BMRB Entry 15604

Title:
Solution NMR structure of Ssl0352 protein from Synechocystis sp. - Northeast Structural Genomics Consortium target SgR42
Deposition date:
2007-12-22
Original release date:
2008-03-07
Authors:
Eletsky, Alexander; Sukumaran, Dinesh; Wang, Dongyan; Hamilton, Keith; Foote, Erica; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Eletsky, Alexander; Sukumaran, Dinesh; Wang, Dongyan; Hamilton, Keith; Foote, Erica; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Rost, Burkhard; Acton, Thomas; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of Ssl0352 protein from Synechocystis sp."  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:

Assembly members:
SgR42_protein, polymer, 66 residues, 7657.740 Da.

Natural source:

Natural source:   Common Name: Synechocystis sp.   Taxonomy ID: 1143   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Synechocystis sp.

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts268
15N chemical shifts66
1H chemical shifts446

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SgR42_protein1

Entities:

Entity 1, SgR42_protein 66 residues - 7657.740 Da.

C-terminal His-tag LEHHHHHH

1   METILEPHEPROGLYALATHRVALARGVAL
2   THRASNVALASPASPTHRTYRTYRARGPHE
3   GLUGLYLEUVALGLNARGVALSERASPGLY
4   LYSALAALAVALLEUPHEGLUASNGLYASN
5   TRPASPLYSLEUVALTHRPHEARGLEUSER
6   GLULEUGLUALAVALLYSPROILELEUGLU
7   HISHISHISHISHISHIS

Samples:

NC: SgR42 protein, [U-100% 13C; U-100% 15N], 1.17 mM; calcium chloride 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; sodium azide 0.03%

NC5: SgR42 protein, [U-5% 13C; U-100% 15N], 1.17 mM; calcium chloride 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; sodium azide 0.03%

sample_conditions_1: ionic strength: 135 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNCisotropicsample_conditions_1
2D 1H-13C HSQC aromaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
(4,3)D GFT CABCA(CO)NHNNCisotropicsample_conditions_1
(4,3)D GFT HNNCABCANCisotropicsample_conditions_1
(4,3)D GFT HABCAB(CO)NHNNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aliphaticNCisotropicsample_conditions_1
3D HCCH-TOCSY aliphaticNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aromaticNCisotropicsample_conditions_1
3D 1H-15N,13C NOESYNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC 28ms methylNC5isotropicsample_conditions_1
2D 1H-13C CT-HSQC 56ms methylNC5isotropicsample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

PROSA v6.0.2, Guntert - processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

CSI v2.0, Wishart and Sykes - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

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

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure solution

AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

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

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

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA10423 BAK51208 BAL30206 BAL33375 BAL36544
GB AGF52715

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