BMRB Entry 18112
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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/BMR18112
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Title: Minimal Constraints Solution NMR Structure of Prospero Homeobox protein 1 from Homo sapiens. Northeast Structural Genomics Consortium Target HR4660B.
Deposition date: 2011-11-29 Original release date: 2011-12-20
Authors: Rossi, Paolo; Lange, Oliver; Lee, Hsiau-Wei; Maglaqui, Melissa; Janjua, Haleema; Ciccosanti, Colleen; Zhao, Li; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano
Citation: Rossi, Paolo; Lange, Oliver; Lee, Hsiau-Wei; Maglaqui, Melissa; Janjua, Haleema; Ciccosanti, Colleen; Zhao, Li; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano. "Minimal Constraints Solution NMR Structure of Prospero Homeobox protein 1 from Homo sapiens. Northeast Structural Genomics Consortium Target HR4660B." To be published ., .-..
Assembly members:
HR4660B, polymer, 174 residues, 20723.934 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):
HR4660B: MGHHHHHHSHMAMQEGLSPN
HLKKAKLMFFYTRYPSSNML
KTYFSDVKFNRCITSQLIKW
FSNFREFYYIQMEKYARQAI
NDGVTSTEELSITRDCELYR
ALNMHYNKANDFEVPERFLE
VAQITLREFFNAIIAGKDVD
PSWKKAIYKVICKLDSEVPE
IFKSPNCLQELLHE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 530 |
| 15N chemical shifts | 146 |
| 1H chemical shifts | 690 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR4660B | 1 |
Entities:
Entity 1, HR4660B 174 residues - 20723.934 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | ALA | MET | GLN | GLU | GLY | LEU | SER | PRO | ASN | ||||
| 3 | HIS | LEU | LYS | LYS | ALA | LYS | LEU | MET | PHE | PHE | ||||
| 4 | TYR | THR | ARG | TYR | PRO | SER | SER | ASN | MET | LEU | ||||
| 5 | LYS | THR | TYR | PHE | SER | ASP | VAL | LYS | PHE | ASN | ||||
| 6 | ARG | CYS | ILE | THR | SER | GLN | LEU | ILE | LYS | TRP | ||||
| 7 | PHE | SER | ASN | PHE | ARG | GLU | PHE | TYR | TYR | ILE | ||||
| 8 | GLN | MET | GLU | LYS | TYR | ALA | ARG | GLN | ALA | ILE | ||||
| 9 | ASN | ASP | GLY | VAL | THR | SER | THR | GLU | GLU | LEU | ||||
| 10 | SER | ILE | THR | ARG | ASP | CYS | GLU | LEU | TYR | ARG | ||||
| 11 | ALA | LEU | ASN | MET | HIS | TYR | ASN | LYS | ALA | ASN | ||||
| 12 | ASP | PHE | GLU | VAL | PRO | GLU | ARG | PHE | LEU | GLU | ||||
| 13 | VAL | ALA | GLN | ILE | THR | LEU | ARG | GLU | PHE | PHE | ||||
| 14 | ASN | ALA | ILE | ILE | ALA | GLY | LYS | ASP | VAL | ASP | ||||
| 15 | PRO | SER | TRP | LYS | LYS | ALA | ILE | TYR | LYS | VAL | ||||
| 16 | ILE | CYS | LYS | LEU | ASP | SER | GLU | VAL | PRO | GLU | ||||
| 17 | ILE | PHE | LYS | SER | PRO | ASN | CYS | LEU | GLN | GLU | ||||
| 18 | LEU | LEU | HIS | GLU |
Samples:
sample_1: HR4660B, [U-100% 13C; U-100% 15N], 0.96 mM; sodium chloride 200 mM; DTT 10 mM; Calcium Chloride 5 mM; sodium azide 0.02%; MES 20 mM; H2O 95%; D2O 5%
sample_2: HR4660B, [U-13C; U-15N; U-2H], 0.2 mM; sodium chloride 200 mM; DTT 10 mM; Calcium Chloride 5 mM; sodium azide 0.02%; MES 20 mM; H2O 95%; D2O 5%
sample_3: HR4660B, [5% 13C; U-100% 15N], 0.86 mM; sodium chloride 200 mM; DTT 10 mM; Calcium Chloride 5 mM; sodium azide 0.02%; MES 20 mM; H2O 95%; D2O 5%
sample_conditions_1: 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 | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C arom NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C-13C HSQC_NOESY_HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
SPARKY, Goddard - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PALES, PALES (Zweckstetter, Bax) - geometry optimization
PSVS, Bhattacharya and Montelione - structure validation
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAC35190 BAE25293 BAF82865 BAG10650 BAG60453 |
| GB | AAB30541 AAC32824 AAC50656 AAC59938 AAH24201 |
| REF | NP_001005616 NP_001121962 NP_001180161 NP_001247802 NP_001257545 |
| SP | P48437 Q91018 Q92786 |
| TPG | DAA21012 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts