BMRB Entry 16376
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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/BMR16376
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Title: Solution NMR structure of the monomeric W187R mutant of A/Udorn NS1 effector domain. Northeast Structural Genomics target OR8C[W187R].
Deposition date: 2009-06-29 Original release date: 2009-07-06
Authors: Aramini, James; Ma, Li-Chung; Lee, Hsiau-Wei; Zhao, Li; Cunningham, Kellie; Ciccosanti, Colleen; Janjua, Haleema; Fang, Yingyi; Xiao, Rong; Krug, Robert; Montelione, Gaetano
Citation: Aramini, James; Ma, Li-Chung; Lee, Hsiau-Wei; Zhao, Li; Cunningham, Kellie; Ciccosanti, Colleen; Janjua, Haleema; Fang, Yingyi; Xiao, Rong; Krug, Robert; Montelione, Gaetano. "Solution NMR structure of the monomeric W187R mutant of A/Udorn NS1 effector domain. Northeast Structural Genomics target OR8C[W187R]." Not known ., .-..
Assembly members:
OR8w187r, polymer, 140 residues, 15935.479 Da.
Natural source: Common Name: Influenzavirus A Taxonomy ID: 197911 Superkingdom: Viruses Kingdom: not available Genus/species: Influenza A not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
OR8w187r: MPASRYITDMTIEELSRDWF
MLMPKQKVEGPLCIRIDQAI
MDKNIMLKANFSVIFDRLET
LILLRAFTEEGAIVGEISPL
PSFPGHTIEDVKNAIGVLIG
GLERNDNTVRVSKTLQRFAW
GSSNENGRPPLTLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 614 |
| 15N chemical shifts | 139 |
| 1H chemical shifts | 988 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | OR8w187r | 1 |
Entities:
Entity 1, OR8w187r 140 residues - 15935.479 Da.
| 1 | MET | PRO | ALA | SER | ARG | TYR | ILE | THR | ASP | MET | |
| 2 | THR | ILE | GLU | GLU | LEU | SER | ARG | ASP | TRP | PHE | |
| 3 | MET | LEU | MET | PRO | LYS | GLN | LYS | VAL | GLU | GLY | |
| 4 | PRO | LEU | CYS | ILE | ARG | ILE | ASP | GLN | ALA | ILE | |
| 5 | MET | ASP | LYS | ASN | ILE | MET | LEU | LYS | ALA | ASN | |
| 6 | PHE | SER | VAL | ILE | PHE | ASP | ARG | LEU | GLU | THR | |
| 7 | LEU | ILE | LEU | LEU | ARG | ALA | PHE | THR | GLU | GLU | |
| 8 | GLY | ALA | ILE | VAL | GLY | GLU | ILE | SER | PRO | LEU | |
| 9 | PRO | SER | PHE | PRO | GLY | HIS | THR | ILE | GLU | ASP | |
| 10 | VAL | LYS | ASN | ALA | ILE | GLY | VAL | LEU | ILE | GLY | |
| 11 | GLY | LEU | GLU | ARG | ASN | ASP | ASN | THR | VAL | ARG | |
| 12 | VAL | SER | LYS | THR | LEU | GLN | ARG | PHE | ALA | TRP | |
| 13 | GLY | SER | SER | ASN | GLU | ASN | GLY | ARG | PRO | PRO | |
| 14 | LEU | THR | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: OR8w187r, [U-100% 13C; U-100% 15N], 0.71 mM; sodium phosphate 20 mM; sodium chloride 100 mM; arginine 50 mM; glutamic acid 50 mM; glycerol 1%; DSS 50 uM
sample_2: OR8w187r, [U-5% 13C; U-100% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 100 mM; arginine 50 mM; glutamic acid 50 mM; glycerol 1%; DSS 50 uM
sample_conditions_1: ionic strength: 0.1 M; pH: 6.9; pressure: 1.0 atm; temperature: 300 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_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D simultaneous CN NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC high resolution (L/V methyl stereoassignment) | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N hetNOE | sample_2 | isotropic | sample_conditions_1 |
| 1D 1H-15N T1 and T2 | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY (RDCs) | sample_2 | anisotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, data analysis
SPARKY v3.112, Goddard - data analysis, peak picking
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, validation
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - RPF analysis
PSVS v1.3, Bhattacharya and Montelione - structure quality analysis
MolProbity v3.15, Richardson - structure quality analysis
PDBStat v5.1, Tejero and Montelione - PDB analysis
TALOS vplus, Cornilescu, Delaglio and Bax - dihedral angle constraints
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAJ13312 |
| EMBL | CAA24288 |
| GB | AAC36138 AAO46755 AAO46757 AAO46759 AAO46765 |
| SP | P03495 Q1PUD3 Q288Z0 Q2ICQ4 Q2RFA0 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts