>TX;AA0000 L-alpha-aminoacid C;Formula: C 2 H 3 N 1 O 1 + A;Formula weight: #chem 57.05 + #phys 57.0215 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 C;Comment: This represents an unknown or unidentified residue. C;Sequence code: X A;Abbreviation: Unk >TX;AA0001 L-alanine N;Alternate names: alpha-alanine; alpha-aminopropionic acid N;Systematic name: (S)-2-aminopropanoic acid A;Cross-references: CAS:56-41-7 C;Formula: C 3 H 5 N 1 O 1 A;Formula weight: #chem 71.08 #phys 71.0371 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 C;Sequence code: A A;Abbreviation: Ala >TX;AA0002 L-arginine N;Alternate names: alpha-amino-delta-guanidinovaleric acid N;Systematic name: (S)-2-amino-5-guanidinopentanoic acid A;Cross-references: CAS:74-79-3 C;Formula: C 6 H 12 N 4 O 1 A;Formula weight: #chem 156.19 #phys 156.1011 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 R;Malinowski, D.P.; Friedovich, I. Biochemistry 18, 5909-5917, 1979 A;Title: Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase. A;Reference number: A90436; MUID:80088307 A;Note: chemical modification of an active site arginine C;Sequence code: R A;Abbreviation: Arg F;/Active site: Arg >TX;AA0003 L-asparagine N;Alternate names: alpha-amino-beta-carbamylpropionic acid; alpha-aminosuccinamic acid; aspartic acid beta-amide N;Systematic name: (S)-2-amino-4-butanediamic acid A;Cross-references: CAS:70-47-3 C;Formula: C 4 H 6 N 2 O 2 A;Formula weight: #chem 114.10 #phys 114.0429 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 R;Drenth, J.; Jansonius, J.N.; Koekoek, R.; Swen, H.M.; Wolthers, B.G. Nature 218, 929-932, 1968 A;Title: Structure of papain. A;Reference number: A93155; MUID:69006973 A;Contents: X-ray crystallography, 2.8 angstroms C;Sequence code: N A;Abbreviation: Asn F;/Active site: Asn >TX;AA0004 L-aspartic acid N;Alternate names: aminosuccinic acid N;Systematic name: (S)-2-aminobutanedioic acid A;Cross-references: CAS:56-84-8 C;Formula: C 4 H 5 N 1 O 3 A;Formula weight: #chem 115.09 #phys 115.0269 C;Correction formula: C 0 H 0 N 0 O 0 A;Correction weight: #chem 0.00 #phys 0.0000 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 03-Dec-1999 R;Blow, D.M.; Birktoft, J.J.; Hartley, B.S. Nature 221, 337-340, 1969 A;Title: Role of a buried acid group in the mechanism of action of chymotrypsin. A;Reference number: A93158; MUID:69106266 R;Birktoft, J.J.; Blow, D.M.; Henderson, R.; Steitz, T.A. Philos. Trans. R. Soc. Lond. B257, 67-76, 1970 A;Title: The structure of alpha-chymotrypsin. A;Reference number: A93754 A;Note: X-ray crystallography R;Sepulveda, P.; Marciniszyn Jr., J.; Liu, D.; Tang, J. J. Biol. Chem. 250, 5082-5088, 1975 A;Title: Primary structure of porcine pepsin. III. Amino acid sequence of a cyanogen bromide fragment, CB2A, and the complete structure of porcine pepsin. A;Reference number: A92179; MUID:75211282 R;Andreeva, N.S.; Gustchina, A.E.; Fedorov, A.A.; Shutzkever, N.E.; Volnova, T.V. Adv. Exp. Med. Biol. 95, 23-31, 1977 A;Title: X-ray crystallographic studies of pepsin. A;Reference number: A90016; MUID:78077917 A;Note: X-ray crystallography, 2.7-3.0 angstroms R;Jedrzejewski, P.T.; Girod, A.; Tholey, A.; Koenig, N.; Thullner, S.; Kinzel, V.; Bossemeyer, D. Protein Sci. 7, 457-469, 1998 A;Title: A conserved deamidation site at Asn 2 in the catalytic subunit of mammalian cAMP-dependent protein kinase detected by capillary LC-MS and tandem mass spectrometry. A;Reference number: A58734 A;Note: chromatographic and mass spectrographic identification C;Comment: Some active site aspartic acids may form transient covalent bonds with substrates that are not distinguished in PIR features. C;Comment: Only enzymatic deamidations of asparagine to aspartic acid have the modified site feature. This modification is coupled with myristylation of the immediately preceding glycine (see RESID:AA0059). C;Sequence code: D #link ASP; N #link ASN A;Conditions: incidental to RESID:AA0059 #link ASN A;Abbreviation: Asp F;/Active site: Asp #link ASP F;/Modified site: aspartic acid (Asn) #link ASN >TX;AA0005 L-cysteine N;Alternate names: alpha-amino-beta-thiolpropionic acid N;Systematic name: (R)-2-amino-3-mercaptopropanoic acid A;Cross-references: CAS:52-90-4 C;Formula: C 3 H 5 N 1 O 1 S 1 A;Formula weight: #chem 103.15 #phys 103.0092 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 R;Grau, U.M.; Trommer, W.E.; Rossmann, M.G. J. Mol. Biol. 151, 289-307, 1981 A;Title: Structure of the active ternary complex of pig heart lactate dehydrogenase with S-lac-NAD at 2.7 angstrom resolution. A;Reference number: A92870; MUID:82170431 A;Note: X-ray crystallography, 2.7 angstroms R;Takishima, K.; Mamiya, G. Protein Seq. Data Anal. 1, 103-106, 1987 A;Title: Location of the essential cysteine residue of jack bean urease. A;Reference number: S03364; MUID:88190054 R;Wagner, A.F.V.; Frey, M.; Neugebauer, F.A.; Schaefer, W.; Knappe, J. Proc. Natl. Acad. Sci. U.S.A. 89, 996-1000, 1992 A;Title: The free radical in pyruvate formate-lyase is located on glycine-734. A;Reference number: A46565; MUID:92141244 A;Note: evidence for intermediate cysteine thiyl radical C;Comment: Some active site cysteines may form transient covalent bonds with substrates that are not distinguished in PIR features. C;Sequence code: C A;Abbreviation: Cys F;/Active site: Cys F;/Active site: Cys (cysteine thiyl radical intermediate) >TX;AA0006 L-glutamic acid N;Alternate names: alpha-aminoglutaric acid N;Systematic name: (S)-2-aminopentanedioic acid A;Cross-references: CAS:56-86-0 C;Formula: C 5 H 7 N 1 O 3 A;Formula weight: #chem 129.12 #phys 129.0426 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 R;Kimmel, M.T.; Plummer Jr., T.H. J. Biol. Chem. 247, 7864-7869, 1972 A;Title: Identification of a glutamic acid at the active center of bovine carboxypeptidase B. A;Reference number: A92119; MUID:73061487 R;Schmid, M.F.; Herriott, J.R. J. Mol. Biol. 103, 175-190, 1976 A;Title: Structure of carboxypeptidase B at 2.8 angstrom resolution. A;Reference number: A92839; MUID:76265065 A;Note: X-ray crystallography, 2.8 angstroms R;Hartman, F.C. Biochemistry 10, 146-154, 1971 A;Title: Haloacetol phosphates. Characterization of the active site of rabbit muscle triose phosphate isomerase. A;Reference number: A90351; MUID:71058464 R;Katzin, B.J.; Collins, E.J.; Robertus, J.D. Proteins 10, 251-259, 1991 A;Title: Structure of ricin A-chain at 2.5 angstroms. A;Reference number: A48239 A;Note: X-ray crystallography, 2.5 angstroms C;Comment: Some active site glutamic acids may form transient covalent bonds with substrates that are not distinguished in PIR features. C;Sequence code: E A;Abbreviation: Glu F;/Active site: Glu >TX;AA0007 L-glutamine N;Alternate names: alpha-amino-gamma-carbamylbutyric acid; 2-aminoglutaramic acid; glutamic acid 5-amide N;Systematic name: (S)-2-amino-5-pentanediamic acid A;Cross-references: CAS:56-85-9 C;Formula: C 5 H 8 N 2 O 2 A;Formula weight: #chem 128.13 #phys 128.0586 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 C;Sequence code: Q A;Abbreviation: Gln >TX;AA0008 glycine N;Alternate names: aminoacetic acid N;Systematic name: aminoethanoic acid A;Cross-references: CAS:56-40-6 C;Formula: C 2 H 3 N 1 O 1 A;Formula weight: #chem 57.05 #phys 57.0215 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 R;Wagner, A.F.V.; Frey, M.; Neugebauer, F.A.; Schaefer, W.; Knappe, J. Proc. Natl. Acad. Sci. U.S.A. 89, 996-1000, 1992 A;Title: The free radical in pyruvate formate-lyase is located on glycine-734. A;Reference number: A46565; MUID:92141244 A;Note: evidence for stabilized glycine radical C;Sequence code: G A;Abbreviation: Gly F;/Active site: Gly (stable glycyl radical) >TX;AA0009 L-histidine N;Alternate names: alpha-amino-beta-(4-imidazole)propionic acid N;Systematic name: (S)-2-amino-3-(1H-imidazol-4-yl)propanoic acid A;Cross-references: CAS:71-00-1 C;Formula: C 6 H 7 N 3 O 1 A;Formula weight: #chem 137.14 #phys 137.0589 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 R;Bode, W.; Schwager, P. J. Mol. Biol. 98, 693-717, 1975 A;Title: The refined crystal structure of bovine beta-trypsin at 1.8 angstrom resolution. A;Reference number: A92954; MUID:76072097 A;Note: X-ray crystallography, 1.8 angstroms R;Swenson, R.P.; Williams Jr., C.H.; Massey, V. J. Biol. Chem. 258, 497-502, 1983 A;Title: Identification of the histidine residue in D-amino acid oxidase that is covalently modified during inactivation by 5-dimethylaminonaphthalene-1-sulfonyl chloride. A;Reference number: A92423; MUID:83082913 R;Dijkstra, B.W.; Renetseder, R.; Kalk, K.H.; Hol, W.G.J.; Drenth, J. J. Mol. Biol. 168, 163-179, 1983 A;Title: Structure of porcine pancreatic phospholipase A-2 at 2.6 angstrom resolution and comparison with bovine phospholipase A-2. A;Reference number: A92899; MUID:83268704 A;Note: X-ray crystallography, 2.6 angstroms R;van den Bergh, C.J.; Slotboom, A.J.; Verheij, H.M.; de Haas, G.H. J. Cell. Biochem. 39, 379-390, 1989 A;Title: The role of Asp-49 and other conserved amino acids in phospholipases A2 and their importance for enzymatic activity. A;Reference number: A60719 R;Heinrikson, R.L.; Stein, W.H.; Crestfield, A.M.; Moore, S. J. Biol. Chem. 240, 2921-2934, 1965 A;Title: The reactivities of the histidine residues at the active site of ribonuclease toward halo acids of different structures. A;Reference number: A92020 R;Wyckoff, H.W.; Tsernoglou, D.; Hanson, A.W.; Knox, J.R.; Lee, B.; Richards, F.M. J. Biol. Chem. 245, 305-328, 1970 A;Title: The three-dimensional structure of ribonuclease-S. Interpretation of an electron density map at a nominal resolution of 2 A. A;Reference number: A92059; MUID:70092235 A;Note: X-ray crystallography, 2.0 angstroms C;Comment: Some active site histidines may form transient covalent bonds with substrates that are not distinguished in PIR features. C;Sequence code: H A;Abbreviation: His F;/Active site: His >TX;AA0010 L-isoleucine N;Alternate names: alpha-amino-beta-methylvaleric acid; L-threo-isoleucine N;Systematic name: (2S,3S)-2-amino-3-methylpentanoic acid A;Cross-references: CAS:73-32-5 C;Formula: C 6 H 11 N 1 O 1 A;Formula weight: #chem 113.16 #phys 113.0841 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 C;Sequence code: I A;Abbreviation: Ile >TX;AA0011 L-leucine N;Alternate names: alpha-aminoisocaproic acid N;Systematic name: (S)-2-amino-4-methylpentanoic acid A;Cross-references: CAS:61-90-5 C;Formula: C 6 H 11 N 1 O 1 A;Formula weight: #chem 113.16 #phys 113.0841 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 C;Sequence code: L A;Abbreviation: Leu >TX;AA0012 L-lysine N;Alternate names: alpha,epsilon-diaminocaproic acid N;Systematic name: (S)-2,6-diaminohexanoic acid A;Cross-references: CAS:56-87-1 C;Formula: C 6 H 12 N 2 O 1 A;Formula weight: #chem 128.18 #phys 128.0950 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 R;Swenson, R.P.; Williams Jr., C.H.; Massey, V. J. Biol. Chem. 257, 1937-1944, 1982 A;Title: Chemical modification of D-amino acid oxidase. Amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene. A;Reference number: A92359; MUID:82120157 R;Lusty, C.J.; Ratner, S. Proc. Natl. Acad. Sci. U.S.A. 84, 3176-3180, 1987 A;Title: Reaction of argininosuccinase with bromomesaconic acid: role of an essential lysine in the active site. A;Reference number: A28014; MUID:87204100 C;Comment: Some active site lysines may form transient covalent bonds with substrates that are not distinguished in the PIR features. C;Sequence code: K A;Abbreviation: Lys F;/Active site: Lys >TX;AA0013 L-methionine N;Alternate names: alpha-amino-gamma-methylthiolbutyric acid N;Systematic name: (S)-2-amino-4-(methylthio)butanoic acid A;Cross-references: CAS:63-68-3 C;Formula: C 5 H 9 N 1 O 1 S 1 A;Formula weight: #chem 131.20 #phys 131.0405 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 R;Fowler, A.V.; Smith, P.J. J. Biol. Chem. 258, 10204-10207, 1983 A;Title: The active site regions of lacZ and ebg beta-galactosidases are homologous. A;Reference number: A92390; MUID:83290932 A;Note: chemical modification of an active site methionine C;Sequence code: M A;Abbreviation: Met F;/Active site: Met >TX;AA0014 L-phenylalanine N;Alternate names: alpha-amino-beta-phenylpropionic acid N;Systematic name: (S)-2-amino-3-phenylpropanoic acid A;Cross-references: CAS:63-91-2 C;Formula: C 9 H 9 N 1 O 1 A;Formula weight: #chem 147.18 #phys 147.0684 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 C;Sequence code: F A;Abbreviation: Phe F;/Active site: Phe >TX;AA0015 L-proline N;Systematic name: (S)-2-pyrrolidinecarboxylic acid A;Cross-references: CAS:147-85-3 C;Formula: C 5 H 7 N 1 O 1 A;Formula weight: #chem 97.12 #phys 97.0528 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 17-Mar-2000 R;Subramanya, H.S.; Roper, D.I.; Dauter, Z.; Dodson, E.J.; Davies, G.J.; Wilson, K.S.; Wigley, D.B. Biochemistry 35, 792-802, 1996 A;Title: Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism investigated by the crystal structures of two isomerases. A;Reference number: A59214; MUID:96146412 A;Note: evidence for amino-terminal proline active site C;Sequence code: P A;Abbreviation: Pro F;/Active site: Pro >TX;AA0016 L-serine N;Alternate names: alpha-amino-beta-hydroxypropionic acid N;Systematic name: (S)-2-amino-3-hydroxypropanoic acid A;Cross-references: CAS:56-45-1 C;Formula: C 3 H 5 N 1 O 2 A;Formula weight: #chem 87.08 #phys 87.0320 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 C;Sequence code: S A;Abbreviation: Ser F;/Active site: Ser >TX;AA0017 L-threonine N;Alternate names: alpha-amino-beta-hydroxybutyric acid; beta-methylserine; L-threo-threonine N;Systematic name: (2S,3R)-2-amino-3-hydroxybutanoic acid A;Cross-references: CAS:72-19-5 C;Formula: C 4 H 7 N 1 O 2 A;Formula weight: #chem 101.11 #phys 101.0477 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 06-Nov-1998 R;Culp, J.S.; Blytt, H.J.; Hermodson, M.; Butler, L.G. J. Biol. Chem. 260, 8320-8324, 1985 A;Title: Amino acid sequence of the active site peptide of bovine intestinal 5'-nucleotide phosphodiesterase and identification of the active site residue as threonine. A;Reference number: A25274; MUID:85234541 C;Sequence code: T A;Abbreviation: Thr F;/Active site: Thr >TX;AA0018 L-tryptophan N;Alternate names: alpha-amino-beta-(3-indolyl)propionoic acid N;Systematic name: (S)-2-amino-3-(1H-indol-3-yl)propanoic acid A;Cross-references: CAS:73-22-3 C;Formula: C 11 H 10 N 2 O 1 A;Formula weight: #chem 186.22 #phys 186.0793 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 09-Apr-1999 R;Li, Y.F.; Heelis, P.F.; Sancar, A. Biochemistry 30, 6322-6329, 1991 A;Title: Active site of DNA photolyase: tryptophan-306 is the intrinsic hydrogen atom donor essential for flavin radical photoreduction and DNA repair in vitro. A;Reference number: A39573; MUID:91283477 A;Note: spectrographic characterization C;Sequence code: W A;Abbreviation: Trp F;/Active site: Trp F;/Active site: Trp (tryptophyl radical intermediate) >TX;AA0019 L-tyrosine N;Alternate names: alpha-amino-beta-(para-hydroxyphenyl)propionic acid; para-hydroxyphenylalanine N;Systematic name: (S)-2-amino-3-(4-hydoxyphenyl)propanoic acid A;Cross-references: CAS:60-18-4 C;Formula: C 9 H 9 N 1 O 2 A;Formula weight: #chem 163.18 #phys 163.0633 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 06-Nov-1998 R;Takahashi, K.; Stein, W.H.; Moore, S. J. Biol. Chem. 242, 4682-4690, 1967 A;Title: The identification of a glutamic acid residue as part of the active site of ribonuclease T-1. A;Reference number: A92032; MUID:68054788 R;Takahashi, K. J. Biochem. 69, 331-338, 1971 A;Title: The structure and function of ribonuclese T-1. XII. Further studies on rose bengal-catalyzed photooxidation of ribonuclease T-1- identification of a critical histidine residue. A;Reference number: A91926; MUID:71155511 R;Lynn, R.M.; Bjornsti, M.A.; Caron, P.R.; Wang, J.C. Proc. Natl. Acad. Sci. U.S.A. 86, 3559-3563, 1989 A;Title: Peptide sequencing and site-directed mutagenesis identify tyrosine-727 as the active site tyrosine of Saccharomyces cerevisiae DNA topoisomerase I. A;Reference number: S05792; MUID:89264463 R;Swenson, R.P.; Williams Jr., C.H.; Massey, V. J. Biol. Chem. 257, 1937-1944, 1982 A;Title: Chemical modification of D-amino acid oxidase. Amino acid sequence of the tryptic peptides containing tyrosine and lysine residues modified by fluorodinitrobenzene. A;Reference number: A92359; MUID:82120157 R;Nordlund, P.; Sjoeberg, B.M.; Eklund, H. Nature 345, 593-598, 1990 A;Title: Three-dimensional structure of the free radical protein of ribonucleotide reductase. A;Reference number: A44539 A;Note: X-ray crystallography C;Sequence code: Y A;Abbreviation: Tyr F;/Active site: Tyr F;/Active site: Tyr (stable tyrosyl radical) F;/Active site: Tyr (tyrosyl radical intermediate) >TX;AA0020 L-valine N;Alternate names: alpha-aminoisovaleric acid N;Systematic name: (S)-2-amino-3-methylbutanoic acid A;Cross-references: CAS:72-18-4 C;Formula: C 5 H 9 N 1 O 1 A;Formula weight: #chem 99.13 #phys 99.0684 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 C;Sequence code: V A;Abbreviation: Val >TX;AA0021 N-formyl-L-methionine N;Systematic name: (S)-2-formylamino-4-(methylthio)butanoic acid A;Cross-references: CAS:4289-98-9 C;Formula: C 6 H 10 N 1 O 2 S 1 A;Formula weight: #chem 160.22 #phys 160.0432 C;Correction formula: C 1 H 0 O 1 A;Correction weight: #chem 28.01 #phys 27.9949 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 C;Comment: Because this residue is encoded it is not represented by an amino acid 3 letter code or a formylated amino end post-translational process in the feature. C;Sequence code: M A;Conditions: amino-terminal C;Keywords: blocked amino end F;/Modified site: N-formylmethionine >TX;AA0022 L-selenocysteine N;Alternate names: 3-selenylalanine; selenium cysteine N;Systematic name: (R)-2-amino-3-selenylpropanoic acid A;Cross-references: CAS:10236-58-5 C;Formula: C 3 H 5 N 1 O 1 Se 1 A;Formula weight: #chem 150.04 #phys 150.9536 C;Correction formula: C 0 H 0 S -1 Se 1 A;Correction weight: #chem 46.89 #phys 47.9444 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 13-Sep-1996 R;Condell, R.A.; Tappel, A.L. Biochim. Biophys. Acta 709, 304-309, 1982 A;Title: Amino acid sequence around the active-site selenocysteine of rat liver glutathione peroxidase. A;Reference number: A21598; MUID:83101425 R;Gunzler, W.A.; Steffens, G.J.; Grossmann, A.; Kim, S.M.A.; Otting, F.; Wendel, A.; Flohe, L. Hoppe-Seyler's Z. Physiol. Chem. 365, 195-212, 1984 A;Title: The amino-acid sequence of bovine glutathione peroxidase. A;Reference number: A00504; MUID:84184205 R;Sliwkowski, M.X.; Stadtman, T.C. Proc. Natl. Acad. Sci. U.S.A. 85, 368-371, 1988 A;Title: Selenoprotein A of the clostridial glycine reductase complex: purification and amino acid sequence of the selenocysteine-containing peptide. A;Reference number: A28115; MUID:88124843 R;Hill, K.E.; Lloyd, R.S.; Yang, J.G.; Read, R.; Burk, R.F. J. Biol. Chem. 266, 10050-10053, 1991 A;Title: The cDNA for rat selenoprotein P contains 10 TGA codons in the open reading frame. A;Reference number: A40380; MUID:91244760 C;Comment: Because this residue is encoded it is not represented by an amino acid 3 letter code as a post-translational process in the feature. C;Sequence code: C A;Abbreviation: Sec C;Keywords: selenocysteine F;/Modified site: selenocysteine >TX;AA0023 L-aspartic acid or L-asparagine C;Formula: C 4 H 5 N 1 O 3, C 4 H 6 N 2 O 2 A;Formula weight: #chem 115.09, 114.10 #phys 115.0269, 114.0429 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 C;Comment: This represents an uncertain amidation of an aspartic acid. C;Sequence code: B A;Abbreviation: Asx >TX;AA0024 L-glutamic acid or L-glutamine C;Formula: C 5 H 7 N 1 O 3, C 5 H 8 N 2 O 2 A;Formula weight: #chem 129.12, 128.13 #phys 129.0426, 128.0586 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 C;Comment: This represents an uncertain amidation of a glutamic acid. C;Sequence code: Z A;Abbreviation: Glx >TX;AA0025 L-cystine N;Alternate names: bis(alpha-aminopropionic acid)-beta-disulfide N;Systematic name: (R,R)-3,3'-dithiobis(2-aminopropanoic acid) A;Cross-references: CAS:56-89-3 C;Formula: C 6 H 8 N 2 O 2 S 2 A;Formula weight: #chem 204.27 #phys 204.0027 C;Correction formula: C 0 H -2 A;Correction weight: #chem -2.02 #phys -2.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 17-May-1996 R;Sorensen, H.H.; Thomsen, J.; Bayne, S.; Hojrup, P.; Roepstorff, P. Biomed. Environ. Mass Spectrom. 19, 713-720, 1990 A;Title: Strategies for determination of disulphide bridges in proteins using plasma desorption mass spectrometry. A;Reference number: A37448 A;Note: mass spectrographic identification of disulfide bonds R;Yang, C.Y.; Gu, Z.W.; Blanco-Vaca, F.; Gaskell, S.J.; Yang, M.; Massey, J.B.; Gotto Jr., A.M.; Pownall, H.J. Biochemistry 33, 12451-12455, 1994 A;Title: Structure of human apolipoprotein D: locations of the intermolecular and intramolecular disulfide links. A;Reference number: A55901 A;Note: mass spectrographic identification of disulfide bonds R;Balhorn, R.; Corzett, M.; Mazrimas, J.; Watkins, B. Biochemistry 30, 175-181, 1991 A;Title: Identification of bull protamine disulfides. A;Reference number: A37137 A;Note: chemical titration and characterization of disulfide bonds; results from this methodology must be carefully evaluated R;Forman-Kay, J.D.; Clore, G.M.; Wingfield, P.T.; Gronenborn, A.M. Biochemistry 30, 2685-2698, 1991 A;Title: High-resolution three-dimensional structure of reduced recombinant human thioredoxin in solution. A;Reference number: A38953 A;Note: (1)H-NMR and (15)N-NMR analysis; redox-active disulfide bond R;Soderberg, B.O.; Sjoberg, B.M.; Sonnerstam, U.; Branden, C.I. Proc. Natl. Acad. Sci. U.S.A. 75, 5827-5830, 1978 A;Title: Three-dimensional structure of thioredoxin induced by bacteriophage T4. A;Reference number: A93825; MUID:79096070 A;Note: X-ray crystallography, 2.8 angstroms; redox-active disulfide bond R;Bergenhem, N.; Carlsson, U.; Strid, L. Biochim. Biophys. Acta 871, 55-60, 1986 A;Title: The existence of glutathione and cysteine disulfide-linked to erythrocyte carbonic anhydrase from tiger shark. A;Reference number: A30613 A;Note: chemical characterization R;Doermann, P.; Boerchers, T.; Korf, U.; Hojrup, P.; Roepstorff, P.; Spener, F. J. Biol. Chem. 268, 16286-16292, 1993 A;Title: Amino acid exchange and covalent modification by cysteine and glutathione explain isoforms of fatty acid-binding protein occurring in bovine liver. A;Reference number: A47339 A;Note: mass spectrographic detection C;Comment: Most extracellular proteins appear to undergo normal disulfide bond formation spontaneously during secretion. Some proteins require assistance from chaperonins and protein disulfide-isomerase. C;Comment: Binding of free cysteine extracellularly is probably not enzymatically catalyzed. C;Generating enzyme: protein disulfide-isomerase (EC 5.3.4.1) C;Sequence code: C, C A;Conditions: cross-link 2 C;Keywords: disulfide bond; *redox-active disulfide F;/Disulfide bonds: F;/Disulfide bonds: interchain F;/Disulfide bonds: interchain (to ...) F;/Disulfide bonds: redox-active F;/Binding site: cysteine (Cys) (covalent) >TX;AA0026 L-erythro-beta-hydroxyasparagine N;Systematic name: (2S,3R)-2-amino-3-hydroxy-4-butanediamic acid A;Cross-references: CAS:20790-74-3 C;Formula: C 4 H 6 N 2 O 3 A;Formula weight: #chem 130.10 #phys 130.0378 C;Correction formula: C 0 H 0 O 1 A;Correction weight: #chem 16.00 #phys 15.9949 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 R;Arlaud, G.J.; van Dorsselaer, A.; Bell, A.; Mancini, M.; Aude, C.; Gagnon, J. FEBS Lett. 222, 129-134, 1987 A;Title: Identification of erythro-beta-hydroxyasparagine in the EGF-like domain of human C1r. A;Reference number: S02422; MUID:88005128 C;Generating enzyme: peptide-aspartate beta-dioxygenase (EC 1.14.11.16) C;Sequence code: N C;Keywords: beta-hydroxyasparagine F;/Modified site: erythro-beta-hydroxyasparagine (Asn) >TX;AA0027 L-erythro-beta-hydroxyaspartic acid N;Systematic name: (2S,3R)-2-amino-3-hydroxybutanedioic acid A;Cross-references: CAS:7298-98-8 C;Formula: C 4 H 5 N 1 O 4 A;Formula weight: #chem 131.09 #phys 131.0219 C;Correction formula: C 0 H 0 O 1 A;Correction weight: #chem 16.00 #phys 15.9949 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 R;Drakenberg, T.; Fernlund, P.; Roepstorff, P.; Stenflo, J. Proc. Natl. Acad. Sci. U.S.A. 80, 1802-1806, 1983 A;Title: beta-Hydroxyaspartic acid in vitamin K-dependent protein C. A;Reference number: A19316; MUID:83169769 R;McMullen, B.A.; Fujikawa, K.; Kisiel, W.; Sasagawa, T.; Howald, W.N.; Kwa, E.Y.; Weinstein, B. Biochemistry 22, 2875-2884, 1983 A;Title: Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid. A;Reference number: A20362; MUID:83257207 A;Note: mass spectrographic and (1)H-NMR identification R;Kessler, H.; Steuernagel, S.; Will, M.; Jung, G.; Kellner, R.; Gillessen, D.; Kamiyama, T. Helv. Chim. Acta 71, 1924-1929, 1988 A;Title: The structure of the polycyclic nonadecapeptide Ro 09-0198. A;Reference number: A60555 R;Padmanabhan, K.; Padmanabhan, K.P.; Tulinsky, A.; Park, C.H.; Bode, W.; Huber, R.; Blankenship, D.T.; Cardin, A.D.; Kisiel, W. J. Mol. Biol. 232, 947-966, 1993 A;Title: Structure of human des(1-45) factor Xa at 2.2 angstroms resolution. A;Reference number: A49458 A;Note: X-ray crystallography, 2.2 angstroms C;Generating enzyme: peptide-aspartate beta-dioxygenase (EC 1.14.11.16) C;Sequence code: D C;Keywords: beta-hydroxyaspartic acid F;/Modified site: erythro-beta-hydroxyaspartic acid (Asp) >TX;AA0028 5-hydroxy-L-lysine N;Alternate names: alpha,epsilon-diamino-delta-hydroxycaproic acid; L-threo-delta-hydroxylysine N;Systematic name: (2S,5R)-2,6-diamino-5-hydroxyhexanoic acid A;Cross-references: CAS:1190-94-9 C;Formula: C 6 H 12 N 2 O 2 A;Formula weight: #chem 144.17 #phys 144.0899 C;Correction formula: C 0 H 0 O 1 A;Correction weight: #chem 16.00 #phys 15.9949 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 06-Nov-1998 R;Spiess, J.; Noe, B.D. Proc. Natl. Acad. Sci. U.S.A. 82, 277-281, 1985 A;Title: Processing of an anglerfish somatostatin precursor to a hydroxylysine-containing somatostatin 28. A;Reference number: A94038; MUID:85113184 A;Note: chromatographic detection of PTH derivative R;Teshima, T.; Ueki, Y.; Nakai, T.; Shiba, T. Tetrahedron 42, 829-834, 1986 A;Title: Structure determination of lepidopteran, self-defense substance produced by silkworm. A;Reference number: A01768 A;Note: chromatographic detection C;Generating enzyme: procollagen-lysine 5-dioxygenase (EC 1.14.11.4) C;Sequence code: K C;Keywords: hydroxylysine F;/Modified site: 5-hydroxylysine (Lys) >TX;AA0029 3-hydroxy-L-proline N;Alternate names: gamma-hydroxypyrrolidine-alpha-carboxylic acid; L-threo-3-hydroxyproline; 3-trans-hydroxy-L-proline N;Systematic name: (2S,3R)-3-hydroxy-2-pyrrolidinecarboxylic acid A;Cross-references: CAS:4298-08-2 C;Formula: C 5 H 7 N 1 O 2 A;Formula weight: #chem 113.12 #phys 113.0477 C;Correction formula: C 0 H 0 O 1 A;Correction weight: #chem 16.00 #phys 15.9949 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 09-Apr-1999 R;Fietzek, P.P.; Rexrodt, F.W.; Wendt, P.; Stark, M.; Kuehn, K. Eur. J. Biochem. 30, 163-168, 1972 A;Title: The covalent structure of collagen. Amino acid sequence of peptide alpha1-CB6-C2. A;Reference number: A91200; MUID:73042275 A;Note: chromatographic detection R;Waite, J.H. J. Comp. Physiol. B 156, 491-496, 1986 A;Title: Mussel glue from Mytilus californianus Conrad: a comparative study. A;Reference number: A61093; MUID:86279063 A;Note: chromatographic detection C;Generating enzyme: procollagen-proline dioxygenase (EC 1.14.11.2) C;Sequence code: P C;Keywords: hydroxyproline F;/Modified site: 3-hydroxyproline (Pro) >TX;AA0030 4-hydroxy-L-proline N;Alternate names: L-threo-4-hydroxyproline; 4-trans-hydroxy-L-proline N;Systematic name: (2S,4R)-4-hydroxy-2-pyrrolidinecarboxylic acid A;Cross-references: CAS:51-35-4 C;Formula: C 5 H 7 N 1 O 2 A;Formula weight: #chem 113.12 #phys 113.0477 C;Correction formula: C 0 H 0 O 1 A;Correction weight: #chem 16.00 #phys 15.9949 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 09-Apr-1999 R;Waite, J.H. J. Comp. Physiol. B 156, 491-496, 1986 A;Title: Mussel glue from Mytilus californianus Conrad: a comparative study. A;Reference number: A61093; MUID:86279063 C;Generating enzyme: procollagen-proline dioxygenase (EC 1.14.11.2) C;Sequence code: P C;Keywords: hydroxyproline F;/Modified site: 4-hydroxyproline (Pro) >TX;AA0031 2-pyrrolidone-5-carboxylic acid N;Alternate names: pyroglutamic acid; 5-oxoproline N;Systematic name: (S)-5-oxo-2-pyrrolidinecarboxylic acid A;Cross-references: CAS:98-79-3 C;Formula: C 5 H 6 N 1 O 2 A;Formula weight: #chem 112.11 #phys 112.0399 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 09-Apr-1999 R;Podell, D.N.; Abraham, G.N. Biochem. Biophys. Res. Commun. 81, 176-185, 1978 A;Title: A technique for the removal of pyroglutamic acid from the amino terminus of proteins using calf liver pyroglutamate amino peptidase. A;Reference number: A44724; MUID:92089171 C;Comment: This modification can form non-enzymatically from amino-terminal glutamine. C;Generating enzyme: glutaminyl-peptide cyclotransferase (EC 2.3.2.5) C;Sequence code: Q; Z A;Conditions: amino-terminal C;Keywords: pyroglutamic acid F;/Modified site: pyrrolidone carboxylic acid (Gln) F;/Modified site: pyrrolidone carboxylic acid (Glx) >TX;AA0032 L-gamma-carboxyglutamic acid N;Alternate names: 4-carboxyglutamic acid N;Systematic name: (S)-3-amino-1,1,3-propanetricarboxylic acid A;Cross-references: CAS:53861-57-7 C;Formula: C 6 H 7 N 1 O 5 A;Formula weight: #chem 173.13 #phys 173.0324 C;Correction formula: C 1 H 0 O 2 A;Correction weight: #chem 44.01 #phys 43.9898 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Nov-1997 R;Stenflo, J.; Fernlund, P.; Egan, W.; Roepstorff, P. Proc. Natl. Acad. Sci. U.S.A. 71, 2730-2733, 1974 A;Title: Vitamin K dependent modifications of glutamic acid residues in prothrombin. A;Reference number: A44736 A;Note: mass spectrographic and (1)H-NMR identification R;Smalley, D.M.; Preusch, P.C. Anal. Biochem. 172, 241-247, 1988 A;Title: Analysis of gamma-carboxyglutamic acid by reverse phase HPLC of its phenylthiocarbamyl derivative. A;Reference number: A44723 R;Cairns, J.R.; Williamson, M.K.; Price, P.A. Anal. Biochem. 199, 93-97, 1991 A;Title: Direct identification of gamma-carboxyglutamic acid in the sequencing of vitamin K-dependent proteins. A;Reference number: A44566; MUID:92222128 R;Nakamura, T.; Yu, Z.; Fainzilber, M.; Burlingame, A.L. Protein Sci. 5, 524-530, 1996 A;Title: Mass spectrometric-based revision of the structure of a cysteine-rich peptide toxin with gamma-carboxyglutamic acid, TxVIIA, from the sea snail, Conus textile. A;Reference number: A58175; MUID:97022130 A;Note: mass spectrographic identification R;Rigby, A.C.; Baleja, J.D.; Furie, B.C.; Furie, B. Biochemistry 36, 6906-6914, 1997 A;Title: Three-dimensional structure of a gamma-carboxyglutamic acid-containing conotoxin, conantokin G, from the marine snail Conus geographus: the metal-free conformer. A;Reference number: A58650 A;Note: characterization and conformation by (1)H-NMR C;Comment: The gamma-carboxylation of glutamic acid residues is performed by a vitamin K-dependent enzyme. C;Generating enzyme: gamma-glutamyl carboxylase (EC 4.1.1.-) C;Sequence code: E C;Keywords: carboxyglutamic acid F;/Modified site: gamma-carboxyglutamic acid (Glu) >TX;AA0033 L-aspartic 4-phosphoric anhydride N;Alternate names: beta-aspartyl phosphate; phosphoaspartic acid N;Systematic name: (S)-2-aminobutanedioic 4-phosphoric anhydride A;Cross-references: CAS:22138-53-0 C;Formula: C 4 H 6 N 1 O 6 P 1 A;Formula weight: #chem 195.07 #phys 194.9933 C;Correction formula: C 0 H 1 O 3 P 1 A;Correction weight: #chem 79.98 #phys 79.9663 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 09-Apr-1999 R;Bastide, F.; Meissner, G.; Fleischer, S.; Post, R.L. J. Biol. Chem. 248, 8385-8391, 1973 A;Title: Similarity of the active site of phosphorylation of the adenosine triphosphatase for transport of sodium and potassium ions in kidney to that for transport of calcium ions in the sarcoplasmic reticulum of muscle. A;Reference number: A44719; MUID:74054154 A;Note: chromatographic detection; chemical characterization C;Sequence code: D A;Conditions: combinable C;Keywords: phosphoprotein F;/Active site: Asp (aspartylphosphate intermediate) F;/Binding site: phosphate (Asp) (covalent) >TX;AA0034 S-phospho-L-cysteine N;Alternate names: S3-phosphocysteine; cysteine phosphate thioester N;Systematic name: (R)-2-amino-3-phosphothiopropanoic acid A;Cross-references: CAS:115562-30-6 C;Formula: C 3 H 6 N 1 O 4 P 1 S 1 A;Formula weight: #chem 183.13 #phys 182.9755 C;Correction formula: C 0 H 1 O 3 P 1 A;Correction weight: #chem 79.98 #phys 79.9663 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 06-Nov-1998 R;Pas, H.H.; Robillard, G.T. Biochemistry 27, 5835-5839, 1988 A;Title: S-Phosphocysteine and phosphohistidine are intermediates in the phosphoenolpyruvate-dependent mannitol transport catalyzed by Escherichia coli EII(Mtl). A;Reference number: A44533; MUID:89050920 R;Barford, D.; Flint, A.J.; Tonks, N.K. submitted to the Brookhaven Protein Data Bank, September 1994 A;Reference number: A52879; PDB:2HNP A;Note: X-ray crystallography, 2.8 angstroms R;Barford, D.; Flint, A.J.; Tonks, N.K. Science 263, 1397-1404, 1994 A;Title: Crystal structure of human protein tyrosine phosphatase 1B. A;Reference number: A38904 A;Note: X-ray crystallography, 2.8 angstroms R;Zhou, G.; Denu, J.M.; Wu, L.; Dixon, J.E. J. Biol. Chem. 269, 28084-28090, 1994 A;Title: The catalytic role of Cys(124) in the dual specificity phosphatase VHR. A;Reference number: A55447 C;Sequence code: C C;Keywords: phosphoprotein F;/Active site: Cys (phosphocysteine intermediate) F;/Binding site: phosphate (Cys) (covalent) >TX;AA0035 1'-phospho-L-histidine N;Alternate names: histidine-N1'-phosphate; pi-phosphohistidine; pros-phosphohistidine N;Systematic name: (S)-2-amino-3-(1-phosphono-imidazol-4-yl)propanoic acid A;Cross-references: CAS:5789-14-0 C;Formula: C 6 H 8 N 3 O 4 P 1 A;Formula weight: #chem 217.12 #phys 217.0252 C;Correction formula: C 0 H 1 O 3 P 1 A;Correction weight: #chem 79.98 #phys 79.9663 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 09-Apr-1999 R;Hultquist, D.E. Biochim. Biophys. Acta 153, 329-340, 1968 A;Title: The preparation and characterization of phosphorylated derivatives of histidine. A;Reference number: A44718; MUID:68164389 A;Note: chemical synthesis; chemical characterization; spectrographic characterization C;Generating enzyme: protein-histidine pros-kinase (EC 2.7.3.11) C;Sequence code: H A;Conditions: combinable C;Keywords: phosphohistidine; phosphoprotein F;/Active site: His (phosphohistidine intermediate) F;/Binding site: phosphate (His) (covalent) >TX;AA0036 3'-phospho-L-histidine N;Alternate names: histidine-N3'-phosphate; tau-phosphohistidine; tele-phosphohistidine N;Systematic name: (S)-2-amino-3-(3-phosphono-imidazol-4-yl)propanoic acid A;Cross-references: CAS:5789-15-1 C;Formula: C 6 H 8 N 3 O 4 P 1 A;Formula weight: #chem 217.12 #phys 217.0252 C;Correction formula: C 0 H 1 O 3 P 1 A;Correction weight: #chem 79.98 #phys 79.9663 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 30-Jan-1998 R;Hultquist, D.E. Biochim. Biophys. Acta 153, 329-340, 1968 A;Title: The preparation and characterization of phosphorylated derivatives of histidine. A;Reference number: A44718 A;Note: chemical synthesis; chemical characterization; spectrographic characterization R;Herzberg, O. submitted to the Brookhaven Protein Data Bank, September 1992 A;Reference number: A50888; PDB:2HPR A;Note: X-ray crystallography, 2.0 angstroms R;Herzberg, O.; Reddy, P.; Sutrina, S.; Saier Jr., M.H.; Reizer, J.; Kapadia, G. Proc. Natl. Acad. Sci. U.S.A. 89, 2499-2503, 1992 A;Title: Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-angstrom resolution. A;Reference number: A41987; MUID:92196146 A;Note: X-ray crystallography, 2.0 angstroms R;Rajagopal, P.; Waygood, E.B.; Klevit, R.E. Biochemistry 33, 15271-15282, 1994 A;Title: Structural consequences of histidine phosphorylation: NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli. A;Reference number: A56289 A;Note: conformation by (1)H-NMR R;Jones, B.E.; Rajagopal, P.; Klevit, R.E. submitted to the Brookhaven Protein Data Bank, May 1996 A;Reference number: A67240; PDB:2HID A;Note: conformation by (1)H-NMR C;Generating enzyme: protein-histidine tele-kinase (EC 2.7.3.12) C;Sequence code: H A;Conditions: combinable C;Keywords: phosphohistidine; phosphoprotein F;/Active site: His (phosphohistidine intermediate) F;/Binding site: phosphate (His) (covalent) >TX;AA0037 O-phospho-L-serine N;Alternate names: O3-phosphoserine; serine phosphate ester N;Systematic name: (S)-2-amino-3-hydroxypropanoic acid 3-phosphate A;Cross-references: CAS:407-41-0 C;Formula: C 3 H 6 N 1 O 5 P 1 A;Formula weight: #chem 167.06 #phys 166.9984 C;Correction formula: C 0 H 1 O 3 P 1 A;Correction weight: #chem 79.98 #phys 79.9663 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 24-Apr-1997 R;Clark, R.C. Int. J. Biochem. 17, 983-988, 1985 A;Title: The primary structure of avian phosvitins. Contributions through the Edman degradation of methylmercaptovitins prepared from the constituent phosphoproteins. A;Reference number: A91754; MUID:86056531 A;Note: phosphoserine converted to dl-S-methylcysteine for phenylthiohydantoin identification R;Price, P.A.; Rice, J.S.; Williamson, M.K. Protein Sci. 3, 822-830, 1994 A;Title: Conserved phosphorylation of serines in the Ser-X-Glu/Ser(P) sequences of the vitamin K-dependent matrix Gla protein from shark, lamb, rat, cow, and human. A;Reference number: A58570; MUID:94339842 A;Note: improved methodology for conversion to dl-S-methylcysteine C;Generating enzyme: protein-serine kinase (EC 2.7.1.37) C;Sequence code: S A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: phosphate (Ser) (covalent) F;/Active site: Ser (phosphoserine intermediate) >TX;AA0038 O-phospho-L-threonine N;Alternate names: O3-phosphothreonine; threonine phosphate ester N;Systematic name: (2S,3R)-2-amino-3-hydroxybutanoic acid 3-phosphate A;Cross-references: CAS:1114-81-4 C;Formula: C 4 H 8 N 1 O 5 P 1 A;Formula weight: #chem 181.09 #phys 181.0140 C;Correction formula: C 0 H 1 O 3 P 1 A;Correction weight: #chem 79.98 #phys 79.9663 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 04-Dec-1998 R;Lindberg, R.A.; Fischer, W.H.; Hunter, T. Oncogene 8, 351-359, 1993 A;Title: Characterization of a human protein threonine kinase isolated by screening an expression library with antibodies to phosphotyrosine. A;Reference number: I38144; MUID:93149596 A;Note: antibody detection C;Generating enzyme: protein-threonine kinase (EC 2.7.1.37) C;Sequence code: T A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: phosphate (Thr) (covalent) >TX;AA0039 O4'-phospho-L-tyrosine N;Alternate names: O4-phosphotyrosine; tyrosine phosphate N;Systematic name: (S)-2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-phosphate A;Cross-references: CAS:21820-51-9 C;Formula: C 9 H 10 N 1 O 5 P 1 A;Formula weight: #chem 243.16 #phys 243.0297 C;Correction formula: C 0 H 1 O 3 P 1 A;Correction weight: #chem 79.98 #phys 79.9663 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 13-Sep-1996 R;Aebersold, R.; Watts, J.D.; Morrison, H.D.; Bures, E.J. Anal. Biochem. 199, 51-60, 1991 A;Title: Determination of the site of tyrosine phosphorylation at the low picomole level by automated solid-phase sequence analysis. A;Reference number: A44735; MUID:92222121 A;Note: chromatographic detection C;Generating enzyme: protein-tyrosine kinase (EC 2.7.1.112) C;Sequence code: Y A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: phosphate (Tyr) (covalent) F;/Active site: Tyr (phosphotyrosine intermediate) >TX;AA0040 2'-[3-carboxamido-3-(trimethylammonio)propyl]-L-histidine N;Alternate names: diphthamide; 2'-[3-carboxamido-3-(trimethylammonio)propyl]histidine; alpha-(aminocarbonyl)-4-(2-amino-2-carboxyethyl)-N,N,N-trimethyl-1H-imidazole-2-propanaminium N;Systematic name: 2-[(Xi)-3-carboxamido-3-(trimethylammonio)propyl]-4-((R)-2-amino-2-carboxyethyl)-1H-imidazole A;Cross-references: CAS:75645-22-6 C;Formula: C 13 H 22 N 5 O 2 A;Formula weight: #chem 280.35 #phys 280.1773 C;Correction formula: C 7 H 15 N 2 O 1 A;Correction weight: #chem 143.21 #phys 143.1184 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 09-Apr-1999 R;Van Ness, B.G.; Howard, J.B.; Bodley, J.W. J. Biol. Chem. 255, 10710-10716, 1980 A;Title: ADP-ribosylation of elongation factor 2 by diphtheria toxin. NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products. A;Reference number: A43055; MUID:81046927 A;Note: (1)H-NMR and (13)C-NMR identification C;Comment: Diphthamide appears to occur uniquely in translation elongation factor eEF-2. C;Generating enzyme: diphthine synthase (EC 2.1.1.98); dipthine--ammonia ligase (EC 6.3.2.22) C;Sequence code: H C;Keywords: diphthamide F;/Modified site: 2'-[3-carboxamido-3-(trimethylammonio)propyl]histidine (His) >TX;AA0041 N-acetyl-L-alanine N;Alternate names: acetylalanine N;Systematic name: (S)-2-(acetylamino)propanoic acid A;Cross-references: CAS:97-69-8 C;Formula: C 5 H 8 N 1 O 2 A;Formula weight: #chem 114.13 #phys 114.0555 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Coffee, C.J.; Bradshaw, R.A. J. Biol. Chem. 248, 3305-3312, 1973 A;Title: Carp muscle calcium-binding protein. I. Characterization of the tryptic peptides and the complete amino acid sequence of component B. A;Reference number: A92133 A;Note: chemical characterization and mass spectrographic identification R;Kretsinger, R.H.; Nockolds, C.E. J. Biol. Chem. 248, 3313-3326, 1973 A;Title: Carp muscle calcium-binding protein. II. Structure determination and general description. A;Reference number: A92134; MUID:73166580 A;Note: X-ray crystallography, 1.85 angstroms R;Wittmann-Liebold, B.; Greuer, B. FEBS Lett. 95, 91-98, 1978 A;Title: The primary structure of protein S5 from the small subunit of the Escherichia coli ribosome. A;Reference number: A02707; MUID:79065493 A;Note: chemical characterization and mass spectrographic identification R;Swain, A.L.; Kretsinger, R.H.; Amma, E.L. submitted to the Brookhaven Protein Data Bank, January 1990 A;Reference number: A50711; PDB:5CPV A;Note: X-ray crystallography, 1.6 angstroms C;Generating enzyme: peptide alpha-N-acyltransferase (EC 2.3.1.88); ribosomal-protein-alanine N-acetyltransferase (EC 2.3.1.128) C;Sequence code: A A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Ala) F;/Modified site: acetylated amino end (Ala) (in mature form) >TX;AA0042 N-acetyl-L-aspartic acid N;Alternate names: acetylaspartic acid N;Systematic name: (S)-2-(acetylamino)butanedioic acid A;Cross-references: CAS:997-55-7 C;Formula: C 6 H 8 N 1 O 4 A;Formula weight: #chem 158.14 #phys 158.0453 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Kabsch, W.; Mannherz, H.G.; Suck, D.; Pai, E.; Holmes, K.C. submitted to the Brookhaven Protein Data Bank, March 1991 A;Reference number: A50951; PDB:1ATN R;Kabsch, W.; Mannherz, H.G.; Suck, D.; Pai, E.F.; Holmes, K.C. Nature 347, 37-44, 1990 A;Title: Atomic structure of the actin:DNase I complex. A;Reference number: A44645; MUID:90370087 A;Note: X-ray crystallography, 2.8 angstroms R;Martin, P.; Edwards, B. submitted to the Brookhaven Protein Data Bank, April 1992 A;Reference number: A51637; PDB:1BBR R;Martin, P.D.; Robertson, W.; Turk, D.; Huber, R.; Bode, W.; Edwards, B.F.P. J. Biol. Chem. 267, 7911-7920, 1992 A;Title: The structure of residues 7-16 of the Aalpha-chain of human fibrinogen bound to bovine thrombin at 2.3-angstroms resolution. A;Reference number: A44647; MUID:92218459 A;Note: X-ray crystallography, 2.3 angstroms C;Generating enzyme: aspartate N-acetyltransferase (EC 2.3.1.17) C;Sequence code: D A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Asp) F;/Modified site: acetylated amino end (Asp) (in mature form) >TX;AA0043 N-acetyl-L-cysteine N;Alternate names: N-acetylcysteine N;Systematic name: (R)-2-acetylamino-3-mercaptopropanoic acid A;Cross-references: CAS:616-91-1 C;Formula: C 5 H 8 N 1 O 2 S 1 A;Formula weight: #chem 146.19 #phys 146.0276 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Hasegawa, Y.; Ueda, Y.; Watanabe, M.; Morita, F. J. Biochem. 111, 798-803, 1992 A;Title: Studies on amino acid sequences of two isoforms of 17-kDa essential light chain of smooth muscle myosin from porcine aorta media. A;Reference number: JX0215; MUID:92363918 A;Note: mass spectrographic identification C;Sequence code: C A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Cys) F;/Modified site: acetylated amino end (Cys) (in mature form) >TX;AA0044 N-acetyl-L-glutamic acid N;Alternate names: acetylglutamic acid N;Systematic name: (S)-2-(acetylamino)pentanedioic acid A;Cross-references: CAS:1188-37-0 C;Formula: C 7 H 10 N 1 O 4 A;Formula weight: #chem 172.16 #phys 172.0610 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Generating enzyme: peptide alpha-N-acyltransferase (EC 2.3.1.88) C;Sequence code: E A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Glu) F;/Modified site: acetylated amino end (Glu) (in mature form) >TX;AA0045 N-acetyl-L-glutamine N;Alternate names: acetylglutamine N;Systematic name: (S)-2-acetylamino-5-pentanediamic acid A;Cross-references: CAS:2490-97-3 C;Formula: C 7 H 11 N 2 O 3 A;Formula weight: #chem 171.18 #phys 171.0770 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: Q A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Gln) F;/Modified site: acetylated amino end (Gln) (in mature form) >TX;AA0046 N-acetylglycine N;Alternate names: aceturic acid N;Systematic name: 2-(acetylamino)ethanoic acid A;Cross-references: CAS:543-24-8 C;Formula: C 4 H 6 N 1 O 2 A;Formula weight: #chem 100.10 #phys 100.0399 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Luo, Y.; Brayer, G.D. submitted to the Brookhaven Protein Data Bank, August 1994 A;Reference number: A52805; PDB:1HRC A;Note: X-ray crystallography, 1.9 angstroms R;Dickerson, R.E.; Takano, T.; Eisenberg, D.; Kallai, O.B.; Samson, L.; Cooper, A.; Margoliash, E. J. Biol. Chem. 246, 1511-1533, 1971 A;Title: Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 A resolution. A;Reference number: A92076; MUID:71116428 A;Note: X-ray crystallography, 2.8 angstroms R;Tsunasawa, S.; Narita, K. J. Biochem. 92, 607-613, 1982 A;Title: Micro-identification of amino-terminal acetylamino acids in proteins. A;Reference number: A61297 R;Palmiter, R.D.; Gagnon, J.; Walsh, K.A. Proc. Natl. Acad. Sci. U.S.A. 75, 94-98, 1978 A;Title: Ovalbumin: a secreted protein without a transient hydrophobic leader sequence. A;Reference number: A93827; MUID:78116057 A;Note: biosynthesis C;Sequence code: G A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Gly) F;/Modified site: acetylated amino end (Gly) (in mature form) >TX;AA0047 N-acetyl-L-isoleucine N;Alternate names: acetylisoleucine N;Systematic name: (2S,3S)-2-acetylamino-3-methylpentanoic acid A;Cross-references: CAS:3077-46-1 C;Formula: C 8 H 13 N 1 O 2 A;Formula weight: #chem 155.20 #phys 155.0946 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: I A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Ile) F;/Modified site: acetylated amino end (Ile) (in mature form) >TX;AA0048 N2-acetyl-L-lysine N;Alternate names: N2-acetyllysine N;Systematic name: (S)-2-acetylamino-6-aminohexanoic acid A;Cross-references: CAS:1946-82-3 C;Formula: C 8 H 15 N 2 O 2 A;Formula weight: #chem 171.22 #phys 171.1134 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: K A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Lys) F;/Modified site: acetylated amino end (Lys) (in mature form) >TX;AA0049 N-acetyl-L-methionine N;Alternate names: acetylmethionine; methionamine N;Systematic name: (S)-2-acetylamino-4-(methylthio)butanoic acid A;Cross-references: CAS:65-82-7 C;Formula: C 7 H 12 N 1 O 2 S 1 A;Formula weight: #chem 174.25 #phys 174.0589 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Huang, W.Y.; Chirala, S.S.; Wakil, S.J. Arch. Biochem. Biophys. 314, 45-49, 1994 A;Title: Amino-terminal blocking group and sequence of the animal fatty acid synthase. A;Reference number: S51519; MUID:95031085 A;Note: chromatographic and chemical characterization; chemical synthesis C;Generating enzyme: peptide alpha-N-acyltransferase (EC 2.3.1.88) C;Sequence code: M A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Met) F;/Modified site: acetylated amino end (Met) (in mature form) >TX;AA0050 N-acetyl-L-proline N;Alternate names: acetylproline N;Systematic name: (2S)-1-acetyl-2-pyrrolidinecarboxylic acid A;Cross-references: CAS:68-95-1 C;Formula: C 7 H 10 N 1 O 2 A;Formula weight: #chem 140.16 #phys 140.0712 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Sielecki, A.R.; James, M.N.G. submitted to the Brookhaven Protein Data Bank, May 1990 A;Reference number: A50629; PDB:3SGA A;Note: X-ray crystallography, 1.8 angstroms R;Lim, W.A.; Richards, F.M.; Fox, R.O. submitted to the Brookhaven Protein Data Bank, March 1995 A;Reference number: A66617; PDB:1SEM A;Note: X-ray crystallography, 2.0 angstroms R;Houtz, R.L.; Stults, J.T.; Mulligan, R.M.; Tolbert, N.E. Proc. Natl. Acad. Sci. U.S.A. 86, 1855-1859, 1989 A;Title: Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase. A;Reference number: A32395; MUID:89184526 A;Note: mass spectrographic identification C;Sequence code: P A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Pro) F;/Modified site: acetylated amino end (Pro) (in mature form) >TX;AA0051 N-acetyl-L-serine N;Alternate names: N-acetylserine N;Systematic name: (S)-2-acetylamino-3-hydroxypropanoic acid A;Cross-references: CAS:16354-58-8 C;Formula: C 5 H 8 N 1 O 3 A;Formula weight: #chem 130.12 #phys 130.0504 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Strickland, W.N.; Strickland, M.S.; de Groot, P.C.; von Holt, C. Eur. J. Biochem. 109, 151-158, 1980 A;Title: The primary structure of histone H2A from the sperm cell of the sea urchin Parechinus angulosus. A;Reference number: A37574; MUID:81003893 A;Note: N-acetylserine converted by N->O acyl shift to remove blockage R;Wellner, D.; Panneerselvam, C.; Horecker, B.L. Proc. Natl. Acad. Sci. U.S.A. 87, 1947-1949, 1990 A;Title: Sequencing of peptides and proteins with blocked N-terminal amino acids: N-acetylserine or N-acetylthreonine. A;Reference number: A35060; MUID:90175413 A;Note: N-acetylserine converted by N->O acyl shift to remove blockage R;Declercq, J.P.; Tinant, B.; Parello, J.; Rambaud, J. J. Mol. Biol. 220, 1017-1039, 1991 A;Title: Ionic interactions with parvalbumins: crystal structure determination of pike 4.10 parvalbumin in four different ionic environments. A;Reference number: A58798; MUID:91350177 A;Note: X-ray crystallography, 1.65 angstroms R;Declercq, J.P.; Tinant, B.; Parello, J. submitted to the Brookhaven Protein Data Bank, January 1995 A;Reference number: A67144; PDB:1PVB A;Note: X-ray crystallography, 1.75 angstroms C;Generating enzyme: peptide alpha-N-acyltransferase (EC 2.3.1.88) C;Sequence code: S A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Ser) F;/Modified site: acetylated amino end (Ser) (in mature form) >TX;AA0052 N-acetyl-L-threonine N;Alternate names: N-acetylthreonine N;Systematic name: (2S,3R)-2-acetylamino-3-hydroxybutanoic acid A;Cross-references: CAS:17093-74-2 C;Formula: C 6 H 10 N 1 O 3 A;Formula weight: #chem 144.15 #phys 144.0661 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Strickland, W.N.; Strickland, M.S.; de Groot, P.C.; von Holt, C. Eur. J. Biochem. 109, 151-158, 1980 A;Title: The primary structure of histone H2A from the sperm cell of the sea urchin Parechinus angulosus. A;Reference number: A37574; MUID:81003893 A;Note: N-acetylthreonine converted by N->O acyl shift to remove blockage R;Wellner, D.; Panneerselvam, C.; Horecker, B.L. Proc. Natl. Acad. Sci. U.S.A. 87, 1947-1949, 1990 A;Title: Sequencing of peptides and proteins with blocked N-terminal amino acids: N-acetylserine or N-acetylthreonine. A;Reference number: A35060; MUID:90175413 A;Note: N-acetylthreonine converted by N->O acyl shift to remove blockage C;Sequence code: T A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Thr) F;/Modified site: acetylated amino end (Thr) (in mature form) >TX;AA0053 N-acetyl-L-tyrosine N;Alternate names: N-acetyltyrosine N;Systematic name: (S)-2-acetylamino-3-(4-hydoxyphenyl)propanoic acid A;Cross-references: CAS:537-55-3 C;Formula: C 11 H 12 N 1 O 3 A;Formula weight: #chem 206.22 #phys 206.0817 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Kawauchi, H.; Tsubokawa, M.; Muramoto, K. Biochem. Biophys. Res. Commun. 88, 1249-1254, 1979 A;Title: Isolation and primary structure of endorphin from salmon pituitary glands. A;Reference number: A90214; MUID:79255548 A;Note: chromatographic identification of N-acetyl-O5'-dansyl-tyrosine R;Lee, M.S.; Gippert, G.P.; Soman, K.V.; Case, D.A.; Wright, P.E. submitted to the Brookhaven Protein Data Bank, September 1989 A;Reference number: A50391; PDB:1ZNF A;Note: (1)H-NMR characterization, synthetic peptide R;Lee, M.S.; Cavanagh, J.; Wright, P.E. FEBS Lett. 254, 159-164, 1989 A;Title: Complete assignment of the (1)H NMR spectrum of a synthetic zinc finger from Xfin. Sequential resonance assignments and secondary structure. A;Reference number: S05405; MUID:89378224 A;Note: (1)H-NMR characterization, synthetic peptide R;Tong, L. submitted to the Brookhaven Protein Data Bank, November 1995 A;Reference number: A66050; PDB:1LKK A;Note: X-ray crystallography, 1.0 angstroms, synthetic peptide C;Sequence code: Y A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Tyr) F;/Modified site: acetylated amino end (Tyr) (in mature form) >TX;AA0054 N-acetyl-L-valine N;Alternate names: N-acetylvaline N;Systematic name: (S)-2-acetylamino-3-methylbutanoic acid A;Cross-references: CAS:96-81-1 C;Formula: C 7 H 12 N 1 O 2 A;Formula weight: #chem 142.18 #phys 142.0868 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: V A;Conditions: amino-terminal C;Keywords: acetylated amino end F;/Modified site: acetylated amino end (Val) F;/Modified site: acetylated amino end (Val) (in mature form) >TX;AA0055 N6-acetyl-L-lysine N;Alternate names: epsilon-acetyllysine; N(zeta)-acetyllysine N;Systematic name: (S)-2-amino-6-(acetylamino)hexanoic acid A;Cross-references: CAS:692-04-6 C;Formula: C 8 H 14 N 2 O 2 A;Formula weight: #chem 170.21 #phys 170.1055 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 31-Mar-1995 R;Hase, T.; Wakabayashi, S.; Matsubara, H.; Kerscher, L.; Oesterhelt, D.; Rao, K.K.; Hall, D.O. J. Biochem. 83, 1657-1670, 1978 A;Title: Complete amino acid sequence of Halobacterium halobium ferredoxin containing an N(epsilon)-acetyllysine residue. A;Reference number: A00220; MUID:78218096 A;Note: chemical synthesis; chromatographic detection R;Edde, B.; Rossier, J.; Le Caer, J.P.; Berwald-Netter, Y.; Koulakoff, A.; Gros, F.; Denoulet, P. J. Cell. Biochem. 46, 134-142, 1991 A;Title: A combination of posttranslational modifications is responsible for the production of neuronal alpha-tubulin heterogeneity. A;Reference number: A61275 A;Note: chromatographic and radioactive labeling detection C;Generating enzyme: tubulin N-acetyltransferase (EC 2.3.1.108) C;Sequence code: K A;Conditions: combinable C;Keywords: acetyllysine F;/Binding site: acetyl (Lys) (covalent) >TX;AA0056 S-acetyl-L-cysteine N;Alternate names: S-acetylcysteine; cysteine acetate thioester N;Systematic name: (R)-2-amino-3-(acetylthio)propanoic acid A;Cross-references: CAS:15312-11-5 C;Formula: C 5 H 7 N 1 O 2 S 1 A;Formula weight: #chem 145.18 #phys 145.0197 C;Correction formula: C 2 H 2 O 1 A;Correction weight: #chem 42.04 #phys 42.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 24-Apr-1997 R;Wagner, A.F.V.; Frey, M.; Neugebauer, F.A.; Schaefer, W.; Knappe, J. Proc. Natl. Acad. Sci. U.S.A. 89, 996-1000, 1992 A;Title: The free radical in pyruvate formate-lyase is located on glycine-734. A;Reference number: A46565; MUID:92141244 A;Note: evidence for an S-acetylcysteine intermediate C;Sequence code: C C;Keywords: thiolester bond F;/Active site: Cys (S-acetylcysteine intermediate) F;/Binding site: acetyl (Cys) (covalent) >TX;AA0057 N-formylglycine N;Systematic name: formylaminoethanoic acid A;Cross-references: CAS:2491-15-8 C;Formula: C 3 H 4 N 1 O 2 A;Formula weight: #chem 86.07 #phys 86.0242 C;Correction formula: C 1 H 0 O 1 A;Correction weight: #chem 28.01 #phys 27.9949 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Luebke, K.; Matthes, S.; Kloss, G. Experientia 27, 765-767, 1971 A;Title: Isolation and structure of N(alpha)-formyl melittin. A;Reference number: A91267; MUID:72098669 A;Note: gas chromatographic identification C;Sequence code: G A;Conditions: amino terminal C;Keywords: blocked amino end F;/Modified site: formylated amino end (Gly) F;/Modified site: formylated amino end (Gly) (in mature form) >TX;AA0058 D-glucuronyl-N-glycine N;Systematic name: 2-(glucuronoylamino)ethanoic acid A;Cross-references: CAS:62532-50-7 C;Formula: C 8 H 12 N 1 O 7 A;Formula weight: #chem 234.19 #phys 234.0614 C;Correction formula: C 6 H 8 O 6 A;Correction weight: #chem 176.13 #phys 176.0321 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 28-Jan-2000 R;Lin, T.S.; Kolattukudy, P.E. Eur. J. Biochem. 106, 341-351, 1980 A;Title: Structural studies on cutinase, a glycoprotein containing novel amino acids and glucuronic acid amide at the N terminus. A;Reference number: A44665; MUID:80245930 A;Note: chromatographic detection; chemical and spectrographic characterization C;Comment: The alpha glucuronyl form is shown. C;Sequence code: G A;Conditions: amino-terminal F;/Modified site: glucuronylated amino end (Gly) F;/Modified site: glucuronylated amino end (Gly) (in mature form) >TX;AA0059 N-myristoyl-glycine N;Alternate names: N-(1-oxotetradecyl)glycine N;Systematic name: (tetradecanoylamino)ethanoic acid A;Cross-references: CAS:14246-55-0 C;Formula: C 16 H 30 N 1 O 2 + A;Formula weight: #chem 268.42 + #phys 268.2277 + C;Correction formula: C 14 H 26 O 1 + A;Correction weight: #chem 210.36 + #phys 210.1984 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Ozols, J.; Carr, S.A.; Strittmatter, P. J. Biol. Chem. 259, 13349-13354, 1984 A;Title: Identification of the NH2-terminal blocking group of NADH-cytochrome b5 reductase as myristic acid and the complete amino acid sequence of the membrane-binding domain. A;Reference number: A22182; MUID:85030460 A;Note: GC and FAB mass spectrographic characterization R;Dizhoor, A.M.; Ericsson, L.H.; Johnson, R.S.; Kumar, S.; Olshevskaya, E.; Zozulya, S.; Neubert, T.A.; Stryer, L.; Hurley, J.B.; Walsh, K.A. J. Biol. Chem. 267, 16033-16036, 1992 A;Title: The NH-2 terminus of retinal recoverin is acylated by a small family of fatty acids. A;Reference number: A49064 A;Note: mass spectrographic characterization R;Neubert, T.A.; Johnson, R.S.; Hurley, J.B.; Walsh, K.A. J. Biol. Chem. 267, 18274-18277, 1992 A;Title: The rod transducin alpha subunit amino terminus is heterogeneously fatty acylated. A;Reference number: A49065 A;Note: mass spectrographic and chemical characterization R;Griffith, J.P.; Kim, J.L.; Kim, E.E.; Sintchak, M.D.; Thomson, J.A.; Fitzgibbon, M.J.; Fleming, M.A.; Caron, P.R.; Hsiao, K.; Navia, M.A. submitted to the Brookhaven Protein Data Bank, August 1996 A;Reference number: A66708; PDB:1TCO A;Note: X-ray crystallography, 2.5 angstroms R;Griffith, J.P.; Kim, J.L.; Kim, E.E.; Sintchak, M.D.; Thomson, J.A.; Fitzgibbon, M.J.; Fleming, M.A.; Caron, P.R.; Hsiao, K.; Navia, M.A. Cell 82, 507-522, 1995 A;Title: X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. A;Reference number: A56967; MUID:95360994 A;Note: X-ray crystallography, 2.5 angstroms C;Comment: The myristyl group represents a mixture of saturated and unsaturated fatty acids. C;Generating enzyme: glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) C;Sequence code: G A;Conditions: amino-terminal C;Keywords: blocked amino end; lipoprotein; myristylation F;/Modified site: myristylated amino end (Gly) F;/Modified site: myristylated amino end (Gly) (in mature form) >TX;AA0060 N-palmitoyl-L-cysteine N;Alternate names: N-(1-oxahexadecyl)-L-cysteine N;Systematic name: (R)-2-hexadecanoylamino-3-mercaptopropanoic acid A;Cross-references: CAS:67603-49-0 C;Formula: C 19 H 36 N 1 O 2 S 1 + A;Formula weight: #chem 342.57 + #phys 342.2467 + C;Correction formula: C 16 H 30 O 1 + A;Correction weight: #chem 238.42 + #phys 238.2297 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Hantke, K.; Braun, V. Eur. J. Biochem. 34, 284-296, 1973 A;Title: Covalent binding of lipid to protein. A;Reference number: A91204; MUID:73196685 C;Comment: The palmitate represents a mixture of saturated and unsaturated fatty acids. C;Generating enzyme: glycoprotein N-palmitoyltransferase (EC 2.3.1.96) C;Sequence code: C A;Conditions: amino-terminal; incidental to RESID:AA0107 C;Keywords: blocked amino end; lipoprotein F;/Modified site: fatty acylated amino end (Cys) F;/Modified site: fatty acylated amino end (Cys) (in mature form) >TX;AA0061 N-methyl-L-alanine N;Alternate names: N-methylalanine N;Systematic name: (S)-2-methylaminopropanoic acid A;Cross-references: CAS:3913-67-5 C;Formula: C 4 H 7 N 1 O 1 A;Formula weight: #chem 85.11 #phys 85.0528 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Chen, R.; Brosius, J.; Wittmann-Liebold, B.; Schaefer, W. J. Mol. Biol. 111, 173-181, 1977 A;Title: Occurrence of methylated amino acids as N-termini of proteins from Escherichia coli ribosomes. A;Reference number: A44721 A;Note: chemical characterization and synthesis; chromatographic and mass spectrographic identification R;Kamp, R.; Wittmann-Liebold, B. FEBS Lett. 121, 117-122, 1980 A;Title: Primary structure of protein S11 from Escherichia coli ribosomes. A;Reference number: A02722; MUID:81114582 A;Note: confirmation of monomethylation and premature cleavage during Edman coupling C;Comment: Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence. C;Sequence code: A C;Keywords: methylated amino end F;/Modified site: methylated amino end (Ala) F;/Modified site: methylated amino end (Ala) (in mature form) >TX;AA0062 N,N,N-trimethyl-L-alanine N;Alternate names: (S)-1-carboxy-N,N,N-trimethylethanaminium N;Systematic name: (S)-2-(trimethylammonio)propanoic acid A;Cross-references: CAS:44802-94-0 C;Formula: C 6 H 12 N 1 O 1 A;Formula weight: #chem 114.17 #phys 114.0919 C;Correction formula: C 3 H 7 A;Correction weight: #chem 43.09 #phys 43.0548 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Dognin, M.J.; Wittmann-Liebold, B. Hoppe-Seyler's Z. Physiol. Chem. 361, 1697-1705, 1980 A;Title: Identification of methylated amino acids during sequence analysis. Application to the Escherichia coli ribosomal protein L11. A;Reference number: A44722; MUID:81092289 A;Note: chromatographic detection; mass spectrographic identification; chemical synthesis R;Henry, G.D.; Dalgarno, D.C.; Levine, B.A.; Trayer, I.P. Biochem. Soc. Trans. 10, 362-363, 1982 A;Title: Discovery of alpha-N-trimethylalanine in myosin light chains and its role in actomyosin interaction. A;Reference number: A90347 A;Note: (1)H-NMR identification; chemical synthesis C;Sequence code: A A;Conditions: amino-terminal C;Keywords: blocked amino end; methylated amino end F;/Modified site: trimethylated amino end (Ala) F;/Modified site: trimethylated amino end (Ala) (in mature form) >TX;AA0063 N-methylglycine N;Alternate names: L-sarcosine; methylaminoacetic acid N;Systematic name: methylaminoethanoic acid A;Cross-references: CAS:107-97-1 C;Formula: C 3 H 5 N 1 O 1 A;Formula weight: #chem 71.08 #phys 71.0371 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 28-Jan-2000 R;Kamitori, S.; Takusagawa, F. J. Mol. Biol. 225, 445-456, 1992 A;Title: Crystal structure of the 2:1 complex between d(GAAGCTTC) and the anticancer drug actinomycin D. A;Reference number: A30624; MUID:92277651 A;Note: X-ray crystallography, 3.0 angstroms C;Comment: Sarcosine occurs internally in some nonencoded peptides, but has not been observed as a post-translational modification. C;Comment: Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence. C;Sequence code: G C;Keywords: *methylated amino acid; *methylated amino end F;/Modified site: methylated amino end (Gly) F;/Modified site: methylated amino end (Gly) (in mature form) F;/Modified site: N-methylglycine (Gly) >TX;AA0064 N-methyl-L-methionine N;Alternate names: N-methylmethionine N;Systematic name: (S)-2-methylamino-4-(methylthio)butanoic acid A;Cross-references: CAS:42537-72-4 C;Formula: C 6 H 11 N 1 O 1 S 1 A;Formula weight: #chem 145.23 #phys 145.0561 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Chen, R.; Brosius, J.; Wittmann-Liebold, B.; Schaefer, W. J. Mol. Biol. 111, 173-181, 1977 A;Title: Occurrence of methylated amino acids as N-termini of proteins from Escherichia coli ribosomes. A;Reference number: A44721; MUID:77168237 A;Note: chemical characterization and synthesis; chromatographic and mass spectrographic identification C;Comment: Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence. C;Sequence code: M C;Keywords: methylated amino end F;/Modified site: methylated amino end (Met) F;/Modified site: methylated amino end (Met) (in mature form) >TX;AA0065 N-methyl-L-phenylalanine N;Alternate names: N-methylphenylalanine N;Systematic name: (S)-2-methylamino-3-phenylpropanoic acid A;Cross-references: CAS:2566-30-5 C;Formula: C 10 H 11 N 1 O 1 A;Formula weight: #chem 161.21 #phys 161.0841 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Hermodson, M.A.; Chen, K.C.S.; Buchanan, T.M. Biochemistry 17, 442-445, 1978 A;Title: Neisseria pili proteins: amino-terminal amino acid sequences and identification of an unusual amino acid. A;Reference number: A44726; MUID:78080779 A;Note: chromatographic determination R;McKern, N.M.; Stewart, D.J.; Strike, P.M. J. Protein Chem. 7, 157-164, 1988 A;Title: Amino acid sequences of pilins from serologically distinct strains of Bacteroides nodosus. A;Reference number: A60891; MUID:89351576 A;Note: chromatographic determination C;Comment: Polypeptides with monomethylated amino terminals can undergo premature cleavage during the coupling step of an Edman degradation. This can result in "preview" with both a residue and the following residue being seen from the first step on through a sequence. C;Sequence code: F C;Keywords: methylated amino end F;/Modified site: methylated amino end (Phe) F;/Modified site: methylated amino end (Phe) (in mature form) >TX;AA0066 N,N-dimethyl-L-proline N;Alternate names: (S)-2-carboxy-1,1-dimethylpyrrolidinium N;Systematic name: (S)-1,1-dimethylpyrrolidinium-2-carboxylic acid A;Cross-references: CAS:51705-67-0 C;Formula: C 7 H 13 N 1 O 1 A;Formula weight: #chem 127.19 #phys 127.0997 C;Correction formula: C 2 H 5 A;Correction weight: #chem 29.06 #phys 29.0391 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Smith, G.M.; Pettigrew, G.W. Eur. J. Biochem. 110, 123-130, 1980 A;Title: Identification of N,N-dimethylproline as the N-terminal blocking group of Crithidia oncopelti cytochrome c557. A;Reference number: A37571; MUID:81066625 A;Note: chromatographic separation; mass spectrographic, (1)H-NMR and (13)C-NMR identification R;Martinage, A.; Briand, G.; Van Dorsselaer, A.; Turner, C.H.; Sautiere, P. Eur. J. Biochem. 147, 351-359, 1985 A;Title: Primary structure of histone H2B from gonads of the starfish Asterias rubens. Identification of an N-dimethylproline residue at the amino-terminal. A;Reference number: A02613; MUID:85127049 A;Note: mass spectrographic and (1)H-NMR identification C;Sequence code: P A;Conditions: amino-terminal C;Keywords: blocked amino end; methylated amino end F;/Modified site: dimethylated amino end (Pro) F;/Modified site: dimethylated amino end (Pro) (in mature form) >TX;AA0067 omega-N,omega-N'-dimethyl-L-arginine N;Alternate names: symmetric dimethylarginine N;Systematic name: (S)-2-amino-5-[((methylamino)(methylimino)methyl)amino]pentanoic acid A;Cross-references: CAS:30344-00-4 C;Formula: C 8 H 16 N 4 O 1 A;Formula weight: #chem 184.24 #phys 184.1324 C;Correction formula: C 2 H 4 A;Correction weight: #chem 28.05 #phys 28.0313 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 06-Sep-1996 R;Baldwin, G.S.; Carnegie, P.R. Biochem. J. 123, 69-74, 1971 A;Title: Isolation and partial characterization of methylated arginines from the encephalitogenic basic protein of myelin. A;Reference number: A90257; MUID:72066401 A;Note: chromatographic isolation; chemical characterization R;Scoble, H.A.; Whitaker, J.N.; Biemann, K. J. Neurochem. 47, 614-616, 1986 A;Title: Analysis of the primary sequence of human myelin basic protein peptides 1-44 and 90-170 by fast atom bombardment mass spectrometry. A;Reference number: A60862 A;Note: mass spectrographic analysis C;Generating enzyme: protein-arginine N-methyltransferase (EC 2.1.1.23) C;Sequence code: R C;Keywords: methylated amino acid F;/Modified site: omega-N,omega-N'-dimethylarginine (Arg) >TX;AA0068 omega-N,omega-N-dimethyl-L-arginine N;Alternate names: asymmetric dimethylarginine N;Systematic name: (S)-2-amino-5-[((dimethylamino)iminomethyl)amino]pentanoic acid A;Cross-references: CAS:30315-93-6 C;Formula: C 8 H 16 N 4 O 1 A;Formula weight: #chem 184.24 #phys 184.1324 C;Correction formula: C 2 H 4 A;Correction weight: #chem 28.05 #phys 28.0313 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 13-Sep-1996 R;Merrill, B.M.; Lopresti, M.B.; Stone, K.L.; Williams, K.R. Int. J. Pept. Protein Res. 29, 21-39, 1987 A;Title: Amino acid sequence of UP1, an hnRNP-derived single-stranded nucleic acid binding protein from calf thymus. A;Reference number: A27241; MUID:87193538 A;Note: chromatographic identification C;Sequence code: R C;Keywords: methylated amino acid F;/Modified site: omega-N,omega-N-dimethylarginine (Arg) >TX;AA0069 omega-N-methyl-L-arginine N;Systematic name: (S)-2-amino-5-[(imino(methylamino)methyl)amino]pentanoic acid A;Cross-references: CAS:17035-90-4 C;Formula: C 7 H 14 N 4 O 1 A;Formula weight: #chem 170.22 #phys 170.1168 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 06-Sep-1996 R;Baldwin, G.S.; Carnegie, P.R. Biochem. J. 123, 69-74, 1971 A;Title: Isolation and partial characterization of methylated arginines from the encephalitogenic basic protein of myelin. A;Reference number: A90257; MUID:72066401 A;Note: chromatographic isolation; chemical characterization R;Scoble, H.A.; Whitaker, J.N.; Biemann, K. J. Neurochem. 47, 614-616, 1986 A;Title: Analysis of the primary sequence of human myelin basic protein peptides 1-44 and 90-170 by fast atom bombardment mass spectrometry. A;Reference number: A60862 A;Note: mass spectrographic analysis C;Generating enzyme: protein-arginine N-methyltransferase (EC 2.1.1.23) C;Sequence code: R C;Keywords: methylated amino acid F;/Modified site: omega-N-methylarginine (Arg) >TX;AA0070 N4-methyl-L-asparagine N;Alternate names: beta-methylasparagine; N(gamma)-methylasparagine; N-methylasparagine N;Systematic name: (S)-2-amino-N4-methylbutanediamic acid A;Cross-references: CAS:7175-34-0 C;Formula: C 5 H 8 N 2 O 2 A;Formula weight: #chem 128.13 #phys 128.0586 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 30-Sep-1999 R;Klotz, A.V.; Leary, J.A.; Glazer, A.N. J. Biol. Chem. 261, 15891-15894, 1986 A;Title: Post-translational methylation of asparaginyl residues. Identification of beta-71 gamma-N-methylasparagine in allophycocyanin. A;Reference number: A61422; MUID:87057240 A;Note: mass spectrographic and (1)H-NMR identification R;Stec, B.; Troxler, R.F.; Teeter, M.M. submitted to the Brookhaven Protein Data Bank, June 1995 A;Reference number: A68150; PDB:1PHN A;Note: X-ray crystallography, 1.65 angstroms C;Sequence code: N C;Keywords: methylated amino acid F;/Modified site: N4-methylasparagine (Asn) >TX;AA0071 N5-methyl-L-glutamine N;Alternate names: gamma-methylglutamine; N(delta)-methylglutamine; N-methylglutamine N;Systematic name: (S)-2-amino-N5-methylpentanediamic acid A;Cross-references: CAS:3031-62-7 C;Formula: C 6 H 10 N 2 O 2 A;Formula weight: #chem 142.16 #phys 142.0742 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 06-Sep-1996 R;Muranova, T.A.; Muranov, A.V.; Markova, L.F.; Ovchinnikov, Y.A. FEBS Lett. 96, 301-305, 1978 A;Title: The primary structure of ribosomal protein L3 from Escherichia coli 70 S ribosomes. A;Reference number: A02757; MUID:79086242 C;Sequence code: Q C;Keywords: methylated amino acid F;/Modified site: N5-methylglutamine (Gln) >TX;AA0072 L-glutamic acid 5-methyl ester N;Alternate names: glutamic acid gamma-methyl ester N;Systematic name: (S)-2-aminopentanedioic acid 5-methyl ester A;Cross-references: CAS:1499-55-4 C;Formula: C 6 H 9 N 1 O 3 A;Formula weight: #chem 143.14 #phys 143.0582 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Correction formula: C 1 H 1 N -1 A;Correction weight: #chem -0.99 #phys -0.9952 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 09-Apr-1999 R;Kehry, M.A.; Engstroem, P.; Dahlquist, F.W.; Hazelbauer, G.L. J. Biol. Chem. 258, 5050-5055, 1983 A;Title: Multiple covalent modifications of Trg, a sensory transducer of Escherichia coli. A;Reference number: A37452; MUID:83161122 A;Note: methylated tryptic peptides were isolated C;Comment: Glutamate methylesterase can also act as a glutamine amidohydrolase. C;Generating enzyme: protein-glutamate methylesterase (EC 3.1.1.61); protein-glutamate O-methyltransferase (EC 2.1.1.80) C;Sequence code: E #link GLU; Q #link GLN; Z #link GLX C;Keywords: methylated amino acid F;/Modified site: glutamate methyl ester (Glu) #link GLU F;/Modified site: glutamate methyl ester (Gln) #link GLN F;/Modified site: glutamate methyl ester (Glx) #link GLX >TX;AA0073 3'-methyl-L-histidine N;Alternate names: tau-methylhistidine; tele-methylhistidine N;Systematic name: (S)-2-amino-3-(3-methylimidazol-4-yl)propanoic acid A;Cross-references: CAS:368-16-1 C;Formula: C 7 H 8 N 3 O 1 A;Formula weight: #chem 150.16 #phys 150.0667 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-May-1997 R;Maita, T.; Hayashida, M.; Tanioka, Y.; Komine, Y.; Matsuda, G. Proc. Natl. Acad. Sci. U.S.A. 84, 416-420, 1987 A;Title: The primary structure of the myosin head. A;Reference number: A26365; MUID:87092420 A;Note: identification of 3'-methylhistidine along with methyl- and trimethyllysine R;Raftery, M.J.; Harrison, C.A.; Alewood, P.; Jones, A.; Geczy, C.L. Biochem. J. 316, 285-293, 1996 A;Title: Isolation of the murine S100 protein MRP14 (14 kDa migration-inhibitory-factor-related protein) from activated spleen cells: characterization of post-translational modifications and zinc binding. A;Reference number: S68272 A;Note: mass spectrographic detection; chromatographic identification of PTC derivatives of 1'- and 3'-methylhistidine; the authors' source for the reference standard acknowledges that their name, 1'-methylhistidine, is a misnomer for the IUPAC standard name 3'-methylhistidine C;Generating enzyme: protein-histidine N-methyltransferase (EC 2.1.1.85) C;Sequence code: H C;Keywords: methylated amino acid F;/Modified site: 3'-methylhistidine (His) >TX;AA0074 N6,N6,N6-trimethyl-L-lysine N;Alternate names: epsilon-trimethyllysine; N(zeta)-trimethyllysine; (S)-5-amino-5-carboxy-N,N,N-trimethylpentanaminium N;Systematic name: (S)-2-amino-6-(trimethylammonio)hexanoic acid A;Cross-references: CAS:19253-88-4 C;Formula: C 9 H 19 N 2 O 1 A;Formula weight: #chem 171.26 #phys 171.1497 C;Correction formula: C 3 H 7 A;Correction weight: #chem 43.09 #phys 43.0548 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 24-Apr-1998 R;DeLange, R.J.; Glazer, A.N.; Smith, E.L. J. Biol. Chem. 244, 1385-1388, 1969 A;Title: Presence and location of an unusual amino acid, epsilon-N-trimethyllysine, in cytochrome c of wheat germ and Neurospora. A;Reference number: A92043; MUID:69128197 R;Dognin, M.J.; Wittmann-Liebold, B. Hoppe-Seyler's Z. Physiol. Chem. 361, 1697-1705, 1980 A;Title: Identification of methylated amino acids during sequence analysis. Application to the Escherichia coli ribosomal protein L11. A;Reference number: A44722 A;Note: chromatographic detection; mass spectrographic identification R;Bloxham, D.P.; Parmelee, D.C.; Kumar, S.; Walsh, K.A.; Titani, K. Biochemistry 21, 2028-2036, 1982 A;Title: Complete amino acid sequence of porcine heart citrate synthase. A;Reference number: A90457; MUID:82231993 R;Babu, Y.S.; Bugg, C.E.; Cook, W.J. submitted to the Brookhaven Protein Data Bank, May 1988 A;Reference number: A50576; PDB:3CLN A;Contents: annotation; X-ray crystallography, 2.2 angstroms, residues 6-129,'N',131-148 R;Babu, Y.S.; Bugg, C.E.; Cook, W.J. J. Mol. Biol. 204, 191-204, 1988 A;Title: Structure of calmodulin refined at 2.2 A resolution. A;Reference number: A37299; MUID:89110997 A;Contents: annotation; X-ray crystallography, 2.2 angstroms R;Sundaralingam, M. submitted to the Brookhaven Protein Data Bank, August 1993 A;Reference number: A51326; PDB:1OSA A;Contents: annotation; X-ray crystallography, 1.68 angstroms R;Rao, S.T.; Wu, S.; Satyshur, K.A.; Ling, K.Y.; Kung, C.; Sundaralingam, M. Protein Sci. 2, 436-447, 1993 A;Title: Structure of Paramecium tetraurelia calmodulin at 1.8 angstroms resolution. A;Reference number: A45374; MUID:93200921 A;Contents: annotation; X-ray crystallography, 1.68 angstroms C;Generating enzyme: histone-lysine N-methyltransferase (EC 2.1.1.43); cytochrome-c-lysine N-methyltransferase (EC 2.1.1.59); calmodulin-lysine N-methyltransferase (EC 2.1.1.60) C;Sequence code: K C;Keywords: methylated amino acid F;/Modified site: N6,N6,N6-trimethyllysine (Lys) >TX;AA0075 N6,N6-dimethyl-L-lysine N;Alternate names: epsilon-dimethyllysine; N(zeta)-dimethyllysine N;Systematic name: (S)-2-amino-6-dimethylaminohexanoic acid A;Cross-references: CAS:2259-86-1 C;Formula: C 8 H 16 N 2 O 1 A;Formula weight: #chem 156.23 #phys 156.1263 C;Correction formula: C 2 H 4 A;Correction weight: #chem 28.05 #phys 28.0313 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 24-Apr-1998 R;Schaefer, W.H.; Lukas, T.J.; Blair, I.A.; Schultz, J.E.; Watterson, D.M. J. Biol. Chem. 262, 1025-1029, 1987 A;Title: Amino acid sequence of a novel calmodulin from Paramecium tetraurelia that contains dimethyllysine in the first domain. A;Reference number: JK0006; MUID:87109207 A;Note: mass spectrographic identification R;Sundaralingam, M. submitted to the Brookhaven Protein Data Bank, August 1993 A;Reference number: A51326; PDB:1OSA A;Contents: annotation; X-ray crystallography, 1.68 angstroms R;Rao, S.T.; Wu, S.; Satyshur, K.A.; Ling, K.Y.; Kung, C.; Sundaralingam, M. Protein Sci. 2, 436-447, 1993 A;Title: Structure of Paramecium tetraurelia calmodulin at 1.8 angstroms resolution. A;Reference number: A45374; MUID:93200921 A;Contents: annotation; X-ray crystallography, 1.68 angstroms C;Generating enzyme: histone-lysine N-methyltransferase (EC 2.1.1.43); cytochrome-c-lysine N-methyltransferase (EC 2.1.1.59); calmodulin-lysine N-methyltransferase (EC 2.1.1.60) C;Sequence code: K C;Keywords: methylated amino acid F;/Modified site: N6,N6-dimethyllysine (Lys) >TX;AA0076 N6-methyl-L-lysine N;Alternate names: epsilon-methyllysine; N(zeta)-methyllysine N;Systematic name: (S)-2-amino-6-methylaminohexanoic acid A;Cross-references: CAS:1188-07-4 C;Formula: C 7 H 14 N 2 O 1 A;Formula weight: #chem 142.20 #phys 142.1106 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 06-Sep-1996 R;Minami, Y.; Wakabayashi, S.; Wada, K.; Matsubara, H.; Kerscher, L.; Oesterhelt, D. J. Biochem. 97, 745-753, 1985 A;Title: Amino acid sequence of a ferredoxin from thermoacidophilic archaebacterium, Sulfolobus acidocaldarius. Presence of an N(6)-monomethyllysine and phyletic consideration of archaebacteria. A;Reference number: A00223; MUID:85261163 A;Note: chromatographic and mass spectrographic identification C;Generating enzyme: histone-lysine N-methyltransferase (EC 2.1.1.43); cytochrome-c-lysine N-methyltransferase (EC 2.1.1.59); calmodulin-lysine N-methyltransferase (EC 2.1.1.60) C;Sequence code: K C;Keywords: methylated amino acid F;/Modified site: N6-methyllysine (Lys) >TX;AA0077 N6-palmitoyl-L-lysine N;Alternate names: epsilon-palmitoyllysine; N(zeta)-palmitoyllysine; N6-(1-oxohexadecyl)-L-lysine N;Systematic name: (S)-2-amino-6-(hexadecanoylamino)hexanoic acid A;Cross-references: CAS:559012-43-0 C;Formula: C 22 H 42 N 2 O 2 A;Formula weight: #chem 366.59 #phys 366.3246 C;Correction formula: C 16 H 30 O 1 A;Correction weight: #chem 238.42 #phys 238.2297 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 09-Apr-1999 R;Hackett, M.; Guo, L.; Shabanowitz, J.; Hunt, D.F.; Hewlett, E.L. Science 266, 433-435, 1994 A;Title: Internal lysine palmitoylation in adenylate cyclase toxin from Bordetella pertussis. A;Reference number: A55167; MUID:95025937 A;Note: mass spectrographic identification R;Stanley, P.; Packman, L.C.; Koronakis, V.; Hughes, C. Science 266, 1992-1996, 1994 A;Title: Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin. A;Reference number: A55387; MUID:95099325 A;Note: radioisotope labeling C;Generating enzyme: peptidyl-lysine N6-palmitoyltransferase (EC 2.3.1.-) C;Sequence code: K A;Conditions: combinable C;Keywords: lipoprotein F;/Binding site: palmitate (Lys) (covalent) >TX;AA0078 N6-myristoyl-L-lysine N;Alternate names: epsilon-myristoyllysine; N(zeta)-myristoyllysine; N6-(1-oxotetradecyl)-L-lysine N;Systematic name: (S)-2-amino-6-(tetradecanoylamino)hexanoic acid C;Formula: C 20 H 38 N 2 O 2 A;Formula weight: #chem 338.54 #phys 338.2933 C;Correction formula: C 14 H 26 O 1 A;Correction weight: #chem 210.36 #phys 210.1984 C;Date: 09-Aug-1995 #structure_revision 09-Aug-1995 #text_change 28-Jan-2000 R;Stevenson, F.T.; Bursten, S.L.; Locksley, R.M.; Lovett, D.H. J. Exp. Med. 176, 1053-1062, 1992 A;Title: Myristyl acylation of the tumor necrosis factor alpha precursor on specific lysine residues. A;Reference number: A59163; MUID:93018820 A;Note: radiolabeling; biosynthesis; chromatographic detection R;Stevenson, F.T.; Bursten, S.L.; Fanton, C.; Locksley, R.M.; Lovett, D.H. Proc. Natl. Acad. Sci. U.S.A. 90, 7245-7249, 1993 A;Title: The 31-kDa precursor of interleukin 1alpha is myristoylated on specific lysines within the 16-kDa N-terminal propiece. A;Reference number: A48293; MUID:93348250 A;Note: biosynthesis; chemical synthesis; chromatographic detection C;Generating enzyme: peptidyl-lysine N6-myristoyltransferase (EC 2.3.1.-) C;Sequence code: K A;Conditions: combinable C;Keywords: lipoprotein; myristylation F;/Binding site: myristate (Lys) (covalent) >TX;AA0079 O-palmitoyl-L-threonine N;Alternate names: L-threonine hexadecanoate ester N;Systematic name: (2S,3R)-2-amino-3-(hexadecanoyloxy)butanoic acid A;Cross-references: CAS:88467-30-5 C;Formula: C 20 H 37 N 1 O 3 A;Formula weight: #chem 339.52 #phys 339.2773 C;Correction formula: C 16 H 30 O 1 A;Correction weight: #chem 238.42 #phys 238.2297 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 06-Nov-1998 R;Stoffel, W.; Hillen, H.; Schroeder, W.; Deutzmann, R. Hoppe-Seyler's Z. Physiol. Chem. 364, 1455-1466, 1983 A;Title: The primary structure of bovine brain myelin lipophilin (proteolipid apoprotein). A;Reference number: A91715; MUID:84059642 A;Note: chromatographic and mass spectrographic identification R;Branton, W.D.; Rudnick, M.S.; Zhou, Y.; Eccleston, E.D.; Fields, G.B.; Bowers, L.D. Nature 365, 496-497, 1993 A;Title: Fatty acylated toxin structure. A;Reference number: S38275 A;Note: chromatographic and mass spectrographic identification C;Comment: The palmitate represents a mixture of saturated and unsaturated fatty acids. C;Sequence code: T A;Conditions: combinable; incidental to RESID:AA0097 C;Keywords: lipoprotein F;/Binding site: fatty acid (Thr) (covalent) >TX;AA0080 O-palmitoyl-L-serine N;Alternate names: L-serine hexadecanoate ester N;Systematic name: (2S,3R)-2-amino-3-(hexadecanoyloxy)propanoic acid A;Cross-references: CAS:88815-78-5 C;Formula: C 19 H 35 N 1 O 3 A;Formula weight: #chem 325.50 #phys 325.2617 C;Correction formula: C 16 H 30 O 1 A;Correction weight: #chem 238.42 #phys 238.2297 C;Date: 25-Aug-1995 #structure_revision 25-Aug-1995 #text_change 25-Aug-1995 R;Diehl, H.J.; Schaich, M.; Budzinski, R.M.; Stoffel, W. Proc. Natl. Acad. Sci. U.S.A. 83, 9807-9811, 1986 A;Title: Individual exons encode the integral membrane domains of human myelin proteolipid protein. A;Reference number: A26665; MUID:87092337 A;Note: the fatty acid attachment site is shown without evidence C;Comment: The palmitate represents a mixture of saturated and unsaturated fatty acids. C;Sequence code: S A;Conditions: combinable C;Keywords: lipoprotein F;/Binding site: fatty acid (Ser) (covalent) >TX;AA0081 L-alanine amide N;Alternate names: alaninamide N;Systematic name: (S)-2-aminopropanamide A;Cross-references: CAS:7324-05-2 C;Formula: C 3 H 7 N 2 O 1 A;Formula weight: #chem 87.10 #phys 87.0558 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Fernlund, P. Biochim. Biophys. Acta 439, 17-25, 1976 A;Title: Structure of a light-adapting hormone from the shrimp, Pandalus borealis. A;Reference number: A01473; MUID:76253762 A;Note: chromatographic identification of dansyl derivative R;Lancelin, J.M.; Kohda, D.; Tate, S.I.; Yanagawa, Y.; Abe, T.; Satake, M.; Inagaki, F. Biochemistry 30, 6908-6916, 1991 A;Title: Tertiary structure of conotoxin GIIIA in aqueous solution. A;Reference number: A44659; MUID:91299744 A;Note: (1)H-NMR identification R;Lohr, J.; Klein, J.; Webster, S.G.; Dircksen, H. Comp. Biochem. Physiol. 104B, 699-706, 1993 A;Title: Quantification, immunoaffinity purification and sequence analysis of a pigment-dispersing hormone of the shore crab, Carcinus maenas (L.). A;Reference number: A56903; MUID:93230895 A;Note: mass spectrographic characterization R;Takamatsu, K.; Tatemoto, K. Neurochem. Res. 17, 239-246, 1992 A;Title: Isolation and characterization of two novel peptide amides originating from myelin basic protein in bovine brain. A;Reference number: A61641 A;Note: this peptide has a carboxyl-terminal amide probably produced by a non-enzymatic reaction C;Generating enzyme: peptidylglycine monooxygenase (EC 1.14.17.3) C;Sequence code: A A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Ala) F;/Modified site: amidated carboxyl end (Ala) (in mature form from following glycine) >TX;AA0082 L-arginine amide N;Alternate names: argininamide N;Systematic name: (S)-2-amino-5-guanidinopentanamide A;Cross-references: CAS:2788-83-2 C;Formula: C 6 H 14 N 5 O 1 A;Formula weight: #chem 172.21 #phys 172.1198 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Maeda, N.; Tamiya, N. Biochem. J. 175, 507-517, 1978 A;Title: Three neurotoxins from the venom of a sea snake Astrotia stokesii, including two long-chain neurotoxic proteins with amidated C-termini. A;Reference number: A90302; MUID:79123997 A;Note: chromatographic identification R;Orskov, C.; Bersani, M.; Johnsen, A.H.; Hojrup, P.; Holst, J.J. J. Biol. Chem. 264, 12826-12829, 1989 A;Title: Complete sequences of glucagon-like peptide-1 from human and pig small intestine. A;Reference number: A92732; MUID:89327238 A;Note: mass spectrographic identification by differential methyl esterification R;Muta, T.; Fujimoto, T.; Nakajima, H.; Iwanaga, S. J. Biochem. 108, 261-266, 1990 A;Title: Tachyplesins isolated from hemocytes of southeast Asian horseshoe crabs (Carcinoscorpius rotundicauda and Tachypleus gigas): identification of a new tachyplesin, tachyplesin III, and a processing intermediate of its precursor. A;Reference number: JX0124; MUID:91035357 A;Note: chromatographic identification of the phenylthiocarbamyl derivative C;Sequence code: R A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Arg) F;/Modified site: amidated carboxyl end (Arg) (in mature form from following glycine) >TX;AA0083 L-asparagine amide N;Alternate names: asparaginamide N;Systematic name: (S)-2-amino-butanediamide A;Cross-references: CAS:16748-73-5 C;Formula: C 4 H 8 N 3 O 2 A;Formula weight: #chem 130.13 #phys 130.0617 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Tatemoto, K.; Mutt, V. Proc. Natl. Acad. Sci. U.S.A. 75, 4115-4119, 1978 A;Title: Chemical determination of polypeptide hormones. A;Reference number: A30611 A;Note: chromatographic identification of the dansyl derivatives of most of the amino acid amides R;Jaffe, H.; Raina, A.K.; Riley, C.T.; Fraser, B.A.; Bird, T.G.; Tseng, C.M.; Zhang, Y.S.; Hayes, D.K. Biochem. Biophys. Res. Commun. 155, 344-350, 1988 A;Title: Isolation and primary structure of a neuropeptide hormone from Heliothis zea with hypertrehalosemic and adipokinetic activities. A;Reference number: A31571; MUID:88326324 A;Note: mass spectrographic detection R;Veenstra, J.A. FEBS Lett. 250, 231-234, 1989 A;Title: Isolation and structure of corazonin, a cardioactive peptide from the american cockroach. A;Reference number: S05002; MUID:89325572 A;Note: chromatographic identification of the phenylthiocarbamyl derivative C;Sequence code: N A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Asn) F;/Modified site: amidated carboxyl end (Asn) (in mature form from following glycine) >TX;AA0084 L-aspartic acid 1-amide N;Alternate names: isoasparagine; 3,4-diamino-4-oxabutanoic acid N;Systematic name: (S)-2-amino-1-butanediamic acid A;Cross-references: CAS:498-25-9 C;Formula: C 4 H 6 N 2 O 2 A;Formula weight: #chem 114.10 #phys 114.0429 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 22-Nov-1996 #structure_revision 22-Nov-1996 #text_change 21-Jan-2000 R;Kreil, G.; Barra, D.; Simmaco, M.; Erspamer, V.; Erspamer, G.F.; Negri, L.; Severini, C.; Corsi, R.; Melchiorri, P. Eur. J. Pharmacol. 162, 123-128, 1989 A;Title: Deltorphin, a novel amphibian skin peptide with high selectivity and affinity for delta opioid receptors. A;Reference number: A60595; MUID:89171156 A;Note: chemical synthesis C;Sequence code: D A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Asp) F;/Modified site: amidated carboxyl end (Asp) (in mature form from following glycine) >TX;AA0085 L-cysteine amide N;Alternate names: cysteinamide N;Systematic name: (R)-2-amino-3-mercaptopropanamide A;Cross-references: CAS:74401-72-2 C;Formula: C 3 H 7 N 2 O 1 S 1 A;Formula weight: #chem 119.17 #phys 119.0279 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;McIntosh, M.; Cruz, L.J.; Hunkapiller, M.W.; Gray, W.R.; Olivera, B.M. Arch. Biochem. Biophys. 218, 329-334, 1982 A;Title: Isolation and structure of a peptide toxin from the marine snail Conus magus. A;Reference number: A90071; MUID:83073458 A;Note: chromatographic of radiolabeled S-carboxymethyl derivative R;Myers, R.A.; Zafaralla, G.C.; Gray, W.R.; Abbott, J.; Cruz, L.J.; Olivera, B.M. Biochemistry 30, 9370-9377, 1991 A;Title: alpha-Conotoxins, small peptide probes of nicotinic acetylcholine receptors. A;Reference number: A40312; MUID:91369955 A;Note: mass spectrographic detection C;Sequence code: C A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Cys) F;/Modified site: amidated carboxyl end (Cys) (in mature form from following glycine) >TX;AA0086 L-glutamine amide N;Alternate names: glutaminamide N;Systematic name: (S)-2-amino-pentanediamide A;Cross-references: CAS:2013-17-4 C;Formula: C 5 H 10 N 3 O 2 A;Formula weight: #chem 144.15 #phys 144.0773 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Hopkins, C.; Grilley, M.; Miller, C.; Shon, K.J.; Cruz, L.J.; Gray, W.R.; Dykert, J.; Rivier, J.; Yoshikami, D.; Olivera, B.M. J. Biol. Chem. 270, 22361-22367, 1995 A;Title: A new family of Conus peptides targeted to the nicotinic acetylcholinereceptor. A;Reference number: A58647; MUID:95403432 A;Note: chemical synthesis R;Han, K.H.; Hwang, K.J.; Kim, S.M.; Kim, S.K.; Gray, W.R.; Olivera, B.M.; Rivier, J.; Shon, K.J. submitted to the Brookhaven Protein Data Bank, December 1996 A;Reference number: A67666; PDB:1P1P A;Note: conformation and disulfide bond assignments by (1)H-NMR R;Han, K.H.; Hwang, K.J.; Kim, S.M.; Kim, S.K.; Gray, W.R.; Olivera, B.M.; Rivier, J.; Shon, K.J. Biochemistry 36, 1669-1677, 1997 A;Title: NMR structure determination of a novel conotoxin, [Pro 7,13] alpha A-conotoxin PIVA. A;Reference number: A58646; MUID:97200721 A;Note: conformation and disulfide bond assignments by (1)H-NMR C;Sequence code: Q A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Gln) F;/Modified site: amidated carboxyl end (Gln) (in mature form from following glycine) >TX;AA0087 L-glutamic acid 1-amide N;Alternate names: isoglutamine; 4,5-diamino-5-oxapentanoic acid N;Systematic name: (S)-2-amino-1-pentanediamic acid A;Cross-references: CAS:328-48-3 C;Formula: C 5 H 9 N 2 O 3 A;Formula weight: #chem 145.14 #phys 145.0613 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Kreil, G. FEBS Lett. 54, 100-102, 1975 A;Title: The structure of Apis dorsata melittin: phylogenetic relationships between honeybees as deduced from sequence data. A;Reference number: A01763; MUID:75168194 A;Note: chromatographic identification C;Sequence code: E A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Glu) F;/Modified site: amidated carboxyl end (Glu) (in mature form from following glycine) >TX;AA0088 glycine amide N;Alternate names: 2-aminoacetamide N;Systematic name: 2-aminoethanamide A;Cross-references: CAS:598-41-4 C;Formula: C 2 H 5 N 2 O 1 A;Formula weight: #chem 73.08 #phys 73.0402 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: G A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Gly) F;/Modified site: amidated carboxyl end (Gly) (in mature form from following glycine) >TX;AA0089 L-histidine amide N;Alternate names: histidinamide N;Systematic name: (S)-2-amino-3-(1H-imidazol-4-yl)propanamide A;Cross-references: CAS:7621-14-9 C;Formula: C 6 H 9 N 4 O 1 A;Formula weight: #chem 153.16 #phys 153.0776 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: H A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (His) F;/Modified site: amidated carboxyl end (His) (in mature form from following glycine) >TX;AA0090 L-isoleucine amide N;Alternate names: isoleucinamide N;Systematic name: (2S,3S)-2-amino-3-methylpentanamide A;Cross-references: CAS:14445-54-6 C;Formula: C 6 H 13 N 2 O 1 A;Formula weight: #chem 129.18 #phys 129.1028 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Teshima, T.; Ueki, Y.; Nakai, T.; Shiba, T. Tetrahedron 42, 829-834, 1986 A;Title: Structure determination of lepidopteran, self-defense substance produced by silkworm. A;Reference number: A01768 A;Note: chromatographic detection; chemical synthesis C;Sequence code: I A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Ile) F;/Modified site: amidated carboxyl end (Ile) (in mature form from following glycine) >TX;AA0091 L-leucine amide N;Alternate names: leucinamide N;Systematic name: (S)-2-amino-4-methylpentanamide A;Cross-references: CAS:687-51-4 C;Formula: C 6 H 13 N 2 O 1 A;Formula weight: #chem 129.18 #phys 129.1028 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: L A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Leu) F;/Modified site: amidated carboxyl end (Leu) (in mature form from following glycine) >TX;AA0092 L-lysine amide N;Alternate names: lysinamide N;Systematic name: (S)-2,6-diaminohexanamide A;Cross-references: CAS:32388-19-5 C;Formula: C 6 H 14 N 3 O 1 A;Formula weight: #chem 144.20 #phys 144.1137 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: K A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Lys) F;/Modified site: amidated carboxyl end (Lys) (in mature form from following glycine) >TX;AA0093 L-methionine amide N;Alternate names: methioninamide N;Systematic name: (S)-2-amino-4-(methylthio)butanamide A;Cross-references: CAS:4510-08-1 C;Formula: C 5 H 11 N 2 O 1 S 1 A;Formula weight: #chem 147.22 #phys 147.0592 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: M A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Met) F;/Modified site: amidated carboxyl end (Met) (in mature form from following glycine) >TX;AA0094 L-phenylalanine amide N;Alternate names: phenylalaninamide N;Systematic name: (S)-2-amino-3-phenylpropanamide A;Cross-references: CAS:5241-58-7 C;Formula: C 9 H 11 N 2 O 1 A;Formula weight: #chem 163.20 #phys 163.0871 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Grimmelikhuijzen, C.J.P.; Hahn, M.; Rinehart, K.L.; Spencer, A.N. Brain Res. 475, 198-203, 1988 A;Title: Isolation of TX;AA0095 L-proline amide N;Alternate names: prolinamide N;Systematic name: (S)-pyrrolidine-2-carboxamide A;Cross-references: CAS:7531-52-4 C;Formula: C 5 H 9 N 2 O 1 A;Formula weight: #chem 113.14 #phys 113.0715 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: P A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Pro) F;/Modified site: amidated carboxyl end (Pro) (in mature form from following glycine) >TX;AA0096 L-serine amide N;Alternate names: serinamide N;Systematic name: (S)-2-amino-3-hydroxypropanamide A;Cross-references: CAS:6791-49-7 C;Formula: C 3 H 7 N 2 O 2 A;Formula weight: #chem 103.10 #phys 103.0508 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: S A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Ser) F;/Modified site: amidated carboxyl end (Ser) (in mature form from following glycine) >TX;AA0097 L-threonine amide N;Alternate names: threoninamide N;Systematic name: (2S,3R)-2-amino-3-hydroxybutanamide A;Cross-references: CAS:2280-40-2 C;Formula: C 4 H 9 N 2 O 2 A;Formula weight: #chem 117.13 #phys 117.0664 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: T A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Thr) F;/Modified site: amidated carboxyl end (Thr) (in mature form from following glycine) >TX;AA0098 L-tryptophan amide N;Alternate names: tryptophanamide N;Systematic name: (S)-2-amino-3-(1H-indol-3-yl)propanamide A;Cross-references: CAS:20696-57-5 C;Formula: C 11 H 12 N 3 O 1 A;Formula weight: #chem 202.24 #phys 202.0980 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: W A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Trp) F;/Modified site: amidated carboxyl end (Trp) (in mature form from following glycine) >TX;AA0099 L-tyrosine amide N;Alternate names: tyrosinamide N;Systematic name: (S)-2-amino-3-(4-hydoxyphenyl)propanamide A;Cross-references: CAS:4985-46-0 C;Formula: C 9 H 11 N 2 O 2 A;Formula weight: #chem 179.20 #phys 179.0821 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Olivera, B.M.; McIntosh, J.M.; Cruz, L.J.; Luque, F.A.; Gray, W.R. Biochemistry 23, 5087-5090, 1984 A;Title: Purification and sequence of a presynaptic peptide toxin from Conus geographus venom. A;Reference number: A01785; MUID:85072796 A;Note: chromatographic identification of PTC derivative R;Conlon, J.M.; Schmidt, W.E.; Gallwitz, B.; Falkmer, S.; Thim, L. Regul. Pept. 16, 261-268, 1986 A;Title: Characterization of an amidated form of pancreatic polypeptide from the daddy sculpin (Cottus scorpius). A;Reference number: A60309; MUID:87176585 A;Note: mass spectrographic characterization R;Takamatsu, K.; Tatemoto, K. Neurochem. Res. 17, 239-246, 1992 A;Title: Isolation and characterization of two novel peptide amides originating from myelin basic protein in bovine brain. A;Reference number: A61641 A;Note: this peptide has a carboxyl-terminal amide probably produced by a non-enzymatic reaction C;Generating enzyme: peptidylglycine monooxygenase (EC 1.14.17.3) C;Sequence code: Y A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Tyr) F;/Modified site: amidated carboxyl end (Tyr) (in mature form from following glycine) >TX;AA0100 L-valine amide N;Alternate names: valinamide N;Systematic name: (S)-2-amino-3-methylbutanamide A;Cross-references: CAS:4540-60-7 C;Formula: C 5 H 11 N 2 O 1 A;Formula weight: #chem 115.16 #phys 115.0871 C;Correction formula: C 0 H 1 N 1 O -1 A;Correction weight: #chem -0.98 #phys -0.9840 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: V A;Conditions: carboxyl-terminal C;Keywords: amidated carboxyl end F;/Modified site: amidated carboxyl end (Val) F;/Modified site: amidated carboxyl end (Val) (in mature form from following glycine) >TX;AA0101 L-cysteine methyl disulfide N;Alternate names: L-3-(methyldithio)alanine N;Systematic name: (R)-2-amino-3-(methyldithio)propanoic acid A;Cross-references: CAS:33784-54-2 C;Formula: C 4 H 7 N 1 O 1 S 2 A;Formula weight: #chem 149.24 #phys 148.9969 C;Correction formula: C 1 H 2 S 1 A;Correction weight: #chem 46.09 #phys 45.9877 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Kissinger, C.R.; Sieker, L.C.; Adman, E.T.; Jensen, L.H. J. Mol. Biol. 219, 693-715, 1991 A;Title: Refined crystal structure of ferredoxin II from Desulfovibrio gigas at 1.7 A. A;Reference number: S17118; MUID:91278096 A;Note: X-ray crystallography, 1.7 angstroms C;Sequence code: C C;Keywords: disulfide bond F;/Binding site: methylmercaptan (Cys) (covalent) >TX;AA0102 S-farnesyl-L-cysteine N;Systematic name: (R,E,E)-2-amino-3-(3,7,11-trimethyl-2,6,10-dodecatrienylthio)propanoic acid A;Cross-references: CAS:6800-92-0 C;Formula: C 18 H 29 N 1 O 1 S 1 A;Formula weight: #chem 307.50 #phys 307.1970 C;Correction formula: C 15 H 24 A;Correction weight: #chem 204.36 #phys 204.1878 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Tuinman, A.A.; Thomas, D.A.; Cook, K.D.; Xue, C.B.; Naider, F.; Becker, J.M. Anal. Biochem. 193, 173-177, 1991 A;Title: Mass spectrometric signature of S-prenylated cysteine peptides. A;Reference number: A44567; MUID:91336511 A;Note: mass spectrographic identification R;Heilmeyer Jr., L.M.G.; Serwe, M.; Weber, C.; Metzger, J.; Hoffmann-Posorske, E.; Meyer, H.E. Proc. Natl. Acad. Sci. U.S.A. 89, 9554-9558, 1992 A;Title: Farnesylcysteine, a constituent of the alpha and beta subunits of rabbit skeletal muscle phosphorylase kinase: localization by conversion to S-ethylcysteine and by tandem mass spectrometry. A;Reference number: A47208; MUID:93028500 A;Note: farnesylation not followed by cleavage of the terminal peptide and methylation of the new carboxyl end C;Comment: Formation of S-farnesycysteine may be coupled with subsequent cleavage of a carboxy-terminal tripeptide for the CXXX motif and methyl esterification of the farnesylated cysteine. See L-cysteine methyl ester (RESID:AA0105). C;Comment: The residue may be found at the first position in the sequence motif C-X-X-[SAQCMT]* where the second and third positions are usually aliphatic. C;Generating enzyme: protein-cysteine farnesyltransferase (EC 2.5.1.-) C;Sequence code: C A;Conditions: combinable; incidental to RESID:AA0105 C;Keywords: lipoprotein; prenylated cysteine F;/Binding site: farnesyl (Cys) (covalent) >TX;AA0103 S-12-hydroxyfarnesyl-L-cysteine N;Systematic name: (R,E,E,Z)-2-amino-3-(12-hydroxy-3,7,11-trimethyl-3,6,10-dodecatrienylthio)propanoic acid C;Formula: C 18 H 29 N 1 O 2 S 1 A;Formula weight: #chem 323.50 #phys 323.1919 C;Correction formula: C 15 H 24 O 1 A;Correction weight: #chem 220.36 #phys 220.1827 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Sakagami, Y.; Yoshida, M.; Isogai, A.; Suzuki, A. Science 212, 1525-1527, 1981 A;Title: Peptide sex hormones inducing conjugation tube formation in compatible mating-type cells of Tremella mesenterica. A;Reference number: A94256 A;Note: possible identification of 12-hydroxyfarnesyl C;Comment: Formation of S-12-hydroxyfarnesylcysteine may be coupled with subsequent cleavage of a carboxy-terminal tripeptide for the CAAX motif and methyl esterification of the farnesylated cysteine. See L-cysteine methyl ester (RESID:AA0105). C;Sequence code: C A;Conditions: combinable; incidental to RESID:AA0105 C;Keywords: lipoprotein; prenylated cysteine F;/Binding site: (E,E,Z)-12-hydroxyfarnesyl (Cys) (covalent) >TX;AA0104 S-geranylgeranyl-L-cysteine N;Systematic name: (R,E,E,E)-2-amino-3-(3,7,11,15-tetramethyl-2,6,10,14-hexadecatetraenylthio)propanoic acid A;Cross-references: CAS:131404-69-8 C;Formula: C 23 H 38 N 1 O 1 S 1 A;Formula weight: #chem 376.63 #phys 376.2674 C;Correction formula: C 20 H 33 A;Correction weight: #chem 273.49 #phys 273.2582 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Morishita, R.; Fukada, Y.; Kokame, K.; Yoshizawa, T.; Masuda, K.; Niwa, M.; Kato, K.; Asano, T. Eur. J. Biochem. 210, 1061-1069, 1992 A;Title: Identification and isolation of common and tissue-specific geranylgeranylated gamma subunits of guanine-nucleotide-binding regulatory proteins in various tissues. A;Reference number: S27048; MUID:93130886 A;Note: mass spectrographic and chemical characterization C;Comment: For the type I geranylgeranyltransferase the residue may be found at the first position in the sequence motif C-X-X-[LF]* where the second and third positions are usually aliphatic. C;Comment: Formation of S-geranylgeranylcysteine may be coupled with subsequent cleavage of a carboxy-terminal tripeptide for the CAAX motif and methyl esterification of the geranylgeranylated cysteine. Methyl esterification but not cleavage occurs for the CXC motif. C;Comment: For the type II geranylgeranyltransferase the residue may be found at the first and final positions in the sequence motif C-X-C* or at the final position in the sequence motif C-C*. These motifs are necessary but not sufficient for modification. C;Generating enzyme: protein-cysteine geranylgeranyltransferase (EC 2.5.1.-) C;Sequence code: C A;Conditions: combinable; incidental to RESID:AA0105 C;Keywords: lipoprotein; prenylated cysteine F;/Binding site: geranyl-geranyl (Cys) (covalent) >TX;AA0105 L-cysteine methyl ester N;Systematic name: (R)-2-amino-3-mercaptopropanoic methyl ester A;Cross-references: CAS:2485-63-3 C;Formula: C 4 H 8 N 1 O 2 S 1 A;Formula weight: #chem 134.18 #phys 134.0276 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Tuinman, A.A.; Thomas, D.A.; Cook, K.D.; Xue, C.B.; Naider, F.; Becker, J.M. Anal. Biochem. 193, 173-177, 1991 A;Title: Mass spectrometric signature of S-prenylated cysteine peptides. A;Reference number: A44567; MUID:91336511 A;Note: mass spectrographic identification C;Generating enzyme: protein-S-isoprenylcysteine O-methyltransferase (EC 2.1.1.100) C;Sequence code: C A;Conditions: carboxyl-terminal; secondary to RESID:AA0102; secondary to RESID:AA0103; secondary to RESID:AA0104 C;Keywords: methylated carboxyl end F;/Modified site: methyl ester carboxyl end (Cys) F;/Modified site: methyl ester carboxyl end (Cys) (in mature form) >TX;AA0106 S-palmitoyl-L-cysteine N;Alternate names: hexadecanoate cysteine thioester N;Systematic name: (R)-2-amino-3-(hexadecanoylthio)propanoic acid A;Cross-references: CAS:114507-35-6 C;Formula: C 19 H 35 N 1 O 2 S 1 + A;Formula weight: #chem 341.56 + #phys 341.2388 + C;Correction formula: C 16 H 30 O 1 + A;Correction weight: #chem 238.42 + #phys 238.2297 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Bach, R.; Konigsberg, W.H.; Nemerson, Y. Biochemistry 27, 4227-4231, 1988 A;Title: Human tissue factor contains thioester-linked palmitate and stearate on the cytoplasmic half-cystine. A;Reference number: A37422; MUID:89000604 A;Note: chemical characterization R;Stults, J.T.; Griffin, P.R.; Lesikar, D.D.; Naidu, A.; Moffat, B.; Benson, B.J. Am. J. Physiol. 261, L118-L125, 1991 A;Title: Lung surfactant protein SP-C from human, bovine, and canine sources contains palmityl cysteine thioester linkages. A;Reference number: A61249; MUID:91336436 A;Note: mass spectrographic identification R;Johansson, J.; Szyperski, T.; Curstedt, T.; Wuthrich, K. Biochemistry 33, 6015-6023, 1994 A;Title: The NMR structure of the pulmonary surfactant-associated polypeptide sp-C in an apolar solvent contains a valyl-rich alpha-helix. A;Reference number: A58575; MUID:94235672 A;Note: (1)H-NMR identification C;Comment: The palmitate group represents a mixture of saturated and unsaturated fatty acids. C;Sequence code: C A;Conditions: combinable C;Keywords: lipoprotein; thiolester bond F;/Binding site: palmitate (Cys) (covalent) >TX;AA0107 S-diacylglycerol-L-cysteine N;Alternate names: S-(1-2'-oleoyl-3'-palmitoyl-glycerol)cysteine N;Systematic name: (R)-2-amino-3-[(S)-2-((Z)-9-octadecenoyloxy)-3-(hexadecanoyloxy)propyl]thiopropanoic acid C;Formula: C 40 H 73 N 1 O 5 S 1 A;Formula weight: #chem 680.10 #phys 679.5209 C;Correction formula: C 37 H 68 O 4 A;Correction weight: #chem 576.95 #phys 576.5118 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Hantke, K.; Braun, V. Eur. J. Biochem. 34, 284-296, 1973 A;Title: Covalent binding of lipid to protein. A;Reference number: A91204; MUID:73196685 A;Note: chromatographic and mass spectrographic identification; chemical synthesis R;Weyer, K.A.; Schaefer, W.; Lottspeich, F.; Michel, H. Biochemistry 26, 2909-2914, 1987 A;Title: The cytochrome subunit of the photosynthetic reaction center from Rhodopseudomonas viridis is a lipoprotein. A;Reference number: A44772 A;Note: chromatographic and mass spectrographic identification; this amino-terminal cysteine has a free alpha-amino group C;Comment: The oleate and palmitate actually represent mixtures of saturated (generally at 3') and unsaturated (generally at 2') fatty acids. C;Sequence code: C A;Conditions: incidental to RESID:AA0060 C;Keywords: lipoprotein F;/Binding site: sn-2,3-diacylglycerol (Cys) (covalent) >TX;AA0108 S-(L-isoglutamyl)-L-cysteine N;Alternate names: gamma-(S-cysteinyl)glutamic acid; (S,R)-2-amino-4-[S-(2-amino-2-carboxyethyl)thiocarboxy]butanoic acid N;Systematic name: (S)-2-amino-5-((R)-2-amino-2-carboxyethyl)thio-5-oxopentanoic acid A;Cross-references: CAS:105580-05-0 C;Formula: C 8 H 10 N 2 O 3 S 1 A;Formula weight: #chem 214.25 #phys 214.0412 C;Correction formula: C 0 H -3 N -1 A;Correction weight: #chem -17.03 #phys -17.0265 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Thomas, M.L.; Tack, B.F. Biochemistry 22, 942-947, 1983 A;Title: Identification and alignment of a thiol ester site in the third component of guinea pig complement. A;Reference number: A90479; MUID:83178889 A;Note: chemical characterization C;Sequence code: C, Q A;Conditions: cross-link 2 C;Keywords: thiolester bond F;/Cross-link: thiolester (Cys-Gln) F;/Cross-link: thiolester (Gln-Cys) F;/Cross-link: thiolester (Cys) (interchain to Gln ...) F;/Cross-link: thiolester (Gln) (interchain to Cys ...) >TX;AA0109 2'-(S-L-cysteinyl)-L-histidine N;Alternate names: S-(2'-histidyl)cysteine N;Systematic name: (S)-2-amino-3-[2-((R)-2-amino-2-carboxyethyl)thioimidazol-4-yl]propanoic acid A;Cross-references: CAS:77504-36-0 C;Formula: C 9 H 10 N 4 O 2 S 1 A;Formula weight: #chem 238.27 #phys 238.0524 C;Correction formula: C 0 H -2 A;Correction weight: #chem -2.02 #phys -2.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Lerch, K. J. Biol. Chem. 257, 6414-6419, 1982 A;Title: Primary structure of tyrosinase from Neurospora crassa. II. Complete amino acid sequence and chemical structure of a tripeptide containing an unusual thioether. A;Reference number: A92374; MUID:82190018 A;Note: chemical characterization C;Comment: Cysteinylhistidine probably does not have a functional role in the enzymatic activity of Neurospora crassa tyrosinase. C;Sequence code: C, H A;Conditions: cross-link 2 F;/Cross-link: cysteinylhistidine (Cys-His) F;/Cross-link: cysteinylhistidine (His-Cys) >TX;AA0110 L-lanthionine N;Alternate names: 3,3'-thiobis-L-alanine; (R)-S-(2-amino-2-carboxyethyl)-L-cysteine; (R,R)-3,3'-thiobis-(2-aminopropanoic acid); (R,R)-2,6-diamino-4-thiaheptanedioic acid N;Systematic name: (R,R)-bis(2-amino-2-carboxyethyl)sulfide A;Cross-references: CAS:922-55-4 C;Formula: C 6 H 8 N 2 O 2 S 1 A;Formula weight: #chem 172.21 #phys 172.0306 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 C;Sequence code: C, S A;Conditions: cross-link 2 C;Keywords: lanthionine F;/Cross-link: (2R,6R)-lanthionine (Cys-Ser) F;/Cross-link: (2R,6R)-lanthionine (Ser-Cys) >TX;AA0111 meso-lanthionine N;Alternate names: 3,3'-thiobis-meso-alanine; (R)-S-(2-amino-2-carboxyethyl)-D-cysteine; (R,S)-3,3'-thiobis-(2-aminopropanoic acid); (R,S)-bis(2-amino-2-carboxyethyl)sulfide; (R,S)-2,6-diamino-4-thiaheptanedioic acid N;Systematic name: (R,S)-bis(2-amino-2-carboxyethyl)sulfide A;Cross-references: CAS:922-56-5 C;Formula: C 6 H 8 N 2 O 2 S 1 A;Formula weight: #chem 172.21 #phys 172.0306 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Allgaier, H.; Jung, G.; Werner, R.G.; Schneider, U.; Zaehner, H. Eur. J. Biochem. 160, 9-22, 1986 A;Title: Epidermin: sequencing of a heterodet tetracyclic 21-peptide amide antibiotic. A;Reference number: A61287; MUID:87030262 A;Note: (1)H-NMR and (13)C-NMR identification; chemical synthesis C;Comment: The stereosymmetry is broken within a peptide chain; the higher precidence is assigned to the peptide closest to the amino-terminal. C;Sequence code: C, S A;Conditions: cross-link 2 C;Keywords: lanthionine F;/Cross-link: sn-(2S,6R)-lanthionine (Ser-Cys) F;/Cross-link: sn-(2R,6S)-lanthionine (Cys-Ser) >TX;AA0112 3-methyl-L-lanthionine N;Alternate names: (2S,3S,6R)-2,6-diamino-3-methyl-4-thiaheptanedioic acid; (2S-[2R*,3R*(S*)])-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid N;Systematic name: (2S,3S,2'R)-2-amino-3-[(2-amino-2-carboxyethyl)thio]butanoic acid A;Cross-references: CAS:42849-28-5 C;Formula: C 7 H 10 N 2 O 2 S 1 A;Formula weight: #chem 186.24 #phys 186.0463 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Allgaier, H.; Jung, G.; Werner, R.G.; Schneider, U.; Zaehner, H. Eur. J. Biochem. 160, 9-22, 1986 A;Title: Epidermin: sequencing of a heterodet tetracyclic 21-peptide amide antibiotic. A;Reference number: A61287; MUID:87030262 A;Note: (1)H-NMR and (13)C-NMR identification; chemical synthesis C;Comment: Other stereoisomers at positions 2 and 3 are possible. C;Sequence code: C, T A;Conditions: cross-link 2 C;Keywords: lanthionine F;/Cross-link: (2S,3S,6R)-3-methyl-lanthionine (Cys-Thr) F;/Cross-link: (2S,3S,6R)-3-methyl-lanthionine (Thr-Cys) >TX;AA0113 3'-(S-L-cysteinyl)-L-tyrosine N;Alternate names: S-(3'-tyrosinyl)cysteine N;Systematic name: (S,R)-2-amino-3-[3-(2-amino-2-carboxyethylthio)-4-hydroxyphenyl]propanoic acid C;Formula: C 12 H 11 N 2 O 3 S 1 A;Formula weight: #chem 263.30 #phys 263.0490 C;Correction formula: C 0 H -2 A;Correction weight: #chem -2.02 #phys -2.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Ito, N.; Phililips, S.E.V.; Stevens, C.; Ogel, Z.B.; McPherson, M.J.; Keen, J.N.; Yadav, K.D.S.; Knowles, P.F. Nature 350, 87-90, 1991 A;Title: Novel thioether bond revealed by a 1.7 angstrom crystal structure of galactose oxidase. A;Reference number: A48244; MUID:91163641 C;Comment: Cysteinyltyrosine may exist as a stable free radical; the bond between the sulfur and the phenyl ring appears to have some double bond character. C;Sequence code: C, Y A;Conditions: cross-link 2 F;/Cross-link: cysteinyltyrosine (Cys-Tyr) F;/Cross-link: cysteinyltyrosine (Tyr-Cys) >TX;AA0114 N6-carboxy-L-lysine N;Alternate names: N6-carboxylysine N;Systematic name: (S)-2-amino-6-carbamic hexanoic acid A;Cross-references: CAS:45101-60-8 C;Formula: C 7 H 12 N 2 O 3 A;Formula weight: #chem 172.19 #phys 172.0848 C;Correction formula: C 1 H 0 O 2 A;Correction weight: #chem 44.01 #phys 43.9898 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Morrow, J.S.; Keim, P.; Gurd, F.R.N. J. Biol. Chem. 249, 7484-7494, 1974 A;Title: CO-2 adducts of certain amino acids, peptides, and sperm whale myoglobin studied by carbon 13 and proton nuclear magnetic resonance. A;Reference number: A44725; MUID:75060443 A;Note: (1)H-NMR and (13)C-NMR identification R;Stringer, C.D.; Hartman, F.C. Biochem. Biophys. Res. Commun. 80, 1043-1048, 1978 A;Title: Sequences of two active-site peptides from spinach ribulosebisphosphate carboxylase/oxygenase. A;Reference number: A90208; MUID:78144263 R;Jabri, E.; Carr, M.B.; Hausinger, R.P.; Karplus, P.A. Science 268, 998-1004, 1995 A;Title: The crystal structure of urease from Klebsiella aerogenes. A;Reference number: A56340; MUID:95273988 A;Note: X-ray crystallography, 2.2 angstroms C;Generating enzyme: ribulose-bisphosphate carboxylase activase (EC 6.3.-.-); urease activase (EC 6.3.-.-) C;Sequence code: K A;Conditions: combinable F;/Binding site: carbon dioxide (Lys) (covalent) (by ...) >TX;AA0115 N6-1-carboxyethyl-L-lysine N;Alternate names: N6-(1-carboxyethyl)lysine N;Systematic name: (S,S)-2-amino-6-(1-carboxyethyl)aminohexanoic acid A;Cross-references: CAS:68852-50-6 C;Formula: C 9 H 16 N 2 O 3 A;Formula weight: #chem 200.24 #phys 200.1161 C;Correction formula: C 3 H 4 O 2 A;Correction weight: #chem 72.06 #phys 72.0211 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Thompson, J.; Miller, S.P.F. J. Biol. Chem. 263, 2064-2069, 1988 A;Title: N6-(1-carboxyethyl)lysine formation by Stretococcus lactis. Purification, synthesis, and stereochemical structure. A;Reference number: A43058; MUID:88115337 A;Note: chromatographic detection; (1)H-NMR identification; chemical synthesis confirmation of stereochemistry R;Krook, M.; Ghosh, D.; Stroemberg, R.; Carlquist, M.; Joernvall, H. Proc. Natl. Acad. Sci. U.S.A. 90, 502-506, 1993 A;Title: Carboxyethyllysine in a protein: native carbonyl reductase/NADP+-dependent prostaglandin dehydrogenase. A;Reference number: A47326; MUID:93133816 A;Note: mass spectrographic detection; (1)H-NMR identification; chemical synthesis C;Sequence code: K F;/Modified site: N6-1-carboxyethyllysine (Lys) >TX;AA0116 N6-(4-amino-2-hydroxybutyl)-L-lysine N;Alternate names: hypusine N;Systematic name: (S,R)-2-amino-6-(4-amino-2-hydroxybutylamino)hexanoic acid A;Cross-references: CAS:34994-11-1 C;Formula: C 10 H 21 N 3 O 2 A;Formula weight: #chem 215.30 #phys 215.1634 C;Correction formula: C 4 H 9 N 1 O 1 A;Correction weight: #chem 87.12 #phys 87.0684 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Park, M.H.; Cooper, H.L.; Folk, J.E. J. Biol. Chem. 257, 7217-7222, 1982 A;Title: The biosynthesis of protein-bound hypusine (N(epsilon)-(4-amino-2-hydroxybutyl)lysine). Lysine as the amino acid precursor and the intermediate role of deosyhypusine (N(epsilon)-(4-aminobutyl)lysine). A;Reference number: A44553; MUID:82213873 A;Note: biosynthesis R;Park, M.H.; Wolff, E.C.; Folk, J.E. Trends Biochem. Sci. 18, 475-479, 1993 A;Title: Is hypusine essential for eukaryotic cell proliferation? A;Reference number: A44558; MUID:94151824 A;Note: review article C;Comment: Hypusine appears to occur uniquely in translation initiation factor eIF-5A. C;Sequence code: K C;Keywords: hypusine F;/Modified site: N6-(4-amino-2-hydroxybutyl)lysine (Lys) >TX;AA0117 N6-biotinyl-L-lysine N;Alternate names: biocytin; N6-biotinyllysine N;Systematic name: 2-amino-6-[5-(hexahydro-2-oxo-1H-thieno[3,4-d]imidazol-4-yl)-1-oxopentyl]aminohexanoic acid A;Cross-references: CAS:576-19-2 C;Formula: C 16 H 26 N 4 O 3 S 1 A;Formula weight: #chem 354.48 #phys 354.1726 C;Correction formula: C 10 H 14 N 2 O 2 S 1 A;Correction weight: #chem 226.30 #phys 226.0776 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Thampy, K.G.; Huang, W.Y.; Wakil, S.J. Arch. Biochem. Biophys. 266, 270-276, 1988 A;Title: A rapid purification method for rat liver pyruvate carboxylase and amino acid sequence analyses of NH2-terminal and biotin peptide. A;Reference number: S06440; MUID:89024676 A;Note: affinity chromatography and chromatographic detection R;Duval, M.; DeRose, R.T.; Job, C.; Faucher, D.; Douce, R.; Job, D. Plant Mol. Biol. 26, 265-273, 1994 A;Title: The major biotinyl protein from Pisum sativum seeds covalently binds biotin at a novel site. A;Reference number: S52657; MUID:95035998 A;Note: biotin covalently bound at a site differing from the usual biotin binding homology C;Generating enzyme: biotin--protein ligase (EC 6.3.4.-) C;Sequence code: K A;Conditions: combinable C;Keywords: biotin F;/Binding site: biotin (Lys) (covalent) >TX;AA0118 N6-lipoyl-L-lysine N;Alternate names: N6-lipoyllysine; (2S,6'R)-2-amino-6-(6,8-dithiooctanamido)hexanoic acid; 2-amino-6-(5-[1,2-dithiolan-3-yl]-1-oxopentyl)hexanoic acid N;Systematic name: (S,R)-2-amino-6-[5-(1,2-dithiolan-3-yl)pentanamido]hexanoic acid A;Cross-references: CAS:1676-89-7 C;Formula: C 14 H 24 N 2 O 2 S 2 A;Formula weight: #chem 316.49 #phys 316.1279 C;Correction formula: C 8 H 12 O 1 S 2 A;Correction weight: #chem 188.32 #phys 188.0330 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Fujiwara, K.; Okamura-Ikeda, K.; Motokawa, Y. J. Biol. Chem. 261, 8836-8841, 1986 A;Title: Chicken liver H-protein, a component of the glycine cleavage system: amino acid sequence and identification of the N-lipoyllysine residue. A;Reference number: A25718; MUID:86250806 A;Note: detection of radiolabeled N-ethylmaleimide, PTH derivative R;Packman, L.C.; Borges, A.; Perham, R.N. Biochem. J. 252, 79-86, 1988 A;Title: Amino acid sequence analysis of the lipoyl and peripheral subunit-binding domains in the lipoate acetyltransferase component of the pyruvate dehydrogenase complex from Bacillus stearothermophilus. A;Reference number: S00598; MUID:88339820 A;Note: mass spectrographic identification of bis-pyridethylated derivative R;Cohen-Addad, C.; Pares, S.; Sieker, L.; Neuburger, M.; Douce, R. Nature Struct. Biol. 2, 63-68, 1995 A;Title: The lipoamide arm in the glycine decarboxylase complex is not freely swinging. A;Reference number: A44677; MUID:95236204 A;Note: X-ray crystallography, 2.6 angstroms C;Generating enzyme: lipoate--protein ligase (EC 6.3.4.-) C;Sequence code: K A;Conditions: combinable C;Keywords: lipoamide F;/Binding site: lipoamide (Lys) (covalent) >TX;AA0119 N6-pyridoxal phosphate-L-lysine N;Systematic name: (S)-2-amino-6-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-4-pyridine)methyleneamino]hexanoic acid A;Cross-references: CAS:2440-59-7 C;Formula: C 14 H 20 N 3 O 6 P 1 A;Formula weight: #chem 357.31 #phys 357.1090 C;Correction formula: C 8 H 8 N 1 O 5 P 1 A;Correction weight: #chem 229.13 #phys 229.0140 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 24-Nov-1999 R;Bohney, J.P.; Fonda, M.L.; Feldhoff, R.C. FEBS Lett. 298, 266-268, 1992 A;Title: Identification of Lys(190) as the primary binding site for pyridoxal 5'-phosphate in human serum albumin. A;Reference number: A56294; MUID:92183881 A;Note: sequencing after reaction with (3)H-pyridoxal phosphate and borohydride reduction C;Sequence code: K A;Conditions: combinable C;Keywords: phosphoprotein; pyridoxal phosphate F;/Binding site: pyridoxal phosphate (Lys) (covalent) >TX;AA0120 N6-retinal-L-lysine N;Alternate names: retinylidene-lysine N;Systematic name: (S)-2-amino-6-[3,7-dimethyl-9-(2,6,6-trimethyl-1-cyclohexen-1-yl)-2,4,6,8-nonatetraenylidene]aminohexanoic acid A;Cross-references: CAS:130443-70-8 C;Formula: C 26 H 38 N 2 O 1 A;Formula weight: #chem 394.61 #phys 394.2984 C;Correction formula: C 20 H 26 A;Correction weight: #chem 266.43 #phys 266.2035 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Mullen, E.; Akhtar, M. Biochem. J. 211, 45-54, 1983 A;Title: Structural studies on membrane-bound bovine rhodopsin. A;Reference number: A90318; MUID:83256442 A;Note: chemical conversion and identification as carboxymethyllysine R;Katre, N.V.; Wolber, P.K.; Stoeckenius, W.; Stroud, R.M. Proc. Natl. Acad. Sci. U.S.A. 78, 4068-4072, 1981 A;Title: Attachment site(s) of retinal in bacteriorhodopsin. A;Reference number: A93877; MUID:82037784 A;Note: radiolabeling; chemical conversion and identification as retinyllysine C;Sequence code: K A;Conditions: combinable C;Keywords: chromoprotein; retinal F;/Binding site: retinal (Lys) (covalent) >TX;AA0121 L-allysine N;Alternate names: 2-amino-adipic acid semialdahyde; L-6-oxonorleucine N;Systematic name: (S)-2-amino-6-oxohexanoic acid A;Cross-references: CAS:6665-12-9 C;Formula: C 6 H 9 N 1 O 2 A;Formula weight: #chem 127.14 #phys 127.0633 C;Correction formula: C 0 H -3 N -1 O 1 A;Correction weight: #chem -1.03 #phys -1.0316 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 C;Sequence code: K F;/Modified site: allysine (Lys) >TX;AA0123 L-lysinoalanine N;Alternate names: (2Xi,9S)-lysinoalanine N;Systematic name: (2S)-2-amino-6-((2Xi)-2-amino-2-carboxyethylamino)hexanoic acid A;Cross-references: CAS:18810-04-3 C;Formula: C 9 H 15 N 3 O 2 A;Formula weight: #chem 197.24 #phys 197.1164 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Naruse, N.; Tenmyo, O.; Tomita, K.; Konishi, M.; Miyaki, T.; Kawaguchi, H.; Fukase, K.; Wakamiya, T.; Shiba, T. J. Antibiot. 42, 837-845, 1989 A;Title: Lanthiopeptin, a new peptide antibiotic. Production, isolation and properties of lanthiopeptin. A;Reference number: A45767; MUID:89291558 C;Comment: The stereochemistry for the second chiral center has not been resolved; it appears to epimerize rapidly during acid hydrolysis. The (2R,9S) form is shown. C;Sequence code: K; S A;Conditions: cross-link 2 F;/Cross-link: (2Xi,9S)-lysinoalanine (Lys-Ser) F;/Cross-link: (2Xi,9S)-lysinoalanine (Ser-Lys) >TX;AA0124 N6-(L-isoglutamyl)-L-lysine N;Alternate names: gamma-(N6-lysyl)glutamic acid N;Systematic name: (S,S)-2-amino-6-[(4-amino-4-carboxybutanoyl)amino]hexanoic acid A;Cross-references: CAS:23250-50-2 C;Formula: C 11 H 17 N 3 O 3 A;Formula weight: #chem 239.28 #phys 239.1270 C;Correction formula: C 0 H -3 N -1 A;Correction weight: #chem -17.03 #phys -17.0265 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 C;Generating enzyme: protein-glutamine gamma-glutamyltransferase (EC 2.3.2.13) C;Sequence code: K, Q A;Conditions: cross-link 2 F;/Cross-link: isopeptide (Lys-Gln) F;/Cross-link: isopeptide (Gln-Lys) F;/Cross-link: isopeptide (Lys) (interchain to Gln ...) F;/Cross-link: isopeptide (Gln) (interchain to Lys ...) >TX;AA0125 N6-glycyl-L-lysine N;Alternate names: N6-glycyllysine N;Systematic name: (S)-2-amino-6-[(aminoacetyl)amino]hexanoic acid A;Cross-references: CAS:191-22-6 C;Formula: C 8 H 14 N 3 O 2 A;Formula weight: #chem 184.22 #phys 184.1086 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Vierstra, R.D.; Langan, S.M.; Schaller, G.E. Biochemistry 25, 3105-3108, 1986 A;Title: Complete amino acid sequence of ubiquitin from the higher plant Avena sativa. A;Reference number: A02576 C;Sequence code: G, K A;Conditions: cross-link 2; carboxyl-terminal F;/Cross-link: isopeptide carboxyl end (Gly-Lys) F;/Cross-link: isopeptide carboxyl end (Gly) (interchain to Lys ...) F;/Cross-link: isopeptide (Lys) (interchain to Gly ...) >TX;AA0126 N-(L-isoaspartyl)-glycine N;Alternate names: isoaspartyl glycine; N-beta-aspartylglycine; 2-amino-N4-(carboxymethyl)-butanediamic acid N;Systematic name: (S)-2-amino-4-(carboxymethyl)amino-4-oxobutanoic acid A;Cross-references: CAS:3790-52-1 C;Formula: C 6 H 7 N 2 O 3 A;Formula weight: #chem 155.13 #phys 155.0457 C;Correction formula: C 0 H -3 N -1 A;Correction weight: #chem -17.03 #phys -17.0265 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Wyss, D.F.; Lahm, H.W.; Manneberg, M.; Labhardt, A.M. J. Antibiot. 44, 172-180, 1991 A;Title: Anantin -- a peptide antagonist of the atrial natriuretic factor (ANF). II. Determination of the primary sequence by NMR on the basis of proton assignments. A;Reference number: A61211; MUID:91185186 A;Note: (1)H-NMR identification C;Sequence code: G, N A;Conditions: cross-link 2; amino-terminal F;/Cross-link: isopeptide amino end (Gly-Asn) F;/Cross-link: isopeptide amino end (Gly) (interchain to Asn ...) F;/Cross-link: isopeptide (Asn) (interchain to Gly ...) >TX;AA0127 pyruvic acid N;Systematic name: 2-oxopropanoic acid A;Cross-references: CAS:127-17-3 C;Formula: C 3 H 3 O 2 A;Formula weight: #chem 71.06 #phys 71.0133 C;Correction formula: C 0 H -2 N -1 O 1 S -1 A;Correction weight: #chem -32.09 #phys -31.9959 C;Correction formula: C 0 H -2 N -1 A;Correction weight: #chem -16.02 #phys -16.0187 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Gallagher, T.; Rozwarski, D.A.; Ernst, S.R.; Hackert, M.L. J. Mol. Biol. 230, 516-528, 1993 A;Title: Refined structure of the pyruvoyl-dependent histidine decarboxylase from Lactobacillus 30a. A;Reference number: A58363; MUID:93217991 A;Note: X-ray crystallography, 2.5 angstroms R;Gallagher, T.; Rozwarski, D.A.; Ernst, S.R.; Hackert, M.L. submitted to the Brookhaven Protein Data Bank, December 1992 A;Reference number: A51934; PDB:1PYA A;Contents: annotation; X-ray crystallography, 2.5 angstroms R;Kabisch, U.C.; Graentzdoerffer, A.; Schierhorn, A.; Ruecknagel, K.P.; Andreesen, J.R.; Pich, A. J. Biol. Chem. 274, 8445-8454, 1999 A;Title: Identification of D-proline reductase from clostridium sticklandii as a selenoenzyme and indications for a catalytically active pyruvoyl group derived from a cysteine residue by cleavage of a proprotein. A;Reference number: A59051; MUID:99185060 A;Note: mass spectrographic and chemical characterization R;Dixon, H.B.F.; Fields, R. Methods Enzymol. 25, 409-419, 1972 A;Title: Specific modification of NH2-terminal residues by transamination. A;Reference number: A30653 A;Note: chemical detection and amino terminal release using 1,2-diaminobenzene C;Comment: The pyruvic acid forming an amide bond between its 1-carboxyl group and an amino terminal residue arises from oxidative deamination of an encoded amino acid, either cysteine or serine. It is important to distinguish this modification from an exogenous pyruvic acid forming a ketimine bond with its 2-keto group and an amino terminal residue (see RESID:AA0274 and RESID:AA0275). C;Sequence code: C #link CYS; S #link SER A;Conditions: amino-terminal C;Keywords: blocked amino end F;/Modified site: pyruvic acid (Cys) #link CYS F;/Modified site: pyruvic acid (Cys) (in mature form) #link CYS F;/Modified site: pyruvic acid (Ser) #link SER F;/Modified site: pyruvic acid (Ser) (in mature form) #link SER >TX;AA0128 L-3-phenyllactic acid N;Systematic name: (S)-2-hydroxy-3-phenylpropanoic acid A;Cross-references: CAS:20312-36-1 C;Formula: C 9 H 9 O 2 A;Formula weight: #chem 149.17 #phys 149.0603 C;Correction formula: C 0 H 0 N -1 O 1 A;Correction weight: #chem 1.99 #phys 1.9918 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Grimmelikhuijzen, C.J.P.; Rinehart, K.L.; Jacob, E.; Graff, D.; Reinscheid, R.K.; Nothacker, H.P.; Staley, A.L. Proc. Natl. Acad. Sci. U.S.A. 87, 5410-5414, 1990 A;Title: Isolation of L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide), a sea anemone neuropeptide containing an unusual amino-terminal blocking group. A;Reference number: A35779; MUID:90319122 A;Note: mass spectrographic and (1)H-NMR identification; chromatographic stereochemical characterization; chemical synthesis C;Sequence code: F A;Conditions: amino-terminal C;Keywords: blocked amino end F;/Modified site: L-3-phenyllactic acid (Phe) F;/Modified site: L-3-phenyllactic acid (Phe) (in mature form) >TX;AA0129 2-oxobutanoic acid N;Systematic name: 2-oxobutanoic acid A;Cross-references: CAS:600-18-0 C;Formula: C 4 H 5 O 2 A;Formula weight: #chem 85.08 #phys 85.0290 C;Correction formula: C 0 H -3 N -1 A;Correction weight: #chem -17.03 #phys -17.0265 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 C;Sequence code: T A;Conditions: amino-terminal C;Keywords: blocked amino end F;/Modified site: 2-oxobutanoic acid (Thr) F;/Modified site: 2-oxobutanoic acid (Thr) (in mature form) >TX;AA0130 N2-succinyl-L-tryptophan N;Systematic name: (S)-2-(3-carboxypropanoyl)amino-3-(1H-indol-3-yl)propanoic acid C;Formula: C 15 H 15 N 2 O 4 A;Formula weight: #chem 287.30 #phys 287.1032 C;Correction formula: C 4 H 6 O 3 A;Correction weight: #chem 102.09 #phys 102.0317 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Chan, W.C.; Bycroft, B.W.; Leyland, M.L.; Lian, L.Y.; Roberts, G.C.K. Biochem. J. 291, 23-27, 1993 A;Title: A novel post-translational modification of the peptide antibiotic subtilin: isolation and characterization of a natural variant from Bacillus subtilis A.T.C.C. 6633. A;Reference number: A53265; MUID:93228611 A;Note: mass spectrographic, (1)H-NMR, and (13)C-NMR identification; chemical synthesis C;Sequence code: W A;Conditions: amino-terminal C;Keywords: blocked amino end F;/Modified site: succinylated amino end (Trp) F;/Modified site: succinylated amino end (Trp) (in mature form) >TX;AA0131 S-phycocyanobilin-L-cysteine N;Systematic name: (2R,3R)-18-ethyl-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylthio)ethyl]-1,2,3,19,21,22,24-heptahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid C;Formula: C 36 H 43 N 5 O 7 S 1 A;Formula weight: #chem 689.84 #phys 689.2883 C;Correction formula: C 33 H 38 N 4 O 6 A;Correction weight: #chem 586.69 #phys 586.2791 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 30-Sep-1999 R;Szalontai, B.; Gombos, Z.; Csizmadia, V.; Bagyinka, C.; Lutz, M. Biochemistry 33, 11823-11832, 1994 A;Title: Structure and interactions of phycocyanobilin chromophores in phycocyanin and allophycocyanin from an analysis of their resonance Raman spectra. A;Reference number: A55835; MUID:95001892 A;Note: raman spectroscopy of covalently bound (14)N and (15)N isotopic chromophores R;Nagy, J.O.; Bishop, J.E.; Klotz, A.V.; Glazer, A.N.; Rapoport, H. J. Biol. Chem. 260, 4864-4868, 1985 A;Title: Bilin attachment sites in the alpha, beta, and gamma subunits of R-phycoerythrin. Structural studies on singly and doubly linked phycourobilins. A;Reference number: A22564; MUID:85182602 A;Note: mass spectrographic and (1)H-NMR identification R;Stec, B.; Troxler, R.F.; Teeter, M.M. submitted to the Brookhaven Protein Data Bank, June 1995 A;Reference number: A68150; PDB:1PHN A;Note: X-ray crystallography, 1.65 angstroms C;Comment: A second linkage, an ester between a serine and one of the propanoic acid groups, was reported at one time but was not confirmed. A second cysteine linkage has also been reported to a moiety thought to be phycocyanobilin. C;Comment: The phycocyanobilins transmit blue. C;Sequence code: C A;Conditions: not combinable C;Keywords: chromoprotein; phycocyanobilin F;/Binding site: phycocyanobilin (Cys) (covalent) >TX;AA0132 S-phycoerythrobilin-L-cysteine N;Systematic name: 18-ethyl-3-[1-((2-amino-2-carboxy)ethylthio)ethyl]-1,2,3,19,21,22,24-heptahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-bilin-8,12-dipropanoic acid C;Formula: C 36 H 45 N 5 O 7 S 1 A;Formula weight: #chem 691.86 #phys 691.3040 C;Correction formula: C 33 H 40 N 4 O 6 A;Correction weight: #chem 588.71 #phys 588.2948 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Nagy, J.O.; Bishop, J.E.; Klotz, A.V.; Glazer, A.N.; Rapoport, H. J. Biol. Chem. 260, 4864-4868, 1985 A;Title: Bilin attachment sites in the alpha, beta, and gamma subunits of R-phycoerythrin. Structural studies on singly and doubly linked phycourobilins. A;Reference number: A22564; MUID:85182602 A;Note: mass spectrographic and (1)H-NMR identification C;Comment: See the comment for S-phycocyanobilin-L-cysteine (RESID:AA0131). There is an additional chiral center at C-16. C;Comment: The phytochromobilins and phycoerythrobilins transmit red. C;Sequence code: C A;Conditions: not combinable C;Keywords: chromoprotein; phytochromobilin F;/Binding site: phycoerythrobilin (Cys) (covalent) >TX;AA0133 S-phytochromobilin-L-cysteine N;Alternate names: phytochrome N;Systematic name: 18-ethenyl-3-[1-((2-amino-2-carboxy)ethylthio)ethyl]-1,2,3,19,22,24-hexahydro-2,7,13,17-tetramethyl-1,19-dioxo-21H-biline-8,12-dipropanoic acid C;Formula: C 36 H 41 N 5 O 7 S 1 A;Formula weight: #chem 687.82 #phys 687.2727 C;Correction formula: C 33 H 36 N 4 O 6 A;Correction weight: #chem 584.68 #phys 584.2635 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Szalontai, B.; Gombos, Z.; Csizmadia, V.; Bagyinka, C.; Lutz, M. Biochemistry 33, 11823-11832, 1994 A;Title: Structure and interactions of phycocyanobilin chromophores in phycocyanin and allophycocyanin from an analysis of their resonance Raman spectra. A;Reference number: A55835; MUID:95001892 A;Note: raman spectroscopy of covalently bound (14)N and (15)N isotopic chromophores C;Comment: See the comment for S-phycocyanobilin-L-cysteine (RESID:AA0131). C;Comment: The phytochromobilins and phycoerythrobilins transmit red. C;Sequence code: C A;Conditions: not combinable C;Keywords: chromoprotein; phytochromobilin F;/Binding site: phytochromobilin (Cys) (covalent) >TX;AA0134 heme-bis-L-cysteine N;Alternate names: biscysteinyl heme N;Systematic name: (R,R)-[7,12-bis[1-((2-amino-2-carboxy)ethylthio)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate C;Formula: C 40 H 42 Fe 1 N 6 O 6 S 2 A;Formula weight: #chem 822.80 #phys 822.1957 C;Correction formula: C 34 H 32 Fe 1 N 4 O 4 A;Correction weight: #chem 616.51 #phys 616.1773 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 30-Sep-1999 R;Dickerson, R.E.; Takano, T.; Eisenberg, D.; Kallai, O.B.; Samson, L.; Cooper, A.; Margoliash, E. J. Biol. Chem. 246, 1511-1533, 1971 A;Title: Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 A resolution. A;Reference number: A92076; MUID:71116428 A;Note: X-ray crystallography, 2.8 angstroms R;Gans, P.; Simorre, J.P.; Caffrey, M.; Marion, D.; Richaud, P.; Vermeglio, A. J. Biochem. 119, 1131-1142, 1996 A;Title: Sequential 1H and 15N NMR resonance assignment and secondary structure of ferrocytochrome c2 from Rhodobacter sphaeroides. A;Reference number: JC4794; MUID:96424998 A;Note: (1)H-NMR and (15)N-NMR characterization; conformation of residues 22-145 C;Generating enzyme: holocytochrome-c synthase (EC 4.4.1.17) C;Sequence code: C, C A;Conditions: cross-link 2; not combinable C;Keywords: chromoprotein; heme; iron; metalloprotein F;/Binding site: heme (Cys) (covalent) >TX;AA0135 heme-L-cysteine N;Alternate names: cysteinyl heme N;Systematic name: (R)-[12-ethenyl-7-[1-((2-amino-2-carboxy)ethylthio)ethyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate C;Formula: C 37 H 37 Fe 1 N 5 O 5 S 1 A;Formula weight: #chem 719.65 #phys 719.1865 C;Correction formula: C 34 H 32 Fe 1 N 4 O 4 A;Correction weight: #chem 616.51 #phys 616.1773 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 30-Sep-1999 R;Pettigrew, G.W.; Leaver, J.L.; Meyer, T.E.; Ryle, A.P. Biochem. J. 147, 291-302, 1975 A;Title: Purification, properties and amino acid sequence of atypical cytochrome c from two protozoa, Euglena gracilis and Crithidia oncopelti. A;Reference number: A00068; MUID:76039443 A;Note: chemical and spectrographic characterization; it is uncertain whether the cysteine is linked through the 7-vinyl (as indicated) or through the 12-vinyl group R;Mukai, K.; Yoshida, M.; Toyosaki, H.; Yao, Y.; Wakabayashi, S.; Matsubara, H. Eur. J. Biochem. 178, 649-656, 1989 A;Title: An atypical heme-binding structure of cytochrome c1 of Euglena gracilis mitochondrial complex III. A;Reference number: S02075; MUID:89107187 A;Note: chemical and spectrographic characterization R;Miller, M.J.; Rapoport, H. J. Am. Chem. Soc. 99, 3479-3485, 1977 A;Title: Porphyrin-protein bond of cytochrome c558 from Euglena gracilis. A;Reference number: A30652 A;Note: chemical characterization; the linkage is established to be through the 7-ethenyl group R;Yu, J.; Le Brun, N.E. J. Biol. Chem. 273, 8860-8866, 1998 A;Title: Studies of the cytochrome subunits of menaquinone:cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit. A;Reference number: A59058; MUID:98204874 A;Note: chemical characterization; demonstration of an unusual covalent heme attachment in a cytochrome b C;Generating enzyme: holocytochrome-c synthase (EC 4.4.1.17) C;Sequence code: C A;Conditions: not combinable C;Keywords: chromoprotein; heme; iron; metalloprotein F;/Binding site: heme (Cys) (covalent) >TX;AA0136 tetrakis-L-cysteinyl iron N;Systematic name: tetrakis-S-cysteinyliron C;Formula: C 12 H 16 Fe 1 N 4 O 4 S 4 A;Formula weight: #chem 464.40 #phys 463.9404 C;Correction formula: C 0 H -4 Fe 1 A;Correction weight: #chem 51.82 #phys 51.9036 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Watenpaugh, K.D.; Siecker, L.C.; Herriott, J.R.; Jensen, L.H. Acta Crystallogr. B29, 943-956, 1973 A;Title: Refinement of the model of a protein: rubredoxin at 1.5 angstrom resolution. A;Reference number: A90009 A;Note: X-ray crystallography, 1.5 angstroms R;Day, M.W.; Hsu, B.T.; Joshua-tor, L.; Park, J.B.; Zhou, Z.H.; Adams, M.W.W.; Rees, D.C. Protein Sci. 1, 1494-1507, 1992 A;Title: X-ray crystal structures of the oxidized and reduced forms of the rubredoxin from the marine hyperthermophilic archaebacterium Pyrococcus furiosus. A;Reference number: A44625; MUID:93271899 A;Note: X-ray crystallography, 1.8 angstroms R;Meyer, J.; Gagnon, J.; Sieker, L.C.; Van Dorsselaer, A.; Moulis, J.M. Biochem. J. 271, 839-841, 1990 A;Title: Rubredoxin from Clostridium thermosaccharolyticum. Amino acid sequence, mass-spectrometric and preliminary crystallographic data. A;Reference number: A33173; MUID:91058526 A;Note: mass spectrographic detection C;Comment: Tetrakis-S-cysteinyliron is not classified as a covalent binding site feature, but may be regarded as the simplest iron-sulfur cluster. C;Sequence code: C, C, C, C A;Conditions: cross-link 4 C;Keywords: iron; metalloprotein F;/Binding site: iron (Cys) >TX;AA0137 tetrakis-L-cysteinyl diiron disulfide N;Systematic name: di-mu-sulfidobis(di-S-cysteinyliron) C;Formula: C 12 H 16 Fe 2 N 4 O 4 S 6 A;Formula weight: #chem 584.38 #phys 583.8195 C;Correction formula: C 0 H -4 Fe 2 S 2 A;Correction weight: #chem 171.79 #phys 171.7827 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 11-Jun-1999 R;Tsukihara, T.; Fukuyama, K.; Nakamura, M.; Katsube, Y.; Tanaka, N.; Kakudo, M.; Wada, K.; Hase, T.; Matsubara, H. J. Biochem. 90, 1763-1773, 1981 A;Title: X-Ray analysis of a [2Fe-2S] ferredoxin from Spirulina platensis. Main chain fold and location of side chains at 2.5 angstroms resolution. A;Reference number: A44591; MUID:82142259 A;Note: X-ray crystallography, 2.5 angstroms R;Tsukihara, T.; Fukuyama, K.; Mizushima, M.; Harioka, T.; Kusunoki, M.; Katsube, Y.; Hase, T.; Matsubara, H. J. Mol. Biol. 216, 399-410, 1990 A;Title: Structure of the [2Fe-2S] ferredoxin I from the blue-green alga Aphanothece sacrum at 2.2 angstroms resolution. A;Reference number: A44586; MUID:91073403 A;Note: X-ray crystallography, 2.2 angstroms R;Meyer, J.; Fujinaga, J.; Gaillard, J.; Lutz, M. Biochemistry 33, 13642-13650, 1994 A;Title: Mutated forms of the [2Fe-2S] ferredoxin from Clostridium pasteurianum with noncysteinyl ligands to the iron-sulfur cluster. A;Reference number: A55988; MUID:95034798 A;Note: an atypical 2Fe-2S cluster; three of four ligands are determined C;Comment: See also RESID:AA0225. C;Sequence code: C, C, C, C A;Conditions: cross-link 4 C;Keywords: 2Fe-2S; iron-sulfur protein; metalloprotein F;/Binding site: 2Fe-2S cluster (Cys) (covalent) >TX;AA0138 tris-L-cysteinyl triiron trisulfide N;Systematic name: tri-mu-sulfidotris(S-cysteinyliron) C;Formula: C 9 H 12 Fe 3 N 3 O 3 S 6 A;Formula weight: #chem 570.15 #phys 569.7251 C;Correction formula: C 0 H -3 Fe 3 S 3 A;Correction weight: #chem 260.72 #phys 260.6976 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 11-Jun-1999 C;Comment: The three-iron three-sulfur cluster is now thought not to exist except possibly as an intermediate form. See RESID:AA0139 and RESID:AA0140. C;Sequence code: C, C, C A;Conditions: cross-link 3 C;Keywords: iron-sulfur protein; metalloprotein F;/Binding site: 3Fe-3S cluster (Cys) (covalent) >TX;AA0139 tris-L-cysteinyl triiron tetrasulfide N;Systematic name: mu3-sulfido-tri-mu-sulfidotris(S-cysteinyliron) C;Formula: C 9 H 12 Fe 3 N 3 O 3 S 7 A;Formula weight: #chem 602.22 #phys 601.6972 C;Correction formula: C 0 H -3 Fe 3 S 4 A;Correction weight: #chem 292.78 #phys 292.6696 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 11-Jun-1999 R;Howard, J.B.; Lorsbach, T.W.; Ghosh, D.; Melis, K.; Stout, C.D. J. Biol. Chem. 258, 508-522, 1983 A;Title: Structure of Azotobacter vinelandii 7Fe ferredoxin. Amino acid sequence and electron density maps of residues. A;Reference number: A00218; MUID:83082915 A;Note: X-ray crystallography, 2 angstroms; 3Fe-4S and 4Fe-4S clusters R;Stout, G.H.; Turley, S.; Sieker, L.C.; Jensen, L.H. Proc. Natl. Acad. Sci. U.S.A. 85, 1020-1022, 1988 A;Title: Structure of ferredoxin I from Azotobacter vinelandii. A;Reference number: JS0191; MUID:88124966 A;Note: X-ray crystallography, 2.6 angstroms; 3Fe-4S and 4Fe-4S clusters R;Kissinger, C.R.; Sieker, L.C.; Adman, E.T.; Jensen, L.H. J. Mol. Biol. 219, 693-715, 1991 A;Title: Refined crystal structure of ferredoxin II from Desulfovibrio gigas at 1.7 A. A;Reference number: S17118; MUID:91278096 A;Note: X-ray crystallography, 1.7 angstroms; 3Fe-4S cluster, disulfide and methyl mercaptan (see RESID:AA0101) R;Gorst, C.M.; Yeh, Y.H.; Teng, Q.; Calzolai, L.; Zhou, Z.H.; Adams, M.W.W.; La Mar, G.N. Biochemistry 34, 600-610, 1995 A;Title: [1]H NMR investigation of the paramagnetic cluster environment in Pyrococcus furiosus three-iron ferredoxin: sequence-specific assignment of ligated cysteines independent of tertiary structure. A;Reference number: A56250; MUID:95119047 A;Note: conformation, binding site, and disulfide bond assignments by (1)H-NMR; this ferredoxin can form a 4Fe-4S cluster but it readily converts to a stable 3Fe-4S cluster C;Comment: The activity of 3Fe-4S clusters has been questioned. Reconstitution to 4Fe-4S clusters may occur. See RESID:AA0140. C;Comment: Four cysteine ligands may denote uncertainty as to which set of three actually bind the cluster. C;Sequence code: C, C, C A;Conditions: cross-link 3 C;Keywords: 3Fe-4S; iron-sulfur protein; metalloprotein F;/Binding site: 3Fe-4S cluster (Cys) (covalent) >TX;AA0140 tetrakis-L-cysteinyl tetrairon tetrasulfide N;Systematic name: tetra-mu3-sulfidotetrakis(S-cysteinyliron) C;Formula: C 12 H 16 Fe 4 N 4 O 4 S 8 A;Formula weight: #chem 760.20 #phys 759.6335 C;Correction formula: C 0 H -4 Fe 4 S 4 A;Correction weight: #chem 347.62 #phys 347.5967 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 11-Jun-1999 R;Adman, E.T.; Sieker, L.C.; Jensen, L.H. J. Biol. Chem. 251, 3801-3806, 1976 A;Title: Structure of Peptococcus aerogenes ferredoxin. Refinement at 2 angstroms resolution. A;Reference number: A92192; MUID:76213238 A;Note: X-ray crystallography, 2.0 angstroms; monomer with two 4Fe-4S clusters R;Backes, G.; Mino, Y.; Loehr, T.M.; Meyer, T.E.; Cusanovich, M.A.; Sweeney, W.V.; Adman, E.T.; Sanders-Loehr, J. J. Am. Chem. Soc. 113, 2055-2064, 1991 A;Title: The environment of Fe4S4 clusters in ferredoxins and high-potential iron proteins. New information from x-ray crystallography and resonance Raman spectroscopy. A;Reference number: A44688 A;Note: X-ray crystallography, 2.0 angstroms; Raman spectroscopy; monomer with two 4Fe-4S clusters compared with HiPIP type R;Huber, J.G.; Gaillard, J.; Moulis, J.M. Biochemistry 34, 194-205, 1995 A;Title: NMR of Chromatium vinosum ferredoxin: evidence for structural inequivalence and impeded electron transfer between the two [4Fe-4S] clusters. A;Reference number: A56076; MUID:95118987 A;Note: conformation by (1)H-NMR and (13)C-NMR; monomer with two 4Fe-4S clusters R;Sery, A.; Housset, D.; Serre, L.; Bonicel, J.; Hatchikian, C.; Frey, M.; Roth, M. Biochemistry 33, 15408-15417, 1994 A;Title: Crystal structure of the ferredoxin I from Desulfovibrio africanus at 2.3 angstrom resolution. A;Reference number: A56050; MUID:95101634 A;Note: X-ray crystallography, 2.3 angstroms; single 4Fe-4S cluster R;Fukuyama, K.; Nagahara, Y.; Tsukihara, T.; Katsube, Y.; Hase, T.; Matsubara, H. J. Mol. Biol. 199, 183-193, 1988 A;Title: Tertiary structure of Bacillus thermoproteolyticus [4Fe-4S] ferredoxin. Evolutionary implications for bacterial ferredoxins. A;Reference number: A55790; MUID:88172459 A;Note: X-ray crystallography, 2.3 angstroms; single 4Fe-4S cluster R;Georgiadis, M.M.; Komiya, H.; Chakrabarti, P.; Woo, D.; Kornuc, J.J.; Rees, D.C. Science 257, 1653-1659, 1992 A;Title: Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. A;Reference number: A43282; MUID:92410322 A;Note: X-ray crystallography, 2.9 angstroms; dimer sharing one 4Fe-4S cluster R;Kim, J.; Rees, D.C. Science 257, 1677-1682, 1992 A;Title: Structural models for the metal centers in the nitrogenase molybdenum-iron protein. A;Reference number: A49884; MUID:92410323 A;Note: X-ray crystallography, 2.7 angstroms; two 4Fe-4S cluster shared between two different subunits C;Comment: Several different types of 4Fe-4S cluster are observed. Typically two 4Fe-4S clusters are shared in a single domain. Also observed are: one 4Fe-4S cluster and one 3Fe-4S cluster (see RESID:AA0139) in a single domain, a single 4Fe-4S cluster, one 4Fe-4S cluster shared between dimeric partners, and two 4Fe-4S clusters shared between two different chains. C;Comment: Three cysteine ligands may denote that the fourth iron is labile or that it binds another prosthetic group. C;Sequence code: C, C, C, C A;Conditions: cross-link 4 C;Keywords: 4Fe-4S; iron-sulfur protein; metalloprotein F;/Binding site: 4Fe-4S cluster (Cys) (covalent) >TX;AA0141 L-cysteinyl homocitryl molybdenum-heptairon-nonasulfide N;Alternate names: nitrogenase iron-molybdenum cofactor A;Cross-references: CAS:72994-52-6 C;Formula: C 10 H 12 Fe 7 Mo 1 N 1 O 8 S 10 A;Formula weight: #chem 1081.74 #phys 1083.2270 C;Correction formula: C 7 H 7 Fe 7 Mo 1 O 7 S 9 A;Correction weight: #chem 978.59 #phys 980.2178 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 11-Jun-1999 R;Kim, J.; Rees, D.C. Science 257, 1677-1682, 1992 A;Title: Structural models for the metal centers in the nitrogenase molybdenum-iron protein. A;Reference number: A49884; MUID:92410323 R;Kim, J.; Rees, D.C. Nature 360, 553-560, 1992 A;Title: Crystallographic structure and functional implications of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii. A;Reference number: A49883 R;Ma, L.; Gavini, N.; Liu, H.I.; Hedman, B.; Hodgson, K.O.; Burgess, B.K. J. Biol. Chem. 269, 18007-18015, 1994 A;Title: Large scale isolation and characterization of the molybdenum-iron cluster from nitrogenase. A;Reference number: A44635; MUID:94299515 A;Note: EPR and X-ray absorption spectrographic analysis C;Comment: The cysteine binds one iron of a 4Fe-3S cluster; the other three irons are connected by two mu-sulfides and one other mu-ligand, either sulfur or dinitrogen, to three irons of a Mo-3Fe-3S cluster; the molybdenum is further bound by the 2-oxide and 2-carboxylate of homocitrate (2-hydroxy-1,2,4-butanetricarboxylic acid) and coordinated by a histidine. C;Sequence code: C C;Keywords: molybdenum; iron-sulfur protein; metalloprotein F;/Binding site: homocitryl Mo-7Fe-8S cluster (Cys) (covalent) >TX;AA0142 L-cysteinyl molybdopterin N;Alternate names: cysteinyl Mo-pterin; molybdoenzyme molybdenum cofactor N;Systematic name: 8-amino-2-(2-amino-2-carboxyethyl)thio-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 A;Cross-references: CAS:73508-07-3 C;Formula: C 13 H 16 Mo 1 N 6 O 9 P 1 S 3 A;Formula weight: #chem 623.42 #phys 624.8933 C;Correction formula: C 10 H 11 Mo 1 N 5 O 8 P 1 S 2 A;Correction weight: #chem 520.27 #phys 521.8841 C;Date: 31-Mar-1995 #structure_revision 27-Feb-1998 #text_change 18-Feb-2000 R;Kisker, C.; Schindelin, H.; Pacheco, A.; Wehbi, W.A.; Garrett, R.M.; Rajagopalan, K.V.; Enemark, J.H.; Rees, D.C. Cell 91, 973-983, 1997 A;Title: Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. A;Reference number: A58730; MUID:98088796 R;Chan, M.K.; Mukund, S.; Kletzin, A.; Adams, M.W.W.; Rees, D.C. Science 267, 1463-1469, 1995 A;Title: Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. A;Reference number: A55958; MUID:95184006 C;Comment: A hydrogenated (+4H) structure is shown. The fully oxidized form would be the corresponding 4,9,10-trihydro form. C;Sequence code: C C;Keywords: metalloprotein; molybdenum; molybdopterin; phosphoprotein F;/Binding site: molybdopterin (Cys) (covalent) >TX;AA0143 S-(8alpha-FAD)-L-cysteine N;Alternate names: 8alpha-(S-cysteinyl)FAD N;Systematic name: (R)-2-amino-3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]thiopropanoic acid C;Formula: C 30 H 36 N 10 O 16 P 2 S 1 A;Formula weight: #chem 886.69 #phys 886.1507 C;Correction formula: C 27 H 31 N 9 O 15 P 2 A;Correction weight: #chem 783.55 #phys 783.1415 C;Date: 01-Sep-1995 #structure_revision 01-Sep-1995 #text_change 14-May-1999 R;Wagner, M.A.; Khanna, P.; Jorns, M.S. Biochemistry 38, 5588-5595, 1999 A;Title: Structure of the flavocoenzyme of two homologous amine oxidases: monomeric sarcosine oxidase and N-methyltryptophan oxidase. A;Reference number: A58959; MUID:99238335 A;Note: mass spectrographic and chemical characterization C;Comment: The arrangement of the attachment has not been completely established in some cases. C;Sequence code: C C;Keywords: FAD; flavoprotein; phosphoprotein F;/Modified site: S-(8alpha-FAD)-cysteine (Cys) F;/Modified site: FAD-cysteine (Cys) >TX;AA0144 3'-(8alpha-FAD)-L-histidine N;Alternate names: tau-(8alpha-FAD)-histidine; tele-(8alpha-FAD)-histidine; 8alpha-(N(3)-histidyl)FAD N;Systematic name: (S)-2-amino-3-(3-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid C;Formula: C 33 H 38 N 12 O 16 P 2 A;Formula weight: #chem 920.69 #phys 920.2004 C;Correction formula: C 27 H 31 N 9 O 15 P 2 A;Correction weight: #chem 783.55 #phys 783.1415 C;Date: 31-Mar-1995 #structure_revision 01-Sep-1995 #text_change 09-Apr-1999 R;Pinto, J.T.; Frisell, W.R. Arch. Biochem. Biophys. 169, 483-491, 1975 A;Title: Characterization of the peptide-bound flavin of a bacterial sarcosine dehydrogenase. A;Reference number: A61419; MUID:76038634 A;Note: chemical and spectrographic characterization C;Comment: The arrangement of the attachment has not been completely established in some cases. C;Sequence code: H C;Keywords: FAD; flavoprotein; phosphoprotein F;/Modified site: 3'-FAD-histidine (His) F;/Modified site: FAD-histidine (His) >TX;AA0145 O4'-(8alpha-FAD)-L-tyrosine N;Alternate names: 8alpha-(O4'-tyrosyl)FAD N;Systematic name: (S)-2-amino-3-(4-[8alpha-riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]oxyphenyl)propanoic acid C;Formula: C 36 H 40 N 10 O 17 P 2 A;Formula weight: #chem 946.72 #phys 946.2048 C;Correction formula: C 27 H 31 N 9 O 15 P 2 A;Correction weight: #chem 783.55 #phys 783.1415 C;Date: 01-Sep-1995 #structure_revision 01-Sep-1995 #text_change 09-Apr-1999 R;McIntire, W.; Edmondson, D.E.; Singer, T.P.; Hopper, D.J. J. Biol. Chem. 255, 6553-6555, 1980 A;Title: 8alpha-O-tyrosyl-FAD: a new form of covalently bound flavin from p-cresol methylhydroxylase. A;Reference number: A44734; MUID:80227800 A;Note: chemical and spectrographic characterization C;Sequence code: Y C;Keywords: FAD; flavoprotein; phosphoprotein F;/Modified site: O4'-FAD-tyrosine (Tyr) >TX;AA0146 L-3',4'-dihydroxyphenylalanine N;Alternate names: L-DOPA; levodopa; L-3'-hydroxytyrosine N;Systematic name: (S)-2-amino-3-(3,4-dihydroxyphenyl)propanoic acid A;Cross-references: CAS:59-92-7 C;Formula: C 9 H 9 N 1 O 3 A;Formula weight: #chem 179.18 #phys 179.0582 C;Correction formula: C 0 H 0 O 1 A;Correction weight: #chem 16.00 #phys 15.9949 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Waite, J.H. J. Comp. Physiol. B 156, 491-496, 1986 A;Title: Mussel glue from Mytilus californianus Conrad: a comparative study. A;Reference number: A61093; MUID:86279063 R;Waite, J.H.; Jensen, R.A.; Morse, D.E. Biochemistry 31, 5733-5738, 1992 A;Title: Cement precursor proteins of the reef-building polychaete Phragmatopoma californica (Fewkes). A;Reference number: A42627; MUID:92304953 R;Waite, J.H. Anal. Biochem. 192, 429-433, 1991 A;Title: Detection of peptidyl-3,4-dihydroxyphenylalanine by amino acid analysis and microsequencing techniques. A;Reference number: A59161; MUID:91241559 A;Note: chromatographic identification; PTH derivative C;Sequence code: Y F;/Modified site: 3',4'-dihydroxyphenylalanine (Tyr) >TX;AA0147 L-2',4',5'-topaquinone N;Alternate names: L-2,4,5-TOPAquinone; TPQ N;Systematic name: (S)-2-amino-3-(5-hydroxy-2,5-cyclohexadien-1,4-dion-2-yl)propanoic acid C;Formula: C 9 H 7 N 1 O 4 A;Formula weight: #chem 193.16 #phys 193.0375 C;Correction formula: C 0 H -2 O 2 A;Correction weight: #chem 29.98 #phys 29.9742 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Janes, S.M.; Mu, D.; Wemmer, D.; Smith, A.J.; Kaur, S.; Maltby, D.; Burlingame, A.L.; Klinman, J.P. Science 248, 981-987, 1990 A;Title: A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase. A;Reference number: A48242; MUID:90260648 R;Mu, D.; Janes, S.M.; Smith, A.J.; Brown, D.E.; Dooley, D.M.; Klinman, J.P. J. Biol. Chem. 267, 7979-7982, 1992 A;Title: Tyrosine codon corresponds to topa quinone at the active site of copper amine oxidases. A;Reference number: A38081; MUID:92235001 R;Janes, S.M.; Palcic, M.M.; Scaman, C.H.; Smith, A.J.; Brown, D.E.; Dooley, D.M.; Mure, M.; Klinman, J.P. Biochemistry 31, 12147-12154, 1992 A;Title: Identification of topaquinone and its consensus sequence in copper amine oxidases. A;Reference number: A44239; MUID:93090748 C;Sequence code: Y C;Keywords: quinoprotein; topaquinone F;/Modified site: topaquinone (Tyr) >TX;AA0148 L-tryptophyl quinone N;Systematic name: (S)-3-(2-amino-2-carboxyethyl)-6,7-indolinedione C;Formula: C 11 H 8 N 2 O 3 A;Formula weight: #chem 216.20 #phys 216.0535 C;Correction formula: C 0 H -2 O 2 A;Correction weight: #chem 29.98 #phys 29.9742 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;McIntire, W.S.; Wemmer, D.E.; Chistoserdov, A.; Lidstrom, M.E. Science 252, 817-824, 1991 A;Title: A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase. A;Reference number: A48240; MUID:91227905 C;Sequence code: W A;Conditions: incidental to RESID:AA0149 C;Keywords: quinoprotein F;/Modified site: tryptophyl quinone (Trp) >TX;AA0149 4'-(L-tryptophan)-L-tryptophyl quinone N;Alternate names: TTQ N;Systematic name: (S,S)-3-(2-amino-2-carboxyethyl)-4-[3-(2-amino-2-carboxyethyl)-1H-indol-2-yl]-6,7-indolinedione A;Cross-references: CAS:134645-25-3 C;Formula: C 22 H 16 N 4 O 4 A;Formula weight: #chem 400.40 #phys 400.1172 C;Correction formula: C 0 H -4 O 2 A;Correction weight: #chem 27.97 #phys 27.9585 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;McIntire, W.S.; Wemmer, D.E.; Chistoserdov, A.; Lidstrom, M.E. Science 252, 817-824, 1991 A;Title: A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase. A;Reference number: A48240; MUID:91227905 C;Sequence code: W, W A;Conditions: cross-link 2; secondary to RESID:AA0148 C;Keywords: quinoprotein F;/Cross-link: tryptophan-tryptophyl quinone (Trp-Trp) >TX;AA0150 O-phosphopantetheine-L-serine N;Systematic name: (2R)-4-((2S)-2-amino-2-carboxyethyl)phosphonato-2-hydroxy-N-[3-(2-mercaptoethyl)amino-3-oxopropyl]-3,3-dimethylbutanamide C;Formula: C 14 H 26 N 3 O 8 P 1 S 1 A;Formula weight: #chem 427.42 #phys 427.1178 C;Correction formula: C 11 H 21 N 2 O 6 P 1 S 1 A;Correction weight: #chem 340.34 #phys 340.0858 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 18-Feb-2000 R;Ehmann, D.E.; Gehring, A.M.; Walsh, C.T. Biochemistry 38, 6171-6177, 1999 A;Title: Lysine biosynthesis in Saccharomyces cerevisiae: mechanism of alpha-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5. A;Reference number: A58964; MUID:99255373 C;Sequence code: S A;Conditions: combinable C;Keywords: phosphopantetheine; phosphoprotein F;/Binding site: phosphopantetheine (Ser) (covalent) >TX;AA0151 N4-glycosyl-L-asparagine C;Formula: C 4 H 6 N 2 O 2 + A;Formula weight: #chem 114.10 + #phys 114.0429 + C;Correction formula: C 0 H 0 + A;Correction weight: #chem 0.00 + #phys 0.0000 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Hunt, L.T.; Dayhoff, M.O. Biochem. Biophys. Res. Commun. 39, 757-765, 1970 A;Title: The occurrence in proteins of the tripeptides Asn-X-Ser and Asn-X-Thr and of bound carbohydrate. A;Reference number: A02589; MUID:71065057 A;Note: recognition of glycosylation motif R;Miletich, J.P.; Broze Jr., G.J. J. Biol. Chem. 265, 11397-11404, 1990 A;Title: Beta protein C is not glycosylated at asparagine 329. The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites. A;Reference number: A44605; MUID:90293094 A;Note: partial modification at N-X-C motif R;Shibata, S.; Takeda, T.; Natori, Y. J. Biol. Chem. 263, 12483-12485, 1988 A;Title: The structure of nephritogenoside. A nephritogenic glycopeptide with alpha-N-glycosidic linkage. A;Reference number: A60696; MUID:88315043 A;Note: glycopeptide with trisaccharide N-acetyl-glucosamine attached by an alpha-N-glycosidic linkage, and the N-X-[ST] motif is not present C;Comment: The most common form is N-acetylglucosaminyl asparagine. N-acetylgalactosaminyl asparagine also occurs. C;Comment: This modification typically occurs in extracellar peptides with an N-X-[ST] motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position. Secondary structure features are important, and proline in the second or fourth positions inhibits modification. C;Sequence code: N A;Conditions: combinable C;Keywords: glycoprotein F;/Binding site: carbohydrate (Asn) (covalent) >TX;AA0152 S-glycosyl-L-cysteine C;Formula: C 3 H 5 N 1 O 1 S 1 + A;Formula weight: #chem 103.15 + #phys 103.0092 + C;Correction formula: C 0 H 0 + A;Correction weight: #chem 0.00 + #phys 0.0000 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Weiss, J.B.; Lote, C.J.; Bobinski, H. Nature New Biol. 234, 25-26, 1971 A;Title: New low molecular weight glycopeptide containing triglucosylcysteine in human erythrocyte membrane. A;Reference number: A03187; MUID:72034940 A;Note: chromatographic detection and chemical characterization; S-glucosylcysteine R;Lote, C.J.; Weiss, J.B. FEBS Lett. 16, 81-85, 1971 A;Title: Identification of digalactosylcysteine in a glycopeptide isolated from urine by a new preparative technique. A;Reference number: A44716 A;Note: chromatographic detection and chemical characterization; S-galactosylcysteine C;Comment: The beta form is shown. C;Sequence code: C A;Conditions: combinable C;Keywords: glycoprotein F;/Binding site: carbohydrate (Cys) (covalent) >TX;AA0153 O5-glycosyl-L-hydroxylysine C;Formula: C 6 H 12 N 2 O 2 + A;Formula weight: #chem 144.17 + #phys 144.0899 + C;Correction formula: C 0 H 0 + A;Correction weight: #chem 0.00 + #phys 0.0000 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Morgan, P.H.; Jacobs, H.G.; Segrest, J.P.; Cunningham, L.W. J. Biol. Chem. 245, 5042-5048, 1970 A;Title: Comparative study of glycopeptides derived from selected vertebrate collagens. A possible role of the carbohydrate in fibril formation. A;Reference number: A92069; MUID:71001508 A;Note: attachment of 2-O-alpha-D-glucosyl-O-beta-D-galactose to 5-hydroxylysine C;Comment: The most common form is galactosyl hydroxylysine. See 5-hydroxy-L-lysine (RESID:AA0028). C;Sequence code: K A;Conditions: combinable; secondary to RESID:AA0028 C;Keywords: glycoprotein F;/Binding site: carbohydrate (Lys) (covalent) >TX;AA0154 O-glycosyl-L-serine N;Alternate names: O3-glycosyl-L-serine C;Formula: C 3 H 5 N 1 O 2 + A;Formula weight: #chem 87.08 + #phys 87.0320 + C;Correction formula: C 0 H 0 + A;Correction weight: #chem 0.00 + #phys 0.0000 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 14-Jul-2000 R;Hansen, J.E.; Lund, O.; Engelbrecht, J.; Bohr, H.; Nielsen, J.O.; Hansen, J.E.S.; Brunak, S. Biochem. J. 308, 801-813, 1995 A;Title: Prediction of O-glycosylation of mammalian proteins: specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. A;Reference number: A57787; MUID:97104278 A;Note: prediction using neural network C;Comment: The most common forms are N-acetylgalactosaminyl, mannosyl, galactosyl, and xylosyl serine. C;Sequence code: S A;Conditions: combinable C;Keywords: glycoprotein F;/Binding site: carbohydrate (Ser) (covalent) >TX;AA0155 O-glycosyl-L-threonine N;Alternate names: O3-glycosyl-L-threonine C;Formula: C 4 H 7 N 1 O 2 + A;Formula weight: #chem 101.11 + #phys 101.0477 + C;Correction formula: C 0 H 0 + A;Correction weight: #chem 0.00 + #phys 0.0000 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 14-Jul-2000 R;Hansen, J.E.; Lund, O.; Engelbrecht, J.; Bohr, H.; Nielsen, J.O.; Hansen, J.E.S.; Brunak, S. Biochem. J. 308, 801-813, 1995 A;Title: Prediction of O-glycosylation of mammalian proteins: specificity patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase. A;Reference number: A57787; MUID:97104278 A;Note: prediction using neural network R;Nakakura, N.; Hietter, H.; van Dorsselaer, A.; Luu, B. Eur. J. Biochem. 204, 147-153, 1992 A;Title: Isolation and structural determination of three peptides from the insect Locusta migratoria. Identification of a deoxyhexose-linked peptide. A;Reference number: S23074; MUID:92155197 A;Note: chromatographic and mass spectrographic identification of fucosyl threonine C;Comment: The most common forms are N-acetylgalactosaminyl, mannosyl, and galactosyl threonine. C;Sequence code: T A;Conditions: combinable C;Keywords: glycoprotein F;/Binding site: carbohydrate (Thr) (covalent) >TX;AA0156 1'-glycosyl-L-tryptophan C;Formula: C 11 H 10 N 2 O 1 + A;Formula weight: #chem 186.22 + #phys 186.0793 + C;Correction formula: C 0 H 0 + A;Correction weight: #chem 0.00 + #phys 0.0000 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Gaede, G.; Kellner, R.; Rinehart, K.L.; Proefke, M.L. Biochem. Biophys. Res. Commun. 189, 1303-1309, 1992 A;Title: A tryptophan-substituted member of the AKH/RPCH family isolated from a stick insect corpus cardiacum. A;Reference number: JC1416; MUID:93129188 C;Comment: It is uncertain whether this is an N-glycoside linkage (as indicated), and which particular hexose is involved. C;Sequence code: W C;Keywords: glycoprotein F;/Binding site: carbohydrate (Trp) (covalent) >TX;AA0157 O4'-glycosyl-L-tyrosine C;Formula: C 9 H 9 N 1 O 2 + A;Formula weight: #chem 163.18 + #phys 163.0633 + C;Correction formula: C 0 H 0 + A;Correction weight: #chem 0.00 + #phys 0.0000 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Smythe, C.; Caudwell, F.B.; Ferguson, M.; Cohen, P. EMBO J. 7, 2681-2686, 1988 A;Title: Isolation and structural analysis of a peptide containing the novel tyrosyl-glucose linkage in glycogenin. A;Reference number: A44569; MUID:89030631 A;Note: mass spectrographic and linkage analysis C;Comment: The carbohydrate is glucose, the origin for glycogen. C;Sequence code: Y A;Conditions: combinable C;Keywords: glycoprotein F;/Binding site: carbohydrate (Tyr) (covalent) >TX;AA0158 N-asparaginyl-glycosylphosphatidylinositolethanolamine C;Formula: C 6 H 13 N 3 O 6 P 1 + A;Formula weight: #chem 254.16 + #phys 254.0542 + C;Correction formula: C 2 H 6 N 1 O 3 P 1 + A;Correction weight: #chem 123.05 + #phys 123.0085 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Nuoffer, C.; Jenoe, P.; Conzelmann, A.; Riezman, H. Mol. Cell. Biol. 11, 27-37, 1991 A;Title: Determinants for glycophospholipid anchoring of the Saccharomyces cerevisiae GAS1 protein to the plasma membrane. A;Reference number: A39663; MUID:91094841 R;Sugita, Y.; Nakano, Y.; Oda, E.; Noda, K.; Tobe, T.; Miura, N.H.; Tomita, M. J. Biochem. 114, 473-477, 1993 A;Title: Determination of carboxyl-terminal residue and disulfide bonds of MACIF(CD59), a glycosyl-phosphatidylinositol-anchored membrane protein. A;Reference number: PX0068; MUID:94103166 C;Sequence code: N A;Conditions: carboxyl-terminal C;Keywords: blocked carboxyl end; glycoprotein; lipoprotein; phosphatidylinositol linkage; phosphoprotein F;/Modified site: GPI-anchor ethanolamine amidated carboxyl end (Asn) F;/Modified site: GPI-anchor ethanolamine amidated carboxyl end (Asn) (in mature form) >TX;AA0159 N-aspartyl-glycosylphosphatidylinositolethanolamine C;Formula: C 6 H 12 N 2 O 7 P 1 + A;Formula weight: #chem 255.15 + #phys 255.0382 + C;Correction formula: C 2 H 6 N 1 O 3 P 1 + A;Correction weight: #chem 123.05 + #phys 123.0085 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Allen, G.; Gurnett, L.P.; Cross, G.A.M. J. Mol. Biol. 157, 527-546, 1982 A;Title: Complete amino acid sequence of a variant surface glycoprotein (VSG 117) from Trypanosoma brucei. A;Reference number: A92882; MUID:83010277 C;Sequence code: D A;Conditions: carboxyl-terminal C;Keywords: blocked carboxyl end; glycoprotein; lipoprotein; phosphatidylinositol linkage; phosphoprotein F;/Modified site: GPI-anchor ethanolamine amidated carboxyl end (Asp) F;/Modified site: GPI-anchor ethanolamine amidated carboxyl end (Asp) (in mature form) >TX;AA0160 N-cysteinyl-glycosylphosphatidylinositolethanolamine C;Formula: C 5 H 12 N 2 O 5 P 1 S 1 + A;Formula weight: #chem 243.20 + #phys 243.0205 + C;Correction formula: C 2 H 6 N 1 O 3 P 1 + A;Correction weight: #chem 123.05 + #phys 123.0085 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Homans, S.W.; Ferguson, M.A.J.; Dwek, R.A.; Rademacher, T.W.; Anand, R.; Williams, A.F. Nature 333, 269-272, 1988 A;Title: Complete structure of the glycosyl phosphatidylinositol membrane anchor of rat brain Thy-1 glycoprotein. A;Reference number: A43057; MUID:88216819 C;Sequence code: C A;Conditions: carboxyl-terminal C;Keywords: blocked carboxyl end; glycoprotein; lipoprotein; phosphatidylinositol linkage; phosphoprotein F;/Modified site: GPI-anchor ethanolamine amidated carboxyl end (Cys) F;/Modified site: GPI-anchor ethanolamine amidated carboxyl end (Cys) (in mature form) >TX;AA0161 N-glycyl-glycosylphosphatidylinositolethanolamine C;Formula: C 4 H 10 N 2 O 5 P 1 + A;Formula weight: #chem 197.11 + #phys 197.0327 + C;Correction formula: C 2 H 6 N 1 O 3 P 1 + A;Correction weight: #chem 123.05 + #phys 123.0085 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Hefta, S.A.; Paxton, R.J.; Shively, J.E. J. Biol. Chem. 265, 8618-8626, 1990 A;Title: Sequence and glycosylation site identity of two distinct glycoforms of nonspecific cross-reacting antigen as demonstrated by sequence analysis and fast atom bombardment mass spectrometry. A;Reference number: A36271; MUID:90256782 C;Sequence code: G A;Conditions: carboxyl-terminal C;Keywords: blocked carboxyl end; glycoprotein; lipoprotein; phosphatidylinositol linkage; phosphoprotein F;/Modified site: GPI-anchor ethanolamine amidated carboxyl end (Gly) F;/Modified site: GPI-anchor ethanolamine amidated carboxyl end (Gly) (in mature form) >TX;AA0162 N-seryl-glycosylphosphatidylinositolethanolamine C;Formula: C 5 H 12 N 2 O 6 P 1 + A;Formula weight: #chem 227.14 + #phys 227.0433 + C;Correction formula: C 2 H 6 N 1 O 3 P 1 + A;Correction weight: #chem 123.05 + #phys 123.0085 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 21-Jan-2000 R;Zhu, X.L.; Sly, W.S. J. Biol. Chem. 265, 8795-8801, 1990 A;Title: Carbonic anhydrase IV from human lung. Purification, characterization, and comparison with membrane carbonic anhydrase from human kidney. A;Reference number: A36280; MUID:90256808 A;Note: evidence for glycosyl phosphatidylinositol anchor R;Stahl, N.; Baldwin, M.A.; Teplow, D.B.; Hood, L.; Gibson, B.W.; Burlingame, A.L.; Prusiner, S.B. Biochemistry 32, 1991-2002, 1993 A;Title: Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. A;Reference number: A40665; MUID:93192259 A;Note: mass spectrographic and chemical characterization C;Sequence code: S A;Conditions: carboxyl-terminal C;Keywords: blocked carboxyl end; glycoprotein; lipoprotein; phosphatidylinositol linkage; phosphoprotein F;/Modified site: GPI-anchor ethanolamine amidated carboxyl end (Ser) F;/Modified site: GPI-anchor ethanolamine amidated carboxyl end (Ser) (in mature form) >TX;AA0163 N-alanyl-glycosylphosphatidylinositolethanolamine C;Formula: C 5 H 12 N 2 O 5 P 1 + A;Formula weight: #chem 211.14 + #phys 211.0484 + C;Correction formula: C 2 H 6 N 1 O 3 P 1 + A;Correction weight: #chem 123.05 + #phys 123.0085 + C;Date: 28-Jan-2000 #structure_revision 28-Jan-1995 #text_change 28-Jan-2000 R;Moy, P.; Lobb, R.; Tizard, R.; Olson, D.; Hession, C. J. Biol. Chem. 268, 8835-8841, 1993 A;Title: Cloning of an inflammation-specific phosphatidyl inositol-linked form of murine vascular cell adhesion molecule-1. A;Reference number: A46052; MUID:93232042 A;Note: predicted cleavage site C;Sequence code: A A;Conditions: carboxyl-terminal C;Keywords: blocked carboxyl end; glycoprotein; lipoprotein; phosphatidylinositol linkage; phosphoprotein F;/Modified site: GPI-anchor ethanolamine amidated carboxyl end (Ala) F;/Modified site: GPI-anchor ethanolamine amidated carboxyl end (Ala) (in mature form) >TX;AA0166 N-seryl-glycosylsphingolipidinositolethanolamine C;Formula: C 5 H 12 N 2 O 6 P 1 + A;Formula weight: #chem 227.14 + #phys 227.0433 + C;Correction formula: C 2 H 6 N 1 O 3 P 1 + A;Correction weight: #chem 123.05 + #phys 123.0085 + C;Date: 09-Aug-1995 #structure_revision 09-Aug-1995 #text_change 21-Jan-2000 R;Stadler, J.; Keenan, T.W.; Bauer, G.; Gerisch, G. EMBO J. 8, 371-377, 1989 A;Title: The contact site A glycoprotein of Dictyostelium discoideum carries a phospholipid anchor of a novel type. A;Reference number: A56857; MUID:89251561 A;Note: partial chemical characterization R;Saito, T.; Ochiai, H. Eur. J. Biochem. 218, 623-628, 1993 A;Title: Evidence for a glycolipid anchor of gp64, a putative cell-cell adhesion protein of Polysphondylium pallidum. A;Reference number: A44728; MUID:94094856 A;Note: mass spectrographic and chemical characterization C;Sequence code: S A;Conditions: carboxyl-terminal C;Keywords: blocked carboxyl end; glycoprotein; lipoprotein; sphingolipidinositol linkage; phosphoprotein F;/Modified site: GSI-anchor ethanolamine amidated carboxyl end (Ser) F;/Modified site: GSI-anchor ethanolamine amidated carboxyl end (Ser) (in mature form) >TX;AA0167 O-(phosphoribosyl dephospho-coenzyme A)-L-serine N;Alternate names: O3-(phosphate-5-ribosyl-alpha-2-adenosine-5-diphosphate pantetheine)-L-serine C;Formula: C 29 H 47 N 8 O 21 P 3 S 1 A;Formula weight: #chem 968.73 #phys 968.1789 C;Correction formula: C 26 H 42 N 7 O 19 P 3 S 1 A;Correction weight: #chem 881.65 #phys 881.1469 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Dimroth, P. Eur. J. Biochem. 64, 269-281, 1976 A;Title: The prosthetic group of citrate-lyase acyl-carrier protein. A;Reference number: A48847; MUID:76210214 A;Note: chemical characterization R;Robinson Jr., J.B.; Singh, M.; Srere, P.A. Proc. Natl. Acad. Sci. U.S.A. 73, 1872-1876, 1976 A;Title: Structure of the prosthetic group of Klebsiella aerogenes citrate (pro-3S)-lyase. A;Reference number: A44634; MUID:76222714 A;Note: chemical characterization C;Comment: It is uncertain whether the phosphoribosyl glycosidic attachment to the dephospho coenzyme A is alpha or beta, and through the 2' or the 3' position. It is shown as an alpha 1->2 linkage. C;Sequence code: S A;Conditions: combinable C;Keywords: coenzyme A; phosphoprotein; F;/Binding site: phosphoribosyl dephospho-coenzyme A (Ser) (covalent) >TX;AA0168 omega-N-(ADP-ribosyl)-L-arginine N;Alternate names: N(omega)-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-arginine; N(omega)-alpha-D-ribofuranosyl-L-arginine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) N;Systematic name: (S)-2-amino-5-([imino([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)methyl]amino)pentanoic acid A;Cross-references: CAS:71388-78-8 C;Formula: C 21 H 33 N 9 O 14 P 2 A;Formula weight: #chem 697.50 #phys 697.1622 C;Correction formula: C 15 H 21 N 5 O 13 P 2 A;Correction weight: #chem 541.31 #phys 541.0611 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Oppenheimer, N.J. J. Biol. Chem. 253, 4907-4910, 1978 A;Title: Structural determination and stereospecificity of the choleragen-catalyzed reaction of NAD+ with guanidines. A;Reference number: A44552; MUID:78218136 A;Note: mass spectrographic and (1)H-NMR characterization; chemical synthesis R;Van Dop, C.; Tsubokawa, M.; Bourne, H.R.; Ramachandran, J. J. Biol. Chem. 259, 696-698, 1984 A;Title: Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin. A;Reference number: A61290; MUID:84111542 A;Note: mass spectrographic analysis R;Pope, M.R.; Murrell, S.A.; Ludden, P.W. Proc. Natl. Acad. Sci. U.S.A. 82, 3173-3177, 1985 A;Title: Covalent modification of the iron protein of nitrogenase from Rhodospirillum rubrum by adenosine diphosphoribosylation of a specific arginine residue. A;Reference number: A61610 MUID:85216464 A;Note: mass spectrographic, (1)H-NMR and (31)P-NMR identification R;Pope, M.R.; Saari, L.L.; Ludden, P.W. J. Biol. Chem. 261, 10104-10111, 1986 A;Title: N-glycohydrolysis of adenosine diphosphoribosyl arginine linkages by dinitrogenase reductase activating glycohydrolase (activating enzyme) from Rhodospirillum rubrum. A;Reference number: A44687; MUID:86278057 A;Note: stereochemical characterization; ADP-ribosyl-nitrogenase hydrolase (EC 3.2.2.24) appears to remove only the alpha anomeric form C;Comment: Cholera toxin appears to catalyze formation of the alpha form which subsequently anomerizes to approximately equal concentrations of the alpha and beta forms. The alpha form is presented. C;Comment: The keyword "phosphoprotein" is not used with toxin modification. C;Generating enzyme: NAD(P)+--arginine ADP-ribosyltransferase (EC 2.4.2.31); NAD+--nitrogenase ADP-D-ribosyltransferase (EC 2.4.2.37) C;Sequence code: R C;Keywords: *phosphoprotein F;/Modified site: ADP-ribosylarginine (Arg) (by ...) >TX;AA0169 S-(ADP-ribosyl)-L-cysteine N;Alternate names: S-alpha-D-ribofuranosyl-L-cysteine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate); S-L-cysteine alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) N;Systematic name: (R)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]thio)propanoic acid C;Formula: C 18 H 26 N 6 O 14 P 2 S 1 A;Formula weight: #chem 644.45 #phys 644.0703 C;Correction formula: C 15 H 21 N 5 O 13 P 2 A;Correction weight: #chem 541.31 #phys 541.0611 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;West Jr., R.E.; Moss, J.; Vaughan, M.; Liu, T.; Liu, T.Y. J. Biol. Chem. 260, 14428-14430, 1985 A;Title: Pertussis toxin-catalyzed ADP-ribosylation of transducin. Cysteine 347 is the ADP-ribose acceptor site. A;Reference number: A61415; MUID:86033942 A;Note: radiolabeling; chromatographic separation C;Comment: The anomeric form of the pertussis toxin product has not been characterized; the alpha form is presented. C;Comment: The keyword "phosphoprotein" is not used with toxin modification. C;Generating enzyme: NAD(P)+--cysteine ADP-ribosyltransferase (EC 2.4.2.-) C;Sequence code: C C;Keywords: *phosphoprotein F;/Modified site: ADP-ribosylcysteine (Cys) (by ...) >TX;AA0170 L-glutamyl 5-glycerylphosphorylethanolamine N;Systematic name: (S)-2-amino-5-[((2,3-dihydroxypropyl)phosphonato)ethyl]amino-5-oxopentanoic acid C;Formula: C 10 H 19 N 2 O 8 P 1 A;Formula weight: #chem 326.25 #phys 326.0879 C;Correction formula: C 5 H 12 N 1 O 5 P 1 A;Correction weight: #chem 197.13 #phys 197.0453 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 09-Apr-1999 R;Dever, T.E.; Costello, C.E.; Owens, C.L.; Rosenberry, T.L.; Merrick, W.C. J. Biol. Chem. 264, 20518-20525, 1989 A;Title: Location of seven post-translational modifications in rabbit elongation factor 1alpha including dimethyllysine, trimethyllysine, and glycerylphosphorylethanolamine. A;Reference number: A32684; MUID:90062188 A;Note: mass spectrographic and chemical characterization R;Whiteheart, S.W.; Shenbagamurthi, P.; Chen, L.; Cotter, R.J.; Hart, G.W. J. Biol. Chem. 264, 14334-14341, 1989 A;Title: Murine elongation factor 1alpha (EF-1alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1alpha. A;Reference number: A44784; MUID:89340549 A;Note: mass spectrographic and chemical characterization C;Comment: Glutamyl 5-glycerylphosphorylethanolamine appears to occur uniquely in translation elongation factor eEF-1 alpha chains. It is known to be a modification of glutamic acid. The stereochemistry of the glycerol phosphate has not been determined. The sn-3 form is shown. C;Sequence code: E A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: glycerylphosphorylethanolamine (Glu) (covalent) >TX;AA0171 S-sulfo-L-cysteine N;Alternate names: S3-sulfocysteine; cysteine sulfate thioester N;Systematic name: (R)-2-amino-3-(sulfothio)propanoic acid A;Cross-references: CAS:1637-71-4 C;Formula: C 3 H 5 N 1 O 4 S 2 A;Formula weight: #chem 183.21 #phys 182.9660 C;Correction formula: C 0 H 0 O 3 S 1 A;Correction weight: #chem 80.06 #phys 79.9568 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Ploegman, J.H.; Drent, G.; Kalk, K.H.; Hol, W.G.J.; Heinrikson, R.L.; Keim, P.; Weng, L.; Russell, J. Nature 273, 124-129, 1978 A;Title: The covalent and tertiary structure of bovine liver rhodanese. A;Reference number: A13902; MUID:78156434 A;Note: X-ray crystallography, 2.9 angstroms C;Sequence code: C C;Keywords: sulfoprotein F;/Active site: Cys (sulfocysteine intermediate) F;/Binding site: sulfate (Cys) (covalent) >TX;AA0172 O4'-sulfo-L-tyrosine N;Alternate names: O4-sulfotyrosine; tyrosine sulfate N;Systematic name: (S)-2-amino-3-(4-hydroxyphenyl)propanoic acid 4'-sulfate A;Cross-references: CAS:956-46-7 C;Formula: C 9 H 9 N 1 O 5 S 1 A;Formula weight: #chem 243.24 #phys 243.0201 C;Correction formula: C 0 H 0 O 3 S 1 A;Correction weight: #chem 80.06 #phys 79.9568 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Nachman, R.J.; Holman, G.M.; Cook, B.J.; Haddon, W.F.; Ling, N. Biochem. Biophys. Res. Commun. 140, 357-364, 1986 A;Title: Leucosulfakinin-II, a blocked sulfated insect neuropeptide with homology to cholecystokinin and gastrin. A;Reference number: A26335; MUID:87048769 A;Note: chromatographic detection; mass spectrographic identification; chemical synthesis C;Sequence code: Y A;Conditions: combinable C;Keywords: sulfoprotein F;/Binding site: sulfate (Tyr) (covalent) >TX;AA0173 L-bromohistidine C;Formula: C 6 H 6 Br 1 N 3 O 1 A;Formula weight: #chem 216.04 #phys 214.9694 C;Correction formula: C 0 H -1 Br 1 A;Correction weight: #chem 78.90 #phys 77.9105 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Takao, T.; Yoshino, K.; Suzuki, N.; Shimonishi, Y. Biomed. Environ. Mass Spectrom. 19, 705-712, 1990 A;Title: Analysis of post-translational modifications of proteins by accurate mass measurement in fast atom bombardment mass spectrometry. A;Reference number: A60973; MUID:91167743 A;Note: mass spectrographic identification C;Comment: The position of the bromine substitution is uncertain. The 2'-bromohistidine is shown. C;Sequence code: H C;Keywords: bromine F;/Modified site: bromohistidine (His) >TX;AA0174 L-2'-bromophenylalanine N;Systematic name: (S)-2-amino-3-(2-bromophenyl)propanoic acid A;Cross-references: CAS:42538-40-9 C;Formula: C 9 H 8 Br 1 N 1 O 1 A;Formula weight: #chem 226.07 #phys 224.9789 C;Correction formula: C 0 H -1 Br 1 A;Correction weight: #chem 78.90 #phys 77.9105 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Yoshino, K.; Takao, T.; Suhara, M.; Kitai, T.; Hori, H.; Nomura, K.; Yamaguchi, M.; Shimonishi, Y.; Suzuki, N. Biochemistry 30, 6203-6209, 1991 A;Title: Identification of a novel amino acid, o-bromo-L-phenylalanine, in egg-associated peptides that activate spermatozoa. A;Reference number: A39572; MUID:91283461 R;Takao, T.; Yoshino, K.; Suzuki, N.; Shimonishi, Y. Biomed. Environ. Mass Spectrom. 19, 705-712, 1990 A;Title: Analysis of post-translational modifications of proteins by accurate mass measurement in fast atom bombardment mass spectrometry. A;Reference number: A60973; MUID:91167743 A;Note: chromatographic and mass spectrographic identification; chemical synthesis C;Sequence code: F C;Keywords: bromine F;/Modified site: 2'-bromophenylalanine (Phe) >TX;AA0175 L-3'-bromophenylalanine N;Systematic name: (S)-2-amino-3-(3-bromophenyl)propanoic acid A;Cross-references: CAS:82311-69-1 C;Formula: C 9 H 8 Br 1 N 1 O 1 A;Formula weight: #chem 226.07 #phys 224.9789 C;Correction formula: C 0 H -1 Br 1 A;Correction weight: #chem 78.90 #phys 77.9105 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Takao, T.; Yoshino, K.; Suzuki, N.; Shimonishi, Y. Biomed. Environ. Mass Spectrom. 19, 705-712, 1990 A;Title: Analysis of post-translational modifications of proteins by accurate mass measurement in fast atom bombardment mass spectrometry. A;Reference number: A60973; MUID:91167743 A;Note: chemical synthesis C;Sequence code: F C;Keywords: bromine F;/Modified site: 3'-bromophenylalanine (Phe) >TX;AA0176 L-4'-bromophenylalanine N;Systematic name: (S)-2-amino-3-(4-bromophenyl)propanoic acid A;Cross-references: CAS:24250-84-8 C;Formula: C 9 H 8 Br 1 N 1 O 1 A;Formula weight: #chem 226.07 #phys 224.9789 C;Correction formula: C 0 H -1 Br 1 A;Correction weight: #chem 78.90 #phys 77.9105 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Takao, T.; Yoshino, K.; Suzuki, N.; Shimonishi, Y. Biomed. Environ. Mass Spectrom. 19, 705-712, 1990 A;Title: Analysis of post-translational modifications of proteins by accurate mass measurement in fast atom bombardment mass spectrometry. A;Reference number: A60973; MUID:91167743 A;Note: chemical synthesis C;Sequence code: F C;Keywords: bromine F;/Modified site: 4'-bromophenylalanine (Phe) >TX;AA0177 3',3'',5'-triiodo-L-thyronine N;Alternate names: liothyronine N;Systematic name: (S)-2-amino-3-[4-(4-hydroxy-3-iodophenoxy)-3,5-diiodophenyl]propanoic acid A;Cross-references: CAS:6893-02-3 C;Formula: C 15 H 10 I 3 N 1 O 3 A;Formula weight: #chem 632.97 #phys 632.7791 C;Correction formula: C 6 H 1 I 3 O 1 A;Correction weight: #chem 469.79 #phys 469.7158 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 C;Sequence code: Y C;Keywords: iodine F;/Modified site: triiodothyronine (Tyr) >TX;AA0178 L-thyroxine N;Alternate names: 3',3'',5',5''-tetraiodo-L-thyronine N;Systematic name: (S)-2-amino-3-[4-(4-hydroxy-3,5-diiodophenoxy)-3,5-diiodophenyl]propanoic acid A;Cross-references: CAS:51-48-9 C;Formula: C 15 H 9 I 4 N 1 O 3 A;Formula weight: #chem 758.86 #phys 758.6756 C;Correction formula: C 6 H 0 I 4 O 1 A;Correction weight: #chem 595.68 #phys 595.6123 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Rawitch, A.B.; Litwer, M.R.; Gregg, J.; Turner, C.D.; Rouse, J.B.; Hamilton, J.W. Biochem. Biophys. Res. Commun. 118, 423-429, 1984 A;Title: The isolation of identical thyroxine containing amino acid sequences from bovine, ovine and porcine thyroglobulins. A;Reference number: A32735; MUID:84153804 C;Sequence code: Y C;Keywords: iodine F;/Modified site: thyroxine (Tyr) >TX;AA0179 L-6'-bromotryptophan N;Systematic name: (S)-2-amino-3-(6-bromo-1H-indol-3-yl)propanoic acid A;Cross-references: CAS:52448-17-6 C;Formula: C 11 H 9 Br 1 N 2 O 1 A;Formula weight: #chem 265.11 #phys 263.9898 C;Correction formula: C 0 H -1 Br 1 A;Correction weight: #chem 78.90 #phys 77.9105 C;Date: 28-Feb-1997 #structure_revision 28-Feb-1997 #text_change 23-Apr-1999 R;Jimenez, E.C.; Craig, A.G.; Watkins, M.; Hillyard, D.R.; Gray, W.R.; Gulyas, J.; Rivier, J.E.; Cruz, L.J.; Olivera, B.M. Biochemistry 36, 989-994, 1997 A;Title: Bromocontryphan: post-translational bromination of tryptophan. A;Reference number: A58511; MUID:97185706 A;Note: mass spectrographic detection; chromatographic characterization; chemical synthesis R;Craig, A.G.; Jimenez, E.C.; Dykert, J.; Nielsen, D.B.; Gulyas, J.; Abogadie, F.C.; Porter, J.; Rivier, J.E.; Cruz, L.J.; Olivera, B.M.; McIntosh, J.M. J. Biol. Chem. 272, 4689-4698, 1997 A;Title: A novel post-translational modification involving bromination of tryptophan. Identification of the residue, L-6-bromotryptophan, in peptides from Conus imperialis and Conus radiatus venom. A;Reference number: A58512; MUID:97184108 A;Note: mass spectrographic detection; chromatographic characterization; chemical synthesis C;Sequence code: W C;Keywords: bromine F;/Modified site: 6-bromotryptophan (Trp) >TX;AA0181 dehydroalanine N;Alternate names: 4-methylidene-imidazole-5-one active site N;Systematic name: 2-aminopropenoic acid A;Cross-references: CAS:1948-56-7 C;Formula: C 3 H 3 N 1 O 1 A;Formula weight: #chem 69.06 #phys 69.0215 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Correction formula: C -6 H -6 O -1 A;Correction weight: #chem -94.11 #phys -94.0419 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 14-May-1999 R;Chan, W.C.; Bycroft, B.W.; Leyland, M.L.; Lian, L.Y.; Yang, J.C.; Roberts, G.C.K. FEBS Lett. 300, 56-62, 1992 A;Title: Sequence-specific resonance assignment and conformational analysis of subtilin by 2D NMR. A;Reference number: A44571; MUID:92192284 A;Note: (1)H-NMR identification R;Hernandez, D.; Stroh, J.G.; Phillips, A.T. Arch. Biochem. Biophys. 307, 126-132, 1993 A;Title: Identification of Ser(143) as the site of modification in the active site of histidine ammonia-lyase. A;Reference number: S39381; MUID:94058243 A;Note: mass spectrographic and UV spectrographic characterization R;Langer, M.; Lieber, A.; Retey, J. Biochemistry 33, 14034-14038, 1994 A;Title: Histidine ammonia-lyase mutant S143C is posttranslationally converted into fully active wild-type enzyme. Evidence for serine 143 to be the precursor of active site dehydroalanine. A;Reference number: A44705; MUID:95034846 A;Note: mutational analysis; no chemical characterization R;Schwede, T.F.; Retey, J.; Schulz, G.E. Biochemistry 38, 5355-5361, 1999 A;Title: Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile. A;Reference number: A58958; MUID:99238310 A;Note: X-ray crystallography, 2.1 angstroms C;Comment: The modification of serine to dehydroalanine coupled with the formation of 5-imidazolinone by the two neighboring residues produces the 4-methylidene-imidazole-5-one active site of some amino acid ammonia-lyases that differs by UV and mass spectrographic evidence from other known dehydroalanine containing peptides not containing the second modification. C;Sequence code: S #link SER; Y #link TYR A;Conditions: incidental to RESID:AA0187 F;/Modified site: dehydroalanine (Ser) #link SER F;/Modified site: dehydroalanine (Tyr) #link TYR >TX;AA0182 (Z)-dehydrobutyrine N;Systematic name: (Z)-2-amino-butenoic acid A;Cross-references: CAS:71018-10-5 C;Formula: C 4 H 5 N 1 O 1 A;Formula weight: #chem 83.09 #phys 83.0371 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Allgaier, H.; Jung, G.; Werner, R.G.; Schneider, U.; Zaehner, H. Eur. J. Biochem. 160, 9-22, 1986 A;Title: Epidermin: sequencing of a heterodet tetracyclic 21-peptide amide antibiotic. A;Reference number: A61287; MUID:87030262 A;Note: (1)H-NMR and (13)C-NMR identification R;Chan, W.C.; Bycroft, B.W.; Leyland, M.L.; Lian, L.Y.; Yang, J.C.; Roberts, G.C.K. FEBS Lett. 300, 56-62, 1992 A;Title: Sequence-specific resonance assignment and conformational analysis of subtilin by 2D NMR. A;Reference number: A44571; MUID:92192284 A;Note: (1)H-NMR identification C;Comment: In some cases it has not been firmly established whether the natural form is the Z or the E isomer. C;Sequence code: T F;/Modified site: (Z)-dehydrobutyrine (Thr) F;/Modified site: dehydrobutyrine (Thr) >TX;AA0183 dehydrotyrosine N;Systematic name: (Z)-2-amino-3-(4-hydoxyphenyl)propenoic acid C;Formula: C 9 H 7 N 1 O 2 A;Formula weight: #chem 161.16 #phys 161.0477 C;Correction formula: C 0 H -2 A;Correction weight: #chem -2.02 #phys -2.0157 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 07-May-1999 R;Prasher, D.C.; Eckenrode, V.K.; Ward, W.W.; Prendergast, F.G.; Cormier, M.J. Gene 111, 229-233, 1992 A;Title: Primary structure of the Aequorea victoria green-fluorescent protein. A;Reference number: JQ1514; MUID:92175527 R;Yang, F.; Moss, L.G.; Phillips Jr., G.N. submitted to the Brookhaven Protein Data Bank, August 1996 A;Reference number: A65692; PDB:1GFL A;Note: X-ray crystallography, 1.9 angstroms R;Yang, F.; Moss, L.G.; Phillips Jr., G.N. Nature Biotechnol. 14, 1246-1251, 1996 A;Title: The molecular structure of green fluorescent protein. A;Reference number: A58953; MUID:98294543 A;Note: X-ray crystallography, 1.9 angstroms C;Sequence code: Y A;Conditions: incidental to RESID:AA0184 F;/Modified site: dehydrotyrosine (Tyr) >TX;AA0184 L-seryl-5-imidazolinone glycine N;Systematic name: 2-[(S)-1-amino-2-hydroxyethyl]-1-carboxymethyl-1-imidazolin-5-one C;Formula: C 5 H 6 N 2 O 2 A;Formula weight: #chem 126.12 #phys 126.0429 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Date: 31-Mar-1995 #structure_revision 07-May-1999 #text_change 07-May-1999 R;Prasher, D.C.; Eckenrode, V.K.; Ward, W.W.; Prendergast, F.G.; Cormier, M.J. Gene 111, 229-233, 1992 A;Title: Primary structure of the Aequorea victoria green-fluorescent protein. A;Reference number: JQ1514; MUID:92175527 R;Yang, F.; Moss, L.G.; Phillips Jr., G.N. submitted to the Brookhaven Protein Data Bank, August 1996 A;Reference number: A65692; PDB:1GFL A;Note: X-ray crystallography, 1.9 angstroms R;Yang, F.; Moss, L.G.; Phillips Jr., G.N. Nature Biotechnol. 14, 1246-1251, 1996 A;Title: The molecular structure of green fluorescent protein. A;Reference number: A58953; MUID:98294543 A;Note: X-ray crystallography, 1.9 angstroms C;Comment: This entry represents the cross-link of the peptide backbone from the alpha-carboxyl carbon of residue N, a serine, to the alpha-amino nitrogen of residue N+2, a glycine, coupled with the formation of a double bond to the alpha-amino nitrogen of residue N+1 which loses one hydrogen, and the loss of a molecule of water. C;Comment: This cross-link is accompanied by modification of residue N+1. C;Sequence code: S, G A;Conditions: cross-link 1; incidental to RESID:AA0183 F;/Cross-link: 5-imidazolinone (Ser-Gly) >TX;AA0185 L-3-oxoalanine N;Alternate names: 2-amino-3-oxopropionic acid; L-alpha-formylglycine; L-aminomalonaldehydic acid; L-amino-malonic acid semialdehyde; L-serinesemialdehyde (misnomer) N;Systematic name: (S)-2-amino-3-oxopropanoic acid A;Cross-references: CAS:5735-66-0 C;Formula: C 3 H 3 N 1 O 2 A;Formula weight: #chem 85.06 #phys 85.0164 C;Correction formula: C 0 H -2 O 1 S -1 A;Correction weight: #chem -18.08 #phys -17.9928 C;Correction formula: C 0 H -2 A;Correction weight: #chem -2.02 #phys -2.0157 C;Date: 26-Oct-1995 #structure_revision 26-Oct-1995 #text_change 30-Sep-1999 R;Schmidt, B.; Selmer, T.; Ingendoh, A.; von Figura, K. Cell 82, 271-278, 1995 A;Title: A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. A;Reference number: A57113; MUID:95354208 A;Note: mass spectrographic detection R;Selmer, T.; Hallmann, A.; Schmidt, B.; Sumper, M.; von Figura, K. Eur. J. Biochem. 238, 341-345, 1996 A;Title: The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri. A;Reference number: S68892; MUID:96283826 A;Note: mass spectrographic and chemical characterization R;Miech, C.; Dierks, T.; Selmer, T.; von Figura, K.; Schmidt, B. J. Biol. Chem. 273, 4835-4837, 1998 A;Title: Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine. A;Reference number: A59073; MUID:98148017 A;Note: mass spectrographic and chemical characterization; radiolabeling; modification of serine is demonstrated C;Comment: The modified cysteine is found in sulfatases at the second position in the sequence motif [L/V]-C-[A/C/S/T]-P-S-R. C;Sequence code: C #link CYS; S #link SER F;/Modified site: 3-oxoalanine (Cys) #link CYS F;/Modified site: 3-oxoalanine (Ser) #link SER >TX;AA0186 lactic acid N;Alternate names: alpha-hydroxypropionic acid N;Systematic name: 2-hydroxypropanoic acid A;Cross-references: CAS:598-82-3 C;Formula: C 3 H 5 O 2 A;Formula weight: #chem 73.07 #phys 73.0290 C;Correction formula: C 0 H 0 N -1 A;Correction weight: #chem -14.01 #phys -14.0031 C;Date: 23-Jan-1998 #structure_revision 23-Jan-1998 #text_change 21-Jan-2000 R;Van de Kamp, M.; van den Hooven, H.W.; Konings, R.N.H.; Bierbaum, G.; Sahl, H.G.; Kuipers, O.P.; Siezen, R.J.; de Vos, W.M.; Hilbers, C.W.; van de Ven, F.J.M. Eur. J. Biochem. 230, 587-600, 1995 A;Title: Elucidation of the primary structure of the lantibiotic epilancin K7 from Staphylococcus epidermidis K7. Cloning and characterisation of the epilancin-K7-encoding gene and NMR analysis of mature epilancin K7. A;Reference number: S65680; MUID:95331297 A;Note: (1)H-NMR and (13)C-NMR identification; the stereochemistry was not determined C;Comment: (S)-Lactic acid (the L form) is shown. C;Sequence code: S A;Conditions: amino-terminal C;Keywords: blocked amino end F;/Modified site: lactic acid (Ser) F;/Modified site: lactic acid (Ser) (in mature form) >TX;AA0187 L-alanyl-5-imidazolinone glycine N;Alternate names: 4-methylidene-imidazole-5-one active site N;Systematic name: 2-[(S)-1-aminoethyl]-1-carboxymethyl-1-imidazolin-5-one C;Formula: C 5 H 6 N 2 O 1 A;Formula weight: #chem 110.12 #phys 110.0480 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Date: 14-May-1999 #structure_revision 14-May-1999 #text_change 14-May-1999 R;Schwede, T.F.; Retey, J.; Schulz, G.E. Biochemistry 38, 5355-5361, 1999 A;Title: Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile. A;Reference number: A58958; MUID:99238310 A;Note: X-ray crystallography, 2.1 angstroms C;Comment: This entry represents the cross-link of the peptide backbone from the alpha-carboxyl carbon of residue N, a serine, to the alpha-amino nitrogen of residue N+2, a glycine, coupled with the formation of a double bond to the alpha-amino nitrogen of residue N+1 which loses one hydrogen, and the loss of a molecule of water. C;Comment: This cross-link is accompanied by modification of residue N+1. C;Sequence code: A, G A;Conditions: cross-link 1; incidental to RESID:AA0181 F;/Cross-link: 5-imidazolinone (Ala-Gly) >TX;AA0188 L-cysteinyl-5-imidazolinone glycine N;Systematic name: 2-[(R)-1-amino-2-mercaptoethyl]-1-carboxymethyl-1-imidazolin-5-one C;Formula: C 5 H 6 N 2 O 1 S 1 A;Formula weight: #chem 142.18 #phys 142.0201 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Date: 24-Nov-1999 #structure_revision 24-Nov-1999 #text_change 24-Nov-1999 R;Wu, P.C.; Kroening, T.A.; White, P.J.; Kendrick, K.E. J. Bacteriol. 174, 1647-1655, 1992 A;Title: Purification of histidase from Streptomyces griseus and nucleotide sequence of the hutH structural gene. A;Reference number: A42299; MUID:92165741 A;Note: prediction of dehydroalanine active site C;Comment: This entry represents the cross-link of the peptide backbone from the alpha-carboxyl carbon of residue N, a serine, to the alpha-amino nitrogen of residue N+2, a glycine, coupled with the formation of a double bond to the alpha-amino nitrogen of residue N+1 which loses one hydrogen, and the loss of a molecule of water. C;Comment: This cross-link is accompanied by modification of residue N+1. C;Sequence code: C, G A;Conditions: cross-link 1; incidental to RESID:AA0183 F;/Cross-link: 5-imidazolinone (Cys-Gly) >TX;AA0191 D-alanine N;Systematic name: (R)-2-aminopropanoic acid A;Cross-references: CAS:338-69-2 C;Formula: C 3 H 5 N 1 O 1 A;Formula weight: #chem 71.08 #phys 71.0371 C;Correction formula: C 0 H 0 A;Correction weight: #chem 0.00 #phys 0.0000 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Montecucchi, P.C.; De Castiglione, R.; Erspamer, V. Int. J. Pept. Protein Res. 17, 316-321, 1981 A;Title: Identification of dermorphin and Hyp(6)-dermorphin in skin extracts of the Brazilian frog Phyllomedusa rhodei. A;Reference number: A61324; MUID:82029915 C;Sequence code: A #link ALA; S #link SER C;Keywords: D-amino acid F;/Modified site: D-alanine (Ala) #link ALA F;/Modified site: D-alanine (Ser) #link SER >TX;AA0192 D-allo-isoleucine N;Systematic name: (2R,3S)-2-amino-3-methylpentanoic acid A;Cross-references: CAS:1509-35-9 C;Formula: C 6 H 11 N 1 O 1 A;Formula weight: #chem 113.16 #phys 113.0841 C;Correction formula: C 0 H 0 A;Correction weight: #chem 0.00 #phys 0.0000 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Mignogna, G.; Simmaco, M.; Kreil, G.; Barra, D. EMBO J. 12, 4829-4832, 1993 A;Title: Antibacterial and haemolytic peptides containing D-alloisoleucine from the skin of Bombina variegata. A;Reference number: S39612; MUID:94038967 A;Note: chromatographic separation C;Sequence code: I C;Keywords: D-amino acid F;/Modified site: D-allo-isoleucine (Ile) >TX;AA0193 D-methionine N;Systematic name: (R)-2-amino-4-(methylthio)butanoic acid A;Cross-references: CAS:348-67-4 C;Formula: C 5 H 9 N 1 O 1 S 1 A;Formula weight: #chem 131.20 #phys 131.0405 C;Correction formula: C 0 H 0 A;Correction weight: #chem 0.00 #phys 0.0000 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Kreil, G.; Barra, D.; Simmaco, M.; Erspamer, V.; Erspamer, G.F.; Negri, L.; Severini, C.; Corsi, R.; Melchiorri, P. Eur. J. Pharmacol. 162, 123-128, 1989 A;Title: Deltorphin, a novel amphibian skin peptide with high selectivity and affinity for delta opioid receptors. A;Reference number: A60595; MUID:89251774 C;Sequence code: M C;Keywords: D-amino acid F;/Modified site: D-methionine (Met) >TX;AA0194 D-phenylalanine N;Systematic name: (R)-2-amino-3-phenylpropanoic acid A;Cross-references: CAS:673-06-3 C;Formula: C 9 H 9 N 1 O 1 A;Formula weight: #chem 147.18 #phys 147.0684 C;Correction formula: C 0 H 0 A;Correction weight: #chem 0.00 #phys 0.0000 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Kamatani, Y.; Minakata, H.; Kenny, P.T.M.; Iwashita, T.; Watanabe, K.; Funase, K.; Sun, X.P.; Yongsiri, A.; Kim, K.H.; Novales-Li, P.; Novales, E.T.; Kanapi, C.G.; Takeuchi, H.; Nomoto, K. Biochem. Biophys. Res. Commun. 160, 1015-1020, 1989 A;Title: Achatin-I, an endogenous neuroexcitatory tetrapeptide from Achatina fulica ferussac containing a D-amino acid residue. A;Reference number: A32480; MUID:89273551 A;Note: (1)H-NMR identification; chemical synthesis confirmation of stereochemistry R;Ishida, T.; In, Y.; Inoue, M.; Yasuda-Kamatani, Y.; Minakata, H.; Iwashita, T.; Nomoto, K. FEBS Lett. 307, 253-256, 1992 A;Title: Effect of the D-Phe(2) residue on molecular conformation of an endogenous neuropeptide achatin-I. Comparison of X-ray crystal structures of achatin-I (H-Gly-D-Phe-Ala-Asp-OH) and achatin-II (H-Gly-Phe-Ala-Asp-OH). A;Reference number: A44691; MUID:92354723 A;Note: X-ray crystallography, 0.85 angstroms R;Matsuyama, T.; Kaneda, K.; Nakagawa, Y.; Isa, K.; Hara-Hotta, H.; Yano, I. J. Bacteriol. 174, 1769-1776, 1992 A;Title: A novel extracellular cyclic lipopeptide which promotes flagellum-dependent and -independent spreading growth of Serratia marcescens. A;Reference number: A58728; MUID:92193260 A;Note: mass spectrographic and (1)H-NMR characterization C;Sequence code: F C;Keywords: D-amino acid F;/Modified site: D-phenylalanine (Phe) >TX;AA0195 D-serine N;Systematic name: (R)-2-amino-3-hydroxypropanoic acid A;Cross-references: CAS:312-84-5 C;Formula: C 3 H 5 N 1 O 2 A;Formula weight: #chem 87.08 #phys 87.0320 C;Correction formula: C 0 H 0 A;Correction weight: #chem 0.00 #phys 0.0000 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Heck, S.D.; Siok, C.J.; Krapcho, K.J.; Kelbaugh, P.R.; Thadeio, P.F.; Welch, M.J.; Williams, R.D.; Ganong, A.H.; Kelly, M.E.; Lanzetti, A.J.; Gray, W.R.; Phillips, D.; Parks, T.N.; Jackson, H.; Ahlijanian, M.K.; Saccomano, N.A.; Volkmann, R.A. Science 266, 1065-1068, 1994 A;Title: Functional consequences of posttranslational isomerization of Ser(46) in a calcium channel toxin. A;Reference number: A44663; MUID:95063948 A;Note: identification of enzymatically racemized serine C;Sequence code: S C;Keywords: D-amino acid F;/Modified site: D-serine (Ser) >TX;AA0196 D-asparagine N;Alternate names: D-alpha-aminosuccinamic acid; D-aspartic acid beta-amide N;Systematic name: (R)-2-amino-4-butanediamic acid A;Cross-references: CAS:2058-58-4 C;Formula: C 4 H 6 N 2 O 2 A;Formula weight: #chem 114.10 #phys 114.0429 C;Correction formula: C 0 H 0 A;Correction weight: #chem 0.00 #phys 0.0000 C;Date: 30-Jun-1995 #structure_revision 22-Nov-1996 #text_change 23-Apr-1999 R;Ohta, N.; Kubota, I.; Takao, T.; Shimonishi, Y.; Yasuda-Kamatani, Y.; Minakata, H.; Nomoto, K.; Muneoka, Y.; Kobayashi, M. Biochem. Biophys. Res. Commun. 178, 486-493, 1991 A;Title: Fulicin, a novel neuropeptide containing a D-amino acid residue isolated from the ganglia of Achatina fulica. A;Reference number: A44692; MUID:91315471 A;Note: chromatographic spectrographic identification; stereochemical determination; chemical synthesis C;Sequence code: N C;Keywords: D-amino acid F;/Modified site: D-asparagine (Asn) >TX;AA0197 D-leucine N;Alternate names: alpha-aminoisocaproic acid N;Systematic name: (R)-2-amino-4-methylpentanoic acid A;Cross-references: CAS:328-38-1 C;Formula: C 6 H 11 N 1 O 1 A;Formula weight: #chem 113.16 #phys 113.0841 C;Correction formula: C 0 H 0 A;Correction weight: #chem 0.00 #phys 0.0000 C;Date: 22-Nov-1996 #structure_revision 22-Nov-1996 #text_change 23-Apr-1999 R;Fujisawa, Y.; Ikeda, T.; Nomoto, K.; Yasuda-Kamatani, Y.; Minakata, H.; Kenny, P.T.M.; Kubota, I.; Muneoka, Y. Comp. Biochem. Physiol. C 102, 91-95, 1992 A;Title: The FMRFamide-related decapeptide of Mytilus contains a D-amino acid residue. A;Reference number: A58365; MUID:93047882 A;Note: chromatographic detection; chemical synthesis R;Matsuyama, T.; Kaneda, K.; Nakagawa, Y.; Isa, K.; Hara-Hotta, H.; Yano, I. J. Bacteriol. 174, 1769-1776, 1992 A;Title: A novel extracellular cyclic lipopeptide which promotes flagellum-dependent and -independent spreading growth of Serratia marcescens. A;Reference number: A58728; MUID:92193260 A;Note: mass spectrographic and (1)H-NMR characterization C;Sequence code: L C;Keywords: D-amino acid F;/Modified site: D-leucine (Leu) >TX;AA0198 D-tryptophan N;Alternate names: alpha-amino-beta-(3-indolyl)propionoic acid N;Systematic name: (R)-2-amino-3-(1H-indol-3-yl)propanoic acid A;Cross-references: CAS:153-94-6 C;Formula: C 11 H 10 N 2 O 1 A;Formula weight: #chem 186.22 #phys 186.0793 C;Correction formula: C 0 H 0 A;Correction weight: #chem 0.00 #phys 0.0000 C;Date: 22-Nov-1996 #structure_revision 22-Nov-1996 #text_change 23-Apr-1999 R;Jimenez, E.C.; Olivera, B.M.; Gray, W.R.; Cruz, L.J. J. Biol. Chem. 271, 28002-28005, 1996 A;Title: Contryphan is a D-tryptophan-containing Conus peptide. A;Reference number: A43097; MUID:97067006 A;Note: chromatographic detection; chemical synthesis C;Sequence code: W C;Keywords: D-amino acid F;/Modified site: D-tryptophan (Trp) >TX;AA0201 L-isoglutamyl-polyglycine N;Alternate names: gamma-glutamylpolyglycine C;Formula: C 5 H 6 N 1 O 2 + A;Formula weight: #chem 112.11 + #phys 112.0399 + C;Correction formula: C 0 H -1 O -1 A;Correction weight: #chem -17.01 + #phys -17.0027 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Redeker, V.; Levilliers, N.; Schmitter, J.M.; Le Caer, J.P.; Rossier, J.; Adoutte, A.; Bre, M.H. Science 266, 1688-1691, 1994 A;Title: Polyglycylation of tubulin: a posttranslational modification in axonemal microtubules. A;Reference number: A55244; MUID:95084156 A;Note: mass spectrographic identification; the polyglycine is composed of 3 to 34 residues C;Sequence code: E A;Conditions: combinable F;/Binding site: polyglycine (Glu) (covalent) >TX;AA0202 L-isoglutamyl-polyglutamic acid N;Alternate names: gamma-glutamylpolyglutamic acid C;Formula: C 5 H 6 N 1 O 2 + A;Formula weight: #chem 112.11 + #phys 112.0399 + C;Correction formula: C 0 H -1 O -1 A;Correction weight: #chem -17.01 + #phys -17.0027 + C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Edde, B.; Rossier, J.; Le Caer, J.P.; Berwald-Netter, Y.; Koulakoff, A.; Gros, F.; Denoulet, P. J. Cell. Biochem. 46, 134-142, 1991 A;Title: A combination of posttranslational modifications is responsible for the production of neuronal alpha-tubulin heterogeneity. A;Reference number: A61275; MUID:92011952 A;Note: the polyglutamate is composed of 3 to 6 residues C;Sequence code: E A;Conditions: combinable F;/Binding site: polyglutamate (Glu) (covalent) >TX;AA0203 O4'-(phospho-5'-adenosine)-L-tyrosine N;Alternate names: 5'-adenylic-O-tyrosine; hydrogen 5'-adenylate tyrosine ester; O4'-L-tyrosine 5'-adenosine phosphodiester N;Systematic name: (S)-2-amino-3-[4-(5'-adenosine phosphonoxy)phenyl]propanoic acid A;Cross-references: CAS:93957-03-0 C;Formula: C 19 H 21 N 6 O 8 P 1 A;Formula weight: #chem 492.39 #phys 492.1159 C;Correction formula: C 10 H 12 N 5 O 6 P 1 A;Correction weight: #chem 329.21 #phys 329.0525 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Heinrikson, R.L.; Kingdon, H.S. J. Biol. Chem. 246, 1099-1106, 1971 A;Title: Primary structure of Escherichia coli glutamine synthetase. II. The complete amino acid sequence of a tryptic heneicosapeptide containing covalently bound adenylic acid. A;Reference number: A44678; MUID:71111416 A;Note: chemical characterization C;Sequence code: Y A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: AMP (Tyr) (covalent) >TX;AA0204 S-(2-aminovinyl)-D-cysteine N;Alternate names: (S,Z)-S-(2-aminovinyl)cysteine N;Systematic name: (S)-2-amino-3-[((Z)-2-aminovinyl)thio]propanoic acid C;Formula: C 5 H 7 N 2 O 1 S 1 A;Formula weight: #chem 143.19 #phys 143.0279 C;Correction formula: C -1 H -3 O -2 A;Correction weight: #chem -47.03 #phys -47.0133 C;Date: 30-Jun-1995 #structure_revision 30-Jun-1995 #text_change 23-Apr-1999 R;Allgaier, H.; Jung, G.; Werner, R.G.; Schneider, U.; Zaehner, H. Eur. J. Biochem. 160, 9-22, 1986 A;Title: Epidermin: sequencing of a heterodet tetracyclic 21-peptide amide antibiotic. A;Reference number: A61287; MUID:87030262 A;Note: mass spectrographic, (1)H-NMR, and (13)C-NMR identification; stereochemical determination R;Kellner, R.; Jung, G.; Hoerner, T.; Zaehner, H.; Schnell, N.; Entian, K.D.; Goetz, F. Eur. J. Biochem. 177, 53-59, 1988 A;Title: Gallidermin: a new lanthionine-containing polypeptide antibiotic. A;Reference number: A44573; MUID:89030695 A;Note: mass spectrographic identification C;Comment: This cross-link arises from the decarboxylation of the carboxyl-terminal portion of lanthionine (see RESID:AA0110). C;Comment: This residue is acid labile. It may be identified as (2-aminoethyl)-D-cysteine (D-4-thialysine) after hydrogenation with palladium/charcoal catalyst. C;Sequence code: S, C A;Conditions: carboxyl-terminal; cross-link 2 C;Keywords: blocked carboxyl end; lanthionine F;/Cross-link: (S,Z)-S-(2-aminovinyl)cysteine (Ser-Cys) >TX;AA0205 L-cysteine sulfenic acid N;Alternate names: 2-amino-3-sulfenopropanoic acid; 3-sulfenoalanine N;Systematic name: (R)-2-amino-2-carboxyethanesulfenic acid A;Cross-references: CAS:73243-12-6 C;Formula: C 3 H 5 N 1 O 2 S 1 A;Formula weight: #chem 119.14 #phys 119.0041 C;Correction formula: C 0 H 0 O 1 A;Correction weight: #chem 16.00 #phys 15.9949 C;Date: 30-Jun-1995 #structure_revision 30-Jun-1995 #text_change 23-Apr-1999 R;Poole, L.B.; Claiborne, A. J. Biol. Chem. 264, 12330-12338, 1989 A;Title: The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid. A;Reference number: A44706; MUID:89308658 A;Note: mass spectrographic and chemical characterization R;Yeh, J.I.; Claiborne, A.; Hol, W.G.J. Biochemistry 35, 9951-9957, 1996 A;Title: Structure of the native cysteine-sulfenic acid redox center of enterococcal NADH peroxidase refined at 2.8 Angstroms resolution. A;Reference number: A58603; MUID:96322312 A;Note: X-ray crystallography, 2.8 angstroms, active cysteine sulfenic acid form R;Choi, H.J.; Kang, S.; Yang, C.H.; Rhee, S.; Ryu, S.E. Nature Struct. Biol. 5, 400-406, 1998 A;Title: Crystal structure of a novel human peroxidase enzyme at 2.0 angstroms resolution. A;Reference number: A58908; MUID:98246415 A;Note: X-ray crystallography, 2.0 angstroms R;Nagashima, S.; Nakasako, M.; Dohmae, N.; Tsujimura, M.; Takio, K.; Odaka, M.; Yohada, M.; Kamiya, N.; Endo, I. Nature Struct. Biol. 5, 347-351, 1998 A;Title: Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms. A;Reference number: A58907; MUID:98246406 A;Note: X-ray crystallography, 1.7 angstroms; mass spectroscopic identification C;Comment: This reactive residue must be stabilized by the protein structure. As a active site it may be reduced to cysteine or cysteine anion and reoxidized during the reaction cycle. C;Comment: The "active site" feature is used if the stable form is the reduced cysteine; the "modified site" feature is used if the stable form is the oxidized cysteine sulfenic acid. C;Sequence code: C F;/Active site: Cys (cysteine sulfenic acid intermediate) F;/Modified site: cysteine sulfenic acid (Cys) >TX;AA0206 S-glycyl-L-cysteine N;Alternate names: S-(2-amino-1-oxoethyl)cysteine; glycine cysteine thioester N;Systematic name: (R)-2-amino-3-(aminoacetyl)thiopropanoic acid C;Formula: C 5 H 7 N 2 O 2 S 1 A;Formula weight: #chem 159.19 #phys 159.0228 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Date: 30-Jun-1995 #structure_revision 30-Jun-1995 #text_change 23-Apr-1999 R;Jentsch, S.; McGrath, J.P.; Varshavsky, A. Nature 329, 131-134, 1987 A;Title: The yeast DNA repair gene RAD6 encodes a ubiquitin-conjugating enzyme. A;Reference number: A29592; MUID:87315384 C;Comment: These are thiolester cross-links formed between cysteine residues and the carboxyl end of ubiquitin and other proteins. C;Sequence code: C, G A;Conditions: cross-link 2; carboxyl-terminal C;Keywords: thiolester bond F;/Cross-link: thiolester carboxyl end (Cys-Gly) F;/Cross-link: thiolester carboxyl end (Gly) (interchain to Cys ...) F;/Cross-link: thiolester (Cys) (interchain to Gly ...) >TX;AA0207 S-4-hydroxycinnamyl-L-cysteine N;Alternate names: cinnamate cysteine thioester; S-para-coumaryl-L-cysteine N;Systematic name: (S,E)-2-amino-3-[3-(4-hydroxyphenyl)propenoylthio]propanoic acid C;Formula: C 12 H 11 N 1 O 3 S 1 A;Formula weight: #chem 249.29 #phys 249.0460 C;Correction formula: C 9 H 6 O 2 A;Correction weight: #chem 146.15 #phys 146.0368 C;Date: 30-Jun-1995 #structure_revision 30-Jun-1995 #text_change 23-Apr-1999 R;Hoff, W.D.; Duex, P.; Haard, K.; Devreese, B.; Nugteren-Roodzant, I.M.; Crielaard, W.; Boelens, R.; Kaptein, R.; Van Beeumen, J.; Hellingwerf, K.J. Biochemistry 33, 13959-13962, 1994 A;Title: Thiol ester-linked p-coumaric acid as a new photoactive prosthetic group in a protein with rhodopsin-like photochemistry. A;Reference number: A55949; MUID:95034836 A;Note: spectrographic characterization; (1)H-NMR and (13)C-NMR identification R;Baca, M.; Borgstahl, G.E.O.; Boissinot, M.; Burke, P.M.; Williams, D.R.; Slater, K.A.; Getzoff, E.D. Biochemistry 33, 14369-14377, 1994 A;Title: Complete chemical structure of photoactive yellow protein: novel thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry. A;Reference number: A55993; MUID:95072006 A;Note: mass spectrographic and chemical characterization; X-ray crystallography, 1.4 angstroms C;Sequence code: C A;Conditions: combinable C;Keywords: chromoprotein; photoreceptor; thiolester bond F;/Binding site: 4-hydroxycinnamyl (Cys) (covalent) >TX;AA0208 chondroitin sulfate D-glucuronyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine N;Alternate names: chondroitin 4-sulfate (chondroitin sulfate A); chondroitin 6-sulfate (chondroitin sulfate C) N;Systematic name: poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetylamino-2-deoxy-4-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-serine; poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetylamino-2-deoxy-6-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-serine A;Cross-references: CAS:9007-28-7; CAS:24967-93-9; CAS:25322-46-7 C;Formula: C 3 H 4 N 1 O 2 + A;Formula weight: #chem 86.07 + #phys 86.0242 + C;Correction formula: C 0 H -1 + A;Correction weight: #chem -1.01 + #phys -1.0078 + C;Date: 30-Jun-1995 #structure_revision 30-Jun-1995 #text_change 23-Apr-1999 R;Bourdon, M.A.; Krusius, T.; Campbell, S.; Schwartz, N.B.; Ruoslahti, E. Proc. Natl. Acad. Sci. U.S.A. 84, 3194-3198, 1987 A;Title: Identification and synthesis of a recognition signal for the attachment of glycosaminoglycans to proteins. A;Reference number: A44704; MUID:87204104 R;Enghild, J.J.; Salvesen, G.; Hefta, S.A.; Thogersen, I.B.; Rutherfurd, S.; Pizzo, S.V. J. Biol. Chem. 266, 747-751, 1991 A;Title: Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-alpha-inhibitor. A;Reference number: A39079; MUID:91093267 R;Chirat, F.; Balduyck, M.; Mizon, C.; Laroui, S.; Sautiere, P.; Mizon, J. Int. J. Biochem. 23, 1201-1203, 1991 A;Title: A chondroitin-sulfate chain is located on serine-10 of the urinary trypsin inhibitor. A;Reference number: A61580; MUID:92175157 C;Comment: The attachment polysaccharide has not been characterized for all forms of the chondroitin sulfate proteoglycans. C;Sequence code: S A;Conditions: combinable C;Keywords: chondroitin sulfate proteoglycan; glycoprotein F;/Binding site: chondroitin sulfate (Ser) (covalent) >TX;AA0209 dermatan 4-sulfate D-glucuronyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine N;Alternate names: chondroitin sulfate B; beta-heparin N;Systematic name: poly[beta-1,4-L-idopyranuronosyl-alpha-1,3-(2-acetylamino-2-deoxy-4-sulfate D-galactosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-serine; A;Cross-references: CAS:24967-94-0 C;Formula: C 3 H 4 N 1 O 2 + A;Formula weight: #chem 86.07 + #phys 86.0242 + C;Correction formula: C 0 H -1 + A;Correction weight: #chem -1.01 + #phys -1.0078 + C;Date: 30-Jun-1995 #structure_revision 30-Jun-1995 #text_change 23-Apr-1999 R;Bourdon, M.A.; Krusius, T.; Campbell, S.; Schwartz, N.B.; Ruoslahti, E. Proc. Natl. Acad. Sci. U.S.A. 84, 3194-3198, 1987 A;Title: Identification and synthesis of a recognition signal for the attachment of glycosaminoglycans to proteins. A;Reference number: A44704; MUID:87204104 C;Comment: The attachment polysaccharide has not been characterized for all forms of the chondroitin sulfate proteoglycans. C;Sequence code: S A;Conditions: combinable C;Keywords: chondroitin sulfate proteoglycan; dermatan sulfate; glycoprotein F;/Binding site: dermatan sulfate (Ser) (covalent) >TX;AA0210 heparan sulfate D-glucuronyl-D-galactosyl-D-galactosyl-D-xylosyl-L-serine N;Alternate names: heparin; heparitin sulfate N;Systematic name: poly[alpha-1,4-(2-sulfate D-glucopyranuronosyl)-beta-1,4-(2-sulfamino-2-deoxy-6-sulfate D-glucosyl)]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-serine; A;Cross-references: CAS:9005-49-6 C;Formula: C 3 H 4 N 1 O 2 + A;Formula weight: #chem 86.07 + #phys 86.0242 + C;Correction formula: C 0 H -1 + A;Correction weight: #chem -1.01 + #phys -1.0078 + C;Date: 30-Jun-1995 #structure_revision 30-Jun-1995 #text_change 23-Apr-1999 R;Bourdon, M.A.; Krusius, T.; Campbell, S.; Schwartz, N.B.; Ruoslahti, E. Proc. Natl. Acad. Sci. U.S.A. 84, 3194-3198, 1987 A;Title: Identification and synthesis of a recognition signal for the attachment of glycosaminoglycans to proteins. A;Reference number: A44704; MUID:87204104 C;Comment: The attachment polysaccharide has not been characterized for all forms of the chondroitin sulfate proteoglycans. C;Comment: The glucosamine 2-amino groups are to some extent acetylated rather than sulfated. C;Sequence code: S A;Conditions: combinable C;Keywords: chondroitin sulfate proteoglycan; glycoprotein; heparan sulfate F;/Binding site: heparan sulfate (Ser) (covalent) >TX;AA0211 N6-formyl-L-lysine N;Alternate names: epsilon-formyllysine; N(zeta)-formyllysine N;Systematic name: (S)-2-amino-6-(formylamino)hexanoic acid A;Cross-references: CAS:1190-48-3 C;Formula: C 7 H 11 N 2 O 2 A;Formula weight: #chem 155.18 #phys 155.0821 C;Correction formula: C 1 H 0 O 1 A;Correction weight: #chem 28.01 #phys 27.9949 C;Date: 09-Aug-1995 #structure_revision 09-Aug-1995 #text_change 23-Apr-1999 R;Doonan, S.; Garman, A.J.; Hanson, J.M.; Loudon, A.G.; Vernon, C.A. J. Chem. Soc. Perkin 1978, 1157-1160, 1978 A;Title: Identification by mass spectrometry of N(epsilon)-formyl-lysine residues in a peptide from bee venom. A;Reference number: A44642 A;Note: mass spectrographic identification C;Sequence code: K A;Conditions: combinable F;/Binding site: formyl (Lys) (covalent) >TX;AA0212 O4-glycosyl-L-hydroxyproline C;Formula: C 5 H 7 N 1 O 2 + A;Formula weight: #chem 113.12 + #phys 113.0477 + C;Correction formula: C 0 H 0 O 1 + A;Correction weight: #chem 16.00 + #phys 15.9949 + C;Date: 18-Aug-1995 #structure_revision 18-Aug-1995 #text_change 23-Apr-1999 R;Kieliszewski, M.J.; O'Neill, M.; Leykam, J.; Orlando, R. J. Biol. Chem. 270, 2541-2549, 1995 A;Title: Tandem mass spectrometry and structural elucidation of glycopeptides from a hydroxyproline-rich plant cell wall glycoprotein indicate that contiguous hydroxyproline residues are the major sites of hydroxyproline O-arabinosylation. A;Reference number: A55694; MUID:95155313 A;Note: mass spectrographic detection C;Comment: The most common form is arabinofuranosyl-4-proline. C;Sequence code: P A;Conditions: combinable; secondary to RESID:AA0030 C;Keywords: glycoprotein; hydroxyproline F;/Binding site: carbohydrate (Pro) (covalent) >TX;AA0213 O-(phospho-5'-RNA)-L-serine N;Alternate names: O3-(phospho-5'-RNA)-L-serine; O3-L-serine 5'-RNA phosphodiester N;Systematic name: (S)-2-amino-3-(5'-ribonucleic acid phosphonoxy)propanoic acid C;Formula: C 3 H 5 N 1 O 5 P 1 + A;Formula weight: #chem 166.05 + #phys 165.9905 + C;Correction formula: C 0 H 0 O 3 P 1 + A;Correction weight: #chem 78.97 + #phys 78.9585 + C;Date: 18-Aug-1995 #structure_revision 28-Feb-1997 #text_change 14-Jul-2000 R;Samad, A.; Carroll, R.B. Mol. Cell. Biol. 11, 1598-1606, 1991 A;Title: The tumor suppressor p53 is bound to RNA by a stable covalent linkage. A;Reference number: A44683; MUID:91141509 A;Note: chromatographic detection; chemical characterization C;Sequence code: S A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: phosphoryl-RNA (Ser) (covalent) >TX;AA0214 L-citrulline N;Alternate names: N5-(aminocarbonyl)ornithine; N5-carbamylornithine; ureidonorvaline N;Systematic name: (R)-2-amino-5-(aminocarbonyl)aminopentanoic acid A;Cross-references: CAS:372-75-8 C;Formula: C 6 H 11 N 3 O 2 A;Formula weight: #chem 157.17 #phys 157.0851 C;Correction formula: C 0 H -1 N -1 O 1 A;Correction weight: #chem 0.98 #phys 0.9840 C;Date: 25-Aug-1995 #structure_revision 25-Aug-1995 #text_change 23-Apr-1999 R;Wood, D.D.; Moscarello, M.A. J. Biol. Chem. 264, 5121-5127, 1989 A;Title: The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein. A;Reference number: A33273; MUID:89174797 A;Note: chromatographic identification C;Comment: The mechanism for formation of citrulline from arginine in myelin is not known. C;Generating enzyme: protein-arginine deiminase (EC 3.5.3.15) C;Sequence code: R C;Keywords: citrulline F;/Modified site: citrulline (Arg) >TX;AA0215 4-hydroxy-L-arginine N;Alternate names: gamma-hydroxyarginine N;Systematic name: (2S,4Xi)-2-amino-5-guanidino-4-hydroxypentanoic acid A;Cross-references: CAS:61370-10-3 C;Formula: C 6 H 12 N 4 O 2 A;Formula weight: #chem 172.19 #phys 172.0960 C;Correction formula: C 0 H 0 O 1 A;Correction weight: #chem 16.00 #phys 15.9949 C;Date: 03-Nov-1995 #structure_revision 03-Nov-1995 #text_change 23-Apr-1999 R;Papov, V.V.; Diamond, T.V.; Biemann, K.; Waite, J.H. J. Biol. Chem. 270, 20183-20192, 1995 A;Title: Hydroxyarginine-containing polyphenolic proteins in the adhesive plaques of the marine mussel Mytilus edulis. A;Reference number: A57125; MUID:95378278 A;Note: chromatographic detection; mass spectrographic and chemical characterization C;Comment: The stereochemistry for the second chiral center has not been resolved. The (2S,4R) diastereomer is shown. C;Sequence code: R F;/Modified site: 4-hydroxyarginine (Arg) >TX;AA0216 N-(L-isoaspartyl)-L-cysteine N;Alternate names: N-isoaspartyl cysteine; N-beta-aspartylcysteine; 2-amino-N4-(1-carboxy-2-mercaptoethyl)butanediamic acid; 2-(3-amino-3-carboxypropanoyl)amino-3-mercaptopropanoic acid N;Systematic name: (S)-2-amino-4-((R)-1-carboxy-2-mercaptoethyl)amino-4-oxobutanoic acid C;Formula: C 7 H 9 N 2 O 3 S 1 A;Formula weight: #chem 201.23 #phys 201.0334 C;Correction formula: C 0 H -3 N -1 A;Correction weight: #chem -17.03 #phys -17.0265 C;Date: 01-Sep-1995 #structure_revision 01-Sep-1995 #text_change 23-Apr-1999 R;Frechet, D.; Guitton, J.D.; Herman, F.; Faucher, D.; Helynck, G.; Monegier du Sorbier, B.; Ridoux, J.P.; James-Surcouf, E.; Vuilhorgne, M. Biochemistry 33, 42-50, 1994 A;Title: Solution structure of RP 71955, a new 21 amino acid tricyclic peptide active against HIV-1 virus. A;Reference number: A53630; MUID:94114512 C;Sequence code: C, N A;Conditions: cross-link 2; amino-terminal F;/Cross-link: isopeptide amino end (Cys-Asn) F;/Cross-link: isopeptide amino end (Cys) (interchain to Asn ...) F;/Cross-link: isopeptide (Asn) (interchain to Cys ...) >TX;AA0217 2'-alpha-mannosyl-L-tryptophan N;Alternate names: 2'-tryptophan C-mannoside N;Systematic name: (S)-2-amino-3-[1H-2-alpha-mannopyranosyl-indol-3-yl)propanoic acid C;Formula: C 17 H 20 N 2 O 6 A;Formula weight: #chem 348.36 #phys 348.1321 C;Correction formula: C 6 H 10 O 5 A;Correction weight: #chem 162.14 #phys 162.0528 C;Date: 01-Sep-1995 #structure_revision 24-Jul-1997 #text_change 23-Apr-1999 R;Hofsteenge, J.; Mueller, D.R.; de Beer, T.; Loeffler, A.; Richter, W.J.; Vliegenthart, J.F.G. Biochemistry 33, 13524-13530, 1994 A;Title: New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase U-s. A;Reference number: A44670; MUID:95034787 A;Note: mass spectrographic, (1)H-NMR, and (13)C-NMR identification R;de Beer, T., Vliegenthart, J.F., Loffler, A., and Hofsteenge, J. Biochemistry 34, 11785-11789, 1995 A;Title: The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose. A;Reference number: A58588; MUID:96018866 A;Note: (1)H-NMR and (13)C-NMR identification C;Comment: The carbohydrate, identified as mannose, is linked to tryptophan by an unusual C-glycosidic linkage. C;Sequence code: W C;Keywords: glycoprotein F;/Modified site: 2'-mannosyl-tryptophan (Trp) >TX;AA0218 N6-mureinyl-L-lysine N;Alternate names: N6-[(2R,6S)-2-(N-(N-mureinyl-(R)-alanyl)-(S)-glutamyl)amino-6-amino-6-carboxy-1-oxohex-1-yl]lysine C;Formula: C 6 H 11 N 2 O 1 + A;Formula weight: #chem 127.17 + #phys 127.0871 + C;Correction formula: C 0 H -1 + A;Correction weight: #chem -1.01 + #phys -1.0078 + C;Date: 01-Sep-1995 #structure_revision 01-Sep-1995 #text_change 23-Apr-1999 R;Braun, V.; Bosch, V. Eur. J. Biochem. 28, 51-69, 1972 A;Title: Sequence of the murein-lipoprotein and the attachment site of the lipid. A;Reference number: A91199; MUID:72253465 A;Note: chemical characterization C;Comment: The epsilon-amino group of lysine is covalently linked to bacterial cell wall murein by a peptide-like L-alanyl-D-glutamyl-2,6-diaminopimelic acid linkage. C;Sequence code: K A;Conditions: combinable F;/Binding site: murein (Lys) (covalent) >TX;AA0219 1-chondroitin sulfate-L-aspartic acid ester N;Alternate names: 1-aspartic acid ester with 6-chondroitin 4-sulfate; poly[beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetylamino-2-deoxy-4-sulfate D-galactosyl)]beta-1,4-D-glucopyranuronosyl-beta-1,3-(2-acetylamino-2-deoxy-4-sulfate-6-(1-L-aspartyl)-D-galactose) C;Formula: C 4 H 5 N 1 O 3 A;Formula weight: #chem 115.09 #phys 115.0269 C;Correction formula: C 0 H -1 O -1 + A;Correction weight: #chem -17.01 + #phys -17.0027 + C;Date: 30-Jun-1995 #structure_revision 30-Jun-1995 #text_change 28-Jan-2000 R;Enghild, J.J.; Salvesen, G.; Hefta, S.A.; Thogersen, I.B.; Rutherfurd, S.; Pizzo, S.V. J. Biol. Chem. 266, 747-751, 1991 A;Title: Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-alpha-inhibitor. A;Reference number: A39079; MUID:91093267 C;Sequence code: D A;Conditions: carboxyl-terminal C;Keywords: chondroitin sulfate proteoglycan; glycoprotein F;/Modified site: chondroitin sulfate ester carboxyl end (Asp) F;/Modified site: chondroitin sulfate ester carboxyl end (Asp) (in mature form) >TX;AA0220 S-(6-FMN)-L-cysteine N;Alternate names: 6-[S-cysteinyl]flavin mononucleotide; 6-[S-cysteinyl]FMN N;Systematic name: (R)-2-amino-3-[6-riboflavin 5'-dihydrogen phosphate]thiopropanoic acid C;Formula: C 20 H 26 N 5 O 10 P 1 S 1 A;Formula weight: #chem 559.50 #phys 559.1138 C;Correction formula: C 17 H 19 N 4 O 9 P 1 A;Correction weight: #chem 454.34 #phys 454.0890 C;Date: 01-Sep-1995 #structure_revision 01-Sep-1995 #text_change 30-Sep-1999 R;Kenney, W.C.; McIntire, W.; Steenkamp, D.J.; Benisek, W.F. FEBS Lett. 85, 137-140, 1978 A;Title: Amino acid sequence of a cofactor peptide from trimethylamine dehydrogenase. A;Reference number: A13543; MUID:78084818 R;Barber, M.J.; Neame, P.J.; Lim, L.W.; White, S.; Matthews, F.S. J. Biol. Chem. 267, 6611-6619, 1992 A;Title: Correlation of x-ray deduced and experimental amino acid sequences of trimethylamine dehydrogenase. A;Reference number: A42423; MUID:92202205 A;Contents: X-ray crystallography, 2.4 angstroms R;Mathews, F.S.; Lim, L.W.; White, S. submitted to the Brookhaven Protein Data Bank, October 1993 A;Reference number: A52120; PDB:2TMD A;Contents: X-ray crystallography, 2.4 angstroms C;Sequence code: C C;Keywords: flavoprotein; FMN; phosphoprotein F;/Modified site: S-(6-FMN)-cysteine (Cys) >TX;AA0221 1'-(8alpha-FAD)-L-histidine N;Alternate names: pi-(8alpha-FAD)-histidine; pros-(8alpha-FAD)-histidine; 8alpha-[N(1)-histidyl]FAD N;Systematic name: (S)-2-amino-3-(1-[8alpha riboflavin 5'-(trihydrogen diphosphate) 5'->5'-ester with adenosine]imidazol-4-yl)propanoic acid C;Formula: C 33 H 38 N 12 O 16 P 2 A;Formula weight: #chem 920.69 #phys 920.2004 C;Correction formula: C 27 H 31 N 9 O 15 P 2 A;Correction weight: #chem 783.55 #phys 783.1415 C;Date: 01-Sep-1995 #structure_revision 01-Sep-1995 #text_change 23-Apr-1999 C;Comment: The arrangement of the attachment has not been completely established in some cases. C;Sequence code: H C;Keywords: FAD; flavoprotein; phosphoprotein F;/Modified site: 1'-FAD-histidine (His) F;/Modified site: FAD-histidine (His) >TX;AA0222 omega-N-phospho-L-arginine N;Alternate names: alpha-amino-delta-phosphonoguanidinovaleric acid; N5-[imino(phosphonoamino)methyl]-L-ornithine N;Systematic name: (S)-2-amino-5-[imino(phosphonoamino)methyl]aminopentanoic acid A;Cross-references: CAS:1189-11-3 C;Formula: C 6 H 13 N 4 O 4 P 1 A;Formula weight: #chem 236.17 #phys 236.0674 C;Correction formula: C 0 H 1 O 3 P 1 A;Correction weight: #chem 79.98 #phys 79.9663 C;Date: 10-Nov-1995 #structure_revision 10-Nov-1995 #text_change 23-Apr-1999 R;Wakim, B.T.; Aswad, G.D. J. Biol. Chem. 269, 2722-2727, 1994 A;Title: Ca(2+)-calmodulin-dependent phosphorylation of arginine in histone 3 by a nuclear kinase from mouse leukemia cells. A;Reference number: A49978; MUID:94132040 A;Note: chemical characterization C;Generating enzyme: histone-arginine kinase (EC 2.7.3.-) C;Sequence code: R C;Keywords: phosphoprotein F;/Binding site: phosphate (Arg) (covalent) >TX;AA0223 S-diphytanylglycerol diether-L-cysteine N;Alternate names: S-(1-2',3'-phytanyl glycerol)cysteine N;Systematic name: (R)-2-amino-3-[(S)-2,3-(3,7,11,15-tetramethylhexadecanyloxy)propyl]thiopropanoic acid C;Formula: C 46 H 91 N 1 O 3 S 1 A;Formula weight: #chem 738.31 #phys 737.6720 C;Correction formula: C 43 H 86 O 2 A;Correction weight: #chem 635.16 #phys 634.6628 C;Date: 05-Jan-1996 #structure_revision 05-Jan-1996 #text_change 23-Apr-1999 R;Mattar, S.; Scharf, B.; Kent, S.B.H.; Rodewald, K.; Oesterhelt, D.; Engelhard, M. J. Biol. Chem. 269, 14939-14945, 1994 A;Title: The primary structure of halocyanin, an archaeal blue copper protein, predicts a lipid anchor for membrane fixation. A;Reference number: A53792; MUID:94253046 R;Sagami, H.; Kikuchi, A.; Ogura, K. J. Biol. Chem. 270, 14851-14854, 1995 A;Title: A novel type of protein modification by isoprenoid-derived materials. Diphytanylglycerylated proteins in Halobacteria. A;Reference number: A56980; MUID:95318033 A;Note: chromatographic, mass spectrographic and (1)H-NMR identification C;Comment: The stereochemistry of the glycerol has not been determined. The S form is shown. C;Sequence code: C A;Conditions: combinable; incidental to RESID:AA0043 C;Keywords: lipoprotein F;/Binding site: sn-2,3-diphytanylglycerol diether (Cys) (covalent) >TX;AA0224 alpha-1-microglobulin-Ig alpha complex chromophore C;Formula: C 6 H 8 N 2 O 2 S 2 + A;Formula weight: #chem 204.27 + #phys 204.0027 + C;Correction formula: C 0 H -2 + A;Correction weight: #chem -2.02 + #phys -2.0157 + C;Date: 26-Jan-1996 #sequence_revision 26-Jan-1996 #text_change 23-Apr-1999 R;Calero, M.; Escribano, J.; Grubb, A.; Mendez, E. J. Biol. Chem. 269, 384-389, 1994 A;Title: Location of a novel type of interpolypeptide chain linkage in the human protein HC-IgA complex (HC-IgA) and identification of a heterogeneous chromophore associated with the complex. A;Reference number: A53110; MUID:94103241 R;Akerstroem, B.; Bratt, T.; Enghild, J.J. FEBS Lett. 362, 50-54, 1995 A;Title: Formation of the alpha(1)-microglobulin chromophore in mammalian and insect cells: a novel post-translational mechanism? A;Reference number: S68728; MUID:95212582 C;Comment: The structure of the chromophore is not known. It is probably heterogeneous and involves two cysteines in thioether bonds. C;Sequence code: C, C A;Conditions: cross-link 2 C;Keywords: chromoprotein F;/Cross-link: alpha-1-microglobulin-Ig alpha complex chromophore (Cys) (interchain to ...) >TX;AA0225 bis-L-cysteinyl bis-L-histidino diiron disulfide N;Alternate names: Rieske iron-sulfur cofactor N;Systematic name: di-mu-sulfido(di-S-cysteinyliron)(di-N3'-histidinoiron) C;Formula: C 18 H 22 Fe 2 N 8 O 4 S 4 A;Formula weight: #chem 654.39 #phys 653.9346 C;Correction formula: C 0 H -2 Fe 2 S 2 A;Correction weight: #chem 173.81 #phys 173.7984 C;Date: 08-Mar-1996 #structure_revision 16-Jul-1998 #text_change 11-Jun-1999 R;Gurbiel, R.J.; Batie, C.J.; Sivaraja, M.; True, A.E.; Fee, J.A.; Hoffman, B.M.; Ballou, D.P. Biochemistry 28, 4861-4871, 1989 A;Title: Electron-nuclear double resonance spectroscopy of (15)N-enriched phthalate dioxygenase from Pseudomonas cepacia proves that two histidines are coordinated to the [2Fe-2S] Rieske-type clusters. A;Reference number: A57797; MUID:89352563 A;Note: (15)N-NMR characterization R;Iwata, S.; Saynovits, M.; Link, T.A.; Michel, H. submitted to the Brookhaven Protein Data Bank, February 1996 A;Reference number: A66520; PDB:1RIE A;Note: X-ray crystallography, 1.5 angstroms R;Iwata, S.; Lee, J.W.; Okada, K.; Lee, J.K.; Iwata, M.; Rasmussen, B.; Link, T.A.; Ramaswamy, S.; Jap, B.K. Science 281, 64-71, 1998 A;Title: Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex. A;Reference number: A58841; MUID:98316377 A;Note: X-ray crystallography, 4.0 angstroms C;Sequence code: C, H, C, H A;Conditions: cross-link 4 C;Keywords: 2Fe-2S; metalloprotein; Rieske iron-sulfur protein F;/Binding site: 2Fe-2S cluster (Cys, His, Cys, His) (covalent) >TX;AA0226 hexakis-L-cysteinyl hexairon hexasulfide N;Alternate names: prismane iron-sulfur cofactor N;Systematic name: hexa-mu3-sulfidohexakis(S-cysteinyliron) C;Formula: C 18 H 24 Fe 6 N 6 O 6 S 12 A;Formula weight: #chem 1140.30 #phys 1139.4502 C;Correction formula: C 0 H -6 Fe 6 S 6 A;Correction weight: #chem 521.43 #phys 521.3951 C;Date: 08-Mar-1996 #structure_revision 08-Mar-1996 #text_change 11-Jun-1999 R;Moura, I.; Tavares, P.; Moura, J.J.; Ravi, N.; Huynh, B.H.; Liu, M.Y.; LeGall, J. J. Biol. Chem. 267, 4489-4496, 1992 A;Title: Direct spectroscopic evidence for the presence of a 6Fe cluster in an iron-sulfur protein isolated from Desulfovibrio desulfuricans (ATCC 27774). A;Reference number: A42396; MUID:92165800 A;Note: EPR and Moessbauer spectrographic analysis R;Pierik, A.J.; Hagen, W.R.; Dunham, W.R.; Sands, R.H. Eur. J. Biochem. 206, 705-719, 1992 A;Title: Multi-frequency EPR and high-resolution Moessbauer spectroscopy of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough). A;Reference number: A57798; MUID:92298998 A;Note: EPR and Moessbauer spectrographic analysis C;Comment: The prismane 6Fe-6S cluster is now thought not to exist. The structure determined by X-ray consists of a 4Fe-4S cluster, see RESID:AA0140, and a four iron cluster with mixed ligands, see RESID:AA0268. C;Sequence code: C, C, C, C, C, C A;Conditions: cross-link 6 C;Keywords: iron-sulfur protein; metalloprotein F;/Binding site: 6Fe-6S cluster (Cys) (covalent) >TX;AA0227 N6-(phospho-5'-adenosine)-L-lysine N;Alternate names: 5'-adenylic-N6-L-lysine; L-lysine monoanhydride with 5'-adenylic acid; epsilon-5'-adenylic-L-lysine; N(zeta)-5'-adenylic-L-lysine; N6-L-lysine 5'-adenosine phosphoramidester N;Systematic name: (S)-2-amino-6-(5'-adenosine phosphonamino)hexanoic acid A;Cross-references: CAS:35985-27-4 C;Formula: C 16 H 24 N 7 O 7 P 1 A;Formula weight: #chem 457.39 #phys 457.1475 C;Correction formula: C 10 H 12 N 5 O 6 P 1 A;Correction weight: #chem 329.21 #phys 329.0525 C;Date: 17-May-1996 #structure_revision 17-May-1996 #text_change 23-Apr-1999 R;Gumport, R.I.; Lehman, I.R. Proc. Natl. Acad. Sci. U.S.A. 68, 2559-2563, 1971 A;Title: Structure of the DNA ligase-adenylate intermediate: lysine (epsilon-amino)-linked adenosine monophosphoramidate. A;Reference number: A44741; MUID:72090206 A;Note: chemical characterization R;Thogersen, H.C.; Morris, H.R.; Rand, K.N.; Gait, M.J. Eur. J. Biochem. 147, 325-329, 1985 A;Title: Location of the adenylylation site in T4 RNA ligase. A;Reference number: A30612; MUID:85127046 A;Note: mass spectrographic characterization C;Sequence code: K A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: AMP (Lys) (covalent) F;/Active site: Lys (covalent AMP-binding) >TX;AA0228 N6-(phospho-5'-guanosine)-L-lysine N;Alternate names: 5'-guanylic-N6-L-lysine; epsilon-5'-guanylic-L-lysine; L-lysine monoanhydride with 5'-guanylic acid; N(zeta)-5'-guanylic-lysine; N6-L-lysine 5'-guanosine phosphoramidester N;Systematic name: (S)-2-amino-6-(5'-guanosine phosphonamino)hexanoic acid C;Formula: C 16 H 24 N 7 O 8 P 1 A;Formula weight: #chem 473.39 #phys 473.1424 C;Correction formula: C 10 H 12 N 5 O 7 P 1 A;Correction weight: #chem 345.21 #phys 345.0474 C;Date: 17-May-1996 #structure_revision 17-May-1996 #text_change 23-Apr-1999 R;Shuman, S.; Hurwitz, J. Proc. Natl. Acad. Sci. U.S.A. 78, 187-191, 1981 A;Title: Mechanism of mRNA capping by vaccinia virus guanylyltransferase: characterization of an enzyme-guanylate intermediate. A;Reference number: A44746; MUID:81223710 A;Note: chemical characterization R;Roth, M.J.; Hurwitz, J. J. Biol. Chem. 259, 13488-13494, 1984 A;Title: RNA capping by the vaccinia virus guanylyltransferase. Structure of enzyme-guanylate intermediate. A;Reference number: A44747; MUID:85030479 A;Note: chemical characterization C;Sequence code: K A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: GMP (Lys) (covalent) F;/Active site: Lys (covalent GMP-binding) >TX;AA0229 L-cysteine glutathione disulfide N;Alternate names: N-(N-gamma-glutamyl-cystinyl)-glycine; cysteinyl glutathione; L-gamma-glutamyl-L-cysteinyl-glycine (2-1')-disulfide with L-cysteine A;Cross-references: CAS:13081-14-6 C;Formula: C 13 H 20 N 4 O 7 S 2 A;Formula weight: #chem 408.46 #phys 408.0773 C;Correction formula: C 10 H 14 N 3 O 6 S 1 A;Correction weight: #chem 304.31 #phys 304.0603 C;Date: 17-May-1996 #structure_revision 17-May-1996 #text_change 23-Apr-1999 R;Bergenhem, N.; Carlsson, U.; Strid, L. Biochim. Biophys. Acta 871, 55-60, 1986 A;Title: The existence of glutathione and cysteine disulfide-linked to erythrocyte carbonic anhydrase from tiger shark. A;Reference number: A30613; MUID:86187894 A;Note: chemical characterization R;Doermann, P.; Boerchers, T.; Korf, U.; Hojrup, P.; Roepstorff, P.; Spener, F. J. Biol. Chem. 268, 16286-16292, 1993 A;Title: Amino acid exchange and covalent modification by cysteine and glutathione explain isoforms of fatty acid-binding protein occurring in bovine liver. A;Reference number: A47339; MUID:93346368 A;Note: chemical characterization C;Comment: Binding of free glutatione extracellularly is probably not enzymatically catalyzed. C;Sequence code: C C;Keywords: disulfide bond F;/Binding site: glutathione (Cys) (covalent) >TX;AA0230 S-nitrosyl-L-cysteine N;Alternate names: L-cysteine nitrite ester; S-nitrosocysteine N;Systematic name: (R)-2-amino-3-nitrosothio-propanoic acid A;Cross-references: CAS:51209-75-7 C;Formula: C 3 H 4 N 2 O 2 S 1 A;Formula weight: #chem 132.14 #phys 131.9993 C;Correction formula: C 0 H -1 N 1 O 1 A;Correction weight: #chem 29.00 #phys 28.9902 C;Date: 17-May-1996 #structure_revision 17-May-1996 #text_change 23-Apr-1999 R;Jia, L.; Bonaventura, C.; Bonaventura, J.; Stamler, J.S. Nature 380, 221-226, 1996 A;Title: S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. A;Reference number: A57978; MUID:96207749 A;Note: evidence is presented for the binding of nitrosonium to form S-nitrosocysteine R;Mohr, S.; Stamler, J.S.; Bruene, B. J. Biol. Chem. 271, 4209-4214, 1996 A;Title: Posttranslational modification of glyceraldehyde-3-phosphate dehydrogenase by S-nitrosylation and subsequent NADH attachment. A;Reference number: A57970; MUID:96223996 A;Note: chemical characterization C;Comment: The reaction of nitrosonium (NO+) with cysteine residues may not be enzymatically catalyzed; the reaction of cysteine with, or the reductive production of nitric oxide (NO) has not be clarified. C;Sequence code: C F;/Binding site: nitrosonium (Cys) (covalent) >TX;AA0231 N4-(ADP-ribosyl)-L-asparagine N;Alternate names: N4-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-asparagine; N4-alpha-D-ribofuranosyl-L-asparagine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) N;Systematic name: (S)-2-amino-4-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]amino)-4-oxobutanoic acid C;Formula: C 19 H 27 N 7 O 15 P 2 A;Formula weight: #chem 655.41 #phys 655.1040 C;Correction formula: C 15 H 21 N 5 O 13 P 2 A;Correction weight: #chem 541.31 #phys 541.0611 C;Date: 24-May-1996 #structure_revision 24-May-1996 #text_change 23-Apr-1999 R;Sekine, A.; Fujiwara, M.; Narumiya, S. J. Biol. Chem. 264, 8602-8605, 1989 A;Title: Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. A;Reference number: A33190; MUID:89255316 A;Note: identification of ADP-ribosylation site C;Comment: It is not known whether botulinum exoenzyme C3 catalyzes formation of the alpha or beta isomer. The alpha form is presented. C;Comment: The keyword "phosphoprotein" is not used with toxin modification. C;Generating enzyme: NAD(P)+--asparagine ADP-ribosyltransferase (EC 2.4.2.-) C;Sequence code: N C;Keywords: *phosphoprotein F;/Modified site: ADP-ribosylasparagine (Asn) (by ...) >TX;AA0232 L-beta-methylthioaspartic acid N;Alternate names: beta-methylthio-aspartic acid; 3-carboxy-S-methyl-cysteine; 3-methylthio-aspartic acid N;Systematic name: (2R,3Xi)-2-amino-3-methylthiobutanedioic acid A;Cross-references: CAS:180420-54-6 C;Formula: C 5 H 7 N 1 O 3 S 1 A;Formula weight: #chem 161.18 #phys 161.0147 C;Correction formula: C 1 H 2 S 1 A;Correction weight: #chem 46.09 #phys 45.9877 C;Date: 16-Aug-1996 #structure_revision 16-Aug-1996 #text_change 30-Sep-1999 R;Kowalak, J.A.; Walsh, K.A. Protein Sci. 5, 1625-1632, 1996 A;Title: beta-Methylthio-aspartic acid: Identification of a novel posttranslational modification in ribosomal protein S12 from Escherichia coli. A;Reference number: A57989; MUID:97001859 A;Note: mass spectrographic identification; chemical characterization C;Comment: The stereochemistry for the second chiral center has not been resolved. The (2R,3R) form is shown. C;Comment: beta-Methylthioaspartic acid may occur uniquely in ribosomal protein S12. C;Sequence code: D F;/Modified site: beta-methylthioaspartic acid (Asp) >TX;AA0233 5'-(N6-L-lysine)-L-topaquinone N;Alternate names: 5'-(L-lysine)-L-tyrosylquinone; lysyl oxidase cofactor N;Systematic name: 1-[(S)-5-amino-5-carboxypentyl]amino-2-[(S)-2-amino-2-carboxyethyl]-2,6-cyclohexadien-4,5-dione C;Formula: C 15 H 17 N 3 O 4 A;Formula weight: #chem 303.32 #phys 303.1219 C;Correction formula: C 0 H -4 O +1 A;Correction weight: #chem 11.97 #phys 11.9636 C;Date: 06-Sep-1996 #structure_revision 06-Sep-1996 #text_change 23-Apr-1999 R;Wang, S.X.; Mure, M.; Medzihradszky, K.F.; Burlingame, A.L.; Brown, D.E.; Dooley, D.M.; Smith, A.J.; Kagan, H.M.; Klinman, J.P. Science 273, 1078-1084, 1996 A;Title: A crosslinked cofactor in lysyl oxidase: redox function for amino acid side chains. A;Reference number: A57994; MUID:96338001 A;Note: mass spectrographic, raman spectrographic, visible/UV spectrographic, and chemical characterization; phenylhydrazine derivative C;Comment: The linkage between the two components has not been established with certainty. The relation of this cofactor to the copper binding site has not been established. C;Sequence code: K; Y A;Conditions: cross-link 2; secondary to RESID:AA0147 C;Keywords: quinoprotein F;/Cross-link: lysine-topaquinone (Lys-Tyr) F;/Cross-link: lysine-topaquinone (Tyr-Lys) >TX;AA0234 S-methyl-L-cysteine N;Alternate names: L-3-(methylthio)alanine N;Systematic name: (R)-2-amino-3-(methylthio)propanoic acid A;Cross-references: CAS:1187-84-4 C;Formula: C 4 H 7 N 1 O 1 S 1 A;Formula weight: #chem 117.17 #phys 117.0248 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Date: 06-Sep-1996 #structure_revision 06-Sep-1996 #text_change 23-Apr-1999 R;Gonzalez, J.C.; Banerjee, R.V.; Huang, S.; Sumner, J.S.; Matthews, R.G. Biochemistry 31, 6045-6056, 1992 A;Title: Comparison of cobalamin-independent and cobalamin-dependent methionine synthases from Escherichia coli: two solutions to the same chemical problem. A;Reference number: A42863; MUID:92329421 A;Note: radiolabeling C;Sequence code: C C;Keywords: methylated amino acid F;/Binding site: methyl (Cys) (covalent) F;/Active site: Cys (methylcysteine intermediate) >TX;AA0235 4-hydroxy-L-lysine N;Alternate names: alpha,epsilon-diamino-gamma-hydroxycaproic acid; L-threo-gamma-hydroxylysine N;Systematic name: (2S,4R)-2,6-diamino-4-hydroxyhexanoic acid A;Cross-references: CAS:60594-62-9 C;Formula: C 6 H 12 N 2 O 2 A;Formula weight: #chem 144.17 #phys 144.0899 C;Correction formula: C 0 H 0 O 1 A;Correction weight: #chem 16.00 #phys 15.9949 C;Date: 08-Nov-1996 #structure_revision 08-Nov-1996 #text_change 23-Apr-1999 R;Sidler, W.; Kumpf, B.; Suter, F.; Morisset, W.; Wehrmeyer, W.; Zuber, H. Biol. Chem. Hoppe-Seyler 366, 233-244, 1985 A;Title: Structural studies on cryptomonad biliprotein subunits. Two different alpha-subunits in Chroomonas phycocyanin-645 and Cryptomonas phycoerythrin-545. A;Reference number: A94645; MUID:85225953 A;Note: chromatographic identification; the stereochemistry was not established C;Comment: The (2S,4R) diastereomer is shown. C;Sequence code: K C;Keywords: hydroxylysine F;/Modified site: 4-hydroxylysine (Lys) >TX;AA0236 N4-hydroxymethyl-L-asparagine N;Alternate names: beta-hydroxymethylasparagine; N(gamma)-hydroxymethylasparagine; N4-hydroxymethylasparagine N;Systematic name: (S)-2-amino-N4-hydroxymethylbutanediamic acid C;Formula: C 5 H 8 N 2 O 3 A;Formula weight: #chem 144.13 #phys 144.0535 C;Correction formula: C 1 H 2 O 1 A;Correction weight: #chem 30.03 #phys 30.0106 C;Date: 08-Nov-1996 #structure_revision 22-Nov-1996 #text_change 23-Apr-1999 R;Minami, Y.; Yamada, F.; Hase, T.; Matsubara, H.; Murakami, A.; Fujita, Y.; Takao, T.; Shimonishi, Y. FEBS Lett. 191, 216-220, 1985 A;Title: Amino acid sequences of allophycocyanin alpha- and beta-subunits isolated from Anabaena cylindrica. A;Reference number: A91349 A;Note: chromatographic and mass spectrographic characterization C;Sequence code: N C;Keywords: methylated amino acid F;/Modified site: N4-hydroxymethylasparagine (Asn) >TX;AA0237 O-(ADP-ribosyl)-L-serine N;Alternate names: O3-(ADP-ribosyl)-L-serine; O3-[alpha-D-ribofuranoside 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate)]-L-serine; O3-alpha-D-ribofuranosyl-L-serine 5'->5'-ester with adenosine 5'-(trihydrogen diphosphate) N;Systematic name: (S)-2-amino-3-([adenosine 5'-(trihydrogen diphosphate) 5'->5'-ester with alpha-D-ribofuranosyl]oxy)-propanoic acid C;Formula: C 18 H 26 N 6 O 15 P 2 A;Formula weight: #chem 628.39 #phys 628.0931 C;Correction formula: C 15 H 21 N 5 O 13 P 2 A;Correction weight: #chem 541.31 #phys 541.0611 C;Date: 22-Nov-1996 #structure_revision 22-Nov-1996 #text_change 14-Jul-2000 R;Bokoch, G.M.; Parkos, C.A.; Mumby, S.M. J. Biol. Chem. 263, 16744-16749, 1988 A;Title: Purification and characterization of the 22,000-Dalton GTP-binding protein substrate for ADP-ribosylation by botulinum toxin, G-22K. A;Reference number: A31777; MUID:89034164 A;Note: ADP-ribosylation detected; neither the residue nor the location is determined C;Comment: It is not known whether botulinum exoenzyme C3 catalyzes formation of the alpha or beta isomer. The alpha form is presented. C;Comment: The keyword "phosphoprotein" is not used with toxin modification. C;Generating enzyme: NAD(P)+--serine ADP-ribosyltransferase (EC 2.4.2.-) C;Sequence code: S C;Keywords: *phosphoprotein F;/Modified site: ADP-ribosylserine (Ser) (by ...) >TX;AA0238 L-cysteine oxazolecarboxylic acid N;Systematic name: (R)-2-(1-amino-2-mercaptoethyl)-4-oxazolecarboxylic acid C;Formula: C 6 H 6 N 2 O 2 S 1 A;Formula weight: #chem 170.19 #phys 170.0150 C;Correction formula: C 0 H -4 O -1 A;Correction weight: #chem -20.03 #phys -20.0262 C;Date: 06-Dec-1996 #structure_revision 06-Dec-1996 #text_change 23-Apr-1999 R;Li, Y.M.; Milne, J.C.; Madison, L.L.; Kolter, R.; Walsh, C.T. Science 274, 1188-1193, 1996 A;Title: From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase. A;Reference number: A58368; MUID:97053605 A;Note: mass spectrographic identification of peptides and biosynthetic intermediates R;Yorgey, P.; Lee, J.; Koerdel, J.; Vivas, E.; Warner, P.; Jebaratnam, D.; Kolter, R. Proc. Natl. Acad. Sci. U.S.A. 91, 4519-4523, 1994 A;Title: Posttranslational modifications in microcin B17 define an additional class of DNA gyrase inhibitor. A;Reference number: A58375; MUID:94240167 A;Note: (1)H-NMR identification C;Comment: Formed by the condensation of a serine hydroxyl with the carbonyl of the preceding residue and alpha-beta dehydrogenation. C;Generating enzyme: peptidyl-serine cyclase (EC 4.2.1.-); peptidyl-oxazoline dehydrogenase (EC 1.3.-.-) C;Sequence code: C, S C;Keywords: oxazole/thiazole ring F;/Cross-link: oxazole (Cys-Ser) >TX;AA0239 L-cysteine oxazolinecarboxylic acid N;Systematic name: (S)-2-((R)-1-amino-2-mercaptoethyl)-4-oxazolinecarboxylic acid C;Formula: C 6 H 8 N 2 O 2 S 1 A;Formula weight: #chem 172.21 #phys 172.0306 C;Correction formula: C 0 H -2 O -1 A;Correction weight: #chem -18.02 #phys -18.0106 C;Date: 06-Dec-1996 #structure_revision 06-Dec-1996 #text_change 23-Apr-1999 R;Kettenring, J.; Colombo, L.; Ferrari, P.; Tavecchia, P.; Nebuloni, M.; Vekey, K.; Gallo, G.G.; Selva, E. J. Antibiot. 44, 702-715, 1991 A;Title: Antibiotic GE2270 A: a novel inhibitor of bacterial protein synthesis. II. Structure elucidation. A;Reference number: A61210; MUID:91349090 A;Note: mass spectrographic, (1)H-NMR, (13)C-NMR, and IR identification C;Comment: Formed by the condensation of a serine hydroxyl with the carbonyl of the preceding residue. C;Generating enzyme: peptidyl-serine cyclase (EC 4.2.1.-) C;Sequence code: C, S C;Keywords: oxazole/thiazole ring F;/Cross-link: 2-oxazoline (Cys-Ser) >TX;AA0240 glycine oxazolecarboxylic acid N;Systematic name: 2-aminomethyl-4-oxazolecarboxylic acid C;Formula: C 5 H 4 N 2 O 2 A;Formula weight: #chem 124.10 #phys 124.0273 C;Correction formula: C 0 H -4 O -1 A;Correction weight: #chem -20.03 #phys -20.0262 C;Date: 06-Dec-1996 #structure_revision 06-Dec-1996 #text_change 23-Apr-1999 R;Li, Y.M.; Milne, J.C.; Madison, L.L.; Kolter, R.; Walsh, C.T. Science 274, 1188-1193, 1996 A;Title: From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase. A;Reference number: A58368; MUID:97053605 A;Note: mass spectrographic identification of peptides and biosynthetic intermediates R;Yorgey, P.; Lee, J.; Koerdel, J.; Vivas, E.; Warner, P.; Jebaratnam, D.; Kolter, R. Proc. Natl. Acad. Sci. U.S.A. 91, 4519-4523, 1994 A;Title: Posttranslational modifications in microcin B17 define an additional class of DNA gyrase inhibitor. A;Reference number: A58375; MUID:94240167 A;Note: (1)H-NMR identification C;Comment: Formed by the condensation of a serine hydroxyl with the carbonyl of the preceding residue and alpha-beta dehydrogenation. C;Generating enzyme: peptidyl-serine cyclase (EC 4.2.1.-); peptidyl-oxazoline dehydrogenase (EC 1.3.-.-) C;Sequence code: G, S C;Keywords: oxazole/thiazole ring F;/Cross-link: oxazole (Gly-Ser) >TX;AA0241 glycine thiazolecarboxylic acid N;Systematic name: 2-aminomethyl-4-thiazolecarboxylic acid A;Cross-references: CAS:25438-22-6 C;Formula: C 5 H 4 N 2 O 1 S 1 A;Formula weight: #chem 140.17 #phys 140.0044 C;Correction formula: C 0 H -4 O -1 A;Correction weight: #chem -20.03 #phys -20.0262 C;Date: 06-Dec-1996 #structure_revision 06-Dec-1996 #text_change 23-Apr-1999 R;Li, Y.M.; Milne, J.C.; Madison, L.L.; Kolter, R.; Walsh, C.T. Science 274, 1188-1193, 1996 A;Title: From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase. A;Reference number: A58368; MUID:97053605 A;Note: mass spectrographic identification of peptides and biosynthetic intermediates R;Yorgey, P.; Lee, J.; Koerdel, J.; Vivas, E.; Warner, P.; Jebaratnam, D.; Kolter, R. Proc. Natl. Acad. Sci. U.S.A. 91, 4519-4523, 1994 A;Title: Posttranslational modifications in microcin B17 define an additional class of DNA gyrase inhibitor. A;Reference number: A58375; MUID:94240167 A;Note: (1)H-NMR identification C;Comment: Formed by the condensation of a cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. C;Generating enzyme: peptidyl-cysteine cyclase (EC 4.2.1.-); peptidyl-thiazoline dehydrogenase (EC 1.3.-.-) C;Sequence code: G, C C;Keywords: oxazole/thiazole ring F;/Cross-link: thiazole (Gly-Cys) >TX;AA0242 L-serine thiazolecarboxylic acid N;Systematic name: (R)-2-(1-amino-2-hydroxyethyl)-4-thiazolecarboxylic acid C;Formula: C6 H 6 N 2 O 2 S 1 A;Formula weight: #chem 170.19 #phys 170.0150 C;Correction formula: C 0 H -4 O -1 A;Correction weight: #chem -20.03 #phys -20.0262 C;Date: 06-Dec-1996 #structure_revision 06-Dec-1996 #text_change 23-Apr-1999 R;Li, Y.M.; Milne, J.C.; Madison, L.L.; Kolter, R.; Walsh, C.T. Science 274, 1188-1193, 1996 A;Title: From peptide precursors to oxazole and thiazole-containing peptide antibiotics: microcin B17 synthase. A;Reference number: A58368; MUID:97053605 A;Note: mass spectrographic identification of peptides and biosynthetic intermediates R;Yorgey, P.; Lee, J.; Koerdel, J.; Vivas, E.; Warner, P.; Jebaratnam, D.; Kolter, R. Proc. Natl. Acad. Sci. U.S.A. 91, 4519-4523, 1994 A;Title: Posttranslational modifications in microcin B17 define an additional class of DNA gyrase inhibitor. A;Reference number: A58375; MUID:94240167 A;Note: (1)H-NMR identification C;Comment: Formed by the condensation of a cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. C;Generating enzyme: peptidyl-cysteine cyclase (EC 4.2.1.-); peptidyl-thiazoline dehydrogenase (EC 1.3.-.-) C;Sequence code: S, C C;Keywords: oxazole/thiazole ring F;/Cross-link: thiazole (Ser-Cys) >TX;AA0243 L-phenyalanine thiazolecarboxylic acid N;Systematic name: (R)-2-(1-amino-2-phenylethyl)-4-thiazolecarboxylic acid C;Formula: C 11 H 8 N 2 O 1 S 1 A;Formula weight: #chem 216.27 #phys 216.0357 C;Correction formula: C 0 H -4 O -1 A;Correction weight: #chem -20.03 #phys -20.0262 C;Date: 06-Dec-1996 #structure_revision 06-Dec-1996 #text_change 23-Apr-1999 R;Kettenring, J.; Colombo, L.; Ferrari, P.; Tavecchia, P.; Nebuloni, M.; Vekey, K.; Gallo, G.G.; Selva, E. J. Antibiot. 44, 702-715, 1991 A;Title: Antibiotic GE2270 A: a novel inhibitor of bacterial protein synthesis. II. Structure elucidation. A;Reference number: A61210; MUID:91349090 A;Note: mass spectrographic, (1)H-NMR, (13)C-NMR, and IR identification C;Comment: Formed by the condensation of a cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. C;Generating enzyme: peptidyl-cysteine cyclase (EC 4.2.1.-); peptidyl-thiazoline dehydrogenase (EC 1.3.-.-) C;Sequence code: F, C C;Keywords: oxazole/thiazole ring F;/Cross-link: thiazole (Phe-Cys) >TX;AA0244 L-cysteine thiazolecarboxylic acid N;Systematic name: (S)-2-(1-amino-2-mercaptoethyl)-4-thiazolecarboxylic acid C;Formula: C 6 H 6 N 2 O 1 S 2 A;Formula weight: #chem 186.26 #phys 185.9922 C;Correction formula: C 0 H -4 O -1 A;Correction weight: #chem -20.03 #phys -20.0262 C;Date: 06-Dec-1996 #structure_revision 06-Dec-1996 #text_change 23-Apr-1999 R;Kettenring, J.; Colombo, L.; Ferrari, P.; Tavecchia, P.; Nebuloni, M.; Vekey, K.; Gallo, G.G.; Selva, E. J. Antibiot. 44, 702-715, 1991 A;Title: Antibiotic GE2270 A: a novel inhibitor of bacterial protein synthesis. II. Structure elucidation. A;Reference number: A61210; MUID:91349090 A;Note: mass spectrographic, (1)H-NMR, (13)C-NMR, and IR identification C;Comment: Formed by the condensation of a cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. C;Generating enzyme: peptidyl-cysteine cyclase (EC 4.2.1.-); peptidyl-thiazoline dehydrogenase (EC 1.3.-.-) C;Sequence code: C, C C;Keywords: oxazole/thiazole ring F;/Cross-link: thiazole (Cys-Cys) >TX;AA0245 L-lysine thiazolecarboxylic acid N;Systematic name: (R)-2-(1,5-diaminopentyl)-4-thiazolecarboxylic acid C;Formula: C 9 H 13 N 3 O 1 S 1 A;Formula weight: #chem 211.29 #phys 211.0779 C;Correction formula: C 0 H -4 O -1 A;Correction weight: #chem -20.03 #phys -20.0262 C;Date: 06-Dec-1996 #structure_revision 06-Dec-1996 #text_change 23-Apr-1999 R;Kettenring, J.; Colombo, L.; Ferrari, P.; Tavecchia, P.; Nebuloni, M.; Vekey, K.; Gallo, G.G.; Selva, E. J. Antibiot. 44, 702-715, 1991 A;Title: Antibiotic GE2270 A: a novel inhibitor of bacterial protein synthesis. II. Structure elucidation. A;Reference number: A61210; MUID:91349090 A;Note: mass spectrographic, (1)H-NMR, (13)C-NMR, and IR identification C;Comment: Formed by the condensation of a cysteine thiol with the carbonyl of the preceding residue and alpha-beta dehydrogenation. C;Generating enzyme: peptidyl-cysteine cyclase (EC 4.2.1.-); peptidyl-thiazoline dehydrogenase (EC 1.3.-.-) C;Sequence code: K, C C;Keywords: oxazole/thiazole ring F;/Cross-link: thiazole (Lys-Cys) >TX;AA0246 O-(phospho-5'-DNA)-L-serine N;Alternate names: O3-(phospho-5'-DNA)-L-serine; O3-L-serine 5'-DNA phosphodiester N;Systematic name: (S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)propanoic acid C;Formula: C 3 H 5 N 1 O 5 P 1 + A;Formula weight: #chem 166.05 + #phys 165.9905 + C;Correction formula: C 0 H 0 O 3 P 1 + A;Correction weight: #chem 78.97 + #phys 78.9585 + C;Date: 28-Feb-1997 #structure_revision 28-Feb-1997 #text_change 14-Jul-2000 R;Desiderio, S.V.; Kelly Jr., T.J. J. Mol. Biol. 145, 319-337, 1981 A;Title: Structure of the linkage between adenovirus DNA and the 55,000 molecular weight terminal protein. A;Reference number: A30626; MUID:81267318 A;Note: chromatographic detection; chemical characterization R;Smart, J.E.; Stillman, B.W. J. Biol. Chem. 257, 13499-13506, 1982 A;Title: Adenovirus terminal protein precursor. Partial amino acid sequence and the site of covalent linkage to virus DNA. A;Reference number: A92353; MUID:83056845 A;Note: chromatographic detection; chemical characterization C;Sequence code: S A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: phosphoryl-DNA (Ser) (covalent) >TX;AA0247 keratan sulfate D-glucuronyl-D-galactosyl-D-galactosyl-D-xylosyl-L-threonine N;Alternate names: keratosulfate N;Systematic name: poly[beta-1,4-(2-acetylamino-2-deoxy-6-sulfate D-glucosyl)-beta-1,3-D-galactosyl]-beta-1,4-D-glucopyranuronosyl-beta-1,3-D-galactosyl-beta-1,3-D-galactosyl-beta-1,4-D-xylosyl-beta-1,3-L-threonine C;Formula: C 4 H 6 N 1 O 2 + A;Formula weight: #chem 100.10 + #phys 100.0399 + C;Correction formula: C 0 H -1 + A;Correction weight: #chem -1.01 + #phys -1.0078 + C;Date: 21-Mar-1997 #structure_revision 21-Mar-1997 #text_change 23-Apr-1999 R;Bourdon, M.A.; Krusius, T.; Campbell, S.; Schwartz, N.B.; Ruoslahti, E. Proc. Natl. Acad. Sci. U.S.A. 84, 3194-3198, 1987 A;Title: Identification and synthesis of a recognition signal for the attachment of glycosaminoglycans to proteins. A;Reference number: A44704; MUID:87204104 R;Barry, F.P.; Gaw, J.U.; Young, C.N.; Neame, P.J. Biochem. J. 286, 761-769, 1992 A;Title: Hyaluronan-binding region of aggrecan from pig laryngeal cartilage. Amino acid sequence, analysis of N-linked oligosaccharides and location of the keratan sulphate. A;Reference number: S29139; MUID:93038505 A;Note: antibody detection during sequencing C;Comment: The attachment polysaccharide has not been characterized for all forms of the chondroitin sulfate proteoglycans. C;Sequence code: T A;Conditions: combinable C;Keywords: chondroitin sulfate proteoglycan; glycoprotein; keratan sulfate F;/Binding site: keratan sulfate (Thr) (covalent) >TX;AA0248 L-selenocysteinyl molybdopterin guanine dinucleotide N;Alternate names: formate dehydrogenase selenocysteine molybdenum cofactor N;Systematic name: 8-amino-2-(2-amino-2-carboxyethyl)seleno-1a,3a,4,5a,6,9,10,11,11a-nonahydro-4-(trihydrogen diphosphate 5'-ester with guanosine)methyl-2,2,10-trioxo-pteridino[6,7-5,6]pyrano[3,4-4,3][1,2,5]molybdadithiolene C;Formula: C 23 H 28 Mo 1 N 11 O 16 P 2 S 2 Se 1 A;Formula weight: #chem 1015.52 #phys 1017.8851 C;Correction formula: C 20 H 23 Mo 1 N 10 O 15 P 2 S 2 A;Correction weight: #chem 865.48 #phys 866.9315 C;Date: 12-Sep-1997 #structure_revision 19-Sep-1997 #text_change 14-May-1999 R;Axley, M.J.; Grahame, D.A.; Stadtman, T.C. J. Biol. Chem. 265, 18213-18218, 1990 A;Title: Escherichia coli formate-hydrogen lyase. Purification and properties of the selenium-dependent formate dehydrogenase component. A;Reference number: A36088; MUID:91009309 R;Gladyshev, V.N.; Khangulov, S.V.; Axley, M.J.; Stadtman, T.C. Proc. Natl. Acad. Sci. U.S.A. 91, 7708-7711, 1994 A;Title: Coordination of selenium to molybdenum in formate dehydrogenase H from Escherichia coli. A;Reference number: A58332; MUID:94329585 A;Note: selenium coordination of cofactor by EPR R;Sun, P.D.; Boyington, J.C. submitted to the Brookhaven Protein Data Bank, January 1997 A;Reference number: A67458; PDB:1AA6 A;Note: X-ray crystallography, 2.3 angstroms, reduced form R;Sun, P.D.; Boyington, J.C. submitted to the Brookhaven Protein Data Bank, January 1997 A;Reference number: A67590; PDB:1FDO A;Note: X-ray crystallography, 2.8 angstroms, oxidized form R;Boyington, J.C.; Gladyshev, V.N.; Khangulov, S.V.; Stadtman, T.C.; Sun, P.D. Science 275, 1305-1308, 1997 A;Title: Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster. A;Reference number: A58962; MUID:97190104 A;Note: X-ray crystallography C;Comment: One possible structure of the most reduced form (+6H) is shown. The fully oxidized form would be the corresponding 4,9,10-trihydro form. C;Sequence code: C A;Conditions: secondary to RESID:AA0022 C;Keywords: metalloprotein; molybdenum; molybdopterin; phosphoprotein; selenocysteine F;/Binding site: molybdopterin guanine dinucleotide (Cys) (covalent) >TX;AA0249 O4'-(phospho-5'-RNA)-L-tyrosine N;Alternate names: O4'-L-tyrosine 5'-RNA phosphodiester N;Systematic name: (S)-2-amino-3-[4-(5'-ribonucleic acid phosphonoxy)phenyl]propanoic acid C;Formula: C 9 H 10 N 1 O 5 P 1 A;Formula weight: #chem 243.16 #phys 243.0297 C;Correction formula: C 0 H 1 O 3 P 1 + A;Correction weight: #chem 79.98 + #phys 79.9663 + C;Date: 12-Sep-1997 #structure_revision 12-Sep-1997 #text_change 23-Apr-1999 R;Ambros, V.; Baltimore, D. J. Biol. Chem. 253, 5263-5266, 1978 A;Title: Protein is linked to the 5' end of poliovirus RNA by a phosphodiester linkage to tyrosine. A;Reference number: A30636; MUID:78218195 R;Rothberg, P.G.; Harris, T.J.; Nomoto, A.; Wimmer, E. Proc. Natl. Acad. Sci. U.S.A. 75, 4868-4872, 1978 A;Title: O4-(5'-Uridylyl)tyrosine is the bond between the genome-linked protein and the RNA of poliovirus. A;Reference number: A30637; MUID:79116223 A;Note: chemical characterization R;Kitamura, N.; Semler, B.L.; Rothberg, P.G.; Larsen, G.R.; Adler, C.J.; Dorner, A.J.; Emini, E.A.; Hanecak, R.; Lee, J.J.; van der Werf, S.; Anderson, C.W.; Wimmer, E. Nature 291, 547-553, 1981 A;Title: Primary structure, gene organization and polypeptide expression of poliovirus RNA. A;Reference number: A93258; MUID:81220953 A;Note: protein sequence R;Murphy, J.F.; Rychlik, W.; Rhoads, R.E.; Hunt, A.G.; Shaw, J.G. J. Virol. 65, 511-513, 1991 A;Title: A tyrosine residue in the small nuclear inclusion protein of tobacco vein mottling virus links the VPg to the viral RNA. A;Reference number: A30631; MUID:91087329 A;Note: chemical characterization C;Sequence code: Y A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: phosphoryl-RNA (Tyr) (covalent) >TX;AA0250 3-(3'-L-histidyl)-L-tyrosine N;Alternate names: beta-(N3'-histidyl)tyrosine N;Systematic name: (2S,3R)-2-amino-3-[3-((S)-2-amino-2-carboxy-1-(4-hydoxyphenyl)ethyl)imidazol-4-yl]propanoic acid C;Formula: C 15 H 16 N 4 O 3 A;Formula weight: #chem 300.32 #phys 300.1222 C;Correction formula: C 0 H -2 A;Correction weight: #chem -2.02 #phys -2.0157 C;Date: 21-Nov-1997 #structure_revision 21-Nov-1997 #text_change 14-May-1999 R;Bravo, J.; Fita, I.; Ferrer, J.C.; Ens, W.; Hillar, A.; Switala, J.; Loewen, P.C. Protein Sci. 6, 1016-1023, 1997 A;Title: Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli. A;Reference number: A58661; MUID:97289987 A;Note: X-ray crystallography identification, 1.9 angstroms; mass spectrographic detection C;Comment: The chirality of tyrosine C-3 is not specified; from the model it appears to be 3R. C;Comment: This modification is different from the modification 3'-(1'-L-histidyl)-L-tyrosine, see RESID:AA0270. C;Sequence code: H, Y A;Conditions: cross-link 2 F;/Cross-link: 3'-histidyl-3-tyrosine (His-Tyr) F;/Cross-link: 3'-histidyl-3-tyrosine (Tyr-His) >TX;AA0251 L-methionine sulfone N;Alternate names: S,S-dioxymethionine N;Systematic name: (S)-2-amino-4-(methylsulfonyl)butanoic acid A;Cross-references: CAS:7314-32-1 C;Formula: C 5 H 9 N 1 O 3 S 1 A;Formula weight: #chem 163.20 #phys 163.0303 C;Correction formula: C 0 H 0 O 2 A;Correction weight: #chem 32.00 #phys 31.9898 C;Date: 21-Nov-1997 #structure_revision 21-Nov-1997 #text_change 23-Apr-1999 R;Buzy, A.; Bracchi, V.; Sterjiades, R.; Chroboczek, J.; Thibault, P.; Gagnon, J.; Jouve, H.M.; Hudry-Clergeon, G. J. Protein Chem. 14, 59-72, 1995 A;Title: Complete amino acid sequence of Proteus mirabilis PR catalase. Occurrence of a methionine sulfone in the close proximity of the active site. A;Reference number: A58663; MUID:95305957 A;Note: mass spectrographic detection R;Gouet, P.; Jouve, H.M.; Dideberg, O. J. Mol. Biol. 249, 933-954, 1995 A;Title: Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH. A;Reference number: A58664; MUID:95311317 A;Note: X-ray crystallography, 2.2 angstroms C;Sequence code: M F;/Modified site: methionine sulfone (Met) >TX;AA0252 dipyrrolylmethanemethyl-L-cysteine N;Alternate names: 3-[5-(3-acetic acid-4-propanoic acid-1-pyrrol-2-yl)methyl-3-acetic acid-4-propanoic acid-1-pyrrol-2-yl]methylthio-2-aminopropanoic acid; dipyrrole cofactor; dipyrrolylmethyl-L-cysteine; dipyrromethane cofactor; pyrromethane cofactor N;Systematic name: 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 A;Cross-references: CAS:29261-13-0 C;Formula: C 23 H 27 N 3 O 9 S 1 A;Formula weight: #chem 521.55 #phys 521.1468 C;Correction formula: C 20 H 22 N 2 O 8 A;Correction weight: #chem 418.41 #phys 418.1376 C;Date: 12-Dec-1997 #structure_revision 12-Dec-1997 #text_change 23-Apr-1999 R;Jordan, P.M.; Warren, M.J.; Williams, H.J.; Stolowich, N.J.; Roessner, C.A.; Grant, S.K.; Scott, A.I. FEBS Lett. 235, 189-193, 1988 A;Title: Identification of a cysteine residue as the binding site for the dipyrromethane cofactor at the active site of Escherichia coli porphobilinogen deaminase. A;Reference number: A58694; MUID:88296821 A;Note: radioisotope labeling; (13)C-NMR characterization R;Miller, A.D.; Hart, G.J.; Packman, L.C.; Battersby, A.R. Biochem. J. 254, 915-918, 1988 A;Title: Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound to the protein through the sulphur atom of cysteine-242. A;Reference number: A58695; MUID:89061636 A;Note: chemical characterization R;Hart, G.J.; Miller, A.D.; Battersby, A.R. Biochem. J. 252, 909-912, 1988 A;Title: Evidence that the pyrromethane cofactor of hydroxymethylbilane synthase (porphobilinogen deaminase) is bound through the sulphur atom of a cysteine residue. A;Reference number: A58696; MUID:88339864 A;Note: chemical characterization; (13)C-NMR identification R;Louie, G.V.; Brownlie, P.D.; Lambert, R.; Cooper, J.B.; Blundell, T.L.; Wood, S.P.; Malashkevich, V.N.; Haedener, A.; Warren, M.J.; Shoolingin-Jordan, P.M. Proteins 25, 48-78, 1996 A;Title: The three-dimensional structure of Escherichia coli porphobilinogen deaminase at 1.76-angstroms resolution. A;Reference number: A58699; MUID:96323958 A;Note: X-ray crystallography, 1.76 angstroms R;Louie, G.V.; Brownlie, P.D.; Lambert, R.; Cooper, J.B.; Blundell, T.L.; Wood, S.P.; Warren, M.J.; Woodcock, S.C.; Jordan, P.M. submitted to the Brookhaven Protein Data Bank, November 1992 A;Reference number: A51329; PDB:1PDA A;Note: X-ray crystallography, 1.76 angstroms C;Sequence code: C F;/Modified site: dipyrrolylmethanemethyl (Cys) (covalent) >TX;AA0253 S-(2-aminovinyl)-3-methyl-D-cysteine N;Alternate names: decarboxylated methyllanthionine N;Systematic name: (2S,3S)-2-amino-3-[((Z)-2-aminovinyl)thio]butanoic acid C;Formula: C 6 H 9 N 2 O 1 S 1 A;Formula weight: #chem 157.22 #phys 157.0436 C;Correction formula: C -1 H -3 O -2 A;Correction weight: #chem -47.03 #phys -47.0133 C;Date: 23-Jan-1998 #structure_revision 23-Jan-1998 #text_change 23-Apr-1999 R;Prasch, T.; Naumann, T.; Markert, R.L.M.; Sattler, M.; Schubert, W.; Schaal, S.; Bauch, M.; Kogler, H.; Griesinger, C. Eur. J. Biochem. 244, 501-512, 1997 A;Title: Constitution and solution conformation of the antibiotic mersacidin determined by NMR and molecular dynamics. A;Reference number: A58706; MUID:97234581 A;Note: identification by (1)H- and (13)C-NMR C;Comment: This cross-link arises from the decarboxylation of the carboxyl-terminal portion of 3-methyllanthionine. C;Sequence code: T, C A;Conditions: carboxyl-terminal; cross-link 2 C;Keywords: blocked carboxyl end; lanthionine F;/Cross-link: (2S,3S,5Z)-S-(2-aminovinyl)-3-methylcysteine (Thr-Cys) >TX;AA0254 O4'-(phospho-5'-DNA)-L-tyrosine N;Alternate names: O4'-L-tyrosine 5'-DNA phosphodiester N;Systematic name: (S)-2-amino-3-[4-(5'-deoxyribonucleic acid phosphonoxy)phenyl]propanoic acid C;Formula: C 9 H 10 N 1 O 5 P 1 A;Formula weight: #chem 243.16 #phys 243.0297 C;Correction formula: C 0 H 1 O 3 P 1 + A;Correction weight: #chem 79.98 + #phys 79.9663 + C;Date: 29-May-1998 #structure_revision 29-May-1998 #text_change 23-Apr-1999 R;Hsieh, J.C.; Jung, G.; Leavitt, M.C.; Ito, J. Nucleic Acids Res. 15, 8999-9009, 1987 A;Title: Primary structure of the DNA terminal protein of bacteriophage PRD1. A;Reference number: S01613; MUID:88067710 A;Note: structure prediction C;Sequence code: Y A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: phosphoryl-DNA (Tyr) (covalent) >TX;AA0255 O-(phospho-5'-DNA)-L-threonine N;Alternate names: O3-(phospho-5'-DNA)-L-threonine; O3-L-threonine 5'-DNA phosphodiester N;Systematic name: (S)-2-amino-3-(5'-deoxyribonucleic acid phosphonoxy)butanoic acid C;Formula: C 4 H 7 N 1 O 5 P 1 + A;Formula weight: #chem 180.08 + #phys 180.0062 + C;Correction formula: C 0 H 0 O 3 P 1 + A;Correction weight: #chem 78.97 + #phys 78.9585 + C;Date: 05-Jun-1998 #structure_revision 05-Jun-1998 #text_change 14-Jul-2000 R;Garcia, P.; Hermoso, J.M.; Garcia, J.A.; Garcia, E.; Lopez, R.; Salas, M. J. Virol. 58, 31-35, 1986 A;Title: Formation of a covalent complex between the terminal protein of pneumococcal bacteriophage Cp-1 and 5'-dAMP. A;Reference number: A30638; MUID:86144103 A;Note: chemical characterization C;Sequence code: T A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: phosphoryl-DNA (Thr) (covalent) >TX;AA0256 O4'-(phospho-5'-uridine)-L-tyrosine N;Alternate names: 5'-uridylic-O-tyrosine; hydrogen 5'-uridylate tyrosine ester; O4'-L-tyrosine 5'-uridine phosphodiester N;Systematic name: (S)-2-amino-3-[4-(5'-uridine phosphonoxy)phenyl]propanoic acid C;Formula: C 18 H 20 N 3 O 10 P 1 A;Formula weight: #chem 469.35 #phys 469.0886 C;Correction formula: C 9 H 11 N 2 O 8 P 1 A;Correction weight: #chem 306.17 #phys 306.0253 C;Date: 11-Sep-1998 #structure_revision 11-Sep-1998 #text_change 23-Apr-1999 R;Son, H.S.; Rhee, S.G. J. Biol. Chem. 262, 8690-8695, 1987 A;Title: Cascade control of Escherichia coli glutamine synthetase: purification and properties of P-II protein and nucleotide sequence of its structural gene. A;Reference number: A29307; MUID:87250488 A;Note: chemical detection and spectrographic characterization C;Generating enzyme: uridylyltransferase (EC 2.7.7.59) C;Sequence code: Y A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: UMP (Tyr) (covalent) >TX;AA0257 N-(L-glutamyl)-L-tyrosine N;Systematic name: (S,S)-2-(2-aminopentanedio-1-yl)amino-3-(4-hydoxyphenyl)propanoic acid C;Formula: C 14 H 9 N 8 O 5 A;Formula weight: #chem 369.28 #phys 369.0696 C;Correction formula: C 0 H 0 A;Correction weight: #chem 0.00 #phys 0.0000 C;Date: 11-Sep-1998 #structure_revision 11-Sep-1998 #text_change 23-Apr-1999 R;Ersfeld, K.; Wehland, J.; Plessmann, U.; Dodemont, H.; Gerke, V.; Weber, K. J. Cell Biol. 120, 725-732, 1993 A;Title: Characterization of the tubulin-tyrosine ligase. A;Reference number: A45443; MUID:93147125 A;Note: biosynthesis C;Generating enzyme: tubulin--tyrosine ligase (EC 6.3.2.25) C;Sequence code: E, Y A;Conditions: cross-link 2 F;/Cross-link: peptide (Glu-Tyr) (by tubulin-tyrosine ligase) >TX;AA0258 S-phycobiliviolin-L-cysteine N;Systematic name: (4S)-18-ethyl-3-[(1R)-1-(((2R)-2-amino-2-carboxy)ethylthio)ethyl]-1,4,5,19-tetrahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-biladiene-bc-8,12-dipropanoic acid C;Formula: C 36 H 44 N 5 O 7 S 1 A;Formula weight: #chem 690.85 #phys 690.2961 C;Correction formula: C 33 H 38 N 4 O 6 A;Correction weight: #chem 586.69 #phys 586.2791 C;Date: 30-Sep-1999 #structure_revision 30-Sep-1999 #text_change 30-Sep-1999 R;Bishop, J.E.; Rapoport, H.; Klotz, A.V.; Chan, C.F.; Glazer, A.N.; Fueglistaller, P.; Zuber, H. J. Am. Chem. Soc. 109, 875-881, 1987 A;Title: Chromopeptides from phycoerythrocyanin. Structure and linkage of the three bilin groups. A;Reference number: A30654 A;Note: spectrographic characterization; mass spectrographic and (1)H-NMR identification; peptide linkage R;Duerring, M.; Huber, R.; Bode, W.; Ruembeli, R.; Zuber, H. J. Mol. Biol. 211, 633-644, 1990 A;Title: Refined three-dimensional structure of phycoerythrocyanin from the cyanobacterium Mastigocladus laminosus at 2.7 A. A;Reference number: A30650; MUID:90172426 A;Note: X-ray crystallography, 2.7 angstroms C;Comment: The phycobiliviolins transmit violet. C;Sequence code: C A;Conditions: not combinable C;Keywords: chromoprotein; phycobiliviolin F;/Binding site: phycobiliviolin (Cys) (covalent) >TX;AA0259 phycoerythrobilin-bis-L-cysteine N;Systematic name: 3,18-bis-[1-((2-amino-2-carboxy)ethylthio)ethyl]-1,2,3,16,19-pentahydro-2,7,13,17-tetramethyl-1,19-dioxo-(21H,22H,24H)-biladiene-ab-8,12-dipropanoic acid C;Formula: C 39 H 48 N 6 O 8 S 2 A;Formula weight: #chem 792.99 #phys 792.2975 C;Correction formula: C 33 H 38 N 4 O 6 A;Correction weight: #chem 586.69 #phys 586.2791 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Chang, W.R.; Jiang, T.; Wan, Z.L.; Zhang, J.P.; Yang, Z.X.; Liang, D.C. J. Mol. Biol. 262, 721-731, 1996 A;Title: Crystal structure of R-phycoerythrin from Polysiphonia urceolata at 2.8 angstroms resolution. A;Reference number: A58825; MUID:97030708 R;Nagy, J.O.; Bishop, J.E.; Klotz, A.V.; Glazer, A.N.; Rapoport, H. J. Biol. Chem. 260, 4864-4868, 1985 A;Title: Bilin attachment sites in the alpha, beta, and gamma subunits of R-phycoerythrin. Structural studies on singly and doubly linked phycourobilins. A;Reference number: A22564; MUID:85182602 A;Note: mass spectrographic and (1)H-NMR identification C;Comment: There are additional chiral centers at C-2, C-3, and C-16. C;Comment: The phytochromobilins and phycoerythrobilins transmit red. C;Sequence code: C, C A;Conditions: cross-link 2; not combinable C;Keywords: chromoprotein; phytochromobilin F;/Binding site: phycoerythrobilin (Cys) (covalent) >TX;AA0260 phycourobilin-bis-L-cysteine N;Systematic name: 3,18-bis-[1-((2-amino-2-carboxy)ethylthio)ethyl]-1,4,16,19-tetrahydro-7,13,17-trimethyl-1,19-dioxo-(21H,22H,24H)-bilene-b-8,12-dipropanoic acid C;Formula: C 38 H 46 N 6 O 8 S 2 A;Formula weight: #chem 778.96 #phys 778.2819 C;Correction formula: C 32 H 36 N 4 O 6 S 0 A;Correction weight: #chem 572.67 #phys 572.2635 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 23-Apr-1999 R;Liang, D.C.; Jiang, T.; Chang, W.R. submitted to the Brookhaven Protein Data Bank, January 1996 A;Reference number: A67636; PDB:1LIA A;Contents: annotation; X-ray crystallography, 2.8 angstroms R;Chang, W.R.; Jiang, T.; Wan, Z.L.; Zhang, J.P.; Yang, Z.X.; Liang, D.C. J. Mol. Biol. 262, 721-731, 1996 A;Title: Crystal structure of R-phycoerythrin from Polysiphonia urceolata at 2.8 angstroms resolution. A;Reference number: A58825; MUID:97030708 A;Contents: annotation; X-ray crystallography, 2.8 angstroms C;Comment: There are additional chiral centers at C-4 and C-16. C;Sequence code: C, C A;Conditions: cross-link 2; not combinable C;Keywords: chromoprotein; phycourobilin F;/Binding site: phycourobilin (Cys) (covalent) >TX;AA0261 N-L-glutamyl-poly-L-glutamic acid C;Formula: C 10 H 14 N 2 O 6 + A;Formula weight: #chem 258.23 + #phys 258.0852 + C;Correction formula: C 5 H 7 N 1 O 3 + A;Correction weight: #chem 129.12 + #phys 129.0426 + C;Date: 11-Sep-1998 #structure_revision 11-Sep-1998 #text_change 28-Jan-2000 R;Hitz, H.; Schaefer, D.; Wittmann-Liebold, B. Eur. J. Biochem. 75, 497-512, 1977 A;Title: Determination of the complete amino-acid sequence of protein S6 from the wild-type and a mutant of Escherichia coli. A;Reference number: A02709; MUID:77225229 A;Note: five forms of the protein, which differ only in the number of carboxyl-terminal glutamic acid residues, were isolated and sequenced R;Kang, W.K.; Icho, T.; Isono, S.; Kitakawa, M.; Isono, K. Mol. Gen. Genet. 217, 281-288, 1989 A;Title: Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12. A;Reference number: S04774; MUID:89364710 C;Generating enzyme: ribosomal S6--glutamic acid ligase (EC 6.3.2.-) C;Sequence code: E A;Conditions: carboxyl-terminal F;/Modified site: polyglutamate amidated carboxyl end (Glu) F;/Modified site: polyglutamate amidated carboxyl end (Glu) (in mature form) >TX;AA0262 L-cysteine sulfinic acid N;Alternate names: 2-amino-3-sulfinopropanoic acid; 3-sulfinoalanine N;Systematic name: (R)-2-amino-2-carboxyethanesulfinic acid C;Formula: C 3 H 5 N 1 O 3 S 1 A;Formula weight: #chem 135.14 #phys 134.9990 C;Correction formula: C 0 H 0 O 2 A;Correction weight: #chem 32.00 #phys 31.9898 C;Date: 30-Jun-1995 #structure_revision 30-Jun-1995 #text_change 23-Apr-1999 R;Nagashima, S.; Nakasako, M.; Dohmae, N.; Tsujimura, M.; Takio, K.; Odaka, M.; Yohada, M.; Kamiya, N.; Endo, I. Nature Struct. Biol. 5, 347-351, 1998 A;Title: Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms. A;Reference number: A58907; MUID:98246406 A;Note: X-ray crystallography, 1.7 angstroms; mass spectroscopic identification C;Sequence code: C F;/Active site: Cys (cysteine sulfinic acid intermediate) F;/Modified site: cysteine sulfinic acid (Cys) >TX;AA0263 L-3',4',5'-trihydroxyphenylalanine N;Alternate names: L-3,4,5-TOPA N;Systematic name: (S)-2-amino-3-(3,4,5-trihydroxyphenyl)propanoic acid C;Formula: C 9 H 9 N 1 O 4 A;Formula weight: #chem 195.18 #phys 195.0532 C;Correction formula: C 0 H 0 O 2 A;Correction weight: #chem 32.00 #phys 31.9898 C;Date: 31-Mar-1995 #structure_revision 31-Mar-1995 #text_change 11-Jun-1999 R;Taylor, S.W.; Ross, M.M.; Waite, J.H. Arch. Biochem. Biophys. 324, 228-240, 1995 A;Title: Novel 3,4-di- and 3,4,5-trihydroxyphenylalanine-containing polypeptides from the blood cells of the ascidians Ascidia ceratodes and Molgula manhattensis. A;Reference number: S68325; MUID:96132650 A;Note: chromatographic and mass spectrographic detection; (1)H-NMR identification C;Sequence code: Y F;/Modified site: 3',4',5'-trihydroxyphenylalanine (Tyr) >TX;AA0264 O-(sn-1-glycerophosphoryl)-L-serine N;Alternate names: alpha-glycerophosphoryl serine; O3-(sn-1-glycerophosphoryl)-L-serine; O3-2,3-dihydroxypropyl hydrogenphosphate-L-serine ester; O3-L-serine glyceryl-1-phosphodiester N;Systematic name: (R)-2-amino-3-[(S)-2,3-dihydroxypropyl]phosphonoxypropanoic acid A;Cross-references: CAS:26289-09-8 C;Formula: C 6 H 12 N 1 O 7 P 1 A;Formula weight: #chem 241.14 #phys 241.0351 C;Correction formula: C 3 H 7 O 5 P 1 A;Correction weight: #chem 154.06 #phys 154.0031 C;Date: 04-Dec-1998 #structure_revision 04-Dec-1998 #text_change 14-Jul-2000 R;Stimson, E.; Virji, M.; Barker, S.; Panico, M.; Blench, I.; Saunders, J.; Payne, G.; Moxon, E.R.; Dell, A.; Morris, H.R. Biochem. J. 316, 29-33, 1996 A;Title: Discovery of a novel protein modification: alpha-glycerophosphate is a substituent of meningococcal pilin. A;Reference number: S68270; MUID:96235168 A;Note: mass spectrographic identification C;Comment: The stereochemistry of the glycerol phosphate has not been determined. The sn-1 form is assumed. C;Sequence code: S C;Keywords: phosphoprotein F;/Binding site: sn-1-glycerolphosphate (Ser) (covalent) >TX;AA0265 1-thioglycine N;Alternate names: aminoethanethioic acid; aminoethanethiolic acid; aminothioacetic acid N;Systematic name: aminoethanethionic acid A;Cross-references: CAS:758-10-1 C;Formula: C 2 H 3 N 1 S 1 A;Formula weight: #chem 73.12 #phys 72.9986 C;Correction formula: C 0 H 0 O -1 S 1 A;Correction weight: #chem 16.07 #phys 15.9772 C;Date: 30-Apr-1999 #structure_revision 30-Apr-1999 #text_change 28-Jan-2000 R;Ermler, U.; Grabarse, W.; Shima, S.; Goubeaud, M.; Thauer, R.K. Science 278, 1457-1462, 1997 A;Title: Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation. A;Reference number: A58866; MUID:98035783 A;Note: X-ray crystallography, 1.45 angstroms C;Comment: As a peptide this may exist predominantly in the iminyl-thiol [-C(SH)=NH-] tautomeric form. C;Comment: See also RESID:AA0206. C;Sequence code: G F;/Modified site: 1-thioglycine (Gly) F;/Modified site: thiocarboxylic carboxyl end (Gly) F;/Modified site: thiocarboxylic carboxyl end (Gly) (in mature form) >TX;AA0266 heme P460-bis-L-cysteine-L-tyrosine N;Alternate names: biscysteinyl-tyrosinyl-heme N;Systematic name: 7,12-bis[1-((2R)-2-amino-2-carboxyethyl)thioethyl]-10-[1-2-hydroxy-5-((2S)-2-amino-2-carboxyethyl)phenyl]-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate C;Formula: C 49 H 49 Fe 1 N 7 O 8 S 2 A;Formula weight: #chem 983.96 #phys 983.2433 C;Correction formula: C 34 H 30 Fe 1 N 4 O 4 A;Correction weight: #chem 614.49 #phys 614.1616 C;Date: 30-Apr-1999 #structure_revision 30-Apr-1999 #text_change 11-Jun-1999 R;Arciero, D.M.; Hooper, A.B. J. Biol. Chem. 268, 14645-14654, 1993 A;Title: Hydroxylamine oxidoreductase from Nitrosomonas europaea is a multimer of an octa-heme subunit. A;Reference number: A55000; MUID:93315429 R;Tanaka, N.; Igarashi, N.; Moriyama, H. submitted to the Brookhaven Protein Data Bank, March 1997 A;Reference number: A73171; PDB:1FGJ A;Note: X-ray crystallography, 2.8 angstroms R;Igarashi, N.; Moriyama, H.; Fujiwara, T.; Fukumori, Y.; Tanaka, N. Nature Struct. Biol. 4, 276-284, 1997 A;Title: The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea. A;Reference number: A59035; MUID:97249290 A;Note: X-ray crystallography, 2.8 angstroms C;Sequence code: C; C; Y A;Conditions: cross-link 3 C;Keywords: chromoprotein; heme; iron; metalloprotein F;/Cross-link: heme P460 (Cys-Cys-Tyr) F;/Cross-link: heme P460 (Cys-Cys) (interchain to Tyr ...) F;/Cross-link: heme P460 (Tyr) (interchain to Cys ... and Cys ...) >TX;AA0267 O-(phospho-5'-adenosine)-L-threonine N;Alternate names: 5'-adenylic-O3-L-threonine; beta-5'-adenylic-L-threonine; L-threonine monoanhydride with 5'-adenylic acid; O(gamma)-5'-adenylic-L-threonine; O3-(phospho-5'-adenosine)-L-threonine; O3-L-threonine 5'-adenosine phosphodiester N;Systematic name: (2S,3R)-2-amino-3-(5'-adenosine phosphonoxy)butanoic acid C;Formula: C 14 H 19 N 6 O 8 P 1 A;Formula weight: #chem 430.32 #phys 430.1002 C;Correction formula: C 10 H 12 N 5 O 6 P 1 A;Correction weight: #chem 329.21 #phys 329.0525 C;Date: 30-Apr-1999 #structure_revision 30-Apr-1999 #text_change 14-Jul-2000 R;Culp, J.S.; Blytt, H.J.; Hermodson, M.; Butler, L.G. J. Biol. Chem. 260, 8320-8324, 1985 A;Title: Amino acid sequence of the active site peptide of bovine intestinal 5'-nucleotide phosphodiesterase and identification of the active site residue as threonine. A;Reference number: A25274; MUID:85234541 A;Note: radiolabeling R;Stefan, C.; Stalmans, W.; Bollen, M. Eur. J. Biochem. 241, 338-342, 1996 A;Title: Threonine autophosphorylation and nucleotidylation of the hepatic membrane protein PC-1. A;Reference number: A58950; MUID:97075001 A;Note: radiolabeling; linkage analysis C;Sequence code: T A;Conditions: combinable C;Keywords: phosphoprotein F;/Binding site: AMP (Thr) (covalent) F;/Active site: Thr (covalent AMP-binding) >TX;AA0268 tris-L-cysteinyl-L-cysteine persulfido-bis-L-glutamato-L-histidino tetrairon disulfide trioxide N;Alternate names: 4Fe-2S-3O cluster; hybrid four iron cluster 2; prismane iron-sulfur cofactor (misnomer) N;Systematic name: mu-1:2kappaO-oxido-mu-1:3kappaO-oxido-mu-2:4kappaO-oxido-mu-3:4kappaS-sulfido-mu3-2:3:4kappaS-sulfido-S-cysteinyl-N1'-histidino-glutamato 1-iron-S5-cysteine persulfido-glutamato 2-iron-3,4-bis-(S-cysteinyl iron) C;Formula: C 28 H 34 Fe 4 N 9 O 14 S 7 A;Formula weight: #chem 1168.49 #phys 1167.7668 C;Correction formula: C 0 H -7 Fe 4 O 3 S 3 A;Correction weight: #chem 360.53 #phys 360.5859 C;Date: 07-May-1999 #structure_revision 07-May-1999 #text_change 11-Jun-1999 R;Arendsen, A.F.; Hadden, J.; Card, G.; McAlpine, A.S.; Bailey, S.; Zaitsev, V.; Duke, E.H.M.; Lindley, P.F.; Kroeckel, M.; Trautwein, A.X.; Feiters, M.C.; Charnock, J.M.; Garner, C.D.; Marritt, S.J.; Thomson, A.J.; Kooter, I.M.; Johnson, M.K.; van den Berg, W.A.M.; van Dongen, W.M.A.M.; Hagen, W.R. J. Biol. Inorg. Chem. 3, 81-95, 1998 A;Title: The "prismane" protein resolved: X-ray structure at 1.7 angstroms and multiple spectroscopy of two novel 4Fe clusters. A;Reference number: A58942 A;Note: X-ray crystallography, 1.7 angstroms; EPR, Moessbauer, and MCD spectrographic analysis C;Comment: The name "prismane" for this hybrid cluster is a now known to be a misnomer. The structure determined by X-ray consists of a four iron cluster with mixed ligands. One of the oxygen ligands, designated here as the mu-1:3-oxido, is actually partially occupied by an unidentified atom and is probably the reactive center. C;Sequence code: H, E, C, C, C, C, E A;Conditions: cross-link 7; secondary to RESID:AA0269 C;Keywords: 4Fe-2S-3O; iron-sulfur protein; metalloprotein F;/Binding site: 4Fe-2S-3O cluster (His, Glu, Cys, Cys, Cys, Cys, Glu) (covalent) >TX;AA0269 L-cysteine persulfide N;Alternate names: 2-amino-3-disufanylpropanoic acid; 2-amino-3-hydropersulfidopropanoic acid; 2-amino-3-persulfhydrylpropanoic acid N;Systematic name: (R)-2-amino-3-hydrodisulfidopropanoic acid C;Formula: C 3 H 5 N 1 O 1 S 2 A;Formula weight: #chem 135.21 #phys 134.9813 C;Correction formula: C 0 H 0 S 1 A;Correction weight: #chem 32.07 #phys 31.9721 C;Date: 14-May-1999 #structure_revision 14-May-1999 #text_change 18-Jun-1999 R;Branzoli, U.; Massey, V. J. Biol. Chem. 249, 4346-4349, 1974 A;Title: Evidence for an active site persulfide residue in rabbit liver aldehyde oxidase. A;Reference number: A58961; MUID:74277388 A;Note: investigation of persulfide group chemistry R;Zheng, L.; White, R.H.; Cash, V.L.; Dean, D.R. Biochemistry 33, 4714-4720, 1994 A;Title: Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product. A;Reference number: A54246; MUID:94213847 A;Note: chemical detection of persulfide group R;Arendsen, A.F.; Hadden, J.; Card, G.; McAlpine, A.S.; Bailey, S.; Zaitsev, V.; Duke, E.H.M.; Lindley, P.F.; Kroeckel, M.; Trautwein, A.X.; Feiters, M.C.; Charnock, J.M.; Garner, C.D.; Marritt, S.J.; Thomson, A.J.; Kooter, I.M.; Johnson, M.K.; van den Berg, W.A.M.; van Dongen, W.M.A.M.; Hagen, W.R. J. Biol. Inorg. Chem. 3, 81-95, 1998 A;Title: The "prismane" protein resolved: X-ray structure at 1.7 angstroms and multiple spectroscopy of two novel 4Fe clusters. A;Reference number: A58942 A;Note: X-ray crystallography, 1.7 angstroms; EPR, Moessbauer, and MCD spectrographic analysis C;Comment: See also RESID:AA0101 and RESID:AA0268. C;Sequence code: C F;/Modified site: cysteine persulfide (Cys) F;/Active site: Cys (cysteine persulfide intermediate) >TX;AA0270 3'-(1'-L-histidyl)-L-tyrosine N;Alternate names: C3'-(N1'-histidyl)tyrosine N;Systematic name: (2S)-2-amino-3-[1-(1-((S)-2-amino-2-carboxyethyl)-4-hydoxyphen-3-yl)imidazol-4-yl]propanoic acid C;Formula: C 15 H 16 N 4 O 3 A;Formula weight: #chem 300.32 #phys 300.1222 C;Correction formula: C 0 H -2 A;Correction weight: #chem -2.02 #phys -2.0157 C;Date: 14-May-1999 #structure_revision 14-May-1999 #text_change 14-May-1999 R;Buse, G.; Soulimane, T.; Dewor, M.; Meyer, H.E.; Blueggel, M. Protein Sci. 8, 985-990, 1999 A;Title: Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase. A;Reference number: A58960 A;Note: mass spectrographic and chemical characterization C;Comment: This modification is different from the modification 3-(3'-L-histidyl)-L-tyrosine, see RESID:AA0250. C;Sequence code: H, Y A;Conditions: cross-link 2 F;/Cross-link: 1'-histidyl-3'-tyrosine (His-Tyr) F;/Cross-link: 1'-histidyl-3'-tyrosine (Tyr-His) >TX;AA0271 heme P460-bis-L-cysteine-L-lysine N;Alternate names: biscysteinyl-lysinyl-heme C;Formula: C 46 H 52 Fe 1 N 8 O 7 S 2 A;Formula weight: #chem 948.96 #phys 948.2750 C;Correction formula: C 34 H 30 Fe 1 N 4 O 4 A;Correction weight: #chem 614.49 #phys 614.1616 C;Date: 30-Sep-1999 #structure_revision 30-Sep-1999 #text_change 24-Nov-1999 R;Arciero, D.M.; Hooper, A.B. FEBS Lett. 410, 457-460, 1997 A;Title: Evidence for a crosslink between c-heme and a lysine residue in cytochrome P460 of Nitrosomonas europaea. A;Reference number: A59063; MUID:97379360 A;Note: spectrographic characterization; chemical characterization C;Comment: The structure of the covalent attachment of heme to lysine is not known. See RESID:AA0266. C;Sequence code: C; C; K A;Conditions: cross-link 3; not combinable C;Keywords: chromoprotein; heme; iron; metalloprotein F;/Binding site: heme P460 (Lys, Cys, Cys) (covalent) >TX;AA0272 5-methyl-L-arginine N;Alternate names: delta-methylarginine N;Systematic name: (2S,5S)-2-amino-5-guanidinohexanoic acid C;Formula: C 7 H 14 N 4 O 1 A;Formula weight: #chem 170.22 #phys 170.1168 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Date: 30-Sep-1999 #structure_revision 30-Sep-1999 #text_change 30-Sep-1999 R;Ermler, U.; Grabarse, W.; Shima, S.; Goubeaud, M.; Thauer, R.K. Science 278, 1457-1462, 1997 A;Title: Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation. A;Reference number: A58866; MUID:98035783 A;Note: X-ray crystallography, 1.45 angstroms C;Comment: This modification should not be confused with delta-N-methylarginine (or 2-amino-5-[(aminoiminomethyl)-methyl-amino]pentanoic acid) which has been found in proteins but not sequenced. C;Comment: In methyl-coenzyme M reductase the arginine 5-methyl group is derived from S-adenosyl-methionine and is not produced as a side reaction of the enzyme. C;Sequence code: R C;Keywords: methylated amino acid F;/Modified site: 5-methylarginine (Arg) >TX;AA0273 2-methyl-L-glutamine N;Alternate names: alpha-methylglutamine; 2-methylglutamine N;Systematic name: (S)-2-amino-2-methylpentanediamic acid A;Cross-references: CAS:4247-16-9 C;Formula: C 6 H 10 N 2 O 2 A;Formula weight: #chem 142.16 #phys 142.0742 C;Correction formula: C 1 H 2 A;Correction weight: #chem 14.03 #phys 14.0157 C;Date: 30-Sep-1999 #structure_revision 30-Sep-1999 #text_change 30-Sep-1999 R;Ermler, U.; Grabarse, W.; Shima, S.; Goubeaud, M.; Thauer, R.K. Science 278, 1457-1462, 1997 A;Title: Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation. A;Reference number: A58866; MUID:98035783 A;Note: X-ray crystallography, 1.45 angstroms C;Comment: In methyl-coenzyme M reductase the glutamine 2-methyl group is derived from S-adenosyl-methionine and is not produced as a side reaction of the enzyme. C;Sequence code: Q C;Keywords: methylated amino acid F;/Modified site: 2-methylglutamine (Gln) >TX;AA0274 N-pyruvic acid 2-iminyl-L-cysteine N;Systematic name: (R)-2-(1-carboxy-2-mercaptoethanimino)propanoic acid C;Formula: C 6 H 8 N 1 O 3 S 1 A;Formula weight: #chem 174.20 #phys 174.0225 C;Correction formula: C 3 H 3 O 2 A;Correction weight: #chem 71.06 #phys 71.0133 C;Date: 30-Sep-1999 #structure_revision 30-Sep-1999 #text_change 21-Jan-2000 R;Rose, K.; Simona, M.G.; Savoy, L.A.; Regamey, P.O.; Green, B.N.; Clore, G.M.; Gronenborn, A.M.; Wingfield, P.T. J. Biol. Chem. 267, 19101-19106, 1992 A;Title: Pyruvic acid is attached through its central carbon atom to the amino terminus of the recombinant DNA-derived DNA-binding protein Ner of bacteriophage Mu. A;Reference number: A58979; MUID:92406846 A;Note: mass spectrographic and chemical characterization; (1)H-NMR identification; 2,4-dinitrophenylhydrazine used for detection C;Comment: The cysteine sulfhydryl may cyclize with the imine to form 2-methyl-thiazolidine-2,4-dicarboxylic acid [CAS:152574-58-8]. C;Sequence code: C A;Conditions: amino-terminal C;Keywords: blocked amino end F;/Modified site: pyruvate 2-iminyl amino end (Cys) F;/Modified site: pyruvate 2-iminyl amino end (Cys) (in mature form) >TX;AA0275 N-pyruvic acid 2-iminyl-L-valine N;Systematic name: (S)-2-(1-carboxy-2-methylpropanimino)propanoic acid C;Formula: C 8 H 12 N 1 O 3 A;Formula weight: #chem 170.19 #phys 170.0817 C;Correction formula: C 3 H 3 O 2 A;Correction weight: #chem 71.06 #phys 71.0133 C;Date: 30-Sep-1999 #structure_revision 30-Sep-1999 #text_change 21-Jan-2000 R;Prome, D.; Blouquit, Y.; Ponthus, C.; Prome, J.C.; Rosa, J. J. Biol. Chem. 266, 13050-13054, 1991 A;Title: Structure of the human adult hemoglobin minor fraction A-1b by electrospray and secondary ion mass spectrometry. Pyruvic acid as amino-terminal blocking group. A;Reference number: A39865; MUID:91302324 C;Sequence code: V A;Conditions: amino-terminal C;Keywords: blocked amino end F;/Modified site: pyruvate 2-iminyl amino end (Val) F;/Modified site: pyruvate 2-iminyl amino end (Val) (in mature form) >TX;AA0276 heme-L-histidine N;Alternate names: histidyl heme C;Formula: C 40 H 39 Fe 1 N 7 O 5 A;Formula weight: #chem 753.65 #phys 753.2362 C;Correction formula: C 34 H 32 Fe 1 N 4 O 4 A;Correction weight: #chem 616.51 #phys 616.1773 C;Date: 30-Sep-1999 #structure_revision 30-Sep-1999 #text_change 30-Sep-1999 R;Schulz, H.; Hennecke, H.; Thoeny-Meyer, L. Science 281, 1197-1200, 1998 A;Title: Prototype of a heme chaperone essential for cytochrome c maturation. A;Reference number: A58862; MUID:98378584 A;Note: mass spectrographic identification C;Comment: The structure of the covalent attachment of heme to histidine is not known. C;Sequence code: H A;Conditions: not combinable C;Keywords: chromoprotein; heme; iron; metalloprotein F;/Binding site: heme (His) (covalent) >TX;AA0277 S-selenyl-L-cysteine N;Alternate names: 2-amino-3-hydroselenylsulfidopropanoic acid; 2-amino-3-hydroselenylthiopropanoic acid; 2-amino-3-selanylsulfanylpropanoic acid; S-selanylcysteine N;Systematic name: (R)-2-amino-3-hydroselenosulfidopropanoic acid C;Formula: C 3 H 5 N 1 O 1 S 1 Se 1 A;Formula weight: #chem 182.11 #phys 182.9257 C;Correction formula: C 0 H 0 Se 1 A;Correction weight: #chem 78.96 #phys 79.9165 C;Date: 24-Nov-1999 #structure_revision 24-Nov-1999 #text_change 24-Nov-1999 R;Dobbek, H.; Gremer, L.; Meyer, O.; Huber, R. Proc. Natl. Acad. Sci. U.S.A. 96, 8884-8889, 1999 A;Title: Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine. A;Reference number: A59142; MUID:99362680 A;Note: X-ray crystallography, 2.2 angstroms C;Sequence code: C C;Keywords: selenium F;/Modified site: S-selenylcysteine (Cys) F;/Active site: Cys (S-selenylcysteine intermediate) >TX;AA0278 N6-methyl-N6-poly(N-methyl-propylamine)-L-lysine N;Alternate names: N6-oligo-N-methyl-propylamine-N6-methyl-lysine; silaffin polycationic lysine derivative N;Systematic name: (S)-2-amino-N6-methyl-N6-poly(N-methyl-propylamine)aminohexanoic acid C;Formula: C 25 H 68 N 8 O 1 + A;Formula weight: #chem 496.87 + #phys 496.5516 + C;Correction formula: C 18 H 54 N 6 + A;Correction weight: #chem 354.67 + #phys 354.4410 + C;Date: 24-Nov-1999 #structure_revision 24-Nov-1999 #text_change 24-Nov-1999 R;Kroeger, N.; Deutzmann, R.; Sumper, M. Science 286, 1129-1132, 1999 A;Title: Polycationic peptides from diatom biosilica that direct silica nanosphere formation. A;Reference number: A59141; MUID:20018323 A;Note: chromatographic, mass spectrographic and (1)H-NMR identification C;Comment: In silaffin from the diatom Cylindrotheca fusiformis there are five to eleven N-methyl-propylamine monomeric units on each lysine. Six are shown. C;Sequence code: K C;Keywords: methylated amino acid F;/Modified site: N6-methyl-N6-poly(N-methyl-propylamine)lysine (Lys) >TX;AA0279 hemediol-L-aspartyl ester-L-glutamyl ester N;Alternate names: peroxidase heme cofactor N;Systematic name: 13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-7,12-diethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate C;Formula: C 43 H 40 Fe 1 N 6 O 10 A;Formula weight: #chem 856.68 #phys 856.2155 C;Correction formula: C 34 H 28 Fe 1 N 4 O 4 A;Correction weight: #chem 612.47 #phys 612.1460 C;Date: 24-Nov-1999 #structure_revision 24-Nov-1999 #text_change 24-Nov-1999 R;Kooter, I.M.; Moguilevsky, N.; Bollen, A.; Sijtsema, N.M.; Otto, C.; Dekker, HL.; Wever, R. Eur. J. Biochem. 264, 211-217, 1999 A;Title: Characterization of the Asp94 and Glu242 mutants in myeloperoxidase, the residues linking the heme group via ester bonds. A;Reference number: A59081; MUID:99376860 A;Note: directed mutation analysis; activity comparison C;Comment: For structural studies of the myeloperoxidase heme cofactor, see RESID:AA0280. C;Sequence code: D; E A;Conditions: cross-link 2; not combinable C;Keywords: chromoprotein; heme; iron; metalloprotein F;/Binding site: hemediol (Asp, Glu) (covalent) >TX;AA0280 hemediol-L-aspartyl ester-L-glutamyl ester-L-methionine sulfonium N;Alternate names: myeloperoxidase heme cofactor N;Systematic name: 13-[(S)-(4-amino-4-carboxy)butanoyloxymethyl]-3-[(S)-(3-amino-3-carboxy)propanoyloxymethyl]-12-[(S)-(3-amino-3-carboxy)propylsulfoniumethyl]-7-ethenyl-8,17-dimethyl-21H,23H-porphine-2,18-bis(2-carboxyethyl)-N21,N22,N23,N24]-ferrate C;Formula: C 48 H 50 Fe 1 N 7 O 11 S 1 A;Formula weight: #chem 988.89 #phys 988.2638 C;Correction formula: C 34 H 29 Fe 1 N 4 O 4 A;Correction weight: #chem 613.48 #phys 613.1538 C;Date: 24-Nov-1999 #structure_revision 24-Nov-1999 #text_change 24-Nov-1999 R;Kooter, I.M.; Moguilevsky, N.; Bollen, A.; van der Veen, L.A.; Otto, C.; Dekker, H.L.; Wever, R. J. Biol. Chem. 274, 26794-26802, 1999 A;Title: The sulfonium ion linkage in myeloperoxidase. Direct spectroscopic detection by and effect of mutation. A;Reference number: A59083; MUID:99410411 A;Note: radiolabeling; spectrographic characterization R;Kooter, I.M.; Moguilevsky, N.; Bollen, A.; Sijtsema, N.M.; Otto, C.; Dekker, HL.; Wever, R. Eur. J. Biochem. 264, 211-217, 1999 A;Title: Characterization of the Asp94 and Glu242 mutants in myeloperoxidase, the residues linking the heme group via ester bonds. A;Reference number: A59081; MUID:99376860 A;Note: directed mutation analysis R;Fenna, R.E.; Zeng, J.; Davey, C. submitted to the Brookhaven Protein Data Bank, June 1995 A;Reference number: A66127; PDB:1MHL A;Note: X-ray crystallography, 2.25 angstroms R;Fenna, R.; Zeng, J.; Davey, C. Arch. Biochem. Biophys. 316, 653-656, 1995 A;Title: Structure of the green heme in myeloperoxidase. A;Reference number: A59082; MUID:95142692 A;Note: X-ray crystallography, 2.25 angstroms R;Fenna, R.E.; Zeng, J. submitted to the Brookhaven Protein Data Bank, April 1992 A;Reference number: A51882; PDB:1MYP A;Note: X-ray crystallography, 3.0 angstroms R;Zeng, J.; Fenna, R.E. J. Mol. Biol. 226, 185-207, 1992 A;Title: X-ray crystal structure of canine myeloperoxidase at 3 Angstroms resolution. A;Reference number: A57940; MUID:92318261 A;Note: X-ray crystallography, 3.0 angstroms C;Sequence code: D; E; M A;Conditions: cross-link 3; not combinable C;Keywords: chromoprotein; heme; iron; metalloprotein F;/Binding site: hemediol (Asp, Glu, Met) (covalent) >TX;AA0281 L-cysteinyl molybdopterin guanine dinucleotide N;Systematic name: 8-amino-2-(2-amino-2-carboxyethyl)thio-1a,3a,4,5a,6,9,10,11,11a-nonahydro-4-(trihydrogen diphosphate 5'-ester with guanosine)methyl-2,2,10-trioxo-pteridino[6,7-5,6]pyrano[3,4-4,3][1,2,5]molybdadithiolene C;Formula: C 23 H 28 Mo 1 N 11 O 16 P 2 S 3 A;Formula weight: #chem 968.63 #phys 969.9407 C;Correction formula: C 20 H 23 Mo 1 N 10 O 15 P 2 S 2 A;Correction weight: #chem 865.48 #phys 866.9315 C;Date: 03-Dec-1999 #structure_revision 03-Dec-1999 #text_change 07-Dec-1999 C;Comment: This modification is predicted for enzymes homologous to formate dehydrogenase in certain organisms where the position corresponding to selenocysteine instead encodes cysteine. It is possible either that the cysteine coordinates the molybdenum, that the cysteine is modified to selenocysteine (see RESID:AA0022), or that the cysteine is modified to selenylcysteine (see RESID:AA0277). C;Sequence code: C C;Keywords: metalloprotein; molybdenum; molybdopterin; phosphoprotein F;/Binding site: molybdopterin guanine dinucleotide (Cys) (covalent) >TX;AA0282 trans-2,3-cis-3,4-dihydroxy-L-proline N;Alternate names: 2-alpha-3-beta-4-beta-3,4-dihydroxyproline N;Systematic name: (2S,3S,4S)-3,4-dihydroxy-2-pyrrolidinecarboxylic acid A;Cross-references: CAS:95341-64-3 C;Formula: C 5 H 7 N 1 O 3 A;Formula weight: #chem 129.12 #phys 129.0426 C;Correction formula: C 0 H 0 O 2 A;Correction weight: #chem 32.00 #phys 31.9898 C;Date: 28-Jan-2000 #structure_revision 28-Jan-2000 #text_change 28-Jan-2000 R;Taylor, S.W.; Waite, J.H.; Ross, M.M.; Shabanowitz, J.; Hunt, D.F. J. Am. Chem. Soc. 116, 10803-10804, 1994 A;Title: trans-2,3-cis-3,4-dihydroxyproline, a new naturally occurring amino acid, is the sixth residue in the tandemly repeated consensus decapeptides of an adhesive protein from Mytilus edulis. A;Reference number: A59158 A;Note: chromatographic detection; mass spectrographic and (1)H-NMR identification C;Sequence code: P C;Keywords: hydroxyproline F;/Modified site: trans-2,3-cis-3,4-dihydroxyproline (Pro) >TX;AA0283 pyrroloquinoline quinone N;Alternate names: methoxatin; 2,4,6-tricarboxylic-pyrrolo[2,3-5,6]quinoline 8,9-quinone N;Systematic name: 2,4,6-tricarboxylic-8,9-dihydro-8,9-dioxo-pyrrolo[2,3-5,6]quinoline A;Cross-references: CAS:72909-34-3 C;Formula: C 14 H 6 N 2 O 8 A;Formula weight: #chem 330.21 #phys 330.0124 C;Correction formula: C 0 H -10 O 3 A;Correction weight: #chem 37.92 #phys 37.9065 C;Date: 18-Feb-2000 #structure_revision 18-Feb-2000 #text_change 18-Feb-2000 R;Goosen, N.; Huinen, R.G.; van de Putte, P. J. Bacteriol. 174, 1426-1427, 1992 A;Title: A 24-amino-acid polypeptide is essential for the biosynthesis of the coenzyme pyrrolo-quinoline-quinone. A;Reference number: A59183; MUID:92138642 A;Note: mutagenic evidence that specific glutamic acid and tyrosine residues of the pqqA protein were utilized R;Velterop, J.S.; Sellink, E.; Meulenberg, J.J.; David, S.; Bulder, I.; Postma, P.W. J. Bacteriol. 177, 5088-5098, 1995 A;Title: Synthesis of pyrroloquinoline quinone in vivo and in vitro and detection of an intermediate in the biosynthetic pathway. A;Reference number: A59181; MUID:95394815 A;Note: evidence that the pqqA protein was the origin of pyrroloquinoline quinone C;Comment: In some prokaryotes, the pqqA protein is the origin of pyrroloquinoline quinone. In other organisms the endogenous source, if there is one, has not been established. C;Sequence code: E; Y A;Conditions: cross-link 2 C;Keywords: quinoprotein F;/Cross-link: pyrroloquinoline quinone (Glu, Tyr) >TX;AA0284 tris-L-cysteinyl-L-N1'-histidino tetrairon tetrasulfide N;Systematic name: tetra-mu3-sulfidotris(S-cysteinyliron)(N1'-histidinoiron) C;Formula: C 15 H 18 Fe 4 N 6 O 4 S 7 A;Formula weight: #chem 794.20 #phys 793.6832 C;Correction formula: C 0 H -4 Fe 4 S 4 A;Correction weight: #chem 347.62 #phys 347.5967 C;Date: 17-Mar-2000 #structure_revision 17-Mar-2000 #text_change 17-Mar-2000 R;Peters, J.W.; Lanzilotta, W.N.; Lemon, B.J.; Seefeldt, L.C. Science 282, 1853-1858, 1998 A;Title: X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution. A;Reference number: A59203; MUID:99055388 A;Note: X-ray crystallography, 1.8 angstroms C;Sequence code: C, C, C, H A;Conditions: cross-link 4; not combinable C;Keywords: 4Fe-4S; iron-sulfur protein; metalloprotein F;/Binding site: 4Fe-4S cluster (His, Cys, Cys, Cys) (covalent) (type N1) >TX;AA0285 tris-L-cysteinyl-L-N3'-histidino tetrairon tetrasulfide N;Systematic name: tetra-mu3-sulfidotris(S-cysteinyliron)(N3'-histidinoiron) C;Formula: C 15 H 18 Fe 4 N 6 O 4 S 7 A;Formula weight: #chem 794.20 #phys 793.6832 C;Correction formula: C 0 H -4 Fe 4 S 4 A;Correction weight: #chem 347.62 #phys 347.5967 C;Date: 17-Mar-2000 #structure_revision 17-Mar-2000 #text_change 17-Mar-2000 R;Volbeda, A.; Charon, M.H.; Piras, C.; Hatchikian, E.C.; Frey, M.; Fontecilla-Camps, J.C. Nature 373, 580-587, 1995 A;Title: Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas. A;Reference number: A57765; MUID:95157629 A;Note: X-ray crystallography, 2.85 angstroms R;Volbeda, A.; Frey, M.; Fontecilla-Camps, J.C. submitted to the Brookhaven Protein Data Bank, March 1996 A;Reference number: A65633; PDB:1FRV A;Note: annotation; X-ray crystallography, 2.85 angstroms C;Sequence code: C, C, C, H A;Conditions: cross-link 4; not combinable C;Keywords: 4Fe-4S; iron-sulfur protein; metalloprotein F;/Binding site: 4Fe-4S cluster (His, Cys, Cys, Cys) (covalent) (type N3) >TX;AA0286 tris-L-cysteinyl-L-aspartato tetrairon tetrasulfide N;Systematic name: tetra-mu3-sulfidotris(S-cysteinyliron)(O4-aspartatoiron) C;Formula: C 13 H 16 Fe 4 N 4 O 6 S 7 A;Formula weight: #chem 772.15 #phys 771.6512 C;Correction formula: C 0 H -4 Fe 4 S 4 A;Correction weight: #chem 347.62 #phys 347.5967 C;Date: 17-Mar-2000 #structure_revision 17-Mar-2000 #text_change 17-Mar-2000 R;Gorst, C.M.; Yeh, Y.H.; Teng, Q.; Calzolai, L.; Zhou, Z.H.; Adams, M.W.W.; La Mar, G.N. Biochemistry 34, 600-610, 1995 A;Title: [1]H NMR investigation of the paramagnetic cluster environment in Pyrococcus furiosus three-iron ferredoxin: sequence-specific assignment of ligated cysteines independent of tertiary structure. A;Reference number: A56250; MUID:95119047 A;Note: conformation, binding site, and disulfide bond assignments by (1)H-NMR R;Zhou, Z.H.; Adams, M.W.W. Biochemistry 36, 10892-10900, 1997 A;Title: Site-directed mutations of the 4Fe-ferredoxin from the hyperthermophilic archaeon Pyrococcus furiosus: role of the cluster-coordinating aspartate in physiological electron transfer reactions. A;Reference number: A59198; MUID:97428217 A;Note: demonstration of aspartate binding C;Sequence code: C, C, C, D A;Conditions: cross-link 4; not combinable C;Keywords: 4Fe-4S; iron-sulfur protein; metalloprotein F;/Binding site: 4Fe-4S cluster (Cys, Asp, Cys, Cys) (covalent) >TX;AA0287 N6-pyruvic acid 2-iminyl-L-lysine N;Systematic name: (S)-2-amino-6-(1-carboxy-ethylimino)hexanoic acid C;Formula: C 9 H 14 N 2 O 3 A;Formula weight: #chem 198.22 #phys 198.1004 C;Correction formula: C 3 H 2 O 2 A;Correction weight: #chem 70.05 #phys 70.0055 C;Date: 17-Mar-2000 #structure_revision 17-Mar-2000 #text_change 17-Mar-2000 R;Laber, B.; Gomis-Rueth, F.X.; Romao, M.J.; Huber, R. Biochem. J. 288, 691-695, 1992 A;Title: Escherichia coli dihydrodipicolinate synthase. Identification of the active site and crystallization. A;Reference number: S27165; MUID:93098829 A;Note: evidence for covalent intermediate R;Mirwaldt, C.; Korndoerfer, I.; Huber, R. J. Mol. Biol. 246, 227-239, 1995 A;Title: The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 angstroms resolution. A;Reference number: A59217; MUID:95156485 A;Note: X-ray diffraction, 2.5 angstroms R;Mirwaldt, C.; Korndoerfer, I.; Huber, R. submitted to the Brookhaven Protein Data Bank, February 1995 A;Reference number: A65412; PDB:1DHP A;Note: X-ray diffraction, 2.5 angstroms R;Lawrence, M.C.; Barbosa, J.A.R.G.; Smith, B.J.; Hall, N.E.; Pilling, P.A.; Ooi, H.C.; Marcuccio, S.M. submitted to the Brookhaven Protein Data Bank, July 1996 A;Reference number: A68074; PDB:1FDY A;Note: X-ray diffraction, 2.45 angstroms R;Lawrence, M.C.; Barbosa, J.A.R.G.; Smith, B.J.; Hall, N.E.; Pilling, P.A.; Ooi, H.C.; Marcuccio, S.M. J. Mol. Biol. 266, 381-399, 1997 A;Title: Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase. A;Reference number: A59220; MUID:9799395 A;Note: X-ray diffraction, 2.45 angstroms C;Sequence code: K F;/Active site: Lys (covalent pyruvate-binding) F;/Modified site: pyruvate 2-iminyl (Lys) >TX;AA0288 tris-L-cysteinyl-L-serinyl tetrairon tetrasulfide N;Systematic name: tetra-mu3-sulfidotris(S-cysteinyliron)(O3-serinyliron) C;Formula: C 12 H 16 Fe 4 N 4 O 5 S 7 A;Formula weight: #chem 744.14 #phys 743.6563 C;Correction formula: C 0 H -4 Fe 4 S 4 A;Correction weight: #chem 347.62 #phys 347.5967 C;Date: 20-Apr-2000 #structure_revision 20-Apr-2000 #text_change 20-Apr-2000 C;Comment: The occurrence of serine rather than cysteine in an otherwise strongly conserved homology domain known to bind the 4Fe-4S cluster in other proteins suggests that serine may also bind iron-sulfur clusters. C;Sequence code: C, C, C, S A;Conditions: cross-link 4; not combinable C;Keywords: 4Fe-4S; iron-sulfur protein; metalloprotein F;/Binding site: 4Fe-4S cluster (Cys, Ser, Cys, Cys) (covalent) >TX;AA0289 bis-L-cysteinyl-L-N3'-histidino-L-serinyl tetrairon tetrasulfide N;Systematic name: tetra-mu3-sulfidobis(S-cysteinyliron)(N3'-histidinoiron)(O3-serinyliron) C;Formula: C 15 H 18 Fe 4 N 6 O 5 S 6 A;Formula weight: #chem 778.13 #phys 777.7061 C;Correction formula: C 0 H -4 Fe 4 S 4 A;Correction weight: #chem 347.62 #phys 347.5967 C;Date: 20-Apr-2000 #structure_revision 20-Apr-2000 #text_change 20-Apr-2000 C;Comment: The occurrence of serine rather than cysteine in an otherwise strongly conserved homology domain known to bind the 4Fe-4S cluster in other proteins suggests that serine may also bind iron-sulfur clusters. C;Sequence code: C, C, H, S A;Conditions: cross-link 4; not combinable C;Keywords: 4Fe-4S; iron-sulfur protein; metalloprotein F;/Binding site: 4Fe-4S cluster (His, Ser, Cys, Cys) (covalent) (type N3) >TX;AA0290 O-octanoyl-L-serine N;Alternate names: O3-octanoyl-L-serine; L-serine octanoate ester N;Systematic name: (2S,3R)-2-amino-3-(octanoyloxy)propanoic acid C;Formula: C 11 H 19 N 1 O 3 A;Formula weight: #chem 213.28 #phys 213.1365 C;Correction formula: C 8 H 14 O 1 A;Correction weight: #chem 126.20 #phys 126.1045 C;Date: 16-Jun-2000 #structure_revision 16-Jun-2000 #text_change 14-Jul-2000 R;Kojima, M.; Hosoda, H.; Date, Y.; Nakazato, M.; Matsuo, H.; Kangawa, K. Nature 402, 656-660, 1999 A;Title: Ghrelin is a growth-hormone-releasing acylated peptide from stomach. A;Reference number: A59316; MUID:20067959 A;Note: chromatographic and mass spectrographic identification; chemical synthesis C;Sequence code: S A;Conditions: combinable C;Keywords: lipoprotein F;/Binding site: octanoate (Ser) (covalent)