Header list of 1e8j.pdb file
Complete list - t 9 2 Bytes
HEADER ELECTRON TRANSPORT 21-SEP-00 1E8J
TITLE SOLUTION STRUCTURE OF DESULFOVIBRIO GIGAS ZINC RUBREDOXIN, NMR, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RUBREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: IRON-SULFUR-PROTEIN, ZINC SUBSTITUTED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO GIGAS;
SOURCE 3 ORGANISM_TAXID: 879;
SOURCE 4 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRPPL1;
SOURCE 10 EXPRESSION_SYSTEM_GENE: RDDG
KEYWDS ELECTRON TRANSPORT, ZINC-SUBSTITUTION, THERMOSTABILITY
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.LAMOSA,L.BRENNAN,H.VIS,D.L.TURNER,H.SANTOS
REVDAT 5 09-OCT-19 1E8J 1 JRNL
REVDAT 4 30-JAN-13 1E8J 1 HEADER KEYWDS JRNL REMARK
REVDAT 4 2 1 VERSN
REVDAT 3 24-FEB-09 1E8J 1 VERSN
REVDAT 2 18-JUL-03 1E8J 1 REMARK
REVDAT 1 18-OCT-01 1E8J 0
JRNL AUTH P.LAMOSA,L.BRENNAN,H.VIS,D.L.TURNER,H.SANTOS
JRNL TITL NMR STRUCTURE OF DESULFOVIBRIO GIGAS RUBREDOXIN: A MODEL FOR
JRNL TITL 2 STUDYING PROTEIN STABILIZATION BY COMPATIBLE SOLUTES.
JRNL REF EXTREMOPHILES V. 5 303 2001
JRNL REFN ISSN 1431-0651
JRNL PMID 11699644
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.LAMOSA,A.BURKE,R.PEIST,R.HUBER,M.-Y.LIU,G.SILVA,
REMARK 1 AUTH 2 C.RODRIGUES-POUSADA,J.LEGALL,C.MAYCOCK,H.SANTOS
REMARK 1 TITL THERMOSTABILIZATION OF PROTEINS BY DIGLYCEROL PHOSPHATE, A
REMARK 1 TITL 2 NEW COMPATIBLE SOLUTE FROM THE HYPERTHERMOPHILE
REMARK 1 TITL 3 ARCHAEOGLOBUS FULGIDUS
REMARK 1 REF APPL.ENVIRON.MICROBIOL. V. 66 1974 2000
REMARK 1 REFN ISSN 0099-2240
REMARK 1 PMID 10788369
REMARK 1 DOI 10.1128/AEM.66.5.1974-1979.2000
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : INDYANA
REMARK 3 AUTHORS : D.L.TURNER,L.BRENNAN,H. MEYER,C.LOHAUS,
REMARK 3 C.SIETHOFF,H.S.COSTA,B.GONZALEZ,H.SANTOS,
REMARK 3 J.E.SUAREZ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1E8J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-SEP-00.
REMARK 100 THE DEPOSITION ID IS D_1290005387.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 7.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-1H-NOESY 2D-1H-TOCSY 2D-1H
REMARK 210 -COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : INDYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS WITH
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 500
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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 O TYR A 4 H TYR A 13 1.52
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 ASP A 2 45.71 173.38
REMARK 500 1 ASP A 14 99.85 50.22
REMARK 500 1 SER A 22 -26.88 159.87
REMARK 500 1 PRO A 34 165.54 -42.31
REMARK 500 1 ASP A 36 18.21 -144.87
REMARK 500 1 CYS A 39 100.31 -42.20
REMARK 500 1 ALA A 44 133.05 -24.68
REMARK 500 1 SER A 45 -175.41 -57.75
REMARK 500 1 LYS A 46 38.65 -90.53
REMARK 500 1 LYS A 51 100.71 -42.62
REMARK 500 2 CYS A 9 -68.40 -120.20
REMARK 500 2 ASP A 21 -74.52 -133.62
REMARK 500 2 PRO A 34 165.27 -42.30
REMARK 500 2 ASP A 36 20.68 -148.80
REMARK 500 2 CYS A 39 100.68 -42.98
REMARK 500 2 ALA A 44 135.13 -26.11
REMARK 500 2 SER A 45 -171.57 -60.28
REMARK 500 2 LYS A 46 36.00 -91.08
REMARK 500 2 PHE A 49 149.46 -36.07
REMARK 500 2 LYS A 51 98.20 -44.63
REMARK 500 3 ASP A 2 96.60 -171.88
REMARK 500 3 CYS A 9 -67.81 -120.17
REMARK 500 3 TYR A 11 -151.26 35.29
REMARK 500 3 GLU A 12 82.92 163.58
REMARK 500 3 PRO A 20 -164.11 -60.73
REMARK 500 3 ASP A 21 33.59 81.62
REMARK 500 3 SER A 22 95.39 69.82
REMARK 500 3 PRO A 34 163.38 -41.11
REMARK 500 3 ASP A 36 22.07 -151.70
REMARK 500 3 CYS A 39 100.81 -43.32
REMARK 500 3 ALA A 44 131.57 -23.55
REMARK 500 3 SER A 45 -170.89 -58.67
REMARK 500 3 LYS A 46 30.92 -92.28
REMARK 500 3 PHE A 49 149.62 -36.53
REMARK 500 3 LYS A 51 98.20 -40.20
REMARK 500 4 ASP A 2 135.74 -172.64
REMARK 500 4 CYS A 9 -68.91 -120.32
REMARK 500 4 TYR A 11 -150.18 34.68
REMARK 500 4 GLU A 12 80.25 163.08
REMARK 500 4 ASP A 21 60.92 179.26
REMARK 500 4 SER A 22 52.55 39.57
REMARK 500 4 PRO A 34 -70.82 -31.87
REMARK 500 4 ASP A 35 -49.39 151.80
REMARK 500 4 CYS A 39 101.34 -44.43
REMARK 500 4 ALA A 44 128.79 -21.64
REMARK 500 4 SER A 45 -171.76 -53.78
REMARK 500 4 LYS A 46 30.34 -92.83
REMARK 500 4 PHE A 49 149.81 -35.78
REMARK 500 4 LYS A 51 98.30 -40.51
REMARK 500 5 ASP A 2 -72.99 165.05
REMARK 500
REMARK 500 THIS ENTRY HAS 210 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1E8J A 1 52 UNP P00270 RUBR_DESGI 1 52
SEQRES 1 A 52 MET ASP ILE TYR VAL CYS THR VAL CYS GLY TYR GLU TYR
SEQRES 2 A 52 ASP PRO ALA LYS GLY ASP PRO ASP SER GLY ILE LYS PRO
SEQRES 3 A 52 GLY THR LYS PHE GLU ASP LEU PRO ASP ASP TRP ALA CYS
SEQRES 4 A 52 PRO VAL CYS GLY ALA SER LYS ASP ALA PHE GLU LYS GLN
SHEET 1 A 2 TYR A 4 VAL A 5 0
SHEET 2 A 2 GLU A 50 LYS A 51 -1 O GLU A 50 N VAL A 5
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 - t 9 2 Bytes