HEADER HYDROLASE 07-JUN-99 1QQN
TITLE D206S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D206S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HSC70 ATPASE FRAGMENT;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: T7 BASED;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PT7-7
KEYWDS HYDROLASE (ACTING ON ACID ANHYDRIDES), MOLECULAR CHAPERONE, ATPASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.R.JOHNSON,D.B.MCKAY
REVDAT 6 14-FEB-24 1QQN 1 REMARK SEQADV LINK
REVDAT 5 14-MAR-18 1QQN 1 SEQADV
REVDAT 4 31-JAN-18 1QQN 1 REMARK
REVDAT 3 04-OCT-17 1QQN 1 REMARK
REVDAT 2 24-FEB-09 1QQN 1 VERSN
REVDAT 1 15-SEP-99 1QQN 0
JRNL AUTH E.R.JOHNSON,D.B.MCKAY
JRNL TITL MAPPING THE ROLE OF ACTIVE SITE RESIDUES FOR TRANSDUCING AN
JRNL TITL 2 ATP-INDUCED CONFORMATIONAL CHANGE IN THE BOVINE 70-KDA HEAT
JRNL TITL 3 SHOCK COGNATE PROTEIN.
JRNL REF BIOCHEMISTRY V. 38 10823 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10451379
JRNL DOI 10.1021/BI990816G
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH K.M.FLAHERTY,S.M.WILBANKS,C.DELUCA-FLAHERTY,D.B.MCKAY
REMARK 1 TITL STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE
REMARK 1 TITL 2 PROTEIN ATP HYDROLYTIC ACTIVITY
REMARK 1 REF J.BIOL.CHEM. V. 269 12899 1994
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.M.FLAHERTY,C.DELUCA-FLAHERTY,D.B.MCKAY
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE ATPASE FRAGMENT OF A 70K
REMARK 1 TITL 2 HEAT-SHOCK COGNATE PROTEIN
REMARK 1 REF NATURE V. 346 623 1990
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/346623A0
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER, HENDRICKSON W.A. AND KONNERT
REMARK 3 J.H.
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 373843.450
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.2
REMARK 3 NUMBER OF REFLECTIONS : 29386
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 887
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3758
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 115
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2893
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 415
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.23000
REMARK 3 B22 (A**2) : 1.27000
REMARK 3 B33 (A**2) : 0.96000
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.20
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) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.17
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.980
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) : 0.570 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.000 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 0.950 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 1.500 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 38.29
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 : TOPPAR_EJ:PROTEIN_REP.PAR
REMARK 3 PARAMETER FILE 2 : TOPPAR_EJ:WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : TOPPAR_EJ:ADP+
REMARK 3 PARAMETER FILE 4 : TOPPAR_EJ:PARAMETERS.ION
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : &_1_TOPOLOGY_INFILE_1
REMARK 3 TOPOLOGY FILE 2 : &_1_TOPOLOGY_INFILE_2
REMARK 3 TOPOLOGY FILE 3 : &_1_TOPOLOGY_INFILE_3
REMARK 3 TOPOLOGY FILE 4 : &_1_TOPOLOGY_INFILE_4
REMARK 3 TOPOLOGY FILE 5 : &_1_TOPOLOGY_INFILE_5
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BIJVOET PAIRS WERE TREATED SEPARATELY
REMARK 3 IN REFINEMENT.
REMARK 4
REMARK 4 1QQN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1000009153.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAY-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30514
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.3
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.03800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.1000
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) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.10400
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: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: POLYETHYLENE GLYCOL 8000, POTASSIUM
REMARK 280 CHLORIDE, PH 9, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 4K,
REMARK 280 TEMPERATURE 277.0K
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 71.88400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 23.24300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.21200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 23.24300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 71.88400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.21200
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 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 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 VAL A 189 35.24 -150.70
REMARK 500 LYS A 361 17.35 -142.49
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 K A 490 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 10 OD1
REMARK 620 2 ASP A 10 OD2 38.7
REMARK 620 3 TYR A 15 O 121.7 98.7
REMARK 620 4 ADP A 486 O3B 156.1 119.2 60.4
REMARK 620 5 ADP A 486 O3A 151.9 157.2 84.5 43.6
REMARK 620 6 ADP A 486 O2B 125.4 114.9 106.3 45.9 43.5
REMARK 620 7 HOH A 558 O 92.6 126.8 91.8 111.3 75.3 111.5
REMARK 620 8 HOH A 562 O 74.4 52.1 113.9 83.3 105.9 62.8 154.3
REMARK 620 9 HOH A 563 O 68.2 83.8 166.2 106.5 88.0 60.8 97.6 57.2
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 491 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 199 O
REMARK 620 2 ASP A 199 OD1 64.7
REMARK 620 3 GLY A 201 N 70.9 78.2
REMARK 620 4 THR A 204 OG1 114.4 170.4 110.9
REMARK 620 5 THR A 204 O 71.1 123.4 54.6 63.0
REMARK 620 6 PO4 A 488 O2 157.3 96.8 120.1 81.5 131.6
REMARK 620 7 HOH A 538 O 93.8 84.3 160.4 86.2 133.0 70.4
REMARK 620 8 HOH A 560 O 112.4 55.1 69.5 130.0 119.7 60.3 107.3
REMARK 620 9 HOH A 832 O 135.2 129.1 71.8 58.8 67.3 66.4 127.0 76.0
REMARK 620 N 1 2 3 4 5 6 7 8
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 94.6
REMARK 620 3 K A 490 K 61.6 127.0
REMARK 620 4 HOH A 560 O 77.9 86.9 126.7
REMARK 620 5 HOH A 561 O 176.3 82.9 122.1 99.2
REMARK 620 6 HOH A 562 O 98.6 83.6 57.6 169.6 83.9
REMARK 620 7 HOH A 563 O 97.6 167.9 60.1 95.7 85.0 94.5
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 492
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 493
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 487
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 488
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 486
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HPM RELATED DB: PDB
DBREF 1QQN A 4 381 UNP P19120 HSP7C_BOVIN 4 381
SEQADV 1QQN SER A 206 UNP P19120 ASP 206 ENGINEERED MUTATION
SEQRES 1 A 378 GLY PRO ALA VAL GLY ILE ASP LEU GLY THR THR TYR SER
SEQRES 2 A 378 CYS VAL GLY VAL PHE GLN HIS GLY LYS VAL GLU ILE ILE
SEQRES 3 A 378 ALA ASN ASP GLN GLY ASN ARG THR THR PRO SER TYR VAL
SEQRES 4 A 378 ALA PHE THR ASP THR GLU ARG LEU ILE GLY ASP ALA ALA
SEQRES 5 A 378 LYS ASN GLN VAL ALA MET ASN PRO THR ASN THR VAL PHE
SEQRES 6 A 378 ASP ALA LYS ARG LEU ILE GLY ARG ALA PHE ASP ASP ALA
SEQRES 7 A 378 VAL VAL GLN SER ASP MET LYS HIS TRP PRO PHE MET VAL
SEQRES 8 A 378 VAL ASN ASP ALA GLY ALA PRO LYS VAL GLN VAL GLU TYR
SEQRES 9 A 378 LYS GLY GLU THR LYS SER PHE TYR PRO GLU GLU VAL SER
SEQRES 10 A 378 SER MET VAL LEU THR LYS MET LYS GLU ILE ALA GLU ALA
SEQRES 11 A 378 TYR LEU GLY ALA THR VAL THR ASN ALA VAL VAL THR VAL
SEQRES 12 A 378 PRO ALA TYR PHE ASN ASP SER GLN ARG GLN ALA THR LYS
SEQRES 13 A 378 ASP ALA GLY THR ILE ALA GLY LEU ASN VAL LEU ARG ILE
SEQRES 14 A 378 ILE ASN GLU PRO THR ALA ALA ALA ILE ALA TYR GLY LEU
SEQRES 15 A 378 ASP LYS ALA VAL GLY ALA GLU ARG ASN VAL LEU ILE PHE
SEQRES 16 A 378 ASP LEU GLY GLY GLY THR PHE SER VAL SER ILE LEU THR
SEQRES 17 A 378 ILE GLU ASP GLY ILE PHE GLU VAL LYS SER THR ALA GLY
SEQRES 18 A 378 ASP THR HIS LEU GLY GLY GLU ASP PHE ASP ASN ARG MET
SEQRES 19 A 378 VAL ASN HIS PHE ILE ALA GLU PHE LYS ARG ALA HIS ALA
SEQRES 20 A 378 LYS ASP ILE SER GLU ASN LYS ARG ALA VAL ARG ARG LEU
SEQRES 21 A 378 ALA THR ALA CYS GLU ARG ALA LYS ARG THR LEU SER SER
SEQRES 22 A 378 SER THR GLN ALA SER ILE GLU ILE ASP SER LEU TYR GLU
SEQRES 23 A 378 GLY ILE ASP PHE TYR THR SER ILE THR ARG ALA ARG PHE
SEQRES 24 A 378 GLU GLU LEU ASN ALA ASP LEU PHE ARG GLY THR LEU ASP
SEQRES 25 A 378 PRO VAL GLU LYS ALA LEU ARG ASP ALA LYS LEU ASP LYS
SEQRES 26 A 378 SER GLN ILE HIS ASP ILE VAL LEU VAL GLY GLY SER THR
SEQRES 27 A 378 ARG ILE PRO LYS ILE GLN LYS LEU LEU GLN ASP PHE PHE
SEQRES 28 A 378 ASN GLY LYS GLU LEU ASN LYS SER ILE ASN PRO ASP GLU
SEQRES 29 A 378 ALA VAL ALA TYR GLY ALA ALA VAL GLN ALA ALA ILE LEU
SEQRES 30 A 378 SER
HET K A 490 1
HET K A 491 1
HET CL A 492 1
HET CL A 493 1
HET MG A 487 1
HET PO4 A 488 5
HET ADP A 486 27
HETNAM K POTASSIUM ION
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 2 K 2(K 1+)
FORMUL 4 CL 2(CL 1-)
FORMUL 6 MG MG 2+
FORMUL 7 PO4 O4 P 3-
FORMUL 8 ADP C10 H15 N5 O10 P2
FORMUL 9 HOH *415(H2 O)
HELIX 1 1 GLY A 52 GLN A 58 1 7
HELIX 2 2 ASP A 69 LEU A 73 5 5
HELIX 3 3 ASP A 80 LYS A 88 1 9
HELIX 4 4 TYR A 115 GLY A 136 1 22
HELIX 5 5 ASN A 151 ALA A 165 1 15
HELIX 6 6 GLU A 175 TYR A 183 1 9
HELIX 7 7 GLY A 229 ALA A 250 1 22
HELIX 8 8 ASN A 256 LEU A 274 1 19
HELIX 9 9 ARG A 299 ALA A 307 1 9
HELIX 10 10 ASN A 306 THR A 313 1 8
HELIX 11 11 THR A 313 LYS A 325 1 13
HELIX 12 12 ASP A 327 ILE A 331 5 5
HELIX 13 13 GLY A 338 ARG A 342 5 5
HELIX 14 14 ILE A 343 PHE A 354 1 12
HELIX 15 15 GLU A 367 SER A 381 1 15
SHEET 1 A 5 ASN A 168 ASN A 174 0
SHEET 2 A 5 ASN A 141 VAL A 146 1 O ALA A 142 N LEU A 170
SHEET 3 A 5 VAL A 7 LEU A 11 1 N VAL A 7 O ASN A 141
SHEET 4 A 5 TYR A 15 GLN A 22 -1 O CYS A 17 N ASP A 10
SHEET 5 A 5 LYS A 25 ILE A 28 -1 O LYS A 25 N GLN A 22
SHEET 1 A1 5 ASN A 168 ASN A 174 0
SHEET 2 A1 5 ASN A 141 VAL A 146 1 O ALA A 142 N LEU A 170
SHEET 3 A1 5 VAL A 7 LEU A 11 1 N VAL A 7 O ASN A 141
SHEET 4 A1 5 TYR A 15 GLN A 22 -1 O CYS A 17 N ASP A 10
SHEET 5 A1 5 THR A 38 PRO A 39 -1 O THR A 38 N SER A 16
SHEET 1 B 3 ARG A 49 ILE A 51 0
SHEET 2 B 3 VAL A 42 PHE A 44 -1 O ALA A 43 N LEU A 50
SHEET 3 B 3 THR A 66 VAL A 67 -1 N VAL A 67 O VAL A 42
SHEET 1 C 3 MET A 93 ASP A 97 0
SHEET 2 C 3 ALA A 100 TYR A 107 -1 O ALA A 100 N ASP A 97
SHEET 3 C 3 GLU A 110 PHE A 114 -1 O GLU A 110 N TYR A 107
SHEET 1 D 4 ILE A 216 ASP A 225 0
SHEET 2 D 4 PHE A 205 GLU A 213 -1 O PHE A 205 N ASP A 225
SHEET 3 D 4 ARG A 193 LEU A 200 -1 O ARG A 193 N ILE A 212
SHEET 4 D 4 ASP A 333 VAL A 337 1 O ASP A 333 N LEU A 196
SHEET 1 E 2 GLN A 279 TYR A 288 0
SHEET 2 E 2 ILE A 291 THR A 298 -1 N ILE A 291 O TYR A 288
LINK OD1 ASP A 10 K K A 490 1555 1555 2.93
LINK OD2 ASP A 10 K K A 490 1555 1555 3.50
LINK O TYR A 15 K K A 490 1555 1555 2.88
LINK O ASP A 199 K K A 491 1555 1555 3.45
LINK OD1 ASP A 199 K K A 491 1555 1555 3.12
LINK N GLY A 201 K K A 491 1555 1555 3.47
LINK OG1 THR A 204 K K A 491 1555 1555 3.12
LINK O THR A 204 K K A 491 1555 1555 3.12
LINK O2B ADP A 486 MG MG A 487 1555 1555 2.27
LINK O3B ADP A 486 K K A 490 1555 1555 3.27
LINK O3A ADP A 486 K K A 490 1555 1555 3.56
LINK O2B ADP A 486 K K A 490 1555 1555 3.22
LINK MG MG A 487 O2 PO4 A 488 1555 1555 2.11
LINK MG MG A 487 K K A 490 1555 1555 3.60
LINK MG MG A 487 O HOH A 560 1555 1555 2.02
LINK MG MG A 487 O HOH A 561 1555 1555 2.15
LINK MG MG A 487 O HOH A 562 1555 1555 2.03
LINK MG MG A 487 O HOH A 563 1555 1555 1.99
LINK O2 PO4 A 488 K K A 491 1555 1555 2.99
LINK K K A 490 O HOH A 558 1555 1555 2.64
LINK K K A 490 O HOH A 562 1555 1555 3.04
LINK K K A 490 O HOH A 563 1555 1555 3.13
LINK K K A 491 O HOH A 538 1555 1555 3.37
LINK K K A 491 O HOH A 560 1555 1555 2.63
LINK K K A 491 O HOH A 832 1555 1555 3.68
CISPEP 1 GLY A 4 PRO A 5 0 -0.10
SITE 1 AC1 6 ASP A 10 TYR A 15 ADP A 486 MG A 487
SITE 2 AC1 6 HOH A 558 HOH A 562
SITE 1 AC2 5 ASP A 199 GLY A 201 THR A 204 PO4 A 488
SITE 2 AC2 5 HOH A 560
SITE 1 AC3 4 ASN A 31 ASP A 32 GLN A 33 LYS A 126
SITE 1 AC4 3 LYS A 345 LYS A 348 HOH A 529
SITE 1 AC5 7 ADP A 486 PO4 A 488 K A 490 HOH A 560
SITE 2 AC5 7 HOH A 561 HOH A 562 HOH A 563
SITE 1 AC6 13 GLY A 12 THR A 13 LYS A 71 PRO A 147
SITE 2 AC6 13 GLU A 175 THR A 204 ADP A 486 MG A 487
SITE 3 AC6 13 K A 491 HOH A 560 HOH A 561 HOH A 562
SITE 4 AC6 13 HOH A 832
SITE 1 AC7 27 GLY A 12 THR A 13 THR A 14 TYR A 15
SITE 2 AC7 27 GLY A 201 GLY A 202 GLY A 203 GLY A 230
SITE 3 AC7 27 GLU A 231 GLU A 268 LYS A 271 ARG A 272
SITE 4 AC7 27 SER A 275 GLY A 339 SER A 340 ARG A 342
SITE 5 AC7 27 ASP A 366 MG A 487 PO4 A 488 K A 490
SITE 6 AC7 27 HOH A 534 HOH A 543 HOH A 558 HOH A 560
SITE 7 AC7 27 HOH A 564 HOH A 832 HOH A 837
CRYST1 143.768 64.424 46.486 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 0.006956 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015522 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021512 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
