data_6591 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 6591 _Entry.Title ; On the Importance of Carbohydrate-Aromatic Interactions for the Molecular Recognition of Chitooligosaccharides by Hevein Domains. NMR Studies of the Structure and Binding Affinity of AcAMP2-Like Peptides with non Natural Napthyl and Fluoroaromatic Residues ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2005-04-12 _Entry.Accession_date 2005-04-12 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 M. Chavez . Isabel . 6591 2 Cecilia Andreu . . . 6591 3 Paloma Vidal . . . 6591 4 Felix Freire . . . 6591 5 Nuria Aboitiz . . . 6591 6 Patrick Groves . . . 6591 7 Juan Asensio . L. . 6591 8 Gregorio Asensio . . . 6591 9 Michiro Muraki . . . 6591 10 F. Canada . Javier . 6591 11 Jesus Jimenez-Barbero . . . 6591 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 6591 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 140 6591 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 4 . . 2008-07-31 . update BMRB 'updating non-standard residues' 6591 3 . . 2005-12-16 . update author 'update journal name' 6591 2 . . 2005-06-06 . update author 'changes to author names and polymer abbreviation' 6591 1 . . 2005-05-26 . original author 'Original release' 6591 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 6637 'AcAMP2F18Nalb mutant' 6591 BMRB 6639 'AcAMP2F18W mutant' 6591 BMRB 6647 AcAMP2F18Wb 6591 BMRB 6656 AcAMP2F18Pff/F20Pfff 6591 BMRB 6657 'AcAMP2F18Nal mutant' 6591 PDB 1MMC 'BMRB Entry Tracking System' 6591 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 6591 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 16220560 _Citation.Full_citation . _Citation.Title ; On the Importance of Carbohydrate-Aromatic Interactions for the Molecular Recognition of Oligosaccharides by Proteins: NMR Studies of the Structure and Binding Affinity of AcAMP2-Like Peptides with Non-Natural Napthyl and Fluoroaromatic Residues. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Chem. Eur. J.' _Citation.Journal_name_full . _Citation.Journal_volume 11 _Citation.Journal_issue 23 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 7060 _Citation.Page_last 7074 _Citation.Year 2005 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 M. Chavez . Isabel . 6591 1 2 Cecilia Andreu . . . 6591 1 3 Paloma Vidal . . . 6591 1 4 Nuria Aboitiz . . . 6591 1 5 Felix Freire . . . 6591 1 6 Patrick Groves . . . 6591 1 7 Juan Asensio . L. . 6591 1 8 Gregorio Asensio . . . 6591 1 9 Michiro Muraki . . . 6591 1 10 F. Canada . Javier . 6591 1 11 Jesus Jimenez-Barbero . . . 6591 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID AcAMP2 6591 1 'carbohydrate binding' 6591 1 Chitin 6591 1 hevein 6591 1 'Molecular Dynamics' 6591 1 'molecular recognition' 6591 1 NMR 6591 1 protein 6591 1 stop_ save_ save_reference-1 _Citation.Sf_category citations _Citation.Sf_framecode reference-1 _Citation.Entry_ID 6591 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8627629 _Citation.Full_citation ; Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus. J Mol Biol. 1996 May 3;258(2):322-33. ; _Citation.Title 'H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 258 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 322 _Citation.Page_last 333 _Citation.Year 1996 _Citation.Details ; The conformation in water of antimicrobial protein 2 from Amaranthus caudatus (Ac-AMP2) was determined using 1H NMR, DIANA and restrained molecular modeling. Ac-AMP2 is a 30 amino acid residue, lectin-like protein that specifically binds to chitin, a polymer of beta-1,4-N-acetyl-D-glucosamine. After sequence specific resonance assignments, a total of 198 distance restraints were collected from 2D NOESY buildup spectra at 500 MHz at pH 2, supplemented by a 2D NOESY spectrum at 600 MHz. The location of the three previously unassigned disulfide bridges was determined from preliminary DIANA structures, using a statistical analysis of intercystinyl distances. The solution structure of Ac-AMP2 is presented as a set of 26 DIANA structures, further refined by restrained molecular dynamics using a simulated annealing protocol in the AMBER force field, with a backbone r.m.s.d. for the well defined Glu3-Cys28 segment of 0.69(+/-0.12) angstroms. The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified. This structure is very similar to the equivalent regions of the X-ray structure of wheat germ agglutinin and the NMR structure of hevein. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'J. C.' Martins J. C. . 6591 2 2 D. Maes D. . . 6591 2 3 R. Loris R. . . 6591 2 4 'H. A.' Pepermans H. A. . 6591 2 5 L. Wyns L. . . 6591 2 6 R. Willem R. . . 6591 2 7 P. Verheyden P. . . 6591 2 stop_ save_ save_reference-2 _Citation.Sf_category citations _Citation.Sf_framecode reference-2 _Citation.Entry_ID 6591 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12144516 _Citation.Full_citation ; Muraki M. The importance of CH/pi interactions to the function of carbohydrate binding proteins. Protein Pept Lett. 2002 Jun;9(3):195-209. ; _Citation.Title 'The importance of CH/pi interactions to the function of carbohydrate binding proteins.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Pept. Lett.' _Citation.Journal_name_full 'Protein and peptide letters' _Citation.Journal_volume 9 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0929-8665 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 195 _Citation.Page_last 209 _Citation.Year 2002 _Citation.Details ; It is suggested that the interactions between the hydrophobic C-H groups of carbohydrate residues and the pi-electron systems of aromatic amino-acid residues play an important role in the ligand-recognition function of carbohydrate-binding proteins. This review focuses on our recent structural and functional studies of human lysozyme and hevein-domain type lectins (wheat-germ agglutinin and Ac-AMP2) aimed at understanding how CH/pi interactions are involved in the actual binding events. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Michiro Muraki M. . . 6591 3 stop_ save_ save_reference-3 _Citation.Sf_category citations _Citation.Sf_framecode reference-3 _Citation.Entry_ID 6591 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 15368576 _Citation.Full_citation ; Aboitiz N, Vila-Perello M, Groves P, Asensio JL, Andreu D, Canada FJ, Jimenez-Barbero J. NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides. Chembiochem. 2004 Sep 6;5(9):1245-55. ; _Citation.Title 'NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Chembiochem _Citation.Journal_name_full 'Chembiochem : a European journal of chemical biology' _Citation.Journal_volume 5 _Citation.Journal_issue 9 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1439-4227 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 1245 _Citation.Page_last 1255 _Citation.Year 2004 _Citation.Details ; HEV32, a 32-residue, truncated hevein lacking eleven C-terminal amino acids, was synthesized by solid-phase methodology and correctly folded with three cysteine bridge pairs. The affinities of HEV32 for small chitin fragments--in the forms of N,N',N"-triacetylchitotriose ((GlcNAc)3) (millimolar) and N,N',N",N"',N"",N""'-hexaacetylchitohexaose ((GlcNAc)6) (micromolar)--as measured by NMR and fluorescence methods, are comparable with those of native hevein. The HEV32 ligand-binding process is enthalpy driven, while entropy opposes binding. The NMR structure of ligand-bound HEV32 in aqueous solution was determined to be highly similar to the NMR structure of ligand-bound hevein. Solvated molecular-dynamics simulations were performed in order to monitor the changes in side-chain conformation of the binding site of HEV32 and hevein upon interaction with ligands. The calculations suggest that the Trp21 side-chain orientation of HEV32 in the free form differs from that in the bound state; this agrees with fluorescence and thermodynamic data. HEV32 provides a simple molecular model for studying protein-carbohydrate interactions and for understanding the physiological relevance of small native hevein domains lacking C-terminal residues. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Nuria Aboitiz N. . . 6591 4 2 Miquel Vila-Perello M. . . 6591 4 3 Patrick Groves P. . . 6591 4 4 'Juan Luis' Asensio J. L. . 6591 4 5 David Andreu D. . . 6591 4 6 'Francisco Javier' Canada F. J. . 6591 4 7 Jesus Jimenez-Barbero J. . . 6591 4 stop_ save_ save_reference-4 _Citation.Sf_category citations _Citation.Sf_framecode reference-4 _Citation.Entry_ID 6591 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10842338 _Citation.Full_citation ; Asensio JL, Siebert HC, von Der Lieth CW, Laynez J, Bruix M, Soedjanaamadja UM, Beintema JJ, Canada FJ, Gabius HJ, Jimenez-Barbero J. NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N"-triacetylchitotriose. Proteins. 2000 Aug 1;40(2):218-36. ; _Citation.Title 'NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N"-triacetylchitotriose.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Proteins _Citation.Journal_name_full Proteins _Citation.Journal_volume 40 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0887-3585 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 218 _Citation.Page_last 236 _Citation.Year 2000 _Citation.Details ; Model studies on lectins and their interactions with carbohydrate ligands in solution are essential to gain insights into the driving forces for complex formation and to optimize programs for computer simulations. The specific interaction of pseudohevein with N,N', N"-triacetylchitotriose has been analyzed by (1)H-NMR spectroscopy. Because of its small size, with a chain length of 45 amino acids, this lectin is a prime target to solution-structure determination by NOESY NMR experiments in water. The NMR-analysis was extended to assessment of the topology of the complex between pseudohevein and N, N',N"-triacetylchitotriose. NOESY experiments in water solution provided 342 protein proton-proton distance constraints. Binding of the ligand did not affect the pattern of the protein nuclear Overhauser effect signal noticeably, what would otherwise be indicative of a ligand-induced conformational change. The average backbone (residues 3-41) RMSD of the 20 refined structures was 1.14 A, whereas the heavy atom RMSD was 2.18 A. Two different orientations of the trisaccharide within the pseudohevein binding site are suggested, furnishing an explanation in structural terms for the lectin's capacity to target chitin. In both cases, hydrogen bonds and van der Waals contacts confer stability to the complexes. This conclusion is corroborated by the thermodynamic parameters of binding determined by NMR and isothermal titration calorimetry. The association process was enthalpically driven. In relation to hevein, the Trp/Tyr-substitution in the binding pocket has only a small effect on the free energy of binding in contrast to engineered galectin-1 and a mammalian C-type lectin. A comparison of the three-dimensional structure of pseudohevein in solution to those reported for wheat germ agglutinin (WGA) in the solid state and for hevein and WGA-B in solution has been performed, providing a data source about structural variability of the hevein domains. The experimentally derived structures and the values of the solvent accessibilities for several key residues have also been compared with conformations obtained by molecular dynamics simulations, pointing to the necessity to further refine the programs to enhance their predictive reliability and, thus, underscoring the importance of this kind of combined analysis in model systems. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'J. L.' Asensio J. L. . 6591 5 2 'H. C.' Siebert H. C. . 6591 5 3 'C. W.' 'von Der Lieth' C. W. . 6591 5 4 J. Laynez J. . . 6591 5 5 M. Bruix M. . . 6591 5 6 'U. M.' Soedjanaamadja U. M. . 6591 5 7 'J. J.' Beintema J. J. . 6591 5 8 'F. J.' Canada F. J. . 6591 5 9 'H. J.' Gabius H. J. . 6591 5 10 J. Jimenez-Barbero J. . . 6591 5 stop_ save_ save_reference-5 _Citation.Sf_category citations _Citation.Sf_framecode reference-5 _Citation.Entry_ID 6591 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10903932 _Citation.Full_citation ; Asensio JL, Canada FJ, Siebert HC, Laynez J, Poveda A, Nieto PM, Soedjanaamadja UM, Gabius HJ, Jimenez-Barbero J. Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains. Chem Biol. 2000 Jul;7(7):529-43. ; _Citation.Title 'Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Chem. Biol.' _Citation.Journal_name_full 'Chemistry & biology' _Citation.Journal_volume 7 _Citation.Journal_issue 7 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1074-5521 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 529 _Citation.Page_last 543 _Citation.Year 2000 _Citation.Details ; BACKGROUND: Many plants respond to pathogenic attack by producing defense proteins that are capable of reversible binding to chitin, a polysaccharide present in the cell wall of fungi and the exoskeleton of insects. Most of these chitin-binding proteins include a common structural motif of 30 to 43 residues organized around a conserved four-disulfide core, known as the 'hevein domain' or 'chitin-binding' motif. Although a number of structural and thermodynamic studies on hevein-type domains have been reported, these studies do not clarify how chitin recognition is achieved. RESULTS: The specific interaction of hevein with several (GlcNAc)(n) oligomers has been studied using nuclear magnetic resonance (NMR), analytical ultracentrifugation and isothermal titration microcalorimetry (ITC). The data demonstrate that hevein binds (GlcNAc)(2-4) in 1:1 stoichiometry with millimolar affinity. In contrast, for (GlcNAc)(5), a significant increase in binding affinity is observed. Analytical ultracentrifugation studies on the hevein-(GlcNAc)(5,8) interaction allowed detection of protein-carbohydrate complexes with a ratio of 2:1 in solution. NMR structural studies on the hevein-(GlcNAc)(5) complex showed the existence of an extended binding site with at least five GlcNAc units directly involved in protein-sugar contacts. CONCLUSIONS: The first detailed structural model for the hevein-chitin complex is presented on the basis of the analysis of NMR data. The resulting model, in combination with ITC and analytical ultracentrifugation data, conclusively shows that recognition of chitin by hevein domains is a dynamic process, which is not exclusively restricted to the binding of the nonreducing end of the polymer as previously thought. This allows chitin to bind with high affinity to a variable number of protein molecules, depending on the polysaccharide chain length. The biological process is multivalent. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'J. L.' Asensio J. L. . 6591 6 2 'F. J.' Canada F. J. . 6591 6 3 'H. C.' Siebert H. C. . 6591 6 4 J. Laynez J. . . 6591 6 5 A. Poveda A. . . 6591 6 6 'P. M.' Nieto P. M. . 6591 6 7 'U. M.' Soedjanaamadja U. M. . 6591 6 8 'H. J.' Gabius H. J. . 6591 6 9 J. Jimenez-Barbero J. . . 6591 6 stop_ save_ save_reference-6 _Citation.Sf_category citations _Citation.Sf_framecode reference-6 _Citation.Entry_ID 6591 _Citation.ID 7 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10877847 _Citation.Full_citation ; Muraki M, Morii H, Harata K. Chemically prepared hevein domains: effect of C-terminal truncation and the mutagenesis of aromatic residues on the affinity for chitin. Protein Eng. 2000 Jun;13(6):385-9. ; _Citation.Title 'Chemically prepared hevein domains: effect of C-terminal truncation and the mutagenesis of aromatic residues on the affinity for chitin.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Eng.' _Citation.Journal_name_full 'Protein engineering' _Citation.Journal_volume 13 _Citation.Journal_issue 6 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0269-2139 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 385 _Citation.Page_last 389 _Citation.Year 2000 _Citation.Details ; Chemically prepared hevein domains (HDs), N-terminal domain of an antifungal protein from Nicotiana tabacum (CBP20-N) and an antimicrobial peptide from Amaranthus caudatus (Ac-AMP2), were examined for their affinity for chitin, a beta-1,4-linked polymer of N-acetylglucosamine. An intact binding domain, CBP20-N, showed a higher affinity than a C-terminal truncated domain, Ac-AMP2. The formation of a pyroglutamate residue from N-terminal Gln of CBP20-N increased the affinity. The single replacement of any aromatic residue of Ac-AMP2 with Ala resulted in a significant reduction in affinity, suggesting the importance of the complete set of three aromatic residues in the ligand binding site. The mutations of Phe18 of Ac-AMP2 to the residues with larger aromatic rings, i.e. Trp, beta-(1-naphthyl)alanine or beta-(2-naphthyl)alanine, enhanced the affinity, whereas the mutation of Tyr20 to Trp reduced the affinity. The affinity of an HD for chitin might be improved by adjusting the size and substituent group of stacking aromatic rings. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 M. Muraki M. . . 6591 7 2 H. Morii H. . . 6591 7 3 K. Harata K. . . 6591 7 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_AcAMP2FPff18_Y20Pff _Assembly.Sf_category assembly _Assembly.Sf_framecode system_AcAMP2FPff18_Y20Pff _Assembly.Entry_ID 6591 _Assembly.ID 1 _Assembly.Name 'Phe18Pff and Tyr20Pff AcAMP2 double mutant' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 6591 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 AcAMP2F18Pff/Y20Pff 1 $AcAMP2F18Pff_Y20Pff . . . native . . . . . 6591 1 2 'N, N', N''-triacetylchitotriose' 2 $CTO . . . native . . . . . 6591 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 4 4 SG . 1 . 1 CYS 15 15 SG . . . . . . . . . . 6591 1 2 disulfide single . 1 . 1 CYS 9 9 SG . 1 . 1 CYS 21 21 SG . . . . . . . . . . 6591 1 3 disulfide single . 1 . 1 CYS 14 14 SG . 1 . 1 CYS 28 28 SG . . . . . . . . . . 6591 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID . PDB 1MMC . . . . . ; Residues Phe18 and Tyr20 of AcAMP2 (Amaranthus caudatus Antimicrobial Peptide-2) have been mutated to the non proteinogenic aminoacid 4-fluoro-L-phenylalanine. ; 6591 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID AcAMP2F18Pff/Y20Pff abbreviation 6591 1 'Phe18Pff and Tyr20Pff AcAMP2 double mutant' system 6591 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'chitin binding lectin' 6591 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_AcAMP2F18Pff_Y20Pff _Entity.Sf_category entity _Entity.Sf_framecode AcAMP2F18Pff_Y20Pff _Entity.Entry_ID 6591 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name AcAMP2 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; VGECVRGRCPSGMCCSQXGX CGKGPKYCGR ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 30 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 3209 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; The secondary structure of this protein presents beta-sheet on residues over residues 13 to 23. This protein is a hevein domain, and has high homology with AcAMP2 antimicrobial peptide. Carbohydrate binding site involves residues S16, Pff18, Pff20 and Y27. ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 6656 . AcAMP2F18Pff/F20Pfff . . . . . 100.00 30 100.00 100.00 1.34e-08 . . . . 6591 1 2 no PDB 1ZNT . "18 Nmr Structures Of Acamp2-Like Peptide With Non Natural Fluoroaromatic Residue (Acamp2f18pffY20PFF) COMPLEX WITH N,N,N- Triac" . . . . . 100.00 31 100.00 100.00 1.35e-08 . . . . 6591 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID AcAMP2 common 6591 1 AcAMP2F18Pff/F20Pff abbreviation 6591 1 'Phe18Pff and Tyr20Pff AcAMP2 double mutant' variant 6591 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . VAL . 6591 1 2 . GLY . 6591 1 3 . GLU . 6591 1 4 . CYS . 6591 1 5 . VAL . 6591 1 6 . ARG . 6591 1 7 . GLY . 6591 1 8 . ARG . 6591 1 9 . CYS . 6591 1 10 . PRO . 6591 1 11 . SER . 6591 1 12 . GLY . 6591 1 13 . MET . 6591 1 14 . CYS . 6591 1 15 . CYS . 6591 1 16 . SER . 6591 1 17 . GLN . 6591 1 18 . PFF . 6591 1 19 . GLY . 6591 1 20 . PFF . 6591 1 21 . CYS . 6591 1 22 . GLY . 6591 1 23 . LYS . 6591 1 24 . GLY . 6591 1 25 . PRO . 6591 1 26 . LYS . 6591 1 27 . TYR . 6591 1 28 . CYS . 6591 1 29 . GLY . 6591 1 30 . ARG . 6591 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . VAL 1 1 6591 1 . GLY 2 2 6591 1 . GLU 3 3 6591 1 . CYS 4 4 6591 1 . VAL 5 5 6591 1 . ARG 6 6 6591 1 . GLY 7 7 6591 1 . ARG 8 8 6591 1 . CYS 9 9 6591 1 . PRO 10 10 6591 1 . SER 11 11 6591 1 . GLY 12 12 6591 1 . MET 13 13 6591 1 . CYS 14 14 6591 1 . CYS 15 15 6591 1 . SER 16 16 6591 1 . GLN 17 17 6591 1 . PFF 18 18 6591 1 . GLY 19 19 6591 1 . PFF 20 20 6591 1 . CYS 21 21 6591 1 . GLY 22 22 6591 1 . LYS 23 23 6591 1 . GLY 24 24 6591 1 . PRO 25 25 6591 1 . LYS 26 26 6591 1 . TYR 27 27 6591 1 . CYS 28 28 6591 1 . GLY 29 29 6591 1 . ARG 30 30 6591 1 stop_ save_ save_CTO _Entity.Sf_category entity _Entity.Sf_framecode CTO _Entity.Entry_ID 6591 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name CTO _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID CTO _Entity.Nonpolymer_comp_label $chem_comp_CTO _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . CTO . 6591 2 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 6591 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $AcAMP2F18Pff_Y20Pff . 3567 . . 'Amaranthus caudatus' 'inca wheat' . . Eukaryota Viridiplantae Amaranthus caudatus . . . . . . . . . . . . . . . . . . 'love-lies bleendig, tassel flower. tissue:seed' . . 6591 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 6591 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $AcAMP2F18Pff_Y20Pff . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . ; The residues Phe18 and Tyr20 of the natural AcAMP2 were changed to 4-fluorophenylalanine. The aminoacids were manually assembled by solid phase synthesis using Fmoc chemistry according to satandard protocols The carboxiterminal residue ARG30 is in the amide form. ; . . 6591 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_PFF _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_PFF _Chem_comp.Entry_ID 6591 _Chem_comp.ID PFF _Chem_comp.Provenance . _Chem_comp.Name 4-FLUORO-L-PHENYLALANINE _Chem_comp.Type 'L-peptide linking' _Chem_comp.BMRB_code . _Chem_comp.PDB_code PFF _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2003-07-30 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code F _Chem_comp.Three_letter_code PFF _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID PHE _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic yes _Chem_comp.Formula 'C9 H10 F N O2' _Chem_comp.Formula_weight 183.180 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag yes _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site PDBE _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Aug 4 16:00:38 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID c1cc(ccc1CC(C(=O)O)N)F SMILES 'OpenEye OEToolkits' 1.5.0 6591 PFF c1cc(ccc1C[C@@H](C(=O)O)N)F SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 6591 PFF Fc1ccc(cc1)CC(C(=O)O)N SMILES ACDLabs 10.04 6591 PFF InChI=1S/C9H10FNO2/c10-7-3-1-6(2-4-7)5-8(11)9(12)13/h1-4,8H,5,11H2,(H,12,13)/t8-/m0/s1 InChI InChI 1.03 6591 PFF N[C@@H](Cc1ccc(F)cc1)C(O)=O SMILES_CANONICAL CACTVS 3.341 6591 PFF N[CH](Cc1ccc(F)cc1)C(O)=O SMILES CACTVS 3.341 6591 PFF XWHHYOYVRVGJJY-QMMMGPOBSA-N InChIKey InChI 1.03 6591 PFF stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID '(2S)-2-amino-3-(4-fluorophenyl)propanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 6591 PFF 4-fluoro-L-phenylalanine 'SYSTEMATIC NAME' ACDLabs 10.04 6591 PFF stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID N . N . . N . . N 0 . . . . no no . . . . 46.465 . 27.890 . 1.389 . -0.040 -1.210 0.053 1 . 6591 PFF CA . CA . . C . . S 0 . . . . no no . . . . 47.091 . 29.119 . 0.910 . 1.172 -1.709 0.652 2 . 6591 PFF C . C . . C . . N 0 . . . . no no . . . . 48.578 . 29.095 . 1.054 . 1.083 -3.207 0.905 3 . 6591 PFF O . O . . O . . N 0 . . . . no no . . . . 49.223 . 30.130 . 1.065 . 0.040 -3.770 1.222 4 . 6591 PFF OXT . OXT . . O . . N 0 . . . . no yes . . . . . . . . . . 2.247 -3.882 0.744 5 . 6591 PFF CB . CB . . C . . N 0 . . . . no no . . . . 46.628 . 30.322 . 1.695 . 1.484 -0.975 1.962 6 . 6591 PFF CG . CG . . C . . N 0 . . . . yes no . . . . 45.398 . 31.033 . 1.284 . 2.940 -1.060 2.353 7 . 6591 PFF CD1 . CD1 . . C . . N 0 . . . . yes no . . . . 44.257 . 30.753 . 2.015 . 3.369 -2.109 3.149 8 . 6591 PFF CD2 . CD2 . . C . . N 0 . . . . yes no . . . . 45.270 . 31.304 . -0.071 . 3.820 -0.086 1.907 9 . 6591 PFF CE1 . CE1 . . C . . N 0 . . . . yes no . . . . 43.027 . 30.643 . 1.380 . 4.715 -2.188 3.510 10 . 6591 PFF CE2 . CE2 . . C . . N 0 . . . . yes no . . . . 44.037 . 31.227 . -0.706 . 5.166 -0.165 2.268 11 . 6591 PFF CZ . CZ . . C . . N 0 . . . . yes no . . . . 42.906 . 30.905 . 0.023 . 5.613 -1.216 3.069 12 . 6591 PFF F . F . . F . . N 0 . . . . no no . . . . 41.702 . 30.837 . -0.574 . 6.904 -1.291 3.415 13 . 6591 PFF H . H . . H . . N 0 . . . . no no . . . . 45.440 . 27.989 . 1.351 . -0.102 -1.155 -0.950 14 . 6591 PFF H2 . H2 . . H . . N 0 . . . . no yes . . . . 46.757 . 27.102 . 0.794 . -0.715 -0.741 0.634 15 . 6591 PFF HA . HA . . H . . N 0 . . . . no no . . . . 46.800 . 29.187 . -0.149 . 1.965 -1.558 -0.089 16 . 6591 PFF HXT . HXT . . H . . N 0 . . . . no yes . . . . 0.945 . -0.015 . 0.091 . 2.188 -4.848 0.901 17 . 6591 PFF HB2 . HB2 . . H . . N 0 . . . . no no . . . . 46.472 . 29.987 . 2.731 . 1.215 0.087 1.879 18 . 6591 PFF HB3 . HB3 . . H . . N 0 . . . . no no . . . . 47.423 . 31.063 . 1.523 . 0.859 -1.368 2.775 19 . 6591 PFF HD1 . HD1 . . H . . N 0 . . . . no no . . . . 44.322 . 30.622 . 3.066 . 2.677 -2.871 3.497 20 . 6591 PFF HD2 . HD2 . . H . . N 0 . . . . no no . . . . 46.129 . 31.575 . -0.632 . 3.481 0.736 1.283 21 . 6591 PFF HE1 . HE1 . . H . . N 0 . . . . no no . . . . 42.171 . 30.356 . 1.938 . 5.063 -3.006 4.134 22 . 6591 PFF HE2 . HE2 . . H . . N 0 . . . . no no . . . . 43.963 . 31.415 . -1.748 . 5.865 0.592 1.925 23 . 6591 PFF stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING N CA no N 1 . 6591 PFF 2 . SING N H no N 2 . 6591 PFF 3 . SING N H2 no N 3 . 6591 PFF 4 . SING CA C no N 4 . 6591 PFF 5 . SING CA CB no N 5 . 6591 PFF 6 . SING CA HA no N 6 . 6591 PFF 7 . DOUB C O no N 7 . 6591 PFF 8 . SING C OXT no N 8 . 6591 PFF 9 . SING OXT HXT no N 9 . 6591 PFF 10 . SING CB CG no N 10 . 6591 PFF 11 . SING CB HB2 no N 11 . 6591 PFF 12 . SING CB HB3 no N 12 . 6591 PFF 13 . DOUB CG CD1 yes N 13 . 6591 PFF 14 . SING CG CD2 yes N 14 . 6591 PFF 15 . SING CD1 CE1 yes N 15 . 6591 PFF 16 . SING CD1 HD1 no N 16 . 6591 PFF 17 . DOUB CD2 CE2 yes N 17 . 6591 PFF 18 . SING CD2 HD2 no N 18 . 6591 PFF 19 . DOUB CE1 CZ yes N 19 . 6591 PFF 20 . SING CE1 HE1 no N 20 . 6591 PFF 21 . SING CE2 CZ yes N 21 . 6591 PFF 22 . SING CE2 HE2 no N 22 . 6591 PFF 23 . SING CZ F no N 23 . 6591 PFF stop_ save_ save_chem_comp_CTO _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CTO _Chem_comp.Entry_ID 6591 _Chem_comp.ID CTO _Chem_comp.Provenance . _Chem_comp.Name TRIACETYLCHITOTRIOSE _Chem_comp.Type D-saccharide _Chem_comp.BMRB_code . _Chem_comp.PDB_code CTO _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code CTO _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms CHITOTRIOSE _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'C24 H41 N3 O16' _Chem_comp.Formula_weight 627.593 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 1BB5 _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Aug 4 16:02:37 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID CC(=O)NC1C(C(C(OC1O)CO)OC2C(C(C(C(O2)CO)OC3C(C(C(C(O3)CO)O)O)NC(=O)C)O)NC(=O)C)O SMILES 'OpenEye OEToolkits' 1.5.0 6591 CTO CC(=O)N[C@@H]1[C@H]([C@@H]([C@H](O[C@H]1O)CO)O[C@H]2[C@@H]([C@H]([C@@H]([C@H](O2)CO)O[C@H]3[C@@H]([C@H]([C@@H]([C@H](O3)CO)O)O)NC(=O)C)O)NC(=O)C)O SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 6591 CTO CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O[C@@H]2O[C@H](CO)[C@@H](O[C@@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@H]3NC(C)=O)[C@H](O)[C@H]2NC(C)=O)[C@@H]1O SMILES_CANONICAL CACTVS 3.341 6591 CTO CC(=O)N[CH]1[CH](O)O[CH](CO)[CH](O[CH]2O[CH](CO)[CH](O[CH]3O[CH](CO)[CH](O)[CH](O)[CH]3NC(C)=O)[CH](O)[CH]2NC(C)=O)[CH]1O SMILES CACTVS 3.341 6591 CTO InChI=1S/C24H41N3O16/c1-7(31)25-13-18(36)20(11(5-29)39-22(13)38)42-24-15(27-9(3)33)19(37)21(12(6-30)41-24)43-23-14(26-8(2)32)17(35)16(34)10(4-28)40-23/h10-24,28-30,34-38H,4-6H2,1-3H3,(H,25,31)(H,26,32)(H,27,33)/t10-,11-,12-,13-,14-,15-,16-,17-,18-,19-,20-,21-,22-,23+,24+/m1/s1 InChI InChI 1.03 6591 CTO O=C(NC3C(O)C(O)C(OC3OC2C(OC(OC1C(OC(O)C(NC(=O)C)C1O)CO)C(NC(=O)C)C2O)CO)CO)C SMILES ACDLabs 10.04 6591 CTO WZZVUHWLNMNWLW-VFCSDQTKSA-N InChIKey InChI 1.03 6591 CTO stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID 2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranosyl-(1->4)-2-(acetylamino)-2-deoxy-beta-D-glucopyranose 'SYSTEMATIC NAME' ACDLabs 10.04 6591 CTO N-[(2S,3R,4R,5S,6R)-2-[(2R,3S,4R,5R,6S)-5-acetamido-6-[(2R,3S,4R,5R,6R)-5-acetamido-4,6-dihydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-4-hydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-3-yl]ethanamide 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 6591 CTO stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID C11 . C11 . . C . . S 0 . . . . no no . . . . 14.371 . -10.068 . 33.472 . 0.462 0.035 -3.829 1 . 6591 CTO C21 . C21 . . C . . R 0 . . . . no no . . . . 14.058 . -11.405 . 34.260 . 1.129 -0.639 -5.030 2 . 6591 CTO N21 . N21 . . N . . N 0 . . . . no no . . . . 14.331 . -11.261 . 35.711 . 2.361 -1.302 -4.598 3 . 6591 CTO C71 . C71 . . C . . N 0 . . . . no no . . . . 13.576 . -11.882 . 36.677 . 2.329 -2.587 -4.193 4 . 6591 CTO O71 . O71 . . O . . N 0 . . . . no no . . . . 12.553 . -12.539 . 36.429 . 1.279 -3.194 -4.186 5 . 6591 CTO C81 . C81 . . C . . N 0 . . . . no no . . . . 14.064 . -11.734 . 38.099 . 3.597 -3.269 -3.748 6 . 6591 CTO C31 . C31 . . C . . R 0 . . . . no no . . . . 14.913 . -12.541 . 33.636 . 1.461 0.426 -6.081 7 . 6591 CTO O31 . O31 . . O . . N 0 . . . . no no . . . . 14.640 . -13.793 . 34.299 . 1.948 -0.201 -7.268 8 . 6591 CTO C41 . C41 . . C . . S 0 . . . . no no . . . . 14.589 . -12.674 . 32.143 . 0.185 1.212 -6.401 9 . 6591 CTO O41 . O41 . . O . . N 0 . . . . no no . . . . 15.377 . -13.731 . 31.540 . 0.498 2.305 -7.266 10 . 6591 CTO C51 . C51 . . C . . R 0 . . . . no no . . . . 14.887 . -11.341 . 31.428 . -0.411 1.747 -5.097 11 . 6591 CTO O51 . O51 . . O . . N 0 . . . . no no . . . . 14.099 . -10.256 . 32.057 . -0.752 0.658 -4.240 12 . 6591 CTO C61 . C61 . . C . . N 0 . . . . no no . . . . 14.541 . -11.368 . 29.942 . -1.668 2.561 -5.410 13 . 6591 CTO O61 . O61 . . O . . N 0 . . . . no no . . . . 13.212 . -11.809 . 29.707 . -2.223 3.067 -4.194 14 . 6591 CTO C12 . C12 . . C . . S 0 . . . . no no . . . . 13.364 . -5.213 . 35.038 . -0.984 -0.342 1.074 15 . 6591 CTO C22 . C22 . . C . . R 0 . . . . no no . . . . 12.424 . -5.739 . 33.926 . -2.082 -0.093 0.038 16 . 6591 CTO N22 . N22 . . N . . N 0 . . . . no no . . . . 11.141 . -5.015 . 33.922 . -3.341 -0.677 0.508 17 . 6591 CTO C72 . C72 . . C . . N 0 . . . . no no . . . . 10.744 . -4.173 . 32.925 . -4.194 0.062 1.243 18 . 6591 CTO O72 . O72 . . O . . N 0 . . . . no no . . . . 11.392 . -3.984 . 31.884 . -3.920 1.211 1.515 19 . 6591 CTO C82 . C82 . . C . . N 0 . . . . no no . . . . 9.435 . -3.456 . 33.157 . -5.489 -0.538 1.726 20 . 6591 CTO C32 . C32 . . C . . R 0 . . . . no no . . . . 12.218 . -7.258 . 34.090 . -1.676 -0.749 -1.286 21 . 6591 CTO O32 . O32 . . O . . N 0 . . . . no no . . . . 11.374 . -7.736 . 33.029 . -2.617 -0.402 -2.305 22 . 6591 CTO C42 . C42 . . C . . S 0 . . . . no no . . . . 13.554 . -7.991 . 34.085 . -0.284 -0.240 -1.677 23 . 6591 CTO O42 . O42 . . O . . N 0 . . . . no no . . . . 13.290 . -9.435 . 34.258 . 0.178 -0.946 -2.830 24 . 6591 CTO C52 . C52 . . C . . R 0 . . . . no no . . . . 14.422 . -7.413 . 35.267 . 0.678 -0.475 -0.511 25 . 6591 CTO O52 . O52 . . O . . N 0 . . . . no no . . . . 14.598 . -5.976 . 35.081 . 0.236 0.249 0.634 26 . 6591 CTO C62 . C62 . . C . . N 0 . . . . no no . . . . 15.829 . -7.981 . 35.360 . 2.078 -0.000 -0.905 27 . 6591 CTO O62 . O62 . . O . . N 0 . . . . no no . . . . 16.591 . -7.529 . 34.246 . 2.999 -0.312 0.141 28 . 6591 CTO C13 . C13 . . C . . R 0 . . . . no no . . . . 13.947 . -0.192 . 37.088 . 0.369 -0.290 6.019 29 . 6591 CTO O13 . O13 . . O . . N 0 . . . . no yes . . . . 14.158 . 0.813 . 38.412 . 1.214 -0.696 7.098 30 . 6591 CTO C23 . C23 . . C . . R 0 . . . . no no . . . . 15.181 . -1.105 . 36.926 . 1.156 0.615 5.069 31 . 6591 CTO N23 . N23 . . N . . N 0 . . . . no no . . . . 16.391 . -0.296 . 36.724 . 1.647 1.785 5.802 32 . 6591 CTO C73 . C73 . . C . . N 0 . . . . no no . . . . 17.543 . -0.434 . 37.417 . 2.854 1.749 6.399 33 . 6591 CTO O73 . O73 . . O . . N 0 . . . . no no . . . . 17.639 . -1.026 . 38.495 . 3.535 0.747 6.330 34 . 6591 CTO C83 . C83 . . C . . N 0 . . . . no no . . . . 18.749 . 0.207 . 36.792 . 3.359 2.952 7.153 35 . 6591 CTO C33 . C33 . . C . . R 0 . . . . no no . . . . 14.950 . -2.038 . 35.740 . 0.235 1.071 3.932 36 . 6591 CTO O33 . O33 . . O . . N 0 . . . . no no . . . . 16.078 . -2.913 . 35.603 . 0.989 1.792 2.956 37 . 6591 CTO C43 . C43 . . C . . S 0 . . . . no no . . . . 13.674 . -2.858 . 35.967 . -0.393 -0.167 3.284 38 . 6591 CTO O43 . O43 . . O . . N 0 . . . . no no . . . . 13.439 . -3.729 . 34.841 . -1.369 0.237 2.323 39 . 6591 CTO C53 . C53 . . C . . R 0 . . . . no no . . . . 12.472 . -1.894 . 36.119 . -1.063 -1.014 4.369 40 . 6591 CTO O53 . O53 . . O . . N 0 . . . . no no . . . . 12.735 . -0.983 . 37.239 . -0.088 -1.444 5.317 41 . 6591 CTO C63 . C63 . . C . . N 0 . . . . no no . . . . 11.146 . -2.602 . 36.397 . -1.720 -2.236 3.725 42 . 6591 CTO O63 . O63 . . O . . N 0 . . . . no no . . . . 11.102 . -3.142 . 37.697 . -2.432 -2.974 4.720 43 . 6591 CTO H11 . H11 . . H . . N 0 . . . . no no . . . . 15.371 . -9.578 . 33.422 . 1.134 0.788 -3.417 44 . 6591 CTO H21 . H21 . . H . . N 0 . . . . no no . . . . 12.973 . -11.649 . 34.168 . 0.450 -1.375 -5.460 45 . 6591 CTO HNL . HNL . . H . . N 0 . . . . no no . . . . 15.096 . -10.691 . 36.072 . 3.201 -0.816 -4.603 46 . 6591 CTO H811 . H811 . . H . . N 0 . . . . no no . . . . 13.451 . -12.237 . 38.882 . 3.374 -4.297 -3.459 47 . 6591 CTO H812 . H812 . . H . . N 0 . . . . no no . . . . 15.123 . -12.073 . 38.171 . 4.316 -3.270 -4.567 48 . 6591 CTO H813 . H813 . . H . . N 0 . . . . no no . . . . 14.181 . -10.653 . 38.347 . 4.017 -2.735 -2.896 49 . 6591 CTO H31 . H31 . . H . . N 0 . . . . no no . . . . 15.991 . -12.288 . 33.763 . 2.219 1.104 -5.688 50 . 6591 CTO HOV . HOV . . H . . N 0 . . . . no no . . . . 15.163 . -14.488 . 33.917 . 2.131 0.504 -7.903 51 . 6591 CTO H41 . H41 . . H . . N 0 . . . . no no . . . . 13.508 . -12.927 . 32.036 . -0.535 0.556 -6.889 52 . 6591 CTO HO4 . HO4 . . H . . N 0 . . . . no no . . . . 15.176 . -13.813 . 30.615 . -0.329 2.775 -7.435 53 . 6591 CTO H51 . H51 . . H . . N 0 . . . . no no . . . . 15.984 . -11.168 . 31.526 . 0.318 2.384 -4.599 54 . 6591 CTO H611 . H611 . . H . . N 0 . . . . no no . . . . 14.726 . -10.376 . 29.467 . -1.408 3.393 -6.065 55 . 6591 CTO H612 . H612 . . H . . N 0 . . . . no no . . . . 15.275 . -11.979 . 29.368 . -2.400 1.923 -5.906 56 . 6591 CTO HO6 . HO6 . . H . . N 0 . . . . no no . . . . 12.996 . -11.825 . 28.781 . -3.011 3.572 -4.436 57 . 6591 CTO H12 . H12 . . H . . N 0 . . . . no no . . . . 12.992 . -5.371 . 36.077 . -0.842 -1.415 1.201 58 . 6591 CTO H22 . H22 . . H . . N 0 . . . . no no . . . . 12.902 . -5.553 . 32.936 . -2.211 0.978 -0.109 59 . 6591 CTO HNM . HNM . . H . . N 0 . . . . no no . . . . 10.464 . -5.105 . 34.680 . -3.560 -1.597 0.290 60 . 6591 CTO H821 . H821 . . H . . N 0 . . . . no no . . . . 9.110 . -2.767 . 32.342 . -6.043 0.204 2.300 61 . 6591 CTO H822 . H822 . . H . . N 0 . . . . no no . . . . 8.629 . -4.195 . 33.374 . -6.085 -0.854 0.870 62 . 6591 CTO H823 . H823 . . H . . N 0 . . . . no no . . . . 9.468 . -2.907 . 34.127 . -5.276 -1.400 2.359 63 . 6591 CTO H32 . H32 . . H . . N 0 . . . . no no . . . . 11.728 . -7.456 . 35.071 . -1.649 -1.832 -1.167 64 . 6591 CTO HOW . HOW . . H . . N 0 . . . . no no . . . . 11.247 . -8.672 . 33.130 . -3.476 -0.741 -2.018 65 . 6591 CTO H42 . H42 . . H . . N 0 . . . . no no . . . . 14.108 . -7.848 . 33.128 . -0.334 0.826 -1.898 66 . 6591 CTO H52 . H52 . . H . . N 0 . . . . no no . . . . 13.861 . -7.689 . 36.190 . 0.709 -1.540 -0.277 67 . 6591 CTO H621 . H621 . . H . . N 0 . . . . no no . . . . 16.318 . -7.741 . 36.332 . 2.387 -0.501 -1.822 68 . 6591 CTO H622 . H622 . . H . . N 0 . . . . no no . . . . 15.831 . -9.092 . 35.451 . 2.063 1.077 -1.067 69 . 6591 CTO HO2 . HO2 . . H . . N 0 . . . . no no . . . . 17.470 . -7.884 . 34.304 . 3.867 0.003 -0.146 70 . 6591 CTO H13 . H13 . . H . . N 0 . . . . no no . . . . 13.839 . 0.431 . 36.169 . -0.486 0.256 6.415 71 . 6591 CTO HOD . HOD . . H . . N 0 . . . . no no . . . . 13.398 . 1.374 . 38.511 . 0.681 -1.263 7.672 72 . 6591 CTO H23 . H23 . . H . . N 0 . . . . no no . . . . 15.326 . -1.711 . 37.850 . 2.001 0.064 4.656 73 . 6591 CTO HNN . HNN . . H . . N 0 . . . . no no . . . . 16.436 . 0.444 . 36.024 . 1.102 2.586 5.857 74 . 6591 CTO H831 . H831 . . H . . N 0 . . . . no no . . . . 19.699 . 0.093 . 37.363 . 4.345 2.737 7.564 75 . 6591 CTO H832 . H832 . . H . . N 0 . . . . no no . . . . 18.882 . -0.164 . 35.749 . 3.426 3.804 6.475 76 . 6591 CTO H833 . H833 . . H . . N 0 . . . . no no . . . . 18.549 . 1.285 . 36.592 . 2.670 3.188 7.965 77 . 6591 CTO H33 . H33 . . H . . N 0 . . . . no no . . . . 14.831 . -1.438 . 34.807 . -0.549 1.711 4.335 78 . 6591 CTO HOX . HOX . . H . . N 0 . . . . no no . . . . 15.934 . -3.493 . 34.864 . 1.365 2.561 3.406 79 . 6591 CTO H43 . H43 . . H . . N 0 . . . . no no . . . . 13.793 . -3.473 . 36.889 . 0.382 -0.753 2.792 80 . 6591 CTO H53 . H53 . . H . . N 0 . . . . no no . . . . 12.370 . -1.359 . 35.145 . -1.823 -0.418 4.875 81 . 6591 CTO H631 . H631 . . H . . N 0 . . . . no no . . . . 10.278 . -1.927 . 36.208 . -2.413 -1.910 2.950 82 . 6591 CTO H632 . H632 . . H . . N 0 . . . . no no . . . . 10.932 . -3.380 . 35.627 . -0.952 -2.870 3.282 83 . 6591 CTO HO3 . HO3 . . H . . N 0 . . . . no no . . . . 10.277 . -3.582 . 37.869 . -2.830 -3.734 4.274 84 . 6591 CTO stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING C11 C21 no N 1 . 6591 CTO 2 . SING C11 O51 no N 2 . 6591 CTO 3 . SING C11 O42 no N 3 . 6591 CTO 4 . SING C11 H11 no N 4 . 6591 CTO 5 . SING C21 N21 no N 5 . 6591 CTO 6 . SING C21 C31 no N 6 . 6591 CTO 7 . SING C21 H21 no N 7 . 6591 CTO 8 . SING N21 C71 no N 8 . 6591 CTO 9 . SING N21 HNL no N 9 . 6591 CTO 10 . DOUB C71 O71 no N 10 . 6591 CTO 11 . SING C71 C81 no N 11 . 6591 CTO 12 . SING C81 H811 no N 12 . 6591 CTO 13 . SING C81 H812 no N 13 . 6591 CTO 14 . SING C81 H813 no N 14 . 6591 CTO 15 . SING C31 O31 no N 15 . 6591 CTO 16 . SING C31 C41 no N 16 . 6591 CTO 17 . SING C31 H31 no N 17 . 6591 CTO 18 . SING O31 HOV no N 18 . 6591 CTO 19 . SING C41 O41 no N 19 . 6591 CTO 20 . SING C41 C51 no N 20 . 6591 CTO 21 . SING C41 H41 no N 21 . 6591 CTO 22 . SING O41 HO4 no N 22 . 6591 CTO 23 . SING C51 O51 no N 23 . 6591 CTO 24 . SING C51 C61 no N 24 . 6591 CTO 25 . SING C51 H51 no N 25 . 6591 CTO 26 . SING C61 O61 no N 26 . 6591 CTO 27 . SING C61 H611 no N 27 . 6591 CTO 28 . SING C61 H612 no N 28 . 6591 CTO 29 . SING O61 HO6 no N 29 . 6591 CTO 30 . SING C12 C22 no N 30 . 6591 CTO 31 . SING C12 O52 no N 31 . 6591 CTO 32 . SING C12 O43 no N 32 . 6591 CTO 33 . SING C12 H12 no N 33 . 6591 CTO 34 . SING C22 N22 no N 34 . 6591 CTO 35 . SING C22 C32 no N 35 . 6591 CTO 36 . SING C22 H22 no N 36 . 6591 CTO 37 . SING N22 C72 no N 37 . 6591 CTO 38 . SING N22 HNM no N 38 . 6591 CTO 39 . DOUB C72 O72 no N 39 . 6591 CTO 40 . SING C72 C82 no N 40 . 6591 CTO 41 . SING C82 H821 no N 41 . 6591 CTO 42 . SING C82 H822 no N 42 . 6591 CTO 43 . SING C82 H823 no N 43 . 6591 CTO 44 . SING C32 O32 no N 44 . 6591 CTO 45 . SING C32 C42 no N 45 . 6591 CTO 46 . SING C32 H32 no N 46 . 6591 CTO 47 . SING O32 HOW no N 47 . 6591 CTO 48 . SING C42 O42 no N 48 . 6591 CTO 49 . SING C42 C52 no N 49 . 6591 CTO 50 . SING C42 H42 no N 50 . 6591 CTO 51 . SING C52 O52 no N 51 . 6591 CTO 52 . SING C52 C62 no N 52 . 6591 CTO 53 . SING C52 H52 no N 53 . 6591 CTO 54 . SING C62 O62 no N 54 . 6591 CTO 55 . SING C62 H621 no N 55 . 6591 CTO 56 . SING C62 H622 no N 56 . 6591 CTO 57 . SING O62 HO2 no N 57 . 6591 CTO 58 . SING C13 O13 no N 58 . 6591 CTO 59 . SING C13 C23 no N 59 . 6591 CTO 60 . SING C13 O53 no N 60 . 6591 CTO 61 . SING C13 H13 no N 61 . 6591 CTO 62 . SING O13 HOD no N 62 . 6591 CTO 63 . SING C23 N23 no N 63 . 6591 CTO 64 . SING C23 C33 no N 64 . 6591 CTO 65 . SING C23 H23 no N 65 . 6591 CTO 66 . SING N23 C73 no N 66 . 6591 CTO 67 . SING N23 HNN no N 67 . 6591 CTO 68 . DOUB C73 O73 no N 68 . 6591 CTO 69 . SING C73 C83 no N 69 . 6591 CTO 70 . SING C83 H831 no N 70 . 6591 CTO 71 . SING C83 H832 no N 71 . 6591 CTO 72 . SING C83 H833 no N 72 . 6591 CTO 73 . SING C33 O33 no N 73 . 6591 CTO 74 . SING C33 C43 no N 74 . 6591 CTO 75 . SING C33 H33 no N 75 . 6591 CTO 76 . SING O33 HOX no N 76 . 6591 CTO 77 . SING C43 O43 no N 77 . 6591 CTO 78 . SING C43 C53 no N 78 . 6591 CTO 79 . SING C43 H43 no N 79 . 6591 CTO 80 . SING C53 O53 no N 80 . 6591 CTO 81 . SING C53 C63 no N 81 . 6591 CTO 82 . SING C53 H53 no N 82 . 6591 CTO 83 . SING C63 O63 no N 83 . 6591 CTO 84 . SING C63 H631 no N 84 . 6591 CTO 85 . SING C63 H632 no N 85 . 6591 CTO 86 . SING O63 HO3 no N 86 . 6591 CTO stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample-1 _Sample.Sf_category sample _Sample.Sf_framecode sample-1 _Sample.Entry_ID 6591 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 AcAMP2 . . . 1 $AcAMP2F18Pff_Y20Pff . . 1 . . mM . . . . 6591 1 2 TRIACETYLCHITOTRIOSE . . . 2 $CTO . . 12 . . mM . . . . 6591 1 3 'Phosphate buffer' . . . . . . . 20 . . mM . . . . 6591 1 4 NaCl . . . . . . . 100 . . mM . . . . 6591 1 5 H2O . . . . . . . 90 . . % . . . . 6591 1 6 D2O . . . . . . . 10 . . % . . . . 6591 1 stop_ save_ ####################### # Sample conditions # ####################### save_conditions-1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode conditions-1 _Sample_condition_list.Entry_ID 6591 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.15 0.02 M 6591 1 pH 5.6 0.2 pH 6591 1 temperature 298 0.2 K 6591 1 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 6591 _Software.ID 1 _Software.Name xwinnmr _Software.Version 3.2 _Software.Details ; Bruker The software performs acquisition and processing of NMR experiments ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Data collection' 6591 1 stop_ save_ save_XEASY _Software.Sf_category software _Software.Sf_framecode XEASY _Software.Entry_ID 6591 _Software.ID 2 _Software.Name XEASY _Software.Version 1.3.13 _Software.Details ; Bartels C., Xia T., Billeter M., Guntert P. and Wuthrich K. (1995) J. Biol. NMR 6, 1-10. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. This program helps visualization and assignment of 2D NMR spectra. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Data analysis' 6591 2 stop_ save_ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 6591 _Software.ID 3 _Software.Name DYANA _Software.Version 1.5 _Software.Details ; Guntert P., Mumenthaler C. and Wuthrich K. (1997) J. Mol. Biol. 273, 283-298. Torsion angle dynamics for NMR structure calculation with the new program DYANA. This program yields a collection of protein structures that fit the 1H-1H distance constraints experimentally obtained. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Structure solution' 6591 3 stop_ save_ save_AMBER _Software.Sf_category software _Software.Sf_framecode AMBER _Software.Entry_ID 6591 _Software.ID 4 _Software.Name AMBER _Software.Version 5.0 _Software.Details ; Pearlman D. A., Case D. A., Caldwell J. W., Cheatham T. E., DeBolt S., Ross W. S., Ferguson D., Seibel G. L., and Kollman P. A. (1995) Comp. Phys. Commun. 91, 1-41. AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. The programs used from this package perform molecular dynamics calculations on protein structures. They also convert dyana-format pdb files into amber-format pdb files. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Structure refinement' 6591 4 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 6591 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AVANCE _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 800 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 6591 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer Bruker AVANCE . 800 . . . 6591 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 6591 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 TOCSY . . . . . . . . . . . 1 $sample-1 . . . 1 $conditions-1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 6591 1 2 NOESY . . . . . . . . . . . 1 $sample-1 . . . 1 $conditions-1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 6591 1 stop_ save_ save_NMR_applied_experiment _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_applied_experiment _NMR_spec_expt.Entry_ID 6591 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name . _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 6591 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 6591 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name NOESY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 6591 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 6591 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_AcAMP2_Pff18_20_shift _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode AcAMP2_Pff18_20_shift _Assigned_chem_shift_list.Entry_ID 6591 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $conditions-1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details ; The atom HA3 of GLY22 shows up at 1.795 , due to near by Tyr27 which shifts it highfield. ; _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample-1 . 6591 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 VAL HA H 1 3.813 0.02 . 1 . . . . . . . . 6591 1 2 . 1 1 1 1 VAL HB H 1 2.133 0.02 . 1 . . . . . . . . 6591 1 3 . 1 1 1 1 VAL HG11 H 1 1.047 0.02 . 2 . . . . . . . . 6591 1 4 . 1 1 1 1 VAL HG12 H 1 1.047 0.02 . 2 . . . . . . . . 6591 1 5 . 1 1 1 1 VAL HG13 H 1 1.047 0.02 . 2 . . . . . . . . 6591 1 6 . 1 1 1 1 VAL HG21 H 1 1.089 0.02 . 2 . . . . . . . . 6591 1 7 . 1 1 1 1 VAL HG22 H 1 1.089 0.02 . 2 . . . . . . . . 6591 1 8 . 1 1 1 1 VAL HG23 H 1 1.089 0.02 . 2 . . . . . . . . 6591 1 9 . 1 1 2 2 GLY H H 1 8.936 0.02 . 1 . . . . . . . . 6591 1 10 . 1 1 2 2 GLY HA2 H 1 4.223 0.02 . 2 . . . . . . . . 6591 1 11 . 1 1 2 2 GLY HA3 H 1 3.699 0.02 . 2 . . . . . . . . 6591 1 12 . 1 1 3 3 GLU H H 1 9.121 0.02 . 1 . . . . . . . . 6591 1 13 . 1 1 3 3 GLU HA H 1 4.122 0.02 . 1 . . . . . . . . 6591 1 14 . 1 1 3 3 GLU HB2 H 1 1.831 0.02 . 2 . . . . . . . . 6591 1 15 . 1 1 3 3 GLU HB3 H 1 1.700 0.02 . 2 . . . . . . . . 6591 1 16 . 1 1 3 3 GLU HG2 H 1 2.380 0.02 . 2 . . . . . . . . 6591 1 17 . 1 1 4 4 CYS H H 1 7.596 0.02 . 1 . . . . . . . . 6591 1 18 . 1 1 4 4 CYS HA H 1 4.356 0.02 . 1 . . . . . . . . 6591 1 19 . 1 1 4 4 CYS HB2 H 1 3.076 0.02 . 2 . . . . . . . . 6591 1 20 . 1 1 4 4 CYS HB3 H 1 2.755 0.02 . 2 . . . . . . . . 6591 1 21 . 1 1 5 5 VAL H H 1 8.479 0.02 . 1 . . . . . . . . 6591 1 22 . 1 1 5 5 VAL HA H 1 4.080 0.02 . 1 . . . . . . . . 6591 1 23 . 1 1 5 5 VAL HB H 1 1.859 0.02 . 1 . . . . . . . . 6591 1 24 . 1 1 5 5 VAL HG11 H 1 0.833 0.02 . 2 . . . . . . . . 6591 1 25 . 1 1 5 5 VAL HG12 H 1 0.833 0.02 . 2 . . . . . . . . 6591 1 26 . 1 1 5 5 VAL HG13 H 1 0.833 0.02 . 2 . . . . . . . . 6591 1 27 . 1 1 5 5 VAL HG21 H 1 0.853 0.02 . 2 . . . . . . . . 6591 1 28 . 1 1 5 5 VAL HG22 H 1 0.853 0.02 . 2 . . . . . . . . 6591 1 29 . 1 1 5 5 VAL HG23 H 1 0.853 0.02 . 2 . . . . . . . . 6591 1 30 . 1 1 6 6 ARG H H 1 9.448 0.02 . 1 . . . . . . . . 6591 1 31 . 1 1 6 6 ARG HA H 1 3.816 0.02 . 1 . . . . . . . . 6591 1 32 . 1 1 6 6 ARG HB2 H 1 1.807 0.02 . 2 . . . . . . . . 6591 1 33 . 1 1 6 6 ARG HB3 H 1 1.893 0.02 . 2 . . . . . . . . 6591 1 34 . 1 1 6 6 ARG HG2 H 1 1.547 0.02 . 2 . . . . . . . . 6591 1 35 . 1 1 6 6 ARG HE H 1 7.145 0.02 . 1 . . . . . . . . 6591 1 36 . 1 1 7 7 GLY H H 1 8.280 0.02 . 1 . . . . . . . . 6591 1 37 . 1 1 7 7 GLY HA2 H 1 4.078 0.02 . 2 . . . . . . . . 6591 1 38 . 1 1 7 7 GLY HA3 H 1 3.670 0.02 . 2 . . . . . . . . 6591 1 39 . 1 1 8 8 ARG H H 1 7.831 0.02 . 1 . . . . . . . . 6591 1 40 . 1 1 8 8 ARG HA H 1 4.636 0.02 . 1 . . . . . . . . 6591 1 41 . 1 1 8 8 ARG HB2 H 1 1.848 0.02 . 2 . . . . . . . . 6591 1 42 . 1 1 8 8 ARG HB3 H 1 1.854 0.02 . 2 . . . . . . . . 6591 1 43 . 1 1 8 8 ARG HG2 H 1 1.635 0.02 . 2 . . . . . . . . 6591 1 44 . 1 1 8 8 ARG HG3 H 1 1.533 0.02 . 2 . . . . . . . . 6591 1 45 . 1 1 8 8 ARG HD2 H 1 3.151 0.02 . 2 . . . . . . . . 6591 1 46 . 1 1 9 9 CYS H H 1 8.630 0.02 . 1 . . . . . . . . 6591 1 47 . 1 1 9 9 CYS HA H 1 5.232 0.02 . 1 . . . . . . . . 6591 1 48 . 1 1 9 9 CYS HB2 H 1 2.816 0.02 . 2 . . . . . . . . 6591 1 49 . 1 1 9 9 CYS HB3 H 1 2.191 0.02 . 2 . . . . . . . . 6591 1 50 . 1 1 10 10 PRO HA H 1 4.414 0.02 . 1 . . . . . . . . 6591 1 51 . 1 1 10 10 PRO HB2 H 1 2.357 0.02 . 2 . . . . . . . . 6591 1 52 . 1 1 10 10 PRO HB3 H 1 1.677 0.02 . 2 . . . . . . . . 6591 1 53 . 1 1 10 10 PRO HG2 H 1 1.968 0.02 . 2 . . . . . . . . 6591 1 54 . 1 1 10 10 PRO HD2 H 1 3.935 0.02 . 2 . . . . . . . . 6591 1 55 . 1 1 10 10 PRO HD3 H 1 3.416 0.02 . 2 . . . . . . . . 6591 1 56 . 1 1 11 11 SER H H 1 8.354 0.02 . 1 . . . . . . . . 6591 1 57 . 1 1 11 11 SER HA H 1 4.112 0.02 . 1 . . . . . . . . 6591 1 58 . 1 1 11 11 SER HB2 H 1 3.799 0.02 . 1 . . . . . . . . 6591 1 59 . 1 1 12 12 GLY H H 1 8.888 0.02 . 1 . . . . . . . . 6591 1 60 . 1 1 12 12 GLY HA2 H 1 4.175 0.02 . 2 . . . . . . . . 6591 1 61 . 1 1 12 12 GLY HA3 H 1 3.633 0.02 . 2 . . . . . . . . 6591 1 62 . 1 1 13 13 MET H H 1 7.891 0.02 . 1 . . . . . . . . 6591 1 63 . 1 1 13 13 MET HA H 1 4.592 0.02 . 1 . . . . . . . . 6591 1 64 . 1 1 13 13 MET HB2 H 1 2.011 0.02 . 2 . . . . . . . . 6591 1 65 . 1 1 13 13 MET HB3 H 1 1.691 0.02 . 2 . . . . . . . . 6591 1 66 . 1 1 13 13 MET HG2 H 1 2.276 0.02 . 2 . . . . . . . . 6591 1 67 . 1 1 14 14 CYS H H 1 9.284 0.02 . 1 . . . . . . . . 6591 1 68 . 1 1 14 14 CYS HA H 1 4.528 0.02 . 1 . . . . . . . . 6591 1 69 . 1 1 14 14 CYS HB2 H 1 2.330 0.02 . 2 . . . . . . . . 6591 1 70 . 1 1 14 14 CYS HB3 H 1 3.853 0.02 . 2 . . . . . . . . 6591 1 71 . 1 1 15 15 CYS H H 1 8.766 0.02 . 1 . . . . . . . . 6591 1 72 . 1 1 15 15 CYS HA H 1 4.768 0.02 . 1 . . . . . . . . 6591 1 73 . 1 1 15 15 CYS HB2 H 1 2.905 0.02 . 2 . . . . . . . . 6591 1 74 . 1 1 15 15 CYS HB3 H 1 2.833 0.02 . 2 . . . . . . . . 6591 1 75 . 1 1 16 16 SER H H 1 9.854 0.02 . 1 . . . . . . . . 6591 1 76 . 1 1 16 16 SER HA H 1 5.041 0.02 . 1 . . . . . . . . 6591 1 77 . 1 1 16 16 SER HB2 H 1 4.455 0.02 . 2 . . . . . . . . 6591 1 78 . 1 1 17 17 GLN H H 1 9.186 0.02 . 1 . . . . . . . . 6591 1 79 . 1 1 17 17 GLN HA H 1 4.081 0.02 . 1 . . . . . . . . 6591 1 80 . 1 1 17 17 GLN HB2 H 1 1.755 0.02 . 2 . . . . . . . . 6591 1 81 . 1 1 17 17 GLN HB3 H 1 1.642 0.02 . 2 . . . . . . . . 6591 1 82 . 1 1 17 17 GLN HG2 H 1 1.811 0.02 . 2 . . . . . . . . 6591 1 83 . 1 1 17 17 GLN HE21 H 1 6.784 0.02 . 2 . . . . . . . . 6591 1 84 . 1 1 17 17 GLN HE22 H 1 7.330 0.02 . 2 . . . . . . . . 6591 1 85 . 1 1 18 18 PFF H H 1 7.793 0.02 . 1 . . . . . . . . 6591 1 86 . 1 1 18 18 PFF HA H 1 4.742 0.02 . 1 . . . . . . . . 6591 1 87 . 1 1 18 18 PFF HB2 H 1 2.830 0.02 . 2 . . . . . . . . 6591 1 88 . 1 1 18 18 PFF HB3 H 1 3.576 0.02 . 2 . . . . . . . . 6591 1 89 . 1 1 18 18 PFF HE1 H 1 7.078 0.02 . 3 . . . . . . . . 6591 1 90 . 1 1 18 18 PFF HE2 H 1 7.078 0.02 . 3 . . . . . . . . 6591 1 91 . 1 1 18 18 PFF HD1 H 1 7.119 0.02 . 3 . . . . . . . . 6591 1 92 . 1 1 18 18 PFF HD2 H 1 7.119 0.02 . 3 . . . . . . . . 6591 1 93 . 1 1 19 19 GLY H H 1 7.962 0.02 . 1 . . . . . . . . 6591 1 94 . 1 1 19 19 GLY HA2 H 1 3.956 0.02 . 2 . . . . . . . . 6591 1 95 . 1 1 19 19 GLY HA3 H 1 3.554 0.02 . 2 . . . . . . . . 6591 1 96 . 1 1 20 20 PFF H H 1 7.520 0.02 . 1 . . . . . . . . 6591 1 97 . 1 1 20 20 PFF HA H 1 5.004 0.02 . 1 . . . . . . . . 6591 1 98 . 1 1 20 20 PFF HB2 H 1 3.054 0.02 . 2 . . . . . . . . 6591 1 99 . 1 1 20 20 PFF HB3 H 1 3.498 0.02 . 2 . . . . . . . . 6591 1 100 . 1 1 20 20 PFF HD1 H 1 7.113 0.02 . 3 . . . . . . . . 6591 1 101 . 1 1 20 20 PFF HD2 H 1 7.113 0.02 . 3 . . . . . . . . 6591 1 102 . 1 1 21 21 CYS H H 1 8.887 0.02 . 1 . . . . . . . . 6591 1 103 . 1 1 21 21 CYS HA H 1 5.585 0.02 . 1 . . . . . . . . 6591 1 104 . 1 1 21 21 CYS HB2 H 1 2.793 0.02 . 2 . . . . . . . . 6591 1 105 . 1 1 22 22 GLY H H 1 8.473 0.02 . 1 . . . . . . . . 6591 1 106 . 1 1 22 22 GLY HA2 H 1 3.592 0.02 . 2 . . . . . . . . 6591 1 107 . 1 1 22 22 GLY HA3 H 1 1.795 0.02 . 2 . . . . . . . . 6591 1 108 . 1 1 23 23 LYS H H 1 8.100 0.02 . 1 . . . . . . . . 6591 1 109 . 1 1 23 23 LYS HA H 1 4.926 0.02 . 1 . . . . . . . . 6591 1 110 . 1 1 23 23 LYS HB2 H 1 1.624 0.02 . 2 . . . . . . . . 6591 1 111 . 1 1 23 23 LYS HG2 H 1 1.429 0.02 . 2 . . . . . . . . 6591 1 112 . 1 1 23 23 LYS HG3 H 1 1.291 0.02 . 2 . . . . . . . . 6591 1 113 . 1 1 24 24 GLY H H 1 8.359 0.02 . 1 . . . . . . . . 6591 1 114 . 1 1 24 24 GLY HA2 H 1 4.539 0.02 . 2 . . . . . . . . 6591 1 115 . 1 1 24 24 GLY HA3 H 1 3.930 0.02 . 2 . . . . . . . . 6591 1 116 . 1 1 25 25 PRO HA H 1 4.254 0.02 . 1 . . . . . . . . 6591 1 117 . 1 1 25 25 PRO HB2 H 1 2.287 0.02 . 2 . . . . . . . . 6591 1 118 . 1 1 25 25 PRO HB3 H 1 1.912 0.02 . 2 . . . . . . . . 6591 1 119 . 1 1 25 25 PRO HG2 H 1 2.017 0.02 . 2 . . . . . . . . 6591 1 120 . 1 1 25 25 PRO HD2 H 1 3.623 0.02 . 2 . . . . . . . . 6591 1 121 . 1 1 25 25 PRO HD3 H 1 3.828 0.02 . 2 . . . . . . . . 6591 1 122 . 1 1 26 26 LYS H H 1 8.909 0.02 . 1 . . . . . . . . 6591 1 123 . 1 1 26 26 LYS HA H 1 3.976 0.02 . 1 . . . . . . . . 6591 1 124 . 1 1 26 26 LYS HB2 H 1 1.769 0.02 . 2 . . . . . . . . 6591 1 125 . 1 1 26 26 LYS HB3 H 1 1.398 0.02 . 2 . . . . . . . . 6591 1 126 . 1 1 26 26 LYS HG2 H 1 1.442 0.02 . 2 . . . . . . . . 6591 1 127 . 1 1 26 26 LYS HG3 H 1 1.280 0.02 . 2 . . . . . . . . 6591 1 128 . 1 1 26 26 LYS HD2 H 1 1.625 0.02 . 2 . . . . . . . . 6591 1 129 . 1 1 27 27 TYR H H 1 7.512 0.02 . 1 . . . . . . . . 6591 1 130 . 1 1 27 27 TYR HA H 1 4.089 0.02 . 1 . . . . . . . . 6591 1 131 . 1 1 27 27 TYR HB2 H 1 2.443 0.02 . 2 . . . . . . . . 6591 1 132 . 1 1 27 27 TYR HB3 H 1 2.946 0.02 . 2 . . . . . . . . 6591 1 133 . 1 1 27 27 TYR HE1 H 1 6.602 0.02 . 1 . . . . . . . . 6591 1 134 . 1 1 27 27 TYR HE2 H 1 6.602 0.02 . 1 . . . . . . . . 6591 1 135 . 1 1 27 27 TYR HD1 H 1 7.195 0.02 . 1 . . . . . . . . 6591 1 136 . 1 1 27 27 TYR HD2 H 1 7.195 0.02 . 1 . . . . . . . . 6591 1 137 . 1 1 28 28 CYS H H 1 8.516 0.02 . 1 . . . . . . . . 6591 1 138 . 1 1 28 28 CYS HA H 1 4.481 0.02 . 1 . . . . . . . . 6591 1 139 . 1 1 28 28 CYS HB2 H 1 3.195 0.02 . 2 . . . . . . . . 6591 1 140 . 1 1 28 28 CYS HB3 H 1 2.714 0.02 . 2 . . . . . . . . 6591 1 141 . 1 1 29 29 GLY H H 1 7.914 0.02 . 1 . . . . . . . . 6591 1 142 . 1 1 29 29 GLY HA2 H 1 3.974 0.02 . 2 . . . . . . . . 6591 1 143 . 1 1 30 30 ARG H H 1 8.318 0.02 . 1 . . . . . . . . 6591 1 144 . 1 1 30 30 ARG HA H 1 4.255 0.02 . 1 . . . . . . . . 6591 1 145 . 1 1 30 30 ARG HB2 H 1 1.816 0.02 . 2 . . . . . . . . 6591 1 146 . 1 1 30 30 ARG HB3 H 1 1.694 0.02 . 2 . . . . . . . . 6591 1 147 . 1 1 30 30 ARG HG2 H 1 1.599 0.02 . 2 . . . . . . . . 6591 1 148 . 1 1 30 30 ARG HD2 H 1 3.144 0.02 . 2 . . . . . . . . 6591 1 stop_ save_