Header list of 1wwt.pdb file
Complete list - r 2 2 Bytes
HEADER LIGASE 18-JAN-05 1WWT
TITLE SOLUTION STRUCTURE OF THE TGS DOMAIN FROM HUMAN THREONYL-TRNA
TITLE 2 SYNTHETASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THREONYL-TRNA SYNTHETASE, CYTOPLASMIC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TGS DOMAIN;
COMPND 5 SYNONYM: THREONINE--TRNA LIGASE, THRRS;
COMPND 6 EC: 6.1.1.3;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: THRS;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040524-03;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS TGS DOMAIN, THREONYL-TRNA SYNTHETASE, STRUCTURAL GENOMICS, RIKEN
KEYWDS 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.CHIKAYAMA,T.KIGAWA,T.TOMIZAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WWT 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WWT 1 VERSN
REVDAT 1 18-JUL-05 1WWT 0
JRNL AUTH E.CHIKAYAMA,T.KIGAWA,T.TOMIZAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE TGS DOMAIN FROM HUMAN
JRNL TITL 2 THREONYL-TRNA SYNTHETASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 1.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WWT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000024094.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.20MM TGS DOMAIN U-15N,13C;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 10%
REMARK 210 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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0,
REMARK 210 KUJIRA 0.9, CYANA 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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,TARGET
REMARK 210 FUNCTION
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
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 SER A 6 90.57 41.45
REMARK 500 1 ASP A 8 98.31 54.77
REMARK 500 1 SER A 9 172.02 -46.92
REMARK 500 1 LYS A 28 -56.94 -141.00
REMARK 500 1 SER A 39 122.91 -39.21
REMARK 500 1 ASN A 45 60.37 -103.25
REMARK 500 1 VAL A 47 -83.64 -139.95
REMARK 500 1 LEU A 62 177.20 -52.45
REMARK 500 1 GLU A 64 -177.65 -175.44
REMARK 500 1 PHE A 73 153.62 171.69
REMARK 500 1 GLU A 74 164.07 -47.42
REMARK 500 1 ASP A 75 90.16 -164.33
REMARK 500 1 GLU A 76 70.60 71.30
REMARK 500 1 GLN A 79 -57.76 75.95
REMARK 500 1 TYR A 82 167.86 -45.53
REMARK 500 1 SER A 87 83.27 64.63
REMARK 500 2 LYS A 28 -67.22 -138.23
REMARK 500 2 THR A 46 163.66 -47.26
REMARK 500 2 VAL A 47 -65.21 -122.48
REMARK 500 2 ASN A 52 32.26 80.01
REMARK 500 2 ASP A 59 49.09 -86.52
REMARK 500 2 LEU A 62 -178.66 -58.89
REMARK 500 2 PHE A 73 43.30 -169.68
REMARK 500 2 ASP A 75 84.09 -151.28
REMARK 500 2 GLN A 79 107.47 68.47
REMARK 500 2 ALA A 80 90.18 55.05
REMARK 500 2 VAL A 81 -41.33 -173.05
REMARK 500 2 SER A 83 -49.31 -158.82
REMARK 500 2 SER A 87 95.88 61.02
REMARK 500 3 SER A 3 109.54 63.49
REMARK 500 3 SER A 6 147.28 61.00
REMARK 500 3 LYS A 20 167.81 -48.88
REMARK 500 3 LYS A 28 -63.24 -139.66
REMARK 500 3 ILE A 38 -82.55 -43.84
REMARK 500 3 GLN A 40 107.77 -54.38
REMARK 500 3 ASN A 52 23.20 83.14
REMARK 500 3 ASN A 53 20.78 82.03
REMARK 500 3 LEU A 62 173.96 -52.95
REMARK 500 3 GLU A 64 -167.40 -171.43
REMARK 500 3 ASP A 65 109.47 -50.43
REMARK 500 3 ALA A 78 -72.57 -177.00
REMARK 500 3 GLN A 79 80.33 38.79
REMARK 500 3 ALA A 80 -99.24 57.16
REMARK 500 3 VAL A 81 -5.53 85.61
REMARK 500 3 TYR A 82 -176.80 49.16
REMARK 500 3 SER A 83 90.11 41.07
REMARK 500 3 SER A 86 98.34 -176.81
REMARK 500 4 SER A 2 121.88 60.85
REMARK 500 4 SER A 3 87.18 41.14
REMARK 500 4 SER A 5 94.28 -174.64
REMARK 500
REMARK 500 THIS ENTRY HAS 304 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001001576.1 RELATED DB: TARGETDB
DBREF 1WWT A 8 82 UNP P26639 SYTC_HUMAN 67 141
SEQADV 1WWT GLY A 1 UNP P26639 CLONING ARTIFACT
SEQADV 1WWT SER A 2 UNP P26639 CLONING ARTIFACT
SEQADV 1WWT SER A 3 UNP P26639 CLONING ARTIFACT
SEQADV 1WWT GLY A 4 UNP P26639 CLONING ARTIFACT
SEQADV 1WWT SER A 5 UNP P26639 CLONING ARTIFACT
SEQADV 1WWT SER A 6 UNP P26639 CLONING ARTIFACT
SEQADV 1WWT GLY A 7 UNP P26639 CLONING ARTIFACT
SEQADV 1WWT SER A 83 UNP P26639 CLONING ARTIFACT
SEQADV 1WWT GLY A 84 UNP P26639 CLONING ARTIFACT
SEQADV 1WWT PRO A 85 UNP P26639 CLONING ARTIFACT
SEQADV 1WWT SER A 86 UNP P26639 CLONING ARTIFACT
SEQADV 1WWT SER A 87 UNP P26639 CLONING ARTIFACT
SEQADV 1WWT GLY A 88 UNP P26639 CLONING ARTIFACT
SEQRES 1 A 88 GLY SER SER GLY SER SER GLY ASP SER LYS PRO ILE LYS
SEQRES 2 A 88 VAL THR LEU PRO ASP GLY LYS GLN VAL ASP ALA GLU SER
SEQRES 3 A 88 TRP LYS THR THR PRO TYR GLN ILE ALA CYS GLY ILE SER
SEQRES 4 A 88 GLN GLY LEU ALA ASP ASN THR VAL ILE ALA LYS VAL ASN
SEQRES 5 A 88 ASN VAL VAL TRP ASP LEU ASP ARG PRO LEU GLU GLU ASP
SEQRES 6 A 88 CYS THR LEU GLU LEU LEU LYS PHE GLU ASP GLU GLU ALA
SEQRES 7 A 88 GLN ALA VAL TYR SER GLY PRO SER SER GLY
HELIX 1 1 THR A 30 ILE A 38 1 9
HELIX 2 2 LEU A 42 THR A 46 5 5
SHEET 1 A 5 GLN A 21 GLU A 25 0
SHEET 2 A 5 PRO A 11 THR A 15 -1 N ILE A 12 O ALA A 24
SHEET 3 A 5 CYS A 66 LEU A 70 1 O LEU A 68 N THR A 15
SHEET 4 A 5 ALA A 49 VAL A 51 -1 N LYS A 50 O GLU A 69
SHEET 5 A 5 VAL A 55 TRP A 56 -1 O TRP A 56 N ALA A 49
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 2 2 Bytes