HEADER CHAPERONE 26-JAN-09 3FZF
TITLE CRYSTAL STRUCTURE OF HSC70/BAG1 IN COMPLEX WITH ATP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK COGNATE 71 KDA PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 4-381;
COMPND 5 SYNONYM: HEAT SHOCK 70 KDA PROTEIN 8;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BAG FAMILY MOLECULAR CHAPERONE REGULATOR 1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 222-334;
COMPND 11 SYNONYM: BAG-1, BCL-2-ASSOCIATED ATHANOGENE 1, GLUCOCORTICOID
COMPND 12 RECEPTOR-ASSOCIATED PROTEIN RAP46;
COMPND 13 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: HSPA8, HSC70, HSP73, HSPA10;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET101;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: BAG1, HAP;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS HSP70, HSC70, BAG1, HEAT SHOCK, CHAPERONE, PROTEIN FOLDING,
KEYWDS 2 ADENOSINE, NUCLEOSIDE, NUCLEOTIDE EXCHANGE FACTOR, SMALL MOLECULE
KEYWDS 3 INHIBITOR, ATP-BINDING, NUCLEOTIDE-BINDING, STRESS RESPONSE,
KEYWDS 4 APOPTOSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR P.DOKURNO,D.S.WILLIAMSON,J.B.MURRAY,A.E.SURGENOR
REVDAT 3 01-NOV-23 3FZF 1 REMARK SEQADV
REVDAT 2 31-MAR-09 3FZF 1 JRNL
REVDAT 1 17-MAR-09 3FZF 0
JRNL AUTH D.S.WILLIAMSON,J.BORGOGNONI,A.CLAY,Z.DANIELS,P.DOKURNO,
JRNL AUTH 2 M.J.DRYSDALE,N.FOLOPPE,G.L.FRANCIS,C.J.GRAHAM,R.HOWES,
JRNL AUTH 3 A.T.MACIAS,J.B.MURRAY,R.PARSONS,T.SHAW,A.E.SURGENOR,L.TERRY,
JRNL AUTH 4 Y.WANG,M.WOOD,A.J.MASSEY
JRNL TITL NOVEL ADENOSINE-DERIVED INHIBITORS OF 70 KDA HEAT SHOCK
JRNL TITL 2 PROTEIN, DISCOVERED THROUGH STRUCTURE-BASED DESIGN
JRNL REF J.MED.CHEM. V. 52 1510 2009
JRNL REFN ISSN 0022-2623
JRNL PMID 19256508
JRNL DOI 10.1021/JM801627A
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 22350
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1859
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1615
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE SET COUNT : 128
REMARK 3 BIN FREE R VALUE : 0.3870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3798
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 292
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.43000
REMARK 3 B22 (A**2) : -1.48000
REMARK 3 B33 (A**2) : 3.23000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.22000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.382
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.285
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.243
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.215
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.906
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3884 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5244 ; 1.648 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 486 ; 6.356 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 178 ;38.497 ;24.888
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 713 ;19.157 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;20.948 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 603 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2869 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1882 ; 0.234 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2667 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 299 ; 0.188 ; 0.200
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): 55 ; 0.234 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.199 ; 0.200
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): 2498 ; 0.753 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3899 ; 1.293 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1547 ; 2.081 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1345 ; 3.356 ; 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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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
REMARK 4
REMARK 4 3FZF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000051229.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-AUG-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32145
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 24.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.96
REMARK 200 R MERGE FOR SHELL (I) : 0.53900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
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 1HX1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG3350, 0.1M TRIS BUFFER, 25MM
REMARK 280 SODIUM-POTASSIUM TARTRATE, PH8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 60.56150
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 TYR A 1
REMARK 465 PHE A 2
REMARK 465 GLN A 3
REMARK 465 GLY A 4
REMARK 465 GLU B 261
REMARK 465 THR B 262
REMARK 465 GLU B 263
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 HIS A 227 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 357 CG CD CE NZ
REMARK 470 GLU A 358 CG CD OE1 OE2
REMARK 470 LYS B 231 CG CD CE NZ
REMARK 470 ASN B 257 CG OD1 ND2
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 GLU A 117 CG GLU A 117 CD 0.094
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 LEU A 349 CA - CB - CG ANGL. DEV. = 17.9 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 ASN A 62 55.33 -155.97
REMARK 500 THR A 140 -42.82 -132.88
REMARK 500 PHE A 354 51.89 -102.08
REMARK 500 ASN A 355 116.37 -37.94
REMARK 500 LYS A 361 1.29 -151.57
REMARK 500 ASN B 151 128.68 -39.68
REMARK 500 GLN B 188 -0.38 -59.72
REMARK 500 PHE B 190 -72.94 -119.17
REMARK 500 GLN B 256 92.55 -65.69
REMARK 500 ASN B 257 -50.83 157.74
REMARK 500 CYS B 259 82.09 59.60
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 ATP A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FZH RELATED DB: PDB
REMARK 900 RELATED ID: 3FZK RELATED DB: PDB
REMARK 900 RELATED ID: 3FZL RELATED DB: PDB
REMARK 900 RELATED ID: 3FZM RELATED DB: PDB
DBREF 3FZF A 4 381 UNP P11142 HSP7C_HUMAN 4 381
DBREF 3FZF B 151 263 UNP Q99933 BAG1_HUMAN 222 334
SEQADV 3FZF TYR A 1 UNP P11142 EXPRESSION TAG
SEQADV 3FZF PHE A 2 UNP P11142 EXPRESSION TAG
SEQADV 3FZF GLN A 3 UNP P11142 EXPRESSION TAG
SEQADV 3FZF GLY B 150 UNP Q99933 EXPRESSION TAG
SEQRES 1 A 381 TYR PHE GLN GLY PRO ALA VAL GLY ILE ASP LEU GLY THR
SEQRES 2 A 381 THR TYR SER CYS VAL GLY VAL PHE GLN HIS GLY LYS VAL
SEQRES 3 A 381 GLU ILE ILE ALA ASN ASP GLN GLY ASN ARG THR THR PRO
SEQRES 4 A 381 SER TYR VAL ALA PHE THR ASP THR GLU ARG LEU ILE GLY
SEQRES 5 A 381 ASP ALA ALA LYS ASN GLN VAL ALA MET ASN PRO THR ASN
SEQRES 6 A 381 THR VAL PHE ASP ALA LYS ARG LEU ILE GLY ARG ARG PHE
SEQRES 7 A 381 ASP ASP ALA VAL VAL GLN SER ASP MET LYS HIS TRP PRO
SEQRES 8 A 381 PHE MET VAL VAL ASN ASP ALA GLY ARG PRO LYS VAL GLN
SEQRES 9 A 381 VAL GLU TYR LYS GLY GLU THR LYS SER PHE TYR PRO GLU
SEQRES 10 A 381 GLU VAL SER SER MET VAL LEU THR LYS MET LYS GLU ILE
SEQRES 11 A 381 ALA GLU ALA TYR LEU GLY LYS THR VAL THR ASN ALA VAL
SEQRES 12 A 381 VAL THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG GLN
SEQRES 13 A 381 ALA THR LYS ASP ALA GLY THR ILE ALA GLY LEU ASN VAL
SEQRES 14 A 381 LEU ARG ILE ILE ASN GLU PRO THR ALA ALA ALA ILE ALA
SEQRES 15 A 381 TYR GLY LEU ASP LYS LYS VAL GLY ALA GLU ARG ASN VAL
SEQRES 16 A 381 LEU ILE PHE ASP LEU GLY GLY GLY THR PHE ASP VAL SER
SEQRES 17 A 381 ILE LEU THR ILE GLU ASP GLY ILE PHE GLU VAL LYS SER
SEQRES 18 A 381 THR ALA GLY ASP THR HIS LEU GLY GLY GLU ASP PHE ASP
SEQRES 19 A 381 ASN ARG MET VAL ASN HIS PHE ILE ALA GLU PHE LYS ARG
SEQRES 20 A 381 LYS HIS LYS LYS ASP ILE SER GLU ASN LYS ARG ALA VAL
SEQRES 21 A 381 ARG ARG LEU ARG THR ALA CYS GLU ARG ALA LYS ARG THR
SEQRES 22 A 381 LEU SER SER SER THR GLN ALA SER ILE GLU ILE ASP SER
SEQRES 23 A 381 LEU TYR GLU GLY ILE ASP PHE TYR THR SER ILE THR ARG
SEQRES 24 A 381 ALA ARG PHE GLU GLU LEU ASN ALA ASP LEU PHE ARG GLY
SEQRES 25 A 381 THR LEU ASP PRO VAL GLU LYS ALA LEU ARG ASP ALA LYS
SEQRES 26 A 381 LEU ASP LYS SER GLN ILE HIS ASP ILE VAL LEU VAL GLY
SEQRES 27 A 381 GLY SER THR ARG ILE PRO LYS ILE GLN LYS LEU LEU GLN
SEQRES 28 A 381 ASP PHE PHE ASN GLY LYS GLU LEU ASN LYS SER ILE ASN
SEQRES 29 A 381 PRO ASP GLU ALA VAL ALA TYR GLY ALA ALA VAL GLN ALA
SEQRES 30 A 381 ALA ILE LEU SER
SEQRES 1 B 114 GLY ASN SER PRO GLN GLU GLU VAL GLU LEU LYS LYS LEU
SEQRES 2 B 114 LYS HIS LEU GLU LYS SER VAL GLU LYS ILE ALA ASP GLN
SEQRES 3 B 114 LEU GLU GLU LEU ASN LYS GLU LEU THR GLY ILE GLN GLN
SEQRES 4 B 114 GLY PHE LEU PRO LYS ASP LEU GLN ALA GLU ALA LEU CYS
SEQRES 5 B 114 LYS LEU ASP ARG ARG VAL LYS ALA THR ILE GLU GLN PHE
SEQRES 6 B 114 MET LYS ILE LEU GLU GLU ILE ASP THR LEU ILE LEU PRO
SEQRES 7 B 114 GLU ASN PHE LYS ASP SER ARG LEU LYS ARG LYS GLY LEU
SEQRES 8 B 114 VAL LYS LYS VAL GLN ALA PHE LEU ALA GLU CYS ASP THR
SEQRES 9 B 114 VAL GLU GLN ASN ILE CYS GLN GLU THR GLU
HET ATP A 401 31
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 ATP C10 H16 N5 O13 P3
FORMUL 4 HOH *292(H2 O)
HELIX 1 1 GLY A 52 ASN A 57 1 6
HELIX 2 2 ASN A 62 THR A 64 5 3
HELIX 3 3 ASP A 69 LEU A 73 5 5
HELIX 4 4 ASP A 80 LYS A 88 1 9
HELIX 5 5 TYR A 115 GLY A 136 1 22
HELIX 6 6 ASN A 151 ALA A 165 1 15
HELIX 7 7 GLU A 175 TYR A 183 1 9
HELIX 8 8 GLY A 184 LYS A 188 5 5
HELIX 9 9 GLY A 229 LYS A 250 1 22
HELIX 10 10 ASP A 252 GLU A 255 5 4
HELIX 11 11 ASN A 256 SER A 275 1 20
HELIX 12 12 ARG A 299 ASN A 306 1 8
HELIX 13 13 ASN A 306 THR A 313 1 8
HELIX 14 14 LEU A 314 ALA A 324 1 11
HELIX 15 15 ASP A 327 SER A 329 5 3
HELIX 16 16 GLY A 338 ARG A 342 5 5
HELIX 17 17 ILE A 343 PHE A 354 1 12
HELIX 18 18 GLU A 367 SER A 381 1 15
HELIX 19 19 SER B 152 GLN B 188 1 37
HELIX 20 20 PRO B 192 ASP B 222 1 31
HELIX 21 21 PHE B 230 GLN B 256 1 27
SHEET 1 A 3 LYS A 25 ILE A 28 0
SHEET 2 A 3 TYR A 15 GLN A 22 -1 N VAL A 20 O GLU A 27
SHEET 3 A 3 THR A 38 PRO A 39 -1 O THR A 38 N SER A 16
SHEET 1 B 5 LYS A 25 ILE A 28 0
SHEET 2 B 5 TYR A 15 GLN A 22 -1 N VAL A 20 O GLU A 27
SHEET 3 B 5 ALA A 6 ASP A 10 -1 N ASP A 10 O CYS A 17
SHEET 4 B 5 ASN A 141 VAL A 146 1 O VAL A 143 N ILE A 9
SHEET 5 B 5 ASN A 168 ASN A 174 1 O LEU A 170 N ALA A 142
SHEET 1 C 3 ARG A 49 ILE A 51 0
SHEET 2 C 3 VAL A 42 PHE A 44 -1 N ALA A 43 O LEU A 50
SHEET 3 C 3 THR A 66 VAL A 67 -1 O VAL A 67 N VAL A 42
SHEET 1 D 3 MET A 93 ASP A 97 0
SHEET 2 D 3 ARG A 100 TYR A 107 -1 O ARG A 100 N ASP A 97
SHEET 3 D 3 GLU A 110 PHE A 114 -1 O GLU A 110 N TYR A 107
SHEET 1 E 5 ILE A 216 GLY A 224 0
SHEET 2 E 5 PHE A 205 GLU A 213 -1 N THR A 211 O GLU A 218
SHEET 3 E 5 ARG A 193 LEU A 200 -1 N ILE A 197 O SER A 208
SHEET 4 E 5 ILE A 331 VAL A 337 1 O ASP A 333 N LEU A 196
SHEET 5 E 5 GLU A 358 ASN A 360 1 O ASN A 360 N ILE A 334
SHEET 1 F 2 GLN A 279 TYR A 288 0
SHEET 2 F 2 ILE A 291 THR A 298 -1 O PHE A 293 N ILE A 284
SSBOND 1 CYS B 201 CYS B 259 1555 1555 2.03
SITE 1 AC1 24 THR A 13 THR A 14 TYR A 15 GLY A 201
SITE 2 AC1 24 GLY A 202 THR A 204 GLY A 230 GLU A 268
SITE 3 AC1 24 LYS A 271 ARG A 272 SER A 275 GLY A 338
SITE 4 AC1 24 GLY A 339 SER A 340 ARG A 342 ILE A 343
SITE 5 AC1 24 ASP A 366 HOH A 387 HOH A 420 HOH A 421
SITE 6 AC1 24 HOH A 468 HOH A 484 HOH A 551 HOH A 560
CRYST1 40.289 121.123 52.773 90.00 106.25 90.00 P 1 21 1 2
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 0.024821 0.000000 0.007235 0.00000
SCALE2 0.000000 0.008256 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019737 0.00000
(ATOM LINES ARE NOT SHOWN.)
END