Header list of 1opi.pdb file
Complete list - b 23 2 Bytes
HEADER RNA BINDING PROTEIN 05-MAR-03 1OPI
TITLE SOLUTION STRUCTURE OF THE THIRD RNA RECOGNITION MOTIF (RRM) OF U2AF65
TITLE 2 IN COMPLEX WITH AN N-TERMINAL SF1 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPLICING FACTOR U2AF 65 KDA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL RRM DOMAIN;
COMPND 5 SYNONYM: U2 AUXILIARY FACTOR 65 KDA SUBUNIT, U2 SNRNP AUXILIARY
COMPND 6 FACTOR LARGE SUBUNIT, HU2AF(65);
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SPLICING FACTOR SF1;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: N-TERMINAL PEPTIDE;
COMPND 12 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET24D;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED AND DERIVED
SOURCE 13 FROM THE N-TERMINUS OF SF1. THE SEQUENCE OF THE PEPTIDE IS NATURALLY
SOURCE 14 FOUND IN HOMO SAPIENS (HUMAN).
KEYWDS NON-CANONICAL RNA RECOGNITION MOTIF, 4-STRANDED ANTI-PARALLEL BETA-
KEYWDS 2 SHEET, 2 ALPHA HELICES ADDITIONALLY EXTENDED BY A THIRD HELIX C, RNA
KEYWDS 3 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR P.SELENKO,G.GREGOROVIC,R.SPRANGERS,G.STIER,Z.RHANI,A.KRAMER,M.SATTLER
REVDAT 3 23-FEB-22 1OPI 1 REMARK
REVDAT 2 24-FEB-09 1OPI 1 VERSN
REVDAT 1 16-MAR-04 1OPI 0
JRNL AUTH P.SELENKO,G.GREGOROVIC,R.SPRANGERS,G.STIER,Z.RHANI,A.KRAMER,
JRNL AUTH 2 M.SATTLER
JRNL TITL STRUCTURAL BASIS FOR THE MOLECULAR RECOGNITION BETWEEN HUMAN
JRNL TITL 2 SPLICING FACTORS U2AF65 AND SF1/MBBP
JRNL REF MOL.CELL V. 11 965 2003
JRNL REFN ISSN 1097-2765
JRNL PMID 12718882
JRNL DOI 10.1016/S1097-2765(03)00115-1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, ARIA 1.2
REMARK 3 AUTHORS : BRUNGER (CNS), NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT OF PROTEIN STRUCTURES IN
REMARK 3 WATER SOLVENT, ACCORDING TO LINGE ET AL. (PROTEINS 50:496 -506,
REMARK 3 2003)
REMARK 4
REMARK 4 1OPI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018535.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : 50MM SALT
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM 15N,13C U2AF65-RRM3 + 1MM
REMARK 210 UNLABELED SF1_10-25, 30MM
REMARK 210 PHOSPHATE BUFFER, 20MM NACL, 3MM
REMARK 210 DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_ 15N
REMARK 210 -SEPARATED_NOESY; 3D_13C/15N-
REMARK 210 EDITED/FILTERED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS
REMARK 210 USING CNS AND ARIA FOR AMBIGUOUS
REMARK 210 DISTANCE RESTRAINTS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 HIS A 373 113.69 -173.91
REMARK 500 1 THR A 375 -71.27 -114.78
REMARK 500 1 GLU A 376 -45.91 -176.87
REMARK 500 1 MET A 383 14.45 -164.89
REMARK 500 1 LEU A 389 34.85 -82.87
REMARK 500 1 SER A 407 30.33 -90.03
REMARK 500 1 PRO A 427 77.05 -66.29
REMARK 500 1 ARG A 452 -152.21 -74.80
REMARK 500 1 LYS A 453 117.03 -160.84
REMARK 500 1 ALA A 455 -50.85 -161.18
REMARK 500 1 ASN A 456 24.95 -157.24
REMARK 500 1 PHE A 474 105.96 63.49
REMARK 500 1 SER B 14 -166.76 -102.06
REMARK 500 1 LYS B 18 -54.25 -163.85
REMARK 500 1 TRP B 22 53.09 -142.02
REMARK 500 1 ASN B 23 -156.53 -80.23
REMARK 500 1 GLN B 24 -37.71 -169.32
REMARK 500 2 HIS A 373 98.48 -176.19
REMARK 500 2 GLU A 376 -45.92 -176.24
REMARK 500 2 LEU A 389 37.73 -86.54
REMARK 500 2 PRO A 418 157.52 -47.07
REMARK 500 2 GLU A 425 35.15 -92.19
REMARK 500 2 PRO A 427 80.51 -65.53
REMARK 500 2 ARG A 452 -164.76 -74.05
REMARK 500 2 ALA A 455 -49.77 -157.71
REMARK 500 2 ASN A 456 23.68 -160.23
REMARK 500 2 ASP A 467 -78.66 -63.13
REMARK 500 2 PHE A 474 -90.34 -81.44
REMARK 500 2 SER B 14 -96.58 56.69
REMARK 500 2 LYS B 15 -25.31 -159.78
REMARK 500 2 ARG B 19 -61.19 -164.16
REMARK 500 2 SER B 20 102.81 60.14
REMARK 500 2 TRP B 22 91.98 57.68
REMARK 500 3 HIS A 373 136.39 66.47
REMARK 500 3 THR A 375 -76.40 -100.37
REMARK 500 3 GLU A 376 -43.05 -175.43
REMARK 500 3 LEU A 389 40.90 -83.53
REMARK 500 3 SER A 407 31.58 -90.35
REMARK 500 3 PRO A 418 152.72 -42.58
REMARK 500 3 GLU A 425 34.25 -89.69
REMARK 500 3 PRO A 427 76.94 -66.41
REMARK 500 3 ARG A 452 -162.00 -108.22
REMARK 500 3 ALA A 455 62.56 -152.24
REMARK 500 3 ARG B 21 162.51 62.37
REMARK 500 3 TRP B 22 90.99 53.71
REMARK 500 4 THR A 375 -77.53 -101.55
REMARK 500 4 GLU A 376 -45.78 -175.68
REMARK 500 4 LEU A 389 38.74 -85.98
REMARK 500 4 SER A 407 31.01 -90.07
REMARK 500 4 PRO A 420 125.93 -30.80
REMARK 500
REMARK 500 THIS ENTRY HAS 169 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1O0P RELATED DB: PDB
REMARK 900 THE UNREFINED NMR ENSEMBLE OF THE SAME PROTEIN COMPLEX
DBREF 1OPI A 372 475 UNP P26368 U2AF2_HUMAN 372 475
DBREF 1OPI B 13 25 UNP Q15637 SF01_HUMAN 13 25
SEQRES 1 A 104 GLY HIS PRO THR GLU VAL LEU CYS LEU MET ASN MET VAL
SEQRES 2 A 104 LEU PRO GLU GLU LEU LEU ASP ASP GLU GLU TYR GLU GLU
SEQRES 3 A 104 ILE VAL GLU ASP VAL ARG ASP GLU CYS SER LYS TYR GLY
SEQRES 4 A 104 LEU VAL LYS SER ILE GLU ILE PRO ARG PRO VAL ASP GLY
SEQRES 5 A 104 VAL GLU VAL PRO GLY CYS GLY LYS ILE PHE VAL GLU PHE
SEQRES 6 A 104 THR SER VAL PHE ASP CYS GLN LYS ALA MET GLN GLY LEU
SEQRES 7 A 104 THR GLY ARG LYS PHE ALA ASN ARG VAL VAL VAL THR LYS
SEQRES 8 A 104 TYR CYS ASP PRO ASP SER TYR HIS ARG ARG ASP PHE TRP
SEQRES 1 B 13 PRO SER LYS LYS ARG LYS ARG SER ARG TRP ASN GLN ASP
HELIX 1 1 ASP A 391 SER A 407 1 17
HELIX 2 2 SER A 438 THR A 450 1 13
HELIX 3 3 ASP A 465 ARG A 471 1 7
SHEET 1 A 4 VAL A 412 GLU A 416 0
SHEET 2 A 4 LYS A 431 PHE A 436 -1 O GLU A 435 N SER A 414
SHEET 3 A 4 VAL A 377 MET A 381 -1 N LEU A 380 O ILE A 432
SHEET 4 A 4 VAL A 460 CYS A 464 -1 O LYS A 462 N CYS A 379
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 - b 23 2 Bytes