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Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 16-MAR-06 2DGV TITLE SOLUTION STRUCTURE OF THE RNA BINDING DOMAIN IN HETEROGENEOUS NUCLEAR TITLE 2 RIBONUCLEOPROTEIN M COMPND MOL_ID: 1; COMPND 2 MOLECULE: HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN M; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF; COMPND 5 SYNONYM: HNRNP M; 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: HNRP M; SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P051121-03; 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 2DGV 1 REMARK SEQADV REVDAT 2 24-FEB-09 2DGV 1 VERSN REVDAT 1 16-SEP-06 2DGV 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 M 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 2DGV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAR-06. REMARK 100 THE DEPOSITION ID IS D_1000025403. 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 LYS A 669 -74.15 -65.20 REMARK 500 1 LEU A 679 -61.53 -107.30 REMARK 500 1 ASN A 712 109.72 -54.22 REMARK 500 1 LYS A 715 101.15 -51.94 REMARK 500 1 ASN A 728 71.36 -114.36 REMARK 500 2 ASN A 658 50.17 71.17 REMARK 500 2 PHE A 663 128.40 -38.85 REMARK 500 2 LYS A 669 -74.20 -60.66 REMARK 500 2 LEU A 679 -61.85 -107.47 REMARK 500 2 ASN A 687 48.68 70.98 REMARK 500 2 SER A 690 128.30 -37.69 REMARK 500 2 ASN A 712 112.27 -39.79 REMARK 500 2 LYS A 715 99.13 -54.07 REMARK 500 2 ALA A 729 -49.65 -131.38 REMARK 500 2 PRO A 732 93.83 -69.77 REMARK 500 3 SER A 648 158.08 -42.38 REMARK 500 3 PHE A 663 140.03 -37.60 REMARK 500 3 LYS A 669 -73.69 -64.76 REMARK 500 3 LEU A 679 -64.42 -100.50 REMARK 500 3 ALA A 707 -34.95 -39.61 REMARK 500 3 MET A 714 97.15 -61.34 REMARK 500 3 LYS A 715 101.50 -54.08 REMARK 500 3 SER A 717 41.34 37.64 REMARK 500 3 SER A 733 110.72 -35.38 REMARK 500 4 PHE A 663 124.92 -35.74 REMARK 500 4 LYS A 669 -74.92 -65.47 REMARK 500 4 SER A 717 38.73 36.66 REMARK 500 5 PHE A 663 116.59 -36.84 REMARK 500 5 LYS A 669 -73.12 -65.49 REMARK 500 5 SER A 690 137.56 -35.26 REMARK 500 5 MET A 714 94.07 -69.28 REMARK 500 5 LYS A 715 98.92 -51.13 REMARK 500 5 SER A 717 38.93 36.51 REMARK 500 5 SER A 730 -67.90 -122.16 REMARK 500 5 PRO A 732 0.28 -69.72 REMARK 500 5 SER A 733 98.95 -34.59 REMARK 500 6 SER A 646 98.75 -52.31 REMARK 500 6 PHE A 663 124.96 -39.13 REMARK 500 6 SER A 690 154.16 -41.09 REMARK 500 6 MET A 714 104.31 -59.64 REMARK 500 6 SER A 717 39.70 36.70 REMARK 500 6 ASN A 728 56.74 -96.18 REMARK 500 6 PRO A 732 -173.05 -69.74 REMARK 500 6 SER A 734 114.66 -169.83 REMARK 500 7 ALA A 651 74.78 -69.60 REMARK 500 7 CYS A 652 47.20 -97.14 REMARK 500 7 ASN A 658 52.12 70.66 REMARK 500 7 LYS A 669 -71.45 -62.49 REMARK 500 7 SER A 717 38.62 36.93 REMARK 500 7 ARG A 727 40.79 -81.65 REMARK 500 REMARK 500 THIS ENTRY HAS 137 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSK003002075.3 RELATED DB: TARGETDB DBREF 2DGV A 651 729 UNP P52272 HNRPM_HUMAN 651 729 SEQADV 2DGV GLY A 644 UNP P52272 CLONING ARTIFACT SEQADV 2DGV SER A 645 UNP P52272 CLONING ARTIFACT SEQADV 2DGV SER A 646 UNP P52272 CLONING ARTIFACT SEQADV 2DGV GLY A 647 UNP P52272 CLONING ARTIFACT SEQADV 2DGV SER A 648 UNP P52272 CLONING ARTIFACT SEQADV 2DGV SER A 649 UNP P52272 CLONING ARTIFACT SEQADV 2DGV GLY A 650 UNP P52272 CLONING ARTIFACT SEQADV 2DGV SER A 730 UNP P52272 CLONING ARTIFACT SEQADV 2DGV GLY A 731 UNP P52272 CLONING ARTIFACT SEQADV 2DGV PRO A 732 UNP P52272 CLONING ARTIFACT SEQADV 2DGV SER A 733 UNP P52272 CLONING ARTIFACT SEQADV 2DGV SER A 734 UNP P52272 CLONING ARTIFACT SEQADV 2DGV GLY A 735 UNP P52272 CLONING ARTIFACT SEQRES 1 A 92 GLY SER SER GLY SER SER GLY ALA CYS GLN ILE PHE VAL SEQRES 2 A 92 ARG ASN LEU PRO PHE ASP PHE THR TRP LYS MET LEU LYS SEQRES 3 A 92 ASP LYS PHE ASN GLU CYS GLY HIS VAL LEU TYR ALA ASP SEQRES 4 A 92 ILE LYS MET GLU ASN GLY LYS SER LYS GLY CYS GLY VAL SEQRES 5 A 92 VAL LYS PHE GLU SER PRO GLU VAL ALA GLU ARG ALA CYS SEQRES 6 A 92 ARG MET MET ASN GLY MET LYS LEU SER GLY ARG GLU ILE SEQRES 7 A 92 ASP VAL ARG ILE ASP ARG ASN ALA SER GLY PRO SER SER SEQRES 8 A 92 GLY HELIX 1 1 THR A 664 GLU A 674 1 11 HELIX 2 2 SER A 700 ASN A 712 1 13 SHEET 1 A 4 VAL A 678 MET A 685 0 SHEET 2 A 4 SER A 690 PHE A 698 -1 O LYS A 697 N LEU A 679 SHEET 3 A 4 GLN A 653 VAL A 656 -1 N VAL A 656 O GLY A 694 SHEET 4 A 4 ARG A 724 ILE A 725 -1 O ARG A 724 N PHE A 655 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