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 16692

Title: Solution NMR structure of a domain of protein A6KY75 from Bacteroides vulgatus, Northeast Structural Genomics target BvR106A

Deposition date: 2010-01-26 Original release date: 2010-03-02

Authors: Mills, Jeffrey; Sukumaran, Dinesh; Sathyamoorthy, Bharathwaj; Belote, Rachel; Ciccosanti, Colleen; Hamilton, Keith; Acton, T.; Xiao, R.; Swapna, GVT; Everett, J.; Montelione, G.; Szyperski, Thomas

Citation: Mills, Jeffrey; Sukumaran, Dinesh; Sathyamoorthy, Bharathwaj; Belote, Rachel; Ciccosanti, Colleen; Hamilton, Keith; Acton, T.; Xiao, R.; Swapna, GVT; Everett, J.; Montelione, G.; Szyperski, Thomas. "Solution NMR structure of a domain of protein A6KY75 from Bacteroides vulgatus, Northeast Structural Genomics target BvR106A."  Not known ., .-..

Assembly members:
BvR106A, polymer, 74 residues, 9095.4 Da.

Natural source:   Common Name: Bacteroides vulgatus   Taxonomy ID: 821   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacteroides vulgatus

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

Entity Sequences (FASTA):
BvR106A: MNQNLQGEWMKNYEELKSFV RKYRRFPKSTEGNLGGWCHT QRKMRKQGKLPNDRRLLLDK IGFVWSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts247
15N chemical shifts77
1H chemical shifts518

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 74 residues - 9095.4 Da.

1   METASNGLNASNLEUGLNGLYGLUTRPMET
2   LYSASNTYRGLUGLULEULYSSERPHEVAL
3   ARGLYSTYRARGARGPHEPROLYSSERTHR
4   GLUGLYASNLEUGLYGLYTRPCYSHISTHR
5   GLNARGLYSMETARGLYSGLNGLYLYSLEU
6   PROASNASPARGARGLEULEULEUASPLYS
7   ILEGLYPHEVALTRPSERLEUGLUHISHIS
8   HISHISHISHIS

Samples:

NC: BvR106A, [U-99% 13C; U-99% 15N], 1.11 mM; D2O, [U-2H], 10%; H2O 90%; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.02%

sample_conditions_1: ionic strength: 235 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQCNCisotropicsample_conditions_1
(4,3)D GFT CABCA(CO)NHNCisotropicsample_conditions_1
(4,3)D GFT HNCABCANCisotropicsample_conditions_1
(4,3)D GFT HABCAB(CO)NHNCisotropicsample_conditions_1
3D HCCH-TOCSYNCisotropicsample_conditions_1
3D simultaneous NOESYNCisotropicsample_conditions_1
3D 1H-15N NOESYNCisotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CSI, Wishart and Sykes - structure solution

TALOS, Cornilescu, Delaglio and Bax - structure solution

CYANA, Herrmann, Guntert and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

Molmol, Koradi, Billeter and Wuthrich - data analysis, refinement

PSVS, Bhattacharya and Montelione - refinement

PROSA, Guntert - processing

VNMRJ, Varian - collection

NMR spectrometers:

  • Varian UnityPlus 750 MHz

Related Database Links:

PDB

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