BMRB

Biological Magnetic Resonance Data Bank


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BMRB Entry 4796

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4796

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Title: Solution structure of hypothetical protein MTH1175 from Methanobacterium thermoautotrophicum

Deposition date: 2000-07-26 Original release date: 2002-01-23

Authors: Cort, J.; Yee, A.; Edwards, A.; Arrowsmith, C.; Kennedy, M.

Citation: Cort, J.; Yee, A.; Edwards, A.; Arrowsmith, C.; Kennedy, M.. "NMR Structure Determination and Structure-Based Functional Classification of Conserved Hypothetical Protein MTH1175 from Methanobacterium thermoautotrophicum"  J. Struct. Funct. Gen. 1, 15-25 (2000).

Assembly members:
HYPOTHETICAL PROTEIN MTH1175, polymer, 144 residues, 15323 Da.

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

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

Entity Sequences (FASTA):
HYPOTHETICAL PROTEIN MTH1175: MGSSHHHHHHSSGLVPRGSH MKIAIASSGTDLGSEVSRFF GRAPYFMIVEMKKGNIESSE VIENPSASASGGAGIRTAQI IANNGVKAVIASSPGPNAFE VLNELGIKIYRATGTSVEEN LKLFTEGNLEEIRSPGSGRG RRRR

Data sets:
Data typeCount
1H chemical shifts634
13C chemical shifts435
15N chemical shifts122

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MTH11751

Entities:

Entity 1, MTH1175 144 residues - 15323 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METLYSILEALAILEALASERSERGLYTHR
4   ASPLEUGLYSERGLUVALSERARGPHEPHE
5   GLYARGALAPROTYRPHEMETILEVALGLU
6   METLYSLYSGLYASNILEGLUSERSERGLU
7   VALILEGLUASNPROSERALASERALASER
8   GLYGLYALAGLYILEARGTHRALAGLNILE
9   ILEALAASNASNGLYVALLYSALAVALILE
10   ALASERSERPROGLYPROASNALAPHEGLU
11   VALLEUASNGLULEUGLYILELYSILETYR
12   ARGALATHRGLYTHRSERVALGLUGLUASN
13   LEULYSLEUPHETHRGLUGLYASNLEUGLU
14   GLUILEARGSERPROGLYSERGLYARGGLY
15   ARGARGARGARG

Samples:

sample_1: HYPOTHETICAL PROTEIN MTH1175, [U-13C; U-15N], 1.5 – 2.0 mM; NaCl 150 mM; phosphate buffer 25 mM

sample_2: HYPOTHETICAL PROTEIN MTH1175, [U-15N], 1.5 – 2.0 mM; NaCl 150 mM; phosphate buffer 25 mM

sample_cond_1: pH: 6.5 n.a; temperature: 298 K; ionic strength: 150 mM

Experiments:

NameSampleSample stateSample conditions
4D 13C-separated_NOESYnot availablenot availablesample_cond_1
3D 15N-separated_NOESYnot availablenot availablesample_cond_1
HNHAnot availablenot availablesample_cond_1
3D 13C,15N-simultaneous NOESYnot availablenot availablesample_cond_1
1H-15N HSQC D2O exchangenot availablenot availablesample_cond_1
HNCOnot availablenot availablesample_cond_1
HNCACBnot availablenot availablesample_cond_1
CBCACONNHnot availablenot availablesample_cond_1
CBCACOCAHAnot availablenot availablesample_cond_1
HCCH-TOCSYnot availablenot availablesample_cond_1
HCC-TOCSY-NNHnot availablenot availablesample_cond_1
CCC-TOCSY-NNHnot availablenot availablesample_cond_1

Software:

X-PLOR v3.1 - refinement, structure solution

FELIX v98 - processing

VNMR - collection

NMR spectrometers:

  • Varian Inova 600 MHz
  • Varian Unity Plus 500 MHz
  • Varian Inova 750 MHz

Related Database Links:

PDB
GB AAB85664
REF NP_276303 WP_010876799

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