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 11031

Title: The solution structure of phtotactic transducer protein HtrII linker region from Natronomonas pharaonis   PubMed: 18001143

Deposition date: 2008-02-20 Original release date: 2008-03-31

Authors: Hayashi, Kokoro; Sudo, Yuki; Jee, JunGoo; Mishima, Masaki; Hara, Hideyuki; Kamo, Naoki; Kojima, Chojiro

Citation: Hayashi, Kokoro; Sudo, Yuki; Jee, JunGoo; Mishima, Masaki; Hara, Hideyuki; Kamo, Naoki; Kojima, Chojiro. "Structural Analysis of the Phototactic Transducer Protein HtrII Linker Region from Natoronomonas pharaonis"  Biochemistry 46, 14380-14390 (2007).

Assembly members:
pHtrII(100-159), polymer, 68 residues, 7953.576 Da.

Natural source:   Common Name: Natronomonas pharaonis   Taxonomy ID: 2257   Superkingdom: Archaea   Kingdom: not available   Genus/species: Natronomonas pharaonis

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Entity Sequences (FASTA):
pHtrII(100-159): MGDGDLDVELETRREDEIGD LYAAFDEMRQSVRTSLEDAK NAREDAEQAQKRAEEINTEL LEHHHHHH

Data sets:
Data typeCount
13C chemical shifts243
15N chemical shifts66
1H chemical shifts389

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1pHtrII(100-159)1

Entities:

Entity 1, pHtrII(100-159) 68 residues - 7953.576 Da.

Residues 160-167 represents a non-native affinity tag.

1   METGLYASPGLYASPLEUASPVALGLULEU
2   GLUTHRARGARGGLUASPGLUILEGLYASP
3   LEUTYRALAALAPHEASPGLUMETARGGLN
4   SERVALARGTHRSERLEUGLUASPALALYS
5   ASNALAARGGLUASPALAGLUGLNALAGLN
6   LYSARGALAGLUGLUILEASNTHRGLULEU
7   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: pHtrII(100-159), [U-100% 13C; U-100% 15N], 0.6 – 0.8 mM; citric acid 10 mM; potassium chloride 50 mM; H2O 90%; D2O 10%

sample_2: pHtrII(100-159), [U-100% 15N], 0.8 mM; potassium phosphate 50 mM; potassium chloride 50 mM; H2O 90%; D2O 10%

sample_3: pHtrII(100-159), [U-100% 15N], 0.8 mM; citric acid 10 mM; potassium chloride 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.05 M; pH: 5.0; pressure: 1 atm; temperature: 277 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D H(CACO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution

AMBER v9.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker DRX 800 MHz

Related Database Links:

PDB
EMBL CAA84468 CAI50507
REF WP_049939883
SP P42259
AlphaFold P42259

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