data_5158 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5158 _Entry.Title ; Conformational and Dynamic Characterization of the Molten Globule state of an Apomyoglobin Mutant with an altered Folding Pathway ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2001-09-25 _Entry.Accession_date 2001-09-25 _Entry.Last_release_date 2002-01-25 _Entry.Original_release_date 2002-01-25 _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 Silvia Cavagnero . . . 5158 2 Chiaki Nishimura . . . 5158 3 Stephan Schwarzinger . . . 5158 4 Jane Dyson . . . 5158 5 Peter Wright . E. . 5158 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5158 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 287 5158 '15N chemical shifts' 137 5158 '1H chemical shifts' 137 5158 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 . . 2002-01-25 2001-09-24 original author . 5158 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4695 'myoglobin H64F mutant' 5158 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5158 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code 21581530 _Citation.DOI . _Citation.PubMed_ID 11724558 _Citation.Full_citation . _Citation.Title ; Conformational and Dynamic Characterization of the Molten Globule State of an Apomyoglobin Mutant with an Altered Folding Pathway ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 40 _Citation.Journal_issue 48 _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 14459 _Citation.Page_last 14467 _Citation.Year 2001 _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 Silvia Cavagnero . . . 5158 1 2 Chiaki Nishimura . . . 5158 1 3 Stephan Schwarzinger . . . 5158 1 4 H. Dyson . Jane . 5158 1 5 Peter Wright . E. . 5158 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_apoMb(GG) _Assembly.Sf_category assembly _Assembly.Sf_framecode system_apoMb(GG) _Assembly.Entry_ID 5158 _Assembly.ID 1 _Assembly.Name 'apomyoglobin N132G,E136G mutant' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state '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 5158 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 GG mutant' 1 $apoMb . . . 'molten globule' . . . . . 5158 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID apoMb(GG) abbreviation 5158 1 'apomyoglobin N132G,E136G mutant' system 5158 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_apoMb _Entity.Sf_category entity _Entity.Sf_framecode apoMb _Entity.Entry_ID 5158 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name apomyoglobin _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 GDFGADAQGAMGKALGLFRK 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 . _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 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 1027 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 2 no BMRB 1029 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 3 no BMRB 1200 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 4 no BMRB 1413 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 5 no BMRB 1455 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 6 no BMRB 1457 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 7 no BMRB 1459 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 8 no BMRB 1461 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 9 no BMRB 1463 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 10 no BMRB 1465 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 11 no BMRB 1467 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 12 no BMRB 1469 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 13 no BMRB 1471 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 14 no BMRB 15589 . Apomyoglobin_(1-77) . . . . . 50.33 77 100.00 100.00 6.44e-45 . . . . 5158 1 15 no BMRB 16217 . apomyoglobin . . . . . 77.78 119 100.00 100.00 2.61e-76 . . . . 5158 1 16 no BMRB 16218 . apoMb_1-119_fragment . . . . . 77.78 119 100.00 100.00 2.61e-76 . . . . 5158 1 17 no BMRB 16499 . 1-77_Apomyoglobin . . . . . 50.33 78 100.00 100.00 5.69e-45 . . . . 5158 1 18 no BMRB 16500 . (1-119)Apomyoglobin . . . . . 77.78 120 100.00 100.00 2.98e-76 . . . . 5158 1 19 no BMRB 16501 . (1-153)Apomyoglobin . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 20 no BMRB 1752 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 21 no BMRB 2345 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 22 no BMRB 2346 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 23 no BMRB 2347 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 24 no BMRB 2348 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 25 no BMRB 2431 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 26 no BMRB 2432 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 27 no BMRB 2433 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 28 no BMRB 2434 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 29 no BMRB 291 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 30 no BMRB 292 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 31 no BMRB 293 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 32 no BMRB 40 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 33 no BMRB 4061 . apoMb . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 34 no BMRB 4062 . apoMb . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 35 no BMRB 426 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 36 no BMRB 4568 . apoMb . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 37 no BMRB 4676 . apoMb . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 38 no BMRB 4695 . Mb . . . . . 100.00 153 98.04 98.04 3.37e-100 . . . . 5158 1 39 no BMRB 823 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 40 no BMRB 824 . myoglobin . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 41 no PDB 101M . "Sperm Whale Myoglobin F46v N-Butyl Isocyanide At Ph 9.0" . . . . . 100.00 154 97.39 98.04 7.57e-100 . . . . 5158 1 42 no PDB 102M . "Sperm Whale Myoglobin H64a Aquomet At Ph 9.0" . . . . . 100.00 154 97.39 98.04 8.26e-100 . . . . 5158 1 43 no PDB 103M . "Sperm Whale Myoglobin H64a N-Butyl Isocyanide At Ph 9.0" . . . . . 100.00 154 97.39 98.04 8.26e-100 . . . . 5158 1 44 no PDB 104M . "Sperm Whale Myoglobin N-Butyl Isocyanide At Ph 7.0" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 45 no PDB 105M . "Sperm Whale Myoglobin N-Butyl Isocyanide At Ph 9.0" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 46 no PDB 106M . "Sperm Whale Myoglobin V68f Ethyl Isocyanide At Ph 9.0" . . . . . 100.00 154 97.39 98.04 4.68e-100 . . . . 5158 1 47 no PDB 107M . "Sperm Whale Myoglobin V68f N-Butyl Isocyanide At Ph 9.0" . . . . . 100.00 154 97.39 98.04 4.68e-100 . . . . 5158 1 48 no PDB 108M . "Sperm Whale Myoglobin V68f N-Butyl Isocyanide At Ph 7.0" . . . . . 100.00 154 97.39 98.04 4.68e-100 . . . . 5158 1 49 no PDB 109M . "Sperm Whale Myoglobin D122n Ethyl Isocyanide At Ph 9.0" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 50 no PDB 110M . "Sperm Whale Myoglobin D122n Methyl Isocyanide At Ph 9.0" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 51 no PDB 111M . "Sperm Whale Myoglobin D122n N-Butyl Isocyanide At Ph 9.0" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 52 no PDB 112M . "Sperm Whale Myoglobin D122n N-Propyl Isocyanide At Ph 9.0" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 53 no PDB 1A6G . "Carbonmonoxy-Myoglobin, Atomic Resolution" . . . . . 98.69 151 98.01 98.68 2.93e-99 . . . . 5158 1 54 no PDB 1A6K . "Aquomet-Myoglobin, Atomic Resolution" . . . . . 98.69 151 98.68 98.68 1.03e-99 . . . . 5158 1 55 no PDB 1A6M . "Oxy-Myoglobin, Atomic Resolution" . . . . . 98.69 151 98.68 98.68 1.03e-99 . . . . 5158 1 56 no PDB 1A6N . "Deoxy-Myoglobin, Atomic Resolution" . . . . . 98.69 151 98.68 98.68 1.03e-99 . . . . 5158 1 57 no PDB 1ABS . "Photolysed Carbonmonoxy-Myoglobin At 20 K" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 58 no PDB 1AJG . "Carbonmonoxy Myoglobin At 40 K" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 59 no PDB 1AJH . "Photoproduct Of Carbonmonoxy Myoglobin At 40 K" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 60 no PDB 1BVC . "Structure Of A Biliverdin Apomyoglobin Complex (Form D) At 118 K" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 61 no PDB 1BVD . "Structure Of A Biliverdin Apomyoglobin Complex (Form B) At 98 K" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 62 no PDB 1BZ6 . "Atomic Resolution Crystal Structure Aquomet-Myoglobin From Sperm Whale At Room Temperature" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 63 no PDB 1BZP . "Atomic Resolution Crystal Structure Analysis Of Native Deoxy And Co Myoglobin From Sperm Whale At Room Temperature" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 64 no PDB 1BZR . "Atomic Resolution Crystal Structure Analysis Of Native Deoxy And Co Myoglobin From Sperm Whale At Room Temperature" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 65 no PDB 1CH1 . "Recombinant Sperm Whale Myoglobin L89g Mutatnt (Met)" . . . . . 100.00 154 97.39 98.04 1.32e-99 . . . . 5158 1 66 no PDB 1CH2 . "Recombinant Sperm Whale Myoglobin L89f Mutant (Met)" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 67 no PDB 1CH3 . "Recombinant Sperm Whale Myoglobin L89w Mutant (Met)" . . . . . 100.00 154 97.39 98.04 6.02e-100 . . . . 5158 1 68 no PDB 1CH5 . "Recombinant Sperm Whale Myoglobin H97v Mutant (Met)" . . . . . 100.00 154 97.39 98.04 1.29e-99 . . . . 5158 1 69 no PDB 1CH7 . "Recombinant Sperm Whale Myoglobin H97f Mutant (Met)" . . . . . 100.00 154 97.39 98.04 9.21e-100 . . . . 5158 1 70 no PDB 1CH9 . "Recombinant Sperm Whale Myoglobin H97q Mutant (Met)" . . . . . 100.00 154 97.39 98.04 5.05e-100 . . . . 5158 1 71 no PDB 1CIK . "Recombinant Sperm Whale Myoglobin I99a Mutant (Met)" . . . . . 100.00 154 97.39 98.04 4.20e-100 . . . . 5158 1 72 no PDB 1CIO . "Recombinant Sperm Whale Myoglobin I99v Mutant (Met)" . . . . . 100.00 154 97.39 98.69 1.19e-100 . . . . 5158 1 73 no PDB 1CO8 . "Recombinant Sperm Whale Myoglobin L104a Mutant (Met)" . . . . . 100.00 154 97.39 98.04 4.29e-100 . . . . 5158 1 74 no PDB 1CO9 . "Recombinant Sperm Whale Myoglobin L104v Mutant (Met)" . . . . . 100.00 154 97.39 98.69 1.83e-100 . . . . 5158 1 75 no PDB 1CP0 . "Recombinant Sperm Whale Myoglobin L104n Mutant (Met)" . . . . . 100.00 154 97.39 98.04 5.28e-100 . . . . 5158 1 76 no PDB 1CP5 . "Recombinant Sperm Whale Myoglobin L104f Mutant (Met)" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 77 no PDB 1CPW . "Recombinant Sperm Whale Myoglobin L104w Mutant (Met)" . . . . . 100.00 154 97.39 98.04 6.02e-100 . . . . 5158 1 78 no PDB 1CQ2 . "Neutron Struture Of Fully Deuterated Sperm Whale Myoglobin At 2.0 Angstrom" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 79 no PDB 1DO1 . "Carbonmonoxy-Myoglobin Mutant L29w At 105k" . . . . . 100.00 154 97.39 98.04 8.17e-100 . . . . 5158 1 80 no PDB 1DO3 . "Carbonmonoxy-Myoglobin (Mutant L29w) After Photolysis At T>180k" . . . . . 100.00 154 97.39 98.04 8.17e-100 . . . . 5158 1 81 no PDB 1DO4 . "Carbonmonoxy-Myoglobin (Mutant L29w) After Photolysis At T<180k" . . . . . 100.00 154 97.39 98.04 8.17e-100 . . . . 5158 1 82 no PDB 1DO7 . "Carbonmonoxy-Myoglobin (Mutant L29w) Rebinding Structure After Photolysis At T< 180k" . . . . . 100.00 154 97.39 98.04 8.17e-100 . . . . 5158 1 83 no PDB 1DTI . "Recombinant Sperm Whale Myoglobin H97d, D122n Mutant (Met)" . . . . . 100.00 154 97.39 98.04 1.02e-99 . . . . 5158 1 84 no PDB 1DTM . "Crystal Structure Of The Sperm-Whale Myoglobin Mutant H93g Complexed With 4-Methylimidazole, Metaquo Form" . . . . . 100.00 153 98.04 98.04 6.15e-100 . . . . 5158 1 85 no PDB 1DUK . "Wild-Type Recombinant Sperm Whale Metaquomyoglobin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 86 no PDB 1DUO . "Sperm Whale Metaquomyoglobin Proximal Histidine Mutant H93g With 1-Methylimidazole As Proximal Ligand." . . . . . 100.00 153 98.04 98.04 6.15e-100 . . . . 5158 1 87 no PDB 1EBC . "Sperm Whale Met-Myoglobin:cyanide Complex" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 88 no PDB 1F6H . "Combined Rietveld And Stereochemical Restraint Refinement Of A Protein" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 89 no PDB 1HJT . "Sperm Whale Myoglobin (Ferrous, Nitric Oxide Bound)" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 90 no PDB 1IOP . "Incorporation Of A Hemin With The Shortest Acid Side-Chains Into Myoglobin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 91 no PDB 1IRC . "Cysteine Rich Intestinal Protein" . . . . . 100.00 154 98.04 98.04 5.22e-100 . . . . 5158 1 92 no PDB 1J3F . "Crystal Structure Of An Artificial Metalloprotein:cr(iii)(3, 3'-me2-salophen)/apo-a71g Myoglobin" . . . . . 100.00 154 98.04 98.04 1.07e-100 . . . . 5158 1 93 no PDB 1J52 . "Recombinant Sperm Whale Myoglobin In The Presence Of 7atm Xenon" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 94 no PDB 1JDO . "Sperm Whale Myoglobin (Ferrous, Nitric Oxide Bound)" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 95 no PDB 1JP6 . "Sperm Whale Met-Myoglobin (Room Temperature; Room Pressure)" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 96 no PDB 1JP8 . "Sperm Whale Met-Myoglobin (Room Temperature; High Pressure)" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 97 no PDB 1JP9 . "Sperm Whale Met-Myoglobin (Low Temperature; High Pressure)" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 98 no PDB 1JPB . "Sperm Whale Met-Myoglobin (Low Temperature; High Pressure)" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 99 no PDB 1JW8 . "1.3 Angstrom Resolution Crystal Structure Of P6 Form Of Myoglobin" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 100 no PDB 1L2K . "Neutron Structure Determination Of Sperm Whale Met-Myoglobin At 1.5a Resolution." . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 101 no PDB 1LTW . "Recombinant Sperm Whale Myoglobin 29w Mutant (oxy)" . . . . . 100.00 154 97.39 98.04 6.02e-100 . . . . 5158 1 102 no PDB 1MBC . "X-Ray Structure And Refinement Of Carbon-Monoxy (Fe Ii)- Myoglobin At 1.5 Angstroms Resolution" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 103 no PDB 1MBD . "Neutron Diffraction Reveals Oxygen-Histidine Hydrogen Bond In Oxymyoglobin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 104 no PDB 1MBI . "X-Ray Crystal Structure Of The Ferric Sperm Whale Myoglobin: Imidazole Complex At 2.0 Angstroms Resolution" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 105 no PDB 1MBN . "The Stereochemistry Of The Protein Myoglobin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 106 no PDB 1MBO . "Structure And Refinement Of Oxymyoglobin At 1.6 Angstroms Resolution" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 107 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 97.39 97.39 5.40e-100 . . . . 5158 1 108 no PDB 1MGN . "His64(E7)-> Tyr Apomyoglobin As A Reagent For Measuring Rates Of Hemin Dissociation" . . . . . 100.00 154 97.39 98.69 2.43e-100 . . . . 5158 1 109 no PDB 1MLF . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 97.39 98.04 3.49e-100 . . . . 5158 1 110 no PDB 1MLG . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 97.39 98.04 3.49e-100 . . . . 5158 1 111 no PDB 1MLH . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 97.39 98.04 3.49e-100 . . . . 5158 1 112 no PDB 1MLJ . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 97.39 98.04 4.68e-100 . . . . 5158 1 113 no PDB 1MLK . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 97.39 98.04 4.68e-100 . . . . 5158 1 114 no PDB 1MLL . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 97.39 98.04 4.68e-100 . . . . 5158 1 115 no PDB 1MLM . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 97.39 98.69 1.14e-100 . . . . 5158 1 116 no PDB 1MLN . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 97.39 98.69 1.14e-100 . . . . 5158 1 117 no PDB 1MLO . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 97.39 98.69 1.14e-100 . . . . 5158 1 118 no PDB 1MLQ . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 97.39 98.69 2.54e-100 . . . . 5158 1 119 no PDB 1MLR . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 97.39 98.69 2.54e-100 . . . . 5158 1 120 no PDB 1MLS . "Structural And Functional Effects Of Apolar Mutations Of Val68(E11) In Myoglobin" . . . . . 100.00 154 97.39 98.69 2.54e-100 . . . . 5158 1 121 no PDB 1MOA . "A Novel Site-Directed Mutant Of Myoglobin With An Unusually High O2 Affinity And Low Autooxidation Rate" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 122 no PDB 1MOB . "High-Resolution Crystal Structures Of Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 1.77e-99 . . . . 5158 1 123 no PDB 1MOC . "High-Resolution Crystal Structures Of Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 6.57e-100 . . . . 5158 1 124 no PDB 1MOD . "High-Resolution Crystal Structures Of Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 6.57e-100 . . . . 5158 1 125 no PDB 1MTI . "Phe46(Cd4) Orients The Distal Histidine For Hydrogen Bonding To Bound Ligands In Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 5.58e-100 . . . . 5158 1 126 no PDB 1MTJ . "Phe46(Cd4) Orients The Distal Histidine For Hydrogen Bonding To Bound Ligands In Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 7.57e-100 . . . . 5158 1 127 no PDB 1MTK . "Phe46(cd4) Orients The Distal Histidine For Hydrogen Bonding To Bound Ligands In Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 7.57e-100 . . . . 5158 1 128 no PDB 1MYF . "Solution Structure Of Carbonmonoxy Myoglobin Determined From Nmr Distance And Chemical Shift Constraints" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 129 no PDB 1MYM . "Structural Determinants Of Co Stretching Vibration Frequencies In Myoglobin" . . . . . 100.00 154 97.39 98.04 7.57e-100 . . . . 5158 1 130 no PDB 1SPE . "Sperm Whale Native Co Myoglobin At Ph 4.0, Temp 4c" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 131 no PDB 1SWM . "X-Ray Crystal Structure Of The Ferric Sperm Whale Myoglobin: Imidazole Complex At 2.0 Angstroms Resolution" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 132 no PDB 1TES . "Oxygen Binding Muscle Protein" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 133 no PDB 1U7R . "Crystal Structure Of Native Sperm Whale Myoglobin From Low Ionic Strength Enviroment (form2 )" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 134 no PDB 1U7S . "Crystal Structure Of Native Sperm Whale Myoglobin From Low Ionic Strength Enviroment (form 1)" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 135 no PDB 1UFJ . "Crystal Structure Of An Artificial Metalloprotein:fe(Iii)(3, 3'-Me2-Salophen)APO-A71g Myoglobin" . . . . . 100.00 154 98.04 98.04 1.07e-100 . . . . 5158 1 136 no PDB 1UFP . "Crystal Structure Of An Artificial Metalloprotein:fe(Iii)(3, 3'-Me2-Salophen)APO-Wild Type Myoglobin" . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 137 no PDB 1V9Q . "Crystal Structure Of An Artificial Metalloprotein:mn(iii)(3, 3'-me2-salophen)/apo-a71g Myoglobin" . . . . . 100.00 154 98.04 98.04 1.07e-100 . . . . 5158 1 138 no PDB 1VXA . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 139 no PDB 1VXB . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 140 no PDB 1VXC . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 141 no PDB 1VXD . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 142 no PDB 1VXE . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 143 no PDB 1VXF . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 144 no PDB 1VXG . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 145 no PDB 1VXH . "Native Sperm Whale Myoglobin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 146 no PDB 1WVP . "Structure Of Chemically Modified Myoglobin With Distal N- Tetrazolyl-Histidine E7(64)" . . . . . 100.00 153 98.04 98.04 2.51e-100 . . . . 5158 1 147 no PDB 1YOG . "Cobalt Myoglobin (Deoxy)" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 148 no PDB 1YOH . "Cobalt Myoglobin (Met)" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 149 no PDB 1YOI . "Cobalt Myoglobin (Oxy)" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 150 no PDB 2BLH . "Ligand Migration And Protein Fluctuations In Myoglobin Mutant L29w" . . . . . 100.00 153 97.39 98.04 7.90e-100 . . . . 5158 1 151 no PDB 2BLI . "L29w Mb Deoxy" . . . . . 100.00 153 97.39 98.04 7.90e-100 . . . . 5158 1 152 no PDB 2BLJ . "Structure Of L29w Mbco" . . . . . 100.00 153 97.39 98.04 7.90e-100 . . . . 5158 1 153 no PDB 2BW9 . "Laue Structure Of L29w Mbco" . . . . . 100.00 153 97.39 98.04 7.90e-100 . . . . 5158 1 154 no PDB 2BWH . "Laue Structure Of A Short Lived State Of L29w Myoglobin" . . . . . 100.00 153 97.39 98.04 7.90e-100 . . . . 5158 1 155 no PDB 2CMM . "Structural Analysis Of The Myoglobin Reconstituted With Iron Porphine" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 156 no PDB 2D6C . "Crystal Structure Of Myoglobin Reconstituted With Iron Porphycene" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 157 no PDB 2EB8 . "Crystal Structure Of Cu(Ii)(Sal-Phe)APO-Myoglobin" . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 158 no PDB 2EB9 . "Crystal Structure Of Cu(ii)(sal-leu)/apo-myoglobin" . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 159 no PDB 2EF2 . "Crystal Structure Of An Artificial Metalloprotein:rh(Phebox- Ph)APO-A71g Myoglobin" . . . . . 100.00 154 98.04 98.04 1.07e-100 . . . . 5158 1 160 no PDB 2EKT . "Crystal Structure Of Myoglobin Reconstituted With 6-Methyl-6- Depropionatehemin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 161 no PDB 2EKU . "Crystal Structure Of Myoglobin Reconstituted With 7-Methyl-7- Depropionatehemin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 162 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 98.04 98.04 6.15e-100 . . . . 5158 1 163 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 98.04 98.04 6.15e-100 . . . . 5158 1 164 no PDB 2G0R . "Unphotolyzed Co-bound L29f Myoglobin" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 165 no PDB 2G0S . "Unphotolyzed Co-bound L29f Myoglobin, Crystal 2" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 166 no PDB 2G0V . "Photolyzed Co L29f Myoglobin: 100ps" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 167 no PDB 2G0X . "Photolyzed Co L29f Myoglobin: 316ps" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 168 no PDB 2G0Z . "Photolyzed Co L29f Myoglobin: 1ns" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 169 no PDB 2G10 . "Photolyzed Co L29f Myoglobin: 3.16ns" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 170 no PDB 2G11 . "Photolyzed Co L29f Myoglobin: 31.6ns" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 171 no PDB 2G12 . "Photolyzed Co L29f Myoglobin: 316ns" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 172 no PDB 2G14 . "Photolyzed Co L29f Myoglobin: 3.16us" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 173 no PDB 2JHO . "Cyanomet Sperm Whale Myoglobin At 1.4a Resolution" . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 174 no PDB 2MB5 . "Hydration In Protein Crystals. A Neutron Diffraction Analysis Of Carbonmonoxymyoglobin" . . . . . 99.35 153 98.68 98.68 1.64e-100 . . . . 5158 1 175 no PDB 2MBW . "Recombinant Sperm Whale Myoglobin (Met)" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 176 no PDB 2MGA . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 1.77e-99 . . . . 5158 1 177 no PDB 2MGB . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 1.77e-99 . . . . 5158 1 178 no PDB 2MGC . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 1.13e-99 . . . . 5158 1 179 no PDB 2MGD . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 1.13e-99 . . . . 5158 1 180 no PDB 2MGE . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 1.13e-99 . . . . 5158 1 181 no PDB 2MGF . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 5.05e-100 . . . . 5158 1 182 no PDB 2MGG . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 5.05e-100 . . . . 5158 1 183 no PDB 2MGH . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 5.05e-100 . . . . 5158 1 184 no PDB 2MGI . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 6.57e-100 . . . . 5158 1 185 no PDB 2MGJ . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 97.39 98.04 1.29e-99 . . . . 5158 1 186 no PDB 2MGK . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 187 no PDB 2MGL . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 188 no PDB 2MGM . "High Resolution Crystal Structures Of Five Distal Histidine Mutants Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 189 no PDB 2MYA . "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 190 no PDB 2MYB . "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 191 no PDB 2MYC . "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 192 no PDB 2MYD . "High Resolution X-ray Structures Of Myoglobin-and Hemoglobin-alkyl Isocyanide Complexes" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 193 no PDB 2MYE . "High Resolution X-Ray Structures Of Myoglobin-And Hemoglobin-Alkyl Isocyanide Complexes" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 194 no PDB 2OH8 . "Myoglobin Cavity Mutant I28w" . . . . . 100.00 154 97.39 98.04 1.11e-99 . . . . 5158 1 195 no PDB 2OH9 . "Myoglobin Cavity Mutant V68w" . . . . . 100.00 154 97.39 98.04 1.13e-99 . . . . 5158 1 196 no PDB 2OHA . "Myoglobin Cavity Mutant F138w" . . . . . 100.00 154 97.39 98.69 4.78e-100 . . . . 5158 1 197 no PDB 2OHB . "Myoglobin Cavity Mutant I107w" . . . . . 100.00 154 97.39 98.04 1.11e-99 . . . . 5158 1 198 no PDB 2SPL . "A Novel Site-Directed Mutant Of Myoglobin With An Unusually High O2 Affinity And Low Autooxidation Rate" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 199 no PDB 2SPM . "A Novel Site-Directed Mutant Of Myoglobin With An Unusually High O2 Affinity And Low Autooxidation Rate" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 200 no PDB 2SPN . "A Novel Site-Directed Mutant Of Myoglobin With An Unusually High O2 Affinity And Low Autooxidation Rate" . . . . . 100.00 154 97.39 98.04 2.38e-100 . . . . 5158 1 201 no PDB 2SPO . "A Novel Site-directed Mutant Of Myoglobin With An Unusually High O2 Affinity And Low Autooxidation Rate" . . . . . 100.00 154 97.39 98.69 1.83e-100 . . . . 5158 1 202 no PDB 2W6W . "Crystal Structure Of Recombinant Sperm Whale Myoglobin Under 1atm Of Xenon" . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 203 no PDB 2Z6S . "Crystal Structure Of The Oxy Myoglobin Free From X-ray- Induced Photoreduction" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 204 no PDB 2Z6T . "Crystal Structure Of The Ferric Peroxo Myoglobin" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 205 no PDB 2ZSN . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [300 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 206 no PDB 2ZSO . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [450 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 207 no PDB 2ZSP . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [300 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 208 no PDB 2ZSQ . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser On [150 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 209 no PDB 2ZSR . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [450 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 210 no PDB 2ZSS . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser On [300 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 211 no PDB 2ZST . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser On [450 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 212 no PDB 2ZSX . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser On [600 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 213 no PDB 2ZSY . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser On [750 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 214 no PDB 2ZSZ . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [600 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 215 no PDB 2ZT0 . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [750 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 216 no PDB 2ZT1 . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [810 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 217 no PDB 2ZT2 . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [600 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 218 no PDB 2ZT3 . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [750 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 219 no PDB 2ZT4 . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [810 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 220 no PDB 3A2G . "Crystal Structure Of K102c-Myoglobin Conjugated With Fluorescein" . . . . . 100.00 154 98.04 98.04 1.38e-100 . . . . 5158 1 221 no PDB 3ASE . "Crystal Structure Of Zinc Myoglobin Soaked With Ru3o Cluster" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 222 no PDB 3E4N . "Carbonmonoxy Sperm Whale Myoglobin At 40 K: Laser Off" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 223 no PDB 3E55 . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser Off" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 224 no PDB 3E5I . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser Off" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 225 no PDB 3E5O . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser Off" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 226 no PDB 3ECL . "Carbonmonoxy Sperm Whale Myoglobin At 40 K: Laser On" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 227 no PDB 3ECX . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [30 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 228 no PDB 3ECZ . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [30 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 229 no PDB 3ED9 . "Carbonmonoxy Sperm Whale Myoglobin At 140 K: Laser On [30 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 230 no PDB 3EDA . "Carbonmonoxy Sperm Whale Myoglobin At 100 K: Laser On [150 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 231 no PDB 3EDB . "Carbonmonoxy Sperm Whale Myoglobin At 120 K: Laser On [150 Min]" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 232 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 97.39 97.39 5.90e-99 . . . . 5158 1 233 no PDB 3NML . "Sperm Whale Myoglobin Mutant H64w Carbonmonoxy-Form" . . . . . 100.00 154 97.39 98.04 1.94e-99 . . . . 5158 1 234 no PDB 3O89 . "Crystal Structure Of Sperm Whale Myoglobin G65t" . . . . . 100.00 153 98.04 98.04 1.75e-100 . . . . 5158 1 235 no PDB 3OGB . "Sperm Whale Myoglobin Mutant H64w Deoxy-Form" . . . . . 100.00 154 97.39 98.04 1.94e-99 . . . . 5158 1 236 no PDB 3SDN . "Structure Of G65i Sperm Whale Myoglobin Mutant" . . . . . 100.00 154 98.04 98.04 4.78e-100 . . . . 5158 1 237 no PDB 3U3E . "Complex Of Wild Type Myoglobin With Phenol In Its Proximal Cavity" . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 238 no PDB 4FWZ . "Aquoferric Cub Myoglobin (L29h F43h Sperm Whale Myoglobin)" . . . . . 100.00 153 97.39 97.39 9.96e-99 . . . . 5158 1 239 no PDB 4H07 . "Complex Of G65t Myoglobin With Phenol In Its Proximal Cavity" . . . . . 100.00 154 98.04 98.04 1.91e-100 . . . . 5158 1 240 no PDB 4H0B . "Complex Of G65t Myoglobin With Dmso In Its Distal Cavity" . . . . . 100.00 154 98.04 98.04 1.91e-100 . . . . 5158 1 241 no PDB 4IT8 . "A Sperm Whale Myoglobin Mutant L29h Mb With Two Distal Histidines" . . . . . 100.00 154 98.04 98.04 3.85e-100 . . . . 5158 1 242 no PDB 4LPI . "A Sperm Whale Myoglobin Double Mutant L29h/f43y Mb With A Distal Hydrogen-bonding Network" . . . . . 100.00 154 97.39 98.04 1.18e-99 . . . . 5158 1 243 no PDB 4MBN . "Refinement Of Myoglobin And Cytochrome C" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 244 no PDB 4NXA . "Sperm Whale Myoglobin Under Xenon Pressure 30 Bar" . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 245 no PDB 4NXC . "Sperm Whale Myoglobin Under 30 Bar Nitrous Oxide" . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 246 no PDB 4OF9 . "Structure Of K42n Variant Of Sperm Whale Myoglobin" . . . . . 100.00 153 98.04 98.04 7.30e-101 . . . . 5158 1 247 no PDB 4OOD . "Structure Of K42y Mutant Of Sperm Whale Myoglobin" . . . . . 100.00 154 98.04 98.04 1.42e-100 . . . . 5158 1 248 no PDB 4PNJ . "Recombinant Sperm Whale P6 Myoglobin Solved With Single Pulse Free Electron Laser Data" . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 249 no PDB 4PQ6 . "A Sperm Whale Myoglobin Single Mutant L29e Mb With Native His93 Coordination" . . . . . 100.00 154 98.04 98.04 2.86e-100 . . . . 5158 1 250 no PDB 4PQB . "A Sperm Whale Myoglobin Double Mutant L29e/f43h Mb With A Non-native Bis-his (his64/his93) Coordination" . . . . . 100.00 154 97.39 97.39 5.12e-99 . . . . 5158 1 251 no PDB 4PQC . "A Sperm Whale Myoglobin Single Mutant F43h Mb With Native His93 Coordination" . . . . . 100.00 154 98.04 98.04 5.11e-100 . . . . 5158 1 252 no PDB 5MBN . "Refinement Of Myoglobin And Cytochrome C" . . . . . 100.00 153 98.69 98.69 2.03e-101 . . . . 5158 1 253 no DBJ BAF03579 . "myoglobin [Physeter catodon]" . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 254 no GB AAA72199 . "synthetic myoglobin [synthetic construct]" . . . . . 100.00 154 98.04 98.69 7.15e-101 . . . . 5158 1 255 no PRF 742482A . myoglobin . . . . . 100.00 153 98.04 98.69 6.91e-101 . . . . 5158 1 256 no REF NP_001277651 . "myoglobin [Physeter catodon]" . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 257 no SP P02185 . "RecName: Full=Myoglobin [Physeter catodon]" . . . . . 100.00 154 98.69 98.69 2.10e-101 . . . . 5158 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID apoMb abbreviation 5158 1 apomyoglobin common 5158 1 N132G,E136G variant 5158 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 . 5158 1 2 . LEU . 5158 1 3 . SER . 5158 1 4 . GLU . 5158 1 5 . GLY . 5158 1 6 . GLU . 5158 1 7 . TRP . 5158 1 8 . GLN . 5158 1 9 . LEU . 5158 1 10 . VAL . 5158 1 11 . LEU . 5158 1 12 . HIS . 5158 1 13 . VAL . 5158 1 14 . TRP . 5158 1 15 . ALA . 5158 1 16 . LYS . 5158 1 17 . VAL . 5158 1 18 . GLU . 5158 1 19 . ALA . 5158 1 20 . ASP . 5158 1 21 . VAL . 5158 1 22 . ALA . 5158 1 23 . GLY . 5158 1 24 . HIS . 5158 1 25 . GLY . 5158 1 26 . GLN . 5158 1 27 . ASP . 5158 1 28 . ILE . 5158 1 29 . LEU . 5158 1 30 . ILE . 5158 1 31 . ARG . 5158 1 32 . LEU . 5158 1 33 . PHE . 5158 1 34 . LYS . 5158 1 35 . SER . 5158 1 36 . HIS . 5158 1 37 . PRO . 5158 1 38 . GLU . 5158 1 39 . THR . 5158 1 40 . LEU . 5158 1 41 . GLU . 5158 1 42 . LYS . 5158 1 43 . PHE . 5158 1 44 . ASP . 5158 1 45 . ARG . 5158 1 46 . PHE . 5158 1 47 . LYS . 5158 1 48 . HIS . 5158 1 49 . LEU . 5158 1 50 . LYS . 5158 1 51 . THR . 5158 1 52 . GLU . 5158 1 53 . ALA . 5158 1 54 . GLU . 5158 1 55 . MET . 5158 1 56 . LYS . 5158 1 57 . ALA . 5158 1 58 . SER . 5158 1 59 . GLU . 5158 1 60 . ASP . 5158 1 61 . LEU . 5158 1 62 . LYS . 5158 1 63 . LYS . 5158 1 64 . HIS . 5158 1 65 . GLY . 5158 1 66 . VAL . 5158 1 67 . THR . 5158 1 68 . VAL . 5158 1 69 . LEU . 5158 1 70 . THR . 5158 1 71 . ALA . 5158 1 72 . LEU . 5158 1 73 . GLY . 5158 1 74 . ALA . 5158 1 75 . ILE . 5158 1 76 . LEU . 5158 1 77 . LYS . 5158 1 78 . LYS . 5158 1 79 . LYS . 5158 1 80 . GLY . 5158 1 81 . HIS . 5158 1 82 . HIS . 5158 1 83 . GLU . 5158 1 84 . ALA . 5158 1 85 . GLU . 5158 1 86 . LEU . 5158 1 87 . LYS . 5158 1 88 . PRO . 5158 1 89 . LEU . 5158 1 90 . ALA . 5158 1 91 . GLN . 5158 1 92 . SER . 5158 1 93 . HIS . 5158 1 94 . ALA . 5158 1 95 . THR . 5158 1 96 . LYS . 5158 1 97 . HIS . 5158 1 98 . LYS . 5158 1 99 . ILE . 5158 1 100 . PRO . 5158 1 101 . ILE . 5158 1 102 . LYS . 5158 1 103 . TYR . 5158 1 104 . LEU . 5158 1 105 . GLU . 5158 1 106 . PHE . 5158 1 107 . ILE . 5158 1 108 . SER . 5158 1 109 . GLU . 5158 1 110 . ALA . 5158 1 111 . ILE . 5158 1 112 . ILE . 5158 1 113 . HIS . 5158 1 114 . VAL . 5158 1 115 . LEU . 5158 1 116 . HIS . 5158 1 117 . SER . 5158 1 118 . ARG . 5158 1 119 . HIS . 5158 1 120 . PRO . 5158 1 121 . GLY . 5158 1 122 . ASP . 5158 1 123 . PHE . 5158 1 124 . GLY . 5158 1 125 . ALA . 5158 1 126 . ASP . 5158 1 127 . ALA . 5158 1 128 . GLN . 5158 1 129 . GLY . 5158 1 130 . ALA . 5158 1 131 . MET . 5158 1 132 . GLY . 5158 1 133 . LYS . 5158 1 134 . ALA . 5158 1 135 . LEU . 5158 1 136 . GLY . 5158 1 137 . LEU . 5158 1 138 . PHE . 5158 1 139 . ARG . 5158 1 140 . LYS . 5158 1 141 . ASP . 5158 1 142 . ILE . 5158 1 143 . ALA . 5158 1 144 . ALA . 5158 1 145 . LYS . 5158 1 146 . TYR . 5158 1 147 . LYS . 5158 1 148 . GLU . 5158 1 149 . LEU . 5158 1 150 . GLY . 5158 1 151 . TYR . 5158 1 152 . GLN . 5158 1 153 . GLY . 5158 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 5158 1 . LEU 2 2 5158 1 . SER 3 3 5158 1 . GLU 4 4 5158 1 . GLY 5 5 5158 1 . GLU 6 6 5158 1 . TRP 7 7 5158 1 . GLN 8 8 5158 1 . LEU 9 9 5158 1 . VAL 10 10 5158 1 . LEU 11 11 5158 1 . HIS 12 12 5158 1 . VAL 13 13 5158 1 . TRP 14 14 5158 1 . ALA 15 15 5158 1 . LYS 16 16 5158 1 . VAL 17 17 5158 1 . GLU 18 18 5158 1 . ALA 19 19 5158 1 . ASP 20 20 5158 1 . VAL 21 21 5158 1 . ALA 22 22 5158 1 . GLY 23 23 5158 1 . HIS 24 24 5158 1 . GLY 25 25 5158 1 . GLN 26 26 5158 1 . ASP 27 27 5158 1 . ILE 28 28 5158 1 . LEU 29 29 5158 1 . ILE 30 30 5158 1 . ARG 31 31 5158 1 . LEU 32 32 5158 1 . PHE 33 33 5158 1 . LYS 34 34 5158 1 . SER 35 35 5158 1 . HIS 36 36 5158 1 . PRO 37 37 5158 1 . GLU 38 38 5158 1 . THR 39 39 5158 1 . LEU 40 40 5158 1 . GLU 41 41 5158 1 . LYS 42 42 5158 1 . PHE 43 43 5158 1 . ASP 44 44 5158 1 . ARG 45 45 5158 1 . PHE 46 46 5158 1 . LYS 47 47 5158 1 . HIS 48 48 5158 1 . LEU 49 49 5158 1 . LYS 50 50 5158 1 . THR 51 51 5158 1 . GLU 52 52 5158 1 . ALA 53 53 5158 1 . GLU 54 54 5158 1 . MET 55 55 5158 1 . LYS 56 56 5158 1 . ALA 57 57 5158 1 . SER 58 58 5158 1 . GLU 59 59 5158 1 . ASP 60 60 5158 1 . LEU 61 61 5158 1 . LYS 62 62 5158 1 . LYS 63 63 5158 1 . HIS 64 64 5158 1 . GLY 65 65 5158 1 . VAL 66 66 5158 1 . THR 67 67 5158 1 . VAL 68 68 5158 1 . LEU 69 69 5158 1 . THR 70 70 5158 1 . ALA 71 71 5158 1 . LEU 72 72 5158 1 . GLY 73 73 5158 1 . ALA 74 74 5158 1 . ILE 75 75 5158 1 . LEU 76 76 5158 1 . LYS 77 77 5158 1 . LYS 78 78 5158 1 . LYS 79 79 5158 1 . GLY 80 80 5158 1 . HIS 81 81 5158 1 . HIS 82 82 5158 1 . GLU 83 83 5158 1 . ALA 84 84 5158 1 . GLU 85 85 5158 1 . LEU 86 86 5158 1 . LYS 87 87 5158 1 . PRO 88 88 5158 1 . LEU 89 89 5158 1 . ALA 90 90 5158 1 . GLN 91 91 5158 1 . SER 92 92 5158 1 . HIS 93 93 5158 1 . ALA 94 94 5158 1 . THR 95 95 5158 1 . LYS 96 96 5158 1 . HIS 97 97 5158 1 . LYS 98 98 5158 1 . ILE 99 99 5158 1 . PRO 100 100 5158 1 . ILE 101 101 5158 1 . LYS 102 102 5158 1 . TYR 103 103 5158 1 . LEU 104 104 5158 1 . GLU 105 105 5158 1 . PHE 106 106 5158 1 . ILE 107 107 5158 1 . SER 108 108 5158 1 . GLU 109 109 5158 1 . ALA 110 110 5158 1 . ILE 111 111 5158 1 . ILE 112 112 5158 1 . HIS 113 113 5158 1 . VAL 114 114 5158 1 . LEU 115 115 5158 1 . HIS 116 116 5158 1 . SER 117 117 5158 1 . ARG 118 118 5158 1 . HIS 119 119 5158 1 . PRO 120 120 5158 1 . GLY 121 121 5158 1 . ASP 122 122 5158 1 . PHE 123 123 5158 1 . GLY 124 124 5158 1 . ALA 125 125 5158 1 . ASP 126 126 5158 1 . ALA 127 127 5158 1 . GLN 128 128 5158 1 . GLY 129 129 5158 1 . ALA 130 130 5158 1 . MET 131 131 5158 1 . GLY 132 132 5158 1 . LYS 133 133 5158 1 . ALA 134 134 5158 1 . LEU 135 135 5158 1 . GLY 136 136 5158 1 . LEU 137 137 5158 1 . PHE 138 138 5158 1 . ARG 139 139 5158 1 . LYS 140 140 5158 1 . ASP 141 141 5158 1 . ILE 142 142 5158 1 . ALA 143 143 5158 1 . ALA 144 144 5158 1 . LYS 145 145 5158 1 . TYR 146 146 5158 1 . LYS 147 147 5158 1 . GLU 148 148 5158 1 . LEU 149 149 5158 1 . GLY 150 150 5158 1 . TYR 151 151 5158 1 . GLN 152 152 5158 1 . GLY 153 153 5158 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 5158 _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 . . 'Physeter catodon' 'sperm whale' . . Eukaryota Metazoa Physeter catodon . . . . . . . . . . . . . . . . . . . . . 5158 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 5158 _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' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5158 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5158 _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 apomyoglobin '[U-13C; U-15N]' . . 1 $apoMb . . 0.3 0.2 0.4 mM . . . . 5158 1 2 ethanol [U-2H] . . . . . . 10 . . % . . . . 5158 1 3 H2O . . . . . . . 90 . . % . . . . 5158 1 stop_ save_ ####################### # Sample conditions # ####################### save_cond1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode cond1 _Sample_condition_list.Entry_ID 5158 _Sample_condition_list.ID 1 _Sample_condition_list.Details ; Deuterated ethanol was added to a total concentration of 10% v/v in order to prevent aggregation during the NMR experiments (see Eliezer et al., 2000). ; 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 na 5158 1 temperature 323 1 K 5158 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 5158 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . save_ save_NMRView _Software.Sf_category software _Software.Sf_framecode NMRView _Software.Entry_ID 5158 _Software.ID 2 _Software.Name NMRView _Software.Version . _Software.Details . 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 5158 _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 5158 _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 . . . 5158 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 5158 _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 HNCA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5158 1 2 HN(CO)CA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5158 1 3 HNCO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5158 1 4 (HCA)CO(CA)NH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5158 1 5 CBCA(CO)NH . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5158 1 6 HNCACB . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5158 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 5158 _NMR_spec_expt.ID 1 _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 . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 5158 _NMR_spec_expt.ID 2 _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 . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 5158 _NMR_spec_expt.ID 3 _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 . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 5158 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name (HCA)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 . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 5158 _NMR_spec_expt.ID 5 _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 . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 5158 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name HNCACB _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 5158 _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 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5158 1 H 1 H2O protons . . . . ppm 4.50 internal direct 1.0 internal cylindrical parallel . . . . . . 5158 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5158 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 5158 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $cond1 _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 HNCA 1 $sample_1 . 5158 1 2 HN(CO)CA 1 $sample_1 . 5158 1 3 HNCO 1 $sample_1 . 5158 1 4 (HCA)CO(CA)NH 1 $sample_1 . 5158 1 5 CBCA(CO)NH 1 $sample_1 . 5158 1 6 HNCACB 1 $sample_1 . 5158 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 CA C 13 62.40 0.05 . . . . . . . . . . 5158 1 2 . 1 1 1 1 VAL C C 13 175.12 0.05 . . . . . . . . . . 5158 1 3 . 1 1 2 2 LEU H H 1 8.15 0.02 . . . . . . . . . . 5158 1 4 . 1 1 2 2 LEU N N 15 125.50 0.05 . . . . . . . . . . 5158 1 5 . 1 1 2 2 LEU CA C 13 54.70 0.05 . . . . . . . . . . 5158 1 6 . 1 1 2 2 LEU C C 13 176.71 0.05 . . . . . . . . . . 5158 1 7 . 1 1 3 3 SER H H 1 8.34 0.02 . . . . . . . . . . 5158 1 8 . 1 1 3 3 SER N N 15 116.90 0.05 . . . . . . . . . . 5158 1 9 . 1 1 3 3 SER CA C 13 57.90 0.05 . . . . . . . . . . 5158 1 10 . 1 1 3 3 SER C C 13 174.84 0.05 . . . . . . . . . . 5158 1 11 . 1 1 4 4 GLU H H 1 8.69 0.02 . . . . . . . . . . 5158 1 12 . 1 1 4 4 GLU N N 15 122.00 0.05 . . . . . . . . . . 5158 1 13 . 1 1 4 4 GLU CA C 13 58.80 0.05 . . . . . . . . . . 5158 1 14 . 1 1 4 4 GLU C C 13 178.08 0.05 . . . . . . . . . . 5158 1 15 . 1 1 5 5 GLY H H 1 8.46 0.02 . . . . . . . . . . 5158 1 16 . 1 1 5 5 GLY N N 15 107.00 0.05 . . . . . . . . . . 5158 1 17 . 1 1 5 5 GLY CA C 13 46.50 0.05 . . . . . . . . . . 5158 1 18 . 1 1 5 5 GLY C C 13 176.00 0.05 . . . . . . . . . . 5158 1 19 . 1 1 6 6 GLU H H 1 7.90 0.02 . . . . . . . . . . 5158 1 20 . 1 1 6 6 GLU N N 15 121.30 0.05 . . . . . . . . . . 5158 1 21 . 1 1 6 6 GLU CA C 13 58.60 0.05 . . . . . . . . . . 5158 1 22 . 1 1 6 6 GLU C C 13 177.80 0.05 . . . . . . . . . . 5158 1 23 . 1 1 7 7 TRP CA C 13 59.60 0.05 . . . . . . . . . . 5158 1 24 . 1 1 7 7 TRP C C 13 177.40 0.05 . . . . . . . . . . 5158 1 25 . 1 1 8 8 GLN H H 1 8.03 0.02 . . . . . . . . . . 5158 1 26 . 1 1 8 8 GLN N N 15 116.50 0.05 . . . . . . . . . . 5158 1 27 . 1 1 8 8 GLN CA C 13 58.80 0.05 . . . . . . . . . . 5158 1 28 . 1 1 8 8 GLN C C 13 178.00 0.05 . . . . . . . . . . 5158 1 29 . 1 1 9 9 LEU H H 1 7.51 0.02 . . . . . . . . . . 5158 1 30 . 1 1 9 9 LEU N N 15 120.00 0.05 . . . . . . . . . . 5158 1 31 . 1 1 9 9 LEU CA C 13 57.90 0.05 . . . . . . . . . . 5158 1 32 . 1 1 9 9 LEU C C 13 178.65 0.05 . . . . . . . . . . 5158 1 33 . 1 1 10 10 VAL H H 1 7.84 0.02 . . . . . . . . . . 5158 1 34 . 1 1 10 10 VAL N N 15 118.80 0.05 . . . . . . . . . . 5158 1 35 . 1 1 10 10 VAL CA C 13 66.10 0.05 . . . . . . . . . . 5158 1 36 . 1 1 11 11 LEU H H 1 8.00 0.02 . . . . . . . . . . 5158 1 37 . 1 1 11 11 LEU N N 15 119.00 0.05 . . . . . . . . . . 5158 1 38 . 1 1 11 11 LEU CA C 13 57.50 0.05 . . . . . . . . . . 5158 1 39 . 1 1 11 11 LEU C C 13 178.85 0.05 . . . . . . . . . . 5158 1 40 . 1 1 12 12 HIS H H 1 7.92 0.02 . . . . . . . . . . 5158 1 41 . 1 1 12 12 HIS N N 15 116.30 0.05 . . . . . . . . . . 5158 1 42 . 1 1 12 12 HIS CA C 13 58.00 0.05 . . . . . . . . . . 5158 1 43 . 1 1 12 12 HIS C C 13 176.36 0.05 . . . . . . . . . . 5158 1 44 . 1 1 13 13 VAL H H 1 8.00 0.02 . . . . . . . . . . 5158 1 45 . 1 1 13 13 VAL N N 15 119.00 0.05 . . . . . . . . . . 5158 1 46 . 1 1 13 13 VAL CA C 13 65.20 0.05 . . . . . . . . . . 5158 1 47 . 1 1 13 13 VAL C C 13 177.10 0.05 . . . . . . . . . . 5158 1 48 . 1 1 14 14 TRP H H 1 8.33 0.02 . . . . . . . . . . 5158 1 49 . 1 1 14 14 TRP N N 15 121.20 0.05 . . . . . . . . . . 5158 1 50 . 1 1 14 14 TRP CA C 13 59.30 0.05 . . . . . . . . . . 5158 1 51 . 1 1 14 14 TRP C C 13 178.00 0.05 . . . . . . . . . . 5158 1 52 . 1 1 15 15 ALA H H 1 7.95 0.02 . . . . . . . . . . 5158 1 53 . 1 1 15 15 ALA N N 15 120.00 0.05 . . . . . . . . . . 5158 1 54 . 1 1 15 15 ALA CA C 13 54.10 0.05 . . . . . . . . . . 5158 1 55 . 1 1 15 15 ALA C C 13 178.82 0.05 . . . . . . . . . . 5158 1 56 . 1 1 16 16 LYS H H 1 7.57 0.02 . . . . . . . . . . 5158 1 57 . 1 1 16 16 LYS N N 15 117.10 0.05 . . . . . . . . . . 5158 1 58 . 1 1 16 16 LYS CA C 13 57.60 0.05 . . . . . . . . . . 5158 1 59 . 1 1 16 16 LYS C C 13 177.50 0.05 . . . . . . . . . . 5158 1 60 . 1 1 17 17 VAL H H 1 7.80 0.02 . . . . . . . . . . 5158 1 61 . 1 1 17 17 VAL N N 15 118.10 0.05 . . . . . . . . . . 5158 1 62 . 1 1 17 17 VAL CA C 13 64.00 0.05 . . . . . . . . . . 5158 1 63 . 1 1 17 17 VAL C C 13 176.90 0.05 . . . . . . . . . . 5158 1 64 . 1 1 18 18 GLU H H 1 8.06 0.02 . . . . . . . . . . 5158 1 65 . 1 1 18 18 GLU N N 15 120.30 0.05 . . . . . . . . . . 5158 1 66 . 1 1 18 18 GLU CA C 13 57.40 0.05 . . . . . . . . . . 5158 1 67 . 1 1 18 18 GLU C C 13 176.54 0.05 . . . . . . . . . . 5158 1 68 . 1 1 19 19 ALA H H 1 7.72 0.02 . . . . . . . . . . 5158 1 69 . 1 1 19 19 ALA N N 15 121.60 0.05 . . . . . . . . . . 5158 1 70 . 1 1 19 19 ALA CA C 13 53.30 0.05 . . . . . . . . . . 5158 1 71 . 1 1 19 19 ALA C C 13 177.98 0.05 . . . . . . . . . . 5158 1 72 . 1 1 20 20 ASP H H 1 7.95 0.02 . . . . . . . . . . 5158 1 73 . 1 1 20 20 ASP N N 15 117.90 0.05 . . . . . . . . . . 5158 1 74 . 1 1 20 20 ASP CA C 13 54.70 0.05 . . . . . . . . . . 5158 1 75 . 1 1 20 20 ASP C C 13 176.71 0.05 . . . . . . . . . . 5158 1 76 . 1 1 21 21 VAL H H 1 7.81 0.02 . . . . . . . . . . 5158 1 77 . 1 1 21 21 VAL N N 15 118.70 0.05 . . . . . . . . . . 5158 1 78 . 1 1 21 21 VAL CA C 13 63.30 0.05 . . . . . . . . . . 5158 1 79 . 1 1 21 21 VAL C C 13 176.37 0.05 . . . . . . . . . . 5158 1 80 . 1 1 22 22 ALA H H 1 8.05 0.02 . . . . . . . . . . 5158 1 81 . 1 1 22 22 ALA N N 15 124.10 0.05 . . . . . . . . . . 5158 1 82 . 1 1 22 22 ALA CA C 13 53.10 0.05 . . . . . . . . . . 5158 1 83 . 1 1 22 22 ALA C C 13 178.35 0.05 . . . . . . . . . . 5158 1 84 . 1 1 23 23 GLY H H 1 8.07 0.02 . . . . . . . . . . 5158 1 85 . 1 1 23 23 GLY N N 15 106.40 0.05 . . . . . . . . . . 5158 1 86 . 1 1 23 23 GLY CA C 13 45.70 0.05 . . . . . . . . . . 5158 1 87 . 1 1 23 23 GLY C C 13 174.57 0.05 . . . . . . . . . . 5158 1 88 . 1 1 24 24 HIS H H 1 8.21 0.02 . . . . . . . . . . 5158 1 89 . 1 1 24 24 HIS N N 15 117.20 0.05 . . . . . . . . . . 5158 1 90 . 1 1 24 24 HIS CA C 13 55.80 0.05 . . . . . . . . . . 5158 1 91 . 1 1 24 24 HIS C C 13 175.15 0.05 . . . . . . . . . . 5158 1 92 . 1 1 25 25 GLY H H 1 8.50 0.02 . . . . . . . . . . 5158 1 93 . 1 1 25 25 GLY N N 15 108.70 0.05 . . . . . . . . . . 5158 1 94 . 1 1 25 25 GLY CA C 13 46.20 0.05 . . . . . . . . . . 5158 1 95 . 1 1 25 25 GLY C C 13 174.63 0.05 . . . . . . . . . . 5158 1 96 . 1 1 26 26 GLN H H 1 8.28 0.02 . . . . . . . . . . 5158 1 97 . 1 1 26 26 GLN N N 15 119.30 0.05 . . . . . . . . . . 5158 1 98 . 1 1 26 26 GLN CA C 13 57.70 0.05 . . . . . . . . . . 5158 1 99 . 1 1 26 26 GLN C C 13 176.44 0.05 . . . . . . . . . . 5158 1 100 . 1 1 27 27 ASP H H 1 8.24 0.02 . . . . . . . . . . 5158 1 101 . 1 1 27 27 ASP N N 15 119.10 0.05 . . . . . . . . . . 5158 1 102 . 1 1 27 27 ASP CA C 13 56.10 0.05 . . . . . . . . . . 5158 1 103 . 1 1 27 27 ASP C C 13 177.54 0.05 . . . . . . . . . . 5158 1 104 . 1 1 28 28 ILE H H 1 7.72 0.02 . . . . . . . . . . 5158 1 105 . 1 1 28 28 ILE N N 15 119.10 0.05 . . . . . . . . . . 5158 1 106 . 1 1 28 28 ILE CA C 13 63.40 0.05 . . . . . . . . . . 5158 1 107 . 1 1 28 28 ILE C C 13 176.92 0.05 . . . . . . . . . . 5158 1 108 . 1 1 29 29 LEU H H 1 7.66 0.02 . . . . . . . . . . 5158 1 109 . 1 1 29 29 LEU N N 15 120.60 0.05 . . . . . . . . . . 5158 1 110 . 1 1 29 29 LEU CA C 13 57.50 0.05 . . . . . . . . . . 5158 1 111 . 1 1 29 29 LEU C C 13 178.11 0.05 . . . . . . . . . . 5158 1 112 . 1 1 30 30 ILE H H 1 7.72 0.02 . . . . . . . . . . 5158 1 113 . 1 1 30 30 ILE N N 15 117.50 0.05 . . . . . . . . . . 5158 1 114 . 1 1 30 30 ILE CA C 13 64.00 0.05 . . . . . . . . . . 5158 1 115 . 1 1 30 30 ILE C C 13 177.65 0.05 . . . . . . . . . . 5158 1 116 . 1 1 31 31 ARG H H 1 7.62 0.02 . . . . . . . . . . 5158 1 117 . 1 1 31 31 ARG N N 15 118.90 0.05 . . . . . . . . . . 5158 1 118 . 1 1 31 31 ARG CA C 13 58.80 0.05 . . . . . . . . . . 5158 1 119 . 1 1 31 31 ARG C C 13 178.45 0.05 . . . . . . . . . . 5158 1 120 . 1 1 32 32 LEU H H 1 7.85 0.02 . . . . . . . . . . 5158 1 121 . 1 1 32 32 LEU N N 15 120.10 0.05 . . . . . . . . . . 5158 1 122 . 1 1 32 32 LEU CA C 13 57.20 0.05 . . . . . . . . . . 5158 1 123 . 1 1 32 32 LEU C C 13 178.29 0.05 . . . . . . . . . . 5158 1 124 . 1 1 33 33 PHE H H 1 7.98 0.02 . . . . . . . . . . 5158 1 125 . 1 1 33 33 PHE N N 15 117.30 0.05 . . . . . . . . . . 5158 1 126 . 1 1 33 33 PHE CA C 13 58.80 0.05 . . . . . . . . . . 5158 1 127 . 1 1 33 33 PHE C C 13 176.72 0.05 . . . . . . . . . . 5158 1 128 . 1 1 34 34 LYS H H 1 7.86 0.02 . . . . . . . . . . 5158 1 129 . 1 1 34 34 LYS N N 15 118.30 0.05 . . . . . . . . . . 5158 1 130 . 1 1 34 34 LYS CA C 13 58.00 0.05 . . . . . . . . . . 5158 1 131 . 1 1 34 34 LYS C C 13 177.14 0.05 . . . . . . . . . . 5158 1 132 . 1 1 35 35 SER H H 1 7.81 0.02 . . . . . . . . . . 5158 1 133 . 1 1 35 35 SER N N 15 112.80 0.05 . . . . . . . . . . 5158 1 134 . 1 1 35 35 SER CA C 13 59.20 0.05 . . . . . . . . . . 5158 1 135 . 1 1 35 35 SER C C 13 173.12 0.05 . . . . . . . . . . 5158 1 136 . 1 1 36 36 HIS H H 1 8.10 0.02 . . . . . . . . . . 5158 1 137 . 1 1 36 36 HIS N N 15 118.50 0.05 . . . . . . . . . . 5158 1 138 . 1 1 36 36 HIS CA C 13 53.90 0.05 . . . . . . . . . . 5158 1 139 . 1 1 36 36 HIS C C 13 172.55 0.05 . . . . . . . . . . 5158 1 140 . 1 1 37 37 PRO CA C 13 64.80 0.05 . . . . . . . . . . 5158 1 141 . 1 1 37 37 PRO C C 13 177.61 0.05 . . . . . . . . . . 5158 1 142 . 1 1 38 38 GLU H H 1 9.38 0.02 . . . . . . . . . . 5158 1 143 . 1 1 38 38 GLU N N 15 120.50 0.05 . . . . . . . . . . 5158 1 144 . 1 1 38 38 GLU CA C 13 58.10 0.05 . . . . . . . . . . 5158 1 145 . 1 1 38 38 GLU C C 13 177.43 0.05 . . . . . . . . . . 5158 1 146 . 1 1 39 39 THR H H 1 7.99 0.02 . . . . . . . . . . 5158 1 147 . 1 1 39 39 THR N N 15 114.90 0.05 . . . . . . . . . . 5158 1 148 . 1 1 39 39 THR CA C 13 64.10 0.05 . . . . . . . . . . 5158 1 149 . 1 1 39 39 THR C C 13 175.16 0.05 . . . . . . . . . . 5158 1 150 . 1 1 40 40 LEU H H 1 7.66 0.02 . . . . . . . . . . 5158 1 151 . 1 1 40 40 LEU N N 15 122.00 0.05 . . . . . . . . . . 5158 1 152 . 1 1 40 40 LEU CA C 13 56.60 0.05 . . . . . . . . . . 5158 1 153 . 1 1 40 40 LEU C C 13 177.76 0.05 . . . . . . . . . . 5158 1 154 . 1 1 41 41 GLU H H 1 7.88 0.02 . . . . . . . . . . 5158 1 155 . 1 1 41 41 GLU N N 15 118.60 0.05 . . . . . . . . . . 5158 1 156 . 1 1 41 41 GLU CA C 13 57.60 0.05 . . . . . . . . . . 5158 1 157 . 1 1 41 41 GLU C C 13 177.44 0.05 . . . . . . . . . . 5158 1 158 . 1 1 42 42 LYS H H 1 7.79 0.02 . . . . . . . . . . 5158 1 159 . 1 1 42 42 LYS N N 15 119.00 0.05 . . . . . . . . . . 5158 1 160 . 1 1 42 42 LYS CA C 13 57.00 0.05 . . . . . . . . . . 5158 1 161 . 1 1 43 43 PHE CA C 13 58.60 0.05 . . . . . . . . . . 5158 1 162 . 1 1 43 43 PHE C C 13 175.98 0.05 . . . . . . . . . . 5158 1 163 . 1 1 44 44 ASP H H 1 8.15 0.02 . . . . . . . . . . 5158 1 164 . 1 1 44 44 ASP N N 15 121.00 0.05 . . . . . . . . . . 5158 1 165 . 1 1 44 44 ASP CA C 13 55.40 0.05 . . . . . . . . . . 5158 1 166 . 1 1 44 44 ASP C C 13 177.04 0.05 . . . . . . . . . . 5158 1 167 . 1 1 45 45 ARG H H 1 7.94 0.02 . . . . . . . . . . 5158 1 168 . 1 1 45 45 ARG N N 15 119.70 0.05 . . . . . . . . . . 5158 1 169 . 1 1 45 45 ARG CA C 13 57.80 0.05 . . . . . . . . . . 5158 1 170 . 1 1 45 45 ARG C C 13 176.92 0.05 . . . . . . . . . . 5158 1 171 . 1 1 46 46 PHE H H 1 7.89 0.02 . . . . . . . . . . 5158 1 172 . 1 1 46 46 PHE N N 15 118.10 0.05 . . . . . . . . . . 5158 1 173 . 1 1 46 46 PHE CA C 13 58.70 0.05 . . . . . . . . . . 5158 1 174 . 1 1 46 46 PHE C C 13 176.18 0.05 . . . . . . . . . . 5158 1 175 . 1 1 48 48 HIS CA C 13 55.80 0.05 . . . . . . . . . . 5158 1 176 . 1 1 48 48 HIS C C 13 174.68 0.05 . . . . . . . . . . 5158 1 177 . 1 1 49 49 LEU H H 1 7.97 0.02 . . . . . . . . . . 5158 1 178 . 1 1 49 49 LEU N N 15 122.20 0.05 . . . . . . . . . . 5158 1 179 . 1 1 49 49 LEU CA C 13 55.90 0.05 . . . . . . . . . . 5158 1 180 . 1 1 49 49 LEU C C 13 177.40 0.05 . . . . . . . . . . 5158 1 181 . 1 1 50 50 LYS H H 1 8.13 0.02 . . . . . . . . . . 5158 1 182 . 1 1 50 50 LYS N N 15 121.00 0.05 . . . . . . . . . . 5158 1 183 . 1 1 50 50 LYS CA C 13 57.00 0.05 . . . . . . . . . . 5158 1 184 . 1 1 50 50 LYS C C 13 176.97 0.05 . . . . . . . . . . 5158 1 185 . 1 1 51 51 THR H H 1 7.94 0.02 . . . . . . . . . . 5158 1 186 . 1 1 51 51 THR N N 15 113.80 0.05 . . . . . . . . . . 5158 1 187 . 1 1 51 51 THR CA C 13 62.80 0.05 . . . . . . . . . . 5158 1 188 . 1 1 51 51 THR C C 13 175.29 0.05 . . . . . . . . . . 5158 1 189 . 1 1 52 52 GLU H H 1 8.33 0.02 . . . . . . . . . . 5158 1 190 . 1 1 52 52 GLU N N 15 121.90 0.05 . . . . . . . . . . 5158 1 191 . 1 1 52 52 GLU CA C 13 58.20 0.05 . . . . . . . . . . 5158 1 192 . 1 1 52 52 GLU C C 13 177.25 0.05 . . . . . . . . . . 5158 1 193 . 1 1 53 53 ALA H H 1 8.10 0.02 . . . . . . . . . . 5158 1 194 . 1 1 53 53 ALA N N 15 122.40 0.05 . . . . . . . . . . 5158 1 195 . 1 1 53 53 ALA CA C 13 53.90 0.05 . . . . . . . . . . 5158 1 196 . 1 1 53 53 ALA C C 13 178.98 0.05 . . . . . . . . . . 5158 1 197 . 1 1 54 54 GLU H H 1 7.97 0.02 . . . . . . . . . . 5158 1 198 . 1 1 54 54 GLU N N 15 118.40 0.05 . . . . . . . . . . 5158 1 199 . 1 1 54 54 GLU CA C 13 57.70 0.05 . . . . . . . . . . 5158 1 200 . 1 1 54 54 GLU C C 13 177.60 0.05 . . . . . . . . . . 5158 1 201 . 1 1 55 55 MET H H 1 8.09 0.02 . . . . . . . . . . 5158 1 202 . 1 1 55 55 MET N N 15 120.10 0.05 . . . . . . . . . . 5158 1 203 . 1 1 55 55 MET CA C 13 56.90 0.05 . . . . . . . . . . 5158 1 204 . 1 1 55 55 MET C C 13 177.16 0.05 . . . . . . . . . . 5158 1 205 . 1 1 56 56 LYS H H 1 8.05 0.02 . . . . . . . . . . 5158 1 206 . 1 1 56 56 LYS N N 15 120.90 0.05 . . . . . . . . . . 5158 1 207 . 1 1 56 56 LYS CA C 13 57.30 0.05 . . . . . . . . . . 5158 1 208 . 1 1 56 56 LYS C C 13 177.06 0.05 . . . . . . . . . . 5158 1 209 . 1 1 57 57 ALA H H 1 8.00 0.02 . . . . . . . . . . 5158 1 210 . 1 1 57 57 ALA N N 15 123.00 0.05 . . . . . . . . . . 5158 1 211 . 1 1 57 57 ALA CA C 13 53.50 0.05 . . . . . . . . . . 5158 1 212 . 1 1 57 57 ALA C C 13 178.54 0.05 . . . . . . . . . . 5158 1 213 . 1 1 58 58 SER H H 1 7.96 0.02 . . . . . . . . . . 5158 1 214 . 1 1 58 58 SER N N 15 113.60 0.05 . . . . . . . . . . 5158 1 215 . 1 1 58 58 SER CA C 13 59.70 0.05 . . . . . . . . . . 5158 1 216 . 1 1 58 58 SER C C 13 175.55 0.05 . . . . . . . . . . 5158 1 217 . 1 1 59 59 GLU H H 1 8.12 0.02 . . . . . . . . . . 5158 1 218 . 1 1 59 59 GLU N N 15 122.00 0.05 . . . . . . . . . . 5158 1 219 . 1 1 59 59 GLU CA C 13 57.70 0.05 . . . . . . . . . . 5158 1 220 . 1 1 59 59 GLU C C 13 177.09 0.05 . . . . . . . . . . 5158 1 221 . 1 1 60 60 ASP H H 1 8.16 0.02 . . . . . . . . . . 5158 1 222 . 1 1 60 60 ASP N N 15 120.10 0.05 . . . . . . . . . . 5158 1 223 . 1 1 60 60 ASP CA C 13 55.50 0.05 . . . . . . . . . . 5158 1 224 . 1 1 60 60 ASP C C 13 177.35 0.05 . . . . . . . . . . 5158 1 225 . 1 1 61 61 LEU H H 1 7.90 0.02 . . . . . . . . . . 5158 1 226 . 1 1 61 61 LEU N N 15 121.50 0.05 . . . . . . . . . . 5158 1 227 . 1 1 61 61 LEU CA C 13 56.80 0.05 . . . . . . . . . . 5158 1 228 . 1 1 61 61 LEU C C 13 178.35 0.05 . . . . . . . . . . 5158 1 229 . 1 1 62 62 LYS H H 1 7.85 0.02 . . . . . . . . . . 5158 1 230 . 1 1 62 62 LYS N N 15 119.00 0.05 . . . . . . . . . . 5158 1 231 . 1 1 62 62 LYS CA C 13 57.50 0.05 . . . . . . . . . . 5158 1 232 . 1 1 62 62 LYS C C 13 176.89 0.05 . . . . . . . . . . 5158 1 233 . 1 1 63 63 LYS H H 1 7.72 0.02 . . . . . . . . . . 5158 1 234 . 1 1 63 63 LYS N N 15 118.70 0.05 . . . . . . . . . . 5158 1 235 . 1 1 63 63 LYS CA C 13 57.20 0.05 . . . . . . . . . . 5158 1 236 . 1 1 63 63 LYS C C 13 176.82 0.05 . . . . . . . . . . 5158 1 237 . 1 1 64 64 HIS H H 1 8.09 0.02 . . . . . . . . . . 5158 1 238 . 1 1 64 64 HIS N N 15 117.40 0.05 . . . . . . . . . . 5158 1 239 . 1 1 64 64 HIS CA C 13 55.70 0.05 . . . . . . . . . . 5158 1 240 . 1 1 64 64 HIS C C 13 174.97 0.05 . . . . . . . . . . 5158 1 241 . 1 1 65 65 GLY H H 1 8.20 0.02 . . . . . . . . . . 5158 1 242 . 1 1 65 65 GLY N N 15 109.00 0.05 . . . . . . . . . . 5158 1 243 . 1 1 65 65 GLY CA C 13 45.60 0.05 . . . . . . . . . . 5158 1 244 . 1 1 65 65 GLY C C 13 173.95 0.05 . . . . . . . . . . 5158 1 245 . 1 1 66 66 VAL H H 1 7.90 0.02 . . . . . . . . . . 5158 1 246 . 1 1 66 66 VAL N N 15 118.90 0.05 . . . . . . . . . . 5158 1 247 . 1 1 66 66 VAL CA C 13 62.90 0.05 . . . . . . . . . . 5158 1 248 . 1 1 66 66 VAL C C 13 176.38 0.05 . . . . . . . . . . 5158 1 249 . 1 1 67 67 THR H H 1 8.08 0.02 . . . . . . . . . . 5158 1 250 . 1 1 67 67 THR N N 15 117.90 0.05 . . . . . . . . . . 5158 1 251 . 1 1 67 67 THR CA C 13 62.90 0.05 . . . . . . . . . . 5158 1 252 . 1 1 67 67 THR C C 13 174.66 0.05 . . . . . . . . . . 5158 1 253 . 1 1 68 68 VAL H H 1 7.99 0.02 . . . . . . . . . . 5158 1 254 . 1 1 68 68 VAL N N 15 122.00 0.05 . . . . . . . . . . 5158 1 255 . 1 1 68 68 VAL CA C 13 63.10 0.05 . . . . . . . . . . 5158 1 256 . 1 1 68 68 VAL C C 13 176.04 0.05 . . . . . . . . . . 5158 1 257 . 1 1 69 69 LEU H H 1 8.09 0.02 . . . . . . . . . . 5158 1 258 . 1 1 69 69 LEU N N 15 123.70 0.05 . . . . . . . . . . 5158 1 259 . 1 1 69 69 LEU CA C 13 56.00 0.05 . . . . . . . . . . 5158 1 260 . 1 1 69 69 LEU C C 13 177.94 0.05 . . . . . . . . . . 5158 1 261 . 1 1 70 70 THR H H 1 7.88 0.02 . . . . . . . . . . 5158 1 262 . 1 1 70 70 THR N N 15 114.10 0.05 . . . . . . . . . . 5158 1 263 . 1 1 70 70 THR CA C 13 63.00 0.05 . . . . . . . . . . 5158 1 264 . 1 1 70 70 THR C C 13 174.94 0.05 . . . . . . . . . . 5158 1 265 . 1 1 71 71 ALA H H 1 8.04 0.02 . . . . . . . . . . 5158 1 266 . 1 1 71 71 ALA N N 15 125.30 0.05 . . . . . . . . . . 5158 1 267 . 1 1 71 71 ALA CA C 13 53.30 0.05 . . . . . . . . . . 5158 1 268 . 1 1 71 71 ALA C C 13 178.22 0.05 . . . . . . . . . . 5158 1 269 . 1 1 72 72 LEU H H 1 7.97 0.02 . . . . . . . . . . 5158 1 270 . 1 1 72 72 LEU N N 15 119.50 0.05 . . . . . . . . . . 5158 1 271 . 1 1 72 72 LEU CA C 13 56.30 0.05 . . . . . . . . . . 5158 1 272 . 1 1 72 72 LEU C C 13 178.21 0.05 . . . . . . . . . . 5158 1 273 . 1 1 73 73 GLY H H 1 8.12 0.02 . . . . . . . . . . 5158 1 274 . 1 1 73 73 GLY N N 15 107.10 0.05 . . . . . . . . . . 5158 1 275 . 1 1 73 73 GLY CA C 13 46.10 0.05 . . . . . . . . . . 5158 1 276 . 1 1 73 73 GLY C C 13 174.65 0.05 . . . . . . . . . . 5158 1 277 . 1 1 74 74 ALA H H 1 7.80 0.02 . . . . . . . . . . 5158 1 278 . 1 1 74 74 ALA N N 15 122.60 0.05 . . . . . . . . . . 5158 1 279 . 1 1 74 74 ALA CA C 13 53.30 0.05 . . . . . . . . . . 5158 1 280 . 1 1 74 74 ALA C C 13 178.45 0.05 . . . . . . . . . . 5158 1 281 . 1 1 75 75 ILE H H 1 7.72 0.02 . . . . . . . . . . 5158 1 282 . 1 1 75 75 ILE N N 15 118.10 0.05 . . . . . . . . . . 5158 1 283 . 1 1 75 75 ILE CA C 13 62.30 0.05 . . . . . . . . . . 5158 1 284 . 1 1 75 75 ILE C C 13 176.80 0.05 . . . . . . . . . . 5158 1 285 . 1 1 76 76 LEU H H 1 7.93 0.02 . . . . . . . . . . 5158 1 286 . 1 1 76 76 LEU N N 15 122.90 0.05 . . . . . . . . . . 5158 1 287 . 1 1 76 76 LEU CA C 13 55.90 0.05 . . . . . . . . . . 5158 1 288 . 1 1 76 76 LEU C C 13 177.60 0.05 . . . . . . . . . . 5158 1 289 . 1 1 77 77 LYS H H 1 7.84 0.02 . . . . . . . . . . 5158 1 290 . 1 1 77 77 LYS N N 15 120.30 0.05 . . . . . . . . . . 5158 1 291 . 1 1 77 77 LYS CA C 13 56.70 0.05 . . . . . . . . . . 5158 1 292 . 1 1 77 77 LYS C C 13 176.63 0.05 . . . . . . . . . . 5158 1 293 . 1 1 78 78 LYS H H 1 7.91 0.02 . . . . . . . . . . 5158 1 294 . 1 1 78 78 LYS N N 15 121.00 0.05 . . . . . . . . . . 5158 1 295 . 1 1 78 78 LYS CA C 13 56.70 0.05 . . . . . . . . . . 5158 1 296 . 1 1 78 78 LYS C C 13 176.55 0.05 . . . . . . . . . . 5158 1 297 . 1 1 79 79 LYS H H 1 8.08 0.02 . . . . . . . . . . 5158 1 298 . 1 1 79 79 LYS N N 15 121.60 0.05 . . . . . . . . . . 5158 1 299 . 1 1 79 79 LYS CA C 13 56.70 0.05 . . . . . . . . . . 5158 1 300 . 1 1 79 79 LYS C C 13 176.93 0.05 . . . . . . . . . . 5158 1 301 . 1 1 80 80 GLY H H 1 8.22 0.02 . . . . . . . . . . 5158 1 302 . 1 1 80 80 GLY N N 15 109.10 0.05 . . . . . . . . . . 5158 1 303 . 1 1 80 80 GLY CA C 13 45.10 0.05 . . . . . . . . . . 5158 1 304 . 1 1 80 80 GLY C C 13 173.59 0.05 . . . . . . . . . . 5158 1 305 . 1 1 81 81 HIS H H 1 8.21 0.02 . . . . . . . . . . 5158 1 306 . 1 1 81 81 HIS N N 15 117.90 0.05 . . . . . . . . . . 5158 1 307 . 1 1 81 81 HIS CA C 13 55.10 0.05 . . . . . . . . . . 5158 1 308 . 1 1 81 81 HIS C C 13 177.67 0.05 . . . . . . . . . . 5158 1 309 . 1 1 82 82 HIS H H 1 8.10 0.02 . . . . . . . . . . 5158 1 310 . 1 1 82 82 HIS N N 15 116.80 0.05 . . . . . . . . . . 5158 1 311 . 1 1 82 82 HIS CA C 13 55.60 0.05 . . . . . . . . . . 5158 1 312 . 1 1 82 82 HIS C C 13 174.23 0.05 . . . . . . . . . . 5158 1 313 . 1 1 83 83 GLU H H 1 8.53 0.02 . . . . . . . . . . 5158 1 314 . 1 1 83 83 GLU N N 15 122.50 0.05 . . . . . . . . . . 5158 1 315 . 1 1 83 83 GLU CA C 13 56.90 0.05 . . . . . . . . . . 5158 1 316 . 1 1 83 83 GLU C C 13 175.97 0.05 . . . . . . . . . . 5158 1 317 . 1 1 84 84 ALA H H 1 8.21 0.02 . . . . . . . . . . 5158 1 318 . 1 1 84 84 ALA N N 15 124.00 0.05 . . . . . . . . . . 5158 1 319 . 1 1 84 84 ALA CA C 13 52.60 0.05 . . . . . . . . . . 5158 1 320 . 1 1 84 84 ALA C C 13 177.33 0.05 . . . . . . . . . . 5158 1 321 . 1 1 85 85 GLU H H 1 8.10 0.02 . . . . . . . . . . 5158 1 322 . 1 1 85 85 GLU N N 15 119.40 0.05 . . . . . . . . . . 5158 1 323 . 1 1 85 85 GLU CA C 13 56.30 0.05 . . . . . . . . . . 5158 1 324 . 1 1 85 85 GLU C C 13 176.01 0.05 . . . . . . . . . . 5158 1 325 . 1 1 86 86 LEU H H 1 8.00 0.02 . . . . . . . . . . 5158 1 326 . 1 1 86 86 LEU N N 15 123.00 0.05 . . . . . . . . . . 5158 1 327 . 1 1 86 86 LEU CA C 13 55.10 0.05 . . . . . . . . . . 5158 1 328 . 1 1 86 86 LEU C C 13 176.72 0.05 . . . . . . . . . . 5158 1 329 . 1 1 87 87 LYS H H 1 8.05 0.02 . . . . . . . . . . 5158 1 330 . 1 1 87 87 LYS N N 15 122.80 0.05 . . . . . . . . . . 5158 1 331 . 1 1 87 87 LYS CA C 13 54.30 0.05 . . . . . . . . . . 5158 1 332 . 1 1 88 88 PRO CA C 13 63.30 0.05 . . . . . . . . . . 5158 1 333 . 1 1 88 88 PRO C C 13 176.89 0.05 . . . . . . . . . . 5158 1 334 . 1 1 89 89 LEU H H 1 8.08 0.02 . . . . . . . . . . 5158 1 335 . 1 1 89 89 LEU N N 15 121.80 0.05 . . . . . . . . . . 5158 1 336 . 1 1 89 89 LEU CA C 13 55.30 0.05 . . . . . . . . . . 5158 1 337 . 1 1 89 89 LEU C C 13 177.26 0.05 . . . . . . . . . . 5158 1 338 . 1 1 90 90 ALA H H 1 8.07 0.02 . . . . . . . . . . 5158 1 339 . 1 1 90 90 ALA N N 15 124.10 0.05 . . . . . . . . . . 5158 1 340 . 1 1 90 90 ALA CA C 13 52.60 0.05 . . . . . . . . . . 5158 1 341 . 1 1 90 90 ALA C C 13 177.61 0.05 . . . . . . . . . . 5158 1 342 . 1 1 91 91 GLN H H 1 8.11 0.02 . . . . . . . . . . 5158 1 343 . 1 1 91 91 GLN N N 15 118.90 0.05 . . . . . . . . . . 5158 1 344 . 1 1 91 91 GLN CA C 13 55.80 0.05 . . . . . . . . . . 5158 1 345 . 1 1 91 91 GLN C C 13 175.98 0.05 . . . . . . . . . . 5158 1 346 . 1 1 92 92 SER H H 1 8.10 0.02 . . . . . . . . . . 5158 1 347 . 1 1 92 92 SER N N 15 116.20 0.05 . . . . . . . . . . 5158 1 348 . 1 1 92 92 SER CA C 13 58.50 0.05 . . . . . . . . . . 5158 1 349 . 1 1 92 92 SER C C 13 174.58 0.05 . . . . . . . . . . 5158 1 350 . 1 1 93 93 HIS H H 1 8.15 0.02 . . . . . . . . . . 5158 1 351 . 1 1 93 93 HIS N N 15 121.00 0.05 . . . . . . . . . . 5158 1 352 . 1 1 93 93 HIS CA C 13 55.40 0.05 . . . . . . . . . . 5158 1 353 . 1 1 93 93 HIS C C 13 174.08 0.05 . . . . . . . . . . 5158 1 354 . 1 1 94 94 ALA H H 1 8.12 0.02 . . . . . . . . . . 5158 1 355 . 1 1 94 94 ALA N N 15 124.40 0.05 . . . . . . . . . . 5158 1 356 . 1 1 94 94 ALA CA C 13 52.60 0.05 . . . . . . . . . . 5158 1 357 . 1 1 94 94 ALA C C 13 177.61 0.05 . . . . . . . . . . 5158 1 358 . 1 1 95 95 THR H H 1 8.00 0.02 . . . . . . . . . . 5158 1 359 . 1 1 95 95 THR N N 15 112.70 0.05 . . . . . . . . . . 5158 1 360 . 1 1 95 95 THR CA C 13 62.00 0.05 . . . . . . . . . . 5158 1 361 . 1 1 95 95 THR C C 13 174.33 0.05 . . . . . . . . . . 5158 1 362 . 1 1 96 96 LYS H H 1 8.12 0.02 . . . . . . . . . . 5158 1 363 . 1 1 96 96 LYS N N 15 123.00 0.05 . . . . . . . . . . 5158 1 364 . 1 1 96 96 LYS CA C 13 56.30 0.05 . . . . . . . . . . 5158 1 365 . 1 1 96 96 LYS C C 13 176.53 0.05 . . . . . . . . . . 5158 1 366 . 1 1 97 97 HIS H H 1 8.06 0.02 . . . . . . . . . . 5158 1 367 . 1 1 97 97 HIS N N 15 122.10 0.05 . . . . . . . . . . 5158 1 368 . 1 1 97 97 HIS CA C 13 55.10 0.05 . . . . . . . . . . 5158 1 369 . 1 1 97 97 HIS C C 13 174.07 0.05 . . . . . . . . . . 5158 1 370 . 1 1 98 98 LYS H H 1 8.26 0.02 . . . . . . . . . . 5158 1 371 . 1 1 98 98 LYS N N 15 122.90 0.05 . . . . . . . . . . 5158 1 372 . 1 1 98 98 LYS CA C 13 56.30 0.05 . . . . . . . . . . 5158 1 373 . 1 1 98 98 LYS C C 13 175.86 0.05 . . . . . . . . . . 5158 1 374 . 1 1 99 99 ILE H H 1 8.04 0.02 . . . . . . . . . . 5158 1 375 . 1 1 99 99 ILE N N 15 123.30 0.05 . . . . . . . . . . 5158 1 376 . 1 1 99 99 ILE CA C 13 58.60 0.05 . . . . . . . . . . 5158 1 377 . 1 1 100 100 PRO CA C 13 63.10 0.05 . . . . . . . . . . 5158 1 378 . 1 1 100 100 PRO C C 13 176.88 0.05 . . . . . . . . . . 5158 1 379 . 1 1 101 101 ILE H H 1 8.00 0.02 . . . . . . . . . . 5158 1 380 . 1 1 101 101 ILE N N 15 121.80 0.05 . . . . . . . . . . 5158 1 381 . 1 1 101 101 ILE CA C 13 62.40 0.05 . . . . . . . . . . 5158 1 382 . 1 1 101 101 ILE C C 13 176.53 0.05 . . . . . . . . . . 5158 1 383 . 1 1 102 102 LYS H H 1 8.18 0.02 . . . . . . . . . . 5158 1 384 . 1 1 102 102 LYS N N 15 122.40 0.05 . . . . . . . . . . 5158 1 385 . 1 1 102 102 LYS CA C 13 57.30 0.05 . . . . . . . . . . 5158 1 386 . 1 1 103 103 TYR H H 1 8.13 0.02 . . . . . . . . . . 5158 1 387 . 1 1 103 103 TYR N N 15 117.40 0.05 . . . . . . . . . . 5158 1 388 . 1 1 103 103 TYR CA C 13 56.00 0.05 . . . . . . . . . . 5158 1 389 . 1 1 104 104 LEU H H 1 7.90 0.02 . . . . . . . . . . 5158 1 390 . 1 1 104 104 LEU N N 15 118.90 0.05 . . . . . . . . . . 5158 1 391 . 1 1 104 104 LEU CA C 13 58.30 0.05 . . . . . . . . . . 5158 1 392 . 1 1 104 104 LEU C C 13 177.72 0.05 . . . . . . . . . . 5158 1 393 . 1 1 105 105 GLU H H 1 8.26 0.02 . . . . . . . . . . 5158 1 394 . 1 1 105 105 GLU N N 15 119.90 0.05 . . . . . . . . . . 5158 1 395 . 1 1 105 105 GLU CA C 13 59.50 0.05 . . . . . . . . . . 5158 1 396 . 1 1 106 106 PHE CA C 13 59.10 0.05 . . . . . . . . . . 5158 1 397 . 1 1 107 107 ILE H H 1 7.88 0.02 . . . . . . . . . . 5158 1 398 . 1 1 107 107 ILE N N 15 119.70 0.05 . . . . . . . . . . 5158 1 399 . 1 1 107 107 ILE CA C 13 62.60 0.05 . . . . . . . . . . 5158 1 400 . 1 1 107 107 ILE C C 13 176.45 0.05 . . . . . . . . . . 5158 1 401 . 1 1 108 108 SER H H 1 7.90 0.02 . . . . . . . . . . 5158 1 402 . 1 1 108 108 SER N N 15 116.60 0.05 . . . . . . . . . . 5158 1 403 . 1 1 108 108 SER CA C 13 60.40 0.05 . . . . . . . . . . 5158 1 404 . 1 1 109 109 GLU CA C 13 58.10 0.05 . . . . . . . . . . 5158 1 405 . 1 1 109 109 GLU C C 13 177.20 0.05 . . . . . . . . . . 5158 1 406 . 1 1 110 110 ALA H H 1 7.92 0.02 . . . . . . . . . . 5158 1 407 . 1 1 110 110 ALA N N 15 122.20 0.05 . . . . . . . . . . 5158 1 408 . 1 1 110 110 ALA CA C 13 54.20 0.05 . . . . . . . . . . 5158 1 409 . 1 1 110 110 ALA C C 13 178.93 0.05 . . . . . . . . . . 5158 1 410 . 1 1 111 111 ILE H H 1 7.74 0.02 . . . . . . . . . . 5158 1 411 . 1 1 111 111 ILE N N 15 117.30 0.05 . . . . . . . . . . 5158 1 412 . 1 1 111 111 ILE CA C 13 63.20 0.05 . . . . . . . . . . 5158 1 413 . 1 1 111 111 ILE C C 13 176.37 0.05 . . . . . . . . . . 5158 1 414 . 1 1 112 112 ILE H H 1 8.08 0.02 . . . . . . . . . . 5158 1 415 . 1 1 112 112 ILE N N 15 117.90 0.05 . . . . . . . . . . 5158 1 416 . 1 1 112 112 ILE CA C 13 62.90 0.05 . . . . . . . . . . 5158 1 417 . 1 1 112 112 ILE C C 13 177.05 0.05 . . . . . . . . . . 5158 1 418 . 1 1 113 113 HIS H H 1 8.06 0.02 . . . . . . . . . . 5158 1 419 . 1 1 113 113 HIS N N 15 118.70 0.05 . . . . . . . . . . 5158 1 420 . 1 1 113 113 HIS CA C 13 57.20 0.05 . . . . . . . . . . 5158 1 421 . 1 1 116 116 HIS CA C 13 55.60 0.05 . . . . . . . . . . 5158 1 422 . 1 1 116 116 HIS C C 13 174.52 0.05 . . . . . . . . . . 5158 1 423 . 1 1 117 117 SER H H 1 7.88 0.02 . . . . . . . . . . 5158 1 424 . 1 1 117 117 SER N N 15 115.30 0.05 . . . . . . . . . . 5158 1 425 . 1 1 117 117 SER CA C 13 58.70 0.05 . . . . . . . . . . 5158 1 426 . 1 1 117 117 SER C C 13 174.21 0.05 . . . . . . . . . . 5158 1 427 . 1 1 118 118 ARG H H 1 8.12 0.02 . . . . . . . . . . 5158 1 428 . 1 1 118 118 ARG N N 15 121.30 0.05 . . . . . . . . . . 5158 1 429 . 1 1 118 118 ARG CA C 13 56.20 0.05 . . . . . . . . . . 5158 1 430 . 1 1 118 118 ARG C C 13 175.67 0.05 . . . . . . . . . . 5158 1 431 . 1 1 119 119 HIS H H 1 8.31 0.02 . . . . . . . . . . 5158 1 432 . 1 1 119 119 HIS N N 15 119.20 0.05 . . . . . . . . . . 5158 1 433 . 1 1 119 119 HIS CA C 13 53.30 0.05 . . . . . . . . . . 5158 1 434 . 1 1 120 120 PRO CA C 13 64.20 0.05 . . . . . . . . . . 5158 1 435 . 1 1 120 120 PRO C C 13 177.38 0.05 . . . . . . . . . . 5158 1 436 . 1 1 121 121 GLY H H 1 8.38 0.02 . . . . . . . . . . 5158 1 437 . 1 1 121 121 GLY N N 15 108.80 0.05 . . . . . . . . . . 5158 1 438 . 1 1 121 121 GLY CA C 13 45.40 0.05 . . . . . . . . . . 5158 1 439 . 1 1 121 121 GLY C C 13 173.84 0.05 . . . . . . . . . . 5158 1 440 . 1 1 122 122 ASP H H 1 7.86 0.02 . . . . . . . . . . 5158 1 441 . 1 1 122 122 ASP N N 15 119.70 0.05 . . . . . . . . . . 5158 1 442 . 1 1 122 122 ASP CA C 13 54.20 0.05 . . . . . . . . . . 5158 1 443 . 1 1 122 122 ASP C C 13 175.96 0.05 . . . . . . . . . . 5158 1 444 . 1 1 123 123 PHE H H 1 8.08 0.02 . . . . . . . . . . 5158 1 445 . 1 1 123 123 PHE N N 15 120.00 0.05 . . . . . . . . . . 5158 1 446 . 1 1 123 123 PHE CA C 13 58.00 0.05 . . . . . . . . . . 5158 1 447 . 1 1 123 123 PHE C C 13 176.16 0.05 . . . . . . . . . . 5158 1 448 . 1 1 124 124 GLY H H 1 8.19 0.02 . . . . . . . . . . 5158 1 449 . 1 1 124 124 GLY N N 15 109.30 0.05 . . . . . . . . . . 5158 1 450 . 1 1 124 124 GLY CA C 13 45.40 0.05 . . . . . . . . . . 5158 1 451 . 1 1 124 124 GLY C C 13 174.05 0.05 . . . . . . . . . . 5158 1 452 . 1 1 125 125 ALA H H 1 8.00 0.02 . . . . . . . . . . 5158 1 453 . 1 1 125 125 ALA N N 15 123.00 0.05 . . . . . . . . . . 5158 1 454 . 1 1 125 125 ALA CA C 13 52.90 0.05 . . . . . . . . . . 5158 1 455 . 1 1 125 125 ALA C C 13 177.06 0.05 . . . . . . . . . . 5158 1 456 . 1 1 126 126 ASP H H 1 8.19 0.02 . . . . . . . . . . 5158 1 457 . 1 1 126 126 ASP N N 15 118.00 0.05 . . . . . . . . . . 5158 1 458 . 1 1 126 126 ASP CA C 13 54.20 0.05 . . . . . . . . . . 5158 1 459 . 1 1 126 126 ASP C C 13 176.24 0.05 . . . . . . . . . . 5158 1 460 . 1 1 127 127 ALA H H 1 8.00 0.02 . . . . . . . . . . 5158 1 461 . 1 1 127 127 ALA N N 15 123.60 0.05 . . . . . . . . . . 5158 1 462 . 1 1 127 127 ALA CA C 13 53.30 0.05 . . . . . . . . . . 5158 1 463 . 1 1 127 127 ALA C C 13 178.01 0.05 . . . . . . . . . . 5158 1 464 . 1 1 128 128 GLN H H 1 8.13 0.02 . . . . . . . . . . 5158 1 465 . 1 1 128 128 GLN N N 15 117.40 0.05 . . . . . . . . . . 5158 1 466 . 1 1 128 128 GLN CA C 13 56.90 0.05 . . . . . . . . . . 5158 1 467 . 1 1 128 128 GLN C C 13 177.08 0.05 . . . . . . . . . . 5158 1 468 . 1 1 129 129 GLY H H 1 8.16 0.02 . . . . . . . . . . 5158 1 469 . 1 1 129 129 GLY N N 15 108.45 0.05 . . . . . . . . . . 5158 1 470 . 1 1 129 129 GLY CA C 13 45.70 0.05 . . . . . . . . . . 5158 1 471 . 1 1 129 129 GLY C C 13 174.58 0.05 . . . . . . . . . . 5158 1 472 . 1 1 130 130 ALA H H 1 8.04 0.02 . . . . . . . . . . 5158 1 473 . 1 1 130 130 ALA N N 15 123.30 0.05 . . . . . . . . . . 5158 1 474 . 1 1 130 130 ALA CA C 13 53.40 0.05 . . . . . . . . . . 5158 1 475 . 1 1 130 130 ALA C C 13 178.49 0.05 . . . . . . . . . . 5158 1 476 . 1 1 131 131 MET H H 1 8.18 0.02 . . . . . . . . . . 5158 1 477 . 1 1 131 131 MET N N 15 117.60 0.05 . . . . . . . . . . 5158 1 478 . 1 1 131 131 MET CA C 13 56.60 0.05 . . . . . . . . . . 5158 1 479 . 1 1 131 131 MET C C 13 177.11 0.05 . . . . . . . . . . 5158 1 480 . 1 1 132 132 GLY H H 1 8.12 0.02 . . . . . . . . . . 5158 1 481 . 1 1 132 132 GLY N N 15 107.80 0.05 . . . . . . . . . . 5158 1 482 . 1 1 132 132 GLY CA C 13 46.10 0.05 . . . . . . . . . . 5158 1 483 . 1 1 132 132 GLY C C 13 174.94 0.05 . . . . . . . . . . 5158 1 484 . 1 1 133 133 LYS H H 1 7.87 0.02 . . . . . . . . . . 5158 1 485 . 1 1 133 133 LYS N N 15 120.40 0.05 . . . . . . . . . . 5158 1 486 . 1 1 133 133 LYS CA C 13 57.50 0.05 . . . . . . . . . . 5158 1 487 . 1 1 133 133 LYS C C 13 177.06 0.05 . . . . . . . . . . 5158 1 488 . 1 1 134 134 ALA H H 1 8.00 0.02 . . . . . . . . . . 5158 1 489 . 1 1 134 134 ALA N N 15 122.90 0.05 . . . . . . . . . . 5158 1 490 . 1 1 134 134 ALA CA C 13 53.20 0.05 . . . . . . . . . . 5158 1 491 . 1 1 134 134 ALA C C 13 177.99 0.05 . . . . . . . . . . 5158 1 492 . 1 1 135 135 LEU H H 1 7.94 0.02 . . . . . . . . . . 5158 1 493 . 1 1 135 135 LEU N N 15 119.10 0.05 . . . . . . . . . . 5158 1 494 . 1 1 135 135 LEU CA C 13 56.10 0.05 . . . . . . . . . . 5158 1 495 . 1 1 135 135 LEU C C 13 178.11 0.05 . . . . . . . . . . 5158 1 496 . 1 1 136 136 GLY H H 1 8.03 0.02 . . . . . . . . . . 5158 1 497 . 1 1 136 136 GLY N N 15 107.20 0.05 . . . . . . . . . . 5158 1 498 . 1 1 136 136 GLY CA C 13 45.90 0.05 . . . . . . . . . . 5158 1 499 . 1 1 136 136 GLY C C 13 174.54 0.05 . . . . . . . . . . 5158 1 500 . 1 1 137 137 LEU H H 1 7.70 0.02 . . . . . . . . . . 5158 1 501 . 1 1 137 137 LEU N N 15 120.70 0.05 . . . . . . . . . . 5158 1 502 . 1 1 137 137 LEU CA C 13 55.90 0.05 . . . . . . . . . . 5158 1 503 . 1 1 137 137 LEU C C 13 177.22 0.05 . . . . . . . . . . 5158 1 504 . 1 1 139 139 ARG CA C 13 56.80 0.05 . . . . . . . . . . 5158 1 505 . 1 1 139 139 ARG C C 13 176.51 0.05 . . . . . . . . . . 5158 1 506 . 1 1 140 140 LYS H H 1 8.15 0.02 . . . . . . . . . . 5158 1 507 . 1 1 140 140 LYS N N 15 121.30 0.05 . . . . . . . . . . 5158 1 508 . 1 1 140 140 LYS CA C 13 57.70 0.05 . . . . . . . . . . 5158 1 509 . 1 1 140 140 LYS C C 13 176.77 0.05 . . . . . . . . . . 5158 1 510 . 1 1 141 141 ASP H H 1 8.28 0.02 . . . . . . . . . . 5158 1 511 . 1 1 141 141 ASP N N 15 119.30 0.05 . . . . . . . . . . 5158 1 512 . 1 1 141 141 ASP CA C 13 54.90 0.05 . . . . . . . . . . 5158 1 513 . 1 1 141 141 ASP C C 13 176.78 0.05 . . . . . . . . . . 5158 1 514 . 1 1 142 142 ILE H H 1 7.73 0.02 . . . . . . . . . . 5158 1 515 . 1 1 142 142 ILE N N 15 119.60 0.05 . . . . . . . . . . 5158 1 516 . 1 1 142 142 ILE CA C 13 62.30 0.05 . . . . . . . . . . 5158 1 517 . 1 1 142 142 ILE C C 13 176.37 0.05 . . . . . . . . . . 5158 1 518 . 1 1 143 143 ALA H H 1 7.98 0.02 . . . . . . . . . . 5158 1 519 . 1 1 143 143 ALA N N 15 124.20 0.05 . . . . . . . . . . 5158 1 520 . 1 1 143 143 ALA CA C 13 53.60 0.05 . . . . . . . . . . 5158 1 521 . 1 1 143 143 ALA C C 13 178.35 0.05 . . . . . . . . . . 5158 1 522 . 1 1 144 144 ALA H H 1 7.79 0.02 . . . . . . . . . . 5158 1 523 . 1 1 144 144 ALA N N 15 120.60 0.05 . . . . . . . . . . 5158 1 524 . 1 1 144 144 ALA CA C 13 53.60 0.05 . . . . . . . . . . 5158 1 525 . 1 1 144 144 ALA C C 13 178.50 0.05 . . . . . . . . . . 5158 1 526 . 1 1 145 145 LYS H H 1 7.80 0.02 . . . . . . . . . . 5158 1 527 . 1 1 145 145 LYS N N 15 118.10 0.05 . . . . . . . . . . 5158 1 528 . 1 1 145 145 LYS CA C 13 57.20 0.05 . . . . . . . . . . 5158 1 529 . 1 1 145 145 LYS C C 13 176.92 0.05 . . . . . . . . . . 5158 1 530 . 1 1 146 146 TYR H H 1 7.78 0.02 . . . . . . . . . . 5158 1 531 . 1 1 146 146 TYR N N 15 118.50 0.05 . . . . . . . . . . 5158 1 532 . 1 1 146 146 TYR CA C 13 58.60 0.05 . . . . . . . . . . 5158 1 533 . 1 1 146 146 TYR C C 13 176.40 0.05 . . . . . . . . . . 5158 1 534 . 1 1 147 147 LYS H H 1 7.81 0.02 . . . . . . . . . . 5158 1 535 . 1 1 147 147 LYS N N 15 119.50 0.05 . . . . . . . . . . 5158 1 536 . 1 1 147 147 LYS CA C 13 57.60 0.05 . . . . . . . . . . 5158 1 537 . 1 1 147 147 LYS C C 13 177.07 0.05 . . . . . . . . . . 5158 1 538 . 1 1 148 148 GLU H H 1 8.10 0.02 . . . . . . . . . . 5158 1 539 . 1 1 148 148 GLU N N 15 119.70 0.05 . . . . . . . . . . 5158 1 540 . 1 1 148 148 GLU CA C 13 57.00 0.05 . . . . . . . . . . 5158 1 541 . 1 1 148 148 GLU C C 13 176.49 0.05 . . . . . . . . . . 5158 1 542 . 1 1 149 149 LEU H H 1 7.89 0.02 . . . . . . . . . . 5158 1 543 . 1 1 149 149 LEU N N 15 120.70 0.05 . . . . . . . . . . 5158 1 544 . 1 1 149 149 LEU CA C 13 55.50 0.05 . . . . . . . . . . 5158 1 545 . 1 1 149 149 LEU C C 13 177.52 0.05 . . . . . . . . . . 5158 1 546 . 1 1 150 150 GLY H H 1 8.02 0.02 . . . . . . . . . . 5158 1 547 . 1 1 150 150 GLY N N 15 107.50 0.05 . . . . . . . . . . 5158 1 548 . 1 1 150 150 GLY CA C 13 45.38 0.05 . . . . . . . . . . 5158 1 549 . 1 1 150 150 GLY C C 13 173.83 0.05 . . . . . . . . . . 5158 1 550 . 1 1 151 151 TYR H H 1 7.78 0.02 . . . . . . . . . . 5158 1 551 . 1 1 151 151 TYR N N 15 119.58 0.05 . . . . . . . . . . 5158 1 552 . 1 1 151 151 TYR CA C 13 58.19 0.05 . . . . . . . . . . 5158 1 553 . 1 1 151 151 TYR C C 13 175.41 0.05 . . . . . . . . . . 5158 1 554 . 1 1 152 152 GLN H H 1 8.10 0.02 . . . . . . . . . . 5158 1 555 . 1 1 152 152 GLN N N 15 122.41 0.05 . . . . . . . . . . 5158 1 556 . 1 1 152 152 GLN CA C 13 55.69 0.05 . . . . . . . . . . 5158 1 557 . 1 1 152 152 GLN C C 13 174.82 0.05 . . . . . . . . . . 5158 1 558 . 1 1 153 153 GLY H H 1 7.32 0.02 . . . . . . . . . . 5158 1 559 . 1 1 153 153 GLY N N 15 114.64 0.05 . . . . . . . . . . 5158 1 560 . 1 1 153 153 GLY CA C 13 45.87 0.05 . . . . . . . . . . 5158 1 561 . 1 1 153 153 GLY C C 13 178.12 0.05 . . . . . . . . . . 5158 1 stop_ save_