BMRB Entry 36342

Click here to enlarge.

PDB ID:
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

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:
Data typeCount
13C chemical shifts694
15N chemical shifts170
1H chemical shifts1097

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 164 residues - 18637.480 Da.

1   LEUPROGLUGLNVALALAPROGLUSERARG
2   ASNARGILEARGVALARGGLNASPLEUALA
3   SERLEUPROALAGLULEUILEASNGLNILE
4   GLYASNARGCYSHISPROLYSLEUTYRASP
5   GLUGLYASPPROSERGLULYSLEUGLULEU
6   VALTHRGLYTHRASNVALTYRILETHRARG
7   ALAGLNLEUMETASNCYSHISVALSERALA
8   GLYTHRARGHISLYSVALLEULEUARGARG
9   LEULEUALASERPHEPHEASPARGASNTHR
10   LEUALAASNSERCYSGLYTHRGLYILEARG
11   SERSERTHRASNASPPROARGARGLYSPRO
12   LEUASPSERARGVALLEUHISALAVALLYS
13   TYRTYRCYSGLNASNPHEALAPROASNPHE
14   LYSGLUSERGLUMETASNALAILEALAALA
15   ASPMETCYSTHRASNALAARGARGVALVAL
16   ARGLYSSERTRPMETPROLYSVALLYSVAL
17   LEULYSALAGLU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_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