Header list of 2cp9.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 19-MAY-05 2CP9
TITLE SOLUTION STRUCTURE OF RSGI RUH-042, A UBA DOMAIN FROM HUMAN
TITLE 2 MITOCHONDRIAL ELONGATION FACTOR TS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR TS, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UBA;
COMPND 5 SYNONYM: EF-TS, EF-TSMT;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P041220-07;
SOURCE 7 OTHER_DETAILS: CELL-FREE (E.COLI)
KEYWDS UBA, STRUCTURAL GENOMICS, HUMAN, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.OHASHI,H.HIROTA,K.IZUMI,M.YOSHIDA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CP9 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CP9 1 VERSN
REVDAT 1 19-NOV-05 2CP9 0
JRNL AUTH W.OHASHI,H.HIROTA,K.IZUMI,M.YOSHIDA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RSGI RUH-042, A UBA DOMAIN FROM HUMAN
JRNL TITL 2 MITOCHONDRIAL ELONGATION FACTOR TS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DELTA NMR 4.3, CYANA 2.0.17
REMARK 3 AUTHORS : JEOL (DELTA NMR), GUNTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CP9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024474.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.23MM RSGI RUH-042 U-13C, 15N;
REMARK 210 20MM TRIS-HCL U-2H, 100MM NACL,
REMARK 210 1MM DTT U-2H, 0.02% NAN3; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : ECA
REMARK 210 SPECTROMETER MANUFACTURER : JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 2.0.17
REMARK 210 METHOD USED : SIMULATED ANNELING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 1 SER A 5 96.58 -65.53
REMARK 500 1 TRP A 44 -72.44 -56.25
REMARK 500 1 ALA A 57 147.73 -36.33
REMARK 500 2 SER A 3 103.20 -48.53
REMARK 500 2 TYR A 22 159.97 -44.10
REMARK 500 2 SER A 23 176.11 -47.83
REMARK 500 2 CYS A 34 43.47 -99.34
REMARK 500 3 SER A 2 119.19 -37.00
REMARK 500 3 LYS A 29 -71.85 -76.63
REMARK 500 3 LYS A 56 -58.15 -125.55
REMARK 500 4 SER A 9 41.33 -82.48
REMARK 500 4 SER A 23 168.86 -44.58
REMARK 500 4 CYS A 34 -72.46 -79.00
REMARK 500 4 LYS A 51 -70.06 -74.94
REMARK 500 4 SER A 55 161.06 -42.22
REMARK 500 5 TYR A 22 153.58 -40.35
REMARK 500 5 ASN A 26 -70.41 -67.73
REMARK 500 5 LYS A 29 -71.65 -73.59
REMARK 500 5 ALA A 30 -39.73 -39.56
REMARK 500 6 SER A 2 98.97 -51.33
REMARK 500 6 LEU A 38 -38.53 -34.23
REMARK 500 6 TRP A 44 -70.39 -67.43
REMARK 500 6 TRP A 54 44.01 -83.10
REMARK 500 6 ALA A 58 92.59 -69.29
REMARK 500 7 SER A 23 156.41 -44.91
REMARK 500 7 ASP A 37 76.57 -117.87
REMARK 500 7 SER A 63 48.60 36.05
REMARK 500 8 TYR A 22 171.64 -45.65
REMARK 500 8 TRP A 54 88.23 -68.27
REMARK 500 8 PRO A 61 2.77 -69.73
REMARK 500 8 SER A 63 -64.68 -104.49
REMARK 500 9 SER A 5 89.60 -69.82
REMARK 500 9 LYS A 29 -71.09 -73.04
REMARK 500 9 ASP A 37 76.93 -118.86
REMARK 500 9 SER A 59 79.87 -113.56
REMARK 500 10 SER A 3 107.79 -54.02
REMARK 500 10 SER A 5 171.14 -53.23
REMARK 500 10 SER A 8 137.97 -37.92
REMARK 500 10 TYR A 22 146.45 -37.50
REMARK 500 11 SER A 8 107.41 -51.10
REMARK 500 11 SER A 9 48.83 -81.36
REMARK 500 11 SER A 62 140.62 -37.61
REMARK 500 12 SER A 23 150.73 -42.94
REMARK 500 12 PRO A 61 -177.48 -69.82
REMARK 500 13 SER A 3 -39.63 -38.75
REMARK 500 13 LYS A 10 -61.57 -101.09
REMARK 500 13 TYR A 22 166.08 -43.71
REMARK 500 13 SER A 23 173.64 -46.55
REMARK 500 14 SER A 23 156.44 -37.62
REMARK 500 15 SER A 6 176.77 -59.98
REMARK 500
REMARK 500 THIS ENTRY HAS 79 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002012647.1 RELATED DB: TARGETDB
DBREF 2CP9 A 8 58 UNP P43897 EFTS_HUMAN 45 95
SEQADV 2CP9 GLY A 1 UNP P43897 CLONING ARTIFACT
SEQADV 2CP9 SER A 2 UNP P43897 CLONING ARTIFACT
SEQADV 2CP9 SER A 3 UNP P43897 CLONING ARTIFACT
SEQADV 2CP9 GLY A 4 UNP P43897 CLONING ARTIFACT
SEQADV 2CP9 SER A 5 UNP P43897 CLONING ARTIFACT
SEQADV 2CP9 SER A 6 UNP P43897 CLONING ARTIFACT
SEQADV 2CP9 GLY A 7 UNP P43897 CLONING ARTIFACT
SEQADV 2CP9 SER A 59 UNP P43897 CLONING ARTIFACT
SEQADV 2CP9 GLY A 60 UNP P43897 CLONING ARTIFACT
SEQADV 2CP9 PRO A 61 UNP P43897 CLONING ARTIFACT
SEQADV 2CP9 SER A 62 UNP P43897 CLONING ARTIFACT
SEQADV 2CP9 SER A 63 UNP P43897 CLONING ARTIFACT
SEQADV 2CP9 GLY A 64 UNP P43897 CLONING ARTIFACT
SEQRES 1 A 64 GLY SER SER GLY SER SER GLY SER SER LYS GLU LEU LEU
SEQRES 2 A 64 MET LYS LEU ARG ARG LYS THR GLY TYR SER PHE VAL ASN
SEQRES 3 A 64 CYS LYS LYS ALA LEU GLU THR CYS GLY GLY ASP LEU LYS
SEQRES 4 A 64 GLN ALA GLU ILE TRP LEU HIS LYS GLU ALA GLN LYS GLU
SEQRES 5 A 64 GLY TRP SER LYS ALA ALA SER GLY PRO SER SER GLY
HELIX 1 1 LYS A 10 GLY A 21 1 12
HELIX 2 2 SER A 23 GLY A 35 1 13
HELIX 3 3 ASP A 37 GLY A 53 1 17
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 - r 9 2 Bytes