Header list of 1k8h.pdb file
Complete list - b 23 2 Bytes
HEADER RNA BINDING PROTEIN 24-OCT-01 1K8H
TITLE NMR STRUCTURE OF SMALL PROTEIN B (SMPB) FROM AQUIFEX AEOLICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SMALL PROTEIN B;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SSRA-BINDING PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SMPB, SSRA ASSOCIATED PROTEIN, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR G.DONG,D.W.HOFFMAN
REVDAT 4 23-FEB-22 1K8H 1 REMARK
REVDAT 3 24-FEB-09 1K8H 1 VERSN
REVDAT 2 10-APR-02 1K8H 1 JRNL
REVDAT 1 20-MAR-02 1K8H 0
JRNL AUTH G.DONG,J.NOWAKOWSKI,D.W.HOFFMAN
JRNL TITL STRUCTURE OF SMALL PROTEIN B: THE PROTEIN COMPONENT OF THE
JRNL TITL 2 TMRNA-SMPB SYSTEM FOR RIBOSOME RESCUE.
JRNL REF EMBO J. V. 21 1845 2002
JRNL REFN ISSN 0261-4189
JRNL PMID 11927568
JRNL DOI 10.1093/EMBOJ/21.7.1845
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K8H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-01.
REMARK 100 THE DEPOSITION ID IS D_1000014691.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 100 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM SMPB
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS SOLVED USING STANDARD 2D AND 3D
REMARK 210 HETERONUCLEAR NMR TECHNIQUES.
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 2 -60.06 -98.93
REMARK 500 1 SER A 3 -169.56 -75.48
REMARK 500 1 ASP A 4 179.64 60.58
REMARK 500 1 LYS A 5 27.63 -148.53
REMARK 500 1 ALA A 10 168.09 54.06
REMARK 500 1 LYS A 13 -34.23 174.49
REMARK 500 1 LEU A 22 -68.77 -109.95
REMARK 500 1 LYS A 32 -166.36 -57.07
REMARK 500 1 LYS A 42 -82.15 -57.44
REMARK 500 1 PHE A 47 -68.91 -120.87
REMARK 500 1 ASN A 56 -96.07 54.58
REMARK 500 1 TYR A 65 46.81 -148.07
REMARK 500 1 PRO A 68 160.58 -47.93
REMARK 500 1 ILE A 74 33.34 -98.82
REMARK 500 1 LEU A 80 -51.02 -130.54
REMARK 500 1 ARG A 81 79.75 54.29
REMARK 500 1 LEU A 86 174.19 -49.27
REMARK 500 1 LEU A 87 -156.26 -172.68
REMARK 500 1 HIS A 88 -160.65 -105.33
REMARK 500 1 LEU A 109 -99.70 -123.75
REMARK 500 1 ASN A 115 -57.46 73.45
REMARK 500 1 ASN A 116 -7.44 -177.22
REMARK 500 1 LYS A 128 155.79 61.78
REMARK 500 1 LYS A 129 -175.48 -175.73
REMARK 500 1 LEU A 130 -79.37 63.79
REMARK 500 2 ASP A 4 104.74 57.11
REMARK 500 2 ALA A 10 164.68 55.23
REMARK 500 2 GLU A 11 102.11 179.53
REMARK 500 2 LYS A 13 33.73 -162.69
REMARK 500 2 LYS A 18 77.12 -156.63
REMARK 500 2 TYR A 19 122.60 175.96
REMARK 500 2 LEU A 22 -69.33 -130.07
REMARK 500 2 LYS A 32 69.31 -164.39
REMARK 500 2 SER A 34 -41.45 82.86
REMARK 500 2 LYS A 42 78.47 -165.24
REMARK 500 2 VAL A 45 161.56 51.63
REMARK 500 2 PHE A 47 121.92 -170.67
REMARK 500 2 LYS A 48 -179.64 60.11
REMARK 500 2 ASP A 49 -13.05 80.12
REMARK 500 2 ASN A 56 -102.83 55.68
REMARK 500 2 LYS A 70 99.67 -172.52
REMARK 500 2 GLU A 75 127.17 63.11
REMARK 500 2 HIS A 77 -67.66 68.81
REMARK 500 2 LEU A 87 -130.24 -138.47
REMARK 500 2 HIS A 88 -84.17 -125.40
REMARK 500 2 LYS A 89 -72.68 174.09
REMARK 500 2 VAL A 99 -70.24 -49.90
REMARK 500 2 LEU A 109 -98.89 -123.04
REMARK 500 2 ASN A 115 -56.27 72.32
REMARK 500 2 ASN A 116 -11.78 -177.58
REMARK 500
REMARK 500 THIS ENTRY HAS 258 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1K8H A 1 133 UNP O66640 SSRP_AQUAE 2 134
SEQRES 1 A 133 GLY LYS SER ASP LYS ILE ILE PRO ILE ALA GLU ASN LYS
SEQRES 2 A 133 GLU ALA LYS ALA LYS TYR ASP ILE LEU GLU THR TYR GLU
SEQRES 3 A 133 ALA GLY ILE VAL LEU LYS GLY SER GLU VAL LYS SER LEU
SEQRES 4 A 133 ARG GLU LYS GLY THR VAL SER PHE LYS ASP SER PHE VAL
SEQRES 5 A 133 ARG ILE GLU ASN GLY GLU ALA TRP LEU TYR ASN LEU TYR
SEQRES 6 A 133 ILE ALA PRO TYR LYS HIS ALA THR ILE GLU ASN HIS ASP
SEQRES 7 A 133 PRO LEU ARG LYS ARG LYS LEU LEU LEU HIS LYS ARG GLU
SEQRES 8 A 133 ILE MET ARG LEU TYR GLY LYS VAL GLN GLU LYS GLY TYR
SEQRES 9 A 133 THR ILE ILE PRO LEU LYS LEU TYR TRP LYS ASN ASN LYS
SEQRES 10 A 133 VAL LYS VAL LEU ILE ALA LEU ALA LYS GLY LYS LYS LEU
SEQRES 11 A 133 TYR ASP ARG
HELIX 1 1 LYS A 13 TYR A 19 1 7
HELIX 2 2 GLY A 33 GLY A 43 1 11
HELIX 3 3 LYS A 89 GLY A 103 1 15
SHEET 1 A 3 ILE A 21 ILE A 29 0
SHEET 2 A 3 LYS A 117 ALA A 125 -1 O VAL A 120 N ALA A 27
SHEET 3 A 3 THR A 105 LYS A 114 -1 N TYR A 112 O LYS A 119
SHEET 1 B 3 SER A 50 GLU A 55 0
SHEET 2 B 3 GLU A 58 ASN A 63 -1 O TYR A 62 N PHE A 51
SHEET 3 B 3 ARG A 83 LEU A 85 -1 O ARG A 83 N LEU A 61
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 23 2 Bytes