Found 808 chains in Knotoided chains table. Displaying 451 - 600. Applied filters: Probabilistic

Search results query: topological notation for knotoids: K 3.1, 2.1

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#pdbid|chain|deposition date|is S/K-not|(slip)knot types;
      
  7edc|A|2022-05-16|K|3.1 2.1;
  7e3r|A|2022-05-11|K|3.1 2.1;
  7cww|A|2021-11-23|K|3.1 2.1;
  7onu|F|2021-10-06|K|3.1 2.1;
  7myq|A|2021-07-16|K|3.1 2.1;
  7mys|A|2021-07-16|K|3.1 2.1;
  2fg7|C|2021-05-10|K|3.1 2.1;
  6km5|A|2020-08-20|K|3.1 2.1;
  6sdt|A|2020-08-05|K|3.1 2.1;
  6t9z|A|2020-08-05|K|3.1 2.1;
  6ouh|A|2020-08-04|K|3.1 2.1;
  6oub|A|2020-08-04|K|3.1 2.1;
  6r6y|A|2020-04-17|K|3.1 2.1;
  6r71|A|2020-04-17|K|3.1 2.1;
  6ugz|A|2020-04-02|K|3.1 2.1;
  6ugp|A|2020-04-02|K|3.1 2.1;
  6ugr|A|2020-04-02|K|3.1 2.1;
  6vkg|A|2020-04-02|K|3.1 2.1;
  6ugn|A|2020-04-02|K|3.1 2.1;
  6ugq|A|2020-04-02|K|3.1 2.1;
  6ugo|A|2020-04-02|K|3.1 2.1;
  6uh0|A|2020-04-02|K|3.1 2.1;
  6vj3|A|2020-04-02|K|3.1 2.1;
  6pea|A|2020-03-30|K|3.1 2.1;
  6r6f|A|2020-03-30|K|3.1 2.1;
  6pdv|A|2020-03-30|K|3.1 2.1;
  6qng|A|2020-03-30|K|3.1 2.1;
  6qnl|A|2020-03-30|K|3.1 2.1;
  6qn6|A|2020-03-08|K|3.1 2.1;
  6qn5|A|2020-03-08|K|3.1 2.1;
  6qn2|A|2020-03-08|K|3.1 2.1;
  6qn0|A|2020-03-08|K|3.1 2.1;
  6u4q|A|2020-01-29|K|3.1 2.1;
  6u4t|A|2020-01-29|K|3.1 2.1;
  6nlv|A|2020-01-22|K|3.1 2.1;
  6nm0|A|2020-01-22|K|3.1 2.1;
  6i0w|A|2019-11-28|K|3.1 2.1;
  6i1u|A|2019-11-28|K|3.1 2.1;
  6i2f|A|2019-11-28|K|3.1 2.1;
  6qqm|A|2019-11-15|K|3.1 2.1;
  6hxd|A|2019-11-07|K|3.1 2.1;
  6qqr|A|2019-10-18|K|3.1 2.1;
  6qqq|A|2019-10-18|K|3.1 2.1;
  6qre|A|2019-10-18|K|3.1 2.1;
  6qrd|A|2019-10-18|K|3.1 2.1;
  6qr3|A|2019-10-18|K|3.1 2.1;
  6qr1|A|2019-10-18|K|3.1 2.1;
  6qrf|A|2019-10-18|K|3.1 2.1;
  6qqv|A|2019-10-18|K|3.1 2.1;
  6qr0|A|2019-10-18|K|3.1 2.1;
  6qr2|A|2019-10-18|K|3.1 2.1;
  6qqt|A|2019-10-18|K|3.1 2.1;
  6qqz|A|2019-10-18|K|3.1 2.1;
  6qqw|A|2019-10-18|K|3.1 2.1;
  6qra|A|2019-10-18|K|3.1 2.1;
  6uev|A|2019-10-18|K|3.1 2.1;
  6ql1|A|2019-10-18|K|3.1 2.1;
  6nj2|A|2019-10-18|K|3.1 2.1;
  6nj3|A|2019-10-18|K|3.1 2.1;
  6ql3|A|2019-10-18|K|3.1 2.1;
  6ql2|A|2019-10-18|K|3.1 2.1;
  6nj6|A|2019-10-18|K|3.1 2.1;
  6hr3|A|2019-10-18|K|3.1 2.1;
  6nj5|A|2019-10-18|K|3.1 2.1;
  6nj4|A|2019-10-18|K|3.1 2.1;
  6hzx|A|2019-09-25|K|3.1 2.1;
  6rqn|A|2019-09-24|K|3.1 2.1;
  6rqq|A|2019-09-24|K|3.1 2.1;
  6ac6|A|2019-09-22|K|3.1 2.1;
  6rxt|CN|2019-09-07|K|3.1 2.1;
  6afk|A|2019-09-07|K|3.1 2.1;
  6gdc|A|2019-05-10|K|3.1 2.1;
  6g6t|A|2019-03-22|K|3.1 2.1;
  6g5u|A|2019-03-22|K|3.1 2.1;
  6gcy|A|2019-03-22|K|3.1 2.1;
  6fji|A|2019-03-22|K|3.1 2.1;
  6h38|A|2019-03-22|K|3.1 2.1;
  6fjj|A|2019-03-22|K|3.1 2.1;
  6mby|A|2019-03-22|K|3.1 2.1;
  6mbv|A|2019-03-22|K|3.1 2.1;
  6g5l|A|2019-03-22|K|3.1 2.1;
  6g7a|A|2019-03-22|K|3.1 2.1;
  6h6s|A|2019-01-16|K|3.1 2.1;
  6h37|A|2019-01-09|K|3.1 2.1;
  6h36|A|2019-01-09|K|3.1 2.1;
  6hwz|A|2019-01-09|K|3.1 2.1;
  6hx5|A|2019-01-09|K|3.1 2.1;
  6eea|A|2018-12-02|K|3.1 2.1;
  6ebe|A|2018-12-02|K|3.1 2.1;
  6eda|A|2018-12-02|K|3.1 2.1;
  6eeo|A|2018-12-02|K|3.1 2.1;
  6eeh|A|2018-12-02|K|3.1 2.1;
  6ecz|A|2018-12-02|K|3.1 2.1;
  6g3q|A|2018-12-02|K|3.1 2.1;
  5thi|A|2018-10-25|K|3.1 2.1;
  4knj|A|2018-10-21|K|3.1 2.1;
  4qiz|A|2018-10-21|K|3.1 2.1;
  1bn1|A|2018-10-21|K|3.1 2.1;
  5n25|A|2018-10-21|K|3.1 2.1;
  5ohh|A|2018-10-21|K|3.1 2.1;
  1cak|A|2018-10-21|K|3.1 2.1;
  1rzb|A|2018-10-21|K|3.1 2.1;
  4qsj|A|2018-10-21|K|3.1 2.1;
  1bv3|A|2018-10-21|K|3.1 2.1;
  1ttm|A|2018-10-21|K|3.1 2.1;
  5nea|A|2018-10-21|K|3.1 2.1;
  5fl5|A|2018-10-21|K|3.1 2.1;
  1bnn|A|2018-10-21|K|3.1 2.1;
  4ygl|A|2018-10-21|K|3.1 2.1;
  3iqk|A|2018-10-21|K|3.1 2.1;
  6b59|A|2018-10-21|K|3.1 2.1;
  5e2s|A|2018-10-20|K|3.1 2.1;
  2gd8|A|2018-10-20|K|3.1 2.1;
  6equ|A|2018-10-20|K|3.1 2.1;
  5jgs|B|2018-10-20|K|3.1 2.1;
  5fnj|A|2018-10-20|K|3.1 2.1;
  1lgd|A|2018-10-20|K|3.1 2.1;
  4ygn|A|2018-10-20|K|3.1 2.1;
  4z1n|A|2018-10-20|K|3.1 2.1;
  3fe4|A|2018-10-20|K|3.1 2.1;
  5lmd|A|2018-10-20|K|3.1 2.1;
  1ze8|A|2018-10-20|K|3.1 2.1;
  4k13|A|2018-10-20|K|3.1 2.1;
  3ryj|B|2018-10-20|K|3.1 2.1;
  1te3|X|2018-10-20|K|3.1 2.1;
  3rz1|B|2018-10-20|K|3.1 2.1;
  5sz5|A|2018-10-20|K|3.1 2.1;
  1fql|A|2018-10-20|K|3.1 2.1;
  1z97|A|2018-10-20|K|3.1 2.1;
  5cjf|A|2018-10-20|K|3.1 2.1;
  5txy|A|2018-10-20|K|3.1 2.1;
  1fsq|A|2018-10-20|K|3.1 2.1;
  4q49|A|2018-10-20|K|3.1 2.1;
  1bn4|A|2018-10-20|K|3.1 2.1;
  5bu6|B|2018-10-20|K|3.1 2.1;
  3ryv|B|2018-10-20|K|3.1 2.1;
  2foq|A|2018-10-20|K|3.1 2.1;
  5th4|A|2018-10-20|K|3.1 2.1;
  1yo0|A|2018-10-20|K|3.1 2.1;
  5flo|A|2018-10-20|K|3.1 2.1;
  4qk1|A|2018-10-20|K|3.1 2.1;
  3gz0|A|2018-10-20|K|3.1 2.1;
  5jes|B|2018-10-20|K|3.1 2.1;
  6b5a|A|2018-10-20|K|3.1 2.1;
  2nng|A|2018-10-20|K|3.1 2.1;
  3p3j|A|2018-10-20|K|3.1 2.1;
  5fdi|A|2018-10-20|K|3.1 2.1;
  3mni|A|2018-10-20|K|3.1 2.1;
  1ugd|A|2018-10-20|K|3.1 2.1;
  2x7s|A|2018-10-20|K|3.1 2.1;
  2fnn|A|2018-10-20|K|3.1 2.1;
  5jdf|A|2018-10-20|K|3.1 2.1;
  3mnj|A|2018-10-20|K|3.1 2.1;
  3hlj|A|2018-10-20|K|3.1 2.1;
  3oik|A|2018-10-20|K|3.1 2.1;
  3hkn|A|2018-10-20|K|3.1 2.1;
  3u3a|X|2018-10-20|K|3.1 2.1;
  4qk3|A|2018-10-20|K|3.1 2.1;
  4kp5|A|2018-10-20|K|3.1 2.1;
  5jep|B|2018-10-20|K|3.1 2.1;
  4rn4|A|2018-10-20|K|3.1 2.1;
  4z1e|A|2018-10-20|K|3.1 2.1;
  5eh5|A|2018-10-20|K|3.1 2.1;
  4xe1|A|2018-10-20|K|3.1 2.1;
  5ekh|A|2018-10-20|K|3.1 2.1;
  1bn3|A|2018-10-20|K|3.1 2.1;
  1zsc|A|2018-10-20|K|3.1 2.1;
  2vvb|X|2018-10-20|K|3.1 2.1;
  3mnk|A|2018-10-20|K|3.1 2.1;
  1g3z|A|2018-10-20|K|3.1 2.1;
  2nnv|A|2018-10-20|K|3.1 2.1;
  3dc9|A|2018-10-20|K|3.1 2.1;
  3daz|A|2018-10-20|K|3.1 2.1;
  2cba|A|2018-10-20|K|3.1 2.1;
  3s72|B|2018-10-20|K|3.1 2.1;
  2cbd|A|2018-10-20|K|3.1 2.1;
  3nj9|A|2018-10-20|K|3.1 2.1;
  4e3h|A|2018-10-20|K|3.1 2.1;
  4ca2|A|2018-10-20|K|3.1 2.1;
  4fpt|A|2018-10-20|K|3.1 2.1;
  3r17|B|2018-10-20|K|3.1 2.1;
  4zwz|A|2018-10-20|K|3.1 2.1;
  4q07|A|2018-10-20|K|3.1 2.1;
  5g01|A|2018-10-20|K|3.1 2.1;
  4mdl|A|2018-10-20|K|3.1 2.1;
  5tt3|A|2018-10-20|K|3.1 2.1;
  5umc|A|2018-10-20|K|3.1 2.1;
  4q09|A|2018-10-20|K|3.1 2.1;
  1g46|A|2018-10-20|K|3.1 2.1;
  5ogp|A|2018-10-20|K|3.1 2.1;
  1if6|A|2018-10-20|K|3.1 2.1;
  6eki|A|2018-10-20|K|3.1 2.1;
  3igp|A|2018-10-20|K|3.1 2.1;
  5fnh|A|2018-10-20|K|3.1 2.1;
  3w6h|A|2018-10-20|K|3.1 2.1;
  5clu|A|2018-10-20|K|3.1 2.1;
  1i9n|A|2018-10-20|K|3.1 2.1;
  3mhc|A|2018-10-20|K|3.1 2.1;
  5fls|A|2018-10-20|K|3.1 2.1;
  1cnj|A|2018-10-20|K|3.1 2.1;
  1if4|A|2018-10-20|K|3.1 2.1;
  4pyy|A|2018-10-20|K|3.1 2.1;
  4k0t|A|2018-10-20|K|3.1 2.1;
  4qsb|A|2018-10-20|K|3.1 2.1;
  4k0s|A|2018-10-20|K|3.1 2.1;
  3mna|A|2018-10-20|K|3.1 2.1;
  4n0x|B|2018-10-20|K|3.1 2.1;
  3mzc|A|2018-10-20|K|3.1 2.1;
  5msa|A|2018-10-20|K|3.1 2.1;
  5nee|A|2018-10-20|K|3.1 2.1;
  2hfw|A|2018-10-20|K|3.1 2.1;
  2f14|A|2018-10-20|K|3.1 2.1;
  3d92|A|2018-10-20|K|3.1 2.1;
  4m2r|A|2018-10-20|K|3.1 2.1;
  5ljq|A|2018-10-20|K|3.1 2.1;
  3kon|A|2018-10-20|K|3.1 2.1;
  4qk2|A|2018-10-20|K|3.1 2.1;
  4z0q|A|2018-10-20|K|3.1 2.1;
  6fe2|A|2018-10-20|K|3.1 2.1;
  4gl1|X|2018-10-20|K|3.1 2.1;
  2nwo|A|2018-10-20|K|3.1 2.1;
  1th9|A|2018-10-20|K|3.1 2.1;
  1cao|A|2018-10-20|K|3.1 2.1;
  4bf1|A|2018-10-20|K|3.1 2.1;
  3dc3|A|2018-10-20|K|3.1 2.1;
  2nno|A|2018-10-20|K|3.1 2.1;
  4qj0|A|2018-10-20|K|3.1 2.1;
  4cnv|A|2018-10-20|K|3.1 2.1;
  4r59|A|2018-10-20|K|3.1 2.1;
  4mlt|A|2018-10-20|K|3.1 2.1;
  3mnu|A|2018-10-20|K|3.1 2.1;
  3s75|B|2018-10-20|K|3.1 2.1;
  4mdg|A|2018-10-20|K|3.1 2.1;
  5eij|A|2018-10-20|K|3.1 2.1;
  3v2j|A|2018-10-20|K|3.1 2.1;
  3ml5|A|2018-10-20|K|3.1 2.1;
  1cni|A|2018-10-20|K|3.1 2.1;
  2hoc|A|2018-10-20|K|3.1 2.1;
  4yxi|A|2018-10-20|K|3.1 2.1;
  5fnl|A|2018-10-20|K|3.1 2.1;
  4xz5|A|2018-10-20|K|3.1 2.1;
  4q7p|A|2018-10-20|K|3.1 2.1;
  5flr|A|2018-10-20|K|3.1 2.1;
  5flp|A|2018-10-20|K|3.1 2.1;
  4k0z|A|2018-10-20|K|3.1 2.1;
  4e3f|A|2018-10-19|K|3.1 2.1;
  4jsz|A|2018-10-19|K|3.1 2.1;
  2eu2|A|2018-10-19|K|3.1 2.1;
  5tuo|A|2018-10-19|K|3.1 2.1;
  4n16|A|2018-10-19|K|3.1 2.1;
  5e2k|A|2018-10-19|K|3.1 2.1;
  2nns|A|2018-10-19|K|3.1 2.1;
  5jeh|B|2018-10-19|K|3.1 2.1;
  3m1q|A|2018-10-19|K|3.1 2.1;
  3myq|A|2018-10-19|K|3.1 2.1;
  1zsb|A|2018-10-19|K|3.1 2.1;
  1okn|A|2018-10-19|K|3.1 2.1;
  6d1l|A|2018-10-19|K|3.1 2.1;
  5jmz|A|2018-10-19|K|3.1 2.1;
  4hu1|A|2018-10-19|K|3.1 2.1;
  1cah|A|2018-10-19|K|3.1 2.1;
  5wlr|A|2018-10-19|K|3.1 2.1;
  1fr4|A|2018-10-19|K|3.1 2.1;
  4q90|A|2018-10-19|K|3.1 2.1;
  5amg|A|2018-10-19|K|3.1 2.1;
  4fvn|A|2018-10-19|K|3.1 2.1;
  3vbd|A|2018-10-19|K|3.1 2.1;
  4q7w|A|2018-10-19|K|3.1 2.1;
  3k7k|A|2018-10-19|K|3.1 2.1;
  3v3i|B|2018-10-19|K|3.1 2.1;
  3r16|A|2018-10-19|K|3.1 2.1;
  6g4t|A|2018-10-19|K|3.1 2.1;
  1xq0|A|2018-10-19|K|3.1 2.1;
  5a25|A|2018-10-19|K|3.1 2.1;
  4jsa|A|2018-10-19|K|3.1 2.1;
  2fnm|A|2018-10-19|K|3.1 2.1;
  4rh2|A|2018-10-19|K|3.1 2.1;
  1raz|A|2018-10-19|K|3.1 2.1;
  4q78|A|2018-10-19|K|3.1 2.1;
  4yxu|A|2018-10-19|K|3.1 2.1;
  1caz|A|2018-10-19|K|3.1 2.1;
  3qyk|A|2018-10-19|K|3.1 2.1;
  3ryx|B|2018-10-19|K|3.1 2.1;
  4q8y|A|2018-10-19|K|3.1 2.1;
  5e2r|A|2018-10-19|K|3.1 2.1;
  1t9n|A|2018-10-19|K|3.1 2.1;
  6fe1|A|2018-10-19|K|3.1 2.1;
  5ca2|A|2018-10-19|K|3.1 2.1;
  5flq|A|2018-10-19|K|3.1 2.1;
  2fmz|A|2018-10-19|K|3.1 2.1;
  4pyx|A|2018-10-19|K|3.1 2.1;
  2hnc|A|2018-10-19|K|3.1 2.1;
  5jq0|A|2018-10-19|K|3.1 2.1;
  5n1r|A|2018-10-19|K|3.1 2.1;
  5bnl|A|2018-10-19|K|3.1 2.1;
  3hku|A|2018-10-19|K|3.1 2.1;
  4kuy|A|2018-10-19|K|3.1 2.1;
  4ilx|A|2018-10-19|K|3.1 2.1;
  4zx1|A|2018-10-19|K|3.1 2.1;
  3dvd|A|2018-10-19|K|3.1 2.1;
  1h9n|A|2018-10-19|K|3.1 2.1;
  1g0f|A|2018-10-19|K|3.1 2.1;
  3v2m|A|2018-10-19|K|3.1 2.1;
  3v3h|B|2018-10-19|K|3.1 2.1;
  1v9i|C|2018-10-19|K|3.1 2.1;
  5uln|A|2018-10-19|K|3.1 2.1;
  4qy3|A|2018-10-19|K|3.1 2.1;
  5u0f|A|2018-10-19|K|3.1 2.1;
  2wd3|A|2018-10-19|K|3.1 2.1;
  5vgy|A|2018-10-19|K|3.1 2.1;
  5fdc|A|2018-10-19|K|3.1 2.1;
  3s78|B|2018-10-19|K|3.1 2.1;
  4mo8|A|2018-10-19|K|3.1 2.1;
  4e5q|A|2018-10-19|K|3.1 2.1;
  4g0c|A|2018-10-19|K|3.1 2.1;
  5u0d|A|2018-10-19|K|3.1 2.1;
  3n0n|A|2018-10-19|K|3.1 2.1;
  4mdm|A|2018-10-19|K|3.1 2.1;
  5dsi|A|2018-10-19|K|3.1 2.1;
  5jgt|B|2018-10-19|K|3.1 2.1;
  5a6h|A|2018-10-19|K|3.1 2.1;
  3m1j|A|2018-10-19|K|3.1 2.1;
  4idr|X|2018-10-19|K|3.1 2.1;
  3dd0|A|2018-10-19|K|3.1 2.1;
  1okm|A|2018-10-19|K|3.1 2.1;
  5llc|A|2018-10-19|K|3.1 2.1;
  4q8z|A|2018-10-19|K|3.1 2.1;
  3mmf|A|2018-10-19|K|3.1 2.1;
  5jn1|A|2018-10-19|K|3.1 2.1;
  4qjm|A|2018-10-19|K|3.1 2.1;
  4rux|A|2018-10-19|K|3.1 2.1;
  6cjv|A|2018-10-19|K|3.1 2.1;
  3hs4|A|2018-10-19|K|3.1 2.1;
  3sbh|A|2018-10-19|K|3.1 2.1;
  5jg5|B|2018-10-19|K|3.1 2.1;
  4mlx|A|2018-10-19|K|3.1 2.1;
  3s71|B|2018-10-19|K|3.1 2.1;
  4kni|A|2018-10-19|K|3.1 2.1;
  2q1b|A|2018-10-19|K|3.1 2.1;
  3dv7|A|2018-10-19|K|3.1 2.1;
  4cnr|A|2018-10-19|K|3.1 2.1;
  3ks3|A|2018-10-19|K|3.1 2.1;
  6bbs|A|2018-10-19|K|3.1 2.1;
  3v7x|A|2018-10-19|K|3.1 2.1;
  4ht2|A|2018-10-19|K|3.1 2.1;
  1cal|A|2018-10-19|K|3.1 2.1;
  4qtl|A|2018-10-19|K|3.1 2.1;
  4qsi|A|2018-10-19|K|3.1 2.1;
  3p5l|A|2018-10-19|K|3.1 2.1;
  3s74|B|2018-10-19|K|3.1 2.1;
  3hkq|A|2018-10-19|K|3.1 2.1;
  2fnk|A|2018-10-19|K|3.1 2.1;
  4iwz|A|2018-10-19|K|3.1 2.1;
  5ti0|A|2018-10-19|K|3.1 2.1;
  5dsj|A|2018-10-19|K|3.1 2.1;
  3sap|A|2018-10-19|K|3.1 2.1;
  4q7v|A|2018-10-19|K|3.1 2.1;
  3s9t|A|2018-10-19|K|3.1 2.1;
  4r5a|A|2018-10-19|K|3.1 2.1;
  4qjw|A|2018-10-19|K|3.1 2.1;
  5fnm|A|2018-10-19|K|3.1 2.1;
  5jn7|A|2018-10-19|K|3.1 2.1;
  4m2u|A|2018-10-19|K|3.1 2.1;
  3n2p|A|2018-10-19|K|3.1 2.1;
  5ll9|A|2018-10-19|K|3.1 2.1;
  1g48|A|2018-10-19|K|3.1 2.1;
  3m5t|A|2018-10-19|K|3.1 2.1;
  1cai|A|2018-10-19|K|3.1 2.1;
  1ray|A|2018-10-19|K|3.1 2.1;
  5fni|A|2018-10-19|K|3.1 2.1;
  4yx4|A|2018-10-19|K|3.1 2.1;
  3t5z|A|2018-10-19|K|3.1 2.1;
  4zao|A|2018-10-19|K|3.1 2.1;
  6b00|A|2018-10-19|K|3.1 2.1;
  5g0b|A|2018-10-19|K|3.1 2.1;
  1eou|A|2018-10-19|K|3.1 2.1;
  3oyq|A|2018-10-19|K|3.1 2.1;
  4lhi|A|2018-10-19|K|3.1 2.1;
  5fl6|A|2018-10-19|K|3.1 2.1;
  2pou|A|2018-10-19|K|3.1 2.1;
  5e2n|A|2018-10-19|K|3.1 2.1;
  5eh8|A|2018-10-19|K|3.1 2.1;
  1am6|A|2018-10-19|K|3.1 2.1;
  5aml|A|2018-10-19|K|3.1 2.1;
  1g53|A|2018-10-19|K|3.1 2.1;
  4js6|A|2018-10-19|K|3.1 2.1;
  4jss|A|2018-10-19|K|3.1 2.1;
  1bnt|A|2018-10-19|K|3.1 2.1;
  1bzm|A|2018-10-19|K|3.1 2.1;
  4kp8|A|2018-10-19|K|3.1 2.1;
  4hey|A|2018-10-19|K|3.1 2.1;
  2vva|X|2018-10-19|K|3.1 2.1;
  5ehv|A|2018-10-19|K|3.1 2.1;
  1mua|A|2018-10-19|K|3.1 2.1;
  4z1k|A|2018-10-19|K|3.1 2.1;
  1g45|A|2018-10-19|K|3.1 2.1;
  4q81|A|2018-10-19|K|3.1 2.1;
  4dz7|A|2018-10-19|K|3.1 2.1;
  4knn|A|2018-10-18|K|3.1 2.1;
  5e28|A|2018-10-18|K|3.1 2.1;
  5ll5|A|2018-10-18|K|3.1 2.1;
  5lla|A|2018-10-18|K|3.1 2.1;
  5zxw|A|2018-10-18|K|3.1 2.1;
  5jqt|A|2018-10-18|K|3.1 2.1;
  1cam|A|2018-10-18|K|3.1 2.1;
  6b4d|A|2018-10-18|K|3.1 2.1;
  1caj|A|2018-10-18|K|3.1 2.1;
  1rze|A|2018-10-18|K|3.1 2.1;
  1lzv|A|2018-10-18|K|3.1 2.1;
  1teu|X|2018-10-18|K|3.1 2.1;
  1kwr|A|2018-10-18|K|3.1 2.1;
  2pow|A|2018-10-18|K|3.1 2.1;
  1tg3|A|2018-10-18|K|3.1 2.1;
  3oy0|A|2018-10-18|K|3.1 2.1;
  3p3h|A|2018-10-18|K|3.1 2.1;
  3dvb|A|2018-10-18|K|3.1 2.1;
  3oim|A|2018-10-18|K|3.1 2.1;
  3rge|A|2018-10-18|K|3.1 2.1;
  3rg4|A|2018-10-18|K|3.1 2.1;
  3rg3|A|2018-10-18|K|3.1 2.1;
  4hez|A|2018-10-18|K|3.1 2.1;
  4cac|A|2018-10-18|K|3.1 2.1;
  4itp|A|2018-10-18|K|3.1 2.1;
  4l5w|A|2018-10-18|K|3.1 2.1;
  4q0l|A|2018-10-18|K|3.1 2.1;
  4rfd|A|2018-10-18|K|3.1 2.1;
  3oys|A|2018-10-18|K|3.1 2.1;
  4zx0|A|2018-10-18|K|3.1 2.1;
  5ekm|A|2018-10-18|K|3.1 2.1;
  5c8i|A|2018-10-18|K|3.1 2.1;
  5j8z|A|2018-10-18|K|3.1 2.1;
  5byi|A|2018-10-18|K|3.1 2.1;
  5jeg|B|2018-10-18|K|3.1 2.1;
  5je7|B|2018-10-18|K|3.1 2.1;
  5jg3|B|2018-10-18|K|3.1 2.1;
  5mjn|A|2018-10-18|K|3.1 2.1;
  5wg7|A|2018-10-18|K|3.1 2.1;
  6bc9|A|2018-10-18|K|3.1 2.1;
  2hl4|A|2018-10-18|K|3.1 2.1;
  3p5a|A|2018-10-18|K|3.1 2.1;
  3p58|A|2018-10-18|K|3.1 2.1;
  3mnh|A|2018-10-18|K|3.1 2.1;
  2aw1|A|2018-10-18|K|3.1 2.1;
  2hkk|A|2018-10-18|K|3.1 2.1;
  1i9l|A|2018-10-18|K|3.1 2.1;
  1i9q|A|2018-10-18|K|3.1 2.1;
  3dcc|A|2018-10-18|K|3.1 2.1;
  4cq0|A|2018-10-18|K|3.1 2.1;
  3kwa|A|2018-10-18|K|3.1 2.1;
  4xiw|A|2018-10-18|K|3.1 2.1;
  4cnx|A|2018-10-18|K|3.1 2.1;
  4zwx|A|2018-10-18|K|3.1 2.1;
  4xfw|A|2018-10-18|K|3.1 2.1;
  5ogo|A|2018-10-18|K|3.1 2.1;
  5wex|A|2018-10-18|K|3.1 2.1;
  2weo|A|2018-10-18|K|3.1 2.1;
  5fng|A|2018-10-18|K|3.1 2.1;
  1bnv|A|2018-10-18|K|3.1 2.1;
  3uyq|A|2018-10-18|K|3.1 2.1;
  5fnk|A|2018-10-18|K|3.1 2.1;
  5brw|A|2018-10-18|K|3.1 2.1;
  5llh|A|2018-10-18|K|3.1 2.1;
  1z93|A|2018-10-18|K|3.1 2.1;
  4hew|A|2018-10-18|K|3.1 2.1;
  5n0e|A|2018-10-18|K|3.1 2.1;
  4qef|A|2018-10-18|K|3.1 2.1;
  5amd|A|2018-10-18|K|3.1 2.1;
  3oku|A|2018-10-18|K|3.1 2.1;
  3tvn|X|2018-10-18|K|3.1 2.1;
  5yui|A|2018-10-18|K|3.1 2.1;
  6g98|A|2018-10-18|K|3.1 2.1;
  5dvx|A|2018-10-18|K|3.1 2.1;
  5g0c|A|2018-10-18|K|3.1 2.1;
  5ty8|A|2018-10-18|K|3.1 2.1;
  3s77|B|2018-10-18|K|3.1 2.1;
  5dsl|A|2018-10-18|K|3.1 2.1;
  5dsm|A|2018-10-18|K|3.1 2.1;
  2hfx|A|2018-10-18|K|3.1 2.1;
  3ml2|A|2018-10-18|K|3.1 2.1;
  2nn1|A|2018-10-18|K|3.1 2.1;
  4q8x|A|2018-10-18|K|3.1 2.1;
  3uyn|A|2018-10-18|K|3.1 2.1;
  5t71|A|2018-10-18|K|3.1 2.1;
  1lg6|A|2018-10-18|K|3.1 2.1;
  3dvc|A|2018-10-18|K|3.1 2.1;
  3oil|A|2018-10-18|K|3.1 2.1;
  1ugb|A|2018-10-18|K|3.1 2.1;
  3l14|A|2018-10-18|K|3.1 2.1;
  3p4v|A|2018-10-18|K|3.1 2.1;
  1xpz|A|2018-10-18|K|3.1 2.1;
  3hkt|A|2018-10-18|K|3.1 2.1;
  3lxe|A|2018-10-18|K|3.1 2.1;
  3p55|A|2018-10-18|K|3.1 2.1;
  3u45|X|2018-10-18|K|3.1 2.1;
  3u7c|A|2018-10-18|K|3.1 2.1;
  4zwy|A|2018-10-18|K|3.1 2.1;
  3t83|A|2018-10-18|K|3.1 2.1;
  4fik|A|2018-10-18|K|3.1 2.1;
  5ekj|A|2018-10-18|K|3.1 2.1;
  4jsw|A|2018-10-18|K|3.1 2.1;
  5eoi|A|2018-10-18|K|3.1 2.1;
  4zwi|A|2018-10-18|K|3.1 2.1;
  5fl4|A|2018-10-18|K|3.1 2.1;
  5wgp|A|2018-10-18|K|3.1 2.1;
  4q7s|A|2018-10-18|K|3.1 2.1;
  6g9u|A|2018-10-18|K|3.1 2.1;
  2ili|A|2018-10-18|K|3.1 2.1;
  3rld|A|2018-10-18|K|3.1 2.1;
  2x7t|A|2018-10-18|K|3.1 2.1;
  3k34|A|2018-10-18|K|3.1 2.1;
  2nmx|A|2018-10-18|K|3.1 2.1;
  2osm|A|2018-10-18|K|3.1 2.1;
  3rj7|A|2018-10-18|K|3.1 2.1;
  3k2f|A|2018-10-18|K|3.1 2.1;
  2wej|A|2018-10-18|K|3.1 2.1;
  4e3g|A|2018-10-18|K|3.1 2.1;
  4ruy|A|2018-10-17|K|3.1 2.1;
  3n3j|A|2018-10-17|K|3.1 2.1;
  5thn|A|2018-10-17|K|3.1 2.1;
  1bnm|A|2018-10-17|K|3.1 2.1;
  1uge|A|2018-10-17|K|3.1 2.1;
  1ccu|A|2018-10-17|K|3.1 2.1;
  2geh|A|2018-10-17|K|3.1 2.1;
  4ht0|A|2018-10-17|K|3.1 2.1;
  3s8x|A|2018-10-17|K|3.1 2.1;
  4pzh|A|2018-10-17|K|3.1 2.1;
  4qiy|A|2018-10-17|K|3.1 2.1;
  4qsa|A|2018-10-17|K|3.1 2.1;
  3sax|A|2018-10-17|K|3.1 2.1;
  4q6e|A|2018-10-17|K|3.1 2.1;
  3n4b|A|2018-10-17|K|3.1 2.1;
  4kuw|A|2018-10-17|K|3.1 2.1;
  1xeg|A|2018-10-17|K|3.1 2.1;
  4knm|A|2018-10-17|K|3.1 2.1;
  2nwp|A|2018-10-13|K|3.1 2.1;
  1h4n|A|2018-10-13|K|3.1 2.1;
  6got|A|2018-10-13|K|3.1 2.1;
  1g4j|A|2018-10-12|K|3.1 2.1;
  6faf|A|2018-10-12|K|3.1 2.1;
  3s73|B|2018-10-04|K|3.1 2.1;
  3pjj|A|2018-10-04|K|3.1 2.1;
  4e49|A|2018-10-03|K|3.1 2.1;
  5sz6|A|2018-10-03|K|3.1 2.1;
  4rfc|A|2018-10-03|K|3.1 2.1;
  4kuv|A|2018-10-03|K|3.1 2.1;
  4l5u|A|2018-10-03|K|3.1 2.1;
  4hba|A|2018-10-03|K|3.1 2.1;
  5n24|A|2018-10-03|K|3.1 2.1;
  4qjp|A|2018-10-03|K|3.1 2.1;
  3zp9|A|2018-10-03|K|3.1 2.1;
  4qjo|A|2018-10-03|K|3.1 2.1;
  5l9e|A|2018-10-03|K|3.1 2.1;
  4fvo|A|2018-10-03|K|3.1 2.1;
  4lu3|A|2018-10-03|K|3.1 2.1;
  4kv0|A|2018-10-03|K|3.1 2.1;
  4q99|A|2018-10-03|K|3.1 2.1;
  4q87|A|2018-10-03|K|3.1 2.1;
  4fu5|A|2018-10-03|K|3.1 2.1;
  4q83|A|2018-10-03|K|3.1 2.1;
  5yuj|A|2018-10-03|K|3.1 2.1;
  1kwq|A|2018-10-03|K|3.1 2.1;
  1jd0|A|2018-10-03|K|3.1 2.1;
  1g52|A|2018-10-03|K|3.1 2.1;
  1i90|A|2018-10-03|K|3.1 2.1;
  2cbb|A|2018-10-03|K|3.1 2.1;
  1i8z|A|2018-10-03|K|3.1 2.1;
  1v9e|A|2018-10-03|K|3.1 2.1;
  1g4o|A|2018-10-03|K|3.1 2.1;
  2cbc|A|2018-10-03|K|3.1 2.1;
  1i9o|A|2018-10-03|K|3.1 2.1;
  1g1d|A|2018-10-03|K|3.1 2.1;
  2fou|A|2018-10-03|K|3.1 2.1;
  1if7|A|2018-10-03|K|3.1 2.1;
  1if9|A|2018-10-03|K|3.1 2.1;
  1i91|A|2018-10-03|K|3.1 2.1;
  2ez7|A|2018-10-03|K|3.1 2.1;
  1i9m|A|2018-10-03|K|3.1 2.1;
  1g0e|A|2018-10-03|K|3.1 2.1;
  1i9p|A|2018-10-03|K|3.1 2.1;
  1if8|A|2018-10-03|K|3.1 2.1;
  2fmg|A|2018-10-03|K|3.1 2.1;
  1thk|A|2018-10-03|K|3.1 2.1;
  3eft|A|2018-10-01|K|3.1 2.1;
  3efi|A|2018-10-01|K|3.1 2.1;
  3v5g|A|2018-10-01|K|3.1 2.1;
  3dbu|A|2018-10-01|K|3.1 2.1;
  3czv|A|2018-10-01|K|3.1 2.1;
  2q1q|A|2018-10-01|K|3.1 2.1;
  4cnw|A|2018-10-01|K|3.1 2.1;
  3bl0|A|2018-10-01|K|3.1 2.1;
  2weg|A|2018-10-01|K|3.1 2.1;
  3sbi|A|2018-10-01|K|3.1 2.1;
  3d0n|A|2018-10-01|K|3.1 2.1;
  6h29|A|2018-09-30|K|3.1 2.1;
  1can|A|2018-09-29|K|3.1 2.1;
  5gmn|A|2018-09-26|K|3.1 2.1;
  2ax2|A|2018-09-26|K|3.1 2.1;
  5dsk|A|2018-09-26|K|3.1 2.1;
  5ljt|A|2018-09-26|K|3.1 2.1;
  2abe|A|2018-09-26|K|3.1 2.1;
  1f2w|A|2018-09-26|K|3.1 2.1;
  5l70|A|2018-09-14|K|3.1 2.1;
  1cng|A|2018-09-12|K|3.1 2.1;
  1j85|A|2018-08-14|K|3.1 2.1;
  6emv|A|2018-07-25|K|3.1 2.1;
  5nfj|A|2018-07-23|K|3.1 2.1;
  6emu|A|2018-07-22|K|3.1 2.1;
  6ems|A|2018-07-22|K|3.1 2.1;
  5l0z|A|2018-06-12|K|3.1 2.1;
  5lle|A|2018-06-12|K|3.1 2.1;
  5llp|A|2018-06-12|K|3.1 2.1;
  5m4s|A|2018-06-12|K|3.1 2.1;
  5msb|A|2018-06-12|K|3.1 2.1;
  5nxo|A|2018-06-12|K|3.1 2.1;
  5nxp|A|2018-06-12|K|3.1 2.1;
  5ny1|A|2018-06-12|K|3.1 2.1;
  5ny6|A|2018-06-12|K|3.1 2.1;
  5oql|e|2018-06-12|K|3.1 2.1;
  5sz4|A|2018-06-12|K|3.1 2.1;
  1avn|A|2018-06-12|K|3.1 2.1;
  1k3r|A|2018-06-12|K|3.1 2.1;
  1cra|A|2018-06-11|K|3.1 2.1;
  1f48|A|2018-06-11|K|3.1 2.1;
  1fqn|A|2018-06-11|K|3.1 2.1;
  1fug|A|2018-06-11|K|3.1 2.1;
  1gz0|A|2018-06-11|K|3.1 2.1;
  1hva|A|2018-06-11|K|3.1 2.1;
  1jv0|A|2018-06-11|K|3.1 2.1;
  1mxi|A|2018-06-11|K|3.1 2.1;
  1ns5|A|2018-06-11|K|3.1 2.1;
  1nxz|A|2018-06-11|K|3.1 2.1;
  1o6d|A|2018-06-11|K|3.1 2.1;
  1rza|A|2018-06-11|K|3.1 2.1;
  1rzc|A|2018-06-11|K|3.1 2.1;
  1rzd|A|2018-06-11|K|3.1 2.1;
  1tbt|X|2018-06-11|K|3.1 2.1;
  2cbe|A|2018-06-11|K|3.1 2.1;
  2cx8|A|2018-06-11|K|3.1 2.1;
  2d1g|A|2018-06-11|K|3.1 2.1;
  2egv|A|2018-06-11|K|3.1 2.1;
  2egw|A|2018-06-11|K|3.1 2.1;
  2fg6|C|2018-06-11|K|3.1 2.1;
  2fos|A|2018-06-11|K|3.1 2.1;
  2g7m|C|2018-06-11|K|3.1 2.1;
  2ha8|A|2018-06-11|K|3.1 2.1;
  2i6d|A|2018-06-11|K|3.1 2.1;
  2nxt|A|2018-06-11|K|3.1 2.1;
  2qmm|A|2018-06-11|K|3.1 2.1;
  2qwv|A|2018-06-11|K|3.1 2.1;
  2v3j|A|2018-06-11|K|3.1 2.1;
  2v3k|A|2018-06-11|K|3.1 2.1;
  2w2j|A|2018-06-11|K|3.1 2.1;
  2wd2|A|2018-06-11|K|3.1 2.1;
  2x7u|A|2018-06-11|K|3.1 2.1;
  2yfk|A|2018-06-11|K|3.1 2.1;
  2z0y|A|2018-06-11|K|3.1 2.1;
  2znc|A|2018-06-11|K|3.1 2.1;
  3b1b|A|2018-06-11|K|3.1 2.1;
  3bbd|A|2018-06-11|K|3.1 2.1;
  3bbe|A|2018-06-11|K|3.1 2.1;
  3bet|A|2018-06-11|K|3.1 2.1;
  3c7p|A|2018-06-11|K|3.1 2.1;
  3d93|A|2018-06-11|K|3.1 2.1;
  3dcm|X|2018-06-11|K|3.1 2.1;
  3e5y|A|2018-06-11|K|3.1 2.1;
  3ed7|A|2018-06-11|K|3.1 2.1;
  3gyq|A|2018-06-11|K|3.1 2.1;
  3iai|A|2018-06-11|K|3.1 2.1;
  3ibi|A|2018-06-11|K|3.1 2.1;
  3ibn|A|2018-06-11|K|3.1 2.1;
  3ibu|A|2018-06-11|K|3.1 2.1;
  3ic6|A|2018-06-11|K|3.1 2.1;
  3ilk|A|2018-06-11|K|3.1 2.1;
  3jyw|E|2018-06-11|K|3.1 2.1;
  3knu|A|2018-06-11|K|3.1 2.1;
  3kty|A|2018-06-11|K|3.1 2.1;
  3kw2|A|2018-06-11|K|3.1 2.1;
  3ky7|A|2018-06-11|K|3.1 2.1;
  3kzc|A|2018-06-11|K|3.1 2.1;
  3kzk|A|2018-06-11|K|3.1 2.1;
  3kzm|A|2018-06-11|K|3.1 2.1;
  3kzn|A|2018-06-11|K|3.1 2.1;
  3kzo|A|2018-06-11|K|3.1 2.1;
  3l02|A|2018-06-11|K|3.1 2.1;
  3l04|A|2018-06-11|K|3.1 2.1;
  3l05|A|2018-06-11|K|3.1 2.1;
  3l06|A|2018-06-11|K|3.1 2.1;
  3l8u|A|2018-06-11|K|3.1 2.1;
  3m40|A|2018-06-11|K|3.1 2.1;
  3m4j|A|2018-06-11|K|3.1 2.1;
  3m4n|A|2018-06-11|K|3.1 2.1;
  3m5c|A|2018-06-11|K|3.1 2.1;
  3m5d|A|2018-06-11|K|3.1 2.1;
  3m5e|A|2018-06-11|K|3.1 2.1;
  3m96|A|2018-06-11|K|3.1 2.1;
  3m98|A|2018-06-11|K|3.1 2.1;
  3mhi|A|2018-06-11|K|3.1 2.1;
  3mhm|A|2018-06-11|K|3.1 2.1;
  3n4k|A|2018-06-11|K|3.1 2.1;
  3nk7|A|2018-06-11|K|3.1 2.1;
  3o7b|A|2018-06-11|K|3.1 2.1;
  3oij|A|2018-06-11|K|3.1 2.1;
  3oin|A|2018-06-11|K|3.1 2.1;
  3onp|A|2018-06-11|K|3.1 2.1;
  3q98|A|2018-06-11|K|3.1 2.1;
  3ryz|A|2018-06-11|K|3.1 2.1;
  3rz5|A|2018-06-11|K|3.1 2.1;
  3rz7|A|2018-06-11|K|3.1 2.1;
  3s76|A|2018-06-11|K|3.1 2.1;
  3s97|A|2018-06-11|K|3.1 2.1;
  3sig|A|2018-06-11|K|3.1 2.1;
  3sij|A|2018-06-11|K|3.1 2.1;
  3v5s|A|2018-06-11|K|3.1 2.1;
  3v5u|A|2018-06-11|K|3.1 2.1;
  4cnd|A|2018-06-11|K|3.1 2.1;
  4cnd|B|2018-06-11|K|3.1 2.1;
  4cne|A|2018-06-11|K|3.1 2.1;
  4cne|B|2018-06-11|K|3.1 2.1;
  4cnf|A|2018-06-11|K|3.1 2.1;
  4cnf|B|2018-06-11|K|3.1 2.1;
  4cng|A|2018-06-11|K|3.1 2.1;
  4cng|B|2018-06-11|K|3.1 2.1;
  4e8b|A|2018-06-11|K|3.1 2.1;
  4fak|A|2018-06-11|K|3.1 2.1;
  4fmw|A|2018-06-11|K|3.1 2.1;
  4h6v|A|2018-06-11|K|3.1 2.1;
  4hpv|A|2018-06-11|K|3.1 2.1;
  4ig6|A|2018-06-11|K|3.1 2.1;
  4jak|A|2018-06-11|K|3.1 2.1;
  4jal|A|2018-06-11|K|3.1 2.1;
  4jwf|A|2018-06-11|K|3.1 2.1;
  4jwg|A|2018-06-11|K|3.1 2.1;
  4jwh|A|2018-06-11|K|3.1 2.1;
  4jwj|A|2018-06-11|K|3.1 2.1;
  4k0b|A|2018-06-11|K|3.1 2.1;
  4k1c|A|2018-06-11|K|3.1 2.1;
  4kdz|A|2018-06-11|K|3.1 2.1;
  4kgn|A|2018-06-11|K|3.1 2.1;
  4kjr|A|2018-06-11|K|3.1 2.1;
  4kpp|A|2018-06-11|K|3.1 2.1;
  4ktv|A|2018-06-11|K|3.1 2.1;
  4l69|A|2018-06-11|K|3.1 2.1;
  4l7i|A|2018-06-11|K|3.1 2.1;
  4o6d|A|2018-06-11|K|3.1 2.1;
  4o6d|B|2018-06-11|K|3.1 2.1;
  4pzk|A|2018-06-11|K|3.1 2.1;
  4riv|A|2018-06-11|K|3.1 2.1;
  4twl|A|2018-06-11|K|3.1 2.1;
  4twm|A|2018-06-11|K|3.1 2.1;
  4ws9|A|2018-06-11|K|3.1 2.1;
  4x3m|A|2018-06-11|K|3.1 2.1;
  4ypx|A|2018-06-11|K|3.1 2.1;
  4yqd|A|2018-06-11|K|3.1 2.1;
  4yr1|A|2018-06-11|K|3.1 2.1;
  4yvh|A|2018-06-11|K|3.1 2.1;
  4yvi|A|2018-06-11|K|3.1 2.1;
  4yvj|A|2018-06-11|K|3.1 2.1;
  4yvk|A|2018-06-11|K|3.1 2.1;
  5a7t|A|2018-06-11|K|3.1 2.1;
  5a7y|A|2018-06-11|K|3.1 2.1;
  5a7z|A|2018-06-11|K|3.1 2.1;
  5apg|A|2018-06-11|K|3.1 2.1;
  5c74|A|2018-06-11|K|3.1 2.1;
  5cjl|A|2018-06-11|K|3.1 2.1;
  5co4|A|2018-06-11|K|3.1 2.1;
  5doh|A|2018-06-11|K|3.1 2.1;
  5drs|A|2018-06-11|K|3.1 2.1;
  5dso|A|2018-06-11|K|3.1 2.1;
  5dsq|A|2018-06-11|K|3.1 2.1;
  5dsr|A|2018-06-11|K|3.1 2.1;
  5fai|A|2018-06-11|K|3.1 2.1;
  5gm8|A|2018-06-11|K|3.1 2.1;
  5gmb|A|2018-06-11|K|3.1 2.1;
  5gmc|A|2018-06-11|K|3.1 2.1;
  5gra|A|2018-06-11|K|3.1 2.1;
  5h5e|A|2018-06-11|K|3.1 2.1;
  5h5f|A|2018-06-11|K|3.1 2.1;
  5hwy|A|2018-06-11|K|3.1 2.1;
  5jn3|A|2018-06-11|K|3.1 2.1;
  5jpq|e|2018-06-11|K|3.1 2.1;
  5kzk|A|2018-06-11|K|3.1 2.1;
  5nxg|A|2018-06-11|K|3.1 2.1;
  5ny3|A|2018-06-11|K|3.1 2.1;
  5sz0|A|2018-06-11|K|3.1 2.1;
  5sz1|A|2018-06-11|K|3.1 2.1;
  5t75|A|2018-06-11|K|3.1 2.1;
  5tt8|A|2018-06-11|K|3.1 2.1;
  5tv3|A|2018-06-11|K|3.1 2.1;
  5twk|A|2018-06-11|K|3.1 2.1;
  5wyr|A|2018-06-11|K|3.1 2.1;
  5y2r|A|2018-06-11|K|3.1 2.1;
  1to0|A|2018-06-11|K|3.1 2.1;
  1uaj|A|2018-06-11|K|3.1 2.1;
  1ual|A|2018-06-11|K|3.1 2.1;
  1uam|A|2018-06-11|K|3.1 2.1;
  1ugf|A|2018-06-11|K|3.1 2.1;
  1v2x|A|2018-06-11|K|3.1 2.1;
  1v6z|A|2018-06-11|K|3.1 2.1;
  1vh0|A|2018-06-11|K|3.1 2.1;
  1vhk|A|2018-06-11|K|3.1 2.1;
  1vhy|A|2018-06-11|K|3.1 2.1;
  1x7o|A|2018-06-11|K|3.1 2.1;
  1x7p|A|2018-06-11|K|3.1 2.1;
  1xev|A|2018-06-11|K|3.1 2.1;
  1y7w|A|2018-06-11|K|3.1 2.1;
  1yh1|A|2018-06-11|K|3.1 2.1;
  1zsa|A|2018-06-11|K|3.1 2.1;
  1by7|A|2018-06-10|K|3.1 2.1;
Knotoid types pdb Title
K 3.1, 2.1 4cnxA Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion co2 capture
K 3.1, 2.1 4zwxA Engineered carbonic anhydrase ix mimic in complex with glucosyl sulfamate inhibitor
K 3.1, 2.1 4xfwA Crystal structure of the monoclinic form of alpha-carbonic anhydrase from the human pathogen helicobacter pylori
K 3.1, 2.1 5ogoA Crystal structure of chimeric carbonic anhydrase i with 3-(benzylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide
K 3.1, 2.1 5wexA Discovery of new selenoureido analogs of 4-(4-fluorophenylureido) benzenesulfonamides as carbonic anhydrase inhibitors
K 3.1, 2.1 2weoA Thermodynamic optimisation of carbonic anhydrase fragment inhibitors
K 3.1, 2.1 5fngA Native state mass spectrometry, surface plasmon resonance and x-ray crystallography correlate strongly as a fragment screening combination
K 3.1, 2.1 1bnvA Carbonic anhydrase ii inhibitor
K 3.1, 2.1 3uyqA Hca 3
K 3.1, 2.1 5fnkA Native state mass spectrometry, surface plasmon resonance and x-ray crystallography correlate strongly as a fragment screening combination
K 3.1, 2.1 5brwA Catalytic improvement of an artificial metalloenzyme by computational design
K 3.1, 2.1 5llhA Crystal structure of human carbonic anhydrase isozyme ii with 4-(1,3-benzothiazol-2-ylthio)-2,3,5,6-tetrafluorobenzenesulfonamide
K 3.1, 2.1 1z93A Human carbonic anhydrase iii:structural and kinetic study of catalysis and proton transfer.
K 3.1, 2.1 4hewA Activity enhancers of h64a variant of human carbonic anhydrase ii possess multiple binding sites within and around the enzyme structure
K 3.1, 2.1 5n0eA Crystal structure of human carbonic anhydrase ii in complex with (s)-4-(6,7-dihydroxy-1-phenyl-3,4-tetrahydroisoquinoline-1h-2-carbonyl)benzenesulfonamide.
K 3.1, 2.1 4qefA Human carbonic anhydrase ii v207i - cyanate inhibitor complex
K 3.1, 2.1 5amdA Three dimensional structure of human carbonic anhydrase ii in complex with 2-((2-phenylethyl)sulfamoyl)-4-sulfamoylbenzoic acid
K 3.1, 2.1 3okuA Human carbonic anhydrase ii in complex with 2-ethylestrone-3-o-sulfamate
K 3.1, 2.1 3tvnX Human carbonic anhydrase ii proton transfer mutant
K 3.1, 2.1 5yuiA Co2 release in human carbonic anhydrase ii crystals: reveal histidine 64 and solvent dynamics
K 3.1, 2.1 6g98A Three dimensional structure of human carbonic anhydrase ix in complex with sulfonamide
K 3.1, 2.1 5dvxA Crystal structure of the catalytic-domain of human carbonic anhydrase ix at 1.6 angstrom resolution
K 3.1, 2.1 5g0cA An unusual natural product primary sulfonamide: synthesis, carbonic anhydrase inhibition and protein x-ray structure of psammaplin c
K 3.1, 2.1 5ty8A Identification of a new zinc binding chemotype by fragment screening
K 3.1, 2.1 3s77B The origin of the hydrophobic effect in the molecular recognition of arylsulfonamides by carbonic anhydrase
K 3.1, 2.1 5dslA Structure of co2 released holo-form of human carbonic anhydrase ii with 10 min warming
K 3.1, 2.1 5dsmA Structure of co2 released holo-form of human carbonic anhydrase ii with 25 min warming
K 3.1, 2.1 2hfxA Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase iii
K 3.1, 2.1 3ml2A Human carbonic anhydsase ii in complex with an aryl sulfonamide inhibitor
K 3.1, 2.1 2nn1A Structure of inhibitor binding to carbonic anhydrase i
K 3.1, 2.1 4q8xA Crystal structure of 1-hydroxy-5-(trifluoromethyl)pyridine-2(1h)-thione bound to human carbonic anhydrase ii
K 3.1, 2.1 3uynA Hca 3
K 3.1, 2.1 5t71A Human carboanhydrase f131c_c206s double mutant in complex with sa-2
K 3.1, 2.1 1lg6A Crystal structure analysis of hca ii mutant t199p in complex with thiocyanate
K 3.1, 2.1 3dvcA X-ray crystal structure of mutant n62t of human carbonic anhydrase ii
K 3.1, 2.1 3oilA Human carbonic anhydrase ii mutant a65s, n67q (ca ix mimic) bound by 2-ethylestradiol 3-o-sulfamate
K 3.1, 2.1 1ugbA Human carbonic anhydrase ii[hcaii] (e.c.4.2.1.1) mutant with ala 65 replaced by gly (a65g)
K 3.1, 2.1 3l14A Human carbonic anhydrase ii complexed with althiazide
K 3.1, 2.1 3p4vA Human carbonic anhydrase ii in complex with (+)-xylariamide a
K 3.1, 2.1 1xpzA Structure of human carbonic anhydrase ii with 4-[4-o-sulfamoylbenzyl)(4-cyanophenyl)amino]-4h-[1,2,4]-triazole
K 3.1, 2.1 3hktA Human carbonic anhydrase ii in complex with alpha-d-glucopyranosyl-(1->4)-1-thio-beta-d-glucopyranosylsulfonamide
K 3.1, 2.1 3lxeA Human carbonic anhydrase i in complex with topiramate
K 3.1, 2.1 3p55A Human carbonic anhydrase ii in complex with p-(4-ferrocenyl-1h-1,2,3-triazol-1-yl)benzenesulfonamide
K 3.1, 2.1 3u45X Human carbonic anhydrase ii v143a
K 3.1, 2.1 3u7cA Crystal structure of the v143i mutant of human carbonic anhydrase ii
K 3.1, 2.1 4zwyA Human carbonic anhydrase ii in complex with a glucosyl sulfamate inhibitor
K 3.1, 2.1 3t83A Human carbonic anhydrase ii in complex with acetylated carbohydrate sulfamates
K 3.1, 2.1 4fikA Human carbonic anhydrase ii h64a complexed with thioxolone hydrolysis products
K 3.1, 2.1 5ekjA Human carbonic anhydrase ii complexed with a two-faced guest
K 3.1, 2.1 4jswA Human carbonic anhydrase ii h94c
K 3.1, 2.1 5eoiA Crystal structure of copper bound human carbonic anhydrase ii
K 3.1, 2.1
2
4zwiA Surface lysine acetylated human carbonic anhydrase ii in complex with a sulfamate-based inhibitor
K 3.1, 2.1 5fl4A Three dimensional structure of human carbonic anhydrase ix in complex with 5-(1-naphthalen-1-yl-1,2,3-triazol-4-yl)thiophene-2-sulfonamide
K 3.1, 2.1 5wgpA Human carbonic anhydrase ix-mimic complexed with acek
K 3.1, 2.1 4q7sA Crystal structure of 1-hydroxy-4-methylpyridine-2(1h)-thione bound to human carbonic anhydrase ii
K 3.1, 2.1 6g9uA Three dimensional structure of human carbonic anhydrase ix in complex with sulfonamide
K 3.1, 2.1 2iliA Refine atomic structure of human carbonic anhydrase ii
K 3.1, 2.1 3rldA Crystal structure of the y7i mutant of human carbonic anhydrase ii
K 3.1, 2.1 2x7tA Structures of human carbonic anhydrase ii inhibitor complexes reveal a second binding site for steroidal and non-steroidal inhibitors.
K 3.1, 2.1 3k34A Human carbonic anhydrase ii with a sulfonamide inhibitor
K 3.1, 2.1 2nmxA Structure of inhibitor binding to carbonic anhydrase i
K 3.1, 2.1 2osmA Inhibition of carbonic anhydrase ii by thioxolone: a mechanistic and structural study
K 3.1, 2.1 3rj7A Human carbonic anhydrase ii complexed with its inhibitor rhenium(i)triscarbonyl-cyclopentadienyl-carboxy-4-aminomethylbenzene-sulfonamide
K 3.1, 2.1 3k2fA Nitric oxide-donating carbonic anhydrase inhibitors for the treatment of open-angle glaucoma
K 3.1, 2.1 2wejA Thermodynamic optimisation of carbonic anhydrase fragment inhibitors
K 3.1, 2.1 4e3gA Nucleophile recognition as an alternative inhibition mode for benzoic acid based carbonic anhydrase inhibitors
K 3.1, 2.1 4ruyA Crystal structure of human carbonic anhydrase ii in complex with 4-propoxybenzenesulfonamide
K 3.1, 2.1 3n3jA Crystal structure of human carbonic anhydrase ii in complex with a benzenesulfonamide inhibitor
K 3.1, 2.1 5thnA Crystal structure of 2-hydroxycyclohepta-2,4,6-triene-1-thione bound to human carbonic anhydrase 2
K 3.1, 2.1 1bnmA Carbonic anhydrase ii inhibitor
K 3.1, 2.1 1ugeA Human carbonic anhydrase ii [hcaii] (e.c.4.2.1.1) mutant with ala 65 replaced by leu (a65l)
K 3.1, 2.1 1ccuA Structure-assisted redesign of a protein-zinc binding site with femtomolar affinity
K 3.1, 2.1 2gehA N-hydroxyurea, a versatile zinc binding function in the design of metalloenzyme inhibitors
K 3.1, 2.1 4ht0A Crystal structure of human carbonic anhydrase isozyme ii with the inhibitor.
K 3.1, 2.1 3s8xA Crystal structure of human carbonic anhydrase isozyme ii with 4-{[(4-methyl-6-oxo-1,6-dihydro-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide
K 3.1, 2.1 4pzhA Crystal structure of human carbonic anhydrase isozyme ii with 2,3,5,6-tetrafluoro-4[(2-hydroxyethyl)sulfonyl]benzenesulfonamide
K 3.1, 2.1 4qiyA Crystal structure of human carbonic anhydrase isozyme ii with inhibitor
K 3.1, 2.1 4qsaA Crystal structure of human carbonic anhydrase isozyme ii with 2-chloro-4-{[(4-methyl-6-oxo-1,6-dihydropyrimidin-2-yl)thio]acetyl}benzenesulfonamide
K 3.1, 2.1 3saxA Crystal structure of human carbonic anhydrase isozyme ii with 2-chloro-5-{[(5-ethyl-2-pyrimidinyl)sulfanyl]acetyl}benzenesulfonamide
K 3.1, 2.1 4q6eA Crystal structure of human carbonic anhydrase isozyme ii with 4-{[3-(3,5-dimethyl-1h-pyrazol-1-yl)-3-oxopropyl]amino}benzene-1-sulfonamide
K 3.1, 2.1 3n4bA Crystal structure of human carbonic anhydrase ii in complex with a benzenesulfonamide inhibitor
K 3.1, 2.1 4kuwA Crystal structure of human carbonic anhydrase ii in complex with the 5-(3-(4-fluorophenylsulfonyl)ureido)pyridine-2-sulfonamide inhibitor
K 3.1, 2.1 1xegA Crystal structure of human carbonic anhydrase ii complexed with an acetate ion
K 3.1, 2.1 4knmA Crystal structure of human carbonic anhydrase isozyme xiii with 2-chloro-4-{[(4,6-dimethylpyrimidin-2-yl)sulfanyl]acetyl}benzenesulfonamide
K 3.1, 2.1 2nwpA Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase ii
K 3.1, 2.1 1h4nA H94n carbonic anhydrase ii complexed with tris
K 3.1, 2.1 6gotA Crystal structure of human carbonic anhydrase ii in complex with the inhibitor 4-(phenethylthio)benzenesulfonamide
K 3.1, 2.1 1g4jA Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,3,4,5,6-pentafluorophenyl)methyl]-benzamide
K 3.1, 2.1 6fafA Crystal structure of human carbonic anhydrase i in complex with the 3-(2,5-dimethylphenyl)-1-(2-hydroxy-5-sulfamoylphenyl)urea inhibitor
K 3.1, 2.1 3s73B The origin of the hydrophobic effect in the molecular recognition of arylsulfonamides by carbonic anhydrase
K 3.1, 2.1 3pjjA Synthetic dimer of human carbonic anhydrase ii
K 3.1, 2.1 4e49A Nucleophile recognition as an alternative inhibition mode for benzoic acid based carbonic anhydrase inhibitors
K 3.1, 2.1 5sz6A Carbonic anhydrase ix-mimic in complex with 4-(3-formylphenyl)-benzenesulfonamide
K 3.1, 2.1 4rfcA Human carbonic anhydrase ii in complex with tert-butyl 4-(4-sulfamoylphenoxy)butylcarbamate
K 3.1, 2.1 4kuvA Crystal structure of human carbonic anhydrase ii in complex with the 5-(3-(4-chlorophenylsulfonyl)ureido)pyridine-2-sulfonamide inhibitor
K 3.1, 2.1 4l5uA The structural implications of the secondary co2 binding pocket in human carbonic anhydrase ii
K 3.1, 2.1 4hbaA Structural and catalytic characterization of a thermal and acid stable variant of human carbonic anhydrase ii containing an engineered disulfide bond
K 3.1, 2.1 5n24A Crystal structure of human carbonic anhydrase ii in complex with the inhibitor b4'-cyano-biphenyl-4-sulfonic acid amide
K 3.1, 2.1 4qjpA Crystal structure of human carbonic anhydrase isozyme xiii with inhibitor
K 3.1, 2.1 3zp9A Human carbonic anhydrase ii as a scaffold for an artificial transfer hydrogenase
K 3.1, 2.1 4qjoA Crystal structure of catalytic domain of human carbonic anhydrase isozyme xii with inhibitor
K 3.1, 2.1 5l9eA Crystal structure of human carbonic anhydrase ii in complex with a quinoline oligoamide foldamer
K 3.1, 2.1 4fvoA Carbonic anhydrase ii in complex with n-[(2e)-3,4-dihydroquinazolin-2(1h)-ylidene]sulfuric diamide
K 3.1, 2.1 4lu3A The crystal structure of the human carbonic anhydrase xiv
K 3.1, 2.1 4kv0A Crystal structure of human carbonic anhydrase ii in complex with the 5-(3-tosylureido)pyridine-2-sulfonamide inhibitor
K 3.1, 2.1 4q99A Crystal structure of 2-mercapto-4-methylphenol bound to human carbonic anhydrase ii
K 3.1, 2.1 4q87A Crystal structure of 1-hydroxy-4-(trifluoromethyl)pyridine-2(1h)-thione bound to human carbonic anhydrase ii
K 3.1, 2.1 4fu5A Carbonic anhydrase ii in complex with n-[(2z)-1,3-oxazolidin-2-ylidene]sulfuric diamide
K 3.1, 2.1 4q83A Crystal structure of 1-hydroxy-3-(trifluoromethyl)pyridine-2(1h)-thione bound to human carbonic anhydrase ii
K 3.1, 2.1 5yujA Co2 release in human carbonic anhydrase ii crystals: reveal histidine 64 and solvent dynamics
K 3.1, 2.1 1kwqA Human carbonic anhydrase ii complexed with inhibitor 2000-07
K 3.1, 2.1 1jd0A Crystal structure of the extracellular domain of human carbonic anhydrase xii complexed with acetazolamide
K 3.1, 2.1 1g52A Carbonic anhydrase ii complexed with 4-(aminosulfonyl)-n-[(2,3-difluorophenyl)methyl]-benzamide
K 3.1, 2.1 1i90A Carbonic anhydrase ii complexed with al-8520 2h-thieno[3,2-e]-1,2-thiazine-6-sulfonamide, 4-amino-3,4-dihydro-2-(3-methoxypropyl)-, 1,1-dioxide, (r)
K 3.1, 2.1 2cbbA Structure of native and apo carbonic anhydrase ii and some of its anion-ligand complexes
K 3.1, 2.1 1i8zA Carbonic anhydrase ii complexed with al-6629 2h-thieno[3,2-e]-1,2-thiazine-6-sulfonamide, 2-(3-methoxyphenyl)-3-(4-morpholinyl)-, 1,1-dioxide
K 3.1, 2.1 1v9eA Crystal structure analysis of bovine carbonic anhydrase ii
K 3.1, 2.1 1g4oA Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-phenylmethylbenzamide
K 3.1, 2.1 2cbcA Structure of native and apo carbonic anhydrase ii and some of its anion-ligand complexes
K 3.1, 2.1 1i9oA Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,3,4-trifluorophenyl)methyl]-benzamide
K 3.1, 2.1 1g1dA Carbonic anhydrase ii complexed with 4-(aminosulfonyl)-n-[(2-fluorophenyl)methyl]-benzamide
K 3.1, 2.1
2
2fouA Human carbonic anhydrase ii complexed with two-prong inhibitors
K 3.1, 2.1 1if7A Carbonic anhydrase ii complexed with (r)-n-(3-indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide
K 3.1, 2.1 1if9A Carbonic anhydrase ii complexed with n-[2-(1h-indol-5-yl)-butyl]-4-sulfamoyl-benzamide
K 3.1, 2.1 1i91A Carbonic anhydrase ii complexed with al-6619 2h-thieno[3,2-e]-1,2-thiazine-6-sulfonamide, 2-(3-hydroxyphenyl)-3-(4-morpholinyl)-, 1,1-dioxide
K 3.1, 2.1 2ez7A Carbonic anhydrase activators. activation of isozymes i, ii, iv, va, vii and xiv with l- and d-histidine and crystallographic analysis of their adducts with isoform ii: engineering proton transfer processes within the active site of an enzyme
K 3.1, 2.1 1i9mA Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,4-difluorophenyl)methyl]-benzamide
K 3.1, 2.1 1g0eA Site-specific mutant (his64 replaced with ala) of human carbonic anhydrase ii complexed with 4-methylimidazole
K 3.1, 2.1 1i9pA Carbonic anhydrase ii (f131v) complexed with 4-(aminosulfonyl)-n-[(2,4,6-trifluorophenyl)methyl]-benzamide
K 3.1, 2.1 1if8A Carbonic anhydrase ii complexed with (s)-n-(3-indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide
K 3.1, 2.1 2fmgA Carbonic anhydrase activators. activation of isoforms i, ii, iv, va, vii and xiv with l- and d- phenylalanine and crystallographic analysis of their adducts with isozyme ii: sterospecific recognition within the active site of an enzyme and its consequences for the drug design, structure with l-phenylalanine
K 3.1, 2.1 1thkA Effect of shuttle location and ph environment on h+ transfer in human carbonic anhydrase ii
K 3.1, 2.1
2
3eftA Crystal structure of the complex between carbonic anhydrase ii and a spin-labeled sulfonamide incorporating tempo moiety
K 3.1, 2.1 3efiA Carbonic anhydrase activators: kinetic and x-ray crystallographic study for the interaction of d- and l-tryptophan with the mammalian isoforms i-xiv
K 3.1, 2.1 3v5gA Crystal structure of human carbonic anhydrase ii in complex with the 4-sulfamido-benzenesulfonamide inhibitor
K 3.1, 2.1 3dbuA Use of carbonic anhydrase ii, ix active-site mimic, for the purpose of screening inhibitors for possible anti-cancer properties
K 3.1, 2.1 3czvA Crystal structure of the human carbonic anhydrase xiii in complex with acetazolamide
K 3.1, 2.1 2q1qA Carbonic anhydrase inhibitors. interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: kinetic and x-ray crystallographic studies
K 3.1, 2.1 4cnwA Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion co2 capture
K 3.1, 2.1 3bl0A Carbonic anhydrase inhibitors. interaction of 2-n,n-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide with twelve mammalian isoforms: kinetic and x-ray crystallographic studies
K 3.1, 2.1 2wegA Thermodynamic optimisation of carbonic anhydrase fragment inhibitors
K 3.1, 2.1 3sbiA Crystal structure of human carbonic anhydrase isozyme ii with 4-[(2-pyrimidinylsulfanyl)acetyl]benzenesulfonamide
K 3.1, 2.1 3d0nA Crystal structure of human carbonic anhydrase xiii
K 3.1, 2.1 6h29A Human carbonic anhydrase ii in complex with benzyl carbamate
K 3.1, 2.1 1canA Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions
K 3.1, 2.1 5gmnA Crystal structure of human carbonic anhydrase ii in complex with polmacoxib
K 3.1, 2.1 2ax2A Production and x-ray crystallographic analysis of fully deuterated human carbonic anhydrase ii
K 3.1, 2.1 5dskA Structure of co2 released holo-form of human carbonic anhydrase ii with 3 min warming
K 3.1, 2.1 5ljtA Crystal structure of human carbonic anhydrase ii in complex with the 4-((1-phenyl-1h-1,2,3-triazol-4-yl)methoxy)benzenesulfonamide inhibitor
K 3.1, 2.1 2abeA Carbonic anhydrase activators: x-ray crystal structure of the adduct of human isozyme ii with l-histidine as a platform for the design of stronger activators
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KnotProt | Interdisciplinary Laboratory of Biological Systems Modelling