Header list of 1clf.pdb file
Complete list - 16 20 Bytes
HEADER ELECTRON TRANSFER (IRON-SULFUR PROTEIN) 21-JUN-95 1CLF
TITLE CLOSTRIDIUM PASTEURIANUM FERREDOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERREDOXIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PASTEURIANUM;
SOURCE 3 ORGANISM_TAXID: 1501;
SOURCE 4 STRAIN: WINOGRADSKY;
SOURCE 5 ATCC: 6013
KEYWDS ELECTRON TRANSFER (IRON-SULFUR PROTEIN)
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR I.BERTINI,A.DONAIRE,B.A.FEINBERG,C.LUCHINAT,M.PICCIOLI,H.YUAN
REVDAT 4 16-FEB-22 1CLF 1 REMARK
REVDAT 3 24-MAR-09 1CLF 1 ATOM CONECT
REVDAT 2 24-FEB-09 1CLF 1 VERSN
REVDAT 1 29-JAN-96 1CLF 0
JRNL AUTH I.BERTINI,A.DONAIRE,B.A.FEINBERG,C.LUCHINAT,M.PICCIOLI,
JRNL AUTH 2 H.YUAN
JRNL TITL SOLUTION STRUCTURE OF THE OXIDIZED 2[4FE-4S] FERREDOXIN FROM
JRNL TITL 2 CLOSTRIDIUM PASTEURIANUM.
JRNL REF EUR.J.BIOCHEM. V. 232 192 1995
JRNL REFN ISSN 0014-2956
JRNL PMID 7556151
JRNL DOI 10.1111/J.1432-1033.1995.TB20799.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.BERTINI,F.CAPPOZZI,C.LUCHINAT,M.PICCIOLI,A.J.VILA
REMARK 1 TITL THE FE4S4 CENTERS IN FERREDOXINS STUDIED THROUGH PROTON AND
REMARK 1 TITL 2 CARBON HYPERFINE COUPLING. SEQUENCE SPECIFIC ASSIGNMENTS OF
REMARK 1 TITL 3 CYSTEINES IN FERREDOXINS FROM CLOSTRIDIUM ACIDI URICI AND
REMARK 1 TITL 4 CLOSTRIDIUM PASTEURIANUM
REMARK 1 REF J.AM.CHEM.SOC. V. 116 651 1994
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.D.B.SCROFANI,P.S.BRERETON,A.M.HAMER,M.J.LAVERY,
REMARK 1 AUTH 2 S.G.MCDOWALL,G.A.VINCENT,R.T.C.BROWNLEE,N.J.HOOGENRAAD,
REMARK 1 AUTH 3 M.SADEK,A.G.WEDD
REMARK 1 TITL COMPARISON OF NATIVE AND MUTANT PROTEINS PROVIDES A
REMARK 1 TITL 2 SEQUENCE-SPECIFIC ASSIGNMENT OF THE CYSTEINYL LIGAND PROTON
REMARK 1 TITL 3 NMR RESONANCES IN THE 2[FE4S4] FERREDOXIN FROM CLOSTRIDIUM
REMARK 1 TITL 4 PASTEURIANUM
REMARK 1 REF BIOCHEMISTRY V. 33 14486 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.RABINOWITZ
REMARK 1 TITL PREPARATION AND PROPERTIES OF CLOSTRIDIAL FERREDOXINS
REMARK 1 REF METHODS ENZYMOL. V. 24 431 1972
REMARK 1 REFN ISSN 0076-6879
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA, AMBER 4.0
REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA),
REMARK 3 PEARLMAN,CASE,CALDWELL,SIEBEL,SINGH,WEINER,KOLLMAN
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CLF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172372.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 CYS A 11 CB - CA - C ANGL. DEV. = 7.5 DEGREES
REMARK 500 3 VAL A 9 CA - CB - CG2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 7 CYS A 14 CB - CA - C ANGL. DEV. = 9.7 DEGREES
REMARK 500 13 CYS A 11 CB - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 15 CYS A 40 CB - CA - C ANGL. DEV. = 8.5 DEGREES
REMARK 500 16 CYS A 11 CB - CA - C ANGL. DEV. = 7.5 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 TYR A 2 -159.59 -129.62
REMARK 500 1 SER A 10 70.53 -67.56
REMARK 500 1 CYS A 14 -31.68 -155.59
REMARK 500 1 ALA A 22 36.41 -81.25
REMARK 500 1 SER A 28 -50.51 -141.78
REMARK 500 1 ASP A 39 74.11 -60.96
REMARK 500 1 CYS A 43 -57.56 60.61
REMARK 500 1 PRO A 52 82.30 -60.14
REMARK 500 2 TYR A 2 -158.35 -76.25
REMARK 500 2 CYS A 14 -97.40 -80.43
REMARK 500 2 ALA A 15 -99.01 45.57
REMARK 500 2 ASP A 27 -72.14 -114.80
REMARK 500 2 SER A 28 -61.09 -108.65
REMARK 500 2 ILE A 29 -166.55 -102.90
REMARK 500 2 PRO A 52 82.48 -65.67
REMARK 500 3 TYR A 2 -154.17 -74.25
REMARK 500 3 VAL A 9 -53.32 71.35
REMARK 500 3 SER A 10 29.14 129.08
REMARK 500 3 ALA A 22 31.61 -94.18
REMARK 500 3 ASP A 27 -70.04 -102.99
REMARK 500 3 ILE A 29 -167.24 -101.09
REMARK 500 3 ILE A 38 -112.27 -90.84
REMARK 500 3 PRO A 52 90.14 -60.95
REMARK 500 4 TYR A 2 -137.06 61.45
REMARK 500 4 SER A 10 64.48 -65.39
REMARK 500 4 CYS A 14 -108.62 -79.31
REMARK 500 4 ALA A 15 -101.65 53.76
REMARK 500 4 ALA A 22 32.46 -82.83
REMARK 500 4 SER A 28 -57.70 -140.73
REMARK 500 4 ILE A 29 -162.49 -104.45
REMARK 500 4 ILE A 38 47.28 -79.76
REMARK 500 4 ASP A 39 65.54 14.73
REMARK 500 4 PRO A 52 83.15 -64.29
REMARK 500 5 TYR A 2 -157.71 -123.78
REMARK 500 5 SER A 7 13.19 -65.11
REMARK 500 5 CYS A 8 -73.12 -74.17
REMARK 500 5 VAL A 9 137.63 75.77
REMARK 500 5 SER A 10 57.03 -64.25
REMARK 500 5 ALA A 22 36.34 -85.08
REMARK 500 5 ASP A 27 -77.20 -119.14
REMARK 500 5 ILE A 29 -169.16 -102.82
REMARK 500 5 ILE A 38 -102.39 -80.13
REMARK 500 5 PRO A 52 86.33 -58.36
REMARK 500 6 TYR A 2 -157.46 -85.76
REMARK 500 6 ASP A 27 -71.96 -116.56
REMARK 500 6 ILE A 29 -167.52 -100.94
REMARK 500 6 ASP A 33 91.96 -65.76
REMARK 500 6 ILE A 38 -102.73 -78.33
REMARK 500 6 PRO A 52 84.56 -63.65
REMARK 500 7 TYR A 2 -175.39 66.60
REMARK 500
REMARK 500 THIS ENTRY HAS 128 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 VAL A 53 GLN A 54 1 -138.52
REMARK 500 GLN A 54 GLU A 55 1 146.66
REMARK 500 VAL A 53 GLN A 54 2 -148.38
REMARK 500 TYR A 2 LYS A 3 3 146.71
REMARK 500 VAL A 53 GLN A 54 3 -144.55
REMARK 500 TYR A 2 LYS A 3 4 135.35
REMARK 500 VAL A 53 GLN A 54 4 -143.43
REMARK 500 TYR A 2 LYS A 3 5 143.38
REMARK 500 LYS A 3 ILE A 4 5 147.43
REMARK 500 GLY A 41 ASN A 42 5 -147.53
REMARK 500 VAL A 53 GLN A 54 5 -139.16
REMARK 500 GLN A 54 GLU A 55 5 135.31
REMARK 500 TYR A 2 LYS A 3 6 144.67
REMARK 500 LYS A 3 ILE A 4 6 146.53
REMARK 500 GLY A 41 ASN A 42 6 -147.72
REMARK 500 VAL A 53 GLN A 54 6 -124.12
REMARK 500 TYR A 2 LYS A 3 7 140.71
REMARK 500 VAL A 53 GLN A 54 7 -96.34
REMARK 500 TYR A 2 LYS A 3 8 141.08
REMARK 500 VAL A 53 GLN A 54 8 -121.40
REMARK 500 ALA A 1 TYR A 2 9 142.99
REMARK 500 VAL A 53 GLN A 54 9 -118.69
REMARK 500 TYR A 2 LYS A 3 10 145.78
REMARK 500 VAL A 53 GLN A 54 10 -132.40
REMARK 500 GLN A 54 GLU A 55 10 131.81
REMARK 500 VAL A 53 GLN A 54 11 -128.49
REMARK 500 TYR A 2 LYS A 3 12 149.84
REMARK 500 VAL A 53 GLN A 54 12 -130.38
REMARK 500 TYR A 2 LYS A 3 13 148.48
REMARK 500 VAL A 53 GLN A 54 13 -133.50
REMARK 500 GLN A 54 GLU A 55 13 144.75
REMARK 500 TYR A 2 LYS A 3 14 145.89
REMARK 500 LYS A 3 ILE A 4 14 148.07
REMARK 500 VAL A 53 GLN A 54 14 -128.84
REMARK 500 TYR A 2 LYS A 3 15 144.88
REMARK 500 VAL A 53 GLN A 54 15 -113.14
REMARK 500 TYR A 2 LYS A 3 16 146.32
REMARK 500 VAL A 53 GLN A 54 16 -133.54
REMARK 500 GLN A 54 GLU A 55 16 144.95
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 TYR A 2 0.11 SIDE CHAIN
REMARK 500 3 TYR A 2 0.13 SIDE CHAIN
REMARK 500 3 PHE A 30 0.12 SIDE CHAIN
REMARK 500 4 TYR A 2 0.15 SIDE CHAIN
REMARK 500 5 PHE A 30 0.10 SIDE CHAIN
REMARK 500 6 TYR A 2 0.11 SIDE CHAIN
REMARK 500 7 TYR A 2 0.16 SIDE CHAIN
REMARK 500 8 TYR A 2 0.19 SIDE CHAIN
REMARK 500 11 TYR A 2 0.08 SIDE CHAIN
REMARK 500 11 PHE A 30 0.08 SIDE CHAIN
REMARK 500 12 TYR A 2 0.07 SIDE CHAIN
REMARK 500 13 TYR A 2 0.14 SIDE CHAIN
REMARK 500 14 TYR A 2 0.07 SIDE CHAIN
REMARK 500 15 TYR A 2 0.24 SIDE CHAIN
REMARK 500 16 TYR A 2 0.07 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 SF4 A 56 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 8 SG
REMARK 620 2 SF4 A 56 S2 113.7
REMARK 620 3 SF4 A 56 S3 117.1 104.0
REMARK 620 4 SF4 A 56 S4 113.5 104.0 103.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 56 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 11 SG
REMARK 620 2 SF4 A 56 S1 108.4
REMARK 620 3 SF4 A 56 S3 116.4 105.0
REMARK 620 4 SF4 A 56 S4 116.5 104.9 104.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 56 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 14 SG
REMARK 620 2 SF4 A 56 S1 114.1
REMARK 620 3 SF4 A 56 S2 114.1 103.5
REMARK 620 4 SF4 A 56 S4 114.5 104.6 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 57 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 18 SG
REMARK 620 2 SF4 A 57 S1 112.0
REMARK 620 3 SF4 A 57 S2 115.4 104.2
REMARK 620 4 SF4 A 57 S3 114.2 105.7 104.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 57 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 37 SG
REMARK 620 2 SF4 A 57 S2 112.8
REMARK 620 3 SF4 A 57 S3 117.9 103.5
REMARK 620 4 SF4 A 57 S4 111.7 105.8 104.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 57 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 40 SG
REMARK 620 2 SF4 A 57 S1 108.6
REMARK 620 3 SF4 A 57 S3 115.9 104.6
REMARK 620 4 SF4 A 57 S4 117.3 104.1 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 57 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 43 SG
REMARK 620 2 SF4 A 57 S1 114.6
REMARK 620 3 SF4 A 57 S2 112.2 103.8
REMARK 620 4 SF4 A 57 S4 115.5 104.0 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 56 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 47 SG
REMARK 620 2 SF4 A 56 S1 113.7
REMARK 620 3 SF4 A 56 S2 114.3 104.0
REMARK 620 4 SF4 A 56 S3 113.0 105.7 105.2
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 SF4 A 56
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 57
DBREF 1CLF A 1 55 UNP P00195 FER_CLOPA 1 55
SEQRES 1 A 55 ALA TYR LYS ILE ALA ASP SER CYS VAL SER CYS GLY ALA
SEQRES 2 A 55 CYS ALA SER GLU CYS PRO VAL ASN ALA ILE SER GLN GLY
SEQRES 3 A 55 ASP SER ILE PHE VAL ILE ASP ALA ASP THR CYS ILE ASP
SEQRES 4 A 55 CYS GLY ASN CYS ALA ASN VAL CYS PRO VAL GLY ALA PRO
SEQRES 5 A 55 VAL GLN GLU
HET SF4 A 56 8
HET SF4 A 57 8
HETNAM SF4 IRON/SULFUR CLUSTER
FORMUL 2 SF4 2(FE4 S4)
SHEET 1 A 2 ILE A 23 GLN A 25 0
SHEET 2 A 2 PHE A 30 ILE A 32 -1 N VAL A 31 O SER A 24
LINK SG CYS A 8 FE1 SF4 A 56 1555 1555 2.25
LINK SG CYS A 11 FE2 SF4 A 56 1555 1555 2.16
LINK SG CYS A 14 FE3 SF4 A 56 1555 1555 2.18
LINK SG CYS A 18 FE4 SF4 A 57 1555 1555 2.17
LINK SG CYS A 37 FE1 SF4 A 57 1555 1555 2.19
LINK SG CYS A 40 FE2 SF4 A 57 1555 1555 2.18
LINK SG CYS A 43 FE3 SF4 A 57 1555 1555 2.17
LINK SG CYS A 47 FE4 SF4 A 56 1555 1555 2.15
SITE 1 AC1 9 ILE A 4 CYS A 8 VAL A 9 CYS A 11
SITE 2 AC1 9 GLY A 12 ALA A 13 CYS A 14 PHE A 30
SITE 3 AC1 9 CYS A 47
SITE 1 AC2 8 CYS A 18 PRO A 19 VAL A 20 CYS A 37
SITE 2 AC2 8 ILE A 38 CYS A 40 ASN A 42 CYS A 43
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
Complete list - 16 20 Bytes