BMRB Entry 6688

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6688

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Title:
NMR chemical shift entry for protein Rv1980c (MPT64) from M. tuberculosis
Deposition date:
2005-06-13
Original release date:
2015-09-02
Authors:
Danahy, Jessica; Potter, Belinda; Geisbrecht, Brian; Laity, John
Citation:

Citation: Danahy, Jessica; Potter, Belinda; Geisbrecht, Brian; Laity, John. "NMR Assignment of Protein Rv1980c from Mycobacterium Tuberculosis"  J. Biomol. NMR 33, 73-73 (2005).
PubMed: 16222561

Assembly members:

Assembly members:
Rv1980c (MPT64) polypeptide, polymer, 206 residues, 22564 Da.

Natural source:

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 83332   Superkingdom: Eubacteria   Kingdom: Not applicable   Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rv1980c (MPT64) polypeptide: MAPKTYCEELKGTDTGQACQ IQMSDPAYNINISLPSYYPD QKSLENYIAQTRDKFLSAAT SSTPREAPYELNITSATYQS AIPPRGTQAVVLKVYQNAGG THPTTTYKAFDWDQAYRKPI TYDTLWQADTDPLPVVFPIV QGELSKQTGQQVSIAPNAGL DPVNYQNFAVTNDGVIFFFN PGELLPEAAGPTQVLVPRSA IDSMLA

Data sets:
Data typeCount
13C chemical shifts832
15N chemical shifts199
1H chemical shifts1207

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rv1980c (MPT64)1

Entities:

Entity 1, Rv1980c (MPT64) 206 residues - 22564 Da.

Sequence of recombinant, mature polypeptide.

1   METALAPROLYSTHRTYRCYSGLUGLULEU
2   LYSGLYTHRASPTHRGLYGLNALACYSGLN
3   ILEGLNMETSERASPPROALATYRASNILE
4   ASNILESERLEUPROSERTYRTYRPROASP
5   GLNLYSSERLEUGLUASNTYRILEALAGLN
6   THRARGASPLYSPHELEUSERALAALATHR
7   SERSERTHRPROARGGLUALAPROTYRGLU
8   LEUASNILETHRSERALATHRTYRGLNSER
9   ALAILEPROPROARGGLYTHRGLNALAVAL
10   VALLEULYSVALTYRGLNASNALAGLYGLY
11   THRHISPROTHRTHRTHRTYRLYSALAPHE
12   ASPTRPASPGLNALATYRARGLYSPROILE
13   THRTYRASPTHRLEUTRPGLNALAASPTHR
14   ASPPROLEUPROVALVALPHEPROILEVAL
15   GLNGLYGLULEUSERLYSGLNTHRGLYGLN
16   GLNVALSERILEALAPROASNALAGLYLEU
17   ASPPROVALASNTYRGLNASNPHEALAVAL
18   THRASNASPGLYVALILEPHEPHEPHEASN
19   PROGLYGLULEULEUPROGLUALAALAGLY
20   PROTHRGLNVALLEUVALPROARGSERALA
21   ILEASPSERMETLEUALA

Samples:

sample_1: Rv1980c (MPT64) polypeptide, [U-15N; U-13C], 2.0 ± 0.05 mM; MES 20 mM; D2O 5%; NaN3 1 mM; DSS 0.2 mM

conditions_1: pH: 6.85; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N_HSQCsample_1not availableconditions_1
3D HNCACBsample_1not availableconditions_1
3D CBCA(CO)NHsample_1not availableconditions_1
3D HNCOsample_1not availableconditions_1
3D (HCA)CO(CA)NHsample_1not availableconditions_1
3D HNHAsample_1not availableconditions_1
3D 13C-NOESY-HSQC (centered at 43 ppm)sample_1not availableconditions_1
3D 13C-NOESY-HSQC (centered at 125 ppm)sample_1not availableconditions_1
3D HCCH-COSYsample_1not availableconditions_1
3D HCCH-TOCSYsample_1not availableconditions_1
3D 15N-NOESY-HSQCsample_1not availableconditions_1
3D HNCAsample_1not availableconditions_1

Software:

NMRView v5.0.4 - Data analysis

NMRPipe v97.027.12.56 - Raw spectral data processing

NMR spectrometers:

  • Varian Inova 600 MHz

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