data_7428 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 7428 _Entry.Title ; Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2008-07-02 _Entry.Accession_date 2008-07-02 _Entry.Last_release_date 2008-08-07 _Entry.Original_release_date 2008-08-07 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.8.116 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _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 Jordan Chill . H. . 7428 2 John Louis . M. . 7428 3 Frank Delaglio . . . 7428 4 Ad Bax . . . 7428 stop_ loop_ _Entry_src.ID _Entry_src.Project_name _Entry_src.Organization_full_name _Entry_src.Organization_initials _Entry_src.Entry_ID . . 'National Institutes of Health' . 7428 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 4 7428 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 284 7428 '15N chemical shifts' 139 7428 '1H chemical shifts' 139 7428 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 . . 2008-08-07 2008-07-02 original author . 7428 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 7428 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 17945182 _Citation.Full_citation . _Citation.Title 'Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Biochim. Biophys. Acta.' _Citation.Journal_name_full . _Citation.Journal_volume 1768 _Citation.Journal_issue 12 _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 3260 _Citation.Page_last 3270 _Citation.Year 2007 _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 Jordan Chill . H. . 7428 1 2 John Louis . M. . 7428 1 3 Frank Delaglio . . . 7428 1 4 Ad Bax . . . 7428 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID KcsA 7428 1 NMR 7428 1 'potassium channel' 7428 1 stop_ save_ save_reference_citation _Citation.Sf_category citations _Citation.Sf_framecode reference_citation _Citation.Entry_ID 7428 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 16522799 _Citation.Full_citation . _Citation.Title 'NMR study of the tetrameric KcsA potassium channel in detergent micelles.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full . _Citation.Journal_volume 15 _Citation.Journal_issue 4 _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 684 _Citation.Page_last 698 _Citation.Year 2006 _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 Jordan Chill . H. . 7428 2 2 John Louis . M. . 7428 2 3 C. Miller . . . 7428 2 4 Ad Bax . . . 7428 2 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 7428 _Assembly.ID 1 _Assembly.Name KcsA _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 . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . 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 'KcsA, 1' 1 $KcsA A . yes native no no . . . 7428 1 2 'KcsA, 2' 1 $KcsA B . yes native no no . . . 7428 1 3 'KcsA, 3' 1 $KcsA C . yes native no no . . . 7428 1 4 'KcsA, 4' 1 $KcsA D . yes native no no . . . 7428 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_KcsA _Entity.Sf_category entity _Entity.Sf_framecode KcsA _Entity.Entry_ID 7428 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name KcsA _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 ; LLGRHGSALHWRAAGAATVL LVIVLLAGSYLAVLAERGAP GAQLITYPRALWWSVETATT VGYGDLYPVTLWGRLVAVVV MVAGITSFGLVTAALATWFV GREQERRGHFVRHSEKAAEE AYTRTTRALHERFDRLERML DDNRR ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details 'The first residue with number 1 is in reality the 16th residue.' _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 145 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment 'N-terminal deletion mutant KcsA potassium channel' _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 15853 . KcsA . . . . . 100.00 145 100.00 100.00 1.85e-95 . . . . 7428 1 2 no PDB 1BL8 . "Potassium Channel (Kcsa) From Streptomyces Lividans" . . . . . 66.90 97 98.97 98.97 9.21e-57 . . . . 7428 1 3 no PDB 1F6G . "Potassium Channel (Kcsa) Full-Length Fold" . . . . . 100.00 160 97.93 97.93 2.83e-93 . . . . 7428 1 4 no PDB 1J95 . "Kcsa Potassium Channel With Tba (Tetrabutylammonium) And Potassium" . . . . . 75.86 125 99.09 99.09 2.63e-67 . . . . 7428 1 5 no PDB 1JVM . "Kcsa Potassium Channel With Tba (Tetrabutylammonium) And Rubidium" . . . . . 75.86 125 99.09 99.09 2.02e-67 . . . . 7428 1 6 no PDB 1K4C . "Potassium Channel Kcsa-Fab Complex In High Concentration Of K+" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 7 no PDB 1K4D . "Potassium Channel Kcsa-Fab Complex In Low Concentration Of K+" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 8 no PDB 1R3I . "Potassium Channel Kcsa-Fab Complex In Rb+" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 9 no PDB 1R3J . "Potassium Channel Kcsa-Fab Complex In High Concentration Of Tl+" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 10 no PDB 1R3K . "Potassium Channel Kcsa-Fab Complex In Low Concentration Of Tl+" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 11 no PDB 1R3L . "Potassium Channel Kcsa-Fab Complex In Cs+" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 12 no PDB 1S5H . "Potassium Channel Kcsa-Fab Complex T75c Mutant In K+" . . . . . 75.17 124 99.08 99.08 2.27e-66 . . . . 7428 1 13 no PDB 1ZWI . "Structure Of Mutant Kcsa Potassium Channel" . . . . . 70.34 103 98.04 98.04 7.95e-60 . . . . 7428 1 14 no PDB 2ATK . "Structure Of A Mutant Kcsa K+ Channel" . . . . . 75.17 124 98.17 98.17 1.41e-65 . . . . 7428 1 15 no PDB 2BOB . "Potassium Channel Kcsa-Fab Complex In Thallium With Tetrabutylammonium (Tba)" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 16 no PDB 2BOC . "Potassium Channel Kcsa-Fab Complex In Thallium With Tetraethylarsonium (Teas)" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 17 no PDB 2DWD . "Crystal Structure Of Kcsa-Fab-Tba Complex In Tl+" . . . . . 71.03 103 99.03 99.03 8.97e-62 . . . . 7428 1 18 no PDB 2DWE . "Crystal Structure Of Kcsa-Fab-Tba Complex In Rb+" . . . . . 71.03 103 99.03 99.03 8.97e-62 . . . . 7428 1 19 no PDB 2HJF . "Potassium Channel Kcsa-Fab Complex With Tetrabutylammonium (Tba)" . . . . . 71.03 103 99.03 99.03 8.97e-62 . . . . 7428 1 20 no PDB 2HVJ . "Crystal Structure Of Kcsa-fab-tba Complex In Low K+" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 21 no PDB 2HVK . "Crystal Structure Of The Kcsa-Fab-Tba Complex In High K+" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 22 no PDB 2IH1 . "Ion Selectivity In A Semi-Synthetic K+ Channel Locked In The Conductive Conformation" . . . . . 73.79 122 97.20 98.13 4.70e-63 . . . . 7428 1 23 no PDB 2IH3 . "Ion Selectivity In A Semi-Synthetic K+ Channel Locked In The Conductive Conformation" . . . . . 73.79 122 97.20 98.13 4.70e-63 . . . . 7428 1 24 no PDB 2ITC . "Potassium Channel Kcsa-Fab Complex In Sodium Chloride" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 25 no PDB 2ITD . "Potassium Channel Kcsa-Fab Complex In Barium Chloride" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 26 no PDB 2JK5 . "Potassium Channel Kcsa In Complex With Tetrabutylammonium In High K" . . . . . 75.17 124 99.08 99.08 2.62e-66 . . . . 7428 1 27 no PDB 2NLJ . "Potassium Channel Kcsa(M96v)-Fab Complex In Kcl" . . . . . 75.17 124 98.17 99.08 1.34e-65 . . . . 7428 1 28 no PDB 2P7T . "Crystal Structure Of Kcsa Mutant" . . . . . 71.03 103 98.06 98.06 3.86e-61 . . . . 7428 1 29 no PDB 2QTO . "An Anisotropic Model For Potassium Channel Kcsa" . . . . . 66.90 97 98.97 98.97 9.21e-57 . . . . 7428 1 30 no PDB 2W0F . "Potassium Channel Kcsa-fab Complex With Tetraoctylammonium" . . . . . 75.17 124 99.08 99.08 2.62e-66 . . . . 7428 1 31 no PDB 3EFF . "The Crystal Structure Of Full-Length Kcsa In Its Closed Conformation" . . . . . 95.86 139 100.00 100.00 3.61e-91 . . . . 7428 1 32 no PDB 3F5W . "Kcsa Potassium Channel In The Open-Inactivated State With 32 A Opening At T112" . . . . . 65.52 104 97.89 97.89 4.80e-54 . . . . 7428 1 33 no PDB 3F7V . "Kcsa Potassium Channel In The Open-Inactivated State With 23 A Opening At T112" . . . . . 65.52 104 97.89 97.89 4.80e-54 . . . . 7428 1 34 no PDB 3F7Y . "Kcsa Potassium Channel In The Partially Open State With 17 A Opening At T112" . . . . . 65.52 104 97.89 97.89 4.80e-54 . . . . 7428 1 35 no PDB 3FB5 . "Kcsa Potassium Channel In The Partially Open State With 14.5 A Opening At T112" . . . . . 65.52 104 97.89 97.89 4.80e-54 . . . . 7428 1 36 no PDB 3FB6 . "Kcsa Potassium Channel In The Partially Open State With 16 A Opening At T112" . . . . . 65.52 104 97.89 97.89 4.80e-54 . . . . 7428 1 37 no PDB 3FB7 . "Open Kcsa Potassium Channel In The Presence Of Rb+ Ion" . . . . . 65.52 104 97.89 97.89 4.80e-54 . . . . 7428 1 38 no PDB 3FB8 . "Kcsa Potassium Channel In The Open-Conductive State With 20 At T112 In The Presence Of Rb+ Ion" . . . . . 65.52 104 97.89 97.89 4.80e-54 . . . . 7428 1 39 no PDB 3GB7 . "Potassium Channel Kcsa-Fab Complex In Li+" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 40 no PDB 3HPL . "Kcsa E71h-F103a Mutant In The Closed State" . . . . . 75.17 124 97.25 97.25 3.40e-64 . . . . 7428 1 41 no PDB 3IGA . "Potassium Channel Kcsa-fab Complex In Li+ And K+" . . . . . 75.17 124 99.08 99.08 2.37e-66 . . . . 7428 1 42 no PDB 3OGC . "Kcsa E71a Variant In Presence Of Na+" . . . . . 75.17 131 99.08 99.08 9.90e-66 . . . . 7428 1 43 no PDB 3OR6 . "On The Structural Basis Of Modal Gating Behavior In K+channels - E71q" . . . . . 71.03 103 98.06 99.03 2.03e-61 . . . . 7428 1 44 no PDB 3OR7 . "On The Structural Basis Of Modal Gating Behavior In K+channels - E71i" . . . . . 71.03 103 98.06 98.06 1.47e-60 . . . . 7428 1 45 no PDB 3STL . "Kcsa Potassium Channel Mutant Y82c With Cadmium Bound" . . . . . 71.03 103 99.03 99.03 3.66e-61 . . . . 7428 1 46 no PDB 3STZ . "Kcsa Potassium Channel Mutant Y82c With Nitroxide Spin Label" . . . . . 70.34 102 99.02 99.02 1.68e-60 . . . . 7428 1 47 no PDB 4LBE . "Structure Of Kcsa With R122a Mutation" . . . . . 75.17 130 99.08 99.08 1.07e-65 . . . . 7428 1 48 no PDB 4LCU . "Structure Of Kcsa With E118a Mutation" . . . . . 75.17 131 99.08 99.08 9.90e-66 . . . . 7428 1 49 no PDB 4MSW . "Y78 Ester Mutant Of Kcsa In High K+" . . . . . 71.03 103 99.03 99.03 4.54e-61 . . . . 7428 1 50 no PDB 4UUJ . "Potassium Channel Kcsa-fab With Tetrahexylammonium" . . . . . 71.72 111 99.04 99.04 1.15e-62 . . . . 7428 1 51 no EMBL CAA86025 . "potassium channel protein [Streptomyces lividans 1326]" . . . . . 100.00 160 100.00 100.00 1.39e-95 . . . . 7428 1 52 no EMBL CAC16993 . "voltage-gated potassium channel [Streptomyces coelicolor A3(2)]" . . . . . 100.00 160 100.00 100.00 1.39e-95 . . . . 7428 1 53 no GB AIJ11233 . "Voltage-gated potassium channel [Streptomyces lividans TK24]" . . . . . 100.00 157 100.00 100.00 1.00e-95 . . . . 7428 1 54 no GB EFD64549 . "voltage-gated potassium channel [Streptomyces lividans TK24]" . . . . . 100.00 160 100.00 100.00 1.39e-95 . . . . 7428 1 55 no GB EOY52587 . "Voltage-gated potassium channel [Streptomyces lividans 1326]" . . . . . 100.00 157 100.00 100.00 1.00e-95 . . . . 7428 1 56 no REF NP_631700 . "voltage-gated potassium channel [Streptomyces coelicolor A3(2)]" . . . . . 100.00 160 100.00 100.00 1.39e-95 . . . . 7428 1 57 no REF WP_003971485 . "voltage-gated potassium channel [Streptomyces coelicolor]" . . . . . 100.00 160 100.00 100.00 1.39e-95 . . . . 7428 1 58 no REF WP_016328171 . "Voltage-gated potassium channel [Streptomyces lividans]" . . . . . 100.00 157 100.00 100.00 1.00e-95 . . . . 7428 1 59 no REF WP_030864493 . "voltage-gated potassium channel [Streptomyces violaceoruber]" . . . . . 100.00 157 97.93 99.31 4.82e-94 . . . . 7428 1 60 no SP P0A333 . "RecName: Full=pH-gated potassium channel KcsA [Streptomyces coelicolor A3(2)]" . . . . . 100.00 160 100.00 100.00 1.39e-95 . . . . 7428 1 61 no SP P0A334 . "RecName: Full=pH-gated potassium channel KcsA; AltName: Full=Streptomyces lividans K+ channel; Short=SKC1 [Streptomyces lividan" . . . . . 100.00 160 100.00 100.00 1.39e-95 . . . . 7428 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'selective conduction of K+ ions across the cell membrane' 7428 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 16 LEU . 7428 1 2 17 LEU . 7428 1 3 18 GLY . 7428 1 4 19 ARG . 7428 1 5 20 HIS . 7428 1 6 21 GLY . 7428 1 7 22 SER . 7428 1 8 23 ALA . 7428 1 9 24 LEU . 7428 1 10 25 HIS . 7428 1 11 26 TRP . 7428 1 12 27 ARG . 7428 1 13 28 ALA . 7428 1 14 29 ALA . 7428 1 15 30 GLY . 7428 1 16 31 ALA . 7428 1 17 32 ALA . 7428 1 18 33 THR . 7428 1 19 34 VAL . 7428 1 20 35 LEU . 7428 1 21 36 LEU . 7428 1 22 37 VAL . 7428 1 23 38 ILE . 7428 1 24 39 VAL . 7428 1 25 40 LEU . 7428 1 26 41 LEU . 7428 1 27 42 ALA . 7428 1 28 43 GLY . 7428 1 29 44 SER . 7428 1 30 45 TYR . 7428 1 31 46 LEU . 7428 1 32 47 ALA . 7428 1 33 48 VAL . 7428 1 34 49 LEU . 7428 1 35 50 ALA . 7428 1 36 51 GLU . 7428 1 37 52 ARG . 7428 1 38 53 GLY . 7428 1 39 54 ALA . 7428 1 40 55 PRO . 7428 1 41 56 GLY . 7428 1 42 57 ALA . 7428 1 43 58 GLN . 7428 1 44 59 LEU . 7428 1 45 60 ILE . 7428 1 46 61 THR . 7428 1 47 62 TYR . 7428 1 48 63 PRO . 7428 1 49 64 ARG . 7428 1 50 65 ALA . 7428 1 51 66 LEU . 7428 1 52 67 TRP . 7428 1 53 68 TRP . 7428 1 54 69 SER . 7428 1 55 70 VAL . 7428 1 56 71 GLU . 7428 1 57 72 THR . 7428 1 58 73 ALA . 7428 1 59 74 THR . 7428 1 60 75 THR . 7428 1 61 76 VAL . 7428 1 62 77 GLY . 7428 1 63 78 TYR . 7428 1 64 79 GLY . 7428 1 65 80 ASP . 7428 1 66 81 LEU . 7428 1 67 82 TYR . 7428 1 68 83 PRO . 7428 1 69 84 VAL . 7428 1 70 85 THR . 7428 1 71 86 LEU . 7428 1 72 87 TRP . 7428 1 73 88 GLY . 7428 1 74 89 ARG . 7428 1 75 90 LEU . 7428 1 76 91 VAL . 7428 1 77 92 ALA . 7428 1 78 93 VAL . 7428 1 79 94 VAL . 7428 1 80 95 VAL . 7428 1 81 96 MET . 7428 1 82 97 VAL . 7428 1 83 98 ALA . 7428 1 84 99 GLY . 7428 1 85 100 ILE . 7428 1 86 101 THR . 7428 1 87 102 SER . 7428 1 88 103 PHE . 7428 1 89 104 GLY . 7428 1 90 105 LEU . 7428 1 91 106 VAL . 7428 1 92 107 THR . 7428 1 93 108 ALA . 7428 1 94 109 ALA . 7428 1 95 110 LEU . 7428 1 96 111 ALA . 7428 1 97 112 THR . 7428 1 98 113 TRP . 7428 1 99 114 PHE . 7428 1 100 115 VAL . 7428 1 101 116 GLY . 7428 1 102 117 ARG . 7428 1 103 118 GLU . 7428 1 104 119 GLN . 7428 1 105 120 GLU . 7428 1 106 121 ARG . 7428 1 107 122 ARG . 7428 1 108 123 GLY . 7428 1 109 124 HIS . 7428 1 110 125 PHE . 7428 1 111 126 VAL . 7428 1 112 127 ARG . 7428 1 113 128 HIS . 7428 1 114 129 SER . 7428 1 115 130 GLU . 7428 1 116 131 LYS . 7428 1 117 132 ALA . 7428 1 118 133 ALA . 7428 1 119 134 GLU . 7428 1 120 135 GLU . 7428 1 121 136 ALA . 7428 1 122 137 TYR . 7428 1 123 138 THR . 7428 1 124 139 ARG . 7428 1 125 140 THR . 7428 1 126 141 THR . 7428 1 127 142 ARG . 7428 1 128 143 ALA . 7428 1 129 144 LEU . 7428 1 130 145 HIS . 7428 1 131 146 GLU . 7428 1 132 147 ARG . 7428 1 133 148 PHE . 7428 1 134 149 ASP . 7428 1 135 150 ARG . 7428 1 136 151 LEU . 7428 1 137 152 GLU . 7428 1 138 153 ARG . 7428 1 139 154 MET . 7428 1 140 155 LEU . 7428 1 141 156 ASP . 7428 1 142 157 ASP . 7428 1 143 158 ASN . 7428 1 144 159 ARG . 7428 1 145 160 ARG . 7428 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 . LEU 1 1 7428 1 . LEU 2 2 7428 1 . GLY 3 3 7428 1 . ARG 4 4 7428 1 . HIS 5 5 7428 1 . GLY 6 6 7428 1 . SER 7 7 7428 1 . ALA 8 8 7428 1 . LEU 9 9 7428 1 . HIS 10 10 7428 1 . TRP 11 11 7428 1 . ARG 12 12 7428 1 . ALA 13 13 7428 1 . ALA 14 14 7428 1 . GLY 15 15 7428 1 . ALA 16 16 7428 1 . ALA 17 17 7428 1 . THR 18 18 7428 1 . VAL 19 19 7428 1 . LEU 20 20 7428 1 . LEU 21 21 7428 1 . VAL 22 22 7428 1 . ILE 23 23 7428 1 . VAL 24 24 7428 1 . LEU 25 25 7428 1 . LEU 26 26 7428 1 . ALA 27 27 7428 1 . GLY 28 28 7428 1 . SER 29 29 7428 1 . TYR 30 30 7428 1 . LEU 31 31 7428 1 . ALA 32 32 7428 1 . VAL 33 33 7428 1 . LEU 34 34 7428 1 . ALA 35 35 7428 1 . GLU 36 36 7428 1 . ARG 37 37 7428 1 . GLY 38 38 7428 1 . ALA 39 39 7428 1 . PRO 40 40 7428 1 . GLY 41 41 7428 1 . ALA 42 42 7428 1 . GLN 43 43 7428 1 . LEU 44 44 7428 1 . ILE 45 45 7428 1 . THR 46 46 7428 1 . TYR 47 47 7428 1 . PRO 48 48 7428 1 . ARG 49 49 7428 1 . ALA 50 50 7428 1 . LEU 51 51 7428 1 . TRP 52 52 7428 1 . TRP 53 53 7428 1 . SER 54 54 7428 1 . VAL 55 55 7428 1 . GLU 56 56 7428 1 . THR 57 57 7428 1 . ALA 58 58 7428 1 . THR 59 59 7428 1 . THR 60 60 7428 1 . VAL 61 61 7428 1 . GLY 62 62 7428 1 . TYR 63 63 7428 1 . GLY 64 64 7428 1 . ASP 65 65 7428 1 . LEU 66 66 7428 1 . TYR 67 67 7428 1 . PRO 68 68 7428 1 . VAL 69 69 7428 1 . THR 70 70 7428 1 . LEU 71 71 7428 1 . TRP 72 72 7428 1 . GLY 73 73 7428 1 . ARG 74 74 7428 1 . LEU 75 75 7428 1 . VAL 76 76 7428 1 . ALA 77 77 7428 1 . VAL 78 78 7428 1 . VAL 79 79 7428 1 . VAL 80 80 7428 1 . MET 81 81 7428 1 . VAL 82 82 7428 1 . ALA 83 83 7428 1 . GLY 84 84 7428 1 . ILE 85 85 7428 1 . THR 86 86 7428 1 . SER 87 87 7428 1 . PHE 88 88 7428 1 . GLY 89 89 7428 1 . LEU 90 90 7428 1 . VAL 91 91 7428 1 . THR 92 92 7428 1 . ALA 93 93 7428 1 . ALA 94 94 7428 1 . LEU 95 95 7428 1 . ALA 96 96 7428 1 . THR 97 97 7428 1 . TRP 98 98 7428 1 . PHE 99 99 7428 1 . VAL 100 100 7428 1 . GLY 101 101 7428 1 . ARG 102 102 7428 1 . GLU 103 103 7428 1 . GLN 104 104 7428 1 . GLU 105 105 7428 1 . ARG 106 106 7428 1 . ARG 107 107 7428 1 . GLY 108 108 7428 1 . HIS 109 109 7428 1 . PHE 110 110 7428 1 . VAL 111 111 7428 1 . ARG 112 112 7428 1 . HIS 113 113 7428 1 . SER 114 114 7428 1 . GLU 115 115 7428 1 . LYS 116 116 7428 1 . ALA 117 117 7428 1 . ALA 118 118 7428 1 . GLU 119 119 7428 1 . GLU 120 120 7428 1 . ALA 121 121 7428 1 . TYR 122 122 7428 1 . THR 123 123 7428 1 . ARG 124 124 7428 1 . THR 125 125 7428 1 . THR 126 126 7428 1 . ARG 127 127 7428 1 . ALA 128 128 7428 1 . LEU 129 129 7428 1 . HIS 130 130 7428 1 . GLU 131 131 7428 1 . ARG 132 132 7428 1 . PHE 133 133 7428 1 . ASP 134 134 7428 1 . ARG 135 135 7428 1 . LEU 136 136 7428 1 . GLU 137 137 7428 1 . ARG 138 138 7428 1 . MET 139 139 7428 1 . LEU 140 140 7428 1 . ASP 141 141 7428 1 . ASP 142 142 7428 1 . ASN 143 143 7428 1 . ARG 144 144 7428 1 . ARG 145 145 7428 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 7428 _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 $KcsA . 1902 organism . 'Streptomyces coelicolor' . . . bacteria . Streptomyces coelicolor . . . . . . . . . . . . . . . . . . . . . 7428 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 7428 _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 $KcsA . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pET11a . . . . . . 7428 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_4_for_TableS5 _Sample.Sf_category sample _Sample.Sf_framecode sample_4_for_TableS5 _Sample.Entry_ID 7428 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system SDS _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 KcsA 'natural abundance' . . 1 $KcsA . . 0.5-0.6 . . mM . . . . 7428 1 2 MES 'natural abundance' . . . . . . 25 . . mM . . . . 7428 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_2 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_2 _Sample_condition_list.Entry_ID 7428 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 6 . pH 7428 1 pressure 14.1 . Torr 7428 1 temperature 323 . K 7428 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe_NMRDraw _Software.Sf_category software _Software.Sf_framecode NMRPipe_NMRDraw _Software.Entry_ID 7428 _Software.ID 1 _Software.Name NMRPipe/NMRDraw _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID NIH . . 7428 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 7428 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 7428 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 7428 _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 spectrometer_1 Bruker DRX . 600 . . . 7428 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 7428 _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 '3D HNCO' no . . . . . . . . . . 1 $sample_4_for_TableS5 isotropic . . 2 $sample_conditions_2 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7428 1 2 '3D HN(CA)CO' no . . . . . . . . . . 1 $sample_4_for_TableS5 isotropic . . 2 $sample_conditions_2 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7428 1 3 '3D HNCA' no . . . . . . . . . . 1 $sample_4_for_TableS5 isotropic . . 2 $sample_conditions_2 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 7428 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 7428 _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 0.00 na indirect 0.251449530 . . . . . . . . . 7428 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 7428 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 7428 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_4 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_4 _Assigned_chem_shift_list.Entry_ID 7428 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 2 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_2 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _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 '3D HNCO' 4 $sample_4_for_TableS5 . 7428 1 2 '3D HN(CA)CO' 4 $sample_4_for_TableS5 . 7428 1 3 '3D HNCA' 4 $sample_4_for_TableS5 . 7428 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 LEU H H 1 8.22 0.02 . 1 . . . . 16 LEU H . 7428 1 2 . 1 1 1 1 LEU C C 13 177.4 0.1 . 1 . . . . 16 LEU C . 7428 1 3 . 1 1 1 1 LEU CA C 13 56.5 0.1 . 1 . . . . 16 LEU CA . 7428 1 4 . 1 1 1 1 LEU N N 15 122.6 0.02 . 1 . . . . 16 LEU N . 7428 1 5 . 1 1 2 2 LEU H H 1 7.68 0.02 . 1 . . . . 17 LEU H . 7428 1 6 . 1 1 2 2 LEU C C 13 177.8 0.1 . 1 . . . . 17 LEU C . 7428 1 7 . 1 1 2 2 LEU CA C 13 54.9 0.1 . 1 . . . . 17 LEU CA . 7428 1 8 . 1 1 2 2 LEU N N 15 117.6 0.02 . 1 . . . . 17 LEU N . 7428 1 9 . 1 1 3 3 GLY H H 1 7.95 0.02 . 1 . . . . 18 GLY H . 7428 1 10 . 1 1 3 3 GLY C C 13 175.2 0.1 . 1 . . . . 18 GLY C . 7428 1 11 . 1 1 3 3 GLY CA C 13 45.5 0.1 . 1 . . . . 18 GLY CA . 7428 1 12 . 1 1 3 3 GLY N N 15 107.9 0.02 . 1 . . . . 18 GLY N . 7428 1 13 . 1 1 4 4 ARG H H 1 7.78 0.02 . 1 . . . . 19 ARG H . 7428 1 14 . 1 1 4 4 ARG C C 13 177 0.1 . 1 . . . . 19 ARG C . 7428 1 15 . 1 1 4 4 ARG CA C 13 56.4 0.1 . 1 . . . . 19 ARG CA . 7428 1 16 . 1 1 4 4 ARG N N 15 119.5 0.02 . 1 . . . . 19 ARG N . 7428 1 17 . 1 1 5 5 HIS H H 1 8.2 0.02 . 1 . . . . 20 HIS H . 7428 1 18 . 1 1 5 5 HIS C C 13 175.2 0.1 . 1 . . . . 20 HIS C . 7428 1 19 . 1 1 5 5 HIS CA C 13 55.4 0.1 . 1 . . . . 20 HIS CA . 7428 1 20 . 1 1 5 5 HIS N N 15 117.4 0.02 . 1 . . . . 20 HIS N . 7428 1 21 . 1 1 6 6 GLY H H 1 8.05 0.02 . 1 . . . . 21 GLY H . 7428 1 22 . 1 1 6 6 GLY C C 13 174.6 0.1 . 1 . . . . 21 GLY C . 7428 1 23 . 1 1 6 6 GLY CA C 13 45.6 0.1 . 1 . . . . 21 GLY CA . 7428 1 24 . 1 1 6 6 GLY N N 15 109.1 0.02 . 1 . . . . 21 GLY N . 7428 1 25 . 1 1 7 7 SER H H 1 7.83 0.02 . 1 . . . . 22 SER H . 7428 1 26 . 1 1 7 7 SER C C 13 174.6 0.1 . 1 . . . . 22 SER C . 7428 1 27 . 1 1 7 7 SER CA C 13 58.4 0.1 . 1 . . . . 22 SER CA . 7428 1 28 . 1 1 7 7 SER N N 15 115.6 0.02 . 1 . . . . 22 SER N . 7428 1 29 . 1 1 8 8 ALA H H 1 7.94 0.02 . 1 . . . . 23 ALA H . 7428 1 30 . 1 1 8 8 ALA C C 13 177.4 0.1 . 1 . . . . 23 ALA C . 7428 1 31 . 1 1 8 8 ALA CA C 13 52.5 0.1 . 1 . . . . 23 ALA CA . 7428 1 32 . 1 1 8 8 ALA N N 15 124.9 0.02 . 1 . . . . 23 ALA N . 7428 1 33 . 1 1 9 9 LEU H H 1 7.54 0.02 . 1 . . . . 24 LEU H . 7428 1 34 . 1 1 9 9 LEU C C 13 176.8 0.1 . 1 . . . . 24 LEU C . 7428 1 35 . 1 1 9 9 LEU CA C 13 54.9 0.1 . 1 . . . . 24 LEU CA . 7428 1 36 . 1 1 9 9 LEU N N 15 118.7 0.02 . 1 . . . . 24 LEU N . 7428 1 37 . 1 1 10 10 HIS H H 1 7.77 0.02 . 1 . . . . 25 HIS H . 7428 1 38 . 1 1 10 10 HIS C C 13 174.4 0.1 . 1 . . . . 25 HIS C . 7428 1 39 . 1 1 10 10 HIS CA C 13 54.6 0.1 . 1 . . . . 25 HIS CA . 7428 1 40 . 1 1 10 10 HIS N N 15 117.9 0.02 . 1 . . . . 25 HIS N . 7428 1 41 . 1 1 11 11 TRP H H 1 7.68 0.02 . 1 . . . . 26 TRP H . 7428 1 42 . 1 1 11 11 TRP C C 13 176.8 0.1 . 1 . . . . 26 TRP C . 7428 1 43 . 1 1 11 11 TRP CA C 13 57.9 0.1 . 1 . . . . 26 TRP CA . 7428 1 44 . 1 1 11 11 TRP N N 15 121.6 0.02 . 1 . . . . 26 TRP N . 7428 1 45 . 1 1 12 12 ARG H H 1 7.73 0.02 . 1 . . . . 27 ARG H . 7428 1 46 . 1 1 12 12 ARG C C 13 176.5 0.1 . 1 . . . . 27 ARG C . 7428 1 47 . 1 1 12 12 ARG CA C 13 56.2 0.1 . 1 . . . . 27 ARG CA . 7428 1 48 . 1 1 12 12 ARG N N 15 120.1 0.02 . 1 . . . . 27 ARG N . 7428 1 49 . 1 1 13 13 ALA H H 1 7.81 0.02 . 1 . . . . 28 ALA H . 7428 1 50 . 1 1 13 13 ALA C C 13 178.5 0.1 . 1 . . . . 28 ALA C . 7428 1 51 . 1 1 13 13 ALA CA C 13 53.6 0.1 . 1 . . . . 28 ALA CA . 7428 1 52 . 1 1 13 13 ALA N N 15 123.4 0.02 . 1 . . . . 28 ALA N . 7428 1 53 . 1 1 14 14 ALA H H 1 7.83 0.02 . 1 . . . . 29 ALA H . 7428 1 54 . 1 1 14 14 ALA C C 13 179 0.1 . 1 . . . . 29 ALA C . 7428 1 55 . 1 1 14 14 ALA CA C 13 53.3 0.1 . 1 . . . . 29 ALA CA . 7428 1 56 . 1 1 14 14 ALA N N 15 119.2 0.02 . 1 . . . . 29 ALA N . 7428 1 57 . 1 1 15 15 GLY H H 1 7.76 0.02 . 1 . . . . 30 GLY H . 7428 1 58 . 1 1 15 15 GLY C C 13 174.7 0.1 . 1 . . . . 30 GLY C . 7428 1 59 . 1 1 15 15 GLY CA C 13 46.2 0.1 . 1 . . . . 30 GLY CA . 7428 1 60 . 1 1 15 15 GLY N N 15 107.8 0.02 . 1 . . . . 30 GLY N . 7428 1 61 . 1 1 16 16 ALA H H 1 8.08 0.02 . 1 . . . . 31 ALA H . 7428 1 62 . 1 1 16 16 ALA C C 13 179.2 0.1 . 1 . . . . 31 ALA C . 7428 1 63 . 1 1 16 16 ALA CA C 13 55 0.1 . 1 . . . . 31 ALA CA . 7428 1 64 . 1 1 16 16 ALA N N 15 123.6 0.02 . 1 . . . . 31 ALA N . 7428 1 65 . 1 1 17 17 ALA H H 1 8.07 0.02 . 1 . . . . 32 ALA H . 7428 1 66 . 1 1 17 17 ALA C C 13 178.6 0.1 . 1 . . . . 32 ALA C . 7428 1 67 . 1 1 17 17 ALA CA C 13 54.8 0.1 . 1 . . . . 32 ALA CA . 7428 1 68 . 1 1 17 17 ALA N N 15 118.1 0.02 . 1 . . . . 32 ALA N . 7428 1 69 . 1 1 18 18 THR H H 1 7.48 0.02 . 1 . . . . 33 THR H . 7428 1 70 . 1 1 18 18 THR C C 13 176.2 0.1 . 1 . . . . 33 THR C . 7428 1 71 . 1 1 18 18 THR CA C 13 67.1 0.1 . 1 . . . . 33 THR CA . 7428 1 72 . 1 1 18 18 THR N N 15 114.6 0.02 . 1 . . . . 33 THR N . 7428 1 73 . 1 1 19 19 VAL H H 1 7.73 0.02 . 1 . . . . 34 VAL H . 7428 1 74 . 1 1 19 19 VAL C C 13 177.1 0.1 . 1 . . . . 34 VAL C . 7428 1 75 . 1 1 19 19 VAL CA C 13 67 0.1 . 1 . . . . 34 VAL CA . 7428 1 76 . 1 1 19 19 VAL N N 15 121.1 0.02 . 1 . . . . 34 VAL N . 7428 1 77 . 1 1 20 20 LEU H H 1 7.75 0.02 . 1 . . . . 35 LEU H . 7428 1 78 . 1 1 20 20 LEU C C 13 176.9 0.1 . 1 . . . . 35 LEU C . 7428 1 79 . 1 1 20 20 LEU CA C 13 58 0.1 . 1 . . . . 35 LEU CA . 7428 1 80 . 1 1 20 20 LEU N N 15 119.3 0.02 . 1 . . . . 35 LEU N . 7428 1 81 . 1 1 21 21 LEU H H 1 7.85 0.02 . 1 . . . . 36 LEU H . 7428 1 82 . 1 1 21 21 LEU C C 13 178.2 0.1 . 1 . . . . 36 LEU C . 7428 1 83 . 1 1 21 21 LEU CA C 13 57.9 0.1 . 1 . . . . 36 LEU CA . 7428 1 84 . 1 1 21 21 LEU N N 15 117.6 0.02 . 1 . . . . 36 LEU N . 7428 1 85 . 1 1 22 22 VAL H H 1 8.26 0.02 . 1 . . . . 37 VAL H . 7428 1 86 . 1 1 22 22 VAL C C 13 177.9 0.1 . 1 . . . . 37 VAL C . 7428 1 87 . 1 1 22 22 VAL CA C 13 67.4 0.1 . 1 . . . . 37 VAL CA . 7428 1 88 . 1 1 22 22 VAL N N 15 117.5 0.02 . 1 . . . . 37 VAL N . 7428 1 89 . 1 1 23 23 ILE H H 1 8.26 0.02 . 1 . . . . 38 ILE H . 7428 1 90 . 1 1 23 23 ILE C C 13 177.8 0.1 . 1 . . . . 38 ILE C . 7428 1 91 . 1 1 23 23 ILE CA C 13 66 0.1 . 1 . . . . 38 ILE CA . 7428 1 92 . 1 1 23 23 ILE N N 15 120 0.02 . 1 . . . . 38 ILE N . 7428 1 93 . 1 1 24 24 VAL H H 1 8.21 0.02 . 1 . . . . 39 VAL H . 7428 1 94 . 1 1 24 24 VAL C C 13 178.7 0.1 . 1 . . . . 39 VAL C . 7428 1 95 . 1 1 24 24 VAL CA C 13 67 0.1 . 1 . . . . 39 VAL CA . 7428 1 96 . 1 1 24 24 VAL N N 15 119.8 0.02 . 1 . . . . 39 VAL N . 7428 1 97 . 1 1 25 25 LEU H H 1 8.46 0.02 . 1 . . . . 40 LEU H . 7428 1 98 . 1 1 25 25 LEU C C 13 180.8 0.1 . 1 . . . . 40 LEU C . 7428 1 99 . 1 1 25 25 LEU CA C 13 57.8 0.1 . 1 . . . . 40 LEU CA . 7428 1 100 . 1 1 25 25 LEU N N 15 118.3 0.02 . 1 . . . . 40 LEU N . 7428 1 101 . 1 1 26 26 LEU H H 1 8.77 0.02 . 1 . . . . 41 LEU H . 7428 1 102 . 1 1 26 26 LEU C C 13 180.5 0.1 . 1 . . . . 41 LEU C . 7428 1 103 . 1 1 26 26 LEU CA C 13 57.8 0.1 . 1 . . . . 41 LEU CA . 7428 1 104 . 1 1 26 26 LEU N N 15 120.8 0.02 . 1 . . . . 41 LEU N . 7428 1 105 . 1 1 27 27 ALA H H 1 8.82 0.02 . 1 . . . . 42 ALA H . 7428 1 106 . 1 1 27 27 ALA C C 13 180 0.1 . 1 . . . . 42 ALA C . 7428 1 107 . 1 1 27 27 ALA CA C 13 54.7 0.1 . 1 . . . . 42 ALA CA . 7428 1 108 . 1 1 27 27 ALA N N 15 121.5 0.02 . 1 . . . . 42 ALA N . 7428 1 109 . 1 1 28 28 GLY H H 1 8.9 0.02 . 1 . . . . 43 GLY H . 7428 1 110 . 1 1 28 28 GLY C C 13 175.4 0.1 . 1 . . . . 43 GLY C . 7428 1 111 . 1 1 28 28 GLY CA C 13 47 0.1 . 1 . . . . 43 GLY CA . 7428 1 112 . 1 1 28 28 GLY N N 15 106.6 0.02 . 1 . . . . 43 GLY N . 7428 1 113 . 1 1 29 29 SER H H 1 7.7 0.02 . 1 . . . . 44 SER H . 7428 1 114 . 1 1 29 29 SER C C 13 175.2 0.1 . 1 . . . . 44 SER C . 7428 1 115 . 1 1 29 29 SER CA C 13 62.8 0.1 . 1 . . . . 44 SER CA . 7428 1 116 . 1 1 29 29 SER N N 15 115.6 0.02 . 1 . . . . 44 SER N . 7428 1 117 . 1 1 30 30 TYR H H 1 7.47 0.02 . 1 . . . . 45 TYR H . 7428 1 118 . 1 1 30 30 TYR C C 13 177.1 0.1 . 1 . . . . 45 TYR C . 7428 1 119 . 1 1 30 30 TYR CA C 13 61.2 0.1 . 1 . . . . 45 TYR CA . 7428 1 120 . 1 1 30 30 TYR N N 15 121.4 0.02 . 1 . . . . 45 TYR N . 7428 1 121 . 1 1 31 31 LEU H H 1 7.95 0.02 . 1 . . . . 46 LEU H . 7428 1 122 . 1 1 31 31 LEU C C 13 178.2 0.1 . 1 . . . . 46 LEU C . 7428 1 123 . 1 1 31 31 LEU CA C 13 57.1 0.1 . 1 . . . . 46 LEU CA . 7428 1 124 . 1 1 31 31 LEU N N 15 116.4 0.02 . 1 . . . . 46 LEU N . 7428 1 125 . 1 1 32 32 ALA H H 1 8.09 0.02 . 1 . . . . 47 ALA H . 7428 1 126 . 1 1 32 32 ALA C C 13 178.8 0.1 . 1 . . . . 47 ALA C . 7428 1 127 . 1 1 32 32 ALA CA C 13 55.4 0.1 . 1 . . . . 47 ALA CA . 7428 1 128 . 1 1 32 32 ALA N N 15 120 0.02 . 1 . . . . 47 ALA N . 7428 1 129 . 1 1 33 33 VAL H H 1 7.22 0.02 . 1 . . . . 48 VAL H . 7428 1 130 . 1 1 33 33 VAL C C 13 178.6 0.1 . 1 . . . . 48 VAL C . 7428 1 131 . 1 1 33 33 VAL CA C 13 65 0.1 . 1 . . . . 48 VAL CA . 7428 1 132 . 1 1 33 33 VAL N N 15 116.3 0.02 . 1 . . . . 48 VAL N . 7428 1 133 . 1 1 34 34 LEU H H 1 7.41 0.02 . 1 . . . . 49 LEU H . 7428 1 134 . 1 1 34 34 LEU C C 13 179.4 0.1 . 1 . . . . 49 LEU C . 7428 1 135 . 1 1 34 34 LEU CA C 13 57.4 0.1 . 1 . . . . 49 LEU CA . 7428 1 136 . 1 1 34 34 LEU N N 15 119.5 0.02 . 1 . . . . 49 LEU N . 7428 1 137 . 1 1 35 35 ALA H H 1 7.76 0.02 . 1 . . . . 50 ALA H . 7428 1 138 . 1 1 35 35 ALA C C 13 179.3 0.1 . 1 . . . . 50 ALA C . 7428 1 139 . 1 1 35 35 ALA CA C 13 54.1 0.1 . 1 . . . . 50 ALA CA . 7428 1 140 . 1 1 35 35 ALA N N 15 118.1 0.02 . 1 . . . . 50 ALA N . 7428 1 141 . 1 1 36 36 GLU H H 1 7.82 0.02 . 1 . . . . 51 GLU H . 7428 1 142 . 1 1 36 36 GLU C C 13 177.9 0.1 . 1 . . . . 51 GLU C . 7428 1 143 . 1 1 36 36 GLU CA C 13 57.4 0.1 . 1 . . . . 51 GLU CA . 7428 1 144 . 1 1 36 36 GLU N N 15 114.9 0.02 . 1 . . . . 51 GLU N . 7428 1 145 . 1 1 37 37 ARG H H 1 7.93 0.02 . 1 . . . . 52 ARG H . 7428 1 146 . 1 1 37 37 ARG C C 13 177.9 0.1 . 1 . . . . 52 ARG C . 7428 1 147 . 1 1 37 37 ARG CA C 13 59.3 0.1 . 1 . . . . 52 ARG CA . 7428 1 148 . 1 1 37 37 ARG N N 15 116.9 0.02 . 1 . . . . 52 ARG N . 7428 1 149 . 1 1 38 38 GLY H H 1 8.3 0.02 . 1 . . . . 53 GLY H . 7428 1 150 . 1 1 38 38 GLY C C 13 174.6 0.1 . 1 . . . . 53 GLY C . 7428 1 151 . 1 1 38 38 GLY CA C 13 44.5 0.1 . 1 . . . . 53 GLY CA . 7428 1 152 . 1 1 38 38 GLY N N 15 110.6 0.02 . 1 . . . . 53 GLY N . 7428 1 153 . 1 1 39 39 ALA H H 1 7.67 0.02 . 1 . . . . 54 ALA H . 7428 1 154 . 1 1 39 39 ALA C C 13 176.4 0.1 . 1 . . . . 54 ALA C . 7428 1 155 . 1 1 39 39 ALA CA C 13 49.7 0.1 . 1 . . . . 54 ALA CA . 7428 1 156 . 1 1 39 39 ALA N N 15 126.4 0.02 . 1 . . . . 54 ALA N . 7428 1 157 . 1 1 40 40 PRO C C 13 178.3 0.1 . 1 . . . . 55 PRO C . 7428 1 158 . 1 1 40 40 PRO CA C 13 63.2 0.1 . 1 . . . . 55 PRO CA . 7428 1 159 . 1 1 41 41 GLY H H 1 8.5 0.02 . 1 . . . . 56 GLY H . 7428 1 160 . 1 1 41 41 GLY C C 13 174.4 0.1 . 1 . . . . 56 GLY C . 7428 1 161 . 1 1 41 41 GLY CA C 13 44.9 0.1 . 1 . . . . 56 GLY CA . 7428 1 162 . 1 1 41 41 GLY N N 15 111.7 0.02 . 1 . . . . 56 GLY N . 7428 1 163 . 1 1 42 42 ALA H H 1 7.29 0.02 . 1 . . . . 57 ALA H . 7428 1 164 . 1 1 42 42 ALA C C 13 177.5 0.1 . 1 . . . . 57 ALA C . 7428 1 165 . 1 1 42 42 ALA CA C 13 52.9 0.1 . 1 . . . . 57 ALA CA . 7428 1 166 . 1 1 42 42 ALA N N 15 121.9 0.02 . 1 . . . . 57 ALA N . 7428 1 167 . 1 1 43 43 GLN H H 1 8.63 0.02 . 1 . . . . 58 GLN H . 7428 1 168 . 1 1 43 43 GLN C C 13 176.9 0.1 . 1 . . . . 58 GLN C . 7428 1 169 . 1 1 43 43 GLN CA C 13 54.7 0.1 . 1 . . . . 58 GLN CA . 7428 1 170 . 1 1 43 43 GLN N N 15 116.4 0.02 . 1 . . . . 58 GLN N . 7428 1 171 . 1 1 44 44 LEU H H 1 7.85 0.02 . 1 . . . . 59 LEU H . 7428 1 172 . 1 1 44 44 LEU C C 13 174.6 0.1 . 1 . . . . 59 LEU C . 7428 1 173 . 1 1 44 44 LEU CA C 13 53 0.1 . 1 . . . . 59 LEU CA . 7428 1 174 . 1 1 44 44 LEU N N 15 125.1 0.02 . 1 . . . . 59 LEU N . 7428 1 175 . 1 1 45 45 ILE H H 1 6.88 0.02 . 1 . . . . 60 ILE H . 7428 1 176 . 1 1 45 45 ILE C C 13 175.9 0.1 . 1 . . . . 60 ILE C . 7428 1 177 . 1 1 45 45 ILE CA C 13 61.3 0.1 . 1 . . . . 60 ILE CA . 7428 1 178 . 1 1 45 45 ILE N N 15 107.1 0.02 . 1 . . . . 60 ILE N . 7428 1 179 . 1 1 46 46 THR H H 1 7.15 0.02 . 1 . . . . 61 THR H . 7428 1 180 . 1 1 46 46 THR C C 13 173.9 0.1 . 1 . . . . 61 THR C . 7428 1 181 . 1 1 46 46 THR CA C 13 58.2 0.1 . 1 . . . . 61 THR CA . 7428 1 182 . 1 1 46 46 THR N N 15 109.9 0.02 . 1 . . . . 61 THR N . 7428 1 183 . 1 1 47 47 TYR H H 1 8.98 0.02 . 1 . . . . 62 TYR H . 7428 1 184 . 1 1 47 47 TYR CA C 13 63.3 0.1 . 1 . . . . 62 TYR CA . 7428 1 185 . 1 1 47 47 TYR N N 15 122.4 0.02 . 1 . . . . 62 TYR N . 7428 1 186 . 1 1 48 48 PRO C C 13 177.9 0.1 . 1 . . . . 63 PRO C . 7428 1 187 . 1 1 48 48 PRO CA C 13 66.4 0.1 . 1 . . . . 63 PRO CA . 7428 1 188 . 1 1 49 49 ARG H H 1 6.74 0.02 . 1 . . . . 64 ARG H . 7428 1 189 . 1 1 49 49 ARG C C 13 178.5 0.1 . 1 . . . . 64 ARG C . 7428 1 190 . 1 1 49 49 ARG CA C 13 58.9 0.1 . 1 . . . . 64 ARG CA . 7428 1 191 . 1 1 49 49 ARG N N 15 113.8 0.02 . 1 . . . . 64 ARG N . 7428 1 192 . 1 1 50 50 ALA H H 1 7.79 0.02 . 1 . . . . 65 ALA H . 7428 1 193 . 1 1 50 50 ALA C C 13 178.9 0.1 . 1 . . . . 65 ALA C . 7428 1 194 . 1 1 50 50 ALA CA C 13 54.8 0.1 . 1 . . . . 65 ALA CA . 7428 1 195 . 1 1 50 50 ALA N N 15 120.6 0.02 . 1 . . . . 65 ALA N . 7428 1 196 . 1 1 51 51 LEU H H 1 8.58 0.02 . 1 . . . . 66 LEU H . 7428 1 197 . 1 1 51 51 LEU C C 13 180 0.1 . 1 . . . . 66 LEU C . 7428 1 198 . 1 1 51 51 LEU CA C 13 57.2 0.1 . 1 . . . . 66 LEU CA . 7428 1 199 . 1 1 51 51 LEU N N 15 122.8 0.02 . 1 . . . . 66 LEU N . 7428 1 200 . 1 1 52 52 TRP H H 1 7.86 0.02 . 1 . . . . 67 TRP H . 7428 1 201 . 1 1 52 52 TRP C C 13 176.8 0.1 . 1 . . . . 67 TRP C . 7428 1 202 . 1 1 52 52 TRP CA C 13 59.5 0.1 . 1 . . . . 67 TRP CA . 7428 1 203 . 1 1 52 52 TRP N N 15 121.4 0.02 . 1 . . . . 67 TRP N . 7428 1 204 . 1 1 53 53 TRP H H 1 8.33 0.02 . 1 . . . . 68 TRP H . 7428 1 205 . 1 1 53 53 TRP C C 13 180.2 0.1 . 1 . . . . 68 TRP C . 7428 1 206 . 1 1 53 53 TRP CA C 13 59.8 0.1 . 1 . . . . 68 TRP CA . 7428 1 207 . 1 1 53 53 TRP N N 15 120.3 0.02 . 1 . . . . 68 TRP N . 7428 1 208 . 1 1 54 54 SER H H 1 9.41 0.02 . 1 . . . . 69 SER H . 7428 1 209 . 1 1 54 54 SER C C 13 176.2 0.1 . 1 . . . . 69 SER C . 7428 1 210 . 1 1 54 54 SER CA C 13 63.2 0.1 . 1 . . . . 69 SER CA . 7428 1 211 . 1 1 54 54 SER N N 15 124.5 0.02 . 1 . . . . 69 SER N . 7428 1 212 . 1 1 55 55 VAL H H 1 7.66 0.02 . 1 . . . . 70 VAL H . 7428 1 213 . 1 1 55 55 VAL C C 13 178.1 0.1 . 1 . . . . 70 VAL C . 7428 1 214 . 1 1 55 55 VAL CA C 13 66 0.1 . 1 . . . . 70 VAL CA . 7428 1 215 . 1 1 55 55 VAL N N 15 124.8 0.02 . 1 . . . . 70 VAL N . 7428 1 216 . 1 1 56 56 GLU H H 1 7.98 0.02 . 1 . . . . 71 GLU H . 7428 1 217 . 1 1 56 56 GLU C C 13 180.2 0.1 . 1 . . . . 71 GLU C . 7428 1 218 . 1 1 56 56 GLU CA C 13 58.5 0.1 . 1 . . . . 71 GLU CA . 7428 1 219 . 1 1 56 56 GLU N N 15 120.1 0.02 . 1 . . . . 71 GLU N . 7428 1 220 . 1 1 57 57 THR H H 1 7.89 0.02 . 1 . . . . 72 THR H . 7428 1 221 . 1 1 57 57 THR C C 13 173.6 0.1 . 1 . . . . 72 THR C . 7428 1 222 . 1 1 57 57 THR CA C 13 67.2 0.1 . 1 . . . . 72 THR CA . 7428 1 223 . 1 1 57 57 THR N N 15 119.6 0.02 . 1 . . . . 72 THR N . 7428 1 224 . 1 1 58 58 ALA H H 1 7.57 0.02 . 1 . . . . 73 ALA H . 7428 1 225 . 1 1 58 58 ALA C C 13 177.1 0.1 . 1 . . . . 73 ALA C . 7428 1 226 . 1 1 58 58 ALA CA C 13 54.8 0.1 . 1 . . . . 73 ALA CA . 7428 1 227 . 1 1 58 58 ALA N N 15 120.8 0.02 . 1 . . . . 73 ALA N . 7428 1 228 . 1 1 59 59 THR H H 1 6.98 0.02 . 1 . . . . 74 THR H . 7428 1 229 . 1 1 59 59 THR C C 13 178 0.1 . 1 . . . . 74 THR C . 7428 1 230 . 1 1 59 59 THR CA C 13 61.5 0.1 . 1 . . . . 74 THR CA . 7428 1 231 . 1 1 59 59 THR N N 15 100.1 0.02 . 1 . . . . 74 THR N . 7428 1 232 . 1 1 60 60 THR H H 1 7.3 0.02 . 1 . . . . 75 THR H . 7428 1 233 . 1 1 60 60 THR C C 13 173.6 0.1 . 1 . . . . 75 THR C . 7428 1 234 . 1 1 60 60 THR CA C 13 62.2 0.1 . 1 . . . . 75 THR CA . 7428 1 235 . 1 1 60 60 THR N N 15 116 0.02 . 1 . . . . 75 THR N . 7428 1 236 . 1 1 61 61 VAL H H 1 7.09 0.02 . 1 . . . . 76 VAL H . 7428 1 237 . 1 1 61 61 VAL C C 13 176.4 0.1 . 1 . . . . 76 VAL C . 7428 1 238 . 1 1 61 61 VAL CA C 13 65.2 0.1 . 1 . . . . 76 VAL CA . 7428 1 239 . 1 1 61 61 VAL N N 15 119.7 0.02 . 1 . . . . 76 VAL N . 7428 1 240 . 1 1 62 62 GLY H H 1 8.16 0.02 . 1 . . . . 77 GLY H . 7428 1 241 . 1 1 62 62 GLY C C 13 175.7 0.1 . 1 . . . . 77 GLY C . 7428 1 242 . 1 1 62 62 GLY CA C 13 47.8 0.1 . 1 . . . . 77 GLY CA . 7428 1 243 . 1 1 62 62 GLY N N 15 107.1 0.02 . 1 . . . . 77 GLY N . 7428 1 244 . 1 1 63 63 TYR H H 1 6.09 0.02 . 1 . . . . 78 TYR H . 7428 1 245 . 1 1 63 63 TYR C C 13 178 0.1 . 1 . . . . 78 TYR C . 7428 1 246 . 1 1 63 63 TYR CA C 13 56.9 0.1 . 1 . . . . 78 TYR CA . 7428 1 247 . 1 1 63 63 TYR N N 15 117.4 0.02 . 1 . . . . 78 TYR N . 7428 1 248 . 1 1 64 64 GLY H H 1 8.96 0.02 . 1 . . . . 79 GLY H . 7428 1 249 . 1 1 64 64 GLY C C 13 174.4 0.1 . 1 . . . . 79 GLY C . 7428 1 250 . 1 1 64 64 GLY CA C 13 47.1 0.1 . 1 . . . . 79 GLY CA . 7428 1 251 . 1 1 64 64 GLY N N 15 102.2 0.02 . 1 . . . . 79 GLY N . 7428 1 252 . 1 1 65 65 ASP H H 1 9.61 0.02 . 1 . . . . 80 ASP H . 7428 1 253 . 1 1 65 65 ASP CA C 13 54.4 0.1 . 1 . . . . 80 ASP CA . 7428 1 254 . 1 1 65 65 ASP N N 15 115.6 0.02 . 1 . . . . 80 ASP N . 7428 1 255 . 1 1 68 68 PRO C C 13 176.1 0.1 . 1 . . . . 83 PRO C . 7428 1 256 . 1 1 68 68 PRO CA C 13 61.1 0.1 . 1 . . . . 83 PRO CA . 7428 1 257 . 1 1 69 69 VAL H H 1 10.75 0.02 . 1 . . . . 84 VAL H . 7428 1 258 . 1 1 69 69 VAL C C 13 176.7 0.1 . 1 . . . . 84 VAL C . 7428 1 259 . 1 1 69 69 VAL CA C 13 61 0.1 . 1 . . . . 84 VAL CA . 7428 1 260 . 1 1 69 69 VAL N N 15 116.4 0.02 . 1 . . . . 84 VAL N . 7428 1 261 . 1 1 70 70 THR H H 1 8.7 0.02 . 1 . . . . 85 THR H . 7428 1 262 . 1 1 70 70 THR C C 13 174.7 0.1 . 1 . . . . 85 THR C . 7428 1 263 . 1 1 70 70 THR CA C 13 60 0.1 . 1 . . . . 85 THR CA . 7428 1 264 . 1 1 70 70 THR N N 15 116.8 0.02 . 1 . . . . 85 THR N . 7428 1 265 . 1 1 71 71 LEU H H 1 8.05 0.02 . 1 . . . . 86 LEU H . 7428 1 266 . 1 1 71 71 LEU C C 13 178.7 0.1 . 1 . . . . 86 LEU C . 7428 1 267 . 1 1 71 71 LEU CA C 13 58.4 0.1 . 1 . . . . 86 LEU CA . 7428 1 268 . 1 1 71 71 LEU N N 15 123.6 0.02 . 1 . . . . 86 LEU N . 7428 1 269 . 1 1 72 72 TRP H H 1 7.17 0.02 . 1 . . . . 87 TRP H . 7428 1 270 . 1 1 72 72 TRP C C 13 178.7 0.1 . 1 . . . . 87 TRP C . 7428 1 271 . 1 1 72 72 TRP CA C 13 59 0.1 . 1 . . . . 87 TRP CA . 7428 1 272 . 1 1 72 72 TRP N N 15 116 0.02 . 1 . . . . 87 TRP N . 7428 1 273 . 1 1 73 73 GLY H H 1 8.42 0.02 . 1 . . . . 88 GLY H . 7428 1 274 . 1 1 73 73 GLY C C 13 176.6 0.1 . 1 . . . . 88 GLY C . 7428 1 275 . 1 1 73 73 GLY CA C 13 46 0.1 . 1 . . . . 88 GLY CA . 7428 1 276 . 1 1 73 73 GLY N N 15 107.6 0.02 . 1 . . . . 88 GLY N . 7428 1 277 . 1 1 74 74 ARG H H 1 7.77 0.02 . 1 . . . . 89 ARG H . 7428 1 278 . 1 1 74 74 ARG C C 13 178 0.1 . 1 . . . . 89 ARG C . 7428 1 279 . 1 1 74 74 ARG CA C 13 59.6 0.1 . 1 . . . . 89 ARG CA . 7428 1 280 . 1 1 74 74 ARG N N 15 123.3 0.02 . 1 . . . . 89 ARG N . 7428 1 281 . 1 1 75 75 LEU H H 1 7.87 0.02 . 1 . . . . 90 LEU H . 7428 1 282 . 1 1 75 75 LEU C C 13 179.8 0.1 . 1 . . . . 90 LEU C . 7428 1 283 . 1 1 75 75 LEU CA C 13 58.2 0.1 . 1 . . . . 90 LEU CA . 7428 1 284 . 1 1 75 75 LEU N N 15 120 0.02 . 1 . . . . 90 LEU N . 7428 1 285 . 1 1 76 76 VAL H H 1 8.23 0.02 . 1 . . . . 91 VAL H . 7428 1 286 . 1 1 76 76 VAL C C 13 178.8 0.1 . 1 . . . . 91 VAL C . 7428 1 287 . 1 1 76 76 VAL CA C 13 66.5 0.1 . 1 . . . . 91 VAL CA . 7428 1 288 . 1 1 76 76 VAL N N 15 119.1 0.02 . 1 . . . . 91 VAL N . 7428 1 289 . 1 1 77 77 ALA H H 1 8.44 0.02 . 1 . . . . 92 ALA H . 7428 1 290 . 1 1 77 77 ALA C C 13 179.2 0.1 . 1 . . . . 92 ALA C . 7428 1 291 . 1 1 77 77 ALA CA C 13 55.7 0.1 . 1 . . . . 92 ALA CA . 7428 1 292 . 1 1 77 77 ALA N N 15 121 0.02 . 1 . . . . 92 ALA N . 7428 1 293 . 1 1 78 78 VAL H H 1 8.21 0.02 . 1 . . . . 93 VAL H . 7428 1 294 . 1 1 78 78 VAL C C 13 177.8 0.1 . 1 . . . . 93 VAL C . 7428 1 295 . 1 1 78 78 VAL CA C 13 67.5 0.1 . 1 . . . . 93 VAL CA . 7428 1 296 . 1 1 78 78 VAL N N 15 119 0.02 . 1 . . . . 93 VAL N . 7428 1 297 . 1 1 79 79 VAL H H 1 7.55 0.02 . 1 . . . . 94 VAL H . 7428 1 298 . 1 1 79 79 VAL C C 13 178 0.1 . 1 . . . . 94 VAL C . 7428 1 299 . 1 1 79 79 VAL CA C 13 67 0.1 . 1 . . . . 94 VAL CA . 7428 1 300 . 1 1 79 79 VAL N N 15 119.9 0.02 . 1 . . . . 94 VAL N . 7428 1 301 . 1 1 80 80 VAL H H 1 8.43 0.02 . 1 . . . . 95 VAL H . 7428 1 302 . 1 1 80 80 VAL C C 13 179.4 0.1 . 1 . . . . 95 VAL C . 7428 1 303 . 1 1 80 80 VAL CA C 13 67.2 0.1 . 1 . . . . 95 VAL CA . 7428 1 304 . 1 1 80 80 VAL N N 15 120.1 0.02 . 1 . . . . 95 VAL N . 7428 1 305 . 1 1 81 81 MET H H 1 9.16 0.02 . 1 . . . . 96 MET H . 7428 1 306 . 1 1 81 81 MET C C 13 177.6 0.1 . 1 . . . . 96 MET C . 7428 1 307 . 1 1 81 81 MET CA C 13 59.7 0.1 . 1 . . . . 96 MET CA . 7428 1 308 . 1 1 81 81 MET N N 15 120.6 0.02 . 1 . . . . 96 MET N . 7428 1 309 . 1 1 82 82 VAL H H 1 8.33 0.02 . 1 . . . . 97 VAL H . 7428 1 310 . 1 1 82 82 VAL C C 13 178.2 0.1 . 1 . . . . 97 VAL C . 7428 1 311 . 1 1 82 82 VAL CA C 13 67.5 0.1 . 1 . . . . 97 VAL CA . 7428 1 312 . 1 1 82 82 VAL N N 15 117 0.02 . 1 . . . . 97 VAL N . 7428 1 313 . 1 1 83 83 ALA H H 1 8.61 0.02 . 1 . . . . 98 ALA H . 7428 1 314 . 1 1 83 83 ALA C C 13 180.1 0.1 . 1 . . . . 98 ALA C . 7428 1 315 . 1 1 83 83 ALA CA C 13 54.2 0.1 . 1 . . . . 98 ALA CA . 7428 1 316 . 1 1 83 83 ALA N N 15 119.8 0.02 . 1 . . . . 98 ALA N . 7428 1 317 . 1 1 84 84 GLY H H 1 8.85 0.02 . 1 . . . . 99 GLY H . 7428 1 318 . 1 1 84 84 GLY C C 13 174.6 0.1 . 1 . . . . 99 GLY C . 7428 1 319 . 1 1 84 84 GLY CA C 13 46.7 0.1 . 1 . . . . 99 GLY CA . 7428 1 320 . 1 1 84 84 GLY N N 15 112.1 0.02 . 1 . . . . 99 GLY N . 7428 1 321 . 1 1 85 85 ILE H H 1 8.5 0.02 . 1 . . . . 100 ILE H . 7428 1 322 . 1 1 85 85 ILE C C 13 181 0.1 . 1 . . . . 100 ILE C . 7428 1 323 . 1 1 85 85 ILE CA C 13 65.6 0.1 . 1 . . . . 100 ILE CA . 7428 1 324 . 1 1 85 85 ILE N N 15 124 0.02 . 1 . . . . 100 ILE N . 7428 1 325 . 1 1 86 86 THR H H 1 6.85 0.02 . 1 . . . . 101 THR H . 7428 1 326 . 1 1 86 86 THR C C 13 177.6 0.1 . 1 . . . . 101 THR C . 7428 1 327 . 1 1 86 86 THR CA C 13 67.1 0.1 . 1 . . . . 101 THR CA . 7428 1 328 . 1 1 86 86 THR N N 15 114.9 0.02 . 1 . . . . 101 THR N . 7428 1 329 . 1 1 87 87 SER H H 1 7.69 0.02 . 1 . . . . 102 SER H . 7428 1 330 . 1 1 87 87 SER C C 13 176.5 0.1 . 1 . . . . 102 SER C . 7428 1 331 . 1 1 87 87 SER CA C 13 62.8 0.1 . 1 . . . . 102 SER CA . 7428 1 332 . 1 1 87 87 SER N N 15 116.3 0.02 . 1 . . . . 102 SER N . 7428 1 333 . 1 1 88 88 PHE H H 1 9.09 0.02 . 1 . . . . 103 PHE H . 7428 1 334 . 1 1 88 88 PHE C C 13 177.8 0.1 . 1 . . . . 103 PHE C . 7428 1 335 . 1 1 88 88 PHE CA C 13 62 0.1 . 1 . . . . 103 PHE CA . 7428 1 336 . 1 1 88 88 PHE N N 15 124.4 0.02 . 1 . . . . 103 PHE N . 7428 1 337 . 1 1 89 89 GLY H H 1 8.14 0.02 . 1 . . . . 104 GLY H . 7428 1 338 . 1 1 89 89 GLY C C 13 177.1 0.1 . 1 . . . . 104 GLY C . 7428 1 339 . 1 1 89 89 GLY CA C 13 46.6 0.1 . 1 . . . . 104 GLY CA . 7428 1 340 . 1 1 89 89 GLY N N 15 106.9 0.02 . 1 . . . . 104 GLY N . 7428 1 341 . 1 1 90 90 LEU H H 1 7.31 0.02 . 1 . . . . 105 LEU H . 7428 1 342 . 1 1 90 90 LEU C C 13 179.9 0.1 . 1 . . . . 105 LEU C . 7428 1 343 . 1 1 90 90 LEU CA C 13 57.4 0.1 . 1 . . . . 105 LEU CA . 7428 1 344 . 1 1 90 90 LEU N N 15 122.5 0.02 . 1 . . . . 105 LEU N . 7428 1 345 . 1 1 91 91 VAL H H 1 7.65 0.02 . 1 . . . . 106 VAL H . 7428 1 346 . 1 1 91 91 VAL C C 13 178.2 0.1 . 1 . . . . 106 VAL C . 7428 1 347 . 1 1 91 91 VAL CA C 13 66.7 0.1 . 1 . . . . 106 VAL CA . 7428 1 348 . 1 1 91 91 VAL N N 15 121.8 0.02 . 1 . . . . 106 VAL N . 7428 1 349 . 1 1 92 92 THR H H 1 8.11 0.02 . 1 . . . . 107 THR H . 7428 1 350 . 1 1 92 92 THR C C 13 177.8 0.1 . 1 . . . . 107 THR C . 7428 1 351 . 1 1 92 92 THR CA C 13 65 0.1 . 1 . . . . 107 THR CA . 7428 1 352 . 1 1 92 92 THR N N 15 110.8 0.02 . 1 . . . . 107 THR N . 7428 1 353 . 1 1 93 93 ALA H H 1 7.6 0.02 . 1 . . . . 108 ALA H . 7428 1 354 . 1 1 93 93 ALA C C 13 181 0.1 . 1 . . . . 108 ALA C . 7428 1 355 . 1 1 93 93 ALA CA C 13 54.8 0.1 . 1 . . . . 108 ALA CA . 7428 1 356 . 1 1 93 93 ALA N N 15 124.7 0.02 . 1 . . . . 108 ALA N . 7428 1 357 . 1 1 94 94 ALA H H 1 7.68 0.02 . 1 . . . . 109 ALA H . 7428 1 358 . 1 1 94 94 ALA C C 13 181.2 0.1 . 1 . . . . 109 ALA C . 7428 1 359 . 1 1 94 94 ALA CA C 13 54.7 0.1 . 1 . . . . 109 ALA CA . 7428 1 360 . 1 1 94 94 ALA N N 15 122.7 0.02 . 1 . . . . 109 ALA N . 7428 1 361 . 1 1 95 95 LEU H H 1 8.27 0.02 . 1 . . . . 110 LEU H . 7428 1 362 . 1 1 95 95 LEU C C 13 178.7 0.1 . 1 . . . . 110 LEU C . 7428 1 363 . 1 1 95 95 LEU CA C 13 57.7 0.1 . 1 . . . . 110 LEU CA . 7428 1 364 . 1 1 95 95 LEU N N 15 120.7 0.02 . 1 . . . . 110 LEU N . 7428 1 365 . 1 1 96 96 ALA H H 1 8.53 0.02 . 1 . . . . 111 ALA H . 7428 1 366 . 1 1 96 96 ALA C C 13 179.8 0.1 . 1 . . . . 111 ALA C . 7428 1 367 . 1 1 96 96 ALA CA C 13 55.6 0.1 . 1 . . . . 111 ALA CA . 7428 1 368 . 1 1 96 96 ALA N N 15 122.1 0.02 . 1 . . . . 111 ALA N . 7428 1 369 . 1 1 97 97 THR H H 1 7.92 0.02 . 1 . . . . 112 THR H . 7428 1 370 . 1 1 97 97 THR C C 13 177.3 0.1 . 1 . . . . 112 THR C . 7428 1 371 . 1 1 97 97 THR CA C 13 66.3 0.1 . 1 . . . . 112 THR CA . 7428 1 372 . 1 1 97 97 THR N N 15 114.1 0.02 . 1 . . . . 112 THR N . 7428 1 373 . 1 1 98 98 TRP H H 1 8.15 0.02 . 1 . . . . 113 TRP H . 7428 1 374 . 1 1 98 98 TRP C C 13 178.5 0.1 . 1 . . . . 113 TRP C . 7428 1 375 . 1 1 98 98 TRP CA C 13 61.3 0.1 . 1 . . . . 113 TRP CA . 7428 1 376 . 1 1 98 98 TRP N N 15 125.1 0.02 . 1 . . . . 113 TRP N . 7428 1 377 . 1 1 99 99 PHE H H 1 8.63 0.02 . 1 . . . . 114 PHE H . 7428 1 378 . 1 1 99 99 PHE C C 13 178.2 0.1 . 1 . . . . 114 PHE C . 7428 1 379 . 1 1 99 99 PHE CA C 13 61.3 0.1 . 1 . . . . 114 PHE CA . 7428 1 380 . 1 1 99 99 PHE N N 15 119.7 0.02 . 1 . . . . 114 PHE N . 7428 1 381 . 1 1 100 100 VAL H H 1 8.19 0.02 . 1 . . . . 115 VAL H . 7428 1 382 . 1 1 100 100 VAL C C 13 178.8 0.1 . 1 . . . . 115 VAL C . 7428 1 383 . 1 1 100 100 VAL CA C 13 65.5 0.1 . 1 . . . . 115 VAL CA . 7428 1 384 . 1 1 100 100 VAL N N 15 117.7 0.02 . 1 . . . . 115 VAL N . 7428 1 385 . 1 1 101 101 GLY H H 1 7.63 0.02 . 1 . . . . 116 GLY H . 7428 1 386 . 1 1 101 101 GLY C C 13 176 0.1 . 1 . . . . 116 GLY C . 7428 1 387 . 1 1 101 101 GLY CA C 13 46.1 0.1 . 1 . . . . 116 GLY CA . 7428 1 388 . 1 1 101 101 GLY N N 15 107.5 0.02 . 1 . . . . 116 GLY N . 7428 1 389 . 1 1 102 102 ARG H H 1 7.24 0.02 . 1 . . . . 117 ARG H . 7428 1 390 . 1 1 102 102 ARG C C 13 177.2 0.1 . 1 . . . . 117 ARG C . 7428 1 391 . 1 1 102 102 ARG CA C 13 56.5 0.1 . 1 . . . . 117 ARG CA . 7428 1 392 . 1 1 102 102 ARG N N 15 121.2 0.02 . 1 . . . . 117 ARG N . 7428 1 393 . 1 1 103 103 GLU H H 1 7.87 0.02 . 1 . . . . 118 GLU H . 7428 1 394 . 1 1 103 103 GLU C C 13 177 0.1 . 1 . . . . 118 GLU C . 7428 1 395 . 1 1 103 103 GLU CA C 13 57 0.1 . 1 . . . . 118 GLU CA . 7428 1 396 . 1 1 103 103 GLU N N 15 120.9 0.02 . 1 . . . . 118 GLU N . 7428 1 397 . 1 1 104 104 GLN C C 13 177.6 0.1 . 1 . . . . 119 GLN C . 7428 1 398 . 1 1 104 104 GLN CA C 13 57.1 0.1 . 1 . . . . 119 GLN CA . 7428 1 399 . 1 1 105 105 GLU H H 1 7.9 0.02 . 1 . . . . 120 GLU H . 7428 1 400 . 1 1 105 105 GLU C C 13 177.6 0.1 . 1 . . . . 120 GLU C . 7428 1 401 . 1 1 105 105 GLU CA C 13 56.9 0.1 . 1 . . . . 120 GLU CA . 7428 1 402 . 1 1 105 105 GLU N N 15 119 0.02 . 1 . . . . 120 GLU N . 7428 1 403 . 1 1 106 106 ARG H H 1 7.9 0.1 . 1 . . . . 121 ARG H . 7428 1 404 . 1 1 106 106 ARG C C 13 177 0.1 . 1 . . . . 121 ARG C . 7428 1 405 . 1 1 106 106 ARG CA C 13 56.8 0.1 . 1 . . . . 121 ARG CA . 7428 1 406 . 1 1 106 106 ARG N N 15 119.2 0.1 . 1 . . . . 121 ARG N . 7428 1 407 . 1 1 107 107 ARG H H 1 7.82 0.1 . 1 . . . . 122 ARG H . 7428 1 408 . 1 1 107 107 ARG C C 13 177.3 0.1 . 1 . . . . 122 ARG C . 7428 1 409 . 1 1 107 107 ARG CA C 13 56.8 0.1 . 1 . . . . 122 ARG CA . 7428 1 410 . 1 1 107 107 ARG N N 15 120.4 0.1 . 1 . . . . 122 ARG N . 7428 1 411 . 1 1 108 108 GLY H H 1 7.97 0.1 . 1 . . . . 123 GLY H . 7428 1 412 . 1 1 108 108 GLY C C 13 174.5 0.1 . 1 . . . . 123 GLY C . 7428 1 413 . 1 1 108 108 GLY CA C 13 45.4 0.1 . 1 . . . . 123 GLY CA . 7428 1 414 . 1 1 108 108 GLY N N 15 108.9 0.1 . 1 . . . . 123 GLY N . 7428 1 415 . 1 1 109 109 HIS H H 1 7.86 0.1 . 1 . . . . 124 HIS H . 7428 1 416 . 1 1 109 109 HIS C C 13 174.7 0.1 . 1 . . . . 124 HIS C . 7428 1 417 . 1 1 109 109 HIS CA C 13 55.7 0.1 . 1 . . . . 124 HIS CA . 7428 1 418 . 1 1 109 109 HIS N N 15 117.3 0.1 . 1 . . . . 124 HIS N . 7428 1 419 . 1 1 110 110 PHE H H 1 7.96 0.1 . 1 . . . . 125 PHE H . 7428 1 420 . 1 1 110 110 PHE C C 13 176 0.1 . 1 . . . . 125 PHE C . 7428 1 421 . 1 1 110 110 PHE CA C 13 58.7 0.1 . 1 . . . . 125 PHE CA . 7428 1 422 . 1 1 110 110 PHE N N 15 120.2 0.1 . 1 . . . . 125 PHE N . 7428 1 423 . 1 1 111 111 VAL H H 1 7.54 0.1 . 1 . . . . 126 VAL H . 7428 1 424 . 1 1 111 111 VAL C C 13 176.2 0.1 . 1 . . . . 126 VAL C . 7428 1 425 . 1 1 111 111 VAL CA C 13 62.5 0.1 . 1 . . . . 126 VAL CA . 7428 1 426 . 1 1 111 111 VAL N N 15 119.7 0.1 . 1 . . . . 126 VAL N . 7428 1 427 . 1 1 112 112 ARG H H 1 7.77 0.1 . 1 . . . . 127 ARG H . 7428 1 428 . 1 1 112 112 ARG C C 13 176.9 0.1 . 1 . . . . 127 ARG C . 7428 1 429 . 1 1 112 112 ARG CA C 13 56.5 0.1 . 1 . . . . 127 ARG CA . 7428 1 430 . 1 1 112 112 ARG N N 15 121.8 0.1 . 1 . . . . 127 ARG N . 7428 1 431 . 1 1 113 113 HIS H H 1 8.05 0.1 . 1 . . . . 128 HIS H . 7428 1 432 . 1 1 113 113 HIS C C 13 175 0.1 . 1 . . . . 128 HIS C . 7428 1 433 . 1 1 113 113 HIS CA C 13 55.8 0.1 . 1 . . . . 128 HIS CA . 7428 1 434 . 1 1 113 113 HIS N N 15 118.2 0.1 . 1 . . . . 128 HIS N . 7428 1 435 . 1 1 114 114 SER H H 1 7.93 0.1 . 1 . . . . 129 SER H . 7428 1 436 . 1 1 114 114 SER C C 13 175.1 0.1 . 1 . . . . 129 SER C . 7428 1 437 . 1 1 114 114 SER CA C 13 58.7 0.1 . 1 . . . . 129 SER CA . 7428 1 438 . 1 1 114 114 SER N N 15 116 0.1 . 1 . . . . 129 SER N . 7428 1 439 . 1 1 115 115 GLU H H 1 8.21 0.1 . 1 . . . . 130 GLU H . 7428 1 440 . 1 1 115 115 GLU C C 13 177.1 0.1 . 1 . . . . 130 GLU C . 7428 1 441 . 1 1 115 115 GLU CA C 13 57.2 0.1 . 1 . . . . 130 GLU CA . 7428 1 442 . 1 1 115 115 GLU N N 15 122.9 0.1 . 1 . . . . 130 GLU N . 7428 1 443 . 1 1 116 116 LYS H H 1 7.86 0.1 . 1 . . . . 131 LYS H . 7428 1 444 . 1 1 116 116 LYS C C 13 177.4 0.1 . 1 . . . . 131 LYS C . 7428 1 445 . 1 1 116 116 LYS CA C 13 56.9 0.1 . 1 . . . . 131 LYS CA . 7428 1 446 . 1 1 116 116 LYS N N 15 120.8 0.1 . 1 . . . . 131 LYS N . 7428 1 447 . 1 1 117 117 ALA H H 1 7.86 0.1 . 1 . . . . 132 ALA H . 7428 1 448 . 1 1 117 117 ALA C C 13 178.6 0.1 . 1 . . . . 132 ALA C . 7428 1 449 . 1 1 117 117 ALA CA C 13 53.3 0.1 . 1 . . . . 132 ALA CA . 7428 1 450 . 1 1 117 117 ALA N N 15 123.5 0.1 . 1 . . . . 132 ALA N . 7428 1 451 . 1 1 118 118 ALA H H 1 7.86 0.1 . 1 . . . . 133 ALA H . 7428 1 452 . 1 1 118 118 ALA C C 13 178.6 0.1 . 1 . . . . 133 ALA C . 7428 1 453 . 1 1 118 118 ALA CA C 13 53.5 0.1 . 1 . . . . 133 ALA CA . 7428 1 454 . 1 1 118 118 ALA N N 15 121.7 0.1 . 1 . . . . 133 ALA N . 7428 1 455 . 1 1 119 119 GLU H H 1 7.94 0.1 . 1 . . . . 134 GLU H . 7428 1 456 . 1 1 119 119 GLU C C 13 178.1 0.1 . 1 . . . . 134 GLU C . 7428 1 457 . 1 1 119 119 GLU CA C 13 57.7 0.1 . 1 . . . . 134 GLU CA . 7428 1 458 . 1 1 119 119 GLU N N 15 118.2 0.1 . 1 . . . . 134 GLU N . 7428 1 459 . 1 1 120 120 GLU H H 1 8 0.1 . 1 . . . . 135 GLU H . 7428 1 460 . 1 1 120 120 GLU C C 13 177.4 0.1 . 1 . . . . 135 GLU C . 7428 1 461 . 1 1 120 120 GLU CA C 13 57.3 0.1 . 1 . . . . 135 GLU CA . 7428 1 462 . 1 1 120 120 GLU N N 15 120.2 0.1 . 1 . . . . 135 GLU N . 7428 1 463 . 1 1 121 121 ALA H H 1 7.99 0.1 . 1 . . . . 136 ALA H . 7428 1 464 . 1 1 121 121 ALA C C 13 179 0.1 . 1 . . . . 136 ALA C . 7428 1 465 . 1 1 121 121 ALA CA C 13 53.7 0.1 . 1 . . . . 136 ALA CA . 7428 1 466 . 1 1 121 121 ALA N N 15 123.1 0.1 . 1 . . . . 136 ALA N . 7428 1 467 . 1 1 122 122 TYR H H 1 8.07 0.1 . 1 . . . . 137 TYR H . 7428 1 468 . 1 1 122 122 TYR C C 13 177.2 0.1 . 1 . . . . 137 TYR C . 7428 1 469 . 1 1 122 122 TYR CA C 13 59.4 0.1 . 1 . . . . 137 TYR CA . 7428 1 470 . 1 1 122 122 TYR N N 15 119.5 0.1 . 1 . . . . 137 TYR N . 7428 1 471 . 1 1 123 123 THR H H 1 7.94 0.1 . 1 . . . . 138 THR H . 7428 1 472 . 1 1 123 123 THR C C 13 175.7 0.1 . 1 . . . . 138 THR C . 7428 1 473 . 1 1 123 123 THR CA C 13 63.6 0.1 . 1 . . . . 138 THR CA . 7428 1 474 . 1 1 123 123 THR N N 15 115.7 0.1 . 1 . . . . 138 THR N . 7428 1 475 . 1 1 124 124 ARG H H 1 7.98 0.1 . 1 . . . . 139 ARG H . 7428 1 476 . 1 1 124 124 ARG C C 13 177.9 0.1 . 1 . . . . 139 ARG C . 7428 1 477 . 1 1 124 124 ARG CA C 13 57.6 0.1 . 1 . . . . 139 ARG CA . 7428 1 478 . 1 1 124 124 ARG N N 15 122 0.1 . 1 . . . . 139 ARG N . 7428 1 479 . 1 1 125 125 THR H H 1 7.84 0.1 . 1 . . . . 140 THR H . 7428 1 480 . 1 1 125 125 THR C C 13 175.8 0.1 . 1 . . . . 140 THR C . 7428 1 481 . 1 1 125 125 THR CA C 13 64.3 0.1 . 1 . . . . 140 THR CA . 7428 1 482 . 1 1 125 125 THR N N 15 115 0.1 . 1 . . . . 140 THR N . 7428 1 483 . 1 1 126 126 THR H H 1 7.88 0.1 . 1 . . . . 141 THR H . 7428 1 484 . 1 1 126 126 THR C C 13 176.3 0.1 . 1 . . . . 141 THR C . 7428 1 485 . 1 1 126 126 THR CA C 13 63.9 0.1 . 1 . . . . 141 THR CA . 7428 1 486 . 1 1 126 126 THR N N 15 114.5 0.1 . 1 . . . . 141 THR N . 7428 1 487 . 1 1 127 127 ARG H H 1 7.82 0.1 . 1 . . . . 142 ARG H . 7428 1 488 . 1 1 127 127 ARG C C 13 177.6 0.1 . 1 . . . . 142 ARG C . 7428 1 489 . 1 1 127 127 ARG CA C 13 57.7 0.1 . 1 . . . . 142 ARG CA . 7428 1 490 . 1 1 127 127 ARG N N 15 122.9 0.1 . 1 . . . . 142 ARG N . 7428 1 491 . 1 1 128 128 ALA H H 1 7.81 0.1 . 1 . . . . 143 ALA H . 7428 1 492 . 1 1 128 128 ALA C C 13 179.7 0.1 . 1 . . . . 143 ALA C . 7428 1 493 . 1 1 128 128 ALA CA C 13 53.7 0.1 . 1 . . . . 143 ALA CA . 7428 1 494 . 1 1 128 128 ALA N N 15 123.1 0.1 . 1 . . . . 143 ALA N . 7428 1 495 . 1 1 129 129 LEU H H 1 7.92 0.1 . 1 . . . . 144 LEU H . 7428 1 496 . 1 1 129 129 LEU C C 13 178.5 0.1 . 1 . . . . 144 LEU C . 7428 1 497 . 1 1 129 129 LEU CA C 13 57.1 0.1 . 1 . . . . 144 LEU CA . 7428 1 498 . 1 1 129 129 LEU N N 15 118.8 0.1 . 1 . . . . 144 LEU N . 7428 1 499 . 1 1 130 130 HIS H H 1 8.03 0.1 . 1 . . . . 145 HIS H . 7428 1 500 . 1 1 130 130 HIS C C 13 176.6 0.1 . 1 . . . . 145 HIS C . 7428 1 501 . 1 1 130 130 HIS CA C 13 58.1 0.1 . 1 . . . . 145 HIS CA . 7428 1 502 . 1 1 130 130 HIS N N 15 116.6 0.1 . 1 . . . . 145 HIS N . 7428 1 503 . 1 1 131 131 GLU H H 1 7.97 0.1 . 1 . . . . 146 GLU H . 7428 1 504 . 1 1 131 131 GLU C C 13 178.4 0.1 . 1 . . . . 146 GLU C . 7428 1 505 . 1 1 131 131 GLU CA C 13 58.2 0.1 . 1 . . . . 146 GLU CA . 7428 1 506 . 1 1 131 131 GLU N N 15 118.7 0.1 . 1 . . . . 146 GLU N . 7428 1 507 . 1 1 132 132 ARG H H 1 7.64 0.1 . 1 . . . . 147 ARG H . 7428 1 508 . 1 1 132 132 ARG C C 13 177.1 0.1 . 1 . . . . 147 ARG C . 7428 1 509 . 1 1 132 132 ARG CA C 13 56.5 0.1 . 1 . . . . 147 ARG CA . 7428 1 510 . 1 1 132 132 ARG N N 15 119.1 0.1 . 1 . . . . 147 ARG N . 7428 1 511 . 1 1 133 133 PHE H H 1 7.9 0.1 . 1 . . . . 148 PHE H . 7428 1 512 . 1 1 133 133 PHE C C 13 176.8 0.1 . 1 . . . . 148 PHE C . 7428 1 513 . 1 1 133 133 PHE CA C 13 58.7 0.1 . 1 . . . . 148 PHE CA . 7428 1 514 . 1 1 133 133 PHE N N 15 119.2 0.1 . 1 . . . . 148 PHE N . 7428 1 515 . 1 1 134 134 ASP H H 1 8.02 0.1 . 1 . . . . 149 ASP H . 7428 1 516 . 1 1 134 134 ASP C C 13 178.3 0.1 . 1 . . . . 149 ASP C . 7428 1 517 . 1 1 134 134 ASP CA C 13 57 0.1 . 1 . . . . 149 ASP CA . 7428 1 518 . 1 1 134 134 ASP N N 15 120 0.1 . 1 . . . . 149 ASP N . 7428 1 519 . 1 1 135 135 ARG H H 1 7.74 0.1 . 1 . . . . 150 ARG H . 7428 1 520 . 1 1 135 135 ARG C C 13 178.6 0.1 . 1 . . . . 150 ARG C . 7428 1 521 . 1 1 135 135 ARG CA C 13 56.5 0.1 . 1 . . . . 150 ARG CA . 7428 1 522 . 1 1 135 135 ARG N N 15 119.3 0.1 . 1 . . . . 150 ARG N . 7428 1 523 . 1 1 136 136 LEU H H 1 7.57 0.1 . 1 . . . . 151 LEU H . 7428 1 524 . 1 1 136 136 LEU C C 13 178.4 0.1 . 1 . . . . 151 LEU C . 7428 1 525 . 1 1 136 136 LEU CA C 13 57.2 0.1 . 1 . . . . 151 LEU CA . 7428 1 526 . 1 1 136 136 LEU N N 15 120.3 0.1 . 1 . . . . 151 LEU N . 7428 1 527 . 1 1 137 137 GLU H H 1 8.07 0.1 . 1 . . . . 152 GLU H . 7428 1 528 . 1 1 137 137 GLU C C 13 178.4 0.1 . 1 . . . . 152 GLU C . 7428 1 529 . 1 1 137 137 GLU CA C 13 58.9 0.1 . 1 . . . . 152 GLU CA . 7428 1 530 . 1 1 137 137 GLU N N 15 118.1 0.1 . 1 . . . . 152 GLU N . 7428 1 531 . 1 1 138 138 ARG H H 1 7.66 0.1 . 1 . . . . 153 ARG H . 7428 1 532 . 1 1 138 138 ARG C C 13 178.4 0.1 . 1 . . . . 153 ARG C . 7428 1 533 . 1 1 138 138 ARG CA C 13 58.3 0.1 . 1 . . . . 153 ARG CA . 7428 1 534 . 1 1 138 138 ARG N N 15 118.4 0.1 . 1 . . . . 153 ARG N . 7428 1 535 . 1 1 139 139 MET H H 1 7.68 0.1 . 1 . . . . 154 MET H . 7428 1 536 . 1 1 139 139 MET C C 13 177.9 0.1 . 1 . . . . 154 MET C . 7428 1 537 . 1 1 139 139 MET CA C 13 57.7 0.1 . 1 . . . . 154 MET CA . 7428 1 538 . 1 1 139 139 MET N N 15 118.8 0.1 . 1 . . . . 154 MET N . 7428 1 539 . 1 1 140 140 LEU H H 1 7.73 0.1 . 1 . . . . 155 LEU H . 7428 1 540 . 1 1 140 140 LEU C C 13 178.5 0.1 . 1 . . . . 155 LEU C . 7428 1 541 . 1 1 140 140 LEU CA C 13 57.8 0.1 . 1 . . . . 155 LEU CA . 7428 1 542 . 1 1 140 140 LEU N N 15 119.4 0.1 . 1 . . . . 155 LEU N . 7428 1 543 . 1 1 141 141 ASP H H 1 7.89 0.1 . 1 . . . . 156 ASP H . 7428 1 544 . 1 1 141 141 ASP C C 13 177.5 0.1 . 1 . . . . 156 ASP C . 7428 1 545 . 1 1 141 141 ASP CA C 13 55.4 0.1 . 1 . . . . 156 ASP CA . 7428 1 546 . 1 1 141 141 ASP N N 15 119 0.1 . 1 . . . . 156 ASP N . 7428 1 547 . 1 1 142 142 ASP H H 1 8 0.1 . 1 . . . . 157 ASP H . 7428 1 548 . 1 1 142 142 ASP C C 13 176.9 0.1 . 1 . . . . 157 ASP C . 7428 1 549 . 1 1 142 142 ASP CA C 13 55.2 0.1 . 1 . . . . 157 ASP CA . 7428 1 550 . 1 1 142 142 ASP N N 15 119.2 0.1 . 1 . . . . 157 ASP N . 7428 1 551 . 1 1 143 143 ASN H H 1 7.85 0.1 . 1 . . . . 158 ASN H . 7428 1 552 . 1 1 143 143 ASN C C 13 175.3 0.1 . 1 . . . . 158 ASN C . 7428 1 553 . 1 1 143 143 ASN CA C 13 53.8 0.1 . 1 . . . . 158 ASN CA . 7428 1 554 . 1 1 143 143 ASN N N 15 117.6 0.1 . 1 . . . . 158 ASN N . 7428 1 555 . 1 1 144 144 ARG H H 1 7.67 0.1 . 1 . . . . 159 ARG H . 7428 1 556 . 1 1 144 144 ARG C C 13 175.9 0.1 . 1 . . . . 159 ARG C . 7428 1 557 . 1 1 144 144 ARG CA C 13 56.3 0.1 . 1 . . . . 159 ARG CA . 7428 1 558 . 1 1 144 144 ARG N N 15 120 0.1 . 1 . . . . 159 ARG N . 7428 1 559 . 1 1 145 145 ARG H H 1 7.57 0.1 . 1 . . . . 160 ARG H . 7428 1 560 . 1 1 145 145 ARG C C 13 181.1 0.1 . 1 . . . . 160 ARG C . 7428 1 561 . 1 1 145 145 ARG CA C 13 57.1 0.1 . 1 . . . . 160 ARG CA . 7428 1 562 . 1 1 145 145 ARG N N 15 126.1 0.1 . 1 . . . . 160 ARG N . 7428 1 stop_ save_