BMRB Entry 18198

Name: Chemical Shift Assignment of the PP1 Binding Domain of NIPP1
Published: 2012-09-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18198

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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:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NIPP1: GAMGASGGEDDELKGLLGLP EEETELDNLTEFNTAHNKRI STLTIEEGNLDIQRPKRKRK NSRVTFSEDDEIINPEDVDP SVGRFRNM

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	167
15N chemical shifts	81
1H chemical shifts	81

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PP1 binding domain	1

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

GLY

ALA

MET

GLY

ALA

SER

GLY

GLU

ASP

2

ASP

GLU

LEU

LYS

GLY

LEU

GLY

LEU

PRO

3

GLU

THR

GLU

LEU

ASP

ASN

LEU

THR

4

GLU

PHE

ASN

THR

ALA

HIS

ASN

LYS

ARG

ILE

5

SER

THR

LEU

THR

ILE

GLU

GLY

ASN

LEU

6

ASP

ILE

GLN

ARG

PRO

LYS

ARG

LYS

ARG

LYS

7

ASN

SER

ARG

VAL

THR

PHE

SER

GLU

ASP

8

GLU

ILE

ASN

PRO

GLU

ASP

VAL

ASP

PRO

9

SER

VAL

GLY

ARG

PHE

ARG

ASN

MET

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:

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

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	Q12972 Q28147 Q8R3G1