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 17020

Title: Solution NMR structure of CV_0373(175-257) protein from Chromobacterium violaceum, Northeast Structural Genomics Consortium Target CvR118A   PubMed: 22116783

Authors: Yang, Yunhuang; Ramelot, Theresa; Wang, Dongyan; Ciccosanti, Colleen; Mao, Lei; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Ramelot, Theresa; Yang, Yunhuang; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of BT_0084, a conjugative transposon lipoprotein from Bacteroides thetaiotamicron"  Proteins ., .-. (2011).

Assembly members:
CV_0373(175-257)_protein, polymer, 92 residues, 10580 Da.

Natural source:   Common Name: Chromobacterium violaceum   Taxonomy ID: 536   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Chromobacterium violaceum

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

Entity Sequences (FASTA):
CV_0373(175-257)_protein: MPHKEKHPLQDMFTSAIEAV ARDSGWAELSAVGSYLAKND PSFDPRNWGHGRLSQMVKKL DFLTVQESRNGSKLHSEIRL RHDGLEHHHHHH

Data typeCount
13C chemical shifts382
15N chemical shifts100
1H chemical shifts618

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CV_0373(175-257) protein1

Entities:

Entity 1, CV_0373(175-257) protein 92 residues - 10580 Da.

CV_0373(175-257) protein from Chromobacterium violaceum, preceded by non-native N-terminal Met and followed by 8 non-native C-terminal residues (LEHHHHHH)

1   METPROHISLYSGLULYSHISPROLEUGLN
2   ASPMETPHETHRSERALAILEGLUALAVAL
3   ALAARGASPSERGLYTRPALAGLULEUSER
4   ALAVALGLYSERTYRLEUALALYSASNASP
5   PROSERPHEASPPROARGASNTRPGLYHIS
6   GLYARGLEUSERGLNMETVALLYSLYSLEU
7   ASPPHELEUTHRVALGLNGLUSERARGASN
8   GLYSERLYSLEUHISSERGLUILEARGLEU
9   ARGHISASPGLYLEUGLUHISHISHISHIS
10   HISHIS

Samples:

NC_sample: CV_0373(175-257) protein, [U-100% 13C; U-100% 15N], 0.9 ± 0.09 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %

NC5_sample: CV_0373(175-257) protein, [U-5% 13C; U-100% 15N], 0.82 ± 0.08 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %

NC_sample_in_D2O: CV_0373(175-257) protein, [U-100% 13C; U-100% 15N], 0.9 ± 0.09 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %

sample_conditions_1: ionic strength: 0.2 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC_CTNC5_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESYNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
3D (H)CCH-TOCSYNC_sample_in_D2Oisotropicsample_conditions_1
4D CC NOESYNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-15N HSQC_swN150ppmNC_sampleisotropicsample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - refinement

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.1, (PdbStat)-Roberto Tejero and Gaetano T. Montelione - structure solution

PINE v1.0, Bahrami, A., Assadi, A., Markley, J. L. & Eghbalnia, H. - autoassignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker AvanceIII 850 MHz

Related Database Links:

PDB
GB AAQ58051 ERE17978 KJH66165 KMN49431 KMN84167
REF WP_021475679 WP_045052090 WP_046158018 WP_048404151