BMRB Entry 51514

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51514

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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 CHMP4C (residues 121-233)

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, 115 residues, 12975 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: GSENMDLNKIDDLMQEITEQ QDIAQEISEAFSQRVGFGDD FDEDELMAELEELEQEELNK KMTNIRLPNVPSCSLPAQPN RKPGMSSTARRSRAASSQRA EEEDDDIKQLAAWAT

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	429
15N chemical shifts	105
1H chemical shifts	375
T1 relaxation values	101
T2 relaxation values	101
coupling constants	100

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Human CHMP4C	1

Entities:

Entity 1, Human CHMP4C 115 residues - 12975 Da.

1

GLY

SER

GLU

ASN

MET

ASP

LEU

ASN

LYS

ILE

2

ASP

LEU

MET

GLN

GLU

ILE

THR

GLU

GLN

3

GLN

ASP

ILE

ALA

GLN

GLU

ILE

SER

GLU

ALA

4

PHE

SER

GLN

ARG

VAL

GLY

PHE

GLY

ASP

5

PHE

ASP

GLU

ASP

GLU

LEU

MET

ALA

GLU

LEU

6

GLU

LEU

GLU

GLN

GLU

LEU

ASN

LYS

7

LYS

MET

THR

ASN

ILE

ARG

LEU

PRO

ASN

VAL

8

PRO

SER

CYS

SER

LEU

PRO

ALA

GLN

PRO

ASN

9

ARG

LYS

PRO

GLY

MET

SER

THR

ALA

ARG

10

ARG

SER

ARG

ALA

SER

GLN

ARG

ALA

11

GLU

ASP

ILE

LYS

GLN

LEU

12

ALA

TRP

ALA

THR

Samples:

sample_1: Human CHMP4C, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; EDTA 2 mM; TCEP 1 mM; D2O 7%

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 C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

CcpNMR - data analysis

NMR spectrometers:

Bruker AVANCE NEO 800 MHz
Bruker AVANCE 600 MHz

UNP	Q96CF2
AlphaFold	B2RBZ1