BMRB

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 15179

Title: Intrinsically unstructured proteins provide the specificity for protein phosphatase 1 regulation.   PubMed: 17279777

Authors: Dancheck, Barbara; Peti, Wolfgang

Citation: Kelker, Matthew; Dancheck, Barbara; Ju, Tingting; Kessler, Rene; Hudak, Jebecka; Nairn, Angus; Peti, Wolfgang. "Structural basis for spinophilin-neurabin receptor interaction"  Biochemistry 46, 2333-2344 (2007).

Assembly members:
Inhibitor-2, polymer, 159 residues, 17960 Da.

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

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

Entity Sequences (FASTA):
Inhibitor-2: GHMPIKGILKNKTSTTSSMV ASAEQPRGNVDEELSKKSQK WDEMNILATYHPADKDYGLM KIDEPSTPYHSMMGDDEDAC SDTEATEAMAPDILARKLAA AEGLEPKYRIQEQESSGEED SDLSPEEREKKRQFEMKRKL HYNEGLNIKLARQLISKDL

Data sets:
Data typeCount
13C chemical shifts624
15N chemical shifts141
1H chemical shifts905

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Inhibitor-21

Entities:

Entity 1, Inhibitor-2 159 residues - 17960 Da.

Residues 1 - 2 (G H) are cloning artifacts. Residues 3 - 159 are Inhibitor-2 residues 9 - 164.

1   GLYHISMETPROILELYSGLYILELEULYS
2   ASNLYSTHRSERTHRTHRSERSERMETVAL
3   ALASERALAGLUGLNPROARGGLYASNVAL
4   ASPGLUGLULEUSERLYSLYSSERGLNLYS
5   TRPASPGLUMETASNILELEUALATHRTYR
6   HISPROALAASPLYSASPTYRGLYLEUMET
7   LYSILEASPGLUPROSERTHRPROTYRHIS
8   SERMETMETGLYASPASPGLUASPALACYS
9   SERASPTHRGLUALATHRGLUALAMETALA
10   PROASPILELEUALAARGLYSLEUALAALA
11   ALAGLUGLYLEUGLUPROLYSTYRARGILE
12   GLNGLUGLNGLUSERSERGLYGLUGLUASP
13   SERASPLEUSERPROGLUGLUARGGLULYS
14   LYSARGGLNPHEGLUMETLYSARGLYSLEU
15   HISTYRASNGLUGLYLEUASNILELYSLEU
16   ALAARGGLNLEUILESERLYSASPLEU

Samples:

sample_1: Inhibitor-2, [U-99% 15N], 750 uM; sodium phosphate 20 mM; sodium chloride 50 mM; PMSF 250 uM; D2O 10%

sample_2: Inhibitor-2, [U-99% 13C; U-99% 15N], 750 uM; sodium phosphate 20 mM; sodium chloride 50 mM; PMSF 250 uM; D2O 10%

sample_conditions_1: ionic strength: 70 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

XEASY v1.5, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

BMRB 4720
DBJ BAI46858
EMBL CAA55475 CAA82754 CAB41680
GB AAC51206 AAH07655 AAL48322 ABW23430 ADQ32784
PRF 2007253A
REF NP_001247610 NP_001278433 NP_001303254 NP_006232 XP_002814482
SP P41236