BMRB Entry 7226

Title:
Solution NMR Structure of Conserved protein MTH1368, Northeast Structural Genomics Consortium Target TT821A
Deposition date:
2006-07-14
Original release date:
2010-03-04
Authors:
Liu, G.; Lin, Y.; Parish, D.; Shen, Y.; Sukumaran, D.; Yee, A.; Semesi, A.; Arrowsmith, C.; Szyperski, T.
Citation:

Citation: Liu, G.; Lin, Y.; Parish, D.; Shen, Y.; Sukumaran, D.; Yee, A.; Semesi, A.; Arrowsmith, C.; Szyperski, T.. "Solution NMR Structure of Conserved protein MTH1368, Northeast Structural Genomics Consortium Target TT821A"  .

Assembly members:

Assembly members:
Conserved protein MTH1368, polymer, 125 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Methanobacterium thermoautotrophicum   Taxonomy ID: 145262   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanobacterium thermoautotrophicum

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts341
15N chemical shifts106
1H chemical shifts737

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Conserved protein MTH13681

Entities:

Entity 1, Conserved protein MTH1368 125 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYARGGLUASNLEUTYRPHEGLN
3   GLYHISGLNPROASPGLYVALGLNILEASP
4   SERVALVALPROGLYSERPROALASERLYS
5   VALLEUTHRPROGLYLEUVALILEGLUSER
6   ILEASNGLYMETPROTHRSERASNLEUTHR
7   THRTYRSERALAALALEULYSTHRILESER
8   VALGLYGLUVALILEASNILETHRTHRASP
9   GLNGLYTHRPHEHISLEULYSTHRGLYARG
10   ASNPROASNASNSERSERARGALATYRMET
11   GLYILEARGTHRSERASNHISLEUARGVAL
12   ARGASPSERVALALASERVALLEUGLYASP
13   THRLEUPROPHEALA

Samples:

sample_1: Conserved protein MTH1368, [U-15N; U-13C], 0.5 mM; TRIS BUFFER mM; NaCl2 200 mM; ZnSO4 10 uM; NaN3 0.01%; bezamidine 1 mM; inhibitor 1 x; H2O 93%; D2O 7%

sample_cond_1: pH: 7.0; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
SIMULTANEOUS HETERONUCLEAR RESOLVED [1H,1H]-NOESYsample_1not availablesample_cond_1
3D HNCACBsample_1not availablesample_cond_1
3D CBCACONHsample_1not availablesample_cond_1
GFT (4,3)D HABCAB(CO)NHNsample_1not availablesample_cond_1
GFT (4,3)D HCCHsample_1not availablesample_cond_1

Software:

VNMR v6.1C - collection

NMRPipe v2.3 - processing

AutoAssign v1.15.1 - data analysis

AutoStruct v2.0 - data analysis

CYANA v2.1 - structure solution

CNS v1.1 - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAM70490
GB AAB85845
REF NP_276484 WP_010876980

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks