Header list of 2cpq.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 19-MAY-05 2CPQ
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL KH DOMAIN OF HUMAN FXR1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FRAGILE X MENTAL RETARDATION SYNDROME RELATED PROTEIN 1,
COMPND 3 ISOFORM B';
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: KH DOMAIN;
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: FXR1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040621-02;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS KH 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 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 2CPQ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CPQ 1 VERSN
REVDAT 1 19-NOV-05 2CPQ 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 KH DOMAIN OF HUMAN FXR1
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 2CPQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024484.
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 : 1.20MM 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 : 800 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 SER A 206 153.12 -45.09
REMARK 500 1 HIS A 237 48.28 35.20
REMARK 500 1 PRO A 292 97.77 -69.77
REMARK 500 2 ALA A 216 144.38 -34.81
REMARK 500 2 PRO A 289 87.14 -69.79
REMARK 500 3 SER A 239 -69.30 -91.58
REMARK 500 3 ASP A 284 97.42 -36.15
REMARK 500 3 PRO A 292 94.51 -69.78
REMARK 500 3 SER A 293 37.53 37.26
REMARK 500 4 HIS A 237 41.50 34.77
REMARK 500 4 PRO A 289 2.83 -69.78
REMARK 500 4 SER A 294 102.27 -58.29
REMARK 500 5 LEU A 215 58.05 -97.71
REMARK 500 5 ASP A 284 107.11 -38.74
REMARK 500 5 SER A 293 150.01 -38.50
REMARK 500 6 HIS A 237 45.37 34.85
REMARK 500 6 SER A 294 111.45 -169.22
REMARK 500 7 ALA A 216 133.53 -171.47
REMARK 500 7 SER A 239 -61.51 -92.80
REMARK 500 7 ASP A 284 134.84 -35.63
REMARK 500 7 SER A 290 170.42 -48.98
REMARK 500 8 GLU A 227 -28.21 -38.15
REMARK 500 8 HIS A 237 35.03 73.73
REMARK 500 8 GLU A 280 153.10 -47.92
REMARK 500 9 SER A 209 145.52 -36.86
REMARK 500 9 GLN A 214 46.71 -94.12
REMARK 500 9 ALA A 269 -33.61 -38.50
REMARK 500 9 ASP A 284 112.25 -34.93
REMARK 500 9 PRO A 289 93.07 -69.78
REMARK 500 10 LEU A 215 82.81 -66.11
REMARK 500 10 HIS A 237 33.22 35.37
REMARK 500 10 SER A 293 43.68 37.31
REMARK 500 10 SER A 294 -53.30 -131.56
REMARK 500 11 SER A 206 150.09 -39.51
REMARK 500 11 HIS A 237 30.64 72.93
REMARK 500 12 LEU A 215 45.44 -84.90
REMARK 500 12 HIS A 237 31.34 74.40
REMARK 500 13 ALA A 216 145.62 -38.72
REMARK 500 13 HIS A 237 48.80 35.91
REMARK 500 13 ASP A 284 113.27 -35.56
REMARK 500 13 SER A 294 161.55 -40.51
REMARK 500 14 SER A 207 100.03 -49.73
REMARK 500 14 HIS A 237 49.56 34.63
REMARK 500 14 SER A 239 -61.24 -93.74
REMARK 500 14 ALA A 269 -34.11 -36.80
REMARK 500 15 SER A 210 82.25 -63.44
REMARK 500 15 ALA A 216 -178.90 -69.94
REMARK 500 15 ARG A 226 172.67 -53.90
REMARK 500 15 PRO A 289 92.83 -69.77
REMARK 500 16 GLN A 214 96.60 -64.39
REMARK 500
REMARK 500 THIS ENTRY HAS 68 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: HSS001001578 RELATED DB: TARGETDB
DBREF 2CPQ A 212 289 UNP P51114 FXR1_HUMAN 212 289
SEQADV 2CPQ GLY A 205 UNP P51114 CLONING ARTIFACT
SEQADV 2CPQ SER A 206 UNP P51114 CLONING ARTIFACT
SEQADV 2CPQ SER A 207 UNP P51114 CLONING ARTIFACT
SEQADV 2CPQ GLY A 208 UNP P51114 CLONING ARTIFACT
SEQADV 2CPQ SER A 209 UNP P51114 CLONING ARTIFACT
SEQADV 2CPQ SER A 210 UNP P51114 CLONING ARTIFACT
SEQADV 2CPQ GLY A 211 UNP P51114 CLONING ARTIFACT
SEQADV 2CPQ SER A 290 UNP P51114 CLONING ARTIFACT
SEQADV 2CPQ GLY A 291 UNP P51114 CLONING ARTIFACT
SEQADV 2CPQ PRO A 292 UNP P51114 CLONING ARTIFACT
SEQADV 2CPQ SER A 293 UNP P51114 CLONING ARTIFACT
SEQADV 2CPQ SER A 294 UNP P51114 CLONING ARTIFACT
SEQADV 2CPQ GLY A 295 UNP P51114 CLONING ARTIFACT
SEQRES 1 A 91 GLY SER SER GLY SER SER GLY THR LYS GLN LEU ALA ALA
SEQRES 2 A 91 ALA PHE HIS GLU GLU PHE VAL VAL ARG GLU ASP LEU MET
SEQRES 3 A 91 GLY LEU ALA ILE GLY THR HIS GLY SER ASN ILE GLN GLN
SEQRES 4 A 91 ALA ARG LYS VAL PRO GLY VAL THR ALA ILE GLU LEU ASP
SEQRES 5 A 91 GLU ASP THR GLY THR PHE ARG ILE TYR GLY GLU SER ALA
SEQRES 6 A 91 ASP ALA VAL LYS LYS ALA ARG GLY PHE LEU GLU PHE VAL
SEQRES 7 A 91 GLU ASP PHE ILE GLN VAL PRO SER GLY PRO SER SER GLY
HELIX 1 1 LEU A 229 ILE A 234 1 6
HELIX 2 2 SER A 239 ARG A 245 1 7
HELIX 3 3 ALA A 269 ARG A 276 1 8
SHEET 1 A 3 PHE A 219 VAL A 224 0
SHEET 2 A 3 THR A 261 GLY A 266 -1 O ILE A 264 N GLU A 221
SHEET 3 A 3 VAL A 250 ASP A 256 -1 N GLU A 254 O ARG A 263
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