Header list of 1whq.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 28-MAY-04 1WHQ TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DSRBD FROM HYPOTHETICAL PROTEIN TITLE 2 BAB28848 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RNA HELICASE A; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: DOUBLE-STRANDED RNA BINDING DOMAIN; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: RIKEN CDNA 2810480H04; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021209-25; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS DOUBLE-STRANDED RNA BINDING DOMAIN, DSRBD, DSRM, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS, RNA KEYWDS 3 BINDING PROTEIN 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 1WHQ 1 REMARK SEQADV REVDAT 2 24-FEB-09 1WHQ 1 VERSN REVDAT 1 28-NOV-04 1WHQ 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 N-TERMINAL DSRBD FROM HYPOTHETICAL JRNL TITL 2 PROTEIN BAB28848 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 1WHQ 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_1000023591. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 100MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.16MM PROTEIN U-15N, 13C; 20MM REMARK 210 PHOSPHATE BUFFER NA; 100MM NACL; REMARK 210 1MM 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 SER A 51 136.87 -173.57 REMARK 500 1 ASN A 73 35.18 71.18 REMARK 500 1 SER A 90 94.32 -41.68 REMARK 500 2 ASN A 73 37.34 70.69 REMARK 500 3 SER A 51 149.00 -174.15 REMARK 500 3 ASN A 73 42.82 74.12 REMARK 500 3 VAL A 86 53.56 34.35 REMARK 500 3 SER A 90 145.34 -173.60 REMARK 500 4 PRO A 81 -178.12 -69.78 REMARK 500 4 PRO A 92 98.63 -69.78 REMARK 500 5 PRO A 89 83.62 -69.71 REMARK 500 6 VAL A 83 72.29 -65.96 REMARK 500 7 VAL A 86 138.78 -174.97 REMARK 500 8 SER A -1 106.75 -46.73 REMARK 500 8 SER A 90 157.32 -38.20 REMARK 500 9 SER A 51 129.01 -172.18 REMARK 500 9 SER A 90 43.86 -109.85 REMARK 500 9 PRO A 92 97.48 -69.78 REMARK 500 10 SER A -2 174.96 -54.34 REMARK 500 10 ALA A 57 -34.95 -39.85 REMARK 500 10 SER A 90 126.35 -35.66 REMARK 500 10 PRO A 92 90.51 -69.78 REMARK 500 11 GLU A 41 151.89 -43.14 REMARK 500 11 SER A 51 134.44 -172.94 REMARK 500 11 ASN A 73 44.89 71.37 REMARK 500 11 PRO A 81 -173.69 -69.70 REMARK 500 11 SER A 94 108.87 -59.45 REMARK 500 12 SER A -2 104.88 -36.96 REMARK 500 12 ASN A 73 40.98 71.81 REMARK 500 12 VAL A 86 136.89 -174.21 REMARK 500 12 SER A 93 105.82 -55.81 REMARK 500 14 SER A -2 95.22 -67.23 REMARK 500 14 SER A -1 173.96 -50.96 REMARK 500 14 ARG A 31 71.58 -111.72 REMARK 500 14 SER A 51 131.73 -174.83 REMARK 500 14 PRO A 92 2.01 -69.77 REMARK 500 14 SER A 93 93.92 -68.64 REMARK 500 14 SER A 94 124.24 -34.70 REMARK 500 15 SER A 51 145.11 -172.07 REMARK 500 15 ASN A 73 36.74 72.70 REMARK 500 16 SER A 90 177.97 -49.29 REMARK 500 16 PRO A 92 2.63 -69.76 REMARK 500 17 VAL A 86 138.69 -171.55 REMARK 500 18 SER A 2 141.90 -35.84 REMARK 500 18 GLU A 41 153.26 -48.37 REMARK 500 18 ASN A 73 39.62 72.13 REMARK 500 19 ARG A 31 76.98 -116.26 REMARK 500 19 ASN A 73 42.22 71.68 REMARK 500 20 PRO A 92 1.40 -69.77 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007009190.2 RELATED DB: TARGETDB DBREF 1WHQ A 4 89 UNP O70133 DHX9_MOUSE 4 89 SEQADV 1WHQ GLY A -3 UNP O70133 CLONING ARTIFACT SEQADV 1WHQ SER A -2 UNP O70133 CLONING ARTIFACT SEQADV 1WHQ SER A -1 UNP O70133 CLONING ARTIFACT SEQADV 1WHQ GLY A 0 UNP O70133 CLONING ARTIFACT SEQADV 1WHQ SER A 1 UNP O70133 CLONING ARTIFACT SEQADV 1WHQ SER A 2 UNP O70133 CLONING ARTIFACT SEQADV 1WHQ GLY A 3 UNP O70133 CLONING ARTIFACT SEQADV 1WHQ SER A 90 UNP O70133 CLONING ARTIFACT SEQADV 1WHQ GLY A 91 UNP O70133 CLONING ARTIFACT SEQADV 1WHQ PRO A 92 UNP O70133 CLONING ARTIFACT SEQADV 1WHQ SER A 93 UNP O70133 CLONING ARTIFACT SEQADV 1WHQ SER A 94 UNP O70133 CLONING ARTIFACT SEQADV 1WHQ GLY A 95 UNP O70133 CLONING ARTIFACT SEQRES 1 A 99 GLY SER SER GLY SER SER GLY ILE LYS ASN PHE LEU TYR SEQRES 2 A 99 ALA TRP CYS GLY LYS ARG LYS MET THR PRO ALA TYR GLU SEQRES 3 A 99 ILE ARG ALA VAL GLY ASN LYS ASN ARG GLN LYS PHE MET SEQRES 4 A 99 CYS GLU VAL ARG VAL GLU GLY PHE ASN TYR ALA GLY MET SEQRES 5 A 99 GLY ASN SER THR ASN LYS LYS ASP ALA GLN SER ASN ALA SEQRES 6 A 99 ALA ARG ASP PHE VAL ASN TYR LEU VAL ARG ILE ASN GLU SEQRES 7 A 99 VAL LYS SER GLU GLU VAL PRO ALA VAL GLY ILE VAL PRO SEQRES 8 A 99 PRO PRO SER GLY PRO SER SER GLY HELIX 1 1 LYS A 5 LYS A 14 1 10 HELIX 2 2 LYS A 54 ILE A 72 1 19 SHEET 1 A 3 ALA A 20 GLY A 27 0 SHEET 2 A 3 GLN A 32 ARG A 39 -1 O LYS A 33 N VAL A 26 SHEET 3 A 3 GLY A 47 SER A 51 -1 O GLY A 49 N CYS A 36 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