HEADER TRANSFERASE 08-JUN-09 3HQO
TITLE CRYSTAL STRUCTURES OF LEISHMANIA MEXICANA PYRUVATE KINASE (LMPYK) IN
TITLE 2 COMPLEX WITH ATP AND OXALATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE KINASE;
COMPND 3 CHAIN: K, A, B, C;
COMPND 4 SYNONYM: PK;
COMPND 5 EC: 2.7.1.40;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA MEXICANA;
SOURCE 3 ORGANISM_TAXID: 5665;
SOURCE 4 STRAIN: NHOM/B2/84/BEL46;
SOURCE 5 GENE: PYK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A_LMPYK
KEYWDS TIM BARREL, R-STATE ENZYME, ALLOSTERIC ENZYME, GLYCOLYSIS, KINASE,
KEYWDS 2 MAGNESIUM, METAL-BINDING, PYRUVATE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.P.MORGAN,M.D.WALKINSHAW
REVDAT 4 01-NOV-23 3HQO 1 REMARK LINK
REVDAT 3 28-APR-10 3HQO 1 JRNL
REVDAT 2 23-FEB-10 3HQO 1 JRNL REMARK
REVDAT 1 16-FEB-10 3HQO 0
JRNL AUTH H.P.MORGAN,I.W.MCNAE,M.W.NOWICKI,V.HANNAERT,P.A.M.MICHELS,
JRNL AUTH 2 L.A.FOTHERGILL-GILMORE,M.D.WALKINSHAW
JRNL TITL THE ALLOSTERIC MECHANISM OF PRYUVATE KINASE FROM LEISHMANIA
JRNL TITL 2 MEXICANA: A ROCK AND LOCK MODEL
JRNL REF J.BIOL.CHEM. V. 285 12892 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20123988
JRNL DOI 10.1074/JBC.M109.079905
REMARK 2
REMARK 2 RESOLUTION. 3.40 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) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 34917
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) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.251
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1831
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) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2625
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.44
REMARK 3 BIN R VALUE (WORKING SET) : 0.3510
REMARK 3 BIN FREE R VALUE SET COUNT : 150
REMARK 3 BIN FREE R VALUE : 0.3810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14988
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 158
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.14
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.12000
REMARK 3 B22 (A**2) : 8.06000
REMARK 3 B33 (A**2) : -6.95000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.64000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.670
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.516
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 70.964
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.871
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.845
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15440 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20936 ; 1.009 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1972 ; 4.756 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 688 ;34.335 ;24.826
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2652 ;16.352 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 96 ;14.926 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2420 ; 0.067 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11572 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6736 ; 0.196 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10677 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 333 ; 0.111 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 4 ; 0.102 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 151 ; 0.189 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.117 ; 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): 9784 ; 1.151 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15824 ; 2.377 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5724 ; 3.687 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5112 ; 6.822 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : K A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 K 1 K 85 2
REMARK 3 1 A 1 A 85 2
REMARK 3 1 B 1 B 85 2
REMARK 3 1 C 1 C 85 2
REMARK 3 2 K 190 K 498 1
REMARK 3 2 A 190 A 498 1
REMARK 3 2 B 190 B 498 1
REMARK 3 2 C 190 C 498 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 K (A): 2655 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 A (A): 2655 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 2655 ; 0.02 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 2655 ; 0.02 ; 0.05
REMARK 3 MEDIUM POSITIONAL 1 K (A): 300 ; 0.22 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 A (A): 300 ; 0.25 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 300 ; 0.22 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 300 ; 0.27 ; 0.50
REMARK 3 TIGHT THERMAL 1 K (A**2): 2655 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 1 A (A**2): 2655 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 2655 ; 0.02 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 2655 ; 0.02 ; 0.50
REMARK 3 MEDIUM THERMAL 1 K (A**2): 300 ; 0.16 ; 2.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 300 ; 0.17 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 300 ; 0.15 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 300 ; 0.17 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 3HQO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1000053464.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DNA
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36748
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 82.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.400
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.21000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.52000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1PKL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-16% PEG8000, 20MM TRIETHANOLAMINE
REMARK 280 -HCL, 50MM MGCL2, 100MM KCL, 10-15% GLYCEROL, PH7.2, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 290K
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 53.75800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.06650
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 53.75800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 64.06650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.10700
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -204.36097
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 BIOMT1 2 -1.000000 0.000000 0.000000 107.62300
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -204.36097
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 K 0
REMARK 465 ALA K 481
REMARK 465 ASP K 482
REMARK 465 HIS K 483
REMARK 465 LYS K 484
REMARK 465 VAL K 485
REMARK 465 LYS K 486
REMARK 465 GLY K 487
REMARK 465 MET A 0
REMARK 465 ALA A 481
REMARK 465 ASP A 482
REMARK 465 HIS A 483
REMARK 465 LYS A 484
REMARK 465 VAL A 485
REMARK 465 LYS A 486
REMARK 465 GLY A 487
REMARK 465 MET B 0
REMARK 465 ALA B 481
REMARK 465 ASP B 482
REMARK 465 HIS B 483
REMARK 465 LYS B 484
REMARK 465 VAL B 485
REMARK 465 LYS B 486
REMARK 465 GLY B 487
REMARK 465 MET C 0
REMARK 465 ALA C 481
REMARK 465 ASP C 482
REMARK 465 HIS C 483
REMARK 465 LYS C 484
REMARK 465 VAL C 485
REMARK 465 LYS C 486
REMARK 465 GLY C 487
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 THR K 31 16.02 -140.34
REMARK 500 PRO K 113 61.65 -65.13
REMARK 500 ALA K 114 -3.76 -165.46
REMARK 500 ASP K 144 89.52 61.49
REMARK 500 ASP K 145 42.02 33.90
REMARK 500 GLU K 158 45.85 -87.57
REMARK 500 GLN K 159 -23.55 -164.03
REMARK 500 HIS K 169 140.99 175.28
REMARK 500 ASP K 183 21.32 45.88
REMARK 500 VAL K 184 101.79 -51.14
REMARK 500 PRO K 187 112.93 -27.48
REMARK 500 GLU K 240 22.82 -143.45
REMARK 500 THR K 296 121.81 85.48
REMARK 500 TYR K 304 -52.55 -121.39
REMARK 500 SER K 330 -101.95 -99.26
REMARK 500 SER K 382 -72.02 -45.33
REMARK 500 ARG K 413 72.27 47.02
REMARK 500 LYS K 453 -7.89 66.37
REMARK 500 GLN K 471 -161.61 -105.38
REMARK 500 PRO A 87 46.81 -79.60
REMARK 500 THR A 111 32.61 -96.47
REMARK 500 PRO A 113 -30.44 -29.04
REMARK 500 ASN A 130 1.92 -68.15
REMARK 500 ASP A 144 88.78 68.80
REMARK 500 ASP A 145 42.13 33.69
REMARK 500 ILE A 147 -61.37 -104.54
REMARK 500 SER A 154 172.33 171.95
REMARK 500 GLU A 156 -53.50 -120.57
REMARK 500 ASP A 157 -160.70 -128.00
REMARK 500 GLU A 158 36.05 -87.20
REMARK 500 GLN A 159 -32.19 -156.91
REMARK 500 GLU A 240 22.62 -143.44
REMARK 500 THR A 296 120.88 86.02
REMARK 500 TYR A 304 -52.11 -120.94
REMARK 500 SER A 330 -101.98 -99.83
REMARK 500 SER A 382 -70.45 -45.79
REMARK 500 ARG A 413 72.72 47.08
REMARK 500 LYS A 453 -7.63 66.18
REMARK 500 GLN A 471 -161.49 -104.72
REMARK 500 THR B 31 17.65 -141.11
REMARK 500 PRO B 87 50.67 -62.68
REMARK 500 PRO B 113 4.99 -67.93
REMARK 500 LYS B 118 52.58 -117.54
REMARK 500 LYS B 121 1.33 -59.39
REMARK 500 ASN B 130 31.55 -83.54
REMARK 500 PRO B 137 103.53 -56.32
REMARK 500 ASP B 144 57.61 74.01
REMARK 500 GLN B 153 -73.09 -85.98
REMARK 500 HIS B 169 146.41 178.84
REMARK 500 ARG B 174 50.74 32.66
REMARK 500
REMARK 500 THIS ENTRY HAS 83 RAMACHANDRAN OUTLIERS.
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 K 504 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN K 51 OD1
REMARK 620 2 SER K 53 OG 53.3
REMARK 620 3 ASP K 83 OD1 73.3 121.2
REMARK 620 4 THR K 84 O 101.1 91.8 74.4
REMARK 620 5 SER K 211 OG 138.2 143.9 67.5 55.0
REMARK 620 6 ATP K1001 O3G 81.0 107.3 84.5 156.9 108.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU K 240 OE1
REMARK 620 2 ASP K 264 OD2 66.1
REMARK 620 3 OXL K 510 O4 73.7 102.6
REMARK 620 4 ATP K1001 O2G 121.0 74.9 73.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP K1001 O1B
REMARK 620 2 ATP K1001 O1G 66.6
REMARK 620 3 ATP K1001 O1A 59.5 60.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 504 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 51 OD1
REMARK 620 2 SER A 53 OG 56.4
REMARK 620 3 ASP A 83 OD1 72.7 123.5
REMARK 620 4 THR A 84 O 98.4 88.5 75.4
REMARK 620 5 SER A 211 OG 137.4 140.1 68.4 55.7
REMARK 620 6 ATP A1001 O3G 77.3 109.4 78.5 153.5 110.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 240 OE1
REMARK 620 2 ASP A 264 OD2 59.9
REMARK 620 3 OXL A 510 O4 67.4 94.6
REMARK 620 4 ATP A1001 O2G 111.2 68.4 75.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP A1001 O1G
REMARK 620 2 ATP A1001 O1B 68.6
REMARK 620 3 ATP A1001 O1A 80.3 60.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 504 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 53 OG
REMARK 620 2 ASP B 83 OD1 111.9
REMARK 620 3 THR B 84 O 83.8 69.4
REMARK 620 4 SER B 211 OG 136.7 71.9 56.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 240 OE1
REMARK 620 2 ASP B 264 OD2 64.5
REMARK 620 3 OXL B 510 O4 71.5 93.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 504 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN C 51 OD1
REMARK 620 2 SER C 53 OG 61.8
REMARK 620 3 ASP C 83 OD1 79.8 133.7
REMARK 620 4 THR C 84 O 106.1 92.1 73.8
REMARK 620 5 SER C 211 OG 146.1 139.0 67.5 56.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 240 OE1
REMARK 620 2 ASP C 264 OD2 63.5
REMARK 620 3 OXL C 510 O4 66.1 91.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K K 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXL K 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP K 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXL A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXL B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXL C 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP C 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3E0V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PYRUVATE KINASE FROM LEISHMANIA MEXICANA:
REMARK 900 SULFATE IONS REMOVED BY BACK-SOAKING
REMARK 900 RELATED ID: 3E0W RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PYRUVATE KINASE FROM LEISHMANIA MEXICANA IN
REMARK 900 COMPLEX WITH SULFATE IONS
REMARK 900 RELATED ID: 1PKL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PYRUVATE KINASE FROM LEISHMANIA MEXICANA,
REMARK 900 CRYSTALLIZED UNDER ACIDIC CONDITIONS
REMARK 900 RELATED ID: 3HQN RELATED DB: PDB
REMARK 900 RELATED ID: 3HQP RELATED DB: PDB
REMARK 900 RELATED ID: 3HQQ RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF L. MEXICANA PYRUVATE KINASE HAS BEEN DETERMINED IN
REMARK 999 THE LABORATORY OF PROF. PAUL MICHELS, PUBLISHED AND DEPOSITED IN
REMARK 999 GENBANK. HOWEVER, THE SEQUENCE AS APPEARED IN GENBANK CONTAINED
REMARK 999 ERRORS. THE CORRECTION HAS BEEN INFORMED TO GENBANK WITH THE
REMARK 999 ACCESSION CODE X74944 AND IT WILL BE FILTRATED TO UNIPROT AT A
REMARK 999 LATER TIME.
DBREF 3HQO K 0 498 UNP Q27686 KPYK_LEIME 1 499
DBREF 3HQO A 0 498 UNP Q27686 KPYK_LEIME 1 499
DBREF 3HQO B 0 498 UNP Q27686 KPYK_LEIME 1 499
DBREF 3HQO C 0 498 UNP Q27686 KPYK_LEIME 1 499
SEQADV 3HQO SER K 382 UNP Q27686 GLY 383 SEE REMARK 999
SEQADV 3HQO TYR K 389 UNP Q27686 SER 390 SEE REMARK 999
SEQADV 3HQO ARG K 404 UNP Q27686 ALA 405 SEE REMARK 999
SEQADV 3HQO SER K 405 UNP Q27686 GLY 406 SEE REMARK 999
SEQADV 3HQO SER A 382 UNP Q27686 GLY 383 SEE REMARK 999
SEQADV 3HQO TYR A 389 UNP Q27686 SER 390 SEE REMARK 999
SEQADV 3HQO ARG A 404 UNP Q27686 ALA 405 SEE REMARK 999
SEQADV 3HQO SER A 405 UNP Q27686 GLY 406 SEE REMARK 999
SEQADV 3HQO SER B 382 UNP Q27686 GLY 383 SEE REMARK 999
SEQADV 3HQO TYR B 389 UNP Q27686 SER 390 SEE REMARK 999
SEQADV 3HQO ARG B 404 UNP Q27686 ALA 405 SEE REMARK 999
SEQADV 3HQO SER B 405 UNP Q27686 GLY 406 SEE REMARK 999
SEQADV 3HQO SER C 382 UNP Q27686 GLY 383 SEE REMARK 999
SEQADV 3HQO TYR C 389 UNP Q27686 SER 390 SEE REMARK 999
SEQADV 3HQO ARG C 404 UNP Q27686 ALA 405 SEE REMARK 999
SEQADV 3HQO SER C 405 UNP Q27686 GLY 406 SEE REMARK 999
SEQRES 1 K 499 MET SER GLN LEU ALA HIS ASN LEU THR LEU SER ILE PHE
SEQRES 2 K 499 ASP PRO VAL ALA ASN TYR ARG ALA ALA ARG ILE ILE CYS
SEQRES 3 K 499 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS
SEQRES 4 K 499 GLY LEU ILE GLN SER GLY MET SER VAL ALA ARG MET ASN
SEQRES 5 K 499 PHE SER HIS GLY SER HIS GLU TYR HIS GLN THR THR ILE
SEQRES 6 K 499 ASN ASN VAL ARG GLN ALA ALA ALA GLU LEU GLY VAL ASN
SEQRES 7 K 499 ILE ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 8 K 499 THR GLY GLN PHE VAL GLY GLY ASP ALA VAL MET GLU ARG
SEQRES 9 K 499 GLY ALA THR CYS TYR VAL THR THR ASP PRO ALA PHE ALA
SEQRES 10 K 499 ASP LYS GLY THR LYS ASP LYS PHE TYR ILE ASP TYR GLN
SEQRES 11 K 499 ASN LEU SER LYS VAL VAL ARG PRO GLY ASN TYR ILE TYR
SEQRES 12 K 499 ILE ASP ASP GLY ILE LEU ILE LEU GLN VAL GLN SER HIS
SEQRES 13 K 499 GLU ASP GLU GLN THR LEU GLU CYS THR VAL THR ASN SER
SEQRES 14 K 499 HIS THR ILE SER ASP ARG ARG GLY VAL ASN LEU PRO GLY
SEQRES 15 K 499 CYS ASP VAL ASP LEU PRO ALA VAL SER ALA LYS ASP ARG
SEQRES 16 K 499 VAL ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET
SEQRES 17 K 499 ILE PHE ALA SER PHE ILE ARG SER ALA GLU GLN VAL GLY
SEQRES 18 K 499 ASP VAL ARG LYS ALA LEU GLY PRO LYS GLY ARG ASP ILE
SEQRES 19 K 499 MET ILE ILE CYS LYS ILE GLU ASN HIS GLN GLY VAL GLN
SEQRES 20 K 499 ASN ILE ASP SER ILE ILE GLU GLU SER ASP GLY ILE MET
SEQRES 21 K 499 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU
SEQRES 22 K 499 LYS VAL VAL VAL ALA GLN LYS ILE LEU ILE SER LYS CYS
SEQRES 23 K 499 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 24 K 499 LEU GLU SER MET THR TYR ASN PRO ARG PRO THR ARG ALA
SEQRES 25 K 499 GLU VAL SER ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA
SEQRES 26 K 499 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS
SEQRES 27 K 499 TYR PRO ASN GLU VAL VAL GLN TYR MET ALA ARG ILE CYS
SEQRES 28 K 499 LEU GLU ALA GLN SER ALA LEU ASN GLU TYR VAL PHE PHE
SEQRES 29 K 499 ASN SER ILE LYS LYS LEU GLN HIS ILE PRO MET SER ALA
SEQRES 30 K 499 ASP GLU ALA VAL CYS SER SER ALA VAL ASN SER VAL TYR
SEQRES 31 K 499 GLU THR LYS ALA LYS ALA MET VAL VAL LEU SER ASN THR
SEQRES 32 K 499 GLY ARG SER ALA ARG LEU VAL ALA LYS TYR ARG PRO ASN
SEQRES 33 K 499 CYS PRO ILE VAL CYS VAL THR THR ARG LEU GLN THR CYS
SEQRES 34 K 499 ARG GLN LEU ASN ILE THR GLN GLY VAL GLU SER VAL PHE
SEQRES 35 K 499 PHE ASP ALA ASP LYS LEU GLY HIS ASP GLU GLY LYS GLU
SEQRES 36 K 499 HIS ARG VAL ALA ALA GLY VAL GLU PHE ALA LYS SER LYS
SEQRES 37 K 499 GLY TYR VAL GLN THR GLY ASP TYR CYS VAL VAL ILE HIS
SEQRES 38 K 499 ALA ASP HIS LYS VAL LYS GLY TYR ALA ASN GLN THR ARG
SEQRES 39 K 499 ILE LEU LEU VAL GLU
SEQRES 1 A 499 MET SER GLN LEU ALA HIS ASN LEU THR LEU SER ILE PHE
SEQRES 2 A 499 ASP PRO VAL ALA ASN TYR ARG ALA ALA ARG ILE ILE CYS
SEQRES 3 A 499 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS
SEQRES 4 A 499 GLY LEU ILE GLN SER GLY MET SER VAL ALA ARG MET ASN
SEQRES 5 A 499 PHE SER HIS GLY SER HIS GLU TYR HIS GLN THR THR ILE
SEQRES 6 A 499 ASN ASN VAL ARG GLN ALA ALA ALA GLU LEU GLY VAL ASN
SEQRES 7 A 499 ILE ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 8 A 499 THR GLY GLN PHE VAL GLY GLY ASP ALA VAL MET GLU ARG
SEQRES 9 A 499 GLY ALA THR CYS TYR VAL THR THR ASP PRO ALA PHE ALA
SEQRES 10 A 499 ASP LYS GLY THR LYS ASP LYS PHE TYR ILE ASP TYR GLN
SEQRES 11 A 499 ASN LEU SER LYS VAL VAL ARG PRO GLY ASN TYR ILE TYR
SEQRES 12 A 499 ILE ASP ASP GLY ILE LEU ILE LEU GLN VAL GLN SER HIS
SEQRES 13 A 499 GLU ASP GLU GLN THR LEU GLU CYS THR VAL THR ASN SER
SEQRES 14 A 499 HIS THR ILE SER ASP ARG ARG GLY VAL ASN LEU PRO GLY
SEQRES 15 A 499 CYS ASP VAL ASP LEU PRO ALA VAL SER ALA LYS ASP ARG
SEQRES 16 A 499 VAL ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET
SEQRES 17 A 499 ILE PHE ALA SER PHE ILE ARG SER ALA GLU GLN VAL GLY
SEQRES 18 A 499 ASP VAL ARG LYS ALA LEU GLY PRO LYS GLY ARG ASP ILE
SEQRES 19 A 499 MET ILE ILE CYS LYS ILE GLU ASN HIS GLN GLY VAL GLN
SEQRES 20 A 499 ASN ILE ASP SER ILE ILE GLU GLU SER ASP GLY ILE MET
SEQRES 21 A 499 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU
SEQRES 22 A 499 LYS VAL VAL VAL ALA GLN LYS ILE LEU ILE SER LYS CYS
SEQRES 23 A 499 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 24 A 499 LEU GLU SER MET THR TYR ASN PRO ARG PRO THR ARG ALA
SEQRES 25 A 499 GLU VAL SER ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA
SEQRES 26 A 499 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS
SEQRES 27 A 499 TYR PRO ASN GLU VAL VAL GLN TYR MET ALA ARG ILE CYS
SEQRES 28 A 499 LEU GLU ALA GLN SER ALA LEU ASN GLU TYR VAL PHE PHE
SEQRES 29 A 499 ASN SER ILE LYS LYS LEU GLN HIS ILE PRO MET SER ALA
SEQRES 30 A 499 ASP GLU ALA VAL CYS SER SER ALA VAL ASN SER VAL TYR
SEQRES 31 A 499 GLU THR LYS ALA LYS ALA MET VAL VAL LEU SER ASN THR
SEQRES 32 A 499 GLY ARG SER ALA ARG LEU VAL ALA LYS TYR ARG PRO ASN
SEQRES 33 A 499 CYS PRO ILE VAL CYS VAL THR THR ARG LEU GLN THR CYS
SEQRES 34 A 499 ARG GLN LEU ASN ILE THR GLN GLY VAL GLU SER VAL PHE
SEQRES 35 A 499 PHE ASP ALA ASP LYS LEU GLY HIS ASP GLU GLY LYS GLU
SEQRES 36 A 499 HIS ARG VAL ALA ALA GLY VAL GLU PHE ALA LYS SER LYS
SEQRES 37 A 499 GLY TYR VAL GLN THR GLY ASP TYR CYS VAL VAL ILE HIS
SEQRES 38 A 499 ALA ASP HIS LYS VAL LYS GLY TYR ALA ASN GLN THR ARG
SEQRES 39 A 499 ILE LEU LEU VAL GLU
SEQRES 1 B 499 MET SER GLN LEU ALA HIS ASN LEU THR LEU SER ILE PHE
SEQRES 2 B 499 ASP PRO VAL ALA ASN TYR ARG ALA ALA ARG ILE ILE CYS
SEQRES 3 B 499 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS
SEQRES 4 B 499 GLY LEU ILE GLN SER GLY MET SER VAL ALA ARG MET ASN
SEQRES 5 B 499 PHE SER HIS GLY SER HIS GLU TYR HIS GLN THR THR ILE
SEQRES 6 B 499 ASN ASN VAL ARG GLN ALA ALA ALA GLU LEU GLY VAL ASN
SEQRES 7 B 499 ILE ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 8 B 499 THR GLY GLN PHE VAL GLY GLY ASP ALA VAL MET GLU ARG
SEQRES 9 B 499 GLY ALA THR CYS TYR VAL THR THR ASP PRO ALA PHE ALA
SEQRES 10 B 499 ASP LYS GLY THR LYS ASP LYS PHE TYR ILE ASP TYR GLN
SEQRES 11 B 499 ASN LEU SER LYS VAL VAL ARG PRO GLY ASN TYR ILE TYR
SEQRES 12 B 499 ILE ASP ASP GLY ILE LEU ILE LEU GLN VAL GLN SER HIS
SEQRES 13 B 499 GLU ASP GLU GLN THR LEU GLU CYS THR VAL THR ASN SER
SEQRES 14 B 499 HIS THR ILE SER ASP ARG ARG GLY VAL ASN LEU PRO GLY
SEQRES 15 B 499 CYS ASP VAL ASP LEU PRO ALA VAL SER ALA LYS ASP ARG
SEQRES 16 B 499 VAL ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET
SEQRES 17 B 499 ILE PHE ALA SER PHE ILE ARG SER ALA GLU GLN VAL GLY
SEQRES 18 B 499 ASP VAL ARG LYS ALA LEU GLY PRO LYS GLY ARG ASP ILE
SEQRES 19 B 499 MET ILE ILE CYS LYS ILE GLU ASN HIS GLN GLY VAL GLN
SEQRES 20 B 499 ASN ILE ASP SER ILE ILE GLU GLU SER ASP GLY ILE MET
SEQRES 21 B 499 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU
SEQRES 22 B 499 LYS VAL VAL VAL ALA GLN LYS ILE LEU ILE SER LYS CYS
SEQRES 23 B 499 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 24 B 499 LEU GLU SER MET THR TYR ASN PRO ARG PRO THR ARG ALA
SEQRES 25 B 499 GLU VAL SER ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA
SEQRES 26 B 499 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS
SEQRES 27 B 499 TYR PRO ASN GLU VAL VAL GLN TYR MET ALA ARG ILE CYS
SEQRES 28 B 499 LEU GLU ALA GLN SER ALA LEU ASN GLU TYR VAL PHE PHE
SEQRES 29 B 499 ASN SER ILE LYS LYS LEU GLN HIS ILE PRO MET SER ALA
SEQRES 30 B 499 ASP GLU ALA VAL CYS SER SER ALA VAL ASN SER VAL TYR
SEQRES 31 B 499 GLU THR LYS ALA LYS ALA MET VAL VAL LEU SER ASN THR
SEQRES 32 B 499 GLY ARG SER ALA ARG LEU VAL ALA LYS TYR ARG PRO ASN
SEQRES 33 B 499 CYS PRO ILE VAL CYS VAL THR THR ARG LEU GLN THR CYS
SEQRES 34 B 499 ARG GLN LEU ASN ILE THR GLN GLY VAL GLU SER VAL PHE
SEQRES 35 B 499 PHE ASP ALA ASP LYS LEU GLY HIS ASP GLU GLY LYS GLU
SEQRES 36 B 499 HIS ARG VAL ALA ALA GLY VAL GLU PHE ALA LYS SER LYS
SEQRES 37 B 499 GLY TYR VAL GLN THR GLY ASP TYR CYS VAL VAL ILE HIS
SEQRES 38 B 499 ALA ASP HIS LYS VAL LYS GLY TYR ALA ASN GLN THR ARG
SEQRES 39 B 499 ILE LEU LEU VAL GLU
SEQRES 1 C 499 MET SER GLN LEU ALA HIS ASN LEU THR LEU SER ILE PHE
SEQRES 2 C 499 ASP PRO VAL ALA ASN TYR ARG ALA ALA ARG ILE ILE CYS
SEQRES 3 C 499 THR ILE GLY PRO SER THR GLN SER VAL GLU ALA LEU LYS
SEQRES 4 C 499 GLY LEU ILE GLN SER GLY MET SER VAL ALA ARG MET ASN
SEQRES 5 C 499 PHE SER HIS GLY SER HIS GLU TYR HIS GLN THR THR ILE
SEQRES 6 C 499 ASN ASN VAL ARG GLN ALA ALA ALA GLU LEU GLY VAL ASN
SEQRES 7 C 499 ILE ALA ILE ALA LEU ASP THR LYS GLY PRO GLU ILE ARG
SEQRES 8 C 499 THR GLY GLN PHE VAL GLY GLY ASP ALA VAL MET GLU ARG
SEQRES 9 C 499 GLY ALA THR CYS TYR VAL THR THR ASP PRO ALA PHE ALA
SEQRES 10 C 499 ASP LYS GLY THR LYS ASP LYS PHE TYR ILE ASP TYR GLN
SEQRES 11 C 499 ASN LEU SER LYS VAL VAL ARG PRO GLY ASN TYR ILE TYR
SEQRES 12 C 499 ILE ASP ASP GLY ILE LEU ILE LEU GLN VAL GLN SER HIS
SEQRES 13 C 499 GLU ASP GLU GLN THR LEU GLU CYS THR VAL THR ASN SER
SEQRES 14 C 499 HIS THR ILE SER ASP ARG ARG GLY VAL ASN LEU PRO GLY
SEQRES 15 C 499 CYS ASP VAL ASP LEU PRO ALA VAL SER ALA LYS ASP ARG
SEQRES 16 C 499 VAL ASP LEU GLN PHE GLY VAL GLU GLN GLY VAL ASP MET
SEQRES 17 C 499 ILE PHE ALA SER PHE ILE ARG SER ALA GLU GLN VAL GLY
SEQRES 18 C 499 ASP VAL ARG LYS ALA LEU GLY PRO LYS GLY ARG ASP ILE
SEQRES 19 C 499 MET ILE ILE CYS LYS ILE GLU ASN HIS GLN GLY VAL GLN
SEQRES 20 C 499 ASN ILE ASP SER ILE ILE GLU GLU SER ASP GLY ILE MET
SEQRES 21 C 499 VAL ALA ARG GLY ASP LEU GLY VAL GLU ILE PRO ALA GLU
SEQRES 22 C 499 LYS VAL VAL VAL ALA GLN LYS ILE LEU ILE SER LYS CYS
SEQRES 23 C 499 ASN VAL ALA GLY LYS PRO VAL ILE CYS ALA THR GLN MET
SEQRES 24 C 499 LEU GLU SER MET THR TYR ASN PRO ARG PRO THR ARG ALA
SEQRES 25 C 499 GLU VAL SER ASP VAL ALA ASN ALA VAL PHE ASN GLY ALA
SEQRES 26 C 499 ASP CYS VAL MET LEU SER GLY GLU THR ALA LYS GLY LYS
SEQRES 27 C 499 TYR PRO ASN GLU VAL VAL GLN TYR MET ALA ARG ILE CYS
SEQRES 28 C 499 LEU GLU ALA GLN SER ALA LEU ASN GLU TYR VAL PHE PHE
SEQRES 29 C 499 ASN SER ILE LYS LYS LEU GLN HIS ILE PRO MET SER ALA
SEQRES 30 C 499 ASP GLU ALA VAL CYS SER SER ALA VAL ASN SER VAL TYR
SEQRES 31 C 499 GLU THR LYS ALA LYS ALA MET VAL VAL LEU SER ASN THR
SEQRES 32 C 499 GLY ARG SER ALA ARG LEU VAL ALA LYS TYR ARG PRO ASN
SEQRES 33 C 499 CYS PRO ILE VAL CYS VAL THR THR ARG LEU GLN THR CYS
SEQRES 34 C 499 ARG GLN LEU ASN ILE THR GLN GLY VAL GLU SER VAL PHE
SEQRES 35 C 499 PHE ASP ALA ASP LYS LEU GLY HIS ASP GLU GLY LYS GLU
SEQRES 36 C 499 HIS ARG VAL ALA ALA GLY VAL GLU PHE ALA LYS SER LYS
SEQRES 37 C 499 GLY TYR VAL GLN THR GLY ASP TYR CYS VAL VAL ILE HIS
SEQRES 38 C 499 ALA ASP HIS LYS VAL LYS GLY TYR ALA ASN GLN THR ARG
SEQRES 39 C 499 ILE LEU LEU VAL GLU
HET MG K 500 1
HET MG K 502 1
HET K K 504 1
HET OXL K 510 6
HET ATP K1001 31
HET MG A 500 1
HET MG A 502 1
HET K A 504 1
HET OXL A 510 6
HET ATP A1001 31
HET MG B 502 1
HET K B 504 1
HET OXL B 510 6
HET ATP B1001 31
HET MG C 502 1
HET K C 504 1
HET OXL C 510 6
HET ATP C1001 31
HETNAM MG MAGNESIUM ION
HETNAM K POTASSIUM ION
HETNAM OXL OXALATE ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 5 MG 6(MG 2+)
FORMUL 7 K 4(K 1+)
FORMUL 8 OXL 4(C2 O4 2-)
FORMUL 9 ATP 4(C10 H16 N5 O13 P3)
HELIX 1 1 SER K 1 THR K 8 1 8
HELIX 2 2 SER K 33 GLY K 44 1 12
HELIX 3 3 SER K 56 GLY K 75 1 20
HELIX 4 4 ASN K 130 VAL K 135 1 6
HELIX 5 5 SER K 190 GLY K 204 1 15
HELIX 6 6 SER K 215 GLY K 227 1 13
HELIX 7 7 ASN K 241 ASN K 247 1 7
HELIX 8 8 ASN K 247 SER K 255 1 9
HELIX 9 9 ARG K 262 ILE K 269 1 8
HELIX 10 10 PRO K 270 GLY K 289 1 20
HELIX 11 11 LEU K 299 TYR K 304 5 6
HELIX 12 12 THR K 309 GLY K 323 1 15
HELIX 13 13 SER K 330 LYS K 335 1 6
HELIX 14 14 TYR K 338 ALA K 356 1 19
HELIX 15 15 ASN K 358 LEU K 369 1 12
HELIX 16 16 SER K 375 LYS K 392 1 18
HELIX 17 17 GLY K 403 LYS K 411 1 9
HELIX 18 18 ARG K 424 LEU K 431 1 8
HELIX 19 19 ASP K 443 GLY K 448 1 6
HELIX 20 20 LYS K 453 LYS K 467 1 15
HELIX 21 21 SER A 1 THR A 8 1 8
HELIX 22 22 SER A 33 GLY A 44 1 12
HELIX 23 23 SER A 56 GLY A 75 1 20
HELIX 24 24 ASP A 112 ALA A 116 5 5
HELIX 25 25 ASN A 130 VAL A 135 1 6
HELIX 26 26 SER A 190 GLY A 204 1 15
HELIX 27 27 SER A 215 GLY A 227 1 13
HELIX 28 28 ASN A 241 ASN A 247 1 7
HELIX 29 29 ASN A 247 SER A 255 1 9
HELIX 30 30 ARG A 262 ILE A 269 1 8
HELIX 31 31 PRO A 270 GLY A 289 1 20
HELIX 32 32 LEU A 299 TYR A 304 5 6
HELIX 33 33 THR A 309 GLY A 323 1 15
HELIX 34 34 SER A 330 LYS A 335 1 6
HELIX 35 35 TYR A 338 ALA A 356 1 19
HELIX 36 36 ASN A 358 LEU A 369 1 12
HELIX 37 37 SER A 375 LYS A 392 1 18
HELIX 38 38 GLY A 403 LYS A 411 1 9
HELIX 39 39 ARG A 424 LEU A 431 1 8
HELIX 40 40 ASP A 443 GLY A 448 1 6
HELIX 41 41 LYS A 453 LYS A 467 1 15
HELIX 42 42 SER B 1 THR B 8 1 8
HELIX 43 43 SER B 33 GLY B 44 1 12
HELIX 44 44 SER B 56 GLY B 75 1 20
HELIX 45 45 ASN B 130 VAL B 135 1 6
HELIX 46 46 SER B 190 GLY B 204 1 15
HELIX 47 47 SER B 215 GLY B 227 1 13
HELIX 48 48 ASN B 241 ASN B 247 1 7
HELIX 49 49 ASN B 247 SER B 255 1 9
HELIX 50 50 ARG B 262 ILE B 269 1 8
HELIX 51 51 PRO B 270 GLY B 289 1 20
HELIX 52 52 LEU B 299 TYR B 304 5 6
HELIX 53 53 THR B 309 GLY B 323 1 15
HELIX 54 54 SER B 330 LYS B 335 1 6
HELIX 55 55 TYR B 338 ALA B 356 1 19
HELIX 56 56 ASN B 358 LEU B 369 1 12
HELIX 57 57 SER B 375 LYS B 392 1 18
HELIX 58 58 GLY B 403 LYS B 411 1 9
HELIX 59 59 ARG B 424 LEU B 431 1 8
HELIX 60 60 ASP B 443 GLY B 448 1 6
HELIX 61 61 LYS B 453 LYS B 467 1 15
HELIX 62 62 SER C 1 THR C 8 1 8
HELIX 63 63 SER C 33 GLY C 44 1 12
HELIX 64 64 SER C 56 GLY C 75 1 20
HELIX 65 65 ASP C 112 ALA C 116 5 5
HELIX 66 66 ASN C 130 VAL C 135 1 6
HELIX 67 67 SER C 190 GLY C 204 1 15
HELIX 68 68 SER C 215 GLY C 227 1 13
HELIX 69 69 ASN C 241 ASN C 247 1 7
HELIX 70 70 ASN C 247 SER C 255 1 9
HELIX 71 71 ARG C 262 ILE C 269 1 8
HELIX 72 72 PRO C 270 GLY C 289 1 20
HELIX 73 73 LEU C 299 TYR C 304 5 6
HELIX 74 74 THR C 309 GLY C 323 1 15
HELIX 75 75 SER C 330 LYS C 335 1 6
HELIX 76 76 TYR C 338 ALA C 356 1 19
HELIX 77 77 ASN C 358 LEU C 369 1 12
HELIX 78 78 SER C 375 LYS C 392 1 18
HELIX 79 79 GLY C 403 LYS C 411 1 9
HELIX 80 80 ARG C 424 LEU C 431 1 8
HELIX 81 81 ASP C 443 GLY C 448 1 6
HELIX 82 82 LYS C 453 LYS C 467 1 15
SHEET 1 A 9 ARG K 22 THR K 26 0
SHEET 2 A 9 MET K 45 ASN K 51 1 O ARG K 49 N CYS K 25
SHEET 3 A 9 ALA K 79 ASP K 83 1 O ALA K 81 N ALA K 48
SHEET 4 A 9 MET K 207 ALA K 210 1 O PHE K 209 N LEU K 82
SHEET 5 A 9 MET K 234 ILE K 239 1 O LYS K 238 N ALA K 210
SHEET 6 A 9 GLY K 257 ALA K 261 1 O MET K 259 N CYS K 237
SHEET 7 A 9 VAL K 292 ALA K 295 1 O ILE K 293 N VAL K 260
SHEET 8 A 9 CYS K 326 LEU K 329 1 O CYS K 326 N CYS K 294
SHEET 9 A 9 ARG K 22 THR K 26 1 N ILE K 24 O LEU K 329
SHEET 1 B 7 ILE K 89 ARG K 90 0
SHEET 2 B 7 GLY K 176 ASN K 178 -1 O VAL K 177 N ILE K 89
SHEET 3 B 7 TYR K 140 ILE K 143 -1 N TYR K 142 O ASN K 178
SHEET 4 B 7 LEU K 148 HIS K 155 -1 O LEU K 148 N ILE K 143
SHEET 5 B 7 THR K 160 VAL K 165 -1 O GLU K 162 N GLN K 153
SHEET 6 B 7 THR K 106 THR K 110 -1 N CYS K 107 O CYS K 163
SHEET 7 B 7 LYS K 123 TYR K 125 1 O PHE K 124 N THR K 110
SHEET 1 C 2 ASP K 98 MET K 101 0
SHEET 2 C 2 HIS K 169 SER K 172 -1 O ILE K 171 N ALA K 99
SHEET 1 D 5 VAL K 437 PHE K 441 0
SHEET 2 D 5 ILE K 418 THR K 422 1 N CYS K 420 O GLU K 438
SHEET 3 D 5 ALA K 395 LEU K 399 1 N MET K 396 O VAL K 419
SHEET 4 D 5 TYR K 475 ILE K 479 1 O VAL K 477 N VAL K 397
SHEET 5 D 5 THR K 492 LEU K 496 -1 O ARG K 493 N VAL K 478
SHEET 1 E 9 ARG A 22 THR A 26 0
SHEET 2 E 9 MET A 45 ASN A 51 1 O ARG A 49 N CYS A 25
SHEET 3 E 9 ALA A 79 ASP A 83 1 O ALA A 81 N ALA A 48
SHEET 4 E 9 MET A 207 ALA A 210 1 O PHE A 209 N LEU A 82
SHEET 5 E 9 MET A 234 ILE A 239 1 O LYS A 238 N ALA A 210
SHEET 6 E 9 GLY A 257 ALA A 261 1 O MET A 259 N CYS A 237
SHEET 7 E 9 VAL A 292 ALA A 295 1 O ILE A 293 N VAL A 260
SHEET 8 E 9 CYS A 326 LEU A 329 1 O CYS A 326 N CYS A 294
SHEET 9 E 9 ARG A 22 THR A 26 1 N ILE A 24 O LEU A 329
SHEET 1 F 2 ASP A 98 MET A 101 0
SHEET 2 F 2 HIS A 169 SER A 172 -1 O ILE A 171 N ALA A 99
SHEET 1 G 6 LYS A 123 TYR A 125 0
SHEET 2 G 6 THR A 106 THR A 110 1 N TYR A 108 O PHE A 124
SHEET 3 G 6 THR A 160 VAL A 165 -1 O CYS A 163 N CYS A 107
SHEET 4 G 6 LEU A 148 HIS A 155 -1 N SER A 154 O GLU A 162
SHEET 5 G 6 TYR A 140 ILE A 143 -1 N ILE A 143 O LEU A 148
SHEET 6 G 6 VAL A 177 ASN A 178 -1 O ASN A 178 N TYR A 142
SHEET 1 H 5 VAL A 437 PHE A 441 0
SHEET 2 H 5 ILE A 418 THR A 422 1 N CYS A 420 O GLU A 438
SHEET 3 H 5 ALA A 395 LEU A 399 1 N MET A 396 O VAL A 419
SHEET 4 H 5 TYR A 475 ILE A 479 1 O VAL A 477 N VAL A 397
SHEET 5 H 5 THR A 492 LEU A 496 -1 O ARG A 493 N VAL A 478
SHEET 1 I 9 ARG B 22 THR B 26 0
SHEET 2 I 9 MET B 45 ASN B 51 1 O ARG B 49 N CYS B 25
SHEET 3 I 9 ALA B 79 ASP B 83 1 O ALA B 79 N ALA B 48
SHEET 4 I 9 MET B 207 ALA B 210 1 O PHE B 209 N LEU B 82
SHEET 5 I 9 MET B 234 ILE B 239 1 O MET B 234 N ILE B 208
SHEET 6 I 9 GLY B 257 ALA B 261 1 O MET B 259 N CYS B 237
SHEET 7 I 9 VAL B 292 ALA B 295 1 O ILE B 293 N VAL B 260
SHEET 8 I 9 CYS B 326 LEU B 329 1 O CYS B 326 N CYS B 294
SHEET 9 I 9 ARG B 22 THR B 26 1 N ILE B 24 O LEU B 329
SHEET 1 J 2 ALA B 99 MET B 101 0
SHEET 2 J 2 HIS B 169 ILE B 171 -1 O HIS B 169 N MET B 101
SHEET 1 K 6 LYS B 123 TYR B 125 0
SHEET 2 K 6 TYR B 108 THR B 110 1 N THR B 110 O PHE B 124
SHEET 3 K 6 THR B 160 VAL B 165 -1 O LEU B 161 N VAL B 109
SHEET 4 K 6 LEU B 148 HIS B 155 -1 N GLN B 151 O THR B 164
SHEET 5 K 6 TYR B 140 ILE B 143 -1 N ILE B 143 O LEU B 148
SHEET 6 K 6 VAL B 177 ASN B 178 -1 O ASN B 178 N TYR B 142
SHEET 1 L 5 VAL B 437 PHE B 441 0
SHEET 2 L 5 ILE B 418 THR B 422 1 N CYS B 420 O GLU B 438
SHEET 3 L 5 ALA B 395 LEU B 399 1 N MET B 396 O VAL B 419
SHEET 4 L 5 TYR B 475 ILE B 479 1 O VAL B 477 N VAL B 397
SHEET 5 L 5 THR B 492 LEU B 496 -1 O ARG B 493 N VAL B 478
SHEET 1 M 9 ARG C 22 THR C 26 0
SHEET 2 M 9 MET C 45 ASN C 51 1 O ARG C 49 N CYS C 25
SHEET 3 M 9 ALA C 79 ASP C 83 1 O ALA C 79 N ALA C 48
SHEET 4 M 9 MET C 207 ALA C 210 1 O PHE C 209 N LEU C 82
SHEET 5 M 9 MET C 234 ILE C 239 1 O MET C 234 N ILE C 208
SHEET 6 M 9 GLY C 257 ALA C 261 1 O MET C 259 N CYS C 237
SHEET 7 M 9 VAL C 292 ALA C 295 1 O ILE C 293 N VAL C 260
SHEET 8 M 9 CYS C 326 LEU C 329 1 O CYS C 326 N CYS C 294
SHEET 9 M 9 ARG C 22 THR C 26 1 N ILE C 24 O LEU C 329
SHEET 1 N 2 ILE C 89 ARG C 90 0
SHEET 2 N 2 GLY C 176 VAL C 177 -1 O VAL C 177 N ILE C 89
SHEET 1 O 2 ALA C 99 MET C 101 0
SHEET 2 O 2 HIS C 169 ILE C 171 -1 O HIS C 169 N MET C 101
SHEET 1 P 5 LYS C 123 PHE C 124 0
SHEET 2 P 5 TYR C 108 THR C 110 1 N THR C 110 O PHE C 124
SHEET 3 P 5 THR C 160 VAL C 165 -1 O LEU C 161 N VAL C 109
SHEET 4 P 5 ILE C 149 HIS C 155 -1 N SER C 154 O GLU C 162
SHEET 5 P 5 ASN C 139 TYR C 142 -1 N ASN C 139 O VAL C 152
SHEET 1 Q 5 VAL C 437 PHE C 441 0
SHEET 2 Q 5 ILE C 418 THR C 422 1 N CYS C 420 O GLU C 438
SHEET 3 Q 5 ALA C 395 LEU C 399 1 N MET C 396 O VAL C 419
SHEET 4 Q 5 TYR C 475 ILE C 479 1 O VAL C 477 N VAL C 397
SHEET 5 Q 5 THR C 492 LEU C 496 -1 O ARG C 493 N VAL C 478
LINK OD1 ASN K 51 K K K 504 1555 1555 3.21
LINK OG SER K 53 K K K 504 1555 1555 2.61
LINK OD1 ASP K 83 K K K 504 1555 1555 2.99
LINK O THR K 84 K K K 504 1555 1555 2.88
LINK OG SER K 211 K K K 504 1555 1555 3.33
LINK OE1 GLU K 240 MG MG K 502 1555 1555 2.52
LINK OD2 ASP K 264 MG MG K 502 1555 1555 2.42
LINK MG MG K 500 O1B ATP K1001 1555 1555 2.37
LINK MG MG K 500 O1G ATP K1001 1555 1555 2.59
LINK MG MG K 500 O1A ATP K1001 1555 1555 2.99
LINK MG MG K 502 O4 OXL K 510 1555 1555 2.02
LINK MG MG K 502 O2G ATP K1001 1555 1555 2.67
LINK K K K 504 O3G ATP K1001 1555 1555 2.71
LINK OD1 ASN A 51 K K A 504 1555 1555 3.27
LINK OG SER A 53 K K A 504 1555 1555 2.73
LINK OD1 ASP A 83 K K A 504 1555 1555 3.07
LINK O THR A 84 K K A 504 1555 1555 2.92
LINK OG SER A 211 K K A 504 1555 1555 3.26
LINK OE1 GLU A 240 MG MG A 502 1555 1555 2.71
LINK OD2 ASP A 264 MG MG A 502 1555 1555 2.69
LINK MG MG A 500 O1G ATP A1001 1555 1555 2.18
LINK MG MG A 500 O1B ATP A1001 1555 1555 2.57
LINK MG MG A 500 O1A ATP A1001 1555 1555 2.98
LINK MG MG A 502 O4 OXL A 510 1555 1555 2.16
LINK MG MG A 502 O2G ATP A1001 1555 1555 2.30
LINK K K A 504 O3G ATP A1001 1555 1555 3.10
LINK OG SER B 53 K K B 504 1555 1555 3.07
LINK OD1 ASP B 83 K K B 504 1555 1555 2.84
LINK O THR B 84 K K B 504 1555 1555 3.05
LINK OG SER B 211 K K B 504 1555 1555 3.05
LINK OE1 GLU B 240 MG MG B 502 1555 1555 2.61
LINK OD2 ASP B 264 MG MG B 502 1555 1555 2.23
LINK MG MG B 502 O4 OXL B 510 1555 1555 2.16
LINK OD1 ASN C 51 K K C 504 1555 1555 3.10
LINK OG SER C 53 K K C 504 1555 1555 2.85
LINK OD1 ASP C 83 K K C 504 1555 1555 2.91
LINK O THR C 84 K K C 504 1555 1555 2.79
LINK OG SER C 211 K K C 504 1555 1555 3.21
LINK OE1 GLU C 240 MG MG C 502 1555 1555 2.76
LINK OD2 ASP C 264 MG MG C 502 1555 1555 2.18
LINK MG MG C 502 O4 OXL C 510 1555 1555 2.16
CISPEP 1 ILE K 372 PRO K 373 0 8.93
CISPEP 2 ILE A 372 PRO A 373 0 9.45
CISPEP 3 ILE B 372 PRO B 373 0 8.36
CISPEP 4 ILE C 372 PRO C 373 0 8.78
SITE 1 AC1 4 ASP K 145 THR K 296 OXL K 510 ATP K1001
SITE 1 AC2 5 LYS K 238 GLU K 240 ASP K 264 OXL K 510
SITE 2 AC2 5 ATP K1001
SITE 1 AC3 7 ASN K 51 SER K 53 ASP K 83 THR K 84
SITE 2 AC3 7 GLU K 88 SER K 211 ATP K1001
SITE 1 AC4 10 ARG K 49 LYS K 238 GLU K 240 ALA K 261
SITE 2 AC4 10 GLY K 263 ASP K 264 THR K 296 MG K 500
SITE 3 AC4 10 MG K 502 ATP K1001
SITE 1 AC5 17 THR K 26 PRO K 29 ARG K 49 ASN K 51
SITE 2 AC5 17 HIS K 54 TYR K 59 ARG K 90 ASP K 145
SITE 3 AC5 17 ARG K 175 LYS K 238 ASP K 264 SER K 330
SITE 4 AC5 17 LYS K 335 MG K 500 MG K 502 K K 504
SITE 5 AC5 17 OXL K 510
SITE 1 AC6 4 ASP A 145 THR A 296 OXL A 510 ATP A1001
SITE 1 AC7 5 LYS A 238 GLU A 240 ASP A 264 OXL A 510
SITE 2 AC7 5 ATP A1001
SITE 1 AC8 7 ASN A 51 SER A 53 ASP A 83 THR A 84
SITE 2 AC8 7 GLU A 88 SER A 211 ATP A1001
SITE 1 AC9 9 LYS A 238 GLU A 240 ALA A 261 GLY A 263
SITE 2 AC9 9 ASP A 264 THR A 296 MG A 500 MG A 502
SITE 3 AC9 9 ATP A1001
SITE 1 BC1 16 THR A 26 ILE A 27 ARG A 49 ASN A 51
SITE 2 BC1 16 HIS A 54 ARG A 90 ASP A 145 ARG A 175
SITE 3 BC1 16 LYS A 238 ASP A 264 SER A 330 ALA A 334
SITE 4 BC1 16 MG A 500 MG A 502 K A 504 OXL A 510
SITE 1 BC2 4 PHE B 212 GLU B 240 ASP B 264 OXL B 510
SITE 1 BC3 7 ASN B 51 SER B 53 ASP B 83 THR B 84
SITE 2 BC3 7 GLU B 88 SER B 211 LYS B 238
SITE 1 BC4 8 LYS B 238 GLU B 240 ALA B 261 GLY B 263
SITE 2 BC4 8 ASP B 264 THR B 296 MG B 502 ATP B1001
SITE 1 BC5 8 PRO B 29 ARG B 49 ASN B 51 HIS B 54
SITE 2 BC5 8 ARG B 90 ARG B 175 LYS B 335 OXL B 510
SITE 1 BC6 4 PHE C 212 GLU C 240 ASP C 264 OXL C 510
SITE 1 BC7 6 ASN C 51 SER C 53 ASP C 83 THR C 84
SITE 2 BC7 6 SER C 211 LYS C 238
SITE 1 BC8 8 LYS C 238 GLU C 240 ALA C 261 GLY C 263
SITE 2 BC8 8 ASP C 264 THR C 296 MG C 502 ATP C1001
SITE 1 BC9 7 ARG C 49 ASN C 51 HIS C 54 TYR C 59
SITE 2 BC9 7 ARG C 90 ARG C 175 OXL C 510
CRYST1 107.516 128.133 204.361 90.00 90.03 90.00 C 1 2 1 16
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 0.009301 0.000000 0.000004 0.00000
SCALE2 0.000000 0.007804 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004893 0.00000
(ATOM LINES ARE NOT SHOWN.)
END