HEADER OXIDOREDUCTASE 04-APR-03 1UBU
TITLE THREE-DIMENSIONAL STRUCTURE OF THE CARBON MONOXIDE COMPLEX OF
TITLE 2 [NIFE]HYDROGENASE FROM DESULUFOVIBRIO VULGARIS MIYAZAKI F
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERIPLASMIC [NIFE] HYDROGENASE SMALL SUBUNIT;
COMPND 3 CHAIN: S;
COMPND 4 SYNONYM: SMALL SUBUNIT OF [NIFE]HYDROGENASE;
COMPND 5 EC: 1.12.2.1;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PERIPLASMIC [NIFE] HYDROGENASE LARGE SUBUNIT;
COMPND 8 CHAIN: L;
COMPND 9 FRAGMENT: RESIDUES 19-552;
COMPND 10 SYNONYM: LARGE SUBUNIT OF [NIFE]HYDROGENASE;
COMPND 11 EC: 1.12.2.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS STR. 'MIYAZAKI F';
SOURCE 3 ORGANISM_TAXID: 883;
SOURCE 4 STRAIN: MIYAZAKI F;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS STR. 'MIYAZAKI F';
SOURCE 7 ORGANISM_TAXID: 883;
SOURCE 8 STRAIN: MIYAZAKI F
KEYWDS HIGH RESOLUTION CRYSTAL STRUCTURE, [NIFE]HYDROGENASE, OXIDOREDUCTASE,
KEYWDS 2 CARBON MONOXIDE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.OGATA,Y.MIZOGUCHI,N.MIZUNO,K.MIKI,S.ADACHI,N.YASUOKA,T.YAGI,
AUTHOR 2 O.YAMAUCHI,S.HIROTA,Y.HIGUCHI
REVDAT 4 25-OCT-23 1UBU 1 REMARK LINK
REVDAT 3 16-APR-14 1UBU 1 REMARK VERSN
REVDAT 2 24-FEB-09 1UBU 1 VERSN
REVDAT 1 29-APR-03 1UBU 0
JRNL AUTH H.OGATA,Y.MIZOGUCHI,N.MIZUNO,K.MIKI,S.ADACHI,N.YASUOKA,
JRNL AUTH 2 T.YAGI,O.YAMAUCHI,S.HIROTA,Y.HIGUCHI
JRNL TITL STRUCTURAL STUDIES OF THE CARBON MONOXIDE COMPLEX OF
JRNL TITL 2 [NIFE]HYDROGENASE FROM DESULFOVIBRIO VULGARIS MIYAZAKI F:
JRNL TITL 3 SUGGESTION FOR THE INITIAL ACTIVATION SITE FOR DIHYDROGEN
JRNL REF J.AM.CHEM.SOC. V. 124 11628 2002
JRNL REFN ISSN 0002-7863
JRNL PMID 12296727
JRNL DOI 10.1021/JA012645K
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.9
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.137
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.137
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 7.500
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 12431
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 178151
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.121
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.121
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 7.500
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 9041
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 120219
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6196
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 929
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 7174.0
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 291.00
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 0
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 59856
REMARK 3 NUMBER OF RESTRAINTS : 72936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 ANGLE DISTANCES (A) : 0.075
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.028
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.064
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.083
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.020
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.055
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: NULL
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1UBU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000005658.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.700
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 131082
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.10500
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) : 1.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.44900
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1H2R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, PH 7.4, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 49.00500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.28500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.01000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.28500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.00500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.01000
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -110.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, L
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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASN S 267 C ASN S 267 O 0.132
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU S 1 O - C - N ANGL. DEV. = 11.2 DEGREES
REMARK 500 MET S 2 CA - CB - CG ANGL. DEV. = 18.1 DEGREES
REMARK 500 ARG S 5 NE - CZ - NH1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG S 6 CD - NE - CZ ANGL. DEV. = 39.1 DEGREES
REMARK 500 ARG S 26 CG - CD - NE ANGL. DEV. = -13.2 DEGREES
REMARK 500 ARG S 26 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG S 26 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG S 100 CD - NE - CZ ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG S 100 NE - CZ - NH1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 PHE S 197 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 TYR S 218 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 TYR S 218 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 LYS S 233 CA - CB - CG ANGL. DEV. = 13.7 DEGREES
REMARK 500 LYS S 233 CD - CE - NZ ANGL. DEV. = 19.7 DEGREES
REMARK 500 ARG L 71 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG L 71 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 TYR L 120 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG L 160 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 LEU L 174 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 LEU L 213 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 ARG L 217 NE - CZ - NH1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 LEU L 218 CA - CB - CG ANGL. DEV. = -17.2 DEGREES
REMARK 500 ARG L 224 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 TYR L 247 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 TYR L 273 CB - CG - CD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TYR L 273 CG - CD1 - CE1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 LEU L 277 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 TRP L 287 CA - CB - CG ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG L 340 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG L 426 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG L 430 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG L 430 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG L 479 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG L 487 CB - CG - CD ANGL. DEV. = 22.0 DEGREES
REMARK 500 LEU L 506 CA - CB - CG ANGL. DEV. = 24.5 DEGREES
REMARK 500 ARG L 509 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG L 532 NE - CZ - NH2 ANGL. DEV. = -3.9 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 PRO S 4 -155.50 -41.82
REMARK 500 ARG S 5 -56.86 -15.38
REMARK 500 ASN S 14 -121.02 -100.69
REMARK 500 GLU S 29 70.40 50.55
REMARK 500 HIS S 45 105.90 -167.00
REMARK 500 LYS S 235 -177.85 62.19
REMARK 500 THR S 239 -23.28 -152.57
REMARK 500 SER L 20 -175.42 -52.95
REMARK 500 TYR L 86 -40.69 67.60
REMARK 500 ALA L 231 -47.09 85.28
REMARK 500 HIS L 235 85.63 70.65
REMARK 500 GLN L 237 69.30 -152.86
REMARK 500 PHE L 238 -1.72 -142.02
REMARK 500 VAL L 272 -60.68 -120.91
REMARK 500 PHE L 302 68.13 78.59
REMARK 500 ALA L 347 10.59 -142.71
REMARK 500 ASP L 363 175.85 70.67
REMARK 500 TYR L 370 17.28 -149.49
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S1001 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 17 SG
REMARK 620 2 SF4 S1001 S2 103.3
REMARK 620 3 SF4 S1001 S3 120.7 106.8
REMARK 620 4 SF4 S1001 S4 114.6 104.9 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S1001 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 20 SG
REMARK 620 2 SF4 S1001 S1 105.4
REMARK 620 3 SF4 S1001 S2 120.1 102.0
REMARK 620 4 SF4 S1001 S3 115.9 103.7 107.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S1001 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 114 SG
REMARK 620 2 SF4 S1001 S1 108.6
REMARK 620 3 SF4 S1001 S3 128.6 104.6
REMARK 620 4 SF4 S1001 S4 98.9 109.4 105.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S1001 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 150 SG
REMARK 620 2 SF4 S1001 S1 111.1
REMARK 620 3 SF4 S1001 S2 124.9 103.3
REMARK 620 4 SF4 S1001 S4 102.9 107.7 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S1002 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS S 188 ND1
REMARK 620 2 SF4 S1002 S2 104.3
REMARK 620 3 SF4 S1002 S3 114.0 105.9
REMARK 620 4 SF4 S1002 S4 117.8 109.2 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S1002 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 191 SG
REMARK 620 2 SF4 S1002 S1 121.6
REMARK 620 3 SF4 S1002 S2 112.8 103.3
REMARK 620 4 SF4 S1002 S4 104.6 106.1 107.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S1002 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 216 SG
REMARK 620 2 SF4 S1002 S1 121.7
REMARK 620 3 SF4 S1002 S2 118.9 103.6
REMARK 620 4 SF4 S1002 S3 100.8 104.2 105.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 S1002 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 222 SG
REMARK 620 2 SF4 S1002 S1 118.0
REMARK 620 3 SF4 S1002 S3 112.6 104.7
REMARK 620 4 SF4 S1002 S4 109.4 107.0 104.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S S1003 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 231 SG
REMARK 620 2 F3S S1003 S1 116.6
REMARK 620 3 F3S S1003 S3 110.6 104.0
REMARK 620 4 F3S S1003 S4 109.2 112.1 103.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S S1003 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 249 SG
REMARK 620 2 F3S S1003 S1 114.0
REMARK 620 3 F3S S1003 S2 110.4 112.2
REMARK 620 4 F3S S1003 S3 112.2 103.2 104.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S S1003 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 252 SG
REMARK 620 2 F3S S1003 S2 110.9
REMARK 620 3 F3S S1003 S3 117.4 104.5
REMARK 620 4 F3S S1003 S4 106.6 114.0 103.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L1005 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU L 62 OE2
REMARK 620 2 LEU L 498 O 95.9
REMARK 620 3 HIS L 552 NE2 82.8 88.1
REMARK 620 4 HOH L3001 O 174.3 89.6 96.3
REMARK 620 5 HOH L3002 O 95.3 88.4 175.9 85.9
REMARK 620 6 HOH L3003 O 93.0 171.1 93.7 81.5 90.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FNE L1004 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 81 SG
REMARK 620 2 FNE L1004 FE 149.1
REMARK 620 3 CYS L 84 SG 98.4 55.3
REMARK 620 4 CYS L 546 SG 85.1 120.2 174.8
REMARK 620 5 CYS L 549 SG 107.8 55.1 77.7 97.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FNE L1004 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 84 SG
REMARK 620 2 FNE L1004 NI 54.5
REMARK 620 3 FNE L1004 C1 162.4 107.9
REMARK 620 4 FNE L1004 C2 93.9 112.8 92.8
REMARK 620 5 FNE L1004 C3 99.7 146.8 96.9 86.9
REMARK 620 6 CYS L 549 SG 78.9 57.9 92.4 170.5 100.4
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 MG L 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 S 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 S 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S S 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FNE L 1004
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UBH RELATED DB: PDB
REMARK 900 1UBH CONTAINS DATA WAS COLLECTED BY CO ATMOSPHERE IN THE DARK
REMARK 900 CONDITION AT 1.35 ANGSTROM
REMARK 900 RELATED ID: 1UBJ RELATED DB: PDB
REMARK 900 1UBJ CONTAINS DATA WAS COLLECTED BY HYDROGEN ATMOSPHERE IN THE DARK
REMARK 900 CONDITION
REMARK 900 RELATED ID: 1UBK RELATED DB: PDB
REMARK 900 1UBK CONTAINS DATA WAS COLLECTED BY CO ATMOSPHERE IN THE DARK
REMARK 900 CONDITION AT 1.9 ANGSTROM
REMARK 900 RELATED ID: 1UBL RELATED DB: PDB
REMARK 900 1UBL CONTAINS DATA WAS COLLECTED BY CO ATMOSPHERE IN THE WEAK LIGHT
REMARK 900 AT 1.20 ANGSTROM
REMARK 900 RELATED ID: 1UBM RELATED DB: PDB
REMARK 900 1UBM CONTAINS DATA WAS COLLECTED BY CO ATMOSPHERE IN THE STRONG
REMARK 900 LIGHT AT 1.50 ANGSTROM
REMARK 900 RELATED ID: 1UBO RELATED DB: PDB
REMARK 900 1UBO CONTAINS DATA WAS COLLECTED BY CO ATMOSPHERE IN THE DARK.
REMARK 900 RELATED ID: 1UBR RELATED DB: PDB
REMARK 900 1UBR CONTAINS DATA WAS COLLECTED BY CO ATMOSPHERE IN THE WEAK LIGHT
REMARK 900 AT 1.34 ANGSTROM
REMARK 900 RELATED ID: 1UBT RELATED DB: PDB
REMARK 900 1UBT CONTAINS DATA WAS COLLECTED BY CO ATMOSPHERE IN THE STRONG
REMARK 900 LIGHT AT 1.34 ANGSTROM
DBREF 1UBU S 1 267 UNP P21853 PHNS_DESVM 51 317
DBREF 1UBU L 19 552 UNP P21852 PHNL_DESVM 19 552
SEQADV 1UBU LYS L 514 UNP P21852 ASN 514 SEE REMARK 999
SEQADV 1UBU LEU L 515 UNP P21852 VAL 515 SEE REMARK 999
SEQRES 1 S 267 LEU MET GLY PRO ARG ARG PRO SER VAL VAL TYR LEU HIS
SEQRES 2 S 267 ASN ALA GLU CYS THR GLY CYS SER GLU SER VAL LEU ARG
SEQRES 3 S 267 ALA PHE GLU PRO TYR ILE ASP THR LEU ILE LEU ASP THR
SEQRES 4 S 267 LEU SER LEU ASP TYR HIS GLU THR ILE MET ALA ALA ALA
SEQRES 5 S 267 GLY ASP ALA ALA GLU ALA ALA LEU GLU GLN ALA VAL ASN
SEQRES 6 S 267 SER PRO HIS GLY PHE ILE ALA VAL VAL GLU GLY GLY ILE
SEQRES 7 S 267 PRO THR ALA ALA ASN GLY ILE TYR GLY LYS VAL ALA ASN
SEQRES 8 S 267 HIS THR MET LEU ASP ILE CYS SER ARG ILE LEU PRO LYS
SEQRES 9 S 267 ALA GLN ALA VAL ILE ALA TYR GLY THR CYS ALA THR PHE
SEQRES 10 S 267 GLY GLY VAL GLN ALA ALA LYS PRO ASN PRO THR GLY ALA
SEQRES 11 S 267 LYS GLY VAL ASN ASP ALA LEU LYS HIS LEU GLY VAL LYS
SEQRES 12 S 267 ALA ILE ASN ILE ALA GLY CYS PRO PRO ASN PRO TYR ASN
SEQRES 13 S 267 LEU VAL GLY THR ILE VAL TYR TYR LEU LYS ASN LYS ALA
SEQRES 14 S 267 ALA PRO GLU LEU ASP SER LEU ASN ARG PRO THR MET PHE
SEQRES 15 S 267 PHE GLY GLN THR VAL HIS GLU GLN CYS PRO ARG LEU PRO
SEQRES 16 S 267 HIS PHE ASP ALA GLY GLU PHE ALA PRO SER PHE GLU SER
SEQRES 17 S 267 GLU GLU ALA ARG LYS GLY TRP CYS LEU TYR GLU LEU GLY
SEQRES 18 S 267 CYS LYS GLY PRO VAL THR MET ASN ASN CYS PRO LYS ILE
SEQRES 19 S 267 LYS PHE ASN GLN THR ASN TRP PRO VAL ASP ALA GLY HIS
SEQRES 20 S 267 PRO CYS ILE GLY CYS SER GLU PRO ASP PHE TRP ASP ALA
SEQRES 21 S 267 MET THR PRO PHE TYR GLN ASN
SEQRES 1 L 534 SER SER TYR SER GLY PRO ILE VAL VAL ASP PRO VAL THR
SEQRES 2 L 534 ARG ILE GLU GLY HIS LEU ARG ILE GLU VAL GLU VAL GLU
SEQRES 3 L 534 ASN GLY LYS VAL LYS ASN ALA TYR SER SER SER THR LEU
SEQRES 4 L 534 PHE ARG GLY LEU GLU ILE ILE LEU LYS GLY ARG ASP PRO
SEQRES 5 L 534 ARG ASP ALA GLN HIS PHE THR GLN ARG THR CYS GLY VAL
SEQRES 6 L 534 CYS THR TYR THR HIS ALA LEU ALA SER THR ARG CYS VAL
SEQRES 7 L 534 ASP ASN ALA VAL GLY VAL HIS ILE PRO LYS ASN ALA THR
SEQRES 8 L 534 TYR ILE ARG ASN LEU VAL LEU GLY ALA GLN TYR LEU HIS
SEQRES 9 L 534 ASP HIS ILE VAL HIS PHE TYR HIS LEU HIS ALA LEU ASP
SEQRES 10 L 534 PHE VAL ASP VAL THR ALA ALA LEU LYS ALA ASP PRO ALA
SEQRES 11 L 534 LYS ALA ALA LYS VAL ALA SER SER ILE SER PRO ARG LYS
SEQRES 12 L 534 THR THR ALA ALA ASP LEU LYS ALA VAL GLN ASP LYS LEU
SEQRES 13 L 534 LYS THR PHE VAL GLU THR GLY GLN LEU GLY PRO PHE THR
SEQRES 14 L 534 ASN ALA TYR PHE LEU GLY GLY HIS PRO ALA TYR TYR LEU
SEQRES 15 L 534 ASP PRO GLU THR ASN LEU ILE ALA THR ALA HIS TYR LEU
SEQRES 16 L 534 GLU ALA LEU ARG LEU GLN VAL LYS ALA ALA ARG ALA MET
SEQRES 17 L 534 ALA VAL PHE GLY ALA LYS ASN PRO HIS THR GLN PHE THR
SEQRES 18 L 534 VAL VAL GLY GLY VAL THR CYS TYR ASP ALA LEU THR PRO
SEQRES 19 L 534 GLN ARG ILE ALA GLU PHE GLU ALA LEU TRP LYS GLU THR
SEQRES 20 L 534 LYS ALA PHE VAL ASP GLU VAL TYR ILE PRO ASP LEU LEU
SEQRES 21 L 534 VAL VAL ALA ALA ALA TYR LYS ASP TRP THR GLN TYR GLY
SEQRES 22 L 534 GLY THR ASP ASN PHE ILE THR PHE GLY GLU PHE PRO LYS
SEQRES 23 L 534 ASP GLU TYR ASP LEU ASN SER ARG PHE PHE LYS PRO GLY
SEQRES 24 L 534 VAL VAL PHE LYS ARG ASP PHE LYS ASN ILE LYS PRO PHE
SEQRES 25 L 534 ASP LYS MET GLN ILE GLU GLU HIS VAL ARG HIS SER TRP
SEQRES 26 L 534 TYR GLU GLY ALA GLU ALA ARG HIS PRO TRP LYS GLY GLN
SEQRES 27 L 534 THR GLN PRO LYS TYR THR ASP LEU HIS GLY ASP ASP ARG
SEQRES 28 L 534 TYR SER TRP MET LYS ALA PRO ARG TYR MET GLY GLU PRO
SEQRES 29 L 534 MET GLU THR GLY PRO LEU ALA GLN VAL LEU ILE ALA TYR
SEQRES 30 L 534 SER GLN GLY HIS PRO LYS VAL LYS ALA VAL THR ASP ALA
SEQRES 31 L 534 VAL LEU ALA LYS LEU GLY VAL GLY PRO GLU ALA LEU PHE
SEQRES 32 L 534 SER THR LEU GLY ARG THR ALA ALA ARG GLY ILE GLU THR
SEQRES 33 L 534 ALA VAL ILE ALA GLU TYR VAL GLY VAL MET LEU GLN GLU
SEQRES 34 L 534 TYR LYS ASP ASN ILE ALA LYS GLY ASP ASN VAL ILE CYS
SEQRES 35 L 534 ALA PRO TRP GLU MET PRO LYS GLN ALA GLU GLY VAL GLY
SEQRES 36 L 534 PHE VAL ASN ALA PRO ARG GLY GLY LEU SER HIS TRP ILE
SEQRES 37 L 534 ARG ILE GLU ASP GLY LYS ILE GLY ASN PHE GLN LEU VAL
SEQRES 38 L 534 VAL PRO SER THR TRP THR LEU GLY PRO ARG CYS ASP LYS
SEQRES 39 L 534 ASN LYS LEU SER PRO VAL GLU ALA SER LEU ILE GLY THR
SEQRES 40 L 534 PRO VAL ALA ASP ALA LYS ARG PRO VAL GLU ILE LEU ARG
SEQRES 41 L 534 THR VAL HIS SER PHE ASP PRO CYS ILE ALA CYS GLY VAL
SEQRES 42 L 534 HIS
HET SF4 S1001 8
HET SF4 S1002 8
HET F3S S1003 7
HET MG L1005 1
HET FNE L1004 8
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM F3S FE3-S4 CLUSTER
HETNAM MG MAGNESIUM ION
HETNAM FNE (MU-SULPHIDO)-BIS(MU-CYS,S)-[TRICARBONYLIRON-DI-(CYS,
HETNAM 2 FNE S)NICKEL(II)](FE-NI)
FORMUL 3 SF4 2(FE4 S4)
FORMUL 5 F3S FE3 S4
FORMUL 6 MG MG 2+
FORMUL 7 FNE C3 FE NI O3 S
FORMUL 8 HOH *929(H2 O)
HELIX 1 1 THR S 18 ARG S 26 1 9
HELIX 2 2 TYR S 31 ASP S 38 1 8
HELIX 3 3 ALA S 52 ASN S 65 1 14
HELIX 4 4 ALA S 81 ILE S 85 5 5
HELIX 5 5 MET S 94 LEU S 102 1 9
HELIX 6 6 PRO S 103 ALA S 105 5 3
HELIX 7 7 GLY S 112 GLY S 118 1 7
HELIX 8 8 GLY S 119 ALA S 123 5 5
HELIX 9 9 GLY S 132 LYS S 138 1 7
HELIX 10 10 HIS S 139 GLY S 141 5 3
HELIX 11 11 ASN S 153 LYS S 168 1 16
HELIX 12 12 PRO S 179 GLY S 184 1 6
HELIX 13 13 VAL S 187 CYS S 191 5 5
HELIX 14 14 ARG S 193 ALA S 199 1 7
HELIX 15 15 SER S 208 LYS S 213 1 6
HELIX 16 16 LEU S 217 GLY S 221 5 5
HELIX 17 17 LYS S 223 THR S 227 5 5
HELIX 18 18 ASN S 230 LYS S 235 1 6
HELIX 19 19 PRO S 242 GLY S 246 5 5
HELIX 20 20 ASP S 256 MET S 261 1 6
HELIX 21 21 GLY L 60 LYS L 66 1 7
HELIX 22 22 ASP L 69 ARG L 71 5 3
HELIX 23 23 ASP L 72 ARG L 79 1 8
HELIX 24 24 TYR L 86 GLY L 101 1 16
HELIX 25 25 PRO L 105 LEU L 131 1 27
HELIX 26 26 HIS L 132 PHE L 136 5 5
HELIX 27 27 VAL L 139 ALA L 145 5 7
HELIX 28 28 ASP L 146 SER L 158 1 13
HELIX 29 29 THR L 163 THR L 180 1 18
HELIX 30 30 LEU L 183 THR L 187 5 5
HELIX 31 31 ASP L 201 ALA L 231 1 31
HELIX 32 32 CYS L 246 LEU L 250 5 5
HELIX 33 33 THR L 251 VAL L 272 1 22
HELIX 34 34 VAL L 272 TYR L 284 1 13
HELIX 35 35 LYS L 285 TYR L 290 5 6
HELIX 36 36 ASP L 308 ASN L 310 5 3
HELIX 37 37 ASP L 331 MET L 333 5 3
HELIX 38 38 HIS L 351 GLY L 355 5 5
HELIX 39 39 HIS L 365 ARG L 369 5 5
HELIX 40 40 GLY L 386 GLN L 397 1 12
HELIX 41 41 HIS L 399 GLY L 414 1 16
HELIX 42 42 GLY L 416 PHE L 421 5 6
HELIX 43 43 SER L 422 LYS L 454 1 33
HELIX 44 44 VAL L 500 GLY L 507 1 8
HELIX 45 45 SER L 516 ILE L 523 1 8
HELIX 46 46 PRO L 533 PHE L 543 1 11
HELIX 47 47 CYS L 546 HIS L 552 1 7
SHEET 1 A 5 SER S 41 TYR S 44 0
SHEET 2 A 5 SER S 8 HIS S 13 1 N VAL S 9 O SER S 41
SHEET 3 A 5 ILE S 71 GLU S 75 1 O GLU S 75 N LEU S 12
SHEET 4 A 5 ALA S 107 TYR S 111 1 O TYR S 111 N VAL S 74
SHEET 5 A 5 ILE S 145 ILE S 147 1 O ILE S 147 N ALA S 110
SHEET 1 B 2 ILE S 78 PRO S 79 0
SHEET 2 B 2 ALA S 130 LYS S 131 -1 O LYS S 131 N ILE S 78
SHEET 1 C 2 LYS S 88 VAL S 89 0
SHEET 2 C 2 HIS S 92 THR S 93 -1 O HIS S 92 N VAL S 89
SHEET 1 D 3 GLY L 23 VAL L 27 0
SHEET 2 D 3 LEU L 37 GLU L 44 -1 O VAL L 43 N GLY L 23
SHEET 3 D 3 LYS L 47 SER L 55 -1 O SER L 54 N ARG L 38
SHEET 1 E 2 THR L 239 VAL L 240 0
SHEET 2 E 2 GLY L 243 VAL L 244 -1 O GLY L 243 N VAL L 240
SHEET 1 F 2 PHE L 296 THR L 298 0
SHEET 2 F 2 GLY L 317 VAL L 319 -1 O VAL L 319 N PHE L 296
SHEET 1 G 2 GLU L 301 PRO L 303 0
SHEET 2 G 2 ARG L 312 PHE L 314 -1 O PHE L 314 N GLU L 301
SHEET 1 H 2 ILE L 335 HIS L 338 0
SHEET 2 H 2 ALA L 375 TYR L 378 -1 O ARG L 377 N GLU L 336
SHEET 1 I 3 ALA L 469 ALA L 477 0
SHEET 2 I 3 GLY L 480 GLU L 489 -1 O LEU L 482 N VAL L 475
SHEET 3 I 3 LYS L 492 VAL L 499 -1 O ASN L 495 N ARG L 487
SSBOND 1 CYS L 84 CYS L 549 1555 1555 2.92
LINK SG CYS S 17 FE1 SF4 S1001 1555 1555 2.29
LINK SG CYS S 20 FE4 SF4 S1001 1555 1555 2.27
LINK SG CYS S 114 FE2 SF4 S1001 1555 1555 2.22
LINK SG CYS S 150 FE3 SF4 S1001 1555 1555 2.30
LINK ND1 HIS S 188 FE1 SF4 S1002 1555 1555 2.06
LINK SG CYS S 191 FE3 SF4 S1002 1555 1555 2.31
LINK SG CYS S 216 FE4 SF4 S1002 1555 1555 2.30
LINK SG CYS S 222 FE2 SF4 S1002 1555 1555 2.32
LINK SG CYS S 231 FE3 F3S S1003 1555 1555 2.29
LINK SG CYS S 249 FE1 F3S S1003 1555 1555 2.33
LINK SG CYS S 252 FE4 F3S S1003 1555 1555 2.30
LINK OE2 GLU L 62 MG MG L1005 1555 1555 2.13
LINK SG CYS L 81 NI FNE L1004 1555 1555 2.27
LINK SG CYS L 84 NI FNE L1004 1555 1555 2.26
LINK SG CYS L 84 FE FNE L1004 1555 1555 2.28
LINK O LEU L 498 MG MG L1005 1555 1555 2.16
LINK SG CYS L 546 NI FNE L1004 1555 1555 2.24
LINK SG CYS L 549 NI FNE L1004 1555 1555 2.40
LINK SG CYS L 549 FE FNE L1004 1555 1555 2.32
LINK NE2 HIS L 552 MG MG L1005 1555 1555 2.15
LINK MG MG L1005 O HOH L3001 1555 1555 2.05
LINK MG MG L1005 O HOH L3002 1555 1555 2.08
LINK MG MG L1005 O HOH L3003 1555 1555 2.08
CISPEP 1 GLU S 29 PRO S 30 0 5.17
CISPEP 2 LYS S 124 PRO S 125 0 0.23
CISPEP 3 CYS S 150 PRO S 151 0 -1.80
CISPEP 4 THR S 262 PRO S 263 0 -5.03
CISPEP 5 ASP L 28 PRO L 29 0 7.83
CISPEP 6 ASN L 233 PRO L 234 0 -3.16
SITE 1 AC1 6 GLU L 62 LEU L 498 HIS L 552 HOH L3001
SITE 2 AC1 6 HOH L3002 HOH L3003
SITE 1 AC2 10 ARG L 79 HIS L 235 GLU S 16 CYS S 17
SITE 2 AC2 10 CYS S 20 THR S 113 CYS S 114 GLY S 149
SITE 3 AC2 10 CYS S 150 PRO S 151
SITE 1 AC3 7 HIS S 188 CYS S 191 ARG S 193 LEU S 194
SITE 2 AC3 7 CYS S 216 LEU S 217 CYS S 222
SITE 1 AC4 10 GLN L 237 THR S 227 ASN S 229 CYS S 231
SITE 2 AC4 10 PHE S 236 TRP S 241 PRO S 242 CYS S 249
SITE 3 AC4 10 ILE S 250 CYS S 252
SITE 1 AC5 12 CYS L 81 CYS L 84 HIS L 88 ALA L 477
SITE 2 AC5 12 PRO L 478 ARG L 479 LEU L 482 VAL L 500
SITE 3 AC5 12 PRO L 501 SER L 502 CYS L 546 CYS L 549
CRYST1 98.010 126.020 66.570 90.00 90.00 90.00 P 21 21 21 4
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 0.010203 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007935 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015022 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
