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 19431

Title: NMR structure of hypothetical protein RUMGNA_01855 from Ruminococcus gnavus ATCC 29149

Deposition date: 2013-08-21 Original release date: 2013-10-21

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

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of a hypothetical protein RUMGNA_01855 from Ruminococcus gnavus ATCC 29149"  .

Assembly members:
entity, polymer, 114 residues, 13280.990 Da.

Natural source:   Common Name: Ruminococcus gnavus ATCC 29149   Taxonomy ID: 411470   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Blautia Ruminococcus gnavus

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

Entity Sequences (FASTA):
entity: GEILKELPEGFDKETVRKQA MEDIEIAQSKDYESWKSRFT KDLQSSLTEESYDSYLKILE KQGEFKEFGKCTYLGQIKDN KKYGGVIIVVKYEEGNVNYS LAYDEDMNLVSFTM

Data sets:
Data typeCount
1H chemical shifts801
13C chemical shifts398
15N chemical shifts121

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hypothetical protein1

Entities:

Entity 1, hypothetical protein 114 residues - 13280.990 Da.

1   GLYGLUILELEULYSGLULEUPROGLUGLY
2   PHEASPLYSGLUTHRVALARGLYSGLNALA
3   METGLUASPILEGLUILEALAGLNSERLYS
4   ASPTYRGLUSERTRPLYSSERARGPHETHR
5   LYSASPLEUGLNSERSERLEUTHRGLUGLU
6   SERTYRASPSERTYRLEULYSILELEUGLU
7   LYSGLNGLYGLUPHELYSGLUPHEGLYLYS
8   CYSTHRTYRLEUGLYGLNILELYSASPASN
9   LYSLYSTYRGLYGLYVALILEILEVALVAL
10   LYSTYRGLUGLUGLYASNVALASNTYRSER
11   LEUALATYRASPGLUASPMETASNLEUVAL
12   SERPHETHRMET

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; D2O, [U-99% 2H], 95%; H2O 5%

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

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
4D APSY HACANHsample_1isotropicsample_conditions_1
5D APSY HACACONHsample_1isotropicsample_conditions_1
5D APSY CBCACONHsample_1isotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

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

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

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

TOPSPIN v3.1, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CCZ66509 CUO03677
GB EDN77700 EGN48378 ETD20298
REF WP_004842842 WP_022038064 WP_055168981

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