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- PDB-1tle: LE (LAMININ-TYPE EGF-LIKE) MODULE GIII4 IN SOLUTION AT PH 3.5 AND... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tle | ||||||
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Title | LE (LAMININ-TYPE EGF-LIKE) MODULE GIII4 IN SOLUTION AT PH 3.5 AND 290 K, NMR, 14 STRUCTURES | ||||||
![]() | LAMININ![]() | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Baumgartner, R. / Czisch, M. / Mayer, U. / Schl, E.P. / Huber, R. / Timpl, R. / Holak, T.A. | ||||||
![]() | ![]() Title: Structure of the nidogen binding LE module of the laminin gamma1 chain in solution. Authors: Baumgartner, R. / Czisch, M. / Mayer, U. / Poschl, E. / Huber, R. / Timpl, R. / Holak, T.A. #1: ![]() Title: Two Non-Contiguous Regions Contribute to Nidogen Binding to a Single Egf-Like Motif of the Laminin Gamma 1 Chain Authors: Poschl, E. / Fox, J.W. / Block, D. / Mayer, U. / Timpl, R. #2: ![]() Title: A Single Egf-Like Motif of Laminin is Responsible for High Affinity Nidogen Binding Authors: Mayer, U. / Nischt, R. / Poschl, E. / Mann, K. / Fukuda, K. / Gerl, M. / Yamada, Y. / Timpl, R. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 237.1 KB | Display | ![]() |
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PDB format | ![]() | 205.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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: 6352.206 Da / Num. of mol.: 1 Fragment: NIDOGEN BINDING LE MODULE OF THE LAMININ GAMMA1 CHAIN, MODULE GIII4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Sample conditions | pH: 3.5 / Temperature: 290 K |
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Crystal grow![]() | *PLUS Method: other / Details: NMR |
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Processing
Software |
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NMR software | Name: ![]() | ||||||||||||
NMR ensemble | Conformers submitted total number: 14 |