HEADER TRANSCRIPTION 05-APR-07 2YTC
TITLE SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN PRE-MRNA-SPLICING FACTOR
TITLE 2 RBM22
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRE-MRNA-SPLICING FACTOR RBM22;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RNA BINDING MOTIF;
COMPND 5 SYNONYM: RNA-BINDING MOTIF PROTEIN 22, ZINC FINGER CCCH DOMAIN-
COMPND 6 CONTAINING PROTEIN 16;
COMPND 7 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: RBM22;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P060313-05;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RRM DOMAIN, RBD, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.KASAHARA,K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 16-MAR-22 2YTC 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2YTC 1 VERSN
REVDAT 1 09-OCT-07 2YTC 0
JRNL AUTH N.KASAHARA,K.TSUDA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,
JRNL AUTH 2 M.SHIROUZU,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RNA BINDING DOMAIN IN
JRNL TITL 2 PRE-MRNA-SPLICING FACTOR RBM22
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 2YTC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000027108.
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 : 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_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 : NMRPIPE 20060702, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9820, CYANA 2.0.17
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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
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 234 42.25 -109.98
REMARK 500 1 LYS A 236 -66.89 -93.36
REMARK 500 1 GLN A 275 43.94 34.25
REMARK 500 1 ARG A 284 -36.95 -36.72
REMARK 500 1 PHE A 295 97.07 -47.86
REMARK 500 1 ASN A 296 25.50 45.17
REMARK 500 2 SER A 229 41.90 38.60
REMARK 500 2 LYS A 236 89.43 -63.03
REMARK 500 2 THR A 237 31.05 38.44
REMARK 500 2 GLN A 275 51.09 33.04
REMARK 500 2 ARG A 284 -35.31 -36.13
REMARK 500 2 PHE A 295 109.42 -55.10
REMARK 500 2 LYS A 297 -38.43 -130.96
REMARK 500 3 ARG A 256 -38.67 -39.72
REMARK 500 3 GLN A 275 46.90 34.37
REMARK 500 3 ARG A 284 -34.54 -36.90
REMARK 500 3 ASN A 296 25.03 40.51
REMARK 500 3 LEU A 298 96.52 -61.82
REMARK 500 4 SER A 228 83.50 -66.98
REMARK 500 4 GLU A 234 90.31 -63.50
REMARK 500 4 TYR A 260 -36.19 -39.93
REMARK 500 4 GLN A 275 47.91 35.15
REMARK 500 4 ARG A 284 -35.69 -37.88
REMARK 500 4 PHE A 295 103.11 -57.00
REMARK 500 4 ASN A 296 27.69 42.13
REMARK 500 5 SER A 229 42.25 -104.66
REMARK 500 5 THR A 237 36.80 37.51
REMARK 500 5 GLN A 275 47.37 33.63
REMARK 500 5 PHE A 295 109.47 -50.35
REMARK 500 5 LYS A 297 -33.69 -133.71
REMARK 500 5 LEU A 298 98.30 -67.62
REMARK 500 6 SER A 231 108.99 -166.88
REMARK 500 6 THR A 239 35.39 -95.35
REMARK 500 6 TYR A 260 -35.67 -39.92
REMARK 500 6 ARG A 284 -39.62 -38.29
REMARK 500 6 ASN A 296 26.16 40.18
REMARK 500 7 THR A 239 36.19 -97.57
REMARK 500 7 GLN A 275 50.45 32.26
REMARK 500 7 ARG A 284 -34.20 -36.31
REMARK 500 7 PHE A 295 109.79 -54.08
REMARK 500 7 ASN A 296 29.71 41.51
REMARK 500 7 LEU A 298 98.03 -63.40
REMARK 500 8 SER A 229 -50.98 -126.13
REMARK 500 8 THR A 237 38.10 39.00
REMARK 500 8 GLN A 275 53.14 34.25
REMARK 500 8 PHE A 295 107.06 -46.37
REMARK 500 8 ASN A 296 27.73 40.12
REMARK 500 9 GLN A 275 50.16 32.25
REMARK 500 9 ARG A 284 -37.01 -36.00
REMARK 500 9 PHE A 295 104.11 -57.13
REMARK 500
REMARK 500 THIS ENTRY HAS 115 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001002688.1 RELATED DB: TARGETDB
DBREF 2YTC A 234 311 UNP Q9NW64 RBM22_HUMAN 227 304
SEQADV 2YTC GLY A 227 UNP Q9NW64 EXPRESSION TAG
SEQADV 2YTC SER A 228 UNP Q9NW64 EXPRESSION TAG
SEQADV 2YTC SER A 229 UNP Q9NW64 EXPRESSION TAG
SEQADV 2YTC GLY A 230 UNP Q9NW64 EXPRESSION TAG
SEQADV 2YTC SER A 231 UNP Q9NW64 EXPRESSION TAG
SEQADV 2YTC SER A 232 UNP Q9NW64 EXPRESSION TAG
SEQADV 2YTC GLY A 233 UNP Q9NW64 EXPRESSION TAG
SEQRES 1 A 85 GLY SER SER GLY SER SER GLY GLU ASP LYS THR ILE THR
SEQRES 2 A 85 THR LEU TYR VAL GLY GLY LEU GLY ASP THR ILE THR GLU
SEQRES 3 A 85 THR ASP LEU ARG ASN HIS PHE TYR GLN PHE GLY GLU ILE
SEQRES 4 A 85 ARG THR ILE THR VAL VAL GLN ARG GLN GLN CYS ALA PHE
SEQRES 5 A 85 ILE GLN PHE ALA THR ARG GLN ALA ALA GLU VAL ALA ALA
SEQRES 6 A 85 GLU LYS SER PHE ASN LYS LEU ILE VAL ASN GLY ARG ARG
SEQRES 7 A 85 LEU ASN VAL LYS TRP GLY ARG
HELIX 1 1 THR A 251 GLN A 261 1 11
HELIX 2 2 GLN A 272 GLN A 274 5 3
HELIX 3 3 THR A 283 LYS A 293 1 11
SHEET 1 A 4 ILE A 265 VAL A 271 0
SHEET 2 A 4 CYS A 276 PHE A 281 -1 O GLN A 280 N THR A 267
SHEET 3 A 4 LEU A 241 GLY A 244 -1 N LEU A 241 O ILE A 279
SHEET 4 A 4 VAL A 307 TRP A 309 -1 O LYS A 308 N TYR A 242
SHEET 1 B 2 ILE A 299 VAL A 300 0
SHEET 2 B 2 ARG A 303 ARG A 304 -1 O ARG A 303 N VAL A 300
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
(ATOM LINES ARE NOT SHOWN.)
END
