HEADER OXIDOREDUCTASE 07-OCT-10 3P4R
TITLE CRYSTAL STRUCTURE OF MENAQUINOL:FUMARATE OXIDOREDUCTASE IN COMPLEX
TITLE 2 WITH GLUTARATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FUMARATE REDUCTASE FLAVOPROTEIN SUBUNIT;
COMPND 3 CHAIN: A, M;
COMPND 4 FRAGMENT: UNP RESIDUES 1-577;
COMPND 5 EC: 1.3.99.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: FUMARATE REDUCTASE IRON-SULFUR SUBUNIT;
COMPND 9 CHAIN: B, N;
COMPND 10 EC: 1.3.99.1;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: FUMARATE REDUCTASE SUBUNIT C;
COMPND 14 CHAIN: C, O;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: FUMARATE REDUCTASE SUBUNIT D;
COMPND 18 CHAIN: D, P;
COMPND 19 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI 042;
SOURCE 3 ORGANISM_TAXID: 216592;
SOURCE 4 STRAIN: 042/EAEC;
SOURCE 5 GENE: EC042_4630, FRDA, SDY_4398;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI 042;
SOURCE 10 ORGANISM_TAXID: 216592;
SOURCE 11 STRAIN: 042/EAEC;
SOURCE 12 GENE: FRDB, EC042_4629;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O55:H7;
SOURCE 17 ORGANISM_TAXID: 701177;
SOURCE 18 STRAIN: CB9615/EPEC;
SOURCE 19 GENE: FRDC, G2583_4981;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 22 MOL_ID: 4;
SOURCE 23 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI 042;
SOURCE 24 ORGANISM_TAXID: 216592;
SOURCE 25 STRAIN: 042/EAEC;
SOURCE 26 GENE: FRDD, EC042_4627;
SOURCE 27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 28 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.M.TOMASIAK,T.L.ARCHULETA,J.ANDRELL,C.LUNA-CHAVEZ,T.A.DAVIS,
AUTHOR 2 M.SARWAR,A.J.HAM,W.H.MCDONALD,V.YANKOWSKAYA,H.A.STERN,J.N.JOHNSTON,
AUTHOR 3 E.MAKLASHINA,G.CECCHINI,T.M.IVERSON
REVDAT 3 16-MAR-11 3P4R 1 JRNL
REVDAT 2 08-DEC-10 3P4R 1 JRNL
REVDAT 1 24-NOV-10 3P4R 0
JRNL AUTH T.M.TOMASIAK,T.L.ARCHULETA,J.ANDRELL,C.LUNA-CHAVEZ,
JRNL AUTH 2 T.A.DAVIS,M.SARWAR,A.J.HAM,W.H.MCDONALD,V.YANKOVSKAYA,
JRNL AUTH 3 H.A.STERN,J.N.JOHNSTON,E.MAKLASHINA,G.CECCHINI,T.M.IVERSON
JRNL TITL GEOMETRIC RESTRAINT DRIVES ON- AND OFF-PATHWAY CATALYSIS BY
JRNL TITL 2 THE ESCHERICHIA COLI MENAQUINOL:FUMARATE REDUCTASE.
JRNL REF J.BIOL.CHEM. V. 286 3047 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21098488
JRNL DOI 10.1074/JBC.M110.192849
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC5
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 64607
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 + TEST SET) : 0.249
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.284
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1194
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16642
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 162
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 95.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.45000
REMARK 3 B22 (A**2) : -5.67000
REMARK 3 B33 (A**2) : 5.22000
REMARK 3 B12 (A**2) : 0.00000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.407
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 45.753
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3P4R COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-10.
REMARK 100 THE RCSB ID CODE IS RCSB061954.
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 : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88348
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.3
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 67.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.39400
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14.5% PEG 8000 MME, 125MM MGAC, 95MM
REMARK 280 CITRATE PH 5.8, 0.1% W/V DTT, 0.1MM EDTA, 10MM GLUTARATE, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 298K
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 48.33900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 134.77900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 69.00800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 134.77900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.33900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 69.00800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 17380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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
REMARK 350 BIOMOLECULE: 2
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: 17280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -153.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P
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: 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 SG CYS N 214 FE4 SF4 N 246 1.61
REMARK 500 SG CYS B 210 FE3 F3S B 245 1.71
REMARK 500 SG CYS B 204 FE1 F3S B 245 1.76
REMARK 500 SG CYS B 151 FE1 SF4 B 246 1.81
REMARK 500 O ALA B 32 NH1 ARG B 82 2.10
REMARK 500 NE2 HIS M 44 C8M FAD M 601 2.19
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 CYS B 65 CB CYS B 65 SG -0.123
REMARK 500 ASN D 4 CB ASN D 4 CG 0.180
REMARK 500 LYS D 6 CD LYS D 6 CE 0.270
REMARK 500 VAL D 12 CB VAL D 12 CG1 0.127
REMARK 500 ASP D 47 CG ASP D 47 OD1 0.177
REMARK 500 TYR D 51 CG TYR D 51 CD2 -0.147
REMARK 500 TYR D 51 CG TYR D 51 CD1 -0.206
REMARK 500 TYR D 51 CE1 TYR D 51 CZ -0.268
REMARK 500 TYR D 51 CZ TYR D 51 OH 0.165
REMARK 500 TYR D 51 CZ TYR D 51 CE2 -0.235
REMARK 500 ARG D 81 CZ ARG D 81 NH1 0.089
REMARK 500 ASN P 4 CB ASN P 4 CG 0.288
REMARK 500 ASN P 4 CG ASN P 4 ND2 0.207
REMARK 500 LYS P 6 CD LYS P 6 CE 0.180
REMARK 500 ASP P 9 CG ASP P 9 OD1 0.349
REMARK 500 ASP P 47 CA ASP P 47 CB 0.148
REMARK 500 ASP P 47 CG ASP P 47 OD2 0.247
REMARK 500 TYR P 51 CB TYR P 51 CG -0.169
REMARK 500 TYR P 51 CE1 TYR P 51 CZ -0.079
REMARK 500 TYR P 51 CZ TYR P 51 OH 0.258
REMARK 500 TYR P 51 CZ TYR P 51 CE2 -0.252
REMARK 500 TYR P 51 CE2 TYR P 51 CD2 0.096
REMARK 500 GLU P 52 CG GLU P 52 CD -0.095
REMARK 500 ARG P 64 CZ ARG P 64 NH1 0.099
REMARK 500 ARG P 81 CZ ARG P 81 NH1 0.132
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 LYS D 6 CD - CE - NZ ANGL. DEV. = 15.8 DEGREES
REMARK 500 TYR D 51 N - CA - CB ANGL. DEV. = -16.3 DEGREES
REMARK 500 TYR D 51 CB - CG - CD2 ANGL. DEV. = 16.9 DEGREES
REMARK 500 TYR D 51 CD1 - CG - CD2 ANGL. DEV. = -17.2 DEGREES
REMARK 500 TYR D 51 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 TYR D 51 CG - CD1 - CE1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 TYR D 51 CD1 - CE1 - CZ ANGL. DEV. = 12.8 DEGREES
REMARK 500 TYR D 51 CE1 - CZ - CE2 ANGL. DEV. = -20.3 DEGREES
REMARK 500 TYR D 51 CZ - CE2 - CD2 ANGL. DEV. = 12.4 DEGREES
REMARK 500 ARG D 81 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 PRO M 40 C - N - CA ANGL. DEV. = 9.0 DEGREES
REMARK 500 LYS P 6 CD - CE - NZ ANGL. DEV. = 16.0 DEGREES
REMARK 500 ASP P 9 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP P 47 CA - CB - CG ANGL. DEV. = -15.8 DEGREES
REMARK 500 ASP P 47 CB - CG - OD1 ANGL. DEV. = -13.7 DEGREES
REMARK 500 ASP P 47 CB - CG - OD2 ANGL. DEV. = 20.0 DEGREES
REMARK 500 TYR P 51 CD1 - CG - CD2 ANGL. DEV. = -16.3 DEGREES
REMARK 500 TYR P 51 CB - CG - CD1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 TYR P 51 CG - CD2 - CE2 ANGL. DEV. = 11.3 DEGREES
REMARK 500 TYR P 51 CD1 - CE1 - CZ ANGL. DEV. = 11.8 DEGREES
REMARK 500 ILE P 62 CG1 - CB - CG2 ANGL. DEV. = -14.4 DEGREES
REMARK 500 ARG P 81 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG P 81 NE - CZ - NH2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ILE P 91 CB - CG1 - CD1 ANGL. DEV. = 22.1 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 56 -34.81 -131.11
REMARK 500 ALA A 128 -128.53 45.58
REMARK 500 LYS A 280 -9.56 84.35
REMARK 500 MET A 282 -132.90 59.04
REMARK 500 HIS A 355 -68.51 -125.15
REMARK 500 SER A 393 -7.54 88.56
REMARK 500 CYS A 463 73.90 -104.14
REMARK 500 THR A 571 -75.87 -105.41
REMARK 500 LEU B 47 -60.48 -100.68
REMARK 500 SER B 56 -73.50 -170.28
REMARK 500 MET B 59 30.91 -142.20
REMARK 500 ASP B 86 31.87 -92.82
REMARK 500 ASP B 101 -113.72 42.43
REMARK 500 CYS B 214 107.26 -52.27
REMARK 500 LYS C 18 -72.03 -61.26
REMARK 500 LYS C 99 72.44 37.15
REMARK 500 ASN D 4 106.84 -163.69
REMARK 500 THR D 117 140.30 84.95
REMARK 500 PRO M 40 -35.14 -36.12
REMARK 500 ALA M 56 -68.02 -125.41
REMARK 500 ALA M 128 -127.36 49.14
REMARK 500 ALA M 195 46.39 -141.98
REMARK 500 ASN M 256 -169.68 -102.12
REMARK 500 MET M 282 -124.45 55.20
REMARK 500 HIS M 355 -79.14 -115.85
REMARK 500 ASP M 364 -161.69 -73.64
REMARK 500 CYS M 367 16.89 53.45
REMARK 500 THR M 416 48.28 -107.39
REMARK 500 LYS M 526 63.60 -103.73
REMARK 500 THR M 571 -76.19 -112.66
REMARK 500 PRO M 575 63.57 -68.64
REMARK 500 SER N 56 -75.28 -175.18
REMARK 500 TYR N 84 60.01 -119.83
REMARK 500 ASP N 101 -97.65 38.26
REMARK 500 SER N 183 10.87 -68.95
REMARK 500 ASN O 51 3.83 -69.68
REMARK 500 LYS O 99 -112.06 53.26
REMARK 500 ASN P 4 112.90 -161.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ASP D 9 0.10 SIDE CHAIN
REMARK 500 TYR D 51 0.16 SIDE CHAIN
REMARK 500 ASP P 9 0.09 SIDE CHAIN
REMARK 500 TYR P 51 0.13 SIDE CHAIN
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 SF4 B 246 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 214 SG
REMARK 620 2 SF4 B 246 S1 122.8
REMARK 620 3 SF4 B 246 S2 118.1 102.3
REMARK 620 4 SF4 B 246 S3 107.5 103.4 99.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S N 245 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 204 SG
REMARK 620 2 F3S N 245 S1 106.7
REMARK 620 3 F3S N 245 S2 125.7 103.4
REMARK 620 4 F3S N 245 S3 108.7 100.6 108.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 244 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 62 SG
REMARK 620 2 FES B 244 S1 111.7
REMARK 620 3 FES B 244 S2 117.3 94.4
REMARK 620 4 CYS B 57 SG 120.2 101.7 107.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES N 244 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 57 SG
REMARK 620 2 FES N 244 S1 116.8
REMARK 620 3 FES N 244 S2 115.0 90.2
REMARK 620 4 CYS N 62 SG 111.3 114.0 107.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 246 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 148 SG
REMARK 620 2 SF4 B 246 S1 116.9
REMARK 620 3 SF4 B 246 S3 122.0 102.1
REMARK 620 4 SF4 B 246 S4 106.5 106.8 100.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 244 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 65 SG
REMARK 620 2 FES B 244 S1 135.2
REMARK 620 3 FES B 244 S2 114.9 94.9
REMARK 620 4 CYS B 77 SG 88.4 110.2 113.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S N 245 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 210 SG
REMARK 620 2 F3S N 245 S1 102.3
REMARK 620 3 F3S N 245 S3 124.2 103.4
REMARK 620 4 F3S N 245 S4 108.6 113.4 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES N 244 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 65 SG
REMARK 620 2 FES N 244 S1 119.2
REMARK 620 3 FES N 244 S2 124.8 90.4
REMARK 620 4 CYS N 77 SG 97.8 102.2 121.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S N 245 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 158 SG
REMARK 620 2 F3S N 245 S2 121.0
REMARK 620 3 F3S N 245 S3 106.2 104.1
REMARK 620 4 F3S N 245 S4 107.7 112.3 103.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 N 246 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 154 SG
REMARK 620 2 SF4 N 246 S1 139.0
REMARK 620 3 SF4 N 246 S2 93.9 93.3
REMARK 620 4 SF4 N 246 S4 109.1 111.9 79.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B 245 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 158 SG
REMARK 620 2 F3S B 245 S2 117.9
REMARK 620 3 F3S B 245 S3 106.4 102.8
REMARK 620 4 F3S B 245 S4 112.7 110.2 105.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 246 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 154 SG
REMARK 620 2 SF4 B 246 S1 124.3
REMARK 620 3 SF4 B 246 S2 106.9 107.1
REMARK 620 4 SF4 B 246 S4 106.0 109.8 100.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 N 246 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 148 SG
REMARK 620 2 SF4 N 246 S1 154.9
REMARK 620 3 SF4 N 246 S3 117.0 74.4
REMARK 620 4 SF4 N 246 S4 99.2 93.6 118.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 N 246 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 151 SG
REMARK 620 2 SF4 N 246 S2 144.0
REMARK 620 3 SF4 N 246 S3 118.1 89.0
REMARK 620 4 SF4 N 246 S4 111.8 65.7 120.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 244
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 245
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES N 244
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S N 245
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GUA A 577
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 N 246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GUA M 577
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD M 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3P4Q RELATED DB: PDB
REMARK 900 RELATED ID: 3P4P RELATED DB: PDB
REMARK 900 RELATED ID: 3P4S RELATED DB: PDB
DBREF 3P4R A 0 576 UNP D3GV56 D3GV56_ECO44 1 577
DBREF 3P4R B 1 243 UNP D3GV55 D3GV55_ECO44 2 244
DBREF 3P4R C 1 130 UNP D3QL74 D3QL74_ECOCB 2 131
DBREF 3P4R D 0 118 UNP D3GV53 D3GV53_ECO44 1 119
DBREF 3P4R M 0 576 UNP D3GV56 D3GV56_ECO44 1 577
DBREF 3P4R N 1 243 UNP D3GV55 D3GV55_ECO44 2 244
DBREF 3P4R O 1 130 UNP D3QL74 D3QL74_ECOCB 2 131
DBREF 3P4R P 0 118 UNP D3GV53 D3GV53_ECO44 1 119
SEQRES 1 A 577 MET GLN THR PHE GLN ALA ASP LEU ALA ILE VAL GLY ALA
SEQRES 2 A 577 GLY GLY ALA GLY LEU ARG ALA ALA ILE ALA ALA ALA GLN
SEQRES 3 A 577 ALA ASN PRO ASN ALA LYS ILE ALA LEU ILE SER LYS VAL
SEQRES 4 A 577 TYR PRO MET ARG SER HIS THR VAL ALA ALA GLU GLY GLY
SEQRES 5 A 577 SER ALA ALA VAL ALA GLN ASP HIS ASP SER PHE GLU TYR
SEQRES 6 A 577 HIS PHE HIS ASP THR VAL ALA GLY GLY ASP TRP LEU CYS
SEQRES 7 A 577 GLU GLN ASP VAL VAL ASP TYR PHE VAL HIS HIS CYS PRO
SEQRES 8 A 577 THR GLU MET THR GLN LEU GLU LEU TRP GLY CYS PRO TRP
SEQRES 9 A 577 SER ARG ARG PRO ASP GLY SER VAL ASN VAL ARG ARG PHE
SEQRES 10 A 577 GLY GLY MET LYS ILE GLU ARG THR TRP PHE ALA ALA ASP
SEQRES 11 A 577 LYS THR GLY PHE HIS MET LEU HIS THR LEU PHE GLN THR
SEQRES 12 A 577 SER LEU GLN PHE PRO GLN ILE GLN ARG PHE ASP GLU HIS
SEQRES 13 A 577 PHE VAL LEU ASP ILE LEU VAL ASP ASP GLY HIS VAL ARG
SEQRES 14 A 577 GLY LEU VAL ALA MET ASN MET MET GLU GLY THR LEU VAL
SEQRES 15 A 577 GLN ILE ARG ALA ASN ALA VAL VAL MET ALA THR GLY GLY
SEQRES 16 A 577 ALA GLY ARG VAL TYR ARG TYR ASN THR ASN GLY GLY ILE
SEQRES 17 A 577 VAL THR GLY ASP GLY MET GLY MET ALA LEU SER HIS GLY
SEQRES 18 A 577 VAL PRO LEU ARG ASP MET GLU PHE VAL GLN TYR HIS PRO
SEQRES 19 A 577 THR GLY LEU PRO GLY SER GLY ILE LEU MET THR GLU GLY
SEQRES 20 A 577 CYS ARG GLY GLU GLY GLY ILE LEU VAL ASN LYS ASN GLY
SEQRES 21 A 577 TYR ARG TYR LEU GLN ASP TYR GLY MET GLY PRO GLU THR
SEQRES 22 A 577 PRO LEU GLY GLU PRO LYS ASN LYS TYR MET GLU LEU GLY
SEQRES 23 A 577 PRO ARG ASP LYS VAL SER GLN ALA PHE TRP HIS GLU TRP
SEQRES 24 A 577 ARG LYS GLY ASN THR ILE SER THR PRO ARG GLY ASP VAL
SEQRES 25 A 577 VAL TYR LEU ASP LEU ARG HIS LEU GLY GLU LYS LYS LEU
SEQRES 26 A 577 HIS GLU ARG LEU PRO PHE ILE CYS GLU LEU ALA LYS ALA
SEQRES 27 A 577 TYR VAL GLY VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL
SEQRES 28 A 577 ARG PRO THR ALA HIS TYR THR MET GLY GLY ILE GLU THR
SEQRES 29 A 577 ASP GLN ASN CYS GLU THR ARG ILE LYS GLY LEU PHE ALA
SEQRES 30 A 577 VAL GLY GLU CYS SER SER VAL GLY LEU HIS GLY ALA ASN
SEQRES 31 A 577 ARG LEU GLY SER ASN SER LEU ALA GLU LEU VAL VAL PHE
SEQRES 32 A 577 GLY ARG LEU ALA GLY GLU GLN ALA THR GLU ARG ALA ALA
SEQRES 33 A 577 THR ALA GLY ASN GLY ASN GLU ALA ALA ILE GLU ALA GLN
SEQRES 34 A 577 ALA ALA GLY VAL GLU GLN ARG LEU LYS ASP LEU VAL ASN
SEQRES 35 A 577 GLN ASP GLY GLY GLU ASN TRP ALA LYS ILE ARG ASP GLU
SEQRES 36 A 577 MET GLY LEU ALA MET GLU GLU GLY CYS GLY ILE TYR ARG
SEQRES 37 A 577 THR PRO GLU LEU MET GLN LYS THR ILE ASP LYS LEU ALA
SEQRES 38 A 577 GLU LEU GLN GLU ARG PHE LYS ARG VAL ARG ILE THR ASP
SEQRES 39 A 577 THR SER SER VAL PHE ASN THR ASP LEU LEU TYR THR ILE
SEQRES 40 A 577 GLU LEU GLY HIS GLY LEU ASN VAL ALA GLU CYS MET ALA
SEQRES 41 A 577 HIS SER ALA MET ALA ARG LYS GLU SER ARG GLY ALA HIS
SEQRES 42 A 577 GLN ARG LEU ASP GLU GLY CYS THR GLU ARG ASP ASP VAL
SEQRES 43 A 577 ASN PHE LEU LYS HIS THR LEU ALA PHE ARG ASP ALA ASP
SEQRES 44 A 577 GLY THR THR ARG LEU GLU TYR SER ASP VAL LYS ILE THR
SEQRES 45 A 577 THR LEU PRO PRO ALA
SEQRES 1 B 243 ALA GLU MET LYS ASN LEU LYS ILE GLU VAL VAL ARG TYR
SEQRES 2 B 243 ASN PRO GLU VAL ASP THR ALA PRO HIS SER ALA PHE TYR
SEQRES 3 B 243 GLU VAL PRO TYR ASP ALA THR THR SER LEU LEU ASP ALA
SEQRES 4 B 243 LEU GLY TYR ILE LYS ASP ASN LEU ALA PRO ASP LEU SER
SEQRES 5 B 243 TYR ARG TRP SER CYS ARG MET ALA ILE CYS GLY SER CYS
SEQRES 6 B 243 GLY MET MET VAL ASN ASN VAL PRO LYS LEU ALA CYS LYS
SEQRES 7 B 243 THR PHE LEU ARG ASP TYR THR ASP GLY MET LYS VAL GLU
SEQRES 8 B 243 ALA LEU ALA ASN PHE PRO ILE GLU ARG ASP LEU VAL VAL
SEQRES 9 B 243 ASP MET THR HIS PHE ILE GLU SER LEU GLU ALA ILE LYS
SEQRES 10 B 243 PRO TYR ILE ILE GLY ASN SER ARG THR ALA ASP GLN GLY
SEQRES 11 B 243 THR ASN ILE GLN THR PRO ALA GLN MET ALA LYS TYR HIS
SEQRES 12 B 243 GLN PHE SER GLY CYS ILE ASN CYS GLY LEU CYS TYR ALA
SEQRES 13 B 243 ALA CYS PRO GLN PHE GLY LEU ASN PRO GLU PHE ILE GLY
SEQRES 14 B 243 PRO ALA ALA ILE THR LEU ALA HIS ARG TYR ASN GLU ASP
SEQRES 15 B 243 SER ARG ASP HIS GLY LYS LYS GLU ARG MET ALA GLN LEU
SEQRES 16 B 243 ASN SER GLN ASN GLY VAL TRP SER CYS THR PHE VAL GLY
SEQRES 17 B 243 TYR CYS SER GLU VAL CYS PRO LYS HIS VAL ASP PRO ALA
SEQRES 18 B 243 ALA ALA ILE GLN GLN GLY LYS VAL GLU SER SER LYS ASP
SEQRES 19 B 243 PHE LEU ILE ALA THR LEU LYS PRO ARG
SEQRES 1 C 130 THR THR LYS ARG LYS PRO TYR VAL ARG PRO MET THR SER
SEQRES 2 C 130 THR TRP TRP LYS LYS LEU PRO PHE TYR ARG PHE TYR MET
SEQRES 3 C 130 LEU ARG GLU GLY THR ALA VAL PRO ALA VAL TRP PHE SER
SEQRES 4 C 130 ILE GLU LEU ILE PHE GLY LEU PHE ALA LEU LYS ASN GLY
SEQRES 5 C 130 PRO GLU ALA TRP ALA GLY PHE VAL ASP PHE LEU GLN ASN
SEQRES 6 C 130 PRO VAL ILE VAL ILE ILE ASN LEU ILE THR LEU ALA ALA
SEQRES 7 C 130 ALA LEU LEU HIS THR LYS THR TRP PHE GLU LEU ALA PRO
SEQRES 8 C 130 LYS ALA ALA ASN ILE ILE VAL LYS ASP GLU LYS MET GLY
SEQRES 9 C 130 PRO GLU PRO ILE ILE LYS SER LEU TRP ALA VAL THR VAL
SEQRES 10 C 130 VAL ALA THR ILE VAL ILE LEU PHE VAL ALA LEU TYR TRP
SEQRES 1 D 119 MET ILE ASN PRO ASN PRO LYS ARG SER ASP GLU PRO VAL
SEQRES 2 D 119 PHE TRP GLY LEU PHE GLY ALA GLY GLY MET TRP SER ALA
SEQRES 3 D 119 ILE ILE ALA PRO VAL MET ILE LEU LEU VAL GLY ILE LEU
SEQRES 4 D 119 LEU PRO LEU GLY LEU PHE PRO GLY ASP ALA LEU SER TYR
SEQRES 5 D 119 GLU ARG VAL LEU ALA PHE ALA GLN SER PHE ILE GLY ARG
SEQRES 6 D 119 VAL PHE LEU PHE LEU MET ILE VAL LEU PRO LEU TRP CYS
SEQRES 7 D 119 GLY LEU HIS ARG MET HIS HIS ALA MET HIS ASP LEU LYS
SEQRES 8 D 119 ILE HIS VAL PRO ALA GLY LYS TRP VAL PHE TYR GLY LEU
SEQRES 9 D 119 ALA ALA ILE LEU THR VAL VAL THR LEU ILE GLY VAL VAL
SEQRES 10 D 119 THR ILE
SEQRES 1 M 577 MET GLN THR PHE GLN ALA ASP LEU ALA ILE VAL GLY ALA
SEQRES 2 M 577 GLY GLY ALA GLY LEU ARG ALA ALA ILE ALA ALA ALA GLN
SEQRES 3 M 577 ALA ASN PRO ASN ALA LYS ILE ALA LEU ILE SER LYS VAL
SEQRES 4 M 577 TYR PRO MET ARG SER HIS THR VAL ALA ALA GLU GLY GLY
SEQRES 5 M 577 SER ALA ALA VAL ALA GLN ASP HIS ASP SER PHE GLU TYR
SEQRES 6 M 577 HIS PHE HIS ASP THR VAL ALA GLY GLY ASP TRP LEU CYS
SEQRES 7 M 577 GLU GLN ASP VAL VAL ASP TYR PHE VAL HIS HIS CYS PRO
SEQRES 8 M 577 THR GLU MET THR GLN LEU GLU LEU TRP GLY CYS PRO TRP
SEQRES 9 M 577 SER ARG ARG PRO ASP GLY SER VAL ASN VAL ARG ARG PHE
SEQRES 10 M 577 GLY GLY MET LYS ILE GLU ARG THR TRP PHE ALA ALA ASP
SEQRES 11 M 577 LYS THR GLY PHE HIS MET LEU HIS THR LEU PHE GLN THR
SEQRES 12 M 577 SER LEU GLN PHE PRO GLN ILE GLN ARG PHE ASP GLU HIS
SEQRES 13 M 577 PHE VAL LEU ASP ILE LEU VAL ASP ASP GLY HIS VAL ARG
SEQRES 14 M 577 GLY LEU VAL ALA MET ASN MET MET GLU GLY THR LEU VAL
SEQRES 15 M 577 GLN ILE ARG ALA ASN ALA VAL VAL MET ALA THR GLY GLY
SEQRES 16 M 577 ALA GLY ARG VAL TYR ARG TYR ASN THR ASN GLY GLY ILE
SEQRES 17 M 577 VAL THR GLY ASP GLY MET GLY MET ALA LEU SER HIS GLY
SEQRES 18 M 577 VAL PRO LEU ARG ASP MET GLU PHE VAL GLN TYR HIS PRO
SEQRES 19 M 577 THR GLY LEU PRO GLY SER GLY ILE LEU MET THR GLU GLY
SEQRES 20 M 577 CYS ARG GLY GLU GLY GLY ILE LEU VAL ASN LYS ASN GLY
SEQRES 21 M 577 TYR ARG TYR LEU GLN ASP TYR GLY MET GLY PRO GLU THR
SEQRES 22 M 577 PRO LEU GLY GLU PRO LYS ASN LYS TYR MET GLU LEU GLY
SEQRES 23 M 577 PRO ARG ASP LYS VAL SER GLN ALA PHE TRP HIS GLU TRP
SEQRES 24 M 577 ARG LYS GLY ASN THR ILE SER THR PRO ARG GLY ASP VAL
SEQRES 25 M 577 VAL TYR LEU ASP LEU ARG HIS LEU GLY GLU LYS LYS LEU
SEQRES 26 M 577 HIS GLU ARG LEU PRO PHE ILE CYS GLU LEU ALA LYS ALA
SEQRES 27 M 577 TYR VAL GLY VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL
SEQRES 28 M 577 ARG PRO THR ALA HIS TYR THR MET GLY GLY ILE GLU THR
SEQRES 29 M 577 ASP GLN ASN CYS GLU THR ARG ILE LYS GLY LEU PHE ALA
SEQRES 30 M 577 VAL GLY GLU CYS SER SER VAL GLY LEU HIS GLY ALA ASN
SEQRES 31 M 577 ARG LEU GLY SER ASN SER LEU ALA GLU LEU VAL VAL PHE
SEQRES 32 M 577 GLY ARG LEU ALA GLY GLU GLN ALA THR GLU ARG ALA ALA
SEQRES 33 M 577 THR ALA GLY ASN GLY ASN GLU ALA ALA ILE GLU ALA GLN
SEQRES 34 M 577 ALA ALA GLY VAL GLU GLN ARG LEU LYS ASP LEU VAL ASN
SEQRES 35 M 577 GLN ASP GLY GLY GLU ASN TRP ALA LYS ILE ARG ASP GLU
SEQRES 36 M 577 MET GLY LEU ALA MET GLU GLU GLY CYS GLY ILE TYR ARG
SEQRES 37 M 577 THR PRO GLU LEU MET GLN LYS THR ILE ASP LYS LEU ALA
SEQRES 38 M 577 GLU LEU GLN GLU ARG PHE LYS ARG VAL ARG ILE THR ASP
SEQRES 39 M 577 THR SER SER VAL PHE ASN THR ASP LEU LEU TYR THR ILE
SEQRES 40 M 577 GLU LEU GLY HIS GLY LEU ASN VAL ALA GLU CYS MET ALA
SEQRES 41 M 577 HIS SER ALA MET ALA ARG LYS GLU SER ARG GLY ALA HIS
SEQRES 42 M 577 GLN ARG LEU ASP GLU GLY CYS THR GLU ARG ASP ASP VAL
SEQRES 43 M 577 ASN PHE LEU LYS HIS THR LEU ALA PHE ARG ASP ALA ASP
SEQRES 44 M 577 GLY THR THR ARG LEU GLU TYR SER ASP VAL LYS ILE THR
SEQRES 45 M 577 THR LEU PRO PRO ALA
SEQRES 1 N 243 ALA GLU MET LYS ASN LEU LYS ILE GLU VAL VAL ARG TYR
SEQRES 2 N 243 ASN PRO GLU VAL ASP THR ALA PRO HIS SER ALA PHE TYR
SEQRES 3 N 243 GLU VAL PRO TYR ASP ALA THR THR SER LEU LEU ASP ALA
SEQRES 4 N 243 LEU GLY TYR ILE LYS ASP ASN LEU ALA PRO ASP LEU SER
SEQRES 5 N 243 TYR ARG TRP SER CYS ARG MET ALA ILE CYS GLY SER CYS
SEQRES 6 N 243 GLY MET MET VAL ASN ASN VAL PRO LYS LEU ALA CYS LYS
SEQRES 7 N 243 THR PHE LEU ARG ASP TYR THR ASP GLY MET LYS VAL GLU
SEQRES 8 N 243 ALA LEU ALA ASN PHE PRO ILE GLU ARG ASP LEU VAL VAL
SEQRES 9 N 243 ASP MET THR HIS PHE ILE GLU SER LEU GLU ALA ILE LYS
SEQRES 10 N 243 PRO TYR ILE ILE GLY ASN SER ARG THR ALA ASP GLN GLY
SEQRES 11 N 243 THR ASN ILE GLN THR PRO ALA GLN MET ALA LYS TYR HIS
SEQRES 12 N 243 GLN PHE SER GLY CYS ILE ASN CYS GLY LEU CYS TYR ALA
SEQRES 13 N 243 ALA CYS PRO GLN PHE GLY LEU ASN PRO GLU PHE ILE GLY
SEQRES 14 N 243 PRO ALA ALA ILE THR LEU ALA HIS ARG TYR ASN GLU ASP
SEQRES 15 N 243 SER ARG ASP HIS GLY LYS LYS GLU ARG MET ALA GLN LEU
SEQRES 16 N 243 ASN SER GLN ASN GLY VAL TRP SER CYS THR PHE VAL GLY
SEQRES 17 N 243 TYR CYS SER GLU VAL CYS PRO LYS HIS VAL ASP PRO ALA
SEQRES 18 N 243 ALA ALA ILE GLN GLN GLY LYS VAL GLU SER SER LYS ASP
SEQRES 19 N 243 PHE LEU ILE ALA THR LEU LYS PRO ARG
SEQRES 1 O 130 THR THR LYS ARG LYS PRO TYR VAL ARG PRO MET THR SER
SEQRES 2 O 130 THR TRP TRP LYS LYS LEU PRO PHE TYR ARG PHE TYR MET
SEQRES 3 O 130 LEU ARG GLU GLY THR ALA VAL PRO ALA VAL TRP PHE SER
SEQRES 4 O 130 ILE GLU LEU ILE PHE GLY LEU PHE ALA LEU LYS ASN GLY
SEQRES 5 O 130 PRO GLU ALA TRP ALA GLY PHE VAL ASP PHE LEU GLN ASN
SEQRES 6 O 130 PRO VAL ILE VAL ILE ILE ASN LEU ILE THR LEU ALA ALA
SEQRES 7 O 130 ALA LEU LEU HIS THR LYS THR TRP PHE GLU LEU ALA PRO
SEQRES 8 O 130 LYS ALA ALA ASN ILE ILE VAL LYS ASP GLU LYS MET GLY
SEQRES 9 O 130 PRO GLU PRO ILE ILE LYS SER LEU TRP ALA VAL THR VAL
SEQRES 10 O 130 VAL ALA THR ILE VAL ILE LEU PHE VAL ALA LEU TYR TRP
SEQRES 1 P 119 MET ILE ASN PRO ASN PRO LYS ARG SER ASP GLU PRO VAL
SEQRES 2 P 119 PHE TRP GLY LEU PHE GLY ALA GLY GLY MET TRP SER ALA
SEQRES 3 P 119 ILE ILE ALA PRO VAL MET ILE LEU LEU VAL GLY ILE LEU
SEQRES 4 P 119 LEU PRO LEU GLY LEU PHE PRO GLY ASP ALA LEU SER TYR
SEQRES 5 P 119 GLU ARG VAL LEU ALA PHE ALA GLN SER PHE ILE GLY ARG
SEQRES 6 P 119 VAL PHE LEU PHE LEU MET ILE VAL LEU PRO LEU TRP CYS
SEQRES 7 P 119 GLY LEU HIS ARG MET HIS HIS ALA MET HIS ASP LEU LYS
SEQRES 8 P 119 ILE HIS VAL PRO ALA GLY LYS TRP VAL PHE TYR GLY LEU
SEQRES 9 P 119 ALA ALA ILE LEU THR VAL VAL THR LEU ILE GLY VAL VAL
SEQRES 10 P 119 THR ILE
HET FES B 244 4
HET F3S B 245 7
HET SF4 B 246 8
HET FAD A 601 53
HET FES N 244 4
HET F3S N 245 7
HET GUA A 577 9
HET SF4 N 246 8
HET GUA M 577 9
HET FAD M 601 53
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM F3S FE3-S4 CLUSTER
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM GUA GLUTARIC ACID
FORMUL 9 FES 2(FE2 S2)
FORMUL 10 F3S 2(FE3 S4)
FORMUL 11 SF4 2(FE4 S4)
FORMUL 12 FAD 2(C27 H33 N9 O15 P2)
FORMUL 15 GUA 2(C5 H8 O4)
HELIX 1 1 GLY A 13 ASN A 27 1 15
HELIX 2 2 TYR A 39 ALA A 48 5 10
HELIX 3 3 SER A 61 GLY A 73 1 13
HELIX 4 4 GLU A 78 TRP A 99 1 22
HELIX 5 5 LYS A 130 LEU A 144 1 15
HELIX 6 6 ALA A 195 TYR A 199 5 5
HELIX 7 7 GLY A 210 SER A 218 1 9
HELIX 8 8 GLU A 245 GLU A 250 1 6
HELIX 9 9 ARG A 261 GLY A 267 5 7
HELIX 10 10 TYR A 281 GLY A 285 5 5
HELIX 11 11 PRO A 286 LYS A 300 1 15
HELIX 12 12 LEU A 316 LEU A 319 5 4
HELIX 13 13 GLY A 320 LEU A 328 1 9
HELIX 14 14 LEU A 328 GLY A 340 1 13
HELIX 15 15 SER A 393 ALA A 417 1 25
HELIX 16 16 ASN A 421 GLN A 442 1 22
HELIX 17 17 ASN A 447 CYS A 463 1 17
HELIX 18 18 THR A 468 LYS A 487 1 20
HELIX 19 19 ASN A 499 ARG A 525 1 27
HELIX 20 20 ASP A 543 LEU A 548 1 6
HELIX 21 21 SER B 35 LEU B 47 1 13
HELIX 22 22 PHE B 80 TYR B 84 5 5
HELIX 23 23 MET B 106 ILE B 116 1 11
HELIX 24 24 THR B 126 GLY B 130 5 5
HELIX 25 25 THR B 135 HIS B 143 1 9
HELIX 26 26 GLN B 144 CYS B 148 5 5
HELIX 27 27 GLY B 152 CYS B 158 1 7
HELIX 28 28 CYS B 158 ASN B 164 1 7
HELIX 29 29 GLY B 169 GLU B 181 1 13
HELIX 30 30 GLY B 187 SER B 197 1 11
HELIX 31 31 GLY B 200 CYS B 204 5 5
HELIX 32 32 GLY B 208 CYS B 214 1 7
HELIX 33 33 ASP B 219 LEU B 240 1 22
HELIX 34 34 THR C 14 LYS C 18 5 5
HELIX 35 35 LEU C 19 THR C 31 1 13
HELIX 36 36 THR C 31 ASN C 51 1 21
HELIX 37 37 GLY C 52 LEU C 63 1 12
HELIX 38 38 ASN C 65 ALA C 90 1 26
HELIX 39 39 PRO C 91 ALA C 94 5 4
HELIX 40 40 PRO C 105 TRP C 130 1 26
HELIX 41 41 GLU D 10 ILE D 37 1 28
HELIX 42 42 SER D 50 GLN D 59 1 10
HELIX 43 43 SER D 60 LEU D 89 1 30
HELIX 44 44 ALA D 95 VAL D 116 1 22
HELIX 45 45 GLY M 13 GLN M 25 1 13
HELIX 46 46 TYR M 39 ALA M 48 5 10
HELIX 47 47 SER M 61 ASP M 74 1 14
HELIX 48 48 GLU M 78 TRP M 99 1 22
HELIX 49 49 LYS M 130 LEU M 144 1 15
HELIX 50 50 ALA M 195 TYR M 199 5 5
HELIX 51 51 GLY M 210 LEU M 217 1 8
HELIX 52 52 SER M 218 GLY M 220 5 3
HELIX 53 53 GLU M 245 GLU M 250 1 6
HELIX 54 54 ARG M 261 ASP M 265 5 5
HELIX 55 55 TYR M 281 GLY M 285 5 5
HELIX 56 56 PRO M 286 GLY M 301 1 16
HELIX 57 57 GLY M 320 LEU M 328 1 9
HELIX 58 58 LEU M 328 VAL M 339 1 12
HELIX 59 59 ASN M 394 THR M 416 1 23
HELIX 60 60 ASN M 421 ASN M 441 1 21
HELIX 61 61 ASN M 447 CYS M 463 1 17
HELIX 62 62 THR M 468 LYS M 487 1 20
HELIX 63 63 ASN M 499 ARG M 525 1 27
HELIX 64 64 SER N 35 LEU N 47 1 13
HELIX 65 65 PHE N 80 TYR N 84 5 5
HELIX 66 66 MET N 106 ALA N 115 1 10
HELIX 67 67 THR N 126 GLY N 130 5 5
HELIX 68 68 THR N 135 LYS N 141 1 7
HELIX 69 69 TYR N 142 GLY N 147 1 6
HELIX 70 70 GLY N 152 CYS N 158 1 7
HELIX 71 71 CYS N 158 ASN N 164 1 7
HELIX 72 72 GLY N 169 ASP N 182 1 14
HELIX 73 73 LYS N 188 ASN N 196 1 9
HELIX 74 74 GLY N 200 CYS N 204 5 5
HELIX 75 75 GLY N 208 CYS N 214 1 7
HELIX 76 76 ASP N 219 LYS N 241 1 23
HELIX 77 77 THR O 14 LYS O 18 5 5
HELIX 78 78 LEU O 19 THR O 31 1 13
HELIX 79 79 THR O 31 ASN O 51 1 21
HELIX 80 80 GLY O 52 LEU O 63 1 12
HELIX 81 81 ASN O 65 ALA O 90 1 26
HELIX 82 82 PRO O 91 ALA O 94 5 4
HELIX 83 83 PRO O 105 TRP O 130 1 26
HELIX 84 84 ASP P 9 ILE P 37 1 29
HELIX 85 85 SER P 50 GLN P 59 1 10
HELIX 86 86 SER P 60 LEU P 89 1 30
HELIX 87 87 ALA P 95 ILE P 118 1 24
SHEET 1 A 4 GLN A 1 GLN A 4 0
SHEET 2 A 4 THR A 179 ARG A 184 1 O ARG A 184 N PHE A 3
SHEET 3 A 4 HIS A 166 ASN A 174 -1 N ASN A 174 O THR A 179
SHEET 4 A 4 HIS A 155 ASP A 163 -1 N PHE A 156 O MET A 173
SHEET 1 B 5 ILE A 149 ASP A 153 0
SHEET 2 B 5 ILE A 32 SER A 36 1 N LEU A 34 O PHE A 152
SHEET 3 B 5 LEU A 7 VAL A 10 1 N ILE A 9 O ALA A 33
SHEET 4 B 5 VAL A 188 MET A 190 1 O VAL A 189 N VAL A 10
SHEET 5 B 5 LEU A 374 ALA A 376 1 O PHE A 375 N VAL A 188
SHEET 1 C 3 SER A 52 ALA A 53 0
SHEET 2 C 3 THR A 124 TRP A 125 -1 O TRP A 125 N SER A 52
SHEET 3 C 3 VAL A 113 ARG A 114 -1 N ARG A 114 O THR A 124
SHEET 1 D 5 SER A 381 SER A 382 0
SHEET 2 D 5 GLY A 360 GLU A 362 1 N ILE A 361 O SER A 382
SHEET 3 D 5 LEU A 223 ARG A 224 -1 N ARG A 224 O GLY A 360
SHEET 4 D 5 LYS A 549 ARG A 555 -1 O ALA A 553 N LEU A 223
SHEET 5 D 5 THR A 561 ASP A 567 -1 O GLU A 564 N LEU A 552
SHEET 1 E 4 VAL A 229 GLY A 235 0
SHEET 2 E 4 ILE A 348 THR A 357 -1 O THR A 353 N HIS A 232
SHEET 3 E 4 GLY A 309 ASP A 315 -1 N LEU A 314 O ILE A 348
SHEET 4 E 4 ILE A 253 VAL A 255 -1 N ILE A 253 O ASP A 315
SHEET 1 F 4 VAL A 229 GLY A 235 0
SHEET 2 F 4 ILE A 348 THR A 357 -1 O THR A 353 N HIS A 232
SHEET 3 F 4 GLY A 309 ASP A 315 -1 N LEU A 314 O ILE A 348
SHEET 4 F 4 ILE A 304 THR A 306 -1 N ILE A 304 O VAL A 311
SHEET 1 G 5 HIS B 22 TYR B 30 0
SHEET 2 G 5 LYS B 4 ARG B 12 -1 N VAL B 10 O ALA B 24
SHEET 3 G 5 MET B 88 GLU B 91 1 O VAL B 90 N VAL B 11
SHEET 4 G 5 GLY B 66 VAL B 69 -1 N MET B 68 O GLU B 91
SHEET 5 G 5 VAL B 72 LEU B 75 -1 O LYS B 74 N MET B 67
SHEET 1 H 2 ILE B 98 ARG B 100 0
SHEET 2 H 2 VAL B 103 VAL B 104 -1 O VAL B 103 N ARG B 100
SHEET 1 I 2 ILE C 97 VAL C 98 0
SHEET 2 I 2 GLU C 101 LYS C 102 -1 O GLU C 101 N VAL C 98
SHEET 1 J 4 GLN M 1 GLN M 4 0
SHEET 2 J 4 THR M 179 ARG M 184 1 O GLN M 182 N GLN M 1
SHEET 3 J 4 VAL M 167 ASN M 174 -1 N ALA M 172 O VAL M 181
SHEET 4 J 4 HIS M 155 VAL M 162 -1 N LEU M 158 O VAL M 171
SHEET 1 K 5 ILE M 149 PHE M 152 0
SHEET 2 K 5 ILE M 32 ILE M 35 1 N LEU M 34 O PHE M 152
SHEET 3 K 5 LEU M 7 VAL M 10 1 N ILE M 9 O ILE M 35
SHEET 4 K 5 VAL M 188 MET M 190 1 O VAL M 189 N ALA M 8
SHEET 5 K 5 LEU M 374 ALA M 376 1 O PHE M 375 N VAL M 188
SHEET 1 L 3 SER M 52 ALA M 53 0
SHEET 2 L 3 THR M 124 TRP M 125 -1 O TRP M 125 N SER M 52
SHEET 3 L 3 VAL M 113 ARG M 114 -1 N ARG M 114 O THR M 124
SHEET 1 M 5 SER M 381 SER M 382 0
SHEET 2 M 5 GLY M 360 GLU M 362 1 N ILE M 361 O SER M 382
SHEET 3 M 5 LEU M 223 ARG M 224 -1 N ARG M 224 O GLY M 360
SHEET 4 M 5 HIS M 550 ARG M 555 -1 O ALA M 553 N LEU M 223
SHEET 5 M 5 THR M 561 SER M 566 -1 O SER M 566 N HIS M 550
SHEET 1 N 4 VAL M 229 GLY M 235 0
SHEET 2 N 4 ILE M 348 THR M 357 -1 O HIS M 355 N GLN M 230
SHEET 3 N 4 GLY M 309 ASP M 315 -1 N VAL M 312 O VAL M 350
SHEET 4 N 4 ILE M 253 VAL M 255 -1 N VAL M 255 O TYR M 313
SHEET 1 O 4 VAL M 229 GLY M 235 0
SHEET 2 O 4 ILE M 348 THR M 357 -1 O HIS M 355 N GLN M 230
SHEET 3 O 4 GLY M 309 ASP M 315 -1 N VAL M 312 O VAL M 350
SHEET 4 O 4 ILE M 304 THR M 306 -1 N THR M 306 O GLY M 309
SHEET 1 P 5 HIS N 22 TYR N 30 0
SHEET 2 P 5 LYS N 4 ARG N 12 -1 N ARG N 12 O HIS N 22
SHEET 3 P 5 MET N 88 GLU N 91 1 O VAL N 90 N GLU N 9
SHEET 4 P 5 GLY N 66 VAL N 69 -1 N MET N 68 O GLU N 91
SHEET 5 P 5 VAL N 72 LEU N 75 -1 O VAL N 72 N VAL N 69
SHEET 1 Q 2 ILE N 98 ARG N 100 0
SHEET 2 Q 2 VAL N 103 VAL N 104 -1 O VAL N 103 N ARG N 100
SHEET 1 R 2 ILE O 97 VAL O 98 0
SHEET 2 R 2 GLU O 101 LYS O 102 -1 O GLU O 101 N VAL O 98
LINK SG CYS B 214 FE4 SF4 B 246 1555 1555 1.97
LINK SG CYS N 204 FE1 F3S N 245 1555 1555 2.00
LINK SG CYS B 62 FE2 FES B 244 1555 1555 2.10
LINK SG CYS N 57 FE2 FES N 244 1555 1555 2.13
LINK SG CYS B 148 FE2 SF4 B 246 1555 1555 2.14
LINK SG CYS B 65 FE1 FES B 244 1555 1555 2.15
LINK SG CYS N 210 FE3 F3S N 245 1555 1555 2.16
LINK SG CYS N 65 FE1 FES N 244 1555 1555 2.16
LINK SG CYS B 57 FE2 FES B 244 1555 1555 2.17
LINK SG CYS N 158 FE4 F3S N 245 1555 1555 2.18
LINK SG CYS N 154 FE3 SF4 N 246 1555 1555 2.18
LINK SG CYS N 62 FE2 FES N 244 1555 1555 2.19
LINK SG CYS B 158 FE4 F3S B 245 1555 1555 2.19
LINK SG CYS B 154 FE3 SF4 B 246 1555 1555 2.21
LINK SG CYS B 77 FE1 FES B 244 1555 1555 2.35
LINK SG CYS N 77 FE1 FES N 244 1555 1555 2.38
LINK SG CYS N 148 FE2 SF4 N 246 1555 1555 2.50
LINK SG CYS N 151 FE1 SF4 N 246 1555 1555 2.65
CISPEP 1 GLY A 269 PRO A 270 0 17.64
CISPEP 2 GLY M 269 PRO M 270 0 -1.03
SITE 1 AC1 9 SER B 56 CYS B 57 ARG B 58 ALA B 60
SITE 2 AC1 9 ILE B 61 CYS B 62 GLY B 63 CYS B 65
SITE 3 AC1 9 CYS B 77
SITE 1 AC2 10 CYS B 158 GLN B 160 CYS B 204 THR B 205
SITE 2 AC2 10 PHE B 206 VAL B 207 GLY B 208 TYR B 209
SITE 3 AC2 10 CYS B 210 ILE B 224
SITE 1 AC3 6 CYS B 148 ILE B 149 CYS B 151 GLY B 152
SITE 2 AC3 6 CYS B 154 CYS B 214
SITE 1 AC4 33 GLY A 11 ALA A 12 GLY A 13 GLY A 14
SITE 2 AC4 33 ALA A 15 SER A 36 LYS A 37 VAL A 38
SITE 3 AC4 33 SER A 43 HIS A 44 THR A 45 ALA A 48
SITE 4 AC4 33 GLU A 49 GLY A 50 GLY A 51 HIS A 155
SITE 5 AC4 33 PHE A 156 VAL A 157 ALA A 191 THR A 192
SITE 6 AC4 33 GLY A 193 THR A 203 ASP A 211 HIS A 355
SITE 7 AC4 33 TYR A 356 GLY A 378 GLU A 379 ARG A 390
SITE 8 AC4 33 SER A 393 SER A 395 LEU A 396 LEU A 399
SITE 9 AC4 33 GUA A 577
SITE 1 AC5 8 SER N 56 CYS N 57 ARG N 58 CYS N 62
SITE 2 AC5 8 GLY N 63 SER N 64 CYS N 65 CYS N 77
SITE 1 AC6 10 CYS N 158 GLN N 160 CYS N 204 THR N 205
SITE 2 AC6 10 PHE N 206 VAL N 207 GLY N 208 TYR N 209
SITE 3 AC6 10 CYS N 210 ILE N 224
SITE 1 AC7 10 GLY A 50 PHE A 116 HIS A 232 THR A 244
SITE 2 AC7 10 GLU A 245 HIS A 355 ARG A 390 GLY A 392
SITE 3 AC7 10 SER A 393 FAD A 601
SITE 1 AC8 8 CYS N 148 ILE N 149 ASN N 150 CYS N 151
SITE 2 AC8 8 GLY N 152 CYS N 154 CYS N 214 VAL N 218
SITE 1 AC9 8 PHE M 116 HIS M 232 LEU M 242 THR M 244
SITE 2 AC9 8 GLU M 245 ARG M 390 SER M 393 FAD M 601
SITE 1 BC1 33 VAL M 10 GLY M 11 ALA M 12 GLY M 13
SITE 2 BC1 33 GLY M 14 ALA M 15 ILE M 35 SER M 36
SITE 3 BC1 33 LYS M 37 SER M 43 HIS M 44 THR M 45
SITE 4 BC1 33 ALA M 47 ALA M 48 GLU M 49 GLY M 50
SITE 5 BC1 33 GLY M 51 VAL M 157 ALA M 191 THR M 192
SITE 6 BC1 33 GLY M 193 THR M 203 MET M 215 HIS M 355
SITE 7 BC1 33 TYR M 356 GLY M 378 GLU M 379 SER M 393
SITE 8 BC1 33 ASN M 394 SER M 395 LEU M 396 LEU M 399
SITE 9 BC1 33 GUA M 577
CRYST1 96.678 138.016 269.558 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 0.010344 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007246 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003710 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
