BMRB Entry 25405

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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/BMR25405
MolProbity Validation Chart

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Title:
Solution structure of the C-terminal domain of MvaT
Deposition date:
2014-12-25
Original release date:
2015-06-29
Authors:
Ding, Pengfei; Xia, Bin
Citation:

Citation: Ding, Pengfei; McFarland, Kirsty; Jin, Shujuan; Tong, Grace; Duan, Bo; Yang, Ally; Hughes, Timothy; Liu, Jun; Dove, Simon; Navarre, William; Xia, Bin. "A Novel AT-Rich DNA Recognition Mechanism for Bacterial Xenogeneic Silencer MvaT"  Plos Pathog. 11, e1004967-e1004967 (2015).
PubMed: 26068099

Assembly members:

Assembly members:
MvaT, polymer, 55 residues, 5352.173 Da.

Natural source:

Natural source:   Common Name: Pseudomonas aeruginosa   Taxonomy ID: 287   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MvaT: MKRARKVKQYKNPHTGEVIE TKGGNHKTLKEWKAKWGPEA VESWATLLGHHHHHH

Data sets:
Data typeCount
13C chemical shifts207
15N chemical shifts50
1H chemical shifts331

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1C-terminal domain of MvaT1

Entities:

Entity 1, C-terminal domain of MvaT 55 residues - 5352.173 Da.

1   METLYSARGALAARGLYSVALLYSGLNTYR
2   LYSASNPROHISTHRGLYGLUVALILEGLU
3   THRLYSGLYGLYASNHISLYSTHRLEULYS
4   GLUTRPLYSALALYSTRPGLYPROGLUALA
5   VALGLUSERTRPALATHRLEULEUGLYHIS
6   HISHISHISHISHIS

Samples:

sample_1: MvaT, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 50 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 25407
PDB
DBJ BAK88160 BAP21250 BAP52811 BAQ41953 BAR69621
EMBL CAW29447 CCQ87551 CDH72901 CDH79198 CDI92830
GB AAG07703 AAP33788 ABJ13585 ABR84836 AEO76886
REF NP_253005 WP_003093888 WP_003125172 WP_012077126 WP_015478773

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