BMRB Entry 15507

Title:
Chemical Shift Assignments for Legionella pneumophila Mip bound to rapamycin
Deposition date:
2007-10-04
Original release date:
2008-06-26
Authors:
Ceymann, Andreas; Horstmann, Martin; Ehses, Philipp; Schweimer, Kristian; Faber, Cornelius
Citation:

Citation: Ceymann, Andreas; Horstmann, Martin; Ehses, Philipp; Schweimer, Kristian; Paschke, Anne-Katrin; Steinert, Michael; Faber, Cornelius. "Solution structure of the Legionella pneumophila Mip-rapamycin complex"  BMC Struct. Biol. 8, .-. (2008).
PubMed: 18366641

Assembly members:

Assembly members:
Mip_protein, polymer, 137 residues, 14650.7 Da.
RAPAMYCIN IMMUNOSUPPRESSANT DRUG, non-polymer, 914.172 Da.

Natural source:

Natural source:   Common Name: Legionella pneumophila   Taxonomy ID: 446   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Legionella pneumophila

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: vector pBC KS(+)

Data sets:
Data typeCount
1H chemical shifts884
13C chemical shifts581
15N chemical shifts137

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Mip1
2Rapamycin2

Entities:

Entity 1, Mip 137 residues - 14650.7 Da.

Only the C-terminal FKBP domain of Mip was under investigation (residue 77-213)

1   PHEASNLYSLYSALAASPGLUASNLYSVAL
2   LYSGLYGLUALAPHELEUTHRGLUASNLYS
3   ASNLYSPROGLYVALVALVALLEUPROSER
4   GLYLEUGLNTYRLYSVALILEASNSERGLY
5   ASNGLYVALLYSPROGLYLYSSERASPTHR
6   VALTHRVALGLUTYRTHRGLYARGLEUILE
7   ASPGLYTHRVALPHEASPSERTHRGLULYS
8   THRGLYLYSPROALATHRPHEGLNVALSER
9   GLNVALILEPROGLYTRPTHRGLUALALEU
10   GLNLEUMETPROALAGLYSERTHRTRPGLU
11   ILETYRVALPROSERGLYLEUALATYRGLY
12   PROARGSERVALGLYGLYPROILEGLYPRO
13   ASNGLUTHRLEUILEPHELYSILEHISLEU
14   ILESERVALLYSLYSSERSER

Entity 2, Rapamycin - C51 H79 N O13 - 914.172 Da.

1   RAP

Samples:

complex: Mip protein, [U-98% 13C; U-98% 15N], 2 mM; Rapamycin 2 mM

complex_conditions: temperature: 298 K; pH: 6.5; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D HNCOcomplexisotropiccomplex_conditions
3D HNCAcomplexisotropiccomplex_conditions
3D HNCACBcomplexisotropiccomplex_conditions
3D CBCA(CO)NHcomplexisotropiccomplex_conditions
3D HNHAcomplexisotropiccomplex_conditions
3D HBHA(CO)NHcomplexisotropiccomplex_conditions
3D C(CO)NHcomplexisotropiccomplex_conditions
3D HCCH-TOCSYcomplexisotropiccomplex_conditions
2D 1H-15N HSQCcomplexisotropiccomplex_conditions
3D 1H-15N NOESYcomplexisotropiccomplex_conditions
2D 1H-13C HSQCcomplexisotropiccomplex_conditions
3D 1H-13C NOESYcomplexisotropiccomplex_conditions

Software:

NMRView, Johnson, One Moon Scientific - data analysis

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

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAE48749 GAN16811 GAN19917 GAN22931 GAN25926
EMBL CAD42883 CAD42884 CAD42885 CAD42887 CAD42888
GB AAB03461 AAB03462 AAB22717 AAB31083 AAB81364
PRF 2014249A
REF WP_010946528 WP_011213317 WP_011214989 WP_027221154 WP_040184983
SP A5IGB8 Q5ZXE0 Q70YI1
AlphaFold Q70YI1 Q5ZXE0 A5IGB8

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