<?xml version="1.0" encoding="UTF-8"?>
<ProteinModifications>
    <Revisions>
    <Revision>
    	<Date>2011-08-12</Date>
    		<Change>Added glycosylation entries 386-429</Change>
   		</Revision>
    	<Revision>
    		<Date>2011-07-26</Date>
    		<Change>Added PDBCC cross-references</Change>
   		</Revision>
    </Revisions>
	<Entry>
		<Id>0001</Id>
		<Description>a protein modification that effectively forms a O3-xylosylserine.</Description>
		<SystematicName>(S)-2-amino-3-(alpha-D-xylopyranosyloxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0406</Id>
			<Name>O-xylosyl-L-serine</Name>
			<Status>deprecated</Status>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00814</Id>
			<Name>O-xylosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>XYS</Id>
			<Name>xylopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">XYS</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0002</Id>
		<Description>A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine.</Description>
		<SystematicName>(S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)amino-4-oxobutanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0151</Id>
			<Name>N4-(N-acetylamino)glucosyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00831</Id>
			<Name>N4-(N-acetylamino)glucosyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NAG</Id>
			<Name>N-acetyl-D-glucosamine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ASN</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">NAG</Id>
			</Component>
			<Bond>
				<Atom component="1">ND2</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0003</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-phospho-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-(phosphonosulfanyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CSP</Id>
			<Name>S-phosphocysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0034</Id>
			<Name>S-phospho-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00043</Id>
			<Name>S-phospho-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CSP</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0004</Id>
		<Description>A protein modification that effectively converts an L-histidine residue to tele-phospho-L-histidine (Ntau-phospho-L-histidine, 1'-phospho-L-histidine).</Description>
		<SystematicName>(S)-2-amino-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NEP</Id>
			<Name>N1-phosphonohistidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0035</Id>
			<Name>1'-phospho-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00044</Id>
			<Name>1'-phospho-L-histidine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">NEP</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0005</Id>
		<Description>A protein modification that effectively converts an L-histidine residue to pros-phospho-L-histidine (Npi-phospho-L-histidine, 3'-phospho-L-histidine).</Description>
		<SystematicName>(S)-2-amino-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HIP</Id>
			<Name>ND1-phosphonohistidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0036</Id>
			<Name>3'-phospho-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00045</Id>
			<Name>3'-phospho-L-histidine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HIP</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>phosphohistidine</Keyword>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0006</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O-phospho-L-serine.</Description>
		<SystematicName>(S)-2-amino-3-(phosphonooxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SEP</Id>
			<Name>phosphoserine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0037</Id>
			<Name>O-phospho-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00046</Id>
			<Name>O-phospho-L-serine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SEP</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0007</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to O-phospho-L-threonine.</Description>
		<SystematicName>(2S,3R)-2-amino-3-phosphonooxybutanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>TPO</Id>
			<Name>phosphothreonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0038</Id>
			<Name>O-phospho-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00047</Id>
			<Name>O-phospho-L-threonine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TPO</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0008</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to O4'-phospho-L-tyrosine.</Description>
		<SystematicName>(2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PTR</Id>
			<Name>O-phosphotyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0039</Id>
			<Name>O4'-phospho-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00048</Id>
			<Name>O4'-phospho-L-tyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">PTR</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0009</Id>
		<Description>A protein modification that effectively converts an L-glutamine residue to N-acetyl-L-glutamine.</Description>
		<SystematicName>(S)-2-acetamido-5-pentanediamic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ACE</Id>
			<Name>acetyl group</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0045</Id>
			<Name>N-acetyl-L-glutamine</Name>
			<Status>deprecated</Status>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00054</Id>
			<Name>N-acetyl-L-glutamine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLN</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ACE</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0010</Id>
		<Description>A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine.</Description>
		<SystematicName>(2S)-2-acetamido-4-(methylsulfanyl)butanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0049</Id>
			<Name>N-acetyl-L-methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00058</Id>
			<Name>N-acetyl-L-methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ACE</Id>
			<Name>acetyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MET</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ACE</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>thioether bond</Keyword>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0011</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to N6-acetyl-L-lysine.</Description>
		<SystematicName>(2S)-2-amino-6-acetamidohexanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ALY</Id>
			<Name>N(6)-acetyllysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0055</Id>
			<Name>N6-acetyl-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00064</Id>
			<Name>N6-acetyl-L-lysine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ALY</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>acetyllysine</Keyword>
	</Entry>
	<Entry>
		<Id>0012</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to O4'-sulfo-L-tyrosine.</Description>
		<SystematicName>(S)-2-amino-3-(4-sulfooxyphenyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>TYS</Id>
			<Name>O-sulfo-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0172</Id>
			<Name>O4'-sulfo-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00181</Id>
			<Name>O4'-sulfo-L-tyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYS</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>sulfoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0013</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine.</Description>
		<SystematicName>(S)-2-amino-6-methylaminohexanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MLZ</Id>
			<Name>N-methyl-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0076</Id>
			<Name>N6-methyl-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00085</Id>
			<Name>N6-methyl-L-lysine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MLZ</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0014</Id>
		<Description>A protein modification that effectively converts an L-arginine residue to 5-methyl-L-arginine.</Description>
		<SystematicName>(2S,5S)-2-amino-5-carbamimidamidohexanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>AGM</Id>
			<Name>5-methyl-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0272</Id>
			<Name>5-methyl-L-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00277</Id>
			<Name>5-methyl-L-arginine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">AGM</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0015</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to N6,N6,N6-trimethyl-L-lysine.</Description>
		<SystematicName>(5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>M3L</Id>
			<Name>N-trimethyllysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0074</Id>
			<Name>N6,N6,N6-trimethyl-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00083</Id>
			<Name>N6,N6,N6-trimethyl-L-lysine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">M3L</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0016</Id>
		<Description>A protein modification that effectively converts an L-methionine residue to N-methyl-L-methionine.</Description>
		<SystematicName>(S)-2-methylamino-4-(methylsulfanyl)butanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MME</Id>
			<Name>N-methyl methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0064</Id>
			<Name>N-methyl-L-methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00073</Id>
			<Name>N-methyl-L-methionine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MME</Id>
				<Terminal>N</Terminal>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>thioether bond</Keyword>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0017</Id>
		<Description>A protein modification that effectively converts an L-proline residue to 4-hydroxy-L-proline.</Description>
		<SystematicName>(2S,4R)-4-hydroxypyrrolidine-2-carboxylic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HYP</Id>
			<Name>4-hydroxyproline</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0030</Id>
			<Name>4-hydroxy-L-proline</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00039</Id>
			<Name>4-hydroxy-L-proline</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HYP</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>hydroxylation</Keyword>
	</Entry>
	<Entry>
		<Id>0018</Id>
		<Description>A protein modification that effectively cross-links two L-cysteine residues to form L-cystine.</Description>
		<SystematicName>(R,R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0025</Id>
			<Name>L-cystine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00034</Id>
			<Name>L-cystine (cross-link)</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">SG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>redox-active center</Keyword>
		<Keyword>disulfide bond</Keyword>
	</Entry>
	<Entry>
		<Id>0019</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl disulfide.</Description>
		<SystematicName>(R)-2-amino-3-(methyldisulfanediyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SCH</Id>
			<Name>S-Methyl-thio-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0101</Id>
			<Name>L-cysteine methyl disulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00110</Id>
			<Name>L-cysteine methyl disulfide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SCH</Id>
			</Component>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>modified residue</Category>
		<Keyword>disulfide bond</Keyword>
	</Entry>
	<Entry>
		<Id>0020</Id>
		<Description>A protein modification that effectively converts three L-cysteine residues and a three-iron four-sulfur cluster to tris-L-cysteinyl triiron tetrasulfide.</Description>
		<SystematicName>mu3-sulfido-tri-mu-sulfidotris(cysteinato-kappaS-iron)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0139</Id>
			<Name>tris-L-cysteinyl triiron tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00148</Id>
			<Name>tris-L-cysteinyl triiron tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>F3S</Id>
			<Name>Fe3-S4 cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">F3S</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="4">FE1</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="4">FE3</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="4">FE4</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink3</Category>
		<Keyword>3Fe-4S</Keyword>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0021</Id>
		<Description>A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to tetrakis-L-cysteinyl diiron disulfide.</Description>
		<SystematicName>tetrakis(cysteinato)-1kappaS,1kappaS,2kappaS,2kappaS-di-mu-sulfidodiiron</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0137</Id>
			<Name>tetrakis-L-cysteinyl diiron disulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00146</Id>
			<Name>tetrakis-L-cysteinyl diiron disulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FES</Id>
			<Name>Fe2/S2 (inorganic) cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">FES</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="5" atom="1">FE1</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="5" atom="1">FE1</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="5" atom="2">FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="4">SG</Atom>
				<Atom component="5" atom="2">FE2</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink4</Category>
		<Keyword>2Fe-2S</Keyword>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0022</Id>
		<Description>A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification.</Description>
		<SystematicName>(S)-2-formylamino-4-(methylsulfanyl)butanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FME</Id>
			<Name>N-formylmethionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0021</Id>
			<Name>N-formyl-L-methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00030</Id>
			<Name>N-formyl-L-methionine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">FME</Id>
				<Terminal>N</Terminal>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>thioether bond</Keyword>
		<Keyword>blocked amino end</Keyword>
		<Keyword>formylation</Keyword>
		<Keyword>pretranslational modification</Keyword>
	</Entry>
	<Entry>
		<Id>0023</Id>
		<Description>A protein modification that effectively converts a source amino acid residue to an L-selenocysteine, a natural pretranslational modification.</Description>
		<SystematicName>(R)-2-amino-3-selanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CSE</Id>
			<Name>selenocysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0022</Id>
			<Name>L-selenocysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00031</Id>
			<Name>L-selenocysteine residue</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CSE</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>pretranslational modification</Keyword>
		<Keyword>selenium</Keyword>
		<Keyword>selenocysteine</Keyword>
	</Entry>
	<Entry>
		<Id>0024</Id>
		<Description>A protein modification that effectively converts an L-asparagine residue to (2S,3R)-3-hydroxyasparagine.</Description>
		<SystematicName>(2S,3R)-2-amino-3-hydroxy-4-butanediamic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>AHB</Id>
			<Name>beta-hydroxyasparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0026</Id>
			<Name>(2S,3R)-3-hydroxyasparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00035</Id>
			<Name>(2S,3R)-3-hydroxyasparagine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">AHB</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>hydroxylation</Keyword>
	</Entry>
	<Entry>
		<Id>0025</Id>
		<Description>A protein modification that effectively converts an L-aspartic acid residue to (2S,3R)-3-hydroxyaspartic acid.</Description>
		<SystematicName>(2S,3R)-2-amino-3-hydroxybutanedioic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BHD</Id>
			<Name>beta-hydroxyaspartic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0027</Id>
			<Name>(2S,3R)-3-hydroxyaspartic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00036</Id>
			<Name>(2S,3R)-3-hydroxyaspartic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">BHD</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>hydroxylation</Keyword>
	</Entry>
	<Entry>
		<Id>0026</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to 5-hydroxy-L-lysine.</Description>
		<SystematicName>(2S,5R)-2,6-diamino-5-hydroxyhexanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>LYZ</Id>
			<Name>5-hydroxylysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0028</Id>
			<Name>5-hydroxy-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00037</Id>
			<Name>5-hydroxy-L-lysine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYZ</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>hydroxylation</Keyword>
	</Entry>
	<Entry>
		<Id>0027</Id>
		<Description>A protein modification that effectively converts an L-proline residue to 3-hydroxy-L-proline.</Description>
		<SystematicName>(2S,3S)-3-hydroxypyrrolidine-2-carboxylic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HY3</Id>
			<Name>3-hydroxyproline</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0029</Id>
			<Name>3-hydroxy-L-proline</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00038</Id>
			<Name>3-hydroxy-L-proline</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HY3</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>hydroxylation</Keyword>
	</Entry>
	<Entry>
		<Id>0028</Id>
		<Description>A protein modification that effectively converts an L-glutamine residue to 2-pyrrolidone-5-carboxylic acid.</Description>
		<SystematicName>(S)-5-oxo-2-pyrrolidinecarboxylic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PCA</Id>
			<Name>pyroglutamic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0031</Id>
			<Name>2-pyrrolidone-5-carboxylic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00040</Id>
			<Name>2-pyrrolidone-5-carboxylic acid (Gln)</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">PCA</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>blocked amino end</Keyword>
		<Keyword>pyroglutamic acid</Keyword>
	</Entry>
	<Entry>
		<Id>0029</Id>
		<Description>A protein modification that effectively converts an L-glutamic acid residue to L-gamma-carboxyglutamic acid.</Description>
		<SystematicName>(S)-3-amino-1,1,3-propanetricarboxylic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CGU</Id>
			<Name>gamma-carboxy-glutamic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0032</Id>
			<Name>L-gamma-carboxyglutamic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00041</Id>
			<Name>L-gamma-carboxyglutamic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CGU</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>carboxyglutamic acid</Keyword>
	</Entry>
	<Entry>
		<Id>0030</Id>
		<Description>A protein modification that effectively converts an L-aspartic acid residue to L-aspartic 4-phosphoric anhydride.</Description>
		<SystematicName>(2S)-2-amino-4-oxo-4-(phosphonooxy)butanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PHD</Id>
			<Name>aspartyl phosphate</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0033</Id>
			<Name>L-aspartic 4-phosphoric anhydride</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00042</Id>
			<Name>L-aspartic 4-phosphoric anhydride</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">PHD</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0031</Id>
		<Description>A protein modification that effectively converts an L-histidine residue to diphthamide.</Description>
		<SystematicName>(2R)-1-amino-4-(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-aminium</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DDE</Id>
		    <Name>{3-[4-(2-amino-2-carboxy-ethyl)-1H-imidazol-2-yl]-1-carbamoyl-propyl}-trimethyl-ammonium</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0040</Id>
			<Name>2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00049</Id>
			<Name>2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DDE</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>diphthamide</Keyword>
	</Entry>
	<Entry>
		<Id>0032</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-acetyl-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-(acetylsulfanyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SCY</Id>
			<Name>S-acetyl-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0056</Id>
			<Name>S-acetyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00065</Id>
			<Name>S-acetyl-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SCY</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>thioester bond</Keyword>
	</Entry>
	<Entry>
		<Id>0033</Id>
		<Description>A protein modification that effectively converts a glycine residue to N-myristoylglycine.</Description>
		<SystematicName>(tetradecanoylamino)ethanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0059</Id>
			<Name>N-myristoyl-glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00068</Id>
			<Name>N-myristoylglycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MYR</Id>
			<Name>myristic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLY</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">MYR</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>blocked amino end</Keyword>
		<Keyword>lipoprotein</Keyword>
		<Keyword>myristoylation</Keyword>
	</Entry>
	<Entry>
		<Id>0034</Id>
		<Description>A protein modification that effectively converts an L-alanine residue to N-methyl-L-alanine.</Description>
		<SystematicName>(S)-2-methylaminopropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MAA</Id>
			<Name>N-methyl-L-alanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0061</Id>
			<Name>N-methyl-L-alanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00070</Id>
			<Name>N-methyl-L-alanine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MAA</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0035</Id>
		<Description>A protein modification that effectively converts an L-phenylalanine residue to N-methyl-L-phenylalanine.</Description>
		<SystematicName>(S)-2-methylamino-3-phenylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MEA</Id>
			<Name>N-methylphenylalanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0065</Id>
			<Name>N-methyl-L-phenylalanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00074</Id>
			<Name>N-methyl-L-phenylalanine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MEA</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0036</Id>
		<Description>A protein modification that effectively converts an L-proline residue to N,N-dimethyl-L-proline.</Description>
		<SystematicName>(S)-2-carboxy-1,1-dimethylpyrrolidinium</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0066</Id>
			<Name>N,N-dimethyl-L-proline</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00075</Id>
			<Name>N,N-dimethyl-L-proline</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PBE</Id>
			<Name>1,1-dimethyl-prolinium</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">PBE</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>blocked amino end</Keyword>
		<Keyword>methylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0037</Id>
		<Description>A protein modification that effectively converts an L-arginine residue to N(omega),N'(omega)-dimethyl-L-arginine.</Description>
		<SystematicName>(S)-2-amino-5-[((methylamino)(methylimino)methyl)amino]pentanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>2MR</Id>
			<Name>N3,N4-dimethylarginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0067</Id>
			<Name>omega-N,omega-N'-dimethyl-L-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00076</Id>
			<Name>omega-N,omega-N'-dimethyl-L-arginine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">2MR</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0038</Id>
		<Description>A protein modification that effectively converts an L-arginine residue to N(omega),N(omega)-dimethyl-L-arginine.</Description>
		<SystematicName>(S)-2-amino-5-([(dimethylamino)(imino)methyl]amino)pentanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DA2</Id>
			<Name>NG,NG-dimethyl-L-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0068</Id>
			<Name>omega-N,omega-N-dimethyl-L-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00077</Id>
			<Name>omega-N,omega-N-dimethyl-L-arginine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DA2</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0039</Id>
		<Description>A protein modification that effectively converts an L-asparagine residue to N4-methyl-L-asparagine.</Description>
		<SystematicName>(S)-2-amino-N4-methylbutanediamic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MEN</Id>
			<Name>N-methyl asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0070</Id>
			<Name>N4-methyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00079</Id>
			<Name>N4-methyl-L-asparagine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MEN</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0040</Id>
		<Description>A protein modification that effectively converts an L-glutamine residue to N5-methyl-L-glutamine.</Description>
		<SystematicName>(2S)-2-amino-5-methylamino-5-oxopentanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MEQ</Id>
			<Name>N5-methylglutamine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0071</Id>
			<Name>N5-methyl-L-glutamine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00080</Id>
			<Name>N5-methyl-L-glutamine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MEQ</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0041</Id>
		<Description>A protein modification that effectively converts an L-histidine residue to pros-methyl-L-histidine (N-pi-methyl-L-histidine, 3'-methyl-L-histidine).</Description>
		<SystematicName>(S)-2-amino-3-(3-methyl-3H-imidazol-4-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MHS</Id>
			<Name>N1-methylated histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0073</Id>
			<Name>3'-methyl-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00082</Id>
			<Name>3'-methyl-L-histidine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MHS</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0042</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to N6,N6-dimethyl-L-lysine.</Description>
		<SystematicName>(S)-2-amino-6-dimethylaminohexanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MLY</Id>
			<Name>N-dimethyl-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0075</Id>
			<Name>N6,N6-dimethyl-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00084</Id>
			<Name>N6,N6-dimethyl-L-lysine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MLY</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0043</Id>
		<Description>A protein modification that effectively converts an L-arginine residue to L-arginine amide.</Description>
		<SystematicName>(S)-2-amino-5-carbamimidamidopentanamide</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>AAR</Id>
			<Name>arginineamide</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0082</Id>
			<Name>L-arginine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00091</Id>
			<Name>L-arginine amide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">AAR</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0044</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to L-cysteine amide.</Description>
		<SystematicName>(R)-2-amino-3-sulfanylpropanamide</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CY3</Id>
			<Name>2-amino-3-mercapto-propionamide</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0085</Id>
			<Name>L-cysteine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00094</Id>
			<Name>L-cysteine amide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CY3</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0045</Id>
		<Description>A protein modification that effectively converts an L-leucine residue to L-leucine amide.</Description>
		<SystematicName>(S)-2-amino-4-methylpentanamide</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CLE</Id>
			<Name>leucine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0091</Id>
			<Name>L-leucine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00100</Id>
			<Name>L-leucine amide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CLE</Id>
				<Terminal>C</Terminal>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0046</Id>
		<Description>A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide.</Description>
		<SystematicName>(S)-2-amino-3-phenylpropanamide</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NFA</Id>
			<Name>phenylalanine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0094</Id>
			<Name>L-phenylalanine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00103</Id>
			<Name>L-phenylalanine amide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">NFA</Id>
				<Terminal>C</Terminal>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0047</Id>
		<Description>A protein modification that effectively converts an L-proline residue to L-proline amide.</Description>
		<SystematicName>(S)-pyrrolidine-2-carboxamide</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>LPD</Id>
			<Name>L-prolinamide</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0095</Id>
			<Name>L-proline amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00104</Id>
			<Name>L-proline amide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LPD</Id>
				<Terminal>C</Terminal>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0048</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide.</Description>
		<SystematicName>(S)-2-amino-3-(4-hydoxyphenyl)propanamide</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>TYC</Id>
			<Name>L-tyrosineamide</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0099</Id>
			<Name>L-tyrosine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00108</Id>
			<Name>L-tyrosine amide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYC</Id>
				<Terminal>C</Terminal>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0049</Id>
		<Description>A protein modification that effectively converts an L-valine residue to L-valine amide.</Description>
		<SystematicName>(S)-2-amino-3-methylbutanamide</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>VLM</Id>
			<Name>valinylamine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0100</Id>
			<Name>L-valine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00109</Id>
			<Name>L-valine amide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">VLM</Id>
				<Terminal>C</Terminal>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0050</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl ester.</Description>
		<SystematicName>methyl (2R)-2-amino-3-sulfanylpropanoate</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CMT</Id>
			<Name>O-methylcysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0105</Id>
			<Name>L-cysteine methyl ester</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00114</Id>
			<Name>L-cysteine methyl ester</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CMT</Id>
				<Terminal>C</Terminal>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0051</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-(hexadecanoylsulfanyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>P1L</Id>
			<Name>S-palmitoyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0106</Id>
			<Name>S-palmitoyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00115</Id>
			<Name>S-palmitoyl-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">P1L</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>lipoprotein</Keyword>
		<Keyword>palmitoylation</Keyword>
		<Keyword>thioester bond</Keyword>
	</Entry>
	<Entry>
		<Id>0052</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-(hexadecanoylsulfanyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0106</Id>
			<Name>S-palmitoyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00115</Id>
			<Name>S-palmitoyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PLM</Id>
			<Name>palmitic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PLM</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>lipoprotein</Keyword>
		<Keyword>palmitoylation</Keyword>
		<Keyword>thioester bond</Keyword>
	</Entry>
	<Entry>
		<Id>0053</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to N6-carboxy-L-lysine.</Description>
		<SystematicName>(S)-2-amino-6-(carboxyamino)hexanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>KCX</Id>
			<Name>lysine NZ-carboxylic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0114</Id>
			<Name>N6-carboxy-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00123</Id>
			<Name>N6-carboxy-L-lysine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">KCX</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0054</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to N6-1-carboxyethyl-L-lysine.</Description>
		<SystematicName>(S,S)-2-amino-6-(1-carboxyethyl)aminohexanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MCL</Id>
			<Name>NZ-(1-carboxyethyl)-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0115</Id>
			<Name>N6-1-carboxyethyl-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00124</Id>
			<Name>N6-1-carboxyethyl-L-lysine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MCL</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0055</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to N6-biotinyl-L-lysine.</Description>
		<SystematicName>(S)-2-amino-6-[5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl]aminohexanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0117</Id>
			<Name>N6-biotinyl-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00126</Id>
			<Name>N6-biotinyl-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BTN</Id>
			<Name>biotin</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">BTN</Id>
			</Component>
			<Bond>
				<Atom component="1">NZ</Atom>
				<Atom component="2">C11</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>biotin</Keyword>
	</Entry>
	<Entry>
		<Id>0056</Id>
		<Description>A protein modification that effectively crosslinks an L-glutamine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoglutamyl)-L-lysine and the release of ammonia.</Description>
		<SystematicName>(S,S)-2-amino-6-[(4-amino-4-carboxybutanoyl)amino]hexanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0124</Id>
			<Name>N6-(L-isoglutamyl)-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00133</Id>
			<Name>N6-(L-isoglutamyl)-L-lysine (Gln)</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GLN</Id>
			</Component>
			<Bond>
				<Atom component="1">NZ</Atom>
				<Atom component="2">CD</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>isopeptide bond</Keyword>
	</Entry>
	<Entry>
		<Id>0057</Id>
		<Description>A protein modification that effectively crosslinks an L-glutamic acid residue and an L-lysine residue by an isopeptide bond to form N6-(L-isoglutamyl)-L-lysine.</Description>
		<SystematicName>(S,S)-2-amino-6-[(4-amino-4-carboxybutanoyl)amino]hexanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0124</Id>
			<Name>N6-(L-isoglutamyl)-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01484</Id>
			<Name>N6-(L-isoglutamyl)-L-lysine (Glu)</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GLU</Id>
			</Component>
			<Bond>
				<Atom component="1">NZ</Atom>
				<Atom component="2">CD</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>isopeptide bond</Keyword>
	</Entry>
	<Entry>
		<Id>0058</Id>
		<Description>A protein modification that effectively crosslinks an L-lysine residue and a glycine residue by an isopeptide bond to form N6-glycyl-L-lysine.</Description>
		<SystematicName>(S)-2-amino-6-[(aminoacetyl)amino]hexanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0125</Id>
			<Name>N6-glycyl-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00134</Id>
			<Name>N6-glycyl-L-lysine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GLY</Id>
				<Terminal>C</Terminal>
			</Component>
			<Bond>
				<Atom component="1">NZ</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked carboxyl end</Keyword>
		<Keyword>isopeptide bond</Keyword>
	</Entry>
	<Entry>
		<Id>0059</Id>
		<Description>A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue by an isopeptide bond with formation of N-(L-isoaspartyl)glycine and the release of ammonia.</Description>
		<SystematicName>(S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0126</Id>
			<Name>N-(L-isoaspartyl)-glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00135</Id>
			<Name>N-(L-isoaspartyl)glycine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLY</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ASN</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">CG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked carboxyl end</Keyword>
		<Keyword>isopeptide bond</Keyword>
	</Entry>
	<Entry>
		<Id>0060</Id>
		<Description>A protein modification that effectively crosslinks L-aspartic acid and L-cysteine residues via an isopeptide bond to form N-(L-isoaspartyl)-L-cysteine.</Description>
		<SystematicName>(S)-2-amino-4-((R)-1-carboxy-2-sulfanylethyl)amino-4-oxobutanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0216</Id>
			<Name>N-(L-isoaspartyl)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00221</Id>
			<Name>N-(L-isoaspartyl)-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ASP</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">CG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked amino end</Keyword>
		<Keyword>isopeptide bond</Keyword>
	</Entry>
	<Entry>
		<Id>0061</Id>
		<Description>A protein modification that effectively crosslinks an L-asparagine residue and an L-lysine residue by an isopeptide bond with the formation of N6-(L-isoaspartyl)-L-lysine and the release of ammonia.</Description>
		<SystematicName>(S,S)-2-amino-6-[(3-amino-3-carboxypropanoyl)amino]hexanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0294</Id>
			<Name>N6-(L-isoaspartyl)-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00299</Id>
			<Name>N6-(L-isoaspartyl)-L-lysine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ASN</Id>
			</Component>
			<Bond>
				<Atom component="1">NZ</Atom>
				<Atom component="2">CG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>isopeptide bond</Keyword>
	</Entry>
	<Entry>
		<Id>0062</Id>
		<Description>A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue by an isopeptide bond to form N-(L-isoglutamyl)-glycine.</Description>
		<SystematicName>(S)-2-amino-5-(carboxymethyl)amino-5-oxopentanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0360</Id>
			<Name>N-(L-isoglutamyl)-glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00365</Id>
			<Name>N-(L-isoglutamyl)-glycine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLU</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GLY</Id>
				<Terminal>N</Terminal>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">CD</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked amino end</Keyword>
		<Keyword>isopeptide bond</Keyword>
	</Entry>
	<Entry>
		<Id>0063</Id>
		<Description>A protein modification that effectively crosslinks an L-lysine residue and an L-threonine residue by an isopeptide bond to form N6-(L-threonyl)-L-lysine.</Description>
		<SystematicName>(2S)-2-amino-6-([(2S,3R)-2-amino-3-hydroxybutanoyl]amino)hexanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0440</Id>
			<Name>N6-(L-threonyl)-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00924</Id>
			<Name>N6-(L-threonyl)-L-lysine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">THR</Id>
				<Terminal>C</Terminal>
			</Component>
			<Bond>
				<Atom component="1">NZ</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked amino end</Keyword>
		<Keyword>isopeptide bond</Keyword>
	</Entry>
	<Entry>
		<Id>0064</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to N6-lipoyl-L-lysine.</Description>
		<SystematicName>(S)-2-amino-6-[5-((R)-1,2-dithiolan-3-yl)pentanamido]hexanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0118</Id>
			<Name>N6-lipoyl-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00127</Id>
			<Name>N6-lipoyl-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>LPA</Id>
			<Name>lipoic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">LPA</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">NZ</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>lipoamide</Keyword>
		<Keyword>redox-active center</Keyword>
	</Entry>
	<Entry>
		<Id>0065</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to N6-pyridoxal phosphate-L-lysine.</Description>
		<SystematicName>(S)-2-amino-6-[([3-hydroxy-2-methyl-5-phosphonooxymethylpyridin-4-yl]methylidene)amino]hexanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>LLP</Id>
			<Name>2-lysine(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethane)</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0119</Id>
			<Name>N6-pyridoxal phosphate-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00128</Id>
			<Name>N6-pyridoxal phosphate-L-lysine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LLP</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>phosphoprotein</Keyword>
		<Keyword>pyridoxal phosphate</Keyword>
	</Entry>
	<Entry>
		<Id>0066</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal.</Description>
		<SystematicName>(S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>LYR</Id>
			<Name>N~6~-[(2Z,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)nona-2,4,6,8-tetraenyl]lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0120</Id>
			<Name>N6-retinylidene-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00129</Id>
			<Name>N6-retinylidene-L-lysine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYR</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>chromoprotein</Keyword>
		<Keyword>retinal</Keyword>
	</Entry>
	<Entry>
		<Id>0067</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal.</Description>
		<SystematicName>(S)-2-amino-6-[(2E,4E,6E,8E)-3,7-dimethyl-9-(2,6,6-trimethylcyclohex-1-en-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0120</Id>
			<Name>N6-retinylidene-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00129</Id>
			<Name>N6-retinylidene-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>RET</Id>
			<Name>retinal</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">RET</Id>
			</Component>
			<Bond>
				<Atom component="1">NZ</Atom>
				<Atom component="2">C15</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>chromoprotein</Keyword>
		<Keyword>retinal</Keyword>
	</Entry>
	<Entry>
		<Id>0068</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to L-allysine.</Description>
		<SystematicName>(S)-2-amino-6-oxohexanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0121</Id>
			<Name>L-allysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00130</Id>
			<Name>L-allysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DO2</Id>
			<Name>5,5-dihydroxy-6-oxo-L-norleucine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">DO2</Id>
			</Component>
			<Bond>
				<Atom component="1">NZ</Atom>
				<Atom component="2">CE</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
	</Entry>
	<Entry>
		<Id>0069</Id>
		<Description>A protein modification that effectively crosslinks an L-serine residue and an L-lysine residue to release water and form 2-amino-6-(2-amino-2-carboxyethylamino)hexanoic acid.</Description>
		<SystematicName>(2S)-2-amino-6-((2Xi)-2-amino-2-carboxyethylamino)hexanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0123</Id>
			<Name>L-lysinoalanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00132</Id>
			<Name>L-lysinoalanine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">NZ</Atom>
				<Atom component="2">CB</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
	</Entry>
	<Entry>
		<Id>0070</Id>
		<Description>A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycocyanobilin.</Description>
		<SystematicName>(2R,3R)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-2,7,13,17-tetramethyl-1,2,3,19,21,22,24-heptahydrobilin-1,19(21H,22H,24H)-dione</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0131</Id>
			<Name>S-phycocyanobilin-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00140</Id>
			<Name>S-phycocyanobilin-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CYC</Id>
			<Name>phycocyanobilin</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYC</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">CAC</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>chromoprotein</Keyword>
		<Keyword>phycocyanobilin</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0071</Id>
		<Description>A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoerythrobilin.</Description>
		<SystematicName>(2S,3R,16R)-18-ethenyl-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-2,3,15,16-tetrahydrobilin-1,19(21H,22H,24H)-dione</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0132</Id>
			<Name>S-phycoerythrobilin-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00141</Id>
			<Name>S-phycoerythrobilin-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PEB</Id>
			<Name>phycoerythrobilin</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PEB</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">SG</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>chromoprotein</Keyword>
		<Keyword>phycoerythrobilin</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0072</Id>
		<Description>A protein modification that effectively results from forming an adduct between two cysteine residues and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.</Description>
		<SystematicName>[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0134</Id>
			<Name>heme-bis-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00143</Id>
			<Name>heme-bis-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HEM</Id>
			<Name>protoporphyrin IX containing Fe</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">HEM</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">CBB</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="3">CBC</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>chromoprotein</Keyword>
		<Keyword>heme</Keyword>
		<Keyword>iron</Keyword>
		<Keyword>metalloprotein</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0073</Id>
		<Description>A protein modification that effectively converts four L-cysteine residues iron atom to tetrakis-L-cysteinyl iron.</Description>
		<SystematicName>tetrakis(cysteinato)-1kappaS,2kappaS,3kappaS,4kappaS-iron</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0136</Id>
			<Name>tetrakis-L-cysteinyl iron</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00145</Id>
			<Name>tetrakis-L-cysteinyl iron</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">FE</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="5" atom="1">FE</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="5" atom="1">FE</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="5" atom="1">FE</Atom>
			</Bond>
			<Bond>
				<Atom component="4">SG</Atom>
				<Atom component="5" atom="1">FE</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink4</Category>
		<Keyword>iron</Keyword>
		<Keyword>metalloprotein</Keyword>
		<Comment>covered in metal coordination</Comment>
	</Entry>
	<Entry>
		<Id>0074</Id>
		<Description>A protein modification that effectively converts four L-cysteine residues and a four-iron four-sulfur cluster to tetrakis-L-cysteinyl tetrairon tetrasulfide.</Description>
		<SystematicName>tetrakis(cysteinato)-1kappaS,2kappaS,3kappaS,4kappaS-tetra-mu3-sulfido-tetrahedro-tetrairon</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0140</Id>
			<Name>tetrakis-L-cysteinyl tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00149</Id>
			<Name>tetrakis-L-cysteinyl tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SF4</Id>
			<Name>iron/sulfur cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">SF4</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="5">FE1</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="5">FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="5">FE3</Atom>
			</Bond>
			<Bond>
				<Atom component="4">SG</Atom>
				<Atom component="5">FE4</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink4</Category>
		<Keyword>4Fe-4S</Keyword>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0075</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-molybdenum seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide.</Description>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0141</Id>
			<Name>L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00150</Id>
			<Name>L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CFM</Id>
			<Name>Fe-Mo-S cluster</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HCA</Id>
			<Name>3-hydroxy-3-carboxy-adipic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CFM</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">HCA</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="3">FE1</Atom>
			</Bond>
			<Bond>
				<Atom component="2">ND1</Atom>
				<Atom component="3" atom="1">MO1</Atom>
			</Bond>
			<Bond>
				<Atom component="3" atom="1">MO1</Atom>
				<Atom component="4">O5</Atom>
			</Bond>
			<Bond>
				<Atom component="3" atom="1">MO1</Atom>
				<Atom component="4">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
		<Keyword>molybdenum</Keyword>
	</Entry>
	<Entry>
		<Id>0076</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue, an L-histidine residue, homocitric acid and a one-molybdenum seven-iron nine-sulfur cluster to L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide.</Description>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0141</Id>
			<Name>L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00150</Id>
			<Name>L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CFN</Id>
			<Name>Fe(7)-Mo-S(9)-N cluster</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HCA</Id>
			<Name>3-hydroxy-3-carboxy-adipic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CFN</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">HCA</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="3">FE1</Atom>
			</Bond>
			<Bond>
				<Atom component="2">ND1</Atom>
				<Atom component="3" atom="1">MO1</Atom>
			</Bond>
			<Bond>
				<Atom component="3" atom="1">MO1</Atom>
				<Atom component="4">O5</Atom>
			</Bond>
			<Bond>
				<Atom component="3" atom="1">MO1</Atom>
				<Atom component="4">O7</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
		<Keyword>molybdenum</Keyword>
	</Entry>
	<Entry>
		<Id>0077</Id>
		<Description>modification from UniMod and Resid</Description>
		<SystematicName>8-amino-2-(2-amino-2-carboxyethyl)sulfanyl-4,5a,6,9,10,11,11a-heptahydro-4-(phosphoric acid)methyl-2,2,10-trioxo-pteridino[6,7-5,6]pyrano[3,4-4,3][1,2,5]molybdadithiolene</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0142</Id>
			<Name>L-cysteinyl molybdopterin</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00151</Id>
			<Name>L-cysteinyl molybdopterin</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MTQ</Id>
			<Name>(molybdopterin-S,S)-dioxo-thio-molybdenum(VI)</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">MTQ</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">MOM1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>metalloprotein</Keyword>
		<Keyword>molybdenum</Keyword>
		<Keyword>molybdopterin</Keyword>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0078</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S'-(8alpha-FAD)-L-cystine.</Description>
		<SystematicName>(R)-2-amino-3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0143</Id>
			<Name>S-(8alpha-FAD)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00152</Id>
			<Name>S-(8alpha-FAD)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FAD</Id>
			<Name>flavin-adenine dinucleotide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">FAD</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C8M</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>phosphoprotein</Keyword>
		<Keyword>FAD</Keyword>
		<Keyword>flavoprotein</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0079</Id>
		<Description>A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FAD)-L-histidine.</Description>
		<SystematicName>(S)-2-amino-3-(3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0144</Id>
			<Name>3'-(8alpha-FAD)-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00153</Id>
			<Name>3'-(8alpha-FAD)-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FAD</Id>
			<Name>flavin-adenine dinucleotide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">FAD</Id>
			</Component>
			<Bond>
				<Atom component="1">ND1</Atom>
				<Atom component="2">C8M</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>phosphoprotein</Keyword>
		<Keyword>FAD</Keyword>
		<Keyword>flavoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0080</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to O4'-(8alpha-FAD)-L-tyrosine.</Description>
		<SystematicName>(S)-2-amino-3-(4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxyphenyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0145</Id>
			<Name>O4'-(8alpha-FAD)-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00154</Id>
			<Name>O4'-(8alpha-FAD)-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FAD</Id>
			<Name>flavin-adenine dinucleotide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">FAD</Id>
			</Component>
			<Bond>
				<Atom component="1">OH</Atom>
				<Atom component="2">C8M</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>phosphoprotein</Keyword>
		<Keyword>FAD</Keyword>
		<Keyword>flavoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0081</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to an L-2',4',5'-topaquinone.</Description>
		<SystematicName>(S)-2-amino-3-(5-hydroxy-2,5-cyclohexadien-1,4-dion-2-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>TPQ</Id>
			<Name>5-(2-carboxy-2-aminoethyl)-2-hydroxy-1,4-benzoquinone</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0147</Id>
			<Name>L-2',4',5'-topaquinone</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00156</Id>
			<Name>oxidation of tyrosine to L-2',4',5'-topaquinone</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TPQ</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>quinoprotein</Keyword>
		<Keyword>topaquinone</Keyword>
	</Entry>
	<Entry>
		<Id>0082</Id>
		<Description>A protein modification that effectively converts an L-tryptophan residue to an L-tryptophan quinone.</Description>
		<SystematicName>(S)-3-(2-amino-2-carboxyethyl)-6,7-indolinedione</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>TRQ</Id>
			<Name>2-amino-3-(6,7-dioxo-6,7-dihydro-1H-indol-3-yl)-propionic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0148</Id>
			<Name>L-tryptophyl quinone</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00157</Id>
			<Name>oxidation of tryptophan to L-tryptophyl quinone</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TRQ</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>quinoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0083</Id>
		<Description>A protein modification that effectively cross-links two L-tryptophan residues by a carbon-carbon bond to form 4'-(L-tryptophan)-L-tryptophyl quinone.</Description>
		<SystematicName>(S,S)-3-(2-amino-2-carboxyethyl)-4-[3-(2-amino-2-carboxyethyl)-1H-indol-2-yl]-6,7-indolinedione</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0149</Id>
			<Name>4'-(L-tryptophan)-L-tryptophyl quinone</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00158</Id>
			<Name>4'-(L-tryptophan)-L-tryptophyl quinone</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TRP</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TRP</Id>
			</Component>
			<Bond>
				<Atom component="1">CD1</Atom>
				<Atom component="2">CE3</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>quinoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0084</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O-phosphopantetheine-L-serine.</Description>
		<SystematicName>(2R)-4-((2S)-2-amino-2-carboxyethyl)phosphonato-2-hydroxy-N-[3-(2-sulfanylethyl)amino-3-oxopropyl]-3,3-dimethylbutanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0150</Id>
			<Name>O-phosphopantetheine-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00159</Id>
			<Name>O-phosphopantetheine-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PNS</Id>
			<Name>4'-phosphopantetheine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PNS</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">P24</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>phosphopantetheine</Keyword>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0085</Id>
		<Description>A protein modification that effectively converts an L-asparagine residue to O-(N-acetylaminogalactosyl)-L-threonine.</Description>
		<SystematicName>(2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxygalactopyranosyloxy)butanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GTH</Id>
			<Name>3-O-glucopyranosyl-threonine-[2-deoxy-2-acetamido-glucopyranoside]</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0155</Id>
			<Name>O-(N-acetylamino)galactosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00164</Id>
			<Name>O-(N-acetylamino)galactosyl-L-threonine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GTH</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0086</Id>
		<Description>A protein modification that effectively substitutes an L-tyrosine residue with 3',3'',5'-triiodo-L-thyronine.</Description>
		<SystematicName>(S)-2-amino-3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>T3</Id>
			<Name>3,5,3'triiodothyronine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0177</Id>
			<Name>3',3'',5'-triiodo-L-thyronine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00186</Id>
			<Name>3',3'',5'-triiodo-L-thyronine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">T3</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>iodine</Keyword>
	</Entry>
	<Entry>
		<Id>0087</Id>
		<Description>A protein modification that effectively substitutes an L-tyrosine residue with L-thyroxine.</Description>
		<SystematicName>(S)-2-amino-3-[4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodophenyl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>T44</Id>
			<Name>3,5,3',5'tetraiodo-L-thyronine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0178</Id>
			<Name>L-thyroxine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00187</Id>
			<Name>L-thyroxine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">T44</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>iodine</Keyword>
	</Entry>
	<Entry>
		<Id>0088</Id>
		<Description>A protein modification that effectively converts an L-tryptophan residue to L-6'-bromotryptophan.</Description>
		<SystematicName>(S)-2-amino-3-(6-bromo-1H-indol-3-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BTR</Id>
			<Name>6-bromo-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0179</Id>
			<Name>L-6'-bromotryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00188</Id>
			<Name>L-6'-bromotryptophan</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">BTR</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>bromine</Keyword>
	</Entry>
	<Entry>
		<Id>0089</Id>
		<Description>A protein modification that effectively converts a source amino acid residue to dehydroalanine.</Description>
		<SystematicName>2-aminopropenoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DHA</Id>
			<Name>2-amino-acrylic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0181</Id>
			<Name>dehydroalanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01168</Id>
			<Name>dehydroalanine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DHA</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Comment>This modification occurs on SER or TYR</Comment>
	</Entry>
	<Entry>
		<Id>0090</Id>
		<Description>A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine.</Description>
		<SystematicName>(Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CRQ</Id>
			<Name>[2-(3-carbamoyl-1-imino-propyl)-4-(4-hydroxy-benzylidene)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0183</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00191</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CRQ</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Comment>CRQ has two modifications: RESID:AA0183 and RESID:AA0189</Comment>
	</Entry>
	<Entry>
		<Id>0091</Id>
		<Description>A protein modification that effectively crosslinks an L-glutamine residue and a glycine residue to form 2-imino-glutamine 5-imidazolinone glycine.</Description>
		<SystematicName>2-(3-carbamoyl-1-imino-propyl)-1-carboxymethyl-1-imidazolin-5-one</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CRQ</Id>
			<Name>[2-(3-carbamoyl-1-imino-propyl)-4-(4-hydroxy-benzylidene)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0189</Id>
			<Name>2-imino-glutamine 5-imidazolinone glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00197</Id>
			<Name>2-imino-glutamine 5-imidazolinone glycine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CRQ</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Comment>CRQ has two modifications: RESID:AA0183 and RESID:AA0189</Comment>
		<Keyword>chromoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0092</Id>
		<Description>A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine.</Description>
		<SystematicName>(Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CRO</Id>
			<Name>{2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0183</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00191</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CRO</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Comment>CRO has two modifications: RESID:AA0183 and RESID:AA0184</Comment>
	</Entry>
	<Entry>
		<Id>0093</Id>
		<Description>A protein modification that effectively crosslinks an L-serine residue and a glycine residue to form L-serine 5-imidazolinone glycine.</Description>
		<SystematicName>2-[(R)-1-amino-2-hydroxyethyl]-1-carboxymethyl-1-imidazolin-5-one</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CRO</Id>
			<Name>{2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0184</Id>
			<Name>L-serine 5-imidazolinone glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00192</Id>
			<Name>L-serine 5-imidazolinone glycine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CRO</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Comment>CRO has two modifications: RESID:AA0183 and RESID:AA0184</Comment>
		<Keyword>chromoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0094</Id>
		<Description>A protein modification that effectively converts a source amino acid residue to L-oxoalanine.</Description>
		<SystematicName>(S)-2-amino-3-oxopropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FGL</Id>
			<Name>2-aminopropanedioic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0185</Id>
			<Name>L-3-oxoalanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01169</Id>
			<Name>L-3-oxoalanine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">FGL</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Comment>This modification occurs on SER or CYS</Comment>
	</Entry>
	<Entry>
		<Id>0095</Id>
		<Description>A protein modification that effectively converts a source amino acid residue to D-alanine.</Description>
		<SystematicName>(R)-2-aminopropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DAL</Id>
			<Name>D-alanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0191</Id>
			<Name>D-alanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00862</Id>
			<Name>D-alanine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DAL</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>D-amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0098</Id>
		<Description>A protein modification that effectively converts an L-isoleucine residue to a D-allo-isoleucine.</Description>
		<SystematicName>(2R,3S)-2-amino-3-methylpentanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DIL</Id>
			<Name>D-isoleucine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0192</Id>
			<Name>D-allo-isoleucine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00199</Id>
			<Name>D-allo-isoleucine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DIL</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>D-amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0099</Id>
		<Description>A protein modification that effectively converts an L-asparagine residue to D-asparagine.</Description>
		<SystematicName>(R)-2-amino-4-butanediamic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DSG</Id>
			<Name>D-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0196</Id>
			<Name>D-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00203</Id>
			<Name>D-asparagine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DSG</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>D-amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0100</Id>
		<Description>A protein modification that effectively converts an L-tryptophan residue to D-tryptophan.</Description>
		<SystematicName>(R)-2-amino-3-(1H-indol-3-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DTR</Id>
			<Name>D-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0198</Id>
			<Name>D-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00205</Id>
			<Name>D-tryptophan</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DTR</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>D-amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0101</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to D-allo-threonine.</Description>
		<SystematicName>(2R,3R)-2-amino-3-hydroxybutanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DTH</Id>
			<Name>D-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0199</Id>
			<Name>D-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00863</Id>
			<Name>D-allo-threonine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DTH</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>D-amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0102</Id>
		<Description>A protein modification that effectively converts an L-valine residue to D-valine.</Description>
		<SystematicName>(R)-2-amino-3-methylbutanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DVA</Id>
			<Name>D-valine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0200</Id>
			<Name>D-valine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00705</Id>
			<Name>D-valine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DVA</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>D-amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0103</Id>
		<Description>A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid.</Description>
		<SystematicName>(R)-2-amino-2-carboxyethanesulfenic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CSO</Id>
			<Name>S-hydroxycysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0205</Id>
			<Name>L-cysteine sulfenic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00210</Id>
			<Name>L-cysteine sulfenic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CSO</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0104</Id>
		<Description>A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid.</Description>
		<SystematicName>(R)-2-amino-2-carboxyethanesulfenic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CSX</Id>
			<Name>S-oxy cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0205</Id>
			<Name>L-cysteine sulfenic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00210</Id>
			<Name>L-cysteine sulfenic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CSX</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0105</Id>
		<Description>A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a thioester bond to form S-glycyl-L-cysteine.</Description>
		<SystematicName>(2R)-2-amino-3-[(aminoacetyl)sulfanyl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0206</Id>
			<Name>S-glycyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00211</Id>
			<Name>S-glycyl-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GLY</Id>
				<Terminal>C</Terminal>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked carboxyl end</Keyword>
		<Keyword>thioester bond</Keyword>
	</Entry>
	<Entry>
		<Id>0106</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-4-hydroxycinnamyl-L-cysteine.</Description>
		<SystematicName>(S,E)-2-amino-3-[3-(4-hydroxyphenyl)propenoylsulfanyl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0207</Id>
			<Name>S-4-hydroxycinnamyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00212</Id>
			<Name>S-4-hydroxycinnamyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HC4</Id>
			<Name>4'-hydroxycinnamic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">HC4</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>chromoprotein</Keyword>
		<Keyword>hydroxylation</Keyword>
		<Keyword>photoreceptor</Keyword>
		<Keyword>thioester bond</Keyword>
	</Entry>
	<Entry>
		<Id>0107</Id>
		<Description>A protein modification that effectively converts an L-arginine residue to a 4-hydroxy-L-arginine.</Description>
		<SystematicName>(2S,4Xi)-2-amino-5-[(diaminomethylidene)amino]-4-hydroxypentanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ARO</Id>
			<Name>C-gamma-hydroxy arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0215</Id>
			<Name>4-hydroxy-L-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00220</Id>
			<Name>4-hydroxy-L-arginine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ARO</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>hydroxylation</Keyword>
	</Entry>
	<Entry>
		<Id>0108</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-(6-FMN)-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-[6-riboflavin 5'-dihydrogen phosphate]sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0220</Id>
			<Name>S-(6-FMN)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00225</Id>
			<Name>S-(6-FMN)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FMN</Id>
			<Name>flavin mononucleotide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">FMN</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C6</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>phosphoprotein</Keyword>
		<Keyword>flavoprotein</Keyword>
		<Keyword>FMN</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0109</Id>
		<Description>A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FAD)-L-histidine.</Description>
		<SystematicName>(S)-2-amino-3-(1-[8alpha riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0221</Id>
			<Name>1'-(8alpha-FAD)-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00226</Id>
			<Name>1'-(8alpha-FAD)-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FAD</Id>
			<Name>flavin-adenine dinucleotide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">FAD</Id>
			</Component>
			<Bond>
				<Atom component="1">NE2</Atom>
				<Atom component="2">C8M</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>phosphoprotein</Keyword>
		<Keyword>FAD</Keyword>
		<Keyword>flavoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0110</Id>
		<Description>A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoguanosine through a phosphoramide ester bond to form N6-(phospho-5'-guanosine)-L-lysine.</Description>
		<SystematicName>(S)-2-amino-6-(5'-guanosine phosphonamino)hexanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GPL</Id>
			<Name>lysine guanosine-5'-monophosphate</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0228</Id>
			<Name>N6-(phospho-5'-guanosine)-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00233</Id>
			<Name>N6-(phospho-5'-guanosine)-L-lysine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GPL</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0111</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-nitrosyl-L-cysteine.</Description>
		<SystematicName>(2R)-2-amino-3-nitrososulfanyl-propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SNC</Id>
			<Name>S-nitroso-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0230</Id>
			<Name>S-nitrosyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00235</Id>
			<Name>S-nitrosyl-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SNC</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0112</Id>
		<Description>A protein modification that effectively cross-links an L-lysine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 5'-(N6-L-lysine)-L-topaquinone.</Description>
		<SystematicName>1-[(S)-5-amino-5-carboxypentyl]amino-2-[(S)-2-amino-2-carboxyethyl]-2,6-cyclohexadien-4,5-dione</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0233</Id>
			<Name>2'-(L-lys-N6-yl)-L-4',5'-topaquinone</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00238</Id>
			<Name>5'-(N6-L-lysine)-L-topaquinone</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>TPQ</Id>
			<Name>5-(2-carboxy-2-aminoethyl)-2-hydroxy-1,4-benzoquinone</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TPQ</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">C2</Atom>
				<Atom component="2">NZ</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>quinoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0113</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-methyl-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-(methylsulfanyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SMC</Id>
			<Name>S-methylcysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0234</Id>
			<Name>S-methyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00239</Id>
			<Name>S-methyl-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SMC</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0114</Id>
		<Description>A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3-(3'-L-histidyl)-L-tyrosine.</Description>
		<SystematicName>(2S,3R)-2-amino-3-(5-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)-3-(4-hydroxyphenyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0250</Id>
			<Name>3-(3'-L-histidyl)-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00255</Id>
			<Name>3-(3'-L-histidyl)-L-tyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">ND1</Atom>
				<Atom component="2">CB</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
	</Entry>
	<Entry>
		<Id>0115</Id>
		<Description>A protein modification that dioxygenates an L-methionine residue to L-methionine sulfone.</Description>
		<SystematicName>(S)-2-amino-4-(methylsulfonyl)butanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>OMT</Id>
			<Name>S-dioxymethionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0251</Id>
			<Name>L-methionine sulfone</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00256</Id>
			<Name>L-methionine sulfone</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">OMT</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0116</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to dipyrrolylmethanemethyl-L-cysteine.</Description>
		<SystematicName>3-[5-[4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methyl-4-(2-carboxy)ethyl-3-carboxymethyl-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0252</Id>
			<Name>dipyrrolylmethanemethyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00257</Id>
			<Name>dipyrrolylmethanemethyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DPM</Id>
			<Name>3-{2-[4-(2-carboxy-ethyl)-3-carboxymethyl-5H-pyrrol-2-ylmethyl]-4-carboxymethly-5-methyl-2H-pyrrol-3-yl}-propionic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">DPM</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">CHA</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0117</Id>
		<Description>A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoviolobilin.</Description>
		<SystematicName>(4S)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-8,12-bis(2-carboxyethyl)-18-ethyl-4,5-dihydro-2,7,13,17-tetramethyl-(21H,22H,24H)-biladiene-bc-1,19-dione</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0258</Id>
			<Name>S-phycoviolobilin-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00263</Id>
			<Name>S-phycoviolobilin-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PVN</Id>
			<Name>phycoviolobilin</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PVN</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C31</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>chromoprotein</Keyword>
		<Keyword>phycoviolobilin</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0118</Id>
		<Description>A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycourobilin.</Description>
		<SystematicName>3,18-bis(1-[(R)-2-amino-2-carboxyethyl]sulfanylethyl)-8,12-bis(2-carboxyethyl)-2,7,13,17-tetramethyl-4,5,15,16-tetrahydro-(21H,22H,24H)-bilene-b-1,19(4H,16H)-dione</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0260</Id>
			<Name>phycourobilin-bis-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00265</Id>
			<Name>phycourobilin-bis-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PUB</Id>
			<Name>phycourobilin</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">PUB</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="3">CAA,CAD</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="3">CAA,CAD</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>chromoprotein</Keyword>
		<Keyword>phycourobilin</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0119</Id>
		<Description>A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid.</Description>
		<SystematicName>(R)-2-amino-2-carboxyethanesulfinic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CSD</Id>
			<Name>3-sulfinoalanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0262</Id>
			<Name>(R)-2-amino-2-carboxyethanesulfinic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00267</Id>
			<Name>cysteine-S,S-dioxide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CSD</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0120</Id>
		<Description>A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid.</Description>
		<SystematicName>(R)-2-amino-2-carboxyethanesulfinic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CSW</Id>
			<Name>cysteine-S-dioxide</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0262</Id>
			<Name>(R)-2-amino-2-carboxyethanesulfinic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00267</Id>
			<Name>cysteine-S,S-dioxide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CSW</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0121</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O-(sn-1-glycerophosphoryl)-L-serine.</Description>
		<SystematicName>(2S)-2-amino-3-[(2Xi)-2,3-dihydroxypropyl]phosphonoxypropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0264</Id>
			<Name>O-(sn-1-glycerophosphoryl)-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00269</Id>
			<Name>O-(sn-1-glycerophosphoryl)-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>OPE</Id>
			<Name>phosphoric acid mono-(2-amino-ethlyl) ester</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">OPE</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">CB</Atom>
				<Atom component="2">O3</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0122</Id>
		<Description>A protein modification that effectively converts a glycine residue to an internal 1-thioglycine.</Description>
		<SystematicName>aminoethanethioic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GL3</Id>
			<Name>thioglycin</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0265</Id>
			<Name>1-thioglycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00270</Id>
			<Name>1-thioglycine (internal)</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GL3</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Comment>There are two entries in PSI-MOD MOD:00270 and MOD:01623, corresponding to internal and terminal.</Comment>
	</Entry>
	<Entry>
		<Id>0123</Id>
		<Description>A protein modification that effectively results from forming an adduct between two cysteine residues, the C-3' of a tyrosine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.</Description>
		<SystematicName>(10S,11S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-10-(2-hydroxy-5-[(S)-2-amino-2-carboxy]ethylphenyl)-3,8,13,17-tetramethyl-21H,23H-10,11-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0266</Id>
			<Name>heme P460-bis-L-cysteine-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00271</Id>
			<Name>heme P460-bis-L-cysteine-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HEC</Id>
			<Name>heme C</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">HEC</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="4">CAB</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="4">CAC</Atom>
			</Bond>
			<Bond>
				<Atom component="3">CE1,CE2</Atom>
				<Atom component="4">C4B</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink3</Category>
		<Keyword>chromoprotein</Keyword>
		<Keyword>heme</Keyword>
		<Keyword>iron</Keyword>
		<Keyword>metalloprotein</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0124</Id>
		<Description>A protein modification that effectively results from forming an adduct between two cysteine residues, a lysine residue, and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.</Description>
		<SystematicName>(19S,20S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-20-([(S)-5-amino-5-carboxypentyl]amino)-3,8,13,17-tetramethyl-21H,23H-19,20-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0271</Id>
			<Name>heme P460-bis-L-cysteine-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00276</Id>
			<Name>heme P460-bis-L-cysteine-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HEC</Id>
			<Name>heme C</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">HEC</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="4">CAB,CAC</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="4">CAC,CAB</Atom>
			</Bond>
			<Bond>
				<Atom component="3">NZ</Atom>
				<Atom component="4">CHA</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink3</Category>
		<Keyword>chromoprotein</Keyword>
		<Keyword>heme</Keyword>
		<Keyword>iron</Keyword>
		<Keyword>metalloprotein</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0125</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to L-cysteine persulfide.</Description>
		<SystematicName>(R)-2-amino-3-disulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CSS</Id>
			<Name>S-mercapto-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0269</Id>
			<Name>L-cysteine persulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00274</Id>
			<Name>L-cysteine persulfide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CSS</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0126</Id>
		<Description>A protein modification that effectively cross-links an L-histidine residue and an L-tyrosine residue by a carbon-nitrogen bond to form 3'-(1'-L-histidyl)-L-tyrosine.</Description>
		<SystematicName>(2S)-2-amino-3-[1-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenyl)-1H-imidazol-4-yl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0270</Id>
			<Name>3'-(1'-L-histidyl)-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00275</Id>
			<Name>3'-(1'-L-histidyl)-L-tyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">NE2</Atom>
				<Atom component="2">CE1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
	</Entry>
	<Entry>
		<Id>0127</Id>
		<Description>A protein modification that effectively converts an L-glutamine residue to 2-methyl-L-glutamine.</Description>
		<SystematicName>(S)-2-amino-2-methylpentanediamic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MGN</Id>
			<Name>2-methyl-glutamine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0273</Id>
			<Name>2-methyl-L-glutamine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00278</Id>
			<Name>2-methyl-L-glutamine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MGN</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0128</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-selenyl-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-(selanylsulfanyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CSZ</Id>
			<Name>S-selanyl cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0277</Id>
			<Name>S-selanyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00282</Id>
			<Name>S-selenyl-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CSZ</Id>
			</Component>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>modified residue</Category>
		<Keyword>selenium</Keyword>
	</Entry>
	<Entry>
		<Id>0129</Id>
		<Description>A protein modification that effectively results from forming an adduct between an aspartic acid residue, a glutamic acid residue, a methionine residue (forming a sulfonium ether), and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.</Description>
		<SystematicName>(19S,20S)-[7,12-bis((S)-1-[((R)-2-amino-2-carboxy)ethylsulfanyl]ethyl)-20-([(S)-5-amino-5-carboxypentyl]amino)-3,8,13,17-tetramethyl-21H,23H-19,20-dihydroporphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0280</Id>
			<Name>dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00285</Id>
			<Name>dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HEM</Id>
			<Name>protoporphyrin IX containing Fe</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ASP</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GLU</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">MET</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">HEM</Id>
			</Component>
			<Bond>
				<Atom component="1">OD2</Atom>
				<Atom component="4">CMD</Atom>
			</Bond>
			<Bond>
				<Atom component="2">OE2</Atom>
				<Atom component="4">CMB</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SD</Atom>
				<Atom component="4">CBB</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink3</Category>
		<Keyword>chromoprotein</Keyword>
		<Keyword>heme</Keyword>
		<Keyword>hydroxylation</Keyword>
		<Keyword>iron</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0130</Id>
		<Description>A protein modification that effectively doubly cross-links an L-glutamic acid residue and an L-tyrosine residue with a carbon-carbon bond and a carbon-nitrogen bond to form pyrroloquinoline quinone.</Description>
		<SystematicName>4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-5,6]quinoline-2,7,9-tricarboxylic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0283</Id>
			<Name>pyrroloquinoline quinone</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00288</Id>
			<Name>pyrroloquinoline quinone</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PQQ</Id>
			<Name>pyrroloquinoline quinone</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLU</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">PQQ</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">CG</Atom>
				<Atom component="3">N1</Atom>
			</Bond>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="2">OH</Atom>
				<Atom component="3">C8</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>quinoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0131</Id>
		<Description>A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide.</Description>
		<SystematicName>tetra-mu3-sulfidotris(S-cysteinyliron)(N1'-histidinoiron)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0284</Id>
			<Name>tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00289</Id>
			<Name>tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SF4</Id>
			<Name>iron/sulfur cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">SF4</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="4">NE2</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink4</Category>
		<Keyword>4Fe-4S</Keyword>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0132</Id>
		<Description>A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide.</Description>
		<SystematicName>tetra-mu3-sulfidotris(S-cysteinyliron)(N3'-histidinoiron)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0285</Id>
			<Name>tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00290</Id>
			<Name>tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SF4</Id>
			<Name>iron/sulfur cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">SF4</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="4">ND1</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink4</Category>
		<Keyword>4Fe-4S</Keyword>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0133</Id>
		<Description>A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-aspartato tetrairon tetrasulfide.</Description>
		<SystematicName>tetra-mu3-sulfidotris(S-cysteinyliron)(O4-aspartatoiron)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0286</Id>
			<Name>tris-L-cysteinyl L-aspartato tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00291</Id>
			<Name>tris-L-cysteinyl L-aspartato tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SF4</Id>
			<Name>iron/sulfur cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">ASP</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">SF4</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="4">OD2</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink4</Category>
		<Keyword>4Fe-4S</Keyword>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0134</Id>
		<Description>A protein modification that effectively converts three L-cysteine residues, an L-serine residue and a four-iron four-sulfur cluster to tris-L-cysteinyl L-serinyl tetrairon tetrasulfide.</Description>
		<SystematicName>tetra-mu3-sulfidotris(S-cysteinyliron)(O3-serinyliron)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0288</Id>
			<Name>tris-L-cysteinyl L-serinyl tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00293</Id>
			<Name>tris-L-cysteinyl L-serinyl tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SF4</Id>
			<Name>iron/sulfur cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">SF4</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="4">OG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>crosslink4</Category>
		<Keyword>4Fe-4S</Keyword>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0135</Id>
		<Description>A protein modification that effectively converts two L-cysteine residues, an L-histidine residues, an L-serine residue and a four-iron four-sulfur cluster to bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide.</Description>
		<SystematicName>tetra-mu3-sulfidobis(S-cysteinyliron)(N3'-histidinoiron)(O3-serinyliron)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0289</Id>
			<Name>bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00294</Id>
			<Name>bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SF4</Id>
			<Name>iron/sulfur cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">SF4</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="3">ND1</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="4">OG</Atom>
				<Atom component="5">FE1,FE2,FE3,FE4</Atom>
			</Bond>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>crosslink4</Category>
		<Keyword>4Fe-4S</Keyword>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0136</Id>
		<Description>A protein modification that effectively converts seven L-histidinine residues and a four-copper one-sulfur one-hydroxide cluster to heptakis-L-histidino tetracopper mu4-sulfide hydroxide.</Description>
		<SystematicName>mu4-sulfido bis(bis-N1'-histidino copper)(N1'-histidino-N3'-histidino copper)(N3'-histidino hydroxide copper)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0298</Id>
			<Name>heptakis-L-histidino tetracopper mu4-sulfide hydroxide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00303</Id>
			<Name>heptakis-L-histidino tetracopper mu4-sulfide hydroxide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CUZ</Id>
			<Name>(mu-4-sulfido)-tetra-nuclear copper ion</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="6">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="7">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="8">
				<Id source="PDBCC">CUZ</Id>
			</Component>
			<Bond>
				<Atom component="1">NE2</Atom>
				<Atom component="8" atom="1">CU1,CU2,CU3,CU4</Atom>
			</Bond>
			<Bond>
				<Atom component="2">NE2</Atom>
				<Atom component="8" atom="1">CU1,CU2,CU3,CU4</Atom>
			</Bond>
			<Bond>
				<Atom component="3">NE2</Atom>
				<Atom component="8" atom="2">CU1,CU2,CU3,CU4</Atom>
			</Bond>
			<Bond>
				<Atom component="4">NE2</Atom>
				<Atom component="8" atom="2">CU1,CU2,CU3,CU4</Atom>
			</Bond>
			<Bond>
				<Atom component="5">NE2</Atom>
				<Atom component="8" atom="3">CU1,CU2,CU3,CU4</Atom>
			</Bond>
			<Bond>
				<Atom component="6">ND1</Atom>
				<Atom component="8" atom="3">CU1,CU2,CU3,CU4</Atom>
			</Bond>
			<Bond>
				<Atom component="7">ND1</Atom>
				<Atom component="8">CU1,CU2,CU3,CU4</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink7</Category>
		<Keyword>copper</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0137</Id>
		<Description>A protein modification that effectively converts six L-cysteine residues, an L-serine residue and a eight-iron seven-sulfur cluster to hexakis-L-cysteinyl L-serinyl octairon heptasulfide.</Description>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0300</Id>
			<Name>hexakis-L-cysteinyl L-serinyl octairon heptasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00305</Id>
			<Name>hexakis-L-cysteinyl L-serinyl octairon heptasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CLF</Id>
			<Name>Fe(8)-S(7) cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="6">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="7">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="8">
				<Id source="PDBCC">CLF</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="8">FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="8">FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="8">FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8</Atom>
			</Bond>
			<Bond>
				<Atom component="4">SG</Atom>
				<Atom component="8">FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8</Atom>
			</Bond>
			<Bond>
				<Atom component="5">SG</Atom>
				<Atom component="8">FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8</Atom>
			</Bond>
			<Bond>
				<Atom component="6">SG</Atom>
				<Atom component="8">FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8</Atom>
			</Bond>
			<Bond>
				<Atom component="7">OG</Atom>
				<Atom component="8">FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink7</Category>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0138</Id>
		<Description>A protein modification that effectively cyclizes an L-asparagine residue to form a carboxyl-terminal L-aspartimide.</Description>
		<SystematicName>(S)-3-amino-2,5-pyrrolidinedione</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SNN</Id>
			<Name>L-3-aminosuccinimide</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0302</Id>
			<Name>L-aspartimide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00307</Id>
			<Name>L-aspartimide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SNN</Id>
				<Terminal>C</Terminal>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>blocked carboxyl end</Keyword>
		<Keyword>protein splicing</Keyword>
	</Entry>
	<Entry>
		<Id>0139</Id>
		<Description>A protein modification that effectively converts five L-cysteine residues, an L-histidine residue and a one-nickel four-iron five-sulfur cluster to pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide.</Description>
		<SystematicName>mu-1:2kappaS-sulfido-mu3-1:3:5kappaS-sulfido-mu3-2:3:4kappaS-sulfido-mu3-2:4:5kappaS-sulfido-mu3-3:4:5kappaS-sulfido-N1'-histidino-S-cysteinyl-1-iron-S-cysteinyl-2-nickel-3,4,5-tris-(S-cysteinyl iron)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0310</Id>
			<Name>pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00315</Id>
			<Name>pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NFS</Id>
			<Name>Fe(4)-Ni(1)-S(5) cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="6">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="7">
				<Id source="PDBCC">NFS</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="7" atom="1">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="7">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="7">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="4">SG</Atom>
				<Atom component="7">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="5">SG</Atom>
				<Atom component="7">NI1</Atom>
			</Bond>
			<Bond>
				<Atom component="6">NE2</Atom>
				<Atom component="7" atom="1">FE1,FE2,FE3,FE4</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink6</Category>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
		<Keyword>Ni-4Fe-5S</Keyword>
		<Keyword>nickel</Keyword>
	</Entry>
	<Entry>
		<Id>0140</Id>
		<Description>A protein modification that effectively converts an L-asparagine residue to N4,N4-dimethyl-L-asparagine.</Description>
		<SystematicName>(S)-2-amino-N4,N4-dimethylbutanediamic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DMH</Id>
			<Name>N4,N4-dimethyl-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0311</Id>
			<Name>N4,N4-dimethyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00316</Id>
			<Name>N4,N4-dimethyl-L-asparagine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DMH</Id>
			</Component>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0141</Id>
		<Description>A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 4'-(S-L-cysteinyl)-L-tryptophyl quinone.</Description>
		<SystematicName>(S)-3-(2-amino-2-carboxyethyl)-4-[(R)-2-amino-2-carboxyethyl]sulfanyl-6,7-indolinedione</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0313</Id>
			<Name>4'-(S-L-cysteinyl)-L-tryptophyl quinone</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00318</Id>
			<Name>4'-(S-L-cysteinyl)-L-tryptophyl quinone</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TRP</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">SG</Atom>
				<Atom component="2">CE3</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>quinoprotein</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0142</Id>
		<Description>A protein modification that effectively cross-links an L-cysteine residue and an L-aspartic acid residue by a thioether bond to form 2-(S-L-cysteinyl)-L-aspartic acid.</Description>
		<SystematicName>(2S,3S)-2-amino-3-[(R)-2-amino-2-carboxyethyl]sulfanylbutanedioic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0314</Id>
			<Name>3-(S-L-cysteinyl)-L-aspartic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00319</Id>
			<Name>3-(S-L-cysteinyl)-L-aspartic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ASP</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">CB</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>lanthionine</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0143</Id>
		<Description>A protein modification that effectively cross-links an L-cysteine residue and an L-glutamic acid residue by a thioether bond to form 4-(S-L-cysteinyl)-L-glutamic acid.</Description>
		<SystematicName>(2S,4S)-2-amino-4-[(R)-2-amino-2-carboxyethyl]sulfanylpentanedioic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0315</Id>
			<Name>4-(S-L-cysteinyl)-L-glutamic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00320</Id>
			<Name>4-(S-L-cysteinyl)-L-glutamic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GLU</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">CG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0144</Id>
		<Description>A protein modification that effectively converts an L-histidine residue to tele-methyl-L-histidine.</Description>
		<SystematicName>(S)-2-amino-3-(1-methyl-1H-imidazol-4-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HIC</Id>
			<Name>4-methyl-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0317</Id>
			<Name>1'-methyl-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00322</Id>
			<Name>1'-methyl-L-histidine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HIC</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0145</Id>
		<Description>A protein modification that effectively converts an L-serine residue to L-serinyl molybdenum bis(molybdopterin guanine dinucleotide).</Description>
		<SystematicName>bis[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with guanosine)methyl-6-oxo-3,4-disulfanyl-pteridino[6,7-5,6]pyranoato-S3,S4]-O3-serinyl-molybdenum oxide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0319</Id>
			<Name>L-serinyl molybdenum bis(molybdopterin guanine dinucleotide)</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00324</Id>
			<Name>L-serinyl molybdenum bis(molybdopterin guanine dinucleotide)</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MGD</Id>
			<Name>molybdopterin guanosine dinucleotide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">MGD</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">MGD</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">6MO</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="4">MO</Atom>
			</Bond>
			<Bond>
				<Atom component="2">S12,S13</Atom>
				<Atom component="4">MO</Atom>
			</Bond>
			<Bond>
				<Atom component="3">S12,S13</Atom>
				<Atom component="4">MO</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>metalloprotein</Keyword>
		<Keyword>molybdenum</Keyword>
		<Keyword>molybdopterin</Keyword>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0146</Id>
		<Description>A protein modification that effectively converts an L-tryptophan residue to a 3-hydroxy-L-tryptophan.</Description>
		<SystematicName>(2S,3S)-2-amino-3-hydroxy-3-(1H-indol-3-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HTR</Id>
			<Name>beta-hydroxytryptophane</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0322</Id>
			<Name>3-hydroxy-L-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00327</Id>
			<Name>3-hydroxy-L-tryptophan</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HTR</Id>
			</Component>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>modified residue</Category>
		<Keyword>hydroxylation</Keyword>
	</Entry>
	<Entry>
		<Id>0147</Id>
		<Description>A protein modification that effectively converts four L-cysteine residues and a three-iron four-sulfur cluster to tetrakis-L-cysteinyl triiron tetrasulfide.</Description>
		<SystematicName>di-mu-1:2kappaS-sulfido di-mu-2:3kappaS-sulfido iron bis(bis-S-cysteinyliron)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0326</Id>
			<Name>tetrakis-L-cysteinyl triiron tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00331</Id>
			<Name>tetrakis-L-cysteinyl triiron tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>F3S</Id>
			<Name>Fe3-S4 cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">F3S</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="5" atom="1">FE1,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="5" atom="1">FE1,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="5" atom="2">FE1,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="4">SG</Atom>
				<Atom component="5" atom="2">FE1,FE3,FE4</Atom>
			</Bond>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>crosslink4</Category>
		<Keyword>3Fe-4S</Keyword>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0148</Id>
		<Description>A protein modification that effectively results from forming an adduct between the tele nitrogen of a histidine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.</Description>
		<SystematicName>(S)-[7-ethenyl-12-[1-((2-amino-2-carboxyethyl)-1H-imidazol-1-yl)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0329</Id>
			<Name>1'-heme-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00334</Id>
			<Name>1'-heme-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HEM</Id>
			<Name>protoporphyrin IX containg Fe</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">HEM</Id>
			</Component>
			<Bond>
				<Atom component="1">NE2</Atom>
				<Atom component="2">CAB</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Comment>NE2 is much closer to FE than to CBB.</Comment>
		<Keyword>chromoprotein</Keyword>
		<Keyword>heme</Keyword>
		<Keyword>iron</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0149</Id>
		<Description>A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 3-methyl-L-lanthionine sulfoxide.</Description>
		<SystematicName>(2S,3S,SXi)-2-amino-3-([(R)-2-amino-2-carboxyethyl]sulfinyl)butanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0330</Id>
			<Name>3-methyl-L-lanthionine sulfoxide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00335</Id>
			<Name>3-methyl-L-lanthionine sulfoxide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">THR</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">SG</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
	</Entry>
	<Entry>
		<Id>0150</Id>
		<Description>A protein modification that effectively converts three L-cysteine residues, an L-aspartic acid residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-aspartato diiron disulfide.</Description>
		<SystematicName>di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-O4-aspartatoiron)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0331</Id>
			<Name>tris-L-cysteinyl L-aspartato diiron disulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00336</Id>
			<Name>tris-L-cysteinyl L-aspartato diiron disulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FES</Id>
			<Name>Fe2/S2 (inorganic) cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">ASP</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">FES</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="5" atom="1">FE1,FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="5" atom="1">FE1,FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="5" atom="2">FE1,FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="4">OD2</Atom>
				<Atom component="5" atom="1">FE1,FE2</Atom>
			</Bond>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>crosslink4</Category>
		<Keyword>2Fe-2S</Keyword>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0151</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to L-cysteinyl hydrogenase diiron subcluster.</Description>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0334</Id>
			<Name>L-cysteinyl hydrogenase diiron subcluster</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00339</Id>
			<Name>L-cysteinyl hydrogenase diiron subcluster</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HC1</Id>
			<Name>2 iron/2 sulfur/5 carbonyl/2 water inorganic cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">HC1</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">FE1,FE2</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0152</Id>
		<Description>A protein modification that effectively converts an L-isoleucine residue to N-methyl-L-isoleucine.</Description>
		<SystematicName>(2S,3S)-2-methylamino-3-methylpentanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>IML</Id>
			<Name>N-methyl-isoleucine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0336</Id>
			<Name>N-methyl-L-isoleucine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00341</Id>
			<Name>N-methyl-L-isoleucine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">IML</Id>
			</Component>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0153</Id>
		<Description>A protein modification that effectively converts an L-leucine residue to N-methyl-L-leucine.</Description>
		<SystematicName>(S)-2-methylamino-4-methylpentanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MLE</Id>
			<Name>N-methylleucine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0337</Id>
			<Name>N-methyl-L-leucine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00342</Id>
			<Name>N-methyl-L-leucine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MLE</Id>
			</Component>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0154</Id>
		<Description>A protein modification that effectively converts a glycine residue to N-palmitoylglycine.</Description>
		<SystematicName>(hexadecanoylamino)ethanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0339</Id>
			<Name>N-palmitoyl-glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00344</Id>
			<Name>N-palmitoylglycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>140</Id>
			<Name>N-palmitoylglycine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLY</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">140</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">N</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>blocked amino end</Keyword>
		<Keyword>lipoprotein</Keyword>
		<Keyword>palmitoylation</Keyword>
	</Entry>
	<Entry>
		<Id>0155</Id>
		<Description>A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-L-phenylalanine.</Description>
		<SystematicName>(R)-2-amino-2-[(R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylethanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0340</Id>
			<Name>2-(S-L-cysteinyl)-L-phenylalanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00345</Id>
			<Name>2-(S-L-cysteinyl)-L-phenylalanine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PHE</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">CA</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0156</Id>
		<Description>A protein modification that effectively cross-links an L-cysteine residue and an L-phenylalanine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-phenylalanine.</Description>
		<SystematicName>(S)-2-amino-2-[(R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylethanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0341</Id>
			<Name>2-(S-L-cysteinyl)-D-phenylalanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00346</Id>
			<Name>2-(S-L-cysteinyl)-D-phenylalanine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PHE</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">CA</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>D-amino acid</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0157</Id>
		<Description>A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form 2-(S-L-cysteinyl)-D-allo-threonine.</Description>
		<SystematicName>(2S,3R)-2-amino-2-[(R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0342</Id>
			<Name>2-(S-L-cysteinyl)-D-allo-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00347</Id>
			<Name>2-(S-L-cysteinyl)-D-allo-threonine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">THR</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">CA</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>D-amino acid</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0158</Id>
		<Description>A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form 4-amino-3-isothiazolidinone-L-serine.</Description>
		<SystematicName>(4R)-2-((S)-1-carboxy-2-hydroxyethyl)-4-amino-3(2H)-isothiazolidinone</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0344</Id>
			<Name>4-amino-3-isothiazolidinone-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00349</Id>
			<Name>4-amino-3-isothiazolidinone-L-serine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">N</Atom>
			</Bond>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
	</Entry>
	<Entry>
		<Id>0159</Id>
		<Description>A protein modification that effectively cross-links an L-tryptophan residue with an L-tyrosine residue by a carbon-carbon bond, and cross-links the L-tyrosine residue to an L-methionine residue by a thioether bond to form S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium.</Description>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0348</Id>
			<Name>S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00353</Id>
			<Name>S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MET</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TRP</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">SD</Atom>
				<Atom component="3">CE1,CE2</Atom>
			</Bond>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="2">CH2</Atom>
				<Atom component="3">CE1,CE2</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink3</Category>
	</Entry>
	<Entry>
		<Id>0160</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-(4a-FMN)-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-(4a-riboflavin 5'-dihydrogen phosphate)sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0351</Id>
			<Name>S-(4a-FMN)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00356</Id>
			<Name>S-(4a-FMN)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FMN</Id>
			<Name>flavin mononucleotide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">FMN</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">SG</Atom>
				<Atom component="2">C4A</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>phosphoprotein</Keyword>
		<Keyword>flavoprotein</Keyword>
		<Keyword>FMN</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0161</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide.</Description>
		<SystematicName>[8-amino-1a,2,4a,5,6,7,10-heptahydro-2-(trihydrogen diphosphate 5'-ester with cytosine)methyl-6-oxo-3,4-dimercapto-pteridino[6,7-5,6]pyranoato-S3,S4]-cysteinyl-S-copper-mu-sulfido-molybdenum hydroxide oxide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0355</Id>
			<Name>L-cysteinyl copper sulfido molybdopterin cytosine dinucleotide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00360</Id>
			<Name>L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CUN</Id>
			<Name>Cu(I)-S-Mo(IV)(=O)OH cluster</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MCN</Id>
			<Name>pterin cytosine dinucleotide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CUN</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">MCN</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">SG</Atom>
				<Atom component="2">CU</Atom>
			</Bond>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="2" atom="1">MO</Atom>
				<Atom component="3">S7'</Atom>
			</Bond>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="2" atom="1">MO</Atom>
				<Atom component="3">S8'</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>copper</Keyword>
		<Keyword>metalloprotein</Keyword>
		<Keyword>molybdenum</Keyword>
		<Keyword>molybdopterin</Keyword>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0162</Id>
		<Description>A protein modification that effectively converts three L-cysteine residues, an S-adenosylmethionine and a four-iron four-sulfur cluster to tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide.</Description>
		<SystematicName>tetra-mu3-sulfido(S-adenosylmethion-N,O-diyliron)tris(S-cysteinyliron)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0356</Id>
			<Name>tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00361</Id>
			<Name>tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SF4</Id>
			<Name>iron/sulfur cluster</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SAM</Id>
			<Name>S-adenosylmethionine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">SF4</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">SAM</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="4">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="4">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="4">FE1,FE2,FE3,FE4</Atom>
			</Bond>
			<Bond>
				<Atom component="4" atom="1">FE1,FE2,FE3,FE4</Atom>
				<Atom component="5">N</Atom>
			</Bond>
			<Bond>
				<Atom component="4" atom="1">FE1,FE2,FE3,FE4</Atom>
				<Atom component="5">O,OXT</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink3</Category>
		<Keyword>4Fe-4S</Keyword>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
		<Keyword>S-adenosyl-L-methionine</Keyword>
	</Entry>
	<Entry>
		<Id>0163</Id>
		<Description>A protein modification that effectively converts three L-cysteine residues, an L-arginine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-arginyl diiron disulfide.</Description>
		<SystematicName>di-mu-sulfido(N(eta1)-arginyl-S-cysteinyliron)(bis-S-cysteinyliron)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0357</Id>
			<Name>tris-L-cysteinyl L-arginyl diiron disulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00362</Id>
			<Name>tris-L-cysteinyl L-arginyl diiron disulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FES</Id>
			<Name>Fe2/S2 (inorganic) cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">ARG</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">FES</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="5" atom="1">FE1,FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="5" atom="1">FE1,FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="5" atom="2">FE1,FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="4">NH1,NH2</Atom>
				<Atom component="5" atom="2">FE1,FE2</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink4</Category>
		<Keyword>2Fe-2S</Keyword>
		<Keyword>iron-sulfur protein</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0164</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O-sulfo-L-serine.</Description>
		<SystematicName>(2S)-2-amino-3-(sulfooxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>OSE</Id>
			<Name>O-sulfo-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0361</Id>
			<Name>O-sulfo-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00366</Id>
			<Name>O-sulfo-L-serine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">OSE</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>sulfoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0165</Id>
		<Description>A protein modification that effectively converts an L-methionine residue to N-carboxy-L-methionine.</Description>
		<SystematicName>(S)-2-carboxyamino-4-(methylsulfanyl)butanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CXM</Id>
			<Name>N-carboxymethionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0363</Id>
			<Name>N-carboxy-L-methionine</Name>
			<Status>deprecated</Status>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00368</Id>
			<Name>N-carboxy-L-methionine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CXM</Id>
				<Terminal>N</Terminal>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>blocked amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0166</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O-acetyl-L-serine.</Description>
		<SystematicName>(2S)-3-(acetyloxy)-2-aminopropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>OAS</Id>
			<Name>O-acetylserine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0364</Id>
			<Name>O-acetyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00369</Id>
			<Name>O-acetyl-L-serine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">OAS</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0167</Id>
		<SystematicName>mu3-1:2:3kappaO-oxido-mu3-1:3:4kappaO-oxido-mu3-2:3:4kappaO-oxido-mu4-1:2:4:5kappaO-oxido-N1'-histidino-O5-glutamato 2-manganese-O5,O5-glutamato 3-manganese-O4-aspartato 4-manganese-O4-aspartato-O5-glutamato 5-manganese</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0366</Id>
			<Name>bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>OEC</Id>
			<Name>oxygen evolving system</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ASP</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ASP</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">GLU</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">GLU</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">GLU</Id>
			</Component>
			<Component component="6">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="7">
				<Id source="PDBCC">OEC</Id>
			</Component>
			<Bond>
				<Atom component="1">OD1,OD2</Atom>
				<Atom component="7">MN1,MN2,MN3,MN4</Atom>
			</Bond>
			<Bond>
				<Atom component="2">OD1,OD2</Atom>
				<Atom component="7">MN1,MN2,MN3,MN4</Atom>
			</Bond>
			<Bond>
				<Atom component="3">OE1,OE2</Atom>
				<Atom component="7">MN1,MN2,MN3,MN4</Atom>
			</Bond>
			<Bond>
				<Atom component="4">OE1,OE2</Atom>
				<Atom component="7">MN1,MN2,MN3,MN4</Atom>
			</Bond>
			<Bond>
				<Atom component="4">OE1,OE2</Atom>
				<Atom component="7">MN1,MN2,MN3,MN4</Atom>
			</Bond>
			<Bond>
				<Atom component="5">OE1,OE2</Atom>
				<Atom component="7">MN1,MN2,MN3,MN4</Atom>
			</Bond>
			<Bond>
				<Atom component="6">NE2</Atom>
				<Atom component="7">MN1,MN2,MN3,MN4</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink6</Category>
		<Keyword>calcium</Keyword>
		<Keyword>manganese</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0168</Id>
		<Description>A protein modification that effectively cross-links two L-tyrosine residues with a carbon-carbon bond to form 3'-(3'-L-tyrosinyl)-L-tyrosine.</Description>
		<SystematicName>(2S,2'S)-3,3'-(6,6'-dihydroxybiphenyl-3,3'-diyl)bis(2-aminopropanoic acid)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0367</Id>
			<Name>3'-(L-tyros-3'-yl)-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00372</Id>
			<Name>3'-(3'-L-tyrosinyl)-L-tyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">CE2</Atom>
				<Atom component="2">CE2</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
	</Entry>
	<Entry>
		<Id>0169</Id>
		<Description>A protein modification that effectively cross-links L-tyrosine residues with an ether bond to form 3'-(O4'-L-tyrosinyl)-L-tyrosine.</Description>
		<SystematicName>(2S)-2-amino-3-[3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-4-hydroxyphenyl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0368</Id>
			<Name>3'-(L-tyros-O4'-yl)-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00373</Id>
			<Name>3'-(O4'-L-tyrosinyl)-L-tyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">OH</Atom>
				<Atom component="2">CE2</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
	</Entry>
	<Entry>
		<Id>0170</Id>
		<Description>A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphouridine through a phosphoramide ester bond to form 1'-(phospho-5'-uridine)-L-histidine.</Description>
		<SystematicName>(S)-2-amino-3-[1-(5'-uridine phosphono)imidazol-4-yl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0372</Id>
			<Name>1'-(phospho-5'-uridine)-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00377</Id>
			<Name>1'-(phospho-5'-uridine)-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>U5P</Id>
			<Name>uridine-5'-monophosphate</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">U5P</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">NE2</Atom>
				<Atom component="2">P</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0171</Id>
		<Description>A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue to form 2-imino-glutamic acid 5-imidazolinone glycine.</Description>
		<SystematicName>2-(3-carboxy-1-iminopropyl)-1-carboxymethyl-1-imidazolin-5-one</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CRU</Id>
			<Name>4-[(4Z)-1-(carboxymethyl)-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-2-yl]-4-iminobutanoic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0378</Id>
			<Name>2-imino-glutamic acid 5-imidazolinone glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00383</Id>
			<Name>2-imino-glutamic acid 5-imidazolinone glycine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CRU</Id>
			</Component>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>crosslink1</Category>
		<Comment>CRU has two modifications: RESID:AA0183 and RESID:AA0378</Comment>
		<Keyword>chromoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0172</Id>
		<Description>A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine.</Description>
		<SystematicName>(Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CRU</Id>
			<Name>4-[(4Z)-1-(carboxymethyl)-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-2-yl]-4-iminobutanoic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0183</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00191</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CRU</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Comment>CRU has two modifications: RESID:AA0183 and RESID:AA0378</Comment>
	</Entry>
	<Entry>
		<Id>0173</Id>
		<Description>A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine.</Description>
		<SystematicName>2-[1-imino-3-(methylsulfanyl)propyl]-1-carboxymethyl-1-imidazolin-5-one</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CH6</Id>
			<Name>{(4Z)-2-[(1S)-1-amino-3-(methylsulfanyl)propyl]-4-[(4-hydroxyphenyl)methylidene]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0379</Id>
			<Name>2-imino-methionine 5-imidazolinone glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00384</Id>
			<Name>2-imino-methionine 5-imidazolinone glycine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CH6</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Comment>CH6 has two modifications: RESID:AA0183 and RESID:AA0379</Comment>
		<Keyword>chromoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0174</Id>
		<Description>A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine.</Description>
		<SystematicName>(Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CH6</Id>
			<Name>{(4Z)-2-[(1S)-1-amino-3-(methylsulfanyl)propyl]-4-[(4-hydroxyphenyl)methylidene]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0183</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00191</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CH6</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Comment>CH6 has two modifications: RESID:AA0183 and RESID:AA0379</Comment>
	</Entry>
	<Entry>
		<Id>0175</Id>
		<Description>A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine.</Description>
		<SystematicName>2-[1-imino-3-(methylsulfanyl)propyl]-1-carboxymethyl-1-imidazolin-5-one</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NRQ</Id>
			<Name>{(4Z)-4-(4-hydroxybenzylidene)-2-[3-(methylthio)propanimidoyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0379</Id>
			<Name>2-imino-methionine 5-imidazolinone glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00384</Id>
			<Name>2-imino-methionine 5-imidazolinone glycine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">NRQ</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Comment>NRQ has two modifications: RESID:AA0183 and RESID:AA0379</Comment>
		<Keyword>chromoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0176</Id>
		<Description>A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine.</Description>
		<SystematicName>(Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NRQ</Id>
			<Name>{(4Z)-4-(4-hydroxybenzylidene)-2-[3-(methylthio)propanimidoyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0183</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00191</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">NRQ</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Comment>NRQ has two modifications: RESID:AA0183 and RESID:AA0379</Comment>
	</Entry>
	<Entry>
		<Id>0177</Id>
		<Description>A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue to form L-asparagine 5-imidazolinone glycine.</Description>
		<SystematicName>2-[(S)-1,3-diamino-3-oxopropyl]-1-carboxymethyl-1-imidazolin-5-one</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NYG</Id>
			<Name>[(4Z)-2-[(1S)-1,3-diamino-3-oxoprolyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0380</Id>
			<Name>L-asparagine 5-imidazolinone glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00385</Id>
			<Name>L-asparagine 5-imidazolinone glycine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">NYG</Id>
			</Component>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>crosslink1</Category>
		<Comment>NYG has two modifications: RESID:AA0183 and RESID:AA0380</Comment>
	</Entry>
	<Entry>
		<Id>0178</Id>
		<Description>A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine.</Description>
		<SystematicName>(Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NYG</Id>
			<Name>[(4Z)-2-[(1S)-1,3-diamino-3-oxoprolyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0183</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00191</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">NYG</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Comment>NYG has two modifications: RESID:AA0183 and RESID:AA0380</Comment>
	</Entry>
	<Entry>
		<Id>0179</Id>
		<Description>A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form L-lysine 5-imidazolinone glycine.</Description>
		<SystematicName>2-[(S)-1,5-diaminopentanyl]-1-carboxymethyl-1-imidazolin-5-one</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CR7</Id>
			<Name>[(4Z)-2-[(1S)-1,5-diaminopentyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0381</Id>
			<Name>L-lysine 5-imidazolinone glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00386</Id>
			<Name>L-lysine 5-imidazolinone glycine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CR7</Id>
			</Component>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>crosslink1</Category>
		<Comment>CR7 has two modifications: RESID:AA0183 and RESID:AA0381</Comment>
	</Entry>
	<Entry>
		<Id>0180</Id>
		<Description>A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form 2-tetrahydropyridinyl-5-imidazolinone glycine.</Description>
		<SystematicName>2-(3,4,5,6-tetrahydropyridin-2-yl)-1-carboxymethyl-1-imidazolin-5-one</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CH7</Id>
			<Name>[(4Z)-2-[(1S)-1,5-diaminopentyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0382</Id>
			<Name>2-tetrahydropyridinyl-5-imidazolinone glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00387</Id>
			<Name>2-tetrahydropyridinyl-5-imidazolinone glycine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CH7</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
	</Entry>
	<Entry>
		<Id>0181</Id>
		<Description>A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine.</Description>
		<SystematicName>(Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CR7</Id>
			<Name>[(4Z)-2-[(1S)-1,5-diaminopentyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0183</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00191</Id>
			<Name>(Z)-2,3-didehydrotyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CR7</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Comment>CR7 has two modifications: RESID:AA0183 and RESID:AA0381/AA0382</Comment>
	</Entry>
	<Entry>
		<Id>0182</Id>
		<Description>a protein modification that effectively converts an L-histidine residue to L-histidino vanadium tetraoxide</Description>
		<SystematicName>dihydrogen (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (tetraoxido)vanadate</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0395</Id>
			<Name>L-histidino vanadium tetraoxide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00802</Id>
			<Name>L-histidino vanadium tetraoxide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>VO4</Id>
			<Name>vanadate ion</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">VO4</Id>
			</Component>
			<Bond>
				<Atom component="1">NE2</Atom>
				<Atom component="2">V</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>metalloprotein</Keyword>
		<Keyword>vanadium</Keyword>
	</Entry>
	<Entry>
		<Id>0183</Id>
		<Description>A protein modification that effectively cross-links an L-cysteine residue and an L-tyrosine residue by a thioether bond to form 3-(S-L-cysteinyl)-L-tyrosine.</Description>
		<SystematicName>(S,R)-2-amino-3-(2-amino-2-carboxyethylsulfanyl)-3-(4-hydroxyphenyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0396</Id>
			<Name>3-(S-L-cysteinyl)-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00803</Id>
			<Name>3-(S-L-cysteinyl)-L-tyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">SG</Atom>
				<Atom component="2">CB</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0184</Id>
		<Description>A protein modification that effectively crosslinks an L-alanine residue and an L-cysteine residue by a thioester bond to form S-(L-alanyl)-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-[(S)-2-amino-1-oxopropyl]sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0411</Id>
			<Name>S-(L-alanyl)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00821</Id>
			<Name>S-(L-alanyl)-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ALA</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">SG</Atom>
			</Bond>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked carboxyl end</Keyword>
		<Keyword>thioester bond</Keyword>
	</Entry>
	<Entry>
		<Id>0185</Id>
		<Description>A protein modification that effectively crosslinks an L-leucine residue and an L-cysteine residue by a thioester bond to form S-(L-leucyl)-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-[(S)-2-amino-4-methyl-1-oxopentyl]sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0412</Id>
			<Name>S-(L-leucyl)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00822</Id>
			<Name>S-(L-leucyl)-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">LEU</Id>
				<Terminal>C</Terminal>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked carboxyl end</Keyword>
		<Keyword>thioester bond</Keyword>
	</Entry>
	<Entry>
		<Id>0186</Id>
		<Description>A protein modification that effectively crosslinks an L-methionine residue and an L-cysteine residue by a thioester bond to form S-(L-methionyl)-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-[(S)-2-amino-4-methylsulfanyl-1-oxobutyl]sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0413</Id>
			<Name>S-(L-methionyl)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00823</Id>
			<Name>S-(L-methionyl)-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">MET</Id>
				<Terminal>C</Terminal>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked carboxyl end</Keyword>
		<Keyword>thioester bond</Keyword>
	</Entry>
	<Entry>
		<Id>0187</Id>
		<Description>A protein modification that effectively crosslinks an L-phenylalanine residue and an L-cysteine residue by a thioester bond to form S-(L-phenylalaninyl)-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-[(S)-2-amino-3-phenyl-1-oxopropyl]sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0414</Id>
			<Name>S-(L-phenylalanyl)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00825</Id>
			<Name>S-(L-phenylalanyl)-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PHE</Id>
				<Terminal>C</Terminal>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked carboxyl end</Keyword>
		<Keyword>thioester bond</Keyword>
	</Entry>
	<Entry>
		<Id>0188</Id>
		<Description>A protein modification that effectively crosslinks an L-threonine residue and an L-cysteine residue by a thioester bond to form S-(L-threonyl)-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-[(2S,3R)-2-amino-3-hydroxy-1-oxobutyl]sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0415</Id>
			<Name>S-(L-threonyl)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00826</Id>
			<Name>S-(L-threonyl)-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">THR</Id>
				<Terminal>C</Terminal>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked carboxyl end</Keyword>
		<Keyword>thioester bond</Keyword>
	</Entry>
	<Entry>
		<Id>0189</Id>
		<Description>A protein modification that effectively crosslinks an L-tyrosine residue and an L-cysteine residue by a thioester bond to form S-(L-tyrosyl)-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-[(S)-2-amino-3-(4-hydoxyphenyl)-1-oxopropyl]sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0416</Id>
			<Name>S-(L-tyrosyl)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00827</Id>
			<Name>S-(L-tyrosyl)-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TYR</Id>
				<Terminal>C</Terminal>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked carboxyl end</Keyword>
		<Keyword>thioester bond</Keyword>
	</Entry>
	<Entry>
		<Id>0190</Id>
		<Description>A protein modification that effectively crosslinks an L-tryptophan residue and an L-cysteine residue by a thioester bond to form S-(L-tryptophanyl)-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-[(S)-2-amino-3-(1H-indol-3-yl)-1-oxopropyl]sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0417</Id>
			<Name>S-(L-tryptophanyl)-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00828</Id>
			<Name>S-(L-tryptophanyl)-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TRP</Id>
				<Terminal>C</Terminal>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked carboxyl end</Keyword>
		<Keyword>thioester bond</Keyword>
	</Entry>
	<Entry>
		<Id>0191</Id>
		<Description>A protein modification that effectively crosslinks an L-phenylalanine residue and an L-serine residue by an ester bond to form S-(L-phenylalaninyl)-L-serine.</Description>
		<SystematicName>(R)-2-amino-3-[(S)-2-amino-3-phenyl-1-oxopropyl]oxypropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0418</Id>
			<Name>O-(L-phenylalanyl)-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00829</Id>
			<Name>O-(L-phenylalanyl)-L-serine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PHE</Id>
				<Terminal>C</Terminal>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0192</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to O-acetyl-L-threonine.</Description>
		<SystematicName>(2S,3R)-3-(acetyloxy)-2-aminobutanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>TH5</Id>
			<Name>O-acetyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0423</Id>
			<Name>O-acetyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01171</Id>
			<Name>O-acetyl-L-threonine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TH5</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0193</Id>
		<Description>A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound 15,16-dihydrobiliverdin.</Description>
		<SystematicName>(16R)-18-ethenyl-8,12-bis(2-carboxyethyl)-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,7,13,17-tetramethyl-15,16-dihydrobilin-1,19(21H,24H)-dione</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0428</Id>
			<Name>S-15,16-dihydrobiliverdin-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01142</Id>
			<Name>S-15,16-dihydrobiliverdin-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DBV</Id>
			<Name>15,16-dihydrobiliverdin</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">DBV</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">CAA</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>chromoprotein</Keyword>
		<Keyword>dihydrobiliverdin</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0194</Id>
		<Description>A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound 15,16-dihydrobiliverdin.</Description>
		<SystematicName>(16R)-8,12-bis(2-carboxyethyl)-3-[2-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-18-[(1Xi)-1-(((2R)-2-amino-2-carboxy)ethylsulfanyl)ethyl]-2,7,13,17-tetramethyl-15,16-dihydrobilin-1,19(21H,24H)-dione</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0429</Id>
			<Name>15,16-dihydrobiliverdin-bis-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01143</Id>
			<Name>15,16-dihydrobiliverdin-bis-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DBV</Id>
			<Name>15,16-dihydrobiliverdin</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">DBV</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="3">CBA</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="3">CAD</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>chromoprotein</Keyword>
		<Keyword>dihydrobiliverdin</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0195</Id>
		<Description>A protein modification that effectively cross-links an L-lysine residue and an L-lysine residue converted to allysine with a carbon-nitrogen bond to form L-dehydrolysinonorleucine.</Description>
		<SystematicName>(2S)-2-amino-6-([(5S)-5-amino-5-carboxypentylidene]amino)hexanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0430</Id>
			<Name>L-dehydrolysinonorleucine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01176</Id>
			<Name>L-dehydrolysinonorleucine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Bond>
				<Atom component="1">NZ</Atom>
				<Atom component="2">CE</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
	</Entry>
	<Entry>
		<Id>0196</Id>
		<Description>A protein modification that effectively converts an L-histidine residue to 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine.</Description>
		<SystematicName>(S)-2-amino-3-[1-(1,2,3-trihydroxypropan-2-yl)-1H-imidazol-4-yl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HIQ</Id>
			<Name>1-[1,2-dihydroxy-1-(hydroxymethyl)ethyl]-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0431</Id>
			<Name>1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01177</Id>
			<Name>1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HIQ</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0197</Id>
		<Description>A protein modification that effectively converts an L-aspartic acid residue to S-(aspart-4-yloxy) thiocarbonate.</Description>
		<SystematicName>(2S)-2-amino-4-(carboxysulfanyl)oxy-4-oxobutanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>OHS</Id>
			<Name>O-(carboxysulfanyl)-4-oxo-L-homoserine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0432</Id>
			<Name>S-(aspart-4-yloxy) thiocarbonate</Name>
			<Status>deprecated</Status>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01178</Id>
			<Name>S-(aspart-4-yloxy) thiocarbonate</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">OHS</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0199</Id>
		<Description>A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD.</Description>
		<SystematicName>6-((R)-2-amino-2-carboxyethyl)sulfanyl-8alpha-[4-((S)-2-amino-2-carboxyethyl)imidazol-3-yl]-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0436</Id>
			<Name>6-(S-L-cysteinyl)-8alpha-(N3'-L-histidino)-FAD</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01182</Id>
			<Name>6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FAD</Id>
			<Name>flavin-adenine dinucleotide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">FAD</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">SG</Atom>
				<Atom component="3">C6</Atom>
			</Bond>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="2">ND1</Atom>
				<Atom component="3">C8M</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>phosphoprotein</Keyword>
		<Keyword>FAD</Keyword>
		<Keyword>flavoprotein</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0200</Id>
		<Description>A protein modification that effectively cross-links two L-selenocysteine residues to form L-selenocystine,</Description>
		<SystematicName>(R,R)-3,3'-diselane-1,2-diylbis(2-aminopropanoic acid)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0437</Id>
			<Name>L-selenocystine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01183</Id>
			<Name>L-selenocystine (oxidized selenocysteine) (Sec-Sec)</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SEC</Id>
			<Name>2-amino-3-selenino-propionic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SEC</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">SEC</Id>
			</Component>
			<Bond>
				<Atom component="1">SEG</Atom>
				<Atom component="2">SEG</Atom>
			</Bond>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>redox-active center</Keyword>
		<Keyword>selenium</Keyword>
	</Entry>
	<Entry>
		<Id>0201</Id>
		<Description>A protein modification that effectively converts three L-cysteine residues, an L-histidine residue and a two-iron two-sulfur cluster to tris-L-cysteinyl L-histidino diiron disulfide.</Description>
		<SystematicName>di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-N3'-histidinoiron)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0438</Id>
			<Name>tris-L-cysteinyl L-histidino diiron disulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00864</Id>
			<Name>tris-L-cysteinyl L-histidino diiron disulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FES</Id>
			<Name>Fe2/S2 (inorganic) cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">FES</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="5" atom="1">FE1,FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="5" atom="1">FE1,FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="3">SG</Atom>
				<Atom component="5" atom="2">FE1,FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="4">ND1</Atom>
				<Atom component="5" atom="2">FE1,FE2</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink4</Category>
		<Keyword>2Fe-2S</Keyword>
		<Keyword>metalloprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0202</Id>
		<Description>A modification that effectively oxygenates C5 of an L-leucine residue to form a (2S,4R)-5-oxoleucine.</Description>
		<SystematicName>(2S,4R)-2-amino-5-oxo-4-methylpentanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>LED</Id>
			<Name>(4R)-5-oxo-L-leucine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0444</Id>
			<Name>(2S,4R)-5-oxoleucine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01374</Id>
			<Name>(2S,4R)-5-oxoleucine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LED</Id>
			</Component>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0204</Id>
		<Description>A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4R)-4,5-dihydroxyisoleucine.</Description>
		<SystematicName>(2S,3R,4R)-2-amino-4,5-dihydroxy-3-methylpentanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ILX</Id>
			<Name>(2S,3R,4R)-4,5-dihydroxyisoleucine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0449</Id>
			<Name>(2S,3R,4R)-4,5-dihydroxyisoleucine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01378</Id>
			<Name>(2S,3R,4R)-4,5-dihydroxyisoleucine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ILX</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>hydroxylation</Keyword>
	</Entry>
	<Entry>
		<Id>0205</Id>
		<Description>A protein modification that effectively cross-links an L-cysteine residue and an L-tryptophan residue by a thioether bond to form 2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide.</Description>
		<SystematicName>2-((2R)-2-amino-2carboxyethyl)sulfinyl-3-((2S)-2-amino-2-carboxyethyl)-1H-indole</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0451</Id>
			<Name>2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01380</Id>
			<Name>2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TRP</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">CD1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>hydroxylation</Keyword>
	</Entry>
	<Entry>
		<Id>0206</Id>
		<Description>A protein modification that effectively converts an L-methionine residue to N,N,N-trimethyl-L-methionine.</Description>
		<SystematicName>(1S)-1-carboxy-N,N,N-trimethyl-3-(methylsulfanyl)propan-1-aminium</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0456</Id>
			<Name>N,N,N-trimethyl-L-methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01382</Id>
			<Name>N,N,N-trimethyl-L-methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>4MM</Id>
			<Name>(1S)-1-carboxy-N,N,N-trimethyl-3-(methylsulfanyl)propan-1-aminium</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">4MM</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>thioether bond</Keyword>
		<Keyword>blocked amino end</Keyword>
		<Keyword>methylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0207</Id>
		<Description>A protein modification that effectively cross-links an L-cysteine residue and an L-selenocysteine residues to form L-cysteinyl-L-selenocystine.</Description>
		<SystematicName>(2R)-2-amino-3-[([(2R)-2-amino-2-carboxyethyl]sulfanyl)sulfinyl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0358</Id>
			<Name>L-cysteinyl-L-selenocysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00363</Id>
			<Name>L-cysteinyl-L-selenocysteine (Cys-Sec)</Name>
		</CrossReference>
			<CrossReference>
			<Source>PDBCC</Source>
			<Id>SEC</Id>
			<Name>2-amino-3-selenino-propionic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">SEC</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">SEG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>redox-active center</Keyword>
		<Keyword>selenium</Keyword>
		<Keyword>selenocysteine</Keyword>
	</Entry>
	<Entry>
		<Id>0208</Id>
		<Description>A protein modification that effectively converts an L-serine residue to an aminomalonic acid.</Description>
		<SystematicName>aminopropanedioic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FGL</Id>
			<Name>2-aminopropanedioic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0458</Id>
			<Name>aminomalonic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01384</Id>
			<Name>aminomalonic acid (Ser)</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">FGL</Id>
			</Component>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0209</Id>
		<Description>	A protein modification that effectively cross-links two L-tyrosine residues through their 5' positions by amine nitrogen to form 5'-(L-tyros-5'-yl)amino-L-tyrosine.</Description>
		<SystematicName>(2S,2'S)-3,3'-[iminobis(4-hydroxybenzene-3,1-diyl)]bis(2-aminopropanoic acid)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0459</Id>
			<Name>5'-(L-tyros-5'-yl)amino-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01787</Id>
			<Name>5'-(L-tyros-5'-yl)amino-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>TY2</Id>
			<Name>3-amino-L-tyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TY2</Id>
			</Component>
		   <Bond>
		    	<Atom component="1">CE2,CE1</Atom>
			    <Atom component="2">NE2</Atom>
		    </Bond>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>crosslink2</Category>
	</Entry>
	<Entry>
		<Id>0210</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to O-methyl-L-threonine.</Description>
		<SystematicName>(2S,3R)-2-amino-3-methoxybutanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>OLT</Id>
			<Name>O-methyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0464</Id>
			<Name>O-methyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01387</Id>
			<Name>O-methyl-L-threonine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">OLT</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0213</Id>
		<Description>A protein modification that effectively results from forming an adduct between an isoleucine residue, a threonine residue and the quinaldate compound 2-carboxy-4-(1-hydroxyethyl)--7,8-dihydroquinolin-8-ol.</Description>
		<SystematicName>(7R,8S)-7-[(1S,2S)-1-carboxy-2-methylbutyl]amino-2-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)carbonyl-8-hydroxy-4-[(1S)-1-hydroxyethyl]-7,8-dihydroquinoline</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0472</Id>
			<Name>4-(1-hydroxyethyl)-7-isoleucino-2-(threonin-O3-ylcarbonyl)-7,8-dihydroquinolin-8-ol</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01395</Id>
			<Name>4-(1-hydroxyethyl)-7-isoleucino-2-(threonin-O3-ylcarbonyl)-7,8-dihydroquinolin-8-ol</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>QUA</Id>
			<Name>8-hydroxy-4-(1-hydroxyethyl)quinoline-2-carboxylic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ILE</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="3">
				<Id source="PDBCC">QUA</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">CB</Atom>
				<Atom component="3">O1'</Atom>
			</Bond>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="2">N</Atom>
				<Atom component="3">C7</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0214</Id>
		<Description>A protein modification that effectively converts an L-asparagine residue to a (2S,3S)-3-hydroxyasparagine.</Description>
		<SystematicName>(2S,3S)-2-amino-3-hydroxy-4-butanediamic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>AHB</Id>
			<Name>beta-hydroxyasparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0478</Id>
			<Name>(2S,3S)-3-hydroxyasparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01401</Id>
			<Name>(2S,3S)-3-hydroxyasparagine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">AHB</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>hydroxylation</Keyword>
	</Entry>
	<Entry>
		<Id>0215</Id>
		<Description>A protein modification that effectively cross-links an L-valine residue and an L-tyrosine residue by an ether bond to form 3-(O4'-L-tyrosyl)-L-valine.</Description>
		<SystematicName>(2S)-2-amino-3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-3-methylbutanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0490</Id>
			<Name>3-(O4'-L-tyrosyl)-L-valine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01442</Id>
			<Name>3-(O4'-L-tyrosyl)-L-valine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">VAL</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Bond>
				<Atom component="1">CB</Atom>
				<Atom component="2">OH</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
	</Entry>
	<Entry>
		<Id>0216</Id>
		<Description>	A protein modification that effectively converts a source amino acid residue to L-3,3-dihydroxyoalanine.</Description>
		<SystematicName>(S)-2-amino-3,3-dihydroxypropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DDZ</Id>
			<Name>3,3-dihydroxy L-alanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0492</Id>
			<Name>3,3-dihydroxy-L-alanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01448</Id>
			<Name>L-3,3-dihydroxyoalanine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DDZ</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0217</Id>
		<Description>A protein modification that effectively converts an N-formyl-Lmethionine residue to N-(dihydroxymethyl)-L-methionine.</Description>
		<SystematicName>(2S)-2-[(dihydroxymethyl)amino]-4-(methylsulfanyl)butanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CXM</Id>
			<Name>N-carboxymethionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0493</Id>
			<Name>N-(dihydroxymethyl)-L-methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01446</Id>
			<Name>N-(dihydroxymethyl)-L-methionine (fMet)</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CXM</Id>
			</Component>
		</Condition>
		<Occurrence>hypothetical</Occurrence>
		<Category>modified residue</Category>
		<Keyword>thioether bond</Keyword>
		<Keyword>blocked amino end</Keyword>
		<Keyword>formylation</Keyword>
		<Keyword>pretranslational modification</Keyword>
	</Entry>
	<Entry>
		<Id>0218</Id>
		<Description>A protein modification that effectively crosslinks an N-terminal L-proline residue and a strand of DNA at the C-1 of a ribose, freeing the nucleotide base and forming N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium.</Description>
		<SystematicName>(1Z,2S)-2-carboxy-1-[(3R,4R)-3,4-dihydroxy-5-(phosphonooxy)pentylidene]pyrrolidinium</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PED</Id>
			<Name>pentane-3,4-diol-5-phosphate</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0494</Id>
			<Name>N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01454</Id>
			<Name>N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">PED</Id>
				<Terminal>N</Terminal>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>phosphoprotein</Keyword>
		<Keyword>blocked amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0219</Id>
		<Description>A protein modification that effectively crosslinks an L-serine residue and a glycine residue by an ester bond to form O-glycyl-L-serine.</Description>
		<SystematicName>(2S)-2-amino-3-[(aminoacetyl)oxy]propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0495</Id>
			<Name>O-glycyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01585</Id>
			<Name>O-glycyl-L-serine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GLY</Id>
				<Terminal>C</Terminal>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0220</Id>
		<Description>A protein modification that effectively crosslinks an L-threonine residue and a glycine residue by an ester bond to form O-glycyl-L-threonine</Description>
		<SystematicName>(2S,3R)-2-amino-3-[(aminoacetyl)oxy]butanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0496</Id>
			<Name>O-glycyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01586</Id>
			<Name>O-glycyl-L-threonine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GLY</Id>
				<Terminal>C</Terminal>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">OG1</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
		<Keyword>blocked carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0221</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O-(2-aminoethylphosphoryl)-L-serine.</Description>
		<SystematicName>(2S)-2-amino-3-([(2-aminoethoxy)(hydroxy)phosphoryl]oxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0497</Id>
			<Name>O-(2-aminoethylphosphoryl)-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01587</Id>
			<Name>O-(2-aminoethylphosphoryl)-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>OPE</Id>
			<Name>phosphoric acid mono-(2-amino-ethyl) ester</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">OPE</Id>
			</Component>
			<Bond>
				<Atom component="1">OG,CB</Atom>
				<Atom component="2">P,O1,O2,O3</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0222</Id>
		<Description>A protein modification that effectively converts an L-lysine residue, and an L-methionine residue to S-(L-lysyl)-L-methionine sulfilimine.</Description>
		<SystematicName>(E)-N6-([(3S)-3-amino-3-carboxypropyl](methyl)-lambda4-sulfanylidene)-L-lysine</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0501</Id>
			<Name>S-(L-lysyl)-L-methionine sulfilimine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01602</Id>
			<Name>S-(L-lysyl)-L-methionine sulfilimine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">MET</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">NZ</Atom>
				<Atom component="2">SD</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
	</Entry>
	<Entry>
		<Id>0223</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to 3'-iodo-L-tyrosine.</Description>
		<SystematicName>(2S)-2-amino-3-(4-hydroxy-3-iodophenyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>IYR</Id>
			<Name>3-iodo-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0509</Id>
			<Name>3'-iodo-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01612</Id>
			<Name>3'-iodo-L-tyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">IYR</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>iodine</Keyword>
	</Entry>
	<Entry>
		<Id>0224</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to 3',5'-diiodo-L-tyrosine.</Description>
		<SystematicName>(2S)-2-amino-3-(4-hydroxy-3,5-diiodophenyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>TYI</Id>
			<Name>3,5-diiodotyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0510</Id>
			<Name>3',5'-diiodo-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01613</Id>
			<Name>3',5'-diiodo-L-tyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYI</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>iodine</Keyword>
	</Entry>
	<Entry>
		<Id>0225</Id>
		<Description>A protein modification that effectively cross-links two L-cysteine residues and adds three sulfur atoms to form trithiocystine.</Description>
		<SystematicName>(2R,2'R)-3,3'-pentasulfane-1,5-diylbis(2-aminopropanoic acid)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0513</Id>
			<Name>trithiocystine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01616</Id>
			<Name>trithiocystine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>S3H</Id>
			<Name>trisulfane</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">S3H</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="3">S1</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="3">S3</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink2</Category>
	</Entry>
	<Entry>
		<Id>0226</Id>
		<Description>A protein modification that effectively converts an L-tryptophan residue to a 7'-hydroxy-L-tryptophan.</Description>
		<SystematicName>(2S)-2-amino-3-(7-hydroxy-1H-indol-3-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>0AF</Id>
			<Name>7-hydroxy-L-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0520</Id>
			<Name>7'-hydroxy-L-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01664</Id>
			<Name>7'-hydroxy-L-tryptophan</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">0AF</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>hydroxylation</Keyword>
	</Entry>
	<Entry>
		<Id>0227</Id>
		<Description>A protein modification that effectively converts an L-aspartic acid residue to O4-(8alpha-FAD)-L-aspartate.</Description>
		<SystematicName>(2S)-2-amino-4-oxo-4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxybutanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0522</Id>
			<Name>O4-(8alpha-FAD)-L-aspartate</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01668</Id>
			<Name>O4-(8alpha-FAD)-L-aspartate</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FAD</Id>
			<Name>flavin-adenine dinucleotide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ASP</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">FAD</Id>
			</Component>
			<Bond>
				<!--TODO: verify this-->
				<Atom component="1">OD1,OD2</Atom>
				<Atom component="2">C8M</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>phosphoprotein</Keyword>
		<Keyword>FAD</Keyword>
		<Keyword>flavoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0228</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to O-(L-isoaspartyl)-L-threonine, using free L-asparagine and releasing ammonia. This is not an ester cross-link of peptides.</Description>
		<SystematicName>(2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>AEI</Id>
			<Name>threonine-aspartic ester</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0525</Id>
			<Name>O-(L-isoaspartyl)-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01671</Id>
			<Name>O-(L-isoaspartyl)-L-threonine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">AEI</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
	</Entry>
	<Entry>
		<Id>0229</Id>
		<Description>A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine.</Description>
		<SystematicName>(2S)-2-(acetamido)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0041</Id>
			<Name>N-acetyl-L-alanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00050</Id>
			<Name>N-acetyl-L-alanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ACE</Id>
			<Name>acetyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ALA</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ACE</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0230</Id>
		<Description>A protein modification that effectively converts an L-aspartic acid residue to N-acetyl-L-aspartic acid.</Description>
		<SystematicName>(S)-2-(acetamido)butanedioic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0042</Id>
			<Name>N-acetyl-L-aspartic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00051</Id>
			<Name>N-acetyl-L-aspartic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ACE</Id>
			<Name>acetyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ASP</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ACE</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0231</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine.</Description>
		<SystematicName>(R)-2-acetamido-3-sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0043</Id>
			<Name>N-acetyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00052</Id>
			<Name>N-acetyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ACE</Id>
			<Name>acetyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ACE</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0232</Id>
		<Description>A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid.</Description>
		<SystematicName>(S)-2-(acetamido)pentanedioic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0044</Id>
			<Name>N-acetyl-L-glutamic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00053</Id>
			<Name>N-acetyl-L-glutamic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ACE</Id>
			<Name>acetyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLU</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ACE</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0233</Id>
		<Description>A protein modification that effectively converts a glycine residue to N-acetylglycine.</Description>
		<SystematicName>2-(acetamido)ethanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0046</Id>
			<Name>N-acetylglycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00055</Id>
			<Name>N-acetylglycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ACE</Id>
			<Name>acetyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLY</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ACE</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0234</Id>
		<Description>A protein modification that effectively converts an L-proline residue to N-acetyl-L-proline.</Description>
		<SystematicName>(2S)-1-acetyl-2-pyrrolidinecarboxylic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0050</Id>
			<Name>N-acetyl-L-proline</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00059</Id>
			<Name>N-acetyl-L-proline</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ACE</Id>
			<Name>acetyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">PRO</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ACE</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0235</Id>
		<Description>A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine.</Description>
		<SystematicName>(2S)-2-acetamido-3-hydroxypropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0051</Id>
			<Name>N-acetyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00060</Id>
			<Name>N-acetyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ACE</Id>
			<Name>acetyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ACE</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0236</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine.</Description>
		<SystematicName>(2S,3R)-2-acetamido-3-hydroxybutanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0052</Id>
			<Name>N-acetyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00061</Id>
			<Name>N-acetyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ACE</Id>
			<Name>acetyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ACE</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0237</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine.</Description>
		<SystematicName>(2S)-2-acetamido-3-(4-hydoxyphenyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0053</Id>
			<Name>N-acetyl-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00062</Id>
			<Name>N-acetyl-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ACE</Id>
			<Name>acetyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYR</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ACE</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0238</Id>
		<Description>A protein modification that effectively converts an L-valine residue to N-acetyl-L-valine.</Description>
		<SystematicName>(S)-2-acetamido-3-methylbutanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0054</Id>
			<Name>N-acetyl-L-valine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00063</Id>
			<Name>N-acetyl-L-valine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ACE</Id>
			<Name>acetyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">VAL</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ACE</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0239</Id>
		<Description>A protein modification that effectively converts an L-arginine residue to N2-acetyl-L-arginine.</Description>
		<SystematicName>(S)-2-acetamido-5-carbamimidamidopentanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0354</Id>
			<Name>N2-acetyl-L-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00359</Id>
			<Name>N2-acetyl-L-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ACE</Id>
			<Name>acetyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ARG</Id>
				<Terminal>N</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ACE</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0240</Id>
		<Description>A protein modification that effectively converts an L-alanine residue to L-alanine amide.</Description>
		<SystematicName>(S)-2-aminopropanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0081</Id>
			<Name>L-alanine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00090</Id>
			<Name>L-alanine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ALA</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0241</Id>
		<Description>A protein modification that effectively converts an L-asparagine residue to L-asparagine amide.</Description>
		<SystematicName>(S)-2-amino-butanediamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0083</Id>
			<Name>L-asparagine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00092</Id>
			<Name>L-asparagine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ASN</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0242</Id>
		<Description>A protein modification that effectively converts an L-aspartic acid residue to L-aspartic acid 1-amide.</Description>
		<SystematicName>(S)-2-amino-1-butanediamic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0084</Id>
			<Name>L-aspartic acid 1-amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00093</Id>
			<Name>L-aspartic acid 1-amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ASP</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0243</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to L-cysteine amide.</Description>
		<SystematicName>(R)-2-amino-3-sulfanylpropanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0085</Id>
			<Name>L-cysteine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00094</Id>
			<Name>L-cysteine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0244</Id>
		<Description>A protein modification that effectively converts an L-glutamine residue to L-glutamine amide.</Description>
		<SystematicName>(S)-2-amino-pentanediamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0086</Id>
			<Name>L-glutamine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00095</Id>
			<Name>L-glutamine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLN</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0245</Id>
		<Description>A protein modification that effectively converts an L-glutamic acid residue to L-glutamic acid 1-amide.</Description>
		<SystematicName>(S)-2-amino-1-pentanediamic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0087</Id>
			<Name>L-glutamic acid 1-amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00096</Id>
			<Name>L-glutamic acid 1-amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLU</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0246</Id>
		<Description>A protein modification that effectively converts a glycine residue to glycine amide.</Description>
		<SystematicName>2-aminoethanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0088</Id>
			<Name>glycine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00097</Id>
			<Name>glycine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLY</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0247</Id>
		<Description>A protein modification that effectively converts an L-histidine residue to L-histidine amide.</Description>
		<SystematicName>(S)-2-amino-3-(1H-imidazol-4-yl)propanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0089</Id>
			<Name>L-histidine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00098</Id>
			<Name>L-histidine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">HIS</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0248</Id>
		<Description>A protein modification that effectively converts an L-leucine residue to L-leucine amide.</Description>
		<SystematicName>(S)-2-amino-4-methylpentanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0091</Id>
			<Name>L-leucine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00100</Id>
			<Name>L-leucine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LEU</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0249</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to L-lysine amide.</Description>
		<SystematicName>(S)-2,6-diaminohexanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0092</Id>
			<Name>L-lysine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00101</Id>
			<Name>L-lysine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0250</Id>
		<Description>A protein modification that effectively converts an L-proline residue to L-proline amide.</Description>
		<SystematicName>(S)-pyrrolidine-2-carboxamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0095</Id>
			<Name>L-proline amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00104</Id>
			<Name>L-proline amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">PRO</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0251</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide.</Description>
		<SystematicName>(S)-2-amino-3-(4-hydoxyphenyl)propanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0099</Id>
			<Name>L-tyrosine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00108</Id>
			<Name>L-tyrosine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYR</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0253</Id>
		<Description>A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine.</Description>
		<SystematicName>(2S)-2-(acetamido)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>AYA</Id>
			<Name>N-acetyl-L-alanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0041</Id>
			<Name>N-acetyl-L-alanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00050</Id>
			<Name>N-acetyl-L-alanine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">AYA</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0254</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine.</Description>
		<SystematicName>(R)-2-acetamido-3-sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SC2</Id>
			<Name>N-acetyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0043</Id>
			<Name>N-acetyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00052</Id>
			<Name>N-acetyl-L-cysteine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SC2</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
    <Entry>
		<Id>0255</Id>
		<Description>A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid.</Description>
		<SystematicName>(S)-2-(acetamido)pentanedioic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NLG</Id>
			<Name>N-acetyl-L-glutamic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0044</Id>
			<Name>N-acetyl-L-glutamic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00053</Id>
			<Name>N-acetyl-L-glutamic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">NLG</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>	
    <Entry>
		<Id>0256</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine.</Description>
		<SystematicName>(2S,3R)-2-acetamido-3-hydroxybutanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>THC</Id>
			<Name>N-acetyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0052</Id>
			<Name>N-acetyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00061</Id>
			<Name>N-acetyl-L-threonine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THC</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>	
	<Entry>
		<Id>0257</Id>
		<Description>A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine.</Description>
		<SystematicName>(2S)-2-acetamido-3-hydroxypropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SAC</Id>
			<Name>N-acetyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0051</Id>
			<Name>N-acetyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00060</Id>
			<Name>N-acetyl-L-serine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SAC</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>	
	<Entry>
		<Id>0258</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine.</Description>
		<SystematicName>(2S)-2-acetamido-3-(4-hydoxyphenyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>3NF</Id>
			<Name>N-acetyl-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0053</Id>
			<Name>N-acetyl-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00062</Id>
			<Name>N-acetyl-L-tyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">3NF</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>acetylated amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0259</Id>
		<Description>A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine.</Description>
		<SystematicName>(2S)-2-acetamido-4-(methylsulfanyl)butanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>AME</Id>
			<Name>N-acetyl-L-methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0049</Id>
			<Name>N-acetyl-L-methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00058</Id>
			<Name>N-acetyl-L-methionine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">AME</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>thioether bond</Keyword>
		<Keyword>acetylated amino end</Keyword>
	</Entry>	
	<Entry>
		<Id>0260</Id>
		<Description>A protein modification that effectively converts a glycine residue to N-methylglycine.</Description>
		<SystematicName>methylaminoethanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SAR</Id>
			<Name>N-methylglycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0063</Id>
			<Name>N-methylglycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00072</Id>
			<Name>N-methylglycine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SAR</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>methylated amino acid</Keyword>
		<Keyword>methylated amino end</Keyword>
	</Entry>	
	<Entry>
		<Id>0261</Id>
		<Description>A protein modification that effectively converts an L-arginine residue to L-arginine amide.</Description>
		<SystematicName>(S)-2-amino-5-carbamimidamidopentanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0082</Id>
			<Name>L-arginine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00091</Id>
			<Name>L-arginine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ARG</Id>
				<Terminal>C</Terminal>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0262</Id>
		<Description>A protein modification that effectively converts an L-isoleucine residue to L-isoleucine amide.</Description>
		<SystematicName>(2S,3S)-2-amino-3-methylpentanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0090</Id>
			<Name>L-isoleucine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00099</Id>
			<Name>L-isoleucine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ILE</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0263</Id>
		<Description>A protein modification that effectively converts an L-methionine residue to L-methionine amide.</Description>
		<SystematicName>(2S)-2-amino-4-(methylsulfanyl)butanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0093</Id>
			<Name>L-methionine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00102</Id>
			<Name>L-methionine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MET</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>	
	<Entry>
		<Id>0264</Id>
		<Description>A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide.</Description>
		<SystematicName>(S)-2-amino-3-phenylpropanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0094</Id>
			<Name>L-phenylalanine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00103</Id>
			<Name>L-phenylalanine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">PHE</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0265</Id>
		<Description>A protein modification that effectively converts an L-proline residue to L-proline amide.</Description>
		<SystematicName>(S)-pyrrolidine-2-carboxamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0095</Id>
			<Name>L-proline amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00104</Id>
			<Name>L-proline amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">PRO</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>	
	<Entry>
		<Id>0266</Id>
		<Description>A protein modification that effectively converts an L-serine residue to L-serine amide.</Description>
		<SystematicName>(2S)-2-amino-3-hydroxypropanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0096</Id>
			<Name>L-serine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00105</Id>
			<Name>L-serine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>		
	<Entry>
		<Id>0267</Id>
		<Description>A protein modification that effectively converts an L-serine residue to L-serine amide.</Description>
		<SystematicName>(2S)-2-amino-3-hydroxypropanamide</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>SET</Id>
			<Name>aminoserine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0096</Id>
			<Name>L-serine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00105</Id>
			<Name>L-serine amide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SET</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>	
	<Entry>
		<Id>0268</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to L-threonine amide.</Description>
		<SystematicName>(2S,3R)-2-amino-3-hydroxybutanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0097</Id>
			<Name>L-threonine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00106</Id>
			<Name>L-threonine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>	
    <Entry>
		<Id>0269</Id>
		<Description>A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide.</Description>
		<SystematicName></SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0098</Id>
			<Name>L-tryptophan amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00107</Id>
			<Name>L-tryptophan amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TRP</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
    <Entry>
		<Id>0270</Id>
		<Description>A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide.</Description>
		<SystematicName>(2S)-2-amino-3-(1H-indol-3-yl)propanamide</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>LTN</Id>
			<Name>L-tryptophanamide</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0098</Id>
			<Name>L-tryptophan amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00107</Id>
			<Name>L-tryptophan amide</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LTN</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>	
	<Entry>
		<Id>0271</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide.</Description>
		<SystematicName>(S)-2-amino-3-(4-hydoxyphenyl)propanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0099</Id>
			<Name>L-tyrosine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00108</Id>
			<Name>L-tyrosine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>
	<Entry>
		<Id>0272</Id>
		<Description>A protein modification that effectively converts an L-valine residue to L-valine amide.</Description>
		<SystematicName>(S)-2-amino-3-methylbutanamide</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0100</Id>
			<Name>L-valine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00109</Id>
			<Name>L-valine amide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NH2</Id>
			<Name>amino group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">VAL</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NH2</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>amidated carboxyl end</Keyword>
	</Entry>	
	<Entry>
		<Id>0273</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine.</Description>
		<SystematicName>(2R)-2-amino-3-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl]sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0102</Id>
			<Name>S-farnesyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00109</Id>
			<Name>S-farnesyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FAR</Id>
			<Name>farnesyl</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">FAR</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>lipoprotein</Keyword>
        <Keyword>prenylation</Keyword>
        <Keyword>thioether bond</Keyword>
	</Entry>	
	<Entry>
		<Id>0274</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine.</Description>
		<SystematicName>(2R)-2-amino-3-[(2E,6E,10E)-3,7,11,15-tetramethylhexadeca-2,6,10,14-tetraenyl]sulfanylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0104</Id>
			<Name>S-geranylgeranyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00113</Id>
			<Name>S-geranylgeranyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GER</Id>
			<Name>geran-8-yl geran</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GER</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>lipoprotein</Keyword>
        <Keyword>prenylation</Keyword>
        <Keyword>thioether bond</Keyword>
	</Entry>	
	<Entry>
		<Id>0275</Id>
		<Description>A protein modification that effectively converts an L-cysteine, L-serine, or L-tyrosine residue to pyruvic acid.</Description>
		<SystematicName>2-oxopropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PYR</Id>
			<Name>pyruvic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0127</Id>
			<Name>pyruvic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00136</Id>
			<Name>pyruvic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00807</Id>
			<Name>pyruvic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01661</Id>
			<Name>pyruvic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">PYR</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>blocked amino end</Keyword>
	</Entry>	
    <Entry>
		<Id>0276</Id>
		<Description>A protein modification that effectively converts an L-threonine residue into 2-oxobutanoic acid.</Description>
		<SystematicName>2-oxobutanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>2KT</Id>
			<Name>2-oxobutanoic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0129</Id>
			<Name>2-oxobutanoic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00138</Id>
			<Name>2-oxobutanoic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">2KT</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>blocked amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0277</Id>
		<Description>A protein modification that effectively results from forming an adduct between a cysteine residue and the porphyrin compound heme b, (7,12-diethenyl-3,8,13,17-tetramethylporphyrin-2,18-dipropanoato)iron.</Description>
		<SystematicName>[12-ethenyl-7-((S)-1-[(R)-2-amino-2-carboxy]ethylsulfanyl)ethyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0135</Id>
			<Name>heme-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00144</Id>
			<Name>heme-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>HEM</Id>
			<Name>protoporphyrin IX containing Fe</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">HEM</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
        <Keyword>chromoprotein</Keyword>
        <Keyword>heme</Keyword>
        <Keyword>iron</Keyword>
        <Keyword>metalloprotein</Keyword>
        <Keyword>thioether bond</Keyword>
	</Entry>	
    <Entry>
		<Id>0278</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to L-3',4'-dihydroxyphenylalanine.</Description>
		<SystematicName>(S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DAH</Id>
			<Name>3,4-dihydroxyphenylalanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0146</Id>
			<Name>L-3',4'-dihydroxyphenylalanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00155</Id>
			<Name>L-3',4'-dihydroxyphenylalanine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DAH</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>hydroxylation</Keyword>
	</Entry>	
    <Entry>
		<Id>0279</Id>
		<Description>A protein modification that effectively converts an L-tryptophan residue to L-6'-chlorotryptophan.</Description>
		<SystematicName>(2S)-2-amino-3-(6-chloro-1H-indol-3-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>6CW</Id>
			<Name>6-chloro-L-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0180</Id>
			<Name>6'-chloro-L-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00886</Id>
			<Name>L-6'-chlorotryptophan</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">6CW</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>chlorine</Keyword>
	</Entry>	
    <Entry>
		<Id>0280</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to dehydrobutyrine.</Description>
		<SystematicName>(2Z)-2-aminobut-2-enoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DBU</Id>
			<Name>(2Z)-2-aminobut-2-enoic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0182</Id>
			<Name>(Z)-dehydrobutyrine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00190</Id>
			<Name>dehydrobutyrine (Thr)</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DBU</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword></Keyword>
	</Entry>	
	<Entry>
		<Id>0281</Id>
		<Description>A protein modification that effectively converts an L-serine residue to an amino-terminal lactic acid.</Description>
		<SystematicName>2-hydroxypropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>LAC</Id>
			<Name>lactic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0186</Id>
			<Name>lactic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00194</Id>
			<Name>lactic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LAC</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>blocked amino end</Keyword>
	</Entry>
	<Entry>
		<Id>0282</Id>
		<Description>A protein modification that effectively converts an L-methionine residue to D-methionine.</Description>
		<SystematicName>(R)-2-amino-4-(methylsulfanyl)butanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MED</Id>
			<Name>D-methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0193</Id>
			<Name>D-methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00200</Id>
			<Name>D-methionine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MED</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>D-amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0283</Id>
		<Description>A protein modification that effectively converts an L-phenylalanine residue to D-phenylalanine.</Description>
		<SystematicName>(R)-2-amino-3-phenylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DPN</Id>
			<Name>D-phenylalanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0194</Id>
			<Name>D-phenylalanine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00201</Id>
			<Name>D-phenylalanine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DPN</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>D-amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0284</Id>
		<Description>A protein modification that effectively converts a source amino acid residue to D-serine.</Description>
		<SystematicName>(R)-2-amino-3-hydroxypropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DSN</Id>
			<Name>D-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0195</Id>
			<Name>D-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00891</Id>
			<Name>D-serine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DSN</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>D-amino acid</Keyword>
	</Entry>	
	<Entry>
		<Id>0285</Id>
		<Description>A protein modification that effectively converts an L-leucine residue to D-leucine.</Description>
		<SystematicName>(2R)-2-amino-4-methylpentanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DLE</Id>
			<Name>D-leucine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0197</Id>
			<Name>D-leucine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00204</Id>
			<Name>D-leucine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">DLE</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>D-amino acid</Keyword>
	</Entry>
	<Entry>
		<Id>0286</Id>
		<Description>A protein modification that effectively crosslinks an L-tyrosine residue and 5'-phosphoadenosine through a phosphodiester bond to form O4'-(phospho-5'-adenosine)-L-tyrosine.</Description>
		<SystematicName>(S)-2-amino-3-[4-(5'-adenosine phosphonoxy)phenyl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0203</Id>
			<Name>O4'-(phospho-5'-adenosine)-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00208</Id>
			<Name>O4'-(phospho-5'-adenosine)-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>AMP</Id>
			<Name>adenosine monophosphate</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYR</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">AMP</Id>
			</Component>
			<Bond>
				<Atom component="1">OH</Atom>
				<Atom component="2">P</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
        <Keyword>phosphoprotein</Keyword>
	</Entry>	
	<Entry>
		<Id>0287</Id>
		<Description></Description>
		<SystematicName>(2S)-2-amino-5-([amino(phosphonoamino)methylidene]amino)pentanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0222</Id>
			<Name>omega-N-phospho-L-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00227</Id>
			<Name>omega-N-phospho-L-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PO3</Id>
			<Name>phosphite ion</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ARG</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PO3</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">P</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
        <Keyword>phosphoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0288</Id>
		<Description>A protein modification that effectively converts two L-cysteine residues, two L-histidine residues and a two-iron two-sulfur cluster to bis-L-cysteinyl bis-L-histidino diiron disulfide.</Description>
		<SystematicName>di-mu-sulfido(bis-S-cysteinyliron)(bis-N3'-histidinoiron)</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0225</Id>
			<Name>bis-L-cysteinyl bis-L-histidino diiron disulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00230</Id>
			<Name>bis-L-cysteinyl bis-L-histidino diiron disulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FES</Id>
			<Name>Fe2/S2 (inorganic) cluster</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="3">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="4">
				<Id source="PDBCC">HIS</Id>
			</Component>
			<Component component="5">
				<Id source="PDBCC">FES</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="5">FE1,FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="2">SG</Atom>
				<Atom component="5">FE1,FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="3">ND1</Atom>
				<Atom component="5">FE1,FE2</Atom>
			</Bond>
			<Bond>
				<Atom component="4">ND1</Atom>
				<Atom component="5">FE1,FE2</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink4</Category>
        <Keyword>2Fe-2S</Keyword>
        <Keyword>metalloprotein</Keyword>
        <Keyword>Rieske iron-sulfur protein</Keyword>
	</Entry>
    <Entry>
		<Id>0289</Id>
		<Description>A protein modification that effectively crosslinks an L-lysine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form N6-(phospho-5'-adenosine)-L-lysine.</Description>
		<SystematicName>(S)-2-amino-6-(5'-adenosine phosphonamino)hexanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0227</Id>
			<Name>N6-(phospho-5'-adenosine)-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00232</Id>
			<Name>N6-(phospho-5'-adenosine)-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>AMP</Id>
			<Name>adenosine monophospate</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">AMP</Id>
			</Component>
			<Bond>
				<Atom component="1">NZ</Atom>
				<Atom component="2">P</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
        <Keyword>phosphoprotein</Keyword>
	</Entry>	
	<Entry>
		<Id>0290</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-glutathionyl-L-cysteine.</Description>
		<SystematicName>(2S)-2-amino-3-((2S)-2-((4R)-4-amino-4-carboxyl-1-oxobutyl)amino-3-(carboxylmethyl)amino-3-oxo-propyl)dithio-propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CGL</Id>
			<Name></Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0229</Id>
			<Name>L-cysteine glutathione disulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00234</Id>
			<Name>L-cysteine glutathione disulfide</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>CGL</Id>
			<Name>cystine-glutathione</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CGL</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>disulfide bond</Keyword>
	</Entry>
	<Entry>
		<Id>0291</Id>
		<Description>A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazoline-4-carboxylic acid.</Description>
		<SystematicName>(4S)-2-[(1R)-1-amino-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0239</Id>
			<Name>L-cysteine oxazoline-4-carboxylic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00244</Id>
			<Name>L-cysteine oxazoline-4-carboxylic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">OG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Keyword>oxazole/thiazole ring</Keyword>
	</Entry>
	<Entry>
		<Id>0292</Id>
		<Description>A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid.</Description>
		<SystematicName>2-[(1R)-1-amino-2-sulfanylethyl]-1,3-oxazole-4-carboxylic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0238</Id>
			<Name>L-cysteine oxazole-4-carboxylic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00243</Id>
			<Name>L-cysteine oxazole-4-carboxylic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">OG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Keyword>oxazole/thiazole ring</Keyword>
	</Entry>
	<Entry>
		<Id>0293</Id>
		<Description>A protein modification that effectively crosslinks a glycine residue and an L-serine residue to form glycine oxazole-4-carboxylic acid.</Description>
		<SystematicName>2-aminomethyl-1,3-oxazole-4-carboxylic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0240</Id>
			<Name>glycine oxazole-4-carboxylic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00243</Id>
			<Name>glycine oxazole-4-carboxylic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLY</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">OG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Keyword>oxazole/thiazole ring</Keyword>
	</Entry>
	<Entry>
		<Id>0294</Id>
		<Description>A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form glycine thiazole-4-carboxylic acid.</Description>
		<SystematicName>2-(aminomethyl)-1,3-thiazole-4-carboxylic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0241</Id>
			<Name>glycine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00246</Id>
			<Name>glycine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLY</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">SG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Keyword>oxazole/thiazole ring</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0295</Id>
		<Description>A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-serine thiazole-4-carboxylic acid.</Description>
		<SystematicName>2-[(1S)-1-amino-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0242</Id>
			<Name>L-serine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00247</Id>
			<Name>L-serine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">SG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Keyword>oxazole/thiazole ring</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0296</Id>
		<Description>A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazole-4-carboxylic acid.</Description>
		<SystematicName>2-[(1S)-1-amino-2-phenylethyl]-1,3-thiazole-4-carboxylic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0243</Id>
			<Name>L-phenylalanine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00248</Id>
			<Name>L-phenylalanine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">PHE</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">SG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Keyword>oxazole/thiazole ring</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0297</Id>
		<Description>A protein modification that effectively crosslinks two L-cysteine residues to form L-cysteine thiazole-4-carboxylic acid.</Description>
		<SystematicName>2-[(1S)-1-amino-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0244</Id>
			<Name>L-cysteine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00249</Id>
			<Name>L-cysteine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">SG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Keyword>oxazole/thiazole ring</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0298</Id>
		<Description>A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to form L-lysine thiazole-4-carboxylic acid.</Description>
		<SystematicName>2-[(1S)-1,5-diaminopentyl]-1,3-thiazole-4-carboxylic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0245</Id>
			<Name>L-lysine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00250</Id>
			<Name>L-lysine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">LYS</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">SG</Atom>
			</Bond>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Keyword>oxazole/thiazole ring</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0299</Id>
		<Description>A protein modification that effectively cross-links an L-cysteine residue and an L-threonine residue by a thioether bond to form S-(2-aminovinyl)-3-methyl-D-cysteine.</Description>
		<SystematicName>(2S,3S)-2-amino-3-[((Z)-2-aminovinyl)sulfanyl]butanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0253</Id>
			<Name>S-(2-aminovinyl)-3-methyl-D-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00258</Id>
			<Name>S-(2-aminovinyl)-3-methyl-D-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>TEE</Id>
			<Name>2-amino-ethenethiol</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TEE</Id>
			</Component>
			<Bond>
				<Atom component="1">CB</Atom>
				<Atom component="2">SG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>blocked carboxyl end</Keyword>
		<Keyword>lanthionine</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0300</Id>
		<Description>A protein modification that inserts or replaces a residue with an L-pyrrolysine residue, a natural pretranslational modification.</Description>
		<SystematicName>(2R)-2-amino-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]aminohexanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>PYH</Id>
			<Name>N6-{[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl}-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0321</Id>
			<Name>L-pyrrolysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01187</Id>
			<Name>L-pyrrolysine residue</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">PYH</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>pretranslational modification</Keyword>
	</Entry>
	<Entry>
		<Id>0301</Id>
		<Description>A protein modification that effectively converts an L-glutamic acid residue to L-2-aminobutanoic acid.</Description>
		<SystematicName>(S)-2-aminobutanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>ABA</Id>
			<Name>alpha-aminobutyric acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0409</Id>
			<Name>L-2-aminobutanoic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00819</Id>
			<Name>L-2-aminobutanoic acid (Glu)</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ABA</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword></Keyword>
	</Entry>
	<Entry>
		<Id>0302</Id>
		<Description>A protein modification that effectively crosslinks an L-cysteine residue and an L-isoleucine residue to form L-isoleucine thiazole-4-carboxylic acid.</Description>
		<SystematicName>2-[(1S,2S)-1-amino-2-methylbutyl]-1,3-thiazole-4-carboxylic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0466</Id>
			<Name>L-isoleucine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01389</Id>
			<Name>L-isoleucine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ILE</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">SG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Keyword>oxazole/thiazole ring</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0303</Id>
		<Description>A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue to form L-valine thiazole-4-carboxylic acid.</Description>
		<SystematicName>2-[(1S)-1-amino-2-methylpropyl]-1,3-thiazole-4-carboxylic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0467</Id>
			<Name>L-valine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01390</Id>
			<Name>L-valine thiazole-4-carboxylic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">VAL</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CYS</Id>
			</Component>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">N</Atom>
			</Bond>
			<Bond>
				<Atom component="1">C</Atom>
				<Atom component="2">SG</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>crosslink1</Category>
		<Keyword>oxazole/thiazole ring</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0304</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine.</Description>
		<SystematicName>(2S)-2-amino-3-(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyloxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0499</Id>
			<Name>O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01589</Id>
			<Name>O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>DT6</Id>
			<Name>2,4-bis(acetylamino)-1,5-anhydro-2,4-dideoxy-D-glucitol</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">DT6</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0305</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to 3'-nitro-L-tyrosine.</Description>
		<SystematicName>(2S)-2-amino-3-(4-hydroxy-3-nitrophenyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NIY</Id>
			<Name>meta-nitro-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0537</Id>
			<Name>3'-nitro-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01786</Id>
			<Name>3-nitro-L-tyrosine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">NIY</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword></Keyword>
	</Entry>
    <Entry>
		<Id>0306</Id>
		<Description>A protein modification that effectively converts an L-tryptophan residue to a 2'-hydroxy-L-tryptophan.</Description>
		<SystematicName>(2S)-2-amino-3-(2-hydroxy-1H-indol-3-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>TRO</Id>
			<Name>2-hydroxy-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0542</Id>
			<Name>2'-hydroxy-L-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01816</Id>
			<Name>2'-hydroxy-L-tryptophan</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TRO</Id>
			</Component>
		</Condition>
		<Occurrence>artifactual</Occurrence>
		<Category>modified residue</Category>
		<Keyword>hydroxylation</Keyword>
	</Entry>
    <Entry>
		<Id>0307</Id>
		<Description>A protein modification that effectively converts an L-tryptophan residue to a 2'-oxo-L-tryptophan.</Description>
		<SystematicName>(2S)-2-amino-3-[(3S)-2-oxo-2,3-dihydro-1H-indol-3-yl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>TRO</Id>
			<Name>2-hydroxy-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0543</Id>
			<Name>2'-oxo-L-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01817</Id>
			<Name>oxidation of tryptophan to 2'-oxo-L-tryptophan</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TRO</Id>
			</Component>
		</Condition>
		<Occurrence>artifactual</Occurrence>
		<Category>modified residue</Category>
		<Keyword></Keyword>
	</Entry>
    <Entry>
		<Id>0308</Id>
		<Description>The amino group of the following amino acid forms a thiopeptide bond. This is an amino(sulfanyl)methylidene in the tautomeric form.</Description>
		<SystematicName>5-hydroxy-2-(3-methylbutanoyl)-1,3-oxazole-4-carbothioic O-acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>8LI</Id>
			<Name>(4Z)-4-[hydroxy(sulfanyl)methylidene]-2-(3-methylbutanoyl)-1,3-oxazol-5(4H)-one</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0550</Id>
			<Name>2-(3-methylbutanoyl)-5-hydroxy-oxazole-4-carbothionic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Comment>link to MOD:01844 is broken on PSI-MOD site</Comment>
			<Id>MOD:01844</Id>
			<Name>2-(3-methylbutanoyl)-5-hydroxy-oxazole-4-carbothionic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">8LI</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>imidazolinone/oxazolinone ring</Keyword>
	</Entry>
    <Entry>
		<Id>0309</Id>
		<Description>The amino group of the following amino acid forms a thiopeptide bond. This is an amino(sulfanyl)methylidene in the tautomeric form</Description>
		<SystematicName>5-hydroxy-2-[(2S)-pyrrolidin-2-yl]-1,3-oxazole-4-carbothioic O-acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>66G</Id>
			<Name>(4Z)-4-[hydroxy(sulfanyl)methylidene]-2-[(2S)-pyrrolidin-2-yl]-1,3-oxazol-5(4H)-one</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0551</Id>
			<Name>L-proline 5-hydroxy-oxazole-4-carbothionic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Comment>link to MOD:01844 is broken on PSI-MOD site</Comment>
			<Id>MOD:01844</Id>
			<Name>	L-proline 5-hydroxy-oxazole-4-carbothionic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">66G</Id>
			</Component>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>modified residue</Category>
		<Keyword>imidazolinone/oxazolinone ring</Keyword>
	</Entry>
    <Entry>
		<Id>0310</Id>
		<Description>A protein modification that effectively trioxygenates an L-cysteine residue to L-cysteine sulfonic acid.</Description>
		<SystematicName>(2R)-2-amino-3-sulfopropanoic acid</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>OCS</Id>
			<Name>cysteinesulfonic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0556</Id>
			<Name>L-cysteine sulfonic acid</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00460</Id>
			<Name>L-cysteic acid (L-cysteine sulfonic acid)</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">OCS</Id>
			</Component>
		</Condition>
		<Occurrence>artifactual</Occurrence>
		<Category>modified residue</Category>
		<Keyword></Keyword>
	</Entry>
	<Entry>
		<Id>0311</Id>
		<Description>A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification.</Description>
		<SystematicName>(S)-2-formylamino-4-(methylsulfanyl)butanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0021</Id>
			<Name>N-formyl-L-methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00030</Id>
			<Name>N-formyl-L-methionine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FOR</Id>
			<Name>formyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">MET</Id>
				<Terminal>N</Terminal>
			</Component>
		    <Component component="2">
				<Id source="PDBCC">FOR</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Category>attachment</Category>
		<Occurrence>natural</Occurrence>
		<Keyword>thioether bond</Keyword>
		<Keyword>blocked amino end</Keyword>
		<Keyword>formylation</Keyword>
		<Keyword>pretranslational modification</Keyword>
	</Entry>
	<Entry>
		<Id>0312</Id>
		<Description>A protein modification that effectively converts an L-lysine residue to N6-formyl-L-lysine.</Description>
		<SystematicName>(S)-2-amino-6-(formylamino)hexanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0211</Id>
			<Name>N6-formyl-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00216</Id>
			<Name>N6-formyl-L-lysine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FOR</Id>
			<Name>formyl group</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">LYS</Id>
			</Component>
		    <Component component="2">
				<Id source="PDBCC">FOR</Id>
			</Component>
			<Bond>
				<Atom component="1">NZ</Atom>
				<Atom component="2">C</Atom>
			</Bond>
		</Condition>
		<Category>attachment</Category>
		<Occurrence>natural</Occurrence>
		<Keyword>formylation</Keyword>
	</Entry>
	<Entry>
	    <Id>0313</Id>
        <Description>A protein modification that effectively crosslinks an L-alanine residue and a glycine residue to form L-alanine 5-imidazolinone glycine.</Description>
        <SystematicName>(2-[(1S)-1-aminoethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid</SystematicName>
        <CrossReference>
            <Source>RESID</Source>
            <Id>AA0187</Id>
            <Name>L-alanine 5-imidazolinone glycine</Name>
        </CrossReference>
        <CrossReference>
            <Source>PDBCC</Source>
            <Id>AYG</Id>
            <Name>[(4E)-2-[(1S)-1-aminoethyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid</Name>
        </CrossReference>
        <CrossReference>
            <Source>PDBCC</Source>
            <Id>CRQ</Id>
            <Name>[2-(3-carbamoyl-1-imino-propyl)-4-(4-hydroxy-benzylidene)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid</Name>
        </CrossReference>
        <CrossReference>
            <Source>PDBCC</Source>
            <Id>MDO</Id>
            <Name>{2-[(1S)-1-aminoethyl]-4-methylidene-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid</Name>
        </CrossReference>
        <CrossReference>
            <Source>PDBCC</Source>
            <Id>X9Q</Id>
            <Name>{(2S)-2-[(1S)-1-aminoethyl]-4-benzyl-5-oxo-2,5-dihydro-1H-imidazol-1-yl}acetic acid</Name>
        </CrossReference>
        <CrossReference>
            <Source>PSI-MOD</Source>
            <Id>MOD:00195</Id>
            <Name>L-alanine 5-imidazolinone glycine</Name>
        </CrossReference>
        <Condition>
			<Component component="1">
				<Id source="PDBCC">AYG,CRQ,MDO,X9Q</Id>
			</Component>
		</Condition>
		<Category>modified residue</Category>
        <Occurrence>natural</Occurrence>
        <Keyword>imidazolinone/oxazolinone ring</Keyword>
    </Entry>
    <Entry>
        <Id>0314</Id>
        <Description>A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form L-cysteine 5-imidazolinone glycine.</Description>
        <SystematicName>(2-[(1R)-1-amino-2-sulfanylethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid</SystematicName>
        <CrossReference>
            <Source>RESID</Source>
            <Id>AA0188</Id>
            <Name>L-cysteine 5-imidazolinone glycine</Name>
        </CrossReference>
        <CrossReference>
            <Source>PDBCC</Source>
            <Id>GYC</Id>
            <Name>[(4Z)-2-[(1R)-1-amino-2-mercaptoethyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid</Name>
        </CrossReference>
        <CrossReference>
            <Source>PSI-MOD</Source>
            <Id>MOD:00196</Id>
            <Name>L-cysteine 5-imidazolinone glycine</Name>
        </CrossReference>
        <Condition>
			<Component component="1">
				<Id source="PDBCC">GYC</Id>
			</Component>
		</Condition>
		<Category>modified residue</Category>
        <Occurrence>natural</Occurrence>
        <Keyword>imidazolinone/oxazolinone ring</Keyword>
    </Entry>
    <Entry>
        <Id>0315</Id>
        <Description>A protein modification that effectively crosslinks an L-histidine residue and 5'-phosphoadenosine through a phosphoramide ester bond to form 1'-(phospho-5'-adenosine)-L-histidine.</Description>
        <SystematicName>(2S)-2-amino-3-[1-(5'-adenosine phosphono)imidazol-4-yl]propanoic acid</SystematicName>
        <CrossReference>
            <Source>RESID</Source>
            <Id>AA0371</Id>
            <Name>1'-(phospho-5'-adenosine)-L-histidine</Name>
        </CrossReference>
        <CrossReference>
            <Source>PDBCC</Source>
            <Id>AMP</Id>
            <Name>adenosine monophosphate</Name>
        </CrossReference>
        <CrossReference>
            <Source>PSI-MOD</Source>
            <Id>MOD:00376</Id>
            <Name>1'-(phospho-5'-adenosine)-L-histidine</Name>
        </CrossReference>
        <Condition>
			<Component component="1">
				<Id source="PDBCC">HIS</Id>
			</Component>
		    <Component component="2">
				<Id source="PDBCC">AMP</Id>
			</Component>
			<Bond>
				<Atom component="1">NE2</Atom>
				<Atom component="2">P</Atom>
			</Bond>
		</Condition>
		<Category>attachment</Category>
		<Occurrence>natural</Occurrence>
        <Keyword>phosphoprotein</Keyword>
    </Entry>
    <Entry>
        <Id>0316</Id>
        <Description>a protein modification that effectively forms a O3-(N-acetylaminoglucosyl)serine</Description>
        <SystematicName>(2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)propanoic acid</SystematicName>
        <CrossReference>
            <Source>RESID</Source>
            <Id>AA0398</Id>
            <Name>O-(N-acetylamino)glucosyl-L-serine</Name>
        </CrossReference>
        <CrossReference>
            <Source>PDBCC</Source>
            <Id>NAG</Id>
            <Name>N-acetyl-D-glucosamine</Name>
        </CrossReference>
        <CrossReference>
            <Source>PSI-MOD</Source>
            <Id>MOD:00805</Id>
            <Name>O-(N-acetylaminoglucosyl)-L-serine</Name>
        </CrossReference>
        <Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
		    <Component component="2">
				<Id source="PDBCC">NAG</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Category>attachment</Category>
		<Occurrence>natural</Occurrence>
        <Keyword>glycoprotein</Keyword>
    </Entry>
    <Entry>
        <Id>0317</Id>
        <Description>a protein modification that effectively forms a O3-(N-acetylaminoglucosyl)threonine</Description>
        <SystematicName>(2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxyglucopyranosyloxy)butanoic acid</SystematicName>
        <CrossReference>
            <Source>RESID</Source>
            <Id>AA0399</Id>
            <Name>O-(N-acetylamino)glucosyl-L-threonine</Name>
        </CrossReference>
        <CrossReference>
            <Source>PDBCC</Source>
            <Id>NDG</Id>
            <Name>2-(acetylamino)-2-deoxy-A-D-glucopyranose</Name>
        </CrossReference>
        <CrossReference>
            <Source>PSI-MOD</Source>
            <Id>MOD:00806</Id>
            <Name>O-(N-acetylaminoglucosyl)-L-threonine</Name>
        </CrossReference>
        <Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>
		    <Component component="2">
				<Id source="PDBCC">NDG</Id>
			</Component>
			<Bond>
				<Atom component="1">OG1</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Category>attachment</Category>
        <Occurrence>natural</Occurrence>
        <Keyword>glycoprotein</Keyword>
    </Entry>
    <Entry>
        <Id>0318</Id>
        <Description>A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue to form 2-imino-alanine 5-imidazolinone glycine.</Description>
        <SystematicName>(2-ethanimidoyl-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid</SystematicName>
        <CrossReference>
            <Source>RESID</Source>
            <Id>AA0410</Id>
            <Name>2-imino-alanine 5-imidazolinone glycine</Name>
        </CrossReference>
        <CrossReference>
            <Source>PDBCC</Source>
            <Id>XYG</Id>
            <Name>[(4Z)-2-[(1Z)-ethanimidoyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid</Name> 
        </CrossReference>
        <CrossReference>
            <Source>PSI-MOD</Source>
            <Id>MOD:00820</Id>
            <Name>2-imino-alanine 5-imidazolinone glycine</Name>
        </CrossReference>
        <Condition>
			<Component component="1">
				<Id source="PDBCC">XYG</Id>
			</Component>
		</Condition>
        <Category>modified residue</Category>
        <Occurrence>natural</Occurrence>
        <Keyword>imidazolinone/oxazolinone ring</Keyword>
    </Entry>
    <Entry>
        <Id>0319</Id>
        <Description>A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid.</Description>
        <SystematicName>[(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid</SystematicName>
        <CrossReference>
            <Source>RESID</Source>
            <Id>AA0441</Id>
            <Name>(2-aminosuccinimidyl)acetic acid</Name>
        </CrossReference>
        <CrossReference>
            <Source>PDBCC</Source>
            <Id>SUI</Id>
            <Name>(3-amino-2,5-dioxo-1-pyrrolidinly)acetic acid</Name>
        </CrossReference>
        <CrossReference>
            <Source>PSI-MOD</Source>
            <Id>MOD:00952</Id>
            <Name>(2-aminosuccinimidyl)acetic acid</Name>
        </CrossReference>
        <Condition>
			<Component component="1">
				<Id source="PDBCC">SUI</Id>
			</Component>
		</Condition>
        <Category>modified residue</Category>
        <Occurrence>hypothetical</Occurrence>
    </Entry>
    <Entry>
		<Id>320</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>AG</Id>
            <Name>silver ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">AG</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>321</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>AL</Id>
            <Name>aluminum ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">AL</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>322</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>AU</Id>
            <Name>gold ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">AU</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>323</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>AU3</Id>
            <Name>gold 3+ ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">AU3</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>324</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>BA</Id>
            <Name>barium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">BA</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>325</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>CA</Id>
            <Name>calcium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CA</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>326</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>CD</Id>
            <Name>cadmium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CD</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>327</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>CE</Id>
            <Name>cerium (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CE</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>328</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>CO</Id>
            <Name>cobat (II) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CO</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>329</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>3CO</Id>
            <Name>cobat (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">3CO</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>330</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>CR</Id>
            <Name>chromium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CR</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>331</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>CS</Id>
            <Name>cesium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CS</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>332</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>CU</Id>
            <Name>copper (II) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CU</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>333</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>CU1</Id>
            <Name>copper (I) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CU1</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>334</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>CU3</Id>
            <Name>copper (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">CU3</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>335</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>ER3</Id>
            <Name>erbium (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ER3</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
    <Entry>
		<Id>336</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>EU</Id>
            <Name>europium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">EU</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>337</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>EU3</Id>
            <Name>europium (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">EU3</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>338</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>FE</Id>
            <Name>Fe (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">FE</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>339</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>FE2</Id>
            <Name>Fe (II) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">FE2</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>341</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>GA</Id>
            <Name>gallium (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GA</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>342</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>GD</Id>
            <Name>gadolinium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GD</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>343</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>GD3</Id>
            <Name>gadolinium (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GD3</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>344</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>HG</Id>
            <Name>mercury (II) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">HG</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>345</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>HO</Id>
            <Name>holmium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">HO</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>346</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>HO3</Id>
            <Name>holmium (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">HO3</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>347</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>IN</Id>
            <Name>indium (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">IN</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>348</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>IR</Id>
            <Name>iridium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">IR</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>349</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>IR3</Id>
            <Name>iridium (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">IR3</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>350</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>K</Id>
            <Name>potassium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">K</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>351</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>LA</Id>
            <Name>lanthanum (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">LA</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>352</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>LI</Id>
            <Name>lithium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">LI</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>353</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>LU</Id>
            <Name>lutetium (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">LU</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>354</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>MG</Id>
            <Name>magnesium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">MG</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>355</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>MN</Id>
            <Name>manganese (II) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">MN</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>356</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>MN3</Id>
            <Name>manganese (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">MN3</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>357</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>MO</Id>
            <Name>molybdenum ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">MO</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>358</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>4MO</Id>
            <Name>molybdenum (IV) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">4MO</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
    <Entry>
		<Id>359</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>6MO</Id>
            <Name>molybdenum (VI) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">6MO</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>360</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>NA</Id>
            <Name>sodium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NA</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>361</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>NI</Id>
            <Name>nickel (II) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">NI</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>362</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>3NI</Id>
            <Name>nickel (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">3NI</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>363</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>OS</Id>
            <Name>osmium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">OS</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>364</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>OS4</Id>
            <Name>osmium (IV) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">OS4</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>365</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>PB</Id>
            <Name>lead (II) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PB</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>366</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>PD</Id>
            <Name>palladium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PD</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>367</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>PR</Id>
            <Name>praseodymium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PR</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>368</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>PT</Id>
            <Name>platinum (II) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PT</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>369</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>PT4</Id>
            <Name>platinum (IV) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">PT4</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>370</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>RB</Id>
            <Name>rubidium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">RB</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>371</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>RE</Id>
            <Name>rhenium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">RE</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	    <Entry>
		<Id>0252</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>RH</Id>
            <Name>rhodium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">RH</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>372</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>RH3</Id>
            <Name>rhodium (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">RH3</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>373</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>RU</Id>
            <Name>ruthenium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">RU</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>374</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>SM</Id>
            <Name>samarium (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">SM</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>375</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>SR</Id>
            <Name>strontium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">SR</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>376</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>TB</Id>
            <Name>terbium (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TB</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>377</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>TL</Id>
            <Name>thallium (I) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">TL</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>378</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>U1</Id>
            <Name>uranium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">U1</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
    <Entry>
		<Id>379</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>V</Id>
            <Name>vanadium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">V</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>380</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>W</Id>
            <Name>tungsten ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">W</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>381</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>Y1</Id>
            <Name>yttrium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">Y1</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
    <Entry>
		<Id>382</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>YT3</Id>
            <Name>yttrium (III) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">YT3</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>383</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>YB</Id>
            <Name>ytterbium ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">YB</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>384</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>YB2</Id>
            <Name>ytterbium (II) ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">YB2</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>385</Id>
		<Description>Metal coordination</Description>
		<CrossReference>
            <Source>PDBCC</Source>
            <Id>ZN</Id>
            <Name>zinc ion</Name>
        </CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">*</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">ZN</Id>
			</Component>
			<Bond>
				<Atom component="1">*</Atom>
				<Atom component="2">*</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>undefined</Category>
		<Keyword>Metal coordination</Keyword>
	</Entry>
	<Entry>
		<Id>0386</Id>
		<Description>A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine.</Description>
		<SystematicName>(S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)amino-4-oxobutanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0151</Id>
			<Name>N4-(N-acetylamino)glucosyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00831</Id>
			<Name>N4-(N-acetylamino)glucosyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NDG</Id>
			<Name>2-(acetylamino)-2-deoxy-alpha-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ASN</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">NDG</Id>
			</Component>
			<Bond>
				<Atom component="1">ND2</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0387</Id>
		<Description>A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminogalactosyl)-L-asparagine.</Description>
		<SystematicName>(2S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)amino-4-oxobutanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0420</Id>
			<Name>N4-(N-acetylamino)galactosyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00832</Id>
			<Name>N4-(N-acetylamino)galactosyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>A2G</Id>
			<Name>2-(acetylamino)-2-deoxy-alpha-D-galactopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ASN</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">A2G</Id>
			</Component>
			<Bond>
				<Atom component="1">ND2</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0388</Id>
		<Description>A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminogalactosyl)-L-asparagine.</Description>
		<SystematicName>(2S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)amino-4-oxobutanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0420</Id>
			<Name>N4-(N-acetylamino)galactosyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00832</Id>
			<Name>N4-(N-acetylamino)galactosyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NGA</Id>
			<Name>2-(acetylamino)-2-deoxy-beta-D-galactopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ASN</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">NGA</Id>
			</Component>
			<Bond>
				<Atom component="1">ND2</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0389</Id>
		<Description>A protein modification that effectively converts an L-asparagine residue to N4-glucosyl-asparagine.</Description>
		<SystematicName>(S)-2-amino-4-(D-glucopyranosyl)amino-4-oxobutanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0421</Id>
			<Name>N4-glucosyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00833</Id>
			<Name>N4-glucosyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BGC</Id>
			<Name>beta-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ASN</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">BGC</Id>
			</Component>
			<Bond>
				<Atom component="1">ND2</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0390</Id>
		<Description>A protein modification that effectively converts an L-asparagine residue to N4-glucosyl-asparagine.</Description>
		<SystematicName>(S)-2-amino-4-(D-glucopyranosyl)amino-4-oxobutanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0421</Id>
			<Name>N4-glucosyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00833</Id>
			<Name>N4-glucosyl-L-asparagine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GLC</Id>
			<Name>alpha-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ASN</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GLC</Id>
			</Component>
			<Bond>
				<Atom component="1">ND2</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0391</Id>
		<Description>A protein modification that effectively converts an L-arginine residue to N4-glucosyl-arginine.</Description>
		<SystematicName>(S)-2-amino-5-[beta-glucopyranosyl(imino(methylamino)methyl)amino]pentanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0327</Id>
			<Name>omega-N-glucosyl-L-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00332</Id>
			<Name>omega-N-glucosyl-L-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BGC</Id>
			<Name>beta-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ARG</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">BGC</Id>
			</Component>
			<Bond>
				<Atom component="1">NH1,NH2</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0392</Id>
		<Description>A protein modification that effectively converts an L-arginine residue to N4-glucosyl-arginine.</Description>
		<SystematicName>(S)-2-amino-5-[beta-glucopyranosyl(imino(methylamino)methyl)amino]pentanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0327</Id>
			<Name>omega-N-glucosyl-L-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00332</Id>
			<Name>omega-N-glucosyl-L-arginine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GLC</Id>
			<Name>alpha-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">ARG</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GLC</Id>
			</Component>
			<Bond>
				<Atom component="1">NH1,NH2</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0393</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-(N-acetylamino)glucosyl-L-cysteine.</Description>
		<SystematicName>(2R)-2-amino-3-[(beta-D-2-[N-acetylamino]-2-deoxyglucopyranosyl)sulfanyl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0560</Id>
			<Name>S-(N-acetylamino)glucosyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01858</Id>
			<Name>S-(N-acetylamino)glucosyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NAG</Id>
			<Name>N-acetyl-D-glucosamine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">NAG</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0394</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-(N-acetylamino)glucosyl-L-cysteine.</Description>
		<SystematicName>(2R)-2-amino-3-[(beta-D-2-[N-acetylamino]-2-deoxyglucopyranosyl)sulfanyl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0560</Id>
			<Name>S-(N-acetylamino)glucosyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:01858</Id>
			<Name>S-(N-acetylamino)glucosyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NDG</Id>
			<Name>2-(acetylamino)-2-deoxy-alpha-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">NDG</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0395</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine.</Description>
		<SystematicName>(2R)-2-amino-3-[(beta-D-glucopyranosyl)sulfanyl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0152</Id>
			<Name>S-glucosyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00161</Id>
			<Name>S-glucosyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BGC</Id>
			<Name>beta-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">BGC</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0396</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine.</Description>
		<SystematicName>(2R)-2-amino-3-[(beta-D-glucopyranosyl)sulfanyl]propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0152</Id>
			<Name>S-glucosyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00161</Id>
			<Name>S-glucosyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GLC</Id>
			<Name>alpha-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GLC</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0397</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-galactosyl-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-(beta-D-galactopyranosylsulfanyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0392</Id>
			<Name>S-galactosyl-L-cysteine</Name>
			<Status>deprecated</Status>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00799</Id>
			<Name>S-galactosyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GLA</Id>
			<Name>alpha-D-galactopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GLA</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
		<Id>0398</Id>
		<Description>A protein modification that effectively converts an L-cysteine residue to S-galactosyl-L-cysteine.</Description>
		<SystematicName>(R)-2-amino-3-(beta-D-galactopyranosylsulfanyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0392</Id>
			<Name>S-galactosyl-L-cysteine</Name>
			<Status>deprecated</Status>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00799</Id>
			<Name>S-galactosyl-L-cysteine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GAL</Id>
			<Name>beta-D-galactopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">CYS</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GAL</Id>
			</Component>
			<Bond>
				<Atom component="1">SG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
		<Keyword>thioether bond</Keyword>
	</Entry>
	<Entry>
        <Id>0399</Id>
        <Description>a protein modification that effectively forms a O3-(N-acetylaminoglucosyl)serine</Description>
        <SystematicName>(2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)propanoic acid</SystematicName>
        <CrossReference>
            <Source>RESID</Source>
            <Id>AA0398</Id>
            <Name>O-(N-acetylamino)glucosyl-L-serine</Name>
        </CrossReference>
        <CrossReference>
            <Source>PDBCC</Source>
            <Id>NDG</Id>
            <Name>2-(acetylamino)-2-deoxy-alpha-D-glucopyranose</Name>
        </CrossReference>
        <CrossReference>
            <Source>PSI-MOD</Source>
            <Id>MOD:00805</Id>
            <Name>O-(N-acetylaminoglucosyl)-L-serine</Name>
        </CrossReference>
        <Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
		    <Component component="2">
				<Id source="PDBCC">NDG</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Category>attachment</Category>
		<Occurrence>natural</Occurrence>
        <Keyword>glycoprotein</Keyword>
    </Entry>
    <Entry>
		<Id>0400</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O3-beta-glucosylated L-serine.</Description>
		<SystematicName>(S)-2-amino-3-(beta-D-glucopyranosyloxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0397</Id>
			<Name>O-glucosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00804</Id>
			<Name>O-glucosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BGC</Id>
			<Name>beta-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">BGC</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0401</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O3-beta-glucosylated L-serine.</Description>
		<SystematicName>(S)-2-amino-3-(beta-D-glucopyranosyloxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0397</Id>
			<Name>O-glucosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00804</Id>
			<Name>O-glucosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GLC</Id>
			<Name>alpha-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GLC</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0402</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O3-galactosylserine.</Description>
		<SystematicName>(S)-2-amino-3-(alpha-D-galactopyranosyloxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0400</Id>
			<Name>O-galactosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00808</Id>
			<Name>O-glucosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GLA</Id>
			<Name>alpha-D-galactopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GLA</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0403</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O3-galactosylserine.</Description>
		<SystematicName>(S)-2-amino-3-(alpha-D-galactopyranosyloxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0400</Id>
			<Name>O-galactosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00808</Id>
			<Name>O-glucosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GAL</Id>
			<Name>beta-D-galactopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GAL</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0404</Id>
		<Description>A protein modification that effectively converts an L-serine residue to an O-fucosylserine.</Description>
		<SystematicName>(S)-2-amino-3-(alpha-6-deoxy-D-galactopyranosyloxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0404</Id>
			<Name>O-fucosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00812</Id>
			<Name>O-fucosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FCA</Id>
			<Name>alpha-D-fucose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">FCA</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0405</Id>
		<Description>A protein modification that effectively converts an L-serine residue to an O-fucosylserine.</Description>
		<SystematicName>(S)-2-amino-3-(alpha-6-deoxy-D-galactopyranosyloxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0404</Id>
			<Name>O-fucosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00812</Id>
			<Name>O-fucosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FCB</Id>
			<Name>beta-D-fucose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">FCB</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0406</Id>
		<Description>A protein modification that effectively forms a O3-xylosylserine.</Description>
		<SystematicName>(S)-2-amino-3-(alpha-D-xylopyranosyloxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0406</Id>
			<Name>O-xylosyl-L-serine</Name>
			<Status>deprecated</Status>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00814</Id>
			<Name>O-xylosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>XYP</Id>
			<Name>beta-D-xylopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">XYP</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0407</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O3-mannosylserine.</Description>
		<SystematicName>(S)-2-amino-3-(alpha-D-mannopyranosyloxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0402</Id>
			<Name>O-mannosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00810</Id>
			<Name>O-mannosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MAN</Id>
			<Name>alpha-D-mannopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">MAN</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0408</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O3-mannosylserine.</Description>
		<SystematicName>(S)-2-amino-3-(alpha-D-mannopyranosyloxy)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0402</Id>
			<Name>O-mannosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00810</Id>
			<Name>O-mannosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BMA</Id>
			<Name>beta-D-mannopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">BMA</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0409</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O-D-glucuronosyl-L-serine.</Description>
		<SystematicName>(2S)-2-amino-3-(beta-D-glucopyranuronosyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0291</Id>
			<Name>O-D-glucuronosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00296</Id>
			<Name>O-D-glucuronosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GCU</Id>
			<Name>alpha-D-glucopyranuronic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GCU</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0410</Id>
		<Description>A protein modification that effectively converts an L-serine residue to O-D-glucuronosyl-L-serine.</Description>
		<SystematicName>(2S)-2-amino-3-(beta-D-glucopyranuronosyl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0291</Id>
			<Name>O-D-glucuronosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00296</Id>
			<Name>O-D-glucuronosyl-L-serine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BDP</Id>
			<Name>beta-D-glucopyranuronic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">SER</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">BDP</Id>
			</Component>
			<Bond>
				<Atom component="1">OG</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0411</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminoglucosyl)-L-threonine.</Description>
		<SystematicName>(2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxyglucopyranosyloxy)butanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0399</Id>
			<Name>O-(N-acetylamino)glucosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00806</Id>
			<Name>O-(N-acetylamino)glucosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NAG</Id>
			<Name>N-acetyl-D-glucosamine</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">NAG</Id>
			</Component>
			<Bond>
				<Atom component="1">OG1</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0412</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminoglucosyl)-L-threonine.</Description>
		<SystematicName>(2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxyglucopyranosyloxy)butanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0399</Id>
			<Name>O-(N-acetylamino)glucosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00806</Id>
			<Name>O-(N-acetylamino)glucosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>NDG</Id>
			<Name>2-(acetylamino)-2-deoxy-A-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">NDG</Id>
			</Component>
			<Bond>
				<Atom component="1">OG1</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0413</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to O-glucosylated L-threonine.</Description>
		<SystematicName>O-glucosyl-L-threonine</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BGC</Id>
			<Name>beta-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">BGC</Id>
			</Component>
			<Bond>
				<Atom component="1">OG1</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0414</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to O-glucosylated L-threonine.</Description>
		<SystematicName>O-glucosyl-L-threonine</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GLC</Id>
			<Name>alpha-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GLC</Id>
			</Component>
			<Bond>
				<Atom component="1">OG1</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0415</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to O3-galactosylthreonine.</Description>
		<SystematicName>(2S,3R)-2-amino-3-(alpha-D-galactopyranosyloxy)butanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0401</Id>
			<Name>O-galactosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00809</Id>
			<Name>O-galactosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GLA</Id>
			<Name>alpha-D-galactopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GLA</Id>
			</Component>
			<Bond>
				<Atom component="1">OG1</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0416</Id>
		<Description>A protein modification that effectively converts an L-threonine residue to O3-galactosylthreonine.</Description>
		<SystematicName>(2S,3R)-2-amino-3-(alpha-D-galactopyranosyloxy)butanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0401</Id>
			<Name>O-galactosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00809</Id>
			<Name>O-galactosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GAL</Id>
			<Name>beta-D-galactopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GAL</Id>
			</Component>
			<Bond>
				<Atom component="1">OG1</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0417</Id>
		<Description>A protein modification that effectively converts an threonine residue to an O-fucosylthreonine.</Description>
		<SystematicName>(2S,3R)-2-amino-3-(alpha-6-deoxy-D-galactopyranosyloxy)butanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0405</Id>
			<Name>O-fucosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00813</Id>
			<Name>O-fucosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FCA</Id>
			<Name>alpha-D-fucose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">FCA</Id>
			</Component>
			<Bond>
				<Atom component="1">OG1</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0418</Id>
		<Description>A protein modification that effectively converts an threonine residue to an O-fucosylthreonine.</Description>
		<SystematicName>(2S,3R)-2-amino-3-(alpha-6-deoxy-D-galactopyranosyloxy)butanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0405</Id>
			<Name>O-fucosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00813</Id>
			<Name>O-fucosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>FCB</Id>
			<Name>beta-D-fucose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">FCB</Id>
			</Component>
			<Bond>
				<Atom component="1">OG1</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0419</Id>
		<Description>A protein modification that effectively forms a O3-mannosylthreonine</Description>
		<SystematicName>(2S,3R)-2-amino-3-(alpha-D-mannopyranosyloxy)butanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0403</Id>
			<Name>O-mannosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00811</Id>
			<Name>O-mannosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MAN</Id>
			<Name>alpha-D-mannopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">MAN</Id>
			</Component>
			<Bond>
				<Atom component="1">OG1</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0420</Id>
		<Description>A protein modification that effectively forms a O3-mannosylthreonine</Description>
		<SystematicName>(2S,3R)-2-amino-3-(alpha-D-mannopyranosyloxy)butanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0403</Id>
			<Name>O-mannosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00811</Id>
			<Name>O-mannosyl-L-threonine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BMA</Id>
			<Name>beta-D-mannopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">THR</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">BMA</Id>
			</Component>
			<Bond>
				<Atom component="1">OG1</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0421</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine.</Description>
		<SystematicName>(S)-2-amino-3-(4-alpha-glucopyranosyloxy)phenylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0157</Id>
			<Name>O4'-glucosyl-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00166</Id>
			<Name>O4'-glucosyl-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BGC</Id>
			<Name>beta-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYR</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">BGC</Id>
			</Component>
			<Bond>
				<Atom component="1">OH</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0422</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine.</Description>
		<SystematicName>(S)-2-amino-3-(4-alpha-glucopyranosyloxy)phenylpropanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0157</Id>
			<Name>O4'-glucosyl-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00166</Id>
			<Name>O4'-glucosyl-L-tyrosine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GLC</Id>
			<Name>alpha-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYR</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GLC</Id>
			</Component>
			<Bond>
				<Atom component="1">OH</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0423</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to O-galactosyl-tyrosine.</Description>
		<SystematicName>O-galactosyl-L-tyrosine</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GAL</Id>
			<Name>alpha-D-glucopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYR</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GAL</Id>
			</Component>
			<Bond>
				<Atom component="1">OH</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0424</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to O-galactosyl-tyrosine.</Description>
		<SystematicName>O-galactosyl-L-tyrosine</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GAL</Id>
			<Name>beta-D-galactopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYR</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GAL</Id>
			</Component>
			<Bond>
				<Atom component="1">OH</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0425</Id>
		<Description>A protein modification that effectively converts an L-tyrosine residue to O-galactosyl-tyrosine.</Description>
		<SystematicName>O-galactosyl-L-tyrosine</SystematicName>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GLA</Id>
			<Name>alpha-D-galactopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TYR</Id>
			</Component>			
			<Component component="2">
				<Id source="PDBCC">GLA</Id>
			</Component>
			<Bond>
				<Atom component="1">OH</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0426</Id>
		<Description>A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan.</Description>
		<SystematicName>(2S)-2-amino-3-(2-alpha-mannopyranosyl-1H-indol-3-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0217</Id>
			<Name>2'-alpha-mannosyl-L-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00222</Id>
			<Name>2'-alpha-mannosyl-L-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>MAN</Id>
			<Name>alpha-D-mannopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TRP</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">MAN</Id>
			</Component>
			<Bond>
				<Atom component="1">CD1</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0427</Id>
		<Description>A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan.</Description>
		<SystematicName>(2S)-2-amino-3-(2-alpha-mannopyranosyl-1H-indol-3-yl)propanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0217</Id>
			<Name>2'-alpha-mannosyl-L-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00222</Id>
			<Name>2'-alpha-mannosyl-L-tryptophan</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BMA</Id>
			<Name>beta-D-mannopyranose</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">TRP</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">BMA</Id>
			</Component>
			<Bond>
				<Atom component="1">CD1</Atom>
				<Atom component="2">C1</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0428</Id>
		<Description>A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine.</Description>
		<SystematicName>2-(glucuronoylamino)ethanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0058</Id>
			<Name>N-D-glucuronoyl-glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00067</Id>
			<Name>N-D-glucuronoylglycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>GCU</Id>
			<Name>alpha-D-glucopyranuronic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLY</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">GCU</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C6</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
	<Entry>
		<Id>0429</Id>
		<Description>A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine.</Description>
		<SystematicName>2-(glucuronoylamino)ethanoic acid</SystematicName>
		<CrossReference>
			<Source>RESID</Source>
			<Id>AA0058</Id>
			<Name>N-D-glucuronoyl-glycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PSI-MOD</Source>
			<Id>MOD:00067</Id>
			<Name>N-D-glucuronoylglycine</Name>
		</CrossReference>
		<CrossReference>
			<Source>PDBCC</Source>
			<Id>BDP</Id>
			<Name>beta-D-glucopyranuronic acid</Name>
		</CrossReference>
		<Condition>
			<Component component="1">
				<Id source="PDBCC">GLY</Id>
			</Component>
			<Component component="2">
				<Id source="PDBCC">BDP</Id>
			</Component>
			<Bond>
				<Atom component="1">N</Atom>
				<Atom component="2">C6</Atom>
			</Bond>
		</Condition>
		<Occurrence>natural</Occurrence>
		<Category>attachment</Category>
		<Keyword>glycoprotein</Keyword>
	</Entry>
</ProteinModifications>