BMRB Entry 51132

Name: 1H, 15N and 13C sequence-specific backbone assignment of RRP1B PP1 binding domain
Published: 2022-12-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51132

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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:

1H, 15N and 13C sequence-specific backbone assignment of RRP1B PP1 binding domain

Deposition date:

2021-10-11

Original release date:

2022-12-20

Authors:

Bajaj, Rakhi; Senthil Kumar, Ganesan; Page, Rebecca; Peti, Wolfgang

Citation:

Citation: Srivastava, Gautam; Bajaj, Rakhi; Kumar, Ganesan Senthil; Gaudreau-Lapierre, Antoine; Nicolas, Hannah; Chamousset, Delphine; Kreitler, Dale; Peti, Wolfgang; Trinkle-Mulcahy, Laura; Page, Rebecca. "The ribosomal RNA processing 1B:protein phosphatase 1 holoenzyme reveals non-canonical PP1 interaction motifs" Cell Rep. 41, 111726-111726 (2022).
PubMed: 36450254

Assembly members:

Assembly members:
entity_1, polymer, 105 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: RP1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMRRAKSSTATHPPGPAVQ LNKTPSSSKKVTFGLNRNMT AEFKKTDKSILVSPTGPSRV AFDPEQKPLHGVLKTPTSSP ASSPLVAKKPLTTTPRRRPR AMDFF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	280
15N chemical shifts	83
1H chemical shifts	83

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRP1B	1

Entities:

Entity 1, RRP1B 105 residues - Formula weight is not available

GHM cloning artefact

1

GLY

HIS

MET

ARG

ALA

LYS

SER

THR

2

ALA

THR

HIS

PRO

GLY

PRO

ALA

VAL

GLN

3

LEU

ASN

LYS

THR

PRO

SER

LYS

4

VAL

THR

PHE

GLY

LEU

ASN

ARG

ASN

MET

THR

5

ALA

GLU

PHE

LYS

THR

ASP

LYS

SER

ILE

6

LEU

VAL

SER

PRO

THR

GLY

PRO

SER

ARG

VAL

7

ALA

PHE

ASP

PRO

GLU

GLN

LYS

PRO

LEU

HIS

8

GLY

VAL

LEU

LYS

THR

PRO

THR

SER

PRO

9

ALA

SER

PRO

LEU

VAL

ALA

LYS

PRO

10

LEU

THR

PRO

ARG

PRO

ARG

11

ALA

MET

ASP

PHE

Samples:

sample_1: RRP1B, [U-99% 13C; U-99% 15N], 0.6 mM; RRP1B, [U-99% 15N], 0.6 mM; Bis-Tris 20 mM; NaCl 0.15 M; TCEP 0.5 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.8; 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_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D (H)CC(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CARA - chemical shift assignment

TOPSPIN - collection, processing

NMR spectrometers:

Bruker AVANCE III 850 MHz
Bruker Avance 500 MHz

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