HEADER OXIDOREDUCTASE 11-NOV-02 1O7M
TITLE NAPHTHALENE 1,2-DIOXYGENASE, BINARY COMPLEX WITH DIOXYGEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NAPHTHALENE 1,2-DIOXYGENASE ALPHA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NAPHTHALENE 1,2-DIOXYGENASE ISP ALPHA, NDOB, NAHAC;
COMPND 5 EC: 1.14.12.12;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NAPHTHALENE 1,2-DIOXYGENASE BETA SUBUNIT;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: NAPHTHALENE 1,2-DIOXYGENASE ISP BETA, NDOC, NAHAD;
COMPND 11 EC: 1.14.12.12;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 3 ORGANISM_TAXID: 303;
SOURCE 4 STRAIN: NCIB 9816-4;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDTG141;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 11 ORGANISM_TAXID: 303;
SOURCE 12 STRAIN: NCIB 9816-4;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: JM109(DE3);
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PDTG141
KEYWDS OXIDOREDUCTASE, NON-HEME IRON DIOXYGENASE, ENZYME-SUBSTRATE COMPLEX,
KEYWDS 2 IRON-SULFUR, AROMATIC HYDROCARBON CATABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KARLSSON,J.V.PARALES,R.E.PARALES,D.T.GIBSON,H.EKLUND,S.RAMASWAMY
REVDAT 4 13-DEC-23 1O7M 1 LINK
REVDAT 3 05-JUL-17 1O7M 1 REMARK
REVDAT 2 24-FEB-09 1O7M 1 VERSN
REVDAT 1 20-FEB-03 1O7M 0
JRNL AUTH A.KARLSSON,J.V.PARALES,R.E.PARALES,D.T.GIBSON,H.EKLUND,
JRNL AUTH 2 S.RAMASWAMY
JRNL TITL CRYSTAL STRUCTURE OF NAPHTHALENE DIOXYGENASE: SIDE-ON
JRNL TITL 2 BINDING OF DIOXYGEN TO IRON
JRNL REF SCIENCE V. 299 1039 2003
JRNL REFN ISSN 0036-8075
JRNL PMID 12586937
JRNL DOI 10.1126/SCIENCE.1078020
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0.36
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 77729
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 771
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5479
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 46
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5089
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 553
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.15000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : -0.23000
REMARK 3 B12 (A**2) : 0.07000
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): 0.101
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.089
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.086
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.611
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5252 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4557 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7091 ; 1.625 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10600 ; 1.228 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 638 ; 5.045 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 891 ;16.127 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 740 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5914 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1115 ; 0.004 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1084 ; 0.239 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4461 ; 0.217 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1 ; 0.330 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1007 ; 0.188 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 3 ; 0.120 ; 0.500
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): 38 ; 0.188 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 130 ; 0.220 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 78 ; 0.304 ; 0.500
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): 3168 ; 0.814 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5069 ; 1.514 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2084 ; 2.263 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2020 ; 3.620 ; 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 : BABINET MODEL PLUS MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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. ASN 363 AND MET 366 HAVE BEEN MODELLED WITH DOUBLE
REMARK 3 CONFORMATIONS.
REMARK 4
REMARK 4 1O7M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1290011656.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-01
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
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 RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : CONFOCAL MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU MSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80092
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 3.670
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.32100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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 1EG9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE 2M, MES 0.1M,
REMARK 280 DIOXANE 2-3%, PH 6.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+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 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 70.13850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.49448
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 69.58467
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 70.13850
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 40.49448
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 69.58467
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 70.13850
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 40.49448
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 69.58467
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 70.13850
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 40.49448
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 69.58467
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 70.13850
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 40.49448
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 69.58467
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 70.13850
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 40.49448
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 69.58467
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 80.98896
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 139.16933
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 80.98896
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 139.16933
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 80.98896
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 139.16933
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 80.98896
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 139.16933
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 80.98896
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 139.16933
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 80.98896
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 139.16933
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 ACTIVE ENZYME IS A ALPHA3 BETA3
REMARK 300 HEXAMER GENERATEDBY THE THREEFOLD
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PQS
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 -0.500000 -0.866025 0.000000 70.13850
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 121.48345
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -70.13850
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 121.48345
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 A2253 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 ARG A 449
REMARK 465 MET B 501
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 ASP A 448 CA C O CB CG OD1 OD2
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 37 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 PRO A 235 C - N - CD ANGL. DEV. = -15.7 DEGREES
REMARK 500 ASP A 286 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 293 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP A 320 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 361 CB - CG - OD2 ANGL. DEV. = 5.6 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 ILE A 34 -63.08 -109.78
REMARK 500 LEU A 42 -60.14 -109.03
REMARK 500 THR A 43 -169.81 -166.26
REMARK 500 HIS A 83 -86.51 -82.43
REMARK 500 LYS A 192 59.30 -93.68
REMARK 500 GLU A 221 38.51 73.63
REMARK 500 PRO A 235 -169.41 -61.97
REMARK 500 GLU A 236 -113.44 -30.16
REMARK 500 ASP A 264 1.52 -66.66
REMARK 500 CYS A 309 -57.48 77.61
REMARK 500 SER A 385 50.09 -140.97
REMARK 500 LYS A 445 153.35 -44.01
REMARK 500 THR A 446 -13.52 68.09
REMARK 500 ILE B 503 121.50 -36.31
REMARK 500 CYS B 525 91.36 44.02
REMARK 500 ASN B 582 119.16 -30.82
REMARK 500 ASN B 589 74.39 -157.09
REMARK 500 LYS B 632 -4.26 -55.17
REMARK 500 HIS B 688 -36.16 74.10
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 FES A1453 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 81 SG
REMARK 620 2 FES A1453 S1 109.3
REMARK 620 3 FES A1453 S2 111.5 106.7
REMARK 620 4 CYS A 101 SG 108.6 106.2 114.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A1453 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 83 ND1
REMARK 620 2 FES A1453 S1 115.7
REMARK 620 3 FES A1453 S2 118.6 105.3
REMARK 620 4 HIS A 104 ND1 87.4 113.2 116.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A1454 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 208 NE2
REMARK 620 2 HIS A 213 NE2 102.6
REMARK 620 3 ASP A 362 OD2 94.3 99.5
REMARK 620 4 ASP A 362 OD1 148.2 91.3 54.9
REMARK 620 5 OXY A1451 O2 103.2 116.2 134.9 95.8
REMARK 620 6 OXY A1451 O1 103.2 80.2 162.2 107.3 37.3
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 A1452
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A1454
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1697
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1698
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1448
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1449
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1450
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY A1451
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A1453
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1695
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1696
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1699
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EG9 RELATED DB: PDB
REMARK 900 NAPHTHALENE 1,2-DIOXYGENASE WITH INDOLE BOUND IN THE ACTIVE SITE.
REMARK 900 RELATED ID: 1NDO RELATED DB: PDB
REMARK 900 NAPTHALENE 1,2-DIOXYGENASE
REMARK 900 RELATED ID: 1O7G RELATED DB: PDB
REMARK 900 NAPHTHALENE 1,2-DIOXYGENASE WITH NAPHTHALENE BOUND IN THE ACTIVE
REMARK 900 SITE.
REMARK 900 RELATED ID: 1O7H RELATED DB: PDB
REMARK 900 NAPHTHALENE 1,2-DIOXYGENASE WITH OXIDIZED RIESKE IRON SULPHUR
REMARK 900 CENTER SITE.
REMARK 900 RELATED ID: 1O7N RELATED DB: PDB
REMARK 900 NAPHTHALENE 1,2-DIOXYGENASE, TERNARY COMPLEX WITH DIOXYGEN AND
REMARK 900 INDOLE
REMARK 900 RELATED ID: 1O7P RELATED DB: PDB
REMARK 900 NAPHTHALENE 1,2-DIOXYGENASE, PRODUCT COMPLEX
REMARK 900 RELATED ID: 1O7W RELATED DB: PDB
REMARK 900 NAPHTHALENE 1,2-DIOXYGENASE, FULLY REDUCED FORM
DBREF 1O7M A 1 449 UNP P23094 NDOB_PSEPU 1 449
DBREF 1O7M B 501 694 UNP P23095 NDOC_PSEPU 1 194
SEQRES 1 A 449 MET ASN TYR ASN ASN LYS ILE LEU VAL SER GLU SER GLY
SEQRES 2 A 449 LEU SER GLN LYS HIS LEU ILE HIS GLY ASP GLU GLU LEU
SEQRES 3 A 449 PHE GLN HIS GLU LEU LYS THR ILE PHE ALA ARG ASN TRP
SEQRES 4 A 449 LEU PHE LEU THR HIS ASP SER LEU ILE PRO ALA PRO GLY
SEQRES 5 A 449 ASP TYR VAL THR ALA LYS MET GLY ILE ASP GLU VAL ILE
SEQRES 6 A 449 VAL SER ARG GLN ASN ASP GLY SER ILE ARG ALA PHE LEU
SEQRES 7 A 449 ASN VAL CYS ARG HIS ARG GLY LYS THR LEU VAL SER VAL
SEQRES 8 A 449 GLU ALA GLY ASN ALA LYS GLY PHE VAL CYS SER TYR HIS
SEQRES 9 A 449 GLY TRP GLY PHE GLY SER ASN GLY GLU LEU GLN SER VAL
SEQRES 10 A 449 PRO PHE GLU LYS ASP LEU TYR GLY GLU SER LEU ASN LYS
SEQRES 11 A 449 LYS CYS LEU GLY LEU LYS GLU VAL ALA ARG VAL GLU SER
SEQRES 12 A 449 PHE HIS GLY PHE ILE TYR GLY CYS PHE ASP GLN GLU ALA
SEQRES 13 A 449 PRO PRO LEU MET ASP TYR LEU GLY ASP ALA ALA TRP TYR
SEQRES 14 A 449 LEU GLU PRO MET PHE LYS HIS SER GLY GLY LEU GLU LEU
SEQRES 15 A 449 VAL GLY PRO PRO GLY LYS VAL VAL ILE LYS ALA ASN TRP
SEQRES 16 A 449 LYS ALA PRO ALA GLU ASN PHE VAL GLY ASP ALA TYR HIS
SEQRES 17 A 449 VAL GLY TRP THR HIS ALA SER SER LEU ARG SER GLY GLU
SEQRES 18 A 449 SER ILE PHE SER SER LEU ALA GLY ASN ALA ALA LEU PRO
SEQRES 19 A 449 PRO GLU GLY ALA GLY LEU GLN MET THR SER LYS TYR GLY
SEQRES 20 A 449 SER GLY MET GLY VAL LEU TRP ASP GLY TYR SER GLY VAL
SEQRES 21 A 449 HIS SER ALA ASP LEU VAL PRO GLU LEU MET ALA PHE GLY
SEQRES 22 A 449 GLY ALA LYS GLN GLU ARG LEU ASN LYS GLU ILE GLY ASP
SEQRES 23 A 449 VAL ARG ALA ARG ILE TYR ARG SER HIS LEU ASN CYS THR
SEQRES 24 A 449 VAL PHE PRO ASN ASN SER MET LEU THR CYS SER GLY VAL
SEQRES 25 A 449 PHE LYS VAL TRP ASN PRO ILE ASP ALA ASN THR THR GLU
SEQRES 26 A 449 VAL TRP THR TYR ALA ILE VAL GLU LYS ASP MET PRO GLU
SEQRES 27 A 449 ASP LEU LYS ARG ARG LEU ALA ASP SER VAL GLN ARG THR
SEQRES 28 A 449 PHE GLY PRO ALA GLY PHE TRP GLU SER ASP ASP ASN ASP
SEQRES 29 A 449 ASN MET GLU THR ALA SER GLN ASN GLY LYS LYS TYR GLN
SEQRES 30 A 449 SER ARG ASP SER ASP LEU LEU SER ASN LEU GLY PHE GLY
SEQRES 31 A 449 GLU ASP VAL TYR GLY ASP ALA VAL TYR PRO GLY VAL VAL
SEQRES 32 A 449 GLY LYS SER ALA ILE GLY GLU THR SER TYR ARG GLY PHE
SEQRES 33 A 449 TYR ARG ALA TYR GLN ALA HIS VAL SER SER SER ASN TRP
SEQRES 34 A 449 ALA GLU PHE GLU HIS ALA SER SER THR TRP HIS THR GLU
SEQRES 35 A 449 LEU THR LYS THR THR ASP ARG
SEQRES 1 B 194 MET MET ILE ASN ILE GLN GLU ASP LYS LEU VAL SER ALA
SEQRES 2 B 194 HIS ASP ALA GLU GLU ILE LEU ARG PHE PHE ASN CYS HIS
SEQRES 3 B 194 ASP SER ALA LEU GLN GLN GLU ALA THR THR LEU LEU THR
SEQRES 4 B 194 GLN GLU ALA HIS LEU LEU ASP ILE GLN ALA TYR ARG ALA
SEQRES 5 B 194 TRP LEU GLU HIS CYS VAL GLY SER GLU VAL GLN TYR GLN
SEQRES 6 B 194 VAL ILE SER ARG GLU LEU ARG ALA ALA SER GLU ARG ARG
SEQRES 7 B 194 TYR LYS LEU ASN GLU ALA MET ASN VAL TYR ASN GLU ASN
SEQRES 8 B 194 PHE GLN GLN LEU LYS VAL ARG VAL GLU HIS GLN LEU ASP
SEQRES 9 B 194 PRO GLN ASN TRP GLY ASN SER PRO LYS LEU ARG PHE THR
SEQRES 10 B 194 ARG PHE ILE THR ASN VAL GLN ALA ALA MET ASP VAL ASN
SEQRES 11 B 194 ASP LYS GLU LEU LEU HIS ILE ARG SER ASN VAL ILE LEU
SEQRES 12 B 194 HIS ARG ALA ARG ARG GLY ASN GLN VAL ASP VAL PHE TYR
SEQRES 13 B 194 ALA ALA ARG GLU ASP LYS TRP LYS ARG GLY GLU GLY GLY
SEQRES 14 B 194 VAL ARG LYS LEU VAL GLN ARG PHE VAL ASP TYR PRO GLU
SEQRES 15 B 194 ARG ILE LEU GLN THR HIS ASN LEU MET VAL PHE LEU
HET EDO A1448 4
HET EDO A1449 4
HET EDO A1450 4
HET OXY A1451 2
HET SO4 A1452 5
HET FES A1453 4
HET FE A1454 1
HET EDO B1695 4
HET EDO B1696 4
HET SO4 B1697 5
HET SO4 B1698 5
HET EDO B1699 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM OXY OXYGEN MOLECULE
HETNAM SO4 SULFATE ION
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM FE FE (III) ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 6(C2 H6 O2)
FORMUL 6 OXY O2
FORMUL 7 SO4 3(O4 S 2-)
FORMUL 8 FES FE2 S2
FORMUL 9 FE FE 3+
FORMUL 15 HOH *553(H2 O)
HELIX 1 1 SER A 10 GLY A 13 5 4
HELIX 2 2 LEU A 19 GLY A 22 5 4
HELIX 3 3 ASP A 23 ILE A 34 1 12
HELIX 4 4 SER A 46 ILE A 48 5 3
HELIX 5 5 PHE A 119 GLY A 125 1 7
HELIX 6 6 ASN A 129 LEU A 133 5 5
HELIX 7 7 PRO A 158 GLY A 164 1 7
HELIX 8 8 ASP A 165 LYS A 175 1 11
HELIX 9 9 TRP A 195 ASP A 205 1 11
HELIX 10 10 HIS A 208 HIS A 213 1 6
HELIX 11 11 HIS A 213 GLU A 221 1 9
HELIX 12 12 PHE A 224 ALA A 231 5 8
HELIX 13 13 LEU A 265 GLY A 285 1 21
HELIX 14 14 GLY A 285 ARG A 293 1 9
HELIX 15 15 PRO A 337 GLY A 353 1 17
HELIX 16 16 GLY A 356 GLY A 373 1 18
HELIX 17 17 GLU A 410 SER A 425 1 16
HELIX 18 18 ASN A 428 ALA A 435 1 8
HELIX 19 19 THR A 438 LYS A 445 1 8
HELIX 20 20 SER B 512 ASN B 524 1 13
HELIX 21 21 ASP B 527 ILE B 547 1 21
HELIX 22 22 ALA B 549 CYS B 557 1 9
HELIX 23 23 ASN B 591 ASP B 604 1 14
HELIX 24 24 ASN B 607 SER B 611 5 5
HELIX 25 25 GLU B 667 GLY B 669 5 3
SHEET 1 AA 2 SER A 15 LYS A 17 0
SHEET 2 AA 2 ASP A 382 LEU A 384 -1 O LEU A 383 N GLN A 16
SHEET 1 AB 3 LEU A 40 HIS A 44 0
SHEET 2 AB 3 PHE A 147 CYS A 151 -1 O ILE A 148 N LEU A 42
SHEET 3 AB 3 ARG A 140 PHE A 144 -1 O ARG A 140 N CYS A 151
SHEET 1 AC 4 ILE A 74 LEU A 78 0
SHEET 2 AC 4 ASP A 62 ARG A 68 -1 O ILE A 65 N PHE A 77
SHEET 3 AC 4 ASP A 53 MET A 59 -1 O ASP A 53 N ARG A 68
SHEET 4 AC 4 ALA A 93 ASN A 95 -1 O GLY A 94 N TYR A 54
SHEET 1 AD 3 GLY A 98 VAL A 100 0
SHEET 2 AD 3 GLY A 107 GLY A 109 -1 O PHE A 108 N PHE A 99
SHEET 3 AD 3 LEU A 114 SER A 116 -1 N GLN A 115 O GLY A 107
SHEET 1 AE 9 LEU A 180 ILE A 191 0
SHEET 2 AE 9 THR A 323 GLU A 333 -1 O THR A 324 N ILE A 191
SHEET 3 AE 9 VAL A 312 ASP A 320 -1 O PHE A 313 N TYR A 329
SHEET 4 AE 9 ASN A 304 LEU A 307 -1 O SER A 305 N LYS A 314
SHEET 5 AE 9 HIS A 295 VAL A 300 -1 O CYS A 298 N MET A 306
SHEET 6 AE 9 GLY A 249 LEU A 253 -1 O GLY A 249 N THR A 299
SHEET 7 AE 9 GLY A 239 THR A 243 -1 O LEU A 240 N VAL A 252
SHEET 8 AE 9 VAL A 402 GLY A 404 -1 O VAL A 402 N THR A 243
SHEET 9 AE 9 VAL A 393 TYR A 394 -1 O VAL A 393 N VAL A 403
SHEET 1 BA 6 ALA B 584 GLU B 590 0
SHEET 2 BA 6 VAL B 558 ARG B 569 -1 O TYR B 564 N GLU B 590
SHEET 3 BA 6 ARG B 671 ASP B 679 1 O LEU B 673 N GLY B 559
SHEET 4 BA 6 GLN B 651 ARG B 665 -1 O GLU B 660 N PHE B 677
SHEET 5 BA 6 LEU B 634 ARG B 647 -1 O LEU B 635 N TRP B 663
SHEET 6 BA 6 ARG B 615 MET B 627 -1 O ARG B 615 N ALA B 646
LINK SG CYS A 81 FE2 FES A1453 1555 1555 2.31
LINK ND1 HIS A 83 FE1 FES A1453 1555 1555 2.12
LINK SG CYS A 101 FE2 FES A1453 1555 1555 2.33
LINK ND1 HIS A 104 FE1 FES A1453 1555 1555 2.17
LINK NE2 HIS A 208 FE FE A1454 1555 1555 2.14
LINK NE2 HIS A 213 FE FE A1454 1555 1555 2.04
LINK OD2 ASP A 362 FE FE A1454 1555 1555 2.19
LINK OD1 ASP A 362 FE FE A1454 1555 1555 2.43
LINK O2 OXY A1451 FE FE A1454 1555 1555 2.34
LINK O1 OXY A1451 FE FE A1454 1555 1555 2.15
CISPEP 1 GLY A 184 PRO A 185 0 -2.14
CISPEP 2 PHE A 301 PRO A 302 0 -1.56
CISPEP 3 SER B 611 PRO B 612 0 1.40
SITE 1 AC1 5 LEU A 128 ASN A 129 LYS A 130 LYS A 131
SITE 2 AC1 5 HOH A2146
SITE 1 AC2 4 HIS A 208 HIS A 213 ASP A 362 OXY A1451
SITE 1 AC3 6 GLN B 563 GLN B 565 HOH B2073 HOH B2075
SITE 2 AC3 6 HOH B2150 HOH B2151
SITE 1 AC4 5 GLY B 559 SER B 560 GLU B 561 GLU B 667
SITE 2 AC4 5 LYS B 672
SITE 1 AC5 10 LEU A 31 PHE A 35 ALA A 36 MET A 59
SITE 2 AC5 10 GLY A 60 ILE A 61 ASP A 62 PHE A 152
SITE 3 AC5 10 TYR A 376 GLN A 377
SITE 1 AC6 8 HIS A 18 VAL A 80 CYS A 81 ARG A 82
SITE 2 AC6 8 SER A 381 ASP A 382 HOH A2397 HOH A2398
SITE 1 AC7 4 VAL A 183 ARG A 342 ASP A 346 HOH A2399
SITE 1 AC8 5 ASN A 201 HIS A 208 HIS A 213 ASP A 362
SITE 2 AC8 5 FE A1454
SITE 1 AC9 7 CYS A 81 HIS A 83 ARG A 84 CYS A 101
SITE 2 AC9 7 TYR A 103 HIS A 104 TRP A 106
SITE 1 BC1 7 TYR B 588 GLN B 602 MET B 691 VAL B 692
SITE 2 BC1 7 PHE B 693 HOH B2148 HOH B2149
SITE 1 BC2 8 PRO A 49 ALA A 50 ASP A 53 HOH A2079
SITE 2 BC2 8 ARG B 578 TYR B 579 LYS B 580 LEU B 581
SITE 1 BC3 6 ALA B 658 GLU B 660 PHE B 677 VAL B 678
SITE 2 BC3 6 ASP B 679 HOH B2138
CRYST1 140.277 140.277 208.754 90.00 90.00 120.00 H 3 2 18
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 0.007129 0.004116 0.000000 0.00000
SCALE2 0.000000 0.008231 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004790 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
