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- PDB-2l7h: The solution structure of the HAMP domain of the hypothetical tra... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2l7h | |||||||||
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Title | The solution structure of the HAMP domain of the hypothetical transmembrane receptor Af1503 | |||||||||
![]() | Uncharacterized protein | |||||||||
![]() | SIGNALING PROTEIN / Complementary x-da | |||||||||
Function / homology | ![]() signal transduction / identical protein binding / membrane / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
Model details | minimized average, model 1 | |||||||||
![]() | Coles, M. / Hulko, M. / Martin, J. / Lupas, A.N. | |||||||||
![]() | ![]() Title: The Mechanisms of HAMP-Mediated Signaling in Transmembrane Receptors. Authors: Ferris, H.U. / Dunin-Horkawicz, S. / Mondejar, L.G. / Hulko, M. / Hantke, K. / Martin, J. / Schultz, J.E. / Zeth, K. / Lupas, A.N. / Coles, M. #1: Journal: Cell(Cambridge,Mass.) / Year: 2006 Title: The HAMP domain structure implies helix rotation in transmembrane signaling. Authors: Hulko, M. / Berndt, F. / Gruber, M. / Linder, J.U. / Truffault, V. / Schultz, A. / Martin, J. / Schultz, J.E. / Lupas, A.N. / Coles, M. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 637.4 KB | Display | ![]() |
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PDB format | ![]() | 540.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 399.9 KB | Display | ![]() |
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Full document | ![]() | 571.8 KB | Display | |
Data in XML | ![]() | 28.1 KB | Display | |
Data in CIF | ![]() | 50.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2l7iC ![]() 2y0qC ![]() 2y0tC ![]() 2y20C ![]() 2y21C C: citing same article ( |
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Similar structure data | |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 6421.323 Da / Num. of mol.: 2 / Fragment: HAMP domain residues 278-331 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 |
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Sample conditions | Ionic strength: 150 / pH: 7.2 / Pressure: ambient / Temperature: 308 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: Refinement against a conformational database potential | ||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1063 / NOE intraresidue total count: 195 / NOE long range total count: 168 / NOE medium range total count: 352 / NOE sequential total count: 282 / Protein chi angle constraints total count: 70 / Protein other angle constraints total count: 40 / Protein phi angle constraints total count: 106 / Protein psi angle constraints total count: 104 | ||||||||||||||||||||||||
NMR representative | Selection criteria: minimized average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 18 / Maximum lower distance constraint violation: 0.08 Å / Maximum torsion angle constraint violation: 0.4 ° / Maximum upper distance constraint violation: 0.09 Å | ||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.01 Å / Distance rms dev error: 0.0005 Å |