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 27690

Title: MtFKBP   PubMed: 30879170

Deposition date: 2018-11-13 Original release date: 2019-03-28

Authors: Andrade, Guilherme; Silva, Luis; Oliveira, Danielle; Pires, Jose; Almeida, Fabio; Anobom, Cristiane

Citation: Andrade, Guilherme; Silva, Luis; Oliveira, Danielle; Pires, Jose; Almeida, Fabio; Anobom, Cristiane. "Backbone and side chain 1H, 15N and 13C assignments of a putative peptidyl prolyl cis-trans isomerase FKBP12 from Mycobacterium tuberculosis"  Biomol. NMR Assignments 13, 239-243 (2019).

Assembly members:
MtFKBP, polymer, 126 residues, Formula weight is not available

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: Terrabacteria   Genus/species: Mycobacterium tuberculosis

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

Entity Sequences (FASTA):
MtFKBP: GAMALERPEIDFPEGQPPEY LDITDITEGDGPEAVKGSNV SMHYVGVSWSTGEEFDASWN RGSTLDFTLGTGRVIKGWDM GIAGMKVGGRRKLVIPPHLA YGDRSPSPAIKPGETLIFVV DLVGVG

Data sets:
Data typeCount
13C chemical shifts517
15N chemical shifts133
1H chemical shifts813

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FKBP12 monomer1

Entities:

Entity 1, FKBP12 monomer 126 residues - Formula weight is not available

1   GLYALAMETALALEUGLUARGPROGLUILE
2   ASPPHEPROGLUGLYGLNPROPROGLUTYR
3   LEUASPILETHRASPILETHRGLUGLYASP
4   GLYPROGLUALAVALLYSGLYSERASNVAL
5   SERMETHISTYRVALGLYVALSERTRPSER
6   THRGLYGLUGLUPHEASPALASERTRPASN
7   ARGGLYSERTHRLEUASPPHETHRLEUGLY
8   THRGLYARGVALILELYSGLYTRPASPMET
9   GLYILEALAGLYMETLYSVALGLYGLYARG
10   ARGLYSLEUVALILEPROPROHISLEUALA
11   TYRGLYASPARGSERPROSERPROALAILE
12   LYSPROGLYGLUTHRLEUILEPHEVALVAL
13   ASPLEUVALGLYVALGLY

Samples:

sample_1: PMSF 2 mM; EDTA 5 mM; sodium azide 5 mM; sodium chloride 150 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 0.22 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_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

Software:

TOPSPIN v3.1, Bruker Biospin - processing

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

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 900 MHz

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