BMRB Entry 18198

Title:
Chemical Shift Assignment of the PP1 Binding Domain of NIPP1
Deposition date:
2012-01-17
Original release date:
2012-09-14
Authors:
O'Connell, Nichole; Nichols, Scott; Peti, Wolfgang
Citation:

Citation: Nichols, Nichole; Heroes, Scott; Beullens, Ewald; Bollen, Monique; Peti, Mathieu; Page, Wolfgang. "The molecular basis for substrate specificity of the nuclear NIPP1:PP1 holoenzyme."  Structure 20, 1746-1756 (2012).
PubMed: 22940584

Assembly members:

Assembly members:
NIPP1, polymer, 88 residues, Formula weight is not available

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: pET M30-MBP

Data sets:
Data typeCount
13C chemical shifts167
15N chemical shifts81
1H chemical shifts81

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PP1 binding domain1

Entities:

Entity 1, PP1 binding domain 88 residues - Formula weight is not available

Residues 1-6 are cloning artifacts; protein phosphatase 1 binding domain of NIPP1 (residues 144-225) are 7-end

1   GLYALAMETGLYALASERGLYGLYGLUASP
2   ASPGLULEULYSGLYLEULEUGLYLEUPRO
3   GLUGLUGLUTHRGLULEUASPASNLEUTHR
4   GLUPHEASNTHRALAHISASNLYSARGILE
5   SERTHRLEUTHRILEGLUGLUGLYASNLEU
6   ASPILEGLNARGPROLYSARGLYSARGLYS
7   ASNSERARGVALTHRPHESERGLUASPASP
8   GLUILEILEASNPROGLUASPVALASPPRO
9   SERVALGLYARGPHEARGASNMET

Samples:

sample_1: NIPP1, [U-99% 13C; U-99% 15N], 1 mM; H2O 90%; D2O 10%; NaCl 50 mM

sample_2: NIPP1, [U-98% 15N], 1 mM; H2O 90%; D2O 10%; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

CARA v1.8, Keller and Wuthrich - chemical shift assignment

TOPSPIN v2.1, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

DBJ BAC27653 BAF84766 BAG73611
EMBL CAA90625 CAG31586
GB AAD22486 AAD24669 AAD24670 AAD31541 AAD31542
REF NP_001026062 NP_001101381 NP_001230343 NP_001253391 NP_001277654
SP Q12972 Q28147 Q8R3G1
TPG DAA32062
AlphaFold Q28147 Q12972 Q8R3G1

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