BMRB Entry 18843
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18843
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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
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 512 |
| 15N chemical shifts | 136 |
| 1H chemical shifts | 787 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FUN-EGF3 | 1 |
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 | SER | ALA | ARG | GLY | GLY | GLY | GLY | HIS | ASP | ALA | ||||
| 2 | LEU | LYS | GLY | PRO | ASN | VAL | CYS | GLY | SER | ARG | ||||
| 3 | TYR | ASN | ALA | TYR | CYS | CYS | PRO | GLY | TRP | LYS | ||||
| 4 | THR | LEU | PRO | GLY | GLY | ASN | GLN | CYS | ILE | VAL | ||||
| 5 | PRO | ILE | CYS | ARG | HIS | SER | CYS | GLY | ASP | GLY | ||||
| 6 | PHE | CYS | SER | ARG | PRO | ASN | MET | CYS | THR | CYS | ||||
| 7 | PRO | SER | GLY | GLN | ILE | ALA | PRO | SER | CYS | GLY | ||||
| 8 | SER | ARG | SER | ILE | GLN | HIS | CYS | ASN | ILE | ARG | ||||
| 9 | CYS | MET | ASN | GLY | GLY | SER | CYS | SER | ASP | ASP | ||||
| 10 | HIS | CYS | LEU | CYS | GLN | LYS | GLY | TYR | ILE | GLY | ||||
| 11 | THR | HIS | CYS | GLY | GLN | PRO | VAL | CYS | GLU | SER | ||||
| 12 | GLY | CYS | LEU | ASN | GLY | GLY | ARG | CYS | VAL | ALA | ||||
| 13 | PRO | ASN | ARG | CYS | ALA | CYS | THR | TYR | GLY | PHE | ||||
| 14 | THR | GLY | PRO | GLN | CYS | GLU |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 3D (H)CC(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_4 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_4 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_4 | isotropic | sample_conditions_1 |
| 3D 1H-15N HSQC-NOESY-HSQC | sample_1 | isotropic | sample_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