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Biological Magnetic Resonance Data Bank


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BMRB Entry 34285

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

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Title: Solution structure of the capsid domain from the activity-regulated cytoskeleton-associated protein, Arc   PubMed: 31080121

Deposition date: 2018-06-14 Original release date: 2019-05-17

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

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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts615
15N chemical shifts150
1H chemical shifts917

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 159 residues - 18996.312 Da.

1   SERPROGLYLEUASPTHRGLNILEPHEGLU
2   ASPPROARGGLUPHELEUSERHISLEUGLU
3   GLUTYRLEUARGGLNVALGLYGLYSERGLU
4   GLUTYRTRPLEUSERGLNILEGLNASNHIS
5   METASNGLYPROALALYSLYSTRPTRPGLU
6   PHELYSGLNGLYSERVALLYSASNTRPVAL
7   GLUPHELYSLYSGLUPHELEUGLNTYRSER
8   GLUGLYTHRLEUSERARGGLUALAILEGLN
9   ARGGLULEUASPLEUPROGLNLYSGLNGLY
10   GLUPROLEUASPGLNPHELEUTRPARGLYS
11   ARGASPLEUTYRGLNTHRLEUTYRVALASP
12   ALAGLUGLUGLUGLUILEILEGLNTYRVAL
13   VALGLYTHRLEUGLNPROLYSPHELYSARG
14   PHELEUARGHISPROLEUPROLYSTHRLEU
15   GLUGLNLEUILEGLNARGGLYMETGLUVAL
16   GLNASPGLYLEUGLUGLNALAALAGLU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-13C TOCSY aromaticsample_2isotropicsample_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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts