BMRB Entry 6822

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PDB ID: 2l7h
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR6822
MolProbity Validation Chart

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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 Structure of the Hamp Domain Implies a Rotational Mechanism in Transmembrane Signalling

Deposition date:

2005-09-09

Original release date:

2006-10-19

Authors:

Coles, M.; Truffault, V.; Hulko, M.; Martin, J.; Lupas, A.

Citation:

Citation: Hulko, M.; Berndt, F.; Gruber, M.; Linder, J.; Truffault, V.; Schultz, A.; Martin, J.; Schultz, J.; Lupas, A.; Coles, M.. "The HAMP domain structure implies helix rotation in transmembrane signaling" Cell 126, 929-940 (2006).
PubMed: 16959572

Assembly members:

Assembly members:
hypothetical protein AF1503, polymer, 56 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Archaeoglobus fulgidus Taxonomy ID: 2234 Superkingdom: Archaea Kingdom: not available Genus/species: Archaeoglobus fulgidus

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hypothetical protein AF1503: GSSTITRPIIELSNTADKIA EGNLEAEVPHQNRADEIGIL AKSIERLRRSLKVAME

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
13C chemical shifts	229
15N chemical shifts	55
1H chemical shifts	397

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hypothetical protein AF1503 chain A	1
2	hypothetical protein AF1503 chain B	1

Entities:

Entity 1, hypothetical protein AF1503 chain A 56 residues - Formula weight is not available

1

GLY

SER

THR

ILE

THR

ARG

PRO

ILE

2

GLU

LEU

SER

ASN

THR

ALA

ASP

LYS

ILE

ALA

3

GLU

GLY

ASN

LEU

GLU

ALA

GLU

VAL

PRO

HIS

4

GLN

ASN

ARG

ALA

ASP

GLU

ILE

GLY

ILE

LEU

5

ALA

LYS

SER

ILE

GLU

ARG

LEU

ARG

SER

6

LEU

LYS

VAL

ALA

MET

GLU

Samples:

sample_1: hypothetical protein AF1503 1.0 mM; phosphate buffer 20 mM; NACL 150 mM; H2O 90%; D2O 10%

sample_2: hypothetical protein AF1503, [U-15N], 1.0 mM; phosphate buffer 20 mM; NACL 150 mM; H2O 90%; D2O 10%

sample_3: hypothetical protein AF1503, [U-13C; U-15N], 1.0 mM; phosphate buffer 20 mM; NACL 150 mM; H2O 90%; D2O 10%

sample_cond_1: ionic strength: 150 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	not available	not available	not available
2D NOESY	not available	not available	not available
HNHA	not available	not available	not available
2D 12C-FILTERED/13C-EDITED NOESY	not available	not available	not available
3D-NNH-NOESY	not available	not available	not available
3D-CNH-NOESY	not available	not available	not available

Software:

X-PLOR vNIH-2.9.7 - refinement, structure solution

xwinnmr v3.5 - processing

SPARKY v3.110 - data analysis

NMR spectrometers:

Bruker DMX 900 MHz

BMRB	17775 17776
PDB	2ASW 2ASX 2L7H 2L7I 2LFR 2Y0Q 2Y0T 2Y20 2Y21 3ZCC 3ZRV 3ZRW 3ZRX 3ZX6 4CQ4 4CTI 4GN0
GB	AAB89755 AIG98513
REF	NP_070332 WP_010879000