2011-08-12 Added glycosylation entries 386-429 2011-07-26 Added PDBCC cross-references 0001 a protein modification that effectively forms a O3-xylosylserine. (S)-2-amino-3-(alpha-D-xylopyranosyloxy)propanoic acid RESID AA0406 O-xylosyl-L-serine deprecated PSI-MOD MOD:00814 O-xylosyl-L-serine PDBCC XYS xylopyranose SER XYS OG C1 natural attachment glycoprotein 0002 A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine. (S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)amino-4-oxobutanoic acid RESID AA0151 N4-(N-acetylamino)glucosyl-L-asparagine PSI-MOD MOD:00831 N4-(N-acetylamino)glucosyl-L-asparagine PDBCC NAG N-acetyl-D-glucosamine ASN NAG ND2 C1 natural attachment glycoprotein 0003 A protein modification that effectively converts an L-cysteine residue to S-phospho-L-cysteine. (R)-2-amino-3-(phosphonosulfanyl)propanoic acid PDBCC CSP S-phosphocysteine RESID AA0034 S-phospho-L-cysteine PSI-MOD MOD:00043 S-phospho-L-cysteine CSP natural modified residue phosphoprotein 0004 A protein modification that effectively converts an L-histidine residue to tele-phospho-L-histidine (Ntau-phospho-L-histidine, 1'-phospho-L-histidine). (S)-2-amino-3-(1-phosphono-1H-imidazol-4-yl)propanoic acid PDBCC NEP N1-phosphonohistidine RESID AA0035 1'-phospho-L-histidine PSI-MOD MOD:00044 1'-phospho-L-histidine NEP natural modified residue phosphoprotein 0005 A protein modification that effectively converts an L-histidine residue to pros-phospho-L-histidine (Npi-phospho-L-histidine, 3'-phospho-L-histidine). (S)-2-amino-3-(3-phosphono-3H-imidazol-4-yl)propanoic acid PDBCC HIP ND1-phosphonohistidine RESID AA0036 3'-phospho-L-histidine PSI-MOD MOD:00045 3'-phospho-L-histidine HIP natural modified residue phosphohistidine phosphoprotein 0006 A protein modification that effectively converts an L-serine residue to O-phospho-L-serine. (S)-2-amino-3-(phosphonooxy)propanoic acid PDBCC SEP phosphoserine RESID AA0037 O-phospho-L-serine PSI-MOD MOD:00046 O-phospho-L-serine SEP natural modified residue phosphoprotein 0007 A protein modification that effectively converts an L-threonine residue to O-phospho-L-threonine. (2S,3R)-2-amino-3-phosphonooxybutanoic acid PDBCC TPO phosphothreonine RESID AA0038 O-phospho-L-threonine PSI-MOD MOD:00047 O-phospho-L-threonine TPO natural modified residue phosphoprotein 0008 A protein modification that effectively converts an L-tyrosine residue to O4'-phospho-L-tyrosine. (2S)-2-amino-3-(4-phosphonooxyphenyl)propanoic acid PDBCC PTR O-phosphotyrosine RESID AA0039 O4'-phospho-L-tyrosine PSI-MOD MOD:00048 O4'-phospho-L-tyrosine PTR natural modified residue phosphoprotein 0009 A protein modification that effectively converts an L-glutamine residue to N-acetyl-L-glutamine. (S)-2-acetamido-5-pentanediamic acid PDBCC ACE acetyl group RESID AA0045 N-acetyl-L-glutamine deprecated PSI-MOD MOD:00054 N-acetyl-L-glutamine GLN N ACE N C natural attachment acetylated amino end 0010 A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine. (2S)-2-acetamido-4-(methylsulfanyl)butanoic acid RESID AA0049 N-acetyl-L-methionine PSI-MOD MOD:00058 N-acetyl-L-methionine PDBCC ACE acetyl group MET N ACE N C natural attachment thioether bond acetylated amino end 0011 A protein modification that effectively converts an L-lysine residue to N6-acetyl-L-lysine. (2S)-2-amino-6-acetamidohexanoic acid PDBCC ALY N(6)-acetyllysine RESID AA0055 N6-acetyl-L-lysine PSI-MOD MOD:00064 N6-acetyl-L-lysine ALY natural modified residue acetyllysine 0012 A protein modification that effectively converts an L-tyrosine residue to O4'-sulfo-L-tyrosine. (S)-2-amino-3-(4-sulfooxyphenyl)propanoic acid PDBCC TYS O-sulfo-L-tyrosine RESID AA0172 O4'-sulfo-L-tyrosine PSI-MOD MOD:00181 O4'-sulfo-L-tyrosine TYS natural modified residue sulfoprotein 0013 A protein modification that effectively converts an L-lysine residue to N6-methyl-L-lysine. (S)-2-amino-6-methylaminohexanoic acid PDBCC MLZ N-methyl-lysine RESID AA0076 N6-methyl-L-lysine PSI-MOD MOD:00085 N6-methyl-L-lysine MLZ natural modified residue methylated amino acid 0014 A protein modification that effectively converts an L-arginine residue to 5-methyl-L-arginine. (2S,5S)-2-amino-5-carbamimidamidohexanoic acid PDBCC AGM 5-methyl-arginine RESID AA0272 5-methyl-L-arginine PSI-MOD MOD:00277 5-methyl-L-arginine AGM natural modified residue methylated amino acid 0015 A protein modification that effectively converts an L-lysine residue to N6,N6,N6-trimethyl-L-lysine. (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium PDBCC M3L N-trimethyllysine RESID AA0074 N6,N6,N6-trimethyl-L-lysine PSI-MOD MOD:00083 N6,N6,N6-trimethyl-L-lysine M3L natural modified residue methylated amino acid 0016 A protein modification that effectively converts an L-methionine residue to N-methyl-L-methionine. (S)-2-methylamino-4-(methylsulfanyl)butanoic acid PDBCC MME N-methyl methionine RESID AA0064 N-methyl-L-methionine PSI-MOD MOD:00073 N-methyl-L-methionine MME N natural modified residue thioether bond methylated amino acid 0017 A protein modification that effectively converts an L-proline residue to 4-hydroxy-L-proline. (2S,4R)-4-hydroxypyrrolidine-2-carboxylic acid PDBCC HYP 4-hydroxyproline RESID AA0030 4-hydroxy-L-proline PSI-MOD MOD:00039 4-hydroxy-L-proline HYP natural modified residue hydroxylation 0018 A protein modification that effectively cross-links two L-cysteine residues to form L-cystine. (R,R)-3,3'-disulfane-1,2-diylbis(2-aminopropanoic acid) RESID AA0025 L-cystine PSI-MOD MOD:00034 L-cystine (cross-link) CYS CYS SG SG natural crosslink2 redox-active center disulfide bond 0019 A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl disulfide. (R)-2-amino-3-(methyldisulfanediyl)propanoic acid PDBCC SCH S-Methyl-thio-cysteine RESID AA0101 L-cysteine methyl disulfide PSI-MOD MOD:00110 L-cysteine methyl disulfide SCH hypothetical modified residue disulfide bond 0020 A protein modification that effectively converts three L-cysteine residues and a three-iron four-sulfur cluster to tris-L-cysteinyl triiron tetrasulfide. mu3-sulfido-tri-mu-sulfidotris(cysteinato-kappaS-iron) RESID AA0139 tris-L-cysteinyl triiron tetrasulfide PSI-MOD MOD:00148 tris-L-cysteinyl triiron tetrasulfide PDBCC F3S Fe3-S4 cluster CYS CYS CYS F3S SG FE1 SG FE3 SG FE4 natural crosslink3 3Fe-4S iron-sulfur protein metalloprotein 0021 A protein modification that effectively converts four L-cysteine residues and a two-iron two-sulfur cluster to tetrakis-L-cysteinyl diiron disulfide. tetrakis(cysteinato)-1kappaS,1kappaS,2kappaS,2kappaS-di-mu-sulfidodiiron RESID AA0137 tetrakis-L-cysteinyl diiron disulfide PSI-MOD MOD:00146 tetrakis-L-cysteinyl diiron disulfide PDBCC FES Fe2/S2 (inorganic) cluster CYS CYS CYS CYS FES SG FE1 SG FE1 SG FE2 SG FE2 natural crosslink4 2Fe-2S iron-sulfur protein metalloprotein 0022 A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification. (S)-2-formylamino-4-(methylsulfanyl)butanoic acid PDBCC FME N-formylmethionine RESID AA0021 N-formyl-L-methionine PSI-MOD MOD:00030 N-formyl-L-methionine FME N natural modified residue thioether bond blocked amino end formylation pretranslational modification 0023 A protein modification that effectively converts a source amino acid residue to an L-selenocysteine, a natural pretranslational modification. (R)-2-amino-3-selanylpropanoic acid PDBCC CSE selenocysteine RESID AA0022 L-selenocysteine PSI-MOD MOD:00031 L-selenocysteine residue CSE natural modified residue pretranslational modification selenium selenocysteine 0024 A protein modification that effectively converts an L-asparagine residue to (2S,3R)-3-hydroxyasparagine. (2S,3R)-2-amino-3-hydroxy-4-butanediamic acid PDBCC AHB beta-hydroxyasparagine RESID AA0026 (2S,3R)-3-hydroxyasparagine PSI-MOD MOD:00035 (2S,3R)-3-hydroxyasparagine AHB natural modified residue hydroxylation 0025 A protein modification that effectively converts an L-aspartic acid residue to (2S,3R)-3-hydroxyaspartic acid. (2S,3R)-2-amino-3-hydroxybutanedioic acid PDBCC BHD beta-hydroxyaspartic acid RESID AA0027 (2S,3R)-3-hydroxyaspartic acid PSI-MOD MOD:00036 (2S,3R)-3-hydroxyaspartic acid BHD natural modified residue hydroxylation 0026 A protein modification that effectively converts an L-lysine residue to 5-hydroxy-L-lysine. (2S,5R)-2,6-diamino-5-hydroxyhexanoic acid PDBCC LYZ 5-hydroxylysine RESID AA0028 5-hydroxy-L-lysine PSI-MOD MOD:00037 5-hydroxy-L-lysine LYZ natural modified residue hydroxylation 0027 A protein modification that effectively converts an L-proline residue to 3-hydroxy-L-proline. (2S,3S)-3-hydroxypyrrolidine-2-carboxylic acid PDBCC HY3 3-hydroxyproline RESID AA0029 3-hydroxy-L-proline PSI-MOD MOD:00038 3-hydroxy-L-proline HY3 natural modified residue hydroxylation 0028 A protein modification that effectively converts an L-glutamine residue to 2-pyrrolidone-5-carboxylic acid. (S)-5-oxo-2-pyrrolidinecarboxylic acid PDBCC PCA pyroglutamic acid RESID AA0031 2-pyrrolidone-5-carboxylic acid PSI-MOD MOD:00040 2-pyrrolidone-5-carboxylic acid (Gln) PCA natural modified residue blocked amino end pyroglutamic acid 0029 A protein modification that effectively converts an L-glutamic acid residue to L-gamma-carboxyglutamic acid. (S)-3-amino-1,1,3-propanetricarboxylic acid PDBCC CGU gamma-carboxy-glutamic acid RESID AA0032 L-gamma-carboxyglutamic acid PSI-MOD MOD:00041 L-gamma-carboxyglutamic acid CGU natural modified residue carboxyglutamic acid 0030 A protein modification that effectively converts an L-aspartic acid residue to L-aspartic 4-phosphoric anhydride. (2S)-2-amino-4-oxo-4-(phosphonooxy)butanoic acid PDBCC PHD aspartyl phosphate RESID AA0033 L-aspartic 4-phosphoric anhydride PSI-MOD MOD:00042 L-aspartic 4-phosphoric anhydride PHD natural modified residue phosphoprotein 0031 A protein modification that effectively converts an L-histidine residue to diphthamide. (2R)-1-amino-4-(4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-2-yl)-N,N,N-trimethyl-1-oxobutan-2-aminium PDBCC DDE {3-[4-(2-amino-2-carboxy-ethyl)-1H-imidazol-2-yl]-1-carbamoyl-propyl}-trimethyl-ammonium RESID AA0040 2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine PSI-MOD MOD:00049 2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine DDE natural modified residue diphthamide 0032 A protein modification that effectively converts an L-cysteine residue to S-acetyl-L-cysteine. (R)-2-amino-3-(acetylsulfanyl)propanoic acid PDBCC SCY S-acetyl-cysteine RESID AA0056 S-acetyl-L-cysteine PSI-MOD MOD:00065 S-acetyl-L-cysteine SCY natural modified residue thioester bond 0033 A protein modification that effectively converts a glycine residue to N-myristoylglycine. (tetradecanoylamino)ethanoic acid RESID AA0059 N-myristoyl-glycine PSI-MOD MOD:00068 N-myristoylglycine PDBCC MYR myristic acid GLY MYR N C1 natural attachment blocked amino end lipoprotein myristoylation 0034 A protein modification that effectively converts an L-alanine residue to N-methyl-L-alanine. (S)-2-methylaminopropanoic acid PDBCC MAA N-methyl-L-alanine RESID AA0061 N-methyl-L-alanine PSI-MOD MOD:00070 N-methyl-L-alanine MAA natural modified residue methylated amino end 0035 A protein modification that effectively converts an L-phenylalanine residue to N-methyl-L-phenylalanine. (S)-2-methylamino-3-phenylpropanoic acid PDBCC MEA N-methylphenylalanine RESID AA0065 N-methyl-L-phenylalanine PSI-MOD MOD:00074 N-methyl-L-phenylalanine MEA natural modified residue methylated amino end 0036 A protein modification that effectively converts an L-proline residue to N,N-dimethyl-L-proline. (S)-2-carboxy-1,1-dimethylpyrrolidinium RESID AA0066 N,N-dimethyl-L-proline PSI-MOD MOD:00075 N,N-dimethyl-L-proline PDBCC PBE 1,1-dimethyl-prolinium PBE natural modified residue blocked amino end methylated amino end 0037 A protein modification that effectively converts an L-arginine residue to N(omega),N'(omega)-dimethyl-L-arginine. (S)-2-amino-5-[((methylamino)(methylimino)methyl)amino]pentanoic acid PDBCC 2MR N3,N4-dimethylarginine RESID AA0067 omega-N,omega-N'-dimethyl-L-arginine PSI-MOD MOD:00076 omega-N,omega-N'-dimethyl-L-arginine 2MR natural modified residue methylated amino acid 0038 A protein modification that effectively converts an L-arginine residue to N(omega),N(omega)-dimethyl-L-arginine. (S)-2-amino-5-([(dimethylamino)(imino)methyl]amino)pentanoic acid PDBCC DA2 NG,NG-dimethyl-L-arginine RESID AA0068 omega-N,omega-N-dimethyl-L-arginine PSI-MOD MOD:00077 omega-N,omega-N-dimethyl-L-arginine DA2 natural modified residue methylated amino acid 0039 A protein modification that effectively converts an L-asparagine residue to N4-methyl-L-asparagine. (S)-2-amino-N4-methylbutanediamic acid PDBCC MEN N-methyl asparagine RESID AA0070 N4-methyl-L-asparagine PSI-MOD MOD:00079 N4-methyl-L-asparagine MEN natural modified residue methylated amino acid 0040 A protein modification that effectively converts an L-glutamine residue to N5-methyl-L-glutamine. (2S)-2-amino-5-methylamino-5-oxopentanoic acid PDBCC MEQ N5-methylglutamine RESID AA0071 N5-methyl-L-glutamine PSI-MOD MOD:00080 N5-methyl-L-glutamine MEQ natural modified residue methylated amino acid 0041 A protein modification that effectively converts an L-histidine residue to pros-methyl-L-histidine (N-pi-methyl-L-histidine, 3'-methyl-L-histidine). (S)-2-amino-3-(3-methyl-3H-imidazol-4-yl)propanoic acid PDBCC MHS N1-methylated histidine RESID AA0073 3'-methyl-L-histidine PSI-MOD MOD:00082 3'-methyl-L-histidine MHS natural modified residue methylated amino acid 0042 A protein modification that effectively converts an L-lysine residue to N6,N6-dimethyl-L-lysine. (S)-2-amino-6-dimethylaminohexanoic acid PDBCC MLY N-dimethyl-lysine RESID AA0075 N6,N6-dimethyl-L-lysine PSI-MOD MOD:00084 N6,N6-dimethyl-L-lysine MLY natural modified residue methylated amino acid 0043 A protein modification that effectively converts an L-arginine residue to L-arginine amide. (S)-2-amino-5-carbamimidamidopentanamide PDBCC AAR arginineamide RESID AA0082 L-arginine amide PSI-MOD MOD:00091 L-arginine amide AAR natural modified residue amidated carboxyl end 0044 A protein modification that effectively converts an L-cysteine residue to L-cysteine amide. (R)-2-amino-3-sulfanylpropanamide PDBCC CY3 2-amino-3-mercapto-propionamide RESID AA0085 L-cysteine amide PSI-MOD MOD:00094 L-cysteine amide CY3 natural modified residue amidated carboxyl end 0045 A protein modification that effectively converts an L-leucine residue to L-leucine amide. (S)-2-amino-4-methylpentanamide PDBCC CLE leucine amide RESID AA0091 L-leucine amide PSI-MOD MOD:00100 L-leucine amide CLE C natural modified residue amidated carboxyl end 0046 A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide. (S)-2-amino-3-phenylpropanamide PDBCC NFA phenylalanine amide RESID AA0094 L-phenylalanine amide PSI-MOD MOD:00103 L-phenylalanine amide NFA C natural modified residue amidated carboxyl end 0047 A protein modification that effectively converts an L-proline residue to L-proline amide. (S)-pyrrolidine-2-carboxamide PDBCC LPD L-prolinamide RESID AA0095 L-proline amide PSI-MOD MOD:00104 L-proline amide LPD C natural modified residue amidated carboxyl end 0048 A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide. (S)-2-amino-3-(4-hydoxyphenyl)propanamide PDBCC TYC L-tyrosineamide RESID AA0099 L-tyrosine amide PSI-MOD MOD:00108 L-tyrosine amide TYC C natural modified residue amidated carboxyl end 0049 A protein modification that effectively converts an L-valine residue to L-valine amide. (S)-2-amino-3-methylbutanamide PDBCC VLM valinylamine RESID AA0100 L-valine amide PSI-MOD MOD:00109 L-valine amide VLM C natural modified residue amidated carboxyl end 0050 A protein modification that effectively converts an L-cysteine residue to L-cysteine methyl ester. methyl (2R)-2-amino-3-sulfanylpropanoate PDBCC CMT O-methylcysteine RESID AA0105 L-cysteine methyl ester PSI-MOD MOD:00114 L-cysteine methyl ester CMT C natural modified residue methylated carboxyl end 0051 A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine. (R)-2-amino-3-(hexadecanoylsulfanyl)propanoic acid PDBCC P1L S-palmitoyl-L-cysteine RESID AA0106 S-palmitoyl-L-cysteine PSI-MOD MOD:00115 S-palmitoyl-L-cysteine P1L natural modified residue lipoprotein palmitoylation thioester bond 0052 A protein modification that effectively converts an L-cysteine residue to S-palmitoyl-L-cysteine. (R)-2-amino-3-(hexadecanoylsulfanyl)propanoic acid RESID AA0106 S-palmitoyl-L-cysteine PSI-MOD MOD:00115 S-palmitoyl-L-cysteine PDBCC PLM palmitic acid CYS PLM SG C1 natural attachment lipoprotein palmitoylation thioester bond 0053 A protein modification that effectively converts an L-lysine residue to N6-carboxy-L-lysine. (S)-2-amino-6-(carboxyamino)hexanoic acid PDBCC KCX lysine NZ-carboxylic acid RESID AA0114 N6-carboxy-L-lysine PSI-MOD MOD:00123 N6-carboxy-L-lysine KCX natural modified residue 0054 A protein modification that effectively converts an L-lysine residue to N6-1-carboxyethyl-L-lysine. (S,S)-2-amino-6-(1-carboxyethyl)aminohexanoic acid PDBCC MCL NZ-(1-carboxyethyl)-lysine RESID AA0115 N6-1-carboxyethyl-L-lysine PSI-MOD MOD:00124 N6-1-carboxyethyl-L-lysine MCL natural modified residue 0055 A protein modification that effectively converts an L-lysine residue to N6-biotinyl-L-lysine. (S)-2-amino-6-[5-((3aS,4S,6aR)-hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl]aminohexanoic acid RESID AA0117 N6-biotinyl-L-lysine PSI-MOD MOD:00126 N6-biotinyl-L-lysine PDBCC BTN biotin LYS BTN NZ C11 natural attachment biotin 0056 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. (S,S)-2-amino-6-[(4-amino-4-carboxybutanoyl)amino]hexanoic acid RESID AA0124 N6-(L-isoglutamyl)-L-lysine PSI-MOD MOD:00133 N6-(L-isoglutamyl)-L-lysine (Gln) LYS GLN NZ CD natural crosslink2 isopeptide bond 0057 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. (S,S)-2-amino-6-[(4-amino-4-carboxybutanoyl)amino]hexanoic acid RESID AA0124 N6-(L-isoglutamyl)-L-lysine PSI-MOD MOD:01484 N6-(L-isoglutamyl)-L-lysine (Glu) LYS GLU NZ CD natural crosslink2 isopeptide bond 0058 A protein modification that effectively crosslinks an L-lysine residue and a glycine residue by an isopeptide bond to form N6-glycyl-L-lysine. (S)-2-amino-6-[(aminoacetyl)amino]hexanoic acid RESID AA0125 N6-glycyl-L-lysine PSI-MOD MOD:00134 N6-glycyl-L-lysine LYS GLY C NZ C natural crosslink2 blocked carboxyl end isopeptide bond 0059 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. (S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid RESID AA0126 N-(L-isoaspartyl)-glycine PSI-MOD MOD:00135 N-(L-isoaspartyl)glycine GLY N ASN N CG natural crosslink2 blocked carboxyl end isopeptide bond 0060 A protein modification that effectively crosslinks L-aspartic acid and L-cysteine residues via an isopeptide bond to form N-(L-isoaspartyl)-L-cysteine. (S)-2-amino-4-((R)-1-carboxy-2-sulfanylethyl)amino-4-oxobutanoic acid RESID AA0216 N-(L-isoaspartyl)-L-cysteine PSI-MOD MOD:00221 N-(L-isoaspartyl)-L-cysteine CYS N ASP N CG natural crosslink2 blocked amino end isopeptide bond 0061 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. (S,S)-2-amino-6-[(3-amino-3-carboxypropanoyl)amino]hexanoic acid RESID AA0294 N6-(L-isoaspartyl)-L-lysine PSI-MOD MOD:00299 N6-(L-isoaspartyl)-L-lysine LYS ASN NZ CG natural crosslink2 isopeptide bond 0062 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. (S)-2-amino-5-(carboxymethyl)amino-5-oxopentanoic acid RESID AA0360 N-(L-isoglutamyl)-glycine PSI-MOD MOD:00365 N-(L-isoglutamyl)-glycine GLU GLY N CD N natural crosslink2 blocked amino end isopeptide bond 0063 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. (2S)-2-amino-6-([(2S,3R)-2-amino-3-hydroxybutanoyl]amino)hexanoic acid RESID AA0440 N6-(L-threonyl)-L-lysine PSI-MOD MOD:00924 N6-(L-threonyl)-L-lysine LYS THR C NZ C natural crosslink2 blocked amino end isopeptide bond 0064 A protein modification that effectively converts an L-lysine residue to N6-lipoyl-L-lysine. (S)-2-amino-6-[5-((R)-1,2-dithiolan-3-yl)pentanamido]hexanoic acid RESID AA0118 N6-lipoyl-L-lysine PSI-MOD MOD:00127 N6-lipoyl-L-lysine PDBCC LPA lipoic acid LYS LPA NZ C1 natural attachment lipoamide redox-active center 0065 A protein modification that effectively converts an L-lysine residue to N6-pyridoxal phosphate-L-lysine. (S)-2-amino-6-[([3-hydroxy-2-methyl-5-phosphonooxymethylpyridin-4-yl]methylidene)amino]hexanoic acid PDBCC LLP 2-lysine(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethane) RESID AA0119 N6-pyridoxal phosphate-L-lysine PSI-MOD MOD:00128 N6-pyridoxal phosphate-L-lysine LLP natural modified residue phosphoprotein pyridoxal phosphate 0066 A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal. (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 PDBCC LYR 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 RESID AA0120 N6-retinylidene-L-lysine PSI-MOD MOD:00129 N6-retinylidene-L-lysine LYR natural modified residue chromoprotein retinal 0067 A protein modification that effectively converts an L-lysine residue to N6-retinylidene-L-lysine, the adduct of retinal. (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 RESID AA0120 N6-retinylidene-L-lysine PSI-MOD MOD:00129 N6-retinylidene-L-lysine PDBCC RET retinal LYS RET NZ C15 natural attachment chromoprotein retinal 0068 A protein modification that effectively converts an L-lysine residue to L-allysine. (S)-2-amino-6-oxohexanoic acid RESID AA0121 L-allysine PSI-MOD MOD:00130 L-allysine PDBCC DO2 5,5-dihydroxy-6-oxo-L-norleucine LYS DO2 NZ CE natural attachment 0069 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. (2S)-2-amino-6-((2Xi)-2-amino-2-carboxyethylamino)hexanoic acid RESID AA0123 L-lysinoalanine PSI-MOD MOD:00132 L-lysinoalanine LYS SER NZ CB natural crosslink2 0070 A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycocyanobilin. (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 RESID AA0131 S-phycocyanobilin-L-cysteine PSI-MOD MOD:00140 S-phycocyanobilin-L-cysteine PDBCC CYC phycocyanobilin CYS CYC SG CAC natural attachment chromoprotein phycocyanobilin thioether bond 0071 A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoerythrobilin. (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 RESID AA0132 S-phycoerythrobilin-L-cysteine PSI-MOD MOD:00141 S-phycoerythrobilin-L-cysteine PDBCC PEB phycoerythrobilin CYS PEB SG * natural attachment chromoprotein phycoerythrobilin thioether bond 0072 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. [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 RESID AA0134 heme-bis-L-cysteine PSI-MOD MOD:00143 heme-bis-L-cysteine PDBCC HEM protoporphyrin IX containing Fe CYS CYS HEM SG CBB SG CBC natural crosslink2 chromoprotein heme iron metalloprotein thioether bond 0073 A protein modification that effectively converts four L-cysteine residues iron atom to tetrakis-L-cysteinyl iron. tetrakis(cysteinato)-1kappaS,2kappaS,3kappaS,4kappaS-iron RESID AA0136 tetrakis-L-cysteinyl iron PSI-MOD MOD:00145 tetrakis-L-cysteinyl iron CYS CYS CYS CYS FE SG FE SG FE SG FE SG FE natural crosslink4 iron metalloprotein covered in metal coordination 0074 A protein modification that effectively converts four L-cysteine residues and a four-iron four-sulfur cluster to tetrakis-L-cysteinyl tetrairon tetrasulfide. tetrakis(cysteinato)-1kappaS,2kappaS,3kappaS,4kappaS-tetra-mu3-sulfido-tetrahedro-tetrairon RESID AA0140 tetrakis-L-cysteinyl tetrairon tetrasulfide PSI-MOD MOD:00149 tetrakis-L-cysteinyl tetrairon tetrasulfide PDBCC SF4 iron/sulfur cluster CYS CYS CYS CYS SF4 SG FE1 SG FE2 SG FE3 SG FE4 natural crosslink4 4Fe-4S iron-sulfur protein metalloprotein 0075 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. RESID AA0141 L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide PSI-MOD MOD:00150 L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide PDBCC CFM Fe-Mo-S cluster PDBCC HCA 3-hydroxy-3-carboxy-adipic acid CYS HIS CFM HCA SG FE1 ND1 MO1 MO1 O5 MO1 * natural crosslink2 iron-sulfur protein metalloprotein molybdenum 0076 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. RESID AA0141 L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide PSI-MOD MOD:00150 L-cysteinyl-L-histidino-homocitryl molybdenum heptairon nonasulfide PDBCC CFN Fe(7)-Mo-S(9)-N cluster PDBCC HCA 3-hydroxy-3-carboxy-adipic acid CYS HIS CFN HCA SG FE1 ND1 MO1 MO1 O5 MO1 O7 natural crosslink2 iron-sulfur protein metalloprotein molybdenum 0077 modification from UniMod and Resid 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 RESID AA0142 L-cysteinyl molybdopterin PSI-MOD MOD:00151 L-cysteinyl molybdopterin PDBCC MTQ (molybdopterin-S,S)-dioxo-thio-molybdenum(VI) CYS MTQ SG MOM1 natural attachment metalloprotein molybdenum molybdopterin phosphoprotein 0078 A protein modification that effectively converts an L-cysteine residue to S'-(8alpha-FAD)-L-cystine. (R)-2-amino-3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]sulfanylpropanoic acid RESID AA0143 S-(8alpha-FAD)-L-cysteine PSI-MOD MOD:00152 S-(8alpha-FAD)-L-cysteine PDBCC FAD flavin-adenine dinucleotide CYS FAD SG C8M natural attachment phosphoprotein FAD flavoprotein thioether bond 0079 A protein modification that effectively converts an L-histidine residue to 3'-(8alpha-FAD)-L-histidine. (S)-2-amino-3-(3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid RESID AA0144 3'-(8alpha-FAD)-L-histidine PSI-MOD MOD:00153 3'-(8alpha-FAD)-L-histidine PDBCC FAD flavin-adenine dinucleotide HIS FAD ND1 C8M natural attachment phosphoprotein FAD flavoprotein 0080 A protein modification that effectively converts an L-tyrosine residue to O4'-(8alpha-FAD)-L-tyrosine. (S)-2-amino-3-(4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxyphenyl)propanoic acid RESID AA0145 O4'-(8alpha-FAD)-L-tyrosine PSI-MOD MOD:00154 O4'-(8alpha-FAD)-L-tyrosine PDBCC FAD flavin-adenine dinucleotide TYR FAD OH C8M natural attachment phosphoprotein FAD flavoprotein 0081 A protein modification that effectively converts an L-tyrosine residue to an L-2',4',5'-topaquinone. (S)-2-amino-3-(5-hydroxy-2,5-cyclohexadien-1,4-dion-2-yl)propanoic acid PDBCC TPQ 5-(2-carboxy-2-aminoethyl)-2-hydroxy-1,4-benzoquinone RESID AA0147 L-2',4',5'-topaquinone PSI-MOD MOD:00156 oxidation of tyrosine to L-2',4',5'-topaquinone TPQ natural modified residue quinoprotein topaquinone 0082 A protein modification that effectively converts an L-tryptophan residue to an L-tryptophan quinone. (S)-3-(2-amino-2-carboxyethyl)-6,7-indolinedione PDBCC TRQ 2-amino-3-(6,7-dioxo-6,7-dihydro-1H-indol-3-yl)-propionic acid RESID AA0148 L-tryptophyl quinone PSI-MOD MOD:00157 oxidation of tryptophan to L-tryptophyl quinone TRQ natural modified residue quinoprotein 0083 A protein modification that effectively cross-links two L-tryptophan residues by a carbon-carbon bond to form 4'-(L-tryptophan)-L-tryptophyl quinone. (S,S)-3-(2-amino-2-carboxyethyl)-4-[3-(2-amino-2-carboxyethyl)-1H-indol-2-yl]-6,7-indolinedione RESID AA0149 4'-(L-tryptophan)-L-tryptophyl quinone PSI-MOD MOD:00158 4'-(L-tryptophan)-L-tryptophyl quinone TRP TRP CD1 CE3 natural crosslink2 quinoprotein 0084 A protein modification that effectively converts an L-serine residue to O-phosphopantetheine-L-serine. (2R)-4-((2S)-2-amino-2-carboxyethyl)phosphonato-2-hydroxy-N-[3-(2-sulfanylethyl)amino-3-oxopropyl]-3,3-dimethylbutanamide RESID AA0150 O-phosphopantetheine-L-serine PSI-MOD MOD:00159 O-phosphopantetheine-L-serine PDBCC PNS 4'-phosphopantetheine SER PNS OG P24 natural attachment phosphopantetheine phosphoprotein 0085 A protein modification that effectively converts an L-asparagine residue to O-(N-acetylaminogalactosyl)-L-threonine. (2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxygalactopyranosyloxy)butanoic acid PDBCC GTH 3-O-glucopyranosyl-threonine-[2-deoxy-2-acetamido-glucopyranoside] RESID AA0155 O-(N-acetylamino)galactosyl-L-threonine PSI-MOD MOD:00164 O-(N-acetylamino)galactosyl-L-threonine GTH natural modified residue glycoprotein 0086 A protein modification that effectively substitutes an L-tyrosine residue with 3',3'',5'-triiodo-L-thyronine. (S)-2-amino-3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]propanoic acid PDBCC T3 3,5,3'triiodothyronine RESID AA0177 3',3'',5'-triiodo-L-thyronine PSI-MOD MOD:00186 3',3'',5'-triiodo-L-thyronine T3 natural modified residue iodine 0087 A protein modification that effectively substitutes an L-tyrosine residue with L-thyroxine. (S)-2-amino-3-[4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodophenyl]propanoic acid PDBCC T44 3,5,3',5'tetraiodo-L-thyronine RESID AA0178 L-thyroxine PSI-MOD MOD:00187 L-thyroxine T44 natural modified residue iodine 0088 A protein modification that effectively converts an L-tryptophan residue to L-6'-bromotryptophan. (S)-2-amino-3-(6-bromo-1H-indol-3-yl)propanoic acid PDBCC BTR 6-bromo-tryptophan RESID AA0179 L-6'-bromotryptophan PSI-MOD MOD:00188 L-6'-bromotryptophan BTR natural modified residue bromine 0089 A protein modification that effectively converts a source amino acid residue to dehydroalanine. 2-aminopropenoic acid PDBCC DHA 2-amino-acrylic acid RESID AA0181 dehydroalanine PSI-MOD MOD:01168 dehydroalanine DHA natural modified residue This modification occurs on SER or TYR 0090 A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine. (Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid PDBCC CRQ [2-(3-carbamoyl-1-imino-propyl)-4-(4-hydroxy-benzylidene)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid RESID AA0183 (Z)-2,3-didehydrotyrosine PSI-MOD MOD:00191 (Z)-2,3-didehydrotyrosine CRQ natural modified residue CRQ has two modifications: RESID:AA0183 and RESID:AA0189 0091 A protein modification that effectively crosslinks an L-glutamine residue and a glycine residue to form 2-imino-glutamine 5-imidazolinone glycine. 2-(3-carbamoyl-1-imino-propyl)-1-carboxymethyl-1-imidazolin-5-one PDBCC CRQ [2-(3-carbamoyl-1-imino-propyl)-4-(4-hydroxy-benzylidene)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid RESID AA0189 2-imino-glutamine 5-imidazolinone glycine PSI-MOD MOD:00197 2-imino-glutamine 5-imidazolinone glycine CRQ natural crosslink1 CRQ has two modifications: RESID:AA0183 and RESID:AA0189 chromoprotein 0092 A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine. (Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid PDBCC CRO {2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid RESID AA0183 (Z)-2,3-didehydrotyrosine PSI-MOD MOD:00191 (Z)-2,3-didehydrotyrosine CRO natural crosslink1 CRO has two modifications: RESID:AA0183 and RESID:AA0184 0093 A protein modification that effectively crosslinks an L-serine residue and a glycine residue to form L-serine 5-imidazolinone glycine. 2-[(R)-1-amino-2-hydroxyethyl]-1-carboxymethyl-1-imidazolin-5-one PDBCC CRO {2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid RESID AA0184 L-serine 5-imidazolinone glycine PSI-MOD MOD:00192 L-serine 5-imidazolinone glycine CRO natural crosslink1 CRO has two modifications: RESID:AA0183 and RESID:AA0184 chromoprotein 0094 A protein modification that effectively converts a source amino acid residue to L-oxoalanine. (S)-2-amino-3-oxopropanoic acid PDBCC FGL 2-aminopropanedioic acid RESID AA0185 L-3-oxoalanine PSI-MOD MOD:01169 L-3-oxoalanine FGL natural modified residue This modification occurs on SER or CYS 0095 A protein modification that effectively converts a source amino acid residue to D-alanine. (R)-2-aminopropanoic acid PDBCC DAL D-alanine RESID AA0191 D-alanine PSI-MOD MOD:00862 D-alanine DAL natural modified residue D-amino acid 0098 A protein modification that effectively converts an L-isoleucine residue to a D-allo-isoleucine. (2R,3S)-2-amino-3-methylpentanoic acid PDBCC DIL D-isoleucine RESID AA0192 D-allo-isoleucine PSI-MOD MOD:00199 D-allo-isoleucine DIL natural modified residue D-amino acid 0099 A protein modification that effectively converts an L-asparagine residue to D-asparagine. (R)-2-amino-4-butanediamic acid PDBCC DSG D-asparagine RESID AA0196 D-asparagine PSI-MOD MOD:00203 D-asparagine DSG natural modified residue D-amino acid 0100 A protein modification that effectively converts an L-tryptophan residue to D-tryptophan. (R)-2-amino-3-(1H-indol-3-yl)propanoic acid PDBCC DTR D-tryptophan RESID AA0198 D-tryptophan PSI-MOD MOD:00205 D-tryptophan DTR natural modified residue D-amino acid 0101 A protein modification that effectively converts an L-threonine residue to D-allo-threonine. (2R,3R)-2-amino-3-hydroxybutanoic acid PDBCC DTH D-threonine RESID AA0199 D-threonine PSI-MOD MOD:00863 D-allo-threonine DTH natural modified residue D-amino acid 0102 A protein modification that effectively converts an L-valine residue to D-valine. (R)-2-amino-3-methylbutanoic acid PDBCC DVA D-valine RESID AA0200 D-valine PSI-MOD MOD:00705 D-valine DVA natural modified residue D-amino acid 0103 A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid. (R)-2-amino-2-carboxyethanesulfenic acid PDBCC CSO S-hydroxycysteine RESID AA0205 L-cysteine sulfenic acid PSI-MOD MOD:00210 L-cysteine sulfenic acid CSO natural modified residue 0104 A protein modification that effectively monooxygenates an L-cysteine residue to L-cysteine sulfenic acid. (R)-2-amino-2-carboxyethanesulfenic acid PDBCC CSX S-oxy cysteine RESID AA0205 L-cysteine sulfenic acid PSI-MOD MOD:00210 L-cysteine sulfenic acid CSX natural modified residue 0105 A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue by a thioester bond to form S-glycyl-L-cysteine. (2R)-2-amino-3-[(aminoacetyl)sulfanyl]propanoic acid RESID AA0206 S-glycyl-L-cysteine PSI-MOD MOD:00211 S-glycyl-L-cysteine CYS GLY C SG C natural crosslink2 blocked carboxyl end thioester bond 0106 A protein modification that effectively converts an L-cysteine residue to S-4-hydroxycinnamyl-L-cysteine. (S,E)-2-amino-3-[3-(4-hydroxyphenyl)propenoylsulfanyl]propanoic acid RESID AA0207 S-4-hydroxycinnamyl-L-cysteine PSI-MOD MOD:00212 S-4-hydroxycinnamyl-L-cysteine PDBCC HC4 4'-hydroxycinnamic acid CYS HC4 SG C1 natural attachment chromoprotein hydroxylation photoreceptor thioester bond 0107 A protein modification that effectively converts an L-arginine residue to a 4-hydroxy-L-arginine. (2S,4Xi)-2-amino-5-[(diaminomethylidene)amino]-4-hydroxypentanoic acid PDBCC ARO C-gamma-hydroxy arginine RESID AA0215 4-hydroxy-L-arginine PSI-MOD MOD:00220 4-hydroxy-L-arginine ARO natural modified residue hydroxylation 0108 A protein modification that effectively converts an L-cysteine residue to S-(6-FMN)-L-cysteine. (R)-2-amino-3-[6-riboflavin 5'-dihydrogen phosphate]sulfanylpropanoic acid RESID AA0220 S-(6-FMN)-L-cysteine PSI-MOD MOD:00225 S-(6-FMN)-L-cysteine PDBCC FMN flavin mononucleotide CYS FMN SG C6 natural attachment phosphoprotein flavoprotein FMN thioether bond 0109 A protein modification that effectively converts an L-histidine residue to 1'-(8alpha-FAD)-L-histidine. (S)-2-amino-3-(1-[8alpha riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid RESID AA0221 1'-(8alpha-FAD)-L-histidine PSI-MOD MOD:00226 1'-(8alpha-FAD)-L-histidine PDBCC FAD flavin-adenine dinucleotide HIS FAD NE2 C8M natural attachment phosphoprotein FAD flavoprotein 0110 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. (S)-2-amino-6-(5'-guanosine phosphonamino)hexanoic acid PDBCC GPL lysine guanosine-5'-monophosphate RESID AA0228 N6-(phospho-5'-guanosine)-L-lysine PSI-MOD MOD:00233 N6-(phospho-5'-guanosine)-L-lysine GPL natural modified residue phosphoprotein 0111 A protein modification that effectively converts an L-cysteine residue to S-nitrosyl-L-cysteine. (2R)-2-amino-3-nitrososulfanyl-propanoic acid PDBCC SNC S-nitroso-cysteine RESID AA0230 S-nitrosyl-L-cysteine PSI-MOD MOD:00235 S-nitrosyl-L-cysteine SNC natural modified residue 0112 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. 1-[(S)-5-amino-5-carboxypentyl]amino-2-[(S)-2-amino-2-carboxyethyl]-2,6-cyclohexadien-4,5-dione RESID AA0233 2'-(L-lys-N6-yl)-L-4',5'-topaquinone PSI-MOD MOD:00238 5'-(N6-L-lysine)-L-topaquinone PDBCC TPQ 5-(2-carboxy-2-aminoethyl)-2-hydroxy-1,4-benzoquinone TPQ LYS C2 NZ natural crosslink2 quinoprotein 0113 A protein modification that effectively converts an L-cysteine residue to S-methyl-L-cysteine. (R)-2-amino-3-(methylsulfanyl)propanoic acid PDBCC SMC S-methylcysteine RESID AA0234 S-methyl-L-cysteine PSI-MOD MOD:00239 S-methyl-L-cysteine SMC natural modified residue methylated amino acid thioether bond 0114 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. (2S,3R)-2-amino-3-(5-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl)-3-(4-hydroxyphenyl)propanoic acid RESID AA0250 3-(3'-L-histidyl)-L-tyrosine PSI-MOD MOD:00255 3-(3'-L-histidyl)-L-tyrosine HIS TYR ND1 CB natural crosslink2 0115 A protein modification that dioxygenates an L-methionine residue to L-methionine sulfone. (S)-2-amino-4-(methylsulfonyl)butanoic acid PDBCC OMT S-dioxymethionine RESID AA0251 L-methionine sulfone PSI-MOD MOD:00256 L-methionine sulfone OMT natural modified residue 0116 A protein modification that effectively converts an L-cysteine residue to dipyrrolylmethanemethyl-L-cysteine. 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 RESID AA0252 dipyrrolylmethanemethyl-L-cysteine PSI-MOD MOD:00257 dipyrrolylmethanemethyl-L-cysteine PDBCC DPM 3-{2-[4-(2-carboxy-ethyl)-3-carboxymethyl-5H-pyrrol-2-ylmethyl]-4-carboxymethly-5-methyl-2H-pyrrol-3-yl}-propionic acid CYS DPM SG CHA natural attachment thioether bond 0117 A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound phycoviolobilin. (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 RESID AA0258 S-phycoviolobilin-L-cysteine PSI-MOD MOD:00263 S-phycoviolobilin-L-cysteine PDBCC PVN phycoviolobilin CYS PVN SG C31 natural attachment chromoprotein phycoviolobilin thioether bond 0118 A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound phycourobilin. 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 RESID AA0260 phycourobilin-bis-L-cysteine PSI-MOD MOD:00265 phycourobilin-bis-L-cysteine PDBCC PUB phycourobilin CYS CYS PUB SG CAA,CAD SG CAA,CAD natural crosslink2 chromoprotein phycourobilin thioether bond 0119 A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid. (R)-2-amino-2-carboxyethanesulfinic acid PDBCC CSD 3-sulfinoalanine RESID AA0262 (R)-2-amino-2-carboxyethanesulfinic acid PSI-MOD MOD:00267 cysteine-S,S-dioxide CSD natural modified residue 0120 A protein modification that effectively dioxygenates an L-cysteine residue to L-cysteine sulfinic acid. (R)-2-amino-2-carboxyethanesulfinic acid PDBCC CSW cysteine-S-dioxide RESID AA0262 (R)-2-amino-2-carboxyethanesulfinic acid PSI-MOD MOD:00267 cysteine-S,S-dioxide CSW natural modified residue 0121 A protein modification that effectively converts an L-serine residue to O-(sn-1-glycerophosphoryl)-L-serine. (2S)-2-amino-3-[(2Xi)-2,3-dihydroxypropyl]phosphonoxypropanoic acid RESID AA0264 O-(sn-1-glycerophosphoryl)-L-serine PSI-MOD MOD:00269 O-(sn-1-glycerophosphoryl)-L-serine PDBCC OPE phosphoric acid mono-(2-amino-ethlyl) ester SER OPE CB O3 natural attachment phosphoprotein 0122 A protein modification that effectively converts a glycine residue to an internal 1-thioglycine. aminoethanethioic acid PDBCC GL3 thioglycin RESID AA0265 1-thioglycine PSI-MOD MOD:00270 1-thioglycine (internal) GL3 natural modified residue There are two entries in PSI-MOD MOD:00270 and MOD:01623, corresponding to internal and terminal. 0123 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. (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 RESID AA0266 heme P460-bis-L-cysteine-L-tyrosine PSI-MOD MOD:00271 heme P460-bis-L-cysteine-L-tyrosine PDBCC HEC heme C CYS CYS TYR HEC SG CAB SG CAC CE1,CE2 C4B natural crosslink3 chromoprotein heme iron metalloprotein thioether bond 0124 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. (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 RESID AA0271 heme P460-bis-L-cysteine-L-lysine PSI-MOD MOD:00276 heme P460-bis-L-cysteine-L-lysine PDBCC HEC heme C CYS CYS LYS HEC SG CAB,CAC SG CAC,CAB NZ CHA natural crosslink3 chromoprotein heme iron metalloprotein thioether bond 0125 A protein modification that effectively converts an L-cysteine residue to L-cysteine persulfide. (R)-2-amino-3-disulfanylpropanoic acid PDBCC CSS S-mercapto-cysteine RESID AA0269 L-cysteine persulfide PSI-MOD MOD:00274 L-cysteine persulfide CSS natural modified residue 0126 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. (2S)-2-amino-3-[1-(5-[(2S)-2-amino-2-carboxyethyl]-2-hydroxyphenyl)-1H-imidazol-4-yl]propanoic acid RESID AA0270 3'-(1'-L-histidyl)-L-tyrosine PSI-MOD MOD:00275 3'-(1'-L-histidyl)-L-tyrosine HIS TYR NE2 CE1 natural crosslink2 0127 A protein modification that effectively converts an L-glutamine residue to 2-methyl-L-glutamine. (S)-2-amino-2-methylpentanediamic acid PDBCC MGN 2-methyl-glutamine RESID AA0273 2-methyl-L-glutamine PSI-MOD MOD:00278 2-methyl-L-glutamine MGN natural modified residue methylated amino acid 0128 A protein modification that effectively converts an L-cysteine residue to S-selenyl-L-cysteine. (R)-2-amino-3-(selanylsulfanyl)propanoic acid PDBCC CSZ S-selanyl cysteine RESID AA0277 S-selanyl-L-cysteine PSI-MOD MOD:00282 S-selenyl-L-cysteine CSZ hypothetical modified residue selenium 0129 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. (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 RESID AA0280 dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium PSI-MOD MOD:00285 dihydroxyheme-L-aspartate ester-L-glutamate ester-L-methionine sulfonium PDBCC HEM protoporphyrin IX containing Fe ASP GLU MET HEM OD2 CMD OE2 CMB SD CBB natural crosslink3 chromoprotein heme hydroxylation iron metalloprotein 0130 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. 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3-5,6]quinoline-2,7,9-tricarboxylic acid RESID AA0283 pyrroloquinoline quinone PSI-MOD MOD:00288 pyrroloquinoline quinone PDBCC PQQ pyrroloquinoline quinone GLU TYR PQQ CG N1 OH C8 natural crosslink2 quinoprotein 0131 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. tetra-mu3-sulfidotris(S-cysteinyliron)(N1'-histidinoiron) RESID AA0284 tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide PSI-MOD MOD:00289 tris-L-cysteinyl L-N1'-histidino tetrairon tetrasulfide PDBCC SF4 iron/sulfur cluster CYS CYS CYS HIS SF4 SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 NE2 FE1,FE2,FE3,FE4 natural crosslink4 4Fe-4S iron-sulfur protein metalloprotein 0132 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. tetra-mu3-sulfidotris(S-cysteinyliron)(N3'-histidinoiron) RESID AA0285 tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide PSI-MOD MOD:00290 tris-L-cysteinyl L-N3'-histidino tetrairon tetrasulfide PDBCC SF4 iron/sulfur cluster CYS CYS CYS HIS SF4 SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 ND1 FE1,FE2,FE3,FE4 natural crosslink4 4Fe-4S iron-sulfur protein metalloprotein 0133 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. tetra-mu3-sulfidotris(S-cysteinyliron)(O4-aspartatoiron) RESID AA0286 tris-L-cysteinyl L-aspartato tetrairon tetrasulfide PSI-MOD MOD:00291 tris-L-cysteinyl L-aspartato tetrairon tetrasulfide PDBCC SF4 iron/sulfur cluster CYS CYS CYS ASP SF4 SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 OD2 FE1,FE2,FE3,FE4 natural crosslink4 4Fe-4S iron-sulfur protein metalloprotein 0134 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. tetra-mu3-sulfidotris(S-cysteinyliron)(O3-serinyliron) RESID AA0288 tris-L-cysteinyl L-serinyl tetrairon tetrasulfide PSI-MOD MOD:00293 tris-L-cysteinyl L-serinyl tetrairon tetrasulfide PDBCC SF4 iron/sulfur cluster CYS CYS CYS SER SF4 SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 OG FE1,FE2,FE3,FE4 hypothetical crosslink4 4Fe-4S iron-sulfur protein metalloprotein 0135 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. tetra-mu3-sulfidobis(S-cysteinyliron)(N3'-histidinoiron)(O3-serinyliron) RESID AA0289 bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide PSI-MOD MOD:00294 bis-L-cysteinyl L-N3'-histidino L-serinyl tetrairon tetrasulfide PDBCC SF4 iron/sulfur cluster CYS CYS HIS SER SF4 SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 ND1 FE1,FE2,FE3,FE4 OG FE1,FE2,FE3,FE4 hypothetical crosslink4 4Fe-4S iron-sulfur protein metalloprotein 0136 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. mu4-sulfido bis(bis-N1'-histidino copper)(N1'-histidino-N3'-histidino copper)(N3'-histidino hydroxide copper) RESID AA0298 heptakis-L-histidino tetracopper mu4-sulfide hydroxide PSI-MOD MOD:00303 heptakis-L-histidino tetracopper mu4-sulfide hydroxide PDBCC CUZ (mu-4-sulfido)-tetra-nuclear copper ion HIS HIS HIS HIS HIS HIS HIS CUZ NE2 CU1,CU2,CU3,CU4 NE2 CU1,CU2,CU3,CU4 NE2 CU1,CU2,CU3,CU4 NE2 CU1,CU2,CU3,CU4 NE2 CU1,CU2,CU3,CU4 ND1 CU1,CU2,CU3,CU4 ND1 CU1,CU2,CU3,CU4 natural crosslink7 copper metalloprotein 0137 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. RESID AA0300 hexakis-L-cysteinyl L-serinyl octairon heptasulfide PSI-MOD MOD:00305 hexakis-L-cysteinyl L-serinyl octairon heptasulfide PDBCC CLF Fe(8)-S(7) cluster CYS CYS CYS CYS CYS CYS SER CLF SG FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8 SG FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8 SG FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8 SG FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8 SG FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8 SG FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8 OG FE1,FE2,FE3,FE4,FE5,FE6,FE7,FE8 natural crosslink7 iron-sulfur protein metalloprotein 0138 A protein modification that effectively cyclizes an L-asparagine residue to form a carboxyl-terminal L-aspartimide. (S)-3-amino-2,5-pyrrolidinedione PDBCC SNN L-3-aminosuccinimide RESID AA0302 L-aspartimide PSI-MOD MOD:00307 L-aspartimide SNN C natural modified residue blocked carboxyl end protein splicing 0139 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. 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) RESID AA0310 pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide PSI-MOD MOD:00315 pentakis-L-cysteinyl L-histidino nickel tetrairon pentasulfide PDBCC NFS Fe(4)-Ni(1)-S(5) cluster CYS CYS CYS CYS CYS HIS NFS SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 SG NI1 NE2 FE1,FE2,FE3,FE4 natural crosslink6 iron-sulfur protein metalloprotein Ni-4Fe-5S nickel 0140 A protein modification that effectively converts an L-asparagine residue to N4,N4-dimethyl-L-asparagine. (S)-2-amino-N4,N4-dimethylbutanediamic acid PDBCC DMH N4,N4-dimethyl-asparagine RESID AA0311 N4,N4-dimethyl-L-asparagine PSI-MOD MOD:00316 N4,N4-dimethyl-L-asparagine DMH hypothetical modified residue methylated amino acid 0141 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. (S)-3-(2-amino-2-carboxyethyl)-4-[(R)-2-amino-2-carboxyethyl]sulfanyl-6,7-indolinedione RESID AA0313 4'-(S-L-cysteinyl)-L-tryptophyl quinone PSI-MOD MOD:00318 4'-(S-L-cysteinyl)-L-tryptophyl quinone CYS TRP SG CE3 natural crosslink2 quinoprotein thioether bond 0142 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. (2S,3S)-2-amino-3-[(R)-2-amino-2-carboxyethyl]sulfanylbutanedioic acid RESID AA0314 3-(S-L-cysteinyl)-L-aspartic acid PSI-MOD MOD:00319 3-(S-L-cysteinyl)-L-aspartic acid CYS ASP SG CB natural crosslink2 lanthionine thioether bond 0143 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. (2S,4S)-2-amino-4-[(R)-2-amino-2-carboxyethyl]sulfanylpentanedioic acid RESID AA0315 4-(S-L-cysteinyl)-L-glutamic acid PSI-MOD MOD:00320 4-(S-L-cysteinyl)-L-glutamic acid CYS GLU SG CG natural crosslink2 thioether bond 0144 A protein modification that effectively converts an L-histidine residue to tele-methyl-L-histidine. (S)-2-amino-3-(1-methyl-1H-imidazol-4-yl)propanoic acid PDBCC HIC 4-methyl-histidine RESID AA0317 1'-methyl-L-histidine PSI-MOD MOD:00322 1'-methyl-L-histidine HIC natural modified residue methylated amino acid 0145 A protein modification that effectively converts an L-serine residue to L-serinyl molybdenum bis(molybdopterin guanine dinucleotide). 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 RESID AA0319 L-serinyl molybdenum bis(molybdopterin guanine dinucleotide) PSI-MOD MOD:00324 L-serinyl molybdenum bis(molybdopterin guanine dinucleotide) PDBCC MGD molybdopterin guanosine dinucleotide SER MGD MGD 6MO OG MO S12,S13 MO S12,S13 MO natural attachment metalloprotein molybdenum molybdopterin phosphoprotein 0146 A protein modification that effectively converts an L-tryptophan residue to a 3-hydroxy-L-tryptophan. (2S,3S)-2-amino-3-hydroxy-3-(1H-indol-3-yl)propanoic acid PDBCC HTR beta-hydroxytryptophane RESID AA0322 3-hydroxy-L-tryptophan PSI-MOD MOD:00327 3-hydroxy-L-tryptophan HTR hypothetical modified residue hydroxylation 0147 A protein modification that effectively converts four L-cysteine residues and a three-iron four-sulfur cluster to tetrakis-L-cysteinyl triiron tetrasulfide. di-mu-1:2kappaS-sulfido di-mu-2:3kappaS-sulfido iron bis(bis-S-cysteinyliron) RESID AA0326 tetrakis-L-cysteinyl triiron tetrasulfide PSI-MOD MOD:00331 tetrakis-L-cysteinyl triiron tetrasulfide PDBCC F3S Fe3-S4 cluster CYS CYS CYS CYS F3S SG FE1,FE3,FE4 SG FE1,FE3,FE4 SG FE1,FE3,FE4 SG FE1,FE3,FE4 hypothetical crosslink4 3Fe-4S iron-sulfur protein metalloprotein 0148 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. (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 RESID AA0329 1'-heme-L-histidine PSI-MOD MOD:00334 1'-heme-L-histidine PDBCC HEM protoporphyrin IX containg Fe HIS HEM NE2 CAB natural attachment NE2 is much closer to FE than to CBB. chromoprotein heme iron metalloprotein 0149 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. (2S,3S,SXi)-2-amino-3-([(R)-2-amino-2-carboxyethyl]sulfinyl)butanoic acid RESID AA0330 3-methyl-L-lanthionine sulfoxide PSI-MOD MOD:00335 3-methyl-L-lanthionine sulfoxide CYS THR SG * natural crosslink2 0150 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. di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-O4-aspartatoiron) RESID AA0331 tris-L-cysteinyl L-aspartato diiron disulfide PSI-MOD MOD:00336 tris-L-cysteinyl L-aspartato diiron disulfide PDBCC FES Fe2/S2 (inorganic) cluster CYS CYS CYS ASP FES SG FE1,FE2 SG FE1,FE2 SG FE1,FE2 OD2 FE1,FE2 hypothetical crosslink4 2Fe-2S iron-sulfur protein metalloprotein 0151 A protein modification that effectively converts an L-cysteine residue to L-cysteinyl hydrogenase diiron subcluster. RESID AA0334 L-cysteinyl hydrogenase diiron subcluster PSI-MOD MOD:00339 L-cysteinyl hydrogenase diiron subcluster PDBCC HC1 2 iron/2 sulfur/5 carbonyl/2 water inorganic cluster CYS HC1 SG FE1,FE2 natural attachment iron-sulfur protein metalloprotein 0152 A protein modification that effectively converts an L-isoleucine residue to N-methyl-L-isoleucine. (2S,3S)-2-methylamino-3-methylpentanoic acid PDBCC IML N-methyl-isoleucine RESID AA0336 N-methyl-L-isoleucine PSI-MOD MOD:00341 N-methyl-L-isoleucine IML hypothetical modified residue methylated amino end 0153 A protein modification that effectively converts an L-leucine residue to N-methyl-L-leucine. (S)-2-methylamino-4-methylpentanoic acid PDBCC MLE N-methylleucine RESID AA0337 N-methyl-L-leucine PSI-MOD MOD:00342 N-methyl-L-leucine MLE hypothetical modified residue methylated amino end 0154 A protein modification that effectively converts a glycine residue to N-palmitoylglycine. (hexadecanoylamino)ethanoic acid RESID AA0339 N-palmitoyl-glycine PSI-MOD MOD:00344 N-palmitoylglycine PDBCC 140 N-palmitoylglycine GLY N 140 N C1 natural attachment blocked amino end lipoprotein palmitoylation 0155 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. (R)-2-amino-2-[(R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylethanoic acid RESID AA0340 2-(S-L-cysteinyl)-L-phenylalanine PSI-MOD MOD:00345 2-(S-L-cysteinyl)-L-phenylalanine CYS PHE SG CA natural crosslink2 thioether bond 0156 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. (S)-2-amino-2-[(R)-2-amino-2-carboxyethyl]sulfanyl-3-phenylethanoic acid RESID AA0341 2-(S-L-cysteinyl)-D-phenylalanine PSI-MOD MOD:00346 2-(S-L-cysteinyl)-D-phenylalanine CYS PHE SG CA natural crosslink2 D-amino acid thioether bond 0157 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. (2S,3R)-2-amino-2-[(R)-2-amino-2-carboxyethyl]sulfanyl-3-hydroxybutanoic acid RESID AA0342 2-(S-L-cysteinyl)-D-allo-threonine PSI-MOD MOD:00347 2-(S-L-cysteinyl)-D-allo-threonine CYS THR SG CA natural crosslink2 D-amino acid thioether bond 0158 A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form 4-amino-3-isothiazolidinone-L-serine. (4R)-2-((S)-1-carboxy-2-hydroxyethyl)-4-amino-3(2H)-isothiazolidinone RESID AA0344 4-amino-3-isothiazolidinone-L-serine PSI-MOD MOD:00349 4-amino-3-isothiazolidinone-L-serine CYS SER SG N SG C natural crosslink1 0159 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. RESID AA0348 S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium PSI-MOD MOD:00353 S-[5'-(L-tryptoph-6'-yl)-L-tyrosin-3'-yl]-L-methionin-S-ium MET TRP TYR SD CE1,CE2 CH2 CE1,CE2 natural crosslink3 0160 A protein modification that effectively converts an L-cysteine residue to S-(4a-FMN)-L-cysteine. (R)-2-amino-3-(4a-riboflavin 5'-dihydrogen phosphate)sulfanylpropanoic acid RESID AA0351 S-(4a-FMN)-L-cysteine PSI-MOD MOD:00356 S-(4a-FMN)-L-cysteine PDBCC FMN flavin mononucleotide CYS FMN SG C4A natural attachment phosphoprotein flavoprotein FMN thioether bond 0161 A protein modification that effectively converts an L-cysteine residue to L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide. [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 RESID AA0355 L-cysteinyl copper sulfido molybdopterin cytosine dinucleotide PSI-MOD MOD:00360 L-cysteinyl copper sulfido molybdopterin cytosine dinuncleotide PDBCC CUN Cu(I)-S-Mo(IV)(=O)OH cluster PDBCC MCN pterin cytosine dinucleotide CYS CUN MCN SG CU MO S7' MO S8' natural attachment copper metalloprotein molybdenum molybdopterin phosphoprotein 0162 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. tetra-mu3-sulfido(S-adenosylmethion-N,O-diyliron)tris(S-cysteinyliron) RESID AA0356 tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide PSI-MOD MOD:00361 tris-L-cysteinyl S-adenosylmethion-N,O-diyl tetrairon tetrasulfide PDBCC SF4 iron/sulfur cluster PDBCC SAM S-adenosylmethionine CYS CYS CYS SF4 SAM SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 SG FE1,FE2,FE3,FE4 FE1,FE2,FE3,FE4 N FE1,FE2,FE3,FE4 O,OXT natural crosslink3 4Fe-4S iron-sulfur protein metalloprotein S-adenosyl-L-methionine 0163 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. di-mu-sulfido(N(eta1)-arginyl-S-cysteinyliron)(bis-S-cysteinyliron) RESID AA0357 tris-L-cysteinyl L-arginyl diiron disulfide PSI-MOD MOD:00362 tris-L-cysteinyl L-arginyl diiron disulfide PDBCC FES Fe2/S2 (inorganic) cluster CYS CYS CYS ARG FES SG FE1,FE2 SG FE1,FE2 SG FE1,FE2 NH1,NH2 FE1,FE2 natural crosslink4 2Fe-2S iron-sulfur protein metalloprotein 0164 A protein modification that effectively converts an L-serine residue to O-sulfo-L-serine. (2S)-2-amino-3-(sulfooxy)propanoic acid PDBCC OSE O-sulfo-L-serine RESID AA0361 O-sulfo-L-serine PSI-MOD MOD:00366 O-sulfo-L-serine OSE natural modified residue sulfoprotein 0165 A protein modification that effectively converts an L-methionine residue to N-carboxy-L-methionine. (S)-2-carboxyamino-4-(methylsulfanyl)butanoic acid PDBCC CXM N-carboxymethionine RESID AA0363 N-carboxy-L-methionine deprecated PSI-MOD MOD:00368 N-carboxy-L-methionine CXM N natural modified residue blocked amino end 0166 A protein modification that effectively converts an L-serine residue to O-acetyl-L-serine. (2S)-3-(acetyloxy)-2-aminopropanoic acid PDBCC OAS O-acetylserine RESID AA0364 O-acetyl-L-serine PSI-MOD MOD:00369 O-acetyl-L-serine OAS natural modified residue 0167 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 RESID AA0366 bis-L-aspartato tris-L-glutamato L-histidino calcium tetramanganese tetroxide PDBCC OEC oxygen evolving system ASP ASP GLU GLU GLU HIS OEC OD1,OD2 MN1,MN2,MN3,MN4 OD1,OD2 MN1,MN2,MN3,MN4 OE1,OE2 MN1,MN2,MN3,MN4 OE1,OE2 MN1,MN2,MN3,MN4 OE1,OE2 MN1,MN2,MN3,MN4 OE1,OE2 MN1,MN2,MN3,MN4 NE2 MN1,MN2,MN3,MN4 natural crosslink6 calcium manganese metalloprotein 0168 A protein modification that effectively cross-links two L-tyrosine residues with a carbon-carbon bond to form 3'-(3'-L-tyrosinyl)-L-tyrosine. (2S,2'S)-3,3'-(6,6'-dihydroxybiphenyl-3,3'-diyl)bis(2-aminopropanoic acid) RESID AA0367 3'-(L-tyros-3'-yl)-L-tyrosine PSI-MOD MOD:00372 3'-(3'-L-tyrosinyl)-L-tyrosine TYR TYR CE2 CE2 natural crosslink2 0169 A protein modification that effectively cross-links L-tyrosine residues with an ether bond to form 3'-(O4'-L-tyrosinyl)-L-tyrosine. (2S)-2-amino-3-[3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-4-hydroxyphenyl]propanoic acid RESID AA0368 3'-(L-tyros-O4'-yl)-L-tyrosine PSI-MOD MOD:00373 3'-(O4'-L-tyrosinyl)-L-tyrosine TYR TYR OH CE2 natural crosslink2 0170 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. (S)-2-amino-3-[1-(5'-uridine phosphono)imidazol-4-yl]propanoic acid RESID AA0372 1'-(phospho-5'-uridine)-L-histidine PSI-MOD MOD:00377 1'-(phospho-5'-uridine)-L-histidine PDBCC U5P uridine-5'-monophosphate HIS U5P NE2 P natural attachment phosphoprotein 0171 A protein modification that effectively crosslinks an L-glutamic acid residue and a glycine residue to form 2-imino-glutamic acid 5-imidazolinone glycine. 2-(3-carboxy-1-iminopropyl)-1-carboxymethyl-1-imidazolin-5-one PDBCC CRU 4-[(4Z)-1-(carboxymethyl)-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-2-yl]-4-iminobutanoic acid RESID AA0378 2-imino-glutamic acid 5-imidazolinone glycine PSI-MOD MOD:00383 2-imino-glutamic acid 5-imidazolinone glycine CRU hypothetical crosslink1 CRU has two modifications: RESID:AA0183 and RESID:AA0378 chromoprotein 0172 A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine. (Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid PDBCC CRU 4-[(4Z)-1-(carboxymethyl)-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-2-yl]-4-iminobutanoic acid RESID AA0183 (Z)-2,3-didehydrotyrosine PSI-MOD MOD:00191 (Z)-2,3-didehydrotyrosine CRU natural modified residue CRU has two modifications: RESID:AA0183 and RESID:AA0378 0173 A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine. 2-[1-imino-3-(methylsulfanyl)propyl]-1-carboxymethyl-1-imidazolin-5-one PDBCC CH6 {(4Z)-2-[(1S)-1-amino-3-(methylsulfanyl)propyl]-4-[(4-hydroxyphenyl)methylidene]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid RESID AA0379 2-imino-methionine 5-imidazolinone glycine PSI-MOD MOD:00384 2-imino-methionine 5-imidazolinone glycine CH6 natural crosslink1 CH6 has two modifications: RESID:AA0183 and RESID:AA0379 chromoprotein 0174 A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine. (Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid PDBCC CH6 {(4Z)-2-[(1S)-1-amino-3-(methylsulfanyl)propyl]-4-[(4-hydroxyphenyl)methylidene]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid RESID AA0183 (Z)-2,3-didehydrotyrosine PSI-MOD MOD:00191 (Z)-2,3-didehydrotyrosine CH6 natural modified residue CH6 has two modifications: RESID:AA0183 and RESID:AA0379 0175 A protein modification that effectively crosslinks an L-methionine residue and a glycine residue to form 2-imino-methionine 5-imidazolinone glycine. 2-[1-imino-3-(methylsulfanyl)propyl]-1-carboxymethyl-1-imidazolin-5-one PDBCC NRQ {(4Z)-4-(4-hydroxybenzylidene)-2-[3-(methylthio)propanimidoyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid RESID AA0379 2-imino-methionine 5-imidazolinone glycine PSI-MOD MOD:00384 2-imino-methionine 5-imidazolinone glycine NRQ natural crosslink1 NRQ has two modifications: RESID:AA0183 and RESID:AA0379 chromoprotein 0176 A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine. (Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid PDBCC NRQ {(4Z)-4-(4-hydroxybenzylidene)-2-[3-(methylthio)propanimidoyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid RESID AA0183 (Z)-2,3-didehydrotyrosine PSI-MOD MOD:00191 (Z)-2,3-didehydrotyrosine NRQ natural modified residue NRQ has two modifications: RESID:AA0183 and RESID:AA0379 0177 A protein modification that effectively crosslinks an L-asparagine residue and a glycine residue to form L-asparagine 5-imidazolinone glycine. 2-[(S)-1,3-diamino-3-oxopropyl]-1-carboxymethyl-1-imidazolin-5-one PDBCC NYG [(4Z)-2-[(1S)-1,3-diamino-3-oxoprolyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid RESID AA0380 L-asparagine 5-imidazolinone glycine PSI-MOD MOD:00385 L-asparagine 5-imidazolinone glycine NYG hypothetical crosslink1 NYG has two modifications: RESID:AA0183 and RESID:AA0380 0178 A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine. (Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid PDBCC NYG [(4Z)-2-[(1S)-1,3-diamino-3-oxoprolyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid RESID AA0183 (Z)-2,3-didehydrotyrosine PSI-MOD MOD:00191 (Z)-2,3-didehydrotyrosine NYG natural modified residue NYG has two modifications: RESID:AA0183 and RESID:AA0380 0179 A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form L-lysine 5-imidazolinone glycine. 2-[(S)-1,5-diaminopentanyl]-1-carboxymethyl-1-imidazolin-5-one PDBCC CR7 [(4Z)-2-[(1S)-1,5-diaminopentyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid RESID AA0381 L-lysine 5-imidazolinone glycine PSI-MOD MOD:00386 L-lysine 5-imidazolinone glycine CR7 hypothetical crosslink1 CR7 has two modifications: RESID:AA0183 and RESID:AA0381 0180 A protein modification that effectively crosslinks an L-lysine residue and a glycine residue to form 2-tetrahydropyridinyl-5-imidazolinone glycine. 2-(3,4,5,6-tetrahydropyridin-2-yl)-1-carboxymethyl-1-imidazolin-5-one PDBCC CH7 [(4Z)-2-[(1S)-1,5-diaminopentyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid RESID AA0382 2-tetrahydropyridinyl-5-imidazolinone glycine PSI-MOD MOD:00387 2-tetrahydropyridinyl-5-imidazolinone glycine CH7 natural crosslink1 0181 A protein modification that effectively converts L-tyrosine to (Z)-2,3-didehydrotyrosine. (Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid PDBCC CR7 [(4Z)-2-[(1S)-1,5-diaminopentyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid RESID AA0183 (Z)-2,3-didehydrotyrosine PSI-MOD MOD:00191 (Z)-2,3-didehydrotyrosine CR7 natural modified residue CR7 has two modifications: RESID:AA0183 and RESID:AA0381/AA0382 0182 a protein modification that effectively converts an L-histidine residue to L-histidino vanadium tetraoxide dihydrogen (4-[(2S)-2-amino-2-carboxyethyl]-1H-imidazol-1-yl) (tetraoxido)vanadate RESID AA0395 L-histidino vanadium tetraoxide PSI-MOD MOD:00802 L-histidino vanadium tetraoxide PDBCC VO4 vanadate ion HIS VO4 NE2 V natural attachment metalloprotein vanadium 0183 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. (S,R)-2-amino-3-(2-amino-2-carboxyethylsulfanyl)-3-(4-hydroxyphenyl)propanoic acid RESID AA0396 3-(S-L-cysteinyl)-L-tyrosine PSI-MOD MOD:00803 3-(S-L-cysteinyl)-L-tyrosine CYS TYR SG CB natural crosslink2 thioether bond 0184 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. (R)-2-amino-3-[(S)-2-amino-1-oxopropyl]sulfanylpropanoic acid RESID AA0411 S-(L-alanyl)-L-cysteine PSI-MOD MOD:00821 S-(L-alanyl)-L-cysteine ALA C CYS C SG hypothetical crosslink2 blocked carboxyl end thioester bond 0185 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. (R)-2-amino-3-[(S)-2-amino-4-methyl-1-oxopentyl]sulfanylpropanoic acid RESID AA0412 S-(L-leucyl)-L-cysteine PSI-MOD MOD:00822 S-(L-leucyl)-L-cysteine CYS LEU C SG C natural crosslink2 blocked carboxyl end thioester bond 0186 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. (R)-2-amino-3-[(S)-2-amino-4-methylsulfanyl-1-oxobutyl]sulfanylpropanoic acid RESID AA0413 S-(L-methionyl)-L-cysteine PSI-MOD MOD:00823 S-(L-methionyl)-L-cysteine CYS MET C SG C natural crosslink2 blocked carboxyl end thioester bond 0187 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. (R)-2-amino-3-[(S)-2-amino-3-phenyl-1-oxopropyl]sulfanylpropanoic acid RESID AA0414 S-(L-phenylalanyl)-L-cysteine PSI-MOD MOD:00825 S-(L-phenylalanyl)-L-cysteine CYS PHE C SG C natural crosslink2 blocked carboxyl end thioester bond 0188 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. (R)-2-amino-3-[(2S,3R)-2-amino-3-hydroxy-1-oxobutyl]sulfanylpropanoic acid RESID AA0415 S-(L-threonyl)-L-cysteine PSI-MOD MOD:00826 S-(L-threonyl)-L-cysteine CYS THR C SG C hypothetical crosslink2 blocked carboxyl end thioester bond 0189 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. (R)-2-amino-3-[(S)-2-amino-3-(4-hydoxyphenyl)-1-oxopropyl]sulfanylpropanoic acid RESID AA0416 S-(L-tyrosyl)-L-cysteine PSI-MOD MOD:00827 S-(L-tyrosyl)-L-cysteine CYS TYR C SG C hypothetical crosslink2 blocked carboxyl end thioester bond 0190 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. (R)-2-amino-3-[(S)-2-amino-3-(1H-indol-3-yl)-1-oxopropyl]sulfanylpropanoic acid RESID AA0417 S-(L-tryptophanyl)-L-cysteine PSI-MOD MOD:00828 S-(L-tryptophanyl)-L-cysteine CYS TRP C SG C natural crosslink2 blocked carboxyl end thioester bond 0191 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. (R)-2-amino-3-[(S)-2-amino-3-phenyl-1-oxopropyl]oxypropanoic acid RESID AA0418 O-(L-phenylalanyl)-L-serine PSI-MOD MOD:00829 O-(L-phenylalanyl)-L-serine SER PHE C OG C natural crosslink2 blocked carboxyl end 0192 A protein modification that effectively converts an L-threonine residue to O-acetyl-L-threonine. (2S,3R)-3-(acetyloxy)-2-aminobutanoic acid PDBCC TH5 O-acetyl-L-threonine RESID AA0423 O-acetyl-L-threonine PSI-MOD MOD:01171 O-acetyl-L-threonine TH5 natural modified residue 0193 A protein modification that effectively results from forming an adduct between a cysteine residue and the tetrapyrrole compound 15,16-dihydrobiliverdin. (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 RESID AA0428 S-15,16-dihydrobiliverdin-L-cysteine PSI-MOD MOD:01142 S-15,16-dihydrobiliverdin-L-cysteine PDBCC DBV 15,16-dihydrobiliverdin CYS DBV SG CAA natural attachment chromoprotein dihydrobiliverdin thioether bond 0194 A protein modification that effectively results from forming an adduct between two cysteine residues and the tetrapyrrole compound 15,16-dihydrobiliverdin. (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 RESID AA0429 15,16-dihydrobiliverdin-bis-L-cysteine PSI-MOD MOD:01143 15,16-dihydrobiliverdin-bis-L-cysteine PDBCC DBV 15,16-dihydrobiliverdin CYS CYS DBV SG CBA SG CAD natural crosslink2 chromoprotein dihydrobiliverdin thioether bond 0195 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. (2S)-2-amino-6-([(5S)-5-amino-5-carboxypentylidene]amino)hexanoic acid RESID AA0430 L-dehydrolysinonorleucine PSI-MOD MOD:01176 L-dehydrolysinonorleucine LYS LYS NZ CE natural crosslink2 0196 A protein modification that effectively converts an L-histidine residue to 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine. (S)-2-amino-3-[1-(1,2,3-trihydroxypropan-2-yl)-1H-imidazol-4-yl]propanoic acid PDBCC HIQ 1-[1,2-dihydroxy-1-(hydroxymethyl)ethyl]-L-histidine RESID AA0431 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine PSI-MOD MOD:01177 1'-(1,2,3-trihydroxyprop-2-yl)-L-histidine HIQ natural modified residue 0197 A protein modification that effectively converts an L-aspartic acid residue to S-(aspart-4-yloxy) thiocarbonate. (2S)-2-amino-4-(carboxysulfanyl)oxy-4-oxobutanoic acid PDBCC OHS O-(carboxysulfanyl)-4-oxo-L-homoserine RESID AA0432 S-(aspart-4-yloxy) thiocarbonate deprecated PSI-MOD MOD:01178 S-(aspart-4-yloxy) thiocarbonate OHS natural modified residue 0199 A protein modification that crosslinks a cysteine and a histidine residue by forming the adduct 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD. 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 RESID AA0436 6-(S-L-cysteinyl)-8alpha-(N3'-L-histidino)-FAD PSI-MOD MOD:01182 6-(S-L-cysteinyl)-8alpha-(-3'-L-histidino)-FAD PDBCC FAD flavin-adenine dinucleotide CYS HIS FAD SG C6 ND1 C8M natural crosslink2 phosphoprotein FAD flavoprotein thioether bond 0200 A protein modification that effectively cross-links two L-selenocysteine residues to form L-selenocystine, (R,R)-3,3'-diselane-1,2-diylbis(2-aminopropanoic acid) RESID AA0437 L-selenocystine PSI-MOD MOD:01183 L-selenocystine (oxidized selenocysteine) (Sec-Sec) PDBCC SEC 2-amino-3-selenino-propionic acid SEC SEC SEG SEG hypothetical crosslink2 redox-active center selenium 0201 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. di-mu-sulfido(bis-S-cysteinyliron)(S-cysteinyl-N3'-histidinoiron) RESID AA0438 tris-L-cysteinyl L-histidino diiron disulfide PSI-MOD MOD:00864 tris-L-cysteinyl L-histidino diiron disulfide PDBCC FES Fe2/S2 (inorganic) cluster CYS CYS CYS HIS FES SG FE1,FE2 SG FE1,FE2 SG FE1,FE2 ND1 FE1,FE2 natural crosslink4 2Fe-2S metalloprotein 0202 A modification that effectively oxygenates C5 of an L-leucine residue to form a (2S,4R)-5-oxoleucine. (2S,4R)-2-amino-5-oxo-4-methylpentanoic acid PDBCC LED (4R)-5-oxo-L-leucine RESID AA0444 (2S,4R)-5-oxoleucine PSI-MOD MOD:01374 (2S,4R)-5-oxoleucine LED hypothetical modified residue 0204 A protein modification that effectively converts an L-isoleucine residue to a (2S,3R,4R)-4,5-dihydroxyisoleucine. (2S,3R,4R)-2-amino-4,5-dihydroxy-3-methylpentanoic acid PDBCC ILX (2S,3R,4R)-4,5-dihydroxyisoleucine RESID AA0449 (2S,3R,4R)-4,5-dihydroxyisoleucine PSI-MOD MOD:01378 (2S,3R,4R)-4,5-dihydroxyisoleucine ILX natural modified residue hydroxylation 0205 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. 2-((2R)-2-amino-2carboxyethyl)sulfinyl-3-((2S)-2-amino-2-carboxyethyl)-1H-indole RESID AA0451 2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide PSI-MOD MOD:01380 2'-(S-L-cysteinyl)-6'-hydroxy-L-tryptophan sulfoxide CYS TRP SG CD1 natural crosslink2 hydroxylation 0206 A protein modification that effectively converts an L-methionine residue to N,N,N-trimethyl-L-methionine. (1S)-1-carboxy-N,N,N-trimethyl-3-(methylsulfanyl)propan-1-aminium RESID AA0456 N,N,N-trimethyl-L-methionine PSI-MOD MOD:01382 N,N,N-trimethyl-L-methionine PDBCC 4MM (1S)-1-carboxy-N,N,N-trimethyl-3-(methylsulfanyl)propan-1-aminium 4MM natural modified residue thioether bond blocked amino end methylated amino end 0207 A protein modification that effectively cross-links an L-cysteine residue and an L-selenocysteine residues to form L-cysteinyl-L-selenocystine. (2R)-2-amino-3-[([(2R)-2-amino-2-carboxyethyl]sulfanyl)sulfinyl]propanoic acid RESID AA0358 L-cysteinyl-L-selenocysteine PSI-MOD MOD:00363 L-cysteinyl-L-selenocysteine (Cys-Sec) PDBCC SEC 2-amino-3-selenino-propionic acid SYS SEC SG SEG natural crosslink2 redox-active center selenium selenocysteine 0208 A protein modification that effectively converts an L-serine residue to an aminomalonic acid. aminopropanedioic acid PDBCC FGL 2-aminopropanedioic acid RESID AA0458 aminomalonic acid PSI-MOD MOD:01384 aminomalonic acid (Ser) FGL hypothetical modified residue 0209 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. (2S,2'S)-3,3'-[iminobis(4-hydroxybenzene-3,1-diyl)]bis(2-aminopropanoic acid) RESID AA0459 5'-(L-tyros-5'-yl)amino-L-tyrosine PSI-MOD MOD:01787 5'-(L-tyros-5'-yl)amino-L-tyrosine PDBCC TY2 3-amino-L-tyrosine TYR TY2 CE2,CE1 NE2 hypothetical crosslink2 0210 A protein modification that effectively converts an L-threonine residue to O-methyl-L-threonine. (2S,3R)-2-amino-3-methoxybutanoic acid PDBCC OLT O-methyl-L-threonine RESID AA0464 O-methyl-L-threonine PSI-MOD MOD:01387 O-methyl-L-threonine OLT natural modified residue methylated amino acid 0213 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. (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 RESID AA0472 4-(1-hydroxyethyl)-7-isoleucino-2-(threonin-O3-ylcarbonyl)-7,8-dihydroquinolin-8-ol PSI-MOD MOD:01395 4-(1-hydroxyethyl)-7-isoleucino-2-(threonin-O3-ylcarbonyl)-7,8-dihydroquinolin-8-ol PDBCC QUA 8-hydroxy-4-(1-hydroxyethyl)quinoline-2-carboxylic acid THR ILE N QUA CB O1' N C7 natural crosslink2 blocked amino end 0214 A protein modification that effectively converts an L-asparagine residue to a (2S,3S)-3-hydroxyasparagine. (2S,3S)-2-amino-3-hydroxy-4-butanediamic acid PDBCC AHB beta-hydroxyasparagine RESID AA0478 (2S,3S)-3-hydroxyasparagine PSI-MOD MOD:01401 (2S,3S)-3-hydroxyasparagine AHB natural modified residue hydroxylation 0215 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. (2S)-2-amino-3-(4-[(2S)-2-amino-2-carboxyethyl]phenoxy)-3-methylbutanoic acid RESID AA0490 3-(O4'-L-tyrosyl)-L-valine PSI-MOD MOD:01442 3-(O4'-L-tyrosyl)-L-valine VAL TYR CB OH natural crosslink2 0216 A protein modification that effectively converts a source amino acid residue to L-3,3-dihydroxyoalanine. (S)-2-amino-3,3-dihydroxypropanoic acid PDBCC DDZ 3,3-dihydroxy L-alanine RESID AA0492 3,3-dihydroxy-L-alanine PSI-MOD MOD:01448 L-3,3-dihydroxyoalanine DDZ natural modified residue 0217 A protein modification that effectively converts an N-formyl-Lmethionine residue to N-(dihydroxymethyl)-L-methionine. (2S)-2-[(dihydroxymethyl)amino]-4-(methylsulfanyl)butanoic acid PDBCC CXM N-carboxymethionine RESID AA0493 N-(dihydroxymethyl)-L-methionine PSI-MOD MOD:01446 N-(dihydroxymethyl)-L-methionine (fMet) CXM hypothetical modified residue thioether bond blocked amino end formylation pretranslational modification 0218 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. (1Z,2S)-2-carboxy-1-[(3R,4R)-3,4-dihydroxy-5-(phosphonooxy)pentylidene]pyrrolidinium PDBCC PED pentane-3,4-diol-5-phosphate RESID AA0494 N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium PSI-MOD MOD:01454 N-(DNA-1',2'-dideoxyribos-1'-ylidene)-L-prolinium PED N natural modified residue phosphoprotein blocked amino end 0219 A protein modification that effectively crosslinks an L-serine residue and a glycine residue by an ester bond to form O-glycyl-L-serine. (2S)-2-amino-3-[(aminoacetyl)oxy]propanoic acid RESID AA0495 O-glycyl-L-serine PSI-MOD MOD:01585 O-glycyl-L-serine SER GLY C OG C natural crosslink2 blocked carboxyl end 0220 A protein modification that effectively crosslinks an L-threonine residue and a glycine residue by an ester bond to form O-glycyl-L-threonine (2S,3R)-2-amino-3-[(aminoacetyl)oxy]butanoic acid RESID AA0496 O-glycyl-L-threonine PSI-MOD MOD:01586 O-glycyl-L-threonine THR GLY C OG1 C natural crosslink2 blocked carboxyl end 0221 A protein modification that effectively converts an L-serine residue to O-(2-aminoethylphosphoryl)-L-serine. (2S)-2-amino-3-([(2-aminoethoxy)(hydroxy)phosphoryl]oxy)propanoic acid RESID AA0497 O-(2-aminoethylphosphoryl)-L-serine PSI-MOD MOD:01587 O-(2-aminoethylphosphoryl)-L-serine PDBCC OPE phosphoric acid mono-(2-amino-ethyl) ester SER OPE OG,CB P,O1,O2,O3 natural attachment phosphoprotein 0222 A protein modification that effectively converts an L-lysine residue, and an L-methionine residue to S-(L-lysyl)-L-methionine sulfilimine. (E)-N6-([(3S)-3-amino-3-carboxypropyl](methyl)-lambda4-sulfanylidene)-L-lysine RESID AA0501 S-(L-lysyl)-L-methionine sulfilimine PSI-MOD MOD:01602 S-(L-lysyl)-L-methionine sulfilimine LYS MET NZ SD natural crosslink2 0223 A protein modification that effectively converts an L-tyrosine residue to 3'-iodo-L-tyrosine. (2S)-2-amino-3-(4-hydroxy-3-iodophenyl)propanoic acid PDBCC IYR 3-iodo-tyrosine RESID AA0509 3'-iodo-L-tyrosine PSI-MOD MOD:01612 3'-iodo-L-tyrosine IYR natural modified residue iodine 0224 A protein modification that effectively converts an L-tyrosine residue to 3',5'-diiodo-L-tyrosine. (2S)-2-amino-3-(4-hydroxy-3,5-diiodophenyl)propanoic acid PDBCC TYI 3,5-diiodotyrosine RESID AA0510 3',5'-diiodo-L-tyrosine PSI-MOD MOD:01613 3',5'-diiodo-L-tyrosine TYI natural modified residue iodine 0225 A protein modification that effectively cross-links two L-cysteine residues and adds three sulfur atoms to form trithiocystine. (2R,2'R)-3,3'-pentasulfane-1,5-diylbis(2-aminopropanoic acid) RESID AA0513 trithiocystine PSI-MOD MOD:01616 trithiocystine PDBCC S3H trisulfane CYS CYS S3H SG S1 SG S3 natural crosslink2 0226 A protein modification that effectively converts an L-tryptophan residue to a 7'-hydroxy-L-tryptophan. (2S)-2-amino-3-(7-hydroxy-1H-indol-3-yl)propanoic acid PDBCC 0AF 7-hydroxy-L-tryptophan RESID AA0520 7'-hydroxy-L-tryptophan PSI-MOD MOD:01664 7'-hydroxy-L-tryptophan 0AF natural modified residue hydroxylation 0227 A protein modification that effectively converts an L-aspartic acid residue to O4-(8alpha-FAD)-L-aspartate. (2S)-2-amino-4-oxo-4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxybutanoic acid RESID AA0522 O4-(8alpha-FAD)-L-aspartate PSI-MOD MOD:01668 O4-(8alpha-FAD)-L-aspartate PDBCC FAD flavin-adenine dinucleotide ASP FAD OD1,OD2 C8M natural attachment phosphoprotein FAD flavoprotein 0228 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. (2S)-2-amino-4-([(1S,2R)-1-amino-1-carboxypropan-2-yl]oxy)-4-oxobutanoic acid PDBCC AEI threonine-aspartic ester RESID AA0525 O-(L-isoaspartyl)-L-threonine PSI-MOD MOD:01671 O-(L-isoaspartyl)-L-threonine AEI natural modified residue 0229 A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine. (2S)-2-(acetamido)propanoic acid RESID AA0041 N-acetyl-L-alanine PSI-MOD MOD:00050 N-acetyl-L-alanine PDBCC ACE acetyl group ALA N ACE N C natural attachment acetylated amino end 0230 A protein modification that effectively converts an L-aspartic acid residue to N-acetyl-L-aspartic acid. (S)-2-(acetamido)butanedioic acid RESID AA0042 N-acetyl-L-aspartic acid PSI-MOD MOD:00051 N-acetyl-L-aspartic acid PDBCC ACE acetyl group ASP N ACE N C natural attachment acetylated amino end 0231 A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine. (R)-2-acetamido-3-sulfanylpropanoic acid RESID AA0043 N-acetyl-L-cysteine PSI-MOD MOD:00052 N-acetyl-L-cysteine PDBCC ACE acetyl group CYS N ACE N C natural attachment acetylated amino end 0232 A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid. (S)-2-(acetamido)pentanedioic acid RESID AA0044 N-acetyl-L-glutamic acid PSI-MOD MOD:00053 N-acetyl-L-glutamic acid PDBCC ACE acetyl group GLU N ACE N C natural attachment acetylated amino end 0233 A protein modification that effectively converts a glycine residue to N-acetylglycine. 2-(acetamido)ethanoic acid RESID AA0046 N-acetylglycine PSI-MOD MOD:00055 N-acetylglycine PDBCC ACE acetyl group GLY N ACE N C natural attachment acetylated amino end 0234 A protein modification that effectively converts an L-proline residue to N-acetyl-L-proline. (2S)-1-acetyl-2-pyrrolidinecarboxylic acid RESID AA0050 N-acetyl-L-proline PSI-MOD MOD:00059 N-acetyl-L-proline PDBCC ACE acetyl group PRO N ACE N C natural attachment acetylated amino end 0235 A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine. (2S)-2-acetamido-3-hydroxypropanoic acid RESID AA0051 N-acetyl-L-serine PSI-MOD MOD:00060 N-acetyl-L-serine PDBCC ACE acetyl group SER N ACE N C natural attachment acetylated amino end 0236 A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine. (2S,3R)-2-acetamido-3-hydroxybutanoic acid RESID AA0052 N-acetyl-L-threonine PSI-MOD MOD:00061 N-acetyl-L-threonine PDBCC ACE acetyl group THR N ACE N C natural attachment acetylated amino end 0237 A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine. (2S)-2-acetamido-3-(4-hydoxyphenyl)propanoic acid RESID AA0053 N-acetyl-L-tyrosine PSI-MOD MOD:00062 N-acetyl-L-tyrosine PDBCC ACE acetyl group TYR N ACE N C natural attachment acetylated amino end 0238 A protein modification that effectively converts an L-valine residue to N-acetyl-L-valine. (S)-2-acetamido-3-methylbutanoic acid RESID AA0054 N-acetyl-L-valine PSI-MOD MOD:00063 N-acetyl-L-valine PDBCC ACE acetyl group VAL N ACE N C natural attachment acetylated amino end 0239 A protein modification that effectively converts an L-arginine residue to N2-acetyl-L-arginine. (S)-2-acetamido-5-carbamimidamidopentanoic acid RESID AA0354 N2-acetyl-L-arginine PSI-MOD MOD:00359 N2-acetyl-L-arginine PDBCC ACE acetyl group ARG N ACE N C natural attachment acetylated amino end 0240 A protein modification that effectively converts an L-alanine residue to L-alanine amide. (S)-2-aminopropanamide RESID AA0081 L-alanine amide PSI-MOD MOD:00090 L-alanine amide PDBCC NH2 amino group ALA C NH2 C N natural attachment amidated carboxyl end 0241 A protein modification that effectively converts an L-asparagine residue to L-asparagine amide. (S)-2-amino-butanediamide RESID AA0083 L-asparagine amide PSI-MOD MOD:00092 L-asparagine amide PDBCC NH2 amino group ASN C NH2 C N natural attachment amidated carboxyl end 0242 A protein modification that effectively converts an L-aspartic acid residue to L-aspartic acid 1-amide. (S)-2-amino-1-butanediamic acid RESID AA0084 L-aspartic acid 1-amide PSI-MOD MOD:00093 L-aspartic acid 1-amide PDBCC NH2 amino group ASP C NH2 C N natural attachment amidated carboxyl end 0243 A protein modification that effectively converts an L-cysteine residue to L-cysteine amide. (R)-2-amino-3-sulfanylpropanamide RESID AA0085 L-cysteine amide PSI-MOD MOD:00094 L-cysteine amide PDBCC NH2 amino group CYS C NH2 C N natural attachment amidated carboxyl end 0244 A protein modification that effectively converts an L-glutamine residue to L-glutamine amide. (S)-2-amino-pentanediamide RESID AA0086 L-glutamine amide PSI-MOD MOD:00095 L-glutamine amide PDBCC NH2 amino group GLN C NH2 C N natural attachment amidated carboxyl end 0245 A protein modification that effectively converts an L-glutamic acid residue to L-glutamic acid 1-amide. (S)-2-amino-1-pentanediamic acid RESID AA0087 L-glutamic acid 1-amide PSI-MOD MOD:00096 L-glutamic acid 1-amide PDBCC NH2 amino group GLU C NH2 C N natural attachment amidated carboxyl end 0246 A protein modification that effectively converts a glycine residue to glycine amide. 2-aminoethanamide RESID AA0088 glycine amide PSI-MOD MOD:00097 glycine amide PDBCC NH2 amino group GLY C NH2 C N natural attachment amidated carboxyl end 0247 A protein modification that effectively converts an L-histidine residue to L-histidine amide. (S)-2-amino-3-(1H-imidazol-4-yl)propanamide RESID AA0089 L-histidine amide PSI-MOD MOD:00098 L-histidine amide PDBCC NH2 amino group HIS C NH2 C N natural attachment amidated carboxyl end 0248 A protein modification that effectively converts an L-leucine residue to L-leucine amide. (S)-2-amino-4-methylpentanamide RESID AA0091 L-leucine amide PSI-MOD MOD:00100 L-leucine amide PDBCC NH2 amino group LEU C NH2 C N natural attachment amidated carboxyl end 0249 A protein modification that effectively converts an L-lysine residue to L-lysine amide. (S)-2,6-diaminohexanamide RESID AA0092 L-lysine amide PSI-MOD MOD:00101 L-lysine amide PDBCC NH2 amino group LYS C NH2 C N natural attachment amidated carboxyl end 0250 A protein modification that effectively converts an L-proline residue to L-proline amide. (S)-pyrrolidine-2-carboxamide RESID AA0095 L-proline amide PSI-MOD MOD:00104 L-proline amide PDBCC NH2 amino group PRO C NH2 C N natural attachment amidated carboxyl end 0251 A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide. (S)-2-amino-3-(4-hydoxyphenyl)propanamide RESID AA0099 L-tyrosine amide PSI-MOD MOD:00108 L-tyrosine amide PDBCC NH2 amino group TYR C NH2 C N natural attachment amidated carboxyl end 0253 A protein modification that effectively converts an L-alanine residue to N-acetyl-L-alanine. (2S)-2-(acetamido)propanoic acid PDBCC AYA N-acetyl-L-alanine RESID AA0041 N-acetyl-L-alanine PSI-MOD MOD:00050 N-acetyl-L-alanine AYA natural modified residue acetylated amino end 0254 A protein modification that effectively converts an L-cysteine residue to N-acetyl-L-cysteine. (R)-2-acetamido-3-sulfanylpropanoic acid PDBCC SC2 N-acetyl-L-cysteine RESID AA0043 N-acetyl-L-cysteine PSI-MOD MOD:00052 N-acetyl-L-cysteine SC2 natural modified residue acetylated amino end 0255 A protein modification that effectively converts an L-glutamic acid residue to N-acetyl-L-glutamic acid. (S)-2-(acetamido)pentanedioic acid PDBCC NLG N-acetyl-L-glutamic acid RESID AA0044 N-acetyl-L-glutamic acid PSI-MOD MOD:00053 N-acetyl-L-glutamic acid NLG natural modified residue acetylated amino end 0256 A protein modification that effectively converts an L-threonine residue to N-acetyl-L-threonine. (2S,3R)-2-acetamido-3-hydroxybutanoic acid PDBCC THC N-acetyl-L-threonine RESID AA0052 N-acetyl-L-threonine PSI-MOD MOD:00061 N-acetyl-L-threonine THC natural modified residue acetylated amino end 0257 A protein modification that effectively converts an L-serine residue to N-acetyl-L-serine. (2S)-2-acetamido-3-hydroxypropanoic acid PDBCC SAC N-acetyl-L-serine RESID AA0051 N-acetyl-L-serine PSI-MOD MOD:00060 N-acetyl-L-serine SAC natural modified residue acetylated amino end 0258 A protein modification that effectively converts an L-tyrosine residue to N-acetyl-L-tyrosine. (2S)-2-acetamido-3-(4-hydoxyphenyl)propanoic acid PDBCC 3NF N-acetyl-L-tyrosine RESID AA0053 N-acetyl-L-tyrosine PSI-MOD MOD:00062 N-acetyl-L-tyrosine 3NF natural modified residue acetylated amino end 0259 A protein modification that effectively converts an L-methionine to N-acetyl-L-methionine. (2S)-2-acetamido-4-(methylsulfanyl)butanoic acid PDBCC AME N-acetyl-L-methionine RESID AA0049 N-acetyl-L-methionine PSI-MOD MOD:00058 N-acetyl-L-methionine AME natural modified residue thioether bond acetylated amino end 0260 A protein modification that effectively converts a glycine residue to N-methylglycine. methylaminoethanoic acid PDBCC SAR N-methylglycine RESID AA0063 N-methylglycine PSI-MOD MOD:00072 N-methylglycine SAR natural modified residue methylated amino acid methylated amino end 0261 A protein modification that effectively converts an L-arginine residue to L-arginine amide. (S)-2-amino-5-carbamimidamidopentanamide RESID AA0082 L-arginine amide PSI-MOD MOD:00091 L-arginine amide PDBCC NH2 amino group ARG C NH2 C N natural attachment amidated carboxyl end 0262 A protein modification that effectively converts an L-isoleucine residue to L-isoleucine amide. (2S,3S)-2-amino-3-methylpentanamide RESID AA0090 L-isoleucine amide PSI-MOD MOD:00099 L-isoleucine amide PDBCC NH2 amino group ILE NH2 C N natural attachment amidated carboxyl end 0263 A protein modification that effectively converts an L-methionine residue to L-methionine amide. (2S)-2-amino-4-(methylsulfanyl)butanamide RESID AA0093 L-methionine amide PSI-MOD MOD:00102 L-methionine amide PDBCC NH2 amino group MET NH2 C N natural attachment amidated carboxyl end 0264 A protein modification that effectively converts an L-phenylalanine residue to L-phenylalanine amide. (S)-2-amino-3-phenylpropanamide RESID AA0094 L-phenylalanine amide PSI-MOD MOD:00103 L-phenylalanine amide PDBCC NH2 amino group PHE NH2 C N natural attachment amidated carboxyl end 0265 A protein modification that effectively converts an L-proline residue to L-proline amide. (S)-pyrrolidine-2-carboxamide RESID AA0095 L-proline amide PSI-MOD MOD:00104 L-proline amide PDBCC NH2 amino group PRO NH2 C N natural attachment amidated carboxyl end 0266 A protein modification that effectively converts an L-serine residue to L-serine amide. (2S)-2-amino-3-hydroxypropanamide RESID AA0096 L-serine amide PSI-MOD MOD:00105 L-serine amide PDBCC NH2 amino group SER NH2 C N natural attachment amidated carboxyl end 0267 A protein modification that effectively converts an L-serine residue to L-serine amide. (2S)-2-amino-3-hydroxypropanamide PDBCC SET aminoserine RESID AA0096 L-serine amide PSI-MOD MOD:00105 L-serine amide SET natural modified residue amidated carboxyl end 0268 A protein modification that effectively converts an L-threonine residue to L-threonine amide. (2S,3R)-2-amino-3-hydroxybutanamide RESID AA0097 L-threonine amide PSI-MOD MOD:00106 L-threonine amide PDBCC NH2 amino group THR NH2 C N natural attachment amidated carboxyl end 0269 A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide. RESID AA0098 L-tryptophan amide PSI-MOD MOD:00107 L-tryptophan amide PDBCC NH2 amino group TRP NH2 C N natural attachment amidated carboxyl end 0270 A protein modification that effectively converts an L-tryptophan residue to L-tryptophan amide. (2S)-2-amino-3-(1H-indol-3-yl)propanamide PDBCC LTN L-tryptophanamide RESID AA0098 L-tryptophan amide PSI-MOD MOD:00107 L-tryptophan amide LTN natural modified residue amidated carboxyl end 0271 A protein modification that effectively converts an L-tyrosine residue to L-tyrosine amide. (S)-2-amino-3-(4-hydoxyphenyl)propanamide RESID AA0099 L-tyrosine amide PSI-MOD MOD:00108 L-tyrosine amide PDBCC NH2 amino group TYR NH2 C N natural attachment amidated carboxyl end 0272 A protein modification that effectively converts an L-valine residue to L-valine amide. (S)-2-amino-3-methylbutanamide RESID AA0100 L-valine amide PSI-MOD MOD:00109 L-valine amide PDBCC NH2 amino group VAL NH2 C N natural attachment amidated carboxyl end 0273 A protein modification that effectively converts an L-cysteine residue to S-farnesyl-L-cysteine. (2R)-2-amino-3-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trienyl]sulfanylpropanoic acid RESID AA0102 S-farnesyl-L-cysteine PSI-MOD MOD:00109 S-farnesyl-L-cysteine PDBCC FAR farnesyl CYS FAR SG C1 natural attachment lipoprotein prenylation thioether bond 0274 A protein modification that effectively converts an L-cysteine residue to S-geranylgeranyl-L-cysteine. (2R)-2-amino-3-[(2E,6E,10E)-3,7,11,15-tetramethylhexadeca-2,6,10,14-tetraenyl]sulfanylpropanoic acid RESID AA0104 S-geranylgeranyl-L-cysteine PSI-MOD MOD:00113 S-geranylgeranyl-L-cysteine PDBCC GER geran-8-yl geran CYS GER SG C1 natural attachment lipoprotein prenylation thioether bond 0275 A protein modification that effectively converts an L-cysteine, L-serine, or L-tyrosine residue to pyruvic acid. 2-oxopropanoic acid PDBCC PYR pyruvic acid RESID AA0127 pyruvic acid PSI-MOD MOD:00136 pyruvic acid PSI-MOD MOD:00807 pyruvic acid PSI-MOD MOD:01661 pyruvic acid PYR natural modified residue blocked amino end 0276 A protein modification that effectively converts an L-threonine residue into 2-oxobutanoic acid. 2-oxobutanoic acid PDBCC 2KT 2-oxobutanoic acid RESID AA0129 2-oxobutanoic acid PSI-MOD MOD:00138 2-oxobutanoic acid 2KT natural modified residue blocked amino end 0277 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. [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 RESID AA0135 heme-L-cysteine PSI-MOD MOD:00144 heme-L-cysteine PDBCC HEM protoporphyrin IX containing Fe CYS HEM SG * natural attachment chromoprotein heme iron metalloprotein thioether bond 0278 A protein modification that effectively converts an L-tyrosine residue to L-3',4'-dihydroxyphenylalanine. (S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid PDBCC DAH 3,4-dihydroxyphenylalanine RESID AA0146 L-3',4'-dihydroxyphenylalanine PSI-MOD MOD:00155 L-3',4'-dihydroxyphenylalanine DAH natural modified residue hydroxylation 0279 A protein modification that effectively converts an L-tryptophan residue to L-6'-chlorotryptophan. (2S)-2-amino-3-(6-chloro-1H-indol-3-yl)propanoic acid PDBCC 6CW 6-chloro-L-tryptophan RESID AA0180 6'-chloro-L-tryptophan PSI-MOD MOD:00886 L-6'-chlorotryptophan 6CW natural modified residue chlorine 0280 A protein modification that effectively converts an L-threonine residue to dehydrobutyrine. (2Z)-2-aminobut-2-enoic acid PDBCC DBU (2Z)-2-aminobut-2-enoic acid RESID AA0182 (Z)-dehydrobutyrine PSI-MOD MOD:00190 dehydrobutyrine (Thr) DBU natural modified residue 0281 A protein modification that effectively converts an L-serine residue to an amino-terminal lactic acid. 2-hydroxypropanoic acid PDBCC LAC lactic acid RESID AA0186 lactic acid PSI-MOD MOD:00194 lactic acid LAC natural modified residue blocked amino end 0282 A protein modification that effectively converts an L-methionine residue to D-methionine. (R)-2-amino-4-(methylsulfanyl)butanoic acid PDBCC MED D-methionine RESID AA0193 D-methionine PSI-MOD MOD:00200 D-methionine MED natural modified residue D-amino acid 0283 A protein modification that effectively converts an L-phenylalanine residue to D-phenylalanine. (R)-2-amino-3-phenylpropanoic acid PDBCC DPN D-phenylalanine RESID AA0194 D-phenylalanine PSI-MOD MOD:00201 D-phenylalanine DPN natural modified residue D-amino acid 0284 A protein modification that effectively converts a source amino acid residue to D-serine. (R)-2-amino-3-hydroxypropanoic acid PDBCC DSN D-serine RESID AA0195 D-serine PSI-MOD MOD:00891 D-serine DSN natural modified residue D-amino acid 0285 A protein modification that effectively converts an L-leucine residue to D-leucine. (2R)-2-amino-4-methylpentanoic acid PDBCC DLE D-leucine RESID AA0197 D-leucine PSI-MOD MOD:00204 D-leucine DLE natural modified residue D-amino acid 0286 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. (S)-2-amino-3-[4-(5'-adenosine phosphonoxy)phenyl]propanoic acid RESID AA0203 O4'-(phospho-5'-adenosine)-L-tyrosine PSI-MOD MOD:00208 O4'-(phospho-5'-adenosine)-L-tyrosine PDBCC AMP adenosine monophosphate TYR AMP OH P natural attachment phosphoprotein 0287 (2S)-2-amino-5-([amino(phosphonoamino)methylidene]amino)pentanoic acid RESID AA0222 omega-N-phospho-L-arginine PSI-MOD MOD:00227 omega-N-phospho-L-arginine PDBCC PO3 phosphite ion ARG PO3 * P natural attachment phosphoprotein 0288 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. di-mu-sulfido(bis-S-cysteinyliron)(bis-N3'-histidinoiron) RESID AA0225 bis-L-cysteinyl bis-L-histidino diiron disulfide PSI-MOD MOD:00230 bis-L-cysteinyl bis-L-histidino diiron disulfide PDBCC FES Fe2/S2 (inorganic) cluster CYS CYS HIS HIS FES SG FE1,FE2 SG FE1,FE2 ND1 FE1,FE2 ND1 FE1,FE2 natural crosslink4 2Fe-2S metalloprotein Rieske iron-sulfur protein 0289 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. (S)-2-amino-6-(5'-adenosine phosphonamino)hexanoic acid RESID AA0227 N6-(phospho-5'-adenosine)-L-lysine PSI-MOD MOD:00232 N6-(phospho-5'-adenosine)-L-lysine PDBCC AMP adenosine monophospate LYS AMP NZ P natural attachment phosphoprotein 0290 A protein modification that effectively converts an L-cysteine residue to S-glutathionyl-L-cysteine. (2S)-2-amino-3-((2S)-2-((4R)-4-amino-4-carboxyl-1-oxobutyl)amino-3-(carboxylmethyl)amino-3-oxo-propyl)dithio-propanoic acid PDBCC CGL RESID AA0229 L-cysteine glutathione disulfide PSI-MOD MOD:00234 L-cysteine glutathione disulfide PDBCC CGL cystine-glutathione CGL natural modified residue disulfide bond 0291 A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazoline-4-carboxylic acid. (4S)-2-[(1R)-1-amino-2-sulfanylethyl]-4,5-dihydro-1,3-oxazole-4-carboxylic acid RESID AA0239 L-cysteine oxazoline-4-carboxylic acid PSI-MOD MOD:00244 L-cysteine oxazoline-4-carboxylic acid CYS SER C N C OG natural crosslink1 oxazole/thiazole ring 0292 A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-cysteine oxazole-4-carboxylic acid. 2-[(1R)-1-amino-2-sulfanylethyl]-1,3-oxazole-4-carboxylic acid RESID AA0238 L-cysteine oxazole-4-carboxylic acid PSI-MOD MOD:00243 L-cysteine oxazole-4-carboxylic acid CYS SER C N C OG natural crosslink1 oxazole/thiazole ring 0293 A protein modification that effectively crosslinks a glycine residue and an L-serine residue to form glycine oxazole-4-carboxylic acid. 2-aminomethyl-1,3-oxazole-4-carboxylic acid RESID AA0240 glycine oxazole-4-carboxylic acid PSI-MOD MOD:00243 glycine oxazole-4-carboxylic acid GLY SER C N C OG natural crosslink1 oxazole/thiazole ring 0294 A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form glycine thiazole-4-carboxylic acid. 2-(aminomethyl)-1,3-thiazole-4-carboxylic acid RESID AA0241 glycine thiazole-4-carboxylic acid PSI-MOD MOD:00246 glycine thiazole-4-carboxylic acid GLY CYS C N C SG natural crosslink1 oxazole/thiazole ring thioether bond 0295 A protein modification that effectively crosslinks an L-cysteine residue and an L-serine residue to form L-serine thiazole-4-carboxylic acid. 2-[(1S)-1-amino-2-hydroxyethyl]-1,3-thiazole-4-carboxylic acid RESID AA0242 L-serine thiazole-4-carboxylic acid PSI-MOD MOD:00247 L-serine thiazole-4-carboxylic acid SER CYS C N C SG natural crosslink1 oxazole/thiazole ring thioether bond 0296 A protein modification that effectively crosslinks an L-cysteine residue and an L-phenylalanine residue to form L-phenylalanine thiazole-4-carboxylic acid. 2-[(1S)-1-amino-2-phenylethyl]-1,3-thiazole-4-carboxylic acid RESID AA0243 L-phenylalanine thiazole-4-carboxylic acid PSI-MOD MOD:00248 L-phenylalanine thiazole-4-carboxylic acid PHE CYS C N C SG natural crosslink1 oxazole/thiazole ring thioether bond 0297 A protein modification that effectively crosslinks two L-cysteine residues to form L-cysteine thiazole-4-carboxylic acid. 2-[(1S)-1-amino-2-sulfanylethyl]-1,3-thiazole-4-carboxylic acid RESID AA0244 L-cysteine thiazole-4-carboxylic acid PSI-MOD MOD:00249 L-cysteine thiazole-4-carboxylic acid CYS CYS C N C SG natural crosslink1 oxazole/thiazole ring thioether bond 0298 A protein modification that effectively crosslinks an L-cysteine residue and an L-lysine residue to form L-lysine thiazole-4-carboxylic acid. 2-[(1S)-1,5-diaminopentyl]-1,3-thiazole-4-carboxylic acid RESID AA0245 L-lysine thiazole-4-carboxylic acid PSI-MOD MOD:00250 L-lysine thiazole-4-carboxylic acid CYS LYS C SG C N natural crosslink1 oxazole/thiazole ring thioether bond 0299 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. (2S,3S)-2-amino-3-[((Z)-2-aminovinyl)sulfanyl]butanoic acid RESID AA0253 S-(2-aminovinyl)-3-methyl-D-cysteine PSI-MOD MOD:00258 S-(2-aminovinyl)-3-methyl-D-cysteine PDBCC TEE 2-amino-ethenethiol THR TEE CB SG natural attachment blocked carboxyl end lanthionine thioether bond 0300 A protein modification that inserts or replaces a residue with an L-pyrrolysine residue, a natural pretranslational modification. (2R)-2-amino-6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]aminohexanoic acid PDBCC PYH N6-{[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl}-L-lysine RESID AA0321 L-pyrrolysine PSI-MOD MOD:01187 L-pyrrolysine residue PYH natural modified residue pretranslational modification 0301 A protein modification that effectively converts an L-glutamic acid residue to L-2-aminobutanoic acid. (S)-2-aminobutanoic acid PDBCC ABA alpha-aminobutyric acid RESID AA0409 L-2-aminobutanoic acid PSI-MOD MOD:00819 L-2-aminobutanoic acid (Glu) ABA natural modified residue 0302 A protein modification that effectively crosslinks an L-cysteine residue and an L-isoleucine residue to form L-isoleucine thiazole-4-carboxylic acid. 2-[(1S,2S)-1-amino-2-methylbutyl]-1,3-thiazole-4-carboxylic acid RESID AA0466 L-isoleucine thiazole-4-carboxylic acid PSI-MOD MOD:01389 L-isoleucine thiazole-4-carboxylic acid ILE CYS C N C SG natural crosslink1 oxazole/thiazole ring thioether bond 0303 A protein modification that effectively crosslinks an L-cysteine residue and an L-valine residue to form L-valine thiazole-4-carboxylic acid. 2-[(1S)-1-amino-2-methylpropyl]-1,3-thiazole-4-carboxylic acid RESID AA0467 L-valine thiazole-4-carboxylic acid PSI-MOD MOD:01390 L-valine thiazole-4-carboxylic acid VAL CYS C N C SG natural crosslink1 oxazole/thiazole ring thioether bond 0304 A protein modification that effectively converts an L-serine residue to O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine. (2S)-2-amino-3-(2,4-diacetamido-2,4-dideoxy-beta-D-glucopyranosyloxy)propanoic acid RESID AA0499 O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine PSI-MOD MOD:01589 O-(2,4-diacetamido-2,4-dideoxyglucosyl)-L-serine PDBCC DT6 2,4-bis(acetylamino)-1,5-anhydro-2,4-dideoxy-D-glucitol SER DT6 OG C1 natural attachment glycoprotein 0305 A protein modification that effectively converts an L-tyrosine residue to 3'-nitro-L-tyrosine. (2S)-2-amino-3-(4-hydroxy-3-nitrophenyl)propanoic acid PDBCC NIY meta-nitro-tyrosine RESID AA0537 3'-nitro-L-tyrosine PSI-MOD MOD:01786 3-nitro-L-tyrosine NIY natural modified residue 0306 A protein modification that effectively converts an L-tryptophan residue to a 2'-hydroxy-L-tryptophan. (2S)-2-amino-3-(2-hydroxy-1H-indol-3-yl)propanoic acid PDBCC TRO 2-hydroxy-tryptophan RESID AA0542 2'-hydroxy-L-tryptophan PSI-MOD MOD:01816 2'-hydroxy-L-tryptophan TRO artifactual modified residue hydroxylation 0307 A protein modification that effectively converts an L-tryptophan residue to a 2'-oxo-L-tryptophan. (2S)-2-amino-3-[(3S)-2-oxo-2,3-dihydro-1H-indol-3-yl]propanoic acid PDBCC TRO 2-hydroxy-tryptophan RESID AA0543 2'-oxo-L-tryptophan PSI-MOD MOD:01817 oxidation of tryptophan to 2'-oxo-L-tryptophan TRO artifactual modified residue 0308 The amino group of the following amino acid forms a thiopeptide bond. This is an amino(sulfanyl)methylidene in the tautomeric form. 5-hydroxy-2-(3-methylbutanoyl)-1,3-oxazole-4-carbothioic O-acid PDBCC 8LI (4Z)-4-[hydroxy(sulfanyl)methylidene]-2-(3-methylbutanoyl)-1,3-oxazol-5(4H)-one RESID AA0550 2-(3-methylbutanoyl)-5-hydroxy-oxazole-4-carbothionic acid PSI-MOD link to MOD:01844 is broken on PSI-MOD site MOD:01844 2-(3-methylbutanoyl)-5-hydroxy-oxazole-4-carbothionic acid 8LI natural modified residue imidazolinone/oxazolinone ring 0309 The amino group of the following amino acid forms a thiopeptide bond. This is an amino(sulfanyl)methylidene in the tautomeric form 5-hydroxy-2-[(2S)-pyrrolidin-2-yl]-1,3-oxazole-4-carbothioic O-acid PDBCC 66G (4Z)-4-[hydroxy(sulfanyl)methylidene]-2-[(2S)-pyrrolidin-2-yl]-1,3-oxazol-5(4H)-one RESID AA0551 L-proline 5-hydroxy-oxazole-4-carbothionic acid PSI-MOD link to MOD:01844 is broken on PSI-MOD site MOD:01844 L-proline 5-hydroxy-oxazole-4-carbothionic acid 66G natural modified residue imidazolinone/oxazolinone ring 0310 A protein modification that effectively trioxygenates an L-cysteine residue to L-cysteine sulfonic acid. (2R)-2-amino-3-sulfopropanoic acid PDBCC OCS cysteinesulfonic acid RESID AA0556 L-cysteine sulfonic acid PSI-MOD MOD:00460 L-cysteic acid (L-cysteine sulfonic acid) OCS artifactual modified residue 0311 A protein modification that effectively converts a source amino acid residue to an N-formyl-L-methionine, a natural pretranslational modification. (S)-2-formylamino-4-(methylsulfanyl)butanoic acid RESID AA0021 N-formyl-L-methionine PSI-MOD MOD:00030 N-formyl-L-methionine PDBCC FOR formyl group MET N FOR N C attachment natural thioether bond blocked amino end formylation pretranslational modification 0312 A protein modification that effectively converts an L-lysine residue to N6-formyl-L-lysine. (S)-2-amino-6-(formylamino)hexanoic acid RESID AA0211 N6-formyl-L-lysine PSI-MOD MOD:00216 N6-formyl-L-lysine PDBCC FOR formyl group LYS FOR NZ C attachment natural formylation 0313 A protein modification that effectively crosslinks an L-alanine residue and a glycine residue to form L-alanine 5-imidazolinone glycine. (2-[(1S)-1-aminoethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid RESID AA0187 L-alanine 5-imidazolinone glycine PDBCC AYG [(4E)-2-[(1S)-1-aminoethyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid PDBCC CRQ [2-(3-carbamoyl-1-imino-propyl)-4-(4-hydroxy-benzylidene)-5-oxo-4,5-dihydro-imidazol-1-yl]-acetic acid PDBCC MDO {2-[(1S)-1-aminoethyl]-4-methylidene-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid PDBCC X9Q {(2S)-2-[(1S)-1-aminoethyl]-4-benzyl-5-oxo-2,5-dihydro-1H-imidazol-1-yl}acetic acid PSI-MOD MOD:00195 L-alanine 5-imidazolinone glycine AYG,CRQ,MDO,X9Q modified residue natural imidazolinone/oxazolinone ring 0314 A protein modification that effectively crosslinks an L-cysteine residue and a glycine residue to form L-cysteine 5-imidazolinone glycine. (2-[(1R)-1-amino-2-sulfanylethyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid RESID AA0188 L-cysteine 5-imidazolinone glycine PDBCC GYC [(4Z)-2-[(1R)-1-amino-2-mercaptoethyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid PSI-MOD MOD:00196 L-cysteine 5-imidazolinone glycine GYC modified residue natural imidazolinone/oxazolinone ring 0315 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. (2S)-2-amino-3-[1-(5'-adenosine phosphono)imidazol-4-yl]propanoic acid RESID AA0371 1'-(phospho-5'-adenosine)-L-histidine PDBCC AMP adenosine monophosphate PSI-MOD MOD:00376 1'-(phospho-5'-adenosine)-L-histidine HIS AMP NE2 P attachment natural phosphoprotein 0316 a protein modification that effectively forms a O3-(N-acetylaminoglucosyl)serine (2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)propanoic acid RESID AA0398 O-(N-acetylamino)glucosyl-L-serine PDBCC NAG N-acetyl-D-glucosamine PSI-MOD MOD:00805 O-(N-acetylaminoglucosyl)-L-serine SER NAG OG C1 attachment natural glycoprotein 0317 a protein modification that effectively forms a O3-(N-acetylaminoglucosyl)threonine (2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxyglucopyranosyloxy)butanoic acid RESID AA0399 O-(N-acetylamino)glucosyl-L-threonine PDBCC NDG 2-(acetylamino)-2-deoxy-A-D-glucopyranose PSI-MOD MOD:00806 O-(N-acetylaminoglucosyl)-L-threonine THR NDG OG1 C1 attachment natural glycoprotein 0318 A protein modification that effectively crosslinks an L-aspartic acid residue and a glycine residue to form 2-imino-alanine 5-imidazolinone glycine. (2-ethanimidoyl-5-oxo-4,5-dihydro-1H-imidazol-1-yl)acetic acid RESID AA0410 2-imino-alanine 5-imidazolinone glycine PDBCC XYG [(4Z)-2-[(1Z)-ethanimidoyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl]acetic acid PSI-MOD MOD:00820 2-imino-alanine 5-imidazolinone glycine XYG modified residue natural imidazolinone/oxazolinone ring 0319 A protein modification that crosslinks an aspartic acid and the following glycine residue with the formation of (2-aminosuccinimidyl)acetic acid. [(3S)-3-amino-2,5-dioxopyrrolidin-1-yl]acetic acid RESID AA0441 (2-aminosuccinimidyl)acetic acid PDBCC SUI (3-amino-2,5-dioxo-1-pyrrolidinly)acetic acid PSI-MOD MOD:00952 (2-aminosuccinimidyl)acetic acid SUI modified residue hypothetical 320 Metal coordination PDBCC AG silver ion * AG * * natural undefined Metal coordination 321 Metal coordination PDBCC AL aluminum ion * AL * * natural undefined Metal coordination 322 Metal coordination PDBCC AU gold ion * AU * * natural undefined Metal coordination 323 Metal coordination PDBCC AU3 gold 3+ ion * AU3 * * natural undefined Metal coordination 324 Metal coordination PDBCC BA barium ion * BA * * natural undefined Metal coordination 325 Metal coordination PDBCC CA calcium ion * CA * * natural undefined Metal coordination 326 Metal coordination PDBCC CD cadmium ion * CD * * natural undefined Metal coordination 327 Metal coordination PDBCC CE cerium (III) ion * CE * * natural undefined Metal coordination 328 Metal coordination PDBCC CO cobat (II) ion * CO * * natural undefined Metal coordination 329 Metal coordination PDBCC 3CO cobat (III) ion * 3CO * * natural undefined Metal coordination 330 Metal coordination PDBCC CR chromium ion * CR * * natural undefined Metal coordination 331 Metal coordination PDBCC CS cesium ion * CS * * natural undefined Metal coordination 332 Metal coordination PDBCC CU copper (II) ion * CU * * natural undefined Metal coordination 333 Metal coordination PDBCC CU1 copper (I) ion * CU1 * * natural undefined Metal coordination 334 Metal coordination PDBCC CU3 copper (III) ion * CU3 * * natural undefined Metal coordination 335 Metal coordination PDBCC ER3 erbium (III) ion * ER3 * * natural undefined Metal coordination 336 Metal coordination PDBCC EU europium ion * EU * * natural undefined Metal coordination 337 Metal coordination PDBCC EU3 europium (III) ion * EU3 * * natural undefined Metal coordination 338 Metal coordination PDBCC FE Fe (III) ion * FE * * natural undefined Metal coordination 339 Metal coordination PDBCC FE2 Fe (II) ion * FE2 * * natural undefined Metal coordination 341 Metal coordination PDBCC GA gallium (III) ion * GA * * natural undefined Metal coordination 342 Metal coordination PDBCC GD gadolinium ion * GD * * natural undefined Metal coordination 343 Metal coordination PDBCC GD3 gadolinium (III) ion * GD3 * * natural undefined Metal coordination 344 Metal coordination PDBCC HG mercury (II) ion * HG * * natural undefined Metal coordination 345 Metal coordination PDBCC HO holmium ion * HO * * natural undefined Metal coordination 346 Metal coordination PDBCC HO3 holmium (III) ion * HO3 * * natural undefined Metal coordination 347 Metal coordination PDBCC IN indium (III) ion * IN * * natural undefined Metal coordination 348 Metal coordination PDBCC IR iridium ion * IR * * natural undefined Metal coordination 349 Metal coordination PDBCC IR3 iridium (III) ion * IR3 * * natural undefined Metal coordination 350 Metal coordination PDBCC K potassium ion * K * * natural undefined Metal coordination 351 Metal coordination PDBCC LA lanthanum (III) ion * LA * * natural undefined Metal coordination 352 Metal coordination PDBCC LI lithium ion * LI * * natural undefined Metal coordination 353 Metal coordination PDBCC LU lutetium (III) ion * LU * * natural undefined Metal coordination 354 Metal coordination PDBCC MG magnesium ion * MG * * natural undefined Metal coordination 355 Metal coordination PDBCC MN manganese (II) ion * MN * * natural undefined Metal coordination 356 Metal coordination PDBCC MN3 manganese (III) ion * MN3 * * natural undefined Metal coordination 357 Metal coordination PDBCC MO molybdenum ion * MO * * natural undefined Metal coordination 358 Metal coordination PDBCC 4MO molybdenum (IV) ion * 4MO * * natural undefined Metal coordination 359 Metal coordination PDBCC 6MO molybdenum (VI) ion * 6MO * * natural undefined Metal coordination 360 Metal coordination PDBCC NA sodium ion * NA * * natural undefined Metal coordination 361 Metal coordination PDBCC NI nickel (II) ion * NI * * natural undefined Metal coordination 362 Metal coordination PDBCC 3NI nickel (III) ion * 3NI * * natural undefined Metal coordination 363 Metal coordination PDBCC OS osmium ion * OS * * natural undefined Metal coordination 364 Metal coordination PDBCC OS4 osmium (IV) ion * OS4 * * natural undefined Metal coordination 365 Metal coordination PDBCC PB lead (II) ion * PB * * natural undefined Metal coordination 366 Metal coordination PDBCC PD palladium ion * PD * * natural undefined Metal coordination 367 Metal coordination PDBCC PR praseodymium ion * PR * * natural undefined Metal coordination 368 Metal coordination PDBCC PT platinum (II) ion * PT * * natural undefined Metal coordination 369 Metal coordination PDBCC PT4 platinum (IV) ion * PT4 * * natural undefined Metal coordination 370 Metal coordination PDBCC RB rubidium ion * RB * * natural undefined Metal coordination 371 Metal coordination PDBCC RE rhenium ion * RE * * natural undefined Metal coordination 0252 Metal coordination PDBCC RH rhodium ion * RH * * natural undefined Metal coordination 372 Metal coordination PDBCC RH3 rhodium (III) ion * RH3 * * natural undefined Metal coordination 373 Metal coordination PDBCC RU ruthenium ion * RU * * natural undefined Metal coordination 374 Metal coordination PDBCC SM samarium (III) ion * SM * * natural undefined Metal coordination 375 Metal coordination PDBCC SR strontium ion * SR * * natural undefined Metal coordination 376 Metal coordination PDBCC TB terbium (III) ion * TB * * natural undefined Metal coordination 377 Metal coordination PDBCC TL thallium (I) ion * TL * * natural undefined Metal coordination 378 Metal coordination PDBCC U1 uranium ion * U1 * * natural undefined Metal coordination 379 Metal coordination PDBCC V vanadium ion * V * * natural undefined Metal coordination 380 Metal coordination PDBCC W tungsten ion * W * * natural undefined Metal coordination 381 Metal coordination PDBCC Y1 yttrium ion * Y1 * * natural undefined Metal coordination 382 Metal coordination PDBCC YT3 yttrium (III) ion * YT3 * * natural undefined Metal coordination 383 Metal coordination PDBCC YB ytterbium ion * YB * * natural undefined Metal coordination 384 Metal coordination PDBCC YB2 ytterbium (II) ion * YB2 * * natural undefined Metal coordination 385 Metal coordination PDBCC ZN zinc ion * ZN * * natural undefined Metal coordination 0386 A protein modification that effectively converts an L-asparagine residue to an N4-glycosyl-L-asparagine. (S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)amino-4-oxobutanoic acid RESID AA0151 N4-(N-acetylamino)glucosyl-L-asparagine PSI-MOD MOD:00831 N4-(N-acetylamino)glucosyl-L-asparagine PDBCC NDG 2-(acetylamino)-2-deoxy-alpha-D-glucopyranose ASN NDG ND2 C1 natural attachment glycoprotein 0387 A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminogalactosyl)-L-asparagine. (2S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)amino-4-oxobutanoic acid RESID AA0420 N4-(N-acetylamino)galactosyl-L-asparagine PSI-MOD MOD:00832 N4-(N-acetylamino)galactosyl-L-asparagine PDBCC A2G 2-(acetylamino)-2-deoxy-alpha-D-galactopyranose ASN A2G ND2 C1 natural attachment glycoprotein 0388 A protein modification that effectively converts an L-asparagine residue to N4-(N-acetaminogalactosyl)-L-asparagine. (2S)-2-amino-4-(2-acetamido-2-deoxy-beta-D-galactopyranosyl)amino-4-oxobutanoic acid RESID AA0420 N4-(N-acetylamino)galactosyl-L-asparagine PSI-MOD MOD:00832 N4-(N-acetylamino)galactosyl-L-asparagine PDBCC NGA 2-(acetylamino)-2-deoxy-beta-D-galactopyranose ASN NGA ND2 C1 natural attachment glycoprotein 0389 A protein modification that effectively converts an L-asparagine residue to N4-glucosyl-asparagine. (S)-2-amino-4-(D-glucopyranosyl)amino-4-oxobutanoic acid RESID AA0421 N4-glucosyl-L-asparagine PSI-MOD MOD:00833 N4-glucosyl-L-asparagine PDBCC BGC beta-D-glucopyranose ASN BGC ND2 C1 natural attachment glycoprotein 0390 A protein modification that effectively converts an L-asparagine residue to N4-glucosyl-asparagine. (S)-2-amino-4-(D-glucopyranosyl)amino-4-oxobutanoic acid RESID AA0421 N4-glucosyl-L-asparagine PSI-MOD MOD:00833 N4-glucosyl-L-asparagine PDBCC GLC alpha-D-glucopyranose ASN GLC ND2 C1 natural attachment glycoprotein 0391 A protein modification that effectively converts an L-arginine residue to N4-glucosyl-arginine. (S)-2-amino-5-[beta-glucopyranosyl(imino(methylamino)methyl)amino]pentanoic acid RESID AA0327 omega-N-glucosyl-L-arginine PSI-MOD MOD:00332 omega-N-glucosyl-L-arginine PDBCC BGC beta-D-glucopyranose ARG BGC NH1,NH2 C1 natural attachment glycoprotein 0392 A protein modification that effectively converts an L-arginine residue to N4-glucosyl-arginine. (S)-2-amino-5-[beta-glucopyranosyl(imino(methylamino)methyl)amino]pentanoic acid RESID AA0327 omega-N-glucosyl-L-arginine PSI-MOD MOD:00332 omega-N-glucosyl-L-arginine PDBCC GLC alpha-D-glucopyranose ARG GLC NH1,NH2 C1 natural attachment glycoprotein 0393 A protein modification that effectively converts an L-cysteine residue to S-(N-acetylamino)glucosyl-L-cysteine. (2R)-2-amino-3-[(beta-D-2-[N-acetylamino]-2-deoxyglucopyranosyl)sulfanyl]propanoic acid RESID AA0560 S-(N-acetylamino)glucosyl-L-cysteine PSI-MOD MOD:01858 S-(N-acetylamino)glucosyl-L-cysteine PDBCC NAG N-acetyl-D-glucosamine CYS NAG SG C1 natural attachment glycoprotein thioether bond 0394 A protein modification that effectively converts an L-cysteine residue to S-(N-acetylamino)glucosyl-L-cysteine. (2R)-2-amino-3-[(beta-D-2-[N-acetylamino]-2-deoxyglucopyranosyl)sulfanyl]propanoic acid RESID AA0560 S-(N-acetylamino)glucosyl-L-cysteine PSI-MOD MOD:01858 S-(N-acetylamino)glucosyl-L-cysteine PDBCC NDG 2-(acetylamino)-2-deoxy-alpha-D-glucopyranose CYS NDG SG C1 natural attachment glycoprotein thioether bond 0395 A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine. (2R)-2-amino-3-[(beta-D-glucopyranosyl)sulfanyl]propanoic acid RESID AA0152 S-glucosyl-L-cysteine PSI-MOD MOD:00161 S-glucosyl-L-cysteine PDBCC BGC beta-D-glucopyranose CYS BGC SG C1 natural attachment glycoprotein thioether bond 0396 A protein modification that effectively converts an L-cysteine residue to S-glucosylated L-cysteine. (2R)-2-amino-3-[(beta-D-glucopyranosyl)sulfanyl]propanoic acid RESID AA0152 S-glucosyl-L-cysteine PSI-MOD MOD:00161 S-glucosyl-L-cysteine PDBCC GLC alpha-D-glucopyranose CYS GLC SG C1 natural attachment glycoprotein thioether bond 0397 A protein modification that effectively converts an L-cysteine residue to S-galactosyl-L-cysteine. (R)-2-amino-3-(beta-D-galactopyranosylsulfanyl)propanoic acid RESID AA0392 S-galactosyl-L-cysteine deprecated PSI-MOD MOD:00799 S-galactosyl-L-cysteine PDBCC GLA alpha-D-galactopyranose CYS GLA SG C1 natural attachment glycoprotein thioether bond 0398 A protein modification that effectively converts an L-cysteine residue to S-galactosyl-L-cysteine. (R)-2-amino-3-(beta-D-galactopyranosylsulfanyl)propanoic acid RESID AA0392 S-galactosyl-L-cysteine deprecated PSI-MOD MOD:00799 S-galactosyl-L-cysteine PDBCC GAL beta-D-galactopyranose CYS GAL SG C1 natural attachment glycoprotein thioether bond 0399 a protein modification that effectively forms a O3-(N-acetylaminoglucosyl)serine (2S)-2-amino-3-(2-acetamido-2-deoxy-beta-D-glucopyranosyloxy)propanoic acid RESID AA0398 O-(N-acetylamino)glucosyl-L-serine PDBCC NDG 2-(acetylamino)-2-deoxy-alpha-D-glucopyranose PSI-MOD MOD:00805 O-(N-acetylaminoglucosyl)-L-serine SER NDG OG C1 attachment natural glycoprotein 0400 A protein modification that effectively converts an L-serine residue to O3-beta-glucosylated L-serine. (S)-2-amino-3-(beta-D-glucopyranosyloxy)propanoic acid RESID AA0397 O-glucosyl-L-serine PSI-MOD MOD:00804 O-glucosyl-L-serine PDBCC BGC beta-D-glucopyranose SER BGC OG C1 natural attachment glycoprotein 0401 A protein modification that effectively converts an L-serine residue to O3-beta-glucosylated L-serine. (S)-2-amino-3-(beta-D-glucopyranosyloxy)propanoic acid RESID AA0397 O-glucosyl-L-serine PSI-MOD MOD:00804 O-glucosyl-L-serine PDBCC GLC alpha-D-glucopyranose SER GLC OG C1 natural attachment glycoprotein 0402 A protein modification that effectively converts an L-serine residue to O3-galactosylserine. (S)-2-amino-3-(alpha-D-galactopyranosyloxy)propanoic acid RESID AA0400 O-galactosyl-L-serine PSI-MOD MOD:00808 O-glucosyl-L-serine PDBCC GLA alpha-D-galactopyranose SER GLA OG C1 natural attachment glycoprotein 0403 A protein modification that effectively converts an L-serine residue to O3-galactosylserine. (S)-2-amino-3-(alpha-D-galactopyranosyloxy)propanoic acid RESID AA0400 O-galactosyl-L-serine PSI-MOD MOD:00808 O-glucosyl-L-serine PDBCC GAL beta-D-galactopyranose SER GAL OG C1 natural attachment glycoprotein 0404 A protein modification that effectively converts an L-serine residue to an O-fucosylserine. (S)-2-amino-3-(alpha-6-deoxy-D-galactopyranosyloxy)propanoic acid RESID AA0404 O-fucosyl-L-serine PSI-MOD MOD:00812 O-fucosyl-L-serine PDBCC FCA alpha-D-fucose SER FCA OG C1 natural attachment glycoprotein 0405 A protein modification that effectively converts an L-serine residue to an O-fucosylserine. (S)-2-amino-3-(alpha-6-deoxy-D-galactopyranosyloxy)propanoic acid RESID AA0404 O-fucosyl-L-serine PSI-MOD MOD:00812 O-fucosyl-L-serine PDBCC FCB beta-D-fucose SER FCB OG C1 natural attachment glycoprotein 0406 A protein modification that effectively forms a O3-xylosylserine. (S)-2-amino-3-(alpha-D-xylopyranosyloxy)propanoic acid RESID AA0406 O-xylosyl-L-serine deprecated PSI-MOD MOD:00814 O-xylosyl-L-serine PDBCC XYP beta-D-xylopyranose SER XYP OG C1 natural attachment glycoprotein 0407 A protein modification that effectively converts an L-serine residue to O3-mannosylserine. (S)-2-amino-3-(alpha-D-mannopyranosyloxy)propanoic acid RESID AA0402 O-mannosyl-L-serine PSI-MOD MOD:00810 O-mannosyl-L-serine PDBCC MAN alpha-D-mannopyranose SER MAN OG C1 natural attachment glycoprotein 0408 A protein modification that effectively converts an L-serine residue to O3-mannosylserine. (S)-2-amino-3-(alpha-D-mannopyranosyloxy)propanoic acid RESID AA0402 O-mannosyl-L-serine PSI-MOD MOD:00810 O-mannosyl-L-serine PDBCC BMA beta-D-mannopyranose SER BMA OG C1 natural attachment glycoprotein 0409 A protein modification that effectively converts an L-serine residue to O-D-glucuronosyl-L-serine. (2S)-2-amino-3-(beta-D-glucopyranuronosyl)propanoic acid RESID AA0291 O-D-glucuronosyl-L-serine PSI-MOD MOD:00296 O-D-glucuronosyl-L-serine PDBCC GCU alpha-D-glucopyranuronic acid SER GCU OG C1 natural attachment glycoprotein 0410 A protein modification that effectively converts an L-serine residue to O-D-glucuronosyl-L-serine. (2S)-2-amino-3-(beta-D-glucopyranuronosyl)propanoic acid RESID AA0291 O-D-glucuronosyl-L-serine PSI-MOD MOD:00296 O-D-glucuronosyl-L-serine PDBCC BDP beta-D-glucopyranuronic acid SER BDP OG C1 natural attachment glycoprotein 0411 A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminoglucosyl)-L-threonine. (2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxyglucopyranosyloxy)butanoic acid RESID AA0399 O-(N-acetylamino)glucosyl-L-threonine PSI-MOD MOD:00806 O-(N-acetylamino)glucosyl-L-threonine PDBCC NAG N-acetyl-D-glucosamine THR NAG OG1 C1 natural attachment glycoprotein 0412 A protein modification that effectively converts an L-threonine residue to O3-(N-acetylaminoglucosyl)-L-threonine. (2S,3R)-2-amino-3-(alpha-D-2-acetamido-2-deoxyglucopyranosyloxy)butanoic acid RESID AA0399 O-(N-acetylamino)glucosyl-L-threonine PSI-MOD MOD:00806 O-(N-acetylamino)glucosyl-L-threonine PDBCC NDG 2-(acetylamino)-2-deoxy-A-D-glucopyranose THR NDG OG1 C1 natural attachment glycoprotein 0413 A protein modification that effectively converts an L-threonine residue to O-glucosylated L-threonine. O-glucosyl-L-threonine PDBCC BGC beta-D-glucopyranose THR BGC OG1 C1 natural attachment glycoprotein 0414 A protein modification that effectively converts an L-threonine residue to O-glucosylated L-threonine. O-glucosyl-L-threonine PDBCC GLC alpha-D-glucopyranose THR GLC OG1 C1 natural attachment glycoprotein 0415 A protein modification that effectively converts an L-threonine residue to O3-galactosylthreonine. (2S,3R)-2-amino-3-(alpha-D-galactopyranosyloxy)butanoic acid RESID AA0401 O-galactosyl-L-threonine PSI-MOD MOD:00809 O-galactosyl-L-threonine PDBCC GLA alpha-D-galactopyranose THR GLA OG1 C1 natural attachment glycoprotein 0416 A protein modification that effectively converts an L-threonine residue to O3-galactosylthreonine. (2S,3R)-2-amino-3-(alpha-D-galactopyranosyloxy)butanoic acid RESID AA0401 O-galactosyl-L-threonine PSI-MOD MOD:00809 O-galactosyl-L-threonine PDBCC GAL beta-D-galactopyranose THR GAL OG1 C1 natural attachment glycoprotein 0417 A protein modification that effectively converts an threonine residue to an O-fucosylthreonine. (2S,3R)-2-amino-3-(alpha-6-deoxy-D-galactopyranosyloxy)butanoic acid RESID AA0405 O-fucosyl-L-threonine PSI-MOD MOD:00813 O-fucosyl-L-threonine PDBCC FCA alpha-D-fucose THR FCA OG1 C1 natural attachment glycoprotein 0418 A protein modification that effectively converts an threonine residue to an O-fucosylthreonine. (2S,3R)-2-amino-3-(alpha-6-deoxy-D-galactopyranosyloxy)butanoic acid RESID AA0405 O-fucosyl-L-threonine PSI-MOD MOD:00813 O-fucosyl-L-threonine PDBCC FCB beta-D-fucose THR FCB OG1 C1 natural attachment glycoprotein 0419 A protein modification that effectively forms a O3-mannosylthreonine (2S,3R)-2-amino-3-(alpha-D-mannopyranosyloxy)butanoic acid RESID AA0403 O-mannosyl-L-threonine PSI-MOD MOD:00811 O-mannosyl-L-threonine PDBCC MAN alpha-D-mannopyranose THR MAN OG1 C1 natural attachment glycoprotein 0420 A protein modification that effectively forms a O3-mannosylthreonine (2S,3R)-2-amino-3-(alpha-D-mannopyranosyloxy)butanoic acid RESID AA0403 O-mannosyl-L-threonine PSI-MOD MOD:00811 O-mannosyl-L-threonine PDBCC BMA beta-D-mannopyranose THR BMA OG1 C1 natural attachment glycoprotein 0421 A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine. (S)-2-amino-3-(4-alpha-glucopyranosyloxy)phenylpropanoic acid RESID AA0157 O4'-glucosyl-L-tyrosine PSI-MOD MOD:00166 O4'-glucosyl-L-tyrosine PDBCC BGC beta-D-glucopyranose TYR BGC OH C1 natural attachment glycoprotein 0422 A protein modification that effectively converts an L-tyrosine residue to O4'-glucosyl-tyrosine. (S)-2-amino-3-(4-alpha-glucopyranosyloxy)phenylpropanoic acid RESID AA0157 O4'-glucosyl-L-tyrosine PSI-MOD MOD:00166 O4'-glucosyl-L-tyrosine PDBCC GLC alpha-D-glucopyranose TYR GLC OH C1 natural attachment glycoprotein 0423 A protein modification that effectively converts an L-tyrosine residue to O-galactosyl-tyrosine. O-galactosyl-L-tyrosine PDBCC GAL alpha-D-glucopyranose TYR GAL OH C1 natural attachment glycoprotein 0424 A protein modification that effectively converts an L-tyrosine residue to O-galactosyl-tyrosine. O-galactosyl-L-tyrosine PDBCC GAL beta-D-galactopyranose TYR GAL OH C1 natural attachment glycoprotein 0425 A protein modification that effectively converts an L-tyrosine residue to O-galactosyl-tyrosine. O-galactosyl-L-tyrosine PDBCC GLA alpha-D-galactopyranose TYR GLA OH C1 natural attachment glycoprotein 0426 A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan. (2S)-2-amino-3-(2-alpha-mannopyranosyl-1H-indol-3-yl)propanoic acid RESID AA0217 2'-alpha-mannosyl-L-tryptophan PSI-MOD MOD:00222 2'-alpha-mannosyl-L-tryptophan PDBCC MAN alpha-D-mannopyranose TRP MAN CD1 C1 natural attachment glycoprotein 0427 A protein modification that effectively converts an L-tryptophan residue to 2'-alpha-mannosyl-L-tryptophan. (2S)-2-amino-3-(2-alpha-mannopyranosyl-1H-indol-3-yl)propanoic acid RESID AA0217 2'-alpha-mannosyl-L-tryptophan PSI-MOD MOD:00222 2'-alpha-mannosyl-L-tryptophan PDBCC BMA beta-D-mannopyranose TRP BMA CD1 C1 natural attachment glycoprotein 0428 A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine. 2-(glucuronoylamino)ethanoic acid RESID AA0058 N-D-glucuronoyl-glycine PSI-MOD MOD:00067 N-D-glucuronoylglycine PDBCC GCU alpha-D-glucopyranuronic acid GLY GCU N C6 natural attachment glycoprotein 0429 A protein modification that effectively converts a glycine residue to N-D-glucuronoylglycine. 2-(glucuronoylamino)ethanoic acid RESID AA0058 N-D-glucuronoyl-glycine PSI-MOD MOD:00067 N-D-glucuronoylglycine PDBCC BDP beta-D-glucopyranuronic acid GLY BDP N C6 natural attachment glycoprotein