BMRB Entry 16160

Title:
1H, 13C, and 15N Chemical Shift Assignments for Myosin Phosphatase Trageting Subunit 1 (residues 1-98)
Deposition date:
2009-02-04
Original release date:
2012-08-07
Authors:
Pinheiro, Anderson; Peti, Wolfgang
Citation:

Citation: Pinheiro, Anderson; Peti, Wolfgang. "Understanding the assembly of the myosin phosphatase holoenzyme"  J. Am. Chem. Soc. ., .-..

Assembly members:

Assembly members:
MYPT1_1-98, polymer, 100 residues, 11073.5 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: RP1B

Data sets:
Data typeCount
13C chemical shifts380
15N chemical shifts92
1H chemical shifts351

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MYPT1 1-98 monomer1

Entities:

Entity 1, MYPT1 1-98 monomer 100 residues - 11073.5 Da.

The first 2 residues (Gly1 and His2) are part of the TEV protease cleavage site used during production of the protein.

1   GLYHISMETLYSMETALAASPALALYSGLN
2   LYSARGASNGLUGLNLEULYSARGTRPILE
3   GLYSERGLUTHRASPLEUGLUPROPROVAL
4   VALLYSARGLYSLYSTHRLYSVALLYSPHE
5   ASPASPGLYALAVALPHELEUALAALACYS
6   SERSERGLYASPTHRGLUGLUVALLEUARG
7   LEULEUGLUARGGLYALAASPILEASNTYR
8   ALAASNVALASPGLYLEUTHRALALEUHIS
9   GLNALASERILEASPASPASNVALASPMET
10   VALLYSPHELEUVALGLUASNGLYALAASN

Samples:

sample_1: MYPT1, [U-100% 15N], 1.2 ± 0.2 mM; NACL 50 mM; Sodium Phosphate 20 mM; PMSF 0.25 mM; TCEP 0.5 mM

sample_2: MYPT1, [U-100% 13C; U-100% 15N], 1.0 ± 0.2 mM; NACL 50 mM; Sodium Phosphate 20 mM; PMSF 0.25 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1.0 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCACOsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1

Software:

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

TOPSPIN v1.3, Bruker Biospin - collection, processing

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - chemical shift calculation

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAA07201 BAA07202
EMBL CAG32302
GB KQK73925 KQL94224
REF NP_990454 XP_002194705 XP_005039540 XP_005039541 XP_005039542
SP Q90623
AlphaFold Q90623

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