BMRB Entry 4317
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4317
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Title: 1H, 13C, and 15N Chemical Shift Assignments for NS1(1-73)
Deposition date: 1999-03-12 Original release date: 2004-12-07
Authors: Chien, Chen-ya; Montelione, Gaetano
Citation: Chien, Chen-ya; Tejero, R.; Huang, Y.; Zimmerman, D.; Rios, C.; Krug, R.; Montelione, Gaetano. "A novel RNA-binding motif in influenza A virus non-structural protein 1" Nat. Struct. Biol. 4, 891-. (1997).
Assembly members:
Non-structural protein 1, polymer, 73 residues, 8300 Da.
Natural source: Common Name: Flu Virus Taxonomy ID: 11320 Superkingdom: Viruses Kingdom: not available Genus/species: Influenza virus A and B group Influenza A Virus
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
Non-structural protein 1: MDSNTVSSFQVDCFLWHVRK
QVVDQELGDAPFLDRLRRDQ
KSLRGRGSTLGLNIEAATHV
GKQIVEKILKEES
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 303 |
| 15N chemical shifts | 85 |
| 1H chemical shifts | 534 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NS1(1-73) subunit 1 | 1 |
| 2 | NS1(1-73) subunit 2 | 1 |
Entities:
Entity 1, NS1(1-73) subunit 1 73 residues - 8300 Da.
| 1 | MET | ASP | SER | ASN | THR | VAL | SER | SER | PHE | GLN | ||||
| 2 | VAL | ASP | CYS | PHE | LEU | TRP | HIS | VAL | ARG | LYS | ||||
| 3 | GLN | VAL | VAL | ASP | GLN | GLU | LEU | GLY | ASP | ALA | ||||
| 4 | PRO | PHE | LEU | ASP | ARG | LEU | ARG | ARG | ASP | GLN | ||||
| 5 | LYS | SER | LEU | ARG | GLY | ARG | GLY | SER | THR | LEU | ||||
| 6 | GLY | LEU | ASN | ILE | GLU | ALA | ALA | THR | HIS | VAL | ||||
| 7 | GLY | LYS | GLN | ILE | VAL | GLU | LYS | ILE | LEU | LYS | ||||
| 8 | GLU | GLU | SER |
Samples:
sample_1: NS1(1-73) dimer 2.0 mM; NH4)Ac 50 mM; D2O 5%; H2O 95%
sample_2: NS1(1-73) dimer, [U-100% 15N], 2.5 mM; NH4)Ac 50 mM; D2O 5%; H2O 95%
sample_3: NS1(1-73) dimer, [U-100% 15N; U-100% 13C], 2.0 mM; NH4)Ac 50 mM; D2O 5%; H2O 95%
condition_1: pH: 6.0 na; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H-15N HSQC | not available | not available | condition_1 |
| HNCO | not available | not available | condition_1 |
| CANH | not available | not available | condition_1 |
| CA(CO)NH | not available | not available | condition_1 |
| H(CA)NH | not available | not available | condition_1 |
| H(CA)(CO)NH | not available | not available | condition_1 |
| CBCANH | not available | not available | condition_1 |
| CBCA(CO)NH | not available | not available | condition_1 |
| HCC(CO)NH-TOCSY | not available | not available | condition_1 |
| HCCH-COSY | not available | not available | condition_1 |
| 4 channel probe with pulse field gradient | not available | not available | condition_1 |
Software:
vnmr v5.3 - Data processing
NMRcompass - Spectra analysis and peakpicking
AUTOASSIGN - 1H, 13C, 15N resonance assignment, Software developed in Montelione lab [Zimmerman et al. (1997) J. Mol. Biol. 269:592-610] for automating the peak assignment
NMR spectrometers:
- Varian . 500 MHz
- Varian . 600 MHz
Related Database Links:
| BMRB | 15117 |
| PDB | |
| DBJ | BAA01428 |
| EMBL | CAA24288 CAC09426 |
| GB | AAA43086 AAA43515 AAA43688 AAC36136 AAC36138 |
| PRF | 2005320B 2005320D |
| SP | P03494 P03495 P69277 P69278 Q1PUD3 |
Download simulated HSQC data in one of the following formats:
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