BMRB Entry 19627

Title:
NMR strucutre of the hypothetical protein BACUNI_03114 from Bacteroides uniformis ATCC 8492
Deposition date:
2013-11-21
Original release date:
2013-12-20
Authors:
Shnitkind, Sergey; Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation:

Citation: Shnitkind, Sergey; Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR strucutre of the hypothetical protein BACUNI_03114 from Bacteroides uniformis ATCC 8492"  .

Assembly members:

Assembly members:
entity, polymer, 110 residues, 12814.421 Da.

Natural source:

Natural source:   Common Name: CFB group bacteria   Taxonomy ID: 820   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacteroides uniformis

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts380
15N chemical shifts113
1H chemical shifts773

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 110 residues - 12814.421 Da.

1   GLYASPGLUASPASPLYSVALGLUILEPRO
2   GLNLEUVALGLYLYSTRPILEVALLYSGLU
3   PROVALLEUGLNASPASPPHEVALTHRCYS
4   TYRTHRPHEASNALAASPLYSTHRTYRGLU
5   VALTYRTHRGLYSERPROLEUSERASNGLY
6   VALPROPHEARGGLYTHRTYRILEILESER
7   LEUASPGLULYSLEUILELYSLEUTYRASP
8   LYSGLUGLUHISCYSTHRGLUGLNTYRHIS
9   ILELEULYSLEUTHRSERLYSGLUMETLYS
10   TRPGLUASNALASERPROLYSASPGLYASN
11   SERASPLYSARGLEUGLULYSTYRASNASP

Samples:

sample_1: sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; entity, [U-99% 13C; U-99% 15N], 1.2 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.0798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
4D HACANH APSYsample_1isotropicsample_conditions_1
5D HACACONH APSYsample_1isotropicsample_conditions_1
5D CBCACONH APSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bartels et al., Bruker Biospin - collection, data analysis, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

j-UNIO, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking, structure solution

OPALp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CUN47051 CUP01591 CUQ01617
GB EDO53099 EFA19032 EFV25840
REF WP_005829739

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