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 15943

Title: Solution NMR Structure of protein of unknown function yegP from E. coli. Ontario Center for Structural Proteomics target EC0640_1_123 Northeast Structural Genomics Consortium Target ET102.

Authors: Fares, Christophe; Lemak, Alexander; Gutmanas, Aleksandras; Karra, Murthy; Yee, Adelinda; Semesi, Anthony; Arrowsmith, Cheryl

Citation: Fares, Christophe; Lemak, Alexander; Gutmanas, Aleksandras; Karra, Murthy; Yee, Adelinda; Semesi, Anthony; Arrowsmith, Cheryl. "Solution structure of protein yegP from Escherichia Coli."  Not known ., .-..

Assembly members:
protein_of_unkown_function_yegP_from_E.coli, polymer, 116 residues, 12566.956 Da.

Natural source:   Common Name: not available   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
protein_of_unkown_function_yegP_from_E.coli: GVIMAGWFELSKSSDNQFRF VLKAGNGETILTSELYTSKT SAEKGIASVRSNSPQEERYE KKTASNGKFYFNLKAANHQI IGSSQMYATAQSRETGIASV KANGTSQTVKDNTGSN

Data sets:
Data typeCount
13C chemical shifts440
15N chemical shifts120
1H chemical shifts710

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 116 residues - 12566.956 Da.

1   GLYVALILEMETALAGLYTRPPHEGLULEU
2   SERLYSSERSERASPASNGLNPHEARGPHE
3   VALLEULYSALAGLYASNGLYGLUTHRILE
4   LEUTHRSERGLULEUTYRTHRSERLYSTHR
5   SERALAGLULYSGLYILEALASERVALARG
6   SERASNSERPROGLNGLUGLUARGTYRGLU
7   LYSLYSTHRALASERASNGLYLYSPHETYR
8   PHEASNLEULYSALAALAASNHISGLNILE
9   ILEGLYSERSERGLNMETTYRALATHRALA
10   GLNSERARGGLUTHRGLYILEALASERVAL
11   LYSALAASNGLYTHRSERGLNTHRVALLYS
12   ASPASNTHRGLYSERASN

Samples:

sample_1: EC0640, [U-100% 13C; U-100% 15N], 0.4-0.7 mM; tris 10 mM; NaCl 300 mM; benzamidine 1 mM; NaN3 0.01%

sample_conditions_1: ionic strength: 300 mM; pH: 7.0; 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ABACUS, Lemak, Steren, Arrowsmith, Llinas - chemical shift assignment, structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ - refinement

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB36311 BAE76581 BAG77877 BAH46954 BAI26211
EMBL CAP76586 CAQ32494 CAQ89670 CAQ99003 CAR03465
GB AAC75141 AAG57143 AAN43679 AAN81062 AAP17505
REF NP_310915 NP_416584 NP_707972 WP_000899178 WP_000929408
SP P76402 Q83KI3 Q8FG00 Q8X7I0