HEADER METAL BINDING PROTEIN 07-JAN-14 2MJD
TITLE OXIDIZED YEAST ADRENODOXIN HOMOLOG 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADRENODOXIN HOMOLOG, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 58-172;
COMPND 5 SYNONYM: MITOCHONDRIAL FERREDOXIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: YAH1, YPL252C;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETDUET-1
KEYWDS FERREDOXIN, IRON SULFUR ASSEMBLY, PARAMAGNETIC PROTEIN, 2FE2S
KEYWDS 2 CLUSTER, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR A.GALLO,L.BANCI
REVDAT 2 14-JUN-23 2MJD 1 REMARK LINK
REVDAT 1 19-NOV-14 2MJD 0
JRNL AUTH H.WEBERT,S.A.FREIBERT,A.GALLO,T.HEIDENREICH,U.LINNE,
JRNL AUTH 2 S.AMLACHER,E.HURT,U.MUHLENHOFF,L.BANCI,R.LILL
JRNL TITL FUNCTIONAL RECONSTITUTION OF MITOCHONDRIAL FE/S CLUSTER
JRNL TITL 2 SYNTHESIS ON ISU1 REVEALS THE INVOLVEMENT OF FERREDOXIN.
JRNL REF NAT COMMUN V. 5 5013 2014
JRNL REFN ESSN 2041-1723
JRNL PMID 25358379
JRNL DOI 10.1038/NCOMMS6013
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TOPSPIN TOPSPIN-2.1, AMBER AMBER 11
REMARK 3 AUTHORS : BRUKER BIOSPIN (TOPSPIN), CASE, DARDEN, CHEATHAM,
REMARK 3 III, SIMMERLING, WANG, DUKE, LUO, ... AND KOLLMAN
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2MJD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000103683.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 50
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM [U-100% 15N] PROTEIN, 50 MM
REMARK 210 POTASSIUM PHOSPHATE, 90% H2O/10%
REMARK 210 D2O; 1 MM [U-13C; U-15N] PROTEIN,
REMARK 210 50 MM POTASSIUM PHOSPHATE, 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D CBCA(CO)NH; 3D HNCACB; 3D
REMARK 210 HBHA(CO)NH; 3D HNCO; 3D HN(CO)CA;
REMARK 210 3D HCCH-TOCSY; 3D 1H-15N NOESY;
REMARK 210 3D 1H-13C NOESY; 2D 1H-1H NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 500 MHZ; 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CARA CARA 2, CYANA CYANA-2.1
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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
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 2 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 3 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 4 TYR A 59 CB - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500 4 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ARG A 99 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 5 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 5 ARG A 99 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 7 CYS A 47 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 7 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 7 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 8 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 9 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 9 ARG A 99 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 9 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 10 ARG A 99 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 10 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 11 ARG A 99 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 12 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 12 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 13 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 13 ARG A 99 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 13 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 15 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 16 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 17 ARG A 99 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 17 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 18 ARG A 99 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 18 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 20 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 20 ARG A 107 NE - CZ - NH1 ANGL. DEV. = 3.2 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 1 GLU A 3 147.85 52.81
REMARK 500 1 CYS A 45 -136.09 -133.82
REMARK 500 1 SER A 48 -157.66 -149.07
REMARK 500 1 CYS A 50 -45.82 57.46
REMARK 500 1 ASP A 96 83.24 -53.33
REMARK 500 1 ILE A 98 151.39 -47.92
REMARK 500 1 THR A 106 119.65 -163.44
REMARK 500 2 CYS A 41 -137.48 -157.07
REMARK 500 2 CYS A 47 154.68 60.59
REMARK 500 2 ASP A 96 91.28 -62.20
REMARK 500 3 GLU A 3 -28.52 -148.46
REMARK 500 3 CYS A 47 -179.82 62.79
REMARK 500 3 SER A 48 -158.61 -149.90
REMARK 500 3 THR A 49 5.82 -64.90
REMARK 500 3 CYS A 50 -53.88 61.86
REMARK 500 3 LEU A 73 -60.34 -91.42
REMARK 500 3 GLN A 88 33.74 -83.53
REMARK 500 3 ASP A 96 86.21 -67.97
REMARK 500 3 ARG A 107 167.08 -44.87
REMARK 500 4 CYS A 41 -154.99 -170.03
REMARK 500 4 CYS A 47 163.42 59.89
REMARK 500 4 CYS A 50 72.83 44.08
REMARK 500 4 ASP A 96 86.97 -69.33
REMARK 500 4 LEU A 102 75.57 -117.89
REMARK 500 4 ASN A 111 55.01 -140.20
REMARK 500 5 GLU A 2 28.44 -149.73
REMARK 500 5 CYS A 47 142.97 57.57
REMARK 500 5 ASP A 96 80.42 -64.20
REMARK 500 6 CYS A 41 -153.43 55.84
REMARK 500 6 CYS A 45 -176.62 56.21
REMARK 500 6 CYS A 47 171.36 66.56
REMARK 500 6 SER A 48 -169.50 -55.14
REMARK 500 6 CYS A 50 8.07 56.15
REMARK 500 6 SER A 92 -174.71 -172.12
REMARK 500 6 ASP A 96 84.97 -62.36
REMARK 500 6 ASN A 108 -35.40 -166.25
REMARK 500 6 VAL A 109 138.70 65.64
REMARK 500 7 GLU A 2 -16.12 -159.95
REMARK 500 7 ASP A 36 97.48 -69.81
REMARK 500 7 SER A 44 20.99 -151.18
REMARK 500 7 SER A 48 -160.08 -161.50
REMARK 500 7 CYS A 50 -44.53 56.02
REMARK 500 7 ASP A 74 -13.97 -47.96
REMARK 500 7 CYS A 87 -50.43 54.66
REMARK 500 7 ASP A 96 86.35 -63.27
REMARK 500 7 MET A 105 79.72 -105.62
REMARK 500 7 THR A 106 -65.51 58.51
REMARK 500 8 CYS A 41 -137.55 -165.78
REMARK 500 8 CYS A 45 -131.88 53.52
REMARK 500 8 CYS A 47 164.43 59.25
REMARK 500
REMARK 500 THIS ENTRY HAS 140 RAMACHANDRAN OUTLIERS.
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 46 CYS A 47 1 144.28
REMARK 500 CYS A 47 SER A 48 1 -123.20
REMARK 500 GLY A 86 CYS A 87 1 -139.32
REMARK 500 CYS A 50 HIS A 51 3 -102.93
REMARK 500 ALA A 101 LEU A 102 3 -143.51
REMARK 500 TYR A 59 ASP A 60 4 -149.77
REMARK 500 GLY A 86 CYS A 87 7 135.92
REMARK 500 LYS A 16 THR A 17 11 -149.15
REMARK 500 THR A 17 TYR A 18 11 -149.67
REMARK 500 CYS A 47 SER A 48 11 -147.46
REMARK 500 SER A 44 CYS A 45 12 -146.99
REMARK 500 ARG A 84 LEU A 85 12 -72.36
REMARK 500 MET A 105 THR A 106 12 -146.11
REMARK 500 LEU A 102 PRO A 103 13 -146.79
REMARK 500 LEU A 85 GLY A 86 15 -124.41
REMARK 500 CYS A 87 GLN A 88 15 -148.45
REMARK 500 TYR A 58 TYR A 59 16 149.26
REMARK 500 ARG A 84 LEU A 85 16 -143.61
REMARK 500 CYS A 50 HIS A 51 17 -137.39
REMARK 500 GLU A 38 GLY A 39 18 -146.68
REMARK 500 CYS A 50 HIS A 51 18 -146.38
REMARK 500 GLY A 86 CYS A 87 20 -149.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 84 0.10 SIDE CHAIN
REMARK 500 3 TYR A 77 0.06 SIDE CHAIN
REMARK 500 3 ARG A 84 0.12 SIDE CHAIN
REMARK 500 6 TYR A 59 0.07 SIDE CHAIN
REMARK 500 6 ARG A 107 0.08 SIDE CHAIN
REMARK 500 7 TYR A 59 0.09 SIDE CHAIN
REMARK 500 7 ARG A 84 0.09 SIDE CHAIN
REMARK 500 8 ARG A 84 0.19 SIDE CHAIN
REMARK 500 11 TYR A 59 0.07 SIDE CHAIN
REMARK 500 11 ARG A 84 0.11 SIDE CHAIN
REMARK 500 17 ARG A 84 0.10 SIDE CHAIN
REMARK 500 19 ARG A 99 0.11 SIDE CHAIN
REMARK 500 20 TYR A 59 0.08 SIDE CHAIN
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 201 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 41 SG
REMARK 620 2 FES A 201 S1 112.5
REMARK 620 3 FES A 201 S2 99.1 111.5
REMARK 620 4 CYS A 47 SG 99.4 110.4 122.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 201 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 50 SG
REMARK 620 2 FES A 201 S1 111.3
REMARK 620 3 FES A 201 S2 108.9 111.0
REMARK 620 4 CYS A 87 SG 105.2 116.1 103.7
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 FES A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2MJE RELATED DB: PDB
REMARK 900 RELATED ID: 19717 RELATED DB: BMRB
DBREF 2MJD A 1 115 UNP Q12184 ADRX_YEAST 58 172
SEQRES 1 A 115 GLY GLU GLU LEU LYS ILE THR PHE ILE LEU LYS ASP GLY
SEQRES 2 A 115 SER GLN LYS THR TYR GLU VAL CYS GLU GLY GLU THR ILE
SEQRES 3 A 115 LEU ASP ILE ALA GLN GLY HIS ASN LEU ASP MET GLU GLY
SEQRES 4 A 115 ALA CYS GLY GLY SER CYS ALA CYS SER THR CYS HIS VAL
SEQRES 5 A 115 ILE VAL ASP PRO ASP TYR TYR ASP ALA LEU PRO GLU PRO
SEQRES 6 A 115 GLU ASP ASP GLU ASN ASP MET LEU ASP LEU ALA TYR GLY
SEQRES 7 A 115 LEU THR GLU THR SER ARG LEU GLY CYS GLN ILE LYS MET
SEQRES 8 A 115 SER LYS ASP ILE ASP GLY ILE ARG VAL ALA LEU PRO GLN
SEQRES 9 A 115 MET THR ARG ASN VAL ASN ASN ASN ASP PHE SER
HET FES A 201 4
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
FORMUL 2 FES FE2 S2
HELIX 1 1 THR A 25 ASN A 34 1 10
HELIX 2 2 ASN A 70 LEU A 75 1 6
SHEET 1 A 5 GLN A 15 VAL A 20 0
SHEET 2 A 5 LEU A 4 ILE A 9 -1 N PHE A 8 O LYS A 16
SHEET 3 A 5 ARG A 99 ALA A 101 1 O VAL A 100 N THR A 7
SHEET 4 A 5 HIS A 51 VAL A 54 -1 N ILE A 53 O ALA A 101
SHEET 5 A 5 SER A 83 LEU A 85 -1 O ARG A 84 N VAL A 52
LINK SG CYS A 41 FE1 FES A 201 1555 1555 2.29
LINK SG CYS A 47 FE1 FES A 201 1555 1555 2.28
LINK SG CYS A 50 FE2 FES A 201 1555 1555 2.29
LINK SG CYS A 87 FE2 FES A 201 1555 1555 2.28
SITE 1 AC1 6 CYS A 41 CYS A 47 SER A 48 CYS A 50
SITE 2 AC1 6 MET A 72 CYS A 87
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
