BMRB Entry 5212
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR5212
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Title: SAP/SH2D1A bound to peptide n-pY PubMed: 11823424
Deposition date: 2001-11-15 Original release date: 2002-05-08
Authors: Hwang, P.; Li, C.; Morra, M.; Lillywhite, J.; Gertler, F.; Terhorst, C.; Kay, L.; Pawson, T.; Forman-Kay, J.; Li, S.-C.
Citation: Hwang, P.; Li, C.; Morra, M.; Lillywhite, J.; Muhandiram, D.; Gertler, F.; Terhorst, C.; Kay, L.; Pawson, T.; Forman-Kay, J.; Li, S.-C.. "A "three-pronged" Binding Mechanism for the SAP/SH2D1A SH2 Domain: Structural Basis and Relevance to the XLP Syndrome" EMBO J. 21, 314-323 (2002).
Assembly members:
SAP/SH2D1A, polymer, 128 residues, Formula weight is not available
peptide n-pY, polymer, 9 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):
SAP/SH2D1A: MDAVAVYHGKISRETGEKLL
LATGLDGSYLLRDSESVPGV
YCLCVLYHGYIYTYRVSQTE
TGSWSAETAPGVHKRYFRKI
KNLISAFQKPDQGIVIPLQY
PVEKKSSARSTQGTTGIRED
PDVCLKAP
peptide n-pY: RKSLTIXAX
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 773 |
| 15N chemical shifts | 133 |
| 13C chemical shifts | 557 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SH2 DOMAIN PROTEIN 1A | 1 |
| 2 | peptide n-pY | 2 |
Entities:
Entity 1, SH2 DOMAIN PROTEIN 1A 128 residues - Formula weight is not available
| 1 | MET | ASP | ALA | VAL | ALA | VAL | TYR | HIS | GLY | LYS | ||||
| 2 | ILE | SER | ARG | GLU | THR | GLY | GLU | LYS | LEU | LEU | ||||
| 3 | LEU | ALA | THR | GLY | LEU | ASP | GLY | SER | TYR | LEU | ||||
| 4 | LEU | ARG | ASP | SER | GLU | SER | VAL | PRO | GLY | VAL | ||||
| 5 | TYR | CYS | LEU | CYS | VAL | LEU | TYR | HIS | GLY | TYR | ||||
| 6 | ILE | TYR | THR | TYR | ARG | VAL | SER | GLN | THR | GLU | ||||
| 7 | THR | GLY | SER | TRP | SER | ALA | GLU | THR | ALA | PRO | ||||
| 8 | GLY | VAL | HIS | LYS | ARG | TYR | PHE | ARG | LYS | ILE | ||||
| 9 | LYS | ASN | LEU | ILE | SER | ALA | PHE | GLN | LYS | PRO | ||||
| 10 | ASP | GLN | GLY | ILE | VAL | ILE | PRO | LEU | GLN | TYR | ||||
| 11 | PRO | VAL | GLU | LYS | LYS | SER | SER | ALA | ARG | SER | ||||
| 12 | THR | GLN | GLY | THR | THR | GLY | ILE | ARG | GLU | ASP | ||||
| 13 | PRO | ASP | VAL | CYS | LEU | LYS | ALA | PRO |
Entity 2, peptide n-pY 9 residues - Formula weight is not available
| 1 | ARG | LYS | SER | LEU | THR | ILE | PTR | ALA | NH2 |
Samples:
sample_1: SAP/SH2D1A, [U-15N; U-13C], 1 mM; peptide n-pY 1 mM; phosphate buffer 20 mM; NaCl 100 mM; H2O 90%; D2O 10%
sample_cond_1: pH: 6.0; temperature: 303 K; ionic strength: 120 mM; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HN(CO)HB | sample_1 | not available | sample_cond_1 |
| 3D HNHB | sample_1 | not available | sample_cond_1 |
| 3D 15N,13C-separated NOESY | sample_1 | not available | sample_cond_1 |
Software:
ARIA v1.0 - structure solution
NMRPipe v1.8 - processing
NMRView v3.0 - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| REF | NP_002342.1 XP_865096.1 NP_001028009.1 |
| SWISS-PROT | O60880 |
| GenBank | AAK11578.1 AAX37129.1 AAC62631.1 AAH20732.1 |
| . | 5212 5212 5212 5212 5212 5212 |
| 100 | 2e-69 4e-55 2e-69 4e-55 4e-55 2e-69 4e-55 |
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