BMRB Entry 36112

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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/BMR36112
MolProbity Validation Chart

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Title:
NMR structure of the domain 5 of the E. coli ribosomal protein S1
Deposition date:
2017-08-16
Original release date:
2018-07-11
Authors:
Lu, Y.; Lim, L.; Song, J.
Citation:

Citation: Lim, Liang Zhong; Ee, Shermaine; Fu, Jing; Tan, Yanming; He, Cynthia; Song, Jianxing. "Kinetoplastid membrane protein-11 adopts a four-helix bundle fold in DPC micelle"  FEBS Lett 591, 3793-3804 (2017).
PubMed: 29082514

Assembly members:

Assembly members:
entity_1, polymer, 100 residues, 12071.572 Da.

Natural source:

Natural source:   Common Name: Trypanosoma brucei   Taxonomy ID: 5702   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli K-12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MATTYEEFAAKLDRLDAEFA KKMEEQNKRFFADKPDEATL SPEMKEHYEKFEKMIQEHTD KFNKKMREHSEHFKAKFAEL LEQQKNAQFPGKGSHHHHHH

Data sets:
Data typeCount
13C chemical shifts177
15N chemical shifts89
1H chemical shifts178

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 100 residues - 12071.572 Da.

1   METALATHRTHRTYRGLUGLUPHEALAALA
2   LYSLEUASPARGLEUASPALAGLUPHEALA
3   LYSLYSMETGLUGLUGLNASNLYSARGPHE
4   PHEALAASPLYSPROASPGLUALATHRLEU
5   SERPROGLUMETLYSGLUHISTYRGLULYS
6   PHEGLULYSMETILEGLNGLUHISTHRASP
7   LYSPHEASNLYSLYSMETARGGLUHISSER
8   GLUHISPHELYSALALYSPHEALAGLULEU
9   LEUGLUGLNGLNLYSASNALAGLNPHEPRO
10   GLYLYSGLYSERHISHISHISHISHISHIS

Samples:

sample_1: KMP-11, [U-99% 13C; U-99% 15N], 500 uM; DPC 150 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

AMBER v10, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v2, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNMR v2.4.1, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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