HEADER OXIDOREDUCTASE 11-SEP-08 3EGW
TITLE THE CRYSTAL STRUCTURE OF THE NARGHI MUTANT NARH - C16A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RESPIRATORY NITRATE REDUCTASE 1 ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CHAIN A, NARG;
COMPND 5 SYNONYM: NITRATE REDUCTASE A SUBUNIT ALPHA, QUINOL-NITRATE
COMPND 6 OXIDOREDUCTASE ALPHA SUBUNIT;
COMPND 7 EC: 1.7.99.4;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: RESPIRATORY NITRATE REDUCTASE 1 BETA CHAIN;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: CHAIN B, NARH;
COMPND 13 SYNONYM: NITRATE REDUCTASE A SUBUNIT BETA, QUINOL-NITRATE
COMPND 14 OXIDOREDUCTASE SUBUNIT BETA;
COMPND 15 EC: 1.7.99.4;
COMPND 16 ENGINEERED: YES;
COMPND 17 MUTATION: YES;
COMPND 18 MOL_ID: 3;
COMPND 19 MOLECULE: RESPIRATORY NITRATE REDUCTASE 1 GAMMA CHAIN;
COMPND 20 CHAIN: C;
COMPND 21 FRAGMENT: CHAIN C, NARI;
COMPND 22 SYNONYM: NITRATE REDUCTASE A SUBUNIT GAMMA, QUINOL-NITRATE
COMPND 23 OXIDOREDUCTASE GAMMA SUBUNIT, CYTOCHROME B-NR;
COMPND 24 EC: 1.7.99.4;
COMPND 25 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 GENE: NARG, BISD, NARC, B1224, JW1215;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: LCB79;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PVA700;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 12 ORGANISM_TAXID: 83333;
SOURCE 13 GENE: NARH, B1225, JW1216;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: LCB79;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PVA700;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 21 ORGANISM_TAXID: 83333;
SOURCE 22 GENE: NARI, CHLI, B1227, JW1218;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 25 EXPRESSION_SYSTEM_STRAIN: LCB79;
SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 27 EXPRESSION_SYSTEM_PLASMID: PVA700
KEYWDS OXIDOREDUCTASE, NITRATE REDUCTION, ELECTRON TRANSFER, MEMBRANE
KEYWDS 2 PROTEIN, 4FE-4S, CELL MEMBRANE, ELECTRON TRANSPORT, IRON, IRON-
KEYWDS 3 SULFUR, MEMBRANE, METAL-BINDING, MOLYBDENUM, NITRATE ASSIMILATION,
KEYWDS 4 TRANSPORT, 3FE-4S, CELL INNER MEMBRANE, FORMYLATION, HEME,
KEYWDS 5 TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.G.BERTERO,R.A.ROTHERY,J.H.WEINER,N.C.J.STRYNADKA
REVDAT 4 30-AUG-23 3EGW 1 REMARK
REVDAT 3 20-OCT-21 3EGW 1 REMARK SEQADV LINK
REVDAT 2 25-OCT-17 3EGW 1 REMARK
REVDAT 1 02-MAR-10 3EGW 0
JRNL AUTH A.PARKIN,C.F.BLANFORD,R.A.ROTHERY,R.MACEY,M.BERTERO,
JRNL AUTH 2 N.C.J.STRYNADKA,F.A.ARMSTRONG,J.H.WEINER
JRNL TITL WHEN WIDTH IS MORE IMPORTANT THAN HEIGHT: BARRIERS TO
JRNL TITL 2 ELECTRON TRANSFER IN E.COLI NITRATE REDUCTASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 5799808.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 195208
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) : 0.175
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9737
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 25997
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE : 0.2520
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1322
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.007
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15711
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 267
REMARK 3 SOLVENT ATOMS : 1526
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.94000
REMARK 3 B22 (A**2) : 8.37000
REMARK 3 B33 (A**2) : -7.42000
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) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.18
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 : 0.36
REMARK 3 BSOL : 50.68
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 : COFACT.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : SF.PAR
REMARK 3 PARAMETER FILE 5 : HEME.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : COFACT.TOP
REMARK 3 TOPOLOGY FILE 3 : LIPID.TOP
REMARK 3 TOPOLOGY FILE 4 : SF.TOP
REMARK 3 TOPOLOGY FILE 5 : HEME.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3EGW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-SEP-08.
REMARK 100 THE DEPOSITION ID IS D_1000049307.
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 : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 195446
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.7710
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.25200
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: CNS
REMARK 200 STARTING MODEL: 1Q16
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3000, SODIUM ACETATE, POTASSIUM
REMARK 280 CHLORIDE, EDTA, PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.73750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.73750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 76.99750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 120.84200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 76.99750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 120.84200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.73750
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 76.99750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 120.84200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.73750
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 76.99750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 120.84200
REMARK 290 SMTRY3 8 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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 49470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 109350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -188.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 -1.000000 0.000000 0.000000 -307.99000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -69.73750
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 61280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 OD1 ASP A 222 MO 6MO A 1247 1.99
REMARK 500 OD1 ASP A 222 O HOH A 1836 2.16
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 O HOH A 1886 O HOH A 1886 3354 1.99
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 ALA A 501 N - CA - CB ANGL. DEV. = 8.7 DEGREES
REMARK 500 TYR A 502 C - N - CA ANGL. DEV. = 30.4 DEGREES
REMARK 500 TYR A 502 CB - CG - CD2 ANGL. DEV. = 3.6 DEGREES
REMARK 500 TYR A 502 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ALA A1164 C - N - CA ANGL. DEV. = 29.1 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 TYR A 9 -86.65 -28.85
REMARK 500 ASN A 26 71.83 -118.18
REMARK 500 THR A 54 -4.06 82.52
REMARK 500 ARG A 81 153.39 -48.24
REMARK 500 ARG A 90 -158.24 59.19
REMARK 500 SER A 160 -152.29 -117.72
REMARK 500 ILE A 191 74.61 33.26
REMARK 500 SER A 195 80.24 -170.24
REMARK 500 PHE A 216 -36.89 -145.07
REMARK 500 THR A 235 124.25 -175.77
REMARK 500 ARG A 260 32.03 -142.20
REMARK 500 LEU A 319 -68.07 -98.40
REMARK 500 VAL A 361 -73.04 -40.81
REMARK 500 ALA A 363 29.70 49.63
REMARK 500 SER A 422 23.40 -161.21
REMARK 500 LEU A 447 -101.03 -136.94
REMARK 500 ALA A 501 80.21 -64.60
REMARK 500 TYR A 502 68.10 -162.77
REMARK 500 ARG A 535 46.21 -93.33
REMARK 500 HIS A 549 40.65 -99.44
REMARK 500 VAL A 578 -105.26 -141.75
REMARK 500 ALA A 658 112.83 -172.26
REMARK 500 PRO A 665 -9.72 -58.15
REMARK 500 SER A 719 -75.70 -134.12
REMARK 500 ASP A 796 -176.61 -172.46
REMARK 500 TRP A 817 -127.65 47.48
REMARK 500 LEU A 860 59.82 -91.04
REMARK 500 ALA A 861 -79.29 -80.19
REMARK 500 ASP A 865 -169.97 -162.78
REMARK 500 LYS A 880 -54.31 -140.09
REMARK 500 TYR A 932 177.37 72.69
REMARK 500 HIS A1098 -128.20 64.62
REMARK 500 TYR A1101 -10.53 77.68
REMARK 500 ASN A1139 -166.13 -161.43
REMARK 500 GLU A1166 -162.18 43.02
REMARK 500 ALA A1202 -113.62 53.09
REMARK 500 LEU A1204 73.08 -100.97
REMARK 500 ASN A1217 -6.37 -157.23
REMARK 500 LYS A1228 -68.92 -107.26
REMARK 500 ALA B 90 97.15 -164.04
REMARK 500 ASN B 91 107.35 -58.67
REMARK 500 TYR B 100 -80.63 -95.44
REMARK 500 TYR B 101 152.59 171.15
REMARK 500 ASP B 158 123.00 -39.03
REMARK 500 LEU B 350 66.27 60.08
REMARK 500 ASP B 367 -169.39 -125.65
REMARK 500 ALA B 448 -63.59 -90.34
REMARK 500 ASP B 500 31.69 -98.18
REMARK 500 ASP C 44 93.55 -162.60
REMARK 500 PRO C 210 56.42 -64.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 501 TYR A 502 74.55
REMARK 500 HIS A 1163 ALA A 1164 -107.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA A 501 16.27
REMARK 500 HIS A1163 -12.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 3PH B 806
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 A1248 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 49 ND1
REMARK 620 2 SF4 A1248 S1 114.2
REMARK 620 3 SF4 A1248 S2 114.2 104.9
REMARK 620 4 SF4 A1248 S4 113.1 104.8 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1248 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 53 SG
REMARK 620 2 SF4 A1248 S1 117.1
REMARK 620 3 SF4 A1248 S2 111.0 105.2
REMARK 620 4 SF4 A1248 S3 111.0 105.8 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1248 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 57 SG
REMARK 620 2 SF4 A1248 S2 110.0
REMARK 620 3 SF4 A1248 S3 115.2 106.0
REMARK 620 4 SF4 A1248 S4 115.7 104.5 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1248 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 92 SG
REMARK 620 2 SF4 A1248 S1 114.4
REMARK 620 3 SF4 A1248 S3 112.3 105.2
REMARK 620 4 SF4 A1248 S4 115.2 104.6 104.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 6MO A1247 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MD1 A1245 S12
REMARK 620 2 MD1 A1245 S13 76.5
REMARK 620 3 MGD A1246 S12 129.9 80.4
REMARK 620 4 MGD A1246 S13 72.5 116.2 79.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B 802 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 19 SG
REMARK 620 2 F3S B 802 S1 121.4
REMARK 620 3 F3S B 802 S3 100.9 102.2
REMARK 620 4 F3S B 802 S4 115.6 108.7 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B 802 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 22 SG
REMARK 620 2 F3S B 802 S2 115.1
REMARK 620 3 F3S B 802 S3 109.5 105.3
REMARK 620 4 F3S B 802 S4 111.9 107.9 106.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 803 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 26 SG
REMARK 620 2 SF4 B 803 S1 113.2
REMARK 620 3 SF4 B 803 S2 108.6 103.6
REMARK 620 4 SF4 B 803 S3 120.4 105.6 103.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 804 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 184 SG
REMARK 620 2 SF4 B 804 S2 119.8
REMARK 620 3 SF4 B 804 S3 117.3 104.4
REMARK 620 4 SF4 B 804 S4 104.9 103.2 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 804 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 187 SG
REMARK 620 2 SF4 B 804 S1 120.8
REMARK 620 3 SF4 B 804 S3 111.4 102.9
REMARK 620 4 SF4 B 804 S4 112.7 102.7 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 804 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 192 SG
REMARK 620 2 SF4 B 804 S1 114.2
REMARK 620 3 SF4 B 804 S2 109.7 107.6
REMARK 620 4 SF4 B 804 S4 116.6 104.0 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B 805 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 196 SG
REMARK 620 2 F3S B 805 S1 114.5
REMARK 620 3 F3S B 805 S2 113.8 106.4
REMARK 620 4 F3S B 805 S3 109.0 107.8 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B 805 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 217 SG
REMARK 620 2 F3S B 805 S2 113.6
REMARK 620 3 F3S B 805 S3 116.7 104.9
REMARK 620 4 F3S B 805 S4 108.0 110.5 102.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B 805 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 223 SG
REMARK 620 2 F3S B 805 S1 109.4
REMARK 620 3 F3S B 805 S3 110.9 107.6
REMARK 620 4 F3S B 805 S4 117.1 108.5 102.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 804 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 227 SG
REMARK 620 2 SF4 B 804 S1 115.0
REMARK 620 3 SF4 B 804 S2 108.2 107.8
REMARK 620 4 SF4 B 804 S3 116.7 104.2 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 803 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 244 SG
REMARK 620 2 SF4 B 803 S1 112.3
REMARK 620 3 SF4 B 803 S3 117.2 105.7
REMARK 620 4 SF4 B 803 S4 111.5 105.2 103.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 803 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 247 SG
REMARK 620 2 SF4 B 803 S2 99.1
REMARK 620 3 SF4 B 803 S3 122.3 103.9
REMARK 620 4 SF4 B 803 S4 118.8 106.1 104.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 803 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 259 SG
REMARK 620 2 SF4 B 803 S1 121.5
REMARK 620 3 SF4 B 803 S2 110.6 104.0
REMARK 620 4 SF4 B 803 S4 108.4 105.0 106.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B 802 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 263 SG
REMARK 620 2 F3S B 802 S1 112.1
REMARK 620 3 F3S B 802 S2 111.3 109.8
REMARK 620 4 F3S B 802 S3 115.0 103.1 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 806 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 56 NE2
REMARK 620 2 HEM C 806 NA 89.0
REMARK 620 3 HEM C 806 NB 90.3 89.5
REMARK 620 4 HEM C 806 NC 91.5 179.2 89.9
REMARK 620 5 HEM C 806 ND 90.0 92.4 178.1 88.2
REMARK 620 6 HIS C 205 NE2 179.3 91.1 90.4 88.5 89.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 807 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 66 NE2
REMARK 620 2 HEM C 807 NA 89.4
REMARK 620 3 HEM C 807 NB 91.3 89.3
REMARK 620 4 HEM C 807 NC 90.8 179.4 90.2
REMARK 620 5 HEM C 807 ND 88.3 92.6 178.1 87.9
REMARK 620 6 HIS C 187 NE2 179.1 90.6 89.6 89.2 90.9
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 MD1 A 1245
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD A 1246
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6MO A 1247
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 1248
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3PH B 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGA C 309
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Q16 RELATED DB: PDB
REMARK 900 NARGHI - NATIVE STRUCTURE
REMARK 900 RELATED ID: 1Y4Z RELATED DB: PDB
REMARK 900 NARGHI - NARH MUTANT C26A
DBREF 3EGW A 1 1244 UNP P09152 NARG_ECOLI 2 1245
DBREF 3EGW B 1 509 UNP P11349 NARH_ECOLI 1 509
DBREF 3EGW C 1 225 UNP P11350 NARI_ECOLI 1 225
SEQADV 3EGW ALA A 10 UNP P09152 PHE 11 CONFLICT
SEQADV 3EGW ALA A 362 UNP P09152 ASP 363 CONFLICT
SEQADV 3EGW ALA B 16 UNP P11349 CYS 16 ENGINEERED MUTATION
SEQADV 3EGW ALA C 77 UNP P11350 TYR 77 CONFLICT
SEQADV 3EGW ALA C 78 UNP P11350 GLU 78 CONFLICT
SEQRES 1 A 1244 SER LYS PHE LEU ASP ARG PHE ARG TYR ALA LYS GLN LYS
SEQRES 2 A 1244 GLY GLU THR PHE ALA ASP GLY HIS GLY GLN LEU LEU ASN
SEQRES 3 A 1244 THR ASN ARG ASP TRP GLU ASP GLY TYR ARG GLN ARG TRP
SEQRES 4 A 1244 GLN HIS ASP LYS ILE VAL ARG SER THR HIS GLY VAL ASN
SEQRES 5 A 1244 CYS THR GLY SER CYS SER TRP LYS ILE TYR VAL LYS ASN
SEQRES 6 A 1244 GLY LEU VAL THR TRP GLU THR GLN GLN THR ASP TYR PRO
SEQRES 7 A 1244 ARG THR ARG PRO ASP LEU PRO ASN HIS GLU PRO ARG GLY
SEQRES 8 A 1244 CYS PRO ARG GLY ALA SER TYR SER TRP TYR LEU TYR SER
SEQRES 9 A 1244 ALA ASN ARG LEU LYS TYR PRO MET MET ARG LYS ARG LEU
SEQRES 10 A 1244 MET LYS MET TRP ARG GLU ALA LYS ALA LEU HIS SER ASP
SEQRES 11 A 1244 PRO VAL GLU ALA TRP ALA SER ILE ILE GLU ASP ALA ASP
SEQRES 12 A 1244 LYS ALA LYS SER PHE LYS GLN ALA ARG GLY ARG GLY GLY
SEQRES 13 A 1244 PHE VAL ARG SER SER TRP GLN GLU VAL ASN GLU LEU ILE
SEQRES 14 A 1244 ALA ALA SER ASN VAL TYR THR ILE LYS ASN TYR GLY PRO
SEQRES 15 A 1244 ASP ARG VAL ALA GLY PHE SER PRO ILE PRO ALA MET SER
SEQRES 16 A 1244 MET VAL SER TYR ALA SER GLY ALA ARG TYR LEU SER LEU
SEQRES 17 A 1244 ILE GLY GLY THR CYS LEU SER PHE TYR ASP TRP TYR CYS
SEQRES 18 A 1244 ASP LEU PRO PRO ALA SER PRO GLN THR TRP GLY GLU GLN
SEQRES 19 A 1244 THR ASP VAL PRO GLU SER ALA ASP TRP TYR ASN SER SER
SEQRES 20 A 1244 TYR ILE ILE ALA TRP GLY SER ASN VAL PRO GLN THR ARG
SEQRES 21 A 1244 THR PRO ASP ALA HIS PHE PHE THR GLU VAL ARG TYR LYS
SEQRES 22 A 1244 GLY THR LYS THR VAL ALA VAL THR PRO ASP TYR ALA GLU
SEQRES 23 A 1244 ILE ALA LYS LEU CYS ASP LEU TRP LEU ALA PRO LYS GLN
SEQRES 24 A 1244 GLY THR ASP ALA ALA MET ALA LEU ALA MET GLY HIS VAL
SEQRES 25 A 1244 MET LEU ARG GLU PHE HIS LEU ASP ASN PRO SER GLN TYR
SEQRES 26 A 1244 PHE THR ASP TYR VAL ARG ARG TYR THR ASP MET PRO MET
SEQRES 27 A 1244 LEU VAL MET LEU GLU GLU ARG ASP GLY TYR TYR ALA ALA
SEQRES 28 A 1244 GLY ARG MET LEU ARG ALA ALA ASP LEU VAL ALA ALA LEU
SEQRES 29 A 1244 GLY GLN GLU ASN ASN PRO GLU TRP LYS THR VAL ALA PHE
SEQRES 30 A 1244 ASN THR ASN GLY GLU MET VAL ALA PRO ASN GLY SER ILE
SEQRES 31 A 1244 GLY PHE ARG TRP GLY GLU LYS GLY LYS TRP ASN LEU GLU
SEQRES 32 A 1244 GLN ARG ASP GLY LYS THR GLY GLU GLU THR GLU LEU GLN
SEQRES 33 A 1244 LEU SER LEU LEU GLY SER GLN ASP GLU ILE ALA GLU VAL
SEQRES 34 A 1244 GLY PHE PRO TYR PHE GLY GLY ASP GLY THR GLU HIS PHE
SEQRES 35 A 1244 ASN LYS VAL GLU LEU GLU ASN VAL LEU LEU HIS LYS LEU
SEQRES 36 A 1244 PRO VAL LYS ARG LEU GLN LEU ALA ASP GLY SER THR ALA
SEQRES 37 A 1244 LEU VAL THR THR VAL TYR ASP LEU THR LEU ALA ASN TYR
SEQRES 38 A 1244 GLY LEU GLU ARG GLY LEU ASN ASP VAL ASN CYS ALA THR
SEQRES 39 A 1244 SER TYR ASP ASP VAL LYS ALA TYR THR PRO ALA TRP ALA
SEQRES 40 A 1244 GLU GLN ILE THR GLY VAL SER ARG SER GLN ILE ILE ARG
SEQRES 41 A 1244 ILE ALA ARG GLU PHE ALA ASP ASN ALA ASP LYS THR HIS
SEQRES 42 A 1244 GLY ARG SER MET ILE ILE VAL GLY ALA GLY LEU ASN HIS
SEQRES 43 A 1244 TRP TYR HIS LEU ASP MET ASN TYR ARG GLY LEU ILE ASN
SEQRES 44 A 1244 MET LEU ILE PHE CYS GLY CYS VAL GLY GLN SER GLY GLY
SEQRES 45 A 1244 GLY TRP ALA HIS TYR VAL GLY GLN GLU LYS LEU ARG PRO
SEQRES 46 A 1244 GLN THR GLY TRP GLN PRO LEU ALA PHE ALA LEU ASP TRP
SEQRES 47 A 1244 GLN ARG PRO ALA ARG HIS MET ASN SER THR SER TYR PHE
SEQRES 48 A 1244 TYR ASN HIS SER SER GLN TRP ARG TYR GLU THR VAL THR
SEQRES 49 A 1244 ALA GLU GLU LEU LEU SER PRO MET ALA ASP LYS SER ARG
SEQRES 50 A 1244 TYR THR GLY HIS LEU ILE ASP PHE ASN VAL ARG ALA GLU
SEQRES 51 A 1244 ARG MET GLY TRP LEU PRO SER ALA PRO GLN LEU GLY THR
SEQRES 52 A 1244 ASN PRO LEU THR ILE ALA GLY GLU ALA GLU LYS ALA GLY
SEQRES 53 A 1244 MET ASN PRO VAL ASP TYR THR VAL LYS SER LEU LYS GLU
SEQRES 54 A 1244 GLY SER ILE ARG PHE ALA ALA GLU GLN PRO GLU ASN GLY
SEQRES 55 A 1244 LYS ASN HIS PRO ARG ASN LEU PHE ILE TRP ARG SER ASN
SEQRES 56 A 1244 LEU LEU GLY SER SER GLY LYS GLY HIS GLU PHE MET LEU
SEQRES 57 A 1244 LYS TYR LEU LEU GLY THR GLU HIS GLY ILE GLN GLY LYS
SEQRES 58 A 1244 ASP LEU GLY GLN GLN GLY GLY VAL LYS PRO GLU GLU VAL
SEQRES 59 A 1244 ASP TRP GLN ASP ASN GLY LEU GLU GLY LYS LEU ASP LEU
SEQRES 60 A 1244 VAL VAL THR LEU ASP PHE ARG LEU SER SER THR CYS LEU
SEQRES 61 A 1244 TYR SER ASP ILE ILE LEU PRO THR ALA THR TRP TYR GLU
SEQRES 62 A 1244 LYS ASP ASP MET ASN THR SER ASP MET HIS PRO PHE ILE
SEQRES 63 A 1244 HIS PRO LEU SER ALA ALA VAL ASP PRO ALA TRP GLU ALA
SEQRES 64 A 1244 LYS SER ASP TRP GLU ILE TYR LYS ALA ILE ALA LYS LYS
SEQRES 65 A 1244 PHE SER GLU VAL CYS VAL GLY HIS LEU GLY LYS GLU THR
SEQRES 66 A 1244 ASP ILE VAL THR LEU PRO ILE GLN HIS ASP SER ALA ALA
SEQRES 67 A 1244 GLU LEU ALA GLN PRO LEU ASP VAL LYS ASP TRP LYS LYS
SEQRES 68 A 1244 GLY GLU CYS ASP LEU ILE PRO GLY LYS THR ALA PRO HIS
SEQRES 69 A 1244 ILE MET VAL VAL GLU ARG ASP TYR PRO ALA THR TYR GLU
SEQRES 70 A 1244 ARG PHE THR SER ILE GLY PRO LEU MET GLU LYS ILE GLY
SEQRES 71 A 1244 ASN GLY GLY LYS GLY ILE ALA TRP ASN THR GLN SER GLU
SEQRES 72 A 1244 MET ASP LEU LEU ARG LYS LEU ASN TYR THR LYS ALA GLU
SEQRES 73 A 1244 GLY PRO ALA LYS GLY GLN PRO MET LEU ASN THR ALA ILE
SEQRES 74 A 1244 ASP ALA ALA GLU MET ILE LEU THR LEU ALA PRO GLU THR
SEQRES 75 A 1244 ASN GLY GLN VAL ALA VAL LYS ALA TRP ALA ALA LEU SER
SEQRES 76 A 1244 GLU PHE THR GLY ARG ASP HIS THR HIS LEU ALA LEU ASN
SEQRES 77 A 1244 LYS GLU ASP GLU LYS ILE ARG PHE ARG ASP ILE GLN ALA
SEQRES 78 A 1244 GLN PRO ARG LYS ILE ILE SER SER PRO THR TRP SER GLY
SEQRES 79 A 1244 LEU GLU ASP GLU HIS VAL SER TYR ASN ALA GLY TYR THR
SEQRES 80 A 1244 ASN VAL HIS GLU LEU ILE PRO TRP ARG THR LEU SER GLY
SEQRES 81 A 1244 ARG GLN GLN LEU TYR GLN ASP HIS GLN TRP MET ARG ASP
SEQRES 82 A 1244 PHE GLY GLU SER LEU LEU VAL TYR ARG PRO PRO ILE ASP
SEQRES 83 A 1244 THR ARG SER VAL LYS GLU VAL ILE GLY GLN LYS SER ASN
SEQRES 84 A 1244 GLY ASN GLN GLU LYS ALA LEU ASN PHE LEU THR PRO HIS
SEQRES 85 A 1244 GLN LYS TRP GLY ILE HIS SER THR TYR SER ASP ASN LEU
SEQRES 86 A 1244 LEU MET LEU THR LEU GLY ARG GLY GLY PRO VAL VAL TRP
SEQRES 87 A 1244 LEU SER GLU ALA ASP ALA LYS ASP LEU GLY ILE ALA ASP
SEQRES 88 A 1244 ASN ASP TRP ILE GLU VAL PHE ASN SER ASN GLY ALA LEU
SEQRES 89 A 1244 THR ALA ARG ALA VAL VAL SER GLN ARG VAL PRO ALA GLY
SEQRES 90 A 1244 MET THR MET MET TYR HIS ALA GLN GLU ARG ILE VAL ASN
SEQRES 91 A 1244 LEU PRO GLY SER GLU ILE THR GLN GLN ARG GLY GLY ILE
SEQRES 92 A 1244 HIS ASN SER VAL THR ARG ILE THR PRO LYS PRO THR HIS
SEQRES 93 A 1244 MET ILE GLY GLY TYR ALA HIS LEU ALA TYR GLY PHE ASN
SEQRES 94 A 1244 TYR TYR GLY THR VAL GLY SER ASN ARG ASP GLU PHE VAL
SEQRES 95 A 1244 VAL VAL ARG LYS MET LYS ASN ILE ASP TRP LEU ASP GLY
SEQRES 96 A 1244 GLU GLY ASN ASP GLN VAL GLN GLU SER
SEQRES 1 B 509 MET LYS ILE ARG SER GLN VAL GLY MET VAL LEU ASN LEU
SEQRES 2 B 509 ASP LYS ALA ILE GLY CYS HIS THR CYS SER VAL THR CYS
SEQRES 3 B 509 LYS ASN VAL TRP THR SER ARG GLU GLY VAL GLU TYR ALA
SEQRES 4 B 509 TRP PHE ASN ASN VAL GLU THR LYS PRO GLY GLN GLY PHE
SEQRES 5 B 509 PRO THR ASP TRP GLU ASN GLN GLU LYS TYR LYS GLY GLY
SEQRES 6 B 509 TRP ILE ARG LYS ILE ASN GLY LYS LEU GLN PRO ARG MET
SEQRES 7 B 509 GLY ASN ARG ALA MET LEU LEU GLY LYS ILE PHE ALA ASN
SEQRES 8 B 509 PRO HIS LEU PRO GLY ILE ASP ASP TYR TYR GLU PRO PHE
SEQRES 9 B 509 ASP PHE ASP TYR GLN ASN LEU HIS THR ALA PRO GLU GLY
SEQRES 10 B 509 SER LYS SER GLN PRO ILE ALA ARG PRO ARG SER LEU ILE
SEQRES 11 B 509 THR GLY GLU ARG MET ALA LYS ILE GLU LYS GLY PRO ASN
SEQRES 12 B 509 TRP GLU ASP ASP LEU GLY GLY GLU PHE ASP LYS LEU ALA
SEQRES 13 B 509 LYS ASP LYS ASN PHE ASP ASN ILE GLN LYS ALA MET TYR
SEQRES 14 B 509 SER GLN PHE GLU ASN THR PHE MET MET TYR LEU PRO ARG
SEQRES 15 B 509 LEU CYS GLU HIS CYS LEU ASN PRO ALA CYS VAL ALA THR
SEQRES 16 B 509 CYS PRO SER GLY ALA ILE TYR LYS ARG GLU GLU ASP GLY
SEQRES 17 B 509 ILE VAL LEU ILE ASP GLN ASP LYS CYS ARG GLY TRP ARG
SEQRES 18 B 509 MET CYS ILE THR GLY CYS PRO TYR LYS LYS ILE TYR PHE
SEQRES 19 B 509 ASN TRP LYS SER GLY LYS SER GLU LYS CYS ILE PHE CYS
SEQRES 20 B 509 TYR PRO ARG ILE GLU ALA GLY GLN PRO THR VAL CYS SER
SEQRES 21 B 509 GLU THR CYS VAL GLY ARG ILE ARG TYR LEU GLY VAL LEU
SEQRES 22 B 509 LEU TYR ASP ALA ASP ALA ILE GLU ARG ALA ALA SER THR
SEQRES 23 B 509 GLU ASN GLU LYS ASP LEU TYR GLN ARG GLN LEU ASP VAL
SEQRES 24 B 509 PHE LEU ASP PRO ASN ASP PRO LYS VAL ILE GLU GLN ALA
SEQRES 25 B 509 ILE LYS ASP GLY ILE PRO LEU SER VAL ILE GLU ALA ALA
SEQRES 26 B 509 GLN GLN SER PRO VAL TYR LYS MET ALA MET GLU TRP LYS
SEQRES 27 B 509 LEU ALA LEU PRO LEU HIS PRO GLU TYR ARG THR LEU PRO
SEQRES 28 B 509 MET VAL TRP TYR VAL PRO PRO LEU SER PRO ILE GLN SER
SEQRES 29 B 509 ALA ALA ASP ALA GLY GLU LEU GLY SER ASN GLY ILE LEU
SEQRES 30 B 509 PRO ASP VAL GLU SER LEU ARG ILE PRO VAL GLN TYR LEU
SEQRES 31 B 509 ALA ASN LEU LEU THR ALA GLY ASP THR LYS PRO VAL LEU
SEQRES 32 B 509 ARG ALA LEU LYS ARG MET LEU ALA MET ARG HIS TYR LYS
SEQRES 33 B 509 ARG ALA GLU THR VAL ASP GLY LYS VAL ASP THR ARG ALA
SEQRES 34 B 509 LEU GLU GLU VAL GLY LEU THR GLU ALA GLN ALA GLN GLU
SEQRES 35 B 509 MET TYR ARG TYR LEU ALA ILE ALA ASN TYR GLU ASP ARG
SEQRES 36 B 509 PHE VAL VAL PRO SER SER HIS ARG GLU LEU ALA ARG GLU
SEQRES 37 B 509 ALA PHE PRO GLU LYS ASN GLY CYS GLY PHE THR PHE GLY
SEQRES 38 B 509 ASP GLY CYS HIS GLY SER ASP THR LYS PHE ASN LEU PHE
SEQRES 39 B 509 ASN SER ARG ARG ILE ASP ALA ILE ASP VAL THR SER LYS
SEQRES 40 B 509 THR GLU
SEQRES 1 C 225 FME GLN PHE LEU ASN MET PHE PHE PHE ASP ILE TYR PRO
SEQRES 2 C 225 TYR ILE ALA GLY ALA VAL PHE LEU ILE GLY SER TRP LEU
SEQRES 3 C 225 ARG TYR ASP TYR GLY GLN TYR THR TRP ARG ALA ALA SER
SEQRES 4 C 225 SER GLN MET LEU ASP ARG LYS GLY MET ASN LEU ALA SER
SEQRES 5 C 225 ASN LEU PHE HIS ILE GLY ILE LEU GLY ILE PHE VAL GLY
SEQRES 6 C 225 HIS PHE PHE GLY MET LEU THR PRO HIS TRP MET ALA ALA
SEQRES 7 C 225 ALA TRP LEU PRO ILE GLU VAL LYS GLN LYS MET ALA MET
SEQRES 8 C 225 PHE ALA GLY GLY ALA SER GLY VAL LEU CYS LEU ILE GLY
SEQRES 9 C 225 GLY VAL LEU LEU LEU LYS ARG ARG LEU PHE SER PRO ARG
SEQRES 10 C 225 VAL ARG ALA THR THR THR GLY ALA ASP ILE LEU ILE LEU
SEQRES 11 C 225 SER LEU LEU VAL ILE GLN CYS ALA LEU GLY LEU LEU THR
SEQRES 12 C 225 ILE PRO PHE SER ALA GLN HIS MET ASP GLY SER GLU MET
SEQRES 13 C 225 MET LYS LEU VAL GLY TRP ALA GLN SER VAL VAL THR PHE
SEQRES 14 C 225 HIS GLY GLY ALA SER GLN HIS LEU ASP GLY VAL ALA PHE
SEQRES 15 C 225 ILE PHE ARG LEU HIS LEU VAL LEU GLY MET THR LEU PHE
SEQRES 16 C 225 LEU LEU PHE PRO PHE SER ARG LEU ILE HIS ILE TRP SER
SEQRES 17 C 225 VAL PRO VAL GLU TYR LEU THR ARG LYS TYR GLN LEU VAL
SEQRES 18 C 225 ARG ALA ARG HIS
MODRES 3EGW FME C 1 MET N-FORMYLMETHIONINE
HET FME C 1 10
HET MD1 A1245 47
HET MGD A1246 47
HET 6MO A1247 1
HET SF4 A1248 8
HET F3S B 802 7
HET SF4 B 803 8
HET SF4 B 804 8
HET F3S B 805 7
HET 3PH B 806 18
HET HEM C 806 43
HET HEM C 807 43
HET AGA C 309 30
HETNAM FME N-FORMYLMETHIONINE
HETNAM MD1 PHOSPHORIC ACID 4-(2-AMINO-4-OXO-3,4,5,6,-TETRAHYDRO-
HETNAM 2 MD1 PTERIDIN-6-YL)-2-HYDROXY-3,4-DIMERCAPTO-BUT-3-EN-YL
HETNAM 3 MD1 ESTER GUANYLATE ESTER
HETNAM MGD 2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-
HETNAM 2 MGD OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE
HETNAM 3 MGD DINUCLEOTIDE
HETNAM 6MO MOLYBDENUM(VI) ION
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM F3S FE3-S4 CLUSTER
HETNAM 3PH 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM AGA (1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)
HETNAM 2 AGA PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL
HETNAM 3 AGA OCTANOATE
HETSYN MGD MOLYBDOPTERIN GUANOSINE DINUCLEOTIDE
HETSYN 3PH PHOSPHATIDIC ACID
HETSYN HEM HEME
HETSYN AGA PHOSPHATIDYL GLYCEROL
FORMUL 3 FME C6 H11 N O3 S
FORMUL 4 MD1 C20 H26 N10 O13 P2 S2
FORMUL 5 MGD C20 H26 N10 O13 P2 S2
FORMUL 6 6MO MO 6+
FORMUL 7 SF4 3(FE4 S4)
FORMUL 8 F3S 2(FE3 S4)
FORMUL 12 3PH C39 H77 O8 P
FORMUL 13 HEM 2(C34 H32 FE N4 O4)
FORMUL 15 AGA C19 H36 O10 P 1-
FORMUL 16 HOH *1526(H2 O)
HELIX 1 1 SER A 1 ARG A 6 1 6
HELIX 2 2 PHE A 7 LYS A 11 5 5
HELIX 3 3 ARG A 29 TRP A 31 5 3
HELIX 4 4 GLU A 32 GLN A 40 1 9
HELIX 5 5 CYS A 92 SER A 97 1 6
HELIX 6 6 TYR A 98 SER A 104 5 7
HELIX 7 7 LYS A 115 ALA A 126 1 12
HELIX 8 8 ASP A 130 GLU A 140 1 11
HELIX 9 9 ASP A 141 GLN A 150 1 10
HELIX 10 10 SER A 161 TYR A 180 1 20
HELIX 11 11 GLY A 181 ASP A 183 5 3
HELIX 12 12 ILE A 191 MET A 194 5 4
HELIX 13 13 SER A 195 GLY A 210 1 16
HELIX 14 14 PRO A 225 GLY A 232 1 8
HELIX 15 15 GLU A 239 SER A 246 5 8
HELIX 16 16 ASN A 255 ARG A 260 1 6
HELIX 17 17 ASP A 263 ARG A 271 1 9
HELIX 18 18 TYR A 272 GLY A 274 5 3
HELIX 19 19 ALA A 285 CYS A 291 1 7
HELIX 20 20 THR A 301 HIS A 318 1 18
HELIX 21 21 SER A 323 THR A 334 1 12
HELIX 22 22 ARG A 356 LEU A 360 5 5
HELIX 23 23 ALA A 362 GLN A 366 5 5
HELIX 24 24 ASN A 369 LYS A 373 5 5
HELIX 25 25 SER A 389 ARG A 393 5 5
HELIX 26 26 VAL A 473 TYR A 481 1 9
HELIX 27 27 THR A 503 GLY A 512 1 10
HELIX 28 28 SER A 514 HIS A 533 1 20
HELIX 29 29 GLY A 541 HIS A 546 1 6
HELIX 30 30 HIS A 549 CYS A 564 1 16
HELIX 31 31 PRO A 585 PHE A 594 1 10
HELIX 32 32 ASN A 606 SER A 615 1 10
HELIX 33 33 SER A 616 GLU A 621 5 6
HELIX 34 34 ALA A 625 LEU A 629 5 5
HELIX 35 35 ASP A 634 TYR A 638 5 5
HELIX 36 36 HIS A 641 MET A 652 1 12
HELIX 37 37 THR A 667 ALA A 675 1 9
HELIX 38 38 ASN A 678 GLY A 690 1 13
HELIX 39 39 PHE A 694 GLN A 698 5 5
HELIX 40 40 GLY A 723 LEU A 731 1 9
HELIX 41 41 ASP A 742 GLY A 747 1 6
HELIX 42 42 SER A 776 TYR A 781 1 6
HELIX 43 43 SER A 821 CYS A 837 1 17
HELIX 44 44 SER A 856 LEU A 860 5 5
HELIX 45 45 ASP A 868 GLY A 872 5 5
HELIX 46 46 ALA A 894 THR A 900 1 7
HELIX 47 47 PRO A 904 ILE A 909 1 6
HELIX 48 48 THR A 920 TYR A 932 1 13
HELIX 49 49 THR A 947 ALA A 959 1 13
HELIX 50 50 ASN A 963 GLY A 979 1 17
HELIX 51 51 HIS A 982 GLU A 990 5 9
HELIX 52 52 ARG A 995 GLN A 1002 1 8
HELIX 53 53 GLY A 1025 LEU A 1032 1 8
HELIX 54 54 HIS A 1048 PHE A 1054 1 7
HELIX 55 55 ASN A 1104 GLY A 1111 1 8
HELIX 56 56 GLU A 1121 GLY A 1128 1 8
HELIX 57 57 ILE A 1183 VAL A 1187 5 5
HELIX 58 58 LYS A 1193 MET A 1197 5 5
HELIX 59 59 HIS B 20 THR B 31 1 12
HELIX 60 60 ASN B 58 LYS B 63 1 6
HELIX 61 61 ASN B 80 GLY B 86 1 7
HELIX 62 62 GLY B 96 TYR B 101 1 6
HELIX 63 63 TYR B 108 ALA B 114 1 7
HELIX 64 64 GLU B 151 ALA B 156 1 6
HELIX 65 65 LYS B 157 ASP B 162 5 6
HELIX 66 66 LYS B 166 THR B 175 5 10
HELIX 67 67 PRO B 190 THR B 195 1 6
HELIX 68 68 MET B 222 CYS B 227 1 6
HELIX 69 69 CYS B 247 GLU B 252 1 6
HELIX 70 70 THR B 257 THR B 262 1 6
HELIX 71 71 ALA B 279 SER B 285 1 7
HELIX 72 72 ASN B 288 LYS B 290 5 3
HELIX 73 73 ASP B 291 ASP B 298 1 8
HELIX 74 74 ASP B 305 ASP B 315 1 11
HELIX 75 75 PRO B 318 GLN B 326 1 9
HELIX 76 76 SER B 328 MET B 335 1 8
HELIX 77 77 HIS B 344 ARG B 348 5 5
HELIX 78 78 ASP B 379 LEU B 383 5 5
HELIX 79 79 PRO B 386 THR B 395 1 10
HELIX 80 80 ASP B 398 VAL B 421 1 24
HELIX 81 81 THR B 427 VAL B 433 1 7
HELIX 82 82 THR B 436 ALA B 448 1 13
HELIX 83 83 ASN B 451 ARG B 455 1 5
HELIX 84 84 GLU B 468 CYS B 476 1 9
HELIX 85 85 FME C 1 ILE C 11 1 11
HELIX 86 86 ILE C 11 GLY C 31 1 21
HELIX 87 87 GLN C 32 TRP C 35 5 4
HELIX 88 88 GLY C 47 THR C 72 1 26
HELIX 89 89 PRO C 82 SER C 115 1 34
HELIX 90 90 SER C 115 THR C 122 1 8
HELIX 91 91 THR C 123 ALA C 148 1 26
HELIX 92 92 GLN C 149 MET C 151 5 3
HELIX 93 93 GLY C 153 THR C 168 1 16
HELIX 94 94 GLY C 172 ASP C 178 5 7
HELIX 95 95 ALA C 181 PHE C 198 1 18
HELIX 96 96 PRO C 199 VAL C 209 5 11
HELIX 97 97 PRO C 210 ARG C 216 5 7
SHEET 1 A 5 LYS A 13 PHE A 17 0
SHEET 2 A 5 GLY A 22 LEU A 25 -1 O LEU A 24 N GLY A 14
SHEET 3 A 5 GLN C 219 ARG C 222 1 O VAL C 221 N LEU A 25
SHEET 4 A 5 ILE B 201 ARG B 204 1 N LYS B 203 O LEU C 220
SHEET 5 A 5 VAL B 210 ILE B 212 -1 O LEU B 211 N TYR B 202
SHEET 1 B 3 LYS A 43 SER A 47 0
SHEET 2 B 3 TRP A 59 LYS A 64 -1 O TRP A 59 N SER A 47
SHEET 3 B 3 LEU A 67 GLN A 73 -1 O THR A 72 N LYS A 60
SHEET 1 C 8 PHE A 157 ARG A 159 0
SHEET 2 C 8 MET A 112 ARG A 114 -1 N MET A 113 O VAL A 158
SHEET 3 C 8 ILE A 784 PRO A 787 -1 O ILE A 785 N MET A 112
SHEET 4 C 8 LEU A 767 ASP A 772 1 N THR A 770 O LEU A 786
SHEET 5 C 8 ASN A 708 TRP A 712 1 N ILE A 711 O VAL A 769
SHEET 6 C 8 VAL A 185 PHE A 188 1 N ALA A 186 O ASN A 708
SHEET 7 C 8 THR A 212 LEU A 214 1 O THR A 212 N VAL A 185
SHEET 8 C 8 HIS A 604 MET A 605 1 O MET A 605 N CYS A 213
SHEET 1 D 5 LEU A 293 LEU A 295 0
SHEET 2 D 5 LYS A 276 VAL A 280 1 N ALA A 279 O LEU A 293
SHEET 3 D 5 TYR A 248 TRP A 252 1 N ALA A 251 O VAL A 278
SHEET 4 D 5 SER A 536 VAL A 540 1 O MET A 537 N TYR A 248
SHEET 5 D 5 GLY A 573 HIS A 576 1 O ALA A 575 N ILE A 538
SHEET 1 E 6 LEU A 339 GLU A 344 0
SHEET 2 E 6 TYR A 349 MET A 354 -1 O ALA A 350 N GLU A 343
SHEET 3 E 6 GLU A 425 PRO A 432 1 O GLY A 430 N TYR A 349
SHEET 4 E 6 VAL A 450 GLN A 461 -1 O LEU A 451 N PHE A 431
SHEET 5 E 6 THR A 467 THR A 472 -1 O ALA A 468 N LEU A 460
SHEET 6 E 6 LEU A 339 GLU A 344 -1 N VAL A 340 O THR A 471
SHEET 1 F 2 ALA A 376 PHE A 377 0
SHEET 2 F 2 MET A 383 VAL A 384 -1 O VAL A 384 N ALA A 376
SHEET 1 G 3 ASP A 796 ASN A 798 0
SHEET 2 G 3 PHE A 805 LEU A 809 -1 O LEU A 809 N ASP A 796
SHEET 3 G 3 ARG A1004 LYS A1005 -1 O ARG A1004 N ILE A 806
SHEET 1 H 2 LYS A 843 LEU A 850 0
SHEET 2 H 2 HIS A 884 ASP A 891 -1 O HIS A 884 N LEU A 850
SHEET 1 I 2 ASN A 911 GLY A 913 0
SHEET 2 I 2 ILE A 916 TRP A 918 -1 O TRP A 918 N ASN A 911
SHEET 1 J 7 LYS A1084 LEU A1089 0
SHEET 2 J 7 MET A1158 MET A1160 1 O THR A1159 N LEU A1089
SHEET 3 J 7 VAL A1116 SER A1120 -1 N TRP A1118 O MET A1160
SHEET 4 J 7 GLY A1142 SER A1151 1 O VAL A1149 N LEU A1119
SHEET 5 J 7 TRP A1134 ASN A1139 -1 N ILE A1135 O ALA A1146
SHEET 6 J 7 PHE A1221 LYS A1226 -1 O VAL A1223 N PHE A1138
SHEET 7 J 7 LYS A1084 LEU A1089 -1 N LEU A1086 O VAL A1222
SHEET 1 K 2 ASN A1229 ILE A1230 0
SHEET 2 K 2 GLN A1240 VAL A1241 -1 O GLN A1240 N ILE A1230
SHEET 1 L 5 PHE B 300 LEU B 301 0
SHEET 2 L 5 ARG B 268 ASP B 276 -1 N LEU B 274 O LEU B 301
SHEET 3 L 5 ILE B 3 ASN B 12 -1 N VAL B 10 O TYR B 269
SHEET 4 L 5 VAL B 353 VAL B 356 1 O TRP B 354 N MET B 9
SHEET 5 L 5 LEU B 341 PRO B 342 -1 N LEU B 341 O TYR B 355
SHEET 1 M 3 PHE B 300 LEU B 301 0
SHEET 2 M 3 ARG B 268 ASP B 276 -1 N LEU B 274 O LEU B 301
SHEET 3 M 3 PHE B 456 VAL B 457 1 O VAL B 457 N LEU B 270
SHEET 1 N 2 ASN B 43 LYS B 47 0
SHEET 2 N 2 MET B 178 ARG B 182 -1 O LEU B 180 N GLU B 45
SHEET 1 O 2 TRP B 66 ARG B 68 0
SHEET 2 O 2 LEU B 74 PRO B 76 -1 O GLN B 75 N ILE B 67
SHEET 1 P 2 PHE B 104 PHE B 106 0
SHEET 2 P 2 PRO B 126 SER B 128 -1 O ARG B 127 N ASP B 105
SHEET 1 Q 2 ILE B 232 PHE B 234 0
SHEET 2 Q 2 SER B 241 LYS B 243 -1 O GLU B 242 N TYR B 233
LINK C FME C 1 N GLN C 2 1555 1555 1.35
LINK ND1 HIS A 49 FE3 SF4 A1248 1555 1555 2.00
LINK SG CYS A 53 FE4 SF4 A1248 1555 1555 2.26
LINK SG CYS A 57 FE1 SF4 A1248 1555 1555 2.29
LINK SG CYS A 92 FE2 SF4 A1248 1555 1555 2.28
LINK S12 MD1 A1245 MO 6MO A1247 1555 1555 2.41
LINK S13 MD1 A1245 MO 6MO A1247 1555 1555 2.39
LINK S12 MGD A1246 MO 6MO A1247 1555 1555 2.43
LINK S13 MGD A1246 MO 6MO A1247 1555 1555 2.41
LINK SG CYS B 19 FE3 F3S B 802 1555 1555 2.33
LINK SG CYS B 22 FE4 F3S B 802 1555 1555 2.30
LINK SG CYS B 26 FE4 SF4 B 803 1555 1555 2.30
LINK SG CYS B 184 FE1 SF4 B 804 1555 1555 2.30
LINK SG CYS B 187 FE2 SF4 B 804 1555 1555 2.33
LINK SG CYS B 192 FE3 SF4 B 804 1555 1555 2.29
LINK SG CYS B 196 FE1 F3S B 805 1555 1555 2.30
LINK SG CYS B 217 FE4 F3S B 805 1555 1555 2.31
LINK SG CYS B 223 FE3 F3S B 805 1555 1555 2.29
LINK SG CYS B 227 FE4 SF4 B 804 1555 1555 2.29
LINK SG CYS B 244 FE2 SF4 B 803 1555 1555 2.30
LINK SG CYS B 247 FE1 SF4 B 803 1555 1555 2.32
LINK SG CYS B 259 FE3 SF4 B 803 1555 1555 2.28
LINK SG CYS B 263 FE1 F3S B 802 1555 1555 2.32
LINK NE2 HIS C 56 FE HEM C 806 1555 1555 2.01
LINK NE2 HIS C 66 FE HEM C 807 1555 1555 2.01
LINK NE2 HIS C 187 FE HEM C 807 1555 1555 2.00
LINK NE2 HIS C 205 FE HEM C 806 1555 1555 2.02
CISPEP 1 GLU A 88 PRO A 89 0 0.44
CISPEP 2 ARG A 600 PRO A 601 0 0.04
CISPEP 3 ALA A 658 PRO A 659 0 -0.58
CISPEP 4 LYS B 47 PRO B 48 0 0.06
CISPEP 5 PHE B 52 PRO B 53 0 -0.50
SITE 1 AC1 37 GLY A 50 ASN A 52 PRO A 190 TYR A 220
SITE 2 AC1 37 ASP A 222 HIS A 546 ARG A 713 SER A 714
SITE 3 AC1 37 ASN A 715 SER A 719 SER A 720 LYS A 722
SITE 4 AC1 37 LEU A 771 ASP A 772 PHE A 773 ARG A 774
SITE 5 AC1 37 THR A 788 TRP A 791 LYS A 794 ASP A 822
SITE 6 AC1 37 THR A1090 HIS A1092 ILE A1097 HIS A1098
SITE 7 AC1 37 SER A1099 THR A1100 HIS A1163 ASN A1185
SITE 8 AC1 37 ASN A1217 ARG A1218 MGD A1246 6MO A1247
SITE 9 AC1 37 HOH A1264 HOH A1294 HOH A1311 HOH A1354
SITE 10 AC1 37 HOH A1666
SITE 1 AC2 39 ASN A 52 CYS A 53 ARG A 94 ASP A 222
SITE 2 AC2 39 TRP A 252 GLY A 253 SER A 254 ASN A 255
SITE 3 AC2 39 GLN A 258 THR A 259 VAL A 280 PRO A 282
SITE 4 AC2 39 ASP A 283 ALA A 285 GLN A 299 GLY A 300
SITE 5 AC2 39 ASP A 302 GLY A 541 ALA A 542 GLY A 543
SITE 6 AC2 39 LEU A 544 TRP A 547 TYR A 577 VAL A 578
SITE 7 AC2 39 GLY A 579 LEU A1089 PRO A1091 HIS A1092
SITE 8 AC2 39 GLN A1093 GLY A1096 ILE A1097 HIS A1098
SITE 9 AC2 39 ARG A1218 MD1 A1245 6MO A1247 HOH A1272
SITE 10 AC2 39 HOH A1289 HOH A1303 HOH A1307
SITE 1 AC3 4 ASP A 222 MD1 A1245 MGD A1246 HOH A1836
SITE 1 AC4 11 HIS A 49 VAL A 51 CYS A 53 GLY A 55
SITE 2 AC4 11 SER A 56 CYS A 57 TRP A 59 GLY A 91
SITE 3 AC4 11 CYS A 92 GLY A 95 TYR A1101
SITE 1 AC5 10 ILE B 17 CYS B 19 HIS B 20 CYS B 22
SITE 2 AC5 10 CYS B 263 VAL B 264 GLY B 265 ILE B 267
SITE 3 AC5 10 ARG B 268 HOH B 890
SITE 1 AC6 9 CYS B 26 TRP B 30 ASN B 42 CYS B 244
SITE 2 AC6 9 ILE B 245 PHE B 246 CYS B 247 THR B 257
SITE 3 AC6 9 CYS B 259
SITE 1 AC7 9 CYS B 184 GLU B 185 CYS B 187 ALA B 191
SITE 2 AC7 9 CYS B 192 CYS B 227 TYR B 229 ILE B 232
SITE 3 AC7 9 LYS B 243
SITE 1 AC8 12 CYS B 196 PRO B 197 SER B 198 ILE B 201
SITE 2 AC8 12 CYS B 217 ARG B 218 GLY B 219 TRP B 220
SITE 3 AC8 12 ARG B 221 MET B 222 CYS B 223 SER B 241
SITE 1 AC9 5 HOH B 916 HOH B 937 HOH B1104 GLY C 124
SITE 2 AC9 5 ALA C 125
SITE 1 BC1 19 ILE B 88 PHE B 89 TRP B 220 ARG B 221
SITE 2 BC1 19 SER C 39 SER C 40 GLN C 41 MET C 48
SITE 3 BC1 19 PHE C 55 HIS C 56 ARG C 112 LEU C 130
SITE 4 BC1 19 LEU C 133 ARG C 202 HIS C 205 ILE C 206
SITE 5 BC1 19 HOH C 810 HOH C 812 HOH C 820
SITE 1 BC2 20 ILE C 59 ILE C 62 HIS C 66 ALA C 90
SITE 2 BC2 20 GLY C 94 LEU C 133 GLN C 136 CYS C 137
SITE 3 BC2 20 GLY C 140 MET C 156 LEU C 159 HIS C 187
SITE 4 BC2 20 LEU C 188 GLY C 191 MET C 192 PHE C 195
SITE 5 BC2 20 HOH C 824 HOH C 850 HOH C 864 HOH C 873
SITE 1 BC3 12 PHE A 3 ARG A 6 SER B 198 ARG B 218
SITE 2 BC3 12 SER C 24 TRP C 25 TYR C 28 TRP C 207
SITE 3 BC3 12 SER C 208 VAL C 211 GLU C 212 HOH C 867
CRYST1 153.995 241.684 139.475 90.00 90.00 90.00 C 2 2 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 0.006494 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004138 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007170 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
