data_4568 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4568 _Entry.Title ; Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2000-01-04 _Entry.Accession_date 2000-01-05 _Entry.Last_release_date 2000-05-25 _Entry.Original_release_date 2000-05-25 _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 David Eliezer . . . 4568 2 John Chung . . . 4568 3 Jane Dyson . . . 4568 4 Peter Wright . E. . 4568 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4568 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 286 4568 '13C chemical shifts' 429 4568 '15N chemical shifts' 149 4568 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 . . 2000-05-25 2000-01-04 original author . 4568 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4568 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin ; _Citation.Status submitted _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full Biochemistry _Citation.Journal_volume . _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 . _Citation.Page_last . _Citation.Year . _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 David Eliezer . . . 4568 1 2 John Chung . . . 4568 1 3 Jane Dyson . . . 4568 1 4 Peter Wright . E. . 4568 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'equilibrium folding intermediate' 4568 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 4568 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 98120979 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _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 . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 4568 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 98055460 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _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 . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 4568 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 96026357 _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _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 . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_apoMb _Assembly.Sf_category assembly _Assembly.Sf_framecode system_apoMb _Assembly.Entry_ID 4568 _Assembly.ID 1 _Assembly.Name apomyoglobin _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 4568 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 apoMb 1 $apoMb . . . 'molten globule' . . . . . 4568 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID apomyoglobin system 4568 1 apoMb abbreviation 4568 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'oxygen storage' 4568 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_apoMb _Entity.Sf_category entity _Entity.Sf_framecode apoMb _Entity.Entry_ID 4568 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name myoglobin _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 ; VLSEGEWQLVLHVWAKVEAD VAGHGQDILIRLFKSHPETL EKFDRFKHLKTEAEMKASED LKKHGVTVLTALGAILKKKG HHEAELKPLAQSHATKHKIP IKYLEFISEAIIHVLHSRHP GDFGADAQGAMNKALELFRK DIAAKYKELGYQG ; _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 153 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not present' _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 BMRB 1027 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 2 no BMRB 1029 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 3 no BMRB 1200 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 4 no BMRB 1413 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 5 no BMRB 1455 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 6 no BMRB 1457 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 7 no BMRB 1459 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 8 no BMRB 1461 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 9 no BMRB 1463 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 10 no BMRB 1465 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 11 no BMRB 1467 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 12 no BMRB 1469 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 13 no BMRB 1471 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 14 no BMRB 15589 . Apomyoglobin_(1-77) . . . . . 50.33 77 100.00 100.00 8.13e-45 . . . . 4568 1 15 no BMRB 16217 . apomyoglobin . . . . . 77.78 119 100.00 100.00 3.15e-76 . . . . 4568 1 16 no BMRB 16218 . apoMb_1-119_fragment . . . . . 77.78 119 100.00 100.00 3.15e-76 . . . . 4568 1 17 no BMRB 16499 . 1-77_Apomyoglobin . . . . . 50.33 78 100.00 100.00 6.66e-45 . . . . 4568 1 18 no BMRB 16500 . (1-119)Apomyoglobin . . . . . 77.78 120 100.00 100.00 2.86e-76 . . . . 4568 1 19 no BMRB 16501 . (1-153)Apomyoglobin . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 20 no BMRB 1752 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 21 no BMRB 2345 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 22 no BMRB 2346 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 23 no BMRB 2347 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 24 no BMRB 2348 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 25 no BMRB 2431 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 26 no BMRB 2432 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 27 no BMRB 2433 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 28 no BMRB 2434 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 29 no BMRB 291 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 30 no BMRB 292 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 31 no BMRB 293 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 32 no BMRB 40 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 33 no BMRB 4061 . apomyoglobin . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 34 no BMRB 4062 . apomyoglobin . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 35 no BMRB 426 . myoglobin . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 36 no BMRB 4676 . "unfolded myoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 37 no BMRB 4695 . myoglobin . . . . . 100.00 153 99.35 99.35 3.18e-102 . . . . 4568 1 38 no PDB 101M . "Sperm Whale Myoglobin F46v N-Butyl Isocyanide At Ph 9.0" . . . . . 100.00 154 98.69 99.35 4.67e-102 . . . . 4568 1 39 no PDB 102M . "Sperm Whale Myoglobin H64a Aquomet At Ph 9.0" . . . . . 100.00 154 98.69 99.35 7.98e-102 . . . . 4568 1 40 no PDB 103M . "Sperm Whale Myoglobin H64a N-Butyl Isocyanide At Ph 9.0" . . . . . 100.00 154 98.69 99.35 7.98e-102 . . . . 4568 1 41 no PDB 104M . "Sperm Whale Myoglobin N-Butyl Isocyanide At Ph 7.0" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 42 no PDB 105M . "Sperm Whale Myoglobin N-Butyl Isocyanide At Ph 9.0" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 43 no PDB 106M . "Sperm Whale Myoglobin V68f Ethyl Isocyanide At Ph 9.0" . . . . . 100.00 154 98.69 99.35 3.02e-102 . . . . 4568 1 44 no PDB 107M . "Sperm Whale Myoglobin V68f N-Butyl Isocyanide At Ph 9.0" . . . . . 100.00 154 98.69 99.35 3.02e-102 . . . . 4568 1 45 no PDB 108M . "Sperm Whale Myoglobin V68f N-Butyl Isocyanide At Ph 7.0" . . . . . 100.00 154 98.69 99.35 3.02e-102 . . . . 4568 1 46 no PDB 109M . "Sperm Whale Myoglobin D122n Ethyl Isocyanide At Ph 9.0" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 47 no PDB 110M . "Sperm Whale Myoglobin D122n Methyl Isocyanide At Ph 9.0" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 48 no PDB 111M . "Sperm Whale Myoglobin D122n N-Butyl Isocyanide At Ph 9.0" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 49 no PDB 112M . "Sperm Whale Myoglobin D122n N-Propyl Isocyanide At Ph 9.0" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 50 no PDB 1A6G . "Carbonmonoxy-Myoglobin, Atomic Resolution" . . . . . 98.69 151 99.34 100.00 2.67e-101 . . . . 4568 1 51 no PDB 1A6K . "Aquomet-Myoglobin, Atomic Resolution" . . . . . 98.69 151 100.00 100.00 8.87e-102 . . . . 4568 1 52 no PDB 1A6M . "Oxy-Myoglobin, Atomic Resolution" . . . . . 98.69 151 100.00 100.00 8.87e-102 . . . . 4568 1 53 no PDB 1A6N . "Deoxy-Myoglobin, Atomic Resolution" . . . . . 98.69 151 100.00 100.00 8.87e-102 . . . . 4568 1 54 no PDB 1ABS . "Photolysed Carbonmonoxy-Myoglobin At 20 K" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 55 no PDB 1AJG . "Carbonmonoxy Myoglobin At 40 K" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 56 no PDB 1AJH . "Photoproduct Of Carbonmonoxy Myoglobin At 40 K" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 57 no PDB 1BVC . "Structure Of A Biliverdin Apomyoglobin Complex (Form D) At 118 K" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 58 no PDB 1BVD . "Structure Of A Biliverdin Apomyoglobin Complex (Form B) At 98 K" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 59 no PDB 1BZ6 . "Atomic Resolution Crystal Structure Aquomet-Myoglobin From Sperm Whale At Room Temperature" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 60 no PDB 1BZP . "Atomic Resolution Crystal Structure Analysis Of Native Deoxy And Co Myoglobin From Sperm Whale At Room Temperature" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 61 no PDB 1BZR . "Atomic Resolution Crystal Structure Analysis Of Native Deoxy And Co Myoglobin From Sperm Whale At Room Temperature" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 62 no PDB 1CH1 . "Recombinant Sperm Whale Myoglobin L89g Mutatnt (Met)" . . . . . 100.00 154 98.69 99.35 9.29e-102 . . . . 4568 1 63 no PDB 1CH2 . "Recombinant Sperm Whale Myoglobin L89f Mutant (Met)" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 64 no PDB 1CH3 . "Recombinant Sperm Whale Myoglobin L89w Mutant (Met)" . . . . . 100.00 154 98.69 99.35 5.81e-102 . . . . 4568 1 65 no PDB 1CH5 . "Recombinant Sperm Whale Myoglobin H97v Mutant (Met)" . . . . . 100.00 154 98.69 99.35 9.71e-102 . . . . 4568 1 66 no PDB 1CH7 . "Recombinant Sperm Whale Myoglobin H97f Mutant (Met)" . . . . . 100.00 154 98.69 99.35 6.48e-102 . . . . 4568 1 67 no PDB 1CH9 . "Recombinant Sperm Whale Myoglobin H97q Mutant (Met)" . . . . . 100.00 154 98.69 99.35 3.19e-102 . . . . 4568 1 68 no PDB 1CIK . "Recombinant Sperm Whale Myoglobin I99a Mutant (Met)" . . . . . 100.00 154 98.69 99.35 2.89e-102 . . . . 4568 1 69 no PDB 1CIO . "Recombinant Sperm Whale Myoglobin I99v Mutant (Met)" . . . . . 100.00 154 98.69 100.00 7.13e-103 . . . . 4568 1 70 no PDB 1CO8 . "Recombinant Sperm Whale Myoglobin L104a Mutant (Met)" . . . . . 100.00 154 98.69 99.35 2.70e-102 . . . . 4568 1 71 no PDB 1CO9 . "Recombinant Sperm Whale Myoglobin L104v Mutant (Met)" . . . . . 100.00 154 98.69 100.00 1.33e-102 . . . . 4568 1 72 no PDB 1CP0 . "Recombinant Sperm Whale Myoglobin L104n Mutant (Met)" . . . . . 100.00 154 98.69 99.35 3.55e-102 . . . . 4568 1 73 no PDB 1CP5 . "Recombinant Sperm Whale Myoglobin L104f Mutant (Met)" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 74 no PDB 1CPW . "Recombinant Sperm Whale Myoglobin L104w Mutant (Met)" . . . . . 100.00 154 98.69 99.35 5.81e-102 . . . . 4568 1 75 no PDB 1CQ2 . "Neutron Struture Of Fully Deuterated Sperm Whale Myoglobin At 2.0 Angstrom" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 76 no PDB 1DO1 . "Carbonmonoxy-Myoglobin Mutant L29w At 105k" . . . . . 100.00 154 98.69 99.35 6.48e-102 . . . . 4568 1 77 no PDB 1DO3 . "Carbonmonoxy-Myoglobin (Mutant L29w) After Photolysis At T>180k" . . . . . 100.00 154 98.69 99.35 6.48e-102 . . . . 4568 1 78 no PDB 1DO4 . "Carbonmonoxy-Myoglobin (Mutant L29w) After Photolysis At T<180k" . . . . . 100.00 154 98.69 99.35 6.48e-102 . . . . 4568 1 79 no PDB 1DO7 . "Carbonmonoxy-Myoglobin (Mutant L29w) Rebinding Structure After Photolysis At T< 180k" . . . . . 100.00 154 98.69 99.35 6.48e-102 . . . . 4568 1 80 no PDB 1DTI . "Recombinant Sperm Whale Myoglobin H97d, D122n Mutant (Met)" . . . . . 100.00 154 98.69 99.35 7.31e-102 . . . . 4568 1 81 no PDB 1DTM . "Crystal Structure Of The Sperm-Whale Myoglobin Mutant H93g Complexed With 4-Methylimidazole, Metaquo Form" . . . . . 100.00 153 99.35 99.35 4.23e-102 . . . . 4568 1 82 no PDB 1DUK . "Wild-Type Recombinant Sperm Whale Metaquomyoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 83 no PDB 1DUO . "Sperm Whale Metaquomyoglobin Proximal Histidine Mutant H93g With 1-Methylimidazole As Proximal Ligand." . . . . . 100.00 153 99.35 99.35 4.23e-102 . . . . 4568 1 84 no PDB 1DXC . "Co Complex Of Myoglobin Mb-Yqr At 100k" . . . . . 100.00 154 97.39 98.04 1.17e-100 . . . . 4568 1 85 no PDB 1DXD . "Photolyzed Co Complex Of Myoglobin Mb-Yqr At 20k" . . . . . 100.00 154 97.39 98.04 1.17e-100 . . . . 4568 1 86 no PDB 1EBC . "Sperm Whale Met-Myoglobin:cyanide Complex" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 87 no PDB 1F63 . "Crystal Structure Of Deoxy Sperm Whale Myoglobin Mutant Y(B10)q(E7)r(E10)" . . . . . 100.00 154 97.39 98.04 1.17e-100 . . . . 4568 1 88 no PDB 1F65 . "Crystal Structure Of Oxy Sperm Whale Myoglobin Mutant Y(B10)q(E7)r(E10)" . . . . . 100.00 154 97.39 98.04 1.17e-100 . . . . 4568 1 89 no PDB 1F6H . "Combined Rietveld And Stereochemical Restraint Refinement Of A Protein" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 90 no PDB 1FCS . "Crystal Structure Of A Distal Site Double Mutant Of Sperm Whale Myoglobin At 1.6 Angstroms Resolution" . . . . . 100.00 154 98.04 98.69 1.04e-100 . . . . 4568 1 91 no PDB 1H1X . "Sperm Whale Myoglobin Mutant T67r S92d" . . . . . 100.00 154 98.04 98.69 2.89e-101 . . . . 4568 1 92 no PDB 1HJT . "Sperm Whale Myoglobin (Ferrous, Nitric Oxide Bound)" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 93 no PDB 1IOP . "Incorporation Of A Hemin With The Shortest Acid Side-Chains Into Myoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 94 no PDB 1IRC . "Cysteine Rich Intestinal Protein" . . . . . 100.00 154 99.35 99.35 3.55e-102 . . . . 4568 1 95 no PDB 1J3F . "Crystal Structure Of An Artificial Metalloprotein:cr(iii)(3, 3'-me2-salophen)/apo-a71g Myoglobin" . . . . . 100.00 154 99.35 99.35 8.49e-103 . . . . 4568 1 96 no PDB 1J52 . "Recombinant Sperm Whale Myoglobin In The Presence Of 7atm Xenon" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 97 no PDB 1JDO . "Sperm Whale Myoglobin (Ferrous, Nitric Oxide Bound)" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 98 no PDB 1JP6 . "Sperm Whale Met-Myoglobin (Room Temperature; Room Pressure)" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 99 no PDB 1JP8 . "Sperm Whale Met-Myoglobin (Room Temperature; High Pressure)" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 100 no PDB 1JP9 . "Sperm Whale Met-Myoglobin (Low Temperature; High Pressure)" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 101 no PDB 1JPB . "Sperm Whale Met-Myoglobin (Low Temperature; High Pressure)" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 102 no PDB 1JW8 . "1.3 Angstrom Resolution Crystal Structure Of P6 Form Of Myoglobin" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 103 no PDB 1L2K . "Neutron Structure Determination Of Sperm Whale Met-Myoglobin At 1.5a Resolution." . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 104 no PDB 1LTW . "Recombinant Sperm Whale Myoglobin 29w Mutant (oxy)" . . . . . 100.00 154 98.69 99.35 5.81e-102 . . . . 4568 1 105 no PDB 1LUE . "Recombinant Sperm Whale Myoglobin H64d/v68a/d122n Mutant (met)" . . . . . 100.00 154 98.04 98.69 2.54e-101 . . . . 4568 1 106 no PDB 1MBC . "X-Ray Structure And Refinement Of Carbon-Monoxy (Fe Ii)- Myoglobin At 1.5 Angstroms Resolution" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 107 no PDB 1MBD . "Neutron Diffraction Reveals Oxygen-Histidine Hydrogen Bond In Oxymyoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 108 no PDB 1MBI . "X-Ray Crystal Structure Of The Ferric Sperm Whale Myoglobin: Imidazole Complex At 2.0 Angstroms Resolution" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 109 no PDB 1MBN . "The Stereochemistry Of The Protein Myoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 110 no PDB 1MBO . "Structure And Refinement Of Oxymyoglobin At 1.6 Angstroms Resolution" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 111 no PDB 1MCY . "Sperm Whale Myoglobin (Mutant With Initiator Met And With His 64 Replaced By Gln, Leu 29 Replaced By Phe" . . . . . 100.00 154 98.69 98.69 3.71e-102 . . . . 4568 1 112 no PDB 1MGN . "His64(E7)-> Tyr Apomyoglobin As A Reagent For Measuring Rates Of Hemin Dissociation" . . . . . 100.00 154 98.69 100.00 2.32e-102 . . . . 4568 1 113 no PDB 1MLF . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 98.69 99.35 1.93e-102 . . . . 4568 1 114 no PDB 1MLG . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 98.69 99.35 1.93e-102 . . . . 4568 1 115 no PDB 1MLH . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 98.69 99.35 1.93e-102 . . . . 4568 1 116 no PDB 1MLJ . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 98.69 99.35 3.02e-102 . . . . 4568 1 117 no PDB 1MLK . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 98.69 99.35 3.02e-102 . . . . 4568 1 118 no PDB 1MLL . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 98.69 99.35 3.02e-102 . . . . 4568 1 119 no PDB 1MLM . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 98.69 100.00 8.68e-103 . . . . 4568 1 120 no PDB 1MLN . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 98.69 100.00 8.68e-103 . . . . 4568 1 121 no PDB 1MLO . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 98.69 100.00 8.68e-103 . . . . 4568 1 122 no PDB 1MLQ . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 98.69 100.00 1.93e-102 . . . . 4568 1 123 no PDB 1MLR . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 98.69 100.00 1.93e-102 . . . . 4568 1 124 no PDB 1MLS . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 98.69 100.00 1.93e-102 . . . . 4568 1 125 no PDB 1MLU . "Nitric Oxide Recombination To Double Mutants Of Myoglobin: The Role Of Ligand Diffusion In A Fluctuating Heme Pocket" . . . . . 100.00 154 98.04 98.69 4.24e-101 . . . . 4568 1 126 no PDB 1MOA . "A Novel Site-Directed Mutant Of Myoglobin With An Unusually High O2 Affinity And Low Autooxidation Rate" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 127 no PDB 1MOB . "High-Resolution Crystal Structures Of Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 1.03e-101 . . . . 4568 1 128 no PDB 1MOC . "High-Resolution Crystal Structures Of Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 6.55e-102 . . . . 4568 1 129 no PDB 1MOD . "High-Resolution Crystal Structures Of Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 6.55e-102 . . . . 4568 1 130 no PDB 1MTI . "Phe46(Cd4) Orients The Distal Histidine For Hydrogen Bonding To Bound Ligands In Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 3.59e-102 . . . . 4568 1 131 no PDB 1MTJ . "Phe46(Cd4) Orients The Distal Histidine For Hydrogen Bonding To Bound Ligands In Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 4.67e-102 . . . . 4568 1 132 no PDB 1MTK . "Phe46(cd4) Orients The Distal Histidine For Hydrogen Bonding To Bound Ligands In Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 4.67e-102 . . . . 4568 1 133 no PDB 1MYF . "Solution Structure Of Carbonmonoxy Myoglobin Determined From Nmr Distance And Chemical Shift Constraints" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 134 no PDB 1MYM . "Structural Determinants Of Co Stretching Vibration Frequencies In Myoglobin" . . . . . 100.00 154 98.69 99.35 4.67e-102 . . . . 4568 1 135 no PDB 1MYZ . "Co Complex Of Myoglobin Mb-yqr At Rt Solved From Laue Data." . . . . . 100.00 154 97.39 98.04 1.17e-100 . . . . 4568 1 136 no PDB 1MZ0 . "Structure Of Myoglobin Mb-yqr 316 Ns After Photolysis Of Carbon Monoxide Solved From Laue Data At Rt" . . . . . 100.00 154 97.39 98.04 1.17e-100 . . . . 4568 1 137 no PDB 1N9F . "Structure Of Earth-Grown Oxidized Myoglobin Mutant Yqr (Iss6a)" . . . . . 100.00 154 97.39 98.04 1.17e-100 . . . . 4568 1 138 no PDB 1N9H . "Structure Of Microgravity-Grown Oxidized Myoglobin Mutant Yqr (Iss6a)" . . . . . 100.00 154 97.39 98.04 1.17e-100 . . . . 4568 1 139 no PDB 1N9I . "Structure Of Earth-Grown Oxidized Myoglobin Mutant Yqr (Iss8a)" . . . . . 100.00 154 97.39 98.04 1.17e-100 . . . . 4568 1 140 no PDB 1N9X . "Structure Of Microgravity-Grown Oxidized Myoglobin Mutant Yqr (Iss8a)" . . . . . 100.00 154 97.39 98.04 1.17e-100 . . . . 4568 1 141 no PDB 1NAZ . "Structure Of Microgravity-Grown Oxidized Myoglobin Mutant Yqr (Iss8a)" . . . . . 100.00 154 97.39 98.04 1.17e-100 . . . . 4568 1 142 no PDB 1O16 . "Recombinant Sperm Whale Myoglobin H64dV68SD122N MUTANT (Met)" . . . . . 100.00 154 98.04 98.69 3.49e-101 . . . . 4568 1 143 no PDB 1OBM . "Recombinant Sperm Whale Myoglobin 29f64Q68F122N MUTANT (Met)" . . . . . 100.00 154 97.39 98.04 7.41e-101 . . . . 4568 1 144 no PDB 1OFJ . "Recombinant Sperm Whale Myoglobin L29hH64LD122N MUTANT (With Initiator Met)" . . . . . 100.00 154 98.04 98.69 2.78e-100 . . . . 4568 1 145 no PDB 1OFK . "Recombinant Sperm Whale Myoglobin F43h, H64l Mutant (Met)" . . . . . 100.00 154 98.04 98.69 2.97e-100 . . . . 4568 1 146 no PDB 1SPE . "Sperm Whale Native Co Myoglobin At Ph 4.0, Temp 4c" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 147 no PDB 1SWM . "X-Ray Crystal Structure Of The Ferric Sperm Whale Myoglobin: Imidazole Complex At 2.0 Angstroms Resolution" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 148 no PDB 1TES . "Oxygen Binding Muscle Protein" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 149 no PDB 1U7R . "Crystal Structure Of Native Sperm Whale Myoglobin From Low Ionic Strength Enviroment (form2 )" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 150 no PDB 1U7S . "Crystal Structure Of Native Sperm Whale Myoglobin From Low Ionic Strength Enviroment (form 1)" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 151 no PDB 1UFJ . "Crystal Structure Of An Artificial Metalloprotein:fe(Iii)(3, 3'-Me2-Salophen)APO-A71g Myoglobin" . . . . . 100.00 154 99.35 99.35 8.49e-103 . . . . 4568 1 152 no PDB 1UFP . "Crystal Structure Of An Artificial Metalloprotein:fe(Iii)(3, 3'-Me2-Salophen)APO-Wild Type Myoglobin" . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 153 no PDB 1V9Q . "Crystal Structure Of An Artificial Metalloprotein:mn(iii)(3, 3'-me2-salophen)/apo-a71g Myoglobin" . . . . . 100.00 154 99.35 99.35 8.49e-103 . . . . 4568 1 154 no PDB 1VXA . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 155 no PDB 1VXB . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 156 no PDB 1VXC . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 157 no PDB 1VXD . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 158 no PDB 1VXE . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 159 no PDB 1VXF . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 160 no PDB 1VXG . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 161 no PDB 1VXH . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 162 no PDB 1WVP . "Structure Of Chemically Modified Myoglobin With Distal N- Tetrazolyl-Histidine E7(64)" . . . . . 100.00 153 99.35 99.35 2.53e-102 . . . . 4568 1 163 no PDB 1YOG . "Cobalt Myoglobin (Deoxy)" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 164 no PDB 1YOH . "Cobalt Myoglobin (Met)" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 165 no PDB 1YOI . "Cobalt Myoglobin (Oxy)" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 166 no PDB 2BLH . "Ligand Migration And Protein Fluctuations In Myoglobin Mutant L29w" . . . . . 100.00 153 98.69 99.35 6.27e-102 . . . . 4568 1 167 no PDB 2BLI . "L29w Mb Deoxy" . . . . . 100.00 153 98.69 99.35 6.27e-102 . . . . 4568 1 168 no PDB 2BLJ . "Structure Of L29w Mbco" . . . . . 100.00 153 98.69 99.35 6.27e-102 . . . . 4568 1 169 no PDB 2BW9 . "Laue Structure Of L29w Mbco" . . . . . 100.00 153 98.69 99.35 6.27e-102 . . . . 4568 1 170 no PDB 2BWH . "Laue Structure Of A Short Lived State Of L29w Myoglobin" . . . . . 100.00 153 98.69 99.35 6.27e-102 . . . . 4568 1 171 no PDB 2CMM . "Structural Analysis Of The Myoglobin Reconstituted With Iron Porphine" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 172 no PDB 2D6C . "Crystal Structure Of Myoglobin Reconstituted With Iron Porphycene" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 173 no PDB 2E2Y . "Crystal Structure Of F43wH64DV68I MYOGLOBIN" . . . . . 100.00 154 97.39 99.35 1.17e-100 . . . . 4568 1 174 no PDB 2EB8 . "Crystal Structure Of Cu(Ii)(Sal-Phe)APO-Myoglobin" . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 175 no PDB 2EB9 . "Crystal Structure Of Cu(ii)(sal-leu)/apo-myoglobin" . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 176 no PDB 2EF2 . "Crystal Structure Of An Artificial Metalloprotein:rh(Phebox- Ph)APO-A71g Myoglobin" . . . . . 100.00 154 99.35 99.35 8.49e-103 . . . . 4568 1 177 no PDB 2EKT . "Crystal Structure Of Myoglobin Reconstituted With 6-Methyl-6- Depropionatehemin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 178 no PDB 2EKU . "Crystal Structure Of Myoglobin Reconstituted With 7-Methyl-7- Depropionatehemin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 179 no PDB 2EVK . "The Structures Of Thiolate- And Carboxylate-Ligated Ferric H93g Myoglobin: Models For Cytochrome P450 And For Oxyanion-Bound He" . . . . . 100.00 153 99.35 99.35 4.23e-102 . . . . 4568 1 180 no PDB 2EVP . "The Structures Of Thiolate- And Carboxylate-Ligated Ferric H93g Myoglobin: Models For Cytochrome P450 And For Oxyanion-Bound He" . . . . . 100.00 153 99.35 99.35 4.23e-102 . . . . 4568 1 181 no PDB 2G0R . "Unphotolyzed Co-bound L29f Myoglobin" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 182 no PDB 2G0S . "Unphotolyzed Co-bound L29f Myoglobin, Crystal 2" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 183 no PDB 2G0V . "Photolyzed Co L29f Myoglobin: 100ps" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 184 no PDB 2G0X . "Photolyzed Co L29f Myoglobin: 316ps" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 185 no PDB 2G0Z . "Photolyzed Co L29f Myoglobin: 1ns" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 186 no PDB 2G10 . "Photolyzed Co L29f Myoglobin: 3.16ns" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 187 no PDB 2G11 . "Photolyzed Co L29f Myoglobin: 31.6ns" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 188 no PDB 2G12 . "Photolyzed Co L29f Myoglobin: 316ns" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 189 no PDB 2G14 . "Photolyzed Co L29f Myoglobin: 3.16us" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 190 no PDB 2JHO . "Cyanomet Sperm Whale Myoglobin At 1.4a Resolution" . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 191 no PDB 2MB5 . "Hydration In Protein Crystals. A Neutron Diffraction Analysis Of Carbonmonoxymyoglobin" . . . . . 99.35 153 100.00 100.00 9.57e-103 . . . . 4568 1 192 no PDB 2MBW . "Recombinant Sperm Whale Myoglobin (Met)" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 193 no PDB 2MGA . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 1.03e-101 . . . . 4568 1 194 no PDB 2MGB . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 1.03e-101 . . . . 4568 1 195 no PDB 2MGC . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 1.17e-101 . . . . 4568 1 196 no PDB 2MGD . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 1.17e-101 . . . . 4568 1 197 no PDB 2MGE . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 1.17e-101 . . . . 4568 1 198 no PDB 2MGF . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 3.19e-102 . . . . 4568 1 199 no PDB 2MGG . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 3.19e-102 . . . . 4568 1 200 no PDB 2MGH . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 3.19e-102 . . . . 4568 1 201 no PDB 2MGI . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 6.55e-102 . . . . 4568 1 202 no PDB 2MGJ . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.69 99.35 9.71e-102 . . . . 4568 1 203 no PDB 2MGK . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 204 no PDB 2MGL . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 205 no PDB 2MGM . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 206 no PDB 2MYA . "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 207 no PDB 2MYB . "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 208 no PDB 2MYC . "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 209 no PDB 2MYD . "High Resolution X-ray Structures Of Myoglobin-and Hemoglobin-alkyl Isocyanide Complexes" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 210 no PDB 2MYE . "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 211 no PDB 2OH8 . "Myoglobin Cavity Mutant I28w" . . . . . 100.00 154 98.69 99.35 9.82e-102 . . . . 4568 1 212 no PDB 2OH9 . "Myoglobin Cavity Mutant V68w" . . . . . 100.00 154 98.69 99.35 1.14e-101 . . . . 4568 1 213 no PDB 2OHA . "Myoglobin Cavity Mutant F138w" . . . . . 100.00 154 98.69 100.00 4.57e-102 . . . . 4568 1 214 no PDB 2OHB . "Myoglobin Cavity Mutant I107w" . . . . . 100.00 154 98.69 99.35 9.82e-102 . . . . 4568 1 215 no PDB 2SPL . "A Novel Site-Directed Mutant Of Myoglobin With An Unusually High O2 Affinity And Low Autooxidation Rate" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 216 no PDB 2SPM . "A Novel Site-Directed Mutant Of Myoglobin With An Unusually High O2 Affinity And Low Autooxidation Rate" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 217 no PDB 2SPN . "A Novel Site-Directed Mutant Of Myoglobin With An Unusually High O2 Affinity And Low Autooxidation Rate" . . . . . 100.00 154 98.69 99.35 1.77e-102 . . . . 4568 1 218 no PDB 2SPO . "A Novel Site-directed Mutant Of Myoglobin With An Unusually High O2 Affinity And Low Autooxidation Rate" . . . . . 100.00 154 98.69 100.00 1.33e-102 . . . . 4568 1 219 no PDB 2W6W . "Crystal Structure Of Recombinant Sperm Whale Myoglobin Under 1atm Of Xenon" . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 220 no PDB 2W6X . "Crystal Structure Of Sperm Whale Myoglobin Mutant Yqrf In Complex With Xenon" . . . . . 100.00 154 97.39 97.39 1.98e-100 . . . . 4568 1 221 no PDB 2W6Y . "Crystal Structure Of Sperm Whale Myoglobin Mutant Yqr In Complex With Xenon" . . . . . 100.00 154 98.04 98.04 3.72e-101 . . . . 4568 1 222 no PDB 2Z6S . "Crystal Structure Of The Oxy Myoglobin Free From X-ray- Induced Photoreduction" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 223 no PDB 2Z6T . "Crystal Structure Of The Ferric Peroxo Myoglobin" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 224 no PDB 2ZSN . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [300 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 225 no PDB 2ZSO . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [450 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 226 no PDB 2ZSP . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [300 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 227 no PDB 2ZSQ . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser On [150 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 228 no PDB 2ZSR . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [450 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 229 no PDB 2ZSS . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser On [300 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 230 no PDB 2ZST . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser On [450 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 231 no PDB 2ZSX . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser On [600 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 232 no PDB 2ZSY . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser On [750 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 233 no PDB 2ZSZ . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [600 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 234 no PDB 2ZT0 . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [750 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 235 no PDB 2ZT1 . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [810 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 236 no PDB 2ZT2 . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [600 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 237 no PDB 2ZT3 . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [750 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 238 no PDB 2ZT4 . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [810 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 239 no PDB 3A2G . "Crystal Structure Of K102c-Myoglobin Conjugated With Fluorescein" . . . . . 100.00 154 99.35 99.35 9.07e-103 . . . . 4568 1 240 no PDB 3ASE . "Crystal Structure Of Zinc Myoglobin Soaked With Ru3o Cluster" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 241 no PDB 3E4N . "Carbonmonoxy Sperm Whale Myoglobin At 40 K: Laser Off" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 242 no PDB 3E55 . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser Off" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 243 no PDB 3E5I . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser Off" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 244 no PDB 3E5O . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser Off" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 245 no PDB 3ECL . "Carbonmonoxy Sperm Whale Myoglobin At 40 K: Laser On" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 246 no PDB 3ECX . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [30 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 247 no PDB 3ECZ . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [30 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 248 no PDB 3ED9 . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser On [30 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 249 no PDB 3EDA . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [150 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 250 no PDB 3EDB . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [150 Min]" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 251 no PDB 3H57 . "Myoglobin Cavity Mutant H64lv68n Deoxy Form" . . . . . 100.00 154 98.04 98.69 1.21e-100 . . . . 4568 1 252 no PDB 3H58 . "Myoglobin Cavity Mutant H64lv68n Met Form" . . . . . 100.00 154 98.04 98.69 1.21e-100 . . . . 4568 1 253 no PDB 3K9Z . "Rational Design Of A Structural And Functional Nitric Oxide Reductase" . . . . . 100.00 153 98.04 98.04 8.01e-100 . . . . 4568 1 254 no PDB 3M38 . "The Roles Of Glutamates And Metal Ions In A Rationally Designed Nitric Oxide Reductase Based On Myoglobin: I107e Febmb (No Meta" . . . . . 100.00 153 97.39 97.39 9.35e-99 . . . . 4568 1 255 no PDB 3M39 . "The Roles Of Glutamates And Metal Ions In A Rationally Desig Oxide Reductase Based On Myoglobin: Fe(Ii)-I107e Febmb (Fe( Bindin" . . . . . 100.00 153 97.39 97.39 9.35e-99 . . . . 4568 1 256 no PDB 3M3A . "The Roles Of Glutamates And Metal Ions In A Rationally Desig Oxide Reductase Based On Myoglobin: Cu(Ii)-I107e Febmb (Cu( Bindin" . . . . . 100.00 153 97.39 97.39 9.35e-99 . . . . 4568 1 257 no PDB 3M3B . "The Roles Of Glutamates And Metal Ions In A Rationally Desig Oxide Reductase Based On Myoglobin: Zn(Ii)-I107e Febmb (Zn( Bindin" . . . . . 100.00 153 97.39 97.39 9.35e-99 . . . . 4568 1 258 no PDB 3MN0 . "Introducing A 2-His-1-Glu Non-Heme Iron Center Into Myoglobin Confers Nitric Oxide Reductase Activity: Cu(Ii)-Cn-Febmb(-His) Fo" . . . . . 100.00 153 98.69 98.69 5.05e-101 . . . . 4568 1 259 no PDB 3NML . "Sperm Whale Myoglobin Mutant H64w Carbonmonoxy-Form" . . . . . 100.00 154 98.69 99.35 1.68e-101 . . . . 4568 1 260 no PDB 3O89 . "Crystal Structure Of Sperm Whale Myoglobin G65t" . . . . . 100.00 153 99.35 99.35 1.40e-102 . . . . 4568 1 261 no PDB 3OGB . "Sperm Whale Myoglobin Mutant H64w Deoxy-Form" . . . . . 100.00 154 98.69 99.35 1.68e-101 . . . . 4568 1 262 no PDB 3SDN . "Structure Of G65i Sperm Whale Myoglobin Mutant" . . . . . 100.00 154 99.35 99.35 3.44e-102 . . . . 4568 1 263 no PDB 3U3E . "Complex Of Wild Type Myoglobin With Phenol In Its Proximal Cavity" . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 264 no PDB 4FWX . "Aquoferric F33y Cub Myoglobin (F33y L29h F43h Sperm Whale Myoglobin)" . . . . . 100.00 153 98.04 98.69 1.81e-100 . . . . 4568 1 265 no PDB 4FWY . "F33y Cub Myoglobin (F33y L29h F43h Sperm Whale Myoglobin) With Copper Bound" . . . . . 100.00 153 98.04 98.69 1.81e-100 . . . . 4568 1 266 no PDB 4FWZ . "Aquoferric Cub Myoglobin (L29h F43h Sperm Whale Myoglobin)" . . . . . 100.00 153 98.69 98.69 6.28e-101 . . . . 4568 1 267 no PDB 4H07 . "Complex Of G65t Myoglobin With Phenol In Its Proximal Cavity" . . . . . 100.00 154 99.35 99.35 1.36e-102 . . . . 4568 1 268 no PDB 4H0B . "Complex Of G65t Myoglobin With Dmso In Its Distal Cavity" . . . . . 100.00 154 99.35 99.35 1.36e-102 . . . . 4568 1 269 no PDB 4IT8 . "A Sperm Whale Myoglobin Mutant L29h Mb With Two Distal Histidines" . . . . . 100.00 154 99.35 99.35 4.10e-102 . . . . 4568 1 270 no PDB 4LPI . "A Sperm Whale Myoglobin Double Mutant L29h/f43y Mb With A Distal Hydrogen-bonding Network" . . . . . 100.00 154 98.69 99.35 7.07e-102 . . . . 4568 1 271 no PDB 4MBN . "Refinement Of Myoglobin And Cytochrome C" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 272 no PDB 4MXK . "X-ray Structure Of Fe(ii)-znpixfebmb1" . . . . . 100.00 153 98.04 98.04 8.01e-100 . . . . 4568 1 273 no PDB 4MXL . "X-ray Structure Of Znpfebmb1" . . . . . 100.00 153 98.04 98.04 8.01e-100 . . . . 4568 1 274 no PDB 4NXA . "Sperm Whale Myoglobin Under Xenon Pressure 30 Bar" . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 275 no PDB 4NXC . "Sperm Whale Myoglobin Under 30 Bar Nitrous Oxide" . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 276 no PDB 4OF9 . "Structure Of K42n Variant Of Sperm Whale Myoglobin" . . . . . 100.00 153 99.35 99.35 6.18e-103 . . . . 4568 1 277 no PDB 4OOD . "Structure Of K42y Mutant Of Sperm Whale Myoglobin" . . . . . 100.00 154 99.35 99.35 1.18e-102 . . . . 4568 1 278 no PDB 4PNJ . "Recombinant Sperm Whale P6 Myoglobin Solved With Single Pulse Free Electron Laser Data" . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 279 no PDB 4PQ6 . "A Sperm Whale Myoglobin Single Mutant L29e Mb With Native His93 Coordination" . . . . . 100.00 154 99.35 99.35 1.87e-102 . . . . 4568 1 280 no PDB 4PQB . "A Sperm Whale Myoglobin Double Mutant L29e/f43h Mb With A Non-native Bis-his (his64/his93) Coordination" . . . . . 100.00 154 98.69 98.69 3.85e-101 . . . . 4568 1 281 no PDB 4PQC . "A Sperm Whale Myoglobin Single Mutant F43h Mb With Native His93 Coordination" . . . . . 100.00 154 99.35 99.35 3.88e-102 . . . . 4568 1 282 no PDB 4QAU . "Crystal Structure Of F43y Mutant Of Sperm Whale Myoglobin" . . . . . 100.00 154 99.35 100.00 4.31e-103 . . . . 4568 1 283 no PDB 4TYX . "Structure Of Aquoferric Sperm Whale Myoglobin L29h/f33y/f43h/s92a Mutant" . . . . . 100.00 153 97.39 98.69 6.03e-100 . . . . 4568 1 284 no PDB 5C6Y . "A Sperm Whale Myoglobin Double Mutant L29h/f43y Mb With A Tyr-heme Cross-link" . . . . . 100.00 154 98.69 99.35 7.07e-102 . . . . 4568 1 285 no PDB 5MBN . "Refinement Of Myoglobin And Cytochrome C" . . . . . 100.00 153 100.00 100.00 1.65e-103 . . . . 4568 1 286 no DBJ BAF03579 . "myoglobin [Physeter catodon]" . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 287 no GB AAA72199 . "synthetic myoglobin [synthetic construct]" . . . . . 100.00 154 99.35 100.00 5.31e-103 . . . . 4568 1 288 no PRF 742482A . myoglobin . . . . . 100.00 153 99.35 100.00 5.92e-103 . . . . 4568 1 289 no REF NP_001277651 . "myoglobin [Physeter catodon]" . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 290 no SP P02185 . "RecName: Full=Myoglobin" . . . . . 100.00 154 100.00 100.00 1.70e-103 . . . . 4568 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID myoglobin common 4568 1 'sperm whale sequence' variant 4568 1 Mb abbreviation 4568 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . VAL . 4568 1 2 . LEU . 4568 1 3 . SER . 4568 1 4 . GLU . 4568 1 5 . GLY . 4568 1 6 . GLU . 4568 1 7 . TRP . 4568 1 8 . GLN . 4568 1 9 . LEU . 4568 1 10 . VAL . 4568 1 11 . LEU . 4568 1 12 . HIS . 4568 1 13 . VAL . 4568 1 14 . TRP . 4568 1 15 . ALA . 4568 1 16 . LYS . 4568 1 17 . VAL . 4568 1 18 . GLU . 4568 1 19 . ALA . 4568 1 20 . ASP . 4568 1 21 . VAL . 4568 1 22 . ALA . 4568 1 23 . GLY . 4568 1 24 . HIS . 4568 1 25 . GLY . 4568 1 26 . GLN . 4568 1 27 . ASP . 4568 1 28 . ILE . 4568 1 29 . LEU . 4568 1 30 . ILE . 4568 1 31 . ARG . 4568 1 32 . LEU . 4568 1 33 . PHE . 4568 1 34 . LYS . 4568 1 35 . SER . 4568 1 36 . HIS . 4568 1 37 . PRO . 4568 1 38 . GLU . 4568 1 39 . THR . 4568 1 40 . LEU . 4568 1 41 . GLU . 4568 1 42 . LYS . 4568 1 43 . PHE . 4568 1 44 . ASP . 4568 1 45 . ARG . 4568 1 46 . PHE . 4568 1 47 . LYS . 4568 1 48 . HIS . 4568 1 49 . LEU . 4568 1 50 . LYS . 4568 1 51 . THR . 4568 1 52 . GLU . 4568 1 53 . ALA . 4568 1 54 . GLU . 4568 1 55 . MET . 4568 1 56 . LYS . 4568 1 57 . ALA . 4568 1 58 . SER . 4568 1 59 . GLU . 4568 1 60 . ASP . 4568 1 61 . LEU . 4568 1 62 . LYS . 4568 1 63 . LYS . 4568 1 64 . HIS . 4568 1 65 . GLY . 4568 1 66 . VAL . 4568 1 67 . THR . 4568 1 68 . VAL . 4568 1 69 . LEU . 4568 1 70 . THR . 4568 1 71 . ALA . 4568 1 72 . LEU . 4568 1 73 . GLY . 4568 1 74 . ALA . 4568 1 75 . ILE . 4568 1 76 . LEU . 4568 1 77 . LYS . 4568 1 78 . LYS . 4568 1 79 . LYS . 4568 1 80 . GLY . 4568 1 81 . HIS . 4568 1 82 . HIS . 4568 1 83 . GLU . 4568 1 84 . ALA . 4568 1 85 . GLU . 4568 1 86 . LEU . 4568 1 87 . LYS . 4568 1 88 . PRO . 4568 1 89 . LEU . 4568 1 90 . ALA . 4568 1 91 . GLN . 4568 1 92 . SER . 4568 1 93 . HIS . 4568 1 94 . ALA . 4568 1 95 . THR . 4568 1 96 . LYS . 4568 1 97 . HIS . 4568 1 98 . LYS . 4568 1 99 . ILE . 4568 1 100 . PRO . 4568 1 101 . ILE . 4568 1 102 . LYS . 4568 1 103 . TYR . 4568 1 104 . LEU . 4568 1 105 . GLU . 4568 1 106 . PHE . 4568 1 107 . ILE . 4568 1 108 . SER . 4568 1 109 . GLU . 4568 1 110 . ALA . 4568 1 111 . ILE . 4568 1 112 . ILE . 4568 1 113 . HIS . 4568 1 114 . VAL . 4568 1 115 . LEU . 4568 1 116 . HIS . 4568 1 117 . SER . 4568 1 118 . ARG . 4568 1 119 . HIS . 4568 1 120 . PRO . 4568 1 121 . GLY . 4568 1 122 . ASP . 4568 1 123 . PHE . 4568 1 124 . GLY . 4568 1 125 . ALA . 4568 1 126 . ASP . 4568 1 127 . ALA . 4568 1 128 . GLN . 4568 1 129 . GLY . 4568 1 130 . ALA . 4568 1 131 . MET . 4568 1 132 . ASN . 4568 1 133 . LYS . 4568 1 134 . ALA . 4568 1 135 . LEU . 4568 1 136 . GLU . 4568 1 137 . LEU . 4568 1 138 . PHE . 4568 1 139 . ARG . 4568 1 140 . LYS . 4568 1 141 . ASP . 4568 1 142 . ILE . 4568 1 143 . ALA . 4568 1 144 . ALA . 4568 1 145 . LYS . 4568 1 146 . TYR . 4568 1 147 . LYS . 4568 1 148 . GLU . 4568 1 149 . LEU . 4568 1 150 . GLY . 4568 1 151 . TYR . 4568 1 152 . GLN . 4568 1 153 . GLY . 4568 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . VAL 1 1 4568 1 . LEU 2 2 4568 1 . SER 3 3 4568 1 . GLU 4 4 4568 1 . GLY 5 5 4568 1 . GLU 6 6 4568 1 . TRP 7 7 4568 1 . GLN 8 8 4568 1 . LEU 9 9 4568 1 . VAL 10 10 4568 1 . LEU 11 11 4568 1 . HIS 12 12 4568 1 . VAL 13 13 4568 1 . TRP 14 14 4568 1 . ALA 15 15 4568 1 . LYS 16 16 4568 1 . VAL 17 17 4568 1 . GLU 18 18 4568 1 . ALA 19 19 4568 1 . ASP 20 20 4568 1 . VAL 21 21 4568 1 . ALA 22 22 4568 1 . GLY 23 23 4568 1 . HIS 24 24 4568 1 . GLY 25 25 4568 1 . GLN 26 26 4568 1 . ASP 27 27 4568 1 . ILE 28 28 4568 1 . LEU 29 29 4568 1 . ILE 30 30 4568 1 . ARG 31 31 4568 1 . LEU 32 32 4568 1 . PHE 33 33 4568 1 . LYS 34 34 4568 1 . SER 35 35 4568 1 . HIS 36 36 4568 1 . PRO 37 37 4568 1 . GLU 38 38 4568 1 . THR 39 39 4568 1 . LEU 40 40 4568 1 . GLU 41 41 4568 1 . LYS 42 42 4568 1 . PHE 43 43 4568 1 . ASP 44 44 4568 1 . ARG 45 45 4568 1 . PHE 46 46 4568 1 . LYS 47 47 4568 1 . HIS 48 48 4568 1 . LEU 49 49 4568 1 . LYS 50 50 4568 1 . THR 51 51 4568 1 . GLU 52 52 4568 1 . ALA 53 53 4568 1 . GLU 54 54 4568 1 . MET 55 55 4568 1 . LYS 56 56 4568 1 . ALA 57 57 4568 1 . SER 58 58 4568 1 . GLU 59 59 4568 1 . ASP 60 60 4568 1 . LEU 61 61 4568 1 . LYS 62 62 4568 1 . LYS 63 63 4568 1 . HIS 64 64 4568 1 . GLY 65 65 4568 1 . VAL 66 66 4568 1 . THR 67 67 4568 1 . VAL 68 68 4568 1 . LEU 69 69 4568 1 . THR 70 70 4568 1 . ALA 71 71 4568 1 . LEU 72 72 4568 1 . GLY 73 73 4568 1 . ALA 74 74 4568 1 . ILE 75 75 4568 1 . LEU 76 76 4568 1 . LYS 77 77 4568 1 . LYS 78 78 4568 1 . LYS 79 79 4568 1 . GLY 80 80 4568 1 . HIS 81 81 4568 1 . HIS 82 82 4568 1 . GLU 83 83 4568 1 . ALA 84 84 4568 1 . GLU 85 85 4568 1 . LEU 86 86 4568 1 . LYS 87 87 4568 1 . PRO 88 88 4568 1 . LEU 89 89 4568 1 . ALA 90 90 4568 1 . GLN 91 91 4568 1 . SER 92 92 4568 1 . HIS 93 93 4568 1 . ALA 94 94 4568 1 . THR 95 95 4568 1 . LYS 96 96 4568 1 . HIS 97 97 4568 1 . LYS 98 98 4568 1 . ILE 99 99 4568 1 . PRO 100 100 4568 1 . ILE 101 101 4568 1 . LYS 102 102 4568 1 . TYR 103 103 4568 1 . LEU 104 104 4568 1 . GLU 105 105 4568 1 . PHE 106 106 4568 1 . ILE 107 107 4568 1 . SER 108 108 4568 1 . GLU 109 109 4568 1 . ALA 110 110 4568 1 . ILE 111 111 4568 1 . ILE 112 112 4568 1 . HIS 113 113 4568 1 . VAL 114 114 4568 1 . LEU 115 115 4568 1 . HIS 116 116 4568 1 . SER 117 117 4568 1 . ARG 118 118 4568 1 . HIS 119 119 4568 1 . PRO 120 120 4568 1 . GLY 121 121 4568 1 . ASP 122 122 4568 1 . PHE 123 123 4568 1 . GLY 124 124 4568 1 . ALA 125 125 4568 1 . ASP 126 126 4568 1 . ALA 127 127 4568 1 . GLN 128 128 4568 1 . GLY 129 129 4568 1 . ALA 130 130 4568 1 . MET 131 131 4568 1 . ASN 132 132 4568 1 . LYS 133 133 4568 1 . ALA 134 134 4568 1 . LEU 135 135 4568 1 . GLU 136 136 4568 1 . LEU 137 137 4568 1 . PHE 138 138 4568 1 . ARG 139 139 4568 1 . LYS 140 140 4568 1 . ASP 141 141 4568 1 . ILE 142 142 4568 1 . ALA 143 143 4568 1 . ALA 144 144 4568 1 . LYS 145 145 4568 1 . TYR 146 146 4568 1 . LYS 147 147 4568 1 . GLU 148 148 4568 1 . LEU 149 149 4568 1 . GLY 150 150 4568 1 . TYR 151 151 4568 1 . GLN 152 152 4568 1 . GLY 153 153 4568 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 4568 _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 $apoMb . 9755 organism . 'Physeter catodon' 'sperm whale' . . Eukaryota Metazoa Physeter catodon . . . . muscle . . . . . . . . . . . . . ; sperm whale sequence, recombinant protein obtained from cloned sequence using E. coli ; . . 4568 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 4568 _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 $apoMb . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli K12 BL21(DE3) . . . . . . . . . . . plasmid . . . . . . . . . 4568 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4568 _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 myoglobin '[U-95% 13C; U-90% 15N; U-80% 2H]' . . 1 $apoMb . . 0.3 . . mM . . . . 4568 1 2 'sodium acetate' '[U-90% 2H]' . . . . . . 10 . . mM . . . . 4568 1 3 ethanol '[U-90% 2H]' . . . . . . 10 . . '% by volume' . . . . 4568 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 4568 _Sample_condition_list.ID 1 _Sample_condition_list.Details ; Ionic strength must be kept extremely low or aggregation of the molten globule occurs 10% ethanol is added to increase long-term stability of the molten globule The addition of ethanol does not perturb the HSQC spectrum of the pH 4 state NMR measurements were made at 50C to minimize linewidths. ; 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 4.1 0.1 n/a 4568 1 temperature 323 1 K 4568 1 'ionic strength' 0.005 0.0005 M 4568 1 stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 4568 _Software.ID 1 _Software.Name FELIX _Software.Version 4.2 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data processing' 4568 1 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 4568 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 750 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4568 _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 . 750 . . . 4568 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 4568 _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 HNCO . . . . . . . . . . . 1 $sample_1 . . . 1 $ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4568 1 2 H(CA)CO(CA)NH . . . . . . . . . . . 1 $sample_1 . . . 1 $ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4568 1 3 HNCA . . . . . . . . . . . 1 $sample_1 . . . 1 $ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4568 1 4 HN(CO)CA . . . . . . . . . . . 1 $sample_1 . . . 1 $ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4568 1 5 HN(CA)CB . . . . . . . . . . . 1 $sample_1 . . . 1 $ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4568 1 6 CBCA(CO)NH . . . . . . . . . . . 1 $sample_1 . . . 1 $ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4568 1 7 '1H-15N HSQC-NOESY-HSQC' . . . . . . . . . . . 1 $sample_1 . . . 1 $ex-cond_1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4568 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 4568 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name HNCO _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 1 _NMR_spec_expt.Software_label $FELIX _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 4568 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name H(CA)CO(CA)NH _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 1 _NMR_spec_expt.Software_label $FELIX _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 4568 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name HNCA _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 1 _NMR_spec_expt.Software_label $FELIX _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_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 4568 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name HN(CO)CA _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 1 _NMR_spec_expt.Software_label $FELIX _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_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 4568 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name HN(CA)CB _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 1 _NMR_spec_expt.Software_label $FELIX _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_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 4568 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name CBCA(CO)NH _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 1 _NMR_spec_expt.Software_label $FELIX _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_7 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_7 _NMR_spec_expt.Entry_ID 4568 _NMR_spec_expt.ID 7 _NMR_spec_expt.Name '1H-15N HSQC-NOESY-HSQC' _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 1 _NMR_spec_expt.Software_label $FELIX _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 4568 _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 . direct . . . . . . . . . . 4568 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4568 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 4568 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 4568 _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 HNCO 1 $sample_1 . 4568 1 2 H(CA)CO(CA)NH 1 $sample_1 . 4568 1 3 HNCA 1 $sample_1 . 4568 1 4 HN(CO)CA 1 $sample_1 . 4568 1 5 HN(CA)CB 1 $sample_1 . 4568 1 6 CBCA(CO)NH 1 $sample_1 . 4568 1 7 '1H-15N HSQC-NOESY-HSQC' 1 $sample_1 . 4568 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 VAL H H 1 8.461 0.02 . . . . . . . . . . 4568 1 2 . 1 1 1 1 VAL C C 13 179.807 0.05 . . . . . . . . . . 4568 1 3 . 1 1 1 1 VAL CA C 13 62.426 0.05 . . . . . . . . . . 4568 1 4 . 1 1 1 1 VAL CB C 13 32.969 0.05 . . . . . . . . . . 4568 1 5 . 1 1 1 1 VAL N N 15 123.226 0.05 . . . . . . . . . . 4568 1 6 . 1 1 2 2 LEU H H 1 8.116 0.02 . . . . . . . . . . 4568 1 7 . 1 1 2 2 LEU HA H 1 4.488 0.02 . . . . . . . . . . 4568 1 8 . 1 1 2 2 LEU C C 13 174.999 0.05 . . . . . . . . . . 4568 1 9 . 1 1 2 2 LEU CA C 13 54.396 0.05 . . . . . . . . . . 4568 1 10 . 1 1 2 2 LEU CB C 13 43.107 0.05 . . . . . . . . . . 4568 1 11 . 1 1 2 2 LEU N N 15 125.477 0.05 . . . . . . . . . . 4568 1 12 . 1 1 3 3 SER H H 1 8.427 0.02 . . . . . . . . . . 4568 1 13 . 1 1 3 3 SER HA H 1 4.524 0.02 . . . . . . . . . . 4568 1 14 . 1 1 3 3 SER C C 13 176.634 0.05 . . . . . . . . . . 4568 1 15 . 1 1 3 3 SER CA C 13 57.684 0.05 . . . . . . . . . . 4568 1 16 . 1 1 3 3 SER CB C 13 64.754 0.05 . . . . . . . . . . 4568 1 17 . 1 1 3 3 SER N N 15 117.600 0.05 . . . . . . . . . . 4568 1 18 . 1 1 4 4 GLU H H 1 8.772 0.02 . . . . . . . . . . 4568 1 19 . 1 1 4 4 GLU HA H 1 4.195 0.02 . . . . . . . . . . 4568 1 20 . 1 1 4 4 GLU C C 13 174.911 0.05 . . . . . . . . . . 4568 1 21 . 1 1 4 4 GLU CA C 13 59.119 0.05 . . . . . . . . . . 4568 1 22 . 1 1 4 4 GLU CB C 13 29.271 0.05 . . . . . . . . . . 4568 1 23 . 1 1 4 4 GLU N N 15 122.101 0.05 . . . . . . . . . . 4568 1 24 . 1 1 5 5 GLY H H 1 8.503 0.02 . . . . . . . . . . 4568 1 25 . 1 1 5 5 GLY HA2 H 1 3.857 0.02 . . . . . . . . . . 4568 1 26 . 1 1 5 5 GLY C C 13 178.343 0.05 . . . . . . . . . . 4568 1 27 . 1 1 5 5 GLY CA C 13 46.701 0.05 . . . . . . . . . . 4568 1 28 . 1 1 5 5 GLY N N 15 107.098 0.05 . . . . . . . . . . 4568 1 29 . 1 1 6 6 GLU H H 1 7.844 0.02 . . . . . . . . . . 4568 1 30 . 1 1 6 6 GLU HA H 1 4.001 0.02 . . . . . . . . . . 4568 1 31 . 1 1 6 6 GLU C C 13 176.272 0.05 . . . . . . . . . . 4568 1 32 . 1 1 6 6 GLU CA C 13 58.631 0.05 . . . . . . . . . . 4568 1 33 . 1 1 6 6 GLU CB C 13 29.588 0.05 . . . . . . . . . . 4568 1 34 . 1 1 6 6 GLU N N 15 121.726 0.05 . . . . . . . . . . 4568 1 35 . 1 1 7 7 TRP H H 1 8.341 0.02 . . . . . . . . . . 4568 1 36 . 1 1 7 7 TRP HA H 1 4.418 0.02 . . . . . . . . . . 4568 1 37 . 1 1 7 7 TRP C C 13 177.979 0.05 . . . . . . . . . . 4568 1 38 . 1 1 7 7 TRP CA C 13 59.678 0.05 . . . . . . . . . . 4568 1 39 . 1 1 7 7 TRP CB C 13 29.582 0.05 . . . . . . . . . . 4568 1 40 . 1 1 7 7 TRP N N 15 120.226 0.05 . . . . . . . . . . 4568 1 41 . 1 1 8 8 GLN H H 1 8.061 0.02 . . . . . . . . . . 4568 1 42 . 1 1 8 8 GLN C C 13 177.551 0.05 . . . . . . . . . . 4568 1 43 . 1 1 8 8 GLN CA C 13 58.869 0.05 . . . . . . . . . . 4568 1 44 . 1 1 8 8 GLN CB C 13 28.189 0.05 . . . . . . . . . . 4568 1 45 . 1 1 8 8 GLN N N 15 116.475 0.05 . . . . . . . . . . 4568 1 46 . 1 1 9 9 LEU H H 1 7.483 0.02 . . . . . . . . . . 4568 1 47 . 1 1 9 9 LEU HA H 1 4.104 0.02 . . . . . . . . . . 4568 1 48 . 1 1 9 9 LEU C C 13 178.411 0.05 . . . . . . . . . . 4568 1 49 . 1 1 9 9 LEU CA C 13 58.000 0.05 . . . . . . . . . . 4568 1 50 . 1 1 9 9 LEU N N 15 120.601 0.05 . . . . . . . . . . 4568 1 51 . 1 1 10 10 VAL H H 1 7.857 0.02 . . . . . . . . . . 4568 1 52 . 1 1 10 10 VAL C C 13 178.641 0.05 . . . . . . . . . . 4568 1 53 . 1 1 10 10 VAL CA C 13 66.433 0.05 . . . . . . . . . . 4568 1 54 . 1 1 10 10 VAL CB C 13 33.040 0.05 . . . . . . . . . . 4568 1 55 . 1 1 10 10 VAL N N 15 119.101 0.05 . . . . . . . . . . 4568 1 56 . 1 1 11 11 LEU H H 1 8.071 0.02 . . . . . . . . . . 4568 1 57 . 1 1 11 11 LEU HA H 1 3.952 0.02 . . . . . . . . . . 4568 1 58 . 1 1 11 11 LEU C C 13 177.443 0.05 . . . . . . . . . . 4568 1 59 . 1 1 11 11 LEU CA C 13 57.723 0.05 . . . . . . . . . . 4568 1 60 . 1 1 11 11 LEU CB C 13 41.358 0.05 . . . . . . . . . . 4568 1 61 . 1 1 11 11 LEU N N 15 118.726 0.05 . . . . . . . . . . 4568 1 62 . 1 1 12 12 HIS H H 1 7.964 0.02 . . . . . . . . . . 4568 1 63 . 1 1 12 12 HIS HA H 1 4.407 0.02 . . . . . . . . . . 4568 1 64 . 1 1 12 12 HIS C C 13 179.200 0.05 . . . . . . . . . . 4568 1 65 . 1 1 12 12 HIS CA C 13 57.430 0.05 . . . . . . . . . . 4568 1 66 . 1 1 12 12 HIS N N 15 117.225 0.05 . . . . . . . . . . 4568 1 67 . 1 1 13 13 VAL H H 1 8.106 0.02 . . . . . . . . . . 4568 1 68 . 1 1 13 13 VAL C C 13 176.885 0.05 . . . . . . . . . . 4568 1 69 . 1 1 13 13 VAL CA C 13 65.000 0.05 . . . . . . . . . . 4568 1 70 . 1 1 13 13 VAL N N 15 119.476 0.05 . . . . . . . . . . 4568 1 71 . 1 1 14 14 TRP H H 1 8.484 0.02 . . . . . . . . . . 4568 1 72 . 1 1 14 14 TRP HA H 1 4.286 0.02 . . . . . . . . . . 4568 1 73 . 1 1 14 14 TRP C C 13 177.366 0.05 . . . . . . . . . . 4568 1 74 . 1 1 14 14 TRP CA C 13 59.599 0.05 . . . . . . . . . . 4568 1 75 . 1 1 14 14 TRP CB C 13 29.428 0.05 . . . . . . . . . . 4568 1 76 . 1 1 14 14 TRP N N 15 120.976 0.05 . . . . . . . . . . 4568 1 77 . 1 1 15 15 ALA H H 1 7.996 0.02 . . . . . . . . . . 4568 1 78 . 1 1 15 15 ALA HA H 1 3.909 0.02 . . . . . . . . . . 4568 1 79 . 1 1 15 15 ALA C C 13 176.917 0.05 . . . . . . . . . . 4568 1 80 . 1 1 15 15 ALA CA C 13 54.396 0.05 . . . . . . . . . . 4568 1 81 . 1 1 15 15 ALA CB C 13 18.310 0.05 . . . . . . . . . . 4568 1 82 . 1 1 15 15 ALA N N 15 119.476 0.05 . . . . . . . . . . 4568 1 83 . 1 1 16 16 LYS H H 1 7.481 0.02 . . . . . . . . . . 4568 1 84 . 1 1 16 16 LYS HA H 1 4.091 0.02 . . . . . . . . . . 4568 1 85 . 1 1 16 16 LYS C C 13 179.382 0.05 . . . . . . . . . . 4568 1 86 . 1 1 16 16 LYS CA C 13 57.667 0.05 . . . . . . . . . . 4568 1 87 . 1 1 16 16 LYS CB C 13 32.286 0.05 . . . . . . . . . . 4568 1 88 . 1 1 16 16 LYS N N 15 117.600 0.05 . . . . . . . . . . 4568 1 89 . 1 1 17 17 VAL H H 1 7.846 0.02 . . . . . . . . . . 4568 1 90 . 1 1 17 17 VAL HA H 1 3.774 0.02 . . . . . . . . . . 4568 1 91 . 1 1 17 17 VAL C C 13 177.907 0.05 . . . . . . . . . . 4568 1 92 . 1 1 17 17 VAL N N 15 118.726 0.05 . . . . . . . . . . 4568 1 93 . 1 1 18 18 GLU H H 1 7.836 0.02 . . . . . . . . . . 4568 1 94 . 1 1 18 18 GLU C C 13 175.837 0.05 . . . . . . . . . . 4568 1 95 . 1 1 18 18 GLU CA C 13 57.826 0.05 . . . . . . . . . . 4568 1 96 . 1 1 18 18 GLU CB C 13 28.711 0.05 . . . . . . . . . . 4568 1 97 . 1 1 18 18 GLU N N 15 119.820 0.05 . . . . . . . . . . 4568 1 98 . 1 1 19 19 ALA H H 1 7.615 0.02 . . . . . . . . . . 4568 1 99 . 1 1 19 19 ALA HA H 1 4.104 0.02 . . . . . . . . . . 4568 1 100 . 1 1 19 19 ALA C C 13 176.988 0.05 . . . . . . . . . . 4568 1 101 . 1 1 19 19 ALA CA C 13 53.769 0.05 . . . . . . . . . . 4568 1 102 . 1 1 19 19 ALA CB C 13 18.634 0.05 . . . . . . . . . . 4568 1 103 . 1 1 19 19 ALA N N 15 121.351 0.05 . . . . . . . . . . 4568 1 104 . 1 1 20 20 ASP H H 1 7.908 0.02 . . . . . . . . . . 4568 1 105 . 1 1 20 20 ASP HA H 1 4.540 0.02 . . . . . . . . . . 4568 1 106 . 1 1 20 20 ASP C C 13 178.499 0.05 . . . . . . . . . . 4568 1 107 . 1 1 20 20 ASP CA C 13 55.044 0.05 . . . . . . . . . . 4568 1 108 . 1 1 20 20 ASP CB C 13 40.724 0.05 . . . . . . . . . . 4568 1 109 . 1 1 20 20 ASP N N 15 118.350 0.05 . . . . . . . . . . 4568 1 110 . 1 1 21 21 VAL H H 1 7.851 0.02 . . . . . . . . . . 4568 1 111 . 1 1 21 21 VAL HA H 1 3.933 0.02 . . . . . . . . . . 4568 1 112 . 1 1 21 21 VAL C C 13 177.182 0.05 . . . . . . . . . . 4568 1 113 . 1 1 21 21 VAL CA C 13 63.391 0.05 . . . . . . . . . . 4568 1 114 . 1 1 21 21 VAL CB C 13 32.274 0.05 . . . . . . . . . . 4568 1 115 . 1 1 21 21 VAL N N 15 118.350 0.05 . . . . . . . . . . 4568 1 116 . 1 1 22 22 ALA H H 1 8.000 0.02 . . . . . . . . . . 4568 1 117 . 1 1 22 22 ALA HA H 1 4.158 0.02 . . . . . . . . . . 4568 1 118 . 1 1 22 22 ALA C C 13 176.499 0.05 . . . . . . . . . . 4568 1 119 . 1 1 22 22 ALA CA C 13 53.076 0.05 . . . . . . . . . . 4568 1 120 . 1 1 22 22 ALA CB C 13 18.831 0.05 . . . . . . . . . . 4568 1 121 . 1 1 22 22 ALA N N 15 123.977 0.05 . . . . . . . . . . 4568 1 122 . 1 1 23 23 GLY H H 1 8.027 0.02 . . . . . . . . . . 4568 1 123 . 1 1 23 23 GLY HA2 H 1 3.889 0.02 . . . . . . . . . . 4568 1 124 . 1 1 23 23 GLY C C 13 178.415 0.05 . . . . . . . . . . 4568 1 125 . 1 1 23 23 GLY CA C 13 45.605 0.05 . . . . . . . . . . 4568 1 126 . 1 1 23 23 GLY N N 15 106.723 0.05 . . . . . . . . . . 4568 1 127 . 1 1 24 24 HIS H H 1 8.169 0.02 . . . . . . . . . . 4568 1 128 . 1 1 24 24 HIS HA H 1 4.713 0.02 . . . . . . . . . . 4568 1 129 . 1 1 24 24 HIS C C 13 174.562 0.05 . . . . . . . . . . 4568 1 130 . 1 1 24 24 HIS CA C 13 55.771 0.05 . . . . . . . . . . 4568 1 131 . 1 1 24 24 HIS CB C 13 28.958 0.05 . . . . . . . . . . 4568 1 132 . 1 1 24 24 HIS N N 15 117.600 0.05 . . . . . . . . . . 4568 1 133 . 1 1 25 25 GLY H H 1 8.462 0.02 . . . . . . . . . . 4568 1 134 . 1 1 25 25 GLY HA2 H 1 3.921 0.02 . . . . . . . . . . 4568 1 135 . 1 1 25 25 GLY C C 13 175.129 0.05 . . . . . . . . . . 4568 1 136 . 1 1 25 25 GLY CA C 13 46.384 0.05 . . . . . . . . . . 4568 1 137 . 1 1 25 25 GLY N N 15 108.974 0.05 . . . . . . . . . . 4568 1 138 . 1 1 26 26 GLN H H 1 8.257 0.02 . . . . . . . . . . 4568 1 139 . 1 1 26 26 GLN HA H 1 4.133 0.02 . . . . . . . . . . 4568 1 140 . 1 1 26 26 GLN C C 13 174.561 0.05 . . . . . . . . . . 4568 1 141 . 1 1 26 26 GLN CA C 13 57.500 0.05 . . . . . . . . . . 4568 1 142 . 1 1 26 26 GLN CB C 13 29.026 0.05 . . . . . . . . . . 4568 1 143 . 1 1 26 26 GLN N N 15 119.851 0.05 . . . . . . . . . . 4568 1 144 . 1 1 27 27 ASP H H 1 8.206 0.02 . . . . . . . . . . 4568 1 145 . 1 1 27 27 ASP HA H 1 4.411 0.02 . . . . . . . . . . 4568 1 146 . 1 1 27 27 ASP C C 13 176.321 0.05 . . . . . . . . . . 4568 1 147 . 1 1 27 27 ASP CA C 13 55.853 0.05 . . . . . . . . . . 4568 1 148 . 1 1 27 27 ASP CB C 13 40.673 0.05 . . . . . . . . . . 4568 1 149 . 1 1 27 27 ASP N N 15 119.476 0.05 . . . . . . . . . . 4568 1 150 . 1 1 28 28 ILE H H 1 7.744 0.02 . . . . . . . . . . 4568 1 151 . 1 1 28 28 ILE HA H 1 3.807 0.02 . . . . . . . . . . 4568 1 152 . 1 1 28 28 ILE C C 13 177.443 0.05 . . . . . . . . . . 4568 1 153 . 1 1 28 28 ILE CA C 13 63.302 0.05 . . . . . . . . . . 4568 1 154 . 1 1 28 28 ILE CB C 13 38.010 0.05 . . . . . . . . . . 4568 1 155 . 1 1 28 28 ILE N N 15 119.476 0.05 . . . . . . . . . . 4568 1 156 . 1 1 29 29 LEU H H 1 7.688 0.02 . . . . . . . . . . 4568 1 157 . 1 1 29 29 LEU HA H 1 3.948 0.02 . . . . . . . . . . 4568 1 158 . 1 1 29 29 LEU C C 13 176.822 0.05 . . . . . . . . . . 4568 1 159 . 1 1 29 29 LEU CA C 13 57.246 0.05 . . . . . . . . . . 4568 1 160 . 1 1 29 29 LEU CB C 13 41.627 0.05 . . . . . . . . . . 4568 1 161 . 1 1 29 29 LEU N N 15 120.601 0.05 . . . . . . . . . . 4568 1 162 . 1 1 30 30 ILE H H 1 7.705 0.02 . . . . . . . . . . 4568 1 163 . 1 1 30 30 ILE HA H 1 3.755 0.02 . . . . . . . . . . 4568 1 164 . 1 1 30 30 ILE C C 13 178.139 0.05 . . . . . . . . . . 4568 1 165 . 1 1 30 30 ILE CA C 13 63.769 0.05 . . . . . . . . . . 4568 1 166 . 1 1 30 30 ILE CB C 13 37.612 0.05 . . . . . . . . . . 4568 1 167 . 1 1 30 30 ILE N N 15 117.600 0.05 . . . . . . . . . . 4568 1 168 . 1 1 31 31 ARG H H 1 7.618 0.02 . . . . . . . . . . 4568 1 169 . 1 1 31 31 ARG HA H 1 4.052 0.02 . . . . . . . . . . 4568 1 170 . 1 1 31 31 ARG C C 13 177.592 0.05 . . . . . . . . . . 4568 1 171 . 1 1 31 31 ARG CA C 13 58.628 0.05 . . . . . . . . . . 4568 1 172 . 1 1 31 31 ARG CB C 13 29.998 0.05 . . . . . . . . . . 4568 1 173 . 1 1 31 31 ARG N N 15 119.101 0.05 . . . . . . . . . . 4568 1 174 . 1 1 32 32 LEU H H 1 7.838 0.02 . . . . . . . . . . 4568 1 175 . 1 1 32 32 LEU HA H 1 4.051 0.02 . . . . . . . . . . 4568 1 176 . 1 1 32 32 LEU C C 13 178.306 0.05 . . . . . . . . . . 4568 1 177 . 1 1 32 32 LEU CA C 13 57.219 0.05 . . . . . . . . . . 4568 1 178 . 1 1 32 32 LEU CB C 13 42.090 0.05 . . . . . . . . . . 4568 1 179 . 1 1 32 32 LEU N N 15 120.226 0.05 . . . . . . . . . . 4568 1 180 . 1 1 33 33 PHE H H 1 7.903 0.02 . . . . . . . . . . 4568 1 181 . 1 1 33 33 PHE HA H 1 4.453 0.02 . . . . . . . . . . 4568 1 182 . 1 1 33 33 PHE C C 13 178.139 0.05 . . . . . . . . . . 4568 1 183 . 1 1 33 33 PHE CA C 13 58.332 0.05 . . . . . . . . . . 4568 1 184 . 1 1 33 33 PHE CB C 13 38.945 0.05 . . . . . . . . . . 4568 1 185 . 1 1 33 33 PHE N N 15 117.225 0.05 . . . . . . . . . . 4568 1 186 . 1 1 34 34 LYS H H 1 7.846 0.02 . . . . . . . . . . 4568 1 187 . 1 1 34 34 LYS HA H 1 4.153 0.02 . . . . . . . . . . 4568 1 188 . 1 1 34 34 LYS C C 13 176.571 0.05 . . . . . . . . . . 4568 1 189 . 1 1 34 34 LYS CA C 13 57.644 0.05 . . . . . . . . . . 4568 1 190 . 1 1 34 34 LYS CB C 13 32.708 0.05 . . . . . . . . . . 4568 1 191 . 1 1 34 34 LYS N N 15 118.726 0.05 . . . . . . . . . . 4568 1 192 . 1 1 35 35 SER H H 1 7.802 0.02 . . . . . . . . . . 4568 1 193 . 1 1 35 35 SER HA H 1 4.321 0.02 . . . . . . . . . . 4568 1 194 . 1 1 35 35 SER C C 13 176.980 0.05 . . . . . . . . . . 4568 1 195 . 1 1 35 35 SER CA C 13 59.072 0.05 . . . . . . . . . . 4568 1 196 . 1 1 35 35 SER CB C 13 63.857 0.05 . . . . . . . . . . 4568 1 197 . 1 1 35 35 SER N N 15 113.475 0.05 . . . . . . . . . . 4568 1 198 . 1 1 36 36 HIS H H 1 8.089 0.02 . . . . . . . . . . 4568 1 199 . 1 1 36 36 HIS HA H 1 5.018 0.02 . . . . . . . . . . 4568 1 200 . 1 1 36 36 HIS C C 13 173.838 0.05 . . . . . . . . . . 4568 1 201 . 1 1 36 36 HIS CA C 13 53.900 0.05 . . . . . . . . . . 4568 1 202 . 1 1 36 36 HIS N N 15 118.726 0.05 . . . . . . . . . . 4568 1 203 . 1 1 37 37 PRO CA C 13 64.359 0.05 . . . . . . . . . . 4568 1 204 . 1 1 37 37 PRO CB C 13 31.638 0.05 . . . . . . . . . . 4568 1 205 . 1 1 38 38 GLU H H 1 9.222 0.02 . . . . . . . . . . 4568 1 206 . 1 1 38 38 GLU HA H 1 4.257 0.02 . . . . . . . . . . 4568 1 207 . 1 1 38 38 GLU C C 13 177.400 0.05 . . . . . . . . . . 4568 1 208 . 1 1 38 38 GLU CA C 13 57.744 0.05 . . . . . . . . . . 4568 1 209 . 1 1 38 38 GLU CB C 13 28.621 0.05 . . . . . . . . . . 4568 1 210 . 1 1 38 38 GLU N N 15 120.976 0.05 . . . . . . . . . . 4568 1 211 . 1 1 39 39 THR H H 1 7.945 0.02 . . . . . . . . . . 4568 1 212 . 1 1 39 39 THR HA H 1 4.158 0.02 . . . . . . . . . . 4568 1 213 . 1 1 39 39 THR C C 13 177.226 0.05 . . . . . . . . . . 4568 1 214 . 1 1 39 39 THR CA C 13 63.376 0.05 . . . . . . . . . . 4568 1 215 . 1 1 39 39 THR CB C 13 69.440 0.05 . . . . . . . . . . 4568 1 216 . 1 1 39 39 THR N N 15 114.975 0.05 . . . . . . . . . . 4568 1 217 . 1 1 40 40 LEU H H 1 7.697 0.02 . . . . . . . . . . 4568 1 218 . 1 1 40 40 LEU HA H 1 4.182 0.02 . . . . . . . . . . 4568 1 219 . 1 1 40 40 LEU C C 13 174.984 0.05 . . . . . . . . . . 4568 1 220 . 1 1 40 40 LEU CA C 13 56.003 0.05 . . . . . . . . . . 4568 1 221 . 1 1 40 40 LEU CB C 13 42.251 0.05 . . . . . . . . . . 4568 1 222 . 1 1 40 40 LEU N N 15 122.476 0.05 . . . . . . . . . . 4568 1 223 . 1 1 41 41 GLU H H 1 7.911 0.02 . . . . . . . . . . 4568 1 224 . 1 1 41 41 GLU HA H 1 4.104 0.02 . . . . . . . . . . 4568 1 225 . 1 1 41 41 GLU C C 13 177.617 0.05 . . . . . . . . . . 4568 1 226 . 1 1 41 41 GLU CA C 13 57.434 0.05 . . . . . . . . . . 4568 1 227 . 1 1 41 41 GLU CB C 13 29.507 0.05 . . . . . . . . . . 4568 1 228 . 1 1 41 41 GLU N N 15 119.476 0.05 . . . . . . . . . . 4568 1 229 . 1 1 42 42 LYS H H 1 7.766 0.02 . . . . . . . . . . 4568 1 230 . 1 1 42 42 LYS HA H 1 4.110 0.02 . . . . . . . . . . 4568 1 231 . 1 1 42 42 LYS C C 13 176.853 0.05 . . . . . . . . . . 4568 1 232 . 1 1 42 42 LYS CA C 13 56.805 0.05 . . . . . . . . . . 4568 1 233 . 1 1 42 42 LYS CB C 13 32.633 0.05 . . . . . . . . . . 4568 1 234 . 1 1 42 42 LYS N N 15 119.476 0.05 . . . . . . . . . . 4568 1 235 . 1 1 43 43 PHE H H 1 7.850 0.02 . . . . . . . . . . 4568 1 236 . 1 1 43 43 PHE HA H 1 4.465 0.02 . . . . . . . . . . 4568 1 237 . 1 1 43 43 PHE C C 13 176.703 0.05 . . . . . . . . . . 4568 1 238 . 1 1 43 43 PHE CA C 13 58.202 0.05 . . . . . . . . . . 4568 1 239 . 1 1 43 43 PHE CB C 13 39.401 0.05 . . . . . . . . . . 4568 1 240 . 1 1 43 43 PHE N N 15 119.476 0.05 . . . . . . . . . . 4568 1 241 . 1 1 44 44 ASP H H 1 8.103 0.02 . . . . . . . . . . 4568 1 242 . 1 1 44 44 ASP HA H 1 4.467 0.02 . . . . . . . . . . 4568 1 243 . 1 1 44 44 ASP C C 13 175.822 0.05 . . . . . . . . . . 4568 1 244 . 1 1 44 44 ASP CA C 13 54.871 0.05 . . . . . . . . . . 4568 1 245 . 1 1 44 44 ASP CB C 13 40.965 0.05 . . . . . . . . . . 4568 1 246 . 1 1 44 44 ASP N N 15 121.351 0.05 . . . . . . . . . . 4568 1 247 . 1 1 45 45 ARG H H 1 7.937 0.02 . . . . . . . . . . 4568 1 248 . 1 1 45 45 ARG HA H 1 4.081 0.02 . . . . . . . . . . 4568 1 249 . 1 1 45 45 ARG C C 13 176.882 0.05 . . . . . . . . . . 4568 1 250 . 1 1 45 45 ARG CA C 13 57.335 0.05 . . . . . . . . . . 4568 1 251 . 1 1 45 45 ARG CB C 13 30.005 0.05 . . . . . . . . . . 4568 1 252 . 1 1 45 45 ARG N N 15 120.226 0.05 . . . . . . . . . . 4568 1 253 . 1 1 46 46 PHE H H 1 7.899 0.02 . . . . . . . . . . 4568 1 254 . 1 1 46 46 PHE HA H 1 4.470 0.02 . . . . . . . . . . 4568 1 255 . 1 1 46 46 PHE C C 13 176.748 0.05 . . . . . . . . . . 4568 1 256 . 1 1 46 46 PHE CA C 13 58.268 0.05 . . . . . . . . . . 4568 1 257 . 1 1 46 46 PHE CB C 13 38.925 0.05 . . . . . . . . . . 4568 1 258 . 1 1 46 46 PHE N N 15 118.350 0.05 . . . . . . . . . . 4568 1 259 . 1 1 47 47 LYS H H 1 7.809 0.02 . . . . . . . . . . 4568 1 260 . 1 1 47 47 LYS HA H 1 4.060 0.02 . . . . . . . . . . 4568 1 261 . 1 1 47 47 LYS C C 13 176.062 0.05 . . . . . . . . . . 4568 1 262 . 1 1 47 47 LYS CA C 13 57.283 0.05 . . . . . . . . . . 4568 1 263 . 1 1 47 47 LYS CB C 13 32.467 0.05 . . . . . . . . . . 4568 1 264 . 1 1 47 47 LYS N N 15 120.226 0.05 . . . . . . . . . . 4568 1 265 . 1 1 48 48 HIS H H 1 8.134 0.02 . . . . . . . . . . 4568 1 266 . 1 1 48 48 HIS HA H 1 4.641 0.02 . . . . . . . . . . 4568 1 267 . 1 1 48 48 HIS C C 13 176.619 0.05 . . . . . . . . . . 4568 1 268 . 1 1 48 48 HIS CA C 13 55.813 0.05 . . . . . . . . . . 4568 1 269 . 1 1 48 48 HIS CB C 13 28.972 0.05 . . . . . . . . . . 4568 1 270 . 1 1 48 48 HIS N N 15 118.350 0.05 . . . . . . . . . . 4568 1 271 . 1 1 49 49 LEU H H 1 7.972 0.02 . . . . . . . . . . 4568 1 272 . 1 1 49 49 LEU HA H 1 4.257 0.02 . . . . . . . . . . 4568 1 273 . 1 1 49 49 LEU C C 13 174.550 0.05 . . . . . . . . . . 4568 1 274 . 1 1 49 49 LEU CA C 13 55.653 0.05 . . . . . . . . . . 4568 1 275 . 1 1 49 49 LEU CB C 13 42.530 0.05 . . . . . . . . . . 4568 1 276 . 1 1 49 49 LEU N N 15 122.851 0.05 . . . . . . . . . . 4568 1 277 . 1 1 50 50 LYS H H 1 8.125 0.02 . . . . . . . . . . 4568 1 278 . 1 1 50 50 LYS HA H 1 4.259 0.02 . . . . . . . . . . 4568 1 279 . 1 1 50 50 LYS C C 13 177.310 0.05 . . . . . . . . . . 4568 1 280 . 1 1 50 50 LYS CA C 13 56.802 0.05 . . . . . . . . . . 4568 1 281 . 1 1 50 50 LYS CB C 13 33.008 0.05 . . . . . . . . . . 4568 1 282 . 1 1 50 50 LYS N N 15 121.726 0.05 . . . . . . . . . . 4568 1 283 . 1 1 51 51 THR H H 1 7.927 0.02 . . . . . . . . . . 4568 1 284 . 1 1 51 51 THR HA H 1 4.260 0.02 . . . . . . . . . . 4568 1 285 . 1 1 51 51 THR C C 13 176.948 0.05 . . . . . . . . . . 4568 1 286 . 1 1 51 51 THR CA C 13 62.379 0.05 . . . . . . . . . . 4568 1 287 . 1 1 51 51 THR CG2 C 13 69.944 0.05 . . . . . . . . . . 4568 1 288 . 1 1 51 51 THR N N 15 113.850 0.05 . . . . . . . . . . 4568 1 289 . 1 1 52 52 GLU H H 1 8.345 0.02 . . . . . . . . . . 4568 1 290 . 1 1 52 52 GLU HA H 1 4.156 0.02 . . . . . . . . . . 4568 1 291 . 1 1 52 52 GLU C C 13 175.264 0.05 . . . . . . . . . . 4568 1 292 . 1 1 52 52 GLU CA C 13 57.913 0.05 . . . . . . . . . . 4568 1 293 . 1 1 52 52 GLU CB C 13 29.493 0.05 . . . . . . . . . . 4568 1 294 . 1 1 52 52 GLU N N 15 122.101 0.05 . . . . . . . . . . 4568 1 295 . 1 1 53 53 ALA H H 1 8.075 0.02 . . . . . . . . . . 4568 1 296 . 1 1 53 53 ALA HA H 1 4.124 0.02 . . . . . . . . . . 4568 1 297 . 1 1 53 53 ALA C C 13 177.249 0.05 . . . . . . . . . . 4568 1 298 . 1 1 53 53 ALA CA C 13 53.843 0.05 . . . . . . . . . . 4568 1 299 . 1 1 53 53 ALA CB C 13 19.050 0.05 . . . . . . . . . . 4568 1 300 . 1 1 53 53 ALA N N 15 122.851 0.05 . . . . . . . . . . 4568 1 301 . 1 1 54 54 GLU H H 1 7.948 0.02 . . . . . . . . . . 4568 1 302 . 1 1 54 54 GLU HA H 1 4.110 0.02 . . . . . . . . . . 4568 1 303 . 1 1 54 54 GLU C C 13 178.977 0.05 . . . . . . . . . . 4568 1 304 . 1 1 54 54 GLU CA C 13 57.531 0.05 . . . . . . . . . . 4568 1 305 . 1 1 54 54 GLU CB C 13 29.754 0.05 . . . . . . . . . . 4568 1 306 . 1 1 54 54 GLU N N 15 118.726 0.05 . . . . . . . . . . 4568 1 307 . 1 1 55 55 MET H H 1 8.076 0.02 . . . . . . . . . . 4568 1 308 . 1 1 55 55 MET HA H 1 4.302 0.02 . . . . . . . . . . 4568 1 309 . 1 1 55 55 MET C C 13 177.631 0.05 . . . . . . . . . . 4568 1 310 . 1 1 55 55 MET CA C 13 56.778 0.05 . . . . . . . . . . 4568 1 311 . 1 1 55 55 MET CB C 13 32.622 0.05 . . . . . . . . . . 4568 1 312 . 1 1 55 55 MET N N 15 120.601 0.05 . . . . . . . . . . 4568 1 313 . 1 1 56 56 LYS H H 1 8.041 0.02 . . . . . . . . . . 4568 1 314 . 1 1 56 56 LYS HA H 1 4.163 0.02 . . . . . . . . . . 4568 1 315 . 1 1 56 56 LYS C C 13 177.201 0.05 . . . . . . . . . . 4568 1 316 . 1 1 56 56 LYS CA C 13 57.226 0.05 . . . . . . . . . . 4568 1 317 . 1 1 56 56 LYS CB C 13 32.796 0.05 . . . . . . . . . . 4568 1 318 . 1 1 56 56 LYS N N 15 120.976 0.05 . . . . . . . . . . 4568 1 319 . 1 1 57 57 ALA H H 1 7.971 0.02 . . . . . . . . . . 4568 1 320 . 1 1 57 57 ALA HA H 1 4.261 0.02 . . . . . . . . . . 4568 1 321 . 1 1 57 57 ALA C C 13 177.131 0.05 . . . . . . . . . . 4568 1 322 . 1 1 57 57 ALA CA C 13 53.453 0.05 . . . . . . . . . . 4568 1 323 . 1 1 57 57 ALA CB C 13 18.825 0.05 . . . . . . . . . . 4568 1 324 . 1 1 57 57 ALA N N 15 123.226 0.05 . . . . . . . . . . 4568 1 325 . 1 1 58 58 SER H H 1 7.942 0.02 . . . . . . . . . . 4568 1 326 . 1 1 58 58 SER HA H 1 4.258 0.02 . . . . . . . . . . 4568 1 327 . 1 1 58 58 SER C C 13 178.531 0.05 . . . . . . . . . . 4568 1 328 . 1 1 58 58 SER CA C 13 59.578 0.05 . . . . . . . . . . 4568 1 329 . 1 1 58 58 SER CB C 13 63.420 0.05 . . . . . . . . . . 4568 1 330 . 1 1 58 58 SER N N 15 113.850 0.05 . . . . . . . . . . 4568 1 331 . 1 1 59 59 GLU H H 1 8.096 0.02 . . . . . . . . . . 4568 1 332 . 1 1 59 59 GLU HA H 1 4.156 0.02 . . . . . . . . . . 4568 1 333 . 1 1 59 59 GLU C C 13 175.572 0.05 . . . . . . . . . . 4568 1 334 . 1 1 59 59 GLU CA C 13 57.659 0.05 . . . . . . . . . . 4568 1 335 . 1 1 59 59 GLU CB C 13 29.719 0.05 . . . . . . . . . . 4568 1 336 . 1 1 59 59 GLU N N 15 122.101 0.05 . . . . . . . . . . 4568 1 337 . 1 1 60 60 ASP H H 1 8.140 0.02 . . . . . . . . . . 4568 1 338 . 1 1 60 60 ASP HA H 1 4.468 0.02 . . . . . . . . . . 4568 1 339 . 1 1 60 60 ASP C C 13 177.131 0.05 . . . . . . . . . . 4568 1 340 . 1 1 60 60 ASP CA C 13 55.437 0.05 . . . . . . . . . . 4568 1 341 . 1 1 60 60 ASP CB C 13 40.791 0.05 . . . . . . . . . . 4568 1 342 . 1 1 60 60 ASP N N 15 120.226 0.05 . . . . . . . . . . 4568 1 343 . 1 1 61 61 LEU H H 1 7.894 0.02 . . . . . . . . . . 4568 1 344 . 1 1 61 61 LEU HA H 1 4.105 0.02 . . . . . . . . . . 4568 1 345 . 1 1 61 61 LEU C C 13 177.383 0.05 . . . . . . . . . . 4568 1 346 . 1 1 61 61 LEU CA C 13 56.798 0.05 . . . . . . . . . . 4568 1 347 . 1 1 61 61 LEU CB C 13 41.875 0.05 . . . . . . . . . . 4568 1 348 . 1 1 61 61 LEU N N 15 121.351 0.05 . . . . . . . . . . 4568 1 349 . 1 1 62 62 LYS H H 1 7.848 0.02 . . . . . . . . . . 4568 1 350 . 1 1 62 62 LYS HA H 1 4.109 0.02 . . . . . . . . . . 4568 1 351 . 1 1 62 62 LYS C C 13 178.363 0.05 . . . . . . . . . . 4568 1 352 . 1 1 62 62 LYS CA C 13 57.355 0.05 . . . . . . . . . . 4568 1 353 . 1 1 62 62 LYS CB C 13 32.257 0.05 . . . . . . . . . . 4568 1 354 . 1 1 62 62 LYS N N 15 119.101 0.05 . . . . . . . . . . 4568 1 355 . 1 1 63 63 LYS H H 1 7.790 0.02 . . . . . . . . . . 4568 1 356 . 1 1 63 63 LYS HA H 1 4.155 0.02 . . . . . . . . . . 4568 1 357 . 1 1 63 63 LYS C C 13 177.507 0.05 . . . . . . . . . . 4568 1 358 . 1 1 63 63 LYS CA C 13 57.079 0.05 . . . . . . . . . . 4568 1 359 . 1 1 63 63 LYS CB C 13 32.736 0.05 . . . . . . . . . . 4568 1 360 . 1 1 63 63 LYS N N 15 119.101 0.05 . . . . . . . . . . 4568 1 361 . 1 1 64 64 HIS H H 1 8.074 0.02 . . . . . . . . . . 4568 1 362 . 1 1 64 64 HIS HA H 1 4.661 0.02 . . . . . . . . . . 4568 1 363 . 1 1 64 64 HIS C C 13 176.848 0.05 . . . . . . . . . . 4568 1 364 . 1 1 64 64 HIS CA C 13 55.807 0.05 . . . . . . . . . . 4568 1 365 . 1 1 64 64 HIS CB C 13 29.167 0.05 . . . . . . . . . . 4568 1 366 . 1 1 64 64 HIS N N 15 117.600 0.05 . . . . . . . . . . 4568 1 367 . 1 1 65 65 GLY H H 1 8.186 0.02 . . . . . . . . . . 4568 1 368 . 1 1 65 65 GLY HA2 H 1 3.914 0.02 . . . . . . . . . . 4568 1 369 . 1 1 65 65 GLY C C 13 175.000 0.05 . . . . . . . . . . 4568 1 370 . 1 1 65 65 GLY CA C 13 45.783 0.05 . . . . . . . . . . 4568 1 371 . 1 1 65 65 GLY N N 15 109.349 0.05 . . . . . . . . . . 4568 1 372 . 1 1 66 66 VAL H H 1 7.901 0.02 . . . . . . . . . . 4568 1 373 . 1 1 66 66 VAL HA H 1 4.104 0.02 . . . . . . . . . . 4568 1 374 . 1 1 66 66 VAL C C 13 173.961 0.05 . . . . . . . . . . 4568 1 375 . 1 1 66 66 VAL CA C 13 62.815 0.05 . . . . . . . . . . 4568 1 376 . 1 1 66 66 VAL CB C 13 32.652 0.05 . . . . . . . . . . 4568 1 377 . 1 1 66 66 VAL N N 15 119.101 0.05 . . . . . . . . . . 4568 1 378 . 1 1 67 67 THR H H 1 8.047 0.02 . . . . . . . . . . 4568 1 379 . 1 1 67 67 THR HA H 1 4.297 0.02 . . . . . . . . . . 4568 1 380 . 1 1 67 67 THR C C 13 176.427 0.05 . . . . . . . . . . 4568 1 381 . 1 1 67 67 THR CA C 13 62.459 0.05 . . . . . . . . . . 4568 1 382 . 1 1 67 67 THR CB C 13 69.667 0.05 . . . . . . . . . . 4568 1 383 . 1 1 67 67 THR N N 15 117.975 0.05 . . . . . . . . . . 4568 1 384 . 1 1 68 68 VAL H H 1 7.968 0.02 . . . . . . . . . . 4568 1 385 . 1 1 68 68 VAL HA H 1 3.957 0.02 . . . . . . . . . . 4568 1 386 . 1 1 68 68 VAL C C 13 174.792 0.05 . . . . . . . . . . 4568 1 387 . 1 1 68 68 VAL CA C 13 63.273 0.05 . . . . . . . . . . 4568 1 388 . 1 1 68 68 VAL CB C 13 32.535 0.05 . . . . . . . . . . 4568 1 389 . 1 1 68 68 VAL N N 15 122.101 0.05 . . . . . . . . . . 4568 1 390 . 1 1 69 69 LEU H H 1 8.050 0.02 . . . . . . . . . . 4568 1 391 . 1 1 69 69 LEU HA H 1 4.243 0.02 . . . . . . . . . . 4568 1 392 . 1 1 69 69 LEU C C 13 176.102 0.05 . . . . . . . . . . 4568 1 393 . 1 1 69 69 LEU CA C 13 56.003 0.05 . . . . . . . . . . 4568 1 394 . 1 1 69 69 LEU CB C 13 42.176 0.05 . . . . . . . . . . 4568 1 395 . 1 1 69 69 LEU N N 15 123.602 0.05 . . . . . . . . . . 4568 1 396 . 1 1 70 70 THR H H 1 7.863 0.02 . . . . . . . . . . 4568 1 397 . 1 1 70 70 THR HA H 1 4.216 0.02 . . . . . . . . . . 4568 1 398 . 1 1 70 70 THR C C 13 178.081 0.05 . . . . . . . . . . 4568 1 399 . 1 1 70 70 THR CA C 13 62.896 0.05 . . . . . . . . . . 4568 1 400 . 1 1 70 70 THR CB C 13 69.460 0.05 . . . . . . . . . . 4568 1 401 . 1 1 70 70 THR N N 15 114.600 0.05 . . . . . . . . . . 4568 1 402 . 1 1 71 71 ALA H H 1 8.017 0.02 . . . . . . . . . . 4568 1 403 . 1 1 71 71 ALA HA H 1 4.241 0.02 . . . . . . . . . . 4568 1 404 . 1 1 71 71 ALA C C 13 175.117 0.05 . . . . . . . . . . 4568 1 405 . 1 1 71 71 ALA CA C 13 53.463 0.05 . . . . . . . . . . 4568 1 406 . 1 1 71 71 ALA CB C 13 18.712 0.05 . . . . . . . . . . 4568 1 407 . 1 1 71 71 ALA N N 15 125.477 0.05 . . . . . . . . . . 4568 1 408 . 1 1 72 72 LEU H H 1 7.955 0.02 . . . . . . . . . . 4568 1 409 . 1 1 72 72 LEU HA H 1 4.152 0.02 . . . . . . . . . . 4568 1 410 . 1 1 72 72 LEU C C 13 178.324 0.05 . . . . . . . . . . 4568 1 411 . 1 1 72 72 LEU CA C 13 56.313 0.05 . . . . . . . . . . 4568 1 412 . 1 1 72 72 LEU CB C 13 42.252 0.05 . . . . . . . . . . 4568 1 413 . 1 1 72 72 LEU N N 15 119.476 0.05 . . . . . . . . . . 4568 1 414 . 1 1 73 73 GLY H H 1 8.093 0.02 . . . . . . . . . . 4568 1 415 . 1 1 73 73 GLY HA2 H 1 3.841 0.02 . . . . . . . . . . 4568 1 416 . 1 1 73 73 GLY C C 13 178.242 0.05 . . . . . . . . . . 4568 1 417 . 1 1 73 73 GLY CA C 13 46.354 0.05 . . . . . . . . . . 4568 1 418 . 1 1 73 73 GLY N N 15 107.473 0.05 . . . . . . . . . . 4568 1 419 . 1 1 74 74 ALA H H 1 7.768 0.02 . . . . . . . . . . 4568 1 420 . 1 1 74 74 ALA HA H 1 4.195 0.02 . . . . . . . . . . 4568 1 421 . 1 1 74 74 ALA C C 13 174.617 0.05 . . . . . . . . . . 4568 1 422 . 1 1 74 74 ALA CA C 13 53.481 0.05 . . . . . . . . . . 4568 1 423 . 1 1 74 74 ALA CB C 13 18.958 0.05 . . . . . . . . . . 4568 1 424 . 1 1 74 74 ALA N N 15 122.851 0.05 . . . . . . . . . . 4568 1 425 . 1 1 75 75 ILE H H 1 7.687 0.02 . . . . . . . . . . 4568 1 426 . 1 1 75 75 ILE HA H 1 3.965 0.02 . . . . . . . . . . 4568 1 427 . 1 1 75 75 ILE C C 13 178.558 0.05 . . . . . . . . . . 4568 1 428 . 1 1 75 75 ILE CA C 13 62.287 0.05 . . . . . . . . . . 4568 1 429 . 1 1 75 75 ILE CB C 13 38.385 0.05 . . . . . . . . . . 4568 1 430 . 1 1 75 75 ILE N N 15 117.975 0.05 . . . . . . . . . . 4568 1 431 . 1 1 76 76 LEU H H 1 7.896 0.02 . . . . . . . . . . 4568 1 432 . 1 1 76 76 LEU HA H 1 4.204 0.02 . . . . . . . . . . 4568 1 433 . 1 1 76 76 LEU C C 13 176.822 0.05 . . . . . . . . . . 4568 1 434 . 1 1 76 76 LEU CA C 13 55.837 0.05 . . . . . . . . . . 4568 1 435 . 1 1 76 76 LEU CB C 13 42.008 0.05 . . . . . . . . . . 4568 1 436 . 1 1 76 76 LEU N N 15 122.851 0.05 . . . . . . . . . . 4568 1 437 . 1 1 77 77 LYS H H 1 7.809 0.02 . . . . . . . . . . 4568 1 438 . 1 1 77 77 LYS HA H 1 4.200 0.02 . . . . . . . . . . 4568 1 439 . 1 1 77 77 LYS C C 13 177.608 0.05 . . . . . . . . . . 4568 1 440 . 1 1 77 77 LYS CA C 13 56.754 0.05 . . . . . . . . . . 4568 1 441 . 1 1 77 77 LYS CB C 13 32.883 0.05 . . . . . . . . . . 4568 1 442 . 1 1 77 77 LYS N N 15 120.226 0.05 . . . . . . . . . . 4568 1 443 . 1 1 78 78 LYS H H 1 7.842 0.02 . . . . . . . . . . 4568 1 444 . 1 1 78 78 LYS HA H 1 4.210 0.02 . . . . . . . . . . 4568 1 445 . 1 1 78 78 LYS C C 13 176.666 0.05 . . . . . . . . . . 4568 1 446 . 1 1 78 78 LYS CA C 13 56.522 0.05 . . . . . . . . . . 4568 1 447 . 1 1 78 78 LYS CB C 13 32.969 0.05 . . . . . . . . . . 4568 1 448 . 1 1 78 78 LYS N N 15 120.976 0.05 . . . . . . . . . . 4568 1 449 . 1 1 79 79 LYS H H 1 8.064 0.02 . . . . . . . . . . 4568 1 450 . 1 1 79 79 LYS HA H 1 4.259 0.02 . . . . . . . . . . 4568 1 451 . 1 1 79 79 LYS C C 13 176.542 0.05 . . . . . . . . . . 4568 1 452 . 1 1 79 79 LYS CA C 13 56.442 0.05 . . . . . . . . . . 4568 1 453 . 1 1 79 79 LYS CB C 13 33.040 0.05 . . . . . . . . . . 4568 1 454 . 1 1 79 79 LYS N N 15 121.726 0.05 . . . . . . . . . . 4568 1 455 . 1 1 80 80 GLY H H 1 8.194 0.02 . . . . . . . . . . 4568 1 456 . 1 1 80 80 GLY HA2 H 1 3.904 0.02 . . . . . . . . . . 4568 1 457 . 1 1 80 80 GLY C C 13 176.923 0.05 . . . . . . . . . . 4568 1 458 . 1 1 80 80 GLY CA C 13 45.235 0.05 . . . . . . . . . . 4568 1 459 . 1 1 80 80 GLY N N 15 109.349 0.05 . . . . . . . . . . 4568 1 460 . 1 1 81 81 HIS H H 1 8.208 0.02 . . . . . . . . . . 4568 1 461 . 1 1 81 81 HIS HA H 1 4.529 0.02 . . . . . . . . . . 4568 1 462 . 1 1 81 81 HIS C C 13 173.661 0.05 . . . . . . . . . . 4568 1 463 . 1 1 81 81 HIS CA C 13 55.332 0.05 . . . . . . . . . . 4568 1 464 . 1 1 81 81 HIS CB C 13 29.347 0.05 . . . . . . . . . . 4568 1 465 . 1 1 81 81 HIS N N 15 118.350 0.05 . . . . . . . . . . 4568 1 466 . 1 1 82 82 HIS H H 1 8.460 0.02 . . . . . . . . . . 4568 1 467 . 1 1 82 82 HIS C C 13 174.340 0.05 . . . . . . . . . . 4568 1 468 . 1 1 82 82 HIS CA C 13 55.436 0.05 . . . . . . . . . . 4568 1 469 . 1 1 82 82 HIS CB C 13 29.232 0.05 . . . . . . . . . . 4568 1 470 . 1 1 82 82 HIS N N 15 120.226 0.05 . . . . . . . . . . 4568 1 471 . 1 1 83 83 GLU H H 1 8.527 0.02 . . . . . . . . . . 4568 1 472 . 1 1 83 83 GLU HA H 1 4.221 0.02 . . . . . . . . . . 4568 1 473 . 1 1 83 83 GLU C C 13 174.264 0.05 . . . . . . . . . . 4568 1 474 . 1 1 83 83 GLU CA C 13 56.825 0.05 . . . . . . . . . . 4568 1 475 . 1 1 83 83 GLU CB C 13 30.015 0.05 . . . . . . . . . . 4568 1 476 . 1 1 83 83 GLU N N 15 122.851 0.05 . . . . . . . . . . 4568 1 477 . 1 1 84 84 ALA H H 1 8.208 0.02 . . . . . . . . . . 4568 1 478 . 1 1 84 84 ALA HA H 1 4.241 0.02 . . . . . . . . . . 4568 1 479 . 1 1 84 84 ALA C C 13 175.999 0.05 . . . . . . . . . . 4568 1 480 . 1 1 84 84 ALA CA C 13 52.546 0.05 . . . . . . . . . . 4568 1 481 . 1 1 84 84 ALA CB C 13 19.332 0.05 . . . . . . . . . . 4568 1 482 . 1 1 84 84 ALA N N 15 124.352 0.05 . . . . . . . . . . 4568 1 483 . 1 1 85 85 GLU H H 1 8.081 0.02 . . . . . . . . . . 4568 1 484 . 1 1 85 85 GLU HA H 1 4.210 0.02 . . . . . . . . . . 4568 1 485 . 1 1 85 85 GLU C C 13 177.344 0.05 . . . . . . . . . . 4568 1 486 . 1 1 85 85 GLU CA C 13 56.262 0.05 . . . . . . . . . . 4568 1 487 . 1 1 85 85 GLU CB C 13 30.188 0.05 . . . . . . . . . . 4568 1 488 . 1 1 85 85 GLU N N 15 119.476 0.05 . . . . . . . . . . 4568 1 489 . 1 1 86 86 LEU H H 1 7.975 0.02 . . . . . . . . . . 4568 1 490 . 1 1 86 86 LEU HA H 1 4.289 0.02 . . . . . . . . . . 4568 1 491 . 1 1 86 86 LEU C C 13 175.969 0.05 . . . . . . . . . . 4568 1 492 . 1 1 86 86 LEU CA C 13 54.958 0.05 . . . . . . . . . . 4568 1 493 . 1 1 86 86 LEU CB C 13 42.530 0.05 . . . . . . . . . . 4568 1 494 . 1 1 86 86 LEU N N 15 123.226 0.05 . . . . . . . . . . 4568 1 495 . 1 1 87 87 LYS H H 1 8.008 0.02 . . . . . . . . . . 4568 1 496 . 1 1 87 87 LYS HA H 1 4.554 0.02 . . . . . . . . . . 4568 1 497 . 1 1 87 87 LYS C C 13 176.690 0.05 . . . . . . . . . . 4568 1 498 . 1 1 87 87 LYS CA C 13 54.180 0.05 . . . . . . . . . . 4568 1 499 . 1 1 87 87 LYS N N 15 122.851 0.05 . . . . . . . . . . 4568 1 500 . 1 1 88 88 PRO CA C 13 63.302 0.05 . . . . . . . . . . 4568 1 501 . 1 1 88 88 PRO CB C 13 31.881 0.05 . . . . . . . . . . 4568 1 502 . 1 1 89 89 LEU H H 1 8.041 0.02 . . . . . . . . . . 4568 1 503 . 1 1 89 89 LEU HA H 1 4.214 0.02 . . . . . . . . . . 4568 1 504 . 1 1 89 89 LEU C C 13 176.885 0.05 . . . . . . . . . . 4568 1 505 . 1 1 89 89 LEU CA C 13 55.331 0.05 . . . . . . . . . . 4568 1 506 . 1 1 89 89 LEU CB C 13 42.443 0.05 . . . . . . . . . . 4568 1 507 . 1 1 89 89 LEU N N 15 121.726 0.05 . . . . . . . . . . 4568 1 508 . 1 1 90 90 ALA H H 1 8.054 0.02 . . . . . . . . . . 4568 1 509 . 1 1 90 90 ALA HA H 1 4.225 0.02 . . . . . . . . . . 4568 1 510 . 1 1 90 90 ALA C C 13 177.263 0.05 . . . . . . . . . . 4568 1 511 . 1 1 90 90 ALA CA C 13 52.533 0.05 . . . . . . . . . . 4568 1 512 . 1 1 90 90 ALA CB C 13 19.209 0.05 . . . . . . . . . . 4568 1 513 . 1 1 90 90 ALA N N 15 124.352 0.05 . . . . . . . . . . 4568 1 514 . 1 1 91 91 GLN H H 1 8.083 0.02 . . . . . . . . . . 4568 1 515 . 1 1 91 91 GLN HA H 1 4.269 0.02 . . . . . . . . . . 4568 1 516 . 1 1 91 91 GLN C C 13 177.603 0.05 . . . . . . . . . . 4568 1 517 . 1 1 91 91 GLN CA C 13 55.834 0.05 . . . . . . . . . . 4568 1 518 . 1 1 91 91 GLN CB C 13 29.576 0.05 . . . . . . . . . . 4568 1 519 . 1 1 91 91 GLN N N 15 118.726 0.05 . . . . . . . . . . 4568 1 520 . 1 1 92 92 SER H H 1 8.069 0.02 . . . . . . . . . . 4568 1 521 . 1 1 92 92 SER HA H 1 4.324 0.02 . . . . . . . . . . 4568 1 522 . 1 1 92 92 SER C C 13 176.010 0.05 . . . . . . . . . . 4568 1 523 . 1 1 92 92 SER CA C 13 58.658 0.05 . . . . . . . . . . 4568 1 524 . 1 1 92 92 SER CB C 13 63.831 0.05 . . . . . . . . . . 4568 1 525 . 1 1 92 92 SER N N 15 116.475 0.05 . . . . . . . . . . 4568 1 526 . 1 1 93 93 HIS H H 1 8.336 0.02 . . . . . . . . . . 4568 1 527 . 1 1 93 93 HIS HA H 1 4.469 0.02 . . . . . . . . . . 4568 1 528 . 1 1 93 93 HIS C C 13 174.531 0.05 . . . . . . . . . . 4568 1 529 . 1 1 93 93 HIS CA C 13 55.306 0.05 . . . . . . . . . . 4568 1 530 . 1 1 93 93 HIS CB C 13 29.058 0.05 . . . . . . . . . . 4568 1 531 . 1 1 93 93 HIS N N 15 120.226 0.05 . . . . . . . . . . 4568 1 532 . 1 1 94 94 ALA H H 1 8.104 0.02 . . . . . . . . . . 4568 1 533 . 1 1 94 94 ALA HA H 1 4.345 0.02 . . . . . . . . . . 4568 1 534 . 1 1 94 94 ALA C C 13 174.073 0.05 . . . . . . . . . . 4568 1 535 . 1 1 94 94 ALA CA C 13 52.695 0.05 . . . . . . . . . . 4568 1 536 . 1 1 94 94 ALA CB C 13 19.106 0.05 . . . . . . . . . . 4568 1 537 . 1 1 94 94 ALA N N 15 124.727 0.05 . . . . . . . . . . 4568 1 538 . 1 1 95 95 THR H H 1 7.957 0.02 . . . . . . . . . . 4568 1 539 . 1 1 95 95 THR HA H 1 4.273 0.02 . . . . . . . . . . 4568 1 540 . 1 1 95 95 THR C C 13 177.558 0.05 . . . . . . . . . . 4568 1 541 . 1 1 95 95 THR CA C 13 61.687 0.05 . . . . . . . . . . 4568 1 542 . 1 1 95 95 THR CB C 13 69.880 0.05 . . . . . . . . . . 4568 1 543 . 1 1 95 95 THR N N 15 113.850 0.05 . . . . . . . . . . 4568 1 544 . 1 1 96 96 LYS H H 1 8.096 0.02 . . . . . . . . . . 4568 1 545 . 1 1 96 96 LYS HA H 1 4.261 0.02 . . . . . . . . . . 4568 1 546 . 1 1 96 96 LYS C C 13 174.323 0.05 . . . . . . . . . . 4568 1 547 . 1 1 96 96 LYS CA C 13 56.228 0.05 . . . . . . . . . . 4568 1 548 . 1 1 96 96 LYS CB C 13 33.159 0.05 . . . . . . . . . . 4568 1 549 . 1 1 96 96 LYS N N 15 123.226 0.05 . . . . . . . . . . 4568 1 550 . 1 1 97 97 HIS H H 1 8.269 0.02 . . . . . . . . . . 4568 1 551 . 1 1 97 97 HIS HA H 1 4.921 0.02 . . . . . . . . . . 4568 1 552 . 1 1 97 97 HIS C C 13 176.051 0.05 . . . . . . . . . . 4568 1 553 . 1 1 97 97 HIS CA C 13 54.965 0.05 . . . . . . . . . . 4568 1 554 . 1 1 97 97 HIS CB C 13 29.667 0.05 . . . . . . . . . . 4568 1 555 . 1 1 97 97 HIS N N 15 119.476 0.05 . . . . . . . . . . 4568 1 556 . 1 1 98 98 LYS H H 1 8.249 0.02 . . . . . . . . . . 4568 1 557 . 1 1 98 98 LYS HA H 1 4.325 0.02 . . . . . . . . . . 4568 1 558 . 1 1 98 98 LYS C C 13 174.058 0.05 . . . . . . . . . . 4568 1 559 . 1 1 98 98 LYS CA C 13 56.307 0.05 . . . . . . . . . . 4568 1 560 . 1 1 98 98 LYS CB C 13 33.230 0.05 . . . . . . . . . . 4568 1 561 . 1 1 98 98 LYS N N 15 122.851 0.05 . . . . . . . . . . 4568 1 562 . 1 1 99 99 ILE H H 1 8.075 0.02 . . . . . . . . . . 4568 1 563 . 1 1 99 99 ILE C C 13 175.867 0.05 . . . . . . . . . . 4568 1 564 . 1 1 99 99 ILE CA C 13 58.470 0.05 . . . . . . . . . . 4568 1 565 . 1 1 99 99 ILE N N 15 123.226 0.05 . . . . . . . . . . 4568 1 566 . 1 1 100 100 PRO CA C 13 62.902 0.05 . . . . . . . . . . 4568 1 567 . 1 1 100 100 PRO CB C 13 31.774 0.05 . . . . . . . . . . 4568 1 568 . 1 1 101 101 ILE H H 1 8.112 0.02 . . . . . . . . . . 4568 1 569 . 1 1 101 101 ILE HA H 1 3.869 0.02 . . . . . . . . . . 4568 1 570 . 1 1 101 101 ILE C C 13 177.278 0.05 . . . . . . . . . . 4568 1 571 . 1 1 101 101 ILE CA C 13 62.873 0.05 . . . . . . . . . . 4568 1 572 . 1 1 101 101 ILE CB C 13 38.358 0.05 . . . . . . . . . . 4568 1 573 . 1 1 101 101 ILE N N 15 123.226 0.05 . . . . . . . . . . 4568 1 574 . 1 1 102 102 LYS H H 1 8.277 0.02 . . . . . . . . . . 4568 1 575 . 1 1 102 102 LYS HA H 1 4.117 0.02 . . . . . . . . . . 4568 1 576 . 1 1 102 102 LYS C C 13 176.975 0.05 . . . . . . . . . . 4568 1 577 . 1 1 102 102 LYS CA C 13 58.107 0.05 . . . . . . . . . . 4568 1 578 . 1 1 102 102 LYS CB C 13 32.107 0.05 . . . . . . . . . . 4568 1 579 . 1 1 102 102 LYS N N 15 121.351 0.05 . . . . . . . . . . 4568 1 580 . 1 1 103 103 TYR H H 1 7.596 0.02 . . . . . . . . . . 4568 1 581 . 1 1 103 103 TYR HA H 1 4.390 0.02 . . . . . . . . . . 4568 1 582 . 1 1 103 103 TYR C C 13 177.885 0.05 . . . . . . . . . . 4568 1 583 . 1 1 103 103 TYR CA C 13 59.760 0.05 . . . . . . . . . . 4568 1 584 . 1 1 103 103 TYR CB C 13 38.194 0.05 . . . . . . . . . . 4568 1 585 . 1 1 103 103 TYR N N 15 118.726 0.05 . . . . . . . . . . 4568 1 586 . 1 1 104 104 LEU H H 1 7.682 0.02 . . . . . . . . . . 4568 1 587 . 1 1 104 104 LEU HA H 1 3.953 0.02 . . . . . . . . . . 4568 1 588 . 1 1 104 104 LEU C C 13 176.850 0.05 . . . . . . . . . . 4568 1 589 . 1 1 104 104 LEU CA C 13 57.300 0.05 . . . . . . . . . . 4568 1 590 . 1 1 104 104 LEU CB C 13 41.495 0.05 . . . . . . . . . . 4568 1 591 . 1 1 104 104 LEU N N 15 119.476 0.05 . . . . . . . . . . 4568 1 592 . 1 1 105 105 GLU H H 1 8.195 0.02 . . . . . . . . . . 4568 1 593 . 1 1 105 105 GLU HA H 1 3.962 0.02 . . . . . . . . . . 4568 1 594 . 1 1 105 105 GLU C C 13 179.084 0.05 . . . . . . . . . . 4568 1 595 . 1 1 105 105 GLU CA C 13 59.009 0.05 . . . . . . . . . . 4568 1 596 . 1 1 105 105 GLU CB C 13 29.101 0.05 . . . . . . . . . . 4568 1 597 . 1 1 105 105 GLU N N 15 120.226 0.05 . . . . . . . . . . 4568 1 598 . 1 1 106 106 PHE H H 1 7.744 0.02 . . . . . . . . . . 4568 1 599 . 1 1 106 106 PHE HA H 1 4.309 0.02 . . . . . . . . . . 4568 1 600 . 1 1 106 106 PHE C C 13 177.636 0.05 . . . . . . . . . . 4568 1 601 . 1 1 106 106 PHE CA C 13 60.061 0.05 . . . . . . . . . . 4568 1 602 . 1 1 106 106 PHE CB C 13 38.870 0.05 . . . . . . . . . . 4568 1 603 . 1 1 106 106 PHE N N 15 119.476 0.05 . . . . . . . . . . 4568 1 604 . 1 1 107 107 ILE H H 1 7.994 0.02 . . . . . . . . . . 4568 1 605 . 1 1 107 107 ILE HA H 1 3.573 0.02 . . . . . . . . . . 4568 1 606 . 1 1 107 107 ILE C C 13 177.357 0.05 . . . . . . . . . . 4568 1 607 . 1 1 107 107 ILE CA C 13 63.568 0.05 . . . . . . . . . . 4568 1 608 . 1 1 107 107 ILE CB C 13 37.692 0.05 . . . . . . . . . . 4568 1 609 . 1 1 107 107 ILE N N 15 119.101 0.05 . . . . . . . . . . 4568 1 610 . 1 1 108 108 SER H H 1 7.925 0.02 . . . . . . . . . . 4568 1 611 . 1 1 108 108 SER HA H 1 3.982 0.02 . . . . . . . . . . 4568 1 612 . 1 1 108 108 SER C C 13 176.980 0.05 . . . . . . . . . . 4568 1 613 . 1 1 108 108 SER CA C 13 61.932 0.05 . . . . . . . . . . 4568 1 614 . 1 1 108 108 SER CB C 13 62.945 0.05 . . . . . . . . . . 4568 1 615 . 1 1 108 108 SER N N 15 116.100 0.05 . . . . . . . . . . 4568 1 616 . 1 1 109 109 GLU H H 1 7.923 0.02 . . . . . . . . . . 4568 1 617 . 1 1 109 109 GLU HA H 1 3.904 0.02 . . . . . . . . . . 4568 1 618 . 1 1 109 109 GLU C C 13 175.598 0.05 . . . . . . . . . . 4568 1 619 . 1 1 109 109 GLU CA C 13 58.695 0.05 . . . . . . . . . . 4568 1 620 . 1 1 109 109 GLU CB C 13 28.798 0.05 . . . . . . . . . . 4568 1 621 . 1 1 109 109 GLU N N 15 120.226 0.05 . . . . . . . . . . 4568 1 622 . 1 1 110 110 ALA H H 1 7.880 0.02 . . . . . . . . . . 4568 1 623 . 1 1 110 110 ALA HA H 1 3.966 0.02 . . . . . . . . . . 4568 1 624 . 1 1 110 110 ALA C C 13 178.042 0.05 . . . . . . . . . . 4568 1 625 . 1 1 110 110 ALA CA C 13 54.901 0.05 . . . . . . . . . . 4568 1 626 . 1 1 110 110 ALA CB C 13 18.217 0.05 . . . . . . . . . . 4568 1 627 . 1 1 110 110 ALA N N 15 122.476 0.05 . . . . . . . . . . 4568 1 628 . 1 1 111 111 ILE H H 1 7.889 0.02 . . . . . . . . . . 4568 1 629 . 1 1 111 111 ILE HA H 1 3.601 0.02 . . . . . . . . . . 4568 1 630 . 1 1 111 111 ILE C C 13 179.510 0.05 . . . . . . . . . . 4568 1 631 . 1 1 111 111 ILE CA C 13 64.220 0.05 . . . . . . . . . . 4568 1 632 . 1 1 111 111 ILE CB C 13 38.002 0.05 . . . . . . . . . . 4568 1 633 . 1 1 111 111 ILE N N 15 117.225 0.05 . . . . . . . . . . 4568 1 634 . 1 1 112 112 ILE H H 1 7.816 0.02 . . . . . . . . . . 4568 1 635 . 1 1 112 112 ILE HA H 1 3.596 0.02 . . . . . . . . . . 4568 1 636 . 1 1 112 112 ILE C C 13 177.330 0.05 . . . . . . . . . . 4568 1 637 . 1 1 112 112 ILE CA C 13 64.111 0.05 . . . . . . . . . . 4568 1 638 . 1 1 112 112 ILE CB C 13 37.370 0.05 . . . . . . . . . . 4568 1 639 . 1 1 112 112 ILE N N 15 119.851 0.05 . . . . . . . . . . 4568 1 640 . 1 1 113 113 HIS H H 1 7.990 0.02 . . . . . . . . . . 4568 1 641 . 1 1 113 113 HIS HA H 1 4.366 0.02 . . . . . . . . . . 4568 1 642 . 1 1 113 113 HIS C C 13 177.670 0.05 . . . . . . . . . . 4568 1 643 . 1 1 113 113 HIS CA C 13 58.050 0.05 . . . . . . . . . . 4568 1 644 . 1 1 113 113 HIS N N 15 117.600 0.05 . . . . . . . . . . 4568 1 645 . 1 1 114 114 VAL H H 1 7.874 0.02 . . . . . . . . . . 4568 1 646 . 1 1 114 114 VAL CA C 13 65.265 0.05 . . . . . . . . . . 4568 1 647 . 1 1 114 114 VAL CB C 13 31.881 0.05 . . . . . . . . . . 4568 1 648 . 1 1 114 114 VAL N N 15 120.000 0.05 . . . . . . . . . . 4568 1 649 . 1 1 115 115 LEU H H 1 8.047 0.02 . . . . . . . . . . 4568 1 650 . 1 1 115 115 LEU HA H 1 4.056 0.02 . . . . . . . . . . 4568 1 651 . 1 1 115 115 LEU C C 13 177.207 0.05 . . . . . . . . . . 4568 1 652 . 1 1 115 115 LEU CA C 13 56.693 0.05 . . . . . . . . . . 4568 1 653 . 1 1 115 115 LEU CB C 13 41.893 0.05 . . . . . . . . . . 4568 1 654 . 1 1 115 115 LEU N N 15 120.601 0.05 . . . . . . . . . . 4568 1 655 . 1 1 116 116 HIS H H 1 7.978 0.02 . . . . . . . . . . 4568 1 656 . 1 1 116 116 HIS HA H 1 4.576 0.02 . . . . . . . . . . 4568 1 657 . 1 1 116 116 HIS C C 13 178.075 0.05 . . . . . . . . . . 4568 1 658 . 1 1 116 116 HIS CA C 13 55.929 0.05 . . . . . . . . . . 4568 1 659 . 1 1 116 116 HIS CB C 13 28.717 0.05 . . . . . . . . . . 4568 1 660 . 1 1 116 116 HIS N N 15 116.100 0.05 . . . . . . . . . . 4568 1 661 . 1 1 117 117 SER H H 1 7.727 0.02 . . . . . . . . . . 4568 1 662 . 1 1 117 117 SER HA H 1 4.358 0.02 . . . . . . . . . . 4568 1 663 . 1 1 117 117 SER C C 13 174.706 0.05 . . . . . . . . . . 4568 1 664 . 1 1 117 117 SER CA C 13 59.038 0.05 . . . . . . . . . . 4568 1 665 . 1 1 117 117 SER CB C 13 63.857 0.05 . . . . . . . . . . 4568 1 666 . 1 1 117 117 SER N N 15 114.975 0.05 . . . . . . . . . . 4568 1 667 . 1 1 118 118 ARG H H 1 7.973 0.02 . . . . . . . . . . 4568 1 668 . 1 1 118 118 ARG HA H 1 4.253 0.02 . . . . . . . . . . 4568 1 669 . 1 1 118 118 ARG C C 13 174.235 0.05 . . . . . . . . . . 4568 1 670 . 1 1 118 118 ARG CA C 13 56.003 0.05 . . . . . . . . . . 4568 1 671 . 1 1 118 118 ARG CB C 13 30.904 0.05 . . . . . . . . . . 4568 1 672 . 1 1 118 118 ARG N N 15 120.976 0.05 . . . . . . . . . . 4568 1 673 . 1 1 119 119 HIS H H 1 8.234 0.02 . . . . . . . . . . 4568 1 674 . 1 1 119 119 HIS HA H 1 4.923 0.02 . . . . . . . . . . 4568 1 675 . 1 1 119 119 HIS C C 13 175.645 0.05 . . . . . . . . . . 4568 1 676 . 1 1 119 119 HIS CA C 13 53.290 0.05 . . . . . . . . . . 4568 1 677 . 1 1 119 119 HIS N N 15 119.101 0.05 . . . . . . . . . . 4568 1 678 . 1 1 120 120 PRO CA C 13 63.847 0.05 . . . . . . . . . . 4568 1 679 . 1 1 120 120 PRO CB C 13 31.784 0.05 . . . . . . . . . . 4568 1 680 . 1 1 121 121 GLY H H 1 8.369 0.02 . . . . . . . . . . 4568 1 681 . 1 1 121 121 GLY HA2 H 1 3.878 0.02 . . . . . . . . . . 4568 1 682 . 1 1 121 121 GLY C C 13 177.410 0.05 . . . . . . . . . . 4568 1 683 . 1 1 121 121 GLY CA C 13 45.482 0.05 . . . . . . . . . . 4568 1 684 . 1 1 121 121 GLY N N 15 108.974 0.05 . . . . . . . . . . 4568 1 685 . 1 1 122 122 ASP H H 1 7.856 0.02 . . . . . . . . . . 4568 1 686 . 1 1 122 122 ASP HA H 1 4.557 0.02 . . . . . . . . . . 4568 1 687 . 1 1 122 122 ASP C C 13 173.989 0.05 . . . . . . . . . . 4568 1 688 . 1 1 122 122 ASP CA C 13 54.404 0.05 . . . . . . . . . . 4568 1 689 . 1 1 122 122 ASP CB C 13 40.994 0.05 . . . . . . . . . . 4568 1 690 . 1 1 122 122 ASP N N 15 119.851 0.05 . . . . . . . . . . 4568 1 691 . 1 1 123 123 PHE H H 1 8.066 0.02 . . . . . . . . . . 4568 1 692 . 1 1 123 123 PHE HA H 1 4.515 0.02 . . . . . . . . . . 4568 1 693 . 1 1 123 123 PHE C C 13 175.923 0.05 . . . . . . . . . . 4568 1 694 . 1 1 123 123 PHE CA C 13 57.710 0.05 . . . . . . . . . . 4568 1 695 . 1 1 123 123 PHE CB C 13 39.426 0.05 . . . . . . . . . . 4568 1 696 . 1 1 123 123 PHE N N 15 120.226 0.05 . . . . . . . . . . 4568 1 697 . 1 1 124 124 GLY H H 1 8.137 0.02 . . . . . . . . . . 4568 1 698 . 1 1 124 124 GLY HA2 H 1 3.909 0.02 . . . . . . . . . . 4568 1 699 . 1 1 124 124 GLY C C 13 176.062 0.05 . . . . . . . . . . 4568 1 700 . 1 1 124 124 GLY CA C 13 45.311 0.05 . . . . . . . . . . 4568 1 701 . 1 1 124 124 GLY N N 15 109.349 0.05 . . . . . . . . . . 4568 1 702 . 1 1 125 125 ALA H H 1 8.071 0.02 . . . . . . . . . . 4568 1 703 . 1 1 125 125 ALA HA H 1 4.201 0.02 . . . . . . . . . . 4568 1 704 . 1 1 125 125 ALA C C 13 174.075 0.05 . . . . . . . . . . 4568 1 705 . 1 1 125 125 ALA CA C 13 53.432 0.05 . . . . . . . . . . 4568 1 706 . 1 1 125 125 ALA CB C 13 19.108 0.05 . . . . . . . . . . 4568 1 707 . 1 1 125 125 ALA N N 15 123.226 0.05 . . . . . . . . . . 4568 1 708 . 1 1 126 126 ASP H H 1 8.198 0.02 . . . . . . . . . . 4568 1 709 . 1 1 126 126 ASP HA H 1 4.541 0.02 . . . . . . . . . . 4568 1 710 . 1 1 126 126 ASP C C 13 178.010 0.05 . . . . . . . . . . 4568 1 711 . 1 1 126 126 ASP CA C 13 54.426 0.05 . . . . . . . . . . 4568 1 712 . 1 1 126 126 ASP CB C 13 40.531 0.05 . . . . . . . . . . 4568 1 713 . 1 1 126 126 ASP N N 15 117.975 0.05 . . . . . . . . . . 4568 1 714 . 1 1 127 127 ALA H H 1 8.046 0.02 . . . . . . . . . . 4568 1 715 . 1 1 127 127 ALA HA H 1 4.113 0.02 . . . . . . . . . . 4568 1 716 . 1 1 127 127 ALA C C 13 176.514 0.05 . . . . . . . . . . 4568 1 717 . 1 1 127 127 ALA CA C 13 53.936 0.05 . . . . . . . . . . 4568 1 718 . 1 1 127 127 ALA CB C 13 18.856 0.05 . . . . . . . . . . 4568 1 719 . 1 1 127 127 ALA N N 15 124.352 0.05 . . . . . . . . . . 4568 1 720 . 1 1 128 128 GLN H H 1 8.178 0.02 . . . . . . . . . . 4568 1 721 . 1 1 128 128 GLN HA H 1 4.054 0.02 . . . . . . . . . . 4568 1 722 . 1 1 128 128 GLN C C 13 178.513 0.05 . . . . . . . . . . 4568 1 723 . 1 1 128 128 GLN CA C 13 57.707 0.05 . . . . . . . . . . 4568 1 724 . 1 1 128 128 GLN CB C 13 28.748 0.05 . . . . . . . . . . 4568 1 725 . 1 1 128 128 GLN N N 15 117.600 0.05 . . . . . . . . . . 4568 1 726 . 1 1 129 129 GLY H H 1 8.219 0.02 . . . . . . . . . . 4568 1 727 . 1 1 129 129 GLY HA2 H 1 3.898 0.02 . . . . . . . . . . 4568 1 728 . 1 1 129 129 GLY C C 13 177.640 0.05 . . . . . . . . . . 4568 1 729 . 1 1 129 129 GLY CA C 13 46.528 0.05 . . . . . . . . . . 4568 1 730 . 1 1 129 129 GLY N N 15 108.599 0.05 . . . . . . . . . . 4568 1 731 . 1 1 130 130 ALA H H 1 7.988 0.02 . . . . . . . . . . 4568 1 732 . 1 1 130 130 ALA HA H 1 4.110 0.02 . . . . . . . . . . 4568 1 733 . 1 1 130 130 ALA C C 13 175.514 0.05 . . . . . . . . . . 4568 1 734 . 1 1 130 130 ALA CA C 13 54.356 0.05 . . . . . . . . . . 4568 1 735 . 1 1 130 130 ALA CB C 13 18.958 0.05 . . . . . . . . . . 4568 1 736 . 1 1 130 130 ALA N N 15 123.977 0.05 . . . . . . . . . . 4568 1 737 . 1 1 131 131 MET H H 1 8.148 0.02 . . . . . . . . . . 4568 1 738 . 1 1 131 131 MET HA H 1 4.156 0.02 . . . . . . . . . . 4568 1 739 . 1 1 131 131 MET C C 13 179.268 0.05 . . . . . . . . . . 4568 1 740 . 1 1 131 131 MET CA C 13 57.025 0.05 . . . . . . . . . . 4568 1 741 . 1 1 131 131 MET CB C 13 32.571 0.05 . . . . . . . . . . 4568 1 742 . 1 1 131 131 MET N N 15 117.975 0.05 . . . . . . . . . . 4568 1 743 . 1 1 132 132 ASN H H 1 8.132 0.02 . . . . . . . . . . 4568 1 744 . 1 1 132 132 ASN HA H 1 4.463 0.02 . . . . . . . . . . 4568 1 745 . 1 1 132 132 ASN C C 13 177.231 0.05 . . . . . . . . . . 4568 1 746 . 1 1 132 132 ASN CA C 13 55.479 0.05 . . . . . . . . . . 4568 1 747 . 1 1 132 132 ASN CB C 13 38.184 0.05 . . . . . . . . . . 4568 1 748 . 1 1 132 132 ASN N N 15 118.350 0.05 . . . . . . . . . . 4568 1 749 . 1 1 133 133 LYS H H 1 7.948 0.02 . . . . . . . . . . 4568 1 750 . 1 1 133 133 LYS HA H 1 4.028 0.02 . . . . . . . . . . 4568 1 751 . 1 1 133 133 LYS C C 13 177.392 0.05 . . . . . . . . . . 4568 1 752 . 1 1 133 133 LYS CA C 13 58.608 0.05 . . . . . . . . . . 4568 1 753 . 1 1 133 133 LYS CB C 13 32.101 0.05 . . . . . . . . . . 4568 1 754 . 1 1 133 133 LYS N N 15 120.601 0.05 . . . . . . . . . . 4568 1 755 . 1 1 134 134 ALA H H 1 7.984 0.02 . . . . . . . . . . 4568 1 756 . 1 1 134 134 ALA HA H 1 3.982 0.02 . . . . . . . . . . 4568 1 757 . 1 1 134 134 ALA C C 13 178.122 0.05 . . . . . . . . . . 4568 1 758 . 1 1 134 134 ALA CA C 13 54.901 0.05 . . . . . . . . . . 4568 1 759 . 1 1 134 134 ALA CB C 13 18.310 0.05 . . . . . . . . . . 4568 1 760 . 1 1 134 134 ALA N N 15 122.101 0.05 . . . . . . . . . . 4568 1 761 . 1 1 135 135 LEU H H 1 8.034 0.02 . . . . . . . . . . 4568 1 762 . 1 1 135 135 LEU HA H 1 4.080 0.02 . . . . . . . . . . 4568 1 763 . 1 1 135 135 LEU C C 13 179.135 0.05 . . . . . . . . . . 4568 1 764 . 1 1 135 135 LEU CA C 13 57.390 0.05 . . . . . . . . . . 4568 1 765 . 1 1 135 135 LEU N N 15 117.975 0.05 . . . . . . . . . . 4568 1 766 . 1 1 136 136 GLU H H 1 7.850 0.02 . . . . . . . . . . 4568 1 767 . 1 1 136 136 GLU C C 13 178.658 0.05 . . . . . . . . . . 4568 1 768 . 1 1 136 136 GLU N N 15 119.476 0.05 . . . . . . . . . . 4568 1 769 . 1 1 137 137 LEU H H 1 7.828 0.02 . . . . . . . . . . 4568 1 770 . 1 1 137 137 LEU C C 13 178.395 0.05 . . . . . . . . . . 4568 1 771 . 1 1 137 137 LEU CA C 13 57.303 0.05 . . . . . . . . . . 4568 1 772 . 1 1 137 137 LEU CB C 13 41.650 0.05 . . . . . . . . . . 4568 1 773 . 1 1 137 137 LEU N N 15 119.851 0.05 . . . . . . . . . . 4568 1 774 . 1 1 138 138 PHE H H 1 8.069 0.02 . . . . . . . . . . 4568 1 775 . 1 1 138 138 PHE C C 13 178.594 0.05 . . . . . . . . . . 4568 1 776 . 1 1 138 138 PHE CA C 13 59.760 0.05 . . . . . . . . . . 4568 1 777 . 1 1 138 138 PHE CB C 13 39.321 0.05 . . . . . . . . . . 4568 1 778 . 1 1 138 138 PHE N N 15 119.101 0.05 . . . . . . . . . . 4568 1 779 . 1 1 139 139 ARG H H 1 8.142 0.02 . . . . . . . . . . 4568 1 780 . 1 1 139 139 ARG HA H 1 3.832 0.02 . . . . . . . . . . 4568 1 781 . 1 1 139 139 ARG C C 13 176.748 0.05 . . . . . . . . . . 4568 1 782 . 1 1 139 139 ARG CA C 13 59.159 0.05 . . . . . . . . . . 4568 1 783 . 1 1 139 139 ARG CB C 13 30.529 0.05 . . . . . . . . . . 4568 1 784 . 1 1 139 139 ARG N N 15 119.101 0.05 . . . . . . . . . . 4568 1 785 . 1 1 140 140 LYS H H 1 7.958 0.02 . . . . . . . . . . 4568 1 786 . 1 1 140 140 LYS HA H 1 4.054 0.02 . . . . . . . . . . 4568 1 787 . 1 1 140 140 LYS C C 13 177.930 0.05 . . . . . . . . . . 4568 1 788 . 1 1 140 140 LYS CA C 13 58.107 0.05 . . . . . . . . . . 4568 1 789 . 1 1 140 140 LYS CB C 13 32.482 0.05 . . . . . . . . . . 4568 1 790 . 1 1 140 140 LYS N N 15 119.476 0.05 . . . . . . . . . . 4568 1 791 . 1 1 141 141 ASP H H 1 8.092 0.02 . . . . . . . . . . 4568 1 792 . 1 1 141 141 ASP HA H 1 4.210 0.02 . . . . . . . . . . 4568 1 793 . 1 1 141 141 ASP C C 13 178.004 0.05 . . . . . . . . . . 4568 1 794 . 1 1 141 141 ASP CA C 13 56.007 0.05 . . . . . . . . . . 4568 1 795 . 1 1 141 141 ASP CB C 13 40.384 0.05 . . . . . . . . . . 4568 1 796 . 1 1 141 141 ASP N N 15 119.851 0.05 . . . . . . . . . . 4568 1 797 . 1 1 142 142 ILE H H 1 7.908 0.02 . . . . . . . . . . 4568 1 798 . 1 1 142 142 ILE HA H 1 3.791 0.02 . . . . . . . . . . 4568 1 799 . 1 1 142 142 ILE C C 13 177.629 0.05 . . . . . . . . . . 4568 1 800 . 1 1 142 142 ILE CA C 13 62.865 0.05 . . . . . . . . . . 4568 1 801 . 1 1 142 142 ILE CB C 13 37.452 0.05 . . . . . . . . . . 4568 1 802 . 1 1 142 142 ILE N N 15 119.101 0.05 . . . . . . . . . . 4568 1 803 . 1 1 143 143 ALA H H 1 7.838 0.02 . . . . . . . . . . 4568 1 804 . 1 1 143 143 ALA HA H 1 4.005 0.02 . . . . . . . . . . 4568 1 805 . 1 1 143 143 ALA C C 13 176.969 0.05 . . . . . . . . . . 4568 1 806 . 1 1 143 143 ALA CA C 13 54.425 0.05 . . . . . . . . . . 4568 1 807 . 1 1 143 143 ALA CB C 13 18.505 0.05 . . . . . . . . . . 4568 1 808 . 1 1 143 143 ALA N N 15 122.851 0.05 . . . . . . . . . . 4568 1 809 . 1 1 144 144 ALA H H 1 7.672 0.02 . . . . . . . . . . 4568 1 810 . 1 1 144 144 ALA HA H 1 4.111 0.02 . . . . . . . . . . 4568 1 811 . 1 1 144 144 ALA C C 13 179.157 0.05 . . . . . . . . . . 4568 1 812 . 1 1 144 144 ALA CA C 13 53.978 0.05 . . . . . . . . . . 4568 1 813 . 1 1 144 144 ALA CB C 13 18.680 0.05 . . . . . . . . . . 4568 1 814 . 1 1 144 144 ALA N N 15 119.476 0.05 . . . . . . . . . . 4568 1 815 . 1 1 145 145 LYS H H 1 7.732 0.02 . . . . . . . . . . 4568 1 816 . 1 1 145 145 LYS HA H 1 4.107 0.02 . . . . . . . . . . 4568 1 817 . 1 1 145 145 LYS C C 13 179.209 0.05 . . . . . . . . . . 4568 1 818 . 1 1 145 145 LYS CA C 13 57.270 0.05 . . . . . . . . . . 4568 1 819 . 1 1 145 145 LYS CB C 13 32.369 0.05 . . . . . . . . . . 4568 1 820 . 1 1 145 145 LYS N N 15 117.975 0.05 . . . . . . . . . . 4568 1 821 . 1 1 146 146 TYR H H 1 7.904 0.02 . . . . . . . . . . 4568 1 822 . 1 1 146 146 TYR HA H 1 4.357 0.02 . . . . . . . . . . 4568 1 823 . 1 1 146 146 TYR C C 13 177.443 0.05 . . . . . . . . . . 4568 1 824 . 1 1 146 146 TYR CA C 13 59.141 0.05 . . . . . . . . . . 4568 1 825 . 1 1 146 146 TYR CB C 13 38.105 0.05 . . . . . . . . . . 4568 1 826 . 1 1 146 146 TYR N N 15 118.726 0.05 . . . . . . . . . . 4568 1 827 . 1 1 147 147 LYS H H 1 7.789 0.02 . . . . . . . . . . 4568 1 828 . 1 1 147 147 LYS HA H 1 4.109 0.02 . . . . . . . . . . 4568 1 829 . 1 1 147 147 LYS C C 13 176.867 0.05 . . . . . . . . . . 4568 1 830 . 1 1 147 147 LYS CA C 13 57.900 0.05 . . . . . . . . . . 4568 1 831 . 1 1 147 147 LYS N N 15 120.226 0.05 . . . . . . . . . . 4568 1 832 . 1 1 148 148 GLU H H 1 8.081 0.02 . . . . . . . . . . 4568 1 833 . 1 1 148 148 GLU C C 13 177.817 0.05 . . . . . . . . . . 4568 1 834 . 1 1 148 148 GLU CA C 13 57.345 0.05 . . . . . . . . . . 4568 1 835 . 1 1 148 148 GLU CB C 13 29.485 0.05 . . . . . . . . . . 4568 1 836 . 1 1 148 148 GLU N N 15 119.476 0.05 . . . . . . . . . . 4568 1 837 . 1 1 149 149 LEU H H 1 7.787 0.02 . . . . . . . . . . 4568 1 838 . 1 1 149 149 LEU HA H 1 4.208 0.02 . . . . . . . . . . 4568 1 839 . 1 1 149 149 LEU C C 13 176.876 0.05 . . . . . . . . . . 4568 1 840 . 1 1 149 149 LEU CA C 13 55.372 0.05 . . . . . . . . . . 4568 1 841 . 1 1 149 149 LEU CB C 13 42.566 0.05 . . . . . . . . . . 4568 1 842 . 1 1 149 149 LEU N N 15 119.476 0.05 . . . . . . . . . . 4568 1 843 . 1 1 150 150 GLY H H 1 7.910 0.02 . . . . . . . . . . 4568 1 844 . 1 1 150 150 GLY HA2 H 1 3.878 0.02 . . . . . . . . . . 4568 1 845 . 1 1 150 150 GLY C C 13 177.425 0.05 . . . . . . . . . . 4568 1 846 . 1 1 150 150 GLY CA C 13 45.558 0.05 . . . . . . . . . . 4568 1 847 . 1 1 150 150 GLY N N 15 107.473 0.05 . . . . . . . . . . 4568 1 848 . 1 1 151 151 TYR H H 1 7.743 0.02 . . . . . . . . . . 4568 1 849 . 1 1 151 151 TYR HA H 1 4.460 0.02 . . . . . . . . . . 4568 1 850 . 1 1 151 151 TYR C C 13 173.938 0.05 . . . . . . . . . . 4568 1 851 . 1 1 151 151 TYR CA C 13 57.913 0.05 . . . . . . . . . . 4568 1 852 . 1 1 151 151 TYR CB C 13 38.793 0.05 . . . . . . . . . . 4568 1 853 . 1 1 151 151 TYR N N 15 119.851 0.05 . . . . . . . . . . 4568 1 854 . 1 1 152 152 GLN H H 1 8.079 0.02 . . . . . . . . . . 4568 1 855 . 1 1 152 152 GLN HA H 1 4.280 0.02 . . . . . . . . . . 4568 1 856 . 1 1 152 152 GLN C C 13 175.396 0.05 . . . . . . . . . . 4568 1 857 . 1 1 152 152 GLN CA C 13 55.402 0.05 . . . . . . . . . . 4568 1 858 . 1 1 152 152 GLN CB C 13 29.958 0.05 . . . . . . . . . . 4568 1 859 . 1 1 152 152 GLN N N 15 122.101 0.05 . . . . . . . . . . 4568 1 860 . 1 1 153 153 GLY H H 1 7.341 0.02 . . . . . . . . . . 4568 1 861 . 1 1 153 153 GLY HA2 H 1 3.692 0.02 . . . . . . . . . . 4568 1 862 . 1 1 153 153 GLY C C 13 174.798 0.05 . . . . . . . . . . 4568 1 863 . 1 1 153 153 GLY CA C 13 45.980 0.05 . . . . . . . . . . 4568 1 864 . 1 1 153 153 GLY N N 15 114.975 0.05 . . . . . . . . . . 4568 1 stop_ save_