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BMRB Entry 30348

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Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30348
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Title: Solution structure of the N-terminal domain of the effector NleG5-1 from Escherichia coli O157:H7 str. Sakai

Deposition date: 2017-09-22 Original release date: 2017-11-13

Authors: Valleau, D.; Houliston, S.; Lemak, A.; Anderson, W.; Arrowsmith, C.; Savchenko, A.; Center for Structural Genomics of Infectious Diseases (CSGID), CSGID

Citation: Valleau, D.; Savchenko, A.. "Solution structure of the N-terminal domain of the effector NleG5-1 from Escherichia coli O157:H7 str. Sakai"  . ., .-..

Assembly members:
entity_1, polymer, 137 residues, 15676.563 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 83334   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGRENLYFQ GMPVDLTPYILPGVSFLSDI PQETLSEIRNQTIRGEAQIR LGELMVSIRPMQVNGYFMGS LNQDGLSNDNIQIGLQYIEH IERTLNHGSLTSREVTVLRE IEMLENMDLLSNYQLEE

Data sets:
Data typeCount
13C chemical shifts438
15N chemical shifts97
1H chemical shifts717

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 137 residues - 15676.563 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYARGGLUASNLEUTYRPHEGLN
3   GLYMETPROVALASPLEUTHRPROTYRILE
4   LEUPROGLYVALSERPHELEUSERASPILE
5   PROGLNGLUTHRLEUSERGLUILEARGASN
6   GLNTHRILEARGGLYGLUALAGLNILEARG
7   LEUGLYGLULEUMETVALSERILEARGPRO
8   METGLNVALASNGLYTYRPHEMETGLYSER
9   LEUASNGLNASPGLYLEUSERASNASPASN
10   ILEGLNILEGLYLEUGLNTYRILEGLUHIS
11   ILEGLUARGTHRLEUASNHISGLYSERLEU
12   THRSERARGGLUVALTHRVALLEUARGGLU
13   ILEGLUMETLEUGLUASNMETASPLEULEU
14   SERASNTYRGLNLEUGLUGLU

Samples:

sample_1: DTT 10 uM; HEPES 15 mM; L-arginine 5 mM; NleG5-1, [U-100% 13C; U-100% 15N], 400 uM; benzamidine 1 mM; sodium azide 0.01 % w/v; sodium chloride 250 mM; sodium citrate 5 mM

sample_conditions_1: ionic strength: 400 mM; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - peak picking

TOPSPIN, Bruker Biospin - collection

ABACUS, Lemak and Arrowsmith - chemical shift assignment

NMR spectrometers:

  • Bruker AvanceII 800 MHz
  • Bruker Avance 500 MHz

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