Dino Tracker
Dtelnet is a free telnet client for Windows 3.1/95/NT. And it comes with source! Sourceforge has many advanced tools (forums. A new option to map editing keys. Attention: AdvanceMap 1.95 is currently only a BETA-Release, and there are not all functions in, that should be there. So be careful and make regular Backups!!! But now the the Facts. New important features: - 7digit / Extended Rom Support. Connection window with preview & move Connection in preview.
Re-download advance map, and dont move any files around. OP ShinyJellicent12 GBAtemp Advanced Fan. Joined: Mar 21, 2011 Messages: 709.
We have spent much time to really make the whole plugin much easier to use and simpler to understand by implementing a better way of searching which will always display something instead of an empty result. The whole code has been rebuilt from scratch and tested thoroughly, and we received positive feedback from it. For example, you can now use /track to list the name of all your dinos on the map and browse through the different pages. You can do a partial name search for your own dinos, so /track breed would let you locate a dino named 'Breeder M'. You can use friendly names when searching for a specific species of dinos, for example /track bulbdog (or /track bulb) will let you locate your bulbdogs, instead of having to find the correct Dino Tag.Upcoming Premium Features:
Advance Map 1.95 Download
- Wild Dino Tracker
- Tracking Arrow
- More to be announced
- Auto map coords detection
- Track tames
- Admin track tames
- Simplified search engine (search on dino name, dino type, dino friendly name)
- Search results notification list + pagination system
- Customizable search results (colors, distance, coords, level, etc)
- Customizable commands
- Customizable messages
- ArkShop integration
- TokenBank integration
- Permissions integration
- /dt.reload - Reloads config
- /track - Tracks your tamed dinos
- /trackadmin - Tracks any tribe dinos for admins only
- dt.reload - Reloads config
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Water-molecule network and active-site flexibility of apo protein tyrosine phosphatase 1B.
Pedersen, A.K., Peters G, G.H., Moller, K.B., Iversen, L.F., Kastrup, J.S.
Advance Map 1.95 Download Windows 7
(2004) Acta Crystallogr D Biol Crystallogr 60: 1527-1534
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- PubMed: 15333922Search on PubMed
- DOI: 10.1107/S0907444904015094
- Primary Citation of Related Structures:
1SUG - PubMed Abstract:
- Crystal structure of human protein tyrosine phosphatase 1B
Barford, D., Flint, A.J., Tonks, N.K.
(1994) Science 263: 1397 - Affinity purification of recombinant protein-tyrosine phosphatase 1B using a highly selective inhibitor
Pedersen, A.K., Branner, S., Mortensen, S.B., Andersen, H.S., Klausen, K.M., Moller, K.B., Moller, N.P., Iversen, L.F.
(2004) J Chromatogr B Analyt Technol Biomed Life Sci 799: 1
Protein tyrosine phosphatase 1B (PTP1B) plays a key role as a negative regulator of insulin and leptin signalling and is therefore considered to be an important molecular target for the treatment of type 2 diabetes and obesity. Detailed structural information about the structure of PTP1B, including the conformation and flexibility of active-site residues as well as the water-molecule network, is a key issue in understanding ligand binding and enzyme kinetics and in structure-based drug design ...
Protein tyrosine phosphatase 1B (PTP1B) plays a key role as a negative regulator of insulin and leptin signalling and is therefore considered to be an important molecular target for the treatment of type 2 diabetes and obesity. Detailed structural information about the structure of PTP1B, including the conformation and flexibility of active-site residues as well as the water-molecule network, is a key issue in understanding ligand binding and enzyme kinetics and in structure-based drug design. A 1.95 A apo PTP1B structure has been obtained, showing four highly coordinated water molecules in the active-site pocket of the enzyme; hence, the active site is highly solvated in the apo state. Three of the water molecules are located at positions that approximately correspond to the positions of the phosphate O atoms of the natural substrate phosphotyrosine and form a similar network of hydrogen bonds. The active-site WPD-loop was found to be in the closed conformation, in contrast to previous observations of wild-type PTPs in the apo state, in which the WPD-loop is open. The closed conformation is stabilized by a network of hydrogen bonds. These results provide new insights into and understanding of the active site of PTP1B and form a novel basis for structure-based inhibitor design.
Related Citations:Protein Science, Novo Nordisk, DK-2880 Bagsvaerd, Denmark.