BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19109

Title: Chemical Shift Assignments of the C-terminal Eps15 Homology Domain-3 EH Domain   PubMed: 23754701

Deposition date: 2013-03-22 Original release date: 2013-08-15

Authors: Spagnol, Gaelle; Reiling, Calliste; Kieken, Fabien; Caplan, Steve; Sorgen, Paul

Citation: Spagnol, Gaelle; Reiling, Calliste; Kieken, Fabien; Caplan, Steve; Sorgen, Paul. "Chemical shift assignments of the C-terminal Eps15 homology domain-3 EH domain."  Biomol. NMR Assignments ., .-. (2013).

Assembly members:
EHD3_EH, polymer, 108 residues, 11932.7 Da.
entity_CA, non-polymer, 40.078 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
EHD3_EH: GPLGSGIDDAEWVVARDKPM YDEIFYTLSPVDGKITGANA KKEMVRSKLPNSVLGKIWKL ADIDKDGMLDDDEFALANHL IKVKLEGHELPNELPAHLLP PSKRKVAE

Data sets:
Data typeCount
13C chemical shifts462
15N chemical shifts101
1H chemical shifts773

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1EHD3 EH1
2Calcium2

Entities:

Entity 1, EHD3 EH 108 residues - 11932.7 Da.

Residues 1-5 represent a non-native linker

1   GLYPROLEUGLYSERGLYILEASPASPALA
2   GLUTRPVALVALALAARGASPLYSPROMET
3   TYRASPGLUILEPHETYRTHRLEUSERPRO
4   VALASPGLYLYSILETHRGLYALAASNALA
5   LYSLYSGLUMETVALARGSERLYSLEUPRO
6   ASNSERVALLEUGLYLYSILETRPLYSLEU
7   ALAASPILEASPLYSASPGLYMETLEUASP
8   ASPASPGLUPHEALALEUALAASNHISLEU
9   ILELYSVALLYSLEUGLUGLYHISGLULEU
10   PROASNGLULEUPROALAHISLEULEUPRO
11   PROSERLYSARGLYSVALALAGLU

Entity 2, Calcium - Ca - 40.078 Da.

1   CA

Samples:

sample_1: EHD3 EH, [U-98% 13C; U-98% 15N], 1 mM; TRIS 20 mM; potassium chloride 100 mM; calcium chloride 10 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

NMRView v5.2.2.01 -

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

DBJ BAI45522
EMBL CAH90161 CAH90891
GB AAF32285 AAI56224 AAI56997 AAM14604 EAX00480
REF NP_001125048 NP_001244659 NP_055415 NP_620245 XP_001918139
SP Q8R491 Q9NZN3

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts