<?xml version="1.0" encoding="UTF-8" ?><xml>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>5CHA</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>34.4415</bfactor-bindingsite>
    <bfactor-ligand>40.749</bfactor-ligand>
    <backbone-hbond>-1.41</backbone-hbond>
    <cathid>5chaC00</cathid>
    <dssp-bindingsite>B=6 C=41 E=6 S=35 T=12</dssp-bindingsite>
    <dssp-ligand>C=78 S=22</dssp-ligand>
    <description>THE REFINEMENT AND THE STRUCTURE OF THE DIMER OF ALPHA-*CHYMOTRYPSIN AT 1.67-*ANGSTROMS RESOLUTION</description>
    <foldx-energy>-6.99</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>9</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>6</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.03</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1AFQ</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>28.2745</bfactor-bindingsite>
    <bfactor-ligand>44.5576</bfactor-ligand>
    <backbone-hbond>-3.34</backbone-hbond>
    <cathid>1afqB00</cathid>
    <dssp-bindingsite>B=5 C=40 E=15 S=20 T=20</dssp-bindingsite>
    <dssp-ligand>C=80 S=20</dssp-ligand>
    <description>CRYSTAL STRUCTURE OF BOVINE GAMMA-CHYMOTRYPSIN COMPLEXED WITH A SYNTHETIC INHIBITOR</description>
    <foldx-energy>-14.37</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>10</ligand-size>
    <receptor>BC</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>15</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.76</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1GHA</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>8.35146</bfactor-bindingsite>
    <bfactor-ligand>15.7577</bfactor-ligand>
    <backbone-hbond>-3.44</backbone-hbond>
    <cathid>1ghaG00</cathid>
    <dssp-bindingsite>B=4 C=43 E=22 S=22 T=9</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>A SECOND ACTIVE SITE IN CHYMOTRYPSIN? THE X-RAY CRYSTAL STRUCTURE OF N-ACETYL-D-TRYPTOPHAN BOUND TO GAMMA-CHYMOTRYPSIN</description>
    <foldx-energy>-14.56</foldx-energy>
    <ligand>E</ligand>
    <ligand-size>11</ligand-size>
    <receptor>GF</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>22</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.66</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1VGC</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>16.6183</bfactor-bindingsite>
    <bfactor-ligand>21.5834</bfactor-ligand>
    <backbone-hbond>-3.34</backbone-hbond>
    <cathid>1vgcC00</cathid>
    <dssp-bindingsite>B=5 C=36 E=23 S=18 T=18</dssp-bindingsite>
    <dssp-ligand>C=80 S=20</dssp-ligand>
    <description>GAMMA-CHYMOTRYPSIN L-PARA-CHLORO-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX</description>
    <foldx-energy>-14.33</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>10</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>23</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.78</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>6CHA</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>40.8373</bfactor-bindingsite>
    <bfactor-ligand>45.4327</bfactor-ligand>
    <backbone-hbond>-2.54</backbone-hbond>
    <cathid>6chaC00</cathid>
    <dssp-bindingsite>B=5 C=37 E=11 S=32 T=16</dssp-bindingsite>
    <dssp-ligand>C=78 S=22</dssp-ligand>
    <description>STRUCTURE OF A TETRAHEDRAL TRANSITION STATE COMPLEX OF ALPHA-*CHYMOTRYPSIN AT 1.8-*ANGSTROMS RESOLUTION</description>
    <foldx-energy>-9.95</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>9</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>11</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.05</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1N8O</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>22.2338</bfactor-bindingsite>
    <bfactor-ligand>27.4774</bfactor-ligand>
    <backbone-hbond>-3.82</backbone-hbond>
    <cathid>1n8oC00</cathid>
    <dssp-bindingsite>B=5 C=43 E=14 S=29 T=10</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>Crystal structure of a complex between bovine chymotrypsin and ecotin</description>
    <foldx-energy>-14.53</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>11</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>14</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-2.99</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>4GCH</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>19.2413</bfactor-bindingsite>
    <bfactor-ligand>31.7574</bfactor-ligand>
    <backbone-hbond>-3.19</backbone-hbond>
    <cathid>4gchG00</cathid>
    <dssp-bindingsite>B=5 C=42 E=16 S=26 T=11</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>STRUCTURE AND ACTIVITY OF TWO PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN</description>
    <foldx-energy>-11.45</foldx-energy>
    <ligand>E</ligand>
    <ligand-size>11</ligand-size>
    <receptor>GF</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>16</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.42</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>2CHA</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>-9999</bfactor-bindingsite>
    <bfactor-ligand>-9999</bfactor-ligand>
    <backbone-hbond>-1.26</backbone-hbond>
    <cathid>2chaC00</cathid>
    <dssp-bindingsite>B=5 C=42 E=11 S=32 T=11</dssp-bindingsite>
    <dssp-ligand>C=78 S=22</dssp-ligand>
    <description>THE STRUCTURE OF CRYSTALLINE ALPHA-CHYMOTRYPSIN, $V.THE ATOMIC STRUCTURE OF TOSYL-ALPHA-CHYMOTRYPSIN AT 2 ANGSTROMS RESOLUTION</description>
    <foldx-energy>-9.2</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>9</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>11</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.06</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>2GCH</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>27.6903</bfactor-bindingsite>
    <bfactor-ligand>41.6171</bfactor-ligand>
    <backbone-hbond>-3.34</backbone-hbond>
    <cathid>2gchG00</cathid>
    <dssp-bindingsite>B=5 C=40 E=20 S=25 T=10</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>REFINED CRYSTAL STRUCTURE OF GAMMA-CHYMOTRYPSIN AT 1.9 ANGSTROMS RESOLUTION</description>
    <foldx-energy>-12.65</foldx-energy>
    <ligand>E</ligand>
    <ligand-size>11</ligand-size>
    <receptor>GF</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>20</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.59</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>2P8O</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>8.6146</bfactor-bindingsite>
    <bfactor-ligand>11.9722</bfactor-ligand>
    <backbone-hbond>-3.27</backbone-hbond>
    <cathid>2p8oC00</cathid>
    <dssp-bindingsite>B=4 C=39 E=17 S=17 T=22</dssp-bindingsite>
    <dssp-ligand>C=80 S=20</dssp-ligand>
    <description>Crystal Structure of a Benzohydroxamic Acid/Vanadate complex bound to chymotrypsin A</description>
    <foldx-energy>-8.87</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>10</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>17</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.67</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>3BG4</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>36.5327</bfactor-bindingsite>
    <bfactor-ligand>44.6242</bfactor-ligand>
    <backbone-hbond>-3.11</backbone-hbond>
    <cathid></cathid>
    <dssp-bindingsite>B=5 C=50 E=23 S=18 T=5</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>The crystal structure of guamerin in complex with chymotrypsin and the development of an elastase-specific inhibitor</description>
    <foldx-energy>-13.47</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>11</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>23</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-2.66</sidechain-hbond>
    <uniprot-accession>P00766</uniprot-accession>
    <uniprot-decision>Chymotrypsinogen A</uniprot-decision>
    <uniprot-entry>CTRA_BOVIN</uniprot-entry>
    <uniprot-sequence>CGVPAIQPVLSGLSRIVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTTCVTTGWGLTRYTNANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN</uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>3GCH</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>21.2024</bfactor-bindingsite>
    <bfactor-ligand>33.8229</bfactor-ligand>
    <backbone-hbond>-2.92</backbone-hbond>
    <cathid></cathid>
    <dssp-bindingsite>B=5 C=38 E=19 S=24 T=14</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>CHEMISTRY OF CAGED ENZYMES. BINDING OF PHOTOREVERSIBLE CINNAMATES TO CHYMOTRYPSIN</description>
    <foldx-energy>-11.74</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>11</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>19</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.51</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>6GCH</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>39.4067</bfactor-bindingsite>
    <bfactor-ligand>46.5103</bfactor-ligand>
    <backbone-hbond>-3.11</backbone-hbond>
    <cathid>6gchG00</cathid>
    <dssp-bindingsite>B=5 C=45 E=14 S=27 T=9</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>STRUCTURE OF CHYMOTRYPSIN-*TRIFLUOROMETHYL KETONE INHIBITOR COMPLEXES. COMPARISON OF SLOWLY AND RAPIDLY EQUILIBRATING INHIBITORS</description>
    <foldx-energy>-15.49</foldx-energy>
    <ligand>E</ligand>
    <ligand-size>11</ligand-size>
    <receptor>GF</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>14</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.73</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1CA0</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>41.1006</bfactor-bindingsite>
    <bfactor-ligand>50.9987</bfactor-ligand>
    <backbone-hbond>-3.92</backbone-hbond>
    <cathid>1ca0C00</cathid>
    <dssp-bindingsite>B=4 C=39 E=17 S=17 T=22</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>BOVINE CHYMOTRYPSIN COMPLEXED TO APPI</description>
    <foldx-energy>-12.47</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>11</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>17</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-1.24</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>2GMT</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>14.4988</bfactor-bindingsite>
    <bfactor-ligand>15.2418</bfactor-ligand>
    <backbone-hbond>-3.23</backbone-hbond>
    <cathid></cathid>
    <dssp-bindingsite>B=6 C=44 E=17 S=17 T=17</dssp-bindingsite>
    <dssp-ligand>C=80 S=20</dssp-ligand>
    <description>THREE-DIMENSIONAL STRUCTURE OF CHYMOTRYPSIN INACTIVATED WITH (2S) N-ACETYL-L-ALANYL-L-PHENYLALANYL-CHLOROETHYL KETONE: IMPLICATIONS FOR THE MECHANISM OF INACTIVATION OF SERINE PROTEASES BY CHLOROKETONES</description>
    <foldx-energy>-12.57</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>10</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>17</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.64</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>2GCT</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>20.4244</bfactor-bindingsite>
    <bfactor-ligand>25.2898</bfactor-ligand>
    <backbone-hbond>-3.08</backbone-hbond>
    <cathid></cathid>
    <dssp-bindingsite>B=4 C=38 E=25 S=25 T=8</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>STRUCTURE OF GAMMA-CHYMOTRYPSIN IN THE RANGE PH 2.0 TO PH 10.5 SUGGESTS THAT GAMMA-CHYMOTRYPSIN IS A COVALENT ACYL-ENZYME ADDUCT AT LOW PH</description>
    <foldx-energy>-13.57</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>11</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>25</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.45</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1DLK</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>36.392</bfactor-bindingsite>
    <bfactor-ligand>46.8912</bfactor-ligand>
    <backbone-hbond>-3.88</backbone-hbond>
    <cathid></cathid>
    <dssp-bindingsite>B=4 C=37 E=26 S=19 T=15</dssp-bindingsite>
    <dssp-ligand>C=77 S=23</dssp-ligand>
    <description>CRYSTAL STRUCTURE ANALYSIS OF DELTA-CHYMOTRYPSIN BOUND TO A PEPTIDYL CHLOROMETHYL KETONE INHIBITOR</description>
    <foldx-energy>-12.85</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>13</ligand-size>
    <receptor>C</receptor>
    <scop-class>All beta proteins</scop-class>
    <scop-id>d1dlk.2</scop-id>
    <ss-bindingsite>26</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-1.14</sidechain-hbond>
    <uniprot-accession>P00766</uniprot-accession>
    <uniprot-decision>Chymotrypsinogen A</uniprot-decision>
    <uniprot-entry>CTRA_BOVIN</uniprot-entry>
    <uniprot-sequence>CGVPAIQPVLSGLSRIVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTTCVTTGWGLTRYTNANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN</uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1YPH</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>26.1512</bfactor-bindingsite>
    <bfactor-ligand>35.2142</bfactor-ligand>
    <backbone-hbond>-3.22</backbone-hbond>
    <cathid>1yphE00</cathid>
    <dssp-bindingsite>B=5 C=41 E=18 S=18 T=18</dssp-bindingsite>
    <dssp-ligand>C=80 S=20</dssp-ligand>
    <description>High resolution structure of bovine alpha-chymotrypsin</description>
    <foldx-energy>-12.72</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>10</ligand-size>
    <receptor>EC</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>18</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.75</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>2JET</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>88.6474</bfactor-bindingsite>
    <bfactor-ligand>91.9194</bfactor-ligand>
    <backbone-hbond>-3.77</backbone-hbond>
    <cathid>2jetC00</cathid>
    <dssp-bindingsite>B=4 C=30 E=17 S=35 T=13</dssp-bindingsite>
    <dssp-ligand>C=67 S=33</dssp-ligand>
    <description>CRYSTAL STRUCTURE OF A TRYPSIN-LIKE MUTANT (S189D, A226G) CHYMOTRYPSIN.</description>
    <foldx-energy>-13.11</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>12</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>17</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-1.13</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>7GCH</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>37.8203</bfactor-bindingsite>
    <bfactor-ligand>46.1518</bfactor-ligand>
    <backbone-hbond>-2.63</backbone-hbond>
    <cathid>7gchG00</cathid>
    <dssp-bindingsite>B=5 C=47 E=16 S=26 T=5</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>STRUCTURE OF CHYMOTRYPSIN-*TRIFLUOROMETHYL KETONE INHIBITOR COMPLEXES. COMPARISON OF SLOWLY AND RAPIDLY EQUILIBRATING INHIBITORS</description>
    <foldx-energy>-12.7</foldx-energy>
    <ligand>E</ligand>
    <ligand-size>11</ligand-size>
    <receptor>GF</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>16</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.39</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1GCT</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>18.2446</bfactor-bindingsite>
    <bfactor-ligand>23.4898</bfactor-ligand>
    <backbone-hbond>-3.23</backbone-hbond>
    <cathid></cathid>
    <dssp-bindingsite>B=5 C=41 E=18 S=27 T=9</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?</description>
    <foldx-energy>-13.04</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>11</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>18</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.62</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1GMC</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>12.682</bfactor-bindingsite>
    <bfactor-ligand>22.4577</bfactor-ligand>
    <backbone-hbond>-3.24</backbone-hbond>
    <cathid>1gmcG00</cathid>
    <dssp-bindingsite>B=5 C=36 E=18 S=18 T=23</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>THE X-RAY CRYSTAL STRUCTURE OF THE TETRAHEDRAL INTERMEDIATE OF GAMMA-CHYMOTRYPSIN IN HEXANE</description>
    <foldx-energy>-13.63</foldx-energy>
    <ligand>E</ligand>
    <ligand-size>11</ligand-size>
    <receptor>GF</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>18</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.61</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>2VGC</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>20.3621</bfactor-bindingsite>
    <bfactor-ligand>25.835</bfactor-ligand>
    <backbone-hbond>-3.36</backbone-hbond>
    <cathid>2vgcC00</cathid>
    <dssp-bindingsite>B=5 C=40 E=20 S=25 T=10</dssp-bindingsite>
    <dssp-ligand>C=80 S=20</dssp-ligand>
    <description>GAMMA-CHYMOTRYPSIN D-PARA-CHLORO-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX</description>
    <foldx-energy>-13.26</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>10</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>20</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.75</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>3VGC</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>18.4945</bfactor-bindingsite>
    <bfactor-ligand>25.0732</bfactor-ligand>
    <backbone-hbond>-3.25</backbone-hbond>
    <cathid>3vgcC00</cathid>
    <dssp-bindingsite>B=5 C=36 E=23 S=18 T=18</dssp-bindingsite>
    <dssp-ligand>C=80 S=20</dssp-ligand>
    <description>GAMMA-CHYMOTRYPSIN L-NAPHTHYL-1-ACETAMIDO BORONIC ACID ACID INHIBITOR COMPLEX</description>
    <foldx-energy>-13.38</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>10</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>23</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.75</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1HJA</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>25.3925</bfactor-bindingsite>
    <bfactor-ligand>30.8152</bfactor-ligand>
    <backbone-hbond>-2.94</backbone-hbond>
    <cathid>1hjaC00</cathid>
    <dssp-bindingsite>B=5 C=36 E=23 S=23 T=14</dssp-bindingsite>
    <dssp-ligand>C=80 S=20</dssp-ligand>
    <description>LYS 18 VARIANT OF TURKEY OVOMUCOID INHIBITOR THIRD DOMAIN COMPLEXED WITH ALPHA-CHYMOTRYPSIN</description>
    <foldx-energy>-13.05</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>10</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>23</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.49</sidechain-hbond>
    <uniprot-accession>P00766</uniprot-accession>
    <uniprot-decision>Chymotrypsinogen A</uniprot-decision>
    <uniprot-entry>CTRA_BOVIN</uniprot-entry>
    <uniprot-sequence>CGVPAIQPVLSGLSRIVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTTCVTTGWGLTRYTNANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN</uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1GG6</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>14.1041</bfactor-bindingsite>
    <bfactor-ligand>15.6881</bfactor-ligand>
    <backbone-hbond>-3.26</backbone-hbond>
    <cathid>1gg6C00</cathid>
    <dssp-bindingsite>B=4 C=38 E=21 S=25 T=13</dssp-bindingsite>
    <dssp-ligand>C=80 S=20</dssp-ligand>
    <description>CRYSTAL STUCTURE OF GAMMA CHYMOTRYPSIN WITH N-ACETYL-PHENYLALANINE TRIFLUOROMETHYL KETONE BOUND AT THE ACTIVE SITE</description>
    <foldx-energy>-11.56</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>10</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>21</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.59</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>4VGC</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>21.6909</bfactor-bindingsite>
    <bfactor-ligand>27.3137</bfactor-ligand>
    <backbone-hbond>-3.28</backbone-hbond>
    <cathid>4vgcC00</cathid>
    <dssp-bindingsite>B=4 C=38 E=21 S=17 T=21</dssp-bindingsite>
    <dssp-ligand>C=80 S=20</dssp-ligand>
    <description>GAMMA-CHYMOTRYPSIN D-NAPHTHYL-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX</description>
    <foldx-energy>-13.2</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>10</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>21</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.71</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>4CHA</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>25.8277</bfactor-bindingsite>
    <bfactor-ligand>41.3701</bfactor-ligand>
    <backbone-hbond>-3.13</backbone-hbond>
    <cathid>4chaC00</cathid>
    <dssp-bindingsite>B=5 C=33 E=19 S=33 T=10</dssp-bindingsite>
    <dssp-ligand>C=73 S=27</dssp-ligand>
    <description>STRUCTURE OF ALPHA-*CHYMOTRYPSIN REFINED AT 1.68 ANGSTROMS RESOLUTION</description>
    <foldx-energy>-7.69</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>11</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>19</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.73</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1CHO</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>25.4677</bfactor-bindingsite>
    <bfactor-ligand>33.028</bfactor-ligand>
    <backbone-hbond>-3.07</backbone-hbond>
    <cathid>1choG00</cathid>
    <dssp-bindingsite>B=5 C=40 E=15 S=25 T=15</dssp-bindingsite>
    <dssp-ligand>C=80 S=20</dssp-ligand>
    <description>CRYSTAL AND MOLECULAR STRUCTURES OF THE COMPLEX OF ALPHA-*CHYMOTRYPSIN WITH ITS INHIBITOR TURKEY OVOMUCOID THIRD DOMAIN AT 1.8 ANGSTROMS RESOLUTION</description>
    <foldx-energy>-14.42</foldx-energy>
    <ligand>E</ligand>
    <ligand-size>10</ligand-size>
    <receptor>GF</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>15</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.63</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>3GCT</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>19.9668</bfactor-bindingsite>
    <bfactor-ligand>26.171</bfactor-ligand>
    <backbone-hbond>-3.25</backbone-hbond>
    <cathid>3gctG00</cathid>
    <dssp-bindingsite>B=5 C=41 E=18 S=27 T=9</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>STRUCTURE OF GAMMA-*CHYMOTRYPSIN IN THE RANGE $P*H 2.0 TO $P*H 10.5 SUGGESTS THAT GAMMA-CHYMOTRYPSIN IS A COVALENT ACYL-ENZYME ADDUCT AT LOW $P*H</description>
    <foldx-energy>-13.37</foldx-energy>
    <ligand>E</ligand>
    <ligand-size>11</ligand-size>
    <receptor>GF</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>18</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.72</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>8GCH</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>33.2291</bfactor-bindingsite>
    <bfactor-ligand>42.5639</bfactor-ligand>
    <backbone-hbond>-3.24</backbone-hbond>
    <cathid>8gchG00</cathid>
    <dssp-bindingsite>B=4 C=40 E=20 S=24 T=12</dssp-bindingsite>
    <dssp-ligand>C=82 S=18</dssp-ligand>
    <description>GAMMA-CHYMOTRYPSIN IS A COMPLEX OF ALPHA-CHYMOTRYPSIN WITH ITS OWN AUTOLYSIS PRODUCTS</description>
    <foldx-energy>-15.16</foldx-energy>
    <ligand>E</ligand>
    <ligand-size>11</ligand-size>
    <receptor>GF</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>20</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.65</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1GGD</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>12.7441</bfactor-bindingsite>
    <bfactor-ligand>17.2941</bfactor-ligand>
    <backbone-hbond>-3.3</backbone-hbond>
    <cathid>1ggdC00</cathid>
    <dssp-bindingsite>B=5 C=36 E=23 S=27 T=9</dssp-bindingsite>
    <dssp-ligand>C=80 S=20</dssp-ligand>
    <description>CRYSTAL STUCTURE OF GAMMA CHYMOTRYPSIN WITH N-ACETYL-LEUCIL-PHENYLALANINE ALDEHYDE BOUND AT THE ACTIVE SITE</description>
    <foldx-energy>-13.07</foldx-energy>
    <ligand>A</ligand>
    <ligand-size>10</ligand-size>
    <receptor>CB</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>23</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.69</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
  <node>
    <cluster-id>26843</cluster-id>
    <pdb-id>1GMH</pdb-id>
    <alignment></alignment>
    <bfactor-bindingsite>-9999</bfactor-bindingsite>
    <bfactor-ligand>-9999</bfactor-ligand>
    <backbone-hbond>-3.4</backbone-hbond>
    <cathid>1gmhG00</cathid>
    <dssp-bindingsite>B=5 C=36 E=23 S=27 T=9</dssp-bindingsite>
    <dssp-ligand>C=80 S=20</dssp-ligand>
    <description>REFINED CRYSTAL STRUCTURE OF \&amp;quot;AGED\&amp;quot; AND \&amp;quot;NON-AGED\&amp;quot; ORGANOPHOSPHORYL CONJUGATES OF GAMMA-CHYMOTRYPSIN</description>
    <foldx-energy>-11.59</foldx-energy>
    <ligand>E</ligand>
    <ligand-size>10</ligand-size>
    <receptor>GF</receptor>
    <scop-class></scop-class>
    <scop-id></scop-id>
    <ss-bindingsite>23</ss-bindingsite>
    <ss-ligand>0</ss-ligand>
    <sidechain-hbond>-0.73</sidechain-hbond>
    <uniprot-accession></uniprot-accession>
    <uniprot-decision></uniprot-decision>
    <uniprot-entry></uniprot-entry>
    <uniprot-sequence></uniprot-sequence>
  </node>
</xml>

