data_4465 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4465 _Entry.Title ; The Structural role of the Copper-coordinating and Surface-exposed Histidine Residue in the Blue Copper Protein Azurin ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 1999-11-24 _Entry.Accession_date 1999-11-26 _Entry.Last_release_date 2000-06-19 _Entry.Original_release_date 2000-06-19 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Lars Jeuken . J.C. . 4465 2 Marcellus Ubbink . . . 4465 3 Johannes Bitter . H. . 4465 4 Pieter 'van Vliet' . . . 4465 5 W. Meyer-Klaucke . . . 4465 6 Gerard Canters . W. . 4465 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4465 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 245 4465 '15N chemical shifts' 123 4465 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2000-06-19 1999-11-24 original author . 4465 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4465 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10835281 _Citation.Full_citation ; Jeuken, L.J., Ubbink, M., Bitter, J.H., van Vliet, P., Meyer-Klaucke, W., and Canters, G.W., "The Structural role of the Copper-coordinating and Surface-exposed Histidine Residue in the Blue Copper Protein Azurin," J. Mol. Biol. 299, 737-755 (2000). ; _Citation.Title ; The Structural role of the Copper-coordinating and Surface-exposed Histidine Residue in the Blue Copper Protein Azurin ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of Molecular Biology' _Citation.Journal_volume 299 _Citation.Journal_issue 3 _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 737 _Citation.Page_last 755 _Citation.Year 2000 _Citation.Details ; Copper K-edge EXAFS spectroscopy and 15N NMR relaxation studies were performed on samples of a variant azurin in which the surface exposed histidine ligand of the copper (His117) had been replaced by a glycine ; 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 Lars Jeuken . J.C. . 4465 1 2 Marcellus Ubbink . . . 4465 1 3 Johannes Bitter . H. . 4465 1 4 Pieter 'van Vliet' . . . 4465 1 5 W. Meyer-Klaucke . . . 4465 1 6 Gerard Canters . W. . 4465 1 stop_ save_ save_Ref._1 _Citation.Sf_category citations _Citation.Sf_framecode Ref._1 _Citation.Entry_ID 4465 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; provided by Wayne Boucher and the Department of Biochemistry, University of Cambridge. The code may be obtained via anonymous ftp to www.bio.cam.ac.uk in the directory ~ftp/pub/azara ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ save_Ref._2 _Citation.Sf_category citations _Citation.Sf_framecode Ref._2 _Citation.Entry_ID 4465 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Kraulis, P. J. (1989). ANSIG: A program for the assignment of protein 1H 2D NMR spectra by interactive graphics. J. Magn. Reson. 84, 627-633. ; _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ ############################################# # Molecular system (assembly) description # ############################################# save_H117G_azurin _Assembly.Sf_category assembly _Assembly.Sf_framecode H117G_azurin _Assembly.Entry_ID 4465 _Assembly.ID 1 _Assembly.Name 'His117Gly azurin' _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 'disulfide bound and other bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details ; The copper ligand residue His117 has been replaced by a Gly in the azurin studied here. ; _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4465 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 'His117Gly azurin' 1 $polymer_H117G_azurin . . . native . . . . . 4465 1 2 CU 2 $CU1 . . . native . . . . . 4465 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 3 3 SG . 1 . 1 CYS 26 26 SG . . . . . . . . . . 4465 1 2 coordinative single . 1 . 1 CYS 112 112 SG . 2 . 2 CU1 1 1 CU . . . . . . . . . . 4465 1 stop_ loop_ _Entity_deleted_atom.ID _Entity_deleted_atom.Entity_atom_list_ID _Entity_deleted_atom.Entity_assembly_ID _Entity_deleted_atom.Entity_ID _Entity_deleted_atom.Comp_ID _Entity_deleted_atom.Comp_index_ID _Entity_deleted_atom.Seq_ID _Entity_deleted_atom.Atom_ID _Entity_deleted_atom.Auth_entity_assembly_ID _Entity_deleted_atom.Auth_seq_ID _Entity_deleted_atom.Auth_comp_ID _Entity_deleted_atom.Auth_atom_ID _Entity_deleted_atom.Entry_ID _Entity_deleted_atom.Assembly_ID 1 . 1 1 CYS 3 3 HG . . . . 4465 1 2 . 1 1 CYS 26 26 HG . . . . 4465 1 3 . 1 1 CYS 112 112 HG . . . . 4465 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'His117Gly azurin' system 4465 1 'H117G azurin' abbreviation 4465 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_polymer_H117G_azurin _Entity.Sf_category entity _Entity.Sf_framecode polymer_H117G_azurin _Entity.Entry_ID 4465 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'P. Aeruginosa HIs117Gly azurin' _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 ; AECSVDIQGNDQMQFNTNAI TVDKSCKQFTVNLSHPGNLP KNVMGHNWVLSTAADMQGVV TDGMASGLDKDYLKPDDSRV IAHTKLIGSGEKDSVTFDVS KLKEGEQYMFFCTFPGGSAL MKGTLTLK ; _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 128 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'disulfide bound and other bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 1210 . azurin . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 2 no BMRB 1211 . azurin . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 3 no BMRB 1212 . azurin . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 4 no BMRB 1213 . azurin . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 5 no BMRB 1214 . azurin . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 6 no BMRB 1215 . azurin . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 7 no BMRB 1216 . azurin . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 8 no BMRB 1217 . azurin . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 9 no BMRB 1218 . azurin . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 10 no BMRB 1219 . azurin . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 11 no BMRB 18254 . apo-azurin . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 12 no PDB 1AG0 . "Structure Of Cys 112 Asp Azurin From Pseudomonas Aeruginosa" . . . . . 100.00 129 98.44 98.44 5.66e-86 . . . . 4465 1 13 no PDB 1AZN . "Crystal Structure Of The Azurin Mutant Phe114ala From Pseudomonas Aeruginosa At 2.6 Angstroms Resolution" . . . . . 100.00 128 98.44 98.44 1.49e-86 . . . . 4465 1 14 no PDB 1AZR . "Crystal Structure Of Pseudomonas Aeruginosa Zinc Azurin Mutant Asp47asp At 2.4 Angstroms Resolution" . . . . . 100.00 128 97.66 99.22 2.07e-86 . . . . 4465 1 15 no PDB 1AZU . "Structural Features Of Azurin At 2.7 Angstroms Resolution" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 16 no PDB 1BEX . "Structure Of Ruthenium-modified Pseudomonas Aeruginosa Azurin" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 17 no PDB 1E5Y . "Azurin From Pseudomonas Aeruginosa, Reduced Form, Ph 5.5" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 18 no PDB 1E5Z . "Azurin From Pseudomonas Aeruginosa, Reduced Form, Ph 9.0" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 19 no PDB 1E65 . "Azurin From Pseudomonas Aeruginosa, Apo Form" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 20 no PDB 1E67 . "Zn-azurin From Pseudomonas Aeruginosa" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 21 no PDB 1ETJ . "Azurin Mutant With Met 121 Replaced By Glu" . . . . . 100.00 128 98.44 98.44 1.37e-86 . . . . 4465 1 22 no PDB 1EZL . "Crystal Structure Of The Disulphide Bond-Deficient Azurin Mutant C3aC26A: HOW IMPORTANT IS THE S-S Bond For Folding And Stabili" . . . . . 100.00 128 97.66 97.66 1.01e-85 . . . . 4465 1 23 no PDB 1ILS . "X-Ray Crystal Structure The Two Site-Specific Mutants Ile7ser And Phe110ser Of Azurin From Pseudomonas Aeruginosa" . . . . . 100.00 128 98.44 98.44 9.87e-87 . . . . 4465 1 24 no PDB 1ILU . "X-Ray Crystal Structure The Two Site-Specific Mutants Ile7ser And Phe110ser Of Azurin From Pseudomonas Aeruginosa" . . . . . 100.00 128 98.44 98.44 1.88e-86 . . . . 4465 1 25 no PDB 1JVL . "Azurin Dimer, Covalently Crosslinked Through Bis- Maleimidomethylether" . . . . . 100.00 128 98.44 98.44 3.21e-86 . . . . 4465 1 26 no PDB 1JVO . "Azurin Dimer, Crosslinked Via Disulfide Bridge" . . . . . 100.00 128 98.44 98.44 3.21e-86 . . . . 4465 1 27 no PDB 1JZE . "Pseudomonas Aeruginosa Azurin Ru(Bpy)2(Im)(His83)" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 28 no PDB 1JZF . "Pseudomonas Aeruginosa Oxidized Azurin(Cu2+) Ru(Tpy)(Phen) (His83)" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 29 no PDB 1JZG . "Pseudomonas Aeruginosa Reduced Azurin (Cu1+) Ru(Tpy)(Phen) (His83)" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 30 no PDB 1JZH . "Pseudomonas Aeruginosa Azurin Ru(tpy)(bpy)(his83)" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 31 no PDB 1JZI . "Pseudomonas Aeruginosa Azurin Re(Phen)(Co)3(His83)" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 32 no PDB 1JZJ . "Pseudomonas Aeruginosa Azurin Os(Bpy)2(Im)(His83)" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 33 no PDB 1NZR . "Crystal Structure Of The Azurin Mutant Nickel-trp48met From Pseudomonas Aeruginosa At 2.2 Angstroms Resolution" . . . . . 99.22 128 98.43 98.43 2.08e-85 . . . . 4465 1 34 no PDB 1VLX . "Structure Of Electron Transfer (cobalt-protein)" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 35 no PDB 1XB6 . "The K24r Mutant Of Pseudomonas Aeruginosa Azurin" . . . . . 100.00 128 98.44 99.22 1.80e-87 . . . . 4465 1 36 no PDB 1XB8 . "Zn Substituted Form Of D62cK74C DOUBLE MUTANT OF PSEUDOMONAS Aeruginosa Azurin" . . . . . 100.00 128 97.66 97.66 5.43e-85 . . . . 4465 1 37 no PDB 2AZU . "X-ray Crystal Structure Of The Two Site-specific Mutants His35*gln And His35*leu Of Azurin From Pseudomonas Aeruginosa" . . . . . 100.00 128 97.66 98.44 1.53e-85 . . . . 4465 1 38 no PDB 2GHZ . "Crystal Structure Of Azurin Phe114pro Mutant" . . . . . 100.00 128 98.44 98.44 3.74e-86 . . . . 4465 1 39 no PDB 2GI0 . "Crystal Structure Of Cu(I) Phe114pro Azurin Mutant" . . . . . 100.00 128 98.44 98.44 3.74e-86 . . . . 4465 1 40 no PDB 2IDF . "P. Aeruginosa Azurin N42c/m64e Double Mutant, Bmme-linked Dimer" . . . . . 100.00 128 97.66 97.66 3.63e-85 . . . . 4465 1 41 no PDB 2IWE . "Structure Of A Cavity Mutant (H117g) Of Pseudomonas Aeruginosa Azurin" . . . . . 100.00 128 100.00 100.00 8.63e-89 . . . . 4465 1 42 no PDB 2OJ1 . "Disulfide-Linked Dimer Of Azurin N42cM64E DOUBLE MUTANT" . . . . . 100.00 128 97.66 97.66 3.63e-85 . . . . 4465 1 43 no PDB 2TSA . "Azurin Mutant M121a" . . . . . 100.00 128 98.44 98.44 8.56e-87 . . . . 4465 1 44 no PDB 2TSB . "Azurin Mutant M121a-Azide" . . . . . 100.00 128 98.44 98.44 8.56e-87 . . . . 4465 1 45 no PDB 3AZU . "X-ray Crystal Structure Of The Two Site-specific Mutants His35gln And His35leu Of Azurin From Pseudomonas Aeruginosa" . . . . . 100.00 128 97.66 98.44 5.30e-86 . . . . 4465 1 46 no PDB 3FPY . "Azurin C112dM121L" . . . . . 100.00 128 97.66 98.44 1.69e-85 . . . . 4465 1 47 no PDB 3FQ1 . "Azurin C112dM121I" . . . . . 100.00 128 97.66 98.44 2.45e-85 . . . . 4465 1 48 no PDB 3FQ2 . "Azurin C112dM121F" . . . . . 100.00 128 97.66 97.66 4.13e-85 . . . . 4465 1 49 no PDB 3FQY . "Azurin C112d" . . . . . 100.00 128 98.44 98.44 5.48e-86 . . . . 4465 1 50 no PDB 3IN0 . "Crystal Structure Of The F114pM121Q VARIANT OF PSEUDOMONAS Aeruginosa Azurin In The Cu(Ii) State" . . . . . 100.00 128 97.66 97.66 3.15e-85 . . . . 4465 1 51 no PDB 3IN2 . "Crystal Structure Of The N47sM121L VARIANT OF PSEUDOMONAS Aeruginosa Azurin In The Cu(Ii) State" . . . . . 100.00 128 97.66 99.22 1.96e-86 . . . . 4465 1 52 no PDB 3JT2 . "Cu(Ii) N47sM121L VARIANT OF PSEUDOMONAS AERUGINOSA AZURIN" . . . . . 100.00 128 97.66 99.22 1.96e-86 . . . . 4465 1 53 no PDB 3JTB . "Cu(Ii) N47sF114N VARIANT OF PSEUDOMONAS AERUGINOSA AZURIN" . . . . . 100.00 128 97.66 98.44 1.55e-85 . . . . 4465 1 54 no PDB 3N2J . "Azurin H117g, Oxidized Form" . . . . . 100.00 128 100.00 100.00 8.63e-89 . . . . 4465 1 55 no PDB 3NP3 . "C112dM121E PSEUDOMONAS AERUGINOSA AZURIN" . . . . . 100.00 128 97.66 97.66 7.87e-85 . . . . 4465 1 56 no PDB 3NP4 . "C112dM121E PSEUDOMONAS AERUGINOSA AZURIN" . . . . . 100.00 128 97.66 97.66 7.87e-85 . . . . 4465 1 57 no PDB 3OQR . "C112dM121E AZURIN, PH 10.0" . . . . . 100.00 128 97.66 97.66 7.87e-85 . . . . 4465 1 58 no PDB 3UGE . "Silver Metallated Pseudomonas Aeruginosa Azurin At 1.70 A" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 59 no PDB 4AZU . "Crystal Structure Analysis Of Oxidized Pseudomonas Aeruginosa Azurin At Ph 5.5 And Ph 9.0. A Ph-Induced Conformational Transiti" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 60 no PDB 4BWW . "Crystal Structure Of Spin Labelled Azurin T21r1" . . . . . 100.00 131 98.44 98.44 6.81e-87 . . . . 4465 1 61 no PDB 4HZ1 . "Crystal Structure Of Pseudomonas Aeruginosa Azurin With Iron(Ii) At The Copper-Binding Site." . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 62 no PDB 4JKN . "Mercury Metallated Pseudomonas Aeruginosa Azurin At 1.54 A" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 63 no PDB 4KO9 . "Investigating The Functional Significance Of The Interlocked Pair Structural Determinants In Pseudomonas Aeruginosa Azurin (v95" . . . . . 100.00 128 97.66 99.22 7.27e-87 . . . . 4465 1 64 no PDB 4KOB . "Investigating The Functional Significance Of The Interlocked Pair Structural Determinants In Pseudomonas Aeruginosa Azurin (v31" . . . . . 100.00 128 97.66 99.22 2.09e-87 . . . . 4465 1 65 no PDB 4MFH . "Crystal Structure Of M121g Azurin" . . . . . 100.00 128 98.44 98.44 3.14e-86 . . . . 4465 1 66 no PDB 4QKT . "Azurin Mutant M121em44k With Copper" . . . . . 100.00 128 97.66 97.66 1.33e-85 . . . . 4465 1 67 no PDB 4QLW . "Azurin Mutant M121e With Iron" . . . . . 100.00 128 98.44 98.44 1.37e-86 . . . . 4465 1 68 no PDB 5AZU . "Crystal Structure Analysis Of Oxidized Pseudomonas Aeruginosa Azurin At Ph 5.5 And Ph 9.0. A Ph-Induced Conformational Transiti" . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 69 no DBJ BAK87490 . "azurin precursor [Pseudomonas aeruginosa NCGM2.S1]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 70 no DBJ BAP24727 . "azurin precursor [Pseudomonas aeruginosa]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 71 no DBJ BAP53499 . "azurin precursor [Pseudomonas aeruginosa]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 72 no DBJ BAQ42761 . "azurin precursor [Pseudomonas aeruginosa]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 73 no DBJ BAR70381 . "azurin [Pseudomonas aeruginosa]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 74 no EMBL CAA30279 . "unnamed protein product [Pseudomonas aeruginosa]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 75 no EMBL CAW30062 . "azurin precursor [Pseudomonas aeruginosa LESB58]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 76 no EMBL CCQ86145 . "azurin precursor [Pseudomonas aeruginosa 18A]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 77 no EMBL CDH73668 . "Azurin [Pseudomonas aeruginosa MH38]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 78 no EMBL CDH79986 . "Azurin [Pseudomonas aeruginosa MH27]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 79 no GB AAA25730 . "azurin [Pseudomonas aeruginosa]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 80 no GB AAG08307 . "azurin precursor [Pseudomonas aeruginosa PAO1]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 81 no GB AAP03090 . "azurin [Burkholderia cepacia]" . . . . . 100.00 148 97.66 98.44 6.46e-86 . . . . 4465 1 82 no GB AAT49489 . "PA4922, partial [synthetic construct]" . . . . . 100.00 149 98.44 98.44 4.13e-87 . . . . 4465 1 83 no GB ABJ14307 . "azurin precursor [Pseudomonas aeruginosa UCBPP-PA14]" . . . . . 100.00 148 98.44 99.22 7.60e-88 . . . . 4465 1 84 no PRF 671048A . azurin . . . . . 100.00 128 99.22 99.22 1.03e-87 . . . . 4465 1 85 no REF NP_253609 . "azurin [Pseudomonas aeruginosa PAO1]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 86 no REF WP_003095591 . "MULTISPECIES: azurin [Pseudomonas]" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 87 no REF WP_003141697 . "azurin [Pseudomonas aeruginosa]" . . . . . 100.00 148 98.44 99.22 7.60e-88 . . . . 4465 1 88 no REF WP_031690945 . "azurin [Pseudomonas aeruginosa]" . . . . . 100.00 148 98.44 99.22 5.48e-88 . . . . 4465 1 89 no REF WP_033949908 . "azurin [Pseudomonas aeruginosa]" . . . . . 100.00 148 99.22 99.22 2.39e-88 . . . . 4465 1 90 no SP B3EWN9 . "RecName: Full=Azurin" . . . . . 100.00 128 98.44 98.44 1.88e-86 . . . . 4465 1 91 no SP P00282 . "RecName: Full=Azurin; Flags: Precursor" . . . . . 100.00 148 99.22 99.22 2.34e-88 . . . . 4465 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'P. Aeruginosa HIs117Gly azurin' common 4465 1 His117Gly variant 4465 1 'H117G azurin' abbreviation 4465 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 1 ALA . 4465 1 2 2 GLU . 4465 1 3 3 CYS . 4465 1 4 4 SER . 4465 1 5 5 VAL . 4465 1 6 6 ASP . 4465 1 7 7 ILE . 4465 1 8 8 GLN . 4465 1 9 9 GLY . 4465 1 10 10 ASN . 4465 1 11 11 ASP . 4465 1 12 12 GLN . 4465 1 13 13 MET . 4465 1 14 14 GLN . 4465 1 15 15 PHE . 4465 1 16 16 ASN . 4465 1 17 17 THR . 4465 1 18 18 ASN . 4465 1 19 19 ALA . 4465 1 20 20 ILE . 4465 1 21 21 THR . 4465 1 22 22 VAL . 4465 1 23 23 ASP . 4465 1 24 24 LYS . 4465 1 25 25 SER . 4465 1 26 26 CYS . 4465 1 27 27 LYS . 4465 1 28 28 GLN . 4465 1 29 29 PHE . 4465 1 30 30 THR . 4465 1 31 31 VAL . 4465 1 32 32 ASN . 4465 1 33 33 LEU . 4465 1 34 34 SER . 4465 1 35 35 HIS . 4465 1 36 36 PRO . 4465 1 37 37 GLY . 4465 1 38 38 ASN . 4465 1 39 39 LEU . 4465 1 40 40 PRO . 4465 1 41 41 LYS . 4465 1 42 42 ASN . 4465 1 43 43 VAL . 4465 1 44 44 MET . 4465 1 45 45 GLY . 4465 1 46 46 HIS . 4465 1 47 47 ASN . 4465 1 48 48 TRP . 4465 1 49 49 VAL . 4465 1 50 50 LEU . 4465 1 51 51 SER . 4465 1 52 52 THR . 4465 1 53 53 ALA . 4465 1 54 54 ALA . 4465 1 55 55 ASP . 4465 1 56 56 MET . 4465 1 57 57 GLN . 4465 1 58 58 GLY . 4465 1 59 59 VAL . 4465 1 60 60 VAL . 4465 1 61 61 THR . 4465 1 62 62 ASP . 4465 1 63 63 GLY . 4465 1 64 64 MET . 4465 1 65 65 ALA . 4465 1 66 66 SER . 4465 1 67 67 GLY . 4465 1 68 68 LEU . 4465 1 69 69 ASP . 4465 1 70 70 LYS . 4465 1 71 71 ASP . 4465 1 72 72 TYR . 4465 1 73 73 LEU . 4465 1 74 74 LYS . 4465 1 75 75 PRO . 4465 1 76 76 ASP . 4465 1 77 77 ASP . 4465 1 78 78 SER . 4465 1 79 79 ARG . 4465 1 80 80 VAL . 4465 1 81 81 ILE . 4465 1 82 82 ALA . 4465 1 83 83 HIS . 4465 1 84 84 THR . 4465 1 85 85 LYS . 4465 1 86 86 LEU . 4465 1 87 87 ILE . 4465 1 88 88 GLY . 4465 1 89 89 SER . 4465 1 90 90 GLY . 4465 1 91 91 GLU . 4465 1 92 92 LYS . 4465 1 93 93 ASP . 4465 1 94 94 SER . 4465 1 95 95 VAL . 4465 1 96 96 THR . 4465 1 97 97 PHE . 4465 1 98 98 ASP . 4465 1 99 99 VAL . 4465 1 100 100 SER . 4465 1 101 101 LYS . 4465 1 102 102 LEU . 4465 1 103 103 LYS . 4465 1 104 104 GLU . 4465 1 105 105 GLY . 4465 1 106 106 GLU . 4465 1 107 107 GLN . 4465 1 108 108 TYR . 4465 1 109 109 MET . 4465 1 110 110 PHE . 4465 1 111 111 PHE . 4465 1 112 112 CYS . 4465 1 113 113 THR . 4465 1 114 114 PHE . 4465 1 115 115 PRO . 4465 1 116 116 GLY . 4465 1 117 117 GLY . 4465 1 118 118 SER . 4465 1 119 119 ALA . 4465 1 120 120 LEU . 4465 1 121 121 MET . 4465 1 122 122 LYS . 4465 1 123 123 GLY . 4465 1 124 124 THR . 4465 1 125 125 LEU . 4465 1 126 126 THR . 4465 1 127 127 LEU . 4465 1 128 128 LYS . 4465 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 . ALA 1 1 4465 1 . GLU 2 2 4465 1 . CYS 3 3 4465 1 . SER 4 4 4465 1 . VAL 5 5 4465 1 . ASP 6 6 4465 1 . ILE 7 7 4465 1 . GLN 8 8 4465 1 . GLY 9 9 4465 1 . ASN 10 10 4465 1 . ASP 11 11 4465 1 . GLN 12 12 4465 1 . MET 13 13 4465 1 . GLN 14 14 4465 1 . PHE 15 15 4465 1 . ASN 16 16 4465 1 . THR 17 17 4465 1 . ASN 18 18 4465 1 . ALA 19 19 4465 1 . ILE 20 20 4465 1 . THR 21 21 4465 1 . VAL 22 22 4465 1 . ASP 23 23 4465 1 . LYS 24 24 4465 1 . SER 25 25 4465 1 . CYS 26 26 4465 1 . LYS 27 27 4465 1 . GLN 28 28 4465 1 . PHE 29 29 4465 1 . THR 30 30 4465 1 . VAL 31 31 4465 1 . ASN 32 32 4465 1 . LEU 33 33 4465 1 . SER 34 34 4465 1 . HIS 35 35 4465 1 . PRO 36 36 4465 1 . GLY 37 37 4465 1 . ASN 38 38 4465 1 . LEU 39 39 4465 1 . PRO 40 40 4465 1 . LYS 41 41 4465 1 . ASN 42 42 4465 1 . VAL 43 43 4465 1 . MET 44 44 4465 1 . GLY 45 45 4465 1 . HIS 46 46 4465 1 . ASN 47 47 4465 1 . TRP 48 48 4465 1 . VAL 49 49 4465 1 . LEU 50 50 4465 1 . SER 51 51 4465 1 . THR 52 52 4465 1 . ALA 53 53 4465 1 . ALA 54 54 4465 1 . ASP 55 55 4465 1 . MET 56 56 4465 1 . GLN 57 57 4465 1 . GLY 58 58 4465 1 . VAL 59 59 4465 1 . VAL 60 60 4465 1 . THR 61 61 4465 1 . ASP 62 62 4465 1 . GLY 63 63 4465 1 . MET 64 64 4465 1 . ALA 65 65 4465 1 . SER 66 66 4465 1 . GLY 67 67 4465 1 . LEU 68 68 4465 1 . ASP 69 69 4465 1 . LYS 70 70 4465 1 . ASP 71 71 4465 1 . TYR 72 72 4465 1 . LEU 73 73 4465 1 . LYS 74 74 4465 1 . PRO 75 75 4465 1 . ASP 76 76 4465 1 . ASP 77 77 4465 1 . SER 78 78 4465 1 . ARG 79 79 4465 1 . VAL 80 80 4465 1 . ILE 81 81 4465 1 . ALA 82 82 4465 1 . HIS 83 83 4465 1 . THR 84 84 4465 1 . LYS 85 85 4465 1 . LEU 86 86 4465 1 . ILE 87 87 4465 1 . GLY 88 88 4465 1 . SER 89 89 4465 1 . GLY 90 90 4465 1 . GLU 91 91 4465 1 . LYS 92 92 4465 1 . ASP 93 93 4465 1 . SER 94 94 4465 1 . VAL 95 95 4465 1 . THR 96 96 4465 1 . PHE 97 97 4465 1 . ASP 98 98 4465 1 . VAL 99 99 4465 1 . SER 100 100 4465 1 . LYS 101 101 4465 1 . LEU 102 102 4465 1 . LYS 103 103 4465 1 . GLU 104 104 4465 1 . GLY 105 105 4465 1 . GLU 106 106 4465 1 . GLN 107 107 4465 1 . TYR 108 108 4465 1 . MET 109 109 4465 1 . PHE 110 110 4465 1 . PHE 111 111 4465 1 . CYS 112 112 4465 1 . THR 113 113 4465 1 . PHE 114 114 4465 1 . PRO 115 115 4465 1 . GLY 116 116 4465 1 . GLY 117 117 4465 1 . SER 118 118 4465 1 . ALA 119 119 4465 1 . LEU 120 120 4465 1 . MET 121 121 4465 1 . LYS 122 122 4465 1 . GLY 123 123 4465 1 . THR 124 124 4465 1 . LEU 125 125 4465 1 . THR 126 126 4465 1 . LEU 127 127 4465 1 . LYS 128 128 4465 1 stop_ save_ save_CU1 _Entity.Sf_category entity _Entity.Sf_framecode CU1 _Entity.Entry_ID 4465 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name CU1 _Entity.Type non-polymer _Entity.Polymer_common_type . _Entity.Polymer_type . _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code . _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer . _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID CU1 _Entity.Nonpolymer_comp_label $chem_comp_CU1 _Entity.Number_of_monomers . _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 2 _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 . 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 . CU1 . 4465 2 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 4465 _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 $polymer_H117G_azurin . 287 organism . 'Pseudomonas aeruginosa' 'fluorescent pseudomonads' . . Eubacteria . Pseudomonas aeruginosa . . . . . . . . . . . . periplasm . . . . . . . . 4465 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 4465 _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 $polymer_H117G_azurin . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4465 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_CU1 _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_CU1 _Chem_comp.Entry_ID 4465 _Chem_comp.ID CU1 _Chem_comp.Provenance . _Chem_comp.Name 'COPPER (I) ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code CU1 _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 1999-07-08 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code CU1 _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 1 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Cu _Chem_comp.Formula_weight 63.546 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site RCSB _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 18 11:12:40 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID [Cu+] SMILES ACDLabs 10.04 4465 CU1 [Cu+] SMILES_CANONICAL CACTVS 3.341 4465 CU1 [Cu+] SMILES CACTVS 3.341 4465 CU1 [Cu+] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 4465 CU1 [Cu+] SMILES 'OpenEye OEToolkits' 1.5.0 4465 CU1 InChI=1S/Cu/q+1 InChI InChI 1.03 4465 CU1 VMQMZMRVKUZKQL-UHFFFAOYSA-N InChIKey InChI 1.03 4465 CU1 stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID copper(1+) 'SYSTEMATIC NAME' ACDLabs 10.04 4465 CU1 'copper(+1) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 4465 CU1 stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID CU . CU . . CU . . N 1 . . . . no no . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 1 . 4465 CU1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Typical_Sample _Sample.Sf_category sample _Sample.Sf_framecode Typical_Sample _Sample.Entry_ID 4465 _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 'P. Aeruginosa HIs117Gly azurin' [U-15N] . . 1 $polymer_H117G_azurin . . . 3 5 mM . . . . 4465 1 stop_ save_ ####################### # Sample conditions # ####################### save_Typical_Sample_Conditions _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Typical_Sample_Conditions _Sample_condition_list.Entry_ID 4465 _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 5.5 0.2 n/a 4465 1 temperature 313 2 K 4465 1 stop_ save_ ############################ # Computer software used # ############################ save_azara _Software.Sf_category software _Software.Sf_framecode azara _Software.Entry_ID 4465 _Software.ID 1 _Software.Name azara _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'FID processing' 4465 1 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 2 $Ref._1 4465 1 stop_ save_ save_ANSIG _Software.Sf_category software _Software.Sf_framecode ANSIG _Software.Entry_ID 4465 _Software.ID 2 _Software.Name ANSIG _Software.Version 3.3 _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak assignments and peak integration' 4465 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $Ref._2 4465 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 4465 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model 'Avance DMX' _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4465 _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 'Avance DMX' . 600 . . . 4465 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 4465 _Experiment_list.ID 1 _Experiment_list.Details ; 15N-1H HSQC experiments were recorded with 9 different longitudinal relaxation periods (48, 112, 176, 256, 344, 456, 600, 808 and 944 ms). 15N T2 experiments were recorded with different values for the duration of the CPMG sequence (16, 32, 48, 64, 88, 120, 160, 208 and 248 ms). Two spectra were collected for the measurement of the 1H-15N NOE: one with proton saturation and one without. ; 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 '1H-15N HSQC' . . . . . . . . . . . 1 $Typical_Sample . . . 1 $Typical_Sample_Conditions . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4465 1 2 '1H-15N TROSY' . . . . . . . . . . . 1 $Typical_Sample . . . 1 $Typical_Sample_Conditions . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4465 1 3 '1H-15N TOCSY' . . . . . . . . . . . 1 $Typical_Sample . . . 1 $Typical_Sample_Conditions . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4465 1 4 '1H-1H TOCSY' . . . . . . . . . . . 1 $Typical_Sample . . . 1 $Typical_Sample_Conditions . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4465 1 5 '1H-15N NOESY' . . . . . . . . . . . 1 $Typical_Sample . . . 1 $Typical_Sample_Conditions . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4465 1 6 '1H-1H NOESY' . . . . . . . . . . . 1 $Typical_Sample . . . 1 $Typical_Sample_Conditions . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 4465 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 4465 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name '1H-15N HSQC' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _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 4465 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name '1H-15N TROSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4465 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name '1H-15N TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_4 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_4 _NMR_spec_expt.Entry_ID 4465 _NMR_spec_expt.ID 4 _NMR_spec_expt.Name '1H-1H TOCSY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_5 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_5 _NMR_spec_expt.Entry_ID 4465 _NMR_spec_expt.ID 5 _NMR_spec_expt.Name '1H-15N NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_6 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_6 _NMR_spec_expt.Entry_ID 4465 _NMR_spec_expt.ID 6 _NMR_spec_expt.Name '1H-1H NOESY' _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4465 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 4465 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4465 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_H117G1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode H117G1 _Assigned_chem_shift_list.Entry_ID 4465 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Typical_Sample_Conditions _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID 1 '1H-15N HSQC' 1 $Typical_Sample . 4465 1 2 '1H-15N TROSY' 1 $Typical_Sample . 4465 1 3 '1H-15N TOCSY' 1 $Typical_Sample . 4465 1 4 '1H-1H TOCSY' 1 $Typical_Sample . 4465 1 5 '1H-15N NOESY' 1 $Typical_Sample . 4465 1 6 '1H-1H NOESY' 1 $Typical_Sample . 4465 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 2 2 GLU H H 1 8.88 0.02 . 1 . . . . . . . . 4465 1 2 . 1 1 2 2 GLU HA H 1 4.48 0.02 . 1 . . . . . . . . 4465 1 3 . 1 1 2 2 GLU N N 15 124.9 0.2 . 1 . . . . . . . . 4465 1 4 . 1 1 3 3 CYS H H 1 8.7 0.02 . 1 . . . . . . . . 4465 1 5 . 1 1 3 3 CYS HA H 1 5.03 0.02 . 1 . . . . . . . . 4465 1 6 . 1 1 3 3 CYS N N 15 120.4 0.2 . 1 . . . . . . . . 4465 1 7 . 1 1 4 4 SER H H 1 7.23 0.02 . 1 . . . . . . . . 4465 1 8 . 1 1 4 4 SER HA H 1 4.65 0.02 . 1 . . . . . . . . 4465 1 9 . 1 1 4 4 SER N N 15 113.1 0.2 . 1 . . . . . . . . 4465 1 10 . 1 1 5 5 VAL H H 1 8.06 0.02 . 1 . . . . . . . . 4465 1 11 . 1 1 5 5 VAL HA H 1 4.42 0.02 . 1 . . . . . . . . 4465 1 12 . 1 1 5 5 VAL N N 15 118.9 0.2 . 1 . . . . . . . . 4465 1 13 . 1 1 6 6 ASP H H 1 8.1 0.02 . 1 . . . . . . . . 4465 1 14 . 1 1 6 6 ASP HA H 1 5.27 0.02 . 1 . . . . . . . . 4465 1 15 . 1 1 6 6 ASP N N 15 126.4 0.2 . 1 . . . . . . . . 4465 1 16 . 1 1 7 7 ILE H H 1 8.97 0.02 . 1 . . . . . . . . 4465 1 17 . 1 1 7 7 ILE HA H 1 4.78 0.02 . 1 . . . . . . . . 4465 1 18 . 1 1 7 7 ILE N N 15 124.1 0.2 . 1 . . . . . . . . 4465 1 19 . 1 1 8 8 GLN H H 1 8.33 0.02 . 1 . . . . . . . . 4465 1 20 . 1 1 8 8 GLN HA H 1 5.26 0.02 . 1 . . . . . . . . 4465 1 21 . 1 1 8 8 GLN N N 15 123.6 0.2 . 1 . . . . . . . . 4465 1 22 . 1 1 9 9 GLY H H 1 8.47 0.02 . 1 . . . . . . . . 4465 1 23 . 1 1 9 9 GLY HA2 H 1 4.99 0.02 . 1 . . . . . . . . 4465 1 24 . 1 1 9 9 GLY HA3 H 1 2.46 0.02 . 1 . . . . . . . . 4465 1 25 . 1 1 9 9 GLY N N 15 108 0.2 . 1 . . . . . . . . 4465 1 26 . 1 1 10 10 ASN H H 1 7.56 0.02 . 1 . . . . . . . . 4465 1 27 . 1 1 10 10 ASN HA H 1 5.15 0.02 . 1 . . . . . . . . 4465 1 28 . 1 1 10 10 ASN N N 15 122.4 0.2 . 1 . . . . . . . . 4465 1 29 . 1 1 11 11 ASP H H 1 8.38 0.02 . 1 . . . . . . . . 4465 1 30 . 1 1 11 11 ASP HA H 1 5.15 0.02 . 1 . . . . . . . . 4465 1 31 . 1 1 11 11 ASP N N 15 119.5 0.2 . 1 . . . . . . . . 4465 1 32 . 1 1 12 12 GLN H H 1 7.70 0.02 . 1 . . . . . . . . 4465 1 33 . 1 1 12 12 GLN HA H 1 4.49 0.02 . 1 . . . . . . . . 4465 1 34 . 1 1 12 12 GLN N N 15 117.2 0.2 . 1 . . . . . . . . 4465 1 35 . 1 1 13 13 MET H H 1 7.56 0.02 . 1 . . . . . . . . 4465 1 36 . 1 1 13 13 MET HA H 1 3.96 0.02 . 1 . . . . . . . . 4465 1 37 . 1 1 13 13 MET N N 15 114.2 0.2 . 1 . . . . . . . . 4465 1 38 . 1 1 14 14 GLN H H 1 6.96 0.02 . 1 . . . . . . . . 4465 1 39 . 1 1 14 14 GLN N N 15 111.5 0.2 . 1 . . . . . . . . 4465 1 40 . 1 1 15 15 PHE H H 1 8.93 0.02 . 1 . . . . . . . . 4465 1 41 . 1 1 15 15 PHE HA H 1 6.09 0.02 . 1 . . . . . . . . 4465 1 42 . 1 1 15 15 PHE N N 15 121.7 0.2 . 1 . . . . . . . . 4465 1 43 . 1 1 16 16 ASN H H 1 8.76 0.02 . 1 . . . . . . . . 4465 1 44 . 1 1 16 16 ASN HA H 1 4.68 0.02 . 1 . . . . . . . . 4465 1 45 . 1 1 16 16 ASN N N 15 116.6 0.2 . 1 . . . . . . . . 4465 1 46 . 1 1 17 17 THR H H 1 7.18 0.02 . 1 . . . . . . . . 4465 1 47 . 1 1 17 17 THR HA H 1 4.77 0.02 . 1 . . . . . . . . 4465 1 48 . 1 1 17 17 THR N N 15 112.4 0.2 . 1 . . . . . . . . 4465 1 49 . 1 1 18 18 ASN H H 1 8.43 0.02 . 1 . . . . . . . . 4465 1 50 . 1 1 18 18 ASN HA H 1 5.14 0.02 . 1 . . . . . . . . 4465 1 51 . 1 1 18 18 ASN N N 15 121.5 0.2 . 1 . . . . . . . . 4465 1 52 . 1 1 19 19 ALA H H 1 8.28 0.02 . 1 . . . . . . . . 4465 1 53 . 1 1 19 19 ALA HA H 1 5.51 0.02 . 1 . . . . . . . . 4465 1 54 . 1 1 19 19 ALA N N 15 123.9 0.2 . 1 . . . . . . . . 4465 1 55 . 1 1 20 20 ILE H H 1 8.98 0.02 . 1 . . . . . . . . 4465 1 56 . 1 1 20 20 ILE HA H 1 4.47 0.02 . 1 . . . . . . . . 4465 1 57 . 1 1 20 20 ILE N N 15 122.5 0.2 . 1 . . . . . . . . 4465 1 58 . 1 1 21 21 THR H H 1 8.71 0.02 . 1 . . . . . . . . 4465 1 59 . 1 1 21 21 THR HA H 1 4.95 0.02 . 1 . . . . . . . . 4465 1 60 . 1 1 21 21 THR N N 15 124.1 0.2 . 1 . . . . . . . . 4465 1 61 . 1 1 22 22 VAL H H 1 8.88 0.02 . 1 . . . . . . . . 4465 1 62 . 1 1 22 22 VAL HA H 1 3.64 0.02 . 1 . . . . . . . . 4465 1 63 . 1 1 22 22 VAL N N 15 128.0 0.2 . 1 . . . . . . . . 4465 1 64 . 1 1 23 23 ASP H H 1 8.12 0.02 . 1 . . . . . . . . 4465 1 65 . 1 1 23 23 ASP HA H 1 4.77 0.02 . 1 . . . . . . . . 4465 1 66 . 1 1 23 23 ASP N N 15 128.1 0.2 . 1 . . . . . . . . 4465 1 67 . 1 1 24 24 LYS H H 1 8.89 0.02 . 1 . . . . . . . . 4465 1 68 . 1 1 24 24 LYS HA H 1 3.94 0.02 . 1 . . . . . . . . 4465 1 69 . 1 1 24 24 LYS N N 15 126.1 0.2 . 1 . . . . . . . . 4465 1 70 . 1 1 25 25 SER H H 1 8.98 0.02 . 1 . . . . . . . . 4465 1 71 . 1 1 25 25 SER HA H 1 4.30 0.02 . 1 . . . . . . . . 4465 1 72 . 1 1 25 25 SER N N 15 115.1 0.2 . 1 . . . . . . . . 4465 1 73 . 1 1 26 26 CYS H H 1 8.28 0.02 . 1 . . . . . . . . 4465 1 74 . 1 1 26 26 CYS HA H 1 4.48 0.02 . 1 . . . . . . . . 4465 1 75 . 1 1 26 26 CYS N N 15 122.7 0.2 . 1 . . . . . . . . 4465 1 76 . 1 1 27 27 LYS H H 1 8.70 0.02 . 1 . . . . . . . . 4465 1 77 . 1 1 27 27 LYS HA H 1 4.26 0.02 . 1 . . . . . . . . 4465 1 78 . 1 1 27 27 LYS N N 15 122.6 0.2 . 1 . . . . . . . . 4465 1 79 . 1 1 28 28 GLN H H 1 7.78 0.02 . 1 . . . . . . . . 4465 1 80 . 1 1 28 28 GLN HA H 1 4.99 0.02 . 1 . . . . . . . . 4465 1 81 . 1 1 28 28 GLN N N 15 116.3 0.2 . 1 . . . . . . . . 4465 1 82 . 1 1 29 29 PHE H H 1 8.40 0.02 . 1 . . . . . . . . 4465 1 83 . 1 1 29 29 PHE HA H 1 4.88 0.02 . 1 . . . . . . . . 4465 1 84 . 1 1 29 29 PHE N N 15 121.8 0.2 . 1 . . . . . . . . 4465 1 85 . 1 1 30 30 THR H H 1 7.06 0.02 . 1 . . . . . . . . 4465 1 86 . 1 1 30 30 THR HA H 1 5.07 0.02 . 1 . . . . . . . . 4465 1 87 . 1 1 30 30 THR N N 15 122.8 0.2 . 1 . . . . . . . . 4465 1 88 . 1 1 31 31 VAL H H 1 8.62 0.02 . 1 . . . . . . . . 4465 1 89 . 1 1 31 31 VAL HA H 1 3.86 0.02 . 1 . . . . . . . . 4465 1 90 . 1 1 31 31 VAL N N 15 125.8 0.2 . 1 . . . . . . . . 4465 1 91 . 1 1 32 32 ASN H H 1 8.37 0.02 . 1 . . . . . . . . 4465 1 92 . 1 1 32 32 ASN HA H 1 5.00 0.02 . 1 . . . . . . . . 4465 1 93 . 1 1 32 32 ASN N N 15 125.0 0.2 . 1 . . . . . . . . 4465 1 94 . 1 1 33 33 LEU H H 1 9.12 0.02 . 1 . . . . . . . . 4465 1 95 . 1 1 33 33 LEU HA H 1 5.38 0.02 . 1 . . . . . . . . 4465 1 96 . 1 1 33 33 LEU N N 15 128.2 0.2 . 1 . . . . . . . . 4465 1 97 . 1 1 34 34 SER H H 1 8.66 0.02 . 1 . . . . . . . . 4465 1 98 . 1 1 34 34 SER HA H 1 5.08 0.02 . 1 . . . . . . . . 4465 1 99 . 1 1 34 34 SER N N 15 119.3 0.2 . 1 . . . . . . . . 4465 1 100 . 1 1 35 35 HIS H H 1 8.62 0.02 . 1 . . . . . . . . 4465 1 101 . 1 1 35 35 HIS HA H 1 6.43 0.02 . 1 . . . . . . . . 4465 1 102 . 1 1 35 35 HIS N N 15 118.6 0.2 . 1 . . . . . . . . 4465 1 103 . 1 1 37 37 GLY H H 1 8.62 0.02 . 1 . . . . . . . . 4465 1 104 . 1 1 37 37 GLY N N 15 110.7 0.2 . 1 . . . . . . . . 4465 1 105 . 1 1 38 38 ASN H H 1 11.46 0.02 . 1 . . . . . . . . 4465 1 106 . 1 1 38 38 ASN HA H 1 4.97 0.02 . 1 . . . . . . . . 4465 1 107 . 1 1 38 38 ASN N N 15 119.9 0.2 . 1 . . . . . . . . 4465 1 108 . 1 1 39 39 LEU H H 1 8.60 0.02 . 1 . . . . . . . . 4465 1 109 . 1 1 39 39 LEU N N 15 123.4 0.2 . 1 . . . . . . . . 4465 1 110 . 1 1 41 41 LYS H H 1 8.93 0.02 . 1 . . . . . . . . 4465 1 111 . 1 1 41 41 LYS HA H 1 3.46 0.02 . 1 . . . . . . . . 4465 1 112 . 1 1 41 41 LYS N N 15 119.2 0.2 . 1 . . . . . . . . 4465 1 113 . 1 1 42 42 ASN H H 1 8.11 0.02 . 1 . . . . . . . . 4465 1 114 . 1 1 42 42 ASN HA H 1 4.69 0.02 . 1 . . . . . . . . 4465 1 115 . 1 1 42 42 ASN N N 15 108.6 0.2 . 1 . . . . . . . . 4465 1 116 . 1 1 43 43 VAL H H 1 7.31 0.02 . 1 . . . . . . . . 4465 1 117 . 1 1 43 43 VAL HA H 1 4.25 0.02 . 1 . . . . . . . . 4465 1 118 . 1 1 43 43 VAL N N 15 118.9 0.2 . 1 . . . . . . . . 4465 1 119 . 1 1 44 44 MET H H 1 7.82 0.02 . 1 . . . . . . . . 4465 1 120 . 1 1 44 44 MET HA H 1 3.72 0.02 . 1 . . . . . . . . 4465 1 121 . 1 1 44 44 MET N N 15 118.9 0.2 . 1 . . . . . . . . 4465 1 122 . 1 1 45 45 GLY H H 1 5.05 0.02 . 1 . . . . . . . . 4465 1 123 . 1 1 45 45 GLY HA2 H 1 4.14 0.02 . 1 . . . . . . . . 4465 1 124 . 1 1 45 45 GLY HA3 H 1 2.94 0.02 . 1 . . . . . . . . 4465 1 125 . 1 1 45 45 GLY N N 15 114.7 0.2 . 1 . . . . . . . . 4465 1 126 . 1 1 46 46 HIS H H 1 8.21 0.02 . 1 . . . . . . . . 4465 1 127 . 1 1 46 46 HIS HA H 1 6.72 0.02 . 1 . . . . . . . . 4465 1 128 . 1 1 46 46 HIS N N 15 110.5 0.2 . 1 . . . . . . . . 4465 1 129 . 1 1 47 47 ASN H H 1 9.48 0.02 . 1 . . . . . . . . 4465 1 130 . 1 1 47 47 ASN HA H 1 4.71 0.02 . 1 . . . . . . . . 4465 1 131 . 1 1 47 47 ASN N N 15 122.4 0.2 . 1 . . . . . . . . 4465 1 132 . 1 1 48 48 TRP H H 1 7.47 0.02 . 1 . . . . . . . . 4465 1 133 . 1 1 48 48 TRP N N 15 114.6 0.2 . 1 . . . . . . . . 4465 1 134 . 1 1 49 49 VAL H H 1 8.24 0.02 . 1 . . . . . . . . 4465 1 135 . 1 1 49 49 VAL HA H 1 4.00 0.02 . 1 . . . . . . . . 4465 1 136 . 1 1 49 49 VAL N N 15 129.2 0.2 . 1 . . . . . . . . 4465 1 137 . 1 1 50 50 LEU H H 1 7.57 0.02 . 1 . . . . . . . . 4465 1 138 . 1 1 50 50 LEU HA H 1 4.87 0.02 . 1 . . . . . . . . 4465 1 139 . 1 1 50 50 LEU N N 15 124.2 0.2 . 1 . . . . . . . . 4465 1 140 . 1 1 51 51 SER H H 1 9.13 0.02 . 1 . . . . . . . . 4465 1 141 . 1 1 51 51 SER HA H 1 5.03 0.02 . 1 . . . . . . . . 4465 1 142 . 1 1 51 51 SER N N 15 122.3 0.2 . 1 . . . . . . . . 4465 1 143 . 1 1 52 52 THR H H 1 9.84 0.02 . 1 . . . . . . . . 4465 1 144 . 1 1 52 52 THR HA H 1 4.79 0.02 . 1 . . . . . . . . 4465 1 145 . 1 1 52 52 THR N N 15 111.5 0.2 . 1 . . . . . . . . 4465 1 146 . 1 1 53 53 ALA H H 1 8.91 0.02 . 1 . . . . . . . . 4465 1 147 . 1 1 53 53 ALA HA H 1 3.89 0.02 . 1 . . . . . . . . 4465 1 148 . 1 1 53 53 ALA N N 15 125.7 0.2 . 1 . . . . . . . . 4465 1 149 . 1 1 54 54 ALA H H 1 8.27 0.02 . 1 . . . . . . . . 4465 1 150 . 1 1 54 54 ALA HA H 1 4.09 0.02 . 1 . . . . . . . . 4465 1 151 . 1 1 54 54 ALA N N 15 118.4 0.2 . 1 . . . . . . . . 4465 1 152 . 1 1 55 55 ASP H H 1 7.31 0.02 . 1 . . . . . . . . 4465 1 153 . 1 1 55 55 ASP HA H 1 4.74 0.02 . 1 . . . . . . . . 4465 1 154 . 1 1 55 55 ASP N N 15 115.9 0.2 . 1 . . . . . . . . 4465 1 155 . 1 1 56 56 MET H H 1 7.01 0.02 . 1 . . . . . . . . 4465 1 156 . 1 1 56 56 MET HA H 1 3.55 0.02 . 1 . . . . . . . . 4465 1 157 . 1 1 56 56 MET N N 15 120.1 0.2 . 1 . . . . . . . . 4465 1 158 . 1 1 57 57 GLN H H 1 8.56 0.02 . 1 . . . . . . . . 4465 1 159 . 1 1 57 57 GLN HA H 1 3.72 0.02 . 1 . . . . . . . . 4465 1 160 . 1 1 57 57 GLN N N 15 115.9 0.2 . 1 . . . . . . . . 4465 1 161 . 1 1 58 58 GLY H H 1 8.37 0.02 . 1 . . . . . . . . 4465 1 162 . 1 1 58 58 GLY HA2 H 1 3.80 0.02 . 1 . . . . . . . . 4465 1 163 . 1 1 58 58 GLY HA3 H 1 3.76 0.02 . 1 . . . . . . . . 4465 1 164 . 1 1 58 58 GLY N N 15 109.5 0.2 . 1 . . . . . . . . 4465 1 165 . 1 1 59 59 VAL H H 1 7.87 0.02 . 1 . . . . . . . . 4465 1 166 . 1 1 59 59 VAL HA H 1 3.61 0.02 . 1 . . . . . . . . 4465 1 167 . 1 1 59 59 VAL N N 15 122.0 0.2 . 1 . . . . . . . . 4465 1 168 . 1 1 60 60 VAL H H 1 8.43 0.02 . 1 . . . . . . . . 4465 1 169 . 1 1 60 60 VAL HA H 1 3.59 0.02 . 1 . . . . . . . . 4465 1 170 . 1 1 60 60 VAL N N 15 120.0 0.2 . 1 . . . . . . . . 4465 1 171 . 1 1 61 61 THR H H 1 8.48 0.02 . 1 . . . . . . . . 4465 1 172 . 1 1 61 61 THR HA H 1 3.89 0.02 . 1 . . . . . . . . 4465 1 173 . 1 1 61 61 THR N N 15 117.1 0.2 . 1 . . . . . . . . 4465 1 174 . 1 1 62 62 ASP H H 1 8.42 0.02 . 1 . . . . . . . . 4465 1 175 . 1 1 62 62 ASP N N 15 121.6 0.2 . 1 . . . . . . . . 4465 1 176 . 1 1 63 63 GLY H H 1 8.69 0.02 . 1 . . . . . . . . 4465 1 177 . 1 1 63 63 GLY HA2 H 1 4.13 0.02 . 1 . . . . . . . . 4465 1 178 . 1 1 63 63 GLY HA3 H 1 3.55 0.02 . 1 . . . . . . . . 4465 1 179 . 1 1 63 63 GLY N N 15 113.7 0.2 . 1 . . . . . . . . 4465 1 180 . 1 1 64 64 MET H H 1 8.50 0.02 . 1 . . . . . . . . 4465 1 181 . 1 1 64 64 MET HA H 1 4.15 0.02 . 1 . . . . . . . . 4465 1 182 . 1 1 64 64 MET N N 15 121.9 0.2 . 1 . . . . . . . . 4465 1 183 . 1 1 65 65 ALA H H 1 7.10 0.02 . 1 . . . . . . . . 4465 1 184 . 1 1 65 65 ALA HA H 1 4.24 0.02 . 1 . . . . . . . . 4465 1 185 . 1 1 65 65 ALA N N 15 117.5 0.2 . 1 . . . . . . . . 4465 1 186 . 1 1 66 66 SER H H 1 7.71 0.02 . 1 . . . . . . . . 4465 1 187 . 1 1 66 66 SER HA H 1 4.28 0.02 . 1 . . . . . . . . 4465 1 188 . 1 1 66 66 SER N N 15 114.9 0.2 . 1 . . . . . . . . 4465 1 189 . 1 1 67 67 GLY H H 1 6.76 0.02 . 1 . . . . . . . . 4465 1 190 . 1 1 67 67 GLY HA2 H 1 4.20 0.02 . 1 . . . . . . . . 4465 1 191 . 1 1 67 67 GLY HA3 H 1 3.59 0.02 . 1 . . . . . . . . 4465 1 192 . 1 1 67 67 GLY N N 15 102.7 0.2 . 1 . . . . . . . . 4465 1 193 . 1 1 68 68 LEU H H 1 7.98 0.02 . 1 . . . . . . . . 4465 1 194 . 1 1 68 68 LEU HA H 1 3.00 0.02 . 1 . . . . . . . . 4465 1 195 . 1 1 68 68 LEU N N 15 122.1 0.2 . 1 . . . . . . . . 4465 1 196 . 1 1 69 69 ASP H H 1 8.54 0.02 . 1 . . . . . . . . 4465 1 197 . 1 1 69 69 ASP HA H 1 4.35 0.02 . 1 . . . . . . . . 4465 1 198 . 1 1 69 69 ASP N N 15 116.8 0.2 . 1 . . . . . . . . 4465 1 199 . 1 1 70 70 LYS H H 1 6.89 0.02 . 1 . . . . . . . . 4465 1 200 . 1 1 70 70 LYS HA H 1 4.50 0.02 . 1 . . . . . . . . 4465 1 201 . 1 1 70 70 LYS N N 15 118.7 0.2 . 1 . . . . . . . . 4465 1 202 . 1 1 71 71 ASP H H 1 8.02 0.02 . 1 . . . . . . . . 4465 1 203 . 1 1 71 71 ASP HA H 1 3.99 0.02 . 1 . . . . . . . . 4465 1 204 . 1 1 71 71 ASP N N 15 115.5 0.2 . 1 . . . . . . . . 4465 1 205 . 1 1 72 72 TYR H H 1 7.70 0.02 . 1 . . . . . . . . 4465 1 206 . 1 1 72 72 TYR HA H 1 3.65 0.02 . 1 . . . . . . . . 4465 1 207 . 1 1 72 72 TYR N N 15 105.4 0.2 . 1 . . . . . . . . 4465 1 208 . 1 1 73 73 LEU H H 1 7.10 0.02 . 1 . . . . . . . . 4465 1 209 . 1 1 73 73 LEU N N 15 117.4 0.2 . 1 . . . . . . . . 4465 1 210 . 1 1 74 74 LYS H H 1 8.85 0.02 . 1 . . . . . . . . 4465 1 211 . 1 1 74 74 LYS HA H 1 4.69 0.02 . 1 . . . . . . . . 4465 1 212 . 1 1 74 74 LYS N N 15 126.8 0.2 . 1 . . . . . . . . 4465 1 213 . 1 1 75 75 PRO HA H 1 4.22 0.02 . 1 . . . . . . . . 4465 1 214 . 1 1 76 76 ASP H H 1 8.68 0.02 . 1 . . . . . . . . 4465 1 215 . 1 1 76 76 ASP HA H 1 4.28 0.02 . 1 . . . . . . . . 4465 1 216 . 1 1 76 76 ASP N N 15 118.5 0.2 . 1 . . . . . . . . 4465 1 217 . 1 1 77 77 ASP H H 1 7.30 0.02 . 1 . . . . . . . . 4465 1 218 . 1 1 77 77 ASP HA H 1 4.29 0.02 . 1 . . . . . . . . 4465 1 219 . 1 1 77 77 ASP N N 15 117.5 0.2 . 1 . . . . . . . . 4465 1 220 . 1 1 78 78 SER H H 1 8.59 0.02 . 1 . . . . . . . . 4465 1 221 . 1 1 78 78 SER HA H 1 4.28 0.02 . 1 . . . . . . . . 4465 1 222 . 1 1 78 78 SER N N 15 124.9 0.2 . 1 . . . . . . . . 4465 1 223 . 1 1 79 79 ARG H H 1 8.56 0.02 . 1 . . . . . . . . 4465 1 224 . 1 1 79 79 ARG HA H 1 4.16 0.02 . 1 . . . . . . . . 4465 1 225 . 1 1 79 79 ARG N N 15 119.8 0.2 . 1 . . . . . . . . 4465 1 226 . 1 1 80 80 VAL H H 1 7.33 0.02 . 1 . . . . . . . . 4465 1 227 . 1 1 80 80 VAL HA H 1 3.90 0.02 . 1 . . . . . . . . 4465 1 228 . 1 1 80 80 VAL N N 15 118.3 0.2 . 1 . . . . . . . . 4465 1 229 . 1 1 81 81 ILE H H 1 8.88 0.02 . 1 . . . . . . . . 4465 1 230 . 1 1 81 81 ILE HA H 1 3.72 0.02 . 1 . . . . . . . . 4465 1 231 . 1 1 81 81 ILE N N 15 131.7 0.2 . 1 . . . . . . . . 4465 1 232 . 1 1 82 82 ALA H H 1 7.19 0.02 . 1 . . . . . . . . 4465 1 233 . 1 1 82 82 ALA HA H 1 4.69 0.02 . 1 . . . . . . . . 4465 1 234 . 1 1 82 82 ALA N N 15 116.5 0.2 . 1 . . . . . . . . 4465 1 235 . 1 1 83 83 HIS H H 1 8.59 0.02 . 1 . . . . . . . . 4465 1 236 . 1 1 83 83 HIS HA H 1 6.15 0.02 . 1 . . . . . . . . 4465 1 237 . 1 1 83 83 HIS N N 15 113.1 0.2 . 1 . . . . . . . . 4465 1 238 . 1 1 84 84 THR H H 1 8.79 0.02 . 1 . . . . . . . . 4465 1 239 . 1 1 84 84 THR HA H 1 4.80 0.02 . 1 . . . . . . . . 4465 1 240 . 1 1 84 84 THR N N 15 110.1 0.2 . 1 . . . . . . . . 4465 1 241 . 1 1 85 85 LYS H H 1 9.32 0.02 . 1 . . . . . . . . 4465 1 242 . 1 1 85 85 LYS HA H 1 4.69 0.02 . 1 . . . . . . . . 4465 1 243 . 1 1 85 85 LYS N N 15 121.5 0.2 . 1 . . . . . . . . 4465 1 244 . 1 1 86 86 LEU H H 1 8.05 0.02 . 1 . . . . . . . . 4465 1 245 . 1 1 86 86 LEU HA H 1 4.70 0.02 . 1 . . . . . . . . 4465 1 246 . 1 1 86 86 LEU N N 15 120.6 0.2 . 1 . . . . . . . . 4465 1 247 . 1 1 87 87 ILE H H 1 9.43 0.02 . 1 . . . . . . . . 4465 1 248 . 1 1 87 87 ILE HA H 1 4.88 0.02 . 1 . . . . . . . . 4465 1 249 . 1 1 87 87 ILE N N 15 120.8 0.2 . 1 . . . . . . . . 4465 1 250 . 1 1 88 88 GLY H H 1 9.31 0.02 . 1 . . . . . . . . 4465 1 251 . 1 1 88 88 GLY HA2 H 1 4.12 0.02 . 1 . . . . . . . . 4465 1 252 . 1 1 88 88 GLY HA3 H 1 3.57 0.02 . 1 . . . . . . . . 4465 1 253 . 1 1 88 88 GLY N N 15 110.9 0.2 . 1 . . . . . . . . 4465 1 254 . 1 1 89 89 SER H H 1 6.87 0.02 . 1 . . . . . . . . 4465 1 255 . 1 1 89 89 SER N N 15 111.3 0.2 . 1 . . . . . . . . 4465 1 256 . 1 1 90 90 GLY H H 1 8.39 0.02 . 1 . . . . . . . . 4465 1 257 . 1 1 90 90 GLY N N 15 111.4 0.2 . 1 . . . . . . . . 4465 1 258 . 1 1 91 91 GLU H H 1 7.64 0.02 . 1 . . . . . . . . 4465 1 259 . 1 1 91 91 GLU N N 15 119.0 0.2 . 1 . . . . . . . . 4465 1 260 . 1 1 92 92 LYS H H 1 8.19 0.02 . 1 . . . . . . . . 4465 1 261 . 1 1 92 92 LYS HA H 1 5.22 0.02 . 1 . . . . . . . . 4465 1 262 . 1 1 92 92 LYS N N 15 117.0 0.2 . 1 . . . . . . . . 4465 1 263 . 1 1 93 93 ASP H H 1 8.96 0.02 . 1 . . . . . . . . 4465 1 264 . 1 1 93 93 ASP HA H 1 5.10 0.02 . 1 . . . . . . . . 4465 1 265 . 1 1 93 93 ASP N N 15 118.0 0.2 . 1 . . . . . . . . 4465 1 266 . 1 1 94 94 SER H H 1 8.03 0.02 . 1 . . . . . . . . 4465 1 267 . 1 1 94 94 SER HA H 1 5.70 0.02 . 1 . . . . . . . . 4465 1 268 . 1 1 94 94 SER N N 15 116.2 0.2 . 1 . . . . . . . . 4465 1 269 . 1 1 95 95 VAL H H 1 8.65 0.02 . 1 . . . . . . . . 4465 1 270 . 1 1 95 95 VAL HA H 1 4.69 0.02 . 1 . . . . . . . . 4465 1 271 . 1 1 95 95 VAL N N 15 121.8 0.2 . 1 . . . . . . . . 4465 1 272 . 1 1 96 96 THR H H 1 8.40 0.02 . 1 . . . . . . . . 4465 1 273 . 1 1 96 96 THR HA H 1 5.37 0.02 . 1 . . . . . . . . 4465 1 274 . 1 1 96 96 THR N N 15 124.7 0.2 . 1 . . . . . . . . 4465 1 275 . 1 1 97 97 PHE H H 1 8.78 0.02 . 1 . . . . . . . . 4465 1 276 . 1 1 97 97 PHE HA H 1 5.28 0.02 . 1 . . . . . . . . 4465 1 277 . 1 1 97 97 PHE N N 15 122.5 0.2 . 1 . . . . . . . . 4465 1 278 . 1 1 98 98 ASP H H 1 8.54 0.02 . 1 . . . . . . . . 4465 1 279 . 1 1 98 98 ASP HA H 1 4.74 0.02 . 1 . . . . . . . . 4465 1 280 . 1 1 98 98 ASP N N 15 120.6 0.2 . 1 . . . . . . . . 4465 1 281 . 1 1 99 99 VAL H H 1 7.88 0.02 . 1 . . . . . . . . 4465 1 282 . 1 1 99 99 VAL HA H 1 3.46 0.02 . 1 . . . . . . . . 4465 1 283 . 1 1 99 99 VAL N N 15 127.2 0.2 . 1 . . . . . . . . 4465 1 284 . 1 1 100 100 SER H H 1 8.61 0.02 . 1 . . . . . . . . 4465 1 285 . 1 1 100 100 SER HA H 1 4.36 0.02 . 1 . . . . . . . . 4465 1 286 . 1 1 100 100 SER N N 15 115.4 0.2 . 1 . . . . . . . . 4465 1 287 . 1 1 101 101 LYS H H 1 7.46 0.02 . 1 . . . . . . . . 4465 1 288 . 1 1 101 101 LYS HA H 1 4.20 0.02 . 1 . . . . . . . . 4465 1 289 . 1 1 101 101 LYS N N 15 119.7 0.2 . 1 . . . . . . . . 4465 1 290 . 1 1 102 102 LEU H H 1 7.91 0.02 . 1 . . . . . . . . 4465 1 291 . 1 1 102 102 LEU HA H 1 4.46 0.02 . 1 . . . . . . . . 4465 1 292 . 1 1 102 102 LEU N N 15 118.4 0.2 . 1 . . . . . . . . 4465 1 293 . 1 1 103 103 LYS H H 1 8.72 0.02 . 1 . . . . . . . . 4465 1 294 . 1 1 103 103 LYS HA H 1 4.68 0.02 . 1 . . . . . . . . 4465 1 295 . 1 1 103 103 LYS N N 15 120.7 0.2 . 1 . . . . . . . . 4465 1 296 . 1 1 104 104 GLU H H 1 8.83 0.02 . 1 . . . . . . . . 4465 1 297 . 1 1 104 104 GLU HA H 1 4.16 0.02 . 1 . . . . . . . . 4465 1 298 . 1 1 104 104 GLU N N 15 124.7 0.2 . 1 . . . . . . . . 4465 1 299 . 1 1 105 105 GLY H H 1 8.90 0.02 . 1 . . . . . . . . 4465 1 300 . 1 1 105 105 GLY HA2 H 1 4.24 0.02 . 1 . . . . . . . . 4465 1 301 . 1 1 105 105 GLY HA3 H 1 3.80 0.02 . 1 . . . . . . . . 4465 1 302 . 1 1 105 105 GLY N N 15 112.4 0.2 . 1 . . . . . . . . 4465 1 303 . 1 1 106 106 GLU H H 1 7.20 0.02 . 1 . . . . . . . . 4465 1 304 . 1 1 106 106 GLU HA H 1 4.48 0.02 . 1 . . . . . . . . 4465 1 305 . 1 1 106 106 GLU N N 15 120.5 0.2 . 1 . . . . . . . . 4465 1 306 . 1 1 107 107 GLN H H 1 9.16 0.02 . 1 . . . . . . . . 4465 1 307 . 1 1 107 107 GLN HA H 1 4.66 0.02 . 1 . . . . . . . . 4465 1 308 . 1 1 107 107 GLN N N 15 124.5 0.2 . 1 . . . . . . . . 4465 1 309 . 1 1 108 108 TYR H H 1 8.63 0.02 . 1 . . . . . . . . 4465 1 310 . 1 1 108 108 TYR HA H 1 4.91 0.02 . 1 . . . . . . . . 4465 1 311 . 1 1 108 108 TYR N N 15 123.9 0.2 . 1 . . . . . . . . 4465 1 312 . 1 1 109 109 MET H H 1 8.99 0.02 . 1 . . . . . . . . 4465 1 313 . 1 1 109 109 MET HA H 1 5.53 0.02 . 1 . . . . . . . . 4465 1 314 . 1 1 109 109 MET N N 15 120.3 0.2 . 1 . . . . . . . . 4465 1 315 . 1 1 110 110 PHE H H 1 8.48 0.02 . 1 . . . . . . . . 4465 1 316 . 1 1 110 110 PHE HA H 1 6.00 0.02 . 1 . . . . . . . . 4465 1 317 . 1 1 110 110 PHE N N 15 117.2 0.2 . 1 . . . . . . . . 4465 1 318 . 1 1 111 111 PHE H H 1 8.11 0.02 . 1 . . . . . . . . 4465 1 319 . 1 1 111 111 PHE HA H 1 5.47 0.02 . 1 . . . . . . . . 4465 1 320 . 1 1 111 111 PHE N N 15 115.4 0.2 . 1 . . . . . . . . 4465 1 321 . 1 1 112 112 CYS H H 1 7.24 0.02 . 1 . . . . . . . . 4465 1 322 . 1 1 112 112 CYS HA H 1 5.64 0.02 . 1 . . . . . . . . 4465 1 323 . 1 1 112 112 CYS N N 15 121.3 0.2 . 1 . . . . . . . . 4465 1 324 . 1 1 113 113 THR H H 1 9.91 0.02 . 1 . . . . . . . . 4465 1 325 . 1 1 113 113 THR N N 15 118.0 0.2 . 1 . . . . . . . . 4465 1 326 . 1 1 114 114 PHE H H 1 9.49 0.02 . 1 . . . . . . . . 4465 1 327 . 1 1 114 114 PHE HA H 1 3.70 0.02 . 1 . . . . . . . . 4465 1 328 . 1 1 114 114 PHE N N 15 128.8 0.2 . 1 . . . . . . . . 4465 1 329 . 1 1 116 116 GLY H H 1 8.81 0.02 . 1 . . . . . . . . 4465 1 330 . 1 1 116 116 GLY HA2 H 1 4.12 0.02 . 1 . . . . . . . . 4465 1 331 . 1 1 116 116 GLY N N 15 109.8 0.2 . 1 . . . . . . . . 4465 1 332 . 1 1 117 117 GLY H H 1 8.12 0.02 . 1 . . . . . . . . 4465 1 333 . 1 1 117 117 GLY HA2 H 1 4.21 0.02 . 1 . . . . . . . . 4465 1 334 . 1 1 117 117 GLY HA3 H 1 3.86 0.02 . 1 . . . . . . . . 4465 1 335 . 1 1 117 117 GLY N N 15 111.6 0.2 . 1 . . . . . . . . 4465 1 336 . 1 1 118 118 SER H H 1 8.40 0.02 . 1 . . . . . . . . 4465 1 337 . 1 1 118 118 SER HA H 1 4.32 0.02 . 1 . . . . . . . . 4465 1 338 . 1 1 118 118 SER N N 15 115.9 0.2 . 1 . . . . . . . . 4465 1 339 . 1 1 119 119 ALA H H 1 7.64 0.02 . 1 . . . . . . . . 4465 1 340 . 1 1 119 119 ALA HA H 1 4.26 0.02 . 1 . . . . . . . . 4465 1 341 . 1 1 119 119 ALA N N 15 122.3 0.2 . 1 . . . . . . . . 4465 1 342 . 1 1 120 120 LEU H H 1 7.66 0.02 . 1 . . . . . . . . 4465 1 343 . 1 1 120 120 LEU N N 15 116.9 0.2 . 1 . . . . . . . . 4465 1 344 . 1 1 121 121 MET H H 1 8.94 0.02 . 1 . . . . . . . . 4465 1 345 . 1 1 121 121 MET HA H 1 4.44 0.02 . 1 . . . . . . . . 4465 1 346 . 1 1 121 121 MET N N 15 123.8 0.2 . 1 . . . . . . . . 4465 1 347 . 1 1 122 122 LYS H H 1 7.52 0.02 . 1 . . . . . . . . 4465 1 348 . 1 1 122 122 LYS HA H 1 5.58 0.02 . 1 . . . . . . . . 4465 1 349 . 1 1 122 122 LYS N N 15 117.1 0.2 . 1 . . . . . . . . 4465 1 350 . 1 1 123 123 GLY H H 1 8.38 0.02 . 1 . . . . . . . . 4465 1 351 . 1 1 123 123 GLY HA2 H 1 4.13 0.02 . 1 . . . . . . . . 4465 1 352 . 1 1 123 123 GLY HA3 H 1 3.08 0.02 . 1 . . . . . . . . 4465 1 353 . 1 1 123 123 GLY N N 15 109.7 0.2 . 1 . . . . . . . . 4465 1 354 . 1 1 124 124 THR H H 1 7.86 0.02 . 1 . . . . . . . . 4465 1 355 . 1 1 124 124 THR HA H 1 5.15 0.02 . 1 . . . . . . . . 4465 1 356 . 1 1 124 124 THR N N 15 109.6 0.2 . 1 . . . . . . . . 4465 1 357 . 1 1 125 125 LEU H H 1 8.07 0.02 . 1 . . . . . . . . 4465 1 358 . 1 1 125 125 LEU HA H 1 5.68 0.02 . 1 . . . . . . . . 4465 1 359 . 1 1 125 125 LEU N N 15 125.3 0.2 . 1 . . . . . . . . 4465 1 360 . 1 1 126 126 THR H H 1 8.44 0.02 . 1 . . . . . . . . 4465 1 361 . 1 1 126 126 THR HA H 1 4.87 0.02 . 1 . . . . . . . . 4465 1 362 . 1 1 126 126 THR N N 15 120.2 0.2 . 1 . . . . . . . . 4465 1 363 . 1 1 127 127 LEU H H 1 8.76 0.02 . 1 . . . . . . . . 4465 1 364 . 1 1 127 127 LEU HA H 1 5.15 0.02 . 1 . . . . . . . . 4465 1 365 . 1 1 127 127 LEU N N 15 127.2 0.2 . 1 . . . . . . . . 4465 1 366 . 1 1 128 128 LYS H H 1 8.55 0.02 . 1 . . . . . . . . 4465 1 367 . 1 1 128 128 LYS HA H 1 4.33 0.02 . 1 . . . . . . . . 4465 1 368 . 1 1 128 128 LYS N N 15 130.2 0.2 . 1 . . . . . . . . 4465 1 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