BMRB Entry 17957

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17957
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
1H, 13C and 15N chemical shifts assignments of BA42 from Bizionia argentinensis
Deposition date:
2011-09-23
Original release date:
2011-10-24
Authors:
Smal, Clara; Aran, Martin; Gallo, Mariana; Cicero, Daniel
Citation:

Citation: Smal, Clara; Aran, Martin; Lanzarotti, Esteban; Papouchado, Mariana; Foti, Marcelo; Marti, Marcelo; Coria, Silvia; Vazquez, Susana; Bercovich, Andres; Mac Cormack, Walter; Turjanski, Adrian; Gallo, Mariana; Cicero, Daniel. "1H, 15N and 13C chemical shift assignments of the BA42 protein of the psychrophilic bacteria Bizionia argentinensis sp. nov."  Biomol. NMR Assignments 6, 181-183 (2012).
PubMed: 22201035

Assembly members:

Assembly members:
BA42, polymer, 145 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Bizionia argentinensis   Taxonomy ID: 456455   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bizionia argentinensis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 11 a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BA42: MSKIEEFLTAEEEKAIVDAI RDAEKNTSGEIRVHLEKTSE IDVFDRAMDVFHNLKMDNTK LQNGVLIYVAVEDKTFVIYG DKGINDVVSDDFWDTTRNAI QLQFKQGNFKQGLVDGIEKA GMALAKYFPWKKDDIDELPN TISKG

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
1BA421

Entities:

Entity 1, BA42 145 residues - Formula weight is not available

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: BA42, [U-100% 13C; U-100% 15N], 0.5 mM; potassium phosphate 20 mM; PMSF 0.02 mM; beta-mercaptoethanol 10 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 301 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - data analysis

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

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19974
PDB
GB EGV44639
REF WP_008634846

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