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 19433

Title: NMR structure of the protein YP_002937094.1 from Eubacterium rectale

Deposition date: 2013-08-19 Original release date: 2013-09-03

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

Citation: Proudfoot, Andrew; Wuthrich, Kurt; Serrano, Pedro; Geralt, Michael; Dutta, Samit. "NMR structure of the protein YP_002937094.1 from Eubacterium rectale"  Not known ., .-..

Assembly members:
entity, polymer, 103 residues, 11358.535 Da.

Natural source:   Common Name: Eubacterium rectale   Taxonomy ID: 39491   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Eubacterium rectale

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

Entity Sequences (FASTA):
entity: GAQDGKETTTIRLINQTYFN VKNIKVTWNDGKEQTVNTLG SHDSIDFSSDAGSVYKMDVT GTTQSGEKFTGHFKGLVGKD TRVFIELDENADVQVFIPQG EID

Data sets:
Data typeCount
13C chemical shifts339
15N chemical shifts112
1H chemical shifts693

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YP_002937094.11

Entities:

Entity 1, YP_002937094.1 103 residues - 11358.535 Da.

1   GLYALAGLNASPGLYLYSGLUTHRTHRTHR
2   ILEARGLEUILEASNGLNTHRTYRPHEASN
3   VALLYSASNILELYSVALTHRTRPASNASP
4   GLYLYSGLUGLNTHRVALASNTHRLEUGLY
5   SERHISASPSERILEASPPHESERSERASP
6   ALAGLYSERVALTYRLYSMETASPVALTHR
7   GLYTHRTHRGLNSERGLYGLULYSPHETHR
8   GLYHISPHELYSGLYLEUVALGLYLYSASP
9   THRARGVALPHEILEGLULEUASPGLUASN
10   ALAASPVALGLNVALPHEILEPROGLNGLY
11   GLUILEASP

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM; H20 95%; D2O 5%

sample_conditions_1: ionic strength: 0.220 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
APSY 4D-HACANHsample_1isotropicsample_conditions_1
APSY 5D-CBCACONHsample_1isotropicsample_conditions_1
APSY 5D-HACACONHsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

UNIO, Herrmann and Wuthrich - chemical shift assignment, structure solution

CARA, Keller and Wuthrich - chemical shift assignment

TOPSPIN, Bruker Biospin - collection, processing

Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CBK93813 CDC69040 CUN23035 CUN83241
GB ACR74960
REF WP_012742060 WP_055223681

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