 31 THR D 99 ASN D 105 1 7
HELIX 32 32 GLY D 114 ALA D 124 1 11
HELIX 33 33 ASP D 127 GLY D 135 5 9
HELIX 34 34 VAL D 136 LEU D 143 5 8
HELIX 35 35 GLU D 192 LEU D 198 5 7
HELIX 36 36 GLU D 199 SER D 211 1 13
SHEET 1 A16 ILE A 218 LEU A 220 0
SHEET 2 A16 ILE A 78 ASN A 83 1 N LEU A 80 O THR A 219
SHEET 3 A16 THR A 88 ASP A 93 -1 O VAL A 92 N ASN A 79
SHEET 4 A16 GLY A 183 LEU A 190 -1 O VAL A 186 N ILE A 91
SHEET 5 A16 ALA A 145 LYS A 153 -1 N ILE A 151 O LYS A 185
SHEET 6 A16 TYR A 160 SER A 164 -1 O TRP A 162 N VAL A 150
SHEET 7 A16 SER A 169 THR A 174 -1 O ARG A 173 N ALA A 161
SHEET 8 A16 GLU A 13 ALA A 21 -1 N PHE A 20 O PHE A 170
SHEET 9 A16 GLU C 13 ALA C 21 -1 O THR C 19 N GLU A 13
SHEET 10 A16 SER C 169 THR C 174 -1 O PHE C 170 N PHE C 20
SHEET 11 A16 GLN C 159 SER C 164 -1 N GLU C 163 O THR C 171
SHEET 12 A16 ALA C 145 LYS C 153 -1 N VAL C 150 O TRP C 162
SHEET 13 A16 GLY C 183 LEU C 190 -1 O ILE C 187 N THR C 149
SHEET 14 A16 THR C 88 ASP C 93 -1 N ILE C 91 O VAL C 186
SHEET 15 A16 ILE C 78 ASN C 83 -1 N ASN C 79 O VAL C 92
SHEET 16 A16 ILE C 218 LEU C 220 1 O THR C 219 N LEU C 80
SHEET 1 B16 VAL B 17 ALA B 21 0
SHEET 2 B16 SER B 169 THR B 174 -1 O PHE B 170 N PHE B 20
SHEET 3 B16 GLN B 159 SER B 164 -1 N ALA B 161 O ARG B 173
SHEET 4 B16 ALA B 145 LYS B 153 -1 N VAL B 150 O TRP B 162
SHEET 5 B16 GLY B 183 LEU B 190 -1 O ILE B 187 N THR B 149
SHEET 6 B16 THR B 88 ASP B 93 -1 N ILE B 91 O VAL B 186
SHEET 7 B16 ILE B 78 ASN B 83 -1 N ASN B 79 O VAL B 92
SHEET 8 B16 ILE B 218 GLU B 225 1 O THR B 219 N LEU B 80
SHEET 9 B16 ILE D 218 GLU D 225 -1 O LYS D 224 N LEU B 220
SHEET 10 B16 ILE D 78 ASN D 83 1 N LEU D 80 O THR D 219
SHEET 11 B16 THR D 88 ASP D 93 -1 O THR D 88 N ASN D 83
SHEET 12 B16 GLY D 183 LEU D 190 -1 O VAL D 186 N ILE D 91
SHEET 13 B16 ALA D 145 LYS D 153 -1 N THR D 149 O ILE D 187
SHEET 14 B16 GLN D 159 SER D 164 -1 O TRP D 162 N VAL D 150
SHEET 15 B16 SER D 169 THR D 174 -1 O ARG D 173 N ALA D 161
SHEET 16 B16 VAL D 17 ALA D 21 -1 N PHE D 20 O PHE D 170
SITE 1 AC1 8 ASN A 51 ALA A 55 ASP A 93 ILE A 96
SITE 2 AC1 8 MET A 98 LEU A 107 THR A 184 HOH A 240
SITE 1 AC2 11 HOH B 4 ASN B 51 ASP B 54 ALA B 55
SITE 2 AC2 11 LYS B 58 ASP B 93 ILE B 96 GLY B 97
SITE 3 AC2 11 MET B 98 THR B 184 VAL B 186
SITE 1 AC3 9 ASN C 51 ALA C 55 ASP C 93 ILE C 96
SITE 2 AC3 9 GLY C 97 MET C 98 THR C 184 VAL C 186
SITE 3 AC3 9 HOH C 241
SITE 1 AC4 10 HOH D 2 LEU D 48 ASN D 51 ALA D 55
SITE 2 AC4 10 ASP D 93 GLY D 97 MET D 98 THR D 184
SITE 3 AC4 10 VAL D 186 HOH D 242
CRYST1 46.773 82.958 219.325 90.00 90.00 90.00 P 21 21 21 16
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 0.021380 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012054 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004559 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
