BMRB Entry 19078
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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/BMR19078
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Title: Human fibrillin1 EGF2-EGF3-hybrid1-cbEGF1 PubMed: 23649688
Deposition date: 2013-03-06 Original release date: 2014-04-16
Authors: Robertson, Ian; Osuch, Isabelle; Jensen, Sacha; Yadin, David; Handford, Penny; Redfield, Christina
Citation: Robertson, Ian; Osuch, Isabelle; Yadin, David; Handford, Penny; Jensen, Sacha; Redfield, Christina. "(1)H, (13)C and (15)N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment." Biomol. NMR Assignments 8, 189-194 (2014).
Assembly members:
e2cb1, polymer, 177 residues, 18823.4 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):
e2cb1: SASRSIQHCNIRCMNGGSCS
DDHCLCQKGYIGTHCGQPVC
ESGCLNGGRCVAPNRCACTY
GFTGPQCERDYRTGPCFTVI
SNQMCQGQLSGIVSTKTLCC
ATVGRAWGHPCEMCPAQPHP
CRRGFIPNIRTGACQDVDEC
QAIPGLCQGGNCINTVGSFE
CKCPAGHKLNEVSQKCE
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 624 |
15N chemical shifts | 170 |
1H chemical shifts | 965 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | fibrillin | 1 |
Entities:
Entity 1, fibrillin 177 residues - 18823.4 Da.
1 | SER | ALA | SER | ARG | SER | ILE | GLN | HIS | CYS | ASN | ||||
2 | ILE | ARG | CYS | MET | ASN | GLY | GLY | SER | CYS | SER | ||||
3 | ASP | ASP | HIS | CYS | LEU | CYS | GLN | LYS | GLY | TYR | ||||
4 | ILE | GLY | THR | HIS | CYS | GLY | GLN | PRO | VAL | CYS | ||||
5 | GLU | SER | GLY | CYS | LEU | ASN | GLY | GLY | ARG | CYS | ||||
6 | VAL | ALA | PRO | ASN | ARG | CYS | ALA | CYS | THR | TYR | ||||
7 | GLY | PHE | THR | GLY | PRO | GLN | CYS | GLU | ARG | ASP | ||||
8 | TYR | ARG | THR | GLY | PRO | CYS | PHE | THR | VAL | ILE | ||||
9 | SER | ASN | GLN | MET | CYS | GLN | GLY | GLN | LEU | SER | ||||
10 | GLY | ILE | VAL | SER | THR | LYS | THR | LEU | CYS | CYS | ||||
11 | ALA | THR | VAL | GLY | ARG | ALA | TRP | GLY | HIS | PRO | ||||
12 | CYS | GLU | MET | CYS | PRO | ALA | GLN | PRO | HIS | PRO | ||||
13 | CYS | ARG | ARG | GLY | PHE | ILE | PRO | ASN | ILE | ARG | ||||
14 | THR | GLY | ALA | CYS | GLN | ASP | VAL | ASP | GLU | CYS | ||||
15 | GLN | ALA | ILE | PRO | GLY | LEU | CYS | GLN | GLY | GLY | ||||
16 | ASN | CYS | ILE | ASN | THR | VAL | GLY | SER | PHE | GLU | ||||
17 | CYS | LYS | CYS | PRO | ALA | GLY | HIS | LYS | LEU | ASN | ||||
18 | GLU | VAL | SER | GLN | LYS | CYS | GLU |
Samples:
sample_1: fibrillin e2cb1, [U-13C; U-15N], 1 mM; calcium chloride 5 mM
sample_2: fibrillin e2cb1, [U-13C; U-15N], 1 mM; calcium chloride 5 mM
sample_conditions_1: ionic strength: 15 mM; pH: 5.4; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
No software information available
NMR spectrometers:
- Bruker Avance 500 MHz
- home built OMEGA 950 MHz
- home built OMEGA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts