BMRB Entry 25395

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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/BMR25395
MolProbity Validation Chart

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Title:
Solution structure of the internal EH domain of gamma-synergin
Deposition date:
2014-12-16
Original release date:
2015-12-28
Authors:
Kovermann, Michael; Weininger, Ulrich; Loew, Christian
Citation:

Citation: Kovermann, Michael; Weininger, Ulrich; Loew, Christian. "Solution structure of the internal EH domain of gamma-synergin"  .

Assembly members:

Assembly members:
entity, polymer, 112 residues, 12294.373 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: not applicable

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: SMFPSQDPAQPRMPPWIYNE SLVPDAYKKILETTMTPTGI DTAKLYPILMSSGLPRETLG QIWALANRTTPGKLTKEELY TVLAMIAVTQRGVPAMSPDA LNQFPAAPIPTL

Data sets:
Data typeCount
13C chemical shifts382
15N chemical shifts86
1H chemical shifts776

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 112 residues - 12294.373 Da.

1   SERMETPHEPROSERGLNASPPROALAGLN
2   PROARGMETPROPROTRPILETYRASNGLU
3   SERLEUVALPROASPALATYRLYSLYSILE
4   LEUGLUTHRTHRMETTHRPROTHRGLYILE
5   ASPTHRALALYSLEUTYRPROILELEUMET
6   SERSERGLYLEUPROARGGLUTHRLEUGLY
7   GLNILETRPALALEUALAASNARGTHRTHR
8   PROGLYLYSLEUTHRLYSGLUGLULEUTYR
9   THRVALLEUALAMETILEALAVALTHRGLN
10   ARGGLYVALPROALAMETSERPROASPALA
11   LEUASNGLNPHEPROALAALAPROILEPRO
12   THRLEU

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 1 mM; TRIS 20 mM; sodium chloride 100 mM; calcium chloride 2 mM

sample_conditions_1: pH: 7.5; 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_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC IPAPsample_1anisotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Johnson, One Moon Scientific, Linge, O'Donoghue and Nilges - chemical shift assignment, collection, peak picking, processing, structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 850 MHz

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