data_6637 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 6637 _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 2005-05-16 _Entry.Accession_date 2005-05-16 _Entry.Last_release_date 2005-05-16 _Entry.Original_release_date 2005-05-16 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 3.2.0.16 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _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.ORCID _Entry_author.Entry_ID 1 M. Chavez . Isabel . . 6637 2 Cecilia Andreu . . . . 6637 3 Paloma Vidal . . . . 6637 4 Felix Freire . . . . 6637 5 Nuria Aboitiz . . . . 6637 6 Patrick Groves . . . . 6637 7 Juan Asensio . L. . . 6637 8 Gregorio Asensio . . . . 6637 9 Michiro Muraki . . . . 6637 10 F. Canada . Javier . . 6637 11 Jesus Jimenez-Barbero . . . . 6637 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 6637 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 150 6637 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 3 . . 2008-07-17 . update BMRB 'Updating non-standard residue' 6637 2 . . 2005-12-16 . update author 'update the chemical shifts' 6637 1 . . 2005-05-25 . original author 'original release' 6637 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 6591 AcAMP2F18Pff/Y20Pff 6637 BMRB 6639 'AcAMP2F18W mutant' 6637 BMRB 6647 AcAMP2F18Wb 6637 BMRB 6656 AcAMP2F18Pff/F20Pfff 6637 BMRB 6657 'AcAMP2F18Nal mutant' 6637 PDB 1MMC 'BMRB Entry Tracking System' 6637 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 6637 _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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 M. Chavez . Isabel . . 6637 1 2 Cecilia Andreu . . . . 6637 1 3 Paloma Vidal . . . . 6637 1 4 Nuria Aboitiz . . . . 6637 1 5 Felix Freire . . . . 6637 1 6 Patrick Groves . . . . 6637 1 7 Juan Asensio . L. . . 6637 1 8 Gregorio Asensio . . . . 6637 1 9 Michiro Muraki . . . . 6637 1 10 F. Canada . Javier . . 6637 1 11 Jesus Jimenez-Barbero . . . . 6637 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID AcAMP2 6637 1 Chitin 6637 1 'Molecular Dynamics' 6637 1 NMR 6637 1 'carbohydrate binding' 6637 1 hevein 6637 1 'molecular recognition' 6637 1 protein 6637 1 stop_ save_ save_reference-1 _Citation.Sf_category citations _Citation.Sf_framecode reference-1 _Citation.Entry_ID 6637 _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 P. 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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'J. C.' Martins J. C. . . 6637 2 2 D. Maes D. . . . 6637 2 3 R. Loris R. . . . 6637 2 4 'H. A.' Pepermans H. A. . . 6637 2 5 L. Wyns L. . . . 6637 2 6 R. Willem R. . . . 6637 2 7 P. Verheyden P. . . . 6637 2 stop_ save_ save_reference-2 _Citation.Sf_category citations _Citation.Sf_framecode reference-2 _Citation.Entry_ID 6637 _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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Michiro Muraki M. . . . 6637 3 stop_ save_ save_reference-3 _Citation.Sf_category citations _Citation.Sf_framecode reference-3 _Citation.Entry_ID 6637 _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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Nuria Aboitiz N. . . . 6637 4 2 Miquel Vila-Perello M. . . . 6637 4 3 Patrick Groves P. . . . 6637 4 4 'Juan Luis' Asensio J. L. . . 6637 4 5 David Andreu D. . . . 6637 4 6 'Francisco Javier' Canada F. J. . . 6637 4 7 Jesus Jimenez-Barbero J. . . . 6637 4 stop_ save_ save_reference-4 _Citation.Sf_category citations _Citation.Sf_framecode reference-4 _Citation.Entry_ID 6637 _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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'J. L.' Asensio J. L. . . 6637 5 2 'H. C.' Siebert H. C. . . 6637 5 3 'C. W.' 'von Der Lieth' C. W. . . 6637 5 4 J. Laynez J. . . . 6637 5 5 M. Bruix M. . . . 6637 5 6 'U. M.' Soedjanaamadja U. M. . . 6637 5 7 'J. J.' Beintema J. J. . . 6637 5 8 'F. J.' Canada F. J. . . 6637 5 9 'H. J.' Gabius H. J. . . 6637 5 10 J. Jimenez-Barbero J. . . . 6637 5 stop_ save_ save_reference-5 _Citation.Sf_category citations _Citation.Sf_framecode reference-5 _Citation.Entry_ID 6637 _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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'J. L.' Asensio J. L. . . 6637 6 2 'F. J.' Canada F. J. . . 6637 6 3 'H. C.' Siebert H. C. . . 6637 6 4 J. Laynez J. . . . 6637 6 5 A. Poveda A. . . . 6637 6 6 'P. M.' Nieto P. M. . . 6637 6 7 'U. M.' Soedjanaamadja U. M. . . 6637 6 8 'H. J.' Gabius H. J. . . 6637 6 9 J. Jimenez-Barbero J. . . . 6637 6 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_AcAMP2F18Nalb _Assembly.Sf_category assembly _Assembly.Sf_framecode system_AcAMP2F18Nalb _Assembly.Entry_ID 6637 _Assembly.ID 1 _Assembly.Name 'AcAMP2F18Nalb 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 6637 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 AcAMP2F18Nalb 1 $AcAMP2F18Nalb . . . native . . . . . 6637 1 2 triacetylchitotriose 2 $CTO . . . native . . . . . 6637 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_asym_ID_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_asym_ID_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 . . . . . . . . . . . . 6637 1 2 disulfide single . 1 . 1 CYS 9 9 SG . 1 . 1 CYS 21 21 SG . . . . . . . . . . . . 6637 1 3 disulfide single . 1 . 1 CYS 14 14 SG . 1 . 1 CYS 28 28 SG . . . . . . . . . . . . 6637 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 yes PDB 1MMC . . . . . ; Residue Phe18 have been mutated to beta-(2-naphthyl)-alanine in the molecule studied here. ; 6637 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID AcAMP2F18Nalb abbreviation 6637 1 'AcAMP2F18Nalb mutant' system 6637 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'chitin binding lectin' 6637 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_AcAMP2F18Nalb _Entity.Sf_category entity _Entity.Sf_framecode AcAMP2F18Nalb _Entity.Entry_ID 6637 _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 ; VGECVRGRCPSGMCCSQXGY 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 3240 _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, Nal18, Y20 and Y27. ; _Entity.DB_query_date 2008-03-24 _Entity.DB_query_revised_last_date 2008-03-03 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 6657 . AcAMP2 . . . . . 100.00 30 100 100 4e-12 . . . . 6637 1 2 no PDB 1ZWU . 'A Chain A, 30 Nmr Structures Of Acamp2-LikePeptide With Non Natural Beta-(2-Naphthyl)-AlanineResidue' . . . . . 100.00 30 100 100 10e-12 . . . . 6637 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID AcAMP2 common 6637 1 AcAMP2F18Nalb abbreviation 6637 1 'AcAMP2F18Nalb mutant' variant 6637 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 . 6637 1 2 . GLY . 6637 1 3 . GLU . 6637 1 4 . CYS . 6637 1 5 . VAL . 6637 1 6 . ARG . 6637 1 7 . GLY . 6637 1 8 . ARG . 6637 1 9 . CYS . 6637 1 10 . PRO . 6637 1 11 . SER . 6637 1 12 . GLY . 6637 1 13 . MET . 6637 1 14 . CYS . 6637 1 15 . CYS . 6637 1 16 . SER . 6637 1 17 . GLN . 6637 1 18 . NAL . 6637 1 19 . GLY . 6637 1 20 . TYR . 6637 1 21 . CYS . 6637 1 22 . GLY . 6637 1 23 . LYS . 6637 1 24 . GLY . 6637 1 25 . PRO . 6637 1 26 . LYS . 6637 1 27 . TYR . 6637 1 28 . CYS . 6637 1 29 . GLY . 6637 1 30 . ARG . 6637 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 6637 1 . GLY 2 2 6637 1 . GLU 3 3 6637 1 . CYS 4 4 6637 1 . VAL 5 5 6637 1 . ARG 6 6 6637 1 . GLY 7 7 6637 1 . ARG 8 8 6637 1 . CYS 9 9 6637 1 . PRO 10 10 6637 1 . SER 11 11 6637 1 . GLY 12 12 6637 1 . MET 13 13 6637 1 . CYS 14 14 6637 1 . CYS 15 15 6637 1 . SER 16 16 6637 1 . GLN 17 17 6637 1 . NAL 18 18 6637 1 . GLY 19 19 6637 1 . TYR 20 20 6637 1 . CYS 21 21 6637 1 . GLY 22 22 6637 1 . LYS 23 23 6637 1 . GLY 24 24 6637 1 . PRO 25 25 6637 1 . LYS 26 26 6637 1 . TYR 27 27 6637 1 . CYS 28 28 6637 1 . GLY 29 29 6637 1 . ARG 30 30 6637 1 stop_ save_ save_CTO _Entity.Sf_category entity _Entity.Sf_framecode CTO _Entity.Entry_ID 6637 _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 . 6637 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 6637 _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.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.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $AcAMP2F18Nalb . 3567 organism . 'Amaranthus caudatus' 'inca wheat, love-lies bleendig, tassel flower' . . Eukaryota Viridiplantae Amaranthus caudatus . . . seed . . . . . . . . . 6637 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 6637 _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_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.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $AcAMP2F18Nalb . 'chemical synthesis' . . . . . . . . . . . . . . . ; The residue Phe18 of native AcAMP2 was changed to beta-(2-naphtyl)-alanine. The aminoacid was manually assembled by solid phase synthesis using Fmoc chemistry according to satandard protocols. ; 6637 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_NAL _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_NAL _Chem_comp.Entry_ID 6637 _Chem_comp.ID NAL _Chem_comp.Provenance PDB _Chem_comp.Name BETA-(2-NAPHTHYL)-ALANINE _Chem_comp.Type 'L-peptide linking' _Chem_comp.BMRB_code . _Chem_comp.PDB_code NAL _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 A _Chem_comp.Three_letter_code NAL _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.Atom_nomenclature_source . _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 ALA _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 'C13 H13 N O2' _Chem_comp.Formula_weight 215.248 _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 2ITK _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 Mon Aug 8 12:36:19 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 InChI=1S/C13H13NO2/c14-12(13(15)16)8-9-5-6-10-3-1-2-4-11(10)7-9/h1-7,12H,8,14H2,(H,15,16)/t12-/m0/s1 InChI InChI 1.03 6637 NAL JPZXHKDZASGCLU-LBPRGKRZSA-N InChIKey InChI 1.03 6637 NAL N[C@@H](Cc1ccc2ccccc2c1)C(O)=O SMILES_CANONICAL CACTVS 3.370 6637 NAL N[CH](Cc1ccc2ccccc2c1)C(O)=O SMILES CACTVS 3.370 6637 NAL O=C(O)C(N)Cc2ccc1c(cccc1)c2 SMILES ACDLabs 12.01 6637 NAL c1ccc2cc(ccc2c1)CC(C(=O)O)N SMILES 'OpenEye OEToolkits' 1.7.0 6637 NAL c1ccc2cc(ccc2c1)C[C@@H](C(=O)O)N SMILES_CANONICAL 'OpenEye OEToolkits' 1.7.0 6637 NAL 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-(naphthalen-2-yl)propanoic acid (non-preferred name)' 'SYSTEMATIC NAME' ACDLabs 12.01 6637 NAL '(2S)-2-azanyl-3-naphthalen-2-yl-propanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.7.0 6637 NAL 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 C1 . C1 . . C . . N 0 . . . . yes no . . . . 40.838 . 28.486 . 22.485 . -0.616 0.617 -0.580 1 . 6637 NAL C2 . C2 . . C . . N 0 . . . . yes no . . . . 39.512 . 28.736 . 22.947 . 0.209 -0.463 -0.507 2 . 6637 NAL C3 . C3 . . C . . N 0 . . . . yes no . . . . 38.444 . 28.060 . 22.265 . -0.277 -1.713 -0.129 3 . 6637 NAL C4 . C4 . . C . . N 0 . . . . yes no . . . . 38.645 . 27.166 . 21.158 . -1.592 -1.890 0.178 4 . 6637 NAL C4A . C4A . . C . . N 0 . . . . yes no . . . . 39.985 . 26.941 . 20.710 . -2.474 -0.799 0.113 5 . 6637 NAL C5 . C5 . . C . . N 0 . . . . yes no . . . . 40.308 . 26.077 . 19.612 . -3.837 -0.943 0.422 6 . 6637 NAL C6 . C6 . . C . . N 0 . . . . yes no . . . . 41.647 . 25.860 . 19.177 . -4.662 0.137 0.348 7 . 6637 NAL C7 . C7 . . C . . N 0 . . . . yes no . . . . 42.712 . 26.529 . 19.849 . -4.176 1.387 -0.030 8 . 6637 NAL C8 . C8 . . C . . N 0 . . . . yes no . . . . 42.483 . 27.414 . 20.956 . -2.862 1.564 -0.337 9 . 6637 NAL C8A . C8A . . C . . N 0 . . . . yes no . . . . 41.111 . 27.613 . 21.374 . -1.978 0.474 -0.266 10 . 6637 NAL C9 . C9 . . C . . N 0 . . . . no no . . . . 39.099 . 29.637 . 24.117 . 1.670 -0.304 -0.839 11 . 6637 NAL CA . CA . . C . . S 0 . . . . no no . . . . 39.037 . 28.749 . 25.417 . 2.446 0.058 0.429 12 . 6637 NAL C . C . . C . . N 0 . . . . no no . . . . 39.308 . 29.631 . 26.639 . 3.921 0.096 0.122 13 . 6637 NAL N . N . . N . . N 0 . . . . no no . . . . 37.817 . 27.857 . 25.721 . 2.011 1.377 0.908 14 . 6637 NAL O . O . . O . . N 0 . . . . no no . . . . 38.129 . 30.095 . 27.173 . 4.471 1.155 -0.068 15 . 6637 NAL OXT . OXT . . O . . N 0 . . . . no yes . . . . 40.467 . 29.850 . 27.268 . 4.623 -1.046 0.059 16 . 6637 NAL H1 . H1 . . H . . N 0 . . . . no no . . . . 41.665 . 28.968 . 22.986 . -0.225 1.580 -0.874 17 . 6637 NAL H3 . H3 . . H . . N 0 . . . . no no . . . . 37.433 . 28.233 . 22.603 . 0.399 -2.553 -0.078 18 . 6637 NAL H4 . H4 . . H . . N 0 . . . . no no . . . . 37.809 . 26.678 . 20.678 . -1.954 -2.865 0.468 19 . 6637 NAL H5 . H5 . . H . . N 0 . . . . no no . . . . 39.506 . 25.572 . 19.095 . -4.228 -1.906 0.716 20 . 6637 NAL H6 . H6 . . H . . N 0 . . . . no no . . . . 41.853 . 25.198 . 18.349 . -5.710 0.023 0.586 21 . 6637 NAL H7 . H7 . . H . . N 0 . . . . no no . . . . 43.725 . 26.364 . 19.514 . -4.852 2.227 -0.081 22 . 6637 NAL H8 . H8 . . H . . N 0 . . . . no no . . . . 43.301 . 27.911 . 21.457 . -2.500 2.539 -0.629 23 . 6637 NAL H91 . H91 . . H . . N 0 . . . . no no . . . . 39.835 . 30.444 . 24.248 . 2.054 -1.240 -1.245 24 . 6637 NAL H92 . H92 . . H . . N 0 . . . . no no . . . . 38.113 . 30.082 . 23.919 . 1.791 0.488 -1.578 25 . 6637 NAL HA . HA . . H . . N 0 . . . . no no . . . . 39.807 . 27.998 . 25.189 . 2.254 -0.690 1.198 26 . 6637 NAL H . H . . H . . N 0 . . . . no no . . . . 37.964 . 27.374 . 26.584 . 2.462 1.611 1.780 27 . 6637 NAL H2 . H2 . . H . . N 0 . . . . no yes . . . . 36.998 . 28.426 . 25.793 . 2.179 2.088 0.212 28 . 6637 NAL HXT . HXT . . H . . N 0 . . . . no yes . . . . 40.307 . 30.338 . 28.067 . 5.566 -0.971 -0.140 29 . 6637 NAL 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 . DOUB C6 C5 yes N 1 . 6637 NAL 2 . SING C6 C7 yes N 2 . 6637 NAL 3 . SING C5 C4A yes N 3 . 6637 NAL 4 . DOUB C7 C8 yes N 4 . 6637 NAL 5 . DOUB C4A C4 yes N 5 . 6637 NAL 6 . SING C4A C8A yes N 6 . 6637 NAL 7 . SING C8 C8A yes N 7 . 6637 NAL 8 . SING C4 C3 yes N 8 . 6637 NAL 9 . DOUB C8A C1 yes N 9 . 6637 NAL 10 . DOUB C3 C2 yes N 10 . 6637 NAL 11 . SING C1 C2 yes N 11 . 6637 NAL 12 . SING C2 C9 no N 12 . 6637 NAL 13 . SING C9 CA no N 13 . 6637 NAL 14 . SING CA N no N 14 . 6637 NAL 15 . SING CA C no N 15 . 6637 NAL 16 . DOUB C O no N 16 . 6637 NAL 17 . SING C OXT no N 17 . 6637 NAL 18 . SING C1 H1 no N 18 . 6637 NAL 19 . SING C3 H3 no N 19 . 6637 NAL 20 . SING C4 H4 no N 20 . 6637 NAL 21 . SING C5 H5 no N 21 . 6637 NAL 22 . SING C6 H6 no N 22 . 6637 NAL 23 . SING C7 H7 no N 23 . 6637 NAL 24 . SING C8 H8 no N 24 . 6637 NAL 25 . SING C9 H91 no N 25 . 6637 NAL 26 . SING C9 H92 no N 26 . 6637 NAL 27 . SING CA HA no N 27 . 6637 NAL 28 . SING N H no N 28 . 6637 NAL 29 . SING N H2 no N 29 . 6637 NAL 30 . SING OXT HXT no N 30 . 6637 NAL stop_ save_ save_chem_comp_CTO _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CTO _Chem_comp.Entry_ID 6637 _Chem_comp.ID CTO _Chem_comp.Provenance PDB _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.Atom_nomenclature_source . _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 Mon Aug 8 12:37:48 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 6637 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 6637 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 6637 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 6637 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 6637 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 6637 CTO WZZVUHWLNMNWLW-VFCSDQTKSA-N InChIKey InChI 1.03 6637 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 6637 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 6637 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 . 6637 CTO C21 . C21 . . C . . R 0 . . . . no no . . . . 14.058 . -11.405 . 34.260 . 1.129 -0.639 -5.030 2 . 6637 CTO N21 . N21 . . N . . N 0 . . . . no no . . . . 14.331 . -11.261 . 35.711 . 2.361 -1.302 -4.598 3 . 6637 CTO C71 . C71 . . C . . N 0 . . . . no no . . . . 13.576 . -11.882 . 36.677 . 2.329 -2.587 -4.193 4 . 6637 CTO O71 . O71 . . O . . N 0 . . . . no no . . . . 12.553 . -12.539 . 36.429 . 1.279 -3.194 -4.186 5 . 6637 CTO C81 . C81 . . C . . N 0 . . . . no no . . . . 14.064 . -11.734 . 38.099 . 3.597 -3.269 -3.748 6 . 6637 CTO C31 . C31 . . C . . R 0 . . . . no no . . . . 14.913 . -12.541 . 33.636 . 1.461 0.426 -6.081 7 . 6637 CTO O31 . O31 . . O . . N 0 . . . . no no . . . . 14.640 . -13.793 . 34.299 . 1.948 -0.201 -7.268 8 . 6637 CTO C41 . C41 . . C . . S 0 . . . . no no . . . . 14.589 . -12.674 . 32.143 . 0.185 1.212 -6.401 9 . 6637 CTO O41 . O41 . . O . . N 0 . . . . no no . . . . 15.377 . -13.731 . 31.540 . 0.498 2.305 -7.266 10 . 6637 CTO C51 . C51 . . C . . R 0 . . . . no no . . . . 14.887 . -11.341 . 31.428 . -0.411 1.747 -5.097 11 . 6637 CTO O51 . O51 . . O . . N 0 . . . . no no . . . . 14.099 . -10.256 . 32.057 . -0.752 0.658 -4.240 12 . 6637 CTO C61 . C61 . . C . . N 0 . . . . no no . . . . 14.541 . -11.368 . 29.942 . -1.668 2.561 -5.410 13 . 6637 CTO O61 . O61 . . O . . N 0 . . . . no no . . . . 13.212 . -11.809 . 29.707 . -2.223 3.067 -4.194 14 . 6637 CTO C12 . C12 . . C . . S 0 . . . . no no . . . . 13.364 . -5.213 . 35.038 . -0.984 -0.342 1.074 15 . 6637 CTO C22 . C22 . . C . . R 0 . . . . no no . . . . 12.424 . -5.739 . 33.926 . -2.082 -0.093 0.038 16 . 6637 CTO N22 . N22 . . N . . N 0 . . . . no no . . . . 11.141 . -5.015 . 33.922 . -3.341 -0.677 0.508 17 . 6637 CTO C72 . C72 . . C . . N 0 . . . . no no . . . . 10.744 . -4.173 . 32.925 . -4.194 0.062 1.243 18 . 6637 CTO O72 . O72 . . O . . N 0 . . . . no no . . . . 11.392 . -3.984 . 31.884 . -3.920 1.211 1.515 19 . 6637 CTO C82 . C82 . . C . . N 0 . . . . no no . . . . 9.435 . -3.456 . 33.157 . -5.489 -0.538 1.726 20 . 6637 CTO C32 . C32 . . C . . R 0 . . . . no no . . . . 12.218 . -7.258 . 34.090 . -1.676 -0.749 -1.286 21 . 6637 CTO O32 . O32 . . O . . N 0 . . . . no no . . . . 11.374 . -7.736 . 33.029 . -2.617 -0.402 -2.305 22 . 6637 CTO C42 . C42 . . C . . S 0 . . . . no no . . . . 13.554 . -7.991 . 34.085 . -0.284 -0.240 -1.677 23 . 6637 CTO O42 . O42 . . O . . N 0 . . . . no no . . . . 13.290 . -9.435 . 34.258 . 0.178 -0.946 -2.830 24 . 6637 CTO C52 . C52 . . C . . R 0 . . . . no no . . . . 14.422 . -7.413 . 35.267 . 0.678 -0.475 -0.511 25 . 6637 CTO O52 . O52 . . O . . N 0 . . . . no no . . . . 14.598 . -5.976 . 35.081 . 0.236 0.249 0.634 26 . 6637 CTO C62 . C62 . . C . . N 0 . . . . no no . . . . 15.829 . -7.981 . 35.360 . 2.078 -0.000 -0.905 27 . 6637 CTO O62 . O62 . . O . . N 0 . . . . no no . . . . 16.591 . -7.529 . 34.246 . 2.999 -0.312 0.141 28 . 6637 CTO C13 . C13 . . C . . R 0 . . . . no no . . . . 13.947 . -0.192 . 37.088 . 0.369 -0.290 6.019 29 . 6637 CTO O13 . O13 . . O . . N 0 . . . . no yes . . . . 14.158 . 0.813 . 38.412 . 1.214 -0.696 7.098 30 . 6637 CTO C23 . C23 . . C . . R 0 . . . . no no . . . . 15.181 . -1.105 . 36.926 . 1.156 0.615 5.069 31 . 6637 CTO N23 . N23 . . N . . N 0 . . . . no no . . . . 16.391 . -0.296 . 36.724 . 1.647 1.785 5.802 32 . 6637 CTO C73 . C73 . . C . . N 0 . . . . no no . . . . 17.543 . -0.434 . 37.417 . 2.854 1.749 6.399 33 . 6637 CTO O73 . O73 . . O . . N 0 . . . . no no . . . . 17.639 . -1.026 . 38.495 . 3.535 0.747 6.330 34 . 6637 CTO C83 . C83 . . C . . N 0 . . . . no no . . . . 18.749 . 0.207 . 36.792 . 3.359 2.952 7.153 35 . 6637 CTO C33 . C33 . . C . . R 0 . . . . no no . . . . 14.950 . -2.038 . 35.740 . 0.235 1.071 3.932 36 . 6637 CTO O33 . O33 . . O . . N 0 . . . . no no . . . . 16.078 . -2.913 . 35.603 . 0.989 1.792 2.956 37 . 6637 CTO C43 . C43 . . C . . S 0 . . . . no no . . . . 13.674 . -2.858 . 35.967 . -0.393 -0.167 3.284 38 . 6637 CTO O43 . O43 . . O . . N 0 . . . . no no . . . . 13.439 . -3.729 . 34.841 . -1.369 0.237 2.323 39 . 6637 CTO C53 . C53 . . C . . R 0 . . . . no no . . . . 12.472 . -1.894 . 36.119 . -1.063 -1.014 4.369 40 . 6637 CTO O53 . O53 . . O . . N 0 . . . . no no . . . . 12.735 . -0.983 . 37.239 . -0.088 -1.444 5.317 41 . 6637 CTO C63 . C63 . . C . . N 0 . . . . no no . . . . 11.146 . -2.602 . 36.397 . -1.720 -2.236 3.725 42 . 6637 CTO O63 . O63 . . O . . N 0 . . . . no no . . . . 11.102 . -3.142 . 37.697 . -2.432 -2.974 4.720 43 . 6637 CTO H11 . H11 . . H . . N 0 . . . . no no . . . . 15.371 . -9.578 . 33.422 . 1.134 0.788 -3.417 44 . 6637 CTO H21 . H21 . . H . . N 0 . . . . no no . . . . 12.973 . -11.649 . 34.168 . 0.450 -1.375 -5.460 45 . 6637 CTO HNL . HNL . . H . . N 0 . . . . no no . . . . 15.096 . -10.691 . 36.072 . 3.201 -0.816 -4.603 46 . 6637 CTO H811 . H811 . . H . . N 0 . . . . no no . . . . 13.451 . -12.237 . 38.882 . 3.374 -4.297 -3.459 47 . 6637 CTO H812 . H812 . . H . . N 0 . . . . no no . . . . 15.123 . -12.073 . 38.171 . 4.316 -3.270 -4.567 48 . 6637 CTO H813 . H813 . . H . . N 0 . . . . no no . . . . 14.181 . -10.653 . 38.347 . 4.017 -2.735 -2.896 49 . 6637 CTO H31 . H31 . . H . . N 0 . . . . no no . . . . 15.991 . -12.288 . 33.763 . 2.219 1.104 -5.688 50 . 6637 CTO HOV . HOV . . H . . N 0 . . . . no no . . . . 15.163 . -14.488 . 33.917 . 2.131 0.504 -7.903 51 . 6637 CTO H41 . H41 . . H . . N 0 . . . . no no . . . . 13.508 . -12.927 . 32.036 . -0.535 0.556 -6.889 52 . 6637 CTO HO4 . HO4 . . H . . N 0 . . . . no no . . . . 15.176 . -13.813 . 30.615 . -0.329 2.775 -7.435 53 . 6637 CTO H51 . H51 . . H . . N 0 . . . . no no . . . . 15.984 . -11.168 . 31.526 . 0.318 2.384 -4.599 54 . 6637 CTO H611 . H611 . . H . . N 0 . . . . no no . . . . 14.726 . -10.376 . 29.467 . -1.408 3.393 -6.065 55 . 6637 CTO H612 . H612 . . H . . N 0 . . . . no no . . . . 15.275 . -11.979 . 29.368 . -2.400 1.923 -5.906 56 . 6637 CTO HO6 . HO6 . . H . . N 0 . . . . no no . . . . 12.996 . -11.825 . 28.781 . -3.011 3.572 -4.436 57 . 6637 CTO H12 . H12 . . H . . N 0 . . . . no no . . . . 12.992 . -5.371 . 36.077 . -0.842 -1.415 1.201 58 . 6637 CTO H22 . H22 . . H . . N 0 . . . . no no . . . . 12.902 . -5.553 . 32.936 . -2.211 0.978 -0.109 59 . 6637 CTO HNM . HNM . . H . . N 0 . . . . no no . . . . 10.464 . -5.105 . 34.680 . -3.560 -1.597 0.290 60 . 6637 CTO H821 . H821 . . H . . N 0 . . . . no no . . . . 9.110 . -2.767 . 32.342 . -6.043 0.204 2.300 61 . 6637 CTO H822 . H822 . . H . . N 0 . . . . no no . . . . 8.629 . -4.195 . 33.374 . -6.085 -0.854 0.870 62 . 6637 CTO H823 . H823 . . H . . N 0 . . . . no no . . . . 9.468 . -2.907 . 34.127 . -5.276 -1.400 2.359 63 . 6637 CTO H32 . H32 . . H . . N 0 . . . . no no . . . . 11.728 . -7.456 . 35.071 . -1.649 -1.832 -1.167 64 . 6637 CTO HOW . HOW . . H . . N 0 . . . . no no . . . . 11.247 . -8.672 . 33.130 . -3.476 -0.741 -2.018 65 . 6637 CTO H42 . H42 . . H . . N 0 . . . . no no . . . . 14.108 . -7.848 . 33.128 . -0.334 0.826 -1.898 66 . 6637 CTO H52 . H52 . . H . . N 0 . . . . no no . . . . 13.861 . -7.689 . 36.190 . 0.709 -1.540 -0.277 67 . 6637 CTO H621 . H621 . . H . . N 0 . . . . no no . . . . 16.318 . -7.741 . 36.332 . 2.387 -0.501 -1.822 68 . 6637 CTO H622 . H622 . . H . . N 0 . . . . no no . . . . 15.831 . -9.092 . 35.451 . 2.063 1.077 -1.067 69 . 6637 CTO HO2 . HO2 . . H . . N 0 . . . . no no . . . . 17.470 . -7.884 . 34.304 . 3.867 0.003 -0.146 70 . 6637 CTO H13 . H13 . . H . . N 0 . . . . no no . . . . 13.839 . 0.431 . 36.169 . -0.486 0.256 6.415 71 . 6637 CTO HOD . HOD . . H . . N 0 . . . . no no . . . . 13.398 . 1.374 . 38.511 . 0.681 -1.263 7.672 72 . 6637 CTO H23 . H23 . . H . . N 0 . . . . no no . . . . 15.326 . -1.711 . 37.850 . 2.001 0.064 4.656 73 . 6637 CTO HNN . HNN . . H . . N 0 . . . . no no . . . . 16.436 . 0.444 . 36.024 . 1.102 2.586 5.857 74 . 6637 CTO H831 . H831 . . H . . N 0 . . . . no no . . . . 19.699 . 0.093 . 37.363 . 4.345 2.737 7.564 75 . 6637 CTO H832 . H832 . . H . . N 0 . . . . no no . . . . 18.882 . -0.164 . 35.749 . 3.426 3.804 6.475 76 . 6637 CTO H833 . H833 . . H . . N 0 . . . . no no . . . . 18.549 . 1.285 . 36.592 . 2.670 3.188 7.965 77 . 6637 CTO H33 . H33 . . H . . N 0 . . . . no no . . . . 14.831 . -1.438 . 34.807 . -0.549 1.711 4.335 78 . 6637 CTO HOX . HOX . . H . . N 0 . . . . no no . . . . 15.934 . -3.493 . 34.864 . 1.365 2.561 3.406 79 . 6637 CTO H43 . H43 . . H . . N 0 . . . . no no . . . . 13.793 . -3.473 . 36.889 . 0.382 -0.753 2.792 80 . 6637 CTO H53 . H53 . . H . . N 0 . . . . no no . . . . 12.370 . -1.359 . 35.145 . -1.823 -0.418 4.875 81 . 6637 CTO H631 . H631 . . H . . N 0 . . . . no no . . . . 10.278 . -1.927 . 36.208 . -2.413 -1.910 2.950 82 . 6637 CTO H632 . H632 . . H . . N 0 . . . . no no . . . . 10.932 . -3.380 . 35.627 . -0.952 -2.870 3.282 83 . 6637 CTO HO3 . HO3 . . H . . N 0 . . . . no no . . . . 10.277 . -3.582 . 37.869 . -2.830 -3.734 4.274 84 . 6637 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 . 6637 CTO 2 . SING C11 O51 no N 2 . 6637 CTO 3 . SING C11 O42 no N 3 . 6637 CTO 4 . SING C11 H11 no N 4 . 6637 CTO 5 . SING C21 N21 no N 5 . 6637 CTO 6 . SING C21 C31 no N 6 . 6637 CTO 7 . SING C21 H21 no N 7 . 6637 CTO 8 . SING N21 C71 no N 8 . 6637 CTO 9 . SING N21 HNL no N 9 . 6637 CTO 10 . DOUB C71 O71 no N 10 . 6637 CTO 11 . SING C71 C81 no N 11 . 6637 CTO 12 . SING C81 H811 no N 12 . 6637 CTO 13 . SING C81 H812 no N 13 . 6637 CTO 14 . SING C81 H813 no N 14 . 6637 CTO 15 . SING C31 O31 no N 15 . 6637 CTO 16 . SING C31 C41 no N 16 . 6637 CTO 17 . SING C31 H31 no N 17 . 6637 CTO 18 . SING O31 HOV no N 18 . 6637 CTO 19 . SING C41 O41 no N 19 . 6637 CTO 20 . SING C41 C51 no N 20 . 6637 CTO 21 . SING C41 H41 no N 21 . 6637 CTO 22 . SING O41 HO4 no N 22 . 6637 CTO 23 . SING C51 O51 no N 23 . 6637 CTO 24 . SING C51 C61 no N 24 . 6637 CTO 25 . SING C51 H51 no N 25 . 6637 CTO 26 . SING C61 O61 no N 26 . 6637 CTO 27 . SING C61 H611 no N 27 . 6637 CTO 28 . SING C61 H612 no N 28 . 6637 CTO 29 . SING O61 HO6 no N 29 . 6637 CTO 30 . SING C12 C22 no N 30 . 6637 CTO 31 . SING C12 O52 no N 31 . 6637 CTO 32 . SING C12 O43 no N 32 . 6637 CTO 33 . SING C12 H12 no N 33 . 6637 CTO 34 . SING C22 N22 no N 34 . 6637 CTO 35 . SING C22 C32 no N 35 . 6637 CTO 36 . SING C22 H22 no N 36 . 6637 CTO 37 . SING N22 C72 no N 37 . 6637 CTO 38 . SING N22 HNM no N 38 . 6637 CTO 39 . DOUB C72 O72 no N 39 . 6637 CTO 40 . SING C72 C82 no N 40 . 6637 CTO 41 . SING C82 H821 no N 41 . 6637 CTO 42 . SING C82 H822 no N 42 . 6637 CTO 43 . SING C82 H823 no N 43 . 6637 CTO 44 . SING C32 O32 no N 44 . 6637 CTO 45 . SING C32 C42 no N 45 . 6637 CTO 46 . SING C32 H32 no N 46 . 6637 CTO 47 . SING O32 HOW no N 47 . 6637 CTO 48 . SING C42 O42 no N 48 . 6637 CTO 49 . SING C42 C52 no N 49 . 6637 CTO 50 . SING C42 H42 no N 50 . 6637 CTO 51 . SING C52 O52 no N 51 . 6637 CTO 52 . SING C52 C62 no N 52 . 6637 CTO 53 . SING C52 H52 no N 53 . 6637 CTO 54 . SING C62 O62 no N 54 . 6637 CTO 55 . SING C62 H621 no N 55 . 6637 CTO 56 . SING C62 H622 no N 56 . 6637 CTO 57 . SING O62 HO2 no N 57 . 6637 CTO 58 . SING C13 O13 no N 58 . 6637 CTO 59 . SING C13 C23 no N 59 . 6637 CTO 60 . SING C13 O53 no N 60 . 6637 CTO 61 . SING C13 H13 no N 61 . 6637 CTO 62 . SING O13 HOD no N 62 . 6637 CTO 63 . SING C23 N23 no N 63 . 6637 CTO 64 . SING C23 C33 no N 64 . 6637 CTO 65 . SING C23 H23 no N 65 . 6637 CTO 66 . SING N23 C73 no N 66 . 6637 CTO 67 . SING N23 HNN no N 67 . 6637 CTO 68 . DOUB C73 O73 no N 68 . 6637 CTO 69 . SING C73 C83 no N 69 . 6637 CTO 70 . SING C83 H831 no N 70 . 6637 CTO 71 . SING C83 H832 no N 71 . 6637 CTO 72 . SING C83 H833 no N 72 . 6637 CTO 73 . SING C33 O33 no N 73 . 6637 CTO 74 . SING C33 C43 no N 74 . 6637 CTO 75 . SING C33 H33 no N 75 . 6637 CTO 76 . SING O33 HOX no N 76 . 6637 CTO 77 . SING C43 O43 no N 77 . 6637 CTO 78 . SING C43 C53 no N 78 . 6637 CTO 79 . SING C43 H43 no N 79 . 6637 CTO 80 . SING C53 O53 no N 80 . 6637 CTO 81 . SING C53 C63 no N 81 . 6637 CTO 82 . SING C53 H53 no N 82 . 6637 CTO 83 . SING C63 O63 no N 83 . 6637 CTO 84 . SING C63 H631 no N 84 . 6637 CTO 85 . SING C63 H632 no N 85 . 6637 CTO 86 . SING O63 HO3 no N 86 . 6637 CTO stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample-1 _Sample.Sf_category sample _Sample.Sf_framecode sample-1 _Sample.Entry_ID 6637 _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 $AcAMP2F18Nalb . . 2 . . mM . . . . 6637 1 2 TRIACETYLCHITOTRIOSE . . . 2 $CTO . . 16 . . mM . . . . 6637 1 3 'Phosphate buffer' . . . . . . . 20 . . mM . . . . 6637 1 4 NaCl . . . . . . . 100 . . mM . . . . 6637 1 5 H2O . . . . . . . 90 . . % . . . . 6637 1 6 D2O . . . . . . . 10 . . % . . . . 6637 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 6637 _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 6637 1 pH 5.6 0.2 pH 6637 1 temperature 298 0.2 K 6637 1 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 6637 _Software.ID 1 _Software.Type . _Software.Name xwinnmr _Software.Version 3.2 _Software.DOI . _Software.Details 'The software from Bruker performs acquisition and processing of NMR experiments.' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Data collection' 6637 1 stop_ save_ save_XEASY _Software.Sf_category software _Software.Sf_framecode XEASY _Software.Entry_ID 6637 _Software.ID 2 _Software.Type . _Software.Name XEASY _Software.Version 1.3.13 _Software.DOI . _Software.Details ; This program helps visualization and assignment of 2D NMR spectra. 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. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 6637 2 stop_ save_ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 6637 _Software.ID 3 _Software.Type . _Software.Name DYANA _Software.Version 1.5 _Software.DOI . _Software.Details ; This program yields a collection of protein structures that fit the 1H-1H distance constraints experimentally obtained. 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. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Structure solution' 6637 3 stop_ save_ save_AMBER _Software.Sf_category software _Software.Sf_framecode AMBER _Software.Entry_ID 6637 _Software.ID 4 _Software.Type . _Software.Name AMBER _Software.Version 5.0 _Software.DOI . _Software.Details ; 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. 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. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Structure refinement' 6637 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 6637 _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 6637 _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 . . . 6637 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 6637 _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 . . . . . . . . . . . . . . . . 6637 1 2 NOESY . . . . . . . . . . . 1 $sample-1 . . . 1 $conditions-1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 6637 1 stop_ 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 6637 _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.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . 6637 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_chemical_shifts_AcAMP2F18Nalb _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shifts_AcAMP2F18Nalb _Assigned_chem_shift_list.Entry_ID 6637 _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 HG2 of GLN17 is upfield shifted (at 0.459); residue 17 is shielded due the proximity to the naphtyl aromatic system of the residue 18. ; _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 TOCSY 1 $sample-1 . 6637 1 2 NOESY 1 $sample-1 . 6637 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.Ambiguity_set_ID _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 3.895 0.002 . 1 . . . . . . . . . 6637 1 2 . 1 1 1 1 VAL HB H 1 2.193 0.005 . 1 . . . . . . . . . 6637 1 3 . 1 1 1 1 VAL HG11 H 1 1.079 0.003 . 2 . . . . . . . . . 6637 1 4 . 1 1 1 1 VAL HG12 H 1 1.079 0.003 . 2 . . . . . . . . . 6637 1 5 . 1 1 1 1 VAL HG13 H 1 1.079 0.003 . 2 . . . . . . . . . 6637 1 6 . 1 1 1 1 VAL HG21 H 1 1.131 0.003 . 2 . . . . . . . . . 6637 1 7 . 1 1 1 1 VAL HG22 H 1 1.131 0.003 . 2 . . . . . . . . . 6637 1 8 . 1 1 1 1 VAL HG23 H 1 1.131 0.003 . 2 . . . . . . . . . 6637 1 9 . 1 1 2 2 GLY H H 1 8.992 0.002 . 1 . . . . . . . . . 6637 1 10 . 1 1 2 2 GLY HA2 H 1 3.774 0.007 . 2 . . . . . . . . . 6637 1 11 . 1 1 2 2 GLY HA3 H 1 4.311 0.007 . 2 . . . . . . . . . 6637 1 12 . 1 1 3 3 GLU H H 1 9.139 0.002 . 1 . . . . . . . . . 6637 1 13 . 1 1 3 3 GLU HA H 1 4.236 0.004 . 1 . . . . . . . . . 6637 1 14 . 1 1 3 3 GLU HB2 H 1 1.919 0.007 . 2 . . . . . . . . . 6637 1 15 . 1 1 3 3 GLU HG2 H 1 2.451 0.003 . 2 . . . . . . . . . 6637 1 16 . 1 1 4 4 CYS H H 1 7.741 0.003 . 1 . . . . . . . . . 6637 1 17 . 1 1 4 4 CYS HA H 1 4.428 0.002 . 1 . . . . . . . . . 6637 1 18 . 1 1 4 4 CYS HB2 H 1 2.807 0.002 . 2 . . . . . . . . . 6637 1 19 . 1 1 4 4 CYS HB3 H 1 3.141 0.003 . 2 . . . . . . . . . 6637 1 20 . 1 1 5 5 VAL H H 1 8.523 0.003 . 1 . . . . . . . . . 6637 1 21 . 1 1 5 5 VAL HA H 1 4.146 0.006 . 1 . . . . . . . . . 6637 1 22 . 1 1 5 5 VAL HB H 1 1.916 0.006 . 1 . . . . . . . . . 6637 1 23 . 1 1 5 5 VAL HG11 H 1 0.886 0.003 . 2 . . . . . . . . . 6637 1 24 . 1 1 5 5 VAL HG12 H 1 0.886 0.003 . 2 . . . . . . . . . 6637 1 25 . 1 1 5 5 VAL HG13 H 1 0.886 0.003 . 2 . . . . . . . . . 6637 1 26 . 1 1 5 5 VAL HG21 H 1 0.915 0.005 . 2 . . . . . . . . . 6637 1 27 . 1 1 5 5 VAL HG22 H 1 0.915 0.005 . 2 . . . . . . . . . 6637 1 28 . 1 1 5 5 VAL HG23 H 1 0.915 0.005 . 2 . . . . . . . . . 6637 1 29 . 1 1 6 6 ARG H H 1 9.502 0.002 . 1 . . . . . . . . . 6637 1 30 . 1 1 6 6 ARG HA H 1 3.873 0.005 . 1 . . . . . . . . . 6637 1 31 . 1 1 6 6 ARG HB2 H 1 1.854 0.003 . 2 . . . . . . . . . 6637 1 32 . 1 1 6 6 ARG HB3 H 1 1.956 0.003 . 2 . . . . . . . . . 6637 1 33 . 1 1 6 6 ARG HG2 H 1 1.604 0.006 . 2 . . . . . . . . . 6637 1 34 . 1 1 6 6 ARG HD2 H 1 3.251 0.005 . 2 . . . . . . . . . 6637 1 35 . 1 1 6 6 ARG HE H 1 7.211 0.003 . 1 . . . . . . . . . 6637 1 36 . 1 1 7 7 GLY H H 1 8.336 0.002 . 1 . . . . . . . . . 6637 1 37 . 1 1 7 7 GLY HA2 H 1 3.735 0.006 . 2 . . . . . . . . . 6637 1 38 . 1 1 7 7 GLY HA3 H 1 4.127 0.007 . 2 . . . . . . . . . 6637 1 39 . 1 1 8 8 ARG H H 1 7.891 0.002 . 1 . . . . . . . . . 6637 1 40 . 1 1 8 8 ARG HA H 1 4.696 0.005 . 1 . . . . . . . . . 6637 1 41 . 1 1 8 8 ARG HB2 H 1 1.883 0.006 . 2 . . . . . . . . . 6637 1 42 . 1 1 8 8 ARG HB3 H 1 1.919 0.004 . 2 . . . . . . . . . 6637 1 43 . 1 1 8 8 ARG HG2 H 1 1.587 0.004 . 2 . . . . . . . . . 6637 1 44 . 1 1 8 8 ARG HG3 H 1 1.688 0.004 . 2 . . . . . . . . . 6637 1 45 . 1 1 8 8 ARG HD2 H 1 3.205 0.003 . 2 . . . . . . . . . 6637 1 46 . 1 1 8 8 ARG HE H 1 7.192 0.001 . 1 . . . . . . . . . 6637 1 47 . 1 1 9 9 CYS H H 1 8.691 0.002 . 1 . . . . . . . . . 6637 1 48 . 1 1 9 9 CYS HA H 1 5.286 0.002 . 1 . . . . . . . . . 6637 1 49 . 1 1 9 9 CYS HB2 H 1 2.245 0.002 . 2 . . . . . . . . . 6637 1 50 . 1 1 9 9 CYS HB3 H 1 2.880 0.010 . 2 . . . . . . . . . 6637 1 51 . 1 1 10 10 PRO HA H 1 4.470 0.004 . 1 . . . . . . . . . 6637 1 52 . 1 1 10 10 PRO HB2 H 1 1.733 0.003 . 2 . . . . . . . . . 6637 1 53 . 1 1 10 10 PRO HB3 H 1 2.412 0.005 . 2 . . . . . . . . . 6637 1 54 . 1 1 10 10 PRO HG2 H 1 1.979 0.004 . 2 . . . . . . . . . 6637 1 55 . 1 1 10 10 PRO HG3 H 1 2.028 0.006 . 2 . . . . . . . . . 6637 1 56 . 1 1 10 10 PRO HD2 H 1 3.483 0.005 . 2 . . . . . . . . . 6637 1 57 . 1 1 10 10 PRO HD3 H 1 3.989 0.003 . 2 . . . . . . . . . 6637 1 58 . 1 1 11 11 SER H H 1 8.408 0.003 . 1 . . . . . . . . . 6637 1 59 . 1 1 11 11 SER HA H 1 4.166 0.002 . 1 . . . . . . . . . 6637 1 60 . 1 1 11 11 SER HB2 H 1 3.853 0.003 . 2 . . . . . . . . . 6637 1 61 . 1 1 12 12 GLY H H 1 8.950 0.001 . 1 . . . . . . . . . 6637 1 62 . 1 1 12 12 GLY HA2 H 1 3.689 0.003 . 2 . . . . . . . . . 6637 1 63 . 1 1 12 12 GLY HA3 H 1 4.240 0.007 . 2 . . . . . . . . . 6637 1 64 . 1 1 13 13 MET H H 1 7.944 0.003 . 1 . . . . . . . . . 6637 1 65 . 1 1 13 13 MET HA H 1 4.645 0.001 . 1 . . . . . . . . . 6637 1 66 . 1 1 13 13 MET HB2 H 1 1.758 0.004 . 2 . . . . . . . . . 6637 1 67 . 1 1 13 13 MET HB3 H 1 2.062 0.002 . 2 . . . . . . . . . 6637 1 68 . 1 1 13 13 MET HG2 H 1 2.343 0.005 . 2 . . . . . . . . . 6637 1 69 . 1 1 13 13 MET HE1 H 1 2.105 0.001 . 1 . . . . . . . . . 6637 1 70 . 1 1 13 13 MET HE2 H 1 2.105 0.001 . 1 . . . . . . . . . 6637 1 71 . 1 1 13 13 MET HE3 H 1 2.105 0.001 . 1 . . . . . . . . . 6637 1 72 . 1 1 14 14 CYS H H 1 9.341 0.002 . 1 . . . . . . . . . 6637 1 73 . 1 1 14 14 CYS HA H 1 4.581 0.003 . 1 . . . . . . . . . 6637 1 74 . 1 1 14 14 CYS HB2 H 1 2.394 0.003 . 2 . . . . . . . . . 6637 1 75 . 1 1 14 14 CYS HB3 H 1 3.907 0.003 . 2 . . . . . . . . . 6637 1 76 . 1 1 15 15 CYS H H 1 8.832 0.002 . 1 . . . . . . . . . 6637 1 77 . 1 1 15 15 CYS HA H 1 4.844 0.003 . 1 . . . . . . . . . 6637 1 78 . 1 1 15 15 CYS HB2 H 1 2.893 0.002 . 2 . . . . . . . . . 6637 1 79 . 1 1 15 15 CYS HB3 H 1 2.948 0.003 . 2 . . . . . . . . . 6637 1 80 . 1 1 16 16 SER H H 1 9.964 0.002 . 1 . . . . . . . . . 6637 1 81 . 1 1 16 16 SER HA H 1 5.126 0.003 . 1 . . . . . . . . . 6637 1 82 . 1 1 16 16 SER HB2 H 1 4.597 0.001 . 2 . . . . . . . . . 6637 1 83 . 1 1 17 17 GLN H H 1 9.182 0.002 . 1 . . . . . . . . . 6637 1 84 . 1 1 17 17 GLN HA H 1 4.098 0.003 . 1 . . . . . . . . . 6637 1 85 . 1 1 17 17 GLN HB2 H 1 1.465 0.003 . 2 . . . . . . . . . 6637 1 86 . 1 1 17 17 GLN HB3 H 1 1.689 0.005 . 2 . . . . . . . . . 6637 1 87 . 1 1 17 17 GLN HG2 H 1 0.459 0.003 . 2 . . . . . . . . . 6637 1 88 . 1 1 17 17 GLN HG3 H 1 1.247 0.064 . 2 . . . . . . . . . 6637 1 89 . 1 1 17 17 GLN HE21 H 1 6.320 0.003 . 2 . . . . . . . . . 6637 1 90 . 1 1 17 17 GLN HE22 H 1 6.439 0.003 . 2 . . . . . . . . . 6637 1 91 . 1 1 18 18 NAL H H 1 7.884 0.003 . 1 . . . . . . . . . 6637 1 92 . 1 1 18 18 NAL HA H 1 4.870 0.004 . 1 . . . . . . . . . 6637 1 93 . 1 1 18 18 NAL HB2 H 1 3.084 0.003 . 2 . . . . . . . . . 6637 1 94 . 1 1 18 18 NAL HB3 H 1 3.788 0.003 . 2 . . . . . . . . . 6637 1 95 . 1 1 18 18 NAL HD1 H 1 7.573 0.003 . 1 . . . . . . . . . 6637 1 96 . 1 1 18 18 NAL HD2 H 1 7.432 0.002 . 1 . . . . . . . . . 6637 1 97 . 1 1 18 18 NAL HE2 H 1 7.974 0.003 . 1 . . . . . . . . . 6637 1 98 . 1 1 18 18 NAL HH2 H 1 7.878 0.004 . 1 . . . . . . . . . 6637 1 99 . 1 1 18 18 NAL HP H 1 7.518 0.001 . 1 . . . . . . . . . 6637 1 100 . 1 1 18 18 NAL HH1 H 1 7.546 0.001 . 1 . . . . . . . . . 6637 1 101 . 1 1 18 18 NAL HZ1 H 1 7.847 0.002 . 1 . . . . . . . . . 6637 1 102 . 1 1 19 19 GLY H H 1 8.036 0.002 . 1 . . . . . . . . . 6637 1 103 . 1 1 19 19 GLY HA2 H 1 3.604 0.004 . 2 . . . . . . . . . 6637 1 104 . 1 1 19 19 GLY HA3 H 1 4.064 0.001 . 2 . . . . . . . . . 6637 1 105 . 1 1 20 20 TYR H H 1 7.558 0.003 . 1 . . . . . . . . . 6637 1 106 . 1 1 20 20 TYR HA H 1 5.046 0.003 . 1 . . . . . . . . . 6637 1 107 . 1 1 20 20 TYR HB2 H 1 3.076 0.002 . 2 . . . . . . . . . 6637 1 108 . 1 1 20 20 TYR HB3 H 1 3.441 0.004 . 2 . . . . . . . . . 6637 1 109 . 1 1 20 20 TYR HD1 H 1 7.064 0.003 . 3 . . . . . . . . . 6637 1 110 . 1 1 20 20 TYR HE1 H 1 6.908 0.002 . 3 . . . . . . . . . 6637 1 111 . 1 1 21 21 CYS H H 1 8.928 0.004 . 1 . . . . . . . . . 6637 1 112 . 1 1 21 21 CYS HA H 1 5.658 0.002 . 1 . . . . . . . . . 6637 1 113 . 1 1 21 21 CYS HB2 H 1 2.856 0.001 . 2 . . . . . . . . . 6637 1 114 . 1 1 22 22 GLY H H 1 8.554 0.003 . 1 . . . . . . . . . 6637 1 115 . 1 1 22 22 GLY HA2 H 1 1.829 0.002 . 2 . . . . . . . . . 6637 1 116 . 1 1 22 22 GLY HA3 H 1 3.648 0.001 . 2 . . . . . . . . . 6637 1 117 . 1 1 23 23 LYS H H 1 8.140 0.002 . 1 . . . . . . . . . 6637 1 118 . 1 1 23 23 LYS HA H 1 4.980 0.001 . 1 . . . . . . . . . 6637 1 119 . 1 1 23 23 LYS HB2 H 1 1.685 0.006 . 2 . . . . . . . . . 6637 1 120 . 1 1 23 23 LYS HB3 H 1 1.902 0.003 . 2 . . . . . . . . . 6637 1 121 . 1 1 23 23 LYS HG2 H 1 1.353 0.003 . 2 . . . . . . . . . 6637 1 122 . 1 1 23 23 LYS HG3 H 1 1.484 0.005 . 2 . . . . . . . . . 6637 1 123 . 1 1 23 23 LYS HE2 H 1 2.914 0.001 . 2 . . . . . . . . . 6637 1 124 . 1 1 24 24 GLY H H 1 8.385 0.003 . 1 . . . . . . . . . 6637 1 125 . 1 1 24 24 GLY HA2 H 1 4.003 0.005 . 2 . . . . . . . . . 6637 1 126 . 1 1 24 24 GLY HA3 H 1 4.610 0.005 . 2 . . . . . . . . . 6637 1 127 . 1 1 25 25 PRO HA H 1 4.305 0.054 . 1 . . . . . . . . . 6637 1 128 . 1 1 25 25 PRO HB2 H 1 1.986 0.003 . 2 . . . . . . . . . 6637 1 129 . 1 1 25 25 PRO HB3 H 1 2.352 0.003 . 2 . . . . . . . . . 6637 1 130 . 1 1 25 25 PRO HG2 H 1 2.082 0.002 . 2 . . . . . . . . . 6637 1 131 . 1 1 25 25 PRO HG3 H 1 2.123 0.003 . 2 . . . . . . . . . 6637 1 132 . 1 1 25 25 PRO HD2 H 1 3.687 0.002 . 2 . . . . . . . . . 6637 1 133 . 1 1 25 25 PRO HD3 H 1 3.893 0.002 . 2 . . . . . . . . . 6637 1 134 . 1 1 26 26 LYS H H 1 8.997 0.002 . 1 . . . . . . . . . 6637 1 135 . 1 1 26 26 LYS HA H 1 4.119 0.005 . 1 . . . . . . . . . 6637 1 136 . 1 1 26 26 LYS HB2 H 1 1.548 0.006 . 2 . . . . . . . . . 6637 1 137 . 1 1 26 26 LYS HB3 H 1 1.859 0.009 . 2 . . . . . . . . . 6637 1 138 . 1 1 26 26 LYS HG2 H 1 1.425 0.003 . 1 . . . . . . . . . 6637 1 139 . 1 1 26 26 LYS HD2 H 1 1.711 0.003 . 1 . . . . . . . . . 6637 1 140 . 1 1 26 26 LYS HE2 H 1 3.008 0.002 . 1 . . . . . . . . . 6637 1 141 . 1 1 27 27 TYR H H 1 7.584 0.003 . 1 . . . . . . . . . 6637 1 142 . 1 1 27 27 TYR HA H 1 4.194 0.009 . 1 . . . . . . . . . 6637 1 143 . 1 1 27 27 TYR HB2 H 1 2.549 0.004 . 2 . . . . . . . . . 6637 1 144 . 1 1 27 27 TYR HB3 H 1 3.016 0.004 . 2 . . . . . . . . . 6637 1 145 . 1 1 27 27 TYR HD1 H 1 7.279 0.004 . 3 . . . . . . . . . 6637 1 146 . 1 1 27 27 TYR HE1 H 1 6.695 0.004 . 3 . . . . . . . . . 6637 1 147 . 1 1 28 28 CYS H H 1 8.575 0.002 . 1 . . . . . . . . . 6637 1 148 . 1 1 28 28 CYS HA H 1 4.526 0.004 . 1 . . . . . . . . . 6637 1 149 . 1 1 28 28 CYS HB2 H 1 2.773 0.003 . 2 . . . . . . . . . 6637 1 150 . 1 1 28 28 CYS HB3 H 1 3.254 0.005 . 2 . . . . . . . . . 6637 1 151 . 1 1 29 29 GLY H H 1 7.983 0.003 . 1 . . . . . . . . . 6637 1 152 . 1 1 29 29 GLY HA3 H 1 4.023 0.004 . 2 . . . . . . . . . 6637 1 153 . 1 1 30 30 ARG H H 1 8.359 0.004 . 1 . . . . . . . . . 6637 1 154 . 1 1 30 30 ARG HA H 1 4.296 0.003 . 1 . . . . . . . . . 6637 1 155 . 1 1 30 30 ARG HB2 H 1 1.757 0.064 . 2 . . . . . . . . . 6637 1 156 . 1 1 30 30 ARG HB3 H 1 1.869 0.009 . 2 . . . . . . . . . 6637 1 157 . 1 1 30 30 ARG HG2 H 1 1.610 0.003 . 2 . . . . . . . . . 6637 1 158 . 1 1 30 30 ARG HG3 H 1 1.739 0.000 . 2 . . . . . . . . . 6637 1 159 . 1 1 30 30 ARG HD2 H 1 3.196 0.008 . 2 . . . . . . . . . 6637 1 160 . 1 1 30 30 ARG HE H 1 7.207 0.018 . 1 . . . . . . . . . 6637 1 stop_ save_