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BMRB Entry 19538

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19538
MolProbity Validation Chart

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Title: SOLUTION STRUCTURE OF THE IMS DOMAIN OF THE MITOCHONDRIAL IMPORT PROTEIN TIM21 FROM S. CEREVISIAE   PubMed: 24653034

Deposition date: 2013-10-07 Original release date: 2014-04-14

Authors: Bajaj, Rakhi; Jaremko, Lukasz; Jaremko, Mariusz; Becker, Stefan; Zweckstetter, Markus

Citation: Jaremko, Lukasz; Jaremko, Mariusz; Giller, Karin; Becker, Stefan; Zweckstetter, Markus. "Structure of the mitochondrial translocator protein in complex with a diagnostic ligand."  Science 343, 1363-1366 (2014).

Assembly members:
entity, polymer, 127 residues, 14763.120 Da.

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
entity: GAMGSGDTQLFNRAVSMVEK NKDIRSLLQCDDGITGKERL KAYGELITNDKWTRNRPIVS TKKLDKEGRTHHYMRFHVES KKKIALVHLEAKESKQNYQP DFINMYVDVPGEKRYYLIKP KLHPVSN

Data sets:
Data typeCount
13C chemical shifts451
15N chemical shifts129
1H chemical shifts922

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1IMS DOMAIN1

Entities:

Entity 1, IMS DOMAIN 127 residues - 14763.120 Da.

1   GLYALAMETGLYSERGLYASPTHRGLNLEU
2   PHEASNARGALAVALSERMETVALGLULYS
3   ASNLYSASPILEARGSERLEULEUGLNCYS
4   ASPASPGLYILETHRGLYLYSGLUARGLEU
5   LYSALATYRGLYGLULEUILETHRASNASP
6   LYSTRPTHRARGASNARGPROILEVALSER
7   THRLYSLYSLEUASPLYSGLUGLYARGTHR
8   HISHISTYRMETARGPHEHISVALGLUSER
9   LYSLYSLYSILEALALEUVALHISLEUGLU
10   ALALYSGLUSERLYSGLNASNTYRGLNPRO
11   ASPPHEILEASNMETTYRVALASPVALPRO
12   GLYGLULYSARGTYRTYRLEUILELYSPRO
13   LYSLEUHISPROVALSERASN

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.3 – 0.8 mM; sodium chloride 50 mM; HEPES 20 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CYANA, Guntert, Mumenthaler and Wuthrich - peak picking, structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ GAA23416
EMBL CAA97021 CAY79794
GB AAZ22448 AHY79399 AJP38817 AJR76137 AJR76637
REF NP_011547
SP P53220
TPG DAA08130

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts