BMRB Entry 18995
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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/BMR18995
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: Gupta, Arun; Chou, Ruey-Hwang; Li, Hongchun; Yang, Lee-Wei; Yu, Chin. "Structural insights into the interaction of human S100B and basic fibroblast growth factor (FGF2): Effects on FGFR1 receptor signaling" Biochim. Biophys. Acta. 2013, 2606-2619 (2013).
PubMed: 24063890
Assembly members:
FGF2, polymer, 126 residues, 14422.641 Da.
S100B, polymer, 182 residues, 21173.836 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: pET(20b)+
Entity Sequences (FASTA):
FGF2: DPKRLYCKNGGFFLRIHPDG
RVDGVREKSDPHIKLQLQAE
ERGVVSIKGVSANRYLAMKE
DGRLLASKSVTDECFFFERL
ESNNYNTYRSRKYTSWYVAL
KRTGQYKLGSKTGPGQKAIL
FLPMSA
S100B: SELEKAMVALIDVFHQYSGR
EGDKHKLKKSELKELINNEL
SHFLEEIKEQEVVDKVMETL
DNDGDGECDFQEFMAFVAMV
TTACHEFFEHESELEKAMVA
LIDVFHQYSGREGDKHKLKK
SELKELINNELSHFLEEIKE
QEVVDKVMETLDNDGDGECD
FQEFMAFVAMVTTACHEFFE
HE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 250 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 81 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FGF2_1 | 1 |
| 2 | S100B | 2 |
| 3 | FGF2_2 | 1 |
Entities:
Entity 1, FGF2_1 126 residues - 14422.641 Da.
| 1 | ASP | PRO | LYS | ARG | LEU | TYR | CYS | LYS | ASN | GLY | ||||
| 2 | GLY | PHE | PHE | LEU | ARG | ILE | HIS | PRO | ASP | GLY | ||||
| 3 | ARG | VAL | ASP | GLY | VAL | ARG | GLU | LYS | SER | ASP | ||||
| 4 | PRO | HIS | ILE | LYS | LEU | GLN | LEU | GLN | ALA | GLU | ||||
| 5 | GLU | ARG | GLY | VAL | VAL | SER | ILE | LYS | GLY | VAL | ||||
| 6 | SER | ALA | ASN | ARG | TYR | LEU | ALA | MET | LYS | GLU | ||||
| 7 | ASP | GLY | ARG | LEU | LEU | ALA | SER | LYS | SER | VAL | ||||
| 8 | THR | ASP | GLU | CYS | PHE | PHE | PHE | GLU | ARG | LEU | ||||
| 9 | GLU | SER | ASN | ASN | TYR | ASN | THR | TYR | ARG | SER | ||||
| 10 | ARG | LYS | TYR | THR | SER | TRP | TYR | VAL | ALA | LEU | ||||
| 11 | LYS | ARG | THR | GLY | GLN | TYR | LYS | LEU | GLY | SER | ||||
| 12 | LYS | THR | GLY | PRO | GLY | GLN | LYS | ALA | ILE | LEU | ||||
| 13 | PHE | LEU | PRO | MET | SER | ALA |
Entity 2, S100B 182 residues - 21173.836 Da.
| 1 | SER | GLU | LEU | GLU | LYS | ALA | MET | VAL | ALA | LEU | ||||
| 2 | ILE | ASP | VAL | PHE | HIS | GLN | TYR | SER | GLY | ARG | ||||
| 3 | GLU | GLY | ASP | LYS | HIS | LYS | LEU | LYS | LYS | SER | ||||
| 4 | GLU | LEU | LYS | GLU | LEU | ILE | ASN | ASN | GLU | LEU | ||||
| 5 | SER | HIS | PHE | LEU | GLU | GLU | ILE | LYS | GLU | GLN | ||||
| 6 | GLU | VAL | VAL | ASP | LYS | VAL | MET | GLU | THR | LEU | ||||
| 7 | ASP | ASN | ASP | GLY | ASP | GLY | GLU | CYS | ASP | PHE | ||||
| 8 | GLN | GLU | PHE | MET | ALA | PHE | VAL | ALA | MET | VAL | ||||
| 9 | THR | THR | ALA | CYS | HIS | GLU | PHE | PHE | GLU | HIS | ||||
| 10 | GLU | SER | GLU | LEU | GLU | LYS | ALA | MET | VAL | ALA | ||||
| 11 | LEU | ILE | ASP | VAL | PHE | HIS | GLN | TYR | SER | GLY | ||||
| 12 | ARG | GLU | GLY | ASP | LYS | HIS | LYS | LEU | LYS | LYS | ||||
| 13 | SER | GLU | LEU | LYS | GLU | LEU | ILE | ASN | ASN | GLU | ||||
| 14 | LEU | SER | HIS | PHE | LEU | GLU | GLU | ILE | LYS | GLU | ||||
| 15 | GLN | GLU | VAL | VAL | ASP | LYS | VAL | MET | GLU | THR | ||||
| 16 | LEU | ASP | ASN | ASP | GLY | ASP | GLY | GLU | CYS | ASP | ||||
| 17 | PHE | GLN | GLU | PHE | MET | ALA | PHE | VAL | ALA | MET | ||||
| 18 | VAL | THR | THR | ALA | CYS | HIS | GLU | PHE | PHE | GLU | ||||
| 19 | HIS | GLU |
Samples:
sample_1: S100B, [U-100% 13C; U-100% 15N], 1.2 mM; TRIS 20 mM; ammonium sulfate 50 mM; calcium chloride 5 mM; DTT 5 mM; sodium azide 0.01%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.050 M; pH: 7.2; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMRJ v3.2, Varian - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
HADDOCK, Alexandre Bonvin - refinement, structure solution
NMR spectrometers:
- Varian INOVA 700 MHz
Related Database Links:
| BMRB | 4091 15923 4001 4105 5206 5895 |
| PDB | |
| DBJ | BAG70135 BAG70264 BAE22214 BAE22413 BAE36647 BAE88979 BAG74213 |
| EMBL | CCO13911 CCO13913 CAA25567 CAG46920 |
| GB | AAA31248 AAA52448 AAA52531 AAA52532 AAA52533 AAA03075 AAA42096 AAA60367 AAH01766 AAH61178 |
| REF | NP_001103711 NP_001997 XP_001099284 XP_002717284 XP_002815172 NP_001076199 NP_001247455 NP_001270589 NP_006263 NP_033141 |
| SP | P09038 P48799 Q5IS69 P04271 P04631 P50114 Q6YNR6 |
| PRF | 2003367B |
| AlphaFold | P09038 P48799 Q5IS69 P04271 P04631 P50114 Q6YNR6 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks