Header list of 2cq4.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 19-MAY-05 2CQ4
TITLE SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN RNA BINDING MOTIF PROTEIN
TITLE 2 23
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA BINDING MOTIF PROTEIN 23;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA RECOGNITION MOTIF;
COMPND 5 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: RBM23;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050131-08;
SOURCE 8 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 K.TSUDA,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 2CQ4 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CQ4 1 VERSN
REVDAT 1 19-NOV-05 2CQ4 0
JRNL AUTH K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN RNA BINDING
JRNL TITL 2 MOTIF PROTEIN 23
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 2CQ4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024495.
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 : 2.07MM 13C/15N-PROTEIN, 20MM D
REMARK 210 -TRIS-HCL (PH 7.0), 100MM NACL,
REMARK 210 1MM D-DTT, 0.02% NAN3, 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 0.9297, CYANA 2.0.17
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 SER A 126 143.71 -172.19
REMARK 500 1 VAL A 139 41.81 -86.06
REMARK 500 1 PRO A 144 -19.01 -45.78
REMARK 500 1 ARG A 150 43.99 -83.94
REMARK 500 1 ARG A 160 50.96 -118.39
REMARK 500 1 THR A 211 102.17 -35.52
REMARK 500 1 ARG A 214 107.98 -46.75
REMARK 500 1 PRO A 219 152.27 -49.07
REMARK 500 1 ASN A 230 -39.90 -38.74
REMARK 500 1 SER A 237 159.85 -43.14
REMARK 500 2 LEU A 142 94.17 -69.19
REMARK 500 2 PRO A 144 -19.42 -45.04
REMARK 500 2 ARG A 150 37.70 -83.35
REMARK 500 2 ASP A 165 -36.86 -38.54
REMARK 500 2 ARG A 188 -59.89 -120.93
REMARK 500 2 ARG A 189 -51.20 -129.84
REMARK 500 2 THR A 211 118.13 -36.76
REMARK 500 2 ARG A 214 104.63 -47.49
REMARK 500 2 SER A 225 42.57 -88.57
REMARK 500 3 PRO A 134 172.07 -47.23
REMARK 500 3 GLU A 137 154.73 -37.26
REMARK 500 3 PRO A 144 -19.36 -45.19
REMARK 500 3 ARG A 150 43.99 -87.70
REMARK 500 3 ARG A 160 42.01 -98.28
REMARK 500 3 ASP A 184 -59.18 -126.99
REMARK 500 3 SER A 187 -60.32 -101.98
REMARK 500 3 THR A 211 98.18 -35.79
REMARK 500 3 ARG A 214 108.71 -53.11
REMARK 500 3 GLN A 226 43.61 -85.86
REMARK 500 3 PRO A 235 42.10 -78.18
REMARK 500 4 LEU A 142 115.44 -34.74
REMARK 500 4 PRO A 144 -16.05 -48.88
REMARK 500 4 ARG A 150 46.80 -82.50
REMARK 500 4 ARG A 160 46.67 -98.57
REMARK 500 4 SER A 183 40.71 75.02
REMARK 500 4 ARG A 185 77.99 -116.57
REMARK 500 4 ASN A 186 40.01 37.81
REMARK 500 4 ARG A 188 155.20 -38.59
REMARK 500 4 LYS A 191 126.40 -35.38
REMARK 500 4 THR A 211 99.50 -38.01
REMARK 500 4 ARG A 214 109.90 -54.51
REMARK 500 4 ALA A 224 107.53 -59.09
REMARK 500 4 GLN A 226 41.00 -94.70
REMARK 500 4 ARG A 231 56.68 -92.31
REMARK 500 4 SER A 236 106.01 -59.31
REMARK 500 4 SER A 237 -55.99 -128.02
REMARK 500 5 SER A 129 52.14 34.36
REMARK 500 5 LYS A 132 45.39 34.42
REMARK 500 5 PRO A 144 -17.36 -47.40
REMARK 500 5 ARG A 150 39.57 -82.29
REMARK 500
REMARK 500 THIS ENTRY HAS 185 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002012635.1 RELATED DB: TARGETDB
DBREF 2CQ4 A 132 232 UNP Q86U06 RBM23_HUMAN 132 232
SEQADV 2CQ4 GLY A 125 UNP Q86U06 CLONING ARTIFACT
SEQADV 2CQ4 SER A 126 UNP Q86U06 CLONING ARTIFACT
SEQADV 2CQ4 SER A 127 UNP Q86U06 CLONING ARTIFACT
SEQADV 2CQ4 GLY A 128 UNP Q86U06 CLONING ARTIFACT
SEQADV 2CQ4 SER A 129 UNP Q86U06 CLONING ARTIFACT
SEQADV 2CQ4 SER A 130 UNP Q86U06 CLONING ARTIFACT
SEQADV 2CQ4 GLY A 131 UNP Q86U06 CLONING ARTIFACT
SEQADV 2CQ4 SER A 233 UNP Q86U06 CLONING ARTIFACT
SEQADV 2CQ4 GLY A 234 UNP Q86U06 CLONING ARTIFACT
SEQADV 2CQ4 PRO A 235 UNP Q86U06 CLONING ARTIFACT
SEQADV 2CQ4 SER A 236 UNP Q86U06 CLONING ARTIFACT
SEQADV 2CQ4 SER A 237 UNP Q86U06 CLONING ARTIFACT
SEQADV 2CQ4 GLY A 238 UNP Q86U06 CLONING ARTIFACT
SEQRES 1 A 114 GLY SER SER GLY SER SER GLY LYS SER PRO VAL ARG GLU
SEQRES 2 A 114 PRO VAL ASP ASN LEU SER PRO GLU GLU ARG ASP ALA ARG
SEQRES 3 A 114 THR VAL PHE CYS MET GLN LEU ALA ALA ARG ILE ARG PRO
SEQRES 4 A 114 ARG ASP LEU GLU ASP PHE PHE SER ALA VAL GLY LYS VAL
SEQRES 5 A 114 ARG ASP VAL ARG ILE ILE SER ASP ARG ASN SER ARG ARG
SEQRES 6 A 114 SER LYS GLY ILE ALA TYR VAL GLU PHE CYS GLU ILE GLN
SEQRES 7 A 114 SER VAL PRO LEU ALA ILE GLY LEU THR GLY GLN ARG LEU
SEQRES 8 A 114 LEU GLY VAL PRO ILE ILE VAL GLN ALA SER GLN ALA GLU
SEQRES 9 A 114 LYS ASN ARG LEU SER GLY PRO SER SER GLY
HELIX 1 1 GLU A 145 ARG A 150 1 6
HELIX 2 2 ARG A 162 SER A 171 1 10
HELIX 3 3 GLU A 200 GLN A 202 5 3
HELIX 4 4 SER A 203 THR A 211 1 9
HELIX 5 5 SER A 225 SER A 233 1 9
SHEET 1 A 5 VAL A 176 ILE A 181 0
SHEET 2 A 5 ALA A 194 PHE A 198 -1 O TYR A 195 N ARG A 180
SHEET 3 A 5 THR A 151 MET A 155 -1 N CYS A 154 O ALA A 194
SHEET 4 A 5 VAL A 218 ALA A 224 -1 O ILE A 221 N MET A 155
SHEET 5 A 5 GLN A 213 LEU A 215 -1 N LEU A 215 O VAL A 218
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