BMRB Entry 51513

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51513

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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:

Backbone 1H, 13C and 15N chemical shift assignments, experimental 3JHN-HA scalar couplings, and 15N-relaxation rates of the C-terminal portion of human CHMP4B (residues 121-224)

Deposition date:

2022-07-11

Original release date:

2023-06-06

Authors:

Elias, Ruben; Deshmukh, Lalit

Citation:

Citation: Elias, Ruben; Zu, Yingqi; Su, Qi; Ghirlando, Rodolfo; Zhang, Jin; Deshmukh, Lalit. "Reversible phase separation of ESCRT protein ALIX through tyrosine phosphorylation" Sci. Adv. 9, eadg3913-eadg3913 (2023).
PubMed: 37450591

Assembly members:

Assembly members:
entity_1, polymer, 106 residues, 11852 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: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSDNMDIDKVDELMQDIADQ QELAEEISTAISKPVGFGEE FDEDELMAELEELEQEELDK NLLEICGPETVPLPNVPSIA LPSKPAKKKEEEDDDMKELE NWAGSM

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
coupling_constants
- coupling_constant_list_1
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1

Data type	Count
13C chemical shifts	392
15N chemical shifts	95
1H chemical shifts	314
T1 relaxation values	95
T2 relaxation values	95
coupling constants	89

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Human CHMP4B	1

Entities:

Entity 1, Human CHMP4B 106 residues - 11852 Da.

1

GLY

SER

ASP

ASN

MET

ASP

ILE

ASP

LYS

VAL

2

ASP

GLU

LEU

MET

GLN

ASP

ILE

ALA

ASP

GLN

3

GLN

GLU

LEU

ALA

GLU

ILE

SER

THR

ALA

4

ILE

SER

LYS

PRO

VAL

GLY

PHE

GLY

GLU

5

PHE

ASP

GLU

ASP

GLU

LEU

MET

ALA

GLU

LEU

6

GLU

LEU

GLU

GLN

GLU

LEU

ASP

LYS

7

ASN

LEU

GLU

ILE

CYS

GLY

PRO

GLU

THR

8

VAL

PRO

LEU

PRO

ASN

VAL

PRO

SER

ILE

ALA

9

LEU

PRO

SER

LYS

PRO

ALA

LYS

GLU

10

GLU

ASP

MET

LYS

GLU

LEU

GLU

11

ASN

TRP

ALA

GLY

SER

MET

Samples:

sample_1: Human CHMP4B, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; D2O 7%; EDTA 2 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0 M; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 800 MHz
Bruker Avance 600 MHz

UNP	Q9H444
AlphaFold	Q53ZD6