Header list of 1p1t.pdb file
Complete list - b 23 2 Bytes
HEADER RNA BINDING PROTEIN 14-APR-03 1P1T
TITLE NMR STRUCTURE OF THE N-TERMINAL RRM DOMAIN OF CLEAVAGE STIMULATION
TITLE 2 FACTOR 64 KDA SUBUNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CLEAVAGE STIMULATION FACTOR, 64 KDA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL RRM OF CSTF-64;
COMPND 5 SYNONYM: CSTF 64 KDA SUBUNIT, CF-1 64 KDA SUBUNIT;
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: CSTF2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS RNA RECOGNITION MOTIF, C-TERMINAL HELIX, N-TERMINAL HELIX, RNA
KEYWDS 2 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.M.PEREZ-CANADILLAS,G.VARANI
REVDAT 3 23-FEB-22 1P1T 1 REMARK
REVDAT 2 24-FEB-09 1P1T 1 VERSN
REVDAT 1 12-AUG-03 1P1T 0
JRNL AUTH J.M.PEREZ-CANADILLAS,G.VARANI
JRNL TITL RECOGNITION OF GU-RICH POLYADENYLATION REGULATORY ELEMENTS
JRNL TITL 2 BY HUMAN CSTF-64 PROTEIN
JRNL REF EMBO J. V. 22 2821 2003
JRNL REFN ISSN 0261-4189
JRNL PMID 12773396
JRNL DOI 10.1093/EMBOJ/CDG259
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2001, DYANA 1.5
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, PFEIFER, BAX
REMARK 3 (NMRPIPE), GUNTERT, MUMENTHALER, HERRMANN (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1486 NOE-DERIVED DISTANCE CONTRAINTS AND 115 DIHEDRAL ANGLE
REMARK 3 RESTRAINS FOR PHI AND PSI BACKBONE ANGLES OBTAINED FROM THE
REMARK 3 ANALYSIS OF THE 13C CHEMICAL SHIFTS.
REMARK 4
REMARK 4 1P1T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018907.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 20MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM CSTF U-15N, 20MM PHOSPHATE
REMARK 210 BUFFER; 1MM CSTF U-15N,13C, 20MM
REMARK 210 PHOSPHATE BUFFER; 1MM CSTF ,
REMARK 210 20MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 15N-HSQC; 13C-
REMARK 210 HSQC; HNCA; HNCO; CBCA(CO)NH;
REMARK 210 HCCH-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, TALOS 2001
REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 20 STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONCANCE NMR
REMARK 210 SPECTROSCOPY
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 REMARK: NULL
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 ALA A 10 45.25 177.43
REMARK 500 1 ARG A 16 76.12 -111.18
REMARK 500 1 SER A 17 125.04 175.27
REMARK 500 1 LEU A 77 -90.92 -103.14
REMARK 500 1 ASN A 78 88.65 37.62
REMARK 500 1 PHE A 82 -40.52 178.76
REMARK 500 1 ARG A 85 -66.90 -144.02
REMARK 500 1 ALA A 86 142.03 164.06
REMARK 500 2 PRO A 9 -162.52 -75.07
REMARK 500 2 ALA A 10 89.94 -170.57
REMARK 500 2 ARG A 16 -61.48 -93.10
REMARK 500 2 SER A 17 115.00 -37.49
REMARK 500 2 PRO A 24 -164.12 -74.94
REMARK 500 2 LEU A 77 -92.00 -103.46
REMARK 500 2 ASN A 78 85.00 36.34
REMARK 500 2 PHE A 82 -43.94 -178.60
REMARK 500 2 ARG A 85 -69.64 -139.16
REMARK 500 2 ALA A 86 142.19 164.76
REMARK 500 2 ARG A 88 99.72 -66.93
REMARK 500 2 THR A 106 111.40 -160.53
REMARK 500 2 ALA A 108 89.85 64.50
REMARK 500 3 ALA A 10 59.34 -151.47
REMARK 500 3 ARG A 16 71.62 -107.78
REMARK 500 3 SER A 17 126.34 176.31
REMARK 500 3 VAL A 43 -76.15 -72.06
REMARK 500 3 LEU A 77 -91.79 -103.62
REMARK 500 3 ASN A 78 87.09 37.38
REMARK 500 3 PHE A 82 -43.12 -174.61
REMARK 500 3 ARG A 85 -76.99 -142.50
REMARK 500 3 ALA A 86 141.08 172.30
REMARK 500 4 PRO A 9 -89.71 -74.99
REMARK 500 4 ALA A 10 -5.57 82.95
REMARK 500 4 ARG A 16 54.57 -115.08
REMARK 500 4 VAL A 43 -81.00 -66.07
REMARK 500 4 PHE A 45 114.21 -160.76
REMARK 500 4 LEU A 77 -91.35 -104.75
REMARK 500 4 ASN A 78 90.17 39.59
REMARK 500 4 PHE A 82 117.68 -178.27
REMARK 500 4 SER A 83 13.64 80.18
REMARK 500 5 ARG A 16 59.99 -110.04
REMARK 500 5 SER A 17 122.60 -170.79
REMARK 500 5 VAL A 43 -70.87 -75.13
REMARK 500 5 LEU A 77 -91.45 -102.08
REMARK 500 5 ASN A 78 89.00 37.29
REMARK 500 5 PHE A 82 117.64 -179.07
REMARK 500 5 SER A 83 13.31 82.26
REMARK 500 5 ALA A 108 71.55 50.69
REMARK 500 6 PRO A 9 -89.46 -75.02
REMARK 500 6 ALA A 10 100.27 165.35
REMARK 500 6 SER A 17 120.34 -34.13
REMARK 500
REMARK 500 THIS ENTRY HAS 201 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1P1T A 8 111 UNP P33240 CSTF2_HUMAN 8 111
SEQRES 1 A 104 ASP PRO ALA VAL ASP ARG SER LEU ARG SER VAL PHE VAL
SEQRES 2 A 104 GLY ASN ILE PRO TYR GLU ALA THR GLU GLU GLN LEU LYS
SEQRES 3 A 104 ASP ILE PHE SER GLU VAL GLY PRO VAL VAL SER PHE ARG
SEQRES 4 A 104 LEU VAL TYR ASP ARG GLU THR GLY LYS PRO LYS GLY TYR
SEQRES 5 A 104 GLY PHE CYS GLU TYR GLN ASP GLN GLU THR ALA LEU SER
SEQRES 6 A 104 ALA MET ARG ASN LEU ASN GLY ARG GLU PHE SER GLY ARG
SEQRES 7 A 104 ALA LEU ARG VAL ASP ASN ALA ALA SER GLU LYS ASN LYS
SEQRES 8 A 104 GLU GLU LEU LYS SER LEU GLY THR GLY ALA PRO VAL ILE
HELIX 1 1 VAL A 11 ARG A 16 1 6
HELIX 2 2 THR A 28 GLU A 38 1 11
HELIX 3 3 ASP A 66 LEU A 77 1 12
HELIX 4 4 LYS A 96 GLY A 105 1 10
SHEET 1 A 4 SER A 44 ASP A 50 0
SHEET 2 A 4 LYS A 55 GLU A 63 -1 O PHE A 61 N ARG A 46
SHEET 3 A 4 VAL A 18 GLY A 21 -1 N VAL A 20 O GLY A 60
SHEET 4 A 4 ARG A 88 ASN A 91 -1 O ASP A 90 N PHE A 19
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