BMRB Entry 18808
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18808
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Title: Structure, phosphorylation and U2AF65 binding of the Nterminal domain of splicing factor 1 during 3 splice site recognition PubMed: 23175611
Deposition date: 2012-10-25 Original release date: 2013-01-28
Authors: Madl, Tobias; Sattler, Michael; Zhang, Yun; Bagdiul, Ivona; Kern, Thomas; Kang, Hyun-Seo; Zou, Peijian; Maeusbacher, Nina; Sieber, Stephan; Kraemer, Angela
Citation: Zhang, Yun; Madl, Tobias; Bagdiul, Ivona; Kern, Thomas; Kang, Hyun-Seo; Zou, Peijian; Maeusbacher, Nina; Sieber, Stephan; Kraemer, Angela; Sattler, Michael. "Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition" Nucleic Acids Res. 41, 1343-1354 (2013).
Assembly members:
entity_1, polymer, 145 residues, 16675.199 Da.
entity_2, polymer, 104 residues, 11976.698 Da.
Natural source: Common Name: Humans Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MATGANATPLDFPSKKRKRS
RWNQDTMEQKTVIPGMPTVI
PPGLTREQERAYIVQLQIED
LTRKLRTGDLGIPPNPEDRS
PSPEPIYNSEGKRLNTREFR
TRKKLEEERHNLITEMVALN
PDFKPPADYKPPATRVCDKV
MIPQD
entity_2: GHPTEVLCLMNMVLPEELLD
DEEYEEIVEDVRDECSKYGL
VKSIEIPRPVDGVEVPGCGK
IFVEFTSVFDCQKAMQGLTG
RKFANRVVVTKYCDPDSYHR
RDFW
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 468 |
| 15N chemical shifts | 209 |
| 1H chemical shifts | 576 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 145 residues - 16675.199 Da.
| 1 | MET | ALA | THR | GLY | ALA | ASN | ALA | THR | PRO | LEU | ||||
| 2 | ASP | PHE | PRO | SER | LYS | LYS | ARG | LYS | ARG | SER | ||||
| 3 | ARG | TRP | ASN | GLN | ASP | THR | MET | GLU | GLN | LYS | ||||
| 4 | THR | VAL | ILE | PRO | GLY | MET | PRO | THR | VAL | ILE | ||||
| 5 | PRO | PRO | GLY | LEU | THR | ARG | GLU | GLN | GLU | ARG | ||||
| 6 | ALA | TYR | ILE | VAL | GLN | LEU | GLN | ILE | GLU | ASP | ||||
| 7 | LEU | THR | ARG | LYS | LEU | ARG | THR | GLY | ASP | LEU | ||||
| 8 | GLY | ILE | PRO | PRO | ASN | PRO | GLU | ASP | ARG | SER | ||||
| 9 | PRO | SER | PRO | GLU | PRO | ILE | TYR | ASN | SER | GLU | ||||
| 10 | GLY | LYS | ARG | LEU | ASN | THR | ARG | GLU | PHE | ARG | ||||
| 11 | THR | ARG | LYS | LYS | LEU | GLU | GLU | GLU | ARG | HIS | ||||
| 12 | ASN | LEU | ILE | THR | GLU | MET | VAL | ALA | LEU | ASN | ||||
| 13 | PRO | ASP | PHE | LYS | PRO | PRO | ALA | ASP | TYR | LYS | ||||
| 14 | PRO | PRO | ALA | THR | ARG | VAL | CYS | ASP | LYS | VAL | ||||
| 15 | MET | ILE | PRO | GLN | ASP |
Entity 2, entity_2 104 residues - 11976.698 Da.
| 1 | GLY | HIS | PRO | THR | GLU | VAL | LEU | CYS | LEU | MET | ||||
| 2 | ASN | MET | VAL | LEU | PRO | GLU | GLU | LEU | LEU | ASP | ||||
| 3 | ASP | GLU | GLU | TYR | GLU | GLU | ILE | VAL | GLU | ASP | ||||
| 4 | VAL | ARG | ASP | GLU | CYS | SER | LYS | TYR | GLY | LEU | ||||
| 5 | VAL | LYS | SER | ILE | GLU | ILE | PRO | ARG | PRO | VAL | ||||
| 6 | ASP | GLY | VAL | GLU | VAL | PRO | GLY | CYS | GLY | LYS | ||||
| 7 | ILE | PHE | VAL | GLU | PHE | THR | SER | VAL | PHE | ASP | ||||
| 8 | CYS | GLN | LYS | ALA | MET | GLN | GLY | LEU | THR | GLY | ||||
| 9 | ARG | LYS | PHE | ALA | ASN | ARG | VAL | VAL | VAL | THR | ||||
| 10 | LYS | TYR | CYS | ASP | PRO | ASP | SER | TYR | HIS | ARG | ||||
| 11 | ARG | ASP | PHE | TRP |
Samples:
sample_1: entity, [U-15N], 100 – 600 uM; entity, [U-13C; U-15N], 100 – 600 uM; entity, [U-13C; U-15N; U-2H], 100 – 600 uM; sodium phosphate 20 mM; NaCl 50 mM; sodium azide 0.1%; DTT 1 mM; EDTA 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 70 mM; 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 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v2.1, Linge, O, . - structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment
TOPSPIN, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 750 MHz
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
Related Database Links:
| BMRB | 18802 19034 |
| PDB | |
| DBJ | BAA05116 BAA05117 BAE01434 BAE26935 BAE27661 BAC37309 BAG70075 BAG70201 BAI45669 |
| EMBL | CAA03883 CAA59797 CAA70018 CAA70019 CAA73359 CAA45409 CAA45874 CAA45875 |
| GB | AAB03514 AAB04033 AAH08080 AAH08724 AAH09091 AAH07487 AAH08740 AAH30574 AAH43071 AAH89996 |
| PIR | S52735 |
| REF | NP_001075083 NP_001104261 NP_001104263 NP_001162562 NP_001164798 NP_001012496 NP_001068804 NP_001192160 NP_009210 NP_598432 |
| SP | Q15637 Q64213 P26368 P26369 |
| TPG | DAA13585 DAA19368 |
| PRF | 1805352A |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts