HEADER OXIDOREDUCTASE 16-SEP-03 1UOB
TITLE DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH 2-OXOGLUTARATE AND
TITLE 2 PENICILLIN G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEACETOXYCEPHALOSPORIN C SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DAOCS, EXPANDASE;
COMPND 5 EC: 1.14.20.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES CLAVULIGERUS;
SOURCE 3 ORGANISM_TAXID: 1901;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS OXIDOREDUCTASE, ANTIBIOTIC BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR K.VALEGARD,A.C.TERWISSCHA VAN SCHELTINGA,A.DUBUS,L.M.OSTER,
AUTHOR 2 G.RHANGINO,J.HAJDU,I.ANDERSSON
REVDAT 5 13-DEC-23 1UOB 1 REMARK LINK
REVDAT 4 17-JAN-18 1UOB 1 AUTHOR JRNL REMARK
REVDAT 3 22-DEC-09 1UOB 1 VERSN
REVDAT 2 24-FEB-09 1UOB 1 VERSN
REVDAT 1 09-JAN-04 1UOB 0
JRNL AUTH K.VALEGARD,A.C.TERWISSCHA VAN SCHELTINGA,A.DUBUS,G.RANGHINO,
JRNL AUTH 2 L.M.OSTER,J.HAJDU,I.ANDERSSON
JRNL TITL THE STRUCTURAL BASIS OF CEPHALOSPORIN FORMATION IN A
JRNL TITL 2 MONONUCLEAR FERROUS ENZYME
JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 95 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 14718929
JRNL DOI 10.1038/NSMB712
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 30873
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1435
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2192
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 156
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.00000
REMARK 3 B22 (A**2) : -1.00000
REMARK 3 B33 (A**2) : 1.49000
REMARK 3 B12 (A**2) : -0.50000
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): 0.122
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.125
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.081
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.404
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE RESIDUES MISSING IN THE PDB ENTRY
REMARK 3 (80-96,168-177 AND 310-311) ARE DISORDERED, AND THEREFORE
REMARK 3 OMITTED FROM THE MODEL
REMARK 4
REMARK 4 1UOB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1290013479.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-03
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) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.092
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 : 30873
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 56.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.08500
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) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.23100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1RXF
REMARK 200
REMARK 200 REMARK: THE DATA WERE COLLECTED FROM A MEROHEDRALLY TWINNED
REMARK 200 CRYSTAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.75M AMMONIUM SULPHATE, 5MM 2
REMARK 280 -OXOGLUTARATE,0.1M HEPES PH7.5, PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 53.30000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.77277
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 23.86667
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 53.30000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 30.77277
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 23.86667
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 53.30000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 30.77277
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 23.86667
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 61.54554
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 47.73333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 61.54554
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 47.73333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 61.54554
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 47.73333
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.2 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 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2053 LIES ON A SPECIAL POSITION.
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 LEU A 80
REMARK 465 GLU A 81
REMARK 465 SER A 82
REMARK 465 GLU A 83
REMARK 465 SER A 84
REMARK 465 THR A 85
REMARK 465 ALA A 86
REMARK 465 GLN A 87
REMARK 465 ILE A 88
REMARK 465 THR A 89
REMARK 465 ASN A 90
REMARK 465 THR A 91
REMARK 465 GLY A 92
REMARK 465 SER A 93
REMARK 465 TYR A 94
REMARK 465 SER A 95
REMARK 465 ASP A 96
REMARK 465 PRO A 168
REMARK 465 GLU A 169
REMARK 465 HIS A 170
REMARK 465 ARG A 171
REMARK 465 SER A 172
REMARK 465 ALA A 173
REMARK 465 GLU A 174
REMARK 465 GLU A 175
REMARK 465 GLN A 176
REMARK 465 PRO A 177
REMARK 465 LYS A 310
REMARK 465 ALA A 311
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 ARG A 249 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 250 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 251 CG OD1 OD2
REMARK 470 ILE A 253 CG1 CG2 CD1
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 2144 O HOH A 2145 2.01
REMARK 500 O HOH A 2118 O HOH A 2152 2.03
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 VAL A 70 CB VAL A 70 CG2 -0.163
REMARK 500 TRP A 119 CB TRP A 119 CG -0.111
REMARK 500 GLU A 150 CD GLU A 150 OE1 0.066
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 23 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 23 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 75 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASP A 107 CB - CG - OD2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 TYR A 127 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 135 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ASP A 146 CB - CG - OD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ASP A 154 CB - CG - OD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG A 162 CG - CD - NE ANGL. DEV. = -13.1 DEGREES
REMARK 500 ARG A 162 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 162 NE - CZ - NH2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG A 258 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP A 270 CB - CG - OD1 ANGL. DEV. = 8.2 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 SER A 98 160.04 152.50
REMARK 500 CYS A 155 -140.82 -133.16
REMARK 500 ARG A 179 -48.17 128.68
REMARK 500 ARG A 250 -38.00 77.58
REMARK 500 ASP A 251 -8.31 -56.99
REMARK 500 GLN A 252 26.00 -140.00
REMARK 500 SER A 286 72.75 -115.50
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 FE2 A1310 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 183 NE2
REMARK 620 2 ASP A 185 OD1 91.4
REMARK 620 3 HIS A 243 NE2 86.6 93.4
REMARK 620 4 PNN A1311 S1 93.9 114.0 152.7
REMARK 620 5 AKG A1312 O1 94.0 104.6 162.0 9.4
REMARK 620 6 AKG A1312 O5 97.5 170.2 91.5 61.3 70.6
REMARK 620 7 HOH A2090 O 176.8 90.3 96.0 83.0 83.0 80.7
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PNN A 1311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 1310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AKG A 1312
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DCS RELATED DB: PDB
REMARK 900 DEACETOXYCEPHALOSPORIN C SYNTHASE FROM S. CLAVULIGERUS
REMARK 900 RELATED ID: 1E5H RELATED DB: PDB
REMARK 900 DELTA-R307A DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH
REMARK 900 SUCCINATE AND CARBON DIOXIDE
REMARK 900 RELATED ID: 1E5I RELATED DB: PDB
REMARK 900 DELTA-R306 DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH IRON
REMARK 900 AND 2-OXOGLUTARATE.
REMARK 900 RELATED ID: 1HJF RELATED DB: PDB
REMARK 900 ALTERATION OF THE CO-SUBSTRATE SELECTIVITY OF
REMARK 900 DEACETOXYCEPHALOSPORIN C SYNTHASE: THE ROLE OF ARGININE-258
REMARK 900 RELATED ID: 1HJG RELATED DB: PDB
REMARK 900 ALTERATION OF THE CO-SUBSTRATE SELECTIVITY OF
REMARK 900 DEACETOXYCEPHALOSPORIN C SYNTHASE: THE ROLE OF ARGININE-258
REMARK 900 RELATED ID: 1RXF RELATED DB: PDB
REMARK 900 DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH FE(II)
REMARK 900 RELATED ID: 1RXG RELATED DB: PDB
REMARK 900 DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH FE(II) AND 2-
REMARK 900 OXOGLUTARATE
REMARK 900 RELATED ID: 1UO9 RELATED DB: PDB
REMARK 900 DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH SUCCINATE
REMARK 900 RELATED ID: 1UNB RELATED DB: PDB
REMARK 900 DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH 2-OXOGLUTARATE AND
REMARK 900 AMPICILLIN
REMARK 900 RELATED ID: 1UOF RELATED DB: PDB
REMARK 900 DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH PENICILLIN G
REMARK 900 RELATED ID: 1UOG RELATED DB: PDB
REMARK 900 DEACETOXYCEPHALOSPORIN C SYNTHASE COMPLEXED WITH
REMARK 900 DEACETOXYCEPHALOSPORIN C
DBREF 1UOB A 1 311 UNP P18548 CEFE_STRCL 1 311
SEQRES 1 A 311 MET ASP THR THR VAL PRO THR PHE SER LEU ALA GLU LEU
SEQRES 2 A 311 GLN GLN GLY LEU HIS GLN ASP GLU PHE ARG ARG CYS LEU
SEQRES 3 A 311 ARG ASP LYS GLY LEU PHE TYR LEU THR ASP CYS GLY LEU
SEQRES 4 A 311 THR ASP THR GLU LEU LYS SER ALA LYS ASP LEU VAL ILE
SEQRES 5 A 311 ASP PHE PHE GLU HIS GLY SER GLU ALA GLU LYS ARG ALA
SEQRES 6 A 311 VAL THR SER PRO VAL PRO THR MET ARG ARG GLY PHE THR
SEQRES 7 A 311 GLY LEU GLU SER GLU SER THR ALA GLN ILE THR ASN THR
SEQRES 8 A 311 GLY SER TYR SER ASP TYR SER MET CYS TYR SER MET GLY
SEQRES 9 A 311 THR ALA ASP ASN LEU PHE PRO SER GLY ASP PHE GLU ARG
SEQRES 10 A 311 ILE TRP THR GLN TYR PHE ASP ARG GLN TYR THR ALA SER
SEQRES 11 A 311 ARG ALA VAL ALA ARG GLU VAL LEU ARG ALA THR GLY THR
SEQRES 12 A 311 GLU PRO ASP GLY GLY VAL GLU ALA PHE LEU ASP CYS GLU
SEQRES 13 A 311 PRO LEU LEU ARG PHE ARG TYR PHE PRO GLN VAL PRO GLU
SEQRES 14 A 311 HIS ARG SER ALA GLU GLU GLN PRO LEU ARG MET ALA PRO
SEQRES 15 A 311 HIS TYR ASP LEU SER MET VAL THR LEU ILE GLN GLN THR
SEQRES 16 A 311 PRO CYS ALA ASN GLY PHE VAL SER LEU GLN ALA GLU VAL
SEQRES 17 A 311 GLY GLY ALA PHE THR ASP LEU PRO TYR ARG PRO ASP ALA
SEQRES 18 A 311 VAL LEU VAL PHE CYS GLY ALA ILE ALA THR LEU VAL THR
SEQRES 19 A 311 GLY GLY GLN VAL LYS ALA PRO ARG HIS HIS VAL ALA ALA
SEQRES 20 A 311 PRO ARG ARG ASP GLN ILE ALA GLY SER SER ARG THR SER
SEQRES 21 A 311 SER VAL PHE PHE LEU ARG PRO ASN ALA ASP PHE THR PHE
SEQRES 22 A 311 SER VAL PRO LEU ALA ARG GLU CYS GLY PHE ASP VAL SER
SEQRES 23 A 311 LEU ASP GLY GLU THR ALA THR PHE GLN ASP TRP ILE GLY
SEQRES 24 A 311 GLY ASN TYR VAL ASN ILE ARG ARG THR SER LYS ALA
HET FE2 A1310 1
HET PNN A1311 23
HET AKG A1312 10
HETNAM FE2 FE (II) ION
HETNAM PNN PENICILLIN G
HETNAM AKG 2-OXOGLUTARIC ACID
FORMUL 2 FE2 FE 2+
FORMUL 3 PNN C16 H18 N2 O4 S
FORMUL 4 AKG C5 H6 O5
FORMUL 5 HOH *156(H2 O)
HELIX 1 1 LEU A 10 GLN A 15 1 6
HELIX 2 2 HIS A 18 LYS A 29 1 12
HELIX 3 3 THR A 40 GLY A 58 1 19
HELIX 4 4 SER A 59 ALA A 65 1 7
HELIX 5 5 SER A 112 THR A 141 1 30
HELIX 6 6 GLY A 148 ASP A 154 1 7
HELIX 7 7 GLY A 227 THR A 234 1 8
HELIX 8 8 VAL A 275 CYS A 281 1 7
HELIX 9 9 PHE A 294 GLY A 299 1 6
SHEET 1 AA 8 THR A 7 SER A 9 0
SHEET 2 AA 8 LEU A 31 THR A 35 1 O TYR A 33 N PHE A 8
SHEET 3 AA 8 VAL A 222 CYS A 226 -1 O VAL A 222 N LEU A 34
SHEET 4 AA 8 VAL A 189 THR A 195 -1 O THR A 190 N PHE A 225
SHEET 5 AA 8 ARG A 258 LEU A 265 -1 O THR A 259 N THR A 195
SHEET 6 AA 8 LEU A 158 PHE A 164 -1 O LEU A 158 N PHE A 264
SHEET 7 AA 8 MET A 99 MET A 103 -1 O MET A 99 N TYR A 163
SHEET 8 AA 8 GLY A 76 THR A 78 -1 O GLY A 76 N SER A 102
SHEET 1 AB 5 ALA A 211 ASP A 214 0
SHEET 2 AB 5 LEU A 204 VAL A 208 -1 O ALA A 206 N THR A 213
SHEET 3 AB 5 HIS A 243 VAL A 245 -1 O HIS A 244 N GLN A 205
SHEET 4 AB 5 MET A 180 ASP A 185 -1 O MET A 180 N VAL A 245
SHEET 5 AB 5 ILE A 305 ARG A 306 -1 O ARG A 306 N TYR A 184
SHEET 1 AC 2 THR A 272 SER A 274 0
SHEET 2 AC 2 THR A 291 THR A 293 -1 O ALA A 292 N PHE A 273
LINK NE2 HIS A 183 FE FE2 A1310 1555 1555 2.25
LINK OD1 ASP A 185 FE FE2 A1310 1555 1555 2.18
LINK NE2 HIS A 243 FE FE2 A1310 1555 1555 2.09
LINK FE FE2 A1310 S1 PNN A1311 1555 1555 2.09
LINK FE FE2 A1310 O1 AKG A1312 1555 1555 2.26
LINK FE FE2 A1310 O5 AKG A1312 1555 1555 2.23
LINK FE FE2 A1310 O HOH A2090 1555 1555 2.18
SITE 1 AC1 14 MET A 73 SER A 102 LEU A 158 MET A 180
SITE 2 AC1 14 HIS A 183 ASP A 185 ILE A 192 HIS A 243
SITE 3 AC1 14 SER A 260 VAL A 262 PHE A 264 FE2 A1310
SITE 4 AC1 14 HOH A2090 HOH A2156
SITE 1 AC2 6 HIS A 183 ASP A 185 HIS A 243 PNN A1311
SITE 2 AC2 6 AKG A1312 HOH A2090
SITE 1 AC3 11 ARG A 162 MET A 180 HIS A 183 ASP A 185
SITE 2 AC3 11 LEU A 204 HIS A 243 ARG A 258 SER A 260
SITE 3 AC3 11 PHE A 264 FE2 A1310 HOH A2090
CRYST1 106.600 106.600 71.600 90.00 90.00 120.00 H 3 9
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 0.009381 0.005416 0.000000 0.00000
SCALE2 0.000000 0.010832 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013966 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
