Header list of 2dgw.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 16-MAR-06 2DGW
TITLE SOLUTION STRUCTURE OF THE SECOND RNA RECOGNITION MOTIF IN RNA-BINDING
TITLE 2 PROTEIN 19
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE RNA-BINDING PROTEIN 19;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
COMPND 5 SYNONYM: RNA-BINDING MOTIF PROTEIN 19;
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: RBM19;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P051121-04;
SOURCE 9 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 C.ABE,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 2DGW 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DGW 1 VERSN
REVDAT 1 16-SEP-06 2DGW 0
JRNL AUTH C.ABE,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SECOND RNA RECOGNITION MOTIF IN
JRNL TITL 2 RNA-BINDING PROTEIN 19
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 2DGW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000025404.
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(PH7.0), 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 0.932, 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 THR A 291 125.06 -34.47
REMARK 500 1 HIS A 294 132.00 -38.85
REMARK 500 1 PRO A 302 -165.90 -69.75
REMARK 500 1 ALA A 315 166.56 -46.37
REMARK 500 1 PRO A 319 -179.07 -69.77
REMARK 500 1 ASN A 327 173.43 -47.20
REMARK 500 1 HIS A 329 38.14 -86.06
REMARK 500 1 TYR A 335 121.95 -170.07
REMARK 500 1 CYS A 352 72.23 -69.06
REMARK 500 1 SER A 372 -48.80 -130.15
REMARK 500 2 SER A 288 39.09 -95.45
REMARK 500 2 ASN A 304 35.75 -99.24
REMARK 500 2 PRO A 319 -177.61 -69.73
REMARK 500 2 VAL A 325 103.58 -59.39
REMARK 500 2 HIS A 329 50.23 35.09
REMARK 500 2 CYS A 352 83.19 -64.59
REMARK 500 2 PRO A 371 1.82 -69.82
REMARK 500 3 THR A 291 167.07 -46.60
REMARK 500 3 ALA A 315 166.25 -44.40
REMARK 500 3 LEU A 317 170.80 -50.03
REMARK 500 3 PRO A 319 -175.94 -69.79
REMARK 500 3 VAL A 325 100.53 -47.54
REMARK 500 3 ASN A 327 178.52 -52.42
REMARK 500 3 ASN A 331 120.32 -172.97
REMARK 500 3 LYS A 332 98.04 -54.38
REMARK 500 3 TYR A 335 148.32 -34.54
REMARK 500 3 GLU A 367 79.26 -112.54
REMARK 500 3 PRO A 371 -178.84 -69.78
REMARK 500 3 SER A 373 145.49 -36.12
REMARK 500 4 SER A 286 38.93 39.84
REMARK 500 4 PRO A 302 -176.40 -69.77
REMARK 500 4 ASN A 304 43.76 -92.81
REMARK 500 4 PRO A 319 -163.83 -69.78
REMARK 500 4 ALA A 328 -70.61 -41.07
REMARK 500 4 CYS A 352 72.68 -69.11
REMARK 500 4 GLU A 367 81.88 -64.02
REMARK 500 5 PRO A 302 -173.14 -69.71
REMARK 500 5 ASN A 304 44.44 -95.34
REMARK 500 5 ALA A 315 161.54 -45.54
REMARK 500 5 PRO A 319 -175.39 -69.77
REMARK 500 5 LYS A 332 105.54 -59.70
REMARK 500 6 SER A 285 43.28 34.96
REMARK 500 6 SER A 286 42.27 -88.35
REMARK 500 6 ASN A 304 47.78 -98.71
REMARK 500 6 PRO A 319 -171.94 -69.78
REMARK 500 6 VAL A 325 145.14 -35.38
REMARK 500 6 ARG A 326 108.70 -34.37
REMARK 500 6 LYS A 332 126.14 -38.17
REMARK 500 6 ARG A 354 35.82 73.18
REMARK 500 6 PRO A 371 86.23 -69.75
REMARK 500
REMARK 500 THIS ENTRY HAS 169 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002100665.2 RELATED DB: TARGETDB
DBREF 2DGW A 291 368 UNP Q9Y4C8 RBM19_HUMAN 291 368
SEQADV 2DGW GLY A 284 UNP Q9Y4C8 CLONING ARTIFACT
SEQADV 2DGW SER A 285 UNP Q9Y4C8 CLONING ARTIFACT
SEQADV 2DGW SER A 286 UNP Q9Y4C8 CLONING ARTIFACT
SEQADV 2DGW GLY A 287 UNP Q9Y4C8 CLONING ARTIFACT
SEQADV 2DGW SER A 288 UNP Q9Y4C8 CLONING ARTIFACT
SEQADV 2DGW SER A 289 UNP Q9Y4C8 CLONING ARTIFACT
SEQADV 2DGW GLY A 290 UNP Q9Y4C8 CLONING ARTIFACT
SEQADV 2DGW SER A 369 UNP Q9Y4C8 CLONING ARTIFACT
SEQADV 2DGW GLY A 370 UNP Q9Y4C8 CLONING ARTIFACT
SEQADV 2DGW PRO A 371 UNP Q9Y4C8 CLONING ARTIFACT
SEQADV 2DGW SER A 372 UNP Q9Y4C8 CLONING ARTIFACT
SEQADV 2DGW SER A 373 UNP Q9Y4C8 CLONING ARTIFACT
SEQADV 2DGW GLY A 374 UNP Q9Y4C8 CLONING ARTIFACT
SEQRES 1 A 91 GLY SER SER GLY SER SER GLY THR THR CYS HIS THR VAL
SEQRES 2 A 91 LYS LEU ARG GLY ALA PRO PHE ASN VAL THR GLU LYS ASN
SEQRES 3 A 91 VAL MET GLU PHE LEU ALA PRO LEU LYS PRO VAL ALA ILE
SEQRES 4 A 91 ARG ILE VAL ARG ASN ALA HIS GLY ASN LYS THR GLY TYR
SEQRES 5 A 91 ILE PHE VAL ASP PHE SER ASN GLU GLU GLU VAL LYS GLN
SEQRES 6 A 91 ALA LEU LYS CYS ASN ARG GLU TYR MET GLY GLY ARG TYR
SEQRES 7 A 91 ILE GLU VAL PHE ARG GLU LYS SER GLY PRO SER SER GLY
HELIX 1 1 THR A 306 ALA A 315 1 10
HELIX 2 2 ASN A 342 CYS A 352 1 11
SHEET 1 A 5 ALA A 321 ARG A 326 0
SHEET 2 A 5 LYS A 332 ASP A 339 -1 O PHE A 337 N ARG A 323
SHEET 3 A 5 THR A 295 ARG A 299 -1 N VAL A 296 O VAL A 338
SHEET 4 A 5 ARG A 360 GLU A 367 -1 O PHE A 365 N LYS A 297
SHEET 5 A 5 GLU A 355 MET A 357 -1 N GLU A 355 O ILE A 362
CISPEP 1 ALA A 315 PRO A 316 1 -0.04
CISPEP 2 ALA A 315 PRO A 316 2 0.00
CISPEP 3 ALA A 315 PRO A 316 3 0.03
CISPEP 4 ALA A 315 PRO A 316 4 -0.03
CISPEP 5 ALA A 315 PRO A 316 5 -0.04
CISPEP 6 ALA A 315 PRO A 316 6 -0.02
CISPEP 7 ALA A 315 PRO A 316 7 -0.01
CISPEP 8 ALA A 315 PRO A 316 8 -0.04
CISPEP 9 ALA A 315 PRO A 316 9 0.04
CISPEP 10 ALA A 315 PRO A 316 10 0.07
CISPEP 11 ALA A 315 PRO A 316 11 -0.03
CISPEP 12 ALA A 315 PRO A 316 12 0.07
CISPEP 13 ALA A 315 PRO A 316 13 0.05
CISPEP 14 ALA A 315 PRO A 316 14 0.03
CISPEP 15 ALA A 315 PRO A 316 15 -0.03
CISPEP 16 ALA A 315 PRO A 316 16 -0.03
CISPEP 17 ALA A 315 PRO A 316 17 -0.03
CISPEP 18 ALA A 315 PRO A 316 18 0.05
CISPEP 19 ALA A 315 PRO A 316 19 0.01
CISPEP 20 ALA A 315 PRO A 316 20 0.08
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