HEADER TRANSFERASE 17-APR-08 3CV1
TITLE ATOMIC RESOLUTION STRUCTURES OF ESCHERICHIA COLI AND BACILLIS
TITLE 2 ANTHRACIS MALATE SYNTHASE A: COMPARISON WITH ISOFORM G AND
TITLE 3 IMPLICATIONS FOR STRUCTURE BASED DRUG DESIGN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MALATE SYNTHASE A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MSA;
COMPND 5 EC: 2.3.3.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ACEB, MAS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBAD
KEYWDS MALATE SYNTHASE, TIM BARREL, GLYOXYLATE BYPASS, TRANSFERASE,
KEYWDS 2 TRICARBOXYLIC ACID CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.LOHMAN
REVDAT 5 21-FEB-24 3CV1 1 REMARK LINK
REVDAT 4 25-OCT-17 3CV1 1 REMARK
REVDAT 3 13-JUL-11 3CV1 1 VERSN
REVDAT 2 24-FEB-09 3CV1 1 VERSN
REVDAT 1 11-NOV-08 3CV1 0
JRNL AUTH J.R.LOHMAN,A.C.OLSON,S.J.REMINGTON
JRNL TITL ATOMIC RESOLUTION STRUCTURES OF ESCHERICHIA COLI AND
JRNL TITL 2 BACILLUS ANTHRACIS MALATE SYNTHASE A: COMPARISON WITH
JRNL TITL 3 ISOFORM G AND IMPLICATIONS FOR STRUCTURE-BASED DRUG
JRNL TITL 4 DISCOVERY
JRNL REF PROTEIN SCI. V. 17 1935 2008
JRNL REFN ISSN 0961-8368
JRNL PMID 18714089
JRNL DOI 10.1110/PS.036269.108
REMARK 2
REMARK 2 RESOLUTION. 1.68 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) : 1.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 56011
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2970
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) : 1.68
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.73
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3877
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.4020
REMARK 3 BIN FREE R VALUE SET COUNT : 215
REMARK 3 BIN FREE R VALUE : 0.4850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4187
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 504
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.110
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.105
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.065
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.914
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4348 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5913 ; 1.223 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 546 ; 5.525 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 211 ;31.744 ;24.171
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 731 ;12.007 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;14.279 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 648 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3358 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2173 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3009 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 376 ; 0.112 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.185 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 53 ; 0.176 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 30 ; 0.134 ; 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): 2752 ; 0.656 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4311 ; 1.014 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1829 ; 1.764 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1596 ; 2.688 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3CV1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-08.
REMARK 100 THE DEPOSITION ID IS D_1000047244.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59002
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.680
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
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) : 1.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
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: SIRAS
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 7.5, 0.2M CALCIUM
REMARK 280 ACETATE, 22% PEG 8K, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 37.06200
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 THR A 2
REMARK 465 GLU A 3
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 GLN A 4 N CA CB CG CD OE1 NE2
REMARK 470 GLU A 69 CD OE1 OE2
REMARK 470 LYS A 101 NZ
REMARK 470 GLU A 149 CG CD OE1 OE2
REMARK 470 LYS A 157 CG CD CE NZ
REMARK 470 LYS A 337 CB CG CD CE NZ
REMARK 470 GLU A 339 CG CD OE1 OE2
REMARK 470 GLU A 340 CG CD OE1 OE2
REMARK 470 GLU A 496 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 608 O HOH A 972 1.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 830 O HOH A 980 2755 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 119 -123.48 -100.86
REMARK 500 SER A 207 -148.05 -108.06
REMARK 500 PRO A 296 -168.19 -73.75
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 CA A 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 53 OE1
REMARK 620 2 GLN A 56 OE1 82.1
REMARK 620 3 HOH A 684 O 81.0 88.8
REMARK 620 4 HOH A 718 O 74.5 88.9 155.4
REMARK 620 5 HOH A 814 O 80.8 162.1 83.4 91.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 534 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 250 OE1
REMARK 620 2 ASP A 278 OD2 86.5
REMARK 620 3 HOH A 541 O 94.4 178.9
REMARK 620 4 HOH A 657 O 80.0 86.5 94.2
REMARK 620 5 HOH A 688 O 98.9 92.5 86.8 178.6
REMARK 620 6 HOH A 971 O 170.6 89.2 90.0 91.3 89.7
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 CA A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 534
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 535
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 536
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D8C RELATED DB: PDB
REMARK 900 ISOFORM
REMARK 900 RELATED ID: 3CUX RELATED DB: PDB
REMARK 900 RELATED ID: 3CUZ RELATED DB: PDB
REMARK 900 RELATED ID: 3CV2 RELATED DB: PDB
DBREF 3CV1 A 2 533 UNP P08997 MASY_ECOLI 2 533
SEQRES 1 A 532 THR GLU GLN ALA THR THR THR ASP GLU LEU ALA PHE THR
SEQRES 2 A 532 ARG PRO TYR GLY GLU GLN GLU LYS GLN ILE LEU THR ALA
SEQRES 3 A 532 GLU ALA VAL GLU PHE LEU THR GLU LEU VAL THR HIS PHE
SEQRES 4 A 532 THR PRO GLN ARG ASN LYS LEU LEU ALA ALA ARG ILE GLN
SEQRES 5 A 532 GLN GLN GLN ASP ILE ASP ASN GLY THR LEU PRO ASP PHE
SEQRES 6 A 532 ILE SER GLU THR ALA SER ILE ARG ASP ALA ASP TRP LYS
SEQRES 7 A 532 ILE ARG GLY ILE PRO ALA ASP LEU GLU ASP ARG ARG VAL
SEQRES 8 A 532 GLU ILE THR GLY PRO VAL GLU ARG LYS MET VAL ILE ASN
SEQRES 9 A 532 ALA LEU ASN ALA ASN VAL LYS VAL PHE MET ALA ASP PHE
SEQRES 10 A 532 GLU ASP SER LEU ALA PRO ASP TRP ASN LYS VAL ILE ASP
SEQRES 11 A 532 GLY GLN ILE ASN LEU ARG ASP ALA VAL ASN GLY THR ILE
SEQRES 12 A 532 SER TYR THR ASN GLU ALA GLY LYS ILE TYR GLN LEU LYS
SEQRES 13 A 532 PRO ASN PRO ALA VAL LEU ILE CYS ARG VAL ARG GLY LEU
SEQRES 14 A 532 HIS LEU PRO GLU LYS HIS VAL THR TRP ARG GLY GLU ALA
SEQRES 15 A 532 ILE PRO GLY SER LEU PHE ASP PHE ALA LEU TYR PHE PHE
SEQRES 16 A 532 HIS ASN TYR GLN ALA LEU LEU ALA LYS GLY SER GLY PRO
SEQRES 17 A 532 TYR PHE TYR LEU PRO LYS THR GLN SER TRP GLN GLU ALA
SEQRES 18 A 532 ALA TRP TRP SER GLU VAL PHE SER TYR ALA GLU ASP ARG
SEQRES 19 A 532 PHE ASN LEU PRO ARG GLY THR ILE LYS ALA THR LEU LEU
SEQRES 20 A 532 ILE GLU THR LEU PRO ALA VAL PHE GLN MET ASP GLU ILE
SEQRES 21 A 532 LEU HIS ALA LEU ARG ASP HIS ILE VAL GLY LEU ASN CYS
SEQRES 22 A 532 GLY ARG TRP ASP TYR ILE PHE SER TYR ILE LYS THR LEU
SEQRES 23 A 532 LYS ASN TYR PRO ASP ARG VAL LEU PRO ASP ARG GLN ALA
SEQRES 24 A 532 VAL THR MET ASP LYS PRO PHE LEU ASN ALA TYR SER ARG
SEQRES 25 A 532 LEU LEU ILE LYS THR CYS HIS LYS ARG GLY ALA PHE ALA
SEQRES 26 A 532 MET GLY GLY MET ALA ALA PHE ILE PRO SER LYS ASP GLU
SEQRES 27 A 532 GLU HIS ASN ASN GLN VAL LEU ASN LYS VAL LYS ALA ASP
SEQRES 28 A 532 LYS SER LEU GLU ALA ASN ASN GLY HIS ASP GLY THR TRP
SEQRES 29 A 532 ILE ALA HIS PRO GLY LEU ALA ASP THR ALA MET ALA VAL
SEQRES 30 A 532 PHE ASN ASP ILE LEU GLY SER ARG LYS ASN GLN LEU GLU
SEQRES 31 A 532 VAL MET ARG GLU GLN ASP ALA PRO ILE THR ALA ASP GLN
SEQRES 32 A 532 LEU LEU ALA PRO CYS ASP GLY GLU ARG THR GLU GLU GLY
SEQRES 33 A 532 MET ARG ALA ASN ILE ARG VAL ALA VAL GLN TYR ILE GLU
SEQRES 34 A 532 ALA TRP ILE SER GLY ASN GLY CYS VAL PRO ILE TYR GLY
SEQRES 35 A 532 LEU MET GLU ASP ALA ALA THR ALA GLU ILE SER ARG THR
SEQRES 36 A 532 SER ILE TRP GLN TRP ILE HIS HIS GLN LYS THR LEU SER
SEQRES 37 A 532 ASN GLY LYS PRO VAL THR LYS ALA LEU PHE ARG GLN MET
SEQRES 38 A 532 LEU GLY GLU GLU MET LYS VAL ILE ALA SER GLU LEU GLY
SEQRES 39 A 532 GLU GLU ARG PHE SER GLN GLY ARG PHE ASP ASP ALA ALA
SEQRES 40 A 532 ARG LEU MET GLU GLN ILE THR THR SER ASP GLU LEU ILE
SEQRES 41 A 532 ASP PHE LEU THR LEU PRO GLY TYR ARG LEU LEU ALA
HET CA A 1 1
HET CA A 534 1
HET ACT A 535 4
HET GOL A 536 6
HETNAM CA CALCIUM ION
HETNAM ACT ACETATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 CA 2(CA 2+)
FORMUL 4 ACT C2 H3 O2 1-
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *504(H2 O)
HELIX 1 1 GLY A 18 LEU A 25 1 8
HELIX 2 2 THR A 26 ASN A 60 1 35
HELIX 3 3 THR A 70 ASP A 75 1 6
HELIX 4 4 PRO A 84 GLU A 88 5 5
HELIX 5 5 GLU A 99 ASN A 108 1 10
HELIX 6 6 ASP A 125 ASN A 141 1 17
HELIX 7 7 GLY A 186 LYS A 205 1 20
HELIX 8 8 SER A 218 PHE A 236 1 19
HELIX 9 9 THR A 251 PHE A 256 1 6
HELIX 10 10 GLN A 257 LEU A 265 1 9
HELIX 11 11 ARG A 276 LEU A 287 1 12
HELIX 12 12 ASP A 297 VAL A 301 5 5
HELIX 13 13 LYS A 305 ARG A 322 1 18
HELIX 14 14 ASP A 338 GLY A 360 1 23
HELIX 15 15 HIS A 368 GLY A 370 5 3
HELIX 16 16 LEU A 371 GLY A 384 1 14
HELIX 17 17 THR A 401 ALA A 407 1 7
HELIX 18 18 THR A 414 SER A 434 1 21
HELIX 19 19 ASP A 447 HIS A 464 1 18
HELIX 20 20 THR A 475 GLY A 495 1 21
HELIX 21 21 GLY A 495 GLN A 501 1 7
HELIX 22 22 ARG A 503 SER A 517 1 15
HELIX 23 23 LEU A 524 ARG A 530 1 7
SHEET 1 A 3 ALA A 12 PHE A 13 0
SHEET 2 A 3 PRO A 173 TRP A 179 -1 O THR A 178 N ALA A 12
SHEET 3 A 3 GLU A 182 PRO A 185 -1 O GLU A 182 N TRP A 179
SHEET 1 B 9 VAL A 92 PRO A 97 0
SHEET 2 B 9 VAL A 113 ASP A 117 1 O MET A 115 N ILE A 94
SHEET 3 B 9 VAL A 162 ARG A 166 1 O ARG A 166 N ALA A 116
SHEET 4 B 9 TYR A 210 LEU A 213 1 O TYR A 210 N CYS A 165
SHEET 5 B 9 LYS A 244 LEU A 248 1 O THR A 246 N LEU A 213
SHEET 6 B 9 ILE A 269 ASN A 273 1 O GLY A 271 N LEU A 247
SHEET 7 B 9 PHE A 325 ALA A 331 1 O MET A 327 N LEU A 272
SHEET 8 B 9 GLY A 363 ILE A 366 1 O GLY A 363 N GLY A 328
SHEET 9 B 9 VAL A 92 PRO A 97 1 N GLU A 93 O THR A 364
SHEET 1 C 2 SER A 145 THR A 147 0
SHEET 2 C 2 ILE A 153 GLN A 155 -1 O TYR A 154 N TYR A 146
SHEET 1 D 2 VAL A 439 ILE A 441 0
SHEET 2 D 2 LEU A 444 GLU A 446 -1 O LEU A 444 N ILE A 441
LINK CA CA A 1 OE1 GLN A 53 1555 1555 2.45
LINK CA CA A 1 OE1 GLN A 56 1555 1555 2.24
LINK CA CA A 1 O HOH A 684 1555 1555 2.34
LINK CA CA A 1 O HOH A 718 1555 1555 2.47
LINK CA CA A 1 O HOH A 814 1555 1555 2.44
LINK OE1 GLU A 250 CA CA A 534 1555 1555 2.46
LINK OD2 ASP A 278 CA CA A 534 1555 1555 2.36
LINK CA CA A 534 O HOH A 541 1555 1555 2.31
LINK CA CA A 534 O HOH A 657 1555 1555 2.33
LINK CA CA A 534 O HOH A 688 1555 1555 2.50
LINK CA CA A 534 O HOH A 971 1555 1555 2.04
SITE 1 AC1 5 GLN A 53 GLN A 56 HOH A 684 HOH A 718
SITE 2 AC1 5 HOH A 814
SITE 1 AC2 6 GLU A 250 ASP A 278 HOH A 541 HOH A 657
SITE 2 AC2 6 HOH A 688 HOH A 971
SITE 1 AC3 4 PHE A 13 TYR A 17 HOH A 870 HOH A 987
SITE 1 AC4 6 ILE A 73 TRP A 219 HIS A 263 ALA A 264
SITE 2 AC4 6 HOH A 784 HOH A 907
CRYST1 52.031 74.124 71.917 90.00 97.82 90.00 P 1 21 1 2
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 0.019219 0.000000 0.002639 0.00000
SCALE2 0.000000 0.013491 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014035 0.00000
(ATOM LINES ARE NOT SHOWN.)
END