Header list of 1why.pdb file
Complete list - r 2 2 Bytes
HEADER RNA BINDING PROTEIN 28-MAY-04 1WHY
TITLE SOLUTION STRUCTURE OF THE RNA RECOGNITION MOTIF FROM HYPOTHETICAL RNA
TITLE 2 BINDING PROTEIN BC052180
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN RIKEN CDNA 1810017N16;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
COMPND 5 SYNONYM: HYPOTHETICAL PROTEIN BC052180;
COMPND 6 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 1810017N16;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030916-18;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RNA RECOGNITION MOTIF, RRM, RNA BINDING DOMAIN, RBD, RNP, STRUCTURAL
KEYWDS 2 GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, 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 1WHY 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WHY 1 VERSN
REVDAT 1 28-NOV-04 1WHY 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 RNA RECOGNITION MOTIF FROM
JRNL TITL 2 HYPOTHETICAL RNA BINDING PROTEIN BC052180
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 1WHY 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_1000023597.
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 : 1.13MM 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 75 145.53 -35.80
REMARK 500 1 SER A 76 41.28 -98.27
REMARK 500 1 ILE A 82 151.86 -45.35
REMARK 500 1 ALA A 108 -34.61 -35.15
REMARK 500 1 ARG A 113 -28.62 -39.79
REMARK 500 1 SER A 116 103.56 -50.63
REMARK 500 1 SER A 127 39.23 71.06
REMARK 500 1 ARG A 147 99.06 -34.66
REMARK 500 1 PRO A 150 95.18 -69.79
REMARK 500 2 ARG A 113 -35.33 -38.27
REMARK 500 2 ARG A 147 98.89 -42.45
REMARK 500 2 PRO A 150 97.68 -69.77
REMARK 500 3 THR A 102 104.31 -48.88
REMARK 500 3 PRO A 150 5.29 -69.76
REMARK 500 3 LEU A 151 95.85 -34.21
REMARK 500 3 PHE A 162 154.49 -39.31
REMARK 500 4 TYR A 84 147.72 -171.20
REMARK 500 4 ARG A 147 102.63 -40.72
REMARK 500 4 PRO A 150 5.29 -69.74
REMARK 500 4 LEU A 151 149.40 -34.17
REMARK 500 4 PRO A 167 98.71 -69.74
REMARK 500 5 THR A 102 108.77 -55.76
REMARK 500 5 ALA A 106 -70.06 -52.41
REMARK 500 5 VAL A 123 126.08 -170.99
REMARK 500 5 SER A 127 31.42 70.27
REMARK 500 5 ARG A 147 118.48 -37.50
REMARK 500 5 PRO A 150 5.20 -69.80
REMARK 500 5 LEU A 151 149.57 -34.65
REMARK 500 5 SER A 168 104.14 -57.27
REMARK 500 6 ALA A 108 -26.44 -39.05
REMARK 500 6 ARG A 147 95.82 -35.74
REMARK 500 6 PRO A 150 5.47 -69.76
REMARK 500 6 LEU A 151 136.12 -33.93
REMARK 500 6 SER A 169 131.10 -174.71
REMARK 500 7 SER A 76 41.55 38.93
REMARK 500 7 ARG A 147 95.84 -35.62
REMARK 500 7 PRO A 150 5.47 -69.77
REMARK 500 7 LEU A 151 100.71 -36.93
REMARK 500 8 SER A 79 42.51 34.64
REMARK 500 8 LYS A 81 43.36 -96.92
REMARK 500 8 PRO A 150 5.65 -69.77
REMARK 500 8 LEU A 151 153.94 -36.05
REMARK 500 8 LYS A 164 138.63 -173.91
REMARK 500 8 PRO A 167 94.07 -69.71
REMARK 500 8 SER A 169 107.62 -55.68
REMARK 500 9 ILE A 82 145.79 -38.03
REMARK 500 9 ARG A 147 113.42 -34.93
REMARK 500 9 PRO A 150 5.83 -69.73
REMARK 500 9 LEU A 151 149.61 -33.76
REMARK 500 10 LYS A 124 -62.77 -90.39
REMARK 500
REMARK 500 THIS ENTRY HAS 123 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT007120361.1 RELATED DB: TARGETDB
DBREF 1WHY A 81 164 GB 40254294 NP_780611 81 164
SEQADV 1WHY GLY A 74 GB 40254294 CLONING ARTIFACT
SEQADV 1WHY SER A 75 GB 40254294 CLONING ARTIFACT
SEQADV 1WHY SER A 76 GB 40254294 CLONING ARTIFACT
SEQADV 1WHY GLY A 77 GB 40254294 CLONING ARTIFACT
SEQADV 1WHY SER A 78 GB 40254294 CLONING ARTIFACT
SEQADV 1WHY SER A 79 GB 40254294 CLONING ARTIFACT
SEQADV 1WHY GLY A 80 GB 40254294 CLONING ARTIFACT
SEQADV 1WHY SER A 165 GB 40254294 CLONING ARTIFACT
SEQADV 1WHY GLY A 166 GB 40254294 CLONING ARTIFACT
SEQADV 1WHY PRO A 167 GB 40254294 CLONING ARTIFACT
SEQADV 1WHY SER A 168 GB 40254294 CLONING ARTIFACT
SEQADV 1WHY SER A 169 GB 40254294 CLONING ARTIFACT
SEQADV 1WHY GLY A 170 GB 40254294 CLONING ARTIFACT
SEQRES 1 A 97 GLY SER SER GLY SER SER GLY LYS ILE GLY TYR GLY LYS
SEQRES 2 A 97 ALA ASN PRO THR THR ARG LEU TRP VAL GLY GLY LEU GLY
SEQRES 3 A 97 PRO ASN THR SER LEU ALA ALA LEU ALA ARG GLU PHE ASP
SEQRES 4 A 97 ARG PHE GLY SER ILE ARG THR ILE ASP HIS VAL LYS GLY
SEQRES 5 A 97 ASP SER PHE ALA TYR ILE GLN TYR GLU SER LEU ASP ALA
SEQRES 6 A 97 ALA GLN ALA ALA CYS ALA LYS MET ARG GLY PHE PRO LEU
SEQRES 7 A 97 GLY GLY PRO ASP ARG ARG LEU ARG VAL ASP PHE ALA LYS
SEQRES 8 A 97 SER GLY PRO SER SER GLY
HELIX 1 1 LEU A 104 ASP A 112 1 9
HELIX 2 2 LEU A 136 MET A 146 1 11
SHEET 1 A 4 ILE A 117 HIS A 122 0
SHEET 2 A 4 ALA A 129 TYR A 133 -1 O GLN A 132 N ARG A 118
SHEET 3 A 4 LEU A 93 GLY A 96 -1 N VAL A 95 O ALA A 129
SHEET 4 A 4 ARG A 159 PHE A 162 -1 O ASP A 161 N TRP A 94
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