HEADER RNA BINDING PROTEIN 26-MAY-99 2U2F
TITLE SOLUTION STRUCTURE OF THE SECOND RNA-BINDING DOMAIN OF HU2AF65
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (SPLICING FACTOR U2AF 65 KD SUBUNIT);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SECOND RNA-BINDING DOMAIN;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PK7
KEYWDS SPLICING, U2 SNRNP, RBD, RNA-BINDING PROTEIN, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS, RNA
KEYWDS 3 BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR T.ITO,Y.MUTO,M.R.GREEN,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 5 27-DEC-23 2U2F 1 REMARK
REVDAT 4 16-MAR-22 2U2F 1 KEYWDS REMARK
REVDAT 3 24-FEB-09 2U2F 1 VERSN
REVDAT 2 01-APR-03 2U2F 1 JRNL
REVDAT 1 20-AUG-99 2U2F 0
JRNL AUTH T.ITO,Y.MUTO,M.R.GREEN,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURES OF THE FIRST AND SECOND RNA-BINDING
JRNL TITL 2 DOMAINS OF HUMAN U2 SMALL NUCLEAR RIBONUCLEOPROTEIN PARTICLE
JRNL TITL 3 AUXILIARY FACTOR (U2AF(65)).
JRNL REF EMBO J. V. 18 4523 1999
JRNL REFN ISSN 0261-4189
JRNL PMID 10449418
JRNL DOI 10.1093/EMBOJ/18.16.4523
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING
REMARK 4
REMARK 4 2U2F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000001117.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 PRO A 10 -91.62 -77.86
REMARK 500 ASN A 11 -28.91 175.53
REMARK 500 ASN A 14 -104.50 -131.30
REMARK 500 ASP A 36 -70.48 -48.35
REMARK 500 SER A 37 25.16 48.27
REMARK 500 ALA A 38 -36.73 -132.37
REMARK 500 LEU A 63 -61.50 -147.95
REMARK 500 GLN A 67 172.25 -48.60
REMARK 500 LEU A 68 -75.58 -133.00
REMARK 500 SER A 79 68.71 -160.07
REMARK 500 VAL A 80 -93.11 -108.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 77 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1U2F RELATED DB: PDB
REMARK 900 RELATED ID: AR_001000504.1 RELATED DB: TARGETDB
DBREF 2U2F A 1 85 UNP P26368 U2AF2_HUMAN 258 342
SEQRES 1 A 85 ALA HIS LYS LEU PHE ILE GLY GLY LEU PRO ASN TYR LEU
SEQRES 2 A 85 ASN ASP ASP GLN VAL LYS GLU LEU LEU THR SER PHE GLY
SEQRES 3 A 85 PRO LEU LYS ALA PHE ASN LEU VAL LYS ASP SER ALA THR
SEQRES 4 A 85 GLY LEU SER LYS GLY TYR ALA PHE CYS GLU TYR VAL ASP
SEQRES 5 A 85 ILE ASN VAL THR ASP GLN ALA ILE ALA GLY LEU ASN GLY
SEQRES 6 A 85 MET GLN LEU GLY ASP LYS LYS LEU LEU VAL GLN ARG ALA
SEQRES 7 A 85 SER VAL GLY ALA LYS ASN ALA
HELIX 1 H1 ASP A 15 SER A 24 1 10
HELIX 2 H2 ILE A 53 LEU A 63 1 11
SHEET 1 S1 1 ALA A 30 VAL A 34 0
SHEET 1 S2 1 TYR A 45 GLU A 49 0
SHEET 1 S3 1 LYS A 3 GLY A 7 0
SHEET 1 S4 1 LEU A 74 ARG A 77 0
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
(ATOM LINES ARE NOT SHOWN.)
END