BMRB Entry 6256

Title:
Chemical Shift Assignments of TM1509
Deposition date:
2004-06-29
Original release date:
2005-08-22
Authors:
Herve du Penhoat, Catherine; Atreya, Hanudatta; Kim, Seho; Yee, Adelinda; Xiao, Rong; Arrowsmith, Cheryl; Szyperski, Thomas
Citation:

Citation: Herve du Penhoat, Catherine; Li, Zhaohui; Atreya, Hanudatta; Kim, Seho; Yee, Adelinda; Xiao, Rong; Murray, Diana; Arrowsmith, Cheryl; Szyperski, Thomas. "NMR solution structure of Thermotoga maritima protein TM1509 reveals a Zn-metalloprotease-like tertiary structure "  J. Struct. Funct. Genomics 6, 51-62 (2005).

Assembly members:

Assembly members:
TM1509, polymer, 150 residues, 17549.8 Da.

Natural source:

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

Experimental source:   Production method: recombinant technology

Experimental source:

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

Experimental source:   Production method: recombinant technology

Data sets:
Data typeCount
1H chemical shifts1050
13C chemical shifts624
15N chemical shifts154

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TM15091

Entities:

Entity 1, TM1509 150 residues - 17549.8 Da.

1   METILEARGILELEUGLYGLUGLYLYSGLY
2   SERLYSLEULEUGLUASNLEULYSGLULYS
3   LEUGLUGLUILEVALLYSLYSGLUILEGLY
4   ASPVALHISVALASNVALILELEUVALSER
5   GLUASPGLUILELYSGLULEUASNGLNGLN
6   PHEARGGLYGLNASPARGPROTHRASPVAL
7   LEUTHRPHEPROLEUMETGLUGLUASPVAL
8   TYRGLYGLUILETYRVALCYSPROLEUILE
9   VALGLUGLUASNALAARGGLUPHEASNASN
10   THRPHEGLULYSGLULEULEUGLUVALVAL
11   ILEHISGLYILELEUHISLEUALAGLYTYR
12   ASPHISGLUPHEGLUASPLYSASNSERLYS
13   GLUMETPHEGLULYSGLNLYSLYSTYRVAL
14   GLUGLUVALTRPGLYGLUTRPARGSERASN
15   PROSERGLUASPSERASPPROGLYLYSARG

Samples:

Sample_1: TM1509, [U-100% 13C; U-100% 15N], 1.0 mM; NaCl 450 mM; NaHPO4 25 mM; DTT 10 mM; NaN3 0.01%; benzamidine 1 mM; inhibitor cocktail pill 1 mM

Sample_2: TM1509, [U-100% 15N; biosynthetically-directed 5% fractionally-labeled 13C], 1.23 mM; NaCl 450 mM; NaHPO4 25 mM; DTT 10 mM; NaN3 0.01%; benzamidine 1 mM; inhibitor cocktail pill 1 mM

all_conditions: pH: 6.5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
gNhsqcnot availablenot availablenot available
CT-gChsqcnot availablenot availablenot available
HNCOnot availablenot availablenot available
HNCACBnot availablenot availablenot available
CBCAcoNHnot availablenot availablenot available
HNcaHAnot availablenot availablenot available
HCCHCOSY [13C,1H,1H]not availablenot availablenot available
HCCHTOCSY [13C,13C,1H]not availablenot availablenot available
13C-resolved aliphatic NOESYnot availablenot availablenot available
13C-resolved aromatic NOESYnot availablenot availablenot available
15N-resolved NOESYnot availablenot availablenot available

Software:

No software information available

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
GB AAD36576 ACB09747 AGL50441 AHD18596 AIY86860
REF NP_229309 WP_004081854 WP_008194976 WP_012311098 YP_001739430
SP B1LBP9 Q9X1J7
AlphaFold Q9X1J7

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