HEADER OXIDOREDUCTASE 22-DEC-04 1YCF
TITLE OXIDIZED (DI-FERRIC) FPRA FROM MOORELLA THERMOACETICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE REDUCTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: DI-IRON NITRIC OXIDE REDUCTASE;
COMPND 5 SYNONYM: TYPE A FLAVOPROTEIN FPRA, FMN- PROTEIN FPRA, FLAVOPROTEIN A;
COMPND 6 EC: 1.-.-.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MOORELLA THERMOACETICA;
SOURCE 3 ORGANISM_TAXID: 1525;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SCAVENGING NITRIC OXIDE REDUCTASE, DIRON SITE STRUCTURE, DIFERROUS-
KEYWDS 2 DINITROSYL, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SILAGHI-DUMITRESCU,D.M.KURTZ,W.N.LANZILOTTA
REVDAT 6 14-FEB-24 1YCF 1 REMARK LINK
REVDAT 5 31-JAN-18 1YCF 1 REMARK
REVDAT 4 21-SEP-16 1YCF 1 REMARK VERSN
REVDAT 3 24-FEB-09 1YCF 1 VERSN
REVDAT 2 10-MAY-05 1YCF 1 JRNL
REVDAT 1 19-APR-05 1YCF 0
JRNL AUTH R.SILAGHI-DUMITRESCU,D.M.KURTZ JR,L.G.LJUNGDAHL,
JRNL AUTH 2 W.N.LANZILOTTA
JRNL TITL X-RAY CRYSTAL STRUCTURES OF MOORELLA THERMOACETICA FPRA.
JRNL TITL 2 NOVEL DIIRON SITE STRUCTURE AND MECHANISTIC INSIGHTS INTO A
JRNL TITL 3 SCAVENGING NITRIC OXIDE REDUCTASE.
JRNL REF BIOCHEMISTRY V. 44 6492 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15850383
JRNL DOI 10.1021/BI0473049
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 4240872.330
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 71781
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 SET) : 0.217
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3631
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.19
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10843
REMARK 3 BIN R VALUE (WORKING SET) : 0.3440
REMARK 3 BIN FREE R VALUE : 0.3960
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 594
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12460
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 147
REMARK 3 SOLVENT ATOMS : 61
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.94000
REMARK 3 B22 (A**2) : -6.94000
REMARK 3 B33 (A**2) : 13.87000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.53
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.44
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.64
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.890
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.33
REMARK 3 BSOL : 36.51
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : FMN.PARAM
REMARK 3 PARAMETER FILE 3 : FEO_OX.PAR
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : ION.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : FMN.TOP
REMARK 3 TOPOLOGY FILE 3 : FEO_OX.TOP
REMARK 3 TOPOLOGY FILE 4 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 5 : ION.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YCF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031373.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : BEAMLINE A1 CHESS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71781
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : 0.05000
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) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.0
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: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 3000, 200 MM ZINC ACETATE,
REMARK 280 SODIUMCACODYLATE PH 6.5, LIQUID DIFFUSION, TEMPERATURE 25K,
REMARK 280 TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 138.39900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 79.83500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 79.83500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 207.59850
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 79.83500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 79.83500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 69.19950
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 79.83500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 79.83500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 207.59850
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 79.83500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 79.83500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 69.19950
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 138.39900
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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: TWO BIOLOGICAL (FUNCTIONAL) DIMERS ARE OBSERVED IN THE
REMARK 300 ASYMMETRIC UNIT, THE FIRST IS MONOMERS A & B, THE SECOND IS
REMARK 300 MONOMERS C & D.
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: 6260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 6080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -280.0 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 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 239.50500
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 79.83500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -345.99750
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -134.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 239.50500
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 79.83500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -345.99750
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 239.50500
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 79.83500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -345.99750
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 OD2 ASP C 296 O HOH C 655 2.12
REMARK 500 OD2 ASP B 296 O HOH B 629 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG SER A 2 OD2 ASP C 275 5653 1.73
REMARK 500 O HOH B 628 O HOH D 675 5653 1.92
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 LEU D 162 CA - CB - CG ANGL. DEV. = 14.0 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 28 -92.82 -62.21
REMARK 500 THR A 35 -157.39 -156.25
REMARK 500 ASP A 44 -165.42 -129.02
REMARK 500 ASP A 51 170.22 66.23
REMARK 500 THR A 52 -130.56 -122.36
REMARK 500 PRO A 56 -5.86 -54.98
REMARK 500 ASP A 70 -74.16 -56.57
REMARK 500 LYS A 73 -87.60 -74.95
REMARK 500 LEU A 74 84.45 64.57
REMARK 500 GLU A 83 -67.57 -16.82
REMARK 500 SER A 84 -39.27 148.02
REMARK 500 TYR A 116 -56.41 -132.80
REMARK 500 SER A 117 -164.42 45.58
REMARK 500 HIS A 118 8.98 43.11
REMARK 500 TYR A 123 -158.69 -117.89
REMARK 500 THR A 124 93.62 169.56
REMARK 500 HIS A 148 -61.40 105.40
REMARK 500 ASN A 166 -119.99 70.69
REMARK 500 TRP A 232 93.63 -64.72
REMARK 500 ASP A 235 75.79 -157.97
REMARK 500 LEU A 264 -32.75 87.27
REMARK 500 SER A 311 142.74 178.76
REMARK 500 ASN A 315 58.36 33.50
REMARK 500 ASN A 316 16.62 48.66
REMARK 500 ASN A 336 70.49 46.48
REMARK 500 TRP A 347 -48.90 -163.81
REMARK 500 LYS A 363 34.94 73.85
REMARK 500 ALA A 368 71.41 -178.30
REMARK 500 GLU A 369 -85.88 -9.49
REMARK 500 TRP A 376 -75.06 74.80
REMARK 500 ALA A 398 -81.59 14.48
REMARK 500 ASP B 18 76.94 -103.14
REMARK 500 ALA B 28 -82.86 -68.82
REMARK 500 THR B 31 79.98 -113.62
REMARK 500 THR B 35 -175.73 -170.71
REMARK 500 ASP B 51 160.66 63.19
REMARK 500 THR B 52 -132.60 -112.42
REMARK 500 PRO B 56 -1.57 -51.86
REMARK 500 ASP B 70 -86.43 -32.35
REMARK 500 LYS B 73 -82.53 -72.18
REMARK 500 LEU B 74 91.26 62.82
REMARK 500 GLU B 83 -71.46 16.27
REMARK 500 SER B 84 -47.03 152.15
REMARK 500 TYR B 116 -58.22 -137.07
REMARK 500 SER B 117 -179.76 46.21
REMARK 500 HIS B 118 -5.12 59.95
REMARK 500 PHE B 121 145.90 -170.41
REMARK 500 THR B 124 89.48 176.41
REMARK 500 THR B 130 177.43 -54.91
REMARK 500 MET B 146 8.20 48.53
REMARK 500
REMARK 500 THIS ENTRY HAS 131 RAMACHANDRAN OUTLIERS.
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 ZN A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 2 OG
REMARK 620 2 SER A 2 N 81.2
REMARK 620 3 HIS C 271 NE2 119.0 97.4
REMARK 620 4 ASP C 275 OD2 44.9 112.4 82.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FEO A 500 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 81 NE2
REMARK 620 2 FEO A 500 O 131.6
REMARK 620 3 GLU A 83 OE2 110.7 71.5
REMARK 620 4 HIS A 148 NE2 80.5 137.7 71.0
REMARK 620 5 ASP A 167 OD2 86.6 107.7 157.9 99.9
REMARK 620 6 OXY A 501 O1 173.5 54.6 67.9 93.1 93.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FEO A 500 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 85 OD2
REMARK 620 2 FEO A 500 O 70.2
REMARK 620 3 HIS A 86 NE2 79.0 102.8
REMARK 620 4 ASP A 167 OD1 159.0 112.4 80.2
REMARK 620 5 HIS A 228 NE2 79.5 141.0 94.9 104.7
REMARK 620 6 OXY A 501 O1 101.8 56.1 155.6 96.2 109.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 271 NE2
REMARK 620 2 ASP A 275 OD2 97.3
REMARK 620 3 SER C 2 N 129.1 109.5
REMARK 620 4 GLU C 60 OE2 91.6 170.2 67.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FEO B 510 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 81 NE2
REMARK 620 2 FEO B 510 O 138.4
REMARK 620 3 GLU B 83 OE2 110.8 67.8
REMARK 620 4 HIS B 148 NE2 95.5 122.4 75.9
REMARK 620 5 ASP B 167 OD2 78.3 104.4 170.7 105.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FEO B 510 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 85 OD2
REMARK 620 2 FEO B 510 O 85.7
REMARK 620 3 HIS B 86 NE2 75.4 132.8
REMARK 620 4 ASP B 167 OD1 164.8 106.5 89.5
REMARK 620 5 HIS B 228 NE2 88.1 137.6 85.3 88.7
REMARK 620 6 OXY B 511 O1 115.4 56.6 167.8 79.5 89.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FEO C 520 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 81 NE2
REMARK 620 2 FEO C 520 O 108.6
REMARK 620 3 GLU C 83 OE1 98.0 67.5
REMARK 620 4 HIS C 148 NE2 104.8 138.1 83.6
REMARK 620 5 ASP C 167 OD2 93.2 103.5 167.5 99.1
REMARK 620 6 OXY C 521 O1 173.1 70.5 75.3 73.3 93.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FEO C 520 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 85 OD2
REMARK 620 2 FEO C 520 O 71.1
REMARK 620 3 HIS C 86 NE2 75.7 105.2
REMARK 620 4 ASP C 167 OD1 167.2 110.6 91.7
REMARK 620 5 HIS C 228 NE2 87.2 152.7 84.4 94.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FEO D 530 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 81 NE2
REMARK 620 2 FEO D 530 O 135.9
REMARK 620 3 GLU D 83 OE2 110.9 72.7
REMARK 620 4 HIS D 148 NE2 89.6 130.1 71.6
REMARK 620 5 ASP D 167 OD2 102.2 96.2 142.0 91.1
REMARK 620 6 OXY D 531 O1 173.4 43.2 75.5 94.2 72.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FEO D 530 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 85 OD2
REMARK 620 2 FEO D 530 O 80.5
REMARK 620 3 HIS D 86 NE2 70.1 110.3
REMARK 620 4 ASP D 167 OD2 145.2 71.3 100.8
REMARK 620 5 ASP D 167 OD1 148.9 117.7 79.7 46.8
REMARK 620 6 HIS D 228 NE2 82.4 145.2 91.8 132.2 92.0
REMARK 620 7 OXY D 531 O1 111.5 53.0 160.8 66.6 99.4 107.4
REMARK 620 8 OXY D 531 O2 129.8 68.8 157.4 57.0 81.2 100.8 19.5
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FEO A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FEO B 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY B 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FEO C 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY C 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN C 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FEO D 530
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OXY D 531
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN D 704
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E5D RELATED DB: PDB
REMARK 900 RELATED ID: 1YCG RELATED DB: PDB
REMARK 900 RELATED ID: 1YCH RELATED DB: PDB
DBREF 1YCF A 2 399 UNP Q9FDN7 FPRA_MOOTH 2 399
DBREF 1YCF B 2 399 UNP Q9FDN7 FPRA_MOOTH 2 399
DBREF 1YCF C 2 399 UNP Q9FDN7 FPRA_MOOTH 2 399
DBREF 1YCF D 2 399 UNP Q9FDN7 FPRA_MOOTH 2 399
SEQRES 1 A 398 SER GLN PRO VAL ALA ILE THR ASP GLY ILE TYR TRP VAL
SEQRES 2 A 398 GLY ALA VAL ASP TRP ASN ILE ARG TYR PHE HIS GLY PRO
SEQRES 3 A 398 ALA PHE SER THR HIS ARG GLY THR THR TYR ASN ALA TYR
SEQRES 4 A 398 LEU ILE VAL ASP ASP LYS THR ALA LEU VAL ASP THR VAL
SEQRES 5 A 398 TYR GLU PRO PHE LYS GLU GLU LEU ILE ALA LYS LEU LYS
SEQRES 6 A 398 GLN ILE LYS ASP PRO VAL LYS LEU ASP TYR LEU VAL VAL
SEQRES 7 A 398 ASN HIS THR GLU SER ASP HIS ALA GLY ALA PHE PRO ALA
SEQRES 8 A 398 ILE MET GLU LEU CYS PRO ASP ALA HIS VAL LEU CYS THR
SEQRES 9 A 398 GLN ARG ALA PHE ASP SER LEU LYS ALA HIS TYR SER HIS
SEQRES 10 A 398 ILE ASP PHE ASN TYR THR ILE VAL LYS THR GLY THR SER
SEQRES 11 A 398 VAL SER LEU GLY LYS ARG SER LEU THR PHE ILE GLU ALA
SEQRES 12 A 398 PRO MET LEU HIS TRP PRO ASP SER MET PHE THR TYR VAL
SEQRES 13 A 398 PRO GLU GLU ALA LEU LEU LEU PRO ASN ASP ALA PHE GLY
SEQRES 14 A 398 GLN HIS ILE ALA THR SER VAL ARG PHE ASP ASP GLN VAL
SEQRES 15 A 398 ASP ALA GLY LEU ILE MET ASP GLU ALA ALA LYS TYR TYR
SEQRES 16 A 398 ALA ASN ILE LEU MET PRO PHE SER ASN LEU ILE THR LYS
SEQRES 17 A 398 LYS LEU ASP GLU ILE GLN LYS ILE ASN LEU ALA ILE LYS
SEQRES 18 A 398 THR ILE ALA PRO SER HIS GLY ILE ILE TRP ARG LYS ASP
SEQRES 19 A 398 PRO GLY ARG ILE ILE GLU ALA TYR ALA ARG TRP ALA GLU
SEQRES 20 A 398 GLY GLN GLY LYS ALA LYS ALA VAL ILE ALA TYR ASP THR
SEQRES 21 A 398 MET TRP LEU SER THR GLU LYS MET ALA HIS ALA LEU MET
SEQRES 22 A 398 ASP GLY LEU VAL ALA GLY GLY CYS GLU VAL LYS LEU PHE
SEQRES 23 A 398 LYS LEU SER VAL SER ASP ARG ASN ASP VAL ILE LYS GLU
SEQRES 24 A 398 ILE LEU ASP ALA ARG ALA VAL LEU VAL GLY SER PRO THR
SEQRES 25 A 398 ILE ASN ASN ASP ILE LEU PRO VAL VAL SER PRO LEU LEU
SEQRES 26 A 398 ASP ASP LEU VAL GLY LEU ARG PRO LYS ASN LYS VAL GLY
SEQRES 27 A 398 LEU ALA PHE GLY ALA TYR GLY TRP GLY GLY GLY ALA GLN
SEQRES 28 A 398 LYS ILE LEU GLU GLU ARG LEU LYS ALA ALA LYS ILE GLU
SEQRES 29 A 398 LEU ILE ALA GLU PRO GLY PRO THR VAL GLN TRP VAL PRO
SEQRES 30 A 398 ARG GLY GLU ASP LEU GLN ARG CYS TYR GLU LEU GLY ARG
SEQRES 31 A 398 LYS ILE ALA ALA ARG ILE ALA ASP
SEQRES 1 B 398 SER GLN PRO VAL ALA ILE THR ASP GLY ILE TYR TRP VAL
SEQRES 2 B 398 GLY ALA VAL ASP TRP ASN ILE ARG TYR PHE HIS GLY PRO
SEQRES 3 B 398 ALA PHE SER THR HIS ARG GLY THR THR TYR ASN ALA TYR
SEQRES 4 B 398 LEU ILE VAL ASP ASP LYS THR ALA LEU VAL ASP THR VAL
SEQRES 5 B 398 TYR GLU PRO PHE LYS GLU GLU LEU ILE ALA LYS LEU LYS
SEQRES 6 B 398 GLN ILE LYS ASP PRO VAL LYS LEU ASP TYR LEU VAL VAL
SEQRES 7 B 398 ASN HIS THR GLU SER ASP HIS ALA GLY ALA PHE PRO ALA
SEQRES 8 B 398 ILE MET GLU LEU CYS PRO ASP ALA HIS VAL LEU CYS THR
SEQRES 9 B 398 GLN ARG ALA PHE ASP SER LEU LYS ALA HIS TYR SER HIS
SEQRES 10 B 398 ILE ASP PHE ASN TYR THR ILE VAL LYS THR GLY THR SER
SEQRES 11 B 398 VAL SER LEU GLY LYS ARG SER LEU THR PHE ILE GLU ALA
SEQRES 12 B 398 PRO MET LEU HIS TRP PRO ASP SER MET PHE THR TYR VAL
SEQRES 13 B 398 PRO GLU GLU ALA LEU LEU LEU PRO ASN ASP ALA PHE GLY
SEQRES 14 B 398 GLN HIS ILE ALA THR SER VAL ARG PHE ASP ASP GLN VAL
SEQRES 15 B 398 ASP ALA GLY LEU ILE MET ASP GLU ALA ALA LYS TYR TYR
SEQRES 16 B 398 ALA ASN ILE LEU MET PRO PHE SER ASN LEU ILE THR LYS
SEQRES 17 B 398 LYS LEU ASP GLU ILE GLN LYS ILE ASN LEU ALA ILE LYS
SEQRES 18 B 398 THR ILE ALA PRO SER HIS GLY ILE ILE TRP ARG LYS ASP
SEQRES 19 B 398 PRO GLY ARG ILE ILE GLU ALA TYR ALA ARG TRP ALA GLU
SEQRES 20 B 398 GLY GLN GLY LYS ALA LYS ALA VAL ILE ALA TYR ASP THR
SEQRES 21 B 398 MET TRP LEU SER THR GLU LYS MET ALA HIS ALA LEU MET
SEQRES 22 B 398 ASP GLY LEU VAL ALA GLY GLY CYS GLU VAL LYS LEU PHE
SEQRES 23 B 398 LYS LEU SER VAL SER ASP ARG ASN ASP VAL ILE LYS GLU
SEQRES 24 B 398 ILE LEU ASP ALA ARG ALA VAL LEU VAL GLY SER PRO THR
SEQRES 25 B 398 ILE ASN ASN ASP ILE LEU PRO VAL VAL SER PRO LEU LEU
SEQRES 26 B 398 ASP ASP LEU VAL GLY LEU ARG PRO LYS ASN LYS VAL GLY
SEQRES 27 B 398 LEU ALA PHE GLY ALA TYR GLY TRP GLY GLY GLY ALA GLN
SEQRES 28 B 398 LYS ILE LEU GLU GLU ARG LEU LYS ALA ALA LYS ILE GLU
SEQRES 29 B 398 LEU ILE ALA GLU PRO GLY PRO THR VAL GLN TRP VAL PRO
SEQRES 30 B 398 ARG GLY GLU ASP LEU GLN ARG CYS TYR GLU LEU GLY ARG
SEQRES 31 B 398 LYS ILE ALA ALA ARG ILE ALA ASP
SEQRES 1 C 398 SER GLN PRO VAL ALA ILE THR ASP GLY ILE TYR TRP VAL
SEQRES 2 C 398 GLY ALA VAL ASP TRP ASN ILE ARG TYR PHE HIS GLY PRO
SEQRES 3 C 398 ALA PHE SER THR HIS ARG GLY THR THR TYR ASN ALA TYR
SEQRES 4 C 398 LEU ILE VAL ASP ASP LYS THR ALA LEU VAL ASP THR VAL
SEQRES 5 C 398 TYR GLU PRO PHE LYS GLU GLU LEU ILE ALA LYS LEU LYS
SEQRES 6 C 398 GLN ILE LYS ASP PRO VAL LYS LEU ASP TYR LEU VAL VAL
SEQRES 7 C 398 ASN HIS THR GLU SER ASP HIS ALA GLY ALA PHE PRO ALA
SEQRES 8 C 398 ILE MET GLU LEU CYS PRO ASP ALA HIS VAL LEU CYS THR
SEQRES 9 C 398 GLN ARG ALA PHE ASP SER LEU LYS ALA HIS TYR SER HIS
SEQRES 10 C 398 ILE ASP PHE ASN TYR THR ILE VAL LYS THR GLY THR SER
SEQRES 11 C 398 VAL SER LEU GLY LYS ARG SER LEU THR PHE ILE GLU ALA
SEQRES 12 C 398 PRO MET LEU HIS TRP PRO ASP SER MET PHE THR TYR VAL
SEQRES 13 C 398 PRO GLU GLU ALA LEU LEU LEU PRO ASN ASP ALA PHE GLY
SEQRES 14 C 398 GLN HIS ILE ALA THR SER VAL ARG PHE ASP ASP GLN VAL
SEQRES 15 C 398 ASP ALA GLY LEU ILE MET ASP GLU ALA ALA LYS TYR TYR
SEQRES 16 C 398 ALA ASN ILE LEU MET PRO PHE SER ASN LEU ILE THR LYS
SEQRES 17 C 398 LYS LEU ASP GLU ILE GLN LYS ILE ASN LEU ALA ILE LYS
SEQRES 18 C 398 THR ILE ALA PRO SER HIS GLY ILE ILE TRP ARG LYS ASP
SEQRES 19 C 398 PRO GLY ARG ILE ILE GLU ALA TYR ALA ARG TRP ALA GLU
SEQRES 20 C 398 GLY GLN GLY LYS ALA LYS ALA VAL ILE ALA TYR ASP THR
SEQRES 21 C 398 MET TRP LEU SER THR GLU LYS MET ALA HIS ALA LEU MET
SEQRES 22 C 398 ASP GLY LEU VAL ALA GLY GLY CYS GLU VAL LYS LEU PHE
SEQRES 23 C 398 LYS LEU SER VAL SER ASP ARG ASN ASP VAL ILE LYS GLU
SEQRES 24 C 398 ILE LEU ASP ALA ARG ALA VAL LEU VAL GLY SER PRO THR
SEQRES 25 C 398 ILE ASN ASN ASP ILE LEU PRO VAL VAL SER PRO LEU LEU
SEQRES 26 C 398 ASP ASP LEU VAL GLY LEU ARG PRO LYS ASN LYS VAL GLY
SEQRES 27 C 398 LEU ALA PHE GLY ALA TYR GLY TRP GLY GLY GLY ALA GLN
SEQRES 28 C 398 LYS ILE LEU GLU GLU ARG LEU LYS ALA ALA LYS ILE GLU
SEQRES 29 C 398 LEU ILE ALA GLU PRO GLY PRO THR VAL GLN TRP VAL PRO
SEQRES 30 C 398 ARG GLY GLU ASP LEU GLN ARG CYS TYR GLU LEU GLY ARG
SEQRES 31 C 398 LYS ILE ALA ALA ARG ILE ALA ASP
SEQRES 1 D 398 SER GLN PRO VAL ALA ILE THR ASP GLY ILE TYR TRP VAL
SEQRES 2 D 398 GLY ALA VAL ASP TRP ASN ILE ARG TYR PHE HIS GLY PRO
SEQRES 3 D 398 ALA PHE SER THR HIS ARG GLY THR THR TYR ASN ALA TYR
SEQRES 4 D 398 LEU ILE VAL ASP ASP LYS THR ALA LEU VAL ASP THR VAL
SEQRES 5 D 398 TYR GLU PRO PHE LYS GLU GLU LEU ILE ALA LYS LEU LYS
SEQRES 6 D 398 GLN ILE LYS ASP PRO VAL LYS LEU ASP TYR LEU VAL VAL
SEQRES 7 D 398 ASN HIS THR GLU SER ASP HIS ALA GLY ALA PHE PRO ALA
SEQRES 8 D 398 ILE MET GLU LEU CYS PRO ASP ALA HIS VAL LEU CYS THR
SEQRES 9 D 398 GLN ARG ALA PHE ASP SER LEU LYS ALA HIS TYR SER HIS
SEQRES 10 D 398 ILE ASP PHE ASN TYR THR ILE VAL LYS THR GLY THR SER
SEQRES 11 D 398 VAL SER LEU GLY LYS ARG SER LEU THR PHE ILE GLU ALA
SEQRES 12 D 398 PRO MET LEU HIS TRP PRO ASP SER MET PHE THR TYR VAL
SEQRES 13 D 398 PRO GLU GLU ALA LEU LEU LEU PRO ASN ASP ALA PHE GLY
SEQRES 14 D 398 GLN HIS ILE ALA THR SER VAL ARG PHE ASP ASP GLN VAL
SEQRES 15 D 398 ASP ALA GLY LEU ILE MET ASP GLU ALA ALA LYS TYR TYR
SEQRES 16 D 398 ALA ASN ILE LEU MET PRO PHE SER ASN LEU ILE THR LYS
SEQRES 17 D 398 LYS LEU ASP GLU ILE GLN LYS ILE ASN LEU ALA ILE LYS
SEQRES 18 D 398 THR ILE ALA PRO SER HIS GLY ILE ILE TRP ARG LYS ASP
SEQRES 19 D 398 PRO GLY ARG ILE ILE GLU ALA TYR ALA ARG TRP ALA GLU
SEQRES 20 D 398 GLY GLN GLY LYS ALA LYS ALA VAL ILE ALA TYR ASP THR
SEQRES 21 D 398 MET TRP LEU SER THR GLU LYS MET ALA HIS ALA LEU MET
SEQRES 22 D 398 ASP GLY LEU VAL ALA GLY GLY CYS GLU VAL LYS LEU PHE
SEQRES 23 D 398 LYS LEU SER VAL SER ASP ARG ASN ASP VAL ILE LYS GLU
SEQRES 24 D 398 ILE LEU ASP ALA ARG ALA VAL LEU VAL GLY SER PRO THR
SEQRES 25 D 398 ILE ASN ASN ASP ILE LEU PRO VAL VAL SER PRO LEU LEU
SEQRES 26 D 398 ASP ASP LEU VAL GLY LEU ARG PRO LYS ASN LYS VAL GLY
SEQRES 27 D 398 LEU ALA PHE GLY ALA TYR GLY TRP GLY GLY GLY ALA GLN
SEQRES 28 D 398 LYS ILE LEU GLU GLU ARG LEU LYS ALA ALA LYS ILE GLU
SEQRES 29 D 398 LEU ILE ALA GLU PRO GLY PRO THR VAL GLN TRP VAL PRO
SEQRES 30 D 398 ARG GLY GLU ASP LEU GLN ARG CYS TYR GLU LEU GLY ARG
SEQRES 31 D 398 LYS ILE ALA ALA ARG ILE ALA ASP
HET ZN A 502 1
HET ZN A 503 1
HET FEO A 500 3
HET OXY A 501 2
HET FMN A 701 31
HET ZN B 512 1
HET FEO B 510 3
HET OXY B 511 2
HET FMN B 702 31
HET FEO C 520 3
HET OXY C 521 2
HET FMN C 703 31
HET FEO D 530 3
HET OXY D 531 2
HET FMN D 704 31
HETNAM ZN ZINC ION
HETNAM FEO MU-OXO-DIIRON
HETNAM OXY OXYGEN MOLECULE
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 5 ZN 3(ZN 2+)
FORMUL 7 FEO 4(FE2 O)
FORMUL 8 OXY 4(O2)
FORMUL 9 FMN 4(C17 H21 N4 O9 P)
FORMUL 20 HOH *61(H2 O)
HELIX 1 1 TYR A 54 PRO A 56 5 3
HELIX 2 2 PHE A 57 GLN A 67 1 11
HELIX 3 3 ALA A 89 CYS A 97 1 9
HELIX 4 4 THR A 105 TYR A 116 1 12
HELIX 5 5 PHE A 179 VAL A 183 5 5
HELIX 6 6 ASP A 184 LEU A 200 1 17
HELIX 7 7 PHE A 203 ILE A 217 1 15
HELIX 8 8 ASP A 235 GLY A 249 1 15
HELIX 9 9 LEU A 264 GLY A 280 1 17
HELIX 10 10 SER A 290 SER A 292 5 3
HELIX 11 11 ASP A 293 ASP A 303 1 11
HELIX 12 12 VAL A 322 ARG A 333 1 12
HELIX 13 13 GLY A 350 ALA A 362 1 13
HELIX 14 14 ARG A 379 ALA A 398 1 20
HELIX 15 15 TYR B 54 PRO B 56 5 3
HELIX 16 16 PHE B 57 GLN B 67 1 11
HELIX 17 17 ALA B 89 CYS B 97 1 9
HELIX 18 18 THR B 105 TYR B 116 1 12
HELIX 19 19 PRO B 158 GLU B 160 5 3
HELIX 20 20 PHE B 179 VAL B 183 5 5
HELIX 21 21 ASP B 184 ILE B 199 1 16
HELIX 22 22 LEU B 200 PRO B 202 5 3
HELIX 23 23 PHE B 203 ILE B 217 1 15
HELIX 24 24 PRO B 236 GLY B 249 1 14
HELIX 25 25 LEU B 264 GLY B 280 1 17
HELIX 26 26 SER B 290 SER B 292 5 3
HELIX 27 27 ASP B 293 ASP B 303 1 11
HELIX 28 28 LEU B 319 VAL B 321 5 3
HELIX 29 29 VAL B 322 ARG B 333 1 12
HELIX 30 30 GLY B 350 ALA B 362 1 13
HELIX 31 31 ARG B 379 ALA B 398 1 20
HELIX 32 32 TYR C 54 PRO C 56 5 3
HELIX 33 33 PHE C 57 GLN C 67 1 11
HELIX 34 34 ALA C 89 CYS C 97 1 9
HELIX 35 35 THR C 105 TYR C 116 1 12
HELIX 36 36 PRO C 158 GLU C 160 5 3
HELIX 37 37 PHE C 179 VAL C 183 5 5
HELIX 38 38 ASP C 184 LEU C 200 1 17
HELIX 39 39 PHE C 203 ILE C 217 1 15
HELIX 40 40 ASP C 235 GLY C 249 1 15
HELIX 41 41 LEU C 264 GLY C 280 1 17
HELIX 42 42 SER C 290 SER C 292 5 3
HELIX 43 43 ASP C 293 ASP C 303 1 11
HELIX 44 44 LEU C 319 VAL C 321 5 3
HELIX 45 45 VAL C 322 ARG C 333 1 12
HELIX 46 46 GLY C 350 ALA C 362 1 13
HELIX 47 47 ARG C 379 ALA C 398 1 20
HELIX 48 48 TYR D 54 PRO D 56 5 3
HELIX 49 49 PHE D 57 GLN D 67 1 11
HELIX 50 50 ALA D 89 CYS D 97 1 9
HELIX 51 51 THR D 105 TYR D 116 1 12
HELIX 52 52 PRO D 158 GLU D 160 5 3
HELIX 53 53 PHE D 179 VAL D 183 5 5
HELIX 54 54 ASP D 184 LEU D 200 1 17
HELIX 55 55 PHE D 203 ILE D 217 1 15
HELIX 56 56 PRO D 236 GLY D 249 1 14
HELIX 57 57 LEU D 264 GLY D 280 1 17
HELIX 58 58 SER D 290 SER D 292 5 3
HELIX 59 59 ASP D 293 ASP D 303 1 11
HELIX 60 60 LEU D 319 VAL D 321 5 3
HELIX 61 61 VAL D 322 ARG D 333 1 12
HELIX 62 62 GLY D 350 ALA D 362 1 13
HELIX 63 63 ARG D 379 ILE D 397 1 19
SHEET 1 A 6 VAL A 5 THR A 8 0
SHEET 2 A 6 ILE A 11 TRP A 13 -1 O TRP A 13 N VAL A 5
SHEET 3 A 6 TYR A 40 ILE A 42 -1 O LEU A 41 N TYR A 12
SHEET 4 A 6 ALA A 48 VAL A 50 -1 O VAL A 50 N TYR A 40
SHEET 5 A 6 TYR A 76 VAL A 78 1 O VAL A 78 N LEU A 49
SHEET 6 A 6 HIS A 101 LEU A 103 1 O LEU A 103 N LEU A 77
SHEET 1 B 2 ALA A 16 ASP A 18 0
SHEET 2 B 2 THR A 35 TYR A 37 -1 O TYR A 37 N ALA A 16
SHEET 1 C 2 TYR A 23 PHE A 24 0
SHEET 2 C 2 PHE A 29 SER A 30 -1 O PHE A 29 N PHE A 24
SHEET 1 D 5 SER A 131 SER A 133 0
SHEET 2 D 5 SER A 138 GLU A 143 -1 O LEU A 139 N VAL A 132
SHEET 3 D 5 MET A 153 VAL A 157 -1 O TYR A 156 N THR A 140
SHEET 4 D 5 LEU A 162 LEU A 164 -1 O LEU A 164 N THR A 155
SHEET 5 D 5 THR A 223 ILE A 224 1 O THR A 223 N LEU A 163
SHEET 1 E 5 GLU A 283 LYS A 288 0
SHEET 2 E 5 LYS A 252 TYR A 259 1 N ILE A 257 O PHE A 287
SHEET 3 E 5 ALA A 304 GLY A 310 1 O LEU A 308 N ALA A 258
SHEET 4 E 5 VAL A 338 TYR A 345 1 O VAL A 338 N VAL A 307
SHEET 5 E 5 GLU A 365 LEU A 366 1 O GLU A 365 N GLY A 339
SHEET 1 F 5 GLU A 283 LYS A 288 0
SHEET 2 F 5 LYS A 252 TYR A 259 1 N ILE A 257 O PHE A 287
SHEET 3 F 5 ALA A 304 GLY A 310 1 O LEU A 308 N ALA A 258
SHEET 4 F 5 VAL A 338 TYR A 345 1 O VAL A 338 N VAL A 307
SHEET 5 F 5 THR A 373 GLN A 375 1 O VAL A 374 N GLY A 343
SHEET 1 G 2 THR A 313 ILE A 314 0
SHEET 2 G 2 ASP A 317 ILE A 318 -1 O ASP A 317 N ILE A 314
SHEET 1 H 7 VAL B 5 THR B 8 0
SHEET 2 H 7 ILE B 11 TRP B 13 -1 O TRP B 13 N VAL B 5
SHEET 3 H 7 TYR B 40 ILE B 42 -1 O LEU B 41 N TYR B 12
SHEET 4 H 7 ALA B 48 VAL B 50 -1 O VAL B 50 N TYR B 40
SHEET 5 H 7 TYR B 76 VAL B 78 1 O VAL B 78 N LEU B 49
SHEET 6 H 7 HIS B 101 CYS B 104 1 O HIS B 101 N LEU B 77
SHEET 7 H 7 ASN B 122 ILE B 125 1 O ASN B 122 N VAL B 102
SHEET 1 I 2 ALA B 16 ASP B 18 0
SHEET 2 I 2 THR B 35 TYR B 37 -1 O THR B 35 N ASP B 18
SHEET 1 J 2 TYR B 23 PHE B 24 0
SHEET 2 J 2 PHE B 29 SER B 30 -1 O PHE B 29 N PHE B 24
SHEET 1 K 5 SER B 131 SER B 133 0
SHEET 2 K 5 SER B 138 GLU B 143 -1 O LEU B 139 N VAL B 132
SHEET 3 K 5 MET B 153 VAL B 157 -1 O TYR B 156 N THR B 140
SHEET 4 K 5 LEU B 162 ASN B 166 -1 O LEU B 162 N VAL B 157
SHEET 5 K 5 THR B 223 PRO B 226 1 O ALA B 225 N LEU B 163
SHEET 1 L 5 GLU B 283 LYS B 288 0
SHEET 2 L 5 LYS B 252 TYR B 259 1 N ILE B 257 O PHE B 287
SHEET 3 L 5 ALA B 304 GLY B 310 1 O LEU B 308 N VAL B 256
SHEET 4 L 5 VAL B 338 TYR B 345 1 O VAL B 338 N VAL B 307
SHEET 5 L 5 GLU B 365 LEU B 366 1 O GLU B 365 N GLY B 339
SHEET 1 M 5 GLU B 283 LYS B 288 0
SHEET 2 M 5 LYS B 252 TYR B 259 1 N ILE B 257 O PHE B 287
SHEET 3 M 5 ALA B 304 GLY B 310 1 O LEU B 308 N VAL B 256
SHEET 4 M 5 VAL B 338 TYR B 345 1 O VAL B 338 N VAL B 307
SHEET 5 M 5 THR B 373 GLN B 375 1 O VAL B 374 N GLY B 343
SHEET 1 N 7 VAL C 5 THR C 8 0
SHEET 2 N 7 ILE C 11 TRP C 13 -1 O TRP C 13 N VAL C 5
SHEET 3 N 7 TYR C 40 ILE C 42 -1 O LEU C 41 N TYR C 12
SHEET 4 N 7 ALA C 48 VAL C 50 -1 O VAL C 50 N TYR C 40
SHEET 5 N 7 TYR C 76 VAL C 78 1 O TYR C 76 N LEU C 49
SHEET 6 N 7 HIS C 101 CYS C 104 1 O HIS C 101 N LEU C 77
SHEET 7 N 7 ASN C 122 ILE C 125 1 O ASN C 122 N VAL C 102
SHEET 1 O 2 ALA C 16 ASP C 18 0
SHEET 2 O 2 THR C 35 TYR C 37 -1 O THR C 35 N ASP C 18
SHEET 1 P 2 TYR C 23 PHE C 24 0
SHEET 2 P 2 PHE C 29 SER C 30 -1 O PHE C 29 N PHE C 24
SHEET 1 Q 5 SER C 131 SER C 133 0
SHEET 2 Q 5 SER C 138 GLU C 143 -1 O LEU C 139 N VAL C 132
SHEET 3 Q 5 MET C 153 VAL C 157 -1 O TYR C 156 N THR C 140
SHEET 4 Q 5 LEU C 162 ASN C 166 -1 O LEU C 164 N THR C 155
SHEET 5 Q 5 THR C 223 PRO C 226 1 O ALA C 225 N LEU C 163
SHEET 1 R 5 GLU C 283 LYS C 288 0
SHEET 2 R 5 LYS C 252 TYR C 259 1 N ILE C 257 O PHE C 287
SHEET 3 R 5 ALA C 304 GLY C 310 1 O LEU C 308 N VAL C 256
SHEET 4 R 5 VAL C 338 TYR C 345 1 O VAL C 338 N VAL C 307
SHEET 5 R 5 GLU C 365 LEU C 366 1 O GLU C 365 N GLY C 339
SHEET 1 S 5 GLU C 283 LYS C 288 0
SHEET 2 S 5 LYS C 252 TYR C 259 1 N ILE C 257 O PHE C 287
SHEET 3 S 5 ALA C 304 GLY C 310 1 O LEU C 308 N VAL C 256
SHEET 4 S 5 VAL C 338 TYR C 345 1 O VAL C 338 N VAL C 307
SHEET 5 S 5 THR C 373 GLN C 375 1 O VAL C 374 N TYR C 345
SHEET 1 T 7 VAL D 5 THR D 8 0
SHEET 2 T 7 ILE D 11 TRP D 13 -1 O TRP D 13 N VAL D 5
SHEET 3 T 7 TYR D 40 ILE D 42 -1 O LEU D 41 N TYR D 12
SHEET 4 T 7 ALA D 48 VAL D 50 -1 O ALA D 48 N ILE D 42
SHEET 5 T 7 TYR D 76 VAL D 78 1 O TYR D 76 N LEU D 49
SHEET 6 T 7 HIS D 101 CYS D 104 1 O HIS D 101 N LEU D 77
SHEET 7 T 7 TYR D 123 ILE D 125 1 O THR D 124 N CYS D 104
SHEET 1 U 2 ALA D 16 ASP D 18 0
SHEET 2 U 2 THR D 35 TYR D 37 -1 O THR D 35 N ASP D 18
SHEET 1 V 2 TYR D 23 PHE D 24 0
SHEET 2 V 2 PHE D 29 SER D 30 -1 O PHE D 29 N PHE D 24
SHEET 1 W 5 SER D 131 SER D 133 0
SHEET 2 W 5 SER D 138 GLU D 143 -1 O LEU D 139 N VAL D 132
SHEET 3 W 5 MET D 153 VAL D 157 -1 O TYR D 156 N THR D 140
SHEET 4 W 5 LEU D 162 ASN D 166 -1 O LEU D 164 N THR D 155
SHEET 5 W 5 THR D 223 PRO D 226 1 O ALA D 225 N LEU D 163
SHEET 1 X 5 GLU D 283 LYS D 288 0
SHEET 2 X 5 LYS D 252 TYR D 259 1 N ALA D 255 O GLU D 283
SHEET 3 X 5 ALA D 304 GLY D 310 1 O ARG D 305 N LYS D 254
SHEET 4 X 5 VAL D 338 TYR D 345 1 O VAL D 338 N ARG D 305
SHEET 5 X 5 GLU D 365 LEU D 366 1 O GLU D 365 N GLY D 339
SHEET 1 Y 5 GLU D 283 LYS D 288 0
SHEET 2 Y 5 LYS D 252 TYR D 259 1 N ALA D 255 O GLU D 283
SHEET 3 Y 5 ALA D 304 GLY D 310 1 O ARG D 305 N LYS D 254
SHEET 4 Y 5 VAL D 338 TYR D 345 1 O VAL D 338 N ARG D 305
SHEET 5 Y 5 THR D 373 GLN D 375 1 O VAL D 374 N GLY D 343
LINK O FEO D 530 O1 OXY D 531 1555 1555 1.99
LINK OG SER A 2 ZN ZN A 502 1555 1555 1.80
LINK N SER A 2 ZN ZN A 502 1555 1555 2.59
LINK NE2 HIS A 81 FE1 FEO A 500 1555 1555 2.67
LINK OE2 GLU A 83 FE1 FEO A 500 1555 1555 2.35
LINK OD2 ASP A 85 FE2 FEO A 500 1555 1555 2.20
LINK NE2 HIS A 86 FE2 FEO A 500 1555 1555 2.09
LINK NE2 HIS A 148 FE1 FEO A 500 1555 1555 2.24
LINK OD2 ASP A 167 FE1 FEO A 500 1555 1555 2.04
LINK OD1 ASP A 167 FE2 FEO A 500 1555 1555 2.09
LINK NE2 HIS A 228 FE2 FEO A 500 1555 1555 1.98
LINK NE2 HIS A 271 ZN ZN A 503 1555 1555 2.22
LINK OD2 ASP A 275 ZN ZN A 503 1555 1555 2.47
LINK FE1 FEO A 500 O1 OXY A 501 1555 1555 2.99
LINK FE2 FEO A 500 O1 OXY A 501 1555 1555 2.92
LINK ZN ZN A 502 NE2 HIS C 271 1555 5653 2.60
LINK ZN ZN A 502 OD2 ASP C 275 1555 5653 2.44
LINK ZN ZN A 503 N SER C 2 1555 5653 2.00
LINK ZN ZN A 503 OE2 GLU C 60 1555 5653 2.49
LINK NE2 HIS B 81 FE1 FEO B 510 1555 1555 2.43
LINK OE2 GLU B 83 FE1 FEO B 510 1555 1555 2.75
LINK OD2 ASP B 85 FE2 FEO B 510 1555 1555 2.11
LINK NE2 HIS B 86 FE2 FEO B 510 1555 1555 2.06
LINK NE2 HIS B 148 FE1 FEO B 510 1555 1555 2.06
LINK OD1 ASP B 167 FE2 FEO B 510 1555 1555 1.96
LINK OD2 ASP B 167 FE1 FEO B 510 1555 1555 2.16
LINK NE2 HIS B 228 FE2 FEO B 510 1555 1555 2.11
LINK FE2 FEO B 510 O1 OXY B 511 1555 1555 2.57
LINK NE2 HIS C 81 FE1 FEO C 520 1555 1555 2.44
LINK OE1 GLU C 83 FE1 FEO C 520 1555 1555 1.94
LINK OD2 ASP C 85 FE2 FEO C 520 1555 1555 2.12
LINK NE2 HIS C 86 FE2 FEO C 520 1555 1555 2.28
LINK NE2 HIS C 148 FE1 FEO C 520 1555 1555 2.34
LINK OD2 ASP C 167 FE1 FEO C 520 1555 1555 2.03
LINK OD1 ASP C 167 FE2 FEO C 520 1555 1555 2.05
LINK NE2 HIS C 228 FE2 FEO C 520 1555 1555 2.01
LINK FE1 FEO C 520 O1 OXY C 521 1555 1555 3.06
LINK NE2 HIS D 81 FE1 FEO D 530 1555 1555 2.37
LINK OE2 GLU D 83 FE1 FEO D 530 1555 1555 1.91
LINK OD2 ASP D 85 FE2 FEO D 530 1555 1555 2.23
LINK NE2 HIS D 86 FE2 FEO D 530 1555 1555 2.21
LINK NE2 HIS D 148 FE1 FEO D 530 1555 1555 2.23
LINK OD2 ASP D 167 FE1 FEO D 530 1555 1555 2.05
LINK OD2 ASP D 167 FE2 FEO D 530 1555 1555 3.01
LINK OD1 ASP D 167 FE2 FEO D 530 1555 1555 2.17
LINK NE2 HIS D 228 FE2 FEO D 530 1555 1555 2.05
LINK FE1 FEO D 530 O1 OXY D 531 1555 1555 2.91
LINK FE2 FEO D 530 O1 OXY D 531 1555 1555 2.37
LINK FE2 FEO D 530 O2 OXY D 531 1555 1555 3.13
SITE 1 AC1 4 SER A 2 GLU A 60 HIS C 271 ASP C 275
SITE 1 AC2 4 HIS A 271 ASP A 275 SER C 2 GLU C 60
SITE 1 AC3 2 VAL B 17 HIS D 271
SITE 1 AC4 8 HIS A 81 GLU A 83 ASP A 85 HIS A 86
SITE 2 AC4 8 HIS A 148 ASP A 167 HIS A 228 OXY A 501
SITE 1 AC5 6 PHE A 24 HIS A 25 GLU A 83 TYR A 195
SITE 2 AC5 6 ILE A 199 FEO A 500
SITE 1 AC6 21 THR A 261 MET A 262 TRP A 263 LEU A 264
SITE 2 AC6 21 SER A 265 THR A 266 PRO A 312 THR A 313
SITE 3 AC6 21 ILE A 314 ASN A 315 ASN A 316 TYR A 345
SITE 4 AC6 21 GLY A 346 TRP A 347 GLY A 348 GLY A 349
SITE 5 AC6 21 TRP A 376 HOH A 623 HIS B 25 GLU B 83
SITE 6 AC6 21 TRP B 149
SITE 1 AC7 9 HIS B 25 HIS B 81 GLU B 83 ASP B 85
SITE 2 AC7 9 HIS B 86 HIS B 148 ASP B 167 HIS B 228
SITE 3 AC7 9 OXY B 511
SITE 1 AC8 6 PHE B 24 HIS B 25 ASP B 167 TYR B 195
SITE 2 AC8 6 HIS B 228 FEO B 510
SITE 1 AC9 20 HIS A 25 GLU A 83 TRP A 149 THR B 261
SITE 2 AC9 20 MET B 262 TRP B 263 LEU B 264 SER B 265
SITE 3 AC9 20 THR B 266 PRO B 312 THR B 313 ILE B 314
SITE 4 AC9 20 ASN B 315 ASN B 316 TYR B 345 GLY B 346
SITE 5 AC9 20 TRP B 347 GLY B 348 GLY B 349 TRP B 376
SITE 1 BC1 8 HIS C 81 GLU C 83 ASP C 85 HIS C 86
SITE 2 BC1 8 HIS C 148 ASP C 167 HIS C 228 OXY C 521
SITE 1 BC2 8 PHE C 24 HIS C 25 GLU C 83 HIS C 148
SITE 2 BC2 8 ASP C 167 TYR C 195 ILE C 199 FEO C 520
SITE 1 BC3 22 THR C 261 MET C 262 TRP C 263 LEU C 264
SITE 2 BC3 22 SER C 265 THR C 266 PRO C 312 THR C 313
SITE 3 BC3 22 ILE C 314 ASN C 315 ASN C 316 ALA C 344
SITE 4 BC3 22 TYR C 345 GLY C 346 TRP C 347 GLY C 348
SITE 5 BC3 22 GLY C 349 TRP C 376 HOH C 650 HIS D 25
SITE 6 BC3 22 GLU D 83 TRP D 149
SITE 1 BC4 8 HIS D 81 GLU D 83 ASP D 85 HIS D 86
SITE 2 BC4 8 HIS D 148 ASP D 167 HIS D 228 OXY D 531
SITE 1 BC5 8 PHE D 24 HIS D 25 GLU D 83 HIS D 148
SITE 2 BC5 8 ASP D 167 TYR D 195 HIS D 228 FEO D 530
SITE 1 BC6 20 HIS C 25 GLU C 83 TRP C 149 THR D 261
SITE 2 BC6 20 MET D 262 TRP D 263 LEU D 264 SER D 265
SITE 3 BC6 20 THR D 266 PRO D 312 THR D 313 ASN D 315
SITE 4 BC6 20 ASN D 316 ALA D 344 TYR D 345 GLY D 346
SITE 5 BC6 20 TRP D 347 GLY D 348 GLY D 349 TRP D 376
CRYST1 159.670 159.670 276.798 90.00 90.00 90.00 P 43 21 2 32
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 0.006263 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006263 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003613 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
