BMRB Entry 16181

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16181
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Structure of the C-terminal domain of EHD1 with FNYESTGPFTAK
Deposition date:
2009-02-20
Original release date:
2009-10-16
Authors:
KIEKEN, Fabien; JOVIC, Marko; TONELLI, Marco; NASLAVSKY, Naava; CAPLAN, Steve; SORGEN, Paul
Citation:

Citation: Kieken, Fabien; Jovic, Marko; Tonelli, Marco; Naslavsky, Naava; Caplan, Steve; Sorgen, Paul. "Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1."  Protein Sci. 18, 2471-2479 (2009).
PubMed: 19798736

Assembly members:

Assembly members:
EH_domain_of_EHD1, polymer, 105 residues, 11654.459 Da.
Rab11-FIP2_GPF_peptide, polymer, 12 residues, 1419.530 Da.
CALCIUM ION, 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: PGex6p-2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
EH_domain_of_EHD1: GPLGSDDVEWVVGKDKPTYD EIFYTLSPVNGKITGANAKK EMVKSKLPNTVLGKIWKLAD VDKDGLLDDEEFALANHLIK VKLEGHELPADLPPHLVPPS KRRHE
Rab11-FIP2_GPF_peptide: FNYESTGPFTAK

Data sets:
Data typeCount
13C chemical shifts365
15N chemical shifts91
1H chemical shifts813

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3CA23

Entities:

Entity 1, entity_1 105 residues - 11654.459 Da.

1   GLYPROLEUGLYSERASPASPVALGLUTRP
2   VALVALGLYLYSASPLYSPROTHRTYRASP
3   GLUILEPHETYRTHRLEUSERPROVALASN
4   GLYLYSILETHRGLYALAASNALALYSLYS
5   GLUMETVALLYSSERLYSLEUPROASNTHR
6   VALLEUGLYLYSILETRPLYSLEUALAASP
7   VALASPLYSASPGLYLEULEUASPASPGLU
8   GLUPHEALALEUALAASNHISLEUILELYS
9   VALLYSLEUGLUGLYHISGLULEUPROALA
10   ASPLEUPROPROHISLEUVALPROPROSER
11   LYSARGARGHISGLU

Entity 2, entity_2 12 residues - 1419.530 Da.

1   PHEASNTYRGLUSERTHRGLYPROPHETHR
2   ALALYS

Entity 3, CA2 - Ca - 40.078 Da.

1   CA

Samples:

sample_1: EH domain of EHD1, [U-99% 13C; U-99% 15N], 0.6 mM; Rab11-FIP2 GPF peptide 3 mM; H20 90%; D20 10%

sample_conditions_1: ionic strength: 0.1 M; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 13CFiltered-13CfilteredNOESYsample_1isotropicsample_conditions_1
2D 13C-filtered-13C editedNOESYsample_1isotropicsample_conditions_1
2D 13C-filtered-15N editedNOESYsample_1isotropicsample_conditions_1
2D 15N filtered Noesysample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - data analysis

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

ProcheckNMR, Laskowski and MacArthur - data analysis

VNMR, Varian - collection

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 15279 16179 16180 16671
PDB
DBJ BAB28540 BAC40684 BAE32742 BAE35499 BAE35852
EMBL CAH90816
GB AAB81204 AAD45423 AAF24223 AAG02009 AAH37094
REF NP_001011939 NP_001015578 NP_001125465 NP_001162473 NP_001248124
SP Q5E9R3 Q5RBP4 Q641Z6 Q9H4M9 Q9WVK4
AlphaFold Q5E9R3 Q5RBP4 Q641Z6 Q9H4M9 Q9WVK4

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