Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16386
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Rossi, Paolo; Chiang, Yiwen; Anderson, Stephen; Montelione, Gaetano. "Solution NMR Structure of the EGF-like 1 Domain of Human Fibulin-4. Northeast Structural Genomics Target HR6275." .
Assembly members:
EGF-like 1 Domain, polymer, 71 residues, 7576.472 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 Vector: na
Entity Sequences (FASTA):
EGF-like 1 Domain: SDVNECLTIPEACKGEMKCI
NHYGGYLCLPRSAAVINDLH
GEGPPPPVPPAQHPNPCPPG
YEPDDQDSCVD
Data type | Count |
13C chemical shifts | 264 |
15N chemical shifts | 67 |
1H chemical shifts | 407 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | EGF-like 1 Domain | 1 |
Entity 1, EGF-like 1 Domain 71 residues - 7576.472 Da.
1 | SER | ASP | VAL | ASN | GLU | CYS | LEU | THR | ILE | PRO | ||||
2 | GLU | ALA | CYS | LYS | GLY | GLU | MET | LYS | CYS | ILE | ||||
3 | ASN | HIS | TYR | GLY | GLY | TYR | LEU | CYS | LEU | PRO | ||||
4 | ARG | SER | ALA | ALA | VAL | ILE | ASN | ASP | LEU | HIS | ||||
5 | GLY | GLU | GLY | PRO | PRO | PRO | PRO | VAL | PRO | PRO | ||||
6 | ALA | GLN | HIS | PRO | ASN | PRO | CYS | PRO | PRO | GLY | ||||
7 | TYR | GLU | PRO | ASP | ASP | GLN | ASP | SER | CYS | VAL | ||||
8 | ASP |
sample_1: entity, [U-100% 13C; U-100% 15N], 0.6 mM; sodium chloride 150 mM; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%
sample_2: entity, [U-100% 15N], 0.3 mM; sodium chloride 150 mM; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HMQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N het_NOE | sample_1 | isotropic | sample_conditions_1 |
1D 15N_T1 series | sample_1 | isotropic | sample_conditions_1 |
1D 15N_T2 series | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN v2.1, Bruker Biospin - collection
PSVS v1.3, Bhattacharya and Montelione - validation
SPARKY v2.113, Goddard - data analysis
PINE, Bahrami, Markley, Assadi, and Eghbalnia - data analysis
Molmol, Koradi, Billeter and Wuthrich - visualization
PyMol, DeLano Scientific - visualization
PDBStat v5.1, Tejero, Montelione - PDB processing
PDB | |
DBJ | BAA92880 BAD92358 BAF84768 BAG37622 BAG50843 |
EMBL | CAA10791 CAG46732 |
GB | AAC03101 AAF65188 AAG45245 AAH10456 AAQ89258 |
REF | NP_001231778 NP_058634 XP_001118071 XP_003274253 XP_003909598 |
SP | O55058 O95967 |
AlphaFold | O55058 O95967 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks