BMRB Entry 15320

Title:
Solution structure of UPF0350 protein VC_2471: Northeast Structural Genomics Target VcR36
Deposition date:
2007-06-20
Original release date:
2007-08-15
Authors:
Wu, Yibing; Parish, David; Singarapu, Kiran kumar; Sukumaran, Dinesh; Eletski, Alex; Shastry, Ritu; Nwosu, Chioma; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Wu, Yibing; Parish, David; Singarapu, Kiran kumar; Sukumaran, Dinesh; Eletski, Alex; Shastry, Ritu; Nwosu, Chioma; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas. "Solution structure of UPF0350 protein VC_2471: Northeast Structural Genomics Target VcR36"  .

Assembly members:

Assembly members:
UPF0350 protein VC_2471, polymer, 94 residues, 10938.577 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 666   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Vibrio cholerae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21(DE3)+ Magic

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts324
15N chemical shifts98
1H chemical shifts657

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UPF0350 protein VC_24711

Entities:

Entity 1, UPF0350 protein VC_2471 94 residues - 10938.577 Da.

1   METTYRTHRALAGLUGLNLYSALAARGILE
2   LYSTRPALACYSARGARGGLYMETLEUGLU
3   LEUASPVALVALILEMETPROPHEPHEGLU
4   GLUCYSPHEASPSERLEUTHRGLUSERGLU
5   GLNASPASPPHEVALALALEULEUGLUSER
6   ASPASPPROASPLEUPHEALATRPVALMET
7   GLYHISGLYARGCYSGLUASNLEUGLYLEU
8   ALAALAMETVALASPLYSILEVALALAHIS
9   ASNLEUSERLYSVALARGLEUGLUHISHIS
10   HISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.2 mM

sample_2: entity, [U-5% 13C; U-100% 15N], 1.1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
4,3D, GFT HNNCABCAsample_1isotropicsample_conditions_1
4,3D, GFT CABCACONNHsample_1isotropicsample_conditions_1
4,3D, GFT HCCH COSYsample_1isotropicsample_conditions_1
3D, 15N-13C RESOLVEDSIMULTANIOUS NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

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

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

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

XEASY, Bartels et al. - peak picking

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAP03857
EMBL CFW06271 CPR24076 CPR24090 CQB51440 CRZ37920
GB AAF95613 ABQ19558 ACP06692 ACP10573 ACQ60053
REF NP_232100 WP_000287741 WP_000287742 WP_000287743 WP_000287745
SP Q9KPA2
AlphaFold Q9KPA2

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