BMRB Entry 34285

Name: Solution structure of the capsid domain from the activity-regulated cytoskeleton-associated protein, Arc
Published: 2019-05-17

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PDB ID: 6gse
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34285
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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:

Solution structure of the capsid domain from the activity-regulated cytoskeleton-associated protein, Arc

Deposition date:

2018-06-14

Original release date:

2019-05-17

Authors:

Nielsen, L.; Erlendsson, S.; Teilum, K.

Citation:

Citation: Nielsen, L.; Pedersen, C.; Erlendsson, S.; Teilum, K.. "The Capsid Domain of Arc Changes Its Oligomerization Propensity through Direct Interaction with the NMDA Receptor" Structure 27, 1071-1081 (2019).
PubMed: 31080121

Assembly members:

Assembly members:
entity_1, polymer, 159 residues, 18996.312 Da.

Natural source:

Natural source: Common Name: Norway Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SPGLDTQIFEDPREFLSHLE EYLRQVGGSEEYWLSQIQNH MNGPAKKWWEFKQGSVKNWV EFKKEFLQYSEGTLSREAIQ RELDLPQKQGEPLDQFLWRK RDLYQTLYVDAEEEEIIQYV VGTLQPKFKRFLRHPLPKTL EQLIQRGMEVQDGLEQAAE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	615
15N chemical shifts	150
1H chemical shifts	917

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 159 residues - 18996.312 Da.

1

SER

PRO

GLY

LEU

ASP

THR

GLN

ILE

PHE

GLU

2

ASP

PRO

ARG

GLU

PHE

LEU

SER

HIS

LEU

GLU

3

GLU

TYR

LEU

ARG

GLN

VAL

GLY

SER

GLU

4

GLU

TYR

TRP

LEU

SER

GLN

ILE

GLN

ASN

HIS

5

MET

ASN

GLY

PRO

ALA

LYS

TRP

GLU

6

PHE

LYS

GLN

GLY

SER

VAL

LYS

ASN

TRP

VAL

7

GLU

PHE

LYS

GLU

PHE

LEU

GLN

TYR

SER

8

GLU

GLY

THR

LEU

SER

ARG

GLU

ALA

ILE

GLN

9

ARG

GLU

LEU

ASP

LEU

PRO

GLN

LYS

GLN

GLY

10

GLU

PRO

LEU

ASP

GLN

PHE

LEU

TRP

ARG

LYS

11

ARG

ASP

LEU

TYR

GLN

THR

LEU

TYR

VAL

ASP

12

ALA

GLU

ILE

GLN

TYR

VAL

13

VAL

GLY

THR

LEU

GLN

PRO

LYS

PHE

LYS

ARG

14

PHE

LEU

ARG

HIS

PRO

LEU

PRO

LYS

THR

LEU

15

GLU

GLN

LEU

ILE

GLN

ARG

GLY

MET

GLU

VAL

16

GLN

ASP

GLY

LEU

GLU

GLN

ALA

GLU

Samples:

sample_1: Arc, [U-15N], 0.5 mM

sample_2: Arc, [U-13C; U-15N], 1 mM

sample_3: Arc, [U-15N], 0.5 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 bar; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C TOCSY aromatic	sample_2	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

Analysis, CCPN - chemical shift assignment

NMR spectrometers:

Bruker AvanceIII 750 MHz
Agilent DD2 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks