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 17509

Title: NMR structure of the protein YP_557733.1 from Burkholderia xenovorans

Deposition date: 2011-03-04 Original release date: 2011-03-25

Authors: Jaudzems, Kristaps; Serrano, Pedro; Michael, Geralt; Reto, Horst; Wuthrich, Kurt

Citation: Jaudzems, Kristaps; Serrano, Pedro; Michael, Geralt; Reto, Horst; Wuthrich, Kurt. "Null"  To be Published ., .-..

Assembly members:
YP_557733.1, polymer, 145 residues, 15414.306 Da.

Natural source:   Common Name: Burkholderia xenovorans   Taxonomy ID: 36873   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Burkholderia xenovorans

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

Entity Sequences (FASTA):
YP_557733.1: IPKHPDSEAVAPDPFNPAAT QLLDDTSWVLSAWKQADGTA RAVPSADQGAPITLTLSTST GQRHASGFSGCNRYMGSYAL KDGKLSFGTLGGTRMACMTP GGQIEGAYLNALTHIDRTGV QMRAPQQMQLVLDNGDTLTF DRSTR

Data sets:
Data typeCount
13C chemical shifts462
15N chemical shifts159
1H chemical shifts969

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YP_557733.11

Entities:

Entity 1, YP_557733.1 145 residues - 15414.306 Da.

1   ILEPROLYSHISPROASPSERGLUALAVAL
2   ALAPROASPPROPHEASNPROALAALATHR
3   GLNLEULEUASPASPTHRSERTRPVALLEU
4   SERALATRPLYSGLNALAASPGLYTHRALA
5   ARGALAVALPROSERALAASPGLNGLYALA
6   PROILETHRLEUTHRLEUSERTHRSERTHR
7   GLYGLNARGHISALASERGLYPHESERGLY
8   CYSASNARGTYRMETGLYSERTYRALALEU
9   LYSASPGLYLYSLEUSERPHEGLYTHRLEU
10   GLYGLYTHRARGMETALACYSMETTHRPRO
11   GLYGLYGLNILEGLUGLYALATYRLEUASN
12   ALALEUTHRHISILEASPARGTHRGLYVAL
13   GLNMETARGALAPROGLNGLNMETGLNLEU
14   VALLEUASPASNGLYASPTHRLEUTHRPHE
15   ASPARGSERTHRARG

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 4.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.225 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_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
5D APSY-HACACONHsample_1isotropicsample_conditions_1
4D APSY-HACANHsample_1isotropicsample_conditions_1
5D APSY-CBCACONHsample_1isotropicsample_conditions_1

Software:

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

UNIO, Unio Herrmann Wuthrich - chemical shift assignment, processing, structure solution

TOPSPIN, Bruker Biospin - collection, data analysis, processing

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

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB ABE29681 EIF32471
REF WP_007175698 WP_011487414

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