Header list of 1pdx.pdb file
Complete list - v 6 2 Bytes
HEADER ELECTRON TRANSFER 15-FEB-99 1PDX
TITLE PUTIDAREDOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (PUTIDAREDOXIN);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PDX;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: 2FE-2S CLUSTER LIGATED BY CYS 39, CYS 45, CYS 48 AND
COMPND 7 CYS 86
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 3 ORGANISM_TAXID: 303;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: TB1;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PKM536;
SOURCE 8 EXPRESSION_SYSTEM_GENE: CAMB;
SOURCE 9 OTHER_DETAILS: ORIGINALLY ISOLATED FROM P. PUTIDA GROWN WITH CAMPHOR
SOURCE 10 AS SOLE CARBON SOURCE
KEYWDS ELECTRON TRANSFER, CYTOCHROME P450CAM, FERREDOXIN, IRON-SULFUR
KEYWDS 2 CLUSTER
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR T.C.POCHAPSKY,N.U.JAIN,M.KUTI,T.A.LYONS,J.HEYMONT
REVDAT 5 06-NOV-19 1PDX 1 JRNL REMARK
REVDAT 4 29-NOV-17 1PDX 1 REMARK HELIX
REVDAT 3 24-FEB-09 1PDX 1 VERSN
REVDAT 2 26-SEP-01 1PDX 3 ATOM
REVDAT 1 12-MAY-99 1PDX 0
JRNL AUTH T.C.POCHAPSKY,N.U.JAIN,M.KUTI,T.A.LYONS,J.HEYMONT
JRNL TITL A REFINED MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED
JRNL TITL 2 PUTIDAREDOXIN.
JRNL REF BIOCHEMISTRY V. 38 4681 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10200155
JRNL DOI 10.1021/BI983030B
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.MULLER,J.J.MULLER,Y.A.MULLER,H.UHLMANN,R.BERNHARDT,
REMARK 1 AUTH 2 U.HEINEMANN
REMARK 1 TITL NEW ASPECTS OF ELECTRON TRANSFER REVEALED BY THE CRYSTAL
REMARK 1 TITL 2 STRUCTURE OF A TRUNCATED BOVINE ADRENODOXIN, ADX(4-108).
REMARK 1 REF STRUCTURE V. 6 269 1998
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 9551550
REMARK 1 DOI 10.1016/S0969-2126(98)00031-8
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.C.POCHAPSKY,X.M.YE,G.RATNASWAMY,T.A.LYONS
REMARK 1 TITL AN NMR-DERIVED MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED
REMARK 1 TITL 2 PUTIDAREDOXIN, A 2-FE, 2-S FERREDOXIN FROM PSEUDOMONAS.
REMARK 1 REF BIOCHEMISTRY V. 33 6424 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 8204575
REMARK 1 DOI 10.1021/BI00187A006
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.C.POCHAPSKY,G.RATNASWAMY,A.PATERA
REMARK 1 TITL REDOX-DEPENDENT 1H NMR SPECTRAL FEATURES AND TERTIARY
REMARK 1 TITL 2 STRUCTURAL CONSTRAINTS ON THE C-TERMINAL REGION OF
REMARK 1 TITL 3 PUTIDAREDOXIN.
REMARK 1 REF BIOCHEMISTRY V. 33 6433 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 8204576
REMARK 1 DOI 10.1021/BI00187A007
REMARK 1 REFERENCE 4
REMARK 1 AUTH G.RATNASWAMY,T.C.POCHAPSKY
REMARK 1 TITL CHARACTERIZATION OF HYPERFINE-SHIFTED 1H RESONANCES IN
REMARK 1 TITL 2 OXIDIZED AND REDUCED PUTIDAREDOXIN, AN FE2S2 FERREDOXIN FROM
REMARK 1 TITL 3 PSEUDOMONAS PUTIDA
REMARK 1 REF MAGN.RESON.CHEM. V. 31 73 1993
REMARK 1 REFN ISSN 0749-1581
REMARK 1 DOI 10.1002/MRC.1260311315
REMARK 1 REFERENCE 5
REMARK 1 AUTH X.M.YE,T.C.POCHAPSKY,S.S.POCHAPSKY
REMARK 1 TITL 1H NMR SEQUENTIAL ASSIGNMENTS AND IDENTIFICATION OF
REMARK 1 TITL 2 SECONDARY STRUCTURAL ELEMENTS IN OXIDIZED PUTIDAREDOXIN, AN
REMARK 1 TITL 3 ELECTRON-TRANSFER PROTEIN FROM PSEUDOMONAS.
REMARK 1 REF BIOCHEMISTRY V. 31 1961 1992
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 1536837
REMARK 1 DOI 10.1021/BI00122A009
REMARK 1 REFERENCE 6
REMARK 1 AUTH T.C.POCHAPSKY,X.M.YE
REMARK 1 TITL 1H NMR IDENTIFICATION OF A BETA-SHEET STRUCTURE AND
REMARK 1 TITL 2 DESCRIPTION OF FOLDING TOPOLOGY IN PUTIDAREDOXIN.
REMARK 1 REF BIOCHEMISTRY V. 30 3850 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 2018758
REMARK 1 DOI 10.1021/BI00230A007
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PDX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-99.
REMARK 100 THE DEPOSITION ID IS D_1000000493.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 290
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; HSQC; HCCH-TOCSY; HNCA;
REMARK 210 HSQC-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX, XPLOR
REMARK 210 METHOD USED : DG,SA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOL.>0.5 A, NO DIHEDRAL
REMARK 210 VIOLATION > 5 DEG.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED PUTIDAREDOXIN
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 O TYR A 51 H ASP A 100 1.49
REMARK 500 O CYS A 73 HE1 TRP A 106 1.54
REMARK 500 H ASN A 53 O VAL A 98 1.56
REMARK 500 H VAL A 6 O VAL A 99 1.58
REMARK 500 H LYS A 79 OG SER A 82 1.60
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 1 LYS A 79 N - CA - CB ANGL. DEV. = -12.3 DEGREES
REMARK 500 2 LYS A 79 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 4 LYS A 79 N - CA - CB ANGL. DEV. = -13.2 DEGREES
REMARK 500 7 LYS A 79 N - CA - CB ANGL. DEV. = -12.4 DEGREES
REMARK 500 8 LYS A 79 N - CA - CB ANGL. DEV. = -12.4 DEGREES
REMARK 500 9 LYS A 79 N - CA - CB ANGL. DEV. = -11.3 DEGREES
REMARK 500 11 LYS A 79 N - CA - CB ANGL. DEV. = -12.5 DEGREES
REMARK 500 12 LYS A 79 N - CA - CB ANGL. DEV. = -12.1 DEGREES
REMARK 500 14 LYS A 79 N - CA - CB ANGL. DEV. = -12.2 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 SER A 7 -155.86 -101.80
REMARK 500 1 LEU A 15 -156.16 -108.71
REMARK 500 1 ASP A 16 71.91 -152.50
REMARK 500 1 GLN A 25 -70.80 -59.68
REMARK 500 1 TYR A 33 48.96 -80.36
REMARK 500 1 VAL A 36 65.33 -112.81
REMARK 500 1 ALA A 46 9.90 -150.06
REMARK 500 1 GLU A 54 -8.09 -58.71
REMARK 500 1 ALA A 63 170.92 -38.65
REMARK 500 1 ASN A 64 -164.25 -111.90
REMARK 500 1 GLU A 65 -39.88 -28.71
REMARK 500 1 VAL A 74 161.55 -40.78
REMARK 500 1 ALA A 76 -165.19 -114.81
REMARK 500 1 GLU A 77 63.26 -54.05
REMARK 500 1 CYS A 85 -28.73 -28.85
REMARK 500 1 CYS A 86 -26.35 -39.76
REMARK 500 1 ARG A 104 75.08 -111.09
REMARK 500 1 GLN A 105 56.75 -98.94
REMARK 500 2 SER A 7 -154.77 -103.12
REMARK 500 2 LEU A 15 -151.11 -109.83
REMARK 500 2 ASP A 16 70.54 -152.19
REMARK 500 2 GLN A 25 -70.21 -89.70
REMARK 500 2 TYR A 33 46.48 -81.05
REMARK 500 2 SER A 44 30.24 -140.09
REMARK 500 2 ALA A 46 9.15 -150.28
REMARK 500 2 GLU A 54 -8.74 -59.47
REMARK 500 2 ALA A 63 161.26 -37.76
REMARK 500 2 GLU A 65 -27.30 -33.67
REMARK 500 2 ARG A 66 -70.62 -53.17
REMARK 500 2 ALA A 76 -148.81 -97.15
REMARK 500 2 SER A 82 158.08 -45.85
REMARK 500 2 CYS A 85 -37.18 -24.05
REMARK 500 2 ARG A 104 70.46 -110.92
REMARK 500 3 SER A 7 -155.92 -103.84
REMARK 500 3 LEU A 15 -157.04 -103.86
REMARK 500 3 ASP A 16 69.58 -152.54
REMARK 500 3 GLN A 25 -62.10 -90.20
REMARK 500 3 SER A 44 16.33 -140.03
REMARK 500 3 ASN A 53 150.00 -45.52
REMARK 500 3 GLU A 54 -8.46 -59.95
REMARK 500 3 ALA A 63 159.48 -37.50
REMARK 500 3 ASN A 64 -154.79 -105.60
REMARK 500 3 GLU A 65 -31.67 -31.98
REMARK 500 3 ARG A 66 -71.68 -52.84
REMARK 500 3 VAL A 74 161.35 -39.20
REMARK 500 3 ALA A 76 -166.50 -114.18
REMARK 500 3 GLU A 77 63.27 -55.75
REMARK 500 3 SER A 82 152.62 -45.61
REMARK 500 3 CYS A 85 -32.79 -28.68
REMARK 500 3 LEU A 94 31.09 -90.50
REMARK 500
REMARK 500 THIS ENTRY HAS 232 RAMACHANDRAN OUTLIERS.
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 13 0.16 SIDE CHAIN
REMARK 500 1 ARG A 66 0.22 SIDE CHAIN
REMARK 500 1 ARG A 83 0.29 SIDE CHAIN
REMARK 500 1 ARG A 104 0.30 SIDE CHAIN
REMARK 500 2 ARG A 12 0.28 SIDE CHAIN
REMARK 500 2 ARG A 13 0.19 SIDE CHAIN
REMARK 500 2 ARG A 66 0.31 SIDE CHAIN
REMARK 500 2 ARG A 104 0.18 SIDE CHAIN
REMARK 500 3 ARG A 12 0.25 SIDE CHAIN
REMARK 500 3 ARG A 13 0.23 SIDE CHAIN
REMARK 500 3 ARG A 66 0.14 SIDE CHAIN
REMARK 500 3 ARG A 83 0.14 SIDE CHAIN
REMARK 500 3 ARG A 104 0.31 SIDE CHAIN
REMARK 500 4 ARG A 12 0.19 SIDE CHAIN
REMARK 500 4 ARG A 13 0.32 SIDE CHAIN
REMARK 500 4 ARG A 66 0.20 SIDE CHAIN
REMARK 500 4 ARG A 83 0.08 SIDE CHAIN
REMARK 500 4 ARG A 104 0.28 SIDE CHAIN
REMARK 500 5 ARG A 12 0.32 SIDE CHAIN
REMARK 500 5 ARG A 13 0.27 SIDE CHAIN
REMARK 500 5 ARG A 66 0.31 SIDE CHAIN
REMARK 500 5 ARG A 83 0.12 SIDE CHAIN
REMARK 500 5 ARG A 104 0.32 SIDE CHAIN
REMARK 500 6 ARG A 12 0.12 SIDE CHAIN
REMARK 500 6 ARG A 13 0.17 SIDE CHAIN
REMARK 500 6 ARG A 66 0.29 SIDE CHAIN
REMARK 500 6 ARG A 83 0.28 SIDE CHAIN
REMARK 500 6 ARG A 104 0.31 SIDE CHAIN
REMARK 500 7 ARG A 12 0.10 SIDE CHAIN
REMARK 500 7 ARG A 66 0.32 SIDE CHAIN
REMARK 500 7 ARG A 83 0.24 SIDE CHAIN
REMARK 500 7 ARG A 104 0.22 SIDE CHAIN
REMARK 500 8 ARG A 12 0.24 SIDE CHAIN
REMARK 500 8 ARG A 13 0.20 SIDE CHAIN
REMARK 500 8 ARG A 66 0.28 SIDE CHAIN
REMARK 500 8 ARG A 83 0.32 SIDE CHAIN
REMARK 500 8 ARG A 104 0.24 SIDE CHAIN
REMARK 500 9 ARG A 12 0.25 SIDE CHAIN
REMARK 500 9 ARG A 13 0.19 SIDE CHAIN
REMARK 500 9 ARG A 66 0.19 SIDE CHAIN
REMARK 500 9 ARG A 83 0.20 SIDE CHAIN
REMARK 500 10 ARG A 13 0.09 SIDE CHAIN
REMARK 500 10 ARG A 66 0.27 SIDE CHAIN
REMARK 500 10 ARG A 83 0.24 SIDE CHAIN
REMARK 500 10 ARG A 104 0.30 SIDE CHAIN
REMARK 500 11 ARG A 12 0.20 SIDE CHAIN
REMARK 500 11 ARG A 13 0.09 SIDE CHAIN
REMARK 500 11 ARG A 66 0.24 SIDE CHAIN
REMARK 500 11 ARG A 104 0.25 SIDE CHAIN
REMARK 500 12 ARG A 13 0.25 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 62 PLANE DEVIATIONS.
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 107 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 39 SG
REMARK 620 2 FES A 107 S1 104.9
REMARK 620 3 FES A 107 S2 104.7 103.2
REMARK 620 4 CYS A 45 SG 132.7 104.4 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 107 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 48 SG
REMARK 620 2 FES A 107 S1 105.7
REMARK 620 3 FES A 107 S2 105.2 103.5
REMARK 620 4 CYS A 86 SG 127.9 106.6 105.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: FS2
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: LIGANDS FOR THE FE2 S2 CLUSTER
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 107
DBREF 1PDX A 1 106 UNP P00259 PUTX_PSEPU 2 107
SEQRES 1 A 106 SER LYS VAL VAL TYR VAL SER HIS ASP GLY THR ARG ARG
SEQRES 2 A 106 GLU LEU ASP VAL ALA ASP GLY VAL SER LEU MET GLN ALA
SEQRES 3 A 106 ALA VAL SER ASN GLY ILE TYR ASP ILE VAL GLY ASP CYS
SEQRES 4 A 106 GLY GLY SER ALA SER CYS ALA THR CYS HIS VAL TYR VAL
SEQRES 5 A 106 ASN GLU ALA PHE THR ASP LYS VAL PRO ALA ALA ASN GLU
SEQRES 6 A 106 ARG GLU ILE GLY MET LEU GLU CYS VAL THR ALA GLU LEU
SEQRES 7 A 106 LYS PRO ASN SER ARG LEU CYS CYS GLN ILE ILE MET THR
SEQRES 8 A 106 PRO GLU LEU ASP GLY ILE VAL VAL ASP VAL PRO ASP ARG
SEQRES 9 A 106 GLN TRP
HET FES A 107 4
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
FORMUL 2 FES FE2 S2
HELIX 1 D LEU A 23 GLY A 31 1 9
HELIX 2 F THR A 57 PRO A 61 1 5
HELIX 3 G GLU A 65 CYS A 73 1 9
SHEET 1 A 5 ARG A 12 VAL A 17 0
SHEET 2 A 5 SER A 1 VAL A 6 -1 N TYR A 5 O ARG A 13
SHEET 3 A 5 VAL A 98 VAL A 101 1 N VAL A 99 O VAL A 4
SHEET 4 A 5 VAL A 50 ASN A 53 -1 O TYR A 51 N ASP A 100
SHEET 5 A 5 SER A 82 ARG A 83 -1 N ARG A 83 O VAL A 50
SHEET 1 B 2 ILE A 89 MET A 90 0
SHEET 2 B 2 VAL A 21 SER A 22 -1 O VAL A 21 N MET A 90
LINK SG CYS A 39 FE1 FES A 107 1555 1555 2.20
LINK SG CYS A 45 FE1 FES A 107 1555 1555 2.20
LINK SG CYS A 48 FE2 FES A 107 1555 1555 2.18
LINK SG CYS A 86 FE2 FES A 107 1555 1555 2.19
SITE 1 FS2 4 CYS A 39 CYS A 45 CYS A 48 CYS A 86
SITE 1 AC1 5 CYS A 39 CYS A 45 CYS A 48 LEU A 84
SITE 2 AC1 5 CYS A 86
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 - v 6 2 Bytes