Header list of 2cpn.pdb file
Complete list - r 9 2 Bytes
HEADER GENE REGULATION 19-MAY-05 2CPN
TITLE SOLUTION STRUCTURE OF THE SECOND DSRBD OF TAR RNA-BINDING PROTEIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TAR RNA-BINDING PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOUBLE-STRANDED RNA BINDING DOMAIN;
COMPND 5 SYNONYM: TRANS-ACTIVATION RESPONSIVE RNA-BINDING PROTEIN;
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: TARBP2;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040322-28;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS DOUBLE-STRANDED RNA BINDING DOMAIN, DSRBD, DSRM., STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, GENE REGULATION
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 09-MAR-22 2CPN 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CPN 1 VERSN
REVDAT 1 19-NOV-05 2CPN 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 SECOND DSRBD OF TAR RNA-BINDING
JRNL TITL 2 PROTEIN 2
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 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CPN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024483.
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 : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.15MM 13C/15N-PROTEIN; 20MM D
REMARK 210 -TRIS-HCL(PH7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801/20031121,
REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.925,
REMARK 210 CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYANAMICS,
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,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 GLU A 157 161.57 -42.18
REMARK 500 1 THR A 181 -60.91 -92.58
REMARK 500 1 PRO A 186 -169.22 -69.72
REMARK 500 2 LEU A 175 143.21 -37.77
REMARK 500 2 PRO A 186 -179.34 -69.78
REMARK 500 3 ASN A 159 144.05 -170.92
REMARK 500 3 PRO A 186 -168.42 -69.73
REMARK 500 3 SER A 229 -61.46 -98.22
REMARK 500 4 ASN A 159 141.20 -171.25
REMARK 500 4 PRO A 186 -164.24 -69.75
REMARK 500 4 GLU A 199 -72.37 -34.01
REMARK 500 4 SER A 230 54.93 -90.87
REMARK 500 5 SER A 145 41.17 -92.41
REMARK 500 5 SER A 156 47.93 -108.23
REMARK 500 5 PRO A 186 -174.77 -69.74
REMARK 500 5 ARG A 189 51.91 -113.34
REMARK 500 5 SER A 226 165.26 -49.87
REMARK 500 6 LEU A 175 143.29 -38.77
REMARK 500 6 PRO A 186 -165.55 -69.78
REMARK 500 6 ALA A 213 -39.61 -35.80
REMARK 500 6 SER A 230 -62.30 -129.38
REMARK 500 7 SER A 145 105.90 -55.72
REMARK 500 7 PRO A 186 -169.32 -69.80
REMARK 500 8 SER A 147 84.37 -64.67
REMARK 500 8 ASN A 159 139.85 -171.05
REMARK 500 8 PRO A 186 -173.13 -69.79
REMARK 500 8 GLU A 199 -70.26 -34.15
REMARK 500 8 ALA A 213 -37.62 -35.24
REMARK 500 9 SER A 144 127.90 -39.91
REMARK 500 9 ASN A 159 155.21 -40.09
REMARK 500 9 LEU A 164 -35.97 -39.81
REMARK 500 9 LEU A 175 142.05 -34.25
REMARK 500 9 PRO A 186 -165.56 -69.77
REMARK 500 9 GLU A 199 -73.79 -34.14
REMARK 500 10 VAL A 151 117.97 -38.65
REMARK 500 10 SER A 156 -55.03 -132.47
REMARK 500 10 LEU A 175 142.35 -34.03
REMARK 500 10 PRO A 186 -164.76 -69.79
REMARK 500 10 ALA A 213 -31.38 -39.71
REMARK 500 10 PRO A 228 -174.69 -69.77
REMARK 500 11 SER A 147 -59.36 -122.07
REMARK 500 11 PRO A 186 -174.13 -69.75
REMARK 500 11 ALA A 213 -31.04 -35.99
REMARK 500 11 SER A 230 155.27 -48.37
REMARK 500 12 SER A 147 44.89 34.69
REMARK 500 12 GLU A 157 45.78 -82.07
REMARK 500 12 LEU A 175 143.99 -39.70
REMARK 500 12 PRO A 186 -172.23 -69.76
REMARK 500 12 GLU A 199 -74.33 -34.30
REMARK 500 12 PRO A 228 90.21 -69.83
REMARK 500
REMARK 500 THIS ENTRY HAS 86 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000376.1 RELATED DB: TARGETDB
DBREF 2CPN A 150 225 UNP Q15633 TRBP2_HUMAN 150 225
SEQADV 2CPN GLY A 143 UNP Q15633 CLONING ARTIFACT
SEQADV 2CPN SER A 144 UNP Q15633 CLONING ARTIFACT
SEQADV 2CPN SER A 145 UNP Q15633 CLONING ARTIFACT
SEQADV 2CPN GLY A 146 UNP Q15633 CLONING ARTIFACT
SEQADV 2CPN SER A 147 UNP Q15633 CLONING ARTIFACT
SEQADV 2CPN SER A 148 UNP Q15633 CLONING ARTIFACT
SEQADV 2CPN GLY A 149 UNP Q15633 CLONING ARTIFACT
SEQADV 2CPN SER A 226 UNP Q15633 CLONING ARTIFACT
SEQADV 2CPN GLY A 227 UNP Q15633 CLONING ARTIFACT
SEQADV 2CPN PRO A 228 UNP Q15633 CLONING ARTIFACT
SEQADV 2CPN SER A 229 UNP Q15633 CLONING ARTIFACT
SEQADV 2CPN SER A 230 UNP Q15633 CLONING ARTIFACT
SEQADV 2CPN GLY A 231 UNP Q15633 CLONING ARTIFACT
SEQRES 1 A 89 GLY SER SER GLY SER SER GLY PRO VAL SER PRO GLN GLN
SEQRES 2 A 89 SER GLU CYS ASN PRO VAL GLY ALA LEU GLN GLU LEU VAL
SEQRES 3 A 89 VAL GLN LYS GLY TRP ARG LEU PRO GLU TYR THR VAL THR
SEQRES 4 A 89 GLN GLU SER GLY PRO ALA HIS ARG LYS GLU PHE THR MET
SEQRES 5 A 89 THR CYS ARG VAL GLU ARG PHE ILE GLU ILE GLY SER GLY
SEQRES 6 A 89 THR SER LYS LYS LEU ALA LYS ARG ASN ALA ALA ALA LYS
SEQRES 7 A 89 MET LEU LEU ARG VAL SER GLY PRO SER SER GLY
HELIX 1 1 VAL A 161 LYS A 171 1 11
HELIX 2 2 LYS A 210 VAL A 225 1 16
SHEET 1 A 3 GLU A 177 SER A 184 0
SHEET 2 A 3 GLU A 191 VAL A 198 -1 O THR A 193 N GLN A 182
SHEET 3 A 3 PHE A 201 GLY A 207 -1 O GLU A 203 N CYS A 196
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