BMRB Entry 30326

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30326
MolProbity Validation Chart

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Title:
NMR solution structure of Enzyme I (nEIt) protein using two 4D-spectra
Deposition date:
2017-08-03
Original release date:
2018-01-29
Authors:
Evangelidis, T.; Nerli, S.; Sgourakis, N.; Tripsianes, K.
Citation:

Citation: Evangelidis, T.; Nerli, S.; Novacek, J.; Brereton, A.; Karplus, P.; Dotas, R.; Venditti, V.; Sgourakis, N.; Tripsianes, K.. "Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra"  Nat. Commun. 9, 384-384 (2018).
PubMed: 29374165

Assembly members:

Assembly members:
entity_1, polymer, 248 residues, 27297.273 Da.

Natural source:

Natural source:   Common Name: Caldanaerobacter subterraneus   Taxonomy ID: 273068   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Caldanaerobacter subterraneus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MLKGVAASPGIAIGKAFLYT KEKVTINVEKIEESKVEEEI AKFRKALEVTQEEIEKIKEK ALKEFGKEKAEIFEAHLMLA SDPELIEGVENMIKTELVTA DNAVNKVIEQNASVMESLND EYLKERAVDLRDVGNRIIEN LLGVKSVNLSDLEEEVVVIA RDLTPSDTATMKKEMVLGFA TDVGGRTSHTAIMARSLEIP AVVGLGNVTSQVKAGDLVIV DGLEGIVIVNPDEKTVEDYK SKKESYEK

Data sets:
Data typeCount
13C chemical shifts800
15N chemical shifts240
1H chemical shifts1699

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 248 residues - 27297.273 Da.

1   METLEULYSGLYVALALAALASERPROGLY
2   ILEALAILEGLYLYSALAPHELEUTYRTHR
3   LYSGLULYSVALTHRILEASNVALGLULYS
4   ILEGLUGLUSERLYSVALGLUGLUGLUILE
5   ALALYSPHEARGLYSALALEUGLUVALTHR
6   GLNGLUGLUILEGLULYSILELYSGLULYS
7   ALALEULYSGLUPHEGLYLYSGLULYSALA
8   GLUILEPHEGLUALAHISLEUMETLEUALA
9   SERASPPROGLULEUILEGLUGLYVALGLU
10   ASNMETILELYSTHRGLULEUVALTHRALA
11   ASPASNALAVALASNLYSVALILEGLUGLN
12   ASNALASERVALMETGLUSERLEUASNASP
13   GLUTYRLEULYSGLUARGALAVALASPLEU
14   ARGASPVALGLYASNARGILEILEGLUASN
15   LEULEUGLYVALLYSSERVALASNLEUSER
16   ASPLEUGLUGLUGLUVALVALVALILEALA
17   ARGASPLEUTHRPROSERASPTHRALATHR
18   METLYSLYSGLUMETVALLEUGLYPHEALA
19   THRASPVALGLYGLYARGTHRSERHISTHR
20   ALAILEMETALAARGSERLEUGLUILEPRO
21   ALAVALVALGLYLEUGLYASNVALTHRSER
22   GLNVALLYSALAGLYASPLEUVALILEVAL
23   ASPGLYLEUGLUGLYILEVALILEVALASN
24   PROASPGLULYSTHRVALGLUASPTYRLYS
25   SERLYSLYSGLUSERTYRGLULYS

Samples:

sample_1: Enzyme I (nEIt) protein, [U-13C; U-15N], 1.8 mM; sodium phosphate 20 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
4D HC(CC TOCSY(CO))NHsample_1isotropicsample_conditions_1
4D 13C,15N edited HMQC-NOESY-HSQCsample_1isotropicsample_conditions_1
4D 13C,13C edited HMQC-NOESY-HSQCsample_1isotropicsample_conditions_1

Software:

CS-Rosetta, Shen, Vernon, Baker and Bax - data analysis, refinement, structure calculation

SPARKY, Goddard - peak picking

4D-CHAINS, Evangelidis and Tripsianes - chemical shift assignment

NMR spectrometers:

  • Bruker AvanceIII 850 MHz

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