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 17010

Title: Backbone Amide relaxation parameters for wild-type Tryptophan Repressor   PubMed: 20718459

Authors: Goel, Anupam

Citation: Goel, Anupam; Tripet, Brian; Tyler, Robert; Nebert, Lucas; Copie, Valerie. "Backbone Amide Dynamics Studies of Apo-L75F-TrpR, a Temperature-Sensitive Mutant of the Tryptophan Repressor Protein (TrpR): Comparison with the (15)N NMR Relaxation Profiles of Wild-Type and A77V Mutant Apo-TrpR Repressors."  Biochemistry 49, 8006-8019 (2010).

Assembly members:
apo-TrpR, polymer, 108 residues, 12355.1 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
apo-TrpR: MAQQSPYSAAMAEQRHQEWL RFVDLLKNAYQNDLHLPLLN LMLTPDEREALGTRVRIVEE LLRGEMSQRELKNELGAGIA TITRGSNSLKAAPVELRQWL EEVLLKSD

Data sets:
Data typeCount
13C chemical shifts158
15N chemical shifts85
1H chemical shifts85
heteronuclear NOE values72
order parameters61
spectral density values62
T1 relaxation values72
T2 relaxation values72

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Tryptophan apo-repressor, chain 11
2Tryptophan apo-repressor, chain 21

Entities:

Entity 1, Tryptophan apo-repressor, chain 1 108 residues - 12355.1 Da.

sample studied as a homodimer. sequence provided is for one protomer.

1   METALAGLNGLNSERPROTYRSERALAALA
2   METALAGLUGLNARGHISGLNGLUTRPLEU
3   ARGPHEVALASPLEULEULYSASNALATYR
4   GLNASNASPLEUHISLEUPROLEULEUASN
5   LEUMETLEUTHRPROASPGLUARGGLUALA
6   LEUGLYTHRARGVALARGILEVALGLUGLU
7   LEULEUARGGLYGLUMETSERGLNARGGLU
8   LEULYSASNGLULEUGLYALAGLYILEALA
9   THRILETHRARGGLYSERASNSERLEULYS
10   ALAALAPROVALGLULEUARGGLNTRPLEU
11   GLUGLUVALLEULEULYSSERASP

Samples:

sample_1: H2O 95%; D2O, [U-100% 2H], 5%; PMSF 0.1 mM; sodium phosphate 50 mM; sodium azide 0.01%; sodium chloride 500 mM; EDTA 1 mM; apo-WT-TrpR, [U-100% 13C; U-100% 15N], 1 mM

sample_conditions_1: ionic strength: 1 M; pH: 5.7; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
3D HNCACBsample_1anisotropicsample_conditions_1
3D CBCA(CO)NHsample_1anisotropicsample_conditions_1
3D HNCAsample_1anisotropicsample_conditions_1
2D 15N T1sample_1anisotropicsample_conditions_1
2D 15N T2 interleavedsample_1anisotropicsample_conditions_1
2D 15N {1H} nOesample_1anisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

ModelFree, Palmer - data analysis, geometry optimization, refinement

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 17012 17013 17041 17046 17047 2040 2042 2043 2074 2173 2209 2764 441 442
PDB
DBJ BAB38774 BAE78382 BAG80193 BAI28718 BAI33927
EMBL CAP78881 CAQ34751 CAQ91905 CAR01357 CAR06215
GB AAA72134 AAA72140 AAA97289 AAC77346 AAG59573
REF NP_313378 NP_418810 NP_710132 WP_000068670 WP_000068671
SP A1AJW2 A7ZVT5 A8A8C2 B1IS26 B1LEK0