Header list of 1f2g.pdb file
Complete list - b 16 2 Bytes
HEADER ELECTRON TRANSPORT 08-OCT-98 1F2G
TITLE THE NMR SOLUTION STRUCTURE OF THE 3FE FERREDOXIN II FROM DESULFOVIBRIO
TITLE 2 GIGAS, 15 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERREDOXIN II;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO GIGAS;
SOURCE 3 ORGANISM_TAXID: 879
KEYWDS ELECTRON TRANSPORT, FDII DESULFOVIBRIO GIGAS, FERREDOXIN II
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR B.J.GOODFELLOW,A.L.MACEDO,P.RODRIGUES,V.WRAY,I.MOURA,J.J.G.MOURA
REVDAT 4 16-FEB-22 1F2G 1 REMARK LINK
REVDAT 3 24-FEB-09 1F2G 1 VERSN
REVDAT 2 01-APR-03 1F2G 1 JRNL
REVDAT 1 02-SEP-99 1F2G 0
JRNL AUTH B.J.GOODFELLOW,A.L.MACEDO,P.RODRIGUES,I.MOURA,V.WRAY,
JRNL AUTH 2 J.J.MOURA
JRNL TITL THE SOLUTION STRUCTURE OF A [3FE-4S] FERREDOXIN: OXIDISED
JRNL TITL 2 FERREDOXIN II FROM DESULFOVIBRIO GIGAS.
JRNL REF J.BIOL.INORG.CHEM. V. 4 421 1999
JRNL REFN ISSN 0949-8257
JRNL PMID 10555576
JRNL DOI 10.1007/S007750050328
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F2G 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_1000173197.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10% D2O/90% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; COSY; TOCSY; 1D NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA
REMARK 210 METHOD USED : TORSION ANGLE DYANAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 2000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TARGET FUNCTION
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: 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: 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 ASN A 5 -169.84 60.30
REMARK 500 1 MET A 9 -84.61 -108.64
REMARK 500 1 ALA A 10 59.56 168.00
REMARK 500 1 ASN A 25 -144.88 -60.89
REMARK 500 1 PRO A 36 35.09 -75.00
REMARK 500 1 ASP A 37 42.68 175.23
REMARK 500 1 SER A 38 -162.95 -58.93
REMARK 500 1 ASP A 39 32.94 -170.59
REMARK 500 1 GLU A 53 45.41 36.19
REMARK 500 1 ARG A 57 43.22 -87.74
REMARK 500 2 MET A 9 -68.06 -98.50
REMARK 500 2 ALA A 10 48.67 167.78
REMARK 500 2 ASN A 25 -155.71 -61.18
REMARK 500 2 PRO A 36 32.84 -74.93
REMARK 500 2 ASP A 37 40.65 177.26
REMARK 500 2 LEU A 40 -144.70 -85.99
REMARK 500 2 ASP A 41 13.38 -140.37
REMARK 500 2 GLU A 53 50.56 37.73
REMARK 500 2 ARG A 57 35.70 -90.31
REMARK 500 3 ASN A 5 -171.12 63.97
REMARK 500 3 CYS A 8 162.12 -47.98
REMARK 500 3 MET A 9 -77.36 -103.01
REMARK 500 3 ALA A 10 41.49 168.80
REMARK 500 3 GLU A 12 17.93 58.85
REMARK 500 3 ILE A 17 -43.66 -133.95
REMARK 500 3 MET A 24 153.10 -40.92
REMARK 500 3 ASN A 25 -150.85 -91.48
REMARK 500 3 GLU A 27 31.07 -154.56
REMARK 500 3 LYS A 30 109.20 -167.33
REMARK 500 3 ALA A 31 104.62 -48.75
REMARK 500 3 PRO A 36 37.58 -74.94
REMARK 500 3 ASP A 37 40.13 179.17
REMARK 500 3 SER A 38 -76.88 -83.43
REMARK 500 3 LEU A 40 44.16 -108.97
REMARK 500 3 ASP A 41 -51.35 79.49
REMARK 500 3 GLU A 53 38.45 38.22
REMARK 500 3 ARG A 57 48.87 -95.87
REMARK 500 4 GLU A 3 -156.13 -135.31
REMARK 500 4 VAL A 4 -104.66 -127.36
REMARK 500 4 ASN A 5 -171.04 178.01
REMARK 500 4 CYS A 8 162.36 -45.38
REMARK 500 4 MET A 9 -86.35 -106.69
REMARK 500 4 ALA A 10 61.17 166.50
REMARK 500 4 GLU A 16 41.40 -85.00
REMARK 500 4 ILE A 17 -40.66 -170.37
REMARK 500 4 MET A 24 163.04 -40.43
REMARK 500 4 ASN A 25 -149.18 -84.69
REMARK 500 4 GLU A 27 19.14 -152.17
REMARK 500 4 PRO A 36 26.25 -74.95
REMARK 500 4 ASP A 37 39.07 178.41
REMARK 500
REMARK 500 THIS ENTRY HAS 187 RAMACHANDRAN OUTLIERS.
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 59 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 8 SG
REMARK 620 2 F3S A 59 S1 118.0
REMARK 620 3 F3S A 59 S2 112.7 107.0
REMARK 620 4 F3S A 59 S3 114.3 103.5 99.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S A 59 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 14 SG
REMARK 620 2 F3S A 59 S2 114.3
REMARK 620 3 F3S A 59 S3 115.9 97.4
REMARK 620 4 F3S A 59 S4 116.9 104.3 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S A 59 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 50 SG
REMARK 620 2 F3S A 59 S1 126.2
REMARK 620 3 F3S A 59 S3 112.2 98.7
REMARK 620 4 F3S A 59 S4 114.3 102.2 98.9
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 F3S A 59
DBREF 1F2G A 1 58 UNP P00209 FER_DESGI 1 58
SEQRES 1 A 58 PRO ILE GLU VAL ASN ASP ASP CYS MET ALA CYS GLU ALA
SEQRES 2 A 58 CYS VAL GLU ILE CYS PRO ASP VAL PHE GLU MET ASN GLU
SEQRES 3 A 58 GLU GLY ASP LYS ALA VAL VAL ILE ASN PRO ASP SER ASP
SEQRES 4 A 58 LEU ASP CYS VAL GLU GLU ALA ILE ASP SER CYS PRO ALA
SEQRES 5 A 58 GLU ALA ILE VAL ARG SER
HET F3S A 59 7
HETNAM F3S FE3-S4 CLUSTER
FORMUL 2 F3S FE3 S4
HELIX 1 1 ALA A 13 ILE A 17 1 5
HELIX 2 2 ASP A 41 ASP A 48 5 8
SHEET 1 A 2 PHE A 22 MET A 24 0
SHEET 2 A 2 ALA A 31 VAL A 33 -1 N VAL A 32 O GLU A 23
SSBOND 1 CYS A 18 CYS A 42 1555 1555 2.08
LINK SG CYS A 8 FE1 F3S A 59 1555 1555 2.30
LINK SG CYS A 14 FE4 F3S A 59 1555 1555 2.30
LINK SG CYS A 50 FE3 F3S A 59 1555 1555 2.30
SITE 1 AC1 9 VAL A 4 CYS A 8 CYS A 11 GLU A 12
SITE 2 AC1 9 ALA A 13 CYS A 14 ALA A 31 CYS A 50
SITE 3 AC1 9 ILE A 55
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 - b 16 2 Bytes