data_16740 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 16740 _Entry.Title ; Amide assignments for Paracoccus denitrificans amicyanin-ZnII. ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2010-02-21 _Entry.Accession_date 2010-02-21 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.9.13 _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 Marcellus Ubbink . . . 16740 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 16740 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 96 16740 '1H chemical shifts' 98 16740 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 2 . . 2010-10-14 2010-02-21 update BMRB 'update entry citation' 16740 1 . . 2010-10-05 2010-02-21 original author 'original release' 16740 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 16741 'Backbone assignments for Paracoccus denitrificans amicyanin-CuI.' 16740 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 16740 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 20873742 _Citation.Full_citation . _Citation.Title 'Amicyanin Transfers Electrons from Methylamine Dehydrogenase to Cytochrome c-551i via a Ping-Pong Mechanism, not a Ternary Complex.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Am. Chem. Soc.' _Citation.Journal_name_full 'Journal of the American Chemical Society' _Citation.Journal_volume 132 _Citation.Journal_issue 41 _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 14537 _Citation.Page_last 14545 _Citation.Year 2010 _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 Francesca Meschi . . . 16740 1 2 Frank Wiertz . . . 16740 1 3 Linda Klauss . . . 16740 1 4 Chiara Cavalieri . . . 16740 1 5 Anneloes Blok . . . 16740 1 6 Bernd Ludwig . . . 16740 1 7 Hendrik Heering . A. . 16740 1 8 Angelo Merli . . . 16740 1 9 'Gian Luigi' Rossi . . . 16740 1 10 Marcellus Ubbink . . . 16740 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'electron transfer' 16740 1 kinetics 16740 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 16740 _Assembly.ID 1 _Assembly.Name Zn-amicyanin _Assembly.BMRB_code . _Assembly.Number_of_components 2 _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 polypeptide 1 $amicyanin A . yes metal-substituted no no . . . 16740 1 2 'zinc(II) ion' 2 $ZN A . no metal-substituted no no . . . 16740 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_amicyanin _Entity.Sf_category entity _Entity.Sf_framecode amicyanin _Entity.Entry_ID 16740 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name amicyanin _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 ; GDKATIPSESPFAAAEVADG AIVVDIAKMKYETPELHVKV GDTVTWINREAMPHNVHFVA GVLGEAALKGPMMKKEQAYS LTFTEAGTYDYHCTPHPFMR GKVVVE ; _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 no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 106 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all other bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 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 16741 . amicyanin . . . . . 100.00 106 100.00 100.00 5.55e-71 . . . . 16740 1 2 no PDB 1AAC . "Amicyanin Oxidized, 1.31 Angstroms" . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 3 no PDB 1AAJ . "Crystal Structure Analysis Of Amicyanin And Apoamicyanin From Paracoccus Denitrificans At 2.0 Angstroms And 1.8 Angstroms Resol" . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 4 no PDB 1AAN . "Crystal Structure Analysis Of Amicyanin And Apoamicyanin From Paracoccus Denitrificans At 2.0 Angstroms And 1.8 Angstroms Resol" . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 5 no PDB 1BXA . "Amicyanin Reduced, Ph 4.4, 1.3 Angstroms" . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 6 no PDB 1MDA . "Crystal Structure Of An Electron-Transfer Complex Between Methylamine Dehydrogenase And Amicyanin" . . . . . 97.17 103 100.00 100.00 1.50e-68 . . . . 16740 1 7 no PDB 1MG2 . "Mutation Of Alpha Phe55 Of Methylamine Dehydrogenase Alters The Reorganization Energy And Electronic Coupling For Its Electron " . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 8 no PDB 1MG3 . "Mutation Of Alpha Phe55 Of Methylamine Dehydrogenase Alters The Reorganization Energy And Electronic Coupling For Its Electron " . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 9 no PDB 1SF3 . "Structure Of The Reduced Form Of The P94a Mutant Of Amicyanin" . . . . . 99.06 105 99.05 99.05 3.92e-69 . . . . 16740 1 10 no PDB 1SF5 . "Structure Of Oxidized State Of The P94a Mutant Of Amicyanin" . . . . . 99.06 105 98.10 98.10 4.13e-68 . . . . 16740 1 11 no PDB 1SFD . "Oxidized Form Of Amicyanin Mutant P94f" . . . . . 99.06 105 99.05 99.05 1.18e-68 . . . . 16740 1 12 no PDB 1SFH . "Reduced State Of Amicyanin Mutant P94f" . . . . . 99.06 105 99.05 99.05 1.18e-68 . . . . 16740 1 13 no PDB 1T5K . "Crystal Structure Of Amicyanin Substituted With Cobalt" . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 14 no PDB 2GB2 . "The P52g Mutant Of Amicyanin In The Cu(Ii) State." . . . . . 99.06 105 99.05 99.05 8.13e-69 . . . . 16740 1 15 no PDB 2GBA . "Reduced Cu(I) Form At Ph 4 Of P52g Mutant Of Amicyanin" . . . . . 99.06 105 99.05 99.05 8.13e-69 . . . . 16740 1 16 no PDB 2GC4 . "Structural Comparison Of The Oxidized Ternary Electron Transfer Complex Of Methylamine Dehydrogenase, Amicyanin And Cytochrome " . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 17 no PDB 2GC7 . "Substrate Reduced, Copper Free Complex Of Methylamine Dehydrogenase, Amicyanin And Cytochrome C551i From Paracoccus Denitrifica" . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 18 no PDB 2IDQ . "Structure Of M98a Mutant Of Amicyanin, Cu(Ii)" . . . . . 99.06 105 99.05 99.05 3.79e-69 . . . . 16740 1 19 no PDB 2IDS . "Structure Of M98a Mutant Of Amicyanin, Cu(I)" . . . . . 99.06 105 99.05 99.05 3.79e-69 . . . . 16740 1 20 no PDB 2IDT . "Structure Of M98q Mutant Of Amicyanin, Cu(Ii)" . . . . . 99.06 105 98.10 98.10 2.01e-68 . . . . 16740 1 21 no PDB 2IDU . "Structure Of M98q Mutant Of Amicyanin, Cu(I)" . . . . . 99.06 105 98.10 98.10 2.01e-68 . . . . 16740 1 22 no PDB 2J55 . "X-ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase O-quinone In Complex With Amicyanin." . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 23 no PDB 2J56 . "X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase N-Semiquinone In Complex With Amicyanin." . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 24 no PDB 2J57 . "X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase N-Quinol In Complex With Amicyanin." . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 25 no PDB 2MTA . "Crystal Structure Of A Ternary Electron Transfer Complex Between Methylamine Dehydrogenase, Amicyanin And A C-Type Cytochrome" . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 26 no PDB 2OV0 . "Structure Of The Blue Copper Protein Amicyanin To 0.75 A Resolution" . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 27 no PDB 2QDV . "Structure Of The Cu(Ii) Form Of The M51a Mutant Of Amicyanin" . . . . . 100.00 106 98.11 98.11 2.58e-67 . . . . 16740 1 28 no PDB 2QDW . "Structure Of Cu(I) Form Of The M51a Mutant Of Amicyanin" . . . . . 100.00 106 98.11 98.11 2.58e-67 . . . . 16740 1 29 no PDB 2RAC . "Amicyanin Reduced, Ph 7.7, 1.3 Angstroms" . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 30 no PDB 3IE9 . "Structure Of Oxidized M98l Mutant Of Amicyanin" . . . . . 99.06 105 99.05 100.00 1.18e-69 . . . . 16740 1 31 no PDB 3IEA . "Structure Of Reduced M98l Mutant Of Amicyanin" . . . . . 99.06 105 99.05 100.00 1.18e-69 . . . . 16740 1 32 no PDB 3L45 . "A Joint Neutron And X-Ray Structure Of Oxidized Amicyanin" . . . . . 99.06 105 100.00 100.00 4.18e-70 . . . . 16740 1 33 no PDB 3PLY . "Structure Of Oxidized P96g Mutant Of Amicyanin" . . . . . 99.06 105 99.05 99.05 8.13e-69 . . . . 16740 1 34 no PDB 3RYM . "Structure Of Oxidized M98k Mutant Of Amicyanin" . . . . . 99.06 105 99.05 99.05 4.37e-69 . . . . 16740 1 35 no PDB 4P5R . "Structure Of Oxidized W45y Mutant Of Amicyanin" . . . . . 99.06 105 99.05 100.00 2.95e-69 . . . . 16740 1 36 no PDB 4P5S . "Structure Of Reduced W45y Mutant Of Amicyanin" . . . . . 99.06 105 99.05 100.00 2.95e-69 . . . . 16740 1 37 no EMBL CAA39199 . "amicyanin [Paracoccus denitrificans]" . . . . . 100.00 131 99.06 99.06 1.13e-70 . . . . 16740 1 38 no GB ABL72795 . "amicyanin [Paracoccus denitrificans PD1222]" . . . . . 100.00 131 99.06 99.06 1.13e-70 . . . . 16740 1 39 no PRF 1702223A . amicyanin . . . . . 100.00 131 99.06 99.06 1.13e-70 . . . . 16740 1 40 no REF WP_041530795 . "amicyanin [Paracoccus denitrificans]" . . . . . 99.06 125 100.00 100.00 1.92e-70 . . . . 16740 1 41 no SP P22364 . "RecName: Full=Amicyanin; Flags: Precursor" . . . . . 100.00 131 99.06 99.06 1.13e-70 . . . . 16740 1 stop_ loop_ _Entity_biological_function.Biological_function _Entity_biological_function.Entry_ID _Entity_biological_function.Entity_ID 'Electron transfer' 16740 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 0 GLY . 16740 1 2 1 ASP . 16740 1 3 2 LYS . 16740 1 4 3 ALA . 16740 1 5 4 THR . 16740 1 6 5 ILE . 16740 1 7 6 PRO . 16740 1 8 7 SER . 16740 1 9 8 GLU . 16740 1 10 9 SER . 16740 1 11 10 PRO . 16740 1 12 11 PHE . 16740 1 13 12 ALA . 16740 1 14 13 ALA . 16740 1 15 14 ALA . 16740 1 16 15 GLU . 16740 1 17 16 VAL . 16740 1 18 17 ALA . 16740 1 19 18 ASP . 16740 1 20 19 GLY . 16740 1 21 20 ALA . 16740 1 22 21 ILE . 16740 1 23 22 VAL . 16740 1 24 23 VAL . 16740 1 25 24 ASP . 16740 1 26 25 ILE . 16740 1 27 26 ALA . 16740 1 28 27 LYS . 16740 1 29 28 MET . 16740 1 30 29 LYS . 16740 1 31 30 TYR . 16740 1 32 31 GLU . 16740 1 33 32 THR . 16740 1 34 33 PRO . 16740 1 35 34 GLU . 16740 1 36 35 LEU . 16740 1 37 36 HIS . 16740 1 38 37 VAL . 16740 1 39 38 LYS . 16740 1 40 39 VAL . 16740 1 41 40 GLY . 16740 1 42 41 ASP . 16740 1 43 42 THR . 16740 1 44 43 VAL . 16740 1 45 44 THR . 16740 1 46 45 TRP . 16740 1 47 46 ILE . 16740 1 48 47 ASN . 16740 1 49 48 ARG . 16740 1 50 49 GLU . 16740 1 51 50 ALA . 16740 1 52 51 MET . 16740 1 53 52 PRO . 16740 1 54 53 HIS . 16740 1 55 54 ASN . 16740 1 56 55 VAL . 16740 1 57 56 HIS . 16740 1 58 57 PHE . 16740 1 59 58 VAL . 16740 1 60 59 ALA . 16740 1 61 60 GLY . 16740 1 62 61 VAL . 16740 1 63 62 LEU . 16740 1 64 63 GLY . 16740 1 65 64 GLU . 16740 1 66 65 ALA . 16740 1 67 66 ALA . 16740 1 68 67 LEU . 16740 1 69 68 LYS . 16740 1 70 69 GLY . 16740 1 71 70 PRO . 16740 1 72 71 MET . 16740 1 73 72 MET . 16740 1 74 73 LYS . 16740 1 75 74 LYS . 16740 1 76 75 GLU . 16740 1 77 76 GLN . 16740 1 78 77 ALA . 16740 1 79 78 TYR . 16740 1 80 79 SER . 16740 1 81 80 LEU . 16740 1 82 81 THR . 16740 1 83 82 PHE . 16740 1 84 83 THR . 16740 1 85 84 GLU . 16740 1 86 85 ALA . 16740 1 87 86 GLY . 16740 1 88 87 THR . 16740 1 89 88 TYR . 16740 1 90 89 ASP . 16740 1 91 90 TYR . 16740 1 92 91 HIS . 16740 1 93 92 CYS . 16740 1 94 93 THR . 16740 1 95 94 PRO . 16740 1 96 95 HIS . 16740 1 97 96 PRO . 16740 1 98 97 PHE . 16740 1 99 98 MET . 16740 1 100 99 ARG . 16740 1 101 100 GLY . 16740 1 102 101 LYS . 16740 1 103 102 VAL . 16740 1 104 103 VAL . 16740 1 105 104 VAL . 16740 1 106 105 GLU . 16740 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 . GLY 1 1 16740 1 . ASP 2 2 16740 1 . LYS 3 3 16740 1 . ALA 4 4 16740 1 . THR 5 5 16740 1 . ILE 6 6 16740 1 . PRO 7 7 16740 1 . SER 8 8 16740 1 . GLU 9 9 16740 1 . SER 10 10 16740 1 . PRO 11 11 16740 1 . PHE 12 12 16740 1 . ALA 13 13 16740 1 . ALA 14 14 16740 1 . ALA 15 15 16740 1 . GLU 16 16 16740 1 . VAL 17 17 16740 1 . ALA 18 18 16740 1 . ASP 19 19 16740 1 . GLY 20 20 16740 1 . ALA 21 21 16740 1 . ILE 22 22 16740 1 . VAL 23 23 16740 1 . VAL 24 24 16740 1 . ASP 25 25 16740 1 . ILE 26 26 16740 1 . ALA 27 27 16740 1 . LYS 28 28 16740 1 . MET 29 29 16740 1 . LYS 30 30 16740 1 . TYR 31 31 16740 1 . GLU 32 32 16740 1 . THR 33 33 16740 1 . PRO 34 34 16740 1 . GLU 35 35 16740 1 . LEU 36 36 16740 1 . HIS 37 37 16740 1 . VAL 38 38 16740 1 . LYS 39 39 16740 1 . VAL 40 40 16740 1 . GLY 41 41 16740 1 . ASP 42 42 16740 1 . THR 43 43 16740 1 . VAL 44 44 16740 1 . THR 45 45 16740 1 . TRP 46 46 16740 1 . ILE 47 47 16740 1 . ASN 48 48 16740 1 . ARG 49 49 16740 1 . GLU 50 50 16740 1 . ALA 51 51 16740 1 . MET 52 52 16740 1 . PRO 53 53 16740 1 . HIS 54 54 16740 1 . ASN 55 55 16740 1 . VAL 56 56 16740 1 . HIS 57 57 16740 1 . PHE 58 58 16740 1 . VAL 59 59 16740 1 . ALA 60 60 16740 1 . GLY 61 61 16740 1 . VAL 62 62 16740 1 . LEU 63 63 16740 1 . GLY 64 64 16740 1 . GLU 65 65 16740 1 . ALA 66 66 16740 1 . ALA 67 67 16740 1 . LEU 68 68 16740 1 . LYS 69 69 16740 1 . GLY 70 70 16740 1 . PRO 71 71 16740 1 . MET 72 72 16740 1 . MET 73 73 16740 1 . LYS 74 74 16740 1 . LYS 75 75 16740 1 . GLU 76 76 16740 1 . GLN 77 77 16740 1 . ALA 78 78 16740 1 . TYR 79 79 16740 1 . SER 80 80 16740 1 . LEU 81 81 16740 1 . THR 82 82 16740 1 . PHE 83 83 16740 1 . THR 84 84 16740 1 . GLU 85 85 16740 1 . ALA 86 86 16740 1 . GLY 87 87 16740 1 . THR 88 88 16740 1 . TYR 89 89 16740 1 . ASP 90 90 16740 1 . TYR 91 91 16740 1 . HIS 92 92 16740 1 . CYS 93 93 16740 1 . THR 94 94 16740 1 . PRO 95 95 16740 1 . HIS 96 96 16740 1 . PRO 97 97 16740 1 . PHE 98 98 16740 1 . MET 99 99 16740 1 . ARG 100 100 16740 1 . GLY 101 101 16740 1 . LYS 102 102 16740 1 . VAL 103 103 16740 1 . VAL 104 104 16740 1 . VAL 105 105 16740 1 . GLU 106 106 16740 1 stop_ save_ save_ZN _Entity.Sf_category entity _Entity.Sf_framecode ZN _Entity.Entry_ID 16740 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name ZN _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 ZN _Entity.Nonpolymer_comp_label $chem_comp_ZN _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 . ZN . 16740 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 16740 _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 $amicyanin . 266 organism . 'Paracoccus denitrificans' 'Paracoccus denitrificans' . . Bacteria . Paracoccus denitrificans Pd1222 . . . . . . . . . . . . . . . mauC . . . . 16740 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 16740 _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 $amicyanin . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pET28ami . . . . . . 16740 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_ZN _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_ZN _Chem_comp.Entry_ID 16740 _Chem_comp.ID ZN _Chem_comp.Provenance . _Chem_comp.Name 'ZINC ION' _Chem_comp.Type non-polymer _Chem_comp.BMRB_code . _Chem_comp.PDB_code ZN _Chem_comp.Ambiguous_flag . _Chem_comp.Initial_date . _Chem_comp.Modified_date . _Chem_comp.Release_status . _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code ZN _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 2 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula Zn _Chem_comp.Formula_weight 65.409 _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 Tue Jun 9 16:52:42 2009 ; _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 InChI=1/Zn/q+2 InChI InChI 1.02b 16740 ZN PTFCDOFLOPIGGS-UHFFFAOYAK InChIKey InChI 1.02b 16740 ZN [Zn++] SMILES CACTVS 3.341 16740 ZN [Zn++] SMILES_CANONICAL CACTVS 3.341 16740 ZN [Zn+2] SMILES ACDLabs 10.04 16740 ZN [Zn+2] SMILES 'OpenEye OEToolkits' 1.5.0 16740 ZN [Zn+2] SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 16740 ZN 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 zinc 'SYSTEMATIC NAME' ACDLabs 10.04 16740 ZN 'zinc(+2) cation' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 16740 ZN 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 ZN . ZN . . ZN . . N 2 . . . . . . . . . . 0.000 . 0.000 . 0.000 . 0.000 0.000 0.000 . . 16740 ZN stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 16740 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '93% H2O/7% D2O' _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 amicyanin [U-15N] . . 1 $amicyanin . . 1.2 . . mM . . . . 16740 1 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 16740 _Sample_condition_list.ID 1 _Sample_condition_list.Details '20 mM KPi' 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 'ionic strength' 0.08 . M 16740 1 pH 7.9 . pH 16740 1 pressure 1 . atm 16740 1 temperature 300 . K 16740 1 stop_ save_ ############################ # Computer software used # ############################ save_AZARA _Software.Sf_category software _Software.Sf_framecode AZARA _Software.Entry_ID 16740 _Software.ID 1 _Software.Name AZARA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Boucher . . 16740 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 16740 1 stop_ save_ save_ANSIG _Software.Sf_category software _Software.Sf_framecode ANSIG _Software.Entry_ID 16740 _Software.ID 2 _Software.Name ANSIG _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Kraulis . . 16740 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 16740 2 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 16740 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 16740 _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 DMX . 600 . . . 16740 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 16740 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16740 1 2 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16740 1 3 '3D 1H-15N TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 16740 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 16740 _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 water protons . . . . ppm 4.70 internal direct 1.0 . . . . . . . . . 16740 1 N 15 DSS 'methyl protons' . . . . ppm 0 na indirect 0.101329118 . . . . . . . . . 16740 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_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 16740 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _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 '2D 1H-15N HSQC' . . . 16740 1 2 '3D 1H-15N NOESY' . . . 16740 1 3 '3D 1H-15N TOCSY' . . . 16740 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 ASP H H 1 8.38 . . . . . . . 1 ASP H . 16740 1 2 . 1 1 2 2 ASP N N 15 121.39 . . . . . . . 1 ASP N . 16740 1 3 . 1 1 3 3 LYS H H 1 7.94 . . . . . . . 2 LYS H . 16740 1 4 . 1 1 3 3 LYS N N 15 114.37 . . . . . . . 2 LYS N . 16740 1 5 . 1 1 4 4 ALA H H 1 6.87 . . . . . . . 3 ALA H . 16740 1 6 . 1 1 4 4 ALA N N 15 116.44 . . . . . . . 3 ALA N . 16740 1 7 . 1 1 5 5 THR H H 1 8.85 . . . . . . . 4 THR H . 16740 1 8 . 1 1 5 5 THR N N 15 112.86 . . . . . . . 4 THR N . 16740 1 9 . 1 1 6 6 ILE H H 1 8.25 . . . . . . . 5 ILE H . 16740 1 10 . 1 1 6 6 ILE N N 15 122.46 . . . . . . . 5 ILE N . 16740 1 11 . 1 1 8 8 SER H H 1 7.69 . . . . . . . 7 SER H . 16740 1 12 . 1 1 8 8 SER N N 15 109.47 . . . . . . . 7 SER N . 16740 1 13 . 1 1 9 9 GLU H H 1 9.02 . . . . . . . 8 GLU H . 16740 1 14 . 1 1 9 9 GLU N N 15 127.93 . . . . . . . 8 GLU N . 16740 1 15 . 1 1 10 10 SER H H 1 7.85 . . . . . . . 9 SER H . 16740 1 16 . 1 1 10 10 SER N N 15 112.1 . . . . . . . 9 SER N . 16740 1 17 . 1 1 12 12 PHE H H 1 8.57 . . . . . . . 11 PHE H . 16740 1 18 . 1 1 12 12 PHE N N 15 120.07 . . . . . . . 11 PHE N . 16740 1 19 . 1 1 13 13 ALA H H 1 8.62 . . . . . . . 12 ALA H . 16740 1 20 . 1 1 13 13 ALA N N 15 122.53 . . . . . . . 12 ALA N . 16740 1 21 . 1 1 14 14 ALA H H 1 8.17 . . . . . . . 13 ALA H . 16740 1 22 . 1 1 14 14 ALA N N 15 123.68 . . . . . . . 13 ALA N . 16740 1 23 . 1 1 15 15 ALA H H 1 8.28 . . . . . . . 14 ALA H . 16740 1 24 . 1 1 15 15 ALA N N 15 117.84 . . . . . . . 14 ALA N . 16740 1 25 . 1 1 16 16 GLU H H 1 7.89 . . . . . . . 15 GLU H . 16740 1 26 . 1 1 16 16 GLU N N 15 114.87 . . . . . . . 15 GLU N . 16740 1 27 . 1 1 17 17 VAL H H 1 7.41 . . . . . . . 16 VAL H . 16740 1 28 . 1 1 17 17 VAL N N 15 121.89 . . . . . . . 16 VAL N . 16740 1 29 . 1 1 18 18 ALA H H 1 8.59 . . . . . . . 17 ALA H . 16740 1 30 . 1 1 18 18 ALA N N 15 132.06 . . . . . . . 17 ALA N . 16740 1 31 . 1 1 19 19 ASP H H 1 8.4 . . . . . . . 18 ASP H . 16740 1 32 . 1 1 19 19 ASP N N 15 121.08 . . . . . . . 18 ASP N . 16740 1 33 . 1 1 20 20 GLY H H 1 8.59 . . . . . . . 19 GLY H . 16740 1 34 . 1 1 20 20 GLY N N 15 112.36 . . . . . . . 19 GLY N . 16740 1 35 . 1 1 21 21 ALA H H 1 7.27 . . . . . . . 20 ALA H . 16740 1 36 . 1 1 21 21 ALA N N 15 122.86 . . . . . . . 20 ALA N . 16740 1 37 . 1 1 22 22 ILE H H 1 8.4 . . . . . . . 21 ILE H . 16740 1 38 . 1 1 22 22 ILE N N 15 123.53 . . . . . . . 21 ILE N . 16740 1 39 . 1 1 23 23 VAL H H 1 8.05 . . . . . . . 22 VAL H . 16740 1 40 . 1 1 23 23 VAL N N 15 129.35 . . . . . . . 22 VAL N . 16740 1 41 . 1 1 24 24 VAL H H 1 8.7 . . . . . . . 23 VAL H . 16740 1 42 . 1 1 24 24 VAL N N 15 128.06 . . . . . . . 23 VAL N . 16740 1 43 . 1 1 25 25 ASP H H 1 8.62 . . . . . . . 24 ASP H . 16740 1 44 . 1 1 25 25 ASP N N 15 127.33 . . . . . . . 24 ASP N . 16740 1 45 . 1 1 26 26 ILE H H 1 8.58 . . . . . . . 25 ILE H . 16740 1 46 . 1 1 26 26 ILE N N 15 120.29 . . . . . . . 25 ILE N . 16740 1 47 . 1 1 27 27 ALA H H 1 8.3 . . . . . . . 26 ALA H . 16740 1 48 . 1 1 27 27 ALA N N 15 124.5 . . . . . . . 26 ALA N . 16740 1 49 . 1 1 28 28 LYS H H 1 8.9 . . . . . . . 27 LYS H . 16740 1 50 . 1 1 28 28 LYS N N 15 119.65 . . . . . . . 27 LYS N . 16740 1 51 . 1 1 29 29 MET H H 1 8.88 . . . . . . . 28 MET H . 16740 1 52 . 1 1 29 29 MET N N 15 108.4 . . . . . . . 28 MET N . 16740 1 53 . 1 1 30 30 LYS H H 1 7.33 . . . . . . . 29 LYS H . 16740 1 54 . 1 1 30 30 LYS N N 15 113.78 . . . . . . . 29 LYS N . 16740 1 55 . 1 1 31 31 TYR H H 1 8.17 . . . . . . . 30 TYR H . 16740 1 56 . 1 1 31 31 TYR N N 15 118.55 . . . . . . . 30 TYR N . 16740 1 57 . 1 1 32 32 GLU H H 1 9.3 . . . . . . . 31 GLU H . 16740 1 58 . 1 1 32 32 GLU N N 15 123.2 . . . . . . . 31 GLU N . 16740 1 59 . 1 1 33 33 THR H H 1 6.23 . . . . . . . 32 THR H . 16740 1 60 . 1 1 33 33 THR N N 15 110.19 . . . . . . . 32 THR N . 16740 1 61 . 1 1 35 35 GLU H H 1 8.09 . . . . . . . 34 GLU H . 16740 1 62 . 1 1 35 35 GLU N N 15 121.99 . . . . . . . 34 GLU N . 16740 1 63 . 1 1 36 36 LEU H H 1 7.69 . . . . . . . 35 LEU H . 16740 1 64 . 1 1 36 36 LEU N N 15 128.59 . . . . . . . 35 LEU N . 16740 1 65 . 1 1 37 37 HIS H H 1 8.93 . . . . . . . 36 HIS H . 16740 1 66 . 1 1 37 37 HIS N N 15 127.22 . . . . . . . 36 HIS N . 16740 1 67 . 1 1 38 38 VAL H H 1 9.1 . . . . . . . 37 VAL H . 16740 1 68 . 1 1 38 38 VAL N N 15 117.18 . . . . . . . 37 VAL N . 16740 1 69 . 1 1 39 39 LYS H H 1 9.19 . . . . . . . 38 LYS H . 16740 1 70 . 1 1 39 39 LYS N N 15 121.13 . . . . . . . 38 LYS N . 16740 1 71 . 1 1 40 40 VAL H H 1 7.92 . . . . . . . 39 VAL H . 16740 1 72 . 1 1 40 40 VAL N N 15 119.45 . . . . . . . 39 VAL N . 16740 1 73 . 1 1 41 41 GLY H H 1 8.87 . . . . . . . 40 GLY H . 16740 1 74 . 1 1 41 41 GLY N N 15 117.11 . . . . . . . 40 GLY N . 16740 1 75 . 1 1 42 42 ASP H H 1 8.36 . . . . . . . 41 ASP H . 16740 1 76 . 1 1 42 42 ASP N N 15 121.88 . . . . . . . 41 ASP N . 16740 1 77 . 1 1 43 43 THR H H 1 8.45 . . . . . . . 42 THR H . 16740 1 78 . 1 1 43 43 THR N N 15 116.62 . . . . . . . 42 THR N . 16740 1 79 . 1 1 44 44 VAL H H 1 9.27 . . . . . . . 43 VAL H . 16740 1 80 . 1 1 44 44 VAL N N 15 129.77 . . . . . . . 43 VAL N . 16740 1 81 . 1 1 45 45 THR H H 1 8.05 . . . . . . . 44 THR H . 16740 1 82 . 1 1 45 45 THR N N 15 122.75 . . . . . . . 44 THR N . 16740 1 83 . 1 1 46 46 TRP H H 1 9.58 . . . . . . . 45 TRP H . 16740 1 84 . 1 1 46 46 TRP N N 15 129.91 . . . . . . . 45 TRP N . 16740 1 85 . 1 1 47 47 ILE H H 1 8.31 . . . . . . . 46 ILE H . 16740 1 86 . 1 1 47 47 ILE N N 15 117.67 . . . . . . . 46 ILE N . 16740 1 87 . 1 1 48 48 ASN H H 1 8.53 . . . . . . . 47 ASN H . 16740 1 88 . 1 1 48 48 ASN N N 15 123.81 . . . . . . . 47 ASN N . 16740 1 89 . 1 1 48 48 ASN HD21 H 1 7.46 . . . . . . . 47 ASN H . 16740 1 90 . 1 1 48 48 ASN HD22 H 1 6.82 . . . . . . . 47 ASN H . 16740 1 91 . 1 1 48 48 ASN ND2 N 15 110.38 . . . . . . . 47 ASN N . 16740 1 92 . 1 1 49 49 ARG H H 1 9.49 . . . . . . . 48 ARG H . 16740 1 93 . 1 1 49 49 ARG N N 15 125.12 . . . . . . . 48 ARG N . 16740 1 94 . 1 1 50 50 GLU H H 1 8.35 . . . . . . . 49 GLU H . 16740 1 95 . 1 1 50 50 GLU N N 15 120.68 . . . . . . . 49 GLU N . 16740 1 96 . 1 1 51 51 ALA H H 1 7.94 . . . . . . . 50 ALA H . 16740 1 97 . 1 1 51 51 ALA N N 15 117.5 . . . . . . . 50 ALA N . 16740 1 98 . 1 1 52 52 MET H H 1 7.46 . . . . . . . 51 MET H . 16740 1 99 . 1 1 52 52 MET N N 15 119.66 . . . . . . . 51 MET N . 16740 1 100 . 1 1 56 56 VAL H H 1 6.55 . . . . . . . 55 VAL H . 16740 1 101 . 1 1 56 56 VAL N N 15 107.59 . . . . . . . 55 VAL N . 16740 1 102 . 1 1 57 57 HIS H H 1 8.48 . . . . . . . 56 HIS H . 16740 1 103 . 1 1 57 57 HIS N N 15 124.47 . . . . . . . 56 HIS N . 16740 1 104 . 1 1 59 59 VAL H H 1 9 . . . . . . . 58 VAL H . 16740 1 105 . 1 1 59 59 VAL N N 15 118.25 . . . . . . . 58 VAL N . 16740 1 106 . 1 1 60 60 ALA H H 1 8.68 . . . . . . . 59 ALA H . 16740 1 107 . 1 1 60 60 ALA N N 15 123.59 . . . . . . . 59 ALA N . 16740 1 108 . 1 1 61 61 GLY H H 1 7.66 . . . . . . . 60 GLY H . 16740 1 109 . 1 1 61 61 GLY N N 15 111.58 . . . . . . . 60 GLY N . 16740 1 110 . 1 1 62 62 VAL H H 1 7.84 . . . . . . . 61 VAL H . 16740 1 111 . 1 1 62 62 VAL N N 15 121.09 . . . . . . . 61 VAL N . 16740 1 112 . 1 1 63 63 LEU H H 1 9.16 . . . . . . . 62 LEU H . 16740 1 113 . 1 1 63 63 LEU N N 15 115.37 . . . . . . . 62 LEU N . 16740 1 114 . 1 1 64 64 GLY H H 1 7.42 . . . . . . . 63 GLY H . 16740 1 115 . 1 1 64 64 GLY N N 15 114.78 . . . . . . . 63 GLY N . 16740 1 116 . 1 1 65 65 GLU H H 1 8.66 . . . . . . . 64 GLU H . 16740 1 117 . 1 1 65 65 GLU N N 15 119.34 . . . . . . . 64 GLU N . 16740 1 118 . 1 1 66 66 ALA H H 1 7.98 . . . . . . . 65 ALA H . 16740 1 119 . 1 1 66 66 ALA N N 15 119.44 . . . . . . . 65 ALA N . 16740 1 120 . 1 1 67 67 ALA H H 1 8.48 . . . . . . . 66 ALA H . 16740 1 121 . 1 1 67 67 ALA N N 15 120.86 . . . . . . . 66 ALA N . 16740 1 122 . 1 1 68 68 LEU H H 1 8.94 . . . . . . . 67 LEU H . 16740 1 123 . 1 1 68 68 LEU N N 15 123.97 . . . . . . . 67 LEU N . 16740 1 124 . 1 1 69 69 LYS H H 1 8.44 . . . . . . . 68 LYS H . 16740 1 125 . 1 1 69 69 LYS N N 15 128.75 . . . . . . . 68 LYS N . 16740 1 126 . 1 1 70 70 GLY H H 1 8.85 . . . . . . . 69 GLY H . 16740 1 127 . 1 1 70 70 GLY N N 15 116.32 . . . . . . . 69 GLY N . 16740 1 128 . 1 1 72 72 MET H H 1 8.31 . . . . . . . 71 MET H . 16740 1 129 . 1 1 72 72 MET N N 15 117.22 . . . . . . . 71 MET N . 16740 1 130 . 1 1 73 73 MET H H 1 8.77 . . . . . . . 72 MET H . 16740 1 131 . 1 1 73 73 MET N N 15 122.8 . . . . . . . 72 MET N . 16740 1 132 . 1 1 74 74 LYS H H 1 8.56 . . . . . . . 73 LYS H . 16740 1 133 . 1 1 74 74 LYS N N 15 123.2 . . . . . . . 73 LYS N . 16740 1 134 . 1 1 75 75 LYS H H 1 7.94 . . . . . . . 74 LYS H . 16740 1 135 . 1 1 75 75 LYS N N 15 119.79 . . . . . . . 74 LYS N . 16740 1 136 . 1 1 76 76 GLU H H 1 9.35 . . . . . . . 75 GLU H . 16740 1 137 . 1 1 76 76 GLU N N 15 118.22 . . . . . . . 75 GLU N . 16740 1 138 . 1 1 77 77 GLN H H 1 7.89 . . . . . . . 76 GLN H . 16740 1 139 . 1 1 77 77 GLN N N 15 116.81 . . . . . . . 76 GLN N . 16740 1 140 . 1 1 77 77 GLN HE21 H 1 7.72 . . . . . . . 76 GLN HE21 . 16740 1 141 . 1 1 77 77 GLN HE22 H 1 6.65 . . . . . . . 76 GLN HE22 . 16740 1 142 . 1 1 77 77 GLN NE2 N 15 112.33 . . . . . . . 76 GLN NE2 . 16740 1 143 . 1 1 78 78 ALA H H 1 8.82 . . . . . . . 77 ALA H . 16740 1 144 . 1 1 78 78 ALA N N 15 122.28 . . . . . . . 77 ALA N . 16740 1 145 . 1 1 79 79 TYR H H 1 8.43 . . . . . . . 78 TYR H . 16740 1 146 . 1 1 79 79 TYR N N 15 117.27 . . . . . . . 78 TYR N . 16740 1 147 . 1 1 80 80 SER H H 1 7.62 . . . . . . . 79 SER H . 16740 1 148 . 1 1 80 80 SER N N 15 121.73 . . . . . . . 79 SER N . 16740 1 149 . 1 1 81 81 LEU H H 1 8.84 . . . . . . . 80 LEU H . 16740 1 150 . 1 1 81 81 LEU N N 15 119.8 . . . . . . . 80 LEU N . 16740 1 151 . 1 1 82 82 THR H H 1 8.49 . . . . . . . 81 THR H . 16740 1 152 . 1 1 82 82 THR N N 15 119.67 . . . . . . . 81 THR N . 16740 1 153 . 1 1 83 83 PHE H H 1 8.09 . . . . . . . 82 PHE H . 16740 1 154 . 1 1 83 83 PHE N N 15 125.1 . . . . . . . 82 PHE N . 16740 1 155 . 1 1 84 84 THR H H 1 8.15 . . . . . . . 83 THR H . 16740 1 156 . 1 1 84 84 THR N N 15 112.24 . . . . . . . 83 THR N . 16740 1 157 . 1 1 85 85 GLU H H 1 7.67 . . . . . . . 84 GLU H . 16740 1 158 . 1 1 85 85 GLU N N 15 120.15 . . . . . . . 84 GLU N . 16740 1 159 . 1 1 86 86 ALA H H 1 9.03 . . . . . . . 85 ALA H . 16740 1 160 . 1 1 86 86 ALA N N 15 131.34 . . . . . . . 85 ALA N . 16740 1 161 . 1 1 87 87 GLY H H 1 8.74 . . . . . . . 86 GLY H . 16740 1 162 . 1 1 87 87 GLY N N 15 109.08 . . . . . . . 86 GLY N . 16740 1 163 . 1 1 88 88 THR H H 1 7.72 . . . . . . . 87 THR H . 16740 1 164 . 1 1 88 88 THR N N 15 114.63 . . . . . . . 87 THR N . 16740 1 165 . 1 1 89 89 TYR H H 1 9.13 . . . . . . . 88 TYR H . 16740 1 166 . 1 1 89 89 TYR N N 15 127.44 . . . . . . . 88 TYR N . 16740 1 167 . 1 1 90 90 ASP H H 1 8.53 . . . . . . . 89 ASP H . 16740 1 168 . 1 1 90 90 ASP N N 15 126.89 . . . . . . . 89 ASP N . 16740 1 169 . 1 1 91 91 TYR H H 1 8.3 . . . . . . . 90 TYR H . 16740 1 170 . 1 1 91 91 TYR N N 15 116.85 . . . . . . . 90 TYR N . 16740 1 171 . 1 1 92 92 HIS H H 1 8.68 . . . . . . . 91 HIS H . 16740 1 172 . 1 1 92 92 HIS N N 15 118.64 . . . . . . . 91 HIS N . 16740 1 173 . 1 1 93 93 CYS H H 1 6.78 . . . . . . . 92 CYS H . 16740 1 174 . 1 1 93 93 CYS N N 15 120.76 . . . . . . . 92 CYS N . 16740 1 175 . 1 1 94 94 THR H H 1 10.23 . . . . . . . 93 THR H . 16740 1 176 . 1 1 94 94 THR N N 15 128.84 . . . . . . . 93 THR N . 16740 1 177 . 1 1 98 98 PHE H H 1 6.41 . . . . . . . 97 PHE H . 16740 1 178 . 1 1 98 98 PHE N N 15 111.11 . . . . . . . 97 PHE N . 16740 1 179 . 1 1 99 99 MET H H 1 8.41 . . . . . . . 98 MET H . 16740 1 180 . 1 1 99 99 MET N N 15 125.63 . . . . . . . 98 MET N . 16740 1 181 . 1 1 100 100 ARG H H 1 7.76 . . . . . . . 99 ARG H . 16740 1 182 . 1 1 100 100 ARG N N 15 121.3 . . . . . . . 99 ARG N . 16740 1 183 . 1 1 101 101 GLY H H 1 7.71 . . . . . . . 100 GLY H . 16740 1 184 . 1 1 101 101 GLY N N 15 109.08 . . . . . . . 100 GLY N . 16740 1 185 . 1 1 102 102 LYS H H 1 8.38 . . . . . . . 101 LYS H . 16740 1 186 . 1 1 102 102 LYS N N 15 117.44 . . . . . . . 101 LYS N . 16740 1 187 . 1 1 103 103 VAL H H 1 9.1 . . . . . . . 102 VAL H . 16740 1 188 . 1 1 103 103 VAL N N 15 126.89 . . . . . . . 102 VAL N . 16740 1 189 . 1 1 104 104 VAL H H 1 9.28 . . . . . . . 103 VAL H . 16740 1 190 . 1 1 104 104 VAL N N 15 130.03 . . . . . . . 103 VAL N . 16740 1 191 . 1 1 105 105 VAL H H 1 9.18 . . . . . . . 104 VAL H . 16740 1 192 . 1 1 105 105 VAL N N 15 128.81 . . . . . . . 104 VAL N . 16740 1 193 . 1 1 106 106 GLU H H 1 8.77 . . . . . . . 105 GLU H . 16740 1 194 . 1 1 106 106 GLU N N 15 133.61 . . . . . . . 105 GLU N . 16740 1 stop_ save_