Header list of 2d9o.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 12-DEC-05 2D9O
TITLE SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN HYPOTHETICAL PROTEIN
TITLE 2 FLJ10634
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNAJ (HSP40) HOMOLOG, SUBFAMILY C, MEMBER 17;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF, RESIDUES 168-254;
COMPND 5 SYNONYM: HYPOTHETICAL PROTEIN FLJ 10634;
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 GENE: FLJ10634;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050314-08;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RRM DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2D9O 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2D9O 1 VERSN
REVDAT 1 12-JUN-06 2D9O 0
JRNL AUTH K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN HYPOTHETICAL
JRNL TITL 2 PROTEIN FLJ10634
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D9O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025159.
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 : 20MM D-TRIS-HCL(PH 7.0), 100MM
REMARK 210 NACL, 1MM D-DTT, 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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9321, CYANA 2.0
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 : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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: 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 PRO A 171 84.08 -69.81
REMARK 500 1 GLU A 182 93.46 -35.09
REMARK 500 1 GLN A 232 -60.70 -106.88
REMARK 500 1 ASN A 233 -74.63 -67.03
REMARK 500 1 PRO A 241 93.36 -69.76
REMARK 500 1 LEU A 242 152.05 -37.71
REMARK 500 1 SER A 255 41.59 -106.12
REMARK 500 2 PRO A 171 85.63 -69.84
REMARK 500 2 VAL A 204 104.77 -57.74
REMARK 500 2 GLN A 232 -71.69 -104.99
REMARK 500 2 ASN A 233 -73.42 -50.77
REMARK 500 2 PRO A 241 93.11 -69.76
REMARK 500 2 LEU A 242 153.72 -38.10
REMARK 500 3 SER A 162 127.54 -36.33
REMARK 500 3 PRO A 171 80.03 -69.74
REMARK 500 3 LYS A 181 173.29 -52.01
REMARK 500 3 GLU A 182 88.64 -60.26
REMARK 500 3 GLU A 203 83.78 -68.02
REMARK 500 3 GLN A 232 -66.27 -97.62
REMARK 500 3 PRO A 241 93.18 -69.77
REMARK 500 4 PRO A 171 81.05 -69.78
REMARK 500 4 LYS A 178 152.68 -49.96
REMARK 500 4 GLU A 182 48.23 36.70
REMARK 500 4 ASP A 183 -61.33 -95.13
REMARK 500 4 LYS A 225 -71.62 -36.74
REMARK 500 4 GLN A 232 -75.13 -91.69
REMARK 500 4 ASN A 233 -70.99 -47.35
REMARK 500 4 PRO A 241 95.69 -69.79
REMARK 500 4 LEU A 242 147.77 -34.20
REMARK 500 5 PRO A 171 79.93 -69.78
REMARK 500 5 LYS A 178 98.62 -64.82
REMARK 500 5 GLU A 203 99.86 -65.73
REMARK 500 5 SER A 210 174.54 -47.92
REMARK 500 5 LYS A 212 -60.37 -126.85
REMARK 500 5 GLN A 232 -72.87 -91.81
REMARK 500 5 ASN A 233 -74.95 -54.87
REMARK 500 5 GLU A 234 109.88 -43.97
REMARK 500 5 PRO A 241 95.02 -69.81
REMARK 500 5 LEU A 242 158.22 -38.54
REMARK 500 5 SER A 258 -73.98 -36.81
REMARK 500 6 GLN A 168 154.41 -45.58
REMARK 500 6 PRO A 171 81.48 -69.76
REMARK 500 6 GLN A 232 -69.32 -90.05
REMARK 500 6 ASN A 233 -74.52 -54.27
REMARK 500 6 PRO A 241 94.90 -69.73
REMARK 500 6 LEU A 242 148.25 -34.18
REMARK 500 7 SER A 162 42.99 37.12
REMARK 500 7 PRO A 171 80.26 -69.78
REMARK 500 7 CYS A 179 148.81 -174.85
REMARK 500 7 GLU A 182 44.37 -80.44
REMARK 500
REMARK 500 THIS ENTRY HAS 193 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSG002001022.1 RELATED DB: TARGETDB
DBREF 2D9O A 168 254 GB 8922563 NP_060633 168 254
SEQADV 2D9O GLY A 161 GB 8922563 CLONING ARTIFACT
SEQADV 2D9O SER A 162 GB 8922563 CLONING ARTIFACT
SEQADV 2D9O SER A 163 GB 8922563 CLONING ARTIFACT
SEQADV 2D9O GLY A 164 GB 8922563 CLONING ARTIFACT
SEQADV 2D9O SER A 165 GB 8922563 CLONING ARTIFACT
SEQADV 2D9O SER A 166 GB 8922563 CLONING ARTIFACT
SEQADV 2D9O GLY A 167 GB 8922563 CLONING ARTIFACT
SEQADV 2D9O SER A 255 GB 8922563 CLONING ARTIFACT
SEQADV 2D9O GLY A 256 GB 8922563 CLONING ARTIFACT
SEQADV 2D9O PRO A 257 GB 8922563 CLONING ARTIFACT
SEQADV 2D9O SER A 258 GB 8922563 CLONING ARTIFACT
SEQADV 2D9O SER A 259 GB 8922563 CLONING ARTIFACT
SEQADV 2D9O GLY A 260 GB 8922563 CLONING ARTIFACT
SEQRES 1 A 100 GLY SER SER GLY SER SER GLY GLN GLY THR PRO LYS LEU
SEQRES 2 A 100 LYS LEU LYS TRP LYS CYS LYS LYS GLU ASP GLU SER LYS
SEQRES 3 A 100 GLY GLY TYR SER LYS ASP VAL LEU LEU ARG LEU LEU GLN
SEQRES 4 A 100 LYS TYR GLY GLU VAL LEU ASN LEU VAL LEU SER SER LYS
SEQRES 5 A 100 LYS PRO GLY THR ALA VAL VAL GLU PHE ALA THR VAL LYS
SEQRES 6 A 100 ALA ALA GLU LEU ALA VAL GLN ASN GLU VAL GLY LEU VAL
SEQRES 7 A 100 ASP ASN PRO LEU LYS ILE SER TRP LEU GLU GLY GLN PRO
SEQRES 8 A 100 GLN ASP ALA SER GLY PRO SER SER GLY
HELIX 1 1 SER A 190 LYS A 200 1 11
HELIX 2 2 THR A 223 ASN A 233 1 11
SHEET 1 A 4 VAL A 204 SER A 210 0
SHEET 2 A 4 THR A 216 PHE A 221 -1 O GLU A 220 N ASN A 206
SHEET 3 A 4 LYS A 172 LYS A 176 -1 N LEU A 173 O VAL A 219
SHEET 4 A 4 LYS A 243 SER A 245 -1 O SER A 245 N LYS A 174
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