data_5535 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5535 _Entry.Title ; NMR structure of R3H domain ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2002-09-20 _Entry.Accession_date 2002-09-20 _Entry.Last_release_date 2003-02-21 _Entry.Original_release_date 2003-02-21 _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 Edvards Liepinsh . . . 5535 2 Gottfried Otting . . . 5535 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5535 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 505 5535 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 . . 2003-02-21 2002-09-20 original author . 5535 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5535 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12547203 _Citation.Full_citation . _Citation.Title 'Solution Structure of the R3H Domain from Human Subp-2' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 326 _Citation.Journal_issue 1 _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 217 _Citation.Page_last 223 _Citation.Year 2003 _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 Edvards Liepinsh . . . 5535 1 2 Ainars Leonchiks . . . 5535 1 3 Anatoly Sharipo . . . 5535 1 4 Laurent Guignard . . . 5535 1 5 Gottfried Otting . . . 5535 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID R3H 5535 1 'NMR structure' 5535 1 stop_ save_ save_reference_1 _Citation.Sf_category citations _Citation.Sf_framecode reference_1 _Citation.Entry_ID 5535 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12547203 _Citation.Full_citation ; Edvards Liepinsh, Ainars Leonchiks, Anatoly Sharipo, Laurent Guignard and Gottfried Otting. Solution structure of the R3H domain from human Subp-2 J. Biol. Chem., submitted. ; _Citation.Title 'Solution structure of the R3H domain from human Smubp-2.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 326 _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 217 _Citation.Page_last 223 _Citation.Year 2003 _Citation.Details ; The R3H domain is a conserved sequence motif, identified in over 100 proteins, that is thought to be involved in polynucleotide-binding, including DNA, RNA and single-stranded DNA. In this work the 3D structure of the R3H domain from human Smubp-2 was determined by NMR spectroscopy. It is the first 3D structure determination of an R3H domain. The fold presents a small motif, consisting of a three-stranded antiparallel beta-sheet and two alpha-helices, which is related to the structures of the YhhP protein and the C-terminal domain of the translational initiation factor IF3. The similarities are non-trivial, as the amino acid identities are below 10%. Three conserved basic residues cluster on the same face of the R3H domain and could play a role in nucleic acid recognition. An extended hydrophobic area at a different site of the molecular surface could act as a protein-binding site. A strong correlation between conservation of hydrophobic amino acids and side-chain solvent protection indicates that the structure of the Smubp-2 R3H domain is representative of R3H domains in general. ; 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 Edvards Liepinsh E. . . 5535 2 2 Ainars Leonchiks A. . . 5535 2 3 Anatoly Sharipo A. . . 5535 2 4 Laurent Guignard L. . . 5535 2 5 Gottfried Otting G. . . 5535 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_R3H _Assembly.Sf_category assembly _Assembly.Sf_framecode system_R3H _Assembly.Entry_ID 5535 _Assembly.ID 1 _Assembly.Name 'R3H domain' _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 'not present' _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 5535 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 'R3H domain' 1 $R3H . . . native . . . . . 5535 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 1MSZ . . . . . 'Residue numbering differs by 708' 5535 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'R3H domain' system 5535 1 R3H abbreviation 5535 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_R3H _Entity.Sf_category entity _Entity.Sf_framecode R3H _Entity.Entry_ID 5535 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'single chain biopolymer' _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 ; MGSLNGGSPEGVESQDGVDH FRAMIVEFMASKKMQLEFPP SLNSHDRLRVHQIAEEHGLR HDSSGEGKRRFITVSKRAGS HHHHHH ; _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 86 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 9674 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 18391 . Smubp2_R3H . . . . . 100.00 86 100.00 100.00 1.33e-53 . . . . 5535 1 2 no PDB 1MSZ . "Solution Structure Of The R3h Domain From Human Smubp-2" . . . . . 100.00 86 100.00 100.00 1.33e-53 . . . . 5535 1 3 no PDB 2LRR . "Solution Structure Of The R3h Domain From Human Smubp-2 In Complex With 2'-Deoxyguanosine-5'-Monophosphate" . . . . . 100.00 86 100.00 100.00 1.33e-53 . . . . 5535 1 4 no DBJ BAD92039 . "immunoglobulin mu binding protein 2 variant [Homo sapiens]" . . . . . 88.37 629 100.00 100.00 2.50e-43 . . . . 5535 1 5 no DBJ BAG35460 . "unnamed protein product [Homo sapiens]" . . . . . 88.37 993 100.00 100.00 6.31e-43 . . . . 5535 1 6 no GB AAA53082 . "DNA-binding protein [Homo sapiens]" . . . . . 88.37 993 100.00 100.00 6.44e-43 . . . . 5535 1 7 no GB AAA58611 . "glial factor-1, partial [Homo sapiens]" . . . . . 88.37 376 100.00 100.00 2.80e-44 . . . . 5535 1 8 no GB AAA70430 . "DNA helicase [Homo sapiens]" . . . . . 88.37 993 100.00 100.00 6.31e-43 . . . . 5535 1 9 no GB AAH00290 . "IGHMBP2 protein, partial [Homo sapiens]" . . . . . 88.37 868 100.00 100.00 4.64e-43 . . . . 5535 1 10 no GB AAH25299 . "IGHMBP2 protein, partial [Homo sapiens]" . . . . . 88.37 868 100.00 100.00 4.64e-43 . . . . 5535 1 11 no REF NP_002171 . "DNA-binding protein SMUBP-2 [Homo sapiens]" . . . . . 88.37 993 100.00 100.00 6.31e-43 . . . . 5535 1 12 no REF XP_002821469 . "PREDICTED: DNA-binding protein SMUBP-2, partial [Pongo abelii]" . . . . . 88.37 780 98.68 98.68 5.29e-42 . . . . 5535 1 13 no REF XP_003274011 . "PREDICTED: DNA-binding protein SMUBP-2 [Nomascus leucogenys]" . . . . . 88.37 1002 100.00 100.00 7.55e-43 . . . . 5535 1 14 no REF XP_003828806 . "PREDICTED: DNA-binding protein SMUBP-2 [Pan paniscus]" . . . . . 88.37 1001 100.00 100.00 7.31e-43 . . . . 5535 1 15 no REF XP_004051731 . "PREDICTED: DNA-binding protein SMUBP-2 [Gorilla gorilla gorilla]" . . . . . 88.37 997 98.68 100.00 2.47e-42 . . . . 5535 1 16 no SP P38935 . "RecName: Full=DNA-binding protein SMUBP-2; AltName: Full=ATP-dependent helicase IGHMBP2; AltName: Full=Glial factor 1; Short=GF" . . . . . 88.37 993 100.00 100.00 6.31e-43 . . . . 5535 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'single chain biopolymer' common 5535 1 R3H abbreviation 5535 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 1 709 MET . 5535 1 2 710 GLY . 5535 1 3 711 SER . 5535 1 4 712 LEU . 5535 1 5 713 ASN . 5535 1 6 714 GLY . 5535 1 7 715 GLY . 5535 1 8 716 SER . 5535 1 9 717 PRO . 5535 1 10 718 GLU . 5535 1 11 719 GLY . 5535 1 12 720 VAL . 5535 1 13 721 GLU . 5535 1 14 722 SER . 5535 1 15 723 GLN . 5535 1 16 724 ASP . 5535 1 17 725 GLY . 5535 1 18 726 VAL . 5535 1 19 727 ASP . 5535 1 20 728 HIS . 5535 1 21 729 PHE . 5535 1 22 730 ARG . 5535 1 23 731 ALA . 5535 1 24 732 MET . 5535 1 25 733 ILE . 5535 1 26 734 VAL . 5535 1 27 735 GLU . 5535 1 28 736 PHE . 5535 1 29 737 MET . 5535 1 30 738 ALA . 5535 1 31 739 SER . 5535 1 32 740 LYS . 5535 1 33 741 LYS . 5535 1 34 742 MET . 5535 1 35 743 GLN . 5535 1 36 744 LEU . 5535 1 37 745 GLU . 5535 1 38 746 PHE . 5535 1 39 747 PRO . 5535 1 40 748 PRO . 5535 1 41 749 SER . 5535 1 42 750 LEU . 5535 1 43 751 ASN . 5535 1 44 752 SER . 5535 1 45 753 HIS . 5535 1 46 754 ASP . 5535 1 47 755 ARG . 5535 1 48 756 LEU . 5535 1 49 757 ARG . 5535 1 50 758 VAL . 5535 1 51 759 HIS . 5535 1 52 760 GLN . 5535 1 53 761 ILE . 5535 1 54 762 ALA . 5535 1 55 763 GLU . 5535 1 56 764 GLU . 5535 1 57 765 HIS . 5535 1 58 766 GLY . 5535 1 59 767 LEU . 5535 1 60 768 ARG . 5535 1 61 769 HIS . 5535 1 62 770 ASP . 5535 1 63 771 SER . 5535 1 64 772 SER . 5535 1 65 773 GLY . 5535 1 66 774 GLU . 5535 1 67 775 GLY . 5535 1 68 776 LYS . 5535 1 69 777 ARG . 5535 1 70 778 ARG . 5535 1 71 779 PHE . 5535 1 72 780 ILE . 5535 1 73 781 THR . 5535 1 74 782 VAL . 5535 1 75 783 SER . 5535 1 76 784 LYS . 5535 1 77 785 ARG . 5535 1 78 786 ALA . 5535 1 79 787 GLY . 5535 1 80 788 SER . 5535 1 81 789 HIS . 5535 1 82 790 HIS . 5535 1 83 791 HIS . 5535 1 84 792 HIS . 5535 1 85 793 HIS . 5535 1 86 794 HIS . 5535 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 . MET 1 1 5535 1 . GLY 2 2 5535 1 . SER 3 3 5535 1 . LEU 4 4 5535 1 . ASN 5 5 5535 1 . GLY 6 6 5535 1 . GLY 7 7 5535 1 . SER 8 8 5535 1 . PRO 9 9 5535 1 . GLU 10 10 5535 1 . GLY 11 11 5535 1 . VAL 12 12 5535 1 . GLU 13 13 5535 1 . SER 14 14 5535 1 . GLN 15 15 5535 1 . ASP 16 16 5535 1 . GLY 17 17 5535 1 . VAL 18 18 5535 1 . ASP 19 19 5535 1 . HIS 20 20 5535 1 . PHE 21 21 5535 1 . ARG 22 22 5535 1 . ALA 23 23 5535 1 . MET 24 24 5535 1 . ILE 25 25 5535 1 . VAL 26 26 5535 1 . GLU 27 27 5535 1 . PHE 28 28 5535 1 . MET 29 29 5535 1 . ALA 30 30 5535 1 . SER 31 31 5535 1 . LYS 32 32 5535 1 . LYS 33 33 5535 1 . MET 34 34 5535 1 . GLN 35 35 5535 1 . LEU 36 36 5535 1 . GLU 37 37 5535 1 . PHE 38 38 5535 1 . PRO 39 39 5535 1 . PRO 40 40 5535 1 . SER 41 41 5535 1 . LEU 42 42 5535 1 . ASN 43 43 5535 1 . SER 44 44 5535 1 . HIS 45 45 5535 1 . ASP 46 46 5535 1 . ARG 47 47 5535 1 . LEU 48 48 5535 1 . ARG 49 49 5535 1 . VAL 50 50 5535 1 . HIS 51 51 5535 1 . GLN 52 52 5535 1 . ILE 53 53 5535 1 . ALA 54 54 5535 1 . GLU 55 55 5535 1 . GLU 56 56 5535 1 . HIS 57 57 5535 1 . GLY 58 58 5535 1 . LEU 59 59 5535 1 . ARG 60 60 5535 1 . HIS 61 61 5535 1 . ASP 62 62 5535 1 . SER 63 63 5535 1 . SER 64 64 5535 1 . GLY 65 65 5535 1 . GLU 66 66 5535 1 . GLY 67 67 5535 1 . LYS 68 68 5535 1 . ARG 69 69 5535 1 . ARG 70 70 5535 1 . PHE 71 71 5535 1 . ILE 72 72 5535 1 . THR 73 73 5535 1 . VAL 74 74 5535 1 . SER 75 75 5535 1 . LYS 76 76 5535 1 . ARG 77 77 5535 1 . ALA 78 78 5535 1 . GLY 79 79 5535 1 . SER 80 80 5535 1 . HIS 81 81 5535 1 . HIS 82 82 5535 1 . HIS 83 83 5535 1 . HIS 84 84 5535 1 . HIS 85 85 5535 1 . HIS 86 86 5535 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 5535 _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 $R3H . 9606 . . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . . . . . . 5535 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 5535 _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 $R3H . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli M15 . . . . . . . . . . . . plasmid . . pQE60 . . . . . . 5535 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5535 _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 'single chain biopolymer' . . . 1 $R3H . . 0.4 . . mM . . . . 5535 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 5535 _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 6.9 0.2 n/a 5535 1 temperature 298 1 K 5535 1 'ionic strength' 0.1 . M 5535 1 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 5535 _Software.ID 1 _Software.Name XWINNMR _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'spectral processing' 5535 1 stop_ save_ save_PROSA _Software.Sf_category software _Software.Sf_framecode PROSA _Software.Entry_ID 5535 _Software.ID 2 _Software.Name PROSA _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'spectral processing' 5535 2 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 5535 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 5535 _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 DMX . 600 . . . 5535 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 5535 _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 '2D 1H-1H HOHAHA' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5535 1 2 '2D 1H-1H NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5535 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 5535 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '2D 1H-1H HOHAHA' _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 . _NMR_spec_expt.NMR_spectrometer_label . _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 5535 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '2D 1H-1H 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 . _NMR_spec_expt.NMR_spectrometer_label . _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 5535 _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 . . . . . . . . . 5535 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5535 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5535 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5535 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_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 . _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 . 5535 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 MET HA H 1 4.05 0.02 . 1 . . . . . . . . 5535 1 2 . 1 1 1 1 MET HB2 H 1 2.03 0.02 . 1 . . . . . . . . 5535 1 3 . 1 1 1 1 MET HB3 H 1 2.03 0.02 . 1 . . . . . . . . 5535 1 4 . 1 1 1 1 MET HG2 H 1 2.31 0.02 . 2 . . . . . . . . 5535 1 5 . 1 1 1 1 MET HG3 H 1 2.41 0.02 . 2 . . . . . . . . 5535 1 6 . 1 1 4 4 LEU H H 1 8.39 0.02 . 1 . . . . . . . . 5535 1 7 . 1 1 4 4 LEU HA H 1 4.34 0.02 . 1 . . . . . . . . 5535 1 8 . 1 1 4 4 LEU HB2 H 1 1.56 0.02 . 1 . . . . . . . . 5535 1 9 . 1 1 4 4 LEU HB3 H 1 1.56 0.02 . 1 . . . . . . . . 5535 1 10 . 1 1 4 4 LEU HD11 H 1 0.81 0.02 . 2 . . . . . . . . 5535 1 11 . 1 1 4 4 LEU HD12 H 1 0.81 0.02 . 2 . . . . . . . . 5535 1 12 . 1 1 4 4 LEU HD13 H 1 0.81 0.02 . 2 . . . . . . . . 5535 1 13 . 1 1 4 4 LEU HD21 H 1 0.86 0.02 . 2 . . . . . . . . 5535 1 14 . 1 1 4 4 LEU HD22 H 1 0.86 0.02 . 2 . . . . . . . . 5535 1 15 . 1 1 4 4 LEU HD23 H 1 0.86 0.02 . 2 . . . . . . . . 5535 1 16 . 1 1 4 4 LEU HG H 1 1.66 0.02 . 1 . . . . . . . . 5535 1 17 . 1 1 5 5 ASN H H 1 7.89 0.02 . 1 . . . . . . . . 5535 1 18 . 1 1 5 5 ASN HA H 1 4.4 0.02 . 1 . . . . . . . . 5535 1 19 . 1 1 5 5 ASN HB2 H 1 2.65 0.02 . 2 . . . . . . . . 5535 1 20 . 1 1 5 5 ASN HB3 H 1 2.76 0.02 . 2 . . . . . . . . 5535 1 21 . 1 1 9 9 PRO HA H 1 4.39 0.02 . 1 . . . . . . . . 5535 1 22 . 1 1 9 9 PRO HB2 H 1 1.89 0.02 . 2 . . . . . . . . 5535 1 23 . 1 1 9 9 PRO HB3 H 1 2.23 0.02 . 2 . . . . . . . . 5535 1 24 . 1 1 9 9 PRO HG2 H 1 1.96 0.02 . 1 . . . . . . . . 5535 1 25 . 1 1 9 9 PRO HG3 H 1 1.96 0.02 . 1 . . . . . . . . 5535 1 26 . 1 1 9 9 PRO HD2 H 1 3.67 0.02 . 2 . . . . . . . . 5535 1 27 . 1 1 9 9 PRO HD3 H 1 3.76 0.02 . 2 . . . . . . . . 5535 1 28 . 1 1 10 10 GLU H H 1 8.44 0.02 . 1 . . . . . . . . 5535 1 29 . 1 1 10 10 GLU HA H 1 4.21 0.02 . 1 . . . . . . . . 5535 1 30 . 1 1 10 10 GLU HB2 H 1 1.89 0.02 . 2 . . . . . . . . 5535 1 31 . 1 1 10 10 GLU HB3 H 1 1.99 0.02 . 2 . . . . . . . . 5535 1 32 . 1 1 10 10 GLU HG2 H 1 2.23 0.02 . 1 . . . . . . . . 5535 1 33 . 1 1 10 10 GLU HG3 H 1 2.23 0.02 . 1 . . . . . . . . 5535 1 34 . 1 1 11 11 GLY H H 1 8.327 0.02 . 1 . . . . . . . . 5535 1 35 . 1 1 11 11 GLY HA2 H 1 3.916 0.02 . 1 . . . . . . . . 5535 1 36 . 1 1 11 11 GLY HA3 H 1 3.916 0.02 . 1 . . . . . . . . 5535 1 37 . 1 1 12 12 VAL H H 1 7.865 0.02 . 1 . . . . . . . . 5535 1 38 . 1 1 12 12 VAL HA H 1 4.076 0.02 . 1 . . . . . . . . 5535 1 39 . 1 1 12 12 VAL HB H 1 2.033 0.02 . 1 . . . . . . . . 5535 1 40 . 1 1 12 12 VAL HG11 H 1 0.845 0.02 . 2 . . . . . . . . 5535 1 41 . 1 1 12 12 VAL HG12 H 1 0.845 0.02 . 2 . . . . . . . . 5535 1 42 . 1 1 12 12 VAL HG13 H 1 0.845 0.02 . 2 . . . . . . . . 5535 1 43 . 1 1 12 12 VAL HG21 H 1 0.867 0.02 . 2 . . . . . . . . 5535 1 44 . 1 1 12 12 VAL HG22 H 1 0.867 0.02 . 2 . . . . . . . . 5535 1 45 . 1 1 12 12 VAL HG23 H 1 0.867 0.02 . 2 . . . . . . . . 5535 1 46 . 1 1 13 13 GLU H H 1 8.54 0.02 . 1 . . . . . . . . 5535 1 47 . 1 1 13 13 GLU HA H 1 4.259 0.02 . 1 . . . . . . . . 5535 1 48 . 1 1 13 13 GLU HB2 H 1 1.891 0.02 . 2 . . . . . . . . 5535 1 49 . 1 1 13 13 GLU HB3 H 1 2.002 0.02 . 2 . . . . . . . . 5535 1 50 . 1 1 13 13 GLU HG2 H 1 2.222 0.02 . 1 . . . . . . . . 5535 1 51 . 1 1 13 13 GLU HG3 H 1 2.222 0.02 . 1 . . . . . . . . 5535 1 52 . 1 1 14 14 SER H H 1 8.312 0.02 . 1 . . . . . . . . 5535 1 53 . 1 1 14 14 SER HA H 1 4.381 0.02 . 1 . . . . . . . . 5535 1 54 . 1 1 14 14 SER HB2 H 1 3.787 0.02 . 2 . . . . . . . . 5535 1 55 . 1 1 14 14 SER HB3 H 1 3.844 0.02 . 2 . . . . . . . . 5535 1 56 . 1 1 15 15 GLN H H 1 8.476 0.02 . 1 . . . . . . . . 5535 1 57 . 1 1 15 15 GLN HA H 1 4.299 0.02 . 1 . . . . . . . . 5535 1 58 . 1 1 15 15 GLN HB2 H 1 1.916 0.02 . 2 . . . . . . . . 5535 1 59 . 1 1 15 15 GLN HB3 H 1 2.096 0.02 . 2 . . . . . . . . 5535 1 60 . 1 1 15 15 GLN HG2 H 1 2.3 0.02 . 1 . . . . . . . . 5535 1 61 . 1 1 15 15 GLN HG3 H 1 2.3 0.02 . 1 . . . . . . . . 5535 1 62 . 1 1 15 15 GLN HE21 H 1 7.482 0.02 . 1 . . . . . . . . 5535 1 63 . 1 1 15 15 GLN HE22 H 1 6.772 0.02 . 1 . . . . . . . . 5535 1 64 . 1 1 16 16 ASP H H 1 8.284 0.02 . 1 . . . . . . . . 5535 1 65 . 1 1 16 16 ASP HA H 1 4.503 0.02 . 1 . . . . . . . . 5535 1 66 . 1 1 16 16 ASP HB2 H 1 2.603 0.02 . 1 . . . . . . . . 5535 1 67 . 1 1 16 16 ASP HB3 H 1 2.603 0.02 . 1 . . . . . . . . 5535 1 68 . 1 1 17 17 GLY H H 1 8.263 0.02 . 1 . . . . . . . . 5535 1 69 . 1 1 17 17 GLY HA2 H 1 3.867 0.02 . 1 . . . . . . . . 5535 1 70 . 1 1 17 17 GLY HA3 H 1 3.867 0.02 . 1 . . . . . . . . 5535 1 71 . 1 1 18 18 VAL H H 1 7.917 0.02 . 1 . . . . . . . . 5535 1 72 . 1 1 18 18 VAL HA H 1 3.881 0.02 . 1 . . . . . . . . 5535 1 73 . 1 1 18 18 VAL HB H 1 1.992 0.02 . 1 . . . . . . . . 5535 1 74 . 1 1 18 18 VAL HG11 H 1 0.811 0.02 . 2 . . . . . . . . 5535 1 75 . 1 1 18 18 VAL HG12 H 1 0.811 0.02 . 2 . . . . . . . . 5535 1 76 . 1 1 18 18 VAL HG13 H 1 0.811 0.02 . 2 . . . . . . . . 5535 1 77 . 1 1 18 18 VAL HG21 H 1 0.878 0.02 . 2 . . . . . . . . 5535 1 78 . 1 1 18 18 VAL HG22 H 1 0.878 0.02 . 2 . . . . . . . . 5535 1 79 . 1 1 18 18 VAL HG23 H 1 0.878 0.02 . 2 . . . . . . . . 5535 1 80 . 1 1 19 19 ASP H H 1 8.353 0.02 . 1 . . . . . . . . 5535 1 81 . 1 1 19 19 ASP HA H 1 4.514 0.02 . 1 . . . . . . . . 5535 1 82 . 1 1 19 19 ASP HB2 H 1 2.557 0.02 . 2 . . . . . . . . 5535 1 83 . 1 1 19 19 ASP HB3 H 1 2.724 0.02 . 2 . . . . . . . . 5535 1 84 . 1 1 20 20 HIS H H 1 7.98 0.02 . 1 . . . . . . . . 5535 1 85 . 1 1 20 20 HIS HA H 1 4.351 0.02 . 1 . . . . . . . . 5535 1 86 . 1 1 20 20 HIS HB2 H 1 2.908 0.02 . 2 . . . . . . . . 5535 1 87 . 1 1 20 20 HIS HB3 H 1 2.99 0.02 . 2 . . . . . . . . 5535 1 88 . 1 1 20 20 HIS HD2 H 1 6.585 0.02 . 1 . . . . . . . . 5535 1 89 . 1 1 20 20 HIS HE1 H 1 7.827 0.02 . 1 . . . . . . . . 5535 1 90 . 1 1 21 21 PHE H H 1 7.853 0.02 . 1 . . . . . . . . 5535 1 91 . 1 1 21 21 PHE HA H 1 4.523 0.02 . 1 . . . . . . . . 5535 1 92 . 1 1 21 21 PHE HB2 H 1 2.9 0.02 . 1 . . . . . . . . 5535 1 93 . 1 1 21 21 PHE HB3 H 1 2.9 0.02 . 1 . . . . . . . . 5535 1 94 . 1 1 21 21 PHE HD1 H 1 7.135 0.02 . 1 . . . . . . . . 5535 1 95 . 1 1 21 21 PHE HD2 H 1 7.135 0.02 . 1 . . . . . . . . 5535 1 96 . 1 1 21 21 PHE HE1 H 1 7.349 0.02 . 1 . . . . . . . . 5535 1 97 . 1 1 21 21 PHE HE2 H 1 7.349 0.02 . 1 . . . . . . . . 5535 1 98 . 1 1 21 21 PHE HZ H 1 7.217 0.02 . 1 . . . . . . . . 5535 1 99 . 1 1 22 22 ARG H H 1 8.238 0.02 . 1 . . . . . . . . 5535 1 100 . 1 1 22 22 ARG HA H 1 3.813 0.02 . 1 . . . . . . . . 5535 1 101 . 1 1 22 22 ARG HB2 H 1 1.87 0.02 . 1 . . . . . . . . 5535 1 102 . 1 1 22 22 ARG HB3 H 1 1.87 0.02 . 1 . . . . . . . . 5535 1 103 . 1 1 22 22 ARG HG2 H 1 1.59 0.02 . 1 . . . . . . . . 5535 1 104 . 1 1 22 22 ARG HG3 H 1 1.59 0.02 . 1 . . . . . . . . 5535 1 105 . 1 1 22 22 ARG HD2 H 1 3.192 0.02 . 2 . . . . . . . . 5535 1 106 . 1 1 22 22 ARG HD3 H 1 3.345 0.02 . 2 . . . . . . . . 5535 1 107 . 1 1 23 23 ALA H H 1 7.985 0.02 . 1 . . . . . . . . 5535 1 108 . 1 1 23 23 ALA HA H 1 4.014 0.02 . 1 . . . . . . . . 5535 1 109 . 1 1 23 23 ALA HB1 H 1 1.428 0.02 . 1 . . . . . . . . 5535 1 110 . 1 1 23 23 ALA HB2 H 1 1.428 0.02 . 1 . . . . . . . . 5535 1 111 . 1 1 23 23 ALA HB3 H 1 1.428 0.02 . 1 . . . . . . . . 5535 1 112 . 1 1 24 24 MET H H 1 7.956 0.02 . 1 . . . . . . . . 5535 1 113 . 1 1 24 24 MET HA H 1 4.038 0.02 . 1 . . . . . . . . 5535 1 114 . 1 1 24 24 MET HB2 H 1 2.001 0.02 . 1 . . . . . . . . 5535 1 115 . 1 1 24 24 MET HB3 H 1 2.311 0.02 . 1 . . . . . . . . 5535 1 116 . 1 1 24 24 MET HG2 H 1 2.418 0.02 . 1 . . . . . . . . 5535 1 117 . 1 1 24 24 MET HG3 H 1 2.578 0.02 . 1 . . . . . . . . 5535 1 118 . 1 1 24 24 MET HE1 H 1 1.775 0.02 . 1 . . . . . . . . 5535 1 119 . 1 1 24 24 MET HE2 H 1 1.775 0.02 . 1 . . . . . . . . 5535 1 120 . 1 1 24 24 MET HE3 H 1 1.775 0.02 . 1 . . . . . . . . 5535 1 121 . 1 1 25 25 ILE H H 1 7.942 0.02 . 1 . . . . . . . . 5535 1 122 . 1 1 25 25 ILE HA H 1 3.712 0.02 . 1 . . . . . . . . 5535 1 123 . 1 1 25 25 ILE HB H 1 1.945 0.02 . 1 . . . . . . . . 5535 1 124 . 1 1 25 25 ILE HG21 H 1 0.512 0.02 . 1 . . . . . . . . 5535 1 125 . 1 1 25 25 ILE HG22 H 1 0.512 0.02 . 1 . . . . . . . . 5535 1 126 . 1 1 25 25 ILE HG23 H 1 0.512 0.02 . 1 . . . . . . . . 5535 1 127 . 1 1 25 25 ILE HG12 H 1 1.174 0.02 . 1 . . . . . . . . 5535 1 128 . 1 1 25 25 ILE HG13 H 1 1.758 0.02 . 1 . . . . . . . . 5535 1 129 . 1 1 25 25 ILE HD11 H 1 0.763 0.02 . 1 . . . . . . . . 5535 1 130 . 1 1 25 25 ILE HD12 H 1 0.763 0.02 . 1 . . . . . . . . 5535 1 131 . 1 1 25 25 ILE HD13 H 1 0.763 0.02 . 1 . . . . . . . . 5535 1 132 . 1 1 26 26 VAL H H 1 8.704 0.02 . 1 . . . . . . . . 5535 1 133 . 1 1 26 26 VAL HA H 1 3.472 0.02 . 1 . . . . . . . . 5535 1 134 . 1 1 26 26 VAL HB H 1 2.054 0.02 . 1 . . . . . . . . 5535 1 135 . 1 1 26 26 VAL HG11 H 1 0.887 0.02 . 1 . . . . . . . . 5535 1 136 . 1 1 26 26 VAL HG12 H 1 0.887 0.02 . 1 . . . . . . . . 5535 1 137 . 1 1 26 26 VAL HG13 H 1 0.887 0.02 . 1 . . . . . . . . 5535 1 138 . 1 1 26 26 VAL HG21 H 1 0.967 0.02 . 1 . . . . . . . . 5535 1 139 . 1 1 26 26 VAL HG22 H 1 0.967 0.02 . 1 . . . . . . . . 5535 1 140 . 1 1 26 26 VAL HG23 H 1 0.967 0.02 . 1 . . . . . . . . 5535 1 141 . 1 1 27 27 GLU H H 1 8.032 0.02 . 1 . . . . . . . . 5535 1 142 . 1 1 27 27 GLU HA H 1 4.02 0.02 . 1 . . . . . . . . 5535 1 143 . 1 1 27 27 GLU HB2 H 1 2.05 0.02 . 1 . . . . . . . . 5535 1 144 . 1 1 27 27 GLU HB3 H 1 2.05 0.02 . 1 . . . . . . . . 5535 1 145 . 1 1 27 27 GLU HG2 H 1 2.187 0.02 . 2 . . . . . . . . 5535 1 146 . 1 1 27 27 GLU HG3 H 1 2.342 0.02 . 2 . . . . . . . . 5535 1 147 . 1 1 28 28 PHE H H 1 7.903 0.02 . 1 . . . . . . . . 5535 1 148 . 1 1 28 28 PHE HA H 1 4.445 0.02 . 1 . . . . . . . . 5535 1 149 . 1 1 28 28 PHE HB2 H 1 3.31 0.02 . 1 . . . . . . . . 5535 1 150 . 1 1 28 28 PHE HB3 H 1 3.31 0.02 . 1 . . . . . . . . 5535 1 151 . 1 1 28 28 PHE HD1 H 1 6.98 0.02 . 1 . . . . . . . . 5535 1 152 . 1 1 28 28 PHE HD2 H 1 6.98 0.02 . 1 . . . . . . . . 5535 1 153 . 1 1 28 28 PHE HE1 H 1 6.808 0.02 . 1 . . . . . . . . 5535 1 154 . 1 1 28 28 PHE HE2 H 1 6.808 0.02 . 1 . . . . . . . . 5535 1 155 . 1 1 28 28 PHE HZ H 1 6.903 0.02 . 1 . . . . . . . . 5535 1 156 . 1 1 29 29 MET H H 1 8.699 0.02 . 1 . . . . . . . . 5535 1 157 . 1 1 29 29 MET HA H 1 3.518 0.02 . 1 . . . . . . . . 5535 1 158 . 1 1 29 29 MET HB2 H 1 2.098 0.02 . 1 . . . . . . . . 5535 1 159 . 1 1 29 29 MET HB3 H 1 2.169 0.02 . 1 . . . . . . . . 5535 1 160 . 1 1 29 29 MET HG2 H 1 2.425 0.02 . 1 . . . . . . . . 5535 1 161 . 1 1 29 29 MET HG3 H 1 2.712 0.02 . 1 . . . . . . . . 5535 1 162 . 1 1 29 29 MET HE1 H 1 2.054 0.02 . 1 . . . . . . . . 5535 1 163 . 1 1 29 29 MET HE2 H 1 2.054 0.02 . 1 . . . . . . . . 5535 1 164 . 1 1 29 29 MET HE3 H 1 2.054 0.02 . 1 . . . . . . . . 5535 1 165 . 1 1 30 30 ALA H H 1 7.088 0.02 . 1 . . . . . . . . 5535 1 166 . 1 1 30 30 ALA HA H 1 4.251 0.02 . 1 . . . . . . . . 5535 1 167 . 1 1 30 30 ALA HB1 H 1 1.418 0.02 . 1 . . . . . . . . 5535 1 168 . 1 1 30 30 ALA HB2 H 1 1.418 0.02 . 1 . . . . . . . . 5535 1 169 . 1 1 30 30 ALA HB3 H 1 1.418 0.02 . 1 . . . . . . . . 5535 1 170 . 1 1 31 31 SER H H 1 7.411 0.02 . 1 . . . . . . . . 5535 1 171 . 1 1 31 31 SER HA H 1 4.545 0.02 . 1 . . . . . . . . 5535 1 172 . 1 1 31 31 SER HB2 H 1 4.133 0.02 . 2 . . . . . . . . 5535 1 173 . 1 1 31 31 SER HB3 H 1 4.179 0.02 . 2 . . . . . . . . 5535 1 174 . 1 1 32 32 LYS H H 1 8.443 0.02 . 1 . . . . . . . . 5535 1 175 . 1 1 32 32 LYS HA H 1 4.333 0.02 . 1 . . . . . . . . 5535 1 176 . 1 1 32 32 LYS HB2 H 1 1.777 0.02 . 1 . . . . . . . . 5535 1 177 . 1 1 32 32 LYS HB3 H 1 1.953 0.02 . 1 . . . . . . . . 5535 1 178 . 1 1 32 32 LYS HG2 H 1 1.479 0.02 . 1 . . . . . . . . 5535 1 179 . 1 1 32 32 LYS HG3 H 1 1.479 0.02 . 1 . . . . . . . . 5535 1 180 . 1 1 32 32 LYS HD2 H 1 1.667 0.02 . 1 . . . . . . . . 5535 1 181 . 1 1 32 32 LYS HD3 H 1 1.667 0.02 . 1 . . . . . . . . 5535 1 182 . 1 1 32 32 LYS HE2 H 1 2.976 0.02 . 1 . . . . . . . . 5535 1 183 . 1 1 32 32 LYS HE3 H 1 2.976 0.02 . 1 . . . . . . . . 5535 1 184 . 1 1 33 33 LYS H H 1 7.961 0.02 . 1 . . . . . . . . 5535 1 185 . 1 1 33 33 LYS HA H 1 4.192 0.02 . 1 . . . . . . . . 5535 1 186 . 1 1 33 33 LYS HB2 H 1 1.911 0.02 . 1 . . . . . . . . 5535 1 187 . 1 1 33 33 LYS HB3 H 1 2.046 0.02 . 1 . . . . . . . . 5535 1 188 . 1 1 33 33 LYS HG2 H 1 1.58 0.02 . 2 . . . . . . . . 5535 1 189 . 1 1 33 33 LYS HG3 H 1 1.624 0.02 . 2 . . . . . . . . 5535 1 190 . 1 1 33 33 LYS HD2 H 1 1.816 0.02 . 1 . . . . . . . . 5535 1 191 . 1 1 33 33 LYS HD3 H 1 1.816 0.02 . 1 . . . . . . . . 5535 1 192 . 1 1 33 33 LYS HE2 H 1 3.073 0.02 . 1 . . . . . . . . 5535 1 193 . 1 1 33 33 LYS HE3 H 1 3.073 0.02 . 1 . . . . . . . . 5535 1 194 . 1 1 34 34 MET H H 1 8.69 0.02 . 1 . . . . . . . . 5535 1 195 . 1 1 34 34 MET HA H 1 4.749 0.02 . 1 . . . . . . . . 5535 1 196 . 1 1 34 34 MET HB2 H 1 2.028 0.02 . 1 . . . . . . . . 5535 1 197 . 1 1 34 34 MET HB3 H 1 2.184 0.02 . 1 . . . . . . . . 5535 1 198 . 1 1 34 34 MET HG2 H 1 2.466 0.02 . 2 . . . . . . . . 5535 1 199 . 1 1 34 34 MET HG3 H 1 2.736 0.02 . 2 . . . . . . . . 5535 1 200 . 1 1 34 34 MET HE1 H 1 1.947 0.02 . 1 . . . . . . . . 5535 1 201 . 1 1 34 34 MET HE2 H 1 1.947 0.02 . 1 . . . . . . . . 5535 1 202 . 1 1 34 34 MET HE3 H 1 1.947 0.02 . 1 . . . . . . . . 5535 1 203 . 1 1 35 35 GLN H H 1 7.798 0.02 . 1 . . . . . . . . 5535 1 204 . 1 1 35 35 GLN HA H 1 5.231 0.02 . 1 . . . . . . . . 5535 1 205 . 1 1 35 35 GLN HB2 H 1 1.876 0.02 . 1 . . . . . . . . 5535 1 206 . 1 1 35 35 GLN HB3 H 1 1.934 0.02 . 1 . . . . . . . . 5535 1 207 . 1 1 35 35 GLN HG2 H 1 2.172 0.02 . 2 . . . . . . . . 5535 1 208 . 1 1 35 35 GLN HG3 H 1 2.264 0.02 . 2 . . . . . . . . 5535 1 209 . 1 1 35 35 GLN HE21 H 1 7.582 0.02 . 1 . . . . . . . . 5535 1 210 . 1 1 35 35 GLN HE22 H 1 6.808 0.02 . 1 . . . . . . . . 5535 1 211 . 1 1 36 36 LEU H H 1 8.84 0.02 . 1 . . . . . . . . 5535 1 212 . 1 1 36 36 LEU HA H 1 4.182 0.02 . 1 . . . . . . . . 5535 1 213 . 1 1 36 36 LEU HB2 H 1 -0.061 0.02 . 1 . . . . . . . . 5535 1 214 . 1 1 36 36 LEU HB3 H 1 0.662 0.02 . 1 . . . . . . . . 5535 1 215 . 1 1 36 36 LEU HD11 H 1 0.196 0.02 . 1 . . . . . . . . 5535 1 216 . 1 1 36 36 LEU HD12 H 1 0.196 0.02 . 1 . . . . . . . . 5535 1 217 . 1 1 36 36 LEU HD13 H 1 0.196 0.02 . 1 . . . . . . . . 5535 1 218 . 1 1 36 36 LEU HD21 H 1 0.436 0.02 . 1 . . . . . . . . 5535 1 219 . 1 1 36 36 LEU HD22 H 1 0.436 0.02 . 1 . . . . . . . . 5535 1 220 . 1 1 36 36 LEU HD23 H 1 0.436 0.02 . 1 . . . . . . . . 5535 1 221 . 1 1 36 36 LEU HG H 1 0.603 0.02 . 1 . . . . . . . . 5535 1 222 . 1 1 37 37 GLU H H 1 8.459 0.02 . 1 . . . . . . . . 5535 1 223 . 1 1 37 37 GLU HA H 1 4.826 0.02 . 1 . . . . . . . . 5535 1 224 . 1 1 37 37 GLU HB2 H 1 1.759 0.02 . 1 . . . . . . . . 5535 1 225 . 1 1 37 37 GLU HB3 H 1 1.833 0.02 . 1 . . . . . . . . 5535 1 226 . 1 1 37 37 GLU HG2 H 1 2.176 0.02 . 2 . . . . . . . . 5535 1 227 . 1 1 37 37 GLU HG3 H 1 2.282 0.02 . 2 . . . . . . . . 5535 1 228 . 1 1 38 38 PHE H H 1 8.849 0.02 . 1 . . . . . . . . 5535 1 229 . 1 1 38 38 PHE HA H 1 4.424 0.02 . 1 . . . . . . . . 5535 1 230 . 1 1 38 38 PHE HB2 H 1 2.894 0.02 . 1 . . . . . . . . 5535 1 231 . 1 1 38 38 PHE HB3 H 1 3.233 0.02 . 1 . . . . . . . . 5535 1 232 . 1 1 38 38 PHE HD1 H 1 7.107 0.02 . 1 . . . . . . . . 5535 1 233 . 1 1 38 38 PHE HD2 H 1 7.107 0.02 . 1 . . . . . . . . 5535 1 234 . 1 1 38 38 PHE HE1 H 1 7.067 0.02 . 1 . . . . . . . . 5535 1 235 . 1 1 38 38 PHE HE2 H 1 7.067 0.02 . 1 . . . . . . . . 5535 1 236 . 1 1 38 38 PHE HZ H 1 6.859 0.02 . 1 . . . . . . . . 5535 1 237 . 1 1 39 39 PRO HA H 1 4.68 0.02 . 1 . . . . . . . . 5535 1 238 . 1 1 39 39 PRO HB2 H 1 2.033 0.02 . 1 . . . . . . . . 5535 1 239 . 1 1 39 39 PRO HB3 H 1 2.392 0.02 . 1 . . . . . . . . 5535 1 240 . 1 1 39 39 PRO HG2 H 1 1.908 0.02 . 1 . . . . . . . . 5535 1 241 . 1 1 39 39 PRO HG3 H 1 2.1 0.02 . 1 . . . . . . . . 5535 1 242 . 1 1 39 39 PRO HD2 H 1 3.761 0.02 . 1 . . . . . . . . 5535 1 243 . 1 1 39 39 PRO HD3 H 1 3.761 0.02 . 1 . . . . . . . . 5535 1 244 . 1 1 40 40 PRO HA H 1 3.759 0.02 . 1 . . . . . . . . 5535 1 245 . 1 1 40 40 PRO HB2 H 1 2.104 0.02 . 1 . . . . . . . . 5535 1 246 . 1 1 40 40 PRO HB3 H 1 2.392 0.02 . 1 . . . . . . . . 5535 1 247 . 1 1 40 40 PRO HG2 H 1 1.917 0.02 . 1 . . . . . . . . 5535 1 248 . 1 1 40 40 PRO HG3 H 1 2.032 0.02 . 1 . . . . . . . . 5535 1 249 . 1 1 40 40 PRO HD2 H 1 3.54 0.02 . 1 . . . . . . . . 5535 1 250 . 1 1 40 40 PRO HD3 H 1 3.736 0.02 . 1 . . . . . . . . 5535 1 251 . 1 1 41 41 SER H H 1 7.04 0.02 . 1 . . . . . . . . 5535 1 252 . 1 1 41 41 SER HA H 1 4.189 0.02 . 1 . . . . . . . . 5535 1 253 . 1 1 41 41 SER HB2 H 1 3.799 0.02 . 2 . . . . . . . . 5535 1 254 . 1 1 41 41 SER HB3 H 1 4.054 0.02 . 2 . . . . . . . . 5535 1 255 . 1 1 42 42 LEU H H 1 7.019 0.02 . 1 . . . . . . . . 5535 1 256 . 1 1 42 42 LEU HA H 1 4.42 0.02 . 1 . . . . . . . . 5535 1 257 . 1 1 42 42 LEU HB2 H 1 1.612 0.02 . 1 . . . . . . . . 5535 1 258 . 1 1 42 42 LEU HB3 H 1 1.68 0.02 . 1 . . . . . . . . 5535 1 259 . 1 1 42 42 LEU HD11 H 1 0.499 0.02 . 1 . . . . . . . . 5535 1 260 . 1 1 42 42 LEU HD12 H 1 0.499 0.02 . 1 . . . . . . . . 5535 1 261 . 1 1 42 42 LEU HD13 H 1 0.499 0.02 . 1 . . . . . . . . 5535 1 262 . 1 1 42 42 LEU HD21 H 1 1.03 0.02 . 1 . . . . . . . . 5535 1 263 . 1 1 42 42 LEU HD22 H 1 1.03 0.02 . 1 . . . . . . . . 5535 1 264 . 1 1 42 42 LEU HD23 H 1 1.03 0.02 . 1 . . . . . . . . 5535 1 265 . 1 1 42 42 LEU HG H 1 1.887 0.02 . 1 . . . . . . . . 5535 1 266 . 1 1 43 43 ASN H H 1 9.247 0.02 . 1 . . . . . . . . 5535 1 267 . 1 1 43 43 ASN HA H 1 4.756 0.02 . 1 . . . . . . . . 5535 1 268 . 1 1 43 43 ASN HB2 H 1 2.961 0.02 . 2 . . . . . . . . 5535 1 269 . 1 1 43 43 ASN HB3 H 1 3.355 0.02 . 2 . . . . . . . . 5535 1 270 . 1 1 43 43 ASN HD21 H 1 7.528 0.02 . 1 . . . . . . . . 5535 1 271 . 1 1 43 43 ASN HD22 H 1 7.027 0.02 . 1 . . . . . . . . 5535 1 272 . 1 1 44 44 SER H H 1 8.227 0.02 . 1 . . . . . . . . 5535 1 273 . 1 1 44 44 SER HA H 1 4.741 0.02 . 1 . . . . . . . . 5535 1 274 . 1 1 44 44 SER HB2 H 1 3.78 0.02 . 2 . . . . . . . . 5535 1 275 . 1 1 44 44 SER HB3 H 1 3.818 0.02 . 2 . . . . . . . . 5535 1 276 . 1 1 45 45 HIS H H 1 7.886 0.02 . 1 . . . . . . . . 5535 1 277 . 1 1 45 45 HIS HA H 1 4.25 0.02 . 1 . . . . . . . . 5535 1 278 . 1 1 45 45 HIS HB2 H 1 3.167 0.02 . 1 . . . . . . . . 5535 1 279 . 1 1 45 45 HIS HB3 H 1 3.167 0.02 . 1 . . . . . . . . 5535 1 280 . 1 1 45 45 HIS HD2 H 1 7.068 0.02 . 1 . . . . . . . . 5535 1 281 . 1 1 45 45 HIS HE1 H 1 7.882 0.02 . 1 . . . . . . . . 5535 1 282 . 1 1 46 46 ASP H H 1 8.547 0.02 . 1 . . . . . . . . 5535 1 283 . 1 1 46 46 ASP HA H 1 4.269 0.02 . 1 . . . . . . . . 5535 1 284 . 1 1 46 46 ASP HB2 H 1 2.435 0.02 . 1 . . . . . . . . 5535 1 285 . 1 1 46 46 ASP HB3 H 1 2.818 0.02 . 1 . . . . . . . . 5535 1 286 . 1 1 47 47 ARG H H 1 8.379 0.02 . 1 . . . . . . . . 5535 1 287 . 1 1 47 47 ARG HA H 1 3.323 0.02 . 1 . . . . . . . . 5535 1 288 . 1 1 47 47 ARG HB2 H 1 1.484 0.02 . 1 . . . . . . . . 5535 1 289 . 1 1 47 47 ARG HB3 H 1 1.833 0.02 . 1 . . . . . . . . 5535 1 290 . 1 1 47 47 ARG HG2 H 1 0.926 0.02 . 1 . . . . . . . . 5535 1 291 . 1 1 47 47 ARG HG3 H 1 1.37 0.02 . 1 . . . . . . . . 5535 1 292 . 1 1 47 47 ARG HD2 H 1 2.993 0.02 . 2 . . . . . . . . 5535 1 293 . 1 1 47 47 ARG HD3 H 1 3.253 0.02 . 2 . . . . . . . . 5535 1 294 . 1 1 48 48 LEU H H 1 7.564 0.02 . 1 . . . . . . . . 5535 1 295 . 1 1 48 48 LEU HA H 1 4.005 0.02 . 1 . . . . . . . . 5535 1 296 . 1 1 48 48 LEU HB2 H 1 1.62 0.02 . 1 . . . . . . . . 5535 1 297 . 1 1 48 48 LEU HB3 H 1 1.739 0.02 . 1 . . . . . . . . 5535 1 298 . 1 1 48 48 LEU HD11 H 1 0.811 0.02 . 2 . . . . . . . . 5535 1 299 . 1 1 48 48 LEU HD12 H 1 0.811 0.02 . 2 . . . . . . . . 5535 1 300 . 1 1 48 48 LEU HD13 H 1 0.811 0.02 . 2 . . . . . . . . 5535 1 301 . 1 1 48 48 LEU HD21 H 1 0.854 0.02 . 2 . . . . . . . . 5535 1 302 . 1 1 48 48 LEU HD22 H 1 0.854 0.02 . 2 . . . . . . . . 5535 1 303 . 1 1 48 48 LEU HD23 H 1 0.854 0.02 . 2 . . . . . . . . 5535 1 304 . 1 1 48 48 LEU HG H 1 1.612 0.02 . 1 . . . . . . . . 5535 1 305 . 1 1 49 49 ARG H H 1 7.52 0.02 . 1 . . . . . . . . 5535 1 306 . 1 1 49 49 ARG HA H 1 3.987 0.02 . 1 . . . . . . . . 5535 1 307 . 1 1 49 49 ARG HB2 H 1 1.826 0.02 . 1 . . . . . . . . 5535 1 308 . 1 1 49 49 ARG HB3 H 1 2.001 0.02 . 1 . . . . . . . . 5535 1 309 . 1 1 49 49 ARG HG2 H 1 1.655 0.02 . 2 . . . . . . . . 5535 1 310 . 1 1 49 49 ARG HG3 H 1 1.746 0.02 . 2 . . . . . . . . 5535 1 311 . 1 1 49 49 ARG HD2 H 1 3.206 0.02 . 2 . . . . . . . . 5535 1 312 . 1 1 49 49 ARG HD3 H 1 3.24 0.02 . 2 . . . . . . . . 5535 1 313 . 1 1 50 50 VAL H H 1 7.677 0.02 . 1 . . . . . . . . 5535 1 314 . 1 1 50 50 VAL HA H 1 2.93 0.02 . 1 . . . . . . . . 5535 1 315 . 1 1 50 50 VAL HB H 1 1.382 0.02 . 1 . . . . . . . . 5535 1 316 . 1 1 50 50 VAL HG11 H 1 -0.302 0.02 . 1 . . . . . . . . 5535 1 317 . 1 1 50 50 VAL HG12 H 1 -0.302 0.02 . 1 . . . . . . . . 5535 1 318 . 1 1 50 50 VAL HG13 H 1 -0.302 0.02 . 1 . . . . . . . . 5535 1 319 . 1 1 50 50 VAL HG21 H 1 -0.116 0.02 . 1 . . . . . . . . 5535 1 320 . 1 1 50 50 VAL HG22 H 1 -0.116 0.02 . 1 . . . . . . . . 5535 1 321 . 1 1 50 50 VAL HG23 H 1 -0.116 0.02 . 1 . . . . . . . . 5535 1 322 . 1 1 51 51 HIS H H 1 8.398 0.02 . 1 . . . . . . . . 5535 1 323 . 1 1 51 51 HIS HA H 1 3.486 0.02 . 1 . . . . . . . . 5535 1 324 . 1 1 51 51 HIS HB2 H 1 2.887 0.02 . 1 . . . . . . . . 5535 1 325 . 1 1 51 51 HIS HB3 H 1 3.223 0.02 . 1 . . . . . . . . 5535 1 326 . 1 1 51 51 HIS HD2 H 1 6.621 0.02 . 1 . . . . . . . . 5535 1 327 . 1 1 51 51 HIS HE1 H 1 7.689 0.02 . 1 . . . . . . . . 5535 1 328 . 1 1 52 52 GLN H H 1 7.792 0.02 . 1 . . . . . . . . 5535 1 329 . 1 1 52 52 GLN HA H 1 3.856 0.02 . 1 . . . . . . . . 5535 1 330 . 1 1 52 52 GLN HB2 H 1 2.033 0.02 . 1 . . . . . . . . 5535 1 331 . 1 1 52 52 GLN HB3 H 1 2.217 0.02 . 1 . . . . . . . . 5535 1 332 . 1 1 52 52 GLN HG2 H 1 2.285 0.02 . 1 . . . . . . . . 5535 1 333 . 1 1 52 52 GLN HG3 H 1 2.524 0.02 . 1 . . . . . . . . 5535 1 334 . 1 1 52 52 GLN HE21 H 1 7.467 0.02 . 1 . . . . . . . . 5535 1 335 . 1 1 52 52 GLN HE22 H 1 6.702 0.02 . 1 . . . . . . . . 5535 1 336 . 1 1 53 53 ILE H H 1 8.454 0.02 . 1 . . . . . . . . 5535 1 337 . 1 1 53 53 ILE HA H 1 3.802 0.02 . 1 . . . . . . . . 5535 1 338 . 1 1 53 53 ILE HB H 1 1.547 0.02 . 1 . . . . . . . . 5535 1 339 . 1 1 53 53 ILE HG21 H 1 0.953 0.02 . 1 . . . . . . . . 5535 1 340 . 1 1 53 53 ILE HG22 H 1 0.953 0.02 . 1 . . . . . . . . 5535 1 341 . 1 1 53 53 ILE HG23 H 1 0.953 0.02 . 1 . . . . . . . . 5535 1 342 . 1 1 53 53 ILE HG12 H 1 1.546 0.02 . 1 . . . . . . . . 5535 1 343 . 1 1 53 53 ILE HG13 H 1 1.902 0.02 . 1 . . . . . . . . 5535 1 344 . 1 1 53 53 ILE HD11 H 1 0.75 0.02 . 1 . . . . . . . . 5535 1 345 . 1 1 53 53 ILE HD12 H 1 0.75 0.02 . 1 . . . . . . . . 5535 1 346 . 1 1 53 53 ILE HD13 H 1 0.75 0.02 . 1 . . . . . . . . 5535 1 347 . 1 1 54 54 ALA H H 1 8.778 0.02 . 1 . . . . . . . . 5535 1 348 . 1 1 54 54 ALA HA H 1 3.925 0.02 . 1 . . . . . . . . 5535 1 349 . 1 1 54 54 ALA HB1 H 1 1.215 0.02 . 1 . . . . . . . . 5535 1 350 . 1 1 54 54 ALA HB2 H 1 1.215 0.02 . 1 . . . . . . . . 5535 1 351 . 1 1 54 54 ALA HB3 H 1 1.215 0.02 . 1 . . . . . . . . 5535 1 352 . 1 1 55 55 GLU H H 1 7.903 0.02 . 1 . . . . . . . . 5535 1 353 . 1 1 55 55 GLU HA H 1 4.151 0.02 . 1 . . . . . . . . 5535 1 354 . 1 1 55 55 GLU HB2 H 1 2.042 0.02 . 1 . . . . . . . . 5535 1 355 . 1 1 55 55 GLU HB3 H 1 2.153 0.02 . 1 . . . . . . . . 5535 1 356 . 1 1 55 55 GLU HG2 H 1 2.291 0.02 . 2 . . . . . . . . 5535 1 357 . 1 1 55 55 GLU HG3 H 1 2.45 0.02 . 2 . . . . . . . . 5535 1 358 . 1 1 56 56 GLU H H 1 8.01 0.02 . 1 . . . . . . . . 5535 1 359 . 1 1 56 56 GLU HA H 1 3.947 0.02 . 1 . . . . . . . . 5535 1 360 . 1 1 56 56 GLU HB2 H 1 2.012 0.02 . 1 . . . . . . . . 5535 1 361 . 1 1 56 56 GLU HB3 H 1 2.168 0.02 . 1 . . . . . . . . 5535 1 362 . 1 1 56 56 GLU HG2 H 1 1.928 0.02 . 2 . . . . . . . . 5535 1 363 . 1 1 56 56 GLU HG3 H 1 2.309 0.02 . 2 . . . . . . . . 5535 1 364 . 1 1 57 57 HIS H H 1 7.411 0.02 . 1 . . . . . . . . 5535 1 365 . 1 1 57 57 HIS HA H 1 4.454 0.02 . 1 . . . . . . . . 5535 1 366 . 1 1 57 57 HIS HB2 H 1 2.69 0.02 . 1 . . . . . . . . 5535 1 367 . 1 1 57 57 HIS HB3 H 1 3.664 0.02 . 1 . . . . . . . . 5535 1 368 . 1 1 57 57 HIS HD2 H 1 7.031 0.02 . 1 . . . . . . . . 5535 1 369 . 1 1 57 57 HIS HE1 H 1 7.552 0.02 . 1 . . . . . . . . 5535 1 370 . 1 1 58 58 GLY H H 1 8.009 0.02 . 1 . . . . . . . . 5535 1 371 . 1 1 58 58 GLY HA2 H 1 3.946 0.02 . 1 . . . . . . . . 5535 1 372 . 1 1 58 58 GLY HA3 H 1 3.984 0.02 . 1 . . . . . . . . 5535 1 373 . 1 1 59 59 LEU H H 1 8.028 0.02 . 1 . . . . . . . . 5535 1 374 . 1 1 59 59 LEU HA H 1 4.585 0.02 . 1 . . . . . . . . 5535 1 375 . 1 1 59 59 LEU HB2 H 1 1.611 0.02 . 1 . . . . . . . . 5535 1 376 . 1 1 59 59 LEU HB3 H 1 1.702 0.02 . 1 . . . . . . . . 5535 1 377 . 1 1 59 59 LEU HD11 H 1 0.945 0.02 . 1 . . . . . . . . 5535 1 378 . 1 1 59 59 LEU HD12 H 1 0.945 0.02 . 1 . . . . . . . . 5535 1 379 . 1 1 59 59 LEU HD13 H 1 0.945 0.02 . 1 . . . . . . . . 5535 1 380 . 1 1 59 59 LEU HD21 H 1 0.965 0.02 . 1 . . . . . . . . 5535 1 381 . 1 1 59 59 LEU HD22 H 1 0.965 0.02 . 1 . . . . . . . . 5535 1 382 . 1 1 59 59 LEU HD23 H 1 0.965 0.02 . 1 . . . . . . . . 5535 1 383 . 1 1 59 59 LEU HG H 1 1.698 0.02 . 1 . . . . . . . . 5535 1 384 . 1 1 60 60 ARG H H 1 8.672 0.02 . 1 . . . . . . . . 5535 1 385 . 1 1 60 60 ARG HA H 1 4.394 0.02 . 1 . . . . . . . . 5535 1 386 . 1 1 60 60 ARG HB2 H 1 1.665 0.02 . 1 . . . . . . . . 5535 1 387 . 1 1 60 60 ARG HB3 H 1 1.69 0.02 . 1 . . . . . . . . 5535 1 388 . 1 1 60 60 ARG HG2 H 1 1.551 0.02 . 2 . . . . . . . . 5535 1 389 . 1 1 60 60 ARG HG3 H 1 1.879 0.02 . 2 . . . . . . . . 5535 1 390 . 1 1 60 60 ARG HD2 H 1 3.012 0.02 . 2 . . . . . . . . 5535 1 391 . 1 1 60 60 ARG HD3 H 1 3.127 0.02 . 2 . . . . . . . . 5535 1 392 . 1 1 61 61 HIS H H 1 8.495 0.02 . 1 . . . . . . . . 5535 1 393 . 1 1 61 61 HIS HA H 1 5.235 0.02 . 1 . . . . . . . . 5535 1 394 . 1 1 61 61 HIS HB2 H 1 2.63 0.02 . 1 . . . . . . . . 5535 1 395 . 1 1 61 61 HIS HB3 H 1 2.777 0.02 . 1 . . . . . . . . 5535 1 396 . 1 1 61 61 HIS HD2 H 1 7.438 0.02 . 1 . . . . . . . . 5535 1 397 . 1 1 61 61 HIS HE1 H 1 8.186 0.02 . 1 . . . . . . . . 5535 1 398 . 1 1 62 62 ASP H H 1 8.205 0.02 . 1 . . . . . . . . 5535 1 399 . 1 1 62 62 ASP HA H 1 4.9 0.02 . 1 . . . . . . . . 5535 1 400 . 1 1 62 62 ASP HB2 H 1 2.359 0.02 . 1 . . . . . . . . 5535 1 401 . 1 1 62 62 ASP HB3 H 1 2.536 0.02 . 1 . . . . . . . . 5535 1 402 . 1 1 63 63 SER H H 1 8.993 0.02 . 1 . . . . . . . . 5535 1 403 . 1 1 63 63 SER HA H 1 5.171 0.02 . 1 . . . . . . . . 5535 1 404 . 1 1 63 63 SER HB2 H 1 3.411 0.02 . 1 . . . . . . . . 5535 1 405 . 1 1 63 63 SER HB3 H 1 3.714 0.02 . 1 . . . . . . . . 5535 1 406 . 1 1 64 64 SER H H 1 8.257 0.02 . 1 . . . . . . . . 5535 1 407 . 1 1 64 64 SER HA H 1 4.471 0.02 . 1 . . . . . . . . 5535 1 408 . 1 1 64 64 SER HB2 H 1 3.282 0.02 . 2 . . . . . . . . 5535 1 409 . 1 1 64 64 SER HB3 H 1 3.325 0.02 . 2 . . . . . . . . 5535 1 410 . 1 1 65 65 GLY H H 1 8.225 0.02 . 1 . . . . . . . . 5535 1 411 . 1 1 65 65 GLY HA2 H 1 3.708 0.02 . 2 . . . . . . . . 5535 1 412 . 1 1 65 65 GLY HA3 H 1 4.361 0.02 . 2 . . . . . . . . 5535 1 413 . 1 1 66 66 GLU H H 1 8.037 0.02 . 1 . . . . . . . . 5535 1 414 . 1 1 66 66 GLU HA H 1 4.643 0.02 . 1 . . . . . . . . 5535 1 415 . 1 1 66 66 GLU HB2 H 1 1.814 0.02 . 2 . . . . . . . . 5535 1 416 . 1 1 66 66 GLU HB3 H 1 1.961 0.02 . 2 . . . . . . . . 5535 1 417 . 1 1 66 66 GLU HG2 H 1 2.145 0.02 . 1 . . . . . . . . 5535 1 418 . 1 1 66 66 GLU HG3 H 1 2.145 0.02 . 1 . . . . . . . . 5535 1 419 . 1 1 67 67 GLY H H 1 8.911 0.02 . 1 . . . . . . . . 5535 1 420 . 1 1 67 67 GLY HA2 H 1 3.726 0.02 . 2 . . . . . . . . 5535 1 421 . 1 1 67 67 GLY HA3 H 1 3.9 0.02 . 2 . . . . . . . . 5535 1 422 . 1 1 68 68 LYS H H 1 7.962 0.02 . 1 . . . . . . . . 5535 1 423 . 1 1 68 68 LYS HA H 1 4.278 0.02 . 1 . . . . . . . . 5535 1 424 . 1 1 68 68 LYS HB2 H 1 1.641 0.02 . 1 . . . . . . . . 5535 1 425 . 1 1 68 68 LYS HB3 H 1 1.951 0.02 . 1 . . . . . . . . 5535 1 426 . 1 1 68 68 LYS HG2 H 1 1.377 0.02 . 1 . . . . . . . . 5535 1 427 . 1 1 68 68 LYS HG3 H 1 1.453 0.02 . 1 . . . . . . . . 5535 1 428 . 1 1 68 68 LYS HD2 H 1 1.605 0.02 . 1 . . . . . . . . 5535 1 429 . 1 1 68 68 LYS HD3 H 1 1.605 0.02 . 1 . . . . . . . . 5535 1 430 . 1 1 68 68 LYS HE2 H 1 2.932 0.02 . 1 . . . . . . . . 5535 1 431 . 1 1 68 68 LYS HE3 H 1 2.932 0.02 . 1 . . . . . . . . 5535 1 432 . 1 1 69 69 ARG H H 1 7.94 0.02 . 1 . . . . . . . . 5535 1 433 . 1 1 69 69 ARG HA H 1 4.36 0.02 . 1 . . . . . . . . 5535 1 434 . 1 1 69 69 ARG HB2 H 1 1.909 0.02 . 1 . . . . . . . . 5535 1 435 . 1 1 69 69 ARG HB3 H 1 2.08 0.02 . 1 . . . . . . . . 5535 1 436 . 1 1 69 69 ARG HG2 H 1 1.571 0.02 . 1 . . . . . . . . 5535 1 437 . 1 1 69 69 ARG HG3 H 1 1.658 0.02 . 1 . . . . . . . . 5535 1 438 . 1 1 69 69 ARG HD2 H 1 3.199 0.02 . 1 . . . . . . . . 5535 1 439 . 1 1 69 69 ARG HD3 H 1 3.199 0.02 . 1 . . . . . . . . 5535 1 440 . 1 1 70 70 ARG H H 1 7.251 0.02 . 1 . . . . . . . . 5535 1 441 . 1 1 70 70 ARG HA H 1 4.693 0.02 . 1 . . . . . . . . 5535 1 442 . 1 1 70 70 ARG HB2 H 1 1.178 0.02 . 2 . . . . . . . . 5535 1 443 . 1 1 70 70 ARG HB3 H 1 1.657 0.02 . 2 . . . . . . . . 5535 1 444 . 1 1 70 70 ARG HG2 H 1 1.04 0.02 . 1 . . . . . . . . 5535 1 445 . 1 1 70 70 ARG HG3 H 1 1.323 0.02 . 1 . . . . . . . . 5535 1 446 . 1 1 70 70 ARG HD2 H 1 2.993 0.02 . 2 . . . . . . . . 5535 1 447 . 1 1 70 70 ARG HD3 H 1 3.041 0.02 . 2 . . . . . . . . 5535 1 448 . 1 1 71 71 PHE H H 1 8.691 0.02 . 1 . . . . . . . . 5535 1 449 . 1 1 71 71 PHE HA H 1 5.104 0.02 . 1 . . . . . . . . 5535 1 450 . 1 1 71 71 PHE HB2 H 1 2.591 0.02 . 2 . . . . . . . . 5535 1 451 . 1 1 71 71 PHE HB3 H 1 3.343 0.02 . 2 . . . . . . . . 5535 1 452 . 1 1 71 71 PHE HD1 H 1 7.297 0.02 . 1 . . . . . . . . 5535 1 453 . 1 1 71 71 PHE HD2 H 1 7.297 0.02 . 1 . . . . . . . . 5535 1 454 . 1 1 71 71 PHE HE1 H 1 7.131 0.02 . 1 . . . . . . . . 5535 1 455 . 1 1 71 71 PHE HE2 H 1 7.131 0.02 . 1 . . . . . . . . 5535 1 456 . 1 1 71 71 PHE HZ H 1 7.104 0.02 . 1 . . . . . . . . 5535 1 457 . 1 1 72 72 ILE H H 1 8.566 0.02 . 1 . . . . . . . . 5535 1 458 . 1 1 72 72 ILE HA H 1 4.631 0.02 . 1 . . . . . . . . 5535 1 459 . 1 1 72 72 ILE HB H 1 1.279 0.02 . 1 . . . . . . . . 5535 1 460 . 1 1 72 72 ILE HG21 H 1 0.508 0.02 . 1 . . . . . . . . 5535 1 461 . 1 1 72 72 ILE HG22 H 1 0.508 0.02 . 1 . . . . . . . . 5535 1 462 . 1 1 72 72 ILE HG23 H 1 0.508 0.02 . 1 . . . . . . . . 5535 1 463 . 1 1 72 72 ILE HG12 H 1 0.558 0.02 . 1 . . . . . . . . 5535 1 464 . 1 1 72 72 ILE HG13 H 1 1.207 0.02 . 1 . . . . . . . . 5535 1 465 . 1 1 72 72 ILE HD11 H 1 -0.096 0.02 . 1 . . . . . . . . 5535 1 466 . 1 1 72 72 ILE HD12 H 1 -0.096 0.02 . 1 . . . . . . . . 5535 1 467 . 1 1 72 72 ILE HD13 H 1 -0.096 0.02 . 1 . . . . . . . . 5535 1 468 . 1 1 73 73 THR H H 1 8.348 0.02 . 1 . . . . . . . . 5535 1 469 . 1 1 73 73 THR HA H 1 5.096 0.02 . 1 . . . . . . . . 5535 1 470 . 1 1 73 73 THR HB H 1 3.811 0.02 . 1 . . . . . . . . 5535 1 471 . 1 1 73 73 THR HG21 H 1 1.009 0.02 . 1 . . . . . . . . 5535 1 472 . 1 1 73 73 THR HG22 H 1 1.009 0.02 . 1 . . . . . . . . 5535 1 473 . 1 1 73 73 THR HG23 H 1 1.009 0.02 . 1 . . . . . . . . 5535 1 474 . 1 1 74 74 VAL H H 1 9.19 0.02 . 1 . . . . . . . . 5535 1 475 . 1 1 74 74 VAL HA H 1 5.276 0.02 . 1 . . . . . . . . 5535 1 476 . 1 1 74 74 VAL HB H 1 1.932 0.02 . 1 . . . . . . . . 5535 1 477 . 1 1 74 74 VAL HG11 H 1 0.75 0.02 . 1 . . . . . . . . 5535 1 478 . 1 1 74 74 VAL HG12 H 1 0.75 0.02 . 1 . . . . . . . . 5535 1 479 . 1 1 74 74 VAL HG13 H 1 0.75 0.02 . 1 . . . . . . . . 5535 1 480 . 1 1 74 74 VAL HG21 H 1 0.893 0.02 . 1 . . . . . . . . 5535 1 481 . 1 1 74 74 VAL HG22 H 1 0.893 0.02 . 1 . . . . . . . . 5535 1 482 . 1 1 74 74 VAL HG23 H 1 0.893 0.02 . 1 . . . . . . . . 5535 1 483 . 1 1 75 75 SER H H 1 8.851 0.02 . 1 . . . . . . . . 5535 1 484 . 1 1 75 75 SER HA H 1 5.5 0.02 . 1 . . . . . . . . 5535 1 485 . 1 1 75 75 SER HB2 H 1 3.818 0.02 . 1 . . . . . . . . 5535 1 486 . 1 1 75 75 SER HB3 H 1 3.888 0.02 . 1 . . . . . . . . 5535 1 487 . 1 1 76 76 LYS H H 1 8.216 0.02 . 1 . . . . . . . . 5535 1 488 . 1 1 76 76 LYS HA H 1 4.472 0.02 . 1 . . . . . . . . 5535 1 489 . 1 1 76 76 LYS HB2 H 1 1.705 0.02 . 1 . . . . . . . . 5535 1 490 . 1 1 76 76 LYS HB3 H 1 1.946 0.02 . 1 . . . . . . . . 5535 1 491 . 1 1 76 76 LYS HG2 H 1 1.219 0.02 . 1 . . . . . . . . 5535 1 492 . 1 1 76 76 LYS HG3 H 1 1.311 0.02 . 1 . . . . . . . . 5535 1 493 . 1 1 77 77 ARG H H 1 8.995 0.02 . 1 . . . . . . . . 5535 1 494 . 1 1 77 77 ARG HA H 1 4.285 0.02 . 1 . . . . . . . . 5535 1 495 . 1 1 77 77 ARG HB2 H 1 1.715 0.02 . 1 . . . . . . . . 5535 1 496 . 1 1 77 77 ARG HB3 H 1 1.816 0.02 . 1 . . . . . . . . 5535 1 497 . 1 1 77 77 ARG HG2 H 1 1.578 0.02 . 1 . . . . . . . . 5535 1 498 . 1 1 77 77 ARG HG3 H 1 1.578 0.02 . 1 . . . . . . . . 5535 1 499 . 1 1 77 77 ARG HD2 H 1 3.145 0.02 . 1 . . . . . . . . 5535 1 500 . 1 1 77 77 ARG HD3 H 1 3.145 0.02 . 1 . . . . . . . . 5535 1 501 . 1 1 78 78 ALA H H 1 8.388 0.02 . 1 . . . . . . . . 5535 1 502 . 1 1 78 78 ALA HA H 1 4.266 0.02 . 1 . . . . . . . . 5535 1 503 . 1 1 78 78 ALA HB1 H 1 1.349 0.02 . 1 . . . . . . . . 5535 1 504 . 1 1 78 78 ALA HB2 H 1 1.349 0.02 . 1 . . . . . . . . 5535 1 505 . 1 1 78 78 ALA HB3 H 1 1.349 0.02 . 1 . . . . . . . . 5535 1 stop_ save_