BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 17502

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17502
MolProbity Validation Chart

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Title: NMR STRUCTURE OF THE C-TERMINAL RRM DOMAIN OF POLY(U) BINDING 1   PubMed: 21931728

Deposition date: 2011-03-01 Original release date: 2012-03-01

Authors: Santiveri, C.M.; Mirassou, Y.; Rico-Lastres, P.; Martinez-Lumbreras, S.; Perez-Canadillas, J.M.

Citation: Santiveri, Clara; Mirassou, Yasmina; Rico-Lastres, Palma; Martinez-Lumbreras, Santiago; Perez-Canadillas, Jose. "Pub1p C-terminal RRM domain interacts with Tif4631p through a conserved region neighbouring the Pab1p binding site"  PLoS One 6, e24481-. (2011).

Assembly members:
NUCLEAR_AND_CYTOPLASMIC_POLYADENYLATED_RNA-BINDING_PUB1, polymer, 101 residues, 11295.992 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI

Entity Sequences (FASTA):
NUCLEAR_AND_CYTOPLASMIC_POLYADENYLATED_RNA-BINDING_PUB1: GSQTIGLPPQVNPQAVDHII RSAPPRVTTAYIGNIPHFAT EADLIPLFQNFGFILDFKHY PEKGCCFIKYDTHEQAAVCI VALANFPFQGRNLRTGWGKE R

Data sets:
Data typeCount
13C chemical shifts451
15N chemical shifts100
1H chemical shifts697

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1NUCLEAR AND CYTOPLASMIC POLYADENYLATED RNA-BINDING PUB11

Entities:

Entity 1, NUCLEAR AND CYTOPLASMIC POLYADENYLATED RNA-BINDING PUB1 101 residues - 11295.992 Da.

1   GLYSERGLNTHRILEGLYLEUPROPROGLN
2   VALASNPROGLNALAVALASPHISILEILE
3   ARGSERALAPROPROARGVALTHRTHRALA
4   TYRILEGLYASNILEPROHISPHEALATHR
5   GLUALAASPLEUILEPROLEUPHEGLNASN
6   PHEGLYPHEILELEUASPPHELYSHISTYR
7   PROGLULYSGLYCYSCYSPHEILELYSTYR
8   ASPTHRHISGLUGLNALAALAVALCYSILE
9   VALALALEUALAASNPHEPROPHEGLNGLY
10   ARGASNLEUARGTHRGLYTRPGLYLYSGLU
11   ARG

Samples:

sample_1: PUB1 RRM3, [U-99% 15N], 0.3 mM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.5 mM; DSS 0.01 mM; H2O 90%; D2O 10%

sample_2: PUB1 RRM3 0.3 mM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.5 mM; DSS 0.01 mM; H2O 90%; D2O 10%

sample_3: PUB1 RRM3 0.3 mM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.5 mM; DSS 0.1 mM; D2O 100%

sample_4: PUB1 RRM3, [U-99% 13C; U-99% 15N], 0.3 mM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.5 mM; DSS 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESY 2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_4isotropicsample_conditions_1
3D HN(CA)COsample_4isotropicsample_conditions_1
3D HNCAsample_4isotropicsample_conditions_1
3D HN(CO)CAsample_4isotropicsample_conditions_1
3D CBCA(CO)NHsample_4isotropicsample_conditions_1
3D CBCANHsample_4isotropicsample_conditions_1
3D HC -TOCSYsample_4isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_4isotropicsample_conditions_1

Software:

TALOS, CORNILESCU, DELAGLIO - refinement

TOPSPIN, Bruker Biospin - collection

ANALYSIS, CCPN - chemical shift assignment, data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - structure analysis

NMR spectrometers:

  • BRUKER AVANCE 800 MHz

Related Database Links:

PDB
DBJ GAA26078
EMBL CAA95877 CAY82177
GB AAA02808 AAC37348 AAC37364 AHY77075 AJP41312
REF NP_014382
SP P32588
TPG DAA10528

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts