BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19167

Title: Structural determination of the Citrus sinensis Poly(A)-Binding Protein CsPABP1

Deposition date: 2013-04-16 Original release date: 2014-04-14

Authors: Sforca, Mauricio; Domingues, Mariane; Zeri, Ana; Benedetti, Celso

Citation: Sforca, Mauricio; Domingues, Mariane; Zeri, Ana; Benedetti, Celso. "Structural determination of the Citrus sinensis Poly(A)-Binding Protein CsPABP1"  To be Published ., .-..

Assembly members:
CsPABP1, polymer, 155 residues, 17187.258 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
CsPABP1: MGSSHHHHHHSSGLVPRGSH MGSDLEDMKKRLKEIEEEAG ALREMQAKVEKEMGAVQDSS STSATQAEKEEVDSRSIYVG NVDYACTPEEVQQHFQSCGT VNRVTILTDKFGQPKGFAYV EFVEIDAVQNALLLNETELH GRQLKVSAKRTNIPG

Data sets:
Data typeCount
13C chemical shifts447
15N chemical shifts108
1H chemical shifts626

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1CsPABP11

Entities:

Entity 1, CsPABP1 155 residues - 17187.258 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METGLYSERASPLEUGLUASPMETLYSLYS
4   ARGLEULYSGLUILEGLUGLUGLUALAGLY
5   ALALEUARGGLUMETGLNALALYSVALGLU
6   LYSGLUMETGLYALAVALGLNASPSERSER
7   SERTHRSERALATHRGLNALAGLULYSGLU
8   GLUVALASPSERARGSERILETYRVALGLY
9   ASNVALASPTYRALACYSTHRPROGLUGLU
10   VALGLNGLNHISPHEGLNSERCYSGLYTHR
11   VALASNARGVALTHRILELEUTHRASPLYS
12   PHEGLYGLNPROLYSGLYPHEALATYRVAL
13   GLUPHEVALGLUILEASPALAVALGLNASN
14   ALALEULEULEUASNGLUTHRGLULEUHIS
15   GLYARGGLNLEULYSVALSERALALYSARG
16   THRASNILEPROGLY

Samples:

sample_1: CsPABP1, [U-98% 15N], 0.6 mM; sodium phosphate 50 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

sample_2: CsPABP1, [U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate 50 mM; sodium chloride 20 mM; D2O 100%

sample_3: CsPABP1, [U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate 50 mM; sodium chloride 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.70 M; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HCACOsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CAN77560
GB EEF51643 EOY22721 ESR50273 ESR50274 KDO57709
REF XP_002511041 XP_006437033 XP_006437034 XP_006485035 XP_007038220

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