BMRB Entry 16572
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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/BMR16572
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Title: NMR solution structure of Lamin-B1 protein from Home sapiens: Northeast Structural Genomics Consortium target, HR5546A(438-548)
Deposition date: 2009-10-21 Original release date: 2009-10-22
Authors: Swapna, G. V. T.; Montelione, Gaetano
Citation: Swapna, G. V. T.; Ciccosanti, Colleen; Belote, Rachel; Hamilton, Keith; Acton, Thomas; Huang, Y; Xiao, Rong; Everett, John; Montelione, Gaetano. "NMR solution structure of Lamin-B1 protein from Home sapiens: Northeast Structural Genomics Consortium target, HR5546A(438-548)" To be Published ., .-..
Assembly members:
Lamin-B1_protein, polymer, 122 residues, 13672.427 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Lamin-B1_protein: MGHHHHHHSHMTGNVCIEEI
DVDGKFIRLKNTSEQDQPMG
GWEMIRKIGDTSVSYKYTSR
YVLKAGQTVTIWAANAGVTA
SPPTDLIWKNQNSWGTGEDV
KVILKNSQGEEVAQRSTVFK
TT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 398 |
| 15N chemical shifts | 134 |
| 1H chemical shifts | 824 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Lamin-B1_protein | 1 |
Entities:
Entity 1, Lamin-B1_protein 122 residues - 13672.427 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | THR | GLY | ASN | VAL | CYS | ILE | GLU | GLU | ILE | ||||
| 3 | ASP | VAL | ASP | GLY | LYS | PHE | ILE | ARG | LEU | LYS | ||||
| 4 | ASN | THR | SER | GLU | GLN | ASP | GLN | PRO | MET | GLY | ||||
| 5 | GLY | TRP | GLU | MET | ILE | ARG | LYS | ILE | GLY | ASP | ||||
| 6 | THR | SER | VAL | SER | TYR | LYS | TYR | THR | SER | ARG | ||||
| 7 | TYR | VAL | LEU | LYS | ALA | GLY | GLN | THR | VAL | THR | ||||
| 8 | ILE | TRP | ALA | ALA | ASN | ALA | GLY | VAL | THR | ALA | ||||
| 9 | SER | PRO | PRO | THR | ASP | LEU | ILE | TRP | LYS | ASN | ||||
| 10 | GLN | ASN | SER | TRP | GLY | THR | GLY | GLU | ASP | VAL | ||||
| 11 | LYS | VAL | ILE | LEU | LYS | ASN | SER | GLN | GLY | GLU | ||||
| 12 | GLU | VAL | ALA | GLN | ARG | SER | THR | VAL | PHE | LYS | ||||
| 13 | THR | THR |
Samples:
HR5546A_sample_1: Lamin-B1 protein, [U-100% 13C; U-100% 15N], 1.219 ± 0.20 mM; NH4OAc 20 mM; DTT 100 mM; NaCl 200 mM; CaCl2 5 mM
HR5546A_sample_2: Lamin-B1 protein, [U-5% 13C; U-100% 15N], 1.219 ± 0.20 mM; NH4OAc 20 mM; DTT 100 mM; NaCl 200 mM; CaCl2 5 mM
sample_conditions_1: ionic strength: 205 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 205 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | HR5546A_sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | HR5546A_sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | HR5546A_sample_1 | isotropic | sample_conditions_1 |
| 3D GFT CBCA(CO)NH | HR5546A_sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | HR5546A_sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | HR5546A_sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | HR5546A_sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | HR5546A_sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | HR5546A_sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aro | HR5546A_sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | HR5546A_sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC | HR5546A_sample_2 | isotropic | sample_conditions_2 |
| 2D HNOE | HR5546A_sample_2 | isotropic | sample_conditions_2 |
| 3D (H)CCH-TOCSY | HR5546A_sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | HR5546A_sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliph | HR5546A_sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | HR5546A_sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | HR5546A_sample_1 | isotropic | sample_conditions_1 |
| 3D GFT HNCACB | HR5546A_sample_1 | isotropic | sample_conditions_1 |
Software:
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
AVS, Moseley and Montelione - chemical shift assignment validation
NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v2.3, Goddard - data analysis, peak picking
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution
CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
TOPSPIN v2.1, Bruker Biospin - collection
VNMRJ v2.1, Varian - collection
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAA08784 BAK63580 |
| EMBL | CAA34677 |
| GB | AAB09600 AAC96023 AAH52729 AAH58392 EDL09872 |
| REF | NP_001267370 NP_034851 NP_446357 XP_003259953 XP_003477267 |
| SP | P14733 P70615 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts