Header list of 2dgs.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 15-MAR-06 2DGS
TITLE SOLUTION STRUCTURE OF THE SECOND RNA BINDING DOMAIN IN DAZ-ASSOCIATED
TITLE 2 PROTEIN 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DAZ-ASSOCIATED PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
COMPND 5 SYNONYM: DELETED IN AZOOSPERMIA-ASSOCIATED PROTEIN 1;
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: DAZAP1;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P051017-03;
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 2DGS 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DGS 1 VERSN
REVDAT 1 15-SEP-06 2DGS 0
JRNL AUTH C.ABE,Y.MUTO,M.INOUE,T.TERADA,T.KIGAWA,M.SHIROUZU,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE SECOND RNA BINDING DOMAIN IN
JRNL TITL 2 DAZ-ASSOCIATED PROTEIN 1
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 2DGS 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_1000025400.
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
REMARK 210 DYNAMICS,RESTRAINTED MOLECULAR
REMARK 210 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 ASN A 113 38.74 -88.21
REMARK 500 1 GLU A 164 -37.70 -36.30
REMARK 500 1 HIS A 174 28.17 48.17
REMARK 500 1 SER A 199 -175.78 -172.05
REMARK 500 2 SER A 108 43.07 -105.45
REMARK 500 2 ASN A 113 34.60 -92.33
REMARK 500 2 ASN A 123 -62.02 -100.23
REMARK 500 2 CYS A 124 120.96 -37.62
REMARK 500 3 SER A 107 100.84 -57.37
REMARK 500 3 SER A 110 40.28 -92.99
REMARK 500 3 LYS A 111 108.99 -53.13
REMARK 500 3 ASN A 113 41.94 -82.63
REMARK 500 3 VAL A 138 109.99 -161.42
REMARK 500 3 SER A 196 143.78 -35.46
REMARK 500 4 SER A 110 109.87 -171.35
REMARK 500 4 HIS A 174 26.46 48.61
REMARK 500 4 ASP A 192 132.07 -38.47
REMARK 500 5 ASN A 113 48.19 -90.41
REMARK 500 5 PHE A 175 144.80 -172.37
REMARK 500 5 ARG A 191 125.24 -35.50
REMARK 500 5 PRO A 198 -177.87 -69.77
REMARK 500 6 PHE A 175 148.32 -171.87
REMARK 500 6 MET A 179 48.22 38.81
REMARK 500 6 LYS A 181 142.81 -175.13
REMARK 500 7 SER A 105 85.04 -69.02
REMARK 500 7 SER A 110 -62.97 -100.71
REMARK 500 7 ASN A 113 56.46 -104.11
REMARK 500 7 GLU A 164 -39.03 -35.17
REMARK 500 8 ASN A 113 34.20 -88.60
REMARK 500 8 ASN A 123 -62.86 -102.43
REMARK 500 8 CYS A 124 128.76 -34.38
REMARK 500 8 PHE A 175 134.72 -172.01
REMARK 500 8 LYS A 181 149.21 -174.15
REMARK 500 8 ASP A 192 75.71 -107.09
REMARK 500 9 ASN A 113 41.75 34.42
REMARK 500 9 GLU A 126 -70.17 -34.57
REMARK 500 10 SER A 110 115.06 -35.27
REMARK 500 10 LYS A 111 111.48 -39.34
REMARK 500 10 ARG A 191 39.66 34.30
REMARK 500 10 LYS A 194 136.85 -173.02
REMARK 500 11 LYS A 111 125.53 -39.39
REMARK 500 11 ASN A 113 42.51 -86.84
REMARK 500 11 ASN A 123 -64.22 -100.25
REMARK 500 11 CYS A 124 126.57 -35.13
REMARK 500 11 HIS A 174 25.22 49.31
REMARK 500 11 PHE A 175 145.99 -170.13
REMARK 500 11 SER A 193 168.35 -45.54
REMARK 500 11 PRO A 198 -168.67 -69.70
REMARK 500 11 SER A 200 -69.19 -99.47
REMARK 500 12 LYS A 194 152.97 -41.31
REMARK 500
REMARK 500 THIS ENTRY HAS 75 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002012495.2 RELATED DB: TARGETDB
DBREF 2DGS A 110 195 UNP Q96EP5 DAZP1_HUMAN 110 195
SEQADV 2DGS GLY A 103 UNP Q96EP5 CLONING ARTIFACT
SEQADV 2DGS SER A 104 UNP Q96EP5 CLONING ARTIFACT
SEQADV 2DGS SER A 105 UNP Q96EP5 CLONING ARTIFACT
SEQADV 2DGS GLY A 106 UNP Q96EP5 CLONING ARTIFACT
SEQADV 2DGS SER A 107 UNP Q96EP5 CLONING ARTIFACT
SEQADV 2DGS SER A 108 UNP Q96EP5 CLONING ARTIFACT
SEQADV 2DGS GLY A 109 UNP Q96EP5 CLONING ARTIFACT
SEQADV 2DGS SER A 196 UNP Q96EP5 CLONING ARTIFACT
SEQADV 2DGS GLY A 197 UNP Q96EP5 CLONING ARTIFACT
SEQADV 2DGS PRO A 198 UNP Q96EP5 CLONING ARTIFACT
SEQADV 2DGS SER A 199 UNP Q96EP5 CLONING ARTIFACT
SEQADV 2DGS SER A 200 UNP Q96EP5 CLONING ARTIFACT
SEQADV 2DGS GLY A 201 UNP Q96EP5 CLONING ARTIFACT
SEQRES 1 A 99 GLY SER SER GLY SER SER GLY SER LYS SER ASN LYS ILE
SEQRES 2 A 99 PHE VAL GLY GLY ILE PRO HIS ASN CYS GLY GLU THR GLU
SEQRES 3 A 99 LEU ARG GLU TYR PHE LYS LYS PHE GLY VAL VAL THR GLU
SEQRES 4 A 99 VAL VAL MET ILE TYR ASP ALA GLU LYS GLN ARG PRO ARG
SEQRES 5 A 99 GLY PHE GLY PHE ILE THR PHE GLU ASP GLU GLN SER VAL
SEQRES 6 A 99 ASP GLN ALA VAL ASN MET HIS PHE HIS ASP ILE MET GLY
SEQRES 7 A 99 LYS LYS VAL GLU VAL LYS ARG ALA GLU PRO ARG ASP SER
SEQRES 8 A 99 LYS SER SER GLY PRO SER SER GLY
HELIX 1 1 GLY A 125 LYS A 134 1 10
HELIX 2 2 ASP A 163 HIS A 174 1 12
SHEET 1 A 4 VAL A 139 MET A 144 0
SHEET 2 A 4 PHE A 156 PHE A 161 -1 O THR A 160 N GLU A 141
SHEET 3 A 4 LYS A 114 GLY A 118 -1 N ILE A 115 O ILE A 159
SHEET 4 A 4 GLU A 184 ARG A 187 -1 O LYS A 186 N PHE A 116
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