Header list of 2dgu.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 15-MAR-06 2DGU TITLE SOLUTION STRUCTURE OF THE RNA BINDING DOMAIN IN HETEROGENEOUS NUCLEAR TITLE 2 RIBONUCLEOPROTEIN Q COMPND MOL_ID: 1; COMPND 2 MOLECULE: HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN Q; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF; COMPND 5 SYNONYM: HNRNP Q, HNRNP-Q, SYNAPTOTAGMIN-BINDING, CYTOPLASMIC RNA- COMPND 6 INTERACTING PROTEIN, GLYCINE- AND TYROSINE-RICH RNA-BINDING PROTEIN, COMPND 7 GRY-RBP, NS1-ASSOCIATED PROTEIN 1; COMPND 8 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: SYNCRIP; SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P051017-06; 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 2DGU 1 REMARK SEQADV REVDAT 2 24-FEB-09 2DGU 1 VERSN REVDAT 1 15-SEP-06 2DGU 0 JRNL AUTH C.ABE,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE RNA BINDING DOMAIN IN JRNL TITL 2 HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN Q 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 2DGU 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_1000025402. 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, 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 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 SER A 328 42.48 -88.55 REMARK 500 1 LYS A 336 46.13 -106.71 REMARK 500 1 ASN A 344 36.40 70.66 REMARK 500 1 GLU A 355 -71.19 -74.21 REMARK 500 1 GLN A 360 -38.28 -37.67 REMARK 500 1 VAL A 385 -37.75 -37.99 REMARK 500 1 ASN A 392 107.72 -38.05 REMARK 500 1 PHE A 405 106.49 -51.67 REMARK 500 1 PRO A 409 90.84 -69.78 REMARK 500 1 GLU A 415 136.95 -170.31 REMARK 500 1 ARG A 416 110.74 -164.46 REMARK 500 2 LYS A 336 36.08 -86.32 REMARK 500 2 ASN A 344 39.61 70.73 REMARK 500 2 GLN A 360 -38.70 -38.84 REMARK 500 2 VAL A 385 -35.35 -36.00 REMARK 500 2 ASN A 392 116.61 -34.12 REMARK 500 3 ASN A 344 54.35 72.22 REMARK 500 3 GLN A 360 -39.18 -35.20 REMARK 500 3 VAL A 385 -38.63 -38.39 REMARK 500 3 ASN A 392 101.73 -34.29 REMARK 500 3 PRO A 409 -175.52 -69.79 REMARK 500 3 LYS A 412 77.92 -63.58 REMARK 500 3 PRO A 426 89.63 -69.75 REMARK 500 3 SER A 428 148.01 -171.11 REMARK 500 4 LYS A 336 42.74 -100.29 REMARK 500 4 ASN A 344 52.38 73.23 REMARK 500 4 ALA A 346 -176.61 -54.58 REMARK 500 4 GLU A 355 -73.48 -68.21 REMARK 500 4 GLN A 360 -38.68 -38.68 REMARK 500 4 VAL A 385 -36.87 -34.92 REMARK 500 4 ASN A 392 92.91 -35.09 REMARK 500 4 ASN A 400 95.88 -69.38 REMARK 500 4 PHE A 405 108.70 -54.71 REMARK 500 4 SER A 427 -60.88 -124.79 REMARK 500 5 LYS A 336 42.11 -107.94 REMARK 500 5 ASN A 344 43.85 73.46 REMARK 500 5 ALA A 346 178.84 -49.40 REMARK 500 5 GLN A 360 -35.37 -34.28 REMARK 500 5 LYS A 371 -72.04 -32.12 REMARK 500 5 VAL A 385 -32.83 -35.39 REMARK 500 5 ARG A 413 119.30 -173.88 REMARK 500 5 LYS A 414 148.74 -174.61 REMARK 500 5 GLN A 421 114.25 -165.65 REMARK 500 5 PRO A 426 -174.17 -69.78 REMARK 500 6 SER A 329 118.14 -168.71 REMARK 500 6 ASN A 344 39.19 70.24 REMARK 500 6 ALA A 346 172.29 -50.26 REMARK 500 6 VAL A 385 -39.87 -38.47 REMARK 500 6 ASN A 392 97.58 -36.68 REMARK 500 6 LYS A 414 143.78 -170.18 REMARK 500 REMARK 500 THIS ENTRY HAS 164 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK003000744.1 RELATED DB: TARGETDB DBREF 2DGU A 334 423 UNP O60506 HNRPQ_HUMAN 334 423 SEQADV 2DGU GLY A 327 UNP O60506 CLONING ARTIFACT SEQADV 2DGU SER A 328 UNP O60506 CLONING ARTIFACT SEQADV 2DGU SER A 329 UNP O60506 CLONING ARTIFACT SEQADV 2DGU GLY A 330 UNP O60506 CLONING ARTIFACT SEQADV 2DGU SER A 331 UNP O60506 CLONING ARTIFACT SEQADV 2DGU SER A 332 UNP O60506 CLONING ARTIFACT SEQADV 2DGU GLY A 333 UNP O60506 CLONING ARTIFACT SEQADV 2DGU SER A 424 UNP O60506 CLONING ARTIFACT SEQADV 2DGU GLY A 425 UNP O60506 CLONING ARTIFACT SEQADV 2DGU PRO A 426 UNP O60506 CLONING ARTIFACT SEQADV 2DGU SER A 427 UNP O60506 CLONING ARTIFACT SEQADV 2DGU SER A 428 UNP O60506 CLONING ARTIFACT SEQADV 2DGU GLY A 429 UNP O60506 CLONING ARTIFACT SEQRES 1 A 103 GLY SER SER GLY SER SER GLY MET ALA LYS VAL LYS VAL SEQRES 2 A 103 LEU PHE VAL ARG ASN LEU ALA ASN THR VAL THR GLU GLU SEQRES 3 A 103 ILE LEU GLU LYS ALA PHE SER GLN PHE GLY LYS LEU GLU SEQRES 4 A 103 ARG VAL LYS LYS LEU LYS ASP TYR ALA PHE ILE HIS PHE SEQRES 5 A 103 ASP GLU ARG ASP GLY ALA VAL LYS ALA MET GLU GLU MET SEQRES 6 A 103 ASN GLY LYS ASP LEU GLU GLY GLU ASN ILE GLU ILE VAL SEQRES 7 A 103 PHE ALA LYS PRO PRO ASP GLN LYS ARG LYS GLU ARG LYS SEQRES 8 A 103 ALA GLN ARG GLN ALA ALA SER GLY PRO SER SER GLY HELIX 1 1 THR A 350 GLY A 362 1 13 HELIX 2 2 GLU A 380 ASN A 392 1 13 SHEET 1 A 5 LEU A 364 LYS A 369 0 SHEET 2 A 5 ALA A 374 PHE A 378 -1 O HIS A 377 N GLU A 365 SHEET 3 A 5 LEU A 340 ARG A 343 -1 N VAL A 342 O ALA A 374 SHEET 4 A 5 GLU A 399 PHE A 405 -1 O VAL A 404 N PHE A 341 SHEET 5 A 5 LYS A 394 LEU A 396 -1 N LEU A 396 O GLU A 399 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