BMRB Entry 25513

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR25513
MolProbity Validation Chart

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Title:
SOLUTION STRUCTURE OF THE A147T VARIANT OF THE MITOCHONDRIAL TRANSLOCATOR PROTEIN (TSPO) IN COMPLEX WITH PK11195
Deposition date:
2015-03-04
Original release date:
2015-06-08
Authors:
Jaremko, Mariusz; Jaremko, Lukasz; Giller, Karin; Becker, Stefan; Zweckstetter, Markus
Citation:

Citation: Jaremko, M.; Jaremko, L.; Giller, K.; Becker, S.; Zweckstetter, M.. "Structural integrity of the A147T polymorph of mammalian TSPO"  Chembiochem 16, 1483-1489 (2015).
PubMed: 25974690

Assembly members:

Assembly members:
TRANSLOCATOR_PROTEIN_A147T, polymer, 169 residues, 18828.873 Da.
N-[(2R)-butan-2-yl]-1-(2-chlorophenyl)-N-methylisoquinoline-3-carboxamide, non-polymer, 352.857 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI   Vector: PET15PBR

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TRANSLOCATOR_PROTEIN_A147T: MPESWVPAVGLTLVPSLGGF MGAYFVRGEGLRWYAGLQKP SWHPPRWTLAPIWGTLYSAM GYGSYIVWKELGGFTEDAMV PLGLYTGQLALNWAWPPIFF GARQMGWALADLLLVSGVAT ATTLAWHRVSPPAARLLYPY LAWLAFTTVLNYYVWRDNSG RRGGSRLAE

Data sets:
Data typeCount
13C chemical shifts588
15N chemical shifts171
1H chemical shifts1171

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TRANSLOCATOR PROTEIN A147T1
2PKA2

Entities:

Entity 1, TRANSLOCATOR PROTEIN A147T 169 residues - 18828.873 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   LEUALATRPLEUALAPHETHRTHRVALLEU
16   ASNTYRTYRVALTRPARGASPASNSERGLY
17   ARGARGGLYGLYSERARGLEUALAGLU

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

1   PKA

Samples:

sample_1: TRANSLOCATOR PROTEIN A147T, [U-100% 13C; U-100% 15N], 0.3 – 0.7 mM; (R)-PK11195 2.9 mM; 2H-DPC, [U-2H], 2%; H2O 90%; D2O, [U-2H], 10%

sample_2: TRANSLOCATOR PROTEIN A147T, [U-100% 13C; U-100% 15N; U-80% 2H], 0.3 – 0.7 mM; (R)-PK11195 2.9 mM; 2H-DPC, [U-2H], 2%; H2O 90%; D2O, [U-2H], 10%

sample_3: TRANSLOCATOR PROTEIN A147T, [U-100% 13C; U-100% 15N], 0.3 – 0.7 mM; (R)-PK11195 2.9 mM; 2H-DPC, [U-2H], 2%; D2O, [U-2H], 100%

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_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_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 HN(CA)CBsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1

Software:

CYANA_3.0, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY, Goddard - chemical shift assignment

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

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

CARA, Keller and Wuthrich - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

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