BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25027

Title: NMR structure of the hypothetical protein BVU_0925 from Bacteroides vulgatus ATCC 8482

Deposition date: 2014-06-18 Original release date: 2014-09-02

Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the hypothetical protein BVU_0925 from Bacteroides vulgatus ATCC 8482"  Not known ., .-..

Assembly members:
entity, polymer, 105 residues, 11296.354 Da.

Natural source:   Common Name: CFB group bacteria   Taxonomy ID: 435590   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacteroides vulgatus

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

Entity Sequences (FASTA):
entity: GHMGSPVSYYFSYADGGTSH TEYPDDSSAGSFILDITSYK KTGNSTKALSWNASGDSWIH VNGSSVSYDENPAKERRTGL VTLKQDESGKTLSLKIVQPG KTSID

Data sets:
Data typeCount
1H chemical shifts654
13C chemical shifts324
15N chemical shifts107

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 105 residues - 11296.354 Da.

1   GLYHISMETGLYSERPROVALSERTYRTYR
2   PHESERTYRALAASPGLYGLYTHRSERHIS
3   THRGLUTYRPROASPASPSERSERALAGLY
4   SERPHEILELEUASPILETHRSERTYRLYS
5   LYSTHRGLYASNSERTHRLYSALALEUSER
6   TRPASNALASERGLYASPSERTRPILEHIS
7   VALASNGLYSERSERVALSERTYRASPGLU
8   ASNPROALALYSGLUARGARGTHRGLYLEU
9   VALTHRLEULYSGLNASPGLUSERGLYLYS
10   THRLEUSERLEULYSILEVALGLNPROGLY
11   LYSTHRSERILEASP

Samples:

sample_1: entity, [U-99% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; H2O 95%; D2O 5%

sample_conditions_1: temperature: 308 K; pH: 6.0; pressure: 1 atm; ionic strength: 0.0798 M

Experiments:

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

Software:

CYANA, G ntert P., Luginbuhl, Guntert, Billeter and Wuthrich - refinement, geometry optimization

TOPSPIN v3.1, Bruker Biospin - collection, processing

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

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

UNP A6KYV6_BACV8
PDB
EMBL CUN71160 CUP76619
GB ABR38620 EGX27430
REF WP_008670674 WP_011964947 WP_057249593 WP_057279461

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