BMRB Entry 16821

Title:
SOLUTION NMR STRUCTURE OF TETRATRICOPEPTIDE REPEAT DOMAIN PROTEIN SRU_0103 FROM SALINIBACTER RUBER, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET SRR115C
Deposition date:
2010-04-01
Original release date:
2012-08-03
Authors:
Liu, Gaohua; Rossi, Paolo; Wang, Dongyan; Nwosu, Chioma; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael; SWAPNA, G.V.T; ACTON, THOMAS; Rost, BURKHARD; Montelione, Gaetano
Citation:

Citation: Liu, Gaohua; Montelione, Gaetano. "SOLUTION NMR STRUCTURE OF TETRATRICOPEPTIDE REPEAT DOMAIN PROTEIN SRU_0103 FROM SALINIBACTER RUBER, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET SRR115C"  .

Assembly members:

Assembly members:
SRU_0103, polymer, 198 residues, 22957.064 Da.

Natural source:

Natural source:   Common Name: Salinibacter ruber   Taxonomy ID: 146919   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Salinibacter ruber

Experimental source:

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

Data sets:
Data typeCount
residual dipolar couplings70

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SRU_01031

Entities:

Entity 1, SRU_0103 198 residues - 22957.064 Da.

1   GLUASPPROGLUASPPROPHETHRARGTYR
2   ALALEUALAGLNGLUHISLEULYSHISASP
3   ASNALASERARGALALEUALALEUPHEGLU
4   GLULEUVALGLUTHRASPPROASPTYRVAL
5   GLYTHRTYRTYRHISLEUGLYLYSLEUTYR
6   GLUARGLEUASPARGTHRASPASPALAILE
7   ASPTHRTYRALAGLNGLYILEGLUVALALA
8   ARGGLUGLUGLYTHRGLNLYSASPLEUSER
9   GLULEUGLNASPALALYSLEULYSALAGLU
10   GLYLEUGLUHISHISHISHISHISHISGLU
11   ASPPROGLUASPPROPHETHRARGTYRALA
12   LEUALAGLNGLUHISLEULYSHISASPASN
13   ALASERARGALALEUALALEUPHEGLUGLU
14   LEUVALGLUTHRASPPROASPTYRVALGLY
15   THRTYRTYRHISLEUGLYLYSLEUTYRGLU
16   ARGLEUASPARGTHRASPASPALAILEASP
17   THRTYRALAGLNGLYILEGLUVALALAARG
18   GLUGLUGLYTHRGLNLYSASPLEUSERGLU
19   LEUGLNASPALALYSLEULYSALAGLUGLY
20   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.37 mM; H2O 95%; D2O 5%

sample_2: entity, [U-10% 13C; U-99% 15N], 1.05 mM; H2O 95%; D2O 5%

sample_3: entity, [U-10% 13C; U-99% 15N], 1.09 mM; H2O 95%; D2O 5%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC-TROSYsample_3isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY-aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY-aromaticsample_1isotropicsample_conditions_1
4,3D GFT CABCACONHNsample_1isotropicsample_conditions_1
4,3D GFT HNNCABCAsample_1isotropicsample_conditions_1
4,3D GFT HABCABCONHNsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution

AutoStruct, Huang, Tejero, Powers and Montelione - data analysis, peak picking, refinement

PSVS, Bhattacharya and Montelione - data analysis, peak picking, refinement

XEASY, Bartels et al. - data analysis, peak picking, refinement

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

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16084
PDB