BMRB Entry 16927

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16927
MolProbity Validation Chart

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Title:
Solution structure of SuR18C from Streptococcus thermophilus. Northeast Structural Genomics Consortium Target SuR18C
Deposition date:
2010-05-13
Original release date:
2012-02-22
Authors:
Liu, Yizhou; Lee, Hsiau-Wei; Belote, Rachel; Ciccosanti, Colleen; Hamilton, Keith; Acton, T.; Xiao, R.; Everett, John; Montelione, Gaetano; Prestegard, James
Citation:

Citation: Liu, Yizhou; Lee, Hsiau-Wei; Belote, Rachel; Ciccosanti, Colleen; Hamilton, Keith; Acton, T.; Xiao, R.; Everett, John; Montelione, Gaetano; Prestegard, James. "Chemical shift assignment for SuR18C from Streptococcus thermophilus, Northeast Structural Genomics Consortium Target SuR18C"  .

Assembly members:

Assembly members:
protein sur18c, polymer, 100 residues, 11015.632 Da.

Natural source:

Natural source:   Common Name: Streptococcus thermophilus   Taxonomy ID: 1308   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Streptococcus thermophilus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
protein sur18c: KISLRKLSKSVPVKLELTGD KASNVSSISYSFDRGHVTIV GSQEAMDKIDSITVPVDISQ VTEDTSKTLELKAEGVTVQP STVKVNLKVTQKLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts386
15N chemical shifts96
1H chemical shifts617

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein sur18c1

Entities:

Entity 1, protein sur18c 100 residues - 11015.632 Da.

1   LYSILESERLEUARGLYSLEUSERLYSSER
2   VALPROVALLYSLEUGLULEUTHRGLYASP
3   LYSALASERASNVALSERSERILESERTYR
4   SERPHEASPARGGLYHISVALTHRILEVAL
5   GLYSERGLNGLUALAMETASPLYSILEASP
6   SERILETHRVALPROVALASPILESERGLN
7   VALTHRGLUASPTHRSERLYSTHRLEUGLU
8   LEULYSALAGLUGLYVALTHRVALGLNPRO
9   SERTHRVALLYSVALASNLEULYSVALTHR
10   GLNLYSLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: protein sur18c, [U-99% 13C; U-99% 15N], 0.935 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 100 mM; sodium azide 3 mM

sample_conditions_1: ionic strength: 0.3 M; pH: 6.5; 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_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
2D J-mod NHsample_1isotropicsample_conditions_1
2D J-mod NCOsample_1isotropicsample_conditions_1
2D J-mod NHsample_1anisotropicsample_conditions_1
2D J-mod NCOsample_1anisotropicsample_conditions_1

Software:

VNMRJ, Varian - collection

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

SPARKY, Goddard - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
EMBL CCC20158 CDA39160
GB AAV60886 AAV62796 ABJ66419 ADQ63244 AFJ83617
REF WP_002951082 WP_011226156

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