Header list of 1whr.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 28-MAY-04 1WHR
TITLE SOLUTION STRUCTURE OF THE R3H DOMAIN FROM HUMAN HYPOTHETICAL PROTEIN
TITLE 2 BAA76846
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL KIAA1002 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: R3H DOMAIN;
COMPND 5 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: RIKEN CDNA HK09859;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040119-75;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS R3H DOMAIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 2 INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.NAGATA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WHR 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WHR 1 VERSN
REVDAT 1 28-NOV-04 1WHR 0
JRNL AUTH T.NAGATA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE R3H DOMAIN FROM HUMAN HYPOTHETICAL
JRNL TITL 2 PROTEIN BAA76846
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRVIEW 5.0.4, CYANA 2.0
REMARK 3 AUTHORS : JOHNSON (NMRVIEW), GUENTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WHR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000023592.
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
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : U-15N, 13C LABELLED PROTEIN;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM
REMARK 210 D-DTT; 0.02% NAN3; 90% H2O; 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
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 : CYANA 2.0, NMRPIPE 2.3, KUJIRA
REMARK 210 0.901
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 SIMULATED ANNEALING
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 ASP A 171 108.55 -59.09
REMARK 500 1 HIS A 191 -39.03 -37.31
REMARK 500 1 PRO A 221 -168.31 -69.76
REMARK 500 1 PHE A 241 41.66 36.12
REMARK 500 2 SER A 130 122.93 -173.24
REMARK 500 2 THR A 133 148.18 -170.47
REMARK 500 2 LYS A 149 -71.43 -91.07
REMARK 500 2 PRO A 180 -168.92 -69.74
REMARK 500 2 GLU A 232 89.51 -57.67
REMARK 500 2 LYS A 233 107.24 -162.68
REMARK 500 2 ARG A 240 144.13 -174.96
REMARK 500 2 PHE A 241 131.02 -172.63
REMARK 500 3 THR A 133 40.15 37.28
REMARK 500 3 GLN A 181 148.08 -39.99
REMARK 500 3 SER A 226 -36.88 -36.62
REMARK 500 3 PRO A 246 86.66 -69.73
REMARK 500 4 ASP A 139 32.29 39.92
REMARK 500 4 MET A 157 -73.46 -47.64
REMARK 500 4 GLN A 181 128.36 -39.63
REMARK 500 4 PRO A 221 -167.80 -69.74
REMARK 500 5 SER A 127 145.43 -171.63
REMARK 500 5 GLN A 181 127.27 -39.19
REMARK 500 5 HIS A 191 -37.68 -38.44
REMARK 500 5 ILE A 229 30.01 -97.38
REMARK 500 5 GLU A 232 48.32 -89.16
REMARK 500 6 ILE A 138 171.12 -57.20
REMARK 500 6 ASP A 171 102.18 -56.33
REMARK 500 6 HIS A 191 -39.08 -39.96
REMARK 500 6 ASN A 234 123.02 -174.84
REMARK 500 6 PHE A 237 127.28 -173.37
REMARK 500 6 ILE A 242 140.86 -173.56
REMARK 500 6 PRO A 246 -167.52 -69.80
REMARK 500 7 ASP A 139 41.45 36.81
REMARK 500 7 GLN A 181 126.83 -34.83
REMARK 500 7 PRO A 221 -179.00 -69.73
REMARK 500 8 ILE A 138 156.66 -47.30
REMARK 500 8 HIS A 141 -70.35 -39.40
REMARK 500 8 ASN A 217 -18.63 -49.67
REMARK 500 8 GLU A 236 143.31 -174.11
REMARK 500 8 PHE A 237 108.76 -166.82
REMARK 500 9 SER A 131 144.97 -174.75
REMARK 500 9 ILE A 138 112.66 -36.04
REMARK 500 9 ASP A 139 88.40 -61.63
REMARK 500 9 LYS A 149 -71.85 -90.71
REMARK 500 9 ARG A 155 -29.08 -37.01
REMARK 500 9 SER A 184 -73.75 -43.04
REMARK 500 9 HIS A 191 -39.46 -36.84
REMARK 500 9 SER A 244 150.86 -40.96
REMARK 500 9 PRO A 246 -169.56 -69.80
REMARK 500 10 ASP A 139 39.52 34.53
REMARK 500
REMARK 500 THIS ENTRY HAS 132 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000978.1 RELATED DB: TARGETDB
DBREF 1WHR A 133 243 UNP Q9Y2K5 K1002_HUMAN 133 243
SEQADV 1WHR GLY A 126 UNP Q9Y2K5 CLONING ARTIFACT
SEQADV 1WHR SER A 127 UNP Q9Y2K5 CLONING ARTIFACT
SEQADV 1WHR SER A 128 UNP Q9Y2K5 CLONING ARTIFACT
SEQADV 1WHR GLY A 129 UNP Q9Y2K5 CLONING ARTIFACT
SEQADV 1WHR SER A 130 UNP Q9Y2K5 CLONING ARTIFACT
SEQADV 1WHR SER A 131 UNP Q9Y2K5 CLONING ARTIFACT
SEQADV 1WHR GLY A 132 UNP Q9Y2K5 CLONING ARTIFACT
SEQADV 1WHR SER A 244 UNP Q9Y2K5 CLONING ARTIFACT
SEQADV 1WHR GLY A 245 UNP Q9Y2K5 CLONING ARTIFACT
SEQADV 1WHR PRO A 246 UNP Q9Y2K5 CLONING ARTIFACT
SEQADV 1WHR SER A 247 UNP Q9Y2K5 CLONING ARTIFACT
SEQADV 1WHR SER A 248 UNP Q9Y2K5 CLONING ARTIFACT
SEQADV 1WHR GLY A 249 UNP Q9Y2K5 CLONING ARTIFACT
SEQRES 1 A 124 GLY SER SER GLY SER SER GLY THR ASP SER THR GLY ILE
SEQRES 2 A 124 ASP LEU HIS GLU PHE LEU VAL ASN THR LEU LYS LYS ASN
SEQRES 3 A 124 PRO ARG ASP ARG MET MET LEU LEU LYS LEU GLU GLN GLU
SEQRES 4 A 124 ILE LEU GLU PHE ILE ASN ASP ASN ASN ASN GLN PHE LYS
SEQRES 5 A 124 LYS PHE PRO GLN MET THR SER TYR HIS ARG MET LEU LEU
SEQRES 6 A 124 HIS ARG VAL ALA ALA TYR PHE GLY MET ASP HIS ASN VAL
SEQRES 7 A 124 ASP GLN THR GLY LYS ALA VAL ILE ILE ASN LYS THR SER
SEQRES 8 A 124 ASN THR ARG ILE PRO GLU GLN ARG PHE SER GLU HIS ILE
SEQRES 9 A 124 LYS ASP GLU LYS ASN THR GLU PHE GLN GLN ARG PHE ILE
SEQRES 10 A 124 LEU SER GLY PRO SER SER GLY
HELIX 1 1 LEU A 140 LYS A 150 1 11
HELIX 2 2 ARG A 155 ASN A 170 1 16
HELIX 3 3 SER A 184 PHE A 197 1 14
HELIX 4 4 PHE A 225 GLU A 227 5 3
SHEET 1 A 3 PHE A 176 LYS A 178 0
SHEET 2 A 3 VAL A 210 ASN A 213 -1 O ILE A 212 N LYS A 177
SHEET 3 A 3 HIS A 201 VAL A 203 -1 N ASN A 202 O ILE A 211
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