BMRB Entry 51475

Name: 53BP1 1140-1225
Published: 2022-12-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51475

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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:

53BP1 1140-1225

Deposition date:

2022-05-26

Original release date:

2022-12-12

Authors:

Howe, Jesse; Weeks, Austin; Reardon, Patrick; Barbar, Elisar

Citation:

Citation: Howe, Jesse; Weeks, Austin; Reardon, Patrick; Barbar, Elisar. "Multivalent binding of the hub protein LC8 at a newly discovered site in 53BP1" Biophys. J. 121, 4433-4442 (2022).
PubMed: 36335430

Assembly members:

Assembly members:
entity_1, polymer, 89 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET24d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAHSKALIERPSQNNIGIQT MESSLRVPETVSAATQTIKN VSEQGTSTVDQNFGKQDATV QTERGSGEKPVSAPGDDTES LHSQGEEEF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	207
15N chemical shifts	73
1H chemical shifts	73

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	53BP1	1

Entities:

Entity 1, 53BP1 89 residues - Formula weight is not available

1

GLY

ALA

HIS

SER

LYS

ALA

LEU

ILE

GLU

ARG

2

PRO

SER

GLN

ASN

ILE

GLY

ILE

GLN

THR

3

MET

GLU

SER

LEU

ARG

VAL

PRO

GLU

THR

4

VAL

SER

ALA

THR

GLN

THR

ILE

LYS

ASN

5

VAL

SER

GLU

GLN

GLY

THR

SER

THR

VAL

ASP

6

GLN

ASN

PHE

GLY

LYS

GLN

ASP

ALA

THR

VAL

7

GLN

THR

GLU

ARG

GLY

SER

GLY

GLU

LYS

PRO

8

VAL

SER

ALA

PRO

GLY

ASP

THR

GLU

SER

9

LEU

HIS

SER

GLN

GLY

GLU

PHE

Samples:

sample_1: 53BP1, [U-100% 15N], 200 uM

sample_conditions_1: ionic strength: 0.070 M; pH: 6.5; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

NMRViewJ - chemical shift assignment

NMRPipe - processing

TOPSPIN - collection

NMR spectrometers:

Bruker AVANCE III HD 800 MHz MHz

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