BMRB Entry 51070

Name: PRC1_DD
Published: 2022-06-24

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51070

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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:

PRC1_DD

Deposition date:

2021-08-26

Original release date:

2022-06-24

Authors:

Tan, Fei

Citation:

Citation: Tan, Fei; Xu, Jin. "Validation of the solution structure of dimerization domain of PRC1" PLoS One 17, e0270572-e0270572 (2022).
PubMed: 35930764

Assembly members:

Assembly members:
entity_1, polymer, 67 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: Pet21A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MRRSEVLAEESIVCLQKALN HLREIWELIGIPEDQRLQRT EVVKKHIKELLDMMIAEEES LKERLEH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	316
15N chemical shifts	68
1H chemical shifts	517

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Prc1 N terminal domain (aa:1-65), chain 1	1
2	Prc1 N terminal domain (aa:1-65), chain 2	1

Entities:

Entity 1, Prc1 N terminal domain (aa:1-65), chain 1 67 residues - Formula weight is not available

1

MET

ARG

SER

GLU

VAL

LEU

ALA

GLU

2

SER

ILE

VAL

CYS

LEU

GLN

LYS

ALA

LEU

ASN

3

HIS

LEU

ARG

GLU

ILE

TRP

GLU

LEU

ILE

GLY

4

ILE

PRO

GLU

ASP

GLN

ARG

LEU

GLN

ARG

THR

5

GLU

VAL

LYS

HIS

ILE

LYS

GLU

LEU

6

LEU

ASP

MET

ILE

ALA

GLU

SER

7

LEU

LYS

GLU

ARG

LEU

GLU

HIS

Samples:

sample_1: PRC1_DD, [U-100% 13C; U-100% 15N], 0.75 mM; PRC1_DD, [U-95% 15N], 0.75 mM; phosphate 50 mM; NaCl 150 mM; DTT 5 mM

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HMQC	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

CANDID - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 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