Header list of 1ji8.pdb file
Complete list - b 23 2 Bytes
HEADER OXIDOREDUCTASE 29-JUN-01 1JI8
TITLE SOLUTION STRUCTURE OF PYROBACULUM AEROPHILUM DSRC/GAMMA SUBUNIT OF
TITLE 2 DISSIMILATORY SULFITE REDUCTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DISSIMILATORY SIROHEME-SULFITE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GAMMA SUBUNIT;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROBACULUM AEROPHILUM;
SOURCE 3 ORGANISM_TAXID: 13773;
SOURCE 4 GENE: DSRC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL221(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET28B
KEYWDS ORTHOGONAL HELICAL BUNDLE, STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 3 NESG, OXIDOREDUCTASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.R.CORT,M.A.KENNEDY,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 4 23-FEB-22 1JI8 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1JI8 1 VERSN
REVDAT 2 25-JAN-05 1JI8 1 AUTHOR KEYWDS REMARK
REVDAT 1 05-DEC-01 1JI8 0
JRNL AUTH J.R.CORT,S.V.MARIAPPAN,C.Y.KIM,M.S.PARK,T.S.PEAT,G.S.WALDO,
JRNL AUTH 2 T.C.TERWILLIGER,M.A.KENNEDY
JRNL TITL SOLUTION STRUCTURE OF PYROBACULUM AEROPHILUM DSRC, AN
JRNL TITL 2 ARCHAEAL HOMOLOGUE OF THE GAMMA SUBUNIT OF DISSIMILATORY
JRNL TITL 3 SULFITE REDUCTASE.
JRNL REF EUR.J.BIOCHEM. V. 268 5842 2001
JRNL REFN ISSN 0014-2956
JRNL PMID 11722571
JRNL DOI 10.1046/J.0014-2956.2001.02529.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.84, X-PLOR 3.84
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 504 NOE-DERIVED DISTANCE RESTRAINTS, 56
REMARK 3 H-BOND RESTRAINTS (2 PER H-BOND), 89 DIHEDRAL RESTRAINTS (50 PHI,
REMARK 3 39 PSI)
REMARK 4
REMARK 4 1JI8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013802.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 100 MM SALT, 25 MM PHOSPHATE
REMARK 210 BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM DSRC U-15N, 25 MM PHOSPHATE
REMARK 210 BUFFER, PH 7.4, 100 MM NACL, 90%
REMARK 210 H2O, 10% D2O; 2 MM DSRC U-13C,
REMARK 210 15N, 25 MM PHOSPHATE BUFFER, PH
REMARK 210 7.4, 100 MM NACL, 90% H2O, 10%
REMARK 210 D2O; 2 MM DSRC U-13C,15N, 25 MM
REMARK 210 PHOSPHATE BUFFER, PH* 7.0 100 MM
REMARK 210 NACL, 99% D2O; 2 MM DSRC U-15N,
REMARK 210 25 MM PHOSPHATE BUFFER, PH* 7.0
REMARK 210 100 MM NACL, 99% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C-SEPARATED_NOESY;
REMARK 210 3D_13C,15N-SIMULTANEOUS NOESY;
REMARK 210 3D_15N-SEPARATED_NOESY; HNHA; 1H-
REMARK 210 15N, HSQC D2O EXCHANGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, VNMR
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 24
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
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: 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 LYS A 4 87.52 -65.15
REMARK 500 1 ASP A 12 74.49 41.38
REMARK 500 1 ASN A 26 68.67 -157.71
REMARK 500 1 LEU A 42 -66.07 -93.01
REMARK 500 1 THR A 49 -169.15 -71.58
REMARK 500 1 PRO A 71 -160.46 -73.07
REMARK 500 1 THR A 79 -74.50 -159.41
REMARK 500 1 ALA A 95 -85.20 -64.99
REMARK 500 1 PRO A 107 -89.99 -72.74
REMARK 500 1 CYS A 110 97.72 58.87
REMARK 500 2 ASP A 21 51.13 -116.79
REMARK 500 2 LEU A 42 -79.49 -83.85
REMARK 500 2 GLU A 43 -79.28 -83.68
REMARK 500 2 PHE A 66 -75.41 -78.90
REMARK 500 2 PRO A 71 -160.21 -72.92
REMARK 500 2 LYS A 73 -44.06 -141.58
REMARK 500 2 THR A 79 -70.69 -68.91
REMARK 500 2 PHE A 81 170.88 -52.18
REMARK 500 2 PRO A 94 -92.45 -72.90
REMARK 500 2 ALA A 95 -89.96 49.60
REMARK 500 3 ASP A 12 -89.66 55.69
REMARK 500 3 ASP A 19 -161.70 -75.42
REMARK 500 3 MET A 24 106.60 -52.61
REMARK 500 3 ASN A 26 68.25 -151.74
REMARK 500 3 ASP A 31 -160.06 -165.65
REMARK 500 3 LEU A 42 -73.54 -91.39
REMARK 500 3 GLU A 43 -76.49 -82.43
REMARK 500 3 LYS A 47 130.58 -177.78
REMARK 500 3 PHE A 66 -35.94 -137.00
REMARK 500 3 PRO A 71 -90.08 -73.40
REMARK 500 3 ILE A 72 74.15 -175.51
REMARK 500 3 LYS A 73 -63.78 -124.88
REMARK 500 3 GLU A 78 -71.00 -102.88
REMARK 500 3 SER A 92 86.17 -67.16
REMARK 500 3 ALA A 104 78.73 177.93
REMARK 500 3 CYS A 110 172.02 -48.22
REMARK 500 4 ASP A 19 -172.94 -59.74
REMARK 500 4 ASP A 29 -81.86 -97.41
REMARK 500 4 TRP A 30 120.34 59.47
REMARK 500 4 GLU A 43 -83.29 -110.24
REMARK 500 4 PRO A 71 -161.95 -72.94
REMARK 500 4 GLU A 78 -78.43 -90.57
REMARK 500 4 SER A 92 94.75 -66.28
REMARK 500 4 ALA A 95 -88.66 -73.50
REMARK 500 4 LYS A 106 77.09 -151.24
REMARK 500 4 THR A 108 -158.72 -106.72
REMARK 500 5 ASP A 12 73.04 43.20
REMARK 500 5 ASP A 19 -162.77 -58.77
REMARK 500 5 ASP A 21 44.26 -106.99
REMARK 500 5 TRP A 30 158.73 -46.32
REMARK 500
REMARK 500 THIS ENTRY HAS 253 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 40 0.26 SIDE CHAIN
REMARK 500 1 ARG A 60 0.31 SIDE CHAIN
REMARK 500 2 ARG A 40 0.27 SIDE CHAIN
REMARK 500 2 ARG A 60 0.24 SIDE CHAIN
REMARK 500 3 ARG A 40 0.27 SIDE CHAIN
REMARK 500 3 ARG A 60 0.17 SIDE CHAIN
REMARK 500 4 ARG A 40 0.29 SIDE CHAIN
REMARK 500 4 ARG A 60 0.20 SIDE CHAIN
REMARK 500 5 ARG A 40 0.20 SIDE CHAIN
REMARK 500 5 ARG A 60 0.27 SIDE CHAIN
REMARK 500 6 ARG A 40 0.19 SIDE CHAIN
REMARK 500 6 ARG A 60 0.25 SIDE CHAIN
REMARK 500 7 ARG A 40 0.29 SIDE CHAIN
REMARK 500 7 ARG A 60 0.32 SIDE CHAIN
REMARK 500 8 ARG A 40 0.31 SIDE CHAIN
REMARK 500 8 ARG A 60 0.19 SIDE CHAIN
REMARK 500 9 ARG A 40 0.19 SIDE CHAIN
REMARK 500 9 ARG A 60 0.31 SIDE CHAIN
REMARK 500 10 ARG A 40 0.31 SIDE CHAIN
REMARK 500 10 ARG A 60 0.24 SIDE CHAIN
REMARK 500 11 ARG A 40 0.31 SIDE CHAIN
REMARK 500 11 ARG A 60 0.28 SIDE CHAIN
REMARK 500 12 ARG A 40 0.09 SIDE CHAIN
REMARK 500 12 ARG A 60 0.31 SIDE CHAIN
REMARK 500 13 ARG A 40 0.15 SIDE CHAIN
REMARK 500 13 ARG A 60 0.31 SIDE CHAIN
REMARK 500 14 ARG A 40 0.11 SIDE CHAIN
REMARK 500 14 ARG A 60 0.17 SIDE CHAIN
REMARK 500 15 ARG A 40 0.31 SIDE CHAIN
REMARK 500 15 ARG A 60 0.11 SIDE CHAIN
REMARK 500 16 ARG A 40 0.25 SIDE CHAIN
REMARK 500 16 ARG A 60 0.25 SIDE CHAIN
REMARK 500 17 ARG A 40 0.26 SIDE CHAIN
REMARK 500 17 ARG A 60 0.26 SIDE CHAIN
REMARK 500 18 ARG A 40 0.23 SIDE CHAIN
REMARK 500 18 ARG A 60 0.22 SIDE CHAIN
REMARK 500 19 ARG A 40 0.20 SIDE CHAIN
REMARK 500 19 ARG A 60 0.32 SIDE CHAIN
REMARK 500 20 ARG A 40 0.30 SIDE CHAIN
REMARK 500 20 ARG A 60 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: OP1 RELATED DB: TARGETDB
DBREF 1JI8 A 1 111 UNP Q8ZUX1 Q8ZUX1_PYRAE 1 111
SEQADV 1JI8 GLN A 10 UNP Q8ZUX1 LYS 10 CONFLICT
SEQADV 1JI8 GLY A 13 UNP Q8ZUX1 ASP 13 CONFLICT
SEQADV 1JI8 LYS A 14 UNP Q8ZUX1 VAL 14 CONFLICT
SEQADV 1JI8 LYS A 15 UNP Q8ZUX1 THR 15 CONFLICT
SEQADV 1JI8 VAL A 16 UNP Q8ZUX1 ILE 16 CONFLICT
SEQADV 1JI8 ASP A 21 UNP Q8ZUX1 GLU 21 CONFLICT
SEQADV 1JI8 MET A 24 UNP Q8ZUX1 LEU 24 CONFLICT
SEQADV 1JI8 GLN A 25 UNP Q8ZUX1 SER 25 CONFLICT
SEQADV 1JI8 ASP A 29 UNP Q8ZUX1 VAL 29 CONFLICT
SEQADV 1JI8 ASP A 31 UNP Q8ZUX1 ASN 31 CONFLICT
SEQADV 1JI8 LEU A 38 UNP Q8ZUX1 MET 38 CONFLICT
SEQADV 1JI8 GLU A 51 UNP Q8ZUX1 ASP 51 CONFLICT
SEQADV 1JI8 LEU A 55 UNP Q8ZUX1 VAL 55 CONFLICT
SEQADV 1JI8 PHE A 66 UNP Q8ZUX1 TYR 66 CONFLICT
SEQADV 1JI8 THR A 68 UNP Q8ZUX1 VAL 68 CONFLICT
SEQADV 1JI8 VAL A 75 UNP Q8ZUX1 LEU 75 CONFLICT
SEQADV 1JI8 THR A 76 UNP Q8ZUX1 LEU 76 CONFLICT
SEQADV 1JI8 SER A 82 UNP Q8ZUX1 THR 82 CONFLICT
SEQADV 1JI8 LYS A 85 UNP Q8ZUX1 GLN 85 CONFLICT
SEQADV 1JI8 HIS A 96 UNP Q8ZUX1 ASN 96 CONFLICT
SEQRES 1 A 111 MET PRO VAL LYS CYS PRO GLY GLU TYR GLN VAL ASP GLY
SEQRES 2 A 111 LYS LYS VAL ILE LEU ASP GLU ASP CYS PHE MET GLN ASN
SEQRES 3 A 111 PRO GLU ASP TRP ASP GLU LYS VAL ALA GLU TRP LEU ALA
SEQRES 4 A 111 ARG GLU LEU GLU GLY ILE GLN LYS MET THR GLU GLU HIS
SEQRES 5 A 111 TRP LYS LEU VAL LYS TYR LEU ARG GLU TYR TRP GLU THR
SEQRES 6 A 111 PHE GLY THR CYS PRO PRO ILE LYS MET VAL THR LYS GLU
SEQRES 7 A 111 THR GLY PHE SER LEU GLU LYS ILE TYR GLN LEU PHE PRO
SEQRES 8 A 111 SER GLY PRO ALA HIS GLY ALA CYS LYS VAL ALA GLY ALA
SEQRES 9 A 111 PRO LYS PRO THR GLY CYS VAL
HELIX 1 1 GLU A 20 CYS A 22 5 3
HELIX 2 2 ASN A 26 TRP A 30 5 5
HELIX 3 3 ASP A 31 GLU A 43 1 13
HELIX 4 4 THR A 49 TRP A 63 1 15
HELIX 5 5 MET A 74 THR A 79 5 6
HELIX 6 6 SER A 82 PHE A 90 1 9
HELIX 7 7 GLY A 93 GLY A 103 1 11
SHEET 1 A 3 GLY A 7 GLN A 10 0
SHEET 2 A 3 LYS A 15 ASP A 19 -1 N VAL A 16 O TYR A 9
SHEET 3 A 3 PHE A 23 MET A 24 -1 O PHE A 23 N ASP A 19
SSBOND 1 CYS A 5 CYS A 22 1555 1555 2.02
SSBOND 2 CYS A 69 CYS A 99 1555 1555 2.02
CISPEP 1 CYS A 5 PRO A 6 1 -0.23
CISPEP 2 CYS A 5 PRO A 6 2 -0.26
CISPEP 3 CYS A 5 PRO A 6 3 -0.15
CISPEP 4 CYS A 5 PRO A 6 4 -0.27
CISPEP 5 CYS A 5 PRO A 6 5 -0.31
CISPEP 6 CYS A 5 PRO A 6 6 0.00
CISPEP 7 CYS A 5 PRO A 6 7 -0.19
CISPEP 8 CYS A 5 PRO A 6 8 -0.11
CISPEP 9 CYS A 5 PRO A 6 9 -0.25
CISPEP 10 CYS A 5 PRO A 6 10 -0.14
CISPEP 11 CYS A 5 PRO A 6 11 -0.27
CISPEP 12 CYS A 5 PRO A 6 12 -0.35
CISPEP 13 CYS A 5 PRO A 6 13 -0.26
CISPEP 14 CYS A 5 PRO A 6 14 -0.11
CISPEP 15 CYS A 5 PRO A 6 15 -0.32
CISPEP 16 CYS A 5 PRO A 6 16 -0.31
CISPEP 17 CYS A 5 PRO A 6 17 -0.35
CISPEP 18 CYS A 5 PRO A 6 18 -0.14
CISPEP 19 CYS A 5 PRO A 6 19 -0.26
CISPEP 20 CYS A 5 PRO A 6 20 -0.15
CRYST1 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 23 2 Bytes