BMRB Entry 17776

Name: Solution structure of the chimeric Af1503 HAMP- EnvZ DHp homodimer; A219F variant
Published: 2011-08-16

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PDB ID: 2lfs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17776
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the chimeric Af1503 HAMP- EnvZ DHp homodimer; A219F variant

Deposition date:

2011-07-10

Original release date:

2011-08-16

Authors:

Coles, Murray; Ferris, Hedda; Hulko, Michael; Martin, Joerg; Lupas, Andrei

Citation:

Citation: Ferris, Hedda; Dunin-Horkawicz, Stanislaw; Hornig, Nora; Hulko, Michael; Martin, Jorg; Schultz, Joachim; Zeth, Kornelius; Lupas, Andrei; Coles, Murray. "Mechanism of regulation of receptor histidine kinases." Structure 20, 56-66 (2012).
PubMed: 22244755

Assembly members:

Assembly members:
HAMP-DHpF, polymer, 112 residues, 12872.684 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET30b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HAMP-DHpF: MSTITRPIIELSNTFDKIAE GNLEAEVPHQNRADEIGILA KSIERLRRSLKQLADDRTLL MAGVSHDLRTPLTRIRLATE MMSEQDGYLAESINKDIEEC NAIIEQFIDYLR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	387
15N chemical shifts	101
1H chemical shifts	627

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HAMP-DHpF, chain 1	1
2	HAMP-DHpF, chain 2	1

Entities:

Entity 1, HAMP-DHpF, chain 1 112 residues - 12872.684 Da.

1

MET

SER

THR

ILE

THR

ARG

PRO

ILE

GLU

2

LEU

SER

ASN

THR

PHE

ASP

LYS

ILE

ALA

GLU

3

GLY

ASN

LEU

GLU

ALA

GLU

VAL

PRO

HIS

GLN

4

ASN

ARG

ALA

ASP

GLU

ILE

GLY

ILE

LEU

ALA

5

LYS

SER

ILE

GLU

ARG

LEU

ARG

SER

LEU

6

LYS

GLN

LEU

ALA

ASP

ARG

THR

LEU

7

MET

ALA

GLY

VAL

SER

HIS

ASP

LEU

ARG

THR

8

PRO

LEU

THR

ARG

ILE

ARG

LEU

ALA

THR

GLU

9

MET

SER

GLU

GLN

ASP

GLY

TYR

LEU

ALA

10

GLU

SER

ILE

ASN

LYS

ASP

ILE

GLU

CYS

11

ASN

ALA

ILE

GLU

GLN

PHE

ILE

ASP

TYR

12

LEU

ARG

Name	Sample	Sample state	Sample conditions
3D HNCO	double_labeled	isotropic	sample_conditions_1
3D HNCA	double_labeled	isotropic	sample_conditions_1
3D CBCA(CO)NH	double_labeled	isotropic	sample_conditions_1
3D CCH-TOCSY	double_labeled	isotropic	sample_conditions_1
3D 1H-15N NOESY	15N_labeled	isotropic	sample_conditions_1
3D NNH NOESY	15N_labeled	isotropic	sample_conditions_1
3D 1H-13C NOESY	double_labeled	isotropic	sample_conditions_1
3D CNH NOESY	double_labeled	isotropic	sample_conditions_1
3D CCH NOESY	double_labeled	isotropic	sample_conditions_1
2D 12C filtered/13C edited NOESY	double_labeled	isotropic	sample_conditions_1
2D 12C/14N filtered 1H-1H NOESY	15N_labeled	isotropic	sample_conditions_1
2D 1H-15N TROSY	15N_labeled	isotropic	sample_conditions_1
2D 1H-15N antiTROSY	15N_labeled	isotropic	sample_conditions_1

BMRB	17775
PDB	2LFR 2LFS 3ZCC 3ZRV 3ZRW 3ZRX 4CTI
GB	ESL47213

BMRB Entry 17776

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links: