BMRB Entry 19974

Title:
NMR structure of BA42 protein from the psychrophilic bacteria Bizionia argentinensis sp. nov.
Deposition date:
2014-05-14
Original release date:
2014-08-25
Authors:
Cicero, Daniel; Aran, Martin; Smal, Clara; Pellizza, Leonardo; Gallo, Mariana
Citation:

Citation: Aran, Martin; Smal, Clara; Pellizza, Leonardo; Gallo, Mariana; Otero, Lisandro; Klinke, Sebastian; Goldbaum, Fernando; Ithurralde, Esteban; Bercovich, Andres; MacCormack, Walter; Turjanski, Adrian; Cicero, Daniel. "Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain"  Proteins ., .-. (2014).
PubMed: 25116514

Assembly members:

Assembly members:
entity, polymer, 145 residues, 16498.727 Da.

Natural source:

Natural source:   Common Name: CFB group bacteria   Taxonomy ID: 1046627   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bizionia argentinensis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pDEST527

Data sets:
Data typeCount
13C chemical shifts638
15N chemical shifts145
1H chemical shifts987

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BA42 protein1

Entities:

Entity 1, BA42 protein 145 residues - 16498.727 Da.

1   METSERLYSILEGLUGLUPHELEUTHRALA
2   GLUGLUGLULYSALAILEVALASPALAILE
3   ARGASPALAGLULYSASNTHRSERGLYGLU
4   ILEARGVALHISLEUGLULYSTHRSERGLU
5   ILEASPVALPHEASPARGALAMETASPVAL
6   PHEHISASNLEULYSMETASPASNTHRLYS
7   LEUGLNASNGLYVALLEUILETYRVALALA
8   VALGLUASPLYSTHRPHEVALILETYRGLY
9   ASPLYSGLYILEASNASPVALVALSERASP
10   ASPPHETRPASPTHRTHRARGASNALAILE
11   GLNLEUGLNPHELYSGLNGLYASNPHELYS
12   GLNGLYLEUVALASPGLYILEGLULYSALA
13   GLYMETALALEUALALYSTYRPHEPROTRP
14   LYSLYSASPASPILEASPGLULEUPROASN
15   THRILESERLYSGLY

Samples:

sample_1: TRIS 10 mM; D2O, [U-100% 2H], 5%; H2O 95%; entity, [U-15N; U-13C], mM

sample_conditions_1: ionic strength: 10 mM; pH: 7.5; pressure: 1 atm; temperature: 301 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1

Software:

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

TOPSPIN, Bruker Biospin - collection

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks