BMRB Entry 30034

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30034
MolProbity Validation Chart

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Title:
Solution structure of Rv1466 from Mycobacterium tuberculosis, a protein associated with [Fe-S] complex assembly and repair - Seattle Structural Genomics Center for Infectious Disease target MytuD.17486.a
Deposition date:
2016-03-13
Original release date:
2016-05-23
Authors:
Buchko, G.; Seattle Structural Genomics Center for Infectious Disease (SSGCID), SSGCID
Citation:

Citation: Buchko, G.; Hewitt, S.; Van Voorhis, W.C.; Myler, P.. "Solution structure of Rv1466, a Mycobacterium tuberculosis protein associated with [Fe-S] cluster assembly and repair."  .

Assembly members:

Assembly members:
entity_1, polymer, 119 residues, 12688.023 Da.

Natural source:

Natural source:   Common Name: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)   Taxonomy ID: 419947   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGSMSETSAPAEELLADVE EAMRDVVDPELGINVVDLGL VYGLDVQDGDEGTVALIDMT LTSAACPLTDVIEDQSRSAL VGSGLVDDIRINWVWNPPWG PDKITEDGREQLRALGFTV

Data typeCount
13C chemical shifts439
15N chemical shifts115
1H chemical shifts703

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 119 residues - 12688.023 Da.

1   GLYPROGLYSERMETSERGLUTHRSERALA
2   PROALAGLUGLULEULEUALAASPVALGLU
3   GLUALAMETARGASPVALVALASPPROGLU
4   LEUGLYILEASNVALVALASPLEUGLYLEU
5   VALTYRGLYLEUASPVALGLNASPGLYASP
6   GLUGLYTHRVALALALEUILEASPMETTHR
7   LEUTHRSERALAALACYSPROLEUTHRASP
8   VALILEGLUASPGLNSERARGSERALALEU
9   VALGLYSERGLYLEUVALASPASPILEARG
10   ILEASNTRPVALTRPASNPROPROTRPGLY
11   PROASPLYSILETHRGLUASPGLYARGGLU
12   GLNLEUARGALALEUGLYPHETHRVAL

Samples:

sample_1: DTT 1 mM; Rv1466, [U-13C; U-15N], 1.0 ± 0.2 mM; TRIS 20 mM; sodium chloride 100 mM

sample_2: DTT 1 mM; Rv1466, [U-15N], 0.5 mM; TRIS 20 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.12 M; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1anisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1anisotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1anisotropicsample_conditions_1
3D HNCACBsample_1anisotropicsample_conditions_1
3D CBCA(CO)NHsample_1anisotropicsample_conditions_1
3D H(CCO)NHsample_1anisotropicsample_conditions_1
3D HNCOsample_1anisotropicsample_conditions_1
Deuterium exchangesample_2anisotropicsample_conditions_1
2D Deltasample_1anisotropicsample_conditions_1
3D C(CO)NHsample_1anisotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1anisotropicsample_conditions_1
3D 1H-15N NOESYsample_1anisotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1anisotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

Felix v2007, Accelrys Software Inc. - processing

PSVS v1.5, Bhattacharya and Montelione - data analysis

SPARKY v3.115, Goddard - data analysis, peak picking

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz
  • Varian VXRS 750 MHz
  • Varian VXRS 800 MHz

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