BMRB Entry 25403

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25403

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Title:
NMR Structural Mapping Reveals Promiscuous Interactions between Clathrin Box Motif Peptides and the N-Terminal Domain of the Clathrin Heavy Chain
Deposition date:
2014-12-20
Original release date:
2015-04-07
Authors:
Zhuo, Yue; Cano, Kristin; Wang, Liping; Ilangovan, Udayar; Hinck, Andrew; Sousa, Rui; Lafer, Eileen
Citation:

Citation: Zhuo, Yue; Cano, Kristin; Wang, Liping; Ilangovan, Udayar; Hinck, Andrew; Sousa, Rui; Lafer, Eileen. "Nuclear Magnetic Resonance Structural Mapping Reveals Promiscuous Interactions between Clathrin-Box Motif Sequences and the N-Terminal Domain of the Clathrin Heavy Chain"  Biochemistry 54, 2571-2580 (2015).
PubMed: 25844500

Assembly members:

Assembly members:
Clathrin_heavy_chain, polymer, 363 residues, Formula weight is not available

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: pBAT4

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Clathrin_heavy_chain: MAQILPIRFQEHLQLQNLGI NPANIGFSTLTMESDKFICI REKVGEQAQVVIIDMNDPSN PIRRPISADSAIMNPASKVI ALKAGKTLQIFNIEMKSKMK AHTMTDDVTFWKWISLNTVA LVTDNAVYHWSMEGESQPVK MFDRHSSLAGCQIINYRTDA KQKWLLLTGISAQQNRVVGA MQLYSVDRKVSQPIEGHAAS FAQFKMEGNAEESTLFCFAV RGQAGGKLHIIEVGTPPTGN QPFPKKAVDVFFPPEAQNDF PVAMQISEKHDVVFLITKYG YIHLYDLETGTCIYMNRISG ETIFVTAPHEATAGIIGVNR KGQVLSVCVEEENIIPYITN VLQNPDLALRMAVRNNLAGA EEL

Data sets:
Data typeCount
13C chemical shifts869
15N chemical shifts268
1H chemical shifts269

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Clathrin TD401

Entities:

Entity 1, Clathrin TD40 363 residues - Formula weight is not available

1   METALAGLNILELEUPROILEARGPHEGLN
2   GLUHISLEUGLNLEUGLNASNLEUGLYILE
3   ASNPROALAASNILEGLYPHESERTHRLEU
4   THRMETGLUSERASPLYSPHEILECYSILE
5   ARGGLULYSVALGLYGLUGLNALAGLNVAL
6   VALILEILEASPMETASNASPPROSERASN
7   PROILEARGARGPROILESERALAASPSER
8   ALAILEMETASNPROALASERLYSVALILE
9   ALALEULYSALAGLYLYSTHRLEUGLNILE
10   PHEASNILEGLUMETLYSSERLYSMETLYS
11   ALAHISTHRMETTHRASPASPVALTHRPHE
12   TRPLYSTRPILESERLEUASNTHRVALALA
13   LEUVALTHRASPASNALAVALTYRHISTRP
14   SERMETGLUGLYGLUSERGLNPROVALLYS
15   METPHEASPARGHISSERSERLEUALAGLY
16   CYSGLNILEILEASNTYRARGTHRASPALA
17   LYSGLNLYSTRPLEULEULEUTHRGLYILE
18   SERALAGLNGLNASNARGVALVALGLYALA
19   METGLNLEUTYRSERVALASPARGLYSVAL
20   SERGLNPROILEGLUGLYHISALAALASER
21   PHEALAGLNPHELYSMETGLUGLYASNALA
22   GLUGLUSERTHRLEUPHECYSPHEALAVAL
23   ARGGLYGLNALAGLYGLYLYSLEUHISILE
24   ILEGLUVALGLYTHRPROPROTHRGLYASN
25   GLNPROPHEPROLYSLYSALAVALASPVAL
26   PHEPHEPROPROGLUALAGLNASNASPPHE
27   PROVALALAMETGLNILESERGLULYSHIS
28   ASPVALVALPHELEUILETHRLYSTYRGLY
29   TYRILEHISLEUTYRASPLEUGLUTHRGLY
30   THRCYSILETYRMETASNARGILESERGLY
31   GLUTHRILEPHEVALTHRALAPROHISGLU
32   ALATHRALAGLYILEILEGLYVALASNARG
33   LYSGLYGLNVALLEUSERVALCYSVALGLU
34   GLUGLUASNILEILEPROTYRILETHRASN
35   VALLEUGLNASNPROASPLEUALALEUARG
36   METALAVALARGASNASNLEUALAGLYALA
37   GLUGLULEU

Samples:

sample_1: Clathrin heavy chain, [U-2H; U-13C; U-15N], 400 uM; sodium phosphate 25 mM; sodium azide 0.02%; D2O, [U-100% 2H], 10%; sodium chloride 50 mM; glycerol, [U-100% 2H], 10%; H2O 90%; DTT 25 mM

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D trHNCAsample_1isotropicsample_conditions_1
3D trHNCACBsample_1isotropicsample_conditions_1
3D trHN(CA)COsample_1isotropicsample_conditions_1
3D trHNCOsample_1isotropicsample_conditions_1
3D trHN(CO)CAsample_1isotropicsample_conditions_1
3D trHN(CO)CACBsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

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