BMRB Entry 17842
Click here to enlarge.
            
                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/BMR17842
MolProbity Validation Chart            
                    NMR-STAR file interactive viewer.
                    NMR-STAR v3 text file.
                    NMR-STAR v2.1 text file (deprecated)
                    XML gzip file.
                    RDF gzip file.
                    All files associated with the entry
                
Title: Solution structure of outer membrane protein H (OprH) from P. aeruginosa in DHPC micelles. PubMed: 21865172
Deposition date: 2011-08-08 Original release date: 2011-08-25
Authors: Edrington, Thomas; Tamm, Lukas
Citation: Edrington, Thomas; Kintz, Erica; Goldberg, Joanna; Tamm, Lukas. "Structural basis for the interaction of lipopolysaccharide with outer membrane protein H (OprH) from Pseudomonas aeruginosa." J. Biol. Chem. 286, 39211-39223 (2011).
Assembly members:
entity, polymer, 179 residues,   19620.729 Da.
Natural source: Common Name: Pseudomonas aeruginosa Taxonomy ID: 287 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas Aeruginosa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: ADNFVGLTWGETSNNIQKSK
SLNRNLNSPNLDKVIDNTGT
WGIRAGQQFEQGRYYATYEN
ISDTSSGNKLRQQNLLGSYD
AFLPIGDNNTKLFGGATLGL
VKLEQDGKGFKRDSDVGYAA
GLQAGILQELSKNASIEGGY
RYLRTNASTEMTPHGGNKLG
SLDLHSSSQFYLGANYKFL
- assigned_chemical_shifts
 
| Data type | Count | 
| 13C chemical shifts | 475 | 
| 15N chemical shifts | 156 | 
| 1H chemical shifts | 156 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | OprH | 1 | 
Entities:
Entity 1, OprH 179 residues - 19620.729 Da.
| 1 | ALA | ASP | ASN | PHE | VAL | GLY | LEU | THR | TRP | GLY | ||||
| 2 | GLU | THR | SER | ASN | ASN | ILE | GLN | LYS | SER | LYS | ||||
| 3 | SER | LEU | ASN | ARG | ASN | LEU | ASN | SER | PRO | ASN | ||||
| 4 | LEU | ASP | LYS | VAL | ILE | ASP | ASN | THR | GLY | THR | ||||
| 5 | TRP | GLY | ILE | ARG | ALA | GLY | GLN | GLN | PHE | GLU | ||||
| 6 | GLN | GLY | ARG | TYR | TYR | ALA | THR | TYR | GLU | ASN | ||||
| 7 | ILE | SER | ASP | THR | SER | SER | GLY | ASN | LYS | LEU | ||||
| 8 | ARG | GLN | GLN | ASN | LEU | LEU | GLY | SER | TYR | ASP | ||||
| 9 | ALA | PHE | LEU | PRO | ILE | GLY | ASP | ASN | ASN | THR | ||||
| 10 | LYS | LEU | PHE | GLY | GLY | ALA | THR | LEU | GLY | LEU | ||||
| 11 | VAL | LYS | LEU | GLU | GLN | ASP | GLY | LYS | GLY | PHE | ||||
| 12 | LYS | ARG | ASP | SER | ASP | VAL | GLY | TYR | ALA | ALA | ||||
| 13 | GLY | LEU | GLN | ALA | GLY | ILE | LEU | GLN | GLU | LEU | ||||
| 14 | SER | LYS | ASN | ALA | SER | ILE | GLU | GLY | GLY | TYR | ||||
| 15 | ARG | TYR | LEU | ARG | THR | ASN | ALA | SER | THR | GLU | ||||
| 16 | MET | THR | PRO | HIS | GLY | GLY | ASN | LYS | LEU | GLY | ||||
| 17 | SER | LEU | ASP | LEU | HIS | SER | SER | SER | GLN | PHE | ||||
| 18 | TYR | LEU | GLY | ALA | ASN | TYR | LYS | PHE | LEU | 
Samples:
sample_1: OprH, [U-13C; U-15N; U-2H], 1.0 mM; sodium phosphate 25 mM; potassium chloride 50 mM; sodium azide 0.05%
sample_conditions_1: pH: 6.1; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions | 
|---|---|---|---|
| 2D 1H-15N HSQC-TROSY | 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)CB | sample_1 | isotropic | sample_conditions_1 | 
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 | 
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 | 
| 3D H(CA)CO | sample_1 | isotropic | sample_conditions_1 | 
| 3D 1H-15N NOESY-TROSY | sample_1 | isotropic | sample_conditions_1 | 
| 3D 1H-15N NOESY-TROSY-NOESY | sample_1 | isotropic | sample_conditions_1 | 
Software:
CNS, Brunger A. T. et.al. - refinement
NMR spectrometers:
- Bruker Avance III 800 MHz
 
Related Database Links:
| PDB | |
| DBJ | BAK88910 BAP20537 BAP52118 BAQ41215 BAR69069 | 
| EMBL | CAW28898 CCQ86522 CDH72267 CDH78538 CDI89324 | 
| GB | AAA25911 AAG04567 AAT50763 ABJ10346 ABR84660 | 
| REF | NP_249869 WP_003082431 WP_012076667 WP_024915192 WP_031670686 | 
Download simulated HSQC data in one of the following formats:
            
CSV: Backbone
            or all simulated shifts
            
SPARKY: Backbone
            or all simulated shifts