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 16084

Title: SOLUTION STRUCTURE OF TETRATRICOPEPTIDE REPEAT DOMAIN PROTEIN SRU_0103 FROM SALINIBACTER RUBER, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET SrR115C

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: 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. "SOLUTION STRUCTURE OF TETRATRICOPEPTIDE REPEAT DOMAIN PROTEIN SRU_0103 FROM SALINIBACTER RUBER, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET SrR115C"  Not known ., .-..

Assembly members:
SRU_0103, polymer, 99 residues, 11487.540 Da.

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

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

Entity Sequences (FASTA):
SRU_0103: EDPEDPFTRYALAQEHLKHD NASRALALFEELVETDPDYV GTYYHLGKLYERLDRTDDAI DTYAQGIEVAREEGTQKDLS ELQDAKLKAEGLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts310
15N chemical shifts99
1H chemical shifts655

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SRU_01031

Entities:

Entity 1, SRU_0103 99 residues - 11487.540 Da.

1   GLUASPPROGLUASPPROPHETHRARGTYR
2   ALALEUALAGLNGLUHISLEULYSHISASP
3   ASNALASERARGALALEUALALEUPHEGLU
4   GLULEUVALGLUTHRASPPROASPTYRVAL
5   GLYTHRTYRTYRHISLEUGLYLYSLEUTYR
6   GLUARGLEUASPARGTHRASPASPALAILE
7   ASPTHRTYRALAGLNGLYILEGLUVALALA
8   ARGGLUGLUGLYTHRGLNLYSASPLEUSER
9   GLULEUGLNASPALALYSLEULYSALAGLU
10   GLYLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: SRU_0103, [U-100% 13C; U-100% 15N], 1.37 mM

sample_2: SRU_0103, [U-10% 13C; U-100% 15N], 1.05 mM

sample_conditions_1: ionic strength: . M; 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
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY (aliph)sample_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-13C HSQCsample_2isotropicsample_conditions_1
3D 1H-13C NOESY (arom)sample_1isotropicsample_conditions_1

Software:

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

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

AutoStruct, Huang, Tejero, Powers and Montelione - data analysis, refinement, structure solution

PSVS, Bhattacharya and Montelione - data analysis, refinement

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

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

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

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16821
PDB
EMBL CBH23027
GB ABC44923
REF WP_011402889 WP_043551686 YP_444256