BMRB Entry 26875

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26875

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Title:
Backbone chemical shift assignments of H24N mutant of Vibrio cholerae peptidyl-tRNA hydrolase
Deposition date:
2016-08-15
Original release date:
2017-02-16
Authors:
Kabra, Ashish; Shahid, Salman; Arora, Ashish
Citation:

Citation: Kabra, Ashish; Shahid, Salman; Pal, Ravikant; Yadav, Rahul; Pulavarti, SVSRK; Jain, Anupam; Tripathi, Sarita; Arora, Ashish. "Unraveling the stereochemical and dynamic aspects of the catalytic site of bacterial peptidyl-tRNA hydrolase"  RNA 23, 202-216 (2017).
PubMed: 28096445

Assembly members:

Assembly members:
VcPth-H24N_mutant, polymer, 199 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: g-proteobacteria   Taxonomy ID: 666   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Vibrio cholerae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-NH6

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VcPth-H24N_mutant: GAMVSQPIKLLVGLANPGPE YAKTRHNAGAWVVEELARIH NVTLKHEPKFFGLTGRLLIN SQELRVLIPTTFMNLSGKAI AALANFYQIKPEEIMVAHDE LDLPPGVAKFKQGGGHGGHN GLKDTISKLGNNKEFYRLRL GIGHPGHKDKVAGYVLGKAP AKEQECLDAAVDESVRCLEI LMKDGLTKAQNRLHTFKAE

Data sets:
Data typeCount
13C chemical shifts550
15N chemical shifts182
1H chemical shifts182

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1VcPth-H24N mutant1

Entities:

Entity 1, VcPth-H24N mutant 199 residues - Formula weight is not available

1   GLYALAMETVALSERGLNPROILELYSLEU
2   LEUVALGLYLEUALAASNPROGLYPROGLU
3   TYRALALYSTHRARGHISASNALAGLYALA
4   TRPVALVALGLUGLULEUALAARGILEHIS
5   ASNVALTHRLEULYSASNGLUPROLYSPHE
6   PHEGLYLEUTHRGLYARGLEULEUILEASN
7   SERGLNGLULEUARGVALLEUILEPROTHR
8   THRPHEMETASNLEUSERGLYLYSALAILE
9   ALAALALEUALAASNPHETYRGLNILELYS
10   PROGLUGLUILEMETVALALAHISASPGLU
11   LEUASPLEUPROPROGLYVALALALYSPHE
12   LYSGLNGLYGLYGLYHISGLYGLYHISASN
13   GLYLEULYSASPTHRILESERLYSLEUGLY
14   ASNASNLYSGLUPHETYRARGLEUARGLEU
15   GLYILEGLYHISPROGLYHISLYSASPLYS
16   VALALAGLYTYRVALLEUGLYLYSALAPRO
17   ALALYSGLUGLNGLUCYSLEUASPALAALA
18   VALASPGLUSERVALARGCYSLEUGLUILE
19   LEUMETLYSASPGLYLEUTHRLYSALAGLN
20   ASNARGLEUHISTHRPHELYSALAGLU

Samples:

sample_1: VcPth-H24N mutant, [U-100% 15N], 0.5 – 1.0 mM; sodium azide 0.1%; DTT 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 95%; D2O 5%

sample_2: VcPth-H24N mutant, [U-100% 13C; U-100% 15N], 0.8 – 1.0 mM; sodium azide 0.1%; DTT 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1

Software:

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

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Agilent DD2 700 MHz

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