BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25744

Title: NMR structure and dynamics of the resuscitation promoting factor RpfC catalytic domain   PubMed: 26576056

Deposition date: 2015-08-07 Original release date: 2015-11-17

Authors: Maione, Vincenzo; Russo, Luigi; Isernia, Carla

Citation: Maione, Vincenzo; Ruggiero, Alessia; Russo, Luigi; De Simone, Alfonso; Pedone, Paolo; Malgieri, Gaetano; Berisio, Rita; Isernia, Carla. "NMR Structure and Dynamics of the Resuscitation Promoting Factor RpfC Catalytic Domain"  PLoS One 10, e0142807-e0142807 (2015).

Assembly members:
entity, polymer, 82 residues, 8180.004 Da.

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

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

Entity Sequences (FASTA):
entity: GAMGPSPNWDAVAQCESGGN WAANTGNGKYGGLQFKPATW AAFGGVGNPAAASREQQIAV ANRVLAEQGLDAWPTCGAAS GL

Data sets:
Data typeCount
13C chemical shifts227
15N chemical shifts72
1H chemical shifts450

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 82 residues - 8180.004 Da.

1   GLYALAMETGLYPROSERPROASNTRPASP
2   ALAVALALAGLNCYSGLUSERGLYGLYASN
3   TRPALAALAASNTHRGLYASNGLYLYSTYR
4   GLYGLYLEUGLNPHELYSPROALATHRTRP
5   ALAALAPHEGLYGLYVALGLYASNPROALA
6   ALAALASERARGGLUGLNGLNILEALAVAL
7   ALAASNARGVALLEUALAGLUGLNGLYLEU
8   ASPALATRPPROTHRCYSGLYALAALASER
9   GLYLEU

Samples:

sample_1: entity, [U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 150 mM

sample_2: entity, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.9; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

VNMRJ, Varian - collection, processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Varian INOVA 500 MHz

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