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- PDB-2hhi: The solution structure of antigen MPT64 from Mycobacterium tuberc... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2hhi | ||||||
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Title | The solution structure of antigen MPT64 from Mycobacterium tuberculosis defines a novel class of beta-grasp proteins | ||||||
![]() | Immunogenic protein MPT64 | ||||||
![]() | UNKNOWN FUNCTION / MPT64 / Secreted Antigen / Tuberculosis / Residual Dipolar Coupling / NMR Solution Structure / beta-grasp | ||||||
Function / homology | ![]() zymogen binding / cell wall / cellular response to starvation / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / Torsion Angle Dynamics, RDC refinement using CNS 1.1 | ||||||
![]() | Wang, Z. / Potter, B.M. / Gray, A.M. / Sacksteder, K.A. / Geisbrecht, B.V. / Laity, J.H. | ||||||
![]() | ![]() Title: The Solution Structure of Antigen MPT64 from Mycobacterium tuberculosis Defines a New Family of Beta-Grasp Proteins. Authors: Wang, Z. / Potter, B.M. / Gray, A.M. / Sacksteder, K.A. / Geisbrecht, B.V. / Laity, J.H. #1: ![]() Title: Design and optimization of a recombinant system for large-scale production of the MPT64 antigen from Mycobacterium tuberculosis. Authors: Geisbrecht, B.V. / Nikonenko, B. / Samala, R. / Nakamura, R. / Nacy, C.A. / Sacksteder, K.A. #2: ![]() Title: NMR assignment of protein Rv1980c from Mycobacterium tuberculosis Authors: Danahy, J.M. / Potter, B.M. / Geisbrecht, B.V. / Laity, J.H. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.4 MB | Display | ![]() |
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PDB format | ![]() | 1.2 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 361.6 KB | Display | ![]() |
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Full document | ![]() | 684.6 KB | Display | |
Data in XML | ![]() | 269.6 KB | Display | |
Data in CIF | ![]() | 358.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 22375.855 Da / Num. of mol.: 1 / Fragment: Recombinant form of mature polypeptide Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details |
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Sample conditions | Ionic strength: no salt / pH: 6.9 / Temperature: 303 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: Torsion Angle Dynamics, RDC refinement using CNS 1.1 Software ordinal: 1 Details: The initial structures were calculated through TAD protocol of CNS with 3761 NOE-derived distance contraints and 292 dihedral angle restraints. The final structures were refined using JNH ...Details: The initial structures were calculated through TAD protocol of CNS with 3761 NOE-derived distance contraints and 292 dihedral angle restraints. The final structures were refined using JNH and JCaCO Residual Dipolar Coupling (RDC) in Cartesian space with same NOE, dihedral angle restraints and 139 JNH RDCs and 114 JCaCO RDCs from stretched gel. | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 24 |