HEADER CHAPERONE 21-SEP-09 3JXU
TITLE CRYSTAL STRUCTURE OF THE HUMAN 70KDA HEAT SHOCK PROTEIN 1A (HSP70-1)
TITLE 2 ATPASE DOMAIN IN COMPLEX WITH ADP AND INORGANIC PHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT SHOCK 70 KDA PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ATPASE DOMAIN, UNP RESIUDES 1-387;
COMPND 5 SYNONYM: HSP70.1, HSP70-1/HSP70-2, 70KDA HEAT SHOCK PROTEIN 1A;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)R3 PRARE;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4
KEYWDS HELIX, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, ATP-
KEYWDS 2 BINDING, CHAPERONE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN,
KEYWDS 3 POLYMORPHISM, STRESS RESPONSE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.M.WISNIEWSKA,T.KARLBERG,C.H.ARROWSMITH,H.BERGLUND,C.BOUNTRA,
AUTHOR 2 R.COLLINS,A.M.EDWARDS,S.FLODIN,A.FLORES,S.GRASLUND,M.HAMMARSTROM,
AUTHOR 3 A.JOHANSSON,I.JOHANSSON,A.KALLAS,P.KRAULIS,T.KOTENYOVA,A.KOTZSCH,
AUTHOR 4 N.MARKOVA,M.MOCHE,T.K.NIELSEN,P.NORDLUND,T.NYMAN,C.PERSSON,A.K.ROOS,
AUTHOR 5 M.I.SIPONEN,P.SCHUTZ,L.SVENSSON,A.G.THORSELL,L.TRESAUGUES,S.VAN DEN
AUTHOR 6 BERG,E.WAHLBERG,J.WEIGELT,M.WELIN,H.SCHULER,STRUCTURAL GENOMICS
AUTHOR 7 CONSORTIUM (SGC)
REVDAT 4 01-NOV-23 3JXU 1 REMARK SEQADV LINK
REVDAT 3 01-NOV-17 3JXU 1 REMARK
REVDAT 2 02-FEB-10 3JXU 1 JRNL
REVDAT 1 20-OCT-09 3JXU 0
JRNL AUTH M.WISNIEWSKA,T.KARLBERG,L.LEHTIO,I.JOHANSSON,T.KOTENYOVA,
JRNL AUTH 2 M.MOCHE,H.SCHULER
JRNL TITL CRYSTAL STRUCTURES OF THE ATPASE DOMAINS OF FOUR HUMAN HSP70
JRNL TITL 2 ISOFORMS: HSPA1L/HSP70-HOM, HSPA2/HSP70-2, HSPA6/HSP70B',
JRNL TITL 3 AND HSPA5/BIP/GRP78
JRNL REF PLOS ONE V. 5 E8625 2010
JRNL REFN ESSN 1932-6203
JRNL PMID 20072699
JRNL DOI 10.1371/JOURNAL.PONE.0008625
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0035
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) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 22346
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) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1205
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) : 2.14
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.19
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1302
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 62
REMARK 3 BIN FREE R VALUE : 0.3290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2930
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 202
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.02000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.256
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.215
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.150
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.788
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.916
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.860
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3011 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2035 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4077 ; 1.407 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4958 ; 0.882 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 377 ; 5.738 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 140 ;35.682 ;24.286
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 518 ;14.842 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;20.186 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 463 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3361 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 611 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1873 ; 0.611 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 771 ; 0.123 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3015 ; 1.130 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1138 ; 1.745 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1062 ; 2.904 ; 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 3JXU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000055295.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 5.5
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 : OTHER
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54166
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER PLATINUM 135
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SAINT, XPREP
REMARK 200 DATA SCALING SOFTWARE : XPREP
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23808
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140
REMARK 200 RESOLUTION RANGE LOW (A) : 26.430
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 12.70
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1BA0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MAGNESIUM CHLORIDE HEXAHYDRATE,
REMARK 280 0.1M BIS-TRIS, 25% PEG 3350, PH 5.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 277K
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 23.00650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.09850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.64900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.09850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.00650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.64900
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 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 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 -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 GLY A -12
REMARK 465 VAL A -11
REMARK 465 ASP A -10
REMARK 465 LEU A -9
REMARK 465 GLY A -8
REMARK 465 THR A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 LYS A 3
REMARK 465 GLY A 382
REMARK 465 ASP A 383
REMARK 465 LYS A 384
REMARK 465 SER A 385
REMARK 465 GLU A 386
REMARK 465 ASN A 387
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 190 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 62 54.31 -151.53
REMARK 500 ASP A 99 18.28 50.89
REMARK 500 LYS A 190 -69.26 63.92
REMARK 500 ASP A 214 60.76 33.77
REMARK 500 ASN A 364 114.05 -35.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 487 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 486 O2B
REMARK 620 2 PO4 A 488 O2 91.8
REMARK 620 3 HOH A 507 O 86.4 88.6
REMARK 620 4 HOH A 508 O 75.5 167.0 87.7
REMARK 620 5 HOH A 548 O 91.0 88.0 175.7 95.0
REMARK 620 6 HOH A 588 O 174.3 87.7 99.2 105.2 83.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 486
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 487
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 488
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3I33 RELATED DB: PDB
REMARK 900 RELATED ID: 3GDQ RELATED DB: PDB
REMARK 900 RELATED ID: 3IUC RELATED DB: PDB
REMARK 900 RELATED ID: 3FE1 RELATED DB: PDB
DBREF 3JXU A 1 387 UNP P08107 HSP71_HUMAN 1 387
SEQADV 3JXU MET A -21 UNP P08107 EXPRESSION TAG
SEQADV 3JXU HIS A -20 UNP P08107 EXPRESSION TAG
SEQADV 3JXU HIS A -19 UNP P08107 EXPRESSION TAG
SEQADV 3JXU HIS A -18 UNP P08107 EXPRESSION TAG
SEQADV 3JXU HIS A -17 UNP P08107 EXPRESSION TAG
SEQADV 3JXU HIS A -16 UNP P08107 EXPRESSION TAG
SEQADV 3JXU HIS A -15 UNP P08107 EXPRESSION TAG
SEQADV 3JXU SER A -14 UNP P08107 EXPRESSION TAG
SEQADV 3JXU SER A -13 UNP P08107 EXPRESSION TAG
SEQADV 3JXU GLY A -12 UNP P08107 EXPRESSION TAG
SEQADV 3JXU VAL A -11 UNP P08107 EXPRESSION TAG
SEQADV 3JXU ASP A -10 UNP P08107 EXPRESSION TAG
SEQADV 3JXU LEU A -9 UNP P08107 EXPRESSION TAG
SEQADV 3JXU GLY A -8 UNP P08107 EXPRESSION TAG
SEQADV 3JXU THR A -7 UNP P08107 EXPRESSION TAG
SEQADV 3JXU GLU A -6 UNP P08107 EXPRESSION TAG
SEQADV 3JXU ASN A -5 UNP P08107 EXPRESSION TAG
SEQADV 3JXU LEU A -4 UNP P08107 EXPRESSION TAG
SEQADV 3JXU TYR A -3 UNP P08107 EXPRESSION TAG
SEQADV 3JXU PHE A -2 UNP P08107 EXPRESSION TAG
SEQADV 3JXU GLN A -1 UNP P08107 EXPRESSION TAG
SEQADV 3JXU SER A 0 UNP P08107 EXPRESSION TAG
SEQRES 1 A 409 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 409 GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA LYS ALA
SEQRES 3 A 409 ALA ALA ILE GLY ILE ASP LEU GLY THR THR TYR SER CYS
SEQRES 4 A 409 VAL GLY VAL PHE GLN HIS GLY LYS VAL GLU ILE ILE ALA
SEQRES 5 A 409 ASN ASP GLN GLY ASN ARG THR THR PRO SER TYR VAL ALA
SEQRES 6 A 409 PHE THR ASP THR GLU ARG LEU ILE GLY ASP ALA ALA LYS
SEQRES 7 A 409 ASN GLN VAL ALA LEU ASN PRO GLN ASN THR VAL PHE ASP
SEQRES 8 A 409 ALA LYS ARG LEU ILE GLY ARG LYS PHE GLY ASP PRO VAL
SEQRES 9 A 409 VAL GLN SER ASP MET LYS HIS TRP PRO PHE GLN VAL ILE
SEQRES 10 A 409 ASN ASP GLY ASP LYS PRO LYS VAL GLN VAL SER TYR LYS
SEQRES 11 A 409 GLY GLU THR LYS ALA PHE TYR PRO GLU GLU ILE SER SER
SEQRES 12 A 409 MET VAL LEU THR LYS MET LYS GLU ILE ALA GLU ALA TYR
SEQRES 13 A 409 LEU GLY TYR PRO VAL THR ASN ALA VAL ILE THR VAL PRO
SEQRES 14 A 409 ALA TYR PHE ASN ASP SER GLN ARG GLN ALA THR LYS ASP
SEQRES 15 A 409 ALA GLY VAL ILE ALA GLY LEU ASN VAL LEU ARG ILE ILE
SEQRES 16 A 409 ASN GLU PRO THR ALA ALA ALA ILE ALA TYR GLY LEU ASP
SEQRES 17 A 409 ARG THR GLY LYS GLY GLU ARG ASN VAL LEU ILE PHE ASP
SEQRES 18 A 409 LEU GLY GLY GLY THR PHE ASP VAL SER ILE LEU THR ILE
SEQRES 19 A 409 ASP ASP GLY ILE PHE GLU VAL LYS ALA THR ALA GLY ASP
SEQRES 20 A 409 THR HIS LEU GLY GLY GLU ASP PHE ASP ASN ARG LEU VAL
SEQRES 21 A 409 ASN HIS PHE VAL GLU GLU PHE LYS ARG LYS HIS LYS LYS
SEQRES 22 A 409 ASP ILE SER GLN ASN LYS ARG ALA VAL ARG ARG LEU ARG
SEQRES 23 A 409 THR ALA CYS GLU ARG ALA LYS ARG THR LEU SER SER SER
SEQRES 24 A 409 THR GLN ALA SER LEU GLU ILE ASP SER LEU PHE GLU GLY
SEQRES 25 A 409 ILE ASP PHE TYR THR SER ILE THR ARG ALA ARG PHE GLU
SEQRES 26 A 409 GLU LEU CYS SER ASP LEU PHE ARG SER THR LEU GLU PRO
SEQRES 27 A 409 VAL GLU LYS ALA LEU ARG ASP ALA LYS LEU ASP LYS ALA
SEQRES 28 A 409 GLN ILE HIS ASP LEU VAL LEU VAL GLY GLY SER THR ARG
SEQRES 29 A 409 ILE PRO LYS VAL GLN LYS LEU LEU GLN ASP PHE PHE ASN
SEQRES 30 A 409 GLY ARG ASP LEU ASN LYS SER ILE ASN PRO ASP GLU ALA
SEQRES 31 A 409 VAL ALA TYR GLY ALA ALA VAL GLN ALA ALA ILE LEU MET
SEQRES 32 A 409 GLY ASP LYS SER GLU ASN
HET ADP A 486 27
HET MG A 487 1
HET PO4 A 488 5
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM PO4 PHOSPHATE ION
FORMUL 2 ADP C10 H15 N5 O10 P2
FORMUL 3 MG MG 2+
FORMUL 4 PO4 O4 P 3-
FORMUL 5 HOH *202(H2 O)
HELIX 1 1 GLY A 52 ASN A 57 1 6
HELIX 2 2 GLN A 58 GLN A 64 5 7
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 THR A 188 5 5
HELIX 9 9 GLY A 229 LYS A 250 1 22
HELIX 10 10 ASN A 256 LEU A 274 1 19
HELIX 11 11 ARG A 299 CYS A 306 1 8
HELIX 12 12 CYS A 306 THR A 313 1 8
HELIX 13 13 THR A 313 ALA A 324 1 12
HELIX 14 14 ASP A 327 ILE A 331 5 5
HELIX 15 15 GLY A 338 ARG A 342 5 5
HELIX 16 16 ILE A 343 PHE A 354 1 12
HELIX 17 17 GLU A 367 MET A 381 1 15
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 ILE A 7 ASP A 10 -1 N GLY A 8 O GLY A 19
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 ILE A 173 N VAL A 146
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 GLN A 93 ASP A 97 0
SHEET 2 D 3 LYS A 100 TYR A 107 -1 O LYS A 100 N ASP A 97
SHEET 3 D 3 GLU A 110 PHE A 114 -1 O PHE A 114 N VAL A 103
SHEET 1 E 4 ILE A 216 ASP A 225 0
SHEET 2 E 4 PHE A 205 ASP A 213 -1 N VAL A 207 O ALA A 223
SHEET 3 E 4 GLU A 192 LEU A 200 -1 N ARG A 193 O ILE A 212
SHEET 4 E 4 ASP A 333 VAL A 337 1 O VAL A 335 N LEU A 196
SHEET 1 F 2 GLN A 279 PHE A 288 0
SHEET 2 F 2 ILE A 291 THR A 298 -1 O THR A 295 N LEU A 282
LINK O2B ADP A 486 MG MG A 487 1555 1555 2.01
LINK MG MG A 487 O2 PO4 A 488 1555 1555 2.19
LINK MG MG A 487 O HOH A 507 1555 1555 2.00
LINK MG MG A 487 O HOH A 508 1555 1555 2.08
LINK MG MG A 487 O HOH A 548 1555 1555 2.22
LINK MG MG A 487 O HOH A 588 1555 1555 2.15
SITE 1 AC1 30 THR A 13 THR A 14 TYR A 15 GLY A 201
SITE 2 AC1 30 GLY A 202 GLY A 230 GLU A 268 LYS A 271
SITE 3 AC1 30 ARG A 272 SER A 275 GLY A 338 GLY A 339
SITE 4 AC1 30 SER A 340 ARG A 342 ILE A 343 ASP A 366
SITE 5 AC1 30 HOH A 388 HOH A 437 HOH A 444 MG A 487
SITE 6 AC1 30 PO4 A 488 HOH A 493 HOH A 503 HOH A 507
SITE 7 AC1 30 HOH A 508 HOH A 509 HOH A 511 HOH A 522
SITE 8 AC1 30 HOH A 548 HOH A 586
SITE 1 AC2 6 ADP A 486 PO4 A 488 HOH A 507 HOH A 508
SITE 2 AC2 6 HOH A 548 HOH A 588
SITE 1 AC3 13 GLY A 12 THR A 13 LYS A 71 GLU A 175
SITE 2 AC3 13 THR A 204 HOH A 446 HOH A 447 ADP A 486
SITE 3 AC3 13 MG A 487 HOH A 493 HOH A 507 HOH A 548
SITE 4 AC3 13 HOH A 588
CRYST1 46.013 63.298 144.197 90.00 90.00 90.00 P 21 21 21 4
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 0.021733 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015798 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006935 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
