HEADER OXIDOREDUCTASE 23-OCT-13 4NBD
TITLE CARBAZOLE-BOUND OXYGENASE WITH PHE275 REPLACED BY TRP AND FERREDOXIN
TITLE 2 COMPLEX OF CARBAZOLE 1,9A-DIOXYGENASE (FORM2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TERMINAL OXYGENASE COMPONENT OF CARBAZOLE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: TERMINAL OXYGENASE COMPONENT OF CARBAZOLE 1,9A-DIOXYGENASE;
COMPND 5 EC: 1.14.12.22;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: FERREDOXIN CARAC;
COMPND 10 CHAIN: D, E;
COMPND 11 SYNONYM: FERREDOXIN OF CARBAZOLE 1,9A-DIOXYGENASE, CARDO;
COMPND 12 EC: 1.14.12.22;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: JANTHINOBACTERIUM;
SOURCE 3 ORGANISM_TAXID: 213804;
SOURCE 4 STRAIN: J3;
SOURCE 5 GENE: CARAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEF275W;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: PSEUDOMONAS RESINOVORANS;
SOURCE 13 ORGANISM_TAXID: 53412;
SOURCE 14 STRAIN: CA10;
SOURCE 15 GENE: CARAC;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PECAC1
KEYWDS RIESKE NON-HEME IRON OXYGENASE, CARBAZOLE 1, 9A-DIOXYGENASE,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ASHIKAWA,Y.USAMI,K.INOUE,H.NOJIRI
REVDAT 3 08-NOV-23 4NBD 1 REMARK
REVDAT 2 24-AUG-22 4NBD 1 JRNL REMARK SEQADV LINK
REVDAT 1 26-MAR-14 4NBD 0
JRNL AUTH K.INOUE,Y.USAMI,Y.ASHIKAWA,H.NOGUCHI,T.UMEDA,
JRNL AUTH 2 A.YAMAGAMI-ASHIKAWA,T.HORISAKI,H.UCHIMURA,T.TERADA,
JRNL AUTH 3 S.NAKAMURA,K.SHIMIZU,H.HABE,H.YAMANE,Z.FUJIMOTO,H.NOJIRI
JRNL TITL STRUCTURAL BASIS OF THE DIVERGENT OXYGENATION REACTIONS
JRNL TITL 2 CATALYZED BY THE RIESKE NONHEME IRON OXYGENASE CARBAZOLE
JRNL TITL 3 1,9A-DIOXYGENASE.
JRNL REF APPL.ENVIRON.MICROBIOL. V. 80 2821 2014
JRNL REFN ESSN 1098-5336
JRNL PMID 24584240
JRNL DOI 10.1128/AEM.04000-13
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1721748.370
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 128027
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) : 0.205
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6398
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 19849
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1030
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.009
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10868
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 897
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.51000
REMARK 3 B22 (A**2) : 0.45000
REMARK 3 B33 (A**2) : 0.06000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.97000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.19
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) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.770
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 : 0.35
REMARK 3 BSOL : 49.45
REMARK 3
REMARK 3 NCS MODEL : NONE
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : CIS_PEPTIDE.PARAM
REMARK 3 PARAMETER FILE 5 : CAR_PRODRG.PARAM
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : CAR_PRODRG.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4NBD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000082988.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-DEC-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NUMERICAL LINK TYPE SI(111)
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR,
REMARK 200 DIRECT WATER COOLING
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 128061
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
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: MOLREP
REMARK 200 STARTING MODEL: 2DE5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M AMMONIUM ACETATE, 12.5% PEG 3350,
REMARK 280 0.05M MES, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 44.10150
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLU A 386
REMARK 465 HIS A 387
REMARK 465 HIS A 388
REMARK 465 HIS A 389
REMARK 465 HIS A 390
REMARK 465 HIS A 391
REMARK 465 HIS A 392
REMARK 465 MET B 1
REMARK 465 GLU B 386
REMARK 465 HIS B 387
REMARK 465 HIS B 388
REMARK 465 HIS B 389
REMARK 465 HIS B 390
REMARK 465 HIS B 391
REMARK 465 HIS B 392
REMARK 465 MET C 1
REMARK 465 HIS C 390
REMARK 465 HIS C 391
REMARK 465 HIS C 392
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 GLN D 3
REMARK 465 LYS D 107
REMARK 465 LEU D 108
REMARK 465 GLU D 109
REMARK 465 HIS D 110
REMARK 465 HIS D 111
REMARK 465 HIS D 112
REMARK 465 HIS D 113
REMARK 465 HIS D 114
REMARK 465 HIS D 115
REMARK 465 MET E 1
REMARK 465 ASN E 2
REMARK 465 HIS E 110
REMARK 465 HIS E 111
REMARK 465 HIS E 112
REMARK 465 HIS E 113
REMARK 465 HIS E 114
REMARK 465 HIS E 115
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 TRP A 15 49.70 -158.94
REMARK 500 ALA A 21 48.55 -76.37
REMARK 500 ASN A 27 37.62 71.83
REMARK 500 ARG A 68 109.19 -161.38
REMARK 500 HIS A 71 -80.82 -68.06
REMARK 500 ASN A 110 71.81 -162.16
REMARK 500 ASN A 152 -18.63 77.13
REMARK 500 ASP A 219 110.33 -179.45
REMARK 500 TYR A 253 35.07 -96.03
REMARK 500 TRP A 275 142.18 -176.69
REMARK 500 LYS A 320 -69.71 -126.23
REMARK 500 ALA A 325 -66.87 -96.02
REMARK 500 ASP A 347 -5.65 72.20
REMARK 500 SER A 383 -92.82 -115.48
REMARK 500 TRP B 15 48.03 -163.85
REMARK 500 HIS B 71 -78.50 -70.98
REMARK 500 TYR B 92 -70.80 -79.08
REMARK 500 ASN B 110 84.84 -166.39
REMARK 500 ALA B 129 135.69 -170.29
REMARK 500 PHE B 179 43.88 -94.43
REMARK 500 ASP B 195 17.26 -65.26
REMARK 500 ASN B 196 22.10 -153.11
REMARK 500 ASP B 197 51.20 32.59
REMARK 500 ARG B 210 -71.68 -40.10
REMARK 500 GLN B 212 -64.06 -24.76
REMARK 500 ASP B 218 28.80 -149.23
REMARK 500 LEU B 230 76.87 -69.72
REMARK 500 HIS B 234 -15.58 -140.91
REMARK 500 ALA B 259 86.66 55.25
REMARK 500 TRP B 275 144.84 -170.15
REMARK 500 ASN B 306 152.37 179.85
REMARK 500 GLU B 308 -165.70 -78.75
REMARK 500 GLU B 309 25.26 40.78
REMARK 500 LYS B 320 -41.11 -138.56
REMARK 500 GLU B 357 -62.27 -26.17
REMARK 500 TRP C 15 47.44 -151.88
REMARK 500 ASN C 27 42.32 71.47
REMARK 500 HIS C 71 -80.77 -68.54
REMARK 500 LYS C 79 88.06 -159.14
REMARK 500 ASN C 110 77.71 -160.23
REMARK 500 ASN C 152 -17.05 77.87
REMARK 500 TYR C 253 45.18 -102.44
REMARK 500 TRP C 275 142.16 -173.29
REMARK 500 LYS C 320 -58.37 -128.07
REMARK 500 ALA C 325 -66.10 -101.54
REMARK 500 ASP C 347 -4.77 70.38
REMARK 500 CYS D 9 173.88 179.54
REMARK 500 ALA D 103 -143.29 -124.88
REMARK 500 VAL E 8 -62.53 -91.33
REMARK 500 CYS E 9 179.84 178.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 502 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 69 SG
REMARK 620 2 FES A 502 S1 107.4
REMARK 620 3 FES A 502 S2 108.9 107.1
REMARK 620 4 CYS A 90 SG 108.3 106.9 117.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 502 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 71 ND1
REMARK 620 2 FES A 502 S1 116.3
REMARK 620 3 FES A 502 S2 119.9 104.2
REMARK 620 4 HIS A 93 ND1 89.9 111.2 115.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 183 NE2
REMARK 620 2 HIS A 187 NE2 104.8
REMARK 620 3 ASP A 333 OD1 104.3 91.1
REMARK 620 4 ASP A 333 OD2 156.0 90.6 56.2
REMARK 620 5 HOH A 778 O 111.3 100.0 138.2 83.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 502 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 69 SG
REMARK 620 2 FES B 502 S1 108.0
REMARK 620 3 FES B 502 S2 107.0 104.2
REMARK 620 4 CYS B 90 SG 108.7 108.0 120.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 502 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 71 ND1
REMARK 620 2 FES B 502 S1 116.2
REMARK 620 3 FES B 502 S2 118.8 103.3
REMARK 620 4 HIS B 93 ND1 88.7 113.5 116.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 B 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 183 NE2
REMARK 620 2 HIS B 187 NE2 113.0
REMARK 620 3 ASP B 333 OD1 118.0 77.4
REMARK 620 4 HOH B 601 O 116.3 84.9 125.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 502 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 69 SG
REMARK 620 2 FES C 502 S1 105.3
REMARK 620 3 FES C 502 S2 112.2 103.6
REMARK 620 4 CYS C 90 SG 107.3 109.9 117.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 502 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 71 ND1
REMARK 620 2 FES C 502 S1 117.5
REMARK 620 3 FES C 502 S2 115.0 103.3
REMARK 620 4 HIS C 93 ND1 91.8 117.7 112.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 C 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 183 NE2
REMARK 620 2 HIS C 187 NE2 109.0
REMARK 620 3 ASP C 333 OD1 112.5 93.1
REMARK 620 4 ASP C 333 OD2 157.3 93.7 63.7
REMARK 620 5 HOH C 601 O 91.3 90.4 153.2 89.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES D 201 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 46 SG
REMARK 620 2 FES D 201 S1 110.3
REMARK 620 3 FES D 201 S2 113.8 104.5
REMARK 620 4 CYS D 65 SG 109.7 111.2 107.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES D 201 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 48 ND1
REMARK 620 2 FES D 201 S1 118.5
REMARK 620 3 FES D 201 S2 109.4 104.6
REMARK 620 4 HIS D 68 ND1 99.2 107.1 118.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES E 201 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 46 SG
REMARK 620 2 FES E 201 S1 113.3
REMARK 620 3 FES E 201 S2 111.9 106.8
REMARK 620 4 CYS E 65 SG 106.3 110.9 107.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES E 201 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 48 ND1
REMARK 620 2 FES E 201 S1 123.2
REMARK 620 3 FES E 201 S2 103.7 101.8
REMARK 620 4 HIS E 68 ND1 100.1 108.5 121.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9CA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9CA B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 9CA C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES E 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NB8 RELATED DB: PDB
REMARK 900 RELATED ID: 4NB9 RELATED DB: PDB
REMARK 900 RELATED ID: 4NBA RELATED DB: PDB
REMARK 900 RELATED ID: 4NBB RELATED DB: PDB
REMARK 900 RELATED ID: 4NBC RELATED DB: PDB
REMARK 900 RELATED ID: 4NBE RELATED DB: PDB
REMARK 900 RELATED ID: 4NBF RELATED DB: PDB
REMARK 900 RELATED ID: 4NBG RELATED DB: PDB
REMARK 900 RELATED ID: 4NBH RELATED DB: PDB
DBREF 4NBD A 1 384 UNP Q84II6 Q84II6_JANS3 1 384
DBREF 4NBD B 1 384 UNP Q84II6 Q84II6_JANS3 1 384
DBREF 4NBD C 1 384 UNP Q84II6 Q84II6_JANS3 1 384
DBREF 4NBD D 1 107 UNP Q8GI16 CARAC_PSERE 1 107
DBREF 4NBD E 1 107 UNP Q8GI16 CARAC_PSERE 1 107
SEQADV 4NBD TRP A 275 UNP Q84II6 PHE 275 ENGINEERED MUTATION
SEQADV 4NBD LEU A 385 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD GLU A 386 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS A 387 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS A 388 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS A 389 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS A 390 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS A 391 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS A 392 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD TRP B 275 UNP Q84II6 PHE 275 ENGINEERED MUTATION
SEQADV 4NBD LEU B 385 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD GLU B 386 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS B 387 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS B 388 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS B 389 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS B 390 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS B 391 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS B 392 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD TRP C 275 UNP Q84II6 PHE 275 ENGINEERED MUTATION
SEQADV 4NBD LEU C 385 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD GLU C 386 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS C 387 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS C 388 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS C 389 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS C 390 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS C 391 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD HIS C 392 UNP Q84II6 EXPRESSION TAG
SEQADV 4NBD LEU D 108 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD GLU D 109 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD HIS D 110 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD HIS D 111 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD HIS D 112 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD HIS D 113 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD HIS D 114 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD HIS D 115 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD LEU E 108 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD GLU E 109 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD HIS E 110 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD HIS E 111 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD HIS E 112 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD HIS E 113 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD HIS E 114 UNP Q8GI16 EXPRESSION TAG
SEQADV 4NBD HIS E 115 UNP Q8GI16 EXPRESSION TAG
SEQRES 1 A 392 MET ALA ASN VAL ASP GLU ALA ILE LEU LYS ARG VAL LYS
SEQRES 2 A 392 GLY TRP ALA PRO TYR VAL ASP ALA LYS LEU GLY PHE ARG
SEQRES 3 A 392 ASN HIS TRP TYR PRO VAL MET PHE SER LYS GLU ILE ASN
SEQRES 4 A 392 GLU GLY GLU PRO LYS THR LEU LYS LEU LEU GLY GLU ASN
SEQRES 5 A 392 LEU LEU VAL ASN ARG ILE ASP GLY LYS LEU TYR CYS LEU
SEQRES 6 A 392 LYS ASP ARG CYS LEU HIS ARG GLY VAL GLN LEU SER VAL
SEQRES 7 A 392 LYS VAL GLU CYS LYS THR LYS SER THR ILE THR CYS TRP
SEQRES 8 A 392 TYR HIS ALA TRP THR TYR ARG TRP GLU ASP GLY VAL LEU
SEQRES 9 A 392 CYS ASP ILE LEU THR ASN PRO THR SER ALA GLN ILE GLY
SEQRES 10 A 392 ARG GLN LYS LEU LYS THR TYR PRO VAL GLN GLU ALA LYS
SEQRES 11 A 392 GLY CYS VAL PHE ILE TYR LEU GLY ASP GLY ASP PRO PRO
SEQRES 12 A 392 PRO LEU ALA ARG ASP THR PRO PRO ASN PHE LEU ASP ASP
SEQRES 13 A 392 ASP MET GLU ILE LEU GLY LYS ASN GLN ILE ILE LYS SER
SEQRES 14 A 392 ASN TRP ARG LEU ALA VAL GLU ASN GLY PHE ASP PRO SER
SEQRES 15 A 392 HIS ILE TYR ILE HIS LYS ASP SER ILE LEU VAL LYS ASP
SEQRES 16 A 392 ASN ASP LEU ALA LEU PRO LEU GLY PHE ALA PRO GLY GLY
SEQRES 17 A 392 ASP ARG LYS GLN GLN THR ARG VAL VAL ASP ASP ASP VAL
SEQRES 18 A 392 VAL GLY ARG LYS GLY VAL TYR ASP LEU ILE GLY GLU HIS
SEQRES 19 A 392 GLY VAL PRO VAL PHE GLU GLY THR ILE GLY GLY GLU VAL
SEQRES 20 A 392 VAL ARG GLU GLY ALA TYR GLY GLU LYS ILE VAL ALA ASN
SEQRES 21 A 392 ASP ILE SER ILE TRP LEU PRO GLY VAL LEU LYS VAL ASN
SEQRES 22 A 392 PRO TRP PRO ASN PRO ASP MET MET GLN PHE GLU TRP TYR
SEQRES 23 A 392 VAL PRO ILE ASP GLU ASN THR HIS TYR TYR PHE GLN THR
SEQRES 24 A 392 LEU GLY LYS PRO CYS ALA ASN ASP GLU GLU ARG LYS LYS
SEQRES 25 A 392 TYR GLU GLN GLU PHE GLU SER LYS TRP LYS PRO MET ALA
SEQRES 26 A 392 LEU GLU GLY PHE ASN ASN ASP ASP ILE TRP ALA ARG GLU
SEQRES 27 A 392 ALA MET VAL ASP PHE TYR ALA ASP ASP LYS GLY TRP VAL
SEQRES 28 A 392 ASN GLU ILE LEU PHE GLU SER ASP GLU ALA ILE VAL ALA
SEQRES 29 A 392 TRP ARG LYS LEU ALA SER GLU HIS ASN GLN GLY ILE GLN
SEQRES 30 A 392 THR GLN ALA HIS VAL SER GLY LEU GLU HIS HIS HIS HIS
SEQRES 31 A 392 HIS HIS
SEQRES 1 B 392 MET ALA ASN VAL ASP GLU ALA ILE LEU LYS ARG VAL LYS
SEQRES 2 B 392 GLY TRP ALA PRO TYR VAL ASP ALA LYS LEU GLY PHE ARG
SEQRES 3 B 392 ASN HIS TRP TYR PRO VAL MET PHE SER LYS GLU ILE ASN
SEQRES 4 B 392 GLU GLY GLU PRO LYS THR LEU LYS LEU LEU GLY GLU ASN
SEQRES 5 B 392 LEU LEU VAL ASN ARG ILE ASP GLY LYS LEU TYR CYS LEU
SEQRES 6 B 392 LYS ASP ARG CYS LEU HIS ARG GLY VAL GLN LEU SER VAL
SEQRES 7 B 392 LYS VAL GLU CYS LYS THR LYS SER THR ILE THR CYS TRP
SEQRES 8 B 392 TYR HIS ALA TRP THR TYR ARG TRP GLU ASP GLY VAL LEU
SEQRES 9 B 392 CYS ASP ILE LEU THR ASN PRO THR SER ALA GLN ILE GLY
SEQRES 10 B 392 ARG GLN LYS LEU LYS THR TYR PRO VAL GLN GLU ALA LYS
SEQRES 11 B 392 GLY CYS VAL PHE ILE TYR LEU GLY ASP GLY ASP PRO PRO
SEQRES 12 B 392 PRO LEU ALA ARG ASP THR PRO PRO ASN PHE LEU ASP ASP
SEQRES 13 B 392 ASP MET GLU ILE LEU GLY LYS ASN GLN ILE ILE LYS SER
SEQRES 14 B 392 ASN TRP ARG LEU ALA VAL GLU ASN GLY PHE ASP PRO SER
SEQRES 15 B 392 HIS ILE TYR ILE HIS LYS ASP SER ILE LEU VAL LYS ASP
SEQRES 16 B 392 ASN ASP LEU ALA LEU PRO LEU GLY PHE ALA PRO GLY GLY
SEQRES 17 B 392 ASP ARG LYS GLN GLN THR ARG VAL VAL ASP ASP ASP VAL
SEQRES 18 B 392 VAL GLY ARG LYS GLY VAL TYR ASP LEU ILE GLY GLU HIS
SEQRES 19 B 392 GLY VAL PRO VAL PHE GLU GLY THR ILE GLY GLY GLU VAL
SEQRES 20 B 392 VAL ARG GLU GLY ALA TYR GLY GLU LYS ILE VAL ALA ASN
SEQRES 21 B 392 ASP ILE SER ILE TRP LEU PRO GLY VAL LEU LYS VAL ASN
SEQRES 22 B 392 PRO TRP PRO ASN PRO ASP MET MET GLN PHE GLU TRP TYR
SEQRES 23 B 392 VAL PRO ILE ASP GLU ASN THR HIS TYR TYR PHE GLN THR
SEQRES 24 B 392 LEU GLY LYS PRO CYS ALA ASN ASP GLU GLU ARG LYS LYS
SEQRES 25 B 392 TYR GLU GLN GLU PHE GLU SER LYS TRP LYS PRO MET ALA
SEQRES 26 B 392 LEU GLU GLY PHE ASN ASN ASP ASP ILE TRP ALA ARG GLU
SEQRES 27 B 392 ALA MET VAL ASP PHE TYR ALA ASP ASP LYS GLY TRP VAL
SEQRES 28 B 392 ASN GLU ILE LEU PHE GLU SER ASP GLU ALA ILE VAL ALA
SEQRES 29 B 392 TRP ARG LYS LEU ALA SER GLU HIS ASN GLN GLY ILE GLN
SEQRES 30 B 392 THR GLN ALA HIS VAL SER GLY LEU GLU HIS HIS HIS HIS
SEQRES 31 B 392 HIS HIS
SEQRES 1 C 392 MET ALA ASN VAL ASP GLU ALA ILE LEU LYS ARG VAL LYS
SEQRES 2 C 392 GLY TRP ALA PRO TYR VAL ASP ALA LYS LEU GLY PHE ARG
SEQRES 3 C 392 ASN HIS TRP TYR PRO VAL MET PHE SER LYS GLU ILE ASN
SEQRES 4 C 392 GLU GLY GLU PRO LYS THR LEU LYS LEU LEU GLY GLU ASN
SEQRES 5 C 392 LEU LEU VAL ASN ARG ILE ASP GLY LYS LEU TYR CYS LEU
SEQRES 6 C 392 LYS ASP ARG CYS LEU HIS ARG GLY VAL GLN LEU SER VAL
SEQRES 7 C 392 LYS VAL GLU CYS LYS THR LYS SER THR ILE THR CYS TRP
SEQRES 8 C 392 TYR HIS ALA TRP THR TYR ARG TRP GLU ASP GLY VAL LEU
SEQRES 9 C 392 CYS ASP ILE LEU THR ASN PRO THR SER ALA GLN ILE GLY
SEQRES 10 C 392 ARG GLN LYS LEU LYS THR TYR PRO VAL GLN GLU ALA LYS
SEQRES 11 C 392 GLY CYS VAL PHE ILE TYR LEU GLY ASP GLY ASP PRO PRO
SEQRES 12 C 392 PRO LEU ALA ARG ASP THR PRO PRO ASN PHE LEU ASP ASP
SEQRES 13 C 392 ASP MET GLU ILE LEU GLY LYS ASN GLN ILE ILE LYS SER
SEQRES 14 C 392 ASN TRP ARG LEU ALA VAL GLU ASN GLY PHE ASP PRO SER
SEQRES 15 C 392 HIS ILE TYR ILE HIS LYS ASP SER ILE LEU VAL LYS ASP
SEQRES 16 C 392 ASN ASP LEU ALA LEU PRO LEU GLY PHE ALA PRO GLY GLY
SEQRES 17 C 392 ASP ARG LYS GLN GLN THR ARG VAL VAL ASP ASP ASP VAL
SEQRES 18 C 392 VAL GLY ARG LYS GLY VAL TYR ASP LEU ILE GLY GLU HIS
SEQRES 19 C 392 GLY VAL PRO VAL PHE GLU GLY THR ILE GLY GLY GLU VAL
SEQRES 20 C 392 VAL ARG GLU GLY ALA TYR GLY GLU LYS ILE VAL ALA ASN
SEQRES 21 C 392 ASP ILE SER ILE TRP LEU PRO GLY VAL LEU LYS VAL ASN
SEQRES 22 C 392 PRO TRP PRO ASN PRO ASP MET MET GLN PHE GLU TRP TYR
SEQRES 23 C 392 VAL PRO ILE ASP GLU ASN THR HIS TYR TYR PHE GLN THR
SEQRES 24 C 392 LEU GLY LYS PRO CYS ALA ASN ASP GLU GLU ARG LYS LYS
SEQRES 25 C 392 TYR GLU GLN GLU PHE GLU SER LYS TRP LYS PRO MET ALA
SEQRES 26 C 392 LEU GLU GLY PHE ASN ASN ASP ASP ILE TRP ALA ARG GLU
SEQRES 27 C 392 ALA MET VAL ASP PHE TYR ALA ASP ASP LYS GLY TRP VAL
SEQRES 28 C 392 ASN GLU ILE LEU PHE GLU SER ASP GLU ALA ILE VAL ALA
SEQRES 29 C 392 TRP ARG LYS LEU ALA SER GLU HIS ASN GLN GLY ILE GLN
SEQRES 30 C 392 THR GLN ALA HIS VAL SER GLY LEU GLU HIS HIS HIS HIS
SEQRES 31 C 392 HIS HIS
SEQRES 1 D 115 MET ASN GLN ILE TRP LEU LYS VAL CYS ALA ALA SER ASP
SEQRES 2 D 115 MET GLN PRO GLY THR ILE ARG ARG VAL ASN ARG VAL GLY
SEQRES 3 D 115 ALA ALA PRO LEU ALA VAL TYR ARG VAL GLY ASP GLN PHE
SEQRES 4 D 115 TYR ALA THR GLU ASP THR CYS THR HIS GLY ILE ALA SER
SEQRES 5 D 115 LEU SER GLU GLY THR LEU ASP GLY ASP VAL ILE GLU CYS
SEQRES 6 D 115 PRO PHE HIS GLY GLY ALA PHE ASN VAL CYS THR GLY MET
SEQRES 7 D 115 PRO ALA SER SER PRO CYS THR VAL PRO LEU GLY VAL PHE
SEQRES 8 D 115 GLU VAL GLU VAL LYS GLU GLY GLU VAL TYR VAL ALA GLY
SEQRES 9 D 115 GLU LYS LYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 E 115 MET ASN GLN ILE TRP LEU LYS VAL CYS ALA ALA SER ASP
SEQRES 2 E 115 MET GLN PRO GLY THR ILE ARG ARG VAL ASN ARG VAL GLY
SEQRES 3 E 115 ALA ALA PRO LEU ALA VAL TYR ARG VAL GLY ASP GLN PHE
SEQRES 4 E 115 TYR ALA THR GLU ASP THR CYS THR HIS GLY ILE ALA SER
SEQRES 5 E 115 LEU SER GLU GLY THR LEU ASP GLY ASP VAL ILE GLU CYS
SEQRES 6 E 115 PRO PHE HIS GLY GLY ALA PHE ASN VAL CYS THR GLY MET
SEQRES 7 E 115 PRO ALA SER SER PRO CYS THR VAL PRO LEU GLY VAL PHE
SEQRES 8 E 115 GLU VAL GLU VAL LYS GLU GLY GLU VAL TYR VAL ALA GLY
SEQRES 9 E 115 GLU LYS LYS LEU GLU HIS HIS HIS HIS HIS HIS
HET FE2 A 501 1
HET FES A 502 4
HET 9CA A 503 13
HET FE2 B 501 1
HET FES B 502 4
HET 9CA B 503 13
HET FE2 C 501 1
HET FES C 502 4
HET 9CA C 503 13
HET FES D 201 4
HET FES E 201 4
HETNAM FE2 FE (II) ION
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM 9CA 9H-CARBAZOLE
FORMUL 6 FE2 3(FE 2+)
FORMUL 7 FES 5(FE2 S2)
FORMUL 8 9CA 3(C12 H9 N)
FORMUL 17 HOH *897(H2 O)
HELIX 1 1 ASP A 5 VAL A 12 1 8
HELIX 2 2 TRP A 15 ALA A 21 1 7
HELIX 3 3 LYS A 36 ILE A 38 5 3
HELIX 4 4 GLN A 75 VAL A 80 5 6
HELIX 5 5 PRO A 144 THR A 149 5 6
HELIX 6 6 ASN A 170 ASP A 180 1 11
HELIX 7 7 PRO A 181 LYS A 188 5 8
HELIX 8 8 SER A 190 ASN A 196 1 7
HELIX 9 9 ASP A 209 GLN A 212 5 4
HELIX 10 10 LEU A 230 GLY A 235 1 6
HELIX 11 11 ASN A 306 LYS A 320 1 15
HELIX 12 12 LYS A 320 ALA A 325 1 6
HELIX 13 13 ASN A 330 MET A 340 1 11
HELIX 14 14 MET A 340 ASP A 346 1 7
HELIX 15 15 LYS A 348 GLU A 353 1 6
HELIX 16 16 PHE A 356 SER A 358 5 3
HELIX 17 17 ASP A 359 ASN A 373 1 15
HELIX 18 18 THR A 378 SER A 383 1 6
HELIX 19 19 ASP B 5 LYS B 10 1 6
HELIX 20 20 TRP B 15 ALA B 21 1 7
HELIX 21 21 LYS B 36 ILE B 38 5 3
HELIX 22 22 GLN B 75 VAL B 80 5 6
HELIX 23 23 PRO B 144 THR B 149 5 6
HELIX 24 24 ASN B 170 PHE B 179 1 10
HELIX 25 25 SER B 182 LYS B 188 5 7
HELIX 26 26 SER B 190 ASP B 195 1 6
HELIX 27 27 ASP B 209 GLN B 213 1 5
HELIX 28 28 LEU B 230 GLY B 235 1 6
HELIX 29 29 ARG B 310 LYS B 320 1 11
HELIX 30 30 LYS B 320 ALA B 325 1 6
HELIX 31 31 ASN B 330 MET B 340 1 11
HELIX 32 32 MET B 340 ASP B 346 1 7
HELIX 33 33 LYS B 348 GLU B 353 1 6
HELIX 34 34 PHE B 356 SER B 358 5 3
HELIX 35 35 ASP B 359 ASN B 373 1 15
HELIX 36 36 THR B 378 SER B 383 1 6
HELIX 37 37 ASP C 5 LYS C 10 1 6
HELIX 38 38 ARG C 11 LYS C 13 5 3
HELIX 39 39 TRP C 15 ALA C 21 1 7
HELIX 40 40 LYS C 36 ILE C 38 5 3
HELIX 41 41 GLN C 75 VAL C 80 5 6
HELIX 42 42 PRO C 144 THR C 149 5 6
HELIX 43 43 ASN C 170 PHE C 179 1 10
HELIX 44 44 SER C 182 LYS C 188 5 7
HELIX 45 45 SER C 190 ASN C 196 1 7
HELIX 46 46 ASP C 209 GLN C 213 1 5
HELIX 47 47 LEU C 230 GLY C 235 1 6
HELIX 48 48 ASN C 306 LYS C 320 1 15
HELIX 49 49 LYS C 320 ALA C 325 1 6
HELIX 50 50 ASN C 330 ALA C 345 1 16
HELIX 51 51 LYS C 348 GLU C 353 1 6
HELIX 52 52 PHE C 356 SER C 358 5 3
HELIX 53 53 ASP C 359 ASN C 373 1 15
HELIX 54 54 THR C 378 GLY C 384 1 7
HELIX 55 55 SER D 52 GLY D 56 5 5
HELIX 56 56 SER E 12 MET E 14 5 3
HELIX 57 57 SER E 52 GLY E 56 5 5
SHEET 1 A 3 HIS A 28 PHE A 34 0
SHEET 2 A 3 CYS A 132 LEU A 137 -1 O VAL A 133 N MET A 33
SHEET 3 A 3 VAL A 126 ALA A 129 -1 N GLN A 127 O PHE A 134
SHEET 1 B 4 LYS A 44 LEU A 48 0
SHEET 2 B 4 GLU A 51 ILE A 58 -1 O LEU A 53 N LEU A 46
SHEET 3 B 4 LYS A 61 LYS A 66 -1 O LYS A 61 N ILE A 58
SHEET 4 B 4 THR A 123 TYR A 124 -1 O TYR A 124 N CYS A 64
SHEET 1 C 3 THR A 87 THR A 89 0
SHEET 2 C 3 TRP A 95 ARG A 98 -1 O TYR A 97 N ILE A 88
SHEET 3 C 3 LEU A 104 ILE A 107 -1 O ASP A 106 N THR A 96
SHEET 1 D 3 MET A 158 LYS A 163 0
SHEET 2 D 3 THR A 293 PRO A 303 -1 O LEU A 300 N LEU A 161
SHEET 3 D 3 ILE A 166 ILE A 167 -1 N ILE A 167 O HIS A 294
SHEET 1 E 7 MET A 158 LYS A 163 0
SHEET 2 E 7 THR A 293 PRO A 303 -1 O LEU A 300 N LEU A 161
SHEET 3 E 7 MET A 281 ASP A 290 -1 N MET A 281 O GLY A 301
SHEET 4 E 7 VAL A 269 ASN A 273 -1 N LEU A 270 O GLU A 284
SHEET 5 E 7 ASP A 261 TRP A 265 -1 N ASP A 261 O ASN A 273
SHEET 6 E 7 GLY A 226 ASP A 229 -1 N ASP A 229 O ILE A 262
SHEET 7 E 7 THR A 214 VAL A 217 -1 N VAL A 217 O GLY A 226
SHEET 1 F 2 ALA A 199 LEU A 200 0
SHEET 2 F 2 ALA A 252 TYR A 253 -1 O ALA A 252 N LEU A 200
SHEET 1 G 2 GLY A 203 ALA A 205 0
SHEET 2 G 2 VAL A 236 VAL A 238 -1 O VAL A 236 N ALA A 205
SHEET 1 H 2 GLU A 240 ILE A 243 0
SHEET 2 H 2 GLU A 246 GLU A 250 -1 O ARG A 249 N GLY A 241
SHEET 1 I 3 TRP B 29 PHE B 34 0
SHEET 2 I 3 CYS B 132 TYR B 136 -1 O VAL B 133 N MET B 33
SHEET 3 I 3 VAL B 126 ALA B 129 -1 N GLN B 127 O PHE B 134
SHEET 1 J 4 LYS B 44 LEU B 48 0
SHEET 2 J 4 GLU B 51 ILE B 58 -1 O LEU B 53 N LEU B 46
SHEET 3 J 4 LYS B 61 LYS B 66 -1 O LYS B 61 N ILE B 58
SHEET 4 J 4 THR B 123 TYR B 124 -1 O TYR B 124 N CYS B 64
SHEET 1 K 3 THR B 87 THR B 89 0
SHEET 2 K 3 TRP B 95 ARG B 98 -1 O TYR B 97 N ILE B 88
SHEET 3 K 3 LEU B 104 ILE B 107 -1 O ASP B 106 N THR B 96
SHEET 1 L 7 MET B 158 ILE B 167 0
SHEET 2 L 7 THR B 293 PRO B 303 -1 O LEU B 300 N LEU B 161
SHEET 3 L 7 MET B 281 ASP B 290 -1 N MET B 281 O GLY B 301
SHEET 4 L 7 VAL B 269 ASN B 273 -1 N LEU B 270 O GLU B 284
SHEET 5 L 7 ASP B 261 TRP B 265 -1 N TRP B 265 O VAL B 269
SHEET 6 L 7 GLY B 226 ASP B 229 -1 N ASP B 229 O ILE B 262
SHEET 7 L 7 THR B 214 VAL B 217 -1 N VAL B 217 O GLY B 226
SHEET 1 M 2 LEU B 198 ALA B 199 0
SHEET 2 M 2 LYS B 256 ILE B 257 1 O LYS B 256 N ALA B 199
SHEET 1 N 2 GLY B 203 ALA B 205 0
SHEET 2 N 2 VAL B 236 VAL B 238 -1 O VAL B 236 N ALA B 205
SHEET 1 O 2 GLU B 240 ILE B 243 0
SHEET 2 O 2 GLU B 246 GLU B 250 -1 O ARG B 249 N GLY B 241
SHEET 1 P 3 HIS C 28 PHE C 34 0
SHEET 2 P 3 CYS C 132 LEU C 137 -1 O VAL C 133 N MET C 33
SHEET 3 P 3 VAL C 126 ALA C 129 -1 N GLN C 127 O PHE C 134
SHEET 1 Q 4 LYS C 44 LEU C 48 0
SHEET 2 Q 4 GLU C 51 ILE C 58 -1 O LEU C 53 N LEU C 46
SHEET 3 Q 4 LYS C 61 LYS C 66 -1 O LYS C 61 N ILE C 58
SHEET 4 Q 4 THR C 123 TYR C 124 -1 O TYR C 124 N CYS C 64
SHEET 1 R 3 THR C 87 THR C 89 0
SHEET 2 R 3 TRP C 95 ARG C 98 -1 O TYR C 97 N ILE C 88
SHEET 3 R 3 LEU C 104 ILE C 107 -1 O ASP C 106 N THR C 96
SHEET 1 S 7 MET C 158 ILE C 167 0
SHEET 2 S 7 THR C 293 PRO C 303 -1 O LEU C 300 N LEU C 161
SHEET 3 S 7 MET C 281 ASP C 290 -1 N MET C 281 O GLY C 301
SHEET 4 S 7 VAL C 269 ASN C 273 -1 N LEU C 270 O GLU C 284
SHEET 5 S 7 ASP C 261 TRP C 265 -1 N SER C 263 O LYS C 271
SHEET 6 S 7 GLY C 226 ASP C 229 -1 N ASP C 229 O ILE C 262
SHEET 7 S 7 THR C 214 VAL C 217 -1 N VAL C 217 O GLY C 226
SHEET 1 T 3 ALA C 252 TYR C 253 0
SHEET 2 T 3 LEU C 198 LEU C 200 -1 N LEU C 200 O ALA C 252
SHEET 3 T 3 LYS C 256 ILE C 257 1 O LYS C 256 N ALA C 199
SHEET 1 U 2 GLY C 203 ALA C 205 0
SHEET 2 U 2 VAL C 236 VAL C 238 -1 O VAL C 236 N ALA C 205
SHEET 1 V 2 GLU C 240 ILE C 243 0
SHEET 2 V 2 GLU C 246 GLU C 250 -1 O ARG C 249 N GLY C 241
SHEET 1 W 3 LEU D 6 ALA D 10 0
SHEET 2 W 3 GLU D 99 GLU D 105 -1 O VAL D 100 N VAL D 8
SHEET 3 W 3 PHE D 91 LYS D 96 -1 N GLU D 94 O TYR D 101
SHEET 1 X 3 ARG D 20 ARG D 24 0
SHEET 2 X 3 ALA D 27 VAL D 35 -1 O LEU D 30 N VAL D 22
SHEET 3 X 3 GLN D 38 GLU D 43 -1 O THR D 42 N ALA D 31
SHEET 1 Y 4 THR D 57 ASP D 59 0
SHEET 2 Y 4 VAL D 62 GLU D 64 -1 O GLU D 64 N THR D 57
SHEET 3 Y 4 ALA D 71 ASN D 73 -1 O PHE D 72 N ILE D 63
SHEET 4 Y 4 PRO D 79 SER D 81 -1 O ALA D 80 N ALA D 71
SHEET 1 Z 3 TRP E 5 ALA E 10 0
SHEET 2 Z 3 GLU E 99 ALA E 103 -1 O VAL E 100 N VAL E 8
SHEET 3 Z 3 VAL E 93 LYS E 96 -1 N GLU E 94 O TYR E 101
SHEET 1 AA 4 ARG E 20 VAL E 22 0
SHEET 2 AA 4 LEU E 30 VAL E 35 -1 O LEU E 30 N VAL E 22
SHEET 3 AA 4 GLN E 38 GLU E 43 -1 O TYR E 40 N TYR E 33
SHEET 4 AA 4 VAL E 90 PHE E 91 -1 O PHE E 91 N ALA E 41
SHEET 1 AB 4 THR E 57 ASP E 59 0
SHEET 2 AB 4 VAL E 62 GLU E 64 -1 O GLU E 64 N THR E 57
SHEET 3 AB 4 ALA E 71 ASN E 73 -1 O PHE E 72 N ILE E 63
SHEET 4 AB 4 PRO E 79 SER E 81 -1 O ALA E 80 N ALA E 71
LINK SG CYS A 69 FE1 FES A 502 1555 1555 2.28
LINK ND1 HIS A 71 FE2 FES A 502 1555 1555 2.11
LINK SG CYS A 90 FE1 FES A 502 1555 1555 2.32
LINK ND1 HIS A 93 FE2 FES A 502 1555 1555 2.11
LINK NE2 HIS A 183 FE FE2 A 501 1555 1555 2.10
LINK NE2 HIS A 187 FE FE2 A 501 1555 1555 2.22
LINK OD1 ASP A 333 FE FE2 A 501 1555 1555 1.96
LINK OD2 ASP A 333 FE FE2 A 501 1555 1555 2.56
LINK FE FE2 A 501 O HOH A 778 1555 1555 1.84
LINK SG CYS B 69 FE1 FES B 502 1555 1555 2.24
LINK ND1 HIS B 71 FE2 FES B 502 1555 1555 2.16
LINK SG CYS B 90 FE1 FES B 502 1555 1555 2.24
LINK ND1 HIS B 93 FE2 FES B 502 1555 1555 2.14
LINK NE2 HIS B 183 FE FE2 B 501 1555 1555 2.07
LINK NE2 HIS B 187 FE FE2 B 501 1555 1555 2.63
LINK OD1 ASP B 333 FE FE2 B 501 1555 1555 2.02
LINK FE FE2 B 501 O HOH B 601 1555 1555 1.84
LINK SG CYS C 69 FE1 FES C 502 1555 1555 2.31
LINK ND1 HIS C 71 FE2 FES C 502 1555 1555 2.03
LINK SG CYS C 90 FE1 FES C 502 1555 1555 2.16
LINK ND1 HIS C 93 FE2 FES C 502 1555 1555 2.15
LINK NE2 HIS C 183 FE FE2 C 501 1555 1555 2.26
LINK NE2 HIS C 187 FE FE2 C 501 1555 1555 2.20
LINK OD1 ASP C 333 FE FE2 C 501 1555 1555 1.81
LINK OD2 ASP C 333 FE FE2 C 501 1555 1555 2.28
LINK FE FE2 C 501 O HOH C 601 1555 1555 1.90
LINK SG CYS D 46 FE2 FES D 201 1555 1555 2.31
LINK ND1 HIS D 48 FE1 FES D 201 1555 1555 2.18
LINK SG CYS D 65 FE2 FES D 201 1555 1555 2.28
LINK ND1 HIS D 68 FE1 FES D 201 1555 1555 2.17
LINK SG CYS E 46 FE1 FES E 201 1555 1555 2.31
LINK ND1 HIS E 48 FE2 FES E 201 1555 1555 2.17
LINK SG CYS E 65 FE1 FES E 201 1555 1555 2.39
LINK ND1 HIS E 68 FE2 FES E 201 1555 1555 2.12
CISPEP 1 LEU A 266 PRO A 267 0 0.45
CISPEP 2 ASN A 273 PRO A 274 0 -1.93
CISPEP 3 TRP A 275 PRO A 276 0 0.03
CISPEP 4 LEU B 266 PRO B 267 0 0.27
CISPEP 5 ASN B 273 PRO B 274 0 -0.60
CISPEP 6 TRP B 275 PRO B 276 0 -0.31
CISPEP 7 LEU C 266 PRO C 267 0 1.40
CISPEP 8 ASN C 273 PRO C 274 0 -3.17
CISPEP 9 TRP C 275 PRO C 276 0 -0.74
CISPEP 10 SER D 82 PRO D 83 0 0.97
CISPEP 11 SER E 82 PRO E 83 0 0.56
SITE 1 AC1 4 HIS A 183 HIS A 187 ASP A 333 HOH A 778
SITE 1 AC2 6 CYS A 69 HIS A 71 ARG A 72 CYS A 90
SITE 2 AC2 6 HIS A 93 TRP A 95
SITE 1 AC3 11 GLY A 178 HIS A 183 ILE A 184 ALA A 259
SITE 2 AC3 11 ILE A 262 LEU A 270 TRP A 275 GLU A 284
SITE 3 AC3 11 ASN A 330 HOH A 730 HOH A 778
SITE 1 AC4 4 HIS B 183 HIS B 187 ASP B 333 HOH B 601
SITE 1 AC5 7 CYS B 69 HIS B 71 ARG B 72 CYS B 90
SITE 2 AC5 7 TYR B 92 HIS B 93 TRP B 95
SITE 1 AC6 10 GLY B 178 HIS B 183 ILE B 184 ILE B 262
SITE 2 AC6 10 LEU B 270 VAL B 272 GLN B 282 GLU B 284
SITE 3 AC6 10 PHE B 329 ASN B 330
SITE 1 AC7 4 HIS C 183 HIS C 187 ASP C 333 HOH C 601
SITE 1 AC8 7 CYS C 69 HIS C 71 ARG C 72 CYS C 90
SITE 2 AC8 7 TYR C 92 HIS C 93 TRP C 95
SITE 1 AC9 9 GLY C 178 HIS C 183 ILE C 184 LEU C 270
SITE 2 AC9 9 TRP C 275 GLN C 282 GLU C 284 PHE C 329
SITE 3 AC9 9 ASN C 330
SITE 1 BC1 6 CYS D 46 HIS D 48 GLY D 49 CYS D 65
SITE 2 BC1 6 HIS D 68 GLY D 70
SITE 1 BC2 6 CYS E 46 HIS E 48 GLY E 49 CYS E 65
SITE 2 BC2 6 HIS E 68 GLY E 70
CRYST1 98.338 88.203 108.106 90.00 107.19 90.00 P 1 21 1 6
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 0.010169 0.000000 0.003145 0.00000
SCALE2 0.000000 0.011337 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009682 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
