HEADER LYASE 02-OCT-01 1K3D
TITLE PHOSPHOENOLPYRUVATE CARBOXYKINASE IN COMPLEX WITH ADP AND ALF3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOENOLPYRUVATE CARBOXYKINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PEP CARBOXYKINASE, PHOSPHOENOLPYRUVATE CARBOXYLASE, PEPCK;
COMPND 5 EC: 4.1.1.49;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: PCKA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K12;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: K12
KEYWDS KINASE, GLUCONEOGENESIS, NUCLEOTIDE-TRIPHOSPHATE HYDROLASE., LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.SUDOM,L.PRASAD,H.GOLDIE,L.T.J.DELBAERE
REVDAT 4 16-AUG-23 1K3D 1 REMARK LINK
REVDAT 3 24-FEB-09 1K3D 1 VERSN
REVDAT 2 01-APR-03 1K3D 1 JRNL
REVDAT 1 19-DEC-01 1K3D 0
JRNL AUTH A.M.SUDOM,L.PRASAD,H.GOLDIE,L.T.DELBAERE
JRNL TITL THE PHOSPHORYL-TRANSFER MECHANISM OF ESCHERICHIA COLI
JRNL TITL 2 PHOSPHOENOLPYRUVATE CARBOXYKINASE FROM THE USE OF ALF(3).
JRNL REF J.MOL.BIOL. V. 314 83 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11724534
JRNL DOI 10.1006/JMBI.2001.5120
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
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 : 35230
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 SET) : 0.196
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1787
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 : 4127
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 275
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.00
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) : 0.20
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) : 0.006
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 : ISOTROPIC
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 1K3D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014509.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-98
REMARK 200 TEMPERATURE (KELVIN) : 290.0
REMARK 200 PH : 4.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-18B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : DIFFRACTOMETER
REMARK 200 DETECTOR MANUFACTURER : WEISSENBERG
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35758
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.8000
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) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.1
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: AMORE
REMARK 200 STARTING MODEL: PDB ID 1AQ2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: ADP, ALUMINUM NITRATE, MAGNESIUM
REMARK 280 CHLORIDE, SODIUM FLUORIDE, EDTA, AMMONIUM ACETATE, SODIUM
REMARK 280 ACETATE BUFFER, DITHIOTHREITOL, PEG 4000, PH 4.8, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 294.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 63.01650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.92200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 63.01650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 47.92200
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 ARG A 2
REMARK 465 VAL A 3
REMARK 465 ASN A 4
REMARK 465 ASN A 5
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 21 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 317 CG CD OE1 OE2
REMARK 470 THR A 394 CB OG1 CG2
REMARK 470 ARG A 396 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 398 CB CG1 CG2 CD1
REMARK 470 THR A 399 OG1 CG2
REMARK 470 GLU A 400 CG CD OE1 OE2
REMARK 470 LYS A 453 CG CD CE NZ
REMARK 470 LYS A 492 CB 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 LYS A 87 -77.14 -109.05
REMARK 500 ASP A 269 -33.54 -154.78
REMARK 500 ASP A 274 -162.12 -112.56
REMARK 500 ASP A 307 -12.46 92.29
REMARK 500 ASN A 331 45.07 -91.39
REMARK 500 ALA A 392 -150.50 -73.24
REMARK 500 THR A 394 3.79 59.17
REMARK 500 GLU A 395 58.93 38.51
REMARK 500 ILE A 398 -30.07 158.25
REMARK 500 THR A 399 141.07 173.43
REMARK 500 GLU A 400 70.28 -171.01
REMARK 500 MET A 477 -58.95 70.81
REMARK 500 THR A 525 31.10 -87.43
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 998 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 255 OG1
REMARK 620 2 ADP A 541 O2B 88.6
REMARK 620 3 HOH A 706 O 103.5 161.5
REMARK 620 4 HOH A 707 O 92.8 92.2 101.0
REMARK 620 5 HOH A 708 O 95.2 85.3 79.8 171.5
REMARK 620 6 AF3 A 999 F3 164.5 75.9 91.3 88.9 82.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 A 999 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 269 OD2
REMARK 620 2 AF3 A 999 F1 162.2
REMARK 620 3 AF3 A 999 F2 41.0 121.4
REMARK 620 4 AF3 A 999 F3 80.2 117.6 120.9
REMARK 620 5 ADP A 541 O3B 123.1 67.8 142.1 66.6
REMARK 620 6 HOH A 749 O 61.6 115.9 60.5 91.0 153.9
REMARK 620 7 HOH A 750 O 86.9 75.5 45.9 165.8 126.3 77.8
REMARK 620 N 1 2 3 4 5 6
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: TAKEN FROM PDB ENTRY 1AQ2.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: TAKEN FROM PDB ENTRY 1AQ2.
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 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 541
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 A 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AQ2 RELATED DB: PDB
REMARK 900 RELATED ID: 1AYL RELATED DB: PDB
REMARK 900 RELATED ID: 1K3C RELATED DB: PDB
REMARK 900 PHOSPHOENOLPYRUVATE CARBOXYKINASE IN COMPLEX WITH ADP, ALF3 AND
REMARK 900 PYRUVATE
DBREF 1K3D A 1 540 UNP P22259 PPCK_ECOLI 1 540
SEQRES 1 A 540 MET ARG VAL ASN ASN GLY LEU THR PRO GLN GLU LEU GLU
SEQRES 2 A 540 ALA TYR GLY ILE SER ASP VAL HIS ASP ILE VAL TYR ASN
SEQRES 3 A 540 PRO SER TYR ASP LEU LEU TYR GLN GLU GLU LEU ASP PRO
SEQRES 4 A 540 SER LEU THR GLY TYR GLU ARG GLY VAL LEU THR ASN LEU
SEQRES 5 A 540 GLY ALA VAL ALA VAL ASP THR GLY ILE PHE THR GLY ARG
SEQRES 6 A 540 SER PRO LYS ASP LYS TYR ILE VAL ARG ASP ASP THR THR
SEQRES 7 A 540 ARG ASP THR PHE TRP TRP ALA ASP LYS GLY LYS GLY LYS
SEQRES 8 A 540 ASN ASP ASN LYS PRO LEU SER PRO GLU THR TRP GLN HIS
SEQRES 9 A 540 LEU LYS GLY LEU VAL THR ARG GLN LEU SER GLY LYS ARG
SEQRES 10 A 540 LEU PHE VAL VAL ASP ALA PHE CYS GLY ALA ASN PRO ASP
SEQRES 11 A 540 THR ARG LEU SER VAL ARG PHE ILE THR GLU VAL ALA TRP
SEQRES 12 A 540 GLN ALA HIS PHE VAL LYS ASN MET PHE ILE ARG PRO SER
SEQRES 13 A 540 ASP GLU GLU LEU ALA GLY PHE LYS PRO ASP PHE ILE VAL
SEQRES 14 A 540 MET ASN GLY ALA LYS CYS THR ASN PRO GLN TRP LYS GLU
SEQRES 15 A 540 GLN GLY LEU ASN SER GLU ASN PHE VAL ALA PHE ASN LEU
SEQRES 16 A 540 THR GLU ARG MET GLN LEU ILE GLY GLY THR TRP TYR GLY
SEQRES 17 A 540 GLY GLU MET LYS LYS GLY MET PHE SER MET MET ASN TYR
SEQRES 18 A 540 LEU LEU PRO LEU LYS GLY ILE ALA SER MET HIS CYS SER
SEQRES 19 A 540 ALA ASN VAL GLY GLU LYS GLY ASP VAL ALA VAL PHE PHE
SEQRES 20 A 540 GLY LEU SER GLY THR GLY LYS THR THR LEU SER THR ASP
SEQRES 21 A 540 PRO LYS ARG ARG LEU ILE GLY ASP ASP GLU HIS GLY TRP
SEQRES 22 A 540 ASP ASP ASP GLY VAL PHE ASN PHE GLU GLY GLY CYS TYR
SEQRES 23 A 540 ALA LYS THR ILE LYS LEU SER LYS GLU ALA GLU PRO GLU
SEQRES 24 A 540 ILE TYR ASN ALA ILE ARG ARG ASP ALA LEU LEU GLU ASN
SEQRES 25 A 540 VAL THR VAL ARG GLU ASP GLY THR ILE ASP PHE ASP ASP
SEQRES 26 A 540 GLY SER LYS THR GLU ASN THR ARG VAL SER TYR PRO ILE
SEQRES 27 A 540 TYR HIS ILE ASP ASN ILE VAL LYS PRO VAL SER LYS ALA
SEQRES 28 A 540 GLY HIS ALA THR LYS VAL ILE PHE LEU THR ALA ASP ALA
SEQRES 29 A 540 PHE GLY VAL LEU PRO PRO VAL SER ARG LEU THR ALA ASP
SEQRES 30 A 540 GLN THR GLN TYR HIS PHE LEU SER GLY PHE THR ALA LYS
SEQRES 31 A 540 LEU ALA GLY THR GLU ARG GLY ILE THR GLU PRO THR PRO
SEQRES 32 A 540 THR PHE SER ALA CYS PHE GLY ALA ALA PHE LEU SER LEU
SEQRES 33 A 540 HIS PRO THR GLN TYR ALA GLU VAL LEU VAL LYS ARG MET
SEQRES 34 A 540 GLN ALA ALA GLY ALA GLN ALA TYR LEU VAL ASN THR GLY
SEQRES 35 A 540 TRP ASN GLY THR GLY LYS ARG ILE SER ILE LYS ASP THR
SEQRES 36 A 540 ARG ALA ILE ILE ASP ALA ILE LEU ASN GLY SER LEU ASP
SEQRES 37 A 540 ASN ALA GLU THR PHE THR LEU PRO MET PHE ASN LEU ALA
SEQRES 38 A 540 ILE PRO THR GLU LEU PRO GLY VAL ASP THR LYS ILE LEU
SEQRES 39 A 540 ASP PRO ARG ASN THR TYR ALA SER PRO GLU GLN TRP GLN
SEQRES 40 A 540 GLU LYS ALA GLU THR LEU ALA LYS LEU PHE ILE ASP ASN
SEQRES 41 A 540 PHE ASP LYS TYR THR ASP THR PRO ALA GLY ALA ALA LEU
SEQRES 42 A 540 VAL ALA ALA GLY PRO LYS LEU
HET MG A 998 1
HET ADP A 541 27
HET AF3 A 999 4
HETNAM MG MAGNESIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM AF3 ALUMINUM FLUORIDE
FORMUL 2 MG MG 2+
FORMUL 3 ADP C10 H15 N5 O10 P2
FORMUL 4 AF3 AL F3
FORMUL 5 HOH *275(H2 O)
HELIX 1 A PRO A 9 GLY A 16 1 8
HELIX 2 B TYR A 29 GLU A 36 1 8
HELIX 3 C PRO A 99 LEU A 113 1 15
HELIX 4 D ALA A 142 MET A 151 1 10
HELIX 5 E GLY A 209 LEU A 225 1 17
HELIX 6 F GLY A 253 SER A 258 1 6
HELIX 7 G PRO A 298 ALA A 303 1 6
HELIX 8 H ALA A 376 SER A 385 1 10
HELIX 9 I PRO A 418 ALA A 432 1 15
HELIX 10 J SER A 451 LEU A 463 1 13
HELIX 11 K THR A 491 LEU A 494 5 4
HELIX 12 L PRO A 503 TYR A 524 1 22
HELIX 13 M PRO A 528 LEU A 533 1 6
HELIX 14 N VAL A 534 ALA A 536 5 3
SHEET 1 A 8 ASP A 22 TYR A 25 0
SHEET 2 A 8 ARG A 117 CYS A 125 1
SHEET 3 A 8 LEU A 133 THR A 139 -1
SHEET 4 A 8 PHE A 167 GLY A 172 1
SHEET 5 A 8 MET A 199 GLY A 203 1
SHEET 6 A 8 PHE A 190 ASN A 194 -1
SHEET 7 A 8 LYS A 70 VAL A 73 1
SHEET 8 A 8 LYS A 95 LEU A 97 1
SHEET 1 B 5 GLY A 47 LEU A 49 0
SHEET 2 B 5 VAL A 55 VAL A 57 -1
SHEET 3 B 5 LEU A 309 GLU A 311 1
SHEET 4 B 5 ARG A 333 TYR A 336 -1
SHEET 5 B 5 GLY A 284 LYS A 288 -1
SHEET 1 C 4 SER A 349 GLY A 352 0
SHEET 2 C 4 GLY A 277 ASN A 280 -1
SHEET 3 C 4 GLU A 270 ASP A 274 -1
SHEET 4 C 4 ALA A 229 HIS A 232 -1
SHEET 1 D 6 ARG A 264 GLY A 267 0
SHEET 2 D 6 SER A 234 VAL A 237 -1
SHEET 3 D 6 VAL A 243 PHE A 247 -1
SHEET 4 D 6 THR A 355 THR A 361 1
SHEET 5 D 6 GLN A 435 ASN A 440 1
SHEET 6 D 6 VAL A 371 ARG A 373 -1
LINK OG1 THR A 255 MG MG A 998 1555 1555 2.08
LINK OD2 ASP A 269 AL AF3 A 999 1555 1555 3.56
LINK O2B ADP A 541 MG MG A 998 1555 1555 2.30
LINK O3B ADP A 541 AL AF3 A 999 1555 1555 2.83
LINK O HOH A 706 MG MG A 998 1555 1555 2.53
LINK O HOH A 707 MG MG A 998 1555 1555 2.24
LINK O HOH A 708 MG MG A 998 1555 1555 2.15
LINK O HOH A 749 AL AF3 A 999 1555 1555 3.34
LINK O HOH A 750 AL AF3 A 999 1555 1555 3.35
LINK MG MG A 998 F3 AF3 A 999 1555 1555 2.02
CISPEP 1 LYS A 346 PRO A 347 0 0.02
SITE 1 AC1 7 THR A 255 ASP A 268 ADP A 541 HOH A 706
SITE 2 AC1 7 HOH A 707 HOH A 708 AF3 A 999
SITE 1 AC2 23 LEU A 249 SER A 250 GLY A 251 THR A 252
SITE 2 AC2 23 GLY A 253 LYS A 254 THR A 255 THR A 256
SITE 3 AC2 23 LYS A 288 GLU A 297 THR A 441 ARG A 449
SITE 4 AC2 23 ILE A 450 SER A 451 ILE A 452 THR A 455
SITE 5 AC2 23 HOH A 691 HOH A 695 HOH A 707 HOH A 708
SITE 6 AC2 23 HOH A 868 MG A 998 AF3 A 999
SITE 1 AC3 11 LYS A 213 HIS A 232 SER A 250 ASP A 269
SITE 2 AC3 11 ARG A 333 ADP A 541 HOH A 707 HOH A 708
SITE 3 AC3 11 HOH A 749 HOH A 750 MG A 998
CRYST1 126.033 95.844 46.608 90.00 95.59 90.00 C 1 2 1 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 0.007930 0.000000 0.000780 0.00000
SCALE2 0.000000 0.010430 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021560 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
