BMRB Entry 36342

Name: The NMR structure of the BEN domain from human NAC1
Published: 2021-02-15

Click here to enlarge.

PDB ID: 7bv9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36342
MolProbity Validation Chart

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:

The NMR structure of the BEN domain from human NAC1

Deposition date:

2020-04-09

Original release date:

2021-02-15

Authors:

Nagata, T.; Kobayashi, N.; Nakayama, N.; Obayashi, E.; Urano, T.

Citation:

Citation: Nakayama, N.; Sakashita, G.; Nagata, T.; Kobayashi, N.; Yoshida, H.; Park, S.Y.; Murphy, L.; Nariai, Y.; Kato, H.; Obayashi, E.; Nakayama, K.; Kyo, S.; Urano, T.. "Nucleus Accumbens-Associated Protein 1 Binds DNA Directly through the BEN Domain in a Sequence-Specific Manner" Biomedicines 8, 608-608 (2020).
PubMed: 33327466

Assembly members:

Assembly members:
Nucleus accumbens-associated protein 1, polymer, 164 residues, 18637.480 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Nucleus accumbens-associated protein 1: LPEQVAPESRNRIRVRQDLA SLPAELINQIGNRCHPKLYD EGDPSEKLELVTGTNVYITR AQLMNCHVSAGTRHKVLLRR LLASFFDRNTLANSCGTGIR SSTNDPRRKPLDSRVLHAVK YYCQNFAPNFKESEMNAIAA DMCTNARRVVRKSWMPKVKV LKAE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	694
15N chemical shifts	170
1H chemical shifts	1097

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 164 residues - 18637.480 Da.

1

LEU

PRO

GLU

GLN

VAL

ALA

PRO

GLU

SER

ARG

2

ASN

ARG

ILE

ARG

VAL

ARG

GLN

ASP

LEU

ALA

3

SER

LEU

PRO

ALA

GLU

LEU

ILE

ASN

GLN

ILE

4

GLY

ASN

ARG

CYS

HIS

PRO

LYS

LEU

TYR

ASP

5

GLU

GLY

ASP

PRO

SER

GLU

LYS

LEU

GLU

LEU

6

VAL

THR

GLY

THR

ASN

VAL

TYR

ILE

THR

ARG

7

ALA

GLN

LEU

MET

ASN

CYS

HIS

VAL

SER

ALA

8

GLY

THR

ARG

HIS

LYS

VAL

LEU

ARG

9

LEU

ALA

SER

PHE

ASP

ARG

ASN

THR

10

LEU

ALA

ASN

SER

CYS

GLY

THR

GLY

ILE

ARG

11

SER

THR

ASN

ASP

PRO

ARG

LYS

PRO

12

LEU

ASP

SER

ARG

VAL

LEU

HIS

ALA

VAL

LYS

13

TYR

CYS

GLN

ASN

PHE

ALA

PRO

ASN

PHE

14

LYS

GLU

SER

GLU

MET

ASN

ALA

ILE

ALA

15

ASP

MET

CYS

THR

ASN

ALA

ARG

VAL

16

ARG

LYS

SER

TRP

MET

PRO

LYS

VAL

LYS

VAL

17

LEU

LYS

ALA

GLU

Samples:

sample_1: BEN domain, [U-13C; U-15N], 500 uM; sodium phosphate 20 mM; NaCl 50 mM; H2O 95%; D2O, [U-2H], 5%

sample_conditions_1: ionic strength: 70 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

Amber v12, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

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

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

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