BMRB Entry 19453

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19453
MolProbity Validation Chart

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Title:
NMR structure of the protein ZP_02042476.1 from Ruminococcus gnavus
Deposition date:
2013-08-27
Original release date:
2013-11-11
Authors:
Martin, Bryan; Serrano, Pedro; Geralt, Michael; Dutta, Samit; Wuthrich, Kurt
Citation:

Citation: Martin, Bryan; Wuthrich, Kurt; Serrano, Pedro; Geralt, Michael; Dutta, Samit. "NMR structure of the protein ZP_02042476.1 from Ruminococcus gnavus."  .

Assembly members:

Assembly members:
entity, polymer, 100 residues, 11710.976 Da.

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 33038   Superkingdom: Bacteria   Kingdom: Firmicutes   Genus/species: Ruminococcus gnavus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: PILPKAENVDSICIDFTNSI QKIYDDSESIQKILSEIATG KRTEKQSIQDYPSAEEYGTI NIENNGGMTTMFYYEENGKY YIECPYKGIYEIENNFEDMI

Data sets:
Data typeCount
13C chemical shifts325
15N chemical shifts108
1H chemical shifts688

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1SP17945A1

Entities:

Entity 1, SP17945A 100 residues - 11710.976 Da.

1   PROILELEUPROLYSALAGLUASNVALASP
2   SERILECYSILEASPPHETHRASNSERILE
3   GLNLYSILETYRASPASPSERGLUSERILE
4   GLNLYSILELEUSERGLUILEALATHRGLY
5   LYSARGTHRGLULYSGLNSERILEGLNASP
6   TYRPROSERALAGLUGLUTYRGLYTHRILE
7   ASNILEGLUASNASNGLYGLYMETTHRTHR
8   METPHETYRTYRGLUGLUASNGLYLYSTYR
9   TYRILEGLUCYSPROTYRLYSGLYILETYR
10   GLUILEGLUASNASNPHEGLUASPMETILE

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; D2O 5%; H2O 95%

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, G ntert, P. - structure solution

TOPSPIN, Bruker Biospin - collection, data analysis, processing

UNIO v2010, Herrmann ann Wuthrich - chemical shift assignment, peak picking, structure solution

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CCZ67861 CUO51325
GB EDN76176 EGN49208 ETD16178
REF WP_004844251 WP_024854441

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