BMRB Entry 15554

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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/BMR15554
MolProbity Validation Chart

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Title:
Structure and Chemical Shift Assignment for the Eps15EH2-Stonin2 complex
Deposition date:
2007-11-12
Original release date:
2008-01-10
Authors:
Rumpf, Julia; Simon, Bernd; Jung, Nadja; Maritzen, Tanja; Haucke, Volker; Sattler, Michael; Groemping, Yvonne
Citation:

Citation: Rumpf, Julia; Simon, Bernd; Groemping, Yvonne; Sattler, Michael. "1H, 13C, and 15N chemical shift assignments for the Eps15-EH2-stonin 2 complex"  Biomol. NMR Assignments 2, 55-58 (2008).
PubMed: 19636924

Assembly members:

Assembly members:
EH2, polymer, 100 residues, 10985.906 Da.
Stonin_peptide, polymer, 45 residues, 4998.502 Da.
CA, non-polymer, 40.078 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: pGEX6P1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EH2: GPLGSPWAVKPEDKAKYDAI FDSLSPVNGFLSGDKVKPVL LNSKLPVDILGRVWELSDID HDGMLDRDEFAVAMFLVYCA LEKEPVPMSLPPALVPPSKR
Stonin_peptide: GPLGSPSVTEASPWRATNPF LNETLQDVQPSPINPFSAFF EEQER

Data sets:
Data typeCount
13C chemical shifts483
15N chemical shifts130
1H chemical shifts996

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EH21
2Stonin2
3CA3

Entities:

Entity 1, EH2 100 residues - 10985.906 Da.

residues 1-5 (GPLGS) in NMR structure calculations originate from the expression vector

1   GLYPROLEUGLYSERPROTRPALAVALLYS
2   PROGLUASPLYSALALYSTYRASPALAILE
3   PHEASPSERLEUSERPROVALASNGLYPHE
4   LEUSERGLYASPLYSVALLYSPROVALLEU
5   LEUASNSERLYSLEUPROVALASPILELEU
6   GLYARGVALTRPGLULEUSERASPILEASP
7   HISASPGLYMETLEUASPARGASPGLUPHE
8   ALAVALALAMETPHELEUVALTYRCYSALA
9   LEUGLULYSGLUPROVALPROMETSERLEU
10   PROPROALALEUVALPROPROSERLYSARG

Entity 2, Stonin 45 residues - 4998.502 Da.

residues 101-105 in NMR structure calculations originate from the expression vector

1   GLYPROLEUGLYSERPROSERVALTHRGLU
2   ALASERPROTRPARGALATHRASNPROPHE
3   LEUASNGLUTHRLEUGLNASPVALGLNPRO
4   SERPROILEASNPROPHESERALAPHEPHE
5   GLUGLUGLNGLUARG

Entity 3, CA - Ca - 40.078 Da.

1   CA

Samples:

sample_1: EH2, [U-99% 13C; U-99% 15N], 0.5-1 mM; Stonin peptide 0.5-1 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM

sample_2: EH2 0.5-1 mM; Stonin peptide, [U-99% 13C; U-99% 15N], 0.5-1 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM

sample_3: EH2, [U-99% 13C; U-99% 15N], 0.5-1 mM; Stonin peptide 0.5-1 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM

sample_4: EH2 0.5-1 mM; Stonin peptide, [U-99% 13C; U-99% 15N], 0.5-1 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM

sample_5: EH2 0.6 mM; Stonin peptide 0.6 mM; CA 2 mM; perdeuterated Tris 10 mM; NaCl 100 mM; CaCl2 2 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_5isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1

Software:

NMRView v5.0.4, Johnson, One Moon Scientific - chemical shift assignment

TOPSPIN v1.3, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

BMRB 4184
PDB
GB ELK26712 AAH69359 AAK57558 AAL47008
REF NP_001243359 NP_149095 XP_002825044 XP_004624764 XP_005390296
SP Q8WXE9
AlphaFold Q8WXE9

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