BMRB Entry 25565

Name: Solution structure of the BCOR PUFD
Published: 2016-04-04

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PDB ID: 2n1l
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25565
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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:

Solution structure of the BCOR PUFD

Deposition date:

2015-04-06

Original release date:

2016-04-04

Authors:

Wong, Sarah; Gearhart, Micah; Ha, Daniel; Corcoran, Connie; Diaz, Victoria; Taylor, Alexander; Schirf, Virgil; Ilangovan, Udayar; Hinck, Andrew; Demeler, Borries; Hart, P; Bardwell, Vivian; Kim, Chongwoo

Citation:

Citation: Wong, Sarah; Gearhart, Micah; Ha, Daniel; Corcoran, Connie; Diaz, Victoria; Taylor, Alexander; Schirf, Virgil; Ilangovan, Udayar; Hinck, Andrew; Demeler, Borries; Hart, John; Bardwell, Vivian; Kim, Chongwoo. "Structural basis for the hierarchical assembly of the core of PRC1.1" .

Assembly members:

Assembly members:
BCOR_PUFD, polymer, 115 residues, 13112.839 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: pET-30a, pET-3c, pCDF-Duet-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BCOR_PUFD: SDVFEFEFSETPLLPSYNIQ VSVAQGPRNWLLLSDVLKKL KMSSRIFRSNFPNVEIVTIA EAEFYRQVSASLLFSSSKDL EAFNPESKELLDLVEFTNEI QTLLGSSVEWLHPSD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	446
15N chemical shifts	102
1H chemical shifts	690

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 115 residues - 13112.839 Da.

1

SER

ASP

VAL

PHE

GLU

PHE

GLU

PHE

SER

GLU

2

THR

PRO

LEU

PRO

SER

TYR

ASN

ILE

GLN

3

VAL

SER

VAL

ALA

GLN

GLY

PRO

ARG

ASN

TRP

4

LEU

SER

ASP

VAL

LEU

LYS

LEU

5

LYS

MET

SER

ARG

ILE

PHE

ARG

SER

ASN

6

PHE

PRO

ASN

VAL

GLU

ILE

VAL

THR

ILE

ALA

7

GLU

ALA

GLU

PHE

TYR

ARG

GLN

VAL

SER

ALA

8

SER

LEU

PHE

SER

LYS

ASP

LEU

9

GLU

ALA

PHE

ASN

PRO

GLU

SER

LYS

GLU

LEU

10

LEU

ASP

LEU

VAL

GLU

PHE

THR

ASN

GLU

ILE

11

GLN

THR

LEU

GLY

SER

VAL

GLU

TRP

12

LEU

HIS

PRO

SER

ASP

Samples:

sample_1: entity, [U-13C; U-15N], 3 mM; TRIS 10 mM; sodium chloride 50 mM; TCEP 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 30 mM; pH: 8; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, chemical shift calculation, data analysis

TOPSPIN, Bruker Biospin - collection

ARIA, Linge, O'Donoghue and Nilges - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 600 MHz

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