Header list of 1bwe.pdb file
Complete list - v 3 2 Bytes
HEADER ELECTRON TRANSPORT 23-SEP-98 1BWE
TITLE ARTIFICIAL FE8S8 FERREDOXIN: THE D13C VARIANT OF BACILLUS SCHLEGELII
TITLE 2 FE7S8 FERREDOXIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SCHLEGELII;
SOURCE 3 ORGANISM_TAXID: 1484;
SOURCE 4 ATCC: ATCC 43741;
SOURCE 5 COLLECTION: ATCC 43741;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM 109;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKKFD D13C
KEYWDS IRON-SULFUR PROTEIN, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.AONO,D.BENTROP,I.BERTINI,G.COSENZA,C.LUCHINAT
REVDAT 6 03-NOV-21 1BWE 1 COMPND REMARK SEQADV LINK
REVDAT 5 06-FEB-19 1BWE 1 REMARK ATOM
REVDAT 4 24-FEB-09 1BWE 1 VERSN
REVDAT 3 01-APR-03 1BWE 1 JRNL
REVDAT 2 29-DEC-99 1BWE 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 30-SEP-98 1BWE 0
JRNL AUTH S.AONO,D.BENTROP,I.BERTINI,G.COSENZA,C.LUCHINAT
JRNL TITL SOLUTION STRUCTURE OF AN ARTIFICIAL FE8S8 FERREDOXIN: THE
JRNL TITL 2 D13C VARIANT OF BACILLUS SCHLEGELII FE7S8 FERREDOXIN.
JRNL REF EUR.J.BIOCHEM. V. 258 502 1998
JRNL REFN ISSN 0014-2956
JRNL PMID 9874217
JRNL DOI 10.1046/J.1432-1327.1998.2580502.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.AONO,D.BENTROP,I.BERTINI,C.LUCHINAT,R.MACINAI
REMARK 1 TITL THE D13C VARIANT OF BACILLUS SCHLEGELII 7FE FERREDOXIN IS AN
REMARK 1 TITL 2 8FE FERREDOXIN AS REVEALED BY 1H-NMR SPECTROSCOPY
REMARK 1 REF FEBS LETT. V. 412 501 1997
REMARK 1 REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 4.1
REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,
REMARK 3 FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE CALCULATIONS WERE CARRIED
REMARK 3 OUT WITH THE TORSION ANGLE DYNAMICS PROGRAM DYANA (BY GUENTERT,
REMARK 3 MUMENTHALER,WUETHRICH). THE 20 STRUCTURES OF THE DYANA FAMILY
REMARK 3 WITH THE LOWEST TARGET FUNCTION VALUES WERE REFINED BY
REMARK 3 RESTRAINED ENERGY MINIMIZATION(REM) AND RESTRAINED MOLECULAR
REMARK 3 DYNAMICS (RMD) IN VACUO. REFINEMENT DETAILSCAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1BWE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008237.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 20 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY; 1D-NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, AMBER 4.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINED ENERGY MINIMIZATION,
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 1H NMR SPECTROSCOPY.
REMARK 210 EXPERIMENTAL DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE.
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 17 CYS A 16 CA - CB - SG ANGL. DEV. = 8.1 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 6 -62.15 -8.52
REMARK 500 1 ILE A 9 90.94 -68.21
REMARK 500 1 THR A 11 73.03 39.56
REMARK 500 1 ALA A 14 40.12 -148.75
REMARK 500 1 GLU A 18 -40.29 75.86
REMARK 500 1 PRO A 21 -37.44 -39.72
REMARK 500 1 ASP A 23 51.71 33.20
REMARK 500 1 CYS A 24 42.34 -94.57
REMARK 500 1 GLU A 29 -60.95 -173.64
REMARK 500 1 ASP A 41 95.36 50.75
REMARK 500 1 ALA A 44 -76.99 -111.67
REMARK 500 1 PRO A 50 20.88 -74.48
REMARK 500 1 SER A 52 81.80 62.27
REMARK 500 1 ALA A 53 -9.92 -144.32
REMARK 500 2 GLU A 6 -61.22 -9.82
REMARK 500 2 LYS A 12 50.18 36.22
REMARK 500 2 ALA A 14 -136.01 58.95
REMARK 500 2 CYS A 16 -28.13 -176.51
REMARK 500 2 GLU A 18 0.30 -67.34
REMARK 500 2 ASP A 23 49.10 35.92
REMARK 500 2 CYS A 24 30.14 -85.89
REMARK 500 2 GLU A 29 -98.45 -175.56
REMARK 500 2 ASP A 30 54.10 -98.21
REMARK 500 2 GLN A 31 137.37 -177.71
REMARK 500 2 ILE A 40 34.03 -96.14
REMARK 500 2 ALA A 44 -67.51 74.17
REMARK 500 2 PRO A 50 49.53 -81.12
REMARK 500 2 VAL A 51 -35.47 -169.35
REMARK 500 3 GLU A 6 -57.65 -15.49
REMARK 500 3 ILE A 9 86.97 -65.34
REMARK 500 3 THR A 11 -153.61 53.28
REMARK 500 3 VAL A 19 -39.74 -137.61
REMARK 500 3 ASP A 23 -173.35 58.99
REMARK 500 3 CYS A 24 -2.18 124.28
REMARK 500 3 GLU A 29 -94.78 -128.94
REMARK 500 3 ASP A 30 58.25 -148.30
REMARK 500 3 ILE A 40 37.72 -95.23
REMARK 500 3 ASP A 41 60.33 38.57
REMARK 500 3 ALA A 44 -70.64 66.89
REMARK 500 3 SER A 52 76.25 54.39
REMARK 500 4 GLU A 6 -72.05 6.87
REMARK 500 4 ALA A 14 71.69 -164.03
REMARK 500 4 SER A 15 -59.00 -141.99
REMARK 500 4 GLU A 18 -12.77 62.97
REMARK 500 4 ASP A 23 149.87 65.87
REMARK 500 4 CYS A 24 -102.09 -163.06
REMARK 500 4 ILE A 25 88.33 13.78
REMARK 500 4 GLU A 29 -78.30 -172.44
REMARK 500 4 ASP A 35 109.07 -52.90
REMARK 500 4 ILE A 40 35.58 -89.87
REMARK 500
REMARK 500 THIS ENTRY HAS 233 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 TYR A 2 0.09 SIDE CHAIN
REMARK 500 1 ARG A 72 0.12 SIDE CHAIN
REMARK 500 2 TYR A 2 0.12 SIDE CHAIN
REMARK 500 2 TYR A 33 0.11 SIDE CHAIN
REMARK 500 2 TYR A 55 0.07 SIDE CHAIN
REMARK 500 3 TYR A 2 0.11 SIDE CHAIN
REMARK 500 3 TYR A 32 0.12 SIDE CHAIN
REMARK 500 3 TYR A 33 0.17 SIDE CHAIN
REMARK 500 3 ARG A 72 0.12 SIDE CHAIN
REMARK 500 4 TYR A 32 0.10 SIDE CHAIN
REMARK 500 4 TYR A 33 0.11 SIDE CHAIN
REMARK 500 5 TYR A 2 0.12 SIDE CHAIN
REMARK 500 5 TYR A 32 0.10 SIDE CHAIN
REMARK 500 5 TYR A 33 0.14 SIDE CHAIN
REMARK 500 5 ARG A 72 0.15 SIDE CHAIN
REMARK 500 6 TYR A 2 0.11 SIDE CHAIN
REMARK 500 6 TYR A 32 0.10 SIDE CHAIN
REMARK 500 6 TYR A 33 0.09 SIDE CHAIN
REMARK 500 6 ARG A 72 0.12 SIDE CHAIN
REMARK 500 6 PHE A 74 0.07 SIDE CHAIN
REMARK 500 7 TYR A 55 0.10 SIDE CHAIN
REMARK 500 7 ARG A 72 0.12 SIDE CHAIN
REMARK 500 9 TYR A 55 0.13 SIDE CHAIN
REMARK 500 9 ARG A 72 0.12 SIDE CHAIN
REMARK 500 10 TYR A 2 0.13 SIDE CHAIN
REMARK 500 10 TYR A 32 0.10 SIDE CHAIN
REMARK 500 10 TYR A 33 0.07 SIDE CHAIN
REMARK 500 11 TYR A 2 0.11 SIDE CHAIN
REMARK 500 11 TYR A 32 0.12 SIDE CHAIN
REMARK 500 11 TYR A 33 0.10 SIDE CHAIN
REMARK 500 11 TYR A 55 0.08 SIDE CHAIN
REMARK 500 11 ARG A 72 0.15 SIDE CHAIN
REMARK 500 12 TYR A 2 0.24 SIDE CHAIN
REMARK 500 12 TYR A 32 0.14 SIDE CHAIN
REMARK 500 12 TYR A 33 0.10 SIDE CHAIN
REMARK 500 12 TYR A 55 0.11 SIDE CHAIN
REMARK 500 13 TYR A 2 0.07 SIDE CHAIN
REMARK 500 13 TYR A 32 0.14 SIDE CHAIN
REMARK 500 13 ARG A 72 0.15 SIDE CHAIN
REMARK 500 14 TYR A 2 0.11 SIDE CHAIN
REMARK 500 14 TYR A 32 0.08 SIDE CHAIN
REMARK 500 14 TYR A 55 0.08 SIDE CHAIN
REMARK 500 15 TYR A 2 0.12 SIDE CHAIN
REMARK 500 15 TYR A 32 0.09 SIDE CHAIN
REMARK 500 15 TYR A 33 0.11 SIDE CHAIN
REMARK 500 15 TYR A 55 0.08 SIDE CHAIN
REMARK 500 15 ARG A 72 0.11 SIDE CHAIN
REMARK 500 16 TYR A 2 0.14 SIDE CHAIN
REMARK 500 16 TYR A 32 0.08 SIDE CHAIN
REMARK 500 16 TYR A 55 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 65 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 SF4 A 78 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 8 SG
REMARK 620 2 SF4 A 78 S2 112.1
REMARK 620 3 SF4 A 78 S3 116.8 106.7
REMARK 620 4 SF4 A 78 S4 116.4 102.7 100.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 78 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 13 SG
REMARK 620 2 SF4 A 78 S1 106.0
REMARK 620 3 SF4 A 78 S3 112.7 103.4
REMARK 620 4 SF4 A 78 S4 111.4 113.7 109.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 78 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 16 SG
REMARK 620 2 SF4 A 78 S1 107.9
REMARK 620 3 SF4 A 78 S2 123.0 101.6
REMARK 620 4 SF4 A 78 S4 107.4 106.4 109.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 79 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 20 SG
REMARK 620 2 SF4 A 79 S2 112.7
REMARK 620 3 SF4 A 79 S3 118.6 103.6
REMARK 620 4 SF4 A 79 S4 114.5 104.1 101.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 79 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 39 SG
REMARK 620 2 SF4 A 79 S1 102.3
REMARK 620 3 SF4 A 79 S3 113.5 105.0
REMARK 620 4 SF4 A 79 S4 114.8 111.0 109.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 79 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 42 SG
REMARK 620 2 SF4 A 79 S1 116.4
REMARK 620 3 SF4 A 79 S2 109.6 102.1
REMARK 620 4 SF4 A 79 S4 113.0 103.7 111.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 79 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 45 SG
REMARK 620 2 SF4 A 79 S1 100.2
REMARK 620 3 SF4 A 79 S2 110.2 106.3
REMARK 620 4 SF4 A 79 S3 123.9 107.3 107.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 78 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 49 SG
REMARK 620 2 SF4 A 78 S1 110.7
REMARK 620 3 SF4 A 78 S2 110.0 105.4
REMARK 620 4 SF4 A 78 S3 114.9 104.7 110.5
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 78
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 79
DBREF 1BWE A 1 77 UNP Q45560 FER_BACSC 2 78
SEQADV 1BWE CYS A 13 UNP Q45560 ASP 14 ENGINEERED MUTATION
SEQRES 1 A 77 ALA TYR VAL ILE THR GLU PRO CYS ILE GLY THR LYS CYS
SEQRES 2 A 77 ALA SER CYS VAL GLU VAL CYS PRO VAL ASP CYS ILE HIS
SEQRES 3 A 77 GLU GLY GLU ASP GLN TYR TYR ILE ASP PRO ASP VAL CYS
SEQRES 4 A 77 ILE ASP CYS GLY ALA CYS GLU ALA VAL CYS PRO VAL SER
SEQRES 5 A 77 ALA ILE TYR HIS GLU ASP PHE VAL PRO GLU GLU TRP LYS
SEQRES 6 A 77 SER TYR ILE GLN LYS ASN ARG ASP PHE PHE LYS LYS
HET SF4 A 78 8
HET SF4 A 79 8
HETNAM SF4 IRON/SULFUR CLUSTER
FORMUL 2 SF4 2(FE4 S4)
HELIX 1 1 GLU A 6 CYS A 8 5 3
HELIX 2 2 CYS A 45 VAL A 48 1 4
HELIX 3 3 GLU A 62 PHE A 75 1 14
SHEET 1 A 2 ILE A 25 GLU A 27 0
SHEET 2 A 2 TYR A 32 ILE A 34 -1 N TYR A 33 O HIS A 26
LINK SG CYS A 8 FE1 SF4 A 78 1555 1555 2.01
LINK SG CYS A 13 FE2 SF4 A 78 1555 1555 2.05
LINK SG CYS A 16 FE3 SF4 A 78 1555 1555 2.16
LINK SG CYS A 20 FE1 SF4 A 79 1555 1555 2.06
LINK SG CYS A 39 FE2 SF4 A 79 1555 1555 2.06
LINK SG CYS A 42 FE3 SF4 A 79 1555 1555 2.14
LINK SG CYS A 45 FE4 SF4 A 79 1555 1555 2.02
LINK SG CYS A 49 FE4 SF4 A 78 1555 1555 2.04
SITE 1 AC1 5 CYS A 8 CYS A 13 CYS A 16 CYS A 49
SITE 2 AC1 5 ILE A 54
SITE 1 AC2 8 TYR A 2 CYS A 20 CYS A 24 ILE A 34
SITE 2 AC2 8 CYS A 39 ILE A 40 CYS A 42 CYS A 45
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 3 2 Bytes