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 18843

Title: 1H, 13C and 15N assignments of the four N-terminal domains of human fibrillin-1   PubMed: 23264024

Deposition date: 2012-11-19 Original release date: 2013-01-29

Authors: Yadin, David; Robertson, Ian; Jensen, Sacha; Handford, Penny; Redfield, Christina

Citation: Yadin, David; Robertson, Ian; Jensen, Sacha; Handford, Penny; Redfield, Christina. "(1)H, (13)C and (15)N assignments of the four N-terminal domains of human fibrillin-1."  Biomol. NMR Assignments ., .-. (2012).

Assembly members:
FUN-EGF3, polymer, 136 residues, 14082 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):
FUN-EGF3: SARGGGGHDALKGPNVCGSR YNAYCCPGWKTLPGGNQCIV PICRHSCGDGFCSRPNMCTC PSGQIAPSCGSRSIQHCNIR CMNGGSCSDDHCLCQKGYIG THCGQPVCESGCLNGGRCVA PNRCACTYGFTGPQCE

Data sets:
Data typeCount
13C chemical shifts512
15N chemical shifts136
1H chemical shifts787

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FUN-EGF31

Entities:

Entity 1, FUN-EGF3 136 residues - 14082 Da.

The four N-terminal domains of fibrillin-1: the fibrillin unique N-terminal domain and the first three non-calcium binding epidermal growth factor-like domains. Residues 1 and 2 are are spacer residues between a factor Xa cleavage site and the native sequence.

1   SERALAARGGLYGLYGLYGLYHISASPALA
2   LEULYSGLYPROASNVALCYSGLYSERARG
3   TYRASNALATYRCYSCYSPROGLYTRPLYS
4   THRLEUPROGLYGLYASNGLNCYSILEVAL
5   PROILECYSARGHISSERCYSGLYASPGLY
6   PHECYSSERARGPROASNMETCYSTHRCYS
7   PROSERGLYGLNILEALAPROSERCYSGLY
8   SERARGSERILEGLNHISCYSASNILEARG
9   CYSMETASNGLYGLYSERCYSSERASPASP
10   HISCYSLEUCYSGLNLYSGLYTYRILEGLY
11   THRHISCYSGLYGLNPROVALCYSGLUSER
12   GLYCYSLEUASNGLYGLYARGCYSVALALA
13   PROASNARGCYSALACYSTHRTYRGLYPHE
14   THRGLYPROGLNCYSGLU

Samples:

sample_1: FUN-EGF3, [U-99% 15N], 1.5 mM

sample_2: FUN-EGF3, [U-99% 15N], 0.5 mM

sample_3: FUN-EGF3, [U-99% 13C; U-99% 15N], 1.5 mM

sample_4: FUN-EGF3, [U-99% 13C; U-99% 15N], 1.5 mM

sample_conditions_1: ionic strength: 0 M; pH: 5.40; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D DQF-COSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D (H)CC(CO)NHsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HN(CA)COsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_4isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_4isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_4isotropicsample_conditions_1
3D 1H-15N HSQC-NOESY-HSQCsample_1isotropicsample_conditions_1

Software:

NMRPipe vJune 2006 Sun Solaris, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpN_Analysis v2.1.5, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • home-built home-built using GE Omega software 750 MHz
  • home-built home-built using GE Omega software 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAD16737 BAD16738 BAD16739 BAG65498
EMBL CAA45118
GB AAA56840 AAA61825 AAA64217 AAA74122 AAB02036
REF NP_000129 NP_001001771 NP_001274014 NP_032019 NP_114013
SP P35555 P98133 Q61554 Q9TV36
TPG DAA25192

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