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Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 19608

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19608
MolProbity Validation Chart

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Title: Solution structure of the mitochondrial translocator protein (TSPO) in complex with its high-affinity ligand PK11195   PubMed: 24653034

Deposition date: 2013-11-11 Original release date: 2014-03-31

Authors: Jaremko, Mariusz; Jaremko, Lukasz; Giller, Karin; Becker, Stefan; Zweckstetter, Markus

Citation: Jaremko, Mariusz; Jaremko, Lukasz; 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_1, polymer, 169 residues, 18798.848 Da.
N-[(2R)-butan-2-yl]-1-(2-chlorophenyl)-N-methylisoquinoline-3-carboxamide, non-polymer, 352.857 Da.

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
entity_1: MPESWVPAVGLTLVPSLGGF MGAYFVRGEGLRWYAGLQKP SWHPPRWTLAPIWGTLYSAM GYGSYIVWKELGGFTEDAMV PLGLYTGQLALNWAWPPIFF GARQMGWALADLLLVSGVAT ATTLAWHRVSPPAARLLYPY LAWLAFATVLNYYVWRDNSG RRGGSRLAE

Data sets:
Data typeCount
1H chemical shifts1168
13C chemical shifts738
15N chemical shifts169

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TSPO1
2PKA2

Entities:

Entity 1, TSPO 169 residues - 18798.848 Da.

1   METPROGLUSERTRPVALPROALAVALGLY
2   LEUTHRLEUVALPROSERLEUGLYGLYPHE
3   METGLYALATYRPHEVALARGGLYGLUGLY
4   LEUARGTRPTYRALAGLYLEUGLNLYSPRO
5   SERTRPHISPROPROARGTRPTHRLEUALA
6   PROILETRPGLYTHRLEUTYRSERALAMET
7   GLYTYRGLYSERTYRILEVALTRPLYSGLU
8   LEUGLYGLYPHETHRGLUASPALAMETVAL
9   PROLEUGLYLEUTYRTHRGLYGLNLEUALA
10   LEUASNTRPALATRPPROPROILEPHEPHE
11   GLYALAARGGLNMETGLYTRPALALEUALA
12   ASPLEULEULEUVALSERGLYVALALATHR
13   ALATHRTHRLEUALATRPHISARGVALSER
14   PROPROALAALAARGLEULEUTYRPROTYR
15   LEUALATRPLEUALAPHEALATHRVALLEU
16   ASNTYRTYRVALTRPARGASPASNSERGLY
17   ARGARGGLYGLYSERARGLEUALAGLU

Entity 2, PKA - C21 H21 Cl N2 O - 352.857 Da.

1   PKA

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.9 mM; PKA 2.9 mM; sodium phosphate buffer 10 mM; DPC micelles, [U-100% 2H], 60 mM; H2O 90%; D2O 10%

sample_2: entity_1, [U-100% 13C; U-100% 15N], 0.9 mM; PKA 2.9 mM; sodium phosphate buffer 10 mM; DPC micelles, [U-2H], 60 mM; D2O 100%

sample_3: entity_1, [U-13C; U-15N; U-2H], 0.8 mM; PKA 2.9 mM; sodium phosphate buffer 10 mM; DPC micelles, [U-100% 2H], 60 mM; H2O 90%; D2O 10%

sample_4: entity_1, [U-2H; U-1H, 15N,13C-TRP, ARG], 0.5 mM; PKA 2.9 mM; sodium phosphate buffer 10 mM; DPC micelles, [U-100% 2H], 60 mM; H2O 90%; D2O 10%

sample_5: entity_1, [U-2H,15N; Idelta1/Leu,ValproS-13CH3], 0.5 mM; PKA 2.9 mM; sodium phosphate buffer 10 mM; DPC micelles, [U-100% 2H], 60 mM; H2O 90%; D2O 10%

sample_6: entity_1, [U-2H; U-1H, 15N,13C-Ile,Lys,Pro,Gly], 0.5 mM; PKA 2.9 mM; sodium phosphate buffer 10 mM; DPC micelles, [U-100% 2H], 60 mM; H2O 90%; D2O 10%

sample_7: entity_1, [U-2H; U-1H,15N-Leu,Phe], 0.5 mM; PKA 2.9 mM; sodium phosphate buffer 10 mM; DPC micelles, [U-100% 2H], 60 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 10 mM; pH: 6.0; pressure: 1 atm; temperature: 315 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 CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_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
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_4isotropicsample_conditions_1
3D HNCOsample_4isotropicsample_conditions_1
3D HNCAsample_4isotropicsample_conditions_1
3D HNCACBsample_4isotropicsample_conditions_1
3D HN(CO)CAsample_4isotropicsample_conditions_1
3D CBCA(CO)NHsample_6isotropicsample_conditions_1
3D HNCOsample_6isotropicsample_conditions_1
3D HNCAsample_6isotropicsample_conditions_1
3D HNCACBsample_6isotropicsample_conditions_1
3D HN(CO)CAsample_6isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_5isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_5isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_7isotropicsample_conditions_1
3D HNCOsample_7isotropicsample_conditions_1
3D HNCAsample_7isotropicsample_conditions_1
3D HNCACBsample_7isotropicsample_conditions_1
3D HN(CO)CAsample_7isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_7isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_7isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_5isotropicsample_conditions_1
2D 1H-15N HSQCsample_6isotropicsample_conditions_1
2D 1H-15N HSQCsample_7isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_6isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_6isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - peak picking

SPARKY, Goddard - chemical shift assignment

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

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

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 25513
PDB
DBJ BAA04749 BAE29056 BAE29628 BAE30386 BAE30511
GB AAA20127 AAH02055 AAL87529 AAL87530 EDL04468
REF NP_033905
SP P50637

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