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Article title matches
- Category:Wild-type cd38 bound with n1-cidpr (65 bytes)
1: List of pages with the keyword Wild-type cd38 bound with n1-cidpr - Category:Wild-type amtb (45 bytes)
1: List of pages with the keyword Wild-type amtb - Category:Wild type protease (49 bytes)
1: List of pages with the keyword Wild type protease - Category:Wild type (40 bytes)
1: List of pages with the keyword Wild type - Category:Recombinant wild type (52 bytes)
1: List of pages with the keyword Recombinant wild type - Category:Wild type humand dhfr (52 bytes)
1: List of pages with the keyword Wild type humand dhfr - Category:Wild-type (40 bytes)
1: List of pages with the keyword Wild-type - Category:Wild type heme protein (53 bytes)
1: List of pages with the keyword Wild type heme protein - Category:Wild type enzyme (47 bytes)
1: List of pages with the keyword Wild type enzyme - Category:Wild type sequence (49 bytes)
1: List of pages with the keyword Wild type sequence - Category:Wild type subtype b hiv protease (63 bytes)
1: List of pages with the keyword Wild type subtype b hiv protease - Category:Wild type subtype f hiv protease (63 bytes)
1: List of pages with the keyword Wild type subtype f hiv protease - Category:Wild-type-selenomethionine substituted (69 bytes)
1: List of pages with the keyword Wild-type-selenomethionine substituted - Image:Wild own.pdb (0 bytes)
- Category:Structure comparison with the wild type fragment (79 bytes)
1: ...es with the keyword Structure comparison with the wild type fragment - Category:Human wild-type transthyretin (60 bytes)
1: List of pages with the keyword Human wild-type transthyretin - Category:Human wild type dhfr active site inhibitor (73 bytes)
1: List of pages with the keyword Human wild type dhfr active site inhibitor - Category:Nt wild-type (43 bytes)
1: List of pages with the keyword Nt wild-type - Image:1EA5 Wild type align.pdb (0 bytes)
- Category:Wild-type hiv-1 protease (55 bytes)
1: List of pages with the keyword Wild-type hiv-1 protease
Page text matches
- 117e (5,307 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...boxylate group is positioned where Wat1 is in the wild-type: the potent Wat1 nucleophile is replaced by ... - 1e4v (4,128 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...ide result we find that mutant Pro-9-->Leu and wild-type form one very similar crystal packing contac... - 1e4y (4,127 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...ide result we find that mutant Pro-9-->Leu and wild-type form one very similar crystal packing contac... - 1vyr (5,031 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...he mutant enzymes is substantially different from wild-type enzyme. Implications for the mechanism of hi... - 1vyp (5,049 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...he mutant enzymes is substantially different from wild-type enzyme. Implications for the mechanism of hi... - 1vys (5,048 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...he mutant enzymes is substantially different from wild-type enzyme. Implications for the mechanism of hi... - 1nvg (3,945 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...increased catalytic activity when compared to the wild-type enzyme. The substitution, located in the coe... - 1rrl (4,805 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...-throughput rigid docking. Data were analyzed for wild soybean lipoxygenase-3 (MW 97 kDa) at 293 and 93 ... - 1rrh (4,819 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...-throughput rigid docking. Data were analyzed for wild soybean lipoxygenase-3 (MW 97 kDa) at 293 and 93 ... - 1boh (5,329 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...wed that Delta1-7 crystallized isomorphously with wild type in polyethyleneglycol, and the structure was... - 1boi (5,313 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...wed that Delta1-7 crystallized isomorphously with wild type in polyethyleneglycol, and the structure was... - 2cnc (5,285 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ... in productive substrate binding, the activity of wild-type CmXyn10B, the mutant A334V/G348D, and severa... - 1xik (5,245 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...ough the iron coordination is very similar to the wild type protein. CONCLUSIONS. Carboxylate shifts are... - 1pfr (5,243 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...ough the iron coordination is very similar to the wild type protein. CONCLUSIONS. Carboxylate shifts are... - 1wcq (4,443 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...nificant active-site perturbation relative to the wild-type enzyme. - 3pcd (5,907 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ... from those of the analogous intermediates of the wild-type enzyme cycle, while all of the other observe... - 2jaz (5,113 bytes)
5: ...ttps://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._W3110 Escherichia coli str. K-12 subst...
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ... H573 is responsible for metal ion binding in the wild-type protein, as the zinc ion is still partially ... - 2jag (4,837 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...CB1 site was found at the same position as in the wild type structure. In addition, a second chloride bi... - 2jaf (4,833 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...CB1 site was found at the same position as in the wild type structure. In addition, a second chloride bi... - 1gkj (4,171 bytes)
13: [[Image:Consurf_key_small.gif|200px|right]]
24: ...t the conformational barrier between aromatic and wild-type states is very low. The data led to a new pr...
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