HEADER OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR) 12-JUL-94 1ISC
TITLE STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE:
TITLE 2 COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IRON(III) SUPEROXIDE DISMUTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.15.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM_STRAIN: K12
KEYWDS OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR)
EXPDTA X-RAY DIFFRACTION
AUTHOR M.S.LAH,M.DIXON,K.A.PATTRIDGE,W.C.STALLINGS,J.A.FEE,
AUTHOR 2 M.L.LUDWIG
REVDAT 2 24-FEB-09 1ISC 1 VERSN
REVDAT 1 30-SEP-94 1ISC 0
JRNL AUTH M.S.LAH,M.M.DIXON,K.A.PATTRIDGE,W.C.STALLINGS,
JRNL AUTH 2 J.A.FEE,M.L.LUDWIG
JRNL TITL STRUCTURE-FUNCTION IN ESCHERICHIA COLI IRON
JRNL TITL 2 SUPEROXIDE DISMUTASE: COMPARISONS WITH THE
JRNL TITL 3 MANGANESE ENZYME FROM THERMUS THERMOPHILUS.
JRNL REF BIOCHEMISTRY V. 34 1646 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7849024
JRNL DOI 10.1021/BI00005A021
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.C.STALLINGS,C.BULL,J.A.FEE,M.S.LAH,M.L.LUDWIG
REMARK 1 TITL IRON AND MANGANESE SUPEROXIDE DISMUTASES:
REMARK 1 TITL 2 CATALYTIC INFERENCES FROM THE STRUCTURES
REMARK 1 EDIT J.G.SCANDALIOS
REMARK 1 REF MOLECULAR BIOLOGY OF FREE 193 1992
REMARK 1 REF 2 RADICAL SCAVENGING SYSTEMS
REMARK 1 PUBL COLD SPRING HARBOR LAB.PRESS, PLAINVIEW,N.Y.
REMARK 1 REFN
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.CARLIOZ,M.L.LUDWIG,W.C.STALLINGS,J.A.FEE,
REMARK 1 AUTH 2 H.M.STEINMAN,D.TOUATI
REMARK 1 TITL IRON SUPEROXIDE DISMUTASE: NUCLEOTIDE SEQUENCE OF
REMARK 1 TITL 2 THE GENE FROM ESCHERICHIA COLI K12 AND CORRELATION
REMARK 1 TITL 3 WITH CRYSTAL STRUCTURES
REMARK 1 REF J.BIOL.CHEM. V. 263 1555 1988
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 36948
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3106
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 272
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 2.79
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ISC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 40.80500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.79000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.58000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.79000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.80500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.58000
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:
REMARK 300 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO
REMARK 300 CHAIN *A*.
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: 1820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 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 HIS A 17 NE2 HIS A 17 CD2 -0.069
REMARK 500 HIS A 30 NE2 HIS A 30 CD2 -0.079
REMARK 500 HIS A 160 NE2 HIS A 160 CD2 -0.067
REMARK 500 HIS A 176 NE2 HIS A 176 CD2 -0.072
REMARK 500 HIS B 17 NE2 HIS B 17 CD2 -0.073
REMARK 500 HIS B 30 NE2 HIS B 30 CD2 -0.077
REMARK 500 HIS B 31 NE2 HIS B 31 CD2 -0.068
REMARK 500 HIS B 160 NE2 HIS B 160 CD2 -0.069
REMARK 500 HIS B 176 NE2 HIS B 176 CD2 -0.068
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 TRP A 71 CD1 - CG - CD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 TRP A 71 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP A 77 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 TRP A 77 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP A 122 CD1 - CG - CD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP A 122 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES
REMARK 500 TRP A 124 CD1 - CG - CD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TRP A 124 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES
REMARK 500 TRP A 158 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 TRP A 158 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 TRP A 178 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP A 178 CE2 - CD2 - CG ANGL. DEV. = -6.1 DEGREES
REMARK 500 TRP A 183 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TRP A 183 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP B 71 CD1 - CG - CD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 TRP B 71 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP B 77 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP B 77 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP B 122 CD1 - CG - CD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP B 122 CE2 - CD2 - CG ANGL. DEV. = -5.1 DEGREES
REMARK 500 TRP B 124 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP B 124 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP B 158 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 TRP B 158 CE2 - CD2 - CG ANGL. DEV. = -5.2 DEGREES
REMARK 500 TRP B 178 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP B 178 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES
REMARK 500 TRP B 178 CG - CD2 - CE3 ANGL. DEV. = 5.5 DEGREES
REMARK 500 TRP B 183 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TRP B 183 CE2 - CD2 - CG ANGL. DEV. = -6.1 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 ALA A 84 -142.55 -139.53
REMARK 500 ASN A 140 -104.72 53.58
REMARK 500 ARG A 167 -122.95 48.83
REMARK 500 ALA B 84 -139.30 -134.07
REMARK 500 ASN B 140 -107.93 55.01
REMARK 500 ARG B 167 -125.08 51.23
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 A 285 DISTANCE = 5.14 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE IRON ATOM AND NEARBY RESIDUES ARE PRESENTED IN TWO
REMARK 600 CONFORMATIONS, DENOTED BY A OR B IN THE ALTERNATE
REMARK 600 CONFORMATION FIELD. THE AZIDE IS PRESENT ONLY FOR
REMARK 600 CONFORMATION A.
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 FE A 193 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 160 NE2
REMARK 620 2 ASP A 156 OD2 102.7
REMARK 620 3 HOH A 196 O 91.8 87.5
REMARK 620 4 HIS A 73 NE2 158.9 96.9 81.1
REMARK 620 5 HIS A 26 NE2 90.8 82.8 170.3 99.5
REMARK 620 6 HIS A 160 NE2 6.7 109.3 93.2 152.9 90.5
REMARK 620 7 ASP A 156 OD2 109.9 7.2 87.4 89.8 83.0 116.5
REMARK 620 8 HIS A 73 NE2 144.6 112.7 89.6 17.5 93.7 138.0 105.5
REMARK 620 9 HOH A 196 O 91.4 88.5 1.0 81.2 171.3 92.6 88.4 89.4
REMARK 620 10 HIS A 26 NE2 89.1 82.9 170.3 101.3 1.8 88.8 83.3
REMARK 620 95.3 171.3
REMARK 620 11 AZI A 195 N1 74.1 176.0 90.3 86.0 99.4 67.5 175.5
REMARK 620 70.6 89.3 99.2
REMARK 620 12 AZI A 195 N1 74.1 176.0 90.3 86.0 99.4 67.5 175.5
REMARK 620 70.6 89.3 99.2 0.0
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620 9 10 11
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 193 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 26 NE2
REMARK 620 2 ASP B 156 OD2 83.7
REMARK 620 3 HIS B 160 NE2 88.2 104.3
REMARK 620 4 HOH B 196 O 176.7 93.4 90.9
REMARK 620 5 HIS B 73 NE2 89.8 105.7 149.5 92.6
REMARK 620 6 HIS B 26 NE2 2.4 81.4 88.8 174.6 90.4
REMARK 620 7 ASP B 156 OD2 80.0 5.0 100.7 97.1 108.9 77.6
REMARK 620 8 HIS B 160 NE2 85.5 114.9 11.4 94.2 138.3 86.5 111.0
REMARK 620 9 HOH B 196 O 166.0 82.5 92.7 11.0 96.4 163.7 86.1 98.0
REMARK 620 10 HIS B 73 NE2 92.7 93.0 162.7 89.0 13.5 92.9 96.5
REMARK 620 151.6 90.5
REMARK 620 11 AZI B 195 N1 93.5 176.7 77.2 89.4 72.5 95.8 173.2
REMARK 620 66.5 100.4 85.4
REMARK 620 12 AZI B 195 N1 93.5 176.7 77.2 89.4 72.5 95.8 173.2
REMARK 620 66.5 100.4 85.4 0.0
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620 9 10 11
REMARK 650
REMARK 650 HELIX
REMARK 650 ASSIGNMENTS OF SECONDARY STRUCTURE ARE BASED ON THE
REMARK 650 ALGORITHM OF KABSCH AND SANDER. EXCEPTIONS: THE FIRST
REMARK 650 HELIX HAS A KINK NEAR RESIDUE 28; SUCCESSIVE 3/10 TURNS
REMARK 650 ARE GIVEN PRIORITY OVER SHORT HELICES.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: FEA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: FEB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 193
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI A 195
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 193
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI B 195
DBREF 1ISC A 1 192 UNP P09157 SODF_ECOLI 1 192
DBREF 1ISC B 1 192 UNP P09157 SODF_ECOLI 1 192
SEQRES 1 A 192 SER PHE GLU LEU PRO ALA LEU PRO TYR ALA LYS ASP ALA
SEQRES 2 A 192 LEU ALA PRO HIS ILE SER ALA GLU THR ILE GLU TYR HIS
SEQRES 3 A 192 TYR GLY LYS HIS HIS GLN THR TYR VAL THR ASN LEU ASN
SEQRES 4 A 192 ASN LEU ILE LYS GLY THR ALA PHE GLU GLY LYS SER LEU
SEQRES 5 A 192 GLU GLU ILE ILE ARG SER SER GLU GLY GLY VAL PHE ASN
SEQRES 6 A 192 ASN ALA ALA GLN VAL TRP ASN HIS THR PHE TYR TRP ASN
SEQRES 7 A 192 CYS LEU ALA PRO ASN ALA GLY GLY GLU PRO THR GLY LYS
SEQRES 8 A 192 VAL ALA GLU ALA ILE ALA ALA SER PHE GLY SER PHE ALA
SEQRES 9 A 192 ASP PHE LYS ALA GLN PHE THR ASP ALA ALA ILE LYS ASN
SEQRES 10 A 192 PHE GLY SER GLY TRP THR TRP LEU VAL LYS ASN SER ASP
SEQRES 11 A 192 GLY LYS LEU ALA ILE VAL SER THR SER ASN ALA GLY THR
SEQRES 12 A 192 PRO LEU THR THR ASP ALA THR PRO LEU LEU THR VAL ASP
SEQRES 13 A 192 VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN ALA
SEQRES 14 A 192 ARG PRO GLY TYR LEU GLU HIS PHE TRP ALA LEU VAL ASN
SEQRES 15 A 192 TRP GLU PHE VAL ALA LYS ASN LEU ALA ALA
SEQRES 1 B 192 SER PHE GLU LEU PRO ALA LEU PRO TYR ALA LYS ASP ALA
SEQRES 2 B 192 LEU ALA PRO HIS ILE SER ALA GLU THR ILE GLU TYR HIS
SEQRES 3 B 192 TYR GLY LYS HIS HIS GLN THR TYR VAL THR ASN LEU ASN
SEQRES 4 B 192 ASN LEU ILE LYS GLY THR ALA PHE GLU GLY LYS SER LEU
SEQRES 5 B 192 GLU GLU ILE ILE ARG SER SER GLU GLY GLY VAL PHE ASN
SEQRES 6 B 192 ASN ALA ALA GLN VAL TRP ASN HIS THR PHE TYR TRP ASN
SEQRES 7 B 192 CYS LEU ALA PRO ASN ALA GLY GLY GLU PRO THR GLY LYS
SEQRES 8 B 192 VAL ALA GLU ALA ILE ALA ALA SER PHE GLY SER PHE ALA
SEQRES 9 B 192 ASP PHE LYS ALA GLN PHE THR ASP ALA ALA ILE LYS ASN
SEQRES 10 B 192 PHE GLY SER GLY TRP THR TRP LEU VAL LYS ASN SER ASP
SEQRES 11 B 192 GLY LYS LEU ALA ILE VAL SER THR SER ASN ALA GLY THR
SEQRES 12 B 192 PRO LEU THR THR ASP ALA THR PRO LEU LEU THR VAL ASP
SEQRES 13 B 192 VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN ALA
SEQRES 14 B 192 ARG PRO GLY TYR LEU GLU HIS PHE TRP ALA LEU VAL ASN
SEQRES 15 B 192 TRP GLU PHE VAL ALA LYS ASN LEU ALA ALA
HET FE A 193 2
HET AZI A 195 3
HET FE B 193 2
HET AZI B 195 3
HETNAM FE FE (III) ION
HETNAM AZI AZIDE ION
FORMUL 3 FE 2(FE 3+)
FORMUL 4 AZI 2(N3 1-)
FORMUL 7 HOH *270(H2 O)
HELIX 1 HA1 ALA A 20 ILE A 42 1 23
HELIX 2 HA2 LEU A 52 SER A 58 1 7
HELIX 3 HA3 GLY A 61 ASN A 78 1 18
HELIX 4 HA4 GLY A 90 PHE A 100 1 11
HELIX 5 HA5 PHE A 103 LYS A 116 1 14
HELIX 6 HA6 PRO A 144 THR A 146 5 3
HELIX 7 HA7 ARG A 170 TRP A 178 1 9
HELIX 8 HA8 TRP A 183 ALA A 191 1 9
HELIX 9 HB1 ALA B 20 ILE B 42 1 23
HELIX 10 HB2 LEU B 52 SER B 58 1 7
HELIX 11 HB3 GLY B 61 ASN B 78 1 18
HELIX 12 HB4 GLY B 90 PHE B 100 1 11
HELIX 13 HB5 PHE B 103 LYS B 116 1 14
HELIX 14 HB6 PRO B 144 THR B 146 5 3
HELIX 15 HB7 ARG B 170 TRP B 178 1 9
HELIX 16 HB8 TRP B 183 ALA B 191 1 9
SHEET 1 B1A 3 LEU A 133 SER A 139 0
SHEET 2 B1A 3 GLY A 121 LYS A 127 -1 O TRP A 122 N THR A 138
SHEET 3 B1A 3 THR A 150 ASP A 156 -1 N THR A 150 O LYS A 127
SHEET 1 B1B 3 LEU B 133 SER B 139 0
SHEET 2 B1B 3 GLY B 121 LYS B 127 -1 O TRP B 122 N THR B 138
SHEET 3 B1B 3 THR B 150 ASP B 156 -1 N THR B 150 O LYS B 127
LINK FE A FE A 193 NE2AHIS A 160 1555 1555 2.15
LINK FE A FE A 193 OD2AASP A 156 1555 1555 2.04
LINK FE A FE A 193 O AHOH A 196 1555 1555 2.02
LINK FE A FE A 193 NE2AHIS A 73 1555 1555 2.13
LINK FE A FE A 193 NE2AHIS A 26 1555 1555 2.20
LINK FE B FE A 193 NE2BHIS A 160 1555 1555 2.06
LINK FE B FE A 193 OD2BASP A 156 1555 1555 1.92
LINK FE B FE A 193 NE2BHIS A 73 1555 1555 2.02
LINK FE B FE A 193 O BHOH A 196 1555 1555 1.95
LINK FE B FE A 193 NE2BHIS A 26 1555 1555 2.13
LINK FE A FE B 193 NE2AHIS B 26 1555 1555 2.23
LINK FE A FE B 193 OD2AASP B 156 1555 1555 2.01
LINK FE A FE B 193 NE2AHIS B 160 1555 1555 2.15
LINK FE A FE B 193 O AHOH B 196 1555 1555 1.98
LINK FE B FE B 193 NE2BHIS B 73 1555 1555 1.97
LINK FE B FE B 193 NE2BHIS B 26 1555 1555 2.15
LINK FE B FE B 193 OD2BASP B 156 1555 1555 1.98
LINK FE B FE B 193 NE2BHIS B 160 1555 1555 2.04
LINK FE B FE B 193 O BHOH B 196 1555 1555 2.02
LINK FE A FE B 193 NE2AHIS B 73 1555 1555 2.13
LINK FE A FE A 193 N1 AZI A 195 1555 1555 2.09
LINK FE B FE A 193 N1 AZI A 195 1555 1555 2.23
LINK FE A FE B 193 N1 AZI B 195 1555 1555 2.16
LINK FE B FE B 193 N1 AZI B 195 1555 1555 2.35
CISPEP 1 ALA A 15 PRO A 16 0 7.29
CISPEP 2 ALA B 15 PRO B 16 0 5.57
SITE 1 FEA 6 HIS A 26 HIS A 73 ASP A 156 HIS A 160
SITE 2 FEA 6 HOH A 196 AZI A 195
SITE 1 FEB 6 HIS B 26 HIS B 73 ASP B 156 HIS B 160
SITE 2 FEB 6 HOH B 196 AZI B 195
SITE 1 AC1 6 HIS A 26 HIS A 73 ASP A 156 HIS A 160
SITE 2 AC1 6 AZI A 195 HOH A 196
SITE 1 AC2 8 HIS A 26 HIS A 30 HIS A 31 TYR A 34
SITE 2 AC2 8 HIS A 73 HIS A 160 FE A 193 HOH A 196
SITE 1 AC3 6 HIS B 26 HIS B 73 ASP B 156 HIS B 160
SITE 2 AC3 6 AZI B 195 HOH B 196
SITE 1 AC4 9 HIS B 26 HIS B 30 HIS B 31 TYR B 34
SITE 2 AC4 9 HIS B 73 HIS B 160 FE B 193 HOH B 196
SITE 3 AC4 9 HOH B 307
CRYST1 81.610 75.160 71.580 90.00 90.00 90.00 P 21 21 21 8
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 0.012253 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013305 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013970 0.00000
MTRIX1 1 -0.147500 -0.953500 0.262700 56.41359 1
MTRIX2 1 -0.954300 0.067400 -0.291200 67.26064 1
MTRIX3 1 0.260000 -0.293700 -0.919900 61.46539 1
(ATOM LINES ARE NOT SHOWN.)
END
