BMRB Entry 11031

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11031

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

The solution structure of phtotactic transducer protein HtrII linker region from Natronomonas pharaonis

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:

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).
PubMed: 18001143

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	243
15N chemical shifts	66
1H chemical shifts	389

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	pHtrII(100-159)	1

Entities:

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

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

1

MET

GLY

ASP

GLY

ASP

LEU

ASP

VAL

GLU

LEU

2

GLU

THR

ARG

GLU

ASP

GLU

ILE

GLY

ASP

3

LEU

TYR

ALA

PHE

ASP

GLU

MET

ARG

GLN

4

SER

VAL

ARG

THR

SER

LEU

GLU

ASP

ALA

LYS

5

ASN

ALA

ARG

GLU

ASP

ALA

GLU

GLN

ALA

GLN

6

LYS

ARG

ALA

GLU

ILE

ASN

THR

GLU

LEU

7

LEU

GLU

HIS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D H(CACO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_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

PDB	2RM8 4GYC
EMBL	CAA84468 CAI50507
REF	WP_049939883
SP	P42259
AlphaFold	P42259