BMRB Entry 15568
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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/BMR15568
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Title: Solution NMR Structure of uncharacterized Lipoprotein B from Nitrosomona europaea. Northeast Structural Genomics Target NeR45A.
Deposition date: 2007-11-27 Original release date: 2007-12-11
Authors: Rossi, Paolo; Wang, Dongyan; Janjua, Haleema; Owens, Leah; Xiao, Rong; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation: Rossi, Paolo; Xiao, Rong; Acton, Thomas; Montelione, Gaetano. "Solution NMR Structure of Uncharacterized Lipoprotein B from Nitrosomona europaea. Northeast Structural Genomics Target NeR45A." . ., .-..
Assembly members:
NeR45A, polymer, 155 residues, 17617.432 Da.
Natural source: Common Name: Nitrosomonas europaea Taxonomy ID: 915 Superkingdom: Bacteria Kingdom: not available Genus/species: Nitrosomonas europaea
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NeR45A: MGFKLRGQVSELPFERVYIT
APAGLTIGSDLERVISTHTR
AKVVNKAEKSEAIIQIVHAI
REKRILSLSESGRVREFELV
YRVAARLLDAHNAELASLQE
IRLTRILPFLDAQELAKAAE
EEMLYKDMQKDAVQQILRQV
SAFTSAGLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 650 |
| 15N chemical shifts | 153 |
| 1H chemical shifts | 1056 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NeR45A | 1 |
Entities:
Entity 1, NeR45A 155 residues - 17617.432 Da.
UniProtKB/TrEMBL ID: Q82VF2_NITEU with trucncated transmembrane region C-term HisTag (LEHHHHHH)
| 1 | MET | GLY | PHE | LYS | LEU | ARG | GLY | GLN | VAL | SER | ||||
| 2 | GLU | LEU | PRO | PHE | GLU | ARG | VAL | TYR | ILE | THR | ||||
| 3 | ALA | PRO | ALA | GLY | LEU | THR | ILE | GLY | SER | ASP | ||||
| 4 | LEU | GLU | ARG | VAL | ILE | SER | THR | HIS | THR | ARG | ||||
| 5 | ALA | LYS | VAL | VAL | ASN | LYS | ALA | GLU | LYS | SER | ||||
| 6 | GLU | ALA | ILE | ILE | GLN | ILE | VAL | HIS | ALA | ILE | ||||
| 7 | ARG | GLU | LYS | ARG | ILE | LEU | SER | LEU | SER | GLU | ||||
| 8 | SER | GLY | ARG | VAL | ARG | GLU | PHE | GLU | LEU | VAL | ||||
| 9 | TYR | ARG | VAL | ALA | ALA | ARG | LEU | LEU | ASP | ALA | ||||
| 10 | HIS | ASN | ALA | GLU | LEU | ALA | SER | LEU | GLN | GLU | ||||
| 11 | ILE | ARG | LEU | THR | ARG | ILE | LEU | PRO | PHE | LEU | ||||
| 12 | ASP | ALA | GLN | GLU | LEU | ALA | LYS | ALA | ALA | GLU | ||||
| 13 | GLU | GLU | MET | LEU | TYR | LYS | ASP | MET | GLN | LYS | ||||
| 14 | ASP | ALA | VAL | GLN | GLN | ILE | LEU | ARG | GLN | VAL | ||||
| 15 | SER | ALA | PHE | THR | SER | ALA | GLY | LEU | GLU | HIS | ||||
| 16 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: entity 1 mM; MES 20 mM; calcium chloride 5 mM; DTT 100 mM; sodium chloride 100 mM; sodium azide 0.02%; D2O, [U-100% 2H], 5%; H2O 95%
sample_2: entity 0.86 mM; MES 20 mM; calcium chloride 5 mM; DTT 100 mM; sodium chloride 100 mM; sodium azide 0.02%; D2O, [U-100% 2H], 100%
sample_3: entity 1.3 mM; MES 20 mM; calcium chloride 5 mM; DTT 100 mM; sodium chloride 100 mM; sodium azide 0.02%; D2O, [U-100% 2H], 5%; H2O 95%
sample_conditions_1: ionic strength: 0.1 M; 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 (aliph) | 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 HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D SIMULTANEOUS 15N-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (arom) | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AutoAssign v2.4, Zimmerman, Moseley, Kulikowski and Montelione - backbone chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PSVS v1.3, Bhattacharya and Montelione - validation
SPARKY v3.112, Goddard - data analysis
TOPSPIN v1.3, Bruker Biospin - collection
Molmol v2.2, Koradi, Billeter and Wuthrich - visualization
RPF v2.1.1, Huang, Powers and Montelione - validation
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Th - validation
MolProbity, Richardson - validation
XEASY, Bartels et al. - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts