BMRB Entry 36368

Title:
Solution structure of the C-terminal domain of Mycobacterium Tuberculosis ribosome maturation factor protein RimM
Deposition date:
2020-08-08
Original release date:
2021-04-29
Authors:
Zhang, H.; Lin, D.
Citation:

Citation: Zhang, H.; Lin, D.. "The structure of CTD of Mycobacterium Tuberculosis RimM"  .

Assembly members:

Assembly members:
entity_1, polymer, 85 residues, 9293.420 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 83332   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium Mycobacterium tuberculosis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET22b

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts321
15N chemical shifts74
1H chemical shifts494

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 85 residues - 9293.420 Da.

1   METASPTHRTYRTYRASPHISGLNLEUVAL
2   GLYLEUMETVALGLNTHRALATHRGLYGLU
3   GLYVALGLYVALVALTHRGLUVALVALHIS
4   THRALAALAGLYGLULEULEUALAVALLYS
5   ARGASPSERASPGLUVALLEUVALPROPHE
6   VALARGALAILEVALTHRSERVALSERLEU
7   ASPASPGLYILEVALGLUILEASPPROPRO
8   HISGLYLEULEUASNLEUGLULEUGLUHIS
9   HISHISHISHISHIS

Samples:

sample_1: C-terminal domain of ribosome maturation factor RimM 0.6 mM; potassium chloride 100 mM; potassium phosphate 20 mM; sodium azide 0.02 % w/v; H2O 90%; D2O, [U-2H], 10%

sample_2: C-terminal domain of ribosome maturation factor RimM, [U-99% 15N], 0.6 mM; potassium chloride 100 mM; potassium phosphate 20 mM; sodium azide 0.02 % w/v; H2O 90%; D2O, [U-2H], 10%

sample_3: C-terminal domain of ribosome maturation factor RimM, [U-99% 13C; U-99% 15N], 0.6 mM; potassium chloride 100 mM; potassium phosphate 20 mM; sodium azide 0.02 % w/v; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 120 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HN(CA)COsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1
3D H(CCO)NHsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D 15N-edited NOESY-HSQCsample_2isotropicsample_conditions_1
3D 13C-edited NOESY-HSQCsample_3isotropicsample_conditions_1

Software:

CNS vAria2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation

NMRFAM-SPARKY v1.4.7, Lee W., Tonelli M., Markley J. L. - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 850 MHz

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