BMRB Entry 25763

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25763
MolProbity Validation Chart

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Title:
Solution structure of an MbtH-like protein from Mycobacterium avium, Seattle Structural Genomics Center for Infectious Disease target MyavA.01649.c
Deposition date:
2015-08-20
Original release date:
2015-12-28
Authors:
Buchko, Garry
Citation:

Citation: Buchko, Garry; Hewitt, Stephen; Van Voorhis, Wesley; Myler, Peter. "Solution structure of a MbtH-like protein from Mycobacterium avium."  .

Assembly members:

Assembly members:
entity, polymer, 80 residues, 8994.921 Da.

Natural source:

Natural source:   Common Name: high GC Gram+   Taxonomy ID: 1794   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium avium

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: AVA0421

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GPGSMSINPFDDDNGSFFVL VNDEEQHSLWPAFADVPAGW RVVHGEADRAACLEYIEEHW PDIRPKSLRDKLATGRGFDQ

Data sets:
Data typeCount
13C chemical shifts235
15N chemical shifts62
1H chemical shifts322

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 80 residues - 8994.921 Da.

The first four residues are non-native and remain after removal of the N-terminal tag containing a poly-histidine site.

1   GLYPROGLYSERMETSERILEASNPROPHE
2   ASPASPASPASNGLYSERPHEPHEVALLEU
3   VALASNASPGLUGLUGLNHISSERLEUTRP
4   PROALAPHEALAASPVALPROALAGLYTRP
5   ARGVALVALHISGLYGLUALAASPARGALA
6   ALACYSLEUGLUTYRILEGLUGLUHISTRP
7   PROASPILEARGPROLYSSERLEUARGASP
8   LYSLEUALATHRGLYARGGLYPHEASPGLN

Samples:

sample_1: sodium chloride 100 ± 3 mM; TRIS 20 ± 0.5 mM; DTT 1 ± 0.01 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.12 M; pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
deuterium exchangesample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

Felix v2007, Accelrys Software Inc. - processing

SPARKY v3.115, Goddard - data analysis, peak picking

PSVS v1.5, Bhattacharya and Montelione - data analysis

NMR spectrometers:

  • Agilent INOVA 600 MHz
  • Agilent INOVA 500 MHz
  • Agilent VNMRS 750 MHz
  • Agilent VNMRS 800 MHz

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