BMRB Entry 16253

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16253
MolProbity Validation Chart

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Title:
NMR chemical shift assignments for Rv2377c, a MbtH-like protein from Mycobacterium tuberculosis: A Structural Genomics Center for Infectious Disease (SSGCID) community request
Deposition date:
2009-04-11
Original release date:
2009-05-20
Authors:
Buchko, Garry
Citation:

Citation: Buchko, Garry; Kim, Chang-Yub; Terwilliger, Thomas; Myler, Peter. "Solution structure of Rv2377c-founding member of the MbtH-like protein family."  Tuberculosis (Edinb) 90, 245-251 (2010).
PubMed: 20434955

Assembly members:

Assembly members:
Rv2377c, polymer, 74 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: modifed pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rv2377c: GSHMSTNPFDDDNGAFFVLV NDEDQHSLWPVFADIPAGWR VVHGEASRAACLDYVEKNWT DLRPKSLRDAMVED

Data sets:
Data typeCount
13C chemical shifts210
15N chemical shifts52
1H chemical shifts320

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rv2377c1

Entities:

Entity 1, Rv2377c 74 residues - Formula weight is not available

The first 3 N-terminal residues, GSH-, are non-native residues that remain after thrombin cleavage of an affinity tag.

1   GLYSERHISMETSERTHRASNPROPHEASP
2   ASPASPASNGLYALAPHEPHEVALLEUVAL
3   ASNASPGLUASPGLNHISSERLEUTRPPRO
4   VALPHEALAASPILEPROALAGLYTRPARG
5   VALVALHISGLYGLUALASERARGALAALA
6   CYSLEUASPTYRVALGLULYSASNTRPTHR
7   ASPLEUARGPROLYSSERLEUARGASPALA
8   METVALGLUASP

Samples:

sample_1: Rv2377c, [U-98% 13C; U-98% 15N], 2 ± 0.2 mM; sodium chloride 300 ± 10 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.1 mM; H2O 90%; D2O 10%

sample_2: Rv2377c, [U-98% 13C; U-98% 15N], 2 ± 0.2 mM; sodium chloride 300 ± 10 mM; TRIS 20 ± 1 mM; DTT 1 ± 0.1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.32 M; pH: 7.1; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HC(CO)NHsample_1isotropicsample_conditions_1
deuterium X-changesample_2isotropicsample_conditions_1

Software:

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

FELIX v2007, Accelrys Software Inc. - processing

SPARKY v3.115, Goddard - chemical shift assignment, peak picking

PSVS, Bhattacharya and Montelione - data analysis

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 900 MHz
  • Varian INOVA 600 MHz
  • Varian UnityPlus 500 MHz

Related Database Links:

PDB
DBJ BAH26669 BAL66401 BAQ06468 GAA46054
EMBL CAL72379 CCC27461 CCC44740 CCC64968 CCE37847
GB AAK46740 ABQ74170 ABR06731 ACT24652 AEB03737
REF NP_216893 NP_856047 WP_003412265 WP_003916994 WP_015290621
SP P59965 P9WIP4 P9WIP5
AlphaFold P59965 P9WIP4 P9WIP5

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