data_6123 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 6123 _Entry.Title ; 1H chemical shift assignments for truncated hevein of 32 aa bound to N,N',N''-triacetylchitotriose ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2004-03-02 _Entry.Accession_date 2004-03-02 _Entry.Last_release_date 2004-10-13 _Entry.Original_release_date 2004-10-13 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _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 Nuria Aboitiz . . . 6123 2 Miquel Vila-Perello . . . 6123 3 Patrick Groves . . . 6123 4 Juan Asensio . L. . 6123 5 David Andreu . . . 6123 6 F. Canada . J. . 6123 7 Jesus Jimenez-Barbero . . . 6123 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 6123 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 179 6123 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 1 . . 2004-10-13 2004-03-02 original author . 6123 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1HEV 'BMRB Entry Tracking System' 6123 PDB 1Q9B 'BMRB Entry Tracking System' 6123 PDB 1T0W 'BMRB Entry Tracking System' 6123 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 6123 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 15368576 _Citation.Full_citation . _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 . _Citation.Journal_volume 5 _Citation.Journal_issue 9 _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 1245 _Citation.Page_last 1245 _Citation.Year 2004 _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 Nuria Aboitiz . . . 6123 1 2 Miquel Vila-Perello . . . 6123 1 3 Patrick Groves . . . 6123 1 4 Juan Asensio . L. . 6123 1 5 David Andreu . . . 6123 1 6 F. Canada . Javier . 6123 1 7 Jesus Jimenez-Barbero . . . 6123 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID carbohydrate 6123 1 hevein 6123 1 'Molecular Dynamics' 6123 1 'molecular recognition' 6123 1 NMR 6123 1 protein 6123 1 stop_ save_ save_reference-1 _Citation.Sf_category citations _Citation.Sf_framecode reference-1 _Citation.Entry_ID 6123 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 7607237 _Citation.Full_citation ; Asensio JL, Canada FJ, Bruix M, Rodriguez-Romero A, Jimenez-Barbero J. Eur J Biochem. 1995 Jun 1;230(2):621-33. ; _Citation.Title 'The interaction of hevein with N-acetylglucosamine-containing oligosaccharides. Solution structure of hevein complexed to chitobiose.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Eur. J. Biochem.' _Citation.Journal_name_full 'European journal of biochemistry / FEBS' _Citation.Journal_volume 230 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0014-2956 _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 621 _Citation.Page_last 633 _Citation.Year 1995 _Citation.Details ; The three-dimensional structure of hevein, a small protein isolated from the latex of Hevea brasiliensis (rubber tree), in water solution has been obtained by using 1H-NMR spectroscopy and dynamic simulated annealing calculations. The average root-mean-square deviation (rmsd) of the best 20 refined structures generated using DIANA prior to simulated annealing was 0.092 nm for the backbone atoms and 0.163 nm for all heavy atoms (residues 3-41). The specific interaction of hevein with N-acetylglucosamine-containing oligosaccharides has also been analyzed by 1H-NMR. The association constants, Ka, for the binding of hevein to GlcNAc, chitobiose [GlcNAc-beta(1-->4)-GlcNAc], chitotriose [GlcNAc-beta(1-->4)-GlcNAc-beta(1-->4)-GlcNAc], and GlcNAc-alpha(1-->6)-Man have been estimated from 1H-NMR titration experiments. Since the measured Ka values for chitobiose binding are almost identical with and without calcium ions, it is shown that these cations are not required for sugar binding. The association increases in the order GlcNAc-alpha(1-->6)-Man < or = GlcNAc < chitobiose < chitotriose. The equilibrium thermodynamic parameters entropy and enthalpy of binding, delta S0 and delta H0, for the hevein-chitobiose and hevein-chitotriose associations have been obtained from van't Hoff analysis of the temperature dependence of the Ka values between 25-40 degrees C. The driving force for the binding process is provided for a negative delta H0 which is partially compensated by a negative delta S0. These negative signs seem to indicate that hydrogen bonding and van der Waals forces are the major interactions stabilizing the complex. Protein-carbohydrate nuclear Overhauser enhancements have allowed a three-dimensional model of the hevein-chitobiose complex to be built. From inspection of this model, a hydrogen bond between Ser19 and the non-reducing N-acetyl carbonyl group is suggested, as well as between Tyr30 and HO-3 of the same sugar residue. The N-acetyl methyl group of the non-reducing GlcNAc displays non-polar contacts to the aromatic Tyr30 and Trp21 residues. In addition, the higher affinities deduced for the beta-linked oligosaccharides with respect to GlcNAc and GlcNAc-alpha(1-->6)-Man can be explained by favourable stacking of the second beta-linked GlcNAc moiety and Trp21. ; 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 Asensio J. L. . 6123 2 2 F Canada F. J. . 6123 2 3 M Bruix M. . . 6123 2 4 A Rodriguez-Romero A. . . 6123 2 5 J Jimenez-Barbero J. . . 6123 2 stop_ save_ save_reference-2 _Citation.Sf_category citations _Citation.Sf_framecode reference-2 _Citation.Entry_ID 6123 _Citation.ID 3 _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. 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 Martins J. C. . 6123 3 2 D Maes D. . . 6123 3 3 R Loris R. . . 6123 3 4 H Pepermans H. A. . 6123 3 5 L Wyns L. . . 6123 3 6 R Willem R. . . 6123 3 7 P Verheyden P. . . 6123 3 stop_ save_ save_reference-3 _Citation.Sf_category citations _Citation.Sf_framecode reference-3 _Citation.Entry_ID 6123 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9592123 _Citation.Full_citation ; Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P. J Mol Biol. 1996 May 3;258(2):322-33. ; _Citation.Title 'NMR investigations of protein-carbohydrate interactions: refined three-dimensional structure of the complex between hevein and methyl beta-chitobioside.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Glycobiology _Citation.Journal_name_full Glycobiology _Citation.Journal_volume 8 _Citation.Journal_issue 6 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0959-6658 _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 569 _Citation.Page_last 577 _Citation.Year 1998 _Citation.Details ; The specific interaction of hevein with GlcNAc-containing oligosaccharides has been analyzed by1H-NMR spectroscopy. The association constants for the binding of hevein to a variety of ligands have been estimated from1H-NMR titration experiments. The association constants increase in the order GlcNAc-alpha(1-->6)-Man < GlcNAc < benzyl-beta-GlcNAc < p-nitrophenyl-beta-GlcNAc < chitobiose < p-nitrophenyl-beta-chitobioside < methyl-beta-chitobioside < chitotriose. Entropy and enthalpy of binding for different complexes have been obtained from van't Hoff analysis. The driving force for the binding process is provided by a negative DeltaH0which is partially compensated by negative DeltaS0. These negative signs indicate that hydrogen bonding and van der Waals forces are the major interactions stabilizing the complex. NOESY NMR experiments in water solution provided 475 accurate protein proton-proton distance constraints after employing the MARDIGRAS program. In addition, 15 unambiguous protein/carbohydrate NOEs were detected. All the experimental constraints were used in a refinement protocol including restrained molecular dynamics in order to determine the highly refined solution conformation of this protein-carbohydrate complex. With regard to the NMR structure of the free protein, no important changes in the protein nOe's were observed, indicating that carbohydrate-induced conformational changes are small. The average backbone rmsd of the 20 refined structures was 0.055 nm, while the heavy atom rmsd was 0.116 nm. It can be deduced that both hydrogen bonds and van der Waals contacts confer stability to the complex. A comparison of the three-dimensional structure of hevein in solution to those reported for wheat germ agglutinin (WGA) and hevein itself in the solid state has also been performed. The polypeptide conformation has also been compared to the NMR-derived structure of a smaller antifungical peptide, Ac-AMP2. ; 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 Asensio J. L. . 6123 4 2 F Canada F. J. . 6123 4 3 M Bruix M. . . 6123 4 4 C Gonzalez C. . . 6123 4 5 N Khiar N. . . 6123 4 6 A Rodriguez-Romero A. . . 6123 4 7 J Jimenez-Barbero J. . . 6123 4 stop_ save_ save_reference-4 _Citation.Sf_category citations _Citation.Sf_framecode reference-4 _Citation.Entry_ID 6123 _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. 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 Asensio J. L. . 6123 5 2 H Siebert H. C. . 6123 5 3 C 'von Der Lieth' C. W. . 6123 5 4 J Laynez J. . . 6123 5 5 M Bruix M. . . 6123 5 6 U Soedjanaamadja U. M. . 6123 5 7 J Beintema J. J. . 6123 5 8 F Canada F. J. . 6123 5 9 H Gabius H. J. . 6123 5 10 J Jimenez-Barbero J. . . 6123 5 stop_ save_ save_reference-5 _Citation.Sf_category citations _Citation.Sf_framecode reference-5 _Citation.Entry_ID 6123 _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. 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 Asensio J. L. . 6123 6 2 F Canada F. J. . 6123 6 3 H Siebert H. C. . 6123 6 4 J Laynez J. . . 6123 6 5 A Poveda A. . . 6123 6 6 P Nieto P. M. . 6123 6 7 U Soedjanaamadja U. M. . 6123 6 8 H Gabius H. J. . 6123 6 9 J Jimenez-Barbero J. . . 6123 6 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_HEV32 _Assembly.Sf_category assembly _Assembly.Sf_framecode system_HEV32 _Assembly.Entry_ID 6123 _Assembly.ID 1 _Assembly.Name 'Truncated hevein of 32 aa' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 6123 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 HEV32 1 $HEV32 . . . native . . . . . 6123 1 2 N,N',N''-triacetylchitotriose 2 $CTO . . . native . . . . . 6123 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 3 3 SG . 1 . 1 CYS 18 18 SG . . . . . . . . . . 6123 1 2 disulfide single . 1 . 1 CYS 12 12 SG . 1 . 1 CYS 24 24 SG . . . . . . . . . . 6123 1 3 disulfide single . 1 . 1 CYS 17 17 SG . 1 . 1 CYS 31 31 SG . . . . . . . . . . 6123 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 1HEV . . . . . 'Residues 33 to 43 have been deleted in the molecule studied here' 6123 1 . PDB 1Q9B . . . . . 'Residues 33 to 43 have been deleted in the molecule studied here.1Q9B has been obtained by X ray crystalografy.' 6123 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID HEV32 abbreviation 6123 1 'Truncated hevein of 32 aa' system 6123 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'chitin binding lectin' 6123 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_HEV32 _Entity.Sf_category entity _Entity.Sf_framecode HEV32 _Entity.Entry_ID 6123 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name hevein _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 ; EQCGRQAGGKLCPNNLCCSQ WGWCGSTDEYCS ; _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 CTO _Entity.Nonpolymer_comp_label $chem_comp_CTO _Entity.Number_of_monomers 32 _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 3485 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; The secondary structure of this protein presents an alfa-helix on residues 29 to 32 and an antiparallel beta-sheet on residues 17 to 25. This protein is a hevein domain, and has high homology with AcAMP2 antimicrobial peptide. Carbohydrate binding site involves residues S19, W21, W23 and Y30. ; _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 PDB 1HEV . "Hevein: The Nmr Assignment And An Assessment Of Solution- State Folding For The Agglutinin-Toxin Motif" . . . . . 100.00 43 100.00 100.00 3.01e-13 . . . . 6123 1 2 no PDB 1Q9B . "Crystal Structure Analysis Of Hev B 6.02 (Hevein) At 1.5 Angstroms Resolution" . . . . . 100.00 43 100.00 100.00 3.01e-13 . . . . 6123 1 3 no PDB 1T0W . "25 Nmr Structures Of Truncated Hevein Of 32 Aa (Hevein-32) Complex With N,N,N-Triacetylglucosamina" . . . . . 100.00 33 100.00 100.00 2.74e-13 . . . . 6123 1 4 no EMBL CAA05978 . "prohevein [Hevea brasiliensis]" . . . . . 100.00 187 100.00 100.00 2.39e-13 . . . . 6123 1 5 no GB AAA33357 . "hevein (HEV1) precursor [Hevea brasiliensis]" . . . . . 100.00 204 100.00 100.00 1.51e-13 . . . . 6123 1 6 no GB AAG16225 . "hevein [Hevea brasiliensis]" . . . . . 100.00 50 100.00 100.00 4.38e-14 . . . . 6123 1 7 no GB AAO63573 . "HEV2.1 [Hevea brasiliensis]" . . . . . 100.00 204 100.00 100.00 1.70e-13 . . . . 6123 1 8 no GB AAO63574 . "HEV2.2 [Hevea brasiliensis]" . . . . . 100.00 204 100.00 100.00 1.70e-13 . . . . 6123 1 9 no GB ABW34946 . "hevein [Hevea brasiliensis]" . . . . . 100.00 204 100.00 100.00 1.70e-13 . . . . 6123 1 10 no SP P02877 . "RecName: Full=Pro-hevein; AltName: Full=Major hevein; Contains: RecName: Full=Hevein; AltName: Allergen=Hev b 6; Contains: RecN" . . . . . 100.00 204 100.00 100.00 1.51e-13 . . . . 6123 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID HEV32 abbreviation 6123 1 hevein common 6123 1 'truncated hevein of 32 aa' variant 6123 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 . GLU . 6123 1 2 . GLN . 6123 1 3 . CYS . 6123 1 4 . GLY . 6123 1 5 . ARG . 6123 1 6 . GLN . 6123 1 7 . ALA . 6123 1 8 . GLY . 6123 1 9 . GLY . 6123 1 10 . LYS . 6123 1 11 . LEU . 6123 1 12 . CYS . 6123 1 13 . PRO . 6123 1 14 . ASN . 6123 1 15 . ASN . 6123 1 16 . LEU . 6123 1 17 . CYS . 6123 1 18 . CYS . 6123 1 19 . SER . 6123 1 20 . GLN . 6123 1 21 . TRP . 6123 1 22 . GLY . 6123 1 23 . TRP . 6123 1 24 . CYS . 6123 1 25 . GLY . 6123 1 26 . SER . 6123 1 27 . THR . 6123 1 28 . ASP . 6123 1 29 . GLU . 6123 1 30 . TYR . 6123 1 31 . CYS . 6123 1 32 . SER . 6123 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 . GLU 1 1 6123 1 . GLN 2 2 6123 1 . CYS 3 3 6123 1 . GLY 4 4 6123 1 . ARG 5 5 6123 1 . GLN 6 6 6123 1 . ALA 7 7 6123 1 . GLY 8 8 6123 1 . GLY 9 9 6123 1 . LYS 10 10 6123 1 . LEU 11 11 6123 1 . CYS 12 12 6123 1 . PRO 13 13 6123 1 . ASN 14 14 6123 1 . ASN 15 15 6123 1 . LEU 16 16 6123 1 . CYS 17 17 6123 1 . CYS 18 18 6123 1 . SER 19 19 6123 1 . GLN 20 20 6123 1 . TRP 21 21 6123 1 . GLY 22 22 6123 1 . TRP 23 23 6123 1 . CYS 24 24 6123 1 . GLY 25 25 6123 1 . SER 26 26 6123 1 . THR 27 27 6123 1 . ASP 28 28 6123 1 . GLU 29 29 6123 1 . TYR 30 30 6123 1 . CYS 31 31 6123 1 . SER 32 32 6123 1 stop_ save_ save_CTO _Entity.Sf_category entity _Entity.Sf_framecode CTO _Entity.Entry_ID 6123 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name CTO _Entity.Type D-SACCHARIDE _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 . _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 . 6123 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 6123 _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 $HEV32 . 3981 . . 'Hevea brasiliensis' 'Para rubber tree' . . Eukaryota Viridiplantae Hevea brasiliensis . . . . . . . . . . . . . . . . . . . . . 6123 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 6123 _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 $HEV32 . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . ; The sequence was prepared on a MBHA resin by standard solid phase peptide synthesis protocols ; . . 6123 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_CTO _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CTO _Chem_comp.Entry_ID 6123 _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 Fri Feb 3 15:57:33 2012 ; _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 6123 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 6123 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 6123 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 6123 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 6123 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 6123 CTO WZZVUHWLNMNWLW-VFCSDQTKSA-N InChIKey InChI 1.03 6123 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 6123 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 6123 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 . 6123 CTO C21 . C21 . . C . . R 0 . . . . no no . . . . 14.058 . -11.405 . 34.260 . 1.129 -0.639 -5.030 2 . 6123 CTO N21 . N21 . . N . . N 0 . . . . no no . . . . 14.331 . -11.261 . 35.711 . 2.361 -1.302 -4.598 3 . 6123 CTO C71 . C71 . . C . . N 0 . . . . no no . . . . 13.576 . -11.882 . 36.677 . 2.329 -2.587 -4.193 4 . 6123 CTO O71 . O71 . . O . . N 0 . . . . no no . . . . 12.553 . -12.539 . 36.429 . 1.279 -3.194 -4.186 5 . 6123 CTO C81 . C81 . . C . . N 0 . . . . no no . . . . 14.064 . -11.734 . 38.099 . 3.597 -3.269 -3.748 6 . 6123 CTO C31 . C31 . . C . . R 0 . . . . no no . . . . 14.913 . -12.541 . 33.636 . 1.461 0.426 -6.081 7 . 6123 CTO O31 . O31 . . O . . N 0 . . . . no no . . . . 14.640 . -13.793 . 34.299 . 1.948 -0.201 -7.268 8 . 6123 CTO C41 . C41 . . C . . S 0 . . . . no no . . . . 14.589 . -12.674 . 32.143 . 0.185 1.212 -6.401 9 . 6123 CTO O41 . O41 . . O . . N 0 . . . . no no . . . . 15.377 . -13.731 . 31.540 . 0.498 2.305 -7.266 10 . 6123 CTO C51 . C51 . . C . . R 0 . . . . no no . . . . 14.887 . -11.341 . 31.428 . -0.411 1.747 -5.097 11 . 6123 CTO O51 . O51 . . O . . N 0 . . . . no no . . . . 14.099 . -10.256 . 32.057 . -0.752 0.658 -4.240 12 . 6123 CTO C61 . C61 . . C . . N 0 . . . . no no . . . . 14.541 . -11.368 . 29.942 . -1.668 2.561 -5.410 13 . 6123 CTO O61 . O61 . . O . . N 0 . . . . no no . . . . 13.212 . -11.809 . 29.707 . -2.223 3.067 -4.194 14 . 6123 CTO C12 . C12 . . C . . S 0 . . . . no no . . . . 13.364 . -5.213 . 35.038 . -0.984 -0.342 1.074 15 . 6123 CTO C22 . C22 . . C . . R 0 . . . . no no . . . . 12.424 . -5.739 . 33.926 . -2.082 -0.093 0.038 16 . 6123 CTO N22 . N22 . . N . . N 0 . . . . no no . . . . 11.141 . -5.015 . 33.922 . -3.341 -0.677 0.508 17 . 6123 CTO C72 . C72 . . C . . N 0 . . . . no no . . . . 10.744 . -4.173 . 32.925 . -4.194 0.062 1.243 18 . 6123 CTO O72 . O72 . . O . . N 0 . . . . no no . . . . 11.392 . -3.984 . 31.884 . -3.920 1.211 1.515 19 . 6123 CTO C82 . C82 . . C . . N 0 . . . . no no . . . . 9.435 . -3.456 . 33.157 . -5.489 -0.538 1.726 20 . 6123 CTO C32 . C32 . . C . . R 0 . . . . no no . . . . 12.218 . -7.258 . 34.090 . -1.676 -0.749 -1.286 21 . 6123 CTO O32 . O32 . . O . . N 0 . . . . no no . . . . 11.374 . -7.736 . 33.029 . -2.617 -0.402 -2.305 22 . 6123 CTO C42 . C42 . . C . . S 0 . . . . no no . . . . 13.554 . -7.991 . 34.085 . -0.284 -0.240 -1.677 23 . 6123 CTO O42 . O42 . . O . . N 0 . . . . no no . . . . 13.290 . -9.435 . 34.258 . 0.178 -0.946 -2.830 24 . 6123 CTO C52 . C52 . . C . . R 0 . . . . no no . . . . 14.422 . -7.413 . 35.267 . 0.678 -0.475 -0.511 25 . 6123 CTO O52 . O52 . . O . . N 0 . . . . no no . . . . 14.598 . -5.976 . 35.081 . 0.236 0.249 0.634 26 . 6123 CTO C62 . C62 . . C . . N 0 . . . . no no . . . . 15.829 . -7.981 . 35.360 . 2.078 -0.000 -0.905 27 . 6123 CTO O62 . O62 . . O . . N 0 . . . . no no . . . . 16.591 . -7.529 . 34.246 . 2.999 -0.312 0.141 28 . 6123 CTO C13 . C13 . . C . . R 0 . . . . no no . . . . 13.947 . -0.192 . 37.088 . 0.369 -0.290 6.019 29 . 6123 CTO O13 . O13 . . O . . N 0 . . . . no yes . . . . 14.158 . 0.813 . 38.412 . 1.214 -0.696 7.098 30 . 6123 CTO C23 . C23 . . C . . R 0 . . . . no no . . . . 15.181 . -1.105 . 36.926 . 1.156 0.615 5.069 31 . 6123 CTO N23 . N23 . . N . . N 0 . . . . no no . . . . 16.391 . -0.296 . 36.724 . 1.647 1.785 5.802 32 . 6123 CTO C73 . C73 . . C . . N 0 . . . . no no . . . . 17.543 . -0.434 . 37.417 . 2.854 1.749 6.399 33 . 6123 CTO O73 . O73 . . O . . N 0 . . . . no no . . . . 17.639 . -1.026 . 38.495 . 3.535 0.747 6.330 34 . 6123 CTO C83 . C83 . . C . . N 0 . . . . no no . . . . 18.749 . 0.207 . 36.792 . 3.359 2.952 7.153 35 . 6123 CTO C33 . C33 . . C . . R 0 . . . . no no . . . . 14.950 . -2.038 . 35.740 . 0.235 1.071 3.932 36 . 6123 CTO O33 . O33 . . O . . N 0 . . . . no no . . . . 16.078 . -2.913 . 35.603 . 0.989 1.792 2.956 37 . 6123 CTO C43 . C43 . . C . . S 0 . . . . no no . . . . 13.674 . -2.858 . 35.967 . -0.393 -0.167 3.284 38 . 6123 CTO O43 . O43 . . O . . N 0 . . . . no no . . . . 13.439 . -3.729 . 34.841 . -1.369 0.237 2.323 39 . 6123 CTO C53 . C53 . . C . . R 0 . . . . no no . . . . 12.472 . -1.894 . 36.119 . -1.063 -1.014 4.369 40 . 6123 CTO O53 . O53 . . O . . N 0 . . . . no no . . . . 12.735 . -0.983 . 37.239 . -0.088 -1.444 5.317 41 . 6123 CTO C63 . C63 . . C . . N 0 . . . . no no . . . . 11.146 . -2.602 . 36.397 . -1.720 -2.236 3.725 42 . 6123 CTO O63 . O63 . . O . . N 0 . . . . no no . . . . 11.102 . -3.142 . 37.697 . -2.432 -2.974 4.720 43 . 6123 CTO H11 . H11 . . H . . N 0 . . . . no no . . . . 15.371 . -9.578 . 33.422 . 1.134 0.788 -3.417 44 . 6123 CTO H21 . H21 . . H . . N 0 . . . . no no . . . . 12.973 . -11.649 . 34.168 . 0.450 -1.375 -5.460 45 . 6123 CTO HNL . HNL . . H . . N 0 . . . . no no . . . . 15.096 . -10.691 . 36.072 . 3.201 -0.816 -4.603 46 . 6123 CTO H811 . H811 . . H . . N 0 . . . . no no . . . . 13.451 . -12.237 . 38.882 . 3.374 -4.297 -3.459 47 . 6123 CTO H812 . H812 . . H . . N 0 . . . . no no . . . . 15.123 . -12.073 . 38.171 . 4.316 -3.270 -4.567 48 . 6123 CTO H813 . H813 . . H . . N 0 . . . . no no . . . . 14.181 . -10.653 . 38.347 . 4.017 -2.735 -2.896 49 . 6123 CTO H31 . H31 . . H . . N 0 . . . . no no . . . . 15.991 . -12.288 . 33.763 . 2.219 1.104 -5.688 50 . 6123 CTO HOV . HOV . . H . . N 0 . . . . no no . . . . 15.163 . -14.488 . 33.917 . 2.131 0.504 -7.903 51 . 6123 CTO H41 . H41 . . H . . N 0 . . . . no no . . . . 13.508 . -12.927 . 32.036 . -0.535 0.556 -6.889 52 . 6123 CTO HO4 . HO4 . . H . . N 0 . . . . no no . . . . 15.176 . -13.813 . 30.615 . -0.329 2.775 -7.435 53 . 6123 CTO H51 . H51 . . H . . N 0 . . . . no no . . . . 15.984 . -11.168 . 31.526 . 0.318 2.384 -4.599 54 . 6123 CTO H611 . H611 . . H . . N 0 . . . . no no . . . . 14.726 . -10.376 . 29.467 . -1.408 3.393 -6.065 55 . 6123 CTO H612 . H612 . . H . . N 0 . . . . no no . . . . 15.275 . -11.979 . 29.368 . -2.400 1.923 -5.906 56 . 6123 CTO HO6 . HO6 . . H . . N 0 . . . . no no . . . . 12.996 . -11.825 . 28.781 . -3.011 3.572 -4.436 57 . 6123 CTO H12 . H12 . . H . . N 0 . . . . no no . . . . 12.992 . -5.371 . 36.077 . -0.842 -1.415 1.201 58 . 6123 CTO H22 . H22 . . H . . N 0 . . . . no no . . . . 12.902 . -5.553 . 32.936 . -2.211 0.978 -0.109 59 . 6123 CTO HNM . HNM . . H . . N 0 . . . . no no . . . . 10.464 . -5.105 . 34.680 . -3.560 -1.597 0.290 60 . 6123 CTO H821 . H821 . . H . . N 0 . . . . no no . . . . 9.110 . -2.767 . 32.342 . -6.043 0.204 2.300 61 . 6123 CTO H822 . H822 . . H . . N 0 . . . . no no . . . . 8.629 . -4.195 . 33.374 . -6.085 -0.854 0.870 62 . 6123 CTO H823 . H823 . . H . . N 0 . . . . no no . . . . 9.468 . -2.907 . 34.127 . -5.276 -1.400 2.359 63 . 6123 CTO H32 . H32 . . H . . N 0 . . . . no no . . . . 11.728 . -7.456 . 35.071 . -1.649 -1.832 -1.167 64 . 6123 CTO HOW . HOW . . H . . N 0 . . . . no no . . . . 11.247 . -8.672 . 33.130 . -3.476 -0.741 -2.018 65 . 6123 CTO H42 . H42 . . H . . N 0 . . . . no no . . . . 14.108 . -7.848 . 33.128 . -0.334 0.826 -1.898 66 . 6123 CTO H52 . H52 . . H . . N 0 . . . . no no . . . . 13.861 . -7.689 . 36.190 . 0.709 -1.540 -0.277 67 . 6123 CTO H621 . H621 . . H . . N 0 . . . . no no . . . . 16.318 . -7.741 . 36.332 . 2.387 -0.501 -1.822 68 . 6123 CTO H622 . H622 . . H . . N 0 . . . . no no . . . . 15.831 . -9.092 . 35.451 . 2.063 1.077 -1.067 69 . 6123 CTO HO2 . HO2 . . H . . N 0 . . . . no no . . . . 17.470 . -7.884 . 34.304 . 3.867 0.003 -0.146 70 . 6123 CTO H13 . H13 . . H . . N 0 . . . . no no . . . . 13.839 . 0.431 . 36.169 . -0.486 0.256 6.415 71 . 6123 CTO HOD . HOD . . H . . N 0 . . . . no no . . . . 13.398 . 1.374 . 38.511 . 0.681 -1.263 7.672 72 . 6123 CTO H23 . H23 . . H . . N 0 . . . . no no . . . . 15.326 . -1.711 . 37.850 . 2.001 0.064 4.656 73 . 6123 CTO HNN . HNN . . H . . N 0 . . . . no no . . . . 16.436 . 0.444 . 36.024 . 1.102 2.586 5.857 74 . 6123 CTO H831 . H831 . . H . . N 0 . . . . no no . . . . 19.699 . 0.093 . 37.363 . 4.345 2.737 7.564 75 . 6123 CTO H832 . H832 . . H . . N 0 . . . . no no . . . . 18.882 . -0.164 . 35.749 . 3.426 3.804 6.475 76 . 6123 CTO H833 . H833 . . H . . N 0 . . . . no no . . . . 18.549 . 1.285 . 36.592 . 2.670 3.188 7.965 77 . 6123 CTO H33 . H33 . . H . . N 0 . . . . no no . . . . 14.831 . -1.438 . 34.807 . -0.549 1.711 4.335 78 . 6123 CTO HOX . HOX . . H . . N 0 . . . . no no . . . . 15.934 . -3.493 . 34.864 . 1.365 2.561 3.406 79 . 6123 CTO H43 . H43 . . H . . N 0 . . . . no no . . . . 13.793 . -3.473 . 36.889 . 0.382 -0.753 2.792 80 . 6123 CTO H53 . H53 . . H . . N 0 . . . . no no . . . . 12.370 . -1.359 . 35.145 . -1.823 -0.418 4.875 81 . 6123 CTO H631 . H631 . . H . . N 0 . . . . no no . . . . 10.278 . -1.927 . 36.208 . -2.413 -1.910 2.950 82 . 6123 CTO H632 . H632 . . H . . N 0 . . . . no no . . . . 10.932 . -3.380 . 35.627 . -0.952 -2.870 3.282 83 . 6123 CTO HO3 . HO3 . . H . . N 0 . . . . no no . . . . 10.277 . -3.582 . 37.869 . -2.830 -3.734 4.274 84 . 6123 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 . 6123 CTO 2 . SING C11 O51 no N 2 . 6123 CTO 3 . SING C11 O42 no N 3 . 6123 CTO 4 . SING C11 H11 no N 4 . 6123 CTO 5 . SING C21 N21 no N 5 . 6123 CTO 6 . SING C21 C31 no N 6 . 6123 CTO 7 . SING C21 H21 no N 7 . 6123 CTO 8 . SING N21 C71 no N 8 . 6123 CTO 9 . SING N21 HNL no N 9 . 6123 CTO 10 . DOUB C71 O71 no N 10 . 6123 CTO 11 . SING C71 C81 no N 11 . 6123 CTO 12 . SING C81 H811 no N 12 . 6123 CTO 13 . SING C81 H812 no N 13 . 6123 CTO 14 . SING C81 H813 no N 14 . 6123 CTO 15 . SING C31 O31 no N 15 . 6123 CTO 16 . SING C31 C41 no N 16 . 6123 CTO 17 . SING C31 H31 no N 17 . 6123 CTO 18 . SING O31 HOV no N 18 . 6123 CTO 19 . SING C41 O41 no N 19 . 6123 CTO 20 . SING C41 C51 no N 20 . 6123 CTO 21 . SING C41 H41 no N 21 . 6123 CTO 22 . SING O41 HO4 no N 22 . 6123 CTO 23 . SING C51 O51 no N 23 . 6123 CTO 24 . SING C51 C61 no N 24 . 6123 CTO 25 . SING C51 H51 no N 25 . 6123 CTO 26 . SING C61 O61 no N 26 . 6123 CTO 27 . SING C61 H611 no N 27 . 6123 CTO 28 . SING C61 H612 no N 28 . 6123 CTO 29 . SING O61 HO6 no N 29 . 6123 CTO 30 . SING C12 C22 no N 30 . 6123 CTO 31 . SING C12 O52 no N 31 . 6123 CTO 32 . SING C12 O43 no N 32 . 6123 CTO 33 . SING C12 H12 no N 33 . 6123 CTO 34 . SING C22 N22 no N 34 . 6123 CTO 35 . SING C22 C32 no N 35 . 6123 CTO 36 . SING C22 H22 no N 36 . 6123 CTO 37 . SING N22 C72 no N 37 . 6123 CTO 38 . SING N22 HNM no N 38 . 6123 CTO 39 . DOUB C72 O72 no N 39 . 6123 CTO 40 . SING C72 C82 no N 40 . 6123 CTO 41 . SING C82 H821 no N 41 . 6123 CTO 42 . SING C82 H822 no N 42 . 6123 CTO 43 . SING C82 H823 no N 43 . 6123 CTO 44 . SING C32 O32 no N 44 . 6123 CTO 45 . SING C32 C42 no N 45 . 6123 CTO 46 . SING C32 H32 no N 46 . 6123 CTO 47 . SING O32 HOW no N 47 . 6123 CTO 48 . SING C42 O42 no N 48 . 6123 CTO 49 . SING C42 C52 no N 49 . 6123 CTO 50 . SING C42 H42 no N 50 . 6123 CTO 51 . SING C52 O52 no N 51 . 6123 CTO 52 . SING C52 C62 no N 52 . 6123 CTO 53 . SING C52 H52 no N 53 . 6123 CTO 54 . SING C62 O62 no N 54 . 6123 CTO 55 . SING C62 H621 no N 55 . 6123 CTO 56 . SING C62 H622 no N 56 . 6123 CTO 57 . SING O62 HO2 no N 57 . 6123 CTO 58 . SING C13 O13 no N 58 . 6123 CTO 59 . SING C13 C23 no N 59 . 6123 CTO 60 . SING C13 O53 no N 60 . 6123 CTO 61 . SING C13 H13 no N 61 . 6123 CTO 62 . SING O13 HOD no N 62 . 6123 CTO 63 . SING C23 N23 no N 63 . 6123 CTO 64 . SING C23 C33 no N 64 . 6123 CTO 65 . SING C23 H23 no N 65 . 6123 CTO 66 . SING N23 C73 no N 66 . 6123 CTO 67 . SING N23 HNN no N 67 . 6123 CTO 68 . DOUB C73 O73 no N 68 . 6123 CTO 69 . SING C73 C83 no N 69 . 6123 CTO 70 . SING C83 H831 no N 70 . 6123 CTO 71 . SING C83 H832 no N 71 . 6123 CTO 72 . SING C83 H833 no N 72 . 6123 CTO 73 . SING C33 O33 no N 73 . 6123 CTO 74 . SING C33 C43 no N 74 . 6123 CTO 75 . SING C33 H33 no N 75 . 6123 CTO 76 . SING O33 HOX no N 76 . 6123 CTO 77 . SING C43 O43 no N 77 . 6123 CTO 78 . SING C43 C53 no N 78 . 6123 CTO 79 . SING C43 H43 no N 79 . 6123 CTO 80 . SING C53 O53 no N 80 . 6123 CTO 81 . SING C53 C63 no N 81 . 6123 CTO 82 . SING C53 H53 no N 82 . 6123 CTO 83 . SING C63 O63 no N 83 . 6123 CTO 84 . SING C63 H631 no N 84 . 6123 CTO 85 . SING C63 H632 no N 85 . 6123 CTO 86 . SING O63 HO3 no N 86 . 6123 CTO stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample-1 _Sample.Sf_category sample _Sample.Sf_framecode sample-1 _Sample.Entry_ID 6123 _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 hevein . . . 1 $HEV32 . . 0.5 . . mM . . . . 6123 1 2 TRIACETYLCHITOTRIOSE . . . 2 $CTO . . 3 . . mM . . . . 6123 1 3 'Phosphate buffer' . . . . . . . 20 . . mM . . . . 6123 1 4 NaCl . . . . . . . 100 . . mM . . . . 6123 1 5 H2O . . . . . . . 90 . . % . . . . 6123 1 6 D2O . . . . . . . 10 . . % . . . . 6123 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 6123 _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' 0.24 0.02 M 6123 1 pH 5.8 0.2 pH 6123 1 temperature 298 0.2 K 6123 1 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 6123 _Software.ID 1 _Software.Name xwinnmr _Software.Version 3.2 _Software.Details 'The software performs acquisition and processing of NMR experiments' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Data collection' 6123 1 stop_ save_ save_XEASY _Software.Sf_category software _Software.Sf_framecode XEASY _Software.Entry_ID 6123 _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' 6123 2 stop_ save_ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 6123 _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' 6123 3 stop_ save_ save_AMBER _Software.Sf_category software _Software.Sf_framecode AMBER _Software.Entry_ID 6123 _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 and carbohydrate structures and interactions. . They also convert dyana-format pdb files into amber-format pdb files. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Structure refinement' 6123 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 6123 _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 6123 _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 . . . 6123 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 6123 _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 . . . . . . . . . . . . . . . . 6123 1 2 NOESY . . . . . . . . . . . 1 $sample-1 . . . 1 $conditions-1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 6123 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 6123 _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 . . . . . . . . . 6123 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_HEV32_shfit _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode HEV32_shfit _Assigned_chem_shift_list.Entry_ID 6123 _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 ; An unassigned signal at 7.018 ppm was observed that may correspond protonated LYS10 (proton in position Z) The atom HG2 of GLN 20 shows up at 0.728 ppm (not in average range) due to near by TRP 21 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 . 6123 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 GLU HA H 1 2.424 0.02 . 1 . . . . . . . . 6123 1 2 . 1 1 1 1 GLU HB2 H 1 1.587 0.005 . 1 . . . . . . . . 6123 1 3 . 1 1 1 1 GLU HB3 H 1 1.960 0.002 . 1 . . . . . . . . 6123 1 4 . 1 1 1 1 GLU HG2 H 1 1.881 0.002 . 1 . . . . . . . . 6123 1 5 . 1 1 1 1 GLU HG3 H 1 2.499 0.001 . 1 . . . . . . . . 6123 1 6 . 1 1 2 2 GLN HA H 1 4.321 0.002 . 1 . . . . . . . . 6123 1 7 . 1 1 2 2 GLN HB2 H 1 1.903 0.005 . 1 . . . . . . . . 6123 1 8 . 1 1 2 2 GLN HB3 H 1 1.982 0.005 . 1 . . . . . . . . 6123 1 9 . 1 1 2 2 GLN HG2 H 1 2.201 0.02 . 1 . . . . . . . . 6123 1 10 . 1 1 2 2 GLN HE21 H 1 6.939 0.02 . 1 . . . . . . . . 6123 1 11 . 1 1 2 2 GLN HE22 H 1 7.531 0.02 . 1 . . . . . . . . 6123 1 12 . 1 1 3 3 CYS H H 1 7.910 0.02 . 1 . . . . . . . . 6123 1 13 . 1 1 3 3 CYS HA H 1 4.815 0.001 . 1 . . . . . . . . 6123 1 14 . 1 1 3 3 CYS HB2 H 1 2.725 0.002 . 1 . . . . . . . . 6123 1 15 . 1 1 3 3 CYS HB3 H 1 3.039 0.003 . 1 . . . . . . . . 6123 1 16 . 1 1 4 4 GLY H H 1 8.495 0.002 . 1 . . . . . . . . 6123 1 17 . 1 1 4 4 GLY HA2 H 1 3.827 0.002 . 1 . . . . . . . . 6123 1 18 . 1 1 4 4 GLY HA3 H 1 4.110 0.004 . 1 . . . . . . . . 6123 1 19 . 1 1 5 5 ARG H H 1 8.883 0.02 . 1 . . . . . . . . 6123 1 20 . 1 1 5 5 ARG HA H 1 3.966 0.004 . 1 . . . . . . . . 6123 1 21 . 1 1 5 5 ARG HB2 H 1 1.749 0.005 . 1 . . . . . . . . 6123 1 22 . 1 1 5 5 ARG HB3 H 1 1.830 0.004 . 1 . . . . . . . . 6123 1 23 . 1 1 5 5 ARG HG2 H 1 1.587 0.006 . 1 . . . . . . . . 6123 1 24 . 1 1 5 5 ARG HD2 H 1 3.178 0.007 . 1 . . . . . . . . 6123 1 25 . 1 1 5 5 ARG HE H 1 7.235 0.005 . 1 . . . . . . . . 6123 1 26 . 1 1 6 6 GLN H H 1 8.977 0.001 . 1 . . . . . . . . 6123 1 27 . 1 1 6 6 GLN HA H 1 4.192 0.002 . 1 . . . . . . . . 6123 1 28 . 1 1 6 6 GLN HB2 H 1 1.936 0.005 . 1 . . . . . . . . 6123 1 29 . 1 1 6 6 GLN HB3 H 1 2.056 0.003 . 1 . . . . . . . . 6123 1 30 . 1 1 6 6 GLN HG2 H 1 2.428 0.003 . 1 . . . . . . . . 6123 1 31 . 1 1 6 6 GLN HG3 H 1 2.620 0.004 . 1 . . . . . . . . 6123 1 32 . 1 1 6 6 GLN HE21 H 1 6.626 0.004 . 1 . . . . . . . . 6123 1 33 . 1 1 6 6 GLN HE22 H 1 7.633 0.002 . 1 . . . . . . . . 6123 1 34 . 1 1 7 7 ALA H H 1 7.627 0.004 . 1 . . . . . . . . 6123 1 35 . 1 1 7 7 ALA HA H 1 4.540 0.004 . 1 . . . . . . . . 6123 1 36 . 1 1 7 7 ALA HB1 H 1 0.826 0.002 . 1 . . . . . . . . 6123 1 37 . 1 1 7 7 ALA HB2 H 1 0.826 0.002 . 1 . . . . . . . . 6123 1 38 . 1 1 7 7 ALA HB3 H 1 0.826 0.002 . 1 . . . . . . . . 6123 1 39 . 1 1 8 8 GLY H H 1 8.044 0.001 . 1 . . . . . . . . 6123 1 40 . 1 1 8 8 GLY HA2 H 1 3.849 0.003 . 1 . . . . . . . . 6123 1 41 . 1 1 8 8 GLY HA3 H 1 3.860 0.003 . 1 . . . . . . . . 6123 1 42 . 1 1 9 9 GLY H H 1 8.298 0.001 . 1 . . . . . . . . 6123 1 43 . 1 1 9 9 GLY HA2 H 1 3.372 0.002 . 1 . . . . . . . . 6123 1 44 . 1 1 9 9 GLY HA3 H 1 4.043 0.001 . 1 . . . . . . . . 6123 1 45 . 1 1 10 10 LYS H H 1 6.941 0.002 . 1 . . . . . . . . 6123 1 46 . 1 1 10 10 LYS HA H 1 4.059 0.003 . 1 . . . . . . . . 6123 1 47 . 1 1 10 10 LYS HB2 H 1 1.774 0.005 . 1 . . . . . . . . 6123 1 48 . 1 1 10 10 LYS HG2 H 1 1.564 0.003 . 1 . . . . . . . . 6123 1 49 . 1 1 10 10 LYS HG3 H 1 1.611 0.02 . 1 . . . . . . . . 6123 1 50 . 1 1 10 10 LYS HD2 H 1 1.724 0.002 . 1 . . . . . . . . 6123 1 51 . 1 1 10 10 LYS HE2 H 1 3.026 0.003 . 1 . . . . . . . . 6123 1 52 . 1 1 10 10 LYS HZ1 H 1 6.751 0.02 . 1 . . . . . . . . 6123 1 53 . 1 1 10 10 LYS HZ2 H 1 6.751 0.02 . 1 . . . . . . . . 6123 1 54 . 1 1 10 10 LYS HZ3 H 1 6.751 0.02 . 1 . . . . . . . . 6123 1 55 . 1 1 11 11 LEU H H 1 8.391 0.004 . 1 . . . . . . . . 6123 1 56 . 1 1 11 11 LEU HA H 1 4.597 0.007 . 1 . . . . . . . . 6123 1 57 . 1 1 11 11 LEU HB2 H 1 1.641 0.003 . 1 . . . . . . . . 6123 1 58 . 1 1 11 11 LEU HD11 H 1 0.911 0.002 . 1 . . . . . . . . 6123 1 59 . 1 1 11 11 LEU HD12 H 1 0.911 0.002 . 1 . . . . . . . . 6123 1 60 . 1 1 11 11 LEU HD13 H 1 0.911 0.002 . 1 . . . . . . . . 6123 1 61 . 1 1 11 11 LEU HD21 H 1 0.964 0.002 . 1 . . . . . . . . 6123 1 62 . 1 1 11 11 LEU HD22 H 1 0.964 0.002 . 1 . . . . . . . . 6123 1 63 . 1 1 11 11 LEU HD23 H 1 0.964 0.002 . 1 . . . . . . . . 6123 1 64 . 1 1 11 11 LEU HG H 1 1.789 0.006 . 1 . . . . . . . . 6123 1 65 . 1 1 12 12 CYS H H 1 9.094 0.001 . 1 . . . . . . . . 6123 1 66 . 1 1 12 12 CYS HA H 1 4.705 0.003 . 1 . . . . . . . . 6123 1 67 . 1 1 12 12 CYS HB2 H 1 2.676 0.004 . 1 . . . . . . . . 6123 1 68 . 1 1 12 12 CYS HB3 H 1 2.836 0.002 . 1 . . . . . . . . 6123 1 69 . 1 1 13 13 PRO HA H 1 4.619 0.006 . 1 . . . . . . . . 6123 1 70 . 1 1 13 13 PRO HB2 H 1 1.919 0.005 . 1 . . . . . . . . 6123 1 71 . 1 1 13 13 PRO HB3 H 1 2.290 0.001 . 1 . . . . . . . . 6123 1 72 . 1 1 13 13 PRO HG2 H 1 1.972 0.001 . 1 . . . . . . . . 6123 1 73 . 1 1 13 13 PRO HG3 H 1 2.092 0.001 . 1 . . . . . . . . 6123 1 74 . 1 1 13 13 PRO HD2 H 1 3.613 0.004 . 1 . . . . . . . . 6123 1 75 . 1 1 13 13 PRO HD3 H 1 3.837 0.004 . 1 . . . . . . . . 6123 1 76 . 1 1 14 14 ASN H H 1 8.731 0.001 . 1 . . . . . . . . 6123 1 77 . 1 1 14 14 ASN HA H 1 4.296 0.005 . 1 . . . . . . . . 6123 1 78 . 1 1 14 14 ASN HB2 H 1 2.623 0.003 . 1 . . . . . . . . 6123 1 79 . 1 1 14 14 ASN HB3 H 1 2.904 0.003 . 1 . . . . . . . . 6123 1 80 . 1 1 14 14 ASN HD21 H 1 6.893 0.02 . 1 . . . . . . . . 6123 1 81 . 1 1 14 14 ASN HD22 H 1 7.500 0.02 . 1 . . . . . . . . 6123 1 82 . 1 1 15 15 ASN H H 1 8.677 0.003 . 1 . . . . . . . . 6123 1 83 . 1 1 15 15 ASN HA H 1 4.427 0.004 . 1 . . . . . . . . 6123 1 84 . 1 1 15 15 ASN HB2 H 1 2.881 0.004 . 1 . . . . . . . . 6123 1 85 . 1 1 15 15 ASN HB3 H 1 3.003 0.005 . 1 . . . . . . . . 6123 1 86 . 1 1 15 15 ASN HD21 H 1 6.878 0.003 . 1 . . . . . . . . 6123 1 87 . 1 1 15 15 ASN HD22 H 1 7.579 0.02 . 1 . . . . . . . . 6123 1 88 . 1 1 16 16 LEU H H 1 7.675 0.002 . 1 . . . . . . . . 6123 1 89 . 1 1 16 16 LEU HA H 1 4.295 0.002 . 1 . . . . . . . . 6123 1 90 . 1 1 16 16 LEU HB2 H 1 1.330 0.002 . 1 . . . . . . . . 6123 1 91 . 1 1 16 16 LEU HB3 H 1 1.757 0.001 . 1 . . . . . . . . 6123 1 92 . 1 1 16 16 LEU HD11 H 1 0.699 0.004 . 1 . . . . . . . . 6123 1 93 . 1 1 16 16 LEU HD12 H 1 0.699 0.004 . 1 . . . . . . . . 6123 1 94 . 1 1 16 16 LEU HD13 H 1 0.699 0.004 . 1 . . . . . . . . 6123 1 95 . 1 1 16 16 LEU HD21 H 1 0.791 0.002 . 1 . . . . . . . . 6123 1 96 . 1 1 16 16 LEU HD22 H 1 0.791 0.002 . 1 . . . . . . . . 6123 1 97 . 1 1 16 16 LEU HD23 H 1 0.791 0.002 . 1 . . . . . . . . 6123 1 98 . 1 1 16 16 LEU HG H 1 1.681 0.002 . 1 . . . . . . . . 6123 1 99 . 1 1 17 17 CYS H H 1 8.650 0.003 . 1 . . . . . . . . 6123 1 100 . 1 1 17 17 CYS HA H 1 4.419 0.002 . 1 . . . . . . . . 6123 1 101 . 1 1 17 17 CYS HB2 H 1 2.856 0.002 . 1 . . . . . . . . 6123 1 102 . 1 1 17 17 CYS HB3 H 1 3.742 0.003 . 1 . . . . . . . . 6123 1 103 . 1 1 18 18 CYS H H 1 8.838 0.002 . 1 . . . . . . . . 6123 1 104 . 1 1 18 18 CYS HA H 1 5.123 0.002 . 1 . . . . . . . . 6123 1 105 . 1 1 18 18 CYS HB2 H 1 2.978 0.003 . 1 . . . . . . . . 6123 1 106 . 1 1 18 18 CYS HB3 H 1 3.202 0.003 . 1 . . . . . . . . 6123 1 107 . 1 1 19 19 SER H H 1 9.971 0.001 . 1 . . . . . . . . 6123 1 108 . 1 1 19 19 SER HA H 1 5.158 0.002 . 1 . . . . . . . . 6123 1 109 . 1 1 19 19 SER HB2 H 1 4.565 0.001 . 1 . . . . . . . . 6123 1 110 . 1 1 19 19 SER HB3 H 1 4.666 0.004 . 1 . . . . . . . . 6123 1 111 . 1 1 20 20 GLN H H 1 9.168 0.003 . 1 . . . . . . . . 6123 1 112 . 1 1 20 20 GLN HA H 1 4.106 0.008 . 1 . . . . . . . . 6123 1 113 . 1 1 20 20 GLN HB2 H 1 1.416 0.008 . 1 . . . . . . . . 6123 1 114 . 1 1 20 20 GLN HB3 H 1 1.582 0.002 . 1 . . . . . . . . 6123 1 115 . 1 1 20 20 GLN HG2 H 1 0.728 0.003 . 1 . . . . . . . . 6123 1 116 . 1 1 20 20 GLN HG3 H 1 1.335 0.003 . 1 . . . . . . . . 6123 1 117 . 1 1 20 20 GLN HE21 H 1 7.154 0.02 . 1 . . . . . . . . 6123 1 118 . 1 1 20 20 GLN HE22 H 1 7.508 0.001 . 1 . . . . . . . . 6123 1 119 . 1 1 21 21 TRP H H 1 7.768 0.003 . 1 . . . . . . . . 6123 1 120 . 1 1 21 21 TRP HA H 1 4.726 0.001 . 1 . . . . . . . . 6123 1 121 . 1 1 21 21 TRP HB2 H 1 3.202 0.003 . 1 . . . . . . . . 6123 1 122 . 1 1 21 21 TRP HB3 H 1 3.782 0.007 . 1 . . . . . . . . 6123 1 123 . 1 1 21 21 TRP HD1 H 1 7.266 0.002 . 1 . . . . . . . . 6123 1 124 . 1 1 21 21 TRP HE1 H 1 10.353 0.005 . 1 . . . . . . . . 6123 1 125 . 1 1 21 21 TRP HE3 H 1 7.651 0.006 . 1 . . . . . . . . 6123 1 126 . 1 1 21 21 TRP HZ2 H 1 7.478 0.001 . 1 . . . . . . . . 6123 1 127 . 1 1 21 21 TRP HZ3 H 1 7.240 0.003 . 1 . . . . . . . . 6123 1 128 . 1 1 21 21 TRP HH2 H 1 7.267 0.002 . 1 . . . . . . . . 6123 1 129 . 1 1 22 22 GLY H H 1 7.965 0.002 . 1 . . . . . . . . 6123 1 130 . 1 1 22 22 GLY HA2 H 1 3.726 0.002 . 1 . . . . . . . . 6123 1 131 . 1 1 22 22 GLY HA3 H 1 3.866 0.001 . 1 . . . . . . . . 6123 1 132 . 1 1 23 23 TRP H H 1 7.521 0.002 . 1 . . . . . . . . 6123 1 133 . 1 1 23 23 TRP HA H 1 5.148 0.005 . 1 . . . . . . . . 6123 1 134 . 1 1 23 23 TRP HB2 H 1 3.288 0.004 . 1 . . . . . . . . 6123 1 135 . 1 1 23 23 TRP HB3 H 1 3.752 0.003 . 1 . . . . . . . . 6123 1 136 . 1 1 23 23 TRP HD1 H 1 7.206 0.003 . 1 . . . . . . . . 6123 1 137 . 1 1 23 23 TRP HE1 H 1 10.485 0.007 . 1 . . . . . . . . 6123 1 138 . 1 1 23 23 TRP HE3 H 1 7.894 0.002 . 1 . . . . . . . . 6123 1 139 . 1 1 23 23 TRP HZ2 H 1 7.592 0.005 . 1 . . . . . . . . 6123 1 140 . 1 1 23 23 TRP HZ3 H 1 7.268 0.001 . 1 . . . . . . . . 6123 1 141 . 1 1 23 23 TRP HH2 H 1 7.356 0.003 . 1 . . . . . . . . 6123 1 142 . 1 1 24 24 CYS H H 1 8.774 0.002 . 1 . . . . . . . . 6123 1 143 . 1 1 24 24 CYS HA H 1 5.916 0.003 . 1 . . . . . . . . 6123 1 144 . 1 1 24 24 CYS HB2 H 1 2.807 0.008 . 1 . . . . . . . . 6123 1 145 . 1 1 24 24 CYS HB3 H 1 3.036 0.003 . 1 . . . . . . . . 6123 1 146 . 1 1 25 25 GLY H H 1 9.169 0.001 . 1 . . . . . . . . 6123 1 147 . 1 1 25 25 GLY HA2 H 1 2.006 0.002 . 1 . . . . . . . . 6123 1 148 . 1 1 25 25 GLY HA3 H 1 3.743 0.004 . 1 . . . . . . . . 6123 1 149 . 1 1 26 26 SER H H 1 8.978 0.002 . 1 . . . . . . . . 6123 1 150 . 1 1 26 26 SER HA H 1 5.076 0.004 . 1 . . . . . . . . 6123 1 151 . 1 1 26 26 SER HB2 H 1 3.650 0.004 . 1 . . . . . . . . 6123 1 152 . 1 1 26 26 SER HB3 H 1 4.056 0.005 . 1 . . . . . . . . 6123 1 153 . 1 1 27 27 THR H H 1 7.144 0.002 . 1 . . . . . . . . 6123 1 154 . 1 1 27 27 THR HA H 1 4.770 0.005 . 1 . . . . . . . . 6123 1 155 . 1 1 27 27 THR HB H 1 4.919 0.005 . 1 . . . . . . . . 6123 1 156 . 1 1 27 27 THR HG21 H 1 1.414 0.004 . 1 . . . . . . . . 6123 1 157 . 1 1 27 27 THR HG22 H 1 1.414 0.004 . 1 . . . . . . . . 6123 1 158 . 1 1 27 27 THR HG23 H 1 1.414 0.004 . 1 . . . . . . . . 6123 1 159 . 1 1 28 28 ASP H H 1 9.119 0.002 . 1 . . . . . . . . 6123 1 160 . 1 1 28 28 ASP HA H 1 4.380 0.002 . 1 . . . . . . . . 6123 1 161 . 1 1 28 28 ASP HB2 H 1 2.755 0.001 . 1 . . . . . . . . 6123 1 162 . 1 1 29 29 GLU H H 1 8.728 0.004 . 1 . . . . . . . . 6123 1 163 . 1 1 29 29 GLU HA H 1 4.161 0.001 . 1 . . . . . . . . 6123 1 164 . 1 1 29 29 GLU HB2 H 1 1.837 0.003 . 1 . . . . . . . . 6123 1 165 . 1 1 29 29 GLU HG2 H 1 2.213 0.006 . 1 . . . . . . . . 6123 1 166 . 1 1 29 29 GLU HG3 H 1 2.219 0.02 . 1 . . . . . . . . 6123 1 167 . 1 1 30 30 TYR H H 1 7.899 0.004 . 1 . . . . . . . . 6123 1 168 . 1 1 30 30 TYR HA H 1 4.154 0.003 . 1 . . . . . . . . 6123 1 169 . 1 1 30 30 TYR HB2 H 1 2.978 0.003 . 1 . . . . . . . . 6123 1 170 . 1 1 30 30 TYR HB3 H 1 3.049 0.008 . 1 . . . . . . . . 6123 1 171 . 1 1 30 30 TYR HD1 H 1 7.522 0.001 . 2 . . . . . . . . 6123 1 172 . 1 1 30 30 TYR HE1 H 1 6.740 0.001 . 2 . . . . . . . . 6123 1 173 . 1 1 31 31 CYS H H 1 7.962 0.001 . 1 . . . . . . . . 6123 1 174 . 1 1 31 31 CYS HA H 1 4.576 0.002 . 1 . . . . . . . . 6123 1 175 . 1 1 31 31 CYS HB2 H 1 2.895 0.001 . 1 . . . . . . . . 6123 1 176 . 1 1 31 31 CYS HB3 H 1 3.345 0.003 . 1 . . . . . . . . 6123 1 177 . 1 1 32 32 SER H H 1 8.332 0.02 . 1 . . . . . . . . 6123 1 178 . 1 1 32 32 SER HA H 1 4.506 0.001 . 1 . . . . . . . . 6123 1 179 . 1 1 32 32 SER HB2 H 1 3.933 0.004 . 1 . . . . . . . . 6123 1 stop_ save_