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 5882

Title: Backbone chemical shift assignments for the C-terminal globular domain of EMILIN-1   PubMed: 15017143

Deposition date: 2003-07-25 Original release date: 2004-04-07

Authors: Verdone, Giuliana; Colebrooke, Simon; Boyd, Jonathan; Viglino, Paolo; Corazza, Alessandra; Esposito, Gennaro; Campbell, Iain

Citation: Verdone, Giuliana; Colebrooke, Simon; Boyd, Jonathan; Viglino, Paolo; Corazza, Alessandra; Doliana, Roberto; Mungiguerra, Gabriella; Colombatti, Alfonso; Esposito, Gennaro; Campbell, Iain. "Letter to the Editor: Sequence-specific backbone NMR assignments for the C-terminal globular domain of EMILIN-1. "  J. Biomol. NMR 29, 91-92 (2004).

Assembly members:
C1q domain of h-EMILIN-1, polymer, 162 residues, 16824 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):
C1q domain of h-EMILIN-1: MRGSHHHHHHGSPVPQVAFS AALSLPRSEPGTVPFDRVLL NDGGYYDPETGVFTAPLAGR YLLSAVLTGHRHEKVEAVLS RSNQGVARVDSGGYEPEGLE NKPVAESQPSPGTLGVFSLI LPLQAGDTVCVDLVMGQLAH SEEPLTIFSGALLYGDPELE HA

Data sets:
Data typeCount
1H chemical shifts142
13C chemical shifts438
15N chemical shifts137

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1C1q subunit 11
2C1q subunit 21
3C1q subunit 31

Entities:

Entity 1, C1q subunit 1 162 residues - 16824 Da.

1   METARGGLYSERHISHISHISHISHISHIS
2   GLYSERPROVALPROGLNVALALAPHESER
3   ALAALALEUSERLEUPROARGSERGLUPRO
4   GLYTHRVALPROPHEASPARGVALLEULEU
5   ASNASPGLYGLYTYRTYRASPPROGLUTHR
6   GLYVALPHETHRALAPROLEUALAGLYARG
7   TYRLEULEUSERALAVALLEUTHRGLYHIS
8   ARGHISGLULYSVALGLUALAVALLEUSER
9   ARGSERASNGLNGLYVALALAARGVALASP
10   SERGLYGLYTYRGLUPROGLUGLYLEUGLU
11   ASNLYSPROVALALAGLUSERGLNPROSER
12   PROGLYTHRLEUGLYVALPHESERLEUILE
13   LEUPROLEUGLNALAGLYASPTHRVALCYS
14   VALASPLEUVALMETGLYGLNLEUALAHIS
15   SERGLUGLUPROLEUTHRILEPHESERGLY
16   ALALEULEUTYRGLYASPPROGLULEUGLU
17   HISALA

Samples:

sample_1: C1q domain of h-EMILIN-1, [U-100% 13C; U-100% 15N; 80% 2H], 1.8 mM; phosphate buffer 20 mM; sodium chloride 100 mM

Ex-cond_1: pH: 7.50; temperature: 310.0 K

Experiments:

NameSampleSample stateSample conditions
1H,15N-HSQCsample_1not availableEx-cond_1
3D [15N, 1H]-TROSY-HNCAsample_1not availableEx-cond_1
3D [15N, 1H]-TROSY-HN(CO)CAsample_1not availableEx-cond_1
3D [15N, 1H]-TROSY-HNCACBsample_1not availableEx-cond_1
3D [15N, 1H]-TROSY-HN(CO)CACBsample_1not availableEx-cond_1
3D [15N, 1H]-TROSY-HNCOsample_1not availableEx-cond_1
3D [15N, 1H]-TROSY-HN(CA)COsample_1not availableEx-cond_1
3D 15N-NOESY-HSQCsample_1not availableEx-cond_1

Software:

FELIX v2.3 - spectra processing

XEasy v1.3.13 - spectra assignment

NMR spectrometers:

  • Oxford Instruments . 750 MHz
  • Oxford Instruments . 600 MHz
  • Oxford Instruments . 500 MHz

Related Database Links:

PDB
EMBL CAB43287
GB AAD42161 AAF25006 AAH07530 AAH09947 AAI36280
REF NP_001247837 NP_008977 XP_002812243 XP_003270673 XP_003827126
SP Q9Y6C2

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