HEADER ELECTRON TRANSPORT 02-MAR-04 1SIZ
TITLE CRYSTAL STRUCTURE OF THE [FE3S4]-FERREDOXIN FROM THE HYPERTHERMOPHILIC
TITLE 2 ARCHAEON PYROCOCCUS FURIOSUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERREDOXIN;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261;
SOURCE 4 GENE: FDXA, PF1909;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS THERMOSTABILITY, IRON-SULFUR CLUSTERS, DIMER, ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.S.NIELSEN,P.HARRIS,H.E.M.CHRISTENSEN
REVDAT 3 23-AUG-23 1SIZ 1 REMARK LINK
REVDAT 2 24-FEB-09 1SIZ 1 VERSN
REVDAT 1 25-MAY-04 1SIZ 0
JRNL AUTH M.S.NIELSEN,P.HARRIS,B.L.OOI,H.E.M.CHRISTENSEN
JRNL TITL THE 1.5 A RESOLUTION CRYSTAL STRUCTURE OF [FE3S4]-FERREDOXIN
JRNL TITL 2 FROM THE HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS FURIOSUS
JRNL REF BIOCHEMISTRY V. 43 5188 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15122884
JRNL DOI 10.1021/BI049942X
REMARK 2
REMARK 2 RESOLUTION. 2.25 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 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 6508
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) : 0.239
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 337
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 992
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 46
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
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 : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 0.020 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 0.405 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.480 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.951 ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SIZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021744.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
REMARK 200 MONOCHROMATOR : SILICIUM
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6508
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.22000
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: PDB ENTRY 1VJW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, HEXAMMINE COBALT(III)-IONS,
REMARK 280 HEPES, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 23.72350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 27.27450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.81850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 27.27450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.72350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.81850
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS EITHER THE DIMER IN THE
REMARK 300 ASYMMETRIC UNIT OR A MONOMER
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 APPLY THE FOLLOWING TO CHAINS: A, 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: 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 CYS A 21 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500 CYS A 48 CA - CB - SG ANGL. DEV. = 11.3 DEGREES
REMARK 500 CYS C 48 CA - CB - SG ANGL. DEV. = 11.0 DEGREES
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 F3S A 70 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 F3S A 70 S1 103.1
REMARK 620 3 F3S A 70 S2 111.8 108.5
REMARK 620 4 F3S A 70 S3 123.4 104.6 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S A 70 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 17 SG
REMARK 620 2 F3S A 70 S1 111.0
REMARK 620 3 F3S A 70 S3 114.2 101.8
REMARK 620 4 F3S A 70 S4 117.7 109.3 101.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S A 70 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 56 SG
REMARK 620 2 F3S A 70 S2 112.7
REMARK 620 3 F3S A 70 S3 111.1 104.9
REMARK 620 4 F3S A 70 S4 120.1 103.2 103.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S C 71 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 11 SG
REMARK 620 2 F3S C 71 S1 103.8
REMARK 620 3 F3S C 71 S2 108.9 108.6
REMARK 620 4 F3S C 71 S3 126.3 103.7 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S C 71 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 17 SG
REMARK 620 2 F3S C 71 S1 111.5
REMARK 620 3 F3S C 71 S3 108.3 100.7
REMARK 620 4 F3S C 71 S4 121.5 111.0 101.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S C 71 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 56 SG
REMARK 620 2 F3S C 71 S2 111.9
REMARK 620 3 F3S C 71 S3 115.9 106.3
REMARK 620 4 F3S C 71 S4 116.7 100.6 103.8
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 3CO A 74
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3CO C 75
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S A 70
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S C 71
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SJ1 RELATED DB: PDB
REMARK 900 THE 1.5 A RESOLUTION CRYSTAL STRUCTURE OF [FE3S4]-FERREDOXIN FROM
REMARK 900 THE HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS FURIOSUS
DBREF 1SIZ A 1 66 UNP P29603 FER_PYRFU 1 66
DBREF 1SIZ C 1 66 UNP P29603 FER_PYRFU 1 66
SEQRES 1 A 66 ALA TRP LYS VAL SER VAL ASP GLN ASP THR CYS ILE GLY
SEQRES 2 A 66 ASP ALA ILE CYS ALA SER LEU CYS PRO ASP VAL PHE GLU
SEQRES 3 A 66 MET ASN ASP GLU GLY LYS ALA GLN PRO LYS VAL GLU VAL
SEQRES 4 A 66 ILE GLU ASP GLU GLU LEU TYR ASN CYS ALA LYS GLU ALA
SEQRES 5 A 66 MET GLU ALA CYS PRO VAL SER ALA ILE THR ILE GLU GLU
SEQRES 6 A 66 ALA
SEQRES 1 C 66 ALA TRP LYS VAL SER VAL ASP GLN ASP THR CYS ILE GLY
SEQRES 2 C 66 ASP ALA ILE CYS ALA SER LEU CYS PRO ASP VAL PHE GLU
SEQRES 3 C 66 MET ASN ASP GLU GLY LYS ALA GLN PRO LYS VAL GLU VAL
SEQRES 4 C 66 ILE GLU ASP GLU GLU LEU TYR ASN CYS ALA LYS GLU ALA
SEQRES 5 C 66 MET GLU ALA CYS PRO VAL SER ALA ILE THR ILE GLU GLU
SEQRES 6 C 66 ALA
HET 3CO A 72 1
HET 3CO A 74 1
HET F3S A 70 7
HET 3CO C 73 1
HET 3CO C 75 1
HET F3S C 71 7
HETNAM 3CO COBALT (III) ION
HETNAM F3S FE3-S4 CLUSTER
FORMUL 3 3CO 4(CO 3+)
FORMUL 5 F3S 2(FE3 S4)
FORMUL 9 HOH *46(H2 O)
HELIX 1 1 ALA A 15 CYS A 21 1 7
HELIX 2 2 ASP A 42 CYS A 56 1 15
HELIX 3 3 ALA C 15 CYS C 21 1 7
HELIX 4 4 ASP C 42 CYS C 56 1 15
SHEET 1 A 4 TRP A 2 VAL A 6 0
SHEET 2 A 4 ILE A 61 GLU A 65 -1 O GLU A 64 N LYS A 3
SHEET 3 A 4 ILE C 61 GLU C 65 -1 O ILE C 63 N GLU A 65
SHEET 4 A 4 TRP C 2 VAL C 6 -1 N LYS C 3 O GLU C 64
SHEET 1 B 2 PHE A 25 MET A 27 0
SHEET 2 B 2 ALA A 33 PRO A 35 -1 O GLN A 34 N GLU A 26
SHEET 1 C 2 PHE C 25 MET C 27 0
SHEET 2 C 2 ALA C 33 PRO C 35 -1 O GLN C 34 N GLU C 26
SSBOND 1 CYS A 21 CYS A 48 1555 1555 2.04
SSBOND 2 CYS C 21 CYS C 48 1555 1555 2.04
LINK SG CYS A 11 FE1 F3S A 70 1555 1555 2.42
LINK SG CYS A 17 FE3 F3S A 70 1555 1555 2.23
LINK SG CYS A 56 FE4 F3S A 70 1555 1555 2.26
LINK CO 3CO A 74 O HOH A 104 1555 1555 2.45
LINK SG CYS C 11 FE1 F3S C 71 1555 1555 2.66
LINK SG CYS C 17 FE3 F3S C 71 1555 1555 2.24
LINK SG CYS C 56 FE4 F3S C 71 1555 1555 2.34
LINK CO 3CO C 75 O HOH C 87 1555 1555 2.04
SITE 1 AC1 2 HOH A 104 ILE C 12
SITE 1 AC2 2 ILE A 12 HOH C 87
SITE 1 AC3 8 CYS A 11 ILE A 12 ASP A 14 ALA A 15
SITE 2 AC3 8 ILE A 16 CYS A 17 ALA A 33 CYS A 56
SITE 1 AC4 8 CYS C 11 ILE C 12 ASP C 14 ALA C 15
SITE 2 AC4 8 ILE C 16 CYS C 17 ALA C 33 CYS C 56
CRYST1 47.447 51.637 54.549 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.021076 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019366 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018332 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
