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BMRB Entry 17775

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PDB ID:
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/BMR17775
MolProbity Validation Chart

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Title: Solution structure of the chimeric Af1503 HAMP- EnvZ DHp homodimer   PubMed: 22244755

Deposition date: 2011-07-10 Original release date: 2011-08-16

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

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).

Assembly members:
HAMP-DHp, polymer, 112 residues, 12738.506 Da.

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

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

Entity Sequences (FASTA):
HAMP-DHp: MSTITRPIIELSNTADKIAE GNLEAEVPHQNRADEIGILA KSIERLRRSLKQLADDRTLL MAGVSHDLRTPLTRIRLATE MMSEQDGYLAESINKDIEEC NAIIEQFIDYLR

Data sets:
Data typeCount
13C chemical shifts456
15N chemical shifts112
1H chemical shifts758

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1HAMP-DHp, chain 11
2HAMP-DHp, chain 21

Entities:

Entity 1, HAMP-DHp, chain 1 112 residues - 12738.506 Da.

The start methionine represents a cloning artifact

1   METSERTHRILETHRARGPROILEILEGLU
2   LEUSERASNTHRALAASPLYSILEALAGLU
3   GLYASNLEUGLUALAGLUVALPROHISGLN
4   ASNARGALAASPGLUILEGLYILELEUALA
5   LYSSERILEGLUARGLEUARGARGSERLEU
6   LYSGLNLEUALAASPASPARGTHRLEULEU
7   METALAGLYVALSERHISASPLEUARGTHR
8   PROLEUTHRARGILEARGLEUALATHRGLU
9   METMETSERGLUGLNASPGLYTYRLEUALA
10   GLUSERILEASNLYSASPILEGLUGLUCYS
11   ASNALAILEILEGLUGLNPHEILEASPTYR
12   LEUARG

Samples:

15N_labeled: HAMP-DHp, [U-100% 15N], 0.6 mM; phosphate buffer 12 mM; sodium chloride 138 mM; H2O 90%; D2O 10%

double_labeled: HAMP-DHp, [U-100% 13C; U-100% 15N], 0.6 mM; phosphate buffer 12 mM; sodium chloride 138 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.150 M; pH: 7.1; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOdouble_labeledisotropicsample_conditions_1
3D HNCAdouble_labeledisotropicsample_conditions_1
3D CBCA(CO)NHdouble_labeledisotropicsample_conditions_1
3D CCH-TOCSYdouble_labeledisotropicsample_conditions_1
3D 1H-15N NOESY15N_labeledisotropicsample_conditions_1
3D NNH NOESY15N_labeledisotropicsample_conditions_1
3D 1H-13C NOESYdouble_labeledisotropicsample_conditions_1
3D CNH NOESYdouble_labeledisotropicsample_conditions_1
3D CCH NOESYdouble_labeledisotropicsample_conditions_1
2D 12C filtered/13C edited NOESYdouble_labeledisotropicsample_conditions_1
2D 12C/14N filtered 1H-1H NOESY15N_labeledisotropicsample_conditions_1
3D HNHA15N_labeledisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - data analysis

X-PLOR NIH v2.21, Goddard - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker AvanceIII 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

UNP P0AEJ4 O28769
BMRB 17776
PDB
GB ESL47213

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