BMRB Entry 18978

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PDB ID: 2m3x
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18978
MolProbity Validation Chart

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Title:
Solution structure of Ph1500: a homohexameric protein centered on a 12-bladed beta-propeller
Deposition date:
2013-01-28
Original release date:
2013-03-01
Authors:
Varnay, Ilka; Truffault, Vincent; Kessler, Horst; Coles, Murray
Citation:

Citation: Varnay, Ilka; Truffault, Vincent; Djuranovic, Sergej; Ursinus, Astrid; Coles, Murray; Kessler, Horst. "Optimized measurement temperature gives access to the solution structure of a 49 kDa homohexameric -propeller."  J. Am. Chem. Soc. 132, 15692-15698 (2010).
PubMed: 20961124

Assembly members:

Assembly members:
Ph1500, polymer, 147 residues, 16728.898 Da.
Ph1500N, polymer, 83 residues, 16728.898 Da.
Ph1500C, polymer, 78 residues, 16728.898 Da.

Natural source:

Natural source:   Common Name: Euryarchaeotes   Taxonomy ID: 53953   Superkingdom: Archaea   Kingdom: not available   Genus/species: Pyrococcus horikoshii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ph1500: EGVIMSELKLKPLPKVELPP DFVDVIRIKLQGKTVRTGDV IGISILGKEVKFKVVQAYPS PLRVEDRTKITLVTHPVDVL EAKIKGIKDVILDENLIVVI TEENEVLIFNQNLEELYRGK FENLNKVLVRNDLVVIIDEQ KLTLIRT
Ph1500N: MHHHHHHEGVIMSELKLKPL PKVELPPDFVDVIRIKLQGK TVRTGDVIGISILGKEVKFK VVQAYPSPLRVEDRTKITLV THP
Ph1500C: MHHHHHHVDVLEAKIKGIKD VILDENLIVVITEENEVLIF NQNLEELYRGKFENLNKVLV RNDLVVIIDEQKLTLIRT

Data sets:
Data typeCount
13C chemical shifts674
15N chemical shifts131
1H chemical shifts1125

Additional metadata:

  • Assembly
  • Samples and Experiments
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  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Ph1500_11
2Ph1500_21
3Ph1500_31
4Ph1500_41
5Ph1500_51
6Ph1500_61
7Ph1500N2
8Ph1500C3

Entities:

Entity 1, Ph1500_1 147 residues - 16728.898 Da.

The first four residues are an artefact of an incorrectly annotated start methionine. Residue numbering refers to the correct start

1   GLUGLYVALILEMETSERGLULEULYSLEU
2   LYSPROLEUPROLYSVALGLULEUPROPRO
3   ASPPHEVALASPVALILEARGILELYSLEU
4   GLNGLYLYSTHRVALARGTHRGLYASPVAL
5   ILEGLYILESERILELEUGLYLYSGLUVAL
6   LYSPHELYSVALVALGLNALATYRPROSER
7   PROLEUARGVALGLUASPARGTHRLYSILE
8   THRLEUVALTHRHISPROVALASPVALLEU
9   GLUALALYSILELYSGLYILELYSASPVAL
10   ILELEUASPGLUASNLEUILEVALVALILE
11   THRGLUGLUASNGLUVALLEUILEPHEASN
12   GLNASNLEUGLUGLULEUTYRARGGLYLYS
13   PHEGLUASNLEUASNLYSVALLEUVALARG
14   ASNASPLEUVALVALILEILEASPGLUGLN
15   LYSLEUTHRLEUILEARGTHR

Entity 2, Ph1500N 83 residues - 16728.898 Da.

The first seven residues are a purification tag. The next four residues are an artefact of an incorrectly annotated start methionine.

1   METHISHISHISHISHISHISGLUGLYVAL
2   ILEMETSERGLULEULYSLEULYSPROLEU
3   PROLYSVALGLULEUPROPROASPPHEVAL
4   ASPVALILEARGILELYSLEUGLNGLYLYS
5   THRVALARGTHRGLYASPVALILEGLYILE
6   SERILELEUGLYLYSGLUVALLYSPHELYS
7   VALVALGLNALATYRPROSERPROLEUARG
8   VALGLUASPARGTHRLYSILETHRLEUVAL
9   THRHISPRO

Entity 3, Ph1500C 78 residues - 16728.898 Da.

The first seven residues are a purification tag

1   METHISHISHISHISHISHISVALASPVAL
2   LEUGLUALALYSILELYSGLYILELYSASP
3   VALILELEUASPGLUASNLEUILEVALVAL
4   ILETHRGLUGLUASNGLUVALLEUILEPHE
5   ASNGLNASNLEUGLUGLULEUTYRARGGLY
6   LYSPHEGLUASNLEUASNLYSVALLEUVAL
7   ARGASNASPLEUVALVALILEILEASPGLU
8   GLNLYSLEUTHRLEUILEARGTHR

Related Database Links:

UNP O59169 O59169
AlphaFold O59169 O59169 O59169

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