Header list of 1ib8.pdb file
Complete list - 23 20 Bytes
HEADER NUCLEIC ACID BINDING PROTEIN 27-MAR-01 1IB8
TITLE SOLUTION STRUCTURE AND FUNCTION OF A CONSERVED PROTEIN SP14.3 ENCODED
TITLE 2 BY AN ESSENTIAL STREPTOCOCCUS PNEUMONIAE GENE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CONSERVED PROTEIN SP14.3;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 1313;
SOURCE 4 GENE: ESSENTIAL GENE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS NUCLEIC ACID BINDING PROTEIN, RIBOSOMAL PROTEIN, ESSENTIAL GENE,
KEYWDS 2 STRUCTURAL GENOMICS
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR L.YU,A.H.GUNASEKERA,J.MACK,E.T.OLEJNICZAK,L.E.CHOVAN,X.RUAN,
AUTHOR 2 D.L.TOWNE,C.G.LERNER,S.W.FESIK
REVDAT 3 23-FEB-22 1IB8 1 REMARK
REVDAT 2 24-FEB-09 1IB8 1 VERSN
REVDAT 1 27-MAR-02 1IB8 0
JRNL AUTH L.YU,A.H.GUNASEKERA,J.MACK,E.T.OLEJNICZAK,L.E.CHOVAN,X.RUAN,
JRNL AUTH 2 D.L.TOWNE,C.G.LERNER,S.W.FESIK
JRNL TITL SOLUTION STRUCTURE AND FUNCTION OF A CONSERVED PROTEIN
JRNL TITL 2 SP14.3 ENCODED BY AN ESSENTIAL STREPTOCOCCUS PNEUMONIAE GENE
JRNL REF J.MOL.BIOL. V. 311 593 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11493012
JRNL DOI 10.1006/JMBI.2001.4894
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : IN-HOUSE SOFTWARE, CNX 2000
REMARK 3 AUTHORS : BRUNGER (CNX)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IB8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013121.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM SP14.3 15N-LABELED, 15N,13C
REMARK 210 -LABELED, AND 15N,13C,2H-LABELED
REMARK 210 WITH SELECTIVELY PROTONATED
REMARK 210 METHYL GROUPS. 50 MM BISTRIS HCL,
REMARK 210 PH 6.5, 50 MM AMMONIUM SULPHATE.
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY, TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNX SOFTWARE 2000 PARALLEL
REMARK 210 METHOD USED : DISTANCE GEOMETRY/SIMULATED
REMARK 210 ANNEALING PROTOCOL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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.
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 SER A 2 -175.78 -174.12
REMARK 500 ASP A 5 130.99 -177.64
REMARK 500 VAL A 21 -71.49 -162.16
REMARK 500 ALA A 24 172.57 58.78
REMARK 500 SER A 38 41.00 -153.47
REMARK 500 GLU A 50 88.25 178.62
REMARK 500 ILE A 52 172.69 54.70
REMARK 500 THR A 53 -174.31 174.41
REMARK 500 ASP A 69 31.30 -98.47
REMARK 500 THR A 70 31.58 -144.43
REMARK 500 ILE A 71 46.19 -94.04
REMARK 500 ASP A 74 72.60 174.69
REMARK 500 GLU A 78 -44.52 169.47
REMARK 500 LEU A 89 -69.43 -157.42
REMARK 500 GLU A 90 -35.36 170.90
REMARK 500 ARG A 91 70.97 -167.34
REMARK 500 LEU A 93 31.66 -99.82
REMARK 500 ALA A 102 -79.45 -48.08
REMARK 500 VAL A 103 96.83 44.49
REMARK 500 GLN A 113 -80.94 -115.63
REMARK 500 ALA A 114 148.01 170.40
REMARK 500 ASP A 116 59.61 -147.53
REMARK 500 PRO A 149 -158.20 -58.05
REMARK 500 SER A 151 31.25 155.92
REMARK 500 LEU A 152 24.20 -142.85
REMARK 500 LEU A 162 173.97 59.18
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IB8 A 5 162 UNP Q97S61 Y552_STRPN 2 159
SEQRES 1 A 164 GLY SER GLY VAL ASP ALA ILE ALA THR ILE VAL GLU LEU
SEQRES 2 A 164 VAL ARG GLU VAL VAL GLU PRO VAL ILE GLU ALA PRO PHE
SEQRES 3 A 164 GLU LEU VAL ASP ILE GLU TYR GLY LYS ILE GLY SER ASP
SEQRES 4 A 164 MET ILE LEU SER ILE PHE VAL ASP LYS PRO GLU GLY ILE
SEQRES 5 A 164 THR LEU ASN ASP THR ALA ASP LEU THR GLU MET ILE SER
SEQRES 6 A 164 PRO VAL LEU ASP THR ILE LYS PRO ASP PRO PHE PRO GLU
SEQRES 7 A 164 GLN TYR PHE LEU GLU ILE THR SER PRO GLY LEU GLU ARG
SEQRES 8 A 164 PRO LEU LYS THR LYS ASP ALA VAL ALA GLY ALA VAL GLY
SEQRES 9 A 164 LYS TYR ILE HIS VAL GLY LEU TYR GLN ALA ILE ASP LYS
SEQRES 10 A 164 GLN LYS VAL PHE GLU GLY THR LEU LEU ALA PHE GLU GLU
SEQRES 11 A 164 ASP GLU LEU THR MET GLU TYR MET ASP LYS THR ARG LYS
SEQRES 12 A 164 LYS THR VAL GLN ILE PRO TYR SER LEU VAL SER LYS ALA
SEQRES 13 A 164 ARG LEU ALA VAL LYS LEU LEU GLU
HELIX 1 1 ASP A 5 GLU A 19 1 15
HELIX 2 2 THR A 53 SER A 65 1 13
HELIX 3 3 THR A 95 VAL A 103 1 9
SHEET 1 A 3 GLU A 27 ILE A 36 0
SHEET 2 A 3 ASP A 39 ASP A 47 -1 O ASP A 39 N ILE A 36
SHEET 3 A 3 TYR A 80 THR A 85 1 O PHE A 81 N LEU A 42
SHEET 1 B 5 LYS A 143 ILE A 148 0
SHEET 2 B 5 GLU A 132 MET A 138 -1 N LEU A 133 O ILE A 148
SHEET 3 B 5 VAL A 120 GLU A 129 -1 N GLU A 122 O MET A 138
SHEET 4 B 5 LYS A 105 GLY A 110 -1 O LYS A 105 N LEU A 125
SHEET 5 B 5 LYS A 155 ALA A 159 -1 N ARG A 157 O HIS A 108
CISPEP 1 ALA A 24 PRO A 25 0 -0.38
CISPEP 2 LYS A 72 PRO A 73 0 -0.02
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
Complete list - 23 20 Bytes