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 16599

Title: Backbone resonance assignments of clytin   PubMed: 20926380

Deposition date: 2009-11-09 Original release date: 2010-09-28

Authors: Feng, Yingang; Wang, Jinfeng

Citation: Titushin, Maxim; Feng, Yingang; Stepanyuk, Galina; Li, Yang; Markova, Svetlana; Golz, Stefan; Wang, Bi-Cheng; Lee, John; Wang, Jinfeng; Vysotski, Eugene; Liu, Zhi-Jie. "NMR-derived topology of a GFP-photoprotein energy transfer complex."  J. Biol. Chem. 285, 40891-40900 (2010).

Assembly members:
clytin, polymer, 198 residues, Formula weight is not available
CZH, non-polymer, 455.462 Da.

Natural source:   Common Name: C. gregaria   Taxonomy ID: 27801   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Clytia gregaria

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

Entity Sequences (FASTA):
clytin: MTDTASKYAVKLKTNFEDPK WVNRHKFMFNFLDINGNGKI TLDEIVSKASDDICAKLGAT PAQTQRHQEAVEAFFKKIGL DYGKEVEFPAFVNGWKELAK HDLKLWSQNKKSLIRNWGEA VFDIFDKDGSGSISLDEWKT YGGISGICPSDEDAEKTFKH CDLDNSGKLDVDEMTRQHLG FWYTLDPNADGLYGNFVP

Data sets:
Data typeCount
13C chemical shifts542
15N chemical shifts194
1H chemical shifts557

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1component11
2component22

Entities:

Entity 1, component1 198 residues - Formula weight is not available

1   METTHRASPTHRALASERLYSTYRALAVAL
2   LYSLEULYSTHRASNPHEGLUASPPROLYS
3   TRPVALASNARGHISLYSPHEMETPHEASN
4   PHELEUASPILEASNGLYASNGLYLYSILE
5   THRLEUASPGLUILEVALSERLYSALASER
6   ASPASPILECYSALALYSLEUGLYALATHR
7   PROALAGLNTHRGLNARGHISGLNGLUALA
8   VALGLUALAPHEPHELYSLYSILEGLYLEU
9   ASPTYRGLYLYSGLUVALGLUPHEPROALA
10   PHEVALASNGLYTRPLYSGLULEUALALYS
11   HISASPLEULYSLEUTRPSERGLNASNLYS
12   LYSSERLEUILEARGASNTRPGLYGLUALA
13   VALPHEASPILEPHEASPLYSASPGLYSER
14   GLYSERILESERLEUASPGLUTRPLYSTHR
15   TYRGLYGLYILESERGLYILECYSPROSER
16   ASPGLUASPALAGLULYSTHRPHELYSHIS
17   CYSASPLEUASPASNSERGLYLYSLEUASP
18   VALASPGLUMETTHRARGGLNHISLEUGLY
19   PHETRPTYRTHRLEUASPPROASNALAASP
20   GLYLEUTYRGLYASNPHEVALPRO

Entity 2, component2 - C26 H21 N3 O5 - 455.462 Da.

1   CZH

Samples:

sample_1: clytin, [U-13C; U-15N], 1.0 mM; Tris-HCl 20 mM; sodium chloride 10 mM; EDTA 2 mM; DSS 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

FELIX, Accelrys Software Inc. - chemical shift assignment, processing

NMR spectrometers:

  • Bruker DMX 600 MHz

Related Database Links:

PDB
GB ADI71937 ADI71938 ADI71939

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