BMRB Entry 17799

Title:
NMR structure of the protein YP_001302112.1 from Parabacteroides distasonis
Deposition date:
2011-07-22
Original release date:
2011-08-25
Authors:
Serrano, Pedro; Mohanty, Biswaranjan; Geralt, Michael; Wuthrich, Kurt
Citation:

Citation: Serrano, Pedro; Mohanty, Biswaranjan; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the protein YP_001302112.1 from Parabacteroides distasonis"  .

Assembly members:

Assembly members:
entity, polymer, 200 residues, 13807.372 Da.

Natural source:

Natural source:   Common Name: Parabacteroides distasonis   Taxonomy ID: 823   Superkingdom: Bacteria   Kingdom: Parabacteroides   Genus/species: Parabacteroides distasonis

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts488
15N chemical shifts124
1H chemical shifts784

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YP_0013021121

Entities:

Entity 1, YP_001302112 200 residues - 13807.372 Da.

1   METARGLYSTYRLEUTYRLEUSERALAVAL
2   CYSVALCYSMETALALEUCYSPHEVALGLY
3   CYSSERLYSASPASPASPGLUPROGLYGLY
4   LYSGLYALAMETTYRGLUVALTHRILEGLU
5   GLNSERGLYASPPHEARGSERPHEILELYS
6   SERVALVALVALVALALAASNGLYTHRGLN
7   LEULYSASPGLYALATHRGLYGLUSERLEU
8   ALASERPROVALILELEUSERASPGLUGLU
9   LEUALAVALGLULYSVALTHRLEUSERTHR
10   THRGLYLYSALAILEGLUPHEALAVALSER
11   GLYGLYVALVALASPGLYGLUASPGLYVAL
12   VALASNGLUPROMETGLNTRPVALVALTHR
13   VALTYRLYSASNGLYLYSGLUILEGLULYS
14   LYSSERLEUVALPHEARGASPGLYLYSGLU
15   ILESERTHRASPASPLEUASNLEUTYRTYR
16   ASNVALVALASPGLYGLUASPGLYVALVAL
17   ASNGLUPROMETGLNTRPVALVALTHRVAL
18   TYRLYSASNGLYLYSGLUILEGLULYSLYS
19   SERLEUVALPHEARGASPGLYLYSGLUILE
20   SERTHRASPASPLEUASNLEUTYRTYRASN

Samples:

sample_1: YP_001302112, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 25 mM; sodium azide 5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.18 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
5D APSY CBCACONHsample_1isotropicsample_conditions_1
4D APSY HACANHsample_1isotropicsample_conditions_1
5D APSY HACACONHsample_1isotropicsample_conditions_1

Software:

CYANA, G ntert P. - refinement, structure solution

TOPSPIN, Bruker Biospin - collection, data analysis, processing

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

UNIO, Unio Herrmann Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 17806
PDB
EMBL CUP04873 CUP86285 CUQ25107
GB AAO45318 ABR42490 EFG18115 EFK63750 EIY16653
REF NP_818973 WP_005842168 WP_007659490 WP_032583709

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