BMRB Entry 50117

Name: UN2A
Published: 2021-03-18

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PDB ID: 7nip
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50117
MolProbity Validation Chart

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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:

UN2A

Deposition date:

2019-12-06

Original release date:

2021-03-18

Authors:

Zhou, Tiankun

Citation:

Citation: Zhou, Tiankun; Fleming, Jennifer; Lange, Stephan; Hessel, Anthony; Bogomolovas, Julius; Stronczek, Chiara; Grundei, David; Ghassemian, Majid; Biju, Andrea; Borgeson, Emma; Bullard, Belinda; Linke, Wolfgang; Chen, Ju; Kovermann, Michael; Mayans, Olga. "Molecular Characterisation of Titin N2A and Its Binding of CARP Reveals a Titin/Actin Cross-linking Mechanism" J. Mol. Biol. 433, 166901-166901 (2021).
PubMed: 33647290

Assembly members:

Assembly members:
entity_1, polymer, 111 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-Trx-1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MDERKKQEKIEGDLRAMLKK TPILKKGAGEEEEIDIMELL KNVDPKEYEKYARMYGITDF RGLLQAFELLKQSQEEETHR LEIEEIERSERDEKEFEELV SFIQQRLSQTE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	253
15N chemical shifts	75
1H chemical shifts	75

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UN2A	1

Entities:

Entity 1, UN2A 111 residues - Formula weight is not available

1

MET

ASP

GLU

ARG

LYS

GLN

GLU

LYS

ILE

2

GLU

GLY

ASP

LEU

ARG

ALA

MET

LEU

LYS

3

THR

PRO

ILE

LEU

LYS

GLY

ALA

GLY

GLU

4

GLU

ILE

ASP

ILE

MET

GLU

LEU

5

LYS

ASN

VAL

ASP

PRO

LYS

GLU

TYR

GLU

LYS

6

TYR

ALA

ARG

MET

TYR

GLY

ILE

THR

ASP

PHE

7

ARG

GLY

LEU

GLN

ALA

PHE

GLU

LEU

8

LYS

GLN

SER

GLN

GLU

THR

HIS

ARG

9

LEU

GLU

ILE

GLU

ILE

GLU

ARG

SER

GLU

10

ARG

ASP

GLU

LYS

GLU

PHE

GLU

LEU

VAL

11

SER

PHE

ILE

GLN

ARG

LEU

SER

GLN

THR

12

GLU

Samples:

sample_1: UN2A, [U-13C; U-15N; U-2H], 1.2 mM; sodium phosphate 30 mM; sodium chloride 100 mM

sample_conditions_1: pH: 7.5; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRViewJ, Johnson, One Moon Scientific - chemical shift assignment

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

NMR spectrometers:

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