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 16366

Title: Solution NMR structure of Themotoga maritima protein TM1076: Northeast Structural Genomics Consortium target VT57

Deposition date: 2009-06-26 Original release date: 2012-08-03

Authors: Cort, John; Yee, Adelinda; Garcia, Maite; Isern, Nancy; Arrowsmith, Cheryl; Kennedy, Michael

Citation: Cort, John; Yee, Adelinda; Garcia, Maite; Isern, Nancy; Arrowsmith, Cheryl; Kennedy, Michael. "solution NMR structure of Themotoga maritima protein TM1076"  Not known ., .-..

Assembly members:
TM1076, polymer, 314 residues, 17614.3 Da.

Natural source:   Common Name: Thermotoga maritima   Taxonomy ID: 2336   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermotoga maritima

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

Entity Sequences (FASTA):
TM1076: VKRFLLISDSHVPVRMASLP DEILNSLKEYDGVIGLGDYV DLDTVILLEKFSKEFYGVHG NMDYPDVKEHLPFSKVLLVE GVTIGMCHGWGAPWDLKDRL LKVFNEKPQVILFGHTHEPE DTVKAGVRFLNPGSLAEGSY AVLELDGGEVRFELKTLVKR FLLISDSHVPVRMASLPDEI LNSLKEYDGVIGLGDYVDLD TVILLEKFSKEFYGVHGNMD YPDVKEHLPFSKVLLVEGVT IGMCHGWGAPWDLKDRLLKV FNEKPQVILFGHTHEPEDTV KAGVRFLNPGSLAEGSYAVL ELDGGEVRFELKTL

Data sets:
Data typeCount
13C chemical shifts621
15N chemical shifts133
1H chemical shifts991

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TM10761

Entities:

Entity 1, TM1076 314 residues - 17614.3 Da.

The protein construct used in the study contains a N-terminal His tag sequence MGSSHHHHHHSSGRENLYFQG before the sequence beginning with Val1 for which coordinates have been submitted

1   VALLYSARGPHELEULEUILESERASPSER
2   HISVALPROVALARGMETALASERLEUPRO
3   ASPGLUILELEUASNSERLEULYSGLUTYR
4   ASPGLYVALILEGLYLEUGLYASPTYRVAL
5   ASPLEUASPTHRVALILELEULEUGLULYS
6   PHESERLYSGLUPHETYRGLYVALHISGLY
7   ASNMETASPTYRPROASPVALLYSGLUHIS
8   LEUPROPHESERLYSVALLEULEUVALGLU
9   GLYVALTHRILEGLYMETCYSHISGLYTRP
10   GLYALAPROTRPASPLEULYSASPARGLEU
11   LEULYSVALPHEASNGLULYSPROGLNVAL
12   ILELEUPHEGLYHISTHRHISGLUPROGLU
13   ASPTHRVALLYSALAGLYVALARGPHELEU
14   ASNPROGLYSERLEUALAGLUGLYSERTYR
15   ALAVALLEUGLULEUASPGLYGLYGLUVAL
16   ARGPHEGLULEULYSTHRLEUVALLYSARG
17   PHELEULEUILESERASPSERHISVALPRO
18   VALARGMETALASERLEUPROASPGLUILE
19   LEUASNSERLEULYSGLUTYRASPGLYVAL
20   ILEGLYLEUGLYASPTYRVALASPLEUASP
21   THRVALILELEULEUGLULYSPHESERLYS
22   GLUPHETYRGLYVALHISGLYASNMETASP
23   TYRPROASPVALLYSGLUHISLEUPROPHE
24   SERLYSVALLEULEUVALGLUGLYVALTHR
25   ILEGLYMETCYSHISGLYTRPGLYALAPRO
26   TRPASPLEULYSASPARGLEULEULYSVAL
27   PHEASNGLULYSPROGLNVALILELEUPHE
28   GLYHISTHRHISGLUPROGLUASPTHRVAL
29   LYSALAGLYVALARGPHELEUASNPROGLY
30   SERLEUALAGLUGLYSERTYRALAVALLEU
31   GLULEUASPGLYGLYGLUVALARGPHEGLU
32   LEULYSTHRLEU

Samples:

sample_3: TM1076, [U-99% 15N, 7% 13C, biosynthetically directed labeling of LV methyls], 0.6 mM; sodium chloride 300 mM; DTT 10 mM; benzamidine 1 mM; sodium azide 0.01%; H2O 93%; D2O 7%

sample_1: TM1076, [U-99% 13C; U-99% 15N], 0.6 mM; sodium chloride 300 mM; DTT 10 mM; benzamidine 1 mM; sodium azide 0.01%; H2O 93%; D2O 7%

sample_2: TM1076, [U-99% 13C; U-99% 15N], 0.6 mM; sodium chloride 300 mM; DTT 10 mM; benzamidine 1 mM; sodium azide 0.01%; D2O 100%

sample_conditions_1: ionic strength: 300 M; pH: 7; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
4D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

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

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

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

PSVS, Bhattacharya and Montelione - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
GB AAD36153 ABQ47673 ACB10074 AGL50004 AHD19016
REF NP_228882 WP_008195716 WP_010865261

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts