BMRB Entry 7118

Title:
Solution structure of neurabin SAM domain
Deposition date:
2006-05-17
Original release date:
2007-09-24
Authors:
Ju, Tingting; Peti, Wolfgang
Citation:

Citation: Ju, Tingting; Ragusa, M.J.; Hudak, J.; Nairn, A.C.; Peti, Wolfgang. "Structural characterization of the neurabin sterile alpha motif domain"  Proteins 69, 192-198 (2007).
PubMed: 17600833

Assembly members:

Assembly members:
Neurabin SAM domain, polymer, 74 residues, 8341.6 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts303
15N chemical shifts83
1H chemical shifts530

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Neurabin SAM domain monomer1

Entities:

Entity 1, Neurabin SAM domain monomer 74 residues - 8341.6 Da.

1   GLYHISMETVALHISGLUTRPSERVALGLN
2   GLNVALSERHISTRPLEUVALGLYLEUSER
3   LEUASPGLNTYRVALSERGLUPHESERALA
4   GLNASNILESERGLYGLUGLNLEULEUGLN
5   LEUASPGLYASNLYSLEULYSALALEUGLY
6   METTHRSERSERGLNASPARGALALEUVAL
7   LYSLYSLYSLEULYSGLUMETLYSMETSER
8   LEUGLULYSALA

Samples:

sample_1: Neurabin SAM domain, [U-95% 13C; U-99% 15N], 1.5 ± 0.1 mM; NaPi 20 mM; NaCl 50 mM; D2O 100%

sample_2: Neurabin SAM domain, [U-99% 15N], 1.5 ± 0.1 mM; NaPi 20 mM; NaCl 50 mM; D2O 100%

sample_3: Neurabin SAM domain 1.5 ± 0.1 mM; NaPi 20 mM; NaCl 50 mM; D2O 100%

conditions_1: pH: 6.8; temperature: 298 K

conditions_2: pH: 6.8; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
15N_edited_NOESYsample_2not availableconditions_1
13C_edited_NOESYsample_1not availableconditions_1
2D_NOESYsample_3not availableconditions_2

Software:

TOPSPIN v1.3, Bruker - data acquisition and processing

CARA v1.5, . - Data analysis

ATNOS v1.1, . - automated peak assignments

CYANA v2.0, LAS - structure calculation

CNS v1.1, . - structure refinement

NMR spectrometers:

  • Bruker AVANCE II 500 MHz

Related Database Links:

PDB
GB AAC53454 EDM15014 EDM15015 EDM15016
REF NP_445925 XP_006236119 XP_006236120 XP_006236123 XP_006236125
SP O35867
AlphaFold O35867

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