BMRB Entry 15179

Name: Intrinsically unstructured proteins provide the specificity for protein phosphatase 1 regulation.
Published: 2007-10-26

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15179

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Intrinsically unstructured proteins provide the specificity for protein phosphatase 1 regulation.

Deposition date:

2007-03-16

Original release date:

2007-10-26

Authors:

Dancheck, Barbara; Peti, Wolfgang

Citation:

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).
PubMed: 17279777

Assembly members:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	624
15N chemical shifts	141
1H chemical shifts	905

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Inhibitor-2	1

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

GLY

HIS

MET

PRO

ILE

LYS

GLY

ILE

LEU

LYS

2

ASN

LYS

THR

SER

THR

SER

MET

VAL

3

ALA

SER

ALA

GLU

GLN

PRO

ARG

GLY

ASN

VAL

4

ASP

GLU

LEU

SER

LYS

SER

GLN

LYS

5

TRP

ASP

GLU

MET

ASN

ILE

LEU

ALA

THR

TYR

6

HIS

PRO

ALA

ASP

LYS

ASP

TYR

GLY

LEU

MET

7

LYS

ILE

ASP

GLU

PRO

SER

THR

PRO

TYR

HIS

8

SER

MET

GLY

ASP

GLU

ASP

ALA

CYS

9

SER

ASP

THR

GLU

ALA

THR

GLU

ALA

MET

ALA

10

PRO

ASP

ILE

LEU

ALA

ARG

LYS

LEU

ALA

11

ALA

GLU

GLY

LEU

GLU

PRO

LYS

TYR

ARG

ILE

12

GLN

GLU

GLN

GLU

SER

GLY

GLU

ASP

13

SER

ASP

LEU

SER

PRO

GLU

ARG

GLU

LYS

14

LYS

ARG

GLN

PHE

GLU

MET

LYS

ARG

LYS

LEU

15

HIS

TYR

ASN

GLU

GLY

LEU

ASN

ILE

LYS

LEU

16

ALA

ARG

GLN

LEU

ILE

SER

LYS

ASP

LEU

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HCACO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_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

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
AlphaFold	P41236