HEADER OXIDOREDUCTASE 29-MAR-05 2BNN
TITLE THE STRUCTURE OF HYDROXYPROPYLPHOSPHONIC ACID EPOXIDASE FROM S.
TITLE 2 WEDMORENIS IN COMPLEX WITH FOSFOMYCIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HYDROXYPROPYLPHOSPHONIC ACID EPOXIDASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES WEDMORENSIS;
SOURCE 3 ORGANISM_TAXID: 43759;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS OXIDOREDUCTASE, EPOXIDASE, CUPIN, HTH, CATION-DEPENDANT, ZINC,
KEYWDS 2 FOSFOMYCIN OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MCLUSKEY,S.CAMERON,W.N.HUNTER
REVDAT 6 28-JUN-17 2BNN 1 REMARK
REVDAT 5 05-MAY-09 2BNN 1 TITLE REMARK
REVDAT 4 24-FEB-09 2BNN 1 VERSN
REVDAT 3 08-MAR-06 2BNN 1 REMARK
REVDAT 2 12-OCT-05 2BNN 1 JRNL
REVDAT 1 05-OCT-05 2BNN 0
JRNL AUTH K.MCLUSKEY,S.CAMERON,F.HAMMERSCHMIDT,W.N.HUNTER
JRNL TITL STRUCTURE AND REACTIVITY OF HYDROXYPROPYLPHOSPHONIC ACID
JRNL TITL 2 EPOXIDASE IN FOSFOMYCIN BIOSYNTHESIS BY A CATION- AND
JRNL TITL 3 FLAVIN-DEPENDENT MECHANISM.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 14221 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 16186494
JRNL DOI 10.1073/PNAS.0504314102
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.CAMERON,K.MCLUSKEY,R.CHAMBERLAYNE,I.HALLYBURTON,W.N.HUNTER
REMARK 1 TITL INITIATING A CRYSTALLOGRAPHIC ANALYSIS OF RECOMBINANT
REMARK 1 TITL 2 (S)-2-HYDROXYPROPYLPHOSPHONIC ACID EPOXIDASE FROM
REMARK 1 TITL 3 STREPTOMYCES WEDMORENSIS.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 61 534 2005
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 16511089
REMARK 1 DOI 10.1107/S1744309105012376
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 16024
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 847
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1138
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE SET COUNT : 56
REMARK 3 BIN FREE R VALUE : 0.3580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2902
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 243
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.91000
REMARK 3 B22 (A**2) : 0.91000
REMARK 3 B33 (A**2) : -1.36000
REMARK 3 B12 (A**2) : 0.45000
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): 0.477
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.310
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.227
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.514
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3039 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4139 ; 1.262 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 380 ; 6.685 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 136 ;37.864 ;25.294
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 505 ;15.955 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;12.829 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 478 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2293 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1451 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2057 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 248 ; 0.141 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 110 ; 0.186 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.164 ; 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): 1959 ; 1.453 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3092 ; 2.467 ; 8.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1191 ; 4.788 ;10.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1041 ; 6.085 ;10.000
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 : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. RESIDUES 97-101 ARE DISORDERED IN SUBUNIT B
REMARK 4
REMARK 4 2BNN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1290023058.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
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 : 81586
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.67000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: STARTING MODEL IS CURRENTLY BEING SUBMITTED AND HENCE HAS
REMARK 200 NOT PDB-CODE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M AMMONIUM SULPHATE, 100 MM TRIS
REMARK 280 PH 7.5, PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 145.32600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 72.66300
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 108.99450
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 36.33150
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 181.65750
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 145.32600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 72.66300
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 36.33150
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 108.99450
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 181.65750
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -254.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 148.26701
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 SER A 2
REMARK 465 ASN A 3
REMARK 465 THR A 4
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ASN B 3
REMARK 465 THR B 4
REMARK 465 ARG B 97
REMARK 465 ASP B 98
REMARK 465 ASN B 99
REMARK 465 VAL B 100
REMARK 465 ASP B 101
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 ASP A 98 -113.57 -97.05
REMARK 500 ALA A 114 70.47 -150.26
REMARK 500 HIS A 177 -3.70 57.65
REMARK 500 LYS A 186 115.28 -39.39
REMARK 500 ASP B 80 56.44 36.02
REMARK 500 ASP B 88 36.64 -98.30
REMARK 500 ALA B 114 72.30 -156.40
REMARK 500 LEU B 117 108.33 -58.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2016 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH A2051 DISTANCE = 6.11 ANGSTROMS
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 ZN A1200 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 138 NE2
REMARK 620 2 GLU A 142 OE2 115.2
REMARK 620 3 HIS A 180 NE2 101.3 112.6
REMARK 620 4 FCN A1199 O3P 77.9 128.1 113.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1200 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 180 NE2
REMARK 620 2 HIS B 138 NE2 98.8
REMARK 620 3 FCN B1199 O 116.5 139.3
REMARK 620 4 FCN B1199 O3P 101.1 85.9 68.8
REMARK 620 5 GLU B 142 OE1 104.2 108.9 82.6 148.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FCN A 1199
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FCN B 1199
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZZ9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FEII HPPE
REMARK 900 RELATED ID: 1ZZ7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FEII HPPE IN COMPLEX WITH SUBSTRATEFORM 1
REMARK 900 RELATED ID: 2BNM RELATED DB: PDB
REMARK 900 THE STRUCTURE OF HYDROXYPROPYLPHOSPHONIC ACID EPOXIDASE FROM S.
REMARK 900 WEDMORENIS.
REMARK 900 RELATED ID: 1ZZ8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF FEII HPPE IN COMPLEX WITH SUBSTRATEFORM 2
REMARK 900 RELATED ID: 1ZZ6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APO-HPPE
REMARK 900 RELATED ID: 1ZZC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF COII HPPE IN COMPLEX WITH TRIS BUFFER
REMARK 900 RELATED ID: 1ZZB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF COII HPPE IN COMPLEX WITH SUBSTRATE
REMARK 900 RELATED ID: 2BNO RELATED DB: PDB
REMARK 900 THE STRUCTURE OF HYDROXYPROPYLPHOSPHONIC ACID EPOXIDASE FROM S.
REMARK 900 WEDMORENIS.
DBREF 2BNN A 1 198 UNP Q56185 Q56185_STRWE 1 198
DBREF 2BNN B 1 198 UNP Q56185 Q56185_STRWE 1 198
SEQRES 1 A 198 MET SER ASN THR LYS THR ALA SER THR GLY PHE ALA GLU
SEQRES 2 A 198 LEU LEU LYS ASP ARG ARG GLU GLN VAL LYS MET ASP HIS
SEQRES 3 A 198 ALA ALA LEU ALA SER LEU LEU GLY GLU THR PRO GLU THR
SEQRES 4 A 198 VAL ALA ALA TRP GLU ASN GLY GLU GLY GLY GLU LEU THR
SEQRES 5 A 198 LEU THR GLN LEU GLY ARG ILE ALA HIS VAL LEU GLY THR
SEQRES 6 A 198 SER ILE GLY ALA LEU THR PRO PRO ALA GLY ASN ASP LEU
SEQRES 7 A 198 ASP ASP GLY VAL ILE ILE GLN MET PRO ASP GLU ARG PRO
SEQRES 8 A 198 ILE LEU LYS GLY VAL ARG ASP ASN VAL ASP TYR TYR VAL
SEQRES 9 A 198 TYR ASN CYS LEU VAL ARG THR LYS ARG ALA PRO SER LEU
SEQRES 10 A 198 VAL PRO LEU VAL VAL ASP VAL LEU THR ASP ASN PRO ASP
SEQRES 11 A 198 ASP ALA LYS PHE ASN SER GLY HIS ALA GLY ASN GLU PHE
SEQRES 12 A 198 LEU PHE VAL LEU GLU GLY GLU ILE HIS MET LYS TRP GLY
SEQRES 13 A 198 ASP LYS GLU ASN PRO LYS GLU ALA LEU LEU PRO THR GLY
SEQRES 14 A 198 ALA SER MET PHE VAL GLU GLU HIS VAL PRO HIS ALA PHE
SEQRES 15 A 198 THR ALA ALA LYS GLY THR GLY SER ALA LYS LEU ILE ALA
SEQRES 16 A 198 VAL ASN PHE
SEQRES 1 B 198 MET SER ASN THR LYS THR ALA SER THR GLY PHE ALA GLU
SEQRES 2 B 198 LEU LEU LYS ASP ARG ARG GLU GLN VAL LYS MET ASP HIS
SEQRES 3 B 198 ALA ALA LEU ALA SER LEU LEU GLY GLU THR PRO GLU THR
SEQRES 4 B 198 VAL ALA ALA TRP GLU ASN GLY GLU GLY GLY GLU LEU THR
SEQRES 5 B 198 LEU THR GLN LEU GLY ARG ILE ALA HIS VAL LEU GLY THR
SEQRES 6 B 198 SER ILE GLY ALA LEU THR PRO PRO ALA GLY ASN ASP LEU
SEQRES 7 B 198 ASP ASP GLY VAL ILE ILE GLN MET PRO ASP GLU ARG PRO
SEQRES 8 B 198 ILE LEU LYS GLY VAL ARG ASP ASN VAL ASP TYR TYR VAL
SEQRES 9 B 198 TYR ASN CYS LEU VAL ARG THR LYS ARG ALA PRO SER LEU
SEQRES 10 B 198 VAL PRO LEU VAL VAL ASP VAL LEU THR ASP ASN PRO ASP
SEQRES 11 B 198 ASP ALA LYS PHE ASN SER GLY HIS ALA GLY ASN GLU PHE
SEQRES 12 B 198 LEU PHE VAL LEU GLU GLY GLU ILE HIS MET LYS TRP GLY
SEQRES 13 B 198 ASP LYS GLU ASN PRO LYS GLU ALA LEU LEU PRO THR GLY
SEQRES 14 B 198 ALA SER MET PHE VAL GLU GLU HIS VAL PRO HIS ALA PHE
SEQRES 15 B 198 THR ALA ALA LYS GLY THR GLY SER ALA LYS LEU ILE ALA
SEQRES 16 B 198 VAL ASN PHE
HET FCN A1199 8
HET ZN A1200 1
HET FCN B1199 8
HET ZN B1200 1
HETNAM FCN FOSFOMYCIN
HETNAM ZN ZINC ION
HETSYN FCN 1,2-EPOXYPROPYLPHOSPHONIC ACID
FORMUL 3 FCN 2(C3 H7 O4 P)
FORMUL 4 ZN 2(ZN 2+)
FORMUL 7 HOH *243(H2 O)
HELIX 1 1 LYS A 5 VAL A 22 1 18
HELIX 2 2 ASP A 25 LEU A 33 1 9
HELIX 3 3 THR A 36 GLU A 44 1 9
HELIX 4 4 THR A 52 LEU A 63 1 12
HELIX 5 5 ILE A 67 THR A 71 5 5
HELIX 6 6 MET A 86 ARG A 90 5 5
HELIX 7 7 ASN A 128 ALA A 132 5 5
HELIX 8 8 THR B 6 VAL B 22 1 17
HELIX 9 9 ASP B 25 LEU B 32 1 8
HELIX 10 10 THR B 36 GLU B 44 1 9
HELIX 11 11 THR B 52 LEU B 63 1 12
HELIX 12 12 SER B 66 THR B 71 1 6
HELIX 13 13 MET B 86 ARG B 90 5 5
HELIX 14 14 ASN B 128 ALA B 132 5 5
SHEET 1 AA 6 ILE A 92 VAL A 96 0
SHEET 2 AA 6 ASP A 101 CYS A 107 -1 N TYR A 102 O GLY A 95
SHEET 3 AA 6 VAL A 118 VAL A 124 -1 O VAL A 121 N ASN A 106
SHEET 4 AA 6 ALA A 191 PHE A 198 -1 O ALA A 191 N VAL A 124
SHEET 5 AA 6 ASN A 141 GLU A 148 -1 O ASN A 141 N PHE A 198
SHEET 6 AA 6 SER A 171 VAL A 174 -1 O MET A 172 N LEU A 144
SHEET 1 AB 3 LYS A 162 PRO A 167 0
SHEET 2 AB 3 GLU A 150 TRP A 155 -1 O ILE A 151 N LEU A 166
SHEET 3 AB 3 HIS A 180 ALA A 184 -1 O ALA A 181 N LYS A 154
SHEET 1 BA 6 ILE B 92 LEU B 93 0
SHEET 2 BA 6 TYR B 103 CYS B 107 -1 O TYR B 105 N LEU B 93
SHEET 3 BA 6 VAL B 118 VAL B 124 -1 O VAL B 121 N ASN B 106
SHEET 4 BA 6 ALA B 191 PHE B 198 -1 O ALA B 191 N VAL B 124
SHEET 5 BA 6 ASN B 141 GLU B 148 -1 O ASN B 141 N PHE B 198
SHEET 6 BA 6 SER B 171 VAL B 174 -1 O MET B 172 N LEU B 144
SHEET 1 BB 3 LYS B 162 LEU B 166 0
SHEET 2 BB 3 ILE B 151 TRP B 155 -1 O ILE B 151 N LEU B 166
SHEET 3 BB 3 HIS B 180 ALA B 184 -1 O ALA B 181 N LYS B 154
LINK ZN ZN A1200 NE2 HIS A 138 1555 1555 2.17
LINK ZN ZN A1200 OE2 GLU A 142 1555 1555 2.04
LINK ZN ZN A1200 NE2 HIS A 180 1555 1555 2.11
LINK ZN ZN A1200 O3P FCN A1199 1555 1555 2.09
LINK ZN ZN B1200 NE2 HIS B 180 1555 1555 2.19
LINK ZN ZN B1200 NE2 HIS B 138 1555 1555 2.07
LINK ZN ZN B1200 O FCN B1199 1555 1555 2.69
LINK ZN ZN B1200 O3P FCN B1199 1555 1555 2.05
LINK ZN ZN B1200 OE1 GLU B 142 1555 1555 1.96
CISPEP 1 GLY B 95 VAL B 96 0 -2.17
SITE 1 AC1 4 HIS A 138 GLU A 142 HIS A 180 FCN A1199
SITE 1 AC2 4 HIS B 138 GLU B 142 HIS B 180 FCN B1199
SITE 1 AC3 11 ARG A 97 TYR A 105 ASN A 135 HIS A 138
SITE 2 AC3 11 GLU A 142 HIS A 180 PHE A 182 ALA A 195
SITE 3 AC3 11 ZN A1200 HOH A2123 LYS B 23
SITE 1 AC4 8 LYS A 23 TYR B 105 ASN B 135 HIS B 138
SITE 2 AC4 8 GLU B 142 HIS B 180 ZN B1200 HOH B2120
CRYST1 85.602 85.602 217.989 90.00 90.00 120.00 P 65 2 2 24
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 0.011682 0.006745 0.000000 0.00000
SCALE2 0.000000 0.013489 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004587 0.00000
MTRIX1 1 -0.999930 0.005650 -0.010690 -4.21315 1
MTRIX2 1 -0.009130 -0.932200 0.361820 145.03496 1
MTRIX3 1 -0.007920 0.361890 0.932190 -26.93200 1
(ATOM LINES ARE NOT SHOWN.)
END
