HEADER ISOMERASE 08-OCT-01 1K4I
TITLE CRYSTAL STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE IN
TITLE 2 COMPLEX WITH TWO MAGNESIUM IONS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 5.4.99.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MAGNAPORTHE GRISEA;
SOURCE 3 ORGANISM_TAXID: 148305;
SOURCE 4 GENE: RICE BLAST FUNGI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-24A(+)
KEYWDS DIHYDROXYBUTANONE PHOSPHATE SYNTHASE, RIBOFLAVIN BIOSYNTHESIS,
KEYWDS 2 ANTIMICROBIAL TARGET, STRUCTURE-BASED DESIGN, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.-I.LIAO,Y.-J.ZHENG,P.V.VIITANEN,D.B.JORDAN
REVDAT 5 16-AUG-23 1K4I 1 REMARK LINK
REVDAT 4 13-JUL-11 1K4I 1 VERSN
REVDAT 3 24-FEB-09 1K4I 1 VERSN
REVDAT 2 01-APR-03 1K4I 1 JRNL
REVDAT 1 06-MAR-02 1K4I 0
JRNL AUTH D.I.LIAO,Y.J.ZHENG,P.V.VIITANEN,D.B.JORDAN
JRNL TITL STRUCTURAL DEFINITION OF THE ACTIVE SITE AND CATALYTIC
JRNL TITL 2 MECHANISM OF 3,4-DIHYDROXY-2-BUTANONE-4-PHOSPHATE SYNTHASE.
JRNL REF BIOCHEMISTRY V. 41 1795 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11827524
JRNL DOI 10.1021/BI015652U
REMARK 2
REMARK 2 RESOLUTION. 0.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 117491
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11665
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 117599
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1631
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 278
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.012 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.200 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : NULL
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K4I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014550.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-FEB-01
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 5ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 117559
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.980
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.27700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: TNT
REMARK 200 STARTING MODEL: 1K49 WITH WATERS REMOVED
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LI2SO4, MES-NAOH, PEG5000 MONOMETHYL
REMARK 280 ETHER, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 26.94450
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.07350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.94450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.07350
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMODIMER. APPLYING THE
REMARK 300 FOLLOWING SYMMETRY RELATED OPERATION ON THE COORDINATES OF THE
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT WOULD GENERATE THE 2ND HALF OF THE
REMARK 300 DIMER. ROTATION MATRIX -1.00000 0.00000 0.00000 0.00000 -1.00000
REMARK 300 0.00000 0.00000 0.00000 1.00000 TRANSLATION -1, -1, 0
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -129.0 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 0.00000
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 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 PRO A 2
REMARK 465 SER A 3
REMARK 465 THR A 4
REMARK 465 ASP A 5
REMARK 465 SER A 6
REMARK 465 ILE A 7
REMARK 465 PRO A 8
REMARK 465 LYS A 9
REMARK 465 SER A 10
REMARK 465 ASN A 11
REMARK 465 GLU A 228
REMARK 465 THR A 229
REMARK 465 ASN A 230
REMARK 465 GLY A 231
REMARK 465 SER A 232
REMARK 465 GLY A 233
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 1068 O HOH A 1077 2.09
REMARK 500 O HOH A 1069 O HOH A 1217 2.14
REMARK 500 N PHE A 12 O HOH A 1099 2.18
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 1114 O HOH A 1114 2555 0.87
REMARK 500 O HOH A 1227 O HOH A 1264 4456 2.17
REMARK 500 O HOH A 1083 O HOH A 1184 2555 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 37 CD GLU A 37 OE2 0.072
REMARK 500 GLU A 72 CD GLU A 72 OE2 0.066
REMARK 500 GLU A 174 CD GLU A 174 OE2 0.077
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 36 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 59 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 78 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 78 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 88 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 125 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 177 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP A 177 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP A 178 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP A 197 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 205 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 215 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
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 ARG A 36 -112.38 -106.89
REMARK 500 HIS A 85 74.93 -111.30
REMARK 500 ASN A 86 109.51 -51.77
REMARK 500 THR A 106 -95.50 -113.91
REMARK 500 PRO A 168 45.12 -78.71
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 A1003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 37 OE2
REMARK 620 2 HIS A 153 ND1 98.8
REMARK 620 3 SO4 A1001 O3 116.7 115.5
REMARK 620 4 SO4 A1001 O2 89.3 82.3 49.1
REMARK 620 5 HOH A1051 O 86.2 89.7 140.6 170.1
REMARK 620 6 HOH A1100 O 88.1 173.1 60.1 97.1 91.5
REMARK 620 7 HOH A1139 O 154.8 102.9 64.5 106.1 81.2 70.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1004 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 37 OE1
REMARK 620 2 HOH A1047 O 96.2
REMARK 620 3 HOH A1084 O 94.2 93.3
REMARK 620 4 HOH A1087 O 173.6 87.4 90.9
REMARK 620 5 HOH A1091 O 91.0 172.2 83.1 85.8
REMARK 620 6 HOH A1100 O 89.4 97.9 167.8 84.8 85.2
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 SO4 A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K49 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE
REMARK 900 (CATION FREE FORM)
DBREF 1K4I A 1 233 UNP Q8TG90 Q8TG90_MAGGR 1 233
SEQRES 1 A 233 MET PRO SER THR ASP SER ILE PRO LYS SER ASN PHE ASP
SEQRES 2 A 233 ALA ILE PRO ASP VAL ILE GLN ALA PHE LYS ASN GLY GLU
SEQRES 3 A 233 PHE VAL VAL VAL LEU ASP ASP PRO SER ARG GLU ASN GLU
SEQRES 4 A 233 ALA ASP LEU ILE ILE ALA ALA GLU SER VAL THR THR GLU
SEQRES 5 A 233 GLN MET ALA PHE MET VAL ARG HIS SER SER GLY LEU ILE
SEQRES 6 A 233 CYS ALA PRO LEU THR PRO GLU ARG THR THR ALA LEU ASP
SEQRES 7 A 233 LEU PRO GLN MET VAL THR HIS ASN ALA ASP PRO ARG GLY
SEQRES 8 A 233 THR ALA TYR THR VAL SER VAL ASP ALA GLU HIS PRO SER
SEQRES 9 A 233 THR THR THR GLY ILE SER ALA HIS ASP ARG ALA LEU ALA
SEQRES 10 A 233 CYS ARG MET LEU ALA ALA PRO ASP ALA GLN PRO SER HIS
SEQRES 11 A 233 PHE ARG ARG PRO GLY HIS VAL PHE PRO LEU ARG ALA VAL
SEQRES 12 A 233 ALA GLY GLY VAL ARG ALA ARG ARG GLY HIS THR GLU ALA
SEQRES 13 A 233 GLY VAL GLU LEU CYS ARG LEU ALA GLY LYS ARG PRO VAL
SEQRES 14 A 233 ALA VAL ILE SER GLU ILE VAL ASP ASP GLY GLN GLU VAL
SEQRES 15 A 233 GLU GLY ARG ALA VAL ARG ALA ALA PRO GLY MET LEU ARG
SEQRES 16 A 233 GLY ASP GLU CYS VAL ALA PHE ALA ARG ARG TRP GLY LEU
SEQRES 17 A 233 LYS VAL CYS THR ILE GLU ASP MET ILE ALA HIS VAL GLU
SEQRES 18 A 233 LYS THR GLU GLY LYS LEU GLU THR ASN GLY SER GLY
HET SO4 A1001 5
HET SO4 A1002 5
HET MG A1003 1
HET MG A1004 1
HETNAM SO4 SULFATE ION
HETNAM MG MAGNESIUM ION
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 MG 2(MG 2+)
FORMUL 6 HOH *278(H2 O)
HELIX 1 1 ALA A 14 ASN A 24 1 11
HELIX 2 2 GLU A 47 VAL A 49 5 3
HELIX 3 3 THR A 50 SER A 61 1 12
HELIX 4 4 THR A 70 LEU A 77 1 8
HELIX 5 5 SER A 110 ALA A 123 1 14
HELIX 6 6 GLN A 127 SER A 129 5 3
HELIX 7 7 GLY A 145 ARG A 150 1 6
HELIX 8 8 GLY A 152 ALA A 164 1 13
HELIX 9 9 ARG A 195 TRP A 206 1 12
HELIX 10 10 ILE A 213 GLY A 225 1 13
SHEET 1 A 4 ALA A 170 GLU A 174 0
SHEET 2 A 4 ALA A 40 ALA A 45 -1 N LEU A 42 O SER A 173
SHEET 3 A 4 VAL A 28 LEU A 31 -1 N VAL A 30 O ASP A 41
SHEET 4 A 4 LYS A 209 THR A 212 1 O CYS A 211 N LEU A 31
SHEET 1 B 3 CYS A 66 LEU A 69 0
SHEET 2 B 3 PHE A 131 ARG A 141 1 O LEU A 140 N LEU A 69
SHEET 3 B 3 VAL A 98 ALA A 100 -1 N ASP A 99 O ARG A 132
SHEET 1 C 2 VAL A 176 ASP A 177 0
SHEET 2 C 2 GLY A 192 MET A 193 -1 O GLY A 192 N ASP A 177
SHEET 1 D 2 GLN A 180 GLU A 181 0
SHEET 2 D 2 ARG A 188 ALA A 189 -1 O ALA A 189 N GLN A 180
LINK OE2 GLU A 37 MG MG A1003 1555 1555 2.17
LINK OE1 GLU A 37 MG MG A1004 1555 1555 1.98
LINK ND1 HIS A 153 MG MG A1003 1555 1555 2.22
LINK O3 SO4 A1001 MG MG A1003 1555 1555 3.10
LINK O2 SO4 A1001 MG MG A1003 1555 1555 2.41
LINK MG MG A1003 O HOH A1051 1555 1555 2.35
LINK MG MG A1003 O HOH A1100 1555 1555 1.82
LINK MG MG A1003 O HOH A1139 1555 1555 2.27
LINK MG MG A1004 O HOH A1047 1555 1555 2.11
LINK MG MG A1004 O HOH A1084 1555 2555 2.01
LINK MG MG A1004 O HOH A1087 1555 2555 2.30
LINK MG MG A1004 O HOH A1091 1555 1555 2.02
LINK MG MG A1004 O HOH A1100 1555 1555 2.08
CISPEP 1 ARG A 133 PRO A 134 0 -2.28
SITE 1 AC1 12 ARG A 36 GLU A 37 THR A 92 ARG A 150
SITE 2 AC1 12 GLY A 152 HIS A 153 THR A 154 MG A1003
SITE 3 AC1 12 HOH A1075 HOH A1091 HOH A1100 HOH A1139
SITE 1 AC2 5 GLN A 81 ARG A 141 ARG A 205 HOH A1105
SITE 2 AC2 5 HOH A1131
SITE 1 AC3 7 GLU A 37 HIS A 153 SO4 A1001 MG A1004
SITE 2 AC3 7 HOH A1051 HOH A1100 HOH A1139
SITE 1 AC4 7 GLU A 37 MG A1003 HOH A1047 HOH A1084
SITE 2 AC4 7 HOH A1087 HOH A1091 HOH A1100
CRYST1 53.889 88.147 43.995 90.00 90.00 90.00 P 21 21 2 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 0.018557 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011345 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022730 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
