BMRB Entry 52577

Name: Relaxation of PHDvC5HCH of NSD1
Published: 2024-08-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52577

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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:

Relaxation of PHDvC5HCH of NSD1

Deposition date:

2024-08-06

Original release date:

2024-08-08

Authors:

Berardi, Andrea; Quilici, Giacomo; Musco, Giovanna

Citation:

Citation: berardi, andrea; Leonie Kaestner, Charlotte; ghitti, michela; quilici, giacomo; cocomazzi, paolo; li, jianping; ballabio, federico; zucchelli, chiara; knapp, stefan; licht, jonathan; musco, giovanna. "The C-terminal PHDVC5HCH tandem domain of NSD2 is a combinatorial reader of unmodified H3K4 and tri-methylated H3K27 that regulates transcription of cell adhesion genes in multiple myeloma" Nucleic Acids Res. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 94 residues, Formula weight is not available
entity_ZN, non-polymer, 65.409 Da.

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet-M11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMEREDECFSCGDAGQLVS CKKPGCPKVYHADCLNLTKR PAGKWECPWHQCDVCGKEAA SFCEMCPSSFCKQHREGMLF ISKLDGRLSCTEHD

Data sets:

heteronucl_NOEs
- heteronucl_NOEs_1
heteronucl_T1_relaxation
- heteronucl_T1_relaxation_1
heteronucl_T2_relaxation
- heteronucl_T2_relaxation_1

Data type	Count
T1 relaxation values	79
T2 relaxation values	79
heteronuclear NOE values	80

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PHDCv5HCH domain of NSD1	1
2	ZINC ION, 1	2
3	ZINC ION, 2	2
4	ZINC ION, 3	2
5	ZINC ION, 4	2

Entities:

Entity 1, PHDCv5HCH domain of NSD1 94 residues - Formula weight is not available

The first three residues do not belong to the natural sequence

1

GLY

ALA

MET

GLU

ARG

GLU

ASP

GLU

CYS

PHE

2

SER

CYS

GLY

ASP

ALA

GLY

GLN

LEU

VAL

SER

3

CYS

LYS

PRO

GLY

CYS

PRO

LYS

VAL

TYR

4

HIS

ALA

ASP

CYS

LEU

ASN

LEU

THR

LYS

ARG

5

PRO

ALA

GLY

LYS

TRP

GLU

CYS

PRO

TRP

HIS

6

GLN

CYS

ASP

VAL

CYS

GLY

LYS

GLU

ALA

7

SER

PHE

CYS

GLU

MET

CYS

PRO

SER

PHE

8

CYS

LYS

GLN

HIS

ARG

GLU

GLY

MET

LEU

PHE

9

ILE

SER

LYS

LEU

ASP

GLY

ARG

LEU

SER

CYS

10

THR

GLU

HIS

ASP

Entity 2, ZINC ION, 1 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: PHDvC5HCH of NSD1, [U-99% 15N], 0.3 mM; ZnCl2 10 mM; NaH2PO4/Na2HPO4 20 mM; NaCl 150 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 170 mM; pH: 6.3; pressure: 1 atm; temperature: 295 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H-15N heteronoe	sample_1	isotropic	sample_conditions_1
T1/R1 relaxation	sample_1	isotropic	sample_conditions_1
T2/R2 relaxation	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.5 - data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz