HEADER HYDROLASE(ACTING ON ACID ANHYDRIDES) 17-MAY-94 1NGB
TITLE STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP
TITLE 2 HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP
TITLE 3 BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAT-SHOCK COGNATE 70 KD PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.6.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: BRAIN
KEYWDS HYDROLASE(ACTING ON ACID ANHYDRIDES)
EXPDTA X-RAY DIFFRACTION
AUTHOR K.M.FLAHERTY,S.M.WILBANKS,C.DELUCA-FLAHERTY,D.B.MCKAY
REVDAT 4 14-FEB-24 1NGB 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1NGB 1 VERSN
REVDAT 2 01-APR-03 1NGB 1 JRNL
REVDAT 1 31-AUG-94 1NGB 0
JRNL AUTH K.M.FLAHERTY,S.M.WILBANKS,C.DELUCA-FLAHERTY,D.B.MCKAY
JRNL TITL STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE
JRNL TITL 2 PROTEIN ATP HYDROLYTIC ACTIVITY. II. STRUCTURE OF THE ACTIVE
JRNL TITL 3 SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE
JRNL TITL 4 FRAGMENT.
JRNL REF J.BIOL.CHEM. V. 269 12899 1994
JRNL REFN ISSN 0021-9258
JRNL PMID 8175707
REMARK 1
REMARK 1 REFERENCE 1
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 2
REMARK 2 RESOLUTION. 2.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 15194
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2928
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 146
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NGB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175274.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 72.65000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 23.45000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 23.45000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 72.65000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.50000
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 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 SER 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 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 57 0.48 -69.04
REMARK 500 THR A 140 -59.00 -121.54
REMARK 500 ARG A 171 148.97 -174.21
REMARK 500 ALA A 191 156.62 171.49
REMARK 500 GLU A 289 -110.71 59.42
REMARK 500 LYS A 361 27.24 -155.88
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 88.0
REMARK 620 3 HOH A 565 O 92.9 94.3
REMARK 620 4 HOH A 566 O 95.8 79.7 169.3
REMARK 620 5 HOH A 567 O 95.4 172.8 79.2 106.2
REMARK 620 6 HOH A 656 O 171.8 86.8 93.9 77.0 90.5
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 MG A 487
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 488
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 486
DBREF 1NGB A 1 386 UNP P19120 HSP7C_BOVIN 1 386
SEQADV 1NGB GLN A 175 UNP P19120 GLU 175 CONFLICT
SEQRES 1 A 386 MET SER LYS GLY PRO ALA VAL GLY ILE ASP LEU GLY THR
SEQRES 2 A 386 THR TYR SER CYS VAL GLY VAL PHE GLN HIS GLY LYS VAL
SEQRES 3 A 386 GLU ILE ILE ALA ASN ASP GLN GLY ASN ARG THR THR PRO
SEQRES 4 A 386 SER TYR VAL ALA PHE THR ASP THR GLU ARG LEU ILE GLY
SEQRES 5 A 386 ASP ALA ALA LYS ASN GLN VAL ALA MET ASN PRO THR ASN
SEQRES 6 A 386 THR VAL PHE ASP ALA LYS ARG LEU ILE GLY ARG ARG PHE
SEQRES 7 A 386 ASP ASP ALA VAL VAL GLN SER ASP MET LYS HIS TRP PRO
SEQRES 8 A 386 PHE MET VAL VAL ASN ASP ALA GLY ARG PRO LYS VAL GLN
SEQRES 9 A 386 VAL GLU TYR LYS GLY GLU THR LYS SER PHE TYR PRO GLU
SEQRES 10 A 386 GLU VAL SER SER MET VAL LEU THR LYS MET LYS GLU ILE
SEQRES 11 A 386 ALA GLU ALA TYR LEU GLY LYS THR VAL THR ASN ALA VAL
SEQRES 12 A 386 VAL THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG GLN
SEQRES 13 A 386 ALA THR LYS ASP ALA GLY THR ILE ALA GLY LEU ASN VAL
SEQRES 14 A 386 LEU ARG ILE ILE ASN GLN PRO THR ALA ALA ALA ILE ALA
SEQRES 15 A 386 TYR GLY LEU ASP LYS LYS VAL GLY ALA GLU ARG ASN VAL
SEQRES 16 A 386 LEU ILE PHE ASP LEU GLY GLY GLY THR PHE ASP VAL SER
SEQRES 17 A 386 ILE LEU THR ILE GLU ASP GLY ILE PHE GLU VAL LYS SER
SEQRES 18 A 386 THR ALA GLY ASP THR HIS LEU GLY GLY GLU ASP PHE ASP
SEQRES 19 A 386 ASN ARG MET VAL ASN HIS PHE ILE ALA GLU PHE LYS ARG
SEQRES 20 A 386 LYS HIS LYS LYS ASP ILE SER GLU ASN LYS ARG ALA VAL
SEQRES 21 A 386 ARG ARG LEU ARG THR ALA CYS GLU ARG ALA LYS ARG THR
SEQRES 22 A 386 LEU SER SER SER THR GLN ALA SER ILE GLU ILE ASP SER
SEQRES 23 A 386 LEU TYR GLU GLY ILE ASP PHE TYR THR SER ILE THR ARG
SEQRES 24 A 386 ALA ARG PHE GLU GLU LEU ASN ALA ASP LEU PHE ARG GLY
SEQRES 25 A 386 THR LEU ASP PRO VAL GLU LYS ALA LEU ARG ASP ALA LYS
SEQRES 26 A 386 LEU ASP LYS SER GLN ILE HIS ASP ILE VAL LEU VAL GLY
SEQRES 27 A 386 GLY SER THR ARG ILE PRO LYS ILE GLN LYS LEU LEU GLN
SEQRES 28 A 386 ASP PHE PHE ASN GLY LYS GLU LEU ASN LYS SER ILE ASN
SEQRES 29 A 386 PRO ASP GLU ALA VAL ALA TYR GLY ALA ALA VAL GLN ALA
SEQRES 30 A 386 ALA ILE LEU SER GLY ASP LYS SER GLU
HET MG A 487 1
HET PO4 A 488 5
HET ADP A 486 27
HETNAM MG MAGNESIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 PO4 O4 P 3-
FORMUL 4 ADP C10 H15 N5 O10 P2
FORMUL 5 HOH *146(H2 O)
HELIX 1 1 GLY A 52 ASN A 57 1 6
HELIX 2 2 GLN A 58 ASN A 62 5 5
HELIX 3 3 ASN A 62 THR A 64 5 3
HELIX 4 4 ASP A 69 LEU A 73 5 5
HELIX 5 5 ASP A 80 MET A 87 1 8
HELIX 6 6 LYS A 88 TRP A 90 5 3
HELIX 7 7 TYR A 115 GLY A 136 1 22
HELIX 8 8 ASN A 151 ALA A 165 1 15
HELIX 9 9 GLN A 175 TYR A 183 1 9
HELIX 10 10 GLY A 229 LYS A 250 1 22
HELIX 11 11 ASN A 256 LEU A 274 1 19
HELIX 12 12 ARG A 299 ASN A 306 1 8
HELIX 13 13 ASN A 306 GLY A 312 1 7
HELIX 14 14 THR A 313 ALA A 324 1 12
HELIX 15 15 ASP A 327 ILE A 331 5 5
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
SHEET 1 A 5 LYS A 25 ILE A 28 0
SHEET 2 A 5 TYR A 15 GLN A 22 -1 O VAL A 20 N GLU A 27
SHEET 3 A 5 VAL A 7 ASP A 10 -1 N GLY A 8 O GLY A 19
SHEET 4 A 5 ASN A 141 VAL A 146 1 O ASN A 141 N VAL A 7
SHEET 5 A 5 ASN A 168 ASN A 174 1 O ASN A 168 N ALA A 142
SHEET 1 B 3 LYS A 25 ILE A 28 0
SHEET 2 B 3 TYR A 15 GLN A 22 -1 O VAL A 20 N GLU A 27
SHEET 3 B 3 THR A 38 PRO A 39 -1 O THR A 38 N SER A 16
SHEET 1 C 3 ARG A 49 ILE A 51 0
SHEET 2 C 3 VAL A 42 PHE A 44 -1 O ALA A 43 N LEU A 50
SHEET 3 C 3 THR A 66 VAL A 67 -1 N VAL A 67 O 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 4 ILE A 216 ASP A 225 0
SHEET 2 E 4 PHE A 205 GLU A 213 -1 N PHE A 205 O ASP A 225
SHEET 3 E 4 ARG A 193 LEU A 200 -1 O ARG A 193 N ILE A 212
SHEET 4 E 4 ASP A 333 VAL A 337 1 O ASP A 333 N LEU A 196
SHEET 1 F 2 GLN A 279 TYR A 288 0
SHEET 2 F 2 ILE A 291 THR A 298 -1 N ILE A 291 O TYR A 288
LINK O2B ADP A 486 MG MG A 487 1555 1555 1.90
LINK MG MG A 487 O2 PO4 A 488 1555 1555 2.04
LINK MG MG A 487 O HOH A 565 1555 1555 2.14
LINK MG MG A 487 O HOH A 566 1555 1555 2.22
LINK MG MG A 487 O HOH A 567 1555 1555 2.09
LINK MG MG A 487 O HOH A 656 1555 1555 2.07
SITE 1 AC1 6 ADP A 486 PO4 A 488 HOH A 565 HOH A 566
SITE 2 AC1 6 HOH A 567 HOH A 656
SITE 1 AC2 11 GLY A 12 THR A 13 LYS A 71 GLN A 175
SITE 2 AC2 11 THR A 204 ADP A 486 MG A 487 HOH A 565
SITE 3 AC2 11 HOH A 566 HOH A 569 HOH A 656
SITE 1 AC3 27 THR A 13 THR A 14 TYR A 15 GLY A 201
SITE 2 AC3 27 GLY A 202 GLY A 230 GLU A 268 LYS A 271
SITE 3 AC3 27 ARG A 272 SER A 275 GLY A 338 GLY A 339
SITE 4 AC3 27 SER A 340 ARG A 342 ILE A 343 ASP A 366
SITE 5 AC3 27 MG A 487 PO4 A 488 HOH A 531 HOH A 542
SITE 6 AC3 27 HOH A 543 HOH A 560 HOH A 565 HOH A 566
SITE 7 AC3 27 HOH A 567 HOH A 568 HOH A 569
CRYST1 145.300 65.000 46.900 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 0.006882 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015385 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021322 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
