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Open data
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Basic information
| Entry | Database: PDB / ID: 9mqo | ||||||
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| Title | Crystal structure of BCMA in complex with CA10v2 Fab | ||||||
Components |
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Keywords | IMMUNE SYSTEM / antibody / B-cell receptor / BCMA | ||||||
| Function / homology | Function and homology informationlymphocyte homeostasis / TNFs bind their physiological receptors / endomembrane system / tumor necrosis factor-mediated signaling pathway / signaling receptor activity / adaptive immune response / signal transduction / membrane / plasma membrane Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.181 Å | ||||||
Authors | Qiu, Y. | ||||||
| Funding support | 1items
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Citation | Journal: To Be PublishedTitle: Crystal structure of BCMA in complex with CA10v2 Fab Authors: Qiu, Y. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9mqo.cif.gz | 513.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9mqo.ent.gz | 424.3 KB | Display | PDB format |
| PDBx/mmJSON format | 9mqo.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mq/9mqo ftp://data.pdbj.org/pub/pdb/validation_reports/mq/9mqo | HTTPS FTP |
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-Related structure data
| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
| #1: Protein | Mass: 6057.875 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Details: BCMA was produced as GST-PreScission-BCMA (1-54) in E. Coli BCMA was prepared by PreScission cleavage, followed by GST and SEC purification Source: (gene. exp.) Homo sapiens (human) / Gene: TNFRSF17, BCM, BCMA / Production host: ![]() #2: Antibody | Mass: 25949.916 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human)#3: Antibody | Mass: 23094.582 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human)Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 2.45 Å3/Da / Density % sol: 49.76 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 0.18 M Sodium Chloride, 0.09 M Phosphate/citrate pH 4.2, 20 % w/v PEG 8000, 0.1M Sodium Malonate |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.97949 Å |
| Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jan 24, 2020 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.97949 Å / Relative weight: 1 |
| Reflection | Resolution: 3.18→84.15 Å / Num. obs: 53814 / % possible obs: 98.4 % / Redundancy: 1.9 % / Rrim(I) all: 0.235 / Net I/σ(I): 1.9 |
| Reflection shell | Resolution: 3.18→3.27 Å / Redundancy: 1.9 % / Mean I/σ(I) obs: 0.7 / Num. unique obs: 3972 / Rrim(I) all: 0.595 / % possible all: 98.2 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.181→83.847 Å / Cross valid method: FREE R-VALUE
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| Refinement step | Cycle: LAST / Resolution: 3.181→83.847 Å
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About Yorodumi




Homo sapiens (human)
X-RAY DIFFRACTION
Citation
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