data_4422 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4422 _Entry.Title ; NMR Solution Structure of Apis mellifera Chymotrypsin Inhibitor (AMCI). ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1999-09-27 _Entry.Accession_date 1999-09-30 _Entry.Last_release_date 2000-12-19 _Entry.Original_release_date 2000-12-19 _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 T. Cierpicki . . . 4422 2 J. Otlewski . . . 4422 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4422 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 350 4422 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 . . 2000-12-19 1999-09-27 original author . 4422 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1CCV 'BMRB Entry Tracking System' 4422 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4422 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 20306980 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Cierpicki, T., Bania, J., and Otlewski, J., "NMR Solution Structure of Apis mellifera Chymotrypsin/Cathepsin G Inhibitor-1 (AMCI-1): Structural Similarity with Ascaris Protease Inhibitors," Protein Sci. 9, 976-984 (2000). ; _Citation.Title ; NMR Solution Structure of Apis mellifera Chymotrypsin/Cathepsin G Inhibitor-1 (AMCI-1): Structural Similarity with Ascaris Protease Inhibitors. ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full 'Protein Science' _Citation.Journal_volume 9 _Citation.Journal_issue . _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 976 _Citation.Page_last 984 _Citation.Year 2000 _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 Tomasz Cierpicki . . . 4422 1 2 Jacek Bania . . . 4422 1 3 Jacek Otlewski . . . 4422 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'Apis mellifera' 4422 1 'canonical inhibitor' 4422 1 hemolymph 4422 1 'protein inhibitor' 4422 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4422 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8520220 _Citation.Full_citation ; Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A, "NMRPipe: a multidimensional spectral processing system based on UNIX pipes," J Biomol NMR 1995 Nov;6(3):277-93 ; _Citation.Title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 6 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _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 277 _Citation.Page_last 293 _Citation.Year 1995 _Citation.Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; 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 F. Delaglio F. . . 4422 2 2 S. Grzesiek S. . . 4422 2 3 'G. W.' Vuister G. W. . 4422 2 4 G. Zhu G. . . 4422 2 5 J. Pfeifer J. . . 4422 2 6 A. Bax A. . . 4422 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4422 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 9367762 _Citation.Full_citation ; Guntert P, Mumenthaler C, Wuthrich K, "Torsion angle dynamics for NMR structure calculation with the new program DYANA," J Mol Biol 1997 Oct 17;273(1):283-98 ; _Citation.Title 'Torsion angle dynamics for NMR structure calculation with the new program DYANA.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 273 _Citation.Journal_issue 1 _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 283 _Citation.Page_last 298 _Citation.Year 1997 _Citation.Details ; The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the "bundle" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures. ; 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 P. Guntert P. . . 4422 3 2 C. Mumenthaler C. . . 4422 3 3 K. Wuthrich K. . . 4422 3 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_AMCI _Assembly.Sf_category assembly _Assembly.Sf_framecode system_AMCI _Assembly.Entry_ID 4422 _Assembly.ID 1 _Assembly.Name 'Apis mellifera chymotrypsin inhibitor' _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 4422 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 AMCI 1 $AMCI . . . native . . . . . 4422 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 36 36 SG . . . . . . . . . . 4422 1 2 disulfide single . 1 . 1 CYS 12 12 SG . 1 . 1 CYS 32 32 SG . . . . . . . . . . 4422 1 3 disulfide single . 1 . 1 CYS 16 16 SG . 1 . 1 CYS 28 28 SG . . . . . . . . . . 4422 1 4 disulfide single . 1 . 1 CYS 20 20 SG . 1 . 1 CYS 56 56 SG . . . . . . . . . . 4422 1 5 disulfide single . 1 . 1 CYS 38 38 SG . 1 . 1 CYS 50 50 SG . . . . . . . . . . 4422 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 1CCV . 'A Chain A, Nmr Solution Structure Of Apis Mellifera Chymotrypsin Inhibitor (Amci)' . . . . 4422 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID AMCI abbreviation 4422 1 'Apis mellifera chymotrypsin inhibitor' system 4422 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'Protease inhibitor' 4422 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_AMCI _Entity.Sf_category entity _Entity.Sf_framecode AMCI _Entity.Entry_ID 4422 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Apis mellifera chymotrypsin inhibitor' _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 ; EECGPNEVFNTCGSACAPTC AQPKTRICTMQCRIGCQCQE GFLRNGEGACVLPENC ; _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 56 _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 . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 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 1CCV . "Nmr Solution Structure Of Apis Mellifera Chymotrypsin Inhibitor (Amci)" . . . . . 100.00 56 100.00 100.00 4.78e-30 . . . . 4422 1 2 no REF XP_006563422 . "PREDICTED: chymotrypsin inhibitor [Apis mellifera]" . . . . . 100.00 76 100.00 100.00 5.61e-31 . . . . 4422 1 3 no SP P56682 . "RecName: Full=Chymotrypsin inhibitor; AltName: Full=AMCI" . . . . . 100.00 56 100.00 100.00 4.78e-30 . . . . 4422 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID AMCI abbreviation 4422 1 'Apis mellifera chymotrypsin inhibitor' common 4422 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 . 4422 1 2 . GLU . 4422 1 3 . CYS . 4422 1 4 . GLY . 4422 1 5 . PRO . 4422 1 6 . ASN . 4422 1 7 . GLU . 4422 1 8 . VAL . 4422 1 9 . PHE . 4422 1 10 . ASN . 4422 1 11 . THR . 4422 1 12 . CYS . 4422 1 13 . GLY . 4422 1 14 . SER . 4422 1 15 . ALA . 4422 1 16 . CYS . 4422 1 17 . ALA . 4422 1 18 . PRO . 4422 1 19 . THR . 4422 1 20 . CYS . 4422 1 21 . ALA . 4422 1 22 . GLN . 4422 1 23 . PRO . 4422 1 24 . LYS . 4422 1 25 . THR . 4422 1 26 . ARG . 4422 1 27 . ILE . 4422 1 28 . CYS . 4422 1 29 . THR . 4422 1 30 . MET . 4422 1 31 . GLN . 4422 1 32 . CYS . 4422 1 33 . ARG . 4422 1 34 . ILE . 4422 1 35 . GLY . 4422 1 36 . CYS . 4422 1 37 . GLN . 4422 1 38 . CYS . 4422 1 39 . GLN . 4422 1 40 . GLU . 4422 1 41 . GLY . 4422 1 42 . PHE . 4422 1 43 . LEU . 4422 1 44 . ARG . 4422 1 45 . ASN . 4422 1 46 . GLY . 4422 1 47 . GLU . 4422 1 48 . GLY . 4422 1 49 . ALA . 4422 1 50 . CYS . 4422 1 51 . VAL . 4422 1 52 . LEU . 4422 1 53 . PRO . 4422 1 54 . GLU . 4422 1 55 . ASN . 4422 1 56 . CYS . 4422 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 4422 1 . GLU 2 2 4422 1 . CYS 3 3 4422 1 . GLY 4 4 4422 1 . PRO 5 5 4422 1 . ASN 6 6 4422 1 . GLU 7 7 4422 1 . VAL 8 8 4422 1 . PHE 9 9 4422 1 . ASN 10 10 4422 1 . THR 11 11 4422 1 . CYS 12 12 4422 1 . GLY 13 13 4422 1 . SER 14 14 4422 1 . ALA 15 15 4422 1 . CYS 16 16 4422 1 . ALA 17 17 4422 1 . PRO 18 18 4422 1 . THR 19 19 4422 1 . CYS 20 20 4422 1 . ALA 21 21 4422 1 . GLN 22 22 4422 1 . PRO 23 23 4422 1 . LYS 24 24 4422 1 . THR 25 25 4422 1 . ARG 26 26 4422 1 . ILE 27 27 4422 1 . CYS 28 28 4422 1 . THR 29 29 4422 1 . MET 30 30 4422 1 . GLN 31 31 4422 1 . CYS 32 32 4422 1 . ARG 33 33 4422 1 . ILE 34 34 4422 1 . GLY 35 35 4422 1 . CYS 36 36 4422 1 . GLN 37 37 4422 1 . CYS 38 38 4422 1 . GLN 39 39 4422 1 . GLU 40 40 4422 1 . GLY 41 41 4422 1 . PHE 42 42 4422 1 . LEU 43 43 4422 1 . ARG 44 44 4422 1 . ASN 45 45 4422 1 . GLY 46 46 4422 1 . GLU 47 47 4422 1 . GLY 48 48 4422 1 . ALA 49 49 4422 1 . CYS 50 50 4422 1 . VAL 51 51 4422 1 . LEU 52 52 4422 1 . PRO 53 53 4422 1 . GLU 54 54 4422 1 . ASN 55 55 4422 1 . CYS 56 56 4422 1 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 4422 _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 $AMCI . 7460 organism . 'Apis mellifera' Honeybee . . Eukaryota Metazoa Apis mellifera . . . . hemolymph . . . . . . . . . . . . . . . . 4422 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 4422 _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 $AMCI . 'purified from natural source' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4422 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 4422 _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 'Apis mellifera chymotrypsin inhibitor' . . . 1 $AMCI . . 6.6 . . mM . . . . 4422 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions _Sample_condition_list.Entry_ID 4422 _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 pH* 2.5 0.1 na 4422 1 temperature 288 1 K 4422 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 4422 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'spectra processing' 4422 1 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 2 $ref_1 4422 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 4422 _Software.ID 2 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'analysis and intergation of NMR spectra' 4422 2 stop_ save_ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 4422 _Software.ID 3 _Software.Name DYANA _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure calculation' 4422 3 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $ref_2 4422 3 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 4422 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model UnityPlus _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4422 _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 Varian UnityPlus . 500 . . . 4422 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 4422 _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 NOESY . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4422 1 2 TOCSY . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4422 1 3 DQFCOSY . . . . . . . . . . . 1 $sample_one . . . 1 $sample_conditions . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4422 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 4422 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name NOESY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4422 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4422 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name DQFCOSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4422 _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 0.00 external direct . External_in_the_sample cylindrical parallel_to_Bo . . . . . . 4422 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_assigned_chemical_shifts _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chemical_shifts _Assigned_chem_shift_list.Entry_ID 4422 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions _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 . _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_one . 4422 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 3.79 0.01 . 1 . . . . . . . . 4422 1 2 . 1 1 1 1 GLU HB2 H 1 1.69 0.01 . 2 . . . . . . . . 4422 1 3 . 1 1 1 1 GLU HB3 H 1 1.72 0.01 . 2 . . . . . . . . 4422 1 4 . 1 1 1 1 GLU HG2 H 1 2.13 0.01 . 1 . . . . . . . . 4422 1 5 . 1 1 1 1 GLU HG3 H 1 2.13 0.01 . 1 . . . . . . . . 4422 1 6 . 1 1 2 2 GLU H H 1 8.69 0.01 . 1 . . . . . . . . 4422 1 7 . 1 1 2 2 GLU HA H 1 4.28 0.01 . 1 . . . . . . . . 4422 1 8 . 1 1 2 2 GLU HB2 H 1 1.84 0.01 . 2 . . . . . . . . 4422 1 9 . 1 1 2 2 GLU HB3 H 1 1.94 0.01 . 2 . . . . . . . . 4422 1 10 . 1 1 2 2 GLU HG2 H 1 2.30 0.01 . 1 . . . . . . . . 4422 1 11 . 1 1 2 2 GLU HG3 H 1 2.30 0.01 . 1 . . . . . . . . 4422 1 12 . 1 1 3 3 CYS H H 1 8.53 0.01 . 1 . . . . . . . . 4422 1 13 . 1 1 3 3 CYS HA H 1 4.89 0.01 . 1 . . . . . . . . 4422 1 14 . 1 1 3 3 CYS HB2 H 1 2.53 0.01 . 2 . . . . . . . . 4422 1 15 . 1 1 3 3 CYS HB3 H 1 3.18 0.01 . 2 . . . . . . . . 4422 1 16 . 1 1 4 4 GLY H H 1 7.51 0.01 . 1 . . . . . . . . 4422 1 17 . 1 1 4 4 GLY HA2 H 1 3.66 0.01 . 2 . . . . . . . . 4422 1 18 . 1 1 4 4 GLY HA3 H 1 4.12 0.01 . 2 . . . . . . . . 4422 1 19 . 1 1 5 5 PRO HA H 1 4.05 0.01 . 1 . . . . . . . . 4422 1 20 . 1 1 5 5 PRO HB2 H 1 2.10 0.01 . 2 . . . . . . . . 4422 1 21 . 1 1 5 5 PRO HB3 H 1 1.65 0.01 . 2 . . . . . . . . 4422 1 22 . 1 1 5 5 PRO HG2 H 1 1.82 0.01 . 2 . . . . . . . . 4422 1 23 . 1 1 5 5 PRO HG3 H 1 1.95 0.01 . 2 . . . . . . . . 4422 1 24 . 1 1 5 5 PRO HD2 H 1 3.49 0.01 . 2 . . . . . . . . 4422 1 25 . 1 1 5 5 PRO HD3 H 1 3.35 0.01 . 2 . . . . . . . . 4422 1 26 . 1 1 6 6 ASN H H 1 8.91 0.01 . 1 . . . . . . . . 4422 1 27 . 1 1 6 6 ASN HA H 1 3.61 0.01 . 1 . . . . . . . . 4422 1 28 . 1 1 6 6 ASN HB2 H 1 2.39 0.01 . 2 . . . . . . . . 4422 1 29 . 1 1 6 6 ASN HB3 H 1 0.98 0.01 . 2 . . . . . . . . 4422 1 30 . 1 1 6 6 ASN HD21 H 1 6.80 0.01 . 2 . . . . . . . . 4422 1 31 . 1 1 6 6 ASN HD22 H 1 6.92 0.01 . 2 . . . . . . . . 4422 1 32 . 1 1 7 7 GLU H H 1 7.14 0.01 . 1 . . . . . . . . 4422 1 33 . 1 1 7 7 GLU HA H 1 5.14 0.01 . 1 . . . . . . . . 4422 1 34 . 1 1 7 7 GLU HB2 H 1 1.97 0.01 . 2 . . . . . . . . 4422 1 35 . 1 1 7 7 GLU HB3 H 1 1.61 0.01 . 2 . . . . . . . . 4422 1 36 . 1 1 7 7 GLU HG2 H 1 2.16 0.01 . 2 . . . . . . . . 4422 1 37 . 1 1 7 7 GLU HG3 H 1 2.22 0.01 . 2 . . . . . . . . 4422 1 38 . 1 1 8 8 VAL H H 1 9.09 0.01 . 1 . . . . . . . . 4422 1 39 . 1 1 8 8 VAL HA H 1 4.38 0.01 . 1 . . . . . . . . 4422 1 40 . 1 1 8 8 VAL HB H 1 1.90 0.01 . 1 . . . . . . . . 4422 1 41 . 1 1 8 8 VAL HG11 H 1 0.80 0.01 . 2 . . . . . . . . 4422 1 42 . 1 1 8 8 VAL HG12 H 1 0.80 0.01 . 2 . . . . . . . . 4422 1 43 . 1 1 8 8 VAL HG13 H 1 0.80 0.01 . 2 . . . . . . . . 4422 1 44 . 1 1 8 8 VAL HG21 H 1 0.72 0.01 . 2 . . . . . . . . 4422 1 45 . 1 1 8 8 VAL HG22 H 1 0.72 0.01 . 2 . . . . . . . . 4422 1 46 . 1 1 8 8 VAL HG23 H 1 0.72 0.01 . 2 . . . . . . . . 4422 1 47 . 1 1 9 9 PHE H H 1 8.88 0.01 . 1 . . . . . . . . 4422 1 48 . 1 1 9 9 PHE HA H 1 4.20 0.01 . 1 . . . . . . . . 4422 1 49 . 1 1 9 9 PHE HB2 H 1 2.94 0.01 . 2 . . . . . . . . 4422 1 50 . 1 1 9 9 PHE HB3 H 1 2.82 0.01 . 2 . . . . . . . . 4422 1 51 . 1 1 9 9 PHE HD1 H 1 6.89 0.01 . 1 . . . . . . . . 4422 1 52 . 1 1 9 9 PHE HD2 H 1 6.89 0.01 . 1 . . . . . . . . 4422 1 53 . 1 1 9 9 PHE HE1 H 1 7.11 0.01 . 1 . . . . . . . . 4422 1 54 . 1 1 9 9 PHE HE2 H 1 7.11 0.01 . 1 . . . . . . . . 4422 1 55 . 1 1 9 9 PHE HZ H 1 7.05 0.01 . 1 . . . . . . . . 4422 1 56 . 1 1 10 10 ASN H H 1 7.56 0.01 . 1 . . . . . . . . 4422 1 57 . 1 1 10 10 ASN HA H 1 4.76 0.01 . 1 . . . . . . . . 4422 1 58 . 1 1 10 10 ASN HB2 H 1 2.61 0.01 . 2 . . . . . . . . 4422 1 59 . 1 1 10 10 ASN HB3 H 1 2.21 0.01 . 2 . . . . . . . . 4422 1 60 . 1 1 10 10 ASN HD21 H 1 6.70 0.01 . 2 . . . . . . . . 4422 1 61 . 1 1 10 10 ASN HD22 H 1 7.54 0.01 . 2 . . . . . . . . 4422 1 62 . 1 1 11 11 THR H H 1 8.28 0.01 . 1 . . . . . . . . 4422 1 63 . 1 1 11 11 THR HA H 1 3.86 0.01 . 1 . . . . . . . . 4422 1 64 . 1 1 11 11 THR HB H 1 4.20 0.01 . 1 . . . . . . . . 4422 1 65 . 1 1 11 11 THR HG21 H 1 1.22 0.01 . 1 . . . . . . . . 4422 1 66 . 1 1 11 11 THR HG22 H 1 1.22 0.01 . 1 . . . . . . . . 4422 1 67 . 1 1 11 11 THR HG23 H 1 1.22 0.01 . 1 . . . . . . . . 4422 1 68 . 1 1 12 12 CYS H H 1 8.58 0.01 . 1 . . . . . . . . 4422 1 69 . 1 1 12 12 CYS HA H 1 4.23 0.01 . 1 . . . . . . . . 4422 1 70 . 1 1 12 12 CYS HB2 H 1 2.59 0.01 . 2 . . . . . . . . 4422 1 71 . 1 1 12 12 CYS HB3 H 1 3.13 0.01 . 2 . . . . . . . . 4422 1 72 . 1 1 13 13 GLY H H 1 8.44 0.01 . 1 . . . . . . . . 4422 1 73 . 1 1 13 13 GLY HA2 H 1 3.62 0.01 . 2 . . . . . . . . 4422 1 74 . 1 1 13 13 GLY HA3 H 1 4.12 0.01 . 2 . . . . . . . . 4422 1 75 . 1 1 14 14 SER H H 1 8.29 0.01 . 1 . . . . . . . . 4422 1 76 . 1 1 14 14 SER HA H 1 4.33 0.01 . 1 . . . . . . . . 4422 1 77 . 1 1 14 14 SER HB2 H 1 3.88 0.01 . 2 . . . . . . . . 4422 1 78 . 1 1 14 14 SER HB3 H 1 3.45 0.01 . 2 . . . . . . . . 4422 1 79 . 1 1 15 15 ALA H H 1 9.23 0.01 . 1 . . . . . . . . 4422 1 80 . 1 1 15 15 ALA HA H 1 4.12 0.01 . 1 . . . . . . . . 4422 1 81 . 1 1 15 15 ALA HB1 H 1 1.35 0.01 . 1 . . . . . . . . 4422 1 82 . 1 1 15 15 ALA HB2 H 1 1.35 0.01 . 1 . . . . . . . . 4422 1 83 . 1 1 15 15 ALA HB3 H 1 1.35 0.01 . 1 . . . . . . . . 4422 1 84 . 1 1 16 16 CYS H H 1 8.55 0.01 . 1 . . . . . . . . 4422 1 85 . 1 1 16 16 CYS HA H 1 4.74 0.01 . 1 . . . . . . . . 4422 1 86 . 1 1 16 16 CYS HB2 H 1 2.91 0.01 . 1 . . . . . . . . 4422 1 87 . 1 1 16 16 CYS HB3 H 1 2.91 0.01 . 1 . . . . . . . . 4422 1 88 . 1 1 17 17 ALA H H 1 7.43 0.01 . 1 . . . . . . . . 4422 1 89 . 1 1 17 17 ALA HA H 1 4.32 0.01 . 1 . . . . . . . . 4422 1 90 . 1 1 17 17 ALA HB1 H 1 1.31 0.01 . 1 . . . . . . . . 4422 1 91 . 1 1 17 17 ALA HB2 H 1 1.31 0.01 . 1 . . . . . . . . 4422 1 92 . 1 1 17 17 ALA HB3 H 1 1.31 0.01 . 1 . . . . . . . . 4422 1 93 . 1 1 18 18 PRO HA H 1 4.51 0.01 . 1 . . . . . . . . 4422 1 94 . 1 1 18 18 PRO HB2 H 1 1.75 0.01 . 2 . . . . . . . . 4422 1 95 . 1 1 18 18 PRO HB3 H 1 2.16 0.01 . 2 . . . . . . . . 4422 1 96 . 1 1 18 18 PRO HG2 H 1 1.85 0.01 . 2 . . . . . . . . 4422 1 97 . 1 1 18 18 PRO HG3 H 1 1.93 0.01 . 2 . . . . . . . . 4422 1 98 . 1 1 18 18 PRO HD2 H 1 3.58 0.01 . 2 . . . . . . . . 4422 1 99 . 1 1 18 18 PRO HD3 H 1 3.79 0.01 . 2 . . . . . . . . 4422 1 100 . 1 1 19 19 THR H H 1 7.87 0.01 . 1 . . . . . . . . 4422 1 101 . 1 1 19 19 THR HA H 1 4.76 0.01 . 1 . . . . . . . . 4422 1 102 . 1 1 19 19 THR HB H 1 4.57 0.01 . 1 . . . . . . . . 4422 1 103 . 1 1 19 19 THR HG21 H 1 1.14 0.01 . 1 . . . . . . . . 4422 1 104 . 1 1 19 19 THR HG22 H 1 1.14 0.01 . 1 . . . . . . . . 4422 1 105 . 1 1 19 19 THR HG23 H 1 1.14 0.01 . 1 . . . . . . . . 4422 1 106 . 1 1 20 20 CYS H H 1 8.52 0.01 . 1 . . . . . . . . 4422 1 107 . 1 1 20 20 CYS HA H 1 4.08 0.01 . 1 . . . . . . . . 4422 1 108 . 1 1 20 20 CYS HB2 H 1 2.91 0.01 . 2 . . . . . . . . 4422 1 109 . 1 1 20 20 CYS HB3 H 1 2.82 0.01 . 2 . . . . . . . . 4422 1 110 . 1 1 21 21 ALA H H 1 7.93 0.01 . 1 . . . . . . . . 4422 1 111 . 1 1 21 21 ALA HA H 1 4.05 0.01 . 1 . . . . . . . . 4422 1 112 . 1 1 21 21 ALA HB1 H 1 1.25 0.01 . 1 . . . . . . . . 4422 1 113 . 1 1 21 21 ALA HB2 H 1 1.25 0.01 . 1 . . . . . . . . 4422 1 114 . 1 1 21 21 ALA HB3 H 1 1.25 0.01 . 1 . . . . . . . . 4422 1 115 . 1 1 22 22 GLN H H 1 7.58 0.01 . 1 . . . . . . . . 4422 1 116 . 1 1 22 22 GLN HA H 1 4.60 0.01 . 1 . . . . . . . . 4422 1 117 . 1 1 22 22 GLN HB2 H 1 1.78 0.01 . 2 . . . . . . . . 4422 1 118 . 1 1 22 22 GLN HB3 H 1 1.92 0.01 . 2 . . . . . . . . 4422 1 119 . 1 1 22 22 GLN HG2 H 1 2.04 0.01 . 2 . . . . . . . . 4422 1 120 . 1 1 22 22 GLN HG3 H 1 2.08 0.01 . 2 . . . . . . . . 4422 1 121 . 1 1 22 22 GLN HE21 H 1 6.73 0.01 . 2 . . . . . . . . 4422 1 122 . 1 1 22 22 GLN HE22 H 1 7.42 0.01 . 2 . . . . . . . . 4422 1 123 . 1 1 23 23 PRO HA H 1 4.56 0.01 . 1 . . . . . . . . 4422 1 124 . 1 1 23 23 PRO HB2 H 1 2.10 0.01 . 2 . . . . . . . . 4422 1 125 . 1 1 23 23 PRO HB3 H 1 1.84 0.01 . 2 . . . . . . . . 4422 1 126 . 1 1 23 23 PRO HG2 H 1 1.73 0.01 . 2 . . . . . . . . 4422 1 127 . 1 1 23 23 PRO HG3 H 1 1.92 0.01 . 2 . . . . . . . . 4422 1 128 . 1 1 23 23 PRO HD2 H 1 3.52 0.01 . 2 . . . . . . . . 4422 1 129 . 1 1 23 23 PRO HD3 H 1 3.25 0.01 . 2 . . . . . . . . 4422 1 130 . 1 1 24 24 LYS H H 1 7.82 0.01 . 1 . . . . . . . . 4422 1 131 . 1 1 24 24 LYS HA H 1 4.31 0.01 . 1 . . . . . . . . 4422 1 132 . 1 1 24 24 LYS HB2 H 1 1.62 0.01 . 2 . . . . . . . . 4422 1 133 . 1 1 24 24 LYS HB3 H 1 1.65 0.01 . 2 . . . . . . . . 4422 1 134 . 1 1 24 24 LYS HG2 H 1 1.26 0.01 . 2 . . . . . . . . 4422 1 135 . 1 1 24 24 LYS HG3 H 1 1.30 0.01 . 2 . . . . . . . . 4422 1 136 . 1 1 24 24 LYS HD2 H 1 1.54 0.01 . 1 . . . . . . . . 4422 1 137 . 1 1 24 24 LYS HD3 H 1 1.54 0.01 . 1 . . . . . . . . 4422 1 138 . 1 1 24 24 LYS HE2 H 1 2.86 0.01 . 1 . . . . . . . . 4422 1 139 . 1 1 24 24 LYS HE3 H 1 2.86 0.01 . 1 . . . . . . . . 4422 1 140 . 1 1 24 24 LYS HZ1 H 1 7.43 0.01 . 3 . . . . . . . . 4422 1 141 . 1 1 24 24 LYS HZ2 H 1 7.43 0.01 . 3 . . . . . . . . 4422 1 142 . 1 1 24 24 LYS HZ3 H 1 7.43 0.01 . 3 . . . . . . . . 4422 1 143 . 1 1 25 25 THR H H 1 8.26 0.01 . 1 . . . . . . . . 4422 1 144 . 1 1 25 25 THR HA H 1 4.03 0.01 . 1 . . . . . . . . 4422 1 145 . 1 1 25 25 THR HB H 1 3.91 0.01 . 1 . . . . . . . . 4422 1 146 . 1 1 25 25 THR HG21 H 1 1.06 0.01 . 1 . . . . . . . . 4422 1 147 . 1 1 25 25 THR HG22 H 1 1.06 0.01 . 1 . . . . . . . . 4422 1 148 . 1 1 25 25 THR HG23 H 1 1.06 0.01 . 1 . . . . . . . . 4422 1 149 . 1 1 26 26 ARG H H 1 8.58 0.01 . 1 . . . . . . . . 4422 1 150 . 1 1 26 26 ARG HA H 1 4.42 0.01 . 1 . . . . . . . . 4422 1 151 . 1 1 26 26 ARG HB2 H 1 1.65 0.01 . 1 . . . . . . . . 4422 1 152 . 1 1 26 26 ARG HB3 H 1 1.65 0.01 . 1 . . . . . . . . 4422 1 153 . 1 1 26 26 ARG HG2 H 1 1.48 0.01 . 1 . . . . . . . . 4422 1 154 . 1 1 26 26 ARG HG3 H 1 1.48 0.01 . 1 . . . . . . . . 4422 1 155 . 1 1 26 26 ARG HD2 H 1 3.02 0.01 . 1 . . . . . . . . 4422 1 156 . 1 1 26 26 ARG HD3 H 1 3.02 0.01 . 1 . . . . . . . . 4422 1 157 . 1 1 26 26 ARG HE H 1 7.29 0.01 . 1 . . . . . . . . 4422 1 158 . 1 1 27 27 ILE H H 1 8.16 0.01 . 1 . . . . . . . . 4422 1 159 . 1 1 27 27 ILE HA H 1 4.06 0.01 . 1 . . . . . . . . 4422 1 160 . 1 1 27 27 ILE HB H 1 1.64 0.01 . 1 . . . . . . . . 4422 1 161 . 1 1 27 27 ILE HG21 H 1 0.72 0.01 . 1 . . . . . . . . 4422 1 162 . 1 1 27 27 ILE HG22 H 1 0.72 0.01 . 1 . . . . . . . . 4422 1 163 . 1 1 27 27 ILE HG23 H 1 0.72 0.01 . 1 . . . . . . . . 4422 1 164 . 1 1 27 27 ILE HG12 H 1 1.05 0.01 . 2 . . . . . . . . 4422 1 165 . 1 1 27 27 ILE HG13 H 1 1.35 0.01 . 2 . . . . . . . . 4422 1 166 . 1 1 27 27 ILE HD11 H 1 0.69 0.01 . 1 . . . . . . . . 4422 1 167 . 1 1 27 27 ILE HD12 H 1 0.69 0.01 . 1 . . . . . . . . 4422 1 168 . 1 1 27 27 ILE HD13 H 1 0.69 0.01 . 1 . . . . . . . . 4422 1 169 . 1 1 28 28 CYS H H 1 8.52 0.01 . 1 . . . . . . . . 4422 1 170 . 1 1 28 28 CYS HA H 1 4.82 0.01 . 1 . . . . . . . . 4422 1 171 . 1 1 28 28 CYS HB2 H 1 3.11 0.01 . 2 . . . . . . . . 4422 1 172 . 1 1 28 28 CYS HB3 H 1 3.03 0.01 . 2 . . . . . . . . 4422 1 173 . 1 1 29 29 THR H H 1 8.22 0.01 . 1 . . . . . . . . 4422 1 174 . 1 1 29 29 THR HA H 1 4.13 0.01 . 1 . . . . . . . . 4422 1 175 . 1 1 29 29 THR HB H 1 4.12 0.01 . 1 . . . . . . . . 4422 1 176 . 1 1 29 29 THR HG21 H 1 1.06 0.01 . 1 . . . . . . . . 4422 1 177 . 1 1 29 29 THR HG22 H 1 1.06 0.01 . 1 . . . . . . . . 4422 1 178 . 1 1 29 29 THR HG23 H 1 1.06 0.01 . 1 . . . . . . . . 4422 1 179 . 1 1 30 30 MET H H 1 8.08 0.01 . 1 . . . . . . . . 4422 1 180 . 1 1 30 30 MET HA H 1 4.31 0.01 . 1 . . . . . . . . 4422 1 181 . 1 1 30 30 MET HB2 H 1 1.80 0.01 . 2 . . . . . . . . 4422 1 182 . 1 1 30 30 MET HB3 H 1 2.00 0.01 . 2 . . . . . . . . 4422 1 183 . 1 1 30 30 MET HG2 H 1 2.41 0.01 . 2 . . . . . . . . 4422 1 184 . 1 1 30 30 MET HG3 H 1 2.47 0.01 . 2 . . . . . . . . 4422 1 185 . 1 1 31 31 GLN H H 1 7.92 0.01 . 1 . . . . . . . . 4422 1 186 . 1 1 31 31 GLN HA H 1 4.10 0.01 . 1 . . . . . . . . 4422 1 187 . 1 1 31 31 GLN HB2 H 1 1.84 0.01 . 1 . . . . . . . . 4422 1 188 . 1 1 31 31 GLN HB3 H 1 1.84 0.01 . 1 . . . . . . . . 4422 1 189 . 1 1 31 31 GLN HG2 H 1 2.21 0.01 . 1 . . . . . . . . 4422 1 190 . 1 1 31 31 GLN HG3 H 1 2.21 0.01 . 1 . . . . . . . . 4422 1 191 . 1 1 31 31 GLN HE21 H 1 6.79 0.01 . 2 . . . . . . . . 4422 1 192 . 1 1 31 31 GLN HE22 H 1 7.46 0.01 . 2 . . . . . . . . 4422 1 193 . 1 1 32 32 CYS H H 1 8.56 0.01 . 1 . . . . . . . . 4422 1 194 . 1 1 32 32 CYS HA H 1 4.53 0.01 . 1 . . . . . . . . 4422 1 195 . 1 1 32 32 CYS HB2 H 1 2.79 0.01 . 2 . . . . . . . . 4422 1 196 . 1 1 32 32 CYS HB3 H 1 3.11 0.01 . 2 . . . . . . . . 4422 1 197 . 1 1 33 33 ARG H H 1 8.45 0.01 . 1 . . . . . . . . 4422 1 198 . 1 1 33 33 ARG HA H 1 4.52 0.01 . 1 . . . . . . . . 4422 1 199 . 1 1 33 33 ARG HB2 H 1 1.27 0.01 . 2 . . . . . . . . 4422 1 200 . 1 1 33 33 ARG HB3 H 1 1.35 0.01 . 2 . . . . . . . . 4422 1 201 . 1 1 33 33 ARG HG2 H 1 1.27 0.01 . 2 . . . . . . . . 4422 1 202 . 1 1 33 33 ARG HG3 H 1 1.35 0.01 . 2 . . . . . . . . 4422 1 203 . 1 1 33 33 ARG HD2 H 1 2.97 0.01 . 1 . . . . . . . . 4422 1 204 . 1 1 33 33 ARG HD3 H 1 2.97 0.01 . 1 . . . . . . . . 4422 1 205 . 1 1 33 33 ARG HE H 1 7.10 0.01 . 1 . . . . . . . . 4422 1 206 . 1 1 34 34 ILE H H 1 8.71 0.01 . 1 . . . . . . . . 4422 1 207 . 1 1 34 34 ILE HA H 1 4.18 0.01 . 1 . . . . . . . . 4422 1 208 . 1 1 34 34 ILE HB H 1 1.60 0.01 . 1 . . . . . . . . 4422 1 209 . 1 1 34 34 ILE HG21 H 1 0.84 0.01 . 1 . . . . . . . . 4422 1 210 . 1 1 34 34 ILE HG22 H 1 0.84 0.01 . 1 . . . . . . . . 4422 1 211 . 1 1 34 34 ILE HG23 H 1 0.84 0.01 . 1 . . . . . . . . 4422 1 212 . 1 1 34 34 ILE HG12 H 1 1.03 0.01 . 2 . . . . . . . . 4422 1 213 . 1 1 34 34 ILE HG13 H 1 1.44 0.01 . 2 . . . . . . . . 4422 1 214 . 1 1 34 34 ILE HD11 H 1 0.86 0.01 . 1 . . . . . . . . 4422 1 215 . 1 1 34 34 ILE HD12 H 1 0.86 0.01 . 1 . . . . . . . . 4422 1 216 . 1 1 34 34 ILE HD13 H 1 0.86 0.01 . 1 . . . . . . . . 4422 1 217 . 1 1 35 35 GLY H H 1 7.75 0.01 . 1 . . . . . . . . 4422 1 218 . 1 1 35 35 GLY HA2 H 1 3.61 0.01 . 2 . . . . . . . . 4422 1 219 . 1 1 35 35 GLY HA3 H 1 4.38 0.01 . 2 . . . . . . . . 4422 1 220 . 1 1 36 36 CYS H H 1 8.90 0.01 . 1 . . . . . . . . 4422 1 221 . 1 1 36 36 CYS HA H 1 4.76 0.01 . 1 . . . . . . . . 4422 1 222 . 1 1 36 36 CYS HB2 H 1 2.81 0.01 . 2 . . . . . . . . 4422 1 223 . 1 1 36 36 CYS HB3 H 1 2.71 0.01 . 2 . . . . . . . . 4422 1 224 . 1 1 37 37 GLN H H 1 9.03 0.01 . 1 . . . . . . . . 4422 1 225 . 1 1 37 37 GLN HA H 1 4.57 0.01 . 1 . . . . . . . . 4422 1 226 . 1 1 37 37 GLN HB2 H 1 2.02 0.01 . 2 . . . . . . . . 4422 1 227 . 1 1 37 37 GLN HB3 H 1 1.80 0.01 . 2 . . . . . . . . 4422 1 228 . 1 1 37 37 GLN HG2 H 1 2.14 0.01 . 2 . . . . . . . . 4422 1 229 . 1 1 37 37 GLN HG3 H 1 2.23 0.01 . 2 . . . . . . . . 4422 1 230 . 1 1 37 37 GLN HE21 H 1 6.90 0.01 . 2 . . . . . . . . 4422 1 231 . 1 1 37 37 GLN HE22 H 1 7.29 0.01 . 2 . . . . . . . . 4422 1 232 . 1 1 38 38 CYS H H 1 8.71 0.01 . 1 . . . . . . . . 4422 1 233 . 1 1 38 38 CYS HA H 1 4.82 0.01 . 1 . . . . . . . . 4422 1 234 . 1 1 38 38 CYS HB2 H 1 2.61 0.01 . 2 . . . . . . . . 4422 1 235 . 1 1 38 38 CYS HB3 H 1 3.04 0.01 . 2 . . . . . . . . 4422 1 236 . 1 1 39 39 GLN H H 1 8.41 0.01 . 1 . . . . . . . . 4422 1 237 . 1 1 39 39 GLN HA H 1 3.99 0.01 . 1 . . . . . . . . 4422 1 238 . 1 1 39 39 GLN HB2 H 1 1.52 0.01 . 2 . . . . . . . . 4422 1 239 . 1 1 39 39 GLN HB3 H 1 1.82 0.01 . 2 . . . . . . . . 4422 1 240 . 1 1 39 39 GLN HG2 H 1 1.90 0.01 . 2 . . . . . . . . 4422 1 241 . 1 1 39 39 GLN HG3 H 1 2.12 0.01 . 2 . . . . . . . . 4422 1 242 . 1 1 39 39 GLN HE21 H 1 6.76 0.01 . 2 . . . . . . . . 4422 1 243 . 1 1 39 39 GLN HE22 H 1 7.05 0.01 . 2 . . . . . . . . 4422 1 244 . 1 1 40 40 GLU H H 1 8.53 0.01 . 1 . . . . . . . . 4422 1 245 . 1 1 40 40 GLU HA H 1 4.01 0.01 . 1 . . . . . . . . 4422 1 246 . 1 1 40 40 GLU HB2 H 1 1.93 0.01 . 2 . . . . . . . . 4422 1 247 . 1 1 40 40 GLU HB3 H 1 1.99 0.01 . 2 . . . . . . . . 4422 1 248 . 1 1 40 40 GLU HG2 H 1 2.41 0.01 . 1 . . . . . . . . 4422 1 249 . 1 1 40 40 GLU HG3 H 1 2.41 0.01 . 1 . . . . . . . . 4422 1 250 . 1 1 41 41 GLY H H 1 8.64 0.01 . 1 . . . . . . . . 4422 1 251 . 1 1 41 41 GLY HA2 H 1 3.31 0.01 . 2 . . . . . . . . 4422 1 252 . 1 1 41 41 GLY HA3 H 1 4.06 0.01 . 2 . . . . . . . . 4422 1 253 . 1 1 42 42 PHE H H 1 8.11 0.01 . 1 . . . . . . . . 4422 1 254 . 1 1 42 42 PHE HA H 1 4.67 0.01 . 1 . . . . . . . . 4422 1 255 . 1 1 42 42 PHE HB2 H 1 3.14 0.01 . 2 . . . . . . . . 4422 1 256 . 1 1 42 42 PHE HB3 H 1 2.44 0.01 . 2 . . . . . . . . 4422 1 257 . 1 1 42 42 PHE HD1 H 1 6.63 0.01 . 1 . . . . . . . . 4422 1 258 . 1 1 42 42 PHE HD2 H 1 6.63 0.01 . 1 . . . . . . . . 4422 1 259 . 1 1 42 42 PHE HE1 H 1 7.05 0.01 . 1 . . . . . . . . 4422 1 260 . 1 1 42 42 PHE HE2 H 1 7.05 0.01 . 1 . . . . . . . . 4422 1 261 . 1 1 43 43 LEU H H 1 9.59 0.01 . 1 . . . . . . . . 4422 1 262 . 1 1 43 43 LEU HA H 1 4.47 0.01 . 1 . . . . . . . . 4422 1 263 . 1 1 43 43 LEU HB2 H 1 1.33 0.01 . 2 . . . . . . . . 4422 1 264 . 1 1 43 43 LEU HB3 H 1 0.95 0.01 . 2 . . . . . . . . 4422 1 265 . 1 1 43 43 LEU HG H 1 1.23 0.01 . 1 . . . . . . . . 4422 1 266 . 1 1 43 43 LEU HD11 H 1 0.68 0.01 . 2 . . . . . . . . 4422 1 267 . 1 1 43 43 LEU HD12 H 1 0.68 0.01 . 2 . . . . . . . . 4422 1 268 . 1 1 43 43 LEU HD13 H 1 0.68 0.01 . 2 . . . . . . . . 4422 1 269 . 1 1 43 43 LEU HD21 H 1 0.57 0.01 . 2 . . . . . . . . 4422 1 270 . 1 1 43 43 LEU HD22 H 1 0.57 0.01 . 2 . . . . . . . . 4422 1 271 . 1 1 43 43 LEU HD23 H 1 0.57 0.01 . 2 . . . . . . . . 4422 1 272 . 1 1 44 44 ARG H H 1 7.52 0.01 . 1 . . . . . . . . 4422 1 273 . 1 1 44 44 ARG HA H 1 4.75 0.01 . 1 . . . . . . . . 4422 1 274 . 1 1 44 44 ARG HB2 H 1 1.63 0.01 . 2 . . . . . . . . 4422 1 275 . 1 1 44 44 ARG HB3 H 1 1.78 0.01 . 2 . . . . . . . . 4422 1 276 . 1 1 44 44 ARG HG2 H 1 1.52 0.01 . 2 . . . . . . . . 4422 1 277 . 1 1 44 44 ARG HG3 H 1 1.77 0.01 . 2 . . . . . . . . 4422 1 278 . 1 1 44 44 ARG HD2 H 1 2.92 0.01 . 1 . . . . . . . . 4422 1 279 . 1 1 44 44 ARG HD3 H 1 2.92 0.01 . 1 . . . . . . . . 4422 1 280 . 1 1 44 44 ARG HE H 1 7.06 0.01 . 1 . . . . . . . . 4422 1 281 . 1 1 45 45 ASN H H 1 9.41 0.01 . 1 . . . . . . . . 4422 1 282 . 1 1 45 45 ASN HA H 1 4.60 0.01 . 1 . . . . . . . . 4422 1 283 . 1 1 45 45 ASN HB2 H 1 3.59 0.01 . 2 . . . . . . . . 4422 1 284 . 1 1 45 45 ASN HB3 H 1 2.83 0.01 . 2 . . . . . . . . 4422 1 285 . 1 1 45 45 ASN HD21 H 1 7.30 0.01 . 2 . . . . . . . . 4422 1 286 . 1 1 45 45 ASN HD22 H 1 7.75 0.01 . 2 . . . . . . . . 4422 1 287 . 1 1 46 46 GLY H H 1 8.66 0.01 . 1 . . . . . . . . 4422 1 288 . 1 1 46 46 GLY HA2 H 1 3.78 0.01 . 1 . . . . . . . . 4422 1 289 . 1 1 46 46 GLY HA3 H 1 3.78 0.01 . 1 . . . . . . . . 4422 1 290 . 1 1 47 47 GLU H H 1 7.46 0.01 . 1 . . . . . . . . 4422 1 291 . 1 1 47 47 GLU HA H 1 4.41 0.01 . 1 . . . . . . . . 4422 1 292 . 1 1 47 47 GLU HB2 H 1 1.91 0.01 . 2 . . . . . . . . 4422 1 293 . 1 1 47 47 GLU HB3 H 1 2.22 0.01 . 2 . . . . . . . . 4422 1 294 . 1 1 47 47 GLU HG2 H 1 2.30 0.01 . 2 . . . . . . . . 4422 1 295 . 1 1 47 47 GLU HG3 H 1 2.42 0.01 . 2 . . . . . . . . 4422 1 296 . 1 1 48 48 GLY H H 1 7.86 0.01 . 1 . . . . . . . . 4422 1 297 . 1 1 48 48 GLY HA2 H 1 3.44 0.01 . 2 . . . . . . . . 4422 1 298 . 1 1 48 48 GLY HA3 H 1 4.19 0.01 . 2 . . . . . . . . 4422 1 299 . 1 1 49 49 ALA H H 1 7.96 0.01 . 1 . . . . . . . . 4422 1 300 . 1 1 49 49 ALA HA H 1 4.35 0.01 . 1 . . . . . . . . 4422 1 301 . 1 1 49 49 ALA HB1 H 1 1.20 0.01 . 1 . . . . . . . . 4422 1 302 . 1 1 49 49 ALA HB2 H 1 1.20 0.01 . 1 . . . . . . . . 4422 1 303 . 1 1 49 49 ALA HB3 H 1 1.20 0.01 . 1 . . . . . . . . 4422 1 304 . 1 1 50 50 CYS H H 1 8.68 0.01 . 1 . . . . . . . . 4422 1 305 . 1 1 50 50 CYS HA H 1 4.93 0.01 . 1 . . . . . . . . 4422 1 306 . 1 1 50 50 CYS HB2 H 1 2.66 0.01 . 2 . . . . . . . . 4422 1 307 . 1 1 50 50 CYS HB3 H 1 2.35 0.01 . 2 . . . . . . . . 4422 1 308 . 1 1 51 51 VAL H H 1 9.47 0.01 . 1 . . . . . . . . 4422 1 309 . 1 1 51 51 VAL HA H 1 4.90 0.01 . 1 . . . . . . . . 4422 1 310 . 1 1 51 51 VAL HB H 1 2.17 0.01 . 1 . . . . . . . . 4422 1 311 . 1 1 51 51 VAL HG11 H 1 0.74 0.01 . 2 . . . . . . . . 4422 1 312 . 1 1 51 51 VAL HG12 H 1 0.74 0.01 . 2 . . . . . . . . 4422 1 313 . 1 1 51 51 VAL HG13 H 1 0.74 0.01 . 2 . . . . . . . . 4422 1 314 . 1 1 51 51 VAL HG21 H 1 0.66 0.01 . 2 . . . . . . . . 4422 1 315 . 1 1 51 51 VAL HG22 H 1 0.66 0.01 . 2 . . . . . . . . 4422 1 316 . 1 1 51 51 VAL HG23 H 1 0.66 0.01 . 2 . . . . . . . . 4422 1 317 . 1 1 52 52 LEU H H 1 8.75 0.01 . 1 . . . . . . . . 4422 1 318 . 1 1 52 52 LEU HA H 1 4.15 0.01 . 1 . . . . . . . . 4422 1 319 . 1 1 52 52 LEU HB2 H 1 1.31 0.01 . 2 . . . . . . . . 4422 1 320 . 1 1 52 52 LEU HB3 H 1 1.39 0.01 . 2 . . . . . . . . 4422 1 321 . 1 1 52 52 LEU HG H 1 1.41 0.01 . 1 . . . . . . . . 4422 1 322 . 1 1 52 52 LEU HD11 H 1 0.71 0.01 . 2 . . . . . . . . 4422 1 323 . 1 1 52 52 LEU HD12 H 1 0.71 0.01 . 2 . . . . . . . . 4422 1 324 . 1 1 52 52 LEU HD13 H 1 0.71 0.01 . 2 . . . . . . . . 4422 1 325 . 1 1 52 52 LEU HD21 H 1 0.13 0.01 . 2 . . . . . . . . 4422 1 326 . 1 1 52 52 LEU HD22 H 1 0.13 0.01 . 2 . . . . . . . . 4422 1 327 . 1 1 52 52 LEU HD23 H 1 0.13 0.01 . 2 . . . . . . . . 4422 1 328 . 1 1 53 53 PRO HA H 1 4.12 0.01 . 1 . . . . . . . . 4422 1 329 . 1 1 53 53 PRO HB2 H 1 1.75 0.01 . 2 . . . . . . . . 4422 1 330 . 1 1 53 53 PRO HB3 H 1 2.17 0.01 . 2 . . . . . . . . 4422 1 331 . 1 1 53 53 PRO HG2 H 1 1.70 0.01 . 2 . . . . . . . . 4422 1 332 . 1 1 53 53 PRO HG3 H 1 1.99 0.01 . 2 . . . . . . . . 4422 1 333 . 1 1 53 53 PRO HD2 H 1 3.42 0.01 . 2 . . . . . . . . 4422 1 334 . 1 1 53 53 PRO HD3 H 1 3.87 0.01 . 2 . . . . . . . . 4422 1 335 . 1 1 54 54 GLU H H 1 8.31 0.01 . 1 . . . . . . . . 4422 1 336 . 1 1 54 54 GLU HA H 1 4.08 0.01 . 1 . . . . . . . . 4422 1 337 . 1 1 54 54 GLU HB2 H 1 1.91 0.01 . 2 . . . . . . . . 4422 1 338 . 1 1 54 54 GLU HB3 H 1 1.94 0.01 . 2 . . . . . . . . 4422 1 339 . 1 1 54 54 GLU HG2 H 1 2.20 0.01 . 2 . . . . . . . . 4422 1 340 . 1 1 54 54 GLU HG3 H 1 2.26 0.01 . 2 . . . . . . . . 4422 1 341 . 1 1 55 55 ASN H H 1 8.38 0.01 . 1 . . . . . . . . 4422 1 342 . 1 1 55 55 ASN HA H 1 4.93 0.01 . 1 . . . . . . . . 4422 1 343 . 1 1 55 55 ASN HB2 H 1 2.55 0.01 . 2 . . . . . . . . 4422 1 344 . 1 1 55 55 ASN HB3 H 1 3.10 0.01 . 2 . . . . . . . . 4422 1 345 . 1 1 55 55 ASN HD21 H 1 6.99 0.01 . 2 . . . . . . . . 4422 1 346 . 1 1 55 55 ASN HD22 H 1 7.74 0.01 . 2 . . . . . . . . 4422 1 347 . 1 1 56 56 CYS H H 1 7.39 0.01 . 1 . . . . . . . . 4422 1 348 . 1 1 56 56 CYS HA H 1 4.23 0.01 . 1 . . . . . . . . 4422 1 349 . 1 1 56 56 CYS HB2 H 1 2.89 0.01 . 2 . . . . . . . . 4422 1 350 . 1 1 56 56 CYS HB3 H 1 3.06 0.01 . 2 . . . . . . . . 4422 1 stop_ save_