BMRB Entry 16099
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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/BMR16099
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Title: Solution NMR Structure of KAZAL-1 domain from Human Follistatin-related protein 3 (FSTL-3). Northeast Structural Genomics Target HR6186A.
Deposition date: 2008-12-30 Original release date: 2010-09-17
Authors: Rossi, Paolo; Chiang, Yiwen; Montelione, Gaetano; Anderson, Stephen
Citation: Rossi, Paolo; Chiang, Yiwen; Montelione, Gaetano; Anderson, Stephen. "Solution NMR Structure of Kazal-1 Domain of Human Follistatin-related protein 3 (FSTL-3). Northeast Structural Genomics Target HR6186A." Not known ., .-..
Assembly members:
FSTL-3, polymer, 74 residues, Formula weight is not available
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):
FSTL-3: SDSCDGVECGPGKACRMLGG
RPRCECAPDCSGLPARLQVC
GSDGATYRDECELRAARCRG
HPDLSVMYRGRCRK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 284 |
| 15N chemical shifts | 67 |
| 1H chemical shifts | 437 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FSTL_3 | 1 |
Entities:
Entity 1, FSTL_3 74 residues - Formula weight is not available
| 1 | SER | ASP | SER | CYS | ASP | GLY | VAL | GLU | CYS | GLY | ||||
| 2 | PRO | GLY | LYS | ALA | CYS | ARG | MET | LEU | GLY | GLY | ||||
| 3 | ARG | PRO | ARG | CYS | GLU | CYS | ALA | PRO | ASP | CYS | ||||
| 4 | SER | GLY | LEU | PRO | ALA | ARG | LEU | GLN | VAL | CYS | ||||
| 5 | GLY | SER | ASP | GLY | ALA | THR | TYR | ARG | ASP | GLU | ||||
| 6 | CYS | GLU | LEU | ARG | ALA | ALA | ARG | CYS | ARG | GLY | ||||
| 7 | HIS | PRO | ASP | LEU | SER | VAL | MET | TYR | ARG | GLY | ||||
| 8 | ARG | CYS | ARG | LYS |
Samples:
sample_1: FSTL-3, [U-100% 13C; U-100% 15N], 0.6 mM; MES 20 mM; sodium chloride 200 mM; H2O 90%; D2O 10%
sample_2: FSTL-3, [U-100% 15N], 0.2 mM; MES 20 mM; sodium chloride 200 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; 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-13C HSQC ali | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aro | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY sim | 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 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 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HET_NOE | sample_2 | isotropic | sample_conditions_1 |
| 2D N15 T1 | sample_2 | isotropic | sample_conditions_1 |
| 2D N15 T2 cpmg | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C NOESY aro | sample_1 | isotropic | sample_conditions_1 |
| 3D NHCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
PSVS v1.3, Bhattacharya and Montelione - structure solution
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v2.113, Goddard - data analysis
TOPSPIN v2.1, Bruker Biospin - collection
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
Molmol, Koradi, Billeter and Wuthrich - visualization
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - refinement
MolProbity, Richardson - refinement
PDBStat, Tejero, Montelione - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAF84647 |
| GB | AAC64321 AAH05839 AAQ89276 EAW61165 EAW61166 |
| REF | NP_005851 XP_001117132 XP_003316016 XP_003788724 XP_004059654 |
| SP | O95633 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts