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Biological Magnetic Resonance Data Bank


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BMRB Entry 17856

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17856
MolProbity Validation Chart

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Title: Structural analysis of a chaperone in type III secretion system   PubMed: 22152477

Deposition date: 2011-08-11 Original release date: 2012-01-05

Authors: Chen, L.; Economou, A.; Kalodimos, C.

Citation: Chen, Li; Balabanidou, Vassilia; Remeta, David; Minetti, Conceicao; Portaliou, Athina; Economou, Anastassios; Kalodimos, Charalampos. "Structural instability tuning as a regulatory mechanism in protein-protein interactions"  Mol. Cell 44, 734-744 (2011).

Assembly members:
CesAB_(Type_III_secretion_system,_chaperone_for_EspA_and_EspB,_LEE_associated), polymer, 107 residues, 12320.233 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: purified from natural source   Host organism: Escherichia coli

Entity Sequences (FASTA):
CesAB_(Type_III_secretion_system,_chaperone_for_EspA_and_EspB,_LEE_associated): MSIVSQTRNKELLDKKIRSE IEAIKKIIAEFDVVKESVNE LSEKAKTDPQAAEKLNKLIE GYTYGEERKLYDSALSKIEK LIETLSPARSKSQSTMNQRN RNNRKIV

Data sets:
Data typeCount
13C chemical shifts191
15N chemical shifts94
1H chemical shifts196

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1CesAB (Type III secretion system, chaperone for EspA and EspB, LEE associated)_11
2CesAB (Type III secretion system, chaperone for EspA and EspB, LEE associated)_21

Entities:

Entity 1, CesAB (Type III secretion system, chaperone for EspA and EspB, LEE associated)_1 107 residues - 12320.233 Da.

1   METSERILEVALSERGLNTHRARGASNLYS
2   GLULEULEUASPLYSLYSILEARGSERGLU
3   ILEGLUALAILELYSLYSILEILEALAGLU
4   PHEASPVALVALLYSGLUSERVALASNGLU
5   LEUSERGLULYSALALYSTHRASPPROGLN
6   ALAALAGLULYSLEUASNLYSLEUILEGLU
7   GLYTYRTHRTYRGLYGLUGLUARGLYSLEU
8   TYRASPSERALALEUSERLYSILEGLULYS
9   LEUILEGLUTHRLEUSERPROALAARGSER
10   LYSSERGLNSERTHRMETASNGLNARGASN
11   ARGASNASNARGLYSILEVAL

Samples:

sample: CesAB (Type III secretion system, chaperone for EspA and EspB, LEE associated), [U-13C; U-15N; U-2H], 0.5 – 1.0 mM; phosphate buffer 50 mM; DTT 1 mM; H2O 93%; D2O 7%; KCl 300 mM

sample_conditions_1: ionic strength: 300 mM; pH: 6.5; pressure: 1 Pa; temperature: 299 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsampleisotropicsample_conditions_1
3D HNCOsampleisotropicsample_conditions_1
3D HNCAsampleisotropicsample_conditions_1
2D 1H-13C HSQCsampleisotropicsample_conditions_1
3D C(CO)NHsampleisotropicsample_conditions_1
3D HNCACBsampleisotropicsample_conditions_1
3D HN(CO)CAsampleisotropicsample_conditions_1
3D H(CCO)NHsampleisotropicsample_conditions_1
3D 1H-15N NOESYsampleisotropicsample_conditions_1
3D 1H-13C NOESYsampleisotropicsample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

  • Bruker AVANCE 700 MHz

Related Database Links:

BMRB 18871
PDB
DBJ BAB38009 BAI37555
EMBL CAG17512 CAS11514 CAX18596 CAX18671 CAX18751
GB AAC31531 AAC38366 AAG58850 ACG59648 ACG59706
REF NP_312613 WP_000029556 WP_000029557 WP_000029558 WP_000029559

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