BMRB Entry 18134

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18134
MolProbity Validation Chart

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Title:
SOLUTION STRUCTURE OF THE FIRST SAM DOMAIN OF ODIN
Deposition date:
2011-12-12
Original release date:
2012-01-25
Authors:
Leone, Marilisa; Mercurio, Flavia
Citation:

Citation: Mercurio, Flavia Anna; Marasco, Daniela; Pirone, Luciano; Pedone, Emilia Maria; Pellecchia, Maurizio; Leone, Marilisa. "Solution structure of the first Sam domain of Odin and binding studies with the EphA2 receptor."  Biochemistry 51, 2136-2145 (2012).
PubMed: 22332920

Assembly members:

Assembly members:
entity, polymer, 101 residues, 11308.773 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   Vector: PET15B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MGSSHHHHHHSSGLVPRGSH MISGLRTLEQSVGEWLESIG LQQYESKLLLNGFDDVHFLG SNVMEEQDLRDIGISDPQHR RKLLQAARSLPKVKALGYDG N

Data sets:
Data typeCount
13C chemical shifts244
15N chemical shifts81
1H chemical shifts554

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FIRST SAM DOMAIN OF ODIN1

Entities:

Entity 1, FIRST SAM DOMAIN OF ODIN 101 residues - 11308.773 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METILESERGLYLEUARGTHRLEUGLUGLN
4   SERVALGLYGLUTRPLEUGLUSERILEGLY
5   LEUGLNGLNTYRGLUSERLYSLEULEULEU
6   ASNGLYPHEASPASPVALHISPHELEUGLY
7   SERASNVALMETGLUGLUGLNASPLEUARG
8   ASPILEGLYILESERASPPROGLNHISARG
9   ARGLYSLEULEUGLNALAALAARGSERLEU
10   PROLYSVALLYSALALEUGLYTYRASPGLY
11   ASN

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 0.9 – 1 mM; potassium chloride 2.7 mM; potassium phosphate 1.8 mM; sodium chloride 140 mM; sodium phosphate 10 mM; sodium azide 0.2%; H2O 95%; D2O, 99%, 5%

sample_2: entity0.9 – 1 mM; potassium chloride 2.7 mM; potassium phosphate 1.8 mM; sodium chloride 140 mM; sodium phosphate 10 mM; sodium azide 0.2%; D2O, 99%, 100%

sample_conditions_1: ionic strength: 0.2 M; pH: 7.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

VNMRJ, Varian - collection, processing

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

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

NMR spectrometers:

  • Varian Unity 600 MHz

Related Database Links:

PDB
DBJ BAA13218 BAG11153
GB AAH31934 AAI32833 EAX03800 EAX03803 EAX03804
REF NP_056060 XP_001111692 XP_003897533 XP_004043913 XP_005249021
SP Q92625
AlphaFold Q92625

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